data_9BCN
# 
_entry.id   9BCN 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9BCN         pdb_00009bcn 10.2210/pdb9bcn/pdb 
WWPDB D_1000283082 ?            ?                   
EMDB  EMD-44431    ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-11-27 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9BCN 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-09 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'Extracellular domain of apo GC-A, state 2' 
_pdbx_database_related.db_id          EMD-44431 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              xyhuang@med.cornell.edu 
_pdbx_contact_author.name_first         Xin-Yun 
_pdbx_contact_author.name_last          Huang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2534-2587 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Liu, S.'   1 0000-0003-0931-8368 
'Huang, X.' 2 0000-0003-2534-2587 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Nat.Struct.Mol.Biol. 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1545-9985 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Architecture and activation of single-pass transmembrane receptor guanylyl cyclase.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41594-024-01426-z 
_citation.pdbx_database_id_PubMed   39543315 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Liu, S.'      1  0000-0003-0931-8368 
primary 'Payne, A.M.'  2  0000-0003-0947-0191 
primary 'Wang, J.'     3  ?                   
primary 'Zhu, L.'      4  ?                   
primary 'Paknejad, N.' 5  0000-0001-8914-7604 
primary 'Eng, E.T.'    6  0000-0002-8014-7269 
primary 'Liu, W.'      7  0000-0002-7568-5521 
primary 'Miao, Y.'     8  0000-0003-3714-1395 
primary 'Hite, R.K.'   9  0000-0003-0496-0669 
primary 'Huang, X.Y.'  10 0000-0003-2534-2587 
# 
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 'Atrial natriuretic peptide receptor 1' 116770.852 2 4.6.1.2 ? ? ? 
2 branched    man 
'alpha-D-mannopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 586.542    4 
?       ? ? ? 
3 non-polymer syn 'CHLORIDE ION' 35.453     2 ?       ? ? ? 
4 non-polymer syn 2-acetamido-2-deoxy-beta-D-glucopyranose 221.208    2 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Atrial natriuretic peptide receptor type A,ANP-A,ANPR-A,NPR-A,Guanylate cyclase A,GC-A' 
# 
_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       
;DYKDDDDKAAAGNLTVAVVLPLANTSYPWSWARVGPAVELALAQVKARPDLLPGWTVRTVLGSSENALGVCSDTAAPLAA
VDLKWEHNPAVFLGPGCVYAAAPVGRFTAHWRVPLLTAGAPALGFGVKDEYALTTRAGPSYAKLGDFVAALHRRLGWERQ
ALMLYAYRPGDEEHCFFLVEGLFMRVRDRLNITVDHLEFAEDDLSHYTRLLRTMPRKGRVIYICSSPDAFRTLMLLALEA
GLCGEDYVFFHLDIFGQSLQGGQGPAPRRPWERGDGQDVSARQAFQAAKIITYKDPDNPEYLEFLKQLKHLAYEQFNFTM
EDGLVNTIPASFHDGLLLYIQAVTETLAHGGTVTDGENITQRMWNRSFQGVTGYLKIDSSGDRETDFSLWDMDPENGAFR
VVLNYNGTSQELVAVSGRKLNWPLGYPPPDIPKCGFDNEDPACNQDHLSTLEVLALVGSLSLLGILIVSFFIYRKMQLEK
ELASELWRVRWEDVEPSSLERHLRSAGSRLTLSGRGSNYGSLLTTEGQFQVFAKTAYYKGNLVAVKRVNRKRIELTRKVL
FELKHMRDVQNEHLTRFVGACTDPPNICILTEYCPRGSLQDILENESITLDWMFRYSLTNDIVKGMLFLHNGAICSHGNL
KSSNCVVDGRFVLKITDYGLESFRDLDPEQGHTVYAKKLWTAPELLRMASPPVRGSQAGDVYSFGIILQEIALRSGVFHV
EGLDLSPKEIIERVTRGEQPPFRPSLALQSHLEELGLLMQRCWAEDPQERPPFQQIRLTLRKFNRENSSNILDNLLSRME
QYANNLEELVEERTQAYLEEKRKAEALLYQILPHSVAEQLKRGETVQAEAFDSVTIYFSDIVGFTALSAESTPMQVVTLL
NDLYTCFDAVIDNFDVYKVETIGDAYMVVSGLPVRNGRLHACEVARMALALLDAVRSFRIRHRPQEQLRLRIGIHTGPVC
AGVVGLKMPRYCLFGDTVNTASRMESNGEALKIHLSSETKAVLEEFGGFELELRGDVEMKGKGKVRTYWLLGERGSSTRG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;DYKDDDDKAAAGNLTVAVVLPLANTSYPWSWARVGPAVELALAQVKARPDLLPGWTVRTVLGSSENALGVCSDTAAPLAA
VDLKWEHNPAVFLGPGCVYAAAPVGRFTAHWRVPLLTAGAPALGFGVKDEYALTTRAGPSYAKLGDFVAALHRRLGWERQ
ALMLYAYRPGDEEHCFFLVEGLFMRVRDRLNITVDHLEFAEDDLSHYTRLLRTMPRKGRVIYICSSPDAFRTLMLLALEA
GLCGEDYVFFHLDIFGQSLQGGQGPAPRRPWERGDGQDVSARQAFQAAKIITYKDPDNPEYLEFLKQLKHLAYEQFNFTM
EDGLVNTIPASFHDGLLLYIQAVTETLAHGGTVTDGENITQRMWNRSFQGVTGYLKIDSSGDRETDFSLWDMDPENGAFR
VVLNYNGTSQELVAVSGRKLNWPLGYPPPDIPKCGFDNEDPACNQDHLSTLEVLALVGSLSLLGILIVSFFIYRKMQLEK
ELASELWRVRWEDVEPSSLERHLRSAGSRLTLSGRGSNYGSLLTTEGQFQVFAKTAYYKGNLVAVKRVNRKRIELTRKVL
FELKHMRDVQNEHLTRFVGACTDPPNICILTEYCPRGSLQDILENESITLDWMFRYSLTNDIVKGMLFLHNGAICSHGNL
KSSNCVVDGRFVLKITDYGLESFRDLDPEQGHTVYAKKLWTAPELLRMASPPVRGSQAGDVYSFGIILQEIALRSGVFHV
EGLDLSPKEIIERVTRGEQPPFRPSLALQSHLEELGLLMQRCWAEDPQERPPFQQIRLTLRKFNRENSSNILDNLLSRME
QYANNLEELVEERTQAYLEEKRKAEALLYQILPHSVAEQLKRGETVQAEAFDSVTIYFSDIVGFTALSAESTPMQVVTLL
NDLYTCFDAVIDNFDVYKVETIGDAYMVVSGLPVRNGRLHACEVARMALALLDAVRSFRIRHRPQEQLRLRIGIHTGPVC
AGVVGLKMPRYCLFGDTVNTASRMESNGEALKIHLSSETKAVLEEFGGFELELRGDVEMKGKGKVRTYWLLGERGSSTRG
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'CHLORIDE ION'                           CL  
4 2-acetamido-2-deoxy-beta-D-glucopyranose NAG 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1    ASP n 
1 2    TYR n 
1 3    LYS n 
1 4    ASP n 
1 5    ASP n 
1 6    ASP n 
1 7    ASP n 
1 8    LYS n 
1 9    ALA n 
1 10   ALA n 
1 11   ALA n 
1 12   GLY n 
1 13   ASN n 
1 14   LEU n 
1 15   THR n 
1 16   VAL n 
1 17   ALA n 
1 18   VAL n 
1 19   VAL n 
1 20   LEU n 
1 21   PRO n 
1 22   LEU n 
1 23   ALA n 
1 24   ASN n 
1 25   THR n 
1 26   SER n 
1 27   TYR n 
1 28   PRO n 
1 29   TRP n 
1 30   SER n 
1 31   TRP n 
1 32   ALA n 
1 33   ARG n 
1 34   VAL n 
1 35   GLY n 
1 36   PRO n 
1 37   ALA n 
1 38   VAL n 
1 39   GLU n 
1 40   LEU n 
1 41   ALA n 
1 42   LEU n 
1 43   ALA n 
1 44   GLN n 
1 45   VAL n 
1 46   LYS n 
1 47   ALA n 
1 48   ARG n 
1 49   PRO n 
1 50   ASP n 
1 51   LEU n 
1 52   LEU n 
1 53   PRO n 
1 54   GLY n 
1 55   TRP n 
1 56   THR n 
1 57   VAL n 
1 58   ARG n 
1 59   THR n 
1 60   VAL n 
1 61   LEU n 
1 62   GLY n 
1 63   SER n 
1 64   SER n 
1 65   GLU n 
1 66   ASN n 
1 67   ALA n 
1 68   LEU n 
1 69   GLY n 
1 70   VAL n 
1 71   CYS n 
1 72   SER n 
1 73   ASP n 
1 74   THR n 
1 75   ALA n 
1 76   ALA n 
1 77   PRO n 
1 78   LEU n 
1 79   ALA n 
1 80   ALA n 
1 81   VAL n 
1 82   ASP n 
1 83   LEU n 
1 84   LYS n 
1 85   TRP n 
1 86   GLU n 
1 87   HIS n 
1 88   ASN n 
1 89   PRO n 
1 90   ALA n 
1 91   VAL n 
1 92   PHE n 
1 93   LEU n 
1 94   GLY n 
1 95   PRO n 
1 96   GLY n 
1 97   CYS n 
1 98   VAL n 
1 99   TYR n 
1 100  ALA n 
1 101  ALA n 
1 102  ALA n 
1 103  PRO n 
1 104  VAL n 
1 105  GLY n 
1 106  ARG n 
1 107  PHE n 
1 108  THR n 
1 109  ALA n 
1 110  HIS n 
1 111  TRP n 
1 112  ARG n 
1 113  VAL n 
1 114  PRO n 
1 115  LEU n 
1 116  LEU n 
1 117  THR n 
1 118  ALA n 
1 119  GLY n 
1 120  ALA n 
1 121  PRO n 
1 122  ALA n 
1 123  LEU n 
1 124  GLY n 
1 125  PHE n 
1 126  GLY n 
1 127  VAL n 
1 128  LYS n 
1 129  ASP n 
1 130  GLU n 
1 131  TYR n 
1 132  ALA n 
1 133  LEU n 
1 134  THR n 
1 135  THR n 
1 136  ARG n 
1 137  ALA n 
1 138  GLY n 
1 139  PRO n 
1 140  SER n 
1 141  TYR n 
1 142  ALA n 
1 143  LYS n 
1 144  LEU n 
1 145  GLY n 
1 146  ASP n 
1 147  PHE n 
1 148  VAL n 
1 149  ALA n 
1 150  ALA n 
1 151  LEU n 
1 152  HIS n 
1 153  ARG n 
1 154  ARG n 
1 155  LEU n 
1 156  GLY n 
1 157  TRP n 
1 158  GLU n 
1 159  ARG n 
1 160  GLN n 
1 161  ALA n 
1 162  LEU n 
1 163  MET n 
1 164  LEU n 
1 165  TYR n 
1 166  ALA n 
1 167  TYR n 
1 168  ARG n 
1 169  PRO n 
1 170  GLY n 
1 171  ASP n 
1 172  GLU n 
1 173  GLU n 
1 174  HIS n 
1 175  CYS n 
1 176  PHE n 
1 177  PHE n 
1 178  LEU n 
1 179  VAL n 
1 180  GLU n 
1 181  GLY n 
1 182  LEU n 
1 183  PHE n 
1 184  MET n 
1 185  ARG n 
1 186  VAL n 
1 187  ARG n 
1 188  ASP n 
1 189  ARG n 
1 190  LEU n 
1 191  ASN n 
1 192  ILE n 
1 193  THR n 
1 194  VAL n 
1 195  ASP n 
1 196  HIS n 
1 197  LEU n 
1 198  GLU n 
1 199  PHE n 
1 200  ALA n 
1 201  GLU n 
1 202  ASP n 
1 203  ASP n 
1 204  LEU n 
1 205  SER n 
1 206  HIS n 
1 207  TYR n 
1 208  THR n 
1 209  ARG n 
1 210  LEU n 
1 211  LEU n 
1 212  ARG n 
1 213  THR n 
1 214  MET n 
1 215  PRO n 
1 216  ARG n 
1 217  LYS n 
1 218  GLY n 
1 219  ARG n 
1 220  VAL n 
1 221  ILE n 
1 222  TYR n 
1 223  ILE n 
1 224  CYS n 
1 225  SER n 
1 226  SER n 
1 227  PRO n 
1 228  ASP n 
1 229  ALA n 
1 230  PHE n 
1 231  ARG n 
1 232  THR n 
1 233  LEU n 
1 234  MET n 
1 235  LEU n 
1 236  LEU n 
1 237  ALA n 
1 238  LEU n 
1 239  GLU n 
1 240  ALA n 
1 241  GLY n 
1 242  LEU n 
1 243  CYS n 
1 244  GLY n 
1 245  GLU n 
1 246  ASP n 
1 247  TYR n 
1 248  VAL n 
1 249  PHE n 
1 250  PHE n 
1 251  HIS n 
1 252  LEU n 
1 253  ASP n 
1 254  ILE n 
1 255  PHE n 
1 256  GLY n 
1 257  GLN n 
1 258  SER n 
1 259  LEU n 
1 260  GLN n 
1 261  GLY n 
1 262  GLY n 
1 263  GLN n 
1 264  GLY n 
1 265  PRO n 
1 266  ALA n 
1 267  PRO n 
1 268  ARG n 
1 269  ARG n 
1 270  PRO n 
1 271  TRP n 
1 272  GLU n 
1 273  ARG n 
1 274  GLY n 
1 275  ASP n 
1 276  GLY n 
1 277  GLN n 
1 278  ASP n 
1 279  VAL n 
1 280  SER n 
1 281  ALA n 
1 282  ARG n 
1 283  GLN n 
1 284  ALA n 
1 285  PHE n 
1 286  GLN n 
1 287  ALA n 
1 288  ALA n 
1 289  LYS n 
1 290  ILE n 
1 291  ILE n 
1 292  THR n 
1 293  TYR n 
1 294  LYS n 
1 295  ASP n 
1 296  PRO n 
1 297  ASP n 
1 298  ASN n 
1 299  PRO n 
1 300  GLU n 
1 301  TYR n 
1 302  LEU n 
1 303  GLU n 
1 304  PHE n 
1 305  LEU n 
1 306  LYS n 
1 307  GLN n 
1 308  LEU n 
1 309  LYS n 
1 310  HIS n 
1 311  LEU n 
1 312  ALA n 
1 313  TYR n 
1 314  GLU n 
1 315  GLN n 
1 316  PHE n 
1 317  ASN n 
1 318  PHE n 
1 319  THR n 
1 320  MET n 
1 321  GLU n 
1 322  ASP n 
1 323  GLY n 
1 324  LEU n 
1 325  VAL n 
1 326  ASN n 
1 327  THR n 
1 328  ILE n 
1 329  PRO n 
1 330  ALA n 
1 331  SER n 
1 332  PHE n 
1 333  HIS n 
1 334  ASP n 
1 335  GLY n 
1 336  LEU n 
1 337  LEU n 
1 338  LEU n 
1 339  TYR n 
1 340  ILE n 
1 341  GLN n 
1 342  ALA n 
1 343  VAL n 
1 344  THR n 
1 345  GLU n 
1 346  THR n 
1 347  LEU n 
1 348  ALA n 
1 349  HIS n 
1 350  GLY n 
1 351  GLY n 
1 352  THR n 
1 353  VAL n 
1 354  THR n 
1 355  ASP n 
1 356  GLY n 
1 357  GLU n 
1 358  ASN n 
1 359  ILE n 
1 360  THR n 
1 361  GLN n 
1 362  ARG n 
1 363  MET n 
1 364  TRP n 
1 365  ASN n 
1 366  ARG n 
1 367  SER n 
1 368  PHE n 
1 369  GLN n 
1 370  GLY n 
1 371  VAL n 
1 372  THR n 
1 373  GLY n 
1 374  TYR n 
1 375  LEU n 
1 376  LYS n 
1 377  ILE n 
1 378  ASP n 
1 379  SER n 
1 380  SER n 
1 381  GLY n 
1 382  ASP n 
1 383  ARG n 
1 384  GLU n 
1 385  THR n 
1 386  ASP n 
1 387  PHE n 
1 388  SER n 
1 389  LEU n 
1 390  TRP n 
1 391  ASP n 
1 392  MET n 
1 393  ASP n 
1 394  PRO n 
1 395  GLU n 
1 396  ASN n 
1 397  GLY n 
1 398  ALA n 
1 399  PHE n 
1 400  ARG n 
1 401  VAL n 
1 402  VAL n 
1 403  LEU n 
1 404  ASN n 
1 405  TYR n 
1 406  ASN n 
1 407  GLY n 
1 408  THR n 
1 409  SER n 
1 410  GLN n 
1 411  GLU n 
1 412  LEU n 
1 413  VAL n 
1 414  ALA n 
1 415  VAL n 
1 416  SER n 
1 417  GLY n 
1 418  ARG n 
1 419  LYS n 
1 420  LEU n 
1 421  ASN n 
1 422  TRP n 
1 423  PRO n 
1 424  LEU n 
1 425  GLY n 
1 426  TYR n 
1 427  PRO n 
1 428  PRO n 
1 429  PRO n 
1 430  ASP n 
1 431  ILE n 
1 432  PRO n 
1 433  LYS n 
1 434  CYS n 
1 435  GLY n 
1 436  PHE n 
1 437  ASP n 
1 438  ASN n 
1 439  GLU n 
1 440  ASP n 
1 441  PRO n 
1 442  ALA n 
1 443  CYS n 
1 444  ASN n 
1 445  GLN n 
1 446  ASP n 
1 447  HIS n 
1 448  LEU n 
1 449  SER n 
1 450  THR n 
1 451  LEU n 
1 452  GLU n 
1 453  VAL n 
1 454  LEU n 
1 455  ALA n 
1 456  LEU n 
1 457  VAL n 
1 458  GLY n 
1 459  SER n 
1 460  LEU n 
1 461  SER n 
1 462  LEU n 
1 463  LEU n 
1 464  GLY n 
1 465  ILE n 
1 466  LEU n 
1 467  ILE n 
1 468  VAL n 
1 469  SER n 
1 470  PHE n 
1 471  PHE n 
1 472  ILE n 
1 473  TYR n 
1 474  ARG n 
1 475  LYS n 
1 476  MET n 
1 477  GLN n 
1 478  LEU n 
1 479  GLU n 
1 480  LYS n 
1 481  GLU n 
1 482  LEU n 
1 483  ALA n 
1 484  SER n 
1 485  GLU n 
1 486  LEU n 
1 487  TRP n 
1 488  ARG n 
1 489  VAL n 
1 490  ARG n 
1 491  TRP n 
1 492  GLU n 
1 493  ASP n 
1 494  VAL n 
1 495  GLU n 
1 496  PRO n 
1 497  SER n 
1 498  SER n 
1 499  LEU n 
1 500  GLU n 
1 501  ARG n 
1 502  HIS n 
1 503  LEU n 
1 504  ARG n 
1 505  SER n 
1 506  ALA n 
1 507  GLY n 
1 508  SER n 
1 509  ARG n 
1 510  LEU n 
1 511  THR n 
1 512  LEU n 
1 513  SER n 
1 514  GLY n 
1 515  ARG n 
1 516  GLY n 
1 517  SER n 
1 518  ASN n 
1 519  TYR n 
1 520  GLY n 
1 521  SER n 
1 522  LEU n 
1 523  LEU n 
1 524  THR n 
1 525  THR n 
1 526  GLU n 
1 527  GLY n 
1 528  GLN n 
1 529  PHE n 
1 530  GLN n 
1 531  VAL n 
1 532  PHE n 
1 533  ALA n 
1 534  LYS n 
1 535  THR n 
1 536  ALA n 
1 537  TYR n 
1 538  TYR n 
1 539  LYS n 
1 540  GLY n 
1 541  ASN n 
1 542  LEU n 
1 543  VAL n 
1 544  ALA n 
1 545  VAL n 
1 546  LYS n 
1 547  ARG n 
1 548  VAL n 
1 549  ASN n 
1 550  ARG n 
1 551  LYS n 
1 552  ARG n 
1 553  ILE n 
1 554  GLU n 
1 555  LEU n 
1 556  THR n 
1 557  ARG n 
1 558  LYS n 
1 559  VAL n 
1 560  LEU n 
1 561  PHE n 
1 562  GLU n 
1 563  LEU n 
1 564  LYS n 
1 565  HIS n 
1 566  MET n 
1 567  ARG n 
1 568  ASP n 
1 569  VAL n 
1 570  GLN n 
1 571  ASN n 
1 572  GLU n 
1 573  HIS n 
1 574  LEU n 
1 575  THR n 
1 576  ARG n 
1 577  PHE n 
1 578  VAL n 
1 579  GLY n 
1 580  ALA n 
1 581  CYS n 
1 582  THR n 
1 583  ASP n 
1 584  PRO n 
1 585  PRO n 
1 586  ASN n 
1 587  ILE n 
1 588  CYS n 
1 589  ILE n 
1 590  LEU n 
1 591  THR n 
1 592  GLU n 
1 593  TYR n 
1 594  CYS n 
1 595  PRO n 
1 596  ARG n 
1 597  GLY n 
1 598  SER n 
1 599  LEU n 
1 600  GLN n 
1 601  ASP n 
1 602  ILE n 
1 603  LEU n 
1 604  GLU n 
1 605  ASN n 
1 606  GLU n 
1 607  SER n 
1 608  ILE n 
1 609  THR n 
1 610  LEU n 
1 611  ASP n 
1 612  TRP n 
1 613  MET n 
1 614  PHE n 
1 615  ARG n 
1 616  TYR n 
1 617  SER n 
1 618  LEU n 
1 619  THR n 
1 620  ASN n 
1 621  ASP n 
1 622  ILE n 
1 623  VAL n 
1 624  LYS n 
1 625  GLY n 
1 626  MET n 
1 627  LEU n 
1 628  PHE n 
1 629  LEU n 
1 630  HIS n 
1 631  ASN n 
1 632  GLY n 
1 633  ALA n 
1 634  ILE n 
1 635  CYS n 
1 636  SER n 
1 637  HIS n 
1 638  GLY n 
1 639  ASN n 
1 640  LEU n 
1 641  LYS n 
1 642  SER n 
1 643  SER n 
1 644  ASN n 
1 645  CYS n 
1 646  VAL n 
1 647  VAL n 
1 648  ASP n 
1 649  GLY n 
1 650  ARG n 
1 651  PHE n 
1 652  VAL n 
1 653  LEU n 
1 654  LYS n 
1 655  ILE n 
1 656  THR n 
1 657  ASP n 
1 658  TYR n 
1 659  GLY n 
1 660  LEU n 
1 661  GLU n 
1 662  SER n 
1 663  PHE n 
1 664  ARG n 
1 665  ASP n 
1 666  LEU n 
1 667  ASP n 
1 668  PRO n 
1 669  GLU n 
1 670  GLN n 
1 671  GLY n 
1 672  HIS n 
1 673  THR n 
1 674  VAL n 
1 675  TYR n 
1 676  ALA n 
1 677  LYS n 
1 678  LYS n 
1 679  LEU n 
1 680  TRP n 
1 681  THR n 
1 682  ALA n 
1 683  PRO n 
1 684  GLU n 
1 685  LEU n 
1 686  LEU n 
1 687  ARG n 
1 688  MET n 
1 689  ALA n 
1 690  SER n 
1 691  PRO n 
1 692  PRO n 
1 693  VAL n 
1 694  ARG n 
1 695  GLY n 
1 696  SER n 
1 697  GLN n 
1 698  ALA n 
1 699  GLY n 
1 700  ASP n 
1 701  VAL n 
1 702  TYR n 
1 703  SER n 
1 704  PHE n 
1 705  GLY n 
1 706  ILE n 
1 707  ILE n 
1 708  LEU n 
1 709  GLN n 
1 710  GLU n 
1 711  ILE n 
1 712  ALA n 
1 713  LEU n 
1 714  ARG n 
1 715  SER n 
1 716  GLY n 
1 717  VAL n 
1 718  PHE n 
1 719  HIS n 
1 720  VAL n 
1 721  GLU n 
1 722  GLY n 
1 723  LEU n 
1 724  ASP n 
1 725  LEU n 
1 726  SER n 
1 727  PRO n 
1 728  LYS n 
1 729  GLU n 
1 730  ILE n 
1 731  ILE n 
1 732  GLU n 
1 733  ARG n 
1 734  VAL n 
1 735  THR n 
1 736  ARG n 
1 737  GLY n 
1 738  GLU n 
1 739  GLN n 
1 740  PRO n 
1 741  PRO n 
1 742  PHE n 
1 743  ARG n 
1 744  PRO n 
1 745  SER n 
1 746  LEU n 
1 747  ALA n 
1 748  LEU n 
1 749  GLN n 
1 750  SER n 
1 751  HIS n 
1 752  LEU n 
1 753  GLU n 
1 754  GLU n 
1 755  LEU n 
1 756  GLY n 
1 757  LEU n 
1 758  LEU n 
1 759  MET n 
1 760  GLN n 
1 761  ARG n 
1 762  CYS n 
1 763  TRP n 
1 764  ALA n 
1 765  GLU n 
1 766  ASP n 
1 767  PRO n 
1 768  GLN n 
1 769  GLU n 
1 770  ARG n 
1 771  PRO n 
1 772  PRO n 
1 773  PHE n 
1 774  GLN n 
1 775  GLN n 
1 776  ILE n 
1 777  ARG n 
1 778  LEU n 
1 779  THR n 
1 780  LEU n 
1 781  ARG n 
1 782  LYS n 
1 783  PHE n 
1 784  ASN n 
1 785  ARG n 
1 786  GLU n 
1 787  ASN n 
1 788  SER n 
1 789  SER n 
1 790  ASN n 
1 791  ILE n 
1 792  LEU n 
1 793  ASP n 
1 794  ASN n 
1 795  LEU n 
1 796  LEU n 
1 797  SER n 
1 798  ARG n 
1 799  MET n 
1 800  GLU n 
1 801  GLN n 
1 802  TYR n 
1 803  ALA n 
1 804  ASN n 
1 805  ASN n 
1 806  LEU n 
1 807  GLU n 
1 808  GLU n 
1 809  LEU n 
1 810  VAL n 
1 811  GLU n 
1 812  GLU n 
1 813  ARG n 
1 814  THR n 
1 815  GLN n 
1 816  ALA n 
1 817  TYR n 
1 818  LEU n 
1 819  GLU n 
1 820  GLU n 
1 821  LYS n 
1 822  ARG n 
1 823  LYS n 
1 824  ALA n 
1 825  GLU n 
1 826  ALA n 
1 827  LEU n 
1 828  LEU n 
1 829  TYR n 
1 830  GLN n 
1 831  ILE n 
1 832  LEU n 
1 833  PRO n 
1 834  HIS n 
1 835  SER n 
1 836  VAL n 
1 837  ALA n 
1 838  GLU n 
1 839  GLN n 
1 840  LEU n 
1 841  LYS n 
1 842  ARG n 
1 843  GLY n 
1 844  GLU n 
1 845  THR n 
1 846  VAL n 
1 847  GLN n 
1 848  ALA n 
1 849  GLU n 
1 850  ALA n 
1 851  PHE n 
1 852  ASP n 
1 853  SER n 
1 854  VAL n 
1 855  THR n 
1 856  ILE n 
1 857  TYR n 
1 858  PHE n 
1 859  SER n 
1 860  ASP n 
1 861  ILE n 
1 862  VAL n 
1 863  GLY n 
1 864  PHE n 
1 865  THR n 
1 866  ALA n 
1 867  LEU n 
1 868  SER n 
1 869  ALA n 
1 870  GLU n 
1 871  SER n 
1 872  THR n 
1 873  PRO n 
1 874  MET n 
1 875  GLN n 
1 876  VAL n 
1 877  VAL n 
1 878  THR n 
1 879  LEU n 
1 880  LEU n 
1 881  ASN n 
1 882  ASP n 
1 883  LEU n 
1 884  TYR n 
1 885  THR n 
1 886  CYS n 
1 887  PHE n 
1 888  ASP n 
1 889  ALA n 
1 890  VAL n 
1 891  ILE n 
1 892  ASP n 
1 893  ASN n 
1 894  PHE n 
1 895  ASP n 
1 896  VAL n 
1 897  TYR n 
1 898  LYS n 
1 899  VAL n 
1 900  GLU n 
1 901  THR n 
1 902  ILE n 
1 903  GLY n 
1 904  ASP n 
1 905  ALA n 
1 906  TYR n 
1 907  MET n 
1 908  VAL n 
1 909  VAL n 
1 910  SER n 
1 911  GLY n 
1 912  LEU n 
1 913  PRO n 
1 914  VAL n 
1 915  ARG n 
1 916  ASN n 
1 917  GLY n 
1 918  ARG n 
1 919  LEU n 
1 920  HIS n 
1 921  ALA n 
1 922  CYS n 
1 923  GLU n 
1 924  VAL n 
1 925  ALA n 
1 926  ARG n 
1 927  MET n 
1 928  ALA n 
1 929  LEU n 
1 930  ALA n 
1 931  LEU n 
1 932  LEU n 
1 933  ASP n 
1 934  ALA n 
1 935  VAL n 
1 936  ARG n 
1 937  SER n 
1 938  PHE n 
1 939  ARG n 
1 940  ILE n 
1 941  ARG n 
1 942  HIS n 
1 943  ARG n 
1 944  PRO n 
1 945  GLN n 
1 946  GLU n 
1 947  GLN n 
1 948  LEU n 
1 949  ARG n 
1 950  LEU n 
1 951  ARG n 
1 952  ILE n 
1 953  GLY n 
1 954  ILE n 
1 955  HIS n 
1 956  THR n 
1 957  GLY n 
1 958  PRO n 
1 959  VAL n 
1 960  CYS n 
1 961  ALA n 
1 962  GLY n 
1 963  VAL n 
1 964  VAL n 
1 965  GLY n 
1 966  LEU n 
1 967  LYS n 
1 968  MET n 
1 969  PRO n 
1 970  ARG n 
1 971  TYR n 
1 972  CYS n 
1 973  LEU n 
1 974  PHE n 
1 975  GLY n 
1 976  ASP n 
1 977  THR n 
1 978  VAL n 
1 979  ASN n 
1 980  THR n 
1 981  ALA n 
1 982  SER n 
1 983  ARG n 
1 984  MET n 
1 985  GLU n 
1 986  SER n 
1 987  ASN n 
1 988  GLY n 
1 989  GLU n 
1 990  ALA n 
1 991  LEU n 
1 992  LYS n 
1 993  ILE n 
1 994  HIS n 
1 995  LEU n 
1 996  SER n 
1 997  SER n 
1 998  GLU n 
1 999  THR n 
1 1000 LYS n 
1 1001 ALA n 
1 1002 VAL n 
1 1003 LEU n 
1 1004 GLU n 
1 1005 GLU n 
1 1006 PHE n 
1 1007 GLY n 
1 1008 GLY n 
1 1009 PHE n 
1 1010 GLU n 
1 1011 LEU n 
1 1012 GLU n 
1 1013 LEU n 
1 1014 ARG n 
1 1015 GLY n 
1 1016 ASP n 
1 1017 VAL n 
1 1018 GLU n 
1 1019 MET n 
1 1020 LYS n 
1 1021 GLY n 
1 1022 LYS n 
1 1023 GLY n 
1 1024 LYS n 
1 1025 VAL n 
1 1026 ARG n 
1 1027 THR n 
1 1028 TYR n 
1 1029 TRP n 
1 1030 LEU n 
1 1031 LEU n 
1 1032 GLY n 
1 1033 GLU n 
1 1034 ARG n 
1 1035 GLY n 
1 1036 SER n 
1 1037 SER n 
1 1038 THR n 
1 1039 ARG n 
1 1040 GLY n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   1040 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'NPR1, ANPRA' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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               'fall armyworm' 
_entity_src_gen.pdbx_host_org_scientific_name      'Spodoptera frugiperda' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7108 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_pdbx_entity_branch.entity_id   2 
_pdbx_entity_branch.type        oligosaccharide 
# 
loop_
_pdbx_entity_branch_descriptor.ordinal 
_pdbx_entity_branch_descriptor.entity_id 
_pdbx_entity_branch_descriptor.descriptor 
_pdbx_entity_branch_descriptor.type 
_pdbx_entity_branch_descriptor.program 
_pdbx_entity_branch_descriptor.program_version 
1 2 DManpa1-3DGlcpNAcb1-4DGlcpNAcb1-ROH                                          'Glycam Condensed Sequence' GMML       1.0   
2 2 'WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1a_1-5]/1-1-2/a4-b1_b3-c1' WURCS                       PDB2Glycan 1.1.0 
3 2 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(3+1)][a-D-Manp]{}}}'           LINUCS                      PDB-CARE   ?     
# 
loop_
_pdbx_entity_branch_link.link_id 
_pdbx_entity_branch_link.entity_id 
_pdbx_entity_branch_link.entity_branch_list_num_1 
_pdbx_entity_branch_link.comp_id_1 
_pdbx_entity_branch_link.atom_id_1 
_pdbx_entity_branch_link.leaving_atom_id_1 
_pdbx_entity_branch_link.entity_branch_list_num_2 
_pdbx_entity_branch_link.comp_id_2 
_pdbx_entity_branch_link.atom_id_2 
_pdbx_entity_branch_link.leaving_atom_id_2 
_pdbx_entity_branch_link.value_order 
_pdbx_entity_branch_link.details 
1 2 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
2 2 3 MAN C1 O1 2 NAG O3 HO3 sing ? 
# 
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 
CL  non-polymer                   . 'CHLORIDE ION'                           ? 'Cl -1'          35.453  
CYS 'L-peptide linking'           y CYSTEINE                                 ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking'           y GLUTAMINE                                ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking'           y 'GLUTAMIC ACID'                          ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'             y GLYCINE                                  ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking'           y HISTIDINE                                ? 'C6 H10 N3 O2 1' 156.162 
ILE 'L-peptide linking'           y ISOLEUCINE                               ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking'           y LEUCINE                                  ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking'           y LYSINE                                   ? 'C6 H15 N2 O2 1' 147.195 
MAN 'D-saccharide, alpha linking' . alpha-D-mannopyranose                    'alpha-D-mannose; D-mannose; mannose' 'C6 H12 O6' 
180.156 
MET 'L-peptide linking'           y METHIONINE                               ? 'C5 H11 N O2 S'  149.211 
NAG 'D-saccharide, beta linking'  . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'    221.208 
PHE 'L-peptide linking'           y PHENYLALANINE                            ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking'           y PROLINE                                  ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking'           y SERINE                                   ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking'           y THREONINE                                ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking'           y TRYPTOPHAN                               ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking'           y TYROSINE                                 ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking'           y VALINE                                   ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
MAN 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DManpa                         
MAN 'COMMON NAME'                         GMML     1.0 a-D-mannopyranose              
MAN 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 a-D-Manp                       
MAN 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Man                            
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1    ASP 1    -10  ?   ?   ?   A . n 
A 1 2    TYR 2    -9   ?   ?   ?   A . n 
A 1 3    LYS 3    -8   ?   ?   ?   A . n 
A 1 4    ASP 4    -7   ?   ?   ?   A . n 
A 1 5    ASP 5    -6   ?   ?   ?   A . n 
A 1 6    ASP 6    -5   ?   ?   ?   A . n 
A 1 7    ASP 7    -4   ?   ?   ?   A . n 
A 1 8    LYS 8    -3   ?   ?   ?   A . n 
A 1 9    ALA 9    -2   ?   ?   ?   A . n 
A 1 10   ALA 10   -1   ?   ?   ?   A . n 
A 1 11   ALA 11   0    ?   ?   ?   A . n 
A 1 12   GLY 12   1    1   GLY GLY A . n 
A 1 13   ASN 13   2    2   ASN ASN A . n 
A 1 14   LEU 14   3    3   LEU LEU A . n 
A 1 15   THR 15   4    4   THR THR A . n 
A 1 16   VAL 16   5    5   VAL VAL A . n 
A 1 17   ALA 17   6    6   ALA ALA A . n 
A 1 18   VAL 18   7    7   VAL VAL A . n 
A 1 19   VAL 19   8    8   VAL VAL A . n 
A 1 20   LEU 20   9    9   LEU LEU A . n 
A 1 21   PRO 21   10   10  PRO PRO A . n 
A 1 22   LEU 22   11   11  LEU LEU A . n 
A 1 23   ALA 23   12   12  ALA ALA A . n 
A 1 24   ASN 24   13   13  ASN ASN A . n 
A 1 25   THR 25   14   14  THR THR A . n 
A 1 26   SER 26   15   15  SER SER A . n 
A 1 27   TYR 27   16   16  TYR TYR A . n 
A 1 28   PRO 28   17   17  PRO PRO A . n 
A 1 29   TRP 29   18   18  TRP TRP A . n 
A 1 30   SER 30   19   19  SER SER A . n 
A 1 31   TRP 31   20   20  TRP TRP A . n 
A 1 32   ALA 32   21   21  ALA ALA A . n 
A 1 33   ARG 33   22   22  ARG ARG A . n 
A 1 34   VAL 34   23   23  VAL VAL A . n 
A 1 35   GLY 35   24   24  GLY GLY A . n 
A 1 36   PRO 36   25   25  PRO PRO A . n 
A 1 37   ALA 37   26   26  ALA ALA A . n 
A 1 38   VAL 38   27   27  VAL VAL A . n 
A 1 39   GLU 39   28   28  GLU GLU A . n 
A 1 40   LEU 40   29   29  LEU LEU A . n 
A 1 41   ALA 41   30   30  ALA ALA A . n 
A 1 42   LEU 42   31   31  LEU LEU A . n 
A 1 43   ALA 43   32   32  ALA ALA A . n 
A 1 44   GLN 44   33   33  GLN GLN A . n 
A 1 45   VAL 45   34   34  VAL VAL A . n 
A 1 46   LYS 46   35   35  LYS LYS A . n 
A 1 47   ALA 47   36   36  ALA ALA A . n 
A 1 48   ARG 48   37   37  ARG ARG A . n 
A 1 49   PRO 49   38   38  PRO PRO A . n 
A 1 50   ASP 50   39   39  ASP ASP A . n 
A 1 51   LEU 51   40   40  LEU LEU A . n 
A 1 52   LEU 52   41   41  LEU LEU A . n 
A 1 53   PRO 53   42   42  PRO PRO A . n 
A 1 54   GLY 54   43   43  GLY GLY A . n 
A 1 55   TRP 55   44   44  TRP TRP A . n 
A 1 56   THR 56   45   45  THR THR A . n 
A 1 57   VAL 57   46   46  VAL VAL A . n 
A 1 58   ARG 58   47   47  ARG ARG A . n 
A 1 59   THR 59   48   48  THR THR A . n 
A 1 60   VAL 60   49   49  VAL VAL A . n 
A 1 61   LEU 61   50   50  LEU LEU A . n 
A 1 62   GLY 62   51   51  GLY GLY A . n 
A 1 63   SER 63   52   52  SER SER A . n 
A 1 64   SER 64   53   53  SER SER A . n 
A 1 65   GLU 65   54   54  GLU GLU A . n 
A 1 66   ASN 66   55   55  ASN ASN A . n 
A 1 67   ALA 67   56   56  ALA ALA A . n 
A 1 68   LEU 68   57   57  LEU LEU A . n 
A 1 69   GLY 69   58   58  GLY GLY A . n 
A 1 70   VAL 70   59   59  VAL VAL A . n 
A 1 71   CYS 71   60   60  CYS CYS A . n 
A 1 72   SER 72   61   61  SER SER A . n 
A 1 73   ASP 73   62   62  ASP ASP A . n 
A 1 74   THR 74   63   63  THR THR A . n 
A 1 75   ALA 75   64   64  ALA ALA A . n 
A 1 76   ALA 76   65   65  ALA ALA A . n 
A 1 77   PRO 77   66   66  PRO PRO A . n 
A 1 78   LEU 78   67   67  LEU LEU A . n 
A 1 79   ALA 79   68   68  ALA ALA A . n 
A 1 80   ALA 80   69   69  ALA ALA A . n 
A 1 81   VAL 81   70   70  VAL VAL A . n 
A 1 82   ASP 82   71   71  ASP ASP A . n 
A 1 83   LEU 83   72   72  LEU LEU A . n 
A 1 84   LYS 84   73   73  LYS LYS A . n 
A 1 85   TRP 85   74   74  TRP TRP A . n 
A 1 86   GLU 86   75   75  GLU GLU A . n 
A 1 87   HIS 87   76   76  HIS HIS A . n 
A 1 88   ASN 88   77   77  ASN ASN A . n 
A 1 89   PRO 89   78   78  PRO PRO A . n 
A 1 90   ALA 90   79   79  ALA ALA A . n 
A 1 91   VAL 91   80   80  VAL VAL A . n 
A 1 92   PHE 92   81   81  PHE PHE A . n 
A 1 93   LEU 93   82   82  LEU LEU A . n 
A 1 94   GLY 94   83   83  GLY GLY A . n 
A 1 95   PRO 95   84   84  PRO PRO A . n 
A 1 96   GLY 96   85   85  GLY GLY A . n 
A 1 97   CYS 97   86   86  CYS CYS A . n 
A 1 98   VAL 98   87   87  VAL VAL A . n 
A 1 99   TYR 99   88   88  TYR TYR A . n 
A 1 100  ALA 100  89   89  ALA ALA A . n 
A 1 101  ALA 101  90   90  ALA ALA A . n 
A 1 102  ALA 102  91   91  ALA ALA A . n 
A 1 103  PRO 103  92   92  PRO PRO A . n 
A 1 104  VAL 104  93   93  VAL VAL A . n 
A 1 105  GLY 105  94   94  GLY GLY A . n 
A 1 106  ARG 106  95   95  ARG ARG A . n 
A 1 107  PHE 107  96   96  PHE PHE A . n 
A 1 108  THR 108  97   97  THR THR A . n 
A 1 109  ALA 109  98   98  ALA ALA A . n 
A 1 110  HIS 110  99   99  HIS HIS A . n 
A 1 111  TRP 111  100  100 TRP TRP A . n 
A 1 112  ARG 112  101  101 ARG ARG A . n 
A 1 113  VAL 113  102  102 VAL VAL A . n 
A 1 114  PRO 114  103  103 PRO PRO A . n 
A 1 115  LEU 115  104  104 LEU LEU A . n 
A 1 116  LEU 116  105  105 LEU LEU A . n 
A 1 117  THR 117  106  106 THR THR A . n 
A 1 118  ALA 118  107  107 ALA ALA A . n 
A 1 119  GLY 119  108  108 GLY GLY A . n 
A 1 120  ALA 120  109  109 ALA ALA A . n 
A 1 121  PRO 121  110  110 PRO PRO A . n 
A 1 122  ALA 122  111  111 ALA ALA A . n 
A 1 123  LEU 123  112  112 LEU LEU A . n 
A 1 124  GLY 124  113  113 GLY GLY A . n 
A 1 125  PHE 125  114  114 PHE PHE A . n 
A 1 126  GLY 126  115  115 GLY GLY A . n 
A 1 127  VAL 127  116  116 VAL VAL A . n 
A 1 128  LYS 128  117  117 LYS LYS A . n 
A 1 129  ASP 129  118  118 ASP ASP A . n 
A 1 130  GLU 130  119  119 GLU GLU A . n 
A 1 131  TYR 131  120  120 TYR TYR A . n 
A 1 132  ALA 132  121  121 ALA ALA A . n 
A 1 133  LEU 133  122  122 LEU LEU A . n 
A 1 134  THR 134  123  123 THR THR A . n 
A 1 135  THR 135  124  124 THR THR A . n 
A 1 136  ARG 136  125  125 ARG ARG A . n 
A 1 137  ALA 137  126  126 ALA ALA A . n 
A 1 138  GLY 138  127  127 GLY GLY A . n 
A 1 139  PRO 139  128  128 PRO PRO A . n 
A 1 140  SER 140  129  129 SER SER A . n 
A 1 141  TYR 141  130  130 TYR TYR A . n 
A 1 142  ALA 142  131  131 ALA ALA A . n 
A 1 143  LYS 143  132  132 LYS LYS A . n 
A 1 144  LEU 144  133  133 LEU LEU A . n 
A 1 145  GLY 145  134  134 GLY GLY A . n 
A 1 146  ASP 146  135  135 ASP ASP A . n 
A 1 147  PHE 147  136  136 PHE PHE A . n 
A 1 148  VAL 148  137  137 VAL VAL A . n 
A 1 149  ALA 149  138  138 ALA ALA A . n 
A 1 150  ALA 150  139  139 ALA ALA A . n 
A 1 151  LEU 151  140  140 LEU LEU A . n 
A 1 152  HIS 152  141  141 HIS HIS A . n 
A 1 153  ARG 153  142  142 ARG ARG A . n 
A 1 154  ARG 154  143  143 ARG ARG A . n 
A 1 155  LEU 155  144  144 LEU LEU A . n 
A 1 156  GLY 156  145  145 GLY GLY A . n 
A 1 157  TRP 157  146  146 TRP TRP A . n 
A 1 158  GLU 158  147  147 GLU GLU A . n 
A 1 159  ARG 159  148  148 ARG ARG A . n 
A 1 160  GLN 160  149  149 GLN GLN A . n 
A 1 161  ALA 161  150  150 ALA ALA A . n 
A 1 162  LEU 162  151  151 LEU LEU A . n 
A 1 163  MET 163  152  152 MET MET A . n 
A 1 164  LEU 164  153  153 LEU LEU A . n 
A 1 165  TYR 165  154  154 TYR TYR A . n 
A 1 166  ALA 166  155  155 ALA ALA A . n 
A 1 167  TYR 167  156  156 TYR TYR A . n 
A 1 168  ARG 168  157  157 ARG ARG A . n 
A 1 169  PRO 169  158  158 PRO PRO A . n 
A 1 170  GLY 170  159  159 GLY GLY A . n 
A 1 171  ASP 171  160  160 ASP ASP A . n 
A 1 172  GLU 172  161  161 GLU GLU A . n 
A 1 173  GLU 173  162  162 GLU GLU A . n 
A 1 174  HIS 174  163  163 HIS HIS A . n 
A 1 175  CYS 175  164  164 CYS CYS A . n 
A 1 176  PHE 176  165  165 PHE PHE A . n 
A 1 177  PHE 177  166  166 PHE PHE A . n 
A 1 178  LEU 178  167  167 LEU LEU A . n 
A 1 179  VAL 179  168  168 VAL VAL A . n 
A 1 180  GLU 180  169  169 GLU GLU A . n 
A 1 181  GLY 181  170  170 GLY GLY A . n 
A 1 182  LEU 182  171  171 LEU LEU A . n 
A 1 183  PHE 183  172  172 PHE PHE A . n 
A 1 184  MET 184  173  173 MET MET A . n 
A 1 185  ARG 185  174  174 ARG ARG A . n 
A 1 186  VAL 186  175  175 VAL VAL A . n 
A 1 187  ARG 187  176  176 ARG ARG A . n 
A 1 188  ASP 188  177  177 ASP ASP A . n 
A 1 189  ARG 189  178  178 ARG ARG A . n 
A 1 190  LEU 190  179  179 LEU LEU A . n 
A 1 191  ASN 191  180  180 ASN ASN A . n 
A 1 192  ILE 192  181  181 ILE ILE A . n 
A 1 193  THR 193  182  182 THR THR A . n 
A 1 194  VAL 194  183  183 VAL VAL A . n 
A 1 195  ASP 195  184  184 ASP ASP A . n 
A 1 196  HIS 196  185  185 HIS HIS A . n 
A 1 197  LEU 197  186  186 LEU LEU A . n 
A 1 198  GLU 198  187  187 GLU GLU A . n 
A 1 199  PHE 199  188  188 PHE PHE A . n 
A 1 200  ALA 200  189  189 ALA ALA A . n 
A 1 201  GLU 201  190  190 GLU GLU A . n 
A 1 202  ASP 202  191  191 ASP ASP A . n 
A 1 203  ASP 203  192  192 ASP ASP A . n 
A 1 204  LEU 204  193  193 LEU LEU A . n 
A 1 205  SER 205  194  194 SER SER A . n 
A 1 206  HIS 206  195  195 HIS HIS A . n 
A 1 207  TYR 207  196  196 TYR TYR A . n 
A 1 208  THR 208  197  197 THR THR A . n 
A 1 209  ARG 209  198  198 ARG ARG A . n 
A 1 210  LEU 210  199  199 LEU LEU A . n 
A 1 211  LEU 211  200  200 LEU LEU A . n 
A 1 212  ARG 212  201  201 ARG ARG A . n 
A 1 213  THR 213  202  202 THR THR A . n 
A 1 214  MET 214  203  203 MET MET A . n 
A 1 215  PRO 215  204  204 PRO PRO A . n 
A 1 216  ARG 216  205  205 ARG ARG A . n 
A 1 217  LYS 217  206  206 LYS LYS A . n 
A 1 218  GLY 218  207  207 GLY GLY A . n 
A 1 219  ARG 219  208  208 ARG ARG A . n 
A 1 220  VAL 220  209  209 VAL VAL A . n 
A 1 221  ILE 221  210  210 ILE ILE A . n 
A 1 222  TYR 222  211  211 TYR TYR A . n 
A 1 223  ILE 223  212  212 ILE ILE A . n 
A 1 224  CYS 224  213  213 CYS CYS A . n 
A 1 225  SER 225  214  214 SER SER A . n 
A 1 226  SER 226  215  215 SER SER A . n 
A 1 227  PRO 227  216  216 PRO PRO A . n 
A 1 228  ASP 228  217  217 ASP ASP A . n 
A 1 229  ALA 229  218  218 ALA ALA A . n 
A 1 230  PHE 230  219  219 PHE PHE A . n 
A 1 231  ARG 231  220  220 ARG ARG A . n 
A 1 232  THR 232  221  221 THR THR A . n 
A 1 233  LEU 233  222  222 LEU LEU A . n 
A 1 234  MET 234  223  223 MET MET A . n 
A 1 235  LEU 235  224  224 LEU LEU A . n 
A 1 236  LEU 236  225  225 LEU LEU A . n 
A 1 237  ALA 237  226  226 ALA ALA A . n 
A 1 238  LEU 238  227  227 LEU LEU A . n 
A 1 239  GLU 239  228  228 GLU GLU A . n 
A 1 240  ALA 240  229  229 ALA ALA A . n 
A 1 241  GLY 241  230  230 GLY GLY A . n 
A 1 242  LEU 242  231  231 LEU LEU A . n 
A 1 243  CYS 243  232  232 CYS CYS A . n 
A 1 244  GLY 244  233  233 GLY GLY A . n 
A 1 245  GLU 245  234  234 GLU GLU A . n 
A 1 246  ASP 246  235  235 ASP ASP A . n 
A 1 247  TYR 247  236  236 TYR TYR A . n 
A 1 248  VAL 248  237  237 VAL VAL A . n 
A 1 249  PHE 249  238  238 PHE PHE A . n 
A 1 250  PHE 250  239  239 PHE PHE A . n 
A 1 251  HIS 251  240  240 HIS HIS A . n 
A 1 252  LEU 252  241  241 LEU LEU A . n 
A 1 253  ASP 253  242  242 ASP ASP A . n 
A 1 254  ILE 254  243  243 ILE ILE A . n 
A 1 255  PHE 255  244  244 PHE PHE A . n 
A 1 256  GLY 256  245  245 GLY GLY A . n 
A 1 257  GLN 257  246  246 GLN GLN A . n 
A 1 258  SER 258  247  247 SER SER A . n 
A 1 259  LEU 259  248  248 LEU LEU A . n 
A 1 260  GLN 260  249  249 GLN GLN A . n 
A 1 261  GLY 261  250  250 GLY GLY A . n 
A 1 262  GLY 262  251  251 GLY GLY A . n 
A 1 263  GLN 263  252  252 GLN GLN A . n 
A 1 264  GLY 264  253  253 GLY GLY A . n 
A 1 265  PRO 265  254  254 PRO PRO A . n 
A 1 266  ALA 266  255  255 ALA ALA A . n 
A 1 267  PRO 267  256  256 PRO PRO A . n 
A 1 268  ARG 268  257  257 ARG ARG A . n 
A 1 269  ARG 269  258  258 ARG ARG A . n 
A 1 270  PRO 270  259  259 PRO PRO A . n 
A 1 271  TRP 271  260  260 TRP TRP A . n 
A 1 272  GLU 272  261  261 GLU GLU A . n 
A 1 273  ARG 273  262  262 ARG ARG A . n 
A 1 274  GLY 274  263  263 GLY GLY A . n 
A 1 275  ASP 275  264  264 ASP ASP A . n 
A 1 276  GLY 276  265  265 GLY GLY A . n 
A 1 277  GLN 277  266  266 GLN GLN A . n 
A 1 278  ASP 278  267  267 ASP ASP A . n 
A 1 279  VAL 279  268  268 VAL VAL A . n 
A 1 280  SER 280  269  269 SER SER A . n 
A 1 281  ALA 281  270  270 ALA ALA A . n 
A 1 282  ARG 282  271  271 ARG ARG A . n 
A 1 283  GLN 283  272  272 GLN GLN A . n 
A 1 284  ALA 284  273  273 ALA ALA A . n 
A 1 285  PHE 285  274  274 PHE PHE A . n 
A 1 286  GLN 286  275  275 GLN GLN A . n 
A 1 287  ALA 287  276  276 ALA ALA A . n 
A 1 288  ALA 288  277  277 ALA ALA A . n 
A 1 289  LYS 289  278  278 LYS LYS A . n 
A 1 290  ILE 290  279  279 ILE ILE A . n 
A 1 291  ILE 291  280  280 ILE ILE A . n 
A 1 292  THR 292  281  281 THR THR A . n 
A 1 293  TYR 293  282  282 TYR TYR A . n 
A 1 294  LYS 294  283  283 LYS LYS A . n 
A 1 295  ASP 295  284  284 ASP ASP A . n 
A 1 296  PRO 296  285  285 PRO PRO A . n 
A 1 297  ASP 297  286  286 ASP ASP A . n 
A 1 298  ASN 298  287  287 ASN ASN A . n 
A 1 299  PRO 299  288  288 PRO PRO A . n 
A 1 300  GLU 300  289  289 GLU GLU A . n 
A 1 301  TYR 301  290  290 TYR TYR A . n 
A 1 302  LEU 302  291  291 LEU LEU A . n 
A 1 303  GLU 303  292  292 GLU GLU A . n 
A 1 304  PHE 304  293  293 PHE PHE A . n 
A 1 305  LEU 305  294  294 LEU LEU A . n 
A 1 306  LYS 306  295  295 LYS LYS A . n 
A 1 307  GLN 307  296  296 GLN GLN A . n 
A 1 308  LEU 308  297  297 LEU LEU A . n 
A 1 309  LYS 309  298  298 LYS LYS A . n 
A 1 310  HIS 310  299  299 HIS HIS A . n 
A 1 311  LEU 311  300  300 LEU LEU A . n 
A 1 312  ALA 312  301  301 ALA ALA A . n 
A 1 313  TYR 313  302  302 TYR TYR A . n 
A 1 314  GLU 314  303  303 GLU GLU A . n 
A 1 315  GLN 315  304  304 GLN GLN A . n 
A 1 316  PHE 316  305  305 PHE PHE A . n 
A 1 317  ASN 317  306  306 ASN ASN A . n 
A 1 318  PHE 318  307  307 PHE PHE A . n 
A 1 319  THR 319  308  308 THR THR A . n 
A 1 320  MET 320  309  309 MET MET A . n 
A 1 321  GLU 321  310  310 GLU GLU A . n 
A 1 322  ASP 322  311  311 ASP ASP A . n 
A 1 323  GLY 323  312  312 GLY GLY A . n 
A 1 324  LEU 324  313  313 LEU LEU A . n 
A 1 325  VAL 325  314  314 VAL VAL A . n 
A 1 326  ASN 326  315  315 ASN ASN A . n 
A 1 327  THR 327  316  316 THR THR A . n 
A 1 328  ILE 328  317  317 ILE ILE A . n 
A 1 329  PRO 329  318  318 PRO PRO A . n 
A 1 330  ALA 330  319  319 ALA ALA A . n 
A 1 331  SER 331  320  320 SER SER A . n 
A 1 332  PHE 332  321  321 PHE PHE A . n 
A 1 333  HIS 333  322  322 HIS HIS A . n 
A 1 334  ASP 334  323  323 ASP ASP A . n 
A 1 335  GLY 335  324  324 GLY GLY A . n 
A 1 336  LEU 336  325  325 LEU LEU A . n 
A 1 337  LEU 337  326  326 LEU LEU A . n 
A 1 338  LEU 338  327  327 LEU LEU A . n 
A 1 339  TYR 339  328  328 TYR TYR A . n 
A 1 340  ILE 340  329  329 ILE ILE A . n 
A 1 341  GLN 341  330  330 GLN GLN A . n 
A 1 342  ALA 342  331  331 ALA ALA A . n 
A 1 343  VAL 343  332  332 VAL VAL A . n 
A 1 344  THR 344  333  333 THR THR A . n 
A 1 345  GLU 345  334  334 GLU GLU A . n 
A 1 346  THR 346  335  335 THR THR A . n 
A 1 347  LEU 347  336  336 LEU LEU A . n 
A 1 348  ALA 348  337  337 ALA ALA A . n 
A 1 349  HIS 349  338  338 HIS HIS A . n 
A 1 350  GLY 350  339  339 GLY GLY A . n 
A 1 351  GLY 351  340  340 GLY GLY A . n 
A 1 352  THR 352  341  341 THR THR A . n 
A 1 353  VAL 353  342  342 VAL VAL A . n 
A 1 354  THR 354  343  343 THR THR A . n 
A 1 355  ASP 355  344  344 ASP ASP A . n 
A 1 356  GLY 356  345  345 GLY GLY A . n 
A 1 357  GLU 357  346  346 GLU GLU A . n 
A 1 358  ASN 358  347  347 ASN ASN A . n 
A 1 359  ILE 359  348  348 ILE ILE A . n 
A 1 360  THR 360  349  349 THR THR A . n 
A 1 361  GLN 361  350  350 GLN GLN A . n 
A 1 362  ARG 362  351  351 ARG ARG A . n 
A 1 363  MET 363  352  352 MET MET A . n 
A 1 364  TRP 364  353  353 TRP TRP A . n 
A 1 365  ASN 365  354  354 ASN ASN A . n 
A 1 366  ARG 366  355  355 ARG ARG A . n 
A 1 367  SER 367  356  356 SER SER A . n 
A 1 368  PHE 368  357  357 PHE PHE A . n 
A 1 369  GLN 369  358  358 GLN GLN A . n 
A 1 370  GLY 370  359  359 GLY GLY A . n 
A 1 371  VAL 371  360  360 VAL VAL A . n 
A 1 372  THR 372  361  361 THR THR A . n 
A 1 373  GLY 373  362  362 GLY GLY A . n 
A 1 374  TYR 374  363  363 TYR TYR A . n 
A 1 375  LEU 375  364  364 LEU LEU A . n 
A 1 376  LYS 376  365  365 LYS LYS A . n 
A 1 377  ILE 377  366  366 ILE ILE A . n 
A 1 378  ASP 378  367  367 ASP ASP A . n 
A 1 379  SER 379  368  368 SER SER A . n 
A 1 380  SER 380  369  369 SER SER A . n 
A 1 381  GLY 381  370  370 GLY GLY A . n 
A 1 382  ASP 382  371  371 ASP ASP A . n 
A 1 383  ARG 383  372  372 ARG ARG A . n 
A 1 384  GLU 384  373  373 GLU GLU A . n 
A 1 385  THR 385  374  374 THR THR A . n 
A 1 386  ASP 386  375  375 ASP ASP A . n 
A 1 387  PHE 387  376  376 PHE PHE A . n 
A 1 388  SER 388  377  377 SER SER A . n 
A 1 389  LEU 389  378  378 LEU LEU A . n 
A 1 390  TRP 390  379  379 TRP TRP A . n 
A 1 391  ASP 391  380  380 ASP ASP A . n 
A 1 392  MET 392  381  381 MET MET A . n 
A 1 393  ASP 393  382  382 ASP ASP A . n 
A 1 394  PRO 394  383  383 PRO PRO A . n 
A 1 395  GLU 395  384  384 GLU GLU A . n 
A 1 396  ASN 396  385  385 ASN ASN A . n 
A 1 397  GLY 397  386  386 GLY GLY A . n 
A 1 398  ALA 398  387  387 ALA ALA A . n 
A 1 399  PHE 399  388  388 PHE PHE A . n 
A 1 400  ARG 400  389  389 ARG ARG A . n 
A 1 401  VAL 401  390  390 VAL VAL A . n 
A 1 402  VAL 402  391  391 VAL VAL A . n 
A 1 403  LEU 403  392  392 LEU LEU A . n 
A 1 404  ASN 404  393  393 ASN ASN A . n 
A 1 405  TYR 405  394  394 TYR TYR A . n 
A 1 406  ASN 406  395  395 ASN ASN A . n 
A 1 407  GLY 407  396  396 GLY GLY A . n 
A 1 408  THR 408  397  397 THR THR A . n 
A 1 409  SER 409  398  398 SER SER A . n 
A 1 410  GLN 410  399  399 GLN GLN A . n 
A 1 411  GLU 411  400  400 GLU GLU A . n 
A 1 412  LEU 412  401  401 LEU LEU A . n 
A 1 413  VAL 413  402  402 VAL VAL A . n 
A 1 414  ALA 414  403  403 ALA ALA A . n 
A 1 415  VAL 415  404  404 VAL VAL A . n 
A 1 416  SER 416  405  405 SER SER A . n 
A 1 417  GLY 417  406  406 GLY GLY A . n 
A 1 418  ARG 418  407  407 ARG ARG A . n 
A 1 419  LYS 419  408  408 LYS LYS A . n 
A 1 420  LEU 420  409  409 LEU LEU A . n 
A 1 421  ASN 421  410  410 ASN ASN A . n 
A 1 422  TRP 422  411  411 TRP TRP A . n 
A 1 423  PRO 423  412  412 PRO PRO A . n 
A 1 424  LEU 424  413  413 LEU LEU A . n 
A 1 425  GLY 425  414  414 GLY GLY A . n 
A 1 426  TYR 426  415  415 TYR TYR A . n 
A 1 427  PRO 427  416  416 PRO PRO A . n 
A 1 428  PRO 428  417  417 PRO PRO A . n 
A 1 429  PRO 429  418  418 PRO PRO A . n 
A 1 430  ASP 430  419  419 ASP ASP A . n 
A 1 431  ILE 431  420  420 ILE ILE A . n 
A 1 432  PRO 432  421  421 PRO PRO A . n 
A 1 433  LYS 433  422  422 LYS LYS A . n 
A 1 434  CYS 434  423  423 CYS CYS A . n 
A 1 435  GLY 435  424  424 GLY GLY A . n 
A 1 436  PHE 436  425  425 PHE PHE A . n 
A 1 437  ASP 437  426  ?   ?   ?   A . n 
A 1 438  ASN 438  427  ?   ?   ?   A . n 
A 1 439  GLU 439  428  ?   ?   ?   A . n 
A 1 440  ASP 440  429  ?   ?   ?   A . n 
A 1 441  PRO 441  430  ?   ?   ?   A . n 
A 1 442  ALA 442  431  ?   ?   ?   A . n 
A 1 443  CYS 443  432  ?   ?   ?   A . n 
A 1 444  ASN 444  433  ?   ?   ?   A . n 
A 1 445  GLN 445  434  ?   ?   ?   A . n 
A 1 446  ASP 446  435  ?   ?   ?   A . n 
A 1 447  HIS 447  436  ?   ?   ?   A . n 
A 1 448  LEU 448  437  ?   ?   ?   A . n 
A 1 449  SER 449  438  ?   ?   ?   A . n 
A 1 450  THR 450  439  ?   ?   ?   A . n 
A 1 451  LEU 451  440  ?   ?   ?   A . n 
A 1 452  GLU 452  441  ?   ?   ?   A . n 
A 1 453  VAL 453  442  ?   ?   ?   A . n 
A 1 454  LEU 454  443  ?   ?   ?   A . n 
A 1 455  ALA 455  444  ?   ?   ?   A . n 
A 1 456  LEU 456  445  ?   ?   ?   A . n 
A 1 457  VAL 457  446  ?   ?   ?   A . n 
A 1 458  GLY 458  447  ?   ?   ?   A . n 
A 1 459  SER 459  448  ?   ?   ?   A . n 
A 1 460  LEU 460  449  ?   ?   ?   A . n 
A 1 461  SER 461  450  ?   ?   ?   A . n 
A 1 462  LEU 462  451  ?   ?   ?   A . n 
A 1 463  LEU 463  452  ?   ?   ?   A . n 
A 1 464  GLY 464  453  ?   ?   ?   A . n 
A 1 465  ILE 465  454  ?   ?   ?   A . n 
A 1 466  LEU 466  455  ?   ?   ?   A . n 
A 1 467  ILE 467  456  ?   ?   ?   A . n 
A 1 468  VAL 468  457  ?   ?   ?   A . n 
A 1 469  SER 469  458  ?   ?   ?   A . n 
A 1 470  PHE 470  459  ?   ?   ?   A . n 
A 1 471  PHE 471  460  ?   ?   ?   A . n 
A 1 472  ILE 472  461  ?   ?   ?   A . n 
A 1 473  TYR 473  462  ?   ?   ?   A . n 
A 1 474  ARG 474  463  ?   ?   ?   A . n 
A 1 475  LYS 475  464  ?   ?   ?   A . n 
A 1 476  MET 476  465  ?   ?   ?   A . n 
A 1 477  GLN 477  466  ?   ?   ?   A . n 
A 1 478  LEU 478  467  ?   ?   ?   A . n 
A 1 479  GLU 479  468  ?   ?   ?   A . n 
A 1 480  LYS 480  469  ?   ?   ?   A . n 
A 1 481  GLU 481  470  ?   ?   ?   A . n 
A 1 482  LEU 482  471  ?   ?   ?   A . n 
A 1 483  ALA 483  472  ?   ?   ?   A . n 
A 1 484  SER 484  473  ?   ?   ?   A . n 
A 1 485  GLU 485  474  ?   ?   ?   A . n 
A 1 486  LEU 486  475  ?   ?   ?   A . n 
A 1 487  TRP 487  476  ?   ?   ?   A . n 
A 1 488  ARG 488  477  ?   ?   ?   A . n 
A 1 489  VAL 489  478  ?   ?   ?   A . n 
A 1 490  ARG 490  479  ?   ?   ?   A . n 
A 1 491  TRP 491  480  ?   ?   ?   A . n 
A 1 492  GLU 492  481  ?   ?   ?   A . n 
A 1 493  ASP 493  482  ?   ?   ?   A . n 
A 1 494  VAL 494  483  ?   ?   ?   A . n 
A 1 495  GLU 495  484  ?   ?   ?   A . n 
A 1 496  PRO 496  485  ?   ?   ?   A . n 
A 1 497  SER 497  486  ?   ?   ?   A . n 
A 1 498  SER 498  487  ?   ?   ?   A . n 
A 1 499  LEU 499  488  ?   ?   ?   A . n 
A 1 500  GLU 500  489  ?   ?   ?   A . n 
A 1 501  ARG 501  490  ?   ?   ?   A . n 
A 1 502  HIS 502  491  ?   ?   ?   A . n 
A 1 503  LEU 503  492  ?   ?   ?   A . n 
A 1 504  ARG 504  493  ?   ?   ?   A . n 
A 1 505  SER 505  494  ?   ?   ?   A . n 
A 1 506  ALA 506  495  ?   ?   ?   A . n 
A 1 507  GLY 507  496  ?   ?   ?   A . n 
A 1 508  SER 508  497  ?   ?   ?   A . n 
A 1 509  ARG 509  498  ?   ?   ?   A . n 
A 1 510  LEU 510  499  ?   ?   ?   A . n 
A 1 511  THR 511  500  ?   ?   ?   A . n 
A 1 512  LEU 512  501  ?   ?   ?   A . n 
A 1 513  SER 513  502  ?   ?   ?   A . n 
A 1 514  GLY 514  503  ?   ?   ?   A . n 
A 1 515  ARG 515  504  ?   ?   ?   A . n 
A 1 516  GLY 516  505  ?   ?   ?   A . n 
A 1 517  SER 517  506  ?   ?   ?   A . n 
A 1 518  ASN 518  507  ?   ?   ?   A . n 
A 1 519  TYR 519  508  ?   ?   ?   A . n 
A 1 520  GLY 520  509  ?   ?   ?   A . n 
A 1 521  SER 521  510  ?   ?   ?   A . n 
A 1 522  LEU 522  511  ?   ?   ?   A . n 
A 1 523  LEU 523  512  ?   ?   ?   A . n 
A 1 524  THR 524  513  ?   ?   ?   A . n 
A 1 525  THR 525  514  ?   ?   ?   A . n 
A 1 526  GLU 526  515  ?   ?   ?   A . n 
A 1 527  GLY 527  516  ?   ?   ?   A . n 
A 1 528  GLN 528  517  ?   ?   ?   A . n 
A 1 529  PHE 529  518  ?   ?   ?   A . n 
A 1 530  GLN 530  519  ?   ?   ?   A . n 
A 1 531  VAL 531  520  ?   ?   ?   A . n 
A 1 532  PHE 532  521  ?   ?   ?   A . n 
A 1 533  ALA 533  522  ?   ?   ?   A . n 
A 1 534  LYS 534  523  ?   ?   ?   A . n 
A 1 535  THR 535  524  ?   ?   ?   A . n 
A 1 536  ALA 536  525  ?   ?   ?   A . n 
A 1 537  TYR 537  526  ?   ?   ?   A . n 
A 1 538  TYR 538  527  ?   ?   ?   A . n 
A 1 539  LYS 539  528  ?   ?   ?   A . n 
A 1 540  GLY 540  529  ?   ?   ?   A . n 
A 1 541  ASN 541  530  ?   ?   ?   A . n 
A 1 542  LEU 542  531  ?   ?   ?   A . n 
A 1 543  VAL 543  532  ?   ?   ?   A . n 
A 1 544  ALA 544  533  ?   ?   ?   A . n 
A 1 545  VAL 545  534  ?   ?   ?   A . n 
A 1 546  LYS 546  535  ?   ?   ?   A . n 
A 1 547  ARG 547  536  ?   ?   ?   A . n 
A 1 548  VAL 548  537  ?   ?   ?   A . n 
A 1 549  ASN 549  538  ?   ?   ?   A . n 
A 1 550  ARG 550  539  ?   ?   ?   A . n 
A 1 551  LYS 551  540  ?   ?   ?   A . n 
A 1 552  ARG 552  541  ?   ?   ?   A . n 
A 1 553  ILE 553  542  ?   ?   ?   A . n 
A 1 554  GLU 554  543  ?   ?   ?   A . n 
A 1 555  LEU 555  544  ?   ?   ?   A . n 
A 1 556  THR 556  545  ?   ?   ?   A . n 
A 1 557  ARG 557  546  ?   ?   ?   A . n 
A 1 558  LYS 558  547  ?   ?   ?   A . n 
A 1 559  VAL 559  548  ?   ?   ?   A . n 
A 1 560  LEU 560  549  ?   ?   ?   A . n 
A 1 561  PHE 561  550  ?   ?   ?   A . n 
A 1 562  GLU 562  551  ?   ?   ?   A . n 
A 1 563  LEU 563  552  ?   ?   ?   A . n 
A 1 564  LYS 564  553  ?   ?   ?   A . n 
A 1 565  HIS 565  554  ?   ?   ?   A . n 
A 1 566  MET 566  555  ?   ?   ?   A . n 
A 1 567  ARG 567  556  ?   ?   ?   A . n 
A 1 568  ASP 568  557  ?   ?   ?   A . n 
A 1 569  VAL 569  558  ?   ?   ?   A . n 
A 1 570  GLN 570  559  ?   ?   ?   A . n 
A 1 571  ASN 571  560  ?   ?   ?   A . n 
A 1 572  GLU 572  561  ?   ?   ?   A . n 
A 1 573  HIS 573  562  ?   ?   ?   A . n 
A 1 574  LEU 574  563  ?   ?   ?   A . n 
A 1 575  THR 575  564  ?   ?   ?   A . n 
A 1 576  ARG 576  565  ?   ?   ?   A . n 
A 1 577  PHE 577  566  ?   ?   ?   A . n 
A 1 578  VAL 578  567  ?   ?   ?   A . n 
A 1 579  GLY 579  568  ?   ?   ?   A . n 
A 1 580  ALA 580  569  ?   ?   ?   A . n 
A 1 581  CYS 581  570  ?   ?   ?   A . n 
A 1 582  THR 582  571  ?   ?   ?   A . n 
A 1 583  ASP 583  572  ?   ?   ?   A . n 
A 1 584  PRO 584  573  ?   ?   ?   A . n 
A 1 585  PRO 585  574  ?   ?   ?   A . n 
A 1 586  ASN 586  575  ?   ?   ?   A . n 
A 1 587  ILE 587  576  ?   ?   ?   A . n 
A 1 588  CYS 588  577  ?   ?   ?   A . n 
A 1 589  ILE 589  578  ?   ?   ?   A . n 
A 1 590  LEU 590  579  ?   ?   ?   A . n 
A 1 591  THR 591  580  ?   ?   ?   A . n 
A 1 592  GLU 592  581  ?   ?   ?   A . n 
A 1 593  TYR 593  582  ?   ?   ?   A . n 
A 1 594  CYS 594  583  ?   ?   ?   A . n 
A 1 595  PRO 595  584  ?   ?   ?   A . n 
A 1 596  ARG 596  585  ?   ?   ?   A . n 
A 1 597  GLY 597  586  ?   ?   ?   A . n 
A 1 598  SER 598  587  ?   ?   ?   A . n 
A 1 599  LEU 599  588  ?   ?   ?   A . n 
A 1 600  GLN 600  589  ?   ?   ?   A . n 
A 1 601  ASP 601  590  ?   ?   ?   A . n 
A 1 602  ILE 602  591  ?   ?   ?   A . n 
A 1 603  LEU 603  592  ?   ?   ?   A . n 
A 1 604  GLU 604  593  ?   ?   ?   A . n 
A 1 605  ASN 605  594  ?   ?   ?   A . n 
A 1 606  GLU 606  595  ?   ?   ?   A . n 
A 1 607  SER 607  596  ?   ?   ?   A . n 
A 1 608  ILE 608  597  ?   ?   ?   A . n 
A 1 609  THR 609  598  ?   ?   ?   A . n 
A 1 610  LEU 610  599  ?   ?   ?   A . n 
A 1 611  ASP 611  600  ?   ?   ?   A . n 
A 1 612  TRP 612  601  ?   ?   ?   A . n 
A 1 613  MET 613  602  ?   ?   ?   A . n 
A 1 614  PHE 614  603  ?   ?   ?   A . n 
A 1 615  ARG 615  604  ?   ?   ?   A . n 
A 1 616  TYR 616  605  ?   ?   ?   A . n 
A 1 617  SER 617  606  ?   ?   ?   A . n 
A 1 618  LEU 618  607  ?   ?   ?   A . n 
A 1 619  THR 619  608  ?   ?   ?   A . n 
A 1 620  ASN 620  609  ?   ?   ?   A . n 
A 1 621  ASP 621  610  ?   ?   ?   A . n 
A 1 622  ILE 622  611  ?   ?   ?   A . n 
A 1 623  VAL 623  612  ?   ?   ?   A . n 
A 1 624  LYS 624  613  ?   ?   ?   A . n 
A 1 625  GLY 625  614  ?   ?   ?   A . n 
A 1 626  MET 626  615  ?   ?   ?   A . n 
A 1 627  LEU 627  616  ?   ?   ?   A . n 
A 1 628  PHE 628  617  ?   ?   ?   A . n 
A 1 629  LEU 629  618  ?   ?   ?   A . n 
A 1 630  HIS 630  619  ?   ?   ?   A . n 
A 1 631  ASN 631  620  ?   ?   ?   A . n 
A 1 632  GLY 632  621  ?   ?   ?   A . n 
A 1 633  ALA 633  622  ?   ?   ?   A . n 
A 1 634  ILE 634  623  ?   ?   ?   A . n 
A 1 635  CYS 635  624  ?   ?   ?   A . n 
A 1 636  SER 636  625  ?   ?   ?   A . n 
A 1 637  HIS 637  626  ?   ?   ?   A . n 
A 1 638  GLY 638  627  ?   ?   ?   A . n 
A 1 639  ASN 639  628  ?   ?   ?   A . n 
A 1 640  LEU 640  629  ?   ?   ?   A . n 
A 1 641  LYS 641  630  ?   ?   ?   A . n 
A 1 642  SER 642  631  ?   ?   ?   A . n 
A 1 643  SER 643  632  ?   ?   ?   A . n 
A 1 644  ASN 644  633  ?   ?   ?   A . n 
A 1 645  CYS 645  634  ?   ?   ?   A . n 
A 1 646  VAL 646  635  ?   ?   ?   A . n 
A 1 647  VAL 647  636  ?   ?   ?   A . n 
A 1 648  ASP 648  637  ?   ?   ?   A . n 
A 1 649  GLY 649  638  ?   ?   ?   A . n 
A 1 650  ARG 650  639  ?   ?   ?   A . n 
A 1 651  PHE 651  640  ?   ?   ?   A . n 
A 1 652  VAL 652  641  ?   ?   ?   A . n 
A 1 653  LEU 653  642  ?   ?   ?   A . n 
A 1 654  LYS 654  643  ?   ?   ?   A . n 
A 1 655  ILE 655  644  ?   ?   ?   A . n 
A 1 656  THR 656  645  ?   ?   ?   A . n 
A 1 657  ASP 657  646  ?   ?   ?   A . n 
A 1 658  TYR 658  647  ?   ?   ?   A . n 
A 1 659  GLY 659  648  ?   ?   ?   A . n 
A 1 660  LEU 660  649  ?   ?   ?   A . n 
A 1 661  GLU 661  650  ?   ?   ?   A . n 
A 1 662  SER 662  651  ?   ?   ?   A . n 
A 1 663  PHE 663  652  ?   ?   ?   A . n 
A 1 664  ARG 664  653  ?   ?   ?   A . n 
A 1 665  ASP 665  654  ?   ?   ?   A . n 
A 1 666  LEU 666  655  ?   ?   ?   A . n 
A 1 667  ASP 667  656  ?   ?   ?   A . n 
A 1 668  PRO 668  657  ?   ?   ?   A . n 
A 1 669  GLU 669  658  ?   ?   ?   A . n 
A 1 670  GLN 670  659  ?   ?   ?   A . n 
A 1 671  GLY 671  660  ?   ?   ?   A . n 
A 1 672  HIS 672  661  ?   ?   ?   A . n 
A 1 673  THR 673  662  ?   ?   ?   A . n 
A 1 674  VAL 674  663  ?   ?   ?   A . n 
A 1 675  TYR 675  664  ?   ?   ?   A . n 
A 1 676  ALA 676  665  ?   ?   ?   A . n 
A 1 677  LYS 677  666  ?   ?   ?   A . n 
A 1 678  LYS 678  667  ?   ?   ?   A . n 
A 1 679  LEU 679  668  ?   ?   ?   A . n 
A 1 680  TRP 680  669  ?   ?   ?   A . n 
A 1 681  THR 681  670  ?   ?   ?   A . n 
A 1 682  ALA 682  671  ?   ?   ?   A . n 
A 1 683  PRO 683  672  ?   ?   ?   A . n 
A 1 684  GLU 684  673  ?   ?   ?   A . n 
A 1 685  LEU 685  674  ?   ?   ?   A . n 
A 1 686  LEU 686  675  ?   ?   ?   A . n 
A 1 687  ARG 687  676  ?   ?   ?   A . n 
A 1 688  MET 688  677  ?   ?   ?   A . n 
A 1 689  ALA 689  678  ?   ?   ?   A . n 
A 1 690  SER 690  679  ?   ?   ?   A . n 
A 1 691  PRO 691  680  ?   ?   ?   A . n 
A 1 692  PRO 692  681  ?   ?   ?   A . n 
A 1 693  VAL 693  682  ?   ?   ?   A . n 
A 1 694  ARG 694  683  ?   ?   ?   A . n 
A 1 695  GLY 695  684  ?   ?   ?   A . n 
A 1 696  SER 696  685  ?   ?   ?   A . n 
A 1 697  GLN 697  686  ?   ?   ?   A . n 
A 1 698  ALA 698  687  ?   ?   ?   A . n 
A 1 699  GLY 699  688  ?   ?   ?   A . n 
A 1 700  ASP 700  689  ?   ?   ?   A . n 
A 1 701  VAL 701  690  ?   ?   ?   A . n 
A 1 702  TYR 702  691  ?   ?   ?   A . n 
A 1 703  SER 703  692  ?   ?   ?   A . n 
A 1 704  PHE 704  693  ?   ?   ?   A . n 
A 1 705  GLY 705  694  ?   ?   ?   A . n 
A 1 706  ILE 706  695  ?   ?   ?   A . n 
A 1 707  ILE 707  696  ?   ?   ?   A . n 
A 1 708  LEU 708  697  ?   ?   ?   A . n 
A 1 709  GLN 709  698  ?   ?   ?   A . n 
A 1 710  GLU 710  699  ?   ?   ?   A . n 
A 1 711  ILE 711  700  ?   ?   ?   A . n 
A 1 712  ALA 712  701  ?   ?   ?   A . n 
A 1 713  LEU 713  702  ?   ?   ?   A . n 
A 1 714  ARG 714  703  ?   ?   ?   A . n 
A 1 715  SER 715  704  ?   ?   ?   A . n 
A 1 716  GLY 716  705  ?   ?   ?   A . n 
A 1 717  VAL 717  706  ?   ?   ?   A . n 
A 1 718  PHE 718  707  ?   ?   ?   A . n 
A 1 719  HIS 719  708  ?   ?   ?   A . n 
A 1 720  VAL 720  709  ?   ?   ?   A . n 
A 1 721  GLU 721  710  ?   ?   ?   A . n 
A 1 722  GLY 722  711  ?   ?   ?   A . n 
A 1 723  LEU 723  712  ?   ?   ?   A . n 
A 1 724  ASP 724  713  ?   ?   ?   A . n 
A 1 725  LEU 725  714  ?   ?   ?   A . n 
A 1 726  SER 726  715  ?   ?   ?   A . n 
A 1 727  PRO 727  716  ?   ?   ?   A . n 
A 1 728  LYS 728  717  ?   ?   ?   A . n 
A 1 729  GLU 729  718  ?   ?   ?   A . n 
A 1 730  ILE 730  719  ?   ?   ?   A . n 
A 1 731  ILE 731  720  ?   ?   ?   A . n 
A 1 732  GLU 732  721  ?   ?   ?   A . n 
A 1 733  ARG 733  722  ?   ?   ?   A . n 
A 1 734  VAL 734  723  ?   ?   ?   A . n 
A 1 735  THR 735  724  ?   ?   ?   A . n 
A 1 736  ARG 736  725  ?   ?   ?   A . n 
A 1 737  GLY 737  726  ?   ?   ?   A . n 
A 1 738  GLU 738  727  ?   ?   ?   A . n 
A 1 739  GLN 739  728  ?   ?   ?   A . n 
A 1 740  PRO 740  729  ?   ?   ?   A . n 
A 1 741  PRO 741  730  ?   ?   ?   A . n 
A 1 742  PHE 742  731  ?   ?   ?   A . n 
A 1 743  ARG 743  732  ?   ?   ?   A . n 
A 1 744  PRO 744  733  ?   ?   ?   A . n 
A 1 745  SER 745  734  ?   ?   ?   A . n 
A 1 746  LEU 746  735  ?   ?   ?   A . n 
A 1 747  ALA 747  736  ?   ?   ?   A . n 
A 1 748  LEU 748  737  ?   ?   ?   A . n 
A 1 749  GLN 749  738  ?   ?   ?   A . n 
A 1 750  SER 750  739  ?   ?   ?   A . n 
A 1 751  HIS 751  740  ?   ?   ?   A . n 
A 1 752  LEU 752  741  ?   ?   ?   A . n 
A 1 753  GLU 753  742  ?   ?   ?   A . n 
A 1 754  GLU 754  743  ?   ?   ?   A . n 
A 1 755  LEU 755  744  ?   ?   ?   A . n 
A 1 756  GLY 756  745  ?   ?   ?   A . n 
A 1 757  LEU 757  746  ?   ?   ?   A . n 
A 1 758  LEU 758  747  ?   ?   ?   A . n 
A 1 759  MET 759  748  ?   ?   ?   A . n 
A 1 760  GLN 760  749  ?   ?   ?   A . n 
A 1 761  ARG 761  750  ?   ?   ?   A . n 
A 1 762  CYS 762  751  ?   ?   ?   A . n 
A 1 763  TRP 763  752  ?   ?   ?   A . n 
A 1 764  ALA 764  753  ?   ?   ?   A . n 
A 1 765  GLU 765  754  ?   ?   ?   A . n 
A 1 766  ASP 766  755  ?   ?   ?   A . n 
A 1 767  PRO 767  756  ?   ?   ?   A . n 
A 1 768  GLN 768  757  ?   ?   ?   A . n 
A 1 769  GLU 769  758  ?   ?   ?   A . n 
A 1 770  ARG 770  759  ?   ?   ?   A . n 
A 1 771  PRO 771  760  ?   ?   ?   A . n 
A 1 772  PRO 772  761  ?   ?   ?   A . n 
A 1 773  PHE 773  762  ?   ?   ?   A . n 
A 1 774  GLN 774  763  ?   ?   ?   A . n 
A 1 775  GLN 775  764  ?   ?   ?   A . n 
A 1 776  ILE 776  765  ?   ?   ?   A . n 
A 1 777  ARG 777  766  ?   ?   ?   A . n 
A 1 778  LEU 778  767  ?   ?   ?   A . n 
A 1 779  THR 779  768  ?   ?   ?   A . n 
A 1 780  LEU 780  769  ?   ?   ?   A . n 
A 1 781  ARG 781  770  ?   ?   ?   A . n 
A 1 782  LYS 782  771  ?   ?   ?   A . n 
A 1 783  PHE 783  772  ?   ?   ?   A . n 
A 1 784  ASN 784  773  ?   ?   ?   A . n 
A 1 785  ARG 785  774  ?   ?   ?   A . n 
A 1 786  GLU 786  775  ?   ?   ?   A . n 
A 1 787  ASN 787  776  ?   ?   ?   A . n 
A 1 788  SER 788  777  ?   ?   ?   A . n 
A 1 789  SER 789  778  ?   ?   ?   A . n 
A 1 790  ASN 790  779  ?   ?   ?   A . n 
A 1 791  ILE 791  780  ?   ?   ?   A . n 
A 1 792  LEU 792  781  ?   ?   ?   A . n 
A 1 793  ASP 793  782  ?   ?   ?   A . n 
A 1 794  ASN 794  783  ?   ?   ?   A . n 
A 1 795  LEU 795  784  ?   ?   ?   A . n 
A 1 796  LEU 796  785  ?   ?   ?   A . n 
A 1 797  SER 797  786  ?   ?   ?   A . n 
A 1 798  ARG 798  787  ?   ?   ?   A . n 
A 1 799  MET 799  788  ?   ?   ?   A . n 
A 1 800  GLU 800  789  ?   ?   ?   A . n 
A 1 801  GLN 801  790  ?   ?   ?   A . n 
A 1 802  TYR 802  791  ?   ?   ?   A . n 
A 1 803  ALA 803  792  ?   ?   ?   A . n 
A 1 804  ASN 804  793  ?   ?   ?   A . n 
A 1 805  ASN 805  794  ?   ?   ?   A . n 
A 1 806  LEU 806  795  ?   ?   ?   A . n 
A 1 807  GLU 807  796  ?   ?   ?   A . n 
A 1 808  GLU 808  797  ?   ?   ?   A . n 
A 1 809  LEU 809  798  ?   ?   ?   A . n 
A 1 810  VAL 810  799  ?   ?   ?   A . n 
A 1 811  GLU 811  800  ?   ?   ?   A . n 
A 1 812  GLU 812  801  ?   ?   ?   A . n 
A 1 813  ARG 813  802  ?   ?   ?   A . n 
A 1 814  THR 814  803  ?   ?   ?   A . n 
A 1 815  GLN 815  804  ?   ?   ?   A . n 
A 1 816  ALA 816  805  ?   ?   ?   A . n 
A 1 817  TYR 817  806  ?   ?   ?   A . n 
A 1 818  LEU 818  807  ?   ?   ?   A . n 
A 1 819  GLU 819  808  ?   ?   ?   A . n 
A 1 820  GLU 820  809  ?   ?   ?   A . n 
A 1 821  LYS 821  810  ?   ?   ?   A . n 
A 1 822  ARG 822  811  ?   ?   ?   A . n 
A 1 823  LYS 823  812  ?   ?   ?   A . n 
A 1 824  ALA 824  813  ?   ?   ?   A . n 
A 1 825  GLU 825  814  ?   ?   ?   A . n 
A 1 826  ALA 826  815  ?   ?   ?   A . n 
A 1 827  LEU 827  816  ?   ?   ?   A . n 
A 1 828  LEU 828  817  ?   ?   ?   A . n 
A 1 829  TYR 829  818  ?   ?   ?   A . n 
A 1 830  GLN 830  819  ?   ?   ?   A . n 
A 1 831  ILE 831  820  ?   ?   ?   A . n 
A 1 832  LEU 832  821  ?   ?   ?   A . n 
A 1 833  PRO 833  822  ?   ?   ?   A . n 
A 1 834  HIS 834  823  ?   ?   ?   A . n 
A 1 835  SER 835  824  ?   ?   ?   A . n 
A 1 836  VAL 836  825  ?   ?   ?   A . n 
A 1 837  ALA 837  826  ?   ?   ?   A . n 
A 1 838  GLU 838  827  ?   ?   ?   A . n 
A 1 839  GLN 839  828  ?   ?   ?   A . n 
A 1 840  LEU 840  829  ?   ?   ?   A . n 
A 1 841  LYS 841  830  ?   ?   ?   A . n 
A 1 842  ARG 842  831  ?   ?   ?   A . n 
A 1 843  GLY 843  832  ?   ?   ?   A . n 
A 1 844  GLU 844  833  ?   ?   ?   A . n 
A 1 845  THR 845  834  ?   ?   ?   A . n 
A 1 846  VAL 846  835  ?   ?   ?   A . n 
A 1 847  GLN 847  836  ?   ?   ?   A . n 
A 1 848  ALA 848  837  ?   ?   ?   A . n 
A 1 849  GLU 849  838  ?   ?   ?   A . n 
A 1 850  ALA 850  839  ?   ?   ?   A . n 
A 1 851  PHE 851  840  ?   ?   ?   A . n 
A 1 852  ASP 852  841  ?   ?   ?   A . n 
A 1 853  SER 853  842  ?   ?   ?   A . n 
A 1 854  VAL 854  843  ?   ?   ?   A . n 
A 1 855  THR 855  844  ?   ?   ?   A . n 
A 1 856  ILE 856  845  ?   ?   ?   A . n 
A 1 857  TYR 857  846  ?   ?   ?   A . n 
A 1 858  PHE 858  847  ?   ?   ?   A . n 
A 1 859  SER 859  848  ?   ?   ?   A . n 
A 1 860  ASP 860  849  ?   ?   ?   A . n 
A 1 861  ILE 861  850  ?   ?   ?   A . n 
A 1 862  VAL 862  851  ?   ?   ?   A . n 
A 1 863  GLY 863  852  ?   ?   ?   A . n 
A 1 864  PHE 864  853  ?   ?   ?   A . n 
A 1 865  THR 865  854  ?   ?   ?   A . n 
A 1 866  ALA 866  855  ?   ?   ?   A . n 
A 1 867  LEU 867  856  ?   ?   ?   A . n 
A 1 868  SER 868  857  ?   ?   ?   A . n 
A 1 869  ALA 869  858  ?   ?   ?   A . n 
A 1 870  GLU 870  859  ?   ?   ?   A . n 
A 1 871  SER 871  860  ?   ?   ?   A . n 
A 1 872  THR 872  861  ?   ?   ?   A . n 
A 1 873  PRO 873  862  ?   ?   ?   A . n 
A 1 874  MET 874  863  ?   ?   ?   A . n 
A 1 875  GLN 875  864  ?   ?   ?   A . n 
A 1 876  VAL 876  865  ?   ?   ?   A . n 
A 1 877  VAL 877  866  ?   ?   ?   A . n 
A 1 878  THR 878  867  ?   ?   ?   A . n 
A 1 879  LEU 879  868  ?   ?   ?   A . n 
A 1 880  LEU 880  869  ?   ?   ?   A . n 
A 1 881  ASN 881  870  ?   ?   ?   A . n 
A 1 882  ASP 882  871  ?   ?   ?   A . n 
A 1 883  LEU 883  872  ?   ?   ?   A . n 
A 1 884  TYR 884  873  ?   ?   ?   A . n 
A 1 885  THR 885  874  ?   ?   ?   A . n 
A 1 886  CYS 886  875  ?   ?   ?   A . n 
A 1 887  PHE 887  876  ?   ?   ?   A . n 
A 1 888  ASP 888  877  ?   ?   ?   A . n 
A 1 889  ALA 889  878  ?   ?   ?   A . n 
A 1 890  VAL 890  879  ?   ?   ?   A . n 
A 1 891  ILE 891  880  ?   ?   ?   A . n 
A 1 892  ASP 892  881  ?   ?   ?   A . n 
A 1 893  ASN 893  882  ?   ?   ?   A . n 
A 1 894  PHE 894  883  ?   ?   ?   A . n 
A 1 895  ASP 895  884  ?   ?   ?   A . n 
A 1 896  VAL 896  885  ?   ?   ?   A . n 
A 1 897  TYR 897  886  ?   ?   ?   A . n 
A 1 898  LYS 898  887  ?   ?   ?   A . n 
A 1 899  VAL 899  888  ?   ?   ?   A . n 
A 1 900  GLU 900  889  ?   ?   ?   A . n 
A 1 901  THR 901  890  ?   ?   ?   A . n 
A 1 902  ILE 902  891  ?   ?   ?   A . n 
A 1 903  GLY 903  892  ?   ?   ?   A . n 
A 1 904  ASP 904  893  ?   ?   ?   A . n 
A 1 905  ALA 905  894  ?   ?   ?   A . n 
A 1 906  TYR 906  895  ?   ?   ?   A . n 
A 1 907  MET 907  896  ?   ?   ?   A . n 
A 1 908  VAL 908  897  ?   ?   ?   A . n 
A 1 909  VAL 909  898  ?   ?   ?   A . n 
A 1 910  SER 910  899  ?   ?   ?   A . n 
A 1 911  GLY 911  900  ?   ?   ?   A . n 
A 1 912  LEU 912  901  ?   ?   ?   A . n 
A 1 913  PRO 913  902  ?   ?   ?   A . n 
A 1 914  VAL 914  903  ?   ?   ?   A . n 
A 1 915  ARG 915  904  ?   ?   ?   A . n 
A 1 916  ASN 916  905  ?   ?   ?   A . n 
A 1 917  GLY 917  906  ?   ?   ?   A . n 
A 1 918  ARG 918  907  ?   ?   ?   A . n 
A 1 919  LEU 919  908  ?   ?   ?   A . n 
A 1 920  HIS 920  909  ?   ?   ?   A . n 
A 1 921  ALA 921  910  ?   ?   ?   A . n 
A 1 922  CYS 922  911  ?   ?   ?   A . n 
A 1 923  GLU 923  912  ?   ?   ?   A . n 
A 1 924  VAL 924  913  ?   ?   ?   A . n 
A 1 925  ALA 925  914  ?   ?   ?   A . n 
A 1 926  ARG 926  915  ?   ?   ?   A . n 
A 1 927  MET 927  916  ?   ?   ?   A . n 
A 1 928  ALA 928  917  ?   ?   ?   A . n 
A 1 929  LEU 929  918  ?   ?   ?   A . n 
A 1 930  ALA 930  919  ?   ?   ?   A . n 
A 1 931  LEU 931  920  ?   ?   ?   A . n 
A 1 932  LEU 932  921  ?   ?   ?   A . n 
A 1 933  ASP 933  922  ?   ?   ?   A . n 
A 1 934  ALA 934  923  ?   ?   ?   A . n 
A 1 935  VAL 935  924  ?   ?   ?   A . n 
A 1 936  ARG 936  925  ?   ?   ?   A . n 
A 1 937  SER 937  926  ?   ?   ?   A . n 
A 1 938  PHE 938  927  ?   ?   ?   A . n 
A 1 939  ARG 939  928  ?   ?   ?   A . n 
A 1 940  ILE 940  929  ?   ?   ?   A . n 
A 1 941  ARG 941  930  ?   ?   ?   A . n 
A 1 942  HIS 942  931  ?   ?   ?   A . n 
A 1 943  ARG 943  932  ?   ?   ?   A . n 
A 1 944  PRO 944  933  ?   ?   ?   A . n 
A 1 945  GLN 945  934  ?   ?   ?   A . n 
A 1 946  GLU 946  935  ?   ?   ?   A . n 
A 1 947  GLN 947  936  ?   ?   ?   A . n 
A 1 948  LEU 948  937  ?   ?   ?   A . n 
A 1 949  ARG 949  938  ?   ?   ?   A . n 
A 1 950  LEU 950  939  ?   ?   ?   A . n 
A 1 951  ARG 951  940  ?   ?   ?   A . n 
A 1 952  ILE 952  941  ?   ?   ?   A . n 
A 1 953  GLY 953  942  ?   ?   ?   A . n 
A 1 954  ILE 954  943  ?   ?   ?   A . n 
A 1 955  HIS 955  944  ?   ?   ?   A . n 
A 1 956  THR 956  945  ?   ?   ?   A . n 
A 1 957  GLY 957  946  ?   ?   ?   A . n 
A 1 958  PRO 958  947  ?   ?   ?   A . n 
A 1 959  VAL 959  948  ?   ?   ?   A . n 
A 1 960  CYS 960  949  ?   ?   ?   A . n 
A 1 961  ALA 961  950  ?   ?   ?   A . n 
A 1 962  GLY 962  951  ?   ?   ?   A . n 
A 1 963  VAL 963  952  ?   ?   ?   A . n 
A 1 964  VAL 964  953  ?   ?   ?   A . n 
A 1 965  GLY 965  954  ?   ?   ?   A . n 
A 1 966  LEU 966  955  ?   ?   ?   A . n 
A 1 967  LYS 967  956  ?   ?   ?   A . n 
A 1 968  MET 968  957  ?   ?   ?   A . n 
A 1 969  PRO 969  958  ?   ?   ?   A . n 
A 1 970  ARG 970  959  ?   ?   ?   A . n 
A 1 971  TYR 971  960  ?   ?   ?   A . n 
A 1 972  CYS 972  961  ?   ?   ?   A . n 
A 1 973  LEU 973  962  ?   ?   ?   A . n 
A 1 974  PHE 974  963  ?   ?   ?   A . n 
A 1 975  GLY 975  964  ?   ?   ?   A . n 
A 1 976  ASP 976  965  ?   ?   ?   A . n 
A 1 977  THR 977  966  ?   ?   ?   A . n 
A 1 978  VAL 978  967  ?   ?   ?   A . n 
A 1 979  ASN 979  968  ?   ?   ?   A . n 
A 1 980  THR 980  969  ?   ?   ?   A . n 
A 1 981  ALA 981  970  ?   ?   ?   A . n 
A 1 982  SER 982  971  ?   ?   ?   A . n 
A 1 983  ARG 983  972  ?   ?   ?   A . n 
A 1 984  MET 984  973  ?   ?   ?   A . n 
A 1 985  GLU 985  974  ?   ?   ?   A . n 
A 1 986  SER 986  975  ?   ?   ?   A . n 
A 1 987  ASN 987  976  ?   ?   ?   A . n 
A 1 988  GLY 988  977  ?   ?   ?   A . n 
A 1 989  GLU 989  978  ?   ?   ?   A . n 
A 1 990  ALA 990  979  ?   ?   ?   A . n 
A 1 991  LEU 991  980  ?   ?   ?   A . n 
A 1 992  LYS 992  981  ?   ?   ?   A . n 
A 1 993  ILE 993  982  ?   ?   ?   A . n 
A 1 994  HIS 994  983  ?   ?   ?   A . n 
A 1 995  LEU 995  984  ?   ?   ?   A . n 
A 1 996  SER 996  985  ?   ?   ?   A . n 
A 1 997  SER 997  986  ?   ?   ?   A . n 
A 1 998  GLU 998  987  ?   ?   ?   A . n 
A 1 999  THR 999  988  ?   ?   ?   A . n 
A 1 1000 LYS 1000 989  ?   ?   ?   A . n 
A 1 1001 ALA 1001 990  ?   ?   ?   A . n 
A 1 1002 VAL 1002 991  ?   ?   ?   A . n 
A 1 1003 LEU 1003 992  ?   ?   ?   A . n 
A 1 1004 GLU 1004 993  ?   ?   ?   A . n 
A 1 1005 GLU 1005 994  ?   ?   ?   A . n 
A 1 1006 PHE 1006 995  ?   ?   ?   A . n 
A 1 1007 GLY 1007 996  ?   ?   ?   A . n 
A 1 1008 GLY 1008 997  ?   ?   ?   A . n 
A 1 1009 PHE 1009 998  ?   ?   ?   A . n 
A 1 1010 GLU 1010 999  ?   ?   ?   A . n 
A 1 1011 LEU 1011 1000 ?   ?   ?   A . n 
A 1 1012 GLU 1012 1001 ?   ?   ?   A . n 
A 1 1013 LEU 1013 1002 ?   ?   ?   A . n 
A 1 1014 ARG 1014 1003 ?   ?   ?   A . n 
A 1 1015 GLY 1015 1004 ?   ?   ?   A . n 
A 1 1016 ASP 1016 1005 ?   ?   ?   A . n 
A 1 1017 VAL 1017 1006 ?   ?   ?   A . n 
A 1 1018 GLU 1018 1007 ?   ?   ?   A . n 
A 1 1019 MET 1019 1008 ?   ?   ?   A . n 
A 1 1020 LYS 1020 1009 ?   ?   ?   A . n 
A 1 1021 GLY 1021 1010 ?   ?   ?   A . n 
A 1 1022 LYS 1022 1011 ?   ?   ?   A . n 
A 1 1023 GLY 1023 1012 ?   ?   ?   A . n 
A 1 1024 LYS 1024 1013 ?   ?   ?   A . n 
A 1 1025 VAL 1025 1014 ?   ?   ?   A . n 
A 1 1026 ARG 1026 1015 ?   ?   ?   A . n 
A 1 1027 THR 1027 1016 ?   ?   ?   A . n 
A 1 1028 TYR 1028 1017 ?   ?   ?   A . n 
A 1 1029 TRP 1029 1018 ?   ?   ?   A . n 
A 1 1030 LEU 1030 1019 ?   ?   ?   A . n 
A 1 1031 LEU 1031 1020 ?   ?   ?   A . n 
A 1 1032 GLY 1032 1021 ?   ?   ?   A . n 
A 1 1033 GLU 1033 1022 ?   ?   ?   A . n 
A 1 1034 ARG 1034 1023 ?   ?   ?   A . n 
A 1 1035 GLY 1035 1024 ?   ?   ?   A . n 
A 1 1036 SER 1036 1025 ?   ?   ?   A . n 
A 1 1037 SER 1037 1026 ?   ?   ?   A . n 
A 1 1038 THR 1038 1027 ?   ?   ?   A . n 
A 1 1039 ARG 1039 1028 ?   ?   ?   A . n 
A 1 1040 GLY 1040 1029 ?   ?   ?   A . n 
B 1 1    ASP 1    -10  ?   ?   ?   B . n 
B 1 2    TYR 2    -9   ?   ?   ?   B . n 
B 1 3    LYS 3    -8   ?   ?   ?   B . n 
B 1 4    ASP 4    -7   ?   ?   ?   B . n 
B 1 5    ASP 5    -6   ?   ?   ?   B . n 
B 1 6    ASP 6    -5   ?   ?   ?   B . n 
B 1 7    ASP 7    -4   ?   ?   ?   B . n 
B 1 8    LYS 8    -3   ?   ?   ?   B . n 
B 1 9    ALA 9    -2   ?   ?   ?   B . n 
B 1 10   ALA 10   -1   ?   ?   ?   B . n 
B 1 11   ALA 11   0    ?   ?   ?   B . n 
B 1 12   GLY 12   1    1   GLY GLY B . n 
B 1 13   ASN 13   2    2   ASN ASN B . n 
B 1 14   LEU 14   3    3   LEU LEU B . n 
B 1 15   THR 15   4    4   THR THR B . n 
B 1 16   VAL 16   5    5   VAL VAL B . n 
B 1 17   ALA 17   6    6   ALA ALA B . n 
B 1 18   VAL 18   7    7   VAL VAL B . n 
B 1 19   VAL 19   8    8   VAL VAL B . n 
B 1 20   LEU 20   9    9   LEU LEU B . n 
B 1 21   PRO 21   10   10  PRO PRO B . n 
B 1 22   LEU 22   11   11  LEU LEU B . n 
B 1 23   ALA 23   12   12  ALA ALA B . n 
B 1 24   ASN 24   13   13  ASN ASN B . n 
B 1 25   THR 25   14   14  THR THR B . n 
B 1 26   SER 26   15   15  SER SER B . n 
B 1 27   TYR 27   16   16  TYR TYR B . n 
B 1 28   PRO 28   17   17  PRO PRO B . n 
B 1 29   TRP 29   18   18  TRP TRP B . n 
B 1 30   SER 30   19   19  SER SER B . n 
B 1 31   TRP 31   20   20  TRP TRP B . n 
B 1 32   ALA 32   21   21  ALA ALA B . n 
B 1 33   ARG 33   22   22  ARG ARG B . n 
B 1 34   VAL 34   23   23  VAL VAL B . n 
B 1 35   GLY 35   24   24  GLY GLY B . n 
B 1 36   PRO 36   25   25  PRO PRO B . n 
B 1 37   ALA 37   26   26  ALA ALA B . n 
B 1 38   VAL 38   27   27  VAL VAL B . n 
B 1 39   GLU 39   28   28  GLU GLU B . n 
B 1 40   LEU 40   29   29  LEU LEU B . n 
B 1 41   ALA 41   30   30  ALA ALA B . n 
B 1 42   LEU 42   31   31  LEU LEU B . n 
B 1 43   ALA 43   32   32  ALA ALA B . n 
B 1 44   GLN 44   33   33  GLN GLN B . n 
B 1 45   VAL 45   34   34  VAL VAL B . n 
B 1 46   LYS 46   35   35  LYS LYS B . n 
B 1 47   ALA 47   36   36  ALA ALA B . n 
B 1 48   ARG 48   37   37  ARG ARG B . n 
B 1 49   PRO 49   38   38  PRO PRO B . n 
B 1 50   ASP 50   39   39  ASP ASP B . n 
B 1 51   LEU 51   40   40  LEU LEU B . n 
B 1 52   LEU 52   41   41  LEU LEU B . n 
B 1 53   PRO 53   42   42  PRO PRO B . n 
B 1 54   GLY 54   43   43  GLY GLY B . n 
B 1 55   TRP 55   44   44  TRP TRP B . n 
B 1 56   THR 56   45   45  THR THR B . n 
B 1 57   VAL 57   46   46  VAL VAL B . n 
B 1 58   ARG 58   47   47  ARG ARG B . n 
B 1 59   THR 59   48   48  THR THR B . n 
B 1 60   VAL 60   49   49  VAL VAL B . n 
B 1 61   LEU 61   50   50  LEU LEU B . n 
B 1 62   GLY 62   51   51  GLY GLY B . n 
B 1 63   SER 63   52   52  SER SER B . n 
B 1 64   SER 64   53   53  SER SER B . n 
B 1 65   GLU 65   54   54  GLU GLU B . n 
B 1 66   ASN 66   55   55  ASN ASN B . n 
B 1 67   ALA 67   56   56  ALA ALA B . n 
B 1 68   LEU 68   57   57  LEU LEU B . n 
B 1 69   GLY 69   58   58  GLY GLY B . n 
B 1 70   VAL 70   59   59  VAL VAL B . n 
B 1 71   CYS 71   60   60  CYS CYS B . n 
B 1 72   SER 72   61   61  SER SER B . n 
B 1 73   ASP 73   62   62  ASP ASP B . n 
B 1 74   THR 74   63   63  THR THR B . n 
B 1 75   ALA 75   64   64  ALA ALA B . n 
B 1 76   ALA 76   65   65  ALA ALA B . n 
B 1 77   PRO 77   66   66  PRO PRO B . n 
B 1 78   LEU 78   67   67  LEU LEU B . n 
B 1 79   ALA 79   68   68  ALA ALA B . n 
B 1 80   ALA 80   69   69  ALA ALA B . n 
B 1 81   VAL 81   70   70  VAL VAL B . n 
B 1 82   ASP 82   71   71  ASP ASP B . n 
B 1 83   LEU 83   72   72  LEU LEU B . n 
B 1 84   LYS 84   73   73  LYS LYS B . n 
B 1 85   TRP 85   74   74  TRP TRP B . n 
B 1 86   GLU 86   75   75  GLU GLU B . n 
B 1 87   HIS 87   76   76  HIS HIS B . n 
B 1 88   ASN 88   77   77  ASN ASN B . n 
B 1 89   PRO 89   78   78  PRO PRO B . n 
B 1 90   ALA 90   79   79  ALA ALA B . n 
B 1 91   VAL 91   80   80  VAL VAL B . n 
B 1 92   PHE 92   81   81  PHE PHE B . n 
B 1 93   LEU 93   82   82  LEU LEU B . n 
B 1 94   GLY 94   83   83  GLY GLY B . n 
B 1 95   PRO 95   84   84  PRO PRO B . n 
B 1 96   GLY 96   85   85  GLY GLY B . n 
B 1 97   CYS 97   86   86  CYS CYS B . n 
B 1 98   VAL 98   87   87  VAL VAL B . n 
B 1 99   TYR 99   88   88  TYR TYR B . n 
B 1 100  ALA 100  89   89  ALA ALA B . n 
B 1 101  ALA 101  90   90  ALA ALA B . n 
B 1 102  ALA 102  91   91  ALA ALA B . n 
B 1 103  PRO 103  92   92  PRO PRO B . n 
B 1 104  VAL 104  93   93  VAL VAL B . n 
B 1 105  GLY 105  94   94  GLY GLY B . n 
B 1 106  ARG 106  95   95  ARG ARG B . n 
B 1 107  PHE 107  96   96  PHE PHE B . n 
B 1 108  THR 108  97   97  THR THR B . n 
B 1 109  ALA 109  98   98  ALA ALA B . n 
B 1 110  HIS 110  99   99  HIS HIS B . n 
B 1 111  TRP 111  100  100 TRP TRP B . n 
B 1 112  ARG 112  101  101 ARG ARG B . n 
B 1 113  VAL 113  102  102 VAL VAL B . n 
B 1 114  PRO 114  103  103 PRO PRO B . n 
B 1 115  LEU 115  104  104 LEU LEU B . n 
B 1 116  LEU 116  105  105 LEU LEU B . n 
B 1 117  THR 117  106  106 THR THR B . n 
B 1 118  ALA 118  107  107 ALA ALA B . n 
B 1 119  GLY 119  108  108 GLY GLY B . n 
B 1 120  ALA 120  109  109 ALA ALA B . n 
B 1 121  PRO 121  110  110 PRO PRO B . n 
B 1 122  ALA 122  111  111 ALA ALA B . n 
B 1 123  LEU 123  112  112 LEU LEU B . n 
B 1 124  GLY 124  113  113 GLY GLY B . n 
B 1 125  PHE 125  114  114 PHE PHE B . n 
B 1 126  GLY 126  115  115 GLY GLY B . n 
B 1 127  VAL 127  116  116 VAL VAL B . n 
B 1 128  LYS 128  117  117 LYS LYS B . n 
B 1 129  ASP 129  118  118 ASP ASP B . n 
B 1 130  GLU 130  119  119 GLU GLU B . n 
B 1 131  TYR 131  120  120 TYR TYR B . n 
B 1 132  ALA 132  121  121 ALA ALA B . n 
B 1 133  LEU 133  122  122 LEU LEU B . n 
B 1 134  THR 134  123  123 THR THR B . n 
B 1 135  THR 135  124  124 THR THR B . n 
B 1 136  ARG 136  125  125 ARG ARG B . n 
B 1 137  ALA 137  126  126 ALA ALA B . n 
B 1 138  GLY 138  127  127 GLY GLY B . n 
B 1 139  PRO 139  128  128 PRO PRO B . n 
B 1 140  SER 140  129  129 SER SER B . n 
B 1 141  TYR 141  130  130 TYR TYR B . n 
B 1 142  ALA 142  131  131 ALA ALA B . n 
B 1 143  LYS 143  132  132 LYS LYS B . n 
B 1 144  LEU 144  133  133 LEU LEU B . n 
B 1 145  GLY 145  134  134 GLY GLY B . n 
B 1 146  ASP 146  135  135 ASP ASP B . n 
B 1 147  PHE 147  136  136 PHE PHE B . n 
B 1 148  VAL 148  137  137 VAL VAL B . n 
B 1 149  ALA 149  138  138 ALA ALA B . n 
B 1 150  ALA 150  139  139 ALA ALA B . n 
B 1 151  LEU 151  140  140 LEU LEU B . n 
B 1 152  HIS 152  141  141 HIS HIS B . n 
B 1 153  ARG 153  142  142 ARG ARG B . n 
B 1 154  ARG 154  143  143 ARG ARG B . n 
B 1 155  LEU 155  144  144 LEU LEU B . n 
B 1 156  GLY 156  145  145 GLY GLY B . n 
B 1 157  TRP 157  146  146 TRP TRP B . n 
B 1 158  GLU 158  147  147 GLU GLU B . n 
B 1 159  ARG 159  148  148 ARG ARG B . n 
B 1 160  GLN 160  149  149 GLN GLN B . n 
B 1 161  ALA 161  150  150 ALA ALA B . n 
B 1 162  LEU 162  151  151 LEU LEU B . n 
B 1 163  MET 163  152  152 MET MET B . n 
B 1 164  LEU 164  153  153 LEU LEU B . n 
B 1 165  TYR 165  154  154 TYR TYR B . n 
B 1 166  ALA 166  155  155 ALA ALA B . n 
B 1 167  TYR 167  156  156 TYR TYR B . n 
B 1 168  ARG 168  157  157 ARG ARG B . n 
B 1 169  PRO 169  158  158 PRO PRO B . n 
B 1 170  GLY 170  159  159 GLY GLY B . n 
B 1 171  ASP 171  160  160 ASP ASP B . n 
B 1 172  GLU 172  161  161 GLU GLU B . n 
B 1 173  GLU 173  162  162 GLU GLU B . n 
B 1 174  HIS 174  163  163 HIS HIS B . n 
B 1 175  CYS 175  164  164 CYS CYS B . n 
B 1 176  PHE 176  165  165 PHE PHE B . n 
B 1 177  PHE 177  166  166 PHE PHE B . n 
B 1 178  LEU 178  167  167 LEU LEU B . n 
B 1 179  VAL 179  168  168 VAL VAL B . n 
B 1 180  GLU 180  169  169 GLU GLU B . n 
B 1 181  GLY 181  170  170 GLY GLY B . n 
B 1 182  LEU 182  171  171 LEU LEU B . n 
B 1 183  PHE 183  172  172 PHE PHE B . n 
B 1 184  MET 184  173  173 MET MET B . n 
B 1 185  ARG 185  174  174 ARG ARG B . n 
B 1 186  VAL 186  175  175 VAL VAL B . n 
B 1 187  ARG 187  176  176 ARG ARG B . n 
B 1 188  ASP 188  177  177 ASP ASP B . n 
B 1 189  ARG 189  178  178 ARG ARG B . n 
B 1 190  LEU 190  179  179 LEU LEU B . n 
B 1 191  ASN 191  180  180 ASN ASN B . n 
B 1 192  ILE 192  181  181 ILE ILE B . n 
B 1 193  THR 193  182  182 THR THR B . n 
B 1 194  VAL 194  183  183 VAL VAL B . n 
B 1 195  ASP 195  184  184 ASP ASP B . n 
B 1 196  HIS 196  185  185 HIS HIS B . n 
B 1 197  LEU 197  186  186 LEU LEU B . n 
B 1 198  GLU 198  187  187 GLU GLU B . n 
B 1 199  PHE 199  188  188 PHE PHE B . n 
B 1 200  ALA 200  189  189 ALA ALA B . n 
B 1 201  GLU 201  190  190 GLU GLU B . n 
B 1 202  ASP 202  191  191 ASP ASP B . n 
B 1 203  ASP 203  192  192 ASP ASP B . n 
B 1 204  LEU 204  193  193 LEU LEU B . n 
B 1 205  SER 205  194  194 SER SER B . n 
B 1 206  HIS 206  195  195 HIS HIS B . n 
B 1 207  TYR 207  196  196 TYR TYR B . n 
B 1 208  THR 208  197  197 THR THR B . n 
B 1 209  ARG 209  198  198 ARG ARG B . n 
B 1 210  LEU 210  199  199 LEU LEU B . n 
B 1 211  LEU 211  200  200 LEU LEU B . n 
B 1 212  ARG 212  201  201 ARG ARG B . n 
B 1 213  THR 213  202  202 THR THR B . n 
B 1 214  MET 214  203  203 MET MET B . n 
B 1 215  PRO 215  204  204 PRO PRO B . n 
B 1 216  ARG 216  205  205 ARG ARG B . n 
B 1 217  LYS 217  206  206 LYS LYS B . n 
B 1 218  GLY 218  207  207 GLY GLY B . n 
B 1 219  ARG 219  208  208 ARG ARG B . n 
B 1 220  VAL 220  209  209 VAL VAL B . n 
B 1 221  ILE 221  210  210 ILE ILE B . n 
B 1 222  TYR 222  211  211 TYR TYR B . n 
B 1 223  ILE 223  212  212 ILE ILE B . n 
B 1 224  CYS 224  213  213 CYS CYS B . n 
B 1 225  SER 225  214  214 SER SER B . n 
B 1 226  SER 226  215  215 SER SER B . n 
B 1 227  PRO 227  216  216 PRO PRO B . n 
B 1 228  ASP 228  217  217 ASP ASP B . n 
B 1 229  ALA 229  218  218 ALA ALA B . n 
B 1 230  PHE 230  219  219 PHE PHE B . n 
B 1 231  ARG 231  220  220 ARG ARG B . n 
B 1 232  THR 232  221  221 THR THR B . n 
B 1 233  LEU 233  222  222 LEU LEU B . n 
B 1 234  MET 234  223  223 MET MET B . n 
B 1 235  LEU 235  224  224 LEU LEU B . n 
B 1 236  LEU 236  225  225 LEU LEU B . n 
B 1 237  ALA 237  226  226 ALA ALA B . n 
B 1 238  LEU 238  227  227 LEU LEU B . n 
B 1 239  GLU 239  228  228 GLU GLU B . n 
B 1 240  ALA 240  229  229 ALA ALA B . n 
B 1 241  GLY 241  230  230 GLY GLY B . n 
B 1 242  LEU 242  231  231 LEU LEU B . n 
B 1 243  CYS 243  232  232 CYS CYS B . n 
B 1 244  GLY 244  233  233 GLY GLY B . n 
B 1 245  GLU 245  234  234 GLU GLU B . n 
B 1 246  ASP 246  235  235 ASP ASP B . n 
B 1 247  TYR 247  236  236 TYR TYR B . n 
B 1 248  VAL 248  237  237 VAL VAL B . n 
B 1 249  PHE 249  238  238 PHE PHE B . n 
B 1 250  PHE 250  239  239 PHE PHE B . n 
B 1 251  HIS 251  240  240 HIS HIS B . n 
B 1 252  LEU 252  241  241 LEU LEU B . n 
B 1 253  ASP 253  242  242 ASP ASP B . n 
B 1 254  ILE 254  243  243 ILE ILE B . n 
B 1 255  PHE 255  244  244 PHE PHE B . n 
B 1 256  GLY 256  245  245 GLY GLY B . n 
B 1 257  GLN 257  246  246 GLN GLN B . n 
B 1 258  SER 258  247  247 SER SER B . n 
B 1 259  LEU 259  248  248 LEU LEU B . n 
B 1 260  GLN 260  249  249 GLN GLN B . n 
B 1 261  GLY 261  250  250 GLY GLY B . n 
B 1 262  GLY 262  251  251 GLY GLY B . n 
B 1 263  GLN 263  252  252 GLN GLN B . n 
B 1 264  GLY 264  253  253 GLY GLY B . n 
B 1 265  PRO 265  254  254 PRO PRO B . n 
B 1 266  ALA 266  255  255 ALA ALA B . n 
B 1 267  PRO 267  256  256 PRO PRO B . n 
B 1 268  ARG 268  257  257 ARG ARG B . n 
B 1 269  ARG 269  258  258 ARG ARG B . n 
B 1 270  PRO 270  259  259 PRO PRO B . n 
B 1 271  TRP 271  260  260 TRP TRP B . n 
B 1 272  GLU 272  261  261 GLU GLU B . n 
B 1 273  ARG 273  262  262 ARG ARG B . n 
B 1 274  GLY 274  263  263 GLY GLY B . n 
B 1 275  ASP 275  264  264 ASP ASP B . n 
B 1 276  GLY 276  265  265 GLY GLY B . n 
B 1 277  GLN 277  266  266 GLN GLN B . n 
B 1 278  ASP 278  267  267 ASP ASP B . n 
B 1 279  VAL 279  268  268 VAL VAL B . n 
B 1 280  SER 280  269  269 SER SER B . n 
B 1 281  ALA 281  270  270 ALA ALA B . n 
B 1 282  ARG 282  271  271 ARG ARG B . n 
B 1 283  GLN 283  272  272 GLN GLN B . n 
B 1 284  ALA 284  273  273 ALA ALA B . n 
B 1 285  PHE 285  274  274 PHE PHE B . n 
B 1 286  GLN 286  275  275 GLN GLN B . n 
B 1 287  ALA 287  276  276 ALA ALA B . n 
B 1 288  ALA 288  277  277 ALA ALA B . n 
B 1 289  LYS 289  278  278 LYS LYS B . n 
B 1 290  ILE 290  279  279 ILE ILE B . n 
B 1 291  ILE 291  280  280 ILE ILE B . n 
B 1 292  THR 292  281  281 THR THR B . n 
B 1 293  TYR 293  282  282 TYR TYR B . n 
B 1 294  LYS 294  283  283 LYS LYS B . n 
B 1 295  ASP 295  284  284 ASP ASP B . n 
B 1 296  PRO 296  285  285 PRO PRO B . n 
B 1 297  ASP 297  286  286 ASP ASP B . n 
B 1 298  ASN 298  287  287 ASN ASN B . n 
B 1 299  PRO 299  288  288 PRO PRO B . n 
B 1 300  GLU 300  289  289 GLU GLU B . n 
B 1 301  TYR 301  290  290 TYR TYR B . n 
B 1 302  LEU 302  291  291 LEU LEU B . n 
B 1 303  GLU 303  292  292 GLU GLU B . n 
B 1 304  PHE 304  293  293 PHE PHE B . n 
B 1 305  LEU 305  294  294 LEU LEU B . n 
B 1 306  LYS 306  295  295 LYS LYS B . n 
B 1 307  GLN 307  296  296 GLN GLN B . n 
B 1 308  LEU 308  297  297 LEU LEU B . n 
B 1 309  LYS 309  298  298 LYS LYS B . n 
B 1 310  HIS 310  299  299 HIS HIS B . n 
B 1 311  LEU 311  300  300 LEU LEU B . n 
B 1 312  ALA 312  301  301 ALA ALA B . n 
B 1 313  TYR 313  302  302 TYR TYR B . n 
B 1 314  GLU 314  303  303 GLU GLU B . n 
B 1 315  GLN 315  304  304 GLN GLN B . n 
B 1 316  PHE 316  305  305 PHE PHE B . n 
B 1 317  ASN 317  306  306 ASN ASN B . n 
B 1 318  PHE 318  307  307 PHE PHE B . n 
B 1 319  THR 319  308  308 THR THR B . n 
B 1 320  MET 320  309  309 MET MET B . n 
B 1 321  GLU 321  310  310 GLU GLU B . n 
B 1 322  ASP 322  311  311 ASP ASP B . n 
B 1 323  GLY 323  312  312 GLY GLY B . n 
B 1 324  LEU 324  313  313 LEU LEU B . n 
B 1 325  VAL 325  314  314 VAL VAL B . n 
B 1 326  ASN 326  315  315 ASN ASN B . n 
B 1 327  THR 327  316  316 THR THR B . n 
B 1 328  ILE 328  317  317 ILE ILE B . n 
B 1 329  PRO 329  318  318 PRO PRO B . n 
B 1 330  ALA 330  319  319 ALA ALA B . n 
B 1 331  SER 331  320  320 SER SER B . n 
B 1 332  PHE 332  321  321 PHE PHE B . n 
B 1 333  HIS 333  322  322 HIS HIS B . n 
B 1 334  ASP 334  323  323 ASP ASP B . n 
B 1 335  GLY 335  324  324 GLY GLY B . n 
B 1 336  LEU 336  325  325 LEU LEU B . n 
B 1 337  LEU 337  326  326 LEU LEU B . n 
B 1 338  LEU 338  327  327 LEU LEU B . n 
B 1 339  TYR 339  328  328 TYR TYR B . n 
B 1 340  ILE 340  329  329 ILE ILE B . n 
B 1 341  GLN 341  330  330 GLN GLN B . n 
B 1 342  ALA 342  331  331 ALA ALA B . n 
B 1 343  VAL 343  332  332 VAL VAL B . n 
B 1 344  THR 344  333  333 THR THR B . n 
B 1 345  GLU 345  334  334 GLU GLU B . n 
B 1 346  THR 346  335  335 THR THR B . n 
B 1 347  LEU 347  336  336 LEU LEU B . n 
B 1 348  ALA 348  337  337 ALA ALA B . n 
B 1 349  HIS 349  338  338 HIS HIS B . n 
B 1 350  GLY 350  339  339 GLY GLY B . n 
B 1 351  GLY 351  340  340 GLY GLY B . n 
B 1 352  THR 352  341  341 THR THR B . n 
B 1 353  VAL 353  342  342 VAL VAL B . n 
B 1 354  THR 354  343  343 THR THR B . n 
B 1 355  ASP 355  344  344 ASP ASP B . n 
B 1 356  GLY 356  345  345 GLY GLY B . n 
B 1 357  GLU 357  346  346 GLU GLU B . n 
B 1 358  ASN 358  347  347 ASN ASN B . n 
B 1 359  ILE 359  348  348 ILE ILE B . n 
B 1 360  THR 360  349  349 THR THR B . n 
B 1 361  GLN 361  350  350 GLN GLN B . n 
B 1 362  ARG 362  351  351 ARG ARG B . n 
B 1 363  MET 363  352  352 MET MET B . n 
B 1 364  TRP 364  353  353 TRP TRP B . n 
B 1 365  ASN 365  354  354 ASN ASN B . n 
B 1 366  ARG 366  355  355 ARG ARG B . n 
B 1 367  SER 367  356  356 SER SER B . n 
B 1 368  PHE 368  357  357 PHE PHE B . n 
B 1 369  GLN 369  358  358 GLN GLN B . n 
B 1 370  GLY 370  359  359 GLY GLY B . n 
B 1 371  VAL 371  360  360 VAL VAL B . n 
B 1 372  THR 372  361  361 THR THR B . n 
B 1 373  GLY 373  362  362 GLY GLY B . n 
B 1 374  TYR 374  363  363 TYR TYR B . n 
B 1 375  LEU 375  364  364 LEU LEU B . n 
B 1 376  LYS 376  365  365 LYS LYS B . n 
B 1 377  ILE 377  366  366 ILE ILE B . n 
B 1 378  ASP 378  367  367 ASP ASP B . n 
B 1 379  SER 379  368  368 SER SER B . n 
B 1 380  SER 380  369  369 SER SER B . n 
B 1 381  GLY 381  370  370 GLY GLY B . n 
B 1 382  ASP 382  371  371 ASP ASP B . n 
B 1 383  ARG 383  372  372 ARG ARG B . n 
B 1 384  GLU 384  373  373 GLU GLU B . n 
B 1 385  THR 385  374  374 THR THR B . n 
B 1 386  ASP 386  375  375 ASP ASP B . n 
B 1 387  PHE 387  376  376 PHE PHE B . n 
B 1 388  SER 388  377  377 SER SER B . n 
B 1 389  LEU 389  378  378 LEU LEU B . n 
B 1 390  TRP 390  379  379 TRP TRP B . n 
B 1 391  ASP 391  380  380 ASP ASP B . n 
B 1 392  MET 392  381  381 MET MET B . n 
B 1 393  ASP 393  382  382 ASP ASP B . n 
B 1 394  PRO 394  383  383 PRO PRO B . n 
B 1 395  GLU 395  384  384 GLU GLU B . n 
B 1 396  ASN 396  385  385 ASN ASN B . n 
B 1 397  GLY 397  386  386 GLY GLY B . n 
B 1 398  ALA 398  387  387 ALA ALA B . n 
B 1 399  PHE 399  388  388 PHE PHE B . n 
B 1 400  ARG 400  389  389 ARG ARG B . n 
B 1 401  VAL 401  390  390 VAL VAL B . n 
B 1 402  VAL 402  391  391 VAL VAL B . n 
B 1 403  LEU 403  392  392 LEU LEU B . n 
B 1 404  ASN 404  393  393 ASN ASN B . n 
B 1 405  TYR 405  394  394 TYR TYR B . n 
B 1 406  ASN 406  395  395 ASN ASN B . n 
B 1 407  GLY 407  396  396 GLY GLY B . n 
B 1 408  THR 408  397  397 THR THR B . n 
B 1 409  SER 409  398  398 SER SER B . n 
B 1 410  GLN 410  399  399 GLN GLN B . n 
B 1 411  GLU 411  400  400 GLU GLU B . n 
B 1 412  LEU 412  401  401 LEU LEU B . n 
B 1 413  VAL 413  402  402 VAL VAL B . n 
B 1 414  ALA 414  403  403 ALA ALA B . n 
B 1 415  VAL 415  404  404 VAL VAL B . n 
B 1 416  SER 416  405  405 SER SER B . n 
B 1 417  GLY 417  406  406 GLY GLY B . n 
B 1 418  ARG 418  407  407 ARG ARG B . n 
B 1 419  LYS 419  408  408 LYS LYS B . n 
B 1 420  LEU 420  409  409 LEU LEU B . n 
B 1 421  ASN 421  410  410 ASN ASN B . n 
B 1 422  TRP 422  411  411 TRP TRP B . n 
B 1 423  PRO 423  412  412 PRO PRO B . n 
B 1 424  LEU 424  413  413 LEU LEU B . n 
B 1 425  GLY 425  414  414 GLY GLY B . n 
B 1 426  TYR 426  415  415 TYR TYR B . n 
B 1 427  PRO 427  416  416 PRO PRO B . n 
B 1 428  PRO 428  417  417 PRO PRO B . n 
B 1 429  PRO 429  418  418 PRO PRO B . n 
B 1 430  ASP 430  419  419 ASP ASP B . n 
B 1 431  ILE 431  420  420 ILE ILE B . n 
B 1 432  PRO 432  421  421 PRO PRO B . n 
B 1 433  LYS 433  422  422 LYS LYS B . n 
B 1 434  CYS 434  423  423 CYS CYS B . n 
B 1 435  GLY 435  424  424 GLY GLY B . n 
B 1 436  PHE 436  425  425 PHE PHE B . n 
B 1 437  ASP 437  426  ?   ?   ?   B . n 
B 1 438  ASN 438  427  ?   ?   ?   B . n 
B 1 439  GLU 439  428  ?   ?   ?   B . n 
B 1 440  ASP 440  429  ?   ?   ?   B . n 
B 1 441  PRO 441  430  ?   ?   ?   B . n 
B 1 442  ALA 442  431  ?   ?   ?   B . n 
B 1 443  CYS 443  432  ?   ?   ?   B . n 
B 1 444  ASN 444  433  ?   ?   ?   B . n 
B 1 445  GLN 445  434  ?   ?   ?   B . n 
B 1 446  ASP 446  435  ?   ?   ?   B . n 
B 1 447  HIS 447  436  ?   ?   ?   B . n 
B 1 448  LEU 448  437  ?   ?   ?   B . n 
B 1 449  SER 449  438  ?   ?   ?   B . n 
B 1 450  THR 450  439  ?   ?   ?   B . n 
B 1 451  LEU 451  440  ?   ?   ?   B . n 
B 1 452  GLU 452  441  ?   ?   ?   B . n 
B 1 453  VAL 453  442  ?   ?   ?   B . n 
B 1 454  LEU 454  443  ?   ?   ?   B . n 
B 1 455  ALA 455  444  ?   ?   ?   B . n 
B 1 456  LEU 456  445  ?   ?   ?   B . n 
B 1 457  VAL 457  446  ?   ?   ?   B . n 
B 1 458  GLY 458  447  ?   ?   ?   B . n 
B 1 459  SER 459  448  ?   ?   ?   B . n 
B 1 460  LEU 460  449  ?   ?   ?   B . n 
B 1 461  SER 461  450  ?   ?   ?   B . n 
B 1 462  LEU 462  451  ?   ?   ?   B . n 
B 1 463  LEU 463  452  ?   ?   ?   B . n 
B 1 464  GLY 464  453  ?   ?   ?   B . n 
B 1 465  ILE 465  454  ?   ?   ?   B . n 
B 1 466  LEU 466  455  ?   ?   ?   B . n 
B 1 467  ILE 467  456  ?   ?   ?   B . n 
B 1 468  VAL 468  457  ?   ?   ?   B . n 
B 1 469  SER 469  458  ?   ?   ?   B . n 
B 1 470  PHE 470  459  ?   ?   ?   B . n 
B 1 471  PHE 471  460  ?   ?   ?   B . n 
B 1 472  ILE 472  461  ?   ?   ?   B . n 
B 1 473  TYR 473  462  ?   ?   ?   B . n 
B 1 474  ARG 474  463  ?   ?   ?   B . n 
B 1 475  LYS 475  464  ?   ?   ?   B . n 
B 1 476  MET 476  465  ?   ?   ?   B . n 
B 1 477  GLN 477  466  ?   ?   ?   B . n 
B 1 478  LEU 478  467  ?   ?   ?   B . n 
B 1 479  GLU 479  468  ?   ?   ?   B . n 
B 1 480  LYS 480  469  ?   ?   ?   B . n 
B 1 481  GLU 481  470  ?   ?   ?   B . n 
B 1 482  LEU 482  471  ?   ?   ?   B . n 
B 1 483  ALA 483  472  ?   ?   ?   B . n 
B 1 484  SER 484  473  ?   ?   ?   B . n 
B 1 485  GLU 485  474  ?   ?   ?   B . n 
B 1 486  LEU 486  475  ?   ?   ?   B . n 
B 1 487  TRP 487  476  ?   ?   ?   B . n 
B 1 488  ARG 488  477  ?   ?   ?   B . n 
B 1 489  VAL 489  478  ?   ?   ?   B . n 
B 1 490  ARG 490  479  ?   ?   ?   B . n 
B 1 491  TRP 491  480  ?   ?   ?   B . n 
B 1 492  GLU 492  481  ?   ?   ?   B . n 
B 1 493  ASP 493  482  ?   ?   ?   B . n 
B 1 494  VAL 494  483  ?   ?   ?   B . n 
B 1 495  GLU 495  484  ?   ?   ?   B . n 
B 1 496  PRO 496  485  ?   ?   ?   B . n 
B 1 497  SER 497  486  ?   ?   ?   B . n 
B 1 498  SER 498  487  ?   ?   ?   B . n 
B 1 499  LEU 499  488  ?   ?   ?   B . n 
B 1 500  GLU 500  489  ?   ?   ?   B . n 
B 1 501  ARG 501  490  ?   ?   ?   B . n 
B 1 502  HIS 502  491  ?   ?   ?   B . n 
B 1 503  LEU 503  492  ?   ?   ?   B . n 
B 1 504  ARG 504  493  ?   ?   ?   B . n 
B 1 505  SER 505  494  ?   ?   ?   B . n 
B 1 506  ALA 506  495  ?   ?   ?   B . n 
B 1 507  GLY 507  496  ?   ?   ?   B . n 
B 1 508  SER 508  497  ?   ?   ?   B . n 
B 1 509  ARG 509  498  ?   ?   ?   B . n 
B 1 510  LEU 510  499  ?   ?   ?   B . n 
B 1 511  THR 511  500  ?   ?   ?   B . n 
B 1 512  LEU 512  501  ?   ?   ?   B . n 
B 1 513  SER 513  502  ?   ?   ?   B . n 
B 1 514  GLY 514  503  ?   ?   ?   B . n 
B 1 515  ARG 515  504  ?   ?   ?   B . n 
B 1 516  GLY 516  505  ?   ?   ?   B . n 
B 1 517  SER 517  506  ?   ?   ?   B . n 
B 1 518  ASN 518  507  ?   ?   ?   B . n 
B 1 519  TYR 519  508  ?   ?   ?   B . n 
B 1 520  GLY 520  509  ?   ?   ?   B . n 
B 1 521  SER 521  510  ?   ?   ?   B . n 
B 1 522  LEU 522  511  ?   ?   ?   B . n 
B 1 523  LEU 523  512  ?   ?   ?   B . n 
B 1 524  THR 524  513  ?   ?   ?   B . n 
B 1 525  THR 525  514  ?   ?   ?   B . n 
B 1 526  GLU 526  515  ?   ?   ?   B . n 
B 1 527  GLY 527  516  ?   ?   ?   B . n 
B 1 528  GLN 528  517  ?   ?   ?   B . n 
B 1 529  PHE 529  518  ?   ?   ?   B . n 
B 1 530  GLN 530  519  ?   ?   ?   B . n 
B 1 531  VAL 531  520  ?   ?   ?   B . n 
B 1 532  PHE 532  521  ?   ?   ?   B . n 
B 1 533  ALA 533  522  ?   ?   ?   B . n 
B 1 534  LYS 534  523  ?   ?   ?   B . n 
B 1 535  THR 535  524  ?   ?   ?   B . n 
B 1 536  ALA 536  525  ?   ?   ?   B . n 
B 1 537  TYR 537  526  ?   ?   ?   B . n 
B 1 538  TYR 538  527  ?   ?   ?   B . n 
B 1 539  LYS 539  528  ?   ?   ?   B . n 
B 1 540  GLY 540  529  ?   ?   ?   B . n 
B 1 541  ASN 541  530  ?   ?   ?   B . n 
B 1 542  LEU 542  531  ?   ?   ?   B . n 
B 1 543  VAL 543  532  ?   ?   ?   B . n 
B 1 544  ALA 544  533  ?   ?   ?   B . n 
B 1 545  VAL 545  534  ?   ?   ?   B . n 
B 1 546  LYS 546  535  ?   ?   ?   B . n 
B 1 547  ARG 547  536  ?   ?   ?   B . n 
B 1 548  VAL 548  537  ?   ?   ?   B . n 
B 1 549  ASN 549  538  ?   ?   ?   B . n 
B 1 550  ARG 550  539  ?   ?   ?   B . n 
B 1 551  LYS 551  540  ?   ?   ?   B . n 
B 1 552  ARG 552  541  ?   ?   ?   B . n 
B 1 553  ILE 553  542  ?   ?   ?   B . n 
B 1 554  GLU 554  543  ?   ?   ?   B . n 
B 1 555  LEU 555  544  ?   ?   ?   B . n 
B 1 556  THR 556  545  ?   ?   ?   B . n 
B 1 557  ARG 557  546  ?   ?   ?   B . n 
B 1 558  LYS 558  547  ?   ?   ?   B . n 
B 1 559  VAL 559  548  ?   ?   ?   B . n 
B 1 560  LEU 560  549  ?   ?   ?   B . n 
B 1 561  PHE 561  550  ?   ?   ?   B . n 
B 1 562  GLU 562  551  ?   ?   ?   B . n 
B 1 563  LEU 563  552  ?   ?   ?   B . n 
B 1 564  LYS 564  553  ?   ?   ?   B . n 
B 1 565  HIS 565  554  ?   ?   ?   B . n 
B 1 566  MET 566  555  ?   ?   ?   B . n 
B 1 567  ARG 567  556  ?   ?   ?   B . n 
B 1 568  ASP 568  557  ?   ?   ?   B . n 
B 1 569  VAL 569  558  ?   ?   ?   B . n 
B 1 570  GLN 570  559  ?   ?   ?   B . n 
B 1 571  ASN 571  560  ?   ?   ?   B . n 
B 1 572  GLU 572  561  ?   ?   ?   B . n 
B 1 573  HIS 573  562  ?   ?   ?   B . n 
B 1 574  LEU 574  563  ?   ?   ?   B . n 
B 1 575  THR 575  564  ?   ?   ?   B . n 
B 1 576  ARG 576  565  ?   ?   ?   B . n 
B 1 577  PHE 577  566  ?   ?   ?   B . n 
B 1 578  VAL 578  567  ?   ?   ?   B . n 
B 1 579  GLY 579  568  ?   ?   ?   B . n 
B 1 580  ALA 580  569  ?   ?   ?   B . n 
B 1 581  CYS 581  570  ?   ?   ?   B . n 
B 1 582  THR 582  571  ?   ?   ?   B . n 
B 1 583  ASP 583  572  ?   ?   ?   B . n 
B 1 584  PRO 584  573  ?   ?   ?   B . n 
B 1 585  PRO 585  574  ?   ?   ?   B . n 
B 1 586  ASN 586  575  ?   ?   ?   B . n 
B 1 587  ILE 587  576  ?   ?   ?   B . n 
B 1 588  CYS 588  577  ?   ?   ?   B . n 
B 1 589  ILE 589  578  ?   ?   ?   B . n 
B 1 590  LEU 590  579  ?   ?   ?   B . n 
B 1 591  THR 591  580  ?   ?   ?   B . n 
B 1 592  GLU 592  581  ?   ?   ?   B . n 
B 1 593  TYR 593  582  ?   ?   ?   B . n 
B 1 594  CYS 594  583  ?   ?   ?   B . n 
B 1 595  PRO 595  584  ?   ?   ?   B . n 
B 1 596  ARG 596  585  ?   ?   ?   B . n 
B 1 597  GLY 597  586  ?   ?   ?   B . n 
B 1 598  SER 598  587  ?   ?   ?   B . n 
B 1 599  LEU 599  588  ?   ?   ?   B . n 
B 1 600  GLN 600  589  ?   ?   ?   B . n 
B 1 601  ASP 601  590  ?   ?   ?   B . n 
B 1 602  ILE 602  591  ?   ?   ?   B . n 
B 1 603  LEU 603  592  ?   ?   ?   B . n 
B 1 604  GLU 604  593  ?   ?   ?   B . n 
B 1 605  ASN 605  594  ?   ?   ?   B . n 
B 1 606  GLU 606  595  ?   ?   ?   B . n 
B 1 607  SER 607  596  ?   ?   ?   B . n 
B 1 608  ILE 608  597  ?   ?   ?   B . n 
B 1 609  THR 609  598  ?   ?   ?   B . n 
B 1 610  LEU 610  599  ?   ?   ?   B . n 
B 1 611  ASP 611  600  ?   ?   ?   B . n 
B 1 612  TRP 612  601  ?   ?   ?   B . n 
B 1 613  MET 613  602  ?   ?   ?   B . n 
B 1 614  PHE 614  603  ?   ?   ?   B . n 
B 1 615  ARG 615  604  ?   ?   ?   B . n 
B 1 616  TYR 616  605  ?   ?   ?   B . n 
B 1 617  SER 617  606  ?   ?   ?   B . n 
B 1 618  LEU 618  607  ?   ?   ?   B . n 
B 1 619  THR 619  608  ?   ?   ?   B . n 
B 1 620  ASN 620  609  ?   ?   ?   B . n 
B 1 621  ASP 621  610  ?   ?   ?   B . n 
B 1 622  ILE 622  611  ?   ?   ?   B . n 
B 1 623  VAL 623  612  ?   ?   ?   B . n 
B 1 624  LYS 624  613  ?   ?   ?   B . n 
B 1 625  GLY 625  614  ?   ?   ?   B . n 
B 1 626  MET 626  615  ?   ?   ?   B . n 
B 1 627  LEU 627  616  ?   ?   ?   B . n 
B 1 628  PHE 628  617  ?   ?   ?   B . n 
B 1 629  LEU 629  618  ?   ?   ?   B . n 
B 1 630  HIS 630  619  ?   ?   ?   B . n 
B 1 631  ASN 631  620  ?   ?   ?   B . n 
B 1 632  GLY 632  621  ?   ?   ?   B . n 
B 1 633  ALA 633  622  ?   ?   ?   B . n 
B 1 634  ILE 634  623  ?   ?   ?   B . n 
B 1 635  CYS 635  624  ?   ?   ?   B . n 
B 1 636  SER 636  625  ?   ?   ?   B . n 
B 1 637  HIS 637  626  ?   ?   ?   B . n 
B 1 638  GLY 638  627  ?   ?   ?   B . n 
B 1 639  ASN 639  628  ?   ?   ?   B . n 
B 1 640  LEU 640  629  ?   ?   ?   B . n 
B 1 641  LYS 641  630  ?   ?   ?   B . n 
B 1 642  SER 642  631  ?   ?   ?   B . n 
B 1 643  SER 643  632  ?   ?   ?   B . n 
B 1 644  ASN 644  633  ?   ?   ?   B . n 
B 1 645  CYS 645  634  ?   ?   ?   B . n 
B 1 646  VAL 646  635  ?   ?   ?   B . n 
B 1 647  VAL 647  636  ?   ?   ?   B . n 
B 1 648  ASP 648  637  ?   ?   ?   B . n 
B 1 649  GLY 649  638  ?   ?   ?   B . n 
B 1 650  ARG 650  639  ?   ?   ?   B . n 
B 1 651  PHE 651  640  ?   ?   ?   B . n 
B 1 652  VAL 652  641  ?   ?   ?   B . n 
B 1 653  LEU 653  642  ?   ?   ?   B . n 
B 1 654  LYS 654  643  ?   ?   ?   B . n 
B 1 655  ILE 655  644  ?   ?   ?   B . n 
B 1 656  THR 656  645  ?   ?   ?   B . n 
B 1 657  ASP 657  646  ?   ?   ?   B . n 
B 1 658  TYR 658  647  ?   ?   ?   B . n 
B 1 659  GLY 659  648  ?   ?   ?   B . n 
B 1 660  LEU 660  649  ?   ?   ?   B . n 
B 1 661  GLU 661  650  ?   ?   ?   B . n 
B 1 662  SER 662  651  ?   ?   ?   B . n 
B 1 663  PHE 663  652  ?   ?   ?   B . n 
B 1 664  ARG 664  653  ?   ?   ?   B . n 
B 1 665  ASP 665  654  ?   ?   ?   B . n 
B 1 666  LEU 666  655  ?   ?   ?   B . n 
B 1 667  ASP 667  656  ?   ?   ?   B . n 
B 1 668  PRO 668  657  ?   ?   ?   B . n 
B 1 669  GLU 669  658  ?   ?   ?   B . n 
B 1 670  GLN 670  659  ?   ?   ?   B . n 
B 1 671  GLY 671  660  ?   ?   ?   B . n 
B 1 672  HIS 672  661  ?   ?   ?   B . n 
B 1 673  THR 673  662  ?   ?   ?   B . n 
B 1 674  VAL 674  663  ?   ?   ?   B . n 
B 1 675  TYR 675  664  ?   ?   ?   B . n 
B 1 676  ALA 676  665  ?   ?   ?   B . n 
B 1 677  LYS 677  666  ?   ?   ?   B . n 
B 1 678  LYS 678  667  ?   ?   ?   B . n 
B 1 679  LEU 679  668  ?   ?   ?   B . n 
B 1 680  TRP 680  669  ?   ?   ?   B . n 
B 1 681  THR 681  670  ?   ?   ?   B . n 
B 1 682  ALA 682  671  ?   ?   ?   B . n 
B 1 683  PRO 683  672  ?   ?   ?   B . n 
B 1 684  GLU 684  673  ?   ?   ?   B . n 
B 1 685  LEU 685  674  ?   ?   ?   B . n 
B 1 686  LEU 686  675  ?   ?   ?   B . n 
B 1 687  ARG 687  676  ?   ?   ?   B . n 
B 1 688  MET 688  677  ?   ?   ?   B . n 
B 1 689  ALA 689  678  ?   ?   ?   B . n 
B 1 690  SER 690  679  ?   ?   ?   B . n 
B 1 691  PRO 691  680  ?   ?   ?   B . n 
B 1 692  PRO 692  681  ?   ?   ?   B . n 
B 1 693  VAL 693  682  ?   ?   ?   B . n 
B 1 694  ARG 694  683  ?   ?   ?   B . n 
B 1 695  GLY 695  684  ?   ?   ?   B . n 
B 1 696  SER 696  685  ?   ?   ?   B . n 
B 1 697  GLN 697  686  ?   ?   ?   B . n 
B 1 698  ALA 698  687  ?   ?   ?   B . n 
B 1 699  GLY 699  688  ?   ?   ?   B . n 
B 1 700  ASP 700  689  ?   ?   ?   B . n 
B 1 701  VAL 701  690  ?   ?   ?   B . n 
B 1 702  TYR 702  691  ?   ?   ?   B . n 
B 1 703  SER 703  692  ?   ?   ?   B . n 
B 1 704  PHE 704  693  ?   ?   ?   B . n 
B 1 705  GLY 705  694  ?   ?   ?   B . n 
B 1 706  ILE 706  695  ?   ?   ?   B . n 
B 1 707  ILE 707  696  ?   ?   ?   B . n 
B 1 708  LEU 708  697  ?   ?   ?   B . n 
B 1 709  GLN 709  698  ?   ?   ?   B . n 
B 1 710  GLU 710  699  ?   ?   ?   B . n 
B 1 711  ILE 711  700  ?   ?   ?   B . n 
B 1 712  ALA 712  701  ?   ?   ?   B . n 
B 1 713  LEU 713  702  ?   ?   ?   B . n 
B 1 714  ARG 714  703  ?   ?   ?   B . n 
B 1 715  SER 715  704  ?   ?   ?   B . n 
B 1 716  GLY 716  705  ?   ?   ?   B . n 
B 1 717  VAL 717  706  ?   ?   ?   B . n 
B 1 718  PHE 718  707  ?   ?   ?   B . n 
B 1 719  HIS 719  708  ?   ?   ?   B . n 
B 1 720  VAL 720  709  ?   ?   ?   B . n 
B 1 721  GLU 721  710  ?   ?   ?   B . n 
B 1 722  GLY 722  711  ?   ?   ?   B . n 
B 1 723  LEU 723  712  ?   ?   ?   B . n 
B 1 724  ASP 724  713  ?   ?   ?   B . n 
B 1 725  LEU 725  714  ?   ?   ?   B . n 
B 1 726  SER 726  715  ?   ?   ?   B . n 
B 1 727  PRO 727  716  ?   ?   ?   B . n 
B 1 728  LYS 728  717  ?   ?   ?   B . n 
B 1 729  GLU 729  718  ?   ?   ?   B . n 
B 1 730  ILE 730  719  ?   ?   ?   B . n 
B 1 731  ILE 731  720  ?   ?   ?   B . n 
B 1 732  GLU 732  721  ?   ?   ?   B . n 
B 1 733  ARG 733  722  ?   ?   ?   B . n 
B 1 734  VAL 734  723  ?   ?   ?   B . n 
B 1 735  THR 735  724  ?   ?   ?   B . n 
B 1 736  ARG 736  725  ?   ?   ?   B . n 
B 1 737  GLY 737  726  ?   ?   ?   B . n 
B 1 738  GLU 738  727  ?   ?   ?   B . n 
B 1 739  GLN 739  728  ?   ?   ?   B . n 
B 1 740  PRO 740  729  ?   ?   ?   B . n 
B 1 741  PRO 741  730  ?   ?   ?   B . n 
B 1 742  PHE 742  731  ?   ?   ?   B . n 
B 1 743  ARG 743  732  ?   ?   ?   B . n 
B 1 744  PRO 744  733  ?   ?   ?   B . n 
B 1 745  SER 745  734  ?   ?   ?   B . n 
B 1 746  LEU 746  735  ?   ?   ?   B . n 
B 1 747  ALA 747  736  ?   ?   ?   B . n 
B 1 748  LEU 748  737  ?   ?   ?   B . n 
B 1 749  GLN 749  738  ?   ?   ?   B . n 
B 1 750  SER 750  739  ?   ?   ?   B . n 
B 1 751  HIS 751  740  ?   ?   ?   B . n 
B 1 752  LEU 752  741  ?   ?   ?   B . n 
B 1 753  GLU 753  742  ?   ?   ?   B . n 
B 1 754  GLU 754  743  ?   ?   ?   B . n 
B 1 755  LEU 755  744  ?   ?   ?   B . n 
B 1 756  GLY 756  745  ?   ?   ?   B . n 
B 1 757  LEU 757  746  ?   ?   ?   B . n 
B 1 758  LEU 758  747  ?   ?   ?   B . n 
B 1 759  MET 759  748  ?   ?   ?   B . n 
B 1 760  GLN 760  749  ?   ?   ?   B . n 
B 1 761  ARG 761  750  ?   ?   ?   B . n 
B 1 762  CYS 762  751  ?   ?   ?   B . n 
B 1 763  TRP 763  752  ?   ?   ?   B . n 
B 1 764  ALA 764  753  ?   ?   ?   B . n 
B 1 765  GLU 765  754  ?   ?   ?   B . n 
B 1 766  ASP 766  755  ?   ?   ?   B . n 
B 1 767  PRO 767  756  ?   ?   ?   B . n 
B 1 768  GLN 768  757  ?   ?   ?   B . n 
B 1 769  GLU 769  758  ?   ?   ?   B . n 
B 1 770  ARG 770  759  ?   ?   ?   B . n 
B 1 771  PRO 771  760  ?   ?   ?   B . n 
B 1 772  PRO 772  761  ?   ?   ?   B . n 
B 1 773  PHE 773  762  ?   ?   ?   B . n 
B 1 774  GLN 774  763  ?   ?   ?   B . n 
B 1 775  GLN 775  764  ?   ?   ?   B . n 
B 1 776  ILE 776  765  ?   ?   ?   B . n 
B 1 777  ARG 777  766  ?   ?   ?   B . n 
B 1 778  LEU 778  767  ?   ?   ?   B . n 
B 1 779  THR 779  768  ?   ?   ?   B . n 
B 1 780  LEU 780  769  ?   ?   ?   B . n 
B 1 781  ARG 781  770  ?   ?   ?   B . n 
B 1 782  LYS 782  771  ?   ?   ?   B . n 
B 1 783  PHE 783  772  ?   ?   ?   B . n 
B 1 784  ASN 784  773  ?   ?   ?   B . n 
B 1 785  ARG 785  774  ?   ?   ?   B . n 
B 1 786  GLU 786  775  ?   ?   ?   B . n 
B 1 787  ASN 787  776  ?   ?   ?   B . n 
B 1 788  SER 788  777  ?   ?   ?   B . n 
B 1 789  SER 789  778  ?   ?   ?   B . n 
B 1 790  ASN 790  779  ?   ?   ?   B . n 
B 1 791  ILE 791  780  ?   ?   ?   B . n 
B 1 792  LEU 792  781  ?   ?   ?   B . n 
B 1 793  ASP 793  782  ?   ?   ?   B . n 
B 1 794  ASN 794  783  ?   ?   ?   B . n 
B 1 795  LEU 795  784  ?   ?   ?   B . n 
B 1 796  LEU 796  785  ?   ?   ?   B . n 
B 1 797  SER 797  786  ?   ?   ?   B . n 
B 1 798  ARG 798  787  ?   ?   ?   B . n 
B 1 799  MET 799  788  ?   ?   ?   B . n 
B 1 800  GLU 800  789  ?   ?   ?   B . n 
B 1 801  GLN 801  790  ?   ?   ?   B . n 
B 1 802  TYR 802  791  ?   ?   ?   B . n 
B 1 803  ALA 803  792  ?   ?   ?   B . n 
B 1 804  ASN 804  793  ?   ?   ?   B . n 
B 1 805  ASN 805  794  ?   ?   ?   B . n 
B 1 806  LEU 806  795  ?   ?   ?   B . n 
B 1 807  GLU 807  796  ?   ?   ?   B . n 
B 1 808  GLU 808  797  ?   ?   ?   B . n 
B 1 809  LEU 809  798  ?   ?   ?   B . n 
B 1 810  VAL 810  799  ?   ?   ?   B . n 
B 1 811  GLU 811  800  ?   ?   ?   B . n 
B 1 812  GLU 812  801  ?   ?   ?   B . n 
B 1 813  ARG 813  802  ?   ?   ?   B . n 
B 1 814  THR 814  803  ?   ?   ?   B . n 
B 1 815  GLN 815  804  ?   ?   ?   B . n 
B 1 816  ALA 816  805  ?   ?   ?   B . n 
B 1 817  TYR 817  806  ?   ?   ?   B . n 
B 1 818  LEU 818  807  ?   ?   ?   B . n 
B 1 819  GLU 819  808  ?   ?   ?   B . n 
B 1 820  GLU 820  809  ?   ?   ?   B . n 
B 1 821  LYS 821  810  ?   ?   ?   B . n 
B 1 822  ARG 822  811  ?   ?   ?   B . n 
B 1 823  LYS 823  812  ?   ?   ?   B . n 
B 1 824  ALA 824  813  ?   ?   ?   B . n 
B 1 825  GLU 825  814  ?   ?   ?   B . n 
B 1 826  ALA 826  815  ?   ?   ?   B . n 
B 1 827  LEU 827  816  ?   ?   ?   B . n 
B 1 828  LEU 828  817  ?   ?   ?   B . n 
B 1 829  TYR 829  818  ?   ?   ?   B . n 
B 1 830  GLN 830  819  ?   ?   ?   B . n 
B 1 831  ILE 831  820  ?   ?   ?   B . n 
B 1 832  LEU 832  821  ?   ?   ?   B . n 
B 1 833  PRO 833  822  ?   ?   ?   B . n 
B 1 834  HIS 834  823  ?   ?   ?   B . n 
B 1 835  SER 835  824  ?   ?   ?   B . n 
B 1 836  VAL 836  825  ?   ?   ?   B . n 
B 1 837  ALA 837  826  ?   ?   ?   B . n 
B 1 838  GLU 838  827  ?   ?   ?   B . n 
B 1 839  GLN 839  828  ?   ?   ?   B . n 
B 1 840  LEU 840  829  ?   ?   ?   B . n 
B 1 841  LYS 841  830  ?   ?   ?   B . n 
B 1 842  ARG 842  831  ?   ?   ?   B . n 
B 1 843  GLY 843  832  ?   ?   ?   B . n 
B 1 844  GLU 844  833  ?   ?   ?   B . n 
B 1 845  THR 845  834  ?   ?   ?   B . n 
B 1 846  VAL 846  835  ?   ?   ?   B . n 
B 1 847  GLN 847  836  ?   ?   ?   B . n 
B 1 848  ALA 848  837  ?   ?   ?   B . n 
B 1 849  GLU 849  838  ?   ?   ?   B . n 
B 1 850  ALA 850  839  ?   ?   ?   B . n 
B 1 851  PHE 851  840  ?   ?   ?   B . n 
B 1 852  ASP 852  841  ?   ?   ?   B . n 
B 1 853  SER 853  842  ?   ?   ?   B . n 
B 1 854  VAL 854  843  ?   ?   ?   B . n 
B 1 855  THR 855  844  ?   ?   ?   B . n 
B 1 856  ILE 856  845  ?   ?   ?   B . n 
B 1 857  TYR 857  846  ?   ?   ?   B . n 
B 1 858  PHE 858  847  ?   ?   ?   B . n 
B 1 859  SER 859  848  ?   ?   ?   B . n 
B 1 860  ASP 860  849  ?   ?   ?   B . n 
B 1 861  ILE 861  850  ?   ?   ?   B . n 
B 1 862  VAL 862  851  ?   ?   ?   B . n 
B 1 863  GLY 863  852  ?   ?   ?   B . n 
B 1 864  PHE 864  853  ?   ?   ?   B . n 
B 1 865  THR 865  854  ?   ?   ?   B . n 
B 1 866  ALA 866  855  ?   ?   ?   B . n 
B 1 867  LEU 867  856  ?   ?   ?   B . n 
B 1 868  SER 868  857  ?   ?   ?   B . n 
B 1 869  ALA 869  858  ?   ?   ?   B . n 
B 1 870  GLU 870  859  ?   ?   ?   B . n 
B 1 871  SER 871  860  ?   ?   ?   B . n 
B 1 872  THR 872  861  ?   ?   ?   B . n 
B 1 873  PRO 873  862  ?   ?   ?   B . n 
B 1 874  MET 874  863  ?   ?   ?   B . n 
B 1 875  GLN 875  864  ?   ?   ?   B . n 
B 1 876  VAL 876  865  ?   ?   ?   B . n 
B 1 877  VAL 877  866  ?   ?   ?   B . n 
B 1 878  THR 878  867  ?   ?   ?   B . n 
B 1 879  LEU 879  868  ?   ?   ?   B . n 
B 1 880  LEU 880  869  ?   ?   ?   B . n 
B 1 881  ASN 881  870  ?   ?   ?   B . n 
B 1 882  ASP 882  871  ?   ?   ?   B . n 
B 1 883  LEU 883  872  ?   ?   ?   B . n 
B 1 884  TYR 884  873  ?   ?   ?   B . n 
B 1 885  THR 885  874  ?   ?   ?   B . n 
B 1 886  CYS 886  875  ?   ?   ?   B . n 
B 1 887  PHE 887  876  ?   ?   ?   B . n 
B 1 888  ASP 888  877  ?   ?   ?   B . n 
B 1 889  ALA 889  878  ?   ?   ?   B . n 
B 1 890  VAL 890  879  ?   ?   ?   B . n 
B 1 891  ILE 891  880  ?   ?   ?   B . n 
B 1 892  ASP 892  881  ?   ?   ?   B . n 
B 1 893  ASN 893  882  ?   ?   ?   B . n 
B 1 894  PHE 894  883  ?   ?   ?   B . n 
B 1 895  ASP 895  884  ?   ?   ?   B . n 
B 1 896  VAL 896  885  ?   ?   ?   B . n 
B 1 897  TYR 897  886  ?   ?   ?   B . n 
B 1 898  LYS 898  887  ?   ?   ?   B . n 
B 1 899  VAL 899  888  ?   ?   ?   B . n 
B 1 900  GLU 900  889  ?   ?   ?   B . n 
B 1 901  THR 901  890  ?   ?   ?   B . n 
B 1 902  ILE 902  891  ?   ?   ?   B . n 
B 1 903  GLY 903  892  ?   ?   ?   B . n 
B 1 904  ASP 904  893  ?   ?   ?   B . n 
B 1 905  ALA 905  894  ?   ?   ?   B . n 
B 1 906  TYR 906  895  ?   ?   ?   B . n 
B 1 907  MET 907  896  ?   ?   ?   B . n 
B 1 908  VAL 908  897  ?   ?   ?   B . n 
B 1 909  VAL 909  898  ?   ?   ?   B . n 
B 1 910  SER 910  899  ?   ?   ?   B . n 
B 1 911  GLY 911  900  ?   ?   ?   B . n 
B 1 912  LEU 912  901  ?   ?   ?   B . n 
B 1 913  PRO 913  902  ?   ?   ?   B . n 
B 1 914  VAL 914  903  ?   ?   ?   B . n 
B 1 915  ARG 915  904  ?   ?   ?   B . n 
B 1 916  ASN 916  905  ?   ?   ?   B . n 
B 1 917  GLY 917  906  ?   ?   ?   B . n 
B 1 918  ARG 918  907  ?   ?   ?   B . n 
B 1 919  LEU 919  908  ?   ?   ?   B . n 
B 1 920  HIS 920  909  ?   ?   ?   B . n 
B 1 921  ALA 921  910  ?   ?   ?   B . n 
B 1 922  CYS 922  911  ?   ?   ?   B . n 
B 1 923  GLU 923  912  ?   ?   ?   B . n 
B 1 924  VAL 924  913  ?   ?   ?   B . n 
B 1 925  ALA 925  914  ?   ?   ?   B . n 
B 1 926  ARG 926  915  ?   ?   ?   B . n 
B 1 927  MET 927  916  ?   ?   ?   B . n 
B 1 928  ALA 928  917  ?   ?   ?   B . n 
B 1 929  LEU 929  918  ?   ?   ?   B . n 
B 1 930  ALA 930  919  ?   ?   ?   B . n 
B 1 931  LEU 931  920  ?   ?   ?   B . n 
B 1 932  LEU 932  921  ?   ?   ?   B . n 
B 1 933  ASP 933  922  ?   ?   ?   B . n 
B 1 934  ALA 934  923  ?   ?   ?   B . n 
B 1 935  VAL 935  924  ?   ?   ?   B . n 
B 1 936  ARG 936  925  ?   ?   ?   B . n 
B 1 937  SER 937  926  ?   ?   ?   B . n 
B 1 938  PHE 938  927  ?   ?   ?   B . n 
B 1 939  ARG 939  928  ?   ?   ?   B . n 
B 1 940  ILE 940  929  ?   ?   ?   B . n 
B 1 941  ARG 941  930  ?   ?   ?   B . n 
B 1 942  HIS 942  931  ?   ?   ?   B . n 
B 1 943  ARG 943  932  ?   ?   ?   B . n 
B 1 944  PRO 944  933  ?   ?   ?   B . n 
B 1 945  GLN 945  934  ?   ?   ?   B . n 
B 1 946  GLU 946  935  ?   ?   ?   B . n 
B 1 947  GLN 947  936  ?   ?   ?   B . n 
B 1 948  LEU 948  937  ?   ?   ?   B . n 
B 1 949  ARG 949  938  ?   ?   ?   B . n 
B 1 950  LEU 950  939  ?   ?   ?   B . n 
B 1 951  ARG 951  940  ?   ?   ?   B . n 
B 1 952  ILE 952  941  ?   ?   ?   B . n 
B 1 953  GLY 953  942  ?   ?   ?   B . n 
B 1 954  ILE 954  943  ?   ?   ?   B . n 
B 1 955  HIS 955  944  ?   ?   ?   B . n 
B 1 956  THR 956  945  ?   ?   ?   B . n 
B 1 957  GLY 957  946  ?   ?   ?   B . n 
B 1 958  PRO 958  947  ?   ?   ?   B . n 
B 1 959  VAL 959  948  ?   ?   ?   B . n 
B 1 960  CYS 960  949  ?   ?   ?   B . n 
B 1 961  ALA 961  950  ?   ?   ?   B . n 
B 1 962  GLY 962  951  ?   ?   ?   B . n 
B 1 963  VAL 963  952  ?   ?   ?   B . n 
B 1 964  VAL 964  953  ?   ?   ?   B . n 
B 1 965  GLY 965  954  ?   ?   ?   B . n 
B 1 966  LEU 966  955  ?   ?   ?   B . n 
B 1 967  LYS 967  956  ?   ?   ?   B . n 
B 1 968  MET 968  957  ?   ?   ?   B . n 
B 1 969  PRO 969  958  ?   ?   ?   B . n 
B 1 970  ARG 970  959  ?   ?   ?   B . n 
B 1 971  TYR 971  960  ?   ?   ?   B . n 
B 1 972  CYS 972  961  ?   ?   ?   B . n 
B 1 973  LEU 973  962  ?   ?   ?   B . n 
B 1 974  PHE 974  963  ?   ?   ?   B . n 
B 1 975  GLY 975  964  ?   ?   ?   B . n 
B 1 976  ASP 976  965  ?   ?   ?   B . n 
B 1 977  THR 977  966  ?   ?   ?   B . n 
B 1 978  VAL 978  967  ?   ?   ?   B . n 
B 1 979  ASN 979  968  ?   ?   ?   B . n 
B 1 980  THR 980  969  ?   ?   ?   B . n 
B 1 981  ALA 981  970  ?   ?   ?   B . n 
B 1 982  SER 982  971  ?   ?   ?   B . n 
B 1 983  ARG 983  972  ?   ?   ?   B . n 
B 1 984  MET 984  973  ?   ?   ?   B . n 
B 1 985  GLU 985  974  ?   ?   ?   B . n 
B 1 986  SER 986  975  ?   ?   ?   B . n 
B 1 987  ASN 987  976  ?   ?   ?   B . n 
B 1 988  GLY 988  977  ?   ?   ?   B . n 
B 1 989  GLU 989  978  ?   ?   ?   B . n 
B 1 990  ALA 990  979  ?   ?   ?   B . n 
B 1 991  LEU 991  980  ?   ?   ?   B . n 
B 1 992  LYS 992  981  ?   ?   ?   B . n 
B 1 993  ILE 993  982  ?   ?   ?   B . n 
B 1 994  HIS 994  983  ?   ?   ?   B . n 
B 1 995  LEU 995  984  ?   ?   ?   B . n 
B 1 996  SER 996  985  ?   ?   ?   B . n 
B 1 997  SER 997  986  ?   ?   ?   B . n 
B 1 998  GLU 998  987  ?   ?   ?   B . n 
B 1 999  THR 999  988  ?   ?   ?   B . n 
B 1 1000 LYS 1000 989  ?   ?   ?   B . n 
B 1 1001 ALA 1001 990  ?   ?   ?   B . n 
B 1 1002 VAL 1002 991  ?   ?   ?   B . n 
B 1 1003 LEU 1003 992  ?   ?   ?   B . n 
B 1 1004 GLU 1004 993  ?   ?   ?   B . n 
B 1 1005 GLU 1005 994  ?   ?   ?   B . n 
B 1 1006 PHE 1006 995  ?   ?   ?   B . n 
B 1 1007 GLY 1007 996  ?   ?   ?   B . n 
B 1 1008 GLY 1008 997  ?   ?   ?   B . n 
B 1 1009 PHE 1009 998  ?   ?   ?   B . n 
B 1 1010 GLU 1010 999  ?   ?   ?   B . n 
B 1 1011 LEU 1011 1000 ?   ?   ?   B . n 
B 1 1012 GLU 1012 1001 ?   ?   ?   B . n 
B 1 1013 LEU 1013 1002 ?   ?   ?   B . n 
B 1 1014 ARG 1014 1003 ?   ?   ?   B . n 
B 1 1015 GLY 1015 1004 ?   ?   ?   B . n 
B 1 1016 ASP 1016 1005 ?   ?   ?   B . n 
B 1 1017 VAL 1017 1006 ?   ?   ?   B . n 
B 1 1018 GLU 1018 1007 ?   ?   ?   B . n 
B 1 1019 MET 1019 1008 ?   ?   ?   B . n 
B 1 1020 LYS 1020 1009 ?   ?   ?   B . n 
B 1 1021 GLY 1021 1010 ?   ?   ?   B . n 
B 1 1022 LYS 1022 1011 ?   ?   ?   B . n 
B 1 1023 GLY 1023 1012 ?   ?   ?   B . n 
B 1 1024 LYS 1024 1013 ?   ?   ?   B . n 
B 1 1025 VAL 1025 1014 ?   ?   ?   B . n 
B 1 1026 ARG 1026 1015 ?   ?   ?   B . n 
B 1 1027 THR 1027 1016 ?   ?   ?   B . n 
B 1 1028 TYR 1028 1017 ?   ?   ?   B . n 
B 1 1029 TRP 1029 1018 ?   ?   ?   B . n 
B 1 1030 LEU 1030 1019 ?   ?   ?   B . n 
B 1 1031 LEU 1031 1020 ?   ?   ?   B . n 
B 1 1032 GLY 1032 1021 ?   ?   ?   B . n 
B 1 1033 GLU 1033 1022 ?   ?   ?   B . n 
B 1 1034 ARG 1034 1023 ?   ?   ?   B . n 
B 1 1035 GLY 1035 1024 ?   ?   ?   B . n 
B 1 1036 SER 1036 1025 ?   ?   ?   B . n 
B 1 1037 SER 1037 1026 ?   ?   ?   B . n 
B 1 1038 THR 1038 1027 ?   ?   ?   B . n 
B 1 1039 ARG 1039 1028 ?   ?   ?   B . n 
B 1 1040 GLY 1040 1029 ?   ?   ?   B . n 
# 
loop_
_pdbx_branch_scheme.asym_id 
_pdbx_branch_scheme.entity_id 
_pdbx_branch_scheme.mon_id 
_pdbx_branch_scheme.num 
_pdbx_branch_scheme.pdb_asym_id 
_pdbx_branch_scheme.pdb_mon_id 
_pdbx_branch_scheme.pdb_seq_num 
_pdbx_branch_scheme.auth_asym_id 
_pdbx_branch_scheme.auth_mon_id 
_pdbx_branch_scheme.auth_seq_num 
_pdbx_branch_scheme.hetero 
C 2 NAG 1 C NAG 1 A NAG 451 n 
C 2 NAG 2 C NAG 2 A NAG 452 n 
C 2 MAN 3 C MAN 3 A MAN 604 n 
D 2 NAG 1 D NAG 1 A NAG 461 n 
D 2 NAG 2 D NAG 2 A NAG 462 n 
D 2 MAN 3 D MAN 3 A MAN 601 n 
E 2 NAG 1 E NAG 1 B NAG 451 n 
E 2 NAG 2 E NAG 2 B NAG 452 n 
E 2 MAN 3 E MAN 3 B MAN 602 n 
F 2 NAG 1 F NAG 1 B NAG 461 n 
F 2 NAG 2 F NAG 2 B NAG 462 n 
F 2 MAN 3 F MAN 3 B MAN 601 n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 CL  ? ? CL  ? ? 'SUBJECT OF INVESTIGATION' ? 
2 MAN ? ? MAN ? ? 'SUBJECT OF INVESTIGATION' ? 
3 NAG ? ? NAG ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 
G 3 CL  1 1101 600 CL  CL  A . 
H 4 NAG 1 1102 603 NAG NAG A . 
I 3 CL  1 1101 600 CL  CL  B . 
J 4 NAG 1 1102 608 NAG NAG B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A LYS 35  ? CG  ? A LYS 46  CG  
2   1 Y 1 A LYS 35  ? CD  ? A LYS 46  CD  
3   1 Y 1 A LYS 35  ? CE  ? A LYS 46  CE  
4   1 Y 1 A LYS 35  ? NZ  ? A LYS 46  NZ  
5   1 Y 1 A ASP 39  ? CG  ? A ASP 50  CG  
6   1 Y 1 A ASP 39  ? OD1 ? A ASP 50  OD1 
7   1 Y 1 A ASP 39  ? OD2 ? A ASP 50  OD2 
8   1 Y 1 A GLU 75  ? CG  ? A GLU 86  CG  
9   1 Y 1 A GLU 75  ? CD  ? A GLU 86  CD  
10  1 Y 1 A GLU 75  ? OE1 ? A GLU 86  OE1 
11  1 Y 1 A GLU 75  ? OE2 ? A GLU 86  OE2 
12  1 Y 1 A ASP 118 ? CG  ? A ASP 129 CG  
13  1 Y 1 A ASP 118 ? OD1 ? A ASP 129 OD1 
14  1 Y 1 A ASP 118 ? OD2 ? A ASP 129 OD2 
15  1 Y 1 A GLU 161 ? CG  ? A GLU 172 CG  
16  1 Y 1 A GLU 161 ? CD  ? A GLU 172 CD  
17  1 Y 1 A GLU 161 ? OE1 ? A GLU 172 OE1 
18  1 Y 1 A GLU 161 ? OE2 ? A GLU 172 OE2 
19  1 Y 1 A ASN 180 ? CG  ? A ASN 191 CG  
20  1 Y 1 A ASN 180 ? OD1 ? A ASN 191 OD1 
21  1 Y 1 A ASN 180 ? ND2 ? A ASN 191 ND2 
22  1 Y 1 A ASP 184 ? CG  ? A ASP 195 CG  
23  1 Y 1 A ASP 184 ? OD1 ? A ASP 195 OD1 
24  1 Y 1 A ASP 184 ? OD2 ? A ASP 195 OD2 
25  1 Y 1 A ASP 191 ? CG  ? A ASP 202 CG  
26  1 Y 1 A ASP 191 ? OD1 ? A ASP 202 OD1 
27  1 Y 1 A ASP 191 ? OD2 ? A ASP 202 OD2 
28  1 Y 1 A LEU 193 ? CG  ? A LEU 204 CG  
29  1 Y 1 A LEU 193 ? CD1 ? A LEU 204 CD1 
30  1 Y 1 A LEU 193 ? CD2 ? A LEU 204 CD2 
31  1 Y 1 A THR 197 ? OG1 ? A THR 208 OG1 
32  1 Y 1 A THR 197 ? CG2 ? A THR 208 CG2 
33  1 Y 1 A ARG 198 ? CG  ? A ARG 209 CG  
34  1 Y 1 A ARG 198 ? CD  ? A ARG 209 CD  
35  1 Y 1 A ARG 198 ? NE  ? A ARG 209 NE  
36  1 Y 1 A ARG 198 ? CZ  ? A ARG 209 CZ  
37  1 Y 1 A ARG 198 ? NH1 ? A ARG 209 NH1 
38  1 Y 1 A ARG 198 ? NH2 ? A ARG 209 NH2 
39  1 Y 1 A ARG 201 ? CG  ? A ARG 212 CG  
40  1 Y 1 A ARG 201 ? CD  ? A ARG 212 CD  
41  1 Y 1 A ARG 201 ? NE  ? A ARG 212 NE  
42  1 Y 1 A ARG 201 ? CZ  ? A ARG 212 CZ  
43  1 Y 1 A ARG 201 ? NH1 ? A ARG 212 NH1 
44  1 Y 1 A ARG 201 ? NH2 ? A ARG 212 NH2 
45  1 Y 1 A ARG 205 ? CG  ? A ARG 216 CG  
46  1 Y 1 A ARG 205 ? CD  ? A ARG 216 CD  
47  1 Y 1 A ARG 205 ? NE  ? A ARG 216 NE  
48  1 Y 1 A ARG 205 ? CZ  ? A ARG 216 CZ  
49  1 Y 1 A ARG 205 ? NH1 ? A ARG 216 NH1 
50  1 Y 1 A ARG 205 ? NH2 ? A ARG 216 NH2 
51  1 Y 1 A LYS 206 ? CG  ? A LYS 217 CG  
52  1 Y 1 A LYS 206 ? CD  ? A LYS 217 CD  
53  1 Y 1 A LYS 206 ? CE  ? A LYS 217 CE  
54  1 Y 1 A LYS 206 ? NZ  ? A LYS 217 NZ  
55  1 Y 1 A ASP 217 ? CG  ? A ASP 228 CG  
56  1 Y 1 A ASP 217 ? OD1 ? A ASP 228 OD1 
57  1 Y 1 A ASP 217 ? OD2 ? A ASP 228 OD2 
58  1 Y 1 A GLU 228 ? CG  ? A GLU 239 CG  
59  1 Y 1 A GLU 228 ? CD  ? A GLU 239 CD  
60  1 Y 1 A GLU 228 ? OE1 ? A GLU 239 OE1 
61  1 Y 1 A GLU 228 ? OE2 ? A GLU 239 OE2 
62  1 Y 1 A GLU 234 ? CG  ? A GLU 245 CG  
63  1 Y 1 A GLU 234 ? CD  ? A GLU 245 CD  
64  1 Y 1 A GLU 234 ? OE1 ? A GLU 245 OE1 
65  1 Y 1 A GLU 234 ? OE2 ? A GLU 245 OE2 
66  1 Y 1 A ASP 235 ? CG  ? A ASP 246 CG  
67  1 Y 1 A ASP 235 ? OD1 ? A ASP 246 OD1 
68  1 Y 1 A ASP 235 ? OD2 ? A ASP 246 OD2 
69  1 Y 1 A ASP 264 ? CG  ? A ASP 275 CG  
70  1 Y 1 A ASP 264 ? OD1 ? A ASP 275 OD1 
71  1 Y 1 A ASP 264 ? OD2 ? A ASP 275 OD2 
72  1 Y 1 A VAL 268 ? CG1 ? A VAL 279 CG1 
73  1 Y 1 A VAL 268 ? CG2 ? A VAL 279 CG2 
74  1 Y 1 A ASP 286 ? CG  ? A ASP 297 CG  
75  1 Y 1 A ASP 286 ? OD1 ? A ASP 297 OD1 
76  1 Y 1 A ASP 286 ? OD2 ? A ASP 297 OD2 
77  1 Y 1 A GLU 289 ? CG  ? A GLU 300 CG  
78  1 Y 1 A GLU 289 ? CD  ? A GLU 300 CD  
79  1 Y 1 A GLU 289 ? OE1 ? A GLU 300 OE1 
80  1 Y 1 A GLU 289 ? OE2 ? A GLU 300 OE2 
81  1 Y 1 A GLU 292 ? CG  ? A GLU 303 CG  
82  1 Y 1 A GLU 292 ? CD  ? A GLU 303 CD  
83  1 Y 1 A GLU 292 ? OE1 ? A GLU 303 OE1 
84  1 Y 1 A GLU 292 ? OE2 ? A GLU 303 OE2 
85  1 Y 1 A GLU 303 ? CG  ? A GLU 314 CG  
86  1 Y 1 A GLU 303 ? CD  ? A GLU 314 CD  
87  1 Y 1 A GLU 303 ? OE1 ? A GLU 314 OE1 
88  1 Y 1 A GLU 303 ? OE2 ? A GLU 314 OE2 
89  1 Y 1 A ASN 306 ? CG  ? A ASN 317 CG  
90  1 Y 1 A ASN 306 ? OD1 ? A ASN 317 OD1 
91  1 Y 1 A ASN 306 ? ND2 ? A ASN 317 ND2 
92  1 Y 1 A GLU 310 ? CG  ? A GLU 321 CG  
93  1 Y 1 A GLU 310 ? CD  ? A GLU 321 CD  
94  1 Y 1 A GLU 310 ? OE1 ? A GLU 321 OE1 
95  1 Y 1 A GLU 310 ? OE2 ? A GLU 321 OE2 
96  1 Y 1 A GLU 384 ? CG  ? A GLU 395 CG  
97  1 Y 1 A GLU 384 ? CD  ? A GLU 395 CD  
98  1 Y 1 A GLU 384 ? OE1 ? A GLU 395 OE1 
99  1 Y 1 A GLU 384 ? OE2 ? A GLU 395 OE2 
100 1 Y 1 A ASN 385 ? CG  ? A ASN 396 CG  
101 1 Y 1 A ASN 385 ? OD1 ? A ASN 396 OD1 
102 1 Y 1 A ASN 385 ? ND2 ? A ASN 396 ND2 
103 1 Y 1 A SER 405 ? OG  ? A SER 416 OG  
104 1 Y 1 A LYS 408 ? CG  ? A LYS 419 CG  
105 1 Y 1 A LYS 408 ? CD  ? A LYS 419 CD  
106 1 Y 1 A LYS 408 ? CE  ? A LYS 419 CE  
107 1 Y 1 A LYS 408 ? NZ  ? A LYS 419 NZ  
108 1 Y 1 A ASN 410 ? CG  ? A ASN 421 CG  
109 1 Y 1 A ASN 410 ? OD1 ? A ASN 421 OD1 
110 1 Y 1 A ASN 410 ? ND2 ? A ASN 421 ND2 
111 1 Y 1 A ILE 420 ? CG1 ? A ILE 431 CG1 
112 1 Y 1 A ILE 420 ? CG2 ? A ILE 431 CG2 
113 1 Y 1 A ILE 420 ? CD1 ? A ILE 431 CD1 
114 1 Y 1 A LYS 422 ? CG  ? A LYS 433 CG  
115 1 Y 1 A LYS 422 ? CD  ? A LYS 433 CD  
116 1 Y 1 A LYS 422 ? CE  ? A LYS 433 CE  
117 1 Y 1 A LYS 422 ? NZ  ? A LYS 433 NZ  
118 1 Y 1 B LYS 35  ? CG  ? B LYS 46  CG  
119 1 Y 1 B LYS 35  ? CD  ? B LYS 46  CD  
120 1 Y 1 B LYS 35  ? CE  ? B LYS 46  CE  
121 1 Y 1 B LYS 35  ? NZ  ? B LYS 46  NZ  
122 1 Y 1 B ASP 39  ? CG  ? B ASP 50  CG  
123 1 Y 1 B ASP 39  ? OD1 ? B ASP 50  OD1 
124 1 Y 1 B ASP 39  ? OD2 ? B ASP 50  OD2 
125 1 Y 1 B GLU 75  ? CG  ? B GLU 86  CG  
126 1 Y 1 B GLU 75  ? CD  ? B GLU 86  CD  
127 1 Y 1 B GLU 75  ? OE1 ? B GLU 86  OE1 
128 1 Y 1 B GLU 75  ? OE2 ? B GLU 86  OE2 
129 1 Y 1 B ASP 118 ? CG  ? B ASP 129 CG  
130 1 Y 1 B ASP 118 ? OD1 ? B ASP 129 OD1 
131 1 Y 1 B ASP 118 ? OD2 ? B ASP 129 OD2 
132 1 Y 1 B GLU 161 ? CG  ? B GLU 172 CG  
133 1 Y 1 B GLU 161 ? CD  ? B GLU 172 CD  
134 1 Y 1 B GLU 161 ? OE1 ? B GLU 172 OE1 
135 1 Y 1 B GLU 161 ? OE2 ? B GLU 172 OE2 
136 1 Y 1 B ASN 180 ? CG  ? B ASN 191 CG  
137 1 Y 1 B ASN 180 ? OD1 ? B ASN 191 OD1 
138 1 Y 1 B ASN 180 ? ND2 ? B ASN 191 ND2 
139 1 Y 1 B ASP 184 ? CG  ? B ASP 195 CG  
140 1 Y 1 B ASP 184 ? OD1 ? B ASP 195 OD1 
141 1 Y 1 B ASP 184 ? OD2 ? B ASP 195 OD2 
142 1 Y 1 B ASP 191 ? CG  ? B ASP 202 CG  
143 1 Y 1 B ASP 191 ? OD1 ? B ASP 202 OD1 
144 1 Y 1 B ASP 191 ? OD2 ? B ASP 202 OD2 
145 1 Y 1 B LEU 193 ? CG  ? B LEU 204 CG  
146 1 Y 1 B LEU 193 ? CD1 ? B LEU 204 CD1 
147 1 Y 1 B LEU 193 ? CD2 ? B LEU 204 CD2 
148 1 Y 1 B THR 197 ? OG1 ? B THR 208 OG1 
149 1 Y 1 B THR 197 ? CG2 ? B THR 208 CG2 
150 1 Y 1 B ARG 198 ? CG  ? B ARG 209 CG  
151 1 Y 1 B ARG 198 ? CD  ? B ARG 209 CD  
152 1 Y 1 B ARG 198 ? NE  ? B ARG 209 NE  
153 1 Y 1 B ARG 198 ? CZ  ? B ARG 209 CZ  
154 1 Y 1 B ARG 198 ? NH1 ? B ARG 209 NH1 
155 1 Y 1 B ARG 198 ? NH2 ? B ARG 209 NH2 
156 1 Y 1 B ARG 201 ? CG  ? B ARG 212 CG  
157 1 Y 1 B ARG 201 ? CD  ? B ARG 212 CD  
158 1 Y 1 B ARG 201 ? NE  ? B ARG 212 NE  
159 1 Y 1 B ARG 201 ? CZ  ? B ARG 212 CZ  
160 1 Y 1 B ARG 201 ? NH1 ? B ARG 212 NH1 
161 1 Y 1 B ARG 201 ? NH2 ? B ARG 212 NH2 
162 1 Y 1 B ARG 205 ? CG  ? B ARG 216 CG  
163 1 Y 1 B ARG 205 ? CD  ? B ARG 216 CD  
164 1 Y 1 B ARG 205 ? NE  ? B ARG 216 NE  
165 1 Y 1 B ARG 205 ? CZ  ? B ARG 216 CZ  
166 1 Y 1 B ARG 205 ? NH1 ? B ARG 216 NH1 
167 1 Y 1 B ARG 205 ? NH2 ? B ARG 216 NH2 
168 1 Y 1 B LYS 206 ? CG  ? B LYS 217 CG  
169 1 Y 1 B LYS 206 ? CD  ? B LYS 217 CD  
170 1 Y 1 B LYS 206 ? CE  ? B LYS 217 CE  
171 1 Y 1 B LYS 206 ? NZ  ? B LYS 217 NZ  
172 1 Y 1 B ASP 217 ? CG  ? B ASP 228 CG  
173 1 Y 1 B ASP 217 ? OD1 ? B ASP 228 OD1 
174 1 Y 1 B ASP 217 ? OD2 ? B ASP 228 OD2 
175 1 Y 1 B GLU 228 ? CG  ? B GLU 239 CG  
176 1 Y 1 B GLU 228 ? CD  ? B GLU 239 CD  
177 1 Y 1 B GLU 228 ? OE1 ? B GLU 239 OE1 
178 1 Y 1 B GLU 228 ? OE2 ? B GLU 239 OE2 
179 1 Y 1 B GLU 234 ? CG  ? B GLU 245 CG  
180 1 Y 1 B GLU 234 ? CD  ? B GLU 245 CD  
181 1 Y 1 B GLU 234 ? OE1 ? B GLU 245 OE1 
182 1 Y 1 B GLU 234 ? OE2 ? B GLU 245 OE2 
183 1 Y 1 B ASP 264 ? CG  ? B ASP 275 CG  
184 1 Y 1 B ASP 264 ? OD1 ? B ASP 275 OD1 
185 1 Y 1 B ASP 264 ? OD2 ? B ASP 275 OD2 
186 1 Y 1 B VAL 268 ? CG1 ? B VAL 279 CG1 
187 1 Y 1 B VAL 268 ? CG2 ? B VAL 279 CG2 
188 1 Y 1 B ASP 286 ? CG  ? B ASP 297 CG  
189 1 Y 1 B ASP 286 ? OD1 ? B ASP 297 OD1 
190 1 Y 1 B ASP 286 ? OD2 ? B ASP 297 OD2 
191 1 Y 1 B GLU 289 ? CG  ? B GLU 300 CG  
192 1 Y 1 B GLU 289 ? CD  ? B GLU 300 CD  
193 1 Y 1 B GLU 289 ? OE1 ? B GLU 300 OE1 
194 1 Y 1 B GLU 289 ? OE2 ? B GLU 300 OE2 
195 1 Y 1 B GLU 292 ? CG  ? B GLU 303 CG  
196 1 Y 1 B GLU 292 ? CD  ? B GLU 303 CD  
197 1 Y 1 B GLU 292 ? OE1 ? B GLU 303 OE1 
198 1 Y 1 B GLU 292 ? OE2 ? B GLU 303 OE2 
199 1 Y 1 B GLU 303 ? CG  ? B GLU 314 CG  
200 1 Y 1 B GLU 303 ? CD  ? B GLU 314 CD  
201 1 Y 1 B GLU 303 ? OE1 ? B GLU 314 OE1 
202 1 Y 1 B GLU 303 ? OE2 ? B GLU 314 OE2 
203 1 Y 1 B ASN 306 ? CG  ? B ASN 317 CG  
204 1 Y 1 B ASN 306 ? OD1 ? B ASN 317 OD1 
205 1 Y 1 B ASN 306 ? ND2 ? B ASN 317 ND2 
206 1 Y 1 B GLU 310 ? CG  ? B GLU 321 CG  
207 1 Y 1 B GLU 310 ? CD  ? B GLU 321 CD  
208 1 Y 1 B GLU 310 ? OE1 ? B GLU 321 OE1 
209 1 Y 1 B GLU 310 ? OE2 ? B GLU 321 OE2 
210 1 Y 1 B ASP 311 ? CG  ? B ASP 322 CG  
211 1 Y 1 B ASP 311 ? OD1 ? B ASP 322 OD1 
212 1 Y 1 B ASP 311 ? OD2 ? B ASP 322 OD2 
213 1 Y 1 B GLU 346 ? CG  ? B GLU 357 CG  
214 1 Y 1 B GLU 346 ? CD  ? B GLU 357 CD  
215 1 Y 1 B GLU 346 ? OE1 ? B GLU 357 OE1 
216 1 Y 1 B GLU 346 ? OE2 ? B GLU 357 OE2 
217 1 Y 1 B GLU 384 ? CG  ? B GLU 395 CG  
218 1 Y 1 B GLU 384 ? CD  ? B GLU 395 CD  
219 1 Y 1 B GLU 384 ? OE1 ? B GLU 395 OE1 
220 1 Y 1 B GLU 384 ? OE2 ? B GLU 395 OE2 
221 1 Y 1 B ASN 385 ? CG  ? B ASN 396 CG  
222 1 Y 1 B ASN 385 ? OD1 ? B ASN 396 OD1 
223 1 Y 1 B ASN 385 ? ND2 ? B ASN 396 ND2 
224 1 Y 1 B SER 405 ? OG  ? B SER 416 OG  
225 1 Y 1 B LYS 408 ? CG  ? B LYS 419 CG  
226 1 Y 1 B LYS 408 ? CD  ? B LYS 419 CD  
227 1 Y 1 B LYS 408 ? CE  ? B LYS 419 CE  
228 1 Y 1 B LYS 408 ? NZ  ? B LYS 419 NZ  
229 1 Y 1 B ASN 410 ? CG  ? B ASN 421 CG  
230 1 Y 1 B ASN 410 ? OD1 ? B ASN 421 OD1 
231 1 Y 1 B ASN 410 ? ND2 ? B ASN 421 ND2 
232 1 Y 1 B ILE 420 ? CG1 ? B ILE 431 CG1 
233 1 Y 1 B ILE 420 ? CG2 ? B ILE 431 CG2 
234 1 Y 1 B ILE 420 ? CD1 ? B ILE 431 CD1 
235 1 Y 1 B LYS 422 ? CG  ? B LYS 433 CG  
236 1 Y 1 B LYS 422 ? CD  ? B LYS 433 CD  
237 1 Y 1 B LYS 422 ? CE  ? B LYS 433 CE  
238 1 Y 1 B LYS 422 ? NZ  ? B LYS 433 NZ  
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BCN 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     1.00 
_cell.length_a_esd                 ? 
_cell.length_b                     1.00 
_cell.length_b_esd                 ? 
_cell.length_c                     1.00 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        ? 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9BCN 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9BCN 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9BCN 
_struct.title                        'Extracellular domain of apo GC-A, state 2' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9BCN 
_struct_keywords.text            
'Single pass transmembrane protein, guanylyl cyclase, atrial natriuretic peptide receptor, hypertension, membrane protein, LYASE' 
_struct_keywords.pdbx_keywords   LYASE 
# 
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 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 3 ? 
H N N 4 ? 
I N N 3 ? 
J N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    ANPRA_HUMAN 
_struct_ref.pdbx_db_accession          P16066 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;AGNLTVAVVLPLANTSYPWSWARVGPAVELALAQVKARPDLLPGWTVRTVLGSSENALGVCSDTAAPLAAVDLKWEHNPA
VFLGPGCVYAAAPVGRFTAHWRVPLLTAGAPALGFGVKDEYALTTRAGPSYAKLGDFVAALHRRLGWERQALMLYAYRPG
DEEHCFFLVEGLFMRVRDRLNITVDHLEFAEDDLSHYTRLLRTMPRKGRVIYICSSPDAFRTLMLLALEAGLCGEDYVFF
HLDIFGQSLQGGQGPAPRRPWERGDGQDVSARQAFQAAKIITYKDPDNPEYLEFLKQLKHLAYEQFNFTMEDGLVNTIPA
SFHDGLLLYIQAVTETLAHGGTVTDGENITQRMWNRSFQGVTGYLKIDSSGDRETDFSLWDMDPENGAFRVVLNYNGTSQ
ELVAVSGRKLNWPLGYPPPDIPKCGFDNEDPACNQDHLSTLEVLALVGSLSLLGILIVSFFIYRKMQLEKELASELWRVR
WEDVEPSSLERHLRSAGSRLTLSGRGSNYGSLLTTEGQFQVFAKTAYYKGNLVAVKRVNRKRIELTRKVLFELKHMRDVQ
NEHLTRFVGACTDPPNICILTEYCPRGSLQDILENESITLDWMFRYSLTNDIVKGMLFLHNGAICSHGNLKSSNCVVDGR
FVLKITDYGLESFRDLDPEQGHTVYAKKLWTAPELLRMASPPVRGSQAGDVYSFGIILQEIALRSGVFHVEGLDLSPKEI
IERVTRGEQPPFRPSLALQSHLEELGLLMQRCWAEDPQERPPFQQIRLTLRKFNRENSSNILDNLLSRMEQYANNLEELV
EERTQAYLEEKRKAEALLYQILPHSVAEQLKRGETVQAEAFDSVTIYFSDIVGFTALSAESTPMQVVTLLNDLYTCFDAV
IDNFDVYKVETIGDAYMVVSGLPVRNGRLHACEVARMALALLDAVRSFRIRHRPQEQLRLRIGIHTGPVCAGVVGLKMPR
YCLFGDTVNTASRMESNGEALKIHLSSETKAVLEEFGGFELELRGDVEMKGKGKVRTYWLLGERGSSTRG
;
_struct_ref.pdbx_align_begin           32 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9BCN A 11 ? 1040 ? P16066 32 ? 1061 ? 0 1029 
2 1 9BCN B 11 ? 1040 ? P16066 32 ? 1061 ? 0 1029 
# 
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 9BCN ASP A 1  ? UNP P16066 ? ? 'expression tag' -10 1  
1 9BCN TYR A 2  ? UNP P16066 ? ? 'expression tag' -9  2  
1 9BCN LYS A 3  ? UNP P16066 ? ? 'expression tag' -8  3  
1 9BCN ASP A 4  ? UNP P16066 ? ? 'expression tag' -7  4  
1 9BCN ASP A 5  ? UNP P16066 ? ? 'expression tag' -6  5  
1 9BCN ASP A 6  ? UNP P16066 ? ? 'expression tag' -5  6  
1 9BCN ASP A 7  ? UNP P16066 ? ? 'expression tag' -4  7  
1 9BCN LYS A 8  ? UNP P16066 ? ? 'expression tag' -3  8  
1 9BCN ALA A 9  ? UNP P16066 ? ? 'expression tag' -2  9  
1 9BCN ALA A 10 ? UNP P16066 ? ? 'expression tag' -1  10 
2 9BCN ASP B 1  ? UNP P16066 ? ? 'expression tag' -10 11 
2 9BCN TYR B 2  ? UNP P16066 ? ? 'expression tag' -9  12 
2 9BCN LYS B 3  ? UNP P16066 ? ? 'expression tag' -8  13 
2 9BCN ASP B 4  ? UNP P16066 ? ? 'expression tag' -7  14 
2 9BCN ASP B 5  ? UNP P16066 ? ? 'expression tag' -6  15 
2 9BCN ASP B 6  ? UNP P16066 ? ? 'expression tag' -5  16 
2 9BCN ASP B 7  ? UNP P16066 ? ? 'expression tag' -4  17 
2 9BCN LYS B 8  ? UNP P16066 ? ? 'expression tag' -3  18 
2 9BCN ALA B 9  ? UNP P16066 ? ? 'expression tag' -2  19 
2 9BCN ALA B 10 ? UNP P16066 ? ? 'expression tag' -1  20 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   ? 
_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_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 30  ? ARG A 48  ? SER A 19  ARG A 37  1 ? 19 
HELX_P HELX_P2  AA2 ALA A 75  ? ASN A 88  ? ALA A 64  ASN A 77  1 ? 14 
HELX_P HELX_P3  AA3 CYS A 97  ? ARG A 112 ? CYS A 86  ARG A 101 1 ? 16 
HELX_P HELX_P4  AA4 ALA A 122 ? VAL A 127 ? ALA A 111 VAL A 116 5 ? 6  
HELX_P HELX_P5  AA5 SER A 140 ? GLY A 156 ? SER A 129 GLY A 145 1 ? 17 
HELX_P HELX_P6  AA6 GLU A 173 ? ARG A 189 ? GLU A 162 ARG A 178 1 ? 17 
HELX_P HELX_P7  AA7 ASP A 203 ? MET A 214 ? ASP A 192 MET A 203 1 ? 12 
HELX_P HELX_P8  AA8 SER A 226 ? ALA A 240 ? SER A 215 ALA A 229 1 ? 15 
HELX_P HELX_P9  AA9 GLY A 256 ? GLN A 260 ? GLY A 245 GLN A 249 5 ? 5  
HELX_P HELX_P10 AB1 ASP A 278 ? PHE A 285 ? ASP A 267 PHE A 274 1 ? 8  
HELX_P HELX_P11 AB2 ASN A 298 ? ASN A 317 ? ASN A 287 ASN A 306 1 ? 20 
HELX_P HELX_P12 AB3 ASN A 326 ? LEU A 347 ? ASN A 315 LEU A 336 1 ? 22 
HELX_P HELX_P13 AB4 ALA A 348 ? GLY A 350 ? ALA A 337 GLY A 339 5 ? 3  
HELX_P HELX_P14 AB5 ASP A 355 ? GLN A 361 ? ASP A 344 GLN A 350 1 ? 7  
HELX_P HELX_P15 AB6 SER B 30  ? ARG B 48  ? SER B 19  ARG B 37  1 ? 19 
HELX_P HELX_P16 AB7 ALA B 75  ? ASN B 88  ? ALA B 64  ASN B 77  1 ? 14 
HELX_P HELX_P17 AB8 CYS B 97  ? ARG B 112 ? CYS B 86  ARG B 101 1 ? 16 
HELX_P HELX_P18 AB9 LEU B 123 ? VAL B 127 ? LEU B 112 VAL B 116 5 ? 5  
HELX_P HELX_P19 AC1 TYR B 141 ? GLY B 156 ? TYR B 130 GLY B 145 1 ? 16 
HELX_P HELX_P20 AC2 GLU B 173 ? LEU B 190 ? GLU B 162 LEU B 179 1 ? 18 
HELX_P HELX_P21 AC3 SER B 205 ? THR B 213 ? SER B 194 THR B 202 1 ? 9  
HELX_P HELX_P22 AC4 THR B 213 ? GLY B 218 ? THR B 202 GLY B 207 1 ? 6  
HELX_P HELX_P23 AC5 SER B 226 ? ALA B 240 ? SER B 215 ALA B 229 1 ? 15 
HELX_P HELX_P24 AC6 GLY B 256 ? GLN B 260 ? GLY B 245 GLN B 249 5 ? 5  
HELX_P HELX_P25 AC7 ASP B 278 ? PHE B 285 ? ASP B 267 PHE B 274 1 ? 8  
HELX_P HELX_P26 AC8 ASN B 298 ? ASN B 317 ? ASN B 287 ASN B 306 1 ? 20 
HELX_P HELX_P27 AC9 ASN B 326 ? HIS B 349 ? ASN B 315 HIS B 338 1 ? 24 
HELX_P HELX_P28 AD1 ASP B 355 ? GLN B 361 ? ASP B 344 GLN B 350 1 ? 7  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ?    ? A CYS 71  SG  ? ? ? 1_555 A CYS 97  SG ? ? A CYS 60  A CYS 86   1_555 ? ? ? ? ? ? ? 2.033 ? ?               
disulf2  disulf ?    ? A CYS 175 SG  ? ? ? 1_555 A CYS 224 SG ? ? A CYS 164 A CYS 213  1_555 ? ? ? ? ? ? ? 2.037 ? ?               
disulf3  disulf ?    ? B CYS 71  SG  ? ? ? 1_555 B CYS 97  SG ? ? B CYS 60  B CYS 86   1_555 ? ? ? ? ? ? ? 2.034 ? ?               
disulf4  disulf ?    ? B CYS 175 SG  ? ? ? 1_555 B CYS 224 SG ? ? B CYS 164 B CYS 213  1_555 ? ? ? ? ? ? ? 2.037 ? ?               
covale1  covale one  ? A ASN 24  ND2 ? ? ? 1_555 C NAG .   C1 ? ? A ASN 13  C NAG 1    1_555 ? ? ? ? ? ? ? 1.439 ? N-Glycosylation 
covale2  covale one  ? A ASN 365 ND2 ? ? ? 1_555 H NAG .   C1 ? ? A ASN 354 A NAG 1102 1_555 ? ? ? ? ? ? ? 1.398 ? N-Glycosylation 
covale3  covale one  ? A ASN 406 ND2 ? ? ? 1_555 D NAG .   C1 ? ? A ASN 395 D NAG 1    1_555 ? ? ? ? ? ? ? 1.449 ? N-Glycosylation 
covale4  covale one  ? B ASN 24  ND2 ? ? ? 1_555 E NAG .   C1 ? ? B ASN 13  E NAG 1    1_555 ? ? ? ? ? ? ? 1.440 ? N-Glycosylation 
covale5  covale one  ? B ASN 365 ND2 ? ? ? 1_555 J NAG .   C1 ? ? B ASN 354 B NAG 1102 1_555 ? ? ? ? ? ? ? 1.419 ? N-Glycosylation 
covale6  covale one  ? B ASN 406 ND2 ? ? ? 1_555 F NAG .   C1 ? ? B ASN 395 F NAG 1    1_555 ? ? ? ? ? ? ? 1.453 ? N-Glycosylation 
covale7  covale both ? C NAG .   O4  ? ? ? 1_555 C NAG .   C1 ? ? C NAG 1   C NAG 2    1_555 ? ? ? ? ? ? ? 1.458 ? ?               
covale8  covale both ? C NAG .   O3  ? ? ? 1_555 C MAN .   C1 ? ? C NAG 2   C MAN 3    1_555 ? ? ? ? ? ? ? 1.448 ? ?               
covale9  covale both ? D NAG .   O4  ? ? ? 1_555 D NAG .   C1 ? ? D NAG 1   D NAG 2    1_555 ? ? ? ? ? ? ? 1.434 ? ?               
covale10 covale both ? D NAG .   O3  ? ? ? 1_555 D MAN .   C1 ? ? D NAG 2   D MAN 3    1_555 ? ? ? ? ? ? ? 1.448 ? ?               
covale11 covale both ? E NAG .   O4  ? ? ? 1_555 E NAG .   C1 ? ? E NAG 1   E NAG 2    1_555 ? ? ? ? ? ? ? 1.459 ? ?               
covale12 covale both ? E NAG .   O3  ? ? ? 1_555 E MAN .   C1 ? ? E NAG 2   E MAN 3    1_555 ? ? ? ? ? ? ? 1.452 ? ?               
covale13 covale both ? F NAG .   O4  ? ? ? 1_555 F NAG .   C1 ? ? F NAG 1   F NAG 2    1_555 ? ? ? ? ? ? ? 1.436 ? ?               
covale14 covale both ? F NAG .   O3  ? ? ? 1_555 F MAN .   C1 ? ? F NAG 2   F MAN 3    1_555 ? ? ? ? ? ? ? 1.448 ? ?               
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1  NAG C .   ? ASN A 24  ? NAG C 1    ? 1_555 ASN A 13  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2  NAG D .   ? ASN A 406 ? NAG D 1    ? 1_555 ASN A 395 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3  NAG E .   ? ASN B 24  ? NAG E 1    ? 1_555 ASN B 13  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
4  NAG F .   ? ASN B 406 ? NAG F 1    ? 1_555 ASN B 395 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
5  NAG H .   ? ASN A 365 ? NAG A 1102 ? 1_555 ASN A 354 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
6  NAG J .   ? ASN B 365 ? NAG B 1102 ? 1_555 ASN B 354 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
7  CYS A 71  ? CYS A 97  ? CYS A 60   ? 1_555 CYS A 86  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
8  CYS A 175 ? CYS A 224 ? CYS A 164  ? 1_555 CYS A 213 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
9  CYS B 71  ? CYS B 97  ? CYS B 60   ? 1_555 CYS B 86  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
10 CYS B 175 ? CYS B 224 ? CYS B 164  ? 1_555 CYS B 213 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 8 ? 
AA3 ? 2 ? 
AA4 ? 3 ? 
AA5 ? 2 ? 
AA6 ? 8 ? 
AA7 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA2 7 8 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA5 1 2 ? parallel      
AA6 1 2 ? parallel      
AA6 2 3 ? parallel      
AA6 3 4 ? parallel      
AA6 4 5 ? parallel      
AA6 5 6 ? anti-parallel 
AA6 6 7 ? anti-parallel 
AA6 7 8 ? anti-parallel 
AA7 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 56  ? SER A 63  ? THR A 45  SER A 52  
AA1 2 ASN A 13  ? LEU A 20  ? ASN A 2   LEU A 9   
AA1 3 VAL A 91  ? LEU A 93  ? VAL A 80  LEU A 82  
AA1 4 LEU A 115 ? THR A 117 ? LEU A 104 THR A 106 
AA1 5 THR A 134 ? ARG A 136 ? THR A 123 ARG A 125 
AA2 1 THR A 193 ? ALA A 200 ? THR A 182 ALA A 189 
AA2 2 GLN A 160 ? TYR A 167 ? GLN A 149 TYR A 156 
AA2 3 VAL A 220 ? CYS A 224 ? VAL A 209 CYS A 213 
AA2 4 VAL A 248 ? LEU A 252 ? VAL A 237 LEU A 241 
AA2 5 ALA A 288 ? TYR A 293 ? ALA A 277 TYR A 282 
AA2 6 PHE A 387 ? MET A 392 ? PHE A 376 MET A 381 
AA2 7 PHE A 399 ? ASN A 406 ? PHE A 388 ASN A 395 
AA2 8 GLU A 411 ? ALA A 414 ? GLU A 400 ALA A 403 
AA3 1 SER A 367 ? GLY A 370 ? SER A 356 GLY A 359 
AA3 2 GLY A 373 ? LYS A 376 ? GLY A 362 LYS A 365 
AA4 1 THR B 56  ? SER B 63  ? THR B 45  SER B 52  
AA4 2 ASN B 13  ? LEU B 20  ? ASN B 2   LEU B 9   
AA4 3 VAL B 91  ? LEU B 93  ? VAL B 80  LEU B 82  
AA5 1 LEU B 115 ? THR B 117 ? LEU B 104 THR B 106 
AA5 2 THR B 134 ? ARG B 136 ? THR B 123 ARG B 125 
AA6 1 THR B 193 ? ALA B 200 ? THR B 182 ALA B 189 
AA6 2 GLN B 160 ? TYR B 167 ? GLN B 149 TYR B 156 
AA6 3 ILE B 221 ? ILE B 223 ? ILE B 210 ILE B 212 
AA6 4 PHE B 249 ? LEU B 252 ? PHE B 238 LEU B 241 
AA6 5 ALA B 288 ? TYR B 293 ? ALA B 277 TYR B 282 
AA6 6 PHE B 387 ? ASP B 391 ? PHE B 376 ASP B 380 
AA6 7 ARG B 400 ? ASN B 406 ? ARG B 389 ASN B 395 
AA6 8 GLU B 411 ? ALA B 414 ? GLU B 400 ALA B 403 
AA7 1 ARG B 366 ? GLY B 370 ? ARG B 355 GLY B 359 
AA7 2 GLY B 373 ? ILE B 377 ? GLY B 362 ILE B 366 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O THR A 56  ? O THR A 45  N LEU A 14  ? N LEU A 3   
AA1 2 3 N ALA A 17  ? N ALA A 6   O LEU A 93  ? O LEU A 82  
AA1 3 4 N PHE A 92  ? N PHE A 81  O LEU A 116 ? O LEU A 105 
AA1 4 5 N LEU A 115 ? N LEU A 104 O THR A 135 ? O THR A 124 
AA2 1 2 O ASP A 195 ? O ASP A 184 N MET A 163 ? N MET A 152 
AA2 2 3 N ALA A 166 ? N ALA A 155 O CYS A 224 ? O CYS A 213 
AA2 3 4 N ILE A 221 ? N ILE A 210 O PHE A 250 ? O PHE A 239 
AA2 4 5 N HIS A 251 ? N HIS A 240 O ILE A 291 ? O ILE A 280 
AA2 5 6 N ILE A 290 ? N ILE A 279 O TRP A 390 ? O TRP A 379 
AA2 6 7 N LEU A 389 ? N LEU A 378 O VAL A 402 ? O VAL A 391 
AA2 7 8 N ASN A 404 ? N ASN A 393 O VAL A 413 ? O VAL A 402 
AA3 1 2 N GLY A 370 ? N GLY A 359 O GLY A 373 ? O GLY A 362 
AA4 1 2 O ARG B 58  ? O ARG B 47  N VAL B 16  ? N VAL B 5   
AA4 2 3 N ALA B 17  ? N ALA B 6   O LEU B 93  ? O LEU B 82  
AA5 1 2 N LEU B 115 ? N LEU B 104 O THR B 135 ? O THR B 124 
AA6 1 2 O ASP B 195 ? O ASP B 184 N MET B 163 ? N MET B 152 
AA6 2 3 N LEU B 164 ? N LEU B 153 O TYR B 222 ? O TYR B 211 
AA6 3 4 N ILE B 223 ? N ILE B 212 O LEU B 252 ? O LEU B 241 
AA6 4 5 N HIS B 251 ? N HIS B 240 O ILE B 291 ? O ILE B 280 
AA6 5 6 N ILE B 290 ? N ILE B 279 O TRP B 390 ? O TRP B 379 
AA6 6 7 N LEU B 389 ? N LEU B 378 O VAL B 402 ? O VAL B 391 
AA6 7 8 N ASN B 406 ? N ASN B 395 O GLU B 411 ? O GLU B 400 
AA7 1 2 N PHE B 368 ? N PHE B 357 O LEU B 375 ? O LEU B 364 
# 
_pdbx_entry_details.entry_id                   9BCN 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   PRO 
_pdbx_validate_close_contact.auth_seq_id_1    204 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   NH2 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   ARG 
_pdbx_validate_close_contact.auth_seq_id_2    208 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.16 
# 
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 LEU A 41  ? ? 39.72   68.97   
2  1 ASN A 77  ? ? 61.77   68.37   
3  1 LYS A 117 ? ? -67.28  0.58    
4  1 TYR A 120 ? ? -100.34 75.00   
5  1 GLU A 147 ? ? -141.50 25.23   
6  1 GLU A 162 ? ? 32.22   66.25   
7  1 ASN A 180 ? ? -91.90  59.02   
8  1 ALA A 229 ? ? -75.17  -166.87 
9  1 LEU B 41  ? ? 39.58   64.97   
10 1 CYS B 60  ? ? -47.11  152.18  
11 1 ASN B 77  ? ? 61.67   67.48   
12 1 LYS B 117 ? ? -69.13  2.21    
13 1 ASN B 180 ? ? -92.80  58.17   
14 1 SER B 214 ? ? -59.81  176.27  
15 1 ASP B 235 ? ? -121.24 -50.86  
16 1 GLN B 399 ? ? 61.37   62.44   
17 1 VAL B 404 ? ? -91.01  -64.11  
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9BCN 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         ? 
_em_3d_fitting.ref_protocol      ? 
# 
_em_3d_reconstruction.entry_id                    9BCN 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  2.9 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               162825 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       ? 
_em_buffer.pH            8 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'Atrial natriuretic peptide receptor 1 dimer' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        9BCN 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'FEI TITAN KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           ? 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             1500 
_em_imaging.nominal_defocus_max             2000 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           ? 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         ? 
# 
_em_vitrification.entry_id              9BCN 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              ? 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   ? 
_em_vitrification.instrument            ? 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9BCN 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1    1 Y 1 A ASP -10  ? A ASP 1    
2    1 Y 1 A TYR -9   ? A TYR 2    
3    1 Y 1 A LYS -8   ? A LYS 3    
4    1 Y 1 A ASP -7   ? A ASP 4    
5    1 Y 1 A ASP -6   ? A ASP 5    
6    1 Y 1 A ASP -5   ? A ASP 6    
7    1 Y 1 A ASP -4   ? A ASP 7    
8    1 Y 1 A LYS -3   ? A LYS 8    
9    1 Y 1 A ALA -2   ? A ALA 9    
10   1 Y 1 A ALA -1   ? A ALA 10   
11   1 Y 1 A ALA 0    ? A ALA 11   
12   1 Y 1 A ASP 426  ? A ASP 437  
13   1 Y 1 A ASN 427  ? A ASN 438  
14   1 Y 1 A GLU 428  ? A GLU 439  
15   1 Y 1 A ASP 429  ? A ASP 440  
16   1 Y 1 A PRO 430  ? A PRO 441  
17   1 Y 1 A ALA 431  ? A ALA 442  
18   1 Y 1 A CYS 432  ? A CYS 443  
19   1 Y 1 A ASN 433  ? A ASN 444  
20   1 Y 1 A GLN 434  ? A GLN 445  
21   1 Y 1 A ASP 435  ? A ASP 446  
22   1 Y 1 A HIS 436  ? A HIS 447  
23   1 Y 1 A LEU 437  ? A LEU 448  
24   1 Y 1 A SER 438  ? A SER 449  
25   1 Y 1 A THR 439  ? A THR 450  
26   1 Y 1 A LEU 440  ? A LEU 451  
27   1 Y 1 A GLU 441  ? A GLU 452  
28   1 Y 1 A VAL 442  ? A VAL 453  
29   1 Y 1 A LEU 443  ? A LEU 454  
30   1 Y 1 A ALA 444  ? A ALA 455  
31   1 Y 1 A LEU 445  ? A LEU 456  
32   1 Y 1 A VAL 446  ? A VAL 457  
33   1 Y 1 A GLY 447  ? A GLY 458  
34   1 Y 1 A SER 448  ? A SER 459  
35   1 Y 1 A LEU 449  ? A LEU 460  
36   1 Y 1 A SER 450  ? A SER 461  
37   1 Y 1 A LEU 451  ? A LEU 462  
38   1 Y 1 A LEU 452  ? A LEU 463  
39   1 Y 1 A GLY 453  ? A GLY 464  
40   1 Y 1 A ILE 454  ? A ILE 465  
41   1 Y 1 A LEU 455  ? A LEU 466  
42   1 Y 1 A ILE 456  ? A ILE 467  
43   1 Y 1 A VAL 457  ? A VAL 468  
44   1 Y 1 A SER 458  ? A SER 469  
45   1 Y 1 A PHE 459  ? A PHE 470  
46   1 Y 1 A PHE 460  ? A PHE 471  
47   1 Y 1 A ILE 461  ? A ILE 472  
48   1 Y 1 A TYR 462  ? A TYR 473  
49   1 Y 1 A ARG 463  ? A ARG 474  
50   1 Y 1 A LYS 464  ? A LYS 475  
51   1 Y 1 A MET 465  ? A MET 476  
52   1 Y 1 A GLN 466  ? A GLN 477  
53   1 Y 1 A LEU 467  ? A LEU 478  
54   1 Y 1 A GLU 468  ? A GLU 479  
55   1 Y 1 A LYS 469  ? A LYS 480  
56   1 Y 1 A GLU 470  ? A GLU 481  
57   1 Y 1 A LEU 471  ? A LEU 482  
58   1 Y 1 A ALA 472  ? A ALA 483  
59   1 Y 1 A SER 473  ? A SER 484  
60   1 Y 1 A GLU 474  ? A GLU 485  
61   1 Y 1 A LEU 475  ? A LEU 486  
62   1 Y 1 A TRP 476  ? A TRP 487  
63   1 Y 1 A ARG 477  ? A ARG 488  
64   1 Y 1 A VAL 478  ? A VAL 489  
65   1 Y 1 A ARG 479  ? A ARG 490  
66   1 Y 1 A TRP 480  ? A TRP 491  
67   1 Y 1 A GLU 481  ? A GLU 492  
68   1 Y 1 A ASP 482  ? A ASP 493  
69   1 Y 1 A VAL 483  ? A VAL 494  
70   1 Y 1 A GLU 484  ? A GLU 495  
71   1 Y 1 A PRO 485  ? A PRO 496  
72   1 Y 1 A SER 486  ? A SER 497  
73   1 Y 1 A SER 487  ? A SER 498  
74   1 Y 1 A LEU 488  ? A LEU 499  
75   1 Y 1 A GLU 489  ? A GLU 500  
76   1 Y 1 A ARG 490  ? A ARG 501  
77   1 Y 1 A HIS 491  ? A HIS 502  
78   1 Y 1 A LEU 492  ? A LEU 503  
79   1 Y 1 A ARG 493  ? A ARG 504  
80   1 Y 1 A SER 494  ? A SER 505  
81   1 Y 1 A ALA 495  ? A ALA 506  
82   1 Y 1 A GLY 496  ? A GLY 507  
83   1 Y 1 A SER 497  ? A SER 508  
84   1 Y 1 A ARG 498  ? A ARG 509  
85   1 Y 1 A LEU 499  ? A LEU 510  
86   1 Y 1 A THR 500  ? A THR 511  
87   1 Y 1 A LEU 501  ? A LEU 512  
88   1 Y 1 A SER 502  ? A SER 513  
89   1 Y 1 A GLY 503  ? A GLY 514  
90   1 Y 1 A ARG 504  ? A ARG 515  
91   1 Y 1 A GLY 505  ? A GLY 516  
92   1 Y 1 A SER 506  ? A SER 517  
93   1 Y 1 A ASN 507  ? A ASN 518  
94   1 Y 1 A TYR 508  ? A TYR 519  
95   1 Y 1 A GLY 509  ? A GLY 520  
96   1 Y 1 A SER 510  ? A SER 521  
97   1 Y 1 A LEU 511  ? A LEU 522  
98   1 Y 1 A LEU 512  ? A LEU 523  
99   1 Y 1 A THR 513  ? A THR 524  
100  1 Y 1 A THR 514  ? A THR 525  
101  1 Y 1 A GLU 515  ? A GLU 526  
102  1 Y 1 A GLY 516  ? A GLY 527  
103  1 Y 1 A GLN 517  ? A GLN 528  
104  1 Y 1 A PHE 518  ? A PHE 529  
105  1 Y 1 A GLN 519  ? A GLN 530  
106  1 Y 1 A VAL 520  ? A VAL 531  
107  1 Y 1 A PHE 521  ? A PHE 532  
108  1 Y 1 A ALA 522  ? A ALA 533  
109  1 Y 1 A LYS 523  ? A LYS 534  
110  1 Y 1 A THR 524  ? A THR 535  
111  1 Y 1 A ALA 525  ? A ALA 536  
112  1 Y 1 A TYR 526  ? A TYR 537  
113  1 Y 1 A TYR 527  ? A TYR 538  
114  1 Y 1 A LYS 528  ? A LYS 539  
115  1 Y 1 A GLY 529  ? A GLY 540  
116  1 Y 1 A ASN 530  ? A ASN 541  
117  1 Y 1 A LEU 531  ? A LEU 542  
118  1 Y 1 A VAL 532  ? A VAL 543  
119  1 Y 1 A ALA 533  ? A ALA 544  
120  1 Y 1 A VAL 534  ? A VAL 545  
121  1 Y 1 A LYS 535  ? A LYS 546  
122  1 Y 1 A ARG 536  ? A ARG 547  
123  1 Y 1 A VAL 537  ? A VAL 548  
124  1 Y 1 A ASN 538  ? A ASN 549  
125  1 Y 1 A ARG 539  ? A ARG 550  
126  1 Y 1 A LYS 540  ? A LYS 551  
127  1 Y 1 A ARG 541  ? A ARG 552  
128  1 Y 1 A ILE 542  ? A ILE 553  
129  1 Y 1 A GLU 543  ? A GLU 554  
130  1 Y 1 A LEU 544  ? A LEU 555  
131  1 Y 1 A THR 545  ? A THR 556  
132  1 Y 1 A ARG 546  ? A ARG 557  
133  1 Y 1 A LYS 547  ? A LYS 558  
134  1 Y 1 A VAL 548  ? A VAL 559  
135  1 Y 1 A LEU 549  ? A LEU 560  
136  1 Y 1 A PHE 550  ? A PHE 561  
137  1 Y 1 A GLU 551  ? A GLU 562  
138  1 Y 1 A LEU 552  ? A LEU 563  
139  1 Y 1 A LYS 553  ? A LYS 564  
140  1 Y 1 A HIS 554  ? A HIS 565  
141  1 Y 1 A MET 555  ? A MET 566  
142  1 Y 1 A ARG 556  ? A ARG 567  
143  1 Y 1 A ASP 557  ? A ASP 568  
144  1 Y 1 A VAL 558  ? A VAL 569  
145  1 Y 1 A GLN 559  ? A GLN 570  
146  1 Y 1 A ASN 560  ? A ASN 571  
147  1 Y 1 A GLU 561  ? A GLU 572  
148  1 Y 1 A HIS 562  ? A HIS 573  
149  1 Y 1 A LEU 563  ? A LEU 574  
150  1 Y 1 A THR 564  ? A THR 575  
151  1 Y 1 A ARG 565  ? A ARG 576  
152  1 Y 1 A PHE 566  ? A PHE 577  
153  1 Y 1 A VAL 567  ? A VAL 578  
154  1 Y 1 A GLY 568  ? A GLY 579  
155  1 Y 1 A ALA 569  ? A ALA 580  
156  1 Y 1 A CYS 570  ? A CYS 581  
157  1 Y 1 A THR 571  ? A THR 582  
158  1 Y 1 A ASP 572  ? A ASP 583  
159  1 Y 1 A PRO 573  ? A PRO 584  
160  1 Y 1 A PRO 574  ? A PRO 585  
161  1 Y 1 A ASN 575  ? A ASN 586  
162  1 Y 1 A ILE 576  ? A ILE 587  
163  1 Y 1 A CYS 577  ? A CYS 588  
164  1 Y 1 A ILE 578  ? A ILE 589  
165  1 Y 1 A LEU 579  ? A LEU 590  
166  1 Y 1 A THR 580  ? A THR 591  
167  1 Y 1 A GLU 581  ? A GLU 592  
168  1 Y 1 A TYR 582  ? A TYR 593  
169  1 Y 1 A CYS 583  ? A CYS 594  
170  1 Y 1 A PRO 584  ? A PRO 595  
171  1 Y 1 A ARG 585  ? A ARG 596  
172  1 Y 1 A GLY 586  ? A GLY 597  
173  1 Y 1 A SER 587  ? A SER 598  
174  1 Y 1 A LEU 588  ? A LEU 599  
175  1 Y 1 A GLN 589  ? A GLN 600  
176  1 Y 1 A ASP 590  ? A ASP 601  
177  1 Y 1 A ILE 591  ? A ILE 602  
178  1 Y 1 A LEU 592  ? A LEU 603  
179  1 Y 1 A GLU 593  ? A GLU 604  
180  1 Y 1 A ASN 594  ? A ASN 605  
181  1 Y 1 A GLU 595  ? A GLU 606  
182  1 Y 1 A SER 596  ? A SER 607  
183  1 Y 1 A ILE 597  ? A ILE 608  
184  1 Y 1 A THR 598  ? A THR 609  
185  1 Y 1 A LEU 599  ? A LEU 610  
186  1 Y 1 A ASP 600  ? A ASP 611  
187  1 Y 1 A TRP 601  ? A TRP 612  
188  1 Y 1 A MET 602  ? A MET 613  
189  1 Y 1 A PHE 603  ? A PHE 614  
190  1 Y 1 A ARG 604  ? A ARG 615  
191  1 Y 1 A TYR 605  ? A TYR 616  
192  1 Y 1 A SER 606  ? A SER 617  
193  1 Y 1 A LEU 607  ? A LEU 618  
194  1 Y 1 A THR 608  ? A THR 619  
195  1 Y 1 A ASN 609  ? A ASN 620  
196  1 Y 1 A ASP 610  ? A ASP 621  
197  1 Y 1 A ILE 611  ? A ILE 622  
198  1 Y 1 A VAL 612  ? A VAL 623  
199  1 Y 1 A LYS 613  ? A LYS 624  
200  1 Y 1 A GLY 614  ? A GLY 625  
201  1 Y 1 A MET 615  ? A MET 626  
202  1 Y 1 A LEU 616  ? A LEU 627  
203  1 Y 1 A PHE 617  ? A PHE 628  
204  1 Y 1 A LEU 618  ? A LEU 629  
205  1 Y 1 A HIS 619  ? A HIS 630  
206  1 Y 1 A ASN 620  ? A ASN 631  
207  1 Y 1 A GLY 621  ? A GLY 632  
208  1 Y 1 A ALA 622  ? A ALA 633  
209  1 Y 1 A ILE 623  ? A ILE 634  
210  1 Y 1 A CYS 624  ? A CYS 635  
211  1 Y 1 A SER 625  ? A SER 636  
212  1 Y 1 A HIS 626  ? A HIS 637  
213  1 Y 1 A GLY 627  ? A GLY 638  
214  1 Y 1 A ASN 628  ? A ASN 639  
215  1 Y 1 A LEU 629  ? A LEU 640  
216  1 Y 1 A LYS 630  ? A LYS 641  
217  1 Y 1 A SER 631  ? A SER 642  
218  1 Y 1 A SER 632  ? A SER 643  
219  1 Y 1 A ASN 633  ? A ASN 644  
220  1 Y 1 A CYS 634  ? A CYS 645  
221  1 Y 1 A VAL 635  ? A VAL 646  
222  1 Y 1 A VAL 636  ? A VAL 647  
223  1 Y 1 A ASP 637  ? A ASP 648  
224  1 Y 1 A GLY 638  ? A GLY 649  
225  1 Y 1 A ARG 639  ? A ARG 650  
226  1 Y 1 A PHE 640  ? A PHE 651  
227  1 Y 1 A VAL 641  ? A VAL 652  
228  1 Y 1 A LEU 642  ? A LEU 653  
229  1 Y 1 A LYS 643  ? A LYS 654  
230  1 Y 1 A ILE 644  ? A ILE 655  
231  1 Y 1 A THR 645  ? A THR 656  
232  1 Y 1 A ASP 646  ? A ASP 657  
233  1 Y 1 A TYR 647  ? A TYR 658  
234  1 Y 1 A GLY 648  ? A GLY 659  
235  1 Y 1 A LEU 649  ? A LEU 660  
236  1 Y 1 A GLU 650  ? A GLU 661  
237  1 Y 1 A SER 651  ? A SER 662  
238  1 Y 1 A PHE 652  ? A PHE 663  
239  1 Y 1 A ARG 653  ? A ARG 664  
240  1 Y 1 A ASP 654  ? A ASP 665  
241  1 Y 1 A LEU 655  ? A LEU 666  
242  1 Y 1 A ASP 656  ? A ASP 667  
243  1 Y 1 A PRO 657  ? A PRO 668  
244  1 Y 1 A GLU 658  ? A GLU 669  
245  1 Y 1 A GLN 659  ? A GLN 670  
246  1 Y 1 A GLY 660  ? A GLY 671  
247  1 Y 1 A HIS 661  ? A HIS 672  
248  1 Y 1 A THR 662  ? A THR 673  
249  1 Y 1 A VAL 663  ? A VAL 674  
250  1 Y 1 A TYR 664  ? A TYR 675  
251  1 Y 1 A ALA 665  ? A ALA 676  
252  1 Y 1 A LYS 666  ? A LYS 677  
253  1 Y 1 A LYS 667  ? A LYS 678  
254  1 Y 1 A LEU 668  ? A LEU 679  
255  1 Y 1 A TRP 669  ? A TRP 680  
256  1 Y 1 A THR 670  ? A THR 681  
257  1 Y 1 A ALA 671  ? A ALA 682  
258  1 Y 1 A PRO 672  ? A PRO 683  
259  1 Y 1 A GLU 673  ? A GLU 684  
260  1 Y 1 A LEU 674  ? A LEU 685  
261  1 Y 1 A LEU 675  ? A LEU 686  
262  1 Y 1 A ARG 676  ? A ARG 687  
263  1 Y 1 A MET 677  ? A MET 688  
264  1 Y 1 A ALA 678  ? A ALA 689  
265  1 Y 1 A SER 679  ? A SER 690  
266  1 Y 1 A PRO 680  ? A PRO 691  
267  1 Y 1 A PRO 681  ? A PRO 692  
268  1 Y 1 A VAL 682  ? A VAL 693  
269  1 Y 1 A ARG 683  ? A ARG 694  
270  1 Y 1 A GLY 684  ? A GLY 695  
271  1 Y 1 A SER 685  ? A SER 696  
272  1 Y 1 A GLN 686  ? A GLN 697  
273  1 Y 1 A ALA 687  ? A ALA 698  
274  1 Y 1 A GLY 688  ? A GLY 699  
275  1 Y 1 A ASP 689  ? A ASP 700  
276  1 Y 1 A VAL 690  ? A VAL 701  
277  1 Y 1 A TYR 691  ? A TYR 702  
278  1 Y 1 A SER 692  ? A SER 703  
279  1 Y 1 A PHE 693  ? A PHE 704  
280  1 Y 1 A GLY 694  ? A GLY 705  
281  1 Y 1 A ILE 695  ? A ILE 706  
282  1 Y 1 A ILE 696  ? A ILE 707  
283  1 Y 1 A LEU 697  ? A LEU 708  
284  1 Y 1 A GLN 698  ? A GLN 709  
285  1 Y 1 A GLU 699  ? A GLU 710  
286  1 Y 1 A ILE 700  ? A ILE 711  
287  1 Y 1 A ALA 701  ? A ALA 712  
288  1 Y 1 A LEU 702  ? A LEU 713  
289  1 Y 1 A ARG 703  ? A ARG 714  
290  1 Y 1 A SER 704  ? A SER 715  
291  1 Y 1 A GLY 705  ? A GLY 716  
292  1 Y 1 A VAL 706  ? A VAL 717  
293  1 Y 1 A PHE 707  ? A PHE 718  
294  1 Y 1 A HIS 708  ? A HIS 719  
295  1 Y 1 A VAL 709  ? A VAL 720  
296  1 Y 1 A GLU 710  ? A GLU 721  
297  1 Y 1 A GLY 711  ? A GLY 722  
298  1 Y 1 A LEU 712  ? A LEU 723  
299  1 Y 1 A ASP 713  ? A ASP 724  
300  1 Y 1 A LEU 714  ? A LEU 725  
301  1 Y 1 A SER 715  ? A SER 726  
302  1 Y 1 A PRO 716  ? A PRO 727  
303  1 Y 1 A LYS 717  ? A LYS 728  
304  1 Y 1 A GLU 718  ? A GLU 729  
305  1 Y 1 A ILE 719  ? A ILE 730  
306  1 Y 1 A ILE 720  ? A ILE 731  
307  1 Y 1 A GLU 721  ? A GLU 732  
308  1 Y 1 A ARG 722  ? A ARG 733  
309  1 Y 1 A VAL 723  ? A VAL 734  
310  1 Y 1 A THR 724  ? A THR 735  
311  1 Y 1 A ARG 725  ? A ARG 736  
312  1 Y 1 A GLY 726  ? A GLY 737  
313  1 Y 1 A GLU 727  ? A GLU 738  
314  1 Y 1 A GLN 728  ? A GLN 739  
315  1 Y 1 A PRO 729  ? A PRO 740  
316  1 Y 1 A PRO 730  ? A PRO 741  
317  1 Y 1 A PHE 731  ? A PHE 742  
318  1 Y 1 A ARG 732  ? A ARG 743  
319  1 Y 1 A PRO 733  ? A PRO 744  
320  1 Y 1 A SER 734  ? A SER 745  
321  1 Y 1 A LEU 735  ? A LEU 746  
322  1 Y 1 A ALA 736  ? A ALA 747  
323  1 Y 1 A LEU 737  ? A LEU 748  
324  1 Y 1 A GLN 738  ? A GLN 749  
325  1 Y 1 A SER 739  ? A SER 750  
326  1 Y 1 A HIS 740  ? A HIS 751  
327  1 Y 1 A LEU 741  ? A LEU 752  
328  1 Y 1 A GLU 742  ? A GLU 753  
329  1 Y 1 A GLU 743  ? A GLU 754  
330  1 Y 1 A LEU 744  ? A LEU 755  
331  1 Y 1 A GLY 745  ? A GLY 756  
332  1 Y 1 A LEU 746  ? A LEU 757  
333  1 Y 1 A LEU 747  ? A LEU 758  
334  1 Y 1 A MET 748  ? A MET 759  
335  1 Y 1 A GLN 749  ? A GLN 760  
336  1 Y 1 A ARG 750  ? A ARG 761  
337  1 Y 1 A CYS 751  ? A CYS 762  
338  1 Y 1 A TRP 752  ? A TRP 763  
339  1 Y 1 A ALA 753  ? A ALA 764  
340  1 Y 1 A GLU 754  ? A GLU 765  
341  1 Y 1 A ASP 755  ? A ASP 766  
342  1 Y 1 A PRO 756  ? A PRO 767  
343  1 Y 1 A GLN 757  ? A GLN 768  
344  1 Y 1 A GLU 758  ? A GLU 769  
345  1 Y 1 A ARG 759  ? A ARG 770  
346  1 Y 1 A PRO 760  ? A PRO 771  
347  1 Y 1 A PRO 761  ? A PRO 772  
348  1 Y 1 A PHE 762  ? A PHE 773  
349  1 Y 1 A GLN 763  ? A GLN 774  
350  1 Y 1 A GLN 764  ? A GLN 775  
351  1 Y 1 A ILE 765  ? A ILE 776  
352  1 Y 1 A ARG 766  ? A ARG 777  
353  1 Y 1 A LEU 767  ? A LEU 778  
354  1 Y 1 A THR 768  ? A THR 779  
355  1 Y 1 A LEU 769  ? A LEU 780  
356  1 Y 1 A ARG 770  ? A ARG 781  
357  1 Y 1 A LYS 771  ? A LYS 782  
358  1 Y 1 A PHE 772  ? A PHE 783  
359  1 Y 1 A ASN 773  ? A ASN 784  
360  1 Y 1 A ARG 774  ? A ARG 785  
361  1 Y 1 A GLU 775  ? A GLU 786  
362  1 Y 1 A ASN 776  ? A ASN 787  
363  1 Y 1 A SER 777  ? A SER 788  
364  1 Y 1 A SER 778  ? A SER 789  
365  1 Y 1 A ASN 779  ? A ASN 790  
366  1 Y 1 A ILE 780  ? A ILE 791  
367  1 Y 1 A LEU 781  ? A LEU 792  
368  1 Y 1 A ASP 782  ? A ASP 793  
369  1 Y 1 A ASN 783  ? A ASN 794  
370  1 Y 1 A LEU 784  ? A LEU 795  
371  1 Y 1 A LEU 785  ? A LEU 796  
372  1 Y 1 A SER 786  ? A SER 797  
373  1 Y 1 A ARG 787  ? A ARG 798  
374  1 Y 1 A MET 788  ? A MET 799  
375  1 Y 1 A GLU 789  ? A GLU 800  
376  1 Y 1 A GLN 790  ? A GLN 801  
377  1 Y 1 A TYR 791  ? A TYR 802  
378  1 Y 1 A ALA 792  ? A ALA 803  
379  1 Y 1 A ASN 793  ? A ASN 804  
380  1 Y 1 A ASN 794  ? A ASN 805  
381  1 Y 1 A LEU 795  ? A LEU 806  
382  1 Y 1 A GLU 796  ? A GLU 807  
383  1 Y 1 A GLU 797  ? A GLU 808  
384  1 Y 1 A LEU 798  ? A LEU 809  
385  1 Y 1 A VAL 799  ? A VAL 810  
386  1 Y 1 A GLU 800  ? A GLU 811  
387  1 Y 1 A GLU 801  ? A GLU 812  
388  1 Y 1 A ARG 802  ? A ARG 813  
389  1 Y 1 A THR 803  ? A THR 814  
390  1 Y 1 A GLN 804  ? A GLN 815  
391  1 Y 1 A ALA 805  ? A ALA 816  
392  1 Y 1 A TYR 806  ? A TYR 817  
393  1 Y 1 A LEU 807  ? A LEU 818  
394  1 Y 1 A GLU 808  ? A GLU 819  
395  1 Y 1 A GLU 809  ? A GLU 820  
396  1 Y 1 A LYS 810  ? A LYS 821  
397  1 Y 1 A ARG 811  ? A ARG 822  
398  1 Y 1 A LYS 812  ? A LYS 823  
399  1 Y 1 A ALA 813  ? A ALA 824  
400  1 Y 1 A GLU 814  ? A GLU 825  
401  1 Y 1 A ALA 815  ? A ALA 826  
402  1 Y 1 A LEU 816  ? A LEU 827  
403  1 Y 1 A LEU 817  ? A LEU 828  
404  1 Y 1 A TYR 818  ? A TYR 829  
405  1 Y 1 A GLN 819  ? A GLN 830  
406  1 Y 1 A ILE 820  ? A ILE 831  
407  1 Y 1 A LEU 821  ? A LEU 832  
408  1 Y 1 A PRO 822  ? A PRO 833  
409  1 Y 1 A HIS 823  ? A HIS 834  
410  1 Y 1 A SER 824  ? A SER 835  
411  1 Y 1 A VAL 825  ? A VAL 836  
412  1 Y 1 A ALA 826  ? A ALA 837  
413  1 Y 1 A GLU 827  ? A GLU 838  
414  1 Y 1 A GLN 828  ? A GLN 839  
415  1 Y 1 A LEU 829  ? A LEU 840  
416  1 Y 1 A LYS 830  ? A LYS 841  
417  1 Y 1 A ARG 831  ? A ARG 842  
418  1 Y 1 A GLY 832  ? A GLY 843  
419  1 Y 1 A GLU 833  ? A GLU 844  
420  1 Y 1 A THR 834  ? A THR 845  
421  1 Y 1 A VAL 835  ? A VAL 846  
422  1 Y 1 A GLN 836  ? A GLN 847  
423  1 Y 1 A ALA 837  ? A ALA 848  
424  1 Y 1 A GLU 838  ? A GLU 849  
425  1 Y 1 A ALA 839  ? A ALA 850  
426  1 Y 1 A PHE 840  ? A PHE 851  
427  1 Y 1 A ASP 841  ? A ASP 852  
428  1 Y 1 A SER 842  ? A SER 853  
429  1 Y 1 A VAL 843  ? A VAL 854  
430  1 Y 1 A THR 844  ? A THR 855  
431  1 Y 1 A ILE 845  ? A ILE 856  
432  1 Y 1 A TYR 846  ? A TYR 857  
433  1 Y 1 A PHE 847  ? A PHE 858  
434  1 Y 1 A SER 848  ? A SER 859  
435  1 Y 1 A ASP 849  ? A ASP 860  
436  1 Y 1 A ILE 850  ? A ILE 861  
437  1 Y 1 A VAL 851  ? A VAL 862  
438  1 Y 1 A GLY 852  ? A GLY 863  
439  1 Y 1 A PHE 853  ? A PHE 864  
440  1 Y 1 A THR 854  ? A THR 865  
441  1 Y 1 A ALA 855  ? A ALA 866  
442  1 Y 1 A LEU 856  ? A LEU 867  
443  1 Y 1 A SER 857  ? A SER 868  
444  1 Y 1 A ALA 858  ? A ALA 869  
445  1 Y 1 A GLU 859  ? A GLU 870  
446  1 Y 1 A SER 860  ? A SER 871  
447  1 Y 1 A THR 861  ? A THR 872  
448  1 Y 1 A PRO 862  ? A PRO 873  
449  1 Y 1 A MET 863  ? A MET 874  
450  1 Y 1 A GLN 864  ? A GLN 875  
451  1 Y 1 A VAL 865  ? A VAL 876  
452  1 Y 1 A VAL 866  ? A VAL 877  
453  1 Y 1 A THR 867  ? A THR 878  
454  1 Y 1 A LEU 868  ? A LEU 879  
455  1 Y 1 A LEU 869  ? A LEU 880  
456  1 Y 1 A ASN 870  ? A ASN 881  
457  1 Y 1 A ASP 871  ? A ASP 882  
458  1 Y 1 A LEU 872  ? A LEU 883  
459  1 Y 1 A TYR 873  ? A TYR 884  
460  1 Y 1 A THR 874  ? A THR 885  
461  1 Y 1 A CYS 875  ? A CYS 886  
462  1 Y 1 A PHE 876  ? A PHE 887  
463  1 Y 1 A ASP 877  ? A ASP 888  
464  1 Y 1 A ALA 878  ? A ALA 889  
465  1 Y 1 A VAL 879  ? A VAL 890  
466  1 Y 1 A ILE 880  ? A ILE 891  
467  1 Y 1 A ASP 881  ? A ASP 892  
468  1 Y 1 A ASN 882  ? A ASN 893  
469  1 Y 1 A PHE 883  ? A PHE 894  
470  1 Y 1 A ASP 884  ? A ASP 895  
471  1 Y 1 A VAL 885  ? A VAL 896  
472  1 Y 1 A TYR 886  ? A TYR 897  
473  1 Y 1 A LYS 887  ? A LYS 898  
474  1 Y 1 A VAL 888  ? A VAL 899  
475  1 Y 1 A GLU 889  ? A GLU 900  
476  1 Y 1 A THR 890  ? A THR 901  
477  1 Y 1 A ILE 891  ? A ILE 902  
478  1 Y 1 A GLY 892  ? A GLY 903  
479  1 Y 1 A ASP 893  ? A ASP 904  
480  1 Y 1 A ALA 894  ? A ALA 905  
481  1 Y 1 A TYR 895  ? A TYR 906  
482  1 Y 1 A MET 896  ? A MET 907  
483  1 Y 1 A VAL 897  ? A VAL 908  
484  1 Y 1 A VAL 898  ? A VAL 909  
485  1 Y 1 A SER 899  ? A SER 910  
486  1 Y 1 A GLY 900  ? A GLY 911  
487  1 Y 1 A LEU 901  ? A LEU 912  
488  1 Y 1 A PRO 902  ? A PRO 913  
489  1 Y 1 A VAL 903  ? A VAL 914  
490  1 Y 1 A ARG 904  ? A ARG 915  
491  1 Y 1 A ASN 905  ? A ASN 916  
492  1 Y 1 A GLY 906  ? A GLY 917  
493  1 Y 1 A ARG 907  ? A ARG 918  
494  1 Y 1 A LEU 908  ? A LEU 919  
495  1 Y 1 A HIS 909  ? A HIS 920  
496  1 Y 1 A ALA 910  ? A ALA 921  
497  1 Y 1 A CYS 911  ? A CYS 922  
498  1 Y 1 A GLU 912  ? A GLU 923  
499  1 Y 1 A VAL 913  ? A VAL 924  
500  1 Y 1 A ALA 914  ? A ALA 925  
501  1 Y 1 A ARG 915  ? A ARG 926  
502  1 Y 1 A MET 916  ? A MET 927  
503  1 Y 1 A ALA 917  ? A ALA 928  
504  1 Y 1 A LEU 918  ? A LEU 929  
505  1 Y 1 A ALA 919  ? A ALA 930  
506  1 Y 1 A LEU 920  ? A LEU 931  
507  1 Y 1 A LEU 921  ? A LEU 932  
508  1 Y 1 A ASP 922  ? A ASP 933  
509  1 Y 1 A ALA 923  ? A ALA 934  
510  1 Y 1 A VAL 924  ? A VAL 935  
511  1 Y 1 A ARG 925  ? A ARG 936  
512  1 Y 1 A SER 926  ? A SER 937  
513  1 Y 1 A PHE 927  ? A PHE 938  
514  1 Y 1 A ARG 928  ? A ARG 939  
515  1 Y 1 A ILE 929  ? A ILE 940  
516  1 Y 1 A ARG 930  ? A ARG 941  
517  1 Y 1 A HIS 931  ? A HIS 942  
518  1 Y 1 A ARG 932  ? A ARG 943  
519  1 Y 1 A PRO 933  ? A PRO 944  
520  1 Y 1 A GLN 934  ? A GLN 945  
521  1 Y 1 A GLU 935  ? A GLU 946  
522  1 Y 1 A GLN 936  ? A GLN 947  
523  1 Y 1 A LEU 937  ? A LEU 948  
524  1 Y 1 A ARG 938  ? A ARG 949  
525  1 Y 1 A LEU 939  ? A LEU 950  
526  1 Y 1 A ARG 940  ? A ARG 951  
527  1 Y 1 A ILE 941  ? A ILE 952  
528  1 Y 1 A GLY 942  ? A GLY 953  
529  1 Y 1 A ILE 943  ? A ILE 954  
530  1 Y 1 A HIS 944  ? A HIS 955  
531  1 Y 1 A THR 945  ? A THR 956  
532  1 Y 1 A GLY 946  ? A GLY 957  
533  1 Y 1 A PRO 947  ? A PRO 958  
534  1 Y 1 A VAL 948  ? A VAL 959  
535  1 Y 1 A CYS 949  ? A CYS 960  
536  1 Y 1 A ALA 950  ? A ALA 961  
537  1 Y 1 A GLY 951  ? A GLY 962  
538  1 Y 1 A VAL 952  ? A VAL 963  
539  1 Y 1 A VAL 953  ? A VAL 964  
540  1 Y 1 A GLY 954  ? A GLY 965  
541  1 Y 1 A LEU 955  ? A LEU 966  
542  1 Y 1 A LYS 956  ? A LYS 967  
543  1 Y 1 A MET 957  ? A MET 968  
544  1 Y 1 A PRO 958  ? A PRO 969  
545  1 Y 1 A ARG 959  ? A ARG 970  
546  1 Y 1 A TYR 960  ? A TYR 971  
547  1 Y 1 A CYS 961  ? A CYS 972  
548  1 Y 1 A LEU 962  ? A LEU 973  
549  1 Y 1 A PHE 963  ? A PHE 974  
550  1 Y 1 A GLY 964  ? A GLY 975  
551  1 Y 1 A ASP 965  ? A ASP 976  
552  1 Y 1 A THR 966  ? A THR 977  
553  1 Y 1 A VAL 967  ? A VAL 978  
554  1 Y 1 A ASN 968  ? A ASN 979  
555  1 Y 1 A THR 969  ? A THR 980  
556  1 Y 1 A ALA 970  ? A ALA 981  
557  1 Y 1 A SER 971  ? A SER 982  
558  1 Y 1 A ARG 972  ? A ARG 983  
559  1 Y 1 A MET 973  ? A MET 984  
560  1 Y 1 A GLU 974  ? A GLU 985  
561  1 Y 1 A SER 975  ? A SER 986  
562  1 Y 1 A ASN 976  ? A ASN 987  
563  1 Y 1 A GLY 977  ? A GLY 988  
564  1 Y 1 A GLU 978  ? A GLU 989  
565  1 Y 1 A ALA 979  ? A ALA 990  
566  1 Y 1 A LEU 980  ? A LEU 991  
567  1 Y 1 A LYS 981  ? A LYS 992  
568  1 Y 1 A ILE 982  ? A ILE 993  
569  1 Y 1 A HIS 983  ? A HIS 994  
570  1 Y 1 A LEU 984  ? A LEU 995  
571  1 Y 1 A SER 985  ? A SER 996  
572  1 Y 1 A SER 986  ? A SER 997  
573  1 Y 1 A GLU 987  ? A GLU 998  
574  1 Y 1 A THR 988  ? A THR 999  
575  1 Y 1 A LYS 989  ? A LYS 1000 
576  1 Y 1 A ALA 990  ? A ALA 1001 
577  1 Y 1 A VAL 991  ? A VAL 1002 
578  1 Y 1 A LEU 992  ? A LEU 1003 
579  1 Y 1 A GLU 993  ? A GLU 1004 
580  1 Y 1 A GLU 994  ? A GLU 1005 
581  1 Y 1 A PHE 995  ? A PHE 1006 
582  1 Y 1 A GLY 996  ? A GLY 1007 
583  1 Y 1 A GLY 997  ? A GLY 1008 
584  1 Y 1 A PHE 998  ? A PHE 1009 
585  1 Y 1 A GLU 999  ? A GLU 1010 
586  1 Y 1 A LEU 1000 ? A LEU 1011 
587  1 Y 1 A GLU 1001 ? A GLU 1012 
588  1 Y 1 A LEU 1002 ? A LEU 1013 
589  1 Y 1 A ARG 1003 ? A ARG 1014 
590  1 Y 1 A GLY 1004 ? A GLY 1015 
591  1 Y 1 A ASP 1005 ? A ASP 1016 
592  1 Y 1 A VAL 1006 ? A VAL 1017 
593  1 Y 1 A GLU 1007 ? A GLU 1018 
594  1 Y 1 A MET 1008 ? A MET 1019 
595  1 Y 1 A LYS 1009 ? A LYS 1020 
596  1 Y 1 A GLY 1010 ? A GLY 1021 
597  1 Y 1 A LYS 1011 ? A LYS 1022 
598  1 Y 1 A GLY 1012 ? A GLY 1023 
599  1 Y 1 A LYS 1013 ? A LYS 1024 
600  1 Y 1 A VAL 1014 ? A VAL 1025 
601  1 Y 1 A ARG 1015 ? A ARG 1026 
602  1 Y 1 A THR 1016 ? A THR 1027 
603  1 Y 1 A TYR 1017 ? A TYR 1028 
604  1 Y 1 A TRP 1018 ? A TRP 1029 
605  1 Y 1 A LEU 1019 ? A LEU 1030 
606  1 Y 1 A LEU 1020 ? A LEU 1031 
607  1 Y 1 A GLY 1021 ? A GLY 1032 
608  1 Y 1 A GLU 1022 ? A GLU 1033 
609  1 Y 1 A ARG 1023 ? A ARG 1034 
610  1 Y 1 A GLY 1024 ? A GLY 1035 
611  1 Y 1 A SER 1025 ? A SER 1036 
612  1 Y 1 A SER 1026 ? A SER 1037 
613  1 Y 1 A THR 1027 ? A THR 1038 
614  1 Y 1 A ARG 1028 ? A ARG 1039 
615  1 Y 1 A GLY 1029 ? A GLY 1040 
616  1 Y 1 B ASP -10  ? B ASP 1    
617  1 Y 1 B TYR -9   ? B TYR 2    
618  1 Y 1 B LYS -8   ? B LYS 3    
619  1 Y 1 B ASP -7   ? B ASP 4    
620  1 Y 1 B ASP -6   ? B ASP 5    
621  1 Y 1 B ASP -5   ? B ASP 6    
622  1 Y 1 B ASP -4   ? B ASP 7    
623  1 Y 1 B LYS -3   ? B LYS 8    
624  1 Y 1 B ALA -2   ? B ALA 9    
625  1 Y 1 B ALA -1   ? B ALA 10   
626  1 Y 1 B ALA 0    ? B ALA 11   
627  1 Y 1 B ASP 426  ? B ASP 437  
628  1 Y 1 B ASN 427  ? B ASN 438  
629  1 Y 1 B GLU 428  ? B GLU 439  
630  1 Y 1 B ASP 429  ? B ASP 440  
631  1 Y 1 B PRO 430  ? B PRO 441  
632  1 Y 1 B ALA 431  ? B ALA 442  
633  1 Y 1 B CYS 432  ? B CYS 443  
634  1 Y 1 B ASN 433  ? B ASN 444  
635  1 Y 1 B GLN 434  ? B GLN 445  
636  1 Y 1 B ASP 435  ? B ASP 446  
637  1 Y 1 B HIS 436  ? B HIS 447  
638  1 Y 1 B LEU 437  ? B LEU 448  
639  1 Y 1 B SER 438  ? B SER 449  
640  1 Y 1 B THR 439  ? B THR 450  
641  1 Y 1 B LEU 440  ? B LEU 451  
642  1 Y 1 B GLU 441  ? B GLU 452  
643  1 Y 1 B VAL 442  ? B VAL 453  
644  1 Y 1 B LEU 443  ? B LEU 454  
645  1 Y 1 B ALA 444  ? B ALA 455  
646  1 Y 1 B LEU 445  ? B LEU 456  
647  1 Y 1 B VAL 446  ? B VAL 457  
648  1 Y 1 B GLY 447  ? B GLY 458  
649  1 Y 1 B SER 448  ? B SER 459  
650  1 Y 1 B LEU 449  ? B LEU 460  
651  1 Y 1 B SER 450  ? B SER 461  
652  1 Y 1 B LEU 451  ? B LEU 462  
653  1 Y 1 B LEU 452  ? B LEU 463  
654  1 Y 1 B GLY 453  ? B GLY 464  
655  1 Y 1 B ILE 454  ? B ILE 465  
656  1 Y 1 B LEU 455  ? B LEU 466  
657  1 Y 1 B ILE 456  ? B ILE 467  
658  1 Y 1 B VAL 457  ? B VAL 468  
659  1 Y 1 B SER 458  ? B SER 469  
660  1 Y 1 B PHE 459  ? B PHE 470  
661  1 Y 1 B PHE 460  ? B PHE 471  
662  1 Y 1 B ILE 461  ? B ILE 472  
663  1 Y 1 B TYR 462  ? B TYR 473  
664  1 Y 1 B ARG 463  ? B ARG 474  
665  1 Y 1 B LYS 464  ? B LYS 475  
666  1 Y 1 B MET 465  ? B MET 476  
667  1 Y 1 B GLN 466  ? B GLN 477  
668  1 Y 1 B LEU 467  ? B LEU 478  
669  1 Y 1 B GLU 468  ? B GLU 479  
670  1 Y 1 B LYS 469  ? B LYS 480  
671  1 Y 1 B GLU 470  ? B GLU 481  
672  1 Y 1 B LEU 471  ? B LEU 482  
673  1 Y 1 B ALA 472  ? B ALA 483  
674  1 Y 1 B SER 473  ? B SER 484  
675  1 Y 1 B GLU 474  ? B GLU 485  
676  1 Y 1 B LEU 475  ? B LEU 486  
677  1 Y 1 B TRP 476  ? B TRP 487  
678  1 Y 1 B ARG 477  ? B ARG 488  
679  1 Y 1 B VAL 478  ? B VAL 489  
680  1 Y 1 B ARG 479  ? B ARG 490  
681  1 Y 1 B TRP 480  ? B TRP 491  
682  1 Y 1 B GLU 481  ? B GLU 492  
683  1 Y 1 B ASP 482  ? B ASP 493  
684  1 Y 1 B VAL 483  ? B VAL 494  
685  1 Y 1 B GLU 484  ? B GLU 495  
686  1 Y 1 B PRO 485  ? B PRO 496  
687  1 Y 1 B SER 486  ? B SER 497  
688  1 Y 1 B SER 487  ? B SER 498  
689  1 Y 1 B LEU 488  ? B LEU 499  
690  1 Y 1 B GLU 489  ? B GLU 500  
691  1 Y 1 B ARG 490  ? B ARG 501  
692  1 Y 1 B HIS 491  ? B HIS 502  
693  1 Y 1 B LEU 492  ? B LEU 503  
694  1 Y 1 B ARG 493  ? B ARG 504  
695  1 Y 1 B SER 494  ? B SER 505  
696  1 Y 1 B ALA 495  ? B ALA 506  
697  1 Y 1 B GLY 496  ? B GLY 507  
698  1 Y 1 B SER 497  ? B SER 508  
699  1 Y 1 B ARG 498  ? B ARG 509  
700  1 Y 1 B LEU 499  ? B LEU 510  
701  1 Y 1 B THR 500  ? B THR 511  
702  1 Y 1 B LEU 501  ? B LEU 512  
703  1 Y 1 B SER 502  ? B SER 513  
704  1 Y 1 B GLY 503  ? B GLY 514  
705  1 Y 1 B ARG 504  ? B ARG 515  
706  1 Y 1 B GLY 505  ? B GLY 516  
707  1 Y 1 B SER 506  ? B SER 517  
708  1 Y 1 B ASN 507  ? B ASN 518  
709  1 Y 1 B TYR 508  ? B TYR 519  
710  1 Y 1 B GLY 509  ? B GLY 520  
711  1 Y 1 B SER 510  ? B SER 521  
712  1 Y 1 B LEU 511  ? B LEU 522  
713  1 Y 1 B LEU 512  ? B LEU 523  
714  1 Y 1 B THR 513  ? B THR 524  
715  1 Y 1 B THR 514  ? B THR 525  
716  1 Y 1 B GLU 515  ? B GLU 526  
717  1 Y 1 B GLY 516  ? B GLY 527  
718  1 Y 1 B GLN 517  ? B GLN 528  
719  1 Y 1 B PHE 518  ? B PHE 529  
720  1 Y 1 B GLN 519  ? B GLN 530  
721  1 Y 1 B VAL 520  ? B VAL 531  
722  1 Y 1 B PHE 521  ? B PHE 532  
723  1 Y 1 B ALA 522  ? B ALA 533  
724  1 Y 1 B LYS 523  ? B LYS 534  
725  1 Y 1 B THR 524  ? B THR 535  
726  1 Y 1 B ALA 525  ? B ALA 536  
727  1 Y 1 B TYR 526  ? B TYR 537  
728  1 Y 1 B TYR 527  ? B TYR 538  
729  1 Y 1 B LYS 528  ? B LYS 539  
730  1 Y 1 B GLY 529  ? B GLY 540  
731  1 Y 1 B ASN 530  ? B ASN 541  
732  1 Y 1 B LEU 531  ? B LEU 542  
733  1 Y 1 B VAL 532  ? B VAL 543  
734  1 Y 1 B ALA 533  ? B ALA 544  
735  1 Y 1 B VAL 534  ? B VAL 545  
736  1 Y 1 B LYS 535  ? B LYS 546  
737  1 Y 1 B ARG 536  ? B ARG 547  
738  1 Y 1 B VAL 537  ? B VAL 548  
739  1 Y 1 B ASN 538  ? B ASN 549  
740  1 Y 1 B ARG 539  ? B ARG 550  
741  1 Y 1 B LYS 540  ? B LYS 551  
742  1 Y 1 B ARG 541  ? B ARG 552  
743  1 Y 1 B ILE 542  ? B ILE 553  
744  1 Y 1 B GLU 543  ? B GLU 554  
745  1 Y 1 B LEU 544  ? B LEU 555  
746  1 Y 1 B THR 545  ? B THR 556  
747  1 Y 1 B ARG 546  ? B ARG 557  
748  1 Y 1 B LYS 547  ? B LYS 558  
749  1 Y 1 B VAL 548  ? B VAL 559  
750  1 Y 1 B LEU 549  ? B LEU 560  
751  1 Y 1 B PHE 550  ? B PHE 561  
752  1 Y 1 B GLU 551  ? B GLU 562  
753  1 Y 1 B LEU 552  ? B LEU 563  
754  1 Y 1 B LYS 553  ? B LYS 564  
755  1 Y 1 B HIS 554  ? B HIS 565  
756  1 Y 1 B MET 555  ? B MET 566  
757  1 Y 1 B ARG 556  ? B ARG 567  
758  1 Y 1 B ASP 557  ? B ASP 568  
759  1 Y 1 B VAL 558  ? B VAL 569  
760  1 Y 1 B GLN 559  ? B GLN 570  
761  1 Y 1 B ASN 560  ? B ASN 571  
762  1 Y 1 B GLU 561  ? B GLU 572  
763  1 Y 1 B HIS 562  ? B HIS 573  
764  1 Y 1 B LEU 563  ? B LEU 574  
765  1 Y 1 B THR 564  ? B THR 575  
766  1 Y 1 B ARG 565  ? B ARG 576  
767  1 Y 1 B PHE 566  ? B PHE 577  
768  1 Y 1 B VAL 567  ? B VAL 578  
769  1 Y 1 B GLY 568  ? B GLY 579  
770  1 Y 1 B ALA 569  ? B ALA 580  
771  1 Y 1 B CYS 570  ? B CYS 581  
772  1 Y 1 B THR 571  ? B THR 582  
773  1 Y 1 B ASP 572  ? B ASP 583  
774  1 Y 1 B PRO 573  ? B PRO 584  
775  1 Y 1 B PRO 574  ? B PRO 585  
776  1 Y 1 B ASN 575  ? B ASN 586  
777  1 Y 1 B ILE 576  ? B ILE 587  
778  1 Y 1 B CYS 577  ? B CYS 588  
779  1 Y 1 B ILE 578  ? B ILE 589  
780  1 Y 1 B LEU 579  ? B LEU 590  
781  1 Y 1 B THR 580  ? B THR 591  
782  1 Y 1 B GLU 581  ? B GLU 592  
783  1 Y 1 B TYR 582  ? B TYR 593  
784  1 Y 1 B CYS 583  ? B CYS 594  
785  1 Y 1 B PRO 584  ? B PRO 595  
786  1 Y 1 B ARG 585  ? B ARG 596  
787  1 Y 1 B GLY 586  ? B GLY 597  
788  1 Y 1 B SER 587  ? B SER 598  
789  1 Y 1 B LEU 588  ? B LEU 599  
790  1 Y 1 B GLN 589  ? B GLN 600  
791  1 Y 1 B ASP 590  ? B ASP 601  
792  1 Y 1 B ILE 591  ? B ILE 602  
793  1 Y 1 B LEU 592  ? B LEU 603  
794  1 Y 1 B GLU 593  ? B GLU 604  
795  1 Y 1 B ASN 594  ? B ASN 605  
796  1 Y 1 B GLU 595  ? B GLU 606  
797  1 Y 1 B SER 596  ? B SER 607  
798  1 Y 1 B ILE 597  ? B ILE 608  
799  1 Y 1 B THR 598  ? B THR 609  
800  1 Y 1 B LEU 599  ? B LEU 610  
801  1 Y 1 B ASP 600  ? B ASP 611  
802  1 Y 1 B TRP 601  ? B TRP 612  
803  1 Y 1 B MET 602  ? B MET 613  
804  1 Y 1 B PHE 603  ? B PHE 614  
805  1 Y 1 B ARG 604  ? B ARG 615  
806  1 Y 1 B TYR 605  ? B TYR 616  
807  1 Y 1 B SER 606  ? B SER 617  
808  1 Y 1 B LEU 607  ? B LEU 618  
809  1 Y 1 B THR 608  ? B THR 619  
810  1 Y 1 B ASN 609  ? B ASN 620  
811  1 Y 1 B ASP 610  ? B ASP 621  
812  1 Y 1 B ILE 611  ? B ILE 622  
813  1 Y 1 B VAL 612  ? B VAL 623  
814  1 Y 1 B LYS 613  ? B LYS 624  
815  1 Y 1 B GLY 614  ? B GLY 625  
816  1 Y 1 B MET 615  ? B MET 626  
817  1 Y 1 B LEU 616  ? B LEU 627  
818  1 Y 1 B PHE 617  ? B PHE 628  
819  1 Y 1 B LEU 618  ? B LEU 629  
820  1 Y 1 B HIS 619  ? B HIS 630  
821  1 Y 1 B ASN 620  ? B ASN 631  
822  1 Y 1 B GLY 621  ? B GLY 632  
823  1 Y 1 B ALA 622  ? B ALA 633  
824  1 Y 1 B ILE 623  ? B ILE 634  
825  1 Y 1 B CYS 624  ? B CYS 635  
826  1 Y 1 B SER 625  ? B SER 636  
827  1 Y 1 B HIS 626  ? B HIS 637  
828  1 Y 1 B GLY 627  ? B GLY 638  
829  1 Y 1 B ASN 628  ? B ASN 639  
830  1 Y 1 B LEU 629  ? B LEU 640  
831  1 Y 1 B LYS 630  ? B LYS 641  
832  1 Y 1 B SER 631  ? B SER 642  
833  1 Y 1 B SER 632  ? B SER 643  
834  1 Y 1 B ASN 633  ? B ASN 644  
835  1 Y 1 B CYS 634  ? B CYS 645  
836  1 Y 1 B VAL 635  ? B VAL 646  
837  1 Y 1 B VAL 636  ? B VAL 647  
838  1 Y 1 B ASP 637  ? B ASP 648  
839  1 Y 1 B GLY 638  ? B GLY 649  
840  1 Y 1 B ARG 639  ? B ARG 650  
841  1 Y 1 B PHE 640  ? B PHE 651  
842  1 Y 1 B VAL 641  ? B VAL 652  
843  1 Y 1 B LEU 642  ? B LEU 653  
844  1 Y 1 B LYS 643  ? B LYS 654  
845  1 Y 1 B ILE 644  ? B ILE 655  
846  1 Y 1 B THR 645  ? B THR 656  
847  1 Y 1 B ASP 646  ? B ASP 657  
848  1 Y 1 B TYR 647  ? B TYR 658  
849  1 Y 1 B GLY 648  ? B GLY 659  
850  1 Y 1 B LEU 649  ? B LEU 660  
851  1 Y 1 B GLU 650  ? B GLU 661  
852  1 Y 1 B SER 651  ? B SER 662  
853  1 Y 1 B PHE 652  ? B PHE 663  
854  1 Y 1 B ARG 653  ? B ARG 664  
855  1 Y 1 B ASP 654  ? B ASP 665  
856  1 Y 1 B LEU 655  ? B LEU 666  
857  1 Y 1 B ASP 656  ? B ASP 667  
858  1 Y 1 B PRO 657  ? B PRO 668  
859  1 Y 1 B GLU 658  ? B GLU 669  
860  1 Y 1 B GLN 659  ? B GLN 670  
861  1 Y 1 B GLY 660  ? B GLY 671  
862  1 Y 1 B HIS 661  ? B HIS 672  
863  1 Y 1 B THR 662  ? B THR 673  
864  1 Y 1 B VAL 663  ? B VAL 674  
865  1 Y 1 B TYR 664  ? B TYR 675  
866  1 Y 1 B ALA 665  ? B ALA 676  
867  1 Y 1 B LYS 666  ? B LYS 677  
868  1 Y 1 B LYS 667  ? B LYS 678  
869  1 Y 1 B LEU 668  ? B LEU 679  
870  1 Y 1 B TRP 669  ? B TRP 680  
871  1 Y 1 B THR 670  ? B THR 681  
872  1 Y 1 B ALA 671  ? B ALA 682  
873  1 Y 1 B PRO 672  ? B PRO 683  
874  1 Y 1 B GLU 673  ? B GLU 684  
875  1 Y 1 B LEU 674  ? B LEU 685  
876  1 Y 1 B LEU 675  ? B LEU 686  
877  1 Y 1 B ARG 676  ? B ARG 687  
878  1 Y 1 B MET 677  ? B MET 688  
879  1 Y 1 B ALA 678  ? B ALA 689  
880  1 Y 1 B SER 679  ? B SER 690  
881  1 Y 1 B PRO 680  ? B PRO 691  
882  1 Y 1 B PRO 681  ? B PRO 692  
883  1 Y 1 B VAL 682  ? B VAL 693  
884  1 Y 1 B ARG 683  ? B ARG 694  
885  1 Y 1 B GLY 684  ? B GLY 695  
886  1 Y 1 B SER 685  ? B SER 696  
887  1 Y 1 B GLN 686  ? B GLN 697  
888  1 Y 1 B ALA 687  ? B ALA 698  
889  1 Y 1 B GLY 688  ? B GLY 699  
890  1 Y 1 B ASP 689  ? B ASP 700  
891  1 Y 1 B VAL 690  ? B VAL 701  
892  1 Y 1 B TYR 691  ? B TYR 702  
893  1 Y 1 B SER 692  ? B SER 703  
894  1 Y 1 B PHE 693  ? B PHE 704  
895  1 Y 1 B GLY 694  ? B GLY 705  
896  1 Y 1 B ILE 695  ? B ILE 706  
897  1 Y 1 B ILE 696  ? B ILE 707  
898  1 Y 1 B LEU 697  ? B LEU 708  
899  1 Y 1 B GLN 698  ? B GLN 709  
900  1 Y 1 B GLU 699  ? B GLU 710  
901  1 Y 1 B ILE 700  ? B ILE 711  
902  1 Y 1 B ALA 701  ? B ALA 712  
903  1 Y 1 B LEU 702  ? B LEU 713  
904  1 Y 1 B ARG 703  ? B ARG 714  
905  1 Y 1 B SER 704  ? B SER 715  
906  1 Y 1 B GLY 705  ? B GLY 716  
907  1 Y 1 B VAL 706  ? B VAL 717  
908  1 Y 1 B PHE 707  ? B PHE 718  
909  1 Y 1 B HIS 708  ? B HIS 719  
910  1 Y 1 B VAL 709  ? B VAL 720  
911  1 Y 1 B GLU 710  ? B GLU 721  
912  1 Y 1 B GLY 711  ? B GLY 722  
913  1 Y 1 B LEU 712  ? B LEU 723  
914  1 Y 1 B ASP 713  ? B ASP 724  
915  1 Y 1 B LEU 714  ? B LEU 725  
916  1 Y 1 B SER 715  ? B SER 726  
917  1 Y 1 B PRO 716  ? B PRO 727  
918  1 Y 1 B LYS 717  ? B LYS 728  
919  1 Y 1 B GLU 718  ? B GLU 729  
920  1 Y 1 B ILE 719  ? B ILE 730  
921  1 Y 1 B ILE 720  ? B ILE 731  
922  1 Y 1 B GLU 721  ? B GLU 732  
923  1 Y 1 B ARG 722  ? B ARG 733  
924  1 Y 1 B VAL 723  ? B VAL 734  
925  1 Y 1 B THR 724  ? B THR 735  
926  1 Y 1 B ARG 725  ? B ARG 736  
927  1 Y 1 B GLY 726  ? B GLY 737  
928  1 Y 1 B GLU 727  ? B GLU 738  
929  1 Y 1 B GLN 728  ? B GLN 739  
930  1 Y 1 B PRO 729  ? B PRO 740  
931  1 Y 1 B PRO 730  ? B PRO 741  
932  1 Y 1 B PHE 731  ? B PHE 742  
933  1 Y 1 B ARG 732  ? B ARG 743  
934  1 Y 1 B PRO 733  ? B PRO 744  
935  1 Y 1 B SER 734  ? B SER 745  
936  1 Y 1 B LEU 735  ? B LEU 746  
937  1 Y 1 B ALA 736  ? B ALA 747  
938  1 Y 1 B LEU 737  ? B LEU 748  
939  1 Y 1 B GLN 738  ? B GLN 749  
940  1 Y 1 B SER 739  ? B SER 750  
941  1 Y 1 B HIS 740  ? B HIS 751  
942  1 Y 1 B LEU 741  ? B LEU 752  
943  1 Y 1 B GLU 742  ? B GLU 753  
944  1 Y 1 B GLU 743  ? B GLU 754  
945  1 Y 1 B LEU 744  ? B LEU 755  
946  1 Y 1 B GLY 745  ? B GLY 756  
947  1 Y 1 B LEU 746  ? B LEU 757  
948  1 Y 1 B LEU 747  ? B LEU 758  
949  1 Y 1 B MET 748  ? B MET 759  
950  1 Y 1 B GLN 749  ? B GLN 760  
951  1 Y 1 B ARG 750  ? B ARG 761  
952  1 Y 1 B CYS 751  ? B CYS 762  
953  1 Y 1 B TRP 752  ? B TRP 763  
954  1 Y 1 B ALA 753  ? B ALA 764  
955  1 Y 1 B GLU 754  ? B GLU 765  
956  1 Y 1 B ASP 755  ? B ASP 766  
957  1 Y 1 B PRO 756  ? B PRO 767  
958  1 Y 1 B GLN 757  ? B GLN 768  
959  1 Y 1 B GLU 758  ? B GLU 769  
960  1 Y 1 B ARG 759  ? B ARG 770  
961  1 Y 1 B PRO 760  ? B PRO 771  
962  1 Y 1 B PRO 761  ? B PRO 772  
963  1 Y 1 B PHE 762  ? B PHE 773  
964  1 Y 1 B GLN 763  ? B GLN 774  
965  1 Y 1 B GLN 764  ? B GLN 775  
966  1 Y 1 B ILE 765  ? B ILE 776  
967  1 Y 1 B ARG 766  ? B ARG 777  
968  1 Y 1 B LEU 767  ? B LEU 778  
969  1 Y 1 B THR 768  ? B THR 779  
970  1 Y 1 B LEU 769  ? B LEU 780  
971  1 Y 1 B ARG 770  ? B ARG 781  
972  1 Y 1 B LYS 771  ? B LYS 782  
973  1 Y 1 B PHE 772  ? B PHE 783  
974  1 Y 1 B ASN 773  ? B ASN 784  
975  1 Y 1 B ARG 774  ? B ARG 785  
976  1 Y 1 B GLU 775  ? B GLU 786  
977  1 Y 1 B ASN 776  ? B ASN 787  
978  1 Y 1 B SER 777  ? B SER 788  
979  1 Y 1 B SER 778  ? B SER 789  
980  1 Y 1 B ASN 779  ? B ASN 790  
981  1 Y 1 B ILE 780  ? B ILE 791  
982  1 Y 1 B LEU 781  ? B LEU 792  
983  1 Y 1 B ASP 782  ? B ASP 793  
984  1 Y 1 B ASN 783  ? B ASN 794  
985  1 Y 1 B LEU 784  ? B LEU 795  
986  1 Y 1 B LEU 785  ? B LEU 796  
987  1 Y 1 B SER 786  ? B SER 797  
988  1 Y 1 B ARG 787  ? B ARG 798  
989  1 Y 1 B MET 788  ? B MET 799  
990  1 Y 1 B GLU 789  ? B GLU 800  
991  1 Y 1 B GLN 790  ? B GLN 801  
992  1 Y 1 B TYR 791  ? B TYR 802  
993  1 Y 1 B ALA 792  ? B ALA 803  
994  1 Y 1 B ASN 793  ? B ASN 804  
995  1 Y 1 B ASN 794  ? B ASN 805  
996  1 Y 1 B LEU 795  ? B LEU 806  
997  1 Y 1 B GLU 796  ? B GLU 807  
998  1 Y 1 B GLU 797  ? B GLU 808  
999  1 Y 1 B LEU 798  ? B LEU 809  
1000 1 Y 1 B VAL 799  ? B VAL 810  
1001 1 Y 1 B GLU 800  ? B GLU 811  
1002 1 Y 1 B GLU 801  ? B GLU 812  
1003 1 Y 1 B ARG 802  ? B ARG 813  
1004 1 Y 1 B THR 803  ? B THR 814  
1005 1 Y 1 B GLN 804  ? B GLN 815  
1006 1 Y 1 B ALA 805  ? B ALA 816  
1007 1 Y 1 B TYR 806  ? B TYR 817  
1008 1 Y 1 B LEU 807  ? B LEU 818  
1009 1 Y 1 B GLU 808  ? B GLU 819  
1010 1 Y 1 B GLU 809  ? B GLU 820  
1011 1 Y 1 B LYS 810  ? B LYS 821  
1012 1 Y 1 B ARG 811  ? B ARG 822  
1013 1 Y 1 B LYS 812  ? B LYS 823  
1014 1 Y 1 B ALA 813  ? B ALA 824  
1015 1 Y 1 B GLU 814  ? B GLU 825  
1016 1 Y 1 B ALA 815  ? B ALA 826  
1017 1 Y 1 B LEU 816  ? B LEU 827  
1018 1 Y 1 B LEU 817  ? B LEU 828  
1019 1 Y 1 B TYR 818  ? B TYR 829  
1020 1 Y 1 B GLN 819  ? B GLN 830  
1021 1 Y 1 B ILE 820  ? B ILE 831  
1022 1 Y 1 B LEU 821  ? B LEU 832  
1023 1 Y 1 B PRO 822  ? B PRO 833  
1024 1 Y 1 B HIS 823  ? B HIS 834  
1025 1 Y 1 B SER 824  ? B SER 835  
1026 1 Y 1 B VAL 825  ? B VAL 836  
1027 1 Y 1 B ALA 826  ? B ALA 837  
1028 1 Y 1 B GLU 827  ? B GLU 838  
1029 1 Y 1 B GLN 828  ? B GLN 839  
1030 1 Y 1 B LEU 829  ? B LEU 840  
1031 1 Y 1 B LYS 830  ? B LYS 841  
1032 1 Y 1 B ARG 831  ? B ARG 842  
1033 1 Y 1 B GLY 832  ? B GLY 843  
1034 1 Y 1 B GLU 833  ? B GLU 844  
1035 1 Y 1 B THR 834  ? B THR 845  
1036 1 Y 1 B VAL 835  ? B VAL 846  
1037 1 Y 1 B GLN 836  ? B GLN 847  
1038 1 Y 1 B ALA 837  ? B ALA 848  
1039 1 Y 1 B GLU 838  ? B GLU 849  
1040 1 Y 1 B ALA 839  ? B ALA 850  
1041 1 Y 1 B PHE 840  ? B PHE 851  
1042 1 Y 1 B ASP 841  ? B ASP 852  
1043 1 Y 1 B SER 842  ? B SER 853  
1044 1 Y 1 B VAL 843  ? B VAL 854  
1045 1 Y 1 B THR 844  ? B THR 855  
1046 1 Y 1 B ILE 845  ? B ILE 856  
1047 1 Y 1 B TYR 846  ? B TYR 857  
1048 1 Y 1 B PHE 847  ? B PHE 858  
1049 1 Y 1 B SER 848  ? B SER 859  
1050 1 Y 1 B ASP 849  ? B ASP 860  
1051 1 Y 1 B ILE 850  ? B ILE 861  
1052 1 Y 1 B VAL 851  ? B VAL 862  
1053 1 Y 1 B GLY 852  ? B GLY 863  
1054 1 Y 1 B PHE 853  ? B PHE 864  
1055 1 Y 1 B THR 854  ? B THR 865  
1056 1 Y 1 B ALA 855  ? B ALA 866  
1057 1 Y 1 B LEU 856  ? B LEU 867  
1058 1 Y 1 B SER 857  ? B SER 868  
1059 1 Y 1 B ALA 858  ? B ALA 869  
1060 1 Y 1 B GLU 859  ? B GLU 870  
1061 1 Y 1 B SER 860  ? B SER 871  
1062 1 Y 1 B THR 861  ? B THR 872  
1063 1 Y 1 B PRO 862  ? B PRO 873  
1064 1 Y 1 B MET 863  ? B MET 874  
1065 1 Y 1 B GLN 864  ? B GLN 875  
1066 1 Y 1 B VAL 865  ? B VAL 876  
1067 1 Y 1 B VAL 866  ? B VAL 877  
1068 1 Y 1 B THR 867  ? B THR 878  
1069 1 Y 1 B LEU 868  ? B LEU 879  
1070 1 Y 1 B LEU 869  ? B LEU 880  
1071 1 Y 1 B ASN 870  ? B ASN 881  
1072 1 Y 1 B ASP 871  ? B ASP 882  
1073 1 Y 1 B LEU 872  ? B LEU 883  
1074 1 Y 1 B TYR 873  ? B TYR 884  
1075 1 Y 1 B THR 874  ? B THR 885  
1076 1 Y 1 B CYS 875  ? B CYS 886  
1077 1 Y 1 B PHE 876  ? B PHE 887  
1078 1 Y 1 B ASP 877  ? B ASP 888  
1079 1 Y 1 B ALA 878  ? B ALA 889  
1080 1 Y 1 B VAL 879  ? B VAL 890  
1081 1 Y 1 B ILE 880  ? B ILE 891  
1082 1 Y 1 B ASP 881  ? B ASP 892  
1083 1 Y 1 B ASN 882  ? B ASN 893  
1084 1 Y 1 B PHE 883  ? B PHE 894  
1085 1 Y 1 B ASP 884  ? B ASP 895  
1086 1 Y 1 B VAL 885  ? B VAL 896  
1087 1 Y 1 B TYR 886  ? B TYR 897  
1088 1 Y 1 B LYS 887  ? B LYS 898  
1089 1 Y 1 B VAL 888  ? B VAL 899  
1090 1 Y 1 B GLU 889  ? B GLU 900  
1091 1 Y 1 B THR 890  ? B THR 901  
1092 1 Y 1 B ILE 891  ? B ILE 902  
1093 1 Y 1 B GLY 892  ? B GLY 903  
1094 1 Y 1 B ASP 893  ? B ASP 904  
1095 1 Y 1 B ALA 894  ? B ALA 905  
1096 1 Y 1 B TYR 895  ? B TYR 906  
1097 1 Y 1 B MET 896  ? B MET 907  
1098 1 Y 1 B VAL 897  ? B VAL 908  
1099 1 Y 1 B VAL 898  ? B VAL 909  
1100 1 Y 1 B SER 899  ? B SER 910  
1101 1 Y 1 B GLY 900  ? B GLY 911  
1102 1 Y 1 B LEU 901  ? B LEU 912  
1103 1 Y 1 B PRO 902  ? B PRO 913  
1104 1 Y 1 B VAL 903  ? B VAL 914  
1105 1 Y 1 B ARG 904  ? B ARG 915  
1106 1 Y 1 B ASN 905  ? B ASN 916  
1107 1 Y 1 B GLY 906  ? B GLY 917  
1108 1 Y 1 B ARG 907  ? B ARG 918  
1109 1 Y 1 B LEU 908  ? B LEU 919  
1110 1 Y 1 B HIS 909  ? B HIS 920  
1111 1 Y 1 B ALA 910  ? B ALA 921  
1112 1 Y 1 B CYS 911  ? B CYS 922  
1113 1 Y 1 B GLU 912  ? B GLU 923  
1114 1 Y 1 B VAL 913  ? B VAL 924  
1115 1 Y 1 B ALA 914  ? B ALA 925  
1116 1 Y 1 B ARG 915  ? B ARG 926  
1117 1 Y 1 B MET 916  ? B MET 927  
1118 1 Y 1 B ALA 917  ? B ALA 928  
1119 1 Y 1 B LEU 918  ? B LEU 929  
1120 1 Y 1 B ALA 919  ? B ALA 930  
1121 1 Y 1 B LEU 920  ? B LEU 931  
1122 1 Y 1 B LEU 921  ? B LEU 932  
1123 1 Y 1 B ASP 922  ? B ASP 933  
1124 1 Y 1 B ALA 923  ? B ALA 934  
1125 1 Y 1 B VAL 924  ? B VAL 935  
1126 1 Y 1 B ARG 925  ? B ARG 936  
1127 1 Y 1 B SER 926  ? B SER 937  
1128 1 Y 1 B PHE 927  ? B PHE 938  
1129 1 Y 1 B ARG 928  ? B ARG 939  
1130 1 Y 1 B ILE 929  ? B ILE 940  
1131 1 Y 1 B ARG 930  ? B ARG 941  
1132 1 Y 1 B HIS 931  ? B HIS 942  
1133 1 Y 1 B ARG 932  ? B ARG 943  
1134 1 Y 1 B PRO 933  ? B PRO 944  
1135 1 Y 1 B GLN 934  ? B GLN 945  
1136 1 Y 1 B GLU 935  ? B GLU 946  
1137 1 Y 1 B GLN 936  ? B GLN 947  
1138 1 Y 1 B LEU 937  ? B LEU 948  
1139 1 Y 1 B ARG 938  ? B ARG 949  
1140 1 Y 1 B LEU 939  ? B LEU 950  
1141 1 Y 1 B ARG 940  ? B ARG 951  
1142 1 Y 1 B ILE 941  ? B ILE 952  
1143 1 Y 1 B GLY 942  ? B GLY 953  
1144 1 Y 1 B ILE 943  ? B ILE 954  
1145 1 Y 1 B HIS 944  ? B HIS 955  
1146 1 Y 1 B THR 945  ? B THR 956  
1147 1 Y 1 B GLY 946  ? B GLY 957  
1148 1 Y 1 B PRO 947  ? B PRO 958  
1149 1 Y 1 B VAL 948  ? B VAL 959  
1150 1 Y 1 B CYS 949  ? B CYS 960  
1151 1 Y 1 B ALA 950  ? B ALA 961  
1152 1 Y 1 B GLY 951  ? B GLY 962  
1153 1 Y 1 B VAL 952  ? B VAL 963  
1154 1 Y 1 B VAL 953  ? B VAL 964  
1155 1 Y 1 B GLY 954  ? B GLY 965  
1156 1 Y 1 B LEU 955  ? B LEU 966  
1157 1 Y 1 B LYS 956  ? B LYS 967  
1158 1 Y 1 B MET 957  ? B MET 968  
1159 1 Y 1 B PRO 958  ? B PRO 969  
1160 1 Y 1 B ARG 959  ? B ARG 970  
1161 1 Y 1 B TYR 960  ? B TYR 971  
1162 1 Y 1 B CYS 961  ? B CYS 972  
1163 1 Y 1 B LEU 962  ? B LEU 973  
1164 1 Y 1 B PHE 963  ? B PHE 974  
1165 1 Y 1 B GLY 964  ? B GLY 975  
1166 1 Y 1 B ASP 965  ? B ASP 976  
1167 1 Y 1 B THR 966  ? B THR 977  
1168 1 Y 1 B VAL 967  ? B VAL 978  
1169 1 Y 1 B ASN 968  ? B ASN 979  
1170 1 Y 1 B THR 969  ? B THR 980  
1171 1 Y 1 B ALA 970  ? B ALA 981  
1172 1 Y 1 B SER 971  ? B SER 982  
1173 1 Y 1 B ARG 972  ? B ARG 983  
1174 1 Y 1 B MET 973  ? B MET 984  
1175 1 Y 1 B GLU 974  ? B GLU 985  
1176 1 Y 1 B SER 975  ? B SER 986  
1177 1 Y 1 B ASN 976  ? B ASN 987  
1178 1 Y 1 B GLY 977  ? B GLY 988  
1179 1 Y 1 B GLU 978  ? B GLU 989  
1180 1 Y 1 B ALA 979  ? B ALA 990  
1181 1 Y 1 B LEU 980  ? B LEU 991  
1182 1 Y 1 B LYS 981  ? B LYS 992  
1183 1 Y 1 B ILE 982  ? B ILE 993  
1184 1 Y 1 B HIS 983  ? B HIS 994  
1185 1 Y 1 B LEU 984  ? B LEU 995  
1186 1 Y 1 B SER 985  ? B SER 996  
1187 1 Y 1 B SER 986  ? B SER 997  
1188 1 Y 1 B GLU 987  ? B GLU 998  
1189 1 Y 1 B THR 988  ? B THR 999  
1190 1 Y 1 B LYS 989  ? B LYS 1000 
1191 1 Y 1 B ALA 990  ? B ALA 1001 
1192 1 Y 1 B VAL 991  ? B VAL 1002 
1193 1 Y 1 B LEU 992  ? B LEU 1003 
1194 1 Y 1 B GLU 993  ? B GLU 1004 
1195 1 Y 1 B GLU 994  ? B GLU 1005 
1196 1 Y 1 B PHE 995  ? B PHE 1006 
1197 1 Y 1 B GLY 996  ? B GLY 1007 
1198 1 Y 1 B GLY 997  ? B GLY 1008 
1199 1 Y 1 B PHE 998  ? B PHE 1009 
1200 1 Y 1 B GLU 999  ? B GLU 1010 
1201 1 Y 1 B LEU 1000 ? B LEU 1011 
1202 1 Y 1 B GLU 1001 ? B GLU 1012 
1203 1 Y 1 B LEU 1002 ? B LEU 1013 
1204 1 Y 1 B ARG 1003 ? B ARG 1014 
1205 1 Y 1 B GLY 1004 ? B GLY 1015 
1206 1 Y 1 B ASP 1005 ? B ASP 1016 
1207 1 Y 1 B VAL 1006 ? B VAL 1017 
1208 1 Y 1 B GLU 1007 ? B GLU 1018 
1209 1 Y 1 B MET 1008 ? B MET 1019 
1210 1 Y 1 B LYS 1009 ? B LYS 1020 
1211 1 Y 1 B GLY 1010 ? B GLY 1021 
1212 1 Y 1 B LYS 1011 ? B LYS 1022 
1213 1 Y 1 B GLY 1012 ? B GLY 1023 
1214 1 Y 1 B LYS 1013 ? B LYS 1024 
1215 1 Y 1 B VAL 1014 ? B VAL 1025 
1216 1 Y 1 B ARG 1015 ? B ARG 1026 
1217 1 Y 1 B THR 1016 ? B THR 1027 
1218 1 Y 1 B TYR 1017 ? B TYR 1028 
1219 1 Y 1 B TRP 1018 ? B TRP 1029 
1220 1 Y 1 B LEU 1019 ? B LEU 1030 
1221 1 Y 1 B LEU 1020 ? B LEU 1031 
1222 1 Y 1 B GLY 1021 ? B GLY 1032 
1223 1 Y 1 B GLU 1022 ? B GLU 1033 
1224 1 Y 1 B ARG 1023 ? B ARG 1034 
1225 1 Y 1 B GLY 1024 ? B GLY 1035 
1226 1 Y 1 B SER 1025 ? B SER 1036 
1227 1 Y 1 B SER 1026 ? B SER 1037 
1228 1 Y 1 B THR 1027 ? B THR 1038 
1229 1 Y 1 B ARG 1028 ? B ARG 1039 
1230 1 Y 1 B GLY 1029 ? B GLY 1040 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CL  CL   CL N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
GLN N    N  N N 89  
GLN CA   C  N S 90  
GLN C    C  N N 91  
GLN O    O  N N 92  
GLN CB   C  N N 93  
GLN CG   C  N N 94  
GLN CD   C  N N 95  
GLN OE1  O  N N 96  
GLN NE2  N  N N 97  
GLN OXT  O  N N 98  
GLN H    H  N N 99  
GLN H2   H  N N 100 
GLN HA   H  N N 101 
GLN HB2  H  N N 102 
GLN HB3  H  N N 103 
GLN HG2  H  N N 104 
GLN HG3  H  N N 105 
GLN HE21 H  N N 106 
GLN HE22 H  N N 107 
GLN HXT  H  N N 108 
GLU N    N  N N 109 
GLU CA   C  N S 110 
GLU C    C  N N 111 
GLU O    O  N N 112 
GLU CB   C  N N 113 
GLU CG   C  N N 114 
GLU CD   C  N N 115 
GLU OE1  O  N N 116 
GLU OE2  O  N N 117 
GLU OXT  O  N N 118 
GLU H    H  N N 119 
GLU H2   H  N N 120 
GLU HA   H  N N 121 
GLU HB2  H  N N 122 
GLU HB3  H  N N 123 
GLU HG2  H  N N 124 
GLU HG3  H  N N 125 
GLU HE2  H  N N 126 
GLU HXT  H  N N 127 
GLY N    N  N N 128 
GLY CA   C  N N 129 
GLY C    C  N N 130 
GLY O    O  N N 131 
GLY OXT  O  N N 132 
GLY H    H  N N 133 
GLY H2   H  N N 134 
GLY HA2  H  N N 135 
GLY HA3  H  N N 136 
GLY HXT  H  N N 137 
HIS N    N  N N 138 
HIS CA   C  N S 139 
HIS C    C  N N 140 
HIS O    O  N N 141 
HIS CB   C  N N 142 
HIS CG   C  Y N 143 
HIS ND1  N  Y N 144 
HIS CD2  C  Y N 145 
HIS CE1  C  Y N 146 
HIS NE2  N  Y N 147 
HIS OXT  O  N N 148 
HIS H    H  N N 149 
HIS H2   H  N N 150 
HIS HA   H  N N 151 
HIS HB2  H  N N 152 
HIS HB3  H  N N 153 
HIS HD1  H  N N 154 
HIS HD2  H  N N 155 
HIS HE1  H  N N 156 
HIS HE2  H  N N 157 
HIS HXT  H  N N 158 
ILE N    N  N N 159 
ILE CA   C  N S 160 
ILE C    C  N N 161 
ILE O    O  N N 162 
ILE CB   C  N S 163 
ILE CG1  C  N N 164 
ILE CG2  C  N N 165 
ILE CD1  C  N N 166 
ILE OXT  O  N N 167 
ILE H    H  N N 168 
ILE H2   H  N N 169 
ILE HA   H  N N 170 
ILE HB   H  N N 171 
ILE HG12 H  N N 172 
ILE HG13 H  N N 173 
ILE HG21 H  N N 174 
ILE HG22 H  N N 175 
ILE HG23 H  N N 176 
ILE HD11 H  N N 177 
ILE HD12 H  N N 178 
ILE HD13 H  N N 179 
ILE HXT  H  N N 180 
LEU N    N  N N 181 
LEU CA   C  N S 182 
LEU C    C  N N 183 
LEU O    O  N N 184 
LEU CB   C  N N 185 
LEU CG   C  N N 186 
LEU CD1  C  N N 187 
LEU CD2  C  N N 188 
LEU OXT  O  N N 189 
LEU H    H  N N 190 
LEU H2   H  N N 191 
LEU HA   H  N N 192 
LEU HB2  H  N N 193 
LEU HB3  H  N N 194 
LEU HG   H  N N 195 
LEU HD11 H  N N 196 
LEU HD12 H  N N 197 
LEU HD13 H  N N 198 
LEU HD21 H  N N 199 
LEU HD22 H  N N 200 
LEU HD23 H  N N 201 
LEU HXT  H  N N 202 
LYS N    N  N N 203 
LYS CA   C  N S 204 
LYS C    C  N N 205 
LYS O    O  N N 206 
LYS CB   C  N N 207 
LYS CG   C  N N 208 
LYS CD   C  N N 209 
LYS CE   C  N N 210 
LYS NZ   N  N N 211 
LYS OXT  O  N N 212 
LYS H    H  N N 213 
LYS H2   H  N N 214 
LYS HA   H  N N 215 
LYS HB2  H  N N 216 
LYS HB3  H  N N 217 
LYS HG2  H  N N 218 
LYS HG3  H  N N 219 
LYS HD2  H  N N 220 
LYS HD3  H  N N 221 
LYS HE2  H  N N 222 
LYS HE3  H  N N 223 
LYS HZ1  H  N N 224 
LYS HZ2  H  N N 225 
LYS HZ3  H  N N 226 
LYS HXT  H  N N 227 
MAN C1   C  N S 228 
MAN C2   C  N S 229 
MAN C3   C  N S 230 
MAN C4   C  N S 231 
MAN C5   C  N R 232 
MAN C6   C  N N 233 
MAN O1   O  N N 234 
MAN O2   O  N N 235 
MAN O3   O  N N 236 
MAN O4   O  N N 237 
MAN O5   O  N N 238 
MAN O6   O  N N 239 
MAN H1   H  N N 240 
MAN H2   H  N N 241 
MAN H3   H  N N 242 
MAN H4   H  N N 243 
MAN H5   H  N N 244 
MAN H61  H  N N 245 
MAN H62  H  N N 246 
MAN HO1  H  N N 247 
MAN HO2  H  N N 248 
MAN HO3  H  N N 249 
MAN HO4  H  N N 250 
MAN HO6  H  N N 251 
MET N    N  N N 252 
MET CA   C  N S 253 
MET C    C  N N 254 
MET O    O  N N 255 
MET CB   C  N N 256 
MET CG   C  N N 257 
MET SD   S  N N 258 
MET CE   C  N N 259 
MET OXT  O  N N 260 
MET H    H  N N 261 
MET H2   H  N N 262 
MET HA   H  N N 263 
MET HB2  H  N N 264 
MET HB3  H  N N 265 
MET HG2  H  N N 266 
MET HG3  H  N N 267 
MET HE1  H  N N 268 
MET HE2  H  N N 269 
MET HE3  H  N N 270 
MET HXT  H  N N 271 
NAG C1   C  N R 272 
NAG C2   C  N R 273 
NAG C3   C  N R 274 
NAG C4   C  N S 275 
NAG C5   C  N R 276 
NAG C6   C  N N 277 
NAG C7   C  N N 278 
NAG C8   C  N N 279 
NAG N2   N  N N 280 
NAG O1   O  N N 281 
NAG O3   O  N N 282 
NAG O4   O  N N 283 
NAG O5   O  N N 284 
NAG O6   O  N N 285 
NAG O7   O  N N 286 
NAG H1   H  N N 287 
NAG H2   H  N N 288 
NAG H3   H  N N 289 
NAG H4   H  N N 290 
NAG H5   H  N N 291 
NAG H61  H  N N 292 
NAG H62  H  N N 293 
NAG H81  H  N N 294 
NAG H82  H  N N 295 
NAG H83  H  N N 296 
NAG HN2  H  N N 297 
NAG HO1  H  N N 298 
NAG HO3  H  N N 299 
NAG HO4  H  N N 300 
NAG HO6  H  N N 301 
PHE N    N  N N 302 
PHE CA   C  N S 303 
PHE C    C  N N 304 
PHE O    O  N N 305 
PHE CB   C  N N 306 
PHE CG   C  Y N 307 
PHE CD1  C  Y N 308 
PHE CD2  C  Y N 309 
PHE CE1  C  Y N 310 
PHE CE2  C  Y N 311 
PHE CZ   C  Y N 312 
PHE OXT  O  N N 313 
PHE H    H  N N 314 
PHE H2   H  N N 315 
PHE HA   H  N N 316 
PHE HB2  H  N N 317 
PHE HB3  H  N N 318 
PHE HD1  H  N N 319 
PHE HD2  H  N N 320 
PHE HE1  H  N N 321 
PHE HE2  H  N N 322 
PHE HZ   H  N N 323 
PHE HXT  H  N N 324 
PRO N    N  N N 325 
PRO CA   C  N S 326 
PRO C    C  N N 327 
PRO O    O  N N 328 
PRO CB   C  N N 329 
PRO CG   C  N N 330 
PRO CD   C  N N 331 
PRO OXT  O  N N 332 
PRO H    H  N N 333 
PRO HA   H  N N 334 
PRO HB2  H  N N 335 
PRO HB3  H  N N 336 
PRO HG2  H  N N 337 
PRO HG3  H  N N 338 
PRO HD2  H  N N 339 
PRO HD3  H  N N 340 
PRO HXT  H  N N 341 
SER N    N  N N 342 
SER CA   C  N S 343 
SER C    C  N N 344 
SER O    O  N N 345 
SER CB   C  N N 346 
SER OG   O  N N 347 
SER OXT  O  N N 348 
SER H    H  N N 349 
SER H2   H  N N 350 
SER HA   H  N N 351 
SER HB2  H  N N 352 
SER HB3  H  N N 353 
SER HG   H  N N 354 
SER HXT  H  N N 355 
THR N    N  N N 356 
THR CA   C  N S 357 
THR C    C  N N 358 
THR O    O  N N 359 
THR CB   C  N R 360 
THR OG1  O  N N 361 
THR CG2  C  N N 362 
THR OXT  O  N N 363 
THR H    H  N N 364 
THR H2   H  N N 365 
THR HA   H  N N 366 
THR HB   H  N N 367 
THR HG1  H  N N 368 
THR HG21 H  N N 369 
THR HG22 H  N N 370 
THR HG23 H  N N 371 
THR HXT  H  N N 372 
TRP N    N  N N 373 
TRP CA   C  N S 374 
TRP C    C  N N 375 
TRP O    O  N N 376 
TRP CB   C  N N 377 
TRP CG   C  Y N 378 
TRP CD1  C  Y N 379 
TRP CD2  C  Y N 380 
TRP NE1  N  Y N 381 
TRP CE2  C  Y N 382 
TRP CE3  C  Y N 383 
TRP CZ2  C  Y N 384 
TRP CZ3  C  Y N 385 
TRP CH2  C  Y N 386 
TRP OXT  O  N N 387 
TRP H    H  N N 388 
TRP H2   H  N N 389 
TRP HA   H  N N 390 
TRP HB2  H  N N 391 
TRP HB3  H  N N 392 
TRP HD1  H  N N 393 
TRP HE1  H  N N 394 
TRP HE3  H  N N 395 
TRP HZ2  H  N N 396 
TRP HZ3  H  N N 397 
TRP HH2  H  N N 398 
TRP HXT  H  N N 399 
TYR N    N  N N 400 
TYR CA   C  N S 401 
TYR C    C  N N 402 
TYR O    O  N N 403 
TYR CB   C  N N 404 
TYR CG   C  Y N 405 
TYR CD1  C  Y N 406 
TYR CD2  C  Y N 407 
TYR CE1  C  Y N 408 
TYR CE2  C  Y N 409 
TYR CZ   C  Y N 410 
TYR OH   O  N N 411 
TYR OXT  O  N N 412 
TYR H    H  N N 413 
TYR H2   H  N N 414 
TYR HA   H  N N 415 
TYR HB2  H  N N 416 
TYR HB3  H  N N 417 
TYR HD1  H  N N 418 
TYR HD2  H  N N 419 
TYR HE1  H  N N 420 
TYR HE2  H  N N 421 
TYR HH   H  N N 422 
TYR HXT  H  N N 423 
VAL N    N  N N 424 
VAL CA   C  N S 425 
VAL C    C  N N 426 
VAL O    O  N N 427 
VAL CB   C  N N 428 
VAL CG1  C  N N 429 
VAL CG2  C  N N 430 
VAL OXT  O  N N 431 
VAL H    H  N N 432 
VAL H2   H  N N 433 
VAL HA   H  N N 434 
VAL HB   H  N N 435 
VAL HG11 H  N N 436 
VAL HG12 H  N N 437 
VAL HG13 H  N N 438 
VAL HG21 H  N N 439 
VAL HG22 H  N N 440 
VAL HG23 H  N N 441 
VAL HXT  H  N N 442 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
ILE N   CA   sing N N 150 
ILE N   H    sing N N 151 
ILE N   H2   sing N N 152 
ILE CA  C    sing N N 153 
ILE CA  CB   sing N N 154 
ILE CA  HA   sing N N 155 
ILE C   O    doub N N 156 
ILE C   OXT  sing N N 157 
ILE CB  CG1  sing N N 158 
ILE CB  CG2  sing N N 159 
ILE CB  HB   sing N N 160 
ILE CG1 CD1  sing N N 161 
ILE CG1 HG12 sing N N 162 
ILE CG1 HG13 sing N N 163 
ILE CG2 HG21 sing N N 164 
ILE CG2 HG22 sing N N 165 
ILE CG2 HG23 sing N N 166 
ILE CD1 HD11 sing N N 167 
ILE CD1 HD12 sing N N 168 
ILE CD1 HD13 sing N N 169 
ILE OXT HXT  sing N N 170 
LEU N   CA   sing N N 171 
LEU N   H    sing N N 172 
LEU N   H2   sing N N 173 
LEU CA  C    sing N N 174 
LEU CA  CB   sing N N 175 
LEU CA  HA   sing N N 176 
LEU C   O    doub N N 177 
LEU C   OXT  sing N N 178 
LEU CB  CG   sing N N 179 
LEU CB  HB2  sing N N 180 
LEU CB  HB3  sing N N 181 
LEU CG  CD1  sing N N 182 
LEU CG  CD2  sing N N 183 
LEU CG  HG   sing N N 184 
LEU CD1 HD11 sing N N 185 
LEU CD1 HD12 sing N N 186 
LEU CD1 HD13 sing N N 187 
LEU CD2 HD21 sing N N 188 
LEU CD2 HD22 sing N N 189 
LEU CD2 HD23 sing N N 190 
LEU OXT HXT  sing N N 191 
LYS N   CA   sing N N 192 
LYS N   H    sing N N 193 
LYS N   H2   sing N N 194 
LYS CA  C    sing N N 195 
LYS CA  CB   sing N N 196 
LYS CA  HA   sing N N 197 
LYS C   O    doub N N 198 
LYS C   OXT  sing N N 199 
LYS CB  CG   sing N N 200 
LYS CB  HB2  sing N N 201 
LYS CB  HB3  sing N N 202 
LYS CG  CD   sing N N 203 
LYS CG  HG2  sing N N 204 
LYS CG  HG3  sing N N 205 
LYS CD  CE   sing N N 206 
LYS CD  HD2  sing N N 207 
LYS CD  HD3  sing N N 208 
LYS CE  NZ   sing N N 209 
LYS CE  HE2  sing N N 210 
LYS CE  HE3  sing N N 211 
LYS NZ  HZ1  sing N N 212 
LYS NZ  HZ2  sing N N 213 
LYS NZ  HZ3  sing N N 214 
LYS OXT HXT  sing N N 215 
MAN C1  C2   sing N N 216 
MAN C1  O1   sing N N 217 
MAN C1  O5   sing N N 218 
MAN C1  H1   sing N N 219 
MAN C2  C3   sing N N 220 
MAN C2  O2   sing N N 221 
MAN C2  H2   sing N N 222 
MAN C3  C4   sing N N 223 
MAN C3  O3   sing N N 224 
MAN C3  H3   sing N N 225 
MAN C4  C5   sing N N 226 
MAN C4  O4   sing N N 227 
MAN C4  H4   sing N N 228 
MAN C5  C6   sing N N 229 
MAN C5  O5   sing N N 230 
MAN C5  H5   sing N N 231 
MAN C6  O6   sing N N 232 
MAN C6  H61  sing N N 233 
MAN C6  H62  sing N N 234 
MAN O1  HO1  sing N N 235 
MAN O2  HO2  sing N N 236 
MAN O3  HO3  sing N N 237 
MAN O4  HO4  sing N N 238 
MAN O6  HO6  sing N N 239 
MET N   CA   sing N N 240 
MET N   H    sing N N 241 
MET N   H2   sing N N 242 
MET CA  C    sing N N 243 
MET CA  CB   sing N N 244 
MET CA  HA   sing N N 245 
MET C   O    doub N N 246 
MET C   OXT  sing N N 247 
MET CB  CG   sing N N 248 
MET CB  HB2  sing N N 249 
MET CB  HB3  sing N N 250 
MET CG  SD   sing N N 251 
MET CG  HG2  sing N N 252 
MET CG  HG3  sing N N 253 
MET SD  CE   sing N N 254 
MET CE  HE1  sing N N 255 
MET CE  HE2  sing N N 256 
MET CE  HE3  sing N N 257 
MET OXT HXT  sing N N 258 
NAG C1  C2   sing N N 259 
NAG C1  O1   sing N N 260 
NAG C1  O5   sing N N 261 
NAG C1  H1   sing N N 262 
NAG C2  C3   sing N N 263 
NAG C2  N2   sing N N 264 
NAG C2  H2   sing N N 265 
NAG C3  C4   sing N N 266 
NAG C3  O3   sing N N 267 
NAG C3  H3   sing N N 268 
NAG C4  C5   sing N N 269 
NAG C4  O4   sing N N 270 
NAG C4  H4   sing N N 271 
NAG C5  C6   sing N N 272 
NAG C5  O5   sing N N 273 
NAG C5  H5   sing N N 274 
NAG C6  O6   sing N N 275 
NAG C6  H61  sing N N 276 
NAG C6  H62  sing N N 277 
NAG C7  C8   sing N N 278 
NAG C7  N2   sing N N 279 
NAG C7  O7   doub N N 280 
NAG C8  H81  sing N N 281 
NAG C8  H82  sing N N 282 
NAG C8  H83  sing N N 283 
NAG N2  HN2  sing N N 284 
NAG O1  HO1  sing N N 285 
NAG O3  HO3  sing N N 286 
NAG O4  HO4  sing N N 287 
NAG O6  HO6  sing N N 288 
PHE N   CA   sing N N 289 
PHE N   H    sing N N 290 
PHE N   H2   sing N N 291 
PHE CA  C    sing N N 292 
PHE CA  CB   sing N N 293 
PHE CA  HA   sing N N 294 
PHE C   O    doub N N 295 
PHE C   OXT  sing N N 296 
PHE CB  CG   sing N N 297 
PHE CB  HB2  sing N N 298 
PHE CB  HB3  sing N N 299 
PHE CG  CD1  doub Y N 300 
PHE CG  CD2  sing Y N 301 
PHE CD1 CE1  sing Y N 302 
PHE CD1 HD1  sing N N 303 
PHE CD2 CE2  doub Y N 304 
PHE CD2 HD2  sing N N 305 
PHE CE1 CZ   doub Y N 306 
PHE CE1 HE1  sing N N 307 
PHE CE2 CZ   sing Y N 308 
PHE CE2 HE2  sing N N 309 
PHE CZ  HZ   sing N N 310 
PHE OXT HXT  sing N N 311 
PRO N   CA   sing N N 312 
PRO N   CD   sing N N 313 
PRO N   H    sing N N 314 
PRO CA  C    sing N N 315 
PRO CA  CB   sing N N 316 
PRO CA  HA   sing N N 317 
PRO C   O    doub N N 318 
PRO C   OXT  sing N N 319 
PRO CB  CG   sing N N 320 
PRO CB  HB2  sing N N 321 
PRO CB  HB3  sing N N 322 
PRO CG  CD   sing N N 323 
PRO CG  HG2  sing N N 324 
PRO CG  HG3  sing N N 325 
PRO CD  HD2  sing N N 326 
PRO CD  HD3  sing N N 327 
PRO OXT HXT  sing N N 328 
SER N   CA   sing N N 329 
SER N   H    sing N N 330 
SER N   H2   sing N N 331 
SER CA  C    sing N N 332 
SER CA  CB   sing N N 333 
SER CA  HA   sing N N 334 
SER C   O    doub N N 335 
SER C   OXT  sing N N 336 
SER CB  OG   sing N N 337 
SER CB  HB2  sing N N 338 
SER CB  HB3  sing N N 339 
SER OG  HG   sing N N 340 
SER OXT HXT  sing N N 341 
THR N   CA   sing N N 342 
THR N   H    sing N N 343 
THR N   H2   sing N N 344 
THR CA  C    sing N N 345 
THR CA  CB   sing N N 346 
THR CA  HA   sing N N 347 
THR C   O    doub N N 348 
THR C   OXT  sing N N 349 
THR CB  OG1  sing N N 350 
THR CB  CG2  sing N N 351 
THR CB  HB   sing N N 352 
THR OG1 HG1  sing N N 353 
THR CG2 HG21 sing N N 354 
THR CG2 HG22 sing N N 355 
THR CG2 HG23 sing N N 356 
THR OXT HXT  sing N N 357 
TRP N   CA   sing N N 358 
TRP N   H    sing N N 359 
TRP N   H2   sing N N 360 
TRP CA  C    sing N N 361 
TRP CA  CB   sing N N 362 
TRP CA  HA   sing N N 363 
TRP C   O    doub N N 364 
TRP C   OXT  sing N N 365 
TRP CB  CG   sing N N 366 
TRP CB  HB2  sing N N 367 
TRP CB  HB3  sing N N 368 
TRP CG  CD1  doub Y N 369 
TRP CG  CD2  sing Y N 370 
TRP CD1 NE1  sing Y N 371 
TRP CD1 HD1  sing N N 372 
TRP CD2 CE2  doub Y N 373 
TRP CD2 CE3  sing Y N 374 
TRP NE1 CE2  sing Y N 375 
TRP NE1 HE1  sing N N 376 
TRP CE2 CZ2  sing Y N 377 
TRP CE3 CZ3  doub Y N 378 
TRP CE3 HE3  sing N N 379 
TRP CZ2 CH2  doub Y N 380 
TRP CZ2 HZ2  sing N N 381 
TRP CZ3 CH2  sing Y N 382 
TRP CZ3 HZ3  sing N N 383 
TRP CH2 HH2  sing N N 384 
TRP OXT HXT  sing N N 385 
TYR N   CA   sing N N 386 
TYR N   H    sing N N 387 
TYR N   H2   sing N N 388 
TYR CA  C    sing N N 389 
TYR CA  CB   sing N N 390 
TYR CA  HA   sing N N 391 
TYR C   O    doub N N 392 
TYR C   OXT  sing N N 393 
TYR CB  CG   sing N N 394 
TYR CB  HB2  sing N N 395 
TYR CB  HB3  sing N N 396 
TYR CG  CD1  doub Y N 397 
TYR CG  CD2  sing Y N 398 
TYR CD1 CE1  sing Y N 399 
TYR CD1 HD1  sing N N 400 
TYR CD2 CE2  doub Y N 401 
TYR CD2 HD2  sing N N 402 
TYR CE1 CZ   doub Y N 403 
TYR CE1 HE1  sing N N 404 
TYR CE2 CZ   sing Y N 405 
TYR CE2 HE2  sing N N 406 
TYR CZ  OH   sing N N 407 
TYR OH  HH   sing N N 408 
TYR OXT HXT  sing N N 409 
VAL N   CA   sing N N 410 
VAL N   H    sing N N 411 
VAL N   H2   sing N N 412 
VAL CA  C    sing N N 413 
VAL CA  CB   sing N N 414 
VAL CA  HA   sing N N 415 
VAL C   O    doub N N 416 
VAL C   OXT  sing N N 417 
VAL CB  CG1  sing N N 418 
VAL CB  CG2  sing N N 419 
VAL CB  HB   sing N N 420 
VAL CG1 HG11 sing N N 421 
VAL CG1 HG12 sing N N 422 
VAL CG1 HG13 sing N N 423 
VAL CG2 HG21 sing N N 424 
VAL CG2 HG22 sing N N 425 
VAL CG2 HG23 sing N N 426 
VAL OXT HXT  sing N N 427 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-04-09 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9BCN 
_em_admin.last_update        2024-11-27 
_em_admin.map_release_date   2024-11-27 
_em_admin.title              'Extracellular domain of apo GC-A, state 2' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          9606 
_em_entity_assembly_naturalsource.organism             'Homo sapiens' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          7108 
_em_entity_assembly_recombinant.organism             'Spodoptera frugiperda' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         51.13 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'       ? 1  1 ? ? ? ? 
'IMAGE ACQUISITION'        ? 2  ? ? 1 ? ? 
MASKING                    ? 3  ? ? ? ? ? 
'CTF CORRECTION'           ? 4  1 ? ? ? ? 
'LAYERLINE INDEXING'       ? 5  ? ? ? ? ? 
'DIFFRACTION INDEXING'     ? 6  ? ? ? ? ? 
'MODEL FITTING'            ? 7  ? ? ? ? ? 
'MODEL REFINEMENT'         ? 8  ? ? ? ? ? 
OTHER                      ? 9  ? ? ? ? ? 
'INITIAL EULER ASSIGNMENT' ? 10 1 ? ? ? ? 
'FINAL EULER ASSIGNMENT'   ? 11 1 ? ? ? ? 
CLASSIFICATION             ? 12 1 ? ? ? ? 
RECONSTRUCTION             ? 13 1 ? ? ? ? 
# 
_em_specimen.concentration           1 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           GM138676 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
2 NAG 1 n 
2 NAG 2 n 
2 MAN 3 n 
# 
_atom_sites.entry_id                    9BCN 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   1.000000 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   1.000000 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   1.000000 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . GLY A 1 12  ? 102.165 100.384 120.168 1.00 45.11 ? 1    GLY A N   1 
ATOM   2    C  CA  . GLY A 1 12  ? 101.397 99.188  119.720 1.00 45.11 ? 1    GLY A CA  1 
ATOM   3    C  C   . GLY A 1 12  ? 102.131 98.382  118.669 1.00 45.11 ? 1    GLY A C   1 
ATOM   4    O  O   . GLY A 1 12  ? 103.332 98.545  118.478 1.00 45.11 ? 1    GLY A O   1 
ATOM   5    N  N   . ASN A 1 13  ? 101.402 97.504  117.987 1.00 43.12 ? 2    ASN A N   1 
ATOM   6    C  CA  . ASN A 1 13  ? 101.952 96.660  116.936 1.00 43.12 ? 2    ASN A CA  1 
ATOM   7    C  C   . ASN A 1 13  ? 101.209 96.937  115.640 1.00 43.12 ? 2    ASN A C   1 
ATOM   8    O  O   . ASN A 1 13  ? 99.975  96.921  115.615 1.00 43.12 ? 2    ASN A O   1 
ATOM   9    C  CB  . ASN A 1 13  ? 101.840 95.180  117.305 1.00 43.12 ? 2    ASN A CB  1 
ATOM   10   C  CG  . ASN A 1 13  ? 102.356 94.886  118.699 1.00 43.12 ? 2    ASN A CG  1 
ATOM   11   O  OD1 . ASN A 1 13  ? 103.380 95.423  119.119 1.00 43.12 ? 2    ASN A OD1 1 
ATOM   12   N  ND2 . ASN A 1 13  ? 101.648 94.029  119.426 1.00 43.12 ? 2    ASN A ND2 1 
ATOM   13   N  N   . LEU A 1 14  ? 101.958 97.191  114.573 1.00 34.15 ? 3    LEU A N   1 
ATOM   14   C  CA  . LEU A 1 14  ? 101.404 97.485  113.256 1.00 34.15 ? 3    LEU A CA  1 
ATOM   15   C  C   . LEU A 1 14  ? 101.690 96.294  112.352 1.00 34.15 ? 3    LEU A C   1 
ATOM   16   O  O   . LEU A 1 14  ? 102.850 96.013  112.039 1.00 34.15 ? 3    LEU A O   1 
ATOM   17   C  CB  . LEU A 1 14  ? 102.010 98.768  112.693 1.00 34.15 ? 3    LEU A CB  1 
ATOM   18   C  CG  . LEU A 1 14  ? 101.288 99.466  111.542 1.00 34.15 ? 3    LEU A CG  1 
ATOM   19   C  CD1 . LEU A 1 14  ? 101.672 100.927 111.513 1.00 34.15 ? 3    LEU A CD1 1 
ATOM   20   C  CD2 . LEU A 1 14  ? 101.614 98.816  110.217 1.00 34.15 ? 3    LEU A CD2 1 
ATOM   21   N  N   . THR A 1 15  ? 100.635 95.601  111.932 1.00 28.42 ? 4    THR A N   1 
ATOM   22   C  CA  . THR A 1 15  ? 100.766 94.418  111.092 1.00 28.42 ? 4    THR A CA  1 
ATOM   23   C  C   . THR A 1 15  ? 100.635 94.804  109.626 1.00 28.42 ? 4    THR A C   1 
ATOM   24   O  O   . THR A 1 15  ? 99.736  95.563  109.257 1.00 28.42 ? 4    THR A O   1 
ATOM   25   C  CB  . THR A 1 15  ? 99.706  93.377  111.454 1.00 28.42 ? 4    THR A CB  1 
ATOM   26   O  OG1 . THR A 1 15  ? 99.924  92.912  112.790 1.00 28.42 ? 4    THR A OG1 1 
ATOM   27   C  CG2 . THR A 1 15  ? 99.759  92.198  110.501 1.00 28.42 ? 4    THR A CG2 1 
ATOM   28   N  N   . VAL A 1 16  ? 101.533 94.281  108.797 1.00 25.19 ? 5    VAL A N   1 
ATOM   29   C  CA  . VAL A 1 16  ? 101.510 94.488  107.355 1.00 25.19 ? 5    VAL A CA  1 
ATOM   30   C  C   . VAL A 1 16  ? 101.262 93.139  106.701 1.00 25.19 ? 5    VAL A C   1 
ATOM   31   O  O   . VAL A 1 16  ? 101.985 92.176  106.970 1.00 25.19 ? 5    VAL A O   1 
ATOM   32   C  CB  . VAL A 1 16  ? 102.824 95.108  106.847 1.00 25.19 ? 5    VAL A CB  1 
ATOM   33   C  CG1 . VAL A 1 16  ? 102.840 95.148  105.336 1.00 25.19 ? 5    VAL A CG1 1 
ATOM   34   C  CG2 . VAL A 1 16  ? 103.017 96.496  107.418 1.00 25.19 ? 5    VAL A CG2 1 
ATOM   35   N  N   . ALA A 1 17  ? 100.244 93.067  105.852 1.00 21.57 ? 6    ALA A N   1 
ATOM   36   C  CA  . ALA A 1 17  ? 99.858  91.822  105.202 1.00 21.57 ? 6    ALA A CA  1 
ATOM   37   C  C   . ALA A 1 17  ? 100.400 91.797  103.783 1.00 21.57 ? 6    ALA A C   1 
ATOM   38   O  O   . ALA A 1 17  ? 100.185 92.738  103.016 1.00 21.57 ? 6    ALA A O   1 
ATOM   39   C  CB  . ALA A 1 17  ? 98.341  91.659  105.189 1.00 21.57 ? 6    ALA A CB  1 
ATOM   40   N  N   . VAL A 1 18  ? 101.092 90.718  103.436 1.00 21.06 ? 7    VAL A N   1 
ATOM   41   C  CA  . VAL A 1 18  ? 101.752 90.573  102.144 1.00 21.06 ? 7    VAL A CA  1 
ATOM   42   C  C   . VAL A 1 18  ? 101.069 89.450  101.384 1.00 21.06 ? 7    VAL A C   1 
ATOM   43   O  O   . VAL A 1 18  ? 100.910 88.345  101.912 1.00 21.06 ? 7    VAL A O   1 
ATOM   44   C  CB  . VAL A 1 18  ? 103.252 90.282  102.311 1.00 21.06 ? 7    VAL A CB  1 
ATOM   45   C  CG1 . VAL A 1 18  ? 103.882 89.971  100.974 1.00 21.06 ? 7    VAL A CG1 1 
ATOM   46   C  CG2 . VAL A 1 18  ? 103.948 91.450  102.969 1.00 21.06 ? 7    VAL A CG2 1 
ATOM   47   N  N   . VAL A 1 19  ? 100.667 89.728  100.148 1.00 19.88 ? 8    VAL A N   1 
ATOM   48   C  CA  . VAL A 1 19  ? 100.084 88.721  99.261  1.00 19.88 ? 8    VAL A CA  1 
ATOM   49   C  C   . VAL A 1 19  ? 100.892 88.773  97.968  1.00 19.88 ? 8    VAL A C   1 
ATOM   50   O  O   . VAL A 1 19  ? 100.578 89.532  97.050  1.00 19.88 ? 8    VAL A O   1 
ATOM   51   C  CB  . VAL A 1 19  ? 98.593  88.950  99.001  1.00 19.88 ? 8    VAL A CB  1 
ATOM   52   C  CG1 . VAL A 1 19  ? 98.055  87.909  98.056  1.00 19.88 ? 8    VAL A CG1 1 
ATOM   53   C  CG2 . VAL A 1 19  ? 97.823  88.917  100.300 1.00 19.88 ? 8    VAL A CG2 1 
ATOM   54   N  N   . LEU A 1 20  ? 101.936 87.955  97.888  1.00 21.69 ? 9    LEU A N   1 
ATOM   55   C  CA  . LEU A 1 20  ? 102.847 87.948  96.753  1.00 21.69 ? 9    LEU A CA  1 
ATOM   56   C  C   . LEU A 1 20  ? 103.239 86.509  96.449  1.00 21.69 ? 9    LEU A C   1 
ATOM   57   O  O   . LEU A 1 20  ? 102.870 85.602  97.201  1.00 21.69 ? 9    LEU A O   1 
ATOM   58   C  CB  . LEU A 1 20  ? 104.086 88.792  97.053  1.00 21.69 ? 9    LEU A CB  1 
ATOM   59   C  CG  . LEU A 1 20  ? 103.918 90.311  97.117  1.00 21.69 ? 9    LEU A CG  1 
ATOM   60   C  CD1 . LEU A 1 20  ? 105.150 90.945  97.710  1.00 21.69 ? 9    LEU A CD1 1 
ATOM   61   C  CD2 . LEU A 1 20  ? 103.643 90.891  95.752  1.00 21.69 ? 9    LEU A CD2 1 
ATOM   62   N  N   . PRO A 1 21  ? 103.954 86.246  95.356  1.00 23.56 ? 10   PRO A N   1 
ATOM   63   C  CA  . PRO A 1 21  ? 104.491 84.897  95.141  1.00 23.56 ? 10   PRO A CA  1 
ATOM   64   C  C   . PRO A 1 21  ? 105.619 84.559  96.102  1.00 23.56 ? 10   PRO A C   1 
ATOM   65   O  O   . PRO A 1 21  ? 106.718 85.109  95.995  1.00 23.56 ? 10   PRO A O   1 
ATOM   66   C  CB  . PRO A 1 21  ? 104.986 84.952  93.692  1.00 23.56 ? 10   PRO A CB  1 
ATOM   67   C  CG  . PRO A 1 21  ? 104.183 86.019  93.069  1.00 23.56 ? 10   PRO A CG  1 
ATOM   68   C  CD  . PRO A 1 21  ? 104.032 87.053  94.131  1.00 23.56 ? 10   PRO A CD  1 
ATOM   69   N  N   . LEU A 1 22  ? 105.365 83.654  97.046  1.00 24.05 ? 11   LEU A N   1 
ATOM   70   C  CA  . LEU A 1 22  ? 106.361 83.323  98.056  1.00 24.05 ? 11   LEU A CA  1 
ATOM   71   C  C   . LEU A 1 22  ? 107.363 82.271  97.607  1.00 24.05 ? 11   LEU A C   1 
ATOM   72   O  O   . LEU A 1 22  ? 108.397 82.115  98.264  1.00 24.05 ? 11   LEU A O   1 
ATOM   73   C  CB  . LEU A 1 22  ? 105.678 82.838  99.332  1.00 24.05 ? 11   LEU A CB  1 
ATOM   74   C  CG  . LEU A 1 22  ? 105.494 83.865  100.440 1.00 24.05 ? 11   LEU A CG  1 
ATOM   75   C  CD1 . LEU A 1 22  ? 104.466 84.868  100.056 1.00 24.05 ? 11   LEU A CD1 1 
ATOM   76   C  CD2 . LEU A 1 22  ? 105.077 83.136  101.692 1.00 24.05 ? 11   LEU A CD2 1 
ATOM   77   N  N   . ALA A 1 23  ? 107.098 81.552  96.519  1.00 27.75 ? 12   ALA A N   1 
ATOM   78   C  CA  . ALA A 1 23  ? 107.959 80.449  96.126  1.00 27.75 ? 12   ALA A CA  1 
ATOM   79   C  C   . ALA A 1 23  ? 108.330 80.421  94.652  1.00 27.75 ? 12   ALA A C   1 
ATOM   80   O  O   . ALA A 1 23  ? 109.170 79.599  94.275  1.00 27.75 ? 12   ALA A O   1 
ATOM   81   C  CB  . ALA A 1 23  ? 107.301 79.109  96.483  1.00 27.75 ? 12   ALA A CB  1 
ATOM   82   N  N   . ASN A 1 24  ? 107.760 81.280  93.811  1.00 28.28 ? 13   ASN A N   1 
ATOM   83   C  CA  . ASN A 1 24  ? 107.988 81.152  92.378  1.00 28.28 ? 13   ASN A CA  1 
ATOM   84   C  C   . ASN A 1 24  ? 109.190 81.946  91.879  1.00 28.28 ? 13   ASN A C   1 
ATOM   85   O  O   . ASN A 1 24  ? 109.731 81.611  90.819  1.00 28.28 ? 13   ASN A O   1 
ATOM   86   C  CB  . ASN A 1 24  ? 106.737 81.568  91.607  1.00 28.28 ? 13   ASN A CB  1 
ATOM   87   C  CG  . ASN A 1 24  ? 106.926 81.477  90.116  1.00 28.28 ? 13   ASN A CG  1 
ATOM   88   O  OD1 . ASN A 1 24  ? 107.480 82.373  89.495  1.00 28.28 ? 13   ASN A OD1 1 
ATOM   89   N  ND2 . ASN A 1 24  ? 106.483 80.373  89.535  1.00 28.28 ? 13   ASN A ND2 1 
ATOM   90   N  N   . THR A 1 25  ? 109.622 82.977  92.603  1.00 27.54 ? 14   THR A N   1 
ATOM   91   C  CA  . THR A 1 25  ? 110.891 83.660  92.346  1.00 27.54 ? 14   THR A CA  1 
ATOM   92   C  C   . THR A 1 25  ? 111.181 83.889  90.866  1.00 27.54 ? 14   THR A C   1 
ATOM   93   O  O   . THR A 1 25  ? 112.328 83.770  90.430  1.00 27.54 ? 14   THR A O   1 
ATOM   94   C  CB  . THR A 1 25  ? 112.044 82.881  92.998  1.00 27.54 ? 14   THR A CB  1 
ATOM   95   O  OG1 . THR A 1 25  ? 113.204 83.714  93.078  1.00 27.54 ? 14   THR A OG1 1 
ATOM   96   C  CG2 . THR A 1 25  ? 112.384 81.598  92.243  1.00 27.54 ? 14   THR A CG2 1 
ATOM   97   N  N   . SER A 1 26  ? 110.161 84.263  90.093  1.00 26.75 ? 15   SER A N   1 
ATOM   98   C  CA  . SER A 1 26  ? 110.356 84.555  88.679  1.00 26.75 ? 15   SER A CA  1 
ATOM   99   C  C   . SER A 1 26  ? 109.577 85.779  88.219  1.00 26.75 ? 15   SER A C   1 
ATOM   100  O  O   . SER A 1 26  ? 109.492 86.017  87.009  1.00 26.75 ? 15   SER A O   1 
ATOM   101  C  CB  . SER A 1 26  ? 109.960 83.361  87.814  1.00 26.75 ? 15   SER A CB  1 
ATOM   102  O  OG  . SER A 1 26  ? 109.748 83.766  86.477  1.00 26.75 ? 15   SER A OG  1 
ATOM   103  N  N   . TYR A 1 27  ? 109.008 86.551  89.131  1.00 25.18 ? 16   TYR A N   1 
ATOM   104  C  CA  . TYR A 1 27  ? 108.249 87.748  88.829  1.00 25.18 ? 16   TYR A CA  1 
ATOM   105  C  C   . TYR A 1 27  ? 109.018 88.975  89.292  1.00 25.18 ? 16   TYR A C   1 
ATOM   106  O  O   . TYR A 1 27  ? 109.860 88.884  90.191  1.00 25.18 ? 16   TYR A O   1 
ATOM   107  C  CB  . TYR A 1 27  ? 106.891 87.713  89.536  1.00 25.18 ? 16   TYR A CB  1 
ATOM   108  C  CG  . TYR A 1 27  ? 105.934 86.674  89.019  1.00 25.18 ? 16   TYR A CG  1 
ATOM   109  C  CD1 . TYR A 1 27  ? 105.189 86.898  87.878  1.00 25.18 ? 16   TYR A CD1 1 
ATOM   110  C  CD2 . TYR A 1 27  ? 105.762 85.477  89.685  1.00 25.18 ? 16   TYR A CD2 1 
ATOM   111  C  CE1 . TYR A 1 27  ? 104.309 85.956  87.412  1.00 25.18 ? 16   TYR A CE1 1 
ATOM   112  C  CE2 . TYR A 1 27  ? 104.885 84.529  89.224  1.00 25.18 ? 16   TYR A CE2 1 
ATOM   113  C  CZ  . TYR A 1 27  ? 104.160 84.774  88.088  1.00 25.18 ? 16   TYR A CZ  1 
ATOM   114  O  OH  . TYR A 1 27  ? 103.282 83.833  87.620  1.00 25.18 ? 16   TYR A OH  1 
ATOM   115  N  N   . PRO A 1 28  ? 108.764 90.145  88.705  1.00 23.76 ? 17   PRO A N   1 
ATOM   116  C  CA  . PRO A 1 28  ? 109.414 91.356  89.224  1.00 23.76 ? 17   PRO A CA  1 
ATOM   117  C  C   . PRO A 1 28  ? 109.072 91.625  90.674  1.00 23.76 ? 17   PRO A C   1 
ATOM   118  O  O   . PRO A 1 28  ? 109.871 92.230  91.397  1.00 23.76 ? 17   PRO A O   1 
ATOM   119  C  CB  . PRO A 1 28  ? 108.886 92.460  88.301  1.00 23.76 ? 17   PRO A CB  1 
ATOM   120  C  CG  . PRO A 1 28  ? 108.442 91.762  87.079  1.00 23.76 ? 17   PRO A CG  1 
ATOM   121  C  CD  . PRO A 1 28  ? 107.943 90.431  87.520  1.00 23.76 ? 17   PRO A CD  1 
ATOM   122  N  N   . TRP A 1 29  ? 107.904 91.169  91.122  1.00 22.96 ? 18   TRP A N   1 
ATOM   123  C  CA  . TRP A 1 29  ? 107.399 91.411  92.466  1.00 22.96 ? 18   TRP A CA  1 
ATOM   124  C  C   . TRP A 1 29  ? 107.405 90.149  93.315  1.00 22.96 ? 18   TRP A C   1 
ATOM   125  O  O   . TRP A 1 29  ? 106.726 90.095  94.342  1.00 22.96 ? 18   TRP A O   1 
ATOM   126  C  CB  . TRP A 1 29  ? 105.986 91.985  92.392  1.00 22.96 ? 18   TRP A CB  1 
ATOM   127  C  CG  . TRP A 1 29  ? 105.142 91.268  91.405  1.00 22.96 ? 18   TRP A CG  1 
ATOM   128  C  CD1 . TRP A 1 29  ? 104.538 90.063  91.569  1.00 22.96 ? 18   TRP A CD1 1 
ATOM   129  C  CD2 . TRP A 1 29  ? 104.839 91.694  90.077  1.00 22.96 ? 18   TRP A CD2 1 
ATOM   130  N  NE1 . TRP A 1 29  ? 103.863 89.715  90.429  1.00 22.96 ? 18   TRP A NE1 1 
ATOM   131  C  CE2 . TRP A 1 29  ? 104.031 90.704  89.498  1.00 22.96 ? 18   TRP A CE2 1 
ATOM   132  C  CE3 . TRP A 1 29  ? 105.165 92.823  89.325  1.00 22.96 ? 18   TRP A CE3 1 
ATOM   133  C  CZ2 . TRP A 1 29  ? 103.548 90.805  88.203  1.00 22.96 ? 18   TRP A CZ2 1 
ATOM   134  C  CZ3 . TRP A 1 29  ? 104.683 92.924  88.044  1.00 22.96 ? 18   TRP A CZ3 1 
ATOM   135  C  CH2 . TRP A 1 29  ? 103.883 91.922  87.494  1.00 22.96 ? 18   TRP A CH2 1 
ATOM   136  N  N   . SER A 1 30  ? 108.148 89.129  92.904  1.00 24.68 ? 19   SER A N   1 
ATOM   137  C  CA  . SER A 1 30  ? 108.206 87.901  93.679  1.00 24.68 ? 19   SER A CA  1 
ATOM   138  C  C   . SER A 1 30  ? 108.803 88.177  95.048  1.00 24.68 ? 19   SER A C   1 
ATOM   139  O  O   . SER A 1 30  ? 109.715 88.993  95.193  1.00 24.68 ? 19   SER A O   1 
ATOM   140  C  CB  . SER A 1 30  ? 109.037 86.854  92.947  1.00 24.68 ? 19   SER A CB  1 
ATOM   141  O  OG  . SER A 1 30  ? 109.067 85.645  93.678  1.00 24.68 ? 19   SER A OG  1 
ATOM   142  N  N   . TRP A 1 31  ? 108.288 87.484  96.061  1.00 23.90 ? 20   TRP A N   1 
ATOM   143  C  CA  . TRP A 1 31  ? 108.789 87.685  97.412  1.00 23.90 ? 20   TRP A CA  1 
ATOM   144  C  C   . TRP A 1 31  ? 110.276 87.387  97.520  1.00 23.90 ? 20   TRP A C   1 
ATOM   145  O  O   . TRP A 1 31  ? 110.931 87.900  98.429  1.00 23.90 ? 20   TRP A O   1 
ATOM   146  C  CB  . TRP A 1 31  ? 108.008 86.809  98.390  1.00 23.90 ? 20   TRP A CB  1 
ATOM   147  C  CG  . TRP A 1 31  ? 108.414 86.977  99.816  1.00 23.90 ? 20   TRP A CG  1 
ATOM   148  C  CD1 . TRP A 1 31  ? 109.034 86.056  100.601 1.00 23.90 ? 20   TRP A CD1 1 
ATOM   149  C  CD2 . TRP A 1 31  ? 108.225 88.137  100.632 1.00 23.90 ? 20   TRP A CD2 1 
ATOM   150  N  NE1 . TRP A 1 31  ? 109.248 86.568  101.854 1.00 23.90 ? 20   TRP A NE1 1 
ATOM   151  C  CE2 . TRP A 1 31  ? 108.757 87.845  101.899 1.00 23.90 ? 20   TRP A CE2 1 
ATOM   152  C  CE3 . TRP A 1 31  ? 107.658 89.394  100.415 1.00 23.90 ? 20   TRP A CE3 1 
ATOM   153  C  CZ2 . TRP A 1 31  ? 108.740 88.761  102.941 1.00 23.90 ? 20   TRP A CZ2 1 
ATOM   154  C  CZ3 . TRP A 1 31  ? 107.643 90.300  101.451 1.00 23.90 ? 20   TRP A CZ3 1 
ATOM   155  C  CH2 . TRP A 1 31  ? 108.180 89.980  102.697 1.00 23.90 ? 20   TRP A CH2 1 
ATOM   156  N  N   . ALA A 1 32  ? 110.832 86.591  96.606  1.00 27.28 ? 21   ALA A N   1 
ATOM   157  C  CA  . ALA A 1 32  ? 112.256 86.285  96.666  1.00 27.28 ? 21   ALA A CA  1 
ATOM   158  C  C   . ALA A 1 32  ? 113.100 87.546  96.546  1.00 27.28 ? 21   ALA A C   1 
ATOM   159  O  O   . ALA A 1 32  ? 114.162 87.651  97.167  1.00 27.28 ? 21   ALA A O   1 
ATOM   160  C  CB  . ALA A 1 32  ? 112.623 85.294  95.565  1.00 27.28 ? 21   ALA A CB  1 
ATOM   161  N  N   . ARG A 1 33  ? 112.647 88.513  95.750  1.00 28.41 ? 22   ARG A N   1 
ATOM   162  C  CA  . ARG A 1 33  ? 113.380 89.754  95.548  1.00 28.41 ? 22   ARG A CA  1 
ATOM   163  C  C   . ARG A 1 33  ? 112.707 90.968  96.171  1.00 28.41 ? 22   ARG A C   1 
ATOM   164  O  O   . ARG A 1 33  ? 113.347 92.018  96.274  1.00 28.41 ? 22   ARG A O   1 
ATOM   165  C  CB  . ARG A 1 33  ? 113.590 90.002  94.049  1.00 28.41 ? 22   ARG A CB  1 
ATOM   166  C  CG  . ARG A 1 33  ? 112.316 90.142  93.265  1.00 28.41 ? 22   ARG A CG  1 
ATOM   167  C  CD  . ARG A 1 33  ? 112.586 90.127  91.778  1.00 28.41 ? 22   ARG A CD  1 
ATOM   168  N  NE  . ARG A 1 33  ? 112.747 88.773  91.266  1.00 28.41 ? 22   ARG A NE  1 
ATOM   169  C  CZ  . ARG A 1 33  ? 113.068 88.485  90.011  1.00 28.41 ? 22   ARG A CZ  1 
ATOM   170  N  NH1 . ARG A 1 33  ? 113.262 89.455  89.132  1.00 28.41 ? 22   ARG A NH1 1 
ATOM   171  N  NH2 . ARG A 1 33  ? 113.194 87.223  89.633  1.00 28.41 ? 22   ARG A NH2 1 
ATOM   172  N  N   . VAL A 1 34  ? 111.447 90.859  96.592  1.00 24.63 ? 23   VAL A N   1 
ATOM   173  C  CA  . VAL A 1 34  ? 110.799 91.947  97.315  1.00 24.63 ? 23   VAL A CA  1 
ATOM   174  C  C   . VAL A 1 34  ? 110.966 91.815  98.825  1.00 24.63 ? 23   VAL A C   1 
ATOM   175  O  O   . VAL A 1 34  ? 110.852 92.820  99.539  1.00 24.63 ? 23   VAL A O   1 
ATOM   176  C  CB  . VAL A 1 34  ? 109.303 92.021  96.952  1.00 24.63 ? 23   VAL A CB  1 
ATOM   177  C  CG1 . VAL A 1 34  ? 108.546 92.886  97.934  1.00 24.63 ? 23   VAL A CG1 1 
ATOM   178  C  CG2 . VAL A 1 34  ? 109.130 92.563  95.554  1.00 24.63 ? 23   VAL A CG2 1 
ATOM   179  N  N   . GLY A 1 35  ? 111.246 90.618  99.330  1.00 26.80 ? 24   GLY A N   1 
ATOM   180  C  CA  . GLY A 1 35  ? 111.384 90.400  100.748 1.00 26.80 ? 24   GLY A CA  1 
ATOM   181  C  C   . GLY A 1 35  ? 112.554 91.147  101.344 1.00 26.80 ? 24   GLY A C   1 
ATOM   182  O  O   . GLY A 1 35  ? 112.439 91.785  102.394 1.00 26.80 ? 24   GLY A O   1 
ATOM   183  N  N   . PRO A 1 36  ? 113.716 91.071  100.694 1.00 30.95 ? 25   PRO A N   1 
ATOM   184  C  CA  . PRO A 1 36  ? 114.852 91.877  101.159 1.00 30.95 ? 25   PRO A CA  1 
ATOM   185  C  C   . PRO A 1 36  ? 114.578 93.368  101.135 1.00 30.95 ? 25   PRO A C   1 
ATOM   186  O  O   . PRO A 1 36  ? 115.060 94.090  102.013 1.00 30.95 ? 25   PRO A O   1 
ATOM   187  C  CB  . PRO A 1 36  ? 115.970 91.485  100.188 1.00 30.95 ? 25   PRO A CB  1 
ATOM   188  C  CG  . PRO A 1 36  ? 115.592 90.146  99.700  1.00 30.95 ? 25   PRO A CG  1 
ATOM   189  C  CD  . PRO A 1 36  ? 114.108 90.158  99.610  1.00 30.95 ? 25   PRO A CD  1 
ATOM   190  N  N   . ALA A 1 37  ? 113.810 93.854  100.159 1.00 29.28 ? 26   ALA A N   1 
ATOM   191  C  CA  . ALA A 1 37  ? 113.488 95.276  100.108 1.00 29.28 ? 26   ALA A CA  1 
ATOM   192  C  C   . ALA A 1 37  ? 112.641 95.687  101.305 1.00 29.28 ? 26   ALA A C   1 
ATOM   193  O  O   . ALA A 1 37  ? 112.921 96.694  101.966 1.00 29.28 ? 26   ALA A O   1 
ATOM   194  C  CB  . ALA A 1 37  ? 112.765 95.595  98.801  1.00 29.28 ? 26   ALA A CB  1 
ATOM   195  N  N   . VAL A 1 38  ? 111.596 94.915  101.599 1.00 27.72 ? 27   VAL A N   1 
ATOM   196  C  CA  . VAL A 1 38  ? 110.758 95.204  102.757 1.00 27.72 ? 27   VAL A CA  1 
ATOM   197  C  C   . VAL A 1 38  ? 111.577 95.115  104.035 1.00 27.72 ? 27   VAL A C   1 
ATOM   198  O  O   . VAL A 1 38  ? 111.398 95.911  104.963 1.00 27.72 ? 27   VAL A O   1 
ATOM   199  C  CB  . VAL A 1 38  ? 109.550 94.249  102.787 1.00 27.72 ? 27   VAL A CB  1 
ATOM   200  C  CG1 . VAL A 1 38  ? 108.867 94.288  104.136 1.00 27.72 ? 27   VAL A CG1 1 
ATOM   201  C  CG2 . VAL A 1 38  ? 108.571 94.604  101.687 1.00 27.72 ? 27   VAL A CG2 1 
ATOM   202  N  N   . GLU A 1 39  ? 112.484 94.141  104.110 1.00 33.55 ? 28   GLU A N   1 
ATOM   203  C  CA  . GLU A 1 39  ? 113.307 93.991  105.304 1.00 33.55 ? 28   GLU A CA  1 
ATOM   204  C  C   . GLU A 1 39  ? 114.222 95.194  105.501 1.00 33.55 ? 28   GLU A C   1 
ATOM   205  O  O   . GLU A 1 39  ? 114.373 95.690  106.622 1.00 33.55 ? 28   GLU A O   1 
ATOM   206  C  CB  . GLU A 1 39  ? 114.118 92.701  105.209 1.00 33.55 ? 28   GLU A CB  1 
ATOM   207  C  CG  . GLU A 1 39  ? 115.194 92.556  106.266 1.00 33.55 ? 28   GLU A CG  1 
ATOM   208  C  CD  . GLU A 1 39  ? 115.803 91.170  106.280 1.00 33.55 ? 28   GLU A CD  1 
ATOM   209  O  OE1 . GLU A 1 39  ? 116.241 90.720  107.358 1.00 33.55 ? 28   GLU A OE1 1 
ATOM   210  O  OE2 . GLU A 1 39  ? 115.838 90.528  105.210 1.00 33.55 ? 28   GLU A OE2 1 
ATOM   211  N  N   . LEU A 1 40  ? 114.841 95.678  104.423 1.00 33.86 ? 29   LEU A N   1 
ATOM   212  C  CA  . LEU A 1 40  ? 115.667 96.877  104.523 1.00 33.86 ? 29   LEU A CA  1 
ATOM   213  C  C   . LEU A 1 40  ? 114.834 98.083  104.932 1.00 33.86 ? 29   LEU A C   1 
ATOM   214  O  O   . LEU A 1 40  ? 115.272 98.903  105.747 1.00 33.86 ? 29   LEU A O   1 
ATOM   215  C  CB  . LEU A 1 40  ? 116.368 97.146  103.193 1.00 33.86 ? 29   LEU A CB  1 
ATOM   216  C  CG  . LEU A 1 40  ? 117.515 96.211  102.814 1.00 33.86 ? 29   LEU A CG  1 
ATOM   217  C  CD1 . LEU A 1 40  ? 117.947 96.471  101.389 1.00 33.86 ? 29   LEU A CD1 1 
ATOM   218  C  CD2 . LEU A 1 40  ? 118.687 96.386  103.759 1.00 33.86 ? 29   LEU A CD2 1 
ATOM   219  N  N   . ALA A 1 41  ? 113.632 98.217  104.370 1.00 31.95 ? 30   ALA A N   1 
ATOM   220  C  CA  . ALA A 1 41  ? 112.762 99.322  104.755 1.00 31.95 ? 30   ALA A CA  1 
ATOM   221  C  C   . ALA A 1 41  ? 112.460 99.281  106.246 1.00 31.95 ? 30   ALA A C   1 
ATOM   222  O  O   . ALA A 1 41  ? 112.589 100.289 106.949 1.00 31.95 ? 30   ALA A O   1 
ATOM   223  C  CB  . ALA A 1 41  ? 111.467 99.275  103.944 1.00 31.95 ? 30   ALA A CB  1 
ATOM   224  N  N   . LEU A 1 42  ? 112.065 98.112  106.750 1.00 32.23 ? 31   LEU A N   1 
ATOM   225  C  CA  . LEU A 1 42  ? 111.711 97.995  108.160 1.00 32.23 ? 31   LEU A CA  1 
ATOM   226  C  C   . LEU A 1 42  ? 112.919 98.209  109.061 1.00 32.23 ? 31   LEU A C   1 
ATOM   227  O  O   . LEU A 1 42  ? 112.778 98.745  110.164 1.00 32.23 ? 31   LEU A O   1 
ATOM   228  C  CB  . LEU A 1 42  ? 111.081 96.631  108.429 1.00 32.23 ? 31   LEU A CB  1 
ATOM   229  C  CG  . LEU A 1 42  ? 109.736 96.359  107.754 1.00 32.23 ? 31   LEU A CG  1 
ATOM   230  C  CD1 . LEU A 1 42  ? 109.181 95.030  108.214 1.00 32.23 ? 31   LEU A CD1 1 
ATOM   231  C  CD2 . LEU A 1 42  ? 108.749 97.468  108.038 1.00 32.23 ? 31   LEU A CD2 1 
ATOM   232  N  N   . ALA A 1 43  ? 114.107 97.791  108.621 1.00 37.15 ? 32   ALA A N   1 
ATOM   233  C  CA  . ALA A 1 43  ? 115.316 98.103  109.374 1.00 37.15 ? 32   ALA A CA  1 
ATOM   234  C  C   . ALA A 1 43  ? 115.554 99.605  109.418 1.00 37.15 ? 32   ALA A C   1 
ATOM   235  O  O   . ALA A 1 43  ? 115.982 100.145 110.444 1.00 37.15 ? 32   ALA A O   1 
ATOM   236  C  CB  . ALA A 1 43  ? 116.517 97.388  108.760 1.00 37.15 ? 32   ALA A CB  1 
ATOM   237  N  N   . GLN A 1 44  ? 115.288 100.298 108.310 1.00 41.12 ? 33   GLN A N   1 
ATOM   238  C  CA  . GLN A 1 44  ? 115.436 101.749 108.296 1.00 41.12 ? 33   GLN A CA  1 
ATOM   239  C  C   . GLN A 1 44  ? 114.431 102.420 109.224 1.00 41.12 ? 33   GLN A C   1 
ATOM   240  O  O   . GLN A 1 44  ? 114.747 103.429 109.862 1.00 41.12 ? 33   GLN A O   1 
ATOM   241  C  CB  . GLN A 1 44  ? 115.282 102.277 106.872 1.00 41.12 ? 33   GLN A CB  1 
ATOM   242  C  CG  . GLN A 1 44  ? 115.366 103.786 106.776 1.00 41.12 ? 33   GLN A CG  1 
ATOM   243  C  CD  . GLN A 1 44  ? 115.497 104.270 105.353 1.00 41.12 ? 33   GLN A CD  1 
ATOM   244  O  OE1 . GLN A 1 44  ? 115.623 103.474 104.425 1.00 41.12 ? 33   GLN A OE1 1 
ATOM   245  N  NE2 . GLN A 1 44  ? 115.466 105.584 105.171 1.00 41.12 ? 33   GLN A NE2 1 
ATOM   246  N  N   . VAL A 1 45  ? 113.211 101.886 109.302 1.00 38.05 ? 34   VAL A N   1 
ATOM   247  C  CA  . VAL A 1 45  ? 112.205 102.467 110.189 1.00 38.05 ? 34   VAL A CA  1 
ATOM   248  C  C   . VAL A 1 45  ? 112.680 102.411 111.633 1.00 38.05 ? 34   VAL A C   1 
ATOM   249  O  O   . VAL A 1 45  ? 112.555 103.386 112.383 1.00 38.05 ? 34   VAL A O   1 
ATOM   250  C  CB  . VAL A 1 45  ? 110.855 101.748 110.012 1.00 38.05 ? 34   VAL A CB  1 
ATOM   251  C  CG1 . VAL A 1 45  ? 109.880 102.170 111.095 1.00 38.05 ? 34   VAL A CG1 1 
ATOM   252  C  CG2 . VAL A 1 45  ? 110.277 102.028 108.642 1.00 38.05 ? 34   VAL A CG2 1 
ATOM   253  N  N   . LYS A 1 46  ? 113.230 101.268 112.049 1.00 42.61 ? 35   LYS A N   1 
ATOM   254  C  CA  . LYS A 1 46  ? 113.695 101.130 113.425 1.00 42.61 ? 35   LYS A CA  1 
ATOM   255  C  C   . LYS A 1 46  ? 114.844 102.086 113.716 1.00 42.61 ? 35   LYS A C   1 
ATOM   256  O  O   . LYS A 1 46  ? 114.915 102.670 114.804 1.00 42.61 ? 35   LYS A O   1 
ATOM   257  C  CB  . LYS A 1 46  ? 114.119 99.687  113.692 1.00 42.61 ? 35   LYS A CB  1 
ATOM   258  N  N   . ALA A 1 47  ? 115.756 102.258 112.758 1.00 45.68 ? 36   ALA A N   1 
ATOM   259  C  CA  . ALA A 1 47  ? 116.904 103.129 112.982 1.00 45.68 ? 36   ALA A CA  1 
ATOM   260  C  C   . ALA A 1 47  ? 116.470 104.569 113.224 1.00 45.68 ? 36   ALA A C   1 
ATOM   261  O  O   . ALA A 1 47  ? 116.995 105.238 114.120 1.00 45.68 ? 36   ALA A O   1 
ATOM   262  C  CB  . ALA A 1 47  ? 117.858 103.055 111.791 1.00 45.68 ? 36   ALA A CB  1 
ATOM   263  N  N   . ARG A 1 48  ? 115.518 105.061 112.441 1.00 47.31 ? 37   ARG A N   1 
ATOM   264  C  CA  . ARG A 1 48  ? 115.080 106.446 112.561 1.00 47.31 ? 37   ARG A CA  1 
ATOM   265  C  C   . ARG A 1 48  ? 114.095 106.589 113.715 1.00 47.31 ? 37   ARG A C   1 
ATOM   266  O  O   . ARG A 1 48  ? 113.047 105.934 113.701 1.00 47.31 ? 37   ARG A O   1 
ATOM   267  C  CB  . ARG A 1 48  ? 114.423 106.912 111.270 1.00 47.31 ? 37   ARG A CB  1 
ATOM   268  C  CG  . ARG A 1 48  ? 115.393 107.148 110.129 1.00 47.31 ? 37   ARG A CG  1 
ATOM   269  C  CD  . ARG A 1 48  ? 114.670 107.530 108.849 1.00 47.31 ? 37   ARG A CD  1 
ATOM   270  N  NE  . ARG A 1 48  ? 113.735 108.635 109.045 1.00 47.31 ? 37   ARG A NE  1 
ATOM   271  C  CZ  . ARG A 1 48  ? 113.160 109.310 108.055 1.00 47.31 ? 37   ARG A CZ  1 
ATOM   272  N  NH1 . ARG A 1 48  ? 113.418 109.000 106.792 1.00 47.31 ? 37   ARG A NH1 1 
ATOM   273  N  NH2 . ARG A 1 48  ? 112.323 110.300 108.329 1.00 47.31 ? 37   ARG A NH2 1 
ATOM   274  N  N   . PRO A 1 49  ? 114.380 107.419 114.724 1.00 52.24 ? 38   PRO A N   1 
ATOM   275  C  CA  . PRO A 1 49  ? 113.359 107.704 115.744 1.00 52.24 ? 38   PRO A CA  1 
ATOM   276  C  C   . PRO A 1 49  ? 112.242 108.607 115.250 1.00 52.24 ? 38   PRO A C   1 
ATOM   277  O  O   . PRO A 1 49  ? 111.250 108.782 115.969 1.00 52.24 ? 38   PRO A O   1 
ATOM   278  C  CB  . PRO A 1 49  ? 114.161 108.381 116.867 1.00 52.24 ? 38   PRO A CB  1 
ATOM   279  C  CG  . PRO A 1 49  ? 115.594 108.051 116.583 1.00 52.24 ? 38   PRO A CG  1 
ATOM   280  C  CD  . PRO A 1 49  ? 115.681 107.996 115.098 1.00 52.24 ? 38   PRO A CD  1 
ATOM   281  N  N   . ASP A 1 50  ? 112.370 109.186 114.056 1.00 49.90 ? 39   ASP A N   1 
ATOM   282  C  CA  . ASP A 1 50  ? 111.352 110.083 113.527 1.00 49.90 ? 39   ASP A CA  1 
ATOM   283  C  C   . ASP A 1 50  ? 110.202 109.351 112.849 1.00 49.90 ? 39   ASP A C   1 
ATOM   284  O  O   . ASP A 1 50  ? 109.240 110.004 112.434 1.00 49.90 ? 39   ASP A O   1 
ATOM   285  C  CB  . ASP A 1 50  ? 111.984 111.060 112.533 1.00 49.90 ? 39   ASP A CB  1 
ATOM   286  N  N   . LEU A 1 51  ? 110.276 108.028 112.720 1.00 43.09 ? 40   LEU A N   1 
ATOM   287  C  CA  . LEU A 1 51  ? 109.223 107.230 112.106 1.00 43.09 ? 40   LEU A CA  1 
ATOM   288  C  C   . LEU A 1 51  ? 108.619 106.314 113.161 1.00 43.09 ? 40   LEU A C   1 
ATOM   289  O  O   . LEU A 1 51  ? 109.335 105.514 113.772 1.00 43.09 ? 40   LEU A O   1 
ATOM   290  C  CB  . LEU A 1 51  ? 109.770 106.409 110.938 1.00 43.09 ? 40   LEU A CB  1 
ATOM   291  C  CG  . LEU A 1 51  ? 110.095 107.161 109.648 1.00 43.09 ? 40   LEU A CG  1 
ATOM   292  C  CD1 . LEU A 1 51  ? 110.592 106.198 108.588 1.00 43.09 ? 40   LEU A CD1 1 
ATOM   293  C  CD2 . LEU A 1 51  ? 108.886 107.922 109.143 1.00 43.09 ? 40   LEU A CD2 1 
ATOM   294  N  N   . LEU A 1 52  ? 107.303 106.428 113.362 1.00 41.28 ? 41   LEU A N   1 
ATOM   295  C  CA  . LEU A 1 52  ? 106.558 105.592 114.296 1.00 41.28 ? 41   LEU A CA  1 
ATOM   296  C  C   . LEU A 1 52  ? 107.357 105.359 115.571 1.00 41.28 ? 41   LEU A C   1 
ATOM   297  O  O   . LEU A 1 52  ? 107.812 104.236 115.821 1.00 41.28 ? 41   LEU A O   1 
ATOM   298  C  CB  . LEU A 1 52  ? 106.203 104.252 113.651 1.00 41.28 ? 41   LEU A CB  1 
ATOM   299  C  CG  . LEU A 1 52  ? 105.030 104.227 112.674 1.00 41.28 ? 41   LEU A CG  1 
ATOM   300  C  CD1 . LEU A 1 52  ? 104.862 102.832 112.116 1.00 41.28 ? 41   LEU A CD1 1 
ATOM   301  C  CD2 . LEU A 1 52  ? 103.751 104.685 113.345 1.00 41.28 ? 41   LEU A CD2 1 
ATOM   302  N  N   . PRO A 1 53  ? 107.559 106.386 116.394 1.00 47.16 ? 42   PRO A N   1 
ATOM   303  C  CA  . PRO A 1 53  ? 108.387 106.217 117.598 1.00 47.16 ? 42   PRO A CA  1 
ATOM   304  C  C   . PRO A 1 53  ? 107.825 105.149 118.524 1.00 47.16 ? 42   PRO A C   1 
ATOM   305  O  O   . PRO A 1 53  ? 106.725 105.284 119.064 1.00 47.16 ? 42   PRO A O   1 
ATOM   306  C  CB  . PRO A 1 53  ? 108.351 107.607 118.241 1.00 47.16 ? 42   PRO A CB  1 
ATOM   307  C  CG  . PRO A 1 53  ? 108.045 108.533 117.112 1.00 47.16 ? 42   PRO A CG  1 
ATOM   308  C  CD  . PRO A 1 53  ? 107.100 107.775 116.239 1.00 47.16 ? 42   PRO A CD  1 
ATOM   309  N  N   . GLY A 1 54  ? 108.595 104.083 118.708 1.00 47.36 ? 43   GLY A N   1 
ATOM   310  C  CA  . GLY A 1 54  ? 108.256 103.008 119.625 1.00 47.36 ? 43   GLY A CA  1 
ATOM   311  C  C   . GLY A 1 54  ? 107.495 101.847 119.017 1.00 47.36 ? 43   GLY A C   1 
ATOM   312  O  O   . GLY A 1 54  ? 107.709 100.697 119.407 1.00 47.36 ? 43   GLY A O   1 
ATOM   313  N  N   . TRP A 1 55  ? 106.612 102.124 118.062 1.00 44.01 ? 44   TRP A N   1 
ATOM   314  C  CA  . TRP A 1 55  ? 105.784 101.077 117.485 1.00 44.01 ? 44   TRP A CA  1 
ATOM   315  C  C   . TRP A 1 55  ? 106.650 99.979  116.879 1.00 44.01 ? 44   TRP A C   1 
ATOM   316  O  O   . TRP A 1 55  ? 107.803 100.195 116.499 1.00 44.01 ? 44   TRP A O   1 
ATOM   317  C  CB  . TRP A 1 55  ? 104.862 101.649 116.409 1.00 44.01 ? 44   TRP A CB  1 
ATOM   318  C  CG  . TRP A 1 55  ? 103.690 102.396 116.944 1.00 44.01 ? 44   TRP A CG  1 
ATOM   319  C  CD1 . TRP A 1 55  ? 103.719 103.527 117.700 1.00 44.01 ? 44   TRP A CD1 1 
ATOM   320  C  CD2 . TRP A 1 55  ? 102.310 102.070 116.762 1.00 44.01 ? 44   TRP A CD2 1 
ATOM   321  N  NE1 . TRP A 1 55  ? 102.441 103.926 118.003 1.00 44.01 ? 44   TRP A NE1 1 
ATOM   322  C  CE2 . TRP A 1 55  ? 101.557 103.046 117.437 1.00 44.01 ? 44   TRP A CE2 1 
ATOM   323  C  CE3 . TRP A 1 55  ? 101.637 101.046 116.093 1.00 44.01 ? 44   TRP A CE3 1 
ATOM   324  C  CZ2 . TRP A 1 55  ? 100.167 103.028 117.465 1.00 44.01 ? 44   TRP A CZ2 1 
ATOM   325  C  CZ3 . TRP A 1 55  ? 100.258 101.029 116.123 1.00 44.01 ? 44   TRP A CZ3 1 
ATOM   326  C  CH2 . TRP A 1 55  ? 99.538  102.012 116.804 1.00 44.01 ? 44   TRP A CH2 1 
ATOM   327  N  N   . THR A 1 56  ? 106.073 98.786  116.794 1.00 40.77 ? 45   THR A N   1 
ATOM   328  C  CA  . THR A 1 56  ? 106.705 97.635  116.164 1.00 40.77 ? 45   THR A CA  1 
ATOM   329  C  C   . THR A 1 56  ? 105.951 97.294  114.887 1.00 40.77 ? 45   THR A C   1 
ATOM   330  O  O   . THR A 1 56  ? 104.720 97.212  114.893 1.00 40.77 ? 45   THR A O   1 
ATOM   331  C  CB  . THR A 1 56  ? 106.717 96.431  117.107 1.00 40.77 ? 45   THR A CB  1 
ATOM   332  O  OG1 . THR A 1 56  ? 107.574 96.701  118.222 1.00 40.77 ? 45   THR A OG1 1 
ATOM   333  C  CG2 . THR A 1 56  ? 107.205 95.187  116.386 1.00 40.77 ? 45   THR A CG2 1 
ATOM   334  N  N   . VAL A 1 57  ? 106.687 97.102  113.797 1.00 34.83 ? 46   VAL A N   1 
ATOM   335  C  CA  . VAL A 1 57  ? 106.116 96.747  112.505 1.00 34.83 ? 46   VAL A CA  1 
ATOM   336  C  C   . VAL A 1 57  ? 106.508 95.312  112.197 1.00 34.83 ? 46   VAL A C   1 
ATOM   337  O  O   . VAL A 1 57  ? 107.689 94.955  112.276 1.00 34.83 ? 46   VAL A O   1 
ATOM   338  C  CB  . VAL A 1 57  ? 106.593 97.697  111.394 1.00 34.83 ? 46   VAL A CB  1 
ATOM   339  C  CG1 . VAL A 1 57  ? 106.018 97.275  110.054 1.00 34.83 ? 46   VAL A CG1 1 
ATOM   340  C  CG2 . VAL A 1 57  ? 106.202 99.126  111.714 1.00 34.83 ? 46   VAL A CG2 1 
ATOM   341  N  N   . ARG A 1 58  ? 105.521 94.490  111.852 1.00 32.80 ? 47   ARG A N   1 
ATOM   342  C  CA  . ARG A 1 58  ? 105.748 93.088  111.546 1.00 32.80 ? 47   ARG A CA  1 
ATOM   343  C  C   . ARG A 1 58  ? 104.907 92.695  110.344 1.00 32.80 ? 47   ARG A C   1 
ATOM   344  O  O   . ARG A 1 58  ? 103.805 93.208  110.148 1.00 32.80 ? 47   ARG A O   1 
ATOM   345  C  CB  . ARG A 1 58  ? 105.403 92.193  112.737 1.00 32.80 ? 47   ARG A CB  1 
ATOM   346  C  CG  . ARG A 1 58  ? 103.920 92.045  112.974 1.00 32.80 ? 47   ARG A CG  1 
ATOM   347  C  CD  . ARG A 1 58  ? 103.616 91.830  114.443 1.00 32.80 ? 47   ARG A CD  1 
ATOM   348  N  NE  . ARG A 1 58  ? 102.238 91.400  114.661 1.00 32.80 ? 47   ARG A NE  1 
ATOM   349  C  CZ  . ARG A 1 58  ? 101.753 90.216  114.300 1.00 32.80 ? 47   ARG A CZ  1 
ATOM   350  N  NH1 . ARG A 1 58  ? 102.533 89.324  113.701 1.00 32.80 ? 47   ARG A NH1 1 
ATOM   351  N  NH2 . ARG A 1 58  ? 100.484 89.919  114.543 1.00 32.80 ? 47   ARG A NH2 1 
ATOM   352  N  N   . THR A 1 59  ? 105.431 91.771  109.547 1.00 26.90 ? 48   THR A N   1 
ATOM   353  C  CA  . THR A 1 59  ? 104.780 91.319  108.327 1.00 26.90 ? 48   THR A CA  1 
ATOM   354  C  C   . THR A 1 59  ? 104.266 89.898  108.502 1.00 26.90 ? 48   THR A C   1 
ATOM   355  O  O   . THR A 1 59  ? 104.897 89.077  109.173 1.00 26.90 ? 48   THR A O   1 
ATOM   356  C  CB  . THR A 1 59  ? 105.738 91.370  107.136 1.00 26.90 ? 48   THR A CB  1 
ATOM   357  O  OG1 . THR A 1 59  ? 106.928 90.636  107.444 1.00 26.90 ? 48   THR A OG1 1 
ATOM   358  C  CG2 . THR A 1 59  ? 106.105 92.800  106.799 1.00 26.90 ? 48   THR A CG2 1 
ATOM   359  N  N   . VAL A 1 60  ? 103.114 89.619  107.899 1.00 24.40 ? 49   VAL A N   1 
ATOM   360  C  CA  . VAL A 1 60  ? 102.540 88.281  107.850 1.00 24.40 ? 49   VAL A CA  1 
ATOM   361  C  C   . VAL A 1 60  ? 102.300 87.937  106.389 1.00 24.40 ? 49   VAL A C   1 
ATOM   362  O  O   . VAL A 1 60  ? 101.756 88.753  105.639 1.00 24.40 ? 49   VAL A O   1 
ATOM   363  C  CB  . VAL A 1 60  ? 101.240 88.183  108.665 1.00 24.40 ? 49   VAL A CB  1 
ATOM   364  C  CG1 . VAL A 1 60  ? 101.528 88.450  110.127 1.00 24.40 ? 49   VAL A CG1 1 
ATOM   365  C  CG2 . VAL A 1 60  ? 100.207 89.162  108.151 1.00 24.40 ? 49   VAL A CG2 1 
ATOM   366  N  N   . LEU A 1 61  ? 102.708 86.739  105.986 1.00 23.26 ? 50   LEU A N   1 
ATOM   367  C  CA  . LEU A 1 61  ? 102.870 86.393  104.583 1.00 23.26 ? 50   LEU A CA  1 
ATOM   368  C  C   . LEU A 1 61  ? 101.751 85.480  104.106 1.00 23.26 ? 50   LEU A C   1 
ATOM   369  O  O   . LEU A 1 61  ? 101.389 84.515  104.784 1.00 23.26 ? 50   LEU A O   1 
ATOM   370  C  CB  . LEU A 1 61  ? 104.214 85.703  104.355 1.00 23.26 ? 50   LEU A CB  1 
ATOM   371  C  CG  . LEU A 1 61  ? 105.451 86.480  104.791 1.00 23.26 ? 50   LEU A CG  1 
ATOM   372  C  CD1 . LEU A 1 61  ? 106.685 85.644  104.560 1.00 23.26 ? 50   LEU A CD1 1 
ATOM   373  C  CD2 . LEU A 1 61  ? 105.548 87.789  104.051 1.00 23.26 ? 50   LEU A CD2 1 
ATOM   374  N  N   . GLY A 1 62  ? 101.214 85.792  102.937 1.00 20.85 ? 51   GLY A N   1 
ATOM   375  C  CA  . GLY A 1 62  ? 100.271 84.915  102.270 1.00 20.85 ? 51   GLY A CA  1 
ATOM   376  C  C   . GLY A 1 62  ? 100.613 84.839  100.800 1.00 20.85 ? 51   GLY A C   1 
ATOM   377  O  O   . GLY A 1 62  ? 101.175 85.770  100.227 1.00 20.85 ? 51   GLY A O   1 
ATOM   378  N  N   . SER A 1 63  ? 100.266 83.715  100.188 1.00 22.62 ? 52   SER A N   1 
ATOM   379  C  CA  . SER A 1 63  ? 100.718 83.409  98.840  1.00 22.62 ? 52   SER A CA  1 
ATOM   380  C  C   . SER A 1 63  ? 99.629  83.706  97.822  1.00 22.62 ? 52   SER A C   1 
ATOM   381  O  O   . SER A 1 63  ? 98.444  83.478  98.073  1.00 22.62 ? 52   SER A O   1 
ATOM   382  C  CB  . SER A 1 63  ? 101.150 81.949  98.731  1.00 22.62 ? 52   SER A CB  1 
ATOM   383  O  OG  . SER A 1 63  ? 101.611 81.661  97.428  1.00 22.62 ? 52   SER A OG  1 
ATOM   384  N  N   . SER A 1 64  ? 100.050 84.212  96.666  1.00 22.35 ? 53   SER A N   1 
ATOM   385  C  CA  . SER A 1 64  ? 99.155  84.694  95.625  1.00 22.35 ? 53   SER A CA  1 
ATOM   386  C  C   . SER A 1 64  ? 99.061  83.741  94.445  1.00 22.35 ? 53   SER A C   1 
ATOM   387  O  O   . SER A 1 64  ? 98.606  84.141  93.372  1.00 22.35 ? 53   SER A O   1 
ATOM   388  C  CB  . SER A 1 64  ? 99.623  86.061  95.140  1.00 22.35 ? 53   SER A CB  1 
ATOM   389  O  OG  . SER A 1 64  ? 98.797  86.531  94.097  1.00 22.35 ? 53   SER A OG  1 
ATOM   390  N  N   . GLU A 1 65  ? 99.476  82.491  94.617  1.00 25.81 ? 54   GLU A N   1 
ATOM   391  C  CA  . GLU A 1 65  ? 99.614  81.566  93.505  1.00 25.81 ? 54   GLU A CA  1 
ATOM   392  C  C   . GLU A 1 65  ? 98.979  80.227  93.838  1.00 25.81 ? 54   GLU A C   1 
ATOM   393  O  O   . GLU A 1 65  ? 98.857  79.846  95.004  1.00 25.81 ? 54   GLU A O   1 
ATOM   394  C  CB  . GLU A 1 65  ? 101.082 81.375  93.141  1.00 25.81 ? 54   GLU A CB  1 
ATOM   395  C  CG  . GLU A 1 65  ? 101.939 80.910  94.288  1.00 25.81 ? 54   GLU A CG  1 
ATOM   396  C  CD  . GLU A 1 65  ? 103.406 81.167  94.050  1.00 25.81 ? 54   GLU A CD  1 
ATOM   397  O  OE1 . GLU A 1 65  ? 103.731 81.910  93.103  1.00 25.81 ? 54   GLU A OE1 1 
ATOM   398  O  OE2 . GLU A 1 65  ? 104.237 80.620  94.803  1.00 25.81 ? 54   GLU A OE2 1 
ATOM   399  N  N   . ASN A 1 66  ? 98.574  79.520  92.788  1.00 27.52 ? 55   ASN A N   1 
ATOM   400  C  CA  . ASN A 1 66  ? 97.882  78.249  92.909  1.00 27.52 ? 55   ASN A CA  1 
ATOM   401  C  C   . ASN A 1 66  ? 98.901  77.111  92.957  1.00 27.52 ? 55   ASN A C   1 
ATOM   402  O  O   . ASN A 1 66  ? 100.105 77.328  93.104  1.00 27.52 ? 55   ASN A O   1 
ATOM   403  C  CB  . ASN A 1 66  ? 96.887  78.091  91.762  1.00 27.52 ? 55   ASN A CB  1 
ATOM   404  C  CG  . ASN A 1 66  ? 97.544  78.166  90.406  1.00 27.52 ? 55   ASN A CG  1 
ATOM   405  O  OD1 . ASN A 1 66  ? 98.742  77.946  90.275  1.00 27.52 ? 55   ASN A OD1 1 
ATOM   406  N  ND2 . ASN A 1 66  ? 96.761  78.483  89.385  1.00 27.52 ? 55   ASN A ND2 1 
ATOM   407  N  N   . ALA A 1 67  ? 98.418  75.873  92.840  1.00 30.07 ? 56   ALA A N   1 
ATOM   408  C  CA  . ALA A 1 67  ? 99.291  74.714  92.967  1.00 30.07 ? 56   ALA A CA  1 
ATOM   409  C  C   . ALA A 1 67  ? 100.258 74.576  91.801  1.00 30.07 ? 56   ALA A C   1 
ATOM   410  O  O   . ALA A 1 67  ? 101.251 73.853  91.923  1.00 30.07 ? 56   ALA A O   1 
ATOM   411  C  CB  . ALA A 1 67  ? 98.454  73.444  93.094  1.00 30.07 ? 56   ALA A CB  1 
ATOM   412  N  N   . LEU A 1 68  ? 99.993  75.238  90.676  1.00 31.21 ? 57   LEU A N   1 
ATOM   413  C  CA  . LEU A 1 68  ? 100.900 75.181  89.537  1.00 31.21 ? 57   LEU A CA  1 
ATOM   414  C  C   . LEU A 1 68  ? 102.077 76.135  89.667  1.00 31.21 ? 57   LEU A C   1 
ATOM   415  O  O   . LEU A 1 68  ? 103.014 76.043  88.869  1.00 31.21 ? 57   LEU A O   1 
ATOM   416  C  CB  . LEU A 1 68  ? 100.147 75.490  88.243  1.00 31.21 ? 57   LEU A CB  1 
ATOM   417  C  CG  . LEU A 1 68  ? 99.285  74.363  87.682  1.00 31.21 ? 57   LEU A CG  1 
ATOM   418  C  CD1 . LEU A 1 68  ? 98.082  74.104  88.569  1.00 31.21 ? 57   LEU A CD1 1 
ATOM   419  C  CD2 . LEU A 1 68  ? 98.848  74.696  86.270  1.00 31.21 ? 57   LEU A CD2 1 
ATOM   420  N  N   . GLY A 1 69  ? 102.054 77.043  90.638  1.00 29.06 ? 58   GLY A N   1 
ATOM   421  C  CA  . GLY A 1 69  ? 103.139 77.970  90.860  1.00 29.06 ? 58   GLY A CA  1 
ATOM   422  C  C   . GLY A 1 69  ? 102.933 79.347  90.269  1.00 29.06 ? 58   GLY A C   1 
ATOM   423  O  O   . GLY A 1 69  ? 103.721 80.249  90.569  1.00 29.06 ? 58   GLY A O   1 
ATOM   424  N  N   . VAL A 1 70  ? 101.917 79.535  89.444  1.00 28.37 ? 59   VAL A N   1 
ATOM   425  C  CA  . VAL A 1 70  ? 101.641 80.827  88.829  1.00 28.37 ? 59   VAL A CA  1 
ATOM   426  C  C   . VAL A 1 70  ? 100.660 81.594  89.701  1.00 28.37 ? 59   VAL A C   1 
ATOM   427  O  O   . VAL A 1 70  ? 99.854  81.009  90.427  1.00 28.37 ? 59   VAL A O   1 
ATOM   428  C  CB  . VAL A 1 70  ? 101.097 80.648  87.399  1.00 28.37 ? 59   VAL A CB  1 
ATOM   429  C  CG1 . VAL A 1 70  ? 102.041 79.805  86.584  1.00 28.37 ? 59   VAL A CG1 1 
ATOM   430  C  CG2 . VAL A 1 70  ? 99.717  80.031  87.425  1.00 28.37 ? 59   VAL A CG2 1 
ATOM   431  N  N   . CYS A 1 71  ? 100.719 82.921  89.624  1.00 27.35 ? 60   CYS A N   1 
ATOM   432  C  CA  . CYS A 1 71  ? 99.801  83.764  90.376  1.00 27.35 ? 60   CYS A CA  1 
ATOM   433  C  C   . CYS A 1 71  ? 98.438  83.769  89.698  1.00 27.35 ? 60   CYS A C   1 
ATOM   434  O  O   . CYS A 1 71  ? 98.338  84.003  88.490  1.00 27.35 ? 60   CYS A O   1 
ATOM   435  C  CB  . CYS A 1 71  ? 100.348 85.186  90.490  1.00 27.35 ? 60   CYS A CB  1 
ATOM   436  S  SG  . CYS A 1 71  ? 100.425 86.110  88.944  1.00 27.35 ? 60   CYS A SG  1 
ATOM   437  N  N   . SER A 1 72  ? 97.389  83.509  90.474  1.00 23.95 ? 61   SER A N   1 
ATOM   438  C  CA  . SER A 1 72  ? 96.047  83.351  89.940  1.00 23.95 ? 61   SER A CA  1 
ATOM   439  C  C   . SER A 1 72  ? 95.062  84.197  90.729  1.00 23.95 ? 61   SER A C   1 
ATOM   440  O  O   . SER A 1 72  ? 95.268  84.482  91.910  1.00 23.95 ? 61   SER A O   1 
ATOM   441  C  CB  . SER A 1 72  ? 95.599  81.892  89.983  1.00 23.95 ? 61   SER A CB  1 
ATOM   442  O  OG  . SER A 1 72  ? 95.269  81.511  91.304  1.00 23.95 ? 61   SER A OG  1 
ATOM   443  N  N   . ASP A 1 73  ? 93.976  84.582  90.061  1.00 21.81 ? 62   ASP A N   1 
ATOM   444  C  CA  . ASP A 1 73  ? 92.922  85.369  90.686  1.00 21.81 ? 62   ASP A CA  1 
ATOM   445  C  C   . ASP A 1 73  ? 92.040  84.549  91.611  1.00 21.81 ? 62   ASP A C   1 
ATOM   446  O  O   . ASP A 1 73  ? 91.191  85.124  92.297  1.00 21.81 ? 62   ASP A O   1 
ATOM   447  C  CB  . ASP A 1 73  ? 92.052  86.022  89.614  1.00 21.81 ? 62   ASP A CB  1 
ATOM   448  C  CG  . ASP A 1 73  ? 91.465  85.022  88.656  1.00 21.81 ? 62   ASP A CG  1 
ATOM   449  O  OD1 . ASP A 1 73  ? 91.813  83.831  88.762  1.00 21.81 ? 62   ASP A OD1 1 
ATOM   450  O  OD2 . ASP A 1 73  ? 90.661  85.426  87.792  1.00 21.81 ? 62   ASP A OD2 1 
ATOM   451  N  N   . THR A 1 74  ? 92.211  83.230  91.639  1.00 21.23 ? 63   THR A N   1 
ATOM   452  C  CA  . THR A 1 74  ? 91.420  82.367  92.504  1.00 21.23 ? 63   THR A CA  1 
ATOM   453  C  C   . THR A 1 74  ? 92.066  82.143  93.861  1.00 21.23 ? 63   THR A C   1 
ATOM   454  O  O   . THR A 1 74  ? 91.353  81.912  94.843  1.00 21.23 ? 63   THR A O   1 
ATOM   455  C  CB  . THR A 1 74  ? 91.203  81.014  91.827  1.00 21.23 ? 63   THR A CB  1 
ATOM   456  O  OG1 . THR A 1 74  ? 90.509  81.199  90.588  1.00 21.23 ? 63   THR A OG1 1 
ATOM   457  C  CG2 . THR A 1 74  ? 90.406  80.092  92.718  1.00 21.23 ? 63   THR A CG2 1 
ATOM   458  N  N   . ALA A 1 75  ? 93.394  82.204  93.943  1.00 21.05 ? 64   ALA A N   1 
ATOM   459  C  CA  . ALA A 1 75  ? 94.114  81.887  95.166  1.00 21.05 ? 64   ALA A CA  1 
ATOM   460  C  C   . ALA A 1 75  ? 94.590  83.115  95.925  1.00 21.05 ? 64   ALA A C   1 
ATOM   461  O  O   . ALA A 1 75  ? 95.033  82.978  97.068  1.00 21.05 ? 64   ALA A O   1 
ATOM   462  C  CB  . ALA A 1 75  ? 95.320  81.000  94.849  1.00 21.05 ? 64   ALA A CB  1 
ATOM   463  N  N   . ALA A 1 76  ? 94.526  84.296  95.324  1.00 20.53 ? 65   ALA A N   1 
ATOM   464  C  CA  . ALA A 1 76  ? 94.929  85.521  95.999  1.00 20.53 ? 65   ALA A CA  1 
ATOM   465  C  C   . ALA A 1 76  ? 93.844  86.003  96.956  1.00 20.53 ? 65   ALA A C   1 
ATOM   466  O  O   . ALA A 1 76  ? 94.148  86.320  98.114  1.00 20.53 ? 65   ALA A O   1 
ATOM   467  C  CB  . ALA A 1 76  ? 95.261  86.606  94.978  1.00 20.53 ? 65   ALA A CB  1 
ATOM   468  N  N   . PRO A 1 77  ? 92.580  86.095  96.526  1.00 19.44 ? 66   PRO A N   1 
ATOM   469  C  CA  . PRO A 1 77  ? 91.528  86.495  97.473  1.00 19.44 ? 66   PRO A CA  1 
ATOM   470  C  C   . PRO A 1 77  ? 91.380  85.555  98.655  1.00 19.44 ? 66   PRO A C   1 
ATOM   471  O  O   . PRO A 1 77  ? 91.068  86.018  99.758  1.00 19.44 ? 66   PRO A O   1 
ATOM   472  C  CB  . PRO A 1 77  ? 90.264  86.520  96.603  1.00 19.44 ? 66   PRO A CB  1 
ATOM   473  C  CG  . PRO A 1 77  ? 90.614  85.776  95.381  1.00 19.44 ? 66   PRO A CG  1 
ATOM   474  C  CD  . PRO A 1 77  ? 92.052  86.037  95.156  1.00 19.44 ? 66   PRO A CD  1 
ATOM   475  N  N   . LEU A 1 78  ? 91.598  84.253  98.474  1.00 19.81 ? 67   LEU A N   1 
ATOM   476  C  CA  . LEU A 1 78  ? 91.518  83.336  99.606  1.00 19.81 ? 67   LEU A CA  1 
ATOM   477  C  C   . LEU A 1 78  ? 92.593  83.641  100.641 1.00 19.81 ? 67   LEU A C   1 
ATOM   478  O  O   . LEU A 1 78  ? 92.316  83.673  101.848 1.00 19.81 ? 67   LEU A O   1 
ATOM   479  C  CB  . LEU A 1 78  ? 91.640  81.895  99.119  1.00 19.81 ? 67   LEU A CB  1 
ATOM   480  C  CG  . LEU A 1 78  ? 90.491  81.359  98.267  1.00 19.81 ? 67   LEU A CG  1 
ATOM   481  C  CD1 . LEU A 1 78  ? 90.874  80.038  97.650  1.00 19.81 ? 67   LEU A CD1 1 
ATOM   482  C  CD2 . LEU A 1 78  ? 89.244  81.195  99.095  1.00 19.81 ? 67   LEU A CD2 1 
ATOM   483  N  N   . ALA A 1 79  ? 93.826  83.877  100.188 1.00 19.56 ? 68   ALA A N   1 
ATOM   484  C  CA  . ALA A 1 79  ? 94.901  84.230  101.110 1.00 19.56 ? 68   ALA A CA  1 
ATOM   485  C  C   . ALA A 1 79  ? 94.628  85.565  101.786 1.00 19.56 ? 68   ALA A C   1 
ATOM   486  O  O   . ALA A 1 79  ? 94.894  85.728  102.983 1.00 19.56 ? 68   ALA A O   1 
ATOM   487  C  CB  . ALA A 1 79  ? 96.232  84.274  100.368 1.00 19.56 ? 68   ALA A CB  1 
ATOM   488  N  N   . ALA A 1 80  ? 94.105  86.535  101.035 1.00 19.07 ? 69   ALA A N   1 
ATOM   489  C  CA  . ALA A 1 80  ? 93.777  87.826  101.628 1.00 19.07 ? 69   ALA A CA  1 
ATOM   490  C  C   . ALA A 1 80  ? 92.725  87.681  102.717 1.00 19.07 ? 69   ALA A C   1 
ATOM   491  O  O   . ALA A 1 80  ? 92.844  88.284  103.787 1.00 19.07 ? 69   ALA A O   1 
ATOM   492  C  CB  . ALA A 1 80  ? 93.293  88.789  100.549 1.00 19.07 ? 69   ALA A CB  1 
ATOM   493  N  N   . VAL A 1 81  ? 91.685  86.885  102.463 1.00 20.14 ? 70   VAL A N   1 
ATOM   494  C  CA  . VAL A 1 81  ? 90.634  86.692  103.459 1.00 20.14 ? 70   VAL A CA  1 
ATOM   495  C  C   . VAL A 1 81  ? 91.192  85.999  104.693 1.00 20.14 ? 70   VAL A C   1 
ATOM   496  O  O   . VAL A 1 81  ? 90.876  86.373  105.831 1.00 20.14 ? 70   VAL A O   1 
ATOM   497  C  CB  . VAL A 1 81  ? 89.461  85.904  102.850 1.00 20.14 ? 70   VAL A CB  1 
ATOM   498  C  CG1 . VAL A 1 81  ? 88.466  85.525  103.923 1.00 20.14 ? 70   VAL A CG1 1 
ATOM   499  C  CG2 . VAL A 1 81  ? 88.782  86.717  101.772 1.00 20.14 ? 70   VAL A CG2 1 
ATOM   500  N  N   . ASP A 1 82  ? 92.027  84.978  104.493 1.00 21.61 ? 71   ASP A N   1 
ATOM   501  C  CA  . ASP A 1 82  ? 92.617  84.282  105.631 1.00 21.61 ? 71   ASP A CA  1 
ATOM   502  C  C   . ASP A 1 82  ? 93.458  85.229  106.475 1.00 21.61 ? 71   ASP A C   1 
ATOM   503  O  O   . ASP A 1 82  ? 93.363  85.231  107.707 1.00 21.61 ? 71   ASP A O   1 
ATOM   504  C  CB  . ASP A 1 82  ? 93.462  83.110  105.142 1.00 21.61 ? 71   ASP A CB  1 
ATOM   505  C  CG  . ASP A 1 82  ? 92.633  81.892  104.821 1.00 21.61 ? 71   ASP A CG  1 
ATOM   506  O  OD1 . ASP A 1 82  ? 91.391  81.975  104.909 1.00 21.61 ? 71   ASP A OD1 1 
ATOM   507  O  OD2 . ASP A 1 82  ? 93.226  80.850  104.477 1.00 21.61 ? 71   ASP A OD2 1 
ATOM   508  N  N   . LEU A 1 83  ? 94.289  86.046  105.826 1.00 21.73 ? 72   LEU A N   1 
ATOM   509  C  CA  . LEU A 1 83  ? 95.110  86.999  106.565 1.00 21.73 ? 72   LEU A CA  1 
ATOM   510  C  C   . LEU A 1 83  ? 94.245  87.998  107.318 1.00 21.73 ? 72   LEU A C   1 
ATOM   511  O  O   . LEU A 1 83  ? 94.494  88.283  108.495 1.00 21.73 ? 72   LEU A O   1 
ATOM   512  C  CB  . LEU A 1 83  ? 96.046  87.733  105.610 1.00 21.73 ? 72   LEU A CB  1 
ATOM   513  C  CG  . LEU A 1 83  ? 97.196  86.931  105.013 1.00 21.73 ? 72   LEU A CG  1 
ATOM   514  C  CD1 . LEU A 1 83  ? 97.769  87.669  103.828 1.00 21.73 ? 72   LEU A CD1 1 
ATOM   515  C  CD2 . LEU A 1 83  ? 98.256  86.679  106.056 1.00 21.73 ? 72   LEU A CD2 1 
ATOM   516  N  N   . LYS A 1 84  ? 93.218  88.533  106.658 1.00 23.14 ? 73   LYS A N   1 
ATOM   517  C  CA  . LYS A 1 84  ? 92.352  89.514  107.299 1.00 23.14 ? 73   LYS A CA  1 
ATOM   518  C  C   . LYS A 1 84  ? 91.696  88.936  108.543 1.00 23.14 ? 73   LYS A C   1 
ATOM   519  O  O   . LYS A 1 84  ? 91.646  89.589  109.591 1.00 23.14 ? 73   LYS A O   1 
ATOM   520  C  CB  . LYS A 1 84  ? 91.293  89.993  106.309 1.00 23.14 ? 73   LYS A CB  1 
ATOM   521  C  CG  . LYS A 1 84  ? 90.302  90.997  106.872 1.00 23.14 ? 73   LYS A CG  1 
ATOM   522  C  CD  . LYS A 1 84  ? 90.957  92.306  107.234 1.00 23.14 ? 73   LYS A CD  1 
ATOM   523  C  CE  . LYS A 1 84  ? 89.918  93.353  107.554 1.00 23.14 ? 73   LYS A CE  1 
ATOM   524  N  NZ  . LYS A 1 84  ? 89.116  92.983  108.741 1.00 23.14 ? 73   LYS A NZ  1 
ATOM   525  N  N   . TRP A 1 85  ? 91.182  87.710  108.451 1.00 25.56 ? 74   TRP A N   1 
ATOM   526  C  CA  . TRP A 1 85  ? 90.472  87.150  109.594 1.00 25.56 ? 74   TRP A CA  1 
ATOM   527  C  C   . TRP A 1 85  ? 91.421  86.704  110.698 1.00 25.56 ? 74   TRP A C   1 
ATOM   528  O  O   . TRP A 1 85  ? 91.061  86.769  111.877 1.00 25.56 ? 74   TRP A O   1 
ATOM   529  C  CB  . TRP A 1 85  ? 89.592  85.981  109.163 1.00 25.56 ? 74   TRP A CB  1 
ATOM   530  C  CG  . TRP A 1 85  ? 88.681  85.519  110.262 1.00 25.56 ? 74   TRP A CG  1 
ATOM   531  C  CD1 . TRP A 1 85  ? 88.649  84.281  110.835 1.00 25.56 ? 74   TRP A CD1 1 
ATOM   532  C  CD2 . TRP A 1 85  ? 87.685  86.298  110.939 1.00 25.56 ? 74   TRP A CD2 1 
ATOM   533  N  NE1 . TRP A 1 85  ? 87.689  84.238  111.816 1.00 25.56 ? 74   TRP A NE1 1 
ATOM   534  C  CE2 . TRP A 1 85  ? 87.085  85.464  111.899 1.00 25.56 ? 74   TRP A CE2 1 
ATOM   535  C  CE3 . TRP A 1 85  ? 87.241  87.619  110.822 1.00 25.56 ? 74   TRP A CE3 1 
ATOM   536  C  CZ2 . TRP A 1 85  ? 86.066  85.906  112.734 1.00 25.56 ? 74   TRP A CZ2 1 
ATOM   537  C  CZ3 . TRP A 1 85  ? 86.228  88.054  111.652 1.00 25.56 ? 74   TRP A CZ3 1 
ATOM   538  C  CH2 . TRP A 1 85  ? 85.653  87.202  112.595 1.00 25.56 ? 74   TRP A CH2 1 
ATOM   539  N  N   . GLU A 1 86  ? 92.628  86.255  110.354 1.00 26.45 ? 75   GLU A N   1 
ATOM   540  C  CA  . GLU A 1 86  ? 93.518  85.709  111.370 1.00 26.45 ? 75   GLU A CA  1 
ATOM   541  C  C   . GLU A 1 86  ? 94.337  86.778  112.081 1.00 26.45 ? 75   GLU A C   1 
ATOM   542  O  O   . GLU A 1 86  ? 94.509  86.704  113.302 1.00 26.45 ? 75   GLU A O   1 
ATOM   543  C  CB  . GLU A 1 86  ? 94.456  84.677  110.742 1.00 26.45 ? 75   GLU A CB  1 
ATOM   544  N  N   . HIS A 1 87  ? 94.848  87.777  111.354 1.00 26.39 ? 76   HIS A N   1 
ATOM   545  C  CA  . HIS A 1 87  ? 95.790  88.730  111.925 1.00 26.39 ? 76   HIS A CA  1 
ATOM   546  C  C   . HIS A 1 87  ? 95.269  90.154  112.022 1.00 26.39 ? 76   HIS A C   1 
ATOM   547  O  O   . HIS A 1 87  ? 95.808  90.933  112.812 1.00 26.39 ? 76   HIS A O   1 
ATOM   548  C  CB  . HIS A 1 87  ? 97.087  88.742  111.106 1.00 26.39 ? 76   HIS A CB  1 
ATOM   549  C  CG  . HIS A 1 87  ? 97.742  87.402  111.000 1.00 26.39 ? 76   HIS A CG  1 
ATOM   550  N  ND1 . HIS A 1 87  ? 98.516  86.871  112.008 1.00 26.39 ? 76   HIS A ND1 1 
ATOM   551  C  CD2 . HIS A 1 87  ? 97.745  86.487  110.003 1.00 26.39 ? 76   HIS A CD2 1 
ATOM   552  C  CE1 . HIS A 1 87  ? 98.964  85.686  111.638 1.00 26.39 ? 76   HIS A CE1 1 
ATOM   553  N  NE2 . HIS A 1 87  ? 98.511  85.429  110.425 1.00 26.39 ? 76   HIS A NE2 1 
ATOM   554  N  N   . ASN A 1 88  ? 94.251  90.518  111.252 1.00 27.32 ? 77   ASN A N   1 
ATOM   555  C  CA  . ASN A 1 88  ? 93.710  91.870  111.308 1.00 27.32 ? 77   ASN A CA  1 
ATOM   556  C  C   . ASN A 1 88  ? 94.775  92.885  110.905 1.00 27.32 ? 77   ASN A C   1 
ATOM   557  O  O   . ASN A 1 88  ? 95.240  93.666  111.743 1.00 27.32 ? 77   ASN A O   1 
ATOM   558  C  CB  . ASN A 1 88  ? 93.182  92.163  112.713 1.00 27.32 ? 77   ASN A CB  1 
ATOM   559  C  CG  . ASN A 1 88  ? 92.039  93.154  112.711 1.00 27.32 ? 77   ASN A CG  1 
ATOM   560  O  OD1 . ASN A 1 88  ? 91.289  93.255  111.741 1.00 27.32 ? 77   ASN A OD1 1 
ATOM   561  N  ND2 . ASN A 1 88  ? 91.899  93.895  113.803 1.00 27.32 ? 77   ASN A ND2 1 
ATOM   562  N  N   . PRO A 1 89  ? 95.186  92.904  109.640 1.00 24.41 ? 78   PRO A N   1 
ATOM   563  C  CA  . PRO A 1 89  ? 96.244  93.825  109.220 1.00 24.41 ? 78   PRO A CA  1 
ATOM   564  C  C   . PRO A 1 89  ? 95.777  95.271  109.229 1.00 24.41 ? 78   PRO A C   1 
ATOM   565  O  O   . PRO A 1 89  ? 94.585  95.574  109.274 1.00 24.41 ? 78   PRO A O   1 
ATOM   566  C  CB  . PRO A 1 89  ? 96.569  93.367  107.795 1.00 24.41 ? 78   PRO A CB  1 
ATOM   567  C  CG  . PRO A 1 89  ? 95.911  92.049  107.636 1.00 24.41 ? 78   PRO A CG  1 
ATOM   568  C  CD  . PRO A 1 89  ? 94.732  92.066  108.525 1.00 24.41 ? 78   PRO A CD  1 
ATOM   569  N  N   . ALA A 1 90  ? 96.755  96.173  109.187 1.00 25.55 ? 79   ALA A N   1 
ATOM   570  C  CA  . ALA A 1 90  ? 96.491  97.590  108.994 1.00 25.55 ? 79   ALA A CA  1 
ATOM   571  C  C   . ALA A 1 90  ? 96.660  98.029  107.548 1.00 25.55 ? 79   ALA A C   1 
ATOM   572  O  O   . ALA A 1 90  ? 96.083  99.047  107.155 1.00 25.55 ? 79   ALA A O   1 
ATOM   573  C  CB  . ALA A 1 90  ? 97.420  98.428  109.878 1.00 25.55 ? 79   ALA A CB  1 
ATOM   574  N  N   . VAL A 1 91  ? 97.431  97.286  106.754 1.00 23.19 ? 80   VAL A N   1 
ATOM   575  C  CA  . VAL A 1 91  ? 97.689  97.633  105.363 1.00 23.19 ? 80   VAL A CA  1 
ATOM   576  C  C   . VAL A 1 91  ? 98.055  96.351  104.637 1.00 23.19 ? 80   VAL A C   1 
ATOM   577  O  O   . VAL A 1 91  ? 98.516  95.389  105.246 1.00 23.19 ? 80   VAL A O   1 
ATOM   578  C  CB  . VAL A 1 91  ? 98.813  98.696  105.250 1.00 23.19 ? 80   VAL A CB  1 
ATOM   579  C  CG1 . VAL A 1 91  ? 100.056 98.237  105.980 1.00 23.19 ? 80   VAL A CG1 1 
ATOM   580  C  CG2 . VAL A 1 91  ? 99.137  98.989  103.802 1.00 23.19 ? 80   VAL A CG2 1 
ATOM   581  N  N   . PHE A 1 92  ? 97.842  96.333  103.327 1.00 20.77 ? 81   PHE A N   1 
ATOM   582  C  CA  . PHE A 1 92  ? 98.188  95.198  102.485 1.00 20.77 ? 81   PHE A CA  1 
ATOM   583  C  C   . PHE A 1 92  ? 99.286  95.600  101.513 1.00 20.77 ? 81   PHE A C   1 
ATOM   584  O  O   . PHE A 1 92  ? 99.217  96.672  100.908 1.00 20.77 ? 81   PHE A O   1 
ATOM   585  C  CB  . PHE A 1 92  ? 96.973  94.697  101.702 1.00 20.77 ? 81   PHE A CB  1 
ATOM   586  C  CG  . PHE A 1 92  ? 96.092  93.755  102.473 1.00 20.77 ? 81   PHE A CG  1 
ATOM   587  C  CD1 . PHE A 1 92  ? 95.223  94.228  103.434 1.00 20.77 ? 81   PHE A CD1 1 
ATOM   588  C  CD2 . PHE A 1 92  ? 96.127  92.397  102.227 1.00 20.77 ? 81   PHE A CD2 1 
ATOM   589  C  CE1 . PHE A 1 92  ? 94.412  93.364  104.138 1.00 20.77 ? 81   PHE A CE1 1 
ATOM   590  C  CE2 . PHE A 1 92  ? 95.318  91.535  102.931 1.00 20.77 ? 81   PHE A CE2 1 
ATOM   591  C  CZ  . PHE A 1 92  ? 94.462  92.021  103.887 1.00 20.77 ? 81   PHE A CZ  1 
ATOM   592  N  N   . LEU A 1 93  ? 100.301 94.749  101.375 1.00 21.33 ? 82   LEU A N   1 
ATOM   593  C  CA  . LEU A 1 93  ? 101.235 94.843  100.252 1.00 21.33 ? 82   LEU A CA  1 
ATOM   594  C  C   . LEU A 1 93  ? 100.681 93.999  99.107  1.00 21.33 ? 82   LEU A C   1 
ATOM   595  O  O   . LEU A 1 93  ? 101.211 92.956  98.730  1.00 21.33 ? 82   LEU A O   1 
ATOM   596  C  CB  . LEU A 1 93  ? 102.630 94.399  100.665 1.00 21.33 ? 82   LEU A CB  1 
ATOM   597  C  CG  . LEU A 1 93  ? 103.671 95.515  100.699 1.00 21.33 ? 82   LEU A CG  1 
ATOM   598  C  CD1 . LEU A 1 93  ? 103.383 96.474  101.832 1.00 21.33 ? 82   LEU A CD1 1 
ATOM   599  C  CD2 . LEU A 1 93  ? 105.063 94.937  100.825 1.00 21.33 ? 82   LEU A CD2 1 
ATOM   600  N  N   . GLY A 1 94  ? 99.582  94.492  98.554  1.00 21.15 ? 83   GLY A N   1 
ATOM   601  C  CA  . GLY A 1 94  ? 98.728  93.711  97.699  1.00 21.15 ? 83   GLY A CA  1 
ATOM   602  C  C   . GLY A 1 94  ? 99.461  93.071  96.548  1.00 21.15 ? 83   GLY A C   1 
ATOM   603  O  O   . GLY A 1 94  ? 100.642 93.328  96.309  1.00 21.15 ? 83   GLY A O   1 
ATOM   604  N  N   . PRO A 1 95  ? 98.762  92.213  95.811  1.00 20.75 ? 84   PRO A N   1 
ATOM   605  C  CA  . PRO A 1 95  ? 99.400  91.487  94.714  1.00 20.75 ? 84   PRO A CA  1 
ATOM   606  C  C   . PRO A 1 95  ? 99.957  92.434  93.667  1.00 20.75 ? 84   PRO A C   1 
ATOM   607  O  O   . PRO A 1 95  ? 99.676  93.632  93.645  1.00 20.75 ? 84   PRO A O   1 
ATOM   608  C  CB  . PRO A 1 95  ? 98.262  90.633  94.153  1.00 20.75 ? 84   PRO A CB  1 
ATOM   609  C  CG  . PRO A 1 95  ? 97.313  90.504  95.268  1.00 20.75 ? 84   PRO A CG  1 
ATOM   610  C  CD  . PRO A 1 95  ? 97.358  91.812  95.974  1.00 20.75 ? 84   PRO A CD  1 
ATOM   611  N  N   . GLY A 1 96  ? 100.779 91.872  92.791  1.00 21.23 ? 85   GLY A N   1 
ATOM   612  C  CA  . GLY A 1 96  ? 101.331 92.618  91.684  1.00 21.23 ? 85   GLY A CA  1 
ATOM   613  C  C   . GLY A 1 96  ? 100.722 92.204  90.365  1.00 21.23 ? 85   GLY A C   1 
ATOM   614  O  O   . GLY A 1 96  ? 100.680 92.997  89.424  1.00 21.23 ? 85   GLY A O   1 
ATOM   615  N  N   . CYS A 1 97  ? 100.253 90.964  90.276  1.00 22.99 ? 86   CYS A N   1 
ATOM   616  C  CA  . CYS A 1 97  ? 99.660  90.487  89.039  1.00 22.99 ? 86   CYS A CA  1 
ATOM   617  C  C   . CYS A 1 97  ? 98.359  91.224  88.757  1.00 22.99 ? 86   CYS A C   1 
ATOM   618  O  O   . CYS A 1 97  ? 97.622  91.605  89.668  1.00 22.99 ? 86   CYS A O   1 
ATOM   619  C  CB  . CYS A 1 97  ? 99.410  88.980  89.106  1.00 22.99 ? 86   CYS A CB  1 
ATOM   620  S  SG  . CYS A 1 97  ? 100.874 88.004  89.530  1.00 22.99 ? 86   CYS A SG  1 
ATOM   621  N  N   . VAL A 1 98  ? 98.086  91.433  87.469  1.00 23.52 ? 87   VAL A N   1 
ATOM   622  C  CA  . VAL A 1 98  ? 96.890  92.165  87.074  1.00 23.52 ? 87   VAL A CA  1 
ATOM   623  C  C   . VAL A 1 98  ? 95.632  91.390  87.431  1.00 23.52 ? 87   VAL A C   1 
ATOM   624  O  O   . VAL A 1 98  ? 94.582  91.986  87.691  1.00 23.52 ? 87   VAL A O   1 
ATOM   625  C  CB  . VAL A 1 98  ? 96.946  92.481  85.571  1.00 23.52 ? 87   VAL A CB  1 
ATOM   626  C  CG1 . VAL A 1 98  ? 95.626  93.043  85.101  1.00 23.52 ? 87   VAL A CG1 1 
ATOM   627  C  CG2 . VAL A 1 98  ? 98.070  93.452  85.286  1.00 23.52 ? 87   VAL A CG2 1 
ATOM   628  N  N   . TYR A 1 99  ? 95.706  90.062  87.441  1.00 24.56 ? 88   TYR A N   1 
ATOM   629  C  CA  . TYR A 1 99  ? 94.539  89.229  87.690  1.00 24.56 ? 88   TYR A CA  1 
ATOM   630  C  C   . TYR A 1 99  ? 94.327  88.939  89.166  1.00 24.56 ? 88   TYR A C   1 
ATOM   631  O  O   . TYR A 1 99  ? 93.180  88.819  89.605  1.00 24.56 ? 88   TYR A O   1 
ATOM   632  C  CB  . TYR A 1 99  ? 94.672  87.911  86.927  1.00 24.56 ? 88   TYR A CB  1 
ATOM   633  C  CG  . TYR A 1 99  ? 94.490  88.052  85.436  1.00 24.56 ? 88   TYR A CG  1 
ATOM   634  C  CD1 . TYR A 1 99  ? 93.383  88.699  84.910  1.00 24.56 ? 88   TYR A CD1 1 
ATOM   635  C  CD2 . TYR A 1 99  ? 95.429  87.546  84.555  1.00 24.56 ? 88   TYR A CD2 1 
ATOM   636  C  CE1 . TYR A 1 99  ? 93.214  88.829  83.553  1.00 24.56 ? 88   TYR A CE1 1 
ATOM   637  C  CE2 . TYR A 1 99  ? 95.268  87.672  83.196  1.00 24.56 ? 88   TYR A CE2 1 
ATOM   638  C  CZ  . TYR A 1 99  ? 94.160  88.315  82.700  1.00 24.56 ? 88   TYR A CZ  1 
ATOM   639  O  OH  . TYR A 1 99  ? 93.991  88.447  81.343  1.00 24.56 ? 88   TYR A OH  1 
ATOM   640  N  N   . ALA A 1 100 ? 95.402  88.818  89.940  1.00 20.64 ? 89   ALA A N   1 
ATOM   641  C  CA  . ALA A 1 100 ? 95.266  88.626  91.376  1.00 20.64 ? 89   ALA A CA  1 
ATOM   642  C  C   . ALA A 1 100 ? 94.902  89.916  92.093  1.00 20.64 ? 89   ALA A C   1 
ATOM   643  O  O   . ALA A 1 100 ? 94.195  89.877  93.104  1.00 20.64 ? 89   ALA A O   1 
ATOM   644  C  CB  . ALA A 1 100 ? 96.563  88.064  91.954  1.00 20.64 ? 89   ALA A CB  1 
ATOM   645  N  N   . ALA A 1 101 ? 95.362  91.061  91.588  1.00 20.73 ? 90   ALA A N   1 
ATOM   646  C  CA  . ALA A 1 101 ? 95.197  92.325  92.291  1.00 20.73 ? 90   ALA A CA  1 
ATOM   647  C  C   . ALA A 1 101 ? 93.779  92.869  92.221  1.00 20.73 ? 90   ALA A C   1 
ATOM   648  O  O   . ALA A 1 101 ? 93.403  93.678  93.074  1.00 20.73 ? 90   ALA A O   1 
ATOM   649  C  CB  . ALA A 1 101 ? 96.168  93.363  91.730  1.00 20.73 ? 90   ALA A CB  1 
ATOM   650  N  N   . ALA A 1 102 ? 92.982  92.453  91.231  1.00 20.93 ? 91   ALA A N   1 
ATOM   651  C  CA  . ALA A 1 102 ? 91.619  92.975  91.131  1.00 20.93 ? 91   ALA A CA  1 
ATOM   652  C  C   . ALA A 1 102 ? 90.737  92.462  92.262  1.00 20.93 ? 91   ALA A C   1 
ATOM   653  O  O   . ALA A 1 102 ? 90.178  93.283  93.011  1.00 20.93 ? 91   ALA A O   1 
ATOM   654  C  CB  . ALA A 1 102 ? 91.038  92.652  89.755  1.00 20.93 ? 91   ALA A CB  1 
ATOM   655  N  N   . PRO A 1 103 ? 90.546  91.151  92.437  1.00 19.32 ? 92   PRO A N   1 
ATOM   656  C  CA  . PRO A 1 103 ? 89.704  90.688  93.553  1.00 19.32 ? 92   PRO A CA  1 
ATOM   657  C  C   . PRO A 1 103 ? 90.184  91.153  94.916  1.00 19.32 ? 92   PRO A C   1 
ATOM   658  O  O   . PRO A 1 103 ? 89.365  91.531  95.763  1.00 19.32 ? 92   PRO A O   1 
ATOM   659  C  CB  . PRO A 1 103 ? 89.763  89.159  93.421  1.00 19.32 ? 92   PRO A CB  1 
ATOM   660  C  CG  . PRO A 1 103 ? 90.866  88.873  92.466  1.00 19.32 ? 92   PRO A CG  1 
ATOM   661  C  CD  . PRO A 1 103 ? 90.938  90.038  91.562  1.00 19.32 ? 92   PRO A CD  1 
ATOM   662  N  N   . VAL A 1 104 ? 91.495  91.154  95.150  1.00 19.02 ? 93   VAL A N   1 
ATOM   663  C  CA  . VAL A 1 104 ? 92.016  91.616  96.430  1.00 19.02 ? 93   VAL A CA  1 
ATOM   664  C  C   . VAL A 1 104 ? 91.775  93.108  96.592  1.00 19.02 ? 93   VAL A C   1 
ATOM   665  O  O   . VAL A 1 104 ? 91.462  93.587  97.688  1.00 19.02 ? 93   VAL A O   1 
ATOM   666  C  CB  . VAL A 1 104 ? 93.508  91.268  96.556  1.00 19.02 ? 93   VAL A CB  1 
ATOM   667  C  CG1 . VAL A 1 104 ? 94.034  91.695  97.910  1.00 19.02 ? 93   VAL A CG1 1 
ATOM   668  C  CG2 . VAL A 1 104 ? 93.723  89.791  96.350  1.00 19.02 ? 93   VAL A CG2 1 
ATOM   669  N  N   . GLY A 1 105 ? 91.927  93.870  95.511  1.00 20.16 ? 94   GLY A N   1 
ATOM   670  C  CA  . GLY A 1 105 ? 91.638  95.290  95.582  1.00 20.16 ? 94   GLY A CA  1 
ATOM   671  C  C   . GLY A 1 105 ? 90.195  95.566  95.950  1.00 20.16 ? 94   GLY A C   1 
ATOM   672  O  O   . GLY A 1 105 ? 89.911  96.435  96.775  1.00 20.16 ? 94   GLY A O   1 
ATOM   673  N  N   . ARG A 1 106 ? 89.263  94.823  95.351  1.00 20.79 ? 95   ARG A N   1 
ATOM   674  C  CA  . ARG A 1 106 ? 87.854  94.999  95.689  1.00 20.79 ? 95   ARG A CA  1 
ATOM   675  C  C   . ARG A 1 106 ? 87.573  94.607  97.135  1.00 20.79 ? 95   ARG A C   1 
ATOM   676  O  O   . ARG A 1 106 ? 86.827  95.300  97.839  1.00 20.79 ? 95   ARG A O   1 
ATOM   677  C  CB  . ARG A 1 106 ? 86.985  94.195  94.727  1.00 20.79 ? 95   ARG A CB  1 
ATOM   678  C  CG  . ARG A 1 106 ? 86.899  94.834  93.358  1.00 20.79 ? 95   ARG A CG  1 
ATOM   679  C  CD  . ARG A 1 106 ? 85.897  94.155  92.462  1.00 20.79 ? 95   ARG A CD  1 
ATOM   680  N  NE  . ARG A 1 106 ? 86.195  92.739  92.265  1.00 20.79 ? 95   ARG A NE  1 
ATOM   681  C  CZ  . ARG A 1 106 ? 86.597  92.195  91.118  1.00 20.79 ? 95   ARG A CZ  1 
ATOM   682  N  NH1 . ARG A 1 106 ? 86.772  92.936  90.031  1.00 20.79 ? 95   ARG A NH1 1 
ATOM   683  N  NH2 . ARG A 1 106 ? 86.827  90.893  91.059  1.00 20.79 ? 95   ARG A NH2 1 
ATOM   684  N  N   . PHE A 1 107 ? 88.169  93.513  97.607  1.00 18.84 ? 96   PHE A N   1 
ATOM   685  C  CA  . PHE A 1 107 ? 87.957  93.110  98.994  1.00 18.84 ? 96   PHE A CA  1 
ATOM   686  C  C   . PHE A 1 107 ? 88.456  94.178  99.961  1.00 18.84 ? 96   PHE A C   1 
ATOM   687  O  O   . PHE A 1 107 ? 87.750  94.555  100.903 1.00 18.84 ? 96   PHE A O   1 
ATOM   688  C  CB  . PHE A 1 107 ? 88.648  91.775  99.263  1.00 18.84 ? 96   PHE A CB  1 
ATOM   689  C  CG  . PHE A 1 107 ? 87.772  90.585  99.015  1.00 18.84 ? 96   PHE A CG  1 
ATOM   690  C  CD1 . PHE A 1 107 ? 86.790  90.231  99.916  1.00 18.84 ? 96   PHE A CD1 1 
ATOM   691  C  CD2 . PHE A 1 107 ? 87.923  89.828  97.873  1.00 18.84 ? 96   PHE A CD2 1 
ATOM   692  C  CE1 . PHE A 1 107 ? 85.987  89.144  99.683  1.00 18.84 ? 96   PHE A CE1 1 
ATOM   693  C  CE2 . PHE A 1 107 ? 87.118  88.744  97.639  1.00 18.84 ? 96   PHE A CE2 1 
ATOM   694  C  CZ  . PHE A 1 107 ? 86.153  88.402  98.543  1.00 18.84 ? 96   PHE A CZ  1 
ATOM   695  N  N   . THR A 1 108 ? 89.673  94.683  99.745  1.00 20.48 ? 97   THR A N   1 
ATOM   696  C  CA  . THR A 1 108 ? 90.223  95.663  100.678 1.00 20.48 ? 97   THR A CA  1 
ATOM   697  C  C   . THR A 1 108 ? 89.517  97.006  100.567 1.00 20.48 ? 97   THR A C   1 
ATOM   698  O  O   . THR A 1 108 ? 89.450  97.747  101.552 1.00 20.48 ? 97   THR A O   1 
ATOM   699  C  CB  . THR A 1 108 ? 91.723  95.844  100.458 1.00 20.48 ? 97   THR A CB  1 
ATOM   700  O  OG1 . THR A 1 108 ? 91.958  96.364  99.147  1.00 20.48 ? 97   THR A OG1 1 
ATOM   701  C  CG2 . THR A 1 108 ? 92.453  94.531  100.628 1.00 20.48 ? 97   THR A CG2 1 
ATOM   702  N  N   . ALA A 1 109 ? 88.994  97.346  99.387  1.00 21.60 ? 98   ALA A N   1 
ATOM   703  C  CA  . ALA A 1 109 ? 88.130  98.514  99.285  1.00 21.60 ? 98   ALA A CA  1 
ATOM   704  C  C   . ALA A 1 109 ? 86.882  98.331  100.131 1.00 21.60 ? 98   ALA A C   1 
ATOM   705  O  O   . ALA A 1 109 ? 86.426  99.270  100.792 1.00 21.60 ? 98   ALA A O   1 
ATOM   706  C  CB  . ALA A 1 109 ? 87.755  98.762  97.828  1.00 21.60 ? 98   ALA A CB  1 
ATOM   707  N  N   . HIS A 1 110 ? 86.312  97.123  100.122 1.00 21.25 ? 99   HIS A N   1 
ATOM   708  C  CA  . HIS A 1 110 ? 85.146  96.851  100.957 1.00 21.25 ? 99   HIS A CA  1 
ATOM   709  C  C   . HIS A 1 110 ? 85.476  96.972  102.441 1.00 21.25 ? 99   HIS A C   1 
ATOM   710  O  O   . HIS A 1 110 ? 84.692  97.538  103.210 1.00 21.25 ? 99   HIS A O   1 
ATOM   711  C  CB  . HIS A 1 110 ? 84.593  95.463  100.647 1.00 21.25 ? 99   HIS A CB  1 
ATOM   712  C  CG  . HIS A 1 110 ? 83.331  95.140  101.382 1.00 21.25 ? 99   HIS A CG  1 
ATOM   713  N  ND1 . HIS A 1 110 ? 82.114  95.689  101.046 1.00 21.25 ? 99   HIS A ND1 1 
ATOM   714  C  CD2 . HIS A 1 110 ? 83.096  94.319  102.432 1.00 21.25 ? 99   HIS A CD2 1 
ATOM   715  C  CE1 . HIS A 1 110 ? 81.184  95.225  101.860 1.00 21.25 ? 99   HIS A CE1 1 
ATOM   716  N  NE2 . HIS A 1 110 ? 81.754  94.391  102.710 1.00 21.25 ? 99   HIS A NE2 1 
ATOM   717  N  N   . TRP A 1 111 ? 86.621  96.438  102.870 1.00 21.58 ? 100  TRP A N   1 
ATOM   718  C  CA  . TRP A 1 111 ? 86.979  96.497  104.284 1.00 21.58 ? 100  TRP A CA  1 
ATOM   719  C  C   . TRP A 1 111 ? 87.483  97.866  104.720 1.00 21.58 ? 100  TRP A C   1 
ATOM   720  O  O   . TRP A 1 111 ? 87.690  98.071  105.920 1.00 21.58 ? 100  TRP A O   1 
ATOM   721  C  CB  . TRP A 1 111 ? 88.058  95.469  104.628 1.00 21.58 ? 100  TRP A CB  1 
ATOM   722  C  CG  . TRP A 1 111 ? 87.727  94.058  104.291 1.00 21.58 ? 100  TRP A CG  1 
ATOM   723  C  CD1 . TRP A 1 111 ? 86.511  93.459  104.364 1.00 21.58 ? 100  TRP A CD1 1 
ATOM   724  C  CD2 . TRP A 1 111 ? 88.644  93.054  103.850 1.00 21.58 ? 100  TRP A CD2 1 
ATOM   725  N  NE1 . TRP A 1 111 ? 86.607  92.145  103.981 1.00 21.58 ? 100  TRP A NE1 1 
ATOM   726  C  CE2 . TRP A 1 111 ? 87.911  91.872  103.663 1.00 21.58 ? 100  TRP A CE2 1 
ATOM   727  C  CE3 . TRP A 1 111 ? 90.017  93.042  103.590 1.00 21.58 ? 100  TRP A CE3 1 
ATOM   728  C  CZ2 . TRP A 1 111 ? 88.501  90.693  103.225 1.00 21.58 ? 100  TRP A CZ2 1 
ATOM   729  C  CZ3 . TRP A 1 111 ? 90.598  91.873  103.155 1.00 21.58 ? 100  TRP A CZ3 1 
ATOM   730  C  CH2 . TRP A 1 111 ? 89.844  90.716  102.977 1.00 21.58 ? 100  TRP A CH2 1 
ATOM   731  N  N   . ARG A 1 112 ? 87.698  98.795  103.788 1.00 25.75 ? 101  ARG A N   1 
ATOM   732  C  CA  . ARG A 1 112 ? 88.241  100.119 104.096 1.00 25.75 ? 101  ARG A CA  1 
ATOM   733  C  C   . ARG A 1 112 ? 89.651  100.009 104.674 1.00 25.75 ? 101  ARG A C   1 
ATOM   734  O  O   . ARG A 1 112 ? 89.962  100.574 105.724 1.00 25.75 ? 101  ARG A O   1 
ATOM   735  C  CB  . ARG A 1 112 ? 87.325  100.890 105.050 1.00 25.75 ? 101  ARG A CB  1 
ATOM   736  C  CG  . ARG A 1 112 ? 85.919  101.211 104.536 1.00 25.75 ? 101  ARG A CG  1 
ATOM   737  C  CD  . ARG A 1 112 ? 85.877  101.672 103.084 1.00 25.75 ? 101  ARG A CD  1 
ATOM   738  N  NE  . ARG A 1 112 ? 86.351  103.041 102.910 1.00 25.75 ? 101  ARG A NE  1 
ATOM   739  C  CZ  . ARG A 1 112 ? 86.369  103.678 101.743 1.00 25.75 ? 101  ARG A CZ  1 
ATOM   740  N  NH1 . ARG A 1 112 ? 86.816  104.924 101.670 1.00 25.75 ? 101  ARG A NH1 1 
ATOM   741  N  NH2 . ARG A 1 112 ? 85.940  103.071 100.645 1.00 25.75 ? 101  ARG A NH2 1 
ATOM   742  N  N   . VAL A 1 113 ? 90.512  99.283  103.969 1.00 23.02 ? 102  VAL A N   1 
ATOM   743  C  CA  . VAL A 1 113 ? 91.896  99.066  104.371 1.00 23.02 ? 102  VAL A CA  1 
ATOM   744  C  C   . VAL A 1 113 ? 92.787  99.511  103.219 1.00 23.02 ? 102  VAL A C   1 
ATOM   745  O  O   . VAL A 1 113 ? 92.501  99.175  102.069 1.00 23.02 ? 102  VAL A O   1 
ATOM   746  C  CB  . VAL A 1 113 ? 92.180  97.596  104.728 1.00 23.02 ? 102  VAL A CB  1 
ATOM   747  C  CG1 . VAL A 1 113 ? 93.648  97.390  105.009 1.00 23.02 ? 102  VAL A CG1 1 
ATOM   748  C  CG2 . VAL A 1 113 ? 91.360  97.175  105.923 1.00 23.02 ? 102  VAL A CG2 1 
ATOM   749  N  N   . PRO A 1 114 ? 93.858  100.265 103.465 1.00 22.74 ? 103  PRO A N   1 
ATOM   750  C  CA  . PRO A 1 114 ? 94.743  100.657 102.363 1.00 22.74 ? 103  PRO A CA  1 
ATOM   751  C  C   . PRO A 1 114 ? 95.424  99.453  101.732 1.00 22.74 ? 103  PRO A C   1 
ATOM   752  O  O   . PRO A 1 114 ? 95.642  98.427  102.375 1.00 22.74 ? 103  PRO A O   1 
ATOM   753  C  CB  . PRO A 1 114 ? 95.761  101.582 103.036 1.00 22.74 ? 103  PRO A CB  1 
ATOM   754  C  CG  . PRO A 1 114 ? 95.114  102.043 104.269 1.00 22.74 ? 103  PRO A CG  1 
ATOM   755  C  CD  . PRO A 1 114 ? 94.214  100.948 104.718 1.00 22.74 ? 103  PRO A CD  1 
ATOM   756  N  N   . LEU A 1 115 ? 95.759  99.587  100.452 1.00 21.24 ? 104  LEU A N   1 
ATOM   757  C  CA  . LEU A 1 115 ? 96.468  98.550  99.709  1.00 21.24 ? 104  LEU A CA  1 
ATOM   758  C  C   . LEU A 1 115 ? 97.604  99.201  98.935  1.00 21.24 ? 104  LEU A C   1 
ATOM   759  O  O   . LEU A 1 115 ? 97.361  99.922  97.965  1.00 21.24 ? 104  LEU A O   1 
ATOM   760  C  CB  . LEU A 1 115 ? 95.530  97.801  98.764  1.00 21.24 ? 104  LEU A CB  1 
ATOM   761  C  CG  . LEU A 1 115 ? 96.150  96.630  98.001  1.00 21.24 ? 104  LEU A CG  1 
ATOM   762  C  CD1 . LEU A 1 115 ? 95.134  95.545  97.789  1.00 21.24 ? 104  LEU A CD1 1 
ATOM   763  C  CD2 . LEU A 1 115 ? 96.699  97.074  96.669  1.00 21.24 ? 104  LEU A CD2 1 
ATOM   764  N  N   . LEU A 1 116 ? 98.836  98.942  99.356  1.00 24.22 ? 105  LEU A N   1 
ATOM   765  C  CA  . LEU A 1 116 ? 100.016 99.420  98.653  1.00 24.22 ? 105  LEU A CA  1 
ATOM   766  C  C   . LEU A 1 116 ? 100.472 98.392  97.634  1.00 24.22 ? 105  LEU A C   1 
ATOM   767  O  O   . LEU A 1 116 ? 100.488 97.193  97.915  1.00 24.22 ? 105  LEU A O   1 
ATOM   768  C  CB  . LEU A 1 116 ? 101.156 99.687  99.629  1.00 24.22 ? 105  LEU A CB  1 
ATOM   769  C  CG  . LEU A 1 116 ? 101.242 101.073 100.242 1.00 24.22 ? 105  LEU A CG  1 
ATOM   770  C  CD1 . LEU A 1 116 ? 102.117 101.016 101.473 1.00 24.22 ? 105  LEU A CD1 1 
ATOM   771  C  CD2 . LEU A 1 116 ? 101.796 102.038 99.221  1.00 24.22 ? 105  LEU A CD2 1 
ATOM   772  N  N   . THR A 1 117 ? 100.858 98.860  96.453  1.00 23.14 ? 106  THR A N   1 
ATOM   773  C  CA  . THR A 1 117 ? 101.432 97.935  95.489  1.00 23.14 ? 106  THR A CA  1 
ATOM   774  C  C   . THR A 1 117 ? 102.315 98.692  94.513  1.00 23.14 ? 106  THR A C   1 
ATOM   775  O  O   . THR A 1 117 ? 102.051 99.849  94.187  1.00 23.14 ? 106  THR A O   1 
ATOM   776  C  CB  . THR A 1 117 ? 100.341 97.165  94.740  1.00 23.14 ? 106  THR A CB  1 
ATOM   777  O  OG1 . THR A 1 117 ? 100.946 96.291  93.785  1.00 23.14 ? 106  THR A OG1 1 
ATOM   778  C  CG2 . THR A 1 117 ? 99.399  98.107  94.029  1.00 23.14 ? 106  THR A CG2 1 
ATOM   779  N  N   . ALA A 1 118 ? 103.383 98.031  94.072  1.00 24.14 ? 107  ALA A N   1 
ATOM   780  C  CA  . ALA A 1 118 ? 104.199 98.507  92.964  1.00 24.14 ? 107  ALA A CA  1 
ATOM   781  C  C   . ALA A 1 118 ? 103.984 97.677  91.707  1.00 24.14 ? 107  ALA A C   1 
ATOM   782  O  O   . ALA A 1 118 ? 104.710 97.856  90.726  1.00 24.14 ? 107  ALA A O   1 
ATOM   783  C  CB  . ALA A 1 118 ? 105.678 98.508  93.346  1.00 24.14 ? 107  ALA A CB  1 
ATOM   784  N  N   . GLY A 1 119 ? 103.015 96.768  91.721  1.00 23.01 ? 108  GLY A N   1 
ATOM   785  C  CA  . GLY A 1 119 ? 102.611 96.054  90.530  1.00 23.01 ? 108  GLY A CA  1 
ATOM   786  C  C   . GLY A 1 119 ? 101.226 96.477  90.093  1.00 23.01 ? 108  GLY A C   1 
ATOM   787  O  O   . GLY A 1 119 ? 100.843 97.634  90.281  1.00 23.01 ? 108  GLY A O   1 
ATOM   788  N  N   . ALA A 1 120 ? 100.463 95.555  89.518  1.00 22.92 ? 109  ALA A N   1 
ATOM   789  C  CA  . ALA A 1 120 ? 99.103  95.821  89.066  1.00 22.92 ? 109  ALA A CA  1 
ATOM   790  C  C   . ALA A 1 120 ? 99.020  97.119  88.259  1.00 22.92 ? 109  ALA A C   1 
ATOM   791  O  O   . ALA A 1 120 ? 98.320  98.056  88.655  1.00 22.92 ? 109  ALA A O   1 
ATOM   792  C  CB  . ALA A 1 120 ? 98.148  95.866  90.250  1.00 22.92 ? 109  ALA A CB  1 
ATOM   793  N  N   . PRO A 1 121 ? 99.721  97.209  87.127  1.00 24.84 ? 110  PRO A N   1 
ATOM   794  C  CA  . PRO A 1 121 ? 99.719  98.454  86.352  1.00 24.84 ? 110  PRO A CA  1 
ATOM   795  C  C   . PRO A 1 121 ? 98.525  98.623  85.430  1.00 24.84 ? 110  PRO A C   1 
ATOM   796  O  O   . PRO A 1 121 ? 98.422  99.665  84.774  1.00 24.84 ? 110  PRO A O   1 
ATOM   797  C  CB  . PRO A 1 121 ? 101.016 98.348  85.533  1.00 24.84 ? 110  PRO A CB  1 
ATOM   798  C  CG  . PRO A 1 121 ? 101.718 97.123  86.019  1.00 24.84 ? 110  PRO A CG  1 
ATOM   799  C  CD  . PRO A 1 121 ? 100.660 96.241  86.547  1.00 24.84 ? 110  PRO A CD  1 
ATOM   800  N  N   . ALA A 1 122 ? 97.626  97.647  85.352  1.00 25.46 ? 111  ALA A N   1 
ATOM   801  C  CA  . ALA A 1 122 ? 96.561  97.685  84.364  1.00 25.46 ? 111  ALA A CA  1 
ATOM   802  C  C   . ALA A 1 122 ? 95.755  98.974  84.480  1.00 25.46 ? 111  ALA A C   1 
ATOM   803  O  O   . ALA A 1 122 ? 95.801  99.682  85.486  1.00 25.46 ? 111  ALA A O   1 
ATOM   804  C  CB  . ALA A 1 122 ? 95.641  96.478  84.527  1.00 25.46 ? 111  ALA A CB  1 
ATOM   805  N  N   . LEU A 1 123 ? 95.011  99.277  83.416  1.00 30.49 ? 112  LEU A N   1 
ATOM   806  C  CA  . LEU A 1 123 ? 94.221  100.503 83.383  1.00 30.49 ? 112  LEU A CA  1 
ATOM   807  C  C   . LEU A 1 123 ? 93.028  100.427 84.328  1.00 30.49 ? 112  LEU A C   1 
ATOM   808  O  O   . LEU A 1 123 ? 92.661  101.428 84.953  1.00 30.49 ? 112  LEU A O   1 
ATOM   809  C  CB  . LEU A 1 123 ? 93.750  100.773 81.956  1.00 30.49 ? 112  LEU A CB  1 
ATOM   810  C  CG  . LEU A 1 123 ? 93.083  102.121 81.697  1.00 30.49 ? 112  LEU A CG  1 
ATOM   811  C  CD1 . LEU A 1 123 ? 94.103  103.241 81.703  1.00 30.49 ? 112  LEU A CD1 1 
ATOM   812  C  CD2 . LEU A 1 123 ? 92.340  102.081 80.386  1.00 30.49 ? 112  LEU A CD2 1 
ATOM   813  N  N   . GLY A 1 124 ? 92.407  99.252  84.443  1.00 26.05 ? 113  GLY A N   1 
ATOM   814  C  CA  . GLY A 1 124 ? 91.192  99.128  85.227  1.00 26.05 ? 113  GLY A CA  1 
ATOM   815  C  C   . GLY A 1 124 ? 91.390  99.299  86.717  1.00 26.05 ? 113  GLY A C   1 
ATOM   816  O  O   . GLY A 1 124 ? 90.414  99.521  87.439  1.00 26.05 ? 113  GLY A O   1 
ATOM   817  N  N   . PHE A 1 125 ? 92.627  99.199  87.196  1.00 24.43 ? 114  PHE A N   1 
ATOM   818  C  CA  . PHE A 1 125 ? 92.908  99.317  88.620  1.00 24.43 ? 114  PHE A CA  1 
ATOM   819  C  C   . PHE A 1 125 ? 92.966  100.761 89.094  1.00 24.43 ? 114  PHE A C   1 
ATOM   820  O  O   . PHE A 1 125 ? 93.039  100.996 90.303  1.00 24.43 ? 114  PHE A O   1 
ATOM   821  C  CB  . PHE A 1 125 ? 94.229  98.615  88.938  1.00 24.43 ? 114  PHE A CB  1 
ATOM   822  C  CG  . PHE A 1 125 ? 94.391  98.242  90.381  1.00 24.43 ? 114  PHE A CG  1 
ATOM   823  C  CD1 . PHE A 1 125 ? 93.833  97.082  90.873  1.00 24.43 ? 114  PHE A CD1 1 
ATOM   824  C  CD2 . PHE A 1 125 ? 95.116  99.044  91.241  1.00 24.43 ? 114  PHE A CD2 1 
ATOM   825  C  CE1 . PHE A 1 125 ? 93.982  96.736  92.195  1.00 24.43 ? 114  PHE A CE1 1 
ATOM   826  C  CE2 . PHE A 1 125 ? 95.268  98.699  92.564  1.00 24.43 ? 114  PHE A CE2 1 
ATOM   827  C  CZ  . PHE A 1 125 ? 94.700  97.544  93.040  1.00 24.43 ? 114  PHE A CZ  1 
ATOM   828  N  N   . GLY A 1 126 ? 92.934  101.728 88.183  1.00 27.58 ? 115  GLY A N   1 
ATOM   829  C  CA  . GLY A 1 126 ? 93.038  103.130 88.522  1.00 27.58 ? 115  GLY A CA  1 
ATOM   830  C  C   . GLY A 1 126 ? 91.725  103.867 88.660  1.00 27.58 ? 115  GLY A C   1 
ATOM   831  O  O   . GLY A 1 126 ? 91.738  105.098 88.773  1.00 27.58 ? 115  GLY A O   1 
ATOM   832  N  N   . VAL A 1 127 ? 90.592  103.167 88.644  1.00 28.34 ? 116  VAL A N   1 
ATOM   833  C  CA  . VAL A 1 127 ? 89.285  103.794 88.846  1.00 28.34 ? 116  VAL A CA  1 
ATOM   834  C  C   . VAL A 1 127 ? 89.033  103.772 90.351  1.00 28.34 ? 116  VAL A C   1 
ATOM   835  O  O   . VAL A 1 127 ? 88.397  102.868 90.888  1.00 28.34 ? 116  VAL A O   1 
ATOM   836  C  CB  . VAL A 1 127 ? 88.181  103.097 88.053  1.00 28.34 ? 116  VAL A CB  1 
ATOM   837  C  CG1 . VAL A 1 127 ? 86.833  103.702 88.388  1.00 28.34 ? 116  VAL A CG1 1 
ATOM   838  C  CG2 . VAL A 1 127 ? 88.440  103.167 86.555  1.00 28.34 ? 116  VAL A CG2 1 
ATOM   839  N  N   . LYS A 1 128 ? 89.537  104.795 91.040  1.00 28.68 ? 117  LYS A N   1 
ATOM   840  C  CA  . LYS A 1 128 ? 89.502  104.824 92.497  1.00 28.68 ? 117  LYS A CA  1 
ATOM   841  C  C   . LYS A 1 128 ? 88.095  104.947 93.062  1.00 28.68 ? 117  LYS A C   1 
ATOM   842  O  O   . LYS A 1 128 ? 87.950  105.010 94.288  1.00 28.68 ? 117  LYS A O   1 
ATOM   843  C  CB  . LYS A 1 128 ? 90.368  105.972 93.015  1.00 28.68 ? 117  LYS A CB  1 
ATOM   844  C  CG  . LYS A 1 128 ? 91.806  105.919 92.534  1.00 28.68 ? 117  LYS A CG  1 
ATOM   845  C  CD  . LYS A 1 128 ? 92.546  104.723 93.103  1.00 28.68 ? 117  LYS A CD  1 
ATOM   846  C  CE  . LYS A 1 128 ? 94.036  104.807 92.817  1.00 28.68 ? 117  LYS A CE  1 
ATOM   847  N  NZ  . LYS A 1 128 ? 94.583  103.534 92.281  1.00 28.68 ? 117  LYS A NZ  1 
ATOM   848  N  N   . ASP A 1 129 ? 87.061  105.003 92.222  1.00 28.73 ? 118  ASP A N   1 
ATOM   849  C  CA  . ASP A 1 129 ? 85.701  104.897 92.738  1.00 28.73 ? 118  ASP A CA  1 
ATOM   850  C  C   . ASP A 1 129 ? 85.408  103.478 93.207  1.00 28.73 ? 118  ASP A C   1 
ATOM   851  O  O   . ASP A 1 129 ? 84.771  103.280 94.248  1.00 28.73 ? 118  ASP A O   1 
ATOM   852  C  CB  . ASP A 1 129 ? 84.700  105.327 91.668  1.00 28.73 ? 118  ASP A CB  1 
ATOM   853  N  N   . GLU A 1 130 ? 85.872  102.480 92.456  1.00 29.59 ? 119  GLU A N   1 
ATOM   854  C  CA  . GLU A 1 130 ? 85.692  101.078 92.811  1.00 29.59 ? 119  GLU A CA  1 
ATOM   855  C  C   . GLU A 1 130 ? 86.826  100.555 93.683  1.00 29.59 ? 119  GLU A C   1 
ATOM   856  O  O   . GLU A 1 130 ? 86.583  99.769  94.605  1.00 29.59 ? 119  GLU A O   1 
ATOM   857  C  CB  . GLU A 1 130 ? 85.587  100.232 91.540  1.00 29.59 ? 119  GLU A CB  1 
ATOM   858  C  CG  . GLU A 1 130 ? 85.525  98.736  91.784  1.00 29.59 ? 119  GLU A CG  1 
ATOM   859  C  CD  . GLU A 1 130 ? 85.326  97.952  90.504  1.00 29.59 ? 119  GLU A CD  1 
ATOM   860  O  OE1 . GLU A 1 130 ? 84.976  96.755  90.584  1.00 29.59 ? 119  GLU A OE1 1 
ATOM   861  O  OE2 . GLU A 1 130 ? 85.524  98.533  89.417  1.00 29.59 ? 119  GLU A OE2 1 
ATOM   862  N  N   . TYR A 1 131 ? 88.063  100.965 93.399  1.00 25.22 ? 120  TYR A N   1 
ATOM   863  C  CA  . TYR A 1 131 ? 89.232  100.545 94.167  1.00 25.22 ? 120  TYR A CA  1 
ATOM   864  C  C   . TYR A 1 131 ? 89.599  101.666 95.135  1.00 25.22 ? 120  TYR A C   1 
ATOM   865  O  O   . TYR A 1 131 ? 90.567  102.399 94.948  1.00 25.22 ? 120  TYR A O   1 
ATOM   866  C  CB  . TYR A 1 131 ? 90.386  100.207 93.233  1.00 25.22 ? 120  TYR A CB  1 
ATOM   867  C  CG  . TYR A 1 131 ? 90.119  99.023  92.339  1.00 25.22 ? 120  TYR A CG  1 
ATOM   868  C  CD1 . TYR A 1 131 ? 90.177  97.732  92.831  1.00 25.22 ? 120  TYR A CD1 1 
ATOM   869  C  CD2 . TYR A 1 131 ? 89.810  99.196  91.005  1.00 25.22 ? 120  TYR A CD2 1 
ATOM   870  C  CE1 . TYR A 1 131 ? 89.933  96.652  92.021  1.00 25.22 ? 120  TYR A CE1 1 
ATOM   871  C  CE2 . TYR A 1 131 ? 89.564  98.120  90.190  1.00 25.22 ? 120  TYR A CE2 1 
ATOM   872  C  CZ  . TYR A 1 131 ? 89.628  96.851  90.703  1.00 25.22 ? 120  TYR A CZ  1 
ATOM   873  O  OH  . TYR A 1 131 ? 89.385  95.775  89.888  1.00 25.22 ? 120  TYR A OH  1 
ATOM   874  N  N   . ALA A 1 132 ? 88.807  101.790 96.191  1.00 25.54 ? 121  ALA A N   1 
ATOM   875  C  CA  . ALA A 1 132 ? 89.033  102.846 97.163  1.00 25.54 ? 121  ALA A CA  1 
ATOM   876  C  C   . ALA A 1 132 ? 90.237  102.526 98.039  1.00 25.54 ? 121  ALA A C   1 
ATOM   877  O  O   . ALA A 1 132 ? 90.423  101.387 98.473  1.00 25.54 ? 121  ALA A O   1 
ATOM   878  C  CB  . ALA A 1 132 ? 87.791  103.038 98.029  1.00 25.54 ? 121  ALA A CB  1 
ATOM   879  N  N   . LEU A 1 133 ? 91.059  103.541 98.293  1.00 26.09 ? 122  LEU A N   1 
ATOM   880  C  CA  . LEU A 1 133 ? 92.185  103.510 99.226  1.00 26.09 ? 122  LEU A CA  1 
ATOM   881  C  C   . LEU A 1 133 ? 93.420  102.802 98.685  1.00 26.09 ? 122  LEU A C   1 
ATOM   882  O  O   . LEU A 1 133 ? 94.368  102.600 99.450  1.00 26.09 ? 122  LEU A O   1 
ATOM   883  C  CB  . LEU A 1 133 ? 91.808  102.847 100.554 1.00 26.09 ? 122  LEU A CB  1 
ATOM   884  C  CG  . LEU A 1 133 ? 90.679  103.497 101.349 1.00 26.09 ? 122  LEU A CG  1 
ATOM   885  C  CD1 . LEU A 1 133 ? 90.242  102.602 102.480 1.00 26.09 ? 122  LEU A CD1 1 
ATOM   886  C  CD2 . LEU A 1 133 ? 91.118  104.836 101.889 1.00 26.09 ? 122  LEU A CD2 1 
ATOM   887  N  N   . THR A 1 134 ? 93.460  102.428 97.411  1.00 24.15 ? 123  THR A N   1 
ATOM   888  C  CA  . THR A 1 134 ? 94.611  101.726 96.859  1.00 24.15 ? 123  THR A CA  1 
ATOM   889  C  C   . THR A 1 134 ? 95.638  102.721 96.337  1.00 24.15 ? 123  THR A C   1 
ATOM   890  O  O   . THR A 1 134 ? 95.287  103.707 95.688  1.00 24.15 ? 123  THR A O   1 
ATOM   891  C  CB  . THR A 1 134 ? 94.193  100.783 95.732  1.00 24.15 ? 123  THR A CB  1 
ATOM   892  O  OG1 . THR A 1 134 ? 93.761  101.548 94.605  1.00 24.15 ? 123  THR A OG1 1 
ATOM   893  C  CG2 . THR A 1 134 ? 93.070  99.871  96.181  1.00 24.15 ? 123  THR A CG2 1 
ATOM   894  N  N   . THR A 1 135 ? 96.909  102.453 96.626  1.00 26.39 ? 124  THR A N   1 
ATOM   895  C  CA  . THR A 1 135 ? 98.018  103.287 96.187  1.00 26.39 ? 124  THR A CA  1 
ATOM   896  C  C   . THR A 1 135 ? 98.978  102.447 95.361  1.00 26.39 ? 124  THR A C   1 
ATOM   897  O  O   . THR A 1 135 ? 99.373  101.350 95.779  1.00 26.39 ? 124  THR A O   1 
ATOM   898  C  CB  . THR A 1 135 ? 98.755  103.903 97.376  1.00 26.39 ? 124  THR A CB  1 
ATOM   899  O  OG1 . THR A 1 135 ? 97.808  104.454 98.296  1.00 26.39 ? 124  THR A OG1 1 
ATOM   900  C  CG2 . THR A 1 135 ? 99.701  104.994 96.915  1.00 26.39 ? 124  THR A CG2 1 
ATOM   901  N  N   . ARG A 1 136 ? 99.345  102.961 94.193  1.00 25.52 ? 125  ARG A N   1 
ATOM   902  C  CA  . ARG A 1 136 ? 100.325 102.333 93.318  1.00 25.52 ? 125  ARG A CA  1 
ATOM   903  C  C   . ARG A 1 136 ? 101.613 103.135 93.410  1.00 25.52 ? 125  ARG A C   1 
ATOM   904  O  O   . ARG A 1 136 ? 101.694 104.251 92.892  1.00 25.52 ? 125  ARG A O   1 
ATOM   905  C  CB  . ARG A 1 136 ? 99.819  102.270 91.882  1.00 25.52 ? 125  ARG A CB  1 
ATOM   906  C  CG  . ARG A 1 136 ? 98.685  101.296 91.683  1.00 25.52 ? 125  ARG A CG  1 
ATOM   907  C  CD  . ARG A 1 136 ? 98.500  100.958 90.223  1.00 25.52 ? 125  ARG A CD  1 
ATOM   908  N  NE  . ARG A 1 136 ? 97.631  101.915 89.550  1.00 25.52 ? 125  ARG A NE  1 
ATOM   909  C  CZ  . ARG A 1 136 ? 97.133  101.741 88.334  1.00 25.52 ? 125  ARG A CZ  1 
ATOM   910  N  NH1 . ARG A 1 136 ? 97.414  100.645 87.653  1.00 25.52 ? 125  ARG A NH1 1 
ATOM   911  N  NH2 . ARG A 1 136 ? 96.352  102.663 87.797  1.00 25.52 ? 125  ARG A NH2 1 
ATOM   912  N  N   . ALA A 1 137 ? 102.613 102.570 94.074  1.00 26.67 ? 126  ALA A N   1 
ATOM   913  C  CA  . ALA A 1 137 ? 103.905 103.217 94.231  1.00 26.67 ? 126  ALA A CA  1 
ATOM   914  C  C   . ALA A 1 137 ? 104.876 102.861 93.119  1.00 26.67 ? 126  ALA A C   1 
ATOM   915  O  O   . ALA A 1 137 ? 106.033 103.283 93.173  1.00 26.67 ? 126  ALA A O   1 
ATOM   916  C  CB  . ALA A 1 137 ? 104.517 102.847 95.581  1.00 26.67 ? 126  ALA A CB  1 
ATOM   917  N  N   . GLY A 1 138 ? 104.439 102.102 92.121  1.00 27.73 ? 127  GLY A N   1 
ATOM   918  C  CA  . GLY A 1 138 ? 105.293 101.712 91.029  1.00 27.73 ? 127  GLY A CA  1 
ATOM   919  C  C   . GLY A 1 138 ? 104.758 102.181 89.697  1.00 27.73 ? 127  GLY A C   1 
ATOM   920  O  O   . GLY A 1 138 ? 103.765 102.907 89.621  1.00 27.73 ? 127  GLY A O   1 
ATOM   921  N  N   . PRO A 1 139 ? 105.405 101.764 88.614  1.00 28.91 ? 128  PRO A N   1 
ATOM   922  C  CA  . PRO A 1 139 ? 104.991 102.226 87.288  1.00 28.91 ? 128  PRO A CA  1 
ATOM   923  C  C   . PRO A 1 139 ? 103.579 101.783 86.941  1.00 28.91 ? 128  PRO A C   1 
ATOM   924  O  O   . PRO A 1 139 ? 103.077 100.774 87.439  1.00 28.91 ? 128  PRO A O   1 
ATOM   925  C  CB  . PRO A 1 139 ? 106.023 101.585 86.357  1.00 28.91 ? 128  PRO A CB  1 
ATOM   926  C  CG  . PRO A 1 139 ? 107.202 101.334 87.229  1.00 28.91 ? 128  PRO A CG  1 
ATOM   927  C  CD  . PRO A 1 139 ? 106.629 100.952 88.547  1.00 28.91 ? 128  PRO A CD  1 
ATOM   928  N  N   . SER A 1 140 ? 102.934 102.568 86.082  1.00 29.43 ? 129  SER A N   1 
ATOM   929  C  CA  . SER A 1 140 ? 101.607 102.265 85.572  1.00 29.43 ? 129  SER A CA  1 
ATOM   930  C  C   . SER A 1 140 ? 101.639 102.340 84.055  1.00 29.43 ? 129  SER A C   1 
ATOM   931  O  O   . SER A 1 140 ? 102.477 103.032 83.474  1.00 29.43 ? 129  SER A O   1 
ATOM   932  C  CB  . SER A 1 140 ? 100.560 103.237 86.114  1.00 29.43 ? 129  SER A CB  1 
ATOM   933  O  OG  . SER A 1 140 ? 100.682 103.382 87.516  1.00 29.43 ? 129  SER A OG  1 
ATOM   934  N  N   . TYR A 1 141 ? 100.729 101.608 83.413  1.00 28.45 ? 130  TYR A N   1 
ATOM   935  C  CA  . TYR A 1 141 ? 100.703 101.590 81.955  1.00 28.45 ? 130  TYR A CA  1 
ATOM   936  C  C   . TYR A 1 141 ? 100.078 102.851 81.381  1.00 28.45 ? 130  TYR A C   1 
ATOM   937  O  O   . TYR A 1 141 ? 100.468 103.288 80.295  1.00 28.45 ? 130  TYR A O   1 
ATOM   938  C  CB  . TYR A 1 141 ? 99.946  100.362 81.452  1.00 28.45 ? 130  TYR A CB  1 
ATOM   939  C  CG  . TYR A 1 141 ? 100.645 99.052  81.727  1.00 28.45 ? 130  TYR A CG  1 
ATOM   940  C  CD1 . TYR A 1 141 ? 102.026 98.953  81.685  1.00 28.45 ? 130  TYR A CD1 1 
ATOM   941  C  CD2 . TYR A 1 141 ? 99.921  97.912  82.024  1.00 28.45 ? 130  TYR A CD2 1 
ATOM   942  C  CE1 . TYR A 1 141 ? 102.659 97.763  81.938  1.00 28.45 ? 130  TYR A CE1 1 
ATOM   943  C  CE2 . TYR A 1 141 ? 100.549 96.717  82.277  1.00 28.45 ? 130  TYR A CE2 1 
ATOM   944  C  CZ  . TYR A 1 141 ? 101.916 96.648  82.232  1.00 28.45 ? 130  TYR A CZ  1 
ATOM   945  O  OH  . TYR A 1 141 ? 102.545 95.455  82.479  1.00 28.45 ? 130  TYR A OH  1 
ATOM   946  N  N   . ALA A 1 142 ? 99.121  103.449 82.089  1.00 32.21 ? 131  ALA A N   1 
ATOM   947  C  CA  . ALA A 1 142 ? 98.495  104.666 81.591  1.00 32.21 ? 131  ALA A CA  1 
ATOM   948  C  C   . ALA A 1 142 ? 99.486  105.818 81.521  1.00 32.21 ? 131  ALA A C   1 
ATOM   949  O  O   . ALA A 1 142 ? 99.408  106.639 80.604  1.00 32.21 ? 131  ALA A O   1 
ATOM   950  C  CB  . ALA A 1 142 ? 97.308  105.041 82.471  1.00 32.21 ? 131  ALA A CB  1 
ATOM   951  N  N   . LYS A 1 143 ? 100.421 105.902 82.468  1.00 32.38 ? 132  LYS A N   1 
ATOM   952  C  CA  . LYS A 1 143 ? 101.410 106.971 82.435  1.00 32.38 ? 132  LYS A CA  1 
ATOM   953  C  C   . LYS A 1 143 ? 102.289 106.901 81.198  1.00 32.38 ? 132  LYS A C   1 
ATOM   954  O  O   . LYS A 1 143 ? 102.806 107.934 80.765  1.00 32.38 ? 132  LYS A O   1 
ATOM   955  C  CB  . LYS A 1 143 ? 102.285 106.918 83.686  1.00 32.38 ? 132  LYS A CB  1 
ATOM   956  C  CG  . LYS A 1 143 ? 101.507 107.020 84.980  1.00 32.38 ? 132  LYS A CG  1 
ATOM   957  C  CD  . LYS A 1 143 ? 101.015 108.425 85.225  1.00 32.38 ? 132  LYS A CD  1 
ATOM   958  C  CE  . LYS A 1 143 ? 100.682 108.637 86.679  1.00 32.38 ? 132  LYS A CE  1 
ATOM   959  N  NZ  . LYS A 1 143 ? 99.646  109.677 86.866  1.00 32.38 ? 132  LYS A NZ  1 
ATOM   960  N  N   . LEU A 1 144 ? 102.439 105.722 80.598  1.00 34.88 ? 133  LEU A N   1 
ATOM   961  C  CA  . LEU A 1 144 ? 103.168 105.629 79.341  1.00 34.88 ? 133  LEU A CA  1 
ATOM   962  C  C   . LEU A 1 144 ? 102.459 106.424 78.256  1.00 34.88 ? 133  LEU A C   1 
ATOM   963  O  O   . LEU A 1 144 ? 103.106 107.049 77.409  1.00 34.88 ? 133  LEU A O   1 
ATOM   964  C  CB  . LEU A 1 144 ? 103.312 104.162 78.941  1.00 34.88 ? 133  LEU A CB  1 
ATOM   965  C  CG  . LEU A 1 144 ? 103.912 103.827 77.578  1.00 34.88 ? 133  LEU A CG  1 
ATOM   966  C  CD1 . LEU A 1 144 ? 105.182 104.609 77.315  1.00 34.88 ? 133  LEU A CD1 1 
ATOM   967  C  CD2 . LEU A 1 144 ? 104.169 102.338 77.499  1.00 34.88 ? 133  LEU A CD2 1 
ATOM   968  N  N   . GLY A 1 145 ? 101.126 106.439 78.289  1.00 37.43 ? 134  GLY A N   1 
ATOM   969  C  CA  . GLY A 1 145 ? 100.381 107.275 77.368  1.00 37.43 ? 134  GLY A CA  1 
ATOM   970  C  C   . GLY A 1 145 ? 100.726 108.743 77.494  1.00 37.43 ? 134  GLY A C   1 
ATOM   971  O  O   . GLY A 1 145 ? 100.631 109.489 76.519  1.00 37.43 ? 134  GLY A O   1 
ATOM   972  N  N   . ASP A 1 146 ? 101.127 109.184 78.687  1.00 38.95 ? 135  ASP A N   1 
ATOM   973  C  CA  . ASP A 1 146 ? 101.624 110.548 78.821  1.00 38.95 ? 135  ASP A CA  1 
ATOM   974  C  C   . ASP A 1 146 ? 102.889 110.739 77.997  1.00 38.95 ? 135  ASP A C   1 
ATOM   975  O  O   . ASP A 1 146 ? 103.015 111.709 77.240  1.00 38.95 ? 135  ASP A O   1 
ATOM   976  C  CB  . ASP A 1 146 ? 101.893 110.872 80.290  1.00 38.95 ? 135  ASP A CB  1 
ATOM   977  C  CG  . ASP A 1 146 ? 100.646 110.810 81.138  1.00 38.95 ? 135  ASP A CG  1 
ATOM   978  O  OD1 . ASP A 1 146 ? 99.635  110.257 80.664  1.00 38.95 ? 135  ASP A OD1 1 
ATOM   979  O  OD2 . ASP A 1 146 ? 100.675 111.309 82.281  1.00 38.95 ? 135  ASP A OD2 1 
ATOM   980  N  N   . PHE A 1 147 ? 103.824 109.794 78.104  1.00 38.26 ? 136  PHE A N   1 
ATOM   981  C  CA  . PHE A 1 147 ? 105.125 109.949 77.466  1.00 38.26 ? 136  PHE A CA  1 
ATOM   982  C  C   . PHE A 1 147 ? 104.973 110.182 75.970  1.00 38.26 ? 136  PHE A C   1 
ATOM   983  O  O   . PHE A 1 147 ? 105.488 111.166 75.427  1.00 38.26 ? 136  PHE A O   1 
ATOM   984  C  CB  . PHE A 1 147 ? 105.976 108.710 77.746  1.00 38.26 ? 136  PHE A CB  1 
ATOM   985  C  CG  . PHE A 1 147 ? 107.302 108.701 77.044  1.00 38.26 ? 136  PHE A CG  1 
ATOM   986  C  CD1 . PHE A 1 147 ? 108.166 109.771 77.151  1.00 38.26 ? 136  PHE A CD1 1 
ATOM   987  C  CD2 . PHE A 1 147 ? 107.693 107.611 76.297  1.00 38.26 ? 136  PHE A CD2 1 
ATOM   988  C  CE1 . PHE A 1 147 ? 109.384 109.755 76.516  1.00 38.26 ? 136  PHE A CE1 1 
ATOM   989  C  CE2 . PHE A 1 147 ? 108.908 107.597 75.662  1.00 38.26 ? 136  PHE A CE2 1 
ATOM   990  C  CZ  . PHE A 1 147 ? 109.753 108.669 75.772  1.00 38.26 ? 136  PHE A CZ  1 
ATOM   991  N  N   . VAL A 1 148 ? 104.228 109.307 75.292  1.00 41.53 ? 137  VAL A N   1 
ATOM   992  C  CA  . VAL A 1 148 ? 104.050 109.455 73.851  1.00 41.53 ? 137  VAL A CA  1 
ATOM   993  C  C   . VAL A 1 148 ? 103.377 110.783 73.539  1.00 41.53 ? 137  VAL A C   1 
ATOM   994  O  O   . VAL A 1 148 ? 103.688 111.432 72.533  1.00 41.53 ? 137  VAL A O   1 
ATOM   995  C  CB  . VAL A 1 148 ? 103.257 108.267 73.276  1.00 41.53 ? 137  VAL A CB  1 
ATOM   996  C  CG1 . VAL A 1 148 ? 103.929 106.957 73.635  1.00 41.53 ? 137  VAL A CG1 1 
ATOM   997  C  CG2 . VAL A 1 148 ? 101.831 108.286 73.773  1.00 41.53 ? 137  VAL A CG2 1 
ATOM   998  N  N   . ALA A 1 149 ? 102.453 111.218 74.398  1.00 42.86 ? 138  ALA A N   1 
ATOM   999  C  CA  . ALA A 1 149 ? 101.820 112.513 74.183  1.00 42.86 ? 138  ALA A CA  1 
ATOM   1000 C  C   . ALA A 1 149 ? 102.853 113.630 74.212  1.00 42.86 ? 138  ALA A C   1 
ATOM   1001 O  O   . ALA A 1 149 ? 102.800 114.555 73.396  1.00 42.86 ? 138  ALA A O   1 
ATOM   1002 C  CB  . ALA A 1 149 ? 100.737 112.751 75.233  1.00 42.86 ? 138  ALA A CB  1 
ATOM   1003 N  N   . ALA A 1 150 ? 103.807 113.559 75.141  1.00 44.35 ? 139  ALA A N   1 
ATOM   1004 C  CA  . ALA A 1 150 ? 104.877 114.547 75.169  1.00 44.35 ? 139  ALA A CA  1 
ATOM   1005 C  C   . ALA A 1 150 ? 105.851 114.360 74.019  1.00 44.35 ? 139  ALA A C   1 
ATOM   1006 O  O   . ALA A 1 150 ? 106.603 115.286 73.703  1.00 44.35 ? 139  ALA A O   1 
ATOM   1007 C  CB  . ALA A 1 150 ? 105.626 114.477 76.497  1.00 44.35 ? 139  ALA A CB  1 
ATOM   1008 N  N   . LEU A 1 151 ? 105.853 113.186 73.389  1.00 45.82 ? 140  LEU A N   1 
ATOM   1009 C  CA  . LEU A 1 151 ? 106.755 112.933 72.273  1.00 45.82 ? 140  LEU A CA  1 
ATOM   1010 C  C   . LEU A 1 151 ? 106.182 113.488 70.976  1.00 45.82 ? 140  LEU A C   1 
ATOM   1011 O  O   . LEU A 1 151 ? 106.854 114.241 70.263  1.00 45.82 ? 140  LEU A O   1 
ATOM   1012 C  CB  . LEU A 1 151 ? 107.015 111.430 72.157  1.00 45.82 ? 140  LEU A CB  1 
ATOM   1013 C  CG  . LEU A 1 151 ? 108.141 110.956 71.241  1.00 45.82 ? 140  LEU A CG  1 
ATOM   1014 C  CD1 . LEU A 1 151 ? 109.481 111.500 71.685  1.00 45.82 ? 140  LEU A CD1 1 
ATOM   1015 C  CD2 . LEU A 1 151 ? 108.165 109.444 71.218  1.00 45.82 ? 140  LEU A CD2 1 
ATOM   1016 N  N   . HIS A 1 152 ? 104.931 113.141 70.666  1.00 49.08 ? 141  HIS A N   1 
ATOM   1017 C  CA  . HIS A 1 152 ? 104.286 113.660 69.466  1.00 49.08 ? 141  HIS A CA  1 
ATOM   1018 C  C   . HIS A 1 152 ? 104.385 115.178 69.409  1.00 49.08 ? 141  HIS A C   1 
ATOM   1019 O  O   . HIS A 1 152 ? 104.830 115.748 68.406  1.00 49.08 ? 141  HIS A O   1 
ATOM   1020 C  CB  . HIS A 1 152 ? 102.823 113.223 69.439  1.00 49.08 ? 141  HIS A CB  1 
ATOM   1021 C  CG  . HIS A 1 152 ? 102.622 111.792 69.052  1.00 49.08 ? 141  HIS A CG  1 
ATOM   1022 N  ND1 . HIS A 1 152 ? 102.589 111.375 67.741  1.00 49.08 ? 141  HIS A ND1 1 
ATOM   1023 C  CD2 . HIS A 1 152 ? 102.438 110.683 69.804  1.00 49.08 ? 141  HIS A CD2 1 
ATOM   1024 C  CE1 . HIS A 1 152 ? 102.393 110.070 67.700  1.00 49.08 ? 141  HIS A CE1 1 
ATOM   1025 N  NE2 . HIS A 1 152 ? 102.299 109.625 68.939  1.00 49.08 ? 141  HIS A NE2 1 
ATOM   1026 N  N   . ARG A 1 153 ? 103.998 115.848 70.496  1.00 49.29 ? 142  ARG A N   1 
ATOM   1027 C  CA  . ARG A 1 153 ? 104.077 117.303 70.537  1.00 49.29 ? 142  ARG A CA  1 
ATOM   1028 C  C   . ARG A 1 153 ? 105.463 117.784 70.142  1.00 49.29 ? 142  ARG A C   1 
ATOM   1029 O  O   . ARG A 1 153 ? 105.604 118.748 69.381  1.00 49.29 ? 142  ARG A O   1 
ATOM   1030 C  CB  . ARG A 1 153 ? 103.724 117.806 71.937  1.00 49.29 ? 142  ARG A CB  1 
ATOM   1031 C  CG  . ARG A 1 153 ? 102.252 117.671 72.294  1.00 49.29 ? 142  ARG A CG  1 
ATOM   1032 C  CD  . ARG A 1 153 ? 101.841 118.634 73.399  1.00 49.29 ? 142  ARG A CD  1 
ATOM   1033 N  NE  . ARG A 1 153 ? 101.737 117.975 74.699  1.00 49.29 ? 142  ARG A NE  1 
ATOM   1034 C  CZ  . ARG A 1 153 ? 102.704 117.938 75.613  1.00 49.29 ? 142  ARG A CZ  1 
ATOM   1035 N  NH1 . ARG A 1 153 ? 103.875 118.518 75.389  1.00 49.29 ? 142  ARG A NH1 1 
ATOM   1036 N  NH2 . ARG A 1 153 ? 102.498 117.310 76.763  1.00 49.29 ? 142  ARG A NH2 1 
ATOM   1037 N  N   . ARG A 1 154 ? 106.503 117.119 70.643  1.00 50.15 ? 143  ARG A N   1 
ATOM   1038 C  CA  . ARG A 1 154 ? 107.861 117.547 70.335  1.00 50.15 ? 143  ARG A CA  1 
ATOM   1039 C  C   . ARG A 1 154 ? 108.173 117.374 68.856  1.00 50.15 ? 143  ARG A C   1 
ATOM   1040 O  O   . ARG A 1 154 ? 108.833 118.227 68.253  1.00 50.15 ? 143  ARG A O   1 
ATOM   1041 C  CB  . ARG A 1 154 ? 108.859 116.765 71.184  1.00 50.15 ? 143  ARG A CB  1 
ATOM   1042 C  CG  . ARG A 1 154 ? 110.303 117.105 70.895  1.00 50.15 ? 143  ARG A CG  1 
ATOM   1043 C  CD  . ARG A 1 154 ? 111.149 117.033 72.151  1.00 50.15 ? 143  ARG A CD  1 
ATOM   1044 N  NE  . ARG A 1 154 ? 112.549 116.762 71.843  1.00 50.15 ? 143  ARG A NE  1 
ATOM   1045 C  CZ  . ARG A 1 154 ? 113.581 117.227 72.540  1.00 50.15 ? 143  ARG A CZ  1 
ATOM   1046 N  NH1 . ARG A 1 154 ? 113.389 117.993 73.604  1.00 50.15 ? 143  ARG A NH1 1 
ATOM   1047 N  NH2 . ARG A 1 154 ? 114.815 116.920 72.170  1.00 50.15 ? 143  ARG A NH2 1 
ATOM   1048 N  N   . LEU A 1 155 ? 107.709 116.281 68.253  1.00 53.61 ? 144  LEU A N   1 
ATOM   1049 C  CA  . LEU A 1 155 ? 108.113 115.912 66.904  1.00 53.61 ? 144  LEU A CA  1 
ATOM   1050 C  C   . LEU A 1 155 ? 107.083 116.279 65.844  1.00 53.61 ? 144  LEU A C   1 
ATOM   1051 O  O   . LEU A 1 155 ? 107.311 116.009 64.662  1.00 53.61 ? 144  LEU A O   1 
ATOM   1052 C  CB  . LEU A 1 155 ? 108.407 114.411 66.846  1.00 53.61 ? 144  LEU A CB  1 
ATOM   1053 C  CG  . LEU A 1 155 ? 109.448 113.932 67.859  1.00 53.61 ? 144  LEU A CG  1 
ATOM   1054 C  CD1 . LEU A 1 155 ? 109.399 112.425 68.021  1.00 53.61 ? 144  LEU A CD1 1 
ATOM   1055 C  CD2 . LEU A 1 155 ? 110.838 114.381 67.446  1.00 53.61 ? 144  LEU A CD2 1 
ATOM   1056 N  N   . GLY A 1 156 ? 105.965 116.884 66.228  1.00 55.27 ? 145  GLY A N   1 
ATOM   1057 C  CA  . GLY A 1 156 ? 105.006 117.387 65.270  1.00 55.27 ? 145  GLY A CA  1 
ATOM   1058 C  C   . GLY A 1 156 ? 104.025 116.371 64.730  1.00 55.27 ? 145  GLY A C   1 
ATOM   1059 O  O   . GLY A 1 156 ? 103.161 116.743 63.927  1.00 55.27 ? 145  GLY A O   1 
ATOM   1060 N  N   . TRP A 1 157 ? 104.116 115.108 65.136  1.00 56.38 ? 146  TRP A N   1 
ATOM   1061 C  CA  . TRP A 1 157 ? 103.161 114.103 64.682  1.00 56.38 ? 146  TRP A CA  1 
ATOM   1062 C  C   . TRP A 1 157 ? 101.830 114.335 65.380  1.00 56.38 ? 146  TRP A C   1 
ATOM   1063 O  O   . TRP A 1 157 ? 101.728 114.189 66.601  1.00 56.38 ? 146  TRP A O   1 
ATOM   1064 C  CB  . TRP A 1 157 ? 103.679 112.699 64.969  1.00 56.38 ? 146  TRP A CB  1 
ATOM   1065 C  CG  . TRP A 1 157 ? 105.011 112.407 64.385  1.00 56.38 ? 146  TRP A CG  1 
ATOM   1066 C  CD1 . TRP A 1 157 ? 105.493 112.832 63.186  1.00 56.38 ? 146  TRP A CD1 1 
ATOM   1067 C  CD2 . TRP A 1 157 ? 106.036 111.602 64.969  1.00 56.38 ? 146  TRP A CD2 1 
ATOM   1068 N  NE1 . TRP A 1 157 ? 106.762 112.350 62.990  1.00 56.38 ? 146  TRP A NE1 1 
ATOM   1069 C  CE2 . TRP A 1 157 ? 107.118 111.590 64.071  1.00 56.38 ? 146  TRP A CE2 1 
ATOM   1070 C  CE3 . TRP A 1 157 ? 106.145 110.894 66.167  1.00 56.38 ? 146  TRP A CE3 1 
ATOM   1071 C  CZ2 . TRP A 1 157 ? 108.293 110.897 64.333  1.00 56.38 ? 146  TRP A CZ2 1 
ATOM   1072 C  CZ3 . TRP A 1 157 ? 107.309 110.209 66.425  1.00 56.38 ? 146  TRP A CZ3 1 
ATOM   1073 C  CH2 . TRP A 1 157 ? 108.369 110.214 65.513  1.00 56.38 ? 146  TRP A CH2 1 
ATOM   1074 N  N   . GLU A 1 158 ? 100.804 114.698 64.611  1.00 61.71 ? 147  GLU A N   1 
ATOM   1075 C  CA  . GLU A 1 158 ? 99.507  115.009 65.199  1.00 61.71 ? 147  GLU A CA  1 
ATOM   1076 C  C   . GLU A 1 158 ? 98.343  114.505 64.355  1.00 61.71 ? 147  GLU A C   1 
ATOM   1077 O  O   . GLU A 1 158 ? 97.241  115.056 64.450  1.00 61.71 ? 147  GLU A O   1 
ATOM   1078 C  CB  . GLU A 1 158 ? 99.388  116.519 65.416  1.00 61.71 ? 147  GLU A CB  1 
ATOM   1079 C  CG  . GLU A 1 158 ? 99.377  117.333 64.139  1.00 61.71 ? 147  GLU A CG  1 
ATOM   1080 C  CD  . GLU A 1 158 ? 99.327  118.820 64.409  1.00 61.71 ? 147  GLU A CD  1 
ATOM   1081 O  OE1 . GLU A 1 158 ? 99.325  119.205 65.597  1.00 61.71 ? 147  GLU A OE1 1 
ATOM   1082 O  OE2 . GLU A 1 158 ? 99.292  119.604 63.438  1.00 61.71 ? 147  GLU A OE2 1 
ATOM   1083 N  N   . ARG A 1 159 ? 98.549  113.469 63.541  1.00 62.05 ? 148  ARG A N   1 
ATOM   1084 C  CA  . ARG A 1 159 ? 97.524  112.978 62.630  1.00 62.05 ? 148  ARG A CA  1 
ATOM   1085 C  C   . ARG A 1 159 ? 97.066  111.563 62.962  1.00 62.05 ? 148  ARG A C   1 
ATOM   1086 O  O   . ARG A 1 159 ? 95.873  111.345 63.182  1.00 62.05 ? 148  ARG A O   1 
ATOM   1087 C  CB  . ARG A 1 159 ? 98.043  113.040 61.187  1.00 62.05 ? 148  ARG A CB  1 
ATOM   1088 C  CG  . ARG A 1 159 ? 98.554  114.409 60.769  1.00 62.05 ? 148  ARG A CG  1 
ATOM   1089 C  CD  . ARG A 1 159 ? 97.467  115.460 60.881  1.00 62.05 ? 148  ARG A CD  1 
ATOM   1090 N  NE  . ARG A 1 159 ? 96.226  115.032 60.243  1.00 62.05 ? 148  ARG A NE  1 
ATOM   1091 C  CZ  . ARG A 1 159 ? 95.965  115.174 58.948  1.00 62.05 ? 148  ARG A CZ  1 
ATOM   1092 N  NH1 . ARG A 1 159 ? 96.861  115.734 58.148  1.00 62.05 ? 148  ARG A NH1 1 
ATOM   1093 N  NH2 . ARG A 1 159 ? 94.809  114.756 58.453  1.00 62.05 ? 148  ARG A NH2 1 
ATOM   1094 N  N   . GLN A 1 160 ? 97.976  110.589 63.008  1.00 58.33 ? 149  GLN A N   1 
ATOM   1095 C  CA  . GLN A 1 160 ? 97.566  109.195 63.104  1.00 58.33 ? 149  GLN A CA  1 
ATOM   1096 C  C   . GLN A 1 160 ? 98.653  108.356 63.761  1.00 58.33 ? 149  GLN A C   1 
ATOM   1097 O  O   . GLN A 1 160 ? 99.831  108.719 63.765  1.00 58.33 ? 149  GLN A O   1 
ATOM   1098 C  CB  . GLN A 1 160 ? 97.228  108.636 61.719  1.00 58.33 ? 149  GLN A CB  1 
ATOM   1099 C  CG  . GLN A 1 160 ? 96.713  107.215 61.723  1.00 58.33 ? 149  GLN A CG  1 
ATOM   1100 C  CD  . GLN A 1 160 ? 96.334  106.747 60.343  1.00 58.33 ? 149  GLN A CD  1 
ATOM   1101 O  OE1 . GLN A 1 160 ? 96.490  107.479 59.368  1.00 58.33 ? 149  GLN A OE1 1 
ATOM   1102 N  NE2 . GLN A 1 160 ? 95.837  105.521 60.247  1.00 58.33 ? 149  GLN A NE2 1 
ATOM   1103 N  N   . ALA A 1 161 ? 98.236  107.216 64.313  1.00 52.78 ? 150  ALA A N   1 
ATOM   1104 C  CA  . ALA A 1 161 ? 99.172  106.297 64.951  1.00 52.78 ? 150  ALA A CA  1 
ATOM   1105 C  C   . ALA A 1 161 ? 98.613  104.877 64.939  1.00 52.78 ? 150  ALA A C   1 
ATOM   1106 O  O   . ALA A 1 161 ? 97.398  104.665 64.890  1.00 52.78 ? 150  ALA A O   1 
ATOM   1107 C  CB  . ALA A 1 161 ? 99.485  106.734 66.385  1.00 52.78 ? 150  ALA A CB  1 
ATOM   1108 N  N   . LEU A 1 162 ? 99.522  103.906 64.999  1.00 49.76 ? 151  LEU A N   1 
ATOM   1109 C  CA  . LEU A 1 162 ? 99.177  102.491 64.966  1.00 49.76 ? 151  LEU A CA  1 
ATOM   1110 C  C   . LEU A 1 162 ? 99.880  101.778 66.111  1.00 49.76 ? 151  LEU A C   1 
ATOM   1111 O  O   . LEU A 1 162 ? 101.054 102.043 66.382  1.00 49.76 ? 151  LEU A O   1 
ATOM   1112 C  CB  . LEU A 1 162 ? 99.574  101.873 63.619  1.00 49.76 ? 151  LEU A CB  1 
ATOM   1113 C  CG  . LEU A 1 162 ? 99.273  100.393 63.386  1.00 49.76 ? 151  LEU A CG  1 
ATOM   1114 C  CD1 . LEU A 1 162 ? 97.830  100.205 62.969  1.00 49.76 ? 151  LEU A CD1 1 
ATOM   1115 C  CD2 . LEU A 1 162 ? 100.201 99.834  62.328  1.00 49.76 ? 151  LEU A CD2 1 
ATOM   1116 N  N   . MET A 1 163 ? 99.166  100.876 66.786  1.00 45.11 ? 152  MET A N   1 
ATOM   1117 C  CA  . MET A 1 163 ? 99.703  100.144 67.930  1.00 45.11 ? 152  MET A CA  1 
ATOM   1118 C  C   . MET A 1 163 ? 99.471  98.649  67.764  1.00 45.11 ? 152  MET A C   1 
ATOM   1119 O  O   . MET A 1 163 ? 98.330  98.181  67.801  1.00 45.11 ? 152  MET A O   1 
ATOM   1120 C  CB  . MET A 1 163 ? 99.097  100.646 69.239  1.00 45.11 ? 152  MET A CB  1 
ATOM   1121 C  CG  . MET A 1 163 ? 99.667  101.974 69.669  1.00 45.11 ? 152  MET A CG  1 
ATOM   1122 S  SD  . MET A 1 163 ? 98.674  102.922 70.821  1.00 45.11 ? 152  MET A SD  1 
ATOM   1123 C  CE  . MET A 1 163 ? 99.296  104.558 70.451  1.00 45.11 ? 152  MET A CE  1 
ATOM   1124 N  N   . LEU A 1 164 ? 100.564 97.912  67.613  1.00 46.36 ? 153  LEU A N   1 
ATOM   1125 C  CA  . LEU A 1 164 ? 100.564 96.464  67.497  1.00 46.36 ? 153  LEU A CA  1 
ATOM   1126 C  C   . LEU A 1 164 ? 100.931 95.845  68.836  1.00 46.36 ? 153  LEU A C   1 
ATOM   1127 O  O   . LEU A 1 164 ? 101.845 96.319  69.516  1.00 46.36 ? 153  LEU A O   1 
ATOM   1128 C  CB  . LEU A 1 164 ? 101.581 96.019  66.450  1.00 46.36 ? 153  LEU A CB  1 
ATOM   1129 C  CG  . LEU A 1 164 ? 101.227 96.160  64.977  1.00 46.36 ? 153  LEU A CG  1 
ATOM   1130 C  CD1 . LEU A 1 164 ? 101.228 97.603  64.575  1.00 46.36 ? 153  LEU A CD1 1 
ATOM   1131 C  CD2 . LEU A 1 164 ? 102.249 95.415  64.163  1.00 46.36 ? 153  LEU A CD2 1 
ATOM   1132 N  N   . TYR A 1 165 ? 100.238 94.774  69.206  1.00 42.42 ? 154  TYR A N   1 
ATOM   1133 C  CA  . TYR A 1 165 ? 100.651 93.988  70.358  1.00 42.42 ? 154  TYR A CA  1 
ATOM   1134 C  C   . TYR A 1 165 ? 100.621 92.504  70.029  1.00 42.42 ? 154  TYR A C   1 
ATOM   1135 O  O   . TYR A 1 165 ? 99.768  92.033  69.268  1.00 42.42 ? 154  TYR A O   1 
ATOM   1136 C  CB  . TYR A 1 165 ? 99.791  94.285  71.591  1.00 42.42 ? 154  TYR A CB  1 
ATOM   1137 C  CG  . TYR A 1 165 ? 98.305  94.111  71.433  1.00 42.42 ? 154  TYR A CG  1 
ATOM   1138 C  CD1 . TYR A 1 165 ? 97.702  92.892  71.685  1.00 42.42 ? 154  TYR A CD1 1 
ATOM   1139 C  CD2 . TYR A 1 165 ? 97.500  95.175  71.070  1.00 42.42 ? 154  TYR A CD2 1 
ATOM   1140 C  CE1 . TYR A 1 165 ? 96.344  92.734  71.561  1.00 42.42 ? 154  TYR A CE1 1 
ATOM   1141 C  CE2 . TYR A 1 165 ? 96.141  95.025  70.942  1.00 42.42 ? 154  TYR A CE2 1 
ATOM   1142 C  CZ  . TYR A 1 165 ? 95.568  93.804  71.191  1.00 42.42 ? 154  TYR A CZ  1 
ATOM   1143 O  OH  . TYR A 1 165 ? 94.211  93.647  71.065  1.00 42.42 ? 154  TYR A OH  1 
ATOM   1144 N  N   . ALA A 1 166 ? 101.577 91.779  70.598  1.00 45.71 ? 155  ALA A N   1 
ATOM   1145 C  CA  . ALA A 1 166 ? 101.713 90.352  70.379  1.00 45.71 ? 155  ALA A CA  1 
ATOM   1146 C  C   . ALA A 1 166 ? 100.953 89.568  71.439  1.00 45.71 ? 155  ALA A C   1 
ATOM   1147 O  O   . ALA A 1 166 ? 100.725 90.044  72.553  1.00 45.71 ? 155  ALA A O   1 
ATOM   1148 C  CB  . ALA A 1 166 ? 103.184 89.950  70.399  1.00 45.71 ? 155  ALA A CB  1 
ATOM   1149 N  N   . TYR A 1 167 ? 100.559 88.354  71.073  1.00 50.84 ? 156  TYR A N   1 
ATOM   1150 C  CA  . TYR A 1 167 ? 99.866  87.442  71.968  1.00 50.84 ? 156  TYR A CA  1 
ATOM   1151 C  C   . TYR A 1 167 ? 100.682 86.166  72.109  1.00 50.84 ? 156  TYR A C   1 
ATOM   1152 O  O   . TYR A 1 167 ? 101.189 85.632  71.119  1.00 50.84 ? 156  TYR A O   1 
ATOM   1153 C  CB  . TYR A 1 167 ? 98.467  87.111  71.452  1.00 50.84 ? 156  TYR A CB  1 
ATOM   1154 C  CG  . TYR A 1 167 ? 97.905  85.841  72.036  1.00 50.84 ? 156  TYR A CG  1 
ATOM   1155 C  CD1 . TYR A 1 167 ? 97.420  85.810  73.334  1.00 50.84 ? 156  TYR A CD1 1 
ATOM   1156 C  CD2 . TYR A 1 167 ? 97.870  84.670  71.296  1.00 50.84 ? 156  TYR A CD2 1 
ATOM   1157 C  CE1 . TYR A 1 167 ? 96.909  84.651  73.877  1.00 50.84 ? 156  TYR A CE1 1 
ATOM   1158 C  CE2 . TYR A 1 167 ? 97.363  83.505  71.831  1.00 50.84 ? 156  TYR A CE2 1 
ATOM   1159 C  CZ  . TYR A 1 167 ? 96.884  83.500  73.122  1.00 50.84 ? 156  TYR A CZ  1 
ATOM   1160 O  OH  . TYR A 1 167 ? 96.377  82.339  73.659  1.00 50.84 ? 156  TYR A OH  1 
ATOM   1161 N  N   . ARG A 1 168 ? 100.811 85.682  73.345  1.00 51.11 ? 157  ARG A N   1 
ATOM   1162 C  CA  . ARG A 1 168 ? 101.607 84.503  73.633  1.00 51.11 ? 157  ARG A CA  1 
ATOM   1163 C  C   . ARG A 1 168 ? 100.921 83.715  74.745  1.00 51.11 ? 157  ARG A C   1 
ATOM   1164 O  O   . ARG A 1 168 ? 100.487 84.314  75.744  1.00 51.11 ? 157  ARG A O   1 
ATOM   1165 C  CB  . ARG A 1 168 ? 103.025 84.896  74.046  1.00 51.11 ? 157  ARG A CB  1 
ATOM   1166 C  CG  . ARG A 1 168 ? 104.044 83.792  73.885  1.00 51.11 ? 157  ARG A CG  1 
ATOM   1167 C  CD  . ARG A 1 168 ? 105.447 84.352  73.735  1.00 51.11 ? 157  ARG A CD  1 
ATOM   1168 N  NE  . ARG A 1 168 ? 105.736 85.392  74.720  1.00 51.11 ? 157  ARG A NE  1 
ATOM   1169 C  CZ  . ARG A 1 168 ? 106.954 85.702  75.153  1.00 51.11 ? 157  ARG A CZ  1 
ATOM   1170 N  NH1 . ARG A 1 168 ? 108.018 85.056  74.694  1.00 51.11 ? 157  ARG A NH1 1 
ATOM   1171 N  NH2 . ARG A 1 168 ? 107.109 86.665  76.049  1.00 51.11 ? 157  ARG A NH2 1 
ATOM   1172 N  N   . PRO A 1 169 ? 100.799 82.391  74.616  1.00 52.63 ? 158  PRO A N   1 
ATOM   1173 C  CA  . PRO A 1 169 ? 100.080 81.625  75.648  1.00 52.63 ? 158  PRO A CA  1 
ATOM   1174 C  C   . PRO A 1 169 ? 100.653 81.780  77.046  1.00 52.63 ? 158  PRO A C   1 
ATOM   1175 O  O   . PRO A 1 169 ? 99.893  81.755  78.022  1.00 52.63 ? 158  PRO A O   1 
ATOM   1176 C  CB  . PRO A 1 169 ? 100.198 80.172  75.167  1.00 52.63 ? 158  PRO A CB  1 
ATOM   1177 C  CG  . PRO A 1 169 ? 100.632 80.220  73.759  1.00 52.63 ? 158  PRO A CG  1 
ATOM   1178 C  CD  . PRO A 1 169 ? 101.067 81.598  73.405  1.00 52.63 ? 158  PRO A CD  1 
ATOM   1179 N  N   . GLY A 1 170 ? 101.966 81.932  77.178  1.00 49.74 ? 159  GLY A N   1 
ATOM   1180 C  CA  . GLY A 1 170 ? 102.598 81.919  78.482  1.00 49.74 ? 159  GLY A CA  1 
ATOM   1181 C  C   . GLY A 1 170 ? 102.376 83.167  79.307  1.00 49.74 ? 159  GLY A C   1 
ATOM   1182 O  O   . GLY A 1 170 ? 101.853 83.093  80.422  1.00 49.74 ? 159  GLY A O   1 
ATOM   1183 N  N   . ASP A 1 171 ? 102.770 84.320  78.772  1.00 45.51 ? 160  ASP A N   1 
ATOM   1184 C  CA  . ASP A 1 171 ? 102.677 85.561  79.526  1.00 45.51 ? 160  ASP A CA  1 
ATOM   1185 C  C   . ASP A 1 171 ? 101.236 85.817  79.944  1.00 45.51 ? 160  ASP A C   1 
ATOM   1186 O  O   . ASP A 1 171 ? 100.288 85.436  79.255  1.00 45.51 ? 160  ASP A O   1 
ATOM   1187 C  CB  . ASP A 1 171 ? 103.203 86.733  78.696  1.00 45.51 ? 160  ASP A CB  1 
ATOM   1188 C  CG  . ASP A 1 171 ? 102.390 86.978  77.437  1.00 45.51 ? 160  ASP A CG  1 
ATOM   1189 O  OD1 . ASP A 1 171 ? 101.475 86.183  77.145  1.00 45.51 ? 160  ASP A OD1 1 
ATOM   1190 O  OD2 . ASP A 1 171 ? 102.671 87.971  76.734  1.00 45.51 ? 160  ASP A OD2 1 
ATOM   1191 N  N   . GLU A 1 172 ? 101.036 86.520  81.061  1.00 38.06 ? 161  GLU A N   1 
ATOM   1192 C  CA  . GLU A 1 172 ? 99.674  86.830  81.577  1.00 38.06 ? 161  GLU A CA  1 
ATOM   1193 C  C   . GLU A 1 172 ? 99.124  88.050  80.826  1.00 38.06 ? 161  GLU A C   1 
ATOM   1194 O  O   . GLU A 1 172 ? 98.931  89.088  81.495  1.00 38.06 ? 161  GLU A O   1 
ATOM   1195 C  CB  . GLU A 1 172 ? 99.719  87.057  83.089  1.00 38.06 ? 161  GLU A CB  1 
ATOM   1196 N  N   . GLU A 1 173 ? 98.802  87.875  79.531  1.00 35.12 ? 162  GLU A N   1 
ATOM   1197 C  CA  . GLU A 1 173 ? 98.321  88.913  78.573  1.00 35.12 ? 162  GLU A CA  1 
ATOM   1198 C  C   . GLU A 1 173 ? 98.957  90.259  78.932  1.00 35.12 ? 162  GLU A C   1 
ATOM   1199 O  O   . GLU A 1 173 ? 98.209  91.174  79.330  1.00 35.12 ? 162  GLU A O   1 
ATOM   1200 C  CB  . GLU A 1 173 ? 96.792  88.981  78.589  1.00 35.12 ? 162  GLU A CB  1 
ATOM   1201 C  CG  . GLU A 1 173 ? 96.126  87.696  78.129  1.00 35.12 ? 162  GLU A CG  1 
ATOM   1202 C  CD  . GLU A 1 173 ? 94.620  87.790  77.955  1.00 35.12 ? 162  GLU A CD  1 
ATOM   1203 O  OE1 . GLU A 1 173 ? 94.061  88.873  78.221  1.00 35.12 ? 162  GLU A OE1 1 
ATOM   1204 O  OE2 . GLU A 1 173 ? 94.009  86.780  77.553  1.00 35.12 ? 162  GLU A OE2 1 
ATOM   1205 N  N   . HIS A 1 174 ? 100.281 90.377  78.783  1.00 34.40 ? 163  HIS A N   1 
ATOM   1206 C  CA  . HIS A 1 174 ? 101.015 91.570  79.197  1.00 34.40 ? 163  HIS A CA  1 
ATOM   1207 C  C   . HIS A 1 174 ? 100.864 92.709  78.195  1.00 34.40 ? 163  HIS A C   1 
ATOM   1208 O  O   . HIS A 1 174 ? 100.446 93.816  78.558  1.00 34.40 ? 163  HIS A O   1 
ATOM   1209 C  CB  . HIS A 1 174 ? 102.491 91.210  79.380  1.00 34.40 ? 163  HIS A CB  1 
ATOM   1210 C  CG  . HIS A 1 174 ? 103.382 92.382  79.647  1.00 34.40 ? 163  HIS A CG  1 
ATOM   1211 N  ND1 . HIS A 1 174 ? 104.371 92.777  78.773  1.00 34.40 ? 163  HIS A ND1 1 
ATOM   1212 C  CD2 . HIS A 1 174 ? 103.453 93.228  80.700  1.00 34.40 ? 163  HIS A CD2 1 
ATOM   1213 C  CE1 . HIS A 1 174 ? 105.003 93.825  79.269  1.00 34.40 ? 163  HIS A CE1 1 
ATOM   1214 N  NE2 . HIS A 1 174 ? 104.466 94.118  80.438  1.00 34.40 ? 163  HIS A NE2 1 
ATOM   1215 N  N   . CYS A 1 175 ? 101.213 92.463  76.932  1.00 37.42 ? 164  CYS A N   1 
ATOM   1216 C  CA  . CYS A 1 175 ? 101.140 93.531  75.945  1.00 37.42 ? 164  CYS A CA  1 
ATOM   1217 C  C   . CYS A 1 175 ? 99.715  93.988  75.697  1.00 37.42 ? 164  CYS A C   1 
ATOM   1218 O  O   . CYS A 1 175 ? 99.504  95.147  75.333  1.00 37.42 ? 164  CYS A O   1 
ATOM   1219 C  CB  . CYS A 1 175 ? 101.793 93.106  74.635  1.00 37.42 ? 164  CYS A CB  1 
ATOM   1220 S  SG  . CYS A 1 175 ? 103.585 93.132  74.689  1.00 37.42 ? 164  CYS A SG  1 
ATOM   1221 N  N   . PHE A 1 176 ? 98.721  93.126  75.896  1.00 34.21 ? 165  PHE A N   1 
ATOM   1222 C  CA  . PHE A 1 176 ? 97.352  93.605  75.764  1.00 34.21 ? 165  PHE A CA  1 
ATOM   1223 C  C   . PHE A 1 176 ? 97.084  94.731  76.749  1.00 34.21 ? 165  PHE A C   1 
ATOM   1224 O  O   . PHE A 1 176 ? 96.591  95.795  76.368  1.00 34.21 ? 165  PHE A O   1 
ATOM   1225 C  CB  . PHE A 1 176 ? 96.344  92.485  75.980  1.00 34.21 ? 165  PHE A CB  1 
ATOM   1226 C  CG  . PHE A 1 176 ? 94.948  92.990  76.190  1.00 34.21 ? 165  PHE A CG  1 
ATOM   1227 C  CD1 . PHE A 1 176 ? 94.287  93.655  75.177  1.00 34.21 ? 165  PHE A CD1 1 
ATOM   1228 C  CD2 . PHE A 1 176 ? 94.310  92.833  77.402  1.00 34.21 ? 165  PHE A CD2 1 
ATOM   1229 C  CE1 . PHE A 1 176 ? 93.014  94.135  75.362  1.00 34.21 ? 165  PHE A CE1 1 
ATOM   1230 C  CE2 . PHE A 1 176 ? 93.034  93.311  77.591  1.00 34.21 ? 165  PHE A CE2 1 
ATOM   1231 C  CZ  . PHE A 1 176 ? 92.386  93.964  76.570  1.00 34.21 ? 165  PHE A CZ  1 
ATOM   1232 N  N   . PHE A 1 177 ? 97.413  94.519  78.024  1.00 30.03 ? 166  PHE A N   1 
ATOM   1233 C  CA  . PHE A 1 177 ? 97.168  95.552  79.024  1.00 30.03 ? 166  PHE A CA  1 
ATOM   1234 C  C   . PHE A 1 177 ? 98.044  96.772  78.783  1.00 30.03 ? 166  PHE A C   1 
ATOM   1235 O  O   . PHE A 1 177 ? 97.585  97.914  78.927  1.00 30.03 ? 166  PHE A O   1 
ATOM   1236 C  CB  . PHE A 1 177 ? 97.401  94.991  80.424  1.00 30.03 ? 166  PHE A CB  1 
ATOM   1237 C  CG  . PHE A 1 177 ? 96.396  93.959  80.836  1.00 30.03 ? 166  PHE A CG  1 
ATOM   1238 C  CD1 . PHE A 1 177 ? 95.046  94.240  80.821  1.00 30.03 ? 166  PHE A CD1 1 
ATOM   1239 C  CD2 . PHE A 1 177 ? 96.802  92.706  81.235  1.00 30.03 ? 166  PHE A CD2 1 
ATOM   1240 C  CE1 . PHE A 1 177 ? 94.127  93.290  81.197  1.00 30.03 ? 166  PHE A CE1 1 
ATOM   1241 C  CE2 . PHE A 1 177 ? 95.887  91.755  81.610  1.00 30.03 ? 166  PHE A CE2 1 
ATOM   1242 C  CZ  . PHE A 1 177 ? 94.550  92.047  81.592  1.00 30.03 ? 166  PHE A CZ  1 
ATOM   1243 N  N   . LEU A 1 178 ? 99.307  96.557  78.416  1.00 32.81 ? 167  LEU A N   1 
ATOM   1244 C  CA  . LEU A 1 178 ? 100.192 97.686  78.157  1.00 32.81 ? 167  LEU A CA  1 
ATOM   1245 C  C   . LEU A 1 178 ? 99.630  98.575  77.055  1.00 32.81 ? 167  LEU A C   1 
ATOM   1246 O  O   . LEU A 1 178 ? 99.496  99.796  77.225  1.00 32.81 ? 167  LEU A O   1 
ATOM   1247 C  CB  . LEU A 1 178 ? 101.582 97.175  77.785  1.00 32.81 ? 167  LEU A CB  1 
ATOM   1248 C  CG  . LEU A 1 178 ? 102.748 98.147  77.947  1.00 32.81 ? 167  LEU A CG  1 
ATOM   1249 C  CD1 . LEU A 1 178 ? 104.053 97.392  77.947  1.00 32.81 ? 167  LEU A CD1 1 
ATOM   1250 C  CD2 . LEU A 1 178 ? 102.748 99.189  76.856  1.00 32.81 ? 167  LEU A CD2 1 
ATOM   1251 N  N   . VAL A 1 179 ? 99.280  97.977  75.915  1.00 37.95 ? 168  VAL A N   1 
ATOM   1252 C  CA  . VAL A 1 179 ? 98.790  98.767  74.797  1.00 37.95 ? 168  VAL A CA  1 
ATOM   1253 C  C   . VAL A 1 179 ? 97.397  99.304  75.081  1.00 37.95 ? 168  VAL A C   1 
ATOM   1254 O  O   . VAL A 1 179 ? 97.030  100.358 74.567  1.00 37.95 ? 168  VAL A O   1 
ATOM   1255 C  CB  . VAL A 1 179 ? 98.829  97.944  73.500  1.00 37.95 ? 168  VAL A CB  1 
ATOM   1256 C  CG1 . VAL A 1 179 ? 98.142  98.696  72.381  1.00 37.95 ? 168  VAL A CG1 1 
ATOM   1257 C  CG2 . VAL A 1 179 ? 100.265 97.639  73.126  1.00 37.95 ? 168  VAL A CG2 1 
ATOM   1258 N  N   . GLU A 1 180 ? 96.604  98.623  75.909  1.00 36.86 ? 169  GLU A N   1 
ATOM   1259 C  CA  . GLU A 1 180 ? 95.306  99.171  76.286  1.00 36.86 ? 169  GLU A CA  1 
ATOM   1260 C  C   . GLU A 1 180 ? 95.472  100.473 77.057  1.00 36.86 ? 169  GLU A C   1 
ATOM   1261 O  O   . GLU A 1 180 ? 94.826  101.482 76.747  1.00 36.86 ? 169  GLU A O   1 
ATOM   1262 C  CB  . GLU A 1 180 ? 94.532  98.154  77.121  1.00 36.86 ? 169  GLU A CB  1 
ATOM   1263 C  CG  . GLU A 1 180 ? 93.073  98.508  77.326  1.00 36.86 ? 169  GLU A CG  1 
ATOM   1264 C  CD  . GLU A 1 180 ? 92.460  97.816  78.527  1.00 36.86 ? 169  GLU A CD  1 
ATOM   1265 O  OE1 . GLU A 1 180 ? 93.212  97.298  79.377  1.00 36.86 ? 169  GLU A OE1 1 
ATOM   1266 O  OE2 . GLU A 1 180 ? 91.216  97.788  78.621  1.00 36.86 ? 169  GLU A OE2 1 
ATOM   1267 N  N   . GLY A 1 181 ? 96.336  100.468 78.071  1.00 33.72 ? 170  GLY A N   1 
ATOM   1268 C  CA  . GLY A 1 181 ? 96.575  101.693 78.815  1.00 33.72 ? 170  GLY A CA  1 
ATOM   1269 C  C   . GLY A 1 181 ? 97.126  102.795 77.932  1.00 33.72 ? 170  GLY A C   1 
ATOM   1270 O  O   . GLY A 1 181 ? 96.656  103.938 77.969  1.00 33.72 ? 170  GLY A O   1 
ATOM   1271 N  N   . LEU A 1 182 ? 98.127  102.463 77.114  1.00 38.28 ? 171  LEU A N   1 
ATOM   1272 C  CA  . LEU A 1 182 ? 98.716  103.462 76.229  1.00 38.28 ? 171  LEU A CA  1 
ATOM   1273 C  C   . LEU A 1 182 ? 97.667  104.037 75.283  1.00 38.28 ? 171  LEU A C   1 
ATOM   1274 O  O   . LEU A 1 182 ? 97.570  105.257 75.108  1.00 38.28 ? 171  LEU A O   1 
ATOM   1275 C  CB  . LEU A 1 182 ? 99.871  102.831 75.452  1.00 38.28 ? 171  LEU A CB  1 
ATOM   1276 C  CG  . LEU A 1 182 ? 100.345 103.509 74.169  1.00 38.28 ? 171  LEU A CG  1 
ATOM   1277 C  CD1 . LEU A 1 182 ? 100.847 104.901 74.451  1.00 38.28 ? 171  LEU A CD1 1 
ATOM   1278 C  CD2 . LEU A 1 182 ? 101.433 102.675 73.522  1.00 38.28 ? 171  LEU A CD2 1 
ATOM   1279 N  N   . PHE A 1 183 ? 96.854  103.166 74.686  1.00 42.78 ? 172  PHE A N   1 
ATOM   1280 C  CA  . PHE A 1 183 ? 95.802  103.584 73.770  1.00 42.78 ? 172  PHE A CA  1 
ATOM   1281 C  C   . PHE A 1 183 ? 94.832  104.544 74.434  1.00 42.78 ? 172  PHE A C   1 
ATOM   1282 O  O   . PHE A 1 183 ? 94.565  105.632 73.916  1.00 42.78 ? 172  PHE A O   1 
ATOM   1283 C  CB  . PHE A 1 183 ? 95.062  102.342 73.286  1.00 42.78 ? 172  PHE A CB  1 
ATOM   1284 C  CG  . PHE A 1 183 ? 93.877  102.629 72.423  1.00 42.78 ? 172  PHE A CG  1 
ATOM   1285 C  CD1 . PHE A 1 183 ? 92.603  102.587 72.956  1.00 42.78 ? 172  PHE A CD1 1 
ATOM   1286 C  CD2 . PHE A 1 183 ? 94.021  102.881 71.076  1.00 42.78 ? 172  PHE A CD2 1 
ATOM   1287 C  CE1 . PHE A 1 183 ? 91.503  102.833 72.173  1.00 42.78 ? 172  PHE A CE1 1 
ATOM   1288 C  CE2 . PHE A 1 183 ? 92.917  103.119 70.288  1.00 42.78 ? 172  PHE A CE2 1 
ATOM   1289 C  CZ  . PHE A 1 183 ? 91.662  103.097 70.837  1.00 42.78 ? 172  PHE A CZ  1 
ATOM   1290 N  N   . MET A 1 184 ? 94.277  104.149 75.578  1.00 38.77 ? 173  MET A N   1 
ATOM   1291 C  CA  . MET A 1 184 ? 93.257  104.977 76.207  1.00 38.77 ? 173  MET A CA  1 
ATOM   1292 C  C   . MET A 1 184 ? 93.830  106.326 76.620  1.00 38.77 ? 173  MET A C   1 
ATOM   1293 O  O   . MET A 1 184 ? 93.227  107.375 76.360  1.00 38.77 ? 173  MET A O   1 
ATOM   1294 C  CB  . MET A 1 184 ? 92.657  104.244 77.403  1.00 38.77 ? 173  MET A CB  1 
ATOM   1295 C  CG  . MET A 1 184 ? 92.012  102.915 77.042  1.00 38.77 ? 173  MET A CG  1 
ATOM   1296 S  SD  . MET A 1 184 ? 90.627  103.064 75.902  1.00 38.77 ? 173  MET A SD  1 
ATOM   1297 C  CE  . MET A 1 184 ? 89.507  104.073 76.861  1.00 38.77 ? 173  MET A CE  1 
ATOM   1298 N  N   . ARG A 1 185 ? 95.015  106.328 77.235  1.00 38.11 ? 174  ARG A N   1 
ATOM   1299 C  CA  . ARG A 1 185 ? 95.551  107.589 77.729  1.00 38.11 ? 174  ARG A CA  1 
ATOM   1300 C  C   . ARG A 1 185 ? 96.082  108.480 76.616  1.00 38.11 ? 174  ARG A C   1 
ATOM   1301 O  O   . ARG A 1 185 ? 96.181  109.692 76.817  1.00 38.11 ? 174  ARG A O   1 
ATOM   1302 C  CB  . ARG A 1 185 ? 96.653  107.337 78.753  1.00 38.11 ? 174  ARG A CB  1 
ATOM   1303 C  CG  . ARG A 1 185 ? 97.329  108.605 79.262  1.00 38.11 ? 174  ARG A CG  1 
ATOM   1304 C  CD  . ARG A 1 185 ? 96.351  109.520 79.969  1.00 38.11 ? 174  ARG A CD  1 
ATOM   1305 N  NE  . ARG A 1 185 ? 95.777  108.885 81.148  1.00 38.11 ? 174  ARG A NE  1 
ATOM   1306 C  CZ  . ARG A 1 185 ? 96.352  108.866 82.345  1.00 38.11 ? 174  ARG A CZ  1 
ATOM   1307 N  NH1 . ARG A 1 185 ? 97.527  109.446 82.535  1.00 38.11 ? 174  ARG A NH1 1 
ATOM   1308 N  NH2 . ARG A 1 185 ? 95.749  108.260 83.356  1.00 38.11 ? 174  ARG A NH2 1 
ATOM   1309 N  N   . VAL A 1 186 ? 96.435  107.929 75.454  1.00 43.22 ? 175  VAL A N   1 
ATOM   1310 C  CA  . VAL A 1 186 ? 96.848  108.802 74.361  1.00 43.22 ? 175  VAL A CA  1 
ATOM   1311 C  C   . VAL A 1 186 ? 95.632  109.314 73.607  1.00 43.22 ? 175  VAL A C   1 
ATOM   1312 O  O   . VAL A 1 186 ? 95.654  110.425 73.069  1.00 43.22 ? 175  VAL A O   1 
ATOM   1313 C  CB  . VAL A 1 186 ? 97.822  108.079 73.418  1.00 43.22 ? 175  VAL A CB  1 
ATOM   1314 C  CG1 . VAL A 1 186 ? 97.116  106.978 72.665  1.00 43.22 ? 175  VAL A CG1 1 
ATOM   1315 C  CG2 . VAL A 1 186 ? 98.449  109.063 72.452  1.00 43.22 ? 175  VAL A CG2 1 
ATOM   1316 N  N   . ARG A 1 187 ? 94.560  108.523 73.544  1.00 46.16 ? 176  ARG A N   1 
ATOM   1317 C  CA  . ARG A 1 187 ? 93.326  109.005 72.940  1.00 46.16 ? 176  ARG A CA  1 
ATOM   1318 C  C   . ARG A 1 187 ? 92.705  110.113 73.778  1.00 46.16 ? 176  ARG A C   1 
ATOM   1319 O  O   . ARG A 1 187 ? 92.102  111.044 73.234  1.00 46.16 ? 176  ARG A O   1 
ATOM   1320 C  CB  . ARG A 1 187 ? 92.349  107.843 72.767  1.00 46.16 ? 176  ARG A CB  1 
ATOM   1321 C  CG  . ARG A 1 187 ? 90.941  108.261 72.404  1.00 46.16 ? 176  ARG A CG  1 
ATOM   1322 C  CD  . ARG A 1 187 ? 90.062  107.059 72.118  1.00 46.16 ? 176  ARG A CD  1 
ATOM   1323 N  NE  . ARG A 1 187 ? 90.240  106.557 70.759  1.00 46.16 ? 176  ARG A NE  1 
ATOM   1324 C  CZ  . ARG A 1 187 ? 89.610  105.497 70.266  1.00 46.16 ? 176  ARG A CZ  1 
ATOM   1325 N  NH1 . ARG A 1 187 ? 88.757  104.816 71.019  1.00 46.16 ? 176  ARG A NH1 1 
ATOM   1326 N  NH2 . ARG A 1 187 ? 89.833  105.112 69.017  1.00 46.16 ? 176  ARG A NH2 1 
ATOM   1327 N  N   . ASP A 1 188 ? 92.839  110.032 75.103  1.00 45.11 ? 177  ASP A N   1 
ATOM   1328 C  CA  . ASP A 1 188 ? 92.227  111.038 75.966  1.00 45.11 ? 177  ASP A CA  1 
ATOM   1329 C  C   . ASP A 1 188 ? 92.783  112.430 75.686  1.00 45.11 ? 177  ASP A C   1 
ATOM   1330 O  O   . ASP A 1 188 ? 92.025  113.399 75.578  1.00 45.11 ? 177  ASP A O   1 
ATOM   1331 C  CB  . ASP A 1 188 ? 92.442  110.669 77.434  1.00 45.11 ? 177  ASP A CB  1 
ATOM   1332 C  CG  . ASP A 1 188 ? 91.364  109.750 77.971  1.00 45.11 ? 177  ASP A CG  1 
ATOM   1333 O  OD1 . ASP A 1 188 ? 91.419  109.412 79.173  1.00 45.11 ? 177  ASP A OD1 1 
ATOM   1334 O  OD2 . ASP A 1 188 ? 90.464  109.362 77.197  1.00 45.11 ? 177  ASP A OD2 1 
ATOM   1335 N  N   . ARG A 1 189 ? 94.105  112.553 75.564  1.00 44.51 ? 178  ARG A N   1 
ATOM   1336 C  CA  . ARG A 1 189 ? 94.768  113.852 75.576  1.00 44.51 ? 178  ARG A CA  1 
ATOM   1337 C  C   . ARG A 1 189 ? 95.524  114.142 74.282  1.00 44.51 ? 178  ARG A C   1 
ATOM   1338 O  O   . ARG A 1 189 ? 96.545  114.830 74.298  1.00 44.51 ? 178  ARG A O   1 
ATOM   1339 C  CB  . ARG A 1 189 ? 95.709  113.952 76.774  1.00 44.51 ? 178  ARG A CB  1 
ATOM   1340 C  CG  . ARG A 1 189 ? 96.704  112.820 76.880  1.00 44.51 ? 178  ARG A CG  1 
ATOM   1341 C  CD  . ARG A 1 189 ? 97.563  112.970 78.115  1.00 44.51 ? 178  ARG A CD  1 
ATOM   1342 N  NE  . ARG A 1 189 ? 98.413  114.152 78.045  1.00 44.51 ? 178  ARG A NE  1 
ATOM   1343 C  CZ  . ARG A 1 189 ? 99.062  114.670 79.082  1.00 44.51 ? 178  ARG A CZ  1 
ATOM   1344 N  NH1 . ARG A 1 189 ? 98.958  114.115 80.281  1.00 44.51 ? 178  ARG A NH1 1 
ATOM   1345 N  NH2 . ARG A 1 189 ? 99.814  115.749 78.921  1.00 44.51 ? 178  ARG A NH2 1 
ATOM   1346 N  N   . LEU A 1 190 ? 95.040  113.631 73.155  1.00 48.61 ? 179  LEU A N   1 
ATOM   1347 C  CA  . LEU A 1 190 ? 95.590  113.995 71.857  1.00 48.61 ? 179  LEU A CA  1 
ATOM   1348 C  C   . LEU A 1 190 ? 94.490  113.886 70.814  1.00 48.61 ? 179  LEU A C   1 
ATOM   1349 O  O   . LEU A 1 190 ? 93.667  112.969 70.864  1.00 48.61 ? 179  LEU A O   1 
ATOM   1350 C  CB  . LEU A 1 190 ? 96.774  113.102 71.462  1.00 48.61 ? 179  LEU A CB  1 
ATOM   1351 C  CG  . LEU A 1 190 ? 98.200  113.610 71.698  1.00 48.61 ? 179  LEU A CG  1 
ATOM   1352 C  CD1 . LEU A 1 190 ? 99.197  112.645 71.090  1.00 48.61 ? 179  LEU A CD1 1 
ATOM   1353 C  CD2 . LEU A 1 190 ? 98.411  114.997 71.128  1.00 48.61 ? 179  LEU A CD2 1 
ATOM   1354 N  N   . ASN A 1 191 ? 94.484  114.825 69.871  1.00 53.99 ? 180  ASN A N   1 
ATOM   1355 C  CA  . ASN A 1 191 ? 93.499  114.828 68.790  1.00 53.99 ? 180  ASN A CA  1 
ATOM   1356 C  C   . ASN A 1 191 ? 94.040  114.068 67.577  1.00 53.99 ? 180  ASN A C   1 
ATOM   1357 O  O   . ASN A 1 191 ? 94.169  114.597 66.474  1.00 53.99 ? 180  ASN A O   1 
ATOM   1358 C  CB  . ASN A 1 191 ? 93.123  116.260 68.424  1.00 53.99 ? 180  ASN A CB  1 
ATOM   1359 N  N   . ILE A 1 192 ? 94.360  112.794 67.807  1.00 53.37 ? 181  ILE A N   1 
ATOM   1360 C  CA  . ILE A 1 192 ? 94.874  111.916 66.767  1.00 53.37 ? 181  ILE A CA  1 
ATOM   1361 C  C   . ILE A 1 192 ? 93.999  110.674 66.707  1.00 53.37 ? 181  ILE A C   1 
ATOM   1362 O  O   . ILE A 1 192 ? 93.341  110.299 67.679  1.00 53.37 ? 181  ILE A O   1 
ATOM   1363 C  CB  . ILE A 1 192 ? 96.348  111.522 67.002  1.00 53.37 ? 181  ILE A CB  1 
ATOM   1364 C  CG1 . ILE A 1 192 ? 96.503  110.739 68.308  1.00 53.37 ? 181  ILE A CG1 1 
ATOM   1365 C  CG2 . ILE A 1 192 ? 97.219  112.757 67.043  1.00 53.37 ? 181  ILE A CG2 1 
ATOM   1366 C  CD1 . ILE A 1 192 ? 97.870  110.125 68.488  1.00 53.37 ? 181  ILE A CD1 1 
ATOM   1367 N  N   . THR A 1 193 ? 94.001  110.036 65.542  1.00 55.20 ? 182  THR A N   1 
ATOM   1368 C  CA  . THR A 1 193 ? 93.318  108.767 65.343  1.00 55.20 ? 182  THR A CA  1 
ATOM   1369 C  C   . THR A 1 193 ? 94.339  107.641 65.431  1.00 55.20 ? 182  THR A C   1 
ATOM   1370 O  O   . THR A 1 193 ? 95.363  107.663 64.738  1.00 55.20 ? 182  THR A O   1 
ATOM   1371 C  CB  . THR A 1 193 ? 92.581  108.737 64.002  1.00 55.20 ? 182  THR A CB  1 
ATOM   1372 O  OG1 . THR A 1 193 ? 91.788  107.547 63.915  1.00 55.20 ? 182  THR A OG1 1 
ATOM   1373 C  CG2 . THR A 1 193 ? 93.550  108.788 62.834  1.00 55.20 ? 182  THR A CG2 1 
ATOM   1374 N  N   . VAL A 1 194 ? 94.074  106.676 66.301  1.00 49.54 ? 183  VAL A N   1 
ATOM   1375 C  CA  . VAL A 1 194 ? 95.029  105.626 66.618  1.00 49.54 ? 183  VAL A CA  1 
ATOM   1376 C  C   . VAL A 1 194 ? 94.325  104.279 66.555  1.00 49.54 ? 183  VAL A C   1 
ATOM   1377 O  O   . VAL A 1 194 ? 93.185  104.143 67.011  1.00 49.54 ? 183  VAL A O   1 
ATOM   1378 C  CB  . VAL A 1 194 ? 95.681  105.864 67.995  1.00 49.54 ? 183  VAL A CB  1 
ATOM   1379 C  CG1 . VAL A 1 194 ? 96.491  107.127 67.991  1.00 49.54 ? 183  VAL A CG1 1 
ATOM   1380 C  CG2 . VAL A 1 194 ? 94.622  105.935 69.068  1.00 49.54 ? 183  VAL A CG2 1 
ATOM   1381 N  N   . ASP A 1 195 ? 95.005  103.286 65.985  1.00 48.33 ? 184  ASP A N   1 
ATOM   1382 C  CA  . ASP A 1 195 ? 94.386  102.006 65.657  1.00 48.33 ? 184  ASP A CA  1 
ATOM   1383 C  C   . ASP A 1 195 ? 95.089  100.851 66.358  1.00 48.33 ? 184  ASP A C   1 
ATOM   1384 O  O   . ASP A 1 195 ? 96.313  100.714 66.266  1.00 48.33 ? 184  ASP A O   1 
ATOM   1385 C  CB  . ASP A 1 195 ? 94.402  101.776 64.146  1.00 48.33 ? 184  ASP A CB  1 
ATOM   1386 N  N   . HIS A 1 196 ? 94.300  100.006 67.023  1.00 47.32 ? 185  HIS A N   1 
ATOM   1387 C  CA  . HIS A 1 196 ? 94.779  98.773  67.636  1.00 47.32 ? 185  HIS A CA  1 
ATOM   1388 C  C   . HIS A 1 196 ? 95.039  97.690  66.597  1.00 47.32 ? 185  HIS A C   1 
ATOM   1389 O  O   . HIS A 1 196 ? 94.424  97.664  65.528  1.00 47.32 ? 185  HIS A O   1 
ATOM   1390 C  CB  . HIS A 1 196 ? 93.746  98.231  68.626  1.00 47.32 ? 185  HIS A CB  1 
ATOM   1391 C  CG  . HIS A 1 196 ? 93.929  98.698  70.034  1.00 47.32 ? 185  HIS A CG  1 
ATOM   1392 N  ND1 . HIS A 1 196 ? 93.040  98.374  71.036  1.00 47.32 ? 185  HIS A ND1 1 
ATOM   1393 C  CD2 . HIS A 1 196 ? 94.900  99.437  70.617  1.00 47.32 ? 185  HIS A CD2 1 
ATOM   1394 C  CE1 . HIS A 1 196 ? 93.450  98.903  72.174  1.00 47.32 ? 185  HIS A CE1 1 
ATOM   1395 N  NE2 . HIS A 1 196 ? 94.576  99.554  71.947  1.00 47.32 ? 185  HIS A NE2 1 
ATOM   1396 N  N   . LEU A 1 197 ? 95.946  96.776  66.935  1.00 48.10 ? 186  LEU A N   1 
ATOM   1397 C  CA  . LEU A 1 197 ? 96.099  95.529  66.197  1.00 48.10 ? 186  LEU A CA  1 
ATOM   1398 C  C   . LEU A 1 197 ? 96.723  94.485  67.110  1.00 48.10 ? 186  LEU A C   1 
ATOM   1399 O  O   . LEU A 1 197 ? 97.609  94.801  67.908  1.00 48.10 ? 186  LEU A O   1 
ATOM   1400 C  CB  . LEU A 1 197 ? 96.965  95.695  64.943  1.00 48.10 ? 186  LEU A CB  1 
ATOM   1401 C  CG  . LEU A 1 197 ? 96.392  96.471  63.761  1.00 48.10 ? 186  LEU A CG  1 
ATOM   1402 C  CD1 . LEU A 1 197 ? 97.431  96.574  62.667  1.00 48.10 ? 186  LEU A CD1 1 
ATOM   1403 C  CD2 . LEU A 1 197 ? 95.135  95.802  63.236  1.00 48.10 ? 186  LEU A CD2 1 
ATOM   1404 N  N   . GLU A 1 198 ? 96.256  93.248  66.982  1.00 47.54 ? 187  GLU A N   1 
ATOM   1405 C  CA  . GLU A 1 198 ? 96.831  92.106  67.673  1.00 47.54 ? 187  GLU A CA  1 
ATOM   1406 C  C   . GLU A 1 198 ? 97.433  91.151  66.656  1.00 47.54 ? 187  GLU A C   1 
ATOM   1407 O  O   . GLU A 1 198 ? 96.884  90.965  65.567  1.00 47.54 ? 187  GLU A O   1 
ATOM   1408 C  CB  . GLU A 1 198 ? 95.784  91.362  68.502  1.00 47.54 ? 187  GLU A CB  1 
ATOM   1409 C  CG  . GLU A 1 198 ? 96.351  90.178  69.269  1.00 47.54 ? 187  GLU A CG  1 
ATOM   1410 C  CD  . GLU A 1 198 ? 95.315  89.467  70.114  1.00 47.54 ? 187  GLU A CD  1 
ATOM   1411 O  OE1 . GLU A 1 198 ? 94.316  90.107  70.501  1.00 47.54 ? 187  GLU A OE1 1 
ATOM   1412 O  OE2 . GLU A 1 198 ? 95.499  88.264  70.392  1.00 47.54 ? 187  GLU A OE2 1 
ATOM   1413 N  N   . PHE A 1 199 ? 98.563  90.548  67.009  1.00 48.78 ? 188  PHE A N   1 
ATOM   1414 C  CA  . PHE A 1 199 ? 99.133  89.492  66.189  1.00 48.78 ? 188  PHE A CA  1 
ATOM   1415 C  C   . PHE A 1 199 ? 99.671  88.397  67.096  1.00 48.78 ? 188  PHE A C   1 
ATOM   1416 O  O   . PHE A 1 199 ? 100.001 88.635  68.257  1.00 48.78 ? 188  PHE A O   1 
ATOM   1417 C  CB  . PHE A 1 199 ? 100.218 90.031  65.243  1.00 48.78 ? 188  PHE A CB  1 
ATOM   1418 C  CG  . PHE A 1 199 ? 101.482 90.466  65.928  1.00 48.78 ? 188  PHE A CG  1 
ATOM   1419 C  CD1 . PHE A 1 199 ? 102.557 89.605  66.038  1.00 48.78 ? 188  PHE A CD1 1 
ATOM   1420 C  CD2 . PHE A 1 199 ? 101.608 91.745  66.433  1.00 48.78 ? 188  PHE A CD2 1 
ATOM   1421 C  CE1 . PHE A 1 199 ? 103.722 90.006  66.655  1.00 48.78 ? 188  PHE A CE1 1 
ATOM   1422 C  CE2 . PHE A 1 199 ? 102.774 92.149  67.051  1.00 48.78 ? 188  PHE A CE2 1 
ATOM   1423 C  CZ  . PHE A 1 199 ? 103.830 91.279  67.157  1.00 48.78 ? 188  PHE A CZ  1 
ATOM   1424 N  N   . ALA A 1 200 ? 99.732  87.182  66.560  1.00 51.94 ? 189  ALA A N   1 
ATOM   1425 C  CA  . ALA A 1 200 ? 100.199 86.026  67.312  1.00 51.94 ? 189  ALA A CA  1 
ATOM   1426 C  C   . ALA A 1 200 ? 101.715 85.949  67.210  1.00 51.94 ? 189  ALA A C   1 
ATOM   1427 O  O   . ALA A 1 200 ? 102.264 85.854  66.108  1.00 51.94 ? 189  ALA A O   1 
ATOM   1428 C  CB  . ALA A 1 200 ? 99.556  84.743  66.793  1.00 51.94 ? 189  ALA A CB  1 
ATOM   1429 N  N   . GLU A 1 201 ? 102.387 85.988  68.360  1.00 52.08 ? 190  GLU A N   1 
ATOM   1430 C  CA  . GLU A 1 201 ? 103.842 86.088  68.365  1.00 52.08 ? 190  GLU A CA  1 
ATOM   1431 C  C   . GLU A 1 201 ? 104.484 84.871  67.714  1.00 52.08 ? 190  GLU A C   1 
ATOM   1432 O  O   . GLU A 1 201 ? 105.412 85.000  66.908  1.00 52.08 ? 190  GLU A O   1 
ATOM   1433 C  CB  . GLU A 1 201 ? 104.342 86.256  69.796  1.00 52.08 ? 190  GLU A CB  1 
ATOM   1434 C  CG  . GLU A 1 201 ? 105.839 86.393  69.899  1.00 52.08 ? 190  GLU A CG  1 
ATOM   1435 C  CD  . GLU A 1 201 ? 106.279 86.945  71.231  1.00 52.08 ? 190  GLU A CD  1 
ATOM   1436 O  OE1 . GLU A 1 201 ? 105.413 87.387  72.014  1.00 52.08 ? 190  GLU A OE1 1 
ATOM   1437 O  OE2 . GLU A 1 201 ? 107.496 86.927  71.499  1.00 52.08 ? 190  GLU A OE2 1 
ATOM   1438 N  N   . ASP A 1 202 ? 104.006 83.678  68.054  1.00 56.04 ? 191  ASP A N   1 
ATOM   1439 C  CA  . ASP A 1 202 ? 104.556 82.439  67.506  1.00 56.04 ? 191  ASP A CA  1 
ATOM   1440 C  C   . ASP A 1 202 ? 103.761 82.008  66.273  1.00 56.04 ? 191  ASP A C   1 
ATOM   1441 O  O   . ASP A 1 202 ? 103.164 80.934  66.219  1.00 56.04 ? 191  ASP A O   1 
ATOM   1442 C  CB  . ASP A 1 202 ? 104.560 81.352  68.573  1.00 56.04 ? 191  ASP A CB  1 
ATOM   1443 N  N   . ASP A 1 203 ? 103.758 82.885  65.268  1.00 56.97 ? 192  ASP A N   1 
ATOM   1444 C  CA  . ASP A 1 203 ? 103.006 82.639  64.039  1.00 56.97 ? 192  ASP A CA  1 
ATOM   1445 C  C   . ASP A 1 203 ? 103.726 83.360  62.903  1.00 56.97 ? 192  ASP A C   1 
ATOM   1446 O  O   . ASP A 1 203 ? 103.507 84.554  62.687  1.00 56.97 ? 192  ASP A O   1 
ATOM   1447 C  CB  . ASP A 1 203 ? 101.567 83.111  64.184  1.00 56.97 ? 192  ASP A CB  1 
ATOM   1448 C  CG  . ASP A 1 203 ? 100.615 82.368  63.278  1.00 56.97 ? 192  ASP A CG  1 
ATOM   1449 O  OD1 . ASP A 1 203 ? 99.875  81.498  63.781  1.00 56.97 ? 192  ASP A OD1 1 
ATOM   1450 O  OD2 . ASP A 1 203 ? 100.597 82.663  62.066  1.00 56.97 ? 192  ASP A OD2 1 
ATOM   1451 N  N   . LEU A 1 204 ? 104.571 82.626  62.177  1.00 58.74 ? 193  LEU A N   1 
ATOM   1452 C  CA  . LEU A 1 204 ? 105.374 83.234  61.122  1.00 58.74 ? 193  LEU A CA  1 
ATOM   1453 C  C   . LEU A 1 204 ? 104.522 83.811  60.000  1.00 58.74 ? 193  LEU A C   1 
ATOM   1454 O  O   . LEU A 1 204 ? 104.995 84.687  59.269  1.00 58.74 ? 193  LEU A O   1 
ATOM   1455 C  CB  . LEU A 1 204 ? 106.348 82.204  60.550  1.00 58.74 ? 193  LEU A CB  1 
ATOM   1456 N  N   . SER A 1 205 ? 103.289 83.334  59.836  1.00 58.58 ? 194  SER A N   1 
ATOM   1457 C  CA  . SER A 1 205 ? 102.409 83.879  58.810  1.00 58.58 ? 194  SER A CA  1 
ATOM   1458 C  C   . SER A 1 205 ? 101.817 85.220  59.218  1.00 58.58 ? 194  SER A C   1 
ATOM   1459 O  O   . SER A 1 205 ? 101.539 86.060  58.353  1.00 58.58 ? 194  SER A O   1 
ATOM   1460 C  CB  . SER A 1 205 ? 101.282 82.895  58.507  1.00 58.58 ? 194  SER A CB  1 
ATOM   1461 O  OG  . SER A 1 205 ? 100.309 83.492  57.671  1.00 58.58 ? 194  SER A OG  1 
ATOM   1462 N  N   . HIS A 1 206 ? 101.611 85.434  60.519  1.00 56.71 ? 195  HIS A N   1 
ATOM   1463 C  CA  . HIS A 1 206 ? 100.995 86.676  60.970  1.00 56.71 ? 195  HIS A CA  1 
ATOM   1464 C  C   . HIS A 1 206 ? 101.861 87.878  60.624  1.00 56.71 ? 195  HIS A C   1 
ATOM   1465 O  O   . HIS A 1 206 ? 101.342 88.940  60.279  1.00 56.71 ? 195  HIS A O   1 
ATOM   1466 C  CB  . HIS A 1 206 ? 100.729 86.618  62.472  1.00 56.71 ? 195  HIS A CB  1 
ATOM   1467 C  CG  . HIS A 1 206 ? 99.384  86.064  62.820  1.00 56.71 ? 195  HIS A CG  1 
ATOM   1468 N  ND1 . HIS A 1 206 ? 98.986  84.797  62.456  1.00 56.71 ? 195  HIS A ND1 1 
ATOM   1469 C  CD2 . HIS A 1 206 ? 98.343  86.606  63.494  1.00 56.71 ? 195  HIS A CD2 1 
ATOM   1470 C  CE1 . HIS A 1 206 ? 97.759  84.580  62.893  1.00 56.71 ? 195  HIS A CE1 1 
ATOM   1471 N  NE2 . HIS A 1 206 ? 97.346  85.663  63.527  1.00 56.71 ? 195  HIS A NE2 1 
ATOM   1472 N  N   . TYR A 1 207 ? 103.183 87.734  60.707  1.00 55.44 ? 196  TYR A N   1 
ATOM   1473 C  CA  . TYR A 1 207 ? 104.058 88.831  60.310  1.00 55.44 ? 196  TYR A CA  1 
ATOM   1474 C  C   . TYR A 1 207 ? 103.893 89.149  58.829  1.00 55.44 ? 196  TYR A C   1 
ATOM   1475 O  O   . TYR A 1 207 ? 103.898 90.321  58.430  1.00 55.44 ? 196  TYR A O   1 
ATOM   1476 C  CB  . TYR A 1 207 ? 105.510 88.483  60.631  1.00 55.44 ? 196  TYR A CB  1 
ATOM   1477 C  CG  . TYR A 1 207 ? 105.720 88.074  62.070  1.00 55.44 ? 196  TYR A CG  1 
ATOM   1478 C  CD1 . TYR A 1 207 ? 105.906 89.022  63.059  1.00 55.44 ? 196  TYR A CD1 1 
ATOM   1479 C  CD2 . TYR A 1 207 ? 105.726 86.740  62.440  1.00 55.44 ? 196  TYR A CD2 1 
ATOM   1480 C  CE1 . TYR A 1 207 ? 106.092 88.654  64.371  1.00 55.44 ? 196  TYR A CE1 1 
ATOM   1481 C  CE2 . TYR A 1 207 ? 105.913 86.365  63.751  1.00 55.44 ? 196  TYR A CE2 1 
ATOM   1482 C  CZ  . TYR A 1 207 ? 106.094 87.326  64.711  1.00 55.44 ? 196  TYR A CZ  1 
ATOM   1483 O  OH  . TYR A 1 207 ? 106.280 86.958  66.019  1.00 55.44 ? 196  TYR A OH  1 
ATOM   1484 N  N   . THR A 1 208 ? 103.750 88.116  57.998  1.00 56.00 ? 197  THR A N   1 
ATOM   1485 C  CA  . THR A 1 208 ? 103.523 88.341  56.575  1.00 56.00 ? 197  THR A CA  1 
ATOM   1486 C  C   . THR A 1 208 ? 102.207 89.068  56.339  1.00 56.00 ? 197  THR A C   1 
ATOM   1487 O  O   . THR A 1 208 ? 102.135 89.983  55.511  1.00 56.00 ? 197  THR A O   1 
ATOM   1488 C  CB  . THR A 1 208 ? 103.537 87.010  55.825  1.00 56.00 ? 197  THR A CB  1 
ATOM   1489 N  N   . ARG A 1 209 ? 101.154 88.681  57.059  1.00 56.06 ? 198  ARG A N   1 
ATOM   1490 C  CA  . ARG A 1 209 ? 99.858  89.330  56.900  1.00 56.06 ? 198  ARG A CA  1 
ATOM   1491 C  C   . ARG A 1 209 ? 99.781  90.676  57.608  1.00 56.06 ? 198  ARG A C   1 
ATOM   1492 O  O   . ARG A 1 209 ? 98.800  91.402  57.420  1.00 56.06 ? 198  ARG A O   1 
ATOM   1493 C  CB  . ARG A 1 209 ? 98.746  88.418  57.419  1.00 56.06 ? 198  ARG A CB  1 
ATOM   1494 N  N   . LEU A 1 210 ? 100.780 91.012  58.419  1.00 53.87 ? 199  LEU A N   1 
ATOM   1495 C  CA  . LEU A 1 210 ? 100.840 92.281  59.132  1.00 53.87 ? 199  LEU A CA  1 
ATOM   1496 C  C   . LEU A 1 210 ? 101.629 93.332  58.369  1.00 53.87 ? 199  LEU A C   1 
ATOM   1497 O  O   . LEU A 1 210 ? 101.263 94.512  58.379  1.00 53.87 ? 199  LEU A O   1 
ATOM   1498 C  CB  . LEU A 1 210 ? 101.479 92.064  60.504  1.00 53.87 ? 199  LEU A CB  1 
ATOM   1499 C  CG  . LEU A 1 210 ? 100.945 92.808  61.722  1.00 53.87 ? 199  LEU A CG  1 
ATOM   1500 C  CD1 . LEU A 1 210 ? 99.503  92.456  62.026  1.00 53.87 ? 199  LEU A CD1 1 
ATOM   1501 C  CD2 . LEU A 1 210 ? 101.836 92.464  62.891  1.00 53.87 ? 199  LEU A CD2 1 
ATOM   1502 N  N   . LEU A 1 211 ? 102.731 92.932  57.737  1.00 55.85 ? 200  LEU A N   1 
ATOM   1503 C  CA  . LEU A 1 211 ? 103.474 93.866  56.903  1.00 55.85 ? 200  LEU A CA  1 
ATOM   1504 C  C   . LEU A 1 211 ? 102.673 94.303  55.687  1.00 55.85 ? 200  LEU A C   1 
ATOM   1505 O  O   . LEU A 1 211 ? 103.009 95.318  55.070  1.00 55.85 ? 200  LEU A O   1 
ATOM   1506 C  CB  . LEU A 1 211 ? 104.795 93.240  56.468  1.00 55.85 ? 200  LEU A CB  1 
ATOM   1507 C  CG  . LEU A 1 211 ? 105.812 93.152  57.603  1.00 55.85 ? 200  LEU A CG  1 
ATOM   1508 C  CD1 . LEU A 1 211 ? 106.776 92.012  57.378  1.00 55.85 ? 200  LEU A CD1 1 
ATOM   1509 C  CD2 . LEU A 1 211 ? 106.556 94.468  57.738  1.00 55.85 ? 200  LEU A CD2 1 
ATOM   1510 N  N   . ARG A 1 212 ? 101.633 93.554  55.321  1.00 58.53 ? 201  ARG A N   1 
ATOM   1511 C  CA  . ARG A 1 212 ? 100.747 93.984  54.247  1.00 58.53 ? 201  ARG A CA  1 
ATOM   1512 C  C   . ARG A 1 212 ? 99.816  95.100  54.705  1.00 58.53 ? 201  ARG A C   1 
ATOM   1513 O  O   . ARG A 1 212 ? 99.596  96.068  53.969  1.00 58.53 ? 201  ARG A O   1 
ATOM   1514 C  CB  . ARG A 1 212 ? 99.936  92.794  53.735  1.00 58.53 ? 201  ARG A CB  1 
ATOM   1515 N  N   . THR A 1 213 ? 99.265  94.985  55.913  1.00 57.20 ? 202  THR A N   1 
ATOM   1516 C  CA  . THR A 1 213 ? 98.281  95.938  56.410  1.00 57.20 ? 202  THR A CA  1 
ATOM   1517 C  C   . THR A 1 213 ? 98.897  97.098  57.180  1.00 57.20 ? 202  THR A C   1 
ATOM   1518 O  O   . THR A 1 213 ? 98.174  98.035  57.533  1.00 57.20 ? 202  THR A O   1 
ATOM   1519 C  CB  . THR A 1 213 ? 97.266  95.229  57.315  1.00 57.20 ? 202  THR A CB  1 
ATOM   1520 O  OG1 . THR A 1 213 ? 96.206  96.133  57.647  1.00 57.20 ? 202  THR A OG1 1 
ATOM   1521 C  CG2 . THR A 1 213 ? 97.926  94.756  58.597  1.00 57.20 ? 202  THR A CG2 1 
ATOM   1522 N  N   . MET A 1 214 ? 100.194 97.062  57.458  1.00 57.27 ? 203  MET A N   1 
ATOM   1523 C  CA  . MET A 1 214 ? 100.827 98.159  58.181  1.00 57.27 ? 203  MET A CA  1 
ATOM   1524 C  C   . MET A 1 214 ? 100.979 99.394  57.298  1.00 57.27 ? 203  MET A C   1 
ATOM   1525 O  O   . MET A 1 214 ? 100.689 100.509 57.747  1.00 57.27 ? 203  MET A O   1 
ATOM   1526 C  CB  . MET A 1 214 ? 102.192 97.725  58.718  1.00 57.27 ? 203  MET A CB  1 
ATOM   1527 C  CG  . MET A 1 214 ? 102.662 98.520  59.923  1.00 57.27 ? 203  MET A CG  1 
ATOM   1528 S  SD  . MET A 1 214 ? 104.225 97.946  60.624  1.00 57.27 ? 203  MET A SD  1 
ATOM   1529 C  CE  . MET A 1 214 ? 104.007 96.167  60.643  1.00 57.27 ? 203  MET A CE  1 
ATOM   1530 N  N   . PRO A 1 215 ? 101.432 99.251  56.049  1.00 59.36 ? 204  PRO A N   1 
ATOM   1531 C  CA  . PRO A 1 215 ? 101.641 100.444 55.213  1.00 59.36 ? 204  PRO A CA  1 
ATOM   1532 C  C   . PRO A 1 215 ? 100.377 101.230 54.925  1.00 59.36 ? 204  PRO A C   1 
ATOM   1533 O  O   . PRO A 1 215 ? 100.474 102.398 54.529  1.00 59.36 ? 204  PRO A O   1 
ATOM   1534 C  CB  . PRO A 1 215 ? 102.243 99.865  53.925  1.00 59.36 ? 204  PRO A CB  1 
ATOM   1535 C  CG  . PRO A 1 215 ? 102.851 98.580  54.342  1.00 59.36 ? 204  PRO A CG  1 
ATOM   1536 C  CD  . PRO A 1 215 ? 101.922 98.036  55.379  1.00 59.36 ? 204  PRO A CD  1 
ATOM   1537 N  N   . ARG A 1 216 ? 99.198  100.634 55.095  1.00 62.39 ? 205  ARG A N   1 
ATOM   1538 C  CA  . ARG A 1 216 ? 97.934  101.318 54.854  1.00 62.39 ? 205  ARG A CA  1 
ATOM   1539 C  C   . ARG A 1 216 ? 97.204  101.651 56.149  1.00 62.39 ? 205  ARG A C   1 
ATOM   1540 O  O   . ARG A 1 216 ? 95.988  101.861 56.132  1.00 62.39 ? 205  ARG A O   1 
ATOM   1541 C  CB  . ARG A 1 216 ? 97.041  100.468 53.950  1.00 62.39 ? 205  ARG A CB  1 
ATOM   1542 N  N   . LYS A 1 217 ? 97.919  101.700 57.275  1.00 58.88 ? 206  LYS A N   1 
ATOM   1543 C  CA  . LYS A 1 217 ? 97.294  101.954 58.564  1.00 58.88 ? 206  LYS A CA  1 
ATOM   1544 C  C   . LYS A 1 217 ? 98.052  102.928 59.455  1.00 58.88 ? 206  LYS A C   1 
ATOM   1545 O  O   . LYS A 1 217 ? 97.508  103.321 60.491  1.00 58.88 ? 206  LYS A O   1 
ATOM   1546 C  CB  . LYS A 1 217 ? 97.105  100.638 59.332  1.00 58.88 ? 206  LYS A CB  1 
ATOM   1547 N  N   . GLY A 1 218 ? 99.267  103.330 59.104  1.00 58.39 ? 207  GLY A N   1 
ATOM   1548 C  CA  . GLY A 1 218 ? 99.980  104.291 59.924  1.00 58.39 ? 207  GLY A CA  1 
ATOM   1549 C  C   . GLY A 1 218 ? 101.418 104.439 59.489  1.00 58.39 ? 207  GLY A C   1 
ATOM   1550 O  O   . GLY A 1 218 ? 101.959 103.625 58.737  1.00 58.39 ? 207  GLY A O   1 
ATOM   1551 N  N   . ARG A 1 219 ? 102.036 105.512 59.987  1.00 59.48 ? 208  ARG A N   1 
ATOM   1552 C  CA  . ARG A 1 219 ? 103.429 105.828 59.705  1.00 59.48 ? 208  ARG A CA  1 
ATOM   1553 C  C   . ARG A 1 219 ? 104.273 105.965 60.961  1.00 59.48 ? 208  ARG A C   1 
ATOM   1554 O  O   . ARG A 1 219 ? 105.492 106.133 60.853  1.00 59.48 ? 208  ARG A O   1 
ATOM   1555 C  CB  . ARG A 1 219 ? 103.524 107.129 58.890  1.00 59.48 ? 208  ARG A CB  1 
ATOM   1556 C  CG  . ARG A 1 219 ? 103.166 107.006 57.411  1.00 59.48 ? 208  ARG A CG  1 
ATOM   1557 C  CD  . ARG A 1 219 ? 103.690 105.727 56.827  1.00 59.48 ? 208  ARG A CD  1 
ATOM   1558 N  NE  . ARG A 1 219 ? 103.981 105.813 55.398  1.00 59.48 ? 208  ARG A NE  1 
ATOM   1559 C  CZ  . ARG A 1 219 ? 103.280 105.211 54.439  1.00 59.48 ? 208  ARG A CZ  1 
ATOM   1560 N  NH1 . ARG A 1 219 ? 102.226 104.457 54.730  1.00 59.48 ? 208  ARG A NH1 1 
ATOM   1561 N  NH2 . ARG A 1 219 ? 103.645 105.363 53.174  1.00 59.48 ? 208  ARG A NH2 1 
ATOM   1562 N  N   . VAL A 1 220 ? 103.668 105.903 62.142  1.00 51.81 ? 209  VAL A N   1 
ATOM   1563 C  CA  . VAL A 1 220 ? 104.385 105.886 63.408  1.00 51.81 ? 209  VAL A CA  1 
ATOM   1564 C  C   . VAL A 1 220 ? 103.808 104.727 64.202  1.00 51.81 ? 209  VAL A C   1 
ATOM   1565 O  O   . VAL A 1 220 ? 102.688 104.822 64.717  1.00 51.81 ? 209  VAL A O   1 
ATOM   1566 C  CB  . VAL A 1 220 ? 104.248 107.207 64.174  1.00 51.81 ? 209  VAL A CB  1 
ATOM   1567 C  CG1 . VAL A 1 220 ? 104.754 107.059 65.594  1.00 51.81 ? 209  VAL A CG1 1 
ATOM   1568 C  CG2 . VAL A 1 220 ? 104.999 108.308 63.451  1.00 51.81 ? 209  VAL A CG2 1 
ATOM   1569 N  N   . ILE A 1 221 ? 104.562 103.637 64.300  1.00 49.07 ? 210  ILE A N   1 
ATOM   1570 C  CA  . ILE A 1 221 ? 104.066 102.366 64.810  1.00 49.07 ? 210  ILE A CA  1 
ATOM   1571 C  C   . ILE A 1 221 ? 104.676 102.110 66.178  1.00 49.07 ? 210  ILE A C   1 
ATOM   1572 O  O   . ILE A 1 221 ? 105.870 102.346 66.387  1.00 49.07 ? 210  ILE A O   1 
ATOM   1573 C  CB  . ILE A 1 221 ? 104.400 101.215 63.843  1.00 49.07 ? 210  ILE A CB  1 
ATOM   1574 C  CG1 . ILE A 1 221 ? 103.929 101.552 62.429  1.00 49.07 ? 210  ILE A CG1 1 
ATOM   1575 C  CG2 . ILE A 1 221 ? 103.756 99.933  64.304  1.00 49.07 ? 210  ILE A CG2 1 
ATOM   1576 C  CD1 . ILE A 1 221 ? 105.016 102.093 61.541  1.00 49.07 ? 210  ILE A CD1 1 
ATOM   1577 N  N   . TYR A 1 222 ? 103.851 101.643 67.112  1.00 43.43 ? 211  TYR A N   1 
ATOM   1578 C  CA  . TYR A 1 222 ? 104.294 101.247 68.444  1.00 43.43 ? 211  TYR A CA  1 
ATOM   1579 C  C   . TYR A 1 222 ? 104.017 99.763  68.617  1.00 43.43 ? 211  TYR A C   1 
ATOM   1580 O  O   . TYR A 1 222 ? 102.859 99.342  68.569  1.00 43.43 ? 211  TYR A O   1 
ATOM   1581 C  CB  . TYR A 1 222 ? 103.577 102.050 69.529  1.00 43.43 ? 211  TYR A CB  1 
ATOM   1582 C  CG  . TYR A 1 222 ? 103.817 103.537 69.458  1.00 43.43 ? 211  TYR A CG  1 
ATOM   1583 C  CD1 . TYR A 1 222 ? 104.871 104.122 70.136  1.00 43.43 ? 211  TYR A CD1 1 
ATOM   1584 C  CD2 . TYR A 1 222 ? 102.982 104.358 68.718  1.00 43.43 ? 211  TYR A CD2 1 
ATOM   1585 C  CE1 . TYR A 1 222 ? 105.091 105.475 70.072  1.00 43.43 ? 211  TYR A CE1 1 
ATOM   1586 C  CE2 . TYR A 1 222 ? 103.195 105.712 68.651  1.00 43.43 ? 211  TYR A CE2 1 
ATOM   1587 C  CZ  . TYR A 1 222 ? 104.251 106.264 69.328  1.00 43.43 ? 211  TYR A CZ  1 
ATOM   1588 O  OH  . TYR A 1 222 ? 104.470 107.617 69.266  1.00 43.43 ? 211  TYR A OH  1 
ATOM   1589 N  N   . ILE A 1 223 ? 105.068 98.980  68.848  1.00 43.71 ? 212  ILE A N   1 
ATOM   1590 C  CA  . ILE A 1 223 ? 104.992 97.523  68.875  1.00 43.71 ? 212  ILE A CA  1 
ATOM   1591 C  C   . ILE A 1 223 ? 105.310 97.041  70.282  1.00 43.71 ? 212  ILE A C   1 
ATOM   1592 O  O   . ILE A 1 223 ? 106.310 97.461  70.872  1.00 43.71 ? 212  ILE A O   1 
ATOM   1593 C  CB  . ILE A 1 223 ? 105.961 96.893  67.860  1.00 43.71 ? 212  ILE A CB  1 
ATOM   1594 C  CG1 . ILE A 1 223 ? 105.630 97.359  66.446  1.00 43.71 ? 212  ILE A CG1 1 
ATOM   1595 C  CG2 . ILE A 1 223 ? 105.902 95.384  67.936  1.00 43.71 ? 212  ILE A CG2 1 
ATOM   1596 C  CD1 . ILE A 1 223 ? 106.800 97.302  65.507  1.00 43.71 ? 212  ILE A CD1 1 
ATOM   1597 N  N   . CYS A 1 224 ? 104.467 96.159  70.816  1.00 40.89 ? 213  CYS A N   1 
ATOM   1598 C  CA  . CYS A 1 224 ? 104.735 95.487  72.086  1.00 40.89 ? 213  CYS A CA  1 
ATOM   1599 C  C   . CYS A 1 224 ? 104.851 93.991  71.831  1.00 40.89 ? 213  CYS A C   1 
ATOM   1600 O  O   . CYS A 1 224 ? 103.840 93.311  71.623  1.00 40.89 ? 213  CYS A O   1 
ATOM   1601 C  CB  . CYS A 1 224 ? 103.646 95.770  73.117  1.00 40.89 ? 213  CYS A CB  1 
ATOM   1602 S  SG  . CYS A 1 224 ? 104.021 95.120  74.767  1.00 40.89 ? 213  CYS A SG  1 
ATOM   1603 N  N   . SER A 1 225 ? 106.073 93.476  71.885  1.00 44.93 ? 214  SER A N   1 
ATOM   1604 C  CA  . SER A 1 225 ? 106.330 92.056  71.699  1.00 44.93 ? 214  SER A CA  1 
ATOM   1605 C  C   . SER A 1 225 ? 107.702 91.751  72.284  1.00 44.93 ? 214  SER A C   1 
ATOM   1606 O  O   . SER A 1 225 ? 108.376 92.630  72.825  1.00 44.93 ? 214  SER A O   1 
ATOM   1607 C  CB  . SER A 1 225 ? 106.246 91.672  70.223  1.00 44.93 ? 214  SER A CB  1 
ATOM   1608 O  OG  . SER A 1 225 ? 107.302 92.258  69.486  1.00 44.93 ? 214  SER A OG  1 
ATOM   1609 N  N   . SER A 1 226 ? 108.113 90.492  72.168  1.00 47.02 ? 215  SER A N   1 
ATOM   1610 C  CA  . SER A 1 226 ? 109.388 90.066  72.712  1.00 47.02 ? 215  SER A CA  1 
ATOM   1611 C  C   . SER A 1 226 ? 110.539 90.632  71.887  1.00 47.02 ? 215  SER A C   1 
ATOM   1612 O  O   . SER A 1 226 ? 110.346 91.071  70.753  1.00 47.02 ? 215  SER A O   1 
ATOM   1613 C  CB  . SER A 1 226 ? 109.475 88.547  72.730  1.00 47.02 ? 215  SER A CB  1 
ATOM   1614 O  OG  . SER A 1 226 ? 108.435 87.994  73.513  1.00 47.02 ? 215  SER A OG  1 
ATOM   1615 N  N   . PRO A 1 227 ? 111.750 90.647  72.446  1.00 45.09 ? 216  PRO A N   1 
ATOM   1616 C  CA  . PRO A 1 227 ? 112.902 91.102  71.651  1.00 45.09 ? 216  PRO A CA  1 
ATOM   1617 C  C   . PRO A 1 227 ? 113.095 90.324  70.362  1.00 45.09 ? 216  PRO A C   1 
ATOM   1618 O  O   . PRO A 1 227 ? 113.386 90.922  69.316  1.00 45.09 ? 216  PRO A O   1 
ATOM   1619 C  CB  . PRO A 1 227 ? 114.076 90.900  72.614  1.00 45.09 ? 216  PRO A CB  1 
ATOM   1620 C  CG  . PRO A 1 227 ? 113.473 90.998  73.961  1.00 45.09 ? 216  PRO A CG  1 
ATOM   1621 C  CD  . PRO A 1 227 ? 112.117 90.386  73.846  1.00 45.09 ? 216  PRO A CD  1 
ATOM   1622 N  N   . ASP A 1 228 ? 112.924 89.000  70.405  1.00 48.78 ? 217  ASP A N   1 
ATOM   1623 C  CA  . ASP A 1 228 ? 113.139 88.187  69.212  1.00 48.78 ? 217  ASP A CA  1 
ATOM   1624 C  C   . ASP A 1 228 ? 112.052 88.432  68.175  1.00 48.78 ? 217  ASP A C   1 
ATOM   1625 O  O   . ASP A 1 228 ? 112.339 88.521  66.975  1.00 48.78 ? 217  ASP A O   1 
ATOM   1626 C  CB  . ASP A 1 228 ? 113.194 86.710  69.590  1.00 48.78 ? 217  ASP A CB  1 
ATOM   1627 N  N   . ALA A 1 229 ? 110.799 88.545  68.615  1.00 49.00 ? 218  ALA A N   1 
ATOM   1628 C  CA  . ALA A 1 229 ? 109.724 88.845  67.679  1.00 49.00 ? 218  ALA A CA  1 
ATOM   1629 C  C   . ALA A 1 229 ? 109.950 90.192  67.008  1.00 49.00 ? 218  ALA A C   1 
ATOM   1630 O  O   . ALA A 1 229 ? 109.753 90.330  65.797  1.00 49.00 ? 218  ALA A O   1 
ATOM   1631 C  CB  . ALA A 1 229 ? 108.377 88.823  68.397  1.00 49.00 ? 218  ALA A CB  1 
ATOM   1632 N  N   . PHE A 1 230 ? 110.365 91.199  67.777  1.00 46.16 ? 219  PHE A N   1 
ATOM   1633 C  CA  . PHE A 1 230 ? 110.614 92.510  67.191  1.00 46.16 ? 219  PHE A CA  1 
ATOM   1634 C  C   . PHE A 1 230 ? 111.773 92.463  66.206  1.00 46.16 ? 219  PHE A C   1 
ATOM   1635 O  O   . PHE A 1 230 ? 111.718 93.103  65.152  1.00 46.16 ? 219  PHE A O   1 
ATOM   1636 C  CB  . PHE A 1 230 ? 110.890 93.537  68.283  1.00 46.16 ? 219  PHE A CB  1 
ATOM   1637 C  CG  . PHE A 1 230 ? 111.101 94.933  67.764  1.00 46.16 ? 219  PHE A CG  1 
ATOM   1638 C  CD1 . PHE A 1 230 ? 112.376 95.438  67.593  1.00 46.16 ? 219  PHE A CD1 1 
ATOM   1639 C  CD2 . PHE A 1 230 ? 110.024 95.740  67.452  1.00 46.16 ? 219  PHE A CD2 1 
ATOM   1640 C  CE1 . PHE A 1 230 ? 112.569 96.716  67.121  1.00 46.16 ? 219  PHE A CE1 1 
ATOM   1641 C  CE2 . PHE A 1 230 ? 110.217 97.017  66.982  1.00 46.16 ? 219  PHE A CE2 1 
ATOM   1642 C  CZ  . PHE A 1 230 ? 111.490 97.504  66.817  1.00 46.16 ? 219  PHE A CZ  1 
ATOM   1643 N  N   . ARG A 1 231 ? 112.837 91.727  66.532  1.00 52.68 ? 220  ARG A N   1 
ATOM   1644 C  CA  . ARG A 1 231 ? 113.957 91.624  65.601  1.00 52.68 ? 220  ARG A CA  1 
ATOM   1645 C  C   . ARG A 1 231 ? 113.535 90.935  64.308  1.00 52.68 ? 220  ARG A C   1 
ATOM   1646 O  O   . ARG A 1 231 ? 113.916 91.365  63.212  1.00 52.68 ? 220  ARG A O   1 
ATOM   1647 C  CB  . ARG A 1 231 ? 115.113 90.875  66.256  1.00 52.68 ? 220  ARG A CB  1 
ATOM   1648 C  CG  . ARG A 1 231 ? 116.386 90.855  65.434  1.00 52.68 ? 220  ARG A CG  1 
ATOM   1649 C  CD  . ARG A 1 231 ? 117.468 90.054  66.130  1.00 52.68 ? 220  ARG A CD  1 
ATOM   1650 N  NE  . ARG A 1 231 ? 118.647 89.863  65.292  1.00 52.68 ? 220  ARG A NE  1 
ATOM   1651 C  CZ  . ARG A 1 231 ? 118.826 88.844  64.457  1.00 52.68 ? 220  ARG A CZ  1 
ATOM   1652 N  NH1 . ARG A 1 231 ? 117.900 87.904  64.328  1.00 52.68 ? 220  ARG A NH1 1 
ATOM   1653 N  NH2 . ARG A 1 231 ? 119.939 88.767  63.744  1.00 52.68 ? 220  ARG A NH2 1 
ATOM   1654 N  N   . THR A 1 232 ? 112.747 89.863  64.415  1.00 51.81 ? 221  THR A N   1 
ATOM   1655 C  CA  . THR A 1 232 ? 112.245 89.192  63.219  1.00 51.81 ? 221  THR A CA  1 
ATOM   1656 C  C   . THR A 1 232 ? 111.378 90.128  62.387  1.00 51.81 ? 221  THR A C   1 
ATOM   1657 O  O   . THR A 1 232 ? 111.504 90.181  61.157  1.00 51.81 ? 221  THR A O   1 
ATOM   1658 C  CB  . THR A 1 232 ? 111.451 87.948  63.612  1.00 51.81 ? 221  THR A CB  1 
ATOM   1659 O  OG1 . THR A 1 232 ? 112.330 86.974  64.186  1.00 51.81 ? 221  THR A OG1 1 
ATOM   1660 C  CG2 . THR A 1 232 ? 110.756 87.353  62.404  1.00 51.81 ? 221  THR A CG2 1 
ATOM   1661 N  N   . LEU A 1 233 ? 110.486 90.869  63.043  1.00 52.22 ? 222  LEU A N   1 
ATOM   1662 C  CA  . LEU A 1 233 ? 109.620 91.798  62.330  1.00 52.22 ? 222  LEU A CA  1 
ATOM   1663 C  C   . LEU A 1 233 ? 110.434 92.881  61.640  1.00 52.22 ? 222  LEU A C   1 
ATOM   1664 O  O   . LEU A 1 233 ? 110.122 93.280  60.515  1.00 52.22 ? 222  LEU A O   1 
ATOM   1665 C  CB  . LEU A 1 233 ? 108.617 92.409  63.308  1.00 52.22 ? 222  LEU A CB  1 
ATOM   1666 C  CG  . LEU A 1 233 ? 107.404 93.165  62.768  1.00 52.22 ? 222  LEU A CG  1 
ATOM   1667 C  CD1 . LEU A 1 233 ? 106.793 92.472  61.568  1.00 52.22 ? 222  LEU A CD1 1 
ATOM   1668 C  CD2 . LEU A 1 233 ? 106.375 93.316  63.875  1.00 52.22 ? 222  LEU A CD2 1 
ATOM   1669 N  N   . MET A 1 234 ? 111.483 93.373  62.301  1.00 51.90 ? 223  MET A N   1 
ATOM   1670 C  CA  . MET A 1 234 ? 112.326 94.400  61.699  1.00 51.90 ? 223  MET A CA  1 
ATOM   1671 C  C   . MET A 1 234 ? 113.076 93.859  60.489  1.00 51.90 ? 223  MET A C   1 
ATOM   1672 O  O   . MET A 1 234 ? 113.208 94.552  59.471  1.00 51.90 ? 223  MET A O   1 
ATOM   1673 C  CB  . MET A 1 234 ? 113.308 94.940  62.736  1.00 51.90 ? 223  MET A CB  1 
ATOM   1674 C  CG  . MET A 1 234 ? 112.735 95.996  63.671  1.00 51.90 ? 223  MET A CG  1 
ATOM   1675 S  SD  . MET A 1 234 ? 112.038 97.434  62.845  1.00 51.90 ? 223  MET A SD  1 
ATOM   1676 C  CE  . MET A 1 234 ? 110.307 96.978  62.790  1.00 51.90 ? 223  MET A CE  1 
ATOM   1677 N  N   . LEU A 1 235 ? 113.582 92.627  60.577  1.00 53.88 ? 224  LEU A N   1 
ATOM   1678 C  CA  . LEU A 1 235 ? 114.237 92.027  59.418  1.00 53.88 ? 224  LEU A CA  1 
ATOM   1679 C  C   . LEU A 1 235 ? 113.263 91.855  58.261  1.00 53.88 ? 224  LEU A C   1 
ATOM   1680 O  O   . LEU A 1 235 ? 113.612 92.121  57.107  1.00 53.88 ? 224  LEU A O   1 
ATOM   1681 C  CB  . LEU A 1 235 ? 114.864 90.689  59.796  1.00 53.88 ? 224  LEU A CB  1 
ATOM   1682 C  CG  . LEU A 1 235 ? 115.877 90.759  60.936  1.00 53.88 ? 224  LEU A CG  1 
ATOM   1683 C  CD1 . LEU A 1 235 ? 116.129 89.387  61.522  1.00 53.88 ? 224  LEU A CD1 1 
ATOM   1684 C  CD2 . LEU A 1 235 ? 117.169 91.355  60.424  1.00 53.88 ? 224  LEU A CD2 1 
ATOM   1685 N  N   . LEU A 1 236 ? 112.036 91.417  58.543  1.00 53.73 ? 225  LEU A N   1 
ATOM   1686 C  CA  . LEU A 1 236 ? 111.044 91.313  57.477  1.00 53.73 ? 225  LEU A CA  1 
ATOM   1687 C  C   . LEU A 1 236 ? 110.747 92.680  56.869  1.00 53.73 ? 225  LEU A C   1 
ATOM   1688 O  O   . LEU A 1 236 ? 110.638 92.817  55.643  1.00 53.73 ? 225  LEU A O   1 
ATOM   1689 C  CB  . LEU A 1 236 ? 109.762 90.679  58.011  1.00 53.73 ? 225  LEU A CB  1 
ATOM   1690 C  CG  . LEU A 1 236 ? 109.849 89.223  58.460  1.00 53.73 ? 225  LEU A CG  1 
ATOM   1691 C  CD1 . LEU A 1 236 ? 108.532 88.795  59.074  1.00 53.73 ? 225  LEU A CD1 1 
ATOM   1692 C  CD2 . LEU A 1 236 ? 110.224 88.318  57.302  1.00 53.73 ? 225  LEU A CD2 1 
ATOM   1693 N  N   . ALA A 1 237 ? 110.613 93.704  57.713  1.00 54.14 ? 226  ALA A N   1 
ATOM   1694 C  CA  . ALA A 1 237 ? 110.339 95.046  57.216  1.00 54.14 ? 226  ALA A CA  1 
ATOM   1695 C  C   . ALA A 1 237 ? 111.450 95.525  56.295  1.00 54.14 ? 226  ALA A C   1 
ATOM   1696 O  O   . ALA A 1 237 ? 111.184 96.134  55.253  1.00 54.14 ? 226  ALA A O   1 
ATOM   1697 C  CB  . ALA A 1 237 ? 110.160 96.010  58.387  1.00 54.14 ? 226  ALA A CB  1 
ATOM   1698 N  N   . LEU A 1 238 ? 112.705 95.270  56.665  1.00 55.46 ? 227  LEU A N   1 
ATOM   1699 C  CA  . LEU A 1 238 ? 113.804 95.615  55.770  1.00 55.46 ? 227  LEU A CA  1 
ATOM   1700 C  C   . LEU A 1 238 ? 113.748 94.783  54.495  1.00 55.46 ? 227  LEU A C   1 
ATOM   1701 O  O   . LEU A 1 238 ? 114.112 95.263  53.417  1.00 55.46 ? 227  LEU A O   1 
ATOM   1702 C  CB  . LEU A 1 238 ? 115.148 95.431  56.474  1.00 55.46 ? 227  LEU A CB  1 
ATOM   1703 C  CG  . LEU A 1 238 ? 116.390 95.560  55.584  1.00 55.46 ? 227  LEU A CG  1 
ATOM   1704 C  CD1 . LEU A 1 238 ? 116.660 97.012  55.236  1.00 55.46 ? 227  LEU A CD1 1 
ATOM   1705 C  CD2 . LEU A 1 238 ? 117.590 94.954  56.275  1.00 55.46 ? 227  LEU A CD2 1 
ATOM   1706 N  N   . GLU A 1 239 ? 113.317 93.523  54.602  1.00 56.82 ? 228  GLU A N   1 
ATOM   1707 C  CA  . GLU A 1 239 ? 113.134 92.709  53.406  1.00 56.82 ? 228  GLU A CA  1 
ATOM   1708 C  C   . GLU A 1 239 ? 112.146 93.360  52.452  1.00 56.82 ? 228  GLU A C   1 
ATOM   1709 O  O   . GLU A 1 239 ? 112.314 93.278  51.231  1.00 56.82 ? 228  GLU A O   1 
ATOM   1710 C  CB  . GLU A 1 239 ? 112.660 91.307  53.785  1.00 56.82 ? 228  GLU A CB  1 
ATOM   1711 N  N   . ALA A 1 240 ? 111.114 94.004  52.987  1.00 57.25 ? 229  ALA A N   1 
ATOM   1712 C  CA  . ALA A 1 240 ? 110.268 94.876  52.185  1.00 57.25 ? 229  ALA A CA  1 
ATOM   1713 C  C   . ALA A 1 240 ? 111.036 96.171  51.927  1.00 57.25 ? 229  ALA A C   1 
ATOM   1714 O  O   . ALA A 1 240 ? 112.246 96.254  52.146  1.00 57.25 ? 229  ALA A O   1 
ATOM   1715 C  CB  . ALA A 1 240 ? 108.933 95.116  52.885  1.00 57.25 ? 229  ALA A CB  1 
ATOM   1716 N  N   . GLY A 1 241 ? 110.349 97.201  51.445  1.00 59.94 ? 230  GLY A N   1 
ATOM   1717 C  CA  . GLY A 1 241 ? 110.999 98.470  51.182  1.00 59.94 ? 230  GLY A CA  1 
ATOM   1718 C  C   . GLY A 1 241 ? 110.729 99.502  52.256  1.00 59.94 ? 230  GLY A C   1 
ATOM   1719 O  O   . GLY A 1 241 ? 110.605 100.694 51.960  1.00 59.94 ? 230  GLY A O   1 
ATOM   1720 N  N   . LEU A 1 242 ? 110.632 99.060  53.509  1.00 57.64 ? 231  LEU A N   1 
ATOM   1721 C  CA  . LEU A 1 242 ? 110.161 99.920  54.594  1.00 57.64 ? 231  LEU A CA  1 
ATOM   1722 C  C   . LEU A 1 242 ? 111.357 100.592 55.271  1.00 57.64 ? 231  LEU A C   1 
ATOM   1723 O  O   . LEU A 1 242 ? 111.750 100.274 56.393  1.00 57.64 ? 231  LEU A O   1 
ATOM   1724 C  CB  . LEU A 1 242 ? 109.340 99.110  55.586  1.00 57.64 ? 231  LEU A CB  1 
ATOM   1725 C  CG  . LEU A 1 242 ? 108.037 98.547  55.012  1.00 57.64 ? 231  LEU A CG  1 
ATOM   1726 C  CD1 . LEU A 1 242 ? 107.257 97.780  56.079  1.00 57.64 ? 231  LEU A CD1 1 
ATOM   1727 C  CD2 . LEU A 1 242 ? 107.185 99.612  54.348  1.00 57.64 ? 231  LEU A CD2 1 
ATOM   1728 N  N   . CYS A 1 243 ? 111.930 101.556 54.557  1.00 64.76 ? 232  CYS A N   1 
ATOM   1729 C  CA  . CYS A 1 243 ? 113.131 102.235 55.013  1.00 64.76 ? 232  CYS A CA  1 
ATOM   1730 C  C   . CYS A 1 243 ? 112.806 103.205 56.147  1.00 64.76 ? 232  CYS A C   1 
ATOM   1731 O  O   . CYS A 1 243 ? 111.645 103.496 56.444  1.00 64.76 ? 232  CYS A O   1 
ATOM   1732 C  CB  . CYS A 1 243 ? 113.789 102.980 53.854  1.00 64.76 ? 232  CYS A CB  1 
ATOM   1733 S  SG  . CYS A 1 243 ? 115.544 103.341 54.095  1.00 64.76 ? 232  CYS A SG  1 
ATOM   1734 N  N   . GLY A 1 244 ? 113.861 103.713 56.783  1.00 62.97 ? 233  GLY A N   1 
ATOM   1735 C  CA  . GLY A 1 244 ? 113.705 104.669 57.861  1.00 62.97 ? 233  GLY A CA  1 
ATOM   1736 C  C   . GLY A 1 244 ? 113.357 106.071 57.423  1.00 62.97 ? 233  GLY A C   1 
ATOM   1737 O  O   . GLY A 1 244 ? 112.945 106.883 58.256  1.00 62.97 ? 233  GLY A O   1 
ATOM   1738 N  N   . GLU A 1 245 ? 113.508 106.376 56.135  1.00 63.30 ? 234  GLU A N   1 
ATOM   1739 C  CA  . GLU A 1 245 ? 113.057 107.657 55.612  1.00 63.30 ? 234  GLU A CA  1 
ATOM   1740 C  C   . GLU A 1 245 ? 111.541 107.784 55.629  1.00 63.30 ? 234  GLU A C   1 
ATOM   1741 O  O   . GLU A 1 245 ? 111.027 108.882 55.395  1.00 63.30 ? 234  GLU A O   1 
ATOM   1742 C  CB  . GLU A 1 245 ? 113.576 107.852 54.188  1.00 63.30 ? 234  GLU A CB  1 
ATOM   1743 N  N   . ASP A 1 246 ? 110.821 106.694 55.889  1.00 61.63 ? 235  ASP A N   1 
ATOM   1744 C  CA  . ASP A 1 246 ? 109.365 106.701 55.907  1.00 61.63 ? 235  ASP A CA  1 
ATOM   1745 C  C   . ASP A 1 246 ? 108.788 106.400 57.281  1.00 61.63 ? 235  ASP A C   1 
ATOM   1746 O  O   . ASP A 1 246 ? 107.981 107.186 57.787  1.00 61.63 ? 235  ASP A O   1 
ATOM   1747 C  CB  . ASP A 1 246 ? 108.829 105.686 54.886  1.00 61.63 ? 235  ASP A CB  1 
ATOM   1748 N  N   . TYR A 1 247 ? 109.096 105.253 57.891  1.00 58.40 ? 236  TYR A N   1 
ATOM   1749 C  CA  . TYR A 1 247 ? 108.473 104.787 59.162  1.00 58.40 ? 236  TYR A CA  1 
ATOM   1750 C  C   . TYR A 1 247 ? 109.400 104.999 60.340  1.00 58.40 ? 236  TYR A C   1 
ATOM   1751 O  O   . TYR A 1 247 ? 110.581 105.235 60.161  1.00 58.40 ? 236  TYR A O   1 
ATOM   1752 C  CB  . TYR A 1 247 ? 108.170 103.278 59.144  1.00 58.40 ? 236  TYR A CB  1 
ATOM   1753 C  CG  . TYR A 1 247 ? 107.146 102.890 58.138  1.00 58.40 ? 236  TYR A CG  1 
ATOM   1754 C  CD1 . TYR A 1 247 ? 105.840 102.951 58.515  1.00 58.40 ? 236  TYR A CD1 1 
ATOM   1755 C  CD2 . TYR A 1 247 ? 107.462 102.451 56.871  1.00 58.40 ? 236  TYR A CD2 1 
ATOM   1756 C  CE1 . TYR A 1 247 ? 104.832 102.524 57.701  1.00 58.40 ? 236  TYR A CE1 1 
ATOM   1757 C  CE2 . TYR A 1 247 ? 106.462 102.067 56.004  1.00 58.40 ? 236  TYR A CE2 1 
ATOM   1758 C  CZ  . TYR A 1 247 ? 105.150 102.121 56.433  1.00 58.40 ? 236  TYR A CZ  1 
ATOM   1759 O  OH  . TYR A 1 247 ? 104.115 101.810 55.640  1.00 58.40 ? 236  TYR A OH  1 
ATOM   1760 N  N   . VAL A 1 248 ? 108.819 104.938 61.523  1.00 51.34 ? 237  VAL A N   1 
ATOM   1761 C  CA  . VAL A 1 248 ? 109.559 104.857 62.776  1.00 51.34 ? 237  VAL A CA  1 
ATOM   1762 C  C   . VAL A 1 248 ? 108.848 103.839 63.653  1.00 51.34 ? 237  VAL A C   1 
ATOM   1763 O  O   . VAL A 1 248 ? 107.649 103.974 63.912  1.00 51.34 ? 237  VAL A O   1 
ATOM   1764 C  CB  . VAL A 1 248 ? 109.662 106.215 63.490  1.00 51.34 ? 237  VAL A CB  1 
ATOM   1765 C  CG1 . VAL A 1 248 ? 108.290 106.739 63.846  1.00 51.34 ? 237  VAL A CG1 1 
ATOM   1766 C  CG2 . VAL A 1 248 ? 110.526 106.093 64.731  1.00 51.34 ? 237  VAL A CG2 1 
ATOM   1767 N  N   . PHE A 1 249 ? 109.572 102.812 64.092  1.00 48.82 ? 238  PHE A N   1 
ATOM   1768 C  CA  . PHE A 1 249 ? 109.022 101.761 64.940  1.00 48.82 ? 238  PHE A CA  1 
ATOM   1769 C  C   . PHE A 1 249 ? 109.525 101.957 66.360  1.00 48.82 ? 238  PHE A C   1 
ATOM   1770 O  O   . PHE A 1 249 ? 110.737 101.954 66.597  1.00 48.82 ? 238  PHE A O   1 
ATOM   1771 C  CB  . PHE A 1 249 ? 109.411 100.369 64.447  1.00 48.82 ? 238  PHE A CB  1 
ATOM   1772 C  CG  . PHE A 1 249 ? 109.198 100.153 62.982  1.00 48.82 ? 238  PHE A CG  1 
ATOM   1773 C  CD1 . PHE A 1 249 ? 110.187 100.468 62.071  1.00 48.82 ? 238  PHE A CD1 1 
ATOM   1774 C  CD2 . PHE A 1 249 ? 108.017 99.611  62.517  1.00 48.82 ? 238  PHE A CD2 1 
ATOM   1775 C  CE1 . PHE A 1 249 ? 109.996 100.260 60.727  1.00 48.82 ? 238  PHE A CE1 1 
ATOM   1776 C  CE2 . PHE A 1 249 ? 107.820 99.403  61.175  1.00 48.82 ? 238  PHE A CE2 1 
ATOM   1777 C  CZ  . PHE A 1 249 ? 108.812 99.725  60.279  1.00 48.82 ? 238  PHE A CZ  1 
ATOM   1778 N  N   . PHE A 1 250 ? 108.599 102.104 67.297  1.00 43.66 ? 239  PHE A N   1 
ATOM   1779 C  CA  . PHE A 1 250 ? 108.921 102.248 68.706  1.00 43.66 ? 239  PHE A CA  1 
ATOM   1780 C  C   . PHE A 1 250 ? 108.637 100.924 69.397  1.00 43.66 ? 239  PHE A C   1 
ATOM   1781 O  O   . PHE A 1 250 ? 107.489 100.474 69.429  1.00 43.66 ? 239  PHE A O   1 
ATOM   1782 C  CB  . PHE A 1 250 ? 108.095 103.366 69.335  1.00 43.66 ? 239  PHE A CB  1 
ATOM   1783 C  CG  . PHE A 1 250 ? 108.530 104.743 68.937  1.00 43.66 ? 239  PHE A CG  1 
ATOM   1784 C  CD1 . PHE A 1 250 ? 109.614 105.342 69.542  1.00 43.66 ? 239  PHE A CD1 1 
ATOM   1785 C  CD2 . PHE A 1 250 ? 107.850 105.441 67.962  1.00 43.66 ? 239  PHE A CD2 1 
ATOM   1786 C  CE1 . PHE A 1 250 ? 110.010 106.605 69.179  1.00 43.66 ? 239  PHE A CE1 1 
ATOM   1787 C  CE2 . PHE A 1 250 ? 108.245 106.702 67.596  1.00 43.66 ? 239  PHE A CE2 1 
ATOM   1788 C  CZ  . PHE A 1 250 ? 109.326 107.284 68.204  1.00 43.66 ? 239  PHE A CZ  1 
ATOM   1789 N  N   . HIS A 1 251 ? 109.674 100.310 69.955  1.00 39.47 ? 240  HIS A N   1 
ATOM   1790 C  CA  . HIS A 1 251 ? 109.527 99.063  70.696  1.00 39.47 ? 240  HIS A CA  1 
ATOM   1791 C  C   . HIS A 1 251 ? 109.298 99.401  72.163  1.00 39.47 ? 240  HIS A C   1 
ATOM   1792 O  O   . HIS A 1 251 ? 110.182 99.953  72.824  1.00 39.47 ? 240  HIS A O   1 
ATOM   1793 C  CB  . HIS A 1 251 ? 110.759 98.180  70.527  1.00 39.47 ? 240  HIS A CB  1 
ATOM   1794 C  CG  . HIS A 1 251 ? 110.596 96.803  71.093  1.00 39.47 ? 240  HIS A CG  1 
ATOM   1795 N  ND1 . HIS A 1 251 ? 111.666 96.010  71.440  1.00 39.47 ? 240  HIS A ND1 1 
ATOM   1796 C  CD2 . HIS A 1 251 ? 109.486 96.080  71.371  1.00 39.47 ? 240  HIS A CD2 1 
ATOM   1797 C  CE1 . HIS A 1 251 ? 111.223 94.857  71.907  1.00 39.47 ? 240  HIS A CE1 1 
ATOM   1798 N  NE2 . HIS A 1 251 ? 109.904 94.875  71.876  1.00 39.47 ? 240  HIS A NE2 1 
ATOM   1799 N  N   . LEU A 1 252 ? 108.115 99.068  72.671  1.00 37.40 ? 241  LEU A N   1 
ATOM   1800 C  CA  . LEU A 1 252 ? 107.788 99.286  74.077  1.00 37.40 ? 241  LEU A CA  1 
ATOM   1801 C  C   . LEU A 1 252 ? 108.342 98.115  74.873  1.00 37.40 ? 241  LEU A C   1 
ATOM   1802 O  O   . LEU A 1 252 ? 107.691 97.085  75.043  1.00 37.40 ? 241  LEU A O   1 
ATOM   1803 C  CB  . LEU A 1 252 ? 106.285 99.429  74.274  1.00 37.40 ? 241  LEU A CB  1 
ATOM   1804 C  CG  . LEU A 1 252 ? 105.564 100.428 73.374  1.00 37.40 ? 241  LEU A CG  1 
ATOM   1805 C  CD1 . LEU A 1 252 ? 104.067 100.317 73.575  1.00 37.40 ? 241  LEU A CD1 1 
ATOM   1806 C  CD2 . LEU A 1 252 ? 106.039 101.838 73.646  1.00 37.40 ? 241  LEU A CD2 1 
ATOM   1807 N  N   . ASP A 1 253 ? 109.564 98.279  75.370  1.00 37.65 ? 242  ASP A N   1 
ATOM   1808 C  CA  . ASP A 1 253 ? 110.256 97.262  76.157  1.00 37.65 ? 242  ASP A CA  1 
ATOM   1809 C  C   . ASP A 1 253 ? 110.507 97.868  77.532  1.00 37.65 ? 242  ASP A C   1 
ATOM   1810 O  O   . ASP A 1 253 ? 111.593 98.381  77.806  1.00 37.65 ? 242  ASP A O   1 
ATOM   1811 C  CB  . ASP A 1 253 ? 111.552 96.845  75.474  1.00 37.65 ? 242  ASP A CB  1 
ATOM   1812 C  CG  . ASP A 1 253 ? 111.972 95.436  75.820  1.00 37.65 ? 242  ASP A CG  1 
ATOM   1813 O  OD1 . ASP A 1 253 ? 111.110 94.629  76.221  1.00 37.65 ? 242  ASP A OD1 1 
ATOM   1814 O  OD2 . ASP A 1 253 ? 113.173 95.134  75.688  1.00 37.65 ? 242  ASP A OD2 1 
ATOM   1815 N  N   . ILE A 1 254 ? 109.506 97.787  78.408  1.00 31.55 ? 243  ILE A N   1 
ATOM   1816 C  CA  . ILE A 1 254 ? 109.541 98.579  79.634  1.00 31.55 ? 243  ILE A CA  1 
ATOM   1817 C  C   . ILE A 1 254 ? 110.708 98.162  80.515  1.00 31.55 ? 243  ILE A C   1 
ATOM   1818 O  O   . ILE A 1 254 ? 111.386 99.008  81.107  1.00 31.55 ? 243  ILE A O   1 
ATOM   1819 C  CB  . ILE A 1 254 ? 108.197 98.478  80.379  1.00 31.55 ? 243  ILE A CB  1 
ATOM   1820 C  CG1 . ILE A 1 254 ? 107.883 97.028  80.744  1.00 31.55 ? 243  ILE A CG1 1 
ATOM   1821 C  CG2 . ILE A 1 254 ? 107.088 99.072  79.534  1.00 31.55 ? 243  ILE A CG2 1 
ATOM   1822 C  CD1 . ILE A 1 254 ? 106.538 96.843  81.388  1.00 31.55 ? 243  ILE A CD1 1 
ATOM   1823 N  N   . PHE A 1 255 ? 110.969 96.862  80.617  1.00 29.86 ? 244  PHE A N   1 
ATOM   1824 C  CA  . PHE A 1 255 ? 111.991 96.348  81.517  1.00 29.86 ? 244  PHE A CA  1 
ATOM   1825 C  C   . PHE A 1 255 ? 113.322 96.106  80.822  1.00 29.86 ? 244  PHE A C   1 
ATOM   1826 O  O   . PHE A 1 255 ? 114.211 95.486  81.409  1.00 29.86 ? 244  PHE A O   1 
ATOM   1827 C  CB  . PHE A 1 255 ? 111.508 95.054  82.176  1.00 29.86 ? 244  PHE A CB  1 
ATOM   1828 C  CG  . PHE A 1 255 ? 110.547 95.268  83.314  1.00 29.86 ? 244  PHE A CG  1 
ATOM   1829 C  CD1 . PHE A 1 255 ? 110.836 96.159  84.331  1.00 29.86 ? 244  PHE A CD1 1 
ATOM   1830 C  CD2 . PHE A 1 255 ? 109.357 94.571  83.366  1.00 29.86 ? 244  PHE A CD2 1 
ATOM   1831 C  CE1 . PHE A 1 255 ? 109.957 96.351  85.367  1.00 29.86 ? 244  PHE A CE1 1 
ATOM   1832 C  CE2 . PHE A 1 255 ? 108.478 94.762  84.403  1.00 29.86 ? 244  PHE A CE2 1 
ATOM   1833 C  CZ  . PHE A 1 255 ? 108.779 95.651  85.404  1.00 29.86 ? 244  PHE A CZ  1 
ATOM   1834 N  N   . GLY A 1 256 ? 113.478 96.571  79.587  1.00 37.84 ? 245  GLY A N   1 
ATOM   1835 C  CA  . GLY A 1 256 ? 114.757 96.452  78.907  1.00 37.84 ? 245  GLY A CA  1 
ATOM   1836 C  C   . GLY A 1 256 ? 115.217 95.026  78.710  1.00 37.84 ? 245  GLY A C   1 
ATOM   1837 O  O   . GLY A 1 256 ? 116.392 94.718  78.938  1.00 37.84 ? 245  GLY A O   1 
ATOM   1838 N  N   . GLN A 1 257 ? 114.312 94.141  78.290  1.00 41.90 ? 246  GLN A N   1 
ATOM   1839 C  CA  . GLN A 1 257 ? 114.689 92.752  78.061  1.00 41.90 ? 246  GLN A CA  1 
ATOM   1840 C  C   . GLN A 1 257 ? 115.640 92.617  76.882  1.00 41.90 ? 246  GLN A C   1 
ATOM   1841 O  O   . GLN A 1 257 ? 116.443 91.680  76.839  1.00 41.90 ? 246  GLN A O   1 
ATOM   1842 C  CB  . GLN A 1 257 ? 113.440 91.907  77.824  1.00 41.90 ? 246  GLN A CB  1 
ATOM   1843 C  CG  . GLN A 1 257 ? 112.510 91.805  79.016  1.00 41.90 ? 246  GLN A CG  1 
ATOM   1844 C  CD  . GLN A 1 257 ? 113.159 91.131  80.202  1.00 41.90 ? 246  GLN A CD  1 
ATOM   1845 O  OE1 . GLN A 1 257 ? 113.459 91.771  81.211  1.00 41.90 ? 246  GLN A OE1 1 
ATOM   1846 N  NE2 . GLN A 1 257 ? 113.392 89.830  80.085  1.00 41.90 ? 246  GLN A NE2 1 
ATOM   1847 N  N   . SER A 1 258 ? 115.564 93.532  75.922  1.00 43.36 ? 247  SER A N   1 
ATOM   1848 C  CA  . SER A 1 258 ? 116.380 93.475  74.718  1.00 43.36 ? 247  SER A CA  1 
ATOM   1849 C  C   . SER A 1 258 ? 117.700 94.215  74.861  1.00 43.36 ? 247  SER A C   1 
ATOM   1850 O  O   . SER A 1 258 ? 118.477 94.251  73.903  1.00 43.36 ? 247  SER A O   1 
ATOM   1851 C  CB  . SER A 1 258 ? 115.602 94.055  73.535  1.00 43.36 ? 247  SER A CB  1 
ATOM   1852 O  OG  . SER A 1 258 ? 115.199 95.386  73.796  1.00 43.36 ? 247  SER A OG  1 
ATOM   1853 N  N   . LEU A 1 259 ? 117.972 94.803  76.023  1.00 44.32 ? 248  LEU A N   1 
ATOM   1854 C  CA  . LEU A 1 259 ? 119.165 95.611  76.242  1.00 44.32 ? 248  LEU A CA  1 
ATOM   1855 C  C   . LEU A 1 259 ? 119.995 95.071  77.400  1.00 44.32 ? 248  LEU A C   1 
ATOM   1856 O  O   . LEU A 1 259 ? 120.702 95.825  78.068  1.00 44.32 ? 248  LEU A O   1 
ATOM   1857 C  CB  . LEU A 1 259 ? 118.781 97.065  76.502  1.00 44.32 ? 248  LEU A CB  1 
ATOM   1858 C  CG  . LEU A 1 259 ? 118.086 97.805  75.363  1.00 44.32 ? 248  LEU A CG  1 
ATOM   1859 C  CD1 . LEU A 1 259 ? 117.347 99.000  75.905  1.00 44.32 ? 248  LEU A CD1 1 
ATOM   1860 C  CD2 . LEU A 1 259 ? 119.092 98.239  74.323  1.00 44.32 ? 248  LEU A CD2 1 
ATOM   1861 N  N   . GLN A 1 260 ? 119.919 93.765  77.647  1.00 46.89 ? 249  GLN A N   1 
ATOM   1862 C  CA  . GLN A 1 260 ? 120.619 93.143  78.769  1.00 46.89 ? 249  GLN A CA  1 
ATOM   1863 C  C   . GLN A 1 260 ? 120.277 93.847  80.078  1.00 46.89 ? 249  GLN A C   1 
ATOM   1864 O  O   . GLN A 1 260 ? 121.142 94.111  80.915  1.00 46.89 ? 249  GLN A O   1 
ATOM   1865 C  CB  . GLN A 1 260 ? 122.130 93.133  78.535  1.00 46.89 ? 249  GLN A CB  1 
ATOM   1866 C  CG  . GLN A 1 260 ? 122.596 92.098  77.528  1.00 46.89 ? 249  GLN A CG  1 
ATOM   1867 C  CD  . GLN A 1 260 ? 122.722 92.661  76.130  1.00 46.89 ? 249  GLN A CD  1 
ATOM   1868 O  OE1 . GLN A 1 260 ? 123.508 93.575  75.888  1.00 46.89 ? 249  GLN A OE1 1 
ATOM   1869 N  NE2 . GLN A 1 260 ? 121.950 92.115  75.200  1.00 46.89 ? 249  GLN A NE2 1 
ATOM   1870 N  N   . GLY A 1 261 ? 118.994 94.163  80.253  1.00 41.50 ? 250  GLY A N   1 
ATOM   1871 C  CA  . GLY A 1 261 ? 118.490 94.808  81.438  1.00 41.50 ? 250  GLY A CA  1 
ATOM   1872 C  C   . GLY A 1 261 ? 118.301 96.305  81.299  1.00 41.50 ? 250  GLY A C   1 
ATOM   1873 O  O   . GLY A 1 261 ? 117.461 96.879  81.998  1.00 41.50 ? 250  GLY A O   1 
ATOM   1874 N  N   . GLY A 1 262 ? 119.061 96.950  80.420  1.00 43.64 ? 251  GLY A N   1 
ATOM   1875 C  CA  . GLY A 1 262 ? 118.885 98.364  80.168  1.00 43.64 ? 251  GLY A CA  1 
ATOM   1876 C  C   . GLY A 1 262 ? 119.412 99.284  81.243  1.00 43.64 ? 251  GLY A C   1 
ATOM   1877 O  O   . GLY A 1 262 ? 119.086 100.476 81.228  1.00 43.64 ? 251  GLY A O   1 
ATOM   1878 N  N   . GLN A 1 263 ? 120.217 98.781  82.172  1.00 45.54 ? 252  GLN A N   1 
ATOM   1879 C  CA  . GLN A 1 263 ? 120.761 99.578  83.260  1.00 45.54 ? 252  GLN A CA  1 
ATOM   1880 C  C   . GLN A 1 263 ? 122.270 99.707  83.108  1.00 45.54 ? 252  GLN A C   1 
ATOM   1881 O  O   . GLN A 1 263 ? 122.956 98.733  82.786  1.00 45.54 ? 252  GLN A O   1 
ATOM   1882 C  CB  . GLN A 1 263 ? 120.424 98.952  84.615  1.00 45.54 ? 252  GLN A CB  1 
ATOM   1883 C  CG  . GLN A 1 263 ? 121.445 99.228  85.704  1.00 45.54 ? 252  GLN A CG  1 
ATOM   1884 C  CD  . GLN A 1 263 ? 120.976 98.768  87.061  1.00 45.54 ? 252  GLN A CD  1 
ATOM   1885 O  OE1 . GLN A 1 263 ? 119.813 98.946  87.420  1.00 45.54 ? 252  GLN A OE1 1 
ATOM   1886 N  NE2 . GLN A 1 263 ? 121.877 98.168  87.825  1.00 45.54 ? 252  GLN A NE2 1 
ATOM   1887 N  N   . GLY A 1 264 ? 122.779 100.911 83.342  1.00 51.89 ? 253  GLY A N   1 
ATOM   1888 C  CA  . GLY A 1 264 ? 124.199 101.161 83.303  1.00 51.89 ? 253  GLY A CA  1 
ATOM   1889 C  C   . GLY A 1 264 ? 124.648 101.737 81.974  1.00 51.89 ? 253  GLY A C   1 
ATOM   1890 O  O   . GLY A 1 264 ? 124.065 101.453 80.924  1.00 51.89 ? 253  GLY A O   1 
ATOM   1891 N  N   . PRO A 1 265 ? 125.698 102.571 81.992  1.00 57.79 ? 254  PRO A N   1 
ATOM   1892 C  CA  . PRO A 1 265 ? 126.207 103.166 80.736  1.00 57.79 ? 254  PRO A CA  1 
ATOM   1893 C  C   . PRO A 1 265 ? 127.166 102.254 79.973  1.00 57.79 ? 254  PRO A C   1 
ATOM   1894 O  O   . PRO A 1 265 ? 128.388 102.362 80.042  1.00 57.79 ? 254  PRO A O   1 
ATOM   1895 C  CB  . PRO A 1 265 ? 126.914 104.431 81.226  1.00 57.79 ? 254  PRO A CB  1 
ATOM   1896 C  CG  . PRO A 1 265 ? 127.326 104.114 82.609  1.00 57.79 ? 254  PRO A CG  1 
ATOM   1897 C  CD  . PRO A 1 265 ? 126.260 103.239 83.177  1.00 57.79 ? 254  PRO A CD  1 
ATOM   1898 N  N   . ALA A 1 266 ? 126.597 101.317 79.218  1.00 55.95 ? 255  ALA A N   1 
ATOM   1899 C  CA  . ALA A 1 266 ? 127.384 100.435 78.375  1.00 55.95 ? 255  ALA A CA  1 
ATOM   1900 C  C   . ALA A 1 266 ? 126.735 100.332 77.001  1.00 55.95 ? 255  ALA A C   1 
ATOM   1901 O  O   . ALA A 1 266 ? 125.503 100.321 76.900  1.00 55.95 ? 255  ALA A O   1 
ATOM   1902 C  CB  . ALA A 1 266 ? 127.507 99.039  78.999  1.00 55.95 ? 255  ALA A CB  1 
ATOM   1903 N  N   . PRO A 1 267 ? 127.525 100.268 75.928  1.00 56.68 ? 256  PRO A N   1 
ATOM   1904 C  CA  . PRO A 1 267 ? 126.925 100.114 74.596  1.00 56.68 ? 256  PRO A CA  1 
ATOM   1905 C  C   . PRO A 1 267 ? 126.147 98.812  74.488  1.00 56.68 ? 256  PRO A C   1 
ATOM   1906 O  O   . PRO A 1 267 ? 126.564 97.771  74.999  1.00 56.68 ? 256  PRO A O   1 
ATOM   1907 C  CB  . PRO A 1 267 ? 128.127 100.132 73.644  1.00 56.68 ? 256  PRO A CB  1 
ATOM   1908 C  CG  . PRO A 1 267 ? 129.304 100.539 74.439  1.00 56.68 ? 256  PRO A CG  1 
ATOM   1909 C  CD  . PRO A 1 267 ? 128.987 100.435 75.886  1.00 56.68 ? 256  PRO A CD  1 
ATOM   1910 N  N   . ARG A 1 268 ? 125.009 98.879  73.801  1.00 51.46 ? 257  ARG A N   1 
ATOM   1911 C  CA  . ARG A 1 268 ? 124.138 97.733  73.601  1.00 51.46 ? 257  ARG A CA  1 
ATOM   1912 C  C   . ARG A 1 268 ? 123.878 97.544  72.116  1.00 51.46 ? 257  ARG A C   1 
ATOM   1913 O  O   . ARG A 1 268 ? 123.811 98.510  71.353  1.00 51.46 ? 257  ARG A O   1 
ATOM   1914 C  CB  . ARG A 1 268 ? 122.800 97.902  74.327  1.00 51.46 ? 257  ARG A CB  1 
ATOM   1915 C  CG  . ARG A 1 268 ? 122.759 97.297  75.708  1.00 51.46 ? 257  ARG A CG  1 
ATOM   1916 C  CD  . ARG A 1 268 ? 123.336 98.235  76.739  1.00 51.46 ? 257  ARG A CD  1 
ATOM   1917 N  NE  . ARG A 1 268 ? 123.046 97.780  78.092  1.00 51.46 ? 257  ARG A NE  1 
ATOM   1918 C  CZ  . ARG A 1 268 ? 123.325 98.473  79.189  1.00 51.46 ? 257  ARG A CZ  1 
ATOM   1919 N  NH1 . ARG A 1 268 ? 123.894 99.666  79.098  1.00 51.46 ? 257  ARG A NH1 1 
ATOM   1920 N  NH2 . ARG A 1 268 ? 123.026 97.977  80.379  1.00 51.46 ? 257  ARG A NH2 1 
ATOM   1921 N  N   . ARG A 1 269 ? 123.729 96.286  71.715  1.00 55.31 ? 258  ARG A N   1 
ATOM   1922 C  CA  . ARG A 1 269 ? 123.423 95.919  70.334  1.00 55.31 ? 258  ARG A CA  1 
ATOM   1923 C  C   . ARG A 1 269 ? 122.265 94.932  70.351  1.00 55.31 ? 258  ARG A C   1 
ATOM   1924 O  O   . ARG A 1 269 ? 122.473 93.713  70.299  1.00 55.31 ? 258  ARG A O   1 
ATOM   1925 C  CB  . ARG A 1 269 ? 124.651 95.337  69.637  1.00 55.31 ? 258  ARG A CB  1 
ATOM   1926 C  CG  . ARG A 1 269 ? 125.668 96.393  69.246  1.00 55.31 ? 258  ARG A CG  1 
ATOM   1927 C  CD  . ARG A 1 269 ? 127.089 95.876  69.264  1.00 55.31 ? 258  ARG A CD  1 
ATOM   1928 N  NE  . ARG A 1 269 ? 128.043 96.964  69.478  1.00 55.31 ? 258  ARG A NE  1 
ATOM   1929 C  CZ  . ARG A 1 269 ? 128.869 97.068  70.518  1.00 55.31 ? 258  ARG A CZ  1 
ATOM   1930 N  NH1 . ARG A 1 269 ? 128.891 96.147  71.475  1.00 55.31 ? 258  ARG A NH1 1 
ATOM   1931 N  NH2 . ARG A 1 269 ? 129.689 98.106  70.599  1.00 55.31 ? 258  ARG A NH2 1 
ATOM   1932 N  N   . PRO A 1 270 ? 121.025 95.423  70.432  1.00 49.75 ? 259  PRO A N   1 
ATOM   1933 C  CA  . PRO A 1 270 ? 119.877 94.507  70.467  1.00 49.75 ? 259  PRO A CA  1 
ATOM   1934 C  C   . PRO A 1 270 ? 119.652 93.767  69.166  1.00 49.75 ? 259  PRO A C   1 
ATOM   1935 O  O   . PRO A 1 270 ? 118.868 92.810  69.149  1.00 49.75 ? 259  PRO A O   1 
ATOM   1936 C  CB  . PRO A 1 270 ? 118.703 95.434  70.790  1.00 49.75 ? 259  PRO A CB  1 
ATOM   1937 C  CG  . PRO A 1 270 ? 119.102 96.741  70.235  1.00 49.75 ? 259  PRO A CG  1 
ATOM   1938 C  CD  . PRO A 1 270 ? 120.597 96.832  70.382  1.00 49.75 ? 259  PRO A CD  1 
ATOM   1939 N  N   . TRP A 1 271 ? 120.299 94.181  68.081  1.00 55.49 ? 260  TRP A N   1 
ATOM   1940 C  CA  . TRP A 1 271 ? 120.200 93.495  66.801  1.00 55.49 ? 260  TRP A CA  1 
ATOM   1941 C  C   . TRP A 1 271 ? 121.268 92.427  66.615  1.00 55.49 ? 260  TRP A C   1 
ATOM   1942 O  O   . TRP A 1 271 ? 121.229 91.703  65.615  1.00 55.49 ? 260  TRP A O   1 
ATOM   1943 C  CB  . TRP A 1 271 ? 120.294 94.506  65.654  1.00 55.49 ? 260  TRP A CB  1 
ATOM   1944 C  CG  . TRP A 1 271 ? 121.446 95.456  65.771  1.00 55.49 ? 260  TRP A CG  1 
ATOM   1945 C  CD1 . TRP A 1 271 ? 121.388 96.764  66.145  1.00 55.49 ? 260  TRP A CD1 1 
ATOM   1946 C  CD2 . TRP A 1 271 ? 122.826 95.175  65.510  1.00 55.49 ? 260  TRP A CD2 1 
ATOM   1947 N  NE1 . TRP A 1 271 ? 122.645 97.316  66.135  1.00 55.49 ? 260  TRP A NE1 1 
ATOM   1948 C  CE2 . TRP A 1 271 ? 123.545 96.360  65.748  1.00 55.49 ? 260  TRP A CE2 1 
ATOM   1949 C  CE3 . TRP A 1 271 ? 123.523 94.036  65.097  1.00 55.49 ? 260  TRP A CE3 1 
ATOM   1950 C  CZ2 . TRP A 1 271 ? 124.925 96.440  65.588  1.00 55.49 ? 260  TRP A CZ2 1 
ATOM   1951 C  CZ3 . TRP A 1 271 ? 124.890 94.117  64.941  1.00 55.49 ? 260  TRP A CZ3 1 
ATOM   1952 C  CH2 . TRP A 1 271 ? 125.577 95.309  65.184  1.00 55.49 ? 260  TRP A CH2 1 
ATOM   1953 N  N   . GLU A 1 272 ? 122.211 92.312  67.544  1.00 58.65 ? 261  GLU A N   1 
ATOM   1954 C  CA  . GLU A 1 272 ? 123.301 91.348  67.449  1.00 58.65 ? 261  GLU A CA  1 
ATOM   1955 C  C   . GLU A 1 272 ? 122.863 90.054  68.121  1.00 58.65 ? 261  GLU A C   1 
ATOM   1956 O  O   . GLU A 1 272 ? 122.751 89.992  69.350  1.00 58.65 ? 261  GLU A O   1 
ATOM   1957 C  CB  . GLU A 1 272 ? 124.562 91.908  68.099  1.00 58.65 ? 261  GLU A CB  1 
ATOM   1958 C  CG  . GLU A 1 272 ? 125.690 90.909  68.235  1.00 58.65 ? 261  GLU A CG  1 
ATOM   1959 C  CD  . GLU A 1 272 ? 127.040 91.581  68.366  1.00 58.65 ? 261  GLU A CD  1 
ATOM   1960 O  OE1 . GLU A 1 272 ? 127.394 91.995  69.491  1.00 58.65 ? 261  GLU A OE1 1 
ATOM   1961 O  OE2 . GLU A 1 272 ? 127.746 91.700  67.343  1.00 58.65 ? 261  GLU A OE2 1 
ATOM   1962 N  N   . ARG A 1 273 ? 122.613 89.023  67.317  1.00 58.05 ? 262  ARG A N   1 
ATOM   1963 C  CA  . ARG A 1 273 ? 122.144 87.741  67.818  1.00 58.05 ? 262  ARG A CA  1 
ATOM   1964 C  C   . ARG A 1 273 ? 123.106 86.597  67.529  1.00 58.05 ? 262  ARG A C   1 
ATOM   1965 O  O   . ARG A 1 273 ? 122.800 85.451  67.874  1.00 58.05 ? 262  ARG A O   1 
ATOM   1966 C  CB  . ARG A 1 273 ? 120.769 87.418  67.216  1.00 58.05 ? 262  ARG A CB  1 
ATOM   1967 C  CG  . ARG A 1 273 ? 119.962 86.384  67.990  1.00 58.05 ? 262  ARG A CG  1 
ATOM   1968 C  CD  . ARG A 1 273 ? 119.580 86.871  69.379  1.00 58.05 ? 262  ARG A CD  1 
ATOM   1969 N  NE  . ARG A 1 273 ? 119.242 88.293  69.410  1.00 58.05 ? 262  ARG A NE  1 
ATOM   1970 C  CZ  . ARG A 1 273 ? 118.005 88.782  69.424  1.00 58.05 ? 262  ARG A CZ  1 
ATOM   1971 N  NH1 . ARG A 1 273 ? 116.952 87.975  69.407  1.00 58.05 ? 262  ARG A NH1 1 
ATOM   1972 N  NH2 . ARG A 1 273 ? 117.819 90.093  69.455  1.00 58.05 ? 262  ARG A NH2 1 
ATOM   1973 N  N   . GLY A 1 274 ? 124.253 86.867  66.915  1.00 63.53 ? 263  GLY A N   1 
ATOM   1974 C  CA  . GLY A 1 274 ? 125.175 85.794  66.581  1.00 63.53 ? 263  GLY A CA  1 
ATOM   1975 C  C   . GLY A 1 274 ? 124.565 84.768  65.652  1.00 63.53 ? 263  GLY A C   1 
ATOM   1976 O  O   . GLY A 1 274 ? 124.834 83.568  65.788  1.00 63.53 ? 263  GLY A O   1 
ATOM   1977 N  N   . ASP A 1 275 ? 123.744 85.217  64.706  1.00 66.94 ? 264  ASP A N   1 
ATOM   1978 C  CA  . ASP A 1 275 ? 123.042 84.331  63.790  1.00 66.94 ? 264  ASP A CA  1 
ATOM   1979 C  C   . ASP A 1 275 ? 123.652 84.322  62.395  1.00 66.94 ? 264  ASP A C   1 
ATOM   1980 O  O   . ASP A 1 275 ? 123.351 83.419  61.608  1.00 66.94 ? 264  ASP A O   1 
ATOM   1981 C  CB  . ASP A 1 275 ? 121.570 84.757  63.696  1.00 66.94 ? 264  ASP A CB  1 
ATOM   1982 N  N   . GLY A 1 276 ? 124.509 85.288  62.079  1.00 63.57 ? 265  GLY A N   1 
ATOM   1983 C  CA  . GLY A 1 276 ? 124.929 85.533  60.723  1.00 63.57 ? 265  GLY A CA  1 
ATOM   1984 C  C   . GLY A 1 276 ? 124.025 86.484  59.973  1.00 63.57 ? 265  GLY A C   1 
ATOM   1985 O  O   . GLY A 1 276 ? 124.434 87.033  58.944  1.00 63.57 ? 265  GLY A O   1 
ATOM   1986 N  N   . GLN A 1 277 ? 122.807 86.689  60.468  1.00 60.40 ? 266  GLN A N   1 
ATOM   1987 C  CA  . GLN A 1 277 ? 121.904 87.709  59.951  1.00 60.40 ? 266  GLN A CA  1 
ATOM   1988 C  C   . GLN A 1 277 ? 122.020 88.957  60.824  1.00 60.40 ? 266  GLN A C   1 
ATOM   1989 O  O   . GLN A 1 277 ? 121.098 89.352  61.537  1.00 60.40 ? 266  GLN A O   1 
ATOM   1990 C  CB  . GLN A 1 277 ? 120.475 87.174  59.917  1.00 60.40 ? 266  GLN A CB  1 
ATOM   1991 C  CG  . GLN A 1 277 ? 119.568 87.873  58.926  1.00 60.40 ? 266  GLN A CG  1 
ATOM   1992 C  CD  . GLN A 1 277 ? 118.204 87.227  58.839  1.00 60.40 ? 266  GLN A CD  1 
ATOM   1993 O  OE1 . GLN A 1 277 ? 117.877 86.337  59.621  1.00 60.40 ? 266  GLN A OE1 1 
ATOM   1994 N  NE2 . GLN A 1 277 ? 117.398 87.673  57.887  1.00 60.40 ? 266  GLN A NE2 1 
ATOM   1995 N  N   . ASP A 1 278 ? 123.197 89.573  60.762  1.00 59.91 ? 267  ASP A N   1 
ATOM   1996 C  CA  . ASP A 1 278 ? 123.501 90.761  61.551  1.00 59.91 ? 267  ASP A CA  1 
ATOM   1997 C  C   . ASP A 1 278 ? 123.790 91.986  60.705  1.00 59.91 ? 267  ASP A C   1 
ATOM   1998 O  O   . ASP A 1 278 ? 123.405 93.093  61.085  1.00 59.91 ? 267  ASP A O   1 
ATOM   1999 C  CB  . ASP A 1 278 ? 124.698 90.498  62.472  1.00 59.91 ? 267  ASP A CB  1 
ATOM   2000 C  CG  . ASP A 1 278 ? 124.346 89.613  63.644  1.00 59.91 ? 267  ASP A CG  1 
ATOM   2001 O  OD1 . ASP A 1 278 ? 123.177 89.639  64.077  1.00 59.91 ? 267  ASP A OD1 1 
ATOM   2002 O  OD2 . ASP A 1 278 ? 125.238 88.894  64.138  1.00 59.91 ? 267  ASP A OD2 1 
ATOM   2003 N  N   . VAL A 1 279 ? 124.467 91.828  59.568  1.00 60.02 ? 268  VAL A N   1 
ATOM   2004 C  CA  . VAL A 1 279 ? 124.663 92.966  58.678  1.00 60.02 ? 268  VAL A CA  1 
ATOM   2005 C  C   . VAL A 1 279 ? 123.314 93.522  58.246  1.00 60.02 ? 268  VAL A C   1 
ATOM   2006 O  O   . VAL A 1 279 ? 123.129 94.739  58.140  1.00 60.02 ? 268  VAL A O   1 
ATOM   2007 C  CB  . VAL A 1 279 ? 125.525 92.560  57.468  1.00 60.02 ? 268  VAL A CB  1 
ATOM   2008 N  N   . SER A 1 280 ? 122.351 92.636  57.992  1.00 58.93 ? 269  SER A N   1 
ATOM   2009 C  CA  . SER A 1 280 ? 121.006 93.079  57.646  1.00 58.93 ? 269  SER A CA  1 
ATOM   2010 C  C   . SER A 1 280 ? 120.263 93.596  58.872  1.00 58.93 ? 269  SER A C   1 
ATOM   2011 O  O   . SER A 1 280 ? 119.481 94.547  58.774  1.00 58.93 ? 269  SER A O   1 
ATOM   2012 C  CB  . SER A 1 280 ? 120.236 91.931  56.997  1.00 58.93 ? 269  SER A CB  1 
ATOM   2013 O  OG  . SER A 1 280 ? 118.919 92.320  56.661  1.00 58.93 ? 269  SER A OG  1 
ATOM   2014 N  N   . ALA A 1 281 ? 120.492 92.981  60.035  1.00 56.49 ? 270  ALA A N   1 
ATOM   2015 C  CA  . ALA A 1 281 ? 119.798 93.406  61.246  1.00 56.49 ? 270  ALA A CA  1 
ATOM   2016 C  C   . ALA A 1 281 ? 120.176 94.829  61.633  1.00 56.49 ? 270  ALA A C   1 
ATOM   2017 O  O   . ALA A 1 281 ? 119.319 95.612  62.054  1.00 56.49 ? 270  ALA A O   1 
ATOM   2018 C  CB  . ALA A 1 281 ? 120.106 92.444  62.389  1.00 56.49 ? 270  ALA A CB  1 
ATOM   2019 N  N   . ARG A 1 282 ? 121.456 95.179  61.506  1.00 57.11 ? 271  ARG A N   1 
ATOM   2020 C  CA  . ARG A 1 282 ? 121.883 96.537  61.829  1.00 57.11 ? 271  ARG A CA  1 
ATOM   2021 C  C   . ARG A 1 282 ? 121.201 97.554  60.924  1.00 57.11 ? 271  ARG A C   1 
ATOM   2022 O  O   . ARG A 1 282 ? 120.765 98.613  61.386  1.00 57.11 ? 271  ARG A O   1 
ATOM   2023 C  CB  . ARG A 1 282 ? 123.403 96.646  61.716  1.00 57.11 ? 271  ARG A CB  1 
ATOM   2024 C  CG  . ARG A 1 282 ? 123.955 98.051  61.902  1.00 57.11 ? 271  ARG A CG  1 
ATOM   2025 C  CD  . ARG A 1 282 ? 125.442 98.091  61.622  1.00 57.11 ? 271  ARG A CD  1 
ATOM   2026 N  NE  . ARG A 1 282 ? 126.008 99.422  61.809  1.00 57.11 ? 271  ARG A NE  1 
ATOM   2027 C  CZ  . ARG A 1 282 ? 127.308 99.673  61.922  1.00 57.11 ? 271  ARG A CZ  1 
ATOM   2028 N  NH1 . ARG A 1 282 ? 128.189 98.683  61.866  1.00 57.11 ? 271  ARG A NH1 1 
ATOM   2029 N  NH2 . ARG A 1 282 ? 127.732 100.918 62.090  1.00 57.11 ? 271  ARG A NH2 1 
ATOM   2030 N  N   . GLN A 1 283 ? 121.103 97.254  59.630  1.00 56.14 ? 272  GLN A N   1 
ATOM   2031 C  CA  . GLN A 1 283 ? 120.448 98.166  58.703  1.00 56.14 ? 272  GLN A CA  1 
ATOM   2032 C  C   . GLN A 1 283 ? 118.948 98.246  58.937  1.00 56.14 ? 272  GLN A C   1 
ATOM   2033 O  O   . GLN A 1 283 ? 118.321 99.225  58.521  1.00 56.14 ? 272  GLN A O   1 
ATOM   2034 C  CB  . GLN A 1 283 ? 120.727 97.742  57.260  1.00 30.00 ? 272  GLN A CB  1 
ATOM   2035 C  CG  . GLN A 1 283 ? 120.185 98.702  56.214  1.00 30.00 ? 272  GLN A CG  1 
ATOM   2036 C  CD  . GLN A 1 283 ? 120.838 100.066 56.278  1.00 30.00 ? 272  GLN A CD  1 
ATOM   2037 O  OE1 . GLN A 1 283 ? 122.053 100.188 56.119  1.00 30.00 ? 272  GLN A OE1 1 
ATOM   2038 N  NE2 . GLN A 1 283 ? 120.034 101.099 56.511  1.00 30.00 ? 272  GLN A NE2 1 
ATOM   2039 N  N   . ALA A 1 284 ? 118.358 97.240  59.578  1.00 53.70 ? 273  ALA A N   1 
ATOM   2040 C  CA  . ALA A 1 284 ? 116.928 97.231  59.846  1.00 53.70 ? 273  ALA A CA  1 
ATOM   2041 C  C   . ALA A 1 284 ? 116.565 97.872  61.177  1.00 53.70 ? 273  ALA A C   1 
ATOM   2042 O  O   . ALA A 1 284 ? 115.381 98.127  61.416  1.00 53.70 ? 273  ALA A O   1 
ATOM   2043 C  CB  . ALA A 1 284 ? 116.395 95.797  59.816  1.00 53.70 ? 273  ALA A CB  1 
ATOM   2044 N  N   . PHE A 1 285 ? 117.540 98.133  62.044  1.00 51.84 ? 274  PHE A N   1 
ATOM   2045 C  CA  . PHE A 1 285 ? 117.301 98.842  63.292  1.00 51.84 ? 274  PHE A CA  1 
ATOM   2046 C  C   . PHE A 1 285 ? 117.640 100.321 63.197  1.00 51.84 ? 274  PHE A C   1 
ATOM   2047 O  O   . PHE A 1 285 ? 117.564 101.026 64.207  1.00 51.84 ? 274  PHE A O   1 
ATOM   2048 C  CB  . PHE A 1 285 ? 118.101 98.203  64.431  1.00 51.84 ? 274  PHE A CB  1 
ATOM   2049 C  CG  . PHE A 1 285 ? 117.329 97.180  65.214  1.00 51.84 ? 274  PHE A CG  1 
ATOM   2050 C  CD1 . PHE A 1 285 ? 117.178 97.306  66.581  1.00 51.84 ? 274  PHE A CD1 1 
ATOM   2051 C  CD2 . PHE A 1 285 ? 116.763 96.088  64.586  1.00 51.84 ? 274  PHE A CD2 1 
ATOM   2052 C  CE1 . PHE A 1 285 ? 116.472 96.368  67.301  1.00 51.84 ? 274  PHE A CE1 1 
ATOM   2053 C  CE2 . PHE A 1 285 ? 116.057 95.150  65.305  1.00 51.84 ? 274  PHE A CE2 1 
ATOM   2054 C  CZ  . PHE A 1 285 ? 115.912 95.291  66.663  1.00 51.84 ? 274  PHE A CZ  1 
ATOM   2055 N  N   . GLN A 1 286 ? 118.014 100.810 62.016  1.00 55.18 ? 275  GLN A N   1 
ATOM   2056 C  CA  . GLN A 1 286 ? 118.231 102.238 61.837  1.00 55.18 ? 275  GLN A CA  1 
ATOM   2057 C  C   . GLN A 1 286 ? 116.928 103.021 61.821  1.00 55.18 ? 275  GLN A C   1 
ATOM   2058 O  O   . GLN A 1 286 ? 116.967 104.255 61.800  1.00 55.18 ? 275  GLN A O   1 
ATOM   2059 C  CB  . GLN A 1 286 ? 119.005 102.495 60.545  1.00 55.18 ? 275  GLN A CB  1 
ATOM   2060 C  CG  . GLN A 1 286 ? 120.371 101.840 60.513  1.00 55.18 ? 275  GLN A CG  1 
ATOM   2061 C  CD  . GLN A 1 286 ? 121.222 102.323 59.360  1.00 55.18 ? 275  GLN A CD  1 
ATOM   2062 O  OE1 . GLN A 1 286 ? 120.758 103.075 58.504  1.00 55.18 ? 275  GLN A OE1 1 
ATOM   2063 N  NE2 . GLN A 1 286 ? 122.477 101.893 59.332  1.00 55.18 ? 275  GLN A NE2 1 
ATOM   2064 N  N   . ALA A 1 287 ? 115.786 102.337 61.818  1.00 53.20 ? 276  ALA A N   1 
ATOM   2065 C  CA  . ALA A 1 287 ? 114.476 102.971 61.843  1.00 53.20 ? 276  ALA A CA  1 
ATOM   2066 C  C   . ALA A 1 287 ? 113.675 102.541 63.067  1.00 53.20 ? 276  ALA A C   1 
ATOM   2067 O  O   . ALA A 1 287 ? 112.445 102.562 63.048  1.00 53.20 ? 276  ALA A O   1 
ATOM   2068 C  CB  . ALA A 1 287 ? 113.705 102.651 60.566  1.00 53.20 ? 276  ALA A CB  1 
ATOM   2069 N  N   . ALA A 1 288 ? 114.361 102.141 64.135  1.00 48.57 ? 277  ALA A N   1 
ATOM   2070 C  CA  . ALA A 1 288 ? 113.712 101.637 65.337  1.00 48.57 ? 277  ALA A CA  1 
ATOM   2071 C  C   . ALA A 1 288 ? 114.284 102.330 66.563  1.00 48.57 ? 277  ALA A C   1 
ATOM   2072 O  O   . ALA A 1 288 ? 115.504 102.446 66.706  1.00 48.57 ? 277  ALA A O   1 
ATOM   2073 C  CB  . ALA A 1 288 ? 113.888 100.123 65.465  1.00 48.57 ? 277  ALA A CB  1 
ATOM   2074 N  N   . LYS A 1 289 ? 113.396 102.782 67.441  1.00 46.34 ? 278  LYS A N   1 
ATOM   2075 C  CA  . LYS A 1 289 ? 113.754 103.344 68.732  1.00 46.34 ? 278  LYS A CA  1 
ATOM   2076 C  C   . LYS A 1 289 ? 113.130 102.481 69.817  1.00 46.34 ? 278  LYS A C   1 
ATOM   2077 O  O   . LYS A 1 289 ? 112.157 101.764 69.573  1.00 46.34 ? 278  LYS A O   1 
ATOM   2078 C  CB  . LYS A 1 289 ? 113.279 104.795 68.869  1.00 46.34 ? 278  LYS A CB  1 
ATOM   2079 C  CG  . LYS A 1 289 ? 113.454 105.650 67.621  1.00 46.34 ? 278  LYS A CG  1 
ATOM   2080 C  CD  . LYS A 1 289 ? 114.713 106.480 67.698  1.00 46.34 ? 278  LYS A CD  1 
ATOM   2081 C  CE  . LYS A 1 289 ? 114.937 107.261 66.418  1.00 46.34 ? 278  LYS A CE  1 
ATOM   2082 N  NZ  . LYS A 1 289 ? 115.535 106.421 65.346  1.00 46.34 ? 278  LYS A NZ  1 
ATOM   2083 N  N   . ILE A 1 290 ? 113.698 102.533 71.020  1.00 41.58 ? 279  ILE A N   1 
ATOM   2084 C  CA  . ILE A 1 290 ? 113.266 101.661 72.110  1.00 41.58 ? 279  ILE A CA  1 
ATOM   2085 C  C   . ILE A 1 290 ? 112.848 102.516 73.298  1.00 41.58 ? 279  ILE A C   1 
ATOM   2086 O  O   . ILE A 1 290 ? 113.586 103.415 73.713  1.00 41.58 ? 279  ILE A O   1 
ATOM   2087 C  CB  . ILE A 1 290 ? 114.368 100.660 72.507  1.00 41.58 ? 279  ILE A CB  1 
ATOM   2088 C  CG1 . ILE A 1 290 ? 114.774 99.818  71.296  1.00 41.58 ? 279  ILE A CG1 1 
ATOM   2089 C  CG2 . ILE A 1 290 ? 113.885 99.748  73.620  1.00 41.58 ? 279  ILE A CG2 1 
ATOM   2090 C  CD1 . ILE A 1 290 ? 116.010 98.996  71.508  1.00 41.58 ? 279  ILE A CD1 1 
ATOM   2091 N  N   . ILE A 1 291 ? 111.669 102.231 73.846  1.00 38.54 ? 280  ILE A N   1 
ATOM   2092 C  CA  . ILE A 1 291 ? 111.112 102.958 74.981  1.00 38.54 ? 280  ILE A CA  1 
ATOM   2093 C  C   . ILE A 1 291 ? 111.177 102.042 76.191  1.00 38.54 ? 280  ILE A C   1 
ATOM   2094 O  O   . ILE A 1 291 ? 110.647 100.926 76.154  1.00 38.54 ? 280  ILE A O   1 
ATOM   2095 C  CB  . ILE A 1 291 ? 109.665 103.399 74.714  1.00 38.54 ? 280  ILE A CB  1 
ATOM   2096 C  CG1 . ILE A 1 291 ? 109.608 104.417 73.576  1.00 38.54 ? 280  ILE A CG1 1 
ATOM   2097 C  CG2 . ILE A 1 291 ? 109.054 103.983 75.966  1.00 38.54 ? 280  ILE A CG2 1 
ATOM   2098 C  CD1 . ILE A 1 291 ? 108.270 104.481 72.892  1.00 38.54 ? 280  ILE A CD1 1 
ATOM   2099 N  N   . THR A 1 292 ? 111.812 102.504 77.267  1.00 35.70 ? 281  THR A N   1 
ATOM   2100 C  CA  . THR A 1 292 ? 111.945 101.704 78.477  1.00 35.70 ? 281  THR A CA  1 
ATOM   2101 C  C   . THR A 1 292 ? 111.645 102.563 79.696  1.00 35.70 ? 281  THR A C   1 
ATOM   2102 O  O   . THR A 1 292 ? 111.533 103.788 79.610  1.00 35.70 ? 281  THR A O   1 
ATOM   2103 C  CB  . THR A 1 292 ? 113.351 101.103 78.613  1.00 35.70 ? 281  THR A CB  1 
ATOM   2104 O  OG1 . THR A 1 292 ? 114.213 102.036 79.270  1.00 35.70 ? 281  THR A OG1 1 
ATOM   2105 C  CG2 . THR A 1 292 ? 113.934 100.787 77.259  1.00 35.70 ? 281  THR A CG2 1 
ATOM   2106 N  N   . TYR A 1 293 ? 111.507 101.907 80.845  1.00 30.94 ? 282  TYR A N   1 
ATOM   2107 C  CA  . TYR A 1 293 ? 111.538 102.635 82.099  1.00 30.94 ? 282  TYR A CA  1 
ATOM   2108 C  C   . TYR A 1 293 ? 112.891 103.321 82.241  1.00 30.94 ? 282  TYR A C   1 
ATOM   2109 O  O   . TYR A 1 293 ? 113.842 103.038 81.511  1.00 30.94 ? 282  TYR A O   1 
ATOM   2110 C  CB  . TYR A 1 293 ? 111.304 101.702 83.284  1.00 30.94 ? 282  TYR A CB  1 
ATOM   2111 C  CG  . TYR A 1 293 ? 109.899 101.163 83.418  1.00 30.94 ? 282  TYR A CG  1 
ATOM   2112 C  CD1 . TYR A 1 293 ? 108.804 101.885 82.976  1.00 30.94 ? 282  TYR A CD1 1 
ATOM   2113 C  CD2 . TYR A 1 293 ? 109.669 99.933  84.008  1.00 30.94 ? 282  TYR A CD2 1 
ATOM   2114 C  CE1 . TYR A 1 293 ? 107.527 101.391 83.107  1.00 30.94 ? 282  TYR A CE1 1 
ATOM   2115 C  CE2 . TYR A 1 293 ? 108.397 99.435  84.143  1.00 30.94 ? 282  TYR A CE2 1 
ATOM   2116 C  CZ  . TYR A 1 293 ? 107.330 100.166 83.690  1.00 30.94 ? 282  TYR A CZ  1 
ATOM   2117 O  OH  . TYR A 1 293 ? 106.059 99.666  83.825  1.00 30.94 ? 282  TYR A OH  1 
ATOM   2118 N  N   . LYS A 1 294 ? 112.978 104.233 83.198  1.00 36.87 ? 283  LYS A N   1 
ATOM   2119 C  CA  . LYS A 1 294 ? 114.180 105.024 83.399  1.00 36.87 ? 283  LYS A CA  1 
ATOM   2120 C  C   . LYS A 1 294 ? 114.942 104.505 84.607  1.00 36.87 ? 283  LYS A C   1 
ATOM   2121 O  O   . LYS A 1 294 ? 114.352 104.267 85.665  1.00 36.87 ? 283  LYS A O   1 
ATOM   2122 C  CB  . LYS A 1 294 ? 113.839 106.500 83.589  1.00 36.87 ? 283  LYS A CB  1 
ATOM   2123 C  CG  . LYS A 1 294 ? 115.052 107.364 83.825  1.00 36.87 ? 283  LYS A CG  1 
ATOM   2124 C  CD  . LYS A 1 294 ? 114.783 108.811 83.490  1.00 36.87 ? 283  LYS A CD  1 
ATOM   2125 C  CE  . LYS A 1 294 ? 115.516 109.733 84.443  1.00 36.87 ? 283  LYS A CE  1 
ATOM   2126 N  NZ  . LYS A 1 294 ? 116.939 109.342 84.607  1.00 36.87 ? 283  LYS A NZ  1 
ATOM   2127 N  N   . ASP A 1 295 ? 116.242 104.324 84.440  1.00 41.43 ? 284  ASP A N   1 
ATOM   2128 C  CA  . ASP A 1 295 ? 117.096 103.937 85.552  1.00 41.43 ? 284  ASP A CA  1 
ATOM   2129 C  C   . ASP A 1 295 ? 117.271 105.108 86.511  1.00 41.43 ? 284  ASP A C   1 
ATOM   2130 O  O   . ASP A 1 295 ? 117.688 106.190 86.083  1.00 41.43 ? 284  ASP A O   1 
ATOM   2131 C  CB  . ASP A 1 295 ? 118.457 103.453 85.047  1.00 30.00 ? 284  ASP A CB  1 
ATOM   2132 C  CG  . ASP A 1 295 ? 119.347 102.947 86.166  1.00 30.00 ? 284  ASP A CG  1 
ATOM   2133 O  OD1 . ASP A 1 295 ? 118.900 102.955 87.332  1.00 30.00 ? 284  ASP A OD1 1 
ATOM   2134 O  OD2 . ASP A 1 295 ? 120.506 102.523 85.973  1.00 30.00 ? 284  ASP A OD2 1 
ATOM   2135 N  N   . PRO A 1 296 ? 116.977 104.945 87.799  1.00 36.22 ? 285  PRO A N   1 
ATOM   2136 C  CA  . PRO A 1 296 ? 117.380 105.972 88.765  1.00 36.22 ? 285  PRO A CA  1 
ATOM   2137 C  C   . PRO A 1 296 ? 118.884 106.187 88.710  1.00 36.22 ? 285  PRO A C   1 
ATOM   2138 O  O   . PRO A 1 296 ? 119.665 105.234 88.694  1.00 36.22 ? 285  PRO A O   1 
ATOM   2139 C  CB  . PRO A 1 296 ? 116.929 105.389 90.106  1.00 36.22 ? 285  PRO A CB  1 
ATOM   2140 C  CG  . PRO A 1 296 ? 115.796 104.508 89.751  1.00 36.22 ? 285  PRO A CG  1 
ATOM   2141 C  CD  . PRO A 1 296 ? 116.163 103.898 88.435  1.00 36.22 ? 285  PRO A CD  1 
ATOM   2142 N  N   . ASP A 1 297 ? 119.289 107.453 88.692  1.00 42.39 ? 286  ASP A N   1 
ATOM   2143 C  CA  . ASP A 1 297 ? 120.681 107.795 88.435  1.00 42.39 ? 286  ASP A CA  1 
ATOM   2144 C  C   . ASP A 1 297 ? 121.292 108.534 89.617  1.00 42.39 ? 286  ASP A C   1 
ATOM   2145 O  O   . ASP A 1 297 ? 121.953 109.561 89.438  1.00 42.39 ? 286  ASP A O   1 
ATOM   2146 C  CB  . ASP A 1 297 ? 120.794 108.644 87.168  1.00 42.39 ? 286  ASP A CB  1 
ATOM   2147 N  N   . ASN A 1 298 ? 121.072 108.023 90.822  1.00 38.85 ? 287  ASN A N   1 
ATOM   2148 C  CA  . ASN A 1 298 ? 121.615 108.610 92.033  1.00 38.85 ? 287  ASN A CA  1 
ATOM   2149 C  C   . ASN A 1 298 ? 122.386 107.557 92.815  1.00 38.85 ? 287  ASN A C   1 
ATOM   2150 O  O   . ASN A 1 298 ? 122.116 106.361 92.681  1.00 38.85 ? 287  ASN A O   1 
ATOM   2151 C  CB  . ASN A 1 298 ? 120.500 109.199 92.908  1.00 38.85 ? 287  ASN A CB  1 
ATOM   2152 C  CG  . ASN A 1 298 ? 119.354 108.231 93.126  1.00 38.85 ? 287  ASN A CG  1 
ATOM   2153 O  OD1 . ASN A 1 298 ? 119.564 107.035 93.308  1.00 38.85 ? 287  ASN A OD1 1 
ATOM   2154 N  ND2 . ASN A 1 298 ? 118.133 108.747 93.103  1.00 38.85 ? 287  ASN A ND2 1 
ATOM   2155 N  N   . PRO A 1 299 ? 123.362 107.972 93.628  1.00 38.92 ? 288  PRO A N   1 
ATOM   2156 C  CA  . PRO A 1 299 ? 124.150 106.984 94.385  1.00 38.92 ? 288  PRO A CA  1 
ATOM   2157 C  C   . PRO A 1 299 ? 123.324 106.143 95.341  1.00 38.92 ? 288  PRO A C   1 
ATOM   2158 O  O   . PRO A 1 299 ? 123.663 104.976 95.584  1.00 38.92 ? 288  PRO A O   1 
ATOM   2159 C  CB  . PRO A 1 299 ? 125.166 107.854 95.141  1.00 38.92 ? 288  PRO A CB  1 
ATOM   2160 C  CG  . PRO A 1 299 ? 125.194 109.150 94.409  1.00 38.92 ? 288  PRO A CG  1 
ATOM   2161 C  CD  . PRO A 1 299 ? 123.814 109.348 93.890  1.00 38.92 ? 288  PRO A CD  1 
ATOM   2162 N  N   . GLU A 1 300 ? 122.254 106.708 95.904  1.00 37.21 ? 289  GLU A N   1 
ATOM   2163 C  CA  . GLU A 1 300 ? 121.462 105.977 96.885  1.00 37.21 ? 289  GLU A CA  1 
ATOM   2164 C  C   . GLU A 1 300 ? 120.883 104.705 96.284  1.00 37.21 ? 289  GLU A C   1 
ATOM   2165 O  O   . GLU A 1 300 ? 120.869 103.655 96.934  1.00 37.21 ? 289  GLU A O   1 
ATOM   2166 C  CB  . GLU A 1 300 ? 120.347 106.871 97.427  1.00 37.21 ? 289  GLU A CB  1 
ATOM   2167 N  N   . TYR A 1 301 ? 120.402 104.778 95.044  1.00 34.24 ? 290  TYR A N   1 
ATOM   2168 C  CA  . TYR A 1 301 ? 119.869 103.588 94.391  1.00 34.24 ? 290  TYR A CA  1 
ATOM   2169 C  C   . TYR A 1 301 ? 120.956 102.544 94.178  1.00 34.24 ? 290  TYR A C   1 
ATOM   2170 O  O   . TYR A 1 301 ? 120.716 101.344 94.348  1.00 34.24 ? 290  TYR A O   1 
ATOM   2171 C  CB  . TYR A 1 301 ? 119.224 103.970 93.062  1.00 34.24 ? 290  TYR A CB  1 
ATOM   2172 C  CG  . TYR A 1 301 ? 118.614 102.811 92.317  1.00 34.24 ? 290  TYR A CG  1 
ATOM   2173 C  CD1 . TYR A 1 301 ? 117.484 102.170 92.796  1.00 34.24 ? 290  TYR A CD1 1 
ATOM   2174 C  CD2 . TYR A 1 301 ? 119.162 102.365 91.128  1.00 34.24 ? 290  TYR A CD2 1 
ATOM   2175 C  CE1 . TYR A 1 301 ? 116.921 101.115 92.114  1.00 34.24 ? 290  TYR A CE1 1 
ATOM   2176 C  CE2 . TYR A 1 301 ? 118.606 101.313 90.441  1.00 34.24 ? 290  TYR A CE2 1 
ATOM   2177 C  CZ  . TYR A 1 301 ? 117.487 100.691 90.938  1.00 34.24 ? 290  TYR A CZ  1 
ATOM   2178 O  OH  . TYR A 1 301 ? 116.935 99.640  90.247  1.00 34.24 ? 290  TYR A OH  1 
ATOM   2179 N  N   . LEU A 1 302 ? 122.156 102.977 93.792  1.00 36.39 ? 291  LEU A N   1 
ATOM   2180 C  CA  . LEU A 1 302 ? 123.245 102.027 93.590  1.00 36.39 ? 291  LEU A CA  1 
ATOM   2181 C  C   . LEU A 1 302 ? 123.596 101.310 94.887  1.00 36.39 ? 291  LEU A C   1 
ATOM   2182 O  O   . LEU A 1 302 ? 123.780 100.089 94.897  1.00 36.39 ? 291  LEU A O   1 
ATOM   2183 C  CB  . LEU A 1 302 ? 124.471 102.744 93.027  1.00 36.39 ? 291  LEU A CB  1 
ATOM   2184 C  CG  . LEU A 1 302 ? 124.541 102.913 91.508  1.00 36.39 ? 291  LEU A CG  1 
ATOM   2185 C  CD1 . LEU A 1 302 ? 124.542 101.565 90.806  1.00 36.39 ? 291  LEU A CD1 1 
ATOM   2186 C  CD2 . LEU A 1 302 ? 123.401 103.776 91.006  1.00 36.39 ? 291  LEU A CD2 1 
ATOM   2187 N  N   . GLU A 1 303 ? 123.692 102.050 95.993  1.00 36.86 ? 292  GLU A N   1 
ATOM   2188 C  CA  . GLU A 1 303 ? 123.978 101.409 97.275  1.00 36.86 ? 292  GLU A CA  1 
ATOM   2189 C  C   . GLU A 1 303 ? 122.844 100.477 97.688  1.00 36.86 ? 292  GLU A C   1 
ATOM   2190 O  O   . GLU A 1 303 ? 123.085 99.375  98.207  1.00 36.86 ? 292  GLU A O   1 
ATOM   2191 C  CB  . GLU A 1 303 ? 124.217 102.469 98.348  1.00 36.86 ? 292  GLU A CB  1 
ATOM   2192 N  N   . PHE A 1 304 ? 121.598 100.906 97.472  1.00 33.44 ? 293  PHE A N   1 
ATOM   2193 C  CA  . PHE A 1 304 ? 120.460 100.066 97.814  1.00 33.44 ? 293  PHE A CA  1 
ATOM   2194 C  C   . PHE A 1 304 ? 120.513 98.752  97.057  1.00 33.44 ? 293  PHE A C   1 
ATOM   2195 O  O   . PHE A 1 304 ? 120.277 97.691  97.635  1.00 33.44 ? 293  PHE A O   1 
ATOM   2196 C  CB  . PHE A 1 304 ? 119.155 100.801 97.519  1.00 33.44 ? 293  PHE A CB  1 
ATOM   2197 C  CG  . PHE A 1 304 ? 117.948 99.909  97.491  1.00 33.44 ? 293  PHE A CG  1 
ATOM   2198 C  CD1 . PHE A 1 304 ? 117.372 99.464  98.664  1.00 33.44 ? 293  PHE A CD1 1 
ATOM   2199 C  CD2 . PHE A 1 304 ? 117.386 99.522  96.293  1.00 33.44 ? 293  PHE A CD2 1 
ATOM   2200 C  CE1 . PHE A 1 304 ? 116.265 98.645  98.635  1.00 33.44 ? 293  PHE A CE1 1 
ATOM   2201 C  CE2 . PHE A 1 304 ? 116.281 98.704  96.265  1.00 33.44 ? 293  PHE A CE2 1 
ATOM   2202 C  CZ  . PHE A 1 304 ? 115.721 98.269  97.435  1.00 33.44 ? 293  PHE A CZ  1 
ATOM   2203 N  N   . LEU A 1 305 ? 120.821 98.799  95.761  1.00 35.56 ? 294  LEU A N   1 
ATOM   2204 C  CA  . LEU A 1 305 ? 120.969 97.564  94.997  1.00 35.56 ? 294  LEU A CA  1 
ATOM   2205 C  C   . LEU A 1 305 ? 122.131 96.733  95.514  1.00 35.56 ? 294  LEU A C   1 
ATOM   2206 O  O   . LEU A 1 305 ? 122.026 95.505  95.635  1.00 35.56 ? 294  LEU A O   1 
ATOM   2207 C  CB  . LEU A 1 305 ? 121.175 97.877  93.519  1.00 35.56 ? 294  LEU A CB  1 
ATOM   2208 C  CG  . LEU A 1 305 ? 119.934 97.892  92.637  1.00 35.56 ? 294  LEU A CG  1 
ATOM   2209 C  CD1 . LEU A 1 305 ? 120.325 97.500  91.229  1.00 35.56 ? 294  LEU A CD1 1 
ATOM   2210 C  CD2 . LEU A 1 305 ? 118.860 96.969  93.179  1.00 35.56 ? 294  LEU A CD2 1 
ATOM   2211 N  N   . LYS A 1 306 ? 123.254 97.386  95.817  1.00 39.29 ? 295  LYS A N   1 
ATOM   2212 C  CA  . LYS A 1 306 ? 124.430 96.667  96.287  1.00 39.29 ? 295  LYS A CA  1 
ATOM   2213 C  C   . LYS A 1 306 ? 124.095 95.811  97.498  1.00 39.29 ? 295  LYS A C   1 
ATOM   2214 O  O   . LYS A 1 306 ? 124.478 94.638  97.567  1.00 39.29 ? 295  LYS A O   1 
ATOM   2215 C  CB  . LYS A 1 306 ? 125.544 97.658  96.620  1.00 39.29 ? 295  LYS A CB  1 
ATOM   2216 C  CG  . LYS A 1 306 ? 126.840 97.013  97.068  1.00 39.29 ? 295  LYS A CG  1 
ATOM   2217 C  CD  . LYS A 1 306 ? 127.925 98.052  97.272  1.00 39.29 ? 295  LYS A CD  1 
ATOM   2218 C  CE  . LYS A 1 306 ? 129.183 97.438  97.863  1.00 39.29 ? 295  LYS A CE  1 
ATOM   2219 N  NZ  . LYS A 1 306 ? 129.833 96.481  96.929  1.00 39.29 ? 295  LYS A NZ  1 
ATOM   2220 N  N   . GLN A 1 307 ? 123.377 96.377  98.466  1.00 37.28 ? 296  GLN A N   1 
ATOM   2221 C  CA  . GLN A 1 307 ? 123.042 95.601  99.657  1.00 37.28 ? 296  GLN A CA  1 
ATOM   2222 C  C   . GLN A 1 307 ? 121.793 94.740  99.490  1.00 37.28 ? 296  GLN A C   1 
ATOM   2223 O  O   . GLN A 1 307 ? 121.678 93.708  100.163 1.00 37.28 ? 296  GLN A O   1 
ATOM   2224 C  CB  . GLN A 1 307 ? 122.888 96.516  100.876 1.00 37.28 ? 296  GLN A CB  1 
ATOM   2225 C  CG  . GLN A 1 307 ? 121.869 97.615  100.749 1.00 37.28 ? 296  GLN A CG  1 
ATOM   2226 C  CD  . GLN A 1 307 ? 121.840 98.500  101.978 1.00 37.28 ? 296  GLN A CD  1 
ATOM   2227 O  OE1 . GLN A 1 307 ? 122.502 98.214  102.973 1.00 37.28 ? 296  GLN A OE1 1 
ATOM   2228 N  NE2 . GLN A 1 307 ? 121.080 99.584  101.913 1.00 37.28 ? 296  GLN A NE2 1 
ATOM   2229 N  N   . LEU A 1 308 ? 120.876 95.109  98.594  1.00 34.01 ? 297  LEU A N   1 
ATOM   2230 C  CA  . LEU A 1 308 ? 119.703 94.282  98.341  1.00 34.01 ? 297  LEU A CA  1 
ATOM   2231 C  C   . LEU A 1 308 ? 120.094 92.951  97.720  1.00 34.01 ? 297  LEU A C   1 
ATOM   2232 O  O   . LEU A 1 308 ? 119.549 91.907  98.089  1.00 34.01 ? 297  LEU A O   1 
ATOM   2233 C  CB  . LEU A 1 308 ? 118.728 95.038  97.435  1.00 34.01 ? 297  LEU A CB  1 
ATOM   2234 C  CG  . LEU A 1 308 ? 117.591 94.274  96.752  1.00 34.01 ? 297  LEU A CG  1 
ATOM   2235 C  CD1 . LEU A 1 308 ? 116.447 94.074  97.705  1.00 34.01 ? 297  LEU A CD1 1 
ATOM   2236 C  CD2 . LEU A 1 308 ? 117.116 95.021  95.525  1.00 34.01 ? 297  LEU A CD2 1 
ATOM   2237 N  N   . LYS A 1 309 ? 121.028 92.964  96.767  1.00 38.68 ? 298  LYS A N   1 
ATOM   2238 C  CA  . LYS A 1 309 ? 121.470 91.712  96.161  1.00 38.68 ? 298  LYS A CA  1 
ATOM   2239 C  C   . LYS A 1 309 ? 122.102 90.796  97.201  1.00 38.68 ? 298  LYS A C   1 
ATOM   2240 O  O   . LYS A 1 309 ? 121.819 89.589  97.242  1.00 38.68 ? 298  LYS A O   1 
ATOM   2241 C  CB  . LYS A 1 309 ? 122.457 92.003  95.032  1.00 38.68 ? 298  LYS A CB  1 
ATOM   2242 C  CG  . LYS A 1 309 ? 121.823 92.636  93.804  1.00 38.68 ? 298  LYS A CG  1 
ATOM   2243 C  CD  . LYS A 1 309 ? 122.867 93.017  92.769  1.00 38.68 ? 298  LYS A CD  1 
ATOM   2244 C  CE  . LYS A 1 309 ? 122.278 93.903  91.682  1.00 38.68 ? 298  LYS A CE  1 
ATOM   2245 N  NZ  . LYS A 1 309 ? 123.306 94.778  91.054  1.00 38.68 ? 298  LYS A NZ  1 
ATOM   2246 N  N   . HIS A 1 310 ? 122.954 91.359  98.057  1.00 40.41 ? 299  HIS A N   1 
ATOM   2247 C  CA  . HIS A 1 310 ? 123.596 90.574  99.103  1.00 40.41 ? 299  HIS A CA  1 
ATOM   2248 C  C   . HIS A 1 310 ? 122.565 89.969  100.045 1.00 40.41 ? 299  HIS A C   1 
ATOM   2249 O  O   . HIS A 1 310 ? 122.632 88.779  100.376 1.00 40.41 ? 299  HIS A O   1 
ATOM   2250 C  CB  . HIS A 1 310 ? 124.578 91.458  99.872  1.00 40.41 ? 299  HIS A CB  1 
ATOM   2251 C  CG  . HIS A 1 310 ? 125.100 90.835  101.128 1.00 40.41 ? 299  HIS A CG  1 
ATOM   2252 N  ND1 . HIS A 1 310 ? 126.241 90.063  101.157 1.00 40.41 ? 299  HIS A ND1 1 
ATOM   2253 C  CD2 . HIS A 1 310 ? 124.640 90.875  102.400 1.00 40.41 ? 299  HIS A CD2 1 
ATOM   2254 C  CE1 . HIS A 1 310 ? 126.460 89.652  102.392 1.00 40.41 ? 299  HIS A CE1 1 
ATOM   2255 N  NE2 . HIS A 1 310 ? 125.503 90.131  103.166 1.00 40.41 ? 299  HIS A NE2 1 
ATOM   2256 N  N   . LEU A 1 311 ? 121.601 90.776  100.493 1.00 35.89 ? 300  LEU A N   1 
ATOM   2257 C  CA  . LEU A 1 311 ? 120.593 90.263  101.414 1.00 35.89 ? 300  LEU A CA  1 
ATOM   2258 C  C   . LEU A 1 311 ? 119.733 89.195  100.753 1.00 35.89 ? 300  LEU A C   1 
ATOM   2259 O  O   . LEU A 1 311 ? 119.381 88.195  101.386 1.00 35.89 ? 300  LEU A O   1 
ATOM   2260 C  CB  . LEU A 1 311 ? 119.720 91.403  101.929 1.00 35.89 ? 300  LEU A CB  1 
ATOM   2261 C  CG  . LEU A 1 311 ? 118.944 91.089  103.204 1.00 35.89 ? 300  LEU A CG  1 
ATOM   2262 C  CD1 . LEU A 1 311 ? 119.887 90.918  104.378 1.00 35.89 ? 300  LEU A CD1 1 
ATOM   2263 C  CD2 . LEU A 1 311 ? 117.946 92.186  103.481 1.00 35.89 ? 300  LEU A CD2 1 
ATOM   2264 N  N   . ALA A 1 312 ? 119.363 89.397  99.488  1.00 35.36 ? 301  ALA A N   1 
ATOM   2265 C  CA  . ALA A 1 312 ? 118.579 88.390  98.788  1.00 35.36 ? 301  ALA A CA  1 
ATOM   2266 C  C   . ALA A 1 312 ? 119.323 87.067  98.752  1.00 35.36 ? 301  ALA A C   1 
ATOM   2267 O  O   . ALA A 1 312 ? 118.767 86.020  99.103  1.00 35.36 ? 301  ALA A O   1 
ATOM   2268 C  CB  . ALA A 1 312 ? 118.256 88.864  97.373  1.00 35.36 ? 301  ALA A CB  1 
ATOM   2269 N  N   . TYR A 1 313 ? 120.599 87.097  98.361  1.00 39.41 ? 302  TYR A N   1 
ATOM   2270 C  CA  . TYR A 1 313 ? 121.369 85.857  98.316  1.00 39.41 ? 302  TYR A CA  1 
ATOM   2271 C  C   . TYR A 1 313 ? 121.472 85.218  99.694  1.00 39.41 ? 302  TYR A C   1 
ATOM   2272 O  O   . TYR A 1 313 ? 121.304 84.002  99.835  1.00 39.41 ? 302  TYR A O   1 
ATOM   2273 C  CB  . TYR A 1 313 ? 122.763 86.112  97.751  1.00 39.41 ? 302  TYR A CB  1 
ATOM   2274 C  CG  . TYR A 1 313 ? 123.590 84.852  97.649  1.00 39.41 ? 302  TYR A CG  1 
ATOM   2275 C  CD1 . TYR A 1 313 ? 124.555 84.552  98.600  1.00 39.41 ? 302  TYR A CD1 1 
ATOM   2276 C  CD2 . TYR A 1 313 ? 123.392 83.952  96.612  1.00 39.41 ? 302  TYR A CD2 1 
ATOM   2277 C  CE1 . TYR A 1 313 ? 125.307 83.398  98.516  1.00 39.41 ? 302  TYR A CE1 1 
ATOM   2278 C  CE2 . TYR A 1 313 ? 124.137 82.795  96.519  1.00 39.41 ? 302  TYR A CE2 1 
ATOM   2279 C  CZ  . TYR A 1 313 ? 125.093 82.523  97.473  1.00 39.41 ? 302  TYR A CZ  1 
ATOM   2280 O  OH  . TYR A 1 313 ? 125.839 81.371  97.382  1.00 39.41 ? 302  TYR A OH  1 
ATOM   2281 N  N   . GLU A 1 314 ? 121.744 86.018  100.726 1.00 38.67 ? 303  GLU A N   1 
ATOM   2282 C  CA  . GLU A 1 314 ? 121.953 85.454  102.055 1.00 38.67 ? 303  GLU A CA  1 
ATOM   2283 C  C   . GLU A 1 314 ? 120.678 84.822  102.601 1.00 38.67 ? 303  GLU A C   1 
ATOM   2284 O  O   . GLU A 1 314 ? 120.687 83.667  103.041 1.00 38.67 ? 303  GLU A O   1 
ATOM   2285 C  CB  . GLU A 1 314 ? 122.464 86.534  103.007 1.00 38.67 ? 303  GLU A CB  1 
ATOM   2286 N  N   . GLN A 1 315 ? 119.566 85.555  102.571 1.00 38.98 ? 304  GLN A N   1 
ATOM   2287 C  CA  . GLN A 1 315 ? 118.358 85.166  103.287 1.00 38.98 ? 304  GLN A CA  1 
ATOM   2288 C  C   . GLN A 1 315 ? 117.330 84.442  102.427 1.00 38.98 ? 304  GLN A C   1 
ATOM   2289 O  O   . GLN A 1 315 ? 116.298 84.027  102.959 1.00 38.98 ? 304  GLN A O   1 
ATOM   2290 C  CB  . GLN A 1 315 ? 117.702 86.403  103.910 1.00 38.98 ? 304  GLN A CB  1 
ATOM   2291 C  CG  . GLN A 1 315 ? 118.113 86.676  105.351 1.00 38.98 ? 304  GLN A CG  1 
ATOM   2292 C  CD  . GLN A 1 315 ? 117.043 87.417  106.135 1.00 38.98 ? 304  GLN A CD  1 
ATOM   2293 O  OE1 . GLN A 1 315 ? 115.850 87.273  105.871 1.00 38.98 ? 304  GLN A OE1 1 
ATOM   2294 N  NE2 . GLN A 1 315 ? 117.468 88.217  107.105 1.00 38.98 ? 304  GLN A NE2 1 
ATOM   2295 N  N   . PHE A 1 316 ? 117.570 84.275  101.125 1.00 33.79 ? 305  PHE A N   1 
ATOM   2296 C  CA  . PHE A 1 316 ? 116.573 83.643  100.272 1.00 33.79 ? 305  PHE A CA  1 
ATOM   2297 C  C   . PHE A 1 316 ? 117.147 82.649  99.273  1.00 33.79 ? 305  PHE A C   1 
ATOM   2298 O  O   . PHE A 1 316 ? 116.373 82.052  98.520  1.00 33.79 ? 305  PHE A O   1 
ATOM   2299 C  CB  . PHE A 1 316 ? 115.777 84.715  99.510  1.00 33.79 ? 305  PHE A CB  1 
ATOM   2300 C  CG  . PHE A 1 316 ? 114.765 85.431  100.357 1.00 33.79 ? 305  PHE A CG  1 
ATOM   2301 C  CD1 . PHE A 1 316 ? 115.123 86.545  101.095 1.00 33.79 ? 305  PHE A CD1 1 
ATOM   2302 C  CD2 . PHE A 1 316 ? 113.458 84.986  100.419 1.00 33.79 ? 305  PHE A CD2 1 
ATOM   2303 C  CE1 . PHE A 1 316 ? 114.197 87.200  101.876 1.00 33.79 ? 305  PHE A CE1 1 
ATOM   2304 C  CE2 . PHE A 1 316 ? 112.531 85.640  101.198 1.00 33.79 ? 305  PHE A CE2 1 
ATOM   2305 C  CZ  . PHE A 1 316 ? 112.901 86.748  101.927 1.00 33.79 ? 305  PHE A CZ  1 
ATOM   2306 N  N   . ASN A 1 317 ? 118.461 82.445  99.240  1.00 39.11 ? 306  ASN A N   1 
ATOM   2307 C  CA  . ASN A 1 317 ? 119.078 81.538  98.274  1.00 39.11 ? 306  ASN A CA  1 
ATOM   2308 C  C   . ASN A 1 317 ? 118.686 81.918  96.849  1.00 39.11 ? 306  ASN A C   1 
ATOM   2309 O  O   . ASN A 1 317 ? 118.403 81.064  96.008  1.00 39.11 ? 306  ASN A O   1 
ATOM   2310 C  CB  . ASN A 1 317 ? 118.705 80.087  98.572  1.00 39.11 ? 306  ASN A CB  1 
ATOM   2311 N  N   . PHE A 1 318 ? 118.666 83.221  96.580  1.00 33.86 ? 307  PHE A N   1 
ATOM   2312 C  CA  . PHE A 1 318 ? 118.336 83.760  95.269  1.00 33.86 ? 307  PHE A CA  1 
ATOM   2313 C  C   . PHE A 1 318 ? 119.392 84.778  94.877  1.00 33.86 ? 307  PHE A C   1 
ATOM   2314 O  O   . PHE A 1 318 ? 119.784 85.618  95.691  1.00 33.86 ? 307  PHE A O   1 
ATOM   2315 C  CB  . PHE A 1 318 ? 116.954 84.420  95.272  1.00 33.86 ? 307  PHE A CB  1 
ATOM   2316 C  CG  . PHE A 1 318 ? 116.533 84.953  93.935  1.00 33.86 ? 307  PHE A CG  1 
ATOM   2317 C  CD1 . PHE A 1 318 ? 116.256 84.097  92.891  1.00 33.86 ? 307  PHE A CD1 1 
ATOM   2318 C  CD2 . PHE A 1 318 ? 116.411 86.311  93.725  1.00 33.86 ? 307  PHE A CD2 1 
ATOM   2319 C  CE1 . PHE A 1 318 ? 115.867 84.587  91.669  1.00 33.86 ? 307  PHE A CE1 1 
ATOM   2320 C  CE2 . PHE A 1 318 ? 116.024 86.801  92.503  1.00 33.86 ? 307  PHE A CE2 1 
ATOM   2321 C  CZ  . PHE A 1 318 ? 115.755 85.940  91.476  1.00 33.86 ? 307  PHE A CZ  1 
ATOM   2322 N  N   . THR A 1 319 ? 119.852 84.703  93.633  1.00 37.58 ? 308  THR A N   1 
ATOM   2323 C  CA  . THR A 1 319 ? 120.847 85.628  93.107  1.00 37.58 ? 308  THR A CA  1 
ATOM   2324 C  C   . THR A 1 319 ? 120.168 86.545  92.098  1.00 37.58 ? 308  THR A C   1 
ATOM   2325 O  O   . THR A 1 319 ? 119.595 86.072  91.111  1.00 37.58 ? 308  THR A O   1 
ATOM   2326 C  CB  . THR A 1 319 ? 122.020 84.880  92.470  1.00 37.58 ? 308  THR A CB  1 
ATOM   2327 O  OG1 . THR A 1 319 ? 122.982 85.821  91.979  1.00 37.58 ? 308  THR A OG1 1 
ATOM   2328 C  CG2 . THR A 1 319 ? 121.556 83.992  91.323  1.00 37.58 ? 308  THR A CG2 1 
ATOM   2329 N  N   . MET A 1 320 ? 120.230 87.849  92.351  1.00 36.89 ? 309  MET A N   1 
ATOM   2330 C  CA  . MET A 1 320 ? 119.531 88.832  91.537  1.00 36.89 ? 309  MET A CA  1 
ATOM   2331 C  C   . MET A 1 320 ? 120.444 89.354  90.438  1.00 36.89 ? 309  MET A C   1 
ATOM   2332 O  O   . MET A 1 320 ? 121.567 89.791  90.708  1.00 36.89 ? 309  MET A O   1 
ATOM   2333 C  CB  . MET A 1 320 ? 119.046 89.995  92.401  1.00 36.89 ? 309  MET A CB  1 
ATOM   2334 C  CG  . MET A 1 320 ? 117.952 89.630  93.382  1.00 36.89 ? 309  MET A CG  1 
ATOM   2335 S  SD  . MET A 1 320 ? 117.475 91.031  94.402  1.00 36.89 ? 309  MET A SD  1 
ATOM   2336 C  CE  . MET A 1 320 ? 116.665 92.056  93.182  1.00 36.89 ? 309  MET A CE  1 
ATOM   2337 N  N   . GLU A 1 321 ? 119.952 89.317  89.203  1.00 40.78 ? 310  GLU A N   1 
ATOM   2338 C  CA  . GLU A 1 321 ? 120.674 89.858  88.062  1.00 40.78 ? 310  GLU A CA  1 
ATOM   2339 C  C   . GLU A 1 321 ? 120.226 91.293  87.825  1.00 40.78 ? 310  GLU A C   1 
ATOM   2340 O  O   . GLU A 1 321 ? 119.025 91.573  87.772  1.00 40.78 ? 310  GLU A O   1 
ATOM   2341 C  CB  . GLU A 1 321 ? 120.426 89.010  86.815  1.00 40.78 ? 310  GLU A CB  1 
ATOM   2342 N  N   . ASP A 1 322 ? 121.191 92.196  87.678  1.00 42.15 ? 311  ASP A N   1 
ATOM   2343 C  CA  . ASP A 1 322 ? 120.871 93.612  87.582  1.00 42.15 ? 311  ASP A CA  1 
ATOM   2344 C  C   . ASP A 1 322 ? 120.039 93.900  86.338  1.00 42.15 ? 311  ASP A C   1 
ATOM   2345 O  O   . ASP A 1 322 ? 120.137 93.212  85.320  1.00 42.15 ? 311  ASP A O   1 
ATOM   2346 C  CB  . ASP A 1 322 ? 122.149 94.448  87.561  1.00 42.15 ? 311  ASP A CB  1 
ATOM   2347 C  CG  . ASP A 1 322 ? 123.111 94.009  86.483  1.00 42.15 ? 311  ASP A CG  1 
ATOM   2348 O  OD1 . ASP A 1 322 ? 122.816 93.009  85.798  1.00 42.15 ? 311  ASP A OD1 1 
ATOM   2349 O  OD2 . ASP A 1 322 ? 124.163 94.662  86.322  1.00 42.15 ? 311  ASP A OD2 1 
ATOM   2350 N  N   . GLY A 1 323 ? 119.208 94.931  86.437  1.00 37.23 ? 312  GLY A N   1 
ATOM   2351 C  CA  . GLY A 1 323 ? 118.330 95.300  85.344  1.00 37.23 ? 312  GLY A CA  1 
ATOM   2352 C  C   . GLY A 1 323 ? 117.376 96.387  85.793  1.00 37.23 ? 312  GLY A C   1 
ATOM   2353 O  O   . GLY A 1 323 ? 117.586 97.020  86.826  1.00 37.23 ? 312  GLY A O   1 
ATOM   2354 N  N   . LEU A 1 324 ? 116.330 96.598  84.998  1.00 33.65 ? 313  LEU A N   1 
ATOM   2355 C  CA  . LEU A 1 324 ? 115.290 97.545  85.373  1.00 33.65 ? 313  LEU A CA  1 
ATOM   2356 C  C   . LEU A 1 324 ? 114.206 96.916  86.233  1.00 33.65 ? 313  LEU A C   1 
ATOM   2357 O  O   . LEU A 1 324 ? 113.492 97.642  86.932  1.00 33.65 ? 313  LEU A O   1 
ATOM   2358 C  CB  . LEU A 1 324 ? 114.652 98.164  84.125  1.00 33.65 ? 313  LEU A CB  1 
ATOM   2359 C  CG  . LEU A 1 324 ? 115.496 99.192  83.366  1.00 33.65 ? 313  LEU A CG  1 
ATOM   2360 C  CD1 . LEU A 1 324 ? 114.803 99.599  82.089  1.00 33.65 ? 313  LEU A CD1 1 
ATOM   2361 C  CD2 . LEU A 1 324 ? 115.783 100.409 84.220  1.00 33.65 ? 313  LEU A CD2 1 
ATOM   2362 N  N   . VAL A 1 325 ? 114.075 95.589  86.214  1.00 29.77 ? 314  VAL A N   1 
ATOM   2363 C  CA  . VAL A 1 325 ? 113.136 94.927  87.114  1.00 29.77 ? 314  VAL A CA  1 
ATOM   2364 C  C   . VAL A 1 325 ? 113.463 95.268  88.558  1.00 29.77 ? 314  VAL A C   1 
ATOM   2365 O  O   . VAL A 1 325 ? 112.580 95.261  89.424  1.00 29.77 ? 314  VAL A O   1 
ATOM   2366 C  CB  . VAL A 1 325 ? 113.146 93.405  86.881  1.00 29.77 ? 314  VAL A CB  1 
ATOM   2367 C  CG1 . VAL A 1 325 ? 112.514 93.071  85.552  1.00 29.77 ? 314  VAL A CG1 1 
ATOM   2368 C  CG2 . VAL A 1 325 ? 114.562 92.864  86.939  1.00 29.77 ? 314  VAL A CG2 1 
ATOM   2369 N  N   . ASN A 1 326 ? 114.720 95.604  88.837  1.00 32.49 ? 315  ASN A N   1 
ATOM   2370 C  CA  . ASN A 1 326 ? 115.127 95.945  90.190  1.00 32.49 ? 315  ASN A CA  1 
ATOM   2371 C  C   . ASN A 1 326 ? 114.481 97.226  90.689  1.00 32.49 ? 315  ASN A C   1 
ATOM   2372 O  O   . ASN A 1 326 ? 114.606 97.533  91.878  1.00 32.49 ? 315  ASN A O   1 
ATOM   2373 C  CB  . ASN A 1 326 ? 116.645 96.077  90.259  1.00 32.49 ? 315  ASN A CB  1 
ATOM   2374 C  CG  . ASN A 1 326 ? 117.350 94.752  90.110  1.00 32.49 ? 315  ASN A CG  1 
ATOM   2375 O  OD1 . ASN A 1 326 ? 116.726 93.729  89.843  1.00 32.49 ? 315  ASN A OD1 1 
ATOM   2376 N  ND2 . ASN A 1 326 ? 118.662 94.761  90.286  1.00 32.49 ? 315  ASN A ND2 1 
ATOM   2377 N  N   . THR A 1 327 ? 113.820 97.990  89.820  1.00 29.34 ? 316  THR A N   1 
ATOM   2378 C  CA  . THR A 1 327 ? 113.072 99.153  90.273  1.00 29.34 ? 316  THR A CA  1 
ATOM   2379 C  C   . THR A 1 327 ? 111.726 98.787  90.877  1.00 29.34 ? 316  THR A C   1 
ATOM   2380 O  O   . THR A 1 327 ? 111.103 99.644  91.508  1.00 29.34 ? 316  THR A O   1 
ATOM   2381 C  CB  . THR A 1 327 ? 112.843 100.137 89.124  1.00 29.34 ? 316  THR A CB  1 
ATOM   2382 O  OG1 . THR A 1 327 ? 111.893 99.592  88.203  1.00 29.34 ? 316  THR A OG1 1 
ATOM   2383 C  CG2 . THR A 1 327 ? 114.140 100.440 88.398  1.00 29.34 ? 316  THR A CG2 1 
ATOM   2384 N  N   . ILE A 1 328 ? 111.257 97.556  90.703  1.00 25.79 ? 317  ILE A N   1 
ATOM   2385 C  CA  . ILE A 1 328 ? 109.971 97.162  91.272  1.00 25.79 ? 317  ILE A CA  1 
ATOM   2386 C  C   . ILE A 1 328 ? 110.158 96.847  92.752  1.00 25.79 ? 317  ILE A C   1 
ATOM   2387 O  O   . ILE A 1 328 ? 109.357 97.308  93.573  1.00 25.79 ? 317  ILE A O   1 
ATOM   2388 C  CB  . ILE A 1 328 ? 109.352 95.980  90.510  1.00 25.79 ? 317  ILE A CB  1 
ATOM   2389 C  CG1 . ILE A 1 328 ? 109.111 96.351  89.046  1.00 25.79 ? 317  ILE A CG1 1 
ATOM   2390 C  CG2 . ILE A 1 328 ? 108.057 95.554  91.163  1.00 25.79 ? 317  ILE A CG2 1 
ATOM   2391 C  CD1 . ILE A 1 328 ? 108.259 97.574  88.840  1.00 25.79 ? 317  ILE A CD1 1 
ATOM   2392 N  N   . PRO A 1 329 ? 111.172 96.073  93.153  1.00 27.42 ? 318  PRO A N   1 
ATOM   2393 C  CA  . PRO A 1 329 ? 111.454 95.972  94.592  1.00 27.42 ? 318  PRO A CA  1 
ATOM   2394 C  C   . PRO A 1 329 ? 111.696 97.319  95.242  1.00 27.42 ? 318  PRO A C   1 
ATOM   2395 O  O   . PRO A 1 329 ? 111.141 97.597  96.312  1.00 27.42 ? 318  PRO A O   1 
ATOM   2396 C  CB  . PRO A 1 329 ? 112.703 95.088  94.634  1.00 27.42 ? 318  PRO A CB  1 
ATOM   2397 C  CG  . PRO A 1 329 ? 112.597 94.255  93.438  1.00 27.42 ? 318  PRO A CG  1 
ATOM   2398 C  CD  . PRO A 1 329 ? 111.993 95.126  92.381  1.00 27.42 ? 318  PRO A CD  1 
ATOM   2399 N  N   . ALA A 1 330 ? 112.480 98.184  94.598  1.00 29.32 ? 319  ALA A N   1 
ATOM   2400 C  CA  . ALA A 1 330 ? 112.780 99.488  95.175  1.00 29.32 ? 319  ALA A CA  1 
ATOM   2401 C  C   . ALA A 1 330 ? 111.508 100.278 95.431  1.00 29.32 ? 319  ALA A C   1 
ATOM   2402 O  O   . ALA A 1 330 ? 111.372 100.928 96.472  1.00 29.32 ? 319  ALA A O   1 
ATOM   2403 C  CB  . ALA A 1 330 ? 113.713 100.266 94.252  1.00 29.32 ? 319  ALA A CB  1 
ATOM   2404 N  N   . SER A 1 331 ? 110.559 100.227 94.497  1.00 27.03 ? 320  SER A N   1 
ATOM   2405 C  CA  . SER A 1 331 ? 109.280 100.894 94.707  1.00 27.03 ? 320  SER A CA  1 
ATOM   2406 C  C   . SER A 1 331 ? 108.605 100.387 95.975  1.00 27.03 ? 320  SER A C   1 
ATOM   2407 O  O   . SER A 1 331 ? 108.118 101.178 96.788  1.00 27.03 ? 320  SER A O   1 
ATOM   2408 C  CB  . SER A 1 331 ? 108.380 100.682 93.494  1.00 27.03 ? 320  SER A CB  1 
ATOM   2409 O  OG  . SER A 1 331 ? 108.900 101.359 92.365  1.00 27.03 ? 320  SER A OG  1 
ATOM   2410 N  N   . PHE A 1 332 ? 108.587 99.066  96.174  1.00 23.54 ? 321  PHE A N   1 
ATOM   2411 C  CA  . PHE A 1 332 ? 108.019 98.526  97.404  1.00 23.54 ? 321  PHE A CA  1 
ATOM   2412 C  C   . PHE A 1 332 ? 108.751 99.059  98.623  1.00 23.54 ? 321  PHE A C   1 
ATOM   2413 O  O   . PHE A 1 332 ? 108.143 99.248  99.681  1.00 23.54 ? 321  PHE A O   1 
ATOM   2414 C  CB  . PHE A 1 332 ? 108.072 97.001  97.393  1.00 23.54 ? 321  PHE A CB  1 
ATOM   2415 C  CG  . PHE A 1 332 ? 106.878 96.351  96.760  1.00 23.54 ? 321  PHE A CG  1 
ATOM   2416 C  CD1 . PHE A 1 332 ? 105.698 96.209  97.459  1.00 23.54 ? 321  PHE A CD1 1 
ATOM   2417 C  CD2 . PHE A 1 332 ? 106.942 95.864  95.471  1.00 23.54 ? 321  PHE A CD2 1 
ATOM   2418 C  CE1 . PHE A 1 332 ? 104.608 95.602  96.884  1.00 23.54 ? 321  PHE A CE1 1 
ATOM   2419 C  CE2 . PHE A 1 332 ? 105.850 95.257  94.894  1.00 23.54 ? 321  PHE A CE2 1 
ATOM   2420 C  CZ  . PHE A 1 332 ? 104.684 95.128  95.603  1.00 23.54 ? 321  PHE A CZ  1 
ATOM   2421 N  N   . HIS A 1 333 ? 110.055 99.298  98.500  1.00 28.95 ? 322  HIS A N   1 
ATOM   2422 C  CA  . HIS A 1 333 ? 110.803 99.887  99.599  1.00 28.95 ? 322  HIS A CA  1 
ATOM   2423 C  C   . HIS A 1 333 ? 110.448 101.353 99.781  1.00 28.95 ? 322  HIS A C   1 
ATOM   2424 O  O   . HIS A 1 333 ? 110.425 101.847 100.912 1.00 28.95 ? 322  HIS A O   1 
ATOM   2425 C  CB  . HIS A 1 333 ? 112.300 99.717  99.349  1.00 28.95 ? 322  HIS A CB  1 
ATOM   2426 C  CG  . HIS A 1 333 ? 113.170 100.527 100.259 1.00 28.95 ? 322  HIS A CG  1 
ATOM   2427 N  ND1 . HIS A 1 333 ? 113.507 101.836 99.997  1.00 28.95 ? 322  HIS A ND1 1 
ATOM   2428 C  CD2 . HIS A 1 333 ? 113.789 100.205 101.418 1.00 28.95 ? 322  HIS A CD2 1 
ATOM   2429 C  CE1 . HIS A 1 333 ? 114.286 102.289 100.961 1.00 28.95 ? 322  HIS A CE1 1 
ATOM   2430 N  NE2 . HIS A 1 333 ? 114.474 101.319 101.836 1.00 28.95 ? 322  HIS A NE2 1 
ATOM   2431 N  N   . ASP A 1 334 ? 110.163 102.062 98.688  1.00 32.12 ? 323  ASP A N   1 
ATOM   2432 C  CA  . ASP A 1 334 ? 109.806 103.473 98.786  1.00 32.12 ? 323  ASP A CA  1 
ATOM   2433 C  C   . ASP A 1 334 ? 108.369 103.644 99.257  1.00 32.12 ? 323  ASP A C   1 
ATOM   2434 O  O   . ASP A 1 334 ? 108.109 104.360 100.228 1.00 32.12 ? 323  ASP A O   1 
ATOM   2435 C  CB  . ASP A 1 334 ? 110.006 104.156 97.435  1.00 32.12 ? 323  ASP A CB  1 
ATOM   2436 C  CG  . ASP A 1 334 ? 111.448 104.532 97.178  1.00 32.12 ? 323  ASP A CG  1 
ATOM   2437 O  OD1 . ASP A 1 334 ? 112.267 104.442 98.114  1.00 32.12 ? 323  ASP A OD1 1 
ATOM   2438 O  OD2 . ASP A 1 334 ? 111.764 104.921 96.035  1.00 32.12 ? 323  ASP A OD2 1 
ATOM   2439 N  N   . GLY A 1 335 ? 107.428 102.971 98.596  1.00 28.25 ? 324  GLY A N   1 
ATOM   2440 C  CA  . GLY A 1 335 ? 106.031 103.135 98.955  1.00 28.25 ? 324  GLY A CA  1 
ATOM   2441 C  C   . GLY A 1 335 ? 105.763 102.820 100.412 1.00 28.25 ? 324  GLY A C   1 
ATOM   2442 O  O   . GLY A 1 335 ? 105.064 103.566 101.099 1.00 28.25 ? 324  GLY A O   1 
ATOM   2443 N  N   . LEU A 1 336 ? 106.325 101.719 100.908 1.00 27.99 ? 325  LEU A N   1 
ATOM   2444 C  CA  . LEU A 1 336 ? 106.115 101.362 102.305 1.00 27.99 ? 325  LEU A CA  1 
ATOM   2445 C  C   . LEU A 1 336 ? 106.687 102.413 103.243 1.00 27.99 ? 325  LEU A C   1 
ATOM   2446 O  O   . LEU A 1 336 ? 106.155 102.619 104.336 1.00 27.99 ? 325  LEU A O   1 
ATOM   2447 C  CB  . LEU A 1 336 ? 106.734 99.997  102.598 1.00 27.99 ? 325  LEU A CB  1 
ATOM   2448 C  CG  . LEU A 1 336 ? 106.529 99.473  104.019 1.00 27.99 ? 325  LEU A CG  1 
ATOM   2449 C  CD1 . LEU A 1 336 ? 105.123 98.946  104.189 1.00 27.99 ? 325  LEU A CD1 1 
ATOM   2450 C  CD2 . LEU A 1 336 ? 107.542 98.398  104.335 1.00 27.99 ? 325  LEU A CD2 1 
ATOM   2451 N  N   . LEU A 1 337 ? 107.768 103.085 102.847 1.00 31.80 ? 326  LEU A N   1 
ATOM   2452 C  CA  . LEU A 1 337 ? 108.282 104.166 103.679 1.00 31.80 ? 326  LEU A CA  1 
ATOM   2453 C  C   . LEU A 1 337 ? 107.403 105.402 103.581 1.00 31.80 ? 326  LEU A C   1 
ATOM   2454 O  O   . LEU A 1 337 ? 107.359 106.205 104.517 1.00 31.80 ? 326  LEU A O   1 
ATOM   2455 C  CB  . LEU A 1 337 ? 109.717 104.503 103.285 1.00 31.80 ? 326  LEU A CB  1 
ATOM   2456 C  CG  . LEU A 1 337 ? 110.806 103.633 103.910 1.00 31.80 ? 326  LEU A CG  1 
ATOM   2457 C  CD1 . LEU A 1 337 ? 112.145 103.936 103.274 1.00 31.80 ? 326  LEU A CD1 1 
ATOM   2458 C  CD2 . LEU A 1 337 ? 110.874 103.842 105.409 1.00 31.80 ? 326  LEU A CD2 1 
ATOM   2459 N  N   . LEU A 1 338 ? 106.707 105.580 102.460 1.00 31.63 ? 327  LEU A N   1 
ATOM   2460 C  CA  . LEU A 1 338 ? 105.740 106.666 102.364 1.00 31.63 ? 327  LEU A CA  1 
ATOM   2461 C  C   . LEU A 1 338 ? 104.556 106.407 103.285 1.00 31.63 ? 327  LEU A C   1 
ATOM   2462 O  O   . LEU A 1 338 ? 104.178 107.270 104.084 1.00 31.63 ? 327  LEU A O   1 
ATOM   2463 C  CB  . LEU A 1 338 ? 105.287 106.825 100.913 1.00 31.63 ? 327  LEU A CB  1 
ATOM   2464 C  CG  . LEU A 1 338 ? 104.098 107.736 100.618 1.00 31.63 ? 327  LEU A CG  1 
ATOM   2465 C  CD1 . LEU A 1 338 ? 104.511 109.190 100.692 1.00 31.63 ? 327  LEU A CD1 1 
ATOM   2466 C  CD2 . LEU A 1 338 ? 103.535 107.412 99.253  1.00 31.63 ? 327  LEU A CD2 1 
ATOM   2467 N  N   . TYR A 1 339 ? 103.985 105.202 103.216 1.00 30.05 ? 328  TYR A N   1 
ATOM   2468 C  CA  . TYR A 1 339 ? 102.886 104.854 104.107 1.00 30.05 ? 328  TYR A CA  1 
ATOM   2469 C  C   . TYR A 1 339 ? 103.291 105.031 105.561 1.00 30.05 ? 328  TYR A C   1 
ATOM   2470 O  O   . TYR A 1 339 ? 102.578 105.668 106.343 1.00 30.05 ? 328  TYR A O   1 
ATOM   2471 C  CB  . TYR A 1 339 ? 102.438 103.416 103.853 1.00 30.05 ? 328  TYR A CB  1 
ATOM   2472 C  CG  . TYR A 1 339 ? 101.521 102.879 104.923 1.00 30.05 ? 328  TYR A CG  1 
ATOM   2473 C  CD1 . TYR A 1 339 ? 100.180 103.214 104.939 1.00 30.05 ? 328  TYR A CD1 1 
ATOM   2474 C  CD2 . TYR A 1 339 ? 101.996 102.047 105.921 1.00 30.05 ? 328  TYR A CD2 1 
ATOM   2475 C  CE1 . TYR A 1 339 ? 99.340  102.739 105.913 1.00 30.05 ? 328  TYR A CE1 1 
ATOM   2476 C  CE2 . TYR A 1 339 ? 101.159 101.565 106.901 1.00 30.05 ? 328  TYR A CE2 1 
ATOM   2477 C  CZ  . TYR A 1 339 ? 99.831  101.915 106.890 1.00 30.05 ? 328  TYR A CZ  1 
ATOM   2478 O  OH  . TYR A 1 339 ? 98.986  101.444 107.861 1.00 30.05 ? 328  TYR A OH  1 
ATOM   2479 N  N   . ILE A 1 340 ? 104.453 104.496 105.938 1.00 35.04 ? 329  ILE A N   1 
ATOM   2480 C  CA  . ILE A 1 340 ? 104.900 104.611 107.321 1.00 35.04 ? 329  ILE A CA  1 
ATOM   2481 C  C   . ILE A 1 340 ? 105.012 106.070 107.726 1.00 35.04 ? 329  ILE A C   1 
ATOM   2482 O  O   . ILE A 1 340 ? 104.839 106.408 108.902 1.00 35.04 ? 329  ILE A O   1 
ATOM   2483 C  CB  . ILE A 1 340 ? 106.237 103.873 107.521 1.00 35.04 ? 329  ILE A CB  1 
ATOM   2484 C  CG1 . ILE A 1 340 ? 106.038 102.355 107.483 1.00 35.04 ? 329  ILE A CG1 1 
ATOM   2485 C  CG2 . ILE A 1 340 ? 106.879 104.290 108.831 1.00 35.04 ? 329  ILE A CG2 1 
ATOM   2486 C  CD1 . ILE A 1 340 ? 105.110 101.811 108.544 1.00 35.04 ? 329  ILE A CD1 1 
ATOM   2487 N  N   . GLN A 1 341 ? 105.314 106.958 106.781 1.00 37.29 ? 330  GLN A N   1 
ATOM   2488 C  CA  . GLN A 1 341 ? 105.336 108.375 107.117 1.00 37.29 ? 330  GLN A CA  1 
ATOM   2489 C  C   . GLN A 1 341 ? 103.922 108.910 107.279 1.00 37.29 ? 330  GLN A C   1 
ATOM   2490 O  O   . GLN A 1 341 ? 103.625 109.619 108.244 1.00 37.29 ? 330  GLN A O   1 
ATOM   2491 C  CB  . GLN A 1 341 ? 106.091 109.166 106.054 1.00 37.29 ? 330  GLN A CB  1 
ATOM   2492 C  CG  . GLN A 1 341 ? 106.508 110.543 106.525 1.00 37.29 ? 330  GLN A CG  1 
ATOM   2493 C  CD  . GLN A 1 341 ? 107.105 111.380 105.421 1.00 37.29 ? 330  GLN A CD  1 
ATOM   2494 O  OE1 . GLN A 1 341 ? 107.041 111.019 104.248 1.00 37.29 ? 330  GLN A OE1 1 
ATOM   2495 N  NE2 . GLN A 1 341 ? 107.700 112.506 105.790 1.00 37.29 ? 330  GLN A NE2 1 
ATOM   2496 N  N   . ALA A 1 342 ? 103.027 108.555 106.357 1.00 35.40 ? 331  ALA A N   1 
ATOM   2497 C  CA  . ALA A 1 342 ? 101.650 109.026 106.447 1.00 35.40 ? 331  ALA A CA  1 
ATOM   2498 C  C   . ALA A 1 342 ? 101.029 108.629 107.778 1.00 35.40 ? 331  ALA A C   1 
ATOM   2499 O  O   . ALA A 1 342 ? 100.505 109.476 108.509 1.00 35.40 ? 331  ALA A O   1 
ATOM   2500 C  CB  . ALA A 1 342 ? 100.832 108.467 105.285 1.00 35.40 ? 331  ALA A CB  1 
ATOM   2501 N  N   . VAL A 1 343 ? 101.104 107.342 108.123 1.00 35.64 ? 332  VAL A N   1 
ATOM   2502 C  CA  . VAL A 1 343 ? 100.555 106.870 109.387 1.00 35.64 ? 332  VAL A CA  1 
ATOM   2503 C  C   . VAL A 1 343 ? 101.299 107.429 110.589 1.00 35.64 ? 332  VAL A C   1 
ATOM   2504 O  O   . VAL A 1 343 ? 100.811 107.307 111.716 1.00 35.64 ? 332  VAL A O   1 
ATOM   2505 C  CB  . VAL A 1 343 ? 100.549 105.327 109.416 1.00 35.64 ? 332  VAL A CB  1 
ATOM   2506 C  CG1 . VAL A 1 343 ? 101.953 104.779 109.329 1.00 35.64 ? 332  VAL A CG1 1 
ATOM   2507 C  CG2 . VAL A 1 343 ? 99.862  104.822 110.664 1.00 35.64 ? 332  VAL A CG2 1 
ATOM   2508 N  N   . THR A 1 344 ? 102.471 108.032 110.383 1.00 38.93 ? 333  THR A N   1 
ATOM   2509 C  CA  . THR A 1 344 ? 103.137 108.745 111.466 1.00 38.93 ? 333  THR A CA  1 
ATOM   2510 C  C   . THR A 1 344 ? 102.546 110.130 111.672 1.00 38.93 ? 333  THR A C   1 
ATOM   2511 O  O   . THR A 1 344 ? 102.508 110.619 112.805 1.00 38.93 ? 333  THR A O   1 
ATOM   2512 C  CB  . THR A 1 344 ? 104.634 108.869 111.185 1.00 38.93 ? 333  THR A CB  1 
ATOM   2513 O  OG1 . THR A 1 344 ? 105.213 107.565 111.068 1.00 38.93 ? 333  THR A OG1 1 
ATOM   2514 C  CG2 . THR A 1 344 ? 105.328 109.626 112.305 1.00 38.93 ? 333  THR A CG2 1 
ATOM   2515 N  N   . GLU A 1 345 ? 102.097 110.779 110.597 1.00 39.91 ? 334  GLU A N   1 
ATOM   2516 C  CA  . GLU A 1 345 ? 101.484 112.094 110.730 1.00 39.91 ? 334  GLU A CA  1 
ATOM   2517 C  C   . GLU A 1 345 ? 100.067 111.984 111.272 1.00 39.91 ? 334  GLU A C   1 
ATOM   2518 O  O   . GLU A 1 345 ? 99.636  112.824 112.068 1.00 39.91 ? 334  GLU A O   1 
ATOM   2519 C  CB  . GLU A 1 345 ? 101.486 112.812 109.383 1.00 39.91 ? 334  GLU A CB  1 
ATOM   2520 C  CG  . GLU A 1 345 ? 102.776 112.652 108.605 1.00 39.91 ? 334  GLU A CG  1 
ATOM   2521 C  CD  . GLU A 1 345 ? 102.835 113.536 107.383 1.00 39.91 ? 334  GLU A CD  1 
ATOM   2522 O  OE1 . GLU A 1 345 ? 101.777 114.055 106.975 1.00 39.91 ? 334  GLU A OE1 1 
ATOM   2523 O  OE2 . GLU A 1 345 ? 103.938 113.705 106.824 1.00 39.91 ? 334  GLU A OE2 1 
ATOM   2524 N  N   . THR A 1 346 ? 99.332  110.952 110.856 1.00 39.23 ? 335  THR A N   1 
ATOM   2525 C  CA  . THR A 1 346 ? 97.993  110.736 111.387 1.00 39.23 ? 335  THR A CA  1 
ATOM   2526 C  C   . THR A 1 346 ? 98.030  110.610 112.903 1.00 39.23 ? 335  THR A C   1 
ATOM   2527 O  O   . THR A 1 346 ? 97.283  111.291 113.615 1.00 39.23 ? 335  THR A O   1 
ATOM   2528 C  CB  . THR A 1 346 ? 97.380  109.488 110.751 1.00 39.23 ? 335  THR A CB  1 
ATOM   2529 O  OG1 . THR A 1 346 ? 97.480  109.578 109.326 1.00 39.23 ? 335  THR A OG1 1 
ATOM   2530 C  CG2 . THR A 1 346 ? 95.925  109.347 111.135 1.00 39.23 ? 335  THR A CG2 1 
ATOM   2531 N  N   . LEU A 1 347 ? 98.921  109.763 113.419 1.00 41.58 ? 336  LEU A N   1 
ATOM   2532 C  CA  . LEU A 1 347 ? 99.054  109.612 114.862 1.00 41.58 ? 336  LEU A CA  1 
ATOM   2533 C  C   . LEU A 1 347 ? 99.473  110.908 115.536 1.00 41.58 ? 336  LEU A C   1 
ATOM   2534 O  O   . LEU A 1 347 ? 99.294  111.047 116.751 1.00 41.58 ? 336  LEU A O   1 
ATOM   2535 C  CB  . LEU A 1 347 ? 100.070 108.520 115.188 1.00 41.58 ? 336  LEU A CB  1 
ATOM   2536 C  CG  . LEU A 1 347 ? 99.705  107.102 114.756 1.00 41.58 ? 336  LEU A CG  1 
ATOM   2537 C  CD1 . LEU A 1 347 ? 100.869 106.168 115.010 1.00 41.58 ? 336  LEU A CD1 1 
ATOM   2538 C  CD2 . LEU A 1 347 ? 98.468  106.622 115.481 1.00 41.58 ? 336  LEU A CD2 1 
ATOM   2539 N  N   . ALA A 1 348 ? 100.035 111.853 114.786 1.00 43.94 ? 337  ALA A N   1 
ATOM   2540 C  CA  . ALA A 1 348 ? 100.433 113.136 115.342 1.00 43.94 ? 337  ALA A CA  1 
ATOM   2541 C  C   . ALA A 1 348 ? 99.298  114.147 115.377 1.00 43.94 ? 337  ALA A C   1 
ATOM   2542 O  O   . ALA A 1 348 ? 99.481  115.235 115.930 1.00 43.94 ? 337  ALA A O   1 
ATOM   2543 C  CB  . ALA A 1 348 ? 101.600 113.720 114.542 1.00 43.94 ? 337  ALA A CB  1 
ATOM   2544 N  N   . HIS A 1 349 ? 98.139  113.820 114.806 1.00 46.00 ? 338  HIS A N   1 
ATOM   2545 C  CA  . HIS A 1 349 ? 97.016  114.746 114.726 1.00 46.00 ? 338  HIS A CA  1 
ATOM   2546 C  C   . HIS A 1 349 ? 95.756  114.152 115.344 1.00 46.00 ? 338  HIS A C   1 
ATOM   2547 O  O   . HIS A 1 349 ? 94.642  114.492 114.946 1.00 46.00 ? 338  HIS A O   1 
ATOM   2548 C  CB  . HIS A 1 349 ? 96.762  115.152 113.276 1.00 46.00 ? 338  HIS A CB  1 
ATOM   2549 C  CG  . HIS A 1 349 ? 97.856  115.986 112.685 1.00 46.00 ? 338  HIS A CG  1 
ATOM   2550 N  ND1 . HIS A 1 349 ? 98.292  115.830 111.387 1.00 46.00 ? 338  HIS A ND1 1 
ATOM   2551 C  CD2 . HIS A 1 349 ? 98.597  116.989 113.212 1.00 46.00 ? 338  HIS A CD2 1 
ATOM   2552 C  CE1 . HIS A 1 349 ? 99.258  116.697 111.142 1.00 46.00 ? 338  HIS A CE1 1 
ATOM   2553 N  NE2 . HIS A 1 349 ? 99.461  117.413 112.233 1.00 46.00 ? 338  HIS A NE2 1 
ATOM   2554 N  N   . GLY A 1 350 ? 95.919  113.263 116.320 1.00 44.74 ? 339  GLY A N   1 
ATOM   2555 C  CA  . GLY A 1 350 ? 94.787  112.690 117.017 1.00 44.74 ? 339  GLY A CA  1 
ATOM   2556 C  C   . GLY A 1 350 ? 94.122  111.524 116.325 1.00 44.74 ? 339  GLY A C   1 
ATOM   2557 O  O   . GLY A 1 350 ? 93.075  111.066 116.793 1.00 44.74 ? 339  GLY A O   1 
ATOM   2558 N  N   . GLY A 1 351 ? 94.689  111.027 115.228 1.00 42.06 ? 340  GLY A N   1 
ATOM   2559 C  CA  . GLY A 1 351 ? 94.129  109.902 114.513 1.00 42.06 ? 340  GLY A CA  1 
ATOM   2560 C  C   . GLY A 1 351 ? 94.605  108.576 115.071 1.00 42.06 ? 340  GLY A C   1 
ATOM   2561 O  O   . GLY A 1 351 ? 95.241  108.496 116.123 1.00 42.06 ? 340  GLY A O   1 
ATOM   2562 N  N   . THR A 1 352 ? 94.279  107.512 114.341 1.00 40.19 ? 341  THR A N   1 
ATOM   2563 C  CA  . THR A 1 352 ? 94.698  106.166 114.701 1.00 40.19 ? 341  THR A CA  1 
ATOM   2564 C  C   . THR A 1 352 ? 95.144  105.431 113.444 1.00 40.19 ? 341  THR A C   1 
ATOM   2565 O  O   . THR A 1 352 ? 94.930  105.887 112.320 1.00 40.19 ? 341  THR A O   1 
ATOM   2566 C  CB  . THR A 1 352 ? 93.579  105.399 115.414 1.00 40.19 ? 341  THR A CB  1 
ATOM   2567 O  OG1 . THR A 1 352 ? 94.045  104.093 115.770 1.00 40.19 ? 341  THR A OG1 1 
ATOM   2568 C  CG2 . THR A 1 352 ? 92.353  105.276 114.524 1.00 40.19 ? 341  THR A CG2 1 
ATOM   2569 N  N   . VAL A 1 353 ? 95.777  104.273 113.650 1.00 38.02 ? 342  VAL A N   1 
ATOM   2570 C  CA  . VAL A 1 353 ? 96.337  103.515 112.538 1.00 38.02 ? 342  VAL A CA  1 
ATOM   2571 C  C   . VAL A 1 353 ? 95.259  102.925 111.639 1.00 38.02 ? 342  VAL A C   1 
ATOM   2572 O  O   . VAL A 1 353 ? 95.549  102.543 110.501 1.00 38.02 ? 342  VAL A O   1 
ATOM   2573 C  CB  . VAL A 1 353 ? 97.256  102.405 113.078 1.00 38.02 ? 342  VAL A CB  1 
ATOM   2574 C  CG1 . VAL A 1 353 ? 97.676  101.470 111.965 1.00 38.02 ? 342  VAL A CG1 1 
ATOM   2575 C  CG2 . VAL A 1 353 ? 98.469  103.015 113.742 1.00 38.02 ? 342  VAL A CG2 1 
ATOM   2576 N  N   . THR A 1 354 ? 94.021  102.842 112.113 1.00 39.78 ? 343  THR A N   1 
ATOM   2577 C  CA  . THR A 1 354 ? 92.943  102.229 111.352 1.00 39.78 ? 343  THR A CA  1 
ATOM   2578 C  C   . THR A 1 354 ? 92.158  103.232 110.518 1.00 39.78 ? 343  THR A C   1 
ATOM   2579 O  O   . THR A 1 354 ? 91.184  102.843 109.866 1.00 39.78 ? 343  THR A O   1 
ATOM   2580 C  CB  . THR A 1 354 ? 91.990  101.494 112.297 1.00 39.78 ? 343  THR A CB  1 
ATOM   2581 O  OG1 . THR A 1 354 ? 91.755  102.295 113.461 1.00 39.78 ? 343  THR A OG1 1 
ATOM   2582 C  CG2 . THR A 1 354 ? 92.584  100.164 112.718 1.00 39.78 ? 343  THR A CG2 1 
ATOM   2583 N  N   . ASP A 1 355 ? 92.549  104.504 110.521 1.00 37.92 ? 344  ASP A N   1 
ATOM   2584 C  CA  . ASP A 1 355 ? 91.899  105.524 109.700 1.00 37.92 ? 344  ASP A CA  1 
ATOM   2585 C  C   . ASP A 1 355 ? 92.460  105.418 108.290 1.00 37.92 ? 344  ASP A C   1 
ATOM   2586 O  O   . ASP A 1 355 ? 93.428  106.085 107.930 1.00 37.92 ? 344  ASP A O   1 
ATOM   2587 C  CB  . ASP A 1 355 ? 92.125  106.912 110.282 1.00 37.92 ? 344  ASP A CB  1 
ATOM   2588 C  CG  . ASP A 1 355 ? 91.397  107.120 111.590 1.00 37.92 ? 344  ASP A CG  1 
ATOM   2589 O  OD1 . ASP A 1 355 ? 90.337  106.492 111.787 1.00 37.92 ? 344  ASP A OD1 1 
ATOM   2590 O  OD2 . ASP A 1 355 ? 91.885  107.911 112.423 1.00 37.92 ? 344  ASP A OD2 1 
ATOM   2591 N  N   . GLY A 1 356 ? 91.844  104.562 107.478 1.00 31.76 ? 345  GLY A N   1 
ATOM   2592 C  CA  . GLY A 1 356 ? 92.319  104.391 106.118 1.00 31.76 ? 345  GLY A CA  1 
ATOM   2593 C  C   . GLY A 1 356 ? 92.211  105.661 105.299 1.00 31.76 ? 345  GLY A C   1 
ATOM   2594 O  O   . GLY A 1 356 ? 93.133  106.015 104.563 1.00 31.76 ? 345  GLY A O   1 
ATOM   2595 N  N   . GLU A 1 357 ? 91.087  106.369 105.424 1.00 32.09 ? 346  GLU A N   1 
ATOM   2596 C  CA  . GLU A 1 357 ? 90.851  107.539 104.585 1.00 32.09 ? 346  GLU A CA  1 
ATOM   2597 C  C   . GLU A 1 357 ? 91.798  108.679 104.932 1.00 32.09 ? 346  GLU A C   1 
ATOM   2598 O  O   . GLU A 1 357 ? 92.330  109.343 104.036 1.00 32.09 ? 346  GLU A O   1 
ATOM   2599 C  CB  . GLU A 1 357 ? 89.399  107.991 104.721 1.00 32.09 ? 346  GLU A CB  1 
ATOM   2600 C  CG  . GLU A 1 357 ? 88.428  107.208 103.852 1.00 32.09 ? 346  GLU A CG  1 
ATOM   2601 C  CD  . GLU A 1 357 ? 87.690  106.127 104.616 1.00 32.09 ? 346  GLU A CD  1 
ATOM   2602 O  OE1 . GLU A 1 357 ? 86.546  105.808 104.234 1.00 32.09 ? 346  GLU A OE1 1 
ATOM   2603 O  OE2 . GLU A 1 357 ? 88.251  105.594 105.595 1.00 32.09 ? 346  GLU A OE2 1 
ATOM   2604 N  N   . ASN A 1 358 ? 92.012  108.934 106.221 1.00 35.16 ? 347  ASN A N   1 
ATOM   2605 C  CA  . ASN A 1 358 ? 92.911  110.013 106.612 1.00 35.16 ? 347  ASN A CA  1 
ATOM   2606 C  C   . ASN A 1 358 ? 94.359  109.679 106.292 1.00 35.16 ? 347  ASN A C   1 
ATOM   2607 O  O   . ASN A 1 358 ? 95.145  110.577 105.974 1.00 35.16 ? 347  ASN A O   1 
ATOM   2608 C  CB  . ASN A 1 358 ? 92.758  110.313 108.100 1.00 35.16 ? 347  ASN A CB  1 
ATOM   2609 C  CG  . ASN A 1 358 ? 91.682  111.337 108.379 1.00 35.16 ? 347  ASN A CG  1 
ATOM   2610 O  OD1 . ASN A 1 358 ? 90.608  111.305 107.781 1.00 35.16 ? 347  ASN A OD1 1 
ATOM   2611 N  ND2 . ASN A 1 358 ? 91.966  112.259 109.289 1.00 35.16 ? 347  ASN A ND2 1 
ATOM   2612 N  N   . ILE A 1 359 ? 94.736  108.405 106.388 1.00 33.96 ? 348  ILE A N   1 
ATOM   2613 C  CA  . ILE A 1 359 ? 96.097  108.004 106.049 1.00 33.96 ? 348  ILE A CA  1 
ATOM   2614 C  C   . ILE A 1 359 ? 96.332  108.147 104.552 1.00 33.96 ? 348  ILE A C   1 
ATOM   2615 O  O   . ILE A 1 359 ? 97.345  108.702 104.117 1.00 33.96 ? 348  ILE A O   1 
ATOM   2616 C  CB  . ILE A 1 359 ? 96.360  106.563 106.518 1.00 33.96 ? 348  ILE A CB  1 
ATOM   2617 C  CG1 . ILE A 1 359 ? 96.400  106.501 108.042 1.00 33.96 ? 348  ILE A CG1 1 
ATOM   2618 C  CG2 . ILE A 1 359 ? 97.659  106.053 105.932 1.00 33.96 ? 348  ILE A CG2 1 
ATOM   2619 C  CD1 . ILE A 1 359 ? 96.352  105.106 108.591 1.00 33.96 ? 348  ILE A CD1 1 
ATOM   2620 N  N   . THR A 1 360 ? 95.394  107.654 103.743 1.00 30.69 ? 349  THR A N   1 
ATOM   2621 C  CA  . THR A 1 360 ? 95.581  107.674 102.298 1.00 30.69 ? 349  THR A CA  1 
ATOM   2622 C  C   . THR A 1 360 ? 95.619  109.098 101.763 1.00 30.69 ? 349  THR A C   1 
ATOM   2623 O  O   . THR A 1 360 ? 96.393  109.401 100.850 1.00 30.69 ? 349  THR A O   1 
ATOM   2624 C  CB  . THR A 1 360 ? 94.474  106.874 101.621 1.00 30.69 ? 349  THR A CB  1 
ATOM   2625 O  OG1 . THR A 1 360 ? 94.501  105.526 102.097 1.00 30.69 ? 349  THR A OG1 1 
ATOM   2626 C  CG2 . THR A 1 360 ? 94.666  106.865 100.134 1.00 30.69 ? 349  THR A CG2 1 
ATOM   2627 N  N   . GLN A 1 361 ? 94.796  109.989 102.315 1.00 34.49 ? 350  GLN A N   1 
ATOM   2628 C  CA  . GLN A 1 361 ? 94.812  111.376 101.871 1.00 34.49 ? 350  GLN A CA  1 
ATOM   2629 C  C   . GLN A 1 361 ? 96.158  112.040 102.115 1.00 34.49 ? 350  GLN A C   1 
ATOM   2630 O  O   . GLN A 1 361 ? 96.448  113.070 101.500 1.00 34.49 ? 350  GLN A O   1 
ATOM   2631 C  CB  . GLN A 1 361 ? 93.716  112.166 102.581 1.00 34.49 ? 350  GLN A CB  1 
ATOM   2632 C  CG  . GLN A 1 361 ? 92.327  111.923 102.030 1.00 34.49 ? 350  GLN A CG  1 
ATOM   2633 C  CD  . GLN A 1 361 ? 91.261  112.670 102.802 1.00 34.49 ? 350  GLN A CD  1 
ATOM   2634 O  OE1 . GLN A 1 361 ? 91.549  113.325 103.802 1.00 34.49 ? 350  GLN A OE1 1 
ATOM   2635 N  NE2 . GLN A 1 361 ? 90.019  112.573 102.342 1.00 34.49 ? 350  GLN A NE2 1 
ATOM   2636 N  N   . ARG A 1 362 ? 96.980  111.484 102.999 1.00 36.85 ? 351  ARG A N   1 
ATOM   2637 C  CA  . ARG A 1 362 ? 98.303  112.022 103.276 1.00 36.85 ? 351  ARG A CA  1 
ATOM   2638 C  C   . ARG A 1 362 ? 99.398  111.351 102.461 1.00 36.85 ? 351  ARG A C   1 
ATOM   2639 O  O   . ARG A 1 362 ? 100.571 111.687 102.638 1.00 36.85 ? 351  ARG A O   1 
ATOM   2640 C  CB  . ARG A 1 362 ? 98.619  111.879 104.761 1.00 36.85 ? 351  ARG A CB  1 
ATOM   2641 C  CG  . ARG A 1 362 ? 97.772  112.759 105.635 1.00 36.85 ? 351  ARG A CG  1 
ATOM   2642 C  CD  . ARG A 1 362 ? 98.284  112.782 107.049 1.00 36.85 ? 351  ARG A CD  1 
ATOM   2643 N  NE  . ARG A 1 362 ? 97.302  113.373 107.951 1.00 36.85 ? 351  ARG A NE  1 
ATOM   2644 C  CZ  . ARG A 1 362 ? 97.356  114.611 108.430 1.00 36.85 ? 351  ARG A CZ  1 
ATOM   2645 N  NH1 . ARG A 1 362 ? 98.348  115.429 108.101 1.00 36.85 ? 351  ARG A NH1 1 
ATOM   2646 N  NH2 . ARG A 1 362 ? 96.401  115.036 109.243 1.00 36.85 ? 351  ARG A NH2 1 
ATOM   2647 N  N   . MET A 1 363 ? 99.049  110.412 101.583 1.00 31.44 ? 352  MET A N   1 
ATOM   2648 C  CA  . MET A 1 363 ? 100.003 109.799 100.672 1.00 31.44 ? 352  MET A CA  1 
ATOM   2649 C  C   . MET A 1 363 ? 99.886  110.316 99.253  1.00 31.44 ? 352  MET A C   1 
ATOM   2650 O  O   . MET A 1 363 ? 100.896 110.414 98.560  1.00 31.44 ? 352  MET A O   1 
ATOM   2651 C  CB  . MET A 1 363 ? 99.815  108.278 100.636 1.00 31.44 ? 352  MET A CB  1 
ATOM   2652 C  CG  . MET A 1 363 ? 99.604  107.630 101.986 1.00 31.44 ? 352  MET A CG  1 
ATOM   2653 S  SD  . MET A 1 363 ? 99.532  105.830 101.929 1.00 31.44 ? 352  MET A SD  1 
ATOM   2654 C  CE  . MET A 1 363 ? 100.832 105.445 100.770 1.00 31.44 ? 352  MET A CE  1 
ATOM   2655 N  N   . TRP A 1 364 ? 98.684  110.656 98.812  1.00 30.97 ? 353  TRP A N   1 
ATOM   2656 C  CA  . TRP A 1 364 ? 98.458  111.129 97.459  1.00 30.97 ? 353  TRP A CA  1 
ATOM   2657 C  C   . TRP A 1 364 ? 98.753  112.619 97.362  1.00 30.97 ? 353  TRP A C   1 
ATOM   2658 O  O   . TRP A 1 364 ? 98.739  113.348 98.355  1.00 30.97 ? 353  TRP A O   1 
ATOM   2659 C  CB  . TRP A 1 364 ? 97.016  110.865 97.021  1.00 30.97 ? 353  TRP A CB  1 
ATOM   2660 C  CG  . TRP A 1 364 ? 96.542  109.445 97.152  1.00 30.97 ? 353  TRP A CG  1 
ATOM   2661 C  CD1 . TRP A 1 364 ? 97.263  108.363 97.563  1.00 30.97 ? 353  TRP A CD1 1 
ATOM   2662 C  CD2 . TRP A 1 364 ? 95.230  108.960 96.856  1.00 30.97 ? 353  TRP A CD2 1 
ATOM   2663 N  NE1 . TRP A 1 364 ? 96.481  107.235 97.538  1.00 30.97 ? 353  TRP A NE1 1 
ATOM   2664 C  CE2 . TRP A 1 364 ? 95.227  107.576 97.107  1.00 30.97 ? 353  TRP A CE2 1 
ATOM   2665 C  CE3 . TRP A 1 364 ? 94.057  109.564 96.399  1.00 30.97 ? 353  TRP A CE3 1 
ATOM   2666 C  CZ2 . TRP A 1 364 ? 94.095  106.789 96.921  1.00 30.97 ? 353  TRP A CZ2 1 
ATOM   2667 C  CZ3 . TRP A 1 364 ? 92.939  108.782 96.215  1.00 30.97 ? 353  TRP A CZ3 1 
ATOM   2668 C  CH2 . TRP A 1 364 ? 92.964  107.410 96.473  1.00 30.97 ? 353  TRP A CH2 1 
ATOM   2669 N  N   . ASN A 1 365 ? 98.850  113.147 96.163  1.00 37.82 ? 354  ASN A N   1 
ATOM   2670 C  CA  . ASN A 1 365 ? 99.111  114.582 95.898  1.00 37.82 ? 354  ASN A CA  1 
ATOM   2671 C  C   . ASN A 1 365 ? 100.325 115.090 96.672  1.00 37.82 ? 354  ASN A C   1 
ATOM   2672 O  O   . ASN A 1 365 ? 100.381 116.282 96.822  1.00 37.82 ? 354  ASN A O   1 
ATOM   2673 C  CB  . ASN A 1 365 ? 97.857  115.408 96.102  1.00 37.82 ? 354  ASN A CB  1 
ATOM   2674 C  CG  . ASN A 1 365 ? 97.954  116.752 95.455  1.00 37.82 ? 354  ASN A CG  1 
ATOM   2675 O  OD1 . ASN A 1 365 ? 98.601  116.902 94.442  1.00 37.82 ? 354  ASN A OD1 1 
ATOM   2676 N  ND2 . ASN A 1 365 ? 97.310  117.724 96.051  1.00 37.82 ? 354  ASN A ND2 1 
ATOM   2677 N  N   . ARG A 1 366 ? 101.333 114.293 97.016  1.00 37.76 ? 355  ARG A N   1 
ATOM   2678 C  CA  . ARG A 1 366 ? 102.498 114.780 97.739  1.00 37.76 ? 355  ARG A CA  1 
ATOM   2679 C  C   . ARG A 1 366 ? 103.748 114.128 97.170  1.00 37.76 ? 355  ARG A C   1 
ATOM   2680 O  O   . ARG A 1 366 ? 103.685 113.094 96.503  1.00 37.76 ? 355  ARG A O   1 
ATOM   2681 C  CB  . ARG A 1 366 ? 102.385 114.510 99.249  1.00 37.76 ? 355  ARG A CB  1 
ATOM   2682 C  CG  . ARG A 1 366 ? 102.877 113.144 99.693  1.00 37.76 ? 355  ARG A CG  1 
ATOM   2683 C  CD  . ARG A 1 366 ? 102.858 112.987 101.203 1.00 37.76 ? 355  ARG A CD  1 
ATOM   2684 N  NE  . ARG A 1 366 ? 103.818 113.860 101.870 1.00 37.76 ? 355  ARG A NE  1 
ATOM   2685 C  CZ  . ARG A 1 366 ? 103.798 114.139 103.170 1.00 37.76 ? 355  ARG A CZ  1 
ATOM   2686 N  NH1 . ARG A 1 366 ? 102.875 113.602 103.955 1.00 37.76 ? 355  ARG A NH1 1 
ATOM   2687 N  NH2 . ARG A 1 366 ? 104.713 114.945 103.690 1.00 37.76 ? 355  ARG A NH2 1 
ATOM   2688 N  N   . SER A 1 367 ? 104.891 114.750 97.442  1.00 37.28 ? 356  SER A N   1 
ATOM   2689 C  CA  . SER A 1 367 ? 106.179 114.261 96.978  1.00 37.28 ? 356  SER A CA  1 
ATOM   2690 C  C   . SER A 1 367 ? 106.953 113.637 98.130  1.00 37.28 ? 356  SER A C   1 
ATOM   2691 O  O   . SER A 1 367 ? 106.804 114.027 99.291  1.00 37.28 ? 356  SER A O   1 
ATOM   2692 C  CB  . SER A 1 367 ? 107.009 115.383 96.355  1.00 37.28 ? 356  SER A CB  1 
ATOM   2693 O  OG  . SER A 1 367 ? 106.373 115.907 95.206  1.00 37.28 ? 356  SER A OG  1 
ATOM   2694 N  N   . PHE A 1 368 ? 107.790 112.664 97.787  1.00 34.16 ? 357  PHE A N   1 
ATOM   2695 C  CA  . PHE A 1 368 ? 108.545 111.891 98.758  1.00 34.16 ? 357  PHE A CA  1 
ATOM   2696 C  C   . PHE A 1 368 ? 109.967 111.714 98.249  1.00 34.16 ? 357  PHE A C   1 
ATOM   2697 O  O   . PHE A 1 368 ? 110.224 111.779 97.045  1.00 34.16 ? 357  PHE A O   1 
ATOM   2698 C  CB  . PHE A 1 368 ? 107.887 110.526 99.009  1.00 34.16 ? 357  PHE A CB  1 
ATOM   2699 C  CG  . PHE A 1 368 ? 108.506 109.749 100.131 1.00 34.16 ? 357  PHE A CG  1 
ATOM   2700 C  CD1 . PHE A 1 368 ? 108.312 110.130 101.445 1.00 34.16 ? 357  PHE A CD1 1 
ATOM   2701 C  CD2 . PHE A 1 368 ? 109.281 108.633 99.874  1.00 34.16 ? 357  PHE A CD2 1 
ATOM   2702 C  CE1 . PHE A 1 368 ? 108.881 109.419 102.477 1.00 34.16 ? 357  PHE A CE1 1 
ATOM   2703 C  CE2 . PHE A 1 368 ? 109.852 107.920 100.905 1.00 34.16 ? 357  PHE A CE2 1 
ATOM   2704 C  CZ  . PHE A 1 368 ? 109.651 108.314 102.206 1.00 34.16 ? 357  PHE A CZ  1 
ATOM   2705 N  N   . GLN A 1 369 ? 110.892 111.508 99.180  1.00 36.71 ? 358  GLN A N   1 
ATOM   2706 C  CA  . GLN A 1 369 ? 112.299 111.291 98.866  1.00 36.71 ? 358  GLN A CA  1 
ATOM   2707 C  C   . GLN A 1 369 ? 112.636 109.842 99.194  1.00 36.71 ? 358  GLN A C   1 
ATOM   2708 O  O   . GLN A 1 369 ? 112.618 109.446 100.363 1.00 36.71 ? 358  GLN A O   1 
ATOM   2709 C  CB  . GLN A 1 369 ? 113.185 112.256 99.651  1.00 36.71 ? 358  GLN A CB  1 
ATOM   2710 C  CG  . GLN A 1 369 ? 114.676 111.955 99.573  1.00 36.71 ? 358  GLN A CG  1 
ATOM   2711 C  CD  . GLN A 1 369 ? 115.244 112.189 98.192  1.00 36.71 ? 358  GLN A CD  1 
ATOM   2712 O  OE1 . GLN A 1 369 ? 114.739 113.013 97.434  1.00 36.71 ? 358  GLN A OE1 1 
ATOM   2713 N  NE2 . GLN A 1 369 ? 116.299 111.462 97.855  1.00 36.71 ? 358  GLN A NE2 1 
ATOM   2714 N  N   . GLY A 1 370 ? 112.947 109.059 98.165  1.00 35.02 ? 359  GLY A N   1 
ATOM   2715 C  CA  . GLY A 1 370 ? 113.297 107.665 98.352  1.00 35.02 ? 359  GLY A CA  1 
ATOM   2716 C  C   . GLY A 1 370 ? 114.581 107.289 97.645  1.00 35.02 ? 359  GLY A C   1 
ATOM   2717 O  O   . GLY A 1 370 ? 115.285 108.159 97.127  1.00 35.02 ? 359  GLY A O   1 
ATOM   2718 N  N   . VAL A 1 371 ? 114.900 105.994 97.617  1.00 33.92 ? 360  VAL A N   1 
ATOM   2719 C  CA  . VAL A 1 371 ? 116.102 105.553 96.916  1.00 33.92 ? 360  VAL A CA  1 
ATOM   2720 C  C   . VAL A 1 371 ? 115.976 105.807 95.422  1.00 33.92 ? 360  VAL A C   1 
ATOM   2721 O  O   . VAL A 1 371 ? 116.970 106.106 94.751  1.00 33.92 ? 360  VAL A O   1 
ATOM   2722 C  CB  . VAL A 1 371 ? 116.393 104.070 97.208  1.00 33.92 ? 360  VAL A CB  1 
ATOM   2723 C  CG1 . VAL A 1 371 ? 116.882 103.902 98.632  1.00 33.92 ? 360  VAL A CG1 1 
ATOM   2724 C  CG2 . VAL A 1 371 ? 115.166 103.211 96.953  1.00 33.92 ? 360  VAL A CG2 1 
ATOM   2725 N  N   . THR A 1 372 ? 114.768 105.697 94.873  1.00 34.40 ? 361  THR A N   1 
ATOM   2726 C  CA  . THR A 1 372 ? 114.531 105.894 93.451  1.00 34.40 ? 361  THR A CA  1 
ATOM   2727 C  C   . THR A 1 372 ? 114.348 107.361 93.084  1.00 34.40 ? 361  THR A C   1 
ATOM   2728 O  O   . THR A 1 372 ? 113.764 107.660 92.038  1.00 34.40 ? 361  THR A O   1 
ATOM   2729 C  CB  . THR A 1 372 ? 113.307 105.090 93.008  1.00 34.40 ? 361  THR A CB  1 
ATOM   2730 O  OG1 . THR A 1 372 ? 113.500 103.706 93.321  1.00 34.40 ? 361  THR A OG1 1 
ATOM   2731 C  CG2 . THR A 1 372 ? 113.081 105.240 91.521  1.00 34.40 ? 361  THR A CG2 1 
ATOM   2732 N  N   . GLY A 1 373 ? 114.826 108.276 93.917  1.00 36.47 ? 362  GLY A N   1 
ATOM   2733 C  CA  . GLY A 1 373 ? 114.775 109.689 93.618  1.00 36.47 ? 362  GLY A CA  1 
ATOM   2734 C  C   . GLY A 1 373 ? 113.657 110.405 94.345  1.00 36.47 ? 362  GLY A C   1 
ATOM   2735 O  O   . GLY A 1 373 ? 113.125 109.945 95.356  1.00 36.47 ? 362  GLY A O   1 
ATOM   2736 N  N   . TYR A 1 374 ? 113.306 111.569 93.809  1.00 39.56 ? 363  TYR A N   1 
ATOM   2737 C  CA  . TYR A 1 374 ? 112.214 112.384 94.336  1.00 39.56 ? 363  TYR A CA  1 
ATOM   2738 C  C   . TYR A 1 374 ? 110.949 112.013 93.574  1.00 39.56 ? 363  TYR A C   1 
ATOM   2739 O  O   . TYR A 1 374 ? 110.742 112.456 92.444  1.00 39.56 ? 363  TYR A O   1 
ATOM   2740 C  CB  . TYR A 1 374 ? 112.540 113.867 94.194  1.00 39.56 ? 363  TYR A CB  1 
ATOM   2741 C  CG  . TYR A 1 374 ? 111.846 114.748 95.204  1.00 39.56 ? 363  TYR A CG  1 
ATOM   2742 C  CD1 . TYR A 1 374 ? 112.274 114.795 96.520  1.00 39.56 ? 363  TYR A CD1 1 
ATOM   2743 C  CD2 . TYR A 1 374 ? 110.765 115.532 94.841  1.00 39.56 ? 363  TYR A CD2 1 
ATOM   2744 C  CE1 . TYR A 1 374 ? 111.644 115.596 97.445  1.00 39.56 ? 363  TYR A CE1 1 
ATOM   2745 C  CE2 . TYR A 1 374 ? 110.131 116.335 95.759  1.00 39.56 ? 363  TYR A CE2 1 
ATOM   2746 C  CZ  . TYR A 1 374 ? 110.572 116.362 97.060  1.00 39.56 ? 363  TYR A CZ  1 
ATOM   2747 O  OH  . TYR A 1 374 ? 109.938 117.164 97.979  1.00 39.56 ? 363  TYR A OH  1 
ATOM   2748 N  N   . LEU A 1 375 ? 110.097 111.200 94.189  1.00 34.41 ? 364  LEU A N   1 
ATOM   2749 C  CA  . LEU A 1 375 ? 108.898 110.718 93.522  1.00 34.41 ? 364  LEU A CA  1 
ATOM   2750 C  C   . LEU A 1 375 ? 107.683 111.560 93.891  1.00 34.41 ? 364  LEU A C   1 
ATOM   2751 O  O   . LEU A 1 375 ? 107.650 112.245 94.914  1.00 34.41 ? 364  LEU A O   1 
ATOM   2752 C  CB  . LEU A 1 375 ? 108.625 109.241 93.839  1.00 34.41 ? 364  LEU A CB  1 
ATOM   2753 C  CG  . LEU A 1 375 ? 108.352 108.776 95.270  1.00 34.41 ? 364  LEU A CG  1 
ATOM   2754 C  CD1 . LEU A 1 375 ? 106.921 109.056 95.656  1.00 34.41 ? 364  LEU A CD1 1 
ATOM   2755 C  CD2 . LEU A 1 375 ? 108.589 107.299 95.375  1.00 34.41 ? 364  LEU A CD2 1 
ATOM   2756 N  N   . LYS A 1 376 ? 106.679 111.496 93.020  1.00 34.54 ? 365  LYS A N   1 
ATOM   2757 C  CA  . LYS A 1 376 ? 105.439 112.247 93.147  1.00 34.54 ? 365  LYS A CA  1 
ATOM   2758 C  C   . LYS A 1 376 ? 104.275 111.281 93.010  1.00 34.54 ? 365  LYS A C   1 
ATOM   2759 O  O   . LYS A 1 376 ? 104.239 110.482 92.071  1.00 34.54 ? 365  LYS A O   1 
ATOM   2760 C  CB  . LYS A 1 376 ? 105.357 113.341 92.074  1.00 34.54 ? 365  LYS A CB  1 
ATOM   2761 C  CG  . LYS A 1 376 ? 104.058 114.131 92.039  1.00 34.54 ? 365  LYS A CG  1 
ATOM   2762 C  CD  . LYS A 1 376 ? 103.891 114.993 93.267  1.00 34.54 ? 365  LYS A CD  1 
ATOM   2763 C  CE  . LYS A 1 376 ? 102.863 116.089 93.048  1.00 34.54 ? 365  LYS A CE  1 
ATOM   2764 N  NZ  . LYS A 1 376 ? 101.835 115.718 92.042  1.00 34.54 ? 365  LYS A NZ  1 
ATOM   2765 N  N   . ILE A 1 377 ? 103.332 111.351 93.942  1.00 32.28 ? 366  ILE A N   1 
ATOM   2766 C  CA  . ILE A 1 377 ? 102.101 110.572 93.877  1.00 32.28 ? 366  ILE A CA  1 
ATOM   2767 C  C   . ILE A 1 377 ? 101.002 111.530 93.440  1.00 32.28 ? 366  ILE A C   1 
ATOM   2768 O  O   . ILE A 1 377 ? 100.623 112.435 94.188  1.00 32.28 ? 366  ILE A O   1 
ATOM   2769 C  CB  . ILE A 1 377 ? 101.768 109.916 95.224  1.00 32.28 ? 366  ILE A CB  1 
ATOM   2770 C  CG1 . ILE A 1 377 ? 102.926 109.049 95.716  1.00 32.28 ? 366  ILE A CG1 1 
ATOM   2771 C  CG2 . ILE A 1 377 ? 100.525 109.064 95.095  1.00 32.28 ? 366  ILE A CG2 1 
ATOM   2772 C  CD1 . ILE A 1 377 ? 103.022 107.707 95.042  1.00 32.28 ? 366  ILE A CD1 1 
ATOM   2773 N  N   . ASP A 1 378 ? 100.484 111.342 92.230  1.00 33.31 ? 367  ASP A N   1 
ATOM   2774 C  CA  . ASP A 1 378 ? 99.503  112.272 91.699  1.00 33.31 ? 367  ASP A CA  1 
ATOM   2775 C  C   . ASP A 1 378 ? 98.236  112.246 92.554  1.00 33.31 ? 367  ASP A C   1 
ATOM   2776 O  O   . ASP A 1 378 ? 98.076  111.425 93.457  1.00 33.31 ? 367  ASP A O   1 
ATOM   2777 C  CB  . ASP A 1 378 ? 99.179  111.937 90.246  1.00 33.31 ? 367  ASP A CB  1 
ATOM   2778 C  CG  . ASP A 1 378 ? 98.397  110.657 90.106  1.00 33.31 ? 367  ASP A CG  1 
ATOM   2779 O  OD1 . ASP A 1 378 ? 97.700  110.487 89.086  1.00 33.31 ? 367  ASP A OD1 1 
ATOM   2780 O  OD2 . ASP A 1 378 ? 98.462  109.825 91.029  1.00 33.31 ? 367  ASP A OD2 1 
ATOM   2781 N  N   . SER A 1 379 ? 97.324  113.169 92.255  1.00 36.58 ? 368  SER A N   1 
ATOM   2782 C  CA  . SER A 1 379 ? 96.127  113.331 93.069  1.00 36.58 ? 368  SER A CA  1 
ATOM   2783 C  C   . SER A 1 379 ? 95.201  112.127 93.011  1.00 36.58 ? 368  SER A C   1 
ATOM   2784 O  O   . SER A 1 379 ? 94.285  112.039 93.834  1.00 36.58 ? 368  SER A O   1 
ATOM   2785 C  CB  . SER A 1 379 ? 95.363  114.576 92.629  1.00 36.58 ? 368  SER A CB  1 
ATOM   2786 O  OG  . SER A 1 379 ? 94.570  114.301 91.492  1.00 36.58 ? 368  SER A OG  1 
ATOM   2787 N  N   . SER A 1 380 ? 95.399  111.214 92.064  1.00 32.90 ? 369  SER A N   1 
ATOM   2788 C  CA  . SER A 1 380 ? 94.574  110.020 91.957  1.00 32.90 ? 369  SER A CA  1 
ATOM   2789 C  C   . SER A 1 380 ? 95.169  108.812 92.663  1.00 32.90 ? 369  SER A C   1 
ATOM   2790 O  O   . SER A 1 380 ? 94.483  107.795 92.787  1.00 32.90 ? 369  SER A O   1 
ATOM   2791 C  CB  . SER A 1 380 ? 94.341  109.669 90.487  1.00 32.90 ? 369  SER A CB  1 
ATOM   2792 O  OG  . SER A 1 380 ? 93.568  108.490 90.372  1.00 32.90 ? 369  SER A OG  1 
ATOM   2793 N  N   . GLY A 1 381 ? 96.412  108.891 93.123  1.00 30.41 ? 370  GLY A N   1 
ATOM   2794 C  CA  . GLY A 1 381 ? 97.026  107.813 93.867  1.00 30.41 ? 370  GLY A CA  1 
ATOM   2795 C  C   . GLY A 1 381 ? 98.007  106.956 93.103  1.00 30.41 ? 370  GLY A C   1 
ATOM   2796 O  O   . GLY A 1 381 ? 98.411  105.911 93.620  1.00 30.41 ? 370  GLY A O   1 
ATOM   2797 N  N   . ASP A 1 382 ? 98.402  107.353 91.899  1.00 30.68 ? 371  ASP A N   1 
ATOM   2798 C  CA  . ASP A 1 382 ? 99.377  106.623 91.105  1.00 30.68 ? 371  ASP A CA  1 
ATOM   2799 C  C   . ASP A 1 382 ? 100.663 107.430 91.012  1.00 30.68 ? 371  ASP A C   1 
ATOM   2800 O  O   . ASP A 1 382 ? 100.628 108.660 90.938  1.00 30.68 ? 371  ASP A O   1 
ATOM   2801 C  CB  . ASP A 1 382 ? 98.846  106.337 89.702  1.00 30.68 ? 371  ASP A CB  1 
ATOM   2802 C  CG  . ASP A 1 382 ? 97.473  105.713 89.715  1.00 30.68 ? 371  ASP A CG  1 
ATOM   2803 O  OD1 . ASP A 1 382 ? 97.199  104.894 90.613  1.00 30.68 ? 371  ASP A OD1 1 
ATOM   2804 O  OD2 . ASP A 1 382 ? 96.668  106.038 88.821  1.00 30.68 ? 371  ASP A OD2 1 
ATOM   2805 N  N   . ARG A 1 383 ? 101.796 106.740 91.020  1.00 31.88 ? 372  ARG A N   1 
ATOM   2806 C  CA  . ARG A 1 383 ? 103.074 107.427 90.938  1.00 31.88 ? 372  ARG A CA  1 
ATOM   2807 C  C   . ARG A 1 383 ? 103.306 107.959 89.533  1.00 31.88 ? 372  ARG A C   1 
ATOM   2808 O  O   . ARG A 1 383 ? 102.910 107.337 88.545  1.00 31.88 ? 372  ARG A O   1 
ATOM   2809 C  CB  . ARG A 1 383 ? 104.210 106.491 91.328  1.00 31.88 ? 372  ARG A CB  1 
ATOM   2810 C  CG  . ARG A 1 383 ? 105.344 107.202 92.031  1.00 31.88 ? 372  ARG A CG  1 
ATOM   2811 C  CD  . ARG A 1 383 ? 106.611 106.385 92.058  1.00 31.88 ? 372  ARG A CD  1 
ATOM   2812 N  NE  . ARG A 1 383 ? 107.019 105.955 90.730  1.00 31.88 ? 372  ARG A NE  1 
ATOM   2813 C  CZ  . ARG A 1 383 ? 108.129 105.275 90.482  1.00 31.88 ? 372  ARG A CZ  1 
ATOM   2814 N  NH1 . ARG A 1 383 ? 108.946 104.952 91.475  1.00 31.88 ? 372  ARG A NH1 1 
ATOM   2815 N  NH2 . ARG A 1 383 ? 108.425 104.920 89.241  1.00 31.88 ? 372  ARG A NH2 1 
ATOM   2816 N  N   . GLU A 1 384 ? 103.955 109.116 89.447  1.00 33.65 ? 373  GLU A N   1 
ATOM   2817 C  CA  . GLU A 1 384 ? 104.314 109.706 88.162  1.00 33.65 ? 373  GLU A CA  1 
ATOM   2818 C  C   . GLU A 1 384 ? 105.610 109.066 87.683  1.00 33.65 ? 373  GLU A C   1 
ATOM   2819 O  O   . GLU A 1 384 ? 106.608 109.284 88.305  1.00 33.65 ? 373  GLU A O   1 
ATOM   2820 C  CB  . GLU A 1 384 ? 104.756 111.148 88.326  1.00 30.00 ? 373  GLU A CB  1 
ATOM   2821 C  CG  . GLU A 1 384 ? 103.714 112.102 88.805  1.00 30.00 ? 373  GLU A CG  1 
ATOM   2822 C  CD  . GLU A 1 384 ? 102.529 112.127 87.892  1.00 30.00 ? 373  GLU A CD  1 
ATOM   2823 O  OE1 . GLU A 1 384 ? 102.742 112.082 86.718  1.00 30.00 ? 373  GLU A OE1 1 
ATOM   2824 O  OE2 . GLU A 1 384 ? 101.421 112.171 88.367  1.00 30.00 ? 373  GLU A OE2 1 
ATOM   2825 N  N   . THR A 1 385 ? 105.532 108.323 86.584  1.00 33.05 ? 374  THR A N   1 
ATOM   2826 C  CA  . THR A 1 385 ? 106.633 107.499 86.112  1.00 33.05 ? 374  THR A CA  1 
ATOM   2827 C  C   . THR A 1 385 ? 107.515 108.266 85.136  1.00 33.05 ? 374  THR A C   1 
ATOM   2828 O  O   . THR A 1 385 ? 107.052 109.154 84.417  1.00 33.05 ? 374  THR A O   1 
ATOM   2829 C  CB  . THR A 1 385 ? 106.098 106.236 85.438  1.00 33.05 ? 374  THR A CB  1 
ATOM   2830 O  OG1 . THR A 1 385 ? 105.080 105.650 86.256  1.00 33.05 ? 374  THR A OG1 1 
ATOM   2831 C  CG2 . THR A 1 385 ? 107.206 105.228 85.229  1.00 33.05 ? 374  THR A CG2 1 
ATOM   2832 N  N   . ASP A 1 386 ? 108.796 107.909 85.119  1.00 35.24 ? 375  ASP A N   1 
ATOM   2833 C  CA  . ASP A 1 386 ? 109.779 108.479 84.212  1.00 35.24 ? 375  ASP A CA  1 
ATOM   2834 C  C   . ASP A 1 386 ? 110.167 107.442 83.168  1.00 35.24 ? 375  ASP A C   1 
ATOM   2835 O  O   . ASP A 1 386 ? 110.155 106.240 83.438  1.00 35.24 ? 375  ASP A O   1 
ATOM   2836 C  CB  . ASP A 1 386 ? 111.027 108.938 84.967  1.00 35.24 ? 375  ASP A CB  1 
ATOM   2837 C  CG  . ASP A 1 386 ? 110.750 110.091 85.903  1.00 35.24 ? 375  ASP A CG  1 
ATOM   2838 O  OD1 . ASP A 1 386 ? 111.644 110.442 86.698  1.00 35.24 ? 375  ASP A OD1 1 
ATOM   2839 O  OD2 . ASP A 1 386 ? 109.635 110.645 85.849  1.00 35.24 ? 375  ASP A OD2 1 
ATOM   2840 N  N   . PHE A 1 387 ? 110.515 107.907 81.970  1.00 34.41 ? 376  PHE A N   1 
ATOM   2841 C  CA  . PHE A 1 387 ? 110.796 106.999 80.864  1.00 34.41 ? 376  PHE A CA  1 
ATOM   2842 C  C   . PHE A 1 387 ? 112.077 107.401 80.147  1.00 34.41 ? 376  PHE A C   1 
ATOM   2843 O  O   . PHE A 1 387 ? 112.582 108.511 80.310  1.00 34.41 ? 376  PHE A O   1 
ATOM   2844 C  CB  . PHE A 1 387 ? 109.639 106.959 79.860  1.00 34.41 ? 376  PHE A CB  1 
ATOM   2845 C  CG  . PHE A 1 387 ? 108.454 106.170 80.330  1.00 34.41 ? 376  PHE A CG  1 
ATOM   2846 C  CD1 . PHE A 1 387 ? 107.419 106.785 81.003  1.00 34.41 ? 376  PHE A CD1 1 
ATOM   2847 C  CD2 . PHE A 1 387 ? 108.374 104.814 80.096  1.00 34.41 ? 376  PHE A CD2 1 
ATOM   2848 C  CE1 . PHE A 1 387 ? 106.334 106.063 81.432  1.00 34.41 ? 376  PHE A CE1 1 
ATOM   2849 C  CE2 . PHE A 1 387 ? 107.289 104.090 80.525  1.00 34.41 ? 376  PHE A CE2 1 
ATOM   2850 C  CZ  . PHE A 1 387 ? 106.270 104.715 81.195  1.00 34.41 ? 376  PHE A CZ  1 
ATOM   2851 N  N   . SER A 1 388 ? 112.603 106.475 79.344  1.00 37.44 ? 377  SER A N   1 
ATOM   2852 C  CA  . SER A 1 388 ? 113.807 106.709 78.560  1.00 37.44 ? 377  SER A CA  1 
ATOM   2853 C  C   . SER A 1 388 ? 113.602 106.236 77.131  1.00 37.44 ? 377  SER A C   1 
ATOM   2854 O  O   . SER A 1 388 ? 112.956 105.209 76.888  1.00 37.44 ? 377  SER A O   1 
ATOM   2855 C  CB  . SER A 1 388 ? 115.017 105.994 79.154  1.00 37.44 ? 377  SER A CB  1 
ATOM   2856 O  OG  . SER A 1 388 ? 115.519 106.684 80.279  1.00 37.44 ? 377  SER A OG  1 
ATOM   2857 N  N   . LEU A 1 389 ? 114.168 106.994 76.193  1.00 42.51 ? 378  LEU A N   1 
ATOM   2858 C  CA  . LEU A 1 389 ? 114.145 106.673 74.772  1.00 42.51 ? 378  LEU A CA  1 
ATOM   2859 C  C   . LEU A 1 389 ? 115.572 106.441 74.297  1.00 42.51 ? 378  LEU A C   1 
ATOM   2860 O  O   . LEU A 1 389 ? 116.427 107.331 74.434  1.00 42.51 ? 378  LEU A O   1 
ATOM   2861 C  CB  . LEU A 1 389 ? 113.486 107.790 73.961  1.00 42.51 ? 378  LEU A CB  1 
ATOM   2862 C  CG  . LEU A 1 389 ? 113.080 107.399 72.538  1.00 42.51 ? 378  LEU A CG  1 
ATOM   2863 C  CD1 . LEU A 1 389 ? 111.769 106.645 72.546  1.00 42.51 ? 378  LEU A CD1 1 
ATOM   2864 C  CD2 . LEU A 1 389 ? 112.983 108.622 71.650  1.00 42.51 ? 378  LEU A CD2 1 
ATOM   2865 N  N   . TRP A 1 390 ? 115.800 105.254 73.726  1.00 43.29 ? 379  TRP A N   1 
ATOM   2866 C  CA  . TRP A 1 390 ? 117.080 104.784 73.218  1.00 43.29 ? 379  TRP A CA  1 
ATOM   2867 C  C   . TRP A 1 390 ? 117.066 104.797 71.697  1.00 43.29 ? 379  TRP A C   1 
ATOM   2868 O  O   . TRP A 1 390 ? 116.099 104.336 71.075  1.00 43.29 ? 379  TRP A O   1 
ATOM   2869 C  CB  . TRP A 1 390 ? 117.367 103.347 73.663  1.00 43.29 ? 379  TRP A CB  1 
ATOM   2870 C  CG  . TRP A 1 390 ? 117.328 103.077 75.127  1.00 43.29 ? 379  TRP A CG  1 
ATOM   2871 C  CD1 . TRP A 1 390 ? 116.261 103.210 75.958  1.00 43.29 ? 379  TRP A CD1 1 
ATOM   2872 C  CD2 . TRP A 1 390 ? 118.402 102.577 75.929  1.00 43.29 ? 379  TRP A CD2 1 
ATOM   2873 N  NE1 . TRP A 1 390 ? 116.608 102.847 77.234  1.00 43.29 ? 379  TRP A NE1 1 
ATOM   2874 C  CE2 . TRP A 1 390 ? 117.917 102.448 77.241  1.00 43.29 ? 379  TRP A CE2 1 
ATOM   2875 C  CE3 . TRP A 1 390 ? 119.729 102.231 75.664  1.00 43.29 ? 379  TRP A CE3 1 
ATOM   2876 C  CZ2 . TRP A 1 390 ? 118.711 101.994 78.286  1.00 43.29 ? 379  TRP A CZ2 1 
ATOM   2877 C  CZ3 . TRP A 1 390 ? 120.514 101.780 76.703  1.00 43.29 ? 379  TRP A CZ3 1 
ATOM   2878 C  CH2 . TRP A 1 390 ? 120.004 101.667 77.997  1.00 43.29 ? 379  TRP A CH2 1 
ATOM   2879 N  N   . ASP A 1 391 ? 118.168 105.267 71.110  1.00 49.05 ? 380  ASP A N   1 
ATOM   2880 C  CA  . ASP A 1 391 ? 118.320 105.375 69.666  1.00 49.05 ? 380  ASP A CA  1 
ATOM   2881 C  C   . ASP A 1 391 ? 119.729 104.944 69.275  1.00 49.05 ? 380  ASP A C   1 
ATOM   2882 O  O   . ASP A 1 391 ? 120.664 105.012 70.075  1.00 49.05 ? 380  ASP A O   1 
ATOM   2883 C  CB  . ASP A 1 391 ? 118.039 106.809 69.192  1.00 49.05 ? 380  ASP A CB  1 
ATOM   2884 C  CG  . ASP A 1 391 ? 117.989 106.930 67.682  1.00 49.05 ? 380  ASP A CG  1 
ATOM   2885 O  OD1 . ASP A 1 391 ? 117.703 105.920 67.007  1.00 49.05 ? 380  ASP A OD1 1 
ATOM   2886 O  OD2 . ASP A 1 391 ? 118.224 108.045 67.169  1.00 49.05 ? 380  ASP A OD2 1 
ATOM   2887 N  N   . MET A 1 392 ? 119.869 104.503 68.026  1.00 53.82 ? 381  MET A N   1 
ATOM   2888 C  CA  . MET A 1 392 ? 121.110 103.931 67.520  1.00 53.82 ? 381  MET A CA  1 
ATOM   2889 C  C   . MET A 1 392 ? 122.152 105.013 67.243  1.00 53.82 ? 381  MET A C   1 
ATOM   2890 O  O   . MET A 1 392 ? 121.836 106.188 67.044  1.00 53.82 ? 381  MET A O   1 
ATOM   2891 C  CB  . MET A 1 392 ? 120.839 103.133 66.242  1.00 53.82 ? 381  MET A CB  1 
ATOM   2892 C  CG  . MET A 1 392 ? 122.078 102.633 65.510  1.00 53.82 ? 381  MET A CG  1 
ATOM   2893 S  SD  . MET A 1 392 ? 121.684 101.759 63.987  1.00 53.82 ? 381  MET A SD  1 
ATOM   2894 C  CE  . MET A 1 392 ? 121.245 100.151 64.630  1.00 53.82 ? 381  MET A CE  1 
ATOM   2895 N  N   . ASP A 1 393 ? 123.419 104.590 67.229  1.00 57.63 ? 382  ASP A N   1 
ATOM   2896 C  CA  . ASP A 1 393 ? 124.538 105.469 66.921  1.00 57.63 ? 382  ASP A CA  1 
ATOM   2897 C  C   . ASP A 1 393 ? 124.976 105.248 65.484  1.00 57.63 ? 382  ASP A C   1 
ATOM   2898 O  O   . ASP A 1 393 ? 125.345 104.117 65.132  1.00 57.63 ? 382  ASP A O   1 
ATOM   2899 C  CB  . ASP A 1 393 ? 125.699 105.201 67.870  1.00 57.63 ? 382  ASP A CB  1 
ATOM   2900 C  CG  . ASP A 1 393 ? 126.820 106.205 67.718  1.00 57.63 ? 382  ASP A CG  1 
ATOM   2901 O  OD1 . ASP A 1 393 ? 126.711 107.093 66.848  1.00 57.63 ? 382  ASP A OD1 1 
ATOM   2902 O  OD2 . ASP A 1 393 ? 127.810 106.108 68.471  1.00 57.63 ? 382  ASP A OD2 1 
ATOM   2903 N  N   . PRO A 1 394 ? 124.954 106.266 64.618  1.00 60.24 ? 383  PRO A N   1 
ATOM   2904 C  CA  . PRO A 1 394 ? 125.402 106.034 63.234  1.00 60.24 ? 383  PRO A CA  1 
ATOM   2905 C  C   . PRO A 1 394 ? 126.835 105.542 63.140  1.00 60.24 ? 383  PRO A C   1 
ATOM   2906 O  O   . PRO A 1 394 ? 127.145 104.713 62.275  1.00 60.24 ? 383  PRO A O   1 
ATOM   2907 C  CB  . PRO A 1 394 ? 125.228 107.410 62.574  1.00 60.24 ? 383  PRO A CB  1 
ATOM   2908 C  CG  . PRO A 1 394 ? 125.169 108.383 63.703  1.00 60.24 ? 383  PRO A CG  1 
ATOM   2909 C  CD  . PRO A 1 394 ? 124.514 107.657 64.824  1.00 60.24 ? 383  PRO A CD  1 
ATOM   2910 N  N   . GLU A 1 395 ? 127.722 106.029 64.008  1.00 60.74 ? 384  GLU A N   1 
ATOM   2911 C  CA  . GLU A 1 395 ? 129.134 105.679 63.900  1.00 60.74 ? 384  GLU A CA  1 
ATOM   2912 C  C   . GLU A 1 395 ? 129.386 104.236 64.324  1.00 60.74 ? 384  GLU A C   1 
ATOM   2913 O  O   . GLU A 1 395 ? 130.091 103.492 63.633  1.00 60.74 ? 384  GLU A O   1 
ATOM   2914 C  CB  . GLU A 1 395 ? 129.974 106.639 64.742  1.00 60.74 ? 384  GLU A CB  1 
ATOM   2915 N  N   . ASN A 1 396 ? 128.812 103.820 65.456  1.00 59.13 ? 385  ASN A N   1 
ATOM   2916 C  CA  . ASN A 1 396 ? 129.134 102.532 66.055  1.00 59.13 ? 385  ASN A CA  1 
ATOM   2917 C  C   . ASN A 1 396 ? 128.011 101.509 65.978  1.00 59.13 ? 385  ASN A C   1 
ATOM   2918 O  O   . ASN A 1 396 ? 128.292 100.309 66.040  1.00 59.13 ? 385  ASN A O   1 
ATOM   2919 C  CB  . ASN A 1 396 ? 129.521 102.717 67.529  1.00 59.13 ? 385  ASN A CB  1 
ATOM   2920 N  N   . GLY A 1 397 ? 126.761 101.941 65.846  1.00 56.75 ? 386  GLY A N   1 
ATOM   2921 C  CA  . GLY A 1 397 ? 125.646 101.021 65.814  1.00 56.75 ? 386  GLY A CA  1 
ATOM   2922 C  C   . GLY A 1 397 ? 125.172 100.545 67.168  1.00 56.75 ? 386  GLY A C   1 
ATOM   2923 O  O   . GLY A 1 397 ? 124.274 99.697  67.227  1.00 56.75 ? 386  GLY A O   1 
ATOM   2924 N  N   . ALA A 1 398 ? 125.750 101.047 68.254  1.00 54.12 ? 387  ALA A N   1 
ATOM   2925 C  CA  . ALA A 1 398 ? 125.296 100.699 69.587  1.00 54.12 ? 387  ALA A CA  1 
ATOM   2926 C  C   . ALA A 1 398 ? 124.110 101.569 69.987  1.00 54.12 ? 387  ALA A C   1 
ATOM   2927 O  O   . ALA A 1 398 ? 123.903 102.664 69.459  1.00 54.12 ? 387  ALA A O   1 
ATOM   2928 C  CB  . ALA A 1 398 ? 126.426 100.862 70.600  1.00 54.12 ? 387  ALA A CB  1 
ATOM   2929 N  N   . PHE A 1 399 ? 123.331 101.068 70.938  1.00 49.24 ? 388  PHE A N   1 
ATOM   2930 C  CA  . PHE A 1 399 ? 122.165 101.768 71.455  1.00 49.24 ? 388  PHE A CA  1 
ATOM   2931 C  C   . PHE A 1 399 ? 122.509 102.427 72.783  1.00 49.24 ? 388  PHE A C   1 
ATOM   2932 O  O   . PHE A 1 399 ? 123.265 101.870 73.583  1.00 49.24 ? 388  PHE A O   1 
ATOM   2933 C  CB  . PHE A 1 399 ? 120.995 100.804 71.650  1.00 49.24 ? 388  PHE A CB  1 
ATOM   2934 C  CG  . PHE A 1 399 ? 120.080 100.717 70.470  1.00 49.24 ? 388  PHE A CG  1 
ATOM   2935 C  CD1 . PHE A 1 399 ? 118.718 100.873 70.625  1.00 49.24 ? 388  PHE A CD1 1 
ATOM   2936 C  CD2 . PHE A 1 399 ? 120.579 100.470 69.209  1.00 49.24 ? 388  PHE A CD2 1 
ATOM   2937 C  CE1 . PHE A 1 399 ? 117.874 100.792 69.543  1.00 49.24 ? 388  PHE A CE1 1 
ATOM   2938 C  CE2 . PHE A 1 399 ? 119.737 100.384 68.126  1.00 49.24 ? 388  PHE A CE2 1 
ATOM   2939 C  CZ  . PHE A 1 399 ? 118.383 100.548 68.292  1.00 49.24 ? 388  PHE A CZ  1 
ATOM   2940 N  N   . ARG A 1 400 ? 122.018 103.644 73.020  1.00 51.20 ? 389  ARG A N   1 
ATOM   2941 C  CA  . ARG A 1 400 ? 122.256 104.388 74.270  1.00 51.20 ? 389  ARG A CA  1 
ATOM   2942 C  C   . ARG A 1 400 ? 121.077 105.314 74.512  1.00 51.20 ? 389  ARG A C   1 
ATOM   2943 O  O   . ARG A 1 400 ? 120.492 105.719 73.547  1.00 51.20 ? 389  ARG A O   1 
ATOM   2944 C  CB  . ARG A 1 400 ? 123.538 105.206 74.163  1.00 51.20 ? 389  ARG A CB  1 
ATOM   2945 C  CG  . ARG A 1 400 ? 123.454 106.414 73.244  1.00 51.20 ? 389  ARG A CG  1 
ATOM   2946 C  CD  . ARG A 1 400 ? 123.705 106.089 71.803  1.00 51.20 ? 389  ARG A CD  1 
ATOM   2947 N  NE  . ARG A 1 400 ? 124.362 107.207 71.176  1.00 51.20 ? 389  ARG A NE  1 
ATOM   2948 C  CZ  . ARG A 1 400 ? 123.804 108.018 70.289  1.00 51.20 ? 389  ARG A CZ  1 
ATOM   2949 N  NH1 . ARG A 1 400 ? 122.553 107.840 69.911  1.00 51.20 ? 389  ARG A NH1 1 
ATOM   2950 N  NH2 . ARG A 1 400 ? 124.503 109.010 69.773  1.00 51.20 ? 389  ARG A NH2 1 
ATOM   2951 N  N   . VAL A 1 401 ? 120.745 105.627 75.755  1.00 46.09 ? 390  VAL A N   1 
ATOM   2952 C  CA  . VAL A 1 401 ? 119.657 106.548 76.055  1.00 46.09 ? 390  VAL A CA  1 
ATOM   2953 C  C   . VAL A 1 401 ? 119.959 107.905 75.438  1.00 46.09 ? 390  VAL A C   1 
ATOM   2954 O  O   . VAL A 1 401 ? 121.036 108.477 75.651  1.00 46.09 ? 390  VAL A O   1 
ATOM   2955 C  CB  . VAL A 1 401 ? 119.450 106.669 77.571  1.00 46.09 ? 390  VAL A CB  1 
ATOM   2956 C  CG1 . VAL A 1 401 ? 118.350 107.656 77.867  1.00 46.09 ? 390  VAL A CG1 1 
ATOM   2957 C  CG2 . VAL A 1 401 ? 119.111 105.329 78.162  1.00 46.09 ? 390  VAL A CG2 1 
ATOM   2958 N  N   . VAL A 1 402 ? 119.004 108.433 74.675  1.00 48.41 ? 391  VAL A N   1 
ATOM   2959 C  CA  . VAL A 1 402 ? 119.104 109.767 74.110  1.00 48.41 ? 391  VAL A CA  1 
ATOM   2960 C  C   . VAL A 1 402 ? 118.131 110.731 74.773  1.00 48.41 ? 391  VAL A C   1 
ATOM   2961 O  O   . VAL A 1 402 ? 118.462 111.902 74.967  1.00 48.41 ? 391  VAL A O   1 
ATOM   2962 C  CB  . VAL A 1 402 ? 118.899 109.753 72.580  1.00 48.41 ? 391  VAL A CB  1 
ATOM   2963 C  CG1 . VAL A 1 402 ? 120.030 109.007 71.899  1.00 48.41 ? 391  VAL A CG1 1 
ATOM   2964 C  CG2 . VAL A 1 402 ? 117.558 109.151 72.217  1.00 48.41 ? 391  VAL A CG2 1 
ATOM   2965 N  N   . LEU A 1 403 ? 116.931 110.272 75.133  1.00 46.16 ? 392  LEU A N   1 
ATOM   2966 C  CA  . LEU A 1 403 ? 115.941 111.160 75.737  1.00 46.16 ? 392  LEU A CA  1 
ATOM   2967 C  C   . LEU A 1 403 ? 115.457 110.617 77.074  1.00 46.16 ? 392  LEU A C   1 
ATOM   2968 O  O   . LEU A 1 403 ? 115.334 109.406 77.261  1.00 46.16 ? 392  LEU A O   1 
ATOM   2969 C  CB  . LEU A 1 403 ? 114.736 111.373 74.811  1.00 46.16 ? 392  LEU A CB  1 
ATOM   2970 C  CG  . LEU A 1 403 ? 114.778 112.558 73.845  1.00 46.16 ? 392  LEU A CG  1 
ATOM   2971 C  CD1 . LEU A 1 403 ? 113.518 112.591 73.008  1.00 46.16 ? 392  LEU A CD1 1 
ATOM   2972 C  CD2 . LEU A 1 403 ? 114.941 113.864 74.590  1.00 46.16 ? 392  LEU A CD2 1 
ATOM   2973 N  N   . ASN A 1 404 ? 115.168 111.534 77.999  1.00 43.48 ? 393  ASN A N   1 
ATOM   2974 C  CA  . ASN A 1 404 ? 114.618 111.194 79.305  1.00 43.48 ? 393  ASN A CA  1 
ATOM   2975 C  C   . ASN A 1 404 ? 113.335 111.981 79.532  1.00 43.48 ? 393  ASN A C   1 
ATOM   2976 O  O   . ASN A 1 404 ? 113.190 113.106 79.050  1.00 43.48 ? 393  ASN A O   1 
ATOM   2977 C  CB  . ASN A 1 404 ? 115.613 111.495 80.428  1.00 43.48 ? 393  ASN A CB  1 
ATOM   2978 C  CG  . ASN A 1 404 ? 116.668 110.425 80.573  1.00 43.48 ? 393  ASN A CG  1 
ATOM   2979 O  OD1 . ASN A 1 404 ? 116.483 109.293 80.139  1.00 43.48 ? 393  ASN A OD1 1 
ATOM   2980 N  ND2 . ASN A 1 404 ? 117.786 110.780 81.190  1.00 43.48 ? 393  ASN A ND2 1 
ATOM   2981 N  N   . TYR A 1 405 ? 112.404 111.384 80.275  1.00 39.31 ? 394  TYR A N   1 
ATOM   2982 C  CA  . TYR A 1 405 ? 111.086 111.965 80.500  1.00 39.31 ? 394  TYR A CA  1 
ATOM   2983 C  C   . TYR A 1 405 ? 110.770 111.940 81.988  1.00 39.31 ? 394  TYR A C   1 
ATOM   2984 O  O   . TYR A 1 405 ? 110.689 110.859 82.587  1.00 39.31 ? 394  TYR A O   1 
ATOM   2985 C  CB  . TYR A 1 405 ? 110.017 111.203 79.716  1.00 39.31 ? 394  TYR A CB  1 
ATOM   2986 C  CG  . TYR A 1 405 ? 108.610 111.689 79.957  1.00 39.31 ? 394  TYR A CG  1 
ATOM   2987 C  CD1 . TYR A 1 405 ? 108.123 112.807 79.297  1.00 39.31 ? 394  TYR A CD1 1 
ATOM   2988 C  CD2 . TYR A 1 405 ? 107.771 111.035 80.842  1.00 39.31 ? 394  TYR A CD2 1 
ATOM   2989 C  CE1 . TYR A 1 405 ? 106.840 113.257 79.511  1.00 39.31 ? 394  TYR A CE1 1 
ATOM   2990 C  CE2 . TYR A 1 405 ? 106.488 111.478 81.063  1.00 39.31 ? 394  TYR A CE2 1 
ATOM   2991 C  CZ  . TYR A 1 405 ? 106.027 112.590 80.394  1.00 39.31 ? 394  TYR A CZ  1 
ATOM   2992 O  OH  . TYR A 1 405 ? 104.746 113.035 80.613  1.00 39.31 ? 394  TYR A OH  1 
ATOM   2993 N  N   . ASN A 1 406 ? 110.584 113.132 82.569  1.00 38.99 ? 395  ASN A N   1 
ATOM   2994 C  CA  . ASN A 1 406 ? 110.212 113.314 83.973  1.00 38.99 ? 395  ASN A CA  1 
ATOM   2995 C  C   . ASN A 1 406 ? 108.692 113.358 84.066  1.00 38.99 ? 395  ASN A C   1 
ATOM   2996 O  O   . ASN A 1 406 ? 108.060 114.289 83.560  1.00 38.99 ? 395  ASN A O   1 
ATOM   2997 C  CB  . ASN A 1 406 ? 110.823 114.600 84.532  1.00 38.99 ? 395  ASN A CB  1 
ATOM   2998 C  CG  . ASN A 1 406 ? 110.540 114.806 86.026  1.00 38.99 ? 395  ASN A CG  1 
ATOM   2999 O  OD1 . ASN A 1 406 ? 109.433 114.569 86.497  1.00 38.99 ? 395  ASN A OD1 1 
ATOM   3000 N  ND2 . ASN A 1 406 ? 111.544 115.287 86.759  1.00 38.99 ? 395  ASN A ND2 1 
ATOM   3001 N  N   . GLY A 1 407 ? 108.102 112.353 84.710  1.00 36.27 ? 396  GLY A N   1 
ATOM   3002 C  CA  . GLY A 1 407 ? 106.654 112.309 84.813  1.00 36.27 ? 396  GLY A CA  1 
ATOM   3003 C  C   . GLY A 1 407 ? 106.082 113.464 85.610  1.00 36.27 ? 396  GLY A C   1 
ATOM   3004 O  O   . GLY A 1 407 ? 104.990 113.953 85.314  1.00 36.27 ? 396  GLY A O   1 
ATOM   3005 N  N   . THR A 1 408 ? 106.800 113.906 86.644  1.00 37.97 ? 397  THR A N   1 
ATOM   3006 C  CA  . THR A 1 408 ? 106.284 114.966 87.506  1.00 37.97 ? 397  THR A CA  1 
ATOM   3007 C  C   . THR A 1 408 ? 106.105 116.265 86.734  1.00 37.97 ? 397  THR A C   1 
ATOM   3008 O  O   . THR A 1 408 ? 105.030 116.872 86.756  1.00 37.97 ? 397  THR A O   1 
ATOM   3009 C  CB  . THR A 1 408 ? 107.222 115.179 88.692  1.00 37.97 ? 397  THR A CB  1 
ATOM   3010 O  OG1 . THR A 1 408 ? 107.126 114.069 89.589  1.00 37.97 ? 397  THR A OG1 1 
ATOM   3011 C  CG2 . THR A 1 408 ? 106.867 116.454 89.435  1.00 37.97 ? 397  THR A CG2 1 
ATOM   3012 N  N   . SER A 1 409 ? 107.155 116.709 86.043  1.00 40.93 ? 398  SER A N   1 
ATOM   3013 C  CA  . SER A 1 409 ? 107.113 117.964 85.307  1.00 40.93 ? 398  SER A CA  1 
ATOM   3014 C  C   . SER A 1 409 ? 106.654 117.794 83.867  1.00 40.93 ? 398  SER A C   1 
ATOM   3015 O  O   . SER A 1 409 ? 106.286 118.786 83.230  1.00 40.93 ? 398  SER A O   1 
ATOM   3016 C  CB  . SER A 1 409 ? 108.494 118.622 85.317  1.00 40.93 ? 398  SER A CB  1 
ATOM   3017 O  OG  . SER A 1 409 ? 109.310 118.095 84.288  1.00 40.93 ? 398  SER A OG  1 
ATOM   3018 N  N   . GLN A 1 410 ? 106.664 116.569 83.343  1.00 42.49 ? 399  GLN A N   1 
ATOM   3019 C  CA  . GLN A 1 410 ? 106.199 116.282 81.988  1.00 42.49 ? 399  GLN A CA  1 
ATOM   3020 C  C   . GLN A 1 410 ? 107.068 116.992 80.949  1.00 42.49 ? 399  GLN A C   1 
ATOM   3021 O  O   . GLN A 1 410 ? 106.589 117.770 80.123  1.00 42.49 ? 399  GLN A O   1 
ATOM   3022 C  CB  . GLN A 1 410 ? 104.727 116.670 81.830  1.00 42.49 ? 399  GLN A CB  1 
ATOM   3023 C  CG  . GLN A 1 410 ? 103.802 115.968 82.799  1.00 42.49 ? 399  GLN A CG  1 
ATOM   3024 C  CD  . GLN A 1 410 ? 102.383 115.891 82.290  1.00 42.49 ? 399  GLN A CD  1 
ATOM   3025 O  OE1 . GLN A 1 410 ? 101.784 114.818 82.244  1.00 42.49 ? 399  GLN A OE1 1 
ATOM   3026 N  NE2 . GLN A 1 410 ? 101.835 117.034 81.901  1.00 42.49 ? 399  GLN A NE2 1 
ATOM   3027 N  N   . GLU A 1 411 ? 108.365 116.703 81.002  1.00 45.28 ? 400  GLU A N   1 
ATOM   3028 C  CA  . GLU A 1 411 ? 109.337 117.319 80.112  1.00 45.28 ? 400  GLU A CA  1 
ATOM   3029 C  C   . GLU A 1 411 ? 110.237 116.258 79.500  1.00 45.28 ? 400  GLU A C   1 
ATOM   3030 O  O   . GLU A 1 411 ? 110.511 115.225 80.112  1.00 45.28 ? 400  GLU A O   1 
ATOM   3031 C  CB  . GLU A 1 411 ? 110.194 118.344 80.852  1.00 45.28 ? 400  GLU A CB  1 
ATOM   3032 C  CG  . GLU A 1 411 ? 109.459 119.623 81.195  1.00 45.28 ? 400  GLU A CG  1 
ATOM   3033 C  CD  . GLU A 1 411 ? 110.374 120.826 81.224  1.00 45.28 ? 400  GLU A CD  1 
ATOM   3034 O  OE1 . GLU A 1 411 ? 109.860 121.962 81.261  1.00 45.28 ? 400  GLU A OE1 1 
ATOM   3035 O  OE2 . GLU A 1 411 ? 111.609 120.636 81.216  1.00 45.28 ? 400  GLU A OE2 1 
ATOM   3036 N  N   . LEU A 1 412 ? 110.694 116.528 78.281  1.00 45.01 ? 401  LEU A N   1 
ATOM   3037 C  CA  . LEU A 1 412 ? 111.668 115.695 77.590  1.00 45.01 ? 401  LEU A CA  1 
ATOM   3038 C  C   . LEU A 1 412 ? 113.017 116.396 77.611  1.00 45.01 ? 401  LEU A C   1 
ATOM   3039 O  O   . LEU A 1 412 ? 113.118 117.567 77.232  1.00 45.01 ? 401  LEU A O   1 
ATOM   3040 C  CB  . LEU A 1 412 ? 111.238 115.423 76.148  1.00 45.01 ? 401  LEU A CB  1 
ATOM   3041 C  CG  . LEU A 1 412 ? 110.065 114.464 75.964  1.00 45.01 ? 401  LEU A CG  1 
ATOM   3042 C  CD1 . LEU A 1 412 ? 109.341 114.755 74.671  1.00 45.01 ? 401  LEU A CD1 1 
ATOM   3043 C  CD2 . LEU A 1 412 ? 110.539 113.031 75.984  1.00 45.01 ? 401  LEU A CD2 1 
ATOM   3044 N  N   . VAL A 1 413 ? 114.048 115.680 78.046  1.00 46.19 ? 402  VAL A N   1 
ATOM   3045 C  CA  . VAL A 1 413 ? 115.382 116.237 78.234  1.00 46.19 ? 402  VAL A CA  1 
ATOM   3046 C  C   . VAL A 1 413 ? 116.376 115.404 77.440  1.00 46.19 ? 402  VAL A C   1 
ATOM   3047 O  O   . VAL A 1 413 ? 116.364 114.169 77.520  1.00 46.19 ? 402  VAL A O   1 
ATOM   3048 C  CB  . VAL A 1 413 ? 115.772 116.275 79.721  1.00 46.19 ? 402  VAL A CB  1 
ATOM   3049 C  CG1 . VAL A 1 413 ? 117.081 117.014 79.905  1.00 46.19 ? 402  VAL A CG1 1 
ATOM   3050 C  CG2 . VAL A 1 413 ? 114.671 116.921 80.539  1.00 46.19 ? 402  VAL A CG2 1 
ATOM   3051 N  N   . ALA A 1 414 ? 117.226 116.080 76.672  1.00 49.75 ? 403  ALA A N   1 
ATOM   3052 C  CA  . ALA A 1 414 ? 118.308 115.422 75.961  1.00 49.75 ? 403  ALA A CA  1 
ATOM   3053 C  C   . ALA A 1 414 ? 119.439 115.087 76.923  1.00 49.75 ? 403  ALA A C   1 
ATOM   3054 O  O   . ALA A 1 414 ? 119.674 115.793 77.908  1.00 49.75 ? 403  ALA A O   1 
ATOM   3055 C  CB  . ALA A 1 414 ? 118.828 116.309 74.832  1.00 49.75 ? 403  ALA A CB  1 
ATOM   3056 N  N   . VAL A 1 415 ? 120.150 114.004 76.624  1.00 51.37 ? 404  VAL A N   1 
ATOM   3057 C  CA  . VAL A 1 415 ? 121.144 113.435 77.526  1.00 51.37 ? 404  VAL A CA  1 
ATOM   3058 C  C   . VAL A 1 415 ? 122.523 113.614 76.911  1.00 51.37 ? 404  VAL A C   1 
ATOM   3059 O  O   . VAL A 1 415 ? 122.775 113.160 75.789  1.00 51.37 ? 404  VAL A O   1 
ATOM   3060 C  CB  . VAL A 1 415 ? 120.863 111.952 77.808  1.00 51.37 ? 404  VAL A CB  1 
ATOM   3061 C  CG1 . VAL A 1 415 ? 121.973 111.355 78.655  1.00 51.37 ? 404  VAL A CG1 1 
ATOM   3062 C  CG2 . VAL A 1 415 ? 119.517 111.789 78.493  1.00 51.37 ? 404  VAL A CG2 1 
ATOM   3063 N  N   . SER A 1 416 ? 123.413 114.278 77.650  1.00 54.02 ? 405  SER A N   1 
ATOM   3064 C  CA  . SER A 1 416 ? 124.836 114.347 77.311  1.00 54.02 ? 405  SER A CA  1 
ATOM   3065 C  C   . SER A 1 416 ? 125.052 114.797 75.869  1.00 54.02 ? 405  SER A C   1 
ATOM   3066 O  O   . SER A 1 416 ? 125.913 114.279 75.156  1.00 54.02 ? 405  SER A O   1 
ATOM   3067 C  CB  . SER A 1 416 ? 125.517 113.000 77.564  1.00 54.02 ? 405  SER A CB  1 
ATOM   3068 N  N   . GLY A 1 417 ? 124.264 115.775 75.435  1.00 56.40 ? 406  GLY A N   1 
ATOM   3069 C  CA  . GLY A 1 417 ? 124.417 116.317 74.100  1.00 56.40 ? 406  GLY A CA  1 
ATOM   3070 C  C   . GLY A 1 417 ? 124.262 115.280 73.007  1.00 56.40 ? 406  GLY A C   1 
ATOM   3071 O  O   . GLY A 1 417 ? 125.075 115.222 72.081  1.00 56.40 ? 406  GLY A O   1 
ATOM   3072 N  N   . ARG A 1 418 ? 123.227 114.450 73.109  1.00 52.85 ? 407  ARG A N   1 
ATOM   3073 C  CA  . ARG A 1 418 ? 122.887 113.475 72.083  1.00 52.85 ? 407  ARG A CA  1 
ATOM   3074 C  C   . ARG A 1 418 ? 121.567 113.864 71.438  1.00 52.85 ? 407  ARG A C   1 
ATOM   3075 O  O   . ARG A 1 418 ? 120.608 114.217 72.130  1.00 52.85 ? 407  ARG A O   1 
ATOM   3076 C  CB  . ARG A 1 418 ? 122.774 112.061 72.662  1.00 52.85 ? 407  ARG A CB  1 
ATOM   3077 C  CG  . ARG A 1 418 ? 123.941 111.621 73.522  1.00 52.85 ? 407  ARG A CG  1 
ATOM   3078 C  CD  . ARG A 1 418 ? 123.539 110.471 74.426  1.00 52.85 ? 407  ARG A CD  1 
ATOM   3079 N  NE  . ARG A 1 418 ? 124.681 109.650 74.811  1.00 52.85 ? 407  ARG A NE  1 
ATOM   3080 C  CZ  . ARG A 1 418 ? 124.694 108.824 75.853  1.00 52.85 ? 407  ARG A CZ  1 
ATOM   3081 N  NH1 . ARG A 1 418 ? 123.623 108.697 76.625  1.00 52.85 ? 407  ARG A NH1 1 
ATOM   3082 N  NH2 . ARG A 1 418 ? 125.783 108.119 76.123  1.00 52.85 ? 407  ARG A NH2 1 
ATOM   3083 N  N   . LYS A 1 419 ? 121.522 113.798 70.113  1.00 53.55 ? 408  LYS A N   1 
ATOM   3084 C  CA  . LYS A 1 419 ? 120.330 114.121 69.347  1.00 53.55 ? 408  LYS A CA  1 
ATOM   3085 C  C   . LYS A 1 419 ? 119.793 112.866 68.674  1.00 53.55 ? 408  LYS A C   1 
ATOM   3086 O  O   . LYS A 1 419 ? 120.555 111.988 68.260  1.00 53.55 ? 408  LYS A O   1 
ATOM   3087 C  CB  . LYS A 1 419 ? 120.626 115.190 68.290  1.00 53.55 ? 408  LYS A CB  1 
ATOM   3088 N  N   . LEU A 1 420 ? 118.470 112.788 68.573  1.00 51.69 ? 409  LEU A N   1 
ATOM   3089 C  CA  . LEU A 1 420 ? 117.842 111.649 67.923  1.00 51.69 ? 409  LEU A CA  1 
ATOM   3090 C  C   . LEU A 1 420 ? 118.387 111.494 66.510  1.00 51.69 ? 409  LEU A C   1 
ATOM   3091 O  O   . LEU A 1 420 ? 118.478 112.466 65.756  1.00 51.69 ? 409  LEU A O   1 
ATOM   3092 C  CB  . LEU A 1 420 ? 116.327 111.836 67.891  1.00 51.69 ? 409  LEU A CB  1 
ATOM   3093 C  CG  . LEU A 1 420 ? 115.565 111.493 69.169  1.00 51.69 ? 409  LEU A CG  1 
ATOM   3094 C  CD1 . LEU A 1 420 ? 114.139 111.993 69.076  1.00 51.69 ? 409  LEU A CD1 1 
ATOM   3095 C  CD2 . LEU A 1 420 ? 115.576 109.999 69.418  1.00 51.69 ? 409  LEU A CD2 1 
ATOM   3096 N  N   . ASN A 1 421 ? 118.753 110.266 66.152  1.00 55.42 ? 410  ASN A N   1 
ATOM   3097 C  CA  . ASN A 1 421 ? 119.370 109.982 64.858  1.00 55.42 ? 410  ASN A CA  1 
ATOM   3098 C  C   . ASN A 1 421 ? 118.277 109.629 63.858  1.00 55.42 ? 410  ASN A C   1 
ATOM   3099 O  O   . ASN A 1 421 ? 117.767 108.507 63.847  1.00 55.42 ? 410  ASN A O   1 
ATOM   3100 C  CB  . ASN A 1 421 ? 120.389 108.856 64.984  1.00 55.42 ? 410  ASN A CB  1 
ATOM   3101 N  N   . TRP A 1 422 ? 117.918 110.594 63.010  1.00 58.55 ? 411  TRP A N   1 
ATOM   3102 C  CA  . TRP A 1 422 ? 116.963 110.364 61.937  1.00 58.55 ? 411  TRP A CA  1 
ATOM   3103 C  C   . TRP A 1 422 ? 117.712 110.261 60.620  1.00 58.55 ? 411  TRP A C   1 
ATOM   3104 O  O   . TRP A 1 422 ? 118.463 111.189 60.282  1.00 58.55 ? 411  TRP A O   1 
ATOM   3105 C  CB  . TRP A 1 422 ? 115.943 111.493 61.873  1.00 58.55 ? 411  TRP A CB  1 
ATOM   3106 C  CG  . TRP A 1 422 ? 115.181 111.690 63.141  1.00 58.55 ? 411  TRP A CG  1 
ATOM   3107 C  CD1 . TRP A 1 422 ? 115.372 112.670 64.064  1.00 58.55 ? 411  TRP A CD1 1 
ATOM   3108 C  CD2 . TRP A 1 422 ? 114.100 110.888 63.624  1.00 58.55 ? 411  TRP A CD2 1 
ATOM   3109 N  NE1 . TRP A 1 422 ? 114.478 112.530 65.095  1.00 58.55 ? 411  TRP A NE1 1 
ATOM   3110 C  CE2 . TRP A 1 422 ? 113.685 111.441 64.848  1.00 58.55 ? 411  TRP A CE2 1 
ATOM   3111 C  CE3 . TRP A 1 422 ? 113.442 109.755 63.141  1.00 58.55 ? 411  TRP A CE3 1 
ATOM   3112 C  CZ2 . TRP A 1 422 ? 112.644 110.900 65.595  1.00 58.55 ? 411  TRP A CZ2 1 
ATOM   3113 C  CZ3 . TRP A 1 422 ? 112.411 109.222 63.883  1.00 58.55 ? 411  TRP A CZ3 1 
ATOM   3114 C  CH2 . TRP A 1 422 ? 112.022 109.792 65.096  1.00 58.55 ? 411  TRP A CH2 1 
ATOM   3115 N  N   . PRO A 1 423 ? 117.561 109.179 59.849  1.00 63.40 ? 412  PRO A N   1 
ATOM   3116 C  CA  . PRO A 1 423 ? 118.314 109.091 58.586  1.00 63.40 ? 412  PRO A CA  1 
ATOM   3117 C  C   . PRO A 1 423 ? 118.043 110.253 57.647  1.00 63.40 ? 412  PRO A C   1 
ATOM   3118 O  O   . PRO A 1 423 ? 118.957 110.713 56.952  1.00 63.40 ? 412  PRO A O   1 
ATOM   3119 C  CB  . PRO A 1 423 ? 117.852 107.754 57.986  1.00 63.40 ? 412  PRO A CB  1 
ATOM   3120 C  CG  . PRO A 1 423 ? 116.633 107.364 58.732  1.00 63.40 ? 412  PRO A CG  1 
ATOM   3121 C  CD  . PRO A 1 423 ? 116.708 108.002 60.075  1.00 63.40 ? 412  PRO A CD  1 
ATOM   3122 N  N   . LEU A 1 424 ? 116.805 110.741 57.608  1.00 65.61 ? 413  LEU A N   1 
ATOM   3123 C  CA  . LEU A 1 424 ? 116.450 111.875 56.767  1.00 65.61 ? 413  LEU A CA  1 
ATOM   3124 C  C   . LEU A 1 424 ? 116.892 113.211 57.351  1.00 65.61 ? 413  LEU A C   1 
ATOM   3125 O  O   . LEU A 1 424 ? 116.807 114.228 56.657  1.00 65.61 ? 413  LEU A O   1 
ATOM   3126 C  CB  . LEU A 1 424 ? 114.937 111.892 56.544  1.00 65.61 ? 413  LEU A CB  1 
ATOM   3127 C  CG  . LEU A 1 424 ? 114.430 112.433 55.209  1.00 65.61 ? 413  LEU A CG  1 
ATOM   3128 C  CD1 . LEU A 1 424 ? 114.819 111.513 54.065  1.00 65.61 ? 413  LEU A CD1 1 
ATOM   3129 C  CD2 . LEU A 1 424 ? 112.924 112.608 55.265  1.00 65.61 ? 413  LEU A CD2 1 
ATOM   3130 N  N   . GLY A 1 425 ? 117.357 113.234 58.600  1.00 64.89 ? 414  GLY A N   1 
ATOM   3131 C  CA  . GLY A 1 425 ? 117.735 114.455 59.270  1.00 64.89 ? 414  GLY A CA  1 
ATOM   3132 C  C   . GLY A 1 425 ? 116.643 115.070 60.119  1.00 64.89 ? 414  GLY A C   1 
ATOM   3133 O  O   . GLY A 1 425 ? 116.947 115.861 61.019  1.00 64.89 ? 414  GLY A O   1 
ATOM   3134 N  N   . TYR A 1 426 ? 115.389 114.729 59.861  1.00 64.29 ? 415  TYR A N   1 
ATOM   3135 C  CA  . TYR A 1 426 ? 114.249 115.193 60.633  1.00 64.29 ? 415  TYR A CA  1 
ATOM   3136 C  C   . TYR A 1 426 ? 113.239 114.062 60.720  1.00 64.29 ? 415  TYR A C   1 
ATOM   3137 O  O   . TYR A 1 426 ? 113.263 113.137 59.901  1.00 64.29 ? 415  TYR A O   1 
ATOM   3138 C  CB  . TYR A 1 426 ? 113.607 116.436 60.004  1.00 64.29 ? 415  TYR A CB  1 
ATOM   3139 C  CG  . TYR A 1 426 ? 113.610 116.420 58.495  1.00 64.29 ? 415  TYR A CG  1 
ATOM   3140 C  CD1 . TYR A 1 426 ? 112.572 115.838 57.783  1.00 64.29 ? 415  TYR A CD1 1 
ATOM   3141 C  CD2 . TYR A 1 426 ? 114.658 116.984 57.781  1.00 64.29 ? 415  TYR A CD2 1 
ATOM   3142 C  CE1 . TYR A 1 426 ? 112.577 115.820 56.405  1.00 64.29 ? 415  TYR A CE1 1 
ATOM   3143 C  CE2 . TYR A 1 426 ? 114.671 116.970 56.404  1.00 64.29 ? 415  TYR A CE2 1 
ATOM   3144 C  CZ  . TYR A 1 426 ? 113.630 116.387 55.720  1.00 64.29 ? 415  TYR A CZ  1 
ATOM   3145 O  OH  . TYR A 1 426 ? 113.641 116.373 54.344  1.00 64.29 ? 415  TYR A OH  1 
ATOM   3146 N  N   . PRO A 1 427 ? 112.344 114.101 61.705  1.00 59.92 ? 416  PRO A N   1 
ATOM   3147 C  CA  . PRO A 1 427 ? 111.389 113.012 61.855  1.00 59.92 ? 416  PRO A CA  1 
ATOM   3148 C  C   . PRO A 1 427 ? 110.515 112.895 60.624  1.00 59.92 ? 416  PRO A C   1 
ATOM   3149 O  O   . PRO A 1 427 ? 110.195 113.905 59.970  1.00 59.92 ? 416  PRO A O   1 
ATOM   3150 C  CB  . PRO A 1 427 ? 110.574 113.422 63.089  1.00 59.92 ? 416  PRO A CB  1 
ATOM   3151 C  CG  . PRO A 1 427 ? 111.399 114.435 63.788  1.00 59.92 ? 416  PRO A CG  1 
ATOM   3152 C  CD  . PRO A 1 427 ? 112.153 115.144 62.724  1.00 59.92 ? 416  PRO A CD  1 
ATOM   3153 N  N   . PRO A 1 428 ? 110.103 111.682 60.266  1.00 61.70 ? 417  PRO A N   1 
ATOM   3154 C  CA  . PRO A 1 428 ? 109.188 111.518 59.139  1.00 61.70 ? 417  PRO A CA  1 
ATOM   3155 C  C   . PRO A 1 428 ? 107.807 112.038 59.490  1.00 61.70 ? 417  PRO A C   1 
ATOM   3156 O  O   . PRO A 1 428 ? 107.484 112.205 60.675  1.00 61.70 ? 417  PRO A O   1 
ATOM   3157 C  CB  . PRO A 1 428 ? 109.174 109.999 58.920  1.00 61.70 ? 417  PRO A CB  1 
ATOM   3158 C  CG  . PRO A 1 428 ? 109.459 109.443 60.258  1.00 61.70 ? 417  PRO A CG  1 
ATOM   3159 C  CD  . PRO A 1 428 ? 110.453 110.385 60.870  1.00 61.70 ? 417  PRO A CD  1 
ATOM   3160 N  N   . PRO A 1 429 ? 106.965 112.323 58.498  1.00 62.58 ? 418  PRO A N   1 
ATOM   3161 C  CA  . PRO A 1 429 ? 105.585 112.713 58.805  1.00 62.58 ? 418  PRO A CA  1 
ATOM   3162 C  C   . PRO A 1 429 ? 104.741 111.513 59.203  1.00 62.58 ? 418  PRO A C   1 
ATOM   3163 O  O   . PRO A 1 429 ? 104.878 110.418 58.651  1.00 62.58 ? 418  PRO A O   1 
ATOM   3164 C  CB  . PRO A 1 429 ? 105.085 113.331 57.491  1.00 62.58 ? 418  PRO A CB  1 
ATOM   3165 C  CG  . PRO A 1 429 ? 106.291 113.445 56.603  1.00 62.58 ? 418  PRO A CG  1 
ATOM   3166 C  CD  . PRO A 1 429 ? 107.234 112.391 57.054  1.00 62.58 ? 418  PRO A CD  1 
ATOM   3167 N  N   . ASP A 1 430 ? 103.855 111.730 60.175  1.00 61.79 ? 419  ASP A N   1 
ATOM   3168 C  CA  . ASP A 1 430 ? 102.913 110.693 60.576  1.00 61.79 ? 419  ASP A CA  1 
ATOM   3169 C  C   . ASP A 1 430 ? 101.862 110.416 59.513  1.00 61.79 ? 419  ASP A C   1 
ATOM   3170 O  O   . ASP A 1 430 ? 101.119 109.437 59.642  1.00 61.79 ? 419  ASP A O   1 
ATOM   3171 C  CB  . ASP A 1 430 ? 102.235 111.084 61.886  1.00 61.79 ? 419  ASP A CB  1 
ATOM   3172 C  CG  . ASP A 1 430 ? 101.414 112.347 61.762  1.00 61.79 ? 419  ASP A CG  1 
ATOM   3173 O  OD1 . ASP A 1 430 ? 101.404 112.946 60.668  1.00 61.79 ? 419  ASP A OD1 1 
ATOM   3174 O  OD2 . ASP A 1 430 ? 100.781 112.744 62.762  1.00 61.79 ? 419  ASP A OD2 1 
ATOM   3175 N  N   . ILE A 1 431 ? 101.772 111.255 58.486  1.00 66.29 ? 420  ILE A N   1 
ATOM   3176 C  CA  . ILE A 1 431 ? 100.888 111.021 57.349  1.00 66.29 ? 420  ILE A CA  1 
ATOM   3177 C  C   . ILE A 1 431 ? 101.632 111.468 56.096  1.00 66.29 ? 420  ILE A C   1 
ATOM   3178 O  O   . ILE A 1 431 ? 101.919 112.664 55.950  1.00 66.29 ? 420  ILE A O   1 
ATOM   3179 C  CB  . ILE A 1 431 ? 99.555  111.768 57.508  1.00 66.29 ? 420  ILE A CB  1 
ATOM   3180 N  N   . PRO A 1 432 ? 101.970 110.569 55.174  1.00 67.94 ? 421  PRO A N   1 
ATOM   3181 C  CA  . PRO A 1 432 ? 102.792 110.971 54.032  1.00 67.94 ? 421  PRO A CA  1 
ATOM   3182 C  C   . PRO A 1 432 ? 101.996 111.748 52.997  1.00 67.94 ? 421  PRO A C   1 
ATOM   3183 O  O   . PRO A 1 432 ? 100.791 111.555 52.823  1.00 67.94 ? 421  PRO A O   1 
ATOM   3184 C  CB  . PRO A 1 432 ? 103.283 109.635 53.461  1.00 67.94 ? 421  PRO A CB  1 
ATOM   3185 C  CG  . PRO A 1 432 ? 102.287 108.624 53.901  1.00 67.94 ? 421  PRO A CG  1 
ATOM   3186 C  CD  . PRO A 1 432 ? 101.476 109.189 55.037  1.00 67.94 ? 421  PRO A CD  1 
ATOM   3187 N  N   . LYS A 1 433 ? 102.700 112.639 52.301  1.00 76.13 ? 422  LYS A N   1 
ATOM   3188 C  CA  . LYS A 1 433 ? 102.076 113.406 51.233  1.00 76.13 ? 422  LYS A CA  1 
ATOM   3189 C  C   . LYS A 1 433 ? 101.560 112.464 50.154  1.00 76.13 ? 422  LYS A C   1 
ATOM   3190 O  O   . LYS A 1 433 ? 102.263 111.544 49.726  1.00 76.13 ? 422  LYS A O   1 
ATOM   3191 C  CB  . LYS A 1 433 ? 103.078 114.397 50.643  1.00 76.13 ? 422  LYS A CB  1 
ATOM   3192 N  N   . CYS A 1 434 ? 100.324 112.695 49.715  1.00 80.34 ? 423  CYS A N   1 
ATOM   3193 C  CA  . CYS A 1 434 ? 99.661  111.801 48.768  1.00 80.34 ? 423  CYS A CA  1 
ATOM   3194 C  C   . CYS A 1 434 ? 99.670  110.371 49.299  1.00 80.34 ? 423  CYS A C   1 
ATOM   3195 O  O   . CYS A 1 434 ? 99.885  109.406 48.562  1.00 80.34 ? 423  CYS A O   1 
ATOM   3196 C  CB  . CYS A 1 434 ? 100.319 111.883 47.389  1.00 80.34 ? 423  CYS A CB  1 
ATOM   3197 S  SG  . CYS A 1 434 ? 99.490  110.923 46.098  1.00 80.34 ? 423  CYS A SG  1 
ATOM   3198 N  N   . GLY A 1 435 ? 99.435  110.237 50.606  1.00 73.26 ? 424  GLY A N   1 
ATOM   3199 C  CA  . GLY A 1 435 ? 99.517  108.964 51.282  1.00 73.26 ? 424  GLY A CA  1 
ATOM   3200 C  C   . GLY A 1 435 ? 98.174  108.256 51.380  1.00 73.26 ? 424  GLY A C   1 
ATOM   3201 O  O   . GLY A 1 435 ? 97.151  108.705 50.872  1.00 73.26 ? 424  GLY A O   1 
ATOM   3202 N  N   . PHE A 1 436 ? 98.208  107.110 52.053  1.00 67.56 ? 425  PHE A N   1 
ATOM   3203 C  CA  . PHE A 1 436 ? 97.016  106.301 52.279  1.00 67.56 ? 425  PHE A CA  1 
ATOM   3204 C  C   . PHE A 1 436 ? 95.866  107.150 52.809  1.00 67.56 ? 425  PHE A C   1 
ATOM   3205 O  O   . PHE A 1 436 ? 96.055  107.990 53.690  1.00 67.56 ? 425  PHE A O   1 
ATOM   3206 C  CB  . PHE A 1 436 ? 97.324  105.171 53.262  1.00 67.56 ? 425  PHE A CB  1 
ATOM   3207 C  CG  . PHE A 1 436 ? 97.729  105.653 54.626  1.00 67.56 ? 425  PHE A CG  1 
ATOM   3208 C  CD1 . PHE A 1 436 ? 99.047  105.967 54.905  1.00 67.56 ? 425  PHE A CD1 1 
ATOM   3209 C  CD2 . PHE A 1 436 ? 96.790  105.788 55.631  1.00 67.56 ? 425  PHE A CD2 1 
ATOM   3210 C  CE1 . PHE A 1 436 ? 99.417  106.411 56.160  1.00 67.56 ? 425  PHE A CE1 1 
ATOM   3211 C  CE2 . PHE A 1 436 ? 97.155  106.230 56.882  1.00 67.56 ? 425  PHE A CE2 1 
ATOM   3212 C  CZ  . PHE A 1 436 ? 98.470  106.542 57.148  1.00 67.56 ? 425  PHE A CZ  1 
ATOM   3213 N  N   . GLY B 1 12  ? 71.022  72.810  120.172 1.00 43.68 ? 1    GLY B N   1 
ATOM   3214 C  CA  . GLY B 1 12  ? 71.816  73.986  119.718 1.00 43.68 ? 1    GLY B CA  1 
ATOM   3215 C  C   . GLY B 1 12  ? 71.083  74.821  118.690 1.00 43.68 ? 1    GLY B C   1 
ATOM   3216 O  O   . GLY B 1 12  ? 69.877  74.683  118.513 1.00 43.68 ? 1    GLY B O   1 
ATOM   3217 N  N   . ASN B 1 13  ? 71.818  75.696  118.011 1.00 41.26 ? 2    ASN B N   1 
ATOM   3218 C  CA  . ASN B 1 13  ? 71.270  76.559  116.975 1.00 41.26 ? 2    ASN B CA  1 
ATOM   3219 C  C   . ASN B 1 13  ? 72.015  76.303  115.676 1.00 41.26 ? 2    ASN B C   1 
ATOM   3220 O  O   . ASN B 1 13  ? 73.248  76.346  115.647 1.00 41.26 ? 2    ASN B O   1 
ATOM   3221 C  CB  . ASN B 1 13  ? 71.386  78.034  117.368 1.00 41.26 ? 2    ASN B CB  1 
ATOM   3222 C  CG  . ASN B 1 13  ? 70.801  78.319  118.737 1.00 41.26 ? 2    ASN B CG  1 
ATOM   3223 O  OD1 . ASN B 1 13  ? 69.765  77.771  119.107 1.00 41.26 ? 2    ASN B OD1 1 
ATOM   3224 N  ND2 . ASN B 1 13  ? 71.466  79.182  119.497 1.00 41.26 ? 2    ASN B ND2 1 
ATOM   3225 N  N   . LEU B 1 14  ? 71.268  76.038  114.610 1.00 33.48 ? 3    LEU B N   1 
ATOM   3226 C  CA  . LEU B 1 14  ? 71.826  75.774  113.291 1.00 33.48 ? 3    LEU B CA  1 
ATOM   3227 C  C   . LEU B 1 14  ? 71.513  76.963  112.395 1.00 33.48 ? 3    LEU B C   1 
ATOM   3228 O  O   . LEU B 1 14  ? 70.344  77.313  112.215 1.00 33.48 ? 3    LEU B O   1 
ATOM   3229 C  CB  . LEU B 1 14  ? 71.249  74.485  112.710 1.00 33.48 ? 3    LEU B CB  1 
ATOM   3230 C  CG  . LEU B 1 14  ? 71.952  73.856  111.508 1.00 33.48 ? 3    LEU B CG  1 
ATOM   3231 C  CD1 . LEU B 1 14  ? 71.675  72.374  111.481 1.00 33.48 ? 3    LEU B CD1 1 
ATOM   3232 C  CD2 . LEU B 1 14  ? 71.500  74.493  110.214 1.00 33.48 ? 3    LEU B CD2 1 
ATOM   3233 N  N   . THR B 1 15  ? 72.552  77.573  111.836 1.00 28.18 ? 4    THR B N   1 
ATOM   3234 C  CA  . THR B 1 15  ? 72.419  78.778  111.028 1.00 28.18 ? 4    THR B CA  1 
ATOM   3235 C  C   . THR B 1 15  ? 72.578  78.430  109.556 1.00 28.18 ? 4    THR B C   1 
ATOM   3236 O  O   . THR B 1 15  ? 73.527  77.739  109.179 1.00 28.18 ? 4    THR B O   1 
ATOM   3237 C  CB  . THR B 1 15  ? 73.460  79.823  111.434 1.00 28.18 ? 4    THR B CB  1 
ATOM   3238 O  OG1 . THR B 1 15  ? 73.126  80.361  112.718 1.00 28.18 ? 4    THR B OG1 1 
ATOM   3239 C  CG2 . THR B 1 15  ? 73.513  80.953  110.425 1.00 28.18 ? 4    THR B CG2 1 
ATOM   3240 N  N   . VAL B 1 16  ? 71.649  78.906  108.733 1.00 25.27 ? 5    VAL B N   1 
ATOM   3241 C  CA  . VAL B 1 16  ? 71.692  78.729  107.287 1.00 25.27 ? 5    VAL B CA  1 
ATOM   3242 C  C   . VAL B 1 16  ? 71.964  80.088  106.662 1.00 25.27 ? 5    VAL B C   1 
ATOM   3243 O  O   . VAL B 1 16  ? 71.251  81.056  106.944 1.00 25.27 ? 5    VAL B O   1 
ATOM   3244 C  CB  . VAL B 1 16  ? 70.380  78.131  106.750 1.00 25.27 ? 5    VAL B CB  1 
ATOM   3245 C  CG1 . VAL B 1 16  ? 70.439  77.992  105.243 1.00 25.27 ? 5    VAL B CG1 1 
ATOM   3246 C  CG2 . VAL B 1 16  ? 70.101  76.790  107.395 1.00 25.27 ? 5    VAL B CG2 1 
ATOM   3247 N  N   . ALA B 1 17  ? 72.992  80.164  105.825 1.00 21.67 ? 6    ALA B N   1 
ATOM   3248 C  CA  . ALA B 1 17  ? 73.392  81.413  105.194 1.00 21.67 ? 6    ALA B CA  1 
ATOM   3249 C  C   . ALA B 1 17  ? 72.869  81.452  103.767 1.00 21.67 ? 6    ALA B C   1 
ATOM   3250 O  O   . ALA B 1 17  ? 73.143  80.546  102.977 1.00 21.67 ? 6    ALA B O   1 
ATOM   3251 C  CB  . ALA B 1 17  ? 74.910  81.569  105.203 1.00 21.67 ? 6    ALA B CB  1 
ATOM   3252 N  N   . VAL B 1 18  ? 72.129  82.506  103.440 1.00 21.15 ? 7    VAL B N   1 
ATOM   3253 C  CA  . VAL B 1 18  ? 71.468  82.650  102.149 1.00 21.15 ? 7    VAL B CA  1 
ATOM   3254 C  C   . VAL B 1 18  ? 72.151  83.771  101.384 1.00 21.15 ? 7    VAL B C   1 
ATOM   3255 O  O   . VAL B 1 18  ? 72.318  84.874  101.913 1.00 21.15 ? 7    VAL B O   1 
ATOM   3256 C  CB  . VAL B 1 18  ? 69.968  82.944  102.318 1.00 21.15 ? 7    VAL B CB  1 
ATOM   3257 C  CG1 . VAL B 1 18  ? 69.344  83.291  100.987 1.00 21.15 ? 7    VAL B CG1 1 
ATOM   3258 C  CG2 . VAL B 1 18  ? 69.265  81.765  102.948 1.00 21.15 ? 7    VAL B CG2 1 
ATOM   3259 N  N   . VAL B 1 19  ? 72.545  83.493  100.145 1.00 19.96 ? 8    VAL B N   1 
ATOM   3260 C  CA  . VAL B 1 19  ? 73.121  84.501  99.255  1.00 19.96 ? 8    VAL B CA  1 
ATOM   3261 C  C   . VAL B 1 19  ? 72.314  84.443  97.962  1.00 19.96 ? 8    VAL B C   1 
ATOM   3262 O  O   . VAL B 1 19  ? 72.641  83.694  97.039  1.00 19.96 ? 8    VAL B O   1 
ATOM   3263 C  CB  . VAL B 1 19  ? 74.613  84.277  98.993  1.00 19.96 ? 8    VAL B CB  1 
ATOM   3264 C  CG1 . VAL B 1 19  ? 75.136  85.290  98.007  1.00 19.96 ? 8    VAL B CG1 1 
ATOM   3265 C  CG2 . VAL B 1 19  ? 75.391  84.362  100.285 1.00 19.96 ? 8    VAL B CG2 1 
ATOM   3266 N  N   . LEU B 1 20  ? 71.257  85.238  97.887  1.00 21.69 ? 9    LEU B N   1 
ATOM   3267 C  CA  . LEU B 1 20  ? 70.331  85.241  96.768  1.00 21.69 ? 9    LEU B CA  1 
ATOM   3268 C  C   . LEU B 1 20  ? 69.896  86.673  96.511  1.00 21.69 ? 9    LEU B C   1 
ATOM   3269 O  O   . LEU B 1 20  ? 70.063  87.540  97.374  1.00 21.69 ? 9    LEU B O   1 
ATOM   3270 C  CB  . LEU B 1 20  ? 69.101  84.369  97.052  1.00 21.69 ? 9    LEU B CB  1 
ATOM   3271 C  CG  . LEU B 1 20  ? 69.299  82.855  97.124  1.00 21.69 ? 9    LEU B CG  1 
ATOM   3272 C  CD1 . LEU B 1 20  ? 68.089  82.204  97.743  1.00 21.69 ? 9    LEU B CD1 1 
ATOM   3273 C  CD2 . LEU B 1 20  ? 69.556  82.277  95.755  1.00 21.69 ? 9    LEU B CD2 1 
ATOM   3274 N  N   . PRO B 1 21  ? 69.344  86.959  95.328  1.00 23.82 ? 10   PRO B N   1 
ATOM   3275 C  CA  . PRO B 1 21  ? 68.789  88.296  95.088  1.00 23.82 ? 10   PRO B CA  1 
ATOM   3276 C  C   . PRO B 1 21  ? 67.698  88.643  96.085  1.00 23.82 ? 10   PRO B C   1 
ATOM   3277 O  O   . PRO B 1 21  ? 66.630  88.027  96.081  1.00 23.82 ? 10   PRO B O   1 
ATOM   3278 C  CB  . PRO B 1 21  ? 68.239  88.188  93.663  1.00 23.82 ? 10   PRO B CB  1 
ATOM   3279 C  CG  . PRO B 1 21  ? 69.055  87.139  93.039  1.00 23.82 ? 10   PRO B CG  1 
ATOM   3280 C  CD  . PRO B 1 21  ? 69.286  86.132  94.115  1.00 23.82 ? 10   PRO B CD  1 
ATOM   3281 N  N   . LEU B 1 22  ? 67.948  89.629  96.940  1.00 24.02 ? 11   LEU B N   1 
ATOM   3282 C  CA  . LEU B 1 22  ? 67.019  89.931  98.020  1.00 24.02 ? 11   LEU B CA  1 
ATOM   3283 C  C   . LEU B 1 22  ? 65.935  90.916  97.617  1.00 24.02 ? 11   LEU B C   1 
ATOM   3284 O  O   . LEU B 1 22  ? 64.856  90.911  98.219  1.00 24.02 ? 11   LEU B O   1 
ATOM   3285 C  CB  . LEU B 1 22  ? 67.775  90.492  99.227  1.00 24.02 ? 11   LEU B CB  1 
ATOM   3286 C  CG  . LEU B 1 22  ? 68.733  89.570  99.982  1.00 24.02 ? 11   LEU B CG  1 
ATOM   3287 C  CD1 . LEU B 1 22  ? 69.070  90.183  101.324 1.00 24.02 ? 11   LEU B CD1 1 
ATOM   3288 C  CD2 . LEU B 1 22  ? 68.165  88.181  100.166 1.00 24.02 ? 11   LEU B CD2 1 
ATOM   3289 N  N   . ALA B 1 23  ? 66.186  91.765  96.619  1.00 27.96 ? 12   ALA B N   1 
ATOM   3290 C  CA  . ALA B 1 23  ? 65.247  92.820  96.267  1.00 27.96 ? 12   ALA B CA  1 
ATOM   3291 C  C   . ALA B 1 23  ? 64.957  92.910  94.774  1.00 27.96 ? 12   ALA B C   1 
ATOM   3292 O  O   . ALA B 1 23  ? 64.410  93.925  94.331  1.00 27.96 ? 12   ALA B O   1 
ATOM   3293 C  CB  . ALA B 1 23  ? 65.767  94.171  96.765  1.00 27.96 ? 12   ALA B CB  1 
ATOM   3294 N  N   . ASN B 1 24  ? 65.289  91.892  93.986  1.00 27.69 ? 13   ASN B N   1 
ATOM   3295 C  CA  . ASN B 1 24  ? 65.070  91.928  92.542  1.00 27.69 ? 13   ASN B CA  1 
ATOM   3296 C  C   . ASN B 1 24  ? 64.252  90.686  92.204  1.00 27.69 ? 13   ASN B C   1 
ATOM   3297 O  O   . ASN B 1 24  ? 64.803  89.607  91.980  1.00 27.69 ? 13   ASN B O   1 
ATOM   3298 C  CB  . ASN B 1 24  ? 66.388  91.972  91.791  1.00 27.69 ? 13   ASN B CB  1 
ATOM   3299 C  CG  . ASN B 1 24  ? 66.214  91.855  90.292  1.00 27.69 ? 13   ASN B CG  1 
ATOM   3300 O  OD1 . ASN B 1 24  ? 65.763  90.842  89.769  1.00 27.69 ? 13   ASN B OD1 1 
ATOM   3301 N  ND2 . ASN B 1 24  ? 66.581  92.922  89.594  1.00 27.69 ? 13   ASN B ND2 1 
ATOM   3302 N  N   . THR B 1 25  ? 62.927  90.843  92.176  1.00 29.20 ? 14   THR B N   1 
ATOM   3303 C  CA  . THR B 1 25  ? 62.004  89.716  92.045  1.00 29.20 ? 14   THR B CA  1 
ATOM   3304 C  C   . THR B 1 25  ? 61.784  89.353  90.575  1.00 29.20 ? 14   THR B C   1 
ATOM   3305 O  O   . THR B 1 25  ? 60.671  89.386  90.055  1.00 29.20 ? 14   THR B O   1 
ATOM   3306 C  CB  . THR B 1 25  ? 60.679  90.045  92.716  1.00 29.20 ? 14   THR B CB  1 
ATOM   3307 O  OG1 . THR B 1 25  ? 59.753  90.511  91.730  1.00 29.20 ? 14   THR B OG1 1 
ATOM   3308 C  CG2 . THR B 1 25  ? 60.860  91.124  93.766  1.00 29.20 ? 14   THR B CG2 1 
ATOM   3309 N  N   . SER B 1 26  ? 62.879  88.995  89.904  1.00 27.16 ? 15   SER B N   1 
ATOM   3310 C  CA  . SER B 1 26  ? 62.813  88.682  88.483  1.00 27.16 ? 15   SER B CA  1 
ATOM   3311 C  C   . SER B 1 26  ? 63.624  87.450  88.110  1.00 27.16 ? 15   SER B C   1 
ATOM   3312 O  O   . SER B 1 26  ? 63.742  87.147  86.917  1.00 27.16 ? 15   SER B O   1 
ATOM   3313 C  CB  . SER B 1 26  ? 63.293  89.871  87.654  1.00 27.16 ? 15   SER B CB  1 
ATOM   3314 O  OG  . SER B 1 26  ? 64.689  89.809  87.444  1.00 27.16 ? 15   SER B OG  1 
ATOM   3315 N  N   . TYR B 1 27  ? 64.181  86.737  89.076  1.00 25.72 ? 16   TYR B N   1 
ATOM   3316 C  CA  . TYR B 1 27  ? 64.922  85.511  88.851  1.00 25.72 ? 16   TYR B CA  1 
ATOM   3317 C  C   . TYR B 1 27  ? 64.124  84.326  89.376  1.00 25.72 ? 16   TYR B C   1 
ATOM   3318 O  O   . TYR B 1 27  ? 63.359  84.470  90.333  1.00 25.72 ? 16   TYR B O   1 
ATOM   3319 C  CB  . TYR B 1 27  ? 66.274  85.545  89.567  1.00 25.72 ? 16   TYR B CB  1 
ATOM   3320 C  CG  . TYR B 1 27  ? 67.249  86.558  89.033  1.00 25.72 ? 16   TYR B CG  1 
ATOM   3321 C  CD1 . TYR B 1 27  ? 67.968  86.316  87.880  1.00 25.72 ? 16   TYR B CD1 1 
ATOM   3322 C  CD2 . TYR B 1 27  ? 67.465  87.750  89.696  1.00 25.72 ? 16   TYR B CD2 1 
ATOM   3323 C  CE1 . TYR B 1 27  ? 68.865  87.234  87.399  1.00 25.72 ? 16   TYR B CE1 1 
ATOM   3324 C  CE2 . TYR B 1 27  ? 68.360  88.675  89.220  1.00 25.72 ? 16   TYR B CE2 1 
ATOM   3325 C  CZ  . TYR B 1 27  ? 69.057  88.411  88.072  1.00 25.72 ? 16   TYR B CZ  1 
ATOM   3326 O  OH  . TYR B 1 27  ? 69.953  89.328  87.588  1.00 25.72 ? 16   TYR B OH  1 
ATOM   3327 N  N   . PRO B 1 28  ? 64.266  83.140  88.784  1.00 24.65 ? 17   PRO B N   1 
ATOM   3328 C  CA  . PRO B 1 28  ? 63.579  81.972  89.349  1.00 24.65 ? 17   PRO B CA  1 
ATOM   3329 C  C   . PRO B 1 28  ? 64.081  81.591  90.727  1.00 24.65 ? 17   PRO B C   1 
ATOM   3330 O  O   . PRO B 1 28  ? 63.368  80.900  91.461  1.00 24.65 ? 17   PRO B O   1 
ATOM   3331 C  CB  . PRO B 1 28  ? 63.844  80.878  88.310  1.00 24.65 ? 17   PRO B CB  1 
ATOM   3332 C  CG  . PRO B 1 28  ? 65.098  81.267  87.674  1.00 24.65 ? 17   PRO B CG  1 
ATOM   3333 C  CD  . PRO B 1 28  ? 65.130  82.767  87.653  1.00 24.65 ? 17   PRO B CD  1 
ATOM   3334 N  N   . TRP B 1 29  ? 65.277  82.038  91.109  1.00 23.68 ? 18   TRP B N   1 
ATOM   3335 C  CA  . TRP B 1 29  ? 65.826  81.818  92.441  1.00 23.68 ? 18   TRP B CA  1 
ATOM   3336 C  C   . TRP B 1 29  ? 65.819  83.090  93.276  1.00 23.68 ? 18   TRP B C   1 
ATOM   3337 O  O   . TRP B 1 29  ? 66.535  83.175  94.276  1.00 23.68 ? 18   TRP B O   1 
ATOM   3338 C  CB  . TRP B 1 29  ? 67.247  81.265  92.348  1.00 23.68 ? 18   TRP B CB  1 
ATOM   3339 C  CG  . TRP B 1 29  ? 68.081  81.988  91.358  1.00 23.68 ? 18   TRP B CG  1 
ATOM   3340 C  CD1 . TRP B 1 29  ? 68.662  83.205  91.513  1.00 23.68 ? 18   TRP B CD1 1 
ATOM   3341 C  CD2 . TRP B 1 29  ? 68.420  81.544  90.046  1.00 23.68 ? 18   TRP B CD2 1 
ATOM   3342 N  NE1 . TRP B 1 29  ? 69.344  83.550  90.377  1.00 23.68 ? 18   TRP B NE1 1 
ATOM   3343 C  CE2 . TRP B 1 29  ? 69.213  82.542  89.460  1.00 23.68 ? 18   TRP B CE2 1 
ATOM   3344 C  CE3 . TRP B 1 29  ? 68.134  80.393  89.310  1.00 23.68 ? 18   TRP B CE3 1 
ATOM   3345 C  CZ2 . TRP B 1 29  ? 69.717  82.430  88.174  1.00 23.68 ? 18   TRP B CZ2 1 
ATOM   3346 C  CZ3 . TRP B 1 29  ? 68.634  80.283  88.037  1.00 23.68 ? 18   TRP B CZ3 1 
ATOM   3347 C  CH2 . TRP B 1 29  ? 69.419  81.293  87.480  1.00 23.68 ? 18   TRP B CH2 1 
ATOM   3348 N  N   . SER B 1 30  ? 65.032  84.085  92.884  1.00 25.29 ? 19   SER B N   1 
ATOM   3349 C  CA  . SER B 1 30  ? 64.959  85.317  93.650  1.00 25.29 ? 19   SER B CA  1 
ATOM   3350 C  C   . SER B 1 30  ? 64.386  85.040  95.029  1.00 25.29 ? 19   SER B C   1 
ATOM   3351 O  O   . SER B 1 30  ? 63.489  84.212  95.191  1.00 25.29 ? 19   SER B O   1 
ATOM   3352 C  CB  . SER B 1 30  ? 64.097  86.340  92.919  1.00 25.29 ? 19   SER B CB  1 
ATOM   3353 O  OG  . SER B 1 30  ? 63.996  87.538  93.661  1.00 25.29 ? 19   SER B OG  1 
ATOM   3354 N  N   . TRP B 1 31  ? 64.906  85.745  96.032  1.00 24.13 ? 20   TRP B N   1 
ATOM   3355 C  CA  . TRP B 1 31  ? 64.421  85.546  97.390  1.00 24.13 ? 20   TRP B CA  1 
ATOM   3356 C  C   . TRP B 1 31  ? 62.932  85.829  97.514  1.00 24.13 ? 20   TRP B C   1 
ATOM   3357 O  O   . TRP B 1 31  ? 62.292  85.304  98.426  1.00 24.13 ? 20   TRP B O   1 
ATOM   3358 C  CB  . TRP B 1 31  ? 65.203  86.432  98.358  1.00 24.13 ? 20   TRP B CB  1 
ATOM   3359 C  CG  . TRP B 1 31  ? 64.810  86.259  99.789  1.00 24.13 ? 20   TRP B CG  1 
ATOM   3360 C  CD1 . TRP B 1 31  ? 64.202  87.180  100.584 1.00 24.13 ? 20   TRP B CD1 1 
ATOM   3361 C  CD2 . TRP B 1 31  ? 64.998  85.094  100.598 1.00 24.13 ? 20   TRP B CD2 1 
ATOM   3362 N  NE1 . TRP B 1 31  ? 63.997  86.663  101.837 1.00 24.13 ? 20   TRP B NE1 1 
ATOM   3363 C  CE2 . TRP B 1 31  ? 64.480  85.383  101.871 1.00 24.13 ? 20   TRP B CE2 1 
ATOM   3364 C  CE3 . TRP B 1 31  ? 65.556  83.834  100.370 1.00 24.13 ? 20   TRP B CE3 1 
ATOM   3365 C  CZ2 . TRP B 1 31  ? 64.501  84.462  102.909 1.00 24.13 ? 20   TRP B CZ2 1 
ATOM   3366 C  CZ3 . TRP B 1 31  ? 65.575  82.924  101.402 1.00 24.13 ? 20   TRP B CZ3 1 
ATOM   3367 C  CH2 . TRP B 1 31  ? 65.051  83.241  102.655 1.00 24.13 ? 20   TRP B CH2 1 
ATOM   3368 N  N   . ALA B 1 32  ? 62.359  86.625  96.612  1.00 28.01 ? 21   ALA B N   1 
ATOM   3369 C  CA  . ALA B 1 32  ? 60.930  86.909  96.686  1.00 28.01 ? 21   ALA B CA  1 
ATOM   3370 C  C   . ALA B 1 32  ? 60.096  85.645  96.543  1.00 28.01 ? 21   ALA B C   1 
ATOM   3371 O  O   . ALA B 1 32  ? 59.020  85.544  97.139  1.00 28.01 ? 21   ALA B O   1 
ATOM   3372 C  CB  . ALA B 1 32  ? 60.542  87.917  95.609  1.00 28.01 ? 21   ALA B CB  1 
ATOM   3373 N  N   . ARG B 1 33  ? 60.569  84.675  95.760  1.00 29.05 ? 22   ARG B N   1 
ATOM   3374 C  CA  . ARG B 1 33  ? 59.848  83.427  95.559  1.00 29.05 ? 22   ARG B CA  1 
ATOM   3375 C  C   . ARG B 1 33  ? 60.520  82.222  96.198  1.00 29.05 ? 22   ARG B C   1 
ATOM   3376 O  O   . ARG B 1 33  ? 59.873  81.181  96.333  1.00 29.05 ? 22   ARG B O   1 
ATOM   3377 C  CB  . ARG B 1 33  ? 59.660  83.154  94.061  1.00 29.05 ? 22   ARG B CB  1 
ATOM   3378 C  CG  . ARG B 1 33  ? 60.924  83.246  93.250  1.00 29.05 ? 22   ARG B CG  1 
ATOM   3379 C  CD  . ARG B 1 33  ? 60.625  83.172  91.773  1.00 29.05 ? 22   ARG B CD  1 
ATOM   3380 N  NE  . ARG B 1 33  ? 60.620  84.490  91.155  1.00 29.05 ? 22   ARG B NE  1 
ATOM   3381 C  CZ  . ARG B 1 33  ? 60.122  84.748  89.952  1.00 29.05 ? 22   ARG B CZ  1 
ATOM   3382 N  NH1 . ARG B 1 33  ? 59.588  83.778  89.228  1.00 29.05 ? 22   ARG B NH1 1 
ATOM   3383 N  NH2 . ARG B 1 33  ? 60.159  85.981  89.472  1.00 29.05 ? 22   ARG B NH2 1 
ATOM   3384 N  N   . VAL B 1 34  ? 61.786  82.333  96.598  1.00 24.79 ? 23   VAL B N   1 
ATOM   3385 C  CA  . VAL B 1 34  ? 62.443  81.253  97.323  1.00 24.79 ? 23   VAL B CA  1 
ATOM   3386 C  C   . VAL B 1 34  ? 62.272  81.388  98.831  1.00 24.79 ? 23   VAL B C   1 
ATOM   3387 O  O   . VAL B 1 34  ? 62.375  80.384  99.548  1.00 24.79 ? 23   VAL B O   1 
ATOM   3388 C  CB  . VAL B 1 34  ? 63.939  81.194  96.957  1.00 24.79 ? 23   VAL B CB  1 
ATOM   3389 C  CG1 . VAL B 1 34  ? 64.728  80.421  97.991  1.00 24.79 ? 23   VAL B CG1 1 
ATOM   3390 C  CG2 . VAL B 1 34  ? 64.120  80.565  95.596  1.00 24.79 ? 23   VAL B CG2 1 
ATOM   3391 N  N   . GLY B 1 35  ? 61.999  82.588  99.333  1.00 26.66 ? 24   GLY B N   1 
ATOM   3392 C  CA  . GLY B 1 35  ? 61.857  82.813  100.749 1.00 26.66 ? 24   GLY B CA  1 
ATOM   3393 C  C   . GLY B 1 35  ? 60.681  82.076  101.345 1.00 26.66 ? 24   GLY B C   1 
ATOM   3394 O  O   . GLY B 1 35  ? 60.790  81.446  102.399 1.00 26.66 ? 24   GLY B O   1 
ATOM   3395 N  N   . PRO B 1 36  ? 59.520  82.155  100.694 1.00 31.18 ? 25   PRO B N   1 
ATOM   3396 C  CA  . PRO B 1 36  ? 58.382  81.352  101.161 1.00 31.18 ? 25   PRO B CA  1 
ATOM   3397 C  C   . PRO B 1 36  ? 58.652  79.861  101.136 1.00 31.18 ? 25   PRO B C   1 
ATOM   3398 O  O   . PRO B 1 36  ? 58.169  79.141  102.016 1.00 31.18 ? 25   PRO B O   1 
ATOM   3399 C  CB  . PRO B 1 36  ? 57.256  81.744  100.198 1.00 31.18 ? 25   PRO B CB  1 
ATOM   3400 C  CG  . PRO B 1 36  ? 57.662  83.028  99.608  1.00 31.18 ? 25   PRO B CG  1 
ATOM   3401 C  CD  . PRO B 1 36  ? 59.144  83.072  99.607  1.00 31.18 ? 25   PRO B CD  1 
ATOM   3402 N  N   . ALA B 1 37  ? 59.418  79.370  100.161 1.00 29.15 ? 26   ALA B N   1 
ATOM   3403 C  CA  . ALA B 1 37  ? 59.738  77.947  100.114 1.00 29.15 ? 26   ALA B CA  1 
ATOM   3404 C  C   . ALA B 1 37  ? 60.584  77.539  101.313 1.00 29.15 ? 26   ALA B C   1 
ATOM   3405 O  O   . ALA B 1 37  ? 60.307  76.531  101.973 1.00 29.15 ? 26   ALA B O   1 
ATOM   3406 C  CB  . ALA B 1 37  ? 60.460  77.623  98.808  1.00 29.15 ? 26   ALA B CB  1 
ATOM   3407 N  N   . VAL B 1 38  ? 61.625  78.315  101.610 1.00 27.85 ? 27   VAL B N   1 
ATOM   3408 C  CA  . VAL B 1 38  ? 62.465  78.025  102.766 1.00 27.85 ? 27   VAL B CA  1 
ATOM   3409 C  C   . VAL B 1 38  ? 61.650  78.118  104.047 1.00 27.85 ? 27   VAL B C   1 
ATOM   3410 O  O   . VAL B 1 38  ? 61.822  77.318  104.972 1.00 27.85 ? 27   VAL B O   1 
ATOM   3411 C  CB  . VAL B 1 38  ? 63.677  78.976  102.792 1.00 27.85 ? 27   VAL B CB  1 
ATOM   3412 C  CG1 . VAL B 1 38  ? 64.381  78.912  104.130 1.00 27.85 ? 27   VAL B CG1 1 
ATOM   3413 C  CG2 . VAL B 1 38  ? 64.636  78.635  101.671 1.00 27.85 ? 27   VAL B CG2 1 
ATOM   3414 N  N   . GLU B 1 39  ? 60.754  79.102  104.126 1.00 33.38 ? 28   GLU B N   1 
ATOM   3415 C  CA  . GLU B 1 39  ? 59.928  79.253  105.319 1.00 33.38 ? 28   GLU B CA  1 
ATOM   3416 C  C   . GLU B 1 39  ? 59.010  78.053  105.510 1.00 33.38 ? 28   GLU B C   1 
ATOM   3417 O  O   . GLU B 1 39  ? 58.850  77.557  106.631 1.00 33.38 ? 28   GLU B O   1 
ATOM   3418 C  CB  . GLU B 1 39  ? 59.120  80.545  105.223 1.00 33.38 ? 28   GLU B CB  1 
ATOM   3419 C  CG  . GLU B 1 39  ? 58.298  80.863  106.457 1.00 33.38 ? 28   GLU B CG  1 
ATOM   3420 C  CD  . GLU B 1 39  ? 57.435  82.092  106.273 1.00 33.38 ? 28   GLU B CD  1 
ATOM   3421 O  OE1 . GLU B 1 39  ? 56.821  82.544  107.261 1.00 33.38 ? 28   GLU B OE1 1 
ATOM   3422 O  OE2 . GLU B 1 39  ? 57.377  82.611  105.140 1.00 33.38 ? 28   GLU B OE2 1 
ATOM   3423 N  N   . LEU B 1 40  ? 58.395  77.573  104.429 1.00 33.64 ? 29   LEU B N   1 
ATOM   3424 C  CA  . LEU B 1 40  ? 57.559  76.382  104.522 1.00 33.64 ? 29   LEU B CA  1 
ATOM   3425 C  C   . LEU B 1 40  ? 58.379  75.169  104.938 1.00 33.64 ? 29   LEU B C   1 
ATOM   3426 O  O   . LEU B 1 40  ? 57.934  74.360  105.759 1.00 33.64 ? 29   LEU B O   1 
ATOM   3427 C  CB  . LEU B 1 40  ? 56.870  76.123  103.183 1.00 33.64 ? 29   LEU B CB  1 
ATOM   3428 C  CG  . LEU B 1 40  ? 55.535  76.829  102.958 1.00 33.64 ? 29   LEU B CG  1 
ATOM   3429 C  CD1 . LEU B 1 40  ? 55.212  76.876  101.482 1.00 33.64 ? 29   LEU B CD1 1 
ATOM   3430 C  CD2 . LEU B 1 40  ? 54.426  76.135  103.724 1.00 33.64 ? 29   LEU B CD2 1 
ATOM   3431 N  N   . ALA B 1 41  ? 59.582  75.024  104.380 1.00 31.74 ? 30   ALA B N   1 
ATOM   3432 C  CA  . ALA B 1 41  ? 60.440  73.910  104.768 1.00 31.74 ? 30   ALA B CA  1 
ATOM   3433 C  C   . ALA B 1 41  ? 60.747  73.954  106.258 1.00 31.74 ? 30   ALA B C   1 
ATOM   3434 O  O   . ALA B 1 41  ? 60.629  72.944  106.960 1.00 31.74 ? 30   ALA B O   1 
ATOM   3435 C  CB  . ALA B 1 41  ? 61.734  73.940  103.954 1.00 31.74 ? 30   ALA B CB  1 
ATOM   3436 N  N   . LEU B 1 42  ? 61.136  75.125  106.761 1.00 31.94 ? 31   LEU B N   1 
ATOM   3437 C  CA  . LEU B 1 42  ? 61.502  75.240  108.168 1.00 31.94 ? 31   LEU B CA  1 
ATOM   3438 C  C   . LEU B 1 42  ? 60.296  75.022  109.072 1.00 31.94 ? 31   LEU B C   1 
ATOM   3439 O  O   . LEU B 1 42  ? 60.427  74.450  110.160 1.00 31.94 ? 31   LEU B O   1 
ATOM   3440 C  CB  . LEU B 1 42  ? 62.135  76.604  108.433 1.00 31.94 ? 31   LEU B CB  1 
ATOM   3441 C  CG  . LEU B 1 42  ? 63.480  76.869  107.756 1.00 31.94 ? 31   LEU B CG  1 
ATOM   3442 C  CD1 . LEU B 1 42  ? 64.041  78.198  108.212 1.00 31.94 ? 31   LEU B CD1 1 
ATOM   3443 C  CD2 . LEU B 1 42  ? 64.464  75.757  108.044 1.00 31.94 ? 31   LEU B CD2 1 
ATOM   3444 N  N   . ALA B 1 43  ? 59.116  75.477  108.649 1.00 36.79 ? 32   ALA B N   1 
ATOM   3445 C  CA  . ALA B 1 43  ? 57.908  75.181  109.408 1.00 36.79 ? 32   ALA B CA  1 
ATOM   3446 C  C   . ALA B 1 43  ? 57.608  73.690  109.410 1.00 36.79 ? 32   ALA B C   1 
ATOM   3447 O  O   . ALA B 1 43  ? 57.054  73.171  110.384 1.00 36.79 ? 32   ALA B O   1 
ATOM   3448 C  CB  . ALA B 1 43  ? 56.723  75.957  108.839 1.00 36.79 ? 32   ALA B CB  1 
ATOM   3449 N  N   . GLN B 1 44  ? 57.959  72.988  108.332 1.00 40.76 ? 33   GLN B N   1 
ATOM   3450 C  CA  . GLN B 1 44  ? 57.780  71.541  108.307 1.00 40.76 ? 33   GLN B CA  1 
ATOM   3451 C  C   . GLN B 1 44  ? 58.785  70.832  109.206 1.00 40.76 ? 33   GLN B C   1 
ATOM   3452 O  O   . GLN B 1 44  ? 58.465  69.791  109.787 1.00 40.76 ? 33   GLN B O   1 
ATOM   3453 C  CB  . GLN B 1 44  ? 57.899  71.025  106.876 1.00 40.76 ? 33   GLN B CB  1 
ATOM   3454 C  CG  . GLN B 1 44  ? 57.752  69.524  106.756 1.00 40.76 ? 33   GLN B CG  1 
ATOM   3455 C  CD  . GLN B 1 44  ? 57.610  69.070  105.324 1.00 40.76 ? 33   GLN B CD  1 
ATOM   3456 O  OE1 . GLN B 1 44  ? 57.559  69.886  104.406 1.00 40.76 ? 33   GLN B OE1 1 
ATOM   3457 N  NE2 . GLN B 1 44  ? 57.547  67.760  105.123 1.00 40.76 ? 33   GLN B NE2 1 
ATOM   3458 N  N   . VAL B 1 45  ? 60.002  71.366  109.321 1.00 37.90 ? 34   VAL B N   1 
ATOM   3459 C  CA  . VAL B 1 45  ? 60.998  70.756  110.200 1.00 37.90 ? 34   VAL B CA  1 
ATOM   3460 C  C   . VAL B 1 45  ? 60.524  70.801  111.645 1.00 37.90 ? 34   VAL B C   1 
ATOM   3461 O  O   . VAL B 1 45  ? 60.642  69.817  112.384 1.00 37.90 ? 34   VAL B O   1 
ATOM   3462 C  CB  . VAL B 1 45  ? 62.360  71.455  110.033 1.00 37.90 ? 34   VAL B CB  1 
ATOM   3463 C  CG1 . VAL B 1 45  ? 63.327  71.003  111.110 1.00 37.90 ? 34   VAL B CG1 1 
ATOM   3464 C  CG2 . VAL B 1 45  ? 62.934  71.184  108.660 1.00 37.90 ? 34   VAL B CG2 1 
ATOM   3465 N  N   . LYS B 1 46  ? 59.982  71.943  112.072 1.00 42.52 ? 35   LYS B N   1 
ATOM   3466 C  CA  . LYS B 1 46  ? 59.516  72.071  113.448 1.00 42.52 ? 35   LYS B CA  1 
ATOM   3467 C  C   . LYS B 1 46  ? 58.357  71.124  113.726 1.00 42.52 ? 35   LYS B C   1 
ATOM   3468 O  O   . LYS B 1 46  ? 58.275  70.531  114.808 1.00 42.52 ? 35   LYS B O   1 
ATOM   3469 C  CB  . LYS B 1 46  ? 59.106  73.515  113.730 1.00 42.52 ? 35   LYS B CB  1 
ATOM   3470 N  N   . ALA B 1 47  ? 57.448  70.969  112.762 1.00 44.88 ? 36   ALA B N   1 
ATOM   3471 C  CA  . ALA B 1 47  ? 56.295  70.101  112.970 1.00 44.88 ? 36   ALA B CA  1 
ATOM   3472 C  C   . ALA B 1 47  ? 56.721  68.660  113.215 1.00 44.88 ? 36   ALA B C   1 
ATOM   3473 O  O   . ALA B 1 47  ? 56.184  67.990  114.103 1.00 44.88 ? 36   ALA B O   1 
ATOM   3474 C  CB  . ALA B 1 47  ? 55.357  70.180  111.767 1.00 44.88 ? 36   ALA B CB  1 
ATOM   3475 N  N   . ARG B 1 48  ? 57.681  68.167  112.442 1.00 45.94 ? 37   ARG B N   1 
ATOM   3476 C  CA  . ARG B 1 48  ? 58.120  66.782  112.569 1.00 45.94 ? 37   ARG B CA  1 
ATOM   3477 C  C   . ARG B 1 48  ? 59.086  66.642  113.739 1.00 45.94 ? 37   ARG B C   1 
ATOM   3478 O  O   . ARG B 1 48  ? 60.137  67.293  113.739 1.00 45.94 ? 37   ARG B O   1 
ATOM   3479 C  CB  . ARG B 1 48  ? 58.798  66.321  111.287 1.00 45.94 ? 37   ARG B CB  1 
ATOM   3480 C  CG  . ARG B 1 48  ? 57.852  66.123  110.121 1.00 45.94 ? 37   ARG B CG  1 
ATOM   3481 C  CD  . ARG B 1 48  ? 58.595  65.681  108.875 1.00 45.94 ? 37   ARG B CD  1 
ATOM   3482 N  NE  . ARG B 1 48  ? 59.371  64.466  109.100 1.00 45.94 ? 37   ARG B NE  1 
ATOM   3483 C  CZ  . ARG B 1 48  ? 60.111  63.867  108.173 1.00 45.94 ? 37   ARG B CZ  1 
ATOM   3484 N  NH1 . ARG B 1 48  ? 60.176  64.362  106.944 1.00 45.94 ? 37   ARG B NH1 1 
ATOM   3485 N  NH2 . ARG B 1 48  ? 60.784  62.766  108.472 1.00 45.94 ? 37   ARG B NH2 1 
ATOM   3486 N  N   . PRO B 1 49  ? 58.783  65.815  114.746 1.00 50.38 ? 38   PRO B N   1 
ATOM   3487 C  CA  . PRO B 1 49  ? 59.784  65.535  115.785 1.00 50.38 ? 38   PRO B CA  1 
ATOM   3488 C  C   . PRO B 1 49  ? 60.908  64.628  115.315 1.00 50.38 ? 38   PRO B C   1 
ATOM   3489 O  O   . PRO B 1 49  ? 61.878  64.441  116.060 1.00 50.38 ? 38   PRO B O   1 
ATOM   3490 C  CB  . PRO B 1 49  ? 58.960  64.863  116.894 1.00 50.38 ? 38   PRO B CB  1 
ATOM   3491 C  CG  . PRO B 1 49  ? 57.540  65.241  116.600 1.00 50.38 ? 38   PRO B CG  1 
ATOM   3492 C  CD  . PRO B 1 49  ? 57.474  65.251  115.112 1.00 50.38 ? 38   PRO B CD  1 
ATOM   3493 N  N   . ASP B 1 50  ? 60.810  64.059  114.117 1.00 48.90 ? 39   ASP B N   1 
ATOM   3494 C  CA  . ASP B 1 50  ? 61.824  63.155  113.595 1.00 48.90 ? 39   ASP B CA  1 
ATOM   3495 C  C   . ASP B 1 50  ? 62.952  63.879  112.871 1.00 48.90 ? 39   ASP B C   1 
ATOM   3496 O  O   . ASP B 1 50  ? 63.881  63.219  112.396 1.00 48.90 ? 39   ASP B O   1 
ATOM   3497 C  CB  . ASP B 1 50  ? 61.181  62.140  112.646 1.00 48.90 ? 39   ASP B CB  1 
ATOM   3498 N  N   . LEU B 1 51  ? 62.894  65.205  112.769 1.00 42.23 ? 40   LEU B N   1 
ATOM   3499 C  CA  . LEU B 1 51  ? 63.931  65.995  112.118 1.00 42.23 ? 40   LEU B CA  1 
ATOM   3500 C  C   . LEU B 1 51  ? 64.570  66.910  113.150 1.00 42.23 ? 40   LEU B C   1 
ATOM   3501 O  O   . LEU B 1 51  ? 63.876  67.711  113.785 1.00 42.23 ? 40   LEU B O   1 
ATOM   3502 C  CB  . LEU B 1 51  ? 63.355  66.817  110.963 1.00 42.23 ? 40   LEU B CB  1 
ATOM   3503 C  CG  . LEU B 1 51  ? 63.057  66.074  109.659 1.00 42.23 ? 40   LEU B CG  1 
ATOM   3504 C  CD1 . LEU B 1 51  ? 62.516  67.034  108.618 1.00 42.23 ? 40   LEU B CD1 1 
ATOM   3505 C  CD2 . LEU B 1 51  ? 64.291  65.368  109.139 1.00 42.23 ? 40   LEU B CD2 1 
ATOM   3506 N  N   . LEU B 1 52  ? 65.891  66.794  113.306 1.00 40.94 ? 41   LEU B N   1 
ATOM   3507 C  CA  . LEU B 1 52  ? 66.680  67.637  114.197 1.00 40.94 ? 41   LEU B CA  1 
ATOM   3508 C  C   . LEU B 1 52  ? 65.934  67.900  115.499 1.00 40.94 ? 41   LEU B C   1 
ATOM   3509 O  O   . LEU B 1 52  ? 65.562  69.046  115.779 1.00 40.94 ? 41   LEU B O   1 
ATOM   3510 C  CB  . LEU B 1 52  ? 67.022  68.960  113.507 1.00 40.94 ? 41   LEU B CB  1 
ATOM   3511 C  CG  . LEU B 1 52  ? 68.319  69.051  112.703 1.00 40.94 ? 41   LEU B CG  1 
ATOM   3512 C  CD1 . LEU B 1 52  ? 68.574  70.492  112.326 1.00 40.94 ? 41   LEU B CD1 1 
ATOM   3513 C  CD2 . LEU B 1 52  ? 69.502  68.495  113.473 1.00 40.94 ? 41   LEU B CD2 1 
ATOM   3514 N  N   . PRO B 1 53  ? 65.681  66.877  116.312 1.00 46.87 ? 42   PRO B N   1 
ATOM   3515 C  CA  . PRO B 1 53  ? 64.956  67.106  117.566 1.00 46.87 ? 42   PRO B CA  1 
ATOM   3516 C  C   . PRO B 1 53  ? 65.708  68.065  118.476 1.00 46.87 ? 42   PRO B C   1 
ATOM   3517 O  O   . PRO B 1 53  ? 66.928  67.978  118.629 1.00 46.87 ? 42   PRO B O   1 
ATOM   3518 C  CB  . PRO B 1 53  ? 64.858  65.704  118.178 1.00 46.87 ? 42   PRO B CB  1 
ATOM   3519 C  CG  . PRO B 1 53  ? 65.068  64.769  117.033 1.00 46.87 ? 42   PRO B CG  1 
ATOM   3520 C  CD  . PRO B 1 53  ? 66.038  65.461  116.140 1.00 46.87 ? 42   PRO B CD  1 
ATOM   3521 N  N   . GLY B 1 54  ? 64.965  68.978  119.092 1.00 48.64 ? 43   GLY B N   1 
ATOM   3522 C  CA  . GLY B 1 54  ? 65.574  69.925  120.012 1.00 48.64 ? 43   GLY B CA  1 
ATOM   3523 C  C   . GLY B 1 54  ? 66.613  70.819  119.373 1.00 48.64 ? 43   GLY B C   1 
ATOM   3524 O  O   . GLY B 1 54  ? 67.685  71.036  119.953 1.00 48.64 ? 43   GLY B O   1 
ATOM   3525 N  N   . TRP B 1 55  ? 66.324  71.338  118.182 1.00 43.23 ? 44   TRP B N   1 
ATOM   3526 C  CA  . TRP B 1 55  ? 67.203  72.270  117.492 1.00 43.23 ? 44   TRP B CA  1 
ATOM   3527 C  C   . TRP B 1 55  ? 66.350  73.348  116.846 1.00 43.23 ? 44   TRP B C   1 
ATOM   3528 O  O   . TRP B 1 55  ? 65.191  73.112  116.498 1.00 43.23 ? 44   TRP B O   1 
ATOM   3529 C  CB  . TRP B 1 55  ? 68.050  71.574  116.416 1.00 43.23 ? 44   TRP B CB  1 
ATOM   3530 C  CG  . TRP B 1 55  ? 69.280  70.900  116.933 1.00 43.23 ? 44   TRP B CG  1 
ATOM   3531 C  CD1 . TRP B 1 55  ? 69.334  69.818  117.755 1.00 43.23 ? 44   TRP B CD1 1 
ATOM   3532 C  CD2 . TRP B 1 55  ? 70.638  71.255  116.648 1.00 43.23 ? 44   TRP B CD2 1 
ATOM   3533 N  NE1 . TRP B 1 55  ? 70.639  69.478  118.007 1.00 43.23 ? 44   TRP B NE1 1 
ATOM   3534 C  CE2 . TRP B 1 55  ? 71.460  70.346  117.338 1.00 43.23 ? 44   TRP B CE2 1 
ATOM   3535 C  CE3 . TRP B 1 55  ? 71.238  72.253  115.879 1.00 43.23 ? 44   TRP B CE3 1 
ATOM   3536 C  CZ2 . TRP B 1 55  ? 72.848  70.407  117.285 1.00 43.23 ? 44   TRP B CZ2 1 
ATOM   3537 C  CZ3 . TRP B 1 55  ? 72.617  72.311  115.829 1.00 43.23 ? 44   TRP B CZ3 1 
ATOM   3538 C  CH2 . TRP B 1 55  ? 73.405  71.397  116.527 1.00 43.23 ? 44   TRP B CH2 1 
ATOM   3539 N  N   . THR B 1 56  ? 66.930  74.533  116.684 1.00 40.57 ? 45   THR B N   1 
ATOM   3540 C  CA  . THR B 1 56  ? 66.280  75.639  115.994 1.00 40.57 ? 45   THR B CA  1 
ATOM   3541 C  C   . THR B 1 56  ? 67.115  76.028  114.785 1.00 40.57 ? 45   THR B C   1 
ATOM   3542 O  O   . THR B 1 56  ? 68.327  76.228  114.901 1.00 40.57 ? 45   THR B O   1 
ATOM   3543 C  CB  . THR B 1 56  ? 66.092  76.846  116.918 1.00 40.57 ? 45   THR B CB  1 
ATOM   3544 O  OG1 . THR B 1 56  ? 67.369  77.387  117.274 1.00 40.57 ? 45   THR B OG1 1 
ATOM   3545 C  CG2 . THR B 1 56  ? 65.349  76.442  118.179 1.00 40.57 ? 45   THR B CG2 1 
ATOM   3546 N  N   . VAL B 1 57  ? 66.468  76.127  113.631 1.00 33.95 ? 46   VAL B N   1 
ATOM   3547 C  CA  . VAL B 1 57  ? 67.121  76.517  112.389 1.00 33.95 ? 46   VAL B CA  1 
ATOM   3548 C  C   . VAL B 1 57  ? 66.849  77.991  112.145 1.00 33.95 ? 46   VAL B C   1 
ATOM   3549 O  O   . VAL B 1 57  ? 65.715  78.459  112.296 1.00 33.95 ? 46   VAL B O   1 
ATOM   3550 C  CB  . VAL B 1 57  ? 66.632  75.660  111.207 1.00 33.95 ? 46   VAL B CB  1 
ATOM   3551 C  CG1 . VAL B 1 57  ? 67.396  76.012  109.944 1.00 33.95 ? 46   VAL B CG1 1 
ATOM   3552 C  CG2 . VAL B 1 57  ? 66.783  74.185  111.525 1.00 33.95 ? 46   VAL B CG2 1 
ATOM   3553 N  N   . ARG B 1 58  ? 67.892  78.729  111.774 1.00 33.20 ? 47   ARG B N   1 
ATOM   3554 C  CA  . ARG B 1 58  ? 67.798  80.159  111.534 1.00 33.20 ? 47   ARG B CA  1 
ATOM   3555 C  C   . ARG B 1 58  ? 68.427  80.488  110.192 1.00 33.20 ? 47   ARG B C   1 
ATOM   3556 O  O   . ARG B 1 58  ? 69.392  79.848  109.771 1.00 33.20 ? 47   ARG B O   1 
ATOM   3557 C  CB  . ARG B 1 58  ? 68.502  80.964  112.624 1.00 33.20 ? 47   ARG B CB  1 
ATOM   3558 C  CG  . ARG B 1 58  ? 68.284  80.434  114.027 1.00 33.20 ? 47   ARG B CG  1 
ATOM   3559 C  CD  . ARG B 1 58  ? 69.062  81.227  115.068 1.00 33.20 ? 47   ARG B CD  1 
ATOM   3560 N  NE  . ARG B 1 58  ? 70.429  81.532  114.651 1.00 33.20 ? 47   ARG B NE  1 
ATOM   3561 C  CZ  . ARG B 1 58  ? 70.796  82.629  113.993 1.00 33.20 ? 47   ARG B CZ  1 
ATOM   3562 N  NH1 . ARG B 1 58  ? 69.901  83.549  113.657 1.00 33.20 ? 47   ARG B NH1 1 
ATOM   3563 N  NH2 . ARG B 1 58  ? 72.067  82.806  113.664 1.00 33.20 ? 47   ARG B NH2 1 
ATOM   3564 N  N   . THR B 1 59  ? 67.877  81.496  109.528 1.00 27.11 ? 48   THR B N   1 
ATOM   3565 C  CA  . THR B 1 59  ? 68.396  81.978  108.259 1.00 27.11 ? 48   THR B CA  1 
ATOM   3566 C  C   . THR B 1 59  ? 68.929  83.392  108.427 1.00 27.11 ? 48   THR B C   1 
ATOM   3567 O  O   . THR B 1 59  ? 68.299  84.230  109.079 1.00 27.11 ? 48   THR B O   1 
ATOM   3568 C  CB  . THR B 1 59  ? 67.318  81.960  107.174 1.00 27.11 ? 48   THR B CB  1 
ATOM   3569 O  OG1 . THR B 1 59  ? 66.082  82.438  107.716 1.00 27.11 ? 48   THR B OG1 1 
ATOM   3570 C  CG2 . THR B 1 59  ? 67.121  80.557  106.636 1.00 27.11 ? 48   THR B CG2 1 
ATOM   3571 N  N   . VAL B 1 60  ? 70.096  83.648  107.846 1.00 24.47 ? 49   VAL B N   1 
ATOM   3572 C  CA  . VAL B 1 60  ? 70.691  84.977  107.798 1.00 24.47 ? 49   VAL B CA  1 
ATOM   3573 C  C   . VAL B 1 60  ? 70.916  85.326  106.336 1.00 24.47 ? 49   VAL B C   1 
ATOM   3574 O  O   . VAL B 1 60  ? 71.479  84.525  105.583 1.00 24.47 ? 49   VAL B O   1 
ATOM   3575 C  CB  . VAL B 1 60  ? 72.002  85.044  108.598 1.00 24.47 ? 49   VAL B CB  1 
ATOM   3576 C  CG1 . VAL B 1 60  ? 71.734  84.723  110.053 1.00 24.47 ? 49   VAL B CG1 1 
ATOM   3577 C  CG2 . VAL B 1 60  ? 73.025  84.088  108.030 1.00 24.47 ? 49   VAL B CG2 1 
ATOM   3578 N  N   . LEU B 1 61  ? 70.472  86.513  105.937 1.00 23.24 ? 50   LEU B N   1 
ATOM   3579 C  CA  . LEU B 1 61  ? 70.320  86.859  104.533 1.00 23.24 ? 50   LEU B CA  1 
ATOM   3580 C  C   . LEU B 1 61  ? 71.454  87.752  104.055 1.00 23.24 ? 50   LEU B C   1 
ATOM   3581 O  O   . LEU B 1 61  ? 71.840  88.705  104.734 1.00 23.24 ? 50   LEU B O   1 
ATOM   3582 C  CB  . LEU B 1 61  ? 68.986  87.567  104.302 1.00 23.24 ? 50   LEU B CB  1 
ATOM   3583 C  CG  . LEU B 1 61  ? 67.749  86.824  104.796 1.00 23.24 ? 50   LEU B CG  1 
ATOM   3584 C  CD1 . LEU B 1 61  ? 66.523  87.682  104.601 1.00 23.24 ? 50   LEU B CD1 1 
ATOM   3585 C  CD2 . LEU B 1 61  ? 67.595  85.505  104.083 1.00 23.24 ? 50   LEU B CD2 1 
ATOM   3586 N  N   . GLY B 1 62  ? 71.977  87.433  102.883 1.00 21.05 ? 51   GLY B N   1 
ATOM   3587 C  CA  . GLY B 1 62  ? 72.916  88.304  102.202 1.00 21.05 ? 51   GLY B CA  1 
ATOM   3588 C  C   . GLY B 1 62  ? 72.534  88.406  100.744 1.00 21.05 ? 51   GLY B C   1 
ATOM   3589 O  O   . GLY B 1 62  ? 71.978  87.475  100.163 1.00 21.05 ? 51   GLY B O   1 
ATOM   3590 N  N   . SER B 1 63  ? 72.826  89.556  100.155 1.00 23.44 ? 52   SER B N   1 
ATOM   3591 C  CA  . SER B 1 63  ? 72.378  89.857  98.805  1.00 23.44 ? 52   SER B CA  1 
ATOM   3592 C  C   . SER B 1 63  ? 73.482  89.559  97.804  1.00 23.44 ? 52   SER B C   1 
ATOM   3593 O  O   . SER B 1 63  ? 74.661  89.802  98.068  1.00 23.44 ? 52   SER B O   1 
ATOM   3594 C  CB  . SER B 1 63  ? 71.944  91.316  98.690  1.00 23.44 ? 52   SER B CB  1 
ATOM   3595 O  OG  . SER B 1 63  ? 71.498  91.606  97.381  1.00 23.44 ? 52   SER B OG  1 
ATOM   3596 N  N   . SER B 1 64  ? 73.084  89.033  96.648  1.00 23.04 ? 53   SER B N   1 
ATOM   3597 C  CA  . SER B 1 64  ? 74.005  88.558  95.627  1.00 23.04 ? 53   SER B CA  1 
ATOM   3598 C  C   . SER B 1 64  ? 74.106  89.505  94.443  1.00 23.04 ? 53   SER B C   1 
ATOM   3599 O  O   . SER B 1 64  ? 74.569  89.099  93.375  1.00 23.04 ? 53   SER B O   1 
ATOM   3600 C  CB  . SER B 1 64  ? 73.569  87.180  95.143  1.00 23.04 ? 53   SER B CB  1 
ATOM   3601 O  OG  . SER B 1 64  ? 74.422  86.718  94.119  1.00 23.04 ? 53   SER B OG  1 
ATOM   3602 N  N   . GLU B 1 65  ? 73.689  90.755  94.607  1.00 27.01 ? 54   GLU B N   1 
ATOM   3603 C  CA  . GLU B 1 65  ? 73.578  91.685  93.496  1.00 27.01 ? 54   GLU B CA  1 
ATOM   3604 C  C   . GLU B 1 65  ? 74.279  92.993  93.824  1.00 27.01 ? 54   GLU B C   1 
ATOM   3605 O  O   . GLU B 1 65  ? 74.466  93.352  94.988  1.00 27.01 ? 54   GLU B O   1 
ATOM   3606 C  CB  . GLU B 1 65  ? 72.115  91.954  93.143  1.00 27.01 ? 54   GLU B CB  1 
ATOM   3607 C  CG  . GLU B 1 65  ? 71.220  92.179  94.336  1.00 27.01 ? 54   GLU B CG  1 
ATOM   3608 C  CD  . GLU B 1 65  ? 69.763  92.021  93.991  1.00 27.01 ? 54   GLU B CD  1 
ATOM   3609 O  OE1 . GLU B 1 65  ? 69.446  91.138  93.171  1.00 27.01 ? 54   GLU B OE1 1 
ATOM   3610 O  OE2 . GLU B 1 65  ? 68.934  92.778  94.536  1.00 27.01 ? 54   GLU B OE2 1 
ATOM   3611 N  N   . ASN B 1 66  ? 74.667  93.699  92.767  1.00 28.89 ? 55   ASN B N   1 
ATOM   3612 C  CA  . ASN B 1 66  ? 75.373  94.963  92.881  1.00 28.89 ? 55   ASN B CA  1 
ATOM   3613 C  C   . ASN B 1 66  ? 74.363  96.107  92.953  1.00 28.89 ? 55   ASN B C   1 
ATOM   3614 O  O   . ASN B 1 66  ? 73.158  95.895  93.104  1.00 28.89 ? 55   ASN B O   1 
ATOM   3615 C  CB  . ASN B 1 66  ? 76.348  95.122  91.718  1.00 28.89 ? 55   ASN B CB  1 
ATOM   3616 C  CG  . ASN B 1 66  ? 75.667  95.054  90.373  1.00 28.89 ? 55   ASN B CG  1 
ATOM   3617 O  OD1 . ASN B 1 66  ? 74.465  95.268  90.267  1.00 28.89 ? 55   ASN B OD1 1 
ATOM   3618 N  ND2 . ASN B 1 66  ? 76.433  94.750  89.336  1.00 28.89 ? 55   ASN B ND2 1 
ATOM   3619 N  N   . ALA B 1 67  ? 74.851  97.343  92.845  1.00 31.75 ? 56   ALA B N   1 
ATOM   3620 C  CA  . ALA B 1 67  ? 73.981  98.504  92.981  1.00 31.75 ? 56   ALA B CA  1 
ATOM   3621 C  C   . ALA B 1 67  ? 72.993  98.633  91.832  1.00 31.75 ? 56   ALA B C   1 
ATOM   3622 O  O   . ALA B 1 67  ? 72.010  99.368  91.961  1.00 31.75 ? 56   ALA B O   1 
ATOM   3623 C  CB  . ALA B 1 67  ? 74.821  99.775  93.083  1.00 31.75 ? 56   ALA B CB  1 
ATOM   3624 N  N   . LEU B 1 68  ? 73.230  97.950  90.713  1.00 32.55 ? 57   LEU B N   1 
ATOM   3625 C  CA  . LEU B 1 68  ? 72.302  97.992  89.591  1.00 32.55 ? 57   LEU B CA  1 
ATOM   3626 C  C   . LEU B 1 68  ? 71.138  97.025  89.747  1.00 32.55 ? 57   LEU B C   1 
ATOM   3627 O  O   . LEU B 1 68  ? 70.199  97.082  88.947  1.00 32.55 ? 57   LEU B O   1 
ATOM   3628 C  CB  . LEU B 1 68  ? 73.037  97.684  88.287  1.00 32.55 ? 57   LEU B CB  1 
ATOM   3629 C  CG  . LEU B 1 68  ? 73.839  98.836  87.688  1.00 32.55 ? 57   LEU B CG  1 
ATOM   3630 C  CD1 . LEU B 1 68  ? 75.086  99.107  88.506  1.00 32.55 ? 57   LEU B CD1 1 
ATOM   3631 C  CD2 . LEU B 1 68  ? 74.198  98.529  86.249  1.00 32.55 ? 57   LEU B CD2 1 
ATOM   3632 N  N   . GLY B 1 69  ? 71.175  96.144  90.741  1.00 30.40 ? 58   GLY B N   1 
ATOM   3633 C  CA  . GLY B 1 69  ? 70.087  95.224  90.983  1.00 30.40 ? 58   GLY B CA  1 
ATOM   3634 C  C   . GLY B 1 69  ? 70.182  93.902  90.262  1.00 30.40 ? 58   GLY B C   1 
ATOM   3635 O  O   . GLY B 1 69  ? 69.183  93.177  90.208  1.00 30.40 ? 58   GLY B O   1 
ATOM   3636 N  N   . VAL B 1 70  ? 71.341  93.560  89.705  1.00 29.63 ? 59   VAL B N   1 
ATOM   3637 C  CA  . VAL B 1 70  ? 71.516  92.330  88.950  1.00 29.63 ? 59   VAL B CA  1 
ATOM   3638 C  C   . VAL B 1 70  ? 72.588  91.481  89.624  1.00 29.63 ? 59   VAL B C   1 
ATOM   3639 O  O   . VAL B 1 70  ? 73.308  91.935  90.509  1.00 29.63 ? 59   VAL B O   1 
ATOM   3640 C  CB  . VAL B 1 70  ? 71.884  92.601  87.481  1.00 29.63 ? 59   VAL B CB  1 
ATOM   3641 C  CG1 . VAL B 1 70  ? 70.917  93.581  86.871  1.00 29.63 ? 59   VAL B CG1 1 
ATOM   3642 C  CG2 . VAL B 1 70  ? 73.295  93.121  87.377  1.00 29.63 ? 59   VAL B CG2 1 
ATOM   3643 N  N   . CYS B 1 71  ? 72.677  90.226  89.183  1.00 31.57 ? 60   CYS B N   1 
ATOM   3644 C  CA  . CYS B 1 71  ? 73.756  89.343  89.603  1.00 31.57 ? 60   CYS B CA  1 
ATOM   3645 C  C   . CYS B 1 71  ? 75.098  90.049  89.502  1.00 31.57 ? 60   CYS B C   1 
ATOM   3646 O  O   . CYS B 1 71  ? 75.294  90.938  88.670  1.00 31.57 ? 60   CYS B O   1 
ATOM   3647 C  CB  . CYS B 1 71  ? 73.806  88.100  88.715  1.00 31.57 ? 60   CYS B CB  1 
ATOM   3648 S  SG  . CYS B 1 71  ? 72.667  86.773  89.089  1.00 31.57 ? 60   CYS B SG  1 
ATOM   3649 N  N   . SER B 1 72  ? 76.040  89.632  90.338  1.00 24.78 ? 61   SER B N   1 
ATOM   3650 C  CA  . SER B 1 72  ? 77.413  90.073  90.171  1.00 24.78 ? 61   SER B CA  1 
ATOM   3651 C  C   . SER B 1 72  ? 78.324  89.077  90.862  1.00 24.78 ? 61   SER B C   1 
ATOM   3652 O  O   . SER B 1 72  ? 78.019  88.608  91.959  1.00 24.78 ? 61   SER B O   1 
ATOM   3653 C  CB  . SER B 1 72  ? 77.639  91.474  90.742  1.00 24.78 ? 61   SER B CB  1 
ATOM   3654 O  OG  . SER B 1 72  ? 77.913  91.416  92.128  1.00 24.78 ? 61   SER B OG  1 
ATOM   3655 N  N   . ASP B 1 73  ? 79.439  88.766  90.215  1.00 22.31 ? 62   ASP B N   1 
ATOM   3656 C  CA  . ASP B 1 73  ? 80.452  87.913  90.814  1.00 22.31 ? 62   ASP B CA  1 
ATOM   3657 C  C   . ASP B 1 73  ? 81.383  88.680  91.735  1.00 22.31 ? 62   ASP B C   1 
ATOM   3658 O  O   . ASP B 1 73  ? 82.282  88.072  92.323  1.00 22.31 ? 62   ASP B O   1 
ATOM   3659 C  CB  . ASP B 1 73  ? 81.263  87.217  89.723  1.00 22.31 ? 62   ASP B CB  1 
ATOM   3660 C  CG  . ASP B 1 73  ? 81.814  88.179  88.706  1.00 22.31 ? 62   ASP B CG  1 
ATOM   3661 O  OD1 . ASP B 1 73  ? 81.494  89.379  88.797  1.00 22.31 ? 62   ASP B OD1 1 
ATOM   3662 O  OD2 . ASP B 1 73  ? 82.562  87.737  87.811  1.00 22.31 ? 62   ASP B OD2 1 
ATOM   3663 N  N   . THR B 1 74  ? 81.194  89.991  91.870  1.00 21.65 ? 63   THR B N   1 
ATOM   3664 C  CA  . THR B 1 74  ? 81.997  90.815  92.758  1.00 21.65 ? 63   THR B CA  1 
ATOM   3665 C  C   . THR B 1 74  ? 81.283  91.164  94.056  1.00 21.65 ? 63   THR B C   1 
ATOM   3666 O  O   . THR B 1 74  ? 81.941  91.608  95.000  1.00 21.65 ? 63   THR B O   1 
ATOM   3667 C  CB  . THR B 1 74  ? 82.405  92.110  92.051  1.00 21.65 ? 63   THR B CB  1 
ATOM   3668 O  OG1 . THR B 1 74  ? 81.317  93.038  92.087  1.00 21.65 ? 63   THR B OG1 1 
ATOM   3669 C  CG2 . THR B 1 74  ? 82.771  91.838  90.606  1.00 21.65 ? 63   THR B CG2 1 
ATOM   3670 N  N   . ALA B 1 75  ? 79.964  90.979  94.128  1.00 21.24 ? 64   ALA B N   1 
ATOM   3671 C  CA  . ALA B 1 75  ? 79.203  91.275  95.335  1.00 21.24 ? 64   ALA B CA  1 
ATOM   3672 C  C   . ALA B 1 75  ? 78.814  90.033  96.116  1.00 21.24 ? 64   ALA B C   1 
ATOM   3673 O  O   . ALA B 1 75  ? 78.763  90.078  97.350  1.00 21.24 ? 64   ALA B O   1 
ATOM   3674 C  CB  . ALA B 1 75  ? 77.934  92.052  94.985  1.00 21.24 ? 64   ALA B CB  1 
ATOM   3675 N  N   . ALA B 1 76  ? 78.527  88.932  95.428  1.00 20.65 ? 65   ALA B N   1 
ATOM   3676 C  CA  . ALA B 1 76  ? 78.226  87.690  96.128  1.00 20.65 ? 65   ALA B CA  1 
ATOM   3677 C  C   . ALA B 1 76  ? 79.382  87.207  96.990  1.00 20.65 ? 65   ALA B C   1 
ATOM   3678 O  O   . ALA B 1 76  ? 79.125  86.778  98.128  1.00 20.65 ? 65   ALA B O   1 
ATOM   3679 C  CB  . ALA B 1 76  ? 77.820  86.615  95.117  1.00 20.65 ? 65   ALA B CB  1 
ATOM   3680 N  N   . PRO B 1 77  ? 80.637  87.206  96.529  1.00 19.35 ? 66   PRO B N   1 
ATOM   3681 C  CA  . PRO B 1 77  ? 81.733  86.813  97.428  1.00 19.35 ? 66   PRO B CA  1 
ATOM   3682 C  C   . PRO B 1 77  ? 81.852  87.708  98.645  1.00 19.35 ? 66   PRO B C   1 
ATOM   3683 O  O   . PRO B 1 77  ? 82.142  87.221  99.743  1.00 19.35 ? 66   PRO B O   1 
ATOM   3684 C  CB  . PRO B 1 77  ? 82.970  86.910  96.527  1.00 19.35 ? 66   PRO B CB  1 
ATOM   3685 C  CG  . PRO B 1 77  ? 82.449  86.876  95.153  1.00 19.35 ? 66   PRO B CG  1 
ATOM   3686 C  CD  . PRO B 1 77  ? 81.134  87.545  95.190  1.00 19.35 ? 66   PRO B CD  1 
ATOM   3687 N  N   . LEU B 1 78  ? 81.624  89.012  98.483  1.00 20.16 ? 67   LEU B N   1 
ATOM   3688 C  CA  . LEU B 1 78  ? 81.684  89.917  99.624  1.00 20.16 ? 67   LEU B CA  1 
ATOM   3689 C  C   . LEU B 1 78  ? 80.588  89.602  100.631 1.00 20.16 ? 67   LEU B C   1 
ATOM   3690 O  O   . LEU B 1 78  ? 80.836  89.570  101.843 1.00 20.16 ? 67   LEU B O   1 
ATOM   3691 C  CB  . LEU B 1 78  ? 81.572  91.361  99.145  1.00 20.16 ? 67   LEU B CB  1 
ATOM   3692 C  CG  . LEU B 1 78  ? 82.732  91.899  98.308  1.00 20.16 ? 67   LEU B CG  1 
ATOM   3693 C  CD1 . LEU B 1 78  ? 82.371  93.241  97.726  1.00 20.16 ? 67   LEU B CD1 1 
ATOM   3694 C  CD2 . LEU B 1 78  ? 83.982  92.021  99.139  1.00 20.16 ? 67   LEU B CD2 1 
ATOM   3695 N  N   . ALA B 1 79  ? 79.368  89.355  100.147 1.00 19.73 ? 68   ALA B N   1 
ATOM   3696 C  CA  . ALA B 1 79  ? 78.279  88.995  101.049 1.00 19.73 ? 68   ALA B CA  1 
ATOM   3697 C  C   . ALA B 1 79  ? 78.565  87.681  101.761 1.00 19.73 ? 68   ALA B C   1 
ATOM   3698 O  O   . ALA B 1 79  ? 78.299  87.544  102.961 1.00 19.73 ? 68   ALA B O   1 
ATOM   3699 C  CB  . ALA B 1 79  ? 76.967  88.905  100.277 1.00 19.73 ? 68   ALA B CB  1 
ATOM   3700 N  N   . ALA B 1 80  ? 79.106  86.700  101.036 1.00 19.01 ? 69   ALA B N   1 
ATOM   3701 C  CA  . ALA B 1 80  ? 79.422  85.415  101.647 1.00 19.01 ? 69   ALA B CA  1 
ATOM   3702 C  C   . ALA B 1 80  ? 80.482  85.561  102.728 1.00 19.01 ? 69   ALA B C   1 
ATOM   3703 O  O   . ALA B 1 80  ? 80.367  84.964  103.802 1.00 19.01 ? 69   ALA B O   1 
ATOM   3704 C  CB  . ALA B 1 80  ? 79.888  84.431  100.580 1.00 19.01 ? 69   ALA B CB  1 
ATOM   3705 N  N   . VAL B 1 81  ? 81.528  86.346  102.462 1.00 19.90 ? 70   VAL B N   1 
ATOM   3706 C  CA  . VAL B 1 81  ? 82.580  86.538  103.456 1.00 19.90 ? 70   VAL B CA  1 
ATOM   3707 C  C   . VAL B 1 81  ? 82.022  87.240  104.686 1.00 19.90 ? 70   VAL B C   1 
ATOM   3708 O  O   . VAL B 1 81  ? 82.334  86.871  105.827 1.00 19.90 ? 70   VAL B O   1 
ATOM   3709 C  CB  . VAL B 1 81  ? 83.759  87.317  102.846 1.00 19.90 ? 70   VAL B CB  1 
ATOM   3710 C  CG1 . VAL B 1 81  ? 84.755  87.690  103.920 1.00 19.90 ? 70   VAL B CG1 1 
ATOM   3711 C  CG2 . VAL B 1 81  ? 84.432  86.499  101.768 1.00 19.90 ? 70   VAL B CG2 1 
ATOM   3712 N  N   . ASP B 1 82  ? 81.192  88.263  104.478 1.00 22.36 ? 71   ASP B N   1 
ATOM   3713 C  CA  . ASP B 1 82  ? 80.598  88.963  105.610 1.00 22.36 ? 71   ASP B CA  1 
ATOM   3714 C  C   . ASP B 1 82  ? 79.745  88.026  106.451 1.00 22.36 ? 71   ASP B C   1 
ATOM   3715 O  O   . ASP B 1 82  ? 79.823  88.042  107.685 1.00 22.36 ? 71   ASP B O   1 
ATOM   3716 C  CB  . ASP B 1 82  ? 79.762  90.136  105.111 1.00 22.36 ? 71   ASP B CB  1 
ATOM   3717 C  CG  . ASP B 1 82  ? 80.569  91.400  104.960 1.00 22.36 ? 71   ASP B CG  1 
ATOM   3718 O  OD1 . ASP B 1 82  ? 79.958  92.482  104.852 1.00 22.36 ? 71   ASP B OD1 1 
ATOM   3719 O  OD2 . ASP B 1 82  ? 81.815  91.315  104.947 1.00 22.36 ? 71   ASP B OD2 1 
ATOM   3720 N  N   . LEU B 1 83  ? 78.917  87.205  105.802 1.00 21.60 ? 72   LEU B N   1 
ATOM   3721 C  CA  . LEU B 1 83  ? 78.085  86.260  106.538 1.00 21.60 ? 72   LEU B CA  1 
ATOM   3722 C  C   . LEU B 1 83  ? 78.941  85.274  107.317 1.00 21.60 ? 72   LEU B C   1 
ATOM   3723 O  O   . LEU B 1 83  ? 78.689  85.010  108.498 1.00 21.60 ? 72   LEU B O   1 
ATOM   3724 C  CB  . LEU B 1 83  ? 77.166  85.515  105.574 1.00 21.60 ? 72   LEU B CB  1 
ATOM   3725 C  CG  . LEU B 1 83  ? 75.984  86.296  105.012 1.00 21.60 ? 72   LEU B CG  1 
ATOM   3726 C  CD1 . LEU B 1 83  ? 75.369  85.533  103.865 1.00 21.60 ? 72   LEU B CD1 1 
ATOM   3727 C  CD2 . LEU B 1 83  ? 74.967  86.564  106.095 1.00 21.60 ? 72   LEU B CD2 1 
ATOM   3728 N  N   . LYS B 1 84  ? 79.967  84.720  106.670 1.00 22.48 ? 73   LYS B N   1 
ATOM   3729 C  CA  . LYS B 1 84  ? 80.834  83.756  107.335 1.00 22.48 ? 73   LYS B CA  1 
ATOM   3730 C  C   . LYS B 1 84  ? 81.467  84.358  108.580 1.00 22.48 ? 73   LYS B C   1 
ATOM   3731 O  O   . LYS B 1 84  ? 81.481  83.734  109.646 1.00 22.48 ? 73   LYS B O   1 
ATOM   3732 C  CB  . LYS B 1 84  ? 81.912  83.277  106.366 1.00 22.48 ? 73   LYS B CB  1 
ATOM   3733 C  CG  . LYS B 1 84  ? 82.913  82.309  106.967 1.00 22.48 ? 73   LYS B CG  1 
ATOM   3734 C  CD  . LYS B 1 84  ? 82.277  80.976  107.287 1.00 22.48 ? 73   LYS B CD  1 
ATOM   3735 C  CE  . LYS B 1 84  ? 83.328  79.908  107.465 1.00 22.48 ? 73   LYS B CE  1 
ATOM   3736 N  NZ  . LYS B 1 84  ? 84.288  80.263  108.535 1.00 22.48 ? 73   LYS B NZ  1 
ATOM   3737 N  N   . TRP B 1 85  ? 82.007  85.571  108.465 1.00 23.35 ? 74   TRP B N   1 
ATOM   3738 C  CA  . TRP B 1 85  ? 82.672  86.179  109.611 1.00 23.35 ? 74   TRP B CA  1 
ATOM   3739 C  C   . TRP B 1 85  ? 81.680  86.506  110.719 1.00 23.35 ? 74   TRP B C   1 
ATOM   3740 O  O   . TRP B 1 85  ? 81.938  86.229  111.895 1.00 23.35 ? 74   TRP B O   1 
ATOM   3741 C  CB  . TRP B 1 85  ? 83.417  87.438  109.181 1.00 23.35 ? 74   TRP B CB  1 
ATOM   3742 C  CG  . TRP B 1 85  ? 84.710  87.181  108.475 1.00 23.35 ? 74   TRP B CG  1 
ATOM   3743 C  CD1 . TRP B 1 85  ? 85.369  85.991  108.363 1.00 23.35 ? 74   TRP B CD1 1 
ATOM   3744 C  CD2 . TRP B 1 85  ? 85.507  88.145  107.787 1.00 23.35 ? 74   TRP B CD2 1 
ATOM   3745 N  NE1 . TRP B 1 85  ? 86.526  86.157  107.644 1.00 23.35 ? 74   TRP B NE1 1 
ATOM   3746 C  CE2 . TRP B 1 85  ? 86.632  87.472  107.279 1.00 23.35 ? 74   TRP B CE2 1 
ATOM   3747 C  CE3 . TRP B 1 85  ? 85.377  89.516  107.548 1.00 23.35 ? 74   TRP B CE3 1 
ATOM   3748 C  CZ2 . TRP B 1 85  ? 87.617  88.120  106.549 1.00 23.35 ? 74   TRP B CZ2 1 
ATOM   3749 C  CZ3 . TRP B 1 85  ? 86.354  90.155  106.825 1.00 23.35 ? 74   TRP B CZ3 1 
ATOM   3750 C  CH2 . TRP B 1 85  ? 87.460  89.459  106.332 1.00 23.35 ? 74   TRP B CH2 1 
ATOM   3751 N  N   . GLU B 1 86  ? 80.537  87.099  110.369 1.00 24.65 ? 75   GLU B N   1 
ATOM   3752 C  CA  . GLU B 1 86  ? 79.637  87.608  111.397 1.00 24.65 ? 75   GLU B CA  1 
ATOM   3753 C  C   . GLU B 1 86  ? 78.875  86.493  112.105 1.00 24.65 ? 75   GLU B C   1 
ATOM   3754 O  O   . GLU B 1 86  ? 78.745  86.520  113.333 1.00 24.65 ? 75   GLU B O   1 
ATOM   3755 C  CB  . GLU B 1 86  ? 78.658  88.606  110.784 1.00 24.65 ? 75   GLU B CB  1 
ATOM   3756 N  N   . HIS B 1 87  ? 78.368  85.505  111.362 1.00 26.01 ? 76   HIS B N   1 
ATOM   3757 C  CA  . HIS B 1 87  ? 77.437  84.534  111.923 1.00 26.01 ? 76   HIS B CA  1 
ATOM   3758 C  C   . HIS B 1 87  ? 77.978  83.116  112.007 1.00 26.01 ? 76   HIS B C   1 
ATOM   3759 O  O   . HIS B 1 87  ? 77.480  82.336  112.823 1.00 26.01 ? 76   HIS B O   1 
ATOM   3760 C  CB  . HIS B 1 87  ? 76.142  84.512  111.102 1.00 26.01 ? 76   HIS B CB  1 
ATOM   3761 C  CG  . HIS B 1 87  ? 75.476  85.846  110.996 1.00 26.01 ? 76   HIS B CG  1 
ATOM   3762 N  ND1 . HIS B 1 87  ? 74.699  86.372  112.005 1.00 26.01 ? 76   HIS B ND1 1 
ATOM   3763 C  CD2 . HIS B 1 87  ? 75.472  86.763  110.002 1.00 26.01 ? 76   HIS B CD2 1 
ATOM   3764 C  CE1 . HIS B 1 87  ? 74.245  87.555  111.636 1.00 26.01 ? 76   HIS B CE1 1 
ATOM   3765 N  NE2 . HIS B 1 87  ? 74.699  87.816  110.424 1.00 26.01 ? 76   HIS B NE2 1 
ATOM   3766 N  N   . ASN B 1 88  ? 78.966  82.758  111.197 1.00 27.13 ? 77   ASN B N   1 
ATOM   3767 C  CA  . ASN B 1 88  ? 79.535  81.419  111.251 1.00 27.13 ? 77   ASN B CA  1 
ATOM   3768 C  C   . ASN B 1 88  ? 78.467  80.384  110.917 1.00 27.13 ? 77   ASN B C   1 
ATOM   3769 O  O   . ASN B 1 88  ? 78.064  79.600  111.785 1.00 27.13 ? 77   ASN B O   1 
ATOM   3770 C  CB  . ASN B 1 88  ? 80.135  81.159  112.633 1.00 27.13 ? 77   ASN B CB  1 
ATOM   3771 C  CG  . ASN B 1 88  ? 81.160  80.047  112.624 1.00 27.13 ? 77   ASN B CG  1 
ATOM   3772 O  OD1 . ASN B 1 88  ? 81.916  79.892  111.666 1.00 27.13 ? 77   ASN B OD1 1 
ATOM   3773 N  ND2 . ASN B 1 88  ? 81.195  79.268  113.697 1.00 27.13 ? 77   ASN B ND2 1 
ATOM   3774 N  N   . PRO B 1 89  ? 77.984  80.351  109.679 1.00 24.11 ? 78   PRO B N   1 
ATOM   3775 C  CA  . PRO B 1 89  ? 76.917  79.414  109.324 1.00 24.11 ? 78   PRO B CA  1 
ATOM   3776 C  C   . PRO B 1 89  ? 77.419  77.983  109.232 1.00 24.11 ? 78   PRO B C   1 
ATOM   3777 O  O   . PRO B 1 89  ? 78.616  77.715  109.125 1.00 24.11 ? 78   PRO B O   1 
ATOM   3778 C  CB  . PRO B 1 89  ? 76.449  79.921  107.960 1.00 24.11 ? 78   PRO B CB  1 
ATOM   3779 C  CG  . PRO B 1 89  ? 77.637  80.573  107.386 1.00 24.11 ? 78   PRO B CG  1 
ATOM   3780 C  CD  . PRO B 1 89  ? 78.405  81.161  108.527 1.00 24.11 ? 78   PRO B CD  1 
ATOM   3781 N  N   . ALA B 1 90  ? 76.469  77.052  109.278 1.00 25.09 ? 79   ALA B N   1 
ATOM   3782 C  CA  . ALA B 1 90  ? 76.769  75.640  109.086 1.00 25.09 ? 79   ALA B CA  1 
ATOM   3783 C  C   . ALA B 1 90  ? 76.631  75.211  107.634 1.00 25.09 ? 79   ALA B C   1 
ATOM   3784 O  O   . ALA B 1 90  ? 77.292  74.257  107.211 1.00 25.09 ? 79   ALA B O   1 
ATOM   3785 C  CB  . ALA B 1 90  ? 75.847  74.783  109.953 1.00 25.09 ? 79   ALA B CB  1 
ATOM   3786 N  N   . VAL B 1 91  ? 75.786  75.894  106.866 1.00 23.07 ? 80   VAL B N   1 
ATOM   3787 C  CA  . VAL B 1 91  ? 75.551  75.572  105.466 1.00 23.07 ? 80   VAL B CA  1 
ATOM   3788 C  C   . VAL B 1 91  ? 75.223  76.864  104.741 1.00 23.07 ? 80   VAL B C   1 
ATOM   3789 O  O   . VAL B 1 91  ? 74.699  77.809  105.332 1.00 23.07 ? 80   VAL B O   1 
ATOM   3790 C  CB  . VAL B 1 91  ? 74.413  74.537  105.307 1.00 23.07 ? 80   VAL B CB  1 
ATOM   3791 C  CG1 . VAL B 1 91  ? 73.099  75.111  105.782 1.00 23.07 ? 80   VAL B CG1 1 
ATOM   3792 C  CG2 . VAL B 1 91  ? 74.290  74.097  103.866 1.00 23.07 ? 80   VAL B CG2 1 
ATOM   3793 N  N   . PHE B 1 92  ? 75.549  76.910  103.455 1.00 20.69 ? 81   PHE B N   1 
ATOM   3794 C  CA  . PHE B 1 92  ? 75.212  78.040  102.601 1.00 20.69 ? 81   PHE B CA  1 
ATOM   3795 C  C   . PHE B 1 92  ? 74.106  77.620  101.649 1.00 20.69 ? 81   PHE B C   1 
ATOM   3796 O  O   . PHE B 1 92  ? 74.246  76.625  100.934 1.00 20.69 ? 81   PHE B O   1 
ATOM   3797 C  CB  . PHE B 1 92  ? 76.426  78.529  101.814 1.00 20.69 ? 81   PHE B CB  1 
ATOM   3798 C  CG  . PHE B 1 92  ? 77.270  79.521  102.556 1.00 20.69 ? 81   PHE B CG  1 
ATOM   3799 C  CD1 . PHE B 1 92  ? 78.150  79.108  103.534 1.00 20.69 ? 81   PHE B CD1 1 
ATOM   3800 C  CD2 . PHE B 1 92  ? 77.178  80.869  102.277 1.00 20.69 ? 81   PHE B CD2 1 
ATOM   3801 C  CE1 . PHE B 1 92  ? 78.922  80.019  104.215 1.00 20.69 ? 81   PHE B CE1 1 
ATOM   3802 C  CE2 . PHE B 1 92  ? 77.947  81.777  102.958 1.00 20.69 ? 81   PHE B CE2 1 
ATOM   3803 C  CZ  . PHE B 1 92  ? 78.820  81.350  103.929 1.00 20.69 ? 81   PHE B CZ  1 
ATOM   3804 N  N   . LEU B 1 93  ? 73.009  78.370  101.646 1.00 21.69 ? 82   LEU B N   1 
ATOM   3805 C  CA  . LEU B 1 93  ? 71.985  78.227  100.615 1.00 21.69 ? 82   LEU B CA  1 
ATOM   3806 C  C   . LEU B 1 93  ? 72.382  79.093  99.420  1.00 21.69 ? 82   LEU B C   1 
ATOM   3807 O  O   . LEU B 1 93  ? 71.714  80.046  99.033  1.00 21.69 ? 82   LEU B O   1 
ATOM   3808 C  CB  . LEU B 1 93  ? 70.620  78.608  101.172 1.00 21.69 ? 82   LEU B CB  1 
ATOM   3809 C  CG  . LEU B 1 93  ? 69.395  77.970  100.523 1.00 21.69 ? 82   LEU B CG  1 
ATOM   3810 C  CD1 . LEU B 1 93  ? 69.372  76.479  100.786 1.00 21.69 ? 82   LEU B CD1 1 
ATOM   3811 C  CD2 . LEU B 1 93  ? 68.130  78.614  101.039 1.00 21.69 ? 82   LEU B CD2 1 
ATOM   3812 N  N   . GLY B 1 94  ? 73.516  78.714  98.837  1.00 21.30 ? 83   GLY B N   1 
ATOM   3813 C  CA  . GLY B 1 94  ? 74.316  79.618  98.065  1.00 21.30 ? 83   GLY B CA  1 
ATOM   3814 C  C   . GLY B 1 94  ? 73.616  80.112  96.825  1.00 21.30 ? 83   GLY B C   1 
ATOM   3815 O  O   . GLY B 1 94  ? 72.440  79.826  96.586  1.00 21.30 ? 83   GLY B O   1 
ATOM   3816 N  N   . PRO B 1 95  ? 74.350  80.873  96.016  1.00 21.07 ? 84   PRO B N   1 
ATOM   3817 C  CA  . PRO B 1 95  ? 73.744  81.496  94.840  1.00 21.07 ? 84   PRO B CA  1 
ATOM   3818 C  C   . PRO B 1 95  ? 73.257  80.466  93.840  1.00 21.07 ? 84   PRO B C   1 
ATOM   3819 O  O   . PRO B 1 95  ? 73.796  79.365  93.732  1.00 21.07 ? 84   PRO B O   1 
ATOM   3820 C  CB  . PRO B 1 95  ? 74.888  82.332  94.258  1.00 21.07 ? 84   PRO B CB  1 
ATOM   3821 C  CG  . PRO B 1 95  ? 75.810  82.540  95.383  1.00 21.07 ? 84   PRO B CG  1 
ATOM   3822 C  CD  . PRO B 1 95  ? 75.755  81.274  96.167  1.00 21.07 ? 84   PRO B CD  1 
ATOM   3823 N  N   . GLY B 1 96  ? 72.216  80.837  93.110  1.00 21.89 ? 85   GLY B N   1 
ATOM   3824 C  CA  . GLY B 1 96  ? 71.772  80.090  91.962  1.00 21.89 ? 85   GLY B CA  1 
ATOM   3825 C  C   . GLY B 1 96  ? 72.259  80.665  90.661  1.00 21.89 ? 85   GLY B C   1 
ATOM   3826 O  O   . GLY B 1 96  ? 71.965  80.111  89.599  1.00 21.89 ? 85   GLY B O   1 
ATOM   3827 N  N   . CYS B 1 97  ? 73.008  81.755  90.712  1.00 23.67 ? 86   CYS B N   1 
ATOM   3828 C  CA  . CYS B 1 97  ? 73.390  82.498  89.528  1.00 23.67 ? 86   CYS B CA  1 
ATOM   3829 C  C   . CYS B 1 97  ? 74.773  82.044  89.081  1.00 23.67 ? 86   CYS B C   1 
ATOM   3830 O  O   . CYS B 1 97  ? 75.666  81.839  89.906  1.00 23.67 ? 86   CYS B O   1 
ATOM   3831 C  CB  . CYS B 1 97  ? 73.365  83.990  89.848  1.00 23.67 ? 86   CYS B CB  1 
ATOM   3832 S  SG  . CYS B 1 97  ? 73.707  85.122  88.514  1.00 23.67 ? 86   CYS B SG  1 
ATOM   3833 N  N   . VAL B 1 98  ? 74.944  81.876  87.770  1.00 23.61 ? 87   VAL B N   1 
ATOM   3834 C  CA  . VAL B 1 98  ? 76.109  81.153  87.265  1.00 23.61 ? 87   VAL B CA  1 
ATOM   3835 C  C   . VAL B 1 98  ? 77.409  81.884  87.572  1.00 23.61 ? 87   VAL B C   1 
ATOM   3836 O  O   . VAL B 1 98  ? 78.464  81.252  87.690  1.00 23.61 ? 87   VAL B O   1 
ATOM   3837 C  CB  . VAL B 1 98  ? 75.960  80.902  85.756  1.00 23.61 ? 87   VAL B CB  1 
ATOM   3838 C  CG1 . VAL B 1 98  ? 77.250  80.363  85.187  1.00 23.61 ? 87   VAL B CG1 1 
ATOM   3839 C  CG2 . VAL B 1 98  ? 74.827  79.936  85.497  1.00 23.61 ? 87   VAL B CG2 1 
ATOM   3840 N  N   . TYR B 1 99  ? 77.373  83.208  87.690  1.00 24.99 ? 88   TYR B N   1 
ATOM   3841 C  CA  . TYR B 1 99  ? 78.596  83.985  87.852  1.00 24.99 ? 88   TYR B CA  1 
ATOM   3842 C  C   . TYR B 1 99  ? 78.944  84.256  89.307  1.00 24.99 ? 88   TYR B C   1 
ATOM   3843 O  O   . TYR B 1 99  ? 80.129  84.367  89.636  1.00 24.99 ? 88   TYR B O   1 
ATOM   3844 C  CB  . TYR B 1 99  ? 78.470  85.309  87.098  1.00 24.99 ? 88   TYR B CB  1 
ATOM   3845 C  CG  . TYR B 1 99  ? 78.672  85.178  85.606  1.00 24.99 ? 88   TYR B CG  1 
ATOM   3846 C  CD1 . TYR B 1 99  ? 79.787  84.536  85.091  1.00 24.99 ? 88   TYR B CD1 1 
ATOM   3847 C  CD2 . TYR B 1 99  ? 77.746  85.689  84.715  1.00 24.99 ? 88   TYR B CD2 1 
ATOM   3848 C  CE1 . TYR B 1 99  ? 79.975  84.414  83.735  1.00 24.99 ? 88   TYR B CE1 1 
ATOM   3849 C  CE2 . TYR B 1 99  ? 77.926  85.571  83.356  1.00 24.99 ? 88   TYR B CE2 1 
ATOM   3850 C  CZ  . TYR B 1 99  ? 79.041  84.932  82.872  1.00 24.99 ? 88   TYR B CZ  1 
ATOM   3851 O  OH  . TYR B 1 99  ? 79.228  84.808  81.517  1.00 24.99 ? 88   TYR B OH  1 
ATOM   3852 N  N   . ALA B 1 100 ? 77.947  84.383  90.181  1.00 20.91 ? 89   ALA B N   1 
ATOM   3853 C  CA  . ALA B 1 100 ? 78.211  84.471  91.613  1.00 20.91 ? 89   ALA B CA  1 
ATOM   3854 C  C   . ALA B 1 100 ? 78.536  83.106  92.205  1.00 20.91 ? 89   ALA B C   1 
ATOM   3855 O  O   . ALA B 1 100 ? 79.381  82.989  93.110  1.00 20.91 ? 89   ALA B O   1 
ATOM   3856 C  CB  . ALA B 1 100 ? 77.001  85.078  92.316  1.00 20.91 ? 89   ALA B CB  1 
ATOM   3857 N  N   . ALA B 1 101 ? 77.872  82.069  91.697  1.00 20.63 ? 90   ALA B N   1 
ATOM   3858 C  CA  . ALA B 1 101 ? 78.003  80.740  92.274  1.00 20.63 ? 90   ALA B CA  1 
ATOM   3859 C  C   . ALA B 1 101 ? 79.438  80.249  92.206  1.00 20.63 ? 90   ALA B C   1 
ATOM   3860 O  O   . ALA B 1 101 ? 79.906  79.576  93.123  1.00 20.63 ? 90   ALA B O   1 
ATOM   3861 C  CB  . ALA B 1 101 ? 77.066  79.768  91.562  1.00 20.63 ? 90   ALA B CB  1 
ATOM   3862 N  N   . ALA B 1 102 ? 80.161  80.583  91.139  1.00 20.46 ? 91   ALA B N   1 
ATOM   3863 C  CA  . ALA B 1 102 ? 81.540  80.113  91.018  1.00 20.46 ? 91   ALA B CA  1 
ATOM   3864 C  C   . ALA B 1 102 ? 82.421  80.617  92.152  1.00 20.46 ? 91   ALA B C   1 
ATOM   3865 O  O   . ALA B 1 102 ? 82.980  79.790  92.896  1.00 20.46 ? 91   ALA B O   1 
ATOM   3866 C  CB  . ALA B 1 102 ? 82.088  80.504  89.645  1.00 20.46 ? 91   ALA B CB  1 
ATOM   3867 N  N   . PRO B 1 103 ? 82.617  81.927  92.332  1.00 18.76 ? 92   PRO B N   1 
ATOM   3868 C  CA  . PRO B 1 103 ? 83.446  82.381  93.459  1.00 18.76 ? 92   PRO B CA  1 
ATOM   3869 C  C   . PRO B 1 103 ? 82.902  81.991  94.821  1.00 18.76 ? 92   PRO B C   1 
ATOM   3870 O  O   . PRO B 1 103 ? 83.691  81.649  95.714  1.00 18.76 ? 92   PRO B O   1 
ATOM   3871 C  CB  . PRO B 1 103 ? 83.480  83.903  93.274  1.00 18.76 ? 92   PRO B CB  1 
ATOM   3872 C  CG  . PRO B 1 103 ? 82.381  84.221  92.340  1.00 18.76 ? 92   PRO B CG  1 
ATOM   3873 C  CD  . PRO B 1 103 ? 82.256  83.046  91.450  1.00 18.76 ? 92   PRO B CD  1 
ATOM   3874 N  N   . VAL B 1 104 ? 81.582  82.018  95.020  1.00 18.78 ? 93   VAL B N   1 
ATOM   3875 C  CA  . VAL B 1 104 ? 81.067  81.640  96.333  1.00 18.78 ? 93   VAL B CA  1 
ATOM   3876 C  C   . VAL B 1 104 ? 81.361  80.171  96.619  1.00 18.78 ? 93   VAL B C   1 
ATOM   3877 O  O   . VAL B 1 104 ? 81.725  79.803  97.742  1.00 18.78 ? 93   VAL B O   1 
ATOM   3878 C  CB  . VAL B 1 104 ? 79.567  81.952  96.437  1.00 18.78 ? 93   VAL B CB  1 
ATOM   3879 C  CG1 . VAL B 1 104 ? 79.030  81.493  97.775  1.00 18.78 ? 93   VAL B CG1 1 
ATOM   3880 C  CG2 . VAL B 1 104 ? 79.330  83.428  96.265  1.00 18.78 ? 93   VAL B CG2 1 
ATOM   3881 N  N   . GLY B 1 105 ? 81.209  79.309  95.614  1.00 19.99 ? 94   GLY B N   1 
ATOM   3882 C  CA  . GLY B 1 105 ? 81.493  77.901  95.809  1.00 19.99 ? 94   GLY B CA  1 
ATOM   3883 C  C   . GLY B 1 105 ? 82.962  77.630  96.049  1.00 19.99 ? 94   GLY B C   1 
ATOM   3884 O  O   . GLY B 1 105 ? 83.314  76.751  96.836  1.00 19.99 ? 94   GLY B O   1 
ATOM   3885 N  N   . ARG B 1 106 ? 83.844  78.370  95.374  1.00 20.23 ? 95   ARG B N   1 
ATOM   3886 C  CA  . ARG B 1 106 ? 85.268  78.220  95.659  1.00 20.23 ? 95   ARG B CA  1 
ATOM   3887 C  C   . ARG B 1 106 ? 85.585  78.614  97.096  1.00 20.23 ? 95   ARG B C   1 
ATOM   3888 O  O   . ARG B 1 106 ? 86.335  77.915  97.792  1.00 20.23 ? 95   ARG B O   1 
ATOM   3889 C  CB  . ARG B 1 106 ? 86.092  79.050  94.681  1.00 20.23 ? 95   ARG B CB  1 
ATOM   3890 C  CG  . ARG B 1 106 ? 86.073  78.506  93.273  1.00 20.23 ? 95   ARG B CG  1 
ATOM   3891 C  CD  . ARG B 1 106 ? 87.228  79.029  92.464  1.00 20.23 ? 95   ARG B CD  1 
ATOM   3892 N  NE  . ARG B 1 106 ? 87.103  80.455  92.181  1.00 20.23 ? 95   ARG B NE  1 
ATOM   3893 C  CZ  . ARG B 1 106 ? 86.608  80.967  91.058  1.00 20.23 ? 95   ARG B CZ  1 
ATOM   3894 N  NH1 . ARG B 1 106 ? 86.178  80.178  90.082  1.00 20.23 ? 95   ARG B NH1 1 
ATOM   3895 N  NH2 . ARG B 1 106 ? 86.549  82.281  90.909  1.00 20.23 ? 95   ARG B NH2 1 
ATOM   3896 N  N   . PHE B 1 107 ? 85.004  79.716  97.571  1.00 18.68 ? 96   PHE B N   1 
ATOM   3897 C  CA  . PHE B 1 107 ? 85.237  80.121  98.954  1.00 18.68 ? 96   PHE B CA  1 
ATOM   3898 C  C   . PHE B 1 107 ? 84.744  79.060  99.931  1.00 18.68 ? 96   PHE B C   1 
ATOM   3899 O  O   . PHE B 1 107 ? 85.457  78.688  100.869 1.00 18.68 ? 96   PHE B O   1 
ATOM   3900 C  CB  . PHE B 1 107 ? 84.557  81.460  99.230  1.00 18.68 ? 96   PHE B CB  1 
ATOM   3901 C  CG  . PHE B 1 107 ? 85.440  82.644  98.983  1.00 18.68 ? 96   PHE B CG  1 
ATOM   3902 C  CD1 . PHE B 1 107 ? 86.403  83.008  99.899  1.00 18.68 ? 96   PHE B CD1 1 
ATOM   3903 C  CD2 . PHE B 1 107 ? 85.314  83.385  97.828  1.00 18.68 ? 96   PHE B CD2 1 
ATOM   3904 C  CE1 . PHE B 1 107 ? 87.214  84.089  99.668  1.00 18.68 ? 96   PHE B CE1 1 
ATOM   3905 C  CE2 . PHE B 1 107 ? 86.126  84.464  97.596  1.00 18.68 ? 96   PHE B CE2 1 
ATOM   3906 C  CZ  . PHE B 1 107 ? 87.073  84.816  98.516  1.00 18.68 ? 96   PHE B CZ  1 
ATOM   3907 N  N   . THR B 1 108 ? 83.525  78.554  99.728  1.00 19.92 ? 97   THR B N   1 
ATOM   3908 C  CA  . THR B 1 108 ? 82.981  77.588  100.681 1.00 19.92 ? 97   THR B CA  1 
ATOM   3909 C  C   . THR B 1 108 ? 83.698  76.248  100.600 1.00 19.92 ? 97   THR B C   1 
ATOM   3910 O  O   . THR B 1 108 ? 83.782  75.535  101.605 1.00 19.92 ? 97   THR B O   1 
ATOM   3911 C  CB  . THR B 1 108 ? 81.483  77.390  100.463 1.00 19.92 ? 97   THR B CB  1 
ATOM   3912 O  OG1 . THR B 1 108 ? 81.252  76.856  99.157  1.00 19.92 ? 97   THR B OG1 1 
ATOM   3913 C  CG2 . THR B 1 108 ? 80.738  78.696  100.626 1.00 19.92 ? 97   THR B CG2 1 
ATOM   3914 N  N   . ALA B 1 109 ? 84.209  75.879  99.424  1.00 21.06 ? 98   ALA B N   1 
ATOM   3915 C  CA  . ALA B 1 109 ? 85.065  74.705  99.332  1.00 21.06 ? 98   ALA B CA  1 
ATOM   3916 C  C   . ALA B 1 109 ? 86.330  74.899  100.149 1.00 21.06 ? 98   ALA B C   1 
ATOM   3917 O  O   . ALA B 1 109 ? 86.794  73.971  100.818 1.00 21.06 ? 98   ALA B O   1 
ATOM   3918 C  CB  . ALA B 1 109 ? 85.411  74.425  97.874  1.00 21.06 ? 98   ALA B CB  1 
ATOM   3919 N  N   . HIS B 1 110 ? 86.905  76.104  100.106 1.00 20.55 ? 99   HIS B N   1 
ATOM   3920 C  CA  . HIS B 1 110 ? 88.073  76.383  100.935 1.00 20.55 ? 99   HIS B CA  1 
ATOM   3921 C  C   . HIS B 1 110 ? 87.740  76.283  102.420 1.00 20.55 ? 99   HIS B C   1 
ATOM   3922 O  O   . HIS B 1 110 ? 88.519  75.723  103.198 1.00 20.55 ? 99   HIS B O   1 
ATOM   3923 C  CB  . HIS B 1 110 ? 88.633  77.764  100.610 1.00 20.55 ? 99   HIS B CB  1 
ATOM   3924 C  CG  . HIS B 1 110 ? 89.884  78.097  101.359 1.00 20.55 ? 99   HIS B CG  1 
ATOM   3925 N  ND1 . HIS B 1 110 ? 91.104  77.537  101.053 1.00 20.55 ? 99   HIS B ND1 1 
ATOM   3926 C  CD2 . HIS B 1 110 ? 90.105  78.933  102.399 1.00 20.55 ? 99   HIS B CD2 1 
ATOM   3927 C  CE1 . HIS B 1 110 ? 92.023  78.012  101.874 1.00 20.55 ? 99   HIS B CE1 1 
ATOM   3928 N  NE2 . HIS B 1 110 ? 91.442  78.862  102.701 1.00 20.55 ? 99   HIS B NE2 1 
ATOM   3929 N  N   . TRP B 1 111 ? 86.596  76.827  102.839 1.00 20.59 ? 100  TRP B N   1 
ATOM   3930 C  CA  . TRP B 1 111 ? 86.227  76.787  104.251 1.00 20.59 ? 100  TRP B CA  1 
ATOM   3931 C  C   . TRP B 1 111 ? 85.732  75.421  104.706 1.00 20.59 ? 100  TRP B C   1 
ATOM   3932 O  O   . TRP B 1 111 ? 85.526  75.232  105.908 1.00 20.59 ? 100  TRP B O   1 
ATOM   3933 C  CB  . TRP B 1 111 ? 85.136  77.810  104.568 1.00 20.59 ? 100  TRP B CB  1 
ATOM   3934 C  CG  . TRP B 1 111 ? 85.475  79.222  104.249 1.00 20.59 ? 100  TRP B CG  1 
ATOM   3935 C  CD1 . TRP B 1 111 ? 86.695  79.813  104.331 1.00 20.59 ? 100  TRP B CD1 1 
ATOM   3936 C  CD2 . TRP B 1 111 ? 84.565  80.234  103.814 1.00 20.59 ? 100  TRP B CD2 1 
ATOM   3937 N  NE1 . TRP B 1 111 ? 86.607  81.130  103.961 1.00 20.59 ? 100  TRP B NE1 1 
ATOM   3938 C  CE2 . TRP B 1 111 ? 85.306  81.413  103.641 1.00 20.59 ? 100  TRP B CE2 1 
ATOM   3939 C  CE3 . TRP B 1 111 ? 83.194  80.256  103.549 1.00 20.59 ? 100  TRP B CE3 1 
ATOM   3940 C  CZ2 . TRP B 1 111 ? 84.724  82.600  103.213 1.00 20.59 ? 100  TRP B CZ2 1 
ATOM   3941 C  CZ3 . TRP B 1 111 ? 82.621  81.431  103.124 1.00 20.59 ? 100  TRP B CZ3 1 
ATOM   3942 C  CH2 . TRP B 1 111 ? 83.382  82.586  102.960 1.00 20.59 ? 100  TRP B CH2 1 
ATOM   3943 N  N   . ARG B 1 112 ? 85.516  74.479  103.785 1.00 24.68 ? 101  ARG B N   1 
ATOM   3944 C  CA  . ARG B 1 112 ? 85.004  73.147  104.115 1.00 24.68 ? 101  ARG B CA  1 
ATOM   3945 C  C   . ARG B 1 112 ? 83.576  73.226  104.659 1.00 24.68 ? 101  ARG B C   1 
ATOM   3946 O  O   . ARG B 1 112 ? 83.241  72.603  105.666 1.00 24.68 ? 101  ARG B O   1 
ATOM   3947 C  CB  . ARG B 1 112 ? 85.923  72.428  105.106 1.00 24.68 ? 101  ARG B CB  1 
ATOM   3948 C  CG  . ARG B 1 112 ? 87.344  72.220  104.616 1.00 24.68 ? 101  ARG B CG  1 
ATOM   3949 C  CD  . ARG B 1 112 ? 87.408  71.213  103.482 1.00 24.68 ? 101  ARG B CD  1 
ATOM   3950 N  NE  . ARG B 1 112 ? 86.981  69.885  103.912 1.00 24.68 ? 101  ARG B NE  1 
ATOM   3951 C  CZ  . ARG B 1 112 ? 86.607  68.910  103.089 1.00 24.68 ? 101  ARG B CZ  1 
ATOM   3952 N  NH1 . ARG B 1 112 ? 86.233  67.738  103.583 1.00 24.68 ? 101  ARG B NH1 1 
ATOM   3953 N  NH2 . ARG B 1 112 ? 86.608  69.099  101.777 1.00 24.68 ? 101  ARG B NH2 1 
ATOM   3954 N  N   . VAL B 1 113 ? 82.733  73.992  103.973 1.00 22.42 ? 102  VAL B N   1 
ATOM   3955 C  CA  . VAL B 1 113 ? 81.337  74.172  104.365 1.00 22.42 ? 102  VAL B CA  1 
ATOM   3956 C  C   . VAL B 1 113 ? 80.450  73.721  103.208 1.00 22.42 ? 102  VAL B C   1 
ATOM   3957 O  O   . VAL B 1 113 ? 80.743  74.047  102.051 1.00 22.42 ? 102  VAL B O   1 
ATOM   3958 C  CB  . VAL B 1 113 ? 81.054  75.633  104.750 1.00 22.42 ? 102  VAL B CB  1 
ATOM   3959 C  CG1 . VAL B 1 113 ? 79.569  75.883  104.842 1.00 22.42 ? 102  VAL B CG1 1 
ATOM   3960 C  CG2 . VAL B 1 113 ? 81.719  75.971  106.062 1.00 22.42 ? 102  VAL B CG2 1 
ATOM   3961 N  N   . PRO B 1 114 ? 79.375  72.975  103.454 1.00 22.12 ? 103  PRO B N   1 
ATOM   3962 C  CA  . PRO B 1 114 ? 78.490  72.580  102.354 1.00 22.12 ? 103  PRO B CA  1 
ATOM   3963 C  C   . PRO B 1 114 ? 77.803  73.780  101.722 1.00 22.12 ? 103  PRO B C   1 
ATOM   3964 O  O   . PRO B 1 114 ? 77.622  74.827  102.340 1.00 22.12 ? 103  PRO B O   1 
ATOM   3965 C  CB  . PRO B 1 114 ? 77.474  71.654  103.027 1.00 22.12 ? 103  PRO B CB  1 
ATOM   3966 C  CG  . PRO B 1 114 ? 78.124  71.193  104.260 1.00 22.12 ? 103  PRO B CG  1 
ATOM   3967 C  CD  . PRO B 1 114 ? 79.017  72.296  104.709 1.00 22.12 ? 103  PRO B CD  1 
ATOM   3968 N  N   . LEU B 1 115 ? 77.418  73.612  100.459 1.00 21.01 ? 104  LEU B N   1 
ATOM   3969 C  CA  . LEU B 1 115 ? 76.720  74.654  99.711  1.00 21.01 ? 104  LEU B CA  1 
ATOM   3970 C  C   . LEU B 1 115 ? 75.588  74.011  98.925  1.00 21.01 ? 104  LEU B C   1 
ATOM   3971 O  O   . LEU B 1 115 ? 75.837  73.302  97.949  1.00 21.01 ? 104  LEU B O   1 
ATOM   3972 C  CB  . LEU B 1 115 ? 77.669  75.401  98.776  1.00 21.01 ? 104  LEU B CB  1 
ATOM   3973 C  CG  . LEU B 1 115 ? 77.049  76.581  98.025  1.00 21.01 ? 104  LEU B CG  1 
ATOM   3974 C  CD1 . LEU B 1 115 ? 78.057  77.677  97.839  1.00 21.01 ? 104  LEU B CD1 1 
ATOM   3975 C  CD2 . LEU B 1 115 ? 76.521  76.151  96.681  1.00 21.01 ? 104  LEU B CD2 1 
ATOM   3976 N  N   . LEU B 1 116 ? 74.353  74.267  99.341  1.00 23.97 ? 105  LEU B N   1 
ATOM   3977 C  CA  . LEU B 1 116 ? 73.176  73.813  98.617  1.00 23.97 ? 105  LEU B CA  1 
ATOM   3978 C  C   . LEU B 1 116 ? 72.748  74.850  97.596  1.00 23.97 ? 105  LEU B C   1 
ATOM   3979 O  O   . LEU B 1 116 ? 72.756  76.049  97.875  1.00 23.97 ? 105  LEU B O   1 
ATOM   3980 C  CB  . LEU B 1 116 ? 72.017  73.561  99.573  1.00 23.97 ? 105  LEU B CB  1 
ATOM   3981 C  CG  . LEU B 1 116 ? 71.908  72.161  100.151 1.00 23.97 ? 105  LEU B CG  1 
ATOM   3982 C  CD1 . LEU B 1 116 ? 71.290  72.209  101.530 1.00 23.97 ? 105  LEU B CD1 1 
ATOM   3983 C  CD2 . LEU B 1 116 ? 71.078  71.308  99.216  1.00 23.97 ? 105  LEU B CD2 1 
ATOM   3984 N  N   . THR B 1 117 ? 72.362  74.387  96.413  1.00 22.51 ? 106  THR B N   1 
ATOM   3985 C  CA  . THR B 1 117 ? 71.786  75.305  95.444  1.00 22.51 ? 106  THR B CA  1 
ATOM   3986 C  C   . THR B 1 117 ? 70.895  74.541  94.480  1.00 22.51 ? 106  THR B C   1 
ATOM   3987 O  O   . THR B 1 117 ? 71.170  73.392  94.138  1.00 22.51 ? 106  THR B O   1 
ATOM   3988 C  CB  . THR B 1 117 ? 72.878  76.067  94.687  1.00 22.51 ? 106  THR B CB  1 
ATOM   3989 O  OG1 . THR B 1 117 ? 72.273  77.010  93.799  1.00 22.51 ? 106  THR B OG1 1 
ATOM   3990 C  CG2 . THR B 1 117 ? 73.757  75.124  93.899  1.00 22.51 ? 106  THR B CG2 1 
ATOM   3991 N  N   . ALA B 1 118 ? 69.803  75.183  94.070  1.00 23.85 ? 107  ALA B N   1 
ATOM   3992 C  CA  . ALA B 1 118 ? 68.976  74.701  92.973  1.00 23.85 ? 107  ALA B CA  1 
ATOM   3993 C  C   . ALA B 1 118 ? 69.191  75.514  91.705  1.00 23.85 ? 107  ALA B C   1 
ATOM   3994 O  O   . ALA B 1 118 ? 68.466  75.324  90.726  1.00 23.85 ? 107  ALA B O   1 
ATOM   3995 C  CB  . ALA B 1 118 ? 67.499  74.719  93.361  1.00 23.85 ? 107  ALA B CB  1 
ATOM   3996 N  N   . GLY B 1 119 ? 70.160  76.425  91.708  1.00 22.69 ? 108  GLY B N   1 
ATOM   3997 C  CA  . GLY B 1 119 ? 70.574  77.112  90.505  1.00 22.69 ? 108  GLY B CA  1 
ATOM   3998 C  C   . GLY B 1 119 ? 71.983  76.712  90.125  1.00 22.69 ? 108  GLY B C   1 
ATOM   3999 O  O   . GLY B 1 119 ? 72.377  75.563  90.332  1.00 22.69 ? 108  GLY B O   1 
ATOM   4000 N  N   . ALA B 1 120 ? 72.754  77.644  89.576  1.00 22.66 ? 109  ALA B N   1 
ATOM   4001 C  CA  . ALA B 1 120 ? 74.134  77.395  89.180  1.00 22.66 ? 109  ALA B CA  1 
ATOM   4002 C  C   . ALA B 1 120 ? 74.252  76.104  88.367  1.00 22.66 ? 109  ALA B C   1 
ATOM   4003 O  O   . ALA B 1 120 ? 75.007  75.199  88.737  1.00 22.66 ? 109  ALA B O   1 
ATOM   4004 C  CB  . ALA B 1 120 ? 75.042  77.345  90.400  1.00 22.66 ? 109  ALA B CB  1 
ATOM   4005 N  N   . PRO B 1 121 ? 73.518  75.985  87.259  1.00 24.74 ? 110  PRO B N   1 
ATOM   4006 C  CA  . PRO B 1 121 ? 73.524  74.737  86.491  1.00 24.74 ? 110  PRO B CA  1 
ATOM   4007 C  C   . PRO B 1 121 ? 74.656  74.611  85.487  1.00 24.74 ? 110  PRO B C   1 
ATOM   4008 O  O   . PRO B 1 121 ? 74.699  73.613  84.761  1.00 24.74 ? 110  PRO B O   1 
ATOM   4009 C  CB  . PRO B 1 121 ? 72.174  74.792  85.776  1.00 24.74 ? 110  PRO B CB  1 
ATOM   4010 C  CG  . PRO B 1 121 ? 71.970  76.226  85.539  1.00 24.74 ? 110  PRO B CG  1 
ATOM   4011 C  CD  . PRO B 1 121 ? 72.528  76.936  86.730  1.00 24.74 ? 110  PRO B CD  1 
ATOM   4012 N  N   . ALA B 1 122 ? 75.572  75.572  85.417  1.00 25.54 ? 111  ALA B N   1 
ATOM   4013 C  CA  . ALA B 1 122 ? 76.605  75.541  84.398  1.00 25.54 ? 111  ALA B CA  1 
ATOM   4014 C  C   . ALA B 1 122 ? 77.416  74.252  84.497  1.00 25.54 ? 111  ALA B C   1 
ATOM   4015 O  O   . ALA B 1 122 ? 77.327  73.497  85.464  1.00 25.54 ? 111  ALA B O   1 
ATOM   4016 C  CB  . ALA B 1 122 ? 77.519  76.755  84.528  1.00 25.54 ? 111  ALA B CB  1 
ATOM   4017 N  N   . LEU B 1 123 ? 78.217  74.002  83.461  1.00 30.64 ? 112  LEU B N   1 
ATOM   4018 C  CA  . LEU B 1 123 ? 79.005  72.774  83.412  1.00 30.64 ? 112  LEU B CA  1 
ATOM   4019 C  C   . LEU B 1 123 ? 80.203  72.840  84.351  1.00 30.64 ? 112  LEU B C   1 
ATOM   4020 O  O   . LEU B 1 123 ? 80.570  71.833  84.967  1.00 30.64 ? 112  LEU B O   1 
ATOM   4021 C  CB  . LEU B 1 123 ? 79.467  72.516  81.980  1.00 30.64 ? 112  LEU B CB  1 
ATOM   4022 C  CG  . LEU B 1 123 ? 80.161  71.183  81.716  1.00 30.64 ? 112  LEU B CG  1 
ATOM   4023 C  CD1 . LEU B 1 123 ? 79.160  70.046  81.701  1.00 30.64 ? 112  LEU B CD1 1 
ATOM   4024 C  CD2 . LEU B 1 123 ? 80.920  71.246  80.413  1.00 30.64 ? 112  LEU B CD2 1 
ATOM   4025 N  N   . GLY B 1 124 ? 80.829  74.011  84.471  1.00 26.40 ? 113  GLY B N   1 
ATOM   4026 C  CA  . GLY B 1 124 ? 82.038  74.129  85.266  1.00 26.40 ? 113  GLY B CA  1 
ATOM   4027 C  C   . GLY B 1 124 ? 81.831  73.917  86.750  1.00 26.40 ? 113  GLY B C   1 
ATOM   4028 O  O   . GLY B 1 124 ? 82.795  73.617  87.460  1.00 26.40 ? 113  GLY B O   1 
ATOM   4029 N  N   . PHE B 1 125 ? 80.602  74.069  87.234  1.00 24.62 ? 114  PHE B N   1 
ATOM   4030 C  CA  . PHE B 1 125 ? 80.313  73.919  88.653  1.00 24.62 ? 114  PHE B CA  1 
ATOM   4031 C  C   . PHE B 1 125 ? 80.267  72.465  89.098  1.00 24.62 ? 114  PHE B C   1 
ATOM   4032 O  O   . PHE B 1 125 ? 80.227  72.206  90.304  1.00 24.62 ? 114  PHE B O   1 
ATOM   4033 C  CB  . PHE B 1 125 ? 78.982  74.600  88.976  1.00 24.62 ? 114  PHE B CB  1 
ATOM   4034 C  CG  . PHE B 1 125 ? 78.825  74.981  90.417  1.00 24.62 ? 114  PHE B CG  1 
ATOM   4035 C  CD1 . PHE B 1 125 ? 79.393  76.139  90.903  1.00 24.62 ? 114  PHE B CD1 1 
ATOM   4036 C  CD2 . PHE B 1 125 ? 78.095  74.189  91.282  1.00 24.62 ? 114  PHE B CD2 1 
ATOM   4037 C  CE1 . PHE B 1 125 ? 79.248  76.492  92.223  1.00 24.62 ? 114  PHE B CE1 1 
ATOM   4038 C  CE2 . PHE B 1 125 ? 77.947  74.541  92.604  1.00 24.62 ? 114  PHE B CE2 1 
ATOM   4039 C  CZ  . PHE B 1 125 ? 78.525  75.694  93.074  1.00 24.62 ? 114  PHE B CZ  1 
ATOM   4040 N  N   . GLY B 1 126 ? 80.269  71.519  88.168  1.00 27.46 ? 115  GLY B N   1 
ATOM   4041 C  CA  . GLY B 1 126 ? 80.157  70.111  88.479  1.00 27.46 ? 115  GLY B CA  1 
ATOM   4042 C  C   . GLY B 1 126 ? 81.464  69.369  88.643  1.00 27.46 ? 115  GLY B C   1 
ATOM   4043 O  O   . GLY B 1 126 ? 81.443  68.142  88.773  1.00 27.46 ? 115  GLY B O   1 
ATOM   4044 N  N   . VAL B 1 127 ? 82.600  70.063  88.628  1.00 28.59 ? 116  VAL B N   1 
ATOM   4045 C  CA  . VAL B 1 127 ? 83.903  69.428  88.838  1.00 28.59 ? 116  VAL B CA  1 
ATOM   4046 C  C   . VAL B 1 127 ? 84.157  69.462  90.343  1.00 28.59 ? 116  VAL B C   1 
ATOM   4047 O  O   . VAL B 1 127 ? 84.765  70.384  90.880  1.00 28.59 ? 116  VAL B O   1 
ATOM   4048 C  CB  . VAL B 1 127 ? 85.009  70.106  88.030  1.00 28.59 ? 116  VAL B CB  1 
ATOM   4049 C  CG1 . VAL B 1 127 ? 86.352  69.496  88.373  1.00 28.59 ? 116  VAL B CG1 1 
ATOM   4050 C  CG2 . VAL B 1 127 ? 84.761  69.980  86.539  1.00 28.59 ? 116  VAL B CG2 1 
ATOM   4051 N  N   . LYS B 1 128 ? 83.684  68.426  91.035  1.00 28.49 ? 117  LYS B N   1 
ATOM   4052 C  CA  . LYS B 1 128 ? 83.722  68.408  92.492  1.00 28.49 ? 117  LYS B CA  1 
ATOM   4053 C  C   . LYS B 1 128 ? 85.130  68.287  93.055  1.00 28.49 ? 117  LYS B C   1 
ATOM   4054 O  O   . LYS B 1 128 ? 85.276  68.204  94.278  1.00 28.49 ? 117  LYS B O   1 
ATOM   4055 C  CB  . LYS B 1 128 ? 82.855  67.269  93.023  1.00 28.49 ? 117  LYS B CB  1 
ATOM   4056 C  CG  . LYS B 1 128 ? 81.423  67.311  92.529  1.00 28.49 ? 117  LYS B CG  1 
ATOM   4057 C  CD  . LYS B 1 128 ? 80.669  68.507  93.084  1.00 28.49 ? 117  LYS B CD  1 
ATOM   4058 C  CE  . LYS B 1 128 ? 79.175  68.378  92.840  1.00 28.49 ? 117  LYS B CE  1 
ATOM   4059 N  NZ  . LYS B 1 128 ? 78.590  69.594  92.218  1.00 28.49 ? 117  LYS B NZ  1 
ATOM   4060 N  N   . ASP B 1 129 ? 86.164  68.256  92.213  1.00 29.53 ? 118  ASP B N   1 
ATOM   4061 C  CA  . ASP B 1 129 ? 87.523  68.367  92.729  1.00 29.53 ? 118  ASP B CA  1 
ATOM   4062 C  C   . ASP B 1 129 ? 87.822  69.795  93.167  1.00 29.53 ? 118  ASP B C   1 
ATOM   4063 O  O   . ASP B 1 129 ? 88.453  70.014  94.206  1.00 29.53 ? 118  ASP B O   1 
ATOM   4064 C  CB  . ASP B 1 129 ? 88.525  67.907  91.673  1.00 29.53 ? 118  ASP B CB  1 
ATOM   4065 N  N   . GLU B 1 130 ? 87.370  70.778  92.388  1.00 30.05 ? 119  GLU B N   1 
ATOM   4066 C  CA  . GLU B 1 130 ? 87.551  72.183  92.724  1.00 30.05 ? 119  GLU B CA  1 
ATOM   4067 C  C   . GLU B 1 130 ? 86.415  72.733  93.574  1.00 30.05 ? 119  GLU B C   1 
ATOM   4068 O  O   . GLU B 1 130 ? 86.638  73.654  94.367  1.00 30.05 ? 119  GLU B O   1 
ATOM   4069 C  CB  . GLU B 1 130 ? 87.672  73.013  91.444  1.00 30.05 ? 119  GLU B CB  1 
ATOM   4070 C  CG  . GLU B 1 130 ? 87.690  74.515  91.666  1.00 30.05 ? 119  GLU B CG  1 
ATOM   4071 C  CD  . GLU B 1 130 ? 87.891  75.285  90.378  1.00 30.05 ? 119  GLU B CD  1 
ATOM   4072 O  OE1 . GLU B 1 130 ? 88.246  76.482  90.447  1.00 30.05 ? 119  GLU B OE1 1 
ATOM   4073 O  OE2 . GLU B 1 130 ? 87.691  74.695  89.297  1.00 30.05 ? 119  GLU B OE2 1 
ATOM   4074 N  N   . TYR B 1 131 ? 85.208  72.196  93.423  1.00 24.88 ? 120  TYR B N   1 
ATOM   4075 C  CA  . TYR B 1 131 ? 84.035  72.619  94.181  1.00 24.88 ? 120  TYR B CA  1 
ATOM   4076 C  C   . TYR B 1 131 ? 83.672  71.481  95.129  1.00 24.88 ? 120  TYR B C   1 
ATOM   4077 O  O   . TYR B 1 131 ? 82.806  70.659  94.833  1.00 24.88 ? 120  TYR B O   1 
ATOM   4078 C  CB  . TYR B 1 131 ? 82.879  72.952  93.250  1.00 24.88 ? 120  TYR B CB  1 
ATOM   4079 C  CG  . TYR B 1 131 ? 83.124  74.150  92.367  1.00 24.88 ? 120  TYR B CG  1 
ATOM   4080 C  CD1 . TYR B 1 131 ? 83.043  75.436  92.870  1.00 24.88 ? 120  TYR B CD1 1 
ATOM   4081 C  CD2 . TYR B 1 131 ? 83.432  73.994  91.030  1.00 24.88 ? 120  TYR B CD2 1 
ATOM   4082 C  CE1 . TYR B 1 131 ? 83.266  76.527  92.067  1.00 24.88 ? 120  TYR B CE1 1 
ATOM   4083 C  CE2 . TYR B 1 131 ? 83.657  75.081  90.223  1.00 24.88 ? 120  TYR B CE2 1 
ATOM   4084 C  CZ  . TYR B 1 131 ? 83.571  76.344  90.747  1.00 24.88 ? 120  TYR B CZ  1 
ATOM   4085 O  OH  . TYR B 1 131 ? 83.793  77.431  89.941  1.00 24.88 ? 120  TYR B OH  1 
ATOM   4086 N  N   . ALA B 1 132 ? 84.329  71.445  96.279  1.00 24.78 ? 121  ALA B N   1 
ATOM   4087 C  CA  . ALA B 1 132 ? 84.127  70.377  97.241  1.00 24.78 ? 121  ALA B CA  1 
ATOM   4088 C  C   . ALA B 1 132 ? 82.934  70.688  98.133  1.00 24.78 ? 121  ALA B C   1 
ATOM   4089 O  O   . ALA B 1 132 ? 82.759  71.822  98.582  1.00 24.78 ? 121  ALA B O   1 
ATOM   4090 C  CB  . ALA B 1 132 ? 85.380  70.183  98.093  1.00 24.78 ? 121  ALA B CB  1 
ATOM   4091 N  N   . LEU B 1 133 ? 82.111  69.672  98.377  1.00 25.00 ? 122  LEU B N   1 
ATOM   4092 C  CA  . LEU B 1 133 ? 80.988  69.704  99.308  1.00 25.00 ? 122  LEU B CA  1 
ATOM   4093 C  C   . LEU B 1 133 ? 79.750  70.393  98.748  1.00 25.00 ? 122  LEU B C   1 
ATOM   4094 O  O   . LEU B 1 133 ? 78.785  70.575  99.496  1.00 25.00 ? 122  LEU B O   1 
ATOM   4095 C  CB  . LEU B 1 133 ? 81.359  70.394  100.624 1.00 25.00 ? 122  LEU B CB  1 
ATOM   4096 C  CG  . LEU B 1 133 ? 82.572  69.854  101.381 1.00 25.00 ? 122  LEU B CG  1 
ATOM   4097 C  CD1 . LEU B 1 133 ? 82.999  70.820  102.459 1.00 25.00 ? 122  LEU B CD1 1 
ATOM   4098 C  CD2 . LEU B 1 133 ? 82.277  68.508  101.987 1.00 25.00 ? 122  LEU B CD2 1 
ATOM   4099 N  N   . THR B 1 134 ? 79.730  70.776  97.475  1.00 23.97 ? 123  THR B N   1 
ATOM   4100 C  CA  . THR B 1 134 ? 78.589  71.482  96.907  1.00 23.97 ? 123  THR B CA  1 
ATOM   4101 C  C   . THR B 1 134 ? 77.569  70.496  96.358  1.00 23.97 ? 123  THR B C   1 
ATOM   4102 O  O   . THR B 1 134 ? 77.927  69.510  95.711  1.00 23.97 ? 123  THR B O   1 
ATOM   4103 C  CB  . THR B 1 134 ? 79.029  72.436  95.796  1.00 23.97 ? 123  THR B CB  1 
ATOM   4104 O  OG1 . THR B 1 134 ? 79.486  71.684  94.671  1.00 23.97 ? 123  THR B OG1 1 
ATOM   4105 C  CG2 . THR B 1 134 ? 80.142  73.346  96.276  1.00 23.97 ? 123  THR B CG2 1 
ATOM   4106 N  N   . THR B 1 135 ? 76.294  70.772  96.618  1.00 25.84 ? 124  THR B N   1 
ATOM   4107 C  CA  . THR B 1 135 ? 75.189  69.933  96.179  1.00 25.84 ? 124  THR B CA  1 
ATOM   4108 C  C   . THR B 1 135 ? 74.221  70.768  95.357  1.00 25.84 ? 124  THR B C   1 
ATOM   4109 O  O   . THR B 1 135 ? 73.820  71.861  95.777  1.00 25.84 ? 124  THR B O   1 
ATOM   4110 C  CB  . THR B 1 135 ? 74.459  69.311  97.372  1.00 25.84 ? 124  THR B CB  1 
ATOM   4111 O  OG1 . THR B 1 135 ? 75.412  68.742  98.275  1.00 25.84 ? 124  THR B OG1 1 
ATOM   4112 C  CG2 . THR B 1 135 ? 73.500  68.231  96.912  1.00 25.84 ? 124  THR B CG2 1 
ATOM   4113 N  N   . ARG B 1 136 ? 73.853  70.251  94.191  1.00 25.32 ? 125  ARG B N   1 
ATOM   4114 C  CA  . ARG B 1 136 ? 72.870  70.872  93.315  1.00 25.32 ? 125  ARG B CA  1 
ATOM   4115 C  C   . ARG B 1 136 ? 71.582  70.069  93.419  1.00 25.32 ? 125  ARG B C   1 
ATOM   4116 O  O   . ARG B 1 136 ? 71.501  68.949  92.909  1.00 25.32 ? 125  ARG B O   1 
ATOM   4117 C  CB  . ARG B 1 136 ? 73.368  70.923  91.876  1.00 25.32 ? 125  ARG B CB  1 
ATOM   4118 C  CG  . ARG B 1 136 ? 74.541  71.848  91.670  1.00 25.32 ? 125  ARG B CG  1 
ATOM   4119 C  CD  . ARG B 1 136 ? 74.699  72.216  90.213  1.00 25.32 ? 125  ARG B CD  1 
ATOM   4120 N  NE  . ARG B 1 136 ? 75.559  71.275  89.506  1.00 25.32 ? 125  ARG B NE  1 
ATOM   4121 C  CZ  . ARG B 1 136 ? 76.094  71.504  88.315  1.00 25.32 ? 125  ARG B CZ  1 
ATOM   4122 N  NH1 . ARG B 1 136 ? 75.860  72.646  87.690  1.00 25.32 ? 125  ARG B NH1 1 
ATOM   4123 N  NH2 . ARG B 1 136 ? 76.865  70.592  87.744  1.00 25.32 ? 125  ARG B NH2 1 
ATOM   4124 N  N   . ALA B 1 137 ? 70.584  70.638  94.083  1.00 25.94 ? 126  ALA B N   1 
ATOM   4125 C  CA  . ALA B 1 137 ? 69.292  69.992  94.240  1.00 25.94 ? 126  ALA B CA  1 
ATOM   4126 C  C   . ALA B 1 137 ? 68.323  70.341  93.125  1.00 25.94 ? 126  ALA B C   1 
ATOM   4127 O  O   . ALA B 1 137 ? 67.173  69.900  93.166  1.00 25.94 ? 126  ALA B O   1 
ATOM   4128 C  CB  . ALA B 1 137 ? 68.676  70.368  95.587  1.00 25.94 ? 126  ALA B CB  1 
ATOM   4129 N  N   . GLY B 1 138 ? 68.756  71.112  92.135  1.00 27.18 ? 127  GLY B N   1 
ATOM   4130 C  CA  . GLY B 1 138 ? 67.905  71.499  91.040  1.00 27.18 ? 127  GLY B CA  1 
ATOM   4131 C  C   . GLY B 1 138 ? 68.451  71.036  89.710  1.00 27.18 ? 127  GLY B C   1 
ATOM   4132 O  O   . GLY B 1 138 ? 69.449  70.316  89.639  1.00 27.18 ? 127  GLY B O   1 
ATOM   4133 N  N   . PRO B 1 139 ? 67.809  71.452  88.623  1.00 28.57 ? 128  PRO B N   1 
ATOM   4134 C  CA  . PRO B 1 139 ? 68.229  70.991  87.298  1.00 28.57 ? 128  PRO B CA  1 
ATOM   4135 C  C   . PRO B 1 139 ? 69.640  71.442  86.953  1.00 28.57 ? 128  PRO B C   1 
ATOM   4136 O  O   . PRO B 1 139 ? 70.152  72.439  87.464  1.00 28.57 ? 128  PRO B O   1 
ATOM   4137 C  CB  . PRO B 1 139 ? 67.197  71.628  86.363  1.00 28.57 ? 128  PRO B CB  1 
ATOM   4138 C  CG  . PRO B 1 139 ? 66.018  71.887  87.231  1.00 28.57 ? 128  PRO B CG  1 
ATOM   4139 C  CD  . PRO B 1 139 ? 66.587  72.265  88.553  1.00 28.57 ? 128  PRO B CD  1 
ATOM   4140 N  N   . SER B 1 140 ? 70.275  70.669  86.077  1.00 29.47 ? 129  SER B N   1 
ATOM   4141 C  CA  . SER B 1 140 ? 71.602  70.972  85.565  1.00 29.47 ? 129  SER B CA  1 
ATOM   4142 C  C   . SER B 1 140 ? 71.571  70.884  84.049  1.00 29.47 ? 129  SER B C   1 
ATOM   4143 O  O   . SER B 1 140 ? 70.735  70.187  83.473  1.00 29.47 ? 129  SER B O   1 
ATOM   4144 C  CB  . SER B 1 140 ? 72.652  70.009  86.115  1.00 29.47 ? 129  SER B CB  1 
ATOM   4145 O  OG  . SER B 1 140 ? 72.534  69.876  87.518  1.00 29.47 ? 129  SER B OG  1 
ATOM   4146 N  N   . TYR B 1 141 ? 72.483  71.610  83.402  1.00 28.76 ? 130  TYR B N   1 
ATOM   4147 C  CA  . TYR B 1 141 ? 72.510  71.619  81.945  1.00 28.76 ? 130  TYR B CA  1 
ATOM   4148 C  C   . TYR B 1 141 ? 73.138  70.357  81.379  1.00 28.76 ? 130  TYR B C   1 
ATOM   4149 O  O   . TYR B 1 141 ? 72.735  69.900  80.306  1.00 28.76 ? 130  TYR B O   1 
ATOM   4150 C  CB  . TYR B 1 141 ? 73.267  72.844  81.435  1.00 28.76 ? 130  TYR B CB  1 
ATOM   4151 C  CG  . TYR B 1 141 ? 72.570  74.158  81.700  1.00 28.76 ? 130  TYR B CG  1 
ATOM   4152 C  CD1 . TYR B 1 141 ? 71.188  74.245  81.737  1.00 28.76 ? 130  TYR B CD1 1 
ATOM   4153 C  CD2 . TYR B 1 141 ? 73.299  75.313  81.913  1.00 28.76 ? 130  TYR B CD2 1 
ATOM   4154 C  CE1 . TYR B 1 141 ? 70.560  75.438  81.981  1.00 28.76 ? 130  TYR B CE1 1 
ATOM   4155 C  CE2 . TYR B 1 141 ? 72.677  76.511  82.153  1.00 28.76 ? 130  TYR B CE2 1 
ATOM   4156 C  CZ  . TYR B 1 141 ? 71.309  76.568  82.189  1.00 28.76 ? 130  TYR B CZ  1 
ATOM   4157 O  OH  . TYR B 1 141 ? 70.685  77.766  82.428  1.00 28.76 ? 130  TYR B OH  1 
ATOM   4158 N  N   . ALA B 1 142 ? 74.114  69.780  82.079  1.00 32.31 ? 131  ALA B N   1 
ATOM   4159 C  CA  . ALA B 1 142 ? 74.756  68.571  81.580  1.00 32.31 ? 131  ALA B CA  1 
ATOM   4160 C  C   . ALA B 1 142 ? 73.768  67.416  81.499  1.00 32.31 ? 131  ALA B C   1 
ATOM   4161 O  O   . ALA B 1 142 ? 73.831  66.604  80.573  1.00 32.31 ? 131  ALA B O   1 
ATOM   4162 C  CB  . ALA B 1 142 ? 75.939  68.203  82.470  1.00 32.31 ? 131  ALA B CB  1 
ATOM   4163 N  N   . LYS B 1 143 ? 72.846  67.324  82.457  1.00 32.33 ? 132  LYS B N   1 
ATOM   4164 C  CA  . LYS B 1 143 ? 71.861  66.252  82.437  1.00 32.33 ? 132  LYS B CA  1 
ATOM   4165 C  C   . LYS B 1 143 ? 70.958  66.319  81.217  1.00 32.33 ? 132  LYS B C   1 
ATOM   4166 O  O   . LYS B 1 143 ? 70.440  65.284  80.792  1.00 32.33 ? 132  LYS B O   1 
ATOM   4167 C  CB  . LYS B 1 143 ? 71.017  66.296  83.709  1.00 32.33 ? 132  LYS B CB  1 
ATOM   4168 C  CG  . LYS B 1 143 ? 71.825  66.095  84.974  1.00 32.33 ? 132  LYS B CG  1 
ATOM   4169 C  CD  . LYS B 1 143 ? 71.911  64.635  85.352  1.00 32.33 ? 132  LYS B CD  1 
ATOM   4170 C  CE  . LYS B 1 143 ? 72.519  64.456  86.723  1.00 32.33 ? 132  LYS B CE  1 
ATOM   4171 N  NZ  . LYS B 1 143 ? 73.882  63.881  86.647  1.00 32.33 ? 132  LYS B NZ  1 
ATOM   4172 N  N   . LEU B 1 144 ? 70.794  67.497  80.618  1.00 35.17 ? 133  LEU B N   1 
ATOM   4173 C  CA  . LEU B 1 144 ? 70.063  67.582  79.361  1.00 35.17 ? 133  LEU B CA  1 
ATOM   4174 C  C   . LEU B 1 144 ? 70.759  66.759  78.288  1.00 35.17 ? 133  LEU B C   1 
ATOM   4175 O  O   . LEU B 1 144 ? 70.101  66.075  77.495  1.00 35.17 ? 133  LEU B O   1 
ATOM   4176 C  CB  . LEU B 1 144 ? 69.942  69.045  78.937  1.00 35.17 ? 133  LEU B CB  1 
ATOM   4177 C  CG  . LEU B 1 144 ? 69.298  69.373  77.592  1.00 35.17 ? 133  LEU B CG  1 
ATOM   4178 C  CD1 . LEU B 1 144 ? 68.035  68.569  77.357  1.00 35.17 ? 133  LEU B CD1 1 
ATOM   4179 C  CD2 . LEU B 1 144 ? 69.011  70.858  77.526  1.00 35.17 ? 133  LEU B CD2 1 
ATOM   4180 N  N   . GLY B 1 145 ? 72.092  66.783  78.275  1.00 37.65 ? 134  GLY B N   1 
ATOM   4181 C  CA  . GLY B 1 145 ? 72.832  65.935  77.362  1.00 37.65 ? 134  GLY B CA  1 
ATOM   4182 C  C   . GLY B 1 145 ? 72.490  64.468  77.508  1.00 37.65 ? 134  GLY B C   1 
ATOM   4183 O  O   . GLY B 1 145 ? 72.544  63.718  76.532  1.00 37.65 ? 134  GLY B O   1 
ATOM   4184 N  N   . ASP B 1 146 ? 72.132  64.033  78.717  1.00 38.99 ? 135  ASP B N   1 
ATOM   4185 C  CA  . ASP B 1 146 ? 71.645  62.667  78.872  1.00 38.99 ? 135  ASP B CA  1 
ATOM   4186 C  C   . ASP B 1 146 ? 70.377  62.460  78.056  1.00 38.99 ? 135  ASP B C   1 
ATOM   4187 O  O   . ASP B 1 146 ? 70.296  61.548  77.224  1.00 38.99 ? 135  ASP B O   1 
ATOM   4188 C  CB  . ASP B 1 146 ? 71.385  62.360  80.346  1.00 38.99 ? 135  ASP B CB  1 
ATOM   4189 C  CG  . ASP B 1 146 ? 72.643  62.400  81.180  1.00 38.99 ? 135  ASP B CG  1 
ATOM   4190 O  OD1 . ASP B 1 146 ? 73.642  62.985  80.720  1.00 38.99 ? 135  ASP B OD1 1 
ATOM   4191 O  OD2 . ASP B 1 146 ? 72.633  61.853  82.302  1.00 38.99 ? 135  ASP B OD2 1 
ATOM   4192 N  N   . PHE B 1 147 ? 69.391  63.338  78.250  1.00 39.07 ? 136  PHE B N   1 
ATOM   4193 C  CA  . PHE B 1 147 ? 68.104  63.193  77.583  1.00 39.07 ? 136  PHE B CA  1 
ATOM   4194 C  C   . PHE B 1 147 ? 68.286  63.052  76.080  1.00 39.07 ? 136  PHE B C   1 
ATOM   4195 O  O   . PHE B 1 147 ? 67.805  62.092  75.469  1.00 39.07 ? 136  PHE B O   1 
ATOM   4196 C  CB  . PHE B 1 147 ? 67.226  64.400  77.921  1.00 39.07 ? 136  PHE B CB  1 
ATOM   4197 C  CG  . PHE B 1 147 ? 65.948  64.477  77.138  1.00 39.07 ? 136  PHE B CG  1 
ATOM   4198 C  CD1 . PHE B 1 147 ? 65.031  63.447  77.170  1.00 39.07 ? 136  PHE B CD1 1 
ATOM   4199 C  CD2 . PHE B 1 147 ? 65.652  65.598  76.392  1.00 39.07 ? 136  PHE B CD2 1 
ATOM   4200 C  CE1 . PHE B 1 147 ? 63.857  63.530  76.461  1.00 39.07 ? 136  PHE B CE1 1 
ATOM   4201 C  CE2 . PHE B 1 147 ? 64.481  65.680  75.683  1.00 39.07 ? 136  PHE B CE2 1 
ATOM   4202 C  CZ  . PHE B 1 147 ? 63.584  64.646  75.719  1.00 39.07 ? 136  PHE B CZ  1 
ATOM   4203 N  N   . VAL B 1 148 ? 69.035  63.977  75.477  1.00 42.16 ? 137  VAL B N   1 
ATOM   4204 C  CA  . VAL B 1 148 ? 69.247  63.938  74.034  1.00 42.16 ? 137  VAL B CA  1 
ATOM   4205 C  C   . VAL B 1 148 ? 69.808  62.587  73.623  1.00 42.16 ? 137  VAL B C   1 
ATOM   4206 O  O   . VAL B 1 148 ? 69.349  61.978  72.649  1.00 42.16 ? 137  VAL B O   1 
ATOM   4207 C  CB  . VAL B 1 148 ? 70.168  65.092  73.600  1.00 42.16 ? 137  VAL B CB  1 
ATOM   4208 C  CG1 . VAL B 1 148 ? 70.725  64.834  72.215  1.00 42.16 ? 137  VAL B CG1 1 
ATOM   4209 C  CG2 . VAL B 1 148 ? 69.412  66.405  73.633  1.00 42.16 ? 137  VAL B CG2 1 
ATOM   4210 N  N   . ALA B 1 149 ? 70.792  62.082  74.368  1.00 44.31 ? 138  ALA B N   1 
ATOM   4211 C  CA  . ALA B 1 149 ? 71.336  60.768  74.052  1.00 44.31 ? 138  ALA B CA  1 
ATOM   4212 C  C   . ALA B 1 149 ? 70.231  59.722  74.042  1.00 44.31 ? 138  ALA B C   1 
ATOM   4213 O  O   . ALA B 1 149 ? 70.047  59.005  73.052  1.00 44.31 ? 138  ALA B O   1 
ATOM   4214 C  CB  . ALA B 1 149 ? 72.427  60.396  75.054  1.00 44.31 ? 138  ALA B CB  1 
ATOM   4215 N  N   . ALA B 1 150 ? 69.446  59.659  75.119  1.00 45.21 ? 139  ALA B N   1 
ATOM   4216 C  CA  . ALA B 1 150 ? 68.369  58.680  75.178  1.00 45.21 ? 139  ALA B CA  1 
ATOM   4217 C  C   . ALA B 1 150 ? 67.392  58.869  74.033  1.00 45.21 ? 139  ALA B C   1 
ATOM   4218 O  O   . ALA B 1 150 ? 66.732  57.913  73.614  1.00 45.21 ? 139  ALA B O   1 
ATOM   4219 C  CB  . ALA B 1 150 ? 67.639  58.778  76.516  1.00 45.21 ? 139  ALA B CB  1 
ATOM   4220 N  N   . LEU B 1 151 ? 67.280  60.093  73.519  1.00 46.37 ? 140  LEU B N   1 
ATOM   4221 C  CA  . LEU B 1 151 ? 66.415  60.333  72.371  1.00 46.37 ? 140  LEU B CA  1 
ATOM   4222 C  C   . LEU B 1 151 ? 67.015  59.729  71.109  1.00 46.37 ? 140  LEU B C   1 
ATOM   4223 O  O   . LEU B 1 151 ? 66.331  59.019  70.362  1.00 46.37 ? 140  LEU B O   1 
ATOM   4224 C  CB  . LEU B 1 151 ? 66.185  61.835  72.207  1.00 46.37 ? 140  LEU B CB  1 
ATOM   4225 C  CG  . LEU B 1 151 ? 65.101  62.297  71.237  1.00 46.37 ? 140  LEU B CG  1 
ATOM   4226 C  CD1 . LEU B 1 151 ? 63.741  61.764  71.634  1.00 46.37 ? 140  LEU B CD1 1 
ATOM   4227 C  CD2 . LEU B 1 151 ? 65.083  63.808  71.189  1.00 46.37 ? 140  LEU B CD2 1 
ATOM   4228 N  N   . HIS B 1 152 ? 68.307  59.967  70.872  1.00 49.84 ? 141  HIS B N   1 
ATOM   4229 C  CA  . HIS B 1 152 ? 68.923  59.506  69.633  1.00 49.84 ? 141  HIS B CA  1 
ATOM   4230 C  C   . HIS B 1 152 ? 68.827  57.993  69.508  1.00 49.84 ? 141  HIS B C   1 
ATOM   4231 O  O   . HIS B 1 152 ? 68.400  57.468  68.473  1.00 49.84 ? 141  HIS B O   1 
ATOM   4232 C  CB  . HIS B 1 152 ? 70.380  59.955  69.572  1.00 49.84 ? 141  HIS B CB  1 
ATOM   4233 C  CG  . HIS B 1 152 ? 70.569  61.323  68.998  1.00 49.84 ? 141  HIS B CG  1 
ATOM   4234 N  ND1 . HIS B 1 152 ? 71.466  61.586  67.987  1.00 49.84 ? 141  HIS B ND1 1 
ATOM   4235 C  CD2 . HIS B 1 152 ? 69.981  62.505  69.295  1.00 49.84 ? 141  HIS B CD2 1 
ATOM   4236 C  CE1 . HIS B 1 152 ? 71.422  62.870  67.685  1.00 49.84 ? 141  HIS B CE1 1 
ATOM   4237 N  NE2 . HIS B 1 152 ? 70.528  63.450  68.464  1.00 49.84 ? 141  HIS B NE2 1 
ATOM   4238 N  N   . ARG B 1 153 ? 69.197  57.273  70.569  1.00 51.02 ? 142  ARG B N   1 
ATOM   4239 C  CA  . ARG B 1 153 ? 69.105  55.819  70.536  1.00 51.02 ? 142  ARG B CA  1 
ATOM   4240 C  C   . ARG B 1 153 ? 67.705  55.373  70.148  1.00 51.02 ? 142  ARG B C   1 
ATOM   4241 O  O   . ARG B 1 153 ? 67.533  54.370  69.448  1.00 51.02 ? 142  ARG B O   1 
ATOM   4242 C  CB  . ARG B 1 153 ? 69.488  55.231  71.895  1.00 51.02 ? 142  ARG B CB  1 
ATOM   4243 C  CG  . ARG B 1 153 ? 70.956  55.387  72.258  1.00 51.02 ? 142  ARG B CG  1 
ATOM   4244 C  CD  . ARG B 1 153 ? 71.328  54.502  73.437  1.00 51.02 ? 142  ARG B CD  1 
ATOM   4245 N  NE  . ARG B 1 153 ? 70.661  54.896  74.676  1.00 51.02 ? 142  ARG B NE  1 
ATOM   4246 C  CZ  . ARG B 1 153 ? 71.165  55.738  75.574  1.00 51.02 ? 142  ARG B CZ  1 
ATOM   4247 N  NH1 . ARG B 1 153 ? 72.356  56.294  75.388  1.00 51.02 ? 142  ARG B NH1 1 
ATOM   4248 N  NH2 . ARG B 1 153 ? 70.474  56.024  76.669  1.00 51.02 ? 142  ARG B NH2 1 
ATOM   4249 N  N   . ARG B 1 154 ? 66.687  56.115  70.586  1.00 50.84 ? 143  ARG B N   1 
ATOM   4250 C  CA  . ARG B 1 154 ? 65.317  55.721  70.285  1.00 50.84 ? 143  ARG B CA  1 
ATOM   4251 C  C   . ARG B 1 154 ? 65.015  55.858  68.801  1.00 50.84 ? 143  ARG B C   1 
ATOM   4252 O  O   . ARG B 1 154 ? 64.310  55.021  68.227  1.00 50.84 ? 143  ARG B O   1 
ATOM   4253 C  CB  . ARG B 1 154 ? 64.342  56.560  71.104  1.00 50.84 ? 143  ARG B CB  1 
ATOM   4254 C  CG  . ARG B 1 154 ? 62.919  56.048  71.082  1.00 50.84 ? 143  ARG B CG  1 
ATOM   4255 C  CD  . ARG B 1 154 ? 62.094  56.704  72.169  1.00 50.84 ? 143  ARG B CD  1 
ATOM   4256 N  NE  . ARG B 1 154 ? 60.664  56.672  71.868  1.00 50.84 ? 143  ARG B NE  1 
ATOM   4257 C  CZ  . ARG B 1 154 ? 59.757  55.969  72.540  1.00 50.84 ? 143  ARG B CZ  1 
ATOM   4258 N  NH1 . ARG B 1 154 ? 60.105  55.212  73.573  1.00 50.84 ? 143  ARG B NH1 1 
ATOM   4259 N  NH2 . ARG B 1 154 ? 58.486  56.023  72.173  1.00 50.84 ? 143  ARG B NH2 1 
ATOM   4260 N  N   . LEU B 1 155 ? 65.541  56.902  68.161  1.00 53.59 ? 144  LEU B N   1 
ATOM   4261 C  CA  . LEU B 1 155 ? 65.165  57.248  66.797  1.00 53.59 ? 144  LEU B CA  1 
ATOM   4262 C  C   . LEU B 1 155 ? 66.254  56.926  65.783  1.00 53.59 ? 144  LEU B C   1 
ATOM   4263 O  O   . LEU B 1 155 ? 66.130  57.303  64.614  1.00 53.59 ? 144  LEU B O   1 
ATOM   4264 C  CB  . LEU B 1 155 ? 64.795  58.730  66.724  1.00 53.59 ? 144  LEU B CB  1 
ATOM   4265 C  CG  . LEU B 1 155 ? 63.781  59.193  67.773  1.00 53.59 ? 144  LEU B CG  1 
ATOM   4266 C  CD1 . LEU B 1 155 ? 63.831  60.697  67.951  1.00 53.59 ? 144  LEU B CD1 1 
ATOM   4267 C  CD2 . LEU B 1 155 ? 62.382  58.743  67.396  1.00 53.59 ? 144  LEU B CD2 1 
ATOM   4268 N  N   . GLY B 1 156 ? 67.312  56.237  66.196  1.00 55.71 ? 145  GLY B N   1 
ATOM   4269 C  CA  . GLY B 1 156 ? 68.336  55.816  65.255  1.00 55.71 ? 145  GLY B CA  1 
ATOM   4270 C  C   . GLY B 1 156 ? 69.065  56.956  64.580  1.00 55.71 ? 145  GLY B C   1 
ATOM   4271 O  O   . GLY B 1 156 ? 69.354  56.880  63.380  1.00 55.71 ? 145  GLY B O   1 
ATOM   4272 N  N   . TRP B 1 157 ? 69.371  58.014  65.323  1.00 55.91 ? 146  TRP B N   1 
ATOM   4273 C  CA  . TRP B 1 157 ? 70.214  59.101  64.839  1.00 55.91 ? 146  TRP B CA  1 
ATOM   4274 C  C   . TRP B 1 157 ? 71.597  58.904  65.444  1.00 55.91 ? 146  TRP B C   1 
ATOM   4275 O  O   . TRP B 1 157 ? 71.783  59.083  66.652  1.00 55.91 ? 146  TRP B O   1 
ATOM   4276 C  CB  . TRP B 1 157 ? 69.636  60.462  65.213  1.00 55.91 ? 146  TRP B CB  1 
ATOM   4277 C  CG  . TRP B 1 157 ? 68.342  60.770  64.541  1.00 55.91 ? 146  TRP B CG  1 
ATOM   4278 C  CD1 . TRP B 1 157 ? 67.936  60.348  63.313  1.00 55.91 ? 146  TRP B CD1 1 
ATOM   4279 C  CD2 . TRP B 1 157 ? 67.282  61.576  65.060  1.00 55.91 ? 146  TRP B CD2 1 
ATOM   4280 N  NE1 . TRP B 1 157 ? 66.685  60.837  63.034  1.00 55.91 ? 146  TRP B NE1 1 
ATOM   4281 C  CE2 . TRP B 1 157 ? 66.262  61.596  64.091  1.00 55.91 ? 146  TRP B CE2 1 
ATOM   4282 C  CE3 . TRP B 1 157 ? 67.095  62.281  66.251  1.00 55.91 ? 146  TRP B CE3 1 
ATOM   4283 C  CZ2 . TRP B 1 157 ? 65.074  62.292  64.277  1.00 55.91 ? 146  TRP B CZ2 1 
ATOM   4284 C  CZ3 . TRP B 1 157 ? 65.919  62.970  66.432  1.00 55.91 ? 146  TRP B CZ3 1 
ATOM   4285 C  CH2 . TRP B 1 157 ? 64.922  62.972  65.451  1.00 55.91 ? 146  TRP B CH2 1 
ATOM   4286 N  N   . GLU B 1 158 ? 72.565  58.537  64.605  1.00 60.80 ? 147  GLU B N   1 
ATOM   4287 C  CA  . GLU B 1 158 ? 73.867  58.096  65.084  1.00 60.80 ? 147  GLU B CA  1 
ATOM   4288 C  C   . GLU B 1 158 ? 75.026  58.732  64.330  1.00 60.80 ? 147  GLU B C   1 
ATOM   4289 O  O   . GLU B 1 158 ? 76.163  58.269  64.474  1.00 60.80 ? 147  GLU B O   1 
ATOM   4290 C  CB  . GLU B 1 158 ? 73.960  56.571  64.980  1.00 60.80 ? 147  GLU B CB  1 
ATOM   4291 C  CG  . GLU B 1 158 ? 73.018  55.844  65.920  1.00 60.80 ? 147  GLU B CG  1 
ATOM   4292 C  CD  . GLU B 1 158 ? 73.108  54.342  65.788  1.00 60.80 ? 147  GLU B CD  1 
ATOM   4293 O  OE1 . GLU B 1 158 ? 73.815  53.868  64.875  1.00 60.80 ? 147  GLU B OE1 1 
ATOM   4294 O  OE2 . GLU B 1 158 ? 72.474  53.635  66.600  1.00 60.80 ? 147  GLU B OE2 1 
ATOM   4295 N  N   . ARG B 1 159 ? 74.782  59.779  63.546  1.00 62.48 ? 148  ARG B N   1 
ATOM   4296 C  CA  . ARG B 1 159 ? 75.792  60.303  62.636  1.00 62.48 ? 148  ARG B CA  1 
ATOM   4297 C  C   . ARG B 1 159 ? 76.209  61.733  62.943  1.00 62.48 ? 148  ARG B C   1 
ATOM   4298 O  O   . ARG B 1 159 ? 77.406  61.990  63.107  1.00 62.48 ? 148  ARG B O   1 
ATOM   4299 C  CB  . ARG B 1 159 ? 75.279  60.195  61.192  1.00 62.48 ? 148  ARG B CB  1 
ATOM   4300 C  CG  . ARG B 1 159 ? 75.362  58.780  60.634  1.00 62.48 ? 148  ARG B CG  1 
ATOM   4301 C  CD  . ARG B 1 159 ? 74.761  58.674  59.243  1.00 62.48 ? 148  ARG B CD  1 
ATOM   4302 N  NE  . ARG B 1 159 ? 73.337  58.354  59.294  1.00 62.48 ? 148  ARG B NE  1 
ATOM   4303 C  CZ  . ARG B 1 159 ? 72.661  57.783  58.303  1.00 62.48 ? 148  ARG B CZ  1 
ATOM   4304 N  NH1 . ARG B 1 159 ? 71.367  57.529  58.441  1.00 62.48 ? 148  ARG B NH1 1 
ATOM   4305 N  NH2 . ARG B 1 159 ? 73.278  57.462  57.174  1.00 62.48 ? 148  ARG B NH2 1 
ATOM   4306 N  N   . GLN B 1 160 ? 75.273  62.677  63.030  1.00 57.90 ? 149  GLN B N   1 
ATOM   4307 C  CA  . GLN B 1 160 ? 75.669  64.076  63.155  1.00 57.90 ? 149  GLN B CA  1 
ATOM   4308 C  C   . GLN B 1 160 ? 74.536  64.903  63.749  1.00 57.90 ? 149  GLN B C   1 
ATOM   4309 O  O   . GLN B 1 160 ? 73.366  64.518  63.701  1.00 57.90 ? 149  GLN B O   1 
ATOM   4310 C  CB  . GLN B 1 160 ? 76.091  64.642  61.798  1.00 57.90 ? 149  GLN B CB  1 
ATOM   4311 C  CG  . GLN B 1 160 ? 76.719  66.017  61.864  1.00 57.90 ? 149  GLN B CG  1 
ATOM   4312 C  CD  . GLN B 1 160 ? 77.266  66.460  60.532  1.00 57.90 ? 149  GLN B CD  1 
ATOM   4313 O  OE1 . GLN B 1 160 ? 77.151  65.748  59.538  1.00 57.90 ? 149  GLN B OE1 1 
ATOM   4314 N  NE2 . GLN B 1 160 ? 77.865  67.643  60.500  1.00 57.90 ? 149  GLN B NE2 1 
ATOM   4315 N  N   . ALA B 1 161 ? 74.911  66.057  64.304  1.00 52.88 ? 150  ALA B N   1 
ATOM   4316 C  CA  . ALA B 1 161 ? 73.955  66.973  64.913  1.00 52.88 ? 150  ALA B CA  1 
ATOM   4317 C  C   . ALA B 1 161 ? 74.533  68.385  64.939  1.00 52.88 ? 150  ALA B C   1 
ATOM   4318 O  O   . ALA B 1 161 ? 75.753  68.577  64.956  1.00 52.88 ? 150  ALA B O   1 
ATOM   4319 C  CB  . ALA B 1 161 ? 73.587  66.527  66.332  1.00 52.88 ? 150  ALA B CB  1 
ATOM   4320 N  N   . LEU B 1 162 ? 73.635  69.369  64.961  1.00 49.79 ? 151  LEU B N   1 
ATOM   4321 C  CA  . LEU B 1 162 ? 73.998  70.780  64.958  1.00 49.79 ? 151  LEU B CA  1 
ATOM   4322 C  C   . LEU B 1 162 ? 73.297  71.482  66.113  1.00 49.79 ? 151  LEU B C   1 
ATOM   4323 O  O   . LEU B 1 162 ? 72.128  71.203  66.396  1.00 49.79 ? 151  LEU B O   1 
ATOM   4324 C  CB  . LEU B 1 162 ? 73.616  71.435  63.623  1.00 49.79 ? 151  LEU B CB  1 
ATOM   4325 C  CG  . LEU B 1 162 ? 73.887  72.931  63.463  1.00 49.79 ? 151  LEU B CG  1 
ATOM   4326 C  CD1 . LEU B 1 162 ? 75.372  73.188  63.318  1.00 49.79 ? 151  LEU B CD1 1 
ATOM   4327 C  CD2 . LEU B 1 162 ? 73.137  73.482  62.267  1.00 49.79 ? 151  LEU B CD2 1 
ATOM   4328 N  N   . MET B 1 163 ? 74.006  72.396  66.776  1.00 45.07 ? 152  MET B N   1 
ATOM   4329 C  CA  . MET B 1 163 ? 73.490  73.077  67.958  1.00 45.07 ? 152  MET B CA  1 
ATOM   4330 C  C   . MET B 1 163 ? 73.716  74.574  67.830  1.00 45.07 ? 152  MET B C   1 
ATOM   4331 O  O   . MET B 1 163 ? 74.862  75.034  67.815  1.00 45.07 ? 152  MET B O   1 
ATOM   4332 C  CB  . MET B 1 163 ? 74.156  72.541  69.224  1.00 45.07 ? 152  MET B CB  1 
ATOM   4333 C  CG  . MET B 1 163 ? 73.780  71.112  69.518  1.00 45.07 ? 152  MET B CG  1 
ATOM   4334 S  SD  . MET B 1 163 ? 74.556  70.457  70.996  1.00 45.07 ? 152  MET B SD  1 
ATOM   4335 C  CE  . MET B 1 163 ? 73.949  68.778  70.932  1.00 45.07 ? 152  MET B CE  1 
ATOM   4336 N  N   . LEU B 1 164 ? 72.624  75.330  67.781  1.00 46.51 ? 153  LEU B N   1 
ATOM   4337 C  CA  . LEU B 1 164 ? 72.650  76.771  67.593  1.00 46.51 ? 153  LEU B CA  1 
ATOM   4338 C  C   . LEU B 1 164 ? 72.231  77.453  68.885  1.00 46.51 ? 153  LEU B C   1 
ATOM   4339 O  O   . LEU B 1 164 ? 71.230  77.065  69.499  1.00 46.51 ? 153  LEU B O   1 
ATOM   4340 C  CB  . LEU B 1 164 ? 71.707  77.187  66.465  1.00 46.51 ? 153  LEU B CB  1 
ATOM   4341 C  CG  . LEU B 1 164 ? 71.859  76.423  65.151  1.00 46.51 ? 153  LEU B CG  1 
ATOM   4342 C  CD1 . LEU B 1 164 ? 70.595  76.522  64.323  1.00 46.51 ? 153  LEU B CD1 1 
ATOM   4343 C  CD2 . LEU B 1 164 ? 73.058  76.906  64.381  1.00 46.51 ? 153  LEU B CD2 1 
ATOM   4344 N  N   . TYR B 1 165 ? 72.988  78.465  69.295  1.00 43.53 ? 154  TYR B N   1 
ATOM   4345 C  CA  . TYR B 1 165 ? 72.598  79.283  70.432  1.00 43.53 ? 154  TYR B CA  1 
ATOM   4346 C  C   . TYR B 1 165 ? 72.621  80.757  70.057  1.00 43.53 ? 154  TYR B C   1 
ATOM   4347 O  O   . TYR B 1 165 ? 73.460  81.202  69.268  1.00 43.53 ? 154  TYR B O   1 
ATOM   4348 C  CB  . TYR B 1 165 ? 73.485  79.029  71.655  1.00 43.53 ? 154  TYR B CB  1 
ATOM   4349 C  CG  . TYR B 1 165 ? 74.972  79.091  71.428  1.00 43.53 ? 154  TYR B CG  1 
ATOM   4350 C  CD1 . TYR B 1 165 ? 75.668  77.989  70.968  1.00 43.53 ? 154  TYR B CD1 1 
ATOM   4351 C  CD2 . TYR B 1 165 ? 75.686  80.241  71.715  1.00 43.53 ? 154  TYR B CD2 1 
ATOM   4352 C  CE1 . TYR B 1 165 ? 77.028  78.037  70.778  1.00 43.53 ? 154  TYR B CE1 1 
ATOM   4353 C  CE2 . TYR B 1 165 ? 77.045  80.297  71.529  1.00 43.53 ? 154  TYR B CE2 1 
ATOM   4354 C  CZ  . TYR B 1 165 ? 77.712  79.193  71.063  1.00 43.53 ? 154  TYR B CZ  1 
ATOM   4355 O  OH  . TYR B 1 165 ? 79.071  79.249  70.875  1.00 43.53 ? 154  TYR B OH  1 
ATOM   4356 N  N   . ALA B 1 166 ? 71.681  81.498  70.626  1.00 47.03 ? 155  ALA B N   1 
ATOM   4357 C  CA  . ALA B 1 166 ? 71.517  82.919  70.378  1.00 47.03 ? 155  ALA B CA  1 
ATOM   4358 C  C   . ALA B 1 166 ? 72.230  83.730  71.450  1.00 47.03 ? 155  ALA B C   1 
ATOM   4359 O  O   . ALA B 1 166 ? 72.498  83.250  72.553  1.00 47.03 ? 155  ALA B O   1 
ATOM   4360 C  CB  . ALA B 1 166 ? 70.035  83.287  70.346  1.00 47.03 ? 155  ALA B CB  1 
ATOM   4361 N  N   . TYR B 1 167 ? 72.541  84.975  71.107  1.00 51.83 ? 156  TYR B N   1 
ATOM   4362 C  CA  . TYR B 1 167 ? 73.233  85.884  72.009  1.00 51.83 ? 156  TYR B CA  1 
ATOM   4363 C  C   . TYR B 1 167 ? 72.418  87.158  72.180  1.00 51.83 ? 156  TYR B C   1 
ATOM   4364 O  O   . TYR B 1 167 ? 71.972  87.750  71.193  1.00 51.83 ? 156  TYR B O   1 
ATOM   4365 C  CB  . TYR B 1 167 ? 74.628  86.217  71.480  1.00 51.83 ? 156  TYR B CB  1 
ATOM   4366 C  CG  . TYR B 1 167 ? 75.236  87.438  72.120  1.00 51.83 ? 156  TYR B CG  1 
ATOM   4367 C  CD1 . TYR B 1 167 ? 75.786  87.373  73.391  1.00 51.83 ? 156  TYR B CD1 1 
ATOM   4368 C  CD2 . TYR B 1 167 ? 75.252  88.656  71.461  1.00 51.83 ? 156  TYR B CD2 1 
ATOM   4369 C  CE1 . TYR B 1 167 ? 76.341  88.487  73.985  1.00 51.83 ? 156  TYR B CE1 1 
ATOM   4370 C  CE2 . TYR B 1 167 ? 75.802  89.777  72.047  1.00 51.83 ? 156  TYR B CE2 1 
ATOM   4371 C  CZ  . TYR B 1 167 ? 76.345  89.687  73.309  1.00 51.83 ? 156  TYR B CZ  1 
ATOM   4372 O  OH  . TYR B 1 167 ? 76.895  90.803  73.897  1.00 51.83 ? 156  TYR B OH  1 
ATOM   4373 N  N   . ARG B 1 168 ? 72.221  87.571  73.429  1.00 53.32 ? 157  ARG B N   1 
ATOM   4374 C  CA  . ARG B 1 168 ? 71.605  88.843  73.767  1.00 53.32 ? 157  ARG B CA  1 
ATOM   4375 C  C   . ARG B 1 168 ? 72.468  89.595  74.768  1.00 53.32 ? 157  ARG B C   1 
ATOM   4376 O  O   . ARG B 1 168 ? 73.106  88.980  75.627  1.00 53.32 ? 157  ARG B O   1 
ATOM   4377 C  CB  . ARG B 1 168 ? 70.208  88.665  74.375  1.00 53.32 ? 157  ARG B CB  1 
ATOM   4378 C  CG  . ARG B 1 168 ? 69.172  88.079  73.455  1.00 53.32 ? 157  ARG B CG  1 
ATOM   4379 C  CD  . ARG B 1 168 ? 67.875  87.870  74.217  1.00 53.32 ? 157  ARG B CD  1 
ATOM   4380 N  NE  . ARG B 1 168 ? 67.290  89.122  74.680  1.00 53.32 ? 157  ARG B NE  1 
ATOM   4381 C  CZ  . ARG B 1 168 ? 66.221  89.201  75.465  1.00 53.32 ? 157  ARG B CZ  1 
ATOM   4382 N  NH1 . ARG B 1 168 ? 65.610  88.099  75.877  1.00 53.32 ? 157  ARG B NH1 1 
ATOM   4383 N  NH2 . ARG B 1 168 ? 65.760  90.387  75.838  1.00 53.32 ? 157  ARG B NH2 1 
ATOM   4384 N  N   . PRO B 1 169 ? 72.501  90.927  74.689  1.00 53.27 ? 158  PRO B N   1 
ATOM   4385 C  CA  . PRO B 1 169 ? 73.202  91.697  75.727  1.00 53.27 ? 158  PRO B CA  1 
ATOM   4386 C  C   . PRO B 1 169 ? 72.629  91.511  77.121  1.00 53.27 ? 158  PRO B C   1 
ATOM   4387 O  O   . PRO B 1 169 ? 73.380  91.562  78.102  1.00 53.27 ? 158  PRO B O   1 
ATOM   4388 C  CB  . PRO B 1 169 ? 73.039  93.144  75.243  1.00 53.27 ? 158  PRO B CB  1 
ATOM   4389 C  CG  . PRO B 1 169 ? 72.915  93.025  73.776  1.00 53.27 ? 158  PRO B CG  1 
ATOM   4390 C  CD  . PRO B 1 169 ? 72.100  91.786  73.562  1.00 53.27 ? 158  PRO B CD  1 
ATOM   4391 N  N   . GLY B 1 170 ? 71.322  91.303  77.240  1.00 50.19 ? 159  GLY B N   1 
ATOM   4392 C  CA  . GLY B 1 170 ? 70.670  91.292  78.534  1.00 50.19 ? 159  GLY B CA  1 
ATOM   4393 C  C   . GLY B 1 170 ? 70.884  90.029  79.339  1.00 50.19 ? 159  GLY B C   1 
ATOM   4394 O  O   . GLY B 1 170 ? 71.451  90.078  80.433  1.00 50.19 ? 159  GLY B O   1 
ATOM   4395 N  N   . ASP B 1 171 ? 70.422  88.894  78.814  1.00 45.64 ? 160  ASP B N   1 
ATOM   4396 C  CA  . ASP B 1 171 ? 70.540  87.633  79.532  1.00 45.64 ? 160  ASP B CA  1 
ATOM   4397 C  C   . ASP B 1 171 ? 71.977  87.417  79.982  1.00 45.64 ? 160  ASP B C   1 
ATOM   4398 O  O   . ASP B 1 171 ? 72.926  87.870  79.338  1.00 45.64 ? 160  ASP B O   1 
ATOM   4399 C  CB  . ASP B 1 171 ? 70.086  86.469  78.648  1.00 45.64 ? 160  ASP B CB  1 
ATOM   4400 C  CG  . ASP B 1 171 ? 70.911  86.336  77.380  1.00 45.64 ? 160  ASP B CG  1 
ATOM   4401 O  OD1 . ASP B 1 171 ? 71.789  87.189  77.140  1.00 45.64 ? 160  ASP B OD1 1 
ATOM   4402 O  OD2 . ASP B 1 171 ? 70.679  85.372  76.621  1.00 45.64 ? 160  ASP B OD2 1 
ATOM   4403 N  N   . GLU B 1 172 ? 72.139  86.717  81.101  1.00 37.64 ? 161  GLU B N   1 
ATOM   4404 C  CA  . GLU B 1 172 ? 73.474  86.496  81.638  1.00 37.64 ? 161  GLU B CA  1 
ATOM   4405 C  C   . GLU B 1 172 ? 74.146  85.349  80.899  1.00 37.64 ? 161  GLU B C   1 
ATOM   4406 O  O   . GLU B 1 172 ? 74.673  84.423  81.521  1.00 37.64 ? 161  GLU B O   1 
ATOM   4407 C  CB  . GLU B 1 172 ? 73.411  86.207  83.137  1.00 37.64 ? 161  GLU B CB  1 
ATOM   4408 N  N   . GLU B 1 173 ? 74.143  85.413  79.569  1.00 35.73 ? 162  GLU B N   1 
ATOM   4409 C  CA  . GLU B 1 173 ? 74.809  84.425  78.730  1.00 35.73 ? 162  GLU B CA  1 
ATOM   4410 C  C   . GLU B 1 173 ? 74.265  83.026  79.030  1.00 35.73 ? 162  GLU B C   1 
ATOM   4411 O  O   . GLU B 1 173 ? 74.985  82.113  79.423  1.00 35.73 ? 162  GLU B O   1 
ATOM   4412 C  CB  . GLU B 1 173 ? 76.324  84.520  78.932  1.00 35.73 ? 162  GLU B CB  1 
ATOM   4413 C  CG  . GLU B 1 173 ? 77.162  83.619  78.070  1.00 35.73 ? 162  GLU B CG  1 
ATOM   4414 C  CD  . GLU B 1 173 ? 78.642  83.833  78.310  1.00 35.73 ? 162  GLU B CD  1 
ATOM   4415 O  OE1 . GLU B 1 173 ? 79.003  84.894  78.859  1.00 35.73 ? 162  GLU B OE1 1 
ATOM   4416 O  OE2 . GLU B 1 173 ? 79.448  82.957  77.938  1.00 35.73 ? 162  GLU B OE2 1 
ATOM   4417 N  N   . HIS B 1 174 ? 72.953  82.883  78.825  1.00 35.76 ? 163  HIS B N   1 
ATOM   4418 C  CA  . HIS B 1 174 ? 72.225  81.684  79.232  1.00 35.76 ? 163  HIS B CA  1 
ATOM   4419 C  C   . HIS B 1 174 ? 72.398  80.546  78.234  1.00 35.76 ? 163  HIS B C   1 
ATOM   4420 O  O   . HIS B 1 174 ? 72.744  79.419  78.614  1.00 35.76 ? 163  HIS B O   1 
ATOM   4421 C  CB  . HIS B 1 174 ? 70.744  82.032  79.398  1.00 35.76 ? 163  HIS B CB  1 
ATOM   4422 C  CG  . HIS B 1 174 ? 69.862  80.854  79.671  1.00 35.76 ? 163  HIS B CG  1 
ATOM   4423 N  ND1 . HIS B 1 174 ? 68.827  80.493  78.836  1.00 35.76 ? 163  HIS B ND1 1 
ATOM   4424 C  CD2 . HIS B 1 174 ? 69.842  79.972  80.696  1.00 35.76 ? 163  HIS B CD2 1 
ATOM   4425 C  CE1 . HIS B 1 174 ? 68.217  79.430  79.328  1.00 35.76 ? 163  HIS B CE1 1 
ATOM   4426 N  NE2 . HIS B 1 174 ? 68.813  79.094  80.457  1.00 35.76 ? 163  HIS B NE2 1 
ATOM   4427 N  N   . CYS B 1 175 ? 72.152  80.816  76.953  1.00 38.49 ? 164  CYS B N   1 
ATOM   4428 C  CA  . CYS B 1 175 ? 72.217  79.750  75.961  1.00 38.49 ? 164  CYS B CA  1 
ATOM   4429 C  C   . CYS B 1 175 ? 73.634  79.272  75.715  1.00 38.49 ? 164  CYS B C   1 
ATOM   4430 O  O   . CYS B 1 175 ? 73.829  78.105  75.368  1.00 38.49 ? 164  CYS B O   1 
ATOM   4431 C  CB  . CYS B 1 175 ? 71.579  80.194  74.655  1.00 38.49 ? 164  CYS B CB  1 
ATOM   4432 S  SG  . CYS B 1 175 ? 69.807  80.175  74.739  1.00 38.49 ? 164  CYS B SG  1 
ATOM   4433 N  N   . PHE B 1 176 ? 74.637  80.129  75.884  1.00 34.85 ? 165  PHE B N   1 
ATOM   4434 C  CA  . PHE B 1 176 ? 75.998  79.627  75.781  1.00 34.85 ? 165  PHE B CA  1 
ATOM   4435 C  C   . PHE B 1 176 ? 76.222  78.501  76.775  1.00 34.85 ? 165  PHE B C   1 
ATOM   4436 O  O   . PHE B 1 176 ? 76.704  77.427  76.409  1.00 34.85 ? 165  PHE B O   1 
ATOM   4437 C  CB  . PHE B 1 176 ? 77.017  80.731  76.017  1.00 34.85 ? 165  PHE B CB  1 
ATOM   4438 C  CG  . PHE B 1 176 ? 78.411  80.210  76.191  1.00 34.85 ? 165  PHE B CG  1 
ATOM   4439 C  CD1 . PHE B 1 176 ? 79.034  79.525  75.168  1.00 34.85 ? 165  PHE B CD1 1 
ATOM   4440 C  CD2 . PHE B 1 176 ? 79.082  80.370  77.384  1.00 34.85 ? 165  PHE B CD2 1 
ATOM   4441 C  CE1 . PHE B 1 176 ? 80.307  79.031  75.324  1.00 34.85 ? 165  PHE B CE1 1 
ATOM   4442 C  CE2 . PHE B 1 176 ? 80.356  79.879  77.545  1.00 34.85 ? 165  PHE B CE2 1 
ATOM   4443 C  CZ  . PHE B 1 176 ? 80.969  79.207  76.514  1.00 34.85 ? 165  PHE B CZ  1 
ATOM   4444 N  N   . PHE B 1 177 ? 75.860  78.721  78.039  1.00 31.10 ? 166  PHE B N   1 
ATOM   4445 C  CA  . PHE B 1 177 ? 76.072  77.694  79.050  1.00 31.10 ? 166  PHE B CA  1 
ATOM   4446 C  C   . PHE B 1 177 ? 75.190  76.480  78.801  1.00 31.10 ? 166  PHE B C   1 
ATOM   4447 O  O   . PHE B 1 177 ? 75.641  75.336  78.944  1.00 31.10 ? 166  PHE B O   1 
ATOM   4448 C  CB  . PHE B 1 177 ? 75.817  78.272  80.439  1.00 31.10 ? 166  PHE B CB  1 
ATOM   4449 C  CG  . PHE B 1 177 ? 76.826  79.297  80.857  1.00 31.10 ? 166  PHE B CG  1 
ATOM   4450 C  CD1 . PHE B 1 177 ? 78.174  79.011  80.838  1.00 31.10 ? 166  PHE B CD1 1 
ATOM   4451 C  CD2 . PHE B 1 177 ? 76.425  80.550  81.263  1.00 31.10 ? 166  PHE B CD2 1 
ATOM   4452 C  CE1 . PHE B 1 177 ? 79.097  79.954  81.216  1.00 31.10 ? 166  PHE B CE1 1 
ATOM   4453 C  CE2 . PHE B 1 177 ? 77.345  81.494  81.641  1.00 31.10 ? 166  PHE B CE2 1 
ATOM   4454 C  CZ  . PHE B 1 177 ? 78.681  81.195  81.619  1.00 31.10 ? 166  PHE B CZ  1 
ATOM   4455 N  N   . LEU B 1 178 ? 73.932  76.702  78.420  1.00 33.24 ? 167  LEU B N   1 
ATOM   4456 C  CA  . LEU B 1 178 ? 73.041  75.576  78.162  1.00 33.24 ? 167  LEU B CA  1 
ATOM   4457 C  C   . LEU B 1 178 ? 73.602  74.677  77.067  1.00 33.24 ? 167  LEU B C   1 
ATOM   4458 O  O   . LEU B 1 178 ? 73.737  73.459  77.249  1.00 33.24 ? 167  LEU B O   1 
ATOM   4459 C  CB  . LEU B 1 178 ? 71.654  76.090  77.786  1.00 33.24 ? 167  LEU B CB  1 
ATOM   4460 C  CG  . LEU B 1 178 ? 70.489  75.116  77.950  1.00 33.24 ? 167  LEU B CG  1 
ATOM   4461 C  CD1 . LEU B 1 178 ? 69.181  75.865  77.948  1.00 33.24 ? 167  LEU B CD1 1 
ATOM   4462 C  CD2 . LEU B 1 178 ? 70.492  74.069  76.863  1.00 33.24 ? 167  LEU B CD2 1 
ATOM   4463 N  N   . VAL B 1 179 ? 73.947  75.263  75.920  1.00 37.91 ? 168  VAL B N   1 
ATOM   4464 C  CA  . VAL B 1 179 ? 74.435  74.463  74.806  1.00 37.91 ? 168  VAL B CA  1 
ATOM   4465 C  C   . VAL B 1 179 ? 75.825  73.920  75.093  1.00 37.91 ? 168  VAL B C   1 
ATOM   4466 O  O   . VAL B 1 179 ? 76.178  72.847  74.606  1.00 37.91 ? 168  VAL B O   1 
ATOM   4467 C  CB  . VAL B 1 179 ? 74.401  75.278  73.504  1.00 37.91 ? 168  VAL B CB  1 
ATOM   4468 C  CG1 . VAL B 1 179 ? 75.022  74.487  72.374  1.00 37.91 ? 168  VAL B CG1 1 
ATOM   4469 C  CG2 . VAL B 1 179 ? 72.972  75.644  73.161  1.00 37.91 ? 168  VAL B CG2 1 
ATOM   4470 N  N   . GLU B 1 180 ? 76.633  74.620  75.890  1.00 37.10 ? 169  GLU B N   1 
ATOM   4471 C  CA  . GLU B 1 180 ? 77.936  74.082  76.263  1.00 37.10 ? 169  GLU B CA  1 
ATOM   4472 C  C   . GLU B 1 180 ? 77.780  72.795  77.058  1.00 37.10 ? 169  GLU B C   1 
ATOM   4473 O  O   . GLU B 1 180 ? 78.427  71.784  76.760  1.00 37.10 ? 169  GLU B O   1 
ATOM   4474 C  CB  . GLU B 1 180 ? 78.714  75.123  77.066  1.00 37.10 ? 169  GLU B CB  1 
ATOM   4475 C  CG  . GLU B 1 180 ? 80.111  74.693  77.471  1.00 37.10 ? 169  GLU B CG  1 
ATOM   4476 C  CD  . GLU B 1 180 ? 80.673  75.528  78.604  1.00 37.10 ? 169  GLU B CD  1 
ATOM   4477 O  OE1 . GLU B 1 180 ? 81.851  75.927  78.515  1.00 37.10 ? 169  GLU B OE1 1 
ATOM   4478 O  OE2 . GLU B 1 180 ? 79.945  75.782  79.585  1.00 37.10 ? 169  GLU B OE2 1 
ATOM   4479 N  N   . GLY B 1 181 ? 76.917  72.810  78.074  1.00 33.58 ? 170  GLY B N   1 
ATOM   4480 C  CA  . GLY B 1 181 ? 76.679  71.593  78.830  1.00 33.58 ? 170  GLY B CA  1 
ATOM   4481 C  C   . GLY B 1 181 ? 76.116  70.484  77.965  1.00 33.58 ? 170  GLY B C   1 
ATOM   4482 O  O   . GLY B 1 181 ? 76.575  69.339  78.017  1.00 33.58 ? 170  GLY B O   1 
ATOM   4483 N  N   . LEU B 1 182 ? 75.115  70.813  77.146  1.00 38.26 ? 171  LEU B N   1 
ATOM   4484 C  CA  . LEU B 1 182 ? 74.503  69.803  76.290  1.00 38.26 ? 171  LEU B CA  1 
ATOM   4485 C  C   . LEU B 1 182 ? 75.534  69.183  75.354  1.00 38.26 ? 171  LEU B C   1 
ATOM   4486 O  O   . LEU B 1 182 ? 75.606  67.957  75.213  1.00 38.26 ? 171  LEU B O   1 
ATOM   4487 C  CB  . LEU B 1 182 ? 73.352  70.432  75.504  1.00 38.26 ? 171  LEU B CB  1 
ATOM   4488 C  CG  . LEU B 1 182 ? 72.809  69.672  74.297  1.00 38.26 ? 171  LEU B CG  1 
ATOM   4489 C  CD1 . LEU B 1 182 ? 72.354  68.291  74.692  1.00 38.26 ? 171  LEU B CD1 1 
ATOM   4490 C  CD2 . LEU B 1 182 ? 71.666  70.444  73.666  1.00 38.26 ? 171  LEU B CD2 1 
ATOM   4491 N  N   . PHE B 1 183 ? 76.360  70.018  74.725  1.00 43.17 ? 172  PHE B N   1 
ATOM   4492 C  CA  . PHE B 1 183 ? 77.370  69.536  73.792  1.00 43.17 ? 172  PHE B CA  1 
ATOM   4493 C  C   . PHE B 1 183 ? 78.390  68.653  74.491  1.00 43.17 ? 172  PHE B C   1 
ATOM   4494 O  O   . PHE B 1 183 ? 78.707  67.553  74.021  1.00 43.17 ? 172  PHE B O   1 
ATOM   4495 C  CB  . PHE B 1 183 ? 78.055  70.736  73.144  1.00 43.17 ? 172  PHE B CB  1 
ATOM   4496 C  CG  . PHE B 1 183 ? 79.221  70.381  72.283  1.00 43.17 ? 172  PHE B CG  1 
ATOM   4497 C  CD1 . PHE B 1 183 ? 79.027  69.878  71.016  1.00 43.17 ? 172  PHE B CD1 1 
ATOM   4498 C  CD2 . PHE B 1 183 ? 80.513  70.568  72.734  1.00 43.17 ? 172  PHE B CD2 1 
ATOM   4499 C  CE1 . PHE B 1 183 ? 80.095  69.556  70.216  1.00 43.17 ? 172  PHE B CE1 1 
ATOM   4500 C  CE2 . PHE B 1 183 ? 81.586  70.248  71.937  1.00 43.17 ? 172  PHE B CE2 1 
ATOM   4501 C  CZ  . PHE B 1 183 ? 81.375  69.742  70.675  1.00 43.17 ? 172  PHE B CZ  1 
ATOM   4502 N  N   . MET B 1 184 ? 78.924  69.123  75.619  1.00 39.96 ? 173  MET B N   1 
ATOM   4503 C  CA  . MET B 1 184 ? 79.956  68.361  76.307  1.00 39.96 ? 173  MET B CA  1 
ATOM   4504 C  C   . MET B 1 184 ? 79.431  67.006  76.753  1.00 39.96 ? 173  MET B C   1 
ATOM   4505 O  O   . MET B 1 184 ? 80.120  65.992  76.608  1.00 39.96 ? 173  MET B O   1 
ATOM   4506 C  CB  . MET B 1 184 ? 80.478  69.157  77.499  1.00 39.96 ? 173  MET B CB  1 
ATOM   4507 C  CG  . MET B 1 184 ? 81.482  70.227  77.121  1.00 39.96 ? 173  MET B CG  1 
ATOM   4508 S  SD  . MET B 1 184 ? 83.124  69.559  76.822  1.00 39.96 ? 173  MET B SD  1 
ATOM   4509 C  CE  . MET B 1 184 ? 83.534  70.369  75.282  1.00 39.96 ? 173  MET B CE  1 
ATOM   4510 N  N   . ARG B 1 185 ? 78.211  66.957  77.290  1.00 37.96 ? 174  ARG B N   1 
ATOM   4511 C  CA  . ARG B 1 185 ? 77.696  65.684  77.775  1.00 37.96 ? 174  ARG B CA  1 
ATOM   4512 C  C   . ARG B 1 185 ? 77.181  64.781  76.662  1.00 37.96 ? 174  ARG B C   1 
ATOM   4513 O  O   . ARG B 1 185 ? 77.106  63.566  76.864  1.00 37.96 ? 174  ARG B O   1 
ATOM   4514 C  CB  . ARG B 1 185 ? 76.586  65.911  78.799  1.00 37.96 ? 174  ARG B CB  1 
ATOM   4515 C  CG  . ARG B 1 185 ? 75.905  64.632  79.278  1.00 37.96 ? 174  ARG B CG  1 
ATOM   4516 C  CD  . ARG B 1 185 ? 76.876  63.714  79.988  1.00 37.96 ? 174  ARG B CD  1 
ATOM   4517 N  NE  . ARG B 1 185 ? 77.440  64.339  81.176  1.00 37.96 ? 174  ARG B NE  1 
ATOM   4518 C  CZ  . ARG B 1 185 ? 76.853  64.357  82.366  1.00 37.96 ? 174  ARG B CZ  1 
ATOM   4519 N  NH1 . ARG B 1 185 ? 75.671  63.785  82.542  1.00 37.96 ? 174  ARG B NH1 1 
ATOM   4520 N  NH2 . ARG B 1 185 ? 77.449  64.955  83.386  1.00 37.96 ? 174  ARG B NH2 1 
ATOM   4521 N  N   . VAL B 1 186 ? 76.819  65.325  75.503  1.00 44.00 ? 175  VAL B N   1 
ATOM   4522 C  CA  . VAL B 1 186 ? 76.359  64.465  74.420  1.00 44.00 ? 175  VAL B CA  1 
ATOM   4523 C  C   . VAL B 1 186 ? 77.527  63.920  73.609  1.00 44.00 ? 175  VAL B C   1 
ATOM   4524 O  O   . VAL B 1 186 ? 77.410  62.851  73.004  1.00 44.00 ? 175  VAL B O   1 
ATOM   4525 C  CB  . VAL B 1 186 ? 75.371  65.212  73.510  1.00 44.00 ? 175  VAL B CB  1 
ATOM   4526 C  CG1 . VAL B 1 186 ? 76.112  65.979  72.440  1.00 44.00 ? 175  VAL B CG1 1 
ATOM   4527 C  CG2 . VAL B 1 186 ? 74.394  64.241  72.884  1.00 44.00 ? 175  VAL B CG2 1 
ATOM   4528 N  N   . ARG B 1 187 ? 78.654  64.631  73.574  1.00 46.72 ? 176  ARG B N   1 
ATOM   4529 C  CA  . ARG B 1 187 ? 79.815  64.122  72.860  1.00 46.72 ? 176  ARG B CA  1 
ATOM   4530 C  C   . ARG B 1 187 ? 80.571  63.062  73.646  1.00 46.72 ? 176  ARG B C   1 
ATOM   4531 O  O   . ARG B 1 187 ? 81.486  62.444  73.095  1.00 46.72 ? 176  ARG B O   1 
ATOM   4532 C  CB  . ARG B 1 187 ? 80.761  65.268  72.500  1.00 46.72 ? 176  ARG B CB  1 
ATOM   4533 C  CG  . ARG B 1 187 ? 81.474  65.053  71.178  1.00 46.72 ? 176  ARG B CG  1 
ATOM   4534 C  CD  . ARG B 1 187 ? 82.196  66.295  70.698  1.00 46.72 ? 176  ARG B CD  1 
ATOM   4535 N  NE  . ARG B 1 187 ? 83.140  66.811  71.682  1.00 46.72 ? 176  ARG B NE  1 
ATOM   4536 C  CZ  . ARG B 1 187 ? 84.022  67.775  71.437  1.00 46.72 ? 176  ARG B CZ  1 
ATOM   4537 N  NH1 . ARG B 1 187 ? 84.096  68.324  70.232  1.00 46.72 ? 176  ARG B NH1 1 
ATOM   4538 N  NH2 . ARG B 1 187 ? 84.842  68.184  72.394  1.00 46.72 ? 176  ARG B NH2 1 
ATOM   4539 N  N   . ASP B 1 188 ? 80.215  62.837  74.910  1.00 46.02 ? 177  ASP B N   1 
ATOM   4540 C  CA  . ASP B 1 188 ? 80.849  61.801  75.714  1.00 46.02 ? 177  ASP B CA  1 
ATOM   4541 C  C   . ASP B 1 188 ? 80.110  60.473  75.652  1.00 46.02 ? 177  ASP B C   1 
ATOM   4542 O  O   . ASP B 1 188 ? 80.728  59.423  75.853  1.00 46.02 ? 177  ASP B O   1 
ATOM   4543 C  CB  . ASP B 1 188 ? 80.940  62.248  77.174  1.00 46.02 ? 177  ASP B CB  1 
ATOM   4544 C  CG  . ASP B 1 188 ? 82.027  63.274  77.403  1.00 46.02 ? 177  ASP B CG  1 
ATOM   4545 O  OD1 . ASP B 1 188 ? 82.758  63.594  76.443  1.00 46.02 ? 177  ASP B OD1 1 
ATOM   4546 O  OD2 . ASP B 1 188 ? 82.149  63.764  78.545  1.00 46.02 ? 177  ASP B OD2 1 
ATOM   4547 N  N   . ARG B 1 189 ? 78.806  60.492  75.379  1.00 45.04 ? 178  ARG B N   1 
ATOM   4548 C  CA  . ARG B 1 189 ? 77.988  59.291  75.419  1.00 45.04 ? 178  ARG B CA  1 
ATOM   4549 C  C   . ARG B 1 189 ? 77.559  58.794  74.047  1.00 45.04 ? 178  ARG B C   1 
ATOM   4550 O  O   . ARG B 1 189 ? 76.958  57.719  73.962  1.00 45.04 ? 178  ARG B O   1 
ATOM   4551 C  CB  . ARG B 1 189 ? 76.733  59.532  76.269  1.00 45.04 ? 178  ARG B CB  1 
ATOM   4552 C  CG  . ARG B 1 189 ? 76.980  60.323  77.539  1.00 45.04 ? 178  ARG B CG  1 
ATOM   4553 C  CD  . ARG B 1 189 ? 75.686  60.628  78.261  1.00 45.04 ? 178  ARG B CD  1 
ATOM   4554 N  NE  . ARG B 1 189 ? 74.743  59.514  78.195  1.00 45.04 ? 178  ARG B NE  1 
ATOM   4555 C  CZ  . ARG B 1 189 ? 74.374  58.762  79.228  1.00 45.04 ? 178  ARG B CZ  1 
ATOM   4556 N  NH1 . ARG B 1 189 ? 74.857  58.982  80.444  1.00 45.04 ? 178  ARG B NH1 1 
ATOM   4557 N  NH2 . ARG B 1 189 ? 73.508  57.776  79.041  1.00 45.04 ? 178  ARG B NH2 1 
ATOM   4558 N  N   . LEU B 1 190 ? 77.835  59.538  72.982  1.00 49.93 ? 179  LEU B N   1 
ATOM   4559 C  CA  . LEU B 1 190 ? 77.478  59.126  71.634  1.00 49.93 ? 179  LEU B CA  1 
ATOM   4560 C  C   . LEU B 1 190 ? 78.673  59.311  70.712  1.00 49.93 ? 179  LEU B C   1 
ATOM   4561 O  O   . LEU B 1 190 ? 79.480  60.227  70.889  1.00 49.93 ? 179  LEU B O   1 
ATOM   4562 C  CB  . LEU B 1 190 ? 76.286  59.927  71.090  1.00 49.93 ? 179  LEU B CB  1 
ATOM   4563 C  CG  . LEU B 1 190 ? 74.884  59.543  71.565  1.00 49.93 ? 179  LEU B CG  1 
ATOM   4564 C  CD1 . LEU B 1 190 ? 73.867  60.520  71.015  1.00 49.93 ? 179  LEU B CD1 1 
ATOM   4565 C  CD2 . LEU B 1 190 ? 74.528  58.129  71.159  1.00 49.93 ? 179  LEU B CD2 1 
ATOM   4566 N  N   . ASN B 1 191 ? 78.777  58.427  69.723  1.00 54.85 ? 180  ASN B N   1 
ATOM   4567 C  CA  . ASN B 1 191 ? 79.817  58.530  68.699  1.00 54.85 ? 180  ASN B CA  1 
ATOM   4568 C  C   . ASN B 1 191 ? 79.289  59.310  67.494  1.00 54.85 ? 180  ASN B C   1 
ATOM   4569 O  O   . ASN B 1 191 ? 79.261  58.831  66.361  1.00 54.85 ? 180  ASN B O   1 
ATOM   4570 C  CB  . ASN B 1 191 ? 80.300  57.141  68.296  1.00 54.85 ? 180  ASN B CB  1 
ATOM   4571 N  N   . ILE B 1 192 ? 78.863  60.542  67.768  1.00 53.24 ? 181  ILE B N   1 
ATOM   4572 C  CA  . ILE B 1 192 ? 78.300  61.421  66.756  1.00 53.24 ? 181  ILE B CA  1 
ATOM   4573 C  C   . ILE B 1 192 ? 79.172  62.663  66.645  1.00 53.24 ? 181  ILE B C   1 
ATOM   4574 O  O   . ILE B 1 192 ? 79.938  63.002  67.550  1.00 53.24 ? 181  ILE B O   1 
ATOM   4575 C  CB  . ILE B 1 192 ? 76.839  61.809  67.065  1.00 53.24 ? 181  ILE B CB  1 
ATOM   4576 C  CG1 . ILE B 1 192 ? 76.749  62.582  68.383  1.00 53.24 ? 181  ILE B CG1 1 
ATOM   4577 C  CG2 . ILE B 1 192 ? 75.971  60.573  67.120  1.00 53.24 ? 181  ILE B CG2 1 
ATOM   4578 C  CD1 . ILE B 1 192 ? 75.393  63.194  68.640  1.00 53.24 ? 181  ILE B CD1 1 
ATOM   4579 N  N   . THR B 1 193 ? 79.045  63.342  65.510  1.00 54.56 ? 182  THR B N   1 
ATOM   4580 C  CA  . THR B 1 193 ? 79.752  64.587  65.248  1.00 54.56 ? 182  THR B CA  1 
ATOM   4581 C  C   . THR B 1 193 ? 78.786  65.739  65.487  1.00 54.56 ? 182  THR B C   1 
ATOM   4582 O  O   . THR B 1 193 ? 77.756  65.838  64.812  1.00 54.56 ? 182  THR B O   1 
ATOM   4583 C  CB  . THR B 1 193 ? 80.285  64.618  63.816  1.00 54.56 ? 182  THR B CB  1 
ATOM   4584 O  OG1 . THR B 1 193 ? 81.189  63.525  63.618  1.00 54.56 ? 182  THR B OG1 1 
ATOM   4585 C  CG2 . THR B 1 193 ? 81.012  65.926  63.539  1.00 54.56 ? 182  THR B CG2 1 
ATOM   4586 N  N   . VAL B 1 194 ? 79.113  66.605  66.438  1.00 50.04 ? 183  VAL B N   1 
ATOM   4587 C  CA  . VAL B 1 194 ? 78.233  67.694  66.836  1.00 50.04 ? 183  VAL B CA  1 
ATOM   4588 C  C   . VAL B 1 194 ? 78.927  69.010  66.527  1.00 50.04 ? 183  VAL B C   1 
ATOM   4589 O  O   . VAL B 1 194 ? 80.126  69.163  66.784  1.00 50.04 ? 183  VAL B O   1 
ATOM   4590 C  CB  . VAL B 1 194 ? 77.858  67.609  68.327  1.00 50.04 ? 183  VAL B CB  1 
ATOM   4591 C  CG1 . VAL B 1 194 ? 77.025  68.809  68.724  1.00 50.04 ? 183  VAL B CG1 1 
ATOM   4592 C  CG2 . VAL B 1 194 ? 77.117  66.318  68.614  1.00 50.04 ? 183  VAL B CG2 1 
ATOM   4593 N  N   . ASP B 1 195 ? 78.175  69.956  65.971  1.00 49.01 ? 184  ASP B N   1 
ATOM   4594 C  CA  . ASP B 1 195 ? 78.725  71.240  65.552  1.00 49.01 ? 184  ASP B CA  1 
ATOM   4595 C  C   . ASP B 1 195 ? 78.062  72.370  66.326  1.00 49.01 ? 184  ASP B C   1 
ATOM   4596 O  O   . ASP B 1 195 ? 76.846  72.561  66.230  1.00 49.01 ? 184  ASP B O   1 
ATOM   4597 C  CB  . ASP B 1 195 ? 78.534  71.445  64.049  1.00 49.01 ? 184  ASP B CB  1 
ATOM   4598 N  N   . HIS B 1 196 ? 78.866  73.128  67.071  1.00 47.81 ? 185  HIS B N   1 
ATOM   4599 C  CA  . HIS B 1 196 ? 78.401  74.352  67.707  1.00 47.81 ? 185  HIS B CA  1 
ATOM   4600 C  C   . HIS B 1 196 ? 78.120  75.430  66.666  1.00 47.81 ? 185  HIS B C   1 
ATOM   4601 O  O   . HIS B 1 196 ? 78.614  75.389  65.538  1.00 47.81 ? 185  HIS B O   1 
ATOM   4602 C  CB  . HIS B 1 196 ? 79.447  74.895  68.681  1.00 47.81 ? 185  HIS B CB  1 
ATOM   4603 C  CG  . HIS B 1 196 ? 79.316  74.382  70.080  1.00 47.81 ? 185  HIS B CG  1 
ATOM   4604 N  ND1 . HIS B 1 196 ? 80.255  74.648  71.052  1.00 47.81 ? 185  HIS B ND1 1 
ATOM   4605 C  CD2 . HIS B 1 196 ? 78.361  73.630  70.675  1.00 47.81 ? 185  HIS B CD2 1 
ATOM   4606 C  CE1 . HIS B 1 196 ? 79.886  74.081  72.185  1.00 47.81 ? 185  HIS B CE1 1 
ATOM   4607 N  NE2 . HIS B 1 196 ? 78.740  73.457  71.984  1.00 47.81 ? 185  HIS B NE2 1 
ATOM   4608 N  N   . LEU B 1 197 ? 77.317  76.412  67.065  1.00 48.66 ? 186  LEU B N   1 
ATOM   4609 C  CA  . LEU B 1 197 ? 77.147  77.614  66.261  1.00 48.66 ? 186  LEU B CA  1 
ATOM   4610 C  C   . LEU B 1 197 ? 76.469  78.681  67.104  1.00 48.66 ? 186  LEU B C   1 
ATOM   4611 O  O   . LEU B 1 197 ? 75.551  78.381  67.871  1.00 48.66 ? 186  LEU B O   1 
ATOM   4612 C  CB  . LEU B 1 197 ? 76.323  77.329  65.001  1.00 48.66 ? 186  LEU B CB  1 
ATOM   4613 C  CG  . LEU B 1 197 ? 77.059  77.187  63.668  1.00 48.66 ? 186  LEU B CG  1 
ATOM   4614 C  CD1 . LEU B 1 197 ? 76.062  77.023  62.540  1.00 48.66 ? 186  LEU B CD1 1 
ATOM   4615 C  CD2 . LEU B 1 197 ? 77.964  78.379  63.402  1.00 48.66 ? 186  LEU B CD2 1 
ATOM   4616 N  N   . GLU B 1 198 ? 76.933  79.918  66.961  1.00 48.63 ? 187  GLU B N   1 
ATOM   4617 C  CA  . GLU B 1 198 ? 76.369  81.063  67.654  1.00 48.63 ? 187  GLU B CA  1 
ATOM   4618 C  C   . GLU B 1 198 ? 75.775  82.034  66.645  1.00 48.63 ? 187  GLU B C   1 
ATOM   4619 O  O   . GLU B 1 198 ? 76.271  82.173  65.525  1.00 48.63 ? 187  GLU B O   1 
ATOM   4620 C  CB  . GLU B 1 198 ? 77.427  81.787  68.488  1.00 48.63 ? 187  GLU B CB  1 
ATOM   4621 C  CG  . GLU B 1 198 ? 76.875  82.934  69.320  1.00 48.63 ? 187  GLU B CG  1 
ATOM   4622 C  CD  . GLU B 1 198 ? 77.961  83.748  69.993  1.00 48.63 ? 187  GLU B CD  1 
ATOM   4623 O  OE1 . GLU B 1 198 ? 79.108  83.262  70.076  1.00 48.63 ? 187  GLU B OE1 1 
ATOM   4624 O  OE2 . GLU B 1 198 ? 77.668  84.876  70.439  1.00 48.63 ? 187  GLU B OE2 1 
ATOM   4625 N  N   . PHE B 1 199 ? 74.702  82.705  67.051  1.00 50.06 ? 188  PHE B N   1 
ATOM   4626 C  CA  . PHE B 1 199 ? 74.143  83.766  66.229  1.00 50.06 ? 188  PHE B CA  1 
ATOM   4627 C  C   . PHE B 1 199 ? 73.596  84.856  67.138  1.00 50.06 ? 188  PHE B C   1 
ATOM   4628 O  O   . PHE B 1 199 ? 73.337  84.631  68.322  1.00 50.06 ? 188  PHE B O   1 
ATOM   4629 C  CB  . PHE B 1 199 ? 73.076  83.227  65.267  1.00 50.06 ? 188  PHE B CB  1 
ATOM   4630 C  CG  . PHE B 1 199 ? 71.790  82.823  65.928  1.00 50.06 ? 188  PHE B CG  1 
ATOM   4631 C  CD1 . PHE B 1 199 ? 70.743  83.715  66.039  1.00 50.06 ? 188  PHE B CD1 1 
ATOM   4632 C  CD2 . PHE B 1 199 ? 71.620  81.541  66.414  1.00 50.06 ? 188  PHE B CD2 1 
ATOM   4633 C  CE1 . PHE B 1 199 ? 69.559  83.342  66.635  1.00 50.06 ? 188  PHE B CE1 1 
ATOM   4634 C  CE2 . PHE B 1 199 ? 70.435  81.166  67.012  1.00 50.06 ? 188  PHE B CE2 1 
ATOM   4635 C  CZ  . PHE B 1 199 ? 69.407  82.068  67.120  1.00 50.06 ? 188  PHE B CZ  1 
ATOM   4636 N  N   . ALA B 1 200 ? 73.456  86.053  66.578  1.00 53.22 ? 189  ALA B N   1 
ATOM   4637 C  CA  . ALA B 1 200 ? 72.995  87.212  67.330  1.00 53.22 ? 189  ALA B CA  1 
ATOM   4638 C  C   . ALA B 1 200 ? 71.484  87.323  67.194  1.00 53.22 ? 189  ALA B C   1 
ATOM   4639 O  O   . ALA B 1 200 ? 70.961  87.433  66.081  1.00 53.22 ? 189  ALA B O   1 
ATOM   4640 C  CB  . ALA B 1 200 ? 73.677  88.486  66.838  1.00 53.22 ? 189  ALA B CB  1 
ATOM   4641 N  N   . GLU B 1 201 ? 70.785  87.300  68.329  1.00 52.40 ? 190  GLU B N   1 
ATOM   4642 C  CA  . GLU B 1 201 ? 69.329  87.258  68.298  1.00 52.40 ? 190  GLU B CA  1 
ATOM   4643 C  C   . GLU B 1 201 ? 68.733  88.577  67.826  1.00 52.40 ? 190  GLU B C   1 
ATOM   4644 O  O   . GLU B 1 201 ? 67.650  88.590  67.232  1.00 52.40 ? 190  GLU B O   1 
ATOM   4645 C  CB  . GLU B 1 201 ? 68.793  86.907  69.682  1.00 52.40 ? 190  GLU B CB  1 
ATOM   4646 C  CG  . GLU B 1 201 ? 67.318  86.587  69.699  1.00 52.40 ? 190  GLU B CG  1 
ATOM   4647 C  CD  . GLU B 1 201 ? 66.855  86.068  71.039  1.00 52.40 ? 190  GLU B CD  1 
ATOM   4648 O  OE1 . GLU B 1 201 ? 67.676  85.463  71.758  1.00 52.40 ? 190  GLU B OE1 1 
ATOM   4649 O  OE2 . GLU B 1 201 ? 65.667  86.258  71.370  1.00 52.40 ? 190  GLU B OE2 1 
ATOM   4650 N  N   . ASP B 1 202 ? 69.419  89.690  68.082  1.00 57.40 ? 191  ASP B N   1 
ATOM   4651 C  CA  . ASP B 1 202 ? 68.866  90.999  67.756  1.00 57.40 ? 191  ASP B CA  1 
ATOM   4652 C  C   . ASP B 1 202 ? 68.641  91.147  66.256  1.00 57.40 ? 191  ASP B C   1 
ATOM   4653 O  O   . ASP B 1 202 ? 67.506  91.311  65.796  1.00 57.40 ? 191  ASP B O   1 
ATOM   4654 C  CB  . ASP B 1 202 ? 69.800  92.095  68.271  1.00 57.40 ? 191  ASP B CB  1 
ATOM   4655 N  N   . ASP B 1 203 ? 69.716  91.087  65.475  1.00 61.36 ? 192  ASP B N   1 
ATOM   4656 C  CA  . ASP B 1 203 ? 69.645  91.424  64.059  1.00 61.36 ? 192  ASP B CA  1 
ATOM   4657 C  C   . ASP B 1 203 ? 69.163  90.236  63.239  1.00 61.36 ? 192  ASP B C   1 
ATOM   4658 O  O   . ASP B 1 203 ? 69.626  89.108  63.426  1.00 61.36 ? 192  ASP B O   1 
ATOM   4659 C  CB  . ASP B 1 203 ? 71.009  91.894  63.555  1.00 61.36 ? 192  ASP B CB  1 
ATOM   4660 C  CG  . ASP B 1 203 ? 72.109  90.898  63.839  1.00 61.36 ? 192  ASP B CG  1 
ATOM   4661 O  OD1 . ASP B 1 203 ? 71.815  89.856  64.454  1.00 61.36 ? 192  ASP B OD1 1 
ATOM   4662 O  OD2 . ASP B 1 203 ? 73.266  91.155  63.447  1.00 61.36 ? 192  ASP B OD2 1 
ATOM   4663 N  N   . LEU B 1 204 ? 68.238  90.501  62.318  1.00 62.04 ? 193  LEU B N   1 
ATOM   4664 C  CA  . LEU B 1 204 ? 67.695  89.479  61.435  1.00 62.04 ? 193  LEU B CA  1 
ATOM   4665 C  C   . LEU B 1 204 ? 68.573  89.229  60.218  1.00 62.04 ? 193  LEU B C   1 
ATOM   4666 O  O   . LEU B 1 204 ? 68.194  88.432  59.354  1.00 62.04 ? 193  LEU B O   1 
ATOM   4667 C  CB  . LEU B 1 204 ? 66.288  89.873  60.981  1.00 62.04 ? 193  LEU B CB  1 
ATOM   4668 N  N   . SER B 1 205 ? 69.719  89.902  60.118  1.00 61.52 ? 194  SER B N   1 
ATOM   4669 C  CA  . SER B 1 205 ? 70.658  89.616  59.043  1.00 61.52 ? 194  SER B CA  1 
ATOM   4670 C  C   . SER B 1 205 ? 71.424  88.326  59.289  1.00 61.52 ? 194  SER B C   1 
ATOM   4671 O  O   . SER B 1 205 ? 71.841  87.669  58.330  1.00 61.52 ? 194  SER B O   1 
ATOM   4672 C  CB  . SER B 1 205 ? 71.640  90.775  58.880  1.00 61.52 ? 194  SER B CB  1 
ATOM   4673 O  OG  . SER B 1 205 ? 72.579  90.497  57.860  1.00 61.52 ? 194  SER B OG  1 
ATOM   4674 N  N   . HIS B 1 206 ? 71.623  87.953  60.555  1.00 58.87 ? 195  HIS B N   1 
ATOM   4675 C  CA  . HIS B 1 206 ? 72.319  86.708  60.862  1.00 58.87 ? 195  HIS B CA  1 
ATOM   4676 C  C   . HIS B 1 206 ? 71.502  85.489  60.460  1.00 58.87 ? 195  HIS B C   1 
ATOM   4677 O  O   . HIS B 1 206 ? 72.074  84.446  60.128  1.00 58.87 ? 195  HIS B O   1 
ATOM   4678 C  CB  . HIS B 1 206 ? 72.650  86.643  62.352  1.00 58.87 ? 195  HIS B CB  1 
ATOM   4679 C  CG  . HIS B 1 206 ? 73.929  87.327  62.716  1.00 58.87 ? 195  HIS B CG  1 
ATOM   4680 N  ND1 . HIS B 1 206 ? 74.070  88.697  62.704  1.00 58.87 ? 195  HIS B ND1 1 
ATOM   4681 C  CD2 . HIS B 1 206 ? 75.124  86.829  63.112  1.00 58.87 ? 195  HIS B CD2 1 
ATOM   4682 C  CE1 . HIS B 1 206 ? 75.299  89.014  63.070  1.00 58.87 ? 195  HIS B CE1 1 
ATOM   4683 N  NE2 . HIS B 1 206 ? 75.959  87.898  63.324  1.00 58.87 ? 195  HIS B NE2 1 
ATOM   4684 N  N   . TYR B 1 207 ? 70.173  85.643  60.462  1.00 54.62 ? 196  TYR B N   1 
ATOM   4685 C  CA  . TYR B 1 207 ? 69.202  84.580  60.105  1.00 54.62 ? 196  TYR B CA  1 
ATOM   4686 C  C   . TYR B 1 207 ? 69.347  84.267  58.614  1.00 54.62 ? 196  TYR B C   1 
ATOM   4687 O  O   . TYR B 1 207 ? 68.959  83.155  58.201  1.00 54.62 ? 196  TYR B O   1 
ATOM   4688 C  CB  . TYR B 1 207 ? 67.779  84.987  60.497  1.00 54.62 ? 196  TYR B CB  1 
ATOM   4689 C  CG  . TYR B 1 207 ? 67.606  85.356  61.949  1.00 54.62 ? 196  TYR B CG  1 
ATOM   4690 C  CD1 . TYR B 1 207 ? 68.381  84.766  62.934  1.00 54.62 ? 196  TYR B CD1 1 
ATOM   4691 C  CD2 . TYR B 1 207 ? 66.667  86.295  62.342  1.00 54.62 ? 196  TYR B CD2 1 
ATOM   4692 C  CE1 . TYR B 1 207 ? 68.229  85.099  64.270  1.00 54.62 ? 196  TYR B CE1 1 
ATOM   4693 C  CE2 . TYR B 1 207 ? 66.501  86.640  63.673  1.00 54.62 ? 196  TYR B CE2 1 
ATOM   4694 C  CZ  . TYR B 1 207 ? 67.285  86.040  64.641  1.00 54.62 ? 196  TYR B CZ  1 
ATOM   4695 O  OH  . TYR B 1 207 ? 67.128  86.374  65.956  1.00 54.62 ? 196  TYR B OH  1 
ATOM   4696 N  N   . THR B 1 208 ? 69.846  85.226  57.824  1.00 56.82 ? 197  THR B N   1 
ATOM   4697 C  CA  . THR B 1 208 ? 70.074  85.027  56.387  1.00 56.82 ? 197  THR B CA  1 
ATOM   4698 C  C   . THR B 1 208 ? 71.243  84.054  56.282  1.00 56.82 ? 197  THR B C   1 
ATOM   4699 O  O   . THR B 1 208 ? 71.092  83.096  55.563  1.00 56.82 ? 197  THR B O   1 
ATOM   4700 C  CB  . THR B 1 208 ? 70.250  86.376  55.689  1.00 56.82 ? 197  THR B CB  1 
ATOM   4701 N  N   . ARG B 1 209 ? 72.312  84.256  57.055  1.00 58.69 ? 198  ARG B N   1 
ATOM   4702 C  CA  . ARG B 1 209 ? 73.526  83.401  57.061  1.00 58.69 ? 198  ARG B CA  1 
ATOM   4703 C  C   . ARG B 1 209 ? 73.246  82.038  57.687  1.00 58.69 ? 198  ARG B C   1 
ATOM   4704 O  O   . ARG B 1 209 ? 73.879  81.081  57.281  1.00 58.69 ? 198  ARG B O   1 
ATOM   4705 C  CB  . ARG B 1 209 ? 74.713  84.088  57.729  1.00 58.69 ? 198  ARG B CB  1 
ATOM   4706 N  N   . LEU B 1 210 ? 72.356  81.998  58.684  1.00 54.75 ? 199  LEU B N   1 
ATOM   4707 C  CA  . LEU B 1 210 ? 72.011  80.783  59.471  1.00 54.75 ? 199  LEU B CA  1 
ATOM   4708 C  C   . LEU B 1 210 ? 71.290  79.772  58.576  1.00 54.75 ? 199  LEU B C   1 
ATOM   4709 O  O   . LEU B 1 210 ? 71.624  78.573  58.650  1.00 54.75 ? 199  LEU B O   1 
ATOM   4710 C  CB  . LEU B 1 210 ? 71.149  81.200  60.667  1.00 54.75 ? 199  LEU B CB  1 
ATOM   4711 C  CG  . LEU B 1 210 ? 71.258  80.306  61.902  1.00 54.75 ? 199  LEU B CG  1 
ATOM   4712 C  CD1 . LEU B 1 210 ? 72.689  80.264  62.416  1.00 54.75 ? 199  LEU B CD1 1 
ATOM   4713 C  CD2 . LEU B 1 210 ? 70.312  80.776  62.996  1.00 54.75 ? 199  LEU B CD2 1 
ATOM   4714 N  N   . LEU B 1 211 ? 70.367  80.252  57.740  1.00 55.96 ? 200  LEU B N   1 
ATOM   4715 C  CA  . LEU B 1 211 ? 69.586  79.408  56.809  1.00 55.96 ? 200  LEU B CA  1 
ATOM   4716 C  C   . LEU B 1 211 ? 70.448  78.923  55.651  1.00 55.96 ? 200  LEU B C   1 
ATOM   4717 O  O   . LEU B 1 211 ? 70.009  78.019  54.992  1.00 55.96 ? 200  LEU B O   1 
ATOM   4718 C  CB  . LEU B 1 211 ? 68.353  80.170  56.333  1.00 55.96 ? 200  LEU B CB  1 
ATOM   4719 C  CG  . LEU B 1 211 ? 67.106  79.973  57.185  1.00 55.96 ? 200  LEU B CG  1 
ATOM   4720 C  CD1 . LEU B 1 211 ? 65.861  80.346  56.404  1.00 55.96 ? 200  LEU B CD1 1 
ATOM   4721 C  CD2 . LEU B 1 211 ? 67.010  78.559  57.686  1.00 55.96 ? 200  LEU B CD2 1 
ATOM   4722 N  N   . ARG B 1 212 ? 71.474  79.665  55.263  1.00 57.88 ? 201  ARG B N   1 
ATOM   4723 C  CA  . ARG B 1 212 ? 72.443  79.286  54.217  1.00 57.88 ? 201  ARG B CA  1 
ATOM   4724 C  C   . ARG B 1 212 ? 73.347  78.149  54.700  1.00 57.88 ? 201  ARG B C   1 
ATOM   4725 O  O   . ARG B 1 212 ? 73.423  77.143  53.998  1.00 57.88 ? 201  ARG B O   1 
ATOM   4726 C  CB  . ARG B 1 212 ? 73.257  80.534  53.868  1.00 57.88 ? 201  ARG B CB  1 
ATOM   4727 N  N   . THR B 1 213 ? 73.864  78.262  55.928  1.00 57.50 ? 202  THR B N   1 
ATOM   4728 C  CA  . THR B 1 213 ? 74.894  77.384  56.546  1.00 57.50 ? 202  THR B CA  1 
ATOM   4729 C  C   . THR B 1 213 ? 74.327  76.200  57.324  1.00 57.50 ? 202  THR B C   1 
ATOM   4730 O  O   . THR B 1 213 ? 75.099  75.484  57.926  1.00 57.50 ? 202  THR B O   1 
ATOM   4731 C  CB  . THR B 1 213 ? 75.758  78.198  57.510  1.00 57.50 ? 202  THR B CB  1 
ATOM   4732 O  OG1 . THR B 1 213 ? 74.921  78.763  58.512  1.00 57.50 ? 202  THR B OG1 1 
ATOM   4733 C  CG2 . THR B 1 213 ? 76.520  79.318  56.845  1.00 57.50 ? 202  THR B CG2 1 
ATOM   4734 N  N   . MET B 1 214 ? 73.019  76.033  57.368  1.00 57.02 ? 203  MET B N   1 
ATOM   4735 C  CA  . MET B 1 214 ? 72.359  74.933  58.115  1.00 57.02 ? 203  MET B CA  1 
ATOM   4736 C  C   . MET B 1 214 ? 71.932  73.758  57.234  1.00 57.02 ? 203  MET B C   1 
ATOM   4737 O  O   . MET B 1 214 ? 71.784  72.697  57.763  1.00 57.02 ? 203  MET B O   1 
ATOM   4738 C  CB  . MET B 1 214 ? 71.149  75.496  58.839  1.00 57.02 ? 203  MET B CB  1 
ATOM   4739 C  CG  . MET B 1 214 ? 70.744  74.718  60.011  1.00 57.02 ? 203  MET B CG  1 
ATOM   4740 S  SD  . MET B 1 214 ? 69.016  75.007  60.133  1.00 57.02 ? 203  MET B SD  1 
ATOM   4741 C  CE  . MET B 1 214 ? 69.039  76.727  60.635  1.00 57.02 ? 203  MET B CE  1 
ATOM   4742 N  N   . PRO B 1 215 ? 71.627  73.880  55.932  1.00 58.73 ? 204  PRO B N   1 
ATOM   4743 C  CA  . PRO B 1 215 ? 71.394  72.721  55.110  1.00 58.73 ? 204  PRO B CA  1 
ATOM   4744 C  C   . PRO B 1 215 ? 72.681  71.966  54.776  1.00 58.73 ? 204  PRO B C   1 
ATOM   4745 O  O   . PRO B 1 215 ? 72.568  70.918  54.201  1.00 58.73 ? 204  PRO B O   1 
ATOM   4746 C  CB  . PRO B 1 215 ? 70.849  73.235  53.786  1.00 58.73 ? 204  PRO B CB  1 
ATOM   4747 C  CG  . PRO B 1 215 ? 70.289  74.552  54.134  1.00 58.73 ? 204  PRO B CG  1 
ATOM   4748 C  CD  . PRO B 1 215 ? 71.178  75.057  55.243  1.00 58.73 ? 204  PRO B CD  1 
ATOM   4749 N  N   . ARG B 1 216 ? 73.859  72.513  55.069  1.00 61.21 ? 205  ARG B N   1 
ATOM   4750 C  CA  . ARG B 1 216 ? 75.080  71.770  54.789  1.00 61.21 ? 205  ARG B CA  1 
ATOM   4751 C  C   . ARG B 1 216 ? 75.755  71.223  56.037  1.00 61.21 ? 205  ARG B C   1 
ATOM   4752 O  O   . ARG B 1 216 ? 76.433  70.194  55.956  1.00 61.21 ? 205  ARG B O   1 
ATOM   4753 C  CB  . ARG B 1 216 ? 76.077  72.659  54.039  1.00 61.21 ? 205  ARG B CB  1 
ATOM   4754 N  N   . LYS B 1 217 ? 75.584  71.873  57.185  1.00 58.40 ? 206  LYS B N   1 
ATOM   4755 C  CA  . LYS B 1 217 ? 76.317  71.525  58.394  1.00 58.40 ? 206  LYS B CA  1 
ATOM   4756 C  C   . LYS B 1 217 ? 75.524  70.660  59.364  1.00 58.40 ? 206  LYS B C   1 
ATOM   4757 O  O   . LYS B 1 217 ? 76.041  70.335  60.436  1.00 58.40 ? 206  LYS B O   1 
ATOM   4758 C  CB  . LYS B 1 217 ? 76.776  72.800  59.110  1.00 58.40 ? 206  LYS B CB  1 
ATOM   4759 N  N   . GLY B 1 218 ? 74.296  70.279  59.035  1.00 58.07 ? 207  GLY B N   1 
ATOM   4760 C  CA  . GLY B 1 218 ? 73.530  69.450  59.949  1.00 58.07 ? 207  GLY B CA  1 
ATOM   4761 C  C   . GLY B 1 218 ? 72.157  69.140  59.399  1.00 58.07 ? 207  GLY B C   1 
ATOM   4762 O  O   . GLY B 1 218 ? 71.703  69.730  58.413  1.00 58.07 ? 207  GLY B O   1 
ATOM   4763 N  N   . ARG B 1 219 ? 71.438  68.139  59.936  1.00 59.32 ? 208  ARG B N   1 
ATOM   4764 C  CA  . ARG B 1 219 ? 70.043  67.831  59.594  1.00 59.32 ? 208  ARG B CA  1 
ATOM   4765 C  C   . ARG B 1 219 ? 69.192  67.550  60.828  1.00 59.32 ? 208  ARG B C   1 
ATOM   4766 O  O   . ARG B 1 219 ? 68.075  67.178  60.599  1.00 59.32 ? 208  ARG B O   1 
ATOM   4767 C  CB  . ARG B 1 219 ? 69.923  66.617  58.698  1.00 59.32 ? 208  ARG B CB  1 
ATOM   4768 C  CG  . ARG B 1 219 ? 68.672  66.641  57.854  1.00 59.32 ? 208  ARG B CG  1 
ATOM   4769 C  CD  . ARG B 1 219 ? 68.936  67.066  56.433  1.00 59.32 ? 208  ARG B CD  1 
ATOM   4770 N  NE  . ARG B 1 219 ? 70.078  67.937  56.229  1.00 59.32 ? 208  ARG B NE  1 
ATOM   4771 C  CZ  . ARG B 1 219 ? 70.409  68.432  55.046  1.00 59.32 ? 208  ARG B CZ  1 
ATOM   4772 N  NH1 . ARG B 1 219 ? 69.660  68.164  53.991  1.00 59.32 ? 208  ARG B NH1 1 
ATOM   4773 N  NH2 . ARG B 1 219 ? 71.465  69.209  54.917  1.00 59.32 ? 208  ARG B NH2 1 
ATOM   4774 N  N   . VAL B 1 220 ? 69.702  67.572  62.066  1.00 52.09 ? 209  VAL B N   1 
ATOM   4775 C  CA  . VAL B 1 220 ? 68.866  67.524  63.259  1.00 52.09 ? 209  VAL B CA  1 
ATOM   4776 C  C   . VAL B 1 220 ? 69.368  68.608  64.200  1.00 52.09 ? 209  VAL B C   1 
ATOM   4777 O  O   . VAL B 1 220 ? 70.391  68.435  64.869  1.00 52.09 ? 209  VAL B O   1 
ATOM   4778 C  CB  . VAL B 1 220 ? 68.913  66.137  63.921  1.00 52.09 ? 209  VAL B CB  1 
ATOM   4779 C  CG1 . VAL B 1 220 ? 68.307  66.184  65.310  1.00 52.09 ? 209  VAL B CG1 1 
ATOM   4780 C  CG2 . VAL B 1 220 ? 68.189  65.123  63.059  1.00 52.09 ? 209  VAL B CG2 1 
ATOM   4781 N  N   . ILE B 1 221 ? 68.655  69.729  64.258  1.00 48.40 ? 210  ILE B N   1 
ATOM   4782 C  CA  . ILE B 1 221 ? 69.167  70.965  64.839  1.00 48.40 ? 210  ILE B CA  1 
ATOM   4783 C  C   . ILE B 1 221 ? 68.544  71.188  66.207  1.00 48.40 ? 210  ILE B C   1 
ATOM   4784 O  O   . ILE B 1 221 ? 67.367  70.878  66.425  1.00 48.40 ? 210  ILE B O   1 
ATOM   4785 C  CB  . ILE B 1 221 ? 68.883  72.156  63.906  1.00 48.40 ? 210  ILE B CB  1 
ATOM   4786 C  CG1 . ILE B 1 221 ? 69.342  71.837  62.486  1.00 48.40 ? 210  ILE B CG1 1 
ATOM   4787 C  CG2 . ILE B 1 221 ? 69.588  73.397  64.401  1.00 48.40 ? 210  ILE B CG2 1 
ATOM   4788 C  CD1 . ILE B 1 221 ? 68.245  71.329  61.594  1.00 48.40 ? 210  ILE B CD1 1 
ATOM   4789 N  N   . TYR B 1 222 ? 69.339  71.725  67.132  1.00 43.29 ? 211  TYR B N   1 
ATOM   4790 C  CA  . TYR B 1 222 ? 68.877  72.102  68.466  1.00 43.29 ? 211  TYR B CA  1 
ATOM   4791 C  C   . TYR B 1 222 ? 69.129  73.591  68.658  1.00 43.29 ? 211  TYR B C   1 
ATOM   4792 O  O   . TYR B 1 222 ? 70.282  74.015  68.765  1.00 43.29 ? 211  TYR B O   1 
ATOM   4793 C  CB  . TYR B 1 222 ? 69.593  71.296  69.547  1.00 43.29 ? 211  TYR B CB  1 
ATOM   4794 C  CG  . TYR B 1 222 ? 69.366  69.807  69.470  1.00 43.29 ? 211  TYR B CG  1 
ATOM   4795 C  CD1 . TYR B 1 222 ? 70.161  69.006  68.668  1.00 43.29 ? 211  TYR B CD1 1 
ATOM   4796 C  CD2 . TYR B 1 222 ? 68.365  69.201  70.208  1.00 43.29 ? 211  TYR B CD2 1 
ATOM   4797 C  CE1 . TYR B 1 222 ? 69.958  67.650  68.597  1.00 43.29 ? 211  TYR B CE1 1 
ATOM   4798 C  CE2 . TYR B 1 222 ? 68.156  67.847  70.140  1.00 43.29 ? 211  TYR B CE2 1 
ATOM   4799 C  CZ  . TYR B 1 222 ? 68.955  67.077  69.334  1.00 43.29 ? 211  TYR B CZ  1 
ATOM   4800 O  OH  . TYR B 1 222 ? 68.746  65.723  69.268  1.00 43.29 ? 211  TYR B OH  1 
ATOM   4801 N  N   . ILE B 1 223 ? 68.055  74.382  68.728  1.00 43.60 ? 212  ILE B N   1 
ATOM   4802 C  CA  . ILE B 1 223 ? 68.138  75.834  68.873  1.00 43.60 ? 212  ILE B CA  1 
ATOM   4803 C  C   . ILE B 1 223 ? 67.849  76.211  70.318  1.00 43.60 ? 212  ILE B C   1 
ATOM   4804 O  O   . ILE B 1 223 ? 66.956  75.635  70.950  1.00 43.60 ? 212  ILE B O   1 
ATOM   4805 C  CB  . ILE B 1 223 ? 67.154  76.544  67.922  1.00 43.60 ? 212  ILE B CB  1 
ATOM   4806 C  CG1 . ILE B 1 223 ? 67.510  76.261  66.466  1.00 43.60 ? 212  ILE B CG1 1 
ATOM   4807 C  CG2 . ILE B 1 223 ? 67.135  78.036  68.192  1.00 43.60 ? 212  ILE B CG2 1 
ATOM   4808 C  CD1 . ILE B 1 223 ? 66.801  75.070  65.890  1.00 43.60 ? 212  ILE B CD1 1 
ATOM   4809 N  N   . CYS B 1 224 ? 68.599  77.179  70.847  1.00 42.08 ? 213  CYS B N   1 
ATOM   4810 C  CA  . CYS B 1 224 ? 68.349  77.685  72.194  1.00 42.08 ? 213  CYS B CA  1 
ATOM   4811 C  C   . CYS B 1 224 ? 67.771  79.096  72.227  1.00 42.08 ? 213  CYS B C   1 
ATOM   4812 O  O   . CYS B 1 224 ? 67.510  79.615  73.314  1.00 42.08 ? 213  CYS B O   1 
ATOM   4813 C  CB  . CYS B 1 224 ? 69.634  77.657  73.027  1.00 42.08 ? 213  CYS B CB  1 
ATOM   4814 S  SG  . CYS B 1 224 ? 69.399  78.179  74.747  1.00 42.08 ? 213  CYS B SG  1 
ATOM   4815 N  N   . SER B 1 225 ? 67.507  79.715  71.084  1.00 45.85 ? 214  SER B N   1 
ATOM   4816 C  CA  . SER B 1 225 ? 67.063  81.103  71.079  1.00 45.85 ? 214  SER B CA  1 
ATOM   4817 C  C   . SER B 1 225 ? 65.765  81.285  71.854  1.00 45.85 ? 214  SER B C   1 
ATOM   4818 O  O   . SER B 1 225 ? 65.183  80.313  72.345  1.00 45.85 ? 214  SER B O   1 
ATOM   4819 C  CB  . SER B 1 225 ? 66.872  81.583  69.645  1.00 45.85 ? 214  SER B CB  1 
ATOM   4820 O  OG  . SER B 1 225 ? 65.643  81.117  69.122  1.00 45.85 ? 214  SER B OG  1 
ATOM   4821 N  N   . SER B 1 226 ? 65.313  82.527  71.976  1.00 46.89 ? 215  SER B N   1 
ATOM   4822 C  CA  . SER B 1 226 ? 64.091  82.848  72.696  1.00 46.89 ? 215  SER B CA  1 
ATOM   4823 C  C   . SER B 1 226 ? 62.872  82.479  71.859  1.00 46.89 ? 215  SER B C   1 
ATOM   4824 O  O   . SER B 1 226 ? 62.991  82.099  70.694  1.00 46.89 ? 215  SER B O   1 
ATOM   4825 C  CB  . SER B 1 226 ? 64.085  84.330  73.055  1.00 46.89 ? 215  SER B CB  1 
ATOM   4826 O  OG  . SER B 1 226 ? 63.704  85.123  71.948  1.00 46.89 ? 215  SER B OG  1 
ATOM   4827 N  N   . PRO B 1 227 ? 61.671  82.568  72.436  1.00 45.61 ? 216  PRO B N   1 
ATOM   4828 C  CA  . PRO B 1 227 ? 60.475  82.150  71.683  1.00 45.61 ? 216  PRO B CA  1 
ATOM   4829 C  C   . PRO B 1 227 ? 60.263  82.903  70.380  1.00 45.61 ? 216  PRO B C   1 
ATOM   4830 O  O   . PRO B 1 227 ? 60.060  82.276  69.329  1.00 45.61 ? 216  PRO B O   1 
ATOM   4831 C  CB  . PRO B 1 227 ? 59.344  82.407  72.684  1.00 45.61 ? 216  PRO B CB  1 
ATOM   4832 C  CG  . PRO B 1 227 ? 59.988  82.277  74.007  1.00 45.61 ? 216  PRO B CG  1 
ATOM   4833 C  CD  . PRO B 1 227 ? 61.355  82.854  73.844  1.00 45.61 ? 216  PRO B CD  1 
ATOM   4834 N  N   . ASP B 1 228 ? 60.287  84.238  70.417  1.00 50.79 ? 217  ASP B N   1 
ATOM   4835 C  CA  . ASP B 1 228 ? 60.051  85.013  69.203  1.00 50.79 ? 217  ASP B CA  1 
ATOM   4836 C  C   . ASP B 1 228 ? 61.147  84.775  68.174  1.00 50.79 ? 217  ASP B C   1 
ATOM   4837 O  O   . ASP B 1 228 ? 60.870  84.670  66.973  1.00 50.79 ? 217  ASP B O   1 
ATOM   4838 C  CB  . ASP B 1 228 ? 59.948  86.500  69.536  1.00 50.79 ? 217  ASP B CB  1 
ATOM   4839 N  N   . ALA B 1 229 ? 62.399  84.694  68.623  1.00 49.28 ? 218  ALA B N   1 
ATOM   4840 C  CA  . ALA B 1 229 ? 63.485  84.404  67.696  1.00 49.28 ? 218  ALA B CA  1 
ATOM   4841 C  C   . ALA B 1 229 ? 63.279  83.054  67.027  1.00 49.28 ? 218  ALA B C   1 
ATOM   4842 O  O   . ALA B 1 229 ? 63.482  82.917  65.816  1.00 49.28 ? 218  ALA B O   1 
ATOM   4843 C  CB  . ALA B 1 229 ? 64.826  84.442  68.426  1.00 49.28 ? 218  ALA B CB  1 
ATOM   4844 N  N   . PHE B 1 230 ? 62.871  82.044  67.796  1.00 46.05 ? 219  PHE B N   1 
ATOM   4845 C  CA  . PHE B 1 230 ? 62.639  80.729  67.211  1.00 46.05 ? 219  PHE B CA  1 
ATOM   4846 C  C   . PHE B 1 230 ? 61.501  80.768  66.204  1.00 46.05 ? 219  PHE B C   1 
ATOM   4847 O  O   . PHE B 1 230 ? 61.582  80.135  65.148  1.00 46.05 ? 219  PHE B O   1 
ATOM   4848 C  CB  . PHE B 1 230 ? 62.340  79.707  68.302  1.00 46.05 ? 219  PHE B CB  1 
ATOM   4849 C  CG  . PHE B 1 230 ? 62.143  78.308  67.784  1.00 46.05 ? 219  PHE B CG  1 
ATOM   4850 C  CD1 . PHE B 1 230 ? 63.228  77.507  67.482  1.00 46.05 ? 219  PHE B CD1 1 
ATOM   4851 C  CD2 . PHE B 1 230 ? 60.873  77.794  67.605  1.00 46.05 ? 219  PHE B CD2 1 
ATOM   4852 C  CE1 . PHE B 1 230 ? 63.047  76.228  67.012  1.00 46.05 ? 219  PHE B CE1 1 
ATOM   4853 C  CE2 . PHE B 1 230 ? 60.691  76.514  67.134  1.00 46.05 ? 219  PHE B CE2 1 
ATOM   4854 C  CZ  . PHE B 1 230 ? 61.778  75.733  66.839  1.00 46.05 ? 219  PHE B CZ  1 
ATOM   4855 N  N   . ARG B 1 231 ? 60.422  81.489  66.514  1.00 51.79 ? 220  ARG B N   1 
ATOM   4856 C  CA  . ARG B 1 231 ? 59.305  81.545  65.577  1.00 51.79 ? 220  ARG B CA  1 
ATOM   4857 C  C   . ARG B 1 231 ? 59.710  82.247  64.286  1.00 51.79 ? 220  ARG B C   1 
ATOM   4858 O  O   . ARG B 1 231 ? 59.358  81.798  63.186  1.00 51.79 ? 220  ARG B O   1 
ATOM   4859 C  CB  . ARG B 1 231 ? 58.113  82.244  66.225  1.00 51.79 ? 220  ARG B CB  1 
ATOM   4860 C  CG  . ARG B 1 231 ? 56.875  82.303  65.350  1.00 51.79 ? 220  ARG B CG  1 
ATOM   4861 C  CD  . ARG B 1 231 ? 55.751  83.049  66.041  1.00 51.79 ? 220  ARG B CD  1 
ATOM   4862 N  NE  . ARG B 1 231 ? 54.697  83.445  65.112  1.00 51.79 ? 220  ARG B NE  1 
ATOM   4863 C  CZ  . ARG B 1 231 ? 54.649  84.607  64.469  1.00 51.79 ? 220  ARG B CZ  1 
ATOM   4864 N  NH1 . ARG B 1 231 ? 55.605  85.511  64.633  1.00 51.79 ? 220  ARG B NH1 1 
ATOM   4865 N  NH2 . ARG B 1 231 ? 53.640  84.863  63.651  1.00 51.79 ? 220  ARG B NH2 1 
ATOM   4866 N  N   . THR B 1 232 ? 60.467  83.341  64.397  1.00 51.53 ? 221  THR B N   1 
ATOM   4867 C  CA  . THR B 1 232 ? 60.965  84.024  63.207  1.00 51.53 ? 221  THR B CA  1 
ATOM   4868 C  C   . THR B 1 232 ? 61.861  83.106  62.385  1.00 51.53 ? 221  THR B C   1 
ATOM   4869 O  O   . THR B 1 232 ? 61.741  83.031  61.156  1.00 51.53 ? 221  THR B O   1 
ATOM   4870 C  CB  . THR B 1 232 ? 61.728  85.285  63.613  1.00 51.53 ? 221  THR B CB  1 
ATOM   4871 O  OG1 . THR B 1 232 ? 60.830  86.217  64.227  1.00 51.53 ? 221  THR B OG1 1 
ATOM   4872 C  CG2 . THR B 1 232 ? 62.381  85.930  62.407  1.00 51.53 ? 221  THR B CG2 1 
ATOM   4873 N  N   . LEU B 1 233 ? 62.771  82.397  63.053  1.00 52.18 ? 222  LEU B N   1 
ATOM   4874 C  CA  . LEU B 1 233 ? 63.685  81.509  62.349  1.00 52.18 ? 222  LEU B CA  1 
ATOM   4875 C  C   . LEU B 1 233 ? 62.929  80.381  61.664  1.00 52.18 ? 222  LEU B C   1 
ATOM   4876 O  O   . LEU B 1 233 ? 63.282  79.973  60.554  1.00 52.18 ? 222  LEU B O   1 
ATOM   4877 C  CB  . LEU B 1 233 ? 64.717  80.955  63.329  1.00 52.18 ? 222  LEU B CB  1 
ATOM   4878 C  CG  . LEU B 1 233 ? 65.866  80.123  62.765  1.00 52.18 ? 222  LEU B CG  1 
ATOM   4879 C  CD1 . LEU B 1 233 ? 66.705  80.933  61.796  1.00 52.18 ? 222  LEU B CD1 1 
ATOM   4880 C  CD2 . LEU B 1 233 ? 66.722  79.605  63.905  1.00 52.18 ? 222  LEU B CD2 1 
ATOM   4881 N  N   . MET B 1 234 ? 61.882  79.863  62.308  1.00 52.04 ? 223  MET B N   1 
ATOM   4882 C  CA  . MET B 1 234 ? 61.109  78.785  61.704  1.00 52.04 ? 223  MET B CA  1 
ATOM   4883 C  C   . MET B 1 234 ? 60.324  79.277  60.496  1.00 52.04 ? 223  MET B C   1 
ATOM   4884 O  O   . MET B 1 234 ? 60.193  78.557  59.499  1.00 52.04 ? 223  MET B O   1 
ATOM   4885 C  CB  . MET B 1 234 ? 60.170  78.170  62.738  1.00 52.04 ? 223  MET B CB  1 
ATOM   4886 C  CG  . MET B 1 234 ? 60.884  77.381  63.813  1.00 52.04 ? 223  MET B CG  1 
ATOM   4887 S  SD  . MET B 1 234 ? 61.768  75.957  63.163  1.00 52.04 ? 223  MET B SD  1 
ATOM   4888 C  CE  . MET B 1 234 ? 60.402  74.954  62.608  1.00 52.04 ? 223  MET B CE  1 
ATOM   4889 N  N   . LEU B 1 235 ? 59.791  80.498  60.560  1.00 54.00 ? 224  LEU B N   1 
ATOM   4890 C  CA  . LEU B 1 235 ? 59.122  81.051  59.387  1.00 54.00 ? 224  LEU B CA  1 
ATOM   4891 C  C   . LEU B 1 235 ? 60.103  81.257  58.240  1.00 54.00 ? 224  LEU B C   1 
ATOM   4892 O  O   . LEU B 1 235 ? 59.782  80.973  57.079  1.00 54.00 ? 224  LEU B O   1 
ATOM   4893 C  CB  . LEU B 1 235 ? 58.428  82.361  59.747  1.00 54.00 ? 224  LEU B CB  1 
ATOM   4894 C  CG  . LEU B 1 235 ? 57.017  82.252  60.328  1.00 54.00 ? 224  LEU B CG  1 
ATOM   4895 C  CD1 . LEU B 1 235 ? 56.363  83.600  60.278  1.00 54.00 ? 224  LEU B CD1 1 
ATOM   4896 C  CD2 . LEU B 1 235 ? 56.168  81.245  59.577  1.00 54.00 ? 224  LEU B CD2 1 
ATOM   4897 N  N   . LEU B 1 236 ? 61.307  81.743  58.542  1.00 53.76 ? 225  LEU B N   1 
ATOM   4898 C  CA  . LEU B 1 236 ? 62.327  81.850  57.502  1.00 53.76 ? 225  LEU B CA  1 
ATOM   4899 C  C   . LEU B 1 236 ? 62.655  80.482  56.916  1.00 53.76 ? 225  LEU B C   1 
ATOM   4900 O  O   . LEU B 1 236 ? 62.797  80.335  55.696  1.00 53.76 ? 225  LEU B O   1 
ATOM   4901 C  CB  . LEU B 1 236 ? 63.590  82.500  58.066  1.00 53.76 ? 225  LEU B CB  1 
ATOM   4902 C  CG  . LEU B 1 236 ? 63.504  83.965  58.488  1.00 53.76 ? 225  LEU B CG  1 
ATOM   4903 C  CD1 . LEU B 1 236 ? 64.893  84.490  58.768  1.00 53.76 ? 225  LEU B CD1 1 
ATOM   4904 C  CD2 . LEU B 1 236 ? 62.822  84.810  57.427  1.00 53.76 ? 225  LEU B CD2 1 
ATOM   4905 N  N   . ALA B 1 237 ? 62.778  79.466  57.772  1.00 54.30 ? 226  ALA B N   1 
ATOM   4906 C  CA  . ALA B 1 237 ? 63.074  78.123  57.292  1.00 54.30 ? 226  ALA B CA  1 
ATOM   4907 C  C   . ALA B 1 237 ? 61.984  77.625  56.357  1.00 54.30 ? 226  ALA B C   1 
ATOM   4908 O  O   . ALA B 1 237 ? 62.273  77.014  55.322  1.00 54.30 ? 226  ALA B O   1 
ATOM   4909 C  CB  . ALA B 1 237 ? 63.240  77.171  58.475  1.00 54.30 ? 226  ALA B CB  1 
ATOM   4910 N  N   . LEU B 1 238 ? 60.721  77.867  56.707  1.00 55.86 ? 227  LEU B N   1 
ATOM   4911 C  CA  . LEU B 1 238 ? 59.637  77.492  55.807  1.00 55.86 ? 227  LEU B CA  1 
ATOM   4912 C  C   . LEU B 1 238 ? 59.749  78.238  54.486  1.00 55.86 ? 227  LEU B C   1 
ATOM   4913 O  O   . LEU B 1 238 ? 59.572  77.648  53.414  1.00 55.86 ? 227  LEU B O   1 
ATOM   4914 C  CB  . LEU B 1 238 ? 58.282  77.763  56.460  1.00 55.86 ? 227  LEU B CB  1 
ATOM   4915 C  CG  . LEU B 1 238 ? 57.075  77.687  55.519  1.00 55.86 ? 227  LEU B CG  1 
ATOM   4916 C  CD1 . LEU B 1 238 ? 57.002  76.328  54.847  1.00 55.86 ? 227  LEU B CD1 1 
ATOM   4917 C  CD2 . LEU B 1 238 ? 55.794  77.972  56.273  1.00 55.86 ? 227  LEU B CD2 1 
ATOM   4918 N  N   . GLU B 1 239 ? 60.050  79.537  54.540  1.00 57.13 ? 228  GLU B N   1 
ATOM   4919 C  CA  . GLU B 1 239 ? 60.215  80.305  53.311  1.00 57.13 ? 228  GLU B CA  1 
ATOM   4920 C  C   . GLU B 1 239 ? 61.369  79.785  52.466  1.00 57.13 ? 228  GLU B C   1 
ATOM   4921 O  O   . GLU B 1 239 ? 61.376  79.996  51.250  1.00 57.13 ? 228  GLU B O   1 
ATOM   4922 C  CB  . GLU B 1 239 ? 60.436  81.782  53.636  1.00 57.13 ? 228  GLU B CB  1 
ATOM   4923 N  N   . ALA B 1 240 ? 62.340  79.115  53.079  1.00 57.31 ? 229  ALA B N   1 
ATOM   4924 C  CA  . ALA B 1 240 ? 63.442  78.501  52.352  1.00 57.31 ? 229  ALA B CA  1 
ATOM   4925 C  C   . ALA B 1 240 ? 63.131  77.081  51.904  1.00 57.31 ? 229  ALA B C   1 
ATOM   4926 O  O   . ALA B 1 240 ? 64.014  76.412  51.359  1.00 57.31 ? 229  ALA B O   1 
ATOM   4927 C  CB  . ALA B 1 240 ? 64.708  78.492  53.215  1.00 57.31 ? 229  ALA B CB  1 
ATOM   4928 N  N   . GLY B 1 241 ? 61.910  76.605  52.121  1.00 56.93 ? 230  GLY B N   1 
ATOM   4929 C  CA  . GLY B 1 241 ? 61.542  75.254  51.734  1.00 56.93 ? 230  GLY B CA  1 
ATOM   4930 C  C   . GLY B 1 241 ? 62.250  74.170  52.517  1.00 56.93 ? 230  GLY B C   1 
ATOM   4931 O  O   . GLY B 1 241 ? 62.637  73.148  51.938  1.00 56.93 ? 230  GLY B O   1 
ATOM   4932 N  N   . LEU B 1 242 ? 62.428  74.365  53.821  1.00 56.38 ? 231  LEU B N   1 
ATOM   4933 C  CA  . LEU B 1 242 ? 63.038  73.355  54.683  1.00 56.38 ? 231  LEU B CA  1 
ATOM   4934 C  C   . LEU B 1 242 ? 61.933  72.545  55.360  1.00 56.38 ? 231  LEU B C   1 
ATOM   4935 O  O   . LEU B 1 242 ? 61.706  72.615  56.568  1.00 56.38 ? 231  LEU B O   1 
ATOM   4936 C  CB  . LEU B 1 242 ? 63.960  74.017  55.701  1.00 56.38 ? 231  LEU B CB  1 
ATOM   4937 C  CG  . LEU B 1 242 ? 65.443  74.033  55.338  1.00 56.38 ? 231  LEU B CG  1 
ATOM   4938 C  CD1 . LEU B 1 242 ? 65.656  74.676  53.982  1.00 56.38 ? 231  LEU B CD1 1 
ATOM   4939 C  CD2 . LEU B 1 242 ? 66.251  74.747  56.405  1.00 56.38 ? 231  LEU B CD2 1 
ATOM   4940 N  N   . CYS B 1 243 ? 61.239  71.762  54.540  1.00 63.83 ? 232  CYS B N   1 
ATOM   4941 C  CA  . CYS B 1 243 ? 60.069  71.035  55.001  1.00 63.83 ? 232  CYS B CA  1 
ATOM   4942 C  C   . CYS B 1 243 ? 60.438  70.084  56.139  1.00 63.83 ? 232  CYS B C   1 
ATOM   4943 O  O   . CYS B 1 243 ? 61.607  69.796  56.400  1.00 63.83 ? 232  CYS B O   1 
ATOM   4944 C  CB  . CYS B 1 243 ? 59.441  70.253  53.848  1.00 63.83 ? 232  CYS B CB  1 
ATOM   4945 S  SG  . CYS B 1 243 ? 57.711  69.797  54.111  1.00 63.83 ? 232  CYS B SG  1 
ATOM   4946 N  N   . GLY B 1 244 ? 59.405  69.589  56.819  1.00 61.71 ? 233  GLY B N   1 
ATOM   4947 C  CA  . GLY B 1 244 ? 59.593  68.635  57.892  1.00 61.71 ? 233  GLY B CA  1 
ATOM   4948 C  C   . GLY B 1 244 ? 59.933  67.236  57.441  1.00 61.71 ? 233  GLY B C   1 
ATOM   4949 O  O   . GLY B 1 244 ? 60.286  66.396  58.273  1.00 61.71 ? 233  GLY B O   1 
ATOM   4950 N  N   . GLU B 1 245 ? 59.835  66.964  56.140  1.00 62.75 ? 234  GLU B N   1 
ATOM   4951 C  CA  . GLU B 1 245 ? 60.224  65.665  55.612  1.00 62.75 ? 234  GLU B CA  1 
ATOM   4952 C  C   . GLU B 1 245 ? 61.722  65.423  55.708  1.00 62.75 ? 234  GLU B C   1 
ATOM   4953 O  O   . GLU B 1 245 ? 62.162  64.288  55.495  1.00 62.75 ? 234  GLU B O   1 
ATOM   4954 C  CB  . GLU B 1 245 ? 59.775  65.545  54.156  1.00 62.75 ? 234  GLU B CB  1 
ATOM   4955 N  N   . ASP B 1 246 ? 62.510  66.453  56.007  1.00 61.47 ? 235  ASP B N   1 
ATOM   4956 C  CA  . ASP B 1 246 ? 63.958  66.335  56.099  1.00 61.47 ? 235  ASP B CA  1 
ATOM   4957 C  C   . ASP B 1 246 ? 64.498  66.728  57.464  1.00 61.47 ? 235  ASP B C   1 
ATOM   4958 O  O   . ASP B 1 246 ? 65.260  65.963  58.065  1.00 61.47 ? 235  ASP B O   1 
ATOM   4959 C  CB  . ASP B 1 246 ? 64.614  67.198  55.012  1.00 61.47 ? 235  ASP B CB  1 
ATOM   4960 C  CG  . ASP B 1 246 ? 64.506  66.579  53.634  1.00 61.47 ? 235  ASP B CG  1 
ATOM   4961 O  OD1 . ASP B 1 246 ? 63.941  67.231  52.732  1.00 61.47 ? 235  ASP B OD1 1 
ATOM   4962 O  OD2 . ASP B 1 246 ? 64.981  65.438  53.455  1.00 61.47 ? 235  ASP B OD2 1 
ATOM   4963 N  N   . TYR B 1 247 ? 64.122  67.895  57.976  1.00 56.76 ? 236  TYR B N   1 
ATOM   4964 C  CA  . TYR B 1 247 ? 64.728  68.467  59.169  1.00 56.76 ? 236  TYR B CA  1 
ATOM   4965 C  C   . TYR B 1 247 ? 63.876  68.202  60.402  1.00 56.76 ? 236  TYR B C   1 
ATOM   4966 O  O   . TYR B 1 247 ? 62.687  67.889  60.316  1.00 56.76 ? 236  TYR B O   1 
ATOM   4967 C  CB  . TYR B 1 247 ? 64.914  69.977  59.010  1.00 56.76 ? 236  TYR B CB  1 
ATOM   4968 C  CG  . TYR B 1 247 ? 65.881  70.378  57.929  1.00 56.76 ? 236  TYR B CG  1 
ATOM   4969 C  CD1 . TYR B 1 247 ? 67.121  70.912  58.243  1.00 56.76 ? 236  TYR B CD1 1 
ATOM   4970 C  CD2 . TYR B 1 247 ? 65.549  70.234  56.592  1.00 56.76 ? 236  TYR B CD2 1 
ATOM   4971 C  CE1 . TYR B 1 247 ? 68.005  71.285  57.255  1.00 56.76 ? 236  TYR B CE1 1 
ATOM   4972 C  CE2 . TYR B 1 247 ? 66.420  70.604  55.599  1.00 56.76 ? 236  TYR B CE2 1 
ATOM   4973 C  CZ  . TYR B 1 247 ? 67.648  71.128  55.933  1.00 56.76 ? 236  TYR B CZ  1 
ATOM   4974 O  OH  . TYR B 1 247 ? 68.518  71.493  54.935  1.00 56.76 ? 236  TYR B OH  1 
ATOM   4975 N  N   . VAL B 1 248 ? 64.512  68.337  61.564  1.00 51.47 ? 237  VAL B N   1 
ATOM   4976 C  CA  . VAL B 1 248 ? 63.819  68.361  62.845  1.00 51.47 ? 237  VAL B CA  1 
ATOM   4977 C  C   . VAL B 1 248 ? 64.488  69.426  63.695  1.00 51.47 ? 237  VAL B C   1 
ATOM   4978 O  O   . VAL B 1 248 ? 65.689  69.336  63.966  1.00 51.47 ? 237  VAL B O   1 
ATOM   4979 C  CB  . VAL B 1 248 ? 63.860  67.006  63.567  1.00 51.47 ? 237  VAL B CB  1 
ATOM   4980 C  CG1 . VAL B 1 248 ? 63.211  67.119  64.934  1.00 51.47 ? 237  VAL B CG1 1 
ATOM   4981 C  CG2 . VAL B 1 248 ? 63.181  65.947  62.736  1.00 51.47 ? 237  VAL B CG2 1 
ATOM   4982 N  N   . PHE B 1 249 ? 63.724  70.430  64.113  1.00 47.94 ? 238  PHE B N   1 
ATOM   4983 C  CA  . PHE B 1 249 ? 64.224  71.498  64.969  1.00 47.94 ? 238  PHE B CA  1 
ATOM   4984 C  C   . PHE B 1 249 ? 63.699  71.282  66.379  1.00 47.94 ? 238  PHE B C   1 
ATOM   4985 O  O   . PHE B 1 249 ? 62.483  71.281  66.598  1.00 47.94 ? 238  PHE B O   1 
ATOM   4986 C  CB  . PHE B 1 249 ? 63.798  72.872  64.456  1.00 47.94 ? 238  PHE B CB  1 
ATOM   4987 C  CG  . PHE B 1 249 ? 64.017  73.071  62.988  1.00 47.94 ? 238  PHE B CG  1 
ATOM   4988 C  CD1 . PHE B 1 249 ? 65.194  73.620  62.523  1.00 47.94 ? 238  PHE B CD1 1 
ATOM   4989 C  CD2 . PHE B 1 249 ? 63.037  72.732  62.076  1.00 47.94 ? 238  PHE B CD2 1 
ATOM   4990 C  CE1 . PHE B 1 249 ? 65.397  73.813  61.178  1.00 47.94 ? 238  PHE B CE1 1 
ATOM   4991 C  CE2 . PHE B 1 249 ? 63.235  72.924  60.728  1.00 47.94 ? 238  PHE B CE2 1 
ATOM   4992 C  CZ  . PHE B 1 249 ? 64.416  73.466  60.279  1.00 47.94 ? 238  PHE B CZ  1 
ATOM   4993 N  N   . PHE B 1 250 ? 64.609  71.106  67.329  1.00 43.62 ? 239  PHE B N   1 
ATOM   4994 C  CA  . PHE B 1 250 ? 64.260  71.012  68.737  1.00 43.62 ? 239  PHE B CA  1 
ATOM   4995 C  C   . PHE B 1 250 ? 64.551  72.351  69.394  1.00 43.62 ? 239  PHE B C   1 
ATOM   4996 O  O   . PHE B 1 250 ? 65.690  72.824  69.366  1.00 43.62 ? 239  PHE B O   1 
ATOM   4997 C  CB  . PHE B 1 250 ? 65.045  69.903  69.432  1.00 43.62 ? 239  PHE B CB  1 
ATOM   4998 C  CG  . PHE B 1 250 ? 64.746  68.527  68.920  1.00 43.62 ? 239  PHE B CG  1 
ATOM   4999 C  CD1 . PHE B 1 250 ? 63.686  67.805  69.428  1.00 43.62 ? 239  PHE B CD1 1 
ATOM   5000 C  CD2 . PHE B 1 250 ? 65.536  67.946  67.953  1.00 43.62 ? 239  PHE B CD2 1 
ATOM   5001 C  CE1 . PHE B 1 250 ? 63.414  66.542  68.970  1.00 43.62 ? 239  PHE B CE1 1 
ATOM   5002 C  CE2 . PHE B 1 250 ? 65.265  66.682  67.494  1.00 43.62 ? 239  PHE B CE2 1 
ATOM   5003 C  CZ  . PHE B 1 250 ? 64.203  65.980  68.003  1.00 43.62 ? 239  PHE B CZ  1 
ATOM   5004 N  N   . HIS B 1 251 ? 63.529  72.950  69.993  1.00 39.88 ? 240  HIS B N   1 
ATOM   5005 C  CA  . HIS B 1 251 ? 63.686  74.194  70.736  1.00 39.88 ? 240  HIS B CA  1 
ATOM   5006 C  C   . HIS B 1 251 ? 63.926  73.849  72.199  1.00 39.88 ? 240  HIS B C   1 
ATOM   5007 O  O   . HIS B 1 251 ? 63.046  73.300  72.867  1.00 39.88 ? 240  HIS B O   1 
ATOM   5008 C  CB  . HIS B 1 251 ? 62.455  75.081  70.575  1.00 39.88 ? 240  HIS B CB  1 
ATOM   5009 C  CG  . HIS B 1 251 ? 62.632  76.463  71.122  1.00 39.88 ? 240  HIS B CG  1 
ATOM   5010 N  ND1 . HIS B 1 251 ? 61.569  77.274  71.450  1.00 39.88 ? 240  HIS B ND1 1 
ATOM   5011 C  CD2 . HIS B 1 251 ? 63.748  77.176  71.398  1.00 39.88 ? 240  HIS B CD2 1 
ATOM   5012 C  CE1 . HIS B 1 251 ? 62.023  78.427  71.905  1.00 39.88 ? 240  HIS B CE1 1 
ATOM   5013 N  NE2 . HIS B 1 251 ? 63.342  78.393  71.884  1.00 39.88 ? 240  HIS B NE2 1 
ATOM   5014 N  N   . LEU B 1 252 ? 65.119  74.166  72.695  1.00 37.79 ? 241  LEU B N   1 
ATOM   5015 C  CA  . LEU B 1 252 ? 65.457  73.951  74.099  1.00 37.79 ? 241  LEU B CA  1 
ATOM   5016 C  C   . LEU B 1 252 ? 64.893  75.113  74.901  1.00 37.79 ? 241  LEU B C   1 
ATOM   5017 O  O   . LEU B 1 252 ? 65.556  76.124  75.126  1.00 37.79 ? 241  LEU B O   1 
ATOM   5018 C  CB  . LEU B 1 252 ? 66.963  73.828  74.286  1.00 37.79 ? 241  LEU B CB  1 
ATOM   5019 C  CG  . LEU B 1 252 ? 67.691  72.842  73.378  1.00 37.79 ? 241  LEU B CG  1 
ATOM   5020 C  CD1 . LEU B 1 252 ? 69.184  72.921  73.616  1.00 37.79 ? 241  LEU B CD1 1 
ATOM   5021 C  CD2 . LEU B 1 252 ? 67.189  71.436  73.616  1.00 37.79 ? 241  LEU B CD2 1 
ATOM   5022 N  N   . ASP B 1 253 ? 63.647  74.963  75.336  1.00 38.14 ? 242  ASP B N   1 
ATOM   5023 C  CA  . ASP B 1 253 ? 62.949  75.970  76.131  1.00 38.14 ? 242  ASP B CA  1 
ATOM   5024 C  C   . ASP B 1 253 ? 62.701  75.350  77.501  1.00 38.14 ? 242  ASP B C   1 
ATOM   5025 O  O   . ASP B 1 253 ? 61.622  74.827  77.775  1.00 38.14 ? 242  ASP B O   1 
ATOM   5026 C  CB  . ASP B 1 253 ? 61.652  76.386  75.450  1.00 38.14 ? 242  ASP B CB  1 
ATOM   5027 C  CG  . ASP B 1 253 ? 61.209  77.777  75.831  1.00 38.14 ? 242  ASP B CG  1 
ATOM   5028 O  OD1 . ASP B 1 253 ? 62.070  78.611  76.176  1.00 38.14 ? 242  ASP B OD1 1 
ATOM   5029 O  OD2 . ASP B 1 253 ? 59.993  78.040  75.782  1.00 38.14 ? 242  ASP B OD2 1 
ATOM   5030 N  N   . ILE B 1 254 ? 63.705  75.432  78.374  1.00 31.84 ? 243  ILE B N   1 
ATOM   5031 C  CA  . ILE B 1 254 ? 63.679  74.633  79.594  1.00 31.84 ? 243  ILE B CA  1 
ATOM   5032 C  C   . ILE B 1 254 ? 62.520  75.047  80.489  1.00 31.84 ? 243  ILE B C   1 
ATOM   5033 O  O   . ILE B 1 254 ? 61.859  74.198  81.096  1.00 31.84 ? 243  ILE B O   1 
ATOM   5034 C  CB  . ILE B 1 254 ? 65.028  74.724  80.328  1.00 31.84 ? 243  ILE B CB  1 
ATOM   5035 C  CG1 . ILE B 1 254 ? 65.378  76.176  80.652  1.00 31.84 ? 243  ILE B CG1 1 
ATOM   5036 C  CG2 . ILE B 1 254 ? 66.120  74.085  79.493  1.00 31.84 ? 243  ILE B CG2 1 
ATOM   5037 C  CD1 . ILE B 1 254 ? 66.657  76.330  81.423  1.00 31.84 ? 243  ILE B CD1 1 
ATOM   5038 N  N   . PHE B 1 255 ? 62.246  76.344  80.586  1.00 30.43 ? 244  PHE B N   1 
ATOM   5039 C  CA  . PHE B 1 255 ? 61.222  76.850  81.488  1.00 30.43 ? 244  PHE B CA  1 
ATOM   5040 C  C   . PHE B 1 255 ? 59.887  77.071  80.794  1.00 30.43 ? 244  PHE B C   1 
ATOM   5041 O  O   . PHE B 1 255 ? 58.990  77.681  81.380  1.00 30.43 ? 244  PHE B O   1 
ATOM   5042 C  CB  . PHE B 1 255 ? 61.693  78.150  82.142  1.00 30.43 ? 244  PHE B CB  1 
ATOM   5043 C  CG  . PHE B 1 255 ? 62.648  77.947  83.288  1.00 30.43 ? 244  PHE B CG  1 
ATOM   5044 C  CD1 . PHE B 1 255 ? 62.359  77.055  84.304  1.00 30.43 ? 244  PHE B CD1 1 
ATOM   5045 C  CD2 . PHE B 1 255 ? 63.832  78.654  83.349  1.00 30.43 ? 244  PHE B CD2 1 
ATOM   5046 C  CE1 . PHE B 1 255 ? 63.231  76.871  85.347  1.00 30.43 ? 244  PHE B CE1 1 
ATOM   5047 C  CE2 . PHE B 1 255 ? 64.705  78.471  84.393  1.00 30.43 ? 244  PHE B CE2 1 
ATOM   5048 C  CZ  . PHE B 1 255 ? 64.403  77.581  85.393  1.00 30.43 ? 244  PHE B CZ  1 
ATOM   5049 N  N   . GLY B 1 256 ? 59.736  76.600  79.560  1.00 38.35 ? 245  GLY B N   1 
ATOM   5050 C  CA  . GLY B 1 256 ? 58.457  76.650  78.882  1.00 38.35 ? 245  GLY B CA  1 
ATOM   5051 C  C   . GLY B 1 256 ? 57.904  78.049  78.734  1.00 38.35 ? 245  GLY B C   1 
ATOM   5052 O  O   . GLY B 1 256 ? 56.728  78.289  79.015  1.00 38.35 ? 245  GLY B O   1 
ATOM   5053 N  N   . GLN B 1 257 ? 58.743  78.985  78.297  1.00 42.86 ? 246  GLN B N   1 
ATOM   5054 C  CA  . GLN B 1 257 ? 58.308  80.363  78.126  1.00 42.86 ? 246  GLN B CA  1 
ATOM   5055 C  C   . GLN B 1 257 ? 57.459  80.560  76.881  1.00 42.86 ? 246  GLN B C   1 
ATOM   5056 O  O   . GLN B 1 257 ? 56.660  81.500  76.835  1.00 42.86 ? 246  GLN B O   1 
ATOM   5057 C  CB  . GLN B 1 257 ? 59.520  81.288  78.072  1.00 42.86 ? 246  GLN B CB  1 
ATOM   5058 C  CG  . GLN B 1 257 ? 60.374  81.221  79.314  1.00 42.86 ? 246  GLN B CG  1 
ATOM   5059 C  CD  . GLN B 1 257 ? 61.382  82.340  79.383  1.00 42.86 ? 246  GLN B CD  1 
ATOM   5060 O  OE1 . GLN B 1 257 ? 61.531  83.113  78.437  1.00 42.86 ? 246  GLN B OE1 1 
ATOM   5061 N  NE2 . GLN B 1 257 ? 62.082  82.437  80.506  1.00 42.86 ? 246  GLN B NE2 1 
ATOM   5062 N  N   . SER B 1 258 ? 57.615  79.707  75.877  1.00 43.87 ? 247  SER B N   1 
ATOM   5063 C  CA  . SER B 1 258 ? 56.810  79.777  74.668  1.00 43.87 ? 247  SER B CA  1 
ATOM   5064 C  C   . SER B 1 258 ? 55.496  79.023  74.797  1.00 43.87 ? 247  SER B C   1 
ATOM   5065 O  O   . SER B 1 258 ? 54.701  79.030  73.854  1.00 43.87 ? 247  SER B O   1 
ATOM   5066 C  CB  . SER B 1 258 ? 57.601  79.224  73.480  1.00 43.87 ? 247  SER B CB  1 
ATOM   5067 O  OG  . SER B 1 258 ? 57.919  77.860  73.672  1.00 43.87 ? 247  SER B OG  1 
ATOM   5068 N  N   . LEU B 1 259 ? 55.249  78.381  75.936  1.00 44.77 ? 248  LEU B N   1 
ATOM   5069 C  CA  . LEU B 1 259 ? 54.053  77.581  76.159  1.00 44.77 ? 248  LEU B CA  1 
ATOM   5070 C  C   . LEU B 1 259 ? 53.222  78.139  77.308  1.00 44.77 ? 248  LEU B C   1 
ATOM   5071 O  O   . LEU B 1 259 ? 52.491  77.401  77.968  1.00 44.77 ? 248  LEU B O   1 
ATOM   5072 C  CB  . LEU B 1 259 ? 54.429  76.128  76.439  1.00 44.77 ? 248  LEU B CB  1 
ATOM   5073 C  CG  . LEU B 1 259 ? 55.129  75.373  75.315  1.00 44.77 ? 248  LEU B CG  1 
ATOM   5074 C  CD1 . LEU B 1 259 ? 55.835  74.167  75.874  1.00 44.77 ? 248  LEU B CD1 1 
ATOM   5075 C  CD2 . LEU B 1 259 ? 54.130  74.955  74.261  1.00 44.77 ? 248  LEU B CD2 1 
ATOM   5076 N  N   . GLN B 1 260 ? 53.327  79.443  77.557  1.00 48.08 ? 249  GLN B N   1 
ATOM   5077 C  CA  . GLN B 1 260 ? 52.651  80.076  78.687  1.00 48.08 ? 249  GLN B CA  1 
ATOM   5078 C  C   . GLN B 1 260 ? 52.986  79.355  79.989  1.00 48.08 ? 249  GLN B C   1 
ATOM   5079 O  O   . GLN B 1 260 ? 52.118  79.088  80.822  1.00 48.08 ? 249  GLN B O   1 
ATOM   5080 C  CB  . GLN B 1 260 ? 51.138  80.127  78.464  1.00 48.08 ? 249  GLN B CB  1 
ATOM   5081 C  CG  . GLN B 1 260 ? 50.709  81.125  77.402  1.00 48.08 ? 249  GLN B CG  1 
ATOM   5082 C  CD  . GLN B 1 260 ? 50.480  80.483  76.051  1.00 48.08 ? 249  GLN B CD  1 
ATOM   5083 O  OE1 . GLN B 1 260 ? 49.950  79.377  75.957  1.00 48.08 ? 249  GLN B OE1 1 
ATOM   5084 N  NE2 . GLN B 1 260 ? 50.886  81.173  74.993  1.00 48.08 ? 249  GLN B NE2 1 
ATOM   5085 N  N   . GLY B 1 261 ? 54.266  79.032  80.160  1.00 42.05 ? 250  GLY B N   1 
ATOM   5086 C  CA  . GLY B 1 261 ? 54.745  78.365  81.345  1.00 42.05 ? 250  GLY B CA  1 
ATOM   5087 C  C   . GLY B 1 261 ? 54.817  76.857  81.248  1.00 42.05 ? 250  GLY B C   1 
ATOM   5088 O  O   . GLY B 1 261 ? 55.505  76.234  82.059  1.00 42.05 ? 250  GLY B O   1 
ATOM   5089 N  N   . GLY B 1 262 ? 54.125  76.249  80.289  1.00 45.60 ? 251  GLY B N   1 
ATOM   5090 C  CA  . GLY B 1 262 ? 54.178  74.805  80.142  1.00 45.60 ? 251  GLY B CA  1 
ATOM   5091 C  C   . GLY B 1 262 ? 53.683  74.048  81.352  1.00 45.60 ? 251  GLY B C   1 
ATOM   5092 O  O   . GLY B 1 262 ? 54.131  72.925  81.600  1.00 45.60 ? 251  GLY B O   1 
ATOM   5093 N  N   . GLN B 1 263 ? 52.756  74.628  82.105  1.00 47.02 ? 252  GLN B N   1 
ATOM   5094 C  CA  . GLN B 1 263 ? 52.256  74.047  83.342  1.00 47.02 ? 252  GLN B CA  1 
ATOM   5095 C  C   . GLN B 1 263 ? 50.796  73.665  83.143  1.00 47.02 ? 252  GLN B C   1 
ATOM   5096 O  O   . GLN B 1 263 ? 49.972  74.516  82.791  1.00 47.02 ? 252  GLN B O   1 
ATOM   5097 C  CB  . GLN B 1 263 ? 52.417  75.042  84.495  1.00 47.02 ? 252  GLN B CB  1 
ATOM   5098 C  CG  . GLN B 1 263 ? 51.545  74.806  85.729  1.00 47.02 ? 252  GLN B CG  1 
ATOM   5099 C  CD  . GLN B 1 263 ? 52.194  73.887  86.734  1.00 47.02 ? 252  GLN B CD  1 
ATOM   5100 O  OE1 . GLN B 1 263 ? 53.378  73.574  86.632  1.00 47.02 ? 252  GLN B OE1 1 
ATOM   5101 N  NE2 . GLN B 1 263 ? 51.421  73.449  87.717  1.00 47.02 ? 252  GLN B NE2 1 
ATOM   5102 N  N   . GLY B 1 264 ? 50.479  72.395  83.367  1.00 52.70 ? 253  GLY B N   1 
ATOM   5103 C  CA  . GLY B 1 264 ? 49.110  71.942  83.362  1.00 52.70 ? 253  GLY B CA  1 
ATOM   5104 C  C   . GLY B 1 264 ? 48.649  71.447  82.005  1.00 52.70 ? 253  GLY B C   1 
ATOM   5105 O  O   . GLY B 1 264 ? 49.211  71.802  80.965  1.00 52.70 ? 253  GLY B O   1 
ATOM   5106 N  N   . PRO B 1 265 ? 47.609  70.603  81.992  1.00 59.96 ? 254  PRO B N   1 
ATOM   5107 C  CA  . PRO B 1 265 ? 47.081  70.042  80.726  1.00 59.96 ? 254  PRO B CA  1 
ATOM   5108 C  C   . PRO B 1 265 ? 46.124  70.972  79.983  1.00 59.96 ? 254  PRO B C   1 
ATOM   5109 O  O   . PRO B 1 265 ? 44.902  70.899  80.095  1.00 59.96 ? 254  PRO B O   1 
ATOM   5110 C  CB  . PRO B 1 265 ? 46.367  68.773  81.195  1.00 59.96 ? 254  PRO B CB  1 
ATOM   5111 C  CG  . PRO B 1 265 ? 45.971  69.062  82.590  1.00 59.96 ? 254  PRO B CG  1 
ATOM   5112 C  CD  . PRO B 1 265 ? 47.051  69.914  83.167  1.00 59.96 ? 254  PRO B CD  1 
ATOM   5113 N  N   . ALA B 1 266 ? 46.689  71.882  79.198  1.00 56.67 ? 255  ALA B N   1 
ATOM   5114 C  CA  . ALA B 1 266 ? 45.901  72.767  78.358  1.00 56.67 ? 255  ALA B CA  1 
ATOM   5115 C  C   . ALA B 1 266 ? 46.483  72.796  76.954  1.00 56.67 ? 255  ALA B C   1 
ATOM   5116 O  O   . ALA B 1 266 ? 47.693  72.622  76.780  1.00 56.67 ? 255  ALA B O   1 
ATOM   5117 C  CB  . ALA B 1 266 ? 45.864  74.191  78.930  1.00 56.67 ? 255  ALA B CB  1 
ATOM   5118 N  N   . PRO B 1 267 ? 45.651  73.000  75.930  1.00 55.74 ? 256  PRO B N   1 
ATOM   5119 C  CA  . PRO B 1 267 ? 46.190  73.120  74.567  1.00 55.74 ? 256  PRO B CA  1 
ATOM   5120 C  C   . PRO B 1 267 ? 46.948  74.429  74.393  1.00 55.74 ? 256  PRO B C   1 
ATOM   5121 O  O   . PRO B 1 267 ? 46.433  75.506  74.699  1.00 55.74 ? 256  PRO B O   1 
ATOM   5122 C  CB  . PRO B 1 267 ? 44.945  73.067  73.674  1.00 55.74 ? 256  PRO B CB  1 
ATOM   5123 C  CG  . PRO B 1 267 ? 43.836  72.585  74.534  1.00 55.74 ? 256  PRO B CG  1 
ATOM   5124 C  CD  . PRO B 1 267 ? 44.181  72.927  75.942  1.00 55.74 ? 256  PRO B CD  1 
ATOM   5125 N  N   . ARG B 1 268 ? 48.176  74.324  73.895  1.00 50.84 ? 257  ARG B N   1 
ATOM   5126 C  CA  . ARG B 1 268 ? 49.055  75.465  73.690  1.00 50.84 ? 257  ARG B CA  1 
ATOM   5127 C  C   . ARG B 1 268 ? 49.357  75.615  72.208  1.00 50.84 ? 257  ARG B C   1 
ATOM   5128 O  O   . ARG B 1 268 ? 49.600  74.626  71.511  1.00 50.84 ? 257  ARG B O   1 
ATOM   5129 C  CB  . ARG B 1 268 ? 50.363  75.302  74.471  1.00 50.84 ? 257  ARG B CB  1 
ATOM   5130 C  CG  . ARG B 1 268 ? 50.299  75.793  75.902  1.00 50.84 ? 257  ARG B CG  1 
ATOM   5131 C  CD  . ARG B 1 268 ? 49.448  74.883  76.756  1.00 50.84 ? 257  ARG B CD  1 
ATOM   5132 N  NE  . ARG B 1 268 ? 49.381  75.331  78.142  1.00 50.84 ? 257  ARG B NE  1 
ATOM   5133 C  CZ  . ARG B 1 268 ? 50.185  74.915  79.113  1.00 50.84 ? 257  ARG B CZ  1 
ATOM   5134 N  NH1 . ARG B 1 268 ? 51.137  74.028  78.868  1.00 50.84 ? 257  ARG B NH1 1 
ATOM   5135 N  NH2 . ARG B 1 268 ? 50.033  75.388  80.340  1.00 50.84 ? 257  ARG B NH2 1 
ATOM   5136 N  N   . ARG B 1 269 ? 49.341  76.859  71.730  1.00 54.15 ? 258  ARG B N   1 
ATOM   5137 C  CA  . ARG B 1 269 ? 49.673  77.192  70.346  1.00 54.15 ? 258  ARG B CA  1 
ATOM   5138 C  C   . ARG B 1 269 ? 50.807  78.207  70.369  1.00 54.15 ? 258  ARG B C   1 
ATOM   5139 O  O   . ARG B 1 269 ? 50.561  79.423  70.370  1.00 54.15 ? 258  ARG B O   1 
ATOM   5140 C  CB  . ARG B 1 269 ? 48.458  77.739  69.602  1.00 54.15 ? 258  ARG B CB  1 
ATOM   5141 C  CG  . ARG B 1 269 ? 47.429  76.680  69.257  1.00 54.15 ? 258  ARG B CG  1 
ATOM   5142 C  CD  . ARG B 1 269 ? 46.015  77.213  69.318  1.00 54.15 ? 258  ARG B CD  1 
ATOM   5143 N  NE  . ARG B 1 269 ? 45.032  76.132  69.255  1.00 54.15 ? 258  ARG B NE  1 
ATOM   5144 C  CZ  . ARG B 1 269 ? 44.276  75.724  70.272  1.00 54.15 ? 258  ARG B CZ  1 
ATOM   5145 N  NH1 . ARG B 1 269 ? 44.364  76.295  71.467  1.00 54.15 ? 258  ARG B NH1 1 
ATOM   5146 N  NH2 . ARG B 1 269 ? 43.418  74.729  70.091  1.00 54.15 ? 258  ARG B NH2 1 
ATOM   5147 N  N   . PRO B 1 270 ? 52.064  77.761  70.384  1.00 49.01 ? 259  PRO B N   1 
ATOM   5148 C  CA  . PRO B 1 270 ? 53.188  78.693  70.495  1.00 49.01 ? 259  PRO B CA  1 
ATOM   5149 C  C   . PRO B 1 270 ? 53.554  79.401  69.202  1.00 49.01 ? 259  PRO B C   1 
ATOM   5150 O  O   . PRO B 1 270 ? 54.561  80.112  69.176  1.00 49.01 ? 259  PRO B O   1 
ATOM   5151 C  CB  . PRO B 1 270 ? 54.330  77.773  70.948  1.00 49.01 ? 259  PRO B CB  1 
ATOM   5152 C  CG  . PRO B 1 270 ? 54.027  76.479  70.312  1.00 49.01 ? 259  PRO B CG  1 
ATOM   5153 C  CD  . PRO B 1 270 ? 52.524  76.370  70.231  1.00 49.01 ? 259  PRO B CD  1 
ATOM   5154 N  N   . TRP B 1 271 ? 52.764  79.236  68.143  1.00 54.61 ? 260  TRP B N   1 
ATOM   5155 C  CA  . TRP B 1 271 ? 53.058  79.827  66.848  1.00 54.61 ? 260  TRP B CA  1 
ATOM   5156 C  C   . TRP B 1 271 ? 52.097  80.944  66.472  1.00 54.61 ? 260  TRP B C   1 
ATOM   5157 O  O   . TRP B 1 271 ? 52.208  81.491  65.370  1.00 54.61 ? 260  TRP B O   1 
ATOM   5158 C  CB  . TRP B 1 271 ? 53.037  78.749  65.759  1.00 54.61 ? 260  TRP B CB  1 
ATOM   5159 C  CG  . TRP B 1 271 ? 51.894  77.789  65.869  1.00 54.61 ? 260  TRP B CG  1 
ATOM   5160 C  CD1 . TRP B 1 271 ? 51.957  76.486  66.256  1.00 54.61 ? 260  TRP B CD1 1 
ATOM   5161 C  CD2 . TRP B 1 271 ? 50.516  78.053  65.577  1.00 54.61 ? 260  TRP B CD2 1 
ATOM   5162 N  NE1 . TRP B 1 271 ? 50.707  75.920  66.229  1.00 54.61 ? 260  TRP B NE1 1 
ATOM   5163 C  CE2 . TRP B 1 271 ? 49.804  76.863  65.815  1.00 54.61 ? 260  TRP B CE2 1 
ATOM   5164 C  CE3 . TRP B 1 271 ? 49.816  79.180  65.137  1.00 54.61 ? 260  TRP B CE3 1 
ATOM   5165 C  CZ2 . TRP B 1 271 ? 48.429  76.768  65.630  1.00 54.61 ? 260  TRP B CZ2 1 
ATOM   5166 C  CZ3 . TRP B 1 271 ? 48.452  79.083  64.956  1.00 54.61 ? 260  TRP B CZ3 1 
ATOM   5167 C  CH2 . TRP B 1 271 ? 47.773  77.887  65.201  1.00 54.61 ? 260  TRP B CH2 1 
ATOM   5168 N  N   . GLU B 1 272 ? 51.163  81.300  67.348  1.00 58.11 ? 261  GLU B N   1 
ATOM   5169 C  CA  . GLU B 1 272 ? 50.178  82.334  67.072  1.00 58.11 ? 261  GLU B CA  1 
ATOM   5170 C  C   . GLU B 1 272 ? 50.512  83.581  67.877  1.00 58.11 ? 261  GLU B C   1 
ATOM   5171 O  O   . GLU B 1 272 ? 50.696  83.511  69.096  1.00 58.11 ? 261  GLU B O   1 
ATOM   5172 C  CB  . GLU B 1 272 ? 48.764  81.834  67.390  1.00 58.11 ? 261  GLU B CB  1 
ATOM   5173 C  CG  . GLU B 1 272 ? 48.292  82.036  68.823  1.00 58.11 ? 261  GLU B CG  1 
ATOM   5174 C  CD  . GLU B 1 272 ? 46.848  81.619  69.014  1.00 58.11 ? 261  GLU B CD  1 
ATOM   5175 O  OE1 . GLU B 1 272 ? 46.072  81.701  68.039  1.00 58.11 ? 261  GLU B OE1 1 
ATOM   5176 O  OE2 . GLU B 1 272 ? 46.487  81.207  70.136  1.00 58.11 ? 261  GLU B OE2 1 
ATOM   5177 N  N   . ARG B 1 273 ? 50.614  84.715  67.184  1.00 56.78 ? 262  ARG B N   1 
ATOM   5178 C  CA  . ARG B 1 273 ? 50.794  86.013  67.815  1.00 56.78 ? 262  ARG B CA  1 
ATOM   5179 C  C   . ARG B 1 273 ? 49.707  87.005  67.437  1.00 56.78 ? 262  ARG B C   1 
ATOM   5180 O  O   . ARG B 1 273 ? 49.795  88.174  67.829  1.00 56.78 ? 262  ARG B O   1 
ATOM   5181 C  CB  . ARG B 1 273 ? 52.159  86.607  67.443  1.00 56.78 ? 262  ARG B CB  1 
ATOM   5182 C  CG  . ARG B 1 273 ? 53.346  85.795  67.906  1.00 56.78 ? 262  ARG B CG  1 
ATOM   5183 C  CD  . ARG B 1 273 ? 53.626  86.031  69.382  1.00 56.78 ? 262  ARG B CD  1 
ATOM   5184 N  NE  . ARG B 1 273 ? 54.904  85.472  69.818  1.00 56.78 ? 262  ARG B NE  1 
ATOM   5185 C  CZ  . ARG B 1 273 ? 55.239  84.187  69.753  1.00 56.78 ? 262  ARG B CZ  1 
ATOM   5186 N  NH1 . ARG B 1 273 ? 54.387  83.282  69.296  1.00 56.78 ? 262  ARG B NH1 1 
ATOM   5187 N  NH2 . ARG B 1 273 ? 56.433  83.801  70.176  1.00 56.78 ? 262  ARG B NH2 1 
ATOM   5188 N  N   . GLY B 1 274 ? 48.695  86.584  66.687  1.00 62.86 ? 263  GLY B N   1 
ATOM   5189 C  CA  . GLY B 1 274 ? 47.706  87.525  66.194  1.00 62.86 ? 263  GLY B CA  1 
ATOM   5190 C  C   . GLY B 1 274 ? 48.314  88.593  65.313  1.00 62.86 ? 263  GLY B C   1 
ATOM   5191 O  O   . GLY B 1 274 ? 47.859  89.743  65.327  1.00 62.86 ? 263  GLY B O   1 
ATOM   5192 N  N   . ASP B 1 275 ? 49.339  88.236  64.541  1.00 64.44 ? 264  ASP B N   1 
ATOM   5193 C  CA  . ASP B 1 275 ? 50.016  89.166  63.651  1.00 64.44 ? 264  ASP B CA  1 
ATOM   5194 C  C   . ASP B 1 275 ? 49.583  89.006  62.201  1.00 64.44 ? 264  ASP B C   1 
ATOM   5195 O  O   . ASP B 1 275 ? 50.172  89.635  61.317  1.00 64.44 ? 264  ASP B O   1 
ATOM   5196 C  CB  . ASP B 1 275 ? 51.532  88.986  63.759  1.00 64.44 ? 264  ASP B CB  1 
ATOM   5197 N  N   . GLY B 1 276 ? 48.576  88.182  61.936  1.00 61.80 ? 265  GLY B N   1 
ATOM   5198 C  CA  . GLY B 1 276 ? 48.136  87.892  60.582  1.00 61.80 ? 265  GLY B CA  1 
ATOM   5199 C  C   . GLY B 1 276 ? 48.947  86.788  59.945  1.00 61.80 ? 265  GLY B C   1 
ATOM   5200 O  O   . GLY B 1 276 ? 48.411  85.955  59.212  1.00 61.80 ? 265  GLY B O   1 
ATOM   5201 N  N   . GLN B 1 277 ? 50.250  86.774  60.215  1.00 59.58 ? 266  GLN B N   1 
ATOM   5202 C  CA  . GLN B 1 277 ? 51.144  85.729  59.724  1.00 59.58 ? 266  GLN B CA  1 
ATOM   5203 C  C   . GLN B 1 277 ? 51.137  84.562  60.712  1.00 59.58 ? 266  GLN B C   1 
ATOM   5204 O  O   . GLN B 1 277 ? 52.066  84.345  61.491  1.00 59.58 ? 266  GLN B O   1 
ATOM   5205 C  CB  . GLN B 1 277 ? 52.542  86.298  59.516  1.00 59.58 ? 266  GLN B CB  1 
ATOM   5206 C  CG  . GLN B 1 277 ? 53.570  85.301  59.026  1.00 59.58 ? 266  GLN B CG  1 
ATOM   5207 C  CD  . GLN B 1 277 ? 54.916  85.942  58.761  1.00 59.58 ? 266  GLN B CD  1 
ATOM   5208 O  OE1 . GLN B 1 277 ? 55.572  85.635  57.769  1.00 59.58 ? 266  GLN B OE1 1 
ATOM   5209 N  NE2 . GLN B 1 277 ? 55.340  86.828  59.652  1.00 59.58 ? 266  GLN B NE2 1 
ATOM   5210 N  N   . ASP B 1 278 ? 50.038  83.812  60.674  1.00 59.46 ? 267  ASP B N   1 
ATOM   5211 C  CA  . ASP B 1 278 ? 49.852  82.626  61.503  1.00 59.46 ? 267  ASP B CA  1 
ATOM   5212 C  C   . ASP B 1 278 ? 49.625  81.361  60.695  1.00 59.46 ? 267  ASP B C   1 
ATOM   5213 O  O   . ASP B 1 278 ? 50.152  80.306  61.055  1.00 59.46 ? 267  ASP B O   1 
ATOM   5214 C  CB  . ASP B 1 278 ? 48.671  82.821  62.461  1.00 59.46 ? 267  ASP B CB  1 
ATOM   5215 C  CG  . ASP B 1 278 ? 48.997  83.753  63.603  1.00 59.46 ? 267  ASP B CG  1 
ATOM   5216 O  OD1 . ASP B 1 278 ? 50.180  83.819  63.994  1.00 59.46 ? 267  ASP B OD1 1 
ATOM   5217 O  OD2 . ASP B 1 278 ? 48.072  84.415  64.116  1.00 59.46 ? 267  ASP B OD2 1 
ATOM   5218 N  N   . VAL B 1 279 ? 48.850  81.432  59.613  1.00 58.88 ? 268  VAL B N   1 
ATOM   5219 C  CA  . VAL B 1 279 ? 48.628  80.247  58.792  1.00 58.88 ? 268  VAL B CA  1 
ATOM   5220 C  C   . VAL B 1 279 ? 49.961  79.681  58.324  1.00 58.88 ? 268  VAL B C   1 
ATOM   5221 O  O   . VAL B 1 279 ? 50.145  78.461  58.251  1.00 58.88 ? 268  VAL B O   1 
ATOM   5222 C  CB  . VAL B 1 279 ? 47.705  80.581  57.606  1.00 58.88 ? 268  VAL B CB  1 
ATOM   5223 N  N   . SER B 1 280 ? 50.910  80.559  57.997  1.00 58.30 ? 269  SER B N   1 
ATOM   5224 C  CA  . SER B 1 280 ? 52.252  80.102  57.659  1.00 58.30 ? 269  SER B CA  1 
ATOM   5225 C  C   . SER B 1 280 ? 53.001  79.613  58.891  1.00 58.30 ? 269  SER B C   1 
ATOM   5226 O  O   . SER B 1 280 ? 53.786  78.664  58.800  1.00 58.30 ? 269  SER B O   1 
ATOM   5227 C  CB  . SER B 1 280 ? 53.032  81.225  56.980  1.00 58.30 ? 269  SER B CB  1 
ATOM   5228 O  OG  . SER B 1 280 ? 54.248  80.745  56.436  1.00 58.30 ? 269  SER B OG  1 
ATOM   5229 N  N   . ALA B 1 281 ? 52.777  80.245  60.045  1.00 55.90 ? 270  ALA B N   1 
ATOM   5230 C  CA  . ALA B 1 281 ? 53.459  79.823  61.264  1.00 55.90 ? 270  ALA B CA  1 
ATOM   5231 C  C   . ALA B 1 281 ? 53.047  78.415  61.668  1.00 55.90 ? 270  ALA B C   1 
ATOM   5232 O  O   . ALA B 1 281 ? 53.879  77.630  62.134  1.00 55.90 ? 270  ALA B O   1 
ATOM   5233 C  CB  . ALA B 1 281 ? 53.169  80.807  62.393  1.00 55.90 ? 270  ALA B CB  1 
ATOM   5234 N  N   . ARG B 1 282 ? 51.766  78.078  61.507  1.00 56.59 ? 271  ARG B N   1 
ATOM   5235 C  CA  . ARG B 1 282 ? 51.316  76.727  61.827  1.00 56.59 ? 271  ARG B CA  1 
ATOM   5236 C  C   . ARG B 1 282 ? 51.991  75.695  60.935  1.00 56.59 ? 271  ARG B C   1 
ATOM   5237 O  O   . ARG B 1 282 ? 52.415  74.636  61.409  1.00 56.59 ? 271  ARG B O   1 
ATOM   5238 C  CB  . ARG B 1 282 ? 49.797  76.639  61.691  1.00 56.59 ? 271  ARG B CB  1 
ATOM   5239 C  CG  . ARG B 1 282 ? 49.226  75.254  61.920  1.00 56.59 ? 271  ARG B CG  1 
ATOM   5240 C  CD  . ARG B 1 282 ? 47.721  75.263  61.777  1.00 56.59 ? 271  ARG B CD  1 
ATOM   5241 N  NE  . ARG B 1 282 ? 47.136  73.941  61.971  1.00 56.59 ? 271  ARG B NE  1 
ATOM   5242 C  CZ  . ARG B 1 282 ? 45.830  73.696  61.957  1.00 56.59 ? 271  ARG B CZ  1 
ATOM   5243 N  NH1 . ARG B 1 282 ? 44.968  74.684  61.758  1.00 56.59 ? 271  ARG B NH1 1 
ATOM   5244 N  NH2 . ARG B 1 282 ? 45.384  72.463  62.142  1.00 56.59 ? 271  ARG B NH2 1 
ATOM   5245 N  N   . GLN B 1 283 ? 52.098  75.981  59.637  1.00 56.24 ? 272  GLN B N   1 
ATOM   5246 C  CA  . GLN B 1 283 ? 52.733  75.044  58.721  1.00 56.24 ? 272  GLN B CA  1 
ATOM   5247 C  C   . GLN B 1 283 ? 54.236  74.967  58.930  1.00 56.24 ? 272  GLN B C   1 
ATOM   5248 O  O   . GLN B 1 283 ? 54.858  73.988  58.507  1.00 56.24 ? 272  GLN B O   1 
ATOM   5249 C  CB  . GLN B 1 283 ? 52.431  75.441  57.277  1.00 56.24 ? 272  GLN B CB  1 
ATOM   5250 C  CG  . GLN B 1 283 ? 52.738  74.356  56.256  1.00 56.24 ? 272  GLN B CG  1 
ATOM   5251 C  CD  . GLN B 1 283 ? 51.711  73.241  56.256  1.00 56.24 ? 272  GLN B CD  1 
ATOM   5252 O  OE1 . GLN B 1 283 ? 52.061  72.063  56.295  1.00 56.24 ? 272  GLN B OE1 1 
ATOM   5253 N  NE2 . GLN B 1 283 ? 50.436  73.608  56.205  1.00 56.24 ? 272  GLN B NE2 1 
ATOM   5254 N  N   . ALA B 1 284 ? 54.834  75.973  59.563  1.00 53.74 ? 273  ALA B N   1 
ATOM   5255 C  CA  . ALA B 1 284 ? 56.264  75.972  59.829  1.00 53.74 ? 273  ALA B CA  1 
ATOM   5256 C  C   . ALA B 1 284 ? 56.620  75.337  61.164  1.00 53.74 ? 273  ALA B C   1 
ATOM   5257 O  O   . ALA B 1 284 ? 57.805  75.116  61.426  1.00 53.74 ? 273  ALA B O   1 
ATOM   5258 C  CB  . ALA B 1 284 ? 56.809  77.401  59.791  1.00 53.74 ? 273  ALA B CB  1 
ATOM   5259 N  N   . PHE B 1 285 ? 55.636  75.040  62.010  1.00 51.33 ? 274  PHE B N   1 
ATOM   5260 C  CA  . PHE B 1 285 ? 55.867  74.336  63.262  1.00 51.33 ? 274  PHE B CA  1 
ATOM   5261 C  C   . PHE B 1 285 ? 55.530  72.855  63.162  1.00 51.33 ? 274  PHE B C   1 
ATOM   5262 O  O   . PHE B 1 285 ? 55.559  72.153  64.176  1.00 51.33 ? 274  PHE B O   1 
ATOM   5263 C  CB  . PHE B 1 285 ? 55.062  74.981  64.392  1.00 51.33 ? 274  PHE B CB  1 
ATOM   5264 C  CG  . PHE B 1 285 ? 55.831  76.005  65.177  1.00 51.33 ? 274  PHE B CG  1 
ATOM   5265 C  CD1 . PHE B 1 285 ? 56.295  77.157  64.572  1.00 51.33 ? 274  PHE B CD1 1 
ATOM   5266 C  CD2 . PHE B 1 285 ? 56.093  75.815  66.519  1.00 51.33 ? 274  PHE B CD2 1 
ATOM   5267 C  CE1 . PHE B 1 285 ? 57.002  78.096  65.292  1.00 51.33 ? 274  PHE B CE1 1 
ATOM   5268 C  CE2 . PHE B 1 285 ? 56.798  76.753  67.240  1.00 51.33 ? 274  PHE B CE2 1 
ATOM   5269 C  CZ  . PHE B 1 285 ? 57.253  77.892  66.626  1.00 51.33 ? 274  PHE B CZ  1 
ATOM   5270 N  N   . GLN B 1 286 ? 55.212  72.364  61.965  1.00 54.16 ? 275  GLN B N   1 
ATOM   5271 C  CA  . GLN B 1 286 ? 55.025  70.933  61.774  1.00 54.16 ? 275  GLN B CA  1 
ATOM   5272 C  C   . GLN B 1 286 ? 56.341  70.171  61.807  1.00 54.16 ? 275  GLN B C   1 
ATOM   5273 O  O   . GLN B 1 286 ? 56.323  68.937  61.779  1.00 54.16 ? 275  GLN B O   1 
ATOM   5274 C  CB  . GLN B 1 286 ? 54.310  70.666  60.449  1.00 54.16 ? 275  GLN B CB  1 
ATOM   5275 C  CG  . GLN B 1 286 ? 52.843  71.040  60.462  1.00 54.16 ? 275  GLN B CG  1 
ATOM   5276 C  CD  . GLN B 1 286 ? 52.149  70.733  59.155  1.00 54.16 ? 275  GLN B CD  1 
ATOM   5277 O  OE1 . GLN B 1 286 ? 52.766  70.244  58.211  1.00 54.16 ? 275  GLN B OE1 1 
ATOM   5278 N  NE2 . GLN B 1 286 ? 50.855  71.020  59.093  1.00 54.16 ? 275  GLN B NE2 1 
ATOM   5279 N  N   . ALA B 1 287 ? 57.471  70.873  61.853  1.00 52.30 ? 276  ALA B N   1 
ATOM   5280 C  CA  . ALA B 1 287 ? 58.790  70.259  61.900  1.00 52.30 ? 276  ALA B CA  1 
ATOM   5281 C  C   . ALA B 1 287 ? 59.561  70.687  63.143  1.00 52.30 ? 276  ALA B C   1 
ATOM   5282 O  O   . ALA B 1 287 ? 60.792  70.681  63.144  1.00 52.30 ? 276  ALA B O   1 
ATOM   5283 C  CB  . ALA B 1 287 ? 59.582  70.603  60.641  1.00 52.30 ? 276  ALA B CB  1 
ATOM   5284 N  N   . ALA B 1 288 ? 58.855  71.069  64.204  1.00 48.70 ? 277  ALA B N   1 
ATOM   5285 C  CA  . ALA B 1 288 ? 59.484  71.575  65.416  1.00 48.70 ? 277  ALA B CA  1 
ATOM   5286 C  C   . ALA B 1 288 ? 58.938  70.850  66.635  1.00 48.70 ? 277  ALA B C   1 
ATOM   5287 O  O   . ALA B 1 288 ? 57.721  70.735  66.802  1.00 48.70 ? 277  ALA B O   1 
ATOM   5288 C  CB  . ALA B 1 288 ? 59.260  73.080  65.566  1.00 48.70 ? 277  ALA B CB  1 
ATOM   5289 N  N   . LYS B 1 289 ? 59.843  70.369  67.479  1.00 46.93 ? 278  LYS B N   1 
ATOM   5290 C  CA  . LYS B 1 289 ? 59.518  69.833  68.791  1.00 46.93 ? 278  LYS B CA  1 
ATOM   5291 C  C   . LYS B 1 289 ? 60.108  70.744  69.857  1.00 46.93 ? 278  LYS B C   1 
ATOM   5292 O  O   . LYS B 1 289 ? 61.053  71.491  69.600  1.00 46.93 ? 278  LYS B O   1 
ATOM   5293 C  CB  . LYS B 1 289 ? 60.053  68.409  68.960  1.00 46.93 ? 278  LYS B CB  1 
ATOM   5294 C  CG  . LYS B 1 289 ? 59.199  67.330  68.319  1.00 46.93 ? 278  LYS B CG  1 
ATOM   5295 C  CD  . LYS B 1 289 ? 59.309  67.337  66.814  1.00 46.93 ? 278  LYS B CD  1 
ATOM   5296 C  CE  . LYS B 1 289 ? 58.524  66.194  66.204  1.00 46.93 ? 278  LYS B CE  1 
ATOM   5297 N  NZ  . LYS B 1 289 ? 58.525  66.259  64.721  1.00 46.93 ? 278  LYS B NZ  1 
ATOM   5298 N  N   . ILE B 1 290 ? 59.540  70.691  71.060  1.00 41.98 ? 279  ILE B N   1 
ATOM   5299 C  CA  . ILE B 1 290 ? 59.958  71.573  72.146  1.00 41.98 ? 279  ILE B CA  1 
ATOM   5300 C  C   . ILE B 1 290 ? 60.382  70.727  73.337  1.00 41.98 ? 279  ILE B C   1 
ATOM   5301 O  O   . ILE B 1 290 ? 59.635  69.848  73.777  1.00 41.98 ? 279  ILE B O   1 
ATOM   5302 C  CB  . ILE B 1 290 ? 58.841  72.561  72.534  1.00 41.98 ? 279  ILE B CB  1 
ATOM   5303 C  CG1 . ILE B 1 290 ? 58.366  73.321  71.293  1.00 41.98 ? 279  ILE B CG1 1 
ATOM   5304 C  CG2 . ILE B 1 290 ? 59.331  73.540  73.592  1.00 41.98 ? 279  ILE B CG2 1 
ATOM   5305 C  CD1 . ILE B 1 290 ? 57.220  74.258  71.540  1.00 41.98 ? 279  ILE B CD1 1 
ATOM   5306 N  N   . ILE B 1 291 ? 61.574  70.997  73.862  1.00 38.86 ? 280  ILE B N   1 
ATOM   5307 C  CA  . ILE B 1 291 ? 62.132  70.271  74.998  1.00 38.86 ? 280  ILE B CA  1 
ATOM   5308 C  C   . ILE B 1 291 ? 62.076  71.191  76.206  1.00 38.86 ? 280  ILE B C   1 
ATOM   5309 O  O   . ILE B 1 291 ? 62.626  72.297  76.170  1.00 38.86 ? 280  ILE B O   1 
ATOM   5310 C  CB  . ILE B 1 291 ? 63.575  69.819  74.727  1.00 38.86 ? 280  ILE B CB  1 
ATOM   5311 C  CG1 . ILE B 1 291 ? 63.619  68.810  73.581  1.00 38.86 ? 280  ILE B CG1 1 
ATOM   5312 C  CG2 . ILE B 1 291 ? 64.181  69.221  75.974  1.00 38.86 ? 280  ILE B CG2 1 
ATOM   5313 C  CD1 . ILE B 1 291 ? 64.957  68.723  72.907  1.00 38.86 ? 280  ILE B CD1 1 
ATOM   5314 N  N   . THR B 1 292 ? 61.425  70.741  77.276  1.00 36.18 ? 281  THR B N   1 
ATOM   5315 C  CA  . THR B 1 292 ? 61.303  71.539  78.488  1.00 36.18 ? 281  THR B CA  1 
ATOM   5316 C  C   . THR B 1 292 ? 61.585  70.671  79.705  1.00 36.18 ? 281  THR B C   1 
ATOM   5317 O  O   . THR B 1 292 ? 61.686  69.446  79.614  1.00 36.18 ? 281  THR B O   1 
ATOM   5318 C  CB  . THR B 1 292 ? 59.909  72.169  78.621  1.00 36.18 ? 281  THR B CB  1 
ATOM   5319 O  OG1 . THR B 1 292 ? 58.961  71.167  79.002  1.00 36.18 ? 281  THR B OG1 1 
ATOM   5320 C  CG2 . THR B 1 292 ? 59.466  72.778  77.314  1.00 36.18 ? 281  THR B CG2 1 
ATOM   5321 N  N   . TYR B 1 293 ? 61.723  71.321  80.857  1.00 31.61 ? 282  TYR B N   1 
ATOM   5322 C  CA  . TYR B 1 293 ? 61.694  70.586  82.107  1.00 31.61 ? 282  TYR B CA  1 
ATOM   5323 C  C   . TYR B 1 293 ? 60.345  69.892  82.242  1.00 31.61 ? 282  TYR B C   1 
ATOM   5324 O  O   . TYR B 1 293 ? 59.395  70.173  81.511  1.00 31.61 ? 282  TYR B O   1 
ATOM   5325 C  CB  . TYR B 1 293 ? 61.921  71.515  83.297  1.00 31.61 ? 282  TYR B CB  1 
ATOM   5326 C  CG  . TYR B 1 293 ? 63.324  72.062  83.434  1.00 31.61 ? 282  TYR B CG  1 
ATOM   5327 C  CD1 . TYR B 1 293 ? 64.422  71.357  82.974  1.00 31.61 ? 282  TYR B CD1 1 
ATOM   5328 C  CD2 . TYR B 1 293 ? 63.546  73.284  84.043  1.00 31.61 ? 282  TYR B CD2 1 
ATOM   5329 C  CE1 . TYR B 1 293 ? 65.695  71.859  83.108  1.00 31.61 ? 282  TYR B CE1 1 
ATOM   5330 C  CE2 . TYR B 1 293 ? 64.815  73.790  84.180  1.00 31.61 ? 282  TYR B CE2 1 
ATOM   5331 C  CZ  . TYR B 1 293 ? 65.885  73.076  83.711  1.00 31.61 ? 282  TYR B CZ  1 
ATOM   5332 O  OH  . TYR B 1 293 ? 67.154  73.584  83.849  1.00 31.61 ? 282  TYR B OH  1 
ATOM   5333 N  N   . LYS B 1 294 ? 60.261  68.974  83.193  1.00 36.57 ? 283  LYS B N   1 
ATOM   5334 C  CA  . LYS B 1 294 ? 59.058  68.185  83.394  1.00 36.57 ? 283  LYS B CA  1 
ATOM   5335 C  C   . LYS B 1 294 ? 58.295  68.712  84.597  1.00 36.57 ? 283  LYS B C   1 
ATOM   5336 O  O   . LYS B 1 294 ? 58.887  68.984  85.645  1.00 36.57 ? 283  LYS B O   1 
ATOM   5337 C  CB  . LYS B 1 294 ? 59.393  66.710  83.593  1.00 36.57 ? 283  LYS B CB  1 
ATOM   5338 C  CG  . LYS B 1 294 ? 58.175  65.860  83.850  1.00 36.57 ? 283  LYS B CG  1 
ATOM   5339 C  CD  . LYS B 1 294 ? 58.393  64.422  83.456  1.00 36.57 ? 283  LYS B CD  1 
ATOM   5340 C  CE  . LYS B 1 294 ? 57.724  63.491  84.442  1.00 36.57 ? 283  LYS B CE  1 
ATOM   5341 N  NZ  . LYS B 1 294 ? 56.281  63.805  84.598  1.00 36.57 ? 283  LYS B NZ  1 
ATOM   5342 N  N   . ASP B 1 295 ? 56.989  68.863  84.437  1.00 41.33 ? 284  ASP B N   1 
ATOM   5343 C  CA  . ASP B 1 295 ? 56.130  69.287  85.532  1.00 41.33 ? 284  ASP B CA  1 
ATOM   5344 C  C   . ASP B 1 295 ? 55.899  68.128  86.493  1.00 41.33 ? 284  ASP B C   1 
ATOM   5345 O  O   . ASP B 1 295 ? 55.412  67.076  86.065  1.00 41.33 ? 284  ASP B O   1 
ATOM   5346 C  CB  . ASP B 1 295 ? 54.796  69.815  85.001  1.00 30.00 ? 284  ASP B CB  1 
ATOM   5347 C  CG  . ASP B 1 295 ? 53.906  70.358  86.102  1.00 30.00 ? 284  ASP B CG  1 
ATOM   5348 O  OD1 . ASP B 1 295 ? 54.332  70.343  87.275  1.00 30.00 ? 284  ASP B OD1 1 
ATOM   5349 O  OD2 . ASP B 1 295 ? 52.765  70.821  85.887  1.00 30.00 ? 284  ASP B OD2 1 
ATOM   5350 N  N   . PRO B 1 296 ? 56.221  68.266  87.777  1.00 36.72 ? 285  PRO B N   1 
ATOM   5351 C  CA  . PRO B 1 296 ? 55.804  67.241  88.740  1.00 36.72 ? 285  PRO B CA  1 
ATOM   5352 C  C   . PRO B 1 296 ? 54.294  67.066  88.708  1.00 36.72 ? 285  PRO B C   1 
ATOM   5353 O  O   . PRO B 1 296 ? 53.536  68.036  88.768  1.00 36.72 ? 285  PRO B O   1 
ATOM   5354 C  CB  . PRO B 1 296 ? 56.291  67.797  90.080  1.00 36.72 ? 285  PRO B CB  1 
ATOM   5355 C  CG  . PRO B 1 296 ? 57.420  68.681  89.722  1.00 36.72 ? 285  PRO B CG  1 
ATOM   5356 C  CD  . PRO B 1 296 ? 57.050  69.301  88.414  1.00 36.72 ? 285  PRO B CD  1 
ATOM   5357 N  N   . ASP B 1 297 ? 53.858  65.815  88.622  1.00 43.42 ? 286  ASP B N   1 
ATOM   5358 C  CA  . ASP B 1 297 ? 52.457  65.478  88.400  1.00 43.42 ? 286  ASP B CA  1 
ATOM   5359 C  C   . ASP B 1 297 ? 51.865  64.733  89.592  1.00 43.42 ? 286  ASP B C   1 
ATOM   5360 O  O   . ASP B 1 297 ? 51.166  63.732  89.433  1.00 43.42 ? 286  ASP B O   1 
ATOM   5361 C  CB  . ASP B 1 297 ? 52.300  64.651  87.128  1.00 43.42 ? 286  ASP B CB  1 
ATOM   5362 N  N   . ASN B 1 298 ? 52.145  65.215  90.800  1.00 39.18 ? 287  ASN B N   1 
ATOM   5363 C  CA  . ASN B 1 298 ? 51.617  64.625  92.014  1.00 39.18 ? 287  ASN B CA  1 
ATOM   5364 C  C   . ASN B 1 298 ? 50.839  65.666  92.811  1.00 39.18 ? 287  ASN B C   1 
ATOM   5365 O  O   . ASN B 1 298 ? 51.102  66.866  92.690  1.00 39.18 ? 287  ASN B O   1 
ATOM   5366 C  CB  . ASN B 1 298 ? 52.744  64.046  92.879  1.00 39.18 ? 287  ASN B CB  1 
ATOM   5367 C  CG  . ASN B 1 298 ? 53.863  65.037  93.125  1.00 39.18 ? 287  ASN B CG  1 
ATOM   5368 O  OD1 . ASN B 1 298 ? 53.621  66.224  93.329  1.00 39.18 ? 287  ASN B OD1 1 
ATOM   5369 N  ND2 . ASN B 1 298 ? 55.097  64.553  93.103  1.00 39.18 ? 287  ASN B ND2 1 
ATOM   5370 N  N   . PRO B 1 299 ? 49.864  65.242  93.621  1.00 39.08 ? 288  PRO B N   1 
ATOM   5371 C  CA  . PRO B 1 299 ? 49.074  66.223  94.386  1.00 39.08 ? 288  PRO B CA  1 
ATOM   5372 C  C   . PRO B 1 299 ? 49.900  67.063  95.343  1.00 39.08 ? 288  PRO B C   1 
ATOM   5373 O  O   . PRO B 1 299 ? 49.556  68.228  95.592  1.00 39.08 ? 288  PRO B O   1 
ATOM   5374 C  CB  . PRO B 1 299 ? 48.067  65.343  95.142  1.00 39.08 ? 288  PRO B CB  1 
ATOM   5375 C  CG  . PRO B 1 299 ? 48.013  64.070  94.375  1.00 39.08 ? 288  PRO B CG  1 
ATOM   5376 C  CD  . PRO B 1 299 ? 49.389  63.867  93.841  1.00 39.08 ? 288  PRO B CD  1 
ATOM   5377 N  N   . GLU B 1 300 ? 50.974  66.501  95.901  1.00 37.15 ? 289  GLU B N   1 
ATOM   5378 C  CA  . GLU B 1 300 ? 51.766  67.232  96.882  1.00 37.15 ? 289  GLU B CA  1 
ATOM   5379 C  C   . GLU B 1 300 ? 52.342  68.506  96.281  1.00 37.15 ? 289  GLU B C   1 
ATOM   5380 O  O   . GLU B 1 300 ? 52.355  69.556  96.931  1.00 37.15 ? 289  GLU B O   1 
ATOM   5381 C  CB  . GLU B 1 300 ? 52.883  66.340  97.420  1.00 37.15 ? 289  GLU B CB  1 
ATOM   5382 N  N   . TYR B 1 301 ? 52.825  68.435  95.041  1.00 34.48 ? 290  TYR B N   1 
ATOM   5383 C  CA  . TYR B 1 301 ? 53.347  69.628  94.385  1.00 34.48 ? 290  TYR B CA  1 
ATOM   5384 C  C   . TYR B 1 301 ? 52.254  70.667  94.184  1.00 34.48 ? 290  TYR B C   1 
ATOM   5385 O  O   . TYR B 1 301 ? 52.489  71.868  94.361  1.00 34.48 ? 290  TYR B O   1 
ATOM   5386 C  CB  . TYR B 1 301 ? 53.980  69.251  93.048  1.00 34.48 ? 290  TYR B CB  1 
ATOM   5387 C  CG  . TYR B 1 301 ? 54.596  70.410  92.309  1.00 34.48 ? 290  TYR B CG  1 
ATOM   5388 C  CD1 . TYR B 1 301 ? 55.727  71.047  92.793  1.00 34.48 ? 290  TYR B CD1 1 
ATOM   5389 C  CD2 . TYR B 1 301 ? 54.054  70.861  91.119  1.00 34.48 ? 290  TYR B CD2 1 
ATOM   5390 C  CE1 . TYR B 1 301 ? 56.295  72.102  92.115  1.00 34.48 ? 290  TYR B CE1 1 
ATOM   5391 C  CE2 . TYR B 1 301 ? 54.614  71.914  90.436  1.00 34.48 ? 290  TYR B CE2 1 
ATOM   5392 C  CZ  . TYR B 1 301 ? 55.733  72.531  90.938  1.00 34.48 ? 290  TYR B CZ  1 
ATOM   5393 O  OH  . TYR B 1 301 ? 56.290  73.582  90.252  1.00 34.48 ? 290  TYR B OH  1 
ATOM   5394 N  N   . LEU B 1 302 ? 51.054  70.230  93.802  1.00 36.28 ? 291  LEU B N   1 
ATOM   5395 C  CA  . LEU B 1 302 ? 49.962  71.176  93.604  1.00 36.28 ? 291  LEU B CA  1 
ATOM   5396 C  C   . LEU B 1 302 ? 49.609  71.889  94.902  1.00 36.28 ? 291  LEU B C   1 
ATOM   5397 O  O   . LEU B 1 302 ? 49.415  73.109  94.913  1.00 36.28 ? 291  LEU B O   1 
ATOM   5398 C  CB  . LEU B 1 302 ? 48.737  70.456  93.040  1.00 36.28 ? 291  LEU B CB  1 
ATOM   5399 C  CG  . LEU B 1 302 ? 48.662  70.307  91.519  1.00 36.28 ? 291  LEU B CG  1 
ATOM   5400 C  CD1 . LEU B 1 302 ? 48.646  71.664  90.836  1.00 36.28 ? 291  LEU B CD1 1 
ATOM   5401 C  CD2 . LEU B 1 302 ? 49.808  69.463  91.000  1.00 36.28 ? 291  LEU B CD2 1 
ATOM   5402 N  N   . GLU B 1 303 ? 49.523  71.150  96.010  1.00 36.19 ? 292  GLU B N   1 
ATOM   5403 C  CA  . GLU B 1 303 ? 49.237  71.791  97.291  1.00 36.19 ? 292  GLU B CA  1 
ATOM   5404 C  C   . GLU B 1 303 ? 50.368  72.725  97.708  1.00 36.19 ? 292  GLU B C   1 
ATOM   5405 O  O   . GLU B 1 303 ? 50.123  73.828  98.225  1.00 36.19 ? 292  GLU B O   1 
ATOM   5406 C  CB  . GLU B 1 303 ? 48.995  70.731  98.364  1.00 36.19 ? 292  GLU B CB  1 
ATOM   5407 N  N   . PHE B 1 304 ? 51.616  72.297  97.499  1.00 33.31 ? 293  PHE B N   1 
ATOM   5408 C  CA  . PHE B 1 304 ? 52.751  73.140  97.845  1.00 33.31 ? 293  PHE B CA  1 
ATOM   5409 C  C   . PHE B 1 304 ? 52.694  74.454  97.088  1.00 33.31 ? 293  PHE B C   1 
ATOM   5410 O  O   . PHE B 1 304 ? 52.919  75.516  97.669  1.00 33.31 ? 293  PHE B O   1 
ATOM   5411 C  CB  . PHE B 1 304 ? 54.059  72.407  97.551  1.00 33.31 ? 293  PHE B CB  1 
ATOM   5412 C  CG  . PHE B 1 304 ? 55.262  73.304  97.511  1.00 33.31 ? 293  PHE B CG  1 
ATOM   5413 C  CD1 . PHE B 1 304 ? 55.850  73.748  98.678  1.00 33.31 ? 293  PHE B CD1 1 
ATOM   5414 C  CD2 . PHE B 1 304 ? 55.811  73.695  96.307  1.00 33.31 ? 293  PHE B CD2 1 
ATOM   5415 C  CE1 . PHE B 1 304 ? 56.954  74.571  98.640  1.00 33.31 ? 293  PHE B CE1 1 
ATOM   5416 C  CE2 . PHE B 1 304 ? 56.912  74.516  96.270  1.00 33.31 ? 293  PHE B CE2 1 
ATOM   5417 C  CZ  . PHE B 1 304 ? 57.484  74.951  97.434  1.00 33.31 ? 293  PHE B CZ  1 
ATOM   5418 N  N   . LEU B 1 305 ? 52.391  74.404  95.791  1.00 35.25 ? 294  LEU B N   1 
ATOM   5419 C  CA  . LEU B 1 305 ? 52.224  75.639  95.032  1.00 35.25 ? 294  LEU B CA  1 
ATOM   5420 C  C   . LEU B 1 305 ? 51.051  76.452  95.557  1.00 35.25 ? 294  LEU B C   1 
ATOM   5421 O  O   . LEU B 1 305 ? 51.144  77.677  95.690  1.00 35.25 ? 294  LEU B O   1 
ATOM   5422 C  CB  . LEU B 1 305 ? 52.018  75.328  93.553  1.00 35.25 ? 294  LEU B CB  1 
ATOM   5423 C  CG  . LEU B 1 305 ? 53.224  74.809  92.782  1.00 35.25 ? 294  LEU B CG  1 
ATOM   5424 C  CD1 . LEU B 1 305 ? 52.824  74.568  91.343  1.00 35.25 ? 294  LEU B CD1 1 
ATOM   5425 C  CD2 . LEU B 1 305 ? 54.386  75.781  92.865  1.00 35.25 ? 294  LEU B CD2 1 
ATOM   5426 N  N   . LYS B 1 306 ? 49.935  75.788  95.855  1.00 37.98 ? 295  LYS B N   1 
ATOM   5427 C  CA  . LYS B 1 306 ? 48.752  76.501  96.316  1.00 37.98 ? 295  LYS B CA  1 
ATOM   5428 C  C   . LYS B 1 306 ? 49.087  77.378  97.513  1.00 37.98 ? 295  LYS B C   1 
ATOM   5429 O  O   . LYS B 1 306 ? 48.699  78.550  97.567  1.00 37.98 ? 295  LYS B O   1 
ATOM   5430 C  CB  . LYS B 1 306 ? 47.646  75.504  96.665  1.00 37.98 ? 295  LYS B CB  1 
ATOM   5431 C  CG  . LYS B 1 306 ? 46.305  76.143  96.990  1.00 37.98 ? 295  LYS B CG  1 
ATOM   5432 C  CD  . LYS B 1 306 ? 46.159  76.427  98.476  1.00 37.98 ? 295  LYS B CD  1 
ATOM   5433 C  CE  . LYS B 1 306 ? 44.792  76.995  98.801  1.00 37.98 ? 295  LYS B CE  1 
ATOM   5434 N  NZ  . LYS B 1 306 ? 44.659  77.309  100.250 1.00 37.98 ? 295  LYS B NZ  1 
ATOM   5435 N  N   . GLN B 1 307 ? 49.818  76.831  98.483  1.00 36.98 ? 296  GLN B N   1 
ATOM   5436 C  CA  . GLN B 1 307 ? 50.159  77.626  99.661  1.00 36.98 ? 296  GLN B CA  1 
ATOM   5437 C  C   . GLN B 1 307 ? 51.401  78.494  99.471  1.00 36.98 ? 296  GLN B C   1 
ATOM   5438 O  O   . GLN B 1 307 ? 51.526  79.525  100.146 1.00 36.98 ? 296  GLN B O   1 
ATOM   5439 C  CB  . GLN B 1 307 ? 50.333  76.727  100.890 1.00 36.98 ? 296  GLN B CB  1 
ATOM   5440 C  CG  . GLN B 1 307 ? 51.340  75.618  100.759 1.00 36.98 ? 296  GLN B CG  1 
ATOM   5441 C  CD  . GLN B 1 307 ? 51.369  74.737  101.990 1.00 36.98 ? 296  GLN B CD  1 
ATOM   5442 O  OE1 . GLN B 1 307 ? 50.709  75.026  102.986 1.00 36.98 ? 296  GLN B OE1 1 
ATOM   5443 N  NE2 . GLN B 1 307 ? 52.128  73.651  101.927 1.00 36.98 ? 296  GLN B NE2 1 
ATOM   5444 N  N   . LEU B 1 308 ? 52.298  78.133  98.553  1.00 33.83 ? 297  LEU B N   1 
ATOM   5445 C  CA  . LEU B 1 308 ? 53.462  78.967  98.280  1.00 33.83 ? 297  LEU B CA  1 
ATOM   5446 C  C   . LEU B 1 308 ? 53.054  80.292  97.653  1.00 33.83 ? 297  LEU B C   1 
ATOM   5447 O  O   . LEU B 1 308 ? 53.610  81.339  97.994  1.00 33.83 ? 297  LEU B O   1 
ATOM   5448 C  CB  . LEU B 1 308 ? 54.434  78.212  97.372  1.00 33.83 ? 297  LEU B CB  1 
ATOM   5449 C  CG  . LEU B 1 308 ? 55.626  78.964  96.775  1.00 33.83 ? 297  LEU B CG  1 
ATOM   5450 C  CD1 . LEU B 1 308 ? 56.730  79.085  97.787  1.00 33.83 ? 297  LEU B CD1 1 
ATOM   5451 C  CD2 . LEU B 1 308 ? 56.133  78.253  95.540  1.00 33.83 ? 297  LEU B CD2 1 
ATOM   5452 N  N   . LYS B 1 309 ? 52.058  80.272  96.769  1.00 37.68 ? 298  LYS B N   1 
ATOM   5453 C  CA  . LYS B 1 309 ? 51.568  81.480  96.073  1.00 37.68 ? 298  LYS B CA  1 
ATOM   5454 C  C   . LYS B 1 309 ? 50.912  82.405  97.077  1.00 37.68 ? 298  LYS B C   1 
ATOM   5455 O  O   . LYS B 1 309 ? 50.928  83.568  96.795  1.00 37.68 ? 298  LYS B O   1 
ATOM   5456 C  CB  . LYS B 1 309 ? 50.498  81.270  95.002  1.00 37.68 ? 298  LYS B CB  1 
ATOM   5457 C  CG  . LYS B 1 309 ? 50.721  80.264  93.882  1.00 37.68 ? 298  LYS B CG  1 
ATOM   5458 C  CD  . LYS B 1 309 ? 51.902  80.467  92.995  1.00 37.68 ? 298  LYS B CD  1 
ATOM   5459 C  CE  . LYS B 1 309 ? 52.049  79.351  91.988  1.00 37.68 ? 298  LYS B CE  1 
ATOM   5460 N  NZ  . LYS B 1 309 ? 50.782  79.082  91.265  1.00 37.68 ? 298  LYS B NZ  1 
ATOM   5461 N  N   . HIS B 1 310 ? 50.228  81.883  98.095  1.00 39.49 ? 299  HIS B N   1 
ATOM   5462 C  CA  . HIS B 1 310 ? 49.626  82.674  99.160  1.00 39.49 ? 299  HIS B CA  1 
ATOM   5463 C  C   . HIS B 1 310 ? 50.693  83.284  100.059 1.00 39.49 ? 299  HIS B C   1 
ATOM   5464 O  O   . HIS B 1 310 ? 50.660  84.484  100.358 1.00 39.49 ? 299  HIS B O   1 
ATOM   5465 C  CB  . HIS B 1 310 ? 48.674  81.793  99.969  1.00 39.49 ? 299  HIS B CB  1 
ATOM   5466 C  CG  . HIS B 1 310 ? 48.124  82.455  101.191 1.00 39.49 ? 299  HIS B CG  1 
ATOM   5467 N  ND1 . HIS B 1 310 ? 46.951  83.178  101.181 1.00 39.49 ? 299  HIS B ND1 1 
ATOM   5468 C  CD2 . HIS B 1 310 ? 48.581  82.498  102.465 1.00 39.49 ? 299  HIS B CD2 1 
ATOM   5469 C  CE1 . HIS B 1 310 ? 46.711  83.641  102.395 1.00 39.49 ? 299  HIS B CE1 1 
ATOM   5470 N  NE2 . HIS B 1 310 ? 47.685  83.243  103.192 1.00 39.49 ? 299  HIS B NE2 1 
ATOM   5471 N  N   . LEU B 1 311 ? 51.655  82.470  100.499 1.00 35.78 ? 300  LEU B N   1 
ATOM   5472 C  CA  . LEU B 1 311 ? 52.696  82.988  101.380 1.00 35.78 ? 300  LEU B CA  1 
ATOM   5473 C  C   . LEU B 1 311 ? 53.533  84.050  100.682 1.00 35.78 ? 300  LEU B C   1 
ATOM   5474 O  O   . LEU B 1 311 ? 53.891  85.065  101.290 1.00 35.78 ? 300  LEU B O   1 
ATOM   5475 C  CB  . LEU B 1 311 ? 53.582  81.847  101.872 1.00 35.78 ? 300  LEU B CB  1 
ATOM   5476 C  CG  . LEU B 1 311 ? 54.373  82.123  103.147 1.00 35.78 ? 300  LEU B CG  1 
ATOM   5477 C  CD1 . LEU B 1 311 ? 53.449  82.445  104.304 1.00 35.78 ? 300  LEU B CD1 1 
ATOM   5478 C  CD2 . LEU B 1 311 ? 55.241  80.934  103.479 1.00 35.78 ? 300  LEU B CD2 1 
ATOM   5479 N  N   . ALA B 1 312 ? 53.862  83.837  99.408  1.00 35.36 ? 301  ALA B N   1 
ATOM   5480 C  CA  . ALA B 1 312 ? 54.639  84.828  98.677  1.00 35.36 ? 301  ALA B CA  1 
ATOM   5481 C  C   . ALA B 1 312 ? 53.894  86.149  98.592  1.00 35.36 ? 301  ALA B C   1 
ATOM   5482 O  O   . ALA B 1 312 ? 54.496  87.217  98.740  1.00 35.36 ? 301  ALA B O   1 
ATOM   5483 C  CB  . ALA B 1 312 ? 54.971  84.312  97.280  1.00 35.36 ? 301  ALA B CB  1 
ATOM   5484 N  N   . TYR B 1 313 ? 52.583  86.102  98.347  1.00 39.85 ? 302  TYR B N   1 
ATOM   5485 C  CA  . TYR B 1 313 ? 51.812  87.341  98.307  1.00 39.85 ? 302  TYR B CA  1 
ATOM   5486 C  C   . TYR B 1 313 ? 51.789  88.023  99.669  1.00 39.85 ? 302  TYR B C   1 
ATOM   5487 O  O   . TYR B 1 313 ? 52.003  89.236  99.769  1.00 39.85 ? 302  TYR B O   1 
ATOM   5488 C  CB  . TYR B 1 313 ? 50.387  87.072  97.830  1.00 39.85 ? 302  TYR B CB  1 
ATOM   5489 C  CG  . TYR B 1 313 ? 49.575  88.338  97.694  1.00 39.85 ? 302  TYR B CG  1 
ATOM   5490 C  CD1 . TYR B 1 313 ? 49.804  89.222  96.650  1.00 39.85 ? 302  TYR B CD1 1 
ATOM   5491 C  CD2 . TYR B 1 313 ? 48.592  88.659  98.620  1.00 39.85 ? 302  TYR B CD2 1 
ATOM   5492 C  CE1 . TYR B 1 313 ? 49.073  90.384  96.526  1.00 39.85 ? 302  TYR B CE1 1 
ATOM   5493 C  CE2 . TYR B 1 313 ? 47.854  89.819  98.505  1.00 39.85 ? 302  TYR B CE2 1 
ATOM   5494 C  CZ  . TYR B 1 313 ? 48.098  90.678  97.456  1.00 39.85 ? 302  TYR B CZ  1 
ATOM   5495 O  OH  . TYR B 1 313 ? 47.366  91.835  97.334  1.00 39.85 ? 302  TYR B OH  1 
ATOM   5496 N  N   . GLU B 1 314 ? 51.520  87.264  100.732 1.00 39.25 ? 303  GLU B N   1 
ATOM   5497 C  CA  . GLU B 1 314 ? 51.396  87.874  102.053 1.00 39.25 ? 303  GLU B CA  1 
ATOM   5498 C  C   . GLU B 1 314 ? 52.731  88.422  102.545 1.00 39.25 ? 303  GLU B C   1 
ATOM   5499 O  O   . GLU B 1 314 ? 52.824  89.586  102.950 1.00 39.25 ? 303  GLU B O   1 
ATOM   5500 C  CB  . GLU B 1 314 ? 50.837  86.856  103.047 1.00 39.25 ? 303  GLU B CB  1 
ATOM   5501 N  N   . GLN B 1 315 ? 53.783  87.602  102.506 1.00 38.72 ? 304  GLN B N   1 
ATOM   5502 C  CA  . GLN B 1 315 ? 55.038  87.957  103.161 1.00 38.72 ? 304  GLN B CA  1 
ATOM   5503 C  C   . GLN B 1 315 ? 55.846  88.976  102.368 1.00 38.72 ? 304  GLN B C   1 
ATOM   5504 O  O   . GLN B 1 315 ? 56.487  89.850  102.959 1.00 38.72 ? 304  GLN B O   1 
ATOM   5505 C  CB  . GLN B 1 315 ? 55.881  86.702  103.389 1.00 38.72 ? 304  GLN B CB  1 
ATOM   5506 C  CG  . GLN B 1 315 ? 55.335  85.744  104.435 1.00 38.72 ? 304  GLN B CG  1 
ATOM   5507 C  CD  . GLN B 1 315 ? 55.094  86.403  105.777 1.00 38.72 ? 304  GLN B CD  1 
ATOM   5508 O  OE1 . GLN B 1 315 ? 54.130  87.147  105.954 1.00 38.72 ? 304  GLN B OE1 1 
ATOM   5509 N  NE2 . GLN B 1 315 ? 55.974  86.133  106.733 1.00 38.72 ? 304  GLN B NE2 1 
ATOM   5510 N  N   . PHE B 1 316 ? 55.843  88.879  101.040 1.00 34.09 ? 305  PHE B N   1 
ATOM   5511 C  CA  . PHE B 1 316 ? 56.767  89.642  100.214 1.00 34.09 ? 305  PHE B CA  1 
ATOM   5512 C  C   . PHE B 1 316 ? 56.087  90.588  99.237  1.00 34.09 ? 305  PHE B C   1 
ATOM   5513 O  O   . PHE B 1 316 ? 56.784  91.245  98.455  1.00 34.09 ? 305  PHE B O   1 
ATOM   5514 C  CB  . PHE B 1 316 ? 57.680  88.684  99.437  1.00 34.09 ? 305  PHE B CB  1 
ATOM   5515 C  CG  . PHE B 1 316 ? 58.653  87.942  100.306 1.00 34.09 ? 305  PHE B CG  1 
ATOM   5516 C  CD1 . PHE B 1 316 ? 58.275  86.783  100.959 1.00 34.09 ? 305  PHE B CD1 1 
ATOM   5517 C  CD2 . PHE B 1 316 ? 59.943  88.407  100.475 1.00 34.09 ? 305  PHE B CD2 1 
ATOM   5518 C  CE1 . PHE B 1 316 ? 59.164  86.104  101.762 1.00 34.09 ? 305  PHE B CE1 1 
ATOM   5519 C  CE2 . PHE B 1 316 ? 60.834  87.730  101.275 1.00 34.09 ? 305  PHE B CE2 1 
ATOM   5520 C  CZ  . PHE B 1 316 ? 60.444  86.577  101.919 1.00 34.09 ? 305  PHE B CZ  1 
ATOM   5521 N  N   . ASN B 1 317 ? 54.762  90.689  99.256  1.00 39.12 ? 306  ASN B N   1 
ATOM   5522 C  CA  . ASN B 1 317 ? 54.034  91.547  98.325  1.00 39.12 ? 306  ASN B CA  1 
ATOM   5523 C  C   . ASN B 1 317 ? 54.422  91.227  96.883  1.00 39.12 ? 306  ASN B C   1 
ATOM   5524 O  O   . ASN B 1 317 ? 54.678  92.113  96.067  1.00 39.12 ? 306  ASN B O   1 
ATOM   5525 C  CB  . ASN B 1 317 ? 54.277  93.022  98.643  1.00 39.12 ? 306  ASN B CB  1 
ATOM   5526 N  N   . PHE B 1 318 ? 54.468  89.933  96.577  1.00 34.77 ? 307  PHE B N   1 
ATOM   5527 C  CA  . PHE B 1 318 ? 54.827  89.439  95.255  1.00 34.77 ? 307  PHE B CA  1 
ATOM   5528 C  C   . PHE B 1 318 ? 53.774  88.441  94.806  1.00 34.77 ? 307  PHE B C   1 
ATOM   5529 O  O   . PHE B 1 318 ? 53.382  87.563  95.580  1.00 34.77 ? 307  PHE B O   1 
ATOM   5530 C  CB  . PHE B 1 318 ? 56.210  88.781  95.270  1.00 34.77 ? 307  PHE B CB  1 
ATOM   5531 C  CG  . PHE B 1 318 ? 56.648  88.258  93.936  1.00 34.77 ? 307  PHE B CG  1 
ATOM   5532 C  CD1 . PHE B 1 318 ? 56.973  89.123  92.913  1.00 34.77 ? 307  PHE B CD1 1 
ATOM   5533 C  CD2 . PHE B 1 318 ? 56.742  86.900  93.707  1.00 34.77 ? 307  PHE B CD2 1 
ATOM   5534 C  CE1 . PHE B 1 318 ? 57.378  88.642  91.692  1.00 34.77 ? 307  PHE B CE1 1 
ATOM   5535 C  CE2 . PHE B 1 318 ? 57.146  86.420  92.487  1.00 34.77 ? 307  PHE B CE2 1 
ATOM   5536 C  CZ  . PHE B 1 318 ? 57.461  87.290  91.480  1.00 34.77 ? 307  PHE B CZ  1 
ATOM   5537 N  N   . THR B 1 319 ? 53.314  88.577  93.566  1.00 37.92 ? 308  THR B N   1 
ATOM   5538 C  CA  . THR B 1 319 ? 52.323  87.674  92.992  1.00 37.92 ? 308  THR B CA  1 
ATOM   5539 C  C   . THR B 1 319 ? 53.040  86.707  92.059  1.00 37.92 ? 308  THR B C   1 
ATOM   5540 O  O   . THR B 1 319 ? 53.570  87.114  91.020  1.00 37.92 ? 308  THR B O   1 
ATOM   5541 C  CB  . THR B 1 319 ? 51.238  88.450  92.248  1.00 37.92 ? 308  THR B CB  1 
ATOM   5542 O  OG1 . THR B 1 319 ? 50.560  89.324  93.158  1.00 37.92 ? 308  THR B OG1 1 
ATOM   5543 C  CG2 . THR B 1 319 ? 50.228  87.498  91.632  1.00 37.92 ? 308  THR B CG2 1 
ATOM   5544 N  N   . MET B 1 320 ? 53.050  85.430  92.426  1.00 36.93 ? 309  MET B N   1 
ATOM   5545 C  CA  . MET B 1 320 ? 53.720  84.403  91.643  1.00 36.93 ? 309  MET B CA  1 
ATOM   5546 C  C   . MET B 1 320 ? 52.780  83.867  90.574  1.00 36.93 ? 309  MET B C   1 
ATOM   5547 O  O   . MET B 1 320 ? 51.672  83.419  90.882  1.00 36.93 ? 309  MET B O   1 
ATOM   5548 C  CB  . MET B 1 320 ? 54.191  83.262  92.540  1.00 36.93 ? 309  MET B CB  1 
ATOM   5549 C  CG  . MET B 1 320 ? 55.286  83.638  93.514  1.00 36.93 ? 309  MET B CG  1 
ATOM   5550 S  SD  . MET B 1 320 ? 55.718  82.260  94.581  1.00 36.93 ? 309  MET B SD  1 
ATOM   5551 C  CE  . MET B 1 320 ? 56.535  81.191  93.405  1.00 36.93 ? 309  MET B CE  1 
ATOM   5552 N  N   . GLU B 1 321 ? 53.230  83.907  89.325  1.00 39.43 ? 310  GLU B N   1 
ATOM   5553 C  CA  . GLU B 1 321 ? 52.441  83.423  88.204  1.00 39.43 ? 310  GLU B CA  1 
ATOM   5554 C  C   . GLU B 1 321 ? 52.709  81.944  87.975  1.00 39.43 ? 310  GLU B C   1 
ATOM   5555 O  O   . GLU B 1 321 ? 53.834  81.469  88.147  1.00 39.43 ? 310  GLU B O   1 
ATOM   5556 C  CB  . GLU B 1 321 ? 52.768  84.215  86.937  1.00 39.43 ? 310  GLU B CB  1 
ATOM   5557 N  N   . ASP B 1 322 ? 51.666  81.218  87.583  1.00 39.98 ? 311  ASP B N   1 
ATOM   5558 C  CA  . ASP B 1 322 ? 51.814  79.797  87.304  1.00 39.98 ? 311  ASP B CA  1 
ATOM   5559 C  C   . ASP B 1 322 ? 52.828  79.585  86.190  1.00 39.98 ? 311  ASP B C   1 
ATOM   5560 O  O   . ASP B 1 322 ? 52.903  80.364  85.237  1.00 39.98 ? 311  ASP B O   1 
ATOM   5561 C  CB  . ASP B 1 322 ? 50.467  79.192  86.911  1.00 39.98 ? 311  ASP B CB  1 
ATOM   5562 N  N   . GLY B 1 323 ? 53.619  78.527  86.316  1.00 37.79 ? 312  GLY B N   1 
ATOM   5563 C  CA  . GLY B 1 323 ? 54.615  78.235  85.309  1.00 37.79 ? 312  GLY B CA  1 
ATOM   5564 C  C   . GLY B 1 323 ? 55.498  77.082  85.739  1.00 37.79 ? 312  GLY B C   1 
ATOM   5565 O  O   . GLY B 1 323 ? 55.232  76.403  86.731  1.00 37.79 ? 312  GLY B O   1 
ATOM   5566 N  N   . LEU B 1 324 ? 56.554  76.879  84.960  1.00 34.19 ? 313  LEU B N   1 
ATOM   5567 C  CA  . LEU B 1 324 ? 57.535  75.835  85.209  1.00 34.19 ? 313  LEU B CA  1 
ATOM   5568 C  C   . LEU B 1 324 ? 58.747  76.352  85.969  1.00 34.19 ? 313  LEU B C   1 
ATOM   5569 O  O   . LEU B 1 324 ? 59.689  75.592  86.198  1.00 34.19 ? 313  LEU B O   1 
ATOM   5570 C  CB  . LEU B 1 324 ? 57.974  75.221  83.875  1.00 34.19 ? 313  LEU B CB  1 
ATOM   5571 C  CG  . LEU B 1 324 ? 58.356  73.746  83.795  1.00 34.19 ? 313  LEU B CG  1 
ATOM   5572 C  CD1 . LEU B 1 324 ? 57.270  72.856  84.358  1.00 34.19 ? 313  LEU B CD1 1 
ATOM   5573 C  CD2 . LEU B 1 324 ? 58.600  73.399  82.349  1.00 34.19 ? 313  LEU B CD2 1 
ATOM   5574 N  N   . VAL B 1 325 ? 58.746  77.632  86.355  1.00 30.77 ? 314  VAL B N   1 
ATOM   5575 C  CA  . VAL B 1 325 ? 59.835  78.196  87.148  1.00 30.77 ? 314  VAL B CA  1 
ATOM   5576 C  C   . VAL B 1 325 ? 59.652  77.971  88.639  1.00 30.77 ? 314  VAL B C   1 
ATOM   5577 O  O   . VAL B 1 325 ? 60.564  78.288  89.417  1.00 30.77 ? 314  VAL B O   1 
ATOM   5578 C  CB  . VAL B 1 325 ? 59.996  79.711  86.906  1.00 30.77 ? 314  VAL B CB  1 
ATOM   5579 C  CG1 . VAL B 1 325 ? 60.597  79.975  85.546  1.00 30.77 ? 314  VAL B CG1 1 
ATOM   5580 C  CG2 . VAL B 1 325 ? 58.663  80.422  87.035  1.00 30.77 ? 314  VAL B CG2 1 
ATOM   5581 N  N   . ASN B 1 326 ? 58.505  77.447  89.069  1.00 32.65 ? 315  ASN B N   1 
ATOM   5582 C  CA  . ASN B 1 326 ? 58.299  77.139  90.477  1.00 32.65 ? 315  ASN B CA  1 
ATOM   5583 C  C   . ASN B 1 326 ? 59.012  75.866  90.904  1.00 32.65 ? 315  ASN B C   1 
ATOM   5584 O  O   . ASN B 1 326 ? 59.148  75.615  92.110  1.00 32.65 ? 315  ASN B O   1 
ATOM   5585 C  CB  . ASN B 1 326 ? 56.806  77.019  90.768  1.00 32.65 ? 315  ASN B CB  1 
ATOM   5586 C  CG  . ASN B 1 326 ? 56.011  78.180  90.213  1.00 32.65 ? 315  ASN B CG  1 
ATOM   5587 O  OD1 . ASN B 1 326 ? 56.299  79.338  90.497  1.00 32.65 ? 315  ASN B OD1 1 
ATOM   5588 N  ND2 . ASN B 1 326 ? 54.995  77.873  89.424  1.00 32.65 ? 315  ASN B ND2 1 
ATOM   5589 N  N   . THR B 1 327 ? 59.485  75.067  89.947  1.00 29.80 ? 316  THR B N   1 
ATOM   5590 C  CA  . THR B 1 327 ? 60.284  73.906  90.295  1.00 29.80 ? 316  THR B CA  1 
ATOM   5591 C  C   . THR B 1 327 ? 61.576  74.300  90.986  1.00 29.80 ? 316  THR B C   1 
ATOM   5592 O  O   . THR B 1 327 ? 62.140  73.484  91.710  1.00 29.80 ? 316  THR B O   1 
ATOM   5593 C  CB  . THR B 1 327 ? 60.602  73.071  89.055  1.00 29.80 ? 316  THR B CB  1 
ATOM   5594 O  OG1 . THR B 1 327 ? 61.481  73.800  88.194  1.00 29.80 ? 316  THR B OG1 1 
ATOM   5595 C  CG2 . THR B 1 327 ? 59.333  72.713  88.303  1.00 29.80 ? 316  THR B CG2 1 
ATOM   5596 N  N   . ILE B 1 328 ? 62.036  75.536  90.829  1.00 26.35 ? 317  ILE B N   1 
ATOM   5597 C  CA  . ILE B 1 328 ? 63.284  75.963  91.458  1.00 26.35 ? 317  ILE B CA  1 
ATOM   5598 C  C   . ILE B 1 328 ? 63.045  76.255  92.939  1.00 26.35 ? 317  ILE B C   1 
ATOM   5599 O  O   . ILE B 1 328 ? 63.822  75.785  93.784  1.00 26.35 ? 317  ILE B O   1 
ATOM   5600 C  CB  . ILE B 1 328 ? 63.891  77.169  90.725  1.00 26.35 ? 317  ILE B CB  1 
ATOM   5601 C  CG1 . ILE B 1 328 ? 64.046  76.865  89.233  1.00 26.35 ? 317  ILE B CG1 1 
ATOM   5602 C  CG2 . ILE B 1 328 ? 65.223  77.542  91.332  1.00 26.35 ? 317  ILE B CG2 1 
ATOM   5603 C  CD1 . ILE B 1 328 ? 65.002  75.750  88.918  1.00 26.35 ? 317  ILE B CD1 1 
ATOM   5604 N  N   . PRO B 1 329 ? 62.017  77.023  93.317  1.00 27.76 ? 318  PRO B N   1 
ATOM   5605 C  CA  . PRO B 1 329 ? 61.660  77.069  94.743  1.00 27.76 ? 318  PRO B CA  1 
ATOM   5606 C  C   . PRO B 1 329 ? 61.357  75.703  95.327  1.00 27.76 ? 318  PRO B C   1 
ATOM   5607 O  O   . PRO B 1 329 ? 61.747  75.416  96.468  1.00 27.76 ? 318  PRO B O   1 
ATOM   5608 C  CB  . PRO B 1 329 ? 60.427  77.975  94.752  1.00 27.76 ? 318  PRO B CB  1 
ATOM   5609 C  CG  . PRO B 1 329 ? 60.637  78.875  93.628  1.00 27.76 ? 318  PRO B CG  1 
ATOM   5610 C  CD  . PRO B 1 329 ? 61.290  78.054  92.558  1.00 27.76 ? 318  PRO B CD  1 
ATOM   5611 N  N   . ALA B 1 330 ? 60.670  74.841  94.574  1.00 29.46 ? 319  ALA B N   1 
ATOM   5612 C  CA  . ALA B 1 330 ? 60.394  73.501  95.079  1.00 29.46 ? 319  ALA B CA  1 
ATOM   5613 C  C   . ALA B 1 330 ? 61.684  72.725  95.305  1.00 29.46 ? 319  ALA B C   1 
ATOM   5614 O  O   . ALA B 1 330 ? 61.807  71.978  96.282  1.00 29.46 ? 319  ALA B O   1 
ATOM   5615 C  CB  . ALA B 1 330 ? 59.482  72.756  94.112  1.00 29.46 ? 319  ALA B CB  1 
ATOM   5616 N  N   . SER B 1 331 ? 62.656  72.885  94.408  1.00 27.33 ? 320  SER B N   1 
ATOM   5617 C  CA  . SER B 1 331 ? 63.941  72.216  94.554  1.00 27.33 ? 320  SER B CA  1 
ATOM   5618 C  C   . SER B 1 331 ? 64.704  72.740  95.760  1.00 27.33 ? 320  SER B C   1 
ATOM   5619 O  O   . SER B 1 331 ? 65.368  71.970  96.453  1.00 27.33 ? 320  SER B O   1 
ATOM   5620 C  CB  . SER B 1 331 ? 64.763  72.397  93.283  1.00 27.33 ? 320  SER B CB  1 
ATOM   5621 O  OG  . SER B 1 331 ? 64.223  71.626  92.225  1.00 27.33 ? 320  SER B OG  1 
ATOM   5622 N  N   . PHE B 1 332 ? 64.639  74.047  96.019  1.00 23.91 ? 321  PHE B N   1 
ATOM   5623 C  CA  . PHE B 1 332 ? 65.261  74.575  97.232  1.00 23.91 ? 321  PHE B CA  1 
ATOM   5624 C  C   . PHE B 1 332 ? 64.626  73.968  98.476  1.00 23.91 ? 321  PHE B C   1 
ATOM   5625 O  O   . PHE B 1 332 ? 65.326  73.574  99.416  1.00 23.91 ? 321  PHE B O   1 
ATOM   5626 C  CB  . PHE B 1 332 ? 65.148  76.097  97.272  1.00 23.91 ? 321  PHE B CB  1 
ATOM   5627 C  CG  . PHE B 1 332 ? 66.335  76.811  96.697  1.00 23.91 ? 321  PHE B CG  1 
ATOM   5628 C  CD1 . PHE B 1 332 ? 67.488  76.969  97.436  1.00 23.91 ? 321  PHE B CD1 1 
ATOM   5629 C  CD2 . PHE B 1 332 ? 66.292  77.336  95.423  1.00 23.91 ? 321  PHE B CD2 1 
ATOM   5630 C  CE1 . PHE B 1 332 ? 68.573  77.630  96.912  1.00 23.91 ? 321  PHE B CE1 1 
ATOM   5631 C  CE2 . PHE B 1 332 ? 67.379  77.997  94.898  1.00 23.91 ? 321  PHE B CE2 1 
ATOM   5632 C  CZ  . PHE B 1 332 ? 68.519  78.142  95.645  1.00 23.91 ? 321  PHE B CZ  1 
ATOM   5633 N  N   . HIS B 1 333 ? 63.296  73.878  98.491  1.00 28.84 ? 322  HIS B N   1 
ATOM   5634 C  CA  . HIS B 1 333 ? 62.593  73.262  99.613  1.00 28.84 ? 322  HIS B CA  1 
ATOM   5635 C  C   . HIS B 1 333 ? 63.048  71.818  99.817  1.00 28.84 ? 322  HIS B C   1 
ATOM   5636 O  O   . HIS B 1 333 ? 63.427  71.415  100.929 1.00 28.84 ? 322  HIS B O   1 
ATOM   5637 C  CB  . HIS B 1 333 ? 61.089  73.350  99.338  1.00 28.84 ? 322  HIS B CB  1 
ATOM   5638 C  CG  . HIS B 1 333 ? 60.231  72.533  100.252 1.00 28.84 ? 322  HIS B CG  1 
ATOM   5639 N  ND1 . HIS B 1 333 ? 59.696  73.037  101.417 1.00 28.84 ? 322  HIS B ND1 1 
ATOM   5640 C  CD2 . HIS B 1 333 ? 59.778  71.263  100.151 1.00 28.84 ? 322  HIS B CD2 1 
ATOM   5641 C  CE1 . HIS B 1 333 ? 58.969  72.105  102.005 1.00 28.84 ? 322  HIS B CE1 1 
ATOM   5642 N  NE2 . HIS B 1 333 ? 59.004  71.018  101.258 1.00 28.84 ? 322  HIS B NE2 1 
ATOM   5643 N  N   . ASP B 1 334 ? 63.052  71.034  98.737  1.00 32.34 ? 323  ASP B N   1 
ATOM   5644 C  CA  . ASP B 1 334 ? 63.436  69.629  98.826  1.00 32.34 ? 323  ASP B CA  1 
ATOM   5645 C  C   . ASP B 1 334 ? 64.889  69.469  99.252  1.00 32.34 ? 323  ASP B C   1 
ATOM   5646 O  O   . ASP B 1 334 ? 65.212  68.600  100.067 1.00 32.34 ? 323  ASP B O   1 
ATOM   5647 C  CB  . ASP B 1 334 ? 63.202  68.942  97.483  1.00 32.34 ? 323  ASP B CB  1 
ATOM   5648 C  CG  . ASP B 1 334 ? 61.743  68.636  97.231  1.00 32.34 ? 323  ASP B CG  1 
ATOM   5649 O  OD1 . ASP B 1 334 ? 60.943  68.709  98.186  1.00 32.34 ? 323  ASP B OD1 1 
ATOM   5650 O  OD2 . ASP B 1 334 ? 61.395  68.321  96.075  1.00 32.34 ? 323  ASP B OD2 1 
ATOM   5651 N  N   . GLY B 1 335 ? 65.785  70.288  98.700  1.00 27.21 ? 324  GLY B N   1 
ATOM   5652 C  CA  . GLY B 1 335 ? 67.190  70.173  99.044  1.00 27.21 ? 324  GLY B CA  1 
ATOM   5653 C  C   . GLY B 1 335 ? 67.466  70.534  100.487 1.00 27.21 ? 324  GLY B C   1 
ATOM   5654 O  O   . GLY B 1 335 ? 68.290  69.897  101.147 1.00 27.21 ? 324  GLY B O   1 
ATOM   5655 N  N   . LEU B 1 336 ? 66.790  71.562  101.000 1.00 28.10 ? 325  LEU B N   1 
ATOM   5656 C  CA  . LEU B 1 336 ? 66.964  71.900  102.405 1.00 28.10 ? 325  LEU B CA  1 
ATOM   5657 C  C   . LEU B 1 336 ? 66.459  70.778  103.301 1.00 28.10 ? 325  LEU B C   1 
ATOM   5658 O  O   . LEU B 1 336 ? 67.096  70.445  104.306 1.00 28.10 ? 325  LEU B O   1 
ATOM   5659 C  CB  . LEU B 1 336 ? 66.251  73.211  102.725 1.00 28.10 ? 325  LEU B CB  1 
ATOM   5660 C  CG  . LEU B 1 336 ? 66.578  73.790  104.100 1.00 28.10 ? 325  LEU B CG  1 
ATOM   5661 C  CD1 . LEU B 1 336 ? 67.911  74.502  104.067 1.00 28.10 ? 325  LEU B CD1 1 
ATOM   5662 C  CD2 . LEU B 1 336 ? 65.483  74.729  104.554 1.00 28.10 ? 325  LEU B CD2 1 
ATOM   5663 N  N   . LEU B 1 337 ? 65.320  70.173  102.957 1.00 31.93 ? 326  LEU B N   1 
ATOM   5664 C  CA  . LEU B 1 337 ? 64.841  69.054  103.765 1.00 31.93 ? 326  LEU B CA  1 
ATOM   5665 C  C   . LEU B 1 337 ? 65.809  67.875  103.710 1.00 31.93 ? 326  LEU B C   1 
ATOM   5666 O  O   . LEU B 1 337 ? 66.046  67.204  104.723 1.00 31.93 ? 326  LEU B O   1 
ATOM   5667 C  CB  . LEU B 1 337 ? 63.449  68.631  103.306 1.00 31.93 ? 326  LEU B CB  1 
ATOM   5668 C  CG  . LEU B 1 337 ? 62.306  69.505  103.821 1.00 31.93 ? 326  LEU B CG  1 
ATOM   5669 C  CD1 . LEU B 1 337 ? 61.021  69.173  103.094 1.00 31.93 ? 326  LEU B CD1 1 
ATOM   5670 C  CD2 . LEU B 1 337 ? 62.128  69.339  105.317 1.00 31.93 ? 326  LEU B CD2 1 
ATOM   5671 N  N   . LEU B 1 338 ? 66.377  67.603  102.535 1.00 30.92 ? 327  LEU B N   1 
ATOM   5672 C  CA  . LEU B 1 338 ? 67.354  66.525  102.413 1.00 30.92 ? 327  LEU B CA  1 
ATOM   5673 C  C   . LEU B 1 338 ? 68.585  66.798  103.268 1.00 30.92 ? 327  LEU B C   1 
ATOM   5674 O  O   . LEU B 1 338 ? 69.103  65.893  103.933 1.00 30.92 ? 327  LEU B O   1 
ATOM   5675 C  CB  . LEU B 1 338 ? 67.745  66.348  100.946 1.00 30.92 ? 327  LEU B CB  1 
ATOM   5676 C  CG  . LEU B 1 338 ? 68.973  65.499  100.617 1.00 30.92 ? 327  LEU B CG  1 
ATOM   5677 C  CD1 . LEU B 1 338 ? 68.634  64.025  100.677 1.00 30.92 ? 327  LEU B CD1 1 
ATOM   5678 C  CD2 . LEU B 1 338 ? 69.502  65.868  99.251  1.00 30.92 ? 327  LEU B CD2 1 
ATOM   5679 N  N   . TYR B 1 339 ? 69.076  68.037  103.254 1.00 29.21 ? 328  TYR B N   1 
ATOM   5680 C  CA  . TYR B 1 339 ? 70.221  68.380  104.088 1.00 29.21 ? 328  TYR B CA  1 
ATOM   5681 C  C   . TYR B 1 339 ? 69.894  68.226  105.565 1.00 29.21 ? 328  TYR B C   1 
ATOM   5682 O  O   . TYR B 1 339 ? 70.728  67.758  106.347 1.00 29.21 ? 328  TYR B O   1 
ATOM   5683 C  CB  . TYR B 1 339 ? 70.680  69.804  103.801 1.00 29.21 ? 328  TYR B CB  1 
ATOM   5684 C  CG  . TYR B 1 339 ? 71.627  70.337  104.848 1.00 29.21 ? 328  TYR B CG  1 
ATOM   5685 C  CD1 . TYR B 1 339 ? 72.959  69.971  104.850 1.00 29.21 ? 328  TYR B CD1 1 
ATOM   5686 C  CD2 . TYR B 1 339 ? 71.186  71.196  105.839 1.00 29.21 ? 328  TYR B CD2 1 
ATOM   5687 C  CE1 . TYR B 1 339 ? 73.825  70.441  105.804 1.00 29.21 ? 328  TYR B CE1 1 
ATOM   5688 C  CE2 . TYR B 1 339 ? 72.049  71.673  106.799 1.00 29.21 ? 328  TYR B CE2 1 
ATOM   5689 C  CZ  . TYR B 1 339 ? 73.368  71.293  106.774 1.00 29.21 ? 328  TYR B CZ  1 
ATOM   5690 O  OH  . TYR B 1 339 ? 74.239  71.759  107.725 1.00 29.21 ? 328  TYR B OH  1 
ATOM   5691 N  N   . ILE B 1 340 ? 68.696  68.640  105.974 1.00 34.48 ? 329  ILE B N   1 
ATOM   5692 C  CA  . ILE B 1 340 ? 68.320  68.497  107.377 1.00 34.48 ? 329  ILE B CA  1 
ATOM   5693 C  C   . ILE B 1 340 ? 68.289  67.027  107.767 1.00 34.48 ? 329  ILE B C   1 
ATOM   5694 O  O   . ILE B 1 340 ? 68.735  66.651  108.857 1.00 34.48 ? 329  ILE B O   1 
ATOM   5695 C  CB  . ILE B 1 340 ? 66.970  69.185  107.648 1.00 34.48 ? 329  ILE B CB  1 
ATOM   5696 C  CG1 . ILE B 1 340 ? 67.096  70.704  107.487 1.00 34.48 ? 329  ILE B CG1 1 
ATOM   5697 C  CG2 . ILE B 1 340 ? 66.476  68.839  109.036 1.00 34.48 ? 329  ILE B CG2 1 
ATOM   5698 C  CD1 . ILE B 1 340 ? 68.007  71.373  108.491 1.00 34.48 ? 329  ILE B CD1 1 
ATOM   5699 N  N   . GLN B 1 341 ? 67.769  66.170  106.889 1.00 36.71 ? 330  GLN B N   1 
ATOM   5700 C  CA  . GLN B 1 341 ? 67.780  64.742  107.191 1.00 36.71 ? 330  GLN B CA  1 
ATOM   5701 C  C   . GLN B 1 341 ? 69.203  64.213  107.306 1.00 36.71 ? 330  GLN B C   1 
ATOM   5702 O  O   . GLN B 1 341 ? 69.513  63.437  108.218 1.00 36.71 ? 330  GLN B O   1 
ATOM   5703 C  CB  . GLN B 1 341 ? 67.014  63.966  106.126 1.00 36.71 ? 330  GLN B CB  1 
ATOM   5704 C  CG  . GLN B 1 341 ? 66.314  62.742  106.676 1.00 36.71 ? 330  GLN B CG  1 
ATOM   5705 C  CD  . GLN B 1 341 ? 65.929  61.760  105.598 1.00 36.71 ? 330  GLN B CD  1 
ATOM   5706 O  OE1 . GLN B 1 341 ? 66.672  61.549  104.641 1.00 36.71 ? 330  GLN B OE1 1 
ATOM   5707 N  NE2 . GLN B 1 341 ? 64.760  61.149  105.746 1.00 36.71 ? 330  GLN B NE2 1 
ATOM   5708 N  N   . ALA B 1 342 ? 70.083  64.619  106.390 1.00 34.24 ? 331  ALA B N   1 
ATOM   5709 C  CA  . ALA B 1 342 ? 71.467  64.159  106.445 1.00 34.24 ? 331  ALA B CA  1 
ATOM   5710 C  C   . ALA B 1 342 ? 72.132  64.576  107.749 1.00 34.24 ? 331  ALA B C   1 
ATOM   5711 O  O   . ALA B 1 342 ? 72.857  63.789  108.368 1.00 34.24 ? 331  ALA B O   1 
ATOM   5712 C  CB  . ALA B 1 342 ? 72.247  64.707  105.252 1.00 34.24 ? 331  ALA B CB  1 
ATOM   5713 N  N   . VAL B 1 343 ? 71.895  65.814  108.183 1.00 34.46 ? 332  VAL B N   1 
ATOM   5714 C  CA  . VAL B 1 343 ? 72.465  66.279  109.444 1.00 34.46 ? 332  VAL B CA  1 
ATOM   5715 C  C   . VAL B 1 343 ? 71.868  65.509  110.614 1.00 34.46 ? 332  VAL B C   1 
ATOM   5716 O  O   . VAL B 1 343 ? 72.554  65.232  111.604 1.00 34.46 ? 332  VAL B O   1 
ATOM   5717 C  CB  . VAL B 1 343 ? 72.256  67.794  109.599 1.00 34.46 ? 332  VAL B CB  1 
ATOM   5718 C  CG1 . VAL B 1 343 ? 72.824  68.270  110.915 1.00 34.46 ? 332  VAL B CG1 1 
ATOM   5719 C  CG2 . VAL B 1 343 ? 72.903  68.533  108.458 1.00 34.46 ? 332  VAL B CG2 1 
ATOM   5720 N  N   . THR B 1 344 ? 70.584  65.159  110.531 1.00 38.08 ? 333  THR B N   1 
ATOM   5721 C  CA  . THR B 1 344 ? 69.978  64.359  111.589 1.00 38.08 ? 333  THR B CA  1 
ATOM   5722 C  C   . THR B 1 344 ? 70.679  63.015  111.716 1.00 38.08 ? 333  THR B C   1 
ATOM   5723 O  O   . THR B 1 344 ? 71.003  62.571  112.822 1.00 38.08 ? 333  THR B O   1 
ATOM   5724 C  CB  . THR B 1 344 ? 68.489  64.158  111.314 1.00 38.08 ? 333  THR B CB  1 
ATOM   5725 O  OG1 . THR B 1 344 ? 67.805  65.411  111.423 1.00 38.08 ? 333  THR B OG1 1 
ATOM   5726 C  CG2 . THR B 1 344 ? 67.894  63.173  112.302 1.00 38.08 ? 333  THR B CG2 1 
ATOM   5727 N  N   . GLU B 1 345 ? 70.935  62.356  110.585 1.00 38.35 ? 334  GLU B N   1 
ATOM   5728 C  CA  . GLU B 1 345 ? 71.649  61.082  110.636 1.00 38.35 ? 334  GLU B CA  1 
ATOM   5729 C  C   . GLU B 1 345 ? 73.059  61.268  111.181 1.00 38.35 ? 334  GLU B C   1 
ATOM   5730 O  O   . GLU B 1 345 ? 73.540  60.453  111.982 1.00 38.35 ? 334  GLU B O   1 
ATOM   5731 C  CB  . GLU B 1 345 ? 71.698  60.432  109.253 1.00 38.35 ? 334  GLU B CB  1 
ATOM   5732 C  CG  . GLU B 1 345 ? 70.360  59.977  108.717 1.00 38.35 ? 334  GLU B CG  1 
ATOM   5733 C  CD  . GLU B 1 345 ? 70.453  59.409  107.322 1.00 38.35 ? 334  GLU B CD  1 
ATOM   5734 O  OE1 . GLU B 1 345 ? 71.525  59.542  106.697 1.00 38.35 ? 334  GLU B OE1 1 
ATOM   5735 O  OE2 . GLU B 1 345 ? 69.455  58.829  106.850 1.00 38.35 ? 334  GLU B OE2 1 
ATOM   5736 N  N   . THR B 1 346 ? 73.740  62.336  110.761 1.00 37.86 ? 335  THR B N   1 
ATOM   5737 C  CA  . THR B 1 346 ? 75.099  62.571  111.234 1.00 37.86 ? 335  THR B CA  1 
ATOM   5738 C  C   . THR B 1 346 ? 75.132  62.739  112.748 1.00 37.86 ? 335  THR B C   1 
ATOM   5739 O  O   . THR B 1 346 ? 75.993  62.165  113.423 1.00 37.86 ? 335  THR B O   1 
ATOM   5740 C  CB  . THR B 1 346 ? 75.691  63.800  110.545 1.00 37.86 ? 335  THR B CB  1 
ATOM   5741 O  OG1 . THR B 1 346 ? 75.746  63.576  109.132 1.00 37.86 ? 335  THR B OG1 1 
ATOM   5742 C  CG2 . THR B 1 346 ? 77.090  64.075  111.052 1.00 37.86 ? 335  THR B CG2 1 
ATOM   5743 N  N   . LEU B 1 347 ? 74.201  63.517  113.303 1.00 40.08 ? 336  LEU B N   1 
ATOM   5744 C  CA  . LEU B 1 347 ? 74.140  63.651  114.755 1.00 40.08 ? 336  LEU B CA  1 
ATOM   5745 C  C   . LEU B 1 347 ? 73.707  62.352  115.420 1.00 40.08 ? 336  LEU B C   1 
ATOM   5746 O  O   . LEU B 1 347 ? 74.067  62.101  116.574 1.00 40.08 ? 336  LEU B O   1 
ATOM   5747 C  CB  . LEU B 1 347 ? 73.190  64.777  115.159 1.00 40.08 ? 336  LEU B CB  1 
ATOM   5748 C  CG  . LEU B 1 347 ? 73.442  66.156  114.556 1.00 40.08 ? 336  LEU B CG  1 
ATOM   5749 C  CD1 . LEU B 1 347 ? 72.359  67.119  114.998 1.00 40.08 ? 336  LEU B CD1 1 
ATOM   5750 C  CD2 . LEU B 1 347 ? 74.807  66.673  114.954 1.00 40.08 ? 336  LEU B CD2 1 
ATOM   5751 N  N   . ALA B 1 348 ? 72.931  61.523  114.720 1.00 42.17 ? 337  ALA B N   1 
ATOM   5752 C  CA  . ALA B 1 348 ? 72.525  60.246  115.294 1.00 42.17 ? 337  ALA B CA  1 
ATOM   5753 C  C   . ALA B 1 348 ? 73.692  59.276  115.390 1.00 42.17 ? 337  ALA B C   1 
ATOM   5754 O  O   . ALA B 1 348 ? 73.700  58.408  116.268 1.00 42.17 ? 337  ALA B O   1 
ATOM   5755 C  CB  . ALA B 1 348 ? 71.401  59.629  114.465 1.00 42.17 ? 337  ALA B CB  1 
ATOM   5756 N  N   . HIS B 1 349 ? 74.682  59.403  114.507 1.00 44.38 ? 338  HIS B N   1 
ATOM   5757 C  CA  . HIS B 1 349 ? 75.820  58.491  114.485 1.00 44.38 ? 338  HIS B CA  1 
ATOM   5758 C  C   . HIS B 1 349 ? 77.060  59.074  115.155 1.00 44.38 ? 338  HIS B C   1 
ATOM   5759 O  O   . HIS B 1 349 ? 78.176  58.637  114.860 1.00 44.38 ? 338  HIS B O   1 
ATOM   5760 C  CB  . HIS B 1 349 ? 76.138  58.084  113.047 1.00 44.38 ? 338  HIS B CB  1 
ATOM   5761 C  CG  . HIS B 1 349 ? 75.092  57.215  112.426 1.00 44.38 ? 338  HIS B CG  1 
ATOM   5762 N  ND1 . HIS B 1 349 ? 74.468  57.537  111.240 1.00 44.38 ? 338  HIS B ND1 1 
ATOM   5763 C  CD2 . HIS B 1 349 ? 74.564  56.032  112.819 1.00 44.38 ? 338  HIS B CD2 1 
ATOM   5764 C  CE1 . HIS B 1 349 ? 73.598  56.592  110.932 1.00 44.38 ? 338  HIS B CE1 1 
ATOM   5765 N  NE2 . HIS B 1 349 ? 73.636  55.667  111.874 1.00 44.38 ? 338  HIS B NE2 1 
ATOM   5766 N  N   . GLY B 1 350 ? 76.889  60.042  116.050 1.00 43.61 ? 339  GLY B N   1 
ATOM   5767 C  CA  . GLY B 1 350 ? 78.004  60.573  116.811 1.00 43.61 ? 339  GLY B CA  1 
ATOM   5768 C  C   . GLY B 1 350 ? 78.867  61.554  116.046 1.00 43.61 ? 339  GLY B C   1 
ATOM   5769 O  O   . GLY B 1 350 ? 80.087  61.385  115.968 1.00 43.61 ? 339  GLY B O   1 
ATOM   5770 N  N   . GLY B 1 351 ? 78.247  62.586  115.479 1.00 40.99 ? 340  GLY B N   1 
ATOM   5771 C  CA  . GLY B 1 351 ? 78.975  63.616  114.764 1.00 40.99 ? 340  GLY B CA  1 
ATOM   5772 C  C   . GLY B 1 351 ? 78.555  65.007  115.186 1.00 40.99 ? 340  GLY B C   1 
ATOM   5773 O  O   . GLY B 1 351 ? 77.995  65.189  116.269 1.00 40.99 ? 340  GLY B O   1 
ATOM   5774 N  N   . THR B 1 352 ? 78.821  65.999  114.339 1.00 39.78 ? 341  THR B N   1 
ATOM   5775 C  CA  . THR B 1 352 ? 78.428  67.374  114.605 1.00 39.78 ? 341  THR B CA  1 
ATOM   5776 C  C   . THR B 1 352 ? 77.959  68.021  113.310 1.00 39.78 ? 341  THR B C   1 
ATOM   5777 O  O   . THR B 1 352 ? 78.234  67.533  112.213 1.00 39.78 ? 341  THR B O   1 
ATOM   5778 C  CB  . THR B 1 352 ? 79.576  68.189  115.211 1.00 39.78 ? 341  THR B CB  1 
ATOM   5779 O  OG1 . THR B 1 352 ? 80.672  68.233  114.291 1.00 39.78 ? 341  THR B OG1 1 
ATOM   5780 C  CG2 . THR B 1 352 ? 80.039  67.573  116.516 1.00 39.78 ? 341  THR B CG2 1 
ATOM   5781 N  N   . VAL B 1 353 ? 77.239  69.136  113.453 1.00 37.67 ? 342  VAL B N   1 
ATOM   5782 C  CA  . VAL B 1 353 ? 76.728  69.856  112.293 1.00 37.67 ? 342  VAL B CA  1 
ATOM   5783 C  C   . VAL B 1 353 ? 77.831  70.477  111.453 1.00 37.67 ? 342  VAL B C   1 
ATOM   5784 O  O   . VAL B 1 353 ? 77.560  70.943  110.342 1.00 37.67 ? 342  VAL B O   1 
ATOM   5785 C  CB  . VAL B 1 353 ? 75.738  70.955  112.727 1.00 37.67 ? 342  VAL B CB  1 
ATOM   5786 C  CG1 . VAL B 1 353 ? 74.548  70.340  113.431 1.00 37.67 ? 342  VAL B CG1 1 
ATOM   5787 C  CG2 . VAL B 1 353 ? 76.419  71.975  113.621 1.00 37.67 ? 342  VAL B CG2 1 
ATOM   5788 N  N   . THR B 1 354 ? 79.064  70.502  111.954 1.00 38.28 ? 343  THR B N   1 
ATOM   5789 C  CA  . THR B 1 354 ? 80.191  71.074  111.235 1.00 38.28 ? 343  THR B CA  1 
ATOM   5790 C  C   . THR B 1 354 ? 80.991  70.027  110.469 1.00 38.28 ? 343  THR B C   1 
ATOM   5791 O  O   . THR B 1 354 ? 82.022  70.361  109.880 1.00 38.28 ? 343  THR B O   1 
ATOM   5792 C  CB  . THR B 1 354 ? 81.110  71.818  112.204 1.00 38.28 ? 343  THR B CB  1 
ATOM   5793 O  OG1 . THR B 1 354 ? 81.840  70.874  112.995 1.00 38.28 ? 343  THR B OG1 1 
ATOM   5794 C  CG2 . THR B 1 354 ? 80.303  72.722  113.117 1.00 38.28 ? 343  THR B CG2 1 
ATOM   5795 N  N   . ASP B 1 355 ? 80.545  68.773  110.468 1.00 36.65 ? 344  ASP B N   1 
ATOM   5796 C  CA  . ASP B 1 355 ? 81.196  67.712  109.701 1.00 36.65 ? 344  ASP B CA  1 
ATOM   5797 C  C   . ASP B 1 355 ? 80.739  67.833  108.257 1.00 36.65 ? 344  ASP B C   1 
ATOM   5798 O  O   . ASP B 1 355 ? 79.733  67.255  107.848 1.00 36.65 ? 344  ASP B O   1 
ATOM   5799 C  CB  . ASP B 1 355 ? 80.859  66.344  110.276 1.00 36.65 ? 344  ASP B CB  1 
ATOM   5800 C  CG  . ASP B 1 355 ? 81.639  66.032  111.531 1.00 36.65 ? 344  ASP B CG  1 
ATOM   5801 O  OD1 . ASP B 1 355 ? 82.860  65.799  111.428 1.00 36.65 ? 344  ASP B OD1 1 
ATOM   5802 O  OD2 . ASP B 1 355 ? 81.032  66.019  112.622 1.00 36.65 ? 344  ASP B OD2 1 
ATOM   5803 N  N   . GLY B 1 356 ? 81.488  68.602  107.469 1.00 30.29 ? 345  GLY B N   1 
ATOM   5804 C  CA  . GLY B 1 356 ? 81.093  68.818  106.089 1.00 30.29 ? 345  GLY B CA  1 
ATOM   5805 C  C   . GLY B 1 356 ? 81.082  67.538  105.280 1.00 30.29 ? 345  GLY B C   1 
ATOM   5806 O  O   . GLY B 1 356 ? 80.121  67.251  104.564 1.00 30.29 ? 345  GLY B O   1 
ATOM   5807 N  N   . GLU B 1 357 ? 82.145  66.740  105.396 1.00 30.48 ? 346  GLU B N   1 
ATOM   5808 C  CA  . GLU B 1 357 ? 82.291  65.569  104.537 1.00 30.48 ? 346  GLU B CA  1 
ATOM   5809 C  C   . GLU B 1 357 ? 81.283  64.484  104.896 1.00 30.48 ? 346  GLU B C   1 
ATOM   5810 O  O   . GLU B 1 357 ? 80.621  63.924  104.016 1.00 30.48 ? 346  GLU B O   1 
ATOM   5811 C  CB  . GLU B 1 357 ? 83.716  65.030  104.633 1.00 30.48 ? 346  GLU B CB  1 
ATOM   5812 N  N   . ASN B 1 358 ? 81.158  64.168  106.184 1.00 33.91 ? 347  ASN B N   1 
ATOM   5813 C  CA  . ASN B 1 358 ? 80.226  63.121  106.589 1.00 33.91 ? 347  ASN B CA  1 
ATOM   5814 C  C   . ASN B 1 358 ? 78.790  63.515  106.282 1.00 33.91 ? 347  ASN B C   1 
ATOM   5815 O  O   . ASN B 1 358 ? 77.983  62.673  105.877 1.00 33.91 ? 347  ASN B O   1 
ATOM   5816 C  CB  . ASN B 1 358 ? 80.392  62.815  108.075 1.00 33.91 ? 347  ASN B CB  1 
ATOM   5817 C  CG  . ASN B 1 358 ? 81.744  62.222  108.399 1.00 33.91 ? 347  ASN B CG  1 
ATOM   5818 O  OD1 . ASN B 1 358 ? 82.551  62.833  109.094 1.00 33.91 ? 347  ASN B OD1 1 
ATOM   5819 N  ND2 . ASN B 1 358 ? 81.998  61.022  107.897 1.00 33.91 ? 347  ASN B ND2 1 
ATOM   5820 N  N   . ILE B 1 359 ? 78.445  64.785  106.484 1.00 32.96 ? 348  ILE B N   1 
ATOM   5821 C  CA  . ILE B 1 359 ? 77.100  65.242  106.155 1.00 32.96 ? 348  ILE B CA  1 
ATOM   5822 C  C   . ILE B 1 359 ? 76.862  65.146  104.656 1.00 32.96 ? 348  ILE B C   1 
ATOM   5823 O  O   . ILE B 1 359 ? 75.855  64.589  104.208 1.00 32.96 ? 348  ILE B O   1 
ATOM   5824 C  CB  . ILE B 1 359 ? 76.875  66.678  106.660 1.00 32.96 ? 348  ILE B CB  1 
ATOM   5825 C  CG1 . ILE B 1 359 ? 76.817  66.704  108.185 1.00 32.96 ? 348  ILE B CG1 1 
ATOM   5826 C  CG2 . ILE B 1 359 ? 75.602  67.245  106.068 1.00 32.96 ? 348  ILE B CG2 1 
ATOM   5827 C  CD1 . ILE B 1 359 ? 76.865  68.087  108.768 1.00 32.96 ? 348  ILE B CD1 1 
ATOM   5828 N  N   . THR B 1 360 ? 77.788  65.676  103.855 1.00 30.04 ? 349  THR B N   1 
ATOM   5829 C  CA  . THR B 1 360 ? 77.528  65.783  102.426 1.00 30.04 ? 349  THR B CA  1 
ATOM   5830 C  C   . THR B 1 360 ? 77.529  64.421  101.753 1.00 30.04 ? 349  THR B C   1 
ATOM   5831 O  O   . THR B 1 360 ? 76.786  64.214  100.790 1.00 30.04 ? 349  THR B O   1 
ATOM   5832 C  CB  . THR B 1 360 ? 78.550  66.704  101.764 1.00 30.04 ? 349  THR B CB  1 
ATOM   5833 O  OG1 . THR B 1 360 ? 78.043  67.150  100.505 1.00 30.04 ? 349  THR B OG1 1 
ATOM   5834 C  CG2 . THR B 1 360 ? 79.848  65.977  101.522 1.00 30.04 ? 349  THR B CG2 1 
ATOM   5835 N  N   . GLN B 1 361 ? 78.340  63.479  102.230 1.00 33.68 ? 350  GLN B N   1 
ATOM   5836 C  CA  . GLN B 1 361 ? 78.345  62.159  101.615 1.00 33.68 ? 350  GLN B CA  1 
ATOM   5837 C  C   . GLN B 1 361 ? 77.167  61.305  102.059 1.00 33.68 ? 350  GLN B C   1 
ATOM   5838 O  O   . GLN B 1 361 ? 76.997  60.198  101.542 1.00 33.68 ? 350  GLN B O   1 
ATOM   5839 C  CB  . GLN B 1 361 ? 79.668  61.444  101.905 1.00 33.68 ? 350  GLN B CB  1 
ATOM   5840 C  CG  . GLN B 1 361 ? 79.824  60.877  103.302 1.00 33.68 ? 350  GLN B CG  1 
ATOM   5841 C  CD  . GLN B 1 361 ? 80.887  59.803  103.362 1.00 33.68 ? 350  GLN B CD  1 
ATOM   5842 O  OE1 . GLN B 1 361 ? 81.997  60.040  103.837 1.00 33.68 ? 350  GLN B OE1 1 
ATOM   5843 N  NE2 . GLN B 1 361 ? 80.557  58.616  102.869 1.00 33.68 ? 350  GLN B NE2 1 
ATOM   5844 N  N   . ARG B 1 362 ? 76.363  61.782  103.004 1.00 35.99 ? 351  ARG B N   1 
ATOM   5845 C  CA  . ARG B 1 362 ? 75.066  61.193  103.299 1.00 35.99 ? 351  ARG B CA  1 
ATOM   5846 C  C   . ARG B 1 362 ? 73.946  61.832  102.492 1.00 35.99 ? 351  ARG B C   1 
ATOM   5847 O  O   . ARG B 1 362 ? 72.795  61.404  102.608 1.00 35.99 ? 351  ARG B O   1 
ATOM   5848 C  CB  . ARG B 1 362 ? 74.755  61.322  104.788 1.00 35.99 ? 351  ARG B CB  1 
ATOM   5849 C  CG  . ARG B 1 362 ? 75.551  60.382  105.653 1.00 35.99 ? 351  ARG B CG  1 
ATOM   5850 C  CD  . ARG B 1 362 ? 74.872  60.151  106.977 1.00 35.99 ? 351  ARG B CD  1 
ATOM   5851 N  NE  . ARG B 1 362 ? 75.829  59.724  107.993 1.00 35.99 ? 351  ARG B NE  1 
ATOM   5852 C  CZ  . ARG B 1 362 ? 75.850  58.526  108.570 1.00 35.99 ? 351  ARG B CZ  1 
ATOM   5853 N  NH1 . ARG B 1 362 ? 74.964  57.592  108.249 1.00 35.99 ? 351  ARG B NH1 1 
ATOM   5854 N  NH2 . ARG B 1 362 ? 76.773  58.260  109.482 1.00 35.99 ? 351  ARG B NH2 1 
ATOM   5855 N  N   . MET B 1 363 ? 74.257  62.854  101.697 1.00 30.72 ? 352  MET B N   1 
ATOM   5856 C  CA  . MET B 1 363 ? 73.321  63.473  100.769 1.00 30.72 ? 352  MET B CA  1 
ATOM   5857 C  C   . MET B 1 363 ? 73.471  62.935  99.359  1.00 30.72 ? 352  MET B C   1 
ATOM   5858 O  O   . MET B 1 363 ? 72.473  62.652  98.696  1.00 30.72 ? 352  MET B O   1 
ATOM   5859 C  CB  . MET B 1 363 ? 73.540  64.986  100.725 1.00 30.72 ? 352  MET B CB  1 
ATOM   5860 C  CG  . MET B 1 363 ? 73.597  65.657  102.077 1.00 30.72 ? 352  MET B CG  1 
ATOM   5861 S  SD  . MET B 1 363 ? 73.626  67.455  101.993 1.00 30.72 ? 352  MET B SD  1 
ATOM   5862 C  CE  . MET B 1 363 ? 72.344  67.787  100.802 1.00 30.72 ? 352  MET B CE  1 
ATOM   5863 N  N   . TRP B 1 364 ? 74.705  62.799  98.892  1.00 30.07 ? 353  TRP B N   1 
ATOM   5864 C  CA  . TRP B 1 364 ? 74.959  62.333  97.542  1.00 30.07 ? 353  TRP B CA  1 
ATOM   5865 C  C   . TRP B 1 364 ? 74.620  60.855  97.429  1.00 30.07 ? 353  TRP B C   1 
ATOM   5866 O  O   . TRP B 1 364 ? 74.697  60.101  98.401  1.00 30.07 ? 353  TRP B O   1 
ATOM   5867 C  CB  . TRP B 1 364 ? 76.426  62.554  97.175  1.00 30.07 ? 353  TRP B CB  1 
ATOM   5868 C  CG  . TRP B 1 364 ? 76.876  63.984  97.193  1.00 30.07 ? 353  TRP B CG  1 
ATOM   5869 C  CD1 . TRP B 1 364 ? 76.144  65.077  97.545  1.00 30.07 ? 353  TRP B CD1 1 
ATOM   5870 C  CD2 . TRP B 1 364 ? 78.178  64.469  96.850  1.00 30.07 ? 353  TRP B CD2 1 
ATOM   5871 N  NE1 . TRP B 1 364 ? 76.906  66.213  97.437  1.00 30.07 ? 353  TRP B NE1 1 
ATOM   5872 C  CE2 . TRP B 1 364 ? 78.160  65.866  97.013  1.00 30.07 ? 353  TRP B CE2 1 
ATOM   5873 C  CE3 . TRP B 1 364 ? 79.355  63.857  96.417  1.00 30.07 ? 353  TRP B CE3 1 
ATOM   5874 C  CZ2 . TRP B 1 364 ? 79.273  66.660  96.756  1.00 30.07 ? 353  TRP B CZ2 1 
ATOM   5875 C  CZ3 . TRP B 1 364 ? 80.457  64.644  96.166  1.00 30.07 ? 353  TRP B CZ3 1 
ATOM   5876 C  CH2 . TRP B 1 364 ? 80.410  66.030  96.336  1.00 30.07 ? 353  TRP B CH2 1 
ATOM   5877 N  N   . ASN B 1 365 ? 74.397  60.402  96.213  1.00 36.50 ? 354  ASN B N   1 
ATOM   5878 C  CA  . ASN B 1 365 ? 74.076  59.008  95.834  1.00 36.50 ? 354  ASN B CA  1 
ATOM   5879 C  C   . ASN B 1 365 ? 72.922  58.395  96.620  1.00 36.50 ? 354  ASN B C   1 
ATOM   5880 O  O   . ASN B 1 365 ? 72.994  57.220  96.836  1.00 36.50 ? 354  ASN B O   1 
ATOM   5881 C  CB  . ASN B 1 365 ? 75.327  58.154  95.944  1.00 36.50 ? 354  ASN B CB  1 
ATOM   5882 C  CG  . ASN B 1 365 ? 75.198  56.788  95.340  1.00 36.50 ? 354  ASN B CG  1 
ATOM   5883 O  OD1 . ASN B 1 365 ? 74.549  56.622  94.334  1.00 36.50 ? 354  ASN B OD1 1 
ATOM   5884 N  ND2 . ASN B 1 365 ? 75.835  55.810  95.947  1.00 36.50 ? 354  ASN B ND2 1 
ATOM   5885 N  N   . ARG B 1 366 ? 71.850  59.113  96.925  1.00 36.53 ? 355  ARG B N   1 
ATOM   5886 C  CA  . ARG B 1 366 ? 70.700  58.563  97.627  1.00 36.53 ? 355  ARG B CA  1 
ATOM   5887 C  C   . ARG B 1 366 ? 69.416  59.165  97.078  1.00 36.53 ? 355  ARG B C   1 
ATOM   5888 O  O   . ARG B 1 366 ? 69.427  60.189  96.393  1.00 36.53 ? 355  ARG B O   1 
ATOM   5889 C  CB  . ARG B 1 366 ? 70.790  58.807  99.138  1.00 36.53 ? 355  ARG B CB  1 
ATOM   5890 C  CG  . ARG B 1 366 ? 70.385  60.195  99.588  1.00 36.53 ? 355  ARG B CG  1 
ATOM   5891 C  CD  . ARG B 1 366 ? 70.487  60.316  101.094 1.00 36.53 ? 355  ARG B CD  1 
ATOM   5892 N  NE  . ARG B 1 366 ? 69.489  59.502  101.778 1.00 36.53 ? 355  ARG B NE  1 
ATOM   5893 C  CZ  . ARG B 1 366 ? 69.525  59.207  103.074 1.00 36.53 ? 355  ARG B CZ  1 
ATOM   5894 N  NH1 . ARG B 1 366 ? 70.511  59.661  103.837 1.00 36.53 ? 355  ARG B NH1 1 
ATOM   5895 N  NH2 . ARG B 1 366 ? 68.573  58.457  103.609 1.00 36.53 ? 355  ARG B NH2 1 
ATOM   5896 N  N   . SER B 1 367 ? 68.304  58.511  97.398  1.00 37.04 ? 356  SER B N   1 
ATOM   5897 C  CA  . SER B 1 367 ? 66.981  58.936  96.970  1.00 37.04 ? 356  SER B CA  1 
ATOM   5898 C  C   . SER B 1 367 ? 66.239  59.613  98.115  1.00 37.04 ? 356  SER B C   1 
ATOM   5899 O  O   . SER B 1 367 ? 66.429  59.283  99.288  1.00 37.04 ? 356  SER B O   1 
ATOM   5900 C  CB  . SER B 1 367 ? 66.163  57.751  96.464  1.00 37.04 ? 356  SER B CB  1 
ATOM   5901 O  OG  . SER B 1 367 ? 66.489  57.440  95.121  1.00 37.04 ? 356  SER B OG  1 
ATOM   5902 N  N   . PHE B 1 368 ? 65.382  60.564  97.757  1.00 33.97 ? 357  PHE B N   1 
ATOM   5903 C  CA  . PHE B 1 368 ? 64.646  61.358  98.727  1.00 33.97 ? 357  PHE B CA  1 
ATOM   5904 C  C   . PHE B 1 368 ? 63.222  61.566  98.235  1.00 33.97 ? 357  PHE B C   1 
ATOM   5905 O  O   . PHE B 1 368 ? 62.965  61.617  97.031  1.00 33.97 ? 357  PHE B O   1 
ATOM   5906 C  CB  . PHE B 1 368 ? 65.323  62.713  98.966  1.00 33.97 ? 357  PHE B CB  1 
ATOM   5907 C  CG  . PHE B 1 368 ? 64.712  63.504  100.079 1.00 33.97 ? 357  PHE B CG  1 
ATOM   5908 C  CD1 . PHE B 1 368 ? 64.899  63.127  101.395 1.00 33.97 ? 357  PHE B CD1 1 
ATOM   5909 C  CD2 . PHE B 1 368 ? 63.943  64.621  99.813  1.00 33.97 ? 357  PHE B CD2 1 
ATOM   5910 C  CE1 . PHE B 1 368 ? 64.334  63.848  102.421 1.00 33.97 ? 357  PHE B CE1 1 
ATOM   5911 C  CE2 . PHE B 1 368 ? 63.376  65.344  100.837 1.00 33.97 ? 357  PHE B CE2 1 
ATOM   5912 C  CZ  . PHE B 1 368 ? 63.572  64.956  102.142 1.00 33.97 ? 357  PHE B CZ  1 
ATOM   5913 N  N   . GLN B 1 369 ? 62.296  61.685  99.179  1.00 36.67 ? 358  GLN B N   1 
ATOM   5914 C  CA  . GLN B 1 369 ? 60.889  61.915  98.876  1.00 36.67 ? 358  GLN B CA  1 
ATOM   5915 C  C   . GLN B 1 369 ? 60.564  63.368  99.199  1.00 36.67 ? 358  GLN B C   1 
ATOM   5916 O  O   . GLN B 1 369 ? 60.603  63.775  100.363 1.00 36.67 ? 358  GLN B O   1 
ATOM   5917 C  CB  . GLN B 1 369 ? 60.002  60.960  99.671  1.00 36.67 ? 358  GLN B CB  1 
ATOM   5918 C  CG  . GLN B 1 369 ? 58.513  61.261  99.583  1.00 36.67 ? 358  GLN B CG  1 
ATOM   5919 C  CD  . GLN B 1 369 ? 57.959  61.046  98.194  1.00 36.67 ? 358  GLN B CD  1 
ATOM   5920 O  OE1 . GLN B 1 369 ? 58.460  60.220  97.437  1.00 36.67 ? 358  GLN B OE1 1 
ATOM   5921 N  NE2 . GLN B 1 369 ? 56.920  61.793  97.849  1.00 36.67 ? 358  GLN B NE2 1 
ATOM   5922 N  N   . GLY B 1 370 ? 60.240  64.146  98.169  1.00 34.86 ? 359  GLY B N   1 
ATOM   5923 C  CA  . GLY B 1 370 ? 59.900  65.542  98.351  1.00 34.86 ? 359  GLY B CA  1 
ATOM   5924 C  C   . GLY B 1 370 ? 58.621  65.924  97.639  1.00 34.86 ? 359  GLY B C   1 
ATOM   5925 O  O   . GLY B 1 370 ? 57.910  65.056  97.127  1.00 34.86 ? 359  GLY B O   1 
ATOM   5926 N  N   . VAL B 1 371 ? 58.312  67.222  97.599  1.00 33.47 ? 360  VAL B N   1 
ATOM   5927 C  CA  . VAL B 1 371 ? 57.109  67.663  96.902  1.00 33.47 ? 360  VAL B CA  1 
ATOM   5928 C  C   . VAL B 1 371 ? 57.230  67.408  95.407  1.00 33.47 ? 360  VAL B C   1 
ATOM   5929 O  O   . VAL B 1 371 ? 56.231  67.122  94.738  1.00 33.47 ? 360  VAL B O   1 
ATOM   5930 C  CB  . VAL B 1 371 ? 56.820  69.146  97.196  1.00 33.47 ? 360  VAL B CB  1 
ATOM   5931 C  CG1 . VAL B 1 371 ? 56.349  69.315  98.626  1.00 33.47 ? 360  VAL B CG1 1 
ATOM   5932 C  CG2 . VAL B 1 371 ? 58.042  70.006  96.924  1.00 33.47 ? 360  VAL B CG2 1 
ATOM   5933 N  N   . THR B 1 372 ? 58.439  67.498  94.857  1.00 34.14 ? 361  THR B N   1 
ATOM   5934 C  CA  . THR B 1 372 ? 58.671  67.284  93.437  1.00 34.14 ? 361  THR B CA  1 
ATOM   5935 C  C   . THR B 1 372 ? 58.836  65.812  93.085  1.00 34.14 ? 361  THR B C   1 
ATOM   5936 O  O   . THR B 1 372 ? 59.410  65.495  92.038  1.00 34.14 ? 361  THR B O   1 
ATOM   5937 C  CB  . THR B 1 372 ? 59.903  68.068  92.981  1.00 34.14 ? 361  THR B CB  1 
ATOM   5938 O  OG1 . THR B 1 372 ? 61.030  67.705  93.786  1.00 34.14 ? 361  THR B OG1 1 
ATOM   5939 C  CG2 . THR B 1 372 ? 59.663  69.554  93.103  1.00 34.14 ? 361  THR B CG2 1 
ATOM   5940 N  N   . GLY B 1 373 ? 58.353  64.912  93.930  1.00 36.40 ? 362  GLY B N   1 
ATOM   5941 C  CA  . GLY B 1 373 ? 58.388  63.495  93.648  1.00 36.40 ? 362  GLY B CA  1 
ATOM   5942 C  C   . GLY B 1 373 ? 59.542  62.790  94.326  1.00 36.40 ? 362  GLY B C   1 
ATOM   5943 O  O   . GLY B 1 373 ? 60.164  63.291  95.265  1.00 36.40 ? 362  GLY B O   1 
ATOM   5944 N  N   . TYR B 1 374 ? 59.823  61.589  93.833  1.00 39.34 ? 363  TYR B N   1 
ATOM   5945 C  CA  . TYR B 1 374 ? 60.939  60.784  94.317  1.00 39.34 ? 363  TYR B CA  1 
ATOM   5946 C  C   . TYR B 1 374 ? 62.176  61.159  93.512  1.00 39.34 ? 363  TYR B C   1 
ATOM   5947 O  O   . TYR B 1 374 ? 62.275  60.830  92.327  1.00 39.34 ? 363  TYR B O   1 
ATOM   5948 C  CB  . TYR B 1 374 ? 60.621  59.298  94.186  1.00 39.34 ? 363  TYR B CB  1 
ATOM   5949 C  CG  . TYR B 1 374 ? 61.326  58.433  95.199  1.00 39.34 ? 363  TYR B CG  1 
ATOM   5950 C  CD1 . TYR B 1 374 ? 60.932  58.428  96.527  1.00 39.34 ? 363  TYR B CD1 1 
ATOM   5951 C  CD2 . TYR B 1 374 ? 62.380  57.618  94.828  1.00 39.34 ? 363  TYR B CD2 1 
ATOM   5952 C  CE1 . TYR B 1 374 ? 61.572  57.641  97.456  1.00 39.34 ? 363  TYR B CE1 1 
ATOM   5953 C  CE2 . TYR B 1 374 ? 63.023  56.826  95.749  1.00 39.34 ? 363  TYR B CE2 1 
ATOM   5954 C  CZ  . TYR B 1 374 ? 62.618  56.844  97.062  1.00 39.34 ? 363  TYR B CZ  1 
ATOM   5955 O  OH  . TYR B 1 374 ? 63.260  56.054  97.986  1.00 39.34 ? 363  TYR B OH  1 
ATOM   5956 N  N   . LEU B 1 375 ? 63.117  61.845  94.151  1.00 33.69 ? 364  LEU B N   1 
ATOM   5957 C  CA  . LEU B 1 375 ? 64.276  62.396  93.470  1.00 33.69 ? 364  LEU B CA  1 
ATOM   5958 C  C   . LEU B 1 375 ? 65.534  61.630  93.853  1.00 33.69 ? 364  LEU B C   1 
ATOM   5959 O  O   . LEU B 1 375 ? 65.599  60.972  94.893  1.00 33.69 ? 364  LEU B O   1 
ATOM   5960 C  CB  . LEU B 1 375 ? 64.435  63.886  93.791  1.00 33.69 ? 364  LEU B CB  1 
ATOM   5961 C  CG  . LEU B 1 375 ? 64.671  64.297  95.244  1.00 33.69 ? 364  LEU B CG  1 
ATOM   5962 C  CD1 . LEU B 1 375 ? 66.144  64.285  95.597  1.00 33.69 ? 364  LEU B CD1 1 
ATOM   5963 C  CD2 . LEU B 1 375 ? 64.079  65.663  95.489  1.00 33.69 ? 364  LEU B CD2 1 
ATOM   5964 N  N   . LYS B 1 376 ? 66.535  61.725  92.983  1.00 34.27 ? 365  LYS B N   1 
ATOM   5965 C  CA  . LYS B 1 376 ? 67.786  60.993  93.116  1.00 34.27 ? 365  LYS B CA  1 
ATOM   5966 C  C   . LYS B 1 376 ? 68.942  61.971  92.991  1.00 34.27 ? 365  LYS B C   1 
ATOM   5967 O  O   . LYS B 1 376 ? 68.989  62.759  92.043  1.00 34.27 ? 365  LYS B O   1 
ATOM   5968 C  CB  . LYS B 1 376 ? 67.887  59.901  92.043  1.00 34.27 ? 365  LYS B CB  1 
ATOM   5969 C  CG  . LYS B 1 376 ? 69.206  59.148  91.999  1.00 34.27 ? 365  LYS B CG  1 
ATOM   5970 C  CD  . LYS B 1 376 ? 69.349  58.194  93.157  1.00 34.27 ? 365  LYS B CD  1 
ATOM   5971 C  CE  . LYS B 1 376 ? 70.687  57.490  93.115  1.00 34.27 ? 365  LYS B CE  1 
ATOM   5972 N  NZ  . LYS B 1 376 ? 70.799  56.585  91.948  1.00 34.27 ? 365  LYS B NZ  1 
ATOM   5973 N  N   . ILE B 1 377 ? 69.866  61.921  93.943  1.00 31.53 ? 366  ILE B N   1 
ATOM   5974 C  CA  . ILE B 1 377 ? 71.101  62.693  93.888  1.00 31.53 ? 366  ILE B CA  1 
ATOM   5975 C  C   . ILE B 1 377 ? 72.199  61.733  93.450  1.00 31.53 ? 366  ILE B C   1 
ATOM   5976 O  O   . ILE B 1 377 ? 72.612  60.860  94.217  1.00 31.53 ? 366  ILE B O   1 
ATOM   5977 C  CB  . ILE B 1 377 ? 71.432  63.340  95.239  1.00 31.53 ? 366  ILE B CB  1 
ATOM   5978 C  CG1 . ILE B 1 377 ? 70.276  64.210  95.733  1.00 31.53 ? 366  ILE B CG1 1 
ATOM   5979 C  CG2 . ILE B 1 377 ? 72.679  64.187  95.123  1.00 31.53 ? 366  ILE B CG2 1 
ATOM   5980 C  CD1 . ILE B 1 377 ? 70.109  65.505  94.982  1.00 31.53 ? 366  ILE B CD1 1 
ATOM   5981 N  N   . ASP B 1 378 ? 72.674  61.883  92.217  1.00 32.76 ? 367  ASP B N   1 
ATOM   5982 C  CA  . ASP B 1 378 ? 73.667  60.962  91.694  1.00 32.76 ? 367  ASP B CA  1 
ATOM   5983 C  C   . ASP B 1 378 ? 74.946  61.029  92.531  1.00 32.76 ? 367  ASP B C   1 
ATOM   5984 O  O   . ASP B 1 378 ? 75.126  61.905  93.377  1.00 32.76 ? 367  ASP B O   1 
ATOM   5985 C  CB  . ASP B 1 378 ? 73.958  61.270  90.226  1.00 32.76 ? 367  ASP B CB  1 
ATOM   5986 C  CG  . ASP B 1 378 ? 74.819  62.496  90.045  1.00 32.76 ? 367  ASP B CG  1 
ATOM   5987 O  OD1 . ASP B 1 378 ? 74.911  63.304  90.986  1.00 32.76 ? 367  ASP B OD1 1 
ATOM   5988 O  OD2 . ASP B 1 378 ? 75.408  62.656  88.957  1.00 32.76 ? 367  ASP B OD2 1 
ATOM   5989 N  N   . SER B 1 379 ? 75.846  60.078  92.282  1.00 36.16 ? 368  SER B N   1 
ATOM   5990 C  CA  . SER B 1 379 ? 77.039  59.943  93.106  1.00 36.16 ? 368  SER B CA  1 
ATOM   5991 C  C   . SER B 1 379 ? 78.007  61.104  92.952  1.00 36.16 ? 368  SER B C   1 
ATOM   5992 O  O   . SER B 1 379 ? 78.942  61.212  93.750  1.00 36.16 ? 368  SER B O   1 
ATOM   5993 C  CB  . SER B 1 379 ? 77.757  58.638  92.778  1.00 36.16 ? 368  SER B CB  1 
ATOM   5994 O  OG  . SER B 1 379 ? 78.257  58.655  91.457  1.00 36.16 ? 368  SER B OG  1 
ATOM   5995 N  N   . SER B 1 380 ? 77.824  61.958  91.950  1.00 32.60 ? 369  SER B N   1 
ATOM   5996 C  CA  . SER B 1 380 ? 78.675  63.124  91.777  1.00 32.60 ? 369  SER B CA  1 
ATOM   5997 C  C   . SER B 1 380 ? 78.183  64.341  92.543  1.00 32.60 ? 369  SER B C   1 
ATOM   5998 O  O   . SER B 1 380 ? 78.911  65.333  92.620  1.00 32.60 ? 369  SER B O   1 
ATOM   5999 C  CB  . SER B 1 380 ? 78.783  63.483  90.296  1.00 32.60 ? 369  SER B CB  1 
ATOM   6000 O  OG  . SER B 1 380 ? 79.582  64.637  90.118  1.00 32.60 ? 369  SER B OG  1 
ATOM   6001 N  N   . GLY B 1 381 ? 76.978  64.296  93.103  1.00 29.58 ? 370  GLY B N   1 
ATOM   6002 C  CA  . GLY B 1 381 ? 76.435  65.391  93.882  1.00 29.58 ? 370  GLY B CA  1 
ATOM   6003 C  C   . GLY B 1 381 ? 75.303  66.141  93.221  1.00 29.58 ? 370  GLY B C   1 
ATOM   6004 O  O   . GLY B 1 381 ? 74.623  66.914  93.902  1.00 29.58 ? 370  GLY B O   1 
ATOM   6005 N  N   . ASP B 1 382 ? 75.075  65.946  91.929  1.00 30.20 ? 371  ASP B N   1 
ATOM   6006 C  CA  . ASP B 1 382 ? 74.000  66.619  91.220  1.00 30.20 ? 371  ASP B CA  1 
ATOM   6007 C  C   . ASP B 1 382 ? 72.745  65.755  91.215  1.00 30.20 ? 371  ASP B C   1 
ATOM   6008 O  O   . ASP B 1 382 ? 72.790  64.550  91.459  1.00 30.20 ? 371  ASP B O   1 
ATOM   6009 C  CB  . ASP B 1 382 ? 74.422  66.936  89.789  1.00 30.20 ? 371  ASP B CB  1 
ATOM   6010 C  CG  . ASP B 1 382 ? 75.733  67.680  89.726  1.00 30.20 ? 371  ASP B CG  1 
ATOM   6011 O  OD1 . ASP B 1 382 ? 76.171  68.204  90.769  1.00 30.20 ? 371  ASP B OD1 1 
ATOM   6012 O  OD2 . ASP B 1 382 ? 76.331  67.739  88.634  1.00 30.20 ? 371  ASP B OD2 1 
ATOM   6013 N  N   . ARG B 1 383 ? 71.614  66.390  90.938  1.00 31.26 ? 372  ARG B N   1 
ATOM   6014 C  CA  . ARG B 1 383 ? 70.337  65.697  90.922  1.00 31.26 ? 372  ARG B CA  1 
ATOM   6015 C  C   . ARG B 1 383 ? 70.005  65.223  89.515  1.00 31.26 ? 372  ARG B C   1 
ATOM   6016 O  O   . ARG B 1 383 ? 70.368  65.859  88.524  1.00 31.26 ? 372  ARG B O   1 
ATOM   6017 C  CB  . ARG B 1 383 ? 69.218  66.601  91.430  1.00 31.26 ? 372  ARG B CB  1 
ATOM   6018 C  CG  . ARG B 1 383 ? 67.999  65.833  91.876  1.00 31.26 ? 372  ARG B CG  1 
ATOM   6019 C  CD  . ARG B 1 383 ? 66.819  66.732  92.106  1.00 31.26 ? 372  ARG B CD  1 
ATOM   6020 N  NE  . ARG B 1 383 ? 66.252  67.191  90.849  1.00 31.26 ? 372  ARG B NE  1 
ATOM   6021 C  CZ  . ARG B 1 383 ? 65.132  67.894  90.750  1.00 31.26 ? 372  ARG B CZ  1 
ATOM   6022 N  NH1 . ARG B 1 383 ? 64.447  68.213  91.839  1.00 31.26 ? 372  ARG B NH1 1 
ATOM   6023 N  NH2 . ARG B 1 383 ? 64.694  68.273  89.559  1.00 31.26 ? 372  ARG B NH2 1 
ATOM   6024 N  N   . GLU B 1 384 ? 69.298  64.100  89.438  1.00 32.80 ? 373  GLU B N   1 
ATOM   6025 C  CA  . GLU B 1 384 ? 68.907  63.511  88.164  1.00 32.80 ? 373  GLU B CA  1 
ATOM   6026 C  C   . GLU B 1 384 ? 67.609  64.155  87.695  1.00 32.80 ? 373  GLU B C   1 
ATOM   6027 O  O   . GLU B 1 384 ? 66.615  63.947  88.329  1.00 32.80 ? 373  GLU B O   1 
ATOM   6028 C  CB  . GLU B 1 384 ? 68.455  62.074  88.341  1.00 30.00 ? 373  GLU B CB  1 
ATOM   6029 C  CG  . GLU B 1 384 ? 69.498  61.110  88.799  1.00 30.00 ? 373  GLU B CG  1 
ATOM   6030 C  CD  . GLU B 1 384 ? 70.664  61.070  87.863  1.00 30.00 ? 373  GLU B CD  1 
ATOM   6031 O  OE1 . GLU B 1 384 ? 70.427  61.115  86.694  1.00 30.00 ? 373  GLU B OE1 1 
ATOM   6032 O  OE2 . GLU B 1 384 ? 71.781  61.017  88.315  1.00 30.00 ? 373  GLU B OE2 1 
ATOM   6033 N  N   . THR B 1 385 ? 67.674  64.860  86.572  1.00 32.49 ? 374  THR B N   1 
ATOM   6034 C  CA  . THR B 1 385 ? 66.574  65.686  86.099  1.00 32.49 ? 374  THR B CA  1 
ATOM   6035 C  C   . THR B 1 385 ? 65.705  64.927  85.106  1.00 32.49 ? 374  THR B C   1 
ATOM   6036 O  O   . THR B 1 385 ? 66.187  64.086  84.345  1.00 32.49 ? 374  THR B O   1 
ATOM   6037 C  CB  . THR B 1 385 ? 67.113  66.958  85.443  1.00 32.49 ? 374  THR B CB  1 
ATOM   6038 O  OG1 . THR B 1 385 ? 68.062  67.583  86.313  1.00 32.49 ? 374  THR B OG1 1 
ATOM   6039 C  CG2 . THR B 1 385 ? 65.989  67.929  85.154  1.00 32.49 ? 374  THR B CG2 1 
ATOM   6040 N  N   . ASP B 1 386 ? 64.410  65.235  85.126  1.00 34.81 ? 375  ASP B N   1 
ATOM   6041 C  CA  . ASP B 1 386 ? 63.438  64.677  84.198  1.00 34.81 ? 375  ASP B CA  1 
ATOM   6042 C  C   . ASP B 1 386 ? 63.055  65.731  83.171  1.00 34.81 ? 375  ASP B C   1 
ATOM   6043 O  O   . ASP B 1 386 ? 63.077  66.929  83.457  1.00 34.81 ? 375  ASP B O   1 
ATOM   6044 C  CB  . ASP B 1 386 ? 62.186  64.196  84.932  1.00 34.81 ? 375  ASP B CB  1 
ATOM   6045 C  CG  . ASP B 1 386 ? 62.481  63.104  85.933  1.00 34.81 ? 375  ASP B CG  1 
ATOM   6046 O  OD1 . ASP B 1 386 ? 61.595  62.789  86.752  1.00 34.81 ? 375  ASP B OD1 1 
ATOM   6047 O  OD2 . ASP B 1 386 ? 63.602  62.560  85.905  1.00 34.81 ? 375  ASP B OD2 1 
ATOM   6048 N  N   . PHE B 1 387 ? 62.699  65.284  81.969  1.00 34.59 ? 376  PHE B N   1 
ATOM   6049 C  CA  . PHE B 1 387 ? 62.427  66.210  80.873  1.00 34.59 ? 376  PHE B CA  1 
ATOM   6050 C  C   . PHE B 1 387 ? 61.140  65.826  80.158  1.00 34.59 ? 376  PHE B C   1 
ATOM   6051 O  O   . PHE B 1 387 ? 60.619  64.723  80.319  1.00 34.59 ? 376  PHE B O   1 
ATOM   6052 C  CB  . PHE B 1 387 ? 63.588  66.248  79.873  1.00 34.59 ? 376  PHE B CB  1 
ATOM   6053 C  CG  . PHE B 1 387 ? 64.767  67.050  80.339  1.00 34.59 ? 376  PHE B CG  1 
ATOM   6054 C  CD1 . PHE B 1 387 ? 65.806  66.446  81.016  1.00 34.59 ? 376  PHE B CD1 1 
ATOM   6055 C  CD2 . PHE B 1 387 ? 64.838  68.405  80.097  1.00 34.59 ? 376  PHE B CD2 1 
ATOM   6056 C  CE1 . PHE B 1 387 ? 66.886  67.178  81.440  1.00 34.59 ? 376  PHE B CE1 1 
ATOM   6057 C  CE2 . PHE B 1 387 ? 65.918  69.138  80.522  1.00 34.59 ? 376  PHE B CE2 1 
ATOM   6058 C  CZ  . PHE B 1 387 ? 66.941  68.524  81.195  1.00 34.59 ? 376  PHE B CZ  1 
ATOM   6059 N  N   . SER B 1 388 ? 60.621  66.757  79.358  1.00 37.73 ? 377  SER B N   1 
ATOM   6060 C  CA  . SER B 1 388 ? 59.417  66.532  78.573  1.00 37.73 ? 377  SER B CA  1 
ATOM   6061 C  C   . SER B 1 388 ? 59.626  67.005  77.145  1.00 37.73 ? 377  SER B C   1 
ATOM   6062 O  O   . SER B 1 388 ? 60.254  68.043  76.905  1.00 37.73 ? 377  SER B O   1 
ATOM   6063 C  CB  . SER B 1 388 ? 58.209  67.253  79.166  1.00 37.73 ? 377  SER B CB  1 
ATOM   6064 O  OG  . SER B 1 388 ? 57.690  66.553  80.278  1.00 37.73 ? 377  SER B OG  1 
ATOM   6065 N  N   . LEU B 1 389 ? 59.087  66.232  76.205  1.00 42.69 ? 378  LEU B N   1 
ATOM   6066 C  CA  . LEU B 1 389 ? 59.097  66.558  74.787  1.00 42.69 ? 378  LEU B CA  1 
ATOM   6067 C  C   . LEU B 1 389 ? 57.666  66.814  74.334  1.00 42.69 ? 378  LEU B C   1 
ATOM   6068 O  O   . LEU B 1 389 ? 56.794  65.948  74.504  1.00 42.69 ? 378  LEU B O   1 
ATOM   6069 C  CB  . LEU B 1 389 ? 59.725  65.435  73.964  1.00 42.69 ? 378  LEU B CB  1 
ATOM   6070 C  CG  . LEU B 1 389 ? 60.120  65.829  72.540  1.00 42.69 ? 378  LEU B CG  1 
ATOM   6071 C  CD1 . LEU B 1 389 ? 61.473  66.503  72.531  1.00 42.69 ? 378  LEU B CD1 1 
ATOM   6072 C  CD2 . LEU B 1 389 ? 60.117  64.621  71.624  1.00 42.69 ? 378  LEU B CD2 1 
ATOM   6073 N  N   . TRP B 1 390 ? 57.452  67.995  73.748  1.00 43.51 ? 379  TRP B N   1 
ATOM   6074 C  CA  . TRP B 1 390 ? 56.166  68.473  73.264  1.00 43.51 ? 379  TRP B CA  1 
ATOM   6075 C  C   . TRP B 1 390 ? 56.159  68.436  71.744  1.00 43.51 ? 379  TRP B C   1 
ATOM   6076 O  O   . TRP B 1 390 ? 57.107  68.917  71.107  1.00 43.51 ? 379  TRP B O   1 
ATOM   6077 C  CB  . TRP B 1 390 ? 55.905  69.915  73.704  1.00 43.51 ? 379  TRP B CB  1 
ATOM   6078 C  CG  . TRP B 1 390 ? 55.932  70.178  75.169  1.00 43.51 ? 379  TRP B CG  1 
ATOM   6079 C  CD1 . TRP B 1 390 ? 56.992  70.042  76.007  1.00 43.51 ? 379  TRP B CD1 1 
ATOM   6080 C  CD2 . TRP B 1 390 ? 54.850  70.669  75.966  1.00 43.51 ? 379  TRP B CD2 1 
ATOM   6081 N  NE1 . TRP B 1 390 ? 56.636  70.400  77.282  1.00 43.51 ? 379  TRP B NE1 1 
ATOM   6082 C  CE2 . TRP B 1 390 ? 55.325  70.792  77.282  1.00 43.51 ? 379  TRP B CE2 1 
ATOM   6083 C  CE3 . TRP B 1 390 ? 53.524  71.011  75.693  1.00 43.51 ? 379  TRP B CE3 1 
ATOM   6084 C  CZ2 . TRP B 1 390 ? 54.521  71.238  78.323  1.00 43.51 ? 379  TRP B CZ2 1 
ATOM   6085 C  CZ3 . TRP B 1 390 ? 52.728  71.452  76.728  1.00 43.51 ? 379  TRP B CZ3 1 
ATOM   6086 C  CH2 . TRP B 1 390 ? 53.228  71.561  78.026  1.00 43.51 ? 379  TRP B CH2 1 
ATOM   6087 N  N   . ASP B 1 391 ? 55.070  67.917  71.177  1.00 49.54 ? 380  ASP B N   1 
ATOM   6088 C  CA  . ASP B 1 391 ? 54.890  67.794  69.739  1.00 49.54 ? 380  ASP B CA  1 
ATOM   6089 C  C   . ASP B 1 391 ? 53.478  68.232  69.376  1.00 49.54 ? 380  ASP B C   1 
ATOM   6090 O  O   . ASP B 1 391 ? 52.568  68.205  70.206  1.00 49.54 ? 380  ASP B O   1 
ATOM   6091 C  CB  . ASP B 1 391 ? 55.143  66.354  69.273  1.00 49.54 ? 380  ASP B CB  1 
ATOM   6092 C  CG  . ASP B 1 391 ? 55.309  66.243  67.772  1.00 49.54 ? 380  ASP B CG  1 
ATOM   6093 O  OD1 . ASP B 1 391 ? 55.209  65.115  67.245  1.00 49.54 ? 380  ASP B OD1 1 
ATOM   6094 O  OD2 . ASP B 1 391 ? 55.535  67.281  67.117  1.00 49.54 ? 380  ASP B OD2 1 
ATOM   6095 N  N   . MET B 1 392 ? 53.301  68.630  68.119  1.00 52.72 ? 381  MET B N   1 
ATOM   6096 C  CA  . MET B 1 392 ? 52.048  69.215  67.664  1.00 52.72 ? 381  MET B CA  1 
ATOM   6097 C  C   . MET B 1 392 ? 51.044  68.137  67.260  1.00 52.72 ? 381  MET B C   1 
ATOM   6098 O  O   . MET B 1 392 ? 51.390  66.977  67.026  1.00 52.72 ? 381  MET B O   1 
ATOM   6099 C  CB  . MET B 1 392 ? 52.295  70.150  66.483  1.00 52.72 ? 381  MET B CB  1 
ATOM   6100 C  CG  . MET B 1 392 ? 51.106  71.020  66.127  1.00 52.72 ? 381  MET B CG  1 
ATOM   6101 S  SD  . MET B 1 392 ? 51.535  72.388  65.040  1.00 52.72 ? 381  MET B SD  1 
ATOM   6102 C  CE  . MET B 1 392 ? 51.802  71.515  63.508  1.00 52.72 ? 381  MET B CE  1 
ATOM   6103 N  N   . ASP B 1 393 ? 49.768  68.549  67.180  1.00 55.99 ? 382  ASP B N   1 
ATOM   6104 C  CA  . ASP B 1 393 ? 48.654  67.679  66.822  1.00 55.99 ? 382  ASP B CA  1 
ATOM   6105 C  C   . ASP B 1 393 ? 48.265  67.901  65.370  1.00 55.99 ? 382  ASP B C   1 
ATOM   6106 O  O   . ASP B 1 393 ? 47.989  69.047  64.984  1.00 55.99 ? 382  ASP B O   1 
ATOM   6107 C  CB  . ASP B 1 393 ? 47.455  67.956  67.723  1.00 55.99 ? 382  ASP B CB  1 
ATOM   6108 C  CG  . ASP B 1 393 ? 46.338  66.953  67.535  1.00 55.99 ? 382  ASP B CG  1 
ATOM   6109 O  OD1 . ASP B 1 393 ? 46.473  66.064  66.670  1.00 55.99 ? 382  ASP B OD1 1 
ATOM   6110 O  OD2 . ASP B 1 393 ? 45.325  67.050  68.257  1.00 55.99 ? 382  ASP B OD2 1 
ATOM   6111 N  N   . PRO B 1 394 ? 48.231  66.866  64.527  1.00 58.58 ? 383  PRO B N   1 
ATOM   6112 C  CA  . PRO B 1 394 ? 47.818  67.097  63.132  1.00 58.58 ? 383  PRO B CA  1 
ATOM   6113 C  C   . PRO B 1 394 ? 46.433  67.706  63.006  1.00 58.58 ? 383  PRO B C   1 
ATOM   6114 O  O   . PRO B 1 394 ? 46.200  68.520  62.104  1.00 58.58 ? 383  PRO B O   1 
ATOM   6115 C  CB  . PRO B 1 394 ? 47.882  65.695  62.506  1.00 58.58 ? 383  PRO B CB  1 
ATOM   6116 C  CG  . PRO B 1 394 ? 47.976  64.741  63.656  1.00 58.58 ? 383  PRO B CG  1 
ATOM   6117 C  CD  . PRO B 1 394 ? 48.669  65.477  64.741  1.00 58.58 ? 383  PRO B CD  1 
ATOM   6118 N  N   . GLU B 1 395 ? 45.502  67.337  63.886  1.00 58.39 ? 384  GLU B N   1 
ATOM   6119 C  CA  . GLU B 1 395 ? 44.129  67.820  63.768  1.00 58.39 ? 384  GLU B CA  1 
ATOM   6120 C  C   . GLU B 1 395 ? 43.969  69.210  64.375  1.00 58.39 ? 384  GLU B C   1 
ATOM   6121 O  O   . GLU B 1 395 ? 43.630  70.170  63.676  1.00 58.39 ? 384  GLU B O   1 
ATOM   6122 C  CB  . GLU B 1 395 ? 43.171  66.831  64.437  1.00 58.39 ? 384  GLU B CB  1 
ATOM   6123 N  N   . ASN B 1 396 ? 44.208  69.334  65.682  1.00 57.15 ? 385  ASN B N   1 
ATOM   6124 C  CA  . ASN B 1 396 ? 43.980  70.602  66.367  1.00 57.15 ? 385  ASN B CA  1 
ATOM   6125 C  C   . ASN B 1 396 ? 45.083  71.616  66.098  1.00 57.15 ? 385  ASN B C   1 
ATOM   6126 O  O   . ASN B 1 396 ? 44.809  72.820  66.039  1.00 57.15 ? 385  ASN B O   1 
ATOM   6127 C  CB  . ASN B 1 396 ? 43.851  70.367  67.872  1.00 57.15 ? 385  ASN B CB  1 
ATOM   6128 N  N   . GLY B 1 397 ? 46.323  71.163  65.934  1.00 55.26 ? 386  GLY B N   1 
ATOM   6129 C  CA  . GLY B 1 397 ? 47.439  72.072  65.787  1.00 55.26 ? 386  GLY B CA  1 
ATOM   6130 C  C   . GLY B 1 397 ? 47.960  72.644  67.085  1.00 55.26 ? 386  GLY B C   1 
ATOM   6131 O  O   . GLY B 1 397 ? 48.717  73.621  67.053  1.00 55.26 ? 386  GLY B O   1 
ATOM   6132 N  N   . ALA B 1 398 ? 47.579  72.072  68.221  1.00 53.03 ? 387  ALA B N   1 
ATOM   6133 C  CA  . ALA B 1 398 ? 48.013  72.534  69.529  1.00 53.03 ? 387  ALA B CA  1 
ATOM   6134 C  C   . ALA B 1 398 ? 49.095  71.616  70.078  1.00 53.03 ? 387  ALA B C   1 
ATOM   6135 O  O   . ALA B 1 398 ? 49.075  70.403  69.859  1.00 53.03 ? 387  ALA B O   1 
ATOM   6136 C  CB  . ALA B 1 398 ? 46.837  72.581  70.504  1.00 53.03 ? 387  ALA B CB  1 
ATOM   6137 N  N   . PHE B 1 399 ? 50.042  72.210  70.797  1.00 49.03 ? 388  PHE B N   1 
ATOM   6138 C  CA  . PHE B 1 399 ? 51.138  71.457  71.383  1.00 49.03 ? 388  PHE B CA  1 
ATOM   6139 C  C   . PHE B 1 399 ? 50.715  70.832  72.706  1.00 49.03 ? 388  PHE B C   1 
ATOM   6140 O  O   . PHE B 1 399 ? 49.878  71.373  73.432  1.00 49.03 ? 388  PHE B O   1 
ATOM   6141 C  CB  . PHE B 1 399 ? 52.344  72.366  71.611  1.00 49.03 ? 388  PHE B CB  1 
ATOM   6142 C  CG  . PHE B 1 399 ? 53.233  72.503  70.417  1.00 49.03 ? 388  PHE B CG  1 
ATOM   6143 C  CD1 . PHE B 1 399 ? 52.706  72.814  69.180  1.00 49.03 ? 388  PHE B CD1 1 
ATOM   6144 C  CD2 . PHE B 1 399 ? 54.596  72.318  70.528  1.00 49.03 ? 388  PHE B CD2 1 
ATOM   6145 C  CE1 . PHE B 1 399 ? 53.522  72.943  68.081  1.00 49.03 ? 388  PHE B CE1 1 
ATOM   6146 C  CE2 . PHE B 1 399 ? 55.414  72.443  69.431  1.00 49.03 ? 388  PHE B CE2 1 
ATOM   6147 C  CZ  . PHE B 1 399 ? 54.876  72.754  68.206  1.00 49.03 ? 388  PHE B CZ  1 
ATOM   6148 N  N   . ARG B 1 400 ? 51.301  69.678  73.015  1.00 51.21 ? 389  ARG B N   1 
ATOM   6149 C  CA  . ARG B 1 400 ? 51.119  69.079  74.330  1.00 51.21 ? 389  ARG B CA  1 
ATOM   6150 C  C   . ARG B 1 400 ? 52.271  68.113  74.550  1.00 51.21 ? 389  ARG B C   1 
ATOM   6151 O  O   . ARG B 1 400 ? 52.966  67.729  73.606  1.00 51.21 ? 389  ARG B O   1 
ATOM   6152 C  CB  . ARG B 1 400 ? 49.773  68.355  74.446  1.00 51.21 ? 389  ARG B CB  1 
ATOM   6153 C  CG  . ARG B 1 400 ? 49.697  67.018  73.729  1.00 51.21 ? 389  ARG B CG  1 
ATOM   6154 C  CD  . ARG B 1 400 ? 49.503  67.136  72.248  1.00 51.21 ? 389  ARG B CD  1 
ATOM   6155 N  NE  . ARG B 1 400 ? 49.191  65.833  71.679  1.00 51.21 ? 389  ARG B NE  1 
ATOM   6156 C  CZ  . ARG B 1 400 ? 49.176  65.573  70.379  1.00 51.21 ? 389  ARG B CZ  1 
ATOM   6157 N  NH1 . ARG B 1 400 ? 48.869  64.359  69.945  1.00 51.21 ? 389  ARG B NH1 1 
ATOM   6158 N  NH2 . ARG B 1 400 ? 49.527  66.510  69.516  1.00 51.21 ? 389  ARG B NH2 1 
ATOM   6159 N  N   . VAL B 1 401 ? 52.461  67.712  75.804  1.00 46.45 ? 390  VAL B N   1 
ATOM   6160 C  CA  . VAL B 1 401 ? 53.541  66.789  76.125  1.00 46.45 ? 390  VAL B CA  1 
ATOM   6161 C  C   . VAL B 1 401 ? 53.248  65.437  75.494  1.00 46.45 ? 390  VAL B C   1 
ATOM   6162 O  O   . VAL B 1 401 ? 52.165  64.869  75.680  1.00 46.45 ? 390  VAL B O   1 
ATOM   6163 C  CB  . VAL B 1 401 ? 53.709  66.659  77.644  1.00 46.45 ? 390  VAL B CB  1 
ATOM   6164 C  CG1 . VAL B 1 401 ? 54.611  65.497  77.969  1.00 46.45 ? 390  VAL B CG1 1 
ATOM   6165 C  CG2 . VAL B 1 401 ? 54.256  67.930  78.218  1.00 46.45 ? 390  VAL B CG2 1 
ATOM   6166 N  N   . VAL B 1 402 ? 54.217  64.909  74.749  1.00 48.99 ? 391  VAL B N   1 
ATOM   6167 C  CA  . VAL B 1 402 ? 54.097  63.601  74.128  1.00 48.99 ? 391  VAL B CA  1 
ATOM   6168 C  C   . VAL B 1 402 ? 55.058  62.594  74.745  1.00 48.99 ? 391  VAL B C   1 
ATOM   6169 O  O   . VAL B 1 402 ? 54.721  61.415  74.863  1.00 48.99 ? 391  VAL B O   1 
ATOM   6170 C  CB  . VAL B 1 402 ? 54.295  63.685  72.599  1.00 48.99 ? 391  VAL B CB  1 
ATOM   6171 C  CG1 . VAL B 1 402 ? 55.719  64.069  72.249  1.00 48.99 ? 391  VAL B CG1 1 
ATOM   6172 C  CG2 . VAL B 1 402 ? 53.931  62.366  71.953  1.00 48.99 ? 391  VAL B CG2 1 
ATOM   6173 N  N   . LEU B 1 403 ? 56.256  63.027  75.148  1.00 46.81 ? 392  LEU B N   1 
ATOM   6174 C  CA  . LEU B 1 403 ? 57.228  62.108  75.734  1.00 46.81 ? 392  LEU B CA  1 
ATOM   6175 C  C   . LEU B 1 403 ? 57.722  62.632  77.074  1.00 46.81 ? 392  LEU B C   1 
ATOM   6176 O  O   . LEU B 1 403 ? 57.870  63.839  77.266  1.00 46.81 ? 392  LEU B O   1 
ATOM   6177 C  CB  . LEU B 1 403 ? 58.430  61.887  74.803  1.00 46.81 ? 392  LEU B CB  1 
ATOM   6178 C  CG  . LEU B 1 403 ? 58.428  60.654  73.897  1.00 46.81 ? 392  LEU B CG  1 
ATOM   6179 C  CD1 . LEU B 1 403 ? 59.704  60.613  73.083  1.00 46.81 ? 392  LEU B CD1 1 
ATOM   6180 C  CD2 . LEU B 1 403 ? 58.280  59.380  74.699  1.00 46.81 ? 392  LEU B CD2 1 
ATOM   6181 N  N   . ASN B 1 404 ? 57.994  61.707  77.996  1.00 44.00 ? 393  ASN B N   1 
ATOM   6182 C  CA  . ASN B 1 404 ? 58.536  62.035  79.309  1.00 44.00 ? 393  ASN B CA  1 
ATOM   6183 C  C   . ASN B 1 404 ? 59.813  61.243  79.538  1.00 44.00 ? 393  ASN B C   1 
ATOM   6184 O  O   . ASN B 1 404 ? 59.908  60.085  79.133  1.00 44.00 ? 393  ASN B O   1 
ATOM   6185 C  CB  . ASN B 1 404 ? 57.530  61.725  80.418  1.00 44.00 ? 393  ASN B CB  1 
ATOM   6186 C  CG  . ASN B 1 404 ? 56.480  62.799  80.568  1.00 44.00 ? 393  ASN B CG  1 
ATOM   6187 O  OD1 . ASN B 1 404 ? 56.664  63.927  80.121  1.00 44.00 ? 393  ASN B OD1 1 
ATOM   6188 N  ND2 . ASN B 1 404 ? 55.368  62.453  81.197  1.00 44.00 ? 393  ASN B ND2 1 
ATOM   6189 N  N   . TYR B 1 405 ? 60.793  61.862  80.191  1.00 39.75 ? 394  TYR B N   1 
ATOM   6190 C  CA  . TYR B 1 405 ? 62.102  61.258  80.406  1.00 39.75 ? 394  TYR B CA  1 
ATOM   6191 C  C   . TYR B 1 405 ? 62.412  61.242  81.894  1.00 39.75 ? 394  TYR B C   1 
ATOM   6192 O  O   . TYR B 1 405 ? 62.506  62.308  82.519  1.00 39.75 ? 394  TYR B O   1 
ATOM   6193 C  CB  . TYR B 1 405 ? 63.184  62.027  79.650  1.00 39.75 ? 394  TYR B CB  1 
ATOM   6194 C  CG  . TYR B 1 405 ? 64.584  61.530  79.909  1.00 39.75 ? 394  TYR B CG  1 
ATOM   6195 C  CD1 . TYR B 1 405 ? 65.059  60.386  79.288  1.00 39.75 ? 394  TYR B CD1 1 
ATOM   6196 C  CD2 . TYR B 1 405 ? 65.430  62.204  80.775  1.00 39.75 ? 394  TYR B CD2 1 
ATOM   6197 C  CE1 . TYR B 1 405 ? 66.336  59.929  79.520  1.00 39.75 ? 394  TYR B CE1 1 
ATOM   6198 C  CE2 . TYR B 1 405 ? 66.707  61.753  81.014  1.00 39.75 ? 394  TYR B CE2 1 
ATOM   6199 C  CZ  . TYR B 1 405 ? 67.156  60.615  80.382  1.00 39.75 ? 394  TYR B CZ  1 
ATOM   6200 O  OH  . TYR B 1 405 ? 68.431  60.160  80.617  1.00 39.75 ? 394  TYR B OH  1 
ATOM   6201 N  N   . ASN B 1 406 ? 62.585  60.032  82.448  1.00 39.57 ? 395  ASN B N   1 
ATOM   6202 C  CA  . ASN B 1 406 ? 62.962  59.823  83.849  1.00 39.57 ? 395  ASN B CA  1 
ATOM   6203 C  C   . ASN B 1 406 ? 64.477  59.659  83.870  1.00 39.57 ? 395  ASN B C   1 
ATOM   6204 O  O   . ASN B 1 406 ? 65.018  58.690  83.324  1.00 39.57 ? 395  ASN B O   1 
ATOM   6205 C  CB  . ASN B 1 406 ? 62.255  58.608  84.450  1.00 39.57 ? 395  ASN B CB  1 
ATOM   6206 C  CG  . ASN B 1 406 ? 62.617  58.366  85.927  1.00 39.57 ? 395  ASN B CG  1 
ATOM   6207 O  OD1 . ASN B 1 406 ? 63.757  58.551  86.339  1.00 39.57 ? 395  ASN B OD1 1 
ATOM   6208 N  ND2 . ASN B 1 406 ? 61.630  57.927  86.715  1.00 39.57 ? 395  ASN B ND2 1 
ATOM   6209 N  N   . GLY B 1 407 ? 65.158  60.636  84.473  1.00 36.19 ? 396  GLY B N   1 
ATOM   6210 C  CA  . GLY B 1 407 ? 66.607  60.640  84.520  1.00 36.19 ? 396  GLY B CA  1 
ATOM   6211 C  C   . GLY B 1 407 ? 67.201  59.685  85.529  1.00 36.19 ? 396  GLY B C   1 
ATOM   6212 O  O   . GLY B 1 407 ? 68.381  59.342  85.416  1.00 36.19 ? 396  GLY B O   1 
ATOM   6213 N  N   . THR B 1 408 ? 66.421  59.254  86.520  1.00 37.97 ? 397  THR B N   1 
ATOM   6214 C  CA  . THR B 1 408 ? 66.914  58.258  87.466  1.00 37.97 ? 397  THR B CA  1 
ATOM   6215 C  C   . THR B 1 408 ? 67.081  56.911  86.781  1.00 37.97 ? 397  THR B C   1 
ATOM   6216 O  O   . THR B 1 408 ? 68.181  56.350  86.738  1.00 37.97 ? 397  THR B O   1 
ATOM   6217 C  CB  . THR B 1 408 ? 65.961  58.139  88.655  1.00 37.97 ? 397  THR B CB  1 
ATOM   6218 O  OG1 . THR B 1 408 ? 66.034  59.325  89.453  1.00 37.97 ? 397  THR B OG1 1 
ATOM   6219 C  CG2 . THR B 1 408 ? 66.317  56.934  89.510  1.00 37.97 ? 397  THR B CG2 1 
ATOM   6220 N  N   . SER B 1 409 ? 65.990  56.375  86.237  1.00 41.17 ? 398  SER B N   1 
ATOM   6221 C  CA  . SER B 1 409 ? 66.045  55.151  85.454  1.00 41.17 ? 398  SER B CA  1 
ATOM   6222 C  C   . SER B 1 409 ? 66.540  55.388  84.037  1.00 41.17 ? 398  SER B C   1 
ATOM   6223 O  O   . SER B 1 409 ? 66.880  54.422  83.348  1.00 41.17 ? 398  SER B O   1 
ATOM   6224 C  CB  . SER B 1 409 ? 64.664  54.500  85.406  1.00 41.17 ? 398  SER B CB  1 
ATOM   6225 O  OG  . SER B 1 409 ? 63.848  55.126  84.435  1.00 41.17 ? 398  SER B OG  1 
ATOM   6226 N  N   . GLN B 1 410 ? 66.593  56.642  83.591  1.00 42.79 ? 399  GLN B N   1 
ATOM   6227 C  CA  . GLN B 1 410 ? 67.121  56.994  82.277  1.00 42.79 ? 399  GLN B CA  1 
ATOM   6228 C  C   . GLN B 1 410 ? 66.307  56.342  81.161  1.00 42.79 ? 399  GLN B C   1 
ATOM   6229 O  O   . GLN B 1 410 ? 66.816  55.537  80.381  1.00 42.79 ? 399  GLN B O   1 
ATOM   6230 C  CB  . GLN B 1 410 ? 68.597  56.600  82.162  1.00 42.79 ? 399  GLN B CB  1 
ATOM   6231 C  CG  . GLN B 1 410 ? 69.539  57.455  82.971  1.00 42.79 ? 399  GLN B CG  1 
ATOM   6232 C  CD  . GLN B 1 410 ? 70.946  57.419  82.424  1.00 42.79 ? 399  GLN B CD  1 
ATOM   6233 O  OE1 . GLN B 1 410 ? 71.475  56.353  82.117  1.00 42.79 ? 399  GLN B OE1 1 
ATOM   6234 N  NE2 . GLN B 1 410 ? 71.561  58.586  82.292  1.00 42.79 ? 399  GLN B NE2 1 
ATOM   6235 N  N   . GLU B 1 411 ? 65.027  56.703  81.080  1.00 46.48 ? 400  GLU B N   1 
ATOM   6236 C  CA  . GLU B 1 411 ? 64.219  56.133  80.009  1.00 46.48 ? 400  GLU B CA  1 
ATOM   6237 C  C   . GLU B 1 411 ? 63.101  57.079  79.597  1.00 46.48 ? 400  GLU B C   1 
ATOM   6238 O  O   . GLU B 1 411 ? 62.687  57.963  80.352  1.00 46.48 ? 400  GLU B O   1 
ATOM   6239 C  CB  . GLU B 1 411 ? 63.640  54.769  80.407  1.00 46.48 ? 400  GLU B CB  1 
ATOM   6240 C  CG  . GLU B 1 411 ? 62.508  54.816  81.408  1.00 46.48 ? 400  GLU B CG  1 
ATOM   6241 C  CD  . GLU B 1 411 ? 61.924  53.444  81.665  1.00 46.48 ? 400  GLU B CD  1 
ATOM   6242 O  OE1 . GLU B 1 411 ? 60.804  53.361  82.209  1.00 46.48 ? 400  GLU B OE1 1 
ATOM   6243 O  OE2 . GLU B 1 411 ? 62.589  52.445  81.317  1.00 46.48 ? 400  GLU B OE2 1 
ATOM   6244 N  N   . LEU B 1 412 ? 62.614  56.856  78.376  1.00 46.06 ? 401  LEU B N   1 
ATOM   6245 C  CA  . LEU B 1 412 ? 61.549  57.638  77.765  1.00 46.06 ? 401  LEU B CA  1 
ATOM   6246 C  C   . LEU B 1 412 ? 60.241  56.858  77.801  1.00 46.06 ? 401  LEU B C   1 
ATOM   6247 O  O   . LEU B 1 412 ? 60.229  55.637  77.630  1.00 46.06 ? 401  LEU B O   1 
ATOM   6248 C  CB  . LEU B 1 412 ? 61.892  57.990  76.317  1.00 46.06 ? 401  LEU B CB  1 
ATOM   6249 C  CG  . LEU B 1 412 ? 63.142  58.837  76.088  1.00 46.06 ? 401  LEU B CG  1 
ATOM   6250 C  CD1 . LEU B 1 412 ? 63.832  58.433  74.804  1.00 46.06 ? 401  LEU B CD1 1 
ATOM   6251 C  CD2 . LEU B 1 412 ? 62.789  60.304  76.047  1.00 46.06 ? 401  LEU B CD2 1 
ATOM   6252 N  N   . VAL B 1 413 ? 59.141  57.574  78.012  1.00 47.05 ? 402  VAL B N   1 
ATOM   6253 C  CA  . VAL B 1 413 ? 57.823  56.973  78.173  1.00 47.05 ? 402  VAL B CA  1 
ATOM   6254 C  C   . VAL B 1 413 ? 56.797  57.816  77.428  1.00 47.05 ? 402  VAL B C   1 
ATOM   6255 O  O   . VAL B 1 413 ? 56.828  59.051  77.488  1.00 47.05 ? 402  VAL B O   1 
ATOM   6256 C  CB  . VAL B 1 413 ? 57.441  56.851  79.661  1.00 47.05 ? 402  VAL B CB  1 
ATOM   6257 C  CG1 . VAL B 1 413 ? 56.154  56.069  79.814  1.00 47.05 ? 402  VAL B CG1 1 
ATOM   6258 C  CG2 . VAL B 1 413 ? 58.565  56.205  80.447  1.00 47.05 ? 402  VAL B CG2 1 
ATOM   6259 N  N   . ALA B 1 414 ? 55.892  57.142  76.721  1.00 51.15 ? 403  ALA B N   1 
ATOM   6260 C  CA  . ALA B 1 414 ? 54.738  57.797  76.126  1.00 51.15 ? 403  ALA B CA  1 
ATOM   6261 C  C   . ALA B 1 414 ? 53.688  58.063  77.196  1.00 51.15 ? 403  ALA B C   1 
ATOM   6262 O  O   . ALA B 1 414 ? 53.550  57.307  78.160  1.00 51.15 ? 403  ALA B O   1 
ATOM   6263 C  CB  . ALA B 1 414 ? 54.146  56.939  75.010  1.00 51.15 ? 403  ALA B CB  1 
ATOM   6264 N  N   . VAL B 1 415 ? 52.932  59.145  77.014  1.00 53.00 ? 404  VAL B N   1 
ATOM   6265 C  CA  . VAL B 1 415 ? 52.129  59.685  78.105  1.00 53.00 ? 404  VAL B CA  1 
ATOM   6266 C  C   . VAL B 1 415 ? 50.726  59.095  78.129  1.00 53.00 ? 404  VAL B C   1 
ATOM   6267 O  O   . VAL B 1 415 ? 50.351  58.408  79.087  1.00 53.00 ? 404  VAL B O   1 
ATOM   6268 C  CB  . VAL B 1 415 ? 52.068  61.219  78.014  1.00 53.00 ? 404  VAL B CB  1 
ATOM   6269 C  CG1 . VAL B 1 415 ? 51.132  61.777  79.075  1.00 53.00 ? 404  VAL B CG1 1 
ATOM   6270 C  CG2 . VAL B 1 415 ? 53.459  61.798  78.168  1.00 53.00 ? 404  VAL B CG2 1 
ATOM   6271 N  N   . SER B 1 416 ? 49.940  59.353  77.089  1.00 56.57 ? 405  SER B N   1 
ATOM   6272 C  CA  . SER B 1 416 ? 48.522  59.001  77.071  1.00 56.57 ? 405  SER B CA  1 
ATOM   6273 C  C   . SER B 1 416 ? 48.153  58.343  75.752  1.00 56.57 ? 405  SER B C   1 
ATOM   6274 O  O   . SER B 1 416 ? 47.156  58.681  75.112  1.00 56.57 ? 405  SER B O   1 
ATOM   6275 C  CB  . SER B 1 416 ? 47.657  60.234  77.319  1.00 56.57 ? 405  SER B CB  1 
ATOM   6276 N  N   . GLY B 1 417 ? 48.965  57.382  75.325  1.00 59.41 ? 406  GLY B N   1 
ATOM   6277 C  CA  . GLY B 1 417 ? 48.713  56.726  74.053  1.00 59.41 ? 406  GLY B CA  1 
ATOM   6278 C  C   . GLY B 1 417 ? 48.774  57.677  72.879  1.00 59.41 ? 406  GLY B C   1 
ATOM   6279 O  O   . GLY B 1 417 ? 48.002  57.532  71.923  1.00 59.41 ? 406  GLY B O   1 
ATOM   6280 N  N   . ARG B 1 418 ? 49.672  58.656  72.935  1.00 54.81 ? 407  ARG B N   1 
ATOM   6281 C  CA  . ARG B 1 418 ? 49.903  59.591  71.843  1.00 54.81 ? 407  ARG B CA  1 
ATOM   6282 C  C   . ARG B 1 418 ? 51.363  59.501  71.430  1.00 54.81 ? 407  ARG B C   1 
ATOM   6283 O  O   . ARG B 1 418 ? 52.254  59.500  72.285  1.00 54.81 ? 407  ARG B O   1 
ATOM   6284 C  CB  . ARG B 1 418 ? 49.543  61.023  72.252  1.00 54.81 ? 407  ARG B CB  1 
ATOM   6285 C  CG  . ARG B 1 418 ? 50.187  61.487  73.547  1.00 54.81 ? 407  ARG B CG  1 
ATOM   6286 C  CD  . ARG B 1 418 ? 50.071  62.992  73.715  1.00 54.81 ? 407  ARG B CD  1 
ATOM   6287 N  NE  . ARG B 1 418 ? 48.768  63.407  74.230  1.00 54.81 ? 407  ARG B NE  1 
ATOM   6288 C  CZ  . ARG B 1 418 ? 48.544  63.873  75.457  1.00 54.81 ? 407  ARG B CZ  1 
ATOM   6289 N  NH1 . ARG B 1 418 ? 49.532  63.998  76.335  1.00 54.81 ? 407  ARG B NH1 1 
ATOM   6290 N  NH2 . ARG B 1 418 ? 47.316  64.223  75.811  1.00 54.81 ? 407  ARG B NH2 1 
ATOM   6291 N  N   . LYS B 1 419 ? 51.603  59.421  70.126  1.00 53.55 ? 408  LYS B N   1 
ATOM   6292 C  CA  . LYS B 1 419 ? 52.934  59.222  69.578  1.00 53.55 ? 408  LYS B CA  1 
ATOM   6293 C  C   . LYS B 1 419 ? 53.387  60.457  68.814  1.00 53.55 ? 408  LYS B C   1 
ATOM   6294 O  O   . LYS B 1 419 ? 52.580  61.287  68.387  1.00 53.55 ? 408  LYS B O   1 
ATOM   6295 C  CB  . LYS B 1 419 ? 52.967  58.000  68.654  1.00 53.55 ? 408  LYS B CB  1 
ATOM   6296 N  N   . LEU B 1 420 ? 54.702  60.565  68.645  1.00 52.02 ? 409  LEU B N   1 
ATOM   6297 C  CA  . LEU B 1 420 ? 55.270  61.683  67.908  1.00 52.02 ? 409  LEU B CA  1 
ATOM   6298 C  C   . LEU B 1 420 ? 54.697  61.726  66.498  1.00 52.02 ? 409  LEU B C   1 
ATOM   6299 O  O   . LEU B 1 420 ? 54.562  60.696  65.832  1.00 52.02 ? 409  LEU B O   1 
ATOM   6300 C  CB  . LEU B 1 420 ? 56.791  61.557  67.853  1.00 52.02 ? 409  LEU B CB  1 
ATOM   6301 C  CG  . LEU B 1 420 ? 57.557  61.923  69.122  1.00 52.02 ? 409  LEU B CG  1 
ATOM   6302 C  CD1 . LEU B 1 420 ? 57.219  60.973  70.250  1.00 52.02 ? 409  LEU B CD1 1 
ATOM   6303 C  CD2 . LEU B 1 420 ? 59.049  61.913  68.853  1.00 52.02 ? 409  LEU B CD2 1 
ATOM   6304 N  N   . ASN B 1 421 ? 54.357  62.928  66.042  1.00 55.64 ? 410  ASN B N   1 
ATOM   6305 C  CA  . ASN B 1 421 ? 53.771  63.132  64.722  1.00 55.64 ? 410  ASN B CA  1 
ATOM   6306 C  C   . ASN B 1 421 ? 54.880  63.514  63.750  1.00 55.64 ? 410  ASN B C   1 
ATOM   6307 O  O   . ASN B 1 421 ? 55.446  64.607  63.841  1.00 55.64 ? 410  ASN B O   1 
ATOM   6308 C  CB  . ASN B 1 421 ? 52.690  64.209  64.768  1.00 55.64 ? 410  ASN B CB  1 
ATOM   6309 N  N   . TRP B 1 422 ? 55.184  62.609  62.816  1.00 57.00 ? 411  TRP B N   1 
ATOM   6310 C  CA  . TRP B 1 422 ? 56.172  62.849  61.780  1.00 57.00 ? 411  TRP B CA  1 
ATOM   6311 C  C   . TRP B 1 422 ? 55.491  62.970  60.421  1.00 57.00 ? 411  TRP B C   1 
ATOM   6312 O  O   . TRP B 1 422 ? 54.586  62.186  60.117  1.00 57.00 ? 411  TRP B O   1 
ATOM   6313 C  CB  . TRP B 1 422 ? 57.200  61.714  61.725  1.00 57.00 ? 411  TRP B CB  1 
ATOM   6314 C  CG  . TRP B 1 422 ? 57.925  61.490  63.012  1.00 57.00 ? 411  TRP B CG  1 
ATOM   6315 C  CD1 . TRP B 1 422 ? 57.704  60.493  63.909  1.00 57.00 ? 411  TRP B CD1 1 
ATOM   6316 C  CD2 . TRP B 1 422 ? 58.995  62.277  63.542  1.00 57.00 ? 411  TRP B CD2 1 
ATOM   6317 N  NE1 . TRP B 1 422 ? 58.567  60.609  64.968  1.00 57.00 ? 411  TRP B NE1 1 
ATOM   6318 C  CE2 . TRP B 1 422 ? 59.371  61.698  64.767  1.00 57.00 ? 411  TRP B CE2 1 
ATOM   6319 C  CE3 . TRP B 1 422 ? 59.671  63.416  63.101  1.00 57.00 ? 411  TRP B CE3 1 
ATOM   6320 C  CZ2 . TRP B 1 422 ? 60.392  62.219  65.554  1.00 57.00 ? 411  TRP B CZ2 1 
ATOM   6321 C  CZ3 . TRP B 1 422 ? 60.683  63.930  63.884  1.00 57.00 ? 411  TRP B CZ3 1 
ATOM   6322 C  CH2 . TRP B 1 422 ? 61.034  63.333  65.096  1.00 57.00 ? 411  TRP B CH2 1 
ATOM   6323 N  N   . PRO B 1 423 ? 55.887  63.936  59.586  1.00 61.39 ? 412  PRO B N   1 
ATOM   6324 C  CA  . PRO B 1 423 ? 55.255  64.039  58.259  1.00 61.39 ? 412  PRO B CA  1 
ATOM   6325 C  C   . PRO B 1 423 ? 55.350  62.764  57.437  1.00 61.39 ? 412  PRO B C   1 
ATOM   6326 O  O   . PRO B 1 423 ? 54.393  62.413  56.736  1.00 61.39 ? 412  PRO B O   1 
ATOM   6327 C  CB  . PRO B 1 423 ? 56.021  65.197  57.609  1.00 61.39 ? 412  PRO B CB  1 
ATOM   6328 C  CG  . PRO B 1 423 ? 56.447  66.040  58.746  1.00 61.39 ? 412  PRO B CG  1 
ATOM   6329 C  CD  . PRO B 1 423 ? 56.763  65.087  59.862  1.00 61.39 ? 412  PRO B CD  1 
ATOM   6330 N  N   . LEU B 1 424 ? 56.478  62.059  57.499  1.00 63.24 ? 413  LEU B N   1 
ATOM   6331 C  CA  . LEU B 1 424 ? 56.660  60.814  56.763  1.00 63.24 ? 413  LEU B CA  1 
ATOM   6332 C  C   . LEU B 1 424 ? 56.163  59.589  57.516  1.00 63.24 ? 413  LEU B C   1 
ATOM   6333 O  O   . LEU B 1 424 ? 56.131  58.499  56.935  1.00 63.24 ? 413  LEU B O   1 
ATOM   6334 C  CB  . LEU B 1 424 ? 58.139  60.613  56.421  1.00 63.24 ? 413  LEU B CB  1 
ATOM   6335 C  CG  . LEU B 1 424 ? 58.676  61.328  55.183  1.00 63.24 ? 413  LEU B CG  1 
ATOM   6336 C  CD1 . LEU B 1 424 ? 58.184  62.758  55.114  1.00 63.24 ? 413  LEU B CD1 1 
ATOM   6337 C  CD2 . LEU B 1 424 ? 60.194  61.286  55.189  1.00 63.24 ? 413  LEU B CD2 1 
ATOM   6338 N  N   . GLY B 1 425 ? 55.784  59.731  58.783  1.00 62.07 ? 414  GLY B N   1 
ATOM   6339 C  CA  . GLY B 1 425 ? 55.425  58.607  59.614  1.00 62.07 ? 414  GLY B CA  1 
ATOM   6340 C  C   . GLY B 1 425 ? 56.577  58.023  60.403  1.00 62.07 ? 414  GLY B C   1 
ATOM   6341 O  O   . GLY B 1 425 ? 56.340  57.294  61.373  1.00 62.07 ? 414  GLY B O   1 
ATOM   6342 N  N   . TYR B 1 426 ? 57.810  58.322  60.017  1.00 62.43 ? 415  TYR B N   1 
ATOM   6343 C  CA  . TYR B 1 426 ? 59.003  57.896  60.727  1.00 62.43 ? 415  TYR B CA  1 
ATOM   6344 C  C   . TYR B 1 426 ? 59.957  59.076  60.797  1.00 62.43 ? 415  TYR B C   1 
ATOM   6345 O  O   . TYR B 1 426 ? 59.868  60.002  59.984  1.00 62.43 ? 415  TYR B O   1 
ATOM   6346 C  CB  . TYR B 1 426 ? 59.689  56.709  60.036  1.00 62.43 ? 415  TYR B CB  1 
ATOM   6347 C  CG  . TYR B 1 426 ? 59.649  56.775  58.529  1.00 62.43 ? 415  TYR B CG  1 
ATOM   6348 C  CD1 . TYR B 1 426 ? 58.587  56.236  57.818  1.00 62.43 ? 415  TYR B CD1 1 
ATOM   6349 C  CD2 . TYR B 1 426 ? 60.675  57.378  57.816  1.00 62.43 ? 415  TYR B CD2 1 
ATOM   6350 C  CE1 . TYR B 1 426 ? 58.547  56.296  56.441  1.00 62.43 ? 415  TYR B CE1 1 
ATOM   6351 C  CE2 . TYR B 1 426 ? 60.644  57.443  56.439  1.00 62.43 ? 415  TYR B CE2 1 
ATOM   6352 C  CZ  . TYR B 1 426 ? 59.577  56.901  55.757  1.00 62.43 ? 415  TYR B CZ  1 
ATOM   6353 O  OH  . TYR B 1 426 ? 59.541  56.962  54.383  1.00 62.43 ? 415  TYR B OH  1 
ATOM   6354 N  N   . PRO B 1 427 ? 60.876  59.077  61.760  1.00 58.85 ? 416  PRO B N   1 
ATOM   6355 C  CA  . PRO B 1 427 ? 61.802  60.196  61.869  1.00 58.85 ? 416  PRO B CA  1 
ATOM   6356 C  C   . PRO B 1 427 ? 62.673  60.289  60.634  1.00 58.85 ? 416  PRO B C   1 
ATOM   6357 O  O   . PRO B 1 427 ? 62.992  59.265  60.000  1.00 58.85 ? 416  PRO B O   1 
ATOM   6358 C  CB  . PRO B 1 427 ? 62.628  59.854  63.118  1.00 58.85 ? 416  PRO B CB  1 
ATOM   6359 C  CG  . PRO B 1 427 ? 61.871  58.795  63.825  1.00 58.85 ? 416  PRO B CG  1 
ATOM   6360 C  CD  . PRO B 1 427 ? 61.129  58.050  62.782  1.00 58.85 ? 416  PRO B CD  1 
ATOM   6361 N  N   . PRO B 1 428 ? 63.083  61.494  60.250  1.00 60.13 ? 417  PRO B N   1 
ATOM   6362 C  CA  . PRO B 1 428 ? 64.009  61.633  59.130  1.00 60.13 ? 417  PRO B CA  1 
ATOM   6363 C  C   . PRO B 1 428 ? 65.391  61.139  59.514  1.00 60.13 ? 417  PRO B C   1 
ATOM   6364 O  O   . PRO B 1 428 ? 65.704  61.024  60.709  1.00 60.13 ? 417  PRO B O   1 
ATOM   6365 C  CB  . PRO B 1 428 ? 64.009  63.144  58.863  1.00 60.13 ? 417  PRO B CB  1 
ATOM   6366 C  CG  . PRO B 1 428 ? 63.711  63.738  60.179  1.00 60.13 ? 417  PRO B CG  1 
ATOM   6367 C  CD  . PRO B 1 428 ? 62.728  62.804  60.822  1.00 60.13 ? 417  PRO B CD  1 
ATOM   6368 N  N   . PRO B 1 429 ? 66.244  60.822  58.543  1.00 62.21 ? 418  PRO B N   1 
ATOM   6369 C  CA  . PRO B 1 429 ? 67.621  60.444  58.879  1.00 62.21 ? 418  PRO B CA  1 
ATOM   6370 C  C   . PRO B 1 429 ? 68.447  61.655  59.282  1.00 62.21 ? 418  PRO B C   1 
ATOM   6371 O  O   . PRO B 1 429 ? 68.287  62.751  58.741  1.00 62.21 ? 418  PRO B O   1 
ATOM   6372 C  CB  . PRO B 1 429 ? 68.150  59.820  57.579  1.00 62.21 ? 418  PRO B CB  1 
ATOM   6373 C  CG  . PRO B 1 429 ? 66.964  59.694  56.667  1.00 62.21 ? 418  PRO B CG  1 
ATOM   6374 C  CD  . PRO B 1 429 ? 66.002  60.739  57.095  1.00 62.21 ? 418  PRO B CD  1 
ATOM   6375 N  N   . ASP B 1 430 ? 69.343  61.445  60.247  1.00 61.19 ? 419  ASP B N   1 
ATOM   6376 C  CA  . ASP B 1 430 ? 70.283  62.489  60.631  1.00 61.19 ? 419  ASP B CA  1 
ATOM   6377 C  C   . ASP B 1 430 ? 71.319  62.763  59.553  1.00 61.19 ? 419  ASP B C   1 
ATOM   6378 O  O   . ASP B 1 430 ? 72.061  63.744  59.667  1.00 61.19 ? 419  ASP B O   1 
ATOM   6379 C  CB  . ASP B 1 430 ? 70.981  62.113  61.936  1.00 61.19 ? 419  ASP B CB  1 
ATOM   6380 C  CG  . ASP B 1 430 ? 71.810  60.855  61.810  1.00 61.19 ? 419  ASP B CG  1 
ATOM   6381 O  OD1 . ASP B 1 430 ? 71.812  60.249  60.720  1.00 61.19 ? 419  ASP B OD1 1 
ATOM   6382 O  OD2 . ASP B 1 430 ? 72.461  60.472  62.804  1.00 61.19 ? 419  ASP B OD2 1 
ATOM   6383 N  N   . ILE B 1 431 ? 71.399  61.916  58.532  1.00 65.37 ? 420  ILE B N   1 
ATOM   6384 C  CA  . ILE B 1 431 ? 72.270  62.143  57.383  1.00 65.37 ? 420  ILE B CA  1 
ATOM   6385 C  C   . ILE B 1 431 ? 71.471  61.814  56.127  1.00 65.37 ? 420  ILE B C   1 
ATOM   6386 O  O   . ILE B 1 431 ? 70.961  60.692  56.001  1.00 65.37 ? 420  ILE B O   1 
ATOM   6387 C  CB  . ILE B 1 431 ? 73.549  61.298  57.473  1.00 65.37 ? 420  ILE B CB  1 
ATOM   6388 N  N   . PRO B 1 432 ? 71.331  62.740  55.179  1.00 68.56 ? 421  PRO B N   1 
ATOM   6389 C  CA  . PRO B 1 432 ? 70.512  62.454  53.997  1.00 68.56 ? 421  PRO B CA  1 
ATOM   6390 C  C   . PRO B 1 432 ? 71.110  61.332  53.162  1.00 68.56 ? 421  PRO B C   1 
ATOM   6391 O  O   . PRO B 1 432 ? 72.319  61.092  53.174  1.00 68.56 ? 421  PRO B O   1 
ATOM   6392 C  CB  . PRO B 1 432 ? 70.509  63.783  53.237  1.00 68.56 ? 421  PRO B CB  1 
ATOM   6393 C  CG  . PRO B 1 432 ? 71.765  64.447  53.653  1.00 68.56 ? 421  PRO B CG  1 
ATOM   6394 C  CD  . PRO B 1 432 ? 72.006  64.045  55.075  1.00 68.56 ? 421  PRO B CD  1 
ATOM   6395 N  N   . LYS B 1 433 ? 70.237  60.641  52.426  1.00 75.17 ? 422  LYS B N   1 
ATOM   6396 C  CA  . LYS B 1 433 ? 70.660  59.449  51.698  1.00 75.17 ? 422  LYS B CA  1 
ATOM   6397 C  C   . LYS B 1 433 ? 71.739  59.772  50.671  1.00 75.17 ? 422  LYS B C   1 
ATOM   6398 O  O   . LYS B 1 433 ? 72.716  59.027  50.534  1.00 75.17 ? 422  LYS B O   1 
ATOM   6399 C  CB  . LYS B 1 433 ? 69.455  58.799  51.018  1.00 75.17 ? 422  LYS B CB  1 
ATOM   6400 N  N   . CYS B 1 434 ? 71.581  60.870  49.936  1.00 80.75 ? 423  CYS B N   1 
ATOM   6401 C  CA  . CYS B 1 434 ? 72.511  61.249  48.878  1.00 80.75 ? 423  CYS B CA  1 
ATOM   6402 C  C   . CYS B 1 434 ? 72.953  62.695  49.045  1.00 80.75 ? 423  CYS B C   1 
ATOM   6403 O  O   . CYS B 1 434 ? 73.100  63.438  48.070  1.00 80.75 ? 423  CYS B O   1 
ATOM   6404 C  CB  . CYS B 1 434 ? 71.886  61.033  47.502  1.00 80.75 ? 423  CYS B CB  1 
ATOM   6405 S  SG  . CYS B 1 434 ? 73.061  61.101  46.127  1.00 80.75 ? 423  CYS B SG  1 
ATOM   6406 N  N   . GLY B 1 435 ? 73.173  63.115  50.288  1.00 74.84 ? 424  GLY B N   1 
ATOM   6407 C  CA  . GLY B 1 435 ? 73.602  64.471  50.566  1.00 74.84 ? 424  GLY B CA  1 
ATOM   6408 C  C   . GLY B 1 435 ? 74.954  64.535  51.242  1.00 74.84 ? 424  GLY B C   1 
ATOM   6409 O  O   . GLY B 1 435 ? 75.726  63.572  51.191  1.00 74.84 ? 424  GLY B O   1 
ATOM   6410 N  N   . PHE B 1 436 ? 75.250  65.666  51.875  1.00 68.34 ? 425  PHE B N   1 
ATOM   6411 C  CA  . PHE B 1 436 ? 76.538  65.878  52.527  1.00 68.34 ? 425  PHE B CA  1 
ATOM   6412 C  C   . PHE B 1 436 ? 76.892  64.710  53.443  1.00 68.34 ? 425  PHE B C   1 
ATOM   6413 O  O   . PHE B 1 436 ? 77.992  64.648  53.991  1.00 68.34 ? 425  PHE B O   1 
ATOM   6414 C  CB  . PHE B 1 436 ? 76.520  67.185  53.323  1.00 68.34 ? 425  PHE B CB  1 
ATOM   6415 C  CG  . PHE B 1 436 ? 75.792  67.088  54.634  1.00 68.34 ? 425  PHE B CG  1 
ATOM   6416 C  CD1 . PHE B 1 436 ? 76.462  66.727  55.790  1.00 68.34 ? 425  PHE B CD1 1 
ATOM   6417 C  CD2 . PHE B 1 436 ? 74.436  67.348  54.711  1.00 68.34 ? 425  PHE B CD2 1 
ATOM   6418 C  CE1 . PHE B 1 436 ? 75.796  66.633  56.991  1.00 68.34 ? 425  PHE B CE1 1 
ATOM   6419 C  CE2 . PHE B 1 436 ? 73.767  67.254  55.916  1.00 68.34 ? 425  PHE B CE2 1 
ATOM   6420 C  CZ  . PHE B 1 436 ? 74.450  66.896  57.055  1.00 68.34 ? 425  PHE B CZ  1 
HETATM 6421 C  C1  . NAG C 2 .   ? 106.618 80.138  88.122  1.00 32.20 ? 1    NAG C C1  1 
HETATM 6422 C  C2  . NAG C 2 .   ? 106.635 78.630  87.859  1.00 32.20 ? 1    NAG C C2  1 
HETATM 6423 C  C3  . NAG C 2 .   ? 106.655 78.308  86.353  1.00 32.20 ? 1    NAG C C3  1 
HETATM 6424 C  C4  . NAG C 2 .   ? 105.866 79.287  85.489  1.00 32.20 ? 1    NAG C C4  1 
HETATM 6425 C  C5  . NAG C 2 .   ? 105.953 80.708  86.018  1.00 32.20 ? 1    NAG C C5  1 
HETATM 6426 C  C6  . NAG C 2 .   ? 105.021 81.665  85.320  1.00 32.20 ? 1    NAG C C6  1 
HETATM 6427 C  C7  . NAG C 2 .   ? 107.735 77.354  89.654  1.00 32.20 ? 1    NAG C C7  1 
HETATM 6428 C  C8  . NAG C 2 .   ? 109.040 76.820  90.165  1.00 32.20 ? 1    NAG C C8  1 
HETATM 6429 N  N2  . NAG C 2 .   ? 107.793 78.033  88.506  1.00 32.20 ? 1    NAG C N2  1 
HETATM 6430 O  O3  . NAG C 2 .   ? 106.120 77.002  86.168  1.00 32.20 ? 1    NAG C O3  1 
HETATM 6431 O  O4  . NAG C 2 .   ? 106.528 79.327  84.233  1.00 32.20 ? 1    NAG C O4  1 
HETATM 6432 O  O5  . NAG C 2 .   ? 105.612 80.720  87.403  1.00 32.20 ? 1    NAG C O5  1 
HETATM 6433 O  O6  . NAG C 2 .   ? 105.668 82.895  85.028  1.00 32.20 ? 1    NAG C O6  1 
HETATM 6434 O  O7  . NAG C 2 .   ? 106.680 77.172  90.251  1.00 32.20 ? 1    NAG C O7  1 
HETATM 6435 C  C1  . NAG C 2 .   ? 105.908 79.043  82.944  1.00 42.83 ? 2    NAG C C1  1 
HETATM 6436 C  C2  . NAG C 2 .   ? 104.377 78.918  82.861  1.00 42.83 ? 2    NAG C C2  1 
HETATM 6437 C  C3  . NAG C 2 .   ? 103.959 78.782  81.396  1.00 42.83 ? 2    NAG C C3  1 
HETATM 6438 C  C4  . NAG C 2 .   ? 104.511 79.943  80.577  1.00 42.83 ? 2    NAG C C4  1 
HETATM 6439 C  C5  . NAG C 2 .   ? 106.018 80.081  80.775  1.00 42.83 ? 2    NAG C C5  1 
HETATM 6440 C  C6  . NAG C 2 .   ? 106.580 81.321  80.127  1.00 42.83 ? 2    NAG C C6  1 
HETATM 6441 C  C7  . NAG C 2 .   ? 102.594 77.476  83.750  1.00 42.83 ? 2    NAG C C7  1 
HETATM 6442 C  C8  . NAG C 2 .   ? 102.278 76.269  84.579  1.00 42.83 ? 2    NAG C C8  1 
HETATM 6443 N  N2  . NAG C 2 .   ? 103.891 77.787  83.634  1.00 42.83 ? 2    NAG C N2  1 
HETATM 6444 O  O3  . NAG C 2 .   ? 102.541 78.722  81.296  1.00 42.83 ? 2    NAG C O3  1 
HETATM 6445 O  O4  . NAG C 2 .   ? 104.287 79.718  79.191  1.00 42.83 ? 2    NAG C O4  1 
HETATM 6446 O  O5  . NAG C 2 .   ? 106.336 80.174  82.169  1.00 42.83 ? 2    NAG C O5  1 
HETATM 6447 O  O6  . NAG C 2 .   ? 107.846 81.665  80.674  1.00 42.83 ? 2    NAG C O6  1 
HETATM 6448 O  O7  . NAG C 2 .   ? 101.715 78.136  83.203  1.00 42.83 ? 2    NAG C O7  1 
HETATM 6449 C  C1  . MAN C 2 .   ? 102.114 78.324  79.971  1.00 56.29 ? 3    MAN C C1  1 
HETATM 6450 C  C2  . MAN C 2 .   ? 100.701 77.703  80.118  1.00 56.29 ? 3    MAN C C2  1 
HETATM 6451 C  C3  . MAN C 2 .   ? 100.394 76.842  78.908  1.00 56.29 ? 3    MAN C C3  1 
HETATM 6452 C  C4  . MAN C 2 .   ? 101.229 77.302  77.711  1.00 56.29 ? 3    MAN C C4  1 
HETATM 6453 C  C5  . MAN C 2 .   ? 102.701 76.999  78.001  1.00 56.29 ? 3    MAN C C5  1 
HETATM 6454 C  C6  . MAN C 2 .   ? 103.660 77.710  77.060  1.00 56.29 ? 3    MAN C C6  1 
HETATM 6455 O  O2  . MAN C 2 .   ? 99.674  78.689  80.134  1.00 56.29 ? 3    MAN C O2  1 
HETATM 6456 O  O3  . MAN C 2 .   ? 99.016  76.876  78.592  1.00 56.29 ? 3    MAN C O3  1 
HETATM 6457 O  O4  . MAN C 2 .   ? 100.823 76.621  76.526  1.00 56.29 ? 3    MAN C O4  1 
HETATM 6458 O  O5  . MAN C 2 .   ? 103.021 77.405  79.370  1.00 56.29 ? 3    MAN C O5  1 
HETATM 6459 O  O6  . MAN C 2 .   ? 104.638 76.782  76.584  1.00 56.29 ? 3    MAN C O6  1 
HETATM 6460 C  C1  . NAG D 2 .   ? 111.480 115.561 88.180  1.00 42.66 ? 1    NAG D C1  1 
HETATM 6461 C  C2  . NAG D 2 .   ? 112.924 115.468 88.697  1.00 42.66 ? 1    NAG D C2  1 
HETATM 6462 C  C3  . NAG D 2 .   ? 113.030 116.001 90.120  1.00 42.66 ? 1    NAG D C3  1 
HETATM 6463 C  C4  . NAG D 2 .   ? 112.537 117.436 90.148  1.00 42.66 ? 1    NAG D C4  1 
HETATM 6464 C  C5  . NAG D 2 .   ? 111.064 117.437 89.765  1.00 42.66 ? 1    NAG D C5  1 
HETATM 6465 C  C6  . NAG D 2 .   ? 110.446 118.813 89.735  1.00 42.66 ? 1    NAG D C6  1 
HETATM 6466 C  C7  . NAG D 2 .   ? 114.541 113.764 87.995  1.00 42.66 ? 1    NAG D C7  1 
HETATM 6467 C  C8  . NAG D 2 .   ? 114.897 112.310 88.015  1.00 42.66 ? 1    NAG D C8  1 
HETATM 6468 N  N2  . NAG D 2 .   ? 113.413 114.101 88.627  1.00 42.66 ? 1    NAG D N2  1 
HETATM 6469 O  O3  . NAG D 2 .   ? 114.383 115.944 90.558  1.00 42.66 ? 1    NAG D O3  1 
HETATM 6470 O  O4  . NAG D 2 .   ? 112.923 118.114 91.345  1.00 42.66 ? 1    NAG D O4  1 
HETATM 6471 O  O5  . NAG D 2 .   ? 110.939 116.913 88.431  1.00 42.66 ? 1    NAG D O5  1 
HETATM 6472 O  O6  . NAG D 2 .   ? 109.552 118.947 88.639  1.00 42.66 ? 1    NAG D O6  1 
HETATM 6473 O  O7  . NAG D 2 .   ? 115.243 114.597 87.434  1.00 42.66 ? 1    NAG D O7  1 
HETATM 6474 C  C1  . NAG D 2 .   ? 112.092 118.360 92.488  1.00 45.47 ? 2    NAG D C1  1 
HETATM 6475 C  C2  . NAG D 2 .   ? 113.104 118.616 93.607  1.00 45.47 ? 2    NAG D C2  1 
HETATM 6476 C  C3  . NAG D 2 .   ? 112.416 119.071 94.895  1.00 45.47 ? 2    NAG D C3  1 
HETATM 6477 C  C4  . NAG D 2 .   ? 111.422 120.189 94.621  1.00 45.47 ? 2    NAG D C4  1 
HETATM 6478 C  C5  . NAG D 2 .   ? 110.489 119.780 93.493  1.00 45.47 ? 2    NAG D C5  1 
HETATM 6479 C  C6  . NAG D 2 .   ? 109.526 120.874 93.099  1.00 45.47 ? 2    NAG D C6  1 
HETATM 6480 C  C7  . NAG D 2 .   ? 115.226 117.464 94.077  1.00 45.47 ? 2    NAG D C7  1 
HETATM 6481 C  C8  . NAG D 2 .   ? 115.870 118.818 94.030  1.00 45.47 ? 2    NAG D C8  1 
HETATM 6482 N  N2  . NAG D 2 .   ? 113.908 117.431 93.858  1.00 45.47 ? 2    NAG D N2  1 
HETATM 6483 O  O3  . NAG D 2 .   ? 113.448 119.547 95.750  1.00 45.47 ? 2    NAG D O3  1 
HETATM 6484 O  O4  . NAG D 2 .   ? 110.652 120.450 95.788  1.00 45.47 ? 2    NAG D O4  1 
HETATM 6485 O  O5  . NAG D 2 .   ? 111.268 119.472 92.333  1.00 45.47 ? 2    NAG D O5  1 
HETATM 6486 O  O6  . NAG D 2 .   ? 108.617 120.435 92.100  1.00 45.47 ? 2    NAG D O6  1 
HETATM 6487 O  O7  . NAG D 2 .   ? 115.874 116.445 94.293  1.00 45.47 ? 2    NAG D O7  1 
HETATM 6488 C  C1  . MAN D 2 .   ? 113.116 119.854 97.126  1.00 46.45 ? 3    MAN D C1  1 
HETATM 6489 C  C2  . MAN D 2 .   ? 114.421 119.457 97.889  1.00 46.45 ? 3    MAN D C2  1 
HETATM 6490 C  C3  . MAN D 2 .   ? 114.106 118.957 99.278  1.00 46.45 ? 3    MAN D C3  1 
HETATM 6491 C  C4  . MAN D 2 .   ? 112.959 119.744 99.833  1.00 46.45 ? 3    MAN D C4  1 
HETATM 6492 C  C5  . MAN D 2 .   ? 111.688 119.293 99.105  1.00 46.45 ? 3    MAN D C5  1 
HETATM 6493 C  C6  . MAN D 2 .   ? 110.479 120.197 99.355  1.00 46.45 ? 3    MAN D C6  1 
HETATM 6494 O  O2  . MAN D 2 .   ? 115.265 120.591 98.080  1.00 46.45 ? 3    MAN D O2  1 
HETATM 6495 O  O3  . MAN D 2 .   ? 115.239 119.027 100.144 1.00 46.45 ? 3    MAN D O3  1 
HETATM 6496 O  O4  . MAN D 2 .   ? 112.829 119.489 101.220 1.00 46.45 ? 3    MAN D O4  1 
HETATM 6497 O  O5  . MAN D 2 .   ? 111.938 119.200 97.635  1.00 46.45 ? 3    MAN D O5  1 
HETATM 6498 O  O6  . MAN D 2 .   ? 110.910 121.361 100.065 1.00 46.45 ? 3    MAN D O6  1 
HETATM 6499 C  C1  . NAG E 2 .   ? 66.486  93.057  88.163  1.00 31.43 ? 1    NAG E C1  1 
HETATM 6500 C  C2  . NAG E 2 .   ? 66.488  94.553  87.846  1.00 31.43 ? 1    NAG E C2  1 
HETATM 6501 C  C3  . NAG E 2 .   ? 66.457  94.813  86.331  1.00 31.43 ? 1    NAG E C3  1 
HETATM 6502 C  C4  . NAG E 2 .   ? 67.303  93.835  85.521  1.00 31.43 ? 1    NAG E C4  1 
HETATM 6503 C  C5  . NAG E 2 .   ? 67.217  92.425  86.085  1.00 31.43 ? 1    NAG E C5  1 
HETATM 6504 C  C6  . NAG E 2 .   ? 68.184  91.463  85.444  1.00 31.43 ? 1    NAG E C6  1 
HETATM 6505 C  C7  . NAG E 2 .   ? 65.438  95.882  89.628  1.00 31.43 ? 1    NAG E C7  1 
HETATM 6506 C  C8  . NAG E 2 .   ? 64.156  96.466  90.141  1.00 31.43 ? 1    NAG E C8  1 
HETATM 6507 N  N2  . NAG E 2 .   ? 65.351  95.195  88.486  1.00 31.43 ? 1    NAG E N2  1 
HETATM 6508 O  O3  . NAG E 2 .   ? 66.934  96.134  86.096  1.00 31.43 ? 1    NAG E O3  1 
HETATM 6509 O  O4  . NAG E 2 .   ? 66.700  93.749  84.237  1.00 31.43 ? 1    NAG E O4  1 
HETATM 6510 O  O5  . NAG E 2 .   ? 67.506  92.440  87.484  1.00 31.43 ? 1    NAG E O5  1 
HETATM 6511 O  O6  . NAG E 2 .   ? 67.544  90.236  85.123  1.00 31.43 ? 1    NAG E O6  1 
HETATM 6512 O  O7  . NAG E 2 .   ? 66.502  96.032  90.216  1.00 31.43 ? 1    NAG E O7  1 
HETATM 6513 C  C1  . NAG E 2 .   ? 67.300  94.116  82.959  1.00 43.30 ? 2    NAG E C1  1 
HETATM 6514 C  C2  . NAG E 2 .   ? 68.825  94.271  82.839  1.00 43.30 ? 2    NAG E C2  1 
HETATM 6515 C  C3  . NAG E 2 .   ? 69.210  94.438  81.367  1.00 43.30 ? 2    NAG E C3  1 
HETATM 6516 C  C4  . NAG E 2 .   ? 68.659  93.283  80.541  1.00 43.30 ? 2    NAG E C4  1 
HETATM 6517 C  C5  . NAG E 2 .   ? 67.159  93.129  80.764  1.00 43.30 ? 2    NAG E C5  1 
HETATM 6518 C  C6  . NAG E 2 .   ? 66.598  91.893  80.108  1.00 43.30 ? 2    NAG E C6  1 
HETATM 6519 C  C7  . NAG E 2 .   ? 70.612  95.693  83.745  1.00 43.30 ? 2    NAG E C7  1 
HETATM 6520 C  C8  . NAG E 2 .   ? 70.937  96.889  84.588  1.00 43.30 ? 2    NAG E C8  1 
HETATM 6521 N  N2  . NAG E 2 .   ? 69.313  95.395  83.621  1.00 43.30 ? 2    NAG E N2  1 
HETATM 6522 O  O3  . NAG E 2 .   ? 70.627  94.510  81.241  1.00 43.30 ? 2    NAG E O3  1 
HETATM 6523 O  O4  . NAG E 2 .   ? 68.868  93.520  79.155  1.00 43.30 ? 2    NAG E O4  1 
HETATM 6524 O  O5  . NAG E 2 .   ? 66.870  93.006  82.161  1.00 43.30 ? 2    NAG E O5  1 
HETATM 6525 O  O6  . NAG E 2 .   ? 65.329  91.549  80.648  1.00 43.30 ? 2    NAG E O6  1 
HETATM 6526 O  O7  . NAG E 2 .   ? 71.486  95.030  83.196  1.00 43.30 ? 2    NAG E O7  1 
HETATM 6527 C  C1  . MAN E 2 .   ? 71.072  94.879  79.909  1.00 55.00 ? 3    MAN E C1  1 
HETATM 6528 C  C2  . MAN E 2 .   ? 72.463  95.569  80.091  1.00 55.00 ? 3    MAN E C2  1 
HETATM 6529 C  C3  . MAN E 2 .   ? 72.810  96.430  78.881  1.00 55.00 ? 3    MAN E C3  1 
HETATM 6530 C  C4  . MAN E 2 .   ? 72.065  95.949  77.662  1.00 55.00 ? 3    MAN E C4  1 
HETATM 6531 C  C5  . MAN E 2 .   ? 70.578  96.248  77.871  1.00 55.00 ? 3    MAN E C5  1 
HETATM 6532 C  C6  . MAN E 2 .   ? 69.692  95.683  76.774  1.00 55.00 ? 3    MAN E C6  1 
HETATM 6533 O  O2  . MAN E 2 .   ? 73.514  94.611  80.179  1.00 55.00 ? 3    MAN E O2  1 
HETATM 6534 O  O3  . MAN E 2 .   ? 74.208  96.455  78.621  1.00 55.00 ? 3    MAN E O3  1 
HETATM 6535 O  O4  . MAN E 2 .   ? 72.524  96.630  76.508  1.00 55.00 ? 3    MAN E O4  1 
HETATM 6536 O  O5  . MAN E 2 .   ? 70.131  95.715  79.191  1.00 55.00 ? 3    MAN E O5  1 
HETATM 6537 O  O6  . MAN E 2 .   ? 68.430  96.340  76.832  1.00 55.00 ? 3    MAN E O6  1 
HETATM 6538 C  C1  . NAG F 2 .   ? 61.733  57.634  88.134  1.00 42.56 ? 1    NAG F C1  1 
HETATM 6539 C  C2  . NAG F 2 .   ? 60.298  57.741  88.682  1.00 42.56 ? 1    NAG F C2  1 
HETATM 6540 C  C3  . NAG F 2 .   ? 60.216  57.213  90.109  1.00 42.56 ? 1    NAG F C3  1 
HETATM 6541 C  C4  . NAG F 2 .   ? 60.698  55.774  90.130  1.00 42.56 ? 1    NAG F C4  1 
HETATM 6542 C  C5  . NAG F 2 .   ? 62.166  55.764  89.727  1.00 42.56 ? 1    NAG F C5  1 
HETATM 6543 C  C6  . NAG F 2 .   ? 62.778  54.386  89.699  1.00 42.56 ? 1    NAG F C6  1 
HETATM 6544 C  C7  . NAG F 2 .   ? 58.683  59.454  88.000  1.00 42.56 ? 1    NAG F C7  1 
HETATM 6545 C  C8  . NAG F 2 .   ? 58.339  60.910  88.019  1.00 42.56 ? 1    NAG F C8  1 
HETATM 6546 N  N2  . NAG F 2 .   ? 59.818  59.111  88.616  1.00 42.56 ? 1    NAG F N2  1 
HETATM 6547 O  O3  . NAG F 2 .   ? 58.872  57.280  90.574  1.00 42.56 ? 1    NAG F O3  1 
HETATM 6548 O  O4  . NAG F 2 .   ? 60.316  55.092  91.326  1.00 42.56 ? 1    NAG F O4  1 
HETATM 6549 O  O5  . NAG F 2 .   ? 62.273  56.278  88.387  1.00 42.56 ? 1    NAG F O5  1 
HETATM 6550 O  O6  . NAG F 2 .   ? 63.700  54.262  88.626  1.00 42.56 ? 1    NAG F O6  1 
HETATM 6551 O  O7  . NAG F 2 .   ? 57.967  58.624  87.453  1.00 42.56 ? 1    NAG F O7  1 
HETATM 6552 C  C1  . NAG F 2 .   ? 61.140  54.853  92.477  1.00 45.02 ? 2    NAG F C1  1 
HETATM 6553 C  C2  . NAG F 2 .   ? 60.126  54.602  93.596  1.00 45.02 ? 2    NAG F C2  1 
HETATM 6554 C  C3  . NAG F 2 .   ? 60.813  54.154  94.887  1.00 45.02 ? 2    NAG F C3  1 
HETATM 6555 C  C4  . NAG F 2 .   ? 61.802  53.030  94.619  1.00 45.02 ? 2    NAG F C4  1 
HETATM 6556 C  C5  . NAG F 2 .   ? 62.740  53.434  93.493  1.00 45.02 ? 2    NAG F C5  1 
HETATM 6557 C  C6  . NAG F 2 .   ? 63.702  52.338  93.104  1.00 45.02 ? 2    NAG F C6  1 
HETATM 6558 C  C7  . NAG F 2 .   ? 58.001  55.752  94.057  1.00 45.02 ? 2    NAG F C7  1 
HETATM 6559 C  C8  . NAG F 2 .   ? 57.360  54.397  94.015  1.00 45.02 ? 2    NAG F C8  1 
HETATM 6560 N  N2  . NAG F 2 .   ? 59.320  55.786  93.840  1.00 45.02 ? 2    NAG F N2  1 
HETATM 6561 O  O3  . NAG F 2 .   ? 59.779  53.692  95.748  1.00 45.02 ? 2    NAG F O3  1 
HETATM 6562 O  O4  . NAG F 2 .   ? 62.568  52.767  95.789  1.00 45.02 ? 2    NAG F O4  1 
HETATM 6563 O  O5  . NAG F 2 .   ? 61.966  53.741  92.329  1.00 45.02 ? 2    NAG F O5  1 
HETATM 6564 O  O6  . NAG F 2 .   ? 64.610  52.772  92.102  1.00 45.02 ? 2    NAG F O6  1 
HETATM 6565 O  O7  . NAG F 2 .   ? 57.351  56.772  94.267  1.00 45.02 ? 2    NAG F O7  1 
HETATM 6566 C  C1  . MAN F 2 .   ? 60.110  53.372  97.121  1.00 45.56 ? 3    MAN F C1  1 
HETATM 6567 C  C2  . MAN F 2 .   ? 58.805  53.761  97.884  1.00 45.56 ? 3    MAN F C2  1 
HETATM 6568 C  C3  . MAN F 2 .   ? 59.120  54.257  99.275  1.00 45.56 ? 3    MAN F C3  1 
HETATM 6569 C  C4  . MAN F 2 .   ? 60.257  53.459  99.833  1.00 45.56 ? 3    MAN F C4  1 
HETATM 6570 C  C5  . MAN F 2 .   ? 61.534  53.901  99.112  1.00 45.56 ? 3    MAN F C5  1 
HETATM 6571 C  C6  . MAN F 2 .   ? 62.727  52.975  99.343  1.00 45.56 ? 3    MAN F C6  1 
HETATM 6572 O  O2  . MAN F 2 .   ? 57.970  52.622  98.072  1.00 45.56 ? 3    MAN F O2  1 
HETATM 6573 O  O3  . MAN F 2 .   ? 57.985  54.192  100.137 1.00 45.56 ? 3    MAN F O3  1 
HETATM 6574 O  O4  . MAN F 2 .   ? 60.385  53.710  101.219 1.00 45.56 ? 3    MAN F O4  1 
HETATM 6575 O  O5  . MAN F 2 .   ? 61.283  54.024  97.642  1.00 45.56 ? 3    MAN F O5  1 
HETATM 6576 O  O6  . MAN F 2 .   ? 62.305  51.856  100.134 1.00 45.56 ? 3    MAN F O6  1 
HETATM 6577 CL CL  . CL  G 3 .   ? 100.794 88.373  93.072  1.00 27.44 ? 1101 CL  A CL  1 
HETATM 6578 C  C1  . NAG H 4 .   ? 97.370  118.989 95.458  1.00 55.73 ? 1102 NAG A C1  1 
HETATM 6579 C  C2  . NAG H 4 .   ? 96.065  119.659 95.151  1.00 55.73 ? 1102 NAG A C2  1 
HETATM 6580 C  C3  . NAG H 4 .   ? 96.404  120.844 94.313  1.00 55.73 ? 1102 NAG A C3  1 
HETATM 6581 C  C4  . NAG H 4 .   ? 97.344  121.726 95.087  1.00 55.73 ? 1102 NAG A C4  1 
HETATM 6582 C  C5  . NAG H 4 .   ? 98.602  120.966 95.413  1.00 55.73 ? 1102 NAG A C5  1 
HETATM 6583 C  C6  . NAG H 4 .   ? 99.483  121.806 96.321  1.00 55.73 ? 1102 NAG A C6  1 
HETATM 6584 C  C7  . NAG H 4 .   ? 94.201  118.177 95.260  1.00 55.73 ? 1102 NAG A C7  1 
HETATM 6585 C  C8  . NAG H 4 .   ? 93.224  117.256 94.611  1.00 55.73 ? 1102 NAG A C8  1 
HETATM 6586 N  N2  . NAG H 4 .   ? 95.087  118.823 94.517  1.00 55.73 ? 1102 NAG A N2  1 
HETATM 6587 O  O3  . NAG H 4 .   ? 95.211  121.535 94.012  1.00 55.73 ? 1102 NAG A O3  1 
HETATM 6588 O  O4  . NAG H 4 .   ? 97.669  122.789 94.209  1.00 55.73 ? 1102 NAG A O4  1 
HETATM 6589 O  O5  . NAG H 4 .   ? 98.217  119.849 96.154  1.00 55.73 ? 1102 NAG A O5  1 
HETATM 6590 O  O6  . NAG H 4 .   ? 100.303 121.037 97.219  1.00 55.73 ? 1102 NAG A O6  1 
HETATM 6591 O  O7  . NAG H 4 .   ? 94.198  118.326 96.448  1.00 55.73 ? 1102 NAG A O7  1 
HETATM 6592 CL CL  . CL  I 3 .   ? 72.497  84.808  93.068  1.00 34.01 ? 1101 CL  B CL  1 
HETATM 6593 C  C1  . NAG J 4 .   ? 75.779  54.491  95.428  1.00 52.28 ? 1102 NAG B C1  1 
HETATM 6594 C  C2  . NAG J 4 .   ? 77.085  53.779  95.196  1.00 52.28 ? 1102 NAG B C2  1 
HETATM 6595 C  C3  . NAG J 4 .   ? 76.793  52.560  94.392  1.00 52.28 ? 1102 NAG B C3  1 
HETATM 6596 C  C4  . NAG J 4 .   ? 75.843  51.696  95.163  1.00 52.28 ? 1102 NAG B C4  1 
HETATM 6597 C  C5  . NAG J 4 .   ? 74.578  52.469  95.410  1.00 52.28 ? 1102 NAG B C5  1 
HETATM 6598 C  C6  . NAG J 4 .   ? 73.688  51.607  96.286  1.00 52.28 ? 1102 NAG B C6  1 
HETATM 6599 C  C7  . NAG J 4 .   ? 79.024  55.138  95.323  1.00 52.28 ? 1102 NAG B C7  1 
HETATM 6600 C  C8  . NAG J 4 .   ? 79.984  56.094  94.700  1.00 52.28 ? 1102 NAG B C8  1 
HETATM 6601 N  N2  . NAG J 4 .   ? 78.104  54.565  94.573  1.00 52.28 ? 1102 NAG B N2  1 
HETATM 6602 O  O3  . NAG J 4 .   ? 78.002  51.879  94.137  1.00 52.28 ? 1102 NAG B O3  1 
HETATM 6603 O  O4  . NAG J 4 .   ? 75.552  50.609  94.299  1.00 52.28 ? 1102 NAG B O4  1 
HETATM 6604 O  O5  . NAG J 4 .   ? 74.920  53.628  96.125  1.00 52.28 ? 1102 NAG B O5  1 
HETATM 6605 O  O6  . NAG J 4 .   ? 72.924  52.342  97.253  1.00 52.28 ? 1102 NAG B O6  1 
HETATM 6606 O  O7  . NAG J 4 .   ? 79.071  54.914  96.499  1.00 52.28 ? 1102 NAG B O7  1 
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