data_9DL4
# 
_entry.id   9DL4 
# 
_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   9DL4         pdb_00009dl4 10.2210/pdb9dl4/pdb 
WWPDB D_1000287812 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2024-11-27 
2 'Structure model' 1 1 2024-12-11 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
2 2 'Structure model' '_citation.title'                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9DL4 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-10 
_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_contact_author.id                 3 
_pdbx_contact_author.email              tannerjj@missouri.edu 
_pdbx_contact_author.name_first         John 
_pdbx_contact_author.name_last          Tanner 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8314-113X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Tanner, J.J.' 1 ? 
'Meeks, K.R.'  2 ? 
# 
_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                   CH 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Molecules 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1420-3049 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            29 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;Crystallographic Fragment Screening of a Bifunctional Proline Catabolic Enzyme Reveals New Inhibitor Templates for Proline Dehydrogenase and L-Glutamate-gamma-semialdehyde Dehydrogenase.
;
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.3390/molecules29225408 
_citation.pdbx_database_id_PubMed   39598797 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Meeks, K.R.'  1 ? 
primary 'Bogner, A.N.' 2 ? 
primary 'Nix, J.C.'    3 ? 
primary 'Tanner, J.J.' 4 ? 
# 
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 'Bifunctional protein PutA'   131961.656 2    1.5.5.2,1.2.1.88 ? ? ? 
2 non-polymer syn 'TRIETHYLENE GLYCOL'          150.173    2    ?                ? ? ? 
3 non-polymer syn 'DI(HYDROXYETHYL)ETHER'       106.120    8    ?                ? ? ? 
4 non-polymer syn 2-PYRIDINETHIOL               111.165    2    ?                ? ? ? 
5 non-polymer syn 'FORMIC ACID'                 46.025     3    ?                ? ? ? 
6 non-polymer syn 'SULFATE ION'                 96.063     6    ?                ? ? ? 
7 non-polymer syn 'FLAVIN-ADENINE DINUCLEOTIDE' 785.550    2    ?                ? ? ? 
8 water       nat water                         18.015     1393 ?                ? ? ? 
# 
_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       
;SMMSPNPLQKPAIDAAPAPFADFAPPVRPQSTLRRAITAAYRRPETECLPPLVEAATQSKEIRDAAASTARKLIEALRGK
HSGSGVEGLVQEYSLSSQEGVALMCLAEALLRIPDTATRDALIRDKIADGNWKSHLGGSRSLFVNAATWGLVVTGKLTST
VNDRSLAAALTRLISRCGEPVIRRGVDMAMRMMGEQFVTGETIREALKRSKELEEKGFSYSYDMLGEAATTAADAERYYR
DYESAIHAIGKASAGRGIYEGPGISIKLSALHPRYSRAQAARVMGELLPRVKALALLAKNYDIGLNIDAEEADRLELSLD
LLEVLCLDGDLSGWNGMGFVVQAYGKRCPFVLDFIIDLARRSGRRIMVRLVKGAYWDAEIKRAQLDGLADFPVFTRKIHT
DVSYIACAAKLLAATDVVFPQFATHNAQTLAAIYHMAGKDFHVGKYEFQCLHGMGEPLYEEVVGRGKLDRPCRIYAPVGT
HETLLAYLVRRLLENGANSSFVHRINDPKVSIDELIADPVEVVRAMPVVGAKHDRIALPAELFGDARTNSAGLDLSNEET
LASLTEALRESAAMKWTALPQLATGPAAGETRTVLNPGDHRDVVGSVTETSEEDARRAVRLAADAAPDWAAVPPSERAAC
LDRAAELMQARMPTLLGLIIREAGKSALNAIAEVREAIDFLRYYAEQTRRTLGPGHGPLGPIVCISPWNFPLAIFTGQIA
AALVAGNPVLAKPAEETPLIAAEGVRILREAGIPASALQLLPGDGRVGAALVAAAETAGVMFTGSTEVARLIQAQLADRL
SPAGRPIPLIAETGGQNAMIVDSSALAEQVVGDVITSAFDSAGQRCSALRVLCLQEDVADRILTMLKGALHELHIGRTDR
LSVDVGPVITSEAKDNIEKHIERMRGLGRKVEQIGLASETGVGTFVPPTIIELEKLSDLQREVFGPVLHVIRYRRDDLDR
LVDDVNATGYGLTFGLHTRLDETIAHVTSRIKAGNLYINRNIIGAVVGVQPFGGRGLSGTGPKAGGPLYLGRLVTTAPVP
PQHSSVHTDPVLLDFAKWLDGKGARAEAEAARNAGSSSALGLDLELPGPVGERNLYTLHARGRILLVPATESGLYHQLAA
ALATGNSVAIDAASGLQASLKNLPQTVGLRVSWSKDWAADGPFAGALVEGDAERIRAVNKAIAALPGPLLLVQAASSGEI
ARNPDAYCLNWLVEEVSASINTAAAGGNASLMAIG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMMSPNPLQKPAIDAAPAPFADFAPPVRPQSTLRRAITAAYRRPETECLPPLVEAATQSKEIRDAAASTARKLIEALRGK
HSGSGVEGLVQEYSLSSQEGVALMCLAEALLRIPDTATRDALIRDKIADGNWKSHLGGSRSLFVNAATWGLVVTGKLTST
VNDRSLAAALTRLISRCGEPVIRRGVDMAMRMMGEQFVTGETIREALKRSKELEEKGFSYSYDMLGEAATTAADAERYYR
DYESAIHAIGKASAGRGIYEGPGISIKLSALHPRYSRAQAARVMGELLPRVKALALLAKNYDIGLNIDAEEADRLELSLD
LLEVLCLDGDLSGWNGMGFVVQAYGKRCPFVLDFIIDLARRSGRRIMVRLVKGAYWDAEIKRAQLDGLADFPVFTRKIHT
DVSYIACAAKLLAATDVVFPQFATHNAQTLAAIYHMAGKDFHVGKYEFQCLHGMGEPLYEEVVGRGKLDRPCRIYAPVGT
HETLLAYLVRRLLENGANSSFVHRINDPKVSIDELIADPVEVVRAMPVVGAKHDRIALPAELFGDARTNSAGLDLSNEET
LASLTEALRESAAMKWTALPQLATGPAAGETRTVLNPGDHRDVVGSVTETSEEDARRAVRLAADAAPDWAAVPPSERAAC
LDRAAELMQARMPTLLGLIIREAGKSALNAIAEVREAIDFLRYYAEQTRRTLGPGHGPLGPIVCISPWNFPLAIFTGQIA
AALVAGNPVLAKPAEETPLIAAEGVRILREAGIPASALQLLPGDGRVGAALVAAAETAGVMFTGSTEVARLIQAQLADRL
SPAGRPIPLIAETGGQNAMIVDSSALAEQVVGDVITSAFDSAGQRCSALRVLCLQEDVADRILTMLKGALHELHIGRTDR
LSVDVGPVITSEAKDNIEKHIERMRGLGRKVEQIGLASETGVGTFVPPTIIELEKLSDLQREVFGPVLHVIRYRRDDLDR
LVDDVNATGYGLTFGLHTRLDETIAHVTSRIKAGNLYINRNIIGAVVGVQPFGGRGLSGTGPKAGGPLYLGRLVTTAPVP
PQHSSVHTDPVLLDFAKWLDGKGARAEAEAARNAGSSSALGLDLELPGPVGERNLYTLHARGRILLVPATESGLYHQLAA
ALATGNSVAIDAASGLQASLKNLPQTVGLRVSWSKDWAADGPFAGALVEGDAERIRAVNKAIAALPGPLLLVQAASSGEI
ARNPDAYCLNWLVEEVSASINTAAAGGNASLMAIG
;
_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 
2 'TRIETHYLENE GLYCOL'          PGE 
3 'DI(HYDROXYETHYL)ETHER'       PEG 
4 2-PYRIDINETHIOL               PYS 
5 'FORMIC ACID'                 FMT 
6 'SULFATE ION'                 SO4 
7 'FLAVIN-ADENINE DINUCLEOTIDE' FAD 
8 water                         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1    SER n 
1 2    MET n 
1 3    MET n 
1 4    SER n 
1 5    PRO n 
1 6    ASN n 
1 7    PRO n 
1 8    LEU n 
1 9    GLN n 
1 10   LYS n 
1 11   PRO n 
1 12   ALA n 
1 13   ILE n 
1 14   ASP n 
1 15   ALA n 
1 16   ALA n 
1 17   PRO n 
1 18   ALA n 
1 19   PRO n 
1 20   PHE n 
1 21   ALA n 
1 22   ASP n 
1 23   PHE n 
1 24   ALA n 
1 25   PRO n 
1 26   PRO n 
1 27   VAL n 
1 28   ARG n 
1 29   PRO n 
1 30   GLN n 
1 31   SER n 
1 32   THR n 
1 33   LEU n 
1 34   ARG n 
1 35   ARG n 
1 36   ALA n 
1 37   ILE n 
1 38   THR n 
1 39   ALA n 
1 40   ALA n 
1 41   TYR n 
1 42   ARG n 
1 43   ARG n 
1 44   PRO n 
1 45   GLU n 
1 46   THR n 
1 47   GLU n 
1 48   CYS n 
1 49   LEU n 
1 50   PRO n 
1 51   PRO n 
1 52   LEU n 
1 53   VAL n 
1 54   GLU n 
1 55   ALA n 
1 56   ALA n 
1 57   THR n 
1 58   GLN n 
1 59   SER n 
1 60   LYS n 
1 61   GLU n 
1 62   ILE n 
1 63   ARG n 
1 64   ASP n 
1 65   ALA n 
1 66   ALA n 
1 67   ALA n 
1 68   SER n 
1 69   THR n 
1 70   ALA n 
1 71   ARG n 
1 72   LYS n 
1 73   LEU n 
1 74   ILE n 
1 75   GLU n 
1 76   ALA n 
1 77   LEU n 
1 78   ARG n 
1 79   GLY n 
1 80   LYS n 
1 81   HIS n 
1 82   SER n 
1 83   GLY n 
1 84   SER n 
1 85   GLY n 
1 86   VAL n 
1 87   GLU n 
1 88   GLY n 
1 89   LEU n 
1 90   VAL n 
1 91   GLN n 
1 92   GLU n 
1 93   TYR n 
1 94   SER n 
1 95   LEU n 
1 96   SER n 
1 97   SER n 
1 98   GLN n 
1 99   GLU n 
1 100  GLY n 
1 101  VAL n 
1 102  ALA n 
1 103  LEU n 
1 104  MET n 
1 105  CYS n 
1 106  LEU n 
1 107  ALA n 
1 108  GLU n 
1 109  ALA n 
1 110  LEU n 
1 111  LEU n 
1 112  ARG n 
1 113  ILE n 
1 114  PRO n 
1 115  ASP n 
1 116  THR n 
1 117  ALA n 
1 118  THR n 
1 119  ARG n 
1 120  ASP n 
1 121  ALA n 
1 122  LEU n 
1 123  ILE n 
1 124  ARG n 
1 125  ASP n 
1 126  LYS n 
1 127  ILE n 
1 128  ALA n 
1 129  ASP n 
1 130  GLY n 
1 131  ASN n 
1 132  TRP n 
1 133  LYS n 
1 134  SER n 
1 135  HIS n 
1 136  LEU n 
1 137  GLY n 
1 138  GLY n 
1 139  SER n 
1 140  ARG n 
1 141  SER n 
1 142  LEU n 
1 143  PHE n 
1 144  VAL n 
1 145  ASN n 
1 146  ALA n 
1 147  ALA n 
1 148  THR n 
1 149  TRP n 
1 150  GLY n 
1 151  LEU n 
1 152  VAL n 
1 153  VAL n 
1 154  THR n 
1 155  GLY n 
1 156  LYS n 
1 157  LEU n 
1 158  THR n 
1 159  SER n 
1 160  THR n 
1 161  VAL n 
1 162  ASN n 
1 163  ASP n 
1 164  ARG n 
1 165  SER n 
1 166  LEU n 
1 167  ALA n 
1 168  ALA n 
1 169  ALA n 
1 170  LEU n 
1 171  THR n 
1 172  ARG n 
1 173  LEU n 
1 174  ILE n 
1 175  SER n 
1 176  ARG n 
1 177  CYS n 
1 178  GLY n 
1 179  GLU n 
1 180  PRO n 
1 181  VAL n 
1 182  ILE n 
1 183  ARG n 
1 184  ARG n 
1 185  GLY n 
1 186  VAL n 
1 187  ASP n 
1 188  MET n 
1 189  ALA n 
1 190  MET n 
1 191  ARG n 
1 192  MET n 
1 193  MET n 
1 194  GLY n 
1 195  GLU n 
1 196  GLN n 
1 197  PHE n 
1 198  VAL n 
1 199  THR n 
1 200  GLY n 
1 201  GLU n 
1 202  THR n 
1 203  ILE n 
1 204  ARG n 
1 205  GLU n 
1 206  ALA n 
1 207  LEU n 
1 208  LYS n 
1 209  ARG n 
1 210  SER n 
1 211  LYS n 
1 212  GLU n 
1 213  LEU n 
1 214  GLU n 
1 215  GLU n 
1 216  LYS n 
1 217  GLY n 
1 218  PHE n 
1 219  SER n 
1 220  TYR n 
1 221  SER n 
1 222  TYR n 
1 223  ASP n 
1 224  MET n 
1 225  LEU n 
1 226  GLY n 
1 227  GLU n 
1 228  ALA n 
1 229  ALA n 
1 230  THR n 
1 231  THR n 
1 232  ALA n 
1 233  ALA n 
1 234  ASP n 
1 235  ALA n 
1 236  GLU n 
1 237  ARG n 
1 238  TYR n 
1 239  TYR n 
1 240  ARG n 
1 241  ASP n 
1 242  TYR n 
1 243  GLU n 
1 244  SER n 
1 245  ALA n 
1 246  ILE n 
1 247  HIS n 
1 248  ALA n 
1 249  ILE n 
1 250  GLY n 
1 251  LYS n 
1 252  ALA n 
1 253  SER n 
1 254  ALA n 
1 255  GLY n 
1 256  ARG n 
1 257  GLY n 
1 258  ILE n 
1 259  TYR n 
1 260  GLU n 
1 261  GLY n 
1 262  PRO n 
1 263  GLY n 
1 264  ILE n 
1 265  SER n 
1 266  ILE n 
1 267  LYS n 
1 268  LEU n 
1 269  SER n 
1 270  ALA n 
1 271  LEU n 
1 272  HIS n 
1 273  PRO n 
1 274  ARG n 
1 275  TYR n 
1 276  SER n 
1 277  ARG n 
1 278  ALA n 
1 279  GLN n 
1 280  ALA n 
1 281  ALA n 
1 282  ARG n 
1 283  VAL n 
1 284  MET n 
1 285  GLY n 
1 286  GLU n 
1 287  LEU n 
1 288  LEU n 
1 289  PRO n 
1 290  ARG n 
1 291  VAL n 
1 292  LYS n 
1 293  ALA n 
1 294  LEU n 
1 295  ALA n 
1 296  LEU n 
1 297  LEU n 
1 298  ALA n 
1 299  LYS n 
1 300  ASN n 
1 301  TYR n 
1 302  ASP n 
1 303  ILE n 
1 304  GLY n 
1 305  LEU n 
1 306  ASN n 
1 307  ILE n 
1 308  ASP n 
1 309  ALA n 
1 310  GLU n 
1 311  GLU n 
1 312  ALA n 
1 313  ASP n 
1 314  ARG n 
1 315  LEU n 
1 316  GLU n 
1 317  LEU n 
1 318  SER n 
1 319  LEU n 
1 320  ASP n 
1 321  LEU n 
1 322  LEU n 
1 323  GLU n 
1 324  VAL n 
1 325  LEU n 
1 326  CYS n 
1 327  LEU n 
1 328  ASP n 
1 329  GLY n 
1 330  ASP n 
1 331  LEU n 
1 332  SER n 
1 333  GLY n 
1 334  TRP n 
1 335  ASN n 
1 336  GLY n 
1 337  MET n 
1 338  GLY n 
1 339  PHE n 
1 340  VAL n 
1 341  VAL n 
1 342  GLN n 
1 343  ALA n 
1 344  TYR n 
1 345  GLY n 
1 346  LYS n 
1 347  ARG n 
1 348  CYS n 
1 349  PRO n 
1 350  PHE n 
1 351  VAL n 
1 352  LEU n 
1 353  ASP n 
1 354  PHE n 
1 355  ILE n 
1 356  ILE n 
1 357  ASP n 
1 358  LEU n 
1 359  ALA n 
1 360  ARG n 
1 361  ARG n 
1 362  SER n 
1 363  GLY n 
1 364  ARG n 
1 365  ARG n 
1 366  ILE n 
1 367  MET n 
1 368  VAL n 
1 369  ARG n 
1 370  LEU n 
1 371  VAL n 
1 372  LYS n 
1 373  GLY n 
1 374  ALA n 
1 375  TYR n 
1 376  TRP n 
1 377  ASP n 
1 378  ALA n 
1 379  GLU n 
1 380  ILE n 
1 381  LYS n 
1 382  ARG n 
1 383  ALA n 
1 384  GLN n 
1 385  LEU n 
1 386  ASP n 
1 387  GLY n 
1 388  LEU n 
1 389  ALA n 
1 390  ASP n 
1 391  PHE n 
1 392  PRO n 
1 393  VAL n 
1 394  PHE n 
1 395  THR n 
1 396  ARG n 
1 397  LYS n 
1 398  ILE n 
1 399  HIS n 
1 400  THR n 
1 401  ASP n 
1 402  VAL n 
1 403  SER n 
1 404  TYR n 
1 405  ILE n 
1 406  ALA n 
1 407  CYS n 
1 408  ALA n 
1 409  ALA n 
1 410  LYS n 
1 411  LEU n 
1 412  LEU n 
1 413  ALA n 
1 414  ALA n 
1 415  THR n 
1 416  ASP n 
1 417  VAL n 
1 418  VAL n 
1 419  PHE n 
1 420  PRO n 
1 421  GLN n 
1 422  PHE n 
1 423  ALA n 
1 424  THR n 
1 425  HIS n 
1 426  ASN n 
1 427  ALA n 
1 428  GLN n 
1 429  THR n 
1 430  LEU n 
1 431  ALA n 
1 432  ALA n 
1 433  ILE n 
1 434  TYR n 
1 435  HIS n 
1 436  MET n 
1 437  ALA n 
1 438  GLY n 
1 439  LYS n 
1 440  ASP n 
1 441  PHE n 
1 442  HIS n 
1 443  VAL n 
1 444  GLY n 
1 445  LYS n 
1 446  TYR n 
1 447  GLU n 
1 448  PHE n 
1 449  GLN n 
1 450  CYS n 
1 451  LEU n 
1 452  HIS n 
1 453  GLY n 
1 454  MET n 
1 455  GLY n 
1 456  GLU n 
1 457  PRO n 
1 458  LEU n 
1 459  TYR n 
1 460  GLU n 
1 461  GLU n 
1 462  VAL n 
1 463  VAL n 
1 464  GLY n 
1 465  ARG n 
1 466  GLY n 
1 467  LYS n 
1 468  LEU n 
1 469  ASP n 
1 470  ARG n 
1 471  PRO n 
1 472  CYS n 
1 473  ARG n 
1 474  ILE n 
1 475  TYR n 
1 476  ALA n 
1 477  PRO n 
1 478  VAL n 
1 479  GLY n 
1 480  THR n 
1 481  HIS n 
1 482  GLU n 
1 483  THR n 
1 484  LEU n 
1 485  LEU n 
1 486  ALA n 
1 487  TYR n 
1 488  LEU n 
1 489  VAL n 
1 490  ARG n 
1 491  ARG n 
1 492  LEU n 
1 493  LEU n 
1 494  GLU n 
1 495  ASN n 
1 496  GLY n 
1 497  ALA n 
1 498  ASN n 
1 499  SER n 
1 500  SER n 
1 501  PHE n 
1 502  VAL n 
1 503  HIS n 
1 504  ARG n 
1 505  ILE n 
1 506  ASN n 
1 507  ASP n 
1 508  PRO n 
1 509  LYS n 
1 510  VAL n 
1 511  SER n 
1 512  ILE n 
1 513  ASP n 
1 514  GLU n 
1 515  LEU n 
1 516  ILE n 
1 517  ALA n 
1 518  ASP n 
1 519  PRO n 
1 520  VAL n 
1 521  GLU n 
1 522  VAL n 
1 523  VAL n 
1 524  ARG n 
1 525  ALA n 
1 526  MET n 
1 527  PRO n 
1 528  VAL n 
1 529  VAL n 
1 530  GLY n 
1 531  ALA n 
1 532  LYS n 
1 533  HIS n 
1 534  ASP n 
1 535  ARG n 
1 536  ILE n 
1 537  ALA n 
1 538  LEU n 
1 539  PRO n 
1 540  ALA n 
1 541  GLU n 
1 542  LEU n 
1 543  PHE n 
1 544  GLY n 
1 545  ASP n 
1 546  ALA n 
1 547  ARG n 
1 548  THR n 
1 549  ASN n 
1 550  SER n 
1 551  ALA n 
1 552  GLY n 
1 553  LEU n 
1 554  ASP n 
1 555  LEU n 
1 556  SER n 
1 557  ASN n 
1 558  GLU n 
1 559  GLU n 
1 560  THR n 
1 561  LEU n 
1 562  ALA n 
1 563  SER n 
1 564  LEU n 
1 565  THR n 
1 566  GLU n 
1 567  ALA n 
1 568  LEU n 
1 569  ARG n 
1 570  GLU n 
1 571  SER n 
1 572  ALA n 
1 573  ALA n 
1 574  MET n 
1 575  LYS n 
1 576  TRP n 
1 577  THR n 
1 578  ALA n 
1 579  LEU n 
1 580  PRO n 
1 581  GLN n 
1 582  LEU n 
1 583  ALA n 
1 584  THR n 
1 585  GLY n 
1 586  PRO n 
1 587  ALA n 
1 588  ALA n 
1 589  GLY n 
1 590  GLU n 
1 591  THR n 
1 592  ARG n 
1 593  THR n 
1 594  VAL n 
1 595  LEU n 
1 596  ASN n 
1 597  PRO n 
1 598  GLY n 
1 599  ASP n 
1 600  HIS n 
1 601  ARG n 
1 602  ASP n 
1 603  VAL n 
1 604  VAL n 
1 605  GLY n 
1 606  SER n 
1 607  VAL n 
1 608  THR n 
1 609  GLU n 
1 610  THR n 
1 611  SER n 
1 612  GLU n 
1 613  GLU n 
1 614  ASP n 
1 615  ALA n 
1 616  ARG n 
1 617  ARG n 
1 618  ALA n 
1 619  VAL n 
1 620  ARG n 
1 621  LEU n 
1 622  ALA n 
1 623  ALA n 
1 624  ASP n 
1 625  ALA n 
1 626  ALA n 
1 627  PRO n 
1 628  ASP n 
1 629  TRP n 
1 630  ALA n 
1 631  ALA n 
1 632  VAL n 
1 633  PRO n 
1 634  PRO n 
1 635  SER n 
1 636  GLU n 
1 637  ARG n 
1 638  ALA n 
1 639  ALA n 
1 640  CYS n 
1 641  LEU n 
1 642  ASP n 
1 643  ARG n 
1 644  ALA n 
1 645  ALA n 
1 646  GLU n 
1 647  LEU n 
1 648  MET n 
1 649  GLN n 
1 650  ALA n 
1 651  ARG n 
1 652  MET n 
1 653  PRO n 
1 654  THR n 
1 655  LEU n 
1 656  LEU n 
1 657  GLY n 
1 658  LEU n 
1 659  ILE n 
1 660  ILE n 
1 661  ARG n 
1 662  GLU n 
1 663  ALA n 
1 664  GLY n 
1 665  LYS n 
1 666  SER n 
1 667  ALA n 
1 668  LEU n 
1 669  ASN n 
1 670  ALA n 
1 671  ILE n 
1 672  ALA n 
1 673  GLU n 
1 674  VAL n 
1 675  ARG n 
1 676  GLU n 
1 677  ALA n 
1 678  ILE n 
1 679  ASP n 
1 680  PHE n 
1 681  LEU n 
1 682  ARG n 
1 683  TYR n 
1 684  TYR n 
1 685  ALA n 
1 686  GLU n 
1 687  GLN n 
1 688  THR n 
1 689  ARG n 
1 690  ARG n 
1 691  THR n 
1 692  LEU n 
1 693  GLY n 
1 694  PRO n 
1 695  GLY n 
1 696  HIS n 
1 697  GLY n 
1 698  PRO n 
1 699  LEU n 
1 700  GLY n 
1 701  PRO n 
1 702  ILE n 
1 703  VAL n 
1 704  CYS n 
1 705  ILE n 
1 706  SER n 
1 707  PRO n 
1 708  TRP n 
1 709  ASN n 
1 710  PHE n 
1 711  PRO n 
1 712  LEU n 
1 713  ALA n 
1 714  ILE n 
1 715  PHE n 
1 716  THR n 
1 717  GLY n 
1 718  GLN n 
1 719  ILE n 
1 720  ALA n 
1 721  ALA n 
1 722  ALA n 
1 723  LEU n 
1 724  VAL n 
1 725  ALA n 
1 726  GLY n 
1 727  ASN n 
1 728  PRO n 
1 729  VAL n 
1 730  LEU n 
1 731  ALA n 
1 732  LYS n 
1 733  PRO n 
1 734  ALA n 
1 735  GLU n 
1 736  GLU n 
1 737  THR n 
1 738  PRO n 
1 739  LEU n 
1 740  ILE n 
1 741  ALA n 
1 742  ALA n 
1 743  GLU n 
1 744  GLY n 
1 745  VAL n 
1 746  ARG n 
1 747  ILE n 
1 748  LEU n 
1 749  ARG n 
1 750  GLU n 
1 751  ALA n 
1 752  GLY n 
1 753  ILE n 
1 754  PRO n 
1 755  ALA n 
1 756  SER n 
1 757  ALA n 
1 758  LEU n 
1 759  GLN n 
1 760  LEU n 
1 761  LEU n 
1 762  PRO n 
1 763  GLY n 
1 764  ASP n 
1 765  GLY n 
1 766  ARG n 
1 767  VAL n 
1 768  GLY n 
1 769  ALA n 
1 770  ALA n 
1 771  LEU n 
1 772  VAL n 
1 773  ALA n 
1 774  ALA n 
1 775  ALA n 
1 776  GLU n 
1 777  THR n 
1 778  ALA n 
1 779  GLY n 
1 780  VAL n 
1 781  MET n 
1 782  PHE n 
1 783  THR n 
1 784  GLY n 
1 785  SER n 
1 786  THR n 
1 787  GLU n 
1 788  VAL n 
1 789  ALA n 
1 790  ARG n 
1 791  LEU n 
1 792  ILE n 
1 793  GLN n 
1 794  ALA n 
1 795  GLN n 
1 796  LEU n 
1 797  ALA n 
1 798  ASP n 
1 799  ARG n 
1 800  LEU n 
1 801  SER n 
1 802  PRO n 
1 803  ALA n 
1 804  GLY n 
1 805  ARG n 
1 806  PRO n 
1 807  ILE n 
1 808  PRO n 
1 809  LEU n 
1 810  ILE n 
1 811  ALA n 
1 812  GLU n 
1 813  THR n 
1 814  GLY n 
1 815  GLY n 
1 816  GLN n 
1 817  ASN n 
1 818  ALA n 
1 819  MET n 
1 820  ILE n 
1 821  VAL n 
1 822  ASP n 
1 823  SER n 
1 824  SER n 
1 825  ALA n 
1 826  LEU n 
1 827  ALA n 
1 828  GLU n 
1 829  GLN n 
1 830  VAL n 
1 831  VAL n 
1 832  GLY n 
1 833  ASP n 
1 834  VAL n 
1 835  ILE n 
1 836  THR n 
1 837  SER n 
1 838  ALA n 
1 839  PHE n 
1 840  ASP n 
1 841  SER n 
1 842  ALA n 
1 843  GLY n 
1 844  GLN n 
1 845  ARG n 
1 846  CYS n 
1 847  SER n 
1 848  ALA n 
1 849  LEU n 
1 850  ARG n 
1 851  VAL n 
1 852  LEU n 
1 853  CYS n 
1 854  LEU n 
1 855  GLN n 
1 856  GLU n 
1 857  ASP n 
1 858  VAL n 
1 859  ALA n 
1 860  ASP n 
1 861  ARG n 
1 862  ILE n 
1 863  LEU n 
1 864  THR n 
1 865  MET n 
1 866  LEU n 
1 867  LYS n 
1 868  GLY n 
1 869  ALA n 
1 870  LEU n 
1 871  HIS n 
1 872  GLU n 
1 873  LEU n 
1 874  HIS n 
1 875  ILE n 
1 876  GLY n 
1 877  ARG n 
1 878  THR n 
1 879  ASP n 
1 880  ARG n 
1 881  LEU n 
1 882  SER n 
1 883  VAL n 
1 884  ASP n 
1 885  VAL n 
1 886  GLY n 
1 887  PRO n 
1 888  VAL n 
1 889  ILE n 
1 890  THR n 
1 891  SER n 
1 892  GLU n 
1 893  ALA n 
1 894  LYS n 
1 895  ASP n 
1 896  ASN n 
1 897  ILE n 
1 898  GLU n 
1 899  LYS n 
1 900  HIS n 
1 901  ILE n 
1 902  GLU n 
1 903  ARG n 
1 904  MET n 
1 905  ARG n 
1 906  GLY n 
1 907  LEU n 
1 908  GLY n 
1 909  ARG n 
1 910  LYS n 
1 911  VAL n 
1 912  GLU n 
1 913  GLN n 
1 914  ILE n 
1 915  GLY n 
1 916  LEU n 
1 917  ALA n 
1 918  SER n 
1 919  GLU n 
1 920  THR n 
1 921  GLY n 
1 922  VAL n 
1 923  GLY n 
1 924  THR n 
1 925  PHE n 
1 926  VAL n 
1 927  PRO n 
1 928  PRO n 
1 929  THR n 
1 930  ILE n 
1 931  ILE n 
1 932  GLU n 
1 933  LEU n 
1 934  GLU n 
1 935  LYS n 
1 936  LEU n 
1 937  SER n 
1 938  ASP n 
1 939  LEU n 
1 940  GLN n 
1 941  ARG n 
1 942  GLU n 
1 943  VAL n 
1 944  PHE n 
1 945  GLY n 
1 946  PRO n 
1 947  VAL n 
1 948  LEU n 
1 949  HIS n 
1 950  VAL n 
1 951  ILE n 
1 952  ARG n 
1 953  TYR n 
1 954  ARG n 
1 955  ARG n 
1 956  ASP n 
1 957  ASP n 
1 958  LEU n 
1 959  ASP n 
1 960  ARG n 
1 961  LEU n 
1 962  VAL n 
1 963  ASP n 
1 964  ASP n 
1 965  VAL n 
1 966  ASN n 
1 967  ALA n 
1 968  THR n 
1 969  GLY n 
1 970  TYR n 
1 971  GLY n 
1 972  LEU n 
1 973  THR n 
1 974  PHE n 
1 975  GLY n 
1 976  LEU n 
1 977  HIS n 
1 978  THR n 
1 979  ARG n 
1 980  LEU n 
1 981  ASP n 
1 982  GLU n 
1 983  THR n 
1 984  ILE n 
1 985  ALA n 
1 986  HIS n 
1 987  VAL n 
1 988  THR n 
1 989  SER n 
1 990  ARG n 
1 991  ILE n 
1 992  LYS n 
1 993  ALA n 
1 994  GLY n 
1 995  ASN n 
1 996  LEU n 
1 997  TYR n 
1 998  ILE n 
1 999  ASN n 
1 1000 ARG n 
1 1001 ASN n 
1 1002 ILE n 
1 1003 ILE n 
1 1004 GLY n 
1 1005 ALA n 
1 1006 VAL n 
1 1007 VAL n 
1 1008 GLY n 
1 1009 VAL n 
1 1010 GLN n 
1 1011 PRO n 
1 1012 PHE n 
1 1013 GLY n 
1 1014 GLY n 
1 1015 ARG n 
1 1016 GLY n 
1 1017 LEU n 
1 1018 SER n 
1 1019 GLY n 
1 1020 THR n 
1 1021 GLY n 
1 1022 PRO n 
1 1023 LYS n 
1 1024 ALA n 
1 1025 GLY n 
1 1026 GLY n 
1 1027 PRO n 
1 1028 LEU n 
1 1029 TYR n 
1 1030 LEU n 
1 1031 GLY n 
1 1032 ARG n 
1 1033 LEU n 
1 1034 VAL n 
1 1035 THR n 
1 1036 THR n 
1 1037 ALA n 
1 1038 PRO n 
1 1039 VAL n 
1 1040 PRO n 
1 1041 PRO n 
1 1042 GLN n 
1 1043 HIS n 
1 1044 SER n 
1 1045 SER n 
1 1046 VAL n 
1 1047 HIS n 
1 1048 THR n 
1 1049 ASP n 
1 1050 PRO n 
1 1051 VAL n 
1 1052 LEU n 
1 1053 LEU n 
1 1054 ASP n 
1 1055 PHE n 
1 1056 ALA n 
1 1057 LYS n 
1 1058 TRP n 
1 1059 LEU n 
1 1060 ASP n 
1 1061 GLY n 
1 1062 LYS n 
1 1063 GLY n 
1 1064 ALA n 
1 1065 ARG n 
1 1066 ALA n 
1 1067 GLU n 
1 1068 ALA n 
1 1069 GLU n 
1 1070 ALA n 
1 1071 ALA n 
1 1072 ARG n 
1 1073 ASN n 
1 1074 ALA n 
1 1075 GLY n 
1 1076 SER n 
1 1077 SER n 
1 1078 SER n 
1 1079 ALA n 
1 1080 LEU n 
1 1081 GLY n 
1 1082 LEU n 
1 1083 ASP n 
1 1084 LEU n 
1 1085 GLU n 
1 1086 LEU n 
1 1087 PRO n 
1 1088 GLY n 
1 1089 PRO n 
1 1090 VAL n 
1 1091 GLY n 
1 1092 GLU n 
1 1093 ARG n 
1 1094 ASN n 
1 1095 LEU n 
1 1096 TYR n 
1 1097 THR n 
1 1098 LEU n 
1 1099 HIS n 
1 1100 ALA n 
1 1101 ARG n 
1 1102 GLY n 
1 1103 ARG n 
1 1104 ILE n 
1 1105 LEU n 
1 1106 LEU n 
1 1107 VAL n 
1 1108 PRO n 
1 1109 ALA n 
1 1110 THR n 
1 1111 GLU n 
1 1112 SER n 
1 1113 GLY n 
1 1114 LEU n 
1 1115 TYR n 
1 1116 HIS n 
1 1117 GLN n 
1 1118 LEU n 
1 1119 ALA n 
1 1120 ALA n 
1 1121 ALA n 
1 1122 LEU n 
1 1123 ALA n 
1 1124 THR n 
1 1125 GLY n 
1 1126 ASN n 
1 1127 SER n 
1 1128 VAL n 
1 1129 ALA n 
1 1130 ILE n 
1 1131 ASP n 
1 1132 ALA n 
1 1133 ALA n 
1 1134 SER n 
1 1135 GLY n 
1 1136 LEU n 
1 1137 GLN n 
1 1138 ALA n 
1 1139 SER n 
1 1140 LEU n 
1 1141 LYS n 
1 1142 ASN n 
1 1143 LEU n 
1 1144 PRO n 
1 1145 GLN n 
1 1146 THR n 
1 1147 VAL n 
1 1148 GLY n 
1 1149 LEU n 
1 1150 ARG n 
1 1151 VAL n 
1 1152 SER n 
1 1153 TRP n 
1 1154 SER n 
1 1155 LYS n 
1 1156 ASP n 
1 1157 TRP n 
1 1158 ALA n 
1 1159 ALA n 
1 1160 ASP n 
1 1161 GLY n 
1 1162 PRO n 
1 1163 PHE n 
1 1164 ALA n 
1 1165 GLY n 
1 1166 ALA n 
1 1167 LEU n 
1 1168 VAL n 
1 1169 GLU n 
1 1170 GLY n 
1 1171 ASP n 
1 1172 ALA n 
1 1173 GLU n 
1 1174 ARG n 
1 1175 ILE n 
1 1176 ARG n 
1 1177 ALA n 
1 1178 VAL n 
1 1179 ASN n 
1 1180 LYS n 
1 1181 ALA n 
1 1182 ILE n 
1 1183 ALA n 
1 1184 ALA n 
1 1185 LEU n 
1 1186 PRO n 
1 1187 GLY n 
1 1188 PRO n 
1 1189 LEU n 
1 1190 LEU n 
1 1191 LEU n 
1 1192 VAL n 
1 1193 GLN n 
1 1194 ALA n 
1 1195 ALA n 
1 1196 SER n 
1 1197 SER n 
1 1198 GLY n 
1 1199 GLU n 
1 1200 ILE n 
1 1201 ALA n 
1 1202 ARG n 
1 1203 ASN n 
1 1204 PRO n 
1 1205 ASP n 
1 1206 ALA n 
1 1207 TYR n 
1 1208 CYS n 
1 1209 LEU n 
1 1210 ASN n 
1 1211 TRP n 
1 1212 LEU n 
1 1213 VAL n 
1 1214 GLU n 
1 1215 GLU n 
1 1216 VAL n 
1 1217 SER n 
1 1218 ALA n 
1 1219 SER n 
1 1220 ILE n 
1 1221 ASN n 
1 1222 THR n 
1 1223 ALA n 
1 1224 ALA n 
1 1225 ALA n 
1 1226 GLY n 
1 1227 GLY n 
1 1228 ASN n 
1 1229 ALA n 
1 1230 SER n 
1 1231 LEU n 
1 1232 MET n 
1 1233 ALA n 
1 1234 ILE n 
1 1235 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                   1235 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'putA, SM11_chr0102' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    SM11 
_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      'Sinorhizobium meliloti' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     707241 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_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                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                       ? 'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE                      ? 'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                    ? 'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'               ? 'C4 H7 N O4'        133.103 
CYS 'L-peptide linking' y CYSTEINE                      ? 'C3 H7 N O2 S'      121.158 
FAD non-polymer         . 'FLAVIN-ADENINE DINUCLEOTIDE' ? 'C27 H33 N9 O15 P2' 785.550 
FMT non-polymer         . 'FORMIC ACID'                 ? 'C H2 O2'           46.025  
GLN 'L-peptide linking' y GLUTAMINE                     ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'               ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                       ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                     ? 'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER                         ? 'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE                    ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                       ? 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                        ? 'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                    ? 'C5 H11 N O2 S'     149.211 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER'       ? 'C4 H10 O3'         106.120 
PGE non-polymer         . 'TRIETHYLENE GLYCOL'          ? 'C6 H14 O4'         150.173 
PHE 'L-peptide linking' y PHENYLALANINE                 ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                       ? 'C5 H9 N O2'        115.130 
PYS non-polymer         . 2-PYRIDINETHIOL               ? 'C5 H5 N S'         111.165 
SER 'L-peptide linking' y SERINE                        ? 'C3 H7 N O3'        105.093 
SO4 non-polymer         . 'SULFATE ION'                 ? 'O4 S -2'           96.063  
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_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    SER 1    -1   ?    ?   ?   A . n 
A 1 2    MET 2    0    ?    ?   ?   A . n 
A 1 3    MET 3    1    ?    ?   ?   A . n 
A 1 4    SER 4    2    ?    ?   ?   A . n 
A 1 5    PRO 5    3    ?    ?   ?   A . n 
A 1 6    ASN 6    4    ?    ?   ?   A . n 
A 1 7    PRO 7    5    ?    ?   ?   A . n 
A 1 8    LEU 8    6    ?    ?   ?   A . n 
A 1 9    GLN 9    7    ?    ?   ?   A . n 
A 1 10   LYS 10   8    ?    ?   ?   A . n 
A 1 11   PRO 11   9    ?    ?   ?   A . n 
A 1 12   ALA 12   10   ?    ?   ?   A . n 
A 1 13   ILE 13   11   ?    ?   ?   A . n 
A 1 14   ASP 14   12   ?    ?   ?   A . n 
A 1 15   ALA 15   13   ?    ?   ?   A . n 
A 1 16   ALA 16   14   ?    ?   ?   A . n 
A 1 17   PRO 17   15   15   PRO PRO A . n 
A 1 18   ALA 18   16   16   ALA ALA A . n 
A 1 19   PRO 19   17   17   PRO PRO A . n 
A 1 20   PHE 20   18   18   PHE PHE A . n 
A 1 21   ALA 21   19   19   ALA ALA A . n 
A 1 22   ASP 22   20   20   ASP ASP A . n 
A 1 23   PHE 23   21   21   PHE PHE A . n 
A 1 24   ALA 24   22   22   ALA ALA A . n 
A 1 25   PRO 25   23   23   PRO PRO A . n 
A 1 26   PRO 26   24   24   PRO PRO A . n 
A 1 27   VAL 27   25   25   VAL VAL A . n 
A 1 28   ARG 28   26   26   ARG ARG A . n 
A 1 29   PRO 29   27   27   PRO PRO A . n 
A 1 30   GLN 30   28   28   GLN GLN A . n 
A 1 31   SER 31   29   29   SER SER A . n 
A 1 32   THR 32   30   30   THR THR A . n 
A 1 33   LEU 33   31   31   LEU LEU A . n 
A 1 34   ARG 34   32   32   ARG ARG A . n 
A 1 35   ARG 35   33   33   ARG ARG A . n 
A 1 36   ALA 36   34   34   ALA ALA A . n 
A 1 37   ILE 37   35   35   ILE ILE A . n 
A 1 38   THR 38   36   36   THR THR A . n 
A 1 39   ALA 39   37   37   ALA ALA A . n 
A 1 40   ALA 40   38   38   ALA ALA A . n 
A 1 41   TYR 41   39   39   TYR TYR A . n 
A 1 42   ARG 42   40   40   ARG ARG A . n 
A 1 43   ARG 43   41   41   ARG ARG A . n 
A 1 44   PRO 44   42   42   PRO PRO A . n 
A 1 45   GLU 45   43   43   GLU GLU A . n 
A 1 46   THR 46   44   44   THR THR A . n 
A 1 47   GLU 47   45   45   GLU GLU A . n 
A 1 48   CYS 48   46   46   CYS CYS A . n 
A 1 49   LEU 49   47   47   LEU LEU A . n 
A 1 50   PRO 50   48   48   PRO PRO A . n 
A 1 51   PRO 51   49   49   PRO PRO A . n 
A 1 52   LEU 52   50   50   LEU LEU A . n 
A 1 53   VAL 53   51   51   VAL VAL A . n 
A 1 54   GLU 54   52   52   GLU GLU A . n 
A 1 55   ALA 55   53   53   ALA ALA A . n 
A 1 56   ALA 56   54   54   ALA ALA A . n 
A 1 57   THR 57   55   55   THR THR A . n 
A 1 58   GLN 58   56   56   GLN GLN A . n 
A 1 59   SER 59   57   57   SER SER A . n 
A 1 60   LYS 60   58   58   LYS LYS A . n 
A 1 61   GLU 61   59   59   GLU GLU A . n 
A 1 62   ILE 62   60   60   ILE ILE A . n 
A 1 63   ARG 63   61   61   ARG ARG A . n 
A 1 64   ASP 64   62   62   ASP ASP A . n 
A 1 65   ALA 65   63   63   ALA ALA A . n 
A 1 66   ALA 66   64   64   ALA ALA A . n 
A 1 67   ALA 67   65   65   ALA ALA A . n 
A 1 68   SER 68   66   66   SER SER A . n 
A 1 69   THR 69   67   67   THR THR A . n 
A 1 70   ALA 70   68   68   ALA ALA A . n 
A 1 71   ARG 71   69   69   ARG ARG A . n 
A 1 72   LYS 72   70   70   LYS LYS A . n 
A 1 73   LEU 73   71   71   LEU LEU A . n 
A 1 74   ILE 74   72   72   ILE ILE A . n 
A 1 75   GLU 75   73   73   GLU GLU A . n 
A 1 76   ALA 76   74   74   ALA ALA A . n 
A 1 77   LEU 77   75   75   LEU LEU A . n 
A 1 78   ARG 78   76   76   ARG ARG A . n 
A 1 79   GLY 79   77   77   GLY GLY A . n 
A 1 80   LYS 80   78   78   LYS LYS A . n 
A 1 81   HIS 81   79   ?    ?   ?   A . n 
A 1 82   SER 82   80   ?    ?   ?   A . n 
A 1 83   GLY 83   81   ?    ?   ?   A . n 
A 1 84   SER 84   82   ?    ?   ?   A . n 
A 1 85   GLY 85   83   83   GLY GLY A . n 
A 1 86   VAL 86   84   84   VAL VAL A . n 
A 1 87   GLU 87   85   85   GLU GLU A . n 
A 1 88   GLY 88   86   86   GLY GLY A . n 
A 1 89   LEU 89   87   87   LEU LEU A . n 
A 1 90   VAL 90   88   88   VAL VAL A . n 
A 1 91   GLN 91   89   89   GLN GLN A . n 
A 1 92   GLU 92   90   90   GLU GLU A . n 
A 1 93   TYR 93   91   91   TYR TYR A . n 
A 1 94   SER 94   92   92   SER SER A . n 
A 1 95   LEU 95   93   93   LEU LEU A . n 
A 1 96   SER 96   94   94   SER SER A . n 
A 1 97   SER 97   95   95   SER SER A . n 
A 1 98   GLN 98   96   96   GLN GLN A . n 
A 1 99   GLU 99   97   97   GLU GLU A . n 
A 1 100  GLY 100  98   98   GLY GLY A . n 
A 1 101  VAL 101  99   99   VAL VAL A . n 
A 1 102  ALA 102  100  100  ALA ALA A . n 
A 1 103  LEU 103  101  101  LEU LEU A . n 
A 1 104  MET 104  102  102  MET MET A . n 
A 1 105  CYS 105  103  103  CYS CYS A . n 
A 1 106  LEU 106  104  104  LEU LEU A . n 
A 1 107  ALA 107  105  105  ALA ALA A . n 
A 1 108  GLU 108  106  106  GLU GLU A . n 
A 1 109  ALA 109  107  107  ALA ALA A . n 
A 1 110  LEU 110  108  108  LEU LEU A . n 
A 1 111  LEU 111  109  109  LEU LEU A . n 
A 1 112  ARG 112  110  110  ARG ARG A . n 
A 1 113  ILE 113  111  111  ILE ILE A . n 
A 1 114  PRO 114  112  112  PRO PRO A . n 
A 1 115  ASP 115  113  113  ASP ASP A . n 
A 1 116  THR 116  114  114  THR THR A . n 
A 1 117  ALA 117  115  115  ALA ALA A . n 
A 1 118  THR 118  116  116  THR THR A . n 
A 1 119  ARG 119  117  117  ARG ARG A . n 
A 1 120  ASP 120  118  118  ASP ASP A . n 
A 1 121  ALA 121  119  119  ALA ALA A . n 
A 1 122  LEU 122  120  120  LEU LEU A . n 
A 1 123  ILE 123  121  121  ILE ILE A . n 
A 1 124  ARG 124  122  122  ARG ARG A . n 
A 1 125  ASP 125  123  123  ASP ASP A . n 
A 1 126  LYS 126  124  124  LYS LYS A . n 
A 1 127  ILE 127  125  125  ILE ILE A . n 
A 1 128  ALA 128  126  126  ALA ALA A . n 
A 1 129  ASP 129  127  127  ASP ASP A . n 
A 1 130  GLY 130  128  128  GLY GLY A . n 
A 1 131  ASN 131  129  129  ASN ASN A . n 
A 1 132  TRP 132  130  130  TRP TRP A . n 
A 1 133  LYS 133  131  131  LYS LYS A . n 
A 1 134  SER 134  132  132  SER SER A . n 
A 1 135  HIS 135  133  133  HIS HIS A . n 
A 1 136  LEU 136  134  134  LEU LEU A . n 
A 1 137  GLY 137  135  ?    ?   ?   A . n 
A 1 138  GLY 138  136  ?    ?   ?   A . n 
A 1 139  SER 139  137  137  SER SER A . n 
A 1 140  ARG 140  138  138  ARG ARG A . n 
A 1 141  SER 141  139  139  SER SER A . n 
A 1 142  LEU 142  140  140  LEU LEU A . n 
A 1 143  PHE 143  141  141  PHE PHE A . n 
A 1 144  VAL 144  142  142  VAL VAL A . n 
A 1 145  ASN 145  143  143  ASN ASN A . n 
A 1 146  ALA 146  144  144  ALA ALA A . n 
A 1 147  ALA 147  145  145  ALA ALA A . n 
A 1 148  THR 148  146  146  THR THR A . n 
A 1 149  TRP 149  147  147  TRP TRP A . n 
A 1 150  GLY 150  148  148  GLY GLY A . n 
A 1 151  LEU 151  149  149  LEU LEU A . n 
A 1 152  VAL 152  150  150  VAL VAL A . n 
A 1 153  VAL 153  151  151  VAL VAL A . n 
A 1 154  THR 154  152  152  THR THR A . n 
A 1 155  GLY 155  153  153  GLY GLY A . n 
A 1 156  LYS 156  154  154  LYS LYS A . n 
A 1 157  LEU 157  155  155  LEU LEU A . n 
A 1 158  THR 158  156  156  THR THR A . n 
A 1 159  SER 159  157  157  SER SER A . n 
A 1 160  THR 160  158  158  THR THR A . n 
A 1 161  VAL 161  159  159  VAL VAL A . n 
A 1 162  ASN 162  160  160  ASN ASN A . n 
A 1 163  ASP 163  161  161  ASP ASP A . n 
A 1 164  ARG 164  162  162  ARG ARG A . n 
A 1 165  SER 165  163  163  SER SER A . n 
A 1 166  LEU 166  164  164  LEU LEU A . n 
A 1 167  ALA 167  165  165  ALA ALA A . n 
A 1 168  ALA 168  166  166  ALA ALA A . n 
A 1 169  ALA 169  167  167  ALA ALA A . n 
A 1 170  LEU 170  168  168  LEU LEU A . n 
A 1 171  THR 171  169  169  THR THR A . n 
A 1 172  ARG 172  170  170  ARG ARG A . n 
A 1 173  LEU 173  171  171  LEU LEU A . n 
A 1 174  ILE 174  172  172  ILE ILE A . n 
A 1 175  SER 175  173  173  SER SER A . n 
A 1 176  ARG 176  174  174  ARG ARG A . n 
A 1 177  CYS 177  175  175  CYS CYS A . n 
A 1 178  GLY 178  176  176  GLY GLY A . n 
A 1 179  GLU 179  177  177  GLU GLU A . n 
A 1 180  PRO 180  178  178  PRO PRO A . n 
A 1 181  VAL 181  179  179  VAL VAL A . n 
A 1 182  ILE 182  180  180  ILE ILE A . n 
A 1 183  ARG 183  181  181  ARG ARG A . n 
A 1 184  ARG 184  182  182  ARG ARG A . n 
A 1 185  GLY 185  183  183  GLY GLY A . n 
A 1 186  VAL 186  184  184  VAL VAL A . n 
A 1 187  ASP 187  185  185  ASP ASP A . n 
A 1 188  MET 188  186  186  MET MET A . n 
A 1 189  ALA 189  187  187  ALA ALA A . n 
A 1 190  MET 190  188  188  MET MET A . n 
A 1 191  ARG 191  189  189  ARG ARG A . n 
A 1 192  MET 192  190  190  MET MET A . n 
A 1 193  MET 193  191  191  MET MET A . n 
A 1 194  GLY 194  192  192  GLY GLY A . n 
A 1 195  GLU 195  193  193  GLU GLU A . n 
A 1 196  GLN 196  194  194  GLN GLN A . n 
A 1 197  PHE 197  195  195  PHE PHE A . n 
A 1 198  VAL 198  196  196  VAL VAL A . n 
A 1 199  THR 199  197  197  THR THR A . n 
A 1 200  GLY 200  198  198  GLY GLY A . n 
A 1 201  GLU 201  199  199  GLU GLU A . n 
A 1 202  THR 202  200  200  THR THR A . n 
A 1 203  ILE 203  201  201  ILE ILE A . n 
A 1 204  ARG 204  202  202  ARG ARG A . n 
A 1 205  GLU 205  203  203  GLU GLU A . n 
A 1 206  ALA 206  204  204  ALA ALA A . n 
A 1 207  LEU 207  205  205  LEU LEU A . n 
A 1 208  LYS 208  206  206  LYS LYS A . n 
A 1 209  ARG 209  207  207  ARG ARG A . n 
A 1 210  SER 210  208  208  SER SER A . n 
A 1 211  LYS 211  209  209  LYS LYS A . n 
A 1 212  GLU 212  210  210  GLU GLU A . n 
A 1 213  LEU 213  211  211  LEU LEU A . n 
A 1 214  GLU 214  212  212  GLU GLU A . n 
A 1 215  GLU 215  213  213  GLU GLU A . n 
A 1 216  LYS 216  214  214  LYS LYS A . n 
A 1 217  GLY 217  215  215  GLY GLY A . n 
A 1 218  PHE 218  216  216  PHE PHE A . n 
A 1 219  SER 219  217  217  SER SER A . n 
A 1 220  TYR 220  218  218  TYR TYR A . n 
A 1 221  SER 221  219  219  SER SER A . n 
A 1 222  TYR 222  220  220  TYR TYR A . n 
A 1 223  ASP 223  221  221  ASP ASP A . n 
A 1 224  MET 224  222  222  MET MET A . n 
A 1 225  LEU 225  223  223  LEU LEU A . n 
A 1 226  GLY 226  224  224  GLY GLY A . n 
A 1 227  GLU 227  225  225  GLU GLU A . n 
A 1 228  ALA 228  226  226  ALA ALA A . n 
A 1 229  ALA 229  227  227  ALA ALA A . n 
A 1 230  THR 230  228  228  THR THR A . n 
A 1 231  THR 231  229  229  THR THR A . n 
A 1 232  ALA 232  230  230  ALA ALA A . n 
A 1 233  ALA 233  231  231  ALA ALA A . n 
A 1 234  ASP 234  232  232  ASP ASP A . n 
A 1 235  ALA 235  233  233  ALA ALA A . n 
A 1 236  GLU 236  234  234  GLU GLU A . n 
A 1 237  ARG 237  235  235  ARG ARG A . n 
A 1 238  TYR 238  236  236  TYR TYR A . n 
A 1 239  TYR 239  237  237  TYR TYR A . n 
A 1 240  ARG 240  238  238  ARG ARG A . n 
A 1 241  ASP 241  239  239  ASP ASP A . n 
A 1 242  TYR 242  240  240  TYR TYR A . n 
A 1 243  GLU 243  241  241  GLU GLU A . n 
A 1 244  SER 244  242  242  SER SER A . n 
A 1 245  ALA 245  243  243  ALA ALA A . n 
A 1 246  ILE 246  244  244  ILE ILE A . n 
A 1 247  HIS 247  245  245  HIS HIS A . n 
A 1 248  ALA 248  246  246  ALA ALA A . n 
A 1 249  ILE 249  247  247  ILE ILE A . n 
A 1 250  GLY 250  248  248  GLY GLY A . n 
A 1 251  LYS 251  249  249  LYS LYS A . n 
A 1 252  ALA 252  250  250  ALA ALA A . n 
A 1 253  SER 253  251  251  SER SER A . n 
A 1 254  ALA 254  252  252  ALA ALA A . n 
A 1 255  GLY 255  253  253  GLY GLY A . n 
A 1 256  ARG 256  254  254  ARG ARG A . n 
A 1 257  GLY 257  255  255  GLY GLY A . n 
A 1 258  ILE 258  256  256  ILE ILE A . n 
A 1 259  TYR 259  257  257  TYR TYR A . n 
A 1 260  GLU 260  258  258  GLU GLU A . n 
A 1 261  GLY 261  259  259  GLY GLY A . n 
A 1 262  PRO 262  260  260  PRO PRO A . n 
A 1 263  GLY 263  261  261  GLY GLY A . n 
A 1 264  ILE 264  262  262  ILE ILE A . n 
A 1 265  SER 265  263  263  SER SER A . n 
A 1 266  ILE 266  264  264  ILE ILE A . n 
A 1 267  LYS 267  265  265  LYS LYS A . n 
A 1 268  LEU 268  266  266  LEU LEU A . n 
A 1 269  SER 269  267  267  SER SER A . n 
A 1 270  ALA 270  268  268  ALA ALA A . n 
A 1 271  LEU 271  269  269  LEU LEU A . n 
A 1 272  HIS 272  270  270  HIS HIS A . n 
A 1 273  PRO 273  271  271  PRO PRO A . n 
A 1 274  ARG 274  272  272  ARG ARG A . n 
A 1 275  TYR 275  273  273  TYR TYR A . n 
A 1 276  SER 276  274  274  SER SER A . n 
A 1 277  ARG 277  275  275  ARG ARG A . n 
A 1 278  ALA 278  276  276  ALA ALA A . n 
A 1 279  GLN 279  277  277  GLN GLN A . n 
A 1 280  ALA 280  278  278  ALA ALA A . n 
A 1 281  ALA 281  279  279  ALA ALA A . n 
A 1 282  ARG 282  280  280  ARG ARG A . n 
A 1 283  VAL 283  281  281  VAL VAL A . n 
A 1 284  MET 284  282  282  MET MET A . n 
A 1 285  GLY 285  283  283  GLY GLY A . n 
A 1 286  GLU 286  284  284  GLU GLU A . n 
A 1 287  LEU 287  285  285  LEU LEU A . n 
A 1 288  LEU 288  286  286  LEU LEU A . n 
A 1 289  PRO 289  287  287  PRO PRO A . n 
A 1 290  ARG 290  288  288  ARG ARG A . n 
A 1 291  VAL 291  289  289  VAL VAL A . n 
A 1 292  LYS 292  290  290  LYS LYS A . n 
A 1 293  ALA 293  291  291  ALA ALA A . n 
A 1 294  LEU 294  292  292  LEU LEU A . n 
A 1 295  ALA 295  293  293  ALA ALA A . n 
A 1 296  LEU 296  294  294  LEU LEU A . n 
A 1 297  LEU 297  295  295  LEU LEU A . n 
A 1 298  ALA 298  296  296  ALA ALA A . n 
A 1 299  LYS 299  297  297  LYS LYS A . n 
A 1 300  ASN 300  298  298  ASN ASN A . n 
A 1 301  TYR 301  299  299  TYR TYR A . n 
A 1 302  ASP 302  300  300  ASP ASP A . n 
A 1 303  ILE 303  301  301  ILE ILE A . n 
A 1 304  GLY 304  302  302  GLY GLY A . n 
A 1 305  LEU 305  303  303  LEU LEU A . n 
A 1 306  ASN 306  304  304  ASN ASN A . n 
A 1 307  ILE 307  305  305  ILE ILE A . n 
A 1 308  ASP 308  306  306  ASP ASP A . n 
A 1 309  ALA 309  307  307  ALA ALA A . n 
A 1 310  GLU 310  308  308  GLU GLU A . n 
A 1 311  GLU 311  309  309  GLU GLU A . n 
A 1 312  ALA 312  310  310  ALA ALA A . n 
A 1 313  ASP 313  311  311  ASP ASP A . n 
A 1 314  ARG 314  312  312  ARG ARG A . n 
A 1 315  LEU 315  313  313  LEU LEU A . n 
A 1 316  GLU 316  314  314  GLU GLU A . n 
A 1 317  LEU 317  315  315  LEU LEU A . n 
A 1 318  SER 318  316  316  SER SER A . n 
A 1 319  LEU 319  317  317  LEU LEU A . n 
A 1 320  ASP 320  318  318  ASP ASP A . n 
A 1 321  LEU 321  319  319  LEU LEU A . n 
A 1 322  LEU 322  320  320  LEU LEU A . n 
A 1 323  GLU 323  321  321  GLU GLU A . n 
A 1 324  VAL 324  322  322  VAL VAL A . n 
A 1 325  LEU 325  323  323  LEU LEU A . n 
A 1 326  CYS 326  324  324  CYS CYS A . n 
A 1 327  LEU 327  325  325  LEU LEU A . n 
A 1 328  ASP 328  326  326  ASP ASP A . n 
A 1 329  GLY 329  327  327  GLY GLY A . n 
A 1 330  ASP 330  328  328  ASP ASP A . n 
A 1 331  LEU 331  329  329  LEU LEU A . n 
A 1 332  SER 332  330  330  SER SER A . n 
A 1 333  GLY 333  331  331  GLY GLY A . n 
A 1 334  TRP 334  332  332  TRP TRP A . n 
A 1 335  ASN 335  333  333  ASN ASN A . n 
A 1 336  GLY 336  334  334  GLY GLY A . n 
A 1 337  MET 337  335  335  MET MET A . n 
A 1 338  GLY 338  336  336  GLY GLY A . n 
A 1 339  PHE 339  337  337  PHE PHE A . n 
A 1 340  VAL 340  338  338  VAL VAL A . n 
A 1 341  VAL 341  339  339  VAL VAL A . n 
A 1 342  GLN 342  340  340  GLN GLN A . n 
A 1 343  ALA 343  341  341  ALA ALA A . n 
A 1 344  TYR 344  342  342  TYR TYR A . n 
A 1 345  GLY 345  343  343  GLY GLY A . n 
A 1 346  LYS 346  344  344  LYS LYS A . n 
A 1 347  ARG 347  345  345  ARG ARG A . n 
A 1 348  CYS 348  346  346  CYS CYS A . n 
A 1 349  PRO 349  347  347  PRO PRO A . n 
A 1 350  PHE 350  348  348  PHE PHE A . n 
A 1 351  VAL 351  349  349  VAL VAL A . n 
A 1 352  LEU 352  350  350  LEU LEU A . n 
A 1 353  ASP 353  351  351  ASP ASP A . n 
A 1 354  PHE 354  352  352  PHE PHE A . n 
A 1 355  ILE 355  353  353  ILE ILE A . n 
A 1 356  ILE 356  354  354  ILE ILE A . n 
A 1 357  ASP 357  355  355  ASP ASP A . n 
A 1 358  LEU 358  356  356  LEU LEU A . n 
A 1 359  ALA 359  357  357  ALA ALA A . n 
A 1 360  ARG 360  358  358  ARG ARG A . n 
A 1 361  ARG 361  359  359  ARG ARG A . n 
A 1 362  SER 362  360  360  SER SER A . n 
A 1 363  GLY 363  361  361  GLY GLY A . n 
A 1 364  ARG 364  362  362  ARG ARG A . n 
A 1 365  ARG 365  363  363  ARG ARG A . n 
A 1 366  ILE 366  364  364  ILE ILE A . n 
A 1 367  MET 367  365  365  MET MET A . n 
A 1 368  VAL 368  366  366  VAL VAL A . n 
A 1 369  ARG 369  367  367  ARG ARG A . n 
A 1 370  LEU 370  368  368  LEU LEU A . n 
A 1 371  VAL 371  369  369  VAL VAL A . n 
A 1 372  LYS 372  370  370  LYS LYS A . n 
A 1 373  GLY 373  371  371  GLY GLY A . n 
A 1 374  ALA 374  372  372  ALA ALA A . n 
A 1 375  TYR 375  373  373  TYR TYR A . n 
A 1 376  TRP 376  374  374  TRP TRP A . n 
A 1 377  ASP 377  375  375  ASP ASP A . n 
A 1 378  ALA 378  376  376  ALA ALA A . n 
A 1 379  GLU 379  377  377  GLU GLU A . n 
A 1 380  ILE 380  378  378  ILE ILE A . n 
A 1 381  LYS 381  379  379  LYS LYS A . n 
A 1 382  ARG 382  380  380  ARG ARG A . n 
A 1 383  ALA 383  381  381  ALA ALA A . n 
A 1 384  GLN 384  382  382  GLN GLN A . n 
A 1 385  LEU 385  383  383  LEU LEU A . n 
A 1 386  ASP 386  384  384  ASP ASP A . n 
A 1 387  GLY 387  385  385  GLY GLY A . n 
A 1 388  LEU 388  386  386  LEU LEU A . n 
A 1 389  ALA 389  387  387  ALA ALA A . n 
A 1 390  ASP 390  388  388  ASP ASP A . n 
A 1 391  PHE 391  389  389  PHE PHE A . n 
A 1 392  PRO 392  390  390  PRO PRO A . n 
A 1 393  VAL 393  391  391  VAL VAL A . n 
A 1 394  PHE 394  392  392  PHE PHE A . n 
A 1 395  THR 395  393  393  THR THR A . n 
A 1 396  ARG 396  394  394  ARG ARG A . n 
A 1 397  LYS 397  395  395  LYS LYS A . n 
A 1 398  ILE 398  396  396  ILE ILE A . n 
A 1 399  HIS 399  397  397  HIS HIS A . n 
A 1 400  THR 400  398  398  THR THR A . n 
A 1 401  ASP 401  399  399  ASP ASP A . n 
A 1 402  VAL 402  400  400  VAL VAL A . n 
A 1 403  SER 403  401  401  SER SER A . n 
A 1 404  TYR 404  402  402  TYR TYR A . n 
A 1 405  ILE 405  403  403  ILE ILE A . n 
A 1 406  ALA 406  404  404  ALA ALA A . n 
A 1 407  CYS 407  405  405  CYS CYS A . n 
A 1 408  ALA 408  406  406  ALA ALA A . n 
A 1 409  ALA 409  407  407  ALA ALA A . n 
A 1 410  LYS 410  408  408  LYS LYS A . n 
A 1 411  LEU 411  409  409  LEU LEU A . n 
A 1 412  LEU 412  410  410  LEU LEU A . n 
A 1 413  ALA 413  411  411  ALA ALA A . n 
A 1 414  ALA 414  412  412  ALA ALA A . n 
A 1 415  THR 415  413  413  THR THR A . n 
A 1 416  ASP 416  414  414  ASP ASP A . n 
A 1 417  VAL 417  415  415  VAL VAL A . n 
A 1 418  VAL 418  416  416  VAL VAL A . n 
A 1 419  PHE 419  417  417  PHE PHE A . n 
A 1 420  PRO 420  418  418  PRO PRO A . n 
A 1 421  GLN 421  419  419  GLN GLN A . n 
A 1 422  PHE 422  420  420  PHE PHE A . n 
A 1 423  ALA 423  421  421  ALA ALA A . n 
A 1 424  THR 424  422  422  THR THR A . n 
A 1 425  HIS 425  423  423  HIS HIS A . n 
A 1 426  ASN 426  424  424  ASN ASN A . n 
A 1 427  ALA 427  425  425  ALA ALA A . n 
A 1 428  GLN 428  426  426  GLN GLN A . n 
A 1 429  THR 429  427  427  THR THR A . n 
A 1 430  LEU 430  428  428  LEU LEU A . n 
A 1 431  ALA 431  429  429  ALA ALA A . n 
A 1 432  ALA 432  430  430  ALA ALA A . n 
A 1 433  ILE 433  431  431  ILE ILE A . n 
A 1 434  TYR 434  432  432  TYR TYR A . n 
A 1 435  HIS 435  433  433  HIS HIS A . n 
A 1 436  MET 436  434  434  MET MET A . n 
A 1 437  ALA 437  435  435  ALA ALA A . n 
A 1 438  GLY 438  436  436  GLY GLY A . n 
A 1 439  LYS 439  437  437  LYS LYS A . n 
A 1 440  ASP 440  438  438  ASP ASP A . n 
A 1 441  PHE 441  439  439  PHE PHE A . n 
A 1 442  HIS 442  440  440  HIS HIS A . n 
A 1 443  VAL 443  441  441  VAL VAL A . n 
A 1 444  GLY 444  442  442  GLY GLY A . n 
A 1 445  LYS 445  443  443  LYS LYS A . n 
A 1 446  TYR 446  444  444  TYR TYR A . n 
A 1 447  GLU 447  445  445  GLU GLU A . n 
A 1 448  PHE 448  446  446  PHE PHE A . n 
A 1 449  GLN 449  447  447  GLN GLN A . n 
A 1 450  CYS 450  448  448  CYS CYS A . n 
A 1 451  LEU 451  449  449  LEU LEU A . n 
A 1 452  HIS 452  450  450  HIS HIS A . n 
A 1 453  GLY 453  451  451  GLY GLY A . n 
A 1 454  MET 454  452  452  MET MET A . n 
A 1 455  GLY 455  453  453  GLY GLY A . n 
A 1 456  GLU 456  454  454  GLU GLU A . n 
A 1 457  PRO 457  455  455  PRO PRO A . n 
A 1 458  LEU 458  456  456  LEU LEU A . n 
A 1 459  TYR 459  457  457  TYR TYR A . n 
A 1 460  GLU 460  458  458  GLU GLU A . n 
A 1 461  GLU 461  459  459  GLU GLU A . n 
A 1 462  VAL 462  460  460  VAL VAL A . n 
A 1 463  VAL 463  461  461  VAL VAL A . n 
A 1 464  GLY 464  462  462  GLY GLY A . n 
A 1 465  ARG 465  463  463  ARG ARG A . n 
A 1 466  GLY 466  464  464  GLY GLY A . n 
A 1 467  LYS 467  465  465  LYS LYS A . n 
A 1 468  LEU 468  466  466  LEU LEU A . n 
A 1 469  ASP 469  467  467  ASP ASP A . n 
A 1 470  ARG 470  468  468  ARG ARG A . n 
A 1 471  PRO 471  469  469  PRO PRO A . n 
A 1 472  CYS 472  470  470  CYS CYS A . n 
A 1 473  ARG 473  471  471  ARG ARG A . n 
A 1 474  ILE 474  472  472  ILE ILE A . n 
A 1 475  TYR 475  473  473  TYR TYR A . n 
A 1 476  ALA 476  474  474  ALA ALA A . n 
A 1 477  PRO 477  475  475  PRO PRO A . n 
A 1 478  VAL 478  476  476  VAL VAL A . n 
A 1 479  GLY 479  477  477  GLY GLY A . n 
A 1 480  THR 480  478  478  THR THR A . n 
A 1 481  HIS 481  479  479  HIS HIS A . n 
A 1 482  GLU 482  480  480  GLU GLU A . n 
A 1 483  THR 483  481  481  THR THR A . n 
A 1 484  LEU 484  482  482  LEU LEU A . n 
A 1 485  LEU 485  483  483  LEU LEU A . n 
A 1 486  ALA 486  484  484  ALA ALA A . n 
A 1 487  TYR 487  485  485  TYR TYR A . n 
A 1 488  LEU 488  486  486  LEU LEU A . n 
A 1 489  VAL 489  487  487  VAL VAL A . n 
A 1 490  ARG 490  488  488  ARG ARG A . n 
A 1 491  ARG 491  489  489  ARG ARG A . n 
A 1 492  LEU 492  490  490  LEU LEU A . n 
A 1 493  LEU 493  491  491  LEU LEU A . n 
A 1 494  GLU 494  492  ?    ?   ?   A . n 
A 1 495  ASN 495  493  ?    ?   ?   A . n 
A 1 496  GLY 496  494  494  GLY GLY A . n 
A 1 497  ALA 497  495  495  ALA ALA A . n 
A 1 498  ASN 498  496  496  ASN ASN A . n 
A 1 499  SER 499  497  497  SER SER A . n 
A 1 500  SER 500  498  498  SER SER A . n 
A 1 501  PHE 501  499  499  PHE PHE A . n 
A 1 502  VAL 502  500  500  VAL VAL A . n 
A 1 503  HIS 503  501  501  HIS HIS A . n 
A 1 504  ARG 504  502  502  ARG ARG A . n 
A 1 505  ILE 505  503  503  ILE ILE A . n 
A 1 506  ASN 506  504  504  ASN ASN A . n 
A 1 507  ASP 507  505  505  ASP ASP A . n 
A 1 508  PRO 508  506  506  PRO PRO A . n 
A 1 509  LYS 509  507  507  LYS LYS A . n 
A 1 510  VAL 510  508  508  VAL VAL A . n 
A 1 511  SER 511  509  509  SER SER A . n 
A 1 512  ILE 512  510  510  ILE ILE A . n 
A 1 513  ASP 513  511  511  ASP ASP A . n 
A 1 514  GLU 514  512  512  GLU GLU A . n 
A 1 515  LEU 515  513  513  LEU LEU A . n 
A 1 516  ILE 516  514  514  ILE ILE A . n 
A 1 517  ALA 517  515  515  ALA ALA A . n 
A 1 518  ASP 518  516  516  ASP ASP A . n 
A 1 519  PRO 519  517  517  PRO PRO A . n 
A 1 520  VAL 520  518  518  VAL VAL A . n 
A 1 521  GLU 521  519  519  GLU GLU A . n 
A 1 522  VAL 522  520  520  VAL VAL A . n 
A 1 523  VAL 523  521  521  VAL VAL A . n 
A 1 524  ARG 524  522  522  ARG ARG A . n 
A 1 525  ALA 525  523  523  ALA ALA A . n 
A 1 526  MET 526  524  524  MET MET A . n 
A 1 527  PRO 527  525  525  PRO PRO A . n 
A 1 528  VAL 528  526  526  VAL VAL A . n 
A 1 529  VAL 529  527  527  VAL VAL A . n 
A 1 530  GLY 530  528  528  GLY GLY A . n 
A 1 531  ALA 531  529  529  ALA ALA A . n 
A 1 532  LYS 532  530  530  LYS LYS A . n 
A 1 533  HIS 533  531  531  HIS HIS A . n 
A 1 534  ASP 534  532  532  ASP ASP A . n 
A 1 535  ARG 535  533  533  ARG ARG A . n 
A 1 536  ILE 536  534  534  ILE ILE A . n 
A 1 537  ALA 537  535  535  ALA ALA A . n 
A 1 538  LEU 538  536  536  LEU LEU A . n 
A 1 539  PRO 539  537  537  PRO PRO A . n 
A 1 540  ALA 540  538  538  ALA ALA A . n 
A 1 541  GLU 541  539  539  GLU GLU A . n 
A 1 542  LEU 542  540  540  LEU LEU A . n 
A 1 543  PHE 543  541  541  PHE PHE A . n 
A 1 544  GLY 544  542  542  GLY GLY A . n 
A 1 545  ASP 545  543  543  ASP ASP A . n 
A 1 546  ALA 546  544  544  ALA ALA A . n 
A 1 547  ARG 547  545  545  ARG ARG A . n 
A 1 548  THR 548  546  546  THR THR A . n 
A 1 549  ASN 549  547  547  ASN ASN A . n 
A 1 550  SER 550  548  548  SER SER A . n 
A 1 551  ALA 551  549  549  ALA ALA A . n 
A 1 552  GLY 552  550  550  GLY GLY A . n 
A 1 553  LEU 553  551  551  LEU LEU A . n 
A 1 554  ASP 554  552  552  ASP ASP A . n 
A 1 555  LEU 555  553  553  LEU LEU A . n 
A 1 556  SER 556  554  554  SER SER A . n 
A 1 557  ASN 557  555  555  ASN ASN A . n 
A 1 558  GLU 558  556  556  GLU GLU A . n 
A 1 559  GLU 559  557  557  GLU GLU A . n 
A 1 560  THR 560  558  558  THR THR A . n 
A 1 561  LEU 561  559  559  LEU LEU A . n 
A 1 562  ALA 562  560  560  ALA ALA A . n 
A 1 563  SER 563  561  561  SER SER A . n 
A 1 564  LEU 564  562  562  LEU LEU A . n 
A 1 565  THR 565  563  563  THR THR A . n 
A 1 566  GLU 566  564  564  GLU GLU A . n 
A 1 567  ALA 567  565  565  ALA ALA A . n 
A 1 568  LEU 568  566  566  LEU LEU A . n 
A 1 569  ARG 569  567  567  ARG ARG A . n 
A 1 570  GLU 570  568  568  GLU GLU A . n 
A 1 571  SER 571  569  569  SER SER A . n 
A 1 572  ALA 572  570  570  ALA ALA A . n 
A 1 573  ALA 573  571  571  ALA ALA A . n 
A 1 574  MET 574  572  572  MET MET A . n 
A 1 575  LYS 575  573  573  LYS LYS A . n 
A 1 576  TRP 576  574  574  TRP TRP A . n 
A 1 577  THR 577  575  575  THR THR A . n 
A 1 578  ALA 578  576  576  ALA ALA A . n 
A 1 579  LEU 579  577  577  LEU LEU A . n 
A 1 580  PRO 580  578  578  PRO PRO A . n 
A 1 581  GLN 581  579  579  GLN GLN A . n 
A 1 582  LEU 582  580  580  LEU LEU A . n 
A 1 583  ALA 583  581  581  ALA ALA A . n 
A 1 584  THR 584  582  582  THR THR A . n 
A 1 585  GLY 585  583  583  GLY GLY A . n 
A 1 586  PRO 586  584  584  PRO PRO A . n 
A 1 587  ALA 587  585  585  ALA ALA A . n 
A 1 588  ALA 588  586  586  ALA ALA A . n 
A 1 589  GLY 589  587  587  GLY GLY A . n 
A 1 590  GLU 590  588  588  GLU GLU A . n 
A 1 591  THR 591  589  589  THR THR A . n 
A 1 592  ARG 592  590  590  ARG ARG A . n 
A 1 593  THR 593  591  591  THR THR A . n 
A 1 594  VAL 594  592  592  VAL VAL A . n 
A 1 595  LEU 595  593  593  LEU LEU A . n 
A 1 596  ASN 596  594  594  ASN ASN A . n 
A 1 597  PRO 597  595  595  PRO PRO A . n 
A 1 598  GLY 598  596  596  GLY GLY A . n 
A 1 599  ASP 599  597  597  ASP ASP A . n 
A 1 600  HIS 600  598  598  HIS HIS A . n 
A 1 601  ARG 601  599  599  ARG ARG A . n 
A 1 602  ASP 602  600  600  ASP ASP A . n 
A 1 603  VAL 603  601  601  VAL VAL A . n 
A 1 604  VAL 604  602  602  VAL VAL A . n 
A 1 605  GLY 605  603  603  GLY GLY A . n 
A 1 606  SER 606  604  604  SER SER A . n 
A 1 607  VAL 607  605  605  VAL VAL A . n 
A 1 608  THR 608  606  606  THR THR A . n 
A 1 609  GLU 609  607  607  GLU GLU A . n 
A 1 610  THR 610  608  608  THR THR A . n 
A 1 611  SER 611  609  609  SER SER A . n 
A 1 612  GLU 612  610  610  GLU GLU A . n 
A 1 613  GLU 613  611  611  GLU GLU A . n 
A 1 614  ASP 614  612  612  ASP ASP A . n 
A 1 615  ALA 615  613  613  ALA ALA A . n 
A 1 616  ARG 616  614  614  ARG ARG A . n 
A 1 617  ARG 617  615  615  ARG ARG A . n 
A 1 618  ALA 618  616  616  ALA ALA A . n 
A 1 619  VAL 619  617  617  VAL VAL A . n 
A 1 620  ARG 620  618  618  ARG ARG A . n 
A 1 621  LEU 621  619  619  LEU LEU A . n 
A 1 622  ALA 622  620  620  ALA ALA A . n 
A 1 623  ALA 623  621  621  ALA ALA A . n 
A 1 624  ASP 624  622  622  ASP ASP A . n 
A 1 625  ALA 625  623  623  ALA ALA A . n 
A 1 626  ALA 626  624  624  ALA ALA A . n 
A 1 627  PRO 627  625  625  PRO PRO A . n 
A 1 628  ASP 628  626  626  ASP ASP A . n 
A 1 629  TRP 629  627  627  TRP TRP A . n 
A 1 630  ALA 630  628  628  ALA ALA A . n 
A 1 631  ALA 631  629  629  ALA ALA A . n 
A 1 632  VAL 632  630  630  VAL VAL A . n 
A 1 633  PRO 633  631  631  PRO PRO A . n 
A 1 634  PRO 634  632  632  PRO PRO A . n 
A 1 635  SER 635  633  633  SER SER A . n 
A 1 636  GLU 636  634  634  GLU GLU A . n 
A 1 637  ARG 637  635  635  ARG ARG A . n 
A 1 638  ALA 638  636  636  ALA ALA A . n 
A 1 639  ALA 639  637  637  ALA ALA A . n 
A 1 640  CYS 640  638  638  CYS CYS A . n 
A 1 641  LEU 641  639  639  LEU LEU A . n 
A 1 642  ASP 642  640  640  ASP ASP A . n 
A 1 643  ARG 643  641  641  ARG ARG A . n 
A 1 644  ALA 644  642  642  ALA ALA A . n 
A 1 645  ALA 645  643  643  ALA ALA A . n 
A 1 646  GLU 646  644  644  GLU GLU A . n 
A 1 647  LEU 647  645  645  LEU LEU A . n 
A 1 648  MET 648  646  646  MET MET A . n 
A 1 649  GLN 649  647  647  GLN GLN A . n 
A 1 650  ALA 650  648  648  ALA ALA A . n 
A 1 651  ARG 651  649  649  ARG ARG A . n 
A 1 652  MET 652  650  650  MET MET A . n 
A 1 653  PRO 653  651  651  PRO PRO A . n 
A 1 654  THR 654  652  652  THR THR A . n 
A 1 655  LEU 655  653  653  LEU LEU A . n 
A 1 656  LEU 656  654  654  LEU LEU A . n 
A 1 657  GLY 657  655  655  GLY GLY A . n 
A 1 658  LEU 658  656  656  LEU LEU A . n 
A 1 659  ILE 659  657  657  ILE ILE A . n 
A 1 660  ILE 660  658  658  ILE ILE A . n 
A 1 661  ARG 661  659  659  ARG ARG A . n 
A 1 662  GLU 662  660  660  GLU GLU A . n 
A 1 663  ALA 663  661  661  ALA ALA A . n 
A 1 664  GLY 664  662  662  GLY GLY A . n 
A 1 665  LYS 665  663  663  LYS LYS A . n 
A 1 666  SER 666  664  664  SER SER A . n 
A 1 667  ALA 667  665  665  ALA ALA A . n 
A 1 668  LEU 668  666  666  LEU LEU A . n 
A 1 669  ASN 669  667  667  ASN ASN A . n 
A 1 670  ALA 670  668  668  ALA ALA A . n 
A 1 671  ILE 671  669  669  ILE ILE A . n 
A 1 672  ALA 672  670  670  ALA ALA A . n 
A 1 673  GLU 673  671  671  GLU GLU A . n 
A 1 674  VAL 674  672  672  VAL VAL A . n 
A 1 675  ARG 675  673  673  ARG ARG A . n 
A 1 676  GLU 676  674  674  GLU GLU A . n 
A 1 677  ALA 677  675  675  ALA ALA A . n 
A 1 678  ILE 678  676  676  ILE ILE A . n 
A 1 679  ASP 679  677  677  ASP ASP A . n 
A 1 680  PHE 680  678  678  PHE PHE A . n 
A 1 681  LEU 681  679  679  LEU LEU A . n 
A 1 682  ARG 682  680  680  ARG ARG A . n 
A 1 683  TYR 683  681  681  TYR TYR A . n 
A 1 684  TYR 684  682  682  TYR TYR A . n 
A 1 685  ALA 685  683  683  ALA ALA A . n 
A 1 686  GLU 686  684  684  GLU GLU A . n 
A 1 687  GLN 687  685  685  GLN GLN A . n 
A 1 688  THR 688  686  686  THR THR A . n 
A 1 689  ARG 689  687  687  ARG ARG A . n 
A 1 690  ARG 690  688  688  ARG ARG A . n 
A 1 691  THR 691  689  689  THR THR A . n 
A 1 692  LEU 692  690  690  LEU LEU A . n 
A 1 693  GLY 693  691  691  GLY GLY A . n 
A 1 694  PRO 694  692  692  PRO PRO A . n 
A 1 695  GLY 695  693  693  GLY GLY A . n 
A 1 696  HIS 696  694  694  HIS HIS A . n 
A 1 697  GLY 697  695  695  GLY GLY A . n 
A 1 698  PRO 698  696  696  PRO PRO A . n 
A 1 699  LEU 699  697  697  LEU LEU A . n 
A 1 700  GLY 700  698  698  GLY GLY A . n 
A 1 701  PRO 701  699  699  PRO PRO A . n 
A 1 702  ILE 702  700  700  ILE ILE A . n 
A 1 703  VAL 703  701  701  VAL VAL A . n 
A 1 704  CYS 704  702  702  CYS CYS A . n 
A 1 705  ILE 705  703  703  ILE ILE A . n 
A 1 706  SER 706  704  704  SER SER A . n 
A 1 707  PRO 707  705  705  PRO PRO A . n 
A 1 708  TRP 708  706  706  TRP TRP A . n 
A 1 709  ASN 709  707  707  ASN ASN A . n 
A 1 710  PHE 710  708  708  PHE PHE A . n 
A 1 711  PRO 711  709  709  PRO PRO A . n 
A 1 712  LEU 712  710  710  LEU LEU A . n 
A 1 713  ALA 713  711  711  ALA ALA A . n 
A 1 714  ILE 714  712  712  ILE ILE A . n 
A 1 715  PHE 715  713  713  PHE PHE A . n 
A 1 716  THR 716  714  714  THR THR A . n 
A 1 717  GLY 717  715  715  GLY GLY A . n 
A 1 718  GLN 718  716  716  GLN GLN A . n 
A 1 719  ILE 719  717  717  ILE ILE A . n 
A 1 720  ALA 720  718  718  ALA ALA A . n 
A 1 721  ALA 721  719  719  ALA ALA A . n 
A 1 722  ALA 722  720  720  ALA ALA A . n 
A 1 723  LEU 723  721  721  LEU LEU A . n 
A 1 724  VAL 724  722  722  VAL VAL A . n 
A 1 725  ALA 725  723  723  ALA ALA A . n 
A 1 726  GLY 726  724  724  GLY GLY A . n 
A 1 727  ASN 727  725  725  ASN ASN A . n 
A 1 728  PRO 728  726  726  PRO PRO A . n 
A 1 729  VAL 729  727  727  VAL VAL A . n 
A 1 730  LEU 730  728  728  LEU LEU A . n 
A 1 731  ALA 731  729  729  ALA ALA A . n 
A 1 732  LYS 732  730  730  LYS LYS A . n 
A 1 733  PRO 733  731  731  PRO PRO A . n 
A 1 734  ALA 734  732  732  ALA ALA A . n 
A 1 735  GLU 735  733  733  GLU GLU A . n 
A 1 736  GLU 736  734  734  GLU GLU A . n 
A 1 737  THR 737  735  735  THR THR A . n 
A 1 738  PRO 738  736  736  PRO PRO A . n 
A 1 739  LEU 739  737  737  LEU LEU A . n 
A 1 740  ILE 740  738  738  ILE ILE A . n 
A 1 741  ALA 741  739  739  ALA ALA A . n 
A 1 742  ALA 742  740  740  ALA ALA A . n 
A 1 743  GLU 743  741  741  GLU GLU A . n 
A 1 744  GLY 744  742  742  GLY GLY A . n 
A 1 745  VAL 745  743  743  VAL VAL A . n 
A 1 746  ARG 746  744  744  ARG ARG A . n 
A 1 747  ILE 747  745  745  ILE ILE A . n 
A 1 748  LEU 748  746  746  LEU LEU A . n 
A 1 749  ARG 749  747  747  ARG ARG A . n 
A 1 750  GLU 750  748  748  GLU GLU A . n 
A 1 751  ALA 751  749  749  ALA ALA A . n 
A 1 752  GLY 752  750  750  GLY GLY A . n 
A 1 753  ILE 753  751  751  ILE ILE A . n 
A 1 754  PRO 754  752  752  PRO PRO A . n 
A 1 755  ALA 755  753  753  ALA ALA A . n 
A 1 756  SER 756  754  754  SER SER A . n 
A 1 757  ALA 757  755  755  ALA ALA A . n 
A 1 758  LEU 758  756  756  LEU LEU A . n 
A 1 759  GLN 759  757  757  GLN GLN A . n 
A 1 760  LEU 760  758  758  LEU LEU A . n 
A 1 761  LEU 761  759  759  LEU LEU A . n 
A 1 762  PRO 762  760  760  PRO PRO A . n 
A 1 763  GLY 763  761  761  GLY GLY A . n 
A 1 764  ASP 764  762  762  ASP ASP A . n 
A 1 765  GLY 765  763  763  GLY GLY A . n 
A 1 766  ARG 766  764  764  ARG ARG A . n 
A 1 767  VAL 767  765  765  VAL VAL A . n 
A 1 768  GLY 768  766  766  GLY GLY A . n 
A 1 769  ALA 769  767  767  ALA ALA A . n 
A 1 770  ALA 770  768  768  ALA ALA A . n 
A 1 771  LEU 771  769  769  LEU LEU A . n 
A 1 772  VAL 772  770  770  VAL VAL A . n 
A 1 773  ALA 773  771  771  ALA ALA A . n 
A 1 774  ALA 774  772  772  ALA ALA A . n 
A 1 775  ALA 775  773  773  ALA ALA A . n 
A 1 776  GLU 776  774  774  GLU GLU A . n 
A 1 777  THR 777  775  775  THR THR A . n 
A 1 778  ALA 778  776  776  ALA ALA A . n 
A 1 779  GLY 779  777  777  GLY GLY A . n 
A 1 780  VAL 780  778  778  VAL VAL A . n 
A 1 781  MET 781  779  779  MET MET A . n 
A 1 782  PHE 782  780  780  PHE PHE A . n 
A 1 783  THR 783  781  781  THR THR A . n 
A 1 784  GLY 784  782  782  GLY GLY A . n 
A 1 785  SER 785  783  783  SER SER A . n 
A 1 786  THR 786  784  784  THR THR A . n 
A 1 787  GLU 787  785  785  GLU GLU A . n 
A 1 788  VAL 788  786  786  VAL VAL A . n 
A 1 789  ALA 789  787  787  ALA ALA A . n 
A 1 790  ARG 790  788  788  ARG ARG A . n 
A 1 791  LEU 791  789  789  LEU LEU A . n 
A 1 792  ILE 792  790  790  ILE ILE A . n 
A 1 793  GLN 793  791  791  GLN GLN A . n 
A 1 794  ALA 794  792  792  ALA ALA A . n 
A 1 795  GLN 795  793  793  GLN GLN A . n 
A 1 796  LEU 796  794  794  LEU LEU A . n 
A 1 797  ALA 797  795  795  ALA ALA A . n 
A 1 798  ASP 798  796  796  ASP ASP A . n 
A 1 799  ARG 799  797  797  ARG ARG A . n 
A 1 800  LEU 800  798  798  LEU LEU A . n 
A 1 801  SER 801  799  799  SER SER A . n 
A 1 802  PRO 802  800  800  PRO PRO A . n 
A 1 803  ALA 803  801  801  ALA ALA A . n 
A 1 804  GLY 804  802  802  GLY GLY A . n 
A 1 805  ARG 805  803  803  ARG ARG A . n 
A 1 806  PRO 806  804  804  PRO PRO A . n 
A 1 807  ILE 807  805  805  ILE ILE A . n 
A 1 808  PRO 808  806  806  PRO PRO A . n 
A 1 809  LEU 809  807  807  LEU LEU A . n 
A 1 810  ILE 810  808  808  ILE ILE A . n 
A 1 811  ALA 811  809  809  ALA ALA A . n 
A 1 812  GLU 812  810  810  GLU GLU A . n 
A 1 813  THR 813  811  811  THR THR A . n 
A 1 814  GLY 814  812  812  GLY GLY A . n 
A 1 815  GLY 815  813  813  GLY GLY A . n 
A 1 816  GLN 816  814  814  GLN GLN A . n 
A 1 817  ASN 817  815  815  ASN ASN A . n 
A 1 818  ALA 818  816  816  ALA ALA A . n 
A 1 819  MET 819  817  817  MET MET A . n 
A 1 820  ILE 820  818  818  ILE ILE A . n 
A 1 821  VAL 821  819  819  VAL VAL A . n 
A 1 822  ASP 822  820  820  ASP ASP A . n 
A 1 823  SER 823  821  821  SER SER A . n 
A 1 824  SER 824  822  822  SER SER A . n 
A 1 825  ALA 825  823  823  ALA ALA A . n 
A 1 826  LEU 826  824  824  LEU LEU A . n 
A 1 827  ALA 827  825  825  ALA ALA A . n 
A 1 828  GLU 828  826  826  GLU GLU A . n 
A 1 829  GLN 829  827  827  GLN GLN A . n 
A 1 830  VAL 830  828  828  VAL VAL A . n 
A 1 831  VAL 831  829  829  VAL VAL A . n 
A 1 832  GLY 832  830  830  GLY GLY A . n 
A 1 833  ASP 833  831  831  ASP ASP A . n 
A 1 834  VAL 834  832  832  VAL VAL A . n 
A 1 835  ILE 835  833  833  ILE ILE A . n 
A 1 836  THR 836  834  834  THR THR A . n 
A 1 837  SER 837  835  835  SER SER A . n 
A 1 838  ALA 838  836  836  ALA ALA A . n 
A 1 839  PHE 839  837  837  PHE PHE A . n 
A 1 840  ASP 840  838  838  ASP ASP A . n 
A 1 841  SER 841  839  839  SER SER A . n 
A 1 842  ALA 842  840  840  ALA ALA A . n 
A 1 843  GLY 843  841  841  GLY GLY A . n 
A 1 844  GLN 844  842  842  GLN GLN A . n 
A 1 845  ARG 845  843  843  ARG ARG A . n 
A 1 846  CYS 846  844  844  CYS CYS A . n 
A 1 847  SER 847  845  845  SER SER A . n 
A 1 848  ALA 848  846  846  ALA ALA A . n 
A 1 849  LEU 849  847  847  LEU LEU A . n 
A 1 850  ARG 850  848  848  ARG ARG A . n 
A 1 851  VAL 851  849  849  VAL VAL A . n 
A 1 852  LEU 852  850  850  LEU LEU A . n 
A 1 853  CYS 853  851  851  CYS CYS A . n 
A 1 854  LEU 854  852  852  LEU LEU A . n 
A 1 855  GLN 855  853  853  GLN GLN A . n 
A 1 856  GLU 856  854  854  GLU GLU A . n 
A 1 857  ASP 857  855  855  ASP ASP A . n 
A 1 858  VAL 858  856  856  VAL VAL A . n 
A 1 859  ALA 859  857  857  ALA ALA A . n 
A 1 860  ASP 860  858  858  ASP ASP A . n 
A 1 861  ARG 861  859  859  ARG ARG A . n 
A 1 862  ILE 862  860  860  ILE ILE A . n 
A 1 863  LEU 863  861  861  LEU LEU A . n 
A 1 864  THR 864  862  862  THR THR A . n 
A 1 865  MET 865  863  863  MET MET A . n 
A 1 866  LEU 866  864  864  LEU LEU A . n 
A 1 867  LYS 867  865  865  LYS LYS A . n 
A 1 868  GLY 868  866  866  GLY GLY A . n 
A 1 869  ALA 869  867  867  ALA ALA A . n 
A 1 870  LEU 870  868  868  LEU LEU A . n 
A 1 871  HIS 871  869  869  HIS HIS A . n 
A 1 872  GLU 872  870  870  GLU GLU A . n 
A 1 873  LEU 873  871  871  LEU LEU A . n 
A 1 874  HIS 874  872  872  HIS HIS A . n 
A 1 875  ILE 875  873  873  ILE ILE A . n 
A 1 876  GLY 876  874  874  GLY GLY A . n 
A 1 877  ARG 877  875  875  ARG ARG A . n 
A 1 878  THR 878  876  876  THR THR A . n 
A 1 879  ASP 879  877  877  ASP ASP A . n 
A 1 880  ARG 880  878  878  ARG ARG A . n 
A 1 881  LEU 881  879  879  LEU LEU A . n 
A 1 882  SER 882  880  880  SER SER A . n 
A 1 883  VAL 883  881  881  VAL VAL A . n 
A 1 884  ASP 884  882  882  ASP ASP A . n 
A 1 885  VAL 885  883  883  VAL VAL A . n 
A 1 886  GLY 886  884  884  GLY GLY A . n 
A 1 887  PRO 887  885  885  PRO PRO A . n 
A 1 888  VAL 888  886  886  VAL VAL A . n 
A 1 889  ILE 889  887  887  ILE ILE A . n 
A 1 890  THR 890  888  888  THR THR A . n 
A 1 891  SER 891  889  889  SER SER A . n 
A 1 892  GLU 892  890  890  GLU GLU A . n 
A 1 893  ALA 893  891  891  ALA ALA A . n 
A 1 894  LYS 894  892  892  LYS LYS A . n 
A 1 895  ASP 895  893  893  ASP ASP A . n 
A 1 896  ASN 896  894  894  ASN ASN A . n 
A 1 897  ILE 897  895  895  ILE ILE A . n 
A 1 898  GLU 898  896  896  GLU GLU A . n 
A 1 899  LYS 899  897  897  LYS LYS A . n 
A 1 900  HIS 900  898  898  HIS HIS A . n 
A 1 901  ILE 901  899  899  ILE ILE A . n 
A 1 902  GLU 902  900  900  GLU GLU A . n 
A 1 903  ARG 903  901  901  ARG ARG A . n 
A 1 904  MET 904  902  902  MET MET A . n 
A 1 905  ARG 905  903  903  ARG ARG A . n 
A 1 906  GLY 906  904  904  GLY GLY A . n 
A 1 907  LEU 907  905  905  LEU LEU A . n 
A 1 908  GLY 908  906  906  GLY GLY A . n 
A 1 909  ARG 909  907  907  ARG ARG A . n 
A 1 910  LYS 910  908  908  LYS LYS A . n 
A 1 911  VAL 911  909  909  VAL VAL A . n 
A 1 912  GLU 912  910  910  GLU GLU A . n 
A 1 913  GLN 913  911  911  GLN GLN A . n 
A 1 914  ILE 914  912  912  ILE ILE A . n 
A 1 915  GLY 915  913  913  GLY GLY A . n 
A 1 916  LEU 916  914  914  LEU LEU A . n 
A 1 917  ALA 917  915  915  ALA ALA A . n 
A 1 918  SER 918  916  916  SER SER A . n 
A 1 919  GLU 919  917  917  GLU GLU A . n 
A 1 920  THR 920  918  918  THR THR A . n 
A 1 921  GLY 921  919  919  GLY GLY A . n 
A 1 922  VAL 922  920  920  VAL VAL A . n 
A 1 923  GLY 923  921  921  GLY GLY A . n 
A 1 924  THR 924  922  922  THR THR A . n 
A 1 925  PHE 925  923  923  PHE PHE A . n 
A 1 926  VAL 926  924  924  VAL VAL A . n 
A 1 927  PRO 927  925  925  PRO PRO A . n 
A 1 928  PRO 928  926  926  PRO PRO A . n 
A 1 929  THR 929  927  927  THR THR A . n 
A 1 930  ILE 930  928  928  ILE ILE A . n 
A 1 931  ILE 931  929  929  ILE ILE A . n 
A 1 932  GLU 932  930  930  GLU GLU A . n 
A 1 933  LEU 933  931  931  LEU LEU A . n 
A 1 934  GLU 934  932  932  GLU GLU A . n 
A 1 935  LYS 935  933  933  LYS LYS A . n 
A 1 936  LEU 936  934  934  LEU LEU A . n 
A 1 937  SER 937  935  935  SER SER A . n 
A 1 938  ASP 938  936  936  ASP ASP A . n 
A 1 939  LEU 939  937  937  LEU LEU A . n 
A 1 940  GLN 940  938  938  GLN GLN A . n 
A 1 941  ARG 941  939  939  ARG ARG A . n 
A 1 942  GLU 942  940  940  GLU GLU A . n 
A 1 943  VAL 943  941  941  VAL VAL A . n 
A 1 944  PHE 944  942  942  PHE PHE A . n 
A 1 945  GLY 945  943  943  GLY GLY A . n 
A 1 946  PRO 946  944  944  PRO PRO A . n 
A 1 947  VAL 947  945  945  VAL VAL A . n 
A 1 948  LEU 948  946  946  LEU LEU A . n 
A 1 949  HIS 949  947  947  HIS HIS A . n 
A 1 950  VAL 950  948  948  VAL VAL A . n 
A 1 951  ILE 951  949  949  ILE ILE A . n 
A 1 952  ARG 952  950  950  ARG ARG A . n 
A 1 953  TYR 953  951  951  TYR TYR A . n 
A 1 954  ARG 954  952  952  ARG ARG A . n 
A 1 955  ARG 955  953  953  ARG ARG A . n 
A 1 956  ASP 956  954  954  ASP ASP A . n 
A 1 957  ASP 957  955  955  ASP ASP A . n 
A 1 958  LEU 958  956  956  LEU LEU A . n 
A 1 959  ASP 959  957  957  ASP ASP A . n 
A 1 960  ARG 960  958  958  ARG ARG A . n 
A 1 961  LEU 961  959  959  LEU LEU A . n 
A 1 962  VAL 962  960  960  VAL VAL A . n 
A 1 963  ASP 963  961  961  ASP ASP A . n 
A 1 964  ASP 964  962  962  ASP ASP A . n 
A 1 965  VAL 965  963  963  VAL VAL A . n 
A 1 966  ASN 966  964  964  ASN ASN A . n 
A 1 967  ALA 967  965  965  ALA ALA A . n 
A 1 968  THR 968  966  966  THR THR A . n 
A 1 969  GLY 969  967  967  GLY GLY A . n 
A 1 970  TYR 970  968  968  TYR TYR A . n 
A 1 971  GLY 971  969  969  GLY GLY A . n 
A 1 972  LEU 972  970  970  LEU LEU A . n 
A 1 973  THR 973  971  971  THR THR A . n 
A 1 974  PHE 974  972  972  PHE PHE A . n 
A 1 975  GLY 975  973  973  GLY GLY A . n 
A 1 976  LEU 976  974  974  LEU LEU A . n 
A 1 977  HIS 977  975  975  HIS HIS A . n 
A 1 978  THR 978  976  976  THR THR A . n 
A 1 979  ARG 979  977  977  ARG ARG A . n 
A 1 980  LEU 980  978  978  LEU LEU A . n 
A 1 981  ASP 981  979  979  ASP ASP A . n 
A 1 982  GLU 982  980  980  GLU GLU A . n 
A 1 983  THR 983  981  981  THR THR A . n 
A 1 984  ILE 984  982  982  ILE ILE A . n 
A 1 985  ALA 985  983  983  ALA ALA A . n 
A 1 986  HIS 986  984  984  HIS HIS A . n 
A 1 987  VAL 987  985  985  VAL VAL A . n 
A 1 988  THR 988  986  986  THR THR A . n 
A 1 989  SER 989  987  987  SER SER A . n 
A 1 990  ARG 990  988  988  ARG ARG A . n 
A 1 991  ILE 991  989  989  ILE ILE A . n 
A 1 992  LYS 992  990  990  LYS LYS A . n 
A 1 993  ALA 993  991  991  ALA ALA A . n 
A 1 994  GLY 994  992  992  GLY GLY A . n 
A 1 995  ASN 995  993  993  ASN ASN A . n 
A 1 996  LEU 996  994  994  LEU LEU A . n 
A 1 997  TYR 997  995  995  TYR TYR A . n 
A 1 998  ILE 998  996  996  ILE ILE A . n 
A 1 999  ASN 999  997  997  ASN ASN A . n 
A 1 1000 ARG 1000 998  998  ARG ARG A . n 
A 1 1001 ASN 1001 999  999  ASN ASN A . n 
A 1 1002 ILE 1002 1000 1000 ILE ILE A . n 
A 1 1003 ILE 1003 1001 1001 ILE ILE A . n 
A 1 1004 GLY 1004 1002 1002 GLY GLY A . n 
A 1 1005 ALA 1005 1003 1003 ALA ALA A . n 
A 1 1006 VAL 1006 1004 1004 VAL VAL A . n 
A 1 1007 VAL 1007 1005 1005 VAL VAL A . n 
A 1 1008 GLY 1008 1006 1006 GLY GLY A . n 
A 1 1009 VAL 1009 1007 1007 VAL VAL A . n 
A 1 1010 GLN 1010 1008 1008 GLN GLN A . n 
A 1 1011 PRO 1011 1009 1009 PRO PRO A . n 
A 1 1012 PHE 1012 1010 1010 PHE PHE A . n 
A 1 1013 GLY 1013 1011 1011 GLY GLY A . n 
A 1 1014 GLY 1014 1012 1012 GLY GLY A . n 
A 1 1015 ARG 1015 1013 1013 ARG ARG A . n 
A 1 1016 GLY 1016 1014 1014 GLY GLY A . n 
A 1 1017 LEU 1017 1015 1015 LEU LEU A . n 
A 1 1018 SER 1018 1016 1016 SER SER A . n 
A 1 1019 GLY 1019 1017 1017 GLY GLY A . n 
A 1 1020 THR 1020 1018 1018 THR THR A . n 
A 1 1021 GLY 1021 1019 1019 GLY GLY A . n 
A 1 1022 PRO 1022 1020 1020 PRO PRO A . n 
A 1 1023 LYS 1023 1021 1021 LYS LYS A . n 
A 1 1024 ALA 1024 1022 1022 ALA ALA A . n 
A 1 1025 GLY 1025 1023 1023 GLY GLY A . n 
A 1 1026 GLY 1026 1024 1024 GLY GLY A . n 
A 1 1027 PRO 1027 1025 1025 PRO PRO A . n 
A 1 1028 LEU 1028 1026 1026 LEU LEU A . n 
A 1 1029 TYR 1029 1027 1027 TYR TYR A . n 
A 1 1030 LEU 1030 1028 1028 LEU LEU A . n 
A 1 1031 GLY 1031 1029 1029 GLY GLY A . n 
A 1 1032 ARG 1032 1030 1030 ARG ARG A . n 
A 1 1033 LEU 1033 1031 1031 LEU LEU A . n 
A 1 1034 VAL 1034 1032 1032 VAL VAL A . n 
A 1 1035 THR 1035 1033 1033 THR THR A . n 
A 1 1036 THR 1036 1034 1034 THR THR A . n 
A 1 1037 ALA 1037 1035 1035 ALA ALA A . n 
A 1 1038 PRO 1038 1036 1036 PRO PRO A . n 
A 1 1039 VAL 1039 1037 1037 VAL VAL A . n 
A 1 1040 PRO 1040 1038 1038 PRO PRO A . n 
A 1 1041 PRO 1041 1039 1039 PRO PRO A . n 
A 1 1042 GLN 1042 1040 1040 GLN GLN A . n 
A 1 1043 HIS 1043 1041 1041 HIS HIS A . n 
A 1 1044 SER 1044 1042 1042 SER SER A . n 
A 1 1045 SER 1045 1043 1043 SER SER A . n 
A 1 1046 VAL 1046 1044 1044 VAL VAL A . n 
A 1 1047 HIS 1047 1045 1045 HIS HIS A . n 
A 1 1048 THR 1048 1046 1046 THR THR A . n 
A 1 1049 ASP 1049 1047 1047 ASP ASP A . n 
A 1 1050 PRO 1050 1048 1048 PRO PRO A . n 
A 1 1051 VAL 1051 1049 1049 VAL VAL A . n 
A 1 1052 LEU 1052 1050 1050 LEU LEU A . n 
A 1 1053 LEU 1053 1051 1051 LEU LEU A . n 
A 1 1054 ASP 1054 1052 1052 ASP ASP A . n 
A 1 1055 PHE 1055 1053 1053 PHE PHE A . n 
A 1 1056 ALA 1056 1054 1054 ALA ALA A . n 
A 1 1057 LYS 1057 1055 1055 LYS LYS A . n 
A 1 1058 TRP 1058 1056 1056 TRP TRP A . n 
A 1 1059 LEU 1059 1057 1057 LEU LEU A . n 
A 1 1060 ASP 1060 1058 1058 ASP ASP A . n 
A 1 1061 GLY 1061 1059 1059 GLY GLY A . n 
A 1 1062 LYS 1062 1060 1060 LYS LYS A . n 
A 1 1063 GLY 1063 1061 1061 GLY GLY A . n 
A 1 1064 ALA 1064 1062 1062 ALA ALA A . n 
A 1 1065 ARG 1065 1063 1063 ARG ARG A . n 
A 1 1066 ALA 1066 1064 1064 ALA ALA A . n 
A 1 1067 GLU 1067 1065 1065 GLU GLU A . n 
A 1 1068 ALA 1068 1066 1066 ALA ALA A . n 
A 1 1069 GLU 1069 1067 1067 GLU GLU A . n 
A 1 1070 ALA 1070 1068 1068 ALA ALA A . n 
A 1 1071 ALA 1071 1069 1069 ALA ALA A . n 
A 1 1072 ARG 1072 1070 1070 ARG ARG A . n 
A 1 1073 ASN 1073 1071 1071 ASN ASN A . n 
A 1 1074 ALA 1074 1072 1072 ALA ALA A . n 
A 1 1075 GLY 1075 1073 1073 GLY GLY A . n 
A 1 1076 SER 1076 1074 1074 SER SER A . n 
A 1 1077 SER 1077 1075 1075 SER SER A . n 
A 1 1078 SER 1078 1076 1076 SER SER A . n 
A 1 1079 ALA 1079 1077 1077 ALA ALA A . n 
A 1 1080 LEU 1080 1078 1078 LEU LEU A . n 
A 1 1081 GLY 1081 1079 1079 GLY GLY A . n 
A 1 1082 LEU 1082 1080 1080 LEU LEU A . n 
A 1 1083 ASP 1083 1081 1081 ASP ASP A . n 
A 1 1084 LEU 1084 1082 1082 LEU LEU A . n 
A 1 1085 GLU 1085 1083 1083 GLU GLU A . n 
A 1 1086 LEU 1086 1084 1084 LEU LEU A . n 
A 1 1087 PRO 1087 1085 1085 PRO PRO A . n 
A 1 1088 GLY 1088 1086 1086 GLY GLY A . n 
A 1 1089 PRO 1089 1087 1087 PRO PRO A . n 
A 1 1090 VAL 1090 1088 1088 VAL VAL A . n 
A 1 1091 GLY 1091 1089 1089 GLY GLY A . n 
A 1 1092 GLU 1092 1090 1090 GLU GLU A . n 
A 1 1093 ARG 1093 1091 1091 ARG ARG A . n 
A 1 1094 ASN 1094 1092 1092 ASN ASN A . n 
A 1 1095 LEU 1095 1093 1093 LEU LEU A . n 
A 1 1096 TYR 1096 1094 1094 TYR TYR A . n 
A 1 1097 THR 1097 1095 1095 THR THR A . n 
A 1 1098 LEU 1098 1096 1096 LEU LEU A . n 
A 1 1099 HIS 1099 1097 1097 HIS HIS A . n 
A 1 1100 ALA 1100 1098 1098 ALA ALA A . n 
A 1 1101 ARG 1101 1099 1099 ARG ARG A . n 
A 1 1102 GLY 1102 1100 1100 GLY GLY A . n 
A 1 1103 ARG 1103 1101 1101 ARG ARG A . n 
A 1 1104 ILE 1104 1102 1102 ILE ILE A . n 
A 1 1105 LEU 1105 1103 1103 LEU LEU A . n 
A 1 1106 LEU 1106 1104 1104 LEU LEU A . n 
A 1 1107 VAL 1107 1105 1105 VAL VAL A . n 
A 1 1108 PRO 1108 1106 1106 PRO PRO A . n 
A 1 1109 ALA 1109 1107 1107 ALA ALA A . n 
A 1 1110 THR 1110 1108 1108 THR THR A . n 
A 1 1111 GLU 1111 1109 1109 GLU GLU A . n 
A 1 1112 SER 1112 1110 1110 SER SER A . n 
A 1 1113 GLY 1113 1111 1111 GLY GLY A . n 
A 1 1114 LEU 1114 1112 1112 LEU LEU A . n 
A 1 1115 TYR 1115 1113 1113 TYR TYR A . n 
A 1 1116 HIS 1116 1114 1114 HIS HIS A . n 
A 1 1117 GLN 1117 1115 1115 GLN GLN A . n 
A 1 1118 LEU 1118 1116 1116 LEU LEU A . n 
A 1 1119 ALA 1119 1117 1117 ALA ALA A . n 
A 1 1120 ALA 1120 1118 1118 ALA ALA A . n 
A 1 1121 ALA 1121 1119 1119 ALA ALA A . n 
A 1 1122 LEU 1122 1120 1120 LEU LEU A . n 
A 1 1123 ALA 1123 1121 1121 ALA ALA A . n 
A 1 1124 THR 1124 1122 1122 THR THR A . n 
A 1 1125 GLY 1125 1123 1123 GLY GLY A . n 
A 1 1126 ASN 1126 1124 1124 ASN ASN A . n 
A 1 1127 SER 1127 1125 1125 SER SER A . n 
A 1 1128 VAL 1128 1126 1126 VAL VAL A . n 
A 1 1129 ALA 1129 1127 1127 ALA ALA A . n 
A 1 1130 ILE 1130 1128 1128 ILE ILE A . n 
A 1 1131 ASP 1131 1129 1129 ASP ASP A . n 
A 1 1132 ALA 1132 1130 1130 ALA ALA A . n 
A 1 1133 ALA 1133 1131 1131 ALA ALA A . n 
A 1 1134 SER 1134 1132 1132 SER SER A . n 
A 1 1135 GLY 1135 1133 1133 GLY GLY A . n 
A 1 1136 LEU 1136 1134 1134 LEU LEU A . n 
A 1 1137 GLN 1137 1135 1135 GLN GLN A . n 
A 1 1138 ALA 1138 1136 1136 ALA ALA A . n 
A 1 1139 SER 1139 1137 1137 SER SER A . n 
A 1 1140 LEU 1140 1138 1138 LEU LEU A . n 
A 1 1141 LYS 1141 1139 1139 LYS LYS A . n 
A 1 1142 ASN 1142 1140 1140 ASN ASN A . n 
A 1 1143 LEU 1143 1141 1141 LEU LEU A . n 
A 1 1144 PRO 1144 1142 1142 PRO PRO A . n 
A 1 1145 GLN 1145 1143 1143 GLN GLN A . n 
A 1 1146 THR 1146 1144 1144 THR THR A . n 
A 1 1147 VAL 1147 1145 1145 VAL VAL A . n 
A 1 1148 GLY 1148 1146 1146 GLY GLY A . n 
A 1 1149 LEU 1149 1147 1147 LEU LEU A . n 
A 1 1150 ARG 1150 1148 1148 ARG ARG A . n 
A 1 1151 VAL 1151 1149 1149 VAL VAL A . n 
A 1 1152 SER 1152 1150 1150 SER SER A . n 
A 1 1153 TRP 1153 1151 1151 TRP TRP A . n 
A 1 1154 SER 1154 1152 1152 SER SER A . n 
A 1 1155 LYS 1155 1153 1153 LYS LYS A . n 
A 1 1156 ASP 1156 1154 1154 ASP ASP A . n 
A 1 1157 TRP 1157 1155 1155 TRP TRP A . n 
A 1 1158 ALA 1158 1156 1156 ALA ALA A . n 
A 1 1159 ALA 1159 1157 1157 ALA ALA A . n 
A 1 1160 ASP 1160 1158 1158 ASP ASP A . n 
A 1 1161 GLY 1161 1159 1159 GLY GLY A . n 
A 1 1162 PRO 1162 1160 1160 PRO PRO A . n 
A 1 1163 PHE 1163 1161 1161 PHE PHE A . n 
A 1 1164 ALA 1164 1162 1162 ALA ALA A . n 
A 1 1165 GLY 1165 1163 1163 GLY GLY A . n 
A 1 1166 ALA 1166 1164 1164 ALA ALA A . n 
A 1 1167 LEU 1167 1165 1165 LEU LEU A . n 
A 1 1168 VAL 1168 1166 1166 VAL VAL A . n 
A 1 1169 GLU 1169 1167 1167 GLU GLU A . n 
A 1 1170 GLY 1170 1168 1168 GLY GLY A . n 
A 1 1171 ASP 1171 1169 1169 ASP ASP A . n 
A 1 1172 ALA 1172 1170 1170 ALA ALA A . n 
A 1 1173 GLU 1173 1171 1171 GLU GLU A . n 
A 1 1174 ARG 1174 1172 1172 ARG ARG A . n 
A 1 1175 ILE 1175 1173 1173 ILE ILE A . n 
A 1 1176 ARG 1176 1174 1174 ARG ARG A . n 
A 1 1177 ALA 1177 1175 1175 ALA ALA A . n 
A 1 1178 VAL 1178 1176 1176 VAL VAL A . n 
A 1 1179 ASN 1179 1177 1177 ASN ASN A . n 
A 1 1180 LYS 1180 1178 1178 LYS LYS A . n 
A 1 1181 ALA 1181 1179 1179 ALA ALA A . n 
A 1 1182 ILE 1182 1180 1180 ILE ILE A . n 
A 1 1183 ALA 1183 1181 1181 ALA ALA A . n 
A 1 1184 ALA 1184 1182 1182 ALA ALA A . n 
A 1 1185 LEU 1185 1183 1183 LEU LEU A . n 
A 1 1186 PRO 1186 1184 1184 PRO PRO A . n 
A 1 1187 GLY 1187 1185 1185 GLY GLY A . n 
A 1 1188 PRO 1188 1186 1186 PRO PRO A . n 
A 1 1189 LEU 1189 1187 1187 LEU LEU A . n 
A 1 1190 LEU 1190 1188 1188 LEU LEU A . n 
A 1 1191 LEU 1191 1189 1189 LEU LEU A . n 
A 1 1192 VAL 1192 1190 1190 VAL VAL A . n 
A 1 1193 GLN 1193 1191 1191 GLN GLN A . n 
A 1 1194 ALA 1194 1192 1192 ALA ALA A . n 
A 1 1195 ALA 1195 1193 1193 ALA ALA A . n 
A 1 1196 SER 1196 1194 1194 SER SER A . n 
A 1 1197 SER 1197 1195 1195 SER SER A . n 
A 1 1198 GLY 1198 1196 1196 GLY GLY A . n 
A 1 1199 GLU 1199 1197 1197 GLU GLU A . n 
A 1 1200 ILE 1200 1198 1198 ILE ILE A . n 
A 1 1201 ALA 1201 1199 1199 ALA ALA A . n 
A 1 1202 ARG 1202 1200 1200 ARG ARG A . n 
A 1 1203 ASN 1203 1201 1201 ASN ASN A . n 
A 1 1204 PRO 1204 1202 1202 PRO PRO A . n 
A 1 1205 ASP 1205 1203 1203 ASP ASP A . n 
A 1 1206 ALA 1206 1204 1204 ALA ALA A . n 
A 1 1207 TYR 1207 1205 1205 TYR TYR A . n 
A 1 1208 CYS 1208 1206 1206 CYS CYS A . n 
A 1 1209 LEU 1209 1207 1207 LEU LEU A . n 
A 1 1210 ASN 1210 1208 1208 ASN ASN A . n 
A 1 1211 TRP 1211 1209 1209 TRP TRP A . n 
A 1 1212 LEU 1212 1210 1210 LEU LEU A . n 
A 1 1213 VAL 1213 1211 1211 VAL VAL A . n 
A 1 1214 GLU 1214 1212 1212 GLU GLU A . n 
A 1 1215 GLU 1215 1213 1213 GLU GLU A . n 
A 1 1216 VAL 1216 1214 1214 VAL VAL A . n 
A 1 1217 SER 1217 1215 1215 SER SER A . n 
A 1 1218 ALA 1218 1216 1216 ALA ALA A . n 
A 1 1219 SER 1219 1217 1217 SER SER A . n 
A 1 1220 ILE 1220 1218 1218 ILE ILE A . n 
A 1 1221 ASN 1221 1219 1219 ASN ASN A . n 
A 1 1222 THR 1222 1220 1220 THR THR A . n 
A 1 1223 ALA 1223 1221 1221 ALA ALA A . n 
A 1 1224 ALA 1224 1222 1222 ALA ALA A . n 
A 1 1225 ALA 1225 1223 1223 ALA ALA A . n 
A 1 1226 GLY 1226 1224 1224 GLY GLY A . n 
A 1 1227 GLY 1227 1225 1225 GLY GLY A . n 
A 1 1228 ASN 1228 1226 1226 ASN ASN A . n 
A 1 1229 ALA 1229 1227 1227 ALA ALA A . n 
A 1 1230 SER 1230 1228 ?    ?   ?   A . n 
A 1 1231 LEU 1231 1229 ?    ?   ?   A . n 
A 1 1232 MET 1232 1230 ?    ?   ?   A . n 
A 1 1233 ALA 1233 1231 ?    ?   ?   A . n 
A 1 1234 ILE 1234 1232 ?    ?   ?   A . n 
A 1 1235 GLY 1235 1233 ?    ?   ?   A . n 
B 1 1    SER 1    -1   ?    ?   ?   B . n 
B 1 2    MET 2    0    ?    ?   ?   B . n 
B 1 3    MET 3    1    ?    ?   ?   B . n 
B 1 4    SER 4    2    ?    ?   ?   B . n 
B 1 5    PRO 5    3    ?    ?   ?   B . n 
B 1 6    ASN 6    4    ?    ?   ?   B . n 
B 1 7    PRO 7    5    ?    ?   ?   B . n 
B 1 8    LEU 8    6    ?    ?   ?   B . n 
B 1 9    GLN 9    7    ?    ?   ?   B . n 
B 1 10   LYS 10   8    ?    ?   ?   B . n 
B 1 11   PRO 11   9    ?    ?   ?   B . n 
B 1 12   ALA 12   10   ?    ?   ?   B . n 
B 1 13   ILE 13   11   ?    ?   ?   B . n 
B 1 14   ASP 14   12   ?    ?   ?   B . n 
B 1 15   ALA 15   13   ?    ?   ?   B . n 
B 1 16   ALA 16   14   ?    ?   ?   B . n 
B 1 17   PRO 17   15   15   PRO PRO B . n 
B 1 18   ALA 18   16   16   ALA ALA B . n 
B 1 19   PRO 19   17   17   PRO PRO B . n 
B 1 20   PHE 20   18   18   PHE PHE B . n 
B 1 21   ALA 21   19   19   ALA ALA B . n 
B 1 22   ASP 22   20   20   ASP ASP B . n 
B 1 23   PHE 23   21   21   PHE PHE B . n 
B 1 24   ALA 24   22   22   ALA ALA B . n 
B 1 25   PRO 25   23   23   PRO PRO B . n 
B 1 26   PRO 26   24   24   PRO PRO B . n 
B 1 27   VAL 27   25   25   VAL VAL B . n 
B 1 28   ARG 28   26   26   ARG ARG B . n 
B 1 29   PRO 29   27   27   PRO PRO B . n 
B 1 30   GLN 30   28   28   GLN GLN B . n 
B 1 31   SER 31   29   29   SER SER B . n 
B 1 32   THR 32   30   30   THR THR B . n 
B 1 33   LEU 33   31   31   LEU LEU B . n 
B 1 34   ARG 34   32   32   ARG ARG B . n 
B 1 35   ARG 35   33   33   ARG ARG B . n 
B 1 36   ALA 36   34   34   ALA ALA B . n 
B 1 37   ILE 37   35   35   ILE ILE B . n 
B 1 38   THR 38   36   36   THR THR B . n 
B 1 39   ALA 39   37   37   ALA ALA B . n 
B 1 40   ALA 40   38   38   ALA ALA B . n 
B 1 41   TYR 41   39   39   TYR TYR B . n 
B 1 42   ARG 42   40   40   ARG ARG B . n 
B 1 43   ARG 43   41   41   ARG ARG B . n 
B 1 44   PRO 44   42   42   PRO PRO B . n 
B 1 45   GLU 45   43   43   GLU GLU B . n 
B 1 46   THR 46   44   44   THR THR B . n 
B 1 47   GLU 47   45   45   GLU GLU B . n 
B 1 48   CYS 48   46   46   CYS CYS B . n 
B 1 49   LEU 49   47   47   LEU LEU B . n 
B 1 50   PRO 50   48   48   PRO PRO B . n 
B 1 51   PRO 51   49   49   PRO PRO B . n 
B 1 52   LEU 52   50   50   LEU LEU B . n 
B 1 53   VAL 53   51   51   VAL VAL B . n 
B 1 54   GLU 54   52   52   GLU GLU B . n 
B 1 55   ALA 55   53   53   ALA ALA B . n 
B 1 56   ALA 56   54   54   ALA ALA B . n 
B 1 57   THR 57   55   55   THR THR B . n 
B 1 58   GLN 58   56   56   GLN GLN B . n 
B 1 59   SER 59   57   57   SER SER B . n 
B 1 60   LYS 60   58   58   LYS LYS B . n 
B 1 61   GLU 61   59   59   GLU GLU B . n 
B 1 62   ILE 62   60   60   ILE ILE B . n 
B 1 63   ARG 63   61   61   ARG ARG B . n 
B 1 64   ASP 64   62   62   ASP ASP B . n 
B 1 65   ALA 65   63   63   ALA ALA B . n 
B 1 66   ALA 66   64   64   ALA ALA B . n 
B 1 67   ALA 67   65   65   ALA ALA B . n 
B 1 68   SER 68   66   66   SER SER B . n 
B 1 69   THR 69   67   67   THR THR B . n 
B 1 70   ALA 70   68   68   ALA ALA B . n 
B 1 71   ARG 71   69   69   ARG ARG B . n 
B 1 72   LYS 72   70   70   LYS LYS B . n 
B 1 73   LEU 73   71   71   LEU LEU B . n 
B 1 74   ILE 74   72   72   ILE ILE B . n 
B 1 75   GLU 75   73   73   GLU GLU B . n 
B 1 76   ALA 76   74   74   ALA ALA B . n 
B 1 77   LEU 77   75   75   LEU LEU B . n 
B 1 78   ARG 78   76   76   ARG ARG B . n 
B 1 79   GLY 79   77   77   GLY GLY B . n 
B 1 80   LYS 80   78   78   LYS LYS B . n 
B 1 81   HIS 81   79   ?    ?   ?   B . n 
B 1 82   SER 82   80   ?    ?   ?   B . n 
B 1 83   GLY 83   81   ?    ?   ?   B . n 
B 1 84   SER 84   82   ?    ?   ?   B . n 
B 1 85   GLY 85   83   83   GLY GLY B . n 
B 1 86   VAL 86   84   84   VAL VAL B . n 
B 1 87   GLU 87   85   85   GLU GLU B . n 
B 1 88   GLY 88   86   86   GLY GLY B . n 
B 1 89   LEU 89   87   87   LEU LEU B . n 
B 1 90   VAL 90   88   88   VAL VAL B . n 
B 1 91   GLN 91   89   89   GLN GLN B . n 
B 1 92   GLU 92   90   90   GLU GLU B . n 
B 1 93   TYR 93   91   91   TYR TYR B . n 
B 1 94   SER 94   92   92   SER SER B . n 
B 1 95   LEU 95   93   93   LEU LEU B . n 
B 1 96   SER 96   94   94   SER SER B . n 
B 1 97   SER 97   95   95   SER SER B . n 
B 1 98   GLN 98   96   96   GLN GLN B . n 
B 1 99   GLU 99   97   97   GLU GLU B . n 
B 1 100  GLY 100  98   98   GLY GLY B . n 
B 1 101  VAL 101  99   99   VAL VAL B . n 
B 1 102  ALA 102  100  100  ALA ALA B . n 
B 1 103  LEU 103  101  101  LEU LEU B . n 
B 1 104  MET 104  102  102  MET MET B . n 
B 1 105  CYS 105  103  103  CYS CYS B . n 
B 1 106  LEU 106  104  104  LEU LEU B . n 
B 1 107  ALA 107  105  105  ALA ALA B . n 
B 1 108  GLU 108  106  106  GLU GLU B . n 
B 1 109  ALA 109  107  107  ALA ALA B . n 
B 1 110  LEU 110  108  108  LEU LEU B . n 
B 1 111  LEU 111  109  109  LEU LEU B . n 
B 1 112  ARG 112  110  110  ARG ARG B . n 
B 1 113  ILE 113  111  111  ILE ILE B . n 
B 1 114  PRO 114  112  112  PRO PRO B . n 
B 1 115  ASP 115  113  113  ASP ASP B . n 
B 1 116  THR 116  114  114  THR THR B . n 
B 1 117  ALA 117  115  115  ALA ALA B . n 
B 1 118  THR 118  116  116  THR THR B . n 
B 1 119  ARG 119  117  117  ARG ARG B . n 
B 1 120  ASP 120  118  118  ASP ASP B . n 
B 1 121  ALA 121  119  119  ALA ALA B . n 
B 1 122  LEU 122  120  120  LEU LEU B . n 
B 1 123  ILE 123  121  121  ILE ILE B . n 
B 1 124  ARG 124  122  122  ARG ARG B . n 
B 1 125  ASP 125  123  123  ASP ASP B . n 
B 1 126  LYS 126  124  124  LYS LYS B . n 
B 1 127  ILE 127  125  125  ILE ILE B . n 
B 1 128  ALA 128  126  126  ALA ALA B . n 
B 1 129  ASP 129  127  127  ASP ASP B . n 
B 1 130  GLY 130  128  128  GLY GLY B . n 
B 1 131  ASN 131  129  129  ASN ASN B . n 
B 1 132  TRP 132  130  130  TRP TRP B . n 
B 1 133  LYS 133  131  131  LYS LYS B . n 
B 1 134  SER 134  132  132  SER SER B . n 
B 1 135  HIS 135  133  133  HIS HIS B . n 
B 1 136  LEU 136  134  134  LEU LEU B . n 
B 1 137  GLY 137  135  ?    ?   ?   B . n 
B 1 138  GLY 138  136  ?    ?   ?   B . n 
B 1 139  SER 139  137  ?    ?   ?   B . n 
B 1 140  ARG 140  138  138  ARG ARG B . n 
B 1 141  SER 141  139  139  SER SER B . n 
B 1 142  LEU 142  140  140  LEU LEU B . n 
B 1 143  PHE 143  141  141  PHE PHE B . n 
B 1 144  VAL 144  142  142  VAL VAL B . n 
B 1 145  ASN 145  143  143  ASN ASN B . n 
B 1 146  ALA 146  144  144  ALA ALA B . n 
B 1 147  ALA 147  145  145  ALA ALA B . n 
B 1 148  THR 148  146  146  THR THR B . n 
B 1 149  TRP 149  147  147  TRP TRP B . n 
B 1 150  GLY 150  148  148  GLY GLY B . n 
B 1 151  LEU 151  149  149  LEU LEU B . n 
B 1 152  VAL 152  150  150  VAL VAL B . n 
B 1 153  VAL 153  151  151  VAL VAL B . n 
B 1 154  THR 154  152  152  THR THR B . n 
B 1 155  GLY 155  153  153  GLY GLY B . n 
B 1 156  LYS 156  154  154  LYS LYS B . n 
B 1 157  LEU 157  155  155  LEU LEU B . n 
B 1 158  THR 158  156  156  THR THR B . n 
B 1 159  SER 159  157  157  SER SER B . n 
B 1 160  THR 160  158  158  THR THR B . n 
B 1 161  VAL 161  159  159  VAL VAL B . n 
B 1 162  ASN 162  160  160  ASN ASN B . n 
B 1 163  ASP 163  161  161  ASP ASP B . n 
B 1 164  ARG 164  162  162  ARG ARG B . n 
B 1 165  SER 165  163  163  SER SER B . n 
B 1 166  LEU 166  164  164  LEU LEU B . n 
B 1 167  ALA 167  165  165  ALA ALA B . n 
B 1 168  ALA 168  166  166  ALA ALA B . n 
B 1 169  ALA 169  167  167  ALA ALA B . n 
B 1 170  LEU 170  168  168  LEU LEU B . n 
B 1 171  THR 171  169  169  THR THR B . n 
B 1 172  ARG 172  170  170  ARG ARG B . n 
B 1 173  LEU 173  171  171  LEU LEU B . n 
B 1 174  ILE 174  172  172  ILE ILE B . n 
B 1 175  SER 175  173  173  SER SER B . n 
B 1 176  ARG 176  174  174  ARG ARG B . n 
B 1 177  CYS 177  175  175  CYS CYS B . n 
B 1 178  GLY 178  176  176  GLY GLY B . n 
B 1 179  GLU 179  177  177  GLU GLU B . n 
B 1 180  PRO 180  178  178  PRO PRO B . n 
B 1 181  VAL 181  179  179  VAL VAL B . n 
B 1 182  ILE 182  180  180  ILE ILE B . n 
B 1 183  ARG 183  181  181  ARG ARG B . n 
B 1 184  ARG 184  182  182  ARG ARG B . n 
B 1 185  GLY 185  183  183  GLY GLY B . n 
B 1 186  VAL 186  184  184  VAL VAL B . n 
B 1 187  ASP 187  185  185  ASP ASP B . n 
B 1 188  MET 188  186  186  MET MET B . n 
B 1 189  ALA 189  187  187  ALA ALA B . n 
B 1 190  MET 190  188  188  MET MET B . n 
B 1 191  ARG 191  189  189  ARG ARG B . n 
B 1 192  MET 192  190  190  MET MET B . n 
B 1 193  MET 193  191  191  MET MET B . n 
B 1 194  GLY 194  192  192  GLY GLY B . n 
B 1 195  GLU 195  193  193  GLU GLU B . n 
B 1 196  GLN 196  194  194  GLN GLN B . n 
B 1 197  PHE 197  195  195  PHE PHE B . n 
B 1 198  VAL 198  196  196  VAL VAL B . n 
B 1 199  THR 199  197  197  THR THR B . n 
B 1 200  GLY 200  198  198  GLY GLY B . n 
B 1 201  GLU 201  199  199  GLU GLU B . n 
B 1 202  THR 202  200  200  THR THR B . n 
B 1 203  ILE 203  201  201  ILE ILE B . n 
B 1 204  ARG 204  202  202  ARG ARG B . n 
B 1 205  GLU 205  203  203  GLU GLU B . n 
B 1 206  ALA 206  204  204  ALA ALA B . n 
B 1 207  LEU 207  205  205  LEU LEU B . n 
B 1 208  LYS 208  206  206  LYS LYS B . n 
B 1 209  ARG 209  207  207  ARG ARG B . n 
B 1 210  SER 210  208  208  SER SER B . n 
B 1 211  LYS 211  209  209  LYS LYS B . n 
B 1 212  GLU 212  210  210  GLU GLU B . n 
B 1 213  LEU 213  211  211  LEU LEU B . n 
B 1 214  GLU 214  212  212  GLU GLU B . n 
B 1 215  GLU 215  213  213  GLU GLU B . n 
B 1 216  LYS 216  214  214  LYS LYS B . n 
B 1 217  GLY 217  215  215  GLY GLY B . n 
B 1 218  PHE 218  216  216  PHE PHE B . n 
B 1 219  SER 219  217  217  SER SER B . n 
B 1 220  TYR 220  218  218  TYR TYR B . n 
B 1 221  SER 221  219  219  SER SER B . n 
B 1 222  TYR 222  220  220  TYR TYR B . n 
B 1 223  ASP 223  221  221  ASP ASP B . n 
B 1 224  MET 224  222  222  MET MET B . n 
B 1 225  LEU 225  223  223  LEU LEU B . n 
B 1 226  GLY 226  224  224  GLY GLY B . n 
B 1 227  GLU 227  225  225  GLU GLU B . n 
B 1 228  ALA 228  226  226  ALA ALA B . n 
B 1 229  ALA 229  227  227  ALA ALA B . n 
B 1 230  THR 230  228  228  THR THR B . n 
B 1 231  THR 231  229  229  THR THR B . n 
B 1 232  ALA 232  230  230  ALA ALA B . n 
B 1 233  ALA 233  231  231  ALA ALA B . n 
B 1 234  ASP 234  232  232  ASP ASP B . n 
B 1 235  ALA 235  233  233  ALA ALA B . n 
B 1 236  GLU 236  234  234  GLU GLU B . n 
B 1 237  ARG 237  235  235  ARG ARG B . n 
B 1 238  TYR 238  236  236  TYR TYR B . n 
B 1 239  TYR 239  237  237  TYR TYR B . n 
B 1 240  ARG 240  238  238  ARG ARG B . n 
B 1 241  ASP 241  239  239  ASP ASP B . n 
B 1 242  TYR 242  240  240  TYR TYR B . n 
B 1 243  GLU 243  241  241  GLU GLU B . n 
B 1 244  SER 244  242  242  SER SER B . n 
B 1 245  ALA 245  243  243  ALA ALA B . n 
B 1 246  ILE 246  244  244  ILE ILE B . n 
B 1 247  HIS 247  245  245  HIS HIS B . n 
B 1 248  ALA 248  246  246  ALA ALA B . n 
B 1 249  ILE 249  247  247  ILE ILE B . n 
B 1 250  GLY 250  248  248  GLY GLY B . n 
B 1 251  LYS 251  249  249  LYS LYS B . n 
B 1 252  ALA 252  250  250  ALA ALA B . n 
B 1 253  SER 253  251  251  SER SER B . n 
B 1 254  ALA 254  252  252  ALA ALA B . n 
B 1 255  GLY 255  253  253  GLY GLY B . n 
B 1 256  ARG 256  254  254  ARG ARG B . n 
B 1 257  GLY 257  255  255  GLY GLY B . n 
B 1 258  ILE 258  256  256  ILE ILE B . n 
B 1 259  TYR 259  257  257  TYR TYR B . n 
B 1 260  GLU 260  258  258  GLU GLU B . n 
B 1 261  GLY 261  259  259  GLY GLY B . n 
B 1 262  PRO 262  260  260  PRO PRO B . n 
B 1 263  GLY 263  261  261  GLY GLY B . n 
B 1 264  ILE 264  262  262  ILE ILE B . n 
B 1 265  SER 265  263  263  SER SER B . n 
B 1 266  ILE 266  264  264  ILE ILE B . n 
B 1 267  LYS 267  265  265  LYS LYS B . n 
B 1 268  LEU 268  266  266  LEU LEU B . n 
B 1 269  SER 269  267  267  SER SER B . n 
B 1 270  ALA 270  268  268  ALA ALA B . n 
B 1 271  LEU 271  269  269  LEU LEU B . n 
B 1 272  HIS 272  270  270  HIS HIS B . n 
B 1 273  PRO 273  271  271  PRO PRO B . n 
B 1 274  ARG 274  272  272  ARG ARG B . n 
B 1 275  TYR 275  273  273  TYR TYR B . n 
B 1 276  SER 276  274  274  SER SER B . n 
B 1 277  ARG 277  275  275  ARG ARG B . n 
B 1 278  ALA 278  276  276  ALA ALA B . n 
B 1 279  GLN 279  277  277  GLN GLN B . n 
B 1 280  ALA 280  278  278  ALA ALA B . n 
B 1 281  ALA 281  279  279  ALA ALA B . n 
B 1 282  ARG 282  280  280  ARG ARG B . n 
B 1 283  VAL 283  281  281  VAL VAL B . n 
B 1 284  MET 284  282  282  MET MET B . n 
B 1 285  GLY 285  283  283  GLY GLY B . n 
B 1 286  GLU 286  284  284  GLU GLU B . n 
B 1 287  LEU 287  285  285  LEU LEU B . n 
B 1 288  LEU 288  286  286  LEU LEU B . n 
B 1 289  PRO 289  287  287  PRO PRO B . n 
B 1 290  ARG 290  288  288  ARG ARG B . n 
B 1 291  VAL 291  289  289  VAL VAL B . n 
B 1 292  LYS 292  290  290  LYS LYS B . n 
B 1 293  ALA 293  291  291  ALA ALA B . n 
B 1 294  LEU 294  292  292  LEU LEU B . n 
B 1 295  ALA 295  293  293  ALA ALA B . n 
B 1 296  LEU 296  294  294  LEU LEU B . n 
B 1 297  LEU 297  295  295  LEU LEU B . n 
B 1 298  ALA 298  296  296  ALA ALA B . n 
B 1 299  LYS 299  297  297  LYS LYS B . n 
B 1 300  ASN 300  298  298  ASN ASN B . n 
B 1 301  TYR 301  299  299  TYR TYR B . n 
B 1 302  ASP 302  300  300  ASP ASP B . n 
B 1 303  ILE 303  301  301  ILE ILE B . n 
B 1 304  GLY 304  302  302  GLY GLY B . n 
B 1 305  LEU 305  303  303  LEU LEU B . n 
B 1 306  ASN 306  304  304  ASN ASN B . n 
B 1 307  ILE 307  305  305  ILE ILE B . n 
B 1 308  ASP 308  306  306  ASP ASP B . n 
B 1 309  ALA 309  307  307  ALA ALA B . n 
B 1 310  GLU 310  308  308  GLU GLU B . n 
B 1 311  GLU 311  309  309  GLU GLU B . n 
B 1 312  ALA 312  310  310  ALA ALA B . n 
B 1 313  ASP 313  311  311  ASP ASP B . n 
B 1 314  ARG 314  312  312  ARG ARG B . n 
B 1 315  LEU 315  313  313  LEU LEU B . n 
B 1 316  GLU 316  314  314  GLU GLU B . n 
B 1 317  LEU 317  315  315  LEU LEU B . n 
B 1 318  SER 318  316  316  SER SER B . n 
B 1 319  LEU 319  317  317  LEU LEU B . n 
B 1 320  ASP 320  318  318  ASP ASP B . n 
B 1 321  LEU 321  319  319  LEU LEU B . n 
B 1 322  LEU 322  320  320  LEU LEU B . n 
B 1 323  GLU 323  321  321  GLU GLU B . n 
B 1 324  VAL 324  322  322  VAL VAL B . n 
B 1 325  LEU 325  323  323  LEU LEU B . n 
B 1 326  CYS 326  324  324  CYS CYS B . n 
B 1 327  LEU 327  325  325  LEU LEU B . n 
B 1 328  ASP 328  326  326  ASP ASP B . n 
B 1 329  GLY 329  327  327  GLY GLY B . n 
B 1 330  ASP 330  328  328  ASP ASP B . n 
B 1 331  LEU 331  329  329  LEU LEU B . n 
B 1 332  SER 332  330  330  SER SER B . n 
B 1 333  GLY 333  331  331  GLY GLY B . n 
B 1 334  TRP 334  332  332  TRP TRP B . n 
B 1 335  ASN 335  333  333  ASN ASN B . n 
B 1 336  GLY 336  334  334  GLY GLY B . n 
B 1 337  MET 337  335  335  MET MET B . n 
B 1 338  GLY 338  336  336  GLY GLY B . n 
B 1 339  PHE 339  337  337  PHE PHE B . n 
B 1 340  VAL 340  338  338  VAL VAL B . n 
B 1 341  VAL 341  339  339  VAL VAL B . n 
B 1 342  GLN 342  340  340  GLN GLN B . n 
B 1 343  ALA 343  341  341  ALA ALA B . n 
B 1 344  TYR 344  342  342  TYR TYR B . n 
B 1 345  GLY 345  343  343  GLY GLY B . n 
B 1 346  LYS 346  344  344  LYS LYS B . n 
B 1 347  ARG 347  345  345  ARG ARG B . n 
B 1 348  CYS 348  346  346  CYS CYS B . n 
B 1 349  PRO 349  347  347  PRO PRO B . n 
B 1 350  PHE 350  348  348  PHE PHE B . n 
B 1 351  VAL 351  349  349  VAL VAL B . n 
B 1 352  LEU 352  350  350  LEU LEU B . n 
B 1 353  ASP 353  351  351  ASP ASP B . n 
B 1 354  PHE 354  352  352  PHE PHE B . n 
B 1 355  ILE 355  353  353  ILE ILE B . n 
B 1 356  ILE 356  354  354  ILE ILE B . n 
B 1 357  ASP 357  355  355  ASP ASP B . n 
B 1 358  LEU 358  356  356  LEU LEU B . n 
B 1 359  ALA 359  357  357  ALA ALA B . n 
B 1 360  ARG 360  358  358  ARG ARG B . n 
B 1 361  ARG 361  359  359  ARG ARG B . n 
B 1 362  SER 362  360  360  SER SER B . n 
B 1 363  GLY 363  361  361  GLY GLY B . n 
B 1 364  ARG 364  362  362  ARG ARG B . n 
B 1 365  ARG 365  363  363  ARG ARG B . n 
B 1 366  ILE 366  364  364  ILE ILE B . n 
B 1 367  MET 367  365  365  MET MET B . n 
B 1 368  VAL 368  366  366  VAL VAL B . n 
B 1 369  ARG 369  367  367  ARG ARG B . n 
B 1 370  LEU 370  368  368  LEU LEU B . n 
B 1 371  VAL 371  369  369  VAL VAL B . n 
B 1 372  LYS 372  370  370  LYS LYS B . n 
B 1 373  GLY 373  371  371  GLY GLY B . n 
B 1 374  ALA 374  372  372  ALA ALA B . n 
B 1 375  TYR 375  373  373  TYR TYR B . n 
B 1 376  TRP 376  374  374  TRP TRP B . n 
B 1 377  ASP 377  375  375  ASP ASP B . n 
B 1 378  ALA 378  376  376  ALA ALA B . n 
B 1 379  GLU 379  377  377  GLU GLU B . n 
B 1 380  ILE 380  378  378  ILE ILE B . n 
B 1 381  LYS 381  379  379  LYS LYS B . n 
B 1 382  ARG 382  380  380  ARG ARG B . n 
B 1 383  ALA 383  381  381  ALA ALA B . n 
B 1 384  GLN 384  382  382  GLN GLN B . n 
B 1 385  LEU 385  383  383  LEU LEU B . n 
B 1 386  ASP 386  384  384  ASP ASP B . n 
B 1 387  GLY 387  385  385  GLY GLY B . n 
B 1 388  LEU 388  386  386  LEU LEU B . n 
B 1 389  ALA 389  387  387  ALA ALA B . n 
B 1 390  ASP 390  388  388  ASP ASP B . n 
B 1 391  PHE 391  389  389  PHE PHE B . n 
B 1 392  PRO 392  390  390  PRO PRO B . n 
B 1 393  VAL 393  391  391  VAL VAL B . n 
B 1 394  PHE 394  392  392  PHE PHE B . n 
B 1 395  THR 395  393  393  THR THR B . n 
B 1 396  ARG 396  394  394  ARG ARG B . n 
B 1 397  LYS 397  395  395  LYS LYS B . n 
B 1 398  ILE 398  396  396  ILE ILE B . n 
B 1 399  HIS 399  397  397  HIS HIS B . n 
B 1 400  THR 400  398  398  THR THR B . n 
B 1 401  ASP 401  399  399  ASP ASP B . n 
B 1 402  VAL 402  400  400  VAL VAL B . n 
B 1 403  SER 403  401  401  SER SER B . n 
B 1 404  TYR 404  402  402  TYR TYR B . n 
B 1 405  ILE 405  403  403  ILE ILE B . n 
B 1 406  ALA 406  404  404  ALA ALA B . n 
B 1 407  CYS 407  405  405  CYS CYS B . n 
B 1 408  ALA 408  406  406  ALA ALA B . n 
B 1 409  ALA 409  407  407  ALA ALA B . n 
B 1 410  LYS 410  408  408  LYS LYS B . n 
B 1 411  LEU 411  409  409  LEU LEU B . n 
B 1 412  LEU 412  410  410  LEU LEU B . n 
B 1 413  ALA 413  411  411  ALA ALA B . n 
B 1 414  ALA 414  412  412  ALA ALA B . n 
B 1 415  THR 415  413  413  THR THR B . n 
B 1 416  ASP 416  414  414  ASP ASP B . n 
B 1 417  VAL 417  415  415  VAL VAL B . n 
B 1 418  VAL 418  416  416  VAL VAL B . n 
B 1 419  PHE 419  417  417  PHE PHE B . n 
B 1 420  PRO 420  418  418  PRO PRO B . n 
B 1 421  GLN 421  419  419  GLN GLN B . n 
B 1 422  PHE 422  420  420  PHE PHE B . n 
B 1 423  ALA 423  421  421  ALA ALA B . n 
B 1 424  THR 424  422  422  THR THR B . n 
B 1 425  HIS 425  423  423  HIS HIS B . n 
B 1 426  ASN 426  424  424  ASN ASN B . n 
B 1 427  ALA 427  425  425  ALA ALA B . n 
B 1 428  GLN 428  426  426  GLN GLN B . n 
B 1 429  THR 429  427  427  THR THR B . n 
B 1 430  LEU 430  428  428  LEU LEU B . n 
B 1 431  ALA 431  429  429  ALA ALA B . n 
B 1 432  ALA 432  430  430  ALA ALA B . n 
B 1 433  ILE 433  431  431  ILE ILE B . n 
B 1 434  TYR 434  432  432  TYR TYR B . n 
B 1 435  HIS 435  433  433  HIS HIS B . n 
B 1 436  MET 436  434  434  MET MET B . n 
B 1 437  ALA 437  435  435  ALA ALA B . n 
B 1 438  GLY 438  436  436  GLY GLY B . n 
B 1 439  LYS 439  437  437  LYS LYS B . n 
B 1 440  ASP 440  438  438  ASP ASP B . n 
B 1 441  PHE 441  439  439  PHE PHE B . n 
B 1 442  HIS 442  440  440  HIS HIS B . n 
B 1 443  VAL 443  441  441  VAL VAL B . n 
B 1 444  GLY 444  442  442  GLY GLY B . n 
B 1 445  LYS 445  443  443  LYS LYS B . n 
B 1 446  TYR 446  444  444  TYR TYR B . n 
B 1 447  GLU 447  445  445  GLU GLU B . n 
B 1 448  PHE 448  446  446  PHE PHE B . n 
B 1 449  GLN 449  447  447  GLN GLN B . n 
B 1 450  CYS 450  448  448  CYS CYS B . n 
B 1 451  LEU 451  449  449  LEU LEU B . n 
B 1 452  HIS 452  450  450  HIS HIS B . n 
B 1 453  GLY 453  451  451  GLY GLY B . n 
B 1 454  MET 454  452  452  MET MET B . n 
B 1 455  GLY 455  453  453  GLY GLY B . n 
B 1 456  GLU 456  454  454  GLU GLU B . n 
B 1 457  PRO 457  455  455  PRO PRO B . n 
B 1 458  LEU 458  456  456  LEU LEU B . n 
B 1 459  TYR 459  457  457  TYR TYR B . n 
B 1 460  GLU 460  458  458  GLU GLU B . n 
B 1 461  GLU 461  459  459  GLU GLU B . n 
B 1 462  VAL 462  460  460  VAL VAL B . n 
B 1 463  VAL 463  461  461  VAL VAL B . n 
B 1 464  GLY 464  462  462  GLY GLY B . n 
B 1 465  ARG 465  463  463  ARG ARG B . n 
B 1 466  GLY 466  464  464  GLY GLY B . n 
B 1 467  LYS 467  465  465  LYS LYS B . n 
B 1 468  LEU 468  466  466  LEU LEU B . n 
B 1 469  ASP 469  467  467  ASP ASP B . n 
B 1 470  ARG 470  468  468  ARG ARG B . n 
B 1 471  PRO 471  469  469  PRO PRO B . n 
B 1 472  CYS 472  470  470  CYS CYS B . n 
B 1 473  ARG 473  471  471  ARG ARG B . n 
B 1 474  ILE 474  472  472  ILE ILE B . n 
B 1 475  TYR 475  473  473  TYR TYR B . n 
B 1 476  ALA 476  474  474  ALA ALA B . n 
B 1 477  PRO 477  475  475  PRO PRO B . n 
B 1 478  VAL 478  476  476  VAL VAL B . n 
B 1 479  GLY 479  477  477  GLY GLY B . n 
B 1 480  THR 480  478  478  THR THR B . n 
B 1 481  HIS 481  479  479  HIS HIS B . n 
B 1 482  GLU 482  480  480  GLU GLU B . n 
B 1 483  THR 483  481  481  THR THR B . n 
B 1 484  LEU 484  482  482  LEU LEU B . n 
B 1 485  LEU 485  483  483  LEU LEU B . n 
B 1 486  ALA 486  484  484  ALA ALA B . n 
B 1 487  TYR 487  485  485  TYR TYR B . n 
B 1 488  LEU 488  486  486  LEU LEU B . n 
B 1 489  VAL 489  487  487  VAL VAL B . n 
B 1 490  ARG 490  488  488  ARG ARG B . n 
B 1 491  ARG 491  489  489  ARG ARG B . n 
B 1 492  LEU 492  490  490  LEU LEU B . n 
B 1 493  LEU 493  491  491  LEU LEU B . n 
B 1 494  GLU 494  492  ?    ?   ?   B . n 
B 1 495  ASN 495  493  ?    ?   ?   B . n 
B 1 496  GLY 496  494  494  GLY GLY B . n 
B 1 497  ALA 497  495  495  ALA ALA B . n 
B 1 498  ASN 498  496  496  ASN ASN B . n 
B 1 499  SER 499  497  497  SER SER B . n 
B 1 500  SER 500  498  498  SER SER B . n 
B 1 501  PHE 501  499  499  PHE PHE B . n 
B 1 502  VAL 502  500  500  VAL VAL B . n 
B 1 503  HIS 503  501  501  HIS HIS B . n 
B 1 504  ARG 504  502  502  ARG ARG B . n 
B 1 505  ILE 505  503  503  ILE ILE B . n 
B 1 506  ASN 506  504  504  ASN ASN B . n 
B 1 507  ASP 507  505  505  ASP ASP B . n 
B 1 508  PRO 508  506  506  PRO PRO B . n 
B 1 509  LYS 509  507  507  LYS LYS B . n 
B 1 510  VAL 510  508  508  VAL VAL B . n 
B 1 511  SER 511  509  509  SER SER B . n 
B 1 512  ILE 512  510  510  ILE ILE B . n 
B 1 513  ASP 513  511  511  ASP ASP B . n 
B 1 514  GLU 514  512  512  GLU GLU B . n 
B 1 515  LEU 515  513  513  LEU LEU B . n 
B 1 516  ILE 516  514  514  ILE ILE B . n 
B 1 517  ALA 517  515  515  ALA ALA B . n 
B 1 518  ASP 518  516  516  ASP ASP B . n 
B 1 519  PRO 519  517  517  PRO PRO B . n 
B 1 520  VAL 520  518  518  VAL VAL B . n 
B 1 521  GLU 521  519  519  GLU GLU B . n 
B 1 522  VAL 522  520  520  VAL VAL B . n 
B 1 523  VAL 523  521  521  VAL VAL B . n 
B 1 524  ARG 524  522  522  ARG ARG B . n 
B 1 525  ALA 525  523  523  ALA ALA B . n 
B 1 526  MET 526  524  524  MET MET B . n 
B 1 527  PRO 527  525  525  PRO PRO B . n 
B 1 528  VAL 528  526  526  VAL VAL B . n 
B 1 529  VAL 529  527  527  VAL VAL B . n 
B 1 530  GLY 530  528  528  GLY GLY B . n 
B 1 531  ALA 531  529  529  ALA ALA B . n 
B 1 532  LYS 532  530  530  LYS LYS B . n 
B 1 533  HIS 533  531  531  HIS HIS B . n 
B 1 534  ASP 534  532  532  ASP ASP B . n 
B 1 535  ARG 535  533  533  ARG ARG B . n 
B 1 536  ILE 536  534  534  ILE ILE B . n 
B 1 537  ALA 537  535  535  ALA ALA B . n 
B 1 538  LEU 538  536  536  LEU LEU B . n 
B 1 539  PRO 539  537  537  PRO PRO B . n 
B 1 540  ALA 540  538  538  ALA ALA B . n 
B 1 541  GLU 541  539  539  GLU GLU B . n 
B 1 542  LEU 542  540  540  LEU LEU B . n 
B 1 543  PHE 543  541  541  PHE PHE B . n 
B 1 544  GLY 544  542  542  GLY GLY B . n 
B 1 545  ASP 545  543  543  ASP ASP B . n 
B 1 546  ALA 546  544  544  ALA ALA B . n 
B 1 547  ARG 547  545  545  ARG ARG B . n 
B 1 548  THR 548  546  546  THR THR B . n 
B 1 549  ASN 549  547  547  ASN ASN B . n 
B 1 550  SER 550  548  548  SER SER B . n 
B 1 551  ALA 551  549  549  ALA ALA B . n 
B 1 552  GLY 552  550  550  GLY GLY B . n 
B 1 553  LEU 553  551  551  LEU LEU B . n 
B 1 554  ASP 554  552  552  ASP ASP B . n 
B 1 555  LEU 555  553  553  LEU LEU B . n 
B 1 556  SER 556  554  554  SER SER B . n 
B 1 557  ASN 557  555  555  ASN ASN B . n 
B 1 558  GLU 558  556  556  GLU GLU B . n 
B 1 559  GLU 559  557  557  GLU GLU B . n 
B 1 560  THR 560  558  558  THR THR B . n 
B 1 561  LEU 561  559  559  LEU LEU B . n 
B 1 562  ALA 562  560  560  ALA ALA B . n 
B 1 563  SER 563  561  561  SER SER B . n 
B 1 564  LEU 564  562  562  LEU LEU B . n 
B 1 565  THR 565  563  563  THR THR B . n 
B 1 566  GLU 566  564  564  GLU GLU B . n 
B 1 567  ALA 567  565  565  ALA ALA B . n 
B 1 568  LEU 568  566  566  LEU LEU B . n 
B 1 569  ARG 569  567  567  ARG ARG B . n 
B 1 570  GLU 570  568  568  GLU GLU B . n 
B 1 571  SER 571  569  569  SER SER B . n 
B 1 572  ALA 572  570  570  ALA ALA B . n 
B 1 573  ALA 573  571  571  ALA ALA B . n 
B 1 574  MET 574  572  572  MET MET B . n 
B 1 575  LYS 575  573  573  LYS LYS B . n 
B 1 576  TRP 576  574  574  TRP TRP B . n 
B 1 577  THR 577  575  575  THR THR B . n 
B 1 578  ALA 578  576  576  ALA ALA B . n 
B 1 579  LEU 579  577  577  LEU LEU B . n 
B 1 580  PRO 580  578  578  PRO PRO B . n 
B 1 581  GLN 581  579  579  GLN GLN B . n 
B 1 582  LEU 582  580  580  LEU LEU B . n 
B 1 583  ALA 583  581  581  ALA ALA B . n 
B 1 584  THR 584  582  582  THR THR B . n 
B 1 585  GLY 585  583  583  GLY GLY B . n 
B 1 586  PRO 586  584  584  PRO PRO B . n 
B 1 587  ALA 587  585  585  ALA ALA B . n 
B 1 588  ALA 588  586  586  ALA ALA B . n 
B 1 589  GLY 589  587  587  GLY GLY B . n 
B 1 590  GLU 590  588  588  GLU GLU B . n 
B 1 591  THR 591  589  589  THR THR B . n 
B 1 592  ARG 592  590  590  ARG ARG B . n 
B 1 593  THR 593  591  591  THR THR B . n 
B 1 594  VAL 594  592  592  VAL VAL B . n 
B 1 595  LEU 595  593  593  LEU LEU B . n 
B 1 596  ASN 596  594  594  ASN ASN B . n 
B 1 597  PRO 597  595  595  PRO PRO B . n 
B 1 598  GLY 598  596  596  GLY GLY B . n 
B 1 599  ASP 599  597  597  ASP ASP B . n 
B 1 600  HIS 600  598  598  HIS HIS B . n 
B 1 601  ARG 601  599  599  ARG ARG B . n 
B 1 602  ASP 602  600  600  ASP ASP B . n 
B 1 603  VAL 603  601  601  VAL VAL B . n 
B 1 604  VAL 604  602  602  VAL VAL B . n 
B 1 605  GLY 605  603  603  GLY GLY B . n 
B 1 606  SER 606  604  604  SER SER B . n 
B 1 607  VAL 607  605  605  VAL VAL B . n 
B 1 608  THR 608  606  606  THR THR B . n 
B 1 609  GLU 609  607  607  GLU GLU B . n 
B 1 610  THR 610  608  608  THR THR B . n 
B 1 611  SER 611  609  609  SER SER B . n 
B 1 612  GLU 612  610  610  GLU GLU B . n 
B 1 613  GLU 613  611  611  GLU GLU B . n 
B 1 614  ASP 614  612  612  ASP ASP B . n 
B 1 615  ALA 615  613  613  ALA ALA B . n 
B 1 616  ARG 616  614  614  ARG ARG B . n 
B 1 617  ARG 617  615  615  ARG ARG B . n 
B 1 618  ALA 618  616  616  ALA ALA B . n 
B 1 619  VAL 619  617  617  VAL VAL B . n 
B 1 620  ARG 620  618  618  ARG ARG B . n 
B 1 621  LEU 621  619  619  LEU LEU B . n 
B 1 622  ALA 622  620  620  ALA ALA B . n 
B 1 623  ALA 623  621  621  ALA ALA B . n 
B 1 624  ASP 624  622  622  ASP ASP B . n 
B 1 625  ALA 625  623  623  ALA ALA B . n 
B 1 626  ALA 626  624  624  ALA ALA B . n 
B 1 627  PRO 627  625  625  PRO PRO B . n 
B 1 628  ASP 628  626  626  ASP ASP B . n 
B 1 629  TRP 629  627  627  TRP TRP B . n 
B 1 630  ALA 630  628  628  ALA ALA B . n 
B 1 631  ALA 631  629  629  ALA ALA B . n 
B 1 632  VAL 632  630  630  VAL VAL B . n 
B 1 633  PRO 633  631  631  PRO PRO B . n 
B 1 634  PRO 634  632  632  PRO PRO B . n 
B 1 635  SER 635  633  633  SER SER B . n 
B 1 636  GLU 636  634  634  GLU GLU B . n 
B 1 637  ARG 637  635  635  ARG ARG B . n 
B 1 638  ALA 638  636  636  ALA ALA B . n 
B 1 639  ALA 639  637  637  ALA ALA B . n 
B 1 640  CYS 640  638  638  CYS CYS B . n 
B 1 641  LEU 641  639  639  LEU LEU B . n 
B 1 642  ASP 642  640  640  ASP ASP B . n 
B 1 643  ARG 643  641  641  ARG ARG B . n 
B 1 644  ALA 644  642  642  ALA ALA B . n 
B 1 645  ALA 645  643  643  ALA ALA B . n 
B 1 646  GLU 646  644  644  GLU GLU B . n 
B 1 647  LEU 647  645  645  LEU LEU B . n 
B 1 648  MET 648  646  646  MET MET B . n 
B 1 649  GLN 649  647  647  GLN GLN B . n 
B 1 650  ALA 650  648  648  ALA ALA B . n 
B 1 651  ARG 651  649  649  ARG ARG B . n 
B 1 652  MET 652  650  650  MET MET B . n 
B 1 653  PRO 653  651  651  PRO PRO B . n 
B 1 654  THR 654  652  652  THR THR B . n 
B 1 655  LEU 655  653  653  LEU LEU B . n 
B 1 656  LEU 656  654  654  LEU LEU B . n 
B 1 657  GLY 657  655  655  GLY GLY B . n 
B 1 658  LEU 658  656  656  LEU LEU B . n 
B 1 659  ILE 659  657  657  ILE ILE B . n 
B 1 660  ILE 660  658  658  ILE ILE B . n 
B 1 661  ARG 661  659  659  ARG ARG B . n 
B 1 662  GLU 662  660  660  GLU GLU B . n 
B 1 663  ALA 663  661  661  ALA ALA B . n 
B 1 664  GLY 664  662  662  GLY GLY B . n 
B 1 665  LYS 665  663  663  LYS LYS B . n 
B 1 666  SER 666  664  664  SER SER B . n 
B 1 667  ALA 667  665  665  ALA ALA B . n 
B 1 668  LEU 668  666  666  LEU LEU B . n 
B 1 669  ASN 669  667  667  ASN ASN B . n 
B 1 670  ALA 670  668  668  ALA ALA B . n 
B 1 671  ILE 671  669  669  ILE ILE B . n 
B 1 672  ALA 672  670  670  ALA ALA B . n 
B 1 673  GLU 673  671  671  GLU GLU B . n 
B 1 674  VAL 674  672  672  VAL VAL B . n 
B 1 675  ARG 675  673  673  ARG ARG B . n 
B 1 676  GLU 676  674  674  GLU GLU B . n 
B 1 677  ALA 677  675  675  ALA ALA B . n 
B 1 678  ILE 678  676  676  ILE ILE B . n 
B 1 679  ASP 679  677  677  ASP ASP B . n 
B 1 680  PHE 680  678  678  PHE PHE B . n 
B 1 681  LEU 681  679  679  LEU LEU B . n 
B 1 682  ARG 682  680  680  ARG ARG B . n 
B 1 683  TYR 683  681  681  TYR TYR B . n 
B 1 684  TYR 684  682  682  TYR TYR B . n 
B 1 685  ALA 685  683  683  ALA ALA B . n 
B 1 686  GLU 686  684  684  GLU GLU B . n 
B 1 687  GLN 687  685  685  GLN GLN B . n 
B 1 688  THR 688  686  686  THR THR B . n 
B 1 689  ARG 689  687  687  ARG ARG B . n 
B 1 690  ARG 690  688  688  ARG ARG B . n 
B 1 691  THR 691  689  689  THR THR B . n 
B 1 692  LEU 692  690  690  LEU LEU B . n 
B 1 693  GLY 693  691  691  GLY GLY B . n 
B 1 694  PRO 694  692  692  PRO PRO B . n 
B 1 695  GLY 695  693  693  GLY GLY B . n 
B 1 696  HIS 696  694  694  HIS HIS B . n 
B 1 697  GLY 697  695  695  GLY GLY B . n 
B 1 698  PRO 698  696  696  PRO PRO B . n 
B 1 699  LEU 699  697  697  LEU LEU B . n 
B 1 700  GLY 700  698  698  GLY GLY B . n 
B 1 701  PRO 701  699  699  PRO PRO B . n 
B 1 702  ILE 702  700  700  ILE ILE B . n 
B 1 703  VAL 703  701  701  VAL VAL B . n 
B 1 704  CYS 704  702  702  CYS CYS B . n 
B 1 705  ILE 705  703  703  ILE ILE B . n 
B 1 706  SER 706  704  704  SER SER B . n 
B 1 707  PRO 707  705  705  PRO PRO B . n 
B 1 708  TRP 708  706  706  TRP TRP B . n 
B 1 709  ASN 709  707  707  ASN ASN B . n 
B 1 710  PHE 710  708  708  PHE PHE B . n 
B 1 711  PRO 711  709  709  PRO PRO B . n 
B 1 712  LEU 712  710  710  LEU LEU B . n 
B 1 713  ALA 713  711  711  ALA ALA B . n 
B 1 714  ILE 714  712  712  ILE ILE B . n 
B 1 715  PHE 715  713  713  PHE PHE B . n 
B 1 716  THR 716  714  714  THR THR B . n 
B 1 717  GLY 717  715  715  GLY GLY B . n 
B 1 718  GLN 718  716  716  GLN GLN B . n 
B 1 719  ILE 719  717  717  ILE ILE B . n 
B 1 720  ALA 720  718  718  ALA ALA B . n 
B 1 721  ALA 721  719  719  ALA ALA B . n 
B 1 722  ALA 722  720  720  ALA ALA B . n 
B 1 723  LEU 723  721  721  LEU LEU B . n 
B 1 724  VAL 724  722  722  VAL VAL B . n 
B 1 725  ALA 725  723  723  ALA ALA B . n 
B 1 726  GLY 726  724  724  GLY GLY B . n 
B 1 727  ASN 727  725  725  ASN ASN B . n 
B 1 728  PRO 728  726  726  PRO PRO B . n 
B 1 729  VAL 729  727  727  VAL VAL B . n 
B 1 730  LEU 730  728  728  LEU LEU B . n 
B 1 731  ALA 731  729  729  ALA ALA B . n 
B 1 732  LYS 732  730  730  LYS LYS B . n 
B 1 733  PRO 733  731  731  PRO PRO B . n 
B 1 734  ALA 734  732  732  ALA ALA B . n 
B 1 735  GLU 735  733  733  GLU GLU B . n 
B 1 736  GLU 736  734  734  GLU GLU B . n 
B 1 737  THR 737  735  735  THR THR B . n 
B 1 738  PRO 738  736  736  PRO PRO B . n 
B 1 739  LEU 739  737  737  LEU LEU B . n 
B 1 740  ILE 740  738  738  ILE ILE B . n 
B 1 741  ALA 741  739  739  ALA ALA B . n 
B 1 742  ALA 742  740  740  ALA ALA B . n 
B 1 743  GLU 743  741  741  GLU GLU B . n 
B 1 744  GLY 744  742  742  GLY GLY B . n 
B 1 745  VAL 745  743  743  VAL VAL B . n 
B 1 746  ARG 746  744  744  ARG ARG B . n 
B 1 747  ILE 747  745  745  ILE ILE B . n 
B 1 748  LEU 748  746  746  LEU LEU B . n 
B 1 749  ARG 749  747  747  ARG ARG B . n 
B 1 750  GLU 750  748  748  GLU GLU B . n 
B 1 751  ALA 751  749  749  ALA ALA B . n 
B 1 752  GLY 752  750  750  GLY GLY B . n 
B 1 753  ILE 753  751  751  ILE ILE B . n 
B 1 754  PRO 754  752  752  PRO PRO B . n 
B 1 755  ALA 755  753  753  ALA ALA B . n 
B 1 756  SER 756  754  754  SER SER B . n 
B 1 757  ALA 757  755  755  ALA ALA B . n 
B 1 758  LEU 758  756  756  LEU LEU B . n 
B 1 759  GLN 759  757  757  GLN GLN B . n 
B 1 760  LEU 760  758  758  LEU LEU B . n 
B 1 761  LEU 761  759  759  LEU LEU B . n 
B 1 762  PRO 762  760  760  PRO PRO B . n 
B 1 763  GLY 763  761  761  GLY GLY B . n 
B 1 764  ASP 764  762  762  ASP ASP B . n 
B 1 765  GLY 765  763  763  GLY GLY B . n 
B 1 766  ARG 766  764  764  ARG ARG B . n 
B 1 767  VAL 767  765  765  VAL VAL B . n 
B 1 768  GLY 768  766  766  GLY GLY B . n 
B 1 769  ALA 769  767  767  ALA ALA B . n 
B 1 770  ALA 770  768  768  ALA ALA B . n 
B 1 771  LEU 771  769  769  LEU LEU B . n 
B 1 772  VAL 772  770  770  VAL VAL B . n 
B 1 773  ALA 773  771  771  ALA ALA B . n 
B 1 774  ALA 774  772  772  ALA ALA B . n 
B 1 775  ALA 775  773  773  ALA ALA B . n 
B 1 776  GLU 776  774  774  GLU GLU B . n 
B 1 777  THR 777  775  775  THR THR B . n 
B 1 778  ALA 778  776  776  ALA ALA B . n 
B 1 779  GLY 779  777  777  GLY GLY B . n 
B 1 780  VAL 780  778  778  VAL VAL B . n 
B 1 781  MET 781  779  779  MET MET B . n 
B 1 782  PHE 782  780  780  PHE PHE B . n 
B 1 783  THR 783  781  781  THR THR B . n 
B 1 784  GLY 784  782  782  GLY GLY B . n 
B 1 785  SER 785  783  783  SER SER B . n 
B 1 786  THR 786  784  784  THR THR B . n 
B 1 787  GLU 787  785  785  GLU GLU B . n 
B 1 788  VAL 788  786  786  VAL VAL B . n 
B 1 789  ALA 789  787  787  ALA ALA B . n 
B 1 790  ARG 790  788  788  ARG ARG B . n 
B 1 791  LEU 791  789  789  LEU LEU B . n 
B 1 792  ILE 792  790  790  ILE ILE B . n 
B 1 793  GLN 793  791  791  GLN GLN B . n 
B 1 794  ALA 794  792  792  ALA ALA B . n 
B 1 795  GLN 795  793  793  GLN GLN B . n 
B 1 796  LEU 796  794  794  LEU LEU B . n 
B 1 797  ALA 797  795  795  ALA ALA B . n 
B 1 798  ASP 798  796  796  ASP ASP B . n 
B 1 799  ARG 799  797  797  ARG ARG B . n 
B 1 800  LEU 800  798  798  LEU LEU B . n 
B 1 801  SER 801  799  799  SER SER B . n 
B 1 802  PRO 802  800  800  PRO PRO B . n 
B 1 803  ALA 803  801  801  ALA ALA B . n 
B 1 804  GLY 804  802  802  GLY GLY B . n 
B 1 805  ARG 805  803  803  ARG ARG B . n 
B 1 806  PRO 806  804  804  PRO PRO B . n 
B 1 807  ILE 807  805  805  ILE ILE B . n 
B 1 808  PRO 808  806  806  PRO PRO B . n 
B 1 809  LEU 809  807  807  LEU LEU B . n 
B 1 810  ILE 810  808  808  ILE ILE B . n 
B 1 811  ALA 811  809  809  ALA ALA B . n 
B 1 812  GLU 812  810  810  GLU GLU B . n 
B 1 813  THR 813  811  811  THR THR B . n 
B 1 814  GLY 814  812  812  GLY GLY B . n 
B 1 815  GLY 815  813  813  GLY GLY B . n 
B 1 816  GLN 816  814  814  GLN GLN B . n 
B 1 817  ASN 817  815  815  ASN ASN B . n 
B 1 818  ALA 818  816  816  ALA ALA B . n 
B 1 819  MET 819  817  817  MET MET B . n 
B 1 820  ILE 820  818  818  ILE ILE B . n 
B 1 821  VAL 821  819  819  VAL VAL B . n 
B 1 822  ASP 822  820  820  ASP ASP B . n 
B 1 823  SER 823  821  821  SER SER B . n 
B 1 824  SER 824  822  822  SER SER B . n 
B 1 825  ALA 825  823  823  ALA ALA B . n 
B 1 826  LEU 826  824  824  LEU LEU B . n 
B 1 827  ALA 827  825  825  ALA ALA B . n 
B 1 828  GLU 828  826  826  GLU GLU B . n 
B 1 829  GLN 829  827  827  GLN GLN B . n 
B 1 830  VAL 830  828  828  VAL VAL B . n 
B 1 831  VAL 831  829  829  VAL VAL B . n 
B 1 832  GLY 832  830  830  GLY GLY B . n 
B 1 833  ASP 833  831  831  ASP ASP B . n 
B 1 834  VAL 834  832  832  VAL VAL B . n 
B 1 835  ILE 835  833  833  ILE ILE B . n 
B 1 836  THR 836  834  834  THR THR B . n 
B 1 837  SER 837  835  835  SER SER B . n 
B 1 838  ALA 838  836  836  ALA ALA B . n 
B 1 839  PHE 839  837  837  PHE PHE B . n 
B 1 840  ASP 840  838  838  ASP ASP B . n 
B 1 841  SER 841  839  839  SER SER B . n 
B 1 842  ALA 842  840  840  ALA ALA B . n 
B 1 843  GLY 843  841  841  GLY GLY B . n 
B 1 844  GLN 844  842  842  GLN GLN B . n 
B 1 845  ARG 845  843  843  ARG ARG B . n 
B 1 846  CYS 846  844  844  CYS CYS B . n 
B 1 847  SER 847  845  845  SER SER B . n 
B 1 848  ALA 848  846  846  ALA ALA B . n 
B 1 849  LEU 849  847  847  LEU LEU B . n 
B 1 850  ARG 850  848  848  ARG ARG B . n 
B 1 851  VAL 851  849  849  VAL VAL B . n 
B 1 852  LEU 852  850  850  LEU LEU B . n 
B 1 853  CYS 853  851  851  CYS CYS B . n 
B 1 854  LEU 854  852  852  LEU LEU B . n 
B 1 855  GLN 855  853  853  GLN GLN B . n 
B 1 856  GLU 856  854  854  GLU GLU B . n 
B 1 857  ASP 857  855  855  ASP ASP B . n 
B 1 858  VAL 858  856  856  VAL VAL B . n 
B 1 859  ALA 859  857  857  ALA ALA B . n 
B 1 860  ASP 860  858  858  ASP ASP B . n 
B 1 861  ARG 861  859  859  ARG ARG B . n 
B 1 862  ILE 862  860  860  ILE ILE B . n 
B 1 863  LEU 863  861  861  LEU LEU B . n 
B 1 864  THR 864  862  862  THR THR B . n 
B 1 865  MET 865  863  863  MET MET B . n 
B 1 866  LEU 866  864  864  LEU LEU B . n 
B 1 867  LYS 867  865  865  LYS LYS B . n 
B 1 868  GLY 868  866  866  GLY GLY B . n 
B 1 869  ALA 869  867  867  ALA ALA B . n 
B 1 870  LEU 870  868  868  LEU LEU B . n 
B 1 871  HIS 871  869  869  HIS HIS B . n 
B 1 872  GLU 872  870  870  GLU GLU B . n 
B 1 873  LEU 873  871  871  LEU LEU B . n 
B 1 874  HIS 874  872  872  HIS HIS B . n 
B 1 875  ILE 875  873  873  ILE ILE B . n 
B 1 876  GLY 876  874  874  GLY GLY B . n 
B 1 877  ARG 877  875  875  ARG ARG B . n 
B 1 878  THR 878  876  876  THR THR B . n 
B 1 879  ASP 879  877  877  ASP ASP B . n 
B 1 880  ARG 880  878  878  ARG ARG B . n 
B 1 881  LEU 881  879  879  LEU LEU B . n 
B 1 882  SER 882  880  880  SER SER B . n 
B 1 883  VAL 883  881  881  VAL VAL B . n 
B 1 884  ASP 884  882  882  ASP ASP B . n 
B 1 885  VAL 885  883  883  VAL VAL B . n 
B 1 886  GLY 886  884  884  GLY GLY B . n 
B 1 887  PRO 887  885  885  PRO PRO B . n 
B 1 888  VAL 888  886  886  VAL VAL B . n 
B 1 889  ILE 889  887  887  ILE ILE B . n 
B 1 890  THR 890  888  888  THR THR B . n 
B 1 891  SER 891  889  889  SER SER B . n 
B 1 892  GLU 892  890  890  GLU GLU B . n 
B 1 893  ALA 893  891  891  ALA ALA B . n 
B 1 894  LYS 894  892  892  LYS LYS B . n 
B 1 895  ASP 895  893  893  ASP ASP B . n 
B 1 896  ASN 896  894  894  ASN ASN B . n 
B 1 897  ILE 897  895  895  ILE ILE B . n 
B 1 898  GLU 898  896  896  GLU GLU B . n 
B 1 899  LYS 899  897  897  LYS LYS B . n 
B 1 900  HIS 900  898  898  HIS HIS B . n 
B 1 901  ILE 901  899  899  ILE ILE B . n 
B 1 902  GLU 902  900  900  GLU GLU B . n 
B 1 903  ARG 903  901  901  ARG ARG B . n 
B 1 904  MET 904  902  902  MET MET B . n 
B 1 905  ARG 905  903  903  ARG ARG B . n 
B 1 906  GLY 906  904  904  GLY GLY B . n 
B 1 907  LEU 907  905  905  LEU LEU B . n 
B 1 908  GLY 908  906  906  GLY GLY B . n 
B 1 909  ARG 909  907  907  ARG ARG B . n 
B 1 910  LYS 910  908  908  LYS LYS B . n 
B 1 911  VAL 911  909  909  VAL VAL B . n 
B 1 912  GLU 912  910  910  GLU GLU B . n 
B 1 913  GLN 913  911  911  GLN GLN B . n 
B 1 914  ILE 914  912  912  ILE ILE B . n 
B 1 915  GLY 915  913  913  GLY GLY B . n 
B 1 916  LEU 916  914  914  LEU LEU B . n 
B 1 917  ALA 917  915  915  ALA ALA B . n 
B 1 918  SER 918  916  916  SER SER B . n 
B 1 919  GLU 919  917  917  GLU GLU B . n 
B 1 920  THR 920  918  918  THR THR B . n 
B 1 921  GLY 921  919  919  GLY GLY B . n 
B 1 922  VAL 922  920  920  VAL VAL B . n 
B 1 923  GLY 923  921  921  GLY GLY B . n 
B 1 924  THR 924  922  922  THR THR B . n 
B 1 925  PHE 925  923  923  PHE PHE B . n 
B 1 926  VAL 926  924  924  VAL VAL B . n 
B 1 927  PRO 927  925  925  PRO PRO B . n 
B 1 928  PRO 928  926  926  PRO PRO B . n 
B 1 929  THR 929  927  927  THR THR B . n 
B 1 930  ILE 930  928  928  ILE ILE B . n 
B 1 931  ILE 931  929  929  ILE ILE B . n 
B 1 932  GLU 932  930  930  GLU GLU B . n 
B 1 933  LEU 933  931  931  LEU LEU B . n 
B 1 934  GLU 934  932  932  GLU GLU B . n 
B 1 935  LYS 935  933  933  LYS LYS B . n 
B 1 936  LEU 936  934  934  LEU LEU B . n 
B 1 937  SER 937  935  935  SER SER B . n 
B 1 938  ASP 938  936  936  ASP ASP B . n 
B 1 939  LEU 939  937  937  LEU LEU B . n 
B 1 940  GLN 940  938  938  GLN GLN B . n 
B 1 941  ARG 941  939  939  ARG ARG B . n 
B 1 942  GLU 942  940  940  GLU GLU B . n 
B 1 943  VAL 943  941  941  VAL VAL B . n 
B 1 944  PHE 944  942  942  PHE PHE B . n 
B 1 945  GLY 945  943  943  GLY GLY B . n 
B 1 946  PRO 946  944  944  PRO PRO B . n 
B 1 947  VAL 947  945  945  VAL VAL B . n 
B 1 948  LEU 948  946  946  LEU LEU B . n 
B 1 949  HIS 949  947  947  HIS HIS B . n 
B 1 950  VAL 950  948  948  VAL VAL B . n 
B 1 951  ILE 951  949  949  ILE ILE B . n 
B 1 952  ARG 952  950  950  ARG ARG B . n 
B 1 953  TYR 953  951  951  TYR TYR B . n 
B 1 954  ARG 954  952  952  ARG ARG B . n 
B 1 955  ARG 955  953  953  ARG ARG B . n 
B 1 956  ASP 956  954  954  ASP ASP B . n 
B 1 957  ASP 957  955  955  ASP ASP B . n 
B 1 958  LEU 958  956  956  LEU LEU B . n 
B 1 959  ASP 959  957  957  ASP ASP B . n 
B 1 960  ARG 960  958  958  ARG ARG B . n 
B 1 961  LEU 961  959  959  LEU LEU B . n 
B 1 962  VAL 962  960  960  VAL VAL B . n 
B 1 963  ASP 963  961  961  ASP ASP B . n 
B 1 964  ASP 964  962  962  ASP ASP B . n 
B 1 965  VAL 965  963  963  VAL VAL B . n 
B 1 966  ASN 966  964  964  ASN ASN B . n 
B 1 967  ALA 967  965  965  ALA ALA B . n 
B 1 968  THR 968  966  966  THR THR B . n 
B 1 969  GLY 969  967  967  GLY GLY B . n 
B 1 970  TYR 970  968  968  TYR TYR B . n 
B 1 971  GLY 971  969  969  GLY GLY B . n 
B 1 972  LEU 972  970  970  LEU LEU B . n 
B 1 973  THR 973  971  971  THR THR B . n 
B 1 974  PHE 974  972  972  PHE PHE B . n 
B 1 975  GLY 975  973  973  GLY GLY B . n 
B 1 976  LEU 976  974  974  LEU LEU B . n 
B 1 977  HIS 977  975  975  HIS HIS B . n 
B 1 978  THR 978  976  976  THR THR B . n 
B 1 979  ARG 979  977  977  ARG ARG B . n 
B 1 980  LEU 980  978  978  LEU LEU B . n 
B 1 981  ASP 981  979  979  ASP ASP B . n 
B 1 982  GLU 982  980  980  GLU GLU B . n 
B 1 983  THR 983  981  981  THR THR B . n 
B 1 984  ILE 984  982  982  ILE ILE B . n 
B 1 985  ALA 985  983  983  ALA ALA B . n 
B 1 986  HIS 986  984  984  HIS HIS B . n 
B 1 987  VAL 987  985  985  VAL VAL B . n 
B 1 988  THR 988  986  986  THR THR B . n 
B 1 989  SER 989  987  987  SER SER B . n 
B 1 990  ARG 990  988  988  ARG ARG B . n 
B 1 991  ILE 991  989  989  ILE ILE B . n 
B 1 992  LYS 992  990  990  LYS LYS B . n 
B 1 993  ALA 993  991  991  ALA ALA B . n 
B 1 994  GLY 994  992  992  GLY GLY B . n 
B 1 995  ASN 995  993  993  ASN ASN B . n 
B 1 996  LEU 996  994  994  LEU LEU B . n 
B 1 997  TYR 997  995  995  TYR TYR B . n 
B 1 998  ILE 998  996  996  ILE ILE B . n 
B 1 999  ASN 999  997  997  ASN ASN B . n 
B 1 1000 ARG 1000 998  998  ARG ARG B . n 
B 1 1001 ASN 1001 999  999  ASN ASN B . n 
B 1 1002 ILE 1002 1000 1000 ILE ILE B . n 
B 1 1003 ILE 1003 1001 1001 ILE ILE B . n 
B 1 1004 GLY 1004 1002 1002 GLY GLY B . n 
B 1 1005 ALA 1005 1003 1003 ALA ALA B . n 
B 1 1006 VAL 1006 1004 1004 VAL VAL B . n 
B 1 1007 VAL 1007 1005 1005 VAL VAL B . n 
B 1 1008 GLY 1008 1006 1006 GLY GLY B . n 
B 1 1009 VAL 1009 1007 1007 VAL VAL B . n 
B 1 1010 GLN 1010 1008 1008 GLN GLN B . n 
B 1 1011 PRO 1011 1009 1009 PRO PRO B . n 
B 1 1012 PHE 1012 1010 1010 PHE PHE B . n 
B 1 1013 GLY 1013 1011 1011 GLY GLY B . n 
B 1 1014 GLY 1014 1012 1012 GLY GLY B . n 
B 1 1015 ARG 1015 1013 1013 ARG ARG B . n 
B 1 1016 GLY 1016 1014 1014 GLY GLY B . n 
B 1 1017 LEU 1017 1015 1015 LEU LEU B . n 
B 1 1018 SER 1018 1016 1016 SER SER B . n 
B 1 1019 GLY 1019 1017 1017 GLY GLY B . n 
B 1 1020 THR 1020 1018 1018 THR THR B . n 
B 1 1021 GLY 1021 1019 1019 GLY GLY B . n 
B 1 1022 PRO 1022 1020 1020 PRO PRO B . n 
B 1 1023 LYS 1023 1021 1021 LYS LYS B . n 
B 1 1024 ALA 1024 1022 1022 ALA ALA B . n 
B 1 1025 GLY 1025 1023 1023 GLY GLY B . n 
B 1 1026 GLY 1026 1024 1024 GLY GLY B . n 
B 1 1027 PRO 1027 1025 1025 PRO PRO B . n 
B 1 1028 LEU 1028 1026 1026 LEU LEU B . n 
B 1 1029 TYR 1029 1027 1027 TYR TYR B . n 
B 1 1030 LEU 1030 1028 1028 LEU LEU B . n 
B 1 1031 GLY 1031 1029 1029 GLY GLY B . n 
B 1 1032 ARG 1032 1030 1030 ARG ARG B . n 
B 1 1033 LEU 1033 1031 1031 LEU LEU B . n 
B 1 1034 VAL 1034 1032 1032 VAL VAL B . n 
B 1 1035 THR 1035 1033 1033 THR THR B . n 
B 1 1036 THR 1036 1034 1034 THR THR B . n 
B 1 1037 ALA 1037 1035 1035 ALA ALA B . n 
B 1 1038 PRO 1038 1036 1036 PRO PRO B . n 
B 1 1039 VAL 1039 1037 1037 VAL VAL B . n 
B 1 1040 PRO 1040 1038 1038 PRO PRO B . n 
B 1 1041 PRO 1041 1039 1039 PRO PRO B . n 
B 1 1042 GLN 1042 1040 1040 GLN GLN B . n 
B 1 1043 HIS 1043 1041 1041 HIS HIS B . n 
B 1 1044 SER 1044 1042 1042 SER SER B . n 
B 1 1045 SER 1045 1043 1043 SER SER B . n 
B 1 1046 VAL 1046 1044 1044 VAL VAL B . n 
B 1 1047 HIS 1047 1045 1045 HIS HIS B . n 
B 1 1048 THR 1048 1046 1046 THR THR B . n 
B 1 1049 ASP 1049 1047 1047 ASP ASP B . n 
B 1 1050 PRO 1050 1048 1048 PRO PRO B . n 
B 1 1051 VAL 1051 1049 1049 VAL VAL B . n 
B 1 1052 LEU 1052 1050 1050 LEU LEU B . n 
B 1 1053 LEU 1053 1051 1051 LEU LEU B . n 
B 1 1054 ASP 1054 1052 1052 ASP ASP B . n 
B 1 1055 PHE 1055 1053 1053 PHE PHE B . n 
B 1 1056 ALA 1056 1054 1054 ALA ALA B . n 
B 1 1057 LYS 1057 1055 1055 LYS LYS B . n 
B 1 1058 TRP 1058 1056 1056 TRP TRP B . n 
B 1 1059 LEU 1059 1057 1057 LEU LEU B . n 
B 1 1060 ASP 1060 1058 1058 ASP ASP B . n 
B 1 1061 GLY 1061 1059 1059 GLY GLY B . n 
B 1 1062 LYS 1062 1060 1060 LYS LYS B . n 
B 1 1063 GLY 1063 1061 1061 GLY GLY B . n 
B 1 1064 ALA 1064 1062 1062 ALA ALA B . n 
B 1 1065 ARG 1065 1063 1063 ARG ARG B . n 
B 1 1066 ALA 1066 1064 1064 ALA ALA B . n 
B 1 1067 GLU 1067 1065 1065 GLU GLU B . n 
B 1 1068 ALA 1068 1066 1066 ALA ALA B . n 
B 1 1069 GLU 1069 1067 1067 GLU GLU B . n 
B 1 1070 ALA 1070 1068 1068 ALA ALA B . n 
B 1 1071 ALA 1071 1069 1069 ALA ALA B . n 
B 1 1072 ARG 1072 1070 1070 ARG ARG B . n 
B 1 1073 ASN 1073 1071 1071 ASN ASN B . n 
B 1 1074 ALA 1074 1072 1072 ALA ALA B . n 
B 1 1075 GLY 1075 1073 1073 GLY GLY B . n 
B 1 1076 SER 1076 1074 1074 SER SER B . n 
B 1 1077 SER 1077 1075 1075 SER SER B . n 
B 1 1078 SER 1078 1076 1076 SER SER B . n 
B 1 1079 ALA 1079 1077 1077 ALA ALA B . n 
B 1 1080 LEU 1080 1078 1078 LEU LEU B . n 
B 1 1081 GLY 1081 1079 1079 GLY GLY B . n 
B 1 1082 LEU 1082 1080 1080 LEU LEU B . n 
B 1 1083 ASP 1083 1081 1081 ASP ASP B . n 
B 1 1084 LEU 1084 1082 1082 LEU LEU B . n 
B 1 1085 GLU 1085 1083 1083 GLU GLU B . n 
B 1 1086 LEU 1086 1084 1084 LEU LEU B . n 
B 1 1087 PRO 1087 1085 1085 PRO PRO B . n 
B 1 1088 GLY 1088 1086 1086 GLY GLY B . n 
B 1 1089 PRO 1089 1087 1087 PRO PRO B . n 
B 1 1090 VAL 1090 1088 1088 VAL VAL B . n 
B 1 1091 GLY 1091 1089 1089 GLY GLY B . n 
B 1 1092 GLU 1092 1090 1090 GLU GLU B . n 
B 1 1093 ARG 1093 1091 1091 ARG ARG B . n 
B 1 1094 ASN 1094 1092 1092 ASN ASN B . n 
B 1 1095 LEU 1095 1093 1093 LEU LEU B . n 
B 1 1096 TYR 1096 1094 1094 TYR TYR B . n 
B 1 1097 THR 1097 1095 1095 THR THR B . n 
B 1 1098 LEU 1098 1096 1096 LEU LEU B . n 
B 1 1099 HIS 1099 1097 1097 HIS HIS B . n 
B 1 1100 ALA 1100 1098 1098 ALA ALA B . n 
B 1 1101 ARG 1101 1099 1099 ARG ARG B . n 
B 1 1102 GLY 1102 1100 1100 GLY GLY B . n 
B 1 1103 ARG 1103 1101 1101 ARG ARG B . n 
B 1 1104 ILE 1104 1102 1102 ILE ILE B . n 
B 1 1105 LEU 1105 1103 1103 LEU LEU B . n 
B 1 1106 LEU 1106 1104 1104 LEU LEU B . n 
B 1 1107 VAL 1107 1105 1105 VAL VAL B . n 
B 1 1108 PRO 1108 1106 1106 PRO PRO B . n 
B 1 1109 ALA 1109 1107 1107 ALA ALA B . n 
B 1 1110 THR 1110 1108 1108 THR THR B . n 
B 1 1111 GLU 1111 1109 1109 GLU GLU B . n 
B 1 1112 SER 1112 1110 1110 SER SER B . n 
B 1 1113 GLY 1113 1111 1111 GLY GLY B . n 
B 1 1114 LEU 1114 1112 1112 LEU LEU B . n 
B 1 1115 TYR 1115 1113 1113 TYR TYR B . n 
B 1 1116 HIS 1116 1114 1114 HIS HIS B . n 
B 1 1117 GLN 1117 1115 1115 GLN GLN B . n 
B 1 1118 LEU 1118 1116 1116 LEU LEU B . n 
B 1 1119 ALA 1119 1117 1117 ALA ALA B . n 
B 1 1120 ALA 1120 1118 1118 ALA ALA B . n 
B 1 1121 ALA 1121 1119 1119 ALA ALA B . n 
B 1 1122 LEU 1122 1120 1120 LEU LEU B . n 
B 1 1123 ALA 1123 1121 1121 ALA ALA B . n 
B 1 1124 THR 1124 1122 1122 THR THR B . n 
B 1 1125 GLY 1125 1123 1123 GLY GLY B . n 
B 1 1126 ASN 1126 1124 1124 ASN ASN B . n 
B 1 1127 SER 1127 1125 1125 SER SER B . n 
B 1 1128 VAL 1128 1126 1126 VAL VAL B . n 
B 1 1129 ALA 1129 1127 1127 ALA ALA B . n 
B 1 1130 ILE 1130 1128 1128 ILE ILE B . n 
B 1 1131 ASP 1131 1129 1129 ASP ASP B . n 
B 1 1132 ALA 1132 1130 1130 ALA ALA B . n 
B 1 1133 ALA 1133 1131 1131 ALA ALA B . n 
B 1 1134 SER 1134 1132 1132 SER SER B . n 
B 1 1135 GLY 1135 1133 1133 GLY GLY B . n 
B 1 1136 LEU 1136 1134 1134 LEU LEU B . n 
B 1 1137 GLN 1137 1135 1135 GLN GLN B . n 
B 1 1138 ALA 1138 1136 1136 ALA ALA B . n 
B 1 1139 SER 1139 1137 1137 SER SER B . n 
B 1 1140 LEU 1140 1138 1138 LEU LEU B . n 
B 1 1141 LYS 1141 1139 1139 LYS LYS B . n 
B 1 1142 ASN 1142 1140 1140 ASN ASN B . n 
B 1 1143 LEU 1143 1141 1141 LEU LEU B . n 
B 1 1144 PRO 1144 1142 1142 PRO PRO B . n 
B 1 1145 GLN 1145 1143 1143 GLN GLN B . n 
B 1 1146 THR 1146 1144 1144 THR THR B . n 
B 1 1147 VAL 1147 1145 1145 VAL VAL B . n 
B 1 1148 GLY 1148 1146 1146 GLY GLY B . n 
B 1 1149 LEU 1149 1147 1147 LEU LEU B . n 
B 1 1150 ARG 1150 1148 1148 ARG ARG B . n 
B 1 1151 VAL 1151 1149 1149 VAL VAL B . n 
B 1 1152 SER 1152 1150 1150 SER SER B . n 
B 1 1153 TRP 1153 1151 1151 TRP TRP B . n 
B 1 1154 SER 1154 1152 1152 SER SER B . n 
B 1 1155 LYS 1155 1153 1153 LYS LYS B . n 
B 1 1156 ASP 1156 1154 1154 ASP ASP B . n 
B 1 1157 TRP 1157 1155 1155 TRP TRP B . n 
B 1 1158 ALA 1158 1156 1156 ALA ALA B . n 
B 1 1159 ALA 1159 1157 1157 ALA ALA B . n 
B 1 1160 ASP 1160 1158 1158 ASP ASP B . n 
B 1 1161 GLY 1161 1159 1159 GLY GLY B . n 
B 1 1162 PRO 1162 1160 1160 PRO PRO B . n 
B 1 1163 PHE 1163 1161 1161 PHE PHE B . n 
B 1 1164 ALA 1164 1162 1162 ALA ALA B . n 
B 1 1165 GLY 1165 1163 1163 GLY GLY B . n 
B 1 1166 ALA 1166 1164 1164 ALA ALA B . n 
B 1 1167 LEU 1167 1165 1165 LEU LEU B . n 
B 1 1168 VAL 1168 1166 1166 VAL VAL B . n 
B 1 1169 GLU 1169 1167 1167 GLU GLU B . n 
B 1 1170 GLY 1170 1168 1168 GLY GLY B . n 
B 1 1171 ASP 1171 1169 1169 ASP ASP B . n 
B 1 1172 ALA 1172 1170 1170 ALA ALA B . n 
B 1 1173 GLU 1173 1171 1171 GLU GLU B . n 
B 1 1174 ARG 1174 1172 1172 ARG ARG B . n 
B 1 1175 ILE 1175 1173 1173 ILE ILE B . n 
B 1 1176 ARG 1176 1174 1174 ARG ARG B . n 
B 1 1177 ALA 1177 1175 1175 ALA ALA B . n 
B 1 1178 VAL 1178 1176 1176 VAL VAL B . n 
B 1 1179 ASN 1179 1177 1177 ASN ASN B . n 
B 1 1180 LYS 1180 1178 1178 LYS LYS B . n 
B 1 1181 ALA 1181 1179 1179 ALA ALA B . n 
B 1 1182 ILE 1182 1180 1180 ILE ILE B . n 
B 1 1183 ALA 1183 1181 1181 ALA ALA B . n 
B 1 1184 ALA 1184 1182 1182 ALA ALA B . n 
B 1 1185 LEU 1185 1183 1183 LEU LEU B . n 
B 1 1186 PRO 1186 1184 1184 PRO PRO B . n 
B 1 1187 GLY 1187 1185 1185 GLY GLY B . n 
B 1 1188 PRO 1188 1186 1186 PRO PRO B . n 
B 1 1189 LEU 1189 1187 1187 LEU LEU B . n 
B 1 1190 LEU 1190 1188 1188 LEU LEU B . n 
B 1 1191 LEU 1191 1189 1189 LEU LEU B . n 
B 1 1192 VAL 1192 1190 1190 VAL VAL B . n 
B 1 1193 GLN 1193 1191 1191 GLN GLN B . n 
B 1 1194 ALA 1194 1192 1192 ALA ALA B . n 
B 1 1195 ALA 1195 1193 1193 ALA ALA B . n 
B 1 1196 SER 1196 1194 1194 SER SER B . n 
B 1 1197 SER 1197 1195 1195 SER SER B . n 
B 1 1198 GLY 1198 1196 1196 GLY GLY B . n 
B 1 1199 GLU 1199 1197 1197 GLU GLU B . n 
B 1 1200 ILE 1200 1198 1198 ILE ILE B . n 
B 1 1201 ALA 1201 1199 1199 ALA ALA B . n 
B 1 1202 ARG 1202 1200 1200 ARG ARG B . n 
B 1 1203 ASN 1203 1201 1201 ASN ASN B . n 
B 1 1204 PRO 1204 1202 1202 PRO PRO B . n 
B 1 1205 ASP 1205 1203 1203 ASP ASP B . n 
B 1 1206 ALA 1206 1204 1204 ALA ALA B . n 
B 1 1207 TYR 1207 1205 1205 TYR TYR B . n 
B 1 1208 CYS 1208 1206 1206 CYS CYS B . n 
B 1 1209 LEU 1209 1207 1207 LEU LEU B . n 
B 1 1210 ASN 1210 1208 1208 ASN ASN B . n 
B 1 1211 TRP 1211 1209 1209 TRP TRP B . n 
B 1 1212 LEU 1212 1210 1210 LEU LEU B . n 
B 1 1213 VAL 1213 1211 1211 VAL VAL B . n 
B 1 1214 GLU 1214 1212 1212 GLU GLU B . n 
B 1 1215 GLU 1215 1213 1213 GLU GLU B . n 
B 1 1216 VAL 1216 1214 1214 VAL VAL B . n 
B 1 1217 SER 1217 1215 1215 SER SER B . n 
B 1 1218 ALA 1218 1216 1216 ALA ALA B . n 
B 1 1219 SER 1219 1217 1217 SER SER B . n 
B 1 1220 ILE 1220 1218 1218 ILE ILE B . n 
B 1 1221 ASN 1221 1219 1219 ASN ASN B . n 
B 1 1222 THR 1222 1220 1220 THR THR B . n 
B 1 1223 ALA 1223 1221 1221 ALA ALA B . n 
B 1 1224 ALA 1224 1222 1222 ALA ALA B . n 
B 1 1225 ALA 1225 1223 ?    ?   ?   B . n 
B 1 1226 GLY 1226 1224 ?    ?   ?   B . n 
B 1 1227 GLY 1227 1225 ?    ?   ?   B . n 
B 1 1228 ASN 1228 1226 ?    ?   ?   B . n 
B 1 1229 ALA 1229 1227 ?    ?   ?   B . n 
B 1 1230 SER 1230 1228 ?    ?   ?   B . n 
B 1 1231 LEU 1231 1229 ?    ?   ?   B . n 
B 1 1232 MET 1232 1230 ?    ?   ?   B . n 
B 1 1233 ALA 1233 1231 ?    ?   ?   B . n 
B 1 1234 ILE 1234 1232 ?    ?   ?   B . n 
B 1 1235 GLY 1235 1233 ?    ?   ?   B . 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 FAD ? ? FAD ? ? 'SUBJECT OF INVESTIGATION' ? 
2 PYS ? ? PYS ? ? '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 
C  2 PGE 1   1301 1301 PGE PGE A . 
D  3 PEG 1   1302 1302 PEG PEG A . 
E  4 PYS 1   1303 1303 PYS PYS A . 
F  3 PEG 1   1304 1304 PEG PEG A . 
G  3 PEG 1   1305 1305 PEG PEG A . 
H  3 PEG 1   1306 1306 PEG PEG A . 
I  5 FMT 1   1307 1307 FMT FMT A . 
J  3 PEG 1   1308 1308 PEG PEG A . 
K  6 SO4 1   1309 2    SO4 SO4 A . 
L  6 SO4 1   1310 3    SO4 SO4 A . 
M  6 SO4 1   1311 4    SO4 SO4 A . 
N  6 SO4 1   1312 5    SO4 SO4 A . 
O  7 FAD 1   1313 2001 FAD FAD A . 
P  2 PGE 1   1301 1301 PGE PGE B . 
Q  3 PEG 1   1302 1303 PEG PEG B . 
R  4 PYS 1   1303 1304 PYS PYS B . 
S  3 PEG 1   1304 1305 PEG PEG B . 
T  3 PEG 1   1305 1307 PEG PEG B . 
U  5 FMT 1   1306 1308 FMT FMT B . 
V  5 FMT 1   1307 1310 FMT FMT B . 
W  6 SO4 1   1308 1    SO4 SO4 B . 
X  6 SO4 1   1309 6    SO4 SO4 B . 
Y  7 FAD 1   1310 2001 FAD FAD B . 
Z  8 HOH 1   1401 1385 HOH HOH A . 
Z  8 HOH 2   1402 955  HOH HOH A . 
Z  8 HOH 3   1403 635  HOH HOH A . 
Z  8 HOH 4   1404 557  HOH HOH A . 
Z  8 HOH 5   1405 656  HOH HOH A . 
Z  8 HOH 6   1406 402  HOH HOH A . 
Z  8 HOH 7   1407 558  HOH HOH A . 
Z  8 HOH 8   1408 982  HOH HOH A . 
Z  8 HOH 9   1409 683  HOH HOH A . 
Z  8 HOH 10  1410 662  HOH HOH A . 
Z  8 HOH 11  1411 1209 HOH HOH A . 
Z  8 HOH 12  1412 716  HOH HOH A . 
Z  8 HOH 13  1413 207  HOH HOH A . 
Z  8 HOH 14  1414 272  HOH HOH A . 
Z  8 HOH 15  1415 1316 HOH HOH A . 
Z  8 HOH 16  1416 464  HOH HOH A . 
Z  8 HOH 17  1417 1544 HOH HOH A . 
Z  8 HOH 18  1418 1130 HOH HOH A . 
Z  8 HOH 19  1419 407  HOH HOH A . 
Z  8 HOH 20  1420 694  HOH HOH A . 
Z  8 HOH 21  1421 625  HOH HOH A . 
Z  8 HOH 22  1422 1171 HOH HOH A . 
Z  8 HOH 23  1423 243  HOH HOH A . 
Z  8 HOH 24  1424 9    HOH HOH A . 
Z  8 HOH 25  1425 1321 HOH HOH A . 
Z  8 HOH 26  1426 1387 HOH HOH A . 
Z  8 HOH 27  1427 171  HOH HOH A . 
Z  8 HOH 28  1428 230  HOH HOH A . 
Z  8 HOH 29  1429 148  HOH HOH A . 
Z  8 HOH 30  1430 168  HOH HOH A . 
Z  8 HOH 31  1431 559  HOH HOH A . 
Z  8 HOH 32  1432 368  HOH HOH A . 
Z  8 HOH 33  1433 1255 HOH HOH A . 
Z  8 HOH 34  1434 240  HOH HOH A . 
Z  8 HOH 35  1435 1362 HOH HOH A . 
Z  8 HOH 36  1436 864  HOH HOH A . 
Z  8 HOH 37  1437 726  HOH HOH A . 
Z  8 HOH 38  1438 784  HOH HOH A . 
Z  8 HOH 39  1439 1486 HOH HOH A . 
Z  8 HOH 40  1440 561  HOH HOH A . 
Z  8 HOH 41  1441 325  HOH HOH A . 
Z  8 HOH 42  1442 1010 HOH HOH A . 
Z  8 HOH 43  1443 685  HOH HOH A . 
Z  8 HOH 44  1444 582  HOH HOH A . 
Z  8 HOH 45  1445 421  HOH HOH A . 
Z  8 HOH 46  1446 118  HOH HOH A . 
Z  8 HOH 47  1447 500  HOH HOH A . 
Z  8 HOH 48  1448 41   HOH HOH A . 
Z  8 HOH 49  1449 1406 HOH HOH A . 
Z  8 HOH 50  1450 102  HOH HOH A . 
Z  8 HOH 51  1451 545  HOH HOH A . 
Z  8 HOH 52  1452 89   HOH HOH A . 
Z  8 HOH 53  1453 528  HOH HOH A . 
Z  8 HOH 54  1454 273  HOH HOH A . 
Z  8 HOH 55  1455 880  HOH HOH A . 
Z  8 HOH 56  1456 515  HOH HOH A . 
Z  8 HOH 57  1457 91   HOH HOH A . 
Z  8 HOH 58  1458 1110 HOH HOH A . 
Z  8 HOH 59  1459 34   HOH HOH A . 
Z  8 HOH 60  1460 1275 HOH HOH A . 
Z  8 HOH 61  1461 547  HOH HOH A . 
Z  8 HOH 62  1462 1423 HOH HOH A . 
Z  8 HOH 63  1463 1279 HOH HOH A . 
Z  8 HOH 64  1464 1428 HOH HOH A . 
Z  8 HOH 65  1465 653  HOH HOH A . 
Z  8 HOH 66  1466 568  HOH HOH A . 
Z  8 HOH 67  1467 821  HOH HOH A . 
Z  8 HOH 68  1468 857  HOH HOH A . 
Z  8 HOH 69  1469 499  HOH HOH A . 
Z  8 HOH 70  1470 1327 HOH HOH A . 
Z  8 HOH 71  1471 1111 HOH HOH A . 
Z  8 HOH 72  1472 26   HOH HOH A . 
Z  8 HOH 73  1473 787  HOH HOH A . 
Z  8 HOH 74  1474 190  HOH HOH A . 
Z  8 HOH 75  1475 1032 HOH HOH A . 
Z  8 HOH 76  1476 525  HOH HOH A . 
Z  8 HOH 77  1477 1473 HOH HOH A . 
Z  8 HOH 78  1478 876  HOH HOH A . 
Z  8 HOH 79  1479 346  HOH HOH A . 
Z  8 HOH 80  1480 835  HOH HOH A . 
Z  8 HOH 81  1481 572  HOH HOH A . 
Z  8 HOH 82  1482 813  HOH HOH A . 
Z  8 HOH 83  1483 1028 HOH HOH A . 
Z  8 HOH 84  1484 264  HOH HOH A . 
Z  8 HOH 85  1485 1464 HOH HOH A . 
Z  8 HOH 86  1486 95   HOH HOH A . 
Z  8 HOH 87  1487 257  HOH HOH A . 
Z  8 HOH 88  1488 197  HOH HOH A . 
Z  8 HOH 89  1489 348  HOH HOH A . 
Z  8 HOH 90  1490 1211 HOH HOH A . 
Z  8 HOH 91  1491 1535 HOH HOH A . 
Z  8 HOH 92  1492 68   HOH HOH A . 
Z  8 HOH 93  1493 369  HOH HOH A . 
Z  8 HOH 94  1494 595  HOH HOH A . 
Z  8 HOH 95  1495 750  HOH HOH A . 
Z  8 HOH 96  1496 1246 HOH HOH A . 
Z  8 HOH 97  1497 263  HOH HOH A . 
Z  8 HOH 98  1498 697  HOH HOH A . 
Z  8 HOH 99  1499 231  HOH HOH A . 
Z  8 HOH 100 1500 614  HOH HOH A . 
Z  8 HOH 101 1501 158  HOH HOH A . 
Z  8 HOH 102 1502 731  HOH HOH A . 
Z  8 HOH 103 1503 1342 HOH HOH A . 
Z  8 HOH 104 1504 425  HOH HOH A . 
Z  8 HOH 105 1505 692  HOH HOH A . 
Z  8 HOH 106 1506 762  HOH HOH A . 
Z  8 HOH 107 1507 463  HOH HOH A . 
Z  8 HOH 108 1508 811  HOH HOH A . 
Z  8 HOH 109 1509 899  HOH HOH A . 
Z  8 HOH 110 1510 354  HOH HOH A . 
Z  8 HOH 111 1511 219  HOH HOH A . 
Z  8 HOH 112 1512 775  HOH HOH A . 
Z  8 HOH 113 1513 134  HOH HOH A . 
Z  8 HOH 114 1514 749  HOH HOH A . 
Z  8 HOH 115 1515 645  HOH HOH A . 
Z  8 HOH 116 1516 364  HOH HOH A . 
Z  8 HOH 117 1517 886  HOH HOH A . 
Z  8 HOH 118 1518 1314 HOH HOH A . 
Z  8 HOH 119 1519 521  HOH HOH A . 
Z  8 HOH 120 1520 746  HOH HOH A . 
Z  8 HOH 121 1521 399  HOH HOH A . 
Z  8 HOH 122 1522 183  HOH HOH A . 
Z  8 HOH 123 1523 1289 HOH HOH A . 
Z  8 HOH 124 1524 330  HOH HOH A . 
Z  8 HOH 125 1525 406  HOH HOH A . 
Z  8 HOH 126 1526 708  HOH HOH A . 
Z  8 HOH 127 1527 201  HOH HOH A . 
Z  8 HOH 128 1528 35   HOH HOH A . 
Z  8 HOH 129 1529 38   HOH HOH A . 
Z  8 HOH 130 1530 130  HOH HOH A . 
Z  8 HOH 131 1531 452  HOH HOH A . 
Z  8 HOH 132 1532 153  HOH HOH A . 
Z  8 HOH 133 1533 1474 HOH HOH A . 
Z  8 HOH 134 1534 342  HOH HOH A . 
Z  8 HOH 135 1535 224  HOH HOH A . 
Z  8 HOH 136 1536 131  HOH HOH A . 
Z  8 HOH 137 1537 203  HOH HOH A . 
Z  8 HOH 138 1538 1124 HOH HOH A . 
Z  8 HOH 139 1539 1261 HOH HOH A . 
Z  8 HOH 140 1540 398  HOH HOH A . 
Z  8 HOH 141 1541 375  HOH HOH A . 
Z  8 HOH 142 1542 191  HOH HOH A . 
Z  8 HOH 143 1543 460  HOH HOH A . 
Z  8 HOH 144 1544 599  HOH HOH A . 
Z  8 HOH 145 1545 826  HOH HOH A . 
Z  8 HOH 146 1546 210  HOH HOH A . 
Z  8 HOH 147 1547 270  HOH HOH A . 
Z  8 HOH 148 1548 738  HOH HOH A . 
Z  8 HOH 149 1549 687  HOH HOH A . 
Z  8 HOH 150 1550 84   HOH HOH A . 
Z  8 HOH 151 1551 493  HOH HOH A . 
Z  8 HOH 152 1552 447  HOH HOH A . 
Z  8 HOH 153 1553 508  HOH HOH A . 
Z  8 HOH 154 1554 459  HOH HOH A . 
Z  8 HOH 155 1555 767  HOH HOH A . 
Z  8 HOH 156 1556 560  HOH HOH A . 
Z  8 HOH 157 1557 1184 HOH HOH A . 
Z  8 HOH 158 1558 234  HOH HOH A . 
Z  8 HOH 159 1559 424  HOH HOH A . 
Z  8 HOH 160 1560 281  HOH HOH A . 
Z  8 HOH 161 1561 660  HOH HOH A . 
Z  8 HOH 162 1562 843  HOH HOH A . 
Z  8 HOH 163 1563 1348 HOH HOH A . 
Z  8 HOH 164 1564 216  HOH HOH A . 
Z  8 HOH 165 1565 250  HOH HOH A . 
Z  8 HOH 166 1566 518  HOH HOH A . 
Z  8 HOH 167 1567 30   HOH HOH A . 
Z  8 HOH 168 1568 108  HOH HOH A . 
Z  8 HOH 169 1569 331  HOH HOH A . 
Z  8 HOH 170 1570 303  HOH HOH A . 
Z  8 HOH 171 1571 502  HOH HOH A . 
Z  8 HOH 172 1572 1503 HOH HOH A . 
Z  8 HOH 173 1573 1550 HOH HOH A . 
Z  8 HOH 174 1574 643  HOH HOH A . 
Z  8 HOH 175 1575 1346 HOH HOH A . 
Z  8 HOH 176 1576 639  HOH HOH A . 
Z  8 HOH 177 1577 537  HOH HOH A . 
Z  8 HOH 178 1578 793  HOH HOH A . 
Z  8 HOH 179 1579 133  HOH HOH A . 
Z  8 HOH 180 1580 541  HOH HOH A . 
Z  8 HOH 181 1581 229  HOH HOH A . 
Z  8 HOH 182 1582 22   HOH HOH A . 
Z  8 HOH 183 1583 1382 HOH HOH A . 
Z  8 HOH 184 1584 204  HOH HOH A . 
Z  8 HOH 185 1585 389  HOH HOH A . 
Z  8 HOH 186 1586 1439 HOH HOH A . 
Z  8 HOH 187 1587 355  HOH HOH A . 
Z  8 HOH 188 1588 462  HOH HOH A . 
Z  8 HOH 189 1589 719  HOH HOH A . 
Z  8 HOH 190 1590 351  HOH HOH A . 
Z  8 HOH 191 1591 206  HOH HOH A . 
Z  8 HOH 192 1592 1402 HOH HOH A . 
Z  8 HOH 193 1593 125  HOH HOH A . 
Z  8 HOH 194 1594 1389 HOH HOH A . 
Z  8 HOH 195 1595 1532 HOH HOH A . 
Z  8 HOH 196 1596 429  HOH HOH A . 
Z  8 HOH 197 1597 101  HOH HOH A . 
Z  8 HOH 198 1598 90   HOH HOH A . 
Z  8 HOH 199 1599 65   HOH HOH A . 
Z  8 HOH 200 1600 573  HOH HOH A . 
Z  8 HOH 201 1601 550  HOH HOH A . 
Z  8 HOH 202 1602 1509 HOH HOH A . 
Z  8 HOH 203 1603 157  HOH HOH A . 
Z  8 HOH 204 1604 400  HOH HOH A . 
Z  8 HOH 205 1605 1212 HOH HOH A . 
Z  8 HOH 206 1606 222  HOH HOH A . 
Z  8 HOH 207 1607 307  HOH HOH A . 
Z  8 HOH 208 1608 1221 HOH HOH A . 
Z  8 HOH 209 1609 259  HOH HOH A . 
Z  8 HOH 210 1610 679  HOH HOH A . 
Z  8 HOH 211 1611 752  HOH HOH A . 
Z  8 HOH 212 1612 977  HOH HOH A . 
Z  8 HOH 213 1613 903  HOH HOH A . 
Z  8 HOH 214 1614 283  HOH HOH A . 
Z  8 HOH 215 1615 1030 HOH HOH A . 
Z  8 HOH 216 1616 1401 HOH HOH A . 
Z  8 HOH 217 1617 360  HOH HOH A . 
Z  8 HOH 218 1618 181  HOH HOH A . 
Z  8 HOH 219 1619 71   HOH HOH A . 
Z  8 HOH 220 1620 1126 HOH HOH A . 
Z  8 HOH 221 1621 376  HOH HOH A . 
Z  8 HOH 222 1622 162  HOH HOH A . 
Z  8 HOH 223 1623 644  HOH HOH A . 
Z  8 HOH 224 1624 132  HOH HOH A . 
Z  8 HOH 225 1625 633  HOH HOH A . 
Z  8 HOH 226 1626 832  HOH HOH A . 
Z  8 HOH 227 1627 388  HOH HOH A . 
Z  8 HOH 228 1628 1002 HOH HOH A . 
Z  8 HOH 229 1629 744  HOH HOH A . 
Z  8 HOH 230 1630 680  HOH HOH A . 
Z  8 HOH 231 1631 628  HOH HOH A . 
Z  8 HOH 232 1632 214  HOH HOH A . 
Z  8 HOH 233 1633 1480 HOH HOH A . 
Z  8 HOH 234 1634 721  HOH HOH A . 
Z  8 HOH 235 1635 43   HOH HOH A . 
Z  8 HOH 236 1636 46   HOH HOH A . 
Z  8 HOH 237 1637 277  HOH HOH A . 
Z  8 HOH 238 1638 39   HOH HOH A . 
Z  8 HOH 239 1639 52   HOH HOH A . 
Z  8 HOH 240 1640 51   HOH HOH A . 
Z  8 HOH 241 1641 317  HOH HOH A . 
Z  8 HOH 242 1642 170  HOH HOH A . 
Z  8 HOH 243 1643 260  HOH HOH A . 
Z  8 HOH 244 1644 256  HOH HOH A . 
Z  8 HOH 245 1645 1299 HOH HOH A . 
Z  8 HOH 246 1646 1203 HOH HOH A . 
Z  8 HOH 247 1647 747  HOH HOH A . 
Z  8 HOH 248 1648 814  HOH HOH A . 
Z  8 HOH 249 1649 669  HOH HOH A . 
Z  8 HOH 250 1650 1336 HOH HOH A . 
Z  8 HOH 251 1651 81   HOH HOH A . 
Z  8 HOH 252 1652 350  HOH HOH A . 
Z  8 HOH 253 1653 965  HOH HOH A . 
Z  8 HOH 254 1654 232  HOH HOH A . 
Z  8 HOH 255 1655 40   HOH HOH A . 
Z  8 HOH 256 1656 532  HOH HOH A . 
Z  8 HOH 257 1657 1144 HOH HOH A . 
Z  8 HOH 258 1658 1482 HOH HOH A . 
Z  8 HOH 259 1659 760  HOH HOH A . 
Z  8 HOH 260 1660 371  HOH HOH A . 
Z  8 HOH 261 1661 978  HOH HOH A . 
Z  8 HOH 262 1662 458  HOH HOH A . 
Z  8 HOH 263 1663 85   HOH HOH A . 
Z  8 HOH 264 1664 49   HOH HOH A . 
Z  8 HOH 265 1665 208  HOH HOH A . 
Z  8 HOH 266 1666 412  HOH HOH A . 
Z  8 HOH 267 1667 1557 HOH HOH A . 
Z  8 HOH 268 1668 332  HOH HOH A . 
Z  8 HOH 269 1669 294  HOH HOH A . 
Z  8 HOH 270 1670 852  HOH HOH A . 
Z  8 HOH 271 1671 837  HOH HOH A . 
Z  8 HOH 272 1672 23   HOH HOH A . 
Z  8 HOH 273 1673 16   HOH HOH A . 
Z  8 HOH 274 1674 986  HOH HOH A . 
Z  8 HOH 275 1675 517  HOH HOH A . 
Z  8 HOH 276 1676 847  HOH HOH A . 
Z  8 HOH 277 1677 1379 HOH HOH A . 
Z  8 HOH 278 1678 385  HOH HOH A . 
Z  8 HOH 279 1679 110  HOH HOH A . 
Z  8 HOH 280 1680 1029 HOH HOH A . 
Z  8 HOH 281 1681 674  HOH HOH A . 
Z  8 HOH 282 1682 449  HOH HOH A . 
Z  8 HOH 283 1683 15   HOH HOH A . 
Z  8 HOH 284 1684 106  HOH HOH A . 
Z  8 HOH 285 1685 237  HOH HOH A . 
Z  8 HOH 286 1686 113  HOH HOH A . 
Z  8 HOH 287 1687 612  HOH HOH A . 
Z  8 HOH 288 1688 320  HOH HOH A . 
Z  8 HOH 289 1689 848  HOH HOH A . 
Z  8 HOH 290 1690 650  HOH HOH A . 
Z  8 HOH 291 1691 10   HOH HOH A . 
Z  8 HOH 292 1692 115  HOH HOH A . 
Z  8 HOH 293 1693 900  HOH HOH A . 
Z  8 HOH 294 1694 976  HOH HOH A . 
Z  8 HOH 295 1695 1418 HOH HOH A . 
Z  8 HOH 296 1696 1391 HOH HOH A . 
Z  8 HOH 297 1697 432  HOH HOH A . 
Z  8 HOH 298 1698 647  HOH HOH A . 
Z  8 HOH 299 1699 293  HOH HOH A . 
Z  8 HOH 300 1700 1515 HOH HOH A . 
Z  8 HOH 301 1701 433  HOH HOH A . 
Z  8 HOH 302 1702 239  HOH HOH A . 
Z  8 HOH 303 1703 315  HOH HOH A . 
Z  8 HOH 304 1704 329  HOH HOH A . 
Z  8 HOH 305 1705 327  HOH HOH A . 
Z  8 HOH 306 1706 254  HOH HOH A . 
Z  8 HOH 307 1707 200  HOH HOH A . 
Z  8 HOH 308 1708 1409 HOH HOH A . 
Z  8 HOH 309 1709 159  HOH HOH A . 
Z  8 HOH 310 1710 226  HOH HOH A . 
Z  8 HOH 311 1711 686  HOH HOH A . 
Z  8 HOH 312 1712 1037 HOH HOH A . 
Z  8 HOH 313 1713 494  HOH HOH A . 
Z  8 HOH 314 1714 441  HOH HOH A . 
Z  8 HOH 315 1715 1188 HOH HOH A . 
Z  8 HOH 316 1716 13   HOH HOH A . 
Z  8 HOH 317 1717 111  HOH HOH A . 
Z  8 HOH 318 1718 700  HOH HOH A . 
Z  8 HOH 319 1719 522  HOH HOH A . 
Z  8 HOH 320 1720 205  HOH HOH A . 
Z  8 HOH 321 1721 439  HOH HOH A . 
Z  8 HOH 322 1722 198  HOH HOH A . 
Z  8 HOH 323 1723 478  HOH HOH A . 
Z  8 HOH 324 1724 252  HOH HOH A . 
Z  8 HOH 325 1725 833  HOH HOH A . 
Z  8 HOH 326 1726 667  HOH HOH A . 
Z  8 HOH 327 1727 816  HOH HOH A . 
Z  8 HOH 328 1728 33   HOH HOH A . 
Z  8 HOH 329 1729 1059 HOH HOH A . 
Z  8 HOH 330 1730 448  HOH HOH A . 
Z  8 HOH 331 1731 112  HOH HOH A . 
Z  8 HOH 332 1732 363  HOH HOH A . 
Z  8 HOH 333 1733 834  HOH HOH A . 
Z  8 HOH 334 1734 1366 HOH HOH A . 
Z  8 HOH 335 1735 1175 HOH HOH A . 
Z  8 HOH 336 1736 19   HOH HOH A . 
Z  8 HOH 337 1737 199  HOH HOH A . 
Z  8 HOH 338 1738 527  HOH HOH A . 
Z  8 HOH 339 1739 213  HOH HOH A . 
Z  8 HOH 340 1740 276  HOH HOH A . 
Z  8 HOH 341 1741 25   HOH HOH A . 
Z  8 HOH 342 1742 1152 HOH HOH A . 
Z  8 HOH 343 1743 86   HOH HOH A . 
Z  8 HOH 344 1744 247  HOH HOH A . 
Z  8 HOH 345 1745 913  HOH HOH A . 
Z  8 HOH 346 1746 980  HOH HOH A . 
Z  8 HOH 347 1747 553  HOH HOH A . 
Z  8 HOH 348 1748 137  HOH HOH A . 
Z  8 HOH 349 1749 1488 HOH HOH A . 
Z  8 HOH 350 1750 569  HOH HOH A . 
Z  8 HOH 351 1751 1266 HOH HOH A . 
Z  8 HOH 352 1752 624  HOH HOH A . 
Z  8 HOH 353 1753 182  HOH HOH A . 
Z  8 HOH 354 1754 1451 HOH HOH A . 
Z  8 HOH 355 1755 1545 HOH HOH A . 
Z  8 HOH 356 1756 1546 HOH HOH A . 
Z  8 HOH 357 1757 55   HOH HOH A . 
Z  8 HOH 358 1758 1502 HOH HOH A . 
Z  8 HOH 359 1759 45   HOH HOH A . 
Z  8 HOH 360 1760 874  HOH HOH A . 
Z  8 HOH 361 1761 1121 HOH HOH A . 
Z  8 HOH 362 1762 353  HOH HOH A . 
Z  8 HOH 363 1763 255  HOH HOH A . 
Z  8 HOH 364 1764 311  HOH HOH A . 
Z  8 HOH 365 1765 147  HOH HOH A . 
Z  8 HOH 366 1766 5    HOH HOH A . 
Z  8 HOH 367 1767 776  HOH HOH A . 
Z  8 HOH 368 1768 1378 HOH HOH A . 
Z  8 HOH 369 1769 1225 HOH HOH A . 
Z  8 HOH 370 1770 1513 HOH HOH A . 
Z  8 HOH 371 1771 100  HOH HOH A . 
Z  8 HOH 372 1772 841  HOH HOH A . 
Z  8 HOH 373 1773 934  HOH HOH A . 
Z  8 HOH 374 1774 1026 HOH HOH A . 
Z  8 HOH 375 1775 413  HOH HOH A . 
Z  8 HOH 376 1776 245  HOH HOH A . 
Z  8 HOH 377 1777 98   HOH HOH A . 
Z  8 HOH 378 1778 571  HOH HOH A . 
Z  8 HOH 379 1779 335  HOH HOH A . 
Z  8 HOH 380 1780 918  HOH HOH A . 
Z  8 HOH 381 1781 1397 HOH HOH A . 
Z  8 HOH 382 1782 602  HOH HOH A . 
Z  8 HOH 383 1783 1051 HOH HOH A . 
Z  8 HOH 384 1784 343  HOH HOH A . 
Z  8 HOH 385 1785 896  HOH HOH A . 
Z  8 HOH 386 1786 1444 HOH HOH A . 
Z  8 HOH 387 1787 70   HOH HOH A . 
Z  8 HOH 388 1788 414  HOH HOH A . 
Z  8 HOH 389 1789 1508 HOH HOH A . 
Z  8 HOH 390 1790 292  HOH HOH A . 
Z  8 HOH 391 1791 96   HOH HOH A . 
Z  8 HOH 392 1792 1278 HOH HOH A . 
Z  8 HOH 393 1793 474  HOH HOH A . 
Z  8 HOH 394 1794 926  HOH HOH A . 
Z  8 HOH 395 1795 344  HOH HOH A . 
Z  8 HOH 396 1796 652  HOH HOH A . 
Z  8 HOH 397 1797 513  HOH HOH A . 
Z  8 HOH 398 1798 733  HOH HOH A . 
Z  8 HOH 399 1799 496  HOH HOH A . 
Z  8 HOH 400 1800 780  HOH HOH A . 
Z  8 HOH 401 1801 516  HOH HOH A . 
Z  8 HOH 402 1802 341  HOH HOH A . 
Z  8 HOH 403 1803 859  HOH HOH A . 
Z  8 HOH 404 1804 347  HOH HOH A . 
Z  8 HOH 405 1805 1539 HOH HOH A . 
Z  8 HOH 406 1806 299  HOH HOH A . 
Z  8 HOH 407 1807 626  HOH HOH A . 
Z  8 HOH 408 1808 296  HOH HOH A . 
Z  8 HOH 409 1809 1396 HOH HOH A . 
Z  8 HOH 410 1810 60   HOH HOH A . 
Z  8 HOH 411 1811 771  HOH HOH A . 
Z  8 HOH 412 1812 1164 HOH HOH A . 
Z  8 HOH 413 1813 709  HOH HOH A . 
Z  8 HOH 414 1814 789  HOH HOH A . 
Z  8 HOH 415 1815 877  HOH HOH A . 
Z  8 HOH 416 1816 707  HOH HOH A . 
Z  8 HOH 417 1817 827  HOH HOH A . 
Z  8 HOH 418 1818 318  HOH HOH A . 
Z  8 HOH 419 1819 305  HOH HOH A . 
Z  8 HOH 420 1820 235  HOH HOH A . 
Z  8 HOH 421 1821 1207 HOH HOH A . 
Z  8 HOH 422 1822 1298 HOH HOH A . 
Z  8 HOH 423 1823 486  HOH HOH A . 
Z  8 HOH 424 1824 807  HOH HOH A . 
Z  8 HOH 425 1825 1333 HOH HOH A . 
Z  8 HOH 426 1826 79   HOH HOH A . 
Z  8 HOH 427 1827 397  HOH HOH A . 
Z  8 HOH 428 1828 688  HOH HOH A . 
Z  8 HOH 429 1829 862  HOH HOH A . 
Z  8 HOH 430 1830 73   HOH HOH A . 
Z  8 HOH 431 1831 1452 HOH HOH A . 
Z  8 HOH 432 1832 1127 HOH HOH A . 
Z  8 HOH 433 1833 436  HOH HOH A . 
Z  8 HOH 434 1834 1454 HOH HOH A . 
Z  8 HOH 435 1835 161  HOH HOH A . 
Z  8 HOH 436 1836 87   HOH HOH A . 
Z  8 HOH 437 1837 278  HOH HOH A . 
Z  8 HOH 438 1838 1247 HOH HOH A . 
Z  8 HOH 439 1839 1215 HOH HOH A . 
Z  8 HOH 440 1840 1052 HOH HOH A . 
Z  8 HOH 441 1841 430  HOH HOH A . 
Z  8 HOH 442 1842 411  HOH HOH A . 
Z  8 HOH 443 1843 136  HOH HOH A . 
Z  8 HOH 444 1844 403  HOH HOH A . 
Z  8 HOH 445 1845 1250 HOH HOH A . 
Z  8 HOH 446 1846 1370 HOH HOH A . 
Z  8 HOH 447 1847 1260 HOH HOH A . 
Z  8 HOH 448 1848 739  HOH HOH A . 
Z  8 HOH 449 1849 1003 HOH HOH A . 
Z  8 HOH 450 1850 761  HOH HOH A . 
Z  8 HOH 451 1851 1514 HOH HOH A . 
Z  8 HOH 452 1852 785  HOH HOH A . 
Z  8 HOH 453 1853 333  HOH HOH A . 
Z  8 HOH 454 1854 840  HOH HOH A . 
Z  8 HOH 455 1855 492  HOH HOH A . 
Z  8 HOH 456 1856 748  HOH HOH A . 
Z  8 HOH 457 1857 936  HOH HOH A . 
Z  8 HOH 458 1858 1264 HOH HOH A . 
Z  8 HOH 459 1859 1504 HOH HOH A . 
Z  8 HOH 460 1860 246  HOH HOH A . 
Z  8 HOH 461 1861 142  HOH HOH A . 
Z  8 HOH 462 1862 268  HOH HOH A . 
Z  8 HOH 463 1863 907  HOH HOH A . 
Z  8 HOH 464 1864 945  HOH HOH A . 
Z  8 HOH 465 1865 472  HOH HOH A . 
Z  8 HOH 466 1866 1388 HOH HOH A . 
Z  8 HOH 467 1867 114  HOH HOH A . 
Z  8 HOH 468 1868 542  HOH HOH A . 
Z  8 HOH 469 1869 799  HOH HOH A . 
Z  8 HOH 470 1870 1053 HOH HOH A . 
Z  8 HOH 471 1871 1313 HOH HOH A . 
Z  8 HOH 472 1872 177  HOH HOH A . 
Z  8 HOH 473 1873 1408 HOH HOH A . 
Z  8 HOH 474 1874 773  HOH HOH A . 
Z  8 HOH 475 1875 992  HOH HOH A . 
Z  8 HOH 476 1876 1419 HOH HOH A . 
Z  8 HOH 477 1877 189  HOH HOH A . 
Z  8 HOH 478 1878 426  HOH HOH A . 
Z  8 HOH 479 1879 1405 HOH HOH A . 
Z  8 HOH 480 1880 149  HOH HOH A . 
Z  8 HOH 481 1881 220  HOH HOH A . 
Z  8 HOH 482 1882 774  HOH HOH A . 
Z  8 HOH 483 1883 681  HOH HOH A . 
Z  8 HOH 484 1884 609  HOH HOH A . 
Z  8 HOH 485 1885 1007 HOH HOH A . 
Z  8 HOH 486 1886 765  HOH HOH A . 
Z  8 HOH 487 1887 1328 HOH HOH A . 
Z  8 HOH 488 1888 1045 HOH HOH A . 
Z  8 HOH 489 1889 446  HOH HOH A . 
Z  8 HOH 490 1890 870  HOH HOH A . 
Z  8 HOH 491 1891 450  HOH HOH A . 
Z  8 HOH 492 1892 923  HOH HOH A . 
Z  8 HOH 493 1893 1383 HOH HOH A . 
Z  8 HOH 494 1894 88   HOH HOH A . 
Z  8 HOH 495 1895 825  HOH HOH A . 
Z  8 HOH 496 1896 175  HOH HOH A . 
Z  8 HOH 497 1897 1001 HOH HOH A . 
Z  8 HOH 498 1898 1076 HOH HOH A . 
Z  8 HOH 499 1899 480  HOH HOH A . 
Z  8 HOH 500 1900 1058 HOH HOH A . 
Z  8 HOH 501 1901 484  HOH HOH A . 
Z  8 HOH 502 1902 706  HOH HOH A . 
Z  8 HOH 503 1903 756  HOH HOH A . 
Z  8 HOH 504 1904 336  HOH HOH A . 
Z  8 HOH 505 1905 469  HOH HOH A . 
Z  8 HOH 506 1906 428  HOH HOH A . 
Z  8 HOH 507 1907 1140 HOH HOH A . 
Z  8 HOH 508 1908 1025 HOH HOH A . 
Z  8 HOH 509 1909 471  HOH HOH A . 
Z  8 HOH 510 1910 1562 HOH HOH A . 
Z  8 HOH 511 1911 1062 HOH HOH A . 
Z  8 HOH 512 1912 241  HOH HOH A . 
Z  8 HOH 513 1913 308  HOH HOH A . 
Z  8 HOH 514 1914 150  HOH HOH A . 
Z  8 HOH 515 1915 891  HOH HOH A . 
Z  8 HOH 516 1916 1341 HOH HOH A . 
Z  8 HOH 517 1917 357  HOH HOH A . 
Z  8 HOH 518 1918 530  HOH HOH A . 
Z  8 HOH 519 1919 908  HOH HOH A . 
Z  8 HOH 520 1920 253  HOH HOH A . 
Z  8 HOH 521 1921 304  HOH HOH A . 
Z  8 HOH 522 1922 1104 HOH HOH A . 
Z  8 HOH 523 1923 622  HOH HOH A . 
Z  8 HOH 524 1924 218  HOH HOH A . 
Z  8 HOH 525 1925 1340 HOH HOH A . 
Z  8 HOH 526 1926 839  HOH HOH A . 
Z  8 HOH 527 1927 924  HOH HOH A . 
Z  8 HOH 528 1928 565  HOH HOH A . 
Z  8 HOH 529 1929 1174 HOH HOH A . 
Z  8 HOH 530 1930 1176 HOH HOH A . 
Z  8 HOH 531 1931 1008 HOH HOH A . 
Z  8 HOH 532 1932 1476 HOH HOH A . 
Z  8 HOH 533 1933 1344 HOH HOH A . 
Z  8 HOH 534 1934 1506 HOH HOH A . 
Z  8 HOH 535 1935 712  HOH HOH A . 
Z  8 HOH 536 1936 1161 HOH HOH A . 
Z  8 HOH 537 1937 589  HOH HOH A . 
Z  8 HOH 538 1938 1420 HOH HOH A . 
Z  8 HOH 539 1939 1048 HOH HOH A . 
Z  8 HOH 540 1940 601  HOH HOH A . 
Z  8 HOH 541 1941 754  HOH HOH A . 
Z  8 HOH 542 1942 846  HOH HOH A . 
Z  8 HOH 543 1943 1168 HOH HOH A . 
Z  8 HOH 544 1944 1407 HOH HOH A . 
Z  8 HOH 545 1945 453  HOH HOH A . 
Z  8 HOH 546 1946 1458 HOH HOH A . 
Z  8 HOH 547 1947 1041 HOH HOH A . 
Z  8 HOH 548 1948 1523 HOH HOH A . 
Z  8 HOH 549 1949 996  HOH HOH A . 
Z  8 HOH 550 1950 914  HOH HOH A . 
Z  8 HOH 551 1951 1511 HOH HOH A . 
Z  8 HOH 552 1952 1453 HOH HOH A . 
Z  8 HOH 553 1953 383  HOH HOH A . 
Z  8 HOH 554 1954 21   HOH HOH A . 
Z  8 HOH 555 1955 1038 HOH HOH A . 
Z  8 HOH 556 1956 810  HOH HOH A . 
Z  8 HOH 557 1957 291  HOH HOH A . 
Z  8 HOH 558 1958 445  HOH HOH A . 
Z  8 HOH 559 1959 104  HOH HOH A . 
Z  8 HOH 560 1960 324  HOH HOH A . 
Z  8 HOH 561 1961 117  HOH HOH A . 
Z  8 HOH 562 1962 1141 HOH HOH A . 
Z  8 HOH 563 1963 538  HOH HOH A . 
Z  8 HOH 564 1964 1384 HOH HOH A . 
Z  8 HOH 565 1965 212  HOH HOH A . 
Z  8 HOH 566 1966 1012 HOH HOH A . 
Z  8 HOH 567 1967 690  HOH HOH A . 
Z  8 HOH 568 1968 672  HOH HOH A . 
Z  8 HOH 569 1969 860  HOH HOH A . 
Z  8 HOH 570 1970 1426 HOH HOH A . 
Z  8 HOH 571 1971 1145 HOH HOH A . 
Z  8 HOH 572 1972 640  HOH HOH A . 
Z  8 HOH 573 1973 1097 HOH HOH A . 
Z  8 HOH 574 1974 1066 HOH HOH A . 
Z  8 HOH 575 1975 374  HOH HOH A . 
Z  8 HOH 576 1976 1510 HOH HOH A . 
Z  8 HOH 577 1977 539  HOH HOH A . 
Z  8 HOH 578 1978 627  HOH HOH A . 
Z  8 HOH 579 1979 798  HOH HOH A . 
Z  8 HOH 580 1980 584  HOH HOH A . 
Z  8 HOH 581 1981 1414 HOH HOH A . 
Z  8 HOH 582 1982 1185 HOH HOH A . 
Z  8 HOH 583 1983 1548 HOH HOH A . 
Z  8 HOH 584 1984 483  HOH HOH A . 
Z  8 HOH 585 1985 578  HOH HOH A . 
Z  8 HOH 586 1986 395  HOH HOH A . 
Z  8 HOH 587 1987 963  HOH HOH A . 
Z  8 HOH 588 1988 772  HOH HOH A . 
Z  8 HOH 589 1989 745  HOH HOH A . 
Z  8 HOH 590 1990 1469 HOH HOH A . 
Z  8 HOH 591 1991 1567 HOH HOH A . 
Z  8 HOH 592 1992 1441 HOH HOH A . 
Z  8 HOH 593 1993 498  HOH HOH A . 
Z  8 HOH 594 1994 322  HOH HOH A . 
Z  8 HOH 595 1995 512  HOH HOH A . 
Z  8 HOH 596 1996 225  HOH HOH A . 
Z  8 HOH 597 1997 1320 HOH HOH A . 
Z  8 HOH 598 1998 1020 HOH HOH A . 
Z  8 HOH 599 1999 607  HOH HOH A . 
Z  8 HOH 600 2000 1159 HOH HOH A . 
Z  8 HOH 601 2001 718  HOH HOH A . 
Z  8 HOH 602 2002 1415 HOH HOH A . 
Z  8 HOH 603 2003 1347 HOH HOH A . 
Z  8 HOH 604 2004 1285 HOH HOH A . 
Z  8 HOH 605 2005 1146 HOH HOH A . 
Z  8 HOH 606 2006 1272 HOH HOH A . 
Z  8 HOH 607 2007 1259 HOH HOH A . 
Z  8 HOH 608 2008 1436 HOH HOH A . 
Z  8 HOH 609 2009 1170 HOH HOH A . 
Z  8 HOH 610 2010 1447 HOH HOH A . 
Z  8 HOH 611 2011 1411 HOH HOH A . 
Z  8 HOH 612 2012 714  HOH HOH A . 
Z  8 HOH 613 2013 1534 HOH HOH A . 
Z  8 HOH 614 2014 491  HOH HOH A . 
Z  8 HOH 615 2015 701  HOH HOH A . 
Z  8 HOH 616 2016 1429 HOH HOH A . 
Z  8 HOH 617 2017 372  HOH HOH A . 
Z  8 HOH 618 2018 993  HOH HOH A . 
Z  8 HOH 619 2019 1206 HOH HOH A . 
Z  8 HOH 620 2020 895  HOH HOH A . 
Z  8 HOH 621 2021 655  HOH HOH A . 
Z  8 HOH 622 2022 1559 HOH HOH A . 
Z  8 HOH 623 2023 384  HOH HOH A . 
Z  8 HOH 624 2024 1162 HOH HOH A . 
Z  8 HOH 625 2025 1323 HOH HOH A . 
Z  8 HOH 626 2026 668  HOH HOH A . 
Z  8 HOH 627 2027 1394 HOH HOH A . 
Z  8 HOH 628 2028 1521 HOH HOH A . 
Z  8 HOH 629 2029 1213 HOH HOH A . 
Z  8 HOH 630 2030 1390 HOH HOH A . 
Z  8 HOH 631 2031 1367 HOH HOH A . 
Z  8 HOH 632 2032 1315 HOH HOH A . 
Z  8 HOH 633 2033 1440 HOH HOH A . 
Z  8 HOH 634 2034 1349 HOH HOH A . 
Z  8 HOH 635 2035 981  HOH HOH A . 
Z  8 HOH 636 2036 1377 HOH HOH A . 
Z  8 HOH 637 2037 1214 HOH HOH A . 
Z  8 HOH 638 2038 1139 HOH HOH A . 
Z  8 HOH 639 2039 1565 HOH HOH A . 
Z  8 HOH 640 2040 1274 HOH HOH A . 
Z  8 HOH 641 2041 1530 HOH HOH A . 
Z  8 HOH 642 2042 1519 HOH HOH A . 
Z  8 HOH 643 2043 1543 HOH HOH A . 
Z  8 HOH 644 2044 1293 HOH HOH A . 
Z  8 HOH 645 2045 1270 HOH HOH A . 
Z  8 HOH 646 2046 1169 HOH HOH A . 
Z  8 HOH 647 2047 1210 HOH HOH A . 
Z  8 HOH 648 2048 1540 HOH HOH A . 
Z  8 HOH 649 2049 1360 HOH HOH A . 
Z  8 HOH 650 2050 946  HOH HOH A . 
Z  8 HOH 651 2051 1466 HOH HOH A . 
Z  8 HOH 652 2052 1220 HOH HOH A . 
Z  8 HOH 653 2053 915  HOH HOH A . 
Z  8 HOH 654 2054 905  HOH HOH A . 
Z  8 HOH 655 2055 1437 HOH HOH A . 
Z  8 HOH 656 2056 1492 HOH HOH A . 
Z  8 HOH 657 2057 1286 HOH HOH A . 
Z  8 HOH 658 2058 795  HOH HOH A . 
Z  8 HOH 659 2059 1395 HOH HOH A . 
Z  8 HOH 660 2060 1335 HOH HOH A . 
Z  8 HOH 661 2061 1455 HOH HOH A . 
Z  8 HOH 662 2062 352  HOH HOH A . 
Z  8 HOH 663 2063 282  HOH HOH A . 
Z  8 HOH 664 2064 1498 HOH HOH A . 
Z  8 HOH 665 2065 1120 HOH HOH A . 
Z  8 HOH 666 2066 911  HOH HOH A . 
Z  8 HOH 667 2067 1324 HOH HOH A . 
Z  8 HOH 668 2068 990  HOH HOH A . 
Z  8 HOH 669 2069 1460 HOH HOH A . 
Z  8 HOH 670 2070 676  HOH HOH A . 
Z  8 HOH 671 2071 1465 HOH HOH A . 
Z  8 HOH 672 2072 1467 HOH HOH A . 
Z  8 HOH 673 2073 1122 HOH HOH A . 
Z  8 HOH 674 2074 1496 HOH HOH A . 
Z  8 HOH 675 2075 818  HOH HOH A . 
Z  8 HOH 676 2076 1361 HOH HOH A . 
Z  8 HOH 677 2077 1295 HOH HOH A . 
Z  8 HOH 678 2078 563  HOH HOH A . 
Z  8 HOH 679 2079 1507 HOH HOH A . 
Z  8 HOH 680 2080 725  HOH HOH A . 
Z  8 HOH 681 2081 1520 HOH HOH A . 
Z  8 HOH 682 2082 1258 HOH HOH A . 
Z  8 HOH 683 2083 881  HOH HOH A . 
Z  8 HOH 684 2084 1009 HOH HOH A . 
Z  8 HOH 685 2085 1368 HOH HOH A . 
Z  8 HOH 686 2086 1371 HOH HOH A . 
Z  8 HOH 687 2087 1143 HOH HOH A . 
Z  8 HOH 688 2088 1497 HOH HOH A . 
Z  8 HOH 689 2089 1495 HOH HOH A . 
Z  8 HOH 690 2090 1438 HOH HOH A . 
Z  8 HOH 691 2091 1292 HOH HOH A . 
Z  8 HOH 692 2092 851  HOH HOH A . 
Z  8 HOH 693 2093 1204 HOH HOH A . 
Z  8 HOH 694 2094 1294 HOH HOH A . 
Z  8 HOH 695 2095 882  HOH HOH A . 
Z  8 HOH 696 2096 1560 HOH HOH A . 
Z  8 HOH 697 2097 1499 HOH HOH A . 
Z  8 HOH 698 2098 1069 HOH HOH A . 
Z  8 HOH 699 2099 1555 HOH HOH A . 
Z  8 HOH 700 2100 586  HOH HOH A . 
Z  8 HOH 701 2101 420  HOH HOH A . 
Z  8 HOH 702 2102 919  HOH HOH A . 
Z  8 HOH 703 2103 910  HOH HOH A . 
Z  8 HOH 704 2104 1317 HOH HOH A . 
Z  8 HOH 705 2105 704  HOH HOH A . 
Z  8 HOH 706 2106 1463 HOH HOH A . 
Z  8 HOH 707 2107 454  HOH HOH A . 
Z  8 HOH 708 2108 661  HOH HOH A . 
Z  8 HOH 709 2109 782  HOH HOH A . 
Z  8 HOH 710 2110 1244 HOH HOH A . 
Z  8 HOH 711 2111 588  HOH HOH A . 
Z  8 HOH 712 2112 1208 HOH HOH A . 
Z  8 HOH 713 2113 1180 HOH HOH A . 
Z  8 HOH 714 2114 1322 HOH HOH A . 
Z  8 HOH 715 2115 1556 HOH HOH A . 
Z  8 HOH 716 2116 367  HOH HOH A . 
Z  8 HOH 717 2117 1398 HOH HOH A . 
Z  8 HOH 718 2118 1276 HOH HOH A . 
Z  8 HOH 719 2119 1296 HOH HOH A . 
Z  8 HOH 720 2120 975  HOH HOH A . 
Z  8 HOH 721 2121 393  HOH HOH A . 
Z  8 HOH 722 2122 979  HOH HOH A . 
Z  8 HOH 723 2123 1063 HOH HOH A . 
Z  8 HOH 724 2124 415  HOH HOH A . 
Z  8 HOH 725 2125 443  HOH HOH A . 
Z  8 HOH 726 2126 724  HOH HOH A . 
Z  8 HOH 727 2127 802  HOH HOH A . 
Z  8 HOH 728 2128 457  HOH HOH A . 
Z  8 HOH 729 2129 973  HOH HOH A . 
Z  8 HOH 730 2130 800  HOH HOH A . 
Z  8 HOH 731 2131 665  HOH HOH A . 
Z  8 HOH 732 2132 634  HOH HOH A . 
Z  8 HOH 733 2133 1427 HOH HOH A . 
Z  8 HOH 734 2134 1375 HOH HOH A . 
Z  8 HOH 735 2135 621  HOH HOH A . 
Z  8 HOH 736 2136 987  HOH HOH A . 
Z  8 HOH 737 2137 1068 HOH HOH A . 
Z  8 HOH 738 2138 1524 HOH HOH A . 
Z  8 HOH 739 2139 1538 HOH HOH A . 
Z  8 HOH 740 2140 1551 HOH HOH A . 
Z  8 HOH 741 2141 1343 HOH HOH A . 
Z  8 HOH 742 2142 985  HOH HOH A . 
Z  8 HOH 743 2143 1318 HOH HOH A . 
Z  8 HOH 744 2144 1531 HOH HOH A . 
Z  8 HOH 745 2145 514  HOH HOH A . 
Z  8 HOH 746 2146 1352 HOH HOH A . 
Z  8 HOH 747 2147 1448 HOH HOH A . 
Z  8 HOH 748 2148 763  HOH HOH A . 
AA 8 HOH 1   1401 379  HOH HOH B . 
AA 8 HOH 2   1402 1306 HOH HOH B . 
AA 8 HOH 3   1403 925  HOH HOH B . 
AA 8 HOH 4   1404 1526 HOH HOH B . 
AA 8 HOH 5   1405 556  HOH HOH B . 
AA 8 HOH 6   1406 36   HOH HOH B . 
AA 8 HOH 7   1407 295  HOH HOH B . 
AA 8 HOH 8   1408 711  HOH HOH B . 
AA 8 HOH 9   1409 1046 HOH HOH B . 
AA 8 HOH 10  1410 781  HOH HOH B . 
AA 8 HOH 11  1411 319  HOH HOH B . 
AA 8 HOH 12  1412 703  HOH HOH B . 
AA 8 HOH 13  1413 146  HOH HOH B . 
AA 8 HOH 14  1414 176  HOH HOH B . 
AA 8 HOH 15  1415 438  HOH HOH B . 
AA 8 HOH 16  1416 401  HOH HOH B . 
AA 8 HOH 17  1417 1301 HOH HOH B . 
AA 8 HOH 18  1418 275  HOH HOH B . 
AA 8 HOH 19  1419 930  HOH HOH B . 
AA 8 HOH 20  1420 248  HOH HOH B . 
AA 8 HOH 21  1421 506  HOH HOH B . 
AA 8 HOH 22  1422 889  HOH HOH B . 
AA 8 HOH 23  1423 93   HOH HOH B . 
AA 8 HOH 24  1424 392  HOH HOH B . 
AA 8 HOH 25  1425 670  HOH HOH B . 
AA 8 HOH 26  1426 1085 HOH HOH B . 
AA 8 HOH 27  1427 223  HOH HOH B . 
AA 8 HOH 28  1428 1036 HOH HOH B . 
AA 8 HOH 29  1429 932  HOH HOH B . 
AA 8 HOH 30  1430 338  HOH HOH B . 
AA 8 HOH 31  1431 1430 HOH HOH B . 
AA 8 HOH 32  1432 435  HOH HOH B . 
AA 8 HOH 33  1433 552  HOH HOH B . 
AA 8 HOH 34  1434 1564 HOH HOH B . 
AA 8 HOH 35  1435 912  HOH HOH B . 
AA 8 HOH 36  1436 579  HOH HOH B . 
AA 8 HOH 37  1437 523  HOH HOH B . 
AA 8 HOH 38  1438 94   HOH HOH B . 
AA 8 HOH 39  1439 878  HOH HOH B . 
AA 8 HOH 40  1440 728  HOH HOH B . 
AA 8 HOH 41  1441 390  HOH HOH B . 
AA 8 HOH 42  1442 1154 HOH HOH B . 
AA 8 HOH 43  1443 727  HOH HOH B . 
AA 8 HOH 44  1444 620  HOH HOH B . 
AA 8 HOH 45  1445 967  HOH HOH B . 
AA 8 HOH 46  1446 340  HOH HOH B . 
AA 8 HOH 47  1447 328  HOH HOH B . 
AA 8 HOH 48  1448 1484 HOH HOH B . 
AA 8 HOH 49  1449 829  HOH HOH B . 
AA 8 HOH 50  1450 1373 HOH HOH B . 
AA 8 HOH 51  1451 566  HOH HOH B . 
AA 8 HOH 52  1452 1339 HOH HOH B . 
AA 8 HOH 53  1453 442  HOH HOH B . 
AA 8 HOH 54  1454 1056 HOH HOH B . 
AA 8 HOH 55  1455 755  HOH HOH B . 
AA 8 HOH 56  1456 535  HOH HOH B . 
AA 8 HOH 57  1457 1167 HOH HOH B . 
AA 8 HOH 58  1458 1071 HOH HOH B . 
AA 8 HOH 59  1459 2    HOH HOH B . 
AA 8 HOH 60  1460 103  HOH HOH B . 
AA 8 HOH 61  1461 391  HOH HOH B . 
AA 8 HOH 62  1462 77   HOH HOH B . 
AA 8 HOH 63  1463 314  HOH HOH B . 
AA 8 HOH 64  1464 581  HOH HOH B . 
AA 8 HOH 65  1465 783  HOH HOH B . 
AA 8 HOH 66  1466 312  HOH HOH B . 
AA 8 HOH 67  1467 1273 HOH HOH B . 
AA 8 HOH 68  1468 209  HOH HOH B . 
AA 8 HOH 69  1469 381  HOH HOH B . 
AA 8 HOH 70  1470 630  HOH HOH B . 
AA 8 HOH 71  1471 678  HOH HOH B . 
AA 8 HOH 72  1472 1417 HOH HOH B . 
AA 8 HOH 73  1473 1364 HOH HOH B . 
AA 8 HOH 74  1474 696  HOH HOH B . 
AA 8 HOH 75  1475 526  HOH HOH B . 
AA 8 HOH 76  1476 139  HOH HOH B . 
AA 8 HOH 77  1477 663  HOH HOH B . 
AA 8 HOH 78  1478 59   HOH HOH B . 
AA 8 HOH 79  1479 1392 HOH HOH B . 
AA 8 HOH 80  1480 642  HOH HOH B . 
AA 8 HOH 81  1481 1042 HOH HOH B . 
AA 8 HOH 82  1482 823  HOH HOH B . 
AA 8 HOH 83  1483 62   HOH HOH B . 
AA 8 HOH 84  1484 1191 HOH HOH B . 
AA 8 HOH 85  1485 1099 HOH HOH B . 
AA 8 HOH 86  1486 1478 HOH HOH B . 
AA 8 HOH 87  1487 47   HOH HOH B . 
AA 8 HOH 88  1488 31   HOH HOH B . 
AA 8 HOH 89  1489 105  HOH HOH B . 
AA 8 HOH 90  1490 654  HOH HOH B . 
AA 8 HOH 91  1491 280  HOH HOH B . 
AA 8 HOH 92  1492 227  HOH HOH B . 
AA 8 HOH 93  1493 6    HOH HOH B . 
AA 8 HOH 94  1494 473  HOH HOH B . 
AA 8 HOH 95  1495 564  HOH HOH B . 
AA 8 HOH 96  1496 1281 HOH HOH B . 
AA 8 HOH 97  1497 1363 HOH HOH B . 
AA 8 HOH 98  1498 56   HOH HOH B . 
AA 8 HOH 99  1499 386  HOH HOH B . 
AA 8 HOH 100 1500 958  HOH HOH B . 
AA 8 HOH 101 1501 164  HOH HOH B . 
AA 8 HOH 102 1502 906  HOH HOH B . 
AA 8 HOH 103 1503 931  HOH HOH B . 
AA 8 HOH 104 1504 124  HOH HOH B . 
AA 8 HOH 105 1505 66   HOH HOH B . 
AA 8 HOH 106 1506 121  HOH HOH B . 
AA 8 HOH 107 1507 476  HOH HOH B . 
AA 8 HOH 108 1508 326  HOH HOH B . 
AA 8 HOH 109 1509 53   HOH HOH B . 
AA 8 HOH 110 1510 451  HOH HOH B . 
AA 8 HOH 111 1511 64   HOH HOH B . 
AA 8 HOH 112 1512 618  HOH HOH B . 
AA 8 HOH 113 1513 361  HOH HOH B . 
AA 8 HOH 114 1514 1112 HOH HOH B . 
AA 8 HOH 115 1515 1291 HOH HOH B . 
AA 8 HOH 116 1516 313  HOH HOH B . 
AA 8 HOH 117 1517 119  HOH HOH B . 
AA 8 HOH 118 1518 1297 HOH HOH B . 
AA 8 HOH 119 1519 461  HOH HOH B . 
AA 8 HOH 120 1520 501  HOH HOH B . 
AA 8 HOH 121 1521 419  HOH HOH B . 
AA 8 HOH 122 1522 416  HOH HOH B . 
AA 8 HOH 123 1523 160  HOH HOH B . 
AA 8 HOH 124 1524 695  HOH HOH B . 
AA 8 HOH 125 1525 83   HOH HOH B . 
AA 8 HOH 126 1526 14   HOH HOH B . 
AA 8 HOH 127 1527 942  HOH HOH B . 
AA 8 HOH 128 1528 631  HOH HOH B . 
AA 8 HOH 129 1529 154  HOH HOH B . 
AA 8 HOH 130 1530 1005 HOH HOH B . 
AA 8 HOH 131 1531 20   HOH HOH B . 
AA 8 HOH 132 1532 37   HOH HOH B . 
AA 8 HOH 133 1533 1105 HOH HOH B . 
AA 8 HOH 134 1534 242  HOH HOH B . 
AA 8 HOH 135 1535 169  HOH HOH B . 
AA 8 HOH 136 1536 236  HOH HOH B . 
AA 8 HOH 137 1537 603  HOH HOH B . 
AA 8 HOH 138 1538 156  HOH HOH B . 
AA 8 HOH 139 1539 1432 HOH HOH B . 
AA 8 HOH 140 1540 109  HOH HOH B . 
AA 8 HOH 141 1541 434  HOH HOH B . 
AA 8 HOH 142 1542 598  HOH HOH B . 
AA 8 HOH 143 1543 339  HOH HOH B . 
AA 8 HOH 144 1544 1271 HOH HOH B . 
AA 8 HOH 145 1545 12   HOH HOH B . 
AA 8 HOH 146 1546 185  HOH HOH B . 
AA 8 HOH 147 1547 301  HOH HOH B . 
AA 8 HOH 148 1548 871  HOH HOH B . 
AA 8 HOH 149 1549 152  HOH HOH B . 
AA 8 HOH 150 1550 741  HOH HOH B . 
AA 8 HOH 151 1551 503  HOH HOH B . 
AA 8 HOH 152 1552 715  HOH HOH B . 
AA 8 HOH 153 1553 1103 HOH HOH B . 
AA 8 HOH 154 1554 76   HOH HOH B . 
AA 8 HOH 155 1555 927  HOH HOH B . 
AA 8 HOH 156 1556 540  HOH HOH B . 
AA 8 HOH 157 1557 258  HOH HOH B . 
AA 8 HOH 158 1558 468  HOH HOH B . 
AA 8 HOH 159 1559 966  HOH HOH B . 
AA 8 HOH 160 1560 838  HOH HOH B . 
AA 8 HOH 161 1561 820  HOH HOH B . 
AA 8 HOH 162 1562 1242 HOH HOH B . 
AA 8 HOH 163 1563 917  HOH HOH B . 
AA 8 HOH 164 1564 1304 HOH HOH B . 
AA 8 HOH 165 1565 382  HOH HOH B . 
AA 8 HOH 166 1566 1372 HOH HOH B . 
AA 8 HOH 167 1567 699  HOH HOH B . 
AA 8 HOH 168 1568 948  HOH HOH B . 
AA 8 HOH 169 1569 1089 HOH HOH B . 
AA 8 HOH 170 1570 1365 HOH HOH B . 
AA 8 HOH 171 1571 188  HOH HOH B . 
AA 8 HOH 172 1572 174  HOH HOH B . 
AA 8 HOH 173 1573 597  HOH HOH B . 
AA 8 HOH 174 1574 824  HOH HOH B . 
AA 8 HOH 175 1575 366  HOH HOH B . 
AA 8 HOH 176 1576 1277 HOH HOH B . 
AA 8 HOH 177 1577 61   HOH HOH B . 
AA 8 HOH 178 1578 576  HOH HOH B . 
AA 8 HOH 179 1579 365  HOH HOH B . 
AA 8 HOH 180 1580 587  HOH HOH B . 
AA 8 HOH 181 1581 302  HOH HOH B . 
AA 8 HOH 182 1582 18   HOH HOH B . 
AA 8 HOH 183 1583 54   HOH HOH B . 
AA 8 HOH 184 1584 1098 HOH HOH B . 
AA 8 HOH 185 1585 819  HOH HOH B . 
AA 8 HOH 186 1586 1217 HOH HOH B . 
AA 8 HOH 187 1587 1303 HOH HOH B . 
AA 8 HOH 188 1588 732  HOH HOH B . 
AA 8 HOH 189 1589 554  HOH HOH B . 
AA 8 HOH 190 1590 120  HOH HOH B . 
AA 8 HOH 191 1591 505  HOH HOH B . 
AA 8 HOH 192 1592 431  HOH HOH B . 
AA 8 HOH 193 1593 1445 HOH HOH B . 
AA 8 HOH 194 1594 1034 HOH HOH B . 
AA 8 HOH 195 1595 80   HOH HOH B . 
AA 8 HOH 196 1596 306  HOH HOH B . 
AA 8 HOH 197 1597 1    HOH HOH B . 
AA 8 HOH 198 1598 1039 HOH HOH B . 
AA 8 HOH 199 1599 126  HOH HOH B . 
AA 8 HOH 200 1600 869  HOH HOH B . 
AA 8 HOH 201 1601 863  HOH HOH B . 
AA 8 HOH 202 1602 48   HOH HOH B . 
AA 8 HOH 203 1603 286  HOH HOH B . 
AA 8 HOH 204 1604 1330 HOH HOH B . 
AA 8 HOH 205 1605 166  HOH HOH B . 
AA 8 HOH 206 1606 794  HOH HOH B . 
AA 8 HOH 207 1607 1381 HOH HOH B . 
AA 8 HOH 208 1608 99   HOH HOH B . 
AA 8 HOH 209 1609 78   HOH HOH B . 
AA 8 HOH 210 1610 850  HOH HOH B . 
AA 8 HOH 211 1611 742  HOH HOH B . 
AA 8 HOH 212 1612 116  HOH HOH B . 
AA 8 HOH 213 1613 822  HOH HOH B . 
AA 8 HOH 214 1614 887  HOH HOH B . 
AA 8 HOH 215 1615 902  HOH HOH B . 
AA 8 HOH 216 1616 489  HOH HOH B . 
AA 8 HOH 217 1617 107  HOH HOH B . 
AA 8 HOH 218 1618 11   HOH HOH B . 
AA 8 HOH 219 1619 698  HOH HOH B . 
AA 8 HOH 220 1620 777  HOH HOH B . 
AA 8 HOH 221 1621 646  HOH HOH B . 
AA 8 HOH 222 1622 97   HOH HOH B . 
AA 8 HOH 223 1623 167  HOH HOH B . 
AA 8 HOH 224 1624 684  HOH HOH B . 
AA 8 HOH 225 1625 145  HOH HOH B . 
AA 8 HOH 226 1626 1083 HOH HOH B . 
AA 8 HOH 227 1627 600  HOH HOH B . 
AA 8 HOH 228 1628 359  HOH HOH B . 
AA 8 HOH 229 1629 1369 HOH HOH B . 
AA 8 HOH 230 1630 950  HOH HOH B . 
AA 8 HOH 231 1631 648  HOH HOH B . 
AA 8 HOH 232 1632 638  HOH HOH B . 
AA 8 HOH 233 1633 892  HOH HOH B . 
AA 8 HOH 234 1634 1410 HOH HOH B . 
AA 8 HOH 235 1635 50   HOH HOH B . 
AA 8 HOH 236 1636 616  HOH HOH B . 
AA 8 HOH 237 1637 380  HOH HOH B . 
AA 8 HOH 238 1638 349  HOH HOH B . 
AA 8 HOH 239 1639 67   HOH HOH B . 
AA 8 HOH 240 1640 404  HOH HOH B . 
AA 8 HOH 241 1641 1023 HOH HOH B . 
AA 8 HOH 242 1642 1074 HOH HOH B . 
AA 8 HOH 243 1643 345  HOH HOH B . 
AA 8 HOH 244 1644 358  HOH HOH B . 
AA 8 HOH 245 1645 853  HOH HOH B . 
AA 8 HOH 246 1646 768  HOH HOH B . 
AA 8 HOH 247 1647 1022 HOH HOH B . 
AA 8 HOH 248 1648 1351 HOH HOH B . 
AA 8 HOH 249 1649 228  HOH HOH B . 
AA 8 HOH 250 1650 519  HOH HOH B . 
AA 8 HOH 251 1651 1541 HOH HOH B . 
AA 8 HOH 252 1652 269  HOH HOH B . 
AA 8 HOH 253 1653 520  HOH HOH B . 
AA 8 HOH 254 1654 659  HOH HOH B . 
AA 8 HOH 255 1655 377  HOH HOH B . 
AA 8 HOH 256 1656 534  HOH HOH B . 
AA 8 HOH 257 1657 1425 HOH HOH B . 
AA 8 HOH 258 1658 265  HOH HOH B . 
AA 8 HOH 259 1659 437  HOH HOH B . 
AA 8 HOH 260 1660 1477 HOH HOH B . 
AA 8 HOH 261 1661 828  HOH HOH B . 
AA 8 HOH 262 1662 1302 HOH HOH B . 
AA 8 HOH 263 1663 285  HOH HOH B . 
AA 8 HOH 264 1664 1300 HOH HOH B . 
AA 8 HOH 265 1665 128  HOH HOH B . 
AA 8 HOH 266 1666 17   HOH HOH B . 
AA 8 HOH 267 1667 1493 HOH HOH B . 
AA 8 HOH 268 1668 155  HOH HOH B . 
AA 8 HOH 269 1669 1311 HOH HOH B . 
AA 8 HOH 270 1670 1413 HOH HOH B . 
AA 8 HOH 271 1671 872  HOH HOH B . 
AA 8 HOH 272 1672 165  HOH HOH B . 
AA 8 HOH 273 1673 1400 HOH HOH B . 
AA 8 HOH 274 1674 947  HOH HOH B . 
AA 8 HOH 275 1675 1424 HOH HOH B . 
AA 8 HOH 276 1676 466  HOH HOH B . 
AA 8 HOH 277 1677 394  HOH HOH B . 
AA 8 HOH 278 1678 173  HOH HOH B . 
AA 8 HOH 279 1679 63   HOH HOH B . 
AA 8 HOH 280 1680 885  HOH HOH B . 
AA 8 HOH 281 1681 909  HOH HOH B . 
AA 8 HOH 282 1682 186  HOH HOH B . 
AA 8 HOH 283 1683 4    HOH HOH B . 
AA 8 HOH 284 1684 69   HOH HOH B . 
AA 8 HOH 285 1685 1552 HOH HOH B . 
AA 8 HOH 286 1686 710  HOH HOH B . 
AA 8 HOH 287 1687 577  HOH HOH B . 
AA 8 HOH 288 1688 735  HOH HOH B . 
AA 8 HOH 289 1689 1359 HOH HOH B . 
AA 8 HOH 290 1690 1399 HOH HOH B . 
AA 8 HOH 291 1691 373  HOH HOH B . 
AA 8 HOH 292 1692 583  HOH HOH B . 
AA 8 HOH 293 1693 72   HOH HOH B . 
AA 8 HOH 294 1694 1470 HOH HOH B . 
AA 8 HOH 295 1695 32   HOH HOH B . 
AA 8 HOH 296 1696 370  HOH HOH B . 
AA 8 HOH 297 1697 689  HOH HOH B . 
AA 8 HOH 298 1698 470  HOH HOH B . 
AA 8 HOH 299 1699 297  HOH HOH B . 
AA 8 HOH 300 1700 74   HOH HOH B . 
AA 8 HOH 301 1701 44   HOH HOH B . 
AA 8 HOH 302 1702 1527 HOH HOH B . 
AA 8 HOH 303 1703 1269 HOH HOH B . 
AA 8 HOH 304 1704 605  HOH HOH B . 
AA 8 HOH 305 1705 574  HOH HOH B . 
AA 8 HOH 306 1706 1312 HOH HOH B . 
AA 8 HOH 307 1707 1353 HOH HOH B . 
AA 8 HOH 308 1708 1462 HOH HOH B . 
AA 8 HOH 309 1709 623  HOH HOH B . 
AA 8 HOH 310 1710 593  HOH HOH B . 
AA 8 HOH 311 1711 791  HOH HOH B . 
AA 8 HOH 312 1712 844  HOH HOH B . 
AA 8 HOH 313 1713 251  HOH HOH B . 
AA 8 HOH 314 1714 362  HOH HOH B . 
AA 8 HOH 315 1715 27   HOH HOH B . 
AA 8 HOH 316 1716 316  HOH HOH B . 
AA 8 HOH 317 1717 606  HOH HOH B . 
AA 8 HOH 318 1718 894  HOH HOH B . 
AA 8 HOH 319 1719 507  HOH HOH B . 
AA 8 HOH 320 1720 533  HOH HOH B . 
AA 8 HOH 321 1721 75   HOH HOH B . 
AA 8 HOH 322 1722 702  HOH HOH B . 
AA 8 HOH 323 1723 897  HOH HOH B . 
AA 8 HOH 324 1724 610  HOH HOH B . 
AA 8 HOH 325 1725 217  HOH HOH B . 
AA 8 HOH 326 1726 883  HOH HOH B . 
AA 8 HOH 327 1727 691  HOH HOH B . 
AA 8 HOH 328 1728 178  HOH HOH B . 
AA 8 HOH 329 1729 544  HOH HOH B . 
AA 8 HOH 330 1730 321  HOH HOH B . 
AA 8 HOH 331 1731 179  HOH HOH B . 
AA 8 HOH 332 1732 962  HOH HOH B . 
AA 8 HOH 333 1733 1287 HOH HOH B . 
AA 8 HOH 334 1734 596  HOH HOH B . 
AA 8 HOH 335 1735 524  HOH HOH B . 
AA 8 HOH 336 1736 196  HOH HOH B . 
AA 8 HOH 337 1737 509  HOH HOH B . 
AA 8 HOH 338 1738 916  HOH HOH B . 
AA 8 HOH 339 1739 941  HOH HOH B . 
AA 8 HOH 340 1740 143  HOH HOH B . 
AA 8 HOH 341 1741 778  HOH HOH B . 
AA 8 HOH 342 1742 1153 HOH HOH B . 
AA 8 HOH 343 1743 1118 HOH HOH B . 
AA 8 HOH 344 1744 649  HOH HOH B . 
AA 8 HOH 345 1745 1280 HOH HOH B . 
AA 8 HOH 346 1746 529  HOH HOH B . 
AA 8 HOH 347 1747 221  HOH HOH B . 
AA 8 HOH 348 1748 1241 HOH HOH B . 
AA 8 HOH 349 1749 418  HOH HOH B . 
AA 8 HOH 350 1750 570  HOH HOH B . 
AA 8 HOH 351 1751 1131 HOH HOH B . 
AA 8 HOH 352 1752 123  HOH HOH B . 
AA 8 HOH 353 1753 288  HOH HOH B . 
AA 8 HOH 354 1754 1518 HOH HOH B . 
AA 8 HOH 355 1755 585  HOH HOH B . 
AA 8 HOH 356 1756 1142 HOH HOH B . 
AA 8 HOH 357 1757 129  HOH HOH B . 
AA 8 HOH 358 1758 611  HOH HOH B . 
AA 8 HOH 359 1759 138  HOH HOH B . 
AA 8 HOH 360 1760 122  HOH HOH B . 
AA 8 HOH 361 1761 24   HOH HOH B . 
AA 8 HOH 362 1762 267  HOH HOH B . 
AA 8 HOH 363 1763 262  HOH HOH B . 
AA 8 HOH 364 1764 604  HOH HOH B . 
AA 8 HOH 365 1765 790  HOH HOH B . 
AA 8 HOH 366 1766 487  HOH HOH B . 
AA 8 HOH 367 1767 58   HOH HOH B . 
AA 8 HOH 368 1768 510  HOH HOH B . 
AA 8 HOH 369 1769 8    HOH HOH B . 
AA 8 HOH 370 1770 845  HOH HOH B . 
AA 8 HOH 371 1771 193  HOH HOH B . 
AA 8 HOH 372 1772 861  HOH HOH B . 
AA 8 HOH 373 1773 271  HOH HOH B . 
AA 8 HOH 374 1774 677  HOH HOH B . 
AA 8 HOH 375 1775 815  HOH HOH B . 
AA 8 HOH 376 1776 1084 HOH HOH B . 
AA 8 HOH 377 1777 920  HOH HOH B . 
AA 8 HOH 378 1778 356  HOH HOH B . 
AA 8 HOH 379 1779 475  HOH HOH B . 
AA 8 HOH 380 1780 180  HOH HOH B . 
AA 8 HOH 381 1781 141  HOH HOH B . 
AA 8 HOH 382 1782 865  HOH HOH B . 
AA 8 HOH 383 1783 427  HOH HOH B . 
AA 8 HOH 384 1784 1536 HOH HOH B . 
AA 8 HOH 385 1785 497  HOH HOH B . 
AA 8 HOH 386 1786 334  HOH HOH B . 
AA 8 HOH 387 1787 274  HOH HOH B . 
AA 8 HOH 388 1788 490  HOH HOH B . 
AA 8 HOH 389 1789 238  HOH HOH B . 
AA 8 HOH 390 1790 591  HOH HOH B . 
AA 8 HOH 391 1791 495  HOH HOH B . 
AA 8 HOH 392 1792 1421 HOH HOH B . 
AA 8 HOH 393 1793 1013 HOH HOH B . 
AA 8 HOH 394 1794 1268 HOH HOH B . 
AA 8 HOH 395 1795 511  HOH HOH B . 
AA 8 HOH 396 1796 637  HOH HOH B . 
AA 8 HOH 397 1797 1035 HOH HOH B . 
AA 8 HOH 398 1798 300  HOH HOH B . 
AA 8 HOH 399 1799 455  HOH HOH B . 
AA 8 HOH 400 1800 1505 HOH HOH B . 
AA 8 HOH 401 1801 151  HOH HOH B . 
AA 8 HOH 402 1802 1133 HOH HOH B . 
AA 8 HOH 403 1803 135  HOH HOH B . 
AA 8 HOH 404 1804 323  HOH HOH B . 
AA 8 HOH 405 1805 1450 HOH HOH B . 
AA 8 HOH 406 1806 202  HOH HOH B . 
AA 8 HOH 407 1807 287  HOH HOH B . 
AA 8 HOH 408 1808 1461 HOH HOH B . 
AA 8 HOH 409 1809 836  HOH HOH B . 
AA 8 HOH 410 1810 194  HOH HOH B . 
AA 8 HOH 411 1811 1481 HOH HOH B . 
AA 8 HOH 412 1812 970  HOH HOH B . 
AA 8 HOH 413 1813 482  HOH HOH B . 
AA 8 HOH 414 1814 467  HOH HOH B . 
AA 8 HOH 415 1815 261  HOH HOH B . 
AA 8 HOH 416 1816 1310 HOH HOH B . 
AA 8 HOH 417 1817 615  HOH HOH B . 
AA 8 HOH 418 1818 969  HOH HOH B . 
AA 8 HOH 419 1819 1516 HOH HOH B . 
AA 8 HOH 420 1820 619  HOH HOH B . 
AA 8 HOH 421 1821 3    HOH HOH B . 
AA 8 HOH 422 1822 1229 HOH HOH B . 
AA 8 HOH 423 1823 57   HOH HOH B . 
AA 8 HOH 424 1824 144  HOH HOH B . 
AA 8 HOH 425 1825 831  HOH HOH B . 
AA 8 HOH 426 1826 984  HOH HOH B . 
AA 8 HOH 427 1827 423  HOH HOH B . 
AA 8 HOH 428 1828 575  HOH HOH B . 
AA 8 HOH 429 1829 82   HOH HOH B . 
AA 8 HOH 430 1830 769  HOH HOH B . 
AA 8 HOH 431 1831 409  HOH HOH B . 
AA 8 HOH 432 1832 1054 HOH HOH B . 
AA 8 HOH 433 1833 693  HOH HOH B . 
AA 8 HOH 434 1834 1137 HOH HOH B . 
AA 8 HOH 435 1835 1537 HOH HOH B . 
AA 8 HOH 436 1836 1197 HOH HOH B . 
AA 8 HOH 437 1837 477  HOH HOH B . 
AA 8 HOH 438 1838 1358 HOH HOH B . 
AA 8 HOH 439 1839 866  HOH HOH B . 
AA 8 HOH 440 1840 1501 HOH HOH B . 
AA 8 HOH 441 1841 440  HOH HOH B . 
AA 8 HOH 442 1842 456  HOH HOH B . 
AA 8 HOH 443 1843 1404 HOH HOH B . 
AA 8 HOH 444 1844 29   HOH HOH B . 
AA 8 HOH 445 1845 796  HOH HOH B . 
AA 8 HOH 446 1846 279  HOH HOH B . 
AA 8 HOH 447 1847 855  HOH HOH B . 
AA 8 HOH 448 1848 310  HOH HOH B . 
AA 8 HOH 449 1849 187  HOH HOH B . 
AA 8 HOH 450 1850 195  HOH HOH B . 
AA 8 HOH 451 1851 1393 HOH HOH B . 
AA 8 HOH 452 1852 1125 HOH HOH B . 
AA 8 HOH 453 1853 7    HOH HOH B . 
AA 8 HOH 454 1854 244  HOH HOH B . 
AA 8 HOH 455 1855 1282 HOH HOH B . 
AA 8 HOH 456 1856 1491 HOH HOH B . 
AA 8 HOH 457 1857 613  HOH HOH B . 
AA 8 HOH 458 1858 284  HOH HOH B . 
AA 8 HOH 459 1859 901  HOH HOH B . 
AA 8 HOH 460 1860 1307 HOH HOH B . 
AA 8 HOH 461 1861 1263 HOH HOH B . 
AA 8 HOH 462 1862 890  HOH HOH B . 
AA 8 HOH 463 1863 485  HOH HOH B . 
AA 8 HOH 464 1864 211  HOH HOH B . 
AA 8 HOH 465 1865 1004 HOH HOH B . 
AA 8 HOH 466 1866 929  HOH HOH B . 
AA 8 HOH 467 1867 127  HOH HOH B . 
AA 8 HOH 468 1868 1329 HOH HOH B . 
AA 8 HOH 469 1869 1434 HOH HOH B . 
AA 8 HOH 470 1870 1235 HOH HOH B . 
AA 8 HOH 471 1871 729  HOH HOH B . 
AA 8 HOH 472 1872 1147 HOH HOH B . 
AA 8 HOH 473 1873 1182 HOH HOH B . 
AA 8 HOH 474 1874 779  HOH HOH B . 
AA 8 HOH 475 1875 410  HOH HOH B . 
AA 8 HOH 476 1876 959  HOH HOH B . 
AA 8 HOH 477 1877 28   HOH HOH B . 
AA 8 HOH 478 1878 1224 HOH HOH B . 
AA 8 HOH 479 1879 875  HOH HOH B . 
AA 8 HOH 480 1880 266  HOH HOH B . 
AA 8 HOH 481 1881 422  HOH HOH B . 
AA 8 HOH 482 1882 879  HOH HOH B . 
AA 8 HOH 483 1883 549  HOH HOH B . 
AA 8 HOH 484 1884 504  HOH HOH B . 
AA 8 HOH 485 1885 673  HOH HOH B . 
AA 8 HOH 486 1886 960  HOH HOH B . 
AA 8 HOH 487 1887 1230 HOH HOH B . 
AA 8 HOH 488 1888 1403 HOH HOH B . 
AA 8 HOH 489 1889 953  HOH HOH B . 
AA 8 HOH 490 1890 1500 HOH HOH B . 
AA 8 HOH 491 1891 92   HOH HOH B . 
AA 8 HOH 492 1892 1331 HOH HOH B . 
AA 8 HOH 493 1893 1186 HOH HOH B . 
AA 8 HOH 494 1894 867  HOH HOH B . 
AA 8 HOH 495 1895 1566 HOH HOH B . 
AA 8 HOH 496 1896 479  HOH HOH B . 
AA 8 HOH 497 1897 465  HOH HOH B . 
AA 8 HOH 498 1898 337  HOH HOH B . 
AA 8 HOH 499 1899 546  HOH HOH B . 
AA 8 HOH 500 1900 1485 HOH HOH B . 
AA 8 HOH 501 1901 555  HOH HOH B . 
AA 8 HOH 502 1902 1490 HOH HOH B . 
AA 8 HOH 503 1903 797  HOH HOH B . 
AA 8 HOH 504 1904 1475 HOH HOH B . 
AA 8 HOH 505 1905 536  HOH HOH B . 
AA 8 HOH 506 1906 1386 HOH HOH B . 
AA 8 HOH 507 1907 1494 HOH HOH B . 
AA 8 HOH 508 1908 1376 HOH HOH B . 
AA 8 HOH 509 1909 417  HOH HOH B . 
AA 8 HOH 510 1910 1187 HOH HOH B . 
AA 8 HOH 511 1911 1195 HOH HOH B . 
AA 8 HOH 512 1912 1483 HOH HOH B . 
AA 8 HOH 513 1913 758  HOH HOH B . 
AA 8 HOH 514 1914 743  HOH HOH B . 
AA 8 HOH 515 1915 140  HOH HOH B . 
AA 8 HOH 516 1916 943  HOH HOH B . 
AA 8 HOH 517 1917 1222 HOH HOH B . 
AA 8 HOH 518 1918 1155 HOH HOH B . 
AA 8 HOH 519 1919 1116 HOH HOH B . 
AA 8 HOH 520 1920 1416 HOH HOH B . 
AA 8 HOH 521 1921 636  HOH HOH B . 
AA 8 HOH 522 1922 1479 HOH HOH B . 
AA 8 HOH 523 1923 1380 HOH HOH B . 
AA 8 HOH 524 1924 1256 HOH HOH B . 
AA 8 HOH 525 1925 921  HOH HOH B . 
AA 8 HOH 526 1926 1284 HOH HOH B . 
AA 8 HOH 527 1927 968  HOH HOH B . 
AA 8 HOH 528 1928 1132 HOH HOH B . 
AA 8 HOH 529 1929 1337 HOH HOH B . 
AA 8 HOH 530 1930 952  HOH HOH B . 
AA 8 HOH 531 1931 1151 HOH HOH B . 
AA 8 HOH 532 1932 1433 HOH HOH B . 
AA 8 HOH 533 1933 1422 HOH HOH B . 
AA 8 HOH 534 1934 1262 HOH HOH B . 
AA 8 HOH 535 1935 1332 HOH HOH B . 
AA 8 HOH 536 1936 1173 HOH HOH B . 
AA 8 HOH 537 1937 956  HOH HOH B . 
AA 8 HOH 538 1938 1558 HOH HOH B . 
AA 8 HOH 539 1939 937  HOH HOH B . 
AA 8 HOH 540 1940 888  HOH HOH B . 
AA 8 HOH 541 1941 1061 HOH HOH B . 
AA 8 HOH 542 1942 1553 HOH HOH B . 
AA 8 HOH 543 1943 1257 HOH HOH B . 
AA 8 HOH 544 1944 1245 HOH HOH B . 
AA 8 HOH 545 1945 713  HOH HOH B . 
AA 8 HOH 546 1946 766  HOH HOH B . 
AA 8 HOH 547 1947 999  HOH HOH B . 
AA 8 HOH 548 1948 1090 HOH HOH B . 
AA 8 HOH 549 1949 954  HOH HOH B . 
AA 8 HOH 550 1950 873  HOH HOH B . 
AA 8 HOH 551 1951 858  HOH HOH B . 
AA 8 HOH 552 1952 1218 HOH HOH B . 
AA 8 HOH 553 1953 1290 HOH HOH B . 
AA 8 HOH 554 1954 849  HOH HOH B . 
AA 8 HOH 555 1955 1529 HOH HOH B . 
AA 8 HOH 556 1956 717  HOH HOH B . 
AA 8 HOH 557 1957 1489 HOH HOH B . 
AA 8 HOH 558 1958 1309 HOH HOH B . 
AA 8 HOH 559 1959 405  HOH HOH B . 
AA 8 HOH 560 1960 770  HOH HOH B . 
AA 8 HOH 561 1961 42   HOH HOH B . 
AA 8 HOH 562 1962 1449 HOH HOH B . 
AA 8 HOH 563 1963 1119 HOH HOH B . 
AA 8 HOH 564 1964 1248 HOH HOH B . 
AA 8 HOH 565 1965 1374 HOH HOH B . 
AA 8 HOH 566 1966 740  HOH HOH B . 
AA 8 HOH 567 1967 957  HOH HOH B . 
AA 8 HOH 568 1968 1308 HOH HOH B . 
AA 8 HOH 569 1969 1459 HOH HOH B . 
AA 8 HOH 570 1970 1267 HOH HOH B . 
AA 8 HOH 571 1971 1129 HOH HOH B . 
AA 8 HOH 572 1972 1163 HOH HOH B . 
AA 8 HOH 573 1973 1232 HOH HOH B . 
AA 8 HOH 574 1974 753  HOH HOH B . 
AA 8 HOH 575 1975 1456 HOH HOH B . 
AA 8 HOH 576 1976 1095 HOH HOH B . 
AA 8 HOH 577 1977 949  HOH HOH B . 
AA 8 HOH 578 1978 854  HOH HOH B . 
AA 8 HOH 579 1979 1123 HOH HOH B . 
AA 8 HOH 580 1980 1355 HOH HOH B . 
AA 8 HOH 581 1981 1528 HOH HOH B . 
AA 8 HOH 582 1982 617  HOH HOH B . 
AA 8 HOH 583 1983 1196 HOH HOH B . 
AA 8 HOH 584 1984 671  HOH HOH B . 
AA 8 HOH 585 1985 1522 HOH HOH B . 
AA 8 HOH 586 1986 664  HOH HOH B . 
AA 8 HOH 587 1987 1102 HOH HOH B . 
AA 8 HOH 588 1988 1223 HOH HOH B . 
AA 8 HOH 589 1989 1412 HOH HOH B . 
AA 8 HOH 590 1990 1305 HOH HOH B . 
AA 8 HOH 591 1991 1356 HOH HOH B . 
AA 8 HOH 592 1992 1156 HOH HOH B . 
AA 8 HOH 593 1993 1231 HOH HOH B . 
AA 8 HOH 594 1994 1435 HOH HOH B . 
AA 8 HOH 595 1995 531  HOH HOH B . 
AA 8 HOH 596 1996 1512 HOH HOH B . 
AA 8 HOH 597 1997 580  HOH HOH B . 
AA 8 HOH 598 1998 1150 HOH HOH B . 
AA 8 HOH 599 1999 1319 HOH HOH B . 
AA 8 HOH 600 2000 184  HOH HOH B . 
AA 8 HOH 601 2001 1194 HOH HOH B . 
AA 8 HOH 602 2002 1533 HOH HOH B . 
AA 8 HOH 603 2003 972  HOH HOH B . 
AA 8 HOH 604 2004 1468 HOH HOH B . 
AA 8 HOH 605 2005 898  HOH HOH B . 
AA 8 HOH 606 2006 1166 HOH HOH B . 
AA 8 HOH 607 2007 1446 HOH HOH B . 
AA 8 HOH 608 2008 378  HOH HOH B . 
AA 8 HOH 609 2009 562  HOH HOH B . 
AA 8 HOH 610 2010 938  HOH HOH B . 
AA 8 HOH 611 2011 1253 HOH HOH B . 
AA 8 HOH 612 2012 1471 HOH HOH B . 
AA 8 HOH 613 2013 705  HOH HOH B . 
AA 8 HOH 614 2014 904  HOH HOH B . 
AA 8 HOH 615 2015 1517 HOH HOH B . 
AA 8 HOH 616 2016 734  HOH HOH B . 
AA 8 HOH 617 2017 1350 HOH HOH B . 
AA 8 HOH 618 2018 803  HOH HOH B . 
AA 8 HOH 619 2019 983  HOH HOH B . 
AA 8 HOH 620 2020 868  HOH HOH B . 
AA 8 HOH 621 2021 1079 HOH HOH B . 
AA 8 HOH 622 2022 722  HOH HOH B . 
AA 8 HOH 623 2023 928  HOH HOH B . 
AA 8 HOH 624 2024 1233 HOH HOH B . 
AA 8 HOH 625 2025 1157 HOH HOH B . 
AA 8 HOH 626 2026 1091 HOH HOH B . 
AA 8 HOH 627 2027 590  HOH HOH B . 
AA 8 HOH 628 2028 1472 HOH HOH B . 
AA 8 HOH 629 2029 884  HOH HOH B . 
AA 8 HOH 630 2030 444  HOH HOH B . 
AA 8 HOH 631 2031 1093 HOH HOH B . 
AA 8 HOH 632 2032 594  HOH HOH B . 
AA 8 HOH 633 2033 961  HOH HOH B . 
AA 8 HOH 634 2034 1547 HOH HOH B . 
AA 8 HOH 635 2035 1117 HOH HOH B . 
AA 8 HOH 636 2036 632  HOH HOH B . 
AA 8 HOH 637 2037 1554 HOH HOH B . 
AA 8 HOH 638 2038 1134 HOH HOH B . 
AA 8 HOH 639 2039 172  HOH HOH B . 
AA 8 HOH 640 2040 1561 HOH HOH B . 
AA 8 HOH 641 2041 1354 HOH HOH B . 
AA 8 HOH 642 2042 1092 HOH HOH B . 
AA 8 HOH 643 2043 641  HOH HOH B . 
AA 8 HOH 644 2044 387  HOH HOH B . 
AA 8 HOH 645 2045 1357 HOH HOH 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 ASP 20   ? CG  ? A ASP 22   CG  
2   1 Y 1 A ASP 20   ? OD1 ? A ASP 22   OD1 
3   1 Y 1 A ASP 20   ? OD2 ? A ASP 22   OD2 
4   1 Y 1 A GLU 52   ? CG  ? A GLU 54   CG  
5   1 Y 1 A GLU 52   ? CD  ? A GLU 54   CD  
6   1 Y 1 A GLU 52   ? OE1 ? A GLU 54   OE1 
7   1 Y 1 A GLU 52   ? OE2 ? A GLU 54   OE2 
8   1 Y 1 A GLU 59   ? CG  ? A GLU 61   CG  
9   1 Y 1 A GLU 59   ? CD  ? A GLU 61   CD  
10  1 Y 1 A GLU 59   ? OE1 ? A GLU 61   OE1 
11  1 Y 1 A GLU 59   ? OE2 ? A GLU 61   OE2 
12  1 Y 1 A GLU 73   ? CG  ? A GLU 75   CG  
13  1 Y 1 A GLU 73   ? CD  ? A GLU 75   CD  
14  1 Y 1 A GLU 73   ? OE1 ? A GLU 75   OE1 
15  1 Y 1 A GLU 73   ? OE2 ? A GLU 75   OE2 
16  1 Y 1 A LYS 78   ? CG  ? A LYS 80   CG  
17  1 Y 1 A LYS 78   ? CD  ? A LYS 80   CD  
18  1 Y 1 A LYS 78   ? CE  ? A LYS 80   CE  
19  1 Y 1 A LYS 78   ? NZ  ? A LYS 80   NZ  
20  1 Y 1 A VAL 84   ? CG1 ? A VAL 86   CG1 
21  1 Y 1 A VAL 84   ? CG2 ? A VAL 86   CG2 
22  1 Y 1 A GLU 85   ? CG  ? A GLU 87   CG  
23  1 Y 1 A GLU 85   ? CD  ? A GLU 87   CD  
24  1 Y 1 A GLU 85   ? OE1 ? A GLU 87   OE1 
25  1 Y 1 A GLU 85   ? OE2 ? A GLU 87   OE2 
26  1 Y 1 A GLN 89   ? CG  ? A GLN 91   CG  
27  1 Y 1 A GLN 89   ? CD  ? A GLN 91   CD  
28  1 Y 1 A GLN 89   ? OE1 ? A GLN 91   OE1 
29  1 Y 1 A GLN 89   ? NE2 ? A GLN 91   NE2 
30  1 Y 1 A ARG 122  ? CG  ? A ARG 124  CG  
31  1 Y 1 A ARG 122  ? CD  ? A ARG 124  CD  
32  1 Y 1 A ARG 122  ? NE  ? A ARG 124  NE  
33  1 Y 1 A ARG 122  ? CZ  ? A ARG 124  CZ  
34  1 Y 1 A ARG 122  ? NH1 ? A ARG 124  NH1 
35  1 Y 1 A ARG 122  ? NH2 ? A ARG 124  NH2 
36  1 Y 1 A LYS 124  ? CG  ? A LYS 126  CG  
37  1 Y 1 A LYS 124  ? CD  ? A LYS 126  CD  
38  1 Y 1 A LYS 124  ? CE  ? A LYS 126  CE  
39  1 Y 1 A LYS 124  ? NZ  ? A LYS 126  NZ  
40  1 Y 1 A ASP 127  ? CG  ? A ASP 129  CG  
41  1 Y 1 A ASP 127  ? OD1 ? A ASP 129  OD1 
42  1 Y 1 A ASP 127  ? OD2 ? A ASP 129  OD2 
43  1 Y 1 A ASN 129  ? CG  ? A ASN 131  CG  
44  1 Y 1 A ASN 129  ? OD1 ? A ASN 131  OD1 
45  1 Y 1 A ASN 129  ? ND2 ? A ASN 131  ND2 
46  1 Y 1 A LYS 131  ? CG  ? A LYS 133  CG  
47  1 Y 1 A LYS 131  ? CD  ? A LYS 133  CD  
48  1 Y 1 A LYS 131  ? CE  ? A LYS 133  CE  
49  1 Y 1 A LYS 131  ? NZ  ? A LYS 133  NZ  
50  1 Y 1 A SER 132  ? OG  ? A SER 134  OG  
51  1 Y 1 A SER 137  ? OG  ? A SER 139  OG  
52  1 Y 1 A LYS 154  ? CG  ? A LYS 156  CG  
53  1 Y 1 A LYS 154  ? CD  ? A LYS 156  CD  
54  1 Y 1 A LYS 154  ? CE  ? A LYS 156  CE  
55  1 Y 1 A LYS 154  ? NZ  ? A LYS 156  NZ  
56  1 Y 1 A LEU 155  ? CG  ? A LEU 157  CG  
57  1 Y 1 A LEU 155  ? CD1 ? A LEU 157  CD1 
58  1 Y 1 A LEU 155  ? CD2 ? A LEU 157  CD2 
59  1 Y 1 A THR 156  ? OG1 ? A THR 158  OG1 
60  1 Y 1 A THR 156  ? CG2 ? A THR 158  CG2 
61  1 Y 1 A ARG 189  ? CG  ? A ARG 191  CG  
62  1 Y 1 A ARG 189  ? CD  ? A ARG 191  CD  
63  1 Y 1 A ARG 189  ? NE  ? A ARG 191  NE  
64  1 Y 1 A ARG 189  ? CZ  ? A ARG 191  CZ  
65  1 Y 1 A ARG 189  ? NH1 ? A ARG 191  NH1 
66  1 Y 1 A ARG 189  ? NH2 ? A ARG 191  NH2 
67  1 Y 1 A LYS 206  ? CG  ? A LYS 208  CG  
68  1 Y 1 A LYS 206  ? CD  ? A LYS 208  CD  
69  1 Y 1 A LYS 206  ? CE  ? A LYS 208  CE  
70  1 Y 1 A LYS 206  ? NZ  ? A LYS 208  NZ  
71  1 Y 1 A LYS 209  ? CG  ? A LYS 211  CG  
72  1 Y 1 A LYS 209  ? CD  ? A LYS 211  CD  
73  1 Y 1 A LYS 209  ? CE  ? A LYS 211  CE  
74  1 Y 1 A LYS 209  ? NZ  ? A LYS 211  NZ  
75  1 Y 1 A GLU 213  ? CG  ? A GLU 215  CG  
76  1 Y 1 A GLU 213  ? CD  ? A GLU 215  CD  
77  1 Y 1 A GLU 213  ? OE1 ? A GLU 215  OE1 
78  1 Y 1 A GLU 213  ? OE2 ? A GLU 215  OE2 
79  1 Y 1 A LYS 214  ? CG  ? A LYS 216  CG  
80  1 Y 1 A LYS 214  ? CD  ? A LYS 216  CD  
81  1 Y 1 A LYS 214  ? CE  ? A LYS 216  CE  
82  1 Y 1 A LYS 214  ? NZ  ? A LYS 216  NZ  
83  1 Y 1 A LYS 437  ? CG  ? A LYS 439  CG  
84  1 Y 1 A LYS 437  ? CD  ? A LYS 439  CD  
85  1 Y 1 A LYS 437  ? CE  ? A LYS 439  CE  
86  1 Y 1 A LYS 437  ? NZ  ? A LYS 439  NZ  
87  1 Y 1 A LEU 449  ? CG  ? A LEU 451  CG  
88  1 Y 1 A LEU 449  ? CD1 ? A LEU 451  CD1 
89  1 Y 1 A LEU 449  ? CD2 ? A LEU 451  CD2 
90  1 Y 1 A ARG 463  ? CG  ? A ARG 465  CG  
91  1 Y 1 A ARG 463  ? CD  ? A ARG 465  CD  
92  1 Y 1 A ARG 463  ? NE  ? A ARG 465  NE  
93  1 Y 1 A ARG 463  ? CZ  ? A ARG 465  CZ  
94  1 Y 1 A ARG 463  ? NH1 ? A ARG 465  NH1 
95  1 Y 1 A ARG 463  ? NH2 ? A ARG 465  NH2 
96  1 Y 1 A GLU 480  ? CG  ? A GLU 482  CG  
97  1 Y 1 A GLU 480  ? CD  ? A GLU 482  CD  
98  1 Y 1 A GLU 480  ? OE1 ? A GLU 482  OE1 
99  1 Y 1 A GLU 480  ? OE2 ? A GLU 482  OE2 
100 1 Y 1 A LEU 482  ? CG  ? A LEU 484  CG  
101 1 Y 1 A LEU 482  ? CD1 ? A LEU 484  CD1 
102 1 Y 1 A LEU 482  ? CD2 ? A LEU 484  CD2 
103 1 Y 1 A ARG 489  ? CG  ? A ARG 491  CG  
104 1 Y 1 A ARG 489  ? CD  ? A ARG 491  CD  
105 1 Y 1 A ARG 489  ? NE  ? A ARG 491  NE  
106 1 Y 1 A ARG 489  ? CZ  ? A ARG 491  CZ  
107 1 Y 1 A ARG 489  ? NH1 ? A ARG 491  NH1 
108 1 Y 1 A ARG 489  ? NH2 ? A ARG 491  NH2 
109 1 Y 1 A ASN 496  ? CG  ? A ASN 498  CG  
110 1 Y 1 A ASN 496  ? OD1 ? A ASN 498  OD1 
111 1 Y 1 A ASN 496  ? ND2 ? A ASN 498  ND2 
112 1 Y 1 A ILE 503  ? CG1 ? A ILE 505  CG1 
113 1 Y 1 A ILE 503  ? CG2 ? A ILE 505  CG2 
114 1 Y 1 A ILE 503  ? CD1 ? A ILE 505  CD1 
115 1 Y 1 A ASN 504  ? CG  ? A ASN 506  CG  
116 1 Y 1 A ASN 504  ? OD1 ? A ASN 506  OD1 
117 1 Y 1 A ASN 504  ? ND2 ? A ASN 506  ND2 
118 1 Y 1 A ASP 505  ? CG  ? A ASP 507  CG  
119 1 Y 1 A ASP 505  ? OD1 ? A ASP 507  OD1 
120 1 Y 1 A ASP 505  ? OD2 ? A ASP 507  OD2 
121 1 Y 1 A LYS 507  ? CG  ? A LYS 509  CG  
122 1 Y 1 A LYS 507  ? CD  ? A LYS 509  CD  
123 1 Y 1 A LYS 507  ? CE  ? A LYS 509  CE  
124 1 Y 1 A LYS 507  ? NZ  ? A LYS 509  NZ  
125 1 Y 1 A ASP 511  ? CG  ? A ASP 513  CG  
126 1 Y 1 A ASP 511  ? OD1 ? A ASP 513  OD1 
127 1 Y 1 A ASP 511  ? OD2 ? A ASP 513  OD2 
128 1 Y 1 A ARG 533  ? CG  ? A ARG 535  CG  
129 1 Y 1 A ARG 533  ? CD  ? A ARG 535  CD  
130 1 Y 1 A ARG 533  ? NE  ? A ARG 535  NE  
131 1 Y 1 A ARG 533  ? CZ  ? A ARG 535  CZ  
132 1 Y 1 A ARG 533  ? NH1 ? A ARG 535  NH1 
133 1 Y 1 A ARG 533  ? NH2 ? A ARG 535  NH2 
134 1 Y 1 A GLU 588  ? CG  ? A GLU 590  CG  
135 1 Y 1 A GLU 588  ? CD  ? A GLU 590  CD  
136 1 Y 1 A GLU 588  ? OE1 ? A GLU 590  OE1 
137 1 Y 1 A GLU 588  ? OE2 ? A GLU 590  OE2 
138 1 Y 1 A GLU 611  ? CG  ? A GLU 613  CG  
139 1 Y 1 A GLU 611  ? CD  ? A GLU 613  CD  
140 1 Y 1 A GLU 611  ? OE1 ? A GLU 613  OE1 
141 1 Y 1 A GLU 611  ? OE2 ? A GLU 613  OE2 
142 1 Y 1 A ARG 615  ? CG  ? A ARG 617  CG  
143 1 Y 1 A ARG 615  ? CD  ? A ARG 617  CD  
144 1 Y 1 A ARG 615  ? NE  ? A ARG 617  NE  
145 1 Y 1 A ARG 615  ? CZ  ? A ARG 617  CZ  
146 1 Y 1 A ARG 615  ? NH1 ? A ARG 617  NH1 
147 1 Y 1 A ARG 615  ? NH2 ? A ARG 617  NH2 
148 1 Y 1 A ARG 618  ? CG  ? A ARG 620  CG  
149 1 Y 1 A ARG 618  ? CD  ? A ARG 620  CD  
150 1 Y 1 A ARG 618  ? NE  ? A ARG 620  NE  
151 1 Y 1 A ARG 618  ? CZ  ? A ARG 620  CZ  
152 1 Y 1 A ARG 618  ? NH1 ? A ARG 620  NH1 
153 1 Y 1 A ARG 618  ? NH2 ? A ARG 620  NH2 
154 1 Y 1 A LEU 824  ? CG  ? A LEU 826  CG  
155 1 Y 1 A LEU 824  ? CD1 ? A LEU 826  CD1 
156 1 Y 1 A LEU 824  ? CD2 ? A LEU 826  CD2 
157 1 Y 1 A ASP 855  ? CG  ? A ASP 857  CG  
158 1 Y 1 A ASP 855  ? OD1 ? A ASP 857  OD1 
159 1 Y 1 A ASP 855  ? OD2 ? A ASP 857  OD2 
160 1 Y 1 A SER 889  ? OG  ? A SER 891  OG  
161 1 Y 1 A LYS 897  ? CG  ? A LYS 899  CG  
162 1 Y 1 A LYS 897  ? CD  ? A LYS 899  CD  
163 1 Y 1 A LYS 897  ? CE  ? A LYS 899  CE  
164 1 Y 1 A LYS 897  ? NZ  ? A LYS 899  NZ  
165 1 Y 1 A LYS 933  ? CG  ? A LYS 935  CG  
166 1 Y 1 A LYS 933  ? CD  ? A LYS 935  CD  
167 1 Y 1 A LYS 933  ? CE  ? A LYS 935  CE  
168 1 Y 1 A LYS 933  ? NZ  ? A LYS 935  NZ  
169 1 Y 1 A GLN 938  ? CG  ? A GLN 940  CG  
170 1 Y 1 A GLN 938  ? CD  ? A GLN 940  CD  
171 1 Y 1 A GLN 938  ? OE1 ? A GLN 940  OE1 
172 1 Y 1 A GLN 938  ? NE2 ? A GLN 940  NE2 
173 1 Y 1 A GLU 940  ? CG  ? A GLU 942  CG  
174 1 Y 1 A GLU 940  ? CD  ? A GLU 942  CD  
175 1 Y 1 A GLU 940  ? OE1 ? A GLU 942  OE1 
176 1 Y 1 A GLU 940  ? OE2 ? A GLU 942  OE2 
177 1 Y 1 A ARG 1063 ? CG  ? A ARG 1065 CG  
178 1 Y 1 A ARG 1063 ? CD  ? A ARG 1065 CD  
179 1 Y 1 A ARG 1063 ? NE  ? A ARG 1065 NE  
180 1 Y 1 A ARG 1063 ? CZ  ? A ARG 1065 CZ  
181 1 Y 1 A ARG 1063 ? NH1 ? A ARG 1065 NH1 
182 1 Y 1 A ARG 1063 ? NH2 ? A ARG 1065 NH2 
183 1 Y 1 A LYS 1139 ? CG  ? A LYS 1141 CG  
184 1 Y 1 A LYS 1139 ? CD  ? A LYS 1141 CD  
185 1 Y 1 A LYS 1139 ? CE  ? A LYS 1141 CE  
186 1 Y 1 A LYS 1139 ? NZ  ? A LYS 1141 NZ  
187 1 Y 1 A GLN 1143 ? CG  ? A GLN 1145 CG  
188 1 Y 1 A GLN 1143 ? CD  ? A GLN 1145 CD  
189 1 Y 1 A GLN 1143 ? OE1 ? A GLN 1145 OE1 
190 1 Y 1 A GLN 1143 ? NE2 ? A GLN 1145 NE2 
191 1 Y 1 A LYS 1153 ? CG  ? A LYS 1155 CG  
192 1 Y 1 A LYS 1153 ? CD  ? A LYS 1155 CD  
193 1 Y 1 A LYS 1153 ? CE  ? A LYS 1155 CE  
194 1 Y 1 A LYS 1153 ? NZ  ? A LYS 1155 NZ  
195 1 Y 1 A GLU 1171 ? CG  ? A GLU 1173 CG  
196 1 Y 1 A GLU 1171 ? CD  ? A GLU 1173 CD  
197 1 Y 1 A GLU 1171 ? OE1 ? A GLU 1173 OE1 
198 1 Y 1 A GLU 1171 ? OE2 ? A GLU 1173 OE2 
199 1 Y 1 B ASP 20   ? CG  ? B ASP 22   CG  
200 1 Y 1 B ASP 20   ? OD1 ? B ASP 22   OD1 
201 1 Y 1 B ASP 20   ? OD2 ? B ASP 22   OD2 
202 1 Y 1 B GLU 52   ? CG  ? B GLU 54   CG  
203 1 Y 1 B GLU 52   ? CD  ? B GLU 54   CD  
204 1 Y 1 B GLU 52   ? OE1 ? B GLU 54   OE1 
205 1 Y 1 B GLU 52   ? OE2 ? B GLU 54   OE2 
206 1 Y 1 B GLN 56   ? CG  ? B GLN 58   CG  
207 1 Y 1 B GLN 56   ? CD  ? B GLN 58   CD  
208 1 Y 1 B GLN 56   ? OE1 ? B GLN 58   OE1 
209 1 Y 1 B GLN 56   ? NE2 ? B GLN 58   NE2 
210 1 Y 1 B SER 57   ? OG  ? B SER 59   OG  
211 1 Y 1 B LYS 58   ? CG  ? B LYS 60   CG  
212 1 Y 1 B LYS 58   ? CD  ? B LYS 60   CD  
213 1 Y 1 B LYS 58   ? CE  ? B LYS 60   CE  
214 1 Y 1 B LYS 58   ? NZ  ? B LYS 60   NZ  
215 1 Y 1 B GLU 59   ? CG  ? B GLU 61   CG  
216 1 Y 1 B GLU 59   ? CD  ? B GLU 61   CD  
217 1 Y 1 B GLU 59   ? OE1 ? B GLU 61   OE1 
218 1 Y 1 B GLU 59   ? OE2 ? B GLU 61   OE2 
219 1 Y 1 B ASP 62   ? CG  ? B ASP 64   CG  
220 1 Y 1 B ASP 62   ? OD1 ? B ASP 64   OD1 
221 1 Y 1 B ASP 62   ? OD2 ? B ASP 64   OD2 
222 1 Y 1 B LYS 70   ? CG  ? B LYS 72   CG  
223 1 Y 1 B LYS 70   ? CD  ? B LYS 72   CD  
224 1 Y 1 B LYS 70   ? CE  ? B LYS 72   CE  
225 1 Y 1 B LYS 70   ? NZ  ? B LYS 72   NZ  
226 1 Y 1 B ILE 72   ? CG1 ? B ILE 74   CG1 
227 1 Y 1 B ILE 72   ? CG2 ? B ILE 74   CG2 
228 1 Y 1 B ILE 72   ? CD1 ? B ILE 74   CD1 
229 1 Y 1 B GLU 73   ? CG  ? B GLU 75   CG  
230 1 Y 1 B GLU 73   ? CD  ? B GLU 75   CD  
231 1 Y 1 B GLU 73   ? OE1 ? B GLU 75   OE1 
232 1 Y 1 B GLU 73   ? OE2 ? B GLU 75   OE2 
233 1 Y 1 B LEU 75   ? CG  ? B LEU 77   CG  
234 1 Y 1 B LEU 75   ? CD1 ? B LEU 77   CD1 
235 1 Y 1 B LEU 75   ? CD2 ? B LEU 77   CD2 
236 1 Y 1 B ARG 76   ? CG  ? B ARG 78   CG  
237 1 Y 1 B ARG 76   ? CD  ? B ARG 78   CD  
238 1 Y 1 B ARG 76   ? NE  ? B ARG 78   NE  
239 1 Y 1 B ARG 76   ? CZ  ? B ARG 78   CZ  
240 1 Y 1 B ARG 76   ? NH1 ? B ARG 78   NH1 
241 1 Y 1 B ARG 76   ? NH2 ? B ARG 78   NH2 
242 1 Y 1 B GLU 85   ? CG  ? B GLU 87   CG  
243 1 Y 1 B GLU 85   ? CD  ? B GLU 87   CD  
244 1 Y 1 B GLU 85   ? OE1 ? B GLU 87   OE1 
245 1 Y 1 B GLU 85   ? OE2 ? B GLU 87   OE2 
246 1 Y 1 B GLN 89   ? CG  ? B GLN 91   CG  
247 1 Y 1 B GLN 89   ? CD  ? B GLN 91   CD  
248 1 Y 1 B GLN 89   ? OE1 ? B GLN 91   OE1 
249 1 Y 1 B GLN 89   ? NE2 ? B GLN 91   NE2 
250 1 Y 1 B THR 116  ? OG1 ? B THR 118  OG1 
251 1 Y 1 B THR 116  ? CG2 ? B THR 118  CG2 
252 1 Y 1 B ARG 122  ? CG  ? B ARG 124  CG  
253 1 Y 1 B ARG 122  ? CD  ? B ARG 124  CD  
254 1 Y 1 B ARG 122  ? NE  ? B ARG 124  NE  
255 1 Y 1 B ARG 122  ? CZ  ? B ARG 124  CZ  
256 1 Y 1 B ARG 122  ? NH1 ? B ARG 124  NH1 
257 1 Y 1 B ARG 122  ? NH2 ? B ARG 124  NH2 
258 1 Y 1 B LYS 124  ? CG  ? B LYS 126  CG  
259 1 Y 1 B LYS 124  ? CD  ? B LYS 126  CD  
260 1 Y 1 B LYS 124  ? CE  ? B LYS 126  CE  
261 1 Y 1 B LYS 124  ? NZ  ? B LYS 126  NZ  
262 1 Y 1 B ASN 129  ? CG  ? B ASN 131  CG  
263 1 Y 1 B ASN 129  ? OD1 ? B ASN 131  OD1 
264 1 Y 1 B ASN 129  ? ND2 ? B ASN 131  ND2 
265 1 Y 1 B LYS 131  ? CG  ? B LYS 133  CG  
266 1 Y 1 B LYS 131  ? CD  ? B LYS 133  CD  
267 1 Y 1 B LYS 131  ? CE  ? B LYS 133  CE  
268 1 Y 1 B LYS 131  ? NZ  ? B LYS 133  NZ  
269 1 Y 1 B SER 132  ? OG  ? B SER 134  OG  
270 1 Y 1 B HIS 133  ? CG  ? B HIS 135  CG  
271 1 Y 1 B HIS 133  ? ND1 ? B HIS 135  ND1 
272 1 Y 1 B HIS 133  ? CD2 ? B HIS 135  CD2 
273 1 Y 1 B HIS 133  ? CE1 ? B HIS 135  CE1 
274 1 Y 1 B HIS 133  ? NE2 ? B HIS 135  NE2 
275 1 Y 1 B ARG 138  ? CG  ? B ARG 140  CG  
276 1 Y 1 B ARG 138  ? CD  ? B ARG 140  CD  
277 1 Y 1 B ARG 138  ? NE  ? B ARG 140  NE  
278 1 Y 1 B ARG 138  ? CZ  ? B ARG 140  CZ  
279 1 Y 1 B ARG 138  ? NH1 ? B ARG 140  NH1 
280 1 Y 1 B ARG 138  ? NH2 ? B ARG 140  NH2 
281 1 Y 1 B LYS 154  ? CG  ? B LYS 156  CG  
282 1 Y 1 B LYS 154  ? CD  ? B LYS 156  CD  
283 1 Y 1 B LYS 154  ? CE  ? B LYS 156  CE  
284 1 Y 1 B LYS 154  ? NZ  ? B LYS 156  NZ  
285 1 Y 1 B LEU 155  ? CG  ? B LEU 157  CG  
286 1 Y 1 B LEU 155  ? CD1 ? B LEU 157  CD1 
287 1 Y 1 B LEU 155  ? CD2 ? B LEU 157  CD2 
288 1 Y 1 B SER 157  ? OG  ? B SER 159  OG  
289 1 Y 1 B ARG 189  ? CG  ? B ARG 191  CG  
290 1 Y 1 B ARG 189  ? CD  ? B ARG 191  CD  
291 1 Y 1 B ARG 189  ? NE  ? B ARG 191  NE  
292 1 Y 1 B ARG 189  ? CZ  ? B ARG 191  CZ  
293 1 Y 1 B ARG 189  ? NH1 ? B ARG 191  NH1 
294 1 Y 1 B ARG 189  ? NH2 ? B ARG 191  NH2 
295 1 Y 1 B GLU 193  ? CG  ? B GLU 195  CG  
296 1 Y 1 B GLU 193  ? CD  ? B GLU 195  CD  
297 1 Y 1 B GLU 193  ? OE1 ? B GLU 195  OE1 
298 1 Y 1 B GLU 193  ? OE2 ? B GLU 195  OE2 
299 1 Y 1 B GLN 194  ? CG  ? B GLN 196  CG  
300 1 Y 1 B GLN 194  ? CD  ? B GLN 196  CD  
301 1 Y 1 B GLN 194  ? OE1 ? B GLN 196  OE1 
302 1 Y 1 B GLN 194  ? NE2 ? B GLN 196  NE2 
303 1 Y 1 B GLU 199  ? CG  ? B GLU 201  CG  
304 1 Y 1 B GLU 199  ? CD  ? B GLU 201  CD  
305 1 Y 1 B GLU 199  ? OE1 ? B GLU 201  OE1 
306 1 Y 1 B GLU 199  ? OE2 ? B GLU 201  OE2 
307 1 Y 1 B LYS 206  ? CG  ? B LYS 208  CG  
308 1 Y 1 B LYS 206  ? CD  ? B LYS 208  CD  
309 1 Y 1 B LYS 206  ? CE  ? B LYS 208  CE  
310 1 Y 1 B LYS 206  ? NZ  ? B LYS 208  NZ  
311 1 Y 1 B GLU 210  ? CG  ? B GLU 212  CG  
312 1 Y 1 B GLU 210  ? CD  ? B GLU 212  CD  
313 1 Y 1 B GLU 210  ? OE1 ? B GLU 212  OE1 
314 1 Y 1 B GLU 210  ? OE2 ? B GLU 212  OE2 
315 1 Y 1 B GLU 213  ? CG  ? B GLU 215  CG  
316 1 Y 1 B GLU 213  ? CD  ? B GLU 215  CD  
317 1 Y 1 B GLU 213  ? OE1 ? B GLU 215  OE1 
318 1 Y 1 B GLU 213  ? OE2 ? B GLU 215  OE2 
319 1 Y 1 B LYS 214  ? CG  ? B LYS 216  CG  
320 1 Y 1 B LYS 214  ? CD  ? B LYS 216  CD  
321 1 Y 1 B LYS 214  ? CE  ? B LYS 216  CE  
322 1 Y 1 B LYS 214  ? NZ  ? B LYS 216  NZ  
323 1 Y 1 B LYS 249  ? CG  ? B LYS 251  CG  
324 1 Y 1 B LYS 249  ? CD  ? B LYS 251  CD  
325 1 Y 1 B LYS 249  ? CE  ? B LYS 251  CE  
326 1 Y 1 B LYS 249  ? NZ  ? B LYS 251  NZ  
327 1 Y 1 B GLU 258  ? CG  ? B GLU 260  CG  
328 1 Y 1 B GLU 258  ? CD  ? B GLU 260  CD  
329 1 Y 1 B GLU 258  ? OE1 ? B GLU 260  OE1 
330 1 Y 1 B GLU 258  ? OE2 ? B GLU 260  OE2 
331 1 Y 1 B LYS 290  ? CG  ? B LYS 292  CG  
332 1 Y 1 B LYS 290  ? CD  ? B LYS 292  CD  
333 1 Y 1 B LYS 290  ? CE  ? B LYS 292  CE  
334 1 Y 1 B LYS 290  ? NZ  ? B LYS 292  NZ  
335 1 Y 1 B LEU 295  ? CG  ? B LEU 297  CG  
336 1 Y 1 B LEU 295  ? CD1 ? B LEU 297  CD1 
337 1 Y 1 B LEU 295  ? CD2 ? B LEU 297  CD2 
338 1 Y 1 B LYS 297  ? CG  ? B LYS 299  CG  
339 1 Y 1 B LYS 297  ? CD  ? B LYS 299  CD  
340 1 Y 1 B LYS 297  ? CE  ? B LYS 299  CE  
341 1 Y 1 B LYS 297  ? NZ  ? B LYS 299  NZ  
342 1 Y 1 B ASP 414  ? CG  ? B ASP 416  CG  
343 1 Y 1 B ASP 414  ? OD1 ? B ASP 416  OD1 
344 1 Y 1 B ASP 414  ? OD2 ? B ASP 416  OD2 
345 1 Y 1 B VAL 415  ? CG1 ? B VAL 417  CG1 
346 1 Y 1 B VAL 415  ? CG2 ? B VAL 417  CG2 
347 1 Y 1 B ASP 438  ? CG  ? B ASP 440  CG  
348 1 Y 1 B ASP 438  ? OD1 ? B ASP 440  OD1 
349 1 Y 1 B ASP 438  ? OD2 ? B ASP 440  OD2 
350 1 Y 1 B PHE 439  ? CG  ? B PHE 441  CG  
351 1 Y 1 B PHE 439  ? CD1 ? B PHE 441  CD1 
352 1 Y 1 B PHE 439  ? CD2 ? B PHE 441  CD2 
353 1 Y 1 B PHE 439  ? CE1 ? B PHE 441  CE1 
354 1 Y 1 B PHE 439  ? CE2 ? B PHE 441  CE2 
355 1 Y 1 B PHE 439  ? CZ  ? B PHE 441  CZ  
356 1 Y 1 B LYS 443  ? CG  ? B LYS 445  CG  
357 1 Y 1 B LYS 443  ? CD  ? B LYS 445  CD  
358 1 Y 1 B LYS 443  ? CE  ? B LYS 445  CE  
359 1 Y 1 B LYS 443  ? NZ  ? B LYS 445  NZ  
360 1 Y 1 B PHE 446  ? CG  ? B PHE 448  CG  
361 1 Y 1 B PHE 446  ? CD1 ? B PHE 448  CD1 
362 1 Y 1 B PHE 446  ? CD2 ? B PHE 448  CD2 
363 1 Y 1 B PHE 446  ? CE1 ? B PHE 448  CE1 
364 1 Y 1 B PHE 446  ? CE2 ? B PHE 448  CE2 
365 1 Y 1 B PHE 446  ? CZ  ? B PHE 448  CZ  
366 1 Y 1 B GLU 454  ? CG  ? B GLU 456  CG  
367 1 Y 1 B GLU 454  ? CD  ? B GLU 456  CD  
368 1 Y 1 B GLU 454  ? OE1 ? B GLU 456  OE1 
369 1 Y 1 B GLU 454  ? OE2 ? B GLU 456  OE2 
370 1 Y 1 B LEU 456  ? CG  ? B LEU 458  CG  
371 1 Y 1 B LEU 456  ? CD1 ? B LEU 458  CD1 
372 1 Y 1 B LEU 456  ? CD2 ? B LEU 458  CD2 
373 1 Y 1 B GLU 458  ? CG  ? B GLU 460  CG  
374 1 Y 1 B GLU 458  ? CD  ? B GLU 460  CD  
375 1 Y 1 B GLU 458  ? OE1 ? B GLU 460  OE1 
376 1 Y 1 B GLU 458  ? OE2 ? B GLU 460  OE2 
377 1 Y 1 B GLU 459  ? CG  ? B GLU 461  CG  
378 1 Y 1 B GLU 459  ? CD  ? B GLU 461  CD  
379 1 Y 1 B GLU 459  ? OE1 ? B GLU 461  OE1 
380 1 Y 1 B GLU 459  ? OE2 ? B GLU 461  OE2 
381 1 Y 1 B VAL 461  ? CG1 ? B VAL 463  CG1 
382 1 Y 1 B VAL 461  ? CG2 ? B VAL 463  CG2 
383 1 Y 1 B ARG 463  ? CG  ? B ARG 465  CG  
384 1 Y 1 B ARG 463  ? CD  ? B ARG 465  CD  
385 1 Y 1 B ARG 463  ? NE  ? B ARG 465  NE  
386 1 Y 1 B ARG 463  ? CZ  ? B ARG 465  CZ  
387 1 Y 1 B ARG 463  ? NH1 ? B ARG 465  NH1 
388 1 Y 1 B ARG 463  ? NH2 ? B ARG 465  NH2 
389 1 Y 1 B GLU 480  ? CG  ? B GLU 482  CG  
390 1 Y 1 B GLU 480  ? CD  ? B GLU 482  CD  
391 1 Y 1 B GLU 480  ? OE1 ? B GLU 482  OE1 
392 1 Y 1 B GLU 480  ? OE2 ? B GLU 482  OE2 
393 1 Y 1 B THR 481  ? OG1 ? B THR 483  OG1 
394 1 Y 1 B THR 481  ? CG2 ? B THR 483  CG2 
395 1 Y 1 B LEU 482  ? CG  ? B LEU 484  CG  
396 1 Y 1 B LEU 482  ? CD1 ? B LEU 484  CD1 
397 1 Y 1 B LEU 482  ? CD2 ? B LEU 484  CD2 
398 1 Y 1 B TYR 485  ? CG  ? B TYR 487  CG  
399 1 Y 1 B TYR 485  ? CD1 ? B TYR 487  CD1 
400 1 Y 1 B TYR 485  ? CD2 ? B TYR 487  CD2 
401 1 Y 1 B TYR 485  ? CE1 ? B TYR 487  CE1 
402 1 Y 1 B TYR 485  ? CE2 ? B TYR 487  CE2 
403 1 Y 1 B TYR 485  ? CZ  ? B TYR 487  CZ  
404 1 Y 1 B TYR 485  ? OH  ? B TYR 487  OH  
405 1 Y 1 B VAL 487  ? CG1 ? B VAL 489  CG1 
406 1 Y 1 B VAL 487  ? CG2 ? B VAL 489  CG2 
407 1 Y 1 B ARG 489  ? CG  ? B ARG 491  CG  
408 1 Y 1 B ARG 489  ? CD  ? B ARG 491  CD  
409 1 Y 1 B ARG 489  ? NE  ? B ARG 491  NE  
410 1 Y 1 B ARG 489  ? CZ  ? B ARG 491  CZ  
411 1 Y 1 B ARG 489  ? NH1 ? B ARG 491  NH1 
412 1 Y 1 B ARG 489  ? NH2 ? B ARG 491  NH2 
413 1 Y 1 B ASN 496  ? CG  ? B ASN 498  CG  
414 1 Y 1 B ASN 496  ? OD1 ? B ASN 498  OD1 
415 1 Y 1 B ASN 496  ? ND2 ? B ASN 498  ND2 
416 1 Y 1 B PHE 499  ? CG  ? B PHE 501  CG  
417 1 Y 1 B PHE 499  ? CD1 ? B PHE 501  CD1 
418 1 Y 1 B PHE 499  ? CD2 ? B PHE 501  CD2 
419 1 Y 1 B PHE 499  ? CE1 ? B PHE 501  CE1 
420 1 Y 1 B PHE 499  ? CE2 ? B PHE 501  CE2 
421 1 Y 1 B PHE 499  ? CZ  ? B PHE 501  CZ  
422 1 Y 1 B VAL 500  ? CG1 ? B VAL 502  CG1 
423 1 Y 1 B VAL 500  ? CG2 ? B VAL 502  CG2 
424 1 Y 1 B HIS 501  ? CG  ? B HIS 503  CG  
425 1 Y 1 B HIS 501  ? ND1 ? B HIS 503  ND1 
426 1 Y 1 B HIS 501  ? CD2 ? B HIS 503  CD2 
427 1 Y 1 B HIS 501  ? CE1 ? B HIS 503  CE1 
428 1 Y 1 B HIS 501  ? NE2 ? B HIS 503  NE2 
429 1 Y 1 B ILE 503  ? CG1 ? B ILE 505  CG1 
430 1 Y 1 B ILE 503  ? CG2 ? B ILE 505  CG2 
431 1 Y 1 B ILE 503  ? CD1 ? B ILE 505  CD1 
432 1 Y 1 B ASN 504  ? CG  ? B ASN 506  CG  
433 1 Y 1 B ASN 504  ? OD1 ? B ASN 506  OD1 
434 1 Y 1 B ASN 504  ? ND2 ? B ASN 506  ND2 
435 1 Y 1 B ASP 505  ? CG  ? B ASP 507  CG  
436 1 Y 1 B ASP 505  ? OD1 ? B ASP 507  OD1 
437 1 Y 1 B ASP 505  ? OD2 ? B ASP 507  OD2 
438 1 Y 1 B LYS 507  ? CG  ? B LYS 509  CG  
439 1 Y 1 B LYS 507  ? CD  ? B LYS 509  CD  
440 1 Y 1 B LYS 507  ? CE  ? B LYS 509  CE  
441 1 Y 1 B LYS 507  ? NZ  ? B LYS 509  NZ  
442 1 Y 1 B VAL 508  ? CG1 ? B VAL 510  CG1 
443 1 Y 1 B VAL 508  ? CG2 ? B VAL 510  CG2 
444 1 Y 1 B SER 509  ? OG  ? B SER 511  OG  
445 1 Y 1 B GLU 512  ? CG  ? B GLU 514  CG  
446 1 Y 1 B GLU 512  ? CD  ? B GLU 514  CD  
447 1 Y 1 B GLU 512  ? OE1 ? B GLU 514  OE1 
448 1 Y 1 B GLU 512  ? OE2 ? B GLU 514  OE2 
449 1 Y 1 B ASP 532  ? CG  ? B ASP 534  CG  
450 1 Y 1 B ASP 532  ? OD1 ? B ASP 534  OD1 
451 1 Y 1 B ASP 532  ? OD2 ? B ASP 534  OD2 
452 1 Y 1 B ARG 533  ? CG  ? B ARG 535  CG  
453 1 Y 1 B ARG 533  ? CD  ? B ARG 535  CD  
454 1 Y 1 B ARG 533  ? NE  ? B ARG 535  NE  
455 1 Y 1 B ARG 533  ? CZ  ? B ARG 535  CZ  
456 1 Y 1 B ARG 533  ? NH1 ? B ARG 535  NH1 
457 1 Y 1 B ARG 533  ? NH2 ? B ARG 535  NH2 
458 1 Y 1 B GLU 588  ? CG  ? B GLU 590  CG  
459 1 Y 1 B GLU 588  ? CD  ? B GLU 590  CD  
460 1 Y 1 B GLU 588  ? OE1 ? B GLU 590  OE1 
461 1 Y 1 B GLU 588  ? OE2 ? B GLU 590  OE2 
462 1 Y 1 B GLU 611  ? CG  ? B GLU 613  CG  
463 1 Y 1 B GLU 611  ? CD  ? B GLU 613  CD  
464 1 Y 1 B GLU 611  ? OE1 ? B GLU 613  OE1 
465 1 Y 1 B GLU 611  ? OE2 ? B GLU 613  OE2 
466 1 Y 1 B ARG 764  ? CG  ? B ARG 766  CG  
467 1 Y 1 B ARG 764  ? CD  ? B ARG 766  CD  
468 1 Y 1 B ARG 764  ? NE  ? B ARG 766  NE  
469 1 Y 1 B ARG 764  ? CZ  ? B ARG 766  CZ  
470 1 Y 1 B ARG 764  ? NH1 ? B ARG 766  NH1 
471 1 Y 1 B ARG 764  ? NH2 ? B ARG 766  NH2 
472 1 Y 1 B GLU 785  ? CG  ? B GLU 787  CG  
473 1 Y 1 B GLU 785  ? CD  ? B GLU 787  CD  
474 1 Y 1 B GLU 785  ? OE1 ? B GLU 787  OE1 
475 1 Y 1 B GLU 785  ? OE2 ? B GLU 787  OE2 
476 1 Y 1 B ARG 788  ? CG  ? B ARG 790  CG  
477 1 Y 1 B ARG 788  ? CD  ? B ARG 790  CD  
478 1 Y 1 B ARG 788  ? NE  ? B ARG 790  NE  
479 1 Y 1 B ARG 788  ? CZ  ? B ARG 790  CZ  
480 1 Y 1 B ARG 788  ? NH1 ? B ARG 790  NH1 
481 1 Y 1 B ARG 788  ? NH2 ? B ARG 790  NH2 
482 1 Y 1 B GLU 810  ? CG  ? B GLU 812  CG  
483 1 Y 1 B GLU 810  ? CD  ? B GLU 812  CD  
484 1 Y 1 B GLU 810  ? OE1 ? B GLU 812  OE1 
485 1 Y 1 B GLU 810  ? OE2 ? B GLU 812  OE2 
486 1 Y 1 B ASP 855  ? CG  ? B ASP 857  CG  
487 1 Y 1 B ASP 855  ? OD1 ? B ASP 857  OD1 
488 1 Y 1 B ASP 855  ? OD2 ? B ASP 857  OD2 
489 1 Y 1 B ARG 878  ? CG  ? B ARG 880  CG  
490 1 Y 1 B ARG 878  ? CD  ? B ARG 880  CD  
491 1 Y 1 B ARG 878  ? NE  ? B ARG 880  NE  
492 1 Y 1 B ARG 878  ? CZ  ? B ARG 880  CZ  
493 1 Y 1 B ARG 878  ? NH1 ? B ARG 880  NH1 
494 1 Y 1 B ARG 878  ? NH2 ? B ARG 880  NH2 
495 1 Y 1 B LEU 905  ? CG  ? B LEU 907  CG  
496 1 Y 1 B LEU 905  ? CD1 ? B LEU 907  CD1 
497 1 Y 1 B LEU 905  ? CD2 ? B LEU 907  CD2 
498 1 Y 1 B ARG 907  ? CG  ? B ARG 909  CG  
499 1 Y 1 B ARG 907  ? CD  ? B ARG 909  CD  
500 1 Y 1 B ARG 907  ? NE  ? B ARG 909  NE  
501 1 Y 1 B ARG 907  ? CZ  ? B ARG 909  CZ  
502 1 Y 1 B ARG 907  ? NH1 ? B ARG 909  NH1 
503 1 Y 1 B ARG 907  ? NH2 ? B ARG 909  NH2 
504 1 Y 1 B LYS 908  ? CG  ? B LYS 910  CG  
505 1 Y 1 B LYS 908  ? CD  ? B LYS 910  CD  
506 1 Y 1 B LYS 908  ? CE  ? B LYS 910  CE  
507 1 Y 1 B LYS 908  ? NZ  ? B LYS 910  NZ  
508 1 Y 1 B ILE 912  ? CG1 ? B ILE 914  CG1 
509 1 Y 1 B ILE 912  ? CG2 ? B ILE 914  CG2 
510 1 Y 1 B ILE 912  ? CD1 ? B ILE 914  CD1 
511 1 Y 1 B SER 916  ? OG  ? B SER 918  OG  
512 1 Y 1 B GLU 917  ? CG  ? B GLU 919  CG  
513 1 Y 1 B GLU 917  ? CD  ? B GLU 919  CD  
514 1 Y 1 B GLU 917  ? OE1 ? B GLU 919  OE1 
515 1 Y 1 B GLU 917  ? OE2 ? B GLU 919  OE2 
516 1 Y 1 B GLU 932  ? CG  ? B GLU 934  CG  
517 1 Y 1 B GLU 932  ? CD  ? B GLU 934  CD  
518 1 Y 1 B GLU 932  ? OE1 ? B GLU 934  OE1 
519 1 Y 1 B GLU 932  ? OE2 ? B GLU 934  OE2 
520 1 Y 1 B LYS 933  ? CG  ? B LYS 935  CG  
521 1 Y 1 B LYS 933  ? CD  ? B LYS 935  CD  
522 1 Y 1 B LYS 933  ? CE  ? B LYS 935  CE  
523 1 Y 1 B LYS 933  ? NZ  ? B LYS 935  NZ  
524 1 Y 1 B GLN 938  ? CG  ? B GLN 940  CG  
525 1 Y 1 B GLN 938  ? CD  ? B GLN 940  CD  
526 1 Y 1 B GLN 938  ? OE1 ? B GLN 940  OE1 
527 1 Y 1 B GLN 938  ? NE2 ? B GLN 940  NE2 
528 1 Y 1 B ARG 952  ? CG  ? B ARG 954  CG  
529 1 Y 1 B ARG 952  ? CD  ? B ARG 954  CD  
530 1 Y 1 B ARG 952  ? NE  ? B ARG 954  NE  
531 1 Y 1 B ARG 952  ? CZ  ? B ARG 954  CZ  
532 1 Y 1 B ARG 952  ? NH1 ? B ARG 954  NH1 
533 1 Y 1 B ARG 952  ? NH2 ? B ARG 954  NH2 
534 1 Y 1 B ARG 958  ? CG  ? B ARG 960  CG  
535 1 Y 1 B ARG 958  ? CD  ? B ARG 960  CD  
536 1 Y 1 B ARG 958  ? NE  ? B ARG 960  NE  
537 1 Y 1 B ARG 958  ? CZ  ? B ARG 960  CZ  
538 1 Y 1 B ARG 958  ? NH1 ? B ARG 960  NH1 
539 1 Y 1 B ARG 958  ? NH2 ? B ARG 960  NH2 
540 1 Y 1 B ARG 1063 ? CG  ? B ARG 1065 CG  
541 1 Y 1 B ARG 1063 ? CD  ? B ARG 1065 CD  
542 1 Y 1 B ARG 1063 ? NE  ? B ARG 1065 NE  
543 1 Y 1 B ARG 1063 ? CZ  ? B ARG 1065 CZ  
544 1 Y 1 B ARG 1063 ? NH1 ? B ARG 1065 NH1 
545 1 Y 1 B ARG 1063 ? NH2 ? B ARG 1065 NH2 
546 1 Y 1 B LYS 1139 ? CG  ? B LYS 1141 CG  
547 1 Y 1 B LYS 1139 ? CD  ? B LYS 1141 CD  
548 1 Y 1 B LYS 1139 ? CE  ? B LYS 1141 CE  
549 1 Y 1 B LYS 1139 ? NZ  ? B LYS 1141 NZ  
550 1 Y 1 B ASN 1140 ? CG  ? B ASN 1142 CG  
551 1 Y 1 B ASN 1140 ? OD1 ? B ASN 1142 OD1 
552 1 Y 1 B ASN 1140 ? ND2 ? B ASN 1142 ND2 
553 1 Y 1 B GLN 1143 ? CG  ? B GLN 1145 CG  
554 1 Y 1 B GLN 1143 ? CD  ? B GLN 1145 CD  
555 1 Y 1 B GLN 1143 ? OE1 ? B GLN 1145 OE1 
556 1 Y 1 B GLN 1143 ? NE2 ? B GLN 1145 NE2 
557 1 Y 1 B LEU 1147 ? CG  ? B LEU 1149 CG  
558 1 Y 1 B LEU 1147 ? CD1 ? B LEU 1149 CD1 
559 1 Y 1 B LEU 1147 ? CD2 ? B LEU 1149 CD2 
560 1 Y 1 B LYS 1153 ? CG  ? B LYS 1155 CG  
561 1 Y 1 B LYS 1153 ? CD  ? B LYS 1155 CD  
562 1 Y 1 B LYS 1153 ? CE  ? B LYS 1155 CE  
563 1 Y 1 B LYS 1153 ? NZ  ? B LYS 1155 NZ  
564 1 Y 1 B GLU 1171 ? CG  ? B GLU 1173 CG  
565 1 Y 1 B GLU 1171 ? CD  ? B GLU 1173 CD  
566 1 Y 1 B GLU 1171 ? OE1 ? B GLU 1173 OE1 
567 1 Y 1 B GLU 1171 ? OE2 ? B GLU 1173 OE2 
568 1 Y 1 B ARG 1200 ? CG  ? B ARG 1202 CG  
569 1 Y 1 B ARG 1200 ? CD  ? B ARG 1202 CD  
570 1 Y 1 B ARG 1200 ? NE  ? B ARG 1202 NE  
571 1 Y 1 B ARG 1200 ? CZ  ? B ARG 1202 CZ  
572 1 Y 1 B ARG 1200 ? NH1 ? B ARG 1202 NH1 
573 1 Y 1 B ARG 1200 ? NH2 ? B ARG 1202 NH2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20.1_4487 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .           4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   106.29 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9DL4 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     101.155 
_cell.length_a_esd                 ? 
_cell.length_b                     102.373 
_cell.length_b_esd                 ? 
_cell.length_c                     127.504 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         9DL4 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 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                   9DL4 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.40 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.77 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;Reservoir contained 0.1 M HEPES, pH 7.5, 0.1 M sodium formate, 0.1 M magnesium chloride, 0.2 M ammonium sulfate, and 20% (w/v) PEG 3350. Crystal was soaked in cryobuffer containing 25 mM 2-pyridinethiol and 20% PEG 200
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CMOS 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'RDI CMOS_8M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-07-01 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.00 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ALS BEAMLINE 4.2.2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.00 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   4.2.2 
_diffrn_source.pdbx_synchrotron_site       ALS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9DL4 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.80 
_reflns.d_resolution_low                               48.55 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     426838 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.17 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.081 
_reflns.pdbx_Rpim_I_all                                0.031 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.074 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.80 
_reflns_shell.d_res_low                                     1.83 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           79769 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             11331 
_reflns_shell.percent_possible_obs                          100.0 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               7.0 
_reflns_shell.pdbx_chi_squared                              0.93 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.6 
_reflns_shell.pdbx_Rrim_I_all                               1.286 
_reflns_shell.pdbx_Rpim_I_all                               0.483 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.628 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.190 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9DL4 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.80 
_refine.ls_d_res_low                             40.77 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     426838 
_refine.ls_number_reflns_R_free                  20891 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    93.81 
_refine.ls_percent_reflns_R_free                 4.89 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1955 
_refine.ls_R_factor_R_free                       0.2242 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1940 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.02 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 25.34 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.25 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.80 
_refine_hist.d_res_low                        40.77 
_refine_hist.number_atoms_solvent             1393 
_refine_hist.number_atoms_total               19151 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        17523 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         235 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.006  ? 18176 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.823  ? 24778 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 13.590 ? 6568  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.049  ? 2913  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008  ? 3230  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.80 1.82  . . 682 14361 100.00 . . . . 0.2844 . . . . . . . . . . . 0.3402 
'X-RAY DIFFRACTION' 1.82 1.84  . . 722 14524 100.00 . . . . 0.2851 . . . . . . . . . . . 0.3128 
'X-RAY DIFFRACTION' 1.84 1.86  . . 760 14246 100.00 . . . . 0.3031 . . . . . . . . . . . 0.3508 
'X-RAY DIFFRACTION' 1.86 1.89  . . 774 14237 99.00  . . . . 0.3535 . . . . . . . . . . . 0.4202 
'X-RAY DIFFRACTION' 1.89 1.91  . . 271 4669  33.00  . . . . 0.6891 . . . . . . . . . . . 0.7278 
'X-RAY DIFFRACTION' 1.91 1.94  . . 476 8377  58.00  . . . . 0.5040 . . . . . . . . . . . 0.5555 
'X-RAY DIFFRACTION' 1.94 1.97  . . 746 14429 100.00 . . . . 0.2756 . . . . . . . . . . . 0.3146 
'X-RAY DIFFRACTION' 1.97 2.00  . . 696 14377 100.00 . . . . 0.2505 . . . . . . . . . . . 0.2762 
'X-RAY DIFFRACTION' 2.00 2.03  . . 861 14397 100.00 . . . . 0.2324 . . . . . . . . . . . 0.2698 
'X-RAY DIFFRACTION' 2.03 2.06  . . 784 14366 100.00 . . . . 0.2204 . . . . . . . . . . . 0.2716 
'X-RAY DIFFRACTION' 2.06 2.10  . . 689 14446 100.00 . . . . 0.2095 . . . . . . . . . . . 0.2537 
'X-RAY DIFFRACTION' 2.10 2.13  . . 720 14445 100.00 . . . . 0.1982 . . . . . . . . . . . 0.2477 
'X-RAY DIFFRACTION' 2.13 2.18  . . 713 14405 100.00 . . . . 0.2092 . . . . . . . . . . . 0.2552 
'X-RAY DIFFRACTION' 2.18 2.22  . . 589 12558 87.00  . . . . 0.3072 . . . . . . . . . . . 0.3462 
'X-RAY DIFFRACTION' 2.22 2.27  . . 413 8070  56.00  . . . . 0.4986 . . . . . . . . . . . 0.5755 
'X-RAY DIFFRACTION' 2.27 2.32  . . 718 13663 95.00  . . . . 0.2309 . . . . . . . . . . . 0.2759 
'X-RAY DIFFRACTION' 2.32 2.38  . . 677 14450 100.00 . . . . 0.1855 . . . . . . . . . . . 0.2384 
'X-RAY DIFFRACTION' 2.38 2.44  . . 726 14532 100.00 . . . . 0.1873 . . . . . . . . . . . 0.2278 
'X-RAY DIFFRACTION' 2.44 2.51  . . 795 14288 100.00 . . . . 0.1871 . . . . . . . . . . . 0.2299 
'X-RAY DIFFRACTION' 2.51 2.60  . . 733 14489 100.00 . . . . 0.1897 . . . . . . . . . . . 0.2157 
'X-RAY DIFFRACTION' 2.60 2.69  . . 777 14300 100.00 . . . . 0.1870 . . . . . . . . . . . 0.2336 
'X-RAY DIFFRACTION' 2.69 2.80  . . 742 14369 100.00 . . . . 0.1894 . . . . . . . . . . . 0.2348 
'X-RAY DIFFRACTION' 2.80 2.92  . . 703 14467 100.00 . . . . 0.1874 . . . . . . . . . . . 0.2230 
'X-RAY DIFFRACTION' 2.92 3.08  . . 761 14322 99.00  . . . . 0.1910 . . . . . . . . . . . 0.2138 
'X-RAY DIFFRACTION' 3.08 3.27  . . 762 14332 99.00  . . . . 0.1871 . . . . . . . . . . . 0.2132 
'X-RAY DIFFRACTION' 3.27 3.52  . . 716 14259 99.00  . . . . 0.1736 . . . . . . . . . . . 0.1987 
'X-RAY DIFFRACTION' 3.52 3.88  . . 740 13659 95.00  . . . . 0.1652 . . . . . . . . . . . 0.1824 
'X-RAY DIFFRACTION' 3.88 4.44  . . 676 14198 98.00  . . . . 0.1382 . . . . . . . . . . . 0.1607 
'X-RAY DIFFRACTION' 4.44 5.59  . . 758 14344 100.00 . . . . 0.1449 . . . . . . . . . . . 0.1646 
'X-RAY DIFFRACTION' 5.59 40.77 . . 711 14368 99.00  . . . . 0.1526 . . . . . . . . . . . 0.1585 
# 
_struct.entry_id                     9DL4 
_struct.title                        'Structure of proline utilization A complexed with 2-pyridinethiol' 
_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        9DL4 
_struct_keywords.text            
;FLAVOENZYME, ROSSMANN FOLD, PROLINE DEHYDROGENASE, ALDEHYDE DEHYDROGENASE, PROLINE CATABOLISM, SUBSTRATE CHANNELING, BIFUNCTIONAL ENZYME, OXIDOREDUCTASE
;
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
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 3 ? 
E  N N 4 ? 
F  N N 3 ? 
G  N N 3 ? 
H  N N 3 ? 
I  N N 5 ? 
J  N N 3 ? 
K  N N 6 ? 
L  N N 6 ? 
M  N N 6 ? 
N  N N 6 ? 
O  N N 7 ? 
P  N N 2 ? 
Q  N N 3 ? 
R  N N 4 ? 
S  N N 3 ? 
T  N N 3 ? 
U  N N 5 ? 
V  N N 5 ? 
W  N N 6 ? 
X  N N 6 ? 
Y  N N 7 ? 
Z  N N 8 ? 
AA N N 8 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    F7X6I3_SINMM 
_struct_ref.pdbx_db_accession          F7X6I3 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSPNPLQKPAIDAAPAPFADFAPPVRPQSTLRRAITAAYRRPETECLPPLVEAATQSKEIRDAAASTARKLIEALRGKHS
GSGVEGLVQEYSLSSQEGVALMCLAEALLRIPDTATRDALIRDKIADGNWKSHLGGSRSLFVNAATWGLVVTGKLTSTVN
DRSLAAALTRLISRCGEPVIRRGVDMAMRMMGEQFVTGETIREALKRSKELEEKGFSYSYDMLGEAATTAADAERYYRDY
ESAIHAIGKASAGRGIYEGPGISIKLSALHPRYSRAQAARVMGELLPRVKALALLAKNYDIGLNIDAEEADRLELSLDLL
EVLCLDGDLSGWNGMGFVVQAYGKRCPFVLDFIIDLARRSGRRIMVRLVKGAYWDAEIKRAQLDGLADFPVFTRKIHTDV
SYIACAAKLLAATDVVFPQFATHNAQTLAAIYHMAGKDFHVGKYEFQCLHGMGEPLYEEVVGRGKLDRPCRIYAPVGTHE
TLLAYLVRRLLENGANSSFVHRINDPKVSIDELIADPVEVVRAMPVVGAKHDRIALPAELFGDARTNSAGLDLSNEETLA
SLTEALRESAAMKWTALPQLATGPAAGETRTVLNPGDHRDVVGSVTETSEEDARRAVRLAADAAPDWAAVPPSERAACLD
RAAELMQARMPTLLGLIIREAGKSALNAIAEVREAIDFLRYYAEQTRRTLGPGHGPLGPIVCISPWNFPLAIFTGQIAAA
LVAGNPVLAKPAEETPLIAAEGVRILREAGIPASALQLLPGDGRVGAALVAAAETAGVMFTGSTEVARLIQAQLADRLSP
AGRPIPLIAETGGQNAMIVDSSALAEQVVGDVITSAFDSAGQRCSALRVLCLQEDVADRILTMLKGALHELHIGRTDRLS
VDVGPVITSEAKDNIEKHIERMRGLGRKVEQIGLASETGVGTFVPPTIIELEKLSDLQREVFGPVLHVIRYRRDDLDRLV
DDVNATGYGLTFGLHTRLDETIAHVTSRIKAGNLYINRNIIGAVVGVQPFGGRGLSGTGPKAGGPLYLGRLVTTAPVPPQ
HSSVHTDPVLLDFAKWLDGKGARAEAEAARNAGSSSALGLDLELPGPVGERNLYTLHARGRILLVPATESGLYHQLAAAL
ATGNSVAIDAASGLQASLKNLPQTVGLRVSWSKDWAADGPFAGALVEGDAERIRAVNKAIAALPGPLLLVQAASSGEIAR
NPDAYCLNWLVEEVSASINTAAAGGNASLMAIG
;
_struct_ref.pdbx_align_begin           1 
# 
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 9DL4 A 3 ? 1235 ? F7X6I3 1 ? 1233 ? 1 1233 
2 1 9DL4 B 3 ? 1235 ? F7X6I3 1 ? 1233 ? 1 1233 
# 
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 9DL4 SER A 1 ? UNP F7X6I3 ? ? 'expression tag' -1 1 
1 9DL4 MET A 2 ? UNP F7X6I3 ? ? 'expression tag' 0  2 
2 9DL4 SER B 1 ? UNP F7X6I3 ? ? 'expression tag' -1 3 
2 9DL4 MET B 2 ? UNP F7X6I3 ? ? 'expression tag' 0  4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric   2 
2 author_defined_assembly              ?    monomeric 1 
3 author_defined_assembly              ?    monomeric 1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 11070 ? 
1 MORE         -83   ? 
1 'SSA (A^2)'  80200 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA 
2 1 A,C,D,E,F,G,H,I,J,K,L,M,N,O,Z                          
3 1 B,P,Q,R,S,T,U,V,W,X,Y,AA                               
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_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 31   ? ALA A 40   ? SER A 29   ALA A 38   1 ? 10 
HELX_P HELX_P2   AA2 PRO A 44   ? THR A 57   ? PRO A 42   THR A 55   1 ? 14 
HELX_P HELX_P3   AA3 SER A 59   ? GLY A 79   ? SER A 57   GLY A 77   1 ? 21 
HELX_P HELX_P4   AA4 VAL A 86   ? TYR A 93   ? VAL A 84   TYR A 91   1 ? 8  
HELX_P HELX_P5   AA5 SER A 96   ? ARG A 112  ? SER A 94   ARG A 110  1 ? 17 
HELX_P HELX_P6   AA6 ASP A 115  ? LYS A 126  ? ASP A 113  LYS A 124  1 ? 12 
HELX_P HELX_P7   AA7 ASN A 131  ? LEU A 136  ? ASN A 129  LEU A 134  1 ? 6  
HELX_P HELX_P8   AA8 ASN A 145  ? GLY A 155  ? ASN A 143  GLY A 153  1 ? 11 
HELX_P HELX_P9   AA9 ASN A 162  ? GLY A 178  ? ASN A 160  GLY A 176  1 ? 17 
HELX_P HELX_P10  AB1 GLY A 178  ? GLN A 196  ? GLY A 176  GLN A 194  1 ? 19 
HELX_P HELX_P11  AB2 THR A 202  ? LYS A 216  ? THR A 200  LYS A 214  1 ? 15 
HELX_P HELX_P12  AB3 THR A 231  ? ALA A 254  ? THR A 229  ALA A 252  1 ? 24 
HELX_P HELX_P13  AB4 ARG A 256  ? GLY A 261  ? ARG A 254  GLY A 259  1 ? 6  
HELX_P HELX_P14  AB5 LYS A 267  ? LEU A 271  ? LYS A 265  LEU A 269  5 ? 5  
HELX_P HELX_P15  AB6 SER A 276  ? ALA A 278  ? SER A 274  ALA A 276  5 ? 3  
HELX_P HELX_P16  AB7 GLN A 279  ? ASP A 302  ? GLN A 277  ASP A 300  1 ? 24 
HELX_P HELX_P17  AB8 GLU A 311  ? ASP A 313  ? GLU A 309  ASP A 311  5 ? 3  
HELX_P HELX_P18  AB9 ARG A 314  ? ASP A 328  ? ARG A 312  ASP A 326  1 ? 15 
HELX_P HELX_P19  AC1 GLY A 329  ? SER A 332  ? GLY A 327  SER A 330  5 ? 4  
HELX_P HELX_P20  AC2 ARG A 347  ? GLY A 363  ? ARG A 345  GLY A 361  1 ? 17 
HELX_P HELX_P21  AC3 TYR A 375  ? ASP A 386  ? TYR A 373  ASP A 384  1 ? 12 
HELX_P HELX_P22  AC4 ARG A 396  ? ALA A 413  ? ARG A 394  ALA A 411  1 ? 18 
HELX_P HELX_P23  AC5 ASN A 426  ? GLY A 438  ? ASN A 424  GLY A 436  1 ? 13 
HELX_P HELX_P24  AC6 GLY A 455  ? GLU A 460  ? GLY A 453  GLU A 458  1 ? 6  
HELX_P HELX_P25  AC7 THR A 480  ? TYR A 487  ? THR A 478  TYR A 485  1 ? 8  
HELX_P HELX_P26  AC8 TYR A 487  ? LEU A 493  ? TYR A 485  LEU A 491  1 ? 7  
HELX_P HELX_P27  AC9 SER A 500  ? ASN A 506  ? SER A 498  ASN A 504  1 ? 7  
HELX_P HELX_P28  AD1 SER A 511  ? ILE A 516  ? SER A 509  ILE A 514  1 ? 6  
HELX_P HELX_P29  AD2 ASP A 518  ? ALA A 525  ? ASP A 516  ALA A 523  1 ? 8  
HELX_P HELX_P30  AD3 LEU A 538  ? LEU A 542  ? LEU A 536  LEU A 540  5 ? 5  
HELX_P HELX_P31  AD4 ASN A 557  ? ALA A 572  ? ASN A 555  ALA A 570  1 ? 16 
HELX_P HELX_P32  AD5 SER A 611  ? VAL A 632  ? SER A 609  VAL A 630  1 ? 22 
HELX_P HELX_P33  AD6 PRO A 633  ? ARG A 651  ? PRO A 631  ARG A 649  1 ? 19 
HELX_P HELX_P34  AD7 ARG A 651  ? GLY A 664  ? ARG A 649  GLY A 662  1 ? 14 
HELX_P HELX_P35  AD8 SER A 666  ? LEU A 692  ? SER A 664  LEU A 690  1 ? 27 
HELX_P HELX_P36  AD9 LEU A 712  ? ALA A 725  ? LEU A 710  ALA A 723  1 ? 14 
HELX_P HELX_P37  AE1 THR A 737  ? ALA A 751  ? THR A 735  ALA A 749  1 ? 15 
HELX_P HELX_P38  AE2 ASP A 764  ? ALA A 774  ? ASP A 762  ALA A 772  1 ? 11 
HELX_P HELX_P39  AE3 SER A 785  ? ASP A 798  ? SER A 783  ASP A 796  1 ? 14 
HELX_P HELX_P40  AE4 LEU A 826  ? ASP A 840  ? LEU A 824  ASP A 838  1 ? 15 
HELX_P HELX_P41  AE5 SER A 841  ? GLN A 844  ? SER A 839  GLN A 842  5 ? 4  
HELX_P HELX_P42  AE6 GLU A 856  ? HIS A 871  ? GLU A 854  HIS A 869  1 ? 16 
HELX_P HELX_P43  AE7 THR A 890  ? LEU A 907  ? THR A 888  LEU A 905  1 ? 18 
HELX_P HELX_P44  AE8 ALA A 917  ? GLY A 923  ? ALA A 915  GLY A 921  5 ? 7  
HELX_P HELX_P45  AE9 LYS A 935  ? LEU A 939  ? LYS A 933  LEU A 937  5 ? 5  
HELX_P HELX_P46  AF1 ARG A 954  ? ASP A 956  ? ARG A 952  ASP A 954  5 ? 3  
HELX_P HELX_P47  AF2 ASP A 957  ? THR A 968  ? ASP A 955  THR A 966  1 ? 12 
HELX_P HELX_P48  AF3 LEU A 980  ? ILE A 991  ? LEU A 978  ILE A 989  1 ? 12 
HELX_P HELX_P49  AF4 ARG A 1015 ? GLY A 1019 ? ARG A 1013 GLY A 1017 5 ? 5  
HELX_P HELX_P50  AF5 TYR A 1029 ? VAL A 1034 ? TYR A 1027 VAL A 1032 5 ? 6  
HELX_P HELX_P51  AF6 ASP A 1049 ? LYS A 1062 ? ASP A 1047 LYS A 1060 1 ? 14 
HELX_P HELX_P52  AF7 ALA A 1064 ? SER A 1078 ? ALA A 1062 SER A 1076 1 ? 15 
HELX_P HELX_P53  AF8 THR A 1110 ? THR A 1124 ? THR A 1108 THR A 1122 1 ? 15 
HELX_P HELX_P54  AF9 ALA A 1133 ? GLY A 1135 ? ALA A 1131 GLY A 1133 5 ? 3  
HELX_P HELX_P55  AG1 LEU A 1136 ? LYS A 1141 ? LEU A 1134 LYS A 1139 5 ? 6  
HELX_P HELX_P56  AG2 PRO A 1144 ? LEU A 1149 ? PRO A 1142 LEU A 1147 1 ? 6  
HELX_P HELX_P57  AG3 ASP A 1156 ? ASP A 1160 ? ASP A 1154 ASP A 1158 5 ? 5  
HELX_P HELX_P58  AG4 ASP A 1171 ? ALA A 1184 ? ASP A 1169 ALA A 1182 1 ? 14 
HELX_P HELX_P59  AG5 SER A 1196 ? ASN A 1203 ? SER A 1194 ASN A 1201 1 ? 8  
HELX_P HELX_P60  AG6 CYS A 1208 ? TRP A 1211 ? CYS A 1206 TRP A 1209 5 ? 4  
HELX_P HELX_P61  AG7 SER B 31   ? ALA B 40   ? SER B 29   ALA B 38   1 ? 10 
HELX_P HELX_P62  AG8 PRO B 44   ? ALA B 56   ? PRO B 42   ALA B 54   1 ? 13 
HELX_P HELX_P63  AG9 SER B 59   ? GLY B 79   ? SER B 57   GLY B 77   1 ? 21 
HELX_P HELX_P64  AH1 VAL B 86   ? SER B 94   ? VAL B 84   SER B 92   1 ? 9  
HELX_P HELX_P65  AH2 SER B 96   ? ARG B 112  ? SER B 94   ARG B 110  1 ? 17 
HELX_P HELX_P66  AH3 ASP B 115  ? LYS B 126  ? ASP B 113  LYS B 124  1 ? 12 
HELX_P HELX_P67  AH4 ASN B 131  ? LEU B 136  ? ASN B 129  LEU B 134  1 ? 6  
HELX_P HELX_P68  AH5 ASN B 145  ? GLY B 155  ? ASN B 143  GLY B 153  1 ? 11 
HELX_P HELX_P69  AH6 ASN B 162  ? GLY B 178  ? ASN B 160  GLY B 176  1 ? 17 
HELX_P HELX_P70  AH7 GLY B 178  ? GLN B 196  ? GLY B 176  GLN B 194  1 ? 19 
HELX_P HELX_P71  AH8 THR B 202  ? LYS B 216  ? THR B 200  LYS B 214  1 ? 15 
HELX_P HELX_P72  AH9 THR B 231  ? ALA B 254  ? THR B 229  ALA B 252  1 ? 24 
HELX_P HELX_P73  AI1 ARG B 256  ? GLY B 261  ? ARG B 254  GLY B 259  1 ? 6  
HELX_P HELX_P74  AI2 LYS B 267  ? HIS B 272  ? LYS B 265  HIS B 270  5 ? 6  
HELX_P HELX_P75  AI3 SER B 276  ? ALA B 278  ? SER B 274  ALA B 276  5 ? 3  
HELX_P HELX_P76  AI4 GLN B 279  ? ASP B 302  ? GLN B 277  ASP B 300  1 ? 24 
HELX_P HELX_P77  AI5 GLU B 311  ? ASP B 313  ? GLU B 309  ASP B 311  5 ? 3  
HELX_P HELX_P78  AI6 ARG B 314  ? ASP B 328  ? ARG B 312  ASP B 326  1 ? 15 
HELX_P HELX_P79  AI7 GLY B 329  ? SER B 332  ? GLY B 327  SER B 330  5 ? 4  
HELX_P HELX_P80  AI8 ARG B 347  ? GLY B 363  ? ARG B 345  GLY B 361  1 ? 17 
HELX_P HELX_P81  AI9 TYR B 375  ? ASP B 386  ? TYR B 373  ASP B 384  1 ? 12 
HELX_P HELX_P82  AJ1 ARG B 396  ? ALA B 413  ? ARG B 394  ALA B 411  1 ? 18 
HELX_P HELX_P83  AJ2 ASN B 426  ? ALA B 437  ? ASN B 424  ALA B 435  1 ? 12 
HELX_P HELX_P84  AJ3 GLY B 455  ? GLU B 461  ? GLY B 453  GLU B 459  1 ? 7  
HELX_P HELX_P85  AJ4 THR B 480  ? LEU B 493  ? THR B 478  LEU B 491  1 ? 14 
HELX_P HELX_P86  AJ5 SER B 500  ? ILE B 505  ? SER B 498  ILE B 503  1 ? 6  
HELX_P HELX_P87  AJ6 SER B 511  ? ILE B 516  ? SER B 509  ILE B 514  1 ? 6  
HELX_P HELX_P88  AJ7 ASP B 518  ? ALA B 525  ? ASP B 516  ALA B 523  1 ? 8  
HELX_P HELX_P89  AJ8 LEU B 538  ? LEU B 542  ? LEU B 536  LEU B 540  5 ? 5  
HELX_P HELX_P90  AJ9 PHE B 543  ? ARG B 547  ? PHE B 541  ARG B 545  5 ? 5  
HELX_P HELX_P91  AK1 ASN B 557  ? ALA B 573  ? ASN B 555  ALA B 571  1 ? 17 
HELX_P HELX_P92  AK2 SER B 611  ? ALA B 631  ? SER B 609  ALA B 629  1 ? 21 
HELX_P HELX_P93  AK3 PRO B 633  ? ARG B 651  ? PRO B 631  ARG B 649  1 ? 19 
HELX_P HELX_P94  AK4 ARG B 651  ? GLY B 664  ? ARG B 649  GLY B 662  1 ? 14 
HELX_P HELX_P95  AK5 SER B 666  ? LEU B 692  ? SER B 664  LEU B 690  1 ? 27 
HELX_P HELX_P96  AK6 LEU B 712  ? ALA B 725  ? LEU B 710  ALA B 723  1 ? 14 
HELX_P HELX_P97  AK7 THR B 737  ? ALA B 751  ? THR B 735  ALA B 749  1 ? 15 
HELX_P HELX_P98  AK8 PRO B 754  ? SER B 756  ? PRO B 752  SER B 754  5 ? 3  
HELX_P HELX_P99  AK9 ASP B 764  ? ALA B 774  ? ASP B 762  ALA B 772  1 ? 11 
HELX_P HELX_P100 AL1 SER B 785  ? ASP B 798  ? SER B 783  ASP B 796  1 ? 14 
HELX_P HELX_P101 AL2 LEU B 826  ? ASP B 840  ? LEU B 824  ASP B 838  1 ? 15 
HELX_P HELX_P102 AL3 SER B 841  ? GLN B 844  ? SER B 839  GLN B 842  5 ? 4  
HELX_P HELX_P103 AL4 GLU B 856  ? HIS B 871  ? GLU B 854  HIS B 869  1 ? 16 
HELX_P HELX_P104 AL5 THR B 890  ? LEU B 907  ? THR B 888  LEU B 905  1 ? 18 
HELX_P HELX_P105 AL6 ALA B 917  ? GLY B 923  ? ALA B 915  GLY B 921  5 ? 7  
HELX_P HELX_P106 AL7 LYS B 935  ? LEU B 939  ? LYS B 933  LEU B 937  5 ? 5  
HELX_P HELX_P107 AL8 ARG B 954  ? ASP B 956  ? ARG B 952  ASP B 954  5 ? 3  
HELX_P HELX_P108 AL9 ASP B 957  ? ALA B 967  ? ASP B 955  ALA B 965  1 ? 11 
HELX_P HELX_P109 AM1 LEU B 980  ? ILE B 991  ? LEU B 978  ILE B 989  1 ? 12 
HELX_P HELX_P110 AM2 ARG B 1015 ? GLY B 1019 ? ARG B 1013 GLY B 1017 5 ? 5  
HELX_P HELX_P111 AM3 TYR B 1029 ? VAL B 1034 ? TYR B 1027 VAL B 1032 5 ? 6  
HELX_P HELX_P112 AM4 ASP B 1049 ? GLY B 1063 ? ASP B 1047 GLY B 1061 1 ? 15 
HELX_P HELX_P113 AM5 ALA B 1064 ? SER B 1078 ? ALA B 1062 SER B 1076 1 ? 15 
HELX_P HELX_P114 AM6 THR B 1110 ? THR B 1124 ? THR B 1108 THR B 1122 1 ? 15 
HELX_P HELX_P115 AM7 ALA B 1133 ? GLY B 1135 ? ALA B 1131 GLY B 1133 5 ? 3  
HELX_P HELX_P116 AM8 LEU B 1136 ? LYS B 1141 ? LEU B 1134 LYS B 1139 5 ? 6  
HELX_P HELX_P117 AM9 PRO B 1144 ? LEU B 1149 ? PRO B 1142 LEU B 1147 1 ? 6  
HELX_P HELX_P118 AN1 ASP B 1156 ? GLY B 1161 ? ASP B 1154 GLY B 1159 1 ? 6  
HELX_P HELX_P119 AN2 ASP B 1171 ? ALA B 1184 ? ASP B 1169 ALA B 1182 1 ? 14 
HELX_P HELX_P120 AN3 SER B 1196 ? ASN B 1203 ? SER B 1194 ASN B 1201 1 ? 8  
HELX_P HELX_P121 AN4 CYS B 1208 ? TRP B 1211 ? CYS B 1206 TRP B 1209 5 ? 4  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLY 1021 A . ? GLY 1019 A PRO 1022 A ? PRO 1020 A 1 -1.65 
2 GLY 1161 A . ? GLY 1159 A PRO 1162 A ? PRO 1160 A 1 0.45  
3 GLY 1021 B . ? GLY 1019 B PRO 1022 B ? PRO 1020 B 1 -2.41 
4 GLY 1161 B . ? GLY 1159 B PRO 1162 B ? PRO 1160 B 1 4.71  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 9  ? 
AA2 ? 3  ? 
AA3 ? 2  ? 
AA4 ? 5  ? 
AA5 ? 10 ? 
AA6 ? 5  ? 
AA7 ? 9  ? 
AA8 ? 3  ? 
AA9 ? 2  ? 
AB1 ? 5  ? 
AB2 ? 10 ? 
AB3 ? 5  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA1 2 3  ? parallel      
AA1 3 4  ? parallel      
AA1 4 5  ? parallel      
AA1 5 6  ? parallel      
AA1 6 7  ? parallel      
AA1 7 8  ? parallel      
AA1 8 9  ? parallel      
AA2 1 2  ? parallel      
AA2 2 3  ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA4 1 2  ? parallel      
AA4 2 3  ? parallel      
AA4 3 4  ? parallel      
AA4 4 5  ? parallel      
AA5 1 2  ? anti-parallel 
AA5 2 3  ? parallel      
AA5 3 4  ? parallel      
AA5 4 5  ? parallel      
AA5 5 6  ? parallel      
AA5 6 7  ? parallel      
AA5 7 8  ? parallel      
AA5 8 9  ? anti-parallel 
AA5 9 10 ? anti-parallel 
AA6 1 2  ? parallel      
AA6 2 3  ? parallel      
AA6 3 4  ? parallel      
AA6 4 5  ? parallel      
AA7 1 2  ? parallel      
AA7 2 3  ? parallel      
AA7 3 4  ? parallel      
AA7 4 5  ? parallel      
AA7 5 6  ? parallel      
AA7 6 7  ? parallel      
AA7 7 8  ? parallel      
AA7 8 9  ? parallel      
AA8 1 2  ? parallel      
AA8 2 3  ? anti-parallel 
AA9 1 2  ? anti-parallel 
AB1 1 2  ? parallel      
AB1 2 3  ? parallel      
AB1 3 4  ? parallel      
AB1 4 5  ? parallel      
AB2 1 2  ? anti-parallel 
AB2 2 3  ? parallel      
AB2 3 4  ? parallel      
AB2 4 5  ? parallel      
AB2 5 6  ? parallel      
AB2 6 7  ? parallel      
AB2 7 8  ? parallel      
AB2 8 9  ? anti-parallel 
AB2 9 10 ? anti-parallel 
AB3 1 2  ? parallel      
AB3 2 3  ? parallel      
AB3 3 4  ? parallel      
AB3 4 5  ? 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  PHE A 218  ? ASP A 223  ? PHE A 216  ASP A 221  
AA1 2  GLY A 263  ? ILE A 266  ? GLY A 261  ILE A 264  
AA1 3  LEU A 305  ? ILE A 307  ? LEU A 303  ILE A 305  
AA1 4  MET A 337  ? GLN A 342  ? MET A 335  GLN A 340  
AA1 5  ILE A 366  ? VAL A 371  ? ILE A 364  VAL A 369  
AA1 6  VAL A 418  ? ALA A 423  ? VAL A 416  ALA A 421  
AA1 7  GLU A 447  ? LEU A 451  ? GLU A 445  LEU A 449  
AA1 8  CYS A 472  ? PRO A 477  ? CYS A 470  PRO A 475  
AA1 9  PHE A 218  ? ASP A 223  ? PHE A 216  ASP A 221  
AA2 1  TRP A 576  ? ALA A 578  ? TRP A 574  ALA A 576  
AA2 2  ASP A 599  ? THR A 608  ? ASP A 597  THR A 606  
AA2 3  THR A 591  ? ASN A 596  ? THR A 589  ASN A 594  
AA3 1  GLN A 581  ? LEU A 582  ? GLN A 579  LEU A 580  
AA3 2  GLY A 585  ? PRO A 586  ? GLY A 583  PRO A 584  
AA4 1  LEU A 758  ? LEU A 760  ? LEU A 756  LEU A 758  
AA4 2  VAL A 729  ? LYS A 732  ? VAL A 727  LYS A 730  
AA4 3  ILE A 702  ? ILE A 705  ? ILE A 700  ILE A 703  
AA4 4  GLY A 779  ? THR A 783  ? GLY A 777  THR A 781  
AA4 5  LEU A 809  ? GLU A 812  ? LEU A 807  GLU A 810  
AA5 1  VAL A 911  ? GLN A 913  ? VAL A 909  GLN A 911  
AA5 2  THR A 929  ? GLU A 932  ? THR A 927  GLU A 930  
AA5 3  VAL A 947  ? TYR A 953  ? VAL A 945  TYR A 951  
AA5 4  LEU A 849  ? GLN A 855  ? LEU A 847  GLN A 853  
AA5 5  ASN A 817  ? VAL A 821  ? ASN A 815  VAL A 819  
AA5 6  THR A 973  ? HIS A 977  ? THR A 971  HIS A 975  
AA5 7  ASN A 995  ? ILE A 998  ? ASN A 993  ILE A 996  
AA5 8  VAL A 1213 ? ASN A 1221 ? VAL A 1211 ASN A 1219 
AA5 9  GLU A 1092 ? ALA A 1100 ? GLU A 1090 ALA A 1098 
AA5 10 ASP A 1083 ? LEU A 1086 ? ASP A 1081 LEU A 1084 
AA6 1  VAL A 1151 ? SER A 1154 ? VAL A 1149 SER A 1152 
AA6 2  SER A 1127 ? ASP A 1131 ? SER A 1125 ASP A 1129 
AA6 3  ARG A 1103 ? VAL A 1107 ? ARG A 1101 VAL A 1105 
AA6 4  ALA A 1166 ? GLU A 1169 ? ALA A 1164 GLU A 1167 
AA6 5  VAL A 1192 ? ALA A 1195 ? VAL A 1190 ALA A 1193 
AA7 1  SER B 219  ? ASP B 223  ? SER B 217  ASP B 221  
AA7 2  GLY B 263  ? ILE B 266  ? GLY B 261  ILE B 264  
AA7 3  LEU B 305  ? ILE B 307  ? LEU B 303  ILE B 305  
AA7 4  MET B 337  ? GLN B 342  ? MET B 335  GLN B 340  
AA7 5  ILE B 366  ? VAL B 371  ? ILE B 364  VAL B 369  
AA7 6  VAL B 418  ? ALA B 423  ? VAL B 416  ALA B 421  
AA7 7  GLU B 447  ? LEU B 451  ? GLU B 445  LEU B 449  
AA7 8  CYS B 472  ? PRO B 477  ? CYS B 470  PRO B 475  
AA7 9  SER B 219  ? ASP B 223  ? SER B 217  ASP B 221  
AA8 1  TRP B 576  ? ALA B 578  ? TRP B 574  ALA B 576  
AA8 2  ASP B 599  ? GLU B 609  ? ASP B 597  GLU B 607  
AA8 3  GLU B 590  ? ASN B 596  ? GLU B 588  ASN B 594  
AA9 1  GLN B 581  ? LEU B 582  ? GLN B 579  LEU B 580  
AA9 2  GLY B 585  ? PRO B 586  ? GLY B 583  PRO B 584  
AB1 1  LEU B 758  ? LEU B 760  ? LEU B 756  LEU B 758  
AB1 2  VAL B 729  ? LYS B 732  ? VAL B 727  LYS B 730  
AB1 3  ILE B 702  ? ILE B 705  ? ILE B 700  ILE B 703  
AB1 4  GLY B 779  ? THR B 783  ? GLY B 777  THR B 781  
AB1 5  LEU B 809  ? GLU B 812  ? LEU B 807  GLU B 810  
AB2 1  VAL B 911  ? GLN B 913  ? VAL B 909  GLN B 911  
AB2 2  THR B 929  ? GLU B 932  ? THR B 927  GLU B 930  
AB2 3  VAL B 947  ? TYR B 953  ? VAL B 945  TYR B 951  
AB2 4  LEU B 849  ? GLN B 855  ? LEU B 847  GLN B 853  
AB2 5  ASN B 817  ? VAL B 821  ? ASN B 815  VAL B 819  
AB2 6  THR B 973  ? HIS B 977  ? THR B 971  HIS B 975  
AB2 7  ASN B 995  ? ILE B 998  ? ASN B 993  ILE B 996  
AB2 8  VAL B 1213 ? ASN B 1221 ? VAL B 1211 ASN B 1219 
AB2 9  GLU B 1092 ? ALA B 1100 ? GLU B 1090 ALA B 1098 
AB2 10 ASP B 1083 ? LEU B 1086 ? ASP B 1081 LEU B 1084 
AB3 1  VAL B 1151 ? SER B 1154 ? VAL B 1149 SER B 1152 
AB3 2  SER B 1127 ? ASP B 1131 ? SER B 1125 ASP B 1129 
AB3 3  ARG B 1103 ? VAL B 1107 ? ARG B 1101 VAL B 1105 
AB3 4  ALA B 1166 ? GLU B 1169 ? ALA B 1164 GLU B 1167 
AB3 5  VAL B 1192 ? ALA B 1195 ? VAL B 1190 ALA B 1193 
# 
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  N TYR A 222  ? N TYR A 220  O SER A 265  ? O SER A 263  
AA1 2 3  N ILE A 266  ? N ILE A 264  O ASN A 306  ? O ASN A 304  
AA1 3 4  N LEU A 305  ? N LEU A 303  O GLY A 338  ? O GLY A 336  
AA1 4 5  N PHE A 339  ? N PHE A 337  O MET A 367  ? O MET A 365  
AA1 5 6  N ILE A 366  ? N ILE A 364  O PHE A 419  ? O PHE A 417  
AA1 6 7  N PHE A 422  ? N PHE A 420  O GLU A 447  ? O GLU A 445  
AA1 7 8  N CYS A 450  ? N CYS A 448  O TYR A 475  ? O TYR A 473  
AA1 8 9  O ILE A 474  ? O ILE A 472  N SER A 219  ? N SER A 217  
AA2 1 2  N ALA A 578  ? N ALA A 576  O THR A 608  ? O THR A 606  
AA2 2 3  O GLY A 605  ? O GLY A 603  N VAL A 594  ? N VAL A 592  
AA3 1 2  N LEU A 582  ? N LEU A 580  O GLY A 585  ? O GLY A 583  
AA4 1 2  O GLN A 759  ? O GLN A 757  N ALA A 731  ? N ALA A 729  
AA4 2 3  O LYS A 732  ? O LYS A 730  N CYS A 704  ? N CYS A 702  
AA4 3 4  N ILE A 705  ? N ILE A 703  O MET A 781  ? O MET A 779  
AA4 4 5  N PHE A 782  ? N PHE A 780  O ILE A 810  ? O ILE A 808  
AA5 1 2  N GLU A 912  ? N GLU A 910  O ILE A 930  ? O ILE A 928  
AA5 2 3  N ILE A 931  ? N ILE A 929  O LEU A 948  ? O LEU A 946  
AA5 3 4  O HIS A 949  ? O HIS A 947  N LEU A 852  ? N LEU A 850  
AA5 4 5  O CYS A 853  ? O CYS A 851  N MET A 819  ? N MET A 817  
AA5 5 6  N ILE A 820  ? N ILE A 818  O HIS A 977  ? O HIS A 975  
AA5 6 7  N LEU A 976  ? N LEU A 974  O TYR A 997  ? O TYR A 995  
AA5 7 8  N LEU A 996  ? N LEU A 994  O SER A 1217 ? O SER A 1215 
AA5 8 9  O GLU A 1214 ? O GLU A 1212 N HIS A 1099 ? N HIS A 1097 
AA5 9 10 O ASN A 1094 ? O ASN A 1092 N LEU A 1086 ? N LEU A 1084 
AA6 1 2  O SER A 1152 ? O SER A 1150 N ILE A 1130 ? N ILE A 1128 
AA6 2 3  O ALA A 1129 ? O ALA A 1127 N LEU A 1106 ? N LEU A 1104 
AA6 3 4  N VAL A 1107 ? N VAL A 1105 O LEU A 1167 ? O LEU A 1165 
AA6 4 5  N VAL A 1168 ? N VAL A 1166 O GLN A 1193 ? O GLN A 1191 
AA7 1 2  N TYR B 222  ? N TYR B 220  O SER B 265  ? O SER B 263  
AA7 2 3  N ILE B 266  ? N ILE B 264  O ASN B 306  ? O ASN B 304  
AA7 3 4  N LEU B 305  ? N LEU B 303  O GLY B 338  ? O GLY B 336  
AA7 4 5  N MET B 337  ? N MET B 335  O MET B 367  ? O MET B 365  
AA7 5 6  N VAL B 368  ? N VAL B 366  O GLN B 421  ? O GLN B 419  
AA7 6 7  N PHE B 422  ? N PHE B 420  O GLU B 447  ? O GLU B 445  
AA7 7 8  N CYS B 450  ? N CYS B 448  O TYR B 475  ? O TYR B 473  
AA7 8 9  O ILE B 474  ? O ILE B 472  N SER B 219  ? N SER B 217  
AA8 1 2  N ALA B 578  ? N ALA B 576  O THR B 608  ? O THR B 606  
AA8 2 3  O GLU B 609  ? O GLU B 607  N GLU B 590  ? N GLU B 588  
AA9 1 2  N LEU B 582  ? N LEU B 580  O GLY B 585  ? O GLY B 583  
AB1 1 2  O GLN B 759  ? O GLN B 757  N ALA B 731  ? N ALA B 729  
AB1 2 3  O LEU B 730  ? O LEU B 728  N CYS B 704  ? N CYS B 702  
AB1 3 4  N ILE B 705  ? N ILE B 703  O MET B 781  ? O MET B 779  
AB1 4 5  N PHE B 782  ? N PHE B 780  O ILE B 810  ? O ILE B 808  
AB2 1 2  N GLU B 912  ? N GLU B 910  O ILE B 930  ? O ILE B 928  
AB2 2 3  N THR B 929  ? N THR B 927  O LEU B 948  ? O LEU B 946  
AB2 3 4  O HIS B 949  ? O HIS B 947  N LEU B 852  ? N LEU B 850  
AB2 4 5  O CYS B 853  ? O CYS B 851  N MET B 819  ? N MET B 817  
AB2 5 6  N ILE B 820  ? N ILE B 818  O HIS B 977  ? O HIS B 975  
AB2 6 7  N LEU B 976  ? N LEU B 974  O TYR B 997  ? O TYR B 995  
AB2 7 8  N LEU B 996  ? N LEU B 994  O SER B 1217 ? O SER B 1215 
AB2 8 9  O GLU B 1214 ? O GLU B 1212 N HIS B 1099 ? N HIS B 1097 
AB2 9 10 O ASN B 1094 ? O ASN B 1092 N LEU B 1086 ? N LEU B 1084 
AB3 1 2  O SER B 1152 ? O SER B 1150 N ILE B 1130 ? N ILE B 1128 
AB3 2 3  O ALA B 1129 ? O ALA B 1127 N LEU B 1106 ? N LEU B 1104 
AB3 3 4  N VAL B 1107 ? N VAL B 1105 O LEU B 1167 ? O LEU B 1165 
AB3 4 5  N VAL B 1168 ? N VAL B 1166 O GLN B 1193 ? O GLN B 1191 
# 
_pdbx_entry_details.entry_id                   9DL4 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   A HOH 1828 ? ? O A HOH 1943 ? ? 2.03 
2 1 OE1 A GLU 539  ? ? O A HOH 1401 ? ? 2.05 
3 1 OE1 B GLU 539  ? ? O B HOH 1401 ? ? 2.12 
4 1 O   B HOH 1886 ? ? O B HOH 2033 ? ? 2.14 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     1611 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     1984 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   1_565 
_pdbx_validate_symm_contact.dist              2.19 
# 
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 ALA A 22   ? ? -157.90 57.99   
2  1 GLU A 225  ? ? -173.38 140.63  
3  1 GLU A 308  ? ? -123.80 -133.94 
4  1 MET A 452  ? ? -164.30 -58.39  
5  1 VAL A 460  ? ? -121.00 -51.09  
6  1 LYS A 465  ? ? -115.27 -125.87 
7  1 ASP A 597  ? ? -169.59 97.06   
8  1 HIS A 694  ? ? -104.42 71.77   
9  1 ASP A 762  ? ? -92.26  -157.91 
10 1 THR A 811  ? ? -126.59 -164.83 
11 1 GLN A 814  ? ? -107.33 71.56   
12 1 LEU A 970  ? ? -97.92  -84.67  
13 1 ALA B 22   ? ? -153.68 66.44   
14 1 LYS B 124  ? ? -132.02 -33.48  
15 1 SER B 157  ? ? 78.41   -44.57  
16 1 LEU B 223  ? ? 45.60   79.30   
17 1 GLU B 308  ? ? -118.43 -133.77 
18 1 MET B 452  ? ? -152.95 -53.30  
19 1 LYS B 465  ? ? -126.88 -106.88 
20 1 PRO B 578  ? ? -67.06  96.42   
21 1 ASP B 597  ? ? -172.27 97.35   
22 1 THR B 689  ? ? -130.11 -45.28  
23 1 GLN B 814  ? ? -112.29 77.63   
24 1 GLN B 842  ? ? -95.65  35.97   
25 1 LEU B 970  ? ? -95.95  -86.57  
26 1 ASP B 1154 ? ? -155.11 86.90   
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -25.7839 66.4536 93.8907 0.2215 ? 0.0119  ? 0.0220  ? 0.1522 ? 0.0270  ? 0.1588 ? 0.9925 ? -0.0129 
? 0.2831 ? 0.1861 ? 0.0233  ? 0.3104 ? -0.0263 ? -0.1127 ? 0.0367  ? 0.0650 ? 0.0492 ? 0.0223  ? -0.0032 ? -0.0410 ? -0.0240 ? 
2 'X-RAY DIFFRACTION' ? refined 6.0519   31.4261 91.9948 0.1749 ? -0.0072 ? -0.0192 ? 0.1839 ? -0.0324 ? 0.1733 ? 0.4880 ? -0.0416 
? 0.2439 ? 0.5247 ? -0.1326 ? 0.6501 ? 0.0468  ? -0.0264 ? -0.0826 ? 0.0754 ? 0.0321 ? -0.0501 ? 0.1160  ? -0.0798 ? -0.0788 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 'chain A and peptide' 
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 'chain B and peptide' 
# 
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 SER -1   ? A SER 1    
2  1 Y 1 A MET 0    ? A MET 2    
3  1 Y 1 A MET 1    ? A MET 3    
4  1 Y 1 A SER 2    ? A SER 4    
5  1 Y 1 A PRO 3    ? A PRO 5    
6  1 Y 1 A ASN 4    ? A ASN 6    
7  1 Y 1 A PRO 5    ? A PRO 7    
8  1 Y 1 A LEU 6    ? A LEU 8    
9  1 Y 1 A GLN 7    ? A GLN 9    
10 1 Y 1 A LYS 8    ? A LYS 10   
11 1 Y 1 A PRO 9    ? A PRO 11   
12 1 Y 1 A ALA 10   ? A ALA 12   
13 1 Y 1 A ILE 11   ? A ILE 13   
14 1 Y 1 A ASP 12   ? A ASP 14   
15 1 Y 1 A ALA 13   ? A ALA 15   
16 1 Y 1 A ALA 14   ? A ALA 16   
17 1 Y 1 A HIS 79   ? A HIS 81   
18 1 Y 1 A SER 80   ? A SER 82   
19 1 Y 1 A GLY 81   ? A GLY 83   
20 1 Y 1 A SER 82   ? A SER 84   
21 1 Y 1 A GLY 135  ? A GLY 137  
22 1 Y 1 A GLY 136  ? A GLY 138  
23 1 Y 1 A GLU 492  ? A GLU 494  
24 1 Y 1 A ASN 493  ? A ASN 495  
25 1 Y 1 A SER 1228 ? A SER 1230 
26 1 Y 1 A LEU 1229 ? A LEU 1231 
27 1 Y 1 A MET 1230 ? A MET 1232 
28 1 Y 1 A ALA 1231 ? A ALA 1233 
29 1 Y 1 A ILE 1232 ? A ILE 1234 
30 1 Y 1 A GLY 1233 ? A GLY 1235 
31 1 Y 1 B SER -1   ? B SER 1    
32 1 Y 1 B MET 0    ? B MET 2    
33 1 Y 1 B MET 1    ? B MET 3    
34 1 Y 1 B SER 2    ? B SER 4    
35 1 Y 1 B PRO 3    ? B PRO 5    
36 1 Y 1 B ASN 4    ? B ASN 6    
37 1 Y 1 B PRO 5    ? B PRO 7    
38 1 Y 1 B LEU 6    ? B LEU 8    
39 1 Y 1 B GLN 7    ? B GLN 9    
40 1 Y 1 B LYS 8    ? B LYS 10   
41 1 Y 1 B PRO 9    ? B PRO 11   
42 1 Y 1 B ALA 10   ? B ALA 12   
43 1 Y 1 B ILE 11   ? B ILE 13   
44 1 Y 1 B ASP 12   ? B ASP 14   
45 1 Y 1 B ALA 13   ? B ALA 15   
46 1 Y 1 B ALA 14   ? B ALA 16   
47 1 Y 1 B HIS 79   ? B HIS 81   
48 1 Y 1 B SER 80   ? B SER 82   
49 1 Y 1 B GLY 81   ? B GLY 83   
50 1 Y 1 B SER 82   ? B SER 84   
51 1 Y 1 B GLY 135  ? B GLY 137  
52 1 Y 1 B GLY 136  ? B GLY 138  
53 1 Y 1 B SER 137  ? B SER 139  
54 1 Y 1 B GLU 492  ? B GLU 494  
55 1 Y 1 B ASN 493  ? B ASN 495  
56 1 Y 1 B ALA 1223 ? B ALA 1225 
57 1 Y 1 B GLY 1224 ? B GLY 1226 
58 1 Y 1 B GLY 1225 ? B GLY 1227 
59 1 Y 1 B ASN 1226 ? B ASN 1228 
60 1 Y 1 B ALA 1227 ? B ALA 1229 
61 1 Y 1 B SER 1228 ? B SER 1230 
62 1 Y 1 B LEU 1229 ? B LEU 1231 
63 1 Y 1 B MET 1230 ? B MET 1232 
64 1 Y 1 B ALA 1231 ? B ALA 1233 
65 1 Y 1 B ILE 1232 ? B ILE 1234 
66 1 Y 1 B GLY 1233 ? B GLY 1235 
# 
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  
CYS N      N N N 74  
CYS CA     C N R 75  
CYS C      C N N 76  
CYS O      O N N 77  
CYS CB     C N N 78  
CYS SG     S N N 79  
CYS OXT    O N N 80  
CYS H      H N N 81  
CYS H2     H N N 82  
CYS HA     H N N 83  
CYS HB2    H N N 84  
CYS HB3    H N N 85  
CYS HG     H N N 86  
CYS HXT    H N N 87  
FAD PA     P N R 88  
FAD O1A    O N N 89  
FAD O2A    O N N 90  
FAD O5B    O N N 91  
FAD C5B    C N N 92  
FAD C4B    C N R 93  
FAD O4B    O N N 94  
FAD C3B    C N S 95  
FAD O3B    O N N 96  
FAD C2B    C N R 97  
FAD O2B    O N N 98  
FAD C1B    C N R 99  
FAD N9A    N Y N 100 
FAD C8A    C Y N 101 
FAD N7A    N Y N 102 
FAD C5A    C Y N 103 
FAD C6A    C Y N 104 
FAD N6A    N N N 105 
FAD N1A    N Y N 106 
FAD C2A    C Y N 107 
FAD N3A    N Y N 108 
FAD C4A    C Y N 109 
FAD N1     N N N 110 
FAD C2     C N N 111 
FAD O2     O N N 112 
FAD N3     N N N 113 
FAD C4     C N N 114 
FAD O4     O N N 115 
FAD C4X    C N N 116 
FAD N5     N N N 117 
FAD C5X    C Y N 118 
FAD C6     C Y N 119 
FAD C7     C Y N 120 
FAD C7M    C N N 121 
FAD C8     C Y N 122 
FAD C8M    C N N 123 
FAD C9     C Y N 124 
FAD C9A    C Y N 125 
FAD N10    N N N 126 
FAD C10    C N N 127 
FAD "C1'"  C N N 128 
FAD "C2'"  C N S 129 
FAD "O2'"  O N N 130 
FAD "C3'"  C N S 131 
FAD "O3'"  O N N 132 
FAD "C4'"  C N R 133 
FAD "O4'"  O N N 134 
FAD "C5'"  C N N 135 
FAD "O5'"  O N N 136 
FAD P      P N R 137 
FAD O1P    O N N 138 
FAD O2P    O N N 139 
FAD O3P    O N N 140 
FAD HOA2   H N N 141 
FAD H51A   H N N 142 
FAD H52A   H N N 143 
FAD H4B    H N N 144 
FAD H3B    H N N 145 
FAD HO3A   H N N 146 
FAD H2B    H N N 147 
FAD HO2A   H N N 148 
FAD H1B    H N N 149 
FAD H8A    H N N 150 
FAD H61A   H N N 151 
FAD H62A   H N N 152 
FAD H2A    H N N 153 
FAD HN3    H N N 154 
FAD H6     H N N 155 
FAD HM71   H N N 156 
FAD HM72   H N N 157 
FAD HM73   H N N 158 
FAD HM81   H N N 159 
FAD HM82   H N N 160 
FAD HM83   H N N 161 
FAD H9     H N N 162 
FAD "H1'1" H N N 163 
FAD "H1'2" H N N 164 
FAD "H2'"  H N N 165 
FAD "HO2'" H N N 166 
FAD "H3'"  H N N 167 
FAD "HO3'" H N N 168 
FAD "H4'"  H N N 169 
FAD "HO4'" H N N 170 
FAD "H5'1" H N N 171 
FAD "H5'2" H N N 172 
FAD HOP2   H N N 173 
FMT C      C N N 174 
FMT O1     O N N 175 
FMT O2     O N N 176 
FMT H      H N N 177 
FMT HO2    H N N 178 
GLN N      N N N 179 
GLN CA     C N S 180 
GLN C      C N N 181 
GLN O      O N N 182 
GLN CB     C N N 183 
GLN CG     C N N 184 
GLN CD     C N N 185 
GLN OE1    O N N 186 
GLN NE2    N N N 187 
GLN OXT    O N N 188 
GLN H      H N N 189 
GLN H2     H N N 190 
GLN HA     H N N 191 
GLN HB2    H N N 192 
GLN HB3    H N N 193 
GLN HG2    H N N 194 
GLN HG3    H N N 195 
GLN HE21   H N N 196 
GLN HE22   H N N 197 
GLN HXT    H N N 198 
GLU N      N N N 199 
GLU CA     C N S 200 
GLU C      C N N 201 
GLU O      O N N 202 
GLU CB     C N N 203 
GLU CG     C N N 204 
GLU CD     C N N 205 
GLU OE1    O N N 206 
GLU OE2    O N N 207 
GLU OXT    O N N 208 
GLU H      H N N 209 
GLU H2     H N N 210 
GLU HA     H N N 211 
GLU HB2    H N N 212 
GLU HB3    H N N 213 
GLU HG2    H N N 214 
GLU HG3    H N N 215 
GLU HE2    H N N 216 
GLU HXT    H N N 217 
GLY N      N N N 218 
GLY CA     C N N 219 
GLY C      C N N 220 
GLY O      O N N 221 
GLY OXT    O N N 222 
GLY H      H N N 223 
GLY H2     H N N 224 
GLY HA2    H N N 225 
GLY HA3    H N N 226 
GLY HXT    H N N 227 
HIS N      N N N 228 
HIS CA     C N S 229 
HIS C      C N N 230 
HIS O      O N N 231 
HIS CB     C N N 232 
HIS CG     C Y N 233 
HIS ND1    N Y N 234 
HIS CD2    C Y N 235 
HIS CE1    C Y N 236 
HIS NE2    N Y N 237 
HIS OXT    O N N 238 
HIS H      H N N 239 
HIS H2     H N N 240 
HIS HA     H N N 241 
HIS HB2    H N N 242 
HIS HB3    H N N 243 
HIS HD1    H N N 244 
HIS HD2    H N N 245 
HIS HE1    H N N 246 
HIS HE2    H N N 247 
HIS HXT    H N N 248 
HOH O      O N N 249 
HOH H1     H N N 250 
HOH H2     H N N 251 
ILE N      N N N 252 
ILE CA     C N S 253 
ILE C      C N N 254 
ILE O      O N N 255 
ILE CB     C N S 256 
ILE CG1    C N N 257 
ILE CG2    C N N 258 
ILE CD1    C N N 259 
ILE OXT    O N N 260 
ILE H      H N N 261 
ILE H2     H N N 262 
ILE HA     H N N 263 
ILE HB     H N N 264 
ILE HG12   H N N 265 
ILE HG13   H N N 266 
ILE HG21   H N N 267 
ILE HG22   H N N 268 
ILE HG23   H N N 269 
ILE HD11   H N N 270 
ILE HD12   H N N 271 
ILE HD13   H N N 272 
ILE HXT    H N N 273 
LEU N      N N N 274 
LEU CA     C N S 275 
LEU C      C N N 276 
LEU O      O N N 277 
LEU CB     C N N 278 
LEU CG     C N N 279 
LEU CD1    C N N 280 
LEU CD2    C N N 281 
LEU OXT    O N N 282 
LEU H      H N N 283 
LEU H2     H N N 284 
LEU HA     H N N 285 
LEU HB2    H N N 286 
LEU HB3    H N N 287 
LEU HG     H N N 288 
LEU HD11   H N N 289 
LEU HD12   H N N 290 
LEU HD13   H N N 291 
LEU HD21   H N N 292 
LEU HD22   H N N 293 
LEU HD23   H N N 294 
LEU HXT    H N N 295 
LYS N      N N N 296 
LYS CA     C N S 297 
LYS C      C N N 298 
LYS O      O N N 299 
LYS CB     C N N 300 
LYS CG     C N N 301 
LYS CD     C N N 302 
LYS CE     C N N 303 
LYS NZ     N N N 304 
LYS OXT    O N N 305 
LYS H      H N N 306 
LYS H2     H N N 307 
LYS HA     H N N 308 
LYS HB2    H N N 309 
LYS HB3    H N N 310 
LYS HG2    H N N 311 
LYS HG3    H N N 312 
LYS HD2    H N N 313 
LYS HD3    H N N 314 
LYS HE2    H N N 315 
LYS HE3    H N N 316 
LYS HZ1    H N N 317 
LYS HZ2    H N N 318 
LYS HZ3    H N N 319 
LYS HXT    H N N 320 
MET N      N N N 321 
MET CA     C N S 322 
MET C      C N N 323 
MET O      O N N 324 
MET CB     C N N 325 
MET CG     C N N 326 
MET SD     S N N 327 
MET CE     C N N 328 
MET OXT    O N N 329 
MET H      H N N 330 
MET H2     H N N 331 
MET HA     H N N 332 
MET HB2    H N N 333 
MET HB3    H N N 334 
MET HG2    H N N 335 
MET HG3    H N N 336 
MET HE1    H N N 337 
MET HE2    H N N 338 
MET HE3    H N N 339 
MET HXT    H N N 340 
PEG C1     C N N 341 
PEG O1     O N N 342 
PEG C2     C N N 343 
PEG O2     O N N 344 
PEG C3     C N N 345 
PEG C4     C N N 346 
PEG O4     O N N 347 
PEG H11    H N N 348 
PEG H12    H N N 349 
PEG HO1    H N N 350 
PEG H21    H N N 351 
PEG H22    H N N 352 
PEG H31    H N N 353 
PEG H32    H N N 354 
PEG H41    H N N 355 
PEG H42    H N N 356 
PEG HO4    H N N 357 
PGE C1     C N N 358 
PGE O1     O N N 359 
PGE C2     C N N 360 
PGE O2     O N N 361 
PGE C3     C N N 362 
PGE C4     C N N 363 
PGE O4     O N N 364 
PGE C6     C N N 365 
PGE C5     C N N 366 
PGE O3     O N N 367 
PGE H1     H N N 368 
PGE H12    H N N 369 
PGE HO1    H N N 370 
PGE H2     H N N 371 
PGE H22    H N N 372 
PGE H3     H N N 373 
PGE H32    H N N 374 
PGE H4     H N N 375 
PGE H42    H N N 376 
PGE HO4    H N N 377 
PGE H6     H N N 378 
PGE H62    H N N 379 
PGE H5     H N N 380 
PGE H52    H N N 381 
PHE N      N N N 382 
PHE CA     C N S 383 
PHE C      C N N 384 
PHE O      O N N 385 
PHE CB     C N N 386 
PHE CG     C Y N 387 
PHE CD1    C Y N 388 
PHE CD2    C Y N 389 
PHE CE1    C Y N 390 
PHE CE2    C Y N 391 
PHE CZ     C Y N 392 
PHE OXT    O N N 393 
PHE H      H N N 394 
PHE H2     H N N 395 
PHE HA     H N N 396 
PHE HB2    H N N 397 
PHE HB3    H N N 398 
PHE HD1    H N N 399 
PHE HD2    H N N 400 
PHE HE1    H N N 401 
PHE HE2    H N N 402 
PHE HZ     H N N 403 
PHE HXT    H N N 404 
PRO N      N N N 405 
PRO CA     C N S 406 
PRO C      C N N 407 
PRO O      O N N 408 
PRO CB     C N N 409 
PRO CG     C N N 410 
PRO CD     C N N 411 
PRO OXT    O N N 412 
PRO H      H N N 413 
PRO HA     H N N 414 
PRO HB2    H N N 415 
PRO HB3    H N N 416 
PRO HG2    H N N 417 
PRO HG3    H N N 418 
PRO HD2    H N N 419 
PRO HD3    H N N 420 
PRO HXT    H N N 421 
PYS N1     N Y N 422 
PYS C2     C Y N 423 
PYS C3     C Y N 424 
PYS C4     C Y N 425 
PYS C5     C Y N 426 
PYS C6     C Y N 427 
PYS S2     S N N 428 
PYS H3     H N N 429 
PYS H4     H N N 430 
PYS H5     H N N 431 
PYS H6     H N N 432 
PYS HS2    H N N 433 
SER N      N N N 434 
SER CA     C N S 435 
SER C      C N N 436 
SER O      O N N 437 
SER CB     C N N 438 
SER OG     O N N 439 
SER OXT    O N N 440 
SER H      H N N 441 
SER H2     H N N 442 
SER HA     H N N 443 
SER HB2    H N N 444 
SER HB3    H N N 445 
SER HG     H N N 446 
SER HXT    H N N 447 
SO4 S      S N N 448 
SO4 O1     O N N 449 
SO4 O2     O N N 450 
SO4 O3     O N N 451 
SO4 O4     O N N 452 
THR N      N N N 453 
THR CA     C N S 454 
THR C      C N N 455 
THR O      O N N 456 
THR CB     C N R 457 
THR OG1    O N N 458 
THR CG2    C N N 459 
THR OXT    O N N 460 
THR H      H N N 461 
THR H2     H N N 462 
THR HA     H N N 463 
THR HB     H N N 464 
THR HG1    H N N 465 
THR HG21   H N N 466 
THR HG22   H N N 467 
THR HG23   H N N 468 
THR HXT    H N N 469 
TRP N      N N N 470 
TRP CA     C N S 471 
TRP C      C N N 472 
TRP O      O N N 473 
TRP CB     C N N 474 
TRP CG     C Y N 475 
TRP CD1    C Y N 476 
TRP CD2    C Y N 477 
TRP NE1    N Y N 478 
TRP CE2    C Y N 479 
TRP CE3    C Y N 480 
TRP CZ2    C Y N 481 
TRP CZ3    C Y N 482 
TRP CH2    C Y N 483 
TRP OXT    O N N 484 
TRP H      H N N 485 
TRP H2     H N N 486 
TRP HA     H N N 487 
TRP HB2    H N N 488 
TRP HB3    H N N 489 
TRP HD1    H N N 490 
TRP HE1    H N N 491 
TRP HE3    H N N 492 
TRP HZ2    H N N 493 
TRP HZ3    H N N 494 
TRP HH2    H N N 495 
TRP HXT    H N N 496 
TYR N      N N N 497 
TYR CA     C N S 498 
TYR C      C N N 499 
TYR O      O N N 500 
TYR CB     C N N 501 
TYR CG     C Y N 502 
TYR CD1    C Y N 503 
TYR CD2    C Y N 504 
TYR CE1    C Y N 505 
TYR CE2    C Y N 506 
TYR CZ     C Y N 507 
TYR OH     O N N 508 
TYR OXT    O N N 509 
TYR H      H N N 510 
TYR H2     H N N 511 
TYR HA     H N N 512 
TYR HB2    H N N 513 
TYR HB3    H N N 514 
TYR HD1    H N N 515 
TYR HD2    H N N 516 
TYR HE1    H N N 517 
TYR HE2    H N N 518 
TYR HH     H N N 519 
TYR HXT    H N N 520 
VAL N      N N N 521 
VAL CA     C N S 522 
VAL C      C N N 523 
VAL O      O N N 524 
VAL CB     C N N 525 
VAL CG1    C N N 526 
VAL CG2    C N N 527 
VAL OXT    O N N 528 
VAL H      H N N 529 
VAL H2     H N N 530 
VAL HA     H N N 531 
VAL HB     H N N 532 
VAL HG11   H N N 533 
VAL HG12   H N N 534 
VAL HG13   H N N 535 
VAL HG21   H N N 536 
VAL HG22   H N N 537 
VAL HG23   H N N 538 
VAL HXT    H N N 539 
# 
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  
FAD PA    O1A    doub N N 83  
FAD PA    O2A    sing N N 84  
FAD PA    O5B    sing N N 85  
FAD PA    O3P    sing N N 86  
FAD O2A   HOA2   sing N N 87  
FAD O5B   C5B    sing N N 88  
FAD C5B   C4B    sing N N 89  
FAD C5B   H51A   sing N N 90  
FAD C5B   H52A   sing N N 91  
FAD C4B   O4B    sing N N 92  
FAD C4B   C3B    sing N N 93  
FAD C4B   H4B    sing N N 94  
FAD O4B   C1B    sing N N 95  
FAD C3B   O3B    sing N N 96  
FAD C3B   C2B    sing N N 97  
FAD C3B   H3B    sing N N 98  
FAD O3B   HO3A   sing N N 99  
FAD C2B   O2B    sing N N 100 
FAD C2B   C1B    sing N N 101 
FAD C2B   H2B    sing N N 102 
FAD O2B   HO2A   sing N N 103 
FAD C1B   N9A    sing N N 104 
FAD C1B   H1B    sing N N 105 
FAD N9A   C8A    sing Y N 106 
FAD N9A   C4A    sing Y N 107 
FAD C8A   N7A    doub Y N 108 
FAD C8A   H8A    sing N N 109 
FAD N7A   C5A    sing Y N 110 
FAD C5A   C6A    sing Y N 111 
FAD C5A   C4A    doub Y N 112 
FAD C6A   N6A    sing N N 113 
FAD C6A   N1A    doub Y N 114 
FAD N6A   H61A   sing N N 115 
FAD N6A   H62A   sing N N 116 
FAD N1A   C2A    sing Y N 117 
FAD C2A   N3A    doub Y N 118 
FAD C2A   H2A    sing N N 119 
FAD N3A   C4A    sing Y N 120 
FAD N1    C2     sing N N 121 
FAD N1    C10    doub N N 122 
FAD C2    O2     doub N N 123 
FAD C2    N3     sing N N 124 
FAD N3    C4     sing N N 125 
FAD N3    HN3    sing N N 126 
FAD C4    O4     doub N N 127 
FAD C4    C4X    sing N N 128 
FAD C4X   N5     doub N N 129 
FAD C4X   C10    sing N N 130 
FAD N5    C5X    sing N N 131 
FAD C5X   C6     doub Y N 132 
FAD C5X   C9A    sing Y N 133 
FAD C6    C7     sing Y N 134 
FAD C6    H6     sing N N 135 
FAD C7    C7M    sing N N 136 
FAD C7    C8     doub Y N 137 
FAD C7M   HM71   sing N N 138 
FAD C7M   HM72   sing N N 139 
FAD C7M   HM73   sing N N 140 
FAD C8    C8M    sing N N 141 
FAD C8    C9     sing Y N 142 
FAD C8M   HM81   sing N N 143 
FAD C8M   HM82   sing N N 144 
FAD C8M   HM83   sing N N 145 
FAD C9    C9A    doub Y N 146 
FAD C9    H9     sing N N 147 
FAD C9A   N10    sing N N 148 
FAD N10   C10    sing N N 149 
FAD N10   "C1'"  sing N N 150 
FAD "C1'" "C2'"  sing N N 151 
FAD "C1'" "H1'1" sing N N 152 
FAD "C1'" "H1'2" sing N N 153 
FAD "C2'" "O2'"  sing N N 154 
FAD "C2'" "C3'"  sing N N 155 
FAD "C2'" "H2'"  sing N N 156 
FAD "O2'" "HO2'" sing N N 157 
FAD "C3'" "O3'"  sing N N 158 
FAD "C3'" "C4'"  sing N N 159 
FAD "C3'" "H3'"  sing N N 160 
FAD "O3'" "HO3'" sing N N 161 
FAD "C4'" "O4'"  sing N N 162 
FAD "C4'" "C5'"  sing N N 163 
FAD "C4'" "H4'"  sing N N 164 
FAD "O4'" "HO4'" sing N N 165 
FAD "C5'" "O5'"  sing N N 166 
FAD "C5'" "H5'1" sing N N 167 
FAD "C5'" "H5'2" sing N N 168 
FAD "O5'" P      sing N N 169 
FAD P     O1P    doub N N 170 
FAD P     O2P    sing N N 171 
FAD P     O3P    sing N N 172 
FAD O2P   HOP2   sing N N 173 
FMT C     O1     doub N N 174 
FMT C     O2     sing N N 175 
FMT C     H      sing N N 176 
FMT O2    HO2    sing N N 177 
GLN N     CA     sing N N 178 
GLN N     H      sing N N 179 
GLN N     H2     sing N N 180 
GLN CA    C      sing N N 181 
GLN CA    CB     sing N N 182 
GLN CA    HA     sing N N 183 
GLN C     O      doub N N 184 
GLN C     OXT    sing N N 185 
GLN CB    CG     sing N N 186 
GLN CB    HB2    sing N N 187 
GLN CB    HB3    sing N N 188 
GLN CG    CD     sing N N 189 
GLN CG    HG2    sing N N 190 
GLN CG    HG3    sing N N 191 
GLN CD    OE1    doub N N 192 
GLN CD    NE2    sing N N 193 
GLN NE2   HE21   sing N N 194 
GLN NE2   HE22   sing N N 195 
GLN OXT   HXT    sing N N 196 
GLU N     CA     sing N N 197 
GLU N     H      sing N N 198 
GLU N     H2     sing N N 199 
GLU CA    C      sing N N 200 
GLU CA    CB     sing N N 201 
GLU CA    HA     sing N N 202 
GLU C     O      doub N N 203 
GLU C     OXT    sing N N 204 
GLU CB    CG     sing N N 205 
GLU CB    HB2    sing N N 206 
GLU CB    HB3    sing N N 207 
GLU CG    CD     sing N N 208 
GLU CG    HG2    sing N N 209 
GLU CG    HG3    sing N N 210 
GLU CD    OE1    doub N N 211 
GLU CD    OE2    sing N N 212 
GLU OE2   HE2    sing N N 213 
GLU OXT   HXT    sing N N 214 
GLY N     CA     sing N N 215 
GLY N     H      sing N N 216 
GLY N     H2     sing N N 217 
GLY CA    C      sing N N 218 
GLY CA    HA2    sing N N 219 
GLY CA    HA3    sing N N 220 
GLY C     O      doub N N 221 
GLY C     OXT    sing N N 222 
GLY OXT   HXT    sing N N 223 
HIS N     CA     sing N N 224 
HIS N     H      sing N N 225 
HIS N     H2     sing N N 226 
HIS CA    C      sing N N 227 
HIS CA    CB     sing N N 228 
HIS CA    HA     sing N N 229 
HIS C     O      doub N N 230 
HIS C     OXT    sing N N 231 
HIS CB    CG     sing N N 232 
HIS CB    HB2    sing N N 233 
HIS CB    HB3    sing N N 234 
HIS CG    ND1    sing Y N 235 
HIS CG    CD2    doub Y N 236 
HIS ND1   CE1    doub Y N 237 
HIS ND1   HD1    sing N N 238 
HIS CD2   NE2    sing Y N 239 
HIS CD2   HD2    sing N N 240 
HIS CE1   NE2    sing Y N 241 
HIS CE1   HE1    sing N N 242 
HIS NE2   HE2    sing N N 243 
HIS OXT   HXT    sing N N 244 
HOH O     H1     sing N N 245 
HOH O     H2     sing N N 246 
ILE N     CA     sing N N 247 
ILE N     H      sing N N 248 
ILE N     H2     sing N N 249 
ILE CA    C      sing N N 250 
ILE CA    CB     sing N N 251 
ILE CA    HA     sing N N 252 
ILE C     O      doub N N 253 
ILE C     OXT    sing N N 254 
ILE CB    CG1    sing N N 255 
ILE CB    CG2    sing N N 256 
ILE CB    HB     sing N N 257 
ILE CG1   CD1    sing N N 258 
ILE CG1   HG12   sing N N 259 
ILE CG1   HG13   sing N N 260 
ILE CG2   HG21   sing N N 261 
ILE CG2   HG22   sing N N 262 
ILE CG2   HG23   sing N N 263 
ILE CD1   HD11   sing N N 264 
ILE CD1   HD12   sing N N 265 
ILE CD1   HD13   sing N N 266 
ILE OXT   HXT    sing N N 267 
LEU N     CA     sing N N 268 
LEU N     H      sing N N 269 
LEU N     H2     sing N N 270 
LEU CA    C      sing N N 271 
LEU CA    CB     sing N N 272 
LEU CA    HA     sing N N 273 
LEU C     O      doub N N 274 
LEU C     OXT    sing N N 275 
LEU CB    CG     sing N N 276 
LEU CB    HB2    sing N N 277 
LEU CB    HB3    sing N N 278 
LEU CG    CD1    sing N N 279 
LEU CG    CD2    sing N N 280 
LEU CG    HG     sing N N 281 
LEU CD1   HD11   sing N N 282 
LEU CD1   HD12   sing N N 283 
LEU CD1   HD13   sing N N 284 
LEU CD2   HD21   sing N N 285 
LEU CD2   HD22   sing N N 286 
LEU CD2   HD23   sing N N 287 
LEU OXT   HXT    sing N N 288 
LYS N     CA     sing N N 289 
LYS N     H      sing N N 290 
LYS N     H2     sing N N 291 
LYS CA    C      sing N N 292 
LYS CA    CB     sing N N 293 
LYS CA    HA     sing N N 294 
LYS C     O      doub N N 295 
LYS C     OXT    sing N N 296 
LYS CB    CG     sing N N 297 
LYS CB    HB2    sing N N 298 
LYS CB    HB3    sing N N 299 
LYS CG    CD     sing N N 300 
LYS CG    HG2    sing N N 301 
LYS CG    HG3    sing N N 302 
LYS CD    CE     sing N N 303 
LYS CD    HD2    sing N N 304 
LYS CD    HD3    sing N N 305 
LYS CE    NZ     sing N N 306 
LYS CE    HE2    sing N N 307 
LYS CE    HE3    sing N N 308 
LYS NZ    HZ1    sing N N 309 
LYS NZ    HZ2    sing N N 310 
LYS NZ    HZ3    sing N N 311 
LYS OXT   HXT    sing N N 312 
MET N     CA     sing N N 313 
MET N     H      sing N N 314 
MET N     H2     sing N N 315 
MET CA    C      sing N N 316 
MET CA    CB     sing N N 317 
MET CA    HA     sing N N 318 
MET C     O      doub N N 319 
MET C     OXT    sing N N 320 
MET CB    CG     sing N N 321 
MET CB    HB2    sing N N 322 
MET CB    HB3    sing N N 323 
MET CG    SD     sing N N 324 
MET CG    HG2    sing N N 325 
MET CG    HG3    sing N N 326 
MET SD    CE     sing N N 327 
MET CE    HE1    sing N N 328 
MET CE    HE2    sing N N 329 
MET CE    HE3    sing N N 330 
MET OXT   HXT    sing N N 331 
PEG C1    O1     sing N N 332 
PEG C1    C2     sing N N 333 
PEG C1    H11    sing N N 334 
PEG C1    H12    sing N N 335 
PEG O1    HO1    sing N N 336 
PEG C2    O2     sing N N 337 
PEG C2    H21    sing N N 338 
PEG C2    H22    sing N N 339 
PEG O2    C3     sing N N 340 
PEG C3    C4     sing N N 341 
PEG C3    H31    sing N N 342 
PEG C3    H32    sing N N 343 
PEG C4    O4     sing N N 344 
PEG C4    H41    sing N N 345 
PEG C4    H42    sing N N 346 
PEG O4    HO4    sing N N 347 
PGE C1    O1     sing N N 348 
PGE C1    C2     sing N N 349 
PGE C1    H1     sing N N 350 
PGE C1    H12    sing N N 351 
PGE O1    HO1    sing N N 352 
PGE C2    O2     sing N N 353 
PGE C2    H2     sing N N 354 
PGE C2    H22    sing N N 355 
PGE O2    C3     sing N N 356 
PGE C3    C4     sing N N 357 
PGE C3    H3     sing N N 358 
PGE C3    H32    sing N N 359 
PGE C4    O3     sing N N 360 
PGE C4    H4     sing N N 361 
PGE C4    H42    sing N N 362 
PGE O4    C6     sing N N 363 
PGE O4    HO4    sing N N 364 
PGE C6    C5     sing N N 365 
PGE C6    H6     sing N N 366 
PGE C6    H62    sing N N 367 
PGE C5    O3     sing N N 368 
PGE C5    H5     sing N N 369 
PGE C5    H52    sing N N 370 
PHE N     CA     sing N N 371 
PHE N     H      sing N N 372 
PHE N     H2     sing N N 373 
PHE CA    C      sing N N 374 
PHE CA    CB     sing N N 375 
PHE CA    HA     sing N N 376 
PHE C     O      doub N N 377 
PHE C     OXT    sing N N 378 
PHE CB    CG     sing N N 379 
PHE CB    HB2    sing N N 380 
PHE CB    HB3    sing N N 381 
PHE CG    CD1    doub Y N 382 
PHE CG    CD2    sing Y N 383 
PHE CD1   CE1    sing Y N 384 
PHE CD1   HD1    sing N N 385 
PHE CD2   CE2    doub Y N 386 
PHE CD2   HD2    sing N N 387 
PHE CE1   CZ     doub Y N 388 
PHE CE1   HE1    sing N N 389 
PHE CE2   CZ     sing Y N 390 
PHE CE2   HE2    sing N N 391 
PHE CZ    HZ     sing N N 392 
PHE OXT   HXT    sing N N 393 
PRO N     CA     sing N N 394 
PRO N     CD     sing N N 395 
PRO N     H      sing N N 396 
PRO CA    C      sing N N 397 
PRO CA    CB     sing N N 398 
PRO CA    HA     sing N N 399 
PRO C     O      doub N N 400 
PRO C     OXT    sing N N 401 
PRO CB    CG     sing N N 402 
PRO CB    HB2    sing N N 403 
PRO CB    HB3    sing N N 404 
PRO CG    CD     sing N N 405 
PRO CG    HG2    sing N N 406 
PRO CG    HG3    sing N N 407 
PRO CD    HD2    sing N N 408 
PRO CD    HD3    sing N N 409 
PRO OXT   HXT    sing N N 410 
PYS N1    C2     doub Y N 411 
PYS N1    C6     sing Y N 412 
PYS C2    C3     sing Y N 413 
PYS C2    S2     sing N N 414 
PYS C3    C4     doub Y N 415 
PYS C3    H3     sing N N 416 
PYS C4    C5     sing Y N 417 
PYS C4    H4     sing N N 418 
PYS C5    C6     doub Y N 419 
PYS C5    H5     sing N N 420 
PYS C6    H6     sing N N 421 
PYS S2    HS2    sing N N 422 
SER N     CA     sing N N 423 
SER N     H      sing N N 424 
SER N     H2     sing N N 425 
SER CA    C      sing N N 426 
SER CA    CB     sing N N 427 
SER CA    HA     sing N N 428 
SER C     O      doub N N 429 
SER C     OXT    sing N N 430 
SER CB    OG     sing N N 431 
SER CB    HB2    sing N N 432 
SER CB    HB3    sing N N 433 
SER OG    HG     sing N N 434 
SER OXT   HXT    sing N N 435 
SO4 S     O1     doub N N 436 
SO4 S     O2     doub N N 437 
SO4 S     O3     sing N N 438 
SO4 S     O4     sing N N 439 
THR N     CA     sing N N 440 
THR N     H      sing N N 441 
THR N     H2     sing N N 442 
THR CA    C      sing N N 443 
THR CA    CB     sing N N 444 
THR CA    HA     sing N N 445 
THR C     O      doub N N 446 
THR C     OXT    sing N N 447 
THR CB    OG1    sing N N 448 
THR CB    CG2    sing N N 449 
THR CB    HB     sing N N 450 
THR OG1   HG1    sing N N 451 
THR CG2   HG21   sing N N 452 
THR CG2   HG22   sing N N 453 
THR CG2   HG23   sing N N 454 
THR OXT   HXT    sing N N 455 
TRP N     CA     sing N N 456 
TRP N     H      sing N N 457 
TRP N     H2     sing N N 458 
TRP CA    C      sing N N 459 
TRP CA    CB     sing N N 460 
TRP CA    HA     sing N N 461 
TRP C     O      doub N N 462 
TRP C     OXT    sing N N 463 
TRP CB    CG     sing N N 464 
TRP CB    HB2    sing N N 465 
TRP CB    HB3    sing N N 466 
TRP CG    CD1    doub Y N 467 
TRP CG    CD2    sing Y N 468 
TRP CD1   NE1    sing Y N 469 
TRP CD1   HD1    sing N N 470 
TRP CD2   CE2    doub Y N 471 
TRP CD2   CE3    sing Y N 472 
TRP NE1   CE2    sing Y N 473 
TRP NE1   HE1    sing N N 474 
TRP CE2   CZ2    sing Y N 475 
TRP CE3   CZ3    doub Y N 476 
TRP CE3   HE3    sing N N 477 
TRP CZ2   CH2    doub Y N 478 
TRP CZ2   HZ2    sing N N 479 
TRP CZ3   CH2    sing Y N 480 
TRP CZ3   HZ3    sing N N 481 
TRP CH2   HH2    sing N N 482 
TRP OXT   HXT    sing N N 483 
TYR N     CA     sing N N 484 
TYR N     H      sing N N 485 
TYR N     H2     sing N N 486 
TYR CA    C      sing N N 487 
TYR CA    CB     sing N N 488 
TYR CA    HA     sing N N 489 
TYR C     O      doub N N 490 
TYR C     OXT    sing N N 491 
TYR CB    CG     sing N N 492 
TYR CB    HB2    sing N N 493 
TYR CB    HB3    sing N N 494 
TYR CG    CD1    doub Y N 495 
TYR CG    CD2    sing Y N 496 
TYR CD1   CE1    sing Y N 497 
TYR CD1   HD1    sing N N 498 
TYR CD2   CE2    doub Y N 499 
TYR CD2   HD2    sing N N 500 
TYR CE1   CZ     doub Y N 501 
TYR CE1   HE1    sing N N 502 
TYR CE2   CZ     sing Y N 503 
TYR CE2   HE2    sing N N 504 
TYR CZ    OH     sing N N 505 
TYR OH    HH     sing N N 506 
TYR OXT   HXT    sing N N 507 
VAL N     CA     sing N N 508 
VAL N     H      sing N N 509 
VAL N     H2     sing N N 510 
VAL CA    C      sing N N 511 
VAL CA    CB     sing N N 512 
VAL CA    HA     sing N N 513 
VAL C     O      doub N N 514 
VAL C     OXT    sing N N 515 
VAL CB    CG1    sing N N 516 
VAL CB    CG2    sing N N 517 
VAL CB    HB     sing N N 518 
VAL CG1   HG11   sing N N 519 
VAL CG1   HG12   sing N N 520 
VAL CG1   HG13   sing N N 521 
VAL CG2   HG21   sing N N 522 
VAL CG2   HG22   sing N N 523 
VAL CG2   HG23   sing N N 524 
VAL OXT   HXT    sing N N 525 
# 
_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           1R01GM132640 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6X9A 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9DL4 
_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]   0.009886 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002889 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009768 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.008171 
_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 
N 
O 
P 
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     . PRO A  1 17   ? -48.954 90.717  104.317 1.00 60.92 ? 15   PRO A N     1 
ATOM   2     C CA    . PRO A  1 17   ? -49.507 89.357  104.257 1.00 54.48 ? 15   PRO A CA    1 
ATOM   3     C C     . PRO A  1 17   ? -49.072 88.511  105.450 1.00 52.25 ? 15   PRO A C     1 
ATOM   4     O O     . PRO A  1 17   ? -47.914 88.593  105.868 1.00 53.19 ? 15   PRO A O     1 
ATOM   5     C CB    . PRO A  1 17   ? -48.931 88.794  102.951 1.00 53.80 ? 15   PRO A CB    1 
ATOM   6     C CG    . PRO A  1 17   ? -48.561 89.997  102.146 1.00 55.30 ? 15   PRO A CG    1 
ATOM   7     C CD    . PRO A  1 17   ? -48.118 91.024  103.144 1.00 53.14 ? 15   PRO A CD    1 
ATOM   8     N N     . ALA A  1 18   ? -49.990 87.717  105.990 1.00 49.24 ? 16   ALA A N     1 
ATOM   9     C CA    . ALA A  1 18   ? -49.668 86.902  107.151 1.00 46.33 ? 16   ALA A CA    1 
ATOM   10    C C     . ALA A  1 18   ? -48.610 85.864  106.780 1.00 46.88 ? 16   ALA A C     1 
ATOM   11    O O     . ALA A  1 18   ? -48.673 85.272  105.693 1.00 43.62 ? 16   ALA A O     1 
ATOM   12    C CB    . ALA A  1 18   ? -50.923 86.215  107.686 1.00 50.26 ? 16   ALA A CB    1 
ATOM   13    N N     . PRO A  1 19   ? -47.620 85.630  107.644 1.00 44.69 ? 17   PRO A N     1 
ATOM   14    C CA    . PRO A  1 19   ? -46.558 84.675  107.308 1.00 44.04 ? 17   PRO A CA    1 
ATOM   15    C C     . PRO A  1 19   ? -47.107 83.270  107.108 1.00 41.81 ? 17   PRO A C     1 
ATOM   16    O O     . PRO A  1 19   ? -47.957 82.798  107.867 1.00 42.21 ? 17   PRO A O     1 
ATOM   17    C CB    . PRO A  1 19   ? -45.621 84.751  108.517 1.00 43.56 ? 17   PRO A CB    1 
ATOM   18    C CG    . PRO A  1 19   ? -45.850 86.115  109.073 1.00 42.03 ? 17   PRO A CG    1 
ATOM   19    C CD    . PRO A  1 19   ? -47.332 86.350  108.895 1.00 43.87 ? 17   PRO A CD    1 
ATOM   20    N N     . PHE A  1 20   ? -46.640 82.627  106.040 1.00 38.96 ? 18   PHE A N     1 
ATOM   21    C CA    . PHE A  1 20   ? -46.924 81.233  105.713 1.00 37.86 ? 18   PHE A CA    1 
ATOM   22    C C     . PHE A  1 20   ? -48.395 80.964  105.433 1.00 38.98 ? 18   PHE A C     1 
ATOM   23    O O     . PHE A  1 20   ? -48.801 79.799  105.365 1.00 38.64 ? 18   PHE A O     1 
ATOM   24    C CB    . PHE A  1 20   ? -46.435 80.300  106.819 1.00 35.48 ? 18   PHE A CB    1 
ATOM   25    C CG    . PHE A  1 20   ? -44.956 80.383  107.063 1.00 34.66 ? 18   PHE A CG    1 
ATOM   26    C CD1   . PHE A  1 20   ? -44.068 79.879  106.136 1.00 33.69 ? 18   PHE A CD1   1 
ATOM   27    C CD2   . PHE A  1 20   ? -44.455 80.971  108.215 1.00 31.45 ? 18   PHE A CD2   1 
ATOM   28    C CE1   . PHE A  1 20   ? -42.701 79.947  106.357 1.00 34.95 ? 18   PHE A CE1   1 
ATOM   29    C CE2   . PHE A  1 20   ? -43.096 81.035  108.439 1.00 31.93 ? 18   PHE A CE2   1 
ATOM   30    C CZ    . PHE A  1 20   ? -42.222 80.516  107.511 1.00 34.93 ? 18   PHE A CZ    1 
ATOM   31    N N     . ALA A  1 21   ? -49.205 82.003  105.254 1.00 39.88 ? 19   ALA A N     1 
ATOM   32    C CA    . ALA A  1 21   ? -50.614 81.776  104.945 1.00 44.40 ? 19   ALA A CA    1 
ATOM   33    C C     . ALA A  1 21   ? -50.821 81.203  103.543 1.00 44.65 ? 19   ALA A C     1 
ATOM   34    O O     . ALA A  1 21   ? -51.878 80.625  103.270 1.00 50.92 ? 19   ALA A O     1 
ATOM   35    C CB    . ALA A  1 21   ? -51.399 83.076  105.109 1.00 44.92 ? 19   ALA A CB    1 
ATOM   36    N N     . ASP A  1 22   ? -49.849 81.347  102.651 1.00 40.61 ? 20   ASP A N     1 
ATOM   37    C CA    . ASP A  1 22   ? -49.948 80.820  101.295 1.00 40.73 ? 20   ASP A CA    1 
ATOM   38    C C     . ASP A  1 22   ? -48.766 79.912  100.972 1.00 34.91 ? 20   ASP A C     1 
ATOM   39    O O     . ASP A  1 22   ? -48.260 79.907  99.850  1.00 30.29 ? 20   ASP A O     1 
ATOM   40    C CB    . ASP A  1 22   ? -50.041 81.955  100.277 1.00 40.25 ? 20   ASP A CB    1 
ATOM   41    N N     . PHE A  1 23   ? -48.317 79.118  101.951 1.00 33.20 ? 21   PHE A N     1 
ATOM   42    C CA    . PHE A  1 23   ? -47.046 78.413  101.799 1.00 30.93 ? 21   PHE A CA    1 
ATOM   43    C C     . PHE A  1 23   ? -47.096 77.407  100.655 1.00 30.70 ? 21   PHE A C     1 
ATOM   44    O O     . PHE A  1 23   ? -46.266 77.448  99.736  1.00 28.83 ? 21   PHE A O     1 
ATOM   45    C CB    . PHE A  1 23   ? -46.652 77.712  103.104 1.00 30.79 ? 21   PHE A CB    1 
ATOM   46    C CG    . PHE A  1 23   ? -45.411 76.858  102.972 1.00 32.14 ? 21   PHE A CG    1 
ATOM   47    C CD1   . PHE A  1 23   ? -44.172 77.438  102.748 1.00 32.81 ? 21   PHE A CD1   1 
ATOM   48    C CD2   . PHE A  1 23   ? -45.487 75.476  103.065 1.00 33.56 ? 21   PHE A CD2   1 
ATOM   49    C CE1   . PHE A  1 23   ? -43.026 76.657  102.627 1.00 29.01 ? 21   PHE A CE1   1 
ATOM   50    C CE2   . PHE A  1 23   ? -44.353 74.695  102.936 1.00 30.91 ? 21   PHE A CE2   1 
ATOM   51    C CZ    . PHE A  1 23   ? -43.120 75.293  102.722 1.00 33.66 ? 21   PHE A CZ    1 
ATOM   52    N N     . ALA A  1 24   ? -48.060 76.483  100.700 1.00 28.36 ? 22   ALA A N     1 
ATOM   53    C CA    . ALA A  1 24   ? -48.109 75.403  99.721  1.00 31.61 ? 22   ALA A CA    1 
ATOM   54    C C     . ALA A  1 24   ? -49.516 74.827  99.621  1.00 29.29 ? 22   ALA A C     1 
ATOM   55    O O     . ALA A  1 24   ? -49.708 73.618  99.808  1.00 30.47 ? 22   ALA A O     1 
ATOM   56    C CB    . ALA A  1 24   ? -47.112 74.300  100.083 1.00 31.17 ? 22   ALA A CB    1 
ATOM   57    N N     . PRO A  1 25   ? -50.513 75.646  99.297  1.00 31.10 ? 23   PRO A N     1 
ATOM   58    C CA    . PRO A  1 25   ? -51.885 75.142  99.206  1.00 30.29 ? 23   PRO A CA    1 
ATOM   59    C C     . PRO A  1 25   ? -51.995 74.119  98.092  1.00 30.81 ? 23   PRO A C     1 
ATOM   60    O O     . PRO A  1 25   ? -51.418 74.312  97.011  1.00 30.05 ? 23   PRO A O     1 
ATOM   61    C CB    . PRO A  1 25   ? -52.704 76.405  98.896  1.00 30.29 ? 23   PRO A CB    1 
ATOM   62    C CG    . PRO A  1 25   ? -51.750 77.269  98.142  1.00 33.84 ? 23   PRO A CG    1 
ATOM   63    C CD    . PRO A  1 25   ? -50.387 77.008  98.746  1.00 29.79 ? 23   PRO A CD    1 
ATOM   64    N N     . PRO A  1 26   ? -52.688 73.005  98.326  1.00 32.24 ? 24   PRO A N     1 
ATOM   65    C CA    . PRO A  1 26   ? -52.856 72.009  97.262  1.00 30.15 ? 24   PRO A CA    1 
ATOM   66    C C     . PRO A  1 26   ? -53.631 72.574  96.080  1.00 32.09 ? 24   PRO A C     1 
ATOM   67    O O     . PRO A  1 26   ? -54.418 73.516  96.217  1.00 30.99 ? 24   PRO A O     1 
ATOM   68    C CB    . PRO A  1 26   ? -53.628 70.878  97.950  1.00 29.25 ? 24   PRO A CB    1 
ATOM   69    C CG    . PRO A  1 26   ? -54.319 71.553  99.143  1.00 32.57 ? 24   PRO A CG    1 
ATOM   70    C CD    . PRO A  1 26   ? -53.299 72.572  99.598  1.00 33.02 ? 24   PRO A CD    1 
ATOM   71    N N     . VAL A  1 27   ? -53.385 71.987  94.903  1.00 30.68 ? 25   VAL A N     1 
ATOM   72    C CA    . VAL A  1 27   ? -54.117 72.367  93.692  1.00 32.58 ? 25   VAL A CA    1 
ATOM   73    C C     . VAL A  1 27   ? -55.619 72.236  93.906  1.00 34.37 ? 25   VAL A C     1 
ATOM   74    O O     . VAL A  1 27   ? -56.395 73.109  93.493  1.00 32.26 ? 25   VAL A O     1 
ATOM   75    C CB    . VAL A  1 27   ? -53.634 71.521  92.495  1.00 33.80 ? 25   VAL A CB    1 
ATOM   76    C CG1   . VAL A  1 27   ? -54.603 71.634  91.316  1.00 33.81 ? 25   VAL A CG1   1 
ATOM   77    C CG2   . VAL A  1 27   ? -52.239 71.951  92.084  1.00 26.95 ? 25   VAL A CG2   1 
ATOM   78    N N     . ARG A  1 28   ? -56.046 71.171  94.584  1.00 32.63 ? 26   ARG A N     1 
ATOM   79    C CA    . ARG A  1 28   ? -57.445 70.891  94.880  1.00 36.61 ? 26   ARG A CA    1 
ATOM   80    C C     . ARG A  1 28   ? -57.515 70.180  96.222  1.00 37.89 ? 26   ARG A C     1 
ATOM   81    O O     . ARG A  1 28   ? -56.513 69.611  96.676  1.00 36.20 ? 26   ARG A O     1 
ATOM   82    C CB    . ARG A  1 28   ? -58.079 70.013  93.793  1.00 37.87 ? 26   ARG A CB    1 
ATOM   83    C CG    . ARG A  1 28   ? -57.693 68.532  93.907  1.00 37.57 ? 26   ARG A CG    1 
ATOM   84    C CD    . ARG A  1 28   ? -58.322 67.680  92.803  1.00 42.20 ? 26   ARG A CD    1 
ATOM   85    N NE    . ARG A  1 28   ? -57.616 67.857  91.540  1.00 41.69 ? 26   ARG A NE    1 
ATOM   86    C CZ    . ARG A  1 28   ? -58.004 68.692  90.586  1.00 42.59 ? 26   ARG A CZ    1 
ATOM   87    N NH1   . ARG A  1 28   ? -59.149 69.356  90.669  1.00 39.20 ? 26   ARG A NH1   1 
ATOM   88    N NH2   . ARG A  1 28   ? -57.218 68.878  89.534  1.00 39.22 ? 26   ARG A NH2   1 
ATOM   89    N N     . PRO A  1 29   ? -58.685 70.170  96.875  1.00 37.90 ? 27   PRO A N     1 
ATOM   90    C CA    . PRO A  1 29   ? -58.816 69.398  98.120  1.00 37.69 ? 27   PRO A CA    1 
ATOM   91    C C     . PRO A  1 29   ? -58.598 67.915  97.859  1.00 36.26 ? 27   PRO A C     1 
ATOM   92    O O     . PRO A  1 29   ? -59.052 67.375  96.851  1.00 36.92 ? 27   PRO A O     1 
ATOM   93    C CB    . PRO A  1 29   ? -60.252 69.684  98.573  1.00 38.67 ? 27   PRO A CB    1 
ATOM   94    C CG    . PRO A  1 29   ? -60.638 70.950  97.868  1.00 37.30 ? 27   PRO A CG    1 
ATOM   95    C CD    . PRO A  1 29   ? -59.927 70.891  96.549  1.00 39.06 ? 27   PRO A CD    1 
ATOM   96    N N     . GLN A  1 30   ? -57.886 67.259  98.775  1.00 36.06 ? 28   GLN A N     1 
ATOM   97    C CA    . GLN A  1 30   ? -57.436 65.885  98.558  1.00 37.09 ? 28   GLN A CA    1 
ATOM   98    C C     . GLN A  1 30   ? -58.570 64.921  98.903  1.00 37.37 ? 28   GLN A C     1 
ATOM   99    O O     . GLN A  1 30   ? -58.964 64.795  100.069 1.00 35.03 ? 28   GLN A O     1 
ATOM   100   C CB    . GLN A  1 30   ? -56.184 65.597  99.386  1.00 35.19 ? 28   GLN A CB    1 
ATOM   101   C CG    . GLN A  1 30   ? -54.997 66.527  99.082  1.00 31.41 ? 28   GLN A CG    1 
ATOM   102   C CD    . GLN A  1 30   ? -54.472 66.347  97.660  1.00 32.60 ? 28   GLN A CD    1 
ATOM   103   O OE1   . GLN A  1 30   ? -53.727 65.402  97.376  1.00 32.53 ? 28   GLN A OE1   1 
ATOM   104   N NE2   . GLN A  1 30   ? -54.864 67.244  96.760  1.00 33.33 ? 28   GLN A NE2   1 
ATOM   105   N N     . SER A  1 31   ? -59.090 64.240  97.884  1.00 33.04 ? 29   SER A N     1 
ATOM   106   C CA    . SER A  1 31   ? -60.127 63.235  98.058  1.00 31.28 ? 29   SER A CA    1 
ATOM   107   C C     . SER A  1 31   ? -59.588 62.024  98.820  1.00 31.94 ? 29   SER A C     1 
ATOM   108   O O     . SER A  1 31   ? -58.378 61.836  98.978  1.00 30.67 ? 29   SER A O     1 
ATOM   109   C CB    . SER A  1 31   ? -60.662 62.802  96.696  1.00 30.77 ? 29   SER A CB    1 
ATOM   110   O OG    . SER A  1 31   ? -59.744 61.937  96.056  1.00 31.08 ? 29   SER A OG    1 
ATOM   111   N N     . THR A  1 32   ? -60.519 61.182  99.287  1.00 29.87 ? 30   THR A N     1 
ATOM   112   C CA    . THR A  1 32   ? -60.142 59.934  99.943  1.00 29.71 ? 30   THR A CA    1 
ATOM   113   C C     . THR A  1 32   ? -59.227 59.101  99.062  1.00 28.17 ? 30   THR A C     1 
ATOM   114   O O     . THR A  1 32   ? -58.260 58.509  99.544  1.00 28.97 ? 30   THR A O     1 
ATOM   115   C CB    . THR A  1 32   ? -61.402 59.137  100.301 1.00 31.60 ? 30   THR A CB    1 
ATOM   116   O OG1   . THR A  1 32   ? -62.156 59.875  101.258 1.00 31.82 ? 30   THR A OG1   1 
ATOM   117   C CG2   . THR A  1 32   ? -61.053 57.771  100.871 1.00 34.40 ? 30   THR A CG2   1 
ATOM   118   N N     . LEU A  1 33   ? -59.520 59.032  97.766  1.00 26.45 ? 31   LEU A N     1 
ATOM   119   C CA    . LEU A  1 33   ? -58.667 58.248  96.880  1.00 28.78 ? 31   LEU A CA    1 
ATOM   120   C C     . LEU A  1 33   ? -57.281 58.869  96.741  1.00 29.52 ? 31   LEU A C     1 
ATOM   121   O O     . LEU A  1 33   ? -56.275 58.151  96.738  1.00 27.90 ? 31   LEU A O     1 
ATOM   122   C CB    . LEU A  1 33   ? -59.336 58.096  95.515  1.00 31.49 ? 31   LEU A CB    1 
ATOM   123   C CG    . LEU A  1 33   ? -60.476 57.076  95.530  1.00 33.02 ? 31   LEU A CG    1 
ATOM   124   C CD1   . LEU A  1 33   ? -61.428 57.310  94.355  1.00 28.97 ? 31   LEU A CD1   1 
ATOM   125   C CD2   . LEU A  1 33   ? -59.905 55.666  95.524  1.00 31.01 ? 31   LEU A CD2   1 
ATOM   126   N N     . ARG A  1 34   ? -57.207 60.196  96.626  1.00 26.45 ? 32   ARG A N     1 
ATOM   127   C CA    . ARG A  1 34   ? -55.904 60.847  96.543  1.00 30.12 ? 32   ARG A CA    1 
ATOM   128   C C     . ARG A  1 34   ? -55.125 60.689  97.842  1.00 27.63 ? 32   ARG A C     1 
ATOM   129   O O     . ARG A  1 34   ? -53.903 60.517  97.819  1.00 28.21 ? 32   ARG A O     1 
ATOM   130   C CB    . ARG A  1 34   ? -56.073 62.328  96.197  1.00 31.15 ? 32   ARG A CB    1 
ATOM   131   C CG    . ARG A  1 34   ? -56.486 62.598  94.765  1.00 32.45 ? 32   ARG A CG    1 
ATOM   132   C CD    . ARG A  1 34   ? -55.345 62.367  93.776  1.00 25.53 ? 32   ARG A CD    1 
ATOM   133   N NE    . ARG A  1 34   ? -54.230 63.298  93.931  1.00 30.80 ? 32   ARG A NE    1 
ATOM   134   C CZ    . ARG A  1 34   ? -54.144 64.482  93.335  1.00 32.67 ? 32   ARG A CZ    1 
ATOM   135   N NH1   . ARG A  1 34   ? -55.100 64.925  92.529  1.00 32.49 ? 32   ARG A NH1   1 
ATOM   136   N NH2   . ARG A  1 34   ? -53.069 65.239  93.547  1.00 29.86 ? 32   ARG A NH2   1 
ATOM   137   N N     . ARG A  1 35   ? -55.813 60.742  98.990  1.00 26.77 ? 33   ARG A N     1 
ATOM   138   C CA    . ARG A  1 35   ? -55.126 60.572  100.268 1.00 28.58 ? 33   ARG A CA    1 
ATOM   139   C C     . ARG A  1 35   ? -54.551 59.169  100.429 1.00 30.46 ? 33   ARG A C     1 
ATOM   140   O O     . ARG A  1 35   ? -53.498 59.007  101.056 1.00 28.19 ? 33   ARG A O     1 
ATOM   141   C CB    . ARG A  1 35   ? -56.068 60.882  101.430 1.00 30.94 ? 33   ARG A CB    1 
ATOM   142   C CG    . ARG A  1 35   ? -56.434 62.355  101.517 1.00 35.23 ? 33   ARG A CG    1 
ATOM   143   C CD    . ARG A  1 35   ? -57.473 62.642  102.590 1.00 44.81 ? 33   ARG A CD    1 
ATOM   144   N NE    . ARG A  1 35   ? -57.730 64.077  102.636 1.00 51.35 ? 33   ARG A NE    1 
ATOM   145   C CZ    . ARG A  1 35   ? -56.962 64.947  103.283 1.00 53.06 ? 33   ARG A CZ    1 
ATOM   146   N NH1   . ARG A  1 35   ? -55.941 64.548  104.022 1.00 53.80 ? 33   ARG A NH1   1 
ATOM   147   N NH2   . ARG A  1 35   ? -57.219 66.250  103.176 1.00 45.97 ? 33   ARG A NH2   1 
ATOM   148   N N     . ALA A  1 36   ? -55.222 58.147  99.890  1.00 25.50 ? 34   ALA A N     1 
ATOM   149   C CA    . ALA A  1 36   ? -54.661 56.799  99.950  1.00 28.02 ? 34   ALA A CA    1 
ATOM   150   C C     . ALA A  1 36   ? -53.378 56.699  99.135  1.00 27.33 ? 34   ALA A C     1 
ATOM   151   O O     . ALA A  1 36   ? -52.468 55.945  99.491  1.00 27.41 ? 34   ALA A O     1 
ATOM   152   C CB    . ALA A  1 36   ? -55.680 55.772  99.450  1.00 26.20 ? 34   ALA A CB    1 
ATOM   153   N N     . ILE A  1 37   ? -53.292 57.438  98.034  1.00 26.95 ? 35   ILE A N     1 
ATOM   154   C CA    . ILE A  1 37   ? -52.048 57.486  97.271  1.00 28.29 ? 35   ILE A CA    1 
ATOM   155   C C     . ILE A  1 37   ? -50.925 58.079  98.111  1.00 25.80 ? 35   ILE A C     1 
ATOM   156   O O     . ILE A  1 37   ? -49.846 57.485  98.258  1.00 24.61 ? 35   ILE A O     1 
ATOM   157   C CB    . ILE A  1 37   ? -52.258 58.289  95.980  1.00 26.69 ? 35   ILE A CB    1 
ATOM   158   C CG1   . ILE A  1 37   ? -53.239 57.553  95.081  1.00 23.94 ? 35   ILE A CG1   1 
ATOM   159   C CG2   . ILE A  1 37   ? -50.931 58.534  95.292  1.00 21.26 ? 35   ILE A CG2   1 
ATOM   160   C CD1   . ILE A  1 37   ? -53.657 58.377  93.896  1.00 23.34 ? 35   ILE A CD1   1 
ATOM   161   N N     . THR A  1 38   ? -51.152 59.276  98.652  1.00 28.66 ? 36   THR A N     1 
ATOM   162   C CA    . THR A  1 38   ? -50.110 59.951  99.410  1.00 26.83 ? 36   THR A CA    1 
ATOM   163   C C     . THR A  1 38   ? -49.697 59.127  100.621 1.00 28.44 ? 36   THR A C     1 
ATOM   164   O O     . THR A  1 38   ? -48.507 59.053  100.956 1.00 27.45 ? 36   THR A O     1 
ATOM   165   C CB    . THR A  1 38   ? -50.591 61.337  99.825  1.00 26.01 ? 36   THR A CB    1 
ATOM   166   O OG1   . THR A  1 38   ? -51.105 62.014  98.677  1.00 27.67 ? 36   THR A OG1   1 
ATOM   167   C CG2   . THR A  1 38   ? -49.444 62.161  100.380 1.00 29.74 ? 36   THR A CG2   1 
ATOM   168   N N     . ALA A  1 39   ? -50.666 58.470  101.263 1.00 26.94 ? 37   ALA A N     1 
ATOM   169   C CA    . ALA A  1 39   ? -50.368 57.642  102.424 1.00 28.54 ? 37   ALA A CA    1 
ATOM   170   C C     . ALA A  1 39   ? -49.386 56.520  102.092 1.00 29.11 ? 37   ALA A C     1 
ATOM   171   O O     . ALA A  1 39   ? -48.652 56.064  102.973 1.00 28.72 ? 37   ALA A O     1 
ATOM   172   C CB    . ALA A  1 39   ? -51.668 57.068  102.996 1.00 28.02 ? 37   ALA A CB    1 
ATOM   173   N N     . ALA A  1 40   ? -49.352 56.066  100.836 1.00 26.53 ? 38   ALA A N     1 
ATOM   174   C CA    . ALA A  1 40   ? -48.519 54.938  100.438 1.00 25.81 ? 38   ALA A CA    1 
ATOM   175   C C     . ALA A  1 40   ? -47.143 55.356  99.939  1.00 26.04 ? 38   ALA A C     1 
ATOM   176   O O     . ALA A  1 40   ? -46.348 54.481  99.590  1.00 27.20 ? 38   ALA A O     1 
ATOM   177   C CB    . ALA A  1 40   ? -49.224 54.118  99.346  1.00 24.23 ? 38   ALA A CB    1 
ATOM   178   N N     . TYR A  1 41   ? -46.854 56.665  99.917  1.00 25.87 ? 39   TYR A N     1 
ATOM   179   C CA    . TYR A  1 41   ? -45.694 57.209  99.208  1.00 24.60 ? 39   TYR A CA    1 
ATOM   180   C C     . TYR A  1 41   ? -44.414 56.466  99.573  1.00 28.84 ? 39   TYR A C     1 
ATOM   181   O O     . TYR A  1 41   ? -43.660 56.029  98.693  1.00 27.23 ? 39   TYR A O     1 
ATOM   182   C CB    . TYR A  1 41   ? -45.567 58.706  99.532  1.00 24.49 ? 39   TYR A CB    1 
ATOM   183   C CG    . TYR A  1 41   ? -44.798 59.574  98.542  1.00 27.06 ? 39   TYR A CG    1 
ATOM   184   C CD1   . TYR A  1 41   ? -43.746 59.069  97.789  1.00 23.77 ? 39   TYR A CD1   1 
ATOM   185   C CD2   . TYR A  1 41   ? -45.129 60.913  98.383  1.00 27.07 ? 39   TYR A CD2   1 
ATOM   186   C CE1   . TYR A  1 41   ? -43.054 59.874  96.905  1.00 26.90 ? 39   TYR A CE1   1 
ATOM   187   C CE2   . TYR A  1 41   ? -44.453 61.722  97.506  1.00 25.13 ? 39   TYR A CE2   1 
ATOM   188   C CZ    . TYR A  1 41   ? -43.414 61.199  96.761  1.00 27.70 ? 39   TYR A CZ    1 
ATOM   189   O OH    . TYR A  1 41   ? -42.726 62.010  95.878  1.00 24.74 ? 39   TYR A OH    1 
ATOM   190   N N     . ARG A  1 42   ? -44.148 56.315  100.866 1.00 26.63 ? 40   ARG A N     1 
ATOM   191   C CA    . ARG A  1 42   ? -42.907 55.690  101.321 1.00 27.25 ? 40   ARG A CA    1 
ATOM   192   C C     . ARG A  1 42   ? -43.207 54.587  102.327 1.00 30.81 ? 40   ARG A C     1 
ATOM   193   O O     . ARG A  1 42   ? -42.468 54.365  103.296 1.00 30.22 ? 40   ARG A O     1 
ATOM   194   C CB    . ARG A  1 42   ? -41.954 56.742  101.885 1.00 31.17 ? 40   ARG A CB    1 
ATOM   195   C CG    . ARG A  1 42   ? -41.424 57.661  100.791 1.00 27.48 ? 40   ARG A CG    1 
ATOM   196   C CD    . ARG A  1 42   ? -40.633 58.847  101.269 1.00 29.47 ? 40   ARG A CD    1 
ATOM   197   N NE    . ARG A  1 42   ? -40.634 59.885  100.241 1.00 28.29 ? 40   ARG A NE    1 
ATOM   198   C CZ    . ARG A  1 42   ? -39.855 59.893  99.167  1.00 27.53 ? 40   ARG A CZ    1 
ATOM   199   N NH1   . ARG A  1 42   ? -38.908 58.981  98.987  1.00 27.05 ? 40   ARG A NH1   1 
ATOM   200   N NH2   . ARG A  1 42   ? -40.030 60.838  98.249  1.00 26.80 ? 40   ARG A NH2   1 
ATOM   201   N N     . ARG A  1 43   ? -44.275 53.850  102.074 1.00 28.62 ? 41   ARG A N     1 
ATOM   202   C CA    . ARG A  1 43   ? -44.697 52.807  102.990 1.00 32.82 ? 41   ARG A CA    1 
ATOM   203   C C     . ARG A  1 43   ? -43.651 51.698  103.046 1.00 33.39 ? 41   ARG A C     1 
ATOM   204   O O     . ARG A  1 43   ? -43.089 51.326  102.013 1.00 30.69 ? 41   ARG A O     1 
ATOM   205   C CB    . ARG A  1 43   ? -46.033 52.238  102.542 1.00 30.11 ? 41   ARG A CB    1 
ATOM   206   C CG    . ARG A  1 43   ? -46.485 51.005  103.285 1.00 30.97 ? 41   ARG A CG    1 
ATOM   207   C CD    . ARG A  1 43   ? -47.905 50.701  102.894 1.00 34.84 ? 41   ARG A CD    1 
ATOM   208   N NE    . ARG A  1 43   ? -48.799 51.804  103.225 1.00 32.59 ? 41   ARG A NE    1 
ATOM   209   C CZ    . ARG A  1 43   ? -49.933 52.050  102.587 1.00 32.37 ? 41   ARG A CZ    1 
ATOM   210   N NH1   . ARG A  1 43   ? -50.312 51.318  101.556 1.00 32.02 ? 41   ARG A NH1   1 
ATOM   211   N NH2   . ARG A  1 43   ? -50.699 53.061  102.985 1.00 31.83 ? 41   ARG A NH2   1 
ATOM   212   N N     . PRO A  1 44   ? -43.361 51.162  104.231 1.00 33.57 ? 42   PRO A N     1 
ATOM   213   C CA    . PRO A  1 44   ? -42.358 50.098  104.333 1.00 33.99 ? 42   PRO A CA    1 
ATOM   214   C C     . PRO A  1 44   ? -42.670 48.944  103.391 1.00 35.33 ? 42   PRO A C     1 
ATOM   215   O O     . PRO A  1 44   ? -43.826 48.563  103.198 1.00 31.98 ? 42   PRO A O     1 
ATOM   216   C CB    . PRO A  1 44   ? -42.442 49.676  105.802 1.00 38.34 ? 42   PRO A CB    1 
ATOM   217   C CG    . PRO A  1 44   ? -42.910 50.911  106.507 1.00 39.23 ? 42   PRO A CG    1 
ATOM   218   C CD    . PRO A  1 44   ? -43.869 51.576  105.550 1.00 38.65 ? 42   PRO A CD    1 
ATOM   219   N N     . GLU A  1 45   ? -41.610 48.405  102.788 1.00 36.16 ? 43   GLU A N     1 
ATOM   220   C CA    . GLU A  1 45   ? -41.747 47.387  101.754 1.00 34.09 ? 43   GLU A CA    1 
ATOM   221   C C     . GLU A  1 45   ? -42.389 46.112  102.292 1.00 35.25 ? 43   GLU A C     1 
ATOM   222   O O     . GLU A  1 45   ? -43.081 45.406  101.549 1.00 33.49 ? 43   GLU A O     1 
ATOM   223   C CB    . GLU A  1 45   ? -40.359 47.117  101.152 1.00 36.07 ? 43   GLU A CB    1 
ATOM   224   C CG    . GLU A  1 45   ? -40.345 46.614  99.733  1.00 35.79 ? 43   GLU A CG    1 
ATOM   225   C CD    . GLU A  1 45   ? -39.001 46.850  99.039  1.00 31.04 ? 43   GLU A CD    1 
ATOM   226   O OE1   . GLU A  1 45   ? -38.142 47.577  99.588  1.00 31.26 ? 43   GLU A OE1   1 
ATOM   227   O OE2   . GLU A  1 45   ? -38.808 46.295  97.946  1.00 31.54 ? 43   GLU A OE2   1 
ATOM   228   N N     . THR A  1 46   ? -42.184 45.803  103.581 1.00 33.93 ? 44   THR A N     1 
ATOM   229   C CA    . THR A  1 46   ? -42.850 44.654  104.185 1.00 35.80 ? 44   THR A CA    1 
ATOM   230   C C     . THR A  1 46   ? -44.358 44.864  104.276 1.00 37.68 ? 44   THR A C     1 
ATOM   231   O O     . THR A  1 46   ? -45.124 43.892  104.270 1.00 35.51 ? 44   THR A O     1 
ATOM   232   C CB    . THR A  1 46   ? -42.268 44.376  105.576 1.00 39.40 ? 44   THR A CB    1 
ATOM   233   O OG1   . THR A  1 46   ? -42.304 45.574  106.370 1.00 34.02 ? 44   THR A OG1   1 
ATOM   234   C CG2   . THR A  1 46   ? -40.827 43.905  105.457 1.00 33.56 ? 44   THR A CG2   1 
ATOM   235   N N     . GLU A  1 47   ? -44.804 46.116  104.342 1.00 35.70 ? 45   GLU A N     1 
ATOM   236   C CA    . GLU A  1 47   ? -46.238 46.381  104.359 1.00 39.05 ? 45   GLU A CA    1 
ATOM   237   C C     . GLU A  1 47   ? -46.848 46.383  102.961 1.00 37.26 ? 45   GLU A C     1 
ATOM   238   O O     . GLU A  1 47   ? -48.042 46.094  102.813 1.00 34.21 ? 45   GLU A O     1 
ATOM   239   C CB    . GLU A  1 47   ? -46.511 47.712  105.058 1.00 38.21 ? 45   GLU A CB    1 
ATOM   240   C CG    . GLU A  1 47   ? -46.015 47.746  106.492 1.00 45.78 ? 45   GLU A CG    1 
ATOM   241   C CD    . GLU A  1 47   ? -46.194 49.102  107.135 1.00 51.76 ? 45   GLU A CD    1 
ATOM   242   O OE1   . GLU A  1 47   ? -47.041 49.884  106.646 1.00 52.32 ? 45   GLU A OE1   1 
ATOM   243   O OE2   . GLU A  1 47   ? -45.487 49.385  108.128 1.00 57.83 ? 45   GLU A OE2   1 
ATOM   244   N N     . CYS A  1 48   ? -46.065 46.695  101.927 1.00 35.02 ? 46   CYS A N     1 
ATOM   245   C CA    . CYS A  1 48   ? -46.651 46.775  100.592 1.00 33.38 ? 46   CYS A CA    1 
ATOM   246   C C     . CYS A  1 48   ? -46.916 45.395  100.004 1.00 34.27 ? 46   CYS A C     1 
ATOM   247   O O     . CYS A  1 48   ? -47.946 45.186  99.347  1.00 30.54 ? 46   CYS A O     1 
ATOM   248   C CB    . CYS A  1 48   ? -45.741 47.569  99.649  1.00 32.05 ? 46   CYS A CB    1 
ATOM   249   S SG    . CYS A  1 48   ? -45.480 49.308  100.091 1.00 35.02 ? 46   CYS A SG    1 
ATOM   250   N N     . LEU A  1 49   ? -46.007 44.438  100.248 1.00 31.99 ? 47   LEU A N     1 
ATOM   251   C CA    . LEU A  1 49   ? -46.013 43.200  99.466  1.00 35.88 ? 47   LEU A CA    1 
ATOM   252   C C     . LEU A  1 49   ? -47.183 42.267  99.764  1.00 30.93 ? 47   LEU A C     1 
ATOM   253   O O     . LEU A  1 49   ? -47.780 41.749  98.802  1.00 38.11 ? 47   LEU A O     1 
ATOM   254   C CB    . LEU A  1 49   ? -44.671 42.476  99.624  1.00 33.44 ? 47   LEU A CB    1 
ATOM   255   C CG    . LEU A  1 49   ? -43.725 42.744  98.449  1.00 34.36 ? 47   LEU A CG    1 
ATOM   256   C CD1   . LEU A  1 49   ? -44.344 42.250  97.142  1.00 34.34 ? 47   LEU A CD1   1 
ATOM   257   C CD2   . LEU A  1 49   ? -43.432 44.220  98.348  1.00 30.41 ? 47   LEU A CD2   1 
ATOM   258   N N     . PRO A  1 50   ? -47.552 41.980  101.016 1.00 37.76 ? 48   PRO A N     1 
ATOM   259   C CA    . PRO A  1 50   ? -48.590 40.946  101.263 1.00 37.38 ? 48   PRO A CA    1 
ATOM   260   C C     . PRO A  1 50   ? -49.872 41.197  100.479 1.00 34.03 ? 48   PRO A C     1 
ATOM   261   O O     . PRO A  1 50   ? -50.388 40.267  99.835  1.00 39.18 ? 48   PRO A O     1 
ATOM   262   C CB    . PRO A  1 50   ? -48.819 41.026  102.781 1.00 36.70 ? 48   PRO A CB    1 
ATOM   263   C CG    . PRO A  1 50   ? -47.497 41.439  103.303 1.00 40.62 ? 48   PRO A CG    1 
ATOM   264   C CD    . PRO A  1 50   ? -46.943 42.424  102.285 1.00 36.65 ? 48   PRO A CD    1 
ATOM   265   N N     . PRO A  1 51   ? -50.429 42.417  100.470 1.00 35.09 ? 49   PRO A N     1 
ATOM   266   C CA    . PRO A  1 51   ? -51.633 42.613  99.647  1.00 38.13 ? 49   PRO A CA    1 
ATOM   267   C C     . PRO A  1 51   ? -51.375 42.464  98.152  1.00 34.05 ? 49   PRO A C     1 
ATOM   268   O O     . PRO A  1 51   ? -52.297 42.092  97.414  1.00 37.78 ? 49   PRO A O     1 
ATOM   269   C CB    . PRO A  1 51   ? -52.094 44.033  100.009 1.00 37.61 ? 49   PRO A CB    1 
ATOM   270   C CG    . PRO A  1 51   ? -50.873 44.716  100.456 1.00 36.69 ? 49   PRO A CG    1 
ATOM   271   C CD    . PRO A  1 51   ? -50.060 43.665  101.168 1.00 35.40 ? 49   PRO A CD    1 
ATOM   272   N N     . LEU A  1 52   ? -50.162 42.746  97.672  1.00 34.64 ? 50   LEU A N     1 
ATOM   273   C CA    . LEU A  1 52   ? -49.880 42.513  96.257  1.00 32.16 ? 50   LEU A CA    1 
ATOM   274   C C     . LEU A  1 52   ? -49.769 41.019  95.968  1.00 36.79 ? 50   LEU A C     1 
ATOM   275   O O     . LEU A  1 52   ? -50.295 40.531  94.959  1.00 32.76 ? 50   LEU A O     1 
ATOM   276   C CB    . LEU A  1 52   ? -48.607 43.259  95.836  1.00 29.56 ? 50   LEU A CB    1 
ATOM   277   C CG    . LEU A  1 52   ? -48.665 44.792  95.957  1.00 30.59 ? 50   LEU A CG    1 
ATOM   278   C CD1   . LEU A  1 52   ? -47.276 45.444  95.995  1.00 30.37 ? 50   LEU A CD1   1 
ATOM   279   C CD2   . LEU A  1 52   ? -49.517 45.422  94.848  1.00 29.46 ? 50   LEU A CD2   1 
ATOM   280   N N     . VAL A  1 53   ? -49.106 40.271  96.853  1.00 36.35 ? 51   VAL A N     1 
ATOM   281   C CA    . VAL A  1 53   ? -49.056 38.819  96.694  1.00 39.45 ? 51   VAL A CA    1 
ATOM   282   C C     . VAL A  1 53   ? -50.463 38.228  96.655  1.00 37.54 ? 51   VAL A C     1 
ATOM   283   O O     . VAL A  1 53   ? -50.770 37.373  95.811  1.00 38.72 ? 51   VAL A O     1 
ATOM   284   C CB    . VAL A  1 53   ? -48.203 38.195  97.811  1.00 39.28 ? 51   VAL A CB    1 
ATOM   285   C CG1   . VAL A  1 53   ? -48.297 36.677  97.757  1.00 41.94 ? 51   VAL A CG1   1 
ATOM   286   C CG2   . VAL A  1 53   ? -46.778 38.664  97.663  1.00 32.36 ? 51   VAL A CG2   1 
ATOM   287   N N     . GLU A  1 54   ? -51.355 38.693  97.536  1.00 38.28 ? 52   GLU A N     1 
ATOM   288   C CA    . GLU A  1 54   ? -52.714 38.153  97.527  1.00 38.18 ? 52   GLU A CA    1 
ATOM   289   C C     . GLU A  1 54   ? -53.443 38.502  96.231  1.00 38.96 ? 52   GLU A C     1 
ATOM   290   O O     . GLU A  1 54   ? -54.128 37.650  95.655  1.00 40.36 ? 52   GLU A O     1 
ATOM   291   C CB    . GLU A  1 54   ? -53.497 38.646  98.747  1.00 37.38 ? 52   GLU A CB    1 
ATOM   292   N N     . ALA A  1 55   ? -53.282 39.736  95.737  1.00 37.63 ? 53   ALA A N     1 
ATOM   293   C CA    . ALA A  1 55   ? -53.994 40.140  94.529  1.00 36.52 ? 53   ALA A CA    1 
ATOM   294   C C     . ALA A  1 55   ? -53.434 39.465  93.280  1.00 37.49 ? 53   ALA A C     1 
ATOM   295   O O     . ALA A  1 55   ? -54.162 39.287  92.301  1.00 36.39 ? 53   ALA A O     1 
ATOM   296   C CB    . ALA A  1 55   ? -53.953 41.658  94.376  1.00 35.72 ? 53   ALA A CB    1 
ATOM   297   N N     . ALA A  1 56   ? -52.162 39.076  93.291  1.00 36.88 ? 54   ALA A N     1 
ATOM   298   C CA    . ALA A  1 56   ? -51.532 38.449  92.134  1.00 36.31 ? 54   ALA A CA    1 
ATOM   299   C C     . ALA A  1 56   ? -51.678 36.930  92.113  1.00 41.52 ? 54   ALA A C     1 
ATOM   300   O O     . ALA A  1 56   ? -51.246 36.295  91.146  1.00 40.94 ? 54   ALA A O     1 
ATOM   301   C CB    . ALA A  1 56   ? -50.042 38.832  92.082  1.00 32.75 ? 54   ALA A CB    1 
ATOM   302   N N     . THR A  1 57   ? -52.294 36.337  93.138  1.00 46.44 ? 55   THR A N     1 
ATOM   303   C CA    . THR A  1 57   ? -52.396 34.883  93.241  1.00 43.86 ? 55   THR A CA    1 
ATOM   304   C C     . THR A  1 57   ? -53.358 34.320  92.197  1.00 41.89 ? 55   THR A C     1 
ATOM   305   O O     . THR A  1 57   ? -54.449 34.858  91.992  1.00 41.99 ? 55   THR A O     1 
ATOM   306   C CB    . THR A  1 57   ? -52.863 34.496  94.644  1.00 44.83 ? 55   THR A CB    1 
ATOM   307   O OG1   . THR A  1 57   ? -51.944 35.014  95.611  1.00 42.58 ? 55   THR A OG1   1 
ATOM   308   C CG2   . THR A  1 57   ? -52.938 32.986  94.786  1.00 51.84 ? 55   THR A CG2   1 
ATOM   309   N N     . GLN A  1 58   ? -52.948 33.242  91.527  1.00 39.79 ? 56   GLN A N     1 
ATOM   310   C CA    . GLN A  1 58   ? -53.790 32.563  90.551  1.00 44.17 ? 56   GLN A CA    1 
ATOM   311   C C     . GLN A  1 58   ? -53.803 31.069  90.858  1.00 48.40 ? 56   GLN A C     1 
ATOM   312   O O     . GLN A  1 58   ? -52.955 30.559  91.596  1.00 45.76 ? 56   GLN A O     1 
ATOM   313   C CB    . GLN A  1 58   ? -53.315 32.803  89.109  1.00 42.64 ? 56   GLN A CB    1 
ATOM   314   C CG    . GLN A  1 58   ? -53.186 34.276  88.715  1.00 39.80 ? 56   GLN A CG    1 
ATOM   315   C CD    . GLN A  1 58   ? -53.143 34.475  87.213  1.00 41.73 ? 56   GLN A CD    1 
ATOM   316   O OE1   . GLN A  1 58   ? -54.156 34.318  86.523  1.00 39.44 ? 56   GLN A OE1   1 
ATOM   317   N NE2   . GLN A  1 58   ? -51.968 34.825  86.695  1.00 39.62 ? 56   GLN A NE2   1 
ATOM   318   N N     . SER A  1 59   ? -54.768 30.368  90.266  1.00 44.18 ? 57   SER A N     1 
ATOM   319   C CA    . SER A  1 59   ? -54.962 28.959  90.587  1.00 45.81 ? 57   SER A CA    1 
ATOM   320   C C     . SER A  1 59   ? -53.752 28.133  90.157  1.00 49.73 ? 57   SER A C     1 
ATOM   321   O O     . SER A  1 59   ? -52.923 28.563  89.347  1.00 45.98 ? 57   SER A O     1 
ATOM   322   C CB    . SER A  1 59   ? -56.226 28.426  89.916  1.00 46.55 ? 57   SER A CB    1 
ATOM   323   O OG    . SER A  1 59   ? -56.134 28.514  88.503  1.00 46.64 ? 57   SER A OG    1 
ATOM   324   N N     . LYS A  1 60   ? -53.643 26.934  90.737  1.00 48.72 ? 58   LYS A N     1 
ATOM   325   C CA    . LYS A  1 60   ? -52.609 26.001  90.301  1.00 49.39 ? 58   LYS A CA    1 
ATOM   326   C C     . LYS A  1 60   ? -52.713 25.735  88.805  1.00 49.47 ? 58   LYS A C     1 
ATOM   327   O O     . LYS A  1 60   ? -51.703 25.739  88.092  1.00 47.13 ? 58   LYS A O     1 
ATOM   328   C CB    . LYS A  1 60   ? -52.717 24.694  91.089  1.00 50.86 ? 58   LYS A CB    1 
ATOM   329   C CG    . LYS A  1 60   ? -51.783 23.584  90.615  1.00 50.00 ? 58   LYS A CG    1 
ATOM   330   C CD    . LYS A  1 60   ? -50.318 23.948  90.807  1.00 52.85 ? 58   LYS A CD    1 
ATOM   331   C CE    . LYS A  1 60   ? -49.417 22.801  90.366  1.00 54.07 ? 58   LYS A CE    1 
ATOM   332   N NZ    . LYS A  1 60   ? -47.972 23.132  90.452  1.00 53.68 ? 58   LYS A NZ    1 
ATOM   333   N N     . GLU A  1 61   ? -53.935 25.534  88.306  1.00 43.24 ? 59   GLU A N     1 
ATOM   334   C CA    . GLU A  1 61   ? -54.122 25.230  86.892  1.00 47.35 ? 59   GLU A CA    1 
ATOM   335   C C     . GLU A  1 61   ? -53.649 26.380  86.007  1.00 46.72 ? 59   GLU A C     1 
ATOM   336   O O     . GLU A  1 61   ? -53.030 26.150  84.964  1.00 46.44 ? 59   GLU A O     1 
ATOM   337   C CB    . GLU A  1 61   ? -55.590 24.908  86.617  1.00 42.58 ? 59   GLU A CB    1 
ATOM   338   N N     . ILE A  1 62   ? -53.927 27.624  86.405  1.00 41.64 ? 60   ILE A N     1 
ATOM   339   C CA    . ILE A  1 62   ? -53.494 28.768  85.600  1.00 46.16 ? 60   ILE A CA    1 
ATOM   340   C C     . ILE A  1 62   ? -51.984 28.957  85.686  1.00 44.54 ? 60   ILE A C     1 
ATOM   341   O O     . ILE A  1 62   ? -51.333 29.312  84.693  1.00 43.85 ? 60   ILE A O     1 
ATOM   342   C CB    . ILE A  1 62   ? -54.244 30.043  86.022  1.00 44.23 ? 60   ILE A CB    1 
ATOM   343   C CG1   . ILE A  1 62   ? -55.629 30.063  85.390  1.00 44.67 ? 60   ILE A CG1   1 
ATOM   344   C CG2   . ILE A  1 62   ? -53.457 31.298  85.620  1.00 41.44 ? 60   ILE A CG2   1 
ATOM   345   C CD1   . ILE A  1 62   ? -56.402 31.304  85.702  1.00 43.76 ? 60   ILE A CD1   1 
ATOM   346   N N     . ARG A  1 63   ? -51.402 28.750  86.870  1.00 44.36 ? 61   ARG A N     1 
ATOM   347   C CA    . ARG A  1 63   ? -49.957 28.901  87.004  1.00 43.62 ? 61   ARG A CA    1 
ATOM   348   C C     . ARG A  1 63   ? -49.219 27.900  86.125  1.00 47.01 ? 61   ARG A C     1 
ATOM   349   O O     . ARG A  1 63   ? -48.248 28.256  85.446  1.00 43.83 ? 61   ARG A O     1 
ATOM   350   C CB    . ARG A  1 63   ? -49.547 28.759  88.467  1.00 45.49 ? 61   ARG A CB    1 
ATOM   351   C CG    . ARG A  1 63   ? -49.930 29.966  89.289  1.00 48.19 ? 61   ARG A CG    1 
ATOM   352   C CD    . ARG A  1 63   ? -49.473 29.872  90.722  1.00 51.94 ? 61   ARG A CD    1 
ATOM   353   N NE    . ARG A  1 63   ? -50.213 28.862  91.462  1.00 54.46 ? 61   ARG A NE    1 
ATOM   354   C CZ    . ARG A  1 63   ? -49.650 27.838  92.086  1.00 54.35 ? 61   ARG A CZ    1 
ATOM   355   N NH1   . ARG A  1 63   ? -48.337 27.676  92.099  1.00 53.64 ? 61   ARG A NH1   1 
ATOM   356   N NH2   . ARG A  1 63   ? -50.424 26.962  92.721  1.00 52.48 ? 61   ARG A NH2   1 
ATOM   357   N N     . ASP A  1 64   ? -49.678 26.645  86.114  1.00 45.97 ? 62   ASP A N     1 
ATOM   358   C CA    . ASP A  1 64   ? -49.115 25.648  85.208  1.00 48.20 ? 62   ASP A CA    1 
ATOM   359   C C     . ASP A  1 64   ? -49.298 26.066  83.754  1.00 47.72 ? 62   ASP A C     1 
ATOM   360   O O     . ASP A  1 64   ? -48.363 25.980  82.950  1.00 46.40 ? 62   ASP A O     1 
ATOM   361   C CB    . ASP A  1 64   ? -49.765 24.284  85.458  1.00 45.98 ? 62   ASP A CB    1 
ATOM   362   C CG    . ASP A  1 64   ? -49.346 23.670  86.784  1.00 51.05 ? 62   ASP A CG    1 
ATOM   363   O OD1   . ASP A  1 64   ? -48.466 24.247  87.455  1.00 48.55 ? 62   ASP A OD1   1 
ATOM   364   O OD2   . ASP A  1 64   ? -49.896 22.609  87.154  1.00 51.03 ? 62   ASP A OD2   1 
ATOM   365   N N     . ALA A  1 65   ? -50.506 26.520  83.402  1.00 42.82 ? 63   ALA A N     1 
ATOM   366   C CA    . ALA A  1 65   ? -50.774 26.959  82.034  1.00 43.63 ? 63   ALA A CA    1 
ATOM   367   C C     . ALA A  1 65   ? -49.896 28.140  81.644  1.00 45.67 ? 63   ALA A C     1 
ATOM   368   O O     . ALA A  1 65   ? -49.418 28.218  80.506  1.00 46.41 ? 63   ALA A O     1 
ATOM   369   C CB    . ALA A  1 65   ? -52.251 27.324  81.876  1.00 41.94 ? 63   ALA A CB    1 
ATOM   370   N N     . ALA A  1 66   ? -49.677 29.077  82.567  1.00 43.15 ? 64   ALA A N     1 
ATOM   371   C CA    . ALA A  1 66   ? -48.844 30.233  82.248  1.00 45.46 ? 64   ALA A CA    1 
ATOM   372   C C     . ALA A  1 66   ? -47.374 29.843  82.121  1.00 47.63 ? 64   ALA A C     1 
ATOM   373   O O     . ALA A  1 66   ? -46.670 30.341  81.235  1.00 44.75 ? 64   ALA A O     1 
ATOM   374   C CB    . ALA A  1 66   ? -49.022 31.321  83.308  1.00 43.87 ? 64   ALA A CB    1 
ATOM   375   N N     . ALA A  1 67   ? -46.892 28.970  83.011  1.00 42.01 ? 65   ALA A N     1 
ATOM   376   C CA    . ALA A  1 67   ? -45.527 28.462  82.900  1.00 48.63 ? 65   ALA A CA    1 
ATOM   377   C C     . ALA A  1 67   ? -45.299 27.789  81.553  1.00 47.75 ? 65   ALA A C     1 
ATOM   378   O O     . ALA A  1 67   ? -44.212 27.893  80.972  1.00 47.58 ? 65   ALA A O     1 
ATOM   379   C CB    . ALA A  1 67   ? -45.231 27.482  84.037  1.00 44.76 ? 65   ALA A CB    1 
ATOM   380   N N     . SER A  1 68   ? -46.315 27.102  81.037  1.00 46.23 ? 66   SER A N     1 
ATOM   381   C CA    . SER A  1 68   ? -46.165 26.440  79.748  1.00 48.03 ? 66   SER A CA    1 
ATOM   382   C C     . SER A  1 68   ? -46.108 27.451  78.611  1.00 46.22 ? 66   SER A C     1 
ATOM   383   O O     . SER A  1 68   ? -45.280 27.324  77.703  1.00 47.11 ? 66   SER A O     1 
ATOM   384   C CB    . SER A  1 68   ? -47.307 25.449  79.537  1.00 44.67 ? 66   SER A CB    1 
ATOM   385   O OG    . SER A  1 68   ? -47.217 24.834  78.266  1.00 49.32 ? 66   SER A OG    1 
ATOM   386   N N     . THR A  1 69   ? -46.976 28.464  78.641  1.00 45.06 ? 67   THR A N     1 
ATOM   387   C CA    . THR A  1 69   ? -46.945 29.476  77.589  1.00 45.55 ? 67   THR A CA    1 
ATOM   388   C C     . THR A  1 69   ? -45.639 30.262  77.620  1.00 42.22 ? 67   THR A C     1 
ATOM   389   O O     . THR A  1 69   ? -45.046 30.527  76.567  1.00 41.33 ? 67   THR A O     1 
ATOM   390   C CB    . THR A  1 69   ? -48.146 30.411  77.722  1.00 43.59 ? 67   THR A CB    1 
ATOM   391   O OG1   . THR A  1 69   ? -49.341 29.688  77.406  1.00 45.05 ? 67   THR A OG1   1 
ATOM   392   C CG2   . THR A  1 69   ? -48.016 31.597  76.778  1.00 37.30 ? 67   THR A CG2   1 
ATOM   393   N N     . ALA A  1 70   ? -45.161 30.618  78.819  1.00 43.87 ? 68   ALA A N     1 
ATOM   394   C CA    . ALA A  1 70   ? -43.913 31.371  78.929  1.00 44.83 ? 68   ALA A CA    1 
ATOM   395   C C     . ALA A  1 70   ? -42.722 30.540  78.468  1.00 48.55 ? 68   ALA A C     1 
ATOM   396   O O     . ALA A  1 70   ? -41.822 31.059  77.797  1.00 45.26 ? 68   ALA A O     1 
ATOM   397   C CB    . ALA A  1 70   ? -43.705 31.854  80.363  1.00 41.46 ? 68   ALA A CB    1 
ATOM   398   N N     . ARG A  1 71   ? -42.695 29.252  78.829  1.00 51.46 ? 69   ARG A N     1 
ATOM   399   C CA    . ARG A  1 71   ? -41.668 28.354  78.309  1.00 49.63 ? 69   ARG A CA    1 
ATOM   400   C C     . ARG A  1 71   ? -41.707 28.304  76.788  1.00 48.66 ? 69   ARG A C     1 
ATOM   401   O O     . ARG A  1 71   ? -40.659 28.383  76.133  1.00 52.82 ? 69   ARG A O     1 
ATOM   402   C CB    . ARG A  1 71   ? -41.840 26.952  78.903  1.00 49.05 ? 69   ARG A CB    1 
ATOM   403   C CG    . ARG A  1 71   ? -41.164 25.847  78.103  1.00 55.62 ? 69   ARG A CG    1 
ATOM   404   C CD    . ARG A  1 71   ? -41.074 24.543  78.888  1.00 54.21 ? 69   ARG A CD    1 
ATOM   405   N NE    . ARG A  1 71   ? -40.105 24.645  79.971  1.00 56.53 ? 69   ARG A NE    1 
ATOM   406   C CZ    . ARG A  1 71   ? -38.792 24.557  79.810  1.00 54.27 ? 69   ARG A CZ    1 
ATOM   407   N NH1   . ARG A  1 71   ? -38.254 24.334  78.621  1.00 55.58 ? 69   ARG A NH1   1 
ATOM   408   N NH2   . ARG A  1 71   ? -37.997 24.710  80.865  1.00 53.80 ? 69   ARG A NH2   1 
ATOM   409   N N     . LYS A  1 72   ? -42.907 28.207  76.206  1.00 46.12 ? 70   LYS A N     1 
ATOM   410   C CA    . LYS A  1 72   ? -43.020 28.157  74.750  1.00 47.45 ? 70   LYS A CA    1 
ATOM   411   C C     . LYS A  1 72   ? -42.495 29.438  74.106  1.00 51.86 ? 70   LYS A C     1 
ATOM   412   O O     . LYS A  1 72   ? -41.757 29.386  73.116  1.00 50.74 ? 70   LYS A O     1 
ATOM   413   C CB    . LYS A  1 72   ? -44.466 27.908  74.330  1.00 44.68 ? 70   LYS A CB    1 
ATOM   414   C CG    . LYS A  1 72   ? -44.622 27.838  72.812  1.00 50.09 ? 70   LYS A CG    1 
ATOM   415   C CD    . LYS A  1 72   ? -46.041 28.090  72.344  1.00 49.99 ? 70   LYS A CD    1 
ATOM   416   C CE    . LYS A  1 72   ? -46.844 26.812  72.238  1.00 57.07 ? 70   LYS A CE    1 
ATOM   417   N NZ    . LYS A  1 72   ? -48.005 26.986  71.318  1.00 58.44 ? 70   LYS A NZ    1 
ATOM   418   N N     . LEU A  1 73   ? -42.871 30.602  74.651  1.00 48.18 ? 71   LEU A N     1 
ATOM   419   C CA    . LEU A  1 73   ? -42.392 31.867  74.096  1.00 44.64 ? 71   LEU A CA    1 
ATOM   420   C C     . LEU A  1 73   ? -40.876 31.984  74.209  1.00 49.55 ? 71   LEU A C     1 
ATOM   421   O O     . LEU A  1 73   ? -40.209 32.467  73.285  1.00 46.94 ? 71   LEU A O     1 
ATOM   422   C CB    . LEU A  1 73   ? -43.057 33.044  74.807  1.00 43.32 ? 71   LEU A CB    1 
ATOM   423   C CG    . LEU A  1 73   ? -44.574 33.162  74.734  1.00 40.77 ? 71   LEU A CG    1 
ATOM   424   C CD1   . LEU A  1 73   ? -45.031 34.331  75.603  1.00 41.55 ? 71   LEU A CD1   1 
ATOM   425   C CD2   . LEU A  1 73   ? -45.002 33.361  73.302  1.00 40.30 ? 71   LEU A CD2   1 
ATOM   426   N N     . ILE A  1 74   ? -40.316 31.561  75.343  1.00 45.63 ? 72   ILE A N     1 
ATOM   427   C CA    . ILE A  1 74   ? -38.876 31.653  75.534  1.00 49.91 ? 72   ILE A CA    1 
ATOM   428   C C     . ILE A  1 74   ? -38.143 30.656  74.646  1.00 50.09 ? 72   ILE A C     1 
ATOM   429   O O     . ILE A  1 74   ? -36.995 30.896  74.254  1.00 48.66 ? 72   ILE A O     1 
ATOM   430   C CB    . ILE A  1 74   ? -38.553 31.475  77.028  1.00 46.33 ? 72   ILE A CB    1 
ATOM   431   C CG1   . ILE A  1 74   ? -39.164 32.645  77.807  1.00 47.39 ? 72   ILE A CG1   1 
ATOM   432   C CG2   . ILE A  1 74   ? -37.045 31.387  77.271  1.00 49.52 ? 72   ILE A CG2   1 
ATOM   433   C CD1   . ILE A  1 74   ? -39.090 32.503  79.306  1.00 50.89 ? 72   ILE A CD1   1 
ATOM   434   N N     . GLU A  1 75   ? -38.794 29.547  74.279  1.00 51.65 ? 73   GLU A N     1 
ATOM   435   C CA    . GLU A  1 75   ? -38.170 28.609  73.349  1.00 54.17 ? 73   GLU A CA    1 
ATOM   436   C C     . GLU A  1 75   ? -37.945 29.256  71.987  1.00 55.62 ? 73   GLU A C     1 
ATOM   437   O O     . GLU A  1 75   ? -36.872 29.105  71.390  1.00 53.08 ? 73   GLU A O     1 
ATOM   438   C CB    . GLU A  1 75   ? -39.020 27.346  73.210  1.00 53.70 ? 73   GLU A CB    1 
ATOM   439   N N     . ALA A  1 76   ? -38.940 30.000  71.488  1.00 52.54 ? 74   ALA A N     1 
ATOM   440   C CA    . ALA A  1 76   ? -38.799 30.649  70.185  1.00 52.07 ? 74   ALA A CA    1 
ATOM   441   C C     . ALA A  1 76   ? -37.821 31.818  70.242  1.00 49.31 ? 74   ALA A C     1 
ATOM   442   O O     . ALA A  1 76   ? -37.058 32.043  69.297  1.00 54.99 ? 74   ALA A O     1 
ATOM   443   C CB    . ALA A  1 76   ? -40.163 31.112  69.681  1.00 51.66 ? 74   ALA A CB    1 
ATOM   444   N N     . LEU A  1 77   ? -37.830 32.575  71.341  1.00 48.68 ? 75   LEU A N     1 
ATOM   445   C CA    . LEU A  1 77   ? -36.903 33.697  71.476  1.00 48.93 ? 75   LEU A CA    1 
ATOM   446   C C     . LEU A  1 77   ? -35.451 33.233  71.424  1.00 51.14 ? 75   LEU A C     1 
ATOM   447   O O     . LEU A  1 77   ? -34.581 33.935  70.892  1.00 52.80 ? 75   LEU A O     1 
ATOM   448   C CB    . LEU A  1 77   ? -37.167 34.441  72.782  1.00 46.86 ? 75   LEU A CB    1 
ATOM   449   C CG    . LEU A  1 77   ? -38.263 35.502  72.762  1.00 42.85 ? 75   LEU A CG    1 
ATOM   450   C CD1   . LEU A  1 77   ? -38.425 36.062  74.156  1.00 43.68 ? 75   LEU A CD1   1 
ATOM   451   C CD2   . LEU A  1 77   ? -37.907 36.596  71.781  1.00 45.46 ? 75   LEU A CD2   1 
ATOM   452   N N     . ARG A  1 78   ? -35.166 32.066  71.983  1.00 51.27 ? 76   ARG A N     1 
ATOM   453   C CA    . ARG A  1 78   ? -33.802 31.565  71.969  1.00 52.80 ? 76   ARG A CA    1 
ATOM   454   C C     . ARG A  1 78   ? -33.461 30.818  70.688  1.00 52.54 ? 76   ARG A C     1 
ATOM   455   O O     . ARG A  1 78   ? -32.277 30.593  70.421  1.00 54.73 ? 76   ARG A O     1 
ATOM   456   C CB    . ARG A  1 78   ? -33.561 30.690  73.202  1.00 47.45 ? 76   ARG A CB    1 
ATOM   457   C CG    . ARG A  1 78   ? -33.187 31.534  74.416  1.00 50.24 ? 76   ARG A CG    1 
ATOM   458   C CD    . ARG A  1 78   ? -33.076 30.740  75.697  1.00 45.55 ? 76   ARG A CD    1 
ATOM   459   N NE    . ARG A  1 78   ? -32.452 31.553  76.733  1.00 48.73 ? 76   ARG A NE    1 
ATOM   460   C CZ    . ARG A  1 78   ? -32.113 31.115  77.937  1.00 49.71 ? 76   ARG A CZ    1 
ATOM   461   N NH1   . ARG A  1 78   ? -32.347 29.867  78.311  1.00 51.63 ? 76   ARG A NH1   1 
ATOM   462   N NH2   . ARG A  1 78   ? -31.521 31.951  78.787  1.00 51.14 ? 76   ARG A NH2   1 
ATOM   463   N N     . GLY A  1 79   ? -34.458 30.463  69.879  1.00 52.96 ? 77   GLY A N     1 
ATOM   464   C CA    . GLY A  1 79   ? -34.216 29.865  68.581  1.00 54.45 ? 77   GLY A CA    1 
ATOM   465   C C     . GLY A  1 79   ? -34.372 30.851  67.441  1.00 57.37 ? 77   GLY A C     1 
ATOM   466   O O     . GLY A  1 79   ? -34.808 30.484  66.346  1.00 58.50 ? 77   GLY A O     1 
ATOM   467   N N     . LYS A  1 80   ? -34.018 32.110  67.685  1.00 62.13 ? 78   LYS A N     1 
ATOM   468   C CA    . LYS A  1 80   ? -34.136 33.151  66.668  1.00 61.55 ? 78   LYS A CA    1 
ATOM   469   C C     . LYS A  1 80   ? -33.243 34.345  66.998  1.00 58.40 ? 78   LYS A C     1 
ATOM   470   O O     . LYS A  1 80   ? -32.042 34.197  67.217  1.00 62.03 ? 78   LYS A O     1 
ATOM   471   C CB    . LYS A  1 80   ? -35.595 33.602  66.531  1.00 55.33 ? 78   LYS A CB    1 
ATOM   472   N N     . GLY A  1 85   ? -25.027 41.697  65.761  1.00 50.26 ? 83   GLY A N     1 
ATOM   473   C CA    . GLY A  1 85   ? -24.844 42.870  64.922  1.00 46.37 ? 83   GLY A CA    1 
ATOM   474   C C     . GLY A  1 85   ? -23.481 43.495  65.153  1.00 42.70 ? 83   GLY A C     1 
ATOM   475   O O     . GLY A  1 85   ? -22.536 43.266  64.397  1.00 43.62 ? 83   GLY A O     1 
ATOM   476   N N     . VAL A  1 86   ? -23.374 44.294  66.216  1.00 42.29 ? 84   VAL A N     1 
ATOM   477   C CA    . VAL A  1 86   ? -22.061 44.762  66.640  1.00 43.35 ? 84   VAL A CA    1 
ATOM   478   C C     . VAL A  1 86   ? -21.176 43.572  66.983  1.00 40.61 ? 84   VAL A C     1 
ATOM   479   O O     . VAL A  1 86   ? -19.952 43.622  66.806  1.00 39.39 ? 84   VAL A O     1 
ATOM   480   C CB    . VAL A  1 86   ? -22.195 45.742  67.824  1.00 44.02 ? 84   VAL A CB    1 
ATOM   481   N N     . GLU A  1 87   ? -21.779 42.474  67.447  1.00 43.21 ? 85   GLU A N     1 
ATOM   482   C CA    . GLU A  1 87   ? -21.000 41.295  67.811  1.00 42.71 ? 85   GLU A CA    1 
ATOM   483   C C     . GLU A  1 87   ? -20.369 40.647  66.586  1.00 43.45 ? 85   GLU A C     1 
ATOM   484   O O     . GLU A  1 87   ? -19.252 40.119  66.663  1.00 40.24 ? 85   GLU A O     1 
ATOM   485   C CB    . GLU A  1 87   ? -21.881 40.291  68.557  1.00 48.13 ? 85   GLU A CB    1 
ATOM   486   N N     . GLY A  1 88   ? -21.064 40.667  65.447  1.00 39.58 ? 86   GLY A N     1 
ATOM   487   C CA    . GLY A  1 88   ? -20.481 40.092  64.247  1.00 40.54 ? 86   GLY A CA    1 
ATOM   488   C C     . GLY A  1 88   ? -19.357 40.939  63.691  1.00 39.55 ? 86   GLY A C     1 
ATOM   489   O O     . GLY A  1 88   ? -18.424 40.417  63.076  1.00 37.31 ? 86   GLY A O     1 
ATOM   490   N N     . LEU A  1 89   ? -19.435 42.255  63.893  1.00 41.02 ? 87   LEU A N     1 
ATOM   491   C CA    . LEU A  1 89   ? -18.348 43.141  63.503  1.00 38.98 ? 87   LEU A CA    1 
ATOM   492   C C     . LEU A  1 89   ? -17.121 42.897  64.377  1.00 36.17 ? 87   LEU A C     1 
ATOM   493   O O     . LEU A  1 89   ? -16.015 42.685  63.869  1.00 34.97 ? 87   LEU A O     1 
ATOM   494   C CB    . LEU A  1 89   ? -18.827 44.591  63.604  1.00 39.53 ? 87   LEU A CB    1 
ATOM   495   C CG    . LEU A  1 89   ? -18.197 45.713  62.783  1.00 40.02 ? 87   LEU A CG    1 
ATOM   496   C CD1   . LEU A  1 89   ? -18.900 47.015  63.133  1.00 40.25 ? 87   LEU A CD1   1 
ATOM   497   C CD2   . LEU A  1 89   ? -16.712 45.830  63.071  1.00 39.42 ? 87   LEU A CD2   1 
ATOM   498   N N     . VAL A  1 90   ? -17.309 42.910  65.701  1.00 35.30 ? 88   VAL A N     1 
ATOM   499   C CA    . VAL A  1 90   ? -16.216 42.609  66.626  1.00 35.48 ? 88   VAL A CA    1 
ATOM   500   C C     . VAL A  1 90   ? -15.547 41.295  66.251  1.00 37.65 ? 88   VAL A C     1 
ATOM   501   O O     . VAL A  1 90   ? -14.314 41.188  66.254  1.00 37.50 ? 88   VAL A O     1 
ATOM   502   C CB    . VAL A  1 90   ? -16.739 42.586  68.073  1.00 33.61 ? 88   VAL A CB    1 
ATOM   503   C CG1   . VAL A  1 90   ? -15.700 42.016  69.004  1.00 36.93 ? 88   VAL A CG1   1 
ATOM   504   C CG2   . VAL A  1 90   ? -17.137 43.985  68.500  1.00 35.02 ? 88   VAL A CG2   1 
ATOM   505   N N     . GLN A  1 91   ? -16.343 40.285  65.889  1.00 38.36 ? 89   GLN A N     1 
ATOM   506   C CA    . GLN A  1 91   ? -15.774 38.995  65.500  1.00 38.19 ? 89   GLN A CA    1 
ATOM   507   C C     . GLN A  1 91   ? -15.008 39.093  64.185  1.00 39.40 ? 89   GLN A C     1 
ATOM   508   O O     . GLN A  1 91   ? -13.883 38.586  64.067  1.00 39.41 ? 89   GLN A O     1 
ATOM   509   C CB    . GLN A  1 91   ? -16.876 37.939  65.399  1.00 42.18 ? 89   GLN A CB    1 
ATOM   510   N N     . GLU A  1 92   ? -15.596 39.743  63.181  1.00 38.05 ? 90   GLU A N     1 
ATOM   511   C CA    . GLU A  1 92   ? -14.992 39.717  61.853  1.00 41.63 ? 90   GLU A CA    1 
ATOM   512   C C     . GLU A  1 92   ? -13.618 40.373  61.856  1.00 38.98 ? 90   GLU A C     1 
ATOM   513   O O     . GLU A  1 92   ? -12.698 39.915  61.170  1.00 38.53 ? 90   GLU A O     1 
ATOM   514   C CB    . GLU A  1 92   ? -15.909 40.394  60.836  1.00 39.11 ? 90   GLU A CB    1 
ATOM   515   C CG    . GLU A  1 92   ? -15.358 40.321  59.412  1.00 46.16 ? 90   GLU A CG    1 
ATOM   516   C CD    . GLU A  1 92   ? -16.279 40.954  58.385  1.00 49.92 ? 90   GLU A CD    1 
ATOM   517   O OE1   . GLU A  1 92   ? -17.395 41.378  58.766  1.00 45.46 ? 90   GLU A OE1   1 
ATOM   518   O OE2   . GLU A  1 92   ? -15.877 41.028  57.201  1.00 48.22 ? 90   GLU A OE2   1 
ATOM   519   N N     . TYR A  1 93   ? -13.443 41.425  62.645  1.00 38.31 ? 91   TYR A N     1 
ATOM   520   C CA    . TYR A  1 93   ? -12.190 42.160  62.639  1.00 34.18 ? 91   TYR A CA    1 
ATOM   521   C C     . TYR A  1 93   ? -11.380 41.962  63.913  1.00 32.39 ? 91   TYR A C     1 
ATOM   522   O O     . TYR A  1 93   ? -10.427 42.708  64.140  1.00 32.80 ? 91   TYR A O     1 
ATOM   523   C CB    . TYR A  1 93   ? -12.470 43.642  62.391  1.00 34.11 ? 91   TYR A CB    1 
ATOM   524   C CG    . TYR A  1 93   ? -12.955 43.890  60.987  1.00 36.85 ? 91   TYR A CG    1 
ATOM   525   C CD1   . TYR A  1 93   ? -14.307 43.807  60.668  1.00 38.10 ? 91   TYR A CD1   1 
ATOM   526   C CD2   . TYR A  1 93   ? -12.055 44.164  59.966  1.00 37.92 ? 91   TYR A CD2   1 
ATOM   527   C CE1   . TYR A  1 93   ? -14.748 44.014  59.371  1.00 40.78 ? 91   TYR A CE1   1 
ATOM   528   C CE2   . TYR A  1 93   ? -12.485 44.370  58.665  1.00 39.55 ? 91   TYR A CE2   1 
ATOM   529   C CZ    . TYR A  1 93   ? -13.824 44.298  58.374  1.00 38.98 ? 91   TYR A CZ    1 
ATOM   530   O OH    . TYR A  1 93   ? -14.251 44.500  57.082  1.00 41.58 ? 91   TYR A OH    1 
ATOM   531   N N     . SER A  1 94   ? -11.735 40.976  64.742  1.00 33.28 ? 92   SER A N     1 
ATOM   532   C CA    . SER A  1 94   ? -10.985 40.652  65.957  1.00 33.34 ? 92   SER A CA    1 
ATOM   533   C C     . SER A  1 94   ? -10.763 41.899  66.817  1.00 32.23 ? 92   SER A C     1 
ATOM   534   O O     . SER A  1 94   ? -9.652  42.181  67.283  1.00 30.26 ? 92   SER A O     1 
ATOM   535   C CB    . SER A  1 94   ? -9.650  39.981  65.612  1.00 33.23 ? 92   SER A CB    1 
ATOM   536   O OG    . SER A  1 94   ? -9.846  38.887  64.722  1.00 38.07 ? 92   SER A OG    1 
ATOM   537   N N     . LEU A  1 95   ? -11.837 42.660  67.008  1.00 29.65 ? 93   LEU A N     1 
ATOM   538   C CA    . LEU A  1 95   ? -11.776 43.879  67.801  1.00 31.75 ? 93   LEU A CA    1 
ATOM   539   C C     . LEU A  1 95   ? -11.799 43.552  69.284  1.00 27.78 ? 93   LEU A C     1 
ATOM   540   O O     . LEU A  1 95   ? -12.530 42.661  69.721  1.00 31.02 ? 93   LEU A O     1 
ATOM   541   C CB    . LEU A  1 95   ? -12.959 44.796  67.471  1.00 30.99 ? 93   LEU A CB    1 
ATOM   542   C CG    . LEU A  1 95   ? -13.099 45.200  66.002  1.00 29.70 ? 93   LEU A CG    1 
ATOM   543   C CD1   . LEU A  1 95   ? -14.314 46.116  65.812  1.00 34.44 ? 93   LEU A CD1   1 
ATOM   544   C CD2   . LEU A  1 95   ? -11.821 45.857  65.488  1.00 29.05 ? 93   LEU A CD2   1 
ATOM   545   N N     . SER A  1 96   ? -11.004 44.285  70.056  1.00 26.44 ? 94   SER A N     1 
ATOM   546   C CA    . SER A  1 96   ? -11.196 44.322  71.500  1.00 28.91 ? 94   SER A CA    1 
ATOM   547   C C     . SER A  1 96   ? -12.437 45.155  71.838  1.00 27.34 ? 94   SER A C     1 
ATOM   548   O O     . SER A  1 96   ? -12.982 45.860  70.992  1.00 25.33 ? 94   SER A O     1 
ATOM   549   C CB    . SER A  1 96   ? -9.975  44.927  72.178  1.00 28.13 ? 94   SER A CB    1 
ATOM   550   O OG    . SER A  1 96   ? -9.858  46.286  71.785  1.00 25.72 ? 94   SER A OG    1 
ATOM   551   N N     . SER A  1 97   ? -12.856 45.111  73.107  1.00 25.35 ? 95   SER A N     1 
ATOM   552   C CA    . SER A  1 97   ? -13.997 45.922  73.524  1.00 29.60 ? 95   SER A CA    1 
ATOM   553   C C     . SER A  1 97   ? -13.735 47.402  73.290  1.00 27.21 ? 95   SER A C     1 
ATOM   554   O O     . SER A  1 97   ? -14.599 48.122  72.772  1.00 24.81 ? 95   SER A O     1 
ATOM   555   C CB    . SER A  1 97   ? -14.325 45.662  74.992  1.00 31.81 ? 95   SER A CB    1 
ATOM   556   O OG    . SER A  1 97   ? -14.839 44.355  75.128  1.00 42.07 ? 95   SER A OG    1 
ATOM   557   N N     . GLN A  1 98   ? -12.544 47.878  73.662  1.00 21.63 ? 96   GLN A N     1 
ATOM   558   C CA    . GLN A  1 98   ? -12.243 49.288  73.459  1.00 21.98 ? 96   GLN A CA    1 
ATOM   559   C C     . GLN A  1 98   ? -12.200 49.636  71.975  1.00 22.47 ? 96   GLN A C     1 
ATOM   560   O O     . GLN A  1 98   ? -12.579 50.745  71.588  1.00 22.09 ? 96   GLN A O     1 
ATOM   561   C CB    . GLN A  1 98   ? -10.927 49.650  74.149  1.00 24.56 ? 96   GLN A CB    1 
ATOM   562   C CG    . GLN A  1 98   ? -11.049 49.727  75.685  1.00 25.20 ? 96   GLN A CG    1 
ATOM   563   C CD    . GLN A  1 98   ? -11.987 50.838  76.136  1.00 20.23 ? 96   GLN A CD    1 
ATOM   564   O OE1   . GLN A  1 98   ? -13.204 50.661  76.184  1.00 25.87 ? 96   GLN A OE1   1 
ATOM   565   N NE2   . GLN A  1 98   ? -11.428 51.996  76.448  1.00 24.83 ? 96   GLN A NE2   1 
ATOM   566   N N     . GLU A  1 99   ? -11.721 48.720  71.129  1.00 24.12 ? 97   GLU A N     1 
ATOM   567   C CA    . GLU A  1 99   ? -11.737 49.005  69.694  1.00 22.69 ? 97   GLU A CA    1 
ATOM   568   C C     . GLU A  1 99   ? -13.160 49.096  69.162  1.00 24.24 ? 97   GLU A C     1 
ATOM   569   O O     . GLU A  1 99   ? -13.468 49.985  68.364  1.00 25.55 ? 97   GLU A O     1 
ATOM   570   C CB    . GLU A  1 99   ? -10.931 47.950  68.918  1.00 21.87 ? 97   GLU A CB    1 
ATOM   571   C CG    . GLU A  1 99   ? -9.431  48.090  69.191  1.00 21.45 ? 97   GLU A CG    1 
ATOM   572   C CD    . GLU A  1 99   ? -8.616  46.930  68.643  1.00 24.65 ? 97   GLU A CD    1 
ATOM   573   O OE1   . GLU A  1 99   ? -9.211  45.950  68.147  1.00 27.31 ? 97   GLU A OE1   1 
ATOM   574   O OE2   . GLU A  1 99   ? -7.378  47.009  68.743  1.00 24.92 ? 97   GLU A OE2   1 
ATOM   575   N N     . GLY A  1 100  ? -14.041 48.200  69.598  1.00 23.76 ? 98   GLY A N     1 
ATOM   576   C CA    . GLY A  1 100  ? -15.427 48.275  69.165  1.00 25.56 ? 98   GLY A CA    1 
ATOM   577   C C     . GLY A  1 100  ? -16.089 49.578  69.576  1.00 24.65 ? 98   GLY A C     1 
ATOM   578   O O     . GLY A  1 100  ? -16.788 50.210  68.779  1.00 23.28 ? 98   GLY A O     1 
ATOM   579   N N     . VAL A  1 101  ? -15.878 50.001  70.825  1.00 20.92 ? 99   VAL A N     1 
ATOM   580   C CA    . VAL A  1 101  ? -16.423 51.284  71.261  1.00 22.48 ? 99   VAL A CA    1 
ATOM   581   C C     . VAL A  1 101  ? -15.838 52.425  70.432  1.00 24.09 ? 99   VAL A C     1 
ATOM   582   O O     . VAL A  1 101  ? -16.569 53.309  69.966  1.00 24.33 ? 99   VAL A O     1 
ATOM   583   C CB    . VAL A  1 101  ? -16.166 51.496  72.761  1.00 22.94 ? 99   VAL A CB    1 
ATOM   584   C CG1   . VAL A  1 101  ? -16.611 52.882  73.158  1.00 20.70 ? 99   VAL A CG1   1 
ATOM   585   C CG2   . VAL A  1 101  ? -16.921 50.431  73.577  1.00 26.25 ? 99   VAL A CG2   1 
ATOM   586   N N     . ALA A  1 102  ? -14.511 52.418  70.228  1.00 21.55 ? 100  ALA A N     1 
ATOM   587   C CA    . ALA A  1 102  ? -13.881 53.516  69.501  1.00 22.64 ? 100  ALA A CA    1 
ATOM   588   C C     . ALA A  1 102  ? -14.394 53.573  68.078  1.00 21.73 ? 100  ALA A C     1 
ATOM   589   O O     . ALA A  1 102  ? -14.633 54.660  67.541  1.00 24.17 ? 100  ALA A O     1 
ATOM   590   C CB    . ALA A  1 102  ? -12.350 53.380  69.499  1.00 20.61 ? 100  ALA A CB    1 
ATOM   591   N N     . LEU A  1 103  ? -14.561 52.406  67.453  1.00 24.66 ? 101  LEU A N     1 
ATOM   592   C CA    . LEU A  1 103  ? -15.080 52.356  66.091  1.00 24.88 ? 101  LEU A CA    1 
ATOM   593   C C     . LEU A  1 103  ? -16.479 52.950  66.026  1.00 25.00 ? 101  LEU A C     1 
ATOM   594   O O     . LEU A  1 103  ? -16.778 53.774  65.156  1.00 25.04 ? 101  LEU A O     1 
ATOM   595   C CB    . LEU A  1 103  ? -15.082 50.914  65.575  1.00 26.14 ? 101  LEU A CB    1 
ATOM   596   C CG    . LEU A  1 103  ? -15.634 50.677  64.163  1.00 24.71 ? 101  LEU A CG    1 
ATOM   597   C CD1   . LEU A  1 103  ? -14.768 51.336  63.097  1.00 25.67 ? 101  LEU A CD1   1 
ATOM   598   C CD2   . LEU A  1 103  ? -15.776 49.198  63.910  1.00 27.64 ? 101  LEU A CD2   1 
ATOM   599   N N     . MET A  1 104  ? -17.352 52.559  66.954  1.00 22.14 ? 102  MET A N     1 
ATOM   600   C CA    . MET A  1 104  ? -18.703 53.120  66.934  1.00 25.34 ? 102  MET A CA    1 
ATOM   601   C C     . MET A  1 104  ? -18.683 54.628  67.162  1.00 24.72 ? 102  MET A C     1 
ATOM   602   O O     . MET A  1 104  ? -19.515 55.350  66.593  1.00 25.06 ? 102  MET A O     1 
ATOM   603   C CB    . MET A  1 104  ? -19.582 52.411  67.961  1.00 21.34 ? 102  MET A CB    1 
ATOM   604   C CG    . MET A  1 104  ? -19.743 50.919  67.668  1.00 23.18 ? 102  MET A CG    1 
ATOM   605   S SD    . MET A  1 104  ? -20.243 50.611  65.947  1.00 33.59 ? 102  MET A SD    1 
ATOM   606   C CE    . MET A  1 104  ? -21.846 51.378  65.929  1.00 31.00 ? 102  MET A CE    1 
ATOM   607   N N     . CYS A  1 105  ? -17.734 55.129  67.962  1.00 22.62 ? 103  CYS A N     1 
ATOM   608   C CA    . CYS A  1 105  ? -17.622 56.575  68.140  1.00 23.98 ? 103  CYS A CA    1 
ATOM   609   C C     . CYS A  1 105  ? -17.160 57.254  66.859  1.00 27.50 ? 103  CYS A C     1 
ATOM   610   O O     . CYS A  1 105  ? -17.659 58.327  66.504  1.00 28.16 ? 103  CYS A O     1 
ATOM   611   C CB    . CYS A  1 105  ? -16.657 56.911  69.268  1.00 22.21 ? 103  CYS A CB    1 
ATOM   612   S SG    . CYS A  1 105  ? -17.257 56.478  70.890  1.00 25.46 ? 103  CYS A SG    1 
ATOM   613   N N     . LEU A  1 106  ? -16.179 56.667  66.172  1.00 23.42 ? 104  LEU A N     1 
ATOM   614   C CA    . LEU A  1 106  ? -15.782 57.194  64.870  1.00 26.00 ? 104  LEU A CA    1 
ATOM   615   C C     . LEU A  1 106  ? -16.960 57.198  63.899  1.00 26.72 ? 104  LEU A C     1 
ATOM   616   O O     . LEU A  1 106  ? -17.202 58.197  63.208  1.00 28.62 ? 104  LEU A O     1 
ATOM   617   C CB    . LEU A  1 106  ? -14.616 56.381  64.304  1.00 27.29 ? 104  LEU A CB    1 
ATOM   618   C CG    . LEU A  1 106  ? -14.244 56.734  62.858  1.00 27.80 ? 104  LEU A CG    1 
ATOM   619   C CD1   . LEU A  1 106  ? -13.680 58.142  62.792  1.00 30.60 ? 104  LEU A CD1   1 
ATOM   620   C CD2   . LEU A  1 106  ? -13.267 55.719  62.305  1.00 27.27 ? 104  LEU A CD2   1 
ATOM   621   N N     . ALA A  1 107  ? -17.697 56.084  63.824  1.00 23.66 ? 105  ALA A N     1 
ATOM   622   C CA    . ALA A  1 107  ? -18.856 56.006  62.936  1.00 27.36 ? 105  ALA A CA    1 
ATOM   623   C C     . ALA A  1 107  ? -19.860 57.110  63.238  1.00 31.39 ? 105  ALA A C     1 
ATOM   624   O O     . ALA A  1 107  ? -20.348 57.788  62.327  1.00 29.54 ? 105  ALA A O     1 
ATOM   625   C CB    . ALA A  1 107  ? -19.525 54.634  63.050  1.00 25.70 ? 105  ALA A CB    1 
ATOM   626   N N     . GLU A  1 108  ? -20.197 57.291  64.521  1.00 27.48 ? 106  GLU A N     1 
ATOM   627   C CA    . GLU A  1 108  ? -21.098 58.370  64.909  1.00 28.14 ? 106  GLU A CA    1 
ATOM   628   C C     . GLU A  1 108  ? -20.629 59.711  64.349  1.00 33.90 ? 106  GLU A C     1 
ATOM   629   O O     . GLU A  1 108  ? -21.432 60.478  63.795  1.00 33.46 ? 106  GLU A O     1 
ATOM   630   C CB    . GLU A  1 108  ? -21.203 58.419  66.439  1.00 28.95 ? 106  GLU A CB    1 
ATOM   631   C CG    . GLU A  1 108  ? -22.116 59.516  66.990  1.00 28.48 ? 106  GLU A CG    1 
ATOM   632   C CD    . GLU A  1 108  ? -21.772 59.907  68.433  1.00 36.08 ? 106  GLU A CD    1 
ATOM   633   O OE1   . GLU A  1 108  ? -21.238 59.054  69.187  1.00 33.79 ? 106  GLU A OE1   1 
ATOM   634   O OE2   . GLU A  1 108  ? -22.018 61.082  68.805  1.00 37.09 ? 106  GLU A OE2   1 
ATOM   635   N N     . ALA A  1 109  ? -19.320 59.992  64.447  1.00 29.00 ? 107  ALA A N     1 
ATOM   636   C CA    . ALA A  1 109  ? -18.791 61.289  64.021  1.00 31.68 ? 107  ALA A CA    1 
ATOM   637   C C     . ALA A  1 109  ? -18.833 61.437  62.508  1.00 35.30 ? 107  ALA A C     1 
ATOM   638   O O     . ALA A  1 109  ? -19.212 62.496  61.992  1.00 38.53 ? 107  ALA A O     1 
ATOM   639   C CB    . ALA A  1 109  ? -17.363 61.474  64.530  1.00 33.48 ? 107  ALA A CB    1 
ATOM   640   N N     . LEU A  1 110  ? -18.422 60.394  61.782  1.00 31.52 ? 108  LEU A N     1 
ATOM   641   C CA    . LEU A  1 110  ? -18.585 60.384  60.332  1.00 35.33 ? 108  LEU A CA    1 
ATOM   642   C C     . LEU A  1 110  ? -20.039 60.606  59.933  1.00 37.16 ? 108  LEU A C     1 
ATOM   643   O O     . LEU A  1 110  ? -20.317 61.255  58.919  1.00 38.79 ? 108  LEU A O     1 
ATOM   644   C CB    . LEU A  1 110  ? -18.075 59.064  59.754  1.00 33.41 ? 108  LEU A CB    1 
ATOM   645   C CG    . LEU A  1 110  ? -16.556 58.923  59.841  1.00 33.58 ? 108  LEU A CG    1 
ATOM   646   C CD1   . LEU A  1 110  ? -16.124 57.509  59.501  1.00 32.40 ? 108  LEU A CD1   1 
ATOM   647   C CD2   . LEU A  1 110  ? -15.891 59.919  58.910  1.00 37.35 ? 108  LEU A CD2   1 
ATOM   648   N N     . LEU A  1 111  ? -20.983 60.065  60.707  1.00 39.73 ? 109  LEU A N     1 
ATOM   649   C CA    . LEU A  1 111  ? -22.387 60.235  60.352  1.00 40.25 ? 109  LEU A CA    1 
ATOM   650   C C     . LEU A  1 111  ? -22.878 61.656  60.597  1.00 43.16 ? 109  LEU A C     1 
ATOM   651   O O     . LEU A  1 111  ? -23.941 62.024  60.088  1.00 46.20 ? 109  LEU A O     1 
ATOM   652   C CB    . LEU A  1 111  ? -23.251 59.224  61.112  1.00 36.83 ? 109  LEU A CB    1 
ATOM   653   C CG    . LEU A  1 111  ? -23.093 57.803  60.555  1.00 33.00 ? 109  LEU A CG    1 
ATOM   654   C CD1   . LEU A  1 111  ? -23.922 56.809  61.307  1.00 33.54 ? 109  LEU A CD1   1 
ATOM   655   C CD2   . LEU A  1 111  ? -23.432 57.779  59.076  1.00 36.13 ? 109  LEU A CD2   1 
ATOM   656   N N     . ARG A  1 112  ? -22.136 62.462  61.360  1.00 41.94 ? 110  ARG A N     1 
ATOM   657   C CA    . ARG A  1 112  ? -22.471 63.876  61.484  1.00 43.67 ? 110  ARG A CA    1 
ATOM   658   C C     . ARG A  1 112  ? -22.106 64.668  60.239  1.00 46.48 ? 110  ARG A C     1 
ATOM   659   O O     . ARG A  1 112  ? -22.450 65.851  60.153  1.00 47.49 ? 110  ARG A O     1 
ATOM   660   C CB    . ARG A  1 112  ? -21.776 64.478  62.703  1.00 45.63 ? 110  ARG A CB    1 
ATOM   661   C CG    . ARG A  1 112  ? -22.209 63.858  64.013  1.00 41.99 ? 110  ARG A CG    1 
ATOM   662   C CD    . ARG A  1 112  ? -21.152 64.051  65.075  1.00 47.50 ? 110  ARG A CD    1 
ATOM   663   N NE    . ARG A  1 112  ? -20.959 65.457  65.400  1.00 49.87 ? 110  ARG A NE    1 
ATOM   664   C CZ    . ARG A  1 112  ? -21.624 66.101  66.349  1.00 55.20 ? 110  ARG A CZ    1 
ATOM   665   N NH1   . ARG A  1 112  ? -22.540 65.493  67.085  1.00 56.18 ? 110  ARG A NH1   1 
ATOM   666   N NH2   . ARG A  1 112  ? -21.366 67.388  66.564  1.00 56.30 ? 110  ARG A NH2   1 
ATOM   667   N N     . ILE A  1 113  ? -21.413 64.054  59.287  1.00 47.97 ? 111  ILE A N     1 
ATOM   668   C CA    . ILE A  1 113  ? -21.134 64.677  57.996  1.00 49.84 ? 111  ILE A CA    1 
ATOM   669   C C     . ILE A  1 113  ? -22.342 64.439  57.101  1.00 49.64 ? 111  ILE A C     1 
ATOM   670   O O     . ILE A  1 113  ? -22.673 63.282  56.798  1.00 49.02 ? 111  ILE A O     1 
ATOM   671   C CB    . ILE A  1 113  ? -19.840 64.130  57.372  1.00 47.35 ? 111  ILE A CB    1 
ATOM   672   C CG1   . ILE A  1 113  ? -18.641 64.469  58.270  1.00 44.93 ? 111  ILE A CG1   1 
ATOM   673   C CG2   . ILE A  1 113  ? -19.656 64.682  55.969  1.00 49.78 ? 111  ILE A CG2   1 
ATOM   674   C CD1   . ILE A  1 113  ? -17.328 63.946  57.762  1.00 43.82 ? 111  ILE A CD1   1 
ATOM   675   N N     . PRO A  1 114  ? -23.025 65.499  56.655  1.00 53.44 ? 112  PRO A N     1 
ATOM   676   C CA    . PRO A  1 114  ? -24.348 65.301  56.033  1.00 54.94 ? 112  PRO A CA    1 
ATOM   677   C C     . PRO A  1 114  ? -24.301 64.633  54.671  1.00 53.58 ? 112  PRO A C     1 
ATOM   678   O O     . PRO A  1 114  ? -25.178 63.816  54.365  1.00 53.05 ? 112  PRO A O     1 
ATOM   679   C CB    . PRO A  1 114  ? -24.909 66.729  55.944  1.00 50.42 ? 112  PRO A CB    1 
ATOM   680   C CG    . PRO A  1 114  ? -24.079 67.542  56.899  1.00 54.06 ? 112  PRO A CG    1 
ATOM   681   C CD    . PRO A  1 114  ? -22.719 66.921  56.870  1.00 52.87 ? 112  PRO A CD    1 
ATOM   682   N N     . ASP A  1 115  ? -23.310 64.950  53.842  1.00 54.72 ? 113  ASP A N     1 
ATOM   683   C CA    . ASP A  1 115  ? -23.282 64.475  52.465  1.00 55.47 ? 113  ASP A CA    1 
ATOM   684   C C     . ASP A  1 115  ? -22.511 63.164  52.361  1.00 55.34 ? 113  ASP A C     1 
ATOM   685   O O     . ASP A  1 115  ? -21.346 63.090  52.763  1.00 55.03 ? 113  ASP A O     1 
ATOM   686   C CB    . ASP A  1 115  ? -22.658 65.530  51.550  1.00 55.22 ? 113  ASP A CB    1 
ATOM   687   C CG    . ASP A  1 115  ? -22.350 64.991  50.167  1.00 58.44 ? 113  ASP A CG    1 
ATOM   688   O OD1   . ASP A  1 115  ? -23.303 64.621  49.442  1.00 57.36 ? 113  ASP A OD1   1 
ATOM   689   O OD2   . ASP A  1 115  ? -21.153 64.934  49.805  1.00 58.18 ? 113  ASP A OD2   1 
ATOM   690   N N     . THR A  1 116  ? -23.156 62.146  51.779  1.00 51.96 ? 114  THR A N     1 
ATOM   691   C CA    . THR A  1 116  ? -22.562 60.812  51.723  1.00 53.78 ? 114  THR A CA    1 
ATOM   692   C C     . THR A  1 116  ? -21.248 60.809  50.949  1.00 55.80 ? 114  THR A C     1 
ATOM   693   O O     . THR A  1 116  ? -20.245 60.250  51.411  1.00 54.36 ? 114  THR A O     1 
ATOM   694   C CB    . THR A  1 116  ? -23.544 59.823  51.100  1.00 52.29 ? 114  THR A CB    1 
ATOM   695   O OG1   . THR A  1 116  ? -24.708 59.721  51.926  1.00 55.00 ? 114  THR A OG1   1 
ATOM   696   C CG2   . THR A  1 116  ? -22.901 58.449  50.961  1.00 53.61 ? 114  THR A CG2   1 
ATOM   697   N N     . ALA A  1 117  ? -21.236 61.419  49.760  1.00 53.54 ? 115  ALA A N     1 
ATOM   698   C CA    . ALA A  1 117  ? -20.023 61.415  48.948  1.00 52.66 ? 115  ALA A CA    1 
ATOM   699   C C     . ALA A  1 117  ? -18.868 62.099  49.668  1.00 52.83 ? 115  ALA A C     1 
ATOM   700   O O     . ALA A  1 117  ? -17.724 61.633  49.601  1.00 55.00 ? 115  ALA A O     1 
ATOM   701   C CB    . ALA A  1 117  ? -20.289 62.083  47.598  1.00 52.67 ? 115  ALA A CB    1 
ATOM   702   N N     . THR A  1 118  ? -19.142 63.205  50.365  1.00 50.59 ? 116  THR A N     1 
ATOM   703   C CA    . THR A  1 118  ? -18.096 63.859  51.146  1.00 54.16 ? 116  THR A CA    1 
ATOM   704   C C     . THR A  1 118  ? -17.568 62.929  52.226  1.00 52.39 ? 116  THR A C     1 
ATOM   705   O O     . THR A  1 118  ? -16.355 62.829  52.442  1.00 49.66 ? 116  THR A O     1 
ATOM   706   C CB    . THR A  1 118  ? -18.628 65.138  51.790  1.00 51.62 ? 116  THR A CB    1 
ATOM   707   O OG1   . THR A  1 118  ? -19.234 65.959  50.789  1.00 60.80 ? 116  THR A OG1   1 
ATOM   708   C CG2   . THR A  1 118  ? -17.492 65.897  52.456  1.00 48.85 ? 116  THR A CG2   1 
ATOM   709   N N     . ARG A  1 119  ? -18.479 62.257  52.929  1.00 48.99 ? 117  ARG A N     1 
ATOM   710   C CA    . ARG A  1 119  ? -18.088 61.339  53.993  1.00 50.57 ? 117  ARG A CA    1 
ATOM   711   C C     . ARG A  1 119  ? -17.217 60.214  53.444  1.00 50.85 ? 117  ARG A C     1 
ATOM   712   O O     . ARG A  1 119  ? -16.118 59.953  53.953  1.00 48.79 ? 117  ARG A O     1 
ATOM   713   C CB    . ARG A  1 119  ? -19.346 60.783  54.665  1.00 43.34 ? 117  ARG A CB    1 
ATOM   714   C CG    . ARG A  1 119  ? -19.100 60.033  55.952  1.00 43.27 ? 117  ARG A CG    1 
ATOM   715   C CD    . ARG A  1 119  ? -20.328 59.246  56.380  1.00 43.12 ? 117  ARG A CD    1 
ATOM   716   N NE    . ARG A  1 119  ? -21.512 60.088  56.505  1.00 46.03 ? 117  ARG A NE    1 
ATOM   717   C CZ    . ARG A  1 119  ? -22.673 59.853  55.906  1.00 45.04 ? 117  ARG A CZ    1 
ATOM   718   N NH1   . ARG A  1 119  ? -22.852 58.797  55.126  1.00 43.29 ? 117  ARG A NH1   1 
ATOM   719   N NH2   . ARG A  1 119  ? -23.684 60.692  56.106  1.00 51.54 ? 117  ARG A NH2   1 
ATOM   720   N N     . ASP A  1 120  ? -17.692 59.551  52.387  1.00 50.85 ? 118  ASP A N     1 
ATOM   721   C CA    . ASP A  1 120  ? -16.937 58.461  51.781  1.00 52.97 ? 118  ASP A CA    1 
ATOM   722   C C     . ASP A  1 120  ? -15.564 58.923  51.319  1.00 51.53 ? 118  ASP A C     1 
ATOM   723   O O     . ASP A  1 120  ? -14.600 58.153  51.380  1.00 50.63 ? 118  ASP A O     1 
ATOM   724   C CB    . ASP A  1 120  ? -17.730 57.863  50.618  1.00 50.58 ? 118  ASP A CB    1 
ATOM   725   C CG    . ASP A  1 120  ? -19.072 57.297  51.060  1.00 55.57 ? 118  ASP A CG    1 
ATOM   726   O OD1   . ASP A  1 120  ? -19.383 57.367  52.270  1.00 52.87 ? 118  ASP A OD1   1 
ATOM   727   O OD2   . ASP A  1 120  ? -19.821 56.779  50.204  1.00 58.50 ? 118  ASP A OD2   1 
ATOM   728   N N     . ALA A  1 121  ? -15.450 60.181  50.883  1.00 51.74 ? 119  ALA A N     1 
ATOM   729   C CA    . ALA A  1 121  ? -14.150 60.717  50.495  1.00 54.86 ? 119  ALA A CA    1 
ATOM   730   C C     . ALA A  1 121  ? -13.242 60.886  51.704  1.00 53.44 ? 119  ALA A C     1 
ATOM   731   O O     . ALA A  1 121  ? -12.057 60.536  51.653  1.00 51.53 ? 119  ALA A O     1 
ATOM   732   C CB    . ALA A  1 121  ? -14.326 62.050  49.770  1.00 54.78 ? 119  ALA A CB    1 
ATOM   733   N N     . LEU A  1 122  ? -13.776 61.431  52.799  1.00 51.13 ? 120  LEU A N     1 
ATOM   734   C CA    . LEU A  1 122  ? -12.975 61.571  54.006  1.00 49.66 ? 120  LEU A CA    1 
ATOM   735   C C     . LEU A  1 122  ? -12.475 60.212  54.485  1.00 51.71 ? 120  LEU A C     1 
ATOM   736   O O     . LEU A  1 122  ? -11.299 60.063  54.841  1.00 50.14 ? 120  LEU A O     1 
ATOM   737   C CB    . LEU A  1 122  ? -13.787 62.268  55.093  1.00 47.59 ? 120  LEU A CB    1 
ATOM   738   C CG    . LEU A  1 122  ? -12.943 62.753  56.265  1.00 48.74 ? 120  LEU A CG    1 
ATOM   739   C CD1   . LEU A  1 122  ? -11.847 63.662  55.763  1.00 50.84 ? 120  LEU A CD1   1 
ATOM   740   C CD2   . LEU A  1 122  ? -13.791 63.465  57.293  1.00 49.17 ? 120  LEU A CD2   1 
ATOM   741   N N     . ILE A  1 123  ? -13.352 59.205  54.472  1.00 51.80 ? 121  ILE A N     1 
ATOM   742   C CA    . ILE A  1 123  ? -12.961 57.850  54.859  1.00 47.52 ? 121  ILE A CA    1 
ATOM   743   C C     . ILE A  1 123  ? -11.844 57.335  53.956  1.00 50.38 ? 121  ILE A C     1 
ATOM   744   O O     . ILE A  1 123  ? -10.764 56.954  54.424  1.00 47.44 ? 121  ILE A O     1 
ATOM   745   C CB    . ILE A  1 123  ? -14.180 56.913  54.821  1.00 45.46 ? 121  ILE A CB    1 
ATOM   746   C CG1   . ILE A  1 123  ? -15.208 57.305  55.896  1.00 41.64 ? 121  ILE A CG1   1 
ATOM   747   C CG2   . ILE A  1 123  ? -13.732 55.460  54.946  1.00 42.68 ? 121  ILE A CG2   1 
ATOM   748   C CD1   . ILE A  1 123  ? -16.595 56.744  55.652  1.00 42.76 ? 121  ILE A CD1   1 
ATOM   749   N N     . ARG A  1 124  ? -12.093 57.315  52.641  1.00 50.68 ? 122  ARG A N     1 
ATOM   750   C CA    . ARG A  1 124  ? -11.159 56.680  51.711  1.00 52.57 ? 122  ARG A CA    1 
ATOM   751   C C     . ARG A  1 124  ? -9.826  57.414  51.657  1.00 55.15 ? 122  ARG A C     1 
ATOM   752   O O     . ARG A  1 124  ? -8.764  56.780  51.647  1.00 61.43 ? 122  ARG A O     1 
ATOM   753   C CB    . ARG A  1 124  ? -11.771 56.609  50.312  1.00 50.16 ? 122  ARG A CB    1 
ATOM   754   N N     . ASP A  1 125  ? -9.857  58.745  51.629  1.00 57.48 ? 123  ASP A N     1 
ATOM   755   C CA    . ASP A  1 125  ? -8.654  59.523  51.361  1.00 58.28 ? 123  ASP A CA    1 
ATOM   756   C C     . ASP A  1 125  ? -7.898  59.913  52.625  1.00 58.10 ? 123  ASP A C     1 
ATOM   757   O O     . ASP A  1 125  ? -6.663  59.927  52.621  1.00 64.26 ? 123  ASP A O     1 
ATOM   758   C CB    . ASP A  1 125  ? -9.010  60.787  50.572  1.00 61.90 ? 123  ASP A CB    1 
ATOM   759   C CG    . ASP A  1 125  ? -9.680  60.482  49.242  1.00 61.92 ? 123  ASP A CG    1 
ATOM   760   O OD1   . ASP A  1 125  ? -9.376  59.428  48.643  1.00 62.10 ? 123  ASP A OD1   1 
ATOM   761   O OD2   . ASP A  1 125  ? -10.514 61.302  48.794  1.00 63.59 ? 123  ASP A OD2   1 
ATOM   762   N N     . LYS A  1 126  ? -8.603  60.225  53.703  1.00 53.17 ? 124  LYS A N     1 
ATOM   763   C CA    . LYS A  1 126  ? -7.981  60.857  54.858  1.00 55.14 ? 124  LYS A CA    1 
ATOM   764   C C     . LYS A  1 126  ? -8.114  60.069  56.155  1.00 56.45 ? 124  LYS A C     1 
ATOM   765   O O     . LYS A  1 126  ? -7.174  60.056  56.953  1.00 57.73 ? 124  LYS A O     1 
ATOM   766   C CB    . LYS A  1 126  ? -8.568  62.263  55.048  1.00 55.31 ? 124  LYS A CB    1 
ATOM   767   N N     . ILE A  1 127  ? -9.254  59.422  56.409  1.00 52.87 ? 125  ILE A N     1 
ATOM   768   C CA    . ILE A  1 127  ? -9.412  58.681  57.660  1.00 51.21 ? 125  ILE A CA    1 
ATOM   769   C C     . ILE A  1 127  ? -8.619  57.382  57.608  1.00 51.83 ? 125  ILE A C     1 
ATOM   770   O O     . ILE A  1 127  ? -7.753  57.130  58.452  1.00 54.52 ? 125  ILE A O     1 
ATOM   771   C CB    . ILE A  1 127  ? -10.896 58.407  57.966  1.00 49.96 ? 125  ILE A CB    1 
ATOM   772   C CG1   . ILE A  1 127  ? -11.696 59.707  58.055  1.00 51.59 ? 125  ILE A CG1   1 
ATOM   773   C CG2   . ILE A  1 127  ? -11.028 57.637  59.278  1.00 46.15 ? 125  ILE A CG2   1 
ATOM   774   C CD1   . ILE A  1 127  ? -11.108 60.719  59.002  1.00 48.41 ? 125  ILE A CD1   1 
ATOM   775   N N     . ALA A  1 128  ? -8.907  56.537  56.615  1.00 48.55 ? 126  ALA A N     1 
ATOM   776   C CA    . ALA A  1 128  ? -8.261  55.234  56.532  1.00 45.28 ? 126  ALA A CA    1 
ATOM   777   C C     . ALA A  1 128  ? -6.748  55.339  56.423  1.00 55.85 ? 126  ALA A C     1 
ATOM   778   O O     . ALA A  1 128  ? -6.051  54.376  56.757  1.00 50.08 ? 126  ALA A O     1 
ATOM   779   C CB    . ALA A  1 128  ? -8.791  54.445  55.339  1.00 42.35 ? 126  ALA A CB    1 
ATOM   780   N N     . ASP A  1 129  ? -6.228  56.481  55.969  1.00 59.83 ? 127  ASP A N     1 
ATOM   781   C CA    . ASP A  1 129  ? -4.792  56.673  55.816  1.00 60.17 ? 127  ASP A CA    1 
ATOM   782   C C     . ASP A  1 129  ? -4.186  57.159  57.124  1.00 59.90 ? 127  ASP A C     1 
ATOM   783   O O     . ASP A  1 129  ? -3.166  57.856  57.126  1.00 67.70 ? 127  ASP A O     1 
ATOM   784   C CB    . ASP A  1 129  ? -4.503  57.665  54.685  1.00 57.98 ? 127  ASP A CB    1 
ATOM   785   N N     . GLY A  1 130  ? -4.807  56.787  58.237  1.00 62.09 ? 128  GLY A N     1 
ATOM   786   C CA    . GLY A  1 130  ? -4.361  57.228  59.533  1.00 59.65 ? 128  GLY A CA    1 
ATOM   787   C C     . GLY A  1 130  ? -4.668  58.699  59.750  1.00 63.32 ? 128  GLY A C     1 
ATOM   788   O O     . GLY A  1 130  ? -5.329  59.363  58.948  1.00 64.55 ? 128  GLY A O     1 
ATOM   789   N N     . ASN A  1 131  ? -4.155  59.204  60.870  1.00 58.77 ? 129  ASN A N     1 
ATOM   790   C CA    . ASN A  1 131  ? -4.332  60.600  61.257  1.00 60.98 ? 129  ASN A CA    1 
ATOM   791   C C     . ASN A  1 131  ? -5.810  60.981  61.240  1.00 56.62 ? 129  ASN A C     1 
ATOM   792   O O     . ASN A  1 131  ? -6.213  61.992  60.661  1.00 59.35 ? 129  ASN A O     1 
ATOM   793   C CB    . ASN A  1 131  ? -3.508  61.527  60.360  1.00 59.79 ? 129  ASN A CB    1 
ATOM   794   N N     . TRP A  1 132  ? -6.628  60.136  61.875  1.00 55.38 ? 130  TRP A N     1 
ATOM   795   C CA    . TRP A  1 132  ? -8.041  60.464  62.053  1.00 50.74 ? 130  TRP A CA    1 
ATOM   796   C C     . TRP A  1 132  ? -8.218  61.705  62.914  1.00 49.81 ? 130  TRP A C     1 
ATOM   797   O O     . TRP A  1 132  ? -9.226  62.415  62.788  1.00 50.40 ? 130  TRP A O     1 
ATOM   798   C CB    . TRP A  1 132  ? -8.787  59.283  62.684  1.00 49.19 ? 130  TRP A CB    1 
ATOM   799   C CG    . TRP A  1 132  ? -8.226  58.851  64.014  1.00 41.07 ? 130  TRP A CG    1 
ATOM   800   C CD1   . TRP A  1 132  ? -7.290  57.880  64.229  1.00 37.15 ? 130  TRP A CD1   1 
ATOM   801   C CD2   . TRP A  1 132  ? -8.560  59.378  65.312  1.00 37.80 ? 130  TRP A CD2   1 
ATOM   802   N NE1   . TRP A  1 132  ? -7.029  57.762  65.577  1.00 36.34 ? 130  TRP A NE1   1 
ATOM   803   C CE2   . TRP A  1 132  ? -7.782  58.677  66.261  1.00 35.46 ? 130  TRP A CE2   1 
ATOM   804   C CE3   . TRP A  1 132  ? -9.429  60.374  65.760  1.00 38.32 ? 130  TRP A CE3   1 
ATOM   805   C CZ2   . TRP A  1 132  ? -7.852  58.940  67.637  1.00 30.00 ? 130  TRP A CZ2   1 
ATOM   806   C CZ3   . TRP A  1 132  ? -9.501  60.635  67.115  1.00 38.23 ? 130  TRP A CZ3   1 
ATOM   807   C CH2   . TRP A  1 132  ? -8.716  59.919  68.042  1.00 35.72 ? 130  TRP A CH2   1 
ATOM   808   N N     . LYS A  1 133  ? -7.258  61.973  63.803  1.00 51.57 ? 131  LYS A N     1 
ATOM   809   C CA    . LYS A  1 133  ? -7.366  63.128  64.687  1.00 53.51 ? 131  LYS A CA    1 
ATOM   810   C C     . LYS A  1 133  ? -7.351  64.428  63.896  1.00 58.46 ? 131  LYS A C     1 
ATOM   811   O O     . LYS A  1 133  ? -8.135  65.342  64.177  1.00 63.51 ? 131  LYS A O     1 
ATOM   812   C CB    . LYS A  1 133  ? -6.235  63.106  65.716  1.00 50.25 ? 131  LYS A CB    1 
ATOM   813   N N     . SER A  1 134  ? -6.484  64.516  62.884  1.00 59.93 ? 132  SER A N     1 
ATOM   814   C CA    . SER A  1 134  ? -6.352  65.747  62.112  1.00 59.24 ? 132  SER A CA    1 
ATOM   815   C C     . SER A  1 134  ? -7.673  66.167  61.475  1.00 60.58 ? 132  SER A C     1 
ATOM   816   O O     . SER A  1 134  ? -7.953  67.366  61.355  1.00 64.19 ? 132  SER A O     1 
ATOM   817   C CB    . SER A  1 134  ? -5.276  65.570  61.039  1.00 59.43 ? 132  SER A CB    1 
ATOM   818   N N     . HIS A  1 135  ? -8.506  65.206  61.084  1.00 59.85 ? 133  HIS A N     1 
ATOM   819   C CA    . HIS A  1 135  ? -9.715  65.516  60.336  1.00 59.14 ? 133  HIS A CA    1 
ATOM   820   C C     . HIS A  1 135  ? -10.973 65.564  61.195  1.00 59.27 ? 133  HIS A C     1 
ATOM   821   O O     . HIS A  1 135  ? -11.965 66.170  60.775  1.00 58.54 ? 133  HIS A O     1 
ATOM   822   C CB    . HIS A  1 135  ? -9.900  64.495  59.208  1.00 57.39 ? 133  HIS A CB    1 
ATOM   823   C CG    . HIS A  1 135  ? -8.667  64.286  58.385  1.00 59.12 ? 133  HIS A CG    1 
ATOM   824   N ND1   . HIS A  1 135  ? -7.678  63.392  58.739  1.00 57.04 ? 133  HIS A ND1   1 
ATOM   825   C CD2   . HIS A  1 135  ? -8.253  64.867  57.235  1.00 57.70 ? 133  HIS A CD2   1 
ATOM   826   C CE1   . HIS A  1 135  ? -6.712  63.426  57.839  1.00 60.74 ? 133  HIS A CE1   1 
ATOM   827   N NE2   . HIS A  1 135  ? -7.035  64.316  56.917  1.00 63.44 ? 133  HIS A NE2   1 
ATOM   828   N N     . LEU A  1 136  ? -10.960 64.958  62.378  1.00 59.34 ? 134  LEU A N     1 
ATOM   829   C CA    . LEU A  1 136  ? -12.137 64.961  63.241  1.00 55.33 ? 134  LEU A CA    1 
ATOM   830   C C     . LEU A  1 136  ? -11.742 65.195  64.698  1.00 60.48 ? 134  LEU A C     1 
ATOM   831   O O     . LEU A  1 136  ? -12.440 65.889  65.441  1.00 61.54 ? 134  LEU A O     1 
ATOM   832   C CB    . LEU A  1 136  ? -12.910 63.644  63.102  1.00 53.48 ? 134  LEU A CB    1 
ATOM   833   C CG    . LEU A  1 136  ? -13.612 63.362  61.770  1.00 53.69 ? 134  LEU A CG    1 
ATOM   834   C CD1   . LEU A  1 136  ? -14.032 61.905  61.666  1.00 44.60 ? 134  LEU A CD1   1 
ATOM   835   C CD2   . LEU A  1 136  ? -14.813 64.273  61.592  1.00 50.38 ? 134  LEU A CD2   1 
ATOM   836   N N     . SER A  1 139  ? -12.871 70.459  68.146  1.00 47.99 ? 137  SER A N     1 
ATOM   837   C CA    . SER A  1 139  ? -13.475 71.195  69.255  1.00 47.44 ? 137  SER A CA    1 
ATOM   838   C C     . SER A  1 139  ? -14.350 70.274  70.113  1.00 48.35 ? 137  SER A C     1 
ATOM   839   O O     . SER A  1 139  ? -14.901 70.686  71.144  1.00 46.91 ? 137  SER A O     1 
ATOM   840   C CB    . SER A  1 139  ? -14.294 72.378  68.725  1.00 44.73 ? 137  SER A CB    1 
ATOM   841   N N     . ARG A  1 140  ? -14.474 69.020  69.688  1.00 44.05 ? 138  ARG A N     1 
ATOM   842   C CA    . ARG A  1 140  ? -15.269 68.048  70.426  1.00 41.51 ? 138  ARG A CA    1 
ATOM   843   C C     . ARG A  1 140  ? -14.617 66.679  70.313  1.00 40.91 ? 138  ARG A C     1 
ATOM   844   O O     . ARG A  1 140  ? -14.287 66.239  69.208  1.00 38.13 ? 138  ARG A O     1 
ATOM   845   C CB    . ARG A  1 140  ? -16.701 67.995  69.897  1.00 40.40 ? 138  ARG A CB    1 
ATOM   846   C CG    . ARG A  1 140  ? -17.602 67.100  70.700  1.00 43.37 ? 138  ARG A CG    1 
ATOM   847   C CD    . ARG A  1 140  ? -18.734 66.572  69.855  1.00 44.35 ? 138  ARG A CD    1 
ATOM   848   N NE    . ARG A  1 140  ? -20.013 66.720  70.536  1.00 49.11 ? 138  ARG A NE    1 
ATOM   849   C CZ    . ARG A  1 140  ? -21.056 65.924  70.351  1.00 50.99 ? 138  ARG A CZ    1 
ATOM   850   N NH1   . ARG A  1 140  ? -20.994 64.882  69.533  1.00 55.02 ? 138  ARG A NH1   1 
ATOM   851   N NH2   . ARG A  1 140  ? -22.185 66.172  71.011  1.00 49.40 ? 138  ARG A NH2   1 
ATOM   852   N N     . SER A  1 141  ? -14.440 66.011  71.451  1.00 34.88 ? 139  SER A N     1 
ATOM   853   C CA    . SER A  1 141  ? -13.878 64.671  71.439  1.00 31.57 ? 139  SER A CA    1 
ATOM   854   C C     . SER A  1 141  ? -14.738 63.749  70.581  1.00 31.68 ? 139  SER A C     1 
ATOM   855   O O     . SER A  1 141  ? -15.964 63.861  70.559  1.00 30.78 ? 139  SER A O     1 
ATOM   856   C CB    . SER A  1 141  ? -13.778 64.143  72.870  1.00 30.45 ? 139  SER A CB    1 
ATOM   857   O OG    . SER A  1 141  ? -13.316 62.798  72.926  1.00 30.38 ? 139  SER A OG    1 
ATOM   858   N N     . LEU A  1 142  ? -14.085 62.862  69.825  1.00 31.27 ? 140  LEU A N     1 
ATOM   859   C CA    . LEU A  1 142  ? -14.829 61.797  69.156  1.00 27.97 ? 140  LEU A CA    1 
ATOM   860   C C     . LEU A  1 142  ? -15.630 60.953  70.129  1.00 27.20 ? 140  LEU A C     1 
ATOM   861   O O     . LEU A  1 142  ? -16.622 60.330  69.735  1.00 27.53 ? 140  LEU A O     1 
ATOM   862   C CB    . LEU A  1 142  ? -13.880 60.860  68.415  1.00 31.41 ? 140  LEU A CB    1 
ATOM   863   C CG    . LEU A  1 142  ? -13.961 60.898  66.906  1.00 35.58 ? 140  LEU A CG    1 
ATOM   864   C CD1   . LEU A  1 142  ? -13.401 62.221  66.452  1.00 41.50 ? 140  LEU A CD1   1 
ATOM   865   C CD2   . LEU A  1 142  ? -13.173 59.725  66.333  1.00 36.11 ? 140  LEU A CD2   1 
ATOM   866   N N     . PHE A  1 143  ? -15.221 60.925  71.392  1.00 25.16 ? 141  PHE A N     1 
ATOM   867   C CA    . PHE A  1 143  ? -15.651 59.906  72.336  1.00 25.93 ? 141  PHE A CA    1 
ATOM   868   C C     . PHE A  1 143  ? -16.621 60.457  73.374  1.00 24.14 ? 141  PHE A C     1 
ATOM   869   O O     . PHE A  1 143  ? -16.788 59.860  74.442  1.00 25.45 ? 141  PHE A O     1 
ATOM   870   C CB    . PHE A  1 143  ? -14.407 59.294  72.992  1.00 23.38 ? 141  PHE A CB    1 
ATOM   871   C CG    . PHE A  1 143  ? -13.359 58.863  71.986  1.00 25.22 ? 141  PHE A CG    1 
ATOM   872   C CD1   . PHE A  1 143  ? -13.655 57.878  71.048  1.00 19.63 ? 141  PHE A CD1   1 
ATOM   873   C CD2   . PHE A  1 143  ? -12.100 59.459  71.959  1.00 23.04 ? 141  PHE A CD2   1 
ATOM   874   C CE1   . PHE A  1 143  ? -12.706 57.472  70.121  1.00 24.43 ? 141  PHE A CE1   1 
ATOM   875   C CE2   . PHE A  1 143  ? -11.157 59.071  71.031  1.00 25.54 ? 141  PHE A CE2   1 
ATOM   876   C CZ    . PHE A  1 143  ? -11.453 58.072  70.105  1.00 24.63 ? 141  PHE A CZ    1 
ATOM   877   N N     . VAL A  1 144  ? -17.266 61.588  73.075  1.00 25.02 ? 142  VAL A N     1 
ATOM   878   C CA    A VAL A  1 144  ? -18.202 62.188  74.025  0.48 27.16 ? 142  VAL A CA    1 
ATOM   879   C CA    B VAL A  1 144  ? -18.198 62.185  74.028  0.52 27.16 ? 142  VAL A CA    1 
ATOM   880   C C     . VAL A  1 144  ? -19.288 61.192  74.417  1.00 26.83 ? 142  VAL A C     1 
ATOM   881   O O     . VAL A  1 144  ? -19.708 61.135  75.576  1.00 27.97 ? 142  VAL A O     1 
ATOM   882   C CB    A VAL A  1 144  ? -18.800 63.483  73.439  0.48 28.46 ? 142  VAL A CB    1 
ATOM   883   C CB    B VAL A  1 144  ? -18.793 63.487  73.456  0.52 28.45 ? 142  VAL A CB    1 
ATOM   884   C CG1   A VAL A  1 144  ? -19.951 63.998  74.303  0.48 28.22 ? 142  VAL A CG1   1 
ATOM   885   C CG1   B VAL A  1 144  ? -17.719 64.556  73.363  0.52 29.69 ? 142  VAL A CG1   1 
ATOM   886   C CG2   A VAL A  1 144  ? -17.719 64.542  73.301  0.48 29.71 ? 142  VAL A CG2   1 
ATOM   887   C CG2   B VAL A  1 144  ? -19.424 63.238  72.086  0.52 28.14 ? 142  VAL A CG2   1 
ATOM   888   N N     . ASN A  1 145  ? -19.753 60.380  73.469  1.00 24.41 ? 143  ASN A N     1 
ATOM   889   C CA    . ASN A  1 145  ? -20.842 59.453  73.762  1.00 26.06 ? 143  ASN A CA    1 
ATOM   890   C C     . ASN A  1 145  ? -20.368 58.018  73.983  1.00 24.06 ? 143  ASN A C     1 
ATOM   891   O O     . ASN A  1 145  ? -21.171 57.082  73.862  1.00 25.19 ? 143  ASN A O     1 
ATOM   892   C CB    . ASN A  1 145  ? -21.879 59.498  72.640  1.00 27.87 ? 143  ASN A CB    1 
ATOM   893   C CG    . ASN A  1 145  ? -22.684 60.771  72.657  1.00 30.33 ? 143  ASN A CG    1 
ATOM   894   O OD1   . ASN A  1 145  ? -23.215 61.160  73.698  1.00 32.51 ? 143  ASN A OD1   1 
ATOM   895   N ND2   . ASN A  1 145  ? -22.757 61.444  71.519  1.00 29.22 ? 143  ASN A ND2   1 
ATOM   896   N N     . ALA A  1 146  ? -19.087 57.823  74.316  1.00 24.51 ? 144  ALA A N     1 
ATOM   897   C CA    . ALA A  1 146  ? -18.536 56.471  74.383  1.00 23.07 ? 144  ALA A CA    1 
ATOM   898   C C     . ALA A  1 146  ? -19.172 55.640  75.492  1.00 25.97 ? 144  ALA A C     1 
ATOM   899   O O     . ALA A  1 146  ? -19.198 54.403  75.396  1.00 26.09 ? 144  ALA A O     1 
ATOM   900   C CB    . ALA A  1 146  ? -17.014 56.532  74.592  1.00 22.68 ? 144  ALA A CB    1 
ATOM   901   N N     . ALA A  1 147  ? -19.643 56.285  76.564  1.00 24.92 ? 145  ALA A N     1 
ATOM   902   C CA    . ALA A  1 147  ? -20.322 55.544  77.616  1.00 28.72 ? 145  ALA A CA    1 
ATOM   903   C C     . ALA A  1 147  ? -21.523 54.815  77.045  1.00 27.62 ? 145  ALA A C     1 
ATOM   904   O O     . ALA A  1 147  ? -21.762 53.645  77.361  1.00 27.78 ? 145  ALA A O     1 
ATOM   905   C CB    . ALA A  1 147  ? -20.745 56.485  78.750  1.00 31.02 ? 145  ALA A CB    1 
ATOM   906   N N     . THR A  1 148  ? -22.257 55.482  76.151  1.00 25.14 ? 146  THR A N     1 
ATOM   907   C CA    . THR A  1 148  ? -23.405 54.855  75.508  1.00 27.82 ? 146  THR A CA    1 
ATOM   908   C C     . THR A  1 148  ? -22.978 53.708  74.601  1.00 26.17 ? 146  THR A C     1 
ATOM   909   O O     . THR A  1 148  ? -23.531 52.604  74.679  1.00 26.73 ? 146  THR A O     1 
ATOM   910   C CB    . THR A  1 148  ? -24.193 55.920  74.740  1.00 28.89 ? 146  THR A CB    1 
ATOM   911   O OG1   . THR A  1 148  ? -24.632 56.913  75.681  1.00 26.25 ? 146  THR A OG1   1 
ATOM   912   C CG2   . THR A  1 148  ? -25.387 55.309  74.056  1.00 28.77 ? 146  THR A CG2   1 
ATOM   913   N N     . TRP A  1 149  ? -21.978 53.934  73.744  1.00 26.41 ? 147  TRP A N     1 
ATOM   914   C CA    . TRP A  1 149  ? -21.482 52.842  72.904  1.00 25.68 ? 147  TRP A CA    1 
ATOM   915   C C     . TRP A  1 149  ? -20.869 51.718  73.736  1.00 22.95 ? 147  TRP A C     1 
ATOM   916   O O     . TRP A  1 149  ? -20.964 50.542  73.364  1.00 26.44 ? 147  TRP A O     1 
ATOM   917   C CB    . TRP A  1 149  ? -20.467 53.370  71.889  1.00 24.99 ? 147  TRP A CB    1 
ATOM   918   C CG    . TRP A  1 149  ? -21.105 54.263  70.889  1.00 26.67 ? 147  TRP A CG    1 
ATOM   919   C CD1   . TRP A  1 149  ? -20.870 55.596  70.701  1.00 26.41 ? 147  TRP A CD1   1 
ATOM   920   C CD2   . TRP A  1 149  ? -22.107 53.891  69.941  1.00 27.49 ? 147  TRP A CD2   1 
ATOM   921   N NE1   . TRP A  1 149  ? -21.674 56.077  69.692  1.00 30.07 ? 147  TRP A NE1   1 
ATOM   922   C CE2   . TRP A  1 149  ? -22.434 55.048  69.203  1.00 27.41 ? 147  TRP A CE2   1 
ATOM   923   C CE3   . TRP A  1 149  ? -22.749 52.687  69.636  1.00 26.46 ? 147  TRP A CE3   1 
ATOM   924   C CZ2   . TRP A  1 149  ? -23.381 55.038  68.179  1.00 28.16 ? 147  TRP A CZ2   1 
ATOM   925   C CZ3   . TRP A  1 149  ? -23.705 52.680  68.624  1.00 31.73 ? 147  TRP A CZ3   1 
ATOM   926   C CH2   . TRP A  1 149  ? -24.010 53.849  67.911  1.00 31.03 ? 147  TRP A CH2   1 
ATOM   927   N N     . GLY A  1 150  ? -20.205 52.062  74.843  1.00 24.81 ? 148  GLY A N     1 
ATOM   928   C CA    . GLY A  1 150  ? -19.731 51.040  75.756  1.00 24.05 ? 148  GLY A CA    1 
ATOM   929   C C     . GLY A  1 150  ? -20.837 50.104  76.197  1.00 27.23 ? 148  GLY A C     1 
ATOM   930   O O     . GLY A  1 150  ? -20.655 48.884  76.232  1.00 30.99 ? 148  GLY A O     1 
ATOM   931   N N     . LEU A  1 151  ? -22.011 50.662  76.524  1.00 29.33 ? 149  LEU A N     1 
ATOM   932   C CA    . LEU A  1 151  ? -23.155 49.819  76.865  1.00 28.63 ? 149  LEU A CA    1 
ATOM   933   C C     . LEU A  1 151  ? -23.555 48.939  75.689  1.00 28.15 ? 149  LEU A C     1 
ATOM   934   O O     . LEU A  1 151  ? -23.818 47.745  75.860  1.00 32.47 ? 149  LEU A O     1 
ATOM   935   C CB    . LEU A  1 151  ? -24.334 50.686  77.307  1.00 30.71 ? 149  LEU A CB    1 
ATOM   936   C CG    . LEU A  1 151  ? -24.826 50.553  78.744  1.00 38.09 ? 149  LEU A CG    1 
ATOM   937   C CD1   . LEU A  1 151  ? -26.143 51.297  78.897  1.00 38.03 ? 149  LEU A CD1   1 
ATOM   938   C CD2   . LEU A  1 151  ? -25.000 49.102  79.130  1.00 33.83 ? 149  LEU A CD2   1 
ATOM   939   N N     . VAL A  1 152  ? -23.605 49.511  74.484  1.00 27.36 ? 150  VAL A N     1 
ATOM   940   C CA    . VAL A  1 152  ? -23.974 48.743  73.295  1.00 26.13 ? 150  VAL A CA    1 
ATOM   941   C C     . VAL A  1 152  ? -22.999 47.596  73.063  1.00 29.50 ? 150  VAL A C     1 
ATOM   942   O O     . VAL A  1 152  ? -23.402 46.466  72.760  1.00 30.19 ? 150  VAL A O     1 
ATOM   943   C CB    . VAL A  1 152  ? -24.047 49.671  72.067  1.00 26.86 ? 150  VAL A CB    1 
ATOM   944   C CG1   . VAL A  1 152  ? -24.146 48.870  70.797  1.00 30.78 ? 150  VAL A CG1   1 
ATOM   945   C CG2   . VAL A  1 152  ? -25.223 50.629  72.183  1.00 28.43 ? 150  VAL A CG2   1 
ATOM   946   N N     . VAL A  1 153  ? -21.702 47.873  73.181  1.00 27.63 ? 151  VAL A N     1 
ATOM   947   C CA    . VAL A  1 153  ? -20.679 46.888  72.839  1.00 26.49 ? 151  VAL A CA    1 
ATOM   948   C C     . VAL A  1 153  ? -20.468 45.893  73.978  1.00 29.69 ? 151  VAL A C     1 
ATOM   949   O O     . VAL A  1 153  ? -20.401 44.678  73.751  1.00 32.14 ? 151  VAL A O     1 
ATOM   950   C CB    . VAL A  1 153  ? -19.367 47.609  72.468  1.00 27.25 ? 151  VAL A CB    1 
ATOM   951   C CG1   . VAL A  1 153  ? -18.223 46.632  72.406  1.00 30.30 ? 151  VAL A CG1   1 
ATOM   952   C CG2   . VAL A  1 153  ? -19.507 48.327  71.147  1.00 26.32 ? 151  VAL A CG2   1 
ATOM   953   N N     . THR A  1 154  ? -20.350 46.380  75.217  1.00 30.77 ? 152  THR A N     1 
ATOM   954   C CA    . THR A  1 154  ? -19.955 45.519  76.333  1.00 31.44 ? 152  THR A CA    1 
ATOM   955   C C     . THR A  1 154  ? -21.097 45.135  77.268  1.00 36.06 ? 152  THR A C     1 
ATOM   956   O O     . THR A  1 154  ? -20.933 44.198  78.054  1.00 34.60 ? 152  THR A O     1 
ATOM   957   C CB    . THR A  1 154  ? -18.855 46.179  77.185  1.00 34.18 ? 152  THR A CB    1 
ATOM   958   O OG1   . THR A  1 154  ? -19.423 47.187  78.042  1.00 34.67 ? 152  THR A OG1   1 
ATOM   959   C CG2   . THR A  1 154  ? -17.788 46.805  76.308  1.00 29.92 ? 152  THR A CG2   1 
ATOM   960   N N     . GLY A  1 155  ? -22.230 45.834  77.227  1.00 36.10 ? 153  GLY A N     1 
ATOM   961   C CA    . GLY A  1 155  ? -23.281 45.615  78.199  1.00 32.77 ? 153  GLY A CA    1 
ATOM   962   C C     . GLY A  1 155  ? -23.061 46.279  79.540  1.00 36.54 ? 153  GLY A C     1 
ATOM   963   O O     . GLY A  1 155  ? -23.931 46.172  80.416  1.00 42.06 ? 153  GLY A O     1 
ATOM   964   N N     . LYS A  1 156  ? -21.945 46.978  79.728  1.00 35.85 ? 154  LYS A N     1 
ATOM   965   C CA    . LYS A  1 156  ? -21.596 47.588  81.001  1.00 36.31 ? 154  LYS A CA    1 
ATOM   966   C C     . LYS A  1 156  ? -21.580 49.106  80.871  1.00 35.83 ? 154  LYS A C     1 
ATOM   967   O O     . LYS A  1 156  ? -21.252 49.649  79.813  1.00 30.47 ? 154  LYS A O     1 
ATOM   968   C CB    . LYS A  1 156  ? -20.229 47.087  81.479  1.00 36.63 ? 154  LYS A CB    1 
ATOM   969   N N     . LEU A  1 157  ? -21.927 49.794  81.957  1.00 33.13 ? 155  LEU A N     1 
ATOM   970   C CA    . LEU A  1 157  ? -22.008 51.249  81.960  1.00 39.16 ? 155  LEU A CA    1 
ATOM   971   C C     . LEU A  1 157  ? -20.815 51.836  82.700  1.00 41.03 ? 155  LEU A C     1 
ATOM   972   O O     . LEU A  1 157  ? -20.455 51.366  83.785  1.00 40.65 ? 155  LEU A O     1 
ATOM   973   C CB    . LEU A  1 157  ? -23.314 51.735  82.595  1.00 41.03 ? 155  LEU A CB    1 
ATOM   974   N N     . THR A  1 158  ? -20.206 52.857  82.102  1.00 40.82 ? 156  THR A N     1 
ATOM   975   C CA    . THR A  1 158  ? -19.158 53.654  82.726  1.00 41.70 ? 156  THR A CA    1 
ATOM   976   C C     . THR A  1 158  ? -19.617 55.104  82.747  1.00 43.00 ? 156  THR A C     1 
ATOM   977   O O     . THR A  1 158  ? -20.145 55.604  81.751  1.00 44.69 ? 156  THR A O     1 
ATOM   978   C CB    . THR A  1 158  ? -17.831 53.526  81.972  1.00 43.79 ? 156  THR A CB    1 
ATOM   979   N N     . SER A  1 159  ? -19.440 55.770  83.885  1.00 34.64 ? 157  SER A N     1 
ATOM   980   C CA    . SER A  1 159  ? -19.902 57.148  84.002  1.00 37.38 ? 157  SER A CA    1 
ATOM   981   C C     . SER A  1 159  ? -19.055 58.088  83.157  1.00 35.26 ? 157  SER A C     1 
ATOM   982   O O     . SER A  1 159  ? -19.565 59.063  82.595  1.00 42.15 ? 157  SER A O     1 
ATOM   983   C CB    . SER A  1 159  ? -19.875 57.575  85.467  1.00 41.25 ? 157  SER A CB    1 
ATOM   984   O OG    . SER A  1 159  ? -19.023 56.714  86.204  1.00 41.06 ? 157  SER A OG    1 
ATOM   985   N N     . THR A  1 160  ? -17.759 57.822  83.067  1.00 36.71 ? 158  THR A N     1 
ATOM   986   C CA    . THR A  1 160  ? -16.850 58.665  82.312  1.00 31.31 ? 158  THR A CA    1 
ATOM   987   C C     . THR A  1 160  ? -16.087 57.809  81.311  1.00 30.37 ? 158  THR A C     1 
ATOM   988   O O     . THR A  1 160  ? -16.100 56.576  81.364  1.00 31.73 ? 158  THR A O     1 
ATOM   989   C CB    . THR A  1 160  ? -15.895 59.418  83.244  1.00 32.90 ? 158  THR A CB    1 
ATOM   990   O OG1   . THR A  1 160  ? -15.217 58.481  84.091  1.00 35.82 ? 158  THR A OG1   1 
ATOM   991   C CG2   . THR A  1 160  ? -16.675 60.407  84.095  1.00 34.06 ? 158  THR A CG2   1 
ATOM   992   N N     . VAL A  1 161  ? -15.411 58.493  80.392  1.00 25.69 ? 159  VAL A N     1 
ATOM   993   C CA    . VAL A  1 161  ? -14.843 57.891  79.199  1.00 24.54 ? 159  VAL A CA    1 
ATOM   994   C C     . VAL A  1 161  ? -13.326 57.932  79.318  1.00 23.14 ? 159  VAL A C     1 
ATOM   995   O O     . VAL A  1 161  ? -12.754 58.993  79.579  1.00 21.39 ? 159  VAL A O     1 
ATOM   996   C CB    . VAL A  1 161  ? -15.330 58.655  77.953  1.00 24.35 ? 159  VAL A CB    1 
ATOM   997   C CG1   . VAL A  1 161  ? -14.551 58.284  76.734  1.00 26.68 ? 159  VAL A CG1   1 
ATOM   998   C CG2   . VAL A  1 161  ? -16.848 58.440  77.768  1.00 29.27 ? 159  VAL A CG2   1 
ATOM   999   N N     . ASN A  1 162  ? -12.672 56.783  79.143  1.00 21.62 ? 160  ASN A N     1 
ATOM   1000  C CA    . ASN A  1 162  ? -11.206 56.798  79.074  1.00 24.13 ? 160  ASN A CA    1 
ATOM   1001  C C     . ASN A  1 162  ? -10.854 57.134  77.637  1.00 18.83 ? 160  ASN A C     1 
ATOM   1002  O O     . ASN A  1 162  ? -10.683 56.250  76.792  1.00 19.63 ? 160  ASN A O     1 
ATOM   1003  C CB    . ASN A  1 162  ? -10.605 55.475  79.513  1.00 20.71 ? 160  ASN A CB    1 
ATOM   1004  C CG    . ASN A  1 162  ? -9.064  55.518  79.562  1.00 26.95 ? 160  ASN A CG    1 
ATOM   1005  O OD1   . ASN A  1 162  ? -8.416  56.340  78.888  1.00 21.23 ? 160  ASN A OD1   1 
ATOM   1006  N ND2   . ASN A  1 162  ? -8.482  54.634  80.369  1.00 24.62 ? 160  ASN A ND2   1 
ATOM   1007  N N     . ASP A  1 163  ? -10.777 58.441  77.353  1.00 19.10 ? 161  ASP A N     1 
ATOM   1008  C CA    . ASP A  1 163  ? -10.604 58.893  75.979  1.00 20.75 ? 161  ASP A CA    1 
ATOM   1009  C C     . ASP A  1 163  ? -9.202  58.602  75.449  1.00 22.57 ? 161  ASP A C     1 
ATOM   1010  O O     . ASP A  1 163  ? -9.021  58.448  74.238  1.00 22.29 ? 161  ASP A O     1 
ATOM   1011  C CB    . ASP A  1 163  ? -10.959 60.391  75.851  1.00 21.83 ? 161  ASP A CB    1 
ATOM   1012  C CG    . ASP A  1 163  ? -10.256 61.302  76.887  1.00 26.10 ? 161  ASP A CG    1 
ATOM   1013  O OD1   . ASP A  1 163  ? -10.101 60.933  78.073  1.00 21.17 ? 161  ASP A OD1   1 
ATOM   1014  O OD2   . ASP A  1 163  ? -9.879  62.431  76.490  1.00 26.86 ? 161  ASP A OD2   1 
ATOM   1015  N N     . ARG A  1 164  ? -8.204  58.482  76.325  1.00 19.80 ? 162  ARG A N     1 
ATOM   1016  C CA    . ARG A  1 164  ? -6.878  58.106  75.843  1.00 19.99 ? 162  ARG A CA    1 
ATOM   1017  C C     . ARG A  1 164  ? -6.826  56.639  75.442  1.00 20.49 ? 162  ARG A C     1 
ATOM   1018  O O     . ARG A  1 164  ? -6.174  56.286  74.452  1.00 21.12 ? 162  ARG A O     1 
ATOM   1019  C CB    . ARG A  1 164  ? -5.810  58.408  76.901  1.00 20.54 ? 162  ARG A CB    1 
ATOM   1020  C CG    . ARG A  1 164  ? -5.624  59.900  77.212  1.00 25.13 ? 162  ARG A CG    1 
ATOM   1021  C CD    . ARG A  1 164  ? -5.766  60.775  75.993  1.00 31.43 ? 162  ARG A CD    1 
ATOM   1022  N NE    . ARG A  1 164  ? -4.827  60.426  74.936  1.00 32.66 ? 162  ARG A NE    1 
ATOM   1023  C CZ    . ARG A  1 164  ? -5.012  60.714  73.652  1.00 35.68 ? 162  ARG A CZ    1 
ATOM   1024  N NH1   . ARG A  1 164  ? -6.088  61.368  73.237  1.00 37.83 ? 162  ARG A NH1   1 
ATOM   1025  N NH2   . ARG A  1 164  ? -4.098  60.330  72.760  1.00 34.40 ? 162  ARG A NH2   1 
ATOM   1026  N N     . SER A  1 165  ? -7.489  55.768  76.206  1.00 20.98 ? 163  SER A N     1 
ATOM   1027  C CA    . SER A  1 165  ? -7.595  54.368  75.805  1.00 22.29 ? 163  SER A CA    1 
ATOM   1028  C C     . SER A  1 165  ? -8.335  54.220  74.482  1.00 22.48 ? 163  SER A C     1 
ATOM   1029  O O     . SER A  1 165  ? -7.954  53.405  73.635  1.00 19.47 ? 163  SER A O     1 
ATOM   1030  C CB    . SER A  1 165  ? -8.323  53.568  76.883  1.00 24.28 ? 163  SER A CB    1 
ATOM   1031  O OG    . SER A  1 165  ? -8.503  52.236  76.458  1.00 21.04 ? 163  SER A OG    1 
ATOM   1032  N N     . LEU A  1 166  ? -9.417  54.973  74.300  1.00 20.51 ? 164  LEU A N     1 
ATOM   1033  C CA    . LEU A  1 166  ? -10.168 54.868  73.051  1.00 20.31 ? 164  LEU A CA    1 
ATOM   1034  C C     . LEU A  1 166  ? -9.382  55.439  71.873  1.00 21.55 ? 164  LEU A C     1 
ATOM   1035  O O     . LEU A  1 166  ? -9.432  54.891  70.762  1.00 19.94 ? 164  LEU A O     1 
ATOM   1036  C CB    . LEU A  1 166  ? -11.517 55.555  73.203  1.00 20.65 ? 164  LEU A CB    1 
ATOM   1037  C CG    . LEU A  1 166  ? -12.427 54.891  74.240  1.00 20.96 ? 164  LEU A CG    1 
ATOM   1038  C CD1   . LEU A  1 166  ? -13.629 55.779  74.459  1.00 23.59 ? 164  LEU A CD1   1 
ATOM   1039  C CD2   . LEU A  1 166  ? -12.896 53.514  73.769  1.00 18.78 ? 164  LEU A CD2   1 
ATOM   1040  N N     . ALA A  1 167  ? -8.651  56.538  72.082  1.00 19.55 ? 165  ALA A N     1 
ATOM   1041  C CA    . ALA A  1 167  ? -7.845  57.062  70.979  1.00 24.64 ? 165  ALA A CA    1 
ATOM   1042  C C     . ALA A  1 167  ? -6.770  56.056  70.568  1.00 23.31 ? 165  ALA A C     1 
ATOM   1043  O O     . ALA A  1 167  ? -6.498  55.885  69.376  1.00 20.78 ? 165  ALA A O     1 
ATOM   1044  C CB    . ALA A  1 167  ? -7.201  58.394  71.356  1.00 24.72 ? 165  ALA A CB    1 
ATOM   1045  N N     . ALA A  1 168  ? -6.154  55.375  71.541  1.00 20.04 ? 166  ALA A N     1 
ATOM   1046  C CA    . ALA A  1 168  ? -5.156  54.361  71.194  1.00 24.72 ? 166  ALA A CA    1 
ATOM   1047  C C     . ALA A  1 168  ? -5.806  53.208  70.436  1.00 22.53 ? 166  ALA A C     1 
ATOM   1048  O O     . ALA A  1 168  ? -5.274  52.730  69.426  1.00 22.38 ? 166  ALA A O     1 
ATOM   1049  C CB    . ALA A  1 168  ? -4.447  53.860  72.459  1.00 22.69 ? 166  ALA A CB    1 
ATOM   1050  N N     . ALA A  1 169  ? -6.993  52.782  70.884  1.00 23.29 ? 167  ALA A N     1 
ATOM   1051  C CA    . ALA A  1 169  ? -7.675  51.667  70.240  1.00 22.85 ? 167  ALA A CA    1 
ATOM   1052  C C     . ALA A  1 169  ? -8.069  52.021  68.814  1.00 21.19 ? 167  ALA A C     1 
ATOM   1053  O O     . ALA A  1 169  ? -7.950  51.193  67.906  1.00 20.53 ? 167  ALA A O     1 
ATOM   1054  C CB    . ALA A  1 169  ? -8.909  51.261  71.057  1.00 21.22 ? 167  ALA A CB    1 
ATOM   1055  N N     . LEU A  1 170  ? -8.514  53.259  68.596  1.00 23.99 ? 168  LEU A N     1 
ATOM   1056  C CA    . LEU A  1 170  ? -8.947  53.670  67.263  1.00 22.91 ? 168  LEU A CA    1 
ATOM   1057  C C     . LEU A  1 170  ? -7.777  53.710  66.296  1.00 23.61 ? 168  LEU A C     1 
ATOM   1058  O O     . LEU A  1 170  ? -7.895  53.272  65.146  1.00 23.27 ? 168  LEU A O     1 
ATOM   1059  C CB    . LEU A  1 170  ? -9.617  55.037  67.341  1.00 24.52 ? 168  LEU A CB    1 
ATOM   1060  C CG    . LEU A  1 170  ? -10.188 55.507  66.005  1.00 23.33 ? 168  LEU A CG    1 
ATOM   1061  C CD1   . LEU A  1 170  ? -11.186 54.488  65.497  1.00 23.83 ? 168  LEU A CD1   1 
ATOM   1062  C CD2   . LEU A  1 170  ? -10.874 56.854  66.180  1.00 31.07 ? 168  LEU A CD2   1 
ATOM   1063  N N     . THR A  1 171  ? -6.639  54.249  66.744  1.00 22.63 ? 169  THR A N     1 
ATOM   1064  C CA    . THR A  1 171  ? -5.433  54.246  65.918  1.00 26.55 ? 169  THR A CA    1 
ATOM   1065  C C     . THR A  1 171  ? -5.007  52.817  65.600  1.00 27.14 ? 169  THR A C     1 
ATOM   1066  O O     . THR A  1 171  ? -4.712  52.478  64.446  1.00 25.26 ? 169  THR A O     1 
ATOM   1067  C CB    . THR A  1 171  ? -4.316  55.001  66.648  1.00 24.25 ? 169  THR A CB    1 
ATOM   1068  O OG1   . THR A  1 171  ? -4.712  56.360  66.835  1.00 29.01 ? 169  THR A OG1   1 
ATOM   1069  C CG2   . THR A  1 171  ? -2.993  54.956  65.864  1.00 28.75 ? 169  THR A CG2   1 
ATOM   1070  N N     . ARG A  1 172  ? -5.017  51.951  66.613  1.00 23.44 ? 170  ARG A N     1 
ATOM   1071  C CA    . ARG A  1 172  ? -4.621  50.563  66.407  1.00 26.00 ? 170  ARG A CA    1 
ATOM   1072  C C     . ARG A  1 172  ? -5.530  49.871  65.391  1.00 24.56 ? 170  ARG A C     1 
ATOM   1073  O O     . ARG A  1 172  ? -5.049  49.209  64.465  1.00 26.68 ? 170  ARG A O     1 
ATOM   1074  C CB    . ARG A  1 172  ? -4.622  49.823  67.751  1.00 24.42 ? 170  ARG A CB    1 
ATOM   1075  C CG    . ARG A  1 172  ? -3.910  48.462  67.708  1.00 25.85 ? 170  ARG A CG    1 
ATOM   1076  C CD    . ARG A  1 172  ? -4.128  47.686  69.000  1.00 25.46 ? 170  ARG A CD    1 
ATOM   1077  N NE    . ARG A  1 172  ? -3.856  48.473  70.197  1.00 22.15 ? 170  ARG A NE    1 
ATOM   1078  C CZ    . ARG A  1 172  ? -4.799  48.941  71.009  1.00 21.08 ? 170  ARG A CZ    1 
ATOM   1079  N NH1   . ARG A  1 172  ? -6.089  48.736  70.767  1.00 23.21 ? 170  ARG A NH1   1 
ATOM   1080  N NH2   . ARG A  1 172  ? -4.441  49.633  72.089  1.00 22.43 ? 170  ARG A NH2   1 
ATOM   1081  N N     . LEU A  1 173  ? -6.859  50.014  65.541  1.00 24.03 ? 171  LEU A N     1 
ATOM   1082  C CA    . LEU A  1 173  ? -7.747  49.262  64.669  1.00 25.70 ? 171  LEU A CA    1 
ATOM   1083  C C     . LEU A  1 173  ? -7.700  49.796  63.247  1.00 26.13 ? 171  LEU A C     1 
ATOM   1084  O O     . LEU A  1 173  ? -7.804  49.018  62.290  1.00 23.97 ? 171  LEU A O     1 
ATOM   1085  C CB    . LEU A  1 173  ? -9.186  49.262  65.215  1.00 25.59 ? 171  LEU A CB    1 
ATOM   1086  C CG    . LEU A  1 173  ? -10.066 50.516  65.188  1.00 24.53 ? 171  LEU A CG    1 
ATOM   1087  C CD1   . LEU A  1 173  ? -10.849 50.583  63.879  1.00 26.86 ? 171  LEU A CD1   1 
ATOM   1088  C CD2   . LEU A  1 173  ? -11.026 50.559  66.370  1.00 24.89 ? 171  LEU A CD2   1 
ATOM   1089  N N     . ILE A  1 174  ? -7.530  51.104  63.082  1.00 25.26 ? 172  ILE A N     1 
ATOM   1090  C CA    . ILE A  1 174  ? -7.451  51.655  61.729  1.00 28.30 ? 172  ILE A CA    1 
ATOM   1091  C C     . ILE A  1 174  ? -6.158  51.215  61.053  1.00 26.03 ? 172  ILE A C     1 
ATOM   1092  O O     . ILE A  1 174  ? -6.157  50.778  59.892  1.00 30.97 ? 172  ILE A O     1 
ATOM   1093  C CB    . ILE A  1 174  ? -7.591  53.188  61.762  1.00 28.72 ? 172  ILE A CB    1 
ATOM   1094  C CG1   . ILE A  1 174  ? -9.046  53.579  62.066  1.00 28.08 ? 172  ILE A CG1   1 
ATOM   1095  C CG2   . ILE A  1 174  ? -7.187  53.793  60.417  1.00 30.99 ? 172  ILE A CG2   1 
ATOM   1096  C CD1   . ILE A  1 174  ? -9.243  55.048  62.346  1.00 30.08 ? 172  ILE A CD1   1 
ATOM   1097  N N     . SER A  1 175  ? -5.039  51.300  61.774  1.00 28.46 ? 173  SER A N     1 
ATOM   1098  C CA    . SER A  1 175  ? -3.757  50.905  61.190  1.00 29.11 ? 173  SER A CA    1 
ATOM   1099  C C     . SER A  1 175  ? -3.715  49.411  60.892  1.00 32.25 ? 173  SER A C     1 
ATOM   1100  O O     . SER A  1 175  ? -2.998  48.978  59.980  1.00 32.08 ? 173  SER A O     1 
ATOM   1101  C CB    . SER A  1 175  ? -2.620  51.286  62.124  1.00 29.87 ? 173  SER A CB    1 
ATOM   1102  O OG    . SER A  1 175  ? -2.501  52.690  62.230  1.00 34.42 ? 173  SER A OG    1 
ATOM   1103  N N     . ARG A  1 176  ? -4.504  48.620  61.619  1.00 28.90 ? 174  ARG A N     1 
ATOM   1104  C CA    . ARG A  1 176  ? -4.521  47.174  61.429  1.00 33.10 ? 174  ARG A CA    1 
ATOM   1105  C C     . ARG A  1 176  ? -5.433  46.767  60.280  1.00 32.91 ? 174  ARG A C     1 
ATOM   1106  O O     . ARG A  1 176  ? -5.040  45.968  59.427  1.00 34.16 ? 174  ARG A O     1 
ATOM   1107  C CB    . ARG A  1 176  ? -4.956  46.474  62.725  1.00 34.26 ? 174  ARG A CB    1 
ATOM   1108  C CG    . ARG A  1 176  ? -4.729  44.946  62.710  1.00 33.59 ? 174  ARG A CG    1 
ATOM   1109  C CD    . ARG A  1 176  ? -5.058  44.275  64.051  1.00 29.92 ? 174  ARG A CD    1 
ATOM   1110  N NE    . ARG A  1 176  ? -6.486  44.299  64.385  1.00 29.22 ? 174  ARG A NE    1 
ATOM   1111  C CZ    . ARG A  1 176  ? -7.039  45.012  65.361  1.00 30.51 ? 174  ARG A CZ    1 
ATOM   1112  N NH1   . ARG A  1 176  ? -6.317  45.802  66.150  1.00 27.83 ? 174  ARG A NH1   1 
ATOM   1113  N NH2   . ARG A  1 176  ? -8.356  44.927  65.560  1.00 30.95 ? 174  ARG A NH2   1 
ATOM   1114  N N     . CYS A  1 177  ? -6.653  47.315  60.231  1.00 32.04 ? 175  CYS A N     1 
ATOM   1115  C CA    . CYS A  1 177  ? -7.669  46.852  59.291  1.00 32.28 ? 175  CYS A CA    1 
ATOM   1116  C C     . CYS A  1 177  ? -8.108  47.878  58.253  1.00 36.56 ? 175  CYS A C     1 
ATOM   1117  O O     . CYS A  1 177  ? -8.769  47.486  57.289  1.00 37.26 ? 175  CYS A O     1 
ATOM   1118  C CB    . CYS A  1 177  ? -8.936  46.390  60.037  1.00 32.01 ? 175  CYS A CB    1 
ATOM   1119  S SG    . CYS A  1 177  ? -8.648  45.354  61.506  1.00 38.74 ? 175  CYS A SG    1 
ATOM   1120  N N     . GLY A  1 178  ? -7.847  49.169  58.459  1.00 36.06 ? 176  GLY A N     1 
ATOM   1121  C CA    . GLY A  1 178  ? -8.023  50.152  57.400  1.00 34.63 ? 176  GLY A CA    1 
ATOM   1122  C C     . GLY A  1 178  ? -9.469  50.441  57.017  1.00 34.29 ? 176  GLY A C     1 
ATOM   1123  O O     . GLY A  1 178  ? -10.405 50.318  57.809  1.00 31.88 ? 176  GLY A O     1 
ATOM   1124  N N     . GLU A  1 179  ? -9.638  50.844  55.763  1.00 34.60 ? 177  GLU A N     1 
ATOM   1125  C CA    . GLU A  1 179  ? -10.948 51.298  55.303  1.00 33.84 ? 177  GLU A CA    1 
ATOM   1126  C C     . GLU A  1 179  ? -12.062 50.268  55.476  1.00 32.66 ? 177  GLU A C     1 
ATOM   1127  O O     . GLU A  1 179  ? -13.171 50.669  55.874  1.00 36.03 ? 177  GLU A O     1 
ATOM   1128  C CB    . GLU A  1 179  ? -10.829 51.757  53.842  1.00 34.80 ? 177  GLU A CB    1 
ATOM   1129  C CG    . GLU A  1 179  ? -12.073 52.444  53.294  1.00 42.33 ? 177  GLU A CG    1 
ATOM   1130  C CD    . GLU A  1 179  ? -12.765 51.623  52.231  1.00 53.54 ? 177  GLU A CD    1 
ATOM   1131  O OE1   . GLU A  1 179  ? -13.116 50.457  52.518  1.00 53.86 ? 177  GLU A OE1   1 
ATOM   1132  O OE2   . GLU A  1 179  ? -12.944 52.135  51.100  1.00 61.87 ? 177  GLU A OE2   1 
ATOM   1133  N N     . PRO A  1 180  ? -11.868 48.968  55.202  1.00 30.00 ? 178  PRO A N     1 
ATOM   1134  C CA    . PRO A  1 180  ? -12.989 48.028  55.359  1.00 34.03 ? 178  PRO A CA    1 
ATOM   1135  C C     . PRO A  1 180  ? -13.651 48.048  56.728  1.00 33.32 ? 178  PRO A C     1 
ATOM   1136  O O     . PRO A  1 180  ? -14.882 47.925  56.803  1.00 35.17 ? 178  PRO A O     1 
ATOM   1137  C CB    . PRO A  1 180  ? -12.330 46.676  55.061  1.00 35.67 ? 178  PRO A CB    1 
ATOM   1138  C CG    . PRO A  1 180  ? -11.312 47.013  54.051  1.00 36.26 ? 178  PRO A CG    1 
ATOM   1139  C CD    . PRO A  1 180  ? -10.718 48.308  54.551  1.00 34.63 ? 178  PRO A CD    1 
ATOM   1140  N N     . VAL A  1 181  ? -12.890 48.204  57.814  1.00 32.20 ? 179  VAL A N     1 
ATOM   1141  C CA    . VAL A  1 181  ? -13.532 48.183  59.126  1.00 31.37 ? 179  VAL A CA    1 
ATOM   1142  C C     . VAL A  1 181  ? -14.277 49.499  59.390  1.00 30.89 ? 179  VAL A C     1 
ATOM   1143  O O     . VAL A  1 181  ? -15.326 49.498  60.040  1.00 28.10 ? 179  VAL A O     1 
ATOM   1144  C CB    . VAL A  1 181  ? -12.502 47.862  60.235  1.00 29.94 ? 179  VAL A CB    1 
ATOM   1145  C CG1   . VAL A  1 181  ? -11.516 49.008  60.455  1.00 29.87 ? 179  VAL A CG1   1 
ATOM   1146  C CG2   . VAL A  1 181  ? -13.215 47.472  61.530  1.00 29.14 ? 179  VAL A CG2   1 
ATOM   1147  N N     . ILE A  1 182  ? -13.766 50.623  58.881  1.00 32.28 ? 180  ILE A N     1 
ATOM   1148  C CA    . ILE A  1 182  ? -14.461 51.899  59.016  1.00 27.86 ? 180  ILE A CA    1 
ATOM   1149  C C     . ILE A  1 182  ? -15.796 51.857  58.280  1.00 30.97 ? 180  ILE A C     1 
ATOM   1150  O O     . ILE A  1 182  ? -16.829 52.290  58.804  1.00 30.41 ? 180  ILE A O     1 
ATOM   1151  C CB    . ILE A  1 182  ? -13.581 53.051  58.497  1.00 29.99 ? 180  ILE A CB    1 
ATOM   1152  C CG1   . ILE A  1 182  ? -12.213 53.067  59.193  1.00 31.03 ? 180  ILE A CG1   1 
ATOM   1153  C CG2   . ILE A  1 182  ? -14.290 54.388  58.711  1.00 29.72 ? 180  ILE A CG2   1 
ATOM   1154  C CD1   . ILE A  1 182  ? -11.235 54.048  58.582  1.00 36.76 ? 180  ILE A CD1   1 
ATOM   1155  N N     . ARG A  1 183  ? -15.782 51.353  57.042  1.00 31.74 ? 181  ARG A N     1 
ATOM   1156  C CA    . ARG A  1 183  ? -17.011 51.206  56.263  1.00 35.54 ? 181  ARG A CA    1 
ATOM   1157  C C     . ARG A  1 183  ? -18.049 50.369  57.010  1.00 35.66 ? 181  ARG A C     1 
ATOM   1158  O O     . ARG A  1 183  ? -19.224 50.753  57.110  1.00 33.15 ? 181  ARG A O     1 
ATOM   1159  C CB    . ARG A  1 183  ? -16.670 50.588  54.903  1.00 33.74 ? 181  ARG A CB    1 
ATOM   1160  C CG    . ARG A  1 183  ? -17.869 50.174  54.039  1.00 43.84 ? 181  ARG A CG    1 
ATOM   1161  C CD    . ARG A  1 183  ? -18.391 51.321  53.186  1.00 45.35 ? 181  ARG A CD    1 
ATOM   1162  N NE    . ARG A  1 183  ? -19.403 52.108  53.879  1.00 45.11 ? 181  ARG A NE    1 
ATOM   1163  C CZ    . ARG A  1 183  ? -19.367 53.425  54.034  1.00 46.72 ? 181  ARG A CZ    1 
ATOM   1164  N NH1   . ARG A  1 183  ? -18.374 54.156  53.546  1.00 42.78 ? 181  ARG A NH1   1 
ATOM   1165  N NH2   . ARG A  1 183  ? -20.361 54.027  54.681  1.00 43.68 ? 181  ARG A NH2   1 
ATOM   1166  N N     . ARG A  1 184  ? -17.627 49.224  57.558  1.00 34.65 ? 182  ARG A N     1 
ATOM   1167  C CA    . ARG A  1 184  ? -18.556 48.367  58.290  1.00 35.62 ? 182  ARG A CA    1 
ATOM   1168  C C     . ARG A  1 184  ? -19.078 49.053  59.551  1.00 29.69 ? 182  ARG A C     1 
ATOM   1169  O O     . ARG A  1 184  ? -20.258 48.909  59.896  1.00 34.29 ? 182  ARG A O     1 
ATOM   1170  C CB    . ARG A  1 184  ? -17.885 47.040  58.643  1.00 34.64 ? 182  ARG A CB    1 
ATOM   1171  C CG    . ARG A  1 184  ? -17.876 46.017  57.518  1.00 37.40 ? 182  ARG A CG    1 
ATOM   1172  C CD    . ARG A  1 184  ? -19.113 45.111  57.571  1.00 37.60 ? 182  ARG A CD    1 
ATOM   1173  N NE    . ARG A  1 184  ? -18.911 43.938  58.420  1.00 38.62 ? 182  ARG A NE    1 
ATOM   1174  C CZ    . ARG A  1 184  ? -19.689 43.580  59.437  1.00 39.53 ? 182  ARG A CZ    1 
ATOM   1175  N NH1   . ARG A  1 184  ? -20.778 44.264  59.756  1.00 41.14 ? 182  ARG A NH1   1 
ATOM   1176  N NH2   . ARG A  1 184  ? -19.370 42.502  60.148  1.00 38.90 ? 182  ARG A NH2   1 
ATOM   1177  N N     . GLY A  1 185  ? -18.216 49.783  60.258  1.00 28.18 ? 183  GLY A N     1 
ATOM   1178  C CA    . GLY A  1 185  ? -18.669 50.513  61.432  1.00 30.42 ? 183  GLY A CA    1 
ATOM   1179  C C     . GLY A  1 185  ? -19.688 51.586  61.090  1.00 30.67 ? 183  GLY A C     1 
ATOM   1180  O O     . GLY A  1 185  ? -20.703 51.729  61.773  1.00 29.64 ? 183  GLY A O     1 
ATOM   1181  N N     . VAL A  1 186  ? -19.453 52.330  60.004  1.00 30.13 ? 184  VAL A N     1 
ATOM   1182  C CA    . VAL A  1 186  ? -20.381 53.390  59.614  1.00 31.77 ? 184  VAL A CA    1 
ATOM   1183  C C     . VAL A  1 186  ? -21.736 52.801  59.257  1.00 31.30 ? 184  VAL A C     1 
ATOM   1184  O O     . VAL A  1 186  ? -22.783 53.301  59.682  1.00 32.52 ? 184  VAL A O     1 
ATOM   1185  C CB    . VAL A  1 186  ? -19.804 54.210  58.448  1.00 35.30 ? 184  VAL A CB    1 
ATOM   1186  C CG1   . VAL A  1 186  ? -20.880 55.118  57.844  1.00 33.32 ? 184  VAL A CG1   1 
ATOM   1187  C CG2   . VAL A  1 186  ? -18.631 55.030  58.933  1.00 25.34 ? 184  VAL A CG2   1 
ATOM   1188  N N     . ASP A  1 187  ? -21.734 51.729  58.467  1.00 33.52 ? 185  ASP A N     1 
ATOM   1189  C CA    . ASP A  1 187  ? -22.987 51.099  58.066  1.00 34.55 ? 185  ASP A CA    1 
ATOM   1190  C C     . ASP A  1 187  ? -23.726 50.510  59.262  1.00 35.47 ? 185  ASP A C     1 
ATOM   1191  O O     . ASP A  1 187  ? -24.956 50.627  59.359  1.00 37.23 ? 185  ASP A O     1 
ATOM   1192  C CB    . ASP A  1 187  ? -22.705 50.038  57.008  1.00 34.52 ? 185  ASP A CB    1 
ATOM   1193  C CG    . ASP A  1 187  ? -22.151 50.642  55.731  1.00 42.11 ? 185  ASP A CG    1 
ATOM   1194  O OD1   . ASP A  1 187  ? -22.356 51.862  55.537  1.00 45.12 ? 185  ASP A OD1   1 
ATOM   1195  O OD2   . ASP A  1 187  ? -21.506 49.916  54.937  1.00 38.79 ? 185  ASP A OD2   1 
ATOM   1196  N N     . MET A  1 188  ? -22.994 49.877  60.183  1.00 34.47 ? 186  MET A N     1 
ATOM   1197  C CA    . MET A  1 188  ? -23.586 49.406  61.435  1.00 31.99 ? 186  MET A CA    1 
ATOM   1198  C C     . MET A  1 188  ? -24.216 50.551  62.223  1.00 32.20 ? 186  MET A C     1 
ATOM   1199  O O     . MET A  1 188  ? -25.389 50.478  62.623  1.00 35.99 ? 186  MET A O     1 
ATOM   1200  C CB    . MET A  1 188  ? -22.518 48.708  62.282  1.00 33.63 ? 186  MET A CB    1 
ATOM   1201  C CG    . MET A  1 188  ? -23.053 48.075  63.569  1.00 39.41 ? 186  MET A CG    1 
ATOM   1202  S SD    . MET A  1 188  ? -24.143 46.687  63.204  1.00 56.31 ? 186  MET A SD    1 
ATOM   1203  C CE    . MET A  1 188  ? -22.995 45.627  62.310  1.00 41.63 ? 186  MET A CE    1 
ATOM   1204  N N     . ALA A  1 189  ? -23.448 51.612  62.478  1.00 30.27 ? 187  ALA A N     1 
ATOM   1205  C CA    . ALA A  1 189  ? -23.977 52.735  63.244  1.00 30.27 ? 187  ALA A CA    1 
ATOM   1206  C C     . ALA A  1 189  ? -25.162 53.368  62.538  1.00 28.99 ? 187  ALA A C     1 
ATOM   1207  O O     . ALA A  1 189  ? -26.087 53.847  63.197  1.00 31.21 ? 187  ALA A O     1 
ATOM   1208  C CB    . ALA A  1 189  ? -22.901 53.790  63.480  1.00 29.61 ? 187  ALA A CB    1 
ATOM   1209  N N     . MET A  1 190  ? -25.138 53.390  61.202  1.00 29.90 ? 188  MET A N     1 
ATOM   1210  C CA    . MET A  1 190  ? -26.233 53.986  60.443  1.00 36.64 ? 188  MET A CA    1 
ATOM   1211  C C     . MET A  1 190  ? -27.527 53.209  60.639  1.00 34.77 ? 188  MET A C     1 
ATOM   1212  O O     . MET A  1 190  ? -28.589 53.808  60.835  1.00 36.45 ? 188  MET A O     1 
ATOM   1213  C CB    . MET A  1 190  ? -25.875 54.053  58.957  1.00 31.15 ? 188  MET A CB    1 
ATOM   1214  C CG    . MET A  1 190  ? -26.869 54.850  58.133  1.00 40.73 ? 188  MET A CG    1 
ATOM   1215  S SD    . MET A  1 190  ? -26.394 54.949  56.394  1.00 51.85 ? 188  MET A SD    1 
ATOM   1216  C CE    . MET A  1 190  ? -24.742 55.636  56.478  1.00 45.11 ? 188  MET A CE    1 
ATOM   1217  N N     . ARG A  1 191  ? -27.455 51.874  60.596  1.00 34.04 ? 189  ARG A N     1 
ATOM   1218  C CA    . ARG A  1 191  ? -28.646 51.065  60.836  1.00 35.07 ? 189  ARG A CA    1 
ATOM   1219  C C     . ARG A  1 191  ? -29.117 51.183  62.281  1.00 36.72 ? 189  ARG A C     1 
ATOM   1220  O O     . ARG A  1 191  ? -30.324 51.265  62.539  1.00 34.59 ? 189  ARG A O     1 
ATOM   1221  C CB    . ARG A  1 191  ? -28.385 49.601  60.486  1.00 32.76 ? 189  ARG A CB    1 
ATOM   1222  N N     . MET A  1 192  ? -28.188 51.183  63.239  1.00 31.88 ? 190  MET A N     1 
ATOM   1223  C CA    . MET A  1 192  ? -28.600 51.191  64.638  1.00 31.88 ? 190  MET A CA    1 
ATOM   1224  C C     . MET A  1 192  ? -29.293 52.496  65.002  1.00 33.64 ? 190  MET A C     1 
ATOM   1225  O O     . MET A  1 192  ? -30.371 52.495  65.612  1.00 33.16 ? 190  MET A O     1 
ATOM   1226  C CB    . MET A  1 192  ? -27.396 50.968  65.546  1.00 34.84 ? 190  MET A CB    1 
ATOM   1227  C CG    . MET A  1 192  ? -26.795 49.592  65.464  1.00 35.49 ? 190  MET A CG    1 
ATOM   1228  S SD    . MET A  1 192  ? -25.508 49.473  66.724  1.00 42.84 ? 190  MET A SD    1 
ATOM   1229  C CE    . MET A  1 192  ? -26.470 48.955  68.136  1.00 40.99 ? 190  MET A CE    1 
ATOM   1230  N N     . MET A  1 193  ? -28.676 53.619  64.648  1.00 29.14 ? 191  MET A N     1 
ATOM   1231  C CA    . MET A  1 193  ? -29.181 54.926  65.031  1.00 35.74 ? 191  MET A CA    1 
ATOM   1232  C C     . MET A  1 193  ? -30.336 55.394  64.158  1.00 34.14 ? 191  MET A C     1 
ATOM   1233  O O     . MET A  1 193  ? -31.089 56.280  64.574  1.00 34.91 ? 191  MET A O     1 
ATOM   1234  C CB    . MET A  1 193  ? -28.050 55.952  64.977  1.00 34.28 ? 191  MET A CB    1 
ATOM   1235  C CG    . MET A  1 193  ? -26.986 55.758  66.051  1.00 33.02 ? 191  MET A CG    1 
ATOM   1236  S SD    . MET A  1 193  ? -25.931 57.213  66.239  1.00 43.70 ? 191  MET A SD    1 
ATOM   1237  C CE    . MET A  1 193  ? -25.129 57.252  64.651  1.00 34.77 ? 191  MET A CE    1 
ATOM   1238  N N     . GLY A  1 194  ? -30.496 54.823  62.969  1.00 35.44 ? 192  GLY A N     1 
ATOM   1239  C CA    . GLY A  1 194  ? -31.552 55.251  62.073  1.00 32.63 ? 192  GLY A CA    1 
ATOM   1240  C C     . GLY A  1 194  ? -32.745 54.315  62.036  1.00 38.19 ? 192  GLY A C     1 
ATOM   1241  O O     . GLY A  1 194  ? -33.847 54.747  61.683  1.00 36.85 ? 192  GLY A O     1 
ATOM   1242  N N     . GLU A  1 195  ? -32.548 53.040  62.408  1.00 34.70 ? 193  GLU A N     1 
ATOM   1243  C CA    . GLU A  1 195  ? -33.595 52.027  62.288  1.00 35.01 ? 193  GLU A CA    1 
ATOM   1244  C C     . GLU A  1 195  ? -33.865 51.205  63.539  1.00 30.76 ? 193  GLU A C     1 
ATOM   1245  O O     . GLU A  1 195  ? -34.940 50.598  63.614  1.00 28.21 ? 193  GLU A O     1 
ATOM   1246  C CB    . GLU A  1 195  ? -33.276 51.041  61.160  1.00 35.04 ? 193  GLU A CB    1 
ATOM   1247  C CG    . GLU A  1 195  ? -33.091 51.676  59.816  1.00 45.37 ? 193  GLU A CG    1 
ATOM   1248  C CD    . GLU A  1 195  ? -32.350 50.759  58.884  1.00 48.95 ? 193  GLU A CD    1 
ATOM   1249  O OE1   . GLU A  1 195  ? -32.788 49.595  58.734  1.00 49.72 ? 193  GLU A OE1   1 
ATOM   1250  O OE2   . GLU A  1 195  ? -31.311 51.191  58.340  1.00 53.07 ? 193  GLU A OE2   1 
ATOM   1251  N N     . GLN A  1 196  ? -32.952 51.151  64.510  1.00 32.26 ? 194  GLN A N     1 
ATOM   1252  C CA    . GLN A  1 196  ? -33.090 50.271  65.666  1.00 31.79 ? 194  GLN A CA    1 
ATOM   1253  C C     . GLN A  1 196  ? -33.326 51.035  66.960  1.00 33.13 ? 194  GLN A C     1 
ATOM   1254  O O     . GLN A  1 196  ? -34.263 50.726  67.699  1.00 34.10 ? 194  GLN A O     1 
ATOM   1255  C CB    . GLN A  1 196  ? -31.848 49.371  65.801  1.00 35.58 ? 194  GLN A CB    1 
ATOM   1256  C CG    . GLN A  1 196  ? -31.608 48.463  64.572  1.00 41.51 ? 194  GLN A CG    1 
ATOM   1257  C CD    . GLN A  1 196  ? -30.321 47.636  64.664  1.00 41.52 ? 194  GLN A CD    1 
ATOM   1258  O OE1   . GLN A  1 196  ? -29.754 47.458  65.746  1.00 47.70 ? 194  GLN A OE1   1 
ATOM   1259  N NE2   . GLN A  1 196  ? -29.858 47.131  63.519  1.00 41.83 ? 194  GLN A NE2   1 
ATOM   1260  N N     . PHE A  1 197  ? -32.514 52.047  67.250  1.00 33.28 ? 195  PHE A N     1 
ATOM   1261  C CA    . PHE A  1 197  ? -32.759 52.854  68.441  1.00 30.15 ? 195  PHE A CA    1 
ATOM   1262  C C     . PHE A  1 197  ? -33.937 53.784  68.241  1.00 31.31 ? 195  PHE A C     1 
ATOM   1263  O O     . PHE A  1 197  ? -34.600 54.159  69.210  1.00 30.93 ? 195  PHE A O     1 
ATOM   1264  C CB    . PHE A  1 197  ? -31.520 53.649  68.799  1.00 31.31 ? 195  PHE A CB    1 
ATOM   1265  C CG    . PHE A  1 197  ? -30.376 52.784  69.231  1.00 36.26 ? 195  PHE A CG    1 
ATOM   1266  C CD1   . PHE A  1 197  ? -30.609 51.669  70.012  1.00 39.19 ? 195  PHE A CD1   1 
ATOM   1267  C CD2   . PHE A  1 197  ? -29.087 53.066  68.831  1.00 36.29 ? 195  PHE A CD2   1 
ATOM   1268  C CE1   . PHE A  1 197  ? -29.567 50.853  70.414  1.00 44.72 ? 195  PHE A CE1   1 
ATOM   1269  C CE2   . PHE A  1 197  ? -28.038 52.255  69.230  1.00 39.77 ? 195  PHE A CE2   1 
ATOM   1270  C CZ    . PHE A  1 197  ? -28.284 51.151  70.020  1.00 35.80 ? 195  PHE A CZ    1 
ATOM   1271  N N     . VAL A  1 198  ? -34.216 54.159  67.001  1.00 27.80 ? 196  VAL A N     1 
ATOM   1272  C CA    . VAL A  1 198  ? -35.423 54.903  66.683  1.00 29.31 ? 196  VAL A CA    1 
ATOM   1273  C C     . VAL A  1 198  ? -36.150 54.173  65.564  1.00 29.21 ? 196  VAL A C     1 
ATOM   1274  O O     . VAL A  1 198  ? -35.556 53.418  64.790  1.00 30.91 ? 196  VAL A O     1 
ATOM   1275  C CB    . VAL A  1 198  ? -35.136 56.374  66.284  1.00 27.10 ? 196  VAL A CB    1 
ATOM   1276  C CG1   . VAL A  1 198  ? -34.426 57.113  67.409  1.00 27.66 ? 196  VAL A CG1   1 
ATOM   1277  C CG2   . VAL A  1 198  ? -34.329 56.439  64.998  1.00 32.07 ? 196  VAL A CG2   1 
ATOM   1278  N N     . THR A  1 199  ? -37.459 54.375  65.501  1.00 28.20 ? 197  THR A N     1 
ATOM   1279  C CA    . THR A  1 199  ? -38.190 53.870  64.351  1.00 28.33 ? 197  THR A CA    1 
ATOM   1280  C C     . THR A  1 199  ? -37.882 54.703  63.115  1.00 31.15 ? 197  THR A C     1 
ATOM   1281  O O     . THR A  1 199  ? -37.848 54.174  61.999  1.00 35.68 ? 197  THR A O     1 
ATOM   1282  C CB    . THR A  1 199  ? -39.687 53.854  64.662  1.00 31.91 ? 197  THR A CB    1 
ATOM   1283  O OG1   . THR A  1 199  ? -39.914 53.038  65.820  1.00 30.82 ? 197  THR A OG1   1 
ATOM   1284  C CG2   . THR A  1 199  ? -40.463 53.283  63.517  1.00 31.35 ? 197  THR A CG2   1 
ATOM   1285  N N     . GLY A  1 200  ? -37.633 55.989  63.298  1.00 30.20 ? 198  GLY A N     1 
ATOM   1286  C CA    . GLY A  1 200  ? -37.235 56.851  62.204  1.00 33.70 ? 198  GLY A CA    1 
ATOM   1287  C C     . GLY A  1 200  ? -36.720 58.164  62.743  1.00 32.98 ? 198  GLY A C     1 
ATOM   1288  O O     . GLY A  1 200  ? -36.929 58.503  63.913  1.00 32.94 ? 198  GLY A O     1 
ATOM   1289  N N     . GLU A  1 201  ? -36.032 58.899  61.867  1.00 30.38 ? 199  GLU A N     1 
ATOM   1290  C CA    . GLU A  1 201  ? -35.452 60.182  62.252  1.00 32.46 ? 199  GLU A CA    1 
ATOM   1291  C C     . GLU A  1 201  ? -36.516 61.262  62.377  1.00 33.14 ? 199  GLU A C     1 
ATOM   1292  O O     . GLU A  1 201  ? -36.382 62.174  63.201  1.00 31.01 ? 199  GLU A O     1 
ATOM   1293  C CB    . GLU A  1 201  ? -34.399 60.593  61.217  1.00 36.29 ? 199  GLU A CB    1 
ATOM   1294  C CG    . GLU A  1 201  ? -33.784 61.969  61.413  1.00 42.22 ? 199  GLU A CG    1 
ATOM   1295  C CD    . GLU A  1 201  ? -32.796 62.318  60.296  1.00 46.73 ? 199  GLU A CD    1 
ATOM   1296  O OE1   . GLU A  1 201  ? -33.041 61.912  59.136  1.00 50.29 ? 199  GLU A OE1   1 
ATOM   1297  O OE2   . GLU A  1 201  ? -31.771 62.979  60.584  1.00 51.34 ? 199  GLU A OE2   1 
ATOM   1298  N N     . THR A  1 202  ? -37.567 61.174  61.565  1.00 30.69 ? 200  THR A N     1 
ATOM   1299  C CA    . THR A  1 202  ? -38.686 62.105  61.574  1.00 28.83 ? 200  THR A CA    1 
ATOM   1300  C C     . THR A  1 202  ? -39.983 61.307  61.674  1.00 30.08 ? 200  THR A C     1 
ATOM   1301  O O     . THR A  1 202  ? -40.015 60.104  61.396  1.00 29.59 ? 200  THR A O     1 
ATOM   1302  C CB    . THR A  1 202  ? -38.707 62.947  60.302  1.00 30.99 ? 200  THR A CB    1 
ATOM   1303  O OG1   . THR A  1 202  ? -38.880 62.058  59.189  1.00 32.67 ? 200  THR A OG1   1 
ATOM   1304  C CG2   . THR A  1 202  ? -37.378 63.701  60.137  1.00 33.79 ? 200  THR A CG2   1 
ATOM   1305  N N     . ILE A  1 203  ? -41.067 61.980  62.065  1.00 26.32 ? 201  ILE A N     1 
ATOM   1306  C CA    . ILE A  1 203  ? -42.332 61.259  62.205  1.00 26.97 ? 201  ILE A CA    1 
ATOM   1307  C C     . ILE A  1 203  ? -42.753 60.672  60.861  1.00 27.44 ? 201  ILE A C     1 
ATOM   1308  O O     . ILE A  1 203  ? -43.231 59.535  60.790  1.00 28.60 ? 201  ILE A O     1 
ATOM   1309  C CB    . ILE A  1 203  ? -43.423 62.168  62.813  1.00 29.55 ? 201  ILE A CB    1 
ATOM   1310  C CG1   . ILE A  1 203  ? -44.695 61.354  63.136  1.00 21.26 ? 201  ILE A CG1   1 
ATOM   1311  C CG2   . ILE A  1 203  ? -43.735 63.333  61.895  1.00 29.50 ? 201  ILE A CG2   1 
ATOM   1312  C CD1   . ILE A  1 203  ? -44.418 60.206  64.115  1.00 25.90 ? 201  ILE A CD1   1 
ATOM   1313  N N     . ARG A  1 204  ? -42.514 61.401  59.769  1.00 26.86 ? 202  ARG A N     1 
ATOM   1314  C CA    . ARG A  1 204  ? -42.895 60.896  58.449  1.00 28.71 ? 202  ARG A CA    1 
ATOM   1315  C C     . ARG A  1 204  ? -42.170 59.602  58.105  1.00 31.50 ? 202  ARG A C     1 
ATOM   1316  O O     . ARG A  1 204  ? -42.779 58.657  57.594  1.00 32.70 ? 202  ARG A O     1 
ATOM   1317  C CB    . ARG A  1 204  ? -42.609 61.953  57.390  1.00 30.22 ? 202  ARG A CB    1 
ATOM   1318  C CG    . ARG A  1 204  ? -43.815 62.735  56.993  1.00 40.19 ? 202  ARG A CG    1 
ATOM   1319  C CD    . ARG A  1 204  ? -43.440 64.059  56.337  1.00 44.61 ? 202  ARG A CD    1 
ATOM   1320  N NE    . ARG A  1 204  ? -44.602 64.936  56.308  1.00 43.55 ? 202  ARG A NE    1 
ATOM   1321  C CZ    . ARG A  1 204  ? -45.074 65.584  57.366  1.00 42.21 ? 202  ARG A CZ    1 
ATOM   1322  N NH1   . ARG A  1 204  ? -44.469 65.520  58.544  1.00 37.97 ? 202  ARG A NH1   1 
ATOM   1323  N NH2   . ARG A  1 204  ? -46.171 66.325  57.234  1.00 38.02 ? 202  ARG A NH2   1 
ATOM   1324  N N     . GLU A  1 205  ? -40.862 59.542  58.371  1.00 32.44 ? 203  GLU A N     1 
ATOM   1325  C CA    . GLU A  1 205  ? -40.110 58.325  58.089  1.00 29.71 ? 203  GLU A CA    1 
ATOM   1326  C C     . GLU A  1 205  ? -40.527 57.195  59.019  1.00 32.70 ? 203  GLU A C     1 
ATOM   1327  O O     . GLU A  1 205  ? -40.661 56.042  58.593  1.00 32.57 ? 203  GLU A O     1 
ATOM   1328  C CB    . GLU A  1 205  ? -38.617 58.627  58.203  1.00 36.17 ? 203  GLU A CB    1 
ATOM   1329  C CG    . GLU A  1 205  ? -37.696 57.435  58.217  1.00 39.19 ? 203  GLU A CG    1 
ATOM   1330  C CD    . GLU A  1 205  ? -36.239 57.871  58.334  1.00 44.58 ? 203  GLU A CD    1 
ATOM   1331  O OE1   . GLU A  1 205  ? -35.746 58.571  57.417  1.00 47.85 ? 203  GLU A OE1   1 
ATOM   1332  O OE2   . GLU A  1 205  ? -35.598 57.545  59.358  1.00 44.94 ? 203  GLU A OE2   1 
ATOM   1333  N N     . ALA A  1 206  ? -40.758 57.516  60.291  1.00 27.91 ? 204  ALA A N     1 
ATOM   1334  C CA    . ALA A  1 206  ? -41.238 56.518  61.237  1.00 30.35 ? 204  ALA A CA    1 
ATOM   1335  C C     . ALA A  1 206  ? -42.579 55.940  60.800  1.00 30.53 ? 204  ALA A C     1 
ATOM   1336  O O     . ALA A  1 206  ? -42.791 54.728  60.878  1.00 26.73 ? 204  ALA A O     1 
ATOM   1337  C CB    . ALA A  1 206  ? -41.341 57.144  62.625  1.00 26.62 ? 204  ALA A CB    1 
ATOM   1338  N N     . LEU A  1 207  ? -43.489 56.793  60.316  1.00 26.97 ? 205  LEU A N     1 
ATOM   1339  C CA    . LEU A  1 207  ? -44.789 56.318  59.848  1.00 29.12 ? 205  LEU A CA    1 
ATOM   1340  C C     . LEU A  1 207  ? -44.657 55.440  58.606  1.00 33.57 ? 205  LEU A C     1 
ATOM   1341  O O     . LEU A  1 207  ? -45.370 54.436  58.476  1.00 32.26 ? 205  LEU A O     1 
ATOM   1342  C CB    . LEU A  1 207  ? -45.713 57.507  59.580  1.00 28.71 ? 205  LEU A CB    1 
ATOM   1343  C CG    . LEU A  1 207  ? -46.255 58.246  60.810  1.00 29.68 ? 205  LEU A CG    1 
ATOM   1344  C CD1   . LEU A  1 207  ? -46.709 59.655  60.451  1.00 27.12 ? 205  LEU A CD1   1 
ATOM   1345  C CD2   . LEU A  1 207  ? -47.403 57.473  61.440  1.00 24.35 ? 205  LEU A CD2   1 
ATOM   1346  N N     . LYS A  1 208  ? -43.754 55.787  57.680  1.00 31.38 ? 206  LYS A N     1 
ATOM   1347  C CA    . LYS A  1 208  ? -43.556 54.930  56.513  1.00 32.77 ? 206  LYS A CA    1 
ATOM   1348  C C     . LYS A  1 208  ? -43.054 53.555  56.927  1.00 31.56 ? 206  LYS A C     1 
ATOM   1349  O O     . LYS A  1 208  ? -43.476 52.538  56.369  1.00 33.66 ? 206  LYS A O     1 
ATOM   1350  C CB    . LYS A  1 208  ? -42.576 55.579  55.529  1.00 32.97 ? 206  LYS A CB    1 
ATOM   1351  N N     . ARG A  1 209  ? -42.174 53.500  57.923  1.00 31.87 ? 207  ARG A N     1 
ATOM   1352  C CA    . ARG A  1 209  ? -41.606 52.232  58.353  1.00 34.88 ? 207  ARG A CA    1 
ATOM   1353  C C     . ARG A  1 209  ? -42.533 51.428  59.246  1.00 35.61 ? 207  ARG A C     1 
ATOM   1354  O O     . ARG A  1 209  ? -42.227 50.268  59.532  1.00 36.41 ? 207  ARG A O     1 
ATOM   1355  C CB    . ARG A  1 209  ? -40.284 52.481  59.070  1.00 35.05 ? 207  ARG A CB    1 
ATOM   1356  C CG    . ARG A  1 209  ? -39.277 53.103  58.150  1.00 39.78 ? 207  ARG A CG    1 
ATOM   1357  C CD    . ARG A  1 209  ? -38.031 53.444  58.885  1.00 37.85 ? 207  ARG A CD    1 
ATOM   1358  N NE    . ARG A  1 209  ? -37.016 53.964  57.981  1.00 41.93 ? 207  ARG A NE    1 
ATOM   1359  C CZ    . ARG A  1 209  ? -35.853 54.455  58.382  1.00 45.47 ? 207  ARG A CZ    1 
ATOM   1360  N NH1   . ARG A  1 209  ? -35.536 54.511  59.667  1.00 41.28 ? 207  ARG A NH1   1 
ATOM   1361  N NH2   . ARG A  1 209  ? -34.990 54.903  57.475  1.00 47.75 ? 207  ARG A NH2   1 
ATOM   1362  N N     . SER A  1 210  ? -43.663 51.999  59.668  1.00 35.62 ? 208  SER A N     1 
ATOM   1363  C CA    . SER A  1 210  ? -44.596 51.290  60.535  1.00 33.12 ? 208  SER A CA    1 
ATOM   1364  C C     . SER A  1 210  ? -45.611 50.456  59.767  1.00 34.17 ? 208  SER A C     1 
ATOM   1365  O O     . SER A  1 210  ? -46.249 49.584  60.366  1.00 33.71 ? 208  SER A O     1 
ATOM   1366  C CB    . SER A  1 210  ? -45.335 52.285  61.434  1.00 31.33 ? 208  SER A CB    1 
ATOM   1367  O OG    . SER A  1 210  ? -44.409 52.987  62.252  1.00 33.58 ? 208  SER A OG    1 
ATOM   1368  N N     . LYS A  1 211  ? -45.770 50.695  58.460  1.00 36.80 ? 209  LYS A N     1 
ATOM   1369  C CA    . LYS A  1 211  ? -46.786 49.976  57.696  1.00 36.69 ? 209  LYS A CA    1 
ATOM   1370  C C     . LYS A  1 211  ? -46.535 48.473  57.701  1.00 37.98 ? 209  LYS A C     1 
ATOM   1371  O O     . LYS A  1 211  ? -47.489 47.686  57.737  1.00 39.95 ? 209  LYS A O     1 
ATOM   1372  C CB    . LYS A  1 211  ? -46.839 50.514  56.263  1.00 36.52 ? 209  LYS A CB    1 
ATOM   1373  N N     . GLU A  1 212  ? -45.266 48.054  57.702  1.00 38.52 ? 210  GLU A N     1 
ATOM   1374  C CA    . GLU A  1 212  ? -44.954 46.630  57.661  1.00 41.92 ? 210  GLU A CA    1 
ATOM   1375  C C     . GLU A  1 212  ? -45.598 45.886  58.828  1.00 39.89 ? 210  GLU A C     1 
ATOM   1376  O O     . GLU A  1 212  ? -46.373 44.946  58.628  1.00 37.75 ? 210  GLU A O     1 
ATOM   1377  C CB    . GLU A  1 212  ? -43.441 46.422  57.660  1.00 43.22 ? 210  GLU A CB    1 
ATOM   1378  C CG    . GLU A  1 212  ? -43.040 44.959  57.521  1.00 42.99 ? 210  GLU A CG    1 
ATOM   1379  C CD    . GLU A  1 212  ? -41.530 44.751  57.579  1.00 52.57 ? 210  GLU A CD    1 
ATOM   1380  O OE1   . GLU A  1 212  ? -40.798 45.736  57.810  1.00 57.55 ? 210  GLU A OE1   1 
ATOM   1381  O OE2   . GLU A  1 212  ? -41.074 43.600  57.394  1.00 59.69 ? 210  GLU A OE2   1 
ATOM   1382  N N     . LEU A  1 213  ? -45.291 46.294  60.060  1.00 37.44 ? 211  LEU A N     1 
ATOM   1383  C CA    . LEU A  1 213  ? -45.796 45.554  61.211  1.00 38.55 ? 211  LEU A CA    1 
ATOM   1384  C C     . LEU A  1 213  ? -47.260 45.848  61.517  1.00 36.62 ? 211  LEU A C     1 
ATOM   1385  O O     . LEU A  1 213  ? -47.922 45.025  62.162  1.00 37.95 ? 211  LEU A O     1 
ATOM   1386  C CB    . LEU A  1 213  ? -44.923 45.826  62.437  1.00 37.82 ? 211  LEU A CB    1 
ATOM   1387  C CG    . LEU A  1 213  ? -43.584 45.086  62.374  1.00 34.75 ? 211  LEU A CG    1 
ATOM   1388  C CD1   . LEU A  1 213  ? -42.817 45.169  63.684  1.00 36.77 ? 211  LEU A CD1   1 
ATOM   1389  C CD2   . LEU A  1 213  ? -43.808 43.636  61.988  1.00 38.30 ? 211  LEU A CD2   1 
ATOM   1390  N N     . GLU A  1 214  ? -47.801 46.970  61.045  1.00 35.54 ? 212  GLU A N     1 
ATOM   1391  C CA    . GLU A  1 214  ? -49.234 47.183  61.211  1.00 37.13 ? 212  GLU A CA    1 
ATOM   1392  C C     . GLU A  1 214  ? -50.038 46.191  60.385  1.00 38.63 ? 212  GLU A C     1 
ATOM   1393  O O     . GLU A  1 214  ? -51.099 45.734  60.821  1.00 38.47 ? 212  GLU A O     1 
ATOM   1394  C CB    . GLU A  1 214  ? -49.609 48.612  60.843  1.00 35.75 ? 212  GLU A CB    1 
ATOM   1395  C CG    . GLU A  1 214  ? -49.282 49.592  61.941  1.00 32.85 ? 212  GLU A CG    1 
ATOM   1396  C CD    . GLU A  1 214  ? -49.660 50.998  61.579  1.00 35.80 ? 212  GLU A CD    1 
ATOM   1397  O OE1   . GLU A  1 214  ? -49.832 51.267  60.366  1.00 35.57 ? 212  GLU A OE1   1 
ATOM   1398  O OE2   . GLU A  1 214  ? -49.789 51.829  62.507  1.00 35.84 ? 212  GLU A OE2   1 
ATOM   1399  N N     . GLU A  1 215  ? -49.544 45.839  59.198  1.00 37.09 ? 213  GLU A N     1 
ATOM   1400  C CA    . GLU A  1 215  ? -50.202 44.827  58.385  1.00 40.62 ? 213  GLU A CA    1 
ATOM   1401  C C     . GLU A  1 215  ? -50.183 43.456  59.047  1.00 42.60 ? 213  GLU A C     1 
ATOM   1402  O O     . GLU A  1 215  ? -51.045 42.625  58.744  1.00 48.96 ? 213  GLU A O     1 
ATOM   1403  C CB    . GLU A  1 215  ? -49.544 44.761  57.005  1.00 42.69 ? 213  GLU A CB    1 
ATOM   1404  N N     . LYS A  1 216  ? -49.234 43.207  59.943  1.00 44.68 ? 214  LYS A N     1 
ATOM   1405  C CA    . LYS A  1 216  ? -49.131 41.951  60.674  1.00 43.45 ? 214  LYS A CA    1 
ATOM   1406  C C     . LYS A  1 216  ? -49.887 41.969  61.996  1.00 43.73 ? 214  LYS A C     1 
ATOM   1407  O O     . LYS A  1 216  ? -49.877 40.963  62.712  1.00 47.38 ? 214  LYS A O     1 
ATOM   1408  C CB    . LYS A  1 216  ? -47.662 41.611  60.932  1.00 37.21 ? 214  LYS A CB    1 
ATOM   1409  N N     . GLY A  1 217  ? -50.528 43.080  62.348  1.00 40.12 ? 215  GLY A N     1 
ATOM   1410  C CA    . GLY A  1 217  ? -51.380 43.134  63.519  1.00 39.29 ? 215  GLY A CA    1 
ATOM   1411  C C     . GLY A  1 217  ? -50.869 43.984  64.662  1.00 40.03 ? 215  GLY A C     1 
ATOM   1412  O O     . GLY A  1 217  ? -51.521 44.024  65.712  1.00 41.00 ? 215  GLY A O     1 
ATOM   1413  N N     . PHE A  1 218  ? -49.722 44.646  64.516  1.00 34.78 ? 216  PHE A N     1 
ATOM   1414  C CA    . PHE A  1 218  ? -49.258 45.563  65.538  1.00 32.53 ? 216  PHE A CA    1 
ATOM   1415  C C     . PHE A  1 218  ? -49.921 46.930  65.373  1.00 30.52 ? 216  PHE A C     1 
ATOM   1416  O O     . PHE A  1 218  ? -50.532 47.245  64.350  1.00 32.04 ? 216  PHE A O     1 
ATOM   1417  C CB    . PHE A  1 218  ? -47.732 45.710  65.484  1.00 29.56 ? 216  PHE A CB    1 
ATOM   1418  C CG    . PHE A  1 218  ? -46.976 44.499  65.960  1.00 32.75 ? 216  PHE A CG    1 
ATOM   1419  C CD1   . PHE A  1 218  ? -46.784 43.408  65.126  1.00 33.79 ? 216  PHE A CD1   1 
ATOM   1420  C CD2   . PHE A  1 218  ? -46.426 44.470  67.229  1.00 31.62 ? 216  PHE A CD2   1 
ATOM   1421  C CE1   . PHE A  1 218  ? -46.081 42.308  65.559  1.00 36.23 ? 216  PHE A CE1   1 
ATOM   1422  C CE2   . PHE A  1 218  ? -45.706 43.368  67.668  1.00 36.44 ? 216  PHE A CE2   1 
ATOM   1423  C CZ    . PHE A  1 218  ? -45.527 42.290  66.837  1.00 31.86 ? 216  PHE A CZ    1 
ATOM   1424  N N     . SER A  1 219  ? -49.793 47.747  66.410  1.00 27.90 ? 217  SER A N     1 
ATOM   1425  C CA    . SER A  1 219  ? -50.142 49.154  66.375  1.00 27.13 ? 217  SER A CA    1 
ATOM   1426  C C     . SER A  1 219  ? -48.933 49.928  66.885  1.00 28.27 ? 217  SER A C     1 
ATOM   1427  O O     . SER A  1 219  ? -47.927 49.335  67.285  1.00 26.80 ? 217  SER A O     1 
ATOM   1428  C CB    . SER A  1 219  ? -51.401 49.436  67.210  1.00 31.38 ? 217  SER A CB    1 
ATOM   1429  O OG    . SER A  1 219  ? -51.133 49.193  68.582  1.00 31.16 ? 217  SER A OG    1 
ATOM   1430  N N     . TYR A  1 220  ? -49.016 51.259  66.870  1.00 26.28 ? 218  TYR A N     1 
ATOM   1431  C CA    . TYR A  1 220  ? -47.862 52.091  67.186  1.00 26.21 ? 218  TYR A CA    1 
ATOM   1432  C C     . TYR A  1 220  ? -48.248 53.244  68.099  1.00 29.26 ? 218  TYR A C     1 
ATOM   1433  O O     . TYR A  1 220  ? -49.356 53.776  68.015  1.00 27.36 ? 218  TYR A O     1 
ATOM   1434  C CB    . TYR A  1 220  ? -47.217 52.666  65.910  1.00 27.06 ? 218  TYR A CB    1 
ATOM   1435  C CG    . TYR A  1 220  ? -46.287 51.707  65.238  1.00 28.39 ? 218  TYR A CG    1 
ATOM   1436  C CD1   . TYR A  1 220  ? -46.769 50.742  64.358  1.00 29.14 ? 218  TYR A CD1   1 
ATOM   1437  C CD2   . TYR A  1 220  ? -44.922 51.749  65.494  1.00 25.74 ? 218  TYR A CD2   1 
ATOM   1438  C CE1   . TYR A  1 220  ? -45.904 49.841  63.749  1.00 32.40 ? 218  TYR A CE1   1 
ATOM   1439  C CE2   . TYR A  1 220  ? -44.056 50.863  64.890  1.00 31.03 ? 218  TYR A CE2   1 
ATOM   1440  C CZ    . TYR A  1 220  ? -44.551 49.912  64.017  1.00 31.16 ? 218  TYR A CZ    1 
ATOM   1441  O OH    . TYR A  1 220  ? -43.684 49.036  63.425  1.00 31.00 ? 218  TYR A OH    1 
ATOM   1442  N N     . SER A  1 221  ? -47.313 53.617  68.979  1.00 27.62 ? 219  SER A N     1 
ATOM   1443  C CA    . SER A  1 221  ? -47.359 54.865  69.731  1.00 24.68 ? 219  SER A CA    1 
ATOM   1444  C C     . SER A  1 221  ? -45.999 55.535  69.595  1.00 27.64 ? 219  SER A C     1 
ATOM   1445  O O     . SER A  1 221  ? -44.976 54.928  69.927  1.00 28.61 ? 219  SER A O     1 
ATOM   1446  C CB    . SER A  1 221  ? -47.677 54.629  71.211  1.00 27.38 ? 219  SER A CB    1 
ATOM   1447  O OG    . SER A  1 221  ? -47.694 55.867  71.909  1.00 29.80 ? 219  SER A OG    1 
ATOM   1448  N N     . TYR A  1 222  ? -45.978 56.780  69.130  1.00 24.39 ? 220  TYR A N     1 
ATOM   1449  C CA    . TYR A  1 222  ? -44.723 57.440  68.781  1.00 24.97 ? 220  TYR A CA    1 
ATOM   1450  C C     . TYR A  1 222  ? -44.249 58.330  69.915  1.00 28.41 ? 220  TYR A C     1 
ATOM   1451  O O     . TYR A  1 222  ? -45.017 59.143  70.435  1.00 24.90 ? 220  TYR A O     1 
ATOM   1452  C CB    . TYR A  1 222  ? -44.879 58.251  67.495  1.00 23.63 ? 220  TYR A CB    1 
ATOM   1453  C CG    . TYR A  1 222  ? -45.233 57.343  66.359  1.00 23.47 ? 220  TYR A CG    1 
ATOM   1454  C CD1   . TYR A  1 222  ? -44.258 56.609  65.713  1.00 26.17 ? 220  TYR A CD1   1 
ATOM   1455  C CD2   . TYR A  1 222  ? -46.562 57.183  65.959  1.00 23.50 ? 220  TYR A CD2   1 
ATOM   1456  C CE1   . TYR A  1 222  ? -44.589 55.755  64.666  1.00 26.22 ? 220  TYR A CE1   1 
ATOM   1457  C CE2   . TYR A  1 222  ? -46.900 56.332  64.946  1.00 24.29 ? 220  TYR A CE2   1 
ATOM   1458  C CZ    . TYR A  1 222  ? -45.913 55.620  64.297  1.00 26.04 ? 220  TYR A CZ    1 
ATOM   1459  O OH    . TYR A  1 222  ? -46.244 54.767  63.277  1.00 28.39 ? 220  TYR A OH    1 
ATOM   1460  N N     . ASP A  1 223  ? -42.976 58.178  70.273  1.00 27.38 ? 221  ASP A N     1 
ATOM   1461  C CA    . ASP A  1 223  ? -42.321 58.916  71.348  1.00 30.54 ? 221  ASP A CA    1 
ATOM   1462  C C     . ASP A  1 223  ? -41.364 59.905  70.701  1.00 32.43 ? 221  ASP A C     1 
ATOM   1463  O O     . ASP A  1 223  ? -40.329 59.506  70.140  1.00 29.72 ? 221  ASP A O     1 
ATOM   1464  C CB    . ASP A  1 223  ? -41.590 57.947  72.270  1.00 31.73 ? 221  ASP A CB    1 
ATOM   1465  C CG    . ASP A  1 223  ? -40.709 58.643  73.312  1.00 38.00 ? 221  ASP A CG    1 
ATOM   1466  O OD1   . ASP A  1 223  ? -40.837 59.862  73.536  1.00 37.11 ? 221  ASP A OD1   1 
ATOM   1467  O OD2   . ASP A  1 223  ? -39.885 57.937  73.923  1.00 42.10 ? 221  ASP A OD2   1 
ATOM   1468  N N     . MET A  1 224  ? -41.705 61.188  70.773  1.00 30.35 ? 222  MET A N     1 
ATOM   1469  C CA    . MET A  1 224  ? -40.906 62.213  70.117  1.00 36.12 ? 222  MET A CA    1 
ATOM   1470  C C     . MET A  1 224  ? -39.652 62.584  70.910  1.00 38.43 ? 222  MET A C     1 
ATOM   1471  O O     . MET A  1 224  ? -39.014 63.596  70.603  1.00 42.93 ? 222  MET A O     1 
ATOM   1472  C CB    . MET A  1 224  ? -41.774 63.438  69.841  1.00 36.75 ? 222  MET A CB    1 
ATOM   1473  C CG    . MET A  1 224  ? -43.010 63.082  68.988  1.00 33.95 ? 222  MET A CG    1 
ATOM   1474  S SD    . MET A  1 224  ? -42.587 62.266  67.415  1.00 34.95 ? 222  MET A SD    1 
ATOM   1475  C CE    . MET A  1 224  ? -41.515 63.503  66.717  1.00 32.27 ? 222  MET A CE    1 
ATOM   1476  N N     . LEU A  1 225  ? -39.288 61.762  71.893  1.00 37.08 ? 223  LEU A N     1 
ATOM   1477  C CA    . LEU A  1 225  ? -38.035 61.877  72.648  1.00 41.45 ? 223  LEU A CA    1 
ATOM   1478  C C     . LEU A  1 225  ? -37.839 63.274  73.241  1.00 45.01 ? 223  LEU A C     1 
ATOM   1479  O O     . LEU A  1 225  ? -36.709 63.700  73.488  1.00 46.23 ? 223  LEU A O     1 
ATOM   1480  C CB    . LEU A  1 225  ? -36.831 61.472  71.790  1.00 37.32 ? 223  LEU A CB    1 
ATOM   1481  C CG    . LEU A  1 225  ? -36.723 59.987  71.399  1.00 37.46 ? 223  LEU A CG    1 
ATOM   1482  C CD1   . LEU A  1 225  ? -35.549 59.725  70.449  1.00 35.85 ? 223  LEU A CD1   1 
ATOM   1483  C CD2   . LEU A  1 225  ? -36.613 59.090  72.623  1.00 32.93 ? 223  LEU A CD2   1 
ATOM   1484  N N     . GLY A  1 226  ? -38.938 63.994  73.481  1.00 43.37 ? 224  GLY A N     1 
ATOM   1485  C CA    . GLY A  1 226  ? -38.857 65.253  74.216  1.00 40.17 ? 224  GLY A CA    1 
ATOM   1486  C C     . GLY A  1 226  ? -38.858 64.996  75.720  1.00 38.47 ? 224  GLY A C     1 
ATOM   1487  O O     . GLY A  1 226  ? -39.503 64.070  76.210  1.00 37.94 ? 224  GLY A O     1 
ATOM   1488  N N     . GLU A  1 227  ? -38.129 65.840  76.453  1.00 38.14 ? 225  GLU A N     1 
ATOM   1489  C CA    . GLU A  1 227  ? -37.930 65.595  77.874  1.00 36.61 ? 225  GLU A CA    1 
ATOM   1490  C C     . GLU A  1 227  ? -37.210 66.769  78.519  1.00 38.66 ? 225  GLU A C     1 
ATOM   1491  O O     . GLU A  1 227  ? -36.288 67.333  77.930  1.00 36.26 ? 225  GLU A O     1 
ATOM   1492  C CB    . GLU A  1 227  ? -37.114 64.312  78.084  1.00 45.38 ? 225  GLU A CB    1 
ATOM   1493  C CG    . GLU A  1 227  ? -37.100 63.792  79.494  1.00 46.84 ? 225  GLU A CG    1 
ATOM   1494  C CD    . GLU A  1 227  ? -36.485 62.411  79.561  1.00 48.52 ? 225  GLU A CD    1 
ATOM   1495  O OE1   . GLU A  1 227  ? -36.292 61.799  78.483  1.00 44.95 ? 225  GLU A OE1   1 
ATOM   1496  O OE2   . GLU A  1 227  ? -36.205 61.937  80.681  1.00 49.50 ? 225  GLU A OE2   1 
ATOM   1497  N N     . ALA A  1 228  ? -37.634 67.112  79.736  1.00 35.82 ? 226  ALA A N     1 
ATOM   1498  C CA    . ALA A  1 228  ? -36.920 68.037  80.616  1.00 31.28 ? 226  ALA A CA    1 
ATOM   1499  C C     . ALA A  1 228  ? -36.571 69.351  79.902  1.00 31.51 ? 226  ALA A C     1 
ATOM   1500  O O     . ALA A  1 228  ? -35.414 69.688  79.669  1.00 32.15 ? 226  ALA A O     1 
ATOM   1501  C CB    . ALA A  1 228  ? -35.665 67.357  81.173  1.00 40.29 ? 226  ALA A CB    1 
ATOM   1502  N N     . ALA A  1 229  ? -37.614 70.102  79.575  1.00 25.26 ? 227  ALA A N     1 
ATOM   1503  C CA    . ALA A  1 229  ? -37.411 71.461  79.087  1.00 29.82 ? 227  ALA A CA    1 
ATOM   1504  C C     . ALA A  1 229  ? -36.680 72.290  80.139  1.00 28.44 ? 227  ALA A C     1 
ATOM   1505  O O     . ALA A  1 229  ? -37.014 72.238  81.328  1.00 27.47 ? 227  ALA A O     1 
ATOM   1506  C CB    . ALA A  1 229  ? -38.753 72.106  78.752  1.00 25.05 ? 227  ALA A CB    1 
ATOM   1507  N N     . THR A  1 230  ? -35.681 73.049  79.698  1.00 26.45 ? 228  THR A N     1 
ATOM   1508  C CA    . THR A  1 230  ? -34.908 73.923  80.571  1.00 31.69 ? 228  THR A CA    1 
ATOM   1509  C C     . THR A  1 230  ? -35.325 75.381  80.456  1.00 27.73 ? 228  THR A C     1 
ATOM   1510  O O     . THR A  1 230  ? -35.172 76.141  81.418  1.00 24.23 ? 228  THR A O     1 
ATOM   1511  C CB    . THR A  1 230  ? -33.400 73.792  80.257  1.00 33.81 ? 228  THR A CB    1 
ATOM   1512  O OG1   . THR A  1 230  ? -33.003 72.416  80.354  1.00 36.31 ? 228  THR A OG1   1 
ATOM   1513  C CG2   . THR A  1 230  ? -32.551 74.609  81.229  1.00 32.05 ? 228  THR A CG2   1 
ATOM   1514  N N     . THR A  1 231  ? -35.844 75.798  79.302  1.00 25.45 ? 229  THR A N     1 
ATOM   1515  C CA    . THR A  1 231  ? -36.239 77.179  79.083  1.00 23.58 ? 229  THR A CA    1 
ATOM   1516  C C     . THR A  1 231  ? -37.644 77.233  78.485  1.00 22.19 ? 229  THR A C     1 
ATOM   1517  O O     . THR A  1 231  ? -38.174 76.237  77.993  1.00 23.53 ? 229  THR A O     1 
ATOM   1518  C CB    . THR A  1 231  ? -35.266 77.894  78.149  1.00 25.92 ? 229  THR A CB    1 
ATOM   1519  O OG1   . THR A  1 231  ? -35.459 77.397  76.821  1.00 26.76 ? 229  THR A OG1   1 
ATOM   1520  C CG2   . THR A  1 231  ? -33.791 77.632  78.570  1.00 25.70 ? 229  THR A CG2   1 
ATOM   1521  N N     . ALA A  1 232  ? -38.260 78.407  78.586  1.00 24.64 ? 230  ALA A N     1 
ATOM   1522  C CA    . ALA A  1 232  ? -39.523 78.645  77.893  1.00 24.83 ? 230  ALA A CA    1 
ATOM   1523  C C     . ALA A  1 232  ? -39.404 78.325  76.404  1.00 27.74 ? 230  ALA A C     1 
ATOM   1524  O O     . ALA A  1 232  ? -40.285 77.678  75.822  1.00 28.99 ? 230  ALA A O     1 
ATOM   1525  C CB    . ALA A  1 232  ? -39.966 80.095  78.104  1.00 26.33 ? 230  ALA A CB    1 
ATOM   1526  N N     . ALA A  1 233  ? -38.302 78.739  75.776  1.00 27.23 ? 231  ALA A N     1 
ATOM   1527  C CA    . ALA A  1 233  ? -38.133 78.477  74.348  1.00 30.39 ? 231  ALA A CA    1 
ATOM   1528  C C     . ALA A  1 233  ? -38.064 76.983  74.061  1.00 29.55 ? 231  ALA A C     1 
ATOM   1529  O O     . ALA A  1 233  ? -38.642 76.511  73.076  1.00 28.71 ? 231  ALA A O     1 
ATOM   1530  C CB    . ALA A  1 233  ? -36.884 79.178  73.819  1.00 30.22 ? 231  ALA A CB    1 
ATOM   1531  N N     . ASP A  1 234  ? -37.375 76.219  74.919  1.00 25.70 ? 232  ASP A N     1 
ATOM   1532  C CA    . ASP A  1 234  ? -37.314 74.770  74.745  1.00 28.19 ? 232  ASP A CA    1 
ATOM   1533  C C     . ASP A  1 234  ? -38.690 74.141  74.857  1.00 27.57 ? 232  ASP A C     1 
ATOM   1534  O O     . ASP A  1 234  ? -39.025 73.231  74.093  1.00 27.38 ? 232  ASP A O     1 
ATOM   1535  C CB    . ASP A  1 234  ? -36.409 74.112  75.791  1.00 32.43 ? 232  ASP A CB    1 
ATOM   1536  C CG    . ASP A  1 234  ? -34.942 74.290  75.506  1.00 36.27 ? 232  ASP A CG    1 
ATOM   1537  O OD1   . ASP A  1 234  ? -34.573 74.603  74.354  1.00 37.36 ? 232  ASP A OD1   1 
ATOM   1538  O OD2   . ASP A  1 234  ? -34.153 74.096  76.461  1.00 43.88 ? 232  ASP A OD2   1 
ATOM   1539  N N     . ALA A  1 235  ? -39.481 74.565  75.842  1.00 24.15 ? 233  ALA A N     1 
ATOM   1540  C CA    . ALA A  1 235  ? -40.814 73.986  75.974  1.00 25.68 ? 233  ALA A CA    1 
ATOM   1541  C C     . ALA A  1 235  ? -41.662 74.313  74.758  1.00 27.78 ? 233  ALA A C     1 
ATOM   1542  O O     . ALA A  1 235  ? -42.449 73.476  74.300  1.00 24.03 ? 233  ALA A O     1 
ATOM   1543  C CB    . ALA A  1 235  ? -41.490 74.478  77.251  1.00 24.81 ? 233  ALA A CB    1 
ATOM   1544  N N     . GLU A  1 236  ? -41.507 75.528  74.213  1.00 26.47 ? 234  GLU A N     1 
ATOM   1545  C CA    . GLU A  1 236  ? -42.234 75.903  73.003  1.00 28.04 ? 234  GLU A CA    1 
ATOM   1546  C C     . GLU A  1 236  ? -41.847 75.004  71.837  1.00 27.77 ? 234  GLU A C     1 
ATOM   1547  O O     . GLU A  1 236  ? -42.710 74.549  71.076  1.00 27.27 ? 234  GLU A O     1 
ATOM   1548  C CB    . GLU A  1 236  ? -41.966 77.374  72.655  1.00 32.09 ? 234  GLU A CB    1 
ATOM   1549  C CG    . GLU A  1 236  ? -42.888 78.376  73.359  1.00 40.30 ? 234  GLU A CG    1 
ATOM   1550  C CD    . GLU A  1 236  ? -42.194 79.681  73.745  1.00 48.76 ? 234  GLU A CD    1 
ATOM   1551  O OE1   . GLU A  1 236  ? -41.231 80.081  73.051  1.00 53.54 ? 234  GLU A OE1   1 
ATOM   1552  O OE2   . GLU A  1 236  ? -42.603 80.306  74.757  1.00 51.38 ? 234  GLU A OE2   1 
ATOM   1553  N N     . ARG A  1 237  ? -40.555 74.740  71.680  1.00 27.26 ? 235  ARG A N     1 
ATOM   1554  C CA    . ARG A  1 237  ? -40.101 73.848  70.620  1.00 29.90 ? 235  ARG A CA    1 
ATOM   1555  C C     . ARG A  1 237  ? -40.687 72.454  70.789  1.00 29.89 ? 235  ARG A C     1 
ATOM   1556  O O     . ARG A  1 237  ? -41.126 71.834  69.816  1.00 26.92 ? 235  ARG A O     1 
ATOM   1557  C CB    . ARG A  1 237  ? -38.573 73.787  70.602  1.00 29.96 ? 235  ARG A CB    1 
ATOM   1558  C CG    . ARG A  1 237  ? -38.018 72.543  69.923  1.00 38.03 ? 235  ARG A CG    1 
ATOM   1559  C CD    . ARG A  1 237  ? -36.631 72.795  69.334  1.00 47.62 ? 235  ARG A CD    1 
ATOM   1560  N NE    . ARG A  1 237  ? -35.755 73.460  70.290  1.00 52.53 ? 235  ARG A NE    1 
ATOM   1561  C CZ    . ARG A  1 237  ? -35.159 72.854  71.308  1.00 52.12 ? 235  ARG A CZ    1 
ATOM   1562  N NH1   . ARG A  1 237  ? -35.310 71.555  71.528  1.00 47.48 ? 235  ARG A NH1   1 
ATOM   1563  N NH2   . ARG A  1 237  ? -34.389 73.569  72.125  1.00 51.68 ? 235  ARG A NH2   1 
ATOM   1564  N N     . TYR A  1 238  ? -40.717 71.949  72.024  1.00 25.44 ? 236  TYR A N     1 
ATOM   1565  C CA    . TYR A  1 238  ? -41.281 70.630  72.254  1.00 24.61 ? 236  TYR A CA    1 
ATOM   1566  C C     . TYR A  1 238  ? -42.776 70.602  71.951  1.00 22.75 ? 236  TYR A C     1 
ATOM   1567  O O     . TYR A  1 238  ? -43.278 69.614  71.402  1.00 25.05 ? 236  TYR A O     1 
ATOM   1568  C CB    . TYR A  1 238  ? -41.007 70.190  73.692  1.00 24.67 ? 236  TYR A CB    1 
ATOM   1569  C CG    . TYR A  1 238  ? -39.577 69.765  73.929  1.00 25.77 ? 236  TYR A CG    1 
ATOM   1570  C CD1   . TYR A  1 238  ? -38.915 68.953  73.016  1.00 32.24 ? 236  TYR A CD1   1 
ATOM   1571  C CD2   . TYR A  1 238  ? -38.887 70.173  75.066  1.00 28.47 ? 236  TYR A CD2   1 
ATOM   1572  C CE1   . TYR A  1 238  ? -37.601 68.565  73.224  1.00 32.72 ? 236  TYR A CE1   1 
ATOM   1573  C CE2   . TYR A  1 238  ? -37.569 69.792  75.277  1.00 30.97 ? 236  TYR A CE2   1 
ATOM   1574  C CZ    . TYR A  1 238  ? -36.935 68.986  74.357  1.00 39.46 ? 236  TYR A CZ    1 
ATOM   1575  O OH    . TYR A  1 238  ? -35.623 68.596  74.568  1.00 39.12 ? 236  TYR A OH    1 
ATOM   1576  N N     . TYR A  1 239  ? -43.500 71.677  72.288  1.00 20.64 ? 237  TYR A N     1 
ATOM   1577  C CA    . TYR A  1 239  ? -44.914 71.748  71.947  1.00 25.42 ? 237  TYR A CA    1 
ATOM   1578  C C     . TYR A  1 239  ? -45.120 71.657  70.438  1.00 26.58 ? 237  TYR A C     1 
ATOM   1579  O O     . TYR A  1 239  ? -45.916 70.842  69.959  1.00 22.98 ? 237  TYR A O     1 
ATOM   1580  C CB    . TYR A  1 239  ? -45.536 73.030  72.493  1.00 25.69 ? 237  TYR A CB    1 
ATOM   1581  C CG    . TYR A  1 239  ? -46.974 73.165  72.096  1.00 25.35 ? 237  TYR A CG    1 
ATOM   1582  C CD1   . TYR A  1 239  ? -47.319 73.755  70.891  1.00 27.02 ? 237  TYR A CD1   1 
ATOM   1583  C CD2   . TYR A  1 239  ? -47.992 72.659  72.902  1.00 26.38 ? 237  TYR A CD2   1 
ATOM   1584  C CE1   . TYR A  1 239  ? -48.634 73.867  70.498  1.00 32.10 ? 237  TYR A CE1   1 
ATOM   1585  C CE2   . TYR A  1 239  ? -49.313 72.780  72.527  1.00 25.70 ? 237  TYR A CE2   1 
ATOM   1586  C CZ    . TYR A  1 239  ? -49.627 73.379  71.315  1.00 30.05 ? 237  TYR A CZ    1 
ATOM   1587  O OH    . TYR A  1 239  ? -50.924 73.518  70.889  1.00 29.58 ? 237  TYR A OH    1 
ATOM   1588  N N     . ARG A  1 240  ? -44.417 72.489  69.665  1.00 24.22 ? 238  ARG A N     1 
ATOM   1589  C CA    . ARG A  1 240  ? -44.669 72.455  68.226  1.00 26.72 ? 238  ARG A CA    1 
ATOM   1590  C C     . ARG A  1 240  ? -44.203 71.137  67.611  1.00 24.01 ? 238  ARG A C     1 
ATOM   1591  O O     . ARG A  1 240  ? -44.769 70.693  66.607  1.00 28.09 ? 238  ARG A O     1 
ATOM   1592  C CB    . ARG A  1 240  ? -44.039 73.672  67.528  1.00 29.01 ? 238  ARG A CB    1 
ATOM   1593  C CG    . ARG A  1 240  ? -42.552 73.748  67.561  1.00 30.15 ? 238  ARG A CG    1 
ATOM   1594  C CD    . ARG A  1 240  ? -42.051 75.008  66.833  1.00 30.88 ? 238  ARG A CD    1 
ATOM   1595  N NE    . ARG A  1 240  ? -40.622 75.176  67.059  1.00 33.58 ? 238  ARG A NE    1 
ATOM   1596  C CZ    . ARG A  1 240  ? -40.096 76.045  67.915  1.00 33.57 ? 238  ARG A CZ    1 
ATOM   1597  N NH1   . ARG A  1 240  ? -40.850 76.922  68.569  1.00 32.89 ? 238  ARG A NH1   1 
ATOM   1598  N NH2   . ARG A  1 240  ? -38.784 76.030  68.126  1.00 37.76 ? 238  ARG A NH2   1 
ATOM   1599  N N     . ASP A  1 241  ? -43.214 70.475  68.210  1.00 25.67 ? 239  ASP A N     1 
ATOM   1600  C CA    A ASP A  1 241  ? -42.831 69.149  67.734  0.49 27.52 ? 239  ASP A CA    1 
ATOM   1601  C CA    B ASP A  1 241  ? -42.831 69.151  67.735  0.51 27.52 ? 239  ASP A CA    1 
ATOM   1602  C C     . ASP A  1 241  ? -43.954 68.140  67.958  1.00 27.71 ? 239  ASP A C     1 
ATOM   1603  O O     . ASP A  1 241  ? -44.242 67.326  67.074  1.00 27.20 ? 239  ASP A O     1 
ATOM   1604  C CB    A ASP A  1 241  ? -41.549 68.677  68.419  0.49 31.03 ? 239  ASP A CB    1 
ATOM   1605  C CB    B ASP A  1 241  ? -41.547 68.700  68.426  0.51 31.02 ? 239  ASP A CB    1 
ATOM   1606  C CG    A ASP A  1 241  ? -40.358 69.570  68.122  0.49 31.00 ? 239  ASP A CG    1 
ATOM   1607  C CG    B ASP A  1 241  ? -40.994 67.420  67.843  0.51 31.08 ? 239  ASP A CG    1 
ATOM   1608  O OD1   A ASP A  1 241  ? -40.374 70.284  67.099  0.49 32.05 ? 239  ASP A OD1   1 
ATOM   1609  O OD1   B ASP A  1 241  ? -40.422 67.466  66.732  0.51 34.49 ? 239  ASP A OD1   1 
ATOM   1610  O OD2   A ASP A  1 241  ? -39.402 69.560  68.929  0.49 34.78 ? 239  ASP A OD2   1 
ATOM   1611  O OD2   B ASP A  1 241  ? -41.133 66.367  68.497  0.51 35.91 ? 239  ASP A OD2   1 
ATOM   1612  N N     . TYR A  1 242  ? -44.609 68.187  69.135  1.00 23.68 ? 240  TYR A N     1 
ATOM   1613  C CA    . TYR A  1 242  ? -45.747 67.302  69.408  1.00 24.09 ? 240  TYR A CA    1 
ATOM   1614  C C     . TYR A  1 242  ? -46.929 67.627  68.507  1.00 23.15 ? 240  TYR A C     1 
ATOM   1615  O O     . TYR A  1 242  ? -47.609 66.720  68.002  1.00 21.72 ? 240  TYR A O     1 
ATOM   1616  C CB    . TYR A  1 242  ? -46.213 67.434  70.861  1.00 20.18 ? 240  TYR A CB    1 
ATOM   1617  C CG    . TYR A  1 242  ? -45.336 66.800  71.913  1.00 24.21 ? 240  TYR A CG    1 
ATOM   1618  C CD1   . TYR A  1 242  ? -44.712 65.581  71.701  1.00 26.34 ? 240  TYR A CD1   1 
ATOM   1619  C CD2   . TYR A  1 242  ? -45.177 67.413  73.148  1.00 24.90 ? 240  TYR A CD2   1 
ATOM   1620  C CE1   . TYR A  1 242  ? -43.915 65.004  72.698  1.00 29.15 ? 240  TYR A CE1   1 
ATOM   1621  C CE2   . TYR A  1 242  ? -44.394 66.857  74.136  1.00 23.55 ? 240  TYR A CE2   1 
ATOM   1622  C CZ    . TYR A  1 242  ? -43.767 65.655  73.911  1.00 26.40 ? 240  TYR A CZ    1 
ATOM   1623  O OH    . TYR A  1 242  ? -43.000 65.105  74.903  1.00 24.13 ? 240  TYR A OH    1 
ATOM   1624  N N     . GLU A  1 243  ? -47.228 68.919  68.357  1.00 22.61 ? 241  GLU A N     1 
ATOM   1625  C CA    . GLU A  1 243  ? -48.335 69.325  67.503  1.00 25.07 ? 241  GLU A CA    1 
ATOM   1626  C C     . GLU A  1 243  ? -48.124 68.828  66.082  1.00 26.61 ? 241  GLU A C     1 
ATOM   1627  O O     . GLU A  1 243  ? -49.050 68.291  65.463  1.00 22.90 ? 241  GLU A O     1 
ATOM   1628  C CB    . GLU A  1 243  ? -48.492 70.848  67.531  1.00 24.64 ? 241  GLU A CB    1 
ATOM   1629  C CG    . GLU A  1 243  ? -49.748 71.405  66.843  1.00 29.08 ? 241  GLU A CG    1 
ATOM   1630  C CD    . GLU A  1 243  ? -49.673 72.921  66.649  1.00 31.82 ? 241  GLU A CD    1 
ATOM   1631  O OE1   . GLU A  1 243  ? -48.545 73.475  66.630  1.00 42.17 ? 241  GLU A OE1   1 
ATOM   1632  O OE2   . GLU A  1 243  ? -50.727 73.562  66.509  1.00 37.41 ? 241  GLU A OE2   1 
ATOM   1633  N N     . SER A  1 244  ? -46.906 68.979  65.549  1.00 25.45 ? 242  SER A N     1 
ATOM   1634  C CA    . SER A  1 244  ? -46.690 68.559  64.167  1.00 24.86 ? 242  SER A CA    1 
ATOM   1635  C C     . SER A  1 244  ? -46.723 67.037  64.034  1.00 25.08 ? 242  SER A C     1 
ATOM   1636  O O     . SER A  1 244  ? -47.196 66.513  63.013  1.00 25.87 ? 242  SER A O     1 
ATOM   1637  C CB    . SER A  1 244  ? -45.369 69.128  63.642  1.00 27.03 ? 242  SER A CB    1 
ATOM   1638  O OG    . SER A  1 244  ? -44.282 68.440  64.217  1.00 31.50 ? 242  SER A OG    1 
ATOM   1639  N N     . ALA A  1 245  ? -46.244 66.308  65.046  1.00 22.72 ? 243  ALA A N     1 
ATOM   1640  C CA    . ALA A  1 245  ? -46.365 64.857  65.005  1.00 24.13 ? 243  ALA A CA    1 
ATOM   1641  C C     . ALA A  1 245  ? -47.831 64.420  65.067  1.00 22.20 ? 243  ALA A C     1 
ATOM   1642  O O     . ALA A  1 245  ? -48.225 63.471  64.383  1.00 22.45 ? 243  ALA A O     1 
ATOM   1643  C CB    . ALA A  1 245  ? -45.569 64.230  66.144  1.00 24.17 ? 243  ALA A CB    1 
ATOM   1644  N N     . ILE A  1 246  ? -48.647 65.081  65.892  1.00 21.77 ? 244  ILE A N     1 
ATOM   1645  C CA    . ILE A  1 246  ? -50.061 64.700  65.990  1.00 23.84 ? 244  ILE A CA    1 
ATOM   1646  C C     . ILE A  1 246  ? -50.744 64.826  64.636  1.00 24.42 ? 244  ILE A C     1 
ATOM   1647  O O     . ILE A  1 246  ? -51.492 63.936  64.220  1.00 24.95 ? 244  ILE A O     1 
ATOM   1648  C CB    . ILE A  1 246  ? -50.784 65.534  67.061  1.00 21.06 ? 244  ILE A CB    1 
ATOM   1649  C CG1   . ILE A  1 246  ? -50.296 65.127  68.456  1.00 22.19 ? 244  ILE A CG1   1 
ATOM   1650  C CG2   . ILE A  1 246  ? -52.308 65.324  66.970  1.00 25.15 ? 244  ILE A CG2   1 
ATOM   1651  C CD1   . ILE A  1 246  ? -50.896 65.963  69.564  1.00 24.45 ? 244  ILE A CD1   1 
ATOM   1652  N N     . HIS A  1 247  ? -50.473 65.913  63.910  1.00 23.03 ? 245  HIS A N     1 
ATOM   1653  C CA    . HIS A  1 247  ? -51.024 66.041  62.562  1.00 26.26 ? 245  HIS A CA    1 
ATOM   1654  C C     . HIS A  1 247  ? -50.589 64.873  61.684  1.00 25.30 ? 245  HIS A C     1 
ATOM   1655  O O     . HIS A  1 247  ? -51.416 64.253  61.008  1.00 29.29 ? 245  HIS A O     1 
ATOM   1656  C CB    . HIS A  1 247  ? -50.597 67.366  61.928  1.00 25.52 ? 245  HIS A CB    1 
ATOM   1657  C CG    . HIS A  1 247  ? -51.273 68.568  62.507  1.00 23.25 ? 245  HIS A CG    1 
ATOM   1658  N ND1   . HIS A  1 247  ? -52.633 68.779  62.412  1.00 26.42 ? 245  HIS A ND1   1 
ATOM   1659  C CD2   . HIS A  1 247  ? -50.769 69.649  63.154  1.00 24.37 ? 245  HIS A CD2   1 
ATOM   1660  C CE1   . HIS A  1 247  ? -52.943 69.927  62.989  1.00 26.64 ? 245  HIS A CE1   1 
ATOM   1661  N NE2   . HIS A  1 247  ? -51.831 70.475  63.446  1.00 24.56 ? 245  HIS A NE2   1 
ATOM   1662  N N     . ALA A  1 248  ? -49.292 64.544  61.699  1.00 24.42 ? 246  ALA A N     1 
ATOM   1663  C CA    . ALA A  1 248  ? -48.796 63.488  60.820  1.00 25.67 ? 246  ALA A CA    1 
ATOM   1664  C C     . ALA A  1 248  ? -49.379 62.133  61.198  1.00 26.54 ? 246  ALA A C     1 
ATOM   1665  O O     . ALA A  1 248  ? -49.769 61.360  60.322  1.00 25.44 ? 246  ALA A O     1 
ATOM   1666  C CB    . ALA A  1 248  ? -47.264 63.441  60.854  1.00 29.07 ? 246  ALA A CB    1 
ATOM   1667  N N     . ILE A  1 249  ? -49.442 61.831  62.498  1.00 23.55 ? 247  ILE A N     1 
ATOM   1668  C CA    . ILE A  1 249  ? -50.022 60.572  62.961  1.00 23.76 ? 247  ILE A CA    1 
ATOM   1669  C C     . ILE A  1 249  ? -51.521 60.532  62.690  1.00 25.00 ? 247  ILE A C     1 
ATOM   1670  O O     . ILE A  1 249  ? -52.070 59.502  62.272  1.00 26.41 ? 247  ILE A O     1 
ATOM   1671  C CB    . ILE A  1 249  ? -49.718 60.375  64.458  1.00 19.95 ? 247  ILE A CB    1 
ATOM   1672  C CG1   . ILE A  1 249  ? -48.206 60.264  64.681  1.00 20.74 ? 247  ILE A CG1   1 
ATOM   1673  C CG2   . ILE A  1 249  ? -50.431 59.102  64.985  1.00 20.29 ? 247  ILE A CG2   1 
ATOM   1674  C CD1   . ILE A  1 249  ? -47.784 60.573  66.169  1.00 18.66 ? 247  ILE A CD1   1 
ATOM   1675  N N     . GLY A  1 250  ? -52.211 61.646  62.927  1.00 24.50 ? 248  GLY A N     1 
ATOM   1676  C CA    . GLY A  1 250  ? -53.647 61.673  62.687  1.00 24.97 ? 248  GLY A CA    1 
ATOM   1677  C C     . GLY A  1 250  ? -53.995 61.546  61.215  1.00 26.36 ? 248  GLY A C     1 
ATOM   1678  O O     . GLY A  1 250  ? -54.963 60.872  60.854  1.00 26.79 ? 248  GLY A O     1 
ATOM   1679  N N     . LYS A  1 251  ? -53.217 62.199  60.348  1.00 25.75 ? 249  LYS A N     1 
ATOM   1680  C CA    . LYS A  1 251  ? -53.385 62.007  58.906  1.00 28.01 ? 249  LYS A CA    1 
ATOM   1681  C C     . LYS A  1 251  ? -53.167 60.548  58.520  1.00 29.65 ? 249  LYS A C     1 
ATOM   1682  O O     . LYS A  1 251  ? -53.934 59.975  57.735  1.00 30.48 ? 249  LYS A O     1 
ATOM   1683  C CB    . LYS A  1 251  ? -52.404 62.896  58.133  1.00 29.64 ? 249  LYS A CB    1 
ATOM   1684  C CG    . LYS A  1 251  ? -52.673 64.392  58.170  1.00 31.39 ? 249  LYS A CG    1 
ATOM   1685  C CD    . LYS A  1 251  ? -51.543 65.114  57.417  1.00 32.58 ? 249  LYS A CD    1 
ATOM   1686  C CE    . LYS A  1 251  ? -51.545 66.609  57.626  1.00 32.08 ? 249  LYS A CE    1 
ATOM   1687  N NZ    . LYS A  1 251  ? -50.258 67.186  57.059  1.00 29.32 ? 249  LYS A NZ    1 
ATOM   1688  N N     . ALA A  1 252  ? -52.099 59.939  59.047  1.00 27.57 ? 250  ALA A N     1 
ATOM   1689  C CA    . ALA A  1 252  ? -51.802 58.545  58.735  1.00 29.72 ? 250  ALA A CA    1 
ATOM   1690  C C     . ALA A  1 252  ? -52.861 57.615  59.306  1.00 28.48 ? 250  ALA A C     1 
ATOM   1691  O O     . ALA A  1 252  ? -53.246 56.632  58.661  1.00 32.80 ? 250  ALA A O     1 
ATOM   1692  C CB    . ALA A  1 252  ? -50.415 58.172  59.270  1.00 26.78 ? 250  ALA A CB    1 
ATOM   1693  N N     . SER A  1 253  ? -53.338 57.904  60.521  1.00 26.97 ? 251  SER A N     1 
ATOM   1694  C CA    . SER A  1 253  ? -54.350 57.056  61.142  1.00 29.72 ? 251  SER A CA    1 
ATOM   1695  C C     . SER A  1 253  ? -55.567 56.899  60.240  1.00 29.92 ? 251  SER A C     1 
ATOM   1696  O O     . SER A  1 253  ? -56.118 55.799  60.113  1.00 26.96 ? 251  SER A O     1 
ATOM   1697  C CB    . SER A  1 253  ? -54.747 57.640  62.497  1.00 26.56 ? 251  SER A CB    1 
ATOM   1698  O OG    . SER A  1 253  ? -55.691 56.817  63.139  1.00 26.95 ? 251  SER A OG    1 
ATOM   1699  N N     . ALA A  1 254  ? -55.991 57.993  59.606  1.00 25.83 ? 252  ALA A N     1 
ATOM   1700  C CA    . ALA A  1 254  ? -57.052 57.981  58.597  1.00 29.77 ? 252  ALA A CA    1 
ATOM   1701  C C     . ALA A  1 254  ? -58.330 57.336  59.126  1.00 32.00 ? 252  ALA A C     1 
ATOM   1702  O O     . ALA A  1 254  ? -59.000 56.571  58.432  1.00 27.69 ? 252  ALA A O     1 
ATOM   1703  C CB    . ALA A  1 254  ? -56.579 57.291  57.314  1.00 33.44 ? 252  ALA A CB    1 
ATOM   1704  N N     . GLY A  1 255  ? -58.681 57.657  60.368  1.00 30.92 ? 253  GLY A N     1 
ATOM   1705  C CA    . GLY A  1 255  ? -59.905 57.146  60.939  1.00 30.94 ? 253  GLY A CA    1 
ATOM   1706  C C     . GLY A  1 255  ? -59.862 55.732  61.482  1.00 33.34 ? 253  GLY A C     1 
ATOM   1707  O O     . GLY A  1 255  ? -60.925 55.177  61.754  1.00 32.18 ? 253  GLY A O     1 
ATOM   1708  N N     . ARG A  1 256  ? -58.682 55.125  61.667  1.00 28.52 ? 254  ARG A N     1 
ATOM   1709  C CA    . ARG A  1 256  ? -58.634 53.784  62.253  1.00 27.74 ? 254  ARG A CA    1 
ATOM   1710  C C     . ARG A  1 256  ? -58.980 53.768  63.736  1.00 31.51 ? 254  ARG A C     1 
ATOM   1711  O O     . ARG A  1 256  ? -59.183 52.683  64.298  1.00 30.51 ? 254  ARG A O     1 
ATOM   1712  C CB    . ARG A  1 256  ? -57.254 53.146  62.059  1.00 28.74 ? 254  ARG A CB    1 
ATOM   1713  C CG    . ARG A  1 256  ? -57.025 52.536  60.667  1.00 32.44 ? 254  ARG A CG    1 
ATOM   1714  C CD    . ARG A  1 256  ? -55.580 52.075  60.517  1.00 33.97 ? 254  ARG A CD    1 
ATOM   1715  N NE    . ARG A  1 256  ? -54.674 53.192  60.275  1.00 30.52 ? 254  ARG A NE    1 
ATOM   1716  C CZ    . ARG A  1 256  ? -53.354 53.079  60.205  1.00 32.66 ? 254  ARG A CZ    1 
ATOM   1717  N NH1   . ARG A  1 256  ? -52.747 51.925  60.440  1.00 36.58 ? 254  ARG A NH1   1 
ATOM   1718  N NH2   . ARG A  1 256  ? -52.626 54.145  59.876  1.00 30.95 ? 254  ARG A NH2   1 
ATOM   1719  N N     . GLY A  1 257  ? -59.041 54.924  64.390  1.00 28.53 ? 255  GLY A N     1 
ATOM   1720  C CA    . GLY A  1 257  ? -59.442 54.957  65.778  1.00 27.59 ? 255  GLY A CA    1 
ATOM   1721  C C     . GLY A  1 257  ? -58.296 54.697  66.738  1.00 29.48 ? 255  GLY A C     1 
ATOM   1722  O O     . GLY A  1 257  ? -57.160 54.423  66.359  1.00 27.71 ? 255  GLY A O     1 
ATOM   1723  N N     . ILE A  1 258  ? -58.619 54.774  68.029  1.00 25.92 ? 256  ILE A N     1 
ATOM   1724  C CA    . ILE A  1 258  ? -57.560 54.790  69.034  1.00 25.99 ? 256  ILE A CA    1 
ATOM   1725  C C     . ILE A  1 258  ? -56.998 53.419  69.356  1.00 28.98 ? 256  ILE A C     1 
ATOM   1726  O O     . ILE A  1 258  ? -55.937 53.334  69.985  1.00 25.27 ? 256  ILE A O     1 
ATOM   1727  C CB    . ILE A  1 258  ? -58.041 55.434  70.341  1.00 26.60 ? 256  ILE A CB    1 
ATOM   1728  C CG1   . ILE A  1 258  ? -59.130 54.577  70.988  1.00 26.36 ? 256  ILE A CG1   1 
ATOM   1729  C CG2   . ILE A  1 258  ? -58.533 56.853  70.090  1.00 26.38 ? 256  ILE A CG2   1 
ATOM   1730  C CD1   . ILE A  1 258  ? -59.705 55.216  72.235  1.00 23.41 ? 256  ILE A CD1   1 
ATOM   1731  N N     . TYR A  1 259  ? -57.665 52.335  68.964  1.00 28.25 ? 257  TYR A N     1 
ATOM   1732  C CA    . TYR A  1 259  ? -57.135 51.016  69.283  1.00 27.20 ? 257  TYR A CA    1 
ATOM   1733  C C     . TYR A  1 259  ? -56.385 50.394  68.113  1.00 29.49 ? 257  TYR A C     1 
ATOM   1734  O O     . TYR A  1 259  ? -55.266 49.894  68.286  1.00 32.27 ? 257  TYR A O     1 
ATOM   1735  C CB    . TYR A  1 259  ? -58.264 50.096  69.752  1.00 30.72 ? 257  TYR A CB    1 
ATOM   1736  C CG    . TYR A  1 259  ? -59.086 50.672  70.889  1.00 28.73 ? 257  TYR A CG    1 
ATOM   1737  C CD1   . TYR A  1 259  ? -58.540 50.854  72.155  1.00 29.16 ? 257  TYR A CD1   1 
ATOM   1738  C CD2   . TYR A  1 259  ? -60.419 51.036  70.691  1.00 29.44 ? 257  TYR A CD2   1 
ATOM   1739  C CE1   . TYR A  1 259  ? -59.308 51.377  73.194  1.00 27.54 ? 257  TYR A CE1   1 
ATOM   1740  C CE2   . TYR A  1 259  ? -61.189 51.559  71.724  1.00 28.61 ? 257  TYR A CE2   1 
ATOM   1741  C CZ    . TYR A  1 259  ? -60.625 51.729  72.970  1.00 28.29 ? 257  TYR A CZ    1 
ATOM   1742  O OH    . TYR A  1 259  ? -61.381 52.262  73.990  1.00 28.94 ? 257  TYR A OH    1 
ATOM   1743  N N     . GLU A  1 260  ? -56.968 50.443  66.917  1.00 26.87 ? 258  GLU A N     1 
ATOM   1744  C CA    . GLU A  1 260  ? -56.291 49.955  65.722  1.00 30.64 ? 258  GLU A CA    1 
ATOM   1745  C C     . GLU A  1 260  ? -55.231 50.927  65.218  1.00 30.65 ? 258  GLU A C     1 
ATOM   1746  O O     . GLU A  1 260  ? -54.190 50.492  64.715  1.00 34.12 ? 258  GLU A O     1 
ATOM   1747  C CB    . GLU A  1 260  ? -57.318 49.674  64.619  1.00 34.61 ? 258  GLU A CB    1 
ATOM   1748  C CG    . GLU A  1 260  ? -56.680 49.444  63.250  1.00 39.58 ? 258  GLU A CG    1 
ATOM   1749  C CD    . GLU A  1 260  ? -57.650 48.922  62.205  1.00 44.99 ? 258  GLU A CD    1 
ATOM   1750  O OE1   . GLU A  1 260  ? -58.874 48.934  62.454  1.00 46.46 ? 258  GLU A OE1   1 
ATOM   1751  O OE2   . GLU A  1 260  ? -57.172 48.497  61.131  1.00 52.44 ? 258  GLU A OE2   1 
ATOM   1752  N N     . GLY A  1 261  ? -55.458 52.231  65.364  1.00 30.42 ? 259  GLY A N     1 
ATOM   1753  C CA    . GLY A  1 261  ? -54.612 53.229  64.751  1.00 25.78 ? 259  GLY A CA    1 
ATOM   1754  C C     . GLY A  1 261  ? -53.535 53.747  65.683  1.00 26.43 ? 259  GLY A C     1 
ATOM   1755  O O     . GLY A  1 261  ? -53.539 53.488  66.892  1.00 29.42 ? 259  GLY A O     1 
ATOM   1756  N N     . PRO A  1 262  ? -52.588 54.493  65.127  1.00 25.26 ? 260  PRO A N     1 
ATOM   1757  C CA    . PRO A  1 262  ? -51.430 54.935  65.907  1.00 25.51 ? 260  PRO A CA    1 
ATOM   1758  C C     . PRO A  1 262  ? -51.792 56.089  66.828  1.00 26.17 ? 260  PRO A C     1 
ATOM   1759  O O     . PRO A  1 262  ? -52.767 56.815  66.620  1.00 25.73 ? 260  PRO A O     1 
ATOM   1760  C CB    . PRO A  1 262  ? -50.428 55.382  64.832  1.00 26.97 ? 260  PRO A CB    1 
ATOM   1761  C CG    . PRO A  1 262  ? -51.299 55.833  63.692  1.00 24.36 ? 260  PRO A CG    1 
ATOM   1762  C CD    . PRO A  1 262  ? -52.534 54.946  63.728  1.00 26.77 ? 260  PRO A CD    1 
ATOM   1763  N N     . GLY A  1 263  ? -50.976 56.246  67.865  1.00 25.58 ? 261  GLY A N     1 
ATOM   1764  C CA    . GLY A  1 263  ? -51.136 57.362  68.776  1.00 24.57 ? 261  GLY A CA    1 
ATOM   1765  C C     . GLY A  1 263  ? -49.801 58.010  69.085  1.00 23.77 ? 261  GLY A C     1 
ATOM   1766  O O     . GLY A  1 263  ? -48.788 57.649  68.478  1.00 21.27 ? 261  GLY A O     1 
ATOM   1767  N N     . ILE A  1 264  ? -49.788 58.962  70.022  1.00 22.82 ? 262  ILE A N     1 
ATOM   1768  C CA    . ILE A  1 264  ? -48.577 59.672  70.418  1.00 22.84 ? 262  ILE A CA    1 
ATOM   1769  C C     . ILE A  1 264  ? -48.410 59.552  71.926  1.00 25.02 ? 262  ILE A C     1 
ATOM   1770  O O     . ILE A  1 264  ? -49.388 59.382  72.661  1.00 21.13 ? 262  ILE A O     1 
ATOM   1771  C CB    . ILE A  1 264  ? -48.626 61.159  70.007  1.00 18.54 ? 262  ILE A CB    1 
ATOM   1772  C CG1   . ILE A  1 264  ? -47.226 61.764  70.087  1.00 21.93 ? 262  ILE A CG1   1 
ATOM   1773  C CG2   . ILE A  1 264  ? -49.642 61.931  70.877  1.00 20.24 ? 262  ILE A CG2   1 
ATOM   1774  C CD1   . ILE A  1 264  ? -47.117 63.170  69.522  1.00 24.95 ? 262  ILE A CD1   1 
ATOM   1775  N N     . SER A  1 265  ? -47.163 59.638  72.383  1.00 21.59 ? 263  SER A N     1 
ATOM   1776  C CA    . SER A  1 265  ? -46.845 59.697  73.806  1.00 24.32 ? 263  SER A CA    1 
ATOM   1777  C C     . SER A  1 265  ? -46.119 61.002  74.083  1.00 23.79 ? 263  SER A C     1 
ATOM   1778  O O     . SER A  1 265  ? -45.271 61.428  73.287  1.00 28.41 ? 263  SER A O     1 
ATOM   1779  C CB    . SER A  1 265  ? -45.966 58.528  74.240  1.00 25.44 ? 263  SER A CB    1 
ATOM   1780  O OG    . SER A  1 265  ? -46.658 57.296  74.140  1.00 33.73 ? 263  SER A OG    1 
ATOM   1781  N N     . ILE A  1 266  ? -46.437 61.640  75.208  1.00 23.23 ? 264  ILE A N     1 
ATOM   1782  C CA    . ILE A  1 266  ? -45.810 62.909  75.561  1.00 24.83 ? 264  ILE A CA    1 
ATOM   1783  C C     . ILE A  1 266  ? -45.280 62.829  76.987  1.00 22.08 ? 264  ILE A C     1 
ATOM   1784  O O     . ILE A  1 266  ? -45.736 62.030  77.806  1.00 22.32 ? 264  ILE A O     1 
ATOM   1785  C CB    . ILE A  1 266  ? -46.765 64.109  75.427  1.00 24.20 ? 264  ILE A CB    1 
ATOM   1786  C CG1   . ILE A  1 266  ? -47.935 63.970  76.411  1.00 24.53 ? 264  ILE A CG1   1 
ATOM   1787  C CG2   . ILE A  1 266  ? -47.313 64.230  73.987  1.00 24.58 ? 264  ILE A CG2   1 
ATOM   1788  C CD1   . ILE A  1 266  ? -48.752 65.252  76.555  1.00 27.70 ? 264  ILE A CD1   1 
ATOM   1789  N N     . LYS A  1 267  ? -44.294 63.673  77.274  1.00 23.75 ? 265  LYS A N     1 
ATOM   1790  C CA    . LYS A  1 267  ? -43.777 63.831  78.625  1.00 19.60 ? 265  LYS A CA    1 
ATOM   1791  C C     . LYS A  1 267  ? -44.086 65.245  79.081  1.00 21.23 ? 265  LYS A C     1 
ATOM   1792  O O     . LYS A  1 267  ? -43.798 66.215  78.369  1.00 21.39 ? 265  LYS A O     1 
ATOM   1793  C CB    . LYS A  1 267  ? -42.273 63.553  78.685  1.00 25.76 ? 265  LYS A CB    1 
ATOM   1794  C CG    . LYS A  1 267  ? -41.948 62.076  78.745  1.00 30.27 ? 265  LYS A CG    1 
ATOM   1795  C CD    . LYS A  1 267  ? -40.471 61.826  78.995  1.00 33.71 ? 265  LYS A CD    1 
ATOM   1796  C CE    . LYS A  1 267  ? -40.189 60.315  79.040  1.00 32.68 ? 265  LYS A CE    1 
ATOM   1797  N NZ    . LYS A  1 267  ? -40.485 59.659  77.732  1.00 33.30 ? 265  LYS A NZ    1 
ATOM   1798  N N     . LEU A  1 268  ? -44.716 65.360  80.253  1.00 18.95 ? 266  LEU A N     1 
ATOM   1799  C CA    . LEU A  1 268  ? -45.109 66.680  80.721  1.00 19.85 ? 266  LEU A CA    1 
ATOM   1800  C C     . LEU A  1 268  ? -43.903 67.562  80.978  1.00 20.77 ? 266  LEU A C     1 
ATOM   1801  O O     . LEU A  1 268  ? -43.986 68.785  80.812  1.00 22.09 ? 266  LEU A O     1 
ATOM   1802  C CB    . LEU A  1 268  ? -45.967 66.554  81.986  1.00 20.29 ? 266  LEU A CB    1 
ATOM   1803  C CG    . LEU A  1 268  ? -47.300 65.817  81.763  1.00 22.68 ? 266  LEU A CG    1 
ATOM   1804  C CD1   . LEU A  1 268  ? -48.048 65.637  83.076  1.00 20.34 ? 266  LEU A CD1   1 
ATOM   1805  C CD2   . LEU A  1 268  ? -48.191 66.540  80.734  1.00 24.17 ? 266  LEU A CD2   1 
ATOM   1806  N N     . SER A  1 269  ? -42.768 66.971  81.364  1.00 21.20 ? 267  SER A N     1 
ATOM   1807  C CA    . SER A  1 269  ? -41.595 67.791  81.638  1.00 22.48 ? 267  SER A CA    1 
ATOM   1808  C C     . SER A  1 269  ? -41.068 68.477  80.385  1.00 24.59 ? 267  SER A C     1 
ATOM   1809  O O     . SER A  1 269  ? -40.346 69.471  80.503  1.00 24.24 ? 267  SER A O     1 
ATOM   1810  C CB    . SER A  1 269  ? -40.487 66.952  82.277  1.00 25.40 ? 267  SER A CB    1 
ATOM   1811  O OG    . SER A  1 269  ? -39.867 66.097  81.339  1.00 25.49 ? 267  SER A OG    1 
ATOM   1812  N N     . ALA A  1 270  ? -41.398 67.954  79.198  1.00 20.57 ? 268  ALA A N     1 
ATOM   1813  C CA    . ALA A  1 270  ? -41.025 68.617  77.950  1.00 23.25 ? 268  ALA A CA    1 
ATOM   1814  C C     . ALA A  1 270  ? -41.791 69.912  77.739  1.00 22.23 ? 268  ALA A C     1 
ATOM   1815  O O     . ALA A  1 270  ? -41.318 70.798  77.025  1.00 20.83 ? 268  ALA A O     1 
ATOM   1816  C CB    . ALA A  1 270  ? -41.282 67.680  76.763  1.00 22.92 ? 268  ALA A CB    1 
ATOM   1817  N N     . LEU A  1 271  ? -42.970 70.044  78.336  1.00 24.99 ? 269  LEU A N     1 
ATOM   1818  C CA    . LEU A  1 271  ? -43.886 71.108  77.972  1.00 23.21 ? 269  LEU A CA    1 
ATOM   1819  C C     . LEU A  1 271  ? -43.833 72.303  78.907  1.00 23.37 ? 269  LEU A C     1 
ATOM   1820  O O     . LEU A  1 271  ? -44.534 73.291  78.666  1.00 23.17 ? 269  LEU A O     1 
ATOM   1821  C CB    . LEU A  1 271  ? -45.306 70.557  77.909  1.00 20.57 ? 269  LEU A CB    1 
ATOM   1822  C CG    . LEU A  1 271  ? -45.475 69.654  76.686  1.00 21.81 ? 269  LEU A CG    1 
ATOM   1823  C CD1   . LEU A  1 271  ? -46.865 69.057  76.652  1.00 23.68 ? 269  LEU A CD1   1 
ATOM   1824  C CD2   . LEU A  1 271  ? -45.202 70.491  75.444  1.00 21.86 ? 269  LEU A CD2   1 
ATOM   1825  N N     . HIS A  1 272  ? -43.043 72.237  79.978  1.00 21.42 ? 270  HIS A N     1 
ATOM   1826  C CA    . HIS A  1 272  ? -42.900 73.392  80.849  1.00 21.30 ? 270  HIS A CA    1 
ATOM   1827  C C     . HIS A  1 272  ? -41.561 73.283  81.561  1.00 25.13 ? 270  HIS A C     1 
ATOM   1828  O O     . HIS A  1 272  ? -41.214 72.186  82.024  1.00 23.80 ? 270  HIS A O     1 
ATOM   1829  C CB    . HIS A  1 272  ? -44.039 73.456  81.873  1.00 23.21 ? 270  HIS A CB    1 
ATOM   1830  C CG    . HIS A  1 272  ? -44.166 74.786  82.535  1.00 26.51 ? 270  HIS A CG    1 
ATOM   1831  N ND1   . HIS A  1 272  ? -43.253 75.245  83.461  1.00 28.69 ? 270  HIS A ND1   1 
ATOM   1832  C CD2   . HIS A  1 272  ? -45.083 75.774  82.385  1.00 28.13 ? 270  HIS A CD2   1 
ATOM   1833  C CE1   . HIS A  1 272  ? -43.611 76.453  83.864  1.00 29.59 ? 270  HIS A CE1   1 
ATOM   1834  N NE2   . HIS A  1 272  ? -44.717 76.798  83.225  1.00 29.52 ? 270  HIS A NE2   1 
ATOM   1835  N N     . PRO A  1 273  ? -40.784 74.370  81.662  1.00 21.99 ? 271  PRO A N     1 
ATOM   1836  C CA    . PRO A  1 273  ? -39.458 74.273  82.292  1.00 21.38 ? 271  PRO A CA    1 
ATOM   1837  C C     . PRO A  1 273  ? -39.481 74.187  83.807  1.00 26.29 ? 271  PRO A C     1 
ATOM   1838  O O     . PRO A  1 273  ? -38.427 73.909  84.397  1.00 24.70 ? 271  PRO A O     1 
ATOM   1839  C CB    . PRO A  1 273  ? -38.760 75.563  81.840  1.00 24.52 ? 271  PRO A CB    1 
ATOM   1840  C CG    . PRO A  1 273  ? -39.885 76.553  81.686  1.00 24.98 ? 271  PRO A CG    1 
ATOM   1841  C CD    . PRO A  1 273  ? -41.068 75.729  81.164  1.00 24.57 ? 271  PRO A CD    1 
ATOM   1842  N N     . ARG A  1 274  ? -40.621 74.427  84.454  1.00 23.06 ? 272  ARG A N     1 
ATOM   1843  C CA    . ARG A  1 274  ? -40.698 74.319  85.911  1.00 23.37 ? 272  ARG A CA    1 
ATOM   1844  C C     . ARG A  1 274  ? -41.799 73.348  86.310  1.00 26.28 ? 272  ARG A C     1 
ATOM   1845  O O     . ARG A  1 274  ? -42.729 73.710  87.050  1.00 23.93 ? 272  ARG A O     1 
ATOM   1846  C CB    . ARG A  1 274  ? -40.942 75.689  86.546  1.00 22.31 ? 272  ARG A CB    1 
ATOM   1847  C CG    . ARG A  1 274  ? -39.805 76.727  86.265  1.00 23.20 ? 272  ARG A CG    1 
ATOM   1848  C CD    . ARG A  1 274  ? -38.432 76.238  86.822  1.00 26.34 ? 272  ARG A CD    1 
ATOM   1849  N NE    . ARG A  1 274  ? -38.501 75.794  88.214  1.00 24.65 ? 272  ARG A NE    1 
ATOM   1850  C CZ    . ARG A  1 274  ? -38.374 76.593  89.268  1.00 25.36 ? 272  ARG A CZ    1 
ATOM   1851  N NH1   . ARG A  1 274  ? -38.225 77.898  89.135  1.00 24.59 ? 272  ARG A NH1   1 
ATOM   1852  N NH2   . ARG A  1 274  ? -38.403 76.069  90.488  1.00 23.11 ? 272  ARG A NH2   1 
ATOM   1853  N N     . TYR A  1 275  ? -41.722 72.121  85.806  1.00 21.87 ? 273  TYR A N     1 
ATOM   1854  C CA    . TYR A  1 275  ? -42.758 71.122  86.071  1.00 21.92 ? 273  TYR A CA    1 
ATOM   1855  C C     . TYR A  1 275  ? -42.411 70.454  87.387  1.00 21.77 ? 273  TYR A C     1 
ATOM   1856  O O     . TYR A  1 275  ? -41.646 69.500  87.431  1.00 23.39 ? 273  TYR A O     1 
ATOM   1857  C CB    . TYR A  1 275  ? -42.857 70.116  84.928  1.00 24.73 ? 273  TYR A CB    1 
ATOM   1858  C CG    . TYR A  1 275  ? -43.764 68.943  85.220  1.00 20.91 ? 273  TYR A CG    1 
ATOM   1859  C CD1   . TYR A  1 275  ? -45.090 69.139  85.596  1.00 24.84 ? 273  TYR A CD1   1 
ATOM   1860  C CD2   . TYR A  1 275  ? -43.307 67.632  85.067  1.00 22.57 ? 273  TYR A CD2   1 
ATOM   1861  C CE1   . TYR A  1 275  ? -45.927 68.066  85.852  1.00 24.44 ? 273  TYR A CE1   1 
ATOM   1862  C CE2   . TYR A  1 275  ? -44.136 66.540  85.339  1.00 24.61 ? 273  TYR A CE2   1 
ATOM   1863  C CZ    . TYR A  1 275  ? -45.442 66.773  85.730  1.00 24.36 ? 273  TYR A CZ    1 
ATOM   1864  O OH    . TYR A  1 275  ? -46.272 65.716  86.000  1.00 26.33 ? 273  TYR A OH    1 
ATOM   1865  N N     . SER A  1 276  ? -42.994 70.952  88.475  1.00 24.83 ? 274  SER A N     1 
ATOM   1866  C CA    . SER A  1 276  ? -42.691 70.410  89.797  1.00 24.25 ? 274  SER A CA    1 
ATOM   1867  C C     . SER A  1 276  ? -43.788 70.828  90.765  1.00 24.65 ? 274  SER A C     1 
ATOM   1868  O O     . SER A  1 276  ? -44.509 71.798  90.521  1.00 23.58 ? 274  SER A O     1 
ATOM   1869  C CB    . SER A  1 276  ? -41.325 70.891  90.299  1.00 26.94 ? 274  SER A CB    1 
ATOM   1870  O OG    . SER A  1 276  ? -41.416 72.251  90.695  1.00 26.15 ? 274  SER A OG    1 
ATOM   1871  N N     . ARG A  1 277  ? -43.907 70.079  91.874  1.00 23.10 ? 275  ARG A N     1 
ATOM   1872  C CA    . ARG A  1 277  ? -44.933 70.400  92.865  1.00 22.24 ? 275  ARG A CA    1 
ATOM   1873  C C     . ARG A  1 277  ? -44.750 71.808  93.421  1.00 25.44 ? 275  ARG A C     1 
ATOM   1874  O O     . ARG A  1 277  ? -45.734 72.499  93.720  1.00 23.79 ? 275  ARG A O     1 
ATOM   1875  C CB    . ARG A  1 277  ? -44.919 69.375  94.006  1.00 24.96 ? 275  ARG A CB    1 
ATOM   1876  C CG    . ARG A  1 277  ? -45.835 69.716  95.186  1.00 24.51 ? 275  ARG A CG    1 
ATOM   1877  C CD    . ARG A  1 277  ? -47.312 69.862  94.781  1.00 24.94 ? 275  ARG A CD    1 
ATOM   1878  N NE    . ARG A  1 277  ? -48.152 70.228  95.919  1.00 24.46 ? 275  ARG A NE    1 
ATOM   1879  C CZ    . ARG A  1 277  ? -48.309 71.466  96.368  1.00 26.32 ? 275  ARG A CZ    1 
ATOM   1880  N NH1   . ARG A  1 277  ? -47.682 72.490  95.811  1.00 25.73 ? 275  ARG A NH1   1 
ATOM   1881  N NH2   . ARG A  1 277  ? -49.127 71.687  97.398  1.00 27.93 ? 275  ARG A NH2   1 
ATOM   1882  N N     . ALA A  1 278  ? -43.496 72.240  93.569  1.00 24.20 ? 276  ALA A N     1 
ATOM   1883  C CA    . ALA A  1 278  ? -43.210 73.568  94.096  1.00 27.60 ? 276  ALA A CA    1 
ATOM   1884  C C     . ALA A  1 278  ? -43.777 74.646  93.193  1.00 25.29 ? 276  ALA A C     1 
ATOM   1885  O O     . ALA A  1 278  ? -44.123 75.733  93.661  1.00 24.71 ? 276  ALA A O     1 
ATOM   1886  C CB    . ALA A  1 278  ? -41.695 73.759  94.248  1.00 24.33 ? 276  ALA A CB    1 
ATOM   1887  N N     . GLN A  1 279  ? -43.860 74.373  91.893  1.00 23.99 ? 277  GLN A N     1 
ATOM   1888  C CA    . GLN A  1 279  ? -44.377 75.338  90.934  1.00 24.36 ? 277  GLN A CA    1 
ATOM   1889  C C     . GLN A  1 279  ? -45.765 74.942  90.438  1.00 26.31 ? 277  GLN A C     1 
ATOM   1890  O O     . GLN A  1 279  ? -46.129 75.242  89.300  1.00 27.34 ? 277  GLN A O     1 
ATOM   1891  C CB    . GLN A  1 279  ? -43.397 75.493  89.768  1.00 23.40 ? 277  GLN A CB    1 
ATOM   1892  C CG    . GLN A  1 279  ? -42.021 75.998  90.204  1.00 25.54 ? 277  GLN A CG    1 
ATOM   1893  C CD    . GLN A  1 279  ? -42.101 77.374  90.819  1.00 29.93 ? 277  GLN A CD    1 
ATOM   1894  O OE1   . GLN A  1 279  ? -42.849 78.226  90.341  1.00 35.87 ? 277  GLN A OE1   1 
ATOM   1895  N NE2   . GLN A  1 279  ? -41.360 77.597  91.899  1.00 25.20 ? 277  GLN A NE2   1 
ATOM   1896  N N     . ALA A  1 280  ? -46.563 74.310  91.311  1.00 27.66 ? 278  ALA A N     1 
ATOM   1897  C CA    . ALA A  1 280  ? -47.827 73.711  90.882  1.00 27.11 ? 278  ALA A CA    1 
ATOM   1898  C C     . ALA A  1 280  ? -48.768 74.739  90.281  1.00 26.38 ? 278  ALA A C     1 
ATOM   1899  O O     . ALA A  1 280  ? -49.511 74.425  89.344  1.00 25.93 ? 278  ALA A O     1 
ATOM   1900  C CB    . ALA A  1 280  ? -48.515 73.008  92.052  1.00 24.72 ? 278  ALA A CB    1 
ATOM   1901  N N     . ALA A  1 281  ? -48.775 75.959  90.820  1.00 23.16 ? 279  ALA A N     1 
ATOM   1902  C CA    . ALA A  1 281  ? -49.652 76.994  90.282  1.00 27.60 ? 279  ALA A CA    1 
ATOM   1903  C C     . ALA A  1 281  ? -49.292 77.331  88.842  1.00 27.79 ? 279  ALA A C     1 
ATOM   1904  O O     . ALA A  1 281  ? -50.182 77.509  87.999  1.00 24.37 ? 279  ALA A O     1 
ATOM   1905  C CB    . ALA A  1 281  ? -49.587 78.250  91.151  1.00 28.66 ? 279  ALA A CB    1 
ATOM   1906  N N     . ARG A  1 282  ? -47.995 77.473  88.553  1.00 22.76 ? 280  ARG A N     1 
ATOM   1907  C CA    . ARG A  1 282  ? -47.576 77.715  87.174  1.00 26.73 ? 280  ARG A CA    1 
ATOM   1908  C C     . ARG A  1 282  ? -47.910 76.523  86.292  1.00 25.95 ? 280  ARG A C     1 
ATOM   1909  O O     . ARG A  1 282  ? -48.259 76.687  85.114  1.00 25.44 ? 280  ARG A O     1 
ATOM   1910  C CB    . ARG A  1 282  ? -46.073 78.008  87.104  1.00 24.43 ? 280  ARG A CB    1 
ATOM   1911  C CG    . ARG A  1 282  ? -45.635 79.332  87.715  1.00 28.22 ? 280  ARG A CG    1 
ATOM   1912  C CD    . ARG A  1 282  ? -44.198 79.644  87.306  1.00 26.06 ? 280  ARG A CD    1 
ATOM   1913  N NE    . ARG A  1 282  ? -44.114 79.798  85.860  1.00 26.38 ? 280  ARG A NE    1 
ATOM   1914  C CZ    . ARG A  1 282  ? -42.988 79.797  85.162  1.00 28.65 ? 280  ARG A CZ    1 
ATOM   1915  N NH1   . ARG A  1 282  ? -41.801 79.680  85.753  1.00 24.97 ? 280  ARG A NH1   1 
ATOM   1916  N NH2   . ARG A  1 282  ? -43.049 79.910  83.836  1.00 26.05 ? 280  ARG A NH2   1 
ATOM   1917  N N     . VAL A  1 283  ? -47.777 75.312  86.840  1.00 23.53 ? 281  VAL A N     1 
ATOM   1918  C CA    . VAL A  1 283  ? -48.052 74.108  86.069  1.00 24.92 ? 281  VAL A CA    1 
ATOM   1919  C C     . VAL A  1 283  ? -49.516 74.070  85.659  1.00 25.29 ? 281  VAL A C     1 
ATOM   1920  O O     . VAL A  1 283  ? -49.846 73.865  84.486  1.00 24.53 ? 281  VAL A O     1 
ATOM   1921  C CB    . VAL A  1 283  ? -47.657 72.861  86.873  1.00 25.50 ? 281  VAL A CB    1 
ATOM   1922  C CG1   . VAL A  1 283  ? -48.302 71.611  86.266  1.00 24.14 ? 281  VAL A CG1   1 
ATOM   1923  C CG2   . VAL A  1 283  ? -46.138 72.751  86.923  1.00 24.52 ? 281  VAL A CG2   1 
ATOM   1924  N N     . MET A  1 284  ? -50.416 74.303  86.618  1.00 23.26 ? 282  MET A N     1 
ATOM   1925  C CA    . MET A  1 284  ? -51.840 74.291  86.297  1.00 27.20 ? 282  MET A CA    1 
ATOM   1926  C C     . MET A  1 284  ? -52.224 75.439  85.372  1.00 26.40 ? 282  MET A C     1 
ATOM   1927  O O     . MET A  1 284  ? -53.111 75.277  84.531  1.00 26.57 ? 282  MET A O     1 
ATOM   1928  C CB    . MET A  1 284  ? -52.665 74.343  87.582  1.00 25.57 ? 282  MET A CB    1 
ATOM   1929  C CG    . MET A  1 284  ? -52.411 73.156  88.504  1.00 25.76 ? 282  MET A CG    1 
ATOM   1930  S SD    . MET A  1 284  ? -52.601 71.555  87.695  1.00 29.07 ? 282  MET A SD    1 
ATOM   1931  C CE    . MET A  1 284  ? -54.375 71.510  87.393  1.00 30.16 ? 282  MET A CE    1 
ATOM   1932  N N     . GLY A  1 285  ? -51.578 76.600  85.514  1.00 27.92 ? 283  GLY A N     1 
ATOM   1933  C CA    . GLY A  1 285  ? -51.932 77.748  84.700  1.00 26.44 ? 283  GLY A CA    1 
ATOM   1934  C C     . GLY A  1 285  ? -51.278 77.762  83.333  1.00 28.64 ? 283  GLY A C     1 
ATOM   1935  O O     . GLY A  1 285  ? -51.847 78.300  82.380  1.00 29.02 ? 283  GLY A O     1 
ATOM   1936  N N     . GLU A  1 286  ? -50.101 77.165  83.198  1.00 27.08 ? 284  GLU A N     1 
ATOM   1937  C CA    . GLU A  1 286  ? -49.359 77.304  81.947  1.00 26.85 ? 284  GLU A CA    1 
ATOM   1938  C C     . GLU A  1 286  ? -49.149 75.989  81.216  1.00 28.55 ? 284  GLU A C     1 
ATOM   1939  O O     . GLU A  1 286  ? -49.181 75.967  79.986  1.00 29.27 ? 284  GLU A O     1 
ATOM   1940  C CB    . GLU A  1 286  ? -47.987 77.961  82.198  1.00 27.43 ? 284  GLU A CB    1 
ATOM   1941  C CG    . GLU A  1 286  ? -48.052 79.321  82.874  1.00 29.41 ? 284  GLU A CG    1 
ATOM   1942  C CD    . GLU A  1 286  ? -46.693 79.767  83.423  1.00 31.39 ? 284  GLU A CD    1 
ATOM   1943  O OE1   . GLU A  1 286  ? -45.651 79.410  82.833  1.00 30.83 ? 284  GLU A OE1   1 
ATOM   1944  O OE2   . GLU A  1 286  ? -46.674 80.459  84.465  1.00 30.46 ? 284  GLU A OE2   1 
ATOM   1945  N N     . LEU A  1 287  ? -48.916 74.893  81.937  1.00 22.93 ? 285  LEU A N     1 
ATOM   1946  C CA    . LEU A  1 287  ? -48.697 73.612  81.283  1.00 27.09 ? 285  LEU A CA    1 
ATOM   1947  C C     . LEU A  1 287  ? -50.024 72.972  80.887  1.00 25.38 ? 285  LEU A C     1 
ATOM   1948  O O     . LEU A  1 287  ? -50.166 72.472  79.768  1.00 26.75 ? 285  LEU A O     1 
ATOM   1949  C CB    . LEU A  1 287  ? -47.877 72.692  82.204  1.00 22.91 ? 285  LEU A CB    1 
ATOM   1950  C CG    . LEU A  1 287  ? -47.799 71.192  81.915  1.00 27.56 ? 285  LEU A CG    1 
ATOM   1951  C CD1   . LEU A  1 287  ? -47.543 70.897  80.470  1.00 26.38 ? 285  LEU A CD1   1 
ATOM   1952  C CD2   . LEU A  1 287  ? -46.700 70.525  82.786  1.00 28.68 ? 285  LEU A CD2   1 
ATOM   1953  N N     . LEU A  1 288  ? -51.011 73.019  81.772  1.00 25.91 ? 286  LEU A N     1 
ATOM   1954  C CA    . LEU A  1 288  ? -52.317 72.425  81.485  1.00 27.86 ? 286  LEU A CA    1 
ATOM   1955  C C     . LEU A  1 288  ? -52.932 72.893  80.168  1.00 26.72 ? 286  LEU A C     1 
ATOM   1956  O O     . LEU A  1 288  ? -53.352 72.030  79.371  1.00 25.06 ? 286  LEU A O     1 
ATOM   1957  C CB    . LEU A  1 288  ? -53.241 72.695  82.678  1.00 28.56 ? 286  LEU A CB    1 
ATOM   1958  C CG    . LEU A  1 288  ? -54.706 72.262  82.570  1.00 36.04 ? 286  LEU A CG    1 
ATOM   1959  C CD1   . LEU A  1 288  ? -54.814 70.781  82.265  1.00 31.57 ? 286  LEU A CD1   1 
ATOM   1960  C CD2   . LEU A  1 288  ? -55.422 72.600  83.867  1.00 37.60 ? 286  LEU A CD2   1 
ATOM   1961  N N     . PRO A  1 289  ? -53.004 74.195  79.857  1.00 25.63 ? 287  PRO A N     1 
ATOM   1962  C CA    . PRO A  1 289  ? -53.620 74.590  78.579  1.00 26.59 ? 287  PRO A CA    1 
ATOM   1963  C C     . PRO A  1 289  ? -52.887 74.066  77.359  1.00 25.13 ? 287  PRO A C     1 
ATOM   1964  O O     . PRO A  1 289  ? -53.522 73.846  76.319  1.00 26.10 ? 287  PRO A O     1 
ATOM   1965  C CB    . PRO A  1 289  ? -53.588 76.122  78.637  1.00 27.48 ? 287  PRO A CB    1 
ATOM   1966  C CG    . PRO A  1 289  ? -53.534 76.439  80.099  1.00 31.61 ? 287  PRO A CG    1 
ATOM   1967  C CD    . PRO A  1 289  ? -52.638 75.383  80.650  1.00 25.72 ? 287  PRO A CD    1 
ATOM   1968  N N     . ARG A  1 290  ? -51.574 73.851  77.457  1.00 26.38 ? 288  ARG A N     1 
ATOM   1969  C CA    . ARG A  1 290  ? -50.823 73.299  76.337  1.00 26.17 ? 288  ARG A CA    1 
ATOM   1970  C C     . ARG A  1 290  ? -51.171 71.843  76.108  1.00 23.80 ? 288  ARG A C     1 
ATOM   1971  O O     . ARG A  1 290  ? -51.331 71.413  74.957  1.00 22.08 ? 288  ARG A O     1 
ATOM   1972  C CB    . ARG A  1 290  ? -49.316 73.449  76.581  1.00 23.88 ? 288  ARG A CB    1 
ATOM   1973  C CG    . ARG A  1 290  ? -48.922 74.870  76.843  1.00 28.86 ? 288  ARG A CG    1 
ATOM   1974  C CD    . ARG A  1 290  ? -47.429 74.987  77.138  1.00 28.47 ? 288  ARG A CD    1 
ATOM   1975  N NE    . ARG A  1 290  ? -47.065 76.389  77.289  1.00 32.86 ? 288  ARG A NE    1 
ATOM   1976  C CZ    . ARG A  1 290  ? -46.041 76.824  78.008  1.00 33.56 ? 288  ARG A CZ    1 
ATOM   1977  N NH1   . ARG A  1 290  ? -45.246 75.987  78.657  1.00 28.88 ? 288  ARG A NH1   1 
ATOM   1978  N NH2   . ARG A  1 290  ? -45.813 78.133  78.085  1.00 37.46 ? 288  ARG A NH2   1 
ATOM   1979  N N     . VAL A  1 291  ? -51.251 71.055  77.180  1.00 20.60 ? 289  VAL A N     1 
ATOM   1980  C CA    . VAL A  1 291  ? -51.657 69.662  77.016  1.00 23.73 ? 289  VAL A CA    1 
ATOM   1981  C C     . VAL A  1 291  ? -53.080 69.593  76.478  1.00 24.36 ? 289  VAL A C     1 
ATOM   1982  O O     . VAL A  1 291  ? -53.411 68.732  75.651  1.00 21.83 ? 289  VAL A O     1 
ATOM   1983  C CB    . VAL A  1 291  ? -51.529 68.900  78.348  1.00 24.34 ? 289  VAL A CB    1 
ATOM   1984  C CG1   . VAL A  1 291  ? -52.003 67.460  78.177  1.00 24.14 ? 289  VAL A CG1   1 
ATOM   1985  C CG2   . VAL A  1 291  ? -50.112 68.957  78.838  1.00 25.46 ? 289  VAL A CG2   1 
ATOM   1986  N N     . LYS A  1 292  ? -53.941 70.500  76.931  1.00 21.50 ? 290  LYS A N     1 
ATOM   1987  C CA    . LYS A  1 292  ? -55.314 70.512  76.438  1.00 21.07 ? 290  LYS A CA    1 
ATOM   1988  C C     . LYS A  1 292  ? -55.359 70.801  74.942  1.00 23.08 ? 290  LYS A C     1 
ATOM   1989  O O     . LYS A  1 292  ? -56.128 70.172  74.204  1.00 19.45 ? 290  LYS A O     1 
ATOM   1990  C CB    . LYS A  1 292  ? -56.152 71.536  77.207  1.00 21.40 ? 290  LYS A CB    1 
ATOM   1991  C CG    . LYS A  1 292  ? -57.552 71.673  76.647  1.00 22.84 ? 290  LYS A CG    1 
ATOM   1992  C CD    . LYS A  1 292  ? -58.373 72.778  77.291  1.00 25.23 ? 290  LYS A CD    1 
ATOM   1993  C CE    . LYS A  1 292  ? -59.781 72.791  76.697  1.00 26.56 ? 290  LYS A CE    1 
ATOM   1994  N NZ    . LYS A  1 292  ? -60.716 73.528  77.579  1.00 29.26 ? 290  LYS A NZ    1 
ATOM   1995  N N     . ALA A  1 293  ? -54.532 71.734  74.471  1.00 22.99 ? 291  ALA A N     1 
ATOM   1996  C CA    . ALA A  1 293  ? -54.530 72.035  73.041  1.00 24.18 ? 291  ALA A CA    1 
ATOM   1997  C C     . ALA A  1 293  ? -54.036 70.845  72.227  1.00 23.52 ? 291  ALA A C     1 
ATOM   1998  O O     . ALA A  1 293  ? -54.518 70.603  71.115  1.00 25.32 ? 291  ALA A O     1 
ATOM   1999  C CB    . ALA A  1 293  ? -53.684 73.280  72.770  1.00 24.76 ? 291  ALA A CB    1 
ATOM   2000  N N     . LEU A  1 294  ? -53.054 70.105  72.740  1.00 22.31 ? 292  LEU A N     1 
ATOM   2001  C CA    . LEU A  1 294  ? -52.623 68.899  72.032  1.00 20.67 ? 292  LEU A CA    1 
ATOM   2002  C C     . LEU A  1 294  ? -53.710 67.830  72.071  1.00 20.44 ? 292  LEU A C     1 
ATOM   2003  O O     . LEU A  1 294  ? -54.001 67.184  71.056  1.00 21.57 ? 292  LEU A O     1 
ATOM   2004  C CB    . LEU A  1 294  ? -51.322 68.376  72.638  1.00 17.93 ? 292  LEU A CB    1 
ATOM   2005  C CG    . LEU A  1 294  ? -50.130 69.335  72.540  1.00 21.47 ? 292  LEU A CG    1 
ATOM   2006  C CD1   . LEU A  1 294  ? -48.903 68.782  73.272  1.00 21.51 ? 292  LEU A CD1   1 
ATOM   2007  C CD2   . LEU A  1 294  ? -49.785 69.621  71.048  1.00 20.90 ? 292  LEU A CD2   1 
ATOM   2008  N N     . ALA A  1 295  ? -54.323 67.630  73.237  1.00 20.01 ? 293  ALA A N     1 
ATOM   2009  C CA    . ALA A  1 295  ? -55.399 66.650  73.336  1.00 22.73 ? 293  ALA A CA    1 
ATOM   2010  C C     . ALA A  1 295  ? -56.559 66.998  72.399  1.00 21.56 ? 293  ALA A C     1 
ATOM   2011  O O     . ALA A  1 295  ? -57.160 66.100  71.796  1.00 23.76 ? 293  ALA A O     1 
ATOM   2012  C CB    . ALA A  1 295  ? -55.874 66.549  74.791  1.00 19.56 ? 293  ALA A CB    1 
ATOM   2013  N N     . LEU A  1 296  ? -56.893 68.290  72.264  1.00 21.63 ? 294  LEU A N     1 
ATOM   2014  C CA    . LEU A  1 296  ? -57.994 68.668  71.368  1.00 22.47 ? 294  LEU A CA    1 
ATOM   2015  C C     . LEU A  1 296  ? -57.705 68.251  69.933  1.00 23.18 ? 294  LEU A C     1 
ATOM   2016  O O     . LEU A  1 296  ? -58.612 67.851  69.195  1.00 20.81 ? 294  LEU A O     1 
ATOM   2017  C CB    . LEU A  1 296  ? -58.244 70.173  71.415  1.00 21.84 ? 294  LEU A CB    1 
ATOM   2018  C CG    . LEU A  1 296  ? -58.976 70.733  72.630  1.00 26.73 ? 294  LEU A CG    1 
ATOM   2019  C CD1   . LEU A  1 296  ? -58.844 72.247  72.671  1.00 28.67 ? 294  LEU A CD1   1 
ATOM   2020  C CD2   . LEU A  1 296  ? -60.453 70.341  72.596  1.00 26.51 ? 294  LEU A CD2   1 
ATOM   2021  N N     . LEU A  1 297  ? -56.445 68.372  69.516  1.00 23.29 ? 295  LEU A N     1 
ATOM   2022  C CA    . LEU A  1 297  ? -56.047 67.932  68.188  1.00 23.34 ? 295  LEU A CA    1 
ATOM   2023  C C     . LEU A  1 297  ? -56.094 66.409  68.084  1.00 23.39 ? 295  LEU A C     1 
ATOM   2024  O O     . LEU A  1 297  ? -56.603 65.864  67.098  1.00 22.97 ? 295  LEU A O     1 
ATOM   2025  C CB    . LEU A  1 297  ? -54.644 68.481  67.890  1.00 25.24 ? 295  LEU A CB    1 
ATOM   2026  C CG    . LEU A  1 297  ? -54.110 68.364  66.473  1.00 24.98 ? 295  LEU A CG    1 
ATOM   2027  C CD1   . LEU A  1 297  ? -55.075 68.997  65.465  1.00 28.56 ? 295  LEU A CD1   1 
ATOM   2028  C CD2   . LEU A  1 297  ? -52.751 69.054  66.424  1.00 28.95 ? 295  LEU A CD2   1 
ATOM   2029  N N     . ALA A  1 298  ? -55.610 65.699  69.111  1.00 23.97 ? 296  ALA A N     1 
ATOM   2030  C CA    . ALA A  1 298  ? -55.711 64.244  69.097  1.00 23.87 ? 296  ALA A CA    1 
ATOM   2031  C C     . ALA A  1 298  ? -57.168 63.800  69.036  1.00 25.20 ? 296  ALA A C     1 
ATOM   2032  O O     . ALA A  1 298  ? -57.501 62.823  68.351  1.00 22.58 ? 296  ALA A O     1 
ATOM   2033  C CB    . ALA A  1 298  ? -55.021 63.647  70.326  1.00 24.16 ? 296  ALA A CB    1 
ATOM   2034  N N     . LYS A  1 299  ? -58.049 64.506  69.750  1.00 20.58 ? 297  LYS A N     1 
ATOM   2035  C CA    . LYS A  1 299  ? -59.474 64.202  69.677  1.00 25.72 ? 297  LYS A CA    1 
ATOM   2036  C C     . LYS A  1 299  ? -59.996 64.342  68.255  1.00 26.75 ? 297  LYS A C     1 
ATOM   2037  O O     . LYS A  1 299  ? -60.744 63.479  67.777  1.00 24.47 ? 297  LYS A O     1 
ATOM   2038  C CB    . LYS A  1 299  ? -60.253 65.117  70.614  1.00 25.19 ? 297  LYS A CB    1 
ATOM   2039  C CG    . LYS A  1 299  ? -61.752 65.123  70.358  1.00 24.32 ? 297  LYS A CG    1 
ATOM   2040  C CD    . LYS A  1 299  ? -62.452 65.985  71.362  1.00 24.30 ? 297  LYS A CD    1 
ATOM   2041  C CE    . LYS A  1 299  ? -63.878 66.291  70.874  1.00 27.96 ? 297  LYS A CE    1 
ATOM   2042  N NZ    . LYS A  1 299  ? -64.587 67.128  71.848  1.00 31.21 ? 297  LYS A NZ    1 
ATOM   2043  N N     . ASN A  1 300  ? -59.597 65.406  67.554  1.00 22.19 ? 298  ASN A N     1 
ATOM   2044  C CA    . ASN A  1 300  ? -60.154 65.626  66.222  1.00 25.82 ? 298  ASN A CA    1 
ATOM   2045  C C     . ASN A  1 300  ? -59.732 64.533  65.253  1.00 25.19 ? 298  ASN A C     1 
ATOM   2046  O O     . ASN A  1 300  ? -60.527 64.114  64.402  1.00 28.25 ? 298  ASN A O     1 
ATOM   2047  C CB    . ASN A  1 300  ? -59.748 66.984  65.672  1.00 27.55 ? 298  ASN A CB    1 
ATOM   2048  C CG    . ASN A  1 300  ? -60.570 67.361  64.459  1.00 31.85 ? 298  ASN A CG    1 
ATOM   2049  O OD1   . ASN A  1 300  ? -61.740 67.760  64.585  1.00 38.70 ? 298  ASN A OD1   1 
ATOM   2050  N ND2   . ASN A  1 300  ? -59.990 67.203  63.281  1.00 29.09 ? 298  ASN A ND2   1 
ATOM   2051  N N     . TYR A  1 301  ? -58.495 64.056  65.362  1.00 24.71 ? 299  TYR A N     1 
ATOM   2052  C CA    . TYR A  1 301  ? -58.046 62.936  64.543  1.00 27.61 ? 299  TYR A CA    1 
ATOM   2053  C C     . TYR A  1 301  ? -58.419 61.583  65.134  1.00 25.57 ? 299  TYR A C     1 
ATOM   2054  O O     . TYR A  1 301  ? -58.226 60.556  64.467  1.00 27.66 ? 299  TYR A O     1 
ATOM   2055  C CB    . TYR A  1 301  ? -56.530 62.973  64.361  1.00 24.36 ? 299  TYR A CB    1 
ATOM   2056  C CG    . TYR A  1 301  ? -55.987 64.061  63.480  1.00 22.22 ? 299  TYR A CG    1 
ATOM   2057  C CD1   . TYR A  1 301  ? -56.175 64.024  62.100  1.00 24.87 ? 299  TYR A CD1   1 
ATOM   2058  C CD2   . TYR A  1 301  ? -55.253 65.109  64.016  1.00 24.66 ? 299  TYR A CD2   1 
ATOM   2059  C CE1   . TYR A  1 301  ? -55.658 65.009  61.278  1.00 25.99 ? 299  TYR A CE1   1 
ATOM   2060  C CE2   . TYR A  1 301  ? -54.724 66.102  63.199  1.00 25.78 ? 299  TYR A CE2   1 
ATOM   2061  C CZ    . TYR A  1 301  ? -54.935 66.046  61.829  1.00 28.83 ? 299  TYR A CZ    1 
ATOM   2062  O OH    . TYR A  1 301  ? -54.414 67.035  61.008  1.00 29.54 ? 299  TYR A OH    1 
ATOM   2063  N N     . ASP A  1 302  ? -58.918 61.564  66.368  1.00 24.94 ? 300  ASP A N     1 
ATOM   2064  C CA    . ASP A  1 302  ? -59.293 60.344  67.087  1.00 27.07 ? 300  ASP A CA    1 
ATOM   2065  C C     . ASP A  1 302  ? -58.109 59.377  67.203  1.00 24.90 ? 300  ASP A C     1 
ATOM   2066  O O     . ASP A  1 302  ? -58.163 58.214  66.783  1.00 22.34 ? 300  ASP A O     1 
ATOM   2067  C CB    . ASP A  1 302  ? -60.509 59.664  66.431  1.00 26.65 ? 300  ASP A CB    1 
ATOM   2068  C CG    . ASP A  1 302  ? -61.222 58.701  67.381  1.00 28.82 ? 300  ASP A CG    1 
ATOM   2069  O OD1   . ASP A  1 302  ? -61.190 58.940  68.606  1.00 27.67 ? 300  ASP A OD1   1 
ATOM   2070  O OD2   . ASP A  1 302  ? -61.808 57.695  66.911  1.00 32.37 ? 300  ASP A OD2   1 
ATOM   2071  N N     . ILE A  1 303  ? -57.035 59.870  67.820  1.00 24.65 ? 301  ILE A N     1 
ATOM   2072  C CA    . ILE A  1 303  ? -55.863 59.050  68.088  1.00 22.72 ? 301  ILE A CA    1 
ATOM   2073  C C     . ILE A  1 303  ? -55.570 59.060  69.580  1.00 22.33 ? 301  ILE A C     1 
ATOM   2074  O O     . ILE A  1 303  ? -56.038 59.918  70.334  1.00 22.88 ? 301  ILE A O     1 
ATOM   2075  C CB    . ILE A  1 303  ? -54.616 59.524  67.303  1.00 23.69 ? 301  ILE A CB    1 
ATOM   2076  C CG1   . ILE A  1 303  ? -54.141 60.879  67.834  1.00 22.62 ? 301  ILE A CG1   1 
ATOM   2077  C CG2   . ILE A  1 303  ? -54.958 59.620  65.817  1.00 22.32 ? 301  ILE A CG2   1 
ATOM   2078  C CD1   . ILE A  1 303  ? -52.763 61.331  67.270  1.00 20.45 ? 301  ILE A CD1   1 
ATOM   2079  N N     . GLY A  1 304  ? -54.769 58.090  69.998  1.00 24.98 ? 302  GLY A N     1 
ATOM   2080  C CA    . GLY A  1 304  ? -54.321 58.057  71.382  1.00 23.32 ? 302  GLY A CA    1 
ATOM   2081  C C     . GLY A  1 304  ? -53.335 59.179  71.674  1.00 22.06 ? 302  GLY A C     1 
ATOM   2082  O O     . GLY A  1 304  ? -52.504 59.546  70.837  1.00 22.19 ? 302  GLY A O     1 
ATOM   2083  N N     . LEU A  1 305  ? -53.460 59.748  72.874  1.00 23.33 ? 303  LEU A N     1 
ATOM   2084  C CA    . LEU A  1 305  ? -52.485 60.679  73.430  1.00 22.15 ? 303  LEU A CA    1 
ATOM   2085  C C     . LEU A  1 305  ? -52.152 60.195  74.838  1.00 21.62 ? 303  LEU A C     1 
ATOM   2086  O O     . LEU A  1 305  ? -52.979 60.295  75.749  1.00 21.68 ? 303  LEU A O     1 
ATOM   2087  C CB    . LEU A  1 305  ? -53.024 62.108  73.441  1.00 21.10 ? 303  LEU A CB    1 
ATOM   2088  C CG    . LEU A  1 305  ? -52.029 63.185  73.899  1.00 27.94 ? 303  LEU A CG    1 
ATOM   2089  C CD1   . LEU A  1 305  ? -52.247 64.500  73.153  1.00 25.10 ? 303  LEU A CD1   1 
ATOM   2090  C CD2   . LEU A  1 305  ? -52.170 63.443  75.389  1.00 28.49 ? 303  LEU A CD2   1 
ATOM   2091  N N     . ASN A  1 306  ? -50.943 59.672  75.014  1.00 22.16 ? 304  ASN A N     1 
ATOM   2092  C CA    . ASN A  1 306  ? -50.512 59.062  76.268  1.00 22.35 ? 304  ASN A CA    1 
ATOM   2093  C C     . ASN A  1 306  ? -49.599 60.007  77.039  1.00 23.20 ? 304  ASN A C     1 
ATOM   2094  O O     . ASN A  1 306  ? -48.656 60.566  76.463  1.00 22.63 ? 304  ASN A O     1 
ATOM   2095  C CB    . ASN A  1 306  ? -49.770 57.751  75.991  1.00 23.29 ? 304  ASN A CB    1 
ATOM   2096  C CG    . ASN A  1 306  ? -49.137 57.156  77.243  1.00 23.21 ? 304  ASN A CG    1 
ATOM   2097  O OD1   . ASN A  1 306  ? -47.923 57.295  77.475  1.00 27.94 ? 304  ASN A OD1   1 
ATOM   2098  N ND2   . ASN A  1 306  ? -49.945 56.505  78.056  1.00 23.72 ? 304  ASN A ND2   1 
ATOM   2099  N N     . ILE A  1 307  ? -49.849 60.151  78.343  1.00 22.28 ? 305  ILE A N     1 
ATOM   2100  C CA    . ILE A  1 307  ? -48.958 60.899  79.234  1.00 23.46 ? 305  ILE A CA    1 
ATOM   2101  C C     . ILE A  1 307  ? -47.984 59.932  79.906  1.00 22.72 ? 305  ILE A C     1 
ATOM   2102  O O     . ILE A  1 307  ? -48.384 59.135  80.762  1.00 20.76 ? 305  ILE A O     1 
ATOM   2103  C CB    . ILE A  1 307  ? -49.747 61.679  80.289  1.00 25.31 ? 305  ILE A CB    1 
ATOM   2104  C CG1   . ILE A  1 307  ? -50.734 62.626  79.614  1.00 24.62 ? 305  ILE A CG1   1 
ATOM   2105  C CG2   . ILE A  1 307  ? -48.785 62.424  81.228  1.00 26.12 ? 305  ILE A CG2   1 
ATOM   2106  C CD1   . ILE A  1 307  ? -51.628 63.317  80.592  1.00 24.31 ? 305  ILE A CD1   1 
ATOM   2107  N N     . ASP A  1 308  ? -46.692 60.039  79.556  1.00 22.44 ? 306  ASP A N     1 
ATOM   2108  C CA    . ASP A  1 308  ? -45.649 59.187  80.125  1.00 22.92 ? 306  ASP A CA    1 
ATOM   2109  C C     . ASP A  1 308  ? -45.430 59.521  81.598  1.00 22.42 ? 306  ASP A C     1 
ATOM   2110  O O     . ASP A  1 308  ? -45.681 60.641  82.045  1.00 21.38 ? 306  ASP A O     1 
ATOM   2111  C CB    . ASP A  1 308  ? -44.317 59.363  79.377  1.00 25.68 ? 306  ASP A CB    1 
ATOM   2112  C CG    . ASP A  1 308  ? -44.294 58.671  78.024  1.00 32.83 ? 306  ASP A CG    1 
ATOM   2113  O OD1   . ASP A  1 308  ? -45.220 57.889  77.724  1.00 32.55 ? 306  ASP A OD1   1 
ATOM   2114  O OD2   . ASP A  1 308  ? -43.341 58.913  77.250  1.00 35.94 ? 306  ASP A OD2   1 
ATOM   2115  N N     . ALA A  1 309  ? -44.977 58.531  82.358  1.00 21.98 ? 307  ALA A N     1 
ATOM   2116  C CA    . ALA A  1 309  ? -44.708 58.717  83.778  1.00 21.42 ? 307  ALA A CA    1 
ATOM   2117  C C     . ALA A  1 309  ? -43.223 59.005  83.978  1.00 25.18 ? 307  ALA A C     1 
ATOM   2118  O O     . ALA A  1 309  ? -42.380 58.430  83.290  1.00 21.60 ? 307  ALA A O     1 
ATOM   2119  C CB    . ALA A  1 309  ? -45.129 57.483  84.578  1.00 20.53 ? 307  ALA A CB    1 
ATOM   2120  N N     . GLU A  1 310  ? -42.906 59.905  84.916  1.00 20.59 ? 308  GLU A N     1 
ATOM   2121  C CA    . GLU A  1 310  ? -41.517 60.333  85.096  1.00 21.68 ? 308  GLU A CA    1 
ATOM   2122  C C     . GLU A  1 310  ? -41.081 60.091  86.538  1.00 21.25 ? 308  GLU A C     1 
ATOM   2123  O O     . GLU A  1 310  ? -41.334 59.010  87.075  1.00 21.84 ? 308  GLU A O     1 
ATOM   2124  C CB    . GLU A  1 310  ? -41.375 61.799  84.660  1.00 23.12 ? 308  GLU A CB    1 
ATOM   2125  C CG    . GLU A  1 310  ? -41.755 61.976  83.185  1.00 24.66 ? 308  GLU A CG    1 
ATOM   2126  C CD    . GLU A  1 310  ? -41.464 63.363  82.629  1.00 23.74 ? 308  GLU A CD    1 
ATOM   2127  O OE1   . GLU A  1 310  ? -40.277 63.682  82.387  1.00 26.45 ? 308  GLU A OE1   1 
ATOM   2128  O OE2   . GLU A  1 310  ? -42.433 64.119  82.410  1.00 23.38 ? 308  GLU A OE2   1 
ATOM   2129  N N     . GLU A  1 311  ? -40.431 61.060  87.173  1.00 21.90 ? 309  GLU A N     1 
ATOM   2130  C CA    . GLU A  1 311  ? -39.872 60.811  88.493  1.00 22.88 ? 309  GLU A CA    1 
ATOM   2131  C C     . GLU A  1 311  ? -40.980 60.701  89.532  1.00 21.25 ? 309  GLU A C     1 
ATOM   2132  O O     . GLU A  1 311  ? -42.111 61.160  89.338  1.00 21.37 ? 309  GLU A O     1 
ATOM   2133  C CB    . GLU A  1 311  ? -38.879 61.910  88.885  1.00 24.45 ? 309  GLU A CB    1 
ATOM   2134  C CG    . GLU A  1 311  ? -37.603 61.982  88.016  1.00 24.33 ? 309  GLU A CG    1 
ATOM   2135  C CD    . GLU A  1 311  ? -37.777 62.870  86.789  1.00 30.30 ? 309  GLU A CD    1 
ATOM   2136  O OE1   . GLU A  1 311  ? -38.924 63.156  86.398  1.00 27.46 ? 309  GLU A OE1   1 
ATOM   2137  O OE2   . GLU A  1 311  ? -36.763 63.284  86.205  1.00 32.15 ? 309  GLU A OE2   1 
ATOM   2138  N N     . ALA A  1 312  ? -40.648 60.053  90.653  1.00 22.04 ? 310  ALA A N     1 
ATOM   2139  C CA    . ALA A  1 312  ? -41.658 59.802  91.678  1.00 21.06 ? 310  ALA A CA    1 
ATOM   2140  C C     . ALA A  1 312  ? -42.264 61.092  92.218  1.00 22.87 ? 310  ALA A C     1 
ATOM   2141  O O     . ALA A  1 312  ? -43.451 61.112  92.576  1.00 23.67 ? 310  ALA A O     1 
ATOM   2142  C CB    . ALA A  1 312  ? -41.060 58.988  92.823  1.00 21.08 ? 310  ALA A CB    1 
ATOM   2143  N N     . ASP A  1 313  ? -41.482 62.173  92.303  1.00 21.88 ? 311  ASP A N     1 
ATOM   2144  C CA    . ASP A  1 313  ? -42.038 63.395  92.888  1.00 22.55 ? 311  ASP A CA    1 
ATOM   2145  C C     . ASP A  1 313  ? -42.909 64.178  91.905  1.00 23.18 ? 311  ASP A C     1 
ATOM   2146  O O     . ASP A  1 313  ? -43.370 65.271  92.249  1.00 22.00 ? 311  ASP A O     1 
ATOM   2147  C CB    . ASP A  1 313  ? -40.917 64.299  93.464  1.00 23.68 ? 311  ASP A CB    1 
ATOM   2148  C CG    . ASP A  1 313  ? -39.947 64.832  92.403  1.00 27.25 ? 311  ASP A CG    1 
ATOM   2149  O OD1   . ASP A  1 313  ? -40.185 64.635  91.201  1.00 27.01 ? 311  ASP A OD1   1 
ATOM   2150  O OD2   . ASP A  1 313  ? -38.923 65.462  92.788  1.00 30.74 ? 311  ASP A OD2   1 
ATOM   2151  N N     . ARG A  1 314  ? -43.134 63.646  90.702  1.00 22.68 ? 312  ARG A N     1 
ATOM   2152  C CA    . ARG A  1 314  ? -44.077 64.220  89.749  1.00 23.27 ? 312  ARG A CA    1 
ATOM   2153  C C     . ARG A  1 314  ? -45.360 63.406  89.591  1.00 22.80 ? 312  ARG A C     1 
ATOM   2154  O O     . ARG A  1 314  ? -46.285 63.875  88.921  1.00 23.10 ? 312  ARG A O     1 
ATOM   2155  C CB    . ARG A  1 314  ? -43.406 64.381  88.379  1.00 22.67 ? 312  ARG A CB    1 
ATOM   2156  C CG    . ARG A  1 314  ? -42.358 65.479  88.409  1.00 23.10 ? 312  ARG A CG    1 
ATOM   2157  C CD    . ARG A  1 314  ? -41.335 65.347  87.305  1.00 27.57 ? 312  ARG A CD    1 
ATOM   2158  N NE    . ARG A  1 314  ? -40.765 66.655  87.000  1.00 25.09 ? 312  ARG A NE    1 
ATOM   2159  C CZ    . ARG A  1 314  ? -39.780 66.869  86.138  1.00 25.29 ? 312  ARG A CZ    1 
ATOM   2160  N NH1   . ARG A  1 314  ? -39.162 65.869  85.527  1.00 22.55 ? 312  ARG A NH1   1 
ATOM   2161  N NH2   . ARG A  1 314  ? -39.415 68.119  85.873  1.00 24.71 ? 312  ARG A NH2   1 
ATOM   2162  N N     . LEU A  1 315  ? -45.455 62.224  90.204  1.00 23.14 ? 313  LEU A N     1 
ATOM   2163  C CA    . LEU A  1 315  ? -46.640 61.383  90.010  1.00 22.42 ? 313  LEU A CA    1 
ATOM   2164  C C     . LEU A  1 315  ? -47.925 62.102  90.415  1.00 24.13 ? 313  LEU A C     1 
ATOM   2165  O O     . LEU A  1 315  ? -48.874 62.189  89.627  1.00 22.81 ? 313  LEU A O     1 
ATOM   2166  C CB    . LEU A  1 315  ? -46.499 60.077  90.788  1.00 23.32 ? 313  LEU A CB    1 
ATOM   2167  C CG    . LEU A  1 315  ? -47.325 58.847  90.383  1.00 23.64 ? 313  LEU A CG    1 
ATOM   2168  C CD1   . LEU A  1 315  ? -46.891 57.661  91.255  1.00 23.54 ? 313  LEU A CD1   1 
ATOM   2169  C CD2   . LEU A  1 315  ? -48.829 59.028  90.480  1.00 26.51 ? 313  LEU A CD2   1 
ATOM   2170  N N     . GLU A  1 316  ? -47.998 62.591  91.652  1.00 23.04 ? 314  GLU A N     1 
ATOM   2171  C CA    . GLU A  1 316  ? -49.290 63.098  92.111  1.00 26.14 ? 314  GLU A CA    1 
ATOM   2172  C C     . GLU A  1 316  ? -49.635 64.421  91.439  1.00 25.58 ? 314  GLU A C     1 
ATOM   2173  O O     . GLU A  1 316  ? -50.816 64.688  91.178  1.00 25.04 ? 314  GLU A O     1 
ATOM   2174  C CB    . GLU A  1 316  ? -49.318 63.199  93.649  1.00 25.53 ? 314  GLU A CB    1 
ATOM   2175  C CG    . GLU A  1 316  ? -49.223 61.825  94.278  1.00 24.44 ? 314  GLU A CG    1 
ATOM   2176  C CD    . GLU A  1 316  ? -49.238 61.830  95.784  1.00 26.77 ? 314  GLU A CD    1 
ATOM   2177  O OE1   . GLU A  1 316  ? -49.970 62.651  96.378  1.00 29.74 ? 314  GLU A OE1   1 
ATOM   2178  O OE2   . GLU A  1 316  ? -48.527 60.984  96.370  1.00 27.99 ? 314  GLU A OE2   1 
ATOM   2179  N N     . LEU A  1 317  ? -48.628 65.232  91.101  1.00 24.83 ? 315  LEU A N     1 
ATOM   2180  C CA    . LEU A  1 317  ? -48.890 66.443  90.321  1.00 25.84 ? 315  LEU A CA    1 
ATOM   2181  C C     . LEU A  1 317  ? -49.519 66.102  88.973  1.00 25.99 ? 315  LEU A C     1 
ATOM   2182  O O     . LEU A  1 317  ? -50.437 66.795  88.514  1.00 23.81 ? 315  LEU A O     1 
ATOM   2183  C CB    . LEU A  1 317  ? -47.591 67.235  90.121  1.00 24.76 ? 315  LEU A CB    1 
ATOM   2184  C CG    . LEU A  1 317  ? -47.730 68.550  89.338  1.00 26.49 ? 315  LEU A CG    1 
ATOM   2185  C CD1   . LEU A  1 317  ? -48.840 69.436  89.909  1.00 25.70 ? 315  LEU A CD1   1 
ATOM   2186  C CD2   . LEU A  1 317  ? -46.419 69.319  89.337  1.00 29.55 ? 315  LEU A CD2   1 
ATOM   2187  N N     . SER A  1 318  ? -49.012 65.053  88.310  1.00 25.13 ? 316  SER A N     1 
ATOM   2188  C CA    . SER A  1 318  ? -49.570 64.660  87.018  1.00 23.63 ? 316  SER A CA    1 
ATOM   2189  C C     . SER A  1 318  ? -51.017 64.206  87.154  1.00 25.36 ? 316  SER A C     1 
ATOM   2190  O O     . SER A  1 318  ? -51.792 64.321  86.204  1.00 23.04 ? 316  SER A O     1 
ATOM   2191  C CB    . SER A  1 318  ? -48.727 63.551  86.383  1.00 21.22 ? 316  SER A CB    1 
ATOM   2192  O OG    . SER A  1 318  ? -48.888 62.303  87.042  1.00 25.28 ? 316  SER A OG    1 
ATOM   2193  N N     . LEU A  1 319  ? -51.396 63.684  88.319  1.00 20.93 ? 317  LEU A N     1 
ATOM   2194  C CA    . LEU A  1 319  ? -52.799 63.327  88.540  1.00 20.88 ? 317  LEU A CA    1 
ATOM   2195  C C     . LEU A  1 319  ? -53.690 64.552  88.513  1.00 21.55 ? 317  LEU A C     1 
ATOM   2196  O O     . LEU A  1 319  ? -54.850 64.474  88.086  1.00 23.61 ? 317  LEU A O     1 
ATOM   2197  C CB    . LEU A  1 319  ? -52.958 62.604  89.877  1.00 21.51 ? 317  LEU A CB    1 
ATOM   2198  C CG    . LEU A  1 319  ? -52.238 61.260  89.939  1.00 27.58 ? 317  LEU A CG    1 
ATOM   2199  C CD1   . LEU A  1 319  ? -52.407 60.668  91.337  1.00 24.27 ? 317  LEU A CD1   1 
ATOM   2200  C CD2   . LEU A  1 319  ? -52.831 60.340  88.871  1.00 23.71 ? 317  LEU A CD2   1 
ATOM   2201  N N     . ASP A  1 320  ? -53.174 65.694  88.962  1.00 27.77 ? 318  ASP A N     1 
ATOM   2202  C CA    . ASP A  1 320  ? -53.993 66.896  88.949  1.00 27.60 ? 318  ASP A CA    1 
ATOM   2203  C C     . ASP A  1 320  ? -54.281 67.361  87.535  1.00 26.32 ? 318  ASP A C     1 
ATOM   2204  O O     . ASP A  1 320  ? -55.378 67.872  87.274  1.00 27.52 ? 318  ASP A O     1 
ATOM   2205  C CB    . ASP A  1 320  ? -53.329 68.001  89.760  1.00 26.06 ? 318  ASP A CB    1 
ATOM   2206  C CG    . ASP A  1 320  ? -53.590 67.847  91.247  1.00 31.25 ? 318  ASP A CG    1 
ATOM   2207  O OD1   . ASP A  1 320  ? -54.778 67.712  91.633  1.00 31.74 ? 318  ASP A OD1   1 
ATOM   2208  O OD2   . ASP A  1 320  ? -52.614 67.833  92.029  1.00 34.12 ? 318  ASP A OD2   1 
ATOM   2209  N N     . LEU A  1 321  ? -53.326 67.188  86.611  1.00 23.90 ? 319  LEU A N     1 
ATOM   2210  C CA    . LEU A  1 321  ? -53.596 67.499  85.210  1.00 25.00 ? 319  LEU A CA    1 
ATOM   2211  C C     . LEU A  1 321  ? -54.536 66.472  84.591  1.00 24.59 ? 319  LEU A C     1 
ATOM   2212  O O     . LEU A  1 321  ? -55.443 66.840  83.836  1.00 21.68 ? 319  LEU A O     1 
ATOM   2213  C CB    . LEU A  1 321  ? -52.296 67.571  84.405  1.00 22.03 ? 319  LEU A CB    1 
ATOM   2214  C CG    . LEU A  1 321  ? -51.346 68.722  84.762  1.00 25.44 ? 319  LEU A CG    1 
ATOM   2215  C CD1   . LEU A  1 321  ? -49.902 68.280  84.676  1.00 30.61 ? 319  LEU A CD1   1 
ATOM   2216  C CD2   . LEU A  1 321  ? -51.579 69.866  83.824  1.00 31.65 ? 319  LEU A CD2   1 
ATOM   2217  N N     . LEU A  1 322  ? -54.318 65.181  84.873  1.00 24.55 ? 320  LEU A N     1 
ATOM   2218  C CA    . LEU A  1 322  ? -55.198 64.140  84.331  1.00 24.24 ? 320  LEU A CA    1 
ATOM   2219  C C     . LEU A  1 322  ? -56.641 64.371  84.746  1.00 24.65 ? 320  LEU A C     1 
ATOM   2220  O O     . LEU A  1 322  ? -57.565 64.133  83.964  1.00 25.25 ? 320  LEU A O     1 
ATOM   2221  C CB    . LEU A  1 322  ? -54.751 62.753  84.800  1.00 22.98 ? 320  LEU A CB    1 
ATOM   2222  C CG    . LEU A  1 322  ? -55.629 61.606  84.294  1.00 20.60 ? 320  LEU A CG    1 
ATOM   2223  C CD1   . LEU A  1 322  ? -55.404 61.401  82.781  1.00 23.79 ? 320  LEU A CD1   1 
ATOM   2224  C CD2   . LEU A  1 322  ? -55.381 60.312  85.065  1.00 23.16 ? 320  LEU A CD2   1 
ATOM   2225  N N     . GLU A  1 323  ? -56.853 64.809  85.984  1.00 23.19 ? 321  GLU A N     1 
ATOM   2226  C CA    . GLU A  1 323  ? -58.210 65.044  86.470  1.00 27.93 ? 321  GLU A CA    1 
ATOM   2227  C C     . GLU A  1 323  ? -58.873 66.188  85.712  1.00 27.22 ? 321  GLU A C     1 
ATOM   2228  O O     . GLU A  1 323  ? -60.012 66.057  85.244  1.00 27.57 ? 321  GLU A O     1 
ATOM   2229  C CB    . GLU A  1 323  ? -58.180 65.324  87.976  1.00 29.39 ? 321  GLU A CB    1 
ATOM   2230  C CG    . GLU A  1 323  ? -59.484 65.903  88.537  1.00 32.56 ? 321  GLU A CG    1 
ATOM   2231  C CD    . GLU A  1 323  ? -60.237 64.961  89.458  1.00 35.41 ? 321  GLU A CD    1 
ATOM   2232  O OE1   . GLU A  1 323  ? -59.627 64.041  90.006  1.00 37.03 ? 321  GLU A OE1   1 
ATOM   2233  O OE2   . GLU A  1 323  ? -61.459 65.148  89.638  1.00 38.76 ? 321  GLU A OE2   1 
ATOM   2234  N N     . VAL A  1 324  ? -58.177 67.320  85.569  1.00 24.56 ? 322  VAL A N     1 
ATOM   2235  C CA    . VAL A  1 324  ? -58.801 68.458  84.910  1.00 21.85 ? 322  VAL A CA    1 
ATOM   2236  C C     . VAL A  1 324  ? -59.125 68.112  83.466  1.00 24.20 ? 322  VAL A C     1 
ATOM   2237  O O     . VAL A  1 324  ? -60.223 68.404  82.978  1.00 28.19 ? 322  VAL A O     1 
ATOM   2238  C CB    . VAL A  1 324  ? -57.911 69.710  85.006  1.00 29.87 ? 322  VAL A CB    1 
ATOM   2239  C CG1   . VAL A  1 324  ? -58.533 70.839  84.200  1.00 30.12 ? 322  VAL A CG1   1 
ATOM   2240  C CG2   . VAL A  1 324  ? -57.751 70.129  86.448  1.00 29.08 ? 322  VAL A CG2   1 
ATOM   2241  N N     . LEU A  1 325  ? -58.193 67.456  82.772  1.00 20.90 ? 323  LEU A N     1 
ATOM   2242  C CA    . LEU A  1 325  ? -58.416 67.110  81.366  1.00 25.06 ? 323  LEU A CA    1 
ATOM   2243  C C     . LEU A  1 325  ? -59.585 66.146  81.201  1.00 24.85 ? 323  LEU A C     1 
ATOM   2244  O O     . LEU A  1 325  ? -60.419 66.314  80.299  1.00 23.17 ? 323  LEU A O     1 
ATOM   2245  C CB    . LEU A  1 325  ? -57.153 66.492  80.768  1.00 21.65 ? 323  LEU A CB    1 
ATOM   2246  C CG    . LEU A  1 325  ? -55.932 67.395  80.652  1.00 25.68 ? 323  LEU A CG    1 
ATOM   2247  C CD1   . LEU A  1 325  ? -54.723 66.522  80.399  1.00 24.28 ? 323  LEU A CD1   1 
ATOM   2248  C CD2   . LEU A  1 325  ? -56.132 68.387  79.526  1.00 22.80 ? 323  LEU A CD2   1 
ATOM   2249  N N     . CYS A  1 326  ? -59.666 65.125  82.059  1.00 26.81 ? 324  CYS A N     1 
ATOM   2250  C CA    . CYS A  1 326  ? -60.759 64.162  81.927  1.00 24.37 ? 324  CYS A CA    1 
ATOM   2251  C C     . CYS A  1 326  ? -62.112 64.762  82.279  1.00 26.28 ? 324  CYS A C     1 
ATOM   2252  O O     . CYS A  1 326  ? -63.147 64.249  81.824  1.00 23.48 ? 324  CYS A O     1 
ATOM   2253  C CB    . CYS A  1 326  ? -60.481 62.934  82.794  1.00 25.39 ? 324  CYS A CB    1 
ATOM   2254  S SG    . CYS A  1 326  ? -59.139 61.909  82.112  1.00 30.83 ? 324  CYS A SG    1 
ATOM   2255  N N     . LEU A  1 327  ? -62.131 65.827  83.069  1.00 24.85 ? 325  LEU A N     1 
ATOM   2256  C CA    . LEU A  1 327  ? -63.367 66.497  83.425  1.00 25.48 ? 325  LEU A CA    1 
ATOM   2257  C C     . LEU A  1 327  ? -63.716 67.630  82.474  1.00 26.67 ? 325  LEU A C     1 
ATOM   2258  O O     . LEU A  1 327  ? -64.805 68.197  82.588  1.00 27.39 ? 325  LEU A O     1 
ATOM   2259  C CB    . LEU A  1 327  ? -63.280 67.018  84.865  1.00 28.67 ? 325  LEU A CB    1 
ATOM   2260  C CG    . LEU A  1 327  ? -63.149 65.905  85.922  1.00 30.53 ? 325  LEU A CG    1 
ATOM   2261  C CD1   . LEU A  1 327  ? -63.009 66.480  87.333  1.00 31.49 ? 325  LEU A CD1   1 
ATOM   2262  C CD2   . LEU A  1 327  ? -64.317 64.936  85.847  1.00 31.61 ? 325  LEU A CD2   1 
ATOM   2263  N N     . ASP A  1 328  ? -62.848 67.938  81.510  1.00 24.31 ? 326  ASP A N     1 
ATOM   2264  C CA    . ASP A  1 328  ? -63.049 69.094  80.637  1.00 26.37 ? 326  ASP A CA    1 
ATOM   2265  C C     . ASP A  1 328  ? -63.990 68.727  79.496  1.00 26.26 ? 326  ASP A C     1 
ATOM   2266  O O     . ASP A  1 328  ? -63.644 67.900  78.644  1.00 25.58 ? 326  ASP A O     1 
ATOM   2267  C CB    . ASP A  1 328  ? -61.705 69.578  80.089  1.00 25.86 ? 326  ASP A CB    1 
ATOM   2268  C CG    . ASP A  1 328  ? -61.826 70.887  79.320  1.00 29.71 ? 326  ASP A CG    1 
ATOM   2269  O OD1   . ASP A  1 328  ? -62.850 71.105  78.627  1.00 28.77 ? 326  ASP A OD1   1 
ATOM   2270  O OD2   . ASP A  1 328  ? -60.901 71.716  79.420  1.00 30.12 ? 326  ASP A OD2   1 
ATOM   2271  N N     . GLY A  1 329  ? -65.159 69.372  79.458  1.00 25.04 ? 327  GLY A N     1 
ATOM   2272  C CA    . GLY A  1 329  ? -66.158 69.031  78.453  1.00 24.03 ? 327  GLY A CA    1 
ATOM   2273  C C     . GLY A  1 329  ? -65.672 69.172  77.020  1.00 27.87 ? 327  GLY A C     1 
ATOM   2274  O O     . GLY A  1 329  ? -66.149 68.462  76.133  1.00 25.07 ? 327  GLY A O     1 
ATOM   2275  N N     . ASP A  1 330  ? -64.710 70.069  76.773  1.00 25.13 ? 328  ASP A N     1 
ATOM   2276  C CA    . ASP A  1 330  ? -64.195 70.266  75.420  1.00 29.24 ? 328  ASP A CA    1 
ATOM   2277  C C     . ASP A  1 330  ? -63.538 69.017  74.851  1.00 23.69 ? 328  ASP A C     1 
ATOM   2278  O O     . ASP A  1 330  ? -63.425 68.897  73.629  1.00 25.51 ? 328  ASP A O     1 
ATOM   2279  C CB    . ASP A  1 330  ? -63.171 71.405  75.384  1.00 28.07 ? 328  ASP A CB    1 
ATOM   2280  C CG    . ASP A  1 330  ? -63.790 72.750  75.670  1.00 30.62 ? 328  ASP A CG    1 
ATOM   2281  O OD1   . ASP A  1 330  ? -65.021 72.873  75.521  1.00 33.48 ? 328  ASP A OD1   1 
ATOM   2282  O OD2   . ASP A  1 330  ? -63.044 73.683  76.043  1.00 27.56 ? 328  ASP A OD2   1 
ATOM   2283  N N     . LEU A  1 331  ? -63.083 68.102  75.698  1.00 22.86 ? 329  LEU A N     1 
ATOM   2284  C CA    . LEU A  1 331  ? -62.467 66.861  75.242  1.00 22.87 ? 329  LEU A CA    1 
ATOM   2285  C C     . LEU A  1 331  ? -63.430 65.678  75.257  1.00 25.03 ? 329  LEU A C     1 
ATOM   2286  O O     . LEU A  1 331  ? -63.001 64.543  75.008  1.00 24.60 ? 329  LEU A O     1 
ATOM   2287  C CB    . LEU A  1 331  ? -61.241 66.531  76.095  1.00 22.37 ? 329  LEU A CB    1 
ATOM   2288  C CG    . LEU A  1 331  ? -60.073 67.511  76.041  1.00 21.71 ? 329  LEU A CG    1 
ATOM   2289  C CD1   . LEU A  1 331  ? -59.014 67.146  77.081  1.00 21.20 ? 329  LEU A CD1   1 
ATOM   2290  C CD2   . LEU A  1 331  ? -59.458 67.501  74.658  1.00 23.33 ? 329  LEU A CD2   1 
ATOM   2291  N N     . SER A  1 332  ? -64.714 65.909  75.529  1.00 27.63 ? 330  SER A N     1 
ATOM   2292  C CA    . SER A  1 332  ? -65.647 64.795  75.620  1.00 28.87 ? 330  SER A CA    1 
ATOM   2293  C C     . SER A  1 332  ? -65.864 64.166  74.247  1.00 25.19 ? 330  SER A C     1 
ATOM   2294  O O     . SER A  1 332  ? -65.646 64.788  73.200  1.00 23.99 ? 330  SER A O     1 
ATOM   2295  C CB    . SER A  1 332  ? -66.986 65.239  76.218  1.00 26.62 ? 330  SER A CB    1 
ATOM   2296  O OG    . SER A  1 332  ? -67.622 66.223  75.434  1.00 27.82 ? 330  SER A OG    1 
ATOM   2297  N N     . GLY A  1 333  ? -66.270 62.899  74.265  1.00 24.40 ? 331  GLY A N     1 
ATOM   2298  C CA    . GLY A  1 333  ? -66.456 62.135  73.048  1.00 28.88 ? 331  GLY A CA    1 
ATOM   2299  C C     . GLY A  1 333  ? -65.219 61.413  72.548  1.00 25.67 ? 331  GLY A C     1 
ATOM   2300  O O     . GLY A  1 333  ? -65.306 60.666  71.564  1.00 27.38 ? 331  GLY A O     1 
ATOM   2301  N N     . TRP A  1 334  ? -64.075 61.608  73.185  1.00 24.73 ? 332  TRP A N     1 
ATOM   2302  C CA    . TRP A  1 334  ? -62.822 60.994  72.777  1.00 24.68 ? 332  TRP A CA    1 
ATOM   2303  C C     . TRP A  1 334  ? -62.260 60.192  73.941  1.00 25.03 ? 332  TRP A C     1 
ATOM   2304  O O     . TRP A  1 334  ? -62.166 60.700  75.066  1.00 24.04 ? 332  TRP A O     1 
ATOM   2305  C CB    . TRP A  1 334  ? -61.853 62.091  72.322  1.00 23.94 ? 332  TRP A CB    1 
ATOM   2306  C CG    . TRP A  1 334  ? -60.416 61.732  72.199  1.00 22.56 ? 332  TRP A CG    1 
ATOM   2307  C CD1   . TRP A  1 334  ? -59.842 60.963  71.233  1.00 23.65 ? 332  TRP A CD1   1 
ATOM   2308  C CD2   . TRP A  1 334  ? -59.350 62.220  73.012  1.00 20.40 ? 332  TRP A CD2   1 
ATOM   2309  N NE1   . TRP A  1 334  ? -58.487 60.912  71.409  1.00 23.18 ? 332  TRP A NE1   1 
ATOM   2310  C CE2   . TRP A  1 334  ? -58.152 61.685  72.494  1.00 22.02 ? 332  TRP A CE2   1 
ATOM   2311  C CE3   . TRP A  1 334  ? -59.289 63.058  74.132  1.00 24.49 ? 332  TRP A CE3   1 
ATOM   2312  C CZ2   . TRP A  1 334  ? -56.908 61.937  73.066  1.00 23.65 ? 332  TRP A CZ2   1 
ATOM   2313  C CZ3   . TRP A  1 334  ? -58.045 63.319  74.701  1.00 25.45 ? 332  TRP A CZ3   1 
ATOM   2314  C CH2   . TRP A  1 334  ? -56.865 62.749  74.166  1.00 22.73 ? 332  TRP A CH2   1 
ATOM   2315  N N     . ASN A  1 335  ? -61.919 58.928  73.679  1.00 22.08 ? 333  ASN A N     1 
ATOM   2316  C CA    . ASN A  1 335  ? -61.400 58.028  74.698  1.00 21.90 ? 333  ASN A CA    1 
ATOM   2317  C C     . ASN A  1 335  ? -59.902 57.790  74.537  1.00 22.68 ? 333  ASN A C     1 
ATOM   2318  O O     . ASN A  1 335  ? -59.364 56.833  75.106  1.00 22.71 ? 333  ASN A O     1 
ATOM   2319  C CB    . ASN A  1 335  ? -62.147 56.688  74.664  1.00 23.81 ? 333  ASN A CB    1 
ATOM   2320  C CG    . ASN A  1 335  ? -63.530 56.754  75.325  1.00 26.67 ? 333  ASN A CG    1 
ATOM   2321  O OD1   . ASN A  1 335  ? -63.752 57.503  76.274  1.00 25.02 ? 333  ASN A OD1   1 
ATOM   2322  N ND2   . ASN A  1 335  ? -64.450 55.936  74.835  1.00 24.13 ? 333  ASN A ND2   1 
ATOM   2323  N N     . GLY A  1 336  ? -59.222 58.643  73.769  1.00 25.10 ? 334  GLY A N     1 
ATOM   2324  C CA    . GLY A  1 336  ? -57.819 58.452  73.451  1.00 22.65 ? 334  GLY A CA    1 
ATOM   2325  C C     . GLY A  1 336  ? -56.833 58.859  74.529  1.00 23.78 ? 334  GLY A C     1 
ATOM   2326  O O     . GLY A  1 336  ? -55.649 58.529  74.411  1.00 22.56 ? 334  GLY A O     1 
ATOM   2327  N N     . MET A  1 337  ? -57.279 59.554  75.573  1.00 24.75 ? 335  MET A N     1 
ATOM   2328  C CA    A MET A  1 337  ? -56.368 59.993  76.623  0.47 23.76 ? 335  MET A CA    1 
ATOM   2329  C CA    B MET A  1 337  ? -56.358 59.988  76.613  0.53 23.76 ? 335  MET A CA    1 
ATOM   2330  C C     . MET A  1 337  ? -55.813 58.794  77.381  1.00 20.80 ? 335  MET A C     1 
ATOM   2331  O O     . MET A  1 337  ? -56.572 57.933  77.839  1.00 22.66 ? 335  MET A O     1 
ATOM   2332  C CB    A MET A  1 337  ? -57.081 60.939  77.587  0.47 23.81 ? 335  MET A CB    1 
ATOM   2333  C CB    B MET A  1 337  ? -57.040 60.949  77.577  0.53 23.82 ? 335  MET A CB    1 
ATOM   2334  C CG    A MET A  1 337  ? -56.174 61.486  78.670  0.47 24.61 ? 335  MET A CG    1 
ATOM   2335  C CG    B MET A  1 337  ? -56.153 61.281  78.752  0.53 24.60 ? 335  MET A CG    1 
ATOM   2336  S SD    A MET A  1 337  ? -54.909 62.579  78.015  0.47 27.40 ? 335  MET A SD    1 
ATOM   2337  S SD    B MET A  1 337  ? -56.253 63.018  79.160  0.53 26.42 ? 335  MET A SD    1 
ATOM   2338  C CE    A MET A  1 337  ? -55.887 63.990  77.512  0.47 25.65 ? 335  MET A CE    1 
ATOM   2339  C CE    B MET A  1 337  ? -55.303 63.706  77.796  0.53 25.29 ? 335  MET A CE    1 
ATOM   2340  N N     . GLY A  1 338  ? -54.487 58.750  77.528  1.00 21.59 ? 336  GLY A N     1 
ATOM   2341  C CA    . GLY A  1 338  ? -53.831 57.662  78.220  1.00 21.66 ? 336  GLY A CA    1 
ATOM   2342  C C     . GLY A  1 338  ? -52.875 58.190  79.272  1.00 21.57 ? 336  GLY A C     1 
ATOM   2343  O O     . GLY A  1 338  ? -52.490 59.355  79.267  1.00 20.96 ? 336  GLY A O     1 
ATOM   2344  N N     . PHE A  1 339  ? -52.522 57.304  80.196  1.00 18.86 ? 337  PHE A N     1 
ATOM   2345  C CA    . PHE A  1 339  ? -51.751 57.642  81.380  1.00 25.25 ? 337  PHE A CA    1 
ATOM   2346  C C     . PHE A  1 339  ? -50.960 56.413  81.809  1.00 22.04 ? 337  PHE A C     1 
ATOM   2347  O O     . PHE A  1 339  ? -51.508 55.309  81.877  1.00 21.87 ? 337  PHE A O     1 
ATOM   2348  C CB    . PHE A  1 339  ? -52.690 58.109  82.496  1.00 24.66 ? 337  PHE A CB    1 
ATOM   2349  C CG    . PHE A  1 339  ? -51.998 58.785  83.649  1.00 23.22 ? 337  PHE A CG    1 
ATOM   2350  C CD1   . PHE A  1 339  ? -51.698 60.148  83.596  1.00 25.78 ? 337  PHE A CD1   1 
ATOM   2351  C CD2   . PHE A  1 339  ? -51.681 58.068  84.793  1.00 21.03 ? 337  PHE A CD2   1 
ATOM   2352  C CE1   . PHE A  1 339  ? -51.067 60.777  84.676  1.00 22.98 ? 337  PHE A CE1   1 
ATOM   2353  C CE2   . PHE A  1 339  ? -51.061 58.690  85.874  1.00 23.62 ? 337  PHE A CE2   1 
ATOM   2354  C CZ    . PHE A  1 339  ? -50.759 60.049  85.806  1.00 21.70 ? 337  PHE A CZ    1 
ATOM   2355  N N     . VAL A  1 340  ? -49.679 56.607  82.086  1.00 22.08 ? 338  VAL A N     1 
ATOM   2356  C CA    . VAL A  1 340  ? -48.780 55.540  82.509  1.00 23.18 ? 338  VAL A CA    1 
ATOM   2357  C C     . VAL A  1 340  ? -48.751 55.474  84.030  1.00 21.16 ? 338  VAL A C     1 
ATOM   2358  O O     . VAL A  1 340  ? -48.703 56.505  84.719  1.00 23.04 ? 338  VAL A O     1 
ATOM   2359  C CB    . VAL A  1 340  ? -47.366 55.775  81.943  1.00 22.58 ? 338  VAL A CB    1 
ATOM   2360  C CG1   . VAL A  1 340  ? -46.407 54.696  82.419  1.00 23.65 ? 338  VAL A CG1   1 
ATOM   2361  C CG2   . VAL A  1 340  ? -47.402 55.828  80.422  1.00 21.22 ? 338  VAL A CG2   1 
ATOM   2362  N N     . VAL A  1 341  ? -48.751 54.258  84.558  1.00 22.83 ? 339  VAL A N     1 
ATOM   2363  C CA    . VAL A  1 341  ? -48.518 54.016  85.980  1.00 19.61 ? 339  VAL A CA    1 
ATOM   2364  C C     . VAL A  1 341  ? -47.378 53.011  86.122  1.00 22.60 ? 339  VAL A C     1 
ATOM   2365  O O     . VAL A  1 341  ? -47.316 52.018  85.391  1.00 24.32 ? 339  VAL A O     1 
ATOM   2366  C CB    . VAL A  1 341  ? -49.807 53.521  86.673  1.00 26.34 ? 339  VAL A CB    1 
ATOM   2367  C CG1   . VAL A  1 341  ? -50.943 54.507  86.434  1.00 25.99 ? 339  VAL A CG1   1 
ATOM   2368  C CG2   . VAL A  1 341  ? -50.220 52.186  86.126  1.00 29.30 ? 339  VAL A CG2   1 
ATOM   2369  N N     . GLN A  1 342  ? -46.464 53.275  87.058  1.00 23.88 ? 340  GLN A N     1 
ATOM   2370  C CA    . GLN A  1 342  ? -45.236 52.497  87.210  1.00 21.75 ? 340  GLN A CA    1 
ATOM   2371  C C     . GLN A  1 342  ? -45.393 51.487  88.340  1.00 24.82 ? 340  GLN A C     1 
ATOM   2372  O O     . GLN A  1 342  ? -45.532 51.875  89.499  1.00 23.21 ? 340  GLN A O     1 
ATOM   2373  C CB    . GLN A  1 342  ? -44.051 53.422  87.494  1.00 19.43 ? 340  GLN A CB    1 
ATOM   2374  C CG    . GLN A  1 342  ? -43.832 54.490  86.427  1.00 20.42 ? 340  GLN A CG    1 
ATOM   2375  C CD    . GLN A  1 342  ? -43.274 55.810  86.968  1.00 22.48 ? 340  GLN A CD    1 
ATOM   2376  O OE1   . GLN A  1 342  ? -43.790 56.391  87.925  1.00 21.12 ? 340  GLN A OE1   1 
ATOM   2377  N NE2   . GLN A  1 342  ? -42.230 56.304  86.318  1.00 22.89 ? 340  GLN A NE2   1 
ATOM   2378  N N     . ALA A  1 343  ? -45.348 50.192  88.001  1.00 24.41 ? 341  ALA A N     1 
ATOM   2379  C CA    . ALA A  1 343  ? -45.532 49.152  89.006  1.00 24.77 ? 341  ALA A CA    1 
ATOM   2380  C C     . ALA A  1 343  ? -44.380 49.084  90.004  1.00 25.35 ? 341  ALA A C     1 
ATOM   2381  O O     . ALA A  1 343  ? -44.531 48.466  91.070  1.00 25.70 ? 341  ALA A O     1 
ATOM   2382  C CB    . ALA A  1 343  ? -45.694 47.791  88.331  1.00 23.68 ? 341  ALA A CB    1 
ATOM   2383  N N     . TYR A  1 344  ? -43.230 49.678  89.699  1.00 23.41 ? 342  TYR A N     1 
ATOM   2384  C CA    . TYR A  1 344  ? -42.185 49.645  90.714  1.00 25.51 ? 342  TYR A CA    1 
ATOM   2385  C C     . TYR A  1 344  ? -42.452 50.626  91.837  1.00 25.28 ? 342  TYR A C     1 
ATOM   2386  O O     . TYR A  1 344  ? -41.707 50.633  92.822  1.00 25.97 ? 342  TYR A O     1 
ATOM   2387  C CB    . TYR A  1 344  ? -40.783 49.875  90.104  1.00 25.63 ? 342  TYR A CB    1 
ATOM   2388  C CG    . TYR A  1 344  ? -40.346 51.257  89.593  1.00 23.21 ? 342  TYR A CG    1 
ATOM   2389  C CD1   . TYR A  1 344  ? -41.209 52.343  89.523  1.00 21.32 ? 342  TYR A CD1   1 
ATOM   2390  C CD2   . TYR A  1 344  ? -39.021 51.446  89.161  1.00 23.51 ? 342  TYR A CD2   1 
ATOM   2391  C CE1   . TYR A  1 344  ? -40.762 53.589  89.024  1.00 24.59 ? 342  TYR A CE1   1 
ATOM   2392  C CE2   . TYR A  1 344  ? -38.575 52.670  88.673  1.00 24.00 ? 342  TYR A CE2   1 
ATOM   2393  C CZ    . TYR A  1 344  ? -39.448 53.732  88.605  1.00 22.33 ? 342  TYR A CZ    1 
ATOM   2394  O OH    . TYR A  1 344  ? -39.000 54.940  88.138  1.00 23.58 ? 342  TYR A OH    1 
ATOM   2395  N N     . GLY A  1 345  ? -43.508 51.426  91.723  1.00 23.66 ? 343  GLY A N     1 
ATOM   2396  C CA    . GLY A  1 345  ? -43.836 52.397  92.739  1.00 23.76 ? 343  GLY A CA    1 
ATOM   2397  C C     . GLY A  1 345  ? -44.819 51.839  93.754  1.00 26.35 ? 343  GLY A C     1 
ATOM   2398  O O     . GLY A  1 345  ? -45.749 51.110  93.413  1.00 24.30 ? 343  GLY A O     1 
ATOM   2399  N N     . LYS A  1 346  ? -44.583 52.195  95.013  1.00 22.88 ? 344  LYS A N     1 
ATOM   2400  C CA    . LYS A  1 346  ? -45.405 51.729  96.119  1.00 25.99 ? 344  LYS A CA    1 
ATOM   2401  C C     . LYS A  1 346  ? -46.843 52.217  96.022  1.00 26.95 ? 344  LYS A C     1 
ATOM   2402  O O     . LYS A  1 346  ? -47.739 51.574  96.579  1.00 27.89 ? 344  LYS A O     1 
ATOM   2403  C CB    . LYS A  1 346  ? -44.766 52.191  97.420  1.00 24.39 ? 344  LYS A CB    1 
ATOM   2404  C CG    . LYS A  1 346  ? -43.442 51.463  97.716  1.00 28.36 ? 344  LYS A CG    1 
ATOM   2405  C CD    . LYS A  1 346  ? -42.638 52.171  98.785  1.00 27.39 ? 344  LYS A CD    1 
ATOM   2406  C CE    . LYS A  1 346  ? -41.547 51.255  99.337  1.00 29.96 ? 344  LYS A CE    1 
ATOM   2407  N NZ    . LYS A  1 346  ? -40.739 51.924  100.411 1.00 30.80 ? 344  LYS A NZ    1 
ATOM   2408  N N     . ARG A  1 347  ? -47.083 53.330  95.322  1.00 25.16 ? 345  ARG A N     1 
ATOM   2409  C CA    . ARG A  1 347  ? -48.419 53.923  95.220  1.00 25.71 ? 345  ARG A CA    1 
ATOM   2410  C C     . ARG A  1 347  ? -49.249 53.364  94.071  1.00 25.26 ? 345  ARG A C     1 
ATOM   2411  O O     . ARG A  1 347  ? -50.441 53.698  93.969  1.00 26.55 ? 345  ARG A O     1 
ATOM   2412  C CB    . ARG A  1 347  ? -48.302 55.451  95.067  1.00 24.39 ? 345  ARG A CB    1 
ATOM   2413  C CG    . ARG A  1 347  ? -47.783 56.132  96.336  1.00 22.00 ? 345  ARG A CG    1 
ATOM   2414  C CD    . ARG A  1 347  ? -47.359 57.582  96.084  1.00 24.29 ? 345  ARG A CD    1 
ATOM   2415  N NE    . ARG A  1 347  ? -46.178 57.652  95.233  1.00 25.56 ? 345  ARG A NE    1 
ATOM   2416  C CZ    . ARG A  1 347  ? -45.709 58.772  94.695  1.00 24.04 ? 345  ARG A CZ    1 
ATOM   2417  N NH1   . ARG A  1 347  ? -46.295 59.941  94.909  1.00 22.84 ? 345  ARG A NH1   1 
ATOM   2418  N NH2   . ARG A  1 347  ? -44.624 58.717  93.930  1.00 25.18 ? 345  ARG A NH2   1 
ATOM   2419  N N     . CYS A  1 348  ? -48.659 52.513  93.233  1.00 24.69 ? 346  CYS A N     1 
ATOM   2420  C CA    . CYS A  1 348  ? -49.294 52.058  91.996  1.00 24.22 ? 346  CYS A CA    1 
ATOM   2421  C C     . CYS A  1 348  ? -50.729 51.553  92.157  1.00 27.52 ? 346  CYS A C     1 
ATOM   2422  O O     . CYS A  1 348  ? -51.599 52.003  91.398  1.00 25.47 ? 346  CYS A O     1 
ATOM   2423  C CB    . CYS A  1 348  ? -48.423 50.974  91.346  1.00 27.97 ? 346  CYS A CB    1 
ATOM   2424  S SG    . CYS A  1 348  ? -48.947 50.655  89.641  1.00 32.83 ? 346  CYS A SG    1 
ATOM   2425  N N     . PRO A  1 349  ? -51.051 50.632  93.070  1.00 26.84 ? 347  PRO A N     1 
ATOM   2426  C CA    . PRO A  1 349  ? -52.449 50.178  93.137  1.00 28.51 ? 347  PRO A CA    1 
ATOM   2427  C C     . PRO A  1 349  ? -53.401 51.284  93.537  1.00 27.91 ? 347  PRO A C     1 
ATOM   2428  O O     . PRO A  1 349  ? -54.551 51.305  93.082  1.00 26.91 ? 347  PRO A O     1 
ATOM   2429  C CB    . PRO A  1 349  ? -52.416 49.046  94.178  1.00 26.82 ? 347  PRO A CB    1 
ATOM   2430  C CG    . PRO A  1 349  ? -51.115 49.206  94.909  1.00 30.84 ? 347  PRO A CG    1 
ATOM   2431  C CD    . PRO A  1 349  ? -50.174 49.873  93.980  1.00 26.42 ? 347  PRO A CD    1 
ATOM   2432  N N     . PHE A  1 350  ? -52.937 52.237  94.340  1.00 26.96 ? 348  PHE A N     1 
ATOM   2433  C CA    . PHE A  1 350  ? -53.803 53.320  94.777  1.00 27.95 ? 348  PHE A CA    1 
ATOM   2434  C C     . PHE A  1 350  ? -54.002 54.354  93.681  1.00 24.13 ? 348  PHE A C     1 
ATOM   2435  O O     . PHE A  1 350  ? -55.091 54.925  93.556  1.00 23.42 ? 348  PHE A O     1 
ATOM   2436  C CB    . PHE A  1 350  ? -53.222 53.927  96.043  1.00 23.43 ? 348  PHE A CB    1 
ATOM   2437  C CG    . PHE A  1 350  ? -52.931 52.898  97.074  1.00 25.55 ? 348  PHE A CG    1 
ATOM   2438  C CD1   . PHE A  1 350  ? -53.972 52.319  97.796  1.00 30.97 ? 348  PHE A CD1   1 
ATOM   2439  C CD2   . PHE A  1 350  ? -51.632 52.447  97.278  1.00 30.15 ? 348  PHE A CD2   1 
ATOM   2440  C CE1   . PHE A  1 350  ? -53.718 51.334  98.730  1.00 29.45 ? 348  PHE A CE1   1 
ATOM   2441  C CE2   . PHE A  1 350  ? -51.370 51.449  98.221  1.00 30.93 ? 348  PHE A CE2   1 
ATOM   2442  C CZ    . PHE A  1 350  ? -52.403 50.900  98.941  1.00 31.67 ? 348  PHE A CZ    1 
ATOM   2443  N N     . VAL A  1 351  ? -52.963 54.600  92.882  1.00 23.67 ? 349  VAL A N     1 
ATOM   2444  C CA    . VAL A  1 351  ? -53.110 55.405  91.668  1.00 22.94 ? 349  VAL A CA    1 
ATOM   2445  C C     . VAL A  1 351  ? -54.143 54.773  90.741  1.00 24.37 ? 349  VAL A C     1 
ATOM   2446  O O     . VAL A  1 351  ? -55.000 55.459  90.166  1.00 24.56 ? 349  VAL A O     1 
ATOM   2447  C CB    . VAL A  1 351  ? -51.742 55.552  90.973  1.00 23.25 ? 349  VAL A CB    1 
ATOM   2448  C CG1   . VAL A  1 351  ? -51.861 56.312  89.665  1.00 22.74 ? 349  VAL A CG1   1 
ATOM   2449  C CG2   . VAL A  1 351  ? -50.741 56.243  91.895  1.00 24.38 ? 349  VAL A CG2   1 
ATOM   2450  N N     . LEU A  1 352  ? -54.054 53.455  90.557  1.00 24.83 ? 350  LEU A N     1 
ATOM   2451  C CA    . LEU A  1 352  ? -54.996 52.778  89.679  1.00 25.13 ? 350  LEU A CA    1 
ATOM   2452  C C     . LEU A  1 352  ? -56.416 52.916  90.204  1.00 26.34 ? 350  LEU A C     1 
ATOM   2453  O O     . LEU A  1 352  ? -57.341 53.194  89.432  1.00 25.71 ? 350  LEU A O     1 
ATOM   2454  C CB    . LEU A  1 352  ? -54.607 51.308  89.529  1.00 24.11 ? 350  LEU A CB    1 
ATOM   2455  C CG    . LEU A  1 352  ? -53.385 51.056  88.645  1.00 27.74 ? 350  LEU A CG    1 
ATOM   2456  C CD1   . LEU A  1 352  ? -52.995 49.591  88.705  1.00 28.49 ? 350  LEU A CD1   1 
ATOM   2457  C CD2   . LEU A  1 352  ? -53.656 51.484  87.197  1.00 23.44 ? 350  LEU A CD2   1 
ATOM   2458  N N     . ASP A  1 353  ? -56.607 52.734  91.518  1.00 27.06 ? 351  ASP A N     1 
ATOM   2459  C CA    . ASP A  1 353  ? -57.925 52.958  92.112  1.00 25.86 ? 351  ASP A CA    1 
ATOM   2460  C C     . ASP A  1 353  ? -58.441 54.347  91.771  1.00 24.17 ? 351  ASP A C     1 
ATOM   2461  O O     . ASP A  1 353  ? -59.614 54.520  91.425  1.00 25.66 ? 351  ASP A O     1 
ATOM   2462  C CB    . ASP A  1 353  ? -57.865 52.804  93.633  1.00 28.90 ? 351  ASP A CB    1 
ATOM   2463  C CG    . ASP A  1 353  ? -57.755 51.362  94.095  1.00 29.83 ? 351  ASP A CG    1 
ATOM   2464  O OD1   . ASP A  1 353  ? -57.942 50.421  93.296  1.00 33.08 ? 351  ASP A OD1   1 
ATOM   2465  O OD2   . ASP A  1 353  ? -57.478 51.169  95.293  1.00 34.77 ? 351  ASP A OD2   1 
ATOM   2466  N N     . PHE A  1 354  ? -57.565 55.349  91.856  1.00 25.06 ? 352  PHE A N     1 
ATOM   2467  C CA    . PHE A  1 354  ? -57.943 56.724  91.559  1.00 24.59 ? 352  PHE A CA    1 
ATOM   2468  C C     . PHE A  1 354  ? -58.287 56.903  90.084  1.00 23.47 ? 352  PHE A C     1 
ATOM   2469  O O     . PHE A  1 354  ? -59.296 57.529  89.750  1.00 25.49 ? 352  PHE A O     1 
ATOM   2470  C CB    . PHE A  1 354  ? -56.807 57.676  91.960  1.00 23.52 ? 352  PHE A CB    1 
ATOM   2471  C CG    . PHE A  1 354  ? -57.009 59.064  91.471  1.00 25.43 ? 352  PHE A CG    1 
ATOM   2472  C CD1   . PHE A  1 354  ? -57.812 59.950  92.175  1.00 26.97 ? 352  PHE A CD1   1 
ATOM   2473  C CD2   . PHE A  1 354  ? -56.424 59.486  90.284  1.00 25.77 ? 352  PHE A CD2   1 
ATOM   2474  C CE1   . PHE A  1 354  ? -58.012 61.251  91.708  1.00 30.30 ? 352  PHE A CE1   1 
ATOM   2475  C CE2   . PHE A  1 354  ? -56.641 60.766  89.801  1.00 27.28 ? 352  PHE A CE2   1 
ATOM   2476  C CZ    . PHE A  1 354  ? -57.422 61.652  90.520  1.00 28.96 ? 352  PHE A CZ    1 
ATOM   2477  N N     . ILE A  1 355  ? -57.463 56.358  89.185  1.00 22.47 ? 353  ILE A N     1 
ATOM   2478  C CA    . ILE A  1 355  ? -57.706 56.516  87.747  1.00 21.86 ? 353  ILE A CA    1 
ATOM   2479  C C     . ILE A  1 355  ? -58.989 55.806  87.328  1.00 23.98 ? 353  ILE A C     1 
ATOM   2480  O O     . ILE A  1 355  ? -59.750 56.309  86.493  1.00 24.04 ? 353  ILE A O     1 
ATOM   2481  C CB    . ILE A  1 355  ? -56.504 55.993  86.937  1.00 22.01 ? 353  ILE A CB    1 
ATOM   2482  C CG1   . ILE A  1 355  ? -55.252 56.846  87.203  1.00 22.36 ? 353  ILE A CG1   1 
ATOM   2483  C CG2   . ILE A  1 355  ? -56.847 55.938  85.440  1.00 23.36 ? 353  ILE A CG2   1 
ATOM   2484  C CD1   . ILE A  1 355  ? -54.001 56.267  86.573  1.00 24.03 ? 353  ILE A CD1   1 
ATOM   2485  N N     . ILE A  1 356  ? -59.227 54.612  87.869  1.00 23.14 ? 354  ILE A N     1 
ATOM   2486  C CA    . ILE A  1 356  ? -60.436 53.862  87.541  1.00 23.37 ? 354  ILE A CA    1 
ATOM   2487  C C     . ILE A  1 356  ? -61.671 54.618  88.016  1.00 26.35 ? 354  ILE A C     1 
ATOM   2488  O O     . ILE A  1 356  ? -62.684 54.684  87.315  1.00 25.31 ? 354  ILE A O     1 
ATOM   2489  C CB    . ILE A  1 356  ? -60.363 52.449  88.150  1.00 25.83 ? 354  ILE A CB    1 
ATOM   2490  C CG1   . ILE A  1 356  ? -59.298 51.613  87.435  1.00 25.01 ? 354  ILE A CG1   1 
ATOM   2491  C CG2   . ILE A  1 356  ? -61.714 51.758  88.069  1.00 29.74 ? 354  ILE A CG2   1 
ATOM   2492  C CD1   . ILE A  1 356  ? -58.942 50.315  88.182  1.00 29.80 ? 354  ILE A CD1   1 
ATOM   2493  N N     . ASP A  1 357  ? -61.596 55.225  89.202  1.00 25.86 ? 355  ASP A N     1 
ATOM   2494  C CA    . ASP A  1 357  ? -62.704 56.050  89.672  1.00 27.98 ? 355  ASP A CA    1 
ATOM   2495  C C     . ASP A  1 357  ? -62.892 57.282  88.796  1.00 27.21 ? 355  ASP A C     1 
ATOM   2496  O O     . ASP A  1 357  ? -64.032 57.688  88.520  1.00 25.38 ? 355  ASP A O     1 
ATOM   2497  C CB    . ASP A  1 357  ? -62.476 56.479  91.118  1.00 23.87 ? 355  ASP A CB    1 
ATOM   2498  C CG    . ASP A  1 357  ? -63.547 57.417  91.603  1.00 26.52 ? 355  ASP A CG    1 
ATOM   2499  O OD1   . ASP A  1 357  ? -64.654 56.917  91.856  1.00 28.82 ? 355  ASP A OD1   1 
ATOM   2500  O OD2   . ASP A  1 357  ? -63.307 58.642  91.700  1.00 29.82 ? 355  ASP A OD2   1 
ATOM   2501  N N     . LEU A  1 358  ? -61.787 57.908  88.379  1.00 24.67 ? 356  LEU A N     1 
ATOM   2502  C CA    . LEU A  1 358  ? -61.886 59.075  87.506  1.00 24.05 ? 356  LEU A CA    1 
ATOM   2503  C C     . LEU A  1 358  ? -62.518 58.699  86.172  1.00 24.52 ? 356  LEU A C     1 
ATOM   2504  O O     . LEU A  1 358  ? -63.335 59.452  85.626  1.00 26.21 ? 356  LEU A O     1 
ATOM   2505  C CB    . LEU A  1 358  ? -60.499 59.693  87.299  1.00 23.12 ? 356  LEU A CB    1 
ATOM   2506  C CG    . LEU A  1 358  ? -60.391 60.863  86.324  1.00 26.63 ? 356  LEU A CG    1 
ATOM   2507  C CD1   . LEU A  1 358  ? -61.227 62.048  86.822  1.00 26.01 ? 356  LEU A CD1   1 
ATOM   2508  C CD2   . LEU A  1 358  ? -58.907 61.269  86.082  1.00 25.74 ? 356  LEU A CD2   1 
ATOM   2509  N N     . ALA A  1 359  ? -62.152 57.532  85.634  1.00 24.66 ? 357  ALA A N     1 
ATOM   2510  C CA    . ALA A  1 359  ? -62.781 57.053  84.408  1.00 25.43 ? 357  ALA A CA    1 
ATOM   2511  C C     . ALA A  1 359  ? -64.285 56.883  84.597  1.00 23.44 ? 357  ALA A C     1 
ATOM   2512  O O     . ALA A  1 359  ? -65.072 57.231  83.710  1.00 27.90 ? 357  ALA A O     1 
ATOM   2513  C CB    . ALA A  1 359  ? -62.134 55.733  83.974  1.00 27.88 ? 357  ALA A CB    1 
ATOM   2514  N N     . ARG A  1 360  ? -64.707 56.373  85.761  1.00 25.86 ? 358  ARG A N     1 
ATOM   2515  C CA    . ARG A  1 360  ? -66.135 56.233  86.029  1.00 25.02 ? 358  ARG A CA    1 
ATOM   2516  C C     . ARG A  1 360  ? -66.831 57.590  86.090  1.00 27.66 ? 358  ARG A C     1 
ATOM   2517  O O     . ARG A  1 360  ? -67.909 57.767  85.507  1.00 28.17 ? 358  ARG A O     1 
ATOM   2518  C CB    . ARG A  1 360  ? -66.368 55.462  87.328  1.00 30.84 ? 358  ARG A CB    1 
ATOM   2519  C CG    . ARG A  1 360  ? -65.999 53.998  87.260  1.00 30.85 ? 358  ARG A CG    1 
ATOM   2520  C CD    . ARG A  1 360  ? -66.500 53.243  88.495  1.00 38.52 ? 358  ARG A CD    1 
ATOM   2521  N NE    . ARG A  1 360  ? -65.806 51.968  88.612  1.00 39.28 ? 358  ARG A NE    1 
ATOM   2522  C CZ    . ARG A  1 360  ? -66.173 50.867  87.975  1.00 42.38 ? 358  ARG A CZ    1 
ATOM   2523  N NH1   . ARG A  1 360  ? -67.273 50.833  87.233  1.00 36.70 ? 358  ARG A NH1   1 
ATOM   2524  N NH2   . ARG A  1 360  ? -65.417 49.776  88.080  1.00 43.01 ? 358  ARG A NH2   1 
ATOM   2525  N N     . ARG A  1 361  ? -66.243 58.557  86.811  1.00 24.21 ? 359  ARG A N     1 
ATOM   2526  C CA    . ARG A  1 361  ? -66.872 59.870  86.975  1.00 25.80 ? 359  ARG A CA    1 
ATOM   2527  C C     . ARG A  1 361  ? -66.960 60.615  85.649  1.00 29.78 ? 359  ARG A C     1 
ATOM   2528  O O     . ARG A  1 361  ? -67.984 61.233  85.334  1.00 29.42 ? 359  ARG A O     1 
ATOM   2529  C CB    . ARG A  1 361  ? -66.085 60.716  87.984  1.00 28.51 ? 359  ARG A CB    1 
ATOM   2530  C CG    . ARG A  1 361  ? -66.066 60.163  89.392  1.00 28.64 ? 359  ARG A CG    1 
ATOM   2531  C CD    . ARG A  1 361  ? -65.405 61.141  90.349  1.00 32.31 ? 359  ARG A CD    1 
ATOM   2532  N NE    . ARG A  1 361  ? -63.950 61.046  90.316  1.00 29.11 ? 359  ARG A NE    1 
ATOM   2533  C CZ    . ARG A  1 361  ? -63.132 62.059  90.067  1.00 32.36 ? 359  ARG A CZ    1 
ATOM   2534  N NH1   . ARG A  1 361  ? -63.592 63.273  89.797  1.00 31.64 ? 359  ARG A NH1   1 
ATOM   2535  N NH2   . ARG A  1 361  ? -61.817 61.854  90.107  1.00 27.36 ? 359  ARG A NH2   1 
ATOM   2536  N N     . SER A  1 362  ? -65.874 60.604  84.878  1.00 24.76 ? 360  SER A N     1 
ATOM   2537  C CA    . SER A  1 362  ? -65.821 61.346  83.626  1.00 26.61 ? 360  SER A CA    1 
ATOM   2538  C C     . SER A  1 362  ? -66.486 60.603  82.477  1.00 28.24 ? 360  SER A C     1 
ATOM   2539  O O     . SER A  1 362  ? -66.848 61.234  81.472  1.00 27.45 ? 360  SER A O     1 
ATOM   2540  C CB    . SER A  1 362  ? -64.361 61.653  83.261  1.00 27.29 ? 360  SER A CB    1 
ATOM   2541  O OG    . SER A  1 362  ? -63.650 60.448  83.011  1.00 24.81 ? 360  SER A OG    1 
ATOM   2542  N N     . GLY A  1 363  ? -66.655 59.289  82.603  1.00 26.86 ? 361  GLY A N     1 
ATOM   2543  C CA    . GLY A  1 363  ? -67.136 58.483  81.498  1.00 26.19 ? 361  GLY A CA    1 
ATOM   2544  C C     . GLY A  1 363  ? -66.169 58.336  80.345  1.00 28.45 ? 361  GLY A C     1 
ATOM   2545  O O     . GLY A  1 363  ? -66.592 57.966  79.246  1.00 29.83 ? 361  GLY A O     1 
ATOM   2546  N N     . ARG A  1 364  ? -64.889 58.656  80.554  1.00 26.19 ? 362  ARG A N     1 
ATOM   2547  C CA    . ARG A  1 364  ? -63.843 58.456  79.562  1.00 27.79 ? 362  ARG A CA    1 
ATOM   2548  C C     . ARG A  1 364  ? -63.145 57.140  79.863  1.00 27.44 ? 362  ARG A C     1 
ATOM   2549  O O     . ARG A  1 364  ? -62.795 56.868  81.017  1.00 29.59 ? 362  ARG A O     1 
ATOM   2550  C CB    . ARG A  1 364  ? -62.820 59.590  79.584  1.00 30.15 ? 362  ARG A CB    1 
ATOM   2551  C CG    . ARG A  1 364  ? -63.423 60.983  79.717  1.00 32.90 ? 362  ARG A CG    1 
ATOM   2552  C CD    . ARG A  1 364  ? -63.164 61.851  78.499  1.00 27.70 ? 362  ARG A CD    1 
ATOM   2553  N NE    . ARG A  1 364  ? -63.993 63.049  78.580  1.00 25.81 ? 362  ARG A NE    1 
ATOM   2554  C CZ    . ARG A  1 364  ? -63.524 64.271  78.790  1.00 29.32 ? 362  ARG A CZ    1 
ATOM   2555  N NH1   . ARG A  1 364  ? -62.218 64.513  78.822  1.00 22.41 ? 362  ARG A NH1   1 
ATOM   2556  N NH2   . ARG A  1 364  ? -64.385 65.280  78.952  1.00 23.70 ? 362  ARG A NH2   1 
ATOM   2557  N N     . ARG A  1 365  ? -62.968 56.321  78.837  1.00 27.48 ? 363  ARG A N     1 
ATOM   2558  C CA    . ARG A  1 365  ? -62.293 55.038  78.994  1.00 26.78 ? 363  ARG A CA    1 
ATOM   2559  C C     . ARG A  1 365  ? -60.786 55.290  78.935  1.00 27.54 ? 363  ARG A C     1 
ATOM   2560  O O     . ARG A  1 365  ? -60.157 55.226  77.877  1.00 27.27 ? 363  ARG A O     1 
ATOM   2561  C CB    . ARG A  1 365  ? -62.765 54.067  77.925  1.00 24.78 ? 363  ARG A CB    1 
ATOM   2562  C CG    . ARG A  1 365  ? -62.146 52.706  78.031  1.00 24.28 ? 363  ARG A CG    1 
ATOM   2563  C CD    . ARG A  1 365  ? -63.076 51.646  77.582  1.00 28.70 ? 363  ARG A CD    1 
ATOM   2564  N NE    . ARG A  1 365  ? -62.548 50.321  77.889  1.00 33.03 ? 363  ARG A NE    1 
ATOM   2565  C CZ    . ARG A  1 365  ? -61.887 49.570  77.024  1.00 27.57 ? 363  ARG A CZ    1 
ATOM   2566  N NH1   . ARG A  1 365  ? -61.696 49.965  75.776  1.00 28.29 ? 363  ARG A NH1   1 
ATOM   2567  N NH2   . ARG A  1 365  ? -61.399 48.401  77.423  1.00 27.98 ? 363  ARG A NH2   1 
ATOM   2568  N N     . ILE A  1 366  ? -60.197 55.587  80.091  1.00 24.97 ? 364  ILE A N     1 
ATOM   2569  C CA    . ILE A  1 366  ? -58.801 56.010  80.123  1.00 25.30 ? 364  ILE A CA    1 
ATOM   2570  C C     . ILE A  1 366  ? -57.899 54.862  79.689  1.00 22.37 ? 364  ILE A C     1 
ATOM   2571  O O     . ILE A  1 366  ? -58.079 53.709  80.105  1.00 22.00 ? 364  ILE A O     1 
ATOM   2572  C CB    . ILE A  1 366  ? -58.429 56.529  81.521  1.00 23.14 ? 364  ILE A CB    1 
ATOM   2573  C CG1   . ILE A  1 366  ? -59.267 57.771  81.831  1.00 24.51 ? 364  ILE A CG1   1 
ATOM   2574  C CG2   . ILE A  1 366  ? -56.882 56.840  81.591  1.00 21.41 ? 364  ILE A CG2   1 
ATOM   2575  C CD1   . ILE A  1 366  ? -59.231 58.215  83.286  1.00 26.66 ? 364  ILE A CD1   1 
ATOM   2576  N N     . MET A  1 367  ? -56.945 55.166  78.820  1.00 24.20 ? 365  MET A N     1 
ATOM   2577  C CA    . MET A  1 367  ? -55.964 54.168  78.395  1.00 25.79 ? 365  MET A CA    1 
ATOM   2578  C C     . MET A  1 367  ? -54.863 54.135  79.442  1.00 25.72 ? 365  MET A C     1 
ATOM   2579  O O     . MET A  1 367  ? -54.158 55.125  79.641  1.00 26.76 ? 365  MET A O     1 
ATOM   2580  C CB    . MET A  1 367  ? -55.426 54.494  77.003  1.00 22.96 ? 365  MET A CB    1 
ATOM   2581  C CG    . MET A  1 367  ? -56.562 54.726  75.970  1.00 24.55 ? 365  MET A CG    1 
ATOM   2582  S SD    . MET A  1 367  ? -56.040 55.108  74.286  1.00 28.12 ? 365  MET A SD    1 
ATOM   2583  C CE    . MET A  1 367  ? -55.599 53.493  73.651  1.00 28.82 ? 365  MET A CE    1 
ATOM   2584  N N     . VAL A  1 368  ? -54.737 53.026  80.150  1.00 23.78 ? 366  VAL A N     1 
ATOM   2585  C CA    . VAL A  1 368  ? -53.793 52.927  81.253  1.00 20.71 ? 366  VAL A CA    1 
ATOM   2586  C C     . VAL A  1 368  ? -52.647 52.042  80.803  1.00 22.22 ? 366  VAL A C     1 
ATOM   2587  O O     . VAL A  1 368  ? -52.824 50.827  80.637  1.00 24.67 ? 366  VAL A O     1 
ATOM   2588  C CB    . VAL A  1 368  ? -54.444 52.361  82.518  1.00 24.18 ? 366  VAL A CB    1 
ATOM   2589  C CG1   . VAL A  1 368  ? -53.401 52.300  83.634  1.00 28.04 ? 366  VAL A CG1   1 
ATOM   2590  C CG2   . VAL A  1 368  ? -55.613 53.203  82.914  1.00 25.20 ? 366  VAL A CG2   1 
ATOM   2591  N N     . ARG A  1 369  ? -51.474 52.640  80.592  1.00 21.46 ? 367  ARG A N     1 
ATOM   2592  C CA    . ARG A  1 369  ? -50.285 51.871  80.259  1.00 21.39 ? 367  ARG A CA    1 
ATOM   2593  C C     . ARG A  1 369  ? -49.557 51.488  81.543  1.00 24.37 ? 367  ARG A C     1 
ATOM   2594  O O     . ARG A  1 369  ? -48.986 52.345  82.229  1.00 23.59 ? 367  ARG A O     1 
ATOM   2595  C CB    . ARG A  1 369  ? -49.354 52.638  79.324  1.00 22.47 ? 367  ARG A CB    1 
ATOM   2596  C CG    . ARG A  1 369  ? -48.119 51.833  78.997  1.00 24.40 ? 367  ARG A CG    1 
ATOM   2597  C CD    . ARG A  1 369  ? -46.990 52.717  78.494  1.00 28.14 ? 367  ARG A CD    1 
ATOM   2598  N NE    . ARG A  1 369  ? -47.334 53.353  77.232  1.00 27.10 ? 367  ARG A NE    1 
ATOM   2599  C CZ    . ARG A  1 369  ? -46.765 54.456  76.758  1.00 32.84 ? 367  ARG A CZ    1 
ATOM   2600  N NH1   . ARG A  1 369  ? -45.789 55.070  77.414  1.00 31.96 ? 367  ARG A NH1   1 
ATOM   2601  N NH2   . ARG A  1 369  ? -47.198 54.966  75.604  1.00 27.68 ? 367  ARG A NH2   1 
ATOM   2602  N N     . LEU A  1 370  ? -49.539 50.195  81.827  1.00 22.35 ? 368  LEU A N     1 
ATOM   2603  C CA    . LEU A  1 370  ? -48.872 49.653  82.997  1.00 23.65 ? 368  LEU A CA    1 
ATOM   2604  C C     . LEU A  1 370  ? -47.427 49.337  82.624  1.00 22.16 ? 368  LEU A C     1 
ATOM   2605  O O     . LEU A  1 370  ? -47.181 48.519  81.732  1.00 24.01 ? 368  LEU A O     1 
ATOM   2606  C CB    . LEU A  1 370  ? -49.588 48.390  83.477  1.00 23.52 ? 368  LEU A CB    1 
ATOM   2607  C CG    . LEU A  1 370  ? -49.024 47.838  84.775  1.00 23.72 ? 368  LEU A CG    1 
ATOM   2608  C CD1   . LEU A  1 370  ? -49.199 48.891  85.857  1.00 24.51 ? 368  LEU A CD1   1 
ATOM   2609  C CD2   . LEU A  1 370  ? -49.683 46.524  85.170  1.00 27.62 ? 368  LEU A CD2   1 
ATOM   2610  N N     . VAL A  1 371  ? -46.477 49.974  83.307  1.00 22.32 ? 369  VAL A N     1 
ATOM   2611  C CA    . VAL A  1 371  ? -45.057 49.721  83.092  1.00 21.48 ? 369  VAL A CA    1 
ATOM   2612  C C     . VAL A  1 371  ? -44.434 49.396  84.443  1.00 24.72 ? 369  VAL A C     1 
ATOM   2613  O O     . VAL A  1 371  ? -45.042 49.595  85.490  1.00 24.14 ? 369  VAL A O     1 
ATOM   2614  C CB    . VAL A  1 371  ? -44.338 50.913  82.433  1.00 26.83 ? 369  VAL A CB    1 
ATOM   2615  C CG1   . VAL A  1 371  ? -45.066 51.344  81.187  1.00 26.61 ? 369  VAL A CG1   1 
ATOM   2616  C CG2   . VAL A  1 371  ? -44.223 52.077  83.393  1.00 25.05 ? 369  VAL A CG2   1 
ATOM   2617  N N     . LYS A  1 372  ? -43.200 48.893  84.417  1.00 25.08 ? 370  LYS A N     1 
ATOM   2618  C CA    . LYS A  1 372  ? -42.504 48.687  85.690  1.00 24.57 ? 370  LYS A CA    1 
ATOM   2619  C C     . LYS A  1 372  ? -41.884 49.991  86.199  1.00 25.34 ? 370  LYS A C     1 
ATOM   2620  O O     . LYS A  1 372  ? -42.272 50.490  87.260  1.00 25.56 ? 370  LYS A O     1 
ATOM   2621  C CB    . LYS A  1 372  ? -41.495 47.543  85.549  1.00 29.61 ? 370  LYS A CB    1 
ATOM   2622  C CG    . LYS A  1 372  ? -42.277 46.222  85.403  1.00 27.69 ? 370  LYS A CG    1 
ATOM   2623  C CD    . LYS A  1 372  ? -41.457 44.949  85.369  1.00 31.32 ? 370  LYS A CD    1 
ATOM   2624  C CE    . LYS A  1 372  ? -42.423 43.751  85.237  1.00 34.47 ? 370  LYS A CE    1 
ATOM   2625  N NZ    . LYS A  1 372  ? -41.775 42.446  84.905  1.00 32.45 ? 370  LYS A NZ    1 
ATOM   2626  N N     . GLY A  1 373  ? -40.994 50.601  85.433  1.00 22.21 ? 371  GLY A N     1 
ATOM   2627  C CA    . GLY A  1 373  ? -40.522 51.951  85.722  1.00 20.98 ? 371  GLY A CA    1 
ATOM   2628  C C     . GLY A  1 373  ? -39.074 52.143  85.275  1.00 26.10 ? 371  GLY A C     1 
ATOM   2629  O O     . GLY A  1 373  ? -38.254 51.237  85.286  1.00 24.14 ? 371  GLY A O     1 
ATOM   2630  N N     . ALA A  1 374  ? -38.747 53.374  84.870  1.00 23.84 ? 372  ALA A N     1 
ATOM   2631  C CA    . ALA A  1 374  ? -37.488 53.632  84.171  1.00 25.91 ? 372  ALA A CA    1 
ATOM   2632  C C     . ALA A  1 374  ? -36.472 54.424  84.981  1.00 25.42 ? 372  ALA A C     1 
ATOM   2633  O O     . ALA A  1 374  ? -35.382 54.697  84.470  1.00 27.78 ? 372  ALA A O     1 
ATOM   2634  C CB    . ALA A  1 374  ? -37.746 54.385  82.857  1.00 23.48 ? 372  ALA A CB    1 
ATOM   2635  N N     . TYR A  1 375  ? -36.794 54.826  86.205  1.00 23.73 ? 373  TYR A N     1 
ATOM   2636  C CA    . TYR A  1 375  ? -35.944 55.754  86.945  1.00 23.92 ? 373  TYR A CA    1 
ATOM   2637  C C     . TYR A  1 375  ? -35.412 55.152  88.245  1.00 21.40 ? 373  TYR A C     1 
ATOM   2638  O O     . TYR A  1 375  ? -35.152 55.886  89.203  1.00 21.25 ? 373  TYR A O     1 
ATOM   2639  C CB    . TYR A  1 375  ? -36.704 57.043  87.251  1.00 23.98 ? 373  TYR A CB    1 
ATOM   2640  C CG    . TYR A  1 375  ? -37.269 57.738  86.037  1.00 22.49 ? 373  TYR A CG    1 
ATOM   2641  C CD1   . TYR A  1 375  ? -38.492 57.347  85.493  1.00 22.36 ? 373  TYR A CD1   1 
ATOM   2642  C CD2   . TYR A  1 375  ? -36.572 58.777  85.424  1.00 26.48 ? 373  TYR A CD2   1 
ATOM   2643  C CE1   . TYR A  1 375  ? -39.009 57.982  84.368  1.00 25.50 ? 373  TYR A CE1   1 
ATOM   2644  C CE2   . TYR A  1 375  ? -37.078 59.418  84.299  1.00 28.61 ? 373  TYR A CE2   1 
ATOM   2645  C CZ    . TYR A  1 375  ? -38.295 59.018  83.778  1.00 28.76 ? 373  TYR A CZ    1 
ATOM   2646  O OH    . TYR A  1 375  ? -38.802 59.663  82.668  1.00 29.90 ? 373  TYR A OH    1 
ATOM   2647  N N     . TRP A  1 376  ? -35.189 53.838  88.281  1.00 21.24 ? 374  TRP A N     1 
ATOM   2648  C CA    . TRP A  1 376  ? -35.000 53.168  89.571  1.00 20.41 ? 374  TRP A CA    1 
ATOM   2649  C C     . TRP A  1 376  ? -33.748 53.660  90.290  1.00 25.66 ? 374  TRP A C     1 
ATOM   2650  O O     . TRP A  1 376  ? -33.825 54.088  91.446  1.00 23.87 ? 374  TRP A O     1 
ATOM   2651  C CB    . TRP A  1 376  ? -34.948 51.652  89.392  1.00 24.38 ? 374  TRP A CB    1 
ATOM   2652  C CG    . TRP A  1 376  ? -34.817 50.927  90.705  1.00 23.19 ? 374  TRP A CG    1 
ATOM   2653  C CD1   . TRP A  1 376  ? -35.817 50.649  91.586  1.00 24.42 ? 374  TRP A CD1   1 
ATOM   2654  C CD2   . TRP A  1 376  ? -33.607 50.422  91.292  1.00 25.90 ? 374  TRP A CD2   1 
ATOM   2655  N NE1   . TRP A  1 376  ? -35.307 49.984  92.689  1.00 26.03 ? 374  TRP A NE1   1 
ATOM   2656  C CE2   . TRP A  1 376  ? -33.954 49.837  92.530  1.00 26.67 ? 374  TRP A CE2   1 
ATOM   2657  C CE3   . TRP A  1 376  ? -32.267 50.410  90.893  1.00 28.67 ? 374  TRP A CE3   1 
ATOM   2658  C CZ2   . TRP A  1 376  ? -33.008 49.237  93.365  1.00 27.38 ? 374  TRP A CZ2   1 
ATOM   2659  C CZ3   . TRP A  1 376  ? -31.323 49.808  91.723  1.00 28.65 ? 374  TRP A CZ3   1 
ATOM   2660  C CH2   . TRP A  1 376  ? -31.699 49.233  92.943  1.00 27.39 ? 374  TRP A CH2   1 
ATOM   2661  N N     . ASP A  1 377  ? -32.582 53.615  89.620  1.00 22.95 ? 375  ASP A N     1 
ATOM   2662  C CA    . ASP A  1 377  ? -31.340 54.087  90.238  1.00 25.56 ? 375  ASP A CA    1 
ATOM   2663  C C     . ASP A  1 377  ? -31.491 55.502  90.771  1.00 24.87 ? 375  ASP A C     1 
ATOM   2664  O O     . ASP A  1 377  ? -31.003 55.820  91.861  1.00 26.30 ? 375  ASP A O     1 
ATOM   2665  C CB    . ASP A  1 377  ? -30.180 54.100  89.229  1.00 28.06 ? 375  ASP A CB    1 
ATOM   2666  C CG    . ASP A  1 377  ? -29.922 52.764  88.579  1.00 38.43 ? 375  ASP A CG    1 
ATOM   2667  O OD1   . ASP A  1 377  ? -30.079 51.726  89.244  1.00 42.32 ? 375  ASP A OD1   1 
ATOM   2668  O OD2   . ASP A  1 377  ? -29.528 52.764  87.388  1.00 44.06 ? 375  ASP A OD2   1 
ATOM   2669  N N     . ALA A  1 378  ? -32.130 56.381  89.986  1.00 24.06 ? 376  ALA A N     1 
ATOM   2670  C CA    . ALA A  1 378  ? -32.249 57.780  90.379  1.00 23.39 ? 376  ALA A CA    1 
ATOM   2671  C C     . ALA A  1 378  ? -33.129 57.932  91.609  1.00 23.92 ? 376  ALA A C     1 
ATOM   2672  O O     . ALA A  1 378  ? -32.857 58.782  92.473  1.00 22.42 ? 376  ALA A O     1 
ATOM   2673  C CB    . ALA A  1 378  ? -32.802 58.618  89.221  1.00 24.03 ? 376  ALA A CB    1 
ATOM   2674  N N     . GLU A  1 379  ? -34.195 57.134  91.700  1.00 21.77 ? 377  GLU A N     1 
ATOM   2675  C CA    . GLU A  1 379  ? -35.063 57.214  92.869  1.00 22.04 ? 377  GLU A CA    1 
ATOM   2676  C C     . GLU A  1 379  ? -34.319 56.788  94.126  1.00 21.90 ? 377  GLU A C     1 
ATOM   2677  O O     . GLU A  1 379  ? -34.525 57.360  95.201  1.00 22.82 ? 377  GLU A O     1 
ATOM   2678  C CB    . GLU A  1 379  ? -36.309 56.344  92.684  1.00 22.69 ? 377  GLU A CB    1 
ATOM   2679  C CG    . GLU A  1 379  ? -37.244 56.746  91.495  1.00 21.23 ? 377  GLU A CG    1 
ATOM   2680  C CD    . GLU A  1 379  ? -37.809 58.171  91.593  1.00 22.77 ? 377  GLU A CD    1 
ATOM   2681  O OE1   . GLU A  1 379  ? -37.747 58.812  92.675  1.00 22.44 ? 377  GLU A OE1   1 
ATOM   2682  O OE2   . GLU A  1 379  ? -38.334 58.659  90.566  1.00 24.09 ? 377  GLU A OE2   1 
ATOM   2683  N N     . ILE A  1 380  ? -33.476 55.757  94.018  1.00 21.99 ? 378  ILE A N     1 
ATOM   2684  C CA    . ILE A  1 380  ? -32.704 55.304  95.175  1.00 22.79 ? 378  ILE A CA    1 
ATOM   2685  C C     . ILE A  1 380  ? -31.774 56.412  95.657  1.00 25.41 ? 378  ILE A C     1 
ATOM   2686  O O     . ILE A  1 380  ? -31.733 56.744  96.848  1.00 22.92 ? 378  ILE A O     1 
ATOM   2687  C CB    . ILE A  1 380  ? -31.917 54.025  94.834  1.00 24.66 ? 378  ILE A CB    1 
ATOM   2688  C CG1   . ILE A  1 380  ? -32.850 52.886  94.427  1.00 25.07 ? 378  ILE A CG1   1 
ATOM   2689  C CG2   . ILE A  1 380  ? -31.019 53.629  96.004  1.00 24.72 ? 378  ILE A CG2   1 
ATOM   2690  C CD1   . ILE A  1 380  ? -33.955 52.558  95.426  1.00 25.40 ? 378  ILE A CD1   1 
ATOM   2691  N N     . LYS A  1 381  ? -31.006 56.996  94.729  1.00 22.52 ? 379  LYS A N     1 
ATOM   2692  C CA    . LYS A  1 381  ? -30.056 58.043  95.084  1.00 24.83 ? 379  LYS A CA    1 
ATOM   2693  C C     . LYS A  1 381  ? -30.758 59.256  95.675  1.00 24.70 ? 379  LYS A C     1 
ATOM   2694  O O     . LYS A  1 381  ? -30.305 59.819  96.679  1.00 21.84 ? 379  LYS A O     1 
ATOM   2695  C CB    . LYS A  1 381  ? -29.254 58.452  93.847  1.00 22.55 ? 379  LYS A CB    1 
ATOM   2696  C CG    . LYS A  1 381  ? -28.305 59.616  94.077  1.00 22.79 ? 379  LYS A CG    1 
ATOM   2697  C CD    . LYS A  1 381  ? -27.431 59.842  92.847  1.00 25.62 ? 379  LYS A CD    1 
ATOM   2698  C CE    . LYS A  1 381  ? -26.357 60.881  93.101  1.00 23.03 ? 379  LYS A CE    1 
ATOM   2699  N NZ    . LYS A  1 381  ? -25.638 61.235  91.828  1.00 24.18 ? 379  LYS A NZ    1 
ATOM   2700  N N     . ARG A  1 382  ? -31.876 59.663  95.074  1.00 23.36 ? 380  ARG A N     1 
ATOM   2701  C CA    . ARG A  1 382  ? -32.551 60.878  95.521  1.00 23.44 ? 380  ARG A CA    1 
ATOM   2702  C C     . ARG A  1 382  ? -33.084 60.731  96.941  1.00 23.29 ? 380  ARG A C     1 
ATOM   2703  O O     . ARG A  1 382  ? -32.919 61.640  97.765  1.00 23.72 ? 380  ARG A O     1 
ATOM   2704  C CB    . ARG A  1 382  ? -33.684 61.232  94.549  1.00 26.91 ? 380  ARG A CB    1 
ATOM   2705  C CG    . ARG A  1 382  ? -34.561 62.378  95.003  1.00 31.14 ? 380  ARG A CG    1 
ATOM   2706  C CD    . ARG A  1 382  ? -34.208 63.677  94.322  1.00 43.55 ? 380  ARG A CD    1 
ATOM   2707  N NE    . ARG A  1 382  ? -32.879 64.157  94.687  1.00 41.70 ? 380  ARG A NE    1 
ATOM   2708  C CZ    . ARG A  1 382  ? -32.151 64.975  93.939  1.00 46.34 ? 380  ARG A CZ    1 
ATOM   2709  N NH1   . ARG A  1 382  ? -32.589 65.413  92.768  1.00 52.97 ? 380  ARG A NH1   1 
ATOM   2710  N NH2   . ARG A  1 382  ? -30.951 65.355  94.373  1.00 46.93 ? 380  ARG A NH2   1 
ATOM   2711  N N     . ALA A  1 383  ? -33.712 59.589  97.254  1.00 22.24 ? 381  ALA A N     1 
ATOM   2712  C CA    . ALA A  1 383  ? -34.209 59.371  98.612  1.00 23.44 ? 381  ALA A CA    1 
ATOM   2713  C C     . ALA A  1 383  ? -33.073 59.395  99.629  1.00 23.70 ? 381  ALA A C     1 
ATOM   2714  O O     . ALA A  1 383  ? -33.241 59.896  100.748 1.00 25.80 ? 381  ALA A O     1 
ATOM   2715  C CB    . ALA A  1 383  ? -34.957 58.043  98.712  1.00 22.89 ? 381  ALA A CB    1 
ATOM   2716  N N     . GLN A  1 384  ? -31.928 58.817  99.273  1.00 23.78 ? 382  GLN A N     1 
ATOM   2717  C CA    . GLN A  1 384  ? -30.790 58.818  100.184 1.00 23.74 ? 382  GLN A CA    1 
ATOM   2718  C C     . GLN A  1 384  ? -30.261 60.233  100.389 1.00 23.90 ? 382  GLN A C     1 
ATOM   2719  O O     . GLN A  1 384  ? -30.042 60.658  101.529 1.00 25.32 ? 382  GLN A O     1 
ATOM   2720  C CB    . GLN A  1 384  ? -29.700 57.884  99.664  1.00 23.86 ? 382  GLN A CB    1 
ATOM   2721  C CG    . GLN A  1 384  ? -30.081 56.400  99.706  1.00 21.24 ? 382  GLN A CG    1 
ATOM   2722  C CD    . GLN A  1 384  ? -28.931 55.493  99.311  1.00 24.26 ? 382  GLN A CD    1 
ATOM   2723  O OE1   . GLN A  1 384  ? -27.988 55.928  98.652  1.00 27.08 ? 382  GLN A OE1   1 
ATOM   2724  N NE2   . GLN A  1 384  ? -29.005 54.225  99.713  1.00 25.71 ? 382  GLN A NE2   1 
ATOM   2725  N N     . LEU A  1 385  ? -30.085 60.993  99.298  1.00 21.88 ? 383  LEU A N     1 
ATOM   2726  C CA    . LEU A  1 385  ? -29.628 62.373  99.425  1.00 23.09 ? 383  LEU A CA    1 
ATOM   2727  C C     . LEU A  1 385  ? -30.561 63.189  100.306 1.00 25.07 ? 383  LEU A C     1 
ATOM   2728  O O     . LEU A  1 385  ? -30.107 64.003  101.116 1.00 26.85 ? 383  LEU A O     1 
ATOM   2729  C CB    . LEU A  1 385  ? -29.503 63.030  98.050  1.00 26.07 ? 383  LEU A CB    1 
ATOM   2730  C CG    . LEU A  1 385  ? -28.306 62.635  97.188  1.00 25.09 ? 383  LEU A CG    1 
ATOM   2731  C CD1   . LEU A  1 385  ? -28.373 63.347  95.841  1.00 28.99 ? 383  LEU A CD1   1 
ATOM   2732  C CD2   . LEU A  1 385  ? -27.023 62.970  97.909  1.00 29.68 ? 383  LEU A CD2   1 
ATOM   2733  N N     . ASP A  1 386  ? -31.866 62.980  100.176 1.00 23.10 ? 384  ASP A N     1 
ATOM   2734  C CA    . ASP A  1 386  ? -32.829 63.833  100.855 1.00 24.97 ? 384  ASP A CA    1 
ATOM   2735  C C     . ASP A  1 386  ? -33.137 63.353  102.264 1.00 25.29 ? 384  ASP A C     1 
ATOM   2736  O O     . ASP A  1 386  ? -33.926 63.996  102.963 1.00 26.22 ? 384  ASP A O     1 
ATOM   2737  C CB    . ASP A  1 386  ? -34.125 63.933  100.042 1.00 24.02 ? 384  ASP A CB    1 
ATOM   2738  C CG    . ASP A  1 386  ? -33.960 64.777  98.765  1.00 34.71 ? 384  ASP A CG    1 
ATOM   2739  O OD1   . ASP A  1 386  ? -32.894 65.424  98.584  1.00 35.65 ? 384  ASP A OD1   1 
ATOM   2740  O OD2   . ASP A  1 386  ? -34.899 64.792  97.939  1.00 33.68 ? 384  ASP A OD2   1 
ATOM   2741  N N     . GLY A  1 387  ? -32.528 62.253  102.691 1.00 25.05 ? 385  GLY A N     1 
ATOM   2742  C CA    . GLY A  1 387  ? -32.737 61.748  104.037 1.00 26.43 ? 385  GLY A CA    1 
ATOM   2743  C C     . GLY A  1 387  ? -34.170 61.362  104.333 1.00 27.22 ? 385  GLY A C     1 
ATOM   2744  O O     . GLY A  1 387  ? -34.646 61.569  105.458 1.00 25.65 ? 385  GLY A O     1 
ATOM   2745  N N     . LEU A  1 388  ? -34.869 60.787  103.359 1.00 26.30 ? 386  LEU A N     1 
ATOM   2746  C CA    . LEU A  1 388  ? -36.290 60.530  103.553 1.00 28.16 ? 386  LEU A CA    1 
ATOM   2747  C C     . LEU A  1 388  ? -36.512 59.178  104.219 1.00 28.49 ? 386  LEU A C     1 
ATOM   2748  O O     . LEU A  1 388  ? -35.598 58.363  104.374 1.00 29.20 ? 386  LEU A O     1 
ATOM   2749  C CB    . LEU A  1 388  ? -37.036 60.632  102.217 1.00 23.82 ? 386  LEU A CB    1 
ATOM   2750  C CG    . LEU A  1 388  ? -36.874 62.062  101.684 1.00 26.54 ? 386  LEU A CG    1 
ATOM   2751  C CD1   . LEU A  1 388  ? -37.556 62.247  100.355 1.00 26.43 ? 386  LEU A CD1   1 
ATOM   2752  C CD2   . LEU A  1 388  ? -37.343 63.089  102.694 1.00 27.43 ? 386  LEU A CD2   1 
ATOM   2753  N N     . ALA A  1 389  ? -37.757 58.953  104.644 1.00 30.22 ? 387  ALA A N     1 
ATOM   2754  C CA    . ALA A  1 389  ? -38.042 57.810  105.502 1.00 28.45 ? 387  ALA A CA    1 
ATOM   2755  C C     . ALA A  1 389  ? -37.786 56.492  104.783 1.00 29.56 ? 387  ALA A C     1 
ATOM   2756  O O     . ALA A  1 389  ? -37.293 55.531  105.388 1.00 29.00 ? 387  ALA A O     1 
ATOM   2757  C CB    . ALA A  1 389  ? -39.486 57.883  105.998 1.00 33.42 ? 387  ALA A CB    1 
ATOM   2758  N N     . ASP A  1 390  ? -38.078 56.432  103.483 1.00 28.42 ? 388  ASP A N     1 
ATOM   2759  C CA    . ASP A  1 390  ? -37.966 55.182  102.747 1.00 26.57 ? 388  ASP A CA    1 
ATOM   2760  C C     . ASP A  1 390  ? -37.932 55.496  101.252 1.00 25.76 ? 388  ASP A C     1 
ATOM   2761  O O     . ASP A  1 390  ? -37.930 56.660  100.835 1.00 22.48 ? 388  ASP A O     1 
ATOM   2762  C CB    . ASP A  1 390  ? -39.124 54.235  103.100 1.00 27.39 ? 388  ASP A CB    1 
ATOM   2763  C CG    . ASP A  1 390  ? -38.755 52.770  102.932 1.00 31.07 ? 388  ASP A CG    1 
ATOM   2764  O OD1   . ASP A  1 390  ? -38.074 52.439  101.942 1.00 30.21 ? 388  ASP A OD1   1 
ATOM   2765  O OD2   . ASP A  1 390  ? -39.133 51.941  103.796 1.00 37.13 ? 388  ASP A OD2   1 
ATOM   2766  N N     . PHE A  1 391  ? -37.889 54.454  100.460 1.00 23.08 ? 389  PHE A N     1 
ATOM   2767  C CA    . PHE A  1 391  ? -37.902 54.735  99.036  1.00 24.15 ? 389  PHE A CA    1 
ATOM   2768  C C     . PHE A  1 391  ? -39.340 54.759  98.518  1.00 25.64 ? 389  PHE A C     1 
ATOM   2769  O O     . PHE A  1 391  ? -40.231 54.147  99.116  1.00 26.17 ? 389  PHE A O     1 
ATOM   2770  C CB    . PHE A  1 391  ? -37.079 53.684  98.290  1.00 24.14 ? 389  PHE A CB    1 
ATOM   2771  C CG    . PHE A  1 391  ? -35.655 53.593  98.781  1.00 21.06 ? 389  PHE A CG    1 
ATOM   2772  C CD1   . PHE A  1 391  ? -34.722 54.535  98.391  1.00 22.55 ? 389  PHE A CD1   1 
ATOM   2773  C CD2   . PHE A  1 391  ? -35.270 52.598  99.661  1.00 27.27 ? 389  PHE A CD2   1 
ATOM   2774  C CE1   . PHE A  1 391  ? -33.402 54.478  98.846  1.00 24.38 ? 389  PHE A CE1   1 
ATOM   2775  C CE2   . PHE A  1 391  ? -33.952 52.527  100.121 1.00 26.16 ? 389  PHE A CE2   1 
ATOM   2776  C CZ    . PHE A  1 391  ? -33.025 53.476  99.714  1.00 23.16 ? 389  PHE A CZ    1 
ATOM   2777  N N     . PRO A  1 392  ? -39.615 55.491  97.437  1.00 24.84 ? 390  PRO A N     1 
ATOM   2778  C CA    . PRO A  1 392  ? -40.952 55.450  96.817  1.00 24.08 ? 390  PRO A CA    1 
ATOM   2779  C C     . PRO A  1 392  ? -41.093 54.347  95.780  1.00 27.24 ? 390  PRO A C     1 
ATOM   2780  O O     . PRO A  1 392  ? -42.112 54.286  95.080  1.00 25.19 ? 390  PRO A O     1 
ATOM   2781  C CB    . PRO A  1 392  ? -41.048 56.830  96.145  1.00 20.63 ? 390  PRO A CB    1 
ATOM   2782  C CG    . PRO A  1 392  ? -39.610 57.077  95.681  1.00 24.96 ? 390  PRO A CG    1 
ATOM   2783  C CD    . PRO A  1 392  ? -38.723 56.471  96.791  1.00 24.12 ? 390  PRO A CD    1 
ATOM   2784  N N     . VAL A  1 393  ? -40.067 53.516  95.644  1.00 26.73 ? 391  VAL A N     1 
ATOM   2785  C CA    . VAL A  1 393  ? -40.047 52.402  94.713  1.00 26.54 ? 391  VAL A CA    1 
ATOM   2786  C C     . VAL A  1 393  ? -39.582 51.192  95.501  1.00 23.72 ? 391  VAL A C     1 
ATOM   2787  O O     . VAL A  1 393  ? -38.997 51.325  96.573  1.00 25.29 ? 391  VAL A O     1 
ATOM   2788  C CB    . VAL A  1 393  ? -39.105 52.648  93.508  1.00 23.96 ? 391  VAL A CB    1 
ATOM   2789  C CG1   . VAL A  1 393  ? -39.647 53.753  92.588  1.00 23.58 ? 391  VAL A CG1   1 
ATOM   2790  C CG2   . VAL A  1 393  ? -37.694 53.020  94.012  1.00 23.92 ? 391  VAL A CG2   1 
ATOM   2791  N N     . PHE A  1 394  ? -39.873 50.004  94.972  1.00 23.90 ? 392  PHE A N     1 
ATOM   2792  C CA    . PHE A  1 394  ? -39.374 48.783  95.588  1.00 25.57 ? 392  PHE A CA    1 
ATOM   2793  C C     . PHE A  1 394  ? -37.861 48.686  95.410  1.00 26.14 ? 392  PHE A C     1 
ATOM   2794  O O     . PHE A  1 394  ? -37.275 49.348  94.550  1.00 25.47 ? 392  PHE A O     1 
ATOM   2795  C CB    . PHE A  1 394  ? -40.078 47.570  94.986  1.00 24.50 ? 392  PHE A CB    1 
ATOM   2796  C CG    . PHE A  1 394  ? -41.561 47.605  95.171  1.00 27.70 ? 392  PHE A CG    1 
ATOM   2797  C CD1   . PHE A  1 394  ? -42.108 47.492  96.440  1.00 29.51 ? 392  PHE A CD1   1 
ATOM   2798  C CD2   . PHE A  1 394  ? -42.405 47.805  94.095  1.00 28.67 ? 392  PHE A CD2   1 
ATOM   2799  C CE1   . PHE A  1 394  ? -43.469 47.554  96.625  1.00 29.23 ? 392  PHE A CE1   1 
ATOM   2800  C CE2   . PHE A  1 394  ? -43.770 47.856  94.276  1.00 25.38 ? 392  PHE A CE2   1 
ATOM   2801  C CZ    . PHE A  1 394  ? -44.300 47.740  95.539  1.00 29.57 ? 392  PHE A CZ    1 
ATOM   2802  N N     . THR A  1 395  ? -37.220 47.877  96.269  1.00 26.17 ? 393  THR A N     1 
ATOM   2803  C CA    . THR A  1 395  ? -35.772 47.677  96.204  1.00 29.18 ? 393  THR A CA    1 
ATOM   2804  C C     . THR A  1 395  ? -35.367 46.304  95.685  1.00 28.74 ? 393  THR A C     1 
ATOM   2805  O O     . THR A  1 395  ? -34.170 46.060  95.510  1.00 30.20 ? 393  THR A O     1 
ATOM   2806  C CB    . THR A  1 395  ? -35.118 47.887  97.583  1.00 28.19 ? 393  THR A CB    1 
ATOM   2807  O OG1   . THR A  1 395  ? -35.770 47.068  98.561  1.00 28.73 ? 393  THR A OG1   1 
ATOM   2808  C CG2   . THR A  1 395  ? -35.184 49.335  98.012  1.00 28.80 ? 393  THR A CG2   1 
ATOM   2809  N N     . ARG A  1 396  ? -36.313 45.393  95.470  1.00 30.31 ? 394  ARG A N     1 
ATOM   2810  C CA    . ARG A  1 396  ? -36.032 44.098  94.865  1.00 32.12 ? 394  ARG A CA    1 
ATOM   2811  C C     . ARG A  1 396  ? -36.829 43.984  93.582  1.00 31.87 ? 394  ARG A C     1 
ATOM   2812  O O     . ARG A  1 396  ? -38.038 44.252  93.575  1.00 33.10 ? 394  ARG A O     1 
ATOM   2813  C CB    . ARG A  1 396  ? -36.386 42.935  95.795  1.00 31.70 ? 394  ARG A CB    1 
ATOM   2814  C CG    . ARG A  1 396  ? -35.599 42.890  97.065  1.00 34.47 ? 394  ARG A CG    1 
ATOM   2815  C CD    . ARG A  1 396  ? -35.817 41.567  97.799  1.00 34.50 ? 394  ARG A CD    1 
ATOM   2816  N NE    . ARG A  1 396  ? -35.202 41.622  99.117  1.00 41.05 ? 394  ARG A NE    1 
ATOM   2817  C CZ    . ARG A  1 396  ? -34.686 40.581  99.754  1.00 44.97 ? 394  ARG A CZ    1 
ATOM   2818  N NH1   . ARG A  1 396  ? -34.710 39.366  99.223  1.00 46.98 ? 394  ARG A NH1   1 
ATOM   2819  N NH2   . ARG A  1 396  ? -34.126 40.765  100.950 1.00 39.31 ? 394  ARG A NH2   1 
ATOM   2820  N N     . LYS A  1 397  ? -36.153 43.586  92.503  1.00 28.35 ? 395  LYS A N     1 
ATOM   2821  C CA    . LYS A  1 397  ? -36.822 43.467  91.208  1.00 31.76 ? 395  LYS A CA    1 
ATOM   2822  C C     . LYS A  1 397  ? -38.029 42.540  91.301  1.00 31.50 ? 395  LYS A C     1 
ATOM   2823  O O     . LYS A  1 397  ? -39.065 42.774  90.665  1.00 29.37 ? 395  LYS A O     1 
ATOM   2824  C CB    . LYS A  1 397  ? -35.819 42.966  90.162  1.00 34.59 ? 395  LYS A CB    1 
ATOM   2825  C CG    . LYS A  1 397  ? -36.255 43.123  88.718  1.00 37.76 ? 395  LYS A CG    1 
ATOM   2826  C CD    . LYS A  1 397  ? -36.949 41.879  88.190  1.00 37.40 ? 395  LYS A CD    1 
ATOM   2827  C CE    . LYS A  1 397  ? -37.367 42.068  86.740  1.00 37.90 ? 395  LYS A CE    1 
ATOM   2828  N NZ    . LYS A  1 397  ? -38.308 40.986  86.299  1.00 38.28 ? 395  LYS A NZ    1 
ATOM   2829  N N     . ILE A  1 398  ? -37.920 41.484  92.106  1.00 30.60 ? 396  ILE A N     1 
ATOM   2830  C CA    . ILE A  1 398  ? -39.025 40.537  92.185  1.00 31.26 ? 396  ILE A CA    1 
ATOM   2831  C C     . ILE A  1 398  ? -40.262 41.184  92.814  1.00 28.49 ? 396  ILE A C     1 
ATOM   2832  O O     . ILE A  1 398  ? -41.400 40.784  92.523  1.00 29.87 ? 396  ILE A O     1 
ATOM   2833  C CB    . ILE A  1 398  ? -38.555 39.275  92.934  1.00 33.73 ? 396  ILE A CB    1 
ATOM   2834  C CG1   . ILE A  1 398  ? -39.513 38.114  92.688  1.00 36.00 ? 396  ILE A CG1   1 
ATOM   2835  C CG2   . ILE A  1 398  ? -38.385 39.549  94.410  1.00 32.24 ? 396  ILE A CG2   1 
ATOM   2836  C CD1   . ILE A  1 398  ? -38.929 36.788  93.119  1.00 39.29 ? 396  ILE A CD1   1 
ATOM   2837  N N     . HIS A  1 399  ? -40.075 42.184  93.680  1.00 28.84 ? 397  HIS A N     1 
ATOM   2838  C CA    . HIS A  1 399  ? -41.225 42.896  94.242  1.00 28.88 ? 397  HIS A CA    1 
ATOM   2839  C C     . HIS A  1 399  ? -41.966 43.675  93.157  1.00 27.57 ? 397  HIS A C     1 
ATOM   2840  O O     . HIS A  1 399  ? -43.204 43.668  93.094  1.00 27.63 ? 397  HIS A O     1 
ATOM   2841  C CB    . HIS A  1 399  ? -40.756 43.840  95.359  1.00 29.51 ? 397  HIS A CB    1 
ATOM   2842  C CG    . HIS A  1 399  ? -40.233 43.133  96.577  1.00 29.41 ? 397  HIS A CG    1 
ATOM   2843  N ND1   . HIS A  1 399  ? -39.544 43.784  97.578  1.00 34.21 ? 397  HIS A ND1   1 
ATOM   2844  C CD2   . HIS A  1 399  ? -40.317 41.837  96.961  1.00 33.07 ? 397  HIS A CD2   1 
ATOM   2845  C CE1   . HIS A  1 399  ? -39.220 42.916  98.522  1.00 33.65 ? 397  HIS A CE1   1 
ATOM   2846  N NE2   . HIS A  1 399  ? -39.675 41.728  98.170  1.00 31.96 ? 397  HIS A NE2   1 
ATOM   2847  N N     . THR A  1 400  ? -41.217 44.344  92.293  1.00 25.14 ? 398  THR A N     1 
ATOM   2848  C CA    . THR A  1 400  ? -41.824 45.034  91.161  1.00 25.44 ? 398  THR A CA    1 
ATOM   2849  C C     . THR A  1 400  ? -42.602 44.070  90.267  1.00 27.37 ? 398  THR A C     1 
ATOM   2850  O O     . THR A  1 400  ? -43.664 44.423  89.738  1.00 28.61 ? 398  THR A O     1 
ATOM   2851  C CB    . THR A  1 400  ? -40.732 45.747  90.376  1.00 26.57 ? 398  THR A CB    1 
ATOM   2852  O OG1   . THR A  1 400  ? -40.175 46.783  91.200  1.00 27.99 ? 398  THR A OG1   1 
ATOM   2853  C CG2   . THR A  1 400  ? -41.281 46.328  89.071  1.00 22.96 ? 398  THR A CG2   1 
ATOM   2854  N N     . ASP A  1 401  ? -42.080 42.861  90.065  1.00 28.39 ? 399  ASP A N     1 
ATOM   2855  C CA    . ASP A  1 401  ? -42.796 41.863  89.269  1.00 26.79 ? 399  ASP A CA    1 
ATOM   2856  C C     . ASP A  1 401  ? -44.133 41.484  89.913  1.00 29.53 ? 399  ASP A C     1 
ATOM   2857  O O     . ASP A  1 401  ? -45.159 41.384  89.229  1.00 29.22 ? 399  ASP A O     1 
ATOM   2858  C CB    . ASP A  1 401  ? -41.925 40.616  89.088  1.00 29.71 ? 399  ASP A CB    1 
ATOM   2859  C CG    . ASP A  1 401  ? -40.766 40.828  88.118  1.00 34.95 ? 399  ASP A CG    1 
ATOM   2860  O OD1   . ASP A  1 401  ? -40.846 41.711  87.233  1.00 33.90 ? 399  ASP A OD1   1 
ATOM   2861  O OD2   . ASP A  1 401  ? -39.762 40.092  88.236  1.00 35.83 ? 399  ASP A OD2   1 
ATOM   2862  N N     . VAL A  1 402  ? -44.134 41.241  91.224  1.00 30.42 ? 400  VAL A N     1 
ATOM   2863  C CA    . VAL A  1 402  ? -45.386 40.928  91.904  1.00 28.20 ? 400  VAL A CA    1 
ATOM   2864  C C     . VAL A  1 402  ? -46.332 42.113  91.821  1.00 28.03 ? 400  VAL A C     1 
ATOM   2865  O O     . VAL A  1 402  ? -47.519 41.943  91.538  1.00 27.68 ? 400  VAL A O     1 
ATOM   2866  C CB    . VAL A  1 402  ? -45.144 40.516  93.364  1.00 30.53 ? 400  VAL A CB    1 
ATOM   2867  C CG1   . VAL A  1 402  ? -46.501 40.293  94.073  1.00 27.62 ? 400  VAL A CG1   1 
ATOM   2868  C CG2   . VAL A  1 402  ? -44.293 39.254  93.424  1.00 32.58 ? 400  VAL A CG2   1 
ATOM   2869  N N     . SER A  1 403  ? -45.815 43.330  92.055  1.00 26.46 ? 401  SER A N     1 
ATOM   2870  C CA    . SER A  1 403  ? -46.643 44.534  91.960  1.00 29.16 ? 401  SER A CA    1 
ATOM   2871  C C     . SER A  1 403  ? -47.284 44.662  90.581  1.00 31.97 ? 401  SER A C     1 
ATOM   2872  O O     . SER A  1 403  ? -48.471 45.005  90.465  1.00 25.94 ? 401  SER A O     1 
ATOM   2873  C CB    . SER A  1 403  ? -45.804 45.782  92.263  1.00 27.73 ? 401  SER A CB    1 
ATOM   2874  O OG    . SER A  1 403  ? -46.569 46.977  92.139  1.00 26.62 ? 401  SER A OG    1 
ATOM   2875  N N     . TYR A  1 404  ? -46.502 44.414  89.524  1.00 26.13 ? 402  TYR A N     1 
ATOM   2876  C CA    . TYR A  1 404  ? -47.032 44.478  88.166  1.00 29.53 ? 402  TYR A CA    1 
ATOM   2877  C C     . TYR A  1 404  ? -48.186 43.496  87.978  1.00 28.57 ? 402  TYR A C     1 
ATOM   2878  O O     . TYR A  1 404  ? -49.245 43.863  87.464  1.00 26.74 ? 402  TYR A O     1 
ATOM   2879  C CB    . TYR A  1 404  ? -45.906 44.208  87.161  1.00 26.94 ? 402  TYR A CB    1 
ATOM   2880  C CG    . TYR A  1 404  ? -46.242 44.543  85.715  1.00 28.44 ? 402  TYR A CG    1 
ATOM   2881  C CD1   . TYR A  1 404  ? -47.016 43.684  84.935  1.00 27.24 ? 402  TYR A CD1   1 
ATOM   2882  C CD2   . TYR A  1 404  ? -45.783 45.711  85.133  1.00 27.75 ? 402  TYR A CD2   1 
ATOM   2883  C CE1   . TYR A  1 404  ? -47.320 43.990  83.616  1.00 29.77 ? 402  TYR A CE1   1 
ATOM   2884  C CE2   . TYR A  1 404  ? -46.071 46.015  83.813  1.00 24.28 ? 402  TYR A CE2   1 
ATOM   2885  C CZ    . TYR A  1 404  ? -46.838 45.157  83.062  1.00 23.54 ? 402  TYR A CZ    1 
ATOM   2886  O OH    . TYR A  1 404  ? -47.131 45.490  81.756  1.00 22.83 ? 402  TYR A OH    1 
ATOM   2887  N N     . ILE A  1 405  ? -48.006 42.245  88.416  1.00 27.61 ? 403  ILE A N     1 
ATOM   2888  C CA    . ILE A  1 405  ? -49.036 41.236  88.207  1.00 30.44 ? 403  ILE A CA    1 
ATOM   2889  C C     . ILE A  1 405  ? -50.281 41.564  89.030  1.00 28.96 ? 403  ILE A C     1 
ATOM   2890  O O     . ILE A  1 405  ? -51.411 41.412  88.548  1.00 27.97 ? 403  ILE A O     1 
ATOM   2891  C CB    . ILE A  1 405  ? -48.469 39.834  88.510  1.00 32.58 ? 403  ILE A CB    1 
ATOM   2892  C CG1   . ILE A  1 405  ? -47.399 39.476  87.467  1.00 35.42 ? 403  ILE A CG1   1 
ATOM   2893  C CG2   . ILE A  1 405  ? -49.553 38.785  88.494  1.00 33.59 ? 403  ILE A CG2   1 
ATOM   2894  C CD1   . ILE A  1 405  ? -46.468 38.313  87.860  1.00 36.52 ? 403  ILE A CD1   1 
ATOM   2895  N N     . ALA A  1 406  ? -50.097 42.078  90.257  1.00 30.35 ? 404  ALA A N     1 
ATOM   2896  C CA    . ALA A  1 406  ? -51.248 42.485  91.072  1.00 30.50 ? 404  ALA A CA    1 
ATOM   2897  C C     . ALA A  1 406  ? -52.006 43.638  90.432  1.00 28.54 ? 404  ALA A C     1 
ATOM   2898  O O     . ALA A  1 406  ? -53.239 43.696  90.494  1.00 31.56 ? 404  ALA A O     1 
ATOM   2899  C CB    . ALA A  1 406  ? -50.800 42.903  92.471  1.00 30.82 ? 404  ALA A CB    1 
ATOM   2900  N N     . CYS A  1 407  ? -51.280 44.606  89.885  1.00 30.04 ? 405  CYS A N     1 
ATOM   2901  C CA    . CYS A  1 407  ? -51.938 45.738  89.249  1.00 27.61 ? 405  CYS A CA    1 
ATOM   2902  C C     . CYS A  1 407  ? -52.623 45.323  87.953  1.00 30.24 ? 405  CYS A C     1 
ATOM   2903  O O     . CYS A  1 407  ? -53.681 45.860  87.613  1.00 28.82 ? 405  CYS A O     1 
ATOM   2904  C CB    . CYS A  1 407  ? -50.908 46.843  89.026  1.00 27.08 ? 405  CYS A CB    1 
ATOM   2905  S SG    . CYS A  1 407  ? -50.469 47.637  90.606  1.00 34.71 ? 405  CYS A SG    1 
ATOM   2906  N N     . ALA A  1 408  ? -52.062 44.342  87.245  1.00 30.65 ? 406  ALA A N     1 
ATOM   2907  C CA    . ALA A  1 408  ? -52.739 43.805  86.072  1.00 32.17 ? 406  ALA A CA    1 
ATOM   2908  C C     . ALA A  1 408  ? -54.053 43.140  86.458  1.00 29.21 ? 406  ALA A C     1 
ATOM   2909  O O     . ALA A  1 408  ? -55.045 43.241  85.729  1.00 29.30 ? 406  ALA A O     1 
ATOM   2910  C CB    . ALA A  1 408  ? -51.818 42.828  85.338  1.00 31.06 ? 406  ALA A CB    1 
ATOM   2911  N N     . ALA A  1 409  ? -54.090 42.470  87.612  1.00 30.33 ? 407  ALA A N     1 
ATOM   2912  C CA    . ALA A  1 409  ? -55.338 41.862  88.059  1.00 33.69 ? 407  ALA A CA    1 
ATOM   2913  C C     . ALA A  1 409  ? -56.388 42.924  88.343  1.00 32.19 ? 407  ALA A C     1 
ATOM   2914  O O     . ALA A  1 409  ? -57.569 42.741  88.027  1.00 30.35 ? 407  ALA A O     1 
ATOM   2915  C CB    . ALA A  1 409  ? -55.102 40.989  89.295  1.00 33.15 ? 407  ALA A CB    1 
ATOM   2916  N N     . LYS A  1 410  ? -55.976 44.050  88.926  1.00 28.42 ? 408  LYS A N     1 
ATOM   2917  C CA    . LYS A  1 410  ? -56.925 45.120  89.191  1.00 25.59 ? 408  LYS A CA    1 
ATOM   2918  C C     . LYS A  1 410  ? -57.417 45.736  87.890  1.00 29.51 ? 408  LYS A C     1 
ATOM   2919  O O     . LYS A  1 410  ? -58.608 46.045  87.751  1.00 30.23 ? 408  LYS A O     1 
ATOM   2920  C CB    . LYS A  1 410  ? -56.276 46.178  90.084  1.00 26.59 ? 408  LYS A CB    1 
ATOM   2921  C CG    . LYS A  1 410  ? -57.227 47.304  90.530  1.00 28.87 ? 408  LYS A CG    1 
ATOM   2922  C CD    . LYS A  1 410  ? -56.438 48.458  91.152  1.00 32.14 ? 408  LYS A CD    1 
ATOM   2923  C CE    . LYS A  1 410  ? -55.880 48.089  92.521  1.00 31.80 ? 408  LYS A CE    1 
ATOM   2924  N NZ    . LYS A  1 410  ? -57.002 47.916  93.468  1.00 30.53 ? 408  LYS A NZ    1 
ATOM   2925  N N     . LEU A  1 411  ? -56.507 45.928  86.925  1.00 27.21 ? 409  LEU A N     1 
ATOM   2926  C CA    . LEU A  1 411  ? -56.895 46.508  85.643  1.00 25.69 ? 409  LEU A CA    1 
ATOM   2927  C C     . LEU A  1 411  ? -57.837 45.589  84.871  1.00 27.51 ? 409  LEU A C     1 
ATOM   2928  O O     . LEU A  1 411  ? -58.810 46.052  84.266  1.00 26.13 ? 409  LEU A O     1 
ATOM   2929  C CB    . LEU A  1 411  ? -55.648 46.812  84.811  1.00 25.60 ? 409  LEU A CB    1 
ATOM   2930  C CG    . LEU A  1 411  ? -54.921 48.103  85.159  1.00 26.59 ? 409  LEU A CG    1 
ATOM   2931  C CD1   . LEU A  1 411  ? -53.507 48.105  84.572  1.00 28.00 ? 409  LEU A CD1   1 
ATOM   2932  C CD2   . LEU A  1 411  ? -55.706 49.327  84.700  1.00 23.58 ? 409  LEU A CD2   1 
ATOM   2933  N N     . LEU A  1 412  ? -57.550 44.286  84.868  1.00 28.05 ? 410  LEU A N     1 
ATOM   2934  C CA    . LEU A  1 412  ? -58.376 43.335  84.136  1.00 28.37 ? 410  LEU A CA    1 
ATOM   2935  C C     . LEU A  1 412  ? -59.759 43.191  84.735  1.00 29.53 ? 410  LEU A C     1 
ATOM   2936  O O     . LEU A  1 412  ? -60.663 42.719  84.046  1.00 31.32 ? 410  LEU A O     1 
ATOM   2937  C CB    . LEU A  1 412  ? -57.687 41.969  84.082  1.00 30.03 ? 410  LEU A CB    1 
ATOM   2938  C CG    . LEU A  1 412  ? -56.542 41.901  83.063  1.00 28.94 ? 410  LEU A CG    1 
ATOM   2939  C CD1   . LEU A  1 412  ? -55.807 40.579  83.203  1.00 29.77 ? 410  LEU A CD1   1 
ATOM   2940  C CD2   . LEU A  1 412  ? -57.061 42.079  81.635  1.00 29.82 ? 410  LEU A CD2   1 
ATOM   2941  N N     . ALA A  1 413  ? -59.949 43.583  85.994  1.00 26.06 ? 411  ALA A N     1 
ATOM   2942  C CA    . ALA A  1 413  ? -61.298 43.632  86.545  1.00 30.86 ? 411  ALA A CA    1 
ATOM   2943  C C     . ALA A  1 413  ? -62.044 44.904  86.169  1.00 31.65 ? 411  ALA A C     1 
ATOM   2944  O O     . ALA A  1 413  ? -63.219 45.040  86.524  1.00 32.16 ? 411  ALA A O     1 
ATOM   2945  C CB    . ALA A  1 413  ? -61.260 43.497  88.070  1.00 28.33 ? 411  ALA A CB    1 
ATOM   2946  N N     . ALA A  1 414  ? -61.412 45.828  85.441  1.00 33.27 ? 412  ALA A N     1 
ATOM   2947  C CA    . ALA A  1 414  ? -62.056 47.098  85.124  1.00 31.89 ? 412  ALA A CA    1 
ATOM   2948  C C     . ALA A  1 414  ? -61.999 47.430  83.635  1.00 31.54 ? 412  ALA A C     1 
ATOM   2949  O O     . ALA A  1 414  ? -62.109 48.609  83.268  1.00 26.48 ? 412  ALA A O     1 
ATOM   2950  C CB    . ALA A  1 414  ? -61.429 48.225  85.944  1.00 30.43 ? 412  ALA A CB    1 
ATOM   2951  N N     . THR A  1 415  ? -61.862 46.415  82.770  1.00 29.46 ? 413  THR A N     1 
ATOM   2952  C CA    . THR A  1 415  ? -61.815 46.646  81.327  1.00 28.11 ? 413  THR A CA    1 
ATOM   2953  C C     . THR A  1 415  ? -63.058 47.345  80.798  1.00 32.53 ? 413  THR A C     1 
ATOM   2954  O O     . THR A  1 415  ? -63.021 47.892  79.693  1.00 31.12 ? 413  THR A O     1 
ATOM   2955  C CB    . THR A  1 415  ? -61.625 45.332  80.560  1.00 31.32 ? 413  THR A CB    1 
ATOM   2956  O OG1   . THR A  1 415  ? -62.686 44.427  80.873  1.00 31.69 ? 413  THR A OG1   1 
ATOM   2957  C CG2   . THR A  1 415  ? -60.277 44.684  80.890  1.00 29.73 ? 413  THR A CG2   1 
ATOM   2958  N N     . ASP A  1 416  ? -64.160 47.339  81.544  1.00 32.55 ? 414  ASP A N     1 
ATOM   2959  C CA    . ASP A  1 416  ? -65.331 48.055  81.057  1.00 36.12 ? 414  ASP A CA    1 
ATOM   2960  C C     . ASP A  1 416  ? -65.145 49.565  81.154  1.00 33.58 ? 414  ASP A C     1 
ATOM   2961  O O     . ASP A  1 416  ? -65.727 50.304  80.358  1.00 34.85 ? 414  ASP A O     1 
ATOM   2962  C CB    . ASP A  1 416  ? -66.584 47.601  81.817  1.00 38.80 ? 414  ASP A CB    1 
ATOM   2963  C CG    . ASP A  1 416  ? -66.519 47.929  83.291  1.00 42.13 ? 414  ASP A CG    1 
ATOM   2964  O OD1   . ASP A  1 416  ? -65.465 47.675  83.919  1.00 42.05 ? 414  ASP A OD1   1 
ATOM   2965  O OD2   . ASP A  1 416  ? -67.514 48.469  83.815  1.00 47.76 ? 414  ASP A OD2   1 
ATOM   2966  N N     . VAL A  1 417  ? -64.307 50.048  82.069  1.00 32.48 ? 415  VAL A N     1 
ATOM   2967  C CA    . VAL A  1 417  ? -64.145 51.487  82.244  1.00 33.98 ? 415  VAL A CA    1 
ATOM   2968  C C     . VAL A  1 417  ? -62.750 51.999  81.903  1.00 29.15 ? 415  VAL A C     1 
ATOM   2969  O O     . VAL A  1 417  ? -62.602 53.213  81.697  1.00 29.42 ? 415  VAL A O     1 
ATOM   2970  C CB    . VAL A  1 417  ? -64.535 51.925  83.671  1.00 34.21 ? 415  VAL A CB    1 
ATOM   2971  C CG1   . VAL A  1 417  ? -66.007 51.629  83.918  1.00 39.03 ? 415  VAL A CG1   1 
ATOM   2972  C CG2   . VAL A  1 417  ? -63.664 51.244  84.697  1.00 34.55 ? 415  VAL A CG2   1 
ATOM   2973  N N     . VAL A  1 418  ? -61.708 51.156  81.881  1.00 27.89 ? 416  VAL A N     1 
ATOM   2974  C CA    . VAL A  1 418  ? -60.386 51.566  81.413  1.00 25.39 ? 416  VAL A CA    1 
ATOM   2975  C C     . VAL A  1 418  ? -59.923 50.590  80.340  1.00 24.82 ? 416  VAL A C     1 
ATOM   2976  O O     . VAL A  1 418  ? -60.441 49.482  80.199  1.00 28.00 ? 416  VAL A O     1 
ATOM   2977  C CB    . VAL A  1 418  ? -59.309 51.661  82.531  1.00 24.50 ? 416  VAL A CB    1 
ATOM   2978  C CG1   . VAL A  1 418  ? -59.632 52.781  83.515  1.00 26.15 ? 416  VAL A CG1   1 
ATOM   2979  C CG2   . VAL A  1 418  ? -59.105 50.318  83.257  1.00 24.87 ? 416  VAL A CG2   1 
ATOM   2980  N N     . PHE A  1 419  ? -58.926 51.020  79.585  1.00 23.07 ? 417  PHE A N     1 
ATOM   2981  C CA    . PHE A  1 419  ? -58.302 50.192  78.558  1.00 23.71 ? 417  PHE A CA    1 
ATOM   2982  C C     . PHE A  1 419  ? -56.898 49.843  79.017  1.00 22.19 ? 417  PHE A C     1 
ATOM   2983  O O     . PHE A  1 419  ? -55.981 50.677  78.889  1.00 23.44 ? 417  PHE A O     1 
ATOM   2984  C CB    . PHE A  1 419  ? -58.256 50.942  77.220  1.00 24.48 ? 417  PHE A CB    1 
ATOM   2985  C CG    . PHE A  1 419  ? -57.522 50.201  76.126  1.00 26.34 ? 417  PHE A CG    1 
ATOM   2986  C CD1   . PHE A  1 419  ? -57.953 48.951  75.708  1.00 25.75 ? 417  PHE A CD1   1 
ATOM   2987  C CD2   . PHE A  1 419  ? -56.410 50.759  75.510  1.00 23.67 ? 417  PHE A CD2   1 
ATOM   2988  C CE1   . PHE A  1 419  ? -57.289 48.269  74.697  1.00 26.86 ? 417  PHE A CE1   1 
ATOM   2989  C CE2   . PHE A  1 419  ? -55.744 50.085  74.499  1.00 22.00 ? 417  PHE A CE2   1 
ATOM   2990  C CZ    . PHE A  1 419  ? -56.180 48.834  74.094  1.00 26.76 ? 417  PHE A CZ    1 
ATOM   2991  N N     . PRO A  1 420  ? -56.664 48.652  79.579  1.00 23.42 ? 418  PRO A N     1 
ATOM   2992  C CA    . PRO A  1 420  ? -55.310 48.336  80.067  1.00 23.80 ? 418  PRO A CA    1 
ATOM   2993  C C     . PRO A  1 420  ? -54.359 48.034  78.921  1.00 24.65 ? 418  PRO A C     1 
ATOM   2994  O O     . PRO A  1 420  ? -54.733 47.406  77.924  1.00 22.14 ? 418  PRO A O     1 
ATOM   2995  C CB    . PRO A  1 420  ? -55.518 47.096  80.954  1.00 20.89 ? 418  PRO A CB    1 
ATOM   2996  C CG    . PRO A  1 420  ? -57.009 46.962  81.136  1.00 24.53 ? 418  PRO A CG    1 
ATOM   2997  C CD    . PRO A  1 420  ? -57.610 47.567  79.880  1.00 25.30 ? 418  PRO A CD    1 
ATOM   2998  N N     . GLN A  1 421  ? -53.109 48.479  79.097  1.00 21.00 ? 419  GLN A N     1 
ATOM   2999  C CA    . GLN A  1 421  ? -52.032 48.317  78.130  1.00 22.19 ? 419  GLN A CA    1 
ATOM   3000  C C     . GLN A  1 421  ? -50.822 47.801  78.892  1.00 22.72 ? 419  GLN A C     1 
ATOM   3001  O O     . GLN A  1 421  ? -50.210 48.544  79.666  1.00 23.60 ? 419  GLN A O     1 
ATOM   3002  C CB    . GLN A  1 421  ? -51.723 49.642  77.436  1.00 22.96 ? 419  GLN A CB    1 
ATOM   3003  C CG    . GLN A  1 421  ? -52.956 50.259  76.788  1.00 24.34 ? 419  GLN A CG    1 
ATOM   3004  C CD    . GLN A  1 421  ? -52.762 51.716  76.429  1.00 24.96 ? 419  GLN A CD    1 
ATOM   3005  O OE1   . GLN A  1 421  ? -52.600 52.558  77.308  1.00 23.35 ? 419  GLN A OE1   1 
ATOM   3006  N NE2   . GLN A  1 421  ? -52.763 52.018  75.133  1.00 26.13 ? 419  GLN A NE2   1 
ATOM   3007  N N     . PHE A  1 422  ? -50.504 46.531  78.708  1.00 22.81 ? 420  PHE A N     1 
ATOM   3008  C CA    . PHE A  1 422  ? -49.484 45.881  79.525  1.00 26.34 ? 420  PHE A CA    1 
ATOM   3009  C C     . PHE A  1 422  ? -48.152 45.959  78.796  1.00 24.69 ? 420  PHE A C     1 
ATOM   3010  O O     . PHE A  1 422  ? -47.849 45.133  77.928  1.00 25.49 ? 420  PHE A O     1 
ATOM   3011  C CB    . PHE A  1 422  ? -49.898 44.451  79.837  1.00 28.06 ? 420  PHE A CB    1 
ATOM   3012  C CG    . PHE A  1 422  ? -51.178 44.383  80.597  1.00 25.01 ? 420  PHE A CG    1 
ATOM   3013  C CD1   . PHE A  1 422  ? -51.237 44.868  81.893  1.00 26.98 ? 420  PHE A CD1   1 
ATOM   3014  C CD2   . PHE A  1 422  ? -52.325 43.894  80.006  1.00 26.29 ? 420  PHE A CD2   1 
ATOM   3015  C CE1   . PHE A  1 422  ? -52.419 44.843  82.602  1.00 28.11 ? 420  PHE A CE1   1 
ATOM   3016  C CE2   . PHE A  1 422  ? -53.517 43.857  80.708  1.00 28.89 ? 420  PHE A CE2   1 
ATOM   3017  C CZ    . PHE A  1 422  ? -53.562 44.329  82.011  1.00 27.05 ? 420  PHE A CZ    1 
ATOM   3018  N N     . ALA A  1 423  ? -47.348 46.950  79.167  1.00 24.68 ? 421  ALA A N     1 
ATOM   3019  C CA    . ALA A  1 423  ? -46.062 47.185  78.526  1.00 26.75 ? 421  ALA A CA    1 
ATOM   3020  C C     . ALA A  1 423  ? -45.035 46.306  79.220  1.00 26.61 ? 421  ALA A C     1 
ATOM   3021  O O     . ALA A  1 423  ? -44.718 46.525  80.393  1.00 27.79 ? 421  ALA A O     1 
ATOM   3022  C CB    . ALA A  1 423  ? -45.669 48.658  78.619  1.00 25.86 ? 421  ALA A CB    1 
ATOM   3023  N N     . THR A  1 424  ? -44.516 45.315  78.510  1.00 25.94 ? 422  THR A N     1 
ATOM   3024  C CA    . THR A  1 424  ? -43.491 44.487  79.140  1.00 26.61 ? 422  THR A CA    1 
ATOM   3025  C C     . THR A  1 424  ? -42.838 43.608  78.085  1.00 31.28 ? 422  THR A C     1 
ATOM   3026  O O     . THR A  1 424  ? -43.492 43.168  77.127  1.00 26.33 ? 422  THR A O     1 
ATOM   3027  C CB    . THR A  1 424  ? -44.068 43.611  80.266  1.00 30.70 ? 422  THR A CB    1 
ATOM   3028  O OG1   . THR A  1 424  ? -43.009 42.863  80.880  1.00 32.88 ? 422  THR A OG1   1 
ATOM   3029  C CG2   . THR A  1 424  ? -45.124 42.658  79.727  1.00 30.49 ? 422  THR A CG2   1 
ATOM   3030  N N     . HIS A  1 425  ? -41.542 43.362  78.277  1.00 27.54 ? 423  HIS A N     1 
ATOM   3031  C CA    . HIS A  1 425  ? -40.796 42.401  77.483  1.00 31.60 ? 423  HIS A CA    1 
ATOM   3032  C C     . HIS A  1 425  ? -40.577 41.090  78.209  1.00 33.42 ? 423  HIS A C     1 
ATOM   3033  O O     . HIS A  1 425  ? -39.942 40.188  77.656  1.00 37.03 ? 423  HIS A O     1 
ATOM   3034  C CB    . HIS A  1 425  ? -39.447 42.992  77.086  1.00 28.34 ? 423  HIS A CB    1 
ATOM   3035  C CG    . HIS A  1 425  ? -39.566 44.241  76.280  1.00 30.00 ? 423  HIS A CG    1 
ATOM   3036  N ND1   . HIS A  1 425  ? -38.907 45.407  76.608  1.00 32.69 ? 423  HIS A ND1   1 
ATOM   3037  C CD2   . HIS A  1 425  ? -40.288 44.513  75.170  1.00 32.47 ? 423  HIS A CD2   1 
ATOM   3038  C CE1   . HIS A  1 425  ? -39.208 46.340  75.723  1.00 32.79 ? 423  HIS A CE1   1 
ATOM   3039  N NE2   . HIS A  1 425  ? -40.051 45.826  74.845  1.00 30.66 ? 423  HIS A NE2   1 
ATOM   3040  N N     . ASN A  1 426  ? -41.090 40.966  79.424  1.00 32.24 ? 424  ASN A N     1 
ATOM   3041  C CA    . ASN A  1 426  ? -40.868 39.788  80.253  1.00 36.83 ? 424  ASN A CA    1 
ATOM   3042  C C     . ASN A  1 426  ? -41.901 38.727  79.892  1.00 36.67 ? 424  ASN A C     1 
ATOM   3043  O O     . ASN A  1 426  ? -43.082 38.872  80.216  1.00 37.66 ? 424  ASN A O     1 
ATOM   3044  C CB    . ASN A  1 426  ? -40.959 40.188  81.720  1.00 36.42 ? 424  ASN A CB    1 
ATOM   3045  C CG    . ASN A  1 426  ? -40.620 39.052  82.661  1.00 36.48 ? 424  ASN A CG    1 
ATOM   3046  O OD1   . ASN A  1 426  ? -41.080 37.923  82.490  1.00 36.08 ? 424  ASN A OD1   1 
ATOM   3047  N ND2   . ASN A  1 426  ? -39.814 39.355  83.672  1.00 33.87 ? 424  ASN A ND2   1 
ATOM   3048  N N     . ALA A  1 427  ? -41.458 37.648  79.240  1.00 34.56 ? 425  ALA A N     1 
ATOM   3049  C CA    . ALA A  1 427  ? -42.385 36.629  78.753  1.00 33.37 ? 425  ALA A CA    1 
ATOM   3050  C C     . ALA A  1 427  ? -43.125 35.910  79.877  1.00 36.94 ? 425  ALA A C     1 
ATOM   3051  O O     . ALA A  1 427  ? -44.216 35.383  79.639  1.00 36.08 ? 425  ALA A O     1 
ATOM   3052  C CB    . ALA A  1 427  ? -41.638 35.605  77.892  1.00 41.83 ? 425  ALA A CB    1 
ATOM   3053  N N     . GLN A  1 428  ? -42.557 35.876  81.087  1.00 37.51 ? 426  GLN A N     1 
ATOM   3054  C CA    . GLN A  1 428  ? -43.260 35.298  82.228  1.00 38.29 ? 426  GLN A CA    1 
ATOM   3055  C C     . GLN A  1 428  ? -44.405 36.199  82.661  1.00 37.18 ? 426  GLN A C     1 
ATOM   3056  O O     . GLN A  1 428  ? -45.510 35.717  82.943  1.00 37.43 ? 426  GLN A O     1 
ATOM   3057  C CB    . GLN A  1 428  ? -42.294 35.069  83.395  1.00 35.34 ? 426  GLN A CB    1 
ATOM   3058  C CG    . GLN A  1 428  ? -42.827 34.138  84.491  1.00 38.93 ? 426  GLN A CG    1 
ATOM   3059  C CD    . GLN A  1 428  ? -43.874 34.793  85.381  1.00 42.37 ? 426  GLN A CD    1 
ATOM   3060  O OE1   . GLN A  1 428  ? -43.833 35.999  85.626  1.00 42.63 ? 426  GLN A OE1   1 
ATOM   3061  N NE2   . GLN A  1 428  ? -44.822 34.000  85.858  1.00 39.96 ? 426  GLN A NE2   1 
ATOM   3062  N N     . THR A  1 429  ? -44.142 37.508  82.730  1.00 38.96 ? 427  THR A N     1 
ATOM   3063  C CA    . THR A  1 429  ? -45.184 38.488  83.015  1.00 38.97 ? 427  THR A CA    1 
ATOM   3064  C C     . THR A  1 429  ? -46.281 38.433  81.957  1.00 37.03 ? 427  THR A C     1 
ATOM   3065  O O     . THR A  1 429  ? -47.473 38.406  82.279  1.00 35.11 ? 427  THR A O     1 
ATOM   3066  C CB    . THR A  1 429  ? -44.567 39.886  83.079  1.00 34.60 ? 427  THR A CB    1 
ATOM   3067  O OG1   . THR A  1 429  ? -43.413 39.868  83.929  1.00 37.49 ? 427  THR A OG1   1 
ATOM   3068  C CG2   . THR A  1 429  ? -45.560 40.894  83.627  1.00 33.90 ? 427  THR A CG2   1 
ATOM   3069  N N     . LEU A  1 430  ? -45.885 38.419  80.681  1.00 33.77 ? 428  LEU A N     1 
ATOM   3070  C CA    . LEU A  1 430  ? -46.831 38.301  79.578  1.00 35.69 ? 428  LEU A CA    1 
ATOM   3071  C C     . LEU A  1 430  ? -47.750 37.099  79.758  1.00 38.19 ? 428  LEU A C     1 
ATOM   3072  O O     . LEU A  1 430  ? -48.981 37.231  79.744  1.00 34.40 ? 428  LEU A O     1 
ATOM   3073  C CB    . LEU A  1 430  ? -46.059 38.198  78.260  1.00 34.89 ? 428  LEU A CB    1 
ATOM   3074  C CG    . LEU A  1 430  ? -46.763 38.496  76.934  1.00 36.08 ? 428  LEU A CG    1 
ATOM   3075  C CD1   . LEU A  1 430  ? -45.722 38.571  75.834  1.00 39.00 ? 428  LEU A CD1   1 
ATOM   3076  C CD2   . LEU A  1 430  ? -47.796 37.455  76.582  1.00 33.70 ? 428  LEU A CD2   1 
ATOM   3077  N N     . ALA A  1 431  ? -47.150 35.913  79.919  1.00 36.80 ? 429  ALA A N     1 
ATOM   3078  C CA    . ALA A  1 431  ? -47.913 34.672  80.023  1.00 37.33 ? 429  ALA A CA    1 
ATOM   3079  C C     . ALA A  1 431  ? -48.891 34.714  81.188  1.00 36.04 ? 429  ALA A C     1 
ATOM   3080  O O     . ALA A  1 431  ? -50.042 34.270  81.062  1.00 35.56 ? 429  ALA A O     1 
ATOM   3081  C CB    . ALA A  1 431  ? -46.950 33.493  80.185  1.00 38.73 ? 429  ALA A CB    1 
ATOM   3082  N N     . ALA A  1 432  ? -48.445 35.242  82.331  1.00 34.70 ? 430  ALA A N     1 
ATOM   3083  C CA    . ALA A  1 432  ? -49.304 35.311  83.509  1.00 39.61 ? 430  ALA A CA    1 
ATOM   3084  C C     . ALA A  1 432  ? -50.546 36.150  83.236  1.00 35.63 ? 430  ALA A C     1 
ATOM   3085  O O     . ALA A  1 432  ? -51.661 35.772  83.622  1.00 37.42 ? 430  ALA A O     1 
ATOM   3086  C CB    . ALA A  1 432  ? -48.518 35.876  84.692  1.00 34.95 ? 430  ALA A CB    1 
ATOM   3087  N N     . ILE A  1 433  ? -50.373 37.276  82.541  1.00 36.35 ? 431  ILE A N     1 
ATOM   3088  C CA    . ILE A  1 433  ? -51.488 38.176  82.256  1.00 35.38 ? 431  ILE A CA    1 
ATOM   3089  C C     . ILE A  1 433  ? -52.393 37.588  81.184  1.00 35.15 ? 431  ILE A C     1 
ATOM   3090  O O     . ILE A  1 433  ? -53.624 37.689  81.268  1.00 36.72 ? 431  ILE A O     1 
ATOM   3091  C CB    . ILE A  1 433  ? -50.940 39.561  81.861  1.00 34.16 ? 431  ILE A CB    1 
ATOM   3092  C CG1   . ILE A  1 433  ? -50.241 40.190  83.065  1.00 34.67 ? 431  ILE A CG1   1 
ATOM   3093  C CG2   . ILE A  1 433  ? -52.045 40.467  81.308  1.00 32.06 ? 431  ILE A CG2   1 
ATOM   3094  C CD1   . ILE A  1 433  ? -49.464 41.401  82.742  1.00 33.43 ? 431  ILE A CD1   1 
ATOM   3095  N N     . TYR A  1 434  ? -51.803 36.945  80.175  1.00 33.92 ? 432  TYR A N     1 
ATOM   3096  C CA    . TYR A  1 434  ? -52.588 36.333  79.108  1.00 36.24 ? 432  TYR A CA    1 
ATOM   3097  C C     . TYR A  1 434  ? -53.577 35.316  79.668  1.00 37.23 ? 432  TYR A C     1 
ATOM   3098  O O     . TYR A  1 434  ? -54.757 35.314  79.304  1.00 37.11 ? 432  TYR A O     1 
ATOM   3099  C CB    . TYR A  1 434  ? -51.641 35.691  78.089  1.00 35.94 ? 432  TYR A CB    1 
ATOM   3100  C CG    . TYR A  1 434  ? -52.300 34.791  77.073  1.00 38.90 ? 432  TYR A CG    1 
ATOM   3101  C CD1   . TYR A  1 434  ? -53.118 35.310  76.072  1.00 37.29 ? 432  TYR A CD1   1 
ATOM   3102  C CD2   . TYR A  1 434  ? -52.083 33.417  77.099  1.00 40.18 ? 432  TYR A CD2   1 
ATOM   3103  C CE1   . TYR A  1 434  ? -53.716 34.475  75.132  1.00 40.09 ? 432  TYR A CE1   1 
ATOM   3104  C CE2   . TYR A  1 434  ? -52.674 32.579  76.173  1.00 40.14 ? 432  TYR A CE2   1 
ATOM   3105  C CZ    . TYR A  1 434  ? -53.486 33.107  75.192  1.00 43.49 ? 432  TYR A CZ    1 
ATOM   3106  O OH    . TYR A  1 434  ? -54.065 32.256  74.275  1.00 43.77 ? 432  TYR A OH    1 
ATOM   3107  N N     . HIS A  1 435  ? -53.120 34.454  80.578  1.00 37.94 ? 433  HIS A N     1 
ATOM   3108  C CA    . HIS A  1 435  ? -54.031 33.473  81.162  1.00 37.29 ? 433  HIS A CA    1 
ATOM   3109  C C     . HIS A  1 435  ? -54.950 34.094  82.208  1.00 39.97 ? 433  HIS A C     1 
ATOM   3110  O O     . HIS A  1 435  ? -56.100 33.657  82.361  1.00 37.61 ? 433  HIS A O     1 
ATOM   3111  C CB    . HIS A  1 435  ? -53.237 32.315  81.764  1.00 41.51 ? 433  HIS A CB    1 
ATOM   3112  C CG    . HIS A  1 435  ? -52.619 31.420  80.735  1.00 42.45 ? 433  HIS A CG    1 
ATOM   3113  N ND1   . HIS A  1 435  ? -53.311 30.392  80.133  1.00 43.99 ? 433  HIS A ND1   1 
ATOM   3114  C CD2   . HIS A  1 435  ? -51.386 31.421  80.176  1.00 43.05 ? 433  HIS A CD2   1 
ATOM   3115  C CE1   . HIS A  1 435  ? -52.526 29.790  79.256  1.00 45.53 ? 433  HIS A CE1   1 
ATOM   3116  N NE2   . HIS A  1 435  ? -51.351 30.394  79.265  1.00 40.96 ? 433  HIS A NE2   1 
ATOM   3117  N N     . MET A  1 436  ? -54.463 35.096  82.942  1.00 38.19 ? 434  MET A N     1 
ATOM   3118  C CA    . MET A  1 436  ? -55.318 35.808  83.883  1.00 37.61 ? 434  MET A CA    1 
ATOM   3119  C C     . MET A  1 436  ? -56.488 36.467  83.169  1.00 37.37 ? 434  MET A C     1 
ATOM   3120  O O     . MET A  1 436  ? -57.600 36.515  83.705  1.00 41.35 ? 434  MET A O     1 
ATOM   3121  C CB    . MET A  1 436  ? -54.504 36.852  84.644  1.00 36.52 ? 434  MET A CB    1 
ATOM   3122  C CG    . MET A  1 436  ? -55.307 37.640  85.655  1.00 39.42 ? 434  MET A CG    1 
ATOM   3123  S SD    . MET A  1 436  ? -54.360 38.995  86.388  1.00 37.92 ? 434  MET A SD    1 
ATOM   3124  C CE    . MET A  1 436  ? -53.136 38.117  87.364  1.00 38.14 ? 434  MET A CE    1 
ATOM   3125  N N     . ALA A  1 437  ? -56.258 36.981  81.958  1.00 35.35 ? 435  ALA A N     1 
ATOM   3126  C CA    . ALA A  1 437  ? -57.317 37.671  81.230  1.00 40.16 ? 435  ALA A CA    1 
ATOM   3127  C C     . ALA A  1 437  ? -58.419 36.726  80.766  1.00 42.77 ? 435  ALA A C     1 
ATOM   3128  O O     . ALA A  1 437  ? -59.534 37.181  80.477  1.00 38.98 ? 435  ALA A O     1 
ATOM   3129  C CB    . ALA A  1 437  ? -56.728 38.421  80.034  1.00 37.73 ? 435  ALA A CB    1 
ATOM   3130  N N     . GLY A  1 438  ? -58.144 35.425  80.698  1.00 42.99 ? 436  GLY A N     1 
ATOM   3131  C CA    . GLY A  1 438  ? -59.173 34.470  80.348  1.00 45.83 ? 436  GLY A CA    1 
ATOM   3132  C C     . GLY A  1 438  ? -59.434 34.409  78.855  1.00 45.25 ? 436  GLY A C     1 
ATOM   3133  O O     . GLY A  1 438  ? -58.723 34.994  78.040  1.00 38.83 ? 436  GLY A O     1 
ATOM   3134  N N     . LYS A  1 439  ? -60.521 33.711  78.506  1.00 48.20 ? 437  LYS A N     1 
ATOM   3135  C CA    . LYS A  1 439  ? -60.768 33.287  77.132  1.00 45.81 ? 437  LYS A CA    1 
ATOM   3136  C C     . LYS A  1 439  ? -61.465 34.333  76.267  1.00 47.20 ? 437  LYS A C     1 
ATOM   3137  O O     . LYS A  1 439  ? -61.262 34.341  75.048  1.00 48.50 ? 437  LYS A O     1 
ATOM   3138  C CB    . LYS A  1 439  ? -61.602 31.999  77.130  1.00 50.96 ? 437  LYS A CB    1 
ATOM   3139  N N     . ASP A  1 440  ? -62.285 35.205  76.849  1.00 44.31 ? 438  ASP A N     1 
ATOM   3140  C CA    . ASP A  1 440  ? -63.036 36.184  76.069  1.00 45.77 ? 438  ASP A CA    1 
ATOM   3141  C C     . ASP A  1 440  ? -62.139 37.355  75.701  1.00 45.12 ? 438  ASP A C     1 
ATOM   3142  O O     . ASP A  1 440  ? -61.604 38.029  76.587  1.00 42.09 ? 438  ASP A O     1 
ATOM   3143  C CB    . ASP A  1 440  ? -64.244 36.680  76.857  1.00 43.84 ? 438  ASP A CB    1 
ATOM   3144  C CG    . ASP A  1 440  ? -65.228 35.571  77.153  1.00 50.97 ? 438  ASP A CG    1 
ATOM   3145  O OD1   . ASP A  1 440  ? -65.141 34.530  76.469  1.00 47.51 ? 438  ASP A OD1   1 
ATOM   3146  O OD2   . ASP A  1 440  ? -66.081 35.741  78.053  1.00 50.75 ? 438  ASP A OD2   1 
ATOM   3147  N N     . PHE A  1 441  ? -61.986 37.613  74.404  1.00 38.96 ? 439  PHE A N     1 
ATOM   3148  C CA    . PHE A  1 441  ? -61.201 38.757  73.979  1.00 39.42 ? 439  PHE A CA    1 
ATOM   3149  C C     . PHE A  1 441  ? -61.834 39.427  72.772  1.00 38.92 ? 439  PHE A C     1 
ATOM   3150  O O     . PHE A  1 441  ? -62.390 38.764  71.895  1.00 34.39 ? 439  PHE A O     1 
ATOM   3151  C CB    . PHE A  1 441  ? -59.755 38.373  73.642  1.00 38.07 ? 439  PHE A CB    1 
ATOM   3152  C CG    . PHE A  1 441  ? -58.894 39.560  73.300  1.00 36.25 ? 439  PHE A CG    1 
ATOM   3153  C CD1   . PHE A  1 441  ? -58.353 40.348  74.302  1.00 36.22 ? 439  PHE A CD1   1 
ATOM   3154  C CD2   . PHE A  1 441  ? -58.669 39.914  71.982  1.00 33.99 ? 439  PHE A CD2   1 
ATOM   3155  C CE1   . PHE A  1 441  ? -57.576 41.462  73.992  1.00 30.60 ? 439  PHE A CE1   1 
ATOM   3156  C CE2   . PHE A  1 441  ? -57.912 41.024  71.667  1.00 35.20 ? 439  PHE A CE2   1 
ATOM   3157  C CZ    . PHE A  1 441  ? -57.366 41.795  72.680  1.00 33.84 ? 439  PHE A CZ    1 
ATOM   3158  N N     . HIS A  1 442  ? -61.725 40.749  72.736  1.00 34.28 ? 440  HIS A N     1 
ATOM   3159  C CA    . HIS A  1 442  ? -62.069 41.547  71.574  1.00 31.95 ? 440  HIS A CA    1 
ATOM   3160  C C     . HIS A  1 442  ? -61.075 42.691  71.503  1.00 37.12 ? 440  HIS A C     1 
ATOM   3161  O O     . HIS A  1 442  ? -60.537 43.114  72.528  1.00 32.42 ? 440  HIS A O     1 
ATOM   3162  C CB    . HIS A  1 442  ? -63.509 42.075  71.650  1.00 34.86 ? 440  HIS A CB    1 
ATOM   3163  C CG    . HIS A  1 442  ? -63.786 42.939  72.842  1.00 32.79 ? 440  HIS A CG    1 
ATOM   3164  N ND1   . HIS A  1 442  ? -63.635 44.311  72.822  1.00 34.77 ? 440  HIS A ND1   1 
ATOM   3165  C CD2   . HIS A  1 442  ? -64.232 42.627  74.084  1.00 33.46 ? 440  HIS A CD2   1 
ATOM   3166  C CE1   . HIS A  1 442  ? -63.968 44.808  74.001  1.00 31.86 ? 440  HIS A CE1   1 
ATOM   3167  N NE2   . HIS A  1 442  ? -64.336 43.808  74.784  1.00 37.15 ? 440  HIS A NE2   1 
ATOM   3168  N N     . VAL A  1 443  ? -60.807 43.174  70.289  1.00 37.01 ? 441  VAL A N     1 
ATOM   3169  C CA    . VAL A  1 443  ? -59.894 44.302  70.157  1.00 36.74 ? 441  VAL A CA    1 
ATOM   3170  C C     . VAL A  1 443  ? -60.521 45.506  70.843  1.00 35.41 ? 441  VAL A C     1 
ATOM   3171  O O     . VAL A  1 443  ? -61.711 45.786  70.664  1.00 33.83 ? 441  VAL A O     1 
ATOM   3172  C CB    . VAL A  1 443  ? -59.572 44.565  68.679  1.00 40.00 ? 441  VAL A CB    1 
ATOM   3173  C CG1   . VAL A  1 443  ? -59.144 46.003  68.476  1.00 36.81 ? 441  VAL A CG1   1 
ATOM   3174  C CG2   . VAL A  1 443  ? -58.471 43.626  68.222  1.00 41.46 ? 441  VAL A CG2   1 
ATOM   3175  N N     . GLY A  1 444  ? -59.732 46.202  71.669  1.00 33.28 ? 442  GLY A N     1 
ATOM   3176  C CA    . GLY A  1 444  ? -60.238 47.238  72.546  1.00 31.62 ? 442  GLY A CA    1 
ATOM   3177  C C     . GLY A  1 444  ? -60.445 46.814  73.991  1.00 29.06 ? 442  GLY A C     1 
ATOM   3178  O O     . GLY A  1 444  ? -60.653 47.681  74.849  1.00 28.33 ? 442  GLY A O     1 
ATOM   3179  N N     . LYS A  1 445  ? -60.400 45.517  74.291  1.00 29.30 ? 443  LYS A N     1 
ATOM   3180  C CA    . LYS A  1 445  ? -60.556 45.081  75.680  1.00 26.93 ? 443  LYS A CA    1 
ATOM   3181  C C     . LYS A  1 445  ? -59.296 45.385  76.482  1.00 28.93 ? 443  LYS A C     1 
ATOM   3182  O O     . LYS A  1 445  ? -59.359 45.981  77.566  1.00 25.60 ? 443  LYS A O     1 
ATOM   3183  C CB    . LYS A  1 445  ? -60.862 43.589  75.735  1.00 32.58 ? 443  LYS A CB    1 
ATOM   3184  C CG    . LYS A  1 445  ? -61.375 43.130  77.094  1.00 34.66 ? 443  LYS A CG    1 
ATOM   3185  C CD    . LYS A  1 445  ? -61.584 41.631  77.156  1.00 36.49 ? 443  LYS A CD    1 
ATOM   3186  C CE    . LYS A  1 445  ? -62.167 41.224  78.504  1.00 42.56 ? 443  LYS A CE    1 
ATOM   3187  N NZ    . LYS A  1 445  ? -62.552 39.770  78.578  1.00 41.00 ? 443  LYS A NZ    1 
ATOM   3188  N N     . TYR A  1 446  ? -58.147 44.950  75.971  1.00 27.44 ? 444  TYR A N     1 
ATOM   3189  C CA    . TYR A  1 446  ? -56.833 45.327  76.487  1.00 25.59 ? 444  TYR A CA    1 
ATOM   3190  C C     . TYR A  1 446  ? -55.816 45.067  75.383  1.00 27.94 ? 444  TYR A C     1 
ATOM   3191  O O     . TYR A  1 446  ? -56.140 44.508  74.332  1.00 28.00 ? 444  TYR A O     1 
ATOM   3192  C CB    . TYR A  1 446  ? -56.461 44.560  77.767  1.00 26.00 ? 444  TYR A CB    1 
ATOM   3193  C CG    . TYR A  1 446  ? -56.242 43.072  77.561  1.00 30.43 ? 444  TYR A CG    1 
ATOM   3194  C CD1   . TYR A  1 446  ? -55.001 42.563  77.198  1.00 31.93 ? 444  TYR A CD1   1 
ATOM   3195  C CD2   . TYR A  1 446  ? -57.292 42.175  77.719  1.00 36.81 ? 444  TYR A CD2   1 
ATOM   3196  C CE1   . TYR A  1 446  ? -54.820 41.191  77.008  1.00 37.10 ? 444  TYR A CE1   1 
ATOM   3197  C CE2   . TYR A  1 446  ? -57.115 40.823  77.534  1.00 33.44 ? 444  TYR A CE2   1 
ATOM   3198  C CZ    . TYR A  1 446  ? -55.894 40.337  77.175  1.00 37.49 ? 444  TYR A CZ    1 
ATOM   3199  O OH    . TYR A  1 446  ? -55.758 38.976  76.997  1.00 47.96 ? 444  TYR A OH    1 
ATOM   3200  N N     . GLU A  1 447  ? -54.572 45.466  75.633  1.00 26.31 ? 445  GLU A N     1 
ATOM   3201  C CA    . GLU A  1 447  ? -53.513 45.178  74.679  1.00 26.07 ? 445  GLU A CA    1 
ATOM   3202  C C     . GLU A  1 447  ? -52.210 45.004  75.438  1.00 26.47 ? 445  GLU A C     1 
ATOM   3203  O O     . GLU A  1 447  ? -52.105 45.348  76.616  1.00 27.05 ? 445  GLU A O     1 
ATOM   3204  C CB    . GLU A  1 447  ? -53.375 46.286  73.621  1.00 23.47 ? 445  GLU A CB    1 
ATOM   3205  C CG    . GLU A  1 447  ? -52.857 47.610  74.174  1.00 25.83 ? 445  GLU A CG    1 
ATOM   3206  C CD    . GLU A  1 447  ? -52.753 48.728  73.140  1.00 25.19 ? 445  GLU A CD    1 
ATOM   3207  O OE1   . GLU A  1 447  ? -53.301 48.592  72.027  1.00 25.58 ? 445  GLU A OE1   1 
ATOM   3208  O OE2   . GLU A  1 447  ? -52.117 49.765  73.445  1.00 29.77 ? 445  GLU A OE2   1 
ATOM   3209  N N     . PHE A  1 448  ? -51.221 44.454  74.746  1.00 24.15 ? 446  PHE A N     1 
ATOM   3210  C CA    . PHE A  1 448  ? -49.842 44.474  75.200  1.00 26.56 ? 446  PHE A CA    1 
ATOM   3211  C C     . PHE A  1 448  ? -49.103 45.606  74.497  1.00 26.93 ? 446  PHE A C     1 
ATOM   3212  O O     . PHE A  1 448  ? -49.590 46.180  73.523  1.00 28.63 ? 446  PHE A O     1 
ATOM   3213  C CB    . PHE A  1 448  ? -49.152 43.133  74.928  1.00 28.52 ? 446  PHE A CB    1 
ATOM   3214  C CG    . PHE A  1 448  ? -49.739 41.982  75.686  1.00 27.85 ? 446  PHE A CG    1 
ATOM   3215  C CD1   . PHE A  1 448  ? -49.411 41.769  77.014  1.00 30.09 ? 446  PHE A CD1   1 
ATOM   3216  C CD2   . PHE A  1 448  ? -50.621 41.102  75.067  1.00 29.37 ? 446  PHE A CD2   1 
ATOM   3217  C CE1   . PHE A  1 448  ? -49.966 40.705  77.720  1.00 30.92 ? 446  PHE A CE1   1 
ATOM   3218  C CE2   . PHE A  1 448  ? -51.168 40.033  75.761  1.00 31.39 ? 446  PHE A CE2   1 
ATOM   3219  C CZ    . PHE A  1 448  ? -50.838 39.833  77.090  1.00 34.40 ? 446  PHE A CZ    1 
ATOM   3220  N N     . GLN A  1 449  ? -47.921 45.941  75.018  1.00 26.14 ? 447  GLN A N     1 
ATOM   3221  C CA    . GLN A  1 449  ? -47.049 46.931  74.399  1.00 24.15 ? 447  GLN A CA    1 
ATOM   3222  C C     . GLN A  1 449  ? -45.596 46.504  74.559  1.00 27.94 ? 447  GLN A C     1 
ATOM   3223  O O     . GLN A  1 449  ? -45.233 45.795  75.504  1.00 25.55 ? 447  GLN A O     1 
ATOM   3224  C CB    . GLN A  1 449  ? -47.213 48.328  75.011  1.00 23.93 ? 447  GLN A CB    1 
ATOM   3225  C CG    . GLN A  1 449  ? -48.626 48.878  74.922  1.00 23.68 ? 447  GLN A CG    1 
ATOM   3226  C CD    . GLN A  1 449  ? -48.697 50.360  75.215  1.00 26.28 ? 447  GLN A CD    1 
ATOM   3227  O OE1   . GLN A  1 449  ? -47.749 50.963  75.735  1.00 27.58 ? 447  GLN A OE1   1 
ATOM   3228  N NE2   . GLN A  1 449  ? -49.812 50.963  74.868  1.00 26.02 ? 447  GLN A NE2   1 
ATOM   3229  N N     . CYS A  1 450  ? -44.762 46.977  73.635  1.00 27.87 ? 448  CYS A N     1 
ATOM   3230  C CA    . CYS A  1 450  ? -43.344 46.663  73.641  1.00 27.48 ? 448  CYS A CA    1 
ATOM   3231  C C     . CYS A  1 450  ? -42.584 47.845  73.062  1.00 27.91 ? 448  CYS A C     1 
ATOM   3232  O O     . CYS A  1 450  ? -43.171 48.786  72.522  1.00 27.12 ? 448  CYS A O     1 
ATOM   3233  C CB    . CYS A  1 450  ? -43.056 45.385  72.857  1.00 27.31 ? 448  CYS A CB    1 
ATOM   3234  S SG    . CYS A  1 450  ? -43.230 45.542  71.062  1.00 33.74 ? 448  CYS A SG    1 
ATOM   3235  N N     . LEU A  1 451  ? -41.261 47.800  73.192  1.00 24.69 ? 449  LEU A N     1 
ATOM   3236  C CA    . LEU A  1 451  ? -40.412 48.848  72.646  1.00 26.44 ? 449  LEU A CA    1 
ATOM   3237  C C     . LEU A  1 451  ? -39.986 48.470  71.234  1.00 27.98 ? 449  LEU A C     1 
ATOM   3238  O O     . LEU A  1 451  ? -39.707 47.304  70.952  1.00 29.44 ? 449  LEU A O     1 
ATOM   3239  C CB    . LEU A  1 451  ? -39.177 49.074  73.526  1.00 27.57 ? 449  LEU A CB    1 
ATOM   3240  N N     . HIS A  1 452  ? -39.956 49.462  70.351  1.00 27.83 ? 450  HIS A N     1 
ATOM   3241  C CA    . HIS A  1 452  ? -39.460 49.258  68.994  1.00 30.14 ? 450  HIS A CA    1 
ATOM   3242  C C     . HIS A  1 452  ? -38.045 48.690  69.011  1.00 31.41 ? 450  HIS A C     1 
ATOM   3243  O O     . HIS A  1 452  ? -37.202 49.113  69.808  1.00 28.51 ? 450  HIS A O     1 
ATOM   3244  C CB    . HIS A  1 452  ? -39.463 50.577  68.217  1.00 30.49 ? 450  HIS A CB    1 
ATOM   3245  C CG    . HIS A  1 452  ? -38.632 50.534  66.970  1.00 29.93 ? 450  HIS A CG    1 
ATOM   3246  N ND1   . HIS A  1 452  ? -39.124 50.087  65.763  1.00 33.11 ? 450  HIS A ND1   1 
ATOM   3247  C CD2   . HIS A  1 452  ? -37.329 50.844  66.756  1.00 31.23 ? 450  HIS A CD2   1 
ATOM   3248  C CE1   . HIS A  1 452  ? -38.166 50.139  64.853  1.00 32.37 ? 450  HIS A CE1   1 
ATOM   3249  N NE2   . HIS A  1 452  ? -37.066 50.590  65.432  1.00 30.37 ? 450  HIS A NE2   1 
ATOM   3250  N N     . GLY A  1 453  ? -37.787 47.747  68.108  1.00 35.56 ? 451  GLY A N     1 
ATOM   3251  C CA    . GLY A  1 453  ? -36.446 47.191  67.948  1.00 36.54 ? 451  GLY A CA    1 
ATOM   3252  C C     . GLY A  1 453  ? -35.963 46.415  69.153  1.00 42.18 ? 451  GLY A C     1 
ATOM   3253  O O     . GLY A  1 453  ? -34.766 46.453  69.482  1.00 46.69 ? 451  GLY A O     1 
ATOM   3254  N N     . MET A  1 454  ? -36.864 45.700  69.817  1.00 39.38 ? 452  MET A N     1 
ATOM   3255  C CA    . MET A  1 454  ? -36.556 45.086  71.100  1.00 39.60 ? 452  MET A CA    1 
ATOM   3256  C C     . MET A  1 454  ? -37.613 44.040  71.416  1.00 40.62 ? 452  MET A C     1 
ATOM   3257  O O     . MET A  1 454  ? -37.297 42.853  71.554  1.00 40.50 ? 452  MET A O     1 
ATOM   3258  C CB    . MET A  1 454  ? -36.483 46.158  72.189  1.00 37.42 ? 452  MET A CB    1 
ATOM   3259  C CG    . MET A  1 454  ? -36.446 45.639  73.616  1.00 39.16 ? 452  MET A CG    1 
ATOM   3260  S SD    . MET A  1 454  ? -34.913 44.799  74.005  1.00 51.23 ? 452  MET A SD    1 
ATOM   3261  C CE    . MET A  1 454  ? -33.716 46.092  73.650  1.00 46.36 ? 452  MET A CE    1 
ATOM   3262  N N     . GLY A  1 455  ? -38.876 44.464  71.474  1.00 35.88 ? 453  GLY A N     1 
ATOM   3263  C CA    . GLY A  1 455  ? -39.965 43.561  71.783  1.00 36.70 ? 453  GLY A CA    1 
ATOM   3264  C C     . GLY A  1 455  ? -40.567 42.793  70.621  1.00 37.75 ? 453  GLY A C     1 
ATOM   3265  O O     . GLY A  1 455  ? -41.282 41.817  70.851  1.00 38.36 ? 453  GLY A O     1 
ATOM   3266  N N     . GLU A  1 456  ? -40.315 43.205  69.379  1.00 36.92 ? 454  GLU A N     1 
ATOM   3267  C CA    . GLU A  1 456  ? -40.887 42.482  68.243  1.00 37.73 ? 454  GLU A CA    1 
ATOM   3268  C C     . GLU A  1 456  ? -40.568 40.996  68.261  1.00 40.84 ? 454  GLU A C     1 
ATOM   3269  O O     . GLU A  1 456  ? -41.491 40.197  68.044  1.00 42.78 ? 454  GLU A O     1 
ATOM   3270  C CB    . GLU A  1 456  ? -40.437 43.099  66.912  1.00 42.06 ? 454  GLU A CB    1 
ATOM   3271  C CG    . GLU A  1 456  ? -40.932 44.520  66.693  1.00 42.97 ? 454  GLU A CG    1 
ATOM   3272  C CD    . GLU A  1 456  ? -39.890 45.538  67.086  1.00 39.99 ? 454  GLU A CD    1 
ATOM   3273  O OE1   . GLU A  1 456  ? -38.994 45.179  67.882  1.00 40.78 ? 454  GLU A OE1   1 
ATOM   3274  O OE2   . GLU A  1 456  ? -39.958 46.687  66.598  1.00 38.44 ? 454  GLU A OE2   1 
ATOM   3275  N N     . PRO A  1 457  ? -39.325 40.553  68.511  1.00 41.05 ? 455  PRO A N     1 
ATOM   3276  C CA    . PRO A  1 457  ? -39.097 39.102  68.627  1.00 43.75 ? 455  PRO A CA    1 
ATOM   3277  C C     . PRO A  1 457  ? -40.113 38.417  69.524  1.00 41.94 ? 455  PRO A C     1 
ATOM   3278  O O     . PRO A  1 457  ? -40.753 37.446  69.106  1.00 40.07 ? 455  PRO A O     1 
ATOM   3279  C CB    . PRO A  1 457  ? -37.675 39.026  69.194  1.00 43.91 ? 455  PRO A CB    1 
ATOM   3280  C CG    . PRO A  1 457  ? -37.009 40.243  68.692  1.00 41.32 ? 455  PRO A CG    1 
ATOM   3281  C CD    . PRO A  1 457  ? -38.072 41.310  68.709  1.00 40.89 ? 455  PRO A CD    1 
ATOM   3282  N N     . LEU A  1 458  ? -40.310 38.926  70.739  1.00 40.08 ? 456  LEU A N     1 
ATOM   3283  C CA    . LEU A  1 458  ? -41.259 38.295  71.649  1.00 38.29 ? 456  LEU A CA    1 
ATOM   3284  C C     . LEU A  1 458  ? -42.678 38.366  71.102  1.00 38.21 ? 456  LEU A C     1 
ATOM   3285  O O     . LEU A  1 458  ? -43.399 37.364  71.076  1.00 41.25 ? 456  LEU A O     1 
ATOM   3286  C CB    . LEU A  1 458  ? -41.184 38.953  73.025  1.00 36.47 ? 456  LEU A CB    1 
ATOM   3287  C CG    . LEU A  1 458  ? -42.253 38.475  74.015  1.00 38.44 ? 456  LEU A CG    1 
ATOM   3288  C CD1   . LEU A  1 458  ? -42.146 36.969  74.274  1.00 38.34 ? 456  LEU A CD1   1 
ATOM   3289  C CD2   . LEU A  1 458  ? -42.153 39.258  75.313  1.00 36.27 ? 456  LEU A CD2   1 
ATOM   3290  N N     . TYR A  1 459  ? -43.094 39.540  70.644  1.00 36.28 ? 457  TYR A N     1 
ATOM   3291  C CA    . TYR A  1 459  ? -44.499 39.707  70.310  1.00 39.84 ? 457  TYR A CA    1 
ATOM   3292  C C     . TYR A  1 459  ? -44.863 39.181  68.930  1.00 40.39 ? 457  TYR A C     1 
ATOM   3293  O O     . TYR A  1 459  ? -46.053 38.996  68.658  1.00 40.15 ? 457  TYR A O     1 
ATOM   3294  C CB    . TYR A  1 459  ? -44.887 41.173  70.480  1.00 34.48 ? 457  TYR A CB    1 
ATOM   3295  C CG    . TYR A  1 459  ? -45.080 41.489  71.942  1.00 31.39 ? 457  TYR A CG    1 
ATOM   3296  C CD1   . TYR A  1 459  ? -46.276 41.176  72.581  1.00 30.46 ? 457  TYR A CD1   1 
ATOM   3297  C CD2   . TYR A  1 459  ? -44.058 42.036  72.700  1.00 31.80 ? 457  TYR A CD2   1 
ATOM   3298  C CE1   . TYR A  1 459  ? -46.457 41.438  73.925  1.00 30.24 ? 457  TYR A CE1   1 
ATOM   3299  C CE2   . TYR A  1 459  ? -44.233 42.309  74.052  1.00 31.00 ? 457  TYR A CE2   1 
ATOM   3300  C CZ    . TYR A  1 459  ? -45.442 42.008  74.655  1.00 33.20 ? 457  TYR A CZ    1 
ATOM   3301  O OH    . TYR A  1 459  ? -45.639 42.265  76.001  1.00 33.81 ? 457  TYR A OH    1 
ATOM   3302  N N     . GLU A  1 460  ? -43.888 38.879  68.070  1.00 39.66 ? 458  GLU A N     1 
ATOM   3303  C CA    . GLU A  1 460  ? -44.261 38.153  66.862  1.00 42.37 ? 458  GLU A CA    1 
ATOM   3304  C C     . GLU A  1 460  ? -44.651 36.714  67.168  1.00 43.53 ? 458  GLU A C     1 
ATOM   3305  O O     . GLU A  1 460  ? -45.192 36.027  66.293  1.00 44.74 ? 458  GLU A O     1 
ATOM   3306  C CB    . GLU A  1 460  ? -43.129 38.214  65.838  1.00 46.32 ? 458  GLU A CB    1 
ATOM   3307  C CG    . GLU A  1 460  ? -42.844 39.639  65.365  1.00 46.32 ? 458  GLU A CG    1 
ATOM   3308  C CD    . GLU A  1 460  ? -42.196 39.706  63.992  1.00 50.71 ? 458  GLU A CD    1 
ATOM   3309  O OE1   . GLU A  1 460  ? -42.736 39.099  63.042  1.00 57.16 ? 458  GLU A OE1   1 
ATOM   3310  O OE2   . GLU A  1 460  ? -41.149 40.377  63.864  1.00 58.01 ? 458  GLU A OE2   1 
ATOM   3311  N N     . GLU A  1 461  ? -44.408 36.256  68.392  1.00 41.56 ? 459  GLU A N     1 
ATOM   3312  C CA    . GLU A  1 461  ? -44.964 35.017  68.907  1.00 45.65 ? 459  GLU A CA    1 
ATOM   3313  C C     . GLU A  1 461  ? -46.295 35.232  69.625  1.00 44.46 ? 459  GLU A C     1 
ATOM   3314  O O     . GLU A  1 461  ? -46.822 34.293  70.226  1.00 41.13 ? 459  GLU A O     1 
ATOM   3315  C CB    . GLU A  1 461  ? -43.958 34.354  69.854  1.00 45.89 ? 459  GLU A CB    1 
ATOM   3316  C CG    . GLU A  1 461  ? -42.538 34.283  69.309  1.00 45.36 ? 459  GLU A CG    1 
ATOM   3317  C CD    . GLU A  1 461  ? -42.421 33.406  68.069  1.00 51.71 ? 459  GLU A CD    1 
ATOM   3318  O OE1   . GLU A  1 461  ? -43.271 32.503  67.884  1.00 50.47 ? 459  GLU A OE1   1 
ATOM   3319  O OE2   . GLU A  1 461  ? -41.475 33.620  67.277  1.00 55.15 ? 459  GLU A OE2   1 
ATOM   3320  N N     . VAL A  1 462  ? -46.842 36.448  69.579  1.00 41.47 ? 460  VAL A N     1 
ATOM   3321  C CA    . VAL A  1 462  ? -48.050 36.812  70.310  1.00 42.58 ? 460  VAL A CA    1 
ATOM   3322  C C     . VAL A  1 462  ? -49.148 37.287  69.366  1.00 43.66 ? 460  VAL A C     1 
ATOM   3323  O O     . VAL A  1 462  ? -50.289 36.809  69.428  1.00 42.82 ? 460  VAL A O     1 
ATOM   3324  C CB    . VAL A  1 462  ? -47.755 37.886  71.380  1.00 40.58 ? 460  VAL A CB    1 
ATOM   3325  C CG1   . VAL A  1 462  ? -49.052 38.341  72.044  1.00 38.53 ? 460  VAL A CG1   1 
ATOM   3326  C CG2   . VAL A  1 462  ? -46.770 37.367  72.402  1.00 40.42 ? 460  VAL A CG2   1 
ATOM   3327  N N     . VAL A  1 463  ? -48.822 38.236  68.485  1.00 37.18 ? 461  VAL A N     1 
ATOM   3328  C CA    . VAL A  1 463  ? -49.818 38.852  67.619  1.00 41.45 ? 461  VAL A CA    1 
ATOM   3329  C C     . VAL A  1 463  ? -50.256 37.863  66.549  1.00 44.58 ? 461  VAL A C     1 
ATOM   3330  O O     . VAL A  1 463  ? -49.452 37.068  66.047  1.00 45.98 ? 461  VAL A O     1 
ATOM   3331  C CB    . VAL A  1 463  ? -49.247 40.132  66.984  1.00 37.80 ? 461  VAL A CB    1 
ATOM   3332  C CG1   . VAL A  1 463  ? -50.264 40.771  66.052  1.00 40.04 ? 461  VAL A CG1   1 
ATOM   3333  C CG2   . VAL A  1 463  ? -48.794 41.115  68.059  1.00 36.01 ? 461  VAL A CG2   1 
ATOM   3334  N N     . GLY A  1 464  ? -51.530 37.903  66.199  1.00 41.89 ? 462  GLY A N     1 
ATOM   3335  C CA    . GLY A  1 464  ? -52.002 37.150  65.056  1.00 46.51 ? 462  GLY A CA    1 
ATOM   3336  C C     . GLY A  1 464  ? -52.747 35.893  65.458  1.00 48.59 ? 462  GLY A C     1 
ATOM   3337  O O     . GLY A  1 464  ? -52.512 35.306  66.519  1.00 47.34 ? 462  GLY A O     1 
ATOM   3338  N N     . ARG A  1 465  ? -53.660 35.462  64.584  1.00 49.37 ? 463  ARG A N     1 
ATOM   3339  C CA    . ARG A  1 465  ? -54.462 34.278  64.861  1.00 48.40 ? 463  ARG A CA    1 
ATOM   3340  C C     . ARG A  1 465  ? -53.607 33.023  64.976  1.00 51.17 ? 463  ARG A C     1 
ATOM   3341  O O     . ARG A  1 465  ? -54.025 32.062  65.629  1.00 56.36 ? 463  ARG A O     1 
ATOM   3342  C CB    . ARG A  1 465  ? -55.532 34.098  63.773  1.00 47.74 ? 463  ARG A CB    1 
ATOM   3343  N N     . GLY A  1 466  ? -52.420 33.014  64.372  1.00 49.11 ? 464  GLY A N     1 
ATOM   3344  C CA    . GLY A  1 466  ? -51.529 31.874  64.463  1.00 52.12 ? 464  GLY A CA    1 
ATOM   3345  C C     . GLY A  1 466  ? -50.744 31.785  65.746  1.00 53.47 ? 464  GLY A C     1 
ATOM   3346  O O     . GLY A  1 466  ? -50.085 30.768  65.984  1.00 57.41 ? 464  GLY A O     1 
ATOM   3347  N N     . LYS A  1 467  ? -50.781 32.833  66.572  1.00 53.35 ? 465  LYS A N     1 
ATOM   3348  C CA    . LYS A  1 467  ? -50.106 32.819  67.863  1.00 48.29 ? 465  LYS A CA    1 
ATOM   3349  C C     . LYS A  1 467  ? -51.130 32.908  68.986  1.00 47.21 ? 465  LYS A C     1 
ATOM   3350  O O     . LYS A  1 467  ? -52.044 32.086  69.045  1.00 49.50 ? 465  LYS A O     1 
ATOM   3351  C CB    . LYS A  1 467  ? -49.092 33.960  67.942  1.00 44.30 ? 465  LYS A CB    1 
ATOM   3352  C CG    . LYS A  1 467  ? -48.068 33.922  66.818  1.00 47.83 ? 465  LYS A CG    1 
ATOM   3353  C CD    . LYS A  1 467  ? -47.281 32.618  66.859  1.00 50.48 ? 465  LYS A CD    1 
ATOM   3354  C CE    . LYS A  1 467  ? -45.960 32.717  66.103  1.00 51.49 ? 465  LYS A CE    1 
ATOM   3355  N NZ    . LYS A  1 467  ? -45.024 31.604  66.464  1.00 51.60 ? 465  LYS A NZ    1 
ATOM   3356  N N     . LEU A  1 468  ? -50.982 33.876  69.893  1.00 48.91 ? 466  LEU A N     1 
ATOM   3357  C CA    . LEU A  1 468  ? -51.941 34.066  70.977  1.00 43.27 ? 466  LEU A CA    1 
ATOM   3358  C C     . LEU A  1 468  ? -53.113 34.960  70.581  1.00 45.86 ? 466  LEU A C     1 
ATOM   3359  O O     . LEU A  1 468  ? -54.089 35.050  71.337  1.00 43.22 ? 466  LEU A O     1 
ATOM   3360  C CB    . LEU A  1 468  ? -51.239 34.654  72.210  1.00 44.05 ? 466  LEU A CB    1 
ATOM   3361  C CG    . LEU A  1 468  ? -50.020 33.894  72.759  1.00 45.61 ? 466  LEU A CG    1 
ATOM   3362  C CD1   . LEU A  1 468  ? -49.347 34.655  73.899  1.00 43.49 ? 466  LEU A CD1   1 
ATOM   3363  C CD2   . LEU A  1 468  ? -50.400 32.487  73.209  1.00 45.21 ? 466  LEU A CD2   1 
ATOM   3364  N N     . ASP A  1 469  ? -53.038 35.610  69.418  1.00 46.53 ? 467  ASP A N     1 
ATOM   3365  C CA    . ASP A  1 469  ? -54.083 36.506  68.917  1.00 44.37 ? 467  ASP A CA    1 
ATOM   3366  C C     . ASP A  1 469  ? -54.393 37.612  69.922  1.00 40.13 ? 467  ASP A C     1 
ATOM   3367  O O     . ASP A  1 469  ? -55.549 37.890  70.249  1.00 38.52 ? 467  ASP A O     1 
ATOM   3368  C CB    . ASP A  1 469  ? -55.348 35.734  68.540  1.00 46.67 ? 467  ASP A CB    1 
ATOM   3369  C CG    . ASP A  1 469  ? -56.160 36.441  67.466  1.00 49.82 ? 467  ASP A CG    1 
ATOM   3370  O OD1   . ASP A  1 469  ? -55.637 37.393  66.852  1.00 50.13 ? 467  ASP A OD1   1 
ATOM   3371  O OD2   . ASP A  1 469  ? -57.316 36.043  67.232  1.00 54.68 ? 467  ASP A OD2   1 
ATOM   3372  N N     . ARG A  1 470  ? -53.339 38.242  70.420  1.00 42.12 ? 468  ARG A N     1 
ATOM   3373  C CA    . ARG A  1 470  ? -53.465 39.408  71.257  1.00 36.52 ? 468  ARG A CA    1 
ATOM   3374  C C     . ARG A  1 470  ? -52.657 40.539  70.637  1.00 36.54 ? 468  ARG A C     1 
ATOM   3375  O O     . ARG A  1 470  ? -51.515 40.315  70.213  1.00 39.65 ? 468  ARG A O     1 
ATOM   3376  C CB    . ARG A  1 470  ? -52.978 39.117  72.671  1.00 34.13 ? 468  ARG A CB    1 
ATOM   3377  C CG    . ARG A  1 470  ? -53.782 38.029  73.387  1.00 38.09 ? 468  ARG A CG    1 
ATOM   3378  C CD    . ARG A  1 470  ? -55.211 38.473  73.677  1.00 38.08 ? 468  ARG A CD    1 
ATOM   3379  N NE    . ARG A  1 470  ? -55.969 37.428  74.356  1.00 39.53 ? 468  ARG A NE    1 
ATOM   3380  C CZ    . ARG A  1 470  ? -56.788 36.583  73.744  1.00 41.97 ? 468  ARG A CZ    1 
ATOM   3381  N NH1   . ARG A  1 470  ? -56.987 36.643  72.438  1.00 39.38 ? 468  ARG A NH1   1 
ATOM   3382  N NH2   . ARG A  1 470  ? -57.429 35.661  74.462  1.00 36.93 ? 468  ARG A NH2   1 
ATOM   3383  N N     . PRO A  1 471  ? -53.199 41.748  70.555  1.00 39.14 ? 469  PRO A N     1 
ATOM   3384  C CA    . PRO A  1 471  ? -52.492 42.832  69.875  1.00 28.44 ? 469  PRO A CA    1 
ATOM   3385  C C     . PRO A  1 471  ? -51.378 43.395  70.738  1.00 32.97 ? 469  PRO A C     1 
ATOM   3386  O O     . PRO A  1 471  ? -51.357 43.252  71.965  1.00 28.55 ? 469  PRO A O     1 
ATOM   3387  C CB    . PRO A  1 471  ? -53.586 43.880  69.659  1.00 34.20 ? 469  PRO A CB    1 
ATOM   3388  C CG    . PRO A  1 471  ? -54.461 43.702  70.848  1.00 31.95 ? 469  PRO A CG    1 
ATOM   3389  C CD    . PRO A  1 471  ? -54.485 42.204  71.110  1.00 35.72 ? 469  PRO A CD    1 
ATOM   3390  N N     . CYS A  1 472  ? -50.453 44.067  70.063  1.00 31.13 ? 470  CYS A N     1 
ATOM   3391  C CA    . CYS A  1 472  ? -49.333 44.715  70.730  1.00 29.11 ? 470  CYS A CA    1 
ATOM   3392  C C     . CYS A  1 472  ? -49.115 46.070  70.092  1.00 26.02 ? 470  CYS A C     1 
ATOM   3393  O O     . CYS A  1 472  ? -49.088 46.186  68.863  1.00 31.00 ? 470  CYS A O     1 
ATOM   3394  C CB    . CYS A  1 472  ? -48.056 43.879  70.630  1.00 29.15 ? 470  CYS A CB    1 
ATOM   3395  S SG    . CYS A  1 472  ? -46.656 44.575  71.518  1.00 33.34 ? 470  CYS A SG    1 
ATOM   3396  N N     . ARG A  1 473  ? -48.975 47.089  70.921  1.00 26.04 ? 471  ARG A N     1 
ATOM   3397  C CA    . ARG A  1 473  ? -48.625 48.420  70.448  1.00 27.76 ? 471  ARG A CA    1 
ATOM   3398  C C     . ARG A  1 473  ? -47.129 48.638  70.621  1.00 27.08 ? 471  ARG A C     1 
ATOM   3399  O O     . ARG A  1 473  ? -46.598 48.490  71.724  1.00 27.07 ? 471  ARG A O     1 
ATOM   3400  C CB    . ARG A  1 473  ? -49.392 49.501  71.200  1.00 27.73 ? 471  ARG A CB    1 
ATOM   3401  C CG    . ARG A  1 473  ? -49.207 50.889  70.612  1.00 25.36 ? 471  ARG A CG    1 
ATOM   3402  C CD    . ARG A  1 473  ? -50.107 51.879  71.314  1.00 26.50 ? 471  ARG A CD    1 
ATOM   3403  N NE    . ARG A  1 473  ? -51.481 51.396  71.326  1.00 27.25 ? 471  ARG A NE    1 
ATOM   3404  C CZ    . ARG A  1 473  ? -52.347 51.576  70.341  1.00 29.75 ? 471  ARG A CZ    1 
ATOM   3405  N NH1   . ARG A  1 473  ? -52.067 52.355  69.309  1.00 27.03 ? 471  ARG A NH1   1 
ATOM   3406  N NH2   . ARG A  1 473  ? -53.512 50.941  70.383  1.00 25.22 ? 471  ARG A NH2   1 
ATOM   3407  N N     . ILE A  1 474  ? -46.473 49.045  69.540  1.00 27.41 ? 472  ILE A N     1 
ATOM   3408  C CA    . ILE A  1 474  ? -45.044 49.312  69.536  1.00 23.97 ? 472  ILE A CA    1 
ATOM   3409  C C     . ILE A  1 474  ? -44.814 50.765  69.931  1.00 26.33 ? 472  ILE A C     1 
ATOM   3410  O O     . ILE A  1 474  ? -45.344 51.682  69.295  1.00 29.64 ? 472  ILE A O     1 
ATOM   3411  C CB    . ILE A  1 474  ? -44.437 49.006  68.156  1.00 25.14 ? 472  ILE A CB    1 
ATOM   3412  C CG1   . ILE A  1 474  ? -44.614 47.522  67.814  1.00 28.94 ? 472  ILE A CG1   1 
ATOM   3413  C CG2   . ILE A  1 474  ? -42.977 49.409  68.111  1.00 26.55 ? 472  ILE A CG2   1 
ATOM   3414  C CD1   . ILE A  1 474  ? -44.237 47.172  66.360  1.00 29.12 ? 472  ILE A CD1   1 
ATOM   3415  N N     . TYR A  1 475  ? -44.061 50.969  71.008  1.00 23.75 ? 473  TYR A N     1 
ATOM   3416  C CA    . TYR A  1 475  ? -43.610 52.292  71.437  1.00 27.72 ? 473  TYR A CA    1 
ATOM   3417  C C     . TYR A  1 475  ? -42.391 52.674  70.594  1.00 29.43 ? 473  TYR A C     1 
ATOM   3418  O O     . TYR A  1 475  ? -41.325 52.046  70.695  1.00 26.89 ? 473  TYR A O     1 
ATOM   3419  C CB    . TYR A  1 475  ? -43.289 52.254  72.928  1.00 29.75 ? 473  TYR A CB    1 
ATOM   3420  C CG    . TYR A  1 475  ? -43.049 53.580  73.634  1.00 33.85 ? 473  TYR A CG    1 
ATOM   3421  C CD1   . TYR A  1 475  ? -44.088 54.480  73.862  1.00 33.93 ? 473  TYR A CD1   1 
ATOM   3422  C CD2   . TYR A  1 475  ? -41.790 53.892  74.131  1.00 40.24 ? 473  TYR A CD2   1 
ATOM   3423  C CE1   . TYR A  1 475  ? -43.859 55.683  74.536  1.00 35.39 ? 473  TYR A CE1   1 
ATOM   3424  C CE2   . TYR A  1 475  ? -41.551 55.074  74.800  1.00 42.81 ? 473  TYR A CE2   1 
ATOM   3425  C CZ    . TYR A  1 475  ? -42.583 55.966  75.005  1.00 41.89 ? 473  TYR A CZ    1 
ATOM   3426  O OH    . TYR A  1 475  ? -42.306 57.143  75.671  1.00 44.53 ? 473  TYR A OH    1 
ATOM   3427  N N     . ALA A  1 476  ? -42.555 53.689  69.756  1.00 30.61 ? 474  ALA A N     1 
ATOM   3428  C CA    . ALA A  1 476  ? -41.654 53.961  68.636  1.00 28.49 ? 474  ALA A CA    1 
ATOM   3429  C C     . ALA A  1 476  ? -40.951 55.291  68.851  1.00 27.90 ? 474  ALA A C     1 
ATOM   3430  O O     . ALA A  1 476  ? -41.557 56.357  68.638  1.00 24.58 ? 474  ALA A O     1 
ATOM   3431  C CB    . ALA A  1 476  ? -42.434 53.977  67.319  1.00 27.31 ? 474  ALA A CB    1 
ATOM   3432  N N     . PRO A  1 477  ? -39.683 55.284  69.271  1.00 26.40 ? 475  PRO A N     1 
ATOM   3433  C CA    . PRO A  1 477  ? -38.952 56.543  69.415  1.00 25.06 ? 475  PRO A CA    1 
ATOM   3434  C C     . PRO A  1 477  ? -38.729 57.161  68.049  1.00 25.56 ? 475  PRO A C     1 
ATOM   3435  O O     . PRO A  1 477  ? -38.537 56.463  67.052  1.00 26.49 ? 475  PRO A O     1 
ATOM   3436  C CB    . PRO A  1 477  ? -37.624 56.123  70.062  1.00 28.14 ? 475  PRO A CB    1 
ATOM   3437  C CG    . PRO A  1 477  ? -37.879 54.766  70.640  1.00 29.85 ? 475  PRO A CG    1 
ATOM   3438  C CD    . PRO A  1 477  ? -38.889 54.131  69.722  1.00 29.78 ? 475  PRO A CD    1 
ATOM   3439  N N     . VAL A  1 478  ? -38.790 58.479  68.006  1.00 23.39 ? 476  VAL A N     1 
ATOM   3440  C CA    . VAL A  1 478  ? -38.610 59.239  66.780  1.00 26.10 ? 476  VAL A CA    1 
ATOM   3441  C C     . VAL A  1 478  ? -37.661 60.378  67.102  1.00 30.58 ? 476  VAL A C     1 
ATOM   3442  O O     . VAL A  1 478  ? -37.875 61.103  68.081  1.00 32.35 ? 476  VAL A O     1 
ATOM   3443  C CB    . VAL A  1 478  ? -39.947 59.778  66.243  1.00 30.40 ? 476  VAL A CB    1 
ATOM   3444  C CG1   . VAL A  1 478  ? -39.722 60.566  64.952  1.00 25.91 ? 476  VAL A CG1   1 
ATOM   3445  C CG2   . VAL A  1 478  ? -40.926 58.631  66.018  1.00 27.13 ? 476  VAL A CG2   1 
ATOM   3446  N N     . GLY A  1 479  ? -36.596 60.513  66.321  1.00 31.32 ? 477  GLY A N     1 
ATOM   3447  C CA    . GLY A  1 479  ? -35.679 61.607  66.565  1.00 31.24 ? 477  GLY A CA    1 
ATOM   3448  C C     . GLY A  1 479  ? -34.372 61.428  65.827  1.00 30.71 ? 477  GLY A C     1 
ATOM   3449  O O     . GLY A  1 479  ? -34.051 60.351  65.306  1.00 25.83 ? 477  GLY A O     1 
ATOM   3450  N N     . THR A  1 480  ? -33.615 62.523  65.798  1.00 29.62 ? 478  THR A N     1 
ATOM   3451  C CA    . THR A  1 480  ? -32.294 62.540  65.184  1.00 30.96 ? 478  THR A CA    1 
ATOM   3452  C C     . THR A  1 480  ? -31.276 61.799  66.058  1.00 34.93 ? 478  THR A C     1 
ATOM   3453  O O     . THR A  1 480  ? -31.548 61.418  67.200  1.00 35.64 ? 478  THR A O     1 
ATOM   3454  C CB    . THR A  1 480  ? -31.818 63.973  64.992  1.00 35.42 ? 478  THR A CB    1 
ATOM   3455  O OG1   . THR A  1 480  ? -31.710 64.588  66.284  1.00 37.14 ? 478  THR A OG1   1 
ATOM   3456  C CG2   . THR A  1 480  ? -32.795 64.757  64.127  1.00 34.38 ? 478  THR A CG2   1 
ATOM   3457  N N     . HIS A  1 481  ? -30.070 61.631  65.507  1.00 35.66 ? 479  HIS A N     1 
ATOM   3458  C CA    . HIS A  1 481  ? -28.968 61.051  66.273  1.00 39.32 ? 479  HIS A CA    1 
ATOM   3459  C C     . HIS A  1 481  ? -28.694 61.843  67.542  1.00 39.14 ? 479  HIS A C     1 
ATOM   3460  O O     . HIS A  1 481  ? -28.465 61.258  68.608  1.00 40.37 ? 479  HIS A O     1 
ATOM   3461  C CB    . HIS A  1 481  ? -27.701 60.987  65.415  1.00 34.64 ? 479  HIS A CB    1 
ATOM   3462  C CG    . HIS A  1 481  ? -27.827 60.088  64.226  1.00 40.02 ? 479  HIS A CG    1 
ATOM   3463  N ND1   . HIS A  1 481  ? -26.815 59.927  63.305  1.00 37.02 ? 479  HIS A ND1   1 
ATOM   3464  C CD2   . HIS A  1 481  ? -28.845 59.294  63.810  1.00 38.46 ? 479  HIS A CD2   1 
ATOM   3465  C CE1   . HIS A  1 481  ? -27.207 59.082  62.368  1.00 43.19 ? 479  HIS A CE1   1 
ATOM   3466  N NE2   . HIS A  1 481  ? -28.433 58.677  62.653  1.00 41.11 ? 479  HIS A NE2   1 
ATOM   3467  N N     . GLU A  1 482  ? -28.711 63.176  67.446  1.00 40.88 ? 480  GLU A N     1 
ATOM   3468  C CA    . GLU A  1 482  ? -28.487 64.018  68.619  1.00 42.18 ? 480  GLU A CA    1 
ATOM   3469  C C     . GLU A  1 482  ? -29.507 63.722  69.706  1.00 45.65 ? 480  GLU A C     1 
ATOM   3470  O O     . GLU A  1 482  ? -29.146 63.456  70.859  1.00 47.53 ? 480  GLU A O     1 
ATOM   3471  C CB    . GLU A  1 482  ? -28.551 65.493  68.223  1.00 46.35 ? 480  GLU A CB    1 
ATOM   3472  N N     . THR A  1 483  ? -30.794 63.763  69.347  1.00 41.83 ? 481  THR A N     1 
ATOM   3473  C CA    . THR A  1 483  ? -31.862 63.545  70.316  1.00 41.95 ? 481  THR A CA    1 
ATOM   3474  C C     . THR A  1 483  ? -31.805 62.140  70.900  1.00 40.00 ? 481  THR A C     1 
ATOM   3475  O O     . THR A  1 483  ? -31.919 61.959  72.116  1.00 42.82 ? 481  THR A O     1 
ATOM   3476  C CB    . THR A  1 483  ? -33.219 63.783  69.653  1.00 39.99 ? 481  THR A CB    1 
ATOM   3477  O OG1   . THR A  1 483  ? -33.239 65.089  69.070  1.00 43.20 ? 481  THR A OG1   1 
ATOM   3478  C CG2   . THR A  1 483  ? -34.329 63.669  70.674  1.00 42.24 ? 481  THR A CG2   1 
ATOM   3479  N N     . LEU A  1 484  ? -31.655 61.130  70.038  1.00 40.87 ? 482  LEU A N     1 
ATOM   3480  C CA    . LEU A  1 484  ? -31.656 59.739  70.486  1.00 40.44 ? 482  LEU A CA    1 
ATOM   3481  C C     . LEU A  1 484  ? -30.615 59.495  71.572  1.00 42.60 ? 482  LEU A C     1 
ATOM   3482  O O     . LEU A  1 484  ? -30.898 58.843  72.586  1.00 43.03 ? 482  LEU A O     1 
ATOM   3483  C CB    . LEU A  1 484  ? -31.403 58.815  69.294  1.00 41.09 ? 482  LEU A CB    1 
ATOM   3484  N N     . LEU A  1 485  ? -29.407 60.030  71.382  1.00 38.67 ? 483  LEU A N     1 
ATOM   3485  C CA    . LEU A  1 485  ? -28.282 59.712  72.257  1.00 43.25 ? 483  LEU A CA    1 
ATOM   3486  C C     . LEU A  1 485  ? -28.412 60.324  73.646  1.00 43.56 ? 483  LEU A C     1 
ATOM   3487  O O     . LEU A  1 485  ? -27.717 59.878  74.565  1.00 43.20 ? 483  LEU A O     1 
ATOM   3488  C CB    . LEU A  1 485  ? -26.975 60.177  71.612  1.00 37.21 ? 483  LEU A CB    1 
ATOM   3489  C CG    . LEU A  1 485  ? -26.508 59.329  70.433  1.00 43.46 ? 483  LEU A CG    1 
ATOM   3490  C CD1   . LEU A  1 485  ? -25.403 60.027  69.651  1.00 43.05 ? 483  LEU A CD1   1 
ATOM   3491  C CD2   . LEU A  1 485  ? -26.056 57.978  70.932  1.00 39.37 ? 483  LEU A CD2   1 
ATOM   3492  N N     . ALA A  1 486  ? -29.290 61.318  73.824  1.00 42.95 ? 484  ALA A N     1 
ATOM   3493  C CA    . ALA A  1 486  ? -29.324 62.051  75.085  1.00 43.93 ? 484  ALA A CA    1 
ATOM   3494  C C     . ALA A  1 486  ? -29.805 61.187  76.246  1.00 48.07 ? 484  ALA A C     1 
ATOM   3495  O O     . ALA A  1 486  ? -29.334 61.363  77.375  1.00 48.95 ? 484  ALA A O     1 
ATOM   3496  C CB    . ALA A  1 486  ? -30.198 63.296  74.946  1.00 41.94 ? 484  ALA A CB    1 
ATOM   3497  N N     . TYR A  1 487  ? -30.732 60.250  76.002  1.00 44.64 ? 485  TYR A N     1 
ATOM   3498  C CA    . TYR A  1 487  ? -31.222 59.380  77.067  1.00 46.59 ? 485  TYR A CA    1 
ATOM   3499  C C     . TYR A  1 487  ? -31.162 57.905  76.686  1.00 46.17 ? 485  TYR A C     1 
ATOM   3500  O O     . TYR A  1 487  ? -31.861 57.087  77.296  1.00 43.76 ? 485  TYR A O     1 
ATOM   3501  C CB    . TYR A  1 487  ? -32.648 59.771  77.476  1.00 51.33 ? 485  TYR A CB    1 
ATOM   3502  C CG    . TYR A  1 487  ? -32.715 61.179  78.026  1.00 52.38 ? 485  TYR A CG    1 
ATOM   3503  C CD1   . TYR A  1 487  ? -32.023 61.519  79.187  1.00 53.05 ? 485  TYR A CD1   1 
ATOM   3504  C CD2   . TYR A  1 487  ? -33.434 62.175  77.372  1.00 49.76 ? 485  TYR A CD2   1 
ATOM   3505  C CE1   . TYR A  1 487  ? -32.057 62.806  79.694  1.00 56.69 ? 485  TYR A CE1   1 
ATOM   3506  C CE2   . TYR A  1 487  ? -33.478 63.469  77.872  1.00 52.73 ? 485  TYR A CE2   1 
ATOM   3507  C CZ    . TYR A  1 487  ? -32.786 63.780  79.033  1.00 57.56 ? 485  TYR A CZ    1 
ATOM   3508  O OH    . TYR A  1 487  ? -32.818 65.062  79.539  1.00 57.96 ? 485  TYR A OH    1 
ATOM   3509  N N     . LEU A  1 488  ? -30.331 57.542  75.703  1.00 45.79 ? 486  LEU A N     1 
ATOM   3510  C CA    . LEU A  1 488  ? -30.248 56.139  75.307  1.00 45.78 ? 486  LEU A CA    1 
ATOM   3511  C C     . LEU A  1 488  ? -29.724 55.268  76.444  1.00 44.39 ? 486  LEU A C     1 
ATOM   3512  O O     . LEU A  1 488  ? -30.107 54.095  76.558  1.00 40.68 ? 486  LEU A O     1 
ATOM   3513  C CB    . LEU A  1 488  ? -29.369 55.994  74.064  1.00 40.92 ? 486  LEU A CB    1 
ATOM   3514  C CG    . LEU A  1 488  ? -29.337 54.603  73.419  1.00 42.54 ? 486  LEU A CG    1 
ATOM   3515  C CD1   . LEU A  1 488  ? -30.738 54.072  73.168  1.00 40.70 ? 486  LEU A CD1   1 
ATOM   3516  C CD2   . LEU A  1 488  ? -28.548 54.641  72.118  1.00 38.02 ? 486  LEU A CD2   1 
ATOM   3517  N N     . VAL A  1 489  ? -28.855 55.824  77.293  1.00 41.15 ? 487  VAL A N     1 
ATOM   3518  C CA    . VAL A  1 489  ? -28.346 55.073  78.438  1.00 43.31 ? 487  VAL A CA    1 
ATOM   3519  C C     . VAL A  1 489  ? -29.499 54.602  79.317  1.00 44.39 ? 487  VAL A C     1 
ATOM   3520  O O     . VAL A  1 489  ? -29.613 53.414  79.635  1.00 42.14 ? 487  VAL A O     1 
ATOM   3521  C CB    . VAL A  1 489  ? -27.337 55.920  79.234  1.00 43.83 ? 487  VAL A CB    1 
ATOM   3522  C CG1   . VAL A  1 489  ? -27.060 55.283  80.590  1.00 43.41 ? 487  VAL A CG1   1 
ATOM   3523  C CG2   . VAL A  1 489  ? -26.047 56.083  78.435  1.00 41.08 ? 487  VAL A CG2   1 
ATOM   3524  N N     . ARG A  1 490  ? -30.381 55.527  79.711  1.00 45.61 ? 488  ARG A N     1 
ATOM   3525  C CA    . ARG A  1 490  ? -31.528 55.142  80.530  1.00 44.21 ? 488  ARG A CA    1 
ATOM   3526  C C     . ARG A  1 490  ? -32.365 54.058  79.845  1.00 45.39 ? 488  ARG A C     1 
ATOM   3527  O O     . ARG A  1 490  ? -32.817 53.109  80.498  1.00 42.03 ? 488  ARG A O     1 
ATOM   3528  C CB    . ARG A  1 490  ? -32.387 56.373  80.853  1.00 41.94 ? 488  ARG A CB    1 
ATOM   3529  C CG    . ARG A  1 490  ? -33.445 56.110  81.936  1.00 45.02 ? 488  ARG A CG    1 
ATOM   3530  C CD    . ARG A  1 490  ? -34.373 57.312  82.199  1.00 42.28 ? 488  ARG A CD    1 
ATOM   3531  N NE    . ARG A  1 490  ? -35.195 57.669  81.046  1.00 44.87 ? 488  ARG A NE    1 
ATOM   3532  C CZ    . ARG A  1 490  ? -35.345 58.906  80.583  1.00 47.95 ? 488  ARG A CZ    1 
ATOM   3533  N NH1   . ARG A  1 490  ? -34.777 59.943  81.180  1.00 40.48 ? 488  ARG A NH1   1 
ATOM   3534  N NH2   . ARG A  1 490  ? -36.095 59.108  79.500  1.00 42.77 ? 488  ARG A NH2   1 
ATOM   3535  N N     . ARG A  1 491  ? -32.557 54.165  78.522  1.00 43.73 ? 489  ARG A N     1 
ATOM   3536  C CA    . ARG A  1 491  ? -33.419 53.209  77.827  1.00 44.08 ? 489  ARG A CA    1 
ATOM   3537  C C     . ARG A  1 491  ? -32.789 51.824  77.754  1.00 45.95 ? 489  ARG A C     1 
ATOM   3538  O O     . ARG A  1 491  ? -33.507 50.820  77.825  1.00 44.34 ? 489  ARG A O     1 
ATOM   3539  C CB    . ARG A  1 491  ? -33.756 53.714  76.425  1.00 42.57 ? 489  ARG A CB    1 
ATOM   3540  N N     . LEU A  1 492  ? -31.459 51.747  77.626  1.00 47.07 ? 490  LEU A N     1 
ATOM   3541  C CA    . LEU A  1 492  ? -30.788 50.448  77.570  1.00 47.58 ? 490  LEU A CA    1 
ATOM   3542  C C     . LEU A  1 492  ? -30.812 49.751  78.927  1.00 48.46 ? 490  LEU A C     1 
ATOM   3543  O O     . LEU A  1 492  ? -30.996 48.528  79.002  1.00 46.91 ? 490  LEU A O     1 
ATOM   3544  C CB    . LEU A  1 492  ? -29.343 50.615  77.083  1.00 43.91 ? 490  LEU A CB    1 
ATOM   3545  C CG    . LEU A  1 492  ? -29.123 51.095  75.646  1.00 42.68 ? 490  LEU A CG    1 
ATOM   3546  C CD1   . LEU A  1 492  ? -27.706 51.635  75.495  1.00 44.85 ? 490  LEU A CD1   1 
ATOM   3547  C CD2   . LEU A  1 492  ? -29.363 49.964  74.657  1.00 39.97 ? 490  LEU A CD2   1 
ATOM   3548  N N     . LEU A  1 493  ? -30.620 50.505  80.007  1.00 46.07 ? 491  LEU A N     1 
ATOM   3549  C CA    . LEU A  1 493  ? -30.658 49.928  81.342  1.00 46.82 ? 491  LEU A CA    1 
ATOM   3550  C C     . LEU A  1 493  ? -32.049 49.382  81.653  1.00 47.41 ? 491  LEU A C     1 
ATOM   3551  O O     . LEU A  1 493  ? -32.186 48.245  82.101  1.00 49.10 ? 491  LEU A O     1 
ATOM   3552  C CB    . LEU A  1 493  ? -30.244 50.963  82.387  1.00 46.44 ? 491  LEU A CB    1 
ATOM   3553  C CG    . LEU A  1 493  ? -28.792 51.432  82.352  1.00 46.73 ? 491  LEU A CG    1 
ATOM   3554  C CD1   . LEU A  1 493  ? -28.563 52.470  83.438  1.00 46.61 ? 491  LEU A CD1   1 
ATOM   3555  C CD2   . LEU A  1 493  ? -27.844 50.256  82.517  1.00 44.47 ? 491  LEU A CD2   1 
ATOM   3556  N N     . GLY A  1 496  ? -31.008 45.911  80.196  1.00 52.68 ? 494  GLY A N     1 
ATOM   3557  C CA    . GLY A  1 496  ? -29.579 45.651  80.115  1.00 50.14 ? 494  GLY A CA    1 
ATOM   3558  C C     . GLY A  1 496  ? -28.902 45.311  81.435  1.00 56.34 ? 494  GLY A C     1 
ATOM   3559  O O     . GLY A  1 496  ? -27.792 44.769  81.450  1.00 58.37 ? 494  GLY A O     1 
ATOM   3560  N N     . ALA A  1 497  ? -29.563 45.637  82.547  1.00 56.18 ? 495  ALA A N     1 
ATOM   3561  C CA    . ALA A  1 497  ? -29.036 45.306  83.864  1.00 53.50 ? 495  ALA A CA    1 
ATOM   3562  C C     . ALA A  1 497  ? -29.029 43.793  84.067  1.00 51.93 ? 495  ALA A C     1 
ATOM   3563  O O     . ALA A  1 497  ? -29.774 43.052  83.419  1.00 52.57 ? 495  ALA A O     1 
ATOM   3564  C CB    . ALA A  1 497  ? -29.867 45.979  84.957  1.00 47.99 ? 495  ALA A CB    1 
ATOM   3565  N N     . ASN A  1 498  ? -28.178 43.333  84.989  1.00 50.08 ? 496  ASN A N     1 
ATOM   3566  C CA    . ASN A  1 498  ? -28.097 41.896  85.254  1.00 51.93 ? 496  ASN A CA    1 
ATOM   3567  C C     . ASN A  1 498  ? -29.465 41.301  85.585  1.00 53.37 ? 496  ASN A C     1 
ATOM   3568  O O     . ASN A  1 498  ? -29.753 40.154  85.217  1.00 51.28 ? 496  ASN A O     1 
ATOM   3569  C CB    . ASN A  1 498  ? -27.107 41.623  86.391  1.00 53.78 ? 496  ASN A CB    1 
ATOM   3570  N N     . SER A  1 499  ? -30.328 42.071  86.247  1.00 51.96 ? 497  SER A N     1 
ATOM   3571  C CA    . SER A  1 499  ? -31.651 41.596  86.634  1.00 51.47 ? 497  SER A CA    1 
ATOM   3572  C C     . SER A  1 499  ? -32.689 41.699  85.515  1.00 48.01 ? 497  SER A C     1 
ATOM   3573  O O     . SER A  1 499  ? -33.782 41.136  85.662  1.00 47.39 ? 497  SER A O     1 
ATOM   3574  C CB    . SER A  1 499  ? -32.137 42.372  87.869  1.00 49.55 ? 497  SER A CB    1 
ATOM   3575  O OG    . SER A  1 499  ? -32.227 43.770  87.617  1.00 44.53 ? 497  SER A OG    1 
ATOM   3576  N N     . SER A  1 500  ? -32.376 42.379  84.412  1.00 46.73 ? 498  SER A N     1 
ATOM   3577  C CA    . SER A  1 500  ? -33.346 42.601  83.344  1.00 46.01 ? 498  SER A CA    1 
ATOM   3578  C C     . SER A  1 500  ? -33.644 41.310  82.588  1.00 48.43 ? 498  SER A C     1 
ATOM   3579  O O     . SER A  1 500  ? -32.784 40.438  82.440  1.00 46.30 ? 498  SER A O     1 
ATOM   3580  C CB    . SER A  1 500  ? -32.834 43.659  82.365  1.00 46.91 ? 498  SER A CB    1 
ATOM   3581  O OG    . SER A  1 500  ? -32.647 44.904  83.012  1.00 50.38 ? 498  SER A OG    1 
ATOM   3582  N N     . PHE A  1 501  ? -34.882 41.205  82.087  1.00 42.60 ? 499  PHE A N     1 
ATOM   3583  C CA    . PHE A  1 501  ? -35.303 39.995  81.385  1.00 46.74 ? 499  PHE A CA    1 
ATOM   3584  C C     . PHE A  1 501  ? -34.526 39.802  80.085  1.00 49.46 ? 499  PHE A C     1 
ATOM   3585  O O     . PHE A  1 501  ? -34.051 38.698  79.795  1.00 49.65 ? 499  PHE A O     1 
ATOM   3586  C CB    . PHE A  1 501  ? -36.810 40.034  81.108  1.00 41.30 ? 499  PHE A CB    1 
ATOM   3587  C CG    . PHE A  1 501  ? -37.343 38.779  80.451  1.00 42.48 ? 499  PHE A CG    1 
ATOM   3588  C CD1   . PHE A  1 501  ? -37.699 37.679  81.216  1.00 42.97 ? 499  PHE A CD1   1 
ATOM   3589  C CD2   . PHE A  1 501  ? -37.483 38.703  79.072  1.00 41.88 ? 499  PHE A CD2   1 
ATOM   3590  C CE1   . PHE A  1 501  ? -38.193 36.523  80.622  1.00 42.95 ? 499  PHE A CE1   1 
ATOM   3591  C CE2   . PHE A  1 501  ? -37.968 37.551  78.466  1.00 41.12 ? 499  PHE A CE2   1 
ATOM   3592  C CZ    . PHE A  1 501  ? -38.329 36.460  79.244  1.00 42.50 ? 499  PHE A CZ    1 
ATOM   3593  N N     . VAL A  1 502  ? -34.393 40.858  79.278  1.00 47.65 ? 500  VAL A N     1 
ATOM   3594  C CA    . VAL A  1 502  ? -33.736 40.674  77.987  1.00 50.10 ? 500  VAL A CA    1 
ATOM   3595  C C     . VAL A  1 502  ? -32.258 40.370  78.185  1.00 52.56 ? 500  VAL A C     1 
ATOM   3596  O O     . VAL A  1 502  ? -31.641 39.687  77.355  1.00 56.20 ? 500  VAL A O     1 
ATOM   3597  C CB    . VAL A  1 502  ? -33.956 41.895  77.070  1.00 46.35 ? 500  VAL A CB    1 
ATOM   3598  C CG1   . VAL A  1 502  ? -35.397 42.401  77.181  1.00 43.41 ? 500  VAL A CG1   1 
ATOM   3599  C CG2   . VAL A  1 502  ? -32.934 42.997  77.350  1.00 50.52 ? 500  VAL A CG2   1 
ATOM   3600  N N     . HIS A  1 503  ? -31.671 40.847  79.286  1.00 48.72 ? 501  HIS A N     1 
ATOM   3601  C CA    . HIS A  1 503  ? -30.306 40.464  79.626  1.00 50.09 ? 501  HIS A CA    1 
ATOM   3602  C C     . HIS A  1 503  ? -30.229 38.983  79.981  1.00 54.24 ? 501  HIS A C     1 
ATOM   3603  O O     . HIS A  1 503  ? -29.239 38.309  79.667  1.00 54.34 ? 501  HIS A O     1 
ATOM   3604  C CB    . HIS A  1 503  ? -29.804 41.325  80.785  1.00 50.38 ? 501  HIS A CB    1 
ATOM   3605  C CG    . HIS A  1 503  ? -28.398 41.028  81.200  1.00 52.11 ? 501  HIS A CG    1 
ATOM   3606  N ND1   . HIS A  1 503  ? -28.075 39.990  82.049  1.00 53.39 ? 501  HIS A ND1   1 
ATOM   3607  C CD2   . HIS A  1 503  ? -27.229 41.639  80.891  1.00 51.39 ? 501  HIS A CD2   1 
ATOM   3608  C CE1   . HIS A  1 503  ? -26.767 39.972  82.241  1.00 52.69 ? 501  HIS A CE1   1 
ATOM   3609  N NE2   . HIS A  1 503  ? -26.231 40.960  81.548  1.00 51.08 ? 501  HIS A NE2   1 
ATOM   3610  N N     . ARG A  1 504  ? -31.271 38.455  80.623  1.00 52.23 ? 502  ARG A N     1 
ATOM   3611  C CA    . ARG A  1 504  ? -31.227 37.074  81.086  1.00 51.01 ? 502  ARG A CA    1 
ATOM   3612  C C     . ARG A  1 504  ? -31.639 36.096  79.990  1.00 52.43 ? 502  ARG A C     1 
ATOM   3613  O O     . ARG A  1 504  ? -31.041 35.019  79.869  1.00 50.82 ? 502  ARG A O     1 
ATOM   3614  C CB    . ARG A  1 504  ? -32.099 36.922  82.335  1.00 50.87 ? 502  ARG A CB    1 
ATOM   3615  C CG    . ARG A  1 504  ? -31.517 37.668  83.544  1.00 53.83 ? 502  ARG A CG    1 
ATOM   3616  C CD    . ARG A  1 504  ? -32.552 37.912  84.632  1.00 53.61 ? 502  ARG A CD    1 
ATOM   3617  N NE    . ARG A  1 504  ? -33.356 36.722  84.884  1.00 54.11 ? 502  ARG A NE    1 
ATOM   3618  C CZ    . ARG A  1 504  ? -32.967 35.693  85.624  1.00 55.98 ? 502  ARG A CZ    1 
ATOM   3619  N NH1   . ARG A  1 504  ? -31.790 35.681  86.229  1.00 52.27 ? 502  ARG A NH1   1 
ATOM   3620  N NH2   . ARG A  1 504  ? -33.776 34.644  85.752  1.00 54.69 ? 502  ARG A NH2   1 
ATOM   3621  N N     . ILE A  1 505  ? -32.640 36.450  79.173  1.00 52.10 ? 503  ILE A N     1 
ATOM   3622  C CA    . ILE A  1 505  ? -32.996 35.584  78.050  1.00 51.57 ? 503  ILE A CA    1 
ATOM   3623  C C     . ILE A  1 505  ? -31.793 35.398  77.136  1.00 55.08 ? 503  ILE A C     1 
ATOM   3624  O O     . ILE A  1 505  ? -31.625 34.337  76.520  1.00 53.65 ? 503  ILE A O     1 
ATOM   3625  C CB    . ILE A  1 505  ? -34.211 36.143  77.280  1.00 48.27 ? 503  ILE A CB    1 
ATOM   3626  N N     . ASN A  1 506  ? -30.920 36.406  77.063  1.00 54.98 ? 504  ASN A N     1 
ATOM   3627  C CA    . ASN A  1 506  ? -29.706 36.354  76.261  1.00 55.71 ? 504  ASN A CA    1 
ATOM   3628  C C     . ASN A  1 506  ? -28.469 35.980  77.080  1.00 58.46 ? 504  ASN A C     1 
ATOM   3629  O O     . ASN A  1 506  ? -27.345 36.170  76.607  1.00 63.29 ? 504  ASN A O     1 
ATOM   3630  C CB    . ASN A  1 506  ? -29.488 37.693  75.552  1.00 57.19 ? 504  ASN A CB    1 
ATOM   3631  N N     . ASP A  1 507  ? -28.650 35.449  78.292  1.00 59.11 ? 505  ASP A N     1 
ATOM   3632  C CA    . ASP A  1 507  ? -27.539 34.983  79.117  1.00 57.04 ? 505  ASP A CA    1 
ATOM   3633  C C     . ASP A  1 507  ? -27.560 33.464  79.185  1.00 61.70 ? 505  ASP A C     1 
ATOM   3634  O O     . ASP A  1 507  ? -28.519 32.888  79.723  1.00 57.59 ? 505  ASP A O     1 
ATOM   3635  C CB    . ASP A  1 507  ? -27.610 35.577  80.522  1.00 57.94 ? 505  ASP A CB    1 
ATOM   3636  N N     . PRO A  1 508  ? -26.537 32.779  78.663  1.00 62.48 ? 506  PRO A N     1 
ATOM   3637  C CA    . PRO A  1 508  ? -26.581 31.305  78.624  1.00 63.56 ? 506  PRO A CA    1 
ATOM   3638  C C     . PRO A  1 508  ? -26.527 30.649  79.994  1.00 58.74 ? 506  PRO A C     1 
ATOM   3639  O O     . PRO A  1 508  ? -26.843 29.458  80.103  1.00 62.54 ? 506  PRO A O     1 
ATOM   3640  C CB    . PRO A  1 508  ? -25.350 30.935  77.781  1.00 62.59 ? 506  PRO A CB    1 
ATOM   3641  C CG    . PRO A  1 508  ? -24.985 32.200  77.042  1.00 65.43 ? 506  PRO A CG    1 
ATOM   3642  C CD    . PRO A  1 508  ? -25.361 33.319  77.961  1.00 63.70 ? 506  PRO A CD    1 
ATOM   3643  N N     . LYS A  1 509  ? -26.143 31.379  81.041  1.00 61.37 ? 507  LYS A N     1 
ATOM   3644  C CA    . LYS A  1 509  ? -26.118 30.811  82.382  1.00 62.21 ? 507  LYS A CA    1 
ATOM   3645  C C     . LYS A  1 509  ? -27.509 30.656  82.989  1.00 60.73 ? 507  LYS A C     1 
ATOM   3646  O O     . LYS A  1 509  ? -27.632 30.063  84.067  1.00 61.52 ? 507  LYS A O     1 
ATOM   3647  C CB    . LYS A  1 509  ? -25.246 31.678  83.293  1.00 60.87 ? 507  LYS A CB    1 
ATOM   3648  N N     . VAL A  1 510  ? -28.552 31.152  82.327  1.00 59.87 ? 508  VAL A N     1 
ATOM   3649  C CA    . VAL A  1 510  ? -29.907 31.178  82.872  1.00 56.49 ? 508  VAL A CA    1 
ATOM   3650  C C     . VAL A  1 510  ? -30.762 30.188  82.091  1.00 53.05 ? 508  VAL A C     1 
ATOM   3651  O O     . VAL A  1 510  ? -30.948 30.337  80.877  1.00 54.15 ? 508  VAL A O     1 
ATOM   3652  C CB    . VAL A  1 510  ? -30.504 32.595  82.818  1.00 54.51 ? 508  VAL A CB    1 
ATOM   3653  C CG1   . VAL A  1 510  ? -31.873 32.643  83.502  1.00 52.96 ? 508  VAL A CG1   1 
ATOM   3654  C CG2   . VAL A  1 510  ? -29.548 33.605  83.450  1.00 53.37 ? 508  VAL A CG2   1 
ATOM   3655  N N     . SER A  1 511  ? -31.285 29.179  82.784  1.00 49.58 ? 509  SER A N     1 
ATOM   3656  C CA    . SER A  1 511  ? -32.145 28.184  82.162  1.00 50.05 ? 509  SER A CA    1 
ATOM   3657  C C     . SER A  1 511  ? -33.547 28.744  81.945  1.00 49.97 ? 509  SER A C     1 
ATOM   3658  O O     . SER A  1 511  ? -33.938 29.758  82.528  1.00 49.43 ? 509  SER A O     1 
ATOM   3659  C CB    . SER A  1 511  ? -32.234 26.928  83.027  1.00 54.31 ? 509  SER A CB    1 
ATOM   3660  O OG    . SER A  1 511  ? -32.859 27.218  84.267  1.00 51.12 ? 509  SER A OG    1 
ATOM   3661  N N     . ILE A  1 512  ? -34.312 28.061  81.093  1.00 52.07 ? 510  ILE A N     1 
ATOM   3662  C CA    . ILE A  1 512  ? -35.712 28.432  80.920  1.00 50.71 ? 510  ILE A CA    1 
ATOM   3663  C C     . ILE A  1 512  ? -36.454 28.313  82.245  1.00 53.40 ? 510  ILE A C     1 
ATOM   3664  O O     . ILE A  1 512  ? -37.253 29.189  82.607  1.00 51.70 ? 510  ILE A O     1 
ATOM   3665  C CB    . ILE A  1 512  ? -36.369 27.577  79.823  1.00 49.81 ? 510  ILE A CB    1 
ATOM   3666  C CG1   . ILE A  1 512  ? -35.605 27.727  78.505  1.00 48.77 ? 510  ILE A CG1   1 
ATOM   3667  C CG2   . ILE A  1 512  ? -37.829 27.970  79.648  1.00 49.71 ? 510  ILE A CG2   1 
ATOM   3668  C CD1   . ILE A  1 512  ? -36.328 27.140  77.307  1.00 52.31 ? 510  ILE A CD1   1 
ATOM   3669  N N     . ASP A  1 513  ? -36.182 27.238  82.998  1.00 51.97 ? 511  ASP A N     1 
ATOM   3670  C CA    . ASP A  1 513  ? -36.838 27.032  84.286  1.00 48.33 ? 511  ASP A CA    1 
ATOM   3671  C C     . ASP A  1 513  ? -36.631 28.229  85.209  1.00 50.38 ? 511  ASP A C     1 
ATOM   3672  O O     . ASP A  1 513  ? -37.549 28.625  85.938  1.00 51.22 ? 511  ASP A O     1 
ATOM   3673  C CB    . ASP A  1 513  ? -36.323 25.747  84.936  1.00 53.80 ? 511  ASP A CB    1 
ATOM   3674  N N     . GLU A  1 514  ? -35.441 28.833  85.176  1.00 49.67 ? 512  GLU A N     1 
ATOM   3675  C CA    . GLU A  1 514  ? -35.222 30.064  85.926  1.00 50.44 ? 512  GLU A CA    1 
ATOM   3676  C C     . GLU A  1 514  ? -36.041 31.220  85.365  1.00 50.39 ? 512  GLU A C     1 
ATOM   3677  O O     . GLU A  1 514  ? -36.403 32.136  86.110  1.00 49.05 ? 512  GLU A O     1 
ATOM   3678  C CB    . GLU A  1 514  ? -33.735 30.433  85.925  1.00 52.22 ? 512  GLU A CB    1 
ATOM   3679  C CG    . GLU A  1 514  ? -32.857 29.498  86.751  1.00 54.05 ? 512  GLU A CG    1 
ATOM   3680  C CD    . GLU A  1 514  ? -31.367 29.775  86.598  1.00 56.57 ? 512  GLU A CD    1 
ATOM   3681  O OE1   . GLU A  1 514  ? -30.996 30.710  85.857  1.00 60.45 ? 512  GLU A OE1   1 
ATOM   3682  O OE2   . GLU A  1 514  ? -30.560 29.055  87.222  1.00 61.05 ? 512  GLU A OE2   1 
ATOM   3683  N N     . LEU A  1 515  ? -36.335 31.200  84.060  1.00 50.42 ? 513  LEU A N     1 
ATOM   3684  C CA    . LEU A  1 515  ? -36.979 32.345  83.420  1.00 53.78 ? 513  LEU A CA    1 
ATOM   3685  C C     . LEU A  1 515  ? -38.492 32.326  83.579  1.00 48.91 ? 513  LEU A C     1 
ATOM   3686  O O     . LEU A  1 515  ? -39.120 33.391  83.610  1.00 46.89 ? 513  LEU A O     1 
ATOM   3687  C CB    . LEU A  1 515  ? -36.622 32.399  81.934  1.00 51.49 ? 513  LEU A CB    1 
ATOM   3688  C CG    . LEU A  1 515  ? -35.202 32.830  81.573  1.00 49.51 ? 513  LEU A CG    1 
ATOM   3689  C CD1   . LEU A  1 515  ? -35.002 32.714  80.072  1.00 48.52 ? 513  LEU A CD1   1 
ATOM   3690  C CD2   . LEU A  1 515  ? -34.919 34.248  82.057  1.00 47.11 ? 513  LEU A CD2   1 
ATOM   3691  N N     . ILE A  1 516  ? -39.095 31.142  83.670  1.00 46.60 ? 514  ILE A N     1 
ATOM   3692  C CA    . ILE A  1 516  ? -40.537 31.024  83.840  1.00 48.23 ? 514  ILE A CA    1 
ATOM   3693  C C     . ILE A  1 516  ? -40.923 30.865  85.305  1.00 48.20 ? 514  ILE A C     1 
ATOM   3694  O O     . ILE A  1 516  ? -42.063 30.493  85.606  1.00 47.30 ? 514  ILE A O     1 
ATOM   3695  C CB    . ILE A  1 516  ? -41.104 29.871  83.002  1.00 46.09 ? 514  ILE A CB    1 
ATOM   3696  C CG1   . ILE A  1 516  ? -40.586 28.530  83.525  1.00 50.03 ? 514  ILE A CG1   1 
ATOM   3697  C CG2   . ILE A  1 516  ? -40.758 30.066  81.533  1.00 48.72 ? 514  ILE A CG2   1 
ATOM   3698  C CD1   . ILE A  1 516  ? -41.219 27.346  82.850  1.00 48.29 ? 514  ILE A CD1   1 
ATOM   3699  N N     . ALA A  1 517  ? -39.998 31.136  86.223  1.00 47.07 ? 515  ALA A N     1 
ATOM   3700  C CA    . ALA A  1 517  ? -40.301 31.042  87.644  1.00 49.67 ? 515  ALA A CA    1 
ATOM   3701  C C     . ALA A  1 517  ? -41.362 32.062  88.037  1.00 45.71 ? 515  ALA A C     1 
ATOM   3702  O O     . ALA A  1 517  ? -41.341 33.211  87.588  1.00 43.69 ? 515  ALA A O     1 
ATOM   3703  C CB    . ALA A  1 517  ? -39.031 31.262  88.467  1.00 50.61 ? 515  ALA A CB    1 
ATOM   3704  N N     . ASP A  1 518  ? -42.292 31.638  88.886  1.00 47.36 ? 516  ASP A N     1 
ATOM   3705  C CA    . ASP A  1 518  ? -43.370 32.508  89.341  1.00 45.98 ? 516  ASP A CA    1 
ATOM   3706  C C     . ASP A  1 518  ? -42.884 33.442  90.444  1.00 42.26 ? 516  ASP A C     1 
ATOM   3707  O O     . ASP A  1 518  ? -42.638 32.998  91.571  1.00 40.68 ? 516  ASP A O     1 
ATOM   3708  C CB    . ASP A  1 518  ? -44.551 31.677  89.840  1.00 46.19 ? 516  ASP A CB    1 
ATOM   3709  C CG    . ASP A  1 518  ? -45.767 32.528  90.175  1.00 47.76 ? 516  ASP A CG    1 
ATOM   3710  O OD1   . ASP A  1 518  ? -45.731 33.770  89.970  1.00 43.80 ? 516  ASP A OD1   1 
ATOM   3711  O OD2   . ASP A  1 518  ? -46.769 31.948  90.647  1.00 50.64 ? 516  ASP A OD2   1 
ATOM   3712  N N     . PRO A  1 519  ? -42.780 34.744  90.178  1.00 41.27 ? 517  PRO A N     1 
ATOM   3713  C CA    . PRO A  1 519  ? -42.303 35.654  91.232  1.00 41.59 ? 517  PRO A CA    1 
ATOM   3714  C C     . PRO A  1 519  ? -43.267 35.761  92.406  1.00 40.90 ? 517  PRO A C     1 
ATOM   3715  O O     . PRO A  1 519  ? -42.829 36.047  93.529  1.00 39.63 ? 517  PRO A O     1 
ATOM   3716  C CB    . PRO A  1 519  ? -42.143 36.994  90.494  1.00 41.18 ? 517  PRO A CB    1 
ATOM   3717  C CG    . PRO A  1 519  ? -43.087 36.903  89.336  1.00 41.57 ? 517  PRO A CG    1 
ATOM   3718  C CD    . PRO A  1 519  ? -43.158 35.452  88.941  1.00 42.22 ? 517  PRO A CD    1 
ATOM   3719  N N     . VAL A  1 520  ? -44.563 35.534  92.180  1.00 42.48 ? 518  VAL A N     1 
ATOM   3720  C CA    . VAL A  1 520  ? -45.532 35.574  93.268  1.00 43.10 ? 518  VAL A CA    1 
ATOM   3721  C C     . VAL A  1 520  ? -45.248 34.463  94.269  1.00 42.88 ? 518  VAL A C     1 
ATOM   3722  O O     . VAL A  1 520  ? -45.196 34.694  95.483  1.00 40.45 ? 518  VAL A O     1 
ATOM   3723  C CB    . VAL A  1 520  ? -46.961 35.477  92.709  1.00 42.79 ? 518  VAL A CB    1 
ATOM   3724  C CG1   . VAL A  1 520  ? -47.983 35.559  93.834  1.00 42.53 ? 518  VAL A CG1   1 
ATOM   3725  C CG2   . VAL A  1 520  ? -47.198 36.567  91.680  1.00 42.10 ? 518  VAL A CG2   1 
ATOM   3726  N N     . GLU A  1 521  ? -45.040 33.242  93.778  1.00 44.02 ? 519  GLU A N     1 
ATOM   3727  C CA    . GLU A  1 521  ? -44.788 32.136  94.696  1.00 47.10 ? 519  GLU A CA    1 
ATOM   3728  C C     . GLU A  1 521  ? -43.411 32.237  95.342  1.00 48.00 ? 519  GLU A C     1 
ATOM   3729  O O     . GLU A  1 521  ? -43.251 31.854  96.506  1.00 45.47 ? 519  GLU A O     1 
ATOM   3730  C CB    . GLU A  1 521  ? -44.955 30.802  93.971  1.00 45.05 ? 519  GLU A CB    1 
ATOM   3731  C CG    . GLU A  1 521  ? -46.368 30.584  93.450  1.00 50.30 ? 519  GLU A CG    1 
ATOM   3732  C CD    . GLU A  1 521  ? -47.423 30.815  94.521  1.00 55.44 ? 519  GLU A CD    1 
ATOM   3733  O OE1   . GLU A  1 521  ? -47.161 30.477  95.698  1.00 51.36 ? 519  GLU A OE1   1 
ATOM   3734  O OE2   . GLU A  1 521  ? -48.513 31.342  94.188  1.00 54.73 ? 519  GLU A OE2   1 
ATOM   3735  N N     . VAL A  1 522  ? -42.416 32.764  94.623  1.00 42.21 ? 520  VAL A N     1 
ATOM   3736  C CA    . VAL A  1 522  ? -41.104 32.970  95.231  1.00 44.00 ? 520  VAL A CA    1 
ATOM   3737  C C     . VAL A  1 522  ? -41.196 33.979  96.374  1.00 47.89 ? 520  VAL A C     1 
ATOM   3738  O O     . VAL A  1 522  ? -40.631 33.770  97.455  1.00 45.34 ? 520  VAL A O     1 
ATOM   3739  C CB    . VAL A  1 522  ? -40.076 33.407  94.169  1.00 43.57 ? 520  VAL A CB    1 
ATOM   3740  C CG1   . VAL A  1 522  ? -38.734 33.632  94.813  1.00 45.64 ? 520  VAL A CG1   1 
ATOM   3741  C CG2   . VAL A  1 522  ? -39.962 32.363  93.064  1.00 43.48 ? 520  VAL A CG2   1 
ATOM   3742  N N     . VAL A  1 523  ? -41.917 35.082  96.163  1.00 39.99 ? 521  VAL A N     1 
ATOM   3743  C CA    . VAL A  1 523  ? -42.061 36.072  97.225  1.00 41.05 ? 521  VAL A CA    1 
ATOM   3744  C C     . VAL A  1 523  ? -42.903 35.519  98.374  1.00 44.14 ? 521  VAL A C     1 
ATOM   3745  O O     . VAL A  1 523  ? -42.587 35.739  99.549  1.00 43.28 ? 521  VAL A O     1 
ATOM   3746  C CB    . VAL A  1 523  ? -42.658 37.372  96.659  1.00 40.55 ? 521  VAL A CB    1 
ATOM   3747  C CG1   . VAL A  1 523  ? -43.151 38.260  97.785  1.00 37.30 ? 521  VAL A CG1   1 
ATOM   3748  C CG2   . VAL A  1 523  ? -41.616 38.096  95.825  1.00 38.33 ? 521  VAL A CG2   1 
ATOM   3749  N N     . ARG A  1 524  ? -43.990 34.809  98.060  1.00 42.68 ? 522  ARG A N     1 
ATOM   3750  C CA    . ARG A  1 524  ? -44.858 34.299  99.122  1.00 46.76 ? 522  ARG A CA    1 
ATOM   3751  C C     . ARG A  1 524  ? -44.099 33.406  100.099 1.00 48.43 ? 522  ARG A C     1 
ATOM   3752  O O     . ARG A  1 524  ? -44.401 33.402  101.299 1.00 50.67 ? 522  ARG A O     1 
ATOM   3753  C CB    . ARG A  1 524  ? -46.036 33.530  98.531  1.00 47.63 ? 522  ARG A CB    1 
ATOM   3754  C CG    . ARG A  1 524  ? -46.988 32.993  99.598  1.00 48.98 ? 522  ARG A CG    1 
ATOM   3755  C CD    . ARG A  1 524  ? -47.835 31.864  99.069  1.00 48.98 ? 522  ARG A CD    1 
ATOM   3756  N NE    . ARG A  1 524  ? -48.374 32.165  97.750  1.00 49.73 ? 522  ARG A NE    1 
ATOM   3757  C CZ    . ARG A  1 524  ? -49.443 32.917  97.529  1.00 47.24 ? 522  ARG A CZ    1 
ATOM   3758  N NH1   . ARG A  1 524  ? -50.098 33.493  98.521  1.00 49.39 ? 522  ARG A NH1   1 
ATOM   3759  N NH2   . ARG A  1 524  ? -49.867 33.089  96.283  1.00 51.56 ? 522  ARG A NH2   1 
ATOM   3760  N N     . ALA A  1 525  ? -43.098 32.675  99.616  1.00 46.65 ? 523  ALA A N     1 
ATOM   3761  C CA    . ALA A  1 525  ? -42.385 31.691  100.416 1.00 46.97 ? 523  ALA A CA    1 
ATOM   3762  C C     . ALA A  1 525  ? -41.100 32.224  101.036 1.00 51.32 ? 523  ALA A C     1 
ATOM   3763  O O     . ALA A  1 525  ? -40.391 31.461  101.702 1.00 51.69 ? 523  ALA A O     1 
ATOM   3764  C CB    . ALA A  1 525  ? -42.069 30.465  99.560  1.00 49.23 ? 523  ALA A CB    1 
ATOM   3765  N N     . MET A  1 526  ? -40.769 33.499  100.832 1.00 47.06 ? 524  MET A N     1 
ATOM   3766  C CA    . MET A  1 526  ? -39.583 34.053  101.459 1.00 49.11 ? 524  MET A CA    1 
ATOM   3767  C C     . MET A  1 526  ? -39.816 34.190  102.965 1.00 51.48 ? 524  MET A C     1 
ATOM   3768  O O     . MET A  1 526  ? -40.962 34.281  103.414 1.00 45.53 ? 524  MET A O     1 
ATOM   3769  C CB    . MET A  1 526  ? -39.220 35.403  100.837 1.00 50.25 ? 524  MET A CB    1 
ATOM   3770  C CG    . MET A  1 526  ? -38.590 35.289  99.451  1.00 48.74 ? 524  MET A CG    1 
ATOM   3771  S SD    . MET A  1 526  ? -37.901 36.840  98.810  1.00 67.60 ? 524  MET A SD    1 
ATOM   3772  C CE    . MET A  1 526  ? -39.220 38.006  99.171  1.00 51.66 ? 524  MET A CE    1 
ATOM   3773  N N     . PRO A  1 527  ? -38.746 34.179  103.773 1.00 49.55 ? 525  PRO A N     1 
ATOM   3774  C CA    . PRO A  1 527  ? -38.951 34.195  105.235 1.00 50.86 ? 525  PRO A CA    1 
ATOM   3775  C C     . PRO A  1 527  ? -39.708 35.422  105.710 1.00 50.08 ? 525  PRO A C     1 
ATOM   3776  O O     . PRO A  1 527  ? -40.676 35.305  106.472 1.00 46.52 ? 525  PRO A O     1 
ATOM   3777  C CB    . PRO A  1 527  ? -37.520 34.150  105.789 1.00 50.53 ? 525  PRO A CB    1 
ATOM   3778  C CG    . PRO A  1 527  ? -36.678 33.650  104.660 1.00 49.44 ? 525  PRO A CG    1 
ATOM   3779  C CD    . PRO A  1 527  ? -37.316 34.185  103.422 1.00 48.97 ? 525  PRO A CD    1 
ATOM   3780  N N     . VAL A  1 528  ? -39.296 36.601  105.270 1.00 45.47 ? 526  VAL A N     1 
ATOM   3781  C CA    . VAL A  1 528  ? -40.003 37.841  105.552 1.00 43.63 ? 526  VAL A CA    1 
ATOM   3782  C C     . VAL A  1 528  ? -40.491 38.378  104.213 1.00 45.73 ? 526  VAL A C     1 
ATOM   3783  O O     . VAL A  1 528  ? -39.685 38.825  103.387 1.00 43.87 ? 526  VAL A O     1 
ATOM   3784  C CB    . VAL A  1 528  ? -39.105 38.852  106.274 1.00 45.95 ? 526  VAL A CB    1 
ATOM   3785  C CG1   . VAL A  1 528  ? -39.840 40.174  106.484 1.00 43.52 ? 526  VAL A CG1   1 
ATOM   3786  C CG2   . VAL A  1 528  ? -38.630 38.272  107.597 1.00 44.98 ? 526  VAL A CG2   1 
ATOM   3787  N N     . VAL A  1 529  ? -41.806 38.309  103.987 1.00 39.65 ? 527  VAL A N     1 
ATOM   3788  C CA    . VAL A  1 529  ? -42.371 38.772  102.724 1.00 44.92 ? 527  VAL A CA    1 
ATOM   3789  C C     . VAL A  1 529  ? -42.101 40.262  102.565 1.00 40.04 ? 527  VAL A C     1 
ATOM   3790  O O     . VAL A  1 529  ? -42.399 41.067  103.456 1.00 38.76 ? 527  VAL A O     1 
ATOM   3791  C CB    . VAL A  1 529  ? -43.875 38.459  102.662 1.00 38.19 ? 527  VAL A CB    1 
ATOM   3792  C CG1   . VAL A  1 529  ? -44.508 39.131  101.448 1.00 37.85 ? 527  VAL A CG1   1 
ATOM   3793  C CG2   . VAL A  1 529  ? -44.101 36.958  102.590 1.00 43.39 ? 527  VAL A CG2   1 
ATOM   3794  N N     . GLY A  1 530  ? -41.506 40.633  101.435 1.00 36.00 ? 528  GLY A N     1 
ATOM   3795  C CA    . GLY A  1 530  ? -41.295 42.036  101.144 1.00 38.90 ? 528  GLY A CA    1 
ATOM   3796  C C     . GLY A  1 530  ? -40.143 42.705  101.859 1.00 35.11 ? 528  GLY A C     1 
ATOM   3797  O O     . GLY A  1 530  ? -40.103 43.937  101.908 1.00 34.17 ? 528  GLY A O     1 
ATOM   3798  N N     . ALA A  1 531  ? -39.198 41.943  102.410 1.00 37.90 ? 529  ALA A N     1 
ATOM   3799  C CA    . ALA A  1 531  ? -38.021 42.550  103.024 1.00 36.86 ? 529  ALA A CA    1 
ATOM   3800  C C     . ALA A  1 531  ? -37.241 43.379  102.006 1.00 34.20 ? 529  ALA A C     1 
ATOM   3801  O O     . ALA A  1 531  ? -37.097 42.985  100.847 1.00 38.96 ? 529  ALA A O     1 
ATOM   3802  C CB    . ALA A  1 531  ? -37.120 41.468  103.629 1.00 36.29 ? 529  ALA A CB    1 
ATOM   3803  N N     . LYS A  1 532  ? -36.759 44.547  102.448 1.00 30.00 ? 530  LYS A N     1 
ATOM   3804  C CA    . LYS A  1 532  ? -35.866 45.393  101.658 1.00 35.38 ? 530  LYS A CA    1 
ATOM   3805  C C     . LYS A  1 532  ? -34.648 44.607  101.178 1.00 34.70 ? 530  LYS A C     1 
ATOM   3806  O O     . LYS A  1 532  ? -34.218 43.638  101.804 1.00 32.41 ? 530  LYS A O     1 
ATOM   3807  C CB    . LYS A  1 532  ? -35.410 46.602  102.500 1.00 36.08 ? 530  LYS A CB    1 
ATOM   3808  C CG    . LYS A  1 532  ? -34.323 47.492  101.863 1.00 40.28 ? 530  LYS A CG    1 
ATOM   3809  C CD    . LYS A  1 532  ? -33.850 48.631  102.773 1.00 34.95 ? 530  LYS A CD    1 
ATOM   3810  C CE    . LYS A  1 532  ? -33.037 48.133  103.965 1.00 39.13 ? 530  LYS A CE    1 
ATOM   3811  N NZ    . LYS A  1 532  ? -31.741 47.508  103.560 1.00 36.25 ? 530  LYS A NZ    1 
ATOM   3812  N N     . HIS A  1 533  ? -34.094 45.035  100.048 1.00 33.31 ? 531  HIS A N     1 
ATOM   3813  C CA    . HIS A  1 533  ? -32.847 44.473  99.549  1.00 34.82 ? 531  HIS A CA    1 
ATOM   3814  C C     . HIS A  1 533  ? -31.722 44.672  100.563 1.00 34.86 ? 531  HIS A C     1 
ATOM   3815  O O     . HIS A  1 533  ? -31.540 45.770  101.093 1.00 32.20 ? 531  HIS A O     1 
ATOM   3816  C CB    . HIS A  1 533  ? -32.488 45.140  98.228  1.00 32.76 ? 531  HIS A CB    1 
ATOM   3817  C CG    . HIS A  1 533  ? -31.454 44.404  97.443  1.00 37.20 ? 531  HIS A CG    1 
ATOM   3818  N ND1   . HIS A  1 533  ? -30.124 44.370  97.811  1.00 38.44 ? 531  HIS A ND1   1 
ATOM   3819  C CD2   . HIS A  1 533  ? -31.550 43.677  96.305  1.00 38.04 ? 531  HIS A CD2   1 
ATOM   3820  C CE1   . HIS A  1 533  ? -29.448 43.648  96.935  1.00 39.66 ? 531  HIS A CE1   1 
ATOM   3821  N NE2   . HIS A  1 533  ? -30.288 43.217  96.011  1.00 41.75 ? 531  HIS A NE2   1 
ATOM   3822  N N     . ASP A  1 534  ? -30.962 43.602  100.828 1.00 36.48 ? 532  ASP A N     1 
ATOM   3823  C CA    . ASP A  1 534  ? -29.939 43.651  101.876 1.00 38.29 ? 532  ASP A CA    1 
ATOM   3824  C C     . ASP A  1 534  ? -28.812 44.628  101.555 1.00 37.40 ? 532  ASP A C     1 
ATOM   3825  O O     . ASP A  1 534  ? -28.130 45.102  102.471 1.00 36.24 ? 532  ASP A O     1 
ATOM   3826  C CB    . ASP A  1 534  ? -29.334 42.266  102.104 1.00 39.90 ? 532  ASP A CB    1 
ATOM   3827  C CG    . ASP A  1 534  ? -30.299 41.310  102.761 1.00 49.56 ? 532  ASP A CG    1 
ATOM   3828  O OD1   . ASP A  1 534  ? -31.247 41.785  103.425 1.00 52.59 ? 532  ASP A OD1   1 
ATOM   3829  O OD2   . ASP A  1 534  ? -30.106 40.081  102.618 1.00 59.55 ? 532  ASP A OD2   1 
ATOM   3830  N N     . ARG A  1 535  ? -28.575 44.914  100.279 1.00 32.91 ? 533  ARG A N     1 
ATOM   3831  C CA    . ARG A  1 535  ? -27.433 45.716  99.863  1.00 33.52 ? 533  ARG A CA    1 
ATOM   3832  C C     . ARG A  1 535  ? -27.806 47.154  99.520  1.00 34.24 ? 533  ARG A C     1 
ATOM   3833  O O     . ARG A  1 535  ? -26.981 47.881  98.954  1.00 35.28 ? 533  ARG A O     1 
ATOM   3834  C CB    . ARG A  1 535  ? -26.733 45.056  98.672  1.00 35.12 ? 533  ARG A CB    1 
ATOM   3835  N N     . ILE A  1 536  ? -29.016 47.592  99.854  1.00 29.28 ? 534  ILE A N     1 
ATOM   3836  C CA    . ILE A  1 536  ? -29.408 48.985  99.686  1.00 33.05 ? 534  ILE A CA    1 
ATOM   3837  C C     . ILE A  1 536  ? -29.697 49.551  101.068 1.00 31.28 ? 534  ILE A C     1 
ATOM   3838  O O     . ILE A  1 536  ? -30.525 49.005  101.803 1.00 35.36 ? 534  ILE A O     1 
ATOM   3839  C CB    . ILE A  1 536  ? -30.632 49.126  98.768  1.00 29.78 ? 534  ILE A CB    1 
ATOM   3840  C CG1   . ILE A  1 536  ? -30.333 48.505  97.406  1.00 34.24 ? 534  ILE A CG1   1 
ATOM   3841  C CG2   . ILE A  1 536  ? -31.062 50.593  98.657  1.00 33.37 ? 534  ILE A CG2   1 
ATOM   3842  C CD1   . ILE A  1 536  ? -31.471 48.641  96.426  1.00 33.23 ? 534  ILE A CD1   1 
ATOM   3843  N N     . ALA A  1 537  ? -29.024 50.643  101.418 1.00 28.31 ? 535  ALA A N     1 
ATOM   3844  C CA    . ALA A  1 537  ? -29.219 51.241  102.730 1.00 32.29 ? 535  ALA A CA    1 
ATOM   3845  C C     . ALA A  1 537  ? -30.417 52.179  102.711 1.00 29.36 ? 535  ALA A C     1 
ATOM   3846  O O     . ALA A  1 537  ? -30.595 52.954  101.771 1.00 28.02 ? 535  ALA A O     1 
ATOM   3847  C CB    . ALA A  1 537  ? -27.967 52.006  103.155 1.00 31.18 ? 535  ALA A CB    1 
ATOM   3848  N N     . LEU A  1 538  ? -31.251 52.101  103.747 1.00 29.91 ? 536  LEU A N     1 
ATOM   3849  C CA    . LEU A  1 538  ? -32.231 53.153  103.942 1.00 26.24 ? 536  LEU A CA    1 
ATOM   3850  C C     . LEU A  1 538  ? -31.499 54.473  104.176 1.00 25.66 ? 536  LEU A C     1 
ATOM   3851  O O     . LEU A  1 538  ? -30.359 54.484  104.652 1.00 27.55 ? 536  LEU A O     1 
ATOM   3852  C CB    . LEU A  1 538  ? -33.146 52.844  105.130 1.00 30.86 ? 536  LEU A CB    1 
ATOM   3853  C CG    . LEU A  1 538  ? -34.179 51.729  104.971 1.00 29.29 ? 536  LEU A CG    1 
ATOM   3854  C CD1   . LEU A  1 538  ? -34.734 51.325  106.328 1.00 34.46 ? 536  LEU A CD1   1 
ATOM   3855  C CD2   . LEU A  1 538  ? -35.322 52.158  104.047 1.00 29.09 ? 536  LEU A CD2   1 
ATOM   3856  N N     . PRO A  1 539  ? -32.125 55.605  103.850 1.00 25.26 ? 537  PRO A N     1 
ATOM   3857  C CA    . PRO A  1 539  ? -31.420 56.884  104.045 1.00 27.54 ? 537  PRO A CA    1 
ATOM   3858  C C     . PRO A  1 539  ? -30.922 57.082  105.469 1.00 25.40 ? 537  PRO A C     1 
ATOM   3859  O O     . PRO A  1 539  ? -29.819 57.605  105.650 1.00 28.03 ? 537  PRO A O     1 
ATOM   3860  C CB    . PRO A  1 539  ? -32.470 57.921  103.634 1.00 24.74 ? 537  PRO A CB    1 
ATOM   3861  C CG    . PRO A  1 539  ? -33.284 57.199  102.586 1.00 24.16 ? 537  PRO A CG    1 
ATOM   3862  C CD    . PRO A  1 539  ? -33.378 55.774  103.094 1.00 25.28 ? 537  PRO A CD    1 
ATOM   3863  N N     . ALA A  1 540  ? -31.682 56.650  106.480 1.00 28.66 ? 538  ALA A N     1 
ATOM   3864  C CA    . ALA A  1 540  ? -31.240 56.802  107.869 1.00 29.50 ? 538  ALA A CA    1 
ATOM   3865  C C     . ALA A  1 540  ? -29.993 55.976  108.168 1.00 32.97 ? 538  ALA A C     1 
ATOM   3866  O O     . ALA A  1 540  ? -29.239 56.294  109.099 1.00 30.68 ? 538  ALA A O     1 
ATOM   3867  C CB    . ALA A  1 540  ? -32.356 56.406  108.836 1.00 35.38 ? 538  ALA A CB    1 
ATOM   3868  N N     . GLU A  1 541  ? -29.773 54.903  107.416 1.00 29.27 ? 539  GLU A N     1 
ATOM   3869  C CA    . GLU A  1 541  ? -28.693 53.971  107.692 1.00 31.50 ? 539  GLU A CA    1 
ATOM   3870  C C     . GLU A  1 541  ? -27.516 54.151  106.748 1.00 30.65 ? 539  GLU A C     1 
ATOM   3871  O O     . GLU A  1 541  ? -26.709 53.228  106.605 1.00 32.44 ? 539  GLU A O     1 
ATOM   3872  C CB    . GLU A  1 541  ? -29.221 52.541  107.629 1.00 32.65 ? 539  GLU A CB    1 
ATOM   3873  C CG    . GLU A  1 541  ? -30.207 52.258  108.761 1.00 40.23 ? 539  GLU A CG    1 
ATOM   3874  C CD    . GLU A  1 541  ? -31.052 51.028  108.507 1.00 47.78 ? 539  GLU A CD    1 
ATOM   3875  O OE1   . GLU A  1 541  ? -30.926 50.445  107.410 1.00 47.21 ? 539  GLU A OE1   1 
ATOM   3876  O OE2   . GLU A  1 541  ? -31.846 50.653  109.397 1.00 49.99 ? 539  GLU A OE2   1 
ATOM   3877  N N     . LEU A  1 542  ? -27.396 55.329  106.121 1.00 29.12 ? 540  LEU A N     1 
ATOM   3878  C CA    . LEU A  1 542  ? -26.344 55.548  105.133 1.00 27.95 ? 540  LEU A CA    1 
ATOM   3879  C C     . LEU A  1 542  ? -24.960 55.340  105.726 1.00 29.58 ? 540  LEU A C     1 
ATOM   3880  O O     . LEU A  1 542  ? -24.053 54.891  105.020 1.00 28.86 ? 540  LEU A O     1 
ATOM   3881  C CB    . LEU A  1 542  ? -26.429 56.962  104.536 1.00 26.18 ? 540  LEU A CB    1 
ATOM   3882  C CG    . LEU A  1 542  ? -26.947 57.178  103.107 1.00 30.26 ? 540  LEU A CG    1 
ATOM   3883  C CD1   . LEU A  1 542  ? -26.510 58.557  102.569 1.00 27.59 ? 540  LEU A CD1   1 
ATOM   3884  C CD2   . LEU A  1 542  ? -26.545 56.048  102.147 1.00 28.88 ? 540  LEU A CD2   1 
ATOM   3885  N N     . PHE A  1 543  ? -24.771 55.669  107.003 1.00 25.36 ? 541  PHE A N     1 
ATOM   3886  C CA    . PHE A  1 543  ? -23.463 55.580  107.631 1.00 28.08 ? 541  PHE A CA    1 
ATOM   3887  C C     . PHE A  1 543  ? -23.326 54.368  108.544 1.00 32.57 ? 541  PHE A C     1 
ATOM   3888  O O     . PHE A  1 543  ? -22.325 54.256  109.262 1.00 30.76 ? 541  PHE A O     1 
ATOM   3889  C CB    . PHE A  1 543  ? -23.176 56.869  108.396 1.00 29.87 ? 541  PHE A CB    1 
ATOM   3890  C CG    . PHE A  1 543  ? -23.373 58.090  107.563 1.00 26.03 ? 541  PHE A CG    1 
ATOM   3891  C CD1   . PHE A  1 543  ? -22.750 58.198  106.337 1.00 30.03 ? 541  PHE A CD1   1 
ATOM   3892  C CD2   . PHE A  1 543  ? -24.230 59.102  107.967 1.00 29.33 ? 541  PHE A CD2   1 
ATOM   3893  C CE1   . PHE A  1 543  ? -22.951 59.308  105.539 1.00 29.13 ? 541  PHE A CE1   1 
ATOM   3894  C CE2   . PHE A  1 543  ? -24.428 60.219  107.169 1.00 28.18 ? 541  PHE A CE2   1 
ATOM   3895  C CZ    . PHE A  1 543  ? -23.796 60.319  105.965 1.00 27.51 ? 541  PHE A CZ    1 
ATOM   3896  N N     . GLY A  1 544  ? -24.300 53.462  108.531 1.00 31.02 ? 542  GLY A N     1 
ATOM   3897  C CA    . GLY A  1 544  ? -24.150 52.215  109.265 1.00 33.55 ? 542  GLY A CA    1 
ATOM   3898  C C     . GLY A  1 544  ? -24.048 52.451  110.761 1.00 35.28 ? 542  GLY A C     1 
ATOM   3899  O O     . GLY A  1 544  ? -24.806 53.229  111.352 1.00 32.84 ? 542  GLY A O     1 
ATOM   3900  N N     . ASP A  1 545  ? -23.083 51.782  111.387 1.00 32.08 ? 543  ASP A N     1 
ATOM   3901  C CA    . ASP A  1 545  ? -22.933 51.866  112.836 1.00 36.54 ? 543  ASP A CA    1 
ATOM   3902  C C     . ASP A  1 545  ? -22.296 53.163  113.319 1.00 34.98 ? 543  ASP A C     1 
ATOM   3903  O O     . ASP A  1 545  ? -22.340 53.439  114.524 1.00 39.27 ? 543  ASP A O     1 
ATOM   3904  C CB    . ASP A  1 545  ? -22.106 50.682  113.342 1.00 38.07 ? 543  ASP A CB    1 
ATOM   3905  C CG    . ASP A  1 545  ? -22.860 49.370  113.242 1.00 50.74 ? 543  ASP A CG    1 
ATOM   3906  O OD1   . ASP A  1 545  ? -24.105 49.412  113.115 1.00 48.35 ? 543  ASP A OD1   1 
ATOM   3907  O OD2   . ASP A  1 545  ? -22.215 48.302  113.295 1.00 62.64 ? 543  ASP A OD2   1 
ATOM   3908  N N     . ALA A  1 546  ? -21.718 53.966  112.430 1.00 33.92 ? 544  ALA A N     1 
ATOM   3909  C CA    . ALA A  1 546  ? -20.967 55.140  112.872 1.00 35.25 ? 544  ALA A CA    1 
ATOM   3910  C C     . ALA A  1 546  ? -21.883 56.186  113.494 1.00 36.00 ? 544  ALA A C     1 
ATOM   3911  O O     . ALA A  1 546  ? -21.582 56.741  114.556 1.00 32.75 ? 544  ALA A O     1 
ATOM   3912  C CB    . ALA A  1 546  ? -20.196 55.742  111.698 1.00 33.78 ? 544  ALA A CB    1 
ATOM   3913  N N     . ARG A  1 547  ? -23.001 56.480  112.838 1.00 30.16 ? 545  ARG A N     1 
ATOM   3914  C CA    . ARG A  1 547  ? -23.916 57.492  113.342 1.00 32.64 ? 545  ARG A CA    1 
ATOM   3915  C C     . ARG A  1 547  ? -25.186 57.426  112.519 1.00 28.34 ? 545  ARG A C     1 
ATOM   3916  O O     . ARG A  1 547  ? -25.210 56.856  111.424 1.00 26.20 ? 545  ARG A O     1 
ATOM   3917  C CB    . ARG A  1 547  ? -23.318 58.898  113.271 1.00 33.38 ? 545  ARG A CB    1 
ATOM   3918  C CG    . ARG A  1 547  ? -23.045 59.322  111.888 1.00 32.83 ? 545  ARG A CG    1 
ATOM   3919  C CD    . ARG A  1 547  ? -22.434 60.694  111.817 1.00 33.99 ? 545  ARG A CD    1 
ATOM   3920  N NE    . ARG A  1 547  ? -21.732 60.825  110.553 1.00 32.97 ? 545  ARG A NE    1 
ATOM   3921  C CZ    . ARG A  1 547  ? -22.121 61.584  109.541 1.00 29.88 ? 545  ARG A CZ    1 
ATOM   3922  N NH1   . ARG A  1 547  ? -23.181 62.372  109.634 1.00 33.67 ? 545  ARG A NH1   1 
ATOM   3923  N NH2   . ARG A  1 547  ? -21.430 61.549  108.409 1.00 31.06 ? 545  ARG A NH2   1 
ATOM   3924  N N     . THR A  1 548  ? -26.236 58.034  113.056 1.00 28.17 ? 546  THR A N     1 
ATOM   3925  C CA    . THR A  1 548  ? -27.527 58.059  112.395 1.00 28.18 ? 546  THR A CA    1 
ATOM   3926  C C     . THR A  1 548  ? -27.589 59.260  111.470 1.00 27.22 ? 546  THR A C     1 
ATOM   3927  O O     . THR A  1 548  ? -27.349 60.393  111.897 1.00 25.48 ? 546  THR A O     1 
ATOM   3928  C CB    . THR A  1 548  ? -28.663 58.111  113.418 1.00 31.22 ? 546  THR A CB    1 
ATOM   3929  O OG1   . THR A  1 548  ? -28.543 56.986  114.291 1.00 32.69 ? 546  THR A OG1   1 
ATOM   3930  C CG2   . THR A  1 548  ? -30.001 58.053  112.706 1.00 28.74 ? 546  THR A CG2   1 
ATOM   3931  N N     . ASN A  1 549  ? -27.899 59.013  110.199 1.00 26.14 ? 547  ASN A N     1 
ATOM   3932  C CA    . ASN A  1 549  ? -28.056 60.120  109.270 1.00 26.20 ? 547  ASN A CA    1 
ATOM   3933  C C     . ASN A  1 549  ? -29.212 61.002  109.724 1.00 22.67 ? 547  ASN A C     1 
ATOM   3934  O O     . ASN A  1 549  ? -30.171 60.533  110.342 1.00 27.30 ? 547  ASN A O     1 
ATOM   3935  C CB    . ASN A  1 549  ? -28.281 59.585  107.848 1.00 23.60 ? 547  ASN A CB    1 
ATOM   3936  C CG    . ASN A  1 549  ? -28.193 60.664  106.789 1.00 26.32 ? 547  ASN A CG    1 
ATOM   3937  O OD1   . ASN A  1 549  ? -27.740 61.778  107.049 1.00 26.88 ? 547  ASN A OD1   1 
ATOM   3938  N ND2   . ASN A  1 549  ? -28.578 60.319  105.562 1.00 23.47 ? 547  ASN A ND2   1 
ATOM   3939  N N     . SER A  1 550  ? -29.109 62.298  109.453 1.00 25.29 ? 548  SER A N     1 
ATOM   3940  C CA    . SER A  1 550  ? -30.241 63.179  109.724 1.00 25.60 ? 548  SER A CA    1 
ATOM   3941  C C     . SER A  1 550  ? -31.354 62.907  108.719 1.00 25.10 ? 548  SER A C     1 
ATOM   3942  O O     . SER A  1 550  ? -31.108 62.455  107.599 1.00 25.91 ? 548  SER A O     1 
ATOM   3943  C CB    . SER A  1 550  ? -29.822 64.650  109.663 1.00 26.51 ? 548  SER A CB    1 
ATOM   3944  O OG    . SER A  1 550  ? -29.325 64.988  108.375 1.00 25.06 ? 548  SER A OG    1 
ATOM   3945  N N     . ALA A  1 551  ? -32.589 63.154  109.142 1.00 26.79 ? 549  ALA A N     1 
ATOM   3946  C CA    . ALA A  1 551  ? -33.763 62.947  108.302 1.00 28.47 ? 549  ALA A CA    1 
ATOM   3947  C C     . ALA A  1 551  ? -34.228 64.275  107.724 1.00 26.21 ? 549  ALA A C     1 
ATOM   3948  O O     . ALA A  1 551  ? -34.258 65.292  108.419 1.00 28.62 ? 549  ALA A O     1 
ATOM   3949  C CB    . ALA A  1 551  ? -34.913 62.311  109.087 1.00 30.63 ? 549  ALA A CB    1 
ATOM   3950  N N     . GLY A  1 552  ? -34.602 64.264  106.451 1.00 26.74 ? 550  GLY A N     1 
ATOM   3951  C CA    . GLY A  1 552  ? -35.160 65.425  105.821 1.00 25.18 ? 550  GLY A CA    1 
ATOM   3952  C C     . GLY A  1 552  ? -36.676 65.416  105.835 1.00 27.06 ? 550  GLY A C     1 
ATOM   3953  O O     . GLY A  1 552  ? -37.321 64.733  106.638 1.00 29.33 ? 550  GLY A O     1 
ATOM   3954  N N     . LEU A  1 553  ? -37.252 66.182  104.912 1.00 27.21 ? 551  LEU A N     1 
ATOM   3955  C CA    . LEU A  1 553  ? -38.694 66.267  104.746 1.00 26.46 ? 551  LEU A CA    1 
ATOM   3956  C C     . LEU A  1 553  ? -39.000 66.295  103.259 1.00 25.16 ? 551  LEU A C     1 
ATOM   3957  O O     . LEU A  1 553  ? -38.278 66.931  102.490 1.00 27.42 ? 551  LEU A O     1 
ATOM   3958  C CB    . LEU A  1 553  ? -39.268 67.521  105.403 1.00 27.69 ? 551  LEU A CB    1 
ATOM   3959  C CG    . LEU A  1 553  ? -39.205 67.670  106.919 1.00 26.49 ? 551  LEU A CG    1 
ATOM   3960  C CD1   . LEU A  1 553  ? -39.754 69.032  107.306 1.00 30.01 ? 551  LEU A CD1   1 
ATOM   3961  C CD2   . LEU A  1 553  ? -39.977 66.570  107.616 1.00 28.94 ? 551  LEU A CD2   1 
ATOM   3962  N N     . ASP A  1 554  ? -40.080 65.632  102.859 1.00 26.95 ? 552  ASP A N     1 
ATOM   3963  C CA    . ASP A  1 554  ? -40.425 65.524  101.441 1.00 27.89 ? 552  ASP A CA    1 
ATOM   3964  C C     . ASP A  1 554  ? -41.385 66.656  101.093 1.00 26.80 ? 552  ASP A C     1 
ATOM   3965  O O     . ASP A  1 554  ? -42.554 66.618  101.475 1.00 25.17 ? 552  ASP A O     1 
ATOM   3966  C CB    . ASP A  1 554  ? -41.042 64.157  101.160 1.00 27.08 ? 552  ASP A CB    1 
ATOM   3967  C CG    . ASP A  1 554  ? -41.299 63.914  99.678  1.00 29.51 ? 552  ASP A CG    1 
ATOM   3968  O OD1   . ASP A  1 554  ? -41.067 64.828  98.850  1.00 30.45 ? 552  ASP A OD1   1 
ATOM   3969  O OD2   . ASP A  1 554  ? -41.730 62.793  99.345  1.00 31.01 ? 552  ASP A OD2   1 
ATOM   3970  N N     . LEU A  1 555  ? -40.898 67.674  100.374 1.00 25.59 ? 553  LEU A N     1 
ATOM   3971  C CA    . LEU A  1 555  ? -41.766 68.797  100.026 1.00 25.38 ? 553  LEU A CA    1 
ATOM   3972  C C     . LEU A  1 555  ? -42.639 68.512  98.807  1.00 27.41 ? 553  LEU A C     1 
ATOM   3973  O O     . LEU A  1 555  ? -43.291 69.431  98.311  1.00 25.46 ? 553  LEU A O     1 
ATOM   3974  C CB    . LEU A  1 555  ? -40.935 70.064  99.802  1.00 25.70 ? 553  LEU A CB    1 
ATOM   3975  C CG    . LEU A  1 555  ? -40.126 70.474  101.037 1.00 28.61 ? 553  LEU A CG    1 
ATOM   3976  C CD1   . LEU A  1 555  ? -39.382 71.785  100.819 1.00 29.75 ? 553  LEU A CD1   1 
ATOM   3977  C CD2   . LEU A  1 555  ? -41.072 70.587  102.250 1.00 30.64 ? 553  LEU A CD2   1 
ATOM   3978  N N     . SER A  1 556  ? -42.656 67.274  98.317  1.00 28.20 ? 554  SER A N     1 
ATOM   3979  C CA    . SER A  1 556  ? -43.623 66.826  97.321  1.00 27.89 ? 554  SER A CA    1 
ATOM   3980  C C     . SER A  1 556  ? -44.760 66.018  97.932  1.00 28.50 ? 554  SER A C     1 
ATOM   3981  O O     . SER A  1 556  ? -45.657 65.574  97.205  1.00 28.26 ? 554  SER A O     1 
ATOM   3982  C CB    . SER A  1 556  ? -42.925 65.984  96.248  1.00 28.74 ? 554  SER A CB    1 
ATOM   3983  O OG    . SER A  1 556  ? -42.618 64.687  96.759  1.00 31.46 ? 554  SER A OG    1 
ATOM   3984  N N     . ASN A  1 557  ? -44.748 65.820  99.246  1.00 28.25 ? 555  ASN A N     1 
ATOM   3985  C CA    . ASN A  1 557  ? -45.740 65.018  99.944  1.00 25.71 ? 555  ASN A CA    1 
ATOM   3986  C C     . ASN A  1 557  ? -46.806 65.941  100.531 1.00 27.41 ? 555  ASN A C     1 
ATOM   3987  O O     . ASN A  1 557  ? -46.500 66.778  101.386 1.00 26.78 ? 555  ASN A O     1 
ATOM   3988  C CB    . ASN A  1 557  ? -45.053 64.201  101.040 1.00 26.47 ? 555  ASN A CB    1 
ATOM   3989  C CG    . ASN A  1 557  ? -46.018 63.328  101.827 1.00 28.47 ? 555  ASN A CG    1 
ATOM   3990  O OD1   . ASN A  1 557  ? -47.056 63.787  102.292 1.00 29.05 ? 555  ASN A OD1   1 
ATOM   3991  N ND2   . ASN A  1 557  ? -45.677 62.054  101.962 1.00 31.82 ? 555  ASN A ND2   1 
ATOM   3992  N N     . GLU A  1 558  ? -48.065 65.761  100.106 1.00 30.50 ? 556  GLU A N     1 
ATOM   3993  C CA    . GLU A  1 558  ? -49.109 66.693  100.528 1.00 27.43 ? 556  GLU A CA    1 
ATOM   3994  C C     . GLU A  1 558  ? -49.293 66.686  102.043 1.00 26.86 ? 556  GLU A C     1 
ATOM   3995  O O     . GLU A  1 558  ? -49.540 67.740  102.645 1.00 30.26 ? 556  GLU A O     1 
ATOM   3996  C CB    . GLU A  1 558  ? -50.437 66.387  99.824  1.00 30.00 ? 556  GLU A CB    1 
ATOM   3997  C CG    . GLU A  1 558  ? -50.468 66.706  98.332  1.00 30.90 ? 556  GLU A CG    1 
ATOM   3998  C CD    . GLU A  1 558  ? -50.276 68.186  97.980  1.00 30.53 ? 556  GLU A CD    1 
ATOM   3999  O OE1   . GLU A  1 558  ? -50.361 69.075  98.866  1.00 28.43 ? 556  GLU A OE1   1 
ATOM   4000  O OE2   . GLU A  1 558  ? -50.038 68.469  96.779  1.00 28.82 ? 556  GLU A OE2   1 
ATOM   4001  N N     . GLU A  1 559  ? -49.188 65.519  102.683 1.00 26.46 ? 557  GLU A N     1 
ATOM   4002  C CA    . GLU A  1 559  ? -49.332 65.496  104.140 1.00 31.27 ? 557  GLU A CA    1 
ATOM   4003  C C     . GLU A  1 559  ? -48.194 66.262  104.805 1.00 28.86 ? 557  GLU A C     1 
ATOM   4004  O O     . GLU A  1 559  ? -48.393 66.942  105.819 1.00 27.55 ? 557  GLU A O     1 
ATOM   4005  C CB    . GLU A  1 559  ? -49.356 64.062  104.676 1.00 28.98 ? 557  GLU A CB    1 
ATOM   4006  C CG    . GLU A  1 559  ? -50.262 63.085  103.973 1.00 30.69 ? 557  GLU A CG    1 
ATOM   4007  C CD    . GLU A  1 559  ? -50.179 61.685  104.571 1.00 41.63 ? 557  GLU A CD    1 
ATOM   4008  O OE1   . GLU A  1 559  ? -49.335 61.468  105.473 1.00 44.11 ? 557  GLU A OE1   1 
ATOM   4009  O OE2   . GLU A  1 559  ? -50.966 60.800  104.155 1.00 40.04 ? 557  GLU A OE2   1 
ATOM   4010  N N     . THR A  1 560  ? -46.989 66.139  104.266 1.00 26.90 ? 558  THR A N     1 
ATOM   4011  C CA    . THR A  1 560  ? -45.879 66.904  104.815 1.00 30.95 ? 558  THR A CA    1 
ATOM   4012  C C     . THR A  1 560  ? -46.096 68.393  104.603 1.00 27.46 ? 558  THR A C     1 
ATOM   4013  O O     . THR A  1 560  ? -45.882 69.193  105.519 1.00 26.55 ? 558  THR A O     1 
ATOM   4014  C CB    . THR A  1 560  ? -44.571 66.445  104.180 1.00 29.20 ? 558  THR A CB    1 
ATOM   4015  O OG1   . THR A  1 560  ? -44.412 65.046  104.430 1.00 30.23 ? 558  THR A OG1   1 
ATOM   4016  C CG2   . THR A  1 560  ? -43.385 67.217  104.748 1.00 26.09 ? 558  THR A CG2   1 
ATOM   4017  N N     . LEU A  1 561  ? -46.553 68.786  103.410 1.00 26.23 ? 559  LEU A N     1 
ATOM   4018  C CA    . LEU A  1 561  ? -46.814 70.206  103.175 1.00 23.66 ? 559  LEU A CA    1 
ATOM   4019  C C     . LEU A  1 561  ? -47.899 70.740  104.106 1.00 30.44 ? 559  LEU A C     1 
ATOM   4020  O O     . LEU A  1 561  ? -47.821 71.888  104.567 1.00 28.87 ? 559  LEU A O     1 
ATOM   4021  C CB    . LEU A  1 561  ? -47.187 70.433  101.708 1.00 25.44 ? 559  LEU A CB    1 
ATOM   4022  C CG    . LEU A  1 561  ? -46.020 70.078  100.782 1.00 23.88 ? 559  LEU A CG    1 
ATOM   4023  C CD1   . LEU A  1 561  ? -46.450 70.136  99.305  1.00 27.91 ? 559  LEU A CD1   1 
ATOM   4024  C CD2   . LEU A  1 561  ? -44.854 71.031  101.046 1.00 25.15 ? 559  LEU A CD2   1 
ATOM   4025  N N     . ALA A  1 562  ? -48.932 69.931  104.382 1.00 28.11 ? 560  ALA A N     1 
ATOM   4026  C CA    . ALA A  1 562  ? -50.022 70.412  105.229 1.00 29.77 ? 560  ALA A CA    1 
ATOM   4027  C C     . ALA A  1 562  ? -49.564 70.563  106.673 1.00 31.09 ? 560  ALA A C     1 
ATOM   4028  O O     . ALA A  1 562  ? -49.896 71.549  107.342 1.00 28.98 ? 560  ALA A O     1 
ATOM   4029  C CB    . ALA A  1 562  ? -51.222 69.462  105.140 1.00 31.80 ? 560  ALA A CB    1 
ATOM   4030  N N     . SER A  1 563  ? -48.795 69.592  107.165 1.00 31.16 ? 561  SER A N     1 
ATOM   4031  C CA    A SER A  1 563  ? -48.265 69.659  108.524 0.61 30.17 ? 561  SER A CA    1 
ATOM   4032  C CA    B SER A  1 563  ? -48.292 69.684  108.531 0.39 30.18 ? 561  SER A CA    1 
ATOM   4033  C C     . SER A  1 563  ? -47.226 70.765  108.660 1.00 33.26 ? 561  SER A C     1 
ATOM   4034  O O     . SER A  1 563  ? -47.173 71.468  109.679 1.00 32.80 ? 561  SER A O     1 
ATOM   4035  C CB    A SER A  1 563  ? -47.654 68.310  108.892 0.61 30.51 ? 561  SER A CB    1 
ATOM   4036  C CB    B SER A  1 563  ? -47.740 68.334  108.977 0.39 30.56 ? 561  SER A CB    1 
ATOM   4037  O OG    A SER A  1 563  ? -47.018 68.368  110.148 0.61 32.62 ? 561  SER A OG    1 
ATOM   4038  O OG    B SER A  1 563  ? -46.717 67.912  108.105 0.39 29.28 ? 561  SER A OG    1 
ATOM   4039  N N     . LEU A  1 564  ? -46.365 70.912  107.651 1.00 28.75 ? 562  LEU A N     1 
ATOM   4040  C CA    . LEU A  1 564  ? -45.358 71.965  107.698 1.00 30.83 ? 562  LEU A CA    1 
ATOM   4041  C C     . LEU A  1 564  ? -46.016 73.343  107.666 1.00 33.22 ? 562  LEU A C     1 
ATOM   4042  O O     . LEU A  1 564  ? -45.598 74.256  108.388 1.00 31.95 ? 562  LEU A O     1 
ATOM   4043  C CB    . LEU A  1 564  ? -44.371 71.782  106.539 1.00 30.26 ? 562  LEU A CB    1 
ATOM   4044  C CG    . LEU A  1 564  ? -43.021 72.475  106.594 1.00 35.72 ? 562  LEU A CG    1 
ATOM   4045  C CD1   . LEU A  1 564  ? -42.325 72.103  107.872 1.00 30.75 ? 562  LEU A CD1   1 
ATOM   4046  C CD2   . LEU A  1 564  ? -42.194 72.042  105.392 1.00 36.16 ? 562  LEU A CD2   1 
ATOM   4047  N N     . THR A  1 565  ? -47.071 73.499  106.862 1.00 26.69 ? 563  THR A N     1 
ATOM   4048  C CA    . THR A  1 565  ? -47.798 74.763  106.829 1.00 32.45 ? 563  THR A CA    1 
ATOM   4049  C C     . THR A  1 565  ? -48.235 75.195  108.230 1.00 33.22 ? 563  THR A C     1 
ATOM   4050  O O     . THR A  1 565  ? -48.047 76.352  108.623 1.00 34.05 ? 563  THR A O     1 
ATOM   4051  C CB    . THR A  1 565  ? -49.008 74.650  105.907 1.00 31.00 ? 563  THR A CB    1 
ATOM   4052  O OG1   . THR A  1 565  ? -48.564 74.448  104.552 1.00 33.82 ? 563  THR A OG1   1 
ATOM   4053  C CG2   . THR A  1 565  ? -49.855 75.923  105.996 1.00 34.39 ? 563  THR A CG2   1 
ATOM   4054  N N     . GLU A  1 566  ? -48.802 74.268  109.006 1.00 32.83 ? 564  GLU A N     1 
ATOM   4055  C CA    . GLU A  1 566  ? -49.242 74.617  110.355 1.00 35.09 ? 564  GLU A CA    1 
ATOM   4056  C C     . GLU A  1 566  ? -48.061 74.944  111.263 1.00 38.06 ? 564  GLU A C     1 
ATOM   4057  O O     . GLU A  1 566  ? -48.107 75.917  112.028 1.00 40.05 ? 564  GLU A O     1 
ATOM   4058  C CB    . GLU A  1 566  ? -50.075 73.483  110.949 1.00 38.96 ? 564  GLU A CB    1 
ATOM   4059  C CG    . GLU A  1 566  ? -51.318 73.163  110.133 1.00 44.41 ? 564  GLU A CG    1 
ATOM   4060  C CD    . GLU A  1 566  ? -52.225 74.380  109.952 1.00 51.92 ? 564  GLU A CD    1 
ATOM   4061  O OE1   . GLU A  1 566  ? -52.493 75.068  110.964 1.00 54.39 ? 564  GLU A OE1   1 
ATOM   4062  O OE2   . GLU A  1 566  ? -52.657 74.654  108.801 1.00 47.67 ? 564  GLU A OE2   1 
ATOM   4063  N N     . ALA A  1 567  ? -46.997 74.146  111.206 1.00 34.82 ? 565  ALA A N     1 
ATOM   4064  C CA    . ALA A  1 567  ? -45.861 74.404  112.083 1.00 36.32 ? 565  ALA A CA    1 
ATOM   4065  C C     . ALA A  1 567  ? -45.223 75.754  111.770 1.00 36.60 ? 565  ALA A C     1 
ATOM   4066  O O     . ALA A  1 567  ? -44.858 76.505  112.685 1.00 36.33 ? 565  ALA A O     1 
ATOM   4067  C CB    . ALA A  1 567  ? -44.839 73.273  111.962 1.00 35.40 ? 565  ALA A CB    1 
ATOM   4068  N N     . LEU A  1 568  ? -45.087 76.083  110.482 1.00 29.07 ? 566  LEU A N     1 
ATOM   4069  C CA    . LEU A  1 568  ? -44.468 77.348  110.109 1.00 33.25 ? 566  LEU A CA    1 
ATOM   4070  C C     . LEU A  1 568  ? -45.304 78.526  110.585 1.00 34.54 ? 566  LEU A C     1 
ATOM   4071  O O     . LEU A  1 568  ? -44.761 79.504  111.113 1.00 36.18 ? 566  LEU A O     1 
ATOM   4072  C CB    . LEU A  1 568  ? -44.248 77.405  108.594 1.00 28.17 ? 566  LEU A CB    1 
ATOM   4073  C CG    . LEU A  1 568  ? -43.340 76.328  108.007 1.00 28.95 ? 566  LEU A CG    1 
ATOM   4074  C CD1   . LEU A  1 568  ? -43.370 76.369  106.483 1.00 29.41 ? 566  LEU A CD1   1 
ATOM   4075  C CD2   . LEU A  1 568  ? -41.892 76.449  108.551 1.00 33.59 ? 566  LEU A CD2   1 
ATOM   4076  N N     . ARG A  1 569  ? -46.629 78.450  110.415 1.00 32.68 ? 567  ARG A N     1 
ATOM   4077  C CA    . ARG A  1 569  ? -47.507 79.487  110.954 1.00 37.90 ? 567  ARG A CA    1 
ATOM   4078  C C     . ARG A  1 569  ? -47.351 79.616  112.465 1.00 39.48 ? 567  ARG A C     1 
ATOM   4079  O O     . ARG A  1 569  ? -47.299 80.730  113.001 1.00 39.10 ? 567  ARG A O     1 
ATOM   4080  C CB    . ARG A  1 569  ? -48.967 79.182  110.611 1.00 36.64 ? 567  ARG A CB    1 
ATOM   4081  C CG    . ARG A  1 569  ? -49.336 79.370  109.144 1.00 42.68 ? 567  ARG A CG    1 
ATOM   4082  C CD    . ARG A  1 569  ? -50.747 78.841  108.887 1.00 45.52 ? 567  ARG A CD    1 
ATOM   4083  N NE    . ARG A  1 569  ? -51.123 78.840  107.476 1.00 48.68 ? 567  ARG A NE    1 
ATOM   4084  C CZ    . ARG A  1 569  ? -52.218 79.416  106.994 1.00 53.63 ? 567  ARG A CZ    1 
ATOM   4085  N NH1   . ARG A  1 569  ? -53.053 80.081  107.779 1.00 48.32 ? 567  ARG A NH1   1 
ATOM   4086  N NH2   . ARG A  1 569  ? -52.489 79.315  105.695 1.00 54.05 ? 567  ARG A NH2   1 
ATOM   4087  N N     . GLU A  1 570  ? -47.286 78.488  113.172 1.00 39.45 ? 568  GLU A N     1 
ATOM   4088  C CA    . GLU A  1 570  ? -47.155 78.550  114.623 1.00 39.48 ? 568  GLU A CA    1 
ATOM   4089  C C     . GLU A  1 570  ? -45.794 79.100  115.041 1.00 44.56 ? 568  GLU A C     1 
ATOM   4090  O O     . GLU A  1 570  ? -45.685 79.754  116.092 1.00 37.98 ? 568  GLU A O     1 
ATOM   4091  C CB    . GLU A  1 570  ? -47.406 77.165  115.225 1.00 41.37 ? 568  GLU A CB    1 
ATOM   4092  C CG    . GLU A  1 570  ? -48.879 76.773  115.214 1.00 49.91 ? 568  GLU A CG    1 
ATOM   4093  C CD    . GLU A  1 570  ? -49.107 75.288  115.417 1.00 51.75 ? 568  GLU A CD    1 
ATOM   4094  O OE1   . GLU A  1 570  ? -48.176 74.505  115.139 1.00 57.31 ? 568  GLU A OE1   1 
ATOM   4095  O OE2   . GLU A  1 570  ? -50.220 74.906  115.848 1.00 59.35 ? 568  GLU A OE2   1 
ATOM   4096  N N     . SER A  1 571  ? -44.756 78.869  114.228 1.00 38.04 ? 569  SER A N     1 
ATOM   4097  C CA    . SER A  1 571  ? -43.442 79.422  114.542 1.00 40.49 ? 569  SER A CA    1 
ATOM   4098  C C     . SER A  1 571  ? -43.437 80.940  114.441 1.00 39.31 ? 569  SER A C     1 
ATOM   4099  O O     . SER A  1 571  ? -42.731 81.603  115.203 1.00 38.55 ? 569  SER A O     1 
ATOM   4100  C CB    . SER A  1 571  ? -42.371 78.835  113.619 1.00 37.77 ? 569  SER A CB    1 
ATOM   4101  O OG    . SER A  1 571  ? -42.362 79.497  112.361 1.00 35.11 ? 569  SER A OG    1 
ATOM   4102  N N     . ALA A  1 572  ? -44.216 81.510  113.522 1.00 39.13 ? 570  ALA A N     1 
ATOM   4103  C CA    . ALA A  1 572  ? -44.243 82.960  113.373 1.00 38.77 ? 570  ALA A CA    1 
ATOM   4104  C C     . ALA A  1 572  ? -45.089 83.650  114.433 1.00 41.19 ? 570  ALA A C     1 
ATOM   4105  O O     . ALA A  1 572  ? -45.116 84.884  114.474 1.00 42.38 ? 570  ALA A O     1 
ATOM   4106  C CB    . ALA A  1 572  ? -44.753 83.341  111.981 1.00 41.21 ? 570  ALA A CB    1 
ATOM   4107  N N     . ALA A  1 573  ? -45.777 82.887  115.279 1.00 42.08 ? 571  ALA A N     1 
ATOM   4108  C CA    . ALA A  1 573  ? -46.536 83.423  116.401 1.00 44.08 ? 571  ALA A CA    1 
ATOM   4109  C C     . ALA A  1 573  ? -45.750 83.395  117.701 1.00 47.38 ? 571  ALA A C     1 
ATOM   4110  O O     . ALA A  1 573  ? -46.288 83.766  118.749 1.00 51.63 ? 571  ALA A O     1 
ATOM   4111  C CB    . ALA A  1 573  ? -47.842 82.643  116.576 1.00 42.11 ? 571  ALA A CB    1 
ATOM   4112  N N     . MET A  1 574  ? -44.500 82.957  117.665 1.00 44.20 ? 572  MET A N     1 
ATOM   4113  C CA    . MET A  1 574  ? -43.688 82.864  118.866 1.00 48.06 ? 572  MET A CA    1 
ATOM   4114  C C     . MET A  1 574  ? -42.868 84.134  119.026 1.00 46.28 ? 572  MET A C     1 
ATOM   4115  O O     . MET A  1 574  ? -42.404 84.714  118.040 1.00 42.05 ? 572  MET A O     1 
ATOM   4116  C CB    . MET A  1 574  ? -42.772 81.646  118.801 1.00 46.05 ? 572  MET A CB    1 
ATOM   4117  C CG    . MET A  1 574  ? -43.512 80.331  118.651 1.00 47.10 ? 572  MET A CG    1 
ATOM   4118  S SD    . MET A  1 574  ? -42.355 78.979  118.433 1.00 52.36 ? 572  MET A SD    1 
ATOM   4119  C CE    . MET A  1 574  ? -43.460 77.580  118.237 1.00 53.64 ? 572  MET A CE    1 
ATOM   4120  N N     . LYS A  1 575  ? -42.715 84.575  120.277 1.00 41.94 ? 573  LYS A N     1 
ATOM   4121  C CA    . LYS A  1 575  ? -41.935 85.772  120.589 1.00 43.51 ? 573  LYS A CA    1 
ATOM   4122  C C     . LYS A  1 575  ? -40.480 85.358  120.808 1.00 41.75 ? 573  LYS A C     1 
ATOM   4123  O O     . LYS A  1 575  ? -39.983 85.248  121.930 1.00 42.32 ? 573  LYS A O     1 
ATOM   4124  C CB    . LYS A  1 575  ? -42.514 86.493  121.800 1.00 47.35 ? 573  LYS A CB    1 
ATOM   4125  C CG    . LYS A  1 575  ? -43.905 87.083  121.584 1.00 52.87 ? 573  LYS A CG    1 
ATOM   4126  C CD    . LYS A  1 575  ? -43.944 88.011  120.373 1.00 52.59 ? 573  LYS A CD    1 
ATOM   4127  C CE    . LYS A  1 575  ? -45.182 88.895  120.393 1.00 56.79 ? 573  LYS A CE    1 
ATOM   4128  N NZ    . LYS A  1 575  ? -45.261 89.742  119.173 1.00 62.56 ? 573  LYS A NZ    1 
ATOM   4129  N N     . TRP A  1 576  ? -39.792 85.119  119.695 1.00 38.35 ? 574  TRP A N     1 
ATOM   4130  C CA    . TRP A  1 576  ? -38.382 84.750  119.739 1.00 35.96 ? 574  TRP A CA    1 
ATOM   4131  C C     . TRP A  1 576  ? -37.545 85.873  120.345 1.00 36.15 ? 574  TRP A C     1 
ATOM   4132  O O     . TRP A  1 576  ? -37.770 87.055  120.062 1.00 36.66 ? 574  TRP A O     1 
ATOM   4133  C CB    . TRP A  1 576  ? -37.885 84.443  118.328 1.00 36.60 ? 574  TRP A CB    1 
ATOM   4134  C CG    . TRP A  1 576  ? -38.595 83.317  117.639 1.00 34.98 ? 574  TRP A CG    1 
ATOM   4135  C CD1   . TRP A  1 576  ? -39.554 83.422  116.671 1.00 35.27 ? 574  TRP A CD1   1 
ATOM   4136  C CD2   . TRP A  1 576  ? -38.382 81.913  117.840 1.00 31.37 ? 574  TRP A CD2   1 
ATOM   4137  N NE1   . TRP A  1 576  ? -39.951 82.174  116.257 1.00 33.79 ? 574  TRP A NE1   1 
ATOM   4138  C CE2   . TRP A  1 576  ? -39.257 81.228  116.962 1.00 31.68 ? 574  TRP A CE2   1 
ATOM   4139  C CE3   . TRP A  1 576  ? -37.546 81.169  118.682 1.00 32.10 ? 574  TRP A CE3   1 
ATOM   4140  C CZ2   . TRP A  1 576  ? -39.318 79.836  116.897 1.00 33.99 ? 574  TRP A CZ2   1 
ATOM   4141  C CZ3   . TRP A  1 576  ? -37.604 79.781  118.622 1.00 36.73 ? 574  TRP A CZ3   1 
ATOM   4142  C CH2   . TRP A  1 576  ? -38.489 79.128  117.735 1.00 39.65 ? 574  TRP A CH2   1 
ATOM   4143  N N     . THR A  1 577  ? -36.592 85.505  121.202 1.00 33.56 ? 575  THR A N     1 
ATOM   4144  C CA    . THR A  1 577  ? -35.619 86.459  121.721 1.00 33.30 ? 575  THR A CA    1 
ATOM   4145  C C     . THR A  1 577  ? -34.224 85.850  121.749 1.00 34.74 ? 575  THR A C     1 
ATOM   4146  O O     . THR A  1 577  ? -34.032 84.637  121.610 1.00 34.98 ? 575  THR A O     1 
ATOM   4147  C CB    . THR A  1 577  ? -35.950 86.954  123.140 1.00 39.82 ? 575  THR A CB    1 
ATOM   4148  O OG1   . THR A  1 577  ? -35.862 85.861  124.062 1.00 36.66 ? 575  THR A OG1   1 
ATOM   4149  C CG2   . THR A  1 577  ? -37.328 87.587  123.199 1.00 40.16 ? 575  THR A CG2   1 
ATOM   4150  N N     . ALA A  1 578  ? -33.245 86.731  121.904 1.00 33.69 ? 576  ALA A N     1 
ATOM   4151  C CA    . ALA A  1 578  ? -31.844 86.359  122.077 1.00 32.03 ? 576  ALA A CA    1 
ATOM   4152  C C     . ALA A  1 578  ? -31.266 87.326  123.091 1.00 37.02 ? 576  ALA A C     1 
ATOM   4153  O O     . ALA A  1 578  ? -31.411 88.541  122.928 1.00 35.83 ? 576  ALA A O     1 
ATOM   4154  C CB    . ALA A  1 578  ? -31.056 86.441  120.767 1.00 31.02 ? 576  ALA A CB    1 
ATOM   4155  N N     . LEU A  1 579  ? -30.636 86.794  124.129 1.00 40.15 ? 577  LEU A N     1 
ATOM   4156  C CA    . LEU A  1 579  ? -30.137 87.578  125.247 1.00 39.23 ? 577  LEU A CA    1 
ATOM   4157  C C     . LEU A  1 579  ? -28.693 87.203  125.513 1.00 36.76 ? 577  LEU A C     1 
ATOM   4158  O O     . LEU A  1 579  ? -28.254 86.104  125.157 1.00 39.81 ? 577  LEU A O     1 
ATOM   4159  C CB    . LEU A  1 579  ? -30.964 87.330  126.518 1.00 39.73 ? 577  LEU A CB    1 
ATOM   4160  C CG    . LEU A  1 579  ? -32.484 87.325  126.378 1.00 44.98 ? 577  LEU A CG    1 
ATOM   4161  C CD1   . LEU A  1 579  ? -33.107 86.845  127.674 1.00 47.62 ? 577  LEU A CD1   1 
ATOM   4162  C CD2   . LEU A  1 579  ? -32.998 88.710  126.015 1.00 46.39 ? 577  LEU A CD2   1 
ATOM   4163  N N     . PRO A  1 580  ? -27.921 88.094  126.146 1.00 39.07 ? 578  PRO A N     1 
ATOM   4164  C CA    . PRO A  1 580  ? -26.597 87.692  126.632 1.00 39.35 ? 578  PRO A CA    1 
ATOM   4165  C C     . PRO A  1 580  ? -26.769 86.682  127.749 1.00 40.57 ? 578  PRO A C     1 
ATOM   4166  O O     . PRO A  1 580  ? -27.130 87.042  128.876 1.00 44.38 ? 578  PRO A O     1 
ATOM   4167  C CB    . PRO A  1 580  ? -25.975 89.005  127.129 1.00 40.97 ? 578  PRO A CB    1 
ATOM   4168  C CG    . PRO A  1 580  ? -26.877 90.102  126.625 1.00 38.57 ? 578  PRO A CG    1 
ATOM   4169  C CD    . PRO A  1 580  ? -28.226 89.495  126.468 1.00 36.00 ? 578  PRO A CD    1 
ATOM   4170  N N     . GLN A  1 581  ? -26.565 85.411  127.431 1.00 37.89 ? 579  GLN A N     1 
ATOM   4171  C CA    . GLN A  1 581  ? -26.807 84.318  128.366 1.00 38.11 ? 579  GLN A CA    1 
ATOM   4172  C C     . GLN A  1 581  ? -25.477 83.988  129.025 1.00 40.92 ? 579  GLN A C     1 
ATOM   4173  O O     . GLN A  1 581  ? -24.732 83.135  128.556 1.00 36.30 ? 579  GLN A O     1 
ATOM   4174  C CB    . GLN A  1 581  ? -27.403 83.109  127.647 1.00 38.50 ? 579  GLN A CB    1 
ATOM   4175  C CG    . GLN A  1 581  ? -28.752 83.374  126.961 1.00 37.59 ? 579  GLN A CG    1 
ATOM   4176  C CD    . GLN A  1 581  ? -29.897 83.587  127.953 1.00 44.27 ? 579  GLN A CD    1 
ATOM   4177  O OE1   . GLN A  1 581  ? -30.984 84.034  127.577 1.00 43.40 ? 579  GLN A OE1   1 
ATOM   4178  N NE2   . GLN A  1 581  ? -29.661 83.260  129.217 1.00 40.78 ? 579  GLN A NE2   1 
ATOM   4179  N N     . LEU A  1 582  ? -25.176 84.682  130.119 1.00 41.00 ? 580  LEU A N     1 
ATOM   4180  C CA    . LEU A  1 582  ? -23.927 84.455  130.828 1.00 42.39 ? 580  LEU A CA    1 
ATOM   4181  C C     . LEU A  1 582  ? -24.041 83.232  131.741 1.00 41.95 ? 580  LEU A C     1 
ATOM   4182  O O     . LEU A  1 582  ? -25.124 82.681  131.962 1.00 40.00 ? 580  LEU A O     1 
ATOM   4183  C CB    . LEU A  1 582  ? -23.534 85.694  131.633 1.00 41.47 ? 580  LEU A CB    1 
ATOM   4184  C CG    . LEU A  1 582  ? -22.653 86.715  130.903 1.00 47.31 ? 580  LEU A CG    1 
ATOM   4185  C CD1   . LEU A  1 582  ? -23.377 87.345  129.719 1.00 48.22 ? 580  LEU A CD1   1 
ATOM   4186  C CD2   . LEU A  1 582  ? -22.174 87.786  131.868 1.00 44.58 ? 580  LEU A CD2   1 
ATOM   4187  N N     . ALA A  1 583  ? -22.891 82.798  132.267 1.00 40.51 ? 581  ALA A N     1 
ATOM   4188  C CA    . ALA A  1 583  ? -22.884 81.667  133.189 1.00 42.40 ? 581  ALA A CA    1 
ATOM   4189  C C     . ALA A  1 583  ? -23.804 81.923  134.375 1.00 47.02 ? 581  ALA A C     1 
ATOM   4190  O O     . ALA A  1 583  ? -24.469 81.004  134.866 1.00 48.50 ? 581  ALA A O     1 
ATOM   4191  C CB    . ALA A  1 583  ? -21.460 81.387  133.668 1.00 47.50 ? 581  ALA A CB    1 
ATOM   4192  N N     . THR A  1 584  ? -23.869 83.175  134.830 1.00 45.85 ? 582  THR A N     1 
ATOM   4193  C CA    . THR A  1 584  ? -24.649 83.554  136.004 1.00 50.58 ? 582  THR A CA    1 
ATOM   4194  C C     . THR A  1 584  ? -26.137 83.718  135.709 1.00 47.58 ? 582  THR A C     1 
ATOM   4195  O O     . THR A  1 584  ? -26.946 83.687  136.645 1.00 51.61 ? 582  THR A O     1 
ATOM   4196  C CB    . THR A  1 584  ? -24.104 84.861  136.577 1.00 53.72 ? 582  THR A CB    1 
ATOM   4197  O OG1   . THR A  1 584  ? -23.962 85.814  135.512 1.00 52.53 ? 582  THR A OG1   1 
ATOM   4198  C CG2   . THR A  1 584  ? -22.753 84.637  137.240 1.00 52.64 ? 582  THR A CG2   1 
ATOM   4199  N N     . GLY A  1 585  ? -26.510 83.888  134.439 1.00 48.89 ? 583  GLY A N     1 
ATOM   4200  C CA    . GLY A  1 585  ? -27.887 84.084  134.043 1.00 48.64 ? 583  GLY A CA    1 
ATOM   4201  C C     . GLY A  1 585  ? -27.997 85.080  132.903 1.00 48.64 ? 583  GLY A C     1 
ATOM   4202  O O     . GLY A  1 585  ? -26.994 85.630  132.436 1.00 51.93 ? 583  GLY A O     1 
ATOM   4203  N N     . PRO A  1 586  ? -29.217 85.323  132.420 1.00 49.16 ? 584  PRO A N     1 
ATOM   4204  C CA    . PRO A  1 586  ? -29.403 86.359  131.396 1.00 45.84 ? 584  PRO A CA    1 
ATOM   4205  C C     . PRO A  1 586  ? -28.929 87.715  131.900 1.00 50.08 ? 584  PRO A C     1 
ATOM   4206  O O     . PRO A  1 586  ? -28.988 88.009  133.093 1.00 48.16 ? 584  PRO A O     1 
ATOM   4207  C CB    . PRO A  1 586  ? -30.916 86.345  131.142 1.00 47.09 ? 584  PRO A CB    1 
ATOM   4208  C CG    . PRO A  1 586  ? -31.508 85.666  132.334 1.00 49.27 ? 584  PRO A CG    1 
ATOM   4209  C CD    . PRO A  1 586  ? -30.486 84.674  132.790 1.00 48.13 ? 584  PRO A CD    1 
ATOM   4210  N N     . ALA A  1 587  ? -28.424 88.534  130.977 1.00 47.20 ? 585  ALA A N     1 
ATOM   4211  C CA    . ALA A  1 587  ? -27.910 89.859  131.298 1.00 47.45 ? 585  ALA A CA    1 
ATOM   4212  C C     . ALA A  1 587  ? -28.699 90.925  130.551 1.00 50.32 ? 585  ALA A C     1 
ATOM   4213  O O     . ALA A  1 587  ? -29.285 90.660  129.499 1.00 52.33 ? 585  ALA A O     1 
ATOM   4214  C CB    . ALA A  1 587  ? -26.414 89.978  130.954 1.00 49.18 ? 585  ALA A CB    1 
ATOM   4215  N N     . ALA A  1 588  ? -28.707 92.135  131.102 1.00 50.54 ? 586  ALA A N     1 
ATOM   4216  C CA    . ALA A  1 588  ? -29.406 93.253  130.488 1.00 52.63 ? 586  ALA A CA    1 
ATOM   4217  C C     . ALA A  1 588  ? -28.521 93.939  129.450 1.00 56.01 ? 586  ALA A C     1 
ATOM   4218  O O     . ALA A  1 588  ? -27.302 93.754  129.416 1.00 53.34 ? 586  ALA A O     1 
ATOM   4219  C CB    . ALA A  1 588  ? -29.845 94.261  131.552 1.00 57.40 ? 586  ALA A CB    1 
ATOM   4220  N N     . GLY A  1 589  ? -29.151 94.738  128.596 1.00 54.18 ? 587  GLY A N     1 
ATOM   4221  C CA    . GLY A  1 589  ? -28.409 95.456  127.581 1.00 50.69 ? 587  GLY A CA    1 
ATOM   4222  C C     . GLY A  1 589  ? -29.342 96.161  126.618 1.00 53.35 ? 587  GLY A C     1 
ATOM   4223  O O     . GLY A  1 589  ? -30.557 96.228  126.830 1.00 53.09 ? 587  GLY A O     1 
ATOM   4224  N N     . GLU A  1 590  ? -28.740 96.686  125.551 1.00 51.90 ? 588  GLU A N     1 
ATOM   4225  C CA    . GLU A  1 590  ? -29.488 97.392  124.518 1.00 49.45 ? 588  GLU A CA    1 
ATOM   4226  C C     . GLU A  1 590  ? -30.284 96.394  123.685 1.00 51.32 ? 588  GLU A C     1 
ATOM   4227  O O     . GLU A  1 590  ? -29.710 95.474  123.087 1.00 47.78 ? 588  GLU A O     1 
ATOM   4228  C CB    . GLU A  1 590  ? -28.532 98.195  123.638 1.00 55.93 ? 588  GLU A CB    1 
ATOM   4229  N N     . THR A  1 591  ? -31.601 96.583  123.639 1.00 44.91 ? 589  THR A N     1 
ATOM   4230  C CA    . THR A  1 591  ? -32.531 95.667  122.987 1.00 46.99 ? 589  THR A CA    1 
ATOM   4231  C C     . THR A  1 591  ? -33.089 96.309  121.723 1.00 47.68 ? 589  THR A C     1 
ATOM   4232  O O     . THR A  1 591  ? -33.533 97.461  121.752 1.00 48.14 ? 589  THR A O     1 
ATOM   4233  C CB    . THR A  1 591  ? -33.684 95.297  123.929 1.00 47.74 ? 589  THR A CB    1 
ATOM   4234  O OG1   . THR A  1 591  ? -33.161 94.741  125.145 1.00 48.55 ? 589  THR A OG1   1 
ATOM   4235  C CG2   . THR A  1 591  ? -34.620 94.289  123.272 1.00 41.03 ? 589  THR A CG2   1 
ATOM   4236  N N     . ARG A  1 592  ? -33.077 95.561  120.621 1.00 43.65 ? 590  ARG A N     1 
ATOM   4237  C CA    . ARG A  1 592  ? -33.684 96.022  119.385 1.00 43.95 ? 590  ARG A CA    1 
ATOM   4238  C C     . ARG A  1 592  ? -34.352 94.840  118.692 1.00 43.25 ? 590  ARG A C     1 
ATOM   4239  O O     . ARG A  1 592  ? -34.094 93.678  119.015 1.00 40.91 ? 590  ARG A O     1 
ATOM   4240  C CB    . ARG A  1 592  ? -32.646 96.670  118.460 1.00 49.48 ? 590  ARG A CB    1 
ATOM   4241  C CG    . ARG A  1 592  ? -31.566 95.702  118.019 1.00 48.48 ? 590  ARG A CG    1 
ATOM   4242  C CD    . ARG A  1 592  ? -30.751 96.236  116.851 1.00 54.72 ? 590  ARG A CD    1 
ATOM   4243  N NE    . ARG A  1 592  ? -29.752 95.262  116.432 1.00 53.53 ? 590  ARG A NE    1 
ATOM   4244  C CZ    . ARG A  1 592  ? -29.990 94.249  115.610 1.00 51.89 ? 590  ARG A CZ    1 
ATOM   4245  N NH1   . ARG A  1 592  ? -31.175 94.081  115.043 1.00 49.95 ? 590  ARG A NH1   1 
ATOM   4246  N NH2   . ARG A  1 592  ? -29.017 93.378  115.357 1.00 50.51 ? 590  ARG A NH2   1 
ATOM   4247  N N     . THR A  1 593  ? -35.204 95.145  117.718 1.00 42.56 ? 591  THR A N     1 
ATOM   4248  C CA    . THR A  1 593  ? -35.931 94.087  117.039 1.00 41.78 ? 591  THR A CA    1 
ATOM   4249  C C     . THR A  1 593  ? -35.084 93.454  115.929 1.00 42.33 ? 591  THR A C     1 
ATOM   4250  O O     . THR A  1 593  ? -34.083 94.011  115.468 1.00 39.23 ? 591  THR A O     1 
ATOM   4251  C CB    . THR A  1 593  ? -37.234 94.623  116.461 1.00 45.20 ? 591  THR A CB    1 
ATOM   4252  O OG1   . THR A  1 593  ? -36.946 95.684  115.539 1.00 45.69 ? 591  THR A OG1   1 
ATOM   4253  C CG2   . THR A  1 593  ? -38.123 95.145  117.579 1.00 46.06 ? 591  THR A CG2   1 
ATOM   4254  N N     . VAL A  1 594  ? -35.499 92.262  115.514 1.00 36.58 ? 592  VAL A N     1 
ATOM   4255  C CA    . VAL A  1 594  ? -34.886 91.539  114.408 1.00 37.43 ? 592  VAL A CA    1 
ATOM   4256  C C     . VAL A  1 594  ? -35.925 91.465  113.301 1.00 39.59 ? 592  VAL A C     1 
ATOM   4257  O O     . VAL A  1 594  ? -37.078 91.085  113.548 1.00 37.16 ? 592  VAL A O     1 
ATOM   4258  C CB    . VAL A  1 594  ? -34.410 90.141  114.841 1.00 33.13 ? 592  VAL A CB    1 
ATOM   4259  C CG1   . VAL A  1 594  ? -33.801 89.389  113.663 1.00 28.91 ? 592  VAL A CG1   1 
ATOM   4260  C CG2   . VAL A  1 594  ? -33.404 90.255  115.983 1.00 35.10 ? 592  VAL A CG2   1 
ATOM   4261  N N     . LEU A  1 595  ? -35.537 91.870  112.094 1.00 39.65 ? 593  LEU A N     1 
ATOM   4262  C CA    . LEU A  1 595  ? -36.473 92.019  110.989 1.00 36.40 ? 593  LEU A CA    1 
ATOM   4263  C C     . LEU A  1 595  ? -36.237 90.944  109.933 1.00 33.81 ? 593  LEU A C     1 
ATOM   4264  O O     . LEU A  1 595  ? -35.117 90.454  109.762 1.00 34.13 ? 593  LEU A O     1 
ATOM   4265  C CB    . LEU A  1 595  ? -36.353 93.410  110.357 1.00 39.82 ? 593  LEU A CB    1 
ATOM   4266  C CG    . LEU A  1 595  ? -36.564 94.616  111.282 1.00 41.44 ? 593  LEU A CG    1 
ATOM   4267  C CD1   . LEU A  1 595  ? -36.318 95.919  110.529 1.00 48.59 ? 593  LEU A CD1   1 
ATOM   4268  C CD2   . LEU A  1 595  ? -37.954 94.595  111.895 1.00 35.74 ? 593  LEU A CD2   1 
ATOM   4269  N N     . ASN A  1 596  ? -37.315 90.573  109.241 1.00 31.83 ? 594  ASN A N     1 
ATOM   4270  C CA    . ASN A  1 596  ? -37.254 89.612  108.136 1.00 34.27 ? 594  ASN A CA    1 
ATOM   4271  C C     . ASN A  1 596  ? -36.615 90.285  106.926 1.00 31.13 ? 594  ASN A C     1 
ATOM   4272  O O     . ASN A  1 596  ? -37.103 91.339  106.495 1.00 33.15 ? 594  ASN A O     1 
ATOM   4273  C CB    . ASN A  1 596  ? -38.676 89.121  107.829 1.00 31.33 ? 594  ASN A CB    1 
ATOM   4274  C CG    . ASN A  1 596  ? -38.744 88.099  106.696 1.00 33.01 ? 594  ASN A CG    1 
ATOM   4275  O OD1   . ASN A  1 596  ? -37.910 88.076  105.795 1.00 33.53 ? 594  ASN A OD1   1 
ATOM   4276  N ND2   . ASN A  1 596  ? -39.769 87.257  106.738 1.00 34.91 ? 594  ASN A ND2   1 
ATOM   4277  N N     . PRO A  1 597  ? -35.528 89.738  106.360 1.00 31.01 ? 595  PRO A N     1 
ATOM   4278  C CA    . PRO A  1 597  ? -34.865 90.429  105.239 1.00 30.01 ? 595  PRO A CA    1 
ATOM   4279  C C     . PRO A  1 597  ? -35.723 90.497  103.987 1.00 32.34 ? 595  PRO A C     1 
ATOM   4280  O O     . PRO A  1 597  ? -35.466 91.348  103.122 1.00 31.04 ? 595  PRO A O     1 
ATOM   4281  C CB    . PRO A  1 597  ? -33.588 89.603  105.013 1.00 32.28 ? 595  PRO A CB    1 
ATOM   4282  C CG    . PRO A  1 597  ? -33.868 88.273  105.628 1.00 33.24 ? 595  PRO A CG    1 
ATOM   4283  C CD    . PRO A  1 597  ? -34.793 88.528  106.779 1.00 27.65 ? 595  PRO A CD    1 
ATOM   4284  N N     . GLY A  1 598  ? -36.755 89.660  103.880 1.00 30.62 ? 596  GLY A N     1 
ATOM   4285  C CA    . GLY A  1 598  ? -37.658 89.713  102.747 1.00 30.73 ? 596  GLY A CA    1 
ATOM   4286  C C     . GLY A  1 598  ? -38.806 90.677  102.899 1.00 34.19 ? 596  GLY A C     1 
ATOM   4287  O O     . GLY A  1 598  ? -39.517 90.943  101.929 1.00 32.24 ? 596  GLY A O     1 
ATOM   4288  N N     . ASP A  1 599  ? -38.990 91.219  104.098 1.00 32.01 ? 597  ASP A N     1 
ATOM   4289  C CA    . ASP A  1 599  ? -40.101 92.110  104.400 1.00 34.70 ? 597  ASP A CA    1 
ATOM   4290  C C     . ASP A  1 599  ? -39.852 92.733  105.762 1.00 33.78 ? 597  ASP A C     1 
ATOM   4291  O O     . ASP A  1 599  ? -40.145 92.118  106.794 1.00 34.93 ? 597  ASP A O     1 
ATOM   4292  C CB    . ASP A  1 599  ? -41.421 91.344  104.391 1.00 34.64 ? 597  ASP A CB    1 
ATOM   4293  C CG    . ASP A  1 599  ? -42.643 92.252  104.448 1.00 38.89 ? 597  ASP A CG    1 
ATOM   4294  O OD1   . ASP A  1 599  ? -42.510 93.466  104.710 1.00 37.60 ? 597  ASP A OD1   1 
ATOM   4295  O OD2   . ASP A  1 599  ? -43.750 91.728  104.216 1.00 41.95 ? 597  ASP A OD2   1 
ATOM   4296  N N     . HIS A  1 600  ? -39.303 93.945  105.770 1.00 34.69 ? 598  HIS A N     1 
ATOM   4297  C CA    . HIS A  1 600  ? -38.918 94.593  107.019 1.00 39.98 ? 598  HIS A CA    1 
ATOM   4298  C C     . HIS A  1 600  ? -40.109 94.908  107.921 1.00 41.74 ? 598  HIS A C     1 
ATOM   4299  O O     . HIS A  1 600  ? -39.904 95.196  109.106 1.00 45.54 ? 598  HIS A O     1 
ATOM   4300  C CB    . HIS A  1 600  ? -38.120 95.864  106.711 1.00 38.44 ? 598  HIS A CB    1 
ATOM   4301  C CG    . HIS A  1 600  ? -36.708 95.597  106.286 1.00 37.63 ? 598  HIS A CG    1 
ATOM   4302  N ND1   . HIS A  1 600  ? -35.757 96.591  106.184 1.00 41.61 ? 598  HIS A ND1   1 
ATOM   4303  C CD2   . HIS A  1 600  ? -36.082 94.445  105.945 1.00 38.66 ? 598  HIS A CD2   1 
ATOM   4304  C CE1   . HIS A  1 600  ? -34.607 96.064  105.803 1.00 41.85 ? 598  HIS A CE1   1 
ATOM   4305  N NE2   . HIS A  1 600  ? -34.777 94.763  105.646 1.00 41.83 ? 598  HIS A NE2   1 
ATOM   4306  N N     . ARG A  1 601  ? -41.340 94.839  107.401 1.00 41.48 ? 599  ARG A N     1 
ATOM   4307  C CA    . ARG A  1 601  ? -42.531 94.976  108.240 1.00 43.98 ? 599  ARG A CA    1 
ATOM   4308  C C     . ARG A  1 601  ? -42.740 93.779  109.164 1.00 41.78 ? 599  ARG A C     1 
ATOM   4309  O O     . ARG A  1 601  ? -43.420 93.913  110.185 1.00 39.72 ? 599  ARG A O     1 
ATOM   4310  C CB    . ARG A  1 601  ? -43.771 95.155  107.363 1.00 41.00 ? 599  ARG A CB    1 
ATOM   4311  C CG    . ARG A  1 601  ? -43.703 96.330  106.405 1.00 40.21 ? 599  ARG A CG    1 
ATOM   4312  C CD    . ARG A  1 601  ? -44.830 96.273  105.390 1.00 38.35 ? 599  ARG A CD    1 
ATOM   4313  N NE    . ARG A  1 601  ? -44.818 95.022  104.643 1.00 41.95 ? 599  ARG A NE    1 
ATOM   4314  C CZ    . ARG A  1 601  ? -45.657 94.731  103.658 1.00 46.19 ? 599  ARG A CZ    1 
ATOM   4315  N NH1   . ARG A  1 601  ? -46.588 95.589  103.265 1.00 45.18 ? 599  ARG A NH1   1 
ATOM   4316  N NH2   . ARG A  1 601  ? -45.555 93.556  103.048 1.00 43.18 ? 599  ARG A NH2   1 
ATOM   4317  N N     . ASP A  1 602  ? -42.182 92.619  108.823 1.00 39.06 ? 600  ASP A N     1 
ATOM   4318  C CA    . ASP A  1 602  ? -42.346 91.394  109.601 1.00 39.03 ? 600  ASP A CA    1 
ATOM   4319  C C     . ASP A  1 602  ? -41.263 91.363  110.672 1.00 40.64 ? 600  ASP A C     1 
ATOM   4320  O O     . ASP A  1 602  ? -40.093 91.083  110.390 1.00 40.58 ? 600  ASP A O     1 
ATOM   4321  C CB    . ASP A  1 602  ? -42.271 90.172  108.690 1.00 39.72 ? 600  ASP A CB    1 
ATOM   4322  C CG    . ASP A  1 602  ? -42.383 88.860  109.451 1.00 41.39 ? 600  ASP A CG    1 
ATOM   4323  O OD1   . ASP A  1 602  ? -42.925 88.873  110.575 1.00 41.51 ? 600  ASP A OD1   1 
ATOM   4324  O OD2   . ASP A  1 602  ? -41.920 87.818  108.929 1.00 37.92 ? 600  ASP A OD2   1 
ATOM   4325  N N     . VAL A  1 603  ? -41.648 91.660  111.906 1.00 40.59 ? 601  VAL A N     1 
ATOM   4326  C CA    . VAL A  1 603  ? -40.724 91.588  113.030 1.00 40.56 ? 601  VAL A CA    1 
ATOM   4327  C C     . VAL A  1 603  ? -40.653 90.141  113.502 1.00 40.65 ? 601  VAL A C     1 
ATOM   4328  O O     . VAL A  1 603  ? -41.675 89.537  113.850 1.00 41.39 ? 601  VAL A O     1 
ATOM   4329  C CB    . VAL A  1 603  ? -41.162 92.527  114.162 1.00 40.75 ? 601  VAL A CB    1 
ATOM   4330  C CG1   . VAL A  1 603  ? -40.218 92.402  115.351 1.00 42.56 ? 601  VAL A CG1   1 
ATOM   4331  C CG2   . VAL A  1 603  ? -41.188 93.959  113.660 1.00 42.54 ? 601  VAL A CG2   1 
ATOM   4332  N N     . VAL A  1 604  ? -39.447 89.583  113.514 1.00 36.22 ? 602  VAL A N     1 
ATOM   4333  C CA    . VAL A  1 604  ? -39.275 88.181  113.869 1.00 34.15 ? 602  VAL A CA    1 
ATOM   4334  C C     . VAL A  1 604  ? -39.058 88.003  115.364 1.00 37.16 ? 602  VAL A C     1 
ATOM   4335  O O     . VAL A  1 604  ? -39.467 86.985  115.930 1.00 36.47 ? 602  VAL A O     1 
ATOM   4336  C CB    . VAL A  1 604  ? -38.106 87.575  113.072 1.00 34.28 ? 602  VAL A CB    1 
ATOM   4337  C CG1   . VAL A  1 604  ? -37.947 86.092  113.380 1.00 33.46 ? 602  VAL A CG1   1 
ATOM   4338  C CG2   . VAL A  1 604  ? -38.321 87.793  111.576 1.00 34.99 ? 602  VAL A CG2   1 
ATOM   4339  N N     . GLY A  1 605  ? -38.414 88.966  116.014 1.00 36.82 ? 603  GLY A N     1 
ATOM   4340  C CA    . GLY A  1 605  ? -38.129 88.839  117.431 1.00 35.92 ? 603  GLY A CA    1 
ATOM   4341  C C     . GLY A  1 605  ? -37.279 89.995  117.913 1.00 37.12 ? 603  GLY A C     1 
ATOM   4342  O O     . GLY A  1 605  ? -37.175 91.027  117.246 1.00 38.10 ? 603  GLY A O     1 
ATOM   4343  N N     . SER A  1 606  ? -36.681 89.809  119.087 1.00 34.49 ? 604  SER A N     1 
ATOM   4344  C CA    . SER A  1 606  ? -35.929 90.865  119.746 1.00 37.66 ? 604  SER A CA    1 
ATOM   4345  C C     . SER A  1 606  ? -34.606 90.327  120.269 1.00 38.21 ? 604  SER A C     1 
ATOM   4346  O O     . SER A  1 606  ? -34.546 89.231  120.833 1.00 40.92 ? 604  SER A O     1 
ATOM   4347  C CB    . SER A  1 606  ? -36.729 91.462  120.894 1.00 38.87 ? 604  SER A CB    1 
ATOM   4348  O OG    . SER A  1 606  ? -37.942 92.013  120.414 1.00 50.03 ? 604  SER A OG    1 
ATOM   4349  N N     . VAL A  1 607  ? -33.545 91.107  120.096 1.00 35.26 ? 605  VAL A N     1 
ATOM   4350  C CA    . VAL A  1 607  ? -32.217 90.724  120.557 1.00 37.99 ? 605  VAL A CA    1 
ATOM   4351  C C     . VAL A  1 607  ? -31.738 91.759  121.561 1.00 37.42 ? 605  VAL A C     1 
ATOM   4352  O O     . VAL A  1 607  ? -31.875 92.963  121.326 1.00 39.02 ? 605  VAL A O     1 
ATOM   4353  C CB    . VAL A  1 607  ? -31.215 90.588  119.392 1.00 38.72 ? 605  VAL A CB    1 
ATOM   4354  C CG1   . VAL A  1 607  ? -31.207 91.839  118.508 1.00 37.81 ? 605  VAL A CG1   1 
ATOM   4355  C CG2   . VAL A  1 607  ? -29.807 90.296  119.933 1.00 35.62 ? 605  VAL A CG2   1 
ATOM   4356  N N     . THR A  1 608  ? -31.194 91.282  122.679 1.00 36.70 ? 606  THR A N     1 
ATOM   4357  C CA    . THR A  1 608  ? -30.519 92.116  123.665 1.00 39.47 ? 606  THR A CA    1 
ATOM   4358  C C     . THR A  1 608  ? -29.020 91.913  123.497 1.00 41.33 ? 606  THR A C     1 
ATOM   4359  O O     . THR A  1 608  ? -28.519 90.794  123.657 1.00 38.68 ? 606  THR A O     1 
ATOM   4360  C CB    . THR A  1 608  ? -30.957 91.759  125.085 1.00 44.93 ? 606  THR A CB    1 
ATOM   4361  O OG1   . THR A  1 608  ? -32.373 91.923  125.199 1.00 43.84 ? 606  THR A OG1   1 
ATOM   4362  C CG2   . THR A  1 608  ? -30.266 92.654  126.107 1.00 45.19 ? 606  THR A CG2   1 
ATOM   4363  N N     . GLU A  1 609  ? -28.311 92.977  123.156 1.00 42.58 ? 607  GLU A N     1 
ATOM   4364  C CA    . GLU A  1 609  ? -26.925 92.829  122.751 1.00 44.73 ? 607  GLU A CA    1 
ATOM   4365  C C     . GLU A  1 609  ? -26.003 92.974  123.959 1.00 44.00 ? 607  GLU A C     1 
ATOM   4366  O O     . GLU A  1 609  ? -26.340 93.629  124.948 1.00 46.28 ? 607  GLU A O     1 
ATOM   4367  C CB    . GLU A  1 609  ? -26.594 93.833  121.641 1.00 47.85 ? 607  GLU A CB    1 
ATOM   4368  C CG    . GLU A  1 609  ? -27.495 93.614  120.397 1.00 49.14 ? 607  GLU A CG    1 
ATOM   4369  C CD    . GLU A  1 609  ? -26.966 94.256  119.118 1.00 55.46 ? 607  GLU A CD    1 
ATOM   4370  O OE1   . GLU A  1 609  ? -26.582 95.450  119.158 1.00 63.49 ? 607  GLU A OE1   1 
ATOM   4371  O OE2   . GLU A  1 609  ? -26.938 93.561  118.069 1.00 52.41 ? 607  GLU A OE2   1 
ATOM   4372  N N     . THR A  1 610  ? -24.855 92.307  123.882 1.00 44.08 ? 608  THR A N     1 
ATOM   4373  C CA    . THR A  1 610  ? -23.932 92.203  125.004 1.00 43.03 ? 608  THR A CA    1 
ATOM   4374  C C     . THR A  1 610  ? -23.068 93.450  125.112 1.00 44.03 ? 608  THR A C     1 
ATOM   4375  O O     . THR A  1 610  ? -22.569 93.963  124.108 1.00 41.92 ? 608  THR A O     1 
ATOM   4376  C CB    . THR A  1 610  ? -23.032 90.976  124.821 1.00 43.99 ? 608  THR A CB    1 
ATOM   4377  O OG1   . THR A  1 610  ? -23.839 89.840  124.499 1.00 40.88 ? 608  THR A OG1   1 
ATOM   4378  C CG2   . THR A  1 610  ? -22.214 90.684  126.091 1.00 41.20 ? 608  THR A CG2   1 
ATOM   4379  N N     . SER A  1 611  ? -22.868 93.921  126.342 1.00 42.39 ? 609  SER A N     1 
ATOM   4380  C CA    . SER A  1 611  ? -21.909 94.988  126.574 1.00 43.21 ? 609  SER A CA    1 
ATOM   4381  C C     . SER A  1 611  ? -20.483 94.441  126.531 1.00 44.84 ? 609  SER A C     1 
ATOM   4382  O O     . SER A  1 611  ? -20.235 93.252  126.760 1.00 43.32 ? 609  SER A O     1 
ATOM   4383  C CB    . SER A  1 611  ? -22.169 95.668  127.918 1.00 45.75 ? 609  SER A CB    1 
ATOM   4384  O OG    . SER A  1 611  ? -21.689 94.874  128.985 1.00 46.45 ? 609  SER A OG    1 
ATOM   4385  N N     . GLU A  1 612  ? -19.535 95.329  126.217 1.00 46.51 ? 610  GLU A N     1 
ATOM   4386  C CA    . GLU A  1 612  ? -18.134 94.915  126.195 1.00 44.90 ? 610  GLU A CA    1 
ATOM   4387  C C     . GLU A  1 612  ? -17.677 94.443  127.566 1.00 43.25 ? 610  GLU A C     1 
ATOM   4388  O O     . GLU A  1 612  ? -16.854 93.524  127.665 1.00 44.09 ? 610  GLU A O     1 
ATOM   4389  C CB    . GLU A  1 612  ? -17.246 96.061  125.714 1.00 50.70 ? 610  GLU A CB    1 
ATOM   4390  C CG    . GLU A  1 612  ? -17.281 96.280  124.213 1.00 52.47 ? 610  GLU A CG    1 
ATOM   4391  C CD    . GLU A  1 612  ? -16.341 97.381  123.765 1.00 60.22 ? 610  GLU A CD    1 
ATOM   4392  O OE1   . GLU A  1 612  ? -15.667 97.980  124.634 1.00 64.43 ? 610  GLU A OE1   1 
ATOM   4393  O OE2   . GLU A  1 612  ? -16.274 97.644  122.543 1.00 59.73 ? 610  GLU A OE2   1 
ATOM   4394  N N     . GLU A  1 613  ? -18.209 95.045  128.631 1.00 44.17 ? 611  GLU A N     1 
ATOM   4395  C CA    . GLU A  1 613  ? -17.865 94.589  129.973 1.00 47.28 ? 611  GLU A CA    1 
ATOM   4396  C C     . GLU A  1 613  ? -18.373 93.174  130.219 1.00 42.04 ? 611  GLU A C     1 
ATOM   4397  O O     . GLU A  1 613  ? -17.644 92.337  130.756 1.00 42.96 ? 611  GLU A O     1 
ATOM   4398  C CB    . GLU A  1 613  ? -18.417 95.552  131.022 1.00 43.95 ? 611  GLU A CB    1 
ATOM   4399  N N     . ASP A  1 614  ? -19.611 92.879  129.812 1.00 46.73 ? 612  ASP A N     1 
ATOM   4400  C CA    . ASP A  1 614  ? -20.154 91.544  130.044 1.00 44.75 ? 612  ASP A CA    1 
ATOM   4401  C C     . ASP A  1 614  ? -19.473 90.486  129.184 1.00 43.00 ? 612  ASP A C     1 
ATOM   4402  O O     . ASP A  1 614  ? -19.328 89.337  129.623 1.00 38.68 ? 612  ASP A O     1 
ATOM   4403  C CB    . ASP A  1 614  ? -21.663 91.544  129.812 1.00 45.50 ? 612  ASP A CB    1 
ATOM   4404  C CG    . ASP A  1 614  ? -22.422 92.182  130.959 1.00 48.56 ? 612  ASP A CG    1 
ATOM   4405  O OD1   . ASP A  1 614  ? -21.828 92.328  132.049 1.00 54.45 ? 612  ASP A OD1   1 
ATOM   4406  O OD2   . ASP A  1 614  ? -23.606 92.536  130.779 1.00 46.17 ? 612  ASP A OD2   1 
ATOM   4407  N N     . ALA A  1 615  ? -19.044 90.842  127.967 1.00 40.89 ? 613  ALA A N     1 
ATOM   4408  C CA    . ALA A  1 615  ? -18.258 89.902  127.174 1.00 37.95 ? 613  ALA A CA    1 
ATOM   4409  C C     . ALA A  1 615  ? -16.952 89.561  127.875 1.00 38.33 ? 613  ALA A C     1 
ATOM   4410  O O     . ALA A  1 615  ? -16.530 88.401  127.880 1.00 37.17 ? 613  ALA A O     1 
ATOM   4411  C CB    . ALA A  1 615  ? -17.980 90.466  125.782 1.00 36.83 ? 613  ALA A CB    1 
ATOM   4412  N N     . ARG A  1 616  ? -16.306 90.553  128.491 1.00 41.09 ? 614  ARG A N     1 
ATOM   4413  C CA    . ARG A  1 616  ? -15.090 90.258  129.239 1.00 41.65 ? 614  ARG A CA    1 
ATOM   4414  C C     . ARG A  1 616  ? -15.398 89.438  130.484 1.00 38.49 ? 614  ARG A C     1 
ATOM   4415  O O     . ARG A  1 616  ? -14.657 88.503  130.812 1.00 36.88 ? 614  ARG A O     1 
ATOM   4416  C CB    . ARG A  1 616  ? -14.360 91.550  129.595 1.00 45.05 ? 614  ARG A CB    1 
ATOM   4417  C CG    . ARG A  1 616  ? -13.333 91.958  128.544 1.00 48.76 ? 614  ARG A CG    1 
ATOM   4418  C CD    . ARG A  1 616  ? -13.553 93.392  128.101 1.00 49.01 ? 614  ARG A CD    1 
ATOM   4419  N NE    . ARG A  1 616  ? -13.764 94.270  129.243 1.00 56.49 ? 614  ARG A NE    1 
ATOM   4420  C CZ    . ARG A  1 616  ? -14.097 95.550  129.151 1.00 58.14 ? 614  ARG A CZ    1 
ATOM   4421  N NH1   . ARG A  1 616  ? -14.213 96.150  127.977 1.00 60.21 ? 614  ARG A NH1   1 
ATOM   4422  N NH2   . ARG A  1 616  ? -14.331 96.241  130.263 1.00 57.93 ? 614  ARG A NH2   1 
ATOM   4423  N N     . ARG A  1 617  ? -16.496 89.759  131.179 1.00 39.89 ? 615  ARG A N     1 
ATOM   4424  C CA    . ARG A  1 617  ? -16.917 88.941  132.316 1.00 39.35 ? 615  ARG A CA    1 
ATOM   4425  C C     . ARG A  1 617  ? -17.204 87.507  131.885 1.00 37.31 ? 615  ARG A C     1 
ATOM   4426  O O     . ARG A  1 617  ? -16.851 86.557  132.590 1.00 37.42 ? 615  ARG A O     1 
ATOM   4427  C CB    . ARG A  1 617  ? -18.152 89.553  132.982 1.00 39.39 ? 615  ARG A CB    1 
ATOM   4428  N N     . ALA A  1 618  ? -17.832 87.335  130.715 1.00 36.65 ? 616  ALA A N     1 
ATOM   4429  C CA    . ALA A  1 618  ? -18.153 85.996  130.226 1.00 35.74 ? 616  ALA A CA    1 
ATOM   4430  C C     . ALA A  1 618  ? -16.902 85.145  130.026 1.00 34.71 ? 616  ALA A C     1 
ATOM   4431  O O     . ALA A  1 618  ? -16.895 83.959  130.380 1.00 35.30 ? 616  ALA A O     1 
ATOM   4432  C CB    . ALA A  1 618  ? -18.960 86.086  128.929 1.00 36.07 ? 616  ALA A CB    1 
ATOM   4433  N N     . VAL A  1 619  ? -15.832 85.716  129.456 1.00 34.76 ? 617  VAL A N     1 
ATOM   4434  C CA    . VAL A  1 619  ? -14.609 84.928  129.285 1.00 36.01 ? 617  VAL A CA    1 
ATOM   4435  C C     . VAL A  1 619  ? -14.075 84.488  130.640 1.00 34.92 ? 617  VAL A C     1 
ATOM   4436  O O     . VAL A  1 619  ? -13.670 83.331  130.815 1.00 35.45 ? 617  VAL A O     1 
ATOM   4437  C CB    . VAL A  1 619  ? -13.537 85.693  128.480 1.00 36.05 ? 617  VAL A CB    1 
ATOM   4438  C CG1   . VAL A  1 619  ? -12.242 84.838  128.363 1.00 34.60 ? 617  VAL A CG1   1 
ATOM   4439  C CG2   . VAL A  1 619  ? -14.049 86.040  127.086 1.00 34.47 ? 617  VAL A CG2   1 
ATOM   4440  N N     . ARG A  1 620  ? -14.075 85.394  131.625 1.00 35.71 ? 618  ARG A N     1 
ATOM   4441  C CA    . ARG A  1 620  ? -13.557 85.029  132.940 1.00 37.96 ? 618  ARG A CA    1 
ATOM   4442  C C     . ARG A  1 620  ? -14.408 83.943  133.588 1.00 40.09 ? 618  ARG A C     1 
ATOM   4443  O O     . ARG A  1 620  ? -13.875 83.045  134.250 1.00 43.23 ? 618  ARG A O     1 
ATOM   4444  C CB    . ARG A  1 620  ? -13.466 86.259  133.845 1.00 41.33 ? 618  ARG A CB    1 
ATOM   4445  N N     . LEU A  1 621  ? -15.732 83.996  133.393 1.00 37.59 ? 619  LEU A N     1 
ATOM   4446  C CA    . LEU A  1 621  ? -16.601 82.932  133.900 1.00 38.20 ? 619  LEU A CA    1 
ATOM   4447  C C     . LEU A  1 621  ? -16.306 81.607  133.207 1.00 39.69 ? 619  LEU A C     1 
ATOM   4448  O O     . LEU A  1 621  ? -16.251 80.554  133.857 1.00 40.34 ? 619  LEU A O     1 
ATOM   4449  C CB    . LEU A  1 621  ? -18.072 83.315  133.715 1.00 37.99 ? 619  LEU A CB    1 
ATOM   4450  C CG    . LEU A  1 621  ? -18.533 84.496  134.570 1.00 38.56 ? 619  LEU A CG    1 
ATOM   4451  C CD1   . LEU A  1 621  ? -19.885 85.019  134.095 1.00 39.63 ? 619  LEU A CD1   1 
ATOM   4452  C CD2   . LEU A  1 621  ? -18.600 84.081  136.034 1.00 40.95 ? 619  LEU A CD2   1 
ATOM   4453  N N     . ALA A  1 622  ? -16.135 81.642  131.883 1.00 35.30 ? 620  ALA A N     1 
ATOM   4454  C CA    . ALA A  1 622  ? -15.726 80.449  131.146 1.00 36.89 ? 620  ALA A CA    1 
ATOM   4455  C C     . ALA A  1 622  ? -14.393 79.915  131.655 1.00 36.49 ? 620  ALA A C     1 
ATOM   4456  O O     . ALA A  1 622  ? -14.225 78.703  131.836 1.00 36.78 ? 620  ALA A O     1 
ATOM   4457  C CB    . ALA A  1 622  ? -15.634 80.767  129.658 1.00 32.62 ? 620  ALA A CB    1 
ATOM   4458  N N     . ALA A  1 623  ? -13.427 80.806  131.877 1.00 35.52 ? 621  ALA A N     1 
ATOM   4459  C CA    . ALA A  1 623  ? -12.142 80.382  132.413 1.00 37.17 ? 621  ALA A CA    1 
ATOM   4460  C C     . ALA A  1 623  ? -12.313 79.685  133.758 1.00 41.50 ? 621  ALA A C     1 
ATOM   4461  O O     . ALA A  1 623  ? -11.714 78.629  134.001 1.00 38.33 ? 621  ALA A O     1 
ATOM   4462  C CB    . ALA A  1 623  ? -11.210 81.590  132.538 1.00 35.42 ? 621  ALA A CB    1 
ATOM   4463  N N     . ASP A  1 624  ? -13.145 80.250  134.636 1.00 41.54 ? 622  ASP A N     1 
ATOM   4464  C CA    . ASP A  1 624  ? -13.327 79.678  135.969 1.00 47.90 ? 622  ASP A CA    1 
ATOM   4465  C C     . ASP A  1 624  ? -13.997 78.307  135.926 1.00 46.64 ? 622  ASP A C     1 
ATOM   4466  O O     . ASP A  1 624  ? -13.726 77.459  136.784 1.00 46.16 ? 622  ASP A O     1 
ATOM   4467  C CB    . ASP A  1 624  ? -14.137 80.633  136.847 1.00 47.83 ? 622  ASP A CB    1 
ATOM   4468  C CG    . ASP A  1 624  ? -13.331 81.848  137.289 1.00 55.97 ? 622  ASP A CG    1 
ATOM   4469  O OD1   . ASP A  1 624  ? -12.080 81.787  137.245 1.00 62.21 ? 622  ASP A OD1   1 
ATOM   4470  O OD2   . ASP A  1 624  ? -13.949 82.860  137.691 1.00 64.01 ? 622  ASP A OD2   1 
ATOM   4471  N N     . ALA A  1 625  ? -14.857 78.065  134.942 1.00 46.92 ? 623  ALA A N     1 
ATOM   4472  C CA    . ALA A  1 625  ? -15.590 76.812  134.855 1.00 48.05 ? 623  ALA A CA    1 
ATOM   4473  C C     . ALA A  1 625  ? -14.917 75.776  133.967 1.00 44.62 ? 623  ALA A C     1 
ATOM   4474  O O     . ALA A  1 625  ? -15.374 74.628  133.934 1.00 43.87 ? 623  ALA A O     1 
ATOM   4475  C CB    . ALA A  1 625  ? -17.003 77.068  134.330 1.00 48.68 ? 623  ALA A CB    1 
ATOM   4476  N N     . ALA A  1 626  ? -13.855 76.145  133.250 1.00 43.24 ? 624  ALA A N     1 
ATOM   4477  C CA    . ALA A  1 626  ? -13.205 75.212  132.331 1.00 41.20 ? 624  ALA A CA    1 
ATOM   4478  C C     . ALA A  1 626  ? -12.828 73.878  132.970 1.00 41.06 ? 624  ALA A C     1 
ATOM   4479  O O     . ALA A  1 626  ? -13.116 72.833  132.364 1.00 43.02 ? 624  ALA A O     1 
ATOM   4480  C CB    . ALA A  1 626  ? -11.982 75.891  131.698 1.00 41.86 ? 624  ALA A CB    1 
ATOM   4481  N N     . PRO A  1 627  ? -12.196 73.822  134.151 1.00 42.44 ? 625  PRO A N     1 
ATOM   4482  C CA    . PRO A  1 627  ? -11.874 72.498  134.720 1.00 45.87 ? 625  PRO A CA    1 
ATOM   4483  C C     . PRO A  1 627  ? -13.085 71.601  134.899 1.00 39.38 ? 625  PRO A C     1 
ATOM   4484  O O     . PRO A  1 627  ? -13.002 70.400  134.622 1.00 42.65 ? 625  PRO A O     1 
ATOM   4485  C CB    . PRO A  1 627  ? -11.230 72.848  136.071 1.00 42.61 ? 625  PRO A CB    1 
ATOM   4486  C CG    . PRO A  1 627  ? -10.651 74.194  135.859 1.00 46.72 ? 625  PRO A CG    1 
ATOM   4487  C CD    . PRO A  1 627  ? -11.626 74.911  134.971 1.00 46.88 ? 625  PRO A CD    1 
ATOM   4488  N N     . ASP A  1 628  ? -14.212 72.155  135.343 1.00 38.73 ? 626  ASP A N     1 
ATOM   4489  C CA    . ASP A  1 628  ? -15.403 71.341  135.575 1.00 43.11 ? 626  ASP A CA    1 
ATOM   4490  C C     . ASP A  1 628  ? -15.912 70.708  134.286 1.00 42.02 ? 626  ASP A C     1 
ATOM   4491  O O     . ASP A  1 628  ? -16.287 69.530  134.267 1.00 43.21 ? 626  ASP A O     1 
ATOM   4492  C CB    . ASP A  1 628  ? -16.495 72.194  136.213 1.00 45.70 ? 626  ASP A CB    1 
ATOM   4493  C CG    . ASP A  1 628  ? -16.031 72.860  137.492 1.00 52.05 ? 626  ASP A CG    1 
ATOM   4494  O OD1   . ASP A  1 628  ? -15.183 72.265  138.189 1.00 53.51 ? 626  ASP A OD1   1 
ATOM   4495  O OD2   . ASP A  1 628  ? -16.507 73.975  137.797 1.00 57.45 ? 626  ASP A OD2   1 
ATOM   4496  N N     . TRP A  1 629  ? -15.946 71.473  133.199 1.00 41.84 ? 627  TRP A N     1 
ATOM   4497  C CA    . TRP A  1 629  ? -16.453 70.918  131.949 1.00 33.58 ? 627  TRP A CA    1 
ATOM   4498  C C     . TRP A  1 629  ? -15.438 69.964  131.328 1.00 39.70 ? 627  TRP A C     1 
ATOM   4499  O O     . TRP A  1 629  ? -15.811 68.926  130.767 1.00 36.43 ? 627  TRP A O     1 
ATOM   4500  C CB    . TRP A  1 629  ? -16.813 72.045  130.983 1.00 35.28 ? 627  TRP A CB    1 
ATOM   4501  C CG    . TRP A  1 629  ? -17.247 71.552  129.633 1.00 34.98 ? 627  TRP A CG    1 
ATOM   4502  C CD1   . TRP A  1 629  ? -16.654 71.817  128.432 1.00 33.87 ? 627  TRP A CD1   1 
ATOM   4503  C CD2   . TRP A  1 629  ? -18.350 70.687  129.353 1.00 34.67 ? 627  TRP A CD2   1 
ATOM   4504  N NE1   . TRP A  1 629  ? -17.332 71.184  127.416 1.00 33.74 ? 627  TRP A NE1   1 
ATOM   4505  C CE2   . TRP A  1 629  ? -18.378 70.483  127.957 1.00 30.58 ? 627  TRP A CE2   1 
ATOM   4506  C CE3   . TRP A  1 629  ? -19.327 70.074  130.144 1.00 36.16 ? 627  TRP A CE3   1 
ATOM   4507  C CZ2   . TRP A  1 629  ? -19.334 69.684  127.338 1.00 33.43 ? 627  TRP A CZ2   1 
ATOM   4508  C CZ3   . TRP A  1 629  ? -20.285 69.284  129.523 1.00 35.73 ? 627  TRP A CZ3   1 
ATOM   4509  C CH2   . TRP A  1 629  ? -20.279 69.095  128.142 1.00 33.78 ? 627  TRP A CH2   1 
ATOM   4510  N N     . ALA A  1 630  ? -14.147 70.288  131.433 1.00 36.63 ? 628  ALA A N     1 
ATOM   4511  C CA    . ALA A  1 630  ? -13.126 69.366  130.956 1.00 40.54 ? 628  ALA A CA    1 
ATOM   4512  C C     . ALA A  1 630  ? -13.154 68.046  131.714 1.00 39.27 ? 628  ALA A C     1 
ATOM   4513  O O     . ALA A  1 630  ? -12.696 67.033  131.181 1.00 37.85 ? 628  ALA A O     1 
ATOM   4514  C CB    . ALA A  1 630  ? -11.745 70.002  131.068 1.00 36.69 ? 628  ALA A CB    1 
ATOM   4515  N N     . ALA A  1 631  ? -13.698 68.034  132.933 1.00 38.54 ? 629  ALA A N     1 
ATOM   4516  C CA    . ALA A  1 631  ? -13.745 66.823  133.744 1.00 42.50 ? 629  ALA A CA    1 
ATOM   4517  C C     . ALA A  1 631  ? -14.887 65.890  133.359 1.00 42.11 ? 629  ALA A C     1 
ATOM   4518  O O     . ALA A  1 631  ? -14.847 64.707  133.718 1.00 44.29 ? 629  ALA A O     1 
ATOM   4519  C CB    . ALA A  1 631  ? -13.855 67.186  135.224 1.00 41.33 ? 629  ALA A CB    1 
ATOM   4520  N N     . VAL A  1 632  ? -15.904 66.384  132.662 1.00 39.67 ? 630  VAL A N     1 
ATOM   4521  C CA    . VAL A  1 632  ? -16.950 65.517  132.123 1.00 40.63 ? 630  VAL A CA    1 
ATOM   4522  C C     . VAL A  1 632  ? -16.298 64.601  131.090 1.00 36.71 ? 630  VAL A C     1 
ATOM   4523  O O     . VAL A  1 632  ? -15.661 65.091  130.143 1.00 36.99 ? 630  VAL A O     1 
ATOM   4524  C CB    . VAL A  1 632  ? -18.106 66.332  131.518 1.00 36.47 ? 630  VAL A CB    1 
ATOM   4525  C CG1   . VAL A  1 632  ? -19.143 65.414  130.842 1.00 32.84 ? 630  VAL A CG1   1 
ATOM   4526  C CG2   . VAL A  1 632  ? -18.774 67.181  132.595 1.00 36.94 ? 630  VAL A CG2   1 
ATOM   4527  N N     . PRO A  1 633  ? -16.400 63.284  131.253 1.00 35.28 ? 631  PRO A N     1 
ATOM   4528  C CA    . PRO A  1 633  ? -15.740 62.351  130.327 1.00 35.56 ? 631  PRO A CA    1 
ATOM   4529  C C     . PRO A  1 633  ? -16.161 62.601  128.889 1.00 38.44 ? 631  PRO A C     1 
ATOM   4530  O O     . PRO A  1 633  ? -17.322 62.959  128.629 1.00 35.64 ? 631  PRO A O     1 
ATOM   4531  C CB    . PRO A  1 633  ? -16.213 60.978  130.816 1.00 37.49 ? 631  PRO A CB    1 
ATOM   4532  C CG    . PRO A  1 633  ? -16.510 61.191  132.283 1.00 37.90 ? 631  PRO A CG    1 
ATOM   4533  C CD    . PRO A  1 633  ? -17.044 62.591  132.390 1.00 38.17 ? 631  PRO A CD    1 
ATOM   4534  N N     . PRO A  1 634  ? -15.235 62.444  127.931 1.00 33.28 ? 632  PRO A N     1 
ATOM   4535  C CA    . PRO A  1 634  ? -15.581 62.685  126.517 1.00 31.39 ? 632  PRO A CA    1 
ATOM   4536  C C     . PRO A  1 634  ? -16.845 61.975  126.068 1.00 34.89 ? 632  PRO A C     1 
ATOM   4537  O O     . PRO A  1 634  ? -17.629 62.528  125.285 1.00 30.39 ? 632  PRO A O     1 
ATOM   4538  C CB    . PRO A  1 634  ? -14.351 62.157  125.772 1.00 32.93 ? 632  PRO A CB    1 
ATOM   4539  C CG    . PRO A  1 634  ? -13.216 62.357  126.731 1.00 34.28 ? 632  PRO A CG    1 
ATOM   4540  C CD    . PRO A  1 634  ? -13.804 62.128  128.112 1.00 35.72 ? 632  PRO A CD    1 
ATOM   4541  N N     . SER A  1 635  ? -17.060 60.750  126.546 1.00 34.77 ? 633  SER A N     1 
ATOM   4542  C CA    . SER A  1 635  ? -18.257 60.007  126.163 1.00 33.82 ? 633  SER A CA    1 
ATOM   4543  C C     . SER A  1 635  ? -19.525 60.740  126.591 1.00 34.24 ? 633  SER A C     1 
ATOM   4544  O O     . SER A  1 635  ? -20.515 60.771  125.849 1.00 33.90 ? 633  SER A O     1 
ATOM   4545  C CB    . SER A  1 635  ? -18.190 58.602  126.770 1.00 39.22 ? 633  SER A CB    1 
ATOM   4546  O OG    . SER A  1 635  ? -19.451 58.160  127.244 1.00 48.51 ? 633  SER A OG    1 
ATOM   4547  N N     . GLU A  1 636  ? -19.511 61.348  127.777 1.00 33.21 ? 634  GLU A N     1 
ATOM   4548  C CA    . GLU A  1 636  ? -20.696 62.041  128.261 1.00 34.74 ? 634  GLU A CA    1 
ATOM   4549  C C     . GLU A  1 636  ? -20.885 63.383  127.564 1.00 35.92 ? 634  GLU A C     1 
ATOM   4550  O O     . GLU A  1 636  ? -22.029 63.783  127.290 1.00 34.36 ? 634  GLU A O     1 
ATOM   4551  C CB    . GLU A  1 636  ? -20.616 62.201  129.784 1.00 38.04 ? 634  GLU A CB    1 
ATOM   4552  C CG    . GLU A  1 636  ? -21.864 62.808  130.412 1.00 45.55 ? 634  GLU A CG    1 
ATOM   4553  C CD    . GLU A  1 636  ? -23.171 62.235  129.847 1.00 47.27 ? 634  GLU A CD    1 
ATOM   4554  O OE1   . GLU A  1 636  ? -23.313 60.992  129.778 1.00 49.33 ? 634  GLU A OE1   1 
ATOM   4555  O OE2   . GLU A  1 636  ? -24.057 63.033  129.466 1.00 45.03 ? 634  GLU A OE2   1 
ATOM   4556  N N     . ARG A  1 637  ? -19.784 64.067  127.239 1.00 32.17 ? 635  ARG A N     1 
ATOM   4557  C CA    . ARG A  1 637  ? -19.873 65.257  126.398 1.00 31.36 ? 635  ARG A CA    1 
ATOM   4558  C C     . ARG A  1 637  ? -20.468 64.918  125.036 1.00 29.67 ? 635  ARG A C     1 
ATOM   4559  O O     . ARG A  1 637  ? -21.315 65.659  124.519 1.00 29.64 ? 635  ARG A O     1 
ATOM   4560  C CB    . ARG A  1 637  ? -18.488 65.897  126.254 1.00 29.85 ? 635  ARG A CB    1 
ATOM   4561  C CG    . ARG A  1 637  ? -17.841 66.175  127.619 1.00 30.08 ? 635  ARG A CG    1 
ATOM   4562  C CD    . ARG A  1 637  ? -16.656 67.137  127.540 1.00 33.12 ? 635  ARG A CD    1 
ATOM   4563  N NE    . ARG A  1 637  ? -15.651 66.733  126.561 1.00 33.07 ? 635  ARG A NE    1 
ATOM   4564  C CZ    . ARG A  1 637  ? -14.417 66.352  126.866 1.00 34.72 ? 635  ARG A CZ    1 
ATOM   4565  N NH1   . ARG A  1 637  ? -14.028 66.215  128.122 1.00 33.78 ? 635  ARG A NH1   1 
ATOM   4566  N NH2   . ARG A  1 637  ? -13.551 66.110  125.885 1.00 29.87 ? 635  ARG A NH2   1 
ATOM   4567  N N     . ALA A  1 638  ? -20.066 63.778  124.460 1.00 27.27 ? 636  ALA A N     1 
ATOM   4568  C CA    . ALA A  1 638  ? -20.624 63.336  123.182 1.00 28.97 ? 636  ALA A CA    1 
ATOM   4569  C C     . ALA A  1 638  ? -22.101 62.983  123.309 1.00 29.34 ? 636  ALA A C     1 
ATOM   4570  O O     . ALA A  1 638  ? -22.888 63.249  122.393 1.00 25.86 ? 636  ALA A O     1 
ATOM   4571  C CB    . ALA A  1 638  ? -19.837 62.133  122.654 1.00 27.59 ? 636  ALA A CB    1 
ATOM   4572  N N     . ALA A  1 639  ? -22.493 62.386  124.437 1.00 33.23 ? 637  ALA A N     1 
ATOM   4573  C CA    . ALA A  1 639  ? -23.904 62.113  124.698 1.00 31.04 ? 637  ALA A CA    1 
ATOM   4574  C C     . ALA A  1 639  ? -24.730 63.395  124.691 1.00 32.13 ? 637  ALA A C     1 
ATOM   4575  O O     . ALA A  1 639  ? -25.879 63.397  124.233 1.00 30.84 ? 637  ALA A O     1 
ATOM   4576  C CB    . ALA A  1 639  ? -24.060 61.381  126.038 1.00 31.14 ? 637  ALA A CB    1 
ATOM   4577  N N     . CYS A  1 640  ? -24.169 64.495  125.214 1.00 32.86 ? 638  CYS A N     1 
ATOM   4578  C CA    . CYS A  1 640  ? -24.851 65.786  125.138 1.00 28.74 ? 638  CYS A CA    1 
ATOM   4579  C C     . CYS A  1 640  ? -25.105 66.184  123.695 1.00 31.28 ? 638  CYS A C     1 
ATOM   4580  O O     . CYS A  1 640  ? -26.179 66.699  123.358 1.00 30.38 ? 638  CYS A O     1 
ATOM   4581  C CB    . CYS A  1 640  ? -24.028 66.878  125.809 1.00 32.33 ? 638  CYS A CB    1 
ATOM   4582  S SG    . CYS A  1 640  ? -23.947 66.810  127.580 1.00 35.70 ? 638  CYS A SG    1 
ATOM   4583  N N     . LEU A  1 641  ? -24.105 66.006  122.840 1.00 26.34 ? 639  LEU A N     1 
ATOM   4584  C CA    . LEU A  1 641  ? -24.275 66.372  121.440 1.00 26.02 ? 639  LEU A CA    1 
ATOM   4585  C C     . LEU A  1 641  ? -25.318 65.496  120.772 1.00 27.24 ? 639  LEU A C     1 
ATOM   4586  O O     . LEU A  1 641  ? -26.133 65.987  119.986 1.00 27.87 ? 639  LEU A O     1 
ATOM   4587  C CB    . LEU A  1 641  ? -22.946 66.260  120.703 1.00 24.70 ? 639  LEU A CB    1 
ATOM   4588  C CG    . LEU A  1 641  ? -22.067 67.495  120.640 1.00 24.57 ? 639  LEU A CG    1 
ATOM   4589  C CD1   . LEU A  1 641  ? -21.717 67.963  122.038 1.00 28.47 ? 639  LEU A CD1   1 
ATOM   4590  C CD2   . LEU A  1 641  ? -20.806 67.110  119.880 1.00 27.64 ? 639  LEU A CD2   1 
ATOM   4591  N N     . ASP A  1 642  ? -25.307 64.193  121.059 1.00 30.02 ? 640  ASP A N     1 
ATOM   4592  C CA    . ASP A  1 642  ? -26.318 63.323  120.465 1.00 26.61 ? 640  ASP A CA    1 
ATOM   4593  C C     . ASP A  1 642  ? -27.714 63.687  120.955 1.00 27.41 ? 640  ASP A C     1 
ATOM   4594  O O     . ASP A  1 642  ? -28.688 63.597  120.198 1.00 27.38 ? 640  ASP A O     1 
ATOM   4595  C CB    . ASP A  1 642  ? -26.006 61.858  120.765 1.00 29.54 ? 640  ASP A CB    1 
ATOM   4596  C CG    . ASP A  1 642  ? -24.895 61.302  119.875 1.00 30.21 ? 640  ASP A CG    1 
ATOM   4597  O OD1   . ASP A  1 642  ? -24.692 61.843  118.761 1.00 29.15 ? 640  ASP A OD1   1 
ATOM   4598  O OD2   . ASP A  1 642  ? -24.228 60.328  120.284 1.00 33.09 ? 640  ASP A OD2   1 
ATOM   4599  N N     . ARG A  1 643  ? -27.841 64.073  122.228 1.00 29.60 ? 641  ARG A N     1 
ATOM   4600  C CA    . ARG A  1 643  ? -29.152 64.496  122.716 1.00 28.87 ? 641  ARG A CA    1 
ATOM   4601  C C     . ARG A  1 643  ? -29.602 65.774  122.022 1.00 30.15 ? 641  ARG A C     1 
ATOM   4602  O O     . ARG A  1 643  ? -30.784 65.923  121.692 1.00 32.89 ? 641  ARG A O     1 
ATOM   4603  C CB    . ARG A  1 643  ? -29.127 64.680  124.233 1.00 32.69 ? 641  ARG A CB    1 
ATOM   4604  C CG    . ARG A  1 643  ? -29.260 63.369  124.994 1.00 32.33 ? 641  ARG A CG    1 
ATOM   4605  C CD    . ARG A  1 643  ? -29.424 63.577  126.511 1.00 32.33 ? 641  ARG A CD    1 
ATOM   4606  N NE    . ARG A  1 643  ? -28.290 64.277  127.106 1.00 35.47 ? 641  ARG A NE    1 
ATOM   4607  C CZ    . ARG A  1 643  ? -27.266 63.684  127.708 1.00 35.47 ? 641  ARG A CZ    1 
ATOM   4608  N NH1   . ARG A  1 643  ? -27.176 62.366  127.785 1.00 34.32 ? 641  ARG A NH1   1 
ATOM   4609  N NH2   . ARG A  1 643  ? -26.309 64.434  128.249 1.00 32.51 ? 641  ARG A NH2   1 
ATOM   4610  N N     . ALA A  1 644  ? -28.673 66.704  121.780 1.00 26.98 ? 642  ALA A N     1 
ATOM   4611  C CA    . ALA A  1 644  ? -29.024 67.927  121.067 1.00 28.54 ? 642  ALA A CA    1 
ATOM   4612  C C     . ALA A  1 644  ? -29.463 67.619  119.645 1.00 30.17 ? 642  ALA A C     1 
ATOM   4613  O O     . ALA A  1 644  ? -30.415 68.228  119.139 1.00 27.04 ? 642  ALA A O     1 
ATOM   4614  C CB    . ALA A  1 644  ? -27.846 68.901  121.056 1.00 30.29 ? 642  ALA A CB    1 
ATOM   4615  N N     . ALA A  1 645  ? -28.794 66.666  118.982 1.00 27.83 ? 643  ALA A N     1 
ATOM   4616  C CA    . ALA A  1 645  ? -29.212 66.316  117.621 1.00 25.12 ? 643  ALA A CA    1 
ATOM   4617  C C     . ALA A  1 645  ? -30.649 65.804  117.606 1.00 30.20 ? 643  ALA A C     1 
ATOM   4618  O O     . ALA A  1 645  ? -31.441 66.174  116.729 1.00 30.22 ? 643  ALA A O     1 
ATOM   4619  C CB    . ALA A  1 645  ? -28.275 65.267  117.012 1.00 26.04 ? 643  ALA A CB    1 
ATOM   4620  N N     . GLU A  1 646  ? -30.997 64.945  118.566 1.00 29.27 ? 644  GLU A N     1 
ATOM   4621  C CA    . GLU A  1 646  ? -32.363 64.441  118.655 1.00 33.16 ? 644  GLU A CA    1 
ATOM   4622  C C     . GLU A  1 646  ? -33.363 65.577  118.849 1.00 29.42 ? 644  GLU A C     1 
ATOM   4623  O O     . GLU A  1 646  ? -34.438 65.578  118.240 1.00 30.58 ? 644  GLU A O     1 
ATOM   4624  C CB    . GLU A  1 646  ? -32.473 63.436  119.798 1.00 31.24 ? 644  GLU A CB    1 
ATOM   4625  C CG    . GLU A  1 646  ? -31.655 62.201  119.584 1.00 37.94 ? 644  GLU A CG    1 
ATOM   4626  C CD    . GLU A  1 646  ? -32.158 61.387  118.414 1.00 42.99 ? 644  GLU A CD    1 
ATOM   4627  O OE1   . GLU A  1 646  ? -33.383 61.140  118.352 1.00 47.04 ? 644  GLU A OE1   1 
ATOM   4628  O OE2   . GLU A  1 646  ? -31.333 61.003  117.554 1.00 45.53 ? 644  GLU A OE2   1 
ATOM   4629  N N     . LEU A  1 647  ? -33.007 66.568  119.667 1.00 27.32 ? 645  LEU A N     1 
ATOM   4630  C CA    . LEU A  1 647  ? -33.898 67.697  119.919 1.00 29.99 ? 645  LEU A CA    1 
ATOM   4631  C C     . LEU A  1 647  ? -34.091 68.542  118.672 1.00 29.62 ? 645  LEU A C     1 
ATOM   4632  O O     . LEU A  1 647  ? -35.206 69.011  118.391 1.00 28.52 ? 645  LEU A O     1 
ATOM   4633  C CB    . LEU A  1 647  ? -33.343 68.559  121.055 1.00 29.60 ? 645  LEU A CB    1 
ATOM   4634  C CG    . LEU A  1 647  ? -33.485 67.974  122.460 1.00 34.18 ? 645  LEU A CG    1 
ATOM   4635  C CD1   . LEU A  1 647  ? -32.746 68.825  123.503 1.00 34.01 ? 645  LEU A CD1   1 
ATOM   4636  C CD2   . LEU A  1 647  ? -34.968 67.843  122.823 1.00 35.79 ? 645  LEU A CD2   1 
ATOM   4637  N N     . MET A  1 648  ? -33.010 68.777  117.932 1.00 27.61 ? 646  MET A N     1 
ATOM   4638  C CA    . MET A  1 648  ? -33.115 69.561  116.710 1.00 27.86 ? 646  MET A CA    1 
ATOM   4639  C C     . MET A  1 648  ? -33.931 68.823  115.665 1.00 29.72 ? 646  MET A C     1 
ATOM   4640  O O     . MET A  1 648  ? -34.682 69.450  114.912 1.00 31.13 ? 646  MET A O     1 
ATOM   4641  C CB    . MET A  1 648  ? -31.726 69.888  116.161 1.00 26.81 ? 646  MET A CB    1 
ATOM   4642  C CG    . MET A  1 648  ? -30.976 70.932  116.939 1.00 30.24 ? 646  MET A CG    1 
ATOM   4643  S SD    . MET A  1 648  ? -29.625 71.647  115.964 1.00 31.40 ? 646  MET A SD    1 
ATOM   4644  C CE    . MET A  1 648  ? -28.933 72.710  117.231 1.00 31.97 ? 646  MET A CE    1 
ATOM   4645  N N     . GLN A  1 649  ? -33.777 67.493  115.590 1.00 28.83 ? 647  GLN A N     1 
ATOM   4646  C CA    . GLN A  1 649  ? -34.565 66.703  114.648 1.00 27.31 ? 647  GLN A CA    1 
ATOM   4647  C C     . GLN A  1 649  ? -36.058 66.808  114.951 1.00 30.71 ? 647  GLN A C     1 
ATOM   4648  O O     . GLN A  1 649  ? -36.878 66.979  114.043 1.00 30.35 ? 647  GLN A O     1 
ATOM   4649  C CB    . GLN A  1 649  ? -34.128 65.240  114.674 1.00 27.42 ? 647  GLN A CB    1 
ATOM   4650  C CG    . GLN A  1 649  ? -34.812 64.400  113.606 1.00 28.78 ? 647  GLN A CG    1 
ATOM   4651  C CD    . GLN A  1 649  ? -34.219 64.621  112.215 1.00 27.27 ? 647  GLN A CD    1 
ATOM   4652  O OE1   . GLN A  1 649  ? -33.147 64.105  111.897 1.00 27.82 ? 647  GLN A OE1   1 
ATOM   4653  N NE2   . GLN A  1 649  ? -34.924 65.385  111.378 1.00 30.14 ? 647  GLN A NE2   1 
ATOM   4654  N N     . ALA A  1 650  ? -36.428 66.688  116.223 1.00 29.69 ? 648  ALA A N     1 
ATOM   4655  C CA    . ALA A  1 650  ? -37.836 66.769  116.588 1.00 31.52 ? 648  ALA A CA    1 
ATOM   4656  C C     . ALA A  1 650  ? -38.380 68.177  116.395 1.00 33.97 ? 648  ALA A C     1 
ATOM   4657  O O     . ALA A  1 650  ? -39.568 68.354  116.109 1.00 33.67 ? 648  ALA A O     1 
ATOM   4658  C CB    . ALA A  1 650  ? -38.021 66.312  118.035 1.00 32.56 ? 648  ALA A CB    1 
ATOM   4659  N N     . ARG A  1 651  ? -37.523 69.182  116.517 1.00 33.23 ? 649  ARG A N     1 
ATOM   4660  C CA    . ARG A  1 651  ? -37.927 70.573  116.435 1.00 30.74 ? 649  ARG A CA    1 
ATOM   4661  C C     . ARG A  1 651  ? -37.723 71.165  115.047 1.00 31.85 ? 649  ARG A C     1 
ATOM   4662  O O     . ARG A  1 651  ? -37.958 72.363  114.863 1.00 31.73 ? 649  ARG A O     1 
ATOM   4663  C CB    . ARG A  1 651  ? -37.158 71.383  117.486 1.00 31.63 ? 649  ARG A CB    1 
ATOM   4664  C CG    . ARG A  1 651  ? -37.832 72.676  117.921 1.00 37.85 ? 649  ARG A CG    1 
ATOM   4665  C CD    . ARG A  1 651  ? -37.596 72.983  119.399 1.00 41.39 ? 649  ARG A CD    1 
ATOM   4666  N NE    . ARG A  1 651  ? -37.970 74.361  119.697 1.00 40.57 ? 649  ARG A NE    1 
ATOM   4667  C CZ    . ARG A  1 651  ? -39.217 74.795  119.816 1.00 48.56 ? 649  ARG A CZ    1 
ATOM   4668  N NH1   . ARG A  1 651  ? -40.251 73.977  119.675 1.00 45.43 ? 649  ARG A NH1   1 
ATOM   4669  N NH2   . ARG A  1 651  ? -39.433 76.082  120.082 1.00 45.57 ? 649  ARG A NH2   1 
ATOM   4670  N N     . MET A  1 652  ? -37.316 70.357  114.064 1.00 29.07 ? 650  MET A N     1 
ATOM   4671  C CA    . MET A  1 652  ? -36.988 70.895  112.743 1.00 29.65 ? 650  MET A CA    1 
ATOM   4672  C C     . MET A  1 652  ? -38.081 71.776  112.160 1.00 33.55 ? 650  MET A C     1 
ATOM   4673  O O     . MET A  1 652  ? -37.752 72.872  111.674 1.00 33.90 ? 650  MET A O     1 
ATOM   4674  C CB    . MET A  1 652  ? -36.632 69.766  111.766 1.00 28.75 ? 650  MET A CB    1 
ATOM   4675  C CG    . MET A  1 652  ? -36.351 70.270  110.350 1.00 29.29 ? 650  MET A CG    1 
ATOM   4676  S SD    . MET A  1 652  ? -36.049 68.923  109.195 1.00 31.74 ? 650  MET A SD    1 
ATOM   4677  C CE    . MET A  1 652  ? -34.383 68.439  109.656 1.00 30.55 ? 650  MET A CE    1 
ATOM   4678  N N     . PRO A  1 653  ? -39.368 71.394  112.173 1.00 31.83 ? 651  PRO A N     1 
ATOM   4679  C CA    . PRO A  1 653  ? -40.372 72.289  111.572 1.00 30.56 ? 651  PRO A CA    1 
ATOM   4680  C C     . PRO A  1 653  ? -40.364 73.680  112.177 1.00 32.31 ? 651  PRO A C     1 
ATOM   4681  O O     . PRO A  1 653  ? -40.451 74.663  111.433 1.00 31.86 ? 651  PRO A O     1 
ATOM   4682  C CB    . PRO A  1 653  ? -41.706 71.563  111.831 1.00 29.57 ? 651  PRO A CB    1 
ATOM   4683  C CG    . PRO A  1 653  ? -41.327 70.129  111.935 1.00 33.54 ? 651  PRO A CG    1 
ATOM   4684  C CD    . PRO A  1 653  ? -39.963 70.113  112.596 1.00 30.18 ? 651  PRO A CD    1 
ATOM   4685  N N     . THR A  1 654  ? -40.237 73.796  113.505 1.00 30.94 ? 652  THR A N     1 
ATOM   4686  C CA    . THR A  1 654  ? -40.196 75.116  114.122 1.00 31.79 ? 652  THR A CA    1 
ATOM   4687  C C     . THR A  1 654  ? -38.902 75.846  113.781 1.00 34.31 ? 652  THR A C     1 
ATOM   4688  O O     . THR A  1 654  ? -38.923 77.051  113.499 1.00 31.99 ? 652  THR A O     1 
ATOM   4689  C CB    . THR A  1 654  ? -40.357 74.995  115.636 1.00 36.02 ? 652  THR A CB    1 
ATOM   4690  O OG1   . THR A  1 654  ? -41.583 74.307  115.927 1.00 34.33 ? 652  THR A OG1   1 
ATOM   4691  C CG2   . THR A  1 654  ? -40.375 76.383  116.290 1.00 36.57 ? 652  THR A CG2   1 
ATOM   4692  N N     . LEU A  1 655  ? -37.768 75.134  113.801 1.00 31.39 ? 653  LEU A N     1 
ATOM   4693  C CA    . LEU A  1 655  ? -36.506 75.749  113.403 1.00 28.38 ? 653  LEU A CA    1 
ATOM   4694  C C     . LEU A  1 655  ? -36.574 76.256  111.967 1.00 32.79 ? 653  LEU A C     1 
ATOM   4695  O O     . LEU A  1 655  ? -36.039 77.329  111.664 1.00 31.19 ? 653  LEU A O     1 
ATOM   4696  C CB    . LEU A  1 655  ? -35.347 74.758  113.575 1.00 32.40 ? 653  LEU A CB    1 
ATOM   4697  C CG    . LEU A  1 655  ? -35.155 74.208  114.994 1.00 31.83 ? 653  LEU A CG    1 
ATOM   4698  C CD1   . LEU A  1 655  ? -33.925 73.291  115.090 1.00 28.97 ? 653  LEU A CD1   1 
ATOM   4699  C CD2   . LEU A  1 655  ? -35.069 75.339  116.005 1.00 33.31 ? 653  LEU A CD2   1 
ATOM   4700  N N     . LEU A  1 656  ? -37.253 75.514  111.075 1.00 30.50 ? 654  LEU A N     1 
ATOM   4701  C CA    . LEU A  1 656  ? -37.375 75.951  109.680 1.00 30.67 ? 654  LEU A CA    1 
ATOM   4702  C C     . LEU A  1 656  ? -37.978 77.339  109.596 1.00 33.56 ? 654  LEU A C     1 
ATOM   4703  O O     . LEU A  1 656  ? -37.447 78.223  108.905 1.00 31.00 ? 654  LEU A O     1 
ATOM   4704  C CB    . LEU A  1 656  ? -38.246 74.987  108.873 1.00 31.81 ? 654  LEU A CB    1 
ATOM   4705  C CG    . LEU A  1 656  ? -37.784 73.549  108.756 1.00 29.31 ? 654  LEU A CG    1 
ATOM   4706  C CD1   . LEU A  1 656  ? -38.678 72.793  107.820 1.00 26.65 ? 654  LEU A CD1   1 
ATOM   4707  C CD2   . LEU A  1 656  ? -36.344 73.528  108.302 1.00 27.89 ? 654  LEU A CD2   1 
ATOM   4708  N N     . GLY A  1 657  ? -39.115 77.533  110.275 1.00 29.86 ? 655  GLY A N     1 
ATOM   4709  C CA    . GLY A  1 657  ? -39.820 78.802  110.198 1.00 33.26 ? 655  GLY A CA    1 
ATOM   4710  C C     . GLY A  1 657  ? -38.988 79.954  110.712 1.00 30.31 ? 655  GLY A C     1 
ATOM   4711  O O     . GLY A  1 657  ? -39.006 81.048  110.148 1.00 29.37 ? 655  GLY A O     1 
ATOM   4712  N N     . LEU A  1 658  ? -38.227 79.722  111.779 1.00 31.01 ? 656  LEU A N     1 
ATOM   4713  C CA    . LEU A  1 658  ? -37.350 80.773  112.271 1.00 31.48 ? 656  LEU A CA    1 
ATOM   4714  C C     . LEU A  1 658  ? -36.252 81.090  111.256 1.00 29.41 ? 656  LEU A C     1 
ATOM   4715  O O     . LEU A  1 658  ? -35.989 82.261  110.958 1.00 30.09 ? 656  LEU A O     1 
ATOM   4716  C CB    . LEU A  1 658  ? -36.767 80.371  113.626 1.00 30.71 ? 656  LEU A CB    1 
ATOM   4717  C CG    . LEU A  1 658  ? -35.849 81.389  114.290 1.00 29.21 ? 656  LEU A CG    1 
ATOM   4718  C CD1   . LEU A  1 658  ? -36.562 82.735  114.435 1.00 31.14 ? 656  LEU A CD1   1 
ATOM   4719  C CD2   . LEU A  1 658  ? -35.415 80.862  115.654 1.00 29.23 ? 656  LEU A CD2   1 
ATOM   4720  N N     . ILE A  1 659  ? -35.612 80.059  110.694 1.00 30.25 ? 657  ILE A N     1 
ATOM   4721  C CA    . ILE A  1 659  ? -34.539 80.296  109.729 1.00 28.52 ? 657  ILE A CA    1 
ATOM   4722  C C     . ILE A  1 659  ? -35.077 81.002  108.493 1.00 30.40 ? 657  ILE A C     1 
ATOM   4723  O O     . ILE A  1 659  ? -34.437 81.911  107.948 1.00 27.05 ? 657  ILE A O     1 
ATOM   4724  C CB    . ILE A  1 659  ? -33.853 78.970  109.362 1.00 28.91 ? 657  ILE A CB    1 
ATOM   4725  C CG1   . ILE A  1 659  ? -33.220 78.365  110.611 1.00 30.04 ? 657  ILE A CG1   1 
ATOM   4726  C CG2   . ILE A  1 659  ? -32.828 79.167  108.258 1.00 29.00 ? 657  ILE A CG2   1 
ATOM   4727  C CD1   . ILE A  1 659  ? -32.449 77.093  110.342 1.00 29.75 ? 657  ILE A CD1   1 
ATOM   4728  N N     . ILE A  1 660  ? -36.256 80.588  108.029 1.00 27.58 ? 658  ILE A N     1 
ATOM   4729  C CA    . ILE A  1 660  ? -36.870 81.219  106.861 1.00 27.56 ? 658  ILE A CA    1 
ATOM   4730  C C     . ILE A  1 660  ? -37.046 82.716  107.097 1.00 30.73 ? 658  ILE A C     1 
ATOM   4731  O O     . ILE A  1 660  ? -36.647 83.547  106.270 1.00 32.35 ? 658  ILE A O     1 
ATOM   4732  C CB    . ILE A  1 660  ? -38.212 80.543  106.524 1.00 30.38 ? 658  ILE A CB    1 
ATOM   4733  C CG1   . ILE A  1 660  ? -38.002 79.127  105.990 1.00 30.05 ? 658  ILE A CG1   1 
ATOM   4734  C CG2   . ILE A  1 660  ? -39.007 81.392  105.520 1.00 27.92 ? 658  ILE A CG2   1 
ATOM   4735  C CD1   . ILE A  1 660  ? -39.305 78.314  105.913 1.00 33.18 ? 658  ILE A CD1   1 
ATOM   4736  N N     . ARG A  1 661  ? -37.621 83.087  108.244 1.00 29.14 ? 659  ARG A N     1 
ATOM   4737  C CA    . ARG A  1 661  ? -37.964 84.488  108.449 1.00 32.69 ? 659  ARG A CA    1 
ATOM   4738  C C     . ARG A  1 661  ? -36.779 85.321  108.912 1.00 32.94 ? 659  ARG A C     1 
ATOM   4739  O O     . ARG A  1 661  ? -36.699 86.500  108.556 1.00 32.03 ? 659  ARG A O     1 
ATOM   4740  C CB    . ARG A  1 661  ? -39.129 84.611  109.437 1.00 34.11 ? 659  ARG A CB    1 
ATOM   4741  C CG    . ARG A  1 661  ? -40.467 84.170  108.835 1.00 32.69 ? 659  ARG A CG    1 
ATOM   4742  C CD    . ARG A  1 661  ? -41.596 84.113  109.872 1.00 37.62 ? 659  ARG A CD    1 
ATOM   4743  N NE    . ARG A  1 661  ? -41.839 85.394  110.527 1.00 35.66 ? 659  ARG A NE    1 
ATOM   4744  C CZ    . ARG A  1 661  ? -41.779 85.595  111.837 1.00 34.77 ? 659  ARG A CZ    1 
ATOM   4745  N NH1   . ARG A  1 661  ? -41.513 84.610  112.677 1.00 36.12 ? 659  ARG A NH1   1 
ATOM   4746  N NH2   . ARG A  1 661  ? -42.007 86.811  112.320 1.00 39.29 ? 659  ARG A NH2   1 
ATOM   4747  N N     . GLU A  1 662  ? -35.854 84.748  109.688 1.00 27.87 ? 660  GLU A N     1 
ATOM   4748  C CA    . GLU A  1 662  ? -34.756 85.557  110.199 1.00 32.80 ? 660  GLU A CA    1 
ATOM   4749  C C     . GLU A  1 662  ? -33.628 85.686  109.179 1.00 28.40 ? 660  GLU A C     1 
ATOM   4750  O O     . GLU A  1 662  ? -33.062 86.773  109.018 1.00 30.44 ? 660  GLU A O     1 
ATOM   4751  C CB    . GLU A  1 662  ? -34.220 84.977  111.514 1.00 35.03 ? 660  GLU A CB    1 
ATOM   4752  C CG    . GLU A  1 662  ? -33.023 85.760  112.049 1.00 33.79 ? 660  GLU A CG    1 
ATOM   4753  C CD    . GLU A  1 662  ? -32.500 85.257  113.394 1.00 36.25 ? 660  GLU A CD    1 
ATOM   4754  O OE1   . GLU A  1 662  ? -32.441 84.032  113.614 1.00 38.49 ? 660  GLU A OE1   1 
ATOM   4755  O OE2   . GLU A  1 662  ? -32.126 86.100  114.232 1.00 34.94 ? 660  GLU A OE2   1 
ATOM   4756  N N     . ALA A  1 663  ? -33.283 84.599  108.492 1.00 29.66 ? 661  ALA A N     1 
ATOM   4757  C CA    . ALA A  1 663  ? -32.134 84.597  107.595 1.00 28.16 ? 661  ALA A CA    1 
ATOM   4758  C C     . ALA A  1 663  ? -32.530 84.725  106.130 1.00 29.45 ? 661  ALA A C     1 
ATOM   4759  O O     . ALA A  1 663  ? -31.646 84.820  105.271 1.00 29.93 ? 661  ALA A O     1 
ATOM   4760  C CB    . ALA A  1 663  ? -31.288 83.327  107.803 1.00 28.17 ? 661  ALA A CB    1 
ATOM   4761  N N     . GLY A  1 664  ? -33.827 84.750  105.827 1.00 28.95 ? 662  GLY A N     1 
ATOM   4762  C CA    . GLY A  1 664  ? -34.286 84.904  104.455 1.00 29.18 ? 662  GLY A CA    1 
ATOM   4763  C C     . GLY A  1 664  ? -34.144 83.680  103.585 1.00 27.69 ? 662  GLY A C     1 
ATOM   4764  O O     . GLY A  1 664  ? -34.082 83.806  102.359 1.00 31.57 ? 662  GLY A O     1 
ATOM   4765  N N     . LYS A  1 665  ? -34.086 82.498  104.181 1.00 28.62 ? 663  LYS A N     1 
ATOM   4766  C CA    . LYS A  1 665  ? -33.846 81.263  103.454 1.00 28.04 ? 663  LYS A CA    1 
ATOM   4767  C C     . LYS A  1 665  ? -35.146 80.650  102.961 1.00 27.30 ? 663  LYS A C     1 
ATOM   4768  O O     . LYS A  1 665  ? -36.203 80.824  103.564 1.00 27.23 ? 663  LYS A O     1 
ATOM   4769  C CB    . LYS A  1 665  ? -33.133 80.250  104.344 1.00 30.30 ? 663  LYS A CB    1 
ATOM   4770  C CG    . LYS A  1 665  ? -31.784 80.716  104.832 1.00 34.51 ? 663  LYS A CG    1 
ATOM   4771  C CD    . LYS A  1 665  ? -30.827 79.557  104.826 1.00 31.58 ? 663  LYS A CD    1 
ATOM   4772  C CE    . LYS A  1 665  ? -29.477 80.013  105.267 1.00 32.92 ? 663  LYS A CE    1 
ATOM   4773  N NZ    . LYS A  1 665  ? -28.488 78.931  105.052 1.00 36.34 ? 663  LYS A NZ    1 
ATOM   4774  N N     . SER A  1 666  ? -35.051 79.897  101.869 1.00 28.72 ? 664  SER A N     1 
ATOM   4775  C CA    . SER A  1 666  ? -36.173 79.072  101.454 1.00 27.48 ? 664  SER A CA    1 
ATOM   4776  C C     . SER A  1 666  ? -36.309 77.869  102.383 1.00 30.77 ? 664  SER A C     1 
ATOM   4777  O O     . SER A  1 666  ? -35.368 77.478  103.078 1.00 29.37 ? 664  SER A O     1 
ATOM   4778  C CB    . SER A  1 666  ? -35.986 78.588  100.022 1.00 30.72 ? 664  SER A CB    1 
ATOM   4779  O OG    . SER A  1 666  ? -34.935 77.647  99.983  1.00 29.79 ? 664  SER A OG    1 
ATOM   4780  N N     . ALA A  1 667  ? -37.504 77.277  102.379 1.00 27.70 ? 665  ALA A N     1 
ATOM   4781  C CA    . ALA A  1 667  ? -37.770 76.108  103.208 1.00 30.24 ? 665  ALA A CA    1 
ATOM   4782  C C     . ALA A  1 667  ? -36.862 74.944  102.833 1.00 28.74 ? 665  ALA A C     1 
ATOM   4783  O O     . ALA A  1 667  ? -36.366 74.229  103.709 1.00 29.45 ? 665  ALA A O     1 
ATOM   4784  C CB    . ALA A  1 667  ? -39.244 75.712  103.082 1.00 28.02 ? 665  ALA A CB    1 
ATOM   4785  N N     . LEU A  1 668  ? -36.647 74.730  101.534 1.00 27.02 ? 666  LEU A N     1 
ATOM   4786  C CA    . LEU A  1 668  ? -35.701 73.720  101.074 1.00 28.58 ? 666  LEU A CA    1 
ATOM   4787  C C     . LEU A  1 668  ? -34.326 73.913  101.700 1.00 29.60 ? 666  LEU A C     1 
ATOM   4788  O O     . LEU A  1 668  ? -33.740 72.974  102.250 1.00 28.24 ? 666  LEU A O     1 
ATOM   4789  C CB    . LEU A  1 668  ? -35.601 73.779  99.549  1.00 34.04 ? 666  LEU A CB    1 
ATOM   4790  C CG    . LEU A  1 668  ? -35.191 72.505  98.843  1.00 35.66 ? 666  LEU A CG    1 
ATOM   4791  C CD1   . LEU A  1 668  ? -35.950 71.346  99.455  1.00 36.66 ? 666  LEU A CD1   1 
ATOM   4792  C CD2   . LEU A  1 668  ? -35.525 72.633  97.360  1.00 40.59 ? 666  LEU A CD2   1 
ATOM   4793  N N     . ASN A  1 669  ? -33.790 75.132  101.617 1.00 30.45 ? 667  ASN A N     1 
ATOM   4794  C CA    . ASN A  1 669  ? -32.465 75.385  102.169 1.00 27.18 ? 667  ASN A CA    1 
ATOM   4795  C C     . ASN A  1 669  ? -32.471 75.352  103.693 1.00 27.69 ? 667  ASN A C     1 
ATOM   4796  O O     . ASN A  1 669  ? -31.447 75.028  104.301 1.00 29.15 ? 667  ASN A O     1 
ATOM   4797  C CB    . ASN A  1 669  ? -31.925 76.730  101.681 1.00 28.00 ? 667  ASN A CB    1 
ATOM   4798  C CG    . ASN A  1 669  ? -31.699 76.769  100.172 1.00 31.25 ? 667  ASN A CG    1 
ATOM   4799  O OD1   . ASN A  1 669  ? -31.931 77.790  99.533  1.00 34.98 ? 667  ASN A OD1   1 
ATOM   4800  N ND2   . ASN A  1 669  ? -31.235 75.662  99.603  1.00 31.23 ? 667  ASN A ND2   1 
ATOM   4801  N N     . ALA A  1 670  ? -33.593 75.703  104.327 1.00 23.20 ? 668  ALA A N     1 
ATOM   4802  C CA    . ALA A  1 670  ? -33.655 75.626  105.785 1.00 25.80 ? 668  ALA A CA    1 
ATOM   4803  C C     . ALA A  1 670  ? -33.613 74.183  106.271 1.00 26.89 ? 668  ALA A C     1 
ATOM   4804  O O     . ALA A  1 670  ? -32.943 73.878  107.269 1.00 24.81 ? 668  ALA A O     1 
ATOM   4805  C CB    . ALA A  1 670  ? -34.908 76.338  106.298 1.00 30.90 ? 668  ALA A CB    1 
ATOM   4806  N N     . ILE A  1 671  ? -34.332 73.280  105.594 1.00 25.09 ? 669  ILE A N     1 
ATOM   4807  C CA    . ILE A  1 671  ? -34.258 71.856  105.938 1.00 25.01 ? 669  ILE A CA    1 
ATOM   4808  C C     . ILE A  1 671  ? -32.814 71.364  105.864 1.00 27.26 ? 669  ILE A C     1 
ATOM   4809  O O     . ILE A  1 671  ? -32.312 70.673  106.765 1.00 24.10 ? 669  ILE A O     1 
ATOM   4810  C CB    . ILE A  1 671  ? -35.166 71.035  105.008 1.00 28.73 ? 669  ILE A CB    1 
ATOM   4811  C CG1   . ILE A  1 671  ? -36.633 71.383  105.251 1.00 29.01 ? 669  ILE A CG1   1 
ATOM   4812  C CG2   . ILE A  1 671  ? -34.910 69.541  105.190 1.00 27.63 ? 669  ILE A CG2   1 
ATOM   4813  C CD1   . ILE A  1 671  ? -37.541 71.001  104.102 1.00 31.37 ? 669  ILE A CD1   1 
ATOM   4814  N N     . ALA A  1 672  ? -32.129 71.696  104.772 1.00 27.38 ? 670  ALA A N     1 
ATOM   4815  C CA    . ALA A  1 672  ? -30.748 71.254  104.628 1.00 28.32 ? 670  ALA A CA    1 
ATOM   4816  C C     . ALA A  1 672  ? -29.879 71.839  105.732 1.00 26.64 ? 670  ALA A C     1 
ATOM   4817  O O     . ALA A  1 672  ? -28.983 71.163  106.250 1.00 27.76 ? 670  ALA A O     1 
ATOM   4818  C CB    . ALA A  1 672  ? -30.210 71.649  103.252 1.00 28.11 ? 670  ALA A CB    1 
ATOM   4819  N N     . GLU A  1 673  ? -30.152 73.083  106.133 1.00 24.28 ? 671  GLU A N     1 
ATOM   4820  C CA    . GLU A  1 673  ? -29.362 73.683  107.203 1.00 24.97 ? 671  GLU A CA    1 
ATOM   4821  C C     . GLU A  1 673  ? -29.601 72.991  108.544 1.00 28.65 ? 671  GLU A C     1 
ATOM   4822  O O     . GLU A  1 673  ? -28.658 72.808  109.327 1.00 25.36 ? 671  GLU A O     1 
ATOM   4823  C CB    . GLU A  1 673  ? -29.656 75.175  107.322 1.00 24.93 ? 671  GLU A CB    1 
ATOM   4824  C CG    . GLU A  1 673  ? -29.061 75.749  108.621 1.00 30.01 ? 671  GLU A CG    1 
ATOM   4825  C CD    . GLU A  1 673  ? -28.558 77.158  108.464 1.00 33.65 ? 671  GLU A CD    1 
ATOM   4826  O OE1   . GLU A  1 673  ? -29.120 77.893  107.618 1.00 36.93 ? 671  GLU A OE1   1 
ATOM   4827  O OE2   . GLU A  1 673  ? -27.607 77.536  109.188 1.00 31.15 ? 671  GLU A OE2   1 
ATOM   4828  N N     . VAL A  1 674  ? -30.851 72.621  108.851 1.00 26.07 ? 672  VAL A N     1 
ATOM   4829  C CA    . VAL A  1 674  ? -31.082 71.925  110.114 1.00 24.92 ? 672  VAL A CA    1 
ATOM   4830  C C     . VAL A  1 674  ? -30.481 70.528  110.056 1.00 24.14 ? 672  VAL A C     1 
ATOM   4831  O O     . VAL A  1 674  ? -29.939 70.026  111.047 1.00 23.92 ? 672  VAL A O     1 
ATOM   4832  C CB    . VAL A  1 674  ? -32.582 71.891  110.467 1.00 27.67 ? 672  VAL A CB    1 
ATOM   4833  C CG1   . VAL A  1 674  ? -32.812 71.126  111.795 1.00 24.87 ? 672  VAL A CG1   1 
ATOM   4834  C CG2   . VAL A  1 674  ? -33.132 73.317  110.562 1.00 24.09 ? 672  VAL A CG2   1 
ATOM   4835  N N     . ARG A  1 675  ? -30.553 69.881  108.892 1.00 22.03 ? 673  ARG A N     1 
ATOM   4836  C CA    . ARG A  1 675  ? -29.886 68.590  108.732 1.00 24.39 ? 673  ARG A CA    1 
ATOM   4837  C C     . ARG A  1 675  ? -28.390 68.706  108.985 1.00 24.01 ? 673  ARG A C     1 
ATOM   4838  O O     . ARG A  1 675  ? -27.800 67.859  109.661 1.00 23.43 ? 673  ARG A O     1 
ATOM   4839  C CB    . ARG A  1 675  ? -30.130 68.036  107.333 1.00 20.48 ? 673  ARG A CB    1 
ATOM   4840  C CG    . ARG A  1 675  ? -31.545 67.521  107.103 1.00 23.40 ? 673  ARG A CG    1 
ATOM   4841  C CD    . ARG A  1 675  ? -31.573 66.736  105.780 1.00 28.48 ? 673  ARG A CD    1 
ATOM   4842  N NE    . ARG A  1 675  ? -30.884 65.461  105.938 1.00 25.85 ? 673  ARG A NE    1 
ATOM   4843  C CZ    . ARG A  1 675  ? -30.481 64.693  104.935 1.00 27.28 ? 673  ARG A CZ    1 
ATOM   4844  N NH1   . ARG A  1 675  ? -30.663 65.054  103.673 1.00 24.27 ? 673  ARG A NH1   1 
ATOM   4845  N NH2   . ARG A  1 675  ? -29.885 63.534  105.207 1.00 23.10 ? 673  ARG A NH2   1 
ATOM   4846  N N     . GLU A  1 676  ? -27.763 69.743  108.428 1.00 25.06 ? 674  GLU A N     1 
ATOM   4847  C CA    . GLU A  1 676  ? -26.332 69.956  108.614 1.00 24.51 ? 674  GLU A CA    1 
ATOM   4848  C C     . GLU A  1 676  ? -26.001 70.131  110.086 1.00 25.18 ? 674  GLU A C     1 
ATOM   4849  O O     . GLU A  1 676  ? -25.014 69.575  110.582 1.00 24.44 ? 674  GLU A O     1 
ATOM   4850  C CB    . GLU A  1 676  ? -25.886 71.186  107.815 1.00 25.68 ? 674  GLU A CB    1 
ATOM   4851  C CG    . GLU A  1 676  ? -24.376 71.327  107.647 1.00 34.49 ? 674  GLU A CG    1 
ATOM   4852  C CD    . GLU A  1 676  ? -23.993 72.387  106.609 1.00 43.70 ? 674  GLU A CD    1 
ATOM   4853  O OE1   . GLU A  1 676  ? -24.888 72.830  105.848 1.00 49.80 ? 674  GLU A OE1   1 
ATOM   4854  O OE2   . GLU A  1 676  ? -22.804 72.779  106.562 1.00 43.67 ? 674  GLU A OE2   1 
ATOM   4855  N N     . ALA A  1 677  ? -26.832 70.882  110.812 1.00 26.41 ? 675  ALA A N     1 
ATOM   4856  C CA    . ALA A  1 677  ? -26.546 71.077  112.229 1.00 23.28 ? 675  ALA A CA    1 
ATOM   4857  C C     . ALA A  1 677  ? -26.665 69.765  112.991 1.00 23.35 ? 675  ALA A C     1 
ATOM   4858  O O     . ALA A  1 677  ? -25.816 69.445  113.834 1.00 26.12 ? 675  ALA A O     1 
ATOM   4859  C CB    . ALA A  1 677  ? -27.468 72.153  112.806 1.00 22.02 ? 675  ALA A CB    1 
ATOM   4860  N N     . ILE A  1 678  ? -27.703 68.980  112.696 1.00 23.23 ? 676  ILE A N     1 
ATOM   4861  C CA    . ILE A  1 678  ? -27.825 67.657  113.298 1.00 24.45 ? 676  ILE A CA    1 
ATOM   4862  C C     . ILE A  1 678  ? -26.618 66.788  112.941 1.00 25.17 ? 676  ILE A C     1 
ATOM   4863  O O     . ILE A  1 678  ? -26.114 66.029  113.772 1.00 21.08 ? 676  ILE A O     1 
ATOM   4864  C CB    . ILE A  1 678  ? -29.140 66.998  112.844 1.00 22.53 ? 676  ILE A CB    1 
ATOM   4865  C CG1   . ILE A  1 678  ? -30.350 67.749  113.421 1.00 26.89 ? 676  ILE A CG1   1 
ATOM   4866  C CG2   . ILE A  1 678  ? -29.158 65.521  113.212 1.00 24.75 ? 676  ILE A CG2   1 
ATOM   4867  C CD1   . ILE A  1 678  ? -31.617 67.578  112.559 1.00 26.47 ? 676  ILE A CD1   1 
ATOM   4868  N N     . ASP A  1 679  ? -26.190 66.833  111.682 1.00 22.57 ? 677  ASP A N     1 
ATOM   4869  C CA    . ASP A  1 679  ? -25.067 66.001  111.246 1.00 23.90 ? 677  ASP A CA    1 
ATOM   4870  C C     . ASP A  1 679  ? -23.773 66.405  111.948 1.00 25.88 ? 677  ASP A C     1 
ATOM   4871  O O     . ASP A  1 679  ? -23.016 65.537  112.397 1.00 23.24 ? 677  ASP A O     1 
ATOM   4872  C CB    . ASP A  1 679  ? -24.895 66.085  109.724 1.00 25.06 ? 677  ASP A CB    1 
ATOM   4873  C CG    . ASP A  1 679  ? -26.042 65.409  108.942 1.00 29.31 ? 677  ASP A CG    1 
ATOM   4874  O OD1   . ASP A  1 679  ? -26.678 64.490  109.476 1.00 27.66 ? 677  ASP A OD1   1 
ATOM   4875  O OD2   . ASP A  1 679  ? -26.289 65.783  107.770 1.00 30.26 ? 677  ASP A OD2   1 
ATOM   4876  N N     . PHE A  1 680  ? -23.507 67.715  112.065 1.00 23.69 ? 678  PHE A N     1 
ATOM   4877  C CA    . PHE A  1 680  ? -22.339 68.174  112.822 1.00 22.05 ? 678  PHE A CA    1 
ATOM   4878  C C     . PHE A  1 680  ? -22.349 67.612  114.239 1.00 25.67 ? 678  PHE A C     1 
ATOM   4879  O O     . PHE A  1 680  ? -21.334 67.105  114.731 1.00 23.76 ? 678  PHE A O     1 
ATOM   4880  C CB    . PHE A  1 680  ? -22.302 69.700  112.894 1.00 22.35 ? 678  PHE A CB    1 
ATOM   4881  C CG    . PHE A  1 680  ? -21.649 70.373  111.715 1.00 24.19 ? 678  PHE A CG    1 
ATOM   4882  C CD1   . PHE A  1 680  ? -20.371 70.011  111.300 1.00 23.18 ? 678  PHE A CD1   1 
ATOM   4883  C CD2   . PHE A  1 680  ? -22.300 71.398  111.061 1.00 25.18 ? 678  PHE A CD2   1 
ATOM   4884  C CE1   . PHE A  1 680  ? -19.757 70.653  110.228 1.00 25.33 ? 678  PHE A CE1   1 
ATOM   4885  C CE2   . PHE A  1 680  ? -21.701 72.051  109.978 1.00 26.15 ? 678  PHE A CE2   1 
ATOM   4886  C CZ    . PHE A  1 680  ? -20.423 71.671  109.561 1.00 27.52 ? 678  PHE A CZ    1 
ATOM   4887  N N     . LEU A  1 681  ? -23.491 67.719  114.916 1.00 25.70 ? 679  LEU A N     1 
ATOM   4888  C CA    . LEU A  1 681  ? -23.589 67.245  116.294 1.00 25.57 ? 679  LEU A CA    1 
ATOM   4889  C C     . LEU A  1 681  ? -23.275 65.758  116.370 1.00 28.14 ? 679  LEU A C     1 
ATOM   4890  O O     . LEU A  1 681  ? -22.487 65.314  117.214 1.00 24.71 ? 679  LEU A O     1 
ATOM   4891  C CB    . LEU A  1 681  ? -24.989 67.537  116.847 1.00 22.66 ? 679  LEU A CB    1 
ATOM   4892  C CG    . LEU A  1 681  ? -25.339 69.012  117.079 1.00 29.81 ? 679  LEU A CG    1 
ATOM   4893  C CD1   . LEU A  1 681  ? -26.853 69.212  117.182 1.00 24.97 ? 679  LEU A CD1   1 
ATOM   4894  C CD2   . LEU A  1 681  ? -24.641 69.533  118.341 1.00 26.82 ? 679  LEU A CD2   1 
ATOM   4895  N N     . ARG A  1 682  ? -23.856 64.972  115.467 1.00 24.52 ? 680  ARG A N     1 
ATOM   4896  C CA    . ARG A  1 682  ? -23.634 63.531  115.539 1.00 26.08 ? 680  ARG A CA    1 
ATOM   4897  C C     . ARG A  1 682  ? -22.248 63.150  115.053 1.00 26.03 ? 680  ARG A C     1 
ATOM   4898  O O     . ARG A  1 682  ? -21.644 62.211  115.581 1.00 25.11 ? 680  ARG A O     1 
ATOM   4899  C CB    . ARG A  1 682  ? -24.705 62.797  114.737 1.00 21.40 ? 680  ARG A CB    1 
ATOM   4900  C CG    . ARG A  1 682  ? -26.037 62.767  115.446 1.00 25.48 ? 680  ARG A CG    1 
ATOM   4901  C CD    . ARG A  1 682  ? -27.118 62.217  114.537 1.00 27.98 ? 680  ARG A CD    1 
ATOM   4902  N NE    . ARG A  1 682  ? -28.415 62.187  115.198 1.00 24.87 ? 680  ARG A NE    1 
ATOM   4903  C CZ    . ARG A  1 682  ? -29.560 61.975  114.564 1.00 29.53 ? 680  ARG A CZ    1 
ATOM   4904  N NH1   . ARG A  1 682  ? -29.600 61.794  113.252 1.00 25.89 ? 680  ARG A NH1   1 
ATOM   4905  N NH2   . ARG A  1 682  ? -30.689 61.974  115.256 1.00 30.28 ? 680  ARG A NH2   1 
ATOM   4906  N N     . TYR A  1 683  ? -21.728 63.864  114.054 1.00 26.25 ? 681  TYR A N     1 
ATOM   4907  C CA    . TYR A  1 683  ? -20.391 63.569  113.558 1.00 25.71 ? 681  TYR A CA    1 
ATOM   4908  C C     . TYR A  1 683  ? -19.329 63.839  114.622 1.00 25.80 ? 681  TYR A C     1 
ATOM   4909  O O     . TYR A  1 683  ? -18.456 62.998  114.861 1.00 24.30 ? 681  TYR A O     1 
ATOM   4910  C CB    . TYR A  1 683  ? -20.110 64.388  112.305 1.00 24.69 ? 681  TYR A CB    1 
ATOM   4911  C CG    . TYR A  1 683  ? -18.715 64.174  111.780 1.00 25.30 ? 681  TYR A CG    1 
ATOM   4912  C CD1   . TYR A  1 683  ? -18.399 63.026  111.065 1.00 24.60 ? 681  TYR A CD1   1 
ATOM   4913  C CD2   . TYR A  1 683  ? -17.706 65.103  112.028 1.00 24.31 ? 681  TYR A CD2   1 
ATOM   4914  C CE1   . TYR A  1 683  ? -17.114 62.811  110.580 1.00 22.14 ? 681  TYR A CE1   1 
ATOM   4915  C CE2   . TYR A  1 683  ? -16.433 64.904  111.559 1.00 23.69 ? 681  TYR A CE2   1 
ATOM   4916  C CZ    . TYR A  1 683  ? -16.137 63.758  110.823 1.00 25.42 ? 681  TYR A CZ    1 
ATOM   4917  O OH    . TYR A  1 683  ? -14.853 63.557  110.351 1.00 23.00 ? 681  TYR A OH    1 
ATOM   4918  N N     . TYR A  1 684  ? -19.372 65.015  115.265 1.00 22.94 ? 682  TYR A N     1 
ATOM   4919  C CA    . TYR A  1 684  ? -18.331 65.317  116.247 1.00 25.36 ? 682  TYR A CA    1 
ATOM   4920  C C     . TYR A  1 684  ? -18.469 64.447  117.488 1.00 29.02 ? 682  TYR A C     1 
ATOM   4921  O O     . TYR A  1 684  ? -17.468 64.169  118.161 1.00 26.78 ? 682  TYR A O     1 
ATOM   4922  C CB    . TYR A  1 684  ? -18.353 66.795  116.635 1.00 24.91 ? 682  TYR A CB    1 
ATOM   4923  C CG    . TYR A  1 684  ? -17.996 67.704  115.480 1.00 25.07 ? 682  TYR A CG    1 
ATOM   4924  C CD1   . TYR A  1 684  ? -16.959 67.376  114.621 1.00 24.25 ? 682  TYR A CD1   1 
ATOM   4925  C CD2   . TYR A  1 684  ? -18.709 68.871  115.243 1.00 21.22 ? 682  TYR A CD2   1 
ATOM   4926  C CE1   . TYR A  1 684  ? -16.621 68.192  113.547 1.00 24.39 ? 682  TYR A CE1   1 
ATOM   4927  C CE2   . TYR A  1 684  ? -18.378 69.700  114.196 1.00 21.46 ? 682  TYR A CE2   1 
ATOM   4928  C CZ    . TYR A  1 684  ? -17.331 69.353  113.343 1.00 26.09 ? 682  TYR A CZ    1 
ATOM   4929  O OH    . TYR A  1 684  ? -17.012 70.166  112.280 1.00 23.67 ? 682  TYR A OH    1 
ATOM   4930  N N     . ALA A  1 685  ? -19.691 64.014  117.812 1.00 25.74 ? 683  ALA A N     1 
ATOM   4931  C CA    . ALA A  1 685  ? -19.858 63.051  118.903 1.00 25.97 ? 683  ALA A CA    1 
ATOM   4932  C C     . ALA A  1 685  ? -19.159 61.734  118.579 1.00 25.84 ? 683  ALA A C     1 
ATOM   4933  O O     . ALA A  1 685  ? -18.409 61.194  119.401 1.00 24.17 ? 683  ALA A O     1 
ATOM   4934  C CB    . ALA A  1 685  ? -21.346 62.813  119.184 1.00 26.66 ? 683  ALA A CB    1 
ATOM   4935  N N     . GLU A  1 686  ? -19.398 61.196  117.379 1.00 27.12 ? 684  GLU A N     1 
ATOM   4936  C CA    . GLU A  1 686  ? -18.756 59.938  117.009 1.00 28.33 ? 684  GLU A CA    1 
ATOM   4937  C C     . GLU A  1 686  ? -17.239 60.092  116.949 1.00 25.92 ? 684  GLU A C     1 
ATOM   4938  O O     . GLU A  1 686  ? -16.506 59.222  117.429 1.00 25.74 ? 684  GLU A O     1 
ATOM   4939  C CB    . GLU A  1 686  ? -19.302 59.422  115.672 1.00 30.10 ? 684  GLU A CB    1 
ATOM   4940  C CG    . GLU A  1 686  ? -18.563 58.190  115.111 1.00 36.07 ? 684  GLU A CG    1 
ATOM   4941  C CD    . GLU A  1 686  ? -18.685 56.924  115.975 1.00 37.84 ? 684  GLU A CD    1 
ATOM   4942  O OE1   . GLU A  1 686  ? -19.500 56.892  116.933 1.00 40.67 ? 684  GLU A OE1   1 
ATOM   4943  O OE2   . GLU A  1 686  ? -17.945 55.948  115.696 1.00 36.62 ? 684  GLU A OE2   1 
ATOM   4944  N N     . GLN A  1 687  ? -16.748 61.191  116.365 1.00 25.03 ? 685  GLN A N     1 
ATOM   4945  C CA    . GLN A  1 687  ? -15.304 61.391  116.303 1.00 24.51 ? 685  GLN A CA    1 
ATOM   4946  C C     . GLN A  1 687  ? -14.709 61.486  117.702 1.00 24.13 ? 685  GLN A C     1 
ATOM   4947  O O     . GLN A  1 687  ? -13.604 60.988  117.944 1.00 22.34 ? 685  GLN A O     1 
ATOM   4948  C CB    . GLN A  1 687  ? -14.968 62.640  115.481 1.00 24.80 ? 685  GLN A CB    1 
ATOM   4949  C CG    . GLN A  1 687  ? -15.374 62.495  114.019 1.00 24.39 ? 685  GLN A CG    1 
ATOM   4950  C CD    . GLN A  1 687  ? -14.661 61.344  113.354 1.00 26.82 ? 685  GLN A CD    1 
ATOM   4951  O OE1   . GLN A  1 687  ? -13.427 61.287  113.338 1.00 27.18 ? 685  GLN A OE1   1 
ATOM   4952  N NE2   . GLN A  1 687  ? -15.428 60.406  112.819 1.00 29.94 ? 685  GLN A NE2   1 
ATOM   4953  N N     . THR A  1 688  ? -15.452 62.074  118.640 1.00 24.67 ? 686  THR A N     1 
ATOM   4954  C CA    . THR A  1 688  ? -15.010 62.101  120.032 1.00 25.11 ? 686  THR A CA    1 
ATOM   4955  C C     . THR A  1 688  ? -14.923 60.695  120.616 1.00 27.81 ? 686  THR A C     1 
ATOM   4956  O O     . THR A  1 688  ? -13.932 60.340  121.277 1.00 28.53 ? 686  THR A O     1 
ATOM   4957  C CB    . THR A  1 688  ? -15.962 62.976  120.853 1.00 27.39 ? 686  THR A CB    1 
ATOM   4958  O OG1   . THR A  1 688  ? -15.785 64.343  120.458 1.00 25.58 ? 686  THR A OG1   1 
ATOM   4959  C CG2   . THR A  1 688  ? -15.677 62.823  122.346 1.00 26.21 ? 686  THR A CG2   1 
ATOM   4960  N N     . ARG A  1 689  ? -15.959 59.880  120.399 1.00 26.75 ? 687  ARG A N     1 
ATOM   4961  C CA    . ARG A  1 689  ? -15.937 58.519  120.923 1.00 26.78 ? 687  ARG A CA    1 
ATOM   4962  C C     . ARG A  1 689  ? -14.815 57.710  120.296 1.00 27.75 ? 687  ARG A C     1 
ATOM   4963  O O     . ARG A  1 689  ? -14.319 56.764  120.913 1.00 28.58 ? 687  ARG A O     1 
ATOM   4964  C CB    . ARG A  1 689  ? -17.292 57.833  120.684 1.00 28.01 ? 687  ARG A CB    1 
ATOM   4965  C CG    . ARG A  1 689  ? -18.441 58.447  121.481 1.00 29.42 ? 687  ARG A CG    1 
ATOM   4966  C CD    . ARG A  1 689  ? -19.692 57.605  121.380 1.00 27.17 ? 687  ARG A CD    1 
ATOM   4967  N NE    . ARG A  1 689  ? -20.231 57.636  120.022 1.00 29.68 ? 687  ARG A NE    1 
ATOM   4968  C CZ    . ARG A  1 689  ? -21.199 58.454  119.626 1.00 31.73 ? 687  ARG A CZ    1 
ATOM   4969  N NH1   . ARG A  1 689  ? -21.772 59.304  120.466 1.00 32.83 ? 687  ARG A NH1   1 
ATOM   4970  N NH2   . ARG A  1 689  ? -21.619 58.401  118.365 1.00 30.01 ? 687  ARG A NH2   1 
ATOM   4971  N N     . ARG A  1 690  ? -14.400 58.068  119.076 1.00 24.70 ? 688  ARG A N     1 
ATOM   4972  C CA    . ARG A  1 690  ? -13.310 57.365  118.416 1.00 28.96 ? 688  ARG A CA    1 
ATOM   4973  C C     . ARG A  1 690  ? -11.930 57.791  118.919 1.00 29.06 ? 688  ARG A C     1 
ATOM   4974  O O     . ARG A  1 690  ? -10.981 57.015  118.768 1.00 27.56 ? 688  ARG A O     1 
ATOM   4975  C CB    . ARG A  1 690  ? -13.370 57.579  116.890 1.00 25.55 ? 688  ARG A CB    1 
ATOM   4976  C CG    . ARG A  1 690  ? -14.568 56.933  116.168 1.00 27.99 ? 688  ARG A CG    1 
ATOM   4977  C CD    . ARG A  1 690  ? -14.495 55.406  116.194 1.00 33.60 ? 688  ARG A CD    1 
ATOM   4978  N NE    . ARG A  1 690  ? -13.366 54.926  115.402 1.00 32.15 ? 688  ARG A NE    1 
ATOM   4979  C CZ    . ARG A  1 690  ? -12.307 54.314  115.911 1.00 33.84 ? 688  ARG A CZ    1 
ATOM   4980  N NH1   . ARG A  1 690  ? -12.230 54.027  117.203 1.00 30.06 ? 688  ARG A NH1   1 
ATOM   4981  N NH2   . ARG A  1 690  ? -11.295 53.994  115.109 1.00 29.73 ? 688  ARG A NH2   1 
ATOM   4982  N N     . THR A  1 691  ? -11.783 58.987  119.509 1.00 27.66 ? 689  THR A N     1 
ATOM   4983  C CA    . THR A  1 691  ? -10.435 59.536  119.661 1.00 27.14 ? 689  THR A CA    1 
ATOM   4984  C C     . THR A  1 691  ? -10.063 60.005  121.059 1.00 33.55 ? 689  THR A C     1 
ATOM   4985  O O     . THR A  1 691  ? -8.979  59.671  121.548 1.00 34.03 ? 689  THR A O     1 
ATOM   4986  C CB    . THR A  1 691  ? -10.205 60.703  118.684 1.00 30.88 ? 689  THR A CB    1 
ATOM   4987  O OG1   . THR A  1 691  ? -11.204 61.723  118.871 1.00 29.18 ? 689  THR A OG1   1 
ATOM   4988  C CG2   . THR A  1 691  ? -10.247 60.213  117.235 1.00 30.17 ? 689  THR A CG2   1 
ATOM   4989  N N     . LEU A  1 692  ? -10.921 60.779  121.711 1.00 34.28 ? 690  LEU A N     1 
ATOM   4990  C CA    . LEU A  1 692  ? -10.464 61.627  122.806 1.00 32.90 ? 690  LEU A CA    1 
ATOM   4991  C C     . LEU A  1 692  ? -10.256 60.846  124.100 1.00 35.98 ? 690  LEU A C     1 
ATOM   4992  O O     . LEU A  1 692  ? -11.130 60.087  124.535 1.00 30.89 ? 690  LEU A O     1 
ATOM   4993  C CB    . LEU A  1 692  ? -11.450 62.773  123.020 1.00 31.46 ? 690  LEU A CB    1 
ATOM   4994  C CG    . LEU A  1 692  ? -11.463 63.749  121.835 1.00 32.46 ? 690  LEU A CG    1 
ATOM   4995  C CD1   . LEU A  1 692  ? -12.380 64.918  122.111 1.00 30.84 ? 690  LEU A CD1   1 
ATOM   4996  C CD2   . LEU A  1 692  ? -10.050 64.241  121.509 1.00 34.77 ? 690  LEU A CD2   1 
ATOM   4997  N N     . GLY A  1 693  ? -9.085  61.040  124.710 1.00 30.60 ? 691  GLY A N     1 
ATOM   4998  C CA    . GLY A  1 693  ? -8.770  60.458  125.991 1.00 34.42 ? 691  GLY A CA    1 
ATOM   4999  C C     . GLY A  1 693  ? -8.221  61.495  126.951 1.00 37.15 ? 691  GLY A C     1 
ATOM   5000  O O     . GLY A  1 693  ? -8.243  62.705  126.690 1.00 34.40 ? 691  GLY A O     1 
ATOM   5001  N N     . PRO A  1 694  ? -7.703  61.027  128.088 1.00 38.04 ? 692  PRO A N     1 
ATOM   5002  C CA    . PRO A  1 694  ? -7.240  61.967  129.125 1.00 38.97 ? 692  PRO A CA    1 
ATOM   5003  C C     . PRO A  1 694  ? -6.037  62.803  128.704 1.00 41.88 ? 692  PRO A C     1 
ATOM   5004  O O     . PRO A  1 694  ? -5.900  63.946  129.159 1.00 41.83 ? 692  PRO A O     1 
ATOM   5005  C CB    . PRO A  1 694  ? -6.904  61.045  130.306 1.00 41.68 ? 692  PRO A CB    1 
ATOM   5006  C CG    . PRO A  1 694  ? -7.725  59.814  130.078 1.00 38.92 ? 692  PRO A CG    1 
ATOM   5007  C CD    . PRO A  1 694  ? -7.786  59.642  128.573 1.00 35.40 ? 692  PRO A CD    1 
ATOM   5008  N N     . GLY A  1 695  ? -5.167  62.282  127.847 1.00 38.26 ? 693  GLY A N     1 
ATOM   5009  C CA    . GLY A  1 695  ? -4.030  63.049  127.398 1.00 41.14 ? 693  GLY A CA    1 
ATOM   5010  C C     . GLY A  1 695  ? -4.319  64.138  126.393 1.00 40.02 ? 693  GLY A C     1 
ATOM   5011  O O     . GLY A  1 695  ? -3.393  64.859  126.006 1.00 40.46 ? 693  GLY A O     1 
ATOM   5012  N N     . HIS A  1 696  ? -5.567  64.288  125.941 1.00 37.60 ? 694  HIS A N     1 
ATOM   5013  C CA    . HIS A  1 696  ? -5.904  65.329  124.969 1.00 34.42 ? 694  HIS A CA    1 
ATOM   5014  C C     . HIS A  1 696  ? -6.634  66.463  125.689 1.00 37.14 ? 694  HIS A C     1 
ATOM   5015  O O     . HIS A  1 696  ? -7.842  66.670  125.549 1.00 40.29 ? 694  HIS A O     1 
ATOM   5016  C CB    . HIS A  1 696  ? -6.740  64.746  123.825 1.00 37.82 ? 694  HIS A CB    1 
ATOM   5017  C CG    . HIS A  1 696  ? -6.207  63.451  123.290 1.00 34.66 ? 694  HIS A CG    1 
ATOM   5018  N ND1   . HIS A  1 696  ? -6.883  62.258  123.422 1.00 34.75 ? 694  HIS A ND1   1 
ATOM   5019  C CD2   . HIS A  1 696  ? -5.053  63.160  122.641 1.00 33.94 ? 694  HIS A CD2   1 
ATOM   5020  C CE1   . HIS A  1 696  ? -6.171  61.285  122.882 1.00 33.94 ? 694  HIS A CE1   1 
ATOM   5021  N NE2   . HIS A  1 696  ? -5.058  61.807  122.394 1.00 34.80 ? 694  HIS A NE2   1 
ATOM   5022  N N     . GLY A  1 697  ? -5.865  67.202  126.481 1.00 38.12 ? 695  GLY A N     1 
ATOM   5023  C CA    . GLY A  1 697  ? -6.415  68.249  127.302 1.00 34.88 ? 695  GLY A CA    1 
ATOM   5024  C C     . GLY A  1 697  ? -7.032  69.352  126.471 1.00 34.07 ? 695  GLY A C     1 
ATOM   5025  O O     . GLY A  1 697  ? -6.582  69.656  125.364 1.00 33.41 ? 695  GLY A O     1 
ATOM   5026  N N     . PRO A  1 698  ? -8.080  69.977  126.990 1.00 35.75 ? 696  PRO A N     1 
ATOM   5027  C CA    . PRO A  1 698  ? -8.701  71.094  126.269 1.00 32.90 ? 696  PRO A CA    1 
ATOM   5028  C C     . PRO A  1 698  ? -7.768  72.294  126.178 1.00 33.49 ? 696  PRO A C     1 
ATOM   5029  O O     . PRO A  1 698  ? -6.841  72.463  126.970 1.00 33.88 ? 696  PRO A O     1 
ATOM   5030  C CB    . PRO A  1 698  ? -9.936  71.419  127.116 1.00 36.19 ? 696  PRO A CB    1 
ATOM   5031  C CG    . PRO A  1 698  ? -10.176 70.170  127.925 1.00 39.57 ? 696  PRO A CG    1 
ATOM   5032  C CD    . PRO A  1 698  ? -8.808  69.647  128.225 1.00 39.61 ? 696  PRO A CD    1 
ATOM   5033  N N     . LEU A  1 699  ? -8.033  73.137  125.176 1.00 31.63 ? 697  LEU A N     1 
ATOM   5034  C CA    . LEU A  1 699  ? -7.327  74.409  125.056 1.00 31.35 ? 697  LEU A CA    1 
ATOM   5035  C C     . LEU A  1 699  ? -7.716  75.370  126.171 1.00 31.94 ? 697  LEU A C     1 
ATOM   5036  O O     . LEU A  1 699  ? -6.855  76.058  126.729 1.00 31.85 ? 697  LEU A O     1 
ATOM   5037  C CB    . LEU A  1 699  ? -7.628  75.050  123.698 1.00 30.13 ? 697  LEU A CB    1 
ATOM   5038  C CG    . LEU A  1 699  ? -7.031  74.428  122.447 1.00 32.64 ? 697  LEU A CG    1 
ATOM   5039  C CD1   . LEU A  1 699  ? -7.452  75.243  121.234 1.00 30.57 ? 697  LEU A CD1   1 
ATOM   5040  C CD2   . LEU A  1 699  ? -5.511  74.334  122.549 1.00 34.21 ? 697  LEU A CD2   1 
ATOM   5041  N N     . GLY A  1 700  ? -9.007  75.433  126.504 1.00 31.72 ? 698  GLY A N     1 
ATOM   5042  C CA    . GLY A  1 700  ? -9.533  76.457  127.376 1.00 30.41 ? 698  GLY A CA    1 
ATOM   5043  C C     . GLY A  1 700  ? -10.723 77.135  126.726 1.00 31.18 ? 698  GLY A C     1 
ATOM   5044  O O     . GLY A  1 700  ? -11.301 76.622  125.754 1.00 33.22 ? 698  GLY A O     1 
ATOM   5045  N N     . PRO A  1 701  ? -11.115 78.299  127.235 1.00 33.69 ? 699  PRO A N     1 
ATOM   5046  C CA    . PRO A  1 701  ? -12.244 79.021  126.627 1.00 31.61 ? 699  PRO A CA    1 
ATOM   5047  C C     . PRO A  1 701  ? -11.985 79.288  125.149 1.00 31.82 ? 699  PRO A C     1 
ATOM   5048  O O     . PRO A  1 701  ? -10.916 79.772  124.763 1.00 31.70 ? 699  PRO A O     1 
ATOM   5049  C CB    . PRO A  1 701  ? -12.312 80.317  127.440 1.00 33.24 ? 699  PRO A CB    1 
ATOM   5050  C CG    . PRO A  1 701  ? -11.741 79.947  128.768 1.00 35.68 ? 699  PRO A CG    1 
ATOM   5051  C CD    . PRO A  1 701  ? -10.667 78.927  128.493 1.00 32.51 ? 699  PRO A CD    1 
ATOM   5052  N N     . ILE A  1 702  ? -12.965 78.941  124.317 1.00 31.87 ? 700  ILE A N     1 
ATOM   5053  C CA    . ILE A  1 702  ? -12.884 79.126  122.874 1.00 30.04 ? 700  ILE A CA    1 
ATOM   5054  C C     . ILE A  1 702  ? -13.971 80.098  122.451 1.00 31.14 ? 700  ILE A C     1 
ATOM   5055  O O     . ILE A  1 702  ? -15.138 79.940  122.830 1.00 29.63 ? 700  ILE A O     1 
ATOM   5056  C CB    . ILE A  1 702  ? -13.020 77.790  122.124 1.00 28.96 ? 700  ILE A CB    1 
ATOM   5057  C CG1   . ILE A  1 702  ? -11.766 76.934  122.379 1.00 28.74 ? 700  ILE A CG1   1 
ATOM   5058  C CG2   . ILE A  1 702  ? -13.278 78.045  120.671 1.00 28.69 ? 700  ILE A CG2   1 
ATOM   5059  C CD1   . ILE A  1 702  ? -11.659 75.744  121.495 1.00 33.08 ? 700  ILE A CD1   1 
ATOM   5060  N N     . VAL A  1 703  ? -13.589 81.112  121.681 1.00 28.13 ? 701  VAL A N     1 
ATOM   5061  C CA    . VAL A  1 703  ? -14.547 82.069  121.151 1.00 27.68 ? 701  VAL A CA    1 
ATOM   5062  C C     . VAL A  1 703  ? -14.989 81.546  119.792 1.00 30.26 ? 701  VAL A C     1 
ATOM   5063  O O     . VAL A  1 703  ? -14.151 81.268  118.935 1.00 27.59 ? 701  VAL A O     1 
ATOM   5064  C CB    . VAL A  1 703  ? -13.941 83.477  121.036 1.00 29.18 ? 701  VAL A CB    1 
ATOM   5065  C CG1   . VAL A  1 703  ? -14.899 84.391  120.277 1.00 28.58 ? 701  VAL A CG1   1 
ATOM   5066  C CG2   . VAL A  1 703  ? -13.666 84.061  122.413 1.00 29.36 ? 701  VAL A CG2   1 
ATOM   5067  N N     . CYS A  1 704  ? -16.294 81.378  119.607 1.00 28.18 ? 702  CYS A N     1 
ATOM   5068  C CA    . CYS A  1 704  ? -16.855 80.914  118.343 1.00 29.71 ? 702  CYS A CA    1 
ATOM   5069  C C     . CYS A  1 704  ? -17.623 82.061  117.708 1.00 28.66 ? 702  CYS A C     1 
ATOM   5070  O O     . CYS A  1 704  ? -18.606 82.540  118.275 1.00 26.78 ? 702  CYS A O     1 
ATOM   5071  C CB    . CYS A  1 704  ? -17.768 79.709  118.555 1.00 26.86 ? 702  CYS A CB    1 
ATOM   5072  S SG    . CYS A  1 704  ? -16.913 78.285  119.246 1.00 31.51 ? 702  CYS A SG    1 
ATOM   5073  N N     . ILE A  1 705  ? -17.174 82.502  116.539 1.00 27.80 ? 703  ILE A N     1 
ATOM   5074  C CA    . ILE A  1 705  ? -17.782 83.624  115.839 1.00 29.46 ? 703  ILE A CA    1 
ATOM   5075  C C     . ILE A  1 705  ? -18.345 83.056  114.550 1.00 27.53 ? 703  ILE A C     1 
ATOM   5076  O O     . ILE A  1 705  ? -17.600 82.496  113.738 1.00 25.92 ? 703  ILE A O     1 
ATOM   5077  C CB    . ILE A  1 705  ? -16.769 84.750  115.569 1.00 31.19 ? 703  ILE A CB    1 
ATOM   5078  C CG1   . ILE A  1 705  ? -16.275 85.346  116.892 1.00 30.62 ? 703  ILE A CG1   1 
ATOM   5079  C CG2   . ILE A  1 705  ? -17.360 85.826  114.686 1.00 27.38 ? 703  ILE A CG2   1 
ATOM   5080  C CD1   . ILE A  1 705  ? -14.989 86.141  116.755 1.00 32.82 ? 703  ILE A CD1   1 
ATOM   5081  N N     . SER A  1 706  ? -19.656 83.148  114.385 1.00 26.87 ? 704  SER A N     1 
ATOM   5082  C CA    . SER A  1 706  ? -20.327 82.468  113.290 1.00 26.91 ? 704  SER A CA    1 
ATOM   5083  C C     . SER A  1 706  ? -20.990 83.479  112.366 1.00 24.43 ? 704  SER A C     1 
ATOM   5084  O O     . SER A  1 706  ? -21.248 84.622  112.766 1.00 26.29 ? 704  SER A O     1 
ATOM   5085  C CB    . SER A  1 706  ? -21.373 81.487  113.833 1.00 26.77 ? 704  SER A CB    1 
ATOM   5086  O OG    . SER A  1 706  ? -22.198 82.153  114.772 1.00 29.51 ? 704  SER A OG    1 
ATOM   5087  N N     . PRO A  1 707  ? -21.262 83.096  111.117 1.00 25.04 ? 705  PRO A N     1 
ATOM   5088  C CA    . PRO A  1 707  ? -21.788 84.035  110.126 1.00 29.47 ? 705  PRO A CA    1 
ATOM   5089  C C     . PRO A  1 707  ? -23.313 84.004  110.045 1.00 28.13 ? 705  PRO A C     1 
ATOM   5090  O O     . PRO A  1 707  ? -23.980 83.160  110.649 1.00 28.57 ? 705  PRO A O     1 
ATOM   5091  C CB    . PRO A  1 707  ? -21.169 83.507  108.828 1.00 24.81 ? 705  PRO A CB    1 
ATOM   5092  C CG    . PRO A  1 707  ? -21.227 82.016  109.031 1.00 28.93 ? 705  PRO A CG    1 
ATOM   5093  C CD    . PRO A  1 707  ? -21.022 81.773  110.517 1.00 27.16 ? 705  PRO A CD    1 
ATOM   5094  N N     . TRP A  1 708  ? -23.858 84.954  109.275 1.00 28.38 ? 706  TRP A N     1 
ATOM   5095  C CA    . TRP A  1 708  ? -25.304 85.055  109.092 1.00 27.42 ? 706  TRP A CA    1 
ATOM   5096  C C     . TRP A  1 708  ? -25.844 84.124  108.007 1.00 28.40 ? 706  TRP A C     1 
ATOM   5097  O O     . TRP A  1 708  ? -27.063 83.897  107.951 1.00 31.94 ? 706  TRP A O     1 
ATOM   5098  C CB    . TRP A  1 708  ? -25.703 86.504  108.760 1.00 30.79 ? 706  TRP A CB    1 
ATOM   5099  C CG    . TRP A  1 708  ? -24.889 87.100  107.647 1.00 31.27 ? 706  TRP A CG    1 
ATOM   5100  C CD1   . TRP A  1 708  ? -23.806 87.925  107.775 1.00 34.71 ? 706  TRP A CD1   1 
ATOM   5101  C CD2   . TRP A  1 708  ? -25.071 86.894  106.236 1.00 25.05 ? 706  TRP A CD2   1 
ATOM   5102  N NE1   . TRP A  1 708  ? -23.311 88.257  106.533 1.00 32.59 ? 706  TRP A NE1   1 
ATOM   5103  C CE2   . TRP A  1 708  ? -24.066 87.634  105.573 1.00 29.67 ? 706  TRP A CE2   1 
ATOM   5104  C CE3   . TRP A  1 708  ? -25.998 86.177  105.472 1.00 24.66 ? 706  TRP A CE3   1 
ATOM   5105  C CZ2   . TRP A  1 708  ? -23.947 87.660  104.183 1.00 29.80 ? 706  TRP A CZ2   1 
ATOM   5106  C CZ3   . TRP A  1 708  ? -25.881 86.197  104.085 1.00 31.39 ? 706  TRP A CZ3   1 
ATOM   5107  C CH2   . TRP A  1 708  ? -24.859 86.935  103.455 1.00 29.72 ? 706  TRP A CH2   1 
ATOM   5108  N N     . ASN A  1 709  ? -24.989 83.583  107.143 1.00 27.21 ? 707  ASN A N     1 
ATOM   5109  C CA    . ASN A  1 709  ? -25.496 82.837  105.992 1.00 29.94 ? 707  ASN A CA    1 
ATOM   5110  C C     . ASN A  1 709  ? -25.794 81.380  106.310 1.00 29.83 ? 707  ASN A C     1 
ATOM   5111  O O     . ASN A  1 709  ? -26.584 80.760  105.597 1.00 32.21 ? 707  ASN A O     1 
ATOM   5112  C CB    . ASN A  1 709  ? -24.514 82.922  104.817 1.00 30.13 ? 707  ASN A CB    1 
ATOM   5113  C CG    . ASN A  1 709  ? -23.175 82.258  105.117 1.00 33.37 ? 707  ASN A CG    1 
ATOM   5114  O OD1   . ASN A  1 709  ? -22.811 82.057  106.271 1.00 33.49 ? 707  ASN A OD1   1 
ATOM   5115  N ND2   . ASN A  1 709  ? -22.434 81.916  104.066 1.00 32.29 ? 707  ASN A ND2   1 
ATOM   5116  N N     . PHE A  1 710  ? -25.185 80.818  107.352 1.00 29.04 ? 708  PHE A N     1 
ATOM   5117  C CA    . PHE A  1 710  ? -25.594 79.531  107.909 1.00 28.63 ? 708  PHE A CA    1 
ATOM   5118  C C     . PHE A  1 710  ? -25.720 79.707  109.413 1.00 32.56 ? 708  PHE A C     1 
ATOM   5119  O O     . PHE A  1 710  ? -24.908 79.199  110.195 1.00 29.08 ? 708  PHE A O     1 
ATOM   5120  C CB    . PHE A  1 710  ? -24.629 78.405  107.548 1.00 30.27 ? 708  PHE A CB    1 
ATOM   5121  C CG    . PHE A  1 710  ? -24.735 77.981  106.120 1.00 32.50 ? 708  PHE A CG    1 
ATOM   5122  C CD1   . PHE A  1 710  ? -25.774 77.165  105.703 1.00 36.99 ? 708  PHE A CD1   1 
ATOM   5123  C CD2   . PHE A  1 710  ? -23.816 78.426  105.188 1.00 36.26 ? 708  PHE A CD2   1 
ATOM   5124  C CE1   . PHE A  1 710  ? -25.891 76.790  104.383 1.00 38.45 ? 708  PHE A CE1   1 
ATOM   5125  C CE2   . PHE A  1 710  ? -23.925 78.050  103.864 1.00 36.07 ? 708  PHE A CE2   1 
ATOM   5126  C CZ    . PHE A  1 710  ? -24.971 77.230  103.466 1.00 37.70 ? 708  PHE A CZ    1 
ATOM   5127  N N     . PRO A  1 711  ? -26.763 80.416  109.844 1.00 27.35 ? 709  PRO A N     1 
ATOM   5128  C CA    . PRO A  1 711  ? -26.834 80.891  111.227 1.00 26.83 ? 709  PRO A CA    1 
ATOM   5129  C C     . PRO A  1 711  ? -27.165 79.808  112.224 1.00 26.85 ? 709  PRO A C     1 
ATOM   5130  O O     . PRO A  1 711  ? -27.108 80.063  113.430 1.00 26.87 ? 709  PRO A O     1 
ATOM   5131  C CB    . PRO A  1 711  ? -27.950 81.935  111.165 1.00 24.91 ? 709  PRO A CB    1 
ATOM   5132  C CG    . PRO A  1 711  ? -28.871 81.413  110.095 1.00 25.82 ? 709  PRO A CG    1 
ATOM   5133  C CD    . PRO A  1 711  ? -27.955 80.794  109.059 1.00 26.91 ? 709  PRO A CD    1 
ATOM   5134  N N     . LEU A  1 712  ? -27.534 78.622  111.776 1.00 28.23 ? 710  LEU A N     1 
ATOM   5135  C CA    . LEU A  1 712  ? -27.697 77.502  112.686 1.00 26.44 ? 710  LEU A CA    1 
ATOM   5136  C C     . LEU A  1 712  ? -26.613 76.455  112.503 1.00 26.94 ? 710  LEU A C     1 
ATOM   5137  O O     . LEU A  1 712  ? -26.054 75.977  113.489 1.00 25.05 ? 710  LEU A O     1 
ATOM   5138  C CB    . LEU A  1 712  ? -29.084 76.861  112.509 1.00 23.65 ? 710  LEU A CB    1 
ATOM   5139  C CG    . LEU A  1 712  ? -29.282 75.625  113.394 1.00 28.21 ? 710  LEU A CG    1 
ATOM   5140  C CD1   . LEU A  1 712  ? -29.266 76.053  114.848 1.00 29.10 ? 710  LEU A CD1   1 
ATOM   5141  C CD2   . LEU A  1 712  ? -30.571 74.869  113.071 1.00 29.40 ? 710  LEU A CD2   1 
ATOM   5142  N N     . ALA A  1 713  ? -26.244 76.136  111.257 1.00 26.62 ? 711  ALA A N     1 
ATOM   5143  C CA    . ALA A  1 713  ? -25.382 74.985  111.030 1.00 24.23 ? 711  ALA A CA    1 
ATOM   5144  C C     . ALA A  1 713  ? -23.921 75.289  111.357 1.00 26.22 ? 711  ALA A C     1 
ATOM   5145  O O     . ALA A  1 713  ? -23.278 74.526  112.077 1.00 26.33 ? 711  ALA A O     1 
ATOM   5146  C CB    . ALA A  1 713  ? -25.526 74.507  109.584 1.00 24.37 ? 711  ALA A CB    1 
ATOM   5147  N N     . ILE A  1 714  ? -23.361 76.372  110.808 1.00 27.33 ? 712  ILE A N     1 
ATOM   5148  C CA    . ILE A  1 714  ? -21.970 76.694  111.131 1.00 25.31 ? 712  ILE A CA    1 
ATOM   5149  C C     . ILE A  1 714  ? -21.860 77.112  112.591 1.00 26.72 ? 712  ILE A C     1 
ATOM   5150  O O     . ILE A  1 714  ? -20.911 76.738  113.296 1.00 26.99 ? 712  ILE A O     1 
ATOM   5151  C CB    . ILE A  1 714  ? -21.433 77.771  110.170 1.00 27.93 ? 712  ILE A CB    1 
ATOM   5152  C CG1   . ILE A  1 714  ? -21.282 77.158  108.768 1.00 28.74 ? 712  ILE A CG1   1 
ATOM   5153  C CG2   . ILE A  1 714  ? -20.107 78.362  110.692 1.00 25.37 ? 712  ILE A CG2   1 
ATOM   5154  C CD1   . ILE A  1 714  ? -20.821 78.139  107.683 1.00 34.41 ? 712  ILE A CD1   1 
ATOM   5155  N N     . PHE A  1 715  ? -22.850 77.857  113.072 1.00 26.46 ? 713  PHE A N     1 
ATOM   5156  C CA    . PHE A  1 715  ? -22.945 78.182  114.492 1.00 29.63 ? 713  PHE A CA    1 
ATOM   5157  C C     . PHE A  1 715  ? -22.865 76.926  115.355 1.00 29.68 ? 713  PHE A C     1 
ATOM   5158  O O     . PHE A  1 715  ? -22.018 76.825  116.255 1.00 28.01 ? 713  PHE A O     1 
ATOM   5159  C CB    . PHE A  1 715  ? -24.254 78.933  114.737 1.00 27.77 ? 713  PHE A CB    1 
ATOM   5160  C CG    . PHE A  1 715  ? -24.561 79.174  116.186 1.00 29.02 ? 713  PHE A CG    1 
ATOM   5161  C CD1   . PHE A  1 715  ? -24.124 80.326  116.806 1.00 27.72 ? 713  PHE A CD1   1 
ATOM   5162  C CD2   . PHE A  1 715  ? -25.306 78.258  116.919 1.00 28.89 ? 713  PHE A CD2   1 
ATOM   5163  C CE1   . PHE A  1 715  ? -24.419 80.577  118.148 1.00 32.31 ? 713  PHE A CE1   1 
ATOM   5164  C CE2   . PHE A  1 715  ? -25.597 78.492  118.270 1.00 29.75 ? 713  PHE A CE2   1 
ATOM   5165  C CZ    . PHE A  1 715  ? -25.160 79.656  118.879 1.00 32.61 ? 713  PHE A CZ    1 
ATOM   5166  N N     . THR A  1 716  ? -23.733 75.951  115.069 1.00 26.72 ? 714  THR A N     1 
ATOM   5167  C CA    . THR A  1 716  ? -23.761 74.696  115.815 1.00 26.37 ? 714  THR A CA    1 
ATOM   5168  C C     . THR A  1 716  ? -22.459 73.919  115.658 1.00 27.56 ? 714  THR A C     1 
ATOM   5169  O O     . THR A  1 716  ? -21.904 73.420  116.640 1.00 26.49 ? 714  THR A O     1 
ATOM   5170  C CB    . THR A  1 716  ? -24.947 73.843  115.358 1.00 28.52 ? 714  THR A CB    1 
ATOM   5171  O OG1   . THR A  1 716  ? -26.169 74.517  115.684 1.00 29.90 ? 714  THR A OG1   1 
ATOM   5172  C CG2   . THR A  1 716  ? -24.940 72.470  116.027 1.00 28.07 ? 714  THR A CG2   1 
ATOM   5173  N N     . GLY A  1 717  ? -21.962 73.793  114.423 1.00 26.07 ? 715  GLY A N     1 
ATOM   5174  C CA    . GLY A  1 717  ? -20.778 72.974  114.199 1.00 24.62 ? 715  GLY A CA    1 
ATOM   5175  C C     . GLY A  1 717  ? -19.559 73.468  114.967 1.00 27.75 ? 715  GLY A C     1 
ATOM   5176  O O     . GLY A  1 717  ? -18.852 72.683  115.609 1.00 25.36 ? 715  GLY A O     1 
ATOM   5177  N N     . GLN A  1 718  ? -19.289 74.774  114.908 1.00 24.63 ? 716  GLN A N     1 
ATOM   5178  C CA    . GLN A  1 718  ? -18.130 75.297  115.625 1.00 25.12 ? 716  GLN A CA    1 
ATOM   5179  C C     . GLN A  1 718  ? -18.287 75.085  117.119 1.00 29.52 ? 716  GLN A C     1 
ATOM   5180  O O     . GLN A  1 718  ? -17.348 74.648  117.795 1.00 25.54 ? 716  GLN A O     1 
ATOM   5181  C CB    . GLN A  1 718  ? -17.920 76.782  115.323 1.00 24.88 ? 716  GLN A CB    1 
ATOM   5182  C CG    . GLN A  1 718  ? -17.609 77.106  113.839 1.00 23.77 ? 716  GLN A CG    1 
ATOM   5183  C CD    . GLN A  1 718  ? -17.321 78.598  113.633 1.00 30.06 ? 716  GLN A CD    1 
ATOM   5184  O OE1   . GLN A  1 718  ? -16.464 78.964  112.825 1.00 30.21 ? 716  GLN A OE1   1 
ATOM   5185  N NE2   . GLN A  1 718  ? -18.035 79.464  114.373 1.00 27.83 ? 716  GLN A NE2   1 
ATOM   5186  N N     . ILE A  1 719  ? -19.480 75.372  117.649 1.00 25.73 ? 717  ILE A N     1 
ATOM   5187  C CA    . ILE A  1 719  ? -19.688 75.268  119.092 1.00 29.15 ? 717  ILE A CA    1 
ATOM   5188  C C     . ILE A  1 719  ? -19.659 73.812  119.541 1.00 27.68 ? 717  ILE A C     1 
ATOM   5189  O O     . ILE A  1 719  ? -19.084 73.481  120.588 1.00 31.04 ? 717  ILE A O     1 
ATOM   5190  C CB    . ILE A  1 719  ? -21.003 75.968  119.469 1.00 28.64 ? 717  ILE A CB    1 
ATOM   5191  C CG1   . ILE A  1 719  ? -20.817 77.476  119.343 1.00 27.30 ? 717  ILE A CG1   1 
ATOM   5192  C CG2   . ILE A  1 719  ? -21.443 75.583  120.863 1.00 33.76 ? 717  ILE A CG2   1 
ATOM   5193  C CD1   . ILE A  1 719  ? -22.113 78.203  119.241 1.00 33.82 ? 717  ILE A CD1   1 
ATOM   5194  N N     . ALA A  1 720  ? -20.271 72.920  118.762 1.00 29.05 ? 718  ALA A N     1 
ATOM   5195  C CA    . ALA A  1 720  ? -20.309 71.509  119.143 1.00 27.25 ? 718  ALA A CA    1 
ATOM   5196  C C     . ALA A  1 720  ? -18.913 70.910  119.203 1.00 24.41 ? 718  ALA A C     1 
ATOM   5197  O O     . ALA A  1 720  ? -18.609 70.122  120.095 1.00 26.07 ? 718  ALA A O     1 
ATOM   5198  C CB    . ALA A  1 720  ? -21.168 70.718  118.161 1.00 24.38 ? 718  ALA A CB    1 
ATOM   5199  N N     . ALA A  1 721  ? -18.065 71.233  118.227 1.00 26.27 ? 719  ALA A N     1 
ATOM   5200  C CA    . ALA A  1 721  ? -16.715 70.685  118.216 1.00 22.69 ? 719  ALA A CA    1 
ATOM   5201  C C     . ALA A  1 721  ? -15.920 71.173  119.421 1.00 26.45 ? 719  ALA A C     1 
ATOM   5202  O O     . ALA A  1 721  ? -15.250 70.389  120.103 1.00 29.53 ? 719  ALA A O     1 
ATOM   5203  C CB    . ALA A  1 721  ? -16.014 71.076  116.916 1.00 24.34 ? 719  ALA A CB    1 
ATOM   5204  N N     . ALA A  1 722  ? -15.971 72.477  119.686 1.00 25.70 ? 720  ALA A N     1 
ATOM   5205  C CA    . ALA A  1 722  ? -15.228 73.029  120.812 1.00 26.48 ? 720  ALA A CA    1 
ATOM   5206  C C     . ALA A  1 722  ? -15.697 72.414  122.123 1.00 27.34 ? 720  ALA A C     1 
ATOM   5207  O O     . ALA A  1 722  ? -14.874 72.023  122.961 1.00 28.75 ? 720  ALA A O     1 
ATOM   5208  C CB    . ALA A  1 722  ? -15.373 74.548  120.841 1.00 24.75 ? 720  ALA A CB    1 
ATOM   5209  N N     . LEU A  1 723  ? -17.019 72.292  122.298 1.00 26.29 ? 721  LEU A N     1 
ATOM   5210  C CA    . LEU A  1 723  ? -17.581 71.746  123.529 1.00 26.76 ? 721  LEU A CA    1 
ATOM   5211  C C     . LEU A  1 723  ? -17.217 70.282  123.708 1.00 28.46 ? 721  LEU A C     1 
ATOM   5212  O O     . LEU A  1 723  ? -16.879 69.848  124.814 1.00 27.14 ? 721  LEU A O     1 
ATOM   5213  C CB    . LEU A  1 723  ? -19.100 71.886  123.522 1.00 27.65 ? 721  LEU A CB    1 
ATOM   5214  C CG    . LEU A  1 723  ? -19.708 73.262  123.736 1.00 28.39 ? 721  LEU A CG    1 
ATOM   5215  C CD1   . LEU A  1 723  ? -21.213 73.201  123.498 1.00 29.02 ? 721  LEU A CD1   1 
ATOM   5216  C CD2   . LEU A  1 723  ? -19.402 73.736  125.162 1.00 28.86 ? 721  LEU A CD2   1 
ATOM   5217  N N     . VAL A  1 724  ? -17.348 69.486  122.647 1.00 30.59 ? 722  VAL A N     1 
ATOM   5218  C CA    . VAL A  1 724  ? -17.136 68.059  122.837 1.00 27.43 ? 722  VAL A CA    1 
ATOM   5219  C C     . VAL A  1 724  ? -15.657 67.776  123.066 1.00 28.88 ? 722  VAL A C     1 
ATOM   5220  O O     . VAL A  1 724  ? -15.308 66.790  123.721 1.00 27.91 ? 722  VAL A O     1 
ATOM   5221  C CB    . VAL A  1 724  ? -17.720 67.265  121.650 1.00 24.63 ? 722  VAL A CB    1 
ATOM   5222  C CG1   . VAL A  1 724  ? -16.835 67.356  120.398 1.00 27.87 ? 722  VAL A CG1   1 
ATOM   5223  C CG2   . VAL A  1 724  ? -18.008 65.827  122.064 1.00 27.07 ? 722  VAL A CG2   1 
ATOM   5224  N N     . ALA A  1 725  ? -14.769 68.649  122.569 1.00 29.08 ? 723  ALA A N     1 
ATOM   5225  C CA    . ALA A  1 725  ? -13.337 68.560  122.867 1.00 29.05 ? 723  ALA A CA    1 
ATOM   5226  C C     . ALA A  1 725  ? -12.981 69.009  124.282 1.00 31.17 ? 723  ALA A C     1 
ATOM   5227  O O     . ALA A  1 725  ? -11.787 69.025  124.605 1.00 31.58 ? 723  ALA A O     1 
ATOM   5228  C CB    . ALA A  1 725  ? -12.529 69.393  121.872 1.00 27.55 ? 723  ALA A CB    1 
ATOM   5229  N N     . GLY A  1 726  ? -13.955 69.395  125.110 1.00 30.57 ? 724  GLY A N     1 
ATOM   5230  C CA    . GLY A  1 726  ? -13.704 69.762  126.488 1.00 31.03 ? 724  GLY A CA    1 
ATOM   5231  C C     . GLY A  1 726  ? -13.521 71.238  126.760 1.00 31.54 ? 724  GLY A C     1 
ATOM   5232  O O     . GLY A  1 726  ? -13.136 71.606  127.879 1.00 32.75 ? 724  GLY A O     1 
ATOM   5233  N N     . ASN A  1 727  ? -13.779 72.089  125.792 1.00 30.40 ? 725  ASN A N     1 
ATOM   5234  C CA    . ASN A  1 727  ? -13.585 73.517  125.965 1.00 31.80 ? 725  ASN A CA    1 
ATOM   5235  C C     . ASN A  1 727  ? -14.901 74.198  126.298 1.00 29.93 ? 725  ASN A C     1 
ATOM   5236  O O     . ASN A  1 727  ? -15.922 73.900  125.675 1.00 32.48 ? 725  ASN A O     1 
ATOM   5237  C CB    . ASN A  1 727  ? -13.026 74.135  124.681 1.00 29.55 ? 725  ASN A CB    1 
ATOM   5238  C CG    . ASN A  1 727  ? -11.762 73.463  124.232 1.00 27.65 ? 725  ASN A CG    1 
ATOM   5239  O OD1   . ASN A  1 727  ? -10.705 73.632  124.846 1.00 30.83 ? 725  ASN A OD1   1 
ATOM   5240  N ND2   . ASN A  1 727  ? -11.858 72.672  123.171 1.00 28.47 ? 725  ASN A ND2   1 
ATOM   5241  N N     . PRO A  1 728  ? -14.914 75.120  127.254 1.00 29.19 ? 726  PRO A N     1 
ATOM   5242  C CA    . PRO A  1 728  ? -16.061 76.017  127.376 1.00 29.62 ? 726  PRO A CA    1 
ATOM   5243  C C     . PRO A  1 728  ? -16.065 77.003  126.221 1.00 31.61 ? 726  PRO A C     1 
ATOM   5244  O O     . PRO A  1 728  ? -15.016 77.378  125.693 1.00 31.21 ? 726  PRO A O     1 
ATOM   5245  C CB    . PRO A  1 728  ? -15.832 76.720  128.722 1.00 30.77 ? 726  PRO A CB    1 
ATOM   5246  C CG    . PRO A  1 728  ? -14.334 76.703  128.903 1.00 30.89 ? 726  PRO A CG    1 
ATOM   5247  C CD    . PRO A  1 728  ? -13.792 75.510  128.130 1.00 31.12 ? 726  PRO A CD    1 
ATOM   5248  N N     . VAL A  1 729  ? -17.263 77.442  125.849 1.00 31.02 ? 727  VAL A N     1 
ATOM   5249  C CA    . VAL A  1 729  ? -17.477 78.192  124.620 1.00 31.40 ? 727  VAL A CA    1 
ATOM   5250  C C     . VAL A  1 729  ? -18.165 79.518  124.912 1.00 31.91 ? 727  VAL A C     1 
ATOM   5251  O O     . VAL A  1 729  ? -19.114 79.591  125.705 1.00 34.16 ? 727  VAL A O     1 
ATOM   5252  C CB    . VAL A  1 729  ? -18.302 77.372  123.606 1.00 29.47 ? 727  VAL A CB    1 
ATOM   5253  C CG1   . VAL A  1 729  ? -18.790 78.273  122.473 1.00 29.22 ? 727  VAL A CG1   1 
ATOM   5254  C CG2   . VAL A  1 729  ? -17.458 76.247  123.085 1.00 28.71 ? 727  VAL A CG2   1 
ATOM   5255  N N     . LEU A  1 730  ? -17.664 80.570  124.272 1.00 28.83 ? 728  LEU A N     1 
ATOM   5256  C CA    . LEU A  1 730  ? -18.339 81.857  124.186 1.00 29.29 ? 728  LEU A CA    1 
ATOM   5257  C C     . LEU A  1 730  ? -18.818 81.989  122.751 1.00 32.01 ? 728  LEU A C     1 
ATOM   5258  O O     . LEU A  1 730  ? -17.994 82.052  121.838 1.00 31.31 ? 728  LEU A O     1 
ATOM   5259  C CB    . LEU A  1 730  ? -17.410 83.018  124.538 1.00 30.04 ? 728  LEU A CB    1 
ATOM   5260  C CG    . LEU A  1 730  ? -16.602 83.067  125.848 1.00 32.57 ? 728  LEU A CG    1 
ATOM   5261  C CD1   . LEU A  1 730  ? -17.496 82.796  127.061 1.00 35.86 ? 728  LEU A CD1   1 
ATOM   5262  C CD2   . LEU A  1 730  ? -15.406 82.115  125.802 1.00 30.82 ? 728  LEU A CD2   1 
ATOM   5263  N N     . ALA A  1 731  ? -20.135 82.029  122.557 1.00 32.95 ? 729  ALA A N     1 
ATOM   5264  C CA    . ALA A  1 731  ? -20.750 81.986  121.234 1.00 32.17 ? 729  ALA A CA    1 
ATOM   5265  C C     . ALA A  1 731  ? -21.167 83.393  120.817 1.00 30.18 ? 729  ALA A C     1 
ATOM   5266  O O     . ALA A  1 731  ? -22.086 83.972  121.401 1.00 37.22 ? 729  ALA A O     1 
ATOM   5267  C CB    . ALA A  1 731  ? -21.956 81.047  121.234 1.00 32.44 ? 729  ALA A CB    1 
ATOM   5268  N N     . LYS A  1 732  ? -20.499 83.938  119.804 1.00 34.09 ? 730  LYS A N     1 
ATOM   5269  C CA    . LYS A  1 732  ? -20.834 85.265  119.295 1.00 32.89 ? 730  LYS A CA    1 
ATOM   5270  C C     . LYS A  1 732  ? -21.512 85.090  117.945 1.00 31.94 ? 730  LYS A C     1 
ATOM   5271  O O     . LYS A  1 732  ? -20.820 84.937  116.925 1.00 27.95 ? 730  LYS A O     1 
ATOM   5272  C CB    . LYS A  1 732  ? -19.580 86.135  119.158 1.00 32.72 ? 730  LYS A CB    1 
ATOM   5273  C CG    . LYS A  1 732  ? -19.777 87.615  119.494 1.00 37.77 ? 730  LYS A CG    1 
ATOM   5274  C CD    . LYS A  1 732  ? -20.783 88.295  118.556 1.00 35.73 ? 730  LYS A CD    1 
ATOM   5275  C CE    . LYS A  1 732  ? -20.245 88.387  117.130 1.00 39.76 ? 730  LYS A CE    1 
ATOM   5276  N NZ    . LYS A  1 732  ? -21.109 89.248  116.266 1.00 39.16 ? 730  LYS A NZ    1 
ATOM   5277  N N     . PRO A  1 733  ? -22.845 85.103  117.877 1.00 28.72 ? 731  PRO A N     1 
ATOM   5278  C CA    . PRO A  1 733  ? -23.518 84.924  116.591 1.00 29.41 ? 731  PRO A CA    1 
ATOM   5279  C C     . PRO A  1 733  ? -23.471 86.199  115.769 1.00 29.84 ? 731  PRO A C     1 
ATOM   5280  O O     . PRO A  1 733  ? -23.267 87.297  116.288 1.00 32.58 ? 731  PRO A O     1 
ATOM   5281  C CB    . PRO A  1 733  ? -24.959 84.581  116.981 1.00 28.33 ? 731  PRO A CB    1 
ATOM   5282  C CG    . PRO A  1 733  ? -25.175 85.306  118.276 1.00 28.59 ? 731  PRO A CG    1 
ATOM   5283  C CD    . PRO A  1 733  ? -23.806 85.286  118.983 1.00 30.97 ? 731  PRO A CD    1 
ATOM   5284  N N     . ALA A  1 734  ? -23.662 86.034  114.459 1.00 28.30 ? 732  ALA A N     1 
ATOM   5285  C CA    . ALA A  1 734  ? -23.732 87.203  113.597 1.00 32.42 ? 732  ALA A CA    1 
ATOM   5286  C C     . ALA A  1 734  ? -24.815 88.155  114.092 1.00 33.95 ? 732  ALA A C     1 
ATOM   5287  O O     . ALA A  1 734  ? -25.854 87.741  114.614 1.00 32.11 ? 732  ALA A O     1 
ATOM   5288  C CB    . ALA A  1 734  ? -24.007 86.800  112.146 1.00 28.22 ? 732  ALA A CB    1 
ATOM   5289  N N     . GLU A  1 735  ? -24.549 89.450  113.932 1.00 35.21 ? 733  GLU A N     1 
ATOM   5290  C CA    . GLU A  1 735  ? -25.485 90.470  114.389 1.00 35.22 ? 733  GLU A CA    1 
ATOM   5291  C C     . GLU A  1 735  ? -26.837 90.352  113.691 1.00 35.70 ? 733  GLU A C     1 
ATOM   5292  O O     . GLU A  1 735  ? -27.869 90.706  114.267 1.00 31.77 ? 733  GLU A O     1 
ATOM   5293  C CB    . GLU A  1 735  ? -24.868 91.849  114.159 1.00 39.75 ? 733  GLU A CB    1 
ATOM   5294  C CG    . GLU A  1 735  ? -25.667 93.020  114.691 1.00 49.47 ? 733  GLU A CG    1 
ATOM   5295  C CD    . GLU A  1 735  ? -24.990 94.349  114.393 1.00 52.41 ? 733  GLU A CD    1 
ATOM   5296  O OE1   . GLU A  1 735  ? -23.868 94.332  113.828 1.00 54.65 ? 733  GLU A OE1   1 
ATOM   5297  O OE2   . GLU A  1 735  ? -25.580 95.402  114.720 1.00 56.61 ? 733  GLU A OE2   1 
ATOM   5298  N N     . GLU A  1 736  ? -26.859 89.829  112.468 1.00 32.26 ? 734  GLU A N     1 
ATOM   5299  C CA    . GLU A  1 736  ? -28.102 89.754  111.716 1.00 31.02 ? 734  GLU A CA    1 
ATOM   5300  C C     . GLU A  1 736  ? -28.998 88.590  112.132 1.00 30.04 ? 734  GLU A C     1 
ATOM   5301  O O     . GLU A  1 736  ? -30.203 88.635  111.861 1.00 33.39 ? 734  GLU A O     1 
ATOM   5302  C CB    . GLU A  1 736  ? -27.792 89.652  110.218 1.00 33.75 ? 734  GLU A CB    1 
ATOM   5303  C CG    . GLU A  1 736  ? -27.078 90.873  109.645 1.00 36.18 ? 734  GLU A CG    1 
ATOM   5304  C CD    . GLU A  1 736  ? -25.549 90.726  109.611 1.00 40.61 ? 734  GLU A CD    1 
ATOM   5305  O OE1   . GLU A  1 736  ? -24.978 89.960  110.432 1.00 33.05 ? 734  GLU A OE1   1 
ATOM   5306  O OE2   . GLU A  1 736  ? -24.920 91.386  108.749 1.00 41.11 ? 734  GLU A OE2   1 
ATOM   5307  N N     . THR A  1 737  ? -28.462 87.545  112.770 1.00 31.92 ? 735  THR A N     1 
ATOM   5308  C CA    . THR A  1 737  ? -29.223 86.310  112.997 1.00 31.58 ? 735  THR A CA    1 
ATOM   5309  C C     . THR A  1 737  ? -29.006 85.757  114.403 1.00 30.39 ? 735  THR A C     1 
ATOM   5310  O O     . THR A  1 737  ? -28.640 84.591  114.570 1.00 31.85 ? 735  THR A O     1 
ATOM   5311  C CB    . THR A  1 737  ? -28.852 85.249  111.958 1.00 30.44 ? 735  THR A CB    1 
ATOM   5312  O OG1   . THR A  1 737  ? -27.441 84.977  112.038 1.00 29.32 ? 735  THR A OG1   1 
ATOM   5313  C CG2   . THR A  1 737  ? -29.209 85.712  110.544 1.00 28.64 ? 735  THR A CG2   1 
ATOM   5314  N N     . PRO A  1 738  ? -29.267 86.561  115.446 1.00 32.95 ? 736  PRO A N     1 
ATOM   5315  C CA    . PRO A  1 738  ? -29.090 86.059  116.820 1.00 33.21 ? 736  PRO A CA    1 
ATOM   5316  C C     . PRO A  1 738  ? -30.194 85.125  117.293 1.00 33.05 ? 736  PRO A C     1 
ATOM   5317  O O     . PRO A  1 738  ? -29.965 84.364  118.247 1.00 29.35 ? 736  PRO A O     1 
ATOM   5318  C CB    . PRO A  1 738  ? -29.095 87.344  117.658 1.00 33.39 ? 736  PRO A CB    1 
ATOM   5319  C CG    . PRO A  1 738  ? -30.090 88.202  116.924 1.00 30.77 ? 736  PRO A CG    1 
ATOM   5320  C CD    . PRO A  1 738  ? -29.849 87.919  115.442 1.00 32.05 ? 736  PRO A CD    1 
ATOM   5321  N N     . LEU A  1 739  ? -31.380 85.163  116.672 1.00 27.83 ? 737  LEU A N     1 
ATOM   5322  C CA    . LEU A  1 739  ? -32.517 84.417  117.213 1.00 30.70 ? 737  LEU A CA    1 
ATOM   5323  C C     . LEU A  1 739  ? -32.312 82.914  117.083 1.00 28.79 ? 737  LEU A C     1 
ATOM   5324  O O     . LEU A  1 739  ? -32.487 82.173  118.053 1.00 28.37 ? 737  LEU A O     1 
ATOM   5325  C CB    . LEU A  1 739  ? -33.812 84.844  116.523 1.00 30.42 ? 737  LEU A CB    1 
ATOM   5326  C CG    . LEU A  1 739  ? -34.243 86.296  116.714 1.00 33.97 ? 737  LEU A CG    1 
ATOM   5327  C CD1   . LEU A  1 739  ? -35.514 86.569  115.939 1.00 35.56 ? 737  LEU A CD1   1 
ATOM   5328  C CD2   . LEU A  1 739  ? -34.442 86.654  118.209 1.00 30.12 ? 737  LEU A CD2   1 
ATOM   5329  N N     . ILE A  1 740  ? -31.952 82.438  115.888 1.00 26.51 ? 738  ILE A N     1 
ATOM   5330  C CA    . ILE A  1 740  ? -31.723 81.007  115.731 1.00 30.41 ? 738  ILE A CA    1 
ATOM   5331  C C     . ILE A  1 740  ? -30.514 80.583  116.556 1.00 29.62 ? 738  ILE A C     1 
ATOM   5332  O O     . ILE A  1 740  ? -30.450 79.446  117.038 1.00 30.59 ? 738  ILE A O     1 
ATOM   5333  C CB    . ILE A  1 740  ? -31.586 80.641  114.234 1.00 31.87 ? 738  ILE A CB    1 
ATOM   5334  C CG1   . ILE A  1 740  ? -31.534 79.118  114.027 1.00 31.36 ? 738  ILE A CG1   1 
ATOM   5335  C CG2   . ILE A  1 740  ? -30.368 81.298  113.607 1.00 30.84 ? 738  ILE A CG2   1 
ATOM   5336  C CD1   . ILE A  1 740  ? -32.818 78.399  114.476 1.00 31.54 ? 738  ILE A CD1   1 
ATOM   5337  N N     . ALA A  1 741  ? -29.566 81.495  116.785 1.00 31.80 ? 739  ALA A N     1 
ATOM   5338  C CA    . ALA A  1 741  ? -28.433 81.161  117.639 1.00 30.81 ? 739  ALA A CA    1 
ATOM   5339  C C     . ALA A  1 741  ? -28.901 80.920  119.062 1.00 31.04 ? 739  ALA A C     1 
ATOM   5340  O O     . ALA A  1 741  ? -28.516 79.931  119.694 1.00 28.08 ? 739  ALA A O     1 
ATOM   5341  C CB    . ALA A  1 741  ? -27.391 82.273  117.607 1.00 31.72 ? 739  ALA A CB    1 
ATOM   5342  N N     . ALA A  1 742  ? -29.757 81.812  119.566 1.00 28.95 ? 740  ALA A N     1 
ATOM   5343  C CA    . ALA A  1 742  ? -30.256 81.676  120.927 1.00 31.76 ? 740  ALA A CA    1 
ATOM   5344  C C     . ALA A  1 742  ? -31.024 80.376  121.095 1.00 32.79 ? 740  ALA A C     1 
ATOM   5345  O O     . ALA A  1 742  ? -30.888 79.694  122.116 1.00 33.56 ? 740  ALA A O     1 
ATOM   5346  C CB    . ALA A  1 742  ? -31.140 82.873  121.285 1.00 31.89 ? 740  ALA A CB    1 
ATOM   5347  N N     . GLU A  1 743  ? -31.838 80.023  120.098 1.00 32.08 ? 741  GLU A N     1 
ATOM   5348  C CA    . GLU A  1 743  ? -32.566 78.759  120.133 1.00 33.26 ? 741  GLU A CA    1 
ATOM   5349  C C     . GLU A  1 743  ? -31.609 77.571  120.098 1.00 32.51 ? 741  GLU A C     1 
ATOM   5350  O O     . GLU A  1 743  ? -31.832 76.559  120.778 1.00 29.44 ? 741  GLU A O     1 
ATOM   5351  C CB    . GLU A  1 743  ? -33.553 78.702  118.965 1.00 34.08 ? 741  GLU A CB    1 
ATOM   5352  C CG    . GLU A  1 743  ? -34.282 77.378  118.809 1.00 33.73 ? 741  GLU A CG    1 
ATOM   5353  C CD    . GLU A  1 743  ? -35.197 77.050  119.975 1.00 37.44 ? 741  GLU A CD    1 
ATOM   5354  O OE1   . GLU A  1 743  ? -35.361 77.890  120.890 1.00 38.21 ? 741  GLU A OE1   1 
ATOM   5355  O OE2   . GLU A  1 743  ? -35.740 75.927  119.986 1.00 41.62 ? 741  GLU A OE2   1 
ATOM   5356  N N     . GLY A  1 744  ? -30.537 77.676  119.310 1.00 30.83 ? 742  GLY A N     1 
ATOM   5357  C CA    . GLY A  1 744  ? -29.526 76.628  119.309 1.00 29.43 ? 742  GLY A CA    1 
ATOM   5358  C C     . GLY A  1 744  ? -28.902 76.420  120.678 1.00 30.20 ? 742  GLY A C     1 
ATOM   5359  O O     . GLY A  1 744  ? -28.750 75.285  121.139 1.00 31.87 ? 742  GLY A O     1 
ATOM   5360  N N     . VAL A  1 745  ? -28.525 77.517  121.346 1.00 27.72 ? 743  VAL A N     1 
ATOM   5361  C CA    . VAL A  1 745  ? -27.964 77.412  122.692 1.00 28.57 ? 743  VAL A CA    1 
ATOM   5362  C C     . VAL A  1 745  ? -28.990 76.820  123.651 1.00 32.03 ? 743  VAL A C     1 
ATOM   5363  O O     . VAL A  1 745  ? -28.653 76.009  124.524 1.00 32.47 ? 743  VAL A O     1 
ATOM   5364  C CB    . VAL A  1 745  ? -27.465 78.790  123.173 1.00 29.13 ? 743  VAL A CB    1 
ATOM   5365  C CG1   . VAL A  1 745  ? -27.241 78.796  124.694 1.00 34.06 ? 743  VAL A CG1   1 
ATOM   5366  C CG2   . VAL A  1 745  ? -26.183 79.170  122.408 1.00 29.08 ? 743  VAL A CG2   1 
ATOM   5367  N N     . ARG A  1 746  ? -30.258 77.224  123.514 1.00 33.70 ? 744  ARG A N     1 
ATOM   5368  C CA    . ARG A  1 746  ? -31.291 76.670  124.384 1.00 32.65 ? 744  ARG A CA    1 
ATOM   5369  C C     . ARG A  1 746  ? -31.341 75.152  124.269 1.00 33.13 ? 744  ARG A C     1 
ATOM   5370  O O     . ARG A  1 746  ? -31.394 74.446  125.283 1.00 33.43 ? 744  ARG A O     1 
ATOM   5371  C CB    . ARG A  1 746  ? -32.657 77.272  124.048 1.00 33.78 ? 744  ARG A CB    1 
ATOM   5372  C CG    . ARG A  1 746  ? -33.710 76.926  125.086 1.00 34.45 ? 744  ARG A CG    1 
ATOM   5373  C CD    . ARG A  1 746  ? -35.123 77.190  124.592 1.00 35.40 ? 744  ARG A CD    1 
ATOM   5374  N NE    . ARG A  1 746  ? -35.442 76.350  123.444 1.00 41.07 ? 744  ARG A NE    1 
ATOM   5375  C CZ    . ARG A  1 746  ? -35.829 75.085  123.536 1.00 41.95 ? 744  ARG A CZ    1 
ATOM   5376  N NH1   . ARG A  1 746  ? -35.943 74.482  124.713 1.00 40.04 ? 744  ARG A NH1   1 
ATOM   5377  N NH2   . ARG A  1 746  ? -36.123 74.414  122.424 1.00 39.55 ? 744  ARG A NH2   1 
ATOM   5378  N N     . ILE A  1 747  ? -31.277 74.638  123.038 1.00 31.42 ? 745  ILE A N     1 
ATOM   5379  C CA    . ILE A  1 747  ? -31.319 73.198  122.796 1.00 33.38 ? 745  ILE A CA    1 
ATOM   5380  C C     . ILE A  1 747  ? -30.075 72.510  123.343 1.00 31.49 ? 745  ILE A C     1 
ATOM   5381  O O     . ILE A  1 747  ? -30.166 71.443  123.966 1.00 30.64 ? 745  ILE A O     1 
ATOM   5382  C CB    . ILE A  1 747  ? -31.496 72.941  121.291 1.00 30.05 ? 745  ILE A CB    1 
ATOM   5383  C CG1   . ILE A  1 747  ? -32.913 73.337  120.884 1.00 34.46 ? 745  ILE A CG1   1 
ATOM   5384  C CG2   . ILE A  1 747  ? -31.161 71.495  120.950 1.00 29.71 ? 745  ILE A CG2   1 
ATOM   5385  C CD1   . ILE A  1 747  ? -33.098 73.557  119.399 1.00 31.78 ? 745  ILE A CD1   1 
ATOM   5386  N N     . LEU A  1 748  ? -28.892 73.096  123.114 1.00 32.09 ? 746  LEU A N     1 
ATOM   5387  C CA    . LEU A  1 748  ? -27.666 72.523  123.672 1.00 31.03 ? 746  LEU A CA    1 
ATOM   5388  C C     . LEU A  1 748  ? -27.715 72.484  125.192 1.00 31.89 ? 746  LEU A C     1 
ATOM   5389  O O     . LEU A  1 748  ? -27.317 71.489  125.806 1.00 31.55 ? 746  LEU A O     1 
ATOM   5390  C CB    . LEU A  1 748  ? -26.443 73.314  123.205 1.00 28.21 ? 746  LEU A CB    1 
ATOM   5391  C CG    . LEU A  1 748  ? -25.987 72.947  121.788 1.00 31.66 ? 746  LEU A CG    1 
ATOM   5392  C CD1   . LEU A  1 748  ? -24.964 73.951  121.271 1.00 31.75 ? 746  LEU A CD1   1 
ATOM   5393  C CD2   . LEU A  1 748  ? -25.408 71.544  121.761 1.00 28.87 ? 746  LEU A CD2   1 
ATOM   5394  N N     . ARG A  1 749  ? -28.184 73.559  125.821 1.00 31.60 ? 747  ARG A N     1 
ATOM   5395  C CA    . ARG A  1 749  ? -28.279 73.548  127.279 1.00 34.03 ? 747  ARG A CA    1 
ATOM   5396  C C     . ARG A  1 749  ? -29.304 72.525  127.756 1.00 35.22 ? 747  ARG A C     1 
ATOM   5397  O O     . ARG A  1 749  ? -29.072 71.819  128.746 1.00 35.77 ? 747  ARG A O     1 
ATOM   5398  C CB    . ARG A  1 749  ? -28.620 74.946  127.797 1.00 36.88 ? 747  ARG A CB    1 
ATOM   5399  C CG    . ARG A  1 749  ? -27.392 75.858  127.907 1.00 39.31 ? 747  ARG A CG    1 
ATOM   5400  C CD    . ARG A  1 749  ? -27.811 77.279  128.200 1.00 44.75 ? 747  ARG A CD    1 
ATOM   5401  N NE    . ARG A  1 749  ? -26.676 78.163  128.439 1.00 41.50 ? 747  ARG A NE    1 
ATOM   5402  C CZ    . ARG A  1 749  ? -26.763 79.278  129.149 1.00 43.40 ? 747  ARG A CZ    1 
ATOM   5403  N NH1   . ARG A  1 749  ? -27.912 79.669  129.673 1.00 44.00 ? 747  ARG A NH1   1 
ATOM   5404  N NH2   . ARG A  1 749  ? -25.671 80.013  129.350 1.00 39.41 ? 747  ARG A NH2   1 
ATOM   5405  N N     . GLU A  1 750  ? -30.447 72.439  127.077 1.00 31.89 ? 748  GLU A N     1 
ATOM   5406  C CA    . GLU A  1 750  ? -31.422 71.404  127.415 1.00 33.79 ? 748  GLU A CA    1 
ATOM   5407  C C     . GLU A  1 750  ? -30.806 70.016  127.291 1.00 34.93 ? 748  GLU A C     1 
ATOM   5408  O O     . GLU A  1 750  ? -31.097 69.124  128.094 1.00 37.85 ? 748  GLU A O     1 
ATOM   5409  C CB    . GLU A  1 750  ? -32.658 71.515  126.522 1.00 37.33 ? 748  GLU A CB    1 
ATOM   5410  C CG    . GLU A  1 750  ? -33.753 70.522  126.906 1.00 42.48 ? 748  GLU A CG    1 
ATOM   5411  C CD    . GLU A  1 750  ? -34.984 70.590  126.009 1.00 47.99 ? 748  GLU A CD    1 
ATOM   5412  O OE1   . GLU A  1 750  ? -35.231 71.646  125.386 1.00 47.89 ? 748  GLU A OE1   1 
ATOM   5413  O OE2   . GLU A  1 750  ? -35.701 69.572  125.917 1.00 51.62 ? 748  GLU A OE2   1 
ATOM   5414  N N     . ALA A  1 751  ? -29.929 69.824  126.309 1.00 31.48 ? 749  ALA A N     1 
ATOM   5415  C CA    . ALA A  1 751  ? -29.305 68.525  126.111 1.00 31.25 ? 749  ALA A CA    1 
ATOM   5416  C C     . ALA A  1 751  ? -28.256 68.224  127.165 1.00 32.13 ? 749  ALA A C     1 
ATOM   5417  O O     . ALA A  1 751  ? -27.733 67.108  127.195 1.00 35.39 ? 749  ALA A O     1 
ATOM   5418  C CB    . ALA A  1 751  ? -28.686 68.450  124.710 1.00 29.71 ? 749  ALA A CB    1 
ATOM   5419  N N     . GLY A  1 752  ? -27.936 69.183  128.026 1.00 34.57 ? 750  GLY A N     1 
ATOM   5420  C CA    . GLY A  1 752  ? -27.066 68.929  129.159 1.00 35.95 ? 750  GLY A CA    1 
ATOM   5421  C C     . GLY A  1 752  ? -25.809 69.770  129.206 1.00 33.31 ? 750  GLY A C     1 
ATOM   5422  O O     . GLY A  1 752  ? -25.055 69.661  130.180 1.00 33.26 ? 750  GLY A O     1 
ATOM   5423  N N     . ILE A  1 753  ? -25.525 70.594  128.204 1.00 35.33 ? 751  ILE A N     1 
ATOM   5424  C CA    . ILE A  1 753  ? -24.361 71.471  128.262 1.00 34.31 ? 751  ILE A CA    1 
ATOM   5425  C C     . ILE A  1 753  ? -24.610 72.482  129.373 1.00 33.94 ? 751  ILE A C     1 
ATOM   5426  O O     . ILE A  1 753  ? -25.578 73.252  129.291 1.00 34.90 ? 751  ILE A O     1 
ATOM   5427  C CB    . ILE A  1 753  ? -24.113 72.171  126.919 1.00 33.07 ? 751  ILE A CB    1 
ATOM   5428  C CG1   . ILE A  1 753  ? -23.938 71.136  125.811 1.00 29.76 ? 751  ILE A CG1   1 
ATOM   5429  C CG2   . ILE A  1 753  ? -22.899 73.075  127.024 1.00 37.21 ? 751  ILE A CG2   1 
ATOM   5430  C CD1   . ILE A  1 753  ? -22.682 70.299  125.947 1.00 31.21 ? 751  ILE A CD1   1 
ATOM   5431  N N     . PRO A  1 754  ? -23.781 72.513  130.423 1.00 34.81 ? 752  PRO A N     1 
ATOM   5432  C CA    . PRO A  1 754  ? -24.011 73.472  131.509 1.00 40.07 ? 752  PRO A CA    1 
ATOM   5433  C C     . PRO A  1 754  ? -23.883 74.908  131.015 1.00 39.32 ? 752  PRO A C     1 
ATOM   5434  O O     . PRO A  1 754  ? -23.149 75.205  130.068 1.00 35.40 ? 752  PRO A O     1 
ATOM   5435  C CB    . PRO A  1 754  ? -22.919 73.130  132.537 1.00 41.52 ? 752  PRO A CB    1 
ATOM   5436  C CG    . PRO A  1 754  ? -22.309 71.804  132.088 1.00 37.82 ? 752  PRO A CG    1 
ATOM   5437  C CD    . PRO A  1 754  ? -22.557 71.712  130.614 1.00 33.23 ? 752  PRO A CD    1 
ATOM   5438  N N     . ALA A  1 755  ? -24.614 75.805  131.682 1.00 36.97 ? 753  ALA A N     1 
ATOM   5439  C CA    . ALA A  1 755  ? -24.609 77.217  131.307 1.00 38.00 ? 753  ALA A CA    1 
ATOM   5440  C C     . ALA A  1 755  ? -23.207 77.823  131.374 1.00 39.04 ? 753  ALA A C     1 
ATOM   5441  O O     . ALA A  1 755  ? -22.887 78.737  130.605 1.00 40.47 ? 753  ALA A O     1 
ATOM   5442  C CB    . ALA A  1 755  ? -25.565 77.999  132.219 1.00 43.70 ? 753  ALA A CB    1 
ATOM   5443  N N     . SER A  1 756  ? -22.359 77.338  132.278 1.00 34.95 ? 754  SER A N     1 
ATOM   5444  C CA    . SER A  1 756  ? -20.999 77.859  132.340 1.00 39.82 ? 754  SER A CA    1 
ATOM   5445  C C     . SER A  1 756  ? -20.141 77.367  131.183 1.00 37.31 ? 754  SER A C     1 
ATOM   5446  O O     . SER A  1 756  ? -19.120 77.992  130.876 1.00 39.89 ? 754  SER A O     1 
ATOM   5447  C CB    . SER A  1 756  ? -20.350 77.481  133.667 1.00 44.18 ? 754  SER A CB    1 
ATOM   5448  O OG    . SER A  1 756  ? -20.250 76.075  133.808 1.00 39.99 ? 754  SER A OG    1 
ATOM   5449  N N     . ALA A  1 757  ? -20.530 76.269  130.539 1.00 37.07 ? 755  ALA A N     1 
ATOM   5450  C CA    . ALA A  1 757  ? -19.798 75.748  129.396 1.00 32.66 ? 755  ALA A CA    1 
ATOM   5451  C C     . ALA A  1 757  ? -20.210 76.383  128.074 1.00 33.62 ? 755  ALA A C     1 
ATOM   5452  O O     . ALA A  1 757  ? -19.474 76.250  127.094 1.00 33.07 ? 755  ALA A O     1 
ATOM   5453  C CB    . ALA A  1 757  ? -19.980 74.228  129.294 1.00 33.34 ? 755  ALA A CB    1 
ATOM   5454  N N     . LEU A  1 758  ? -21.350 77.077  128.025 1.00 33.65 ? 756  LEU A N     1 
ATOM   5455  C CA    . LEU A  1 758  ? -21.854 77.614  126.763 1.00 36.54 ? 756  LEU A CA    1 
ATOM   5456  C C     . LEU A  1 758  ? -22.603 78.910  127.050 1.00 35.99 ? 756  LEU A C     1 
ATOM   5457  O O     . LEU A  1 758  ? -23.744 78.883  127.530 1.00 33.96 ? 756  LEU A O     1 
ATOM   5458  C CB    . LEU A  1 758  ? -22.744 76.605  126.062 1.00 33.15 ? 756  LEU A CB    1 
ATOM   5459  C CG    . LEU A  1 758  ? -23.442 77.165  124.837 1.00 33.45 ? 756  LEU A CG    1 
ATOM   5460  C CD1   . LEU A  1 758  ? -22.403 77.602  123.802 1.00 32.86 ? 756  LEU A CD1   1 
ATOM   5461  C CD2   . LEU A  1 758  ? -24.343 76.098  124.290 1.00 35.03 ? 756  LEU A CD2   1 
ATOM   5462  N N     . GLN A  1 759  ? -21.960 80.030  126.732 1.00 31.21 ? 757  GLN A N     1 
ATOM   5463  C CA    . GLN A  1 759  ? -22.511 81.360  126.936 1.00 36.34 ? 757  GLN A CA    1 
ATOM   5464  C C     . GLN A  1 759  ? -22.794 82.007  125.584 1.00 35.17 ? 757  GLN A C     1 
ATOM   5465  O O     . GLN A  1 759  ? -21.960 81.949  124.671 1.00 33.88 ? 757  GLN A O     1 
ATOM   5466  C CB    . GLN A  1 759  ? -21.550 82.218  127.763 1.00 37.44 ? 757  GLN A CB    1 
ATOM   5467  C CG    . GLN A  1 759  ? -21.371 81.727  129.201 1.00 33.49 ? 757  GLN A CG    1 
ATOM   5468  C CD    . GLN A  1 759  ? -20.337 82.531  129.972 1.00 36.50 ? 757  GLN A CD    1 
ATOM   5469  O OE1   . GLN A  1 759  ? -20.678 83.479  130.678 1.00 35.82 ? 757  GLN A OE1   1 
ATOM   5470  N NE2   . GLN A  1 759  ? -19.064 82.155  129.832 1.00 33.75 ? 757  GLN A NE2   1 
ATOM   5471  N N     . LEU A  1 760  ? -23.968 82.617  125.457 1.00 38.65 ? 758  LEU A N     1 
ATOM   5472  C CA    . LEU A  1 760  ? -24.357 83.303  124.232 1.00 35.65 ? 758  LEU A CA    1 
ATOM   5473  C C     . LEU A  1 760  ? -24.138 84.794  124.425 1.00 34.34 ? 758  LEU A C     1 
ATOM   5474  O O     . LEU A  1 760  ? -24.581 85.362  125.423 1.00 38.23 ? 758  LEU A O     1 
ATOM   5475  C CB    . LEU A  1 760  ? -25.815 83.021  123.871 1.00 33.49 ? 758  LEU A CB    1 
ATOM   5476  C CG    . LEU A  1 760  ? -26.308 83.677  122.576 1.00 33.38 ? 758  LEU A CG    1 
ATOM   5477  C CD1   . LEU A  1 760  ? -25.943 82.845  121.337 1.00 31.33 ? 758  LEU A CD1   1 
ATOM   5478  C CD2   . LEU A  1 760  ? -27.797 83.906  122.630 1.00 35.00 ? 758  LEU A CD2   1 
ATOM   5479  N N     . LEU A  1 761  ? -23.446 85.422  123.479 1.00 33.05 ? 759  LEU A N     1 
ATOM   5480  C CA    . LEU A  1 761  ? -23.123 86.845  123.551 1.00 35.17 ? 759  LEU A CA    1 
ATOM   5481  C C     . LEU A  1 761  ? -23.502 87.496  122.229 1.00 34.54 ? 759  LEU A C     1 
ATOM   5482  O O     . LEU A  1 761  ? -22.643 87.695  121.364 1.00 35.49 ? 759  LEU A O     1 
ATOM   5483  C CB    . LEU A  1 761  ? -21.640 87.081  123.849 1.00 32.90 ? 759  LEU A CB    1 
ATOM   5484  C CG    . LEU A  1 761  ? -20.984 86.626  125.157 1.00 39.45 ? 759  LEU A CG    1 
ATOM   5485  C CD1   . LEU A  1 761  ? -21.835 86.947  126.382 1.00 37.96 ? 759  LEU A CD1   1 
ATOM   5486  C CD2   . LEU A  1 761  ? -20.582 85.153  125.102 1.00 37.44 ? 759  LEU A CD2   1 
ATOM   5487  N N     . PRO A  1 762  ? -24.771 87.864  122.051 1.00 36.11 ? 760  PRO A N     1 
ATOM   5488  C CA    . PRO A  1 762  ? -25.176 88.578  120.830 1.00 38.38 ? 760  PRO A CA    1 
ATOM   5489  C C     . PRO A  1 762  ? -24.561 89.972  120.757 1.00 41.03 ? 760  PRO A C     1 
ATOM   5490  O O     . PRO A  1 762  ? -24.260 90.597  121.777 1.00 39.07 ? 760  PRO A O     1 
ATOM   5491  C CB    . PRO A  1 762  ? -26.705 88.661  120.953 1.00 38.09 ? 760  PRO A CB    1 
ATOM   5492  C CG    . PRO A  1 762  ? -27.078 87.724  122.085 1.00 35.47 ? 760  PRO A CG    1 
ATOM   5493  C CD    . PRO A  1 762  ? -25.887 87.686  122.993 1.00 34.25 ? 760  PRO A CD    1 
ATOM   5494  N N     . GLY A  1 763  ? -24.371 90.457  119.540 1.00 35.05 ? 761  GLY A N     1 
ATOM   5495  C CA    . GLY A  1 763  ? -23.813 91.782  119.347 1.00 41.87 ? 761  GLY A CA    1 
ATOM   5496  C C     . GLY A  1 763  ? -22.996 91.860  118.072 1.00 44.37 ? 761  GLY A C     1 
ATOM   5497  O O     . GLY A  1 763  ? -22.911 90.909  117.295 1.00 42.71 ? 761  GLY A O     1 
ATOM   5498  N N     . ASP A  1 764  ? -22.374 93.027  117.886 1.00 46.55 ? 762  ASP A N     1 
ATOM   5499  C CA    . ASP A  1 764  ? -21.635 93.337  116.668 1.00 49.09 ? 762  ASP A CA    1 
ATOM   5500  C C     . ASP A  1 764  ? -20.164 92.954  116.845 1.00 47.03 ? 762  ASP A C     1 
ATOM   5501  O O     . ASP A  1 764  ? -19.821 92.122  117.688 1.00 42.77 ? 762  ASP A O     1 
ATOM   5502  C CB    . ASP A  1 764  ? -21.824 94.816  116.297 1.00 50.29 ? 762  ASP A CB    1 
ATOM   5503  C CG    . ASP A  1 764  ? -21.533 95.764  117.449 1.00 52.95 ? 762  ASP A CG    1 
ATOM   5504  O OD1   . ASP A  1 764  ? -20.676 95.456  118.306 1.00 51.73 ? 762  ASP A OD1   1 
ATOM   5505  O OD2   . ASP A  1 764  ? -22.181 96.831  117.502 1.00 56.56 ? 762  ASP A OD2   1 
ATOM   5506  N N     . GLY A  1 765  ? -19.279 93.559  116.049 1.00 49.51 ? 763  GLY A N     1 
ATOM   5507  C CA    . GLY A  1 765  ? -17.866 93.234  116.114 1.00 47.48 ? 763  GLY A CA    1 
ATOM   5508  C C     . GLY A  1 765  ? -17.180 93.692  117.381 1.00 43.60 ? 763  GLY A C     1 
ATOM   5509  O O     . GLY A  1 765  ? -16.113 93.167  117.715 1.00 46.32 ? 763  GLY A O     1 
ATOM   5510  N N     . ARG A  1 766  ? -17.759 94.665  118.087 1.00 46.42 ? 764  ARG A N     1 
ATOM   5511  C CA    . ARG A  1 766  ? -17.218 95.059  119.384 1.00 46.32 ? 764  ARG A CA    1 
ATOM   5512  C C     . ARG A  1 766  ? -17.247 93.899  120.363 1.00 44.19 ? 764  ARG A C     1 
ATOM   5513  O O     . ARG A  1 766  ? -16.298 93.696  121.124 1.00 41.43 ? 764  ARG A O     1 
ATOM   5514  C CB    . ARG A  1 766  ? -18.005 96.225  119.966 1.00 47.07 ? 764  ARG A CB    1 
ATOM   5515  C CG    . ARG A  1 766  ? -17.834 97.529  119.268 1.00 53.96 ? 764  ARG A CG    1 
ATOM   5516  C CD    . ARG A  1 766  ? -18.864 98.485  119.823 1.00 58.84 ? 764  ARG A CD    1 
ATOM   5517  N NE    . ARG A  1 766  ? -20.213 97.962  119.627 1.00 58.79 ? 764  ARG A NE    1 
ATOM   5518  C CZ    . ARG A  1 766  ? -21.295 98.416  120.246 1.00 58.24 ? 764  ARG A CZ    1 
ATOM   5519  N NH1   . ARG A  1 766  ? -21.229 99.406  121.122 1.00 56.36 ? 764  ARG A NH1   1 
ATOM   5520  N NH2   . ARG A  1 766  ? -22.476 97.865  119.976 1.00 59.93 ? 764  ARG A NH2   1 
ATOM   5521  N N     . VAL A  1 767  ? -18.340 93.139  120.369 1.00 45.13 ? 765  VAL A N     1 
ATOM   5522  C CA    . VAL A  1 767  ? -18.413 91.947  121.204 1.00 43.53 ? 765  VAL A CA    1 
ATOM   5523  C C     . VAL A  1 767  ? -17.397 90.918  120.733 1.00 38.52 ? 765  VAL A C     1 
ATOM   5524  O O     . VAL A  1 767  ? -16.634 90.360  121.530 1.00 38.14 ? 765  VAL A O     1 
ATOM   5525  C CB    . VAL A  1 767  ? -19.842 91.377  121.194 1.00 40.21 ? 765  VAL A CB    1 
ATOM   5526  C CG1   . VAL A  1 767  ? -19.963 90.225  122.160 1.00 38.41 ? 765  VAL A CG1   1 
ATOM   5527  C CG2   . VAL A  1 767  ? -20.846 92.471  121.513 1.00 46.04 ? 765  VAL A CG2   1 
ATOM   5528  N N     . GLY A  1 768  ? -17.370 90.655  119.427 1.00 39.04 ? 766  GLY A N     1 
ATOM   5529  C CA    . GLY A  1 768  ? -16.410 89.704  118.903 1.00 36.62 ? 766  GLY A CA    1 
ATOM   5530  C C     . GLY A  1 768  ? -14.984 90.114  119.212 1.00 35.05 ? 766  GLY A C     1 
ATOM   5531  O O     . GLY A  1 768  ? -14.165 89.284  119.598 1.00 32.97 ? 766  GLY A O     1 
ATOM   5532  N N     . ALA A  1 769  ? -14.679 91.408  119.078 1.00 34.72 ? 767  ALA A N     1 
ATOM   5533  C CA    . ALA A  1 769  ? -13.306 91.859  119.294 1.00 35.28 ? 767  ALA A CA    1 
ATOM   5534  C C     . ALA A  1 769  ? -12.939 91.819  120.772 1.00 38.18 ? 767  ALA A C     1 
ATOM   5535  O O     . ALA A  1 769  ? -11.803 91.485  121.124 1.00 36.65 ? 767  ALA A O     1 
ATOM   5536  C CB    . ALA A  1 769  ? -13.110 93.262  118.720 1.00 32.98 ? 767  ALA A CB    1 
ATOM   5537  N N     . ALA A  1 770  ? -13.885 92.158  121.653 1.00 37.38 ? 768  ALA A N     1 
ATOM   5538  C CA    . ALA A  1 770  ? -13.615 92.068  123.084 1.00 39.63 ? 768  ALA A CA    1 
ATOM   5539  C C     . ALA A  1 770  ? -13.317 90.631  123.494 1.00 36.16 ? 768  ALA A C     1 
ATOM   5540  O O     . ALA A  1 770  ? -12.447 90.383  124.340 1.00 38.75 ? 768  ALA A O     1 
ATOM   5541  C CB    . ALA A  1 770  ? -14.799 92.623  123.880 1.00 39.74 ? 768  ALA A CB    1 
ATOM   5542  N N     . LEU A  1 771  ? -14.028 89.672  122.902 1.00 34.03 ? 769  LEU A N     1 
ATOM   5543  C CA    . LEU A  1 771  ? -13.827 88.265  123.238 1.00 34.17 ? 769  LEU A CA    1 
ATOM   5544  C C     . LEU A  1 771  ? -12.486 87.764  122.727 1.00 34.39 ? 769  LEU A C     1 
ATOM   5545  O O     . LEU A  1 771  ? -11.755 87.074  123.447 1.00 37.24 ? 769  LEU A O     1 
ATOM   5546  C CB    . LEU A  1 771  ? -14.960 87.415  122.661 1.00 32.23 ? 769  LEU A CB    1 
ATOM   5547  C CG    . LEU A  1 771  ? -16.385 87.586  123.197 1.00 32.84 ? 769  LEU A CG    1 
ATOM   5548  C CD1   . LEU A  1 771  ? -17.400 86.869  122.301 1.00 33.58 ? 769  LEU A CD1   1 
ATOM   5549  C CD2   . LEU A  1 771  ? -16.512 87.106  124.645 1.00 35.08 ? 769  LEU A CD2   1 
ATOM   5550  N N     . VAL A  1 772  ? -12.150 88.085  121.477 1.00 33.32 ? 770  VAL A N     1 
ATOM   5551  C CA    . VAL A  1 772  ? -10.871 87.651  120.932 1.00 31.79 ? 770  VAL A CA    1 
ATOM   5552  C C     . VAL A  1 772  ? -9.718  88.228  121.748 1.00 32.17 ? 770  VAL A C     1 
ATOM   5553  O O     . VAL A  1 772  ? -8.699  87.564  121.961 1.00 34.04 ? 770  VAL A O     1 
ATOM   5554  C CB    . VAL A  1 772  ? -10.768 88.028  119.442 1.00 29.24 ? 770  VAL A CB    1 
ATOM   5555  C CG1   . VAL A  1 772  ? -9.340  87.806  118.930 1.00 30.27 ? 770  VAL A CG1   1 
ATOM   5556  C CG2   . VAL A  1 772  ? -11.757 87.202  118.624 1.00 33.58 ? 770  VAL A CG2   1 
ATOM   5557  N N     . ALA A  1 773  ? -9.865  89.461  122.237 1.00 35.01 ? 771  ALA A N     1 
ATOM   5558  C CA    . ALA A  1 773  ? -8.759  90.105  122.940 1.00 33.59 ? 771  ALA A CA    1 
ATOM   5559  C C     . ALA A  1 773  ? -8.605  89.648  124.387 1.00 40.82 ? 771  ALA A C     1 
ATOM   5560  O O     . ALA A  1 773  ? -7.577  89.960  125.007 1.00 39.54 ? 771  ALA A O     1 
ATOM   5561  C CB    . ALA A  1 773  ? -8.931  91.626  122.913 1.00 35.86 ? 771  ALA A CB    1 
ATOM   5562  N N     . ALA A  1 774  ? -9.585  88.935  124.946 1.00 36.28 ? 772  ALA A N     1 
ATOM   5563  C CA    . ALA A  1 774  ? -9.544  88.591  126.363 1.00 38.60 ? 772  ALA A CA    1 
ATOM   5564  C C     . ALA A  1 774  ? -8.398  87.630  126.658 1.00 36.25 ? 772  ALA A C     1 
ATOM   5565  O O     . ALA A  1 774  ? -8.177  86.658  125.932 1.00 34.22 ? 772  ALA A O     1 
ATOM   5566  C CB    . ALA A  1 774  ? -10.877 87.986  126.803 1.00 36.47 ? 772  ALA A CB    1 
ATOM   5567  N N     . ALA A  1 775  ? -7.664  87.906  127.747 1.00 35.26 ? 773  ALA A N     1 
ATOM   5568  C CA    . ALA A  1 775  ? -6.445  87.154  128.037 1.00 35.54 ? 773  ALA A CA    1 
ATOM   5569  C C     . ALA A  1 775  ? -6.714  85.663  128.202 1.00 36.41 ? 773  ALA A C     1 
ATOM   5570  O O     . ALA A  1 775  ? -5.843  84.840  127.893 1.00 37.65 ? 773  ALA A O     1 
ATOM   5571  C CB    . ALA A  1 775  ? -5.762  87.711  129.296 1.00 38.98 ? 773  ALA A CB    1 
ATOM   5572  N N     . GLU A  1 776  ? -7.906  85.288  128.667 1.00 35.72 ? 774  GLU A N     1 
ATOM   5573  C CA    . GLU A  1 776  ? -8.187  83.882  128.924 1.00 36.46 ? 774  GLU A CA    1 
ATOM   5574  C C     . GLU A  1 776  ? -8.757  83.154  127.714 1.00 36.07 ? 774  GLU A C     1 
ATOM   5575  O O     . GLU A  1 776  ? -8.943  81.936  127.778 1.00 35.23 ? 774  GLU A O     1 
ATOM   5576  C CB    . GLU A  1 776  ? -9.142  83.734  130.110 1.00 36.77 ? 774  GLU A CB    1 
ATOM   5577  C CG    . GLU A  1 776  ? -8.693  84.489  131.346 1.00 47.77 ? 774  GLU A CG    1 
ATOM   5578  C CD    . GLU A  1 776  ? -9.479  85.777  131.550 1.00 49.63 ? 774  GLU A CD    1 
ATOM   5579  O OE1   . GLU A  1 776  ? -9.730  86.514  130.556 1.00 43.94 ? 774  GLU A OE1   1 
ATOM   5580  O OE2   . GLU A  1 776  ? -9.864  86.038  132.708 1.00 55.23 ? 774  GLU A OE2   1 
ATOM   5581  N N     . THR A  1 777  ? -9.036  83.862  126.624 1.00 35.21 ? 775  THR A N     1 
ATOM   5582  C CA    . THR A  1 777  ? -9.432  83.199  125.384 1.00 33.70 ? 775  THR A CA    1 
ATOM   5583  C C     . THR A  1 777  ? -8.278  82.359  124.855 1.00 33.86 ? 775  THR A C     1 
ATOM   5584  O O     . THR A  1 777  ? -7.198  82.882  124.566 1.00 34.31 ? 775  THR A O     1 
ATOM   5585  C CB    . THR A  1 777  ? -9.851  84.230  124.341 1.00 32.88 ? 775  THR A CB    1 
ATOM   5586  O OG1   . THR A  1 777  ? -11.042 84.899  124.776 1.00 34.69 ? 775  THR A OG1   1 
ATOM   5587  C CG2   . THR A  1 777  ? -10.092 83.545  122.995 1.00 29.75 ? 775  THR A CG2   1 
ATOM   5588  N N     . ALA A  1 778  ? -8.507  81.056  124.742 1.00 31.70 ? 776  ALA A N     1 
ATOM   5589  C CA    . ALA A  1 778  ? -7.465  80.099  124.419 1.00 31.88 ? 776  ALA A CA    1 
ATOM   5590  C C     . ALA A  1 778  ? -7.487  79.664  122.965 1.00 30.32 ? 776  ALA A C     1 
ATOM   5591  O O     . ALA A  1 778  ? -6.593  78.931  122.546 1.00 35.50 ? 776  ALA A O     1 
ATOM   5592  C CB    . ALA A  1 778  ? -7.586  78.859  125.322 1.00 32.75 ? 776  ALA A CB    1 
ATOM   5593  N N     . GLY A  1 779  ? -8.480  80.094  122.199 1.00 31.53 ? 777  GLY A N     1 
ATOM   5594  C CA    . GLY A  1 779  ? -8.641  79.694  120.817 1.00 27.69 ? 777  GLY A CA    1 
ATOM   5595  C C     . GLY A  1 779  ? -9.841  80.400  120.225 1.00 27.26 ? 777  GLY A C     1 
ATOM   5596  O O     . GLY A  1 779  ? -10.775 80.758  120.956 1.00 30.37 ? 777  GLY A O     1 
ATOM   5597  N N     . VAL A  1 780  ? -9.830  80.621  118.912 1.00 28.26 ? 778  VAL A N     1 
ATOM   5598  C CA    . VAL A  1 780  ? -10.910 81.308  118.217 1.00 29.57 ? 778  VAL A CA    1 
ATOM   5599  C C     . VAL A  1 780  ? -11.303 80.459  117.013 1.00 26.61 ? 778  VAL A C     1 
ATOM   5600  O O     . VAL A  1 780  ? -10.436 79.994  116.269 1.00 26.75 ? 778  VAL A O     1 
ATOM   5601  C CB    . VAL A  1 780  ? -10.492 82.724  117.765 1.00 27.51 ? 778  VAL A CB    1 
ATOM   5602  C CG1   . VAL A  1 780  ? -11.641 83.425  117.024 1.00 30.52 ? 778  VAL A CG1   1 
ATOM   5603  C CG2   . VAL A  1 780  ? -10.038 83.549  118.955 1.00 28.28 ? 778  VAL A CG2   1 
ATOM   5604  N N     . MET A  1 781  ? -12.598 80.243  116.836 1.00 28.26 ? 779  MET A N     1 
ATOM   5605  C CA    . MET A  1 781  ? -13.131 79.620  115.630 1.00 27.87 ? 779  MET A CA    1 
ATOM   5606  C C     . MET A  1 781  ? -13.957 80.673  114.906 1.00 28.42 ? 779  MET A C     1 
ATOM   5607  O O     . MET A  1 781  ? -14.956 81.160  115.450 1.00 27.12 ? 779  MET A O     1 
ATOM   5608  C CB    . MET A  1 781  ? -13.972 78.391  115.977 1.00 28.14 ? 779  MET A CB    1 
ATOM   5609  C CG    . MET A  1 781  ? -13.179 77.325  116.741 1.00 28.47 ? 779  MET A CG    1 
ATOM   5610  S SD    . MET A  1 781  ? -14.247 76.048  117.469 1.00 29.26 ? 779  MET A SD    1 
ATOM   5611  C CE    . MET A  1 781  ? -14.510 75.029  116.024 1.00 25.78 ? 779  MET A CE    1 
ATOM   5612  N N     . PHE A  1 782  ? -13.525 81.051  113.701 1.00 26.56 ? 780  PHE A N     1 
ATOM   5613  C CA    . PHE A  1 782  ? -14.162 82.136  112.968 1.00 27.92 ? 780  PHE A CA    1 
ATOM   5614  C C     . PHE A  1 782  ? -14.575 81.642  111.591 1.00 28.02 ? 780  PHE A C     1 
ATOM   5615  O O     . PHE A  1 782  ? -13.798 80.967  110.920 1.00 25.27 ? 780  PHE A O     1 
ATOM   5616  C CB    . PHE A  1 782  ? -13.224 83.345  112.820 1.00 26.64 ? 780  PHE A CB    1 
ATOM   5617  C CG    . PHE A  1 782  ? -13.783 84.448  111.954 1.00 27.79 ? 780  PHE A CG    1 
ATOM   5618  C CD1   . PHE A  1 782  ? -14.695 85.367  112.469 1.00 26.93 ? 780  PHE A CD1   1 
ATOM   5619  C CD2   . PHE A  1 782  ? -13.397 84.564  110.620 1.00 26.65 ? 780  PHE A CD2   1 
ATOM   5620  C CE1   . PHE A  1 782  ? -15.217 86.377  111.684 1.00 30.16 ? 780  PHE A CE1   1 
ATOM   5621  C CE2   . PHE A  1 782  ? -13.918 85.576  109.823 1.00 28.60 ? 780  PHE A CE2   1 
ATOM   5622  C CZ    . PHE A  1 782  ? -14.823 86.479  110.348 1.00 31.56 ? 780  PHE A CZ    1 
ATOM   5623  N N     . THR A  1 783  ? -15.797 81.978  111.186 1.00 26.14 ? 781  THR A N     1 
ATOM   5624  C CA    . THR A  1 783  ? -16.260 81.797  109.813 1.00 28.73 ? 781  THR A CA    1 
ATOM   5625  C C     . THR A  1 783  ? -16.874 83.117  109.399 1.00 26.06 ? 781  THR A C     1 
ATOM   5626  O O     . THR A  1 783  ? -17.824 83.580  110.039 1.00 28.44 ? 781  THR A O     1 
ATOM   5627  C CB    . THR A  1 783  ? -17.290 80.666  109.673 1.00 26.67 ? 781  THR A CB    1 
ATOM   5628  O OG1   . THR A  1 783  ? -16.749 79.432  110.158 1.00 26.11 ? 781  THR A OG1   1 
ATOM   5629  C CG2   . THR A  1 783  ? -17.687 80.493  108.191 1.00 28.57 ? 781  THR A CG2   1 
ATOM   5630  N N     . GLY A  1 784  ? -16.333 83.722  108.345 1.00 27.36 ? 782  GLY A N     1 
ATOM   5631  C CA    . GLY A  1 784  ? -16.773 85.042  107.934 1.00 27.72 ? 782  GLY A CA    1 
ATOM   5632  C C     . GLY A  1 784  ? -15.864 85.586  106.851 1.00 30.58 ? 782  GLY A C     1 
ATOM   5633  O O     . GLY A  1 784  ? -15.194 84.829  106.156 1.00 28.08 ? 782  GLY A O     1 
ATOM   5634  N N     . SER A  1 785  ? -15.851 86.907  106.719 1.00 31.24 ? 783  SER A N     1 
ATOM   5635  C CA    . SER A  1 785  ? -15.043 87.518  105.673 1.00 34.39 ? 783  SER A CA    1 
ATOM   5636  C C     . SER A  1 785  ? -13.553 87.396  105.978 1.00 32.80 ? 783  SER A C     1 
ATOM   5637  O O     . SER A  1 785  ? -13.136 87.284  107.138 1.00 30.20 ? 783  SER A O     1 
ATOM   5638  C CB    . SER A  1 785  ? -15.407 88.987  105.511 1.00 34.16 ? 783  SER A CB    1 
ATOM   5639  O OG    . SER A  1 785  ? -15.010 89.709  106.652 1.00 36.61 ? 783  SER A OG    1 
ATOM   5640  N N     . THR A  1 786  ? -12.745 87.424  104.910 1.00 32.34 ? 784  THR A N     1 
ATOM   5641  C CA    . THR A  1 786  ? -11.294 87.432  105.068 1.00 34.36 ? 784  THR A CA    1 
ATOM   5642  C C     . THR A  1 786  ? -10.824 88.691  105.780 1.00 34.17 ? 784  THR A C     1 
ATOM   5643  O O     . THR A  1 786  ? -9.870  88.647  106.569 1.00 34.05 ? 784  THR A O     1 
ATOM   5644  C CB    . THR A  1 786  ? -10.609 87.312  103.704 1.00 37.05 ? 784  THR A CB    1 
ATOM   5645  O OG1   . THR A  1 786  ? -11.057 86.120  103.049 1.00 39.00 ? 784  THR A OG1   1 
ATOM   5646  C CG2   . THR A  1 786  ? -9.094  87.235  103.879 1.00 40.67 ? 784  THR A CG2   1 
ATOM   5647  N N     . GLU A  1 787  ? -11.483 89.825  105.513 1.00 34.28 ? 785  GLU A N     1 
ATOM   5648  C CA    . GLU A  1 787  ? -11.092 91.090  106.131 1.00 36.99 ? 785  GLU A CA    1 
ATOM   5649  C C     . GLU A  1 787  ? -11.167 91.001  107.651 1.00 33.25 ? 785  GLU A C     1 
ATOM   5650  O O     . GLU A  1 787  ? -10.244 91.420  108.358 1.00 32.97 ? 785  GLU A O     1 
ATOM   5651  C CB    . GLU A  1 787  ? -11.983 92.226  105.607 1.00 38.94 ? 785  GLU A CB    1 
ATOM   5652  C CG    . GLU A  1 787  ? -12.549 91.967  104.202 1.00 49.28 ? 785  GLU A CG    1 
ATOM   5653  C CD    . GLU A  1 787  ? -13.719 92.877  103.848 1.00 57.29 ? 785  GLU A CD    1 
ATOM   5654  O OE1   . GLU A  1 787  ? -13.755 94.033  104.332 1.00 54.94 ? 785  GLU A OE1   1 
ATOM   5655  O OE2   . GLU A  1 787  ? -14.606 92.430  103.085 1.00 60.44 ? 785  GLU A OE2   1 
ATOM   5656  N N     . VAL A  1 788  ? -12.262 90.448  108.173 1.00 34.65 ? 786  VAL A N     1 
ATOM   5657  C CA    . VAL A  1 788  ? -12.403 90.335  109.620 1.00 32.31 ? 786  VAL A CA    1 
ATOM   5658  C C     . VAL A  1 788  ? -11.457 89.278  110.163 1.00 29.57 ? 786  VAL A C     1 
ATOM   5659  O O     . VAL A  1 788  ? -10.837 89.466  111.216 1.00 33.19 ? 786  VAL A O     1 
ATOM   5660  C CB    . VAL A  1 788  ? -13.864 90.029  109.985 1.00 33.20 ? 786  VAL A CB    1 
ATOM   5661  C CG1   . VAL A  1 788  ? -13.988 89.711  111.475 1.00 33.24 ? 786  VAL A CG1   1 
ATOM   5662  C CG2   . VAL A  1 788  ? -14.725 91.220  109.627 1.00 38.46 ? 786  VAL A CG2   1 
ATOM   5663  N N     . ALA A  1 789  ? -11.334 88.152  109.458 1.00 28.38 ? 787  ALA A N     1 
ATOM   5664  C CA    . ALA A  1 789  ? -10.399 87.110  109.877 1.00 32.31 ? 787  ALA A CA    1 
ATOM   5665  C C     . ALA A  1 789  ? -8.988  87.665  110.019 1.00 29.68 ? 787  ALA A C     1 
ATOM   5666  O O     . ALA A  1 789  ? -8.260  87.309  110.956 1.00 29.51 ? 787  ALA A O     1 
ATOM   5667  C CB    . ALA A  1 789  ? -10.428 85.951  108.881 1.00 28.47 ? 787  ALA A CB    1 
ATOM   5668  N N     A ARG A  1 790  ? -8.583  88.550  109.104 0.56 31.56 ? 788  ARG A N     1 
ATOM   5669  N N     B ARG A  1 790  ? -8.588  88.553  109.104 0.44 31.58 ? 788  ARG A N     1 
ATOM   5670  C CA    A ARG A  1 790  ? -7.248  89.137  109.196 0.56 33.20 ? 788  ARG A CA    1 
ATOM   5671  C CA    B ARG A  1 790  ? -7.255  89.146  109.178 0.44 33.21 ? 788  ARG A CA    1 
ATOM   5672  C C     A ARG A  1 790  ? -7.136  90.082  110.387 0.56 33.66 ? 788  ARG A C     1 
ATOM   5673  C C     B ARG A  1 790  ? -7.131  90.099  110.364 0.44 33.65 ? 788  ARG A C     1 
ATOM   5674  O O     A ARG A  1 790  ? -6.064  90.189  110.997 0.56 33.36 ? 788  ARG A O     1 
ATOM   5675  O O     B ARG A  1 790  ? -6.049  90.221  110.952 0.44 33.36 ? 788  ARG A O     1 
ATOM   5676  C CB    A ARG A  1 790  ? -6.910  89.862  107.892 0.56 35.71 ? 788  ARG A CB    1 
ATOM   5677  C CB    B ARG A  1 790  ? -6.938  89.858  107.859 0.44 35.71 ? 788  ARG A CB    1 
ATOM   5678  C CG    A ARG A  1 790  ? -5.476  90.335  107.775 0.56 38.22 ? 788  ARG A CG    1 
ATOM   5679  C CG    B ARG A  1 790  ? -5.490  90.270  107.674 0.44 38.20 ? 788  ARG A CG    1 
ATOM   5680  C CD    A ARG A  1 790  ? -5.266  91.109  106.472 0.56 39.06 ? 788  ARG A CD    1 
ATOM   5681  C CD    B ARG A  1 790  ? -5.250  90.866  106.279 0.44 39.12 ? 788  ARG A CD    1 
ATOM   5682  N NE    A ARG A  1 790  ? -5.685  90.349  105.299 0.56 39.70 ? 788  ARG A NE    1 
ATOM   5683  N NE    B ARG A  1 790  ? -5.277  89.863  105.217 0.44 39.76 ? 788  ARG A NE    1 
ATOM   5684  C CZ    A ARG A  1 790  ? -4.948  89.414  104.715 0.56 39.12 ? 788  ARG A CZ    1 
ATOM   5685  C CZ    B ARG A  1 790  ? -6.169  89.820  104.235 0.44 39.04 ? 788  ARG A CZ    1 
ATOM   5686  N NH1   A ARG A  1 790  ? -3.758  89.074  105.191 0.56 38.06 ? 788  ARG A NH1   1 
ATOM   5687  N NH1   B ARG A  1 790  ? -7.151  90.703  104.151 0.44 40.53 ? 788  ARG A NH1   1 
ATOM   5688  N NH2   A ARG A  1 790  ? -5.409  88.814  103.622 0.56 39.32 ? 788  ARG A NH2   1 
ATOM   5689  N NH2   B ARG A  1 790  ? -6.065  88.873  103.307 0.44 39.32 ? 788  ARG A NH2   1 
ATOM   5690  N N     . LEU A  1 791  ? -8.222  90.777  110.731 1.00 30.98 ? 789  LEU A N     1 
ATOM   5691  C CA    . LEU A  1 791  ? -8.203  91.617  111.924 1.00 33.68 ? 789  LEU A CA    1 
ATOM   5692  C C     . LEU A  1 791  ? -8.105  90.767  113.188 1.00 31.30 ? 789  LEU A C     1 
ATOM   5693  O O     . LEU A  1 791  ? -7.427  91.149  114.149 1.00 31.46 ? 789  LEU A O     1 
ATOM   5694  C CB    . LEU A  1 791  ? -9.449  92.510  111.970 1.00 35.01 ? 789  LEU A CB    1 
ATOM   5695  C CG    . LEU A  1 791  ? -9.525  93.712  111.015 1.00 35.67 ? 789  LEU A CG    1 
ATOM   5696  C CD1   . LEU A  1 791  ? -10.906 94.336  111.077 1.00 35.40 ? 789  LEU A CD1   1 
ATOM   5697  C CD2   . LEU A  1 791  ? -8.464  94.761  111.351 1.00 36.90 ? 789  LEU A CD2   1 
ATOM   5698  N N     . ILE A  1 792  ? -8.778  89.615  113.211 1.00 29.26 ? 790  ILE A N     1 
ATOM   5699  C CA    . ILE A  1 792  ? -8.665  88.731  114.368 1.00 32.77 ? 790  ILE A CA    1 
ATOM   5700  C C     . ILE A  1 792  ? -7.257  88.171  114.468 1.00 31.61 ? 790  ILE A C     1 
ATOM   5701  O O     . ILE A  1 792  ? -6.677  88.101  115.559 1.00 30.13 ? 790  ILE A O     1 
ATOM   5702  C CB    . ILE A  1 792  ? -9.715  87.610  114.297 1.00 29.84 ? 790  ILE A CB    1 
ATOM   5703  C CG1   . ILE A  1 792  ? -11.100 88.200  114.577 1.00 29.92 ? 790  ILE A CG1   1 
ATOM   5704  C CG2   . ILE A  1 792  ? -9.367  86.490  115.288 1.00 28.28 ? 790  ILE A CG2   1 
ATOM   5705  C CD1   . ILE A  1 792  ? -12.268 87.387  113.997 1.00 30.07 ? 790  ILE A CD1   1 
ATOM   5706  N N     . GLN A  1 793  ? -6.685  87.772  113.330 1.00 28.03 ? 791  GLN A N     1 
ATOM   5707  C CA    . GLN A  1 793  ? -5.321  87.262  113.309 1.00 31.33 ? 791  GLN A CA    1 
ATOM   5708  C C     . GLN A  1 793  ? -4.351  88.255  113.940 1.00 29.82 ? 791  GLN A C     1 
ATOM   5709  O O     . GLN A  1 793  ? -3.486  87.871  114.734 1.00 30.56 ? 791  GLN A O     1 
ATOM   5710  C CB    . GLN A  1 793  ? -4.916  86.941  111.870 1.00 29.38 ? 791  GLN A CB    1 
ATOM   5711  C CG    . GLN A  1 793  ? -3.485  86.424  111.736 1.00 30.21 ? 791  GLN A CG    1 
ATOM   5712  C CD    . GLN A  1 793  ? -3.017  86.347  110.295 1.00 34.86 ? 791  GLN A CD    1 
ATOM   5713  O OE1   . GLN A  1 793  ? -3.253  87.258  109.498 1.00 39.55 ? 791  GLN A OE1   1 
ATOM   5714  N NE2   . GLN A  1 793  ? -2.351  85.258  109.952 1.00 37.42 ? 791  GLN A NE2   1 
ATOM   5715  N N     . ALA A  1 794  ? -4.490  89.543  113.612 1.00 32.53 ? 792  ALA A N     1 
ATOM   5716  C CA    . ALA A  1 794  ? -3.583  90.541  114.174 1.00 33.66 ? 792  ALA A CA    1 
ATOM   5717  C C     . ALA A  1 794  ? -3.784  90.692  115.680 1.00 31.55 ? 792  ALA A C     1 
ATOM   5718  O O     . ALA A  1 794  ? -2.807  90.846  116.425 1.00 33.61 ? 792  ALA A O     1 
ATOM   5719  C CB    . ALA A  1 794  ? -3.767  91.883  113.467 1.00 32.84 ? 792  ALA A CB    1 
ATOM   5720  N N     . GLN A  1 795  ? -5.037  90.648  116.147 1.00 30.54 ? 793  GLN A N     1 
ATOM   5721  C CA    . GLN A  1 795  ? -5.295  90.687  117.586 1.00 33.11 ? 793  GLN A CA    1 
ATOM   5722  C C     . GLN A  1 795  ? -4.604  89.530  118.290 1.00 31.64 ? 793  GLN A C     1 
ATOM   5723  O O     . GLN A  1 795  ? -3.937  89.718  119.312 1.00 33.99 ? 793  GLN A O     1 
ATOM   5724  C CB    . GLN A  1 795  ? -6.800  90.626  117.878 1.00 34.96 ? 793  GLN A CB    1 
ATOM   5725  C CG    . GLN A  1 795  ? -7.617  91.881  117.592 1.00 37.48 ? 793  GLN A CG    1 
ATOM   5726  C CD    . GLN A  1 795  ? -9.087  91.724  118.020 1.00 39.26 ? 793  GLN A CD    1 
ATOM   5727  O OE1   . GLN A  1 795  ? -9.967  91.429  117.199 1.00 44.51 ? 793  GLN A OE1   1 
ATOM   5728  N NE2   . GLN A  1 795  ? -9.350  91.915  119.308 1.00 36.08 ? 793  GLN A NE2   1 
ATOM   5729  N N     . LEU A  1 796  ? -4.769  88.317  117.758 1.00 30.97 ? 794  LEU A N     1 
ATOM   5730  C CA    . LEU A  1 796  ? -4.255  87.132  118.433 1.00 30.63 ? 794  LEU A CA    1 
ATOM   5731  C C     . LEU A  1 796  ? -2.733  87.099  118.455 1.00 34.80 ? 794  LEU A C     1 
ATOM   5732  O O     . LEU A  1 796  ? -2.145  86.563  119.402 1.00 30.05 ? 794  LEU A O     1 
ATOM   5733  C CB    . LEU A  1 796  ? -4.789  85.869  117.760 1.00 31.76 ? 794  LEU A CB    1 
ATOM   5734  C CG    . LEU A  1 796  ? -6.267  85.581  117.984 1.00 30.08 ? 794  LEU A CG    1 
ATOM   5735  C CD1   . LEU A  1 796  ? -6.650  84.339  117.205 1.00 27.99 ? 794  LEU A CD1   1 
ATOM   5736  C CD2   . LEU A  1 796  ? -6.515  85.390  119.476 1.00 32.32 ? 794  LEU A CD2   1 
ATOM   5737  N N     . ALA A  1 797  ? -2.080  87.654  117.430 1.00 31.71 ? 795  ALA A N     1 
ATOM   5738  C CA    . ALA A  1 797  ? -0.622  87.644  117.403 1.00 33.74 ? 795  ALA A CA    1 
ATOM   5739  C C     . ALA A  1 797  ? -0.024  88.480  118.518 1.00 33.88 ? 795  ALA A C     1 
ATOM   5740  O O     . ALA A  1 797  ? 1.174   88.350  118.790 1.00 34.45 ? 795  ALA A O     1 
ATOM   5741  C CB    . ALA A  1 797  ? -0.097  88.140  116.054 1.00 34.76 ? 795  ALA A CB    1 
ATOM   5742  N N     . ASP A  1 798  ? -0.832  89.325  119.168 1.00 33.48 ? 796  ASP A N     1 
ATOM   5743  C CA    . ASP A  1 798  ? -0.377  90.060  120.341 1.00 35.17 ? 796  ASP A CA    1 
ATOM   5744  C C     . ASP A  1 798  ? -0.190  89.162  121.556 1.00 38.01 ? 796  ASP A C     1 
ATOM   5745  O O     . ASP A  1 798  ? 0.497   89.564  122.502 1.00 36.65 ? 796  ASP A O     1 
ATOM   5746  C CB    . ASP A  1 798  ? -1.381  91.165  120.699 1.00 40.22 ? 796  ASP A CB    1 
ATOM   5747  C CG    . ASP A  1 798  ? -1.169  92.451  119.908 1.00 49.67 ? 796  ASP A CG    1 
ATOM   5748  O OD1   . ASP A  1 798  ? -0.123  92.584  119.227 1.00 50.68 ? 796  ASP A OD1   1 
ATOM   5749  O OD2   . ASP A  1 798  ? -2.053  93.338  119.980 1.00 45.18 ? 796  ASP A OD2   1 
ATOM   5750  N N     . ARG A  1 799  ? -0.793  87.970  121.565 1.00 36.31 ? 797  ARG A N     1 
ATOM   5751  C CA    . ARG A  1 799  ? -0.923  87.187  122.786 1.00 36.60 ? 797  ARG A CA    1 
ATOM   5752  C C     . ARG A  1 799  ? -0.269  85.821  122.639 1.00 35.21 ? 797  ARG A C     1 
ATOM   5753  O O     . ARG A  1 799  ? -0.029  85.321  121.533 1.00 32.76 ? 797  ARG A O     1 
ATOM   5754  C CB    . ARG A  1 799  ? -2.403  86.992  123.190 1.00 39.22 ? 797  ARG A CB    1 
ATOM   5755  C CG    . ARG A  1 799  ? -3.207  88.279  123.407 1.00 37.52 ? 797  ARG A CG    1 
ATOM   5756  C CD    . ARG A  1 799  ? -4.503  88.037  124.207 1.00 35.78 ? 797  ARG A CD    1 
ATOM   5757  N NE    . ARG A  1 799  ? -5.554  87.361  123.450 1.00 41.46 ? 797  ARG A NE    1 
ATOM   5758  C CZ    . ARG A  1 799  ? -5.913  86.095  123.632 1.00 38.66 ? 797  ARG A CZ    1 
ATOM   5759  N NH1   . ARG A  1 799  ? -5.337  85.336  124.551 1.00 36.74 ? 797  ARG A NH1   1 
ATOM   5760  N NH2   . ARG A  1 799  ? -6.866  85.573  122.866 1.00 36.11 ? 797  ARG A NH2   1 
ATOM   5761  N N     . LEU A  1 800  ? 0.021   85.222  123.787 1.00 36.14 ? 798  LEU A N     1 
ATOM   5762  C CA    . LEU A  1 800  ? 0.463   83.838  123.856 1.00 36.79 ? 798  LEU A CA    1 
ATOM   5763  C C     . LEU A  1 800  ? -0.388  83.128  124.898 1.00 34.53 ? 798  LEU A C     1 
ATOM   5764  O O     . LEU A  1 800  ? -1.012  83.762  125.749 1.00 36.23 ? 798  LEU A O     1 
ATOM   5765  C CB    . LEU A  1 800  ? 1.957   83.717  124.214 1.00 39.15 ? 798  LEU A CB    1 
ATOM   5766  C CG    . LEU A  1 800  ? 3.025   84.253  123.249 1.00 40.09 ? 798  LEU A CG    1 
ATOM   5767  C CD1   . LEU A  1 800  ? 4.425   84.267  123.897 1.00 39.87 ? 798  LEU A CD1   1 
ATOM   5768  C CD2   . LEU A  1 800  ? 3.056   83.457  121.966 1.00 35.33 ? 798  LEU A CD2   1 
ATOM   5769  N N     . SER A  1 801  ? -0.433  81.809  124.803 1.00 37.38 ? 799  SER A N     1 
ATOM   5770  C CA    . SER A  1 801  ? -1.042  81.004  125.845 1.00 41.00 ? 799  SER A CA    1 
ATOM   5771  C C     . SER A  1 801  ? -0.165  81.063  127.093 1.00 46.00 ? 799  SER A C     1 
ATOM   5772  O O     . SER A  1 801  ? 0.993   81.482  127.023 1.00 45.05 ? 799  SER A O     1 
ATOM   5773  C CB    . SER A  1 801  ? -1.204  79.560  125.371 1.00 43.52 ? 799  SER A CB    1 
ATOM   5774  O OG    . SER A  1 801  ? 0.045   78.897  125.366 1.00 45.23 ? 799  SER A OG    1 
ATOM   5775  N N     . PRO A  1 802  ? -0.696  80.664  128.255 1.00 45.01 ? 800  PRO A N     1 
ATOM   5776  C CA    . PRO A  1 802  ? 0.153   80.642  129.461 1.00 44.25 ? 800  PRO A CA    1 
ATOM   5777  C C     . PRO A  1 802  ? 1.405   79.797  129.286 1.00 49.91 ? 800  PRO A C     1 
ATOM   5778  O O     . PRO A  1 802  ? 2.434   80.077  129.917 1.00 46.91 ? 800  PRO A O     1 
ATOM   5779  C CB    . PRO A  1 802  ? -0.781  80.080  130.544 1.00 44.48 ? 800  PRO A CB    1 
ATOM   5780  C CG    . PRO A  1 802  ? -1.929  79.456  129.806 1.00 51.34 ? 800  PRO A CG    1 
ATOM   5781  C CD    . PRO A  1 802  ? -2.081  80.249  128.544 1.00 45.94 ? 800  PRO A CD    1 
ATOM   5782  N N     . ALA A  1 803  ? 1.357   78.797  128.408 1.00 48.71 ? 801  ALA A N     1 
ATOM   5783  C CA    . ALA A  1 803  ? 2.519   77.999  128.045 1.00 48.86 ? 801  ALA A CA    1 
ATOM   5784  C C     . ALA A  1 803  ? 3.458   78.716  127.081 1.00 50.04 ? 801  ALA A C     1 
ATOM   5785  O O     . ALA A  1 803  ? 4.507   78.160  126.742 1.00 51.68 ? 801  ALA A O     1 
ATOM   5786  C CB    . ALA A  1 803  ? 2.066   76.675  127.428 1.00 47.66 ? 801  ALA A CB    1 
ATOM   5787  N N     . GLY A  1 804  ? 3.108   79.917  126.626 1.00 46.80 ? 802  GLY A N     1 
ATOM   5788  C CA    . GLY A  1 804  ? 3.958   80.651  125.706 1.00 42.89 ? 802  GLY A CA    1 
ATOM   5789  C C     . GLY A  1 804  ? 3.851   80.231  124.254 1.00 42.98 ? 802  GLY A C     1 
ATOM   5790  O O     . GLY A  1 804  ? 4.843   80.311  123.521 1.00 43.46 ? 802  GLY A O     1 
ATOM   5791  N N     . ARG A  1 805  ? 2.674   79.799  123.810 1.00 42.51 ? 803  ARG A N     1 
ATOM   5792  C CA    . ARG A  1 805  ? 2.440   79.323  122.456 1.00 38.29 ? 803  ARG A CA    1 
ATOM   5793  C C     . ARG A  1 805  ? 1.329   80.123  121.783 1.00 32.13 ? 803  ARG A C     1 
ATOM   5794  O O     . ARG A  1 805  ? 0.499   80.739  122.462 1.00 35.50 ? 803  ARG A O     1 
ATOM   5795  C CB    . ARG A  1 805  ? 2.071   77.833  122.469 1.00 39.88 ? 803  ARG A CB    1 
ATOM   5796  C CG    . ARG A  1 805  ? 3.146   76.964  123.075 1.00 42.70 ? 803  ARG A CG    1 
ATOM   5797  C CD    . ARG A  1 805  ? 4.476   77.291  122.446 1.00 41.96 ? 803  ARG A CD    1 
ATOM   5798  N NE    . ARG A  1 805  ? 5.422   76.187  122.545 1.00 44.45 ? 803  ARG A NE    1 
ATOM   5799  C CZ    . ARG A  1 805  ? 6.513   76.189  123.296 1.00 40.21 ? 803  ARG A CZ    1 
ATOM   5800  N NH1   . ARG A  1 805  ? 6.826   77.224  124.063 1.00 47.34 ? 803  ARG A NH1   1 
ATOM   5801  N NH2   . ARG A  1 805  ? 7.325   75.131  123.261 1.00 45.84 ? 803  ARG A NH2   1 
ATOM   5802  N N     . PRO A  1 806  ? 1.290   80.152  120.448 1.00 33.25 ? 804  PRO A N     1 
ATOM   5803  C CA    . PRO A  1 806  ? 0.269   80.956  119.768 1.00 33.93 ? 804  PRO A CA    1 
ATOM   5804  C C     . PRO A  1 806  ? -1.128  80.428  120.049 1.00 34.56 ? 804  PRO A C     1 
ATOM   5805  O O     . PRO A  1 806  ? -1.329  79.229  120.253 1.00 31.00 ? 804  PRO A O     1 
ATOM   5806  C CB    . PRO A  1 806  ? 0.625   80.811  118.283 1.00 34.59 ? 804  PRO A CB    1 
ATOM   5807  C CG    . PRO A  1 806  ? 2.052   80.364  118.265 1.00 36.75 ? 804  PRO A CG    1 
ATOM   5808  C CD    . PRO A  1 806  ? 2.204   79.515  119.493 1.00 33.85 ? 804  PRO A CD    1 
ATOM   5809  N N     . ILE A  1 807  ? -2.091  81.347  120.059 1.00 30.99 ? 805  ILE A N     1 
ATOM   5810  C CA    . ILE A  1 807  ? -3.506  81.019  120.233 1.00 31.20 ? 805  ILE A CA    1 
ATOM   5811  C C     . ILE A  1 807  ? -4.042  80.454  118.925 1.00 33.15 ? 805  ILE A C     1 
ATOM   5812  O O     . ILE A  1 807  ? -4.010  81.146  117.898 1.00 31.51 ? 805  ILE A O     1 
ATOM   5813  C CB    . ILE A  1 807  ? -4.328  82.248  120.650 1.00 33.17 ? 805  ILE A CB    1 
ATOM   5814  C CG1   . ILE A  1 807  ? -3.732  82.924  121.891 1.00 34.26 ? 805  ILE A CG1   1 
ATOM   5815  C CG2   . ILE A  1 807  ? -5.807  81.871  120.840 1.00 28.55 ? 805  ILE A CG2   1 
ATOM   5816  C CD1   . ILE A  1 807  ? -3.630  82.045  123.123 1.00 33.76 ? 805  ILE A CD1   1 
ATOM   5817  N N     . PRO A  1 808  ? -4.541  79.221  118.912 1.00 31.83 ? 806  PRO A N     1 
ATOM   5818  C CA    . PRO A  1 808  ? -5.034  78.638  117.659 1.00 28.80 ? 806  PRO A CA    1 
ATOM   5819  C C     . PRO A  1 808  ? -6.203  79.431  117.099 1.00 30.94 ? 806  PRO A C     1 
ATOM   5820  O O     . PRO A  1 808  ? -7.103  79.846  117.829 1.00 30.52 ? 806  PRO A O     1 
ATOM   5821  C CB    . PRO A  1 808  ? -5.473  77.227  118.069 1.00 29.41 ? 806  PRO A CB    1 
ATOM   5822  C CG    . PRO A  1 808  ? -4.729  76.957  119.350 1.00 31.84 ? 806  PRO A CG    1 
ATOM   5823  C CD    . PRO A  1 808  ? -4.584  78.271  120.031 1.00 27.89 ? 806  PRO A CD    1 
ATOM   5824  N N     . LEU A  1 809  ? -6.188  79.621  115.783 1.00 31.76 ? 807  LEU A N     1 
ATOM   5825  C CA    . LEU A  1 809  ? -7.267  80.288  115.070 1.00 28.92 ? 807  LEU A CA    1 
ATOM   5826  C C     . LEU A  1 809  ? -7.706  79.388  113.929 1.00 28.86 ? 807  LEU A C     1 
ATOM   5827  O O     . LEU A  1 809  ? -6.879  79.016  113.091 1.00 25.26 ? 807  LEU A O     1 
ATOM   5828  C CB    . LEU A  1 809  ? -6.808  81.643  114.520 1.00 29.32 ? 807  LEU A CB    1 
ATOM   5829  C CG    . LEU A  1 809  ? -7.802  82.272  113.539 1.00 31.23 ? 807  LEU A CG    1 
ATOM   5830  C CD1   . LEU A  1 809  ? -9.123  82.623  114.242 1.00 27.76 ? 807  LEU A CD1   1 
ATOM   5831  C CD2   . LEU A  1 809  ? -7.210  83.503  112.864 1.00 33.47 ? 807  LEU A CD2   1 
ATOM   5832  N N     . ILE A  1 810  ? -8.987  79.017  113.903 1.00 25.57 ? 808  ILE A N     1 
ATOM   5833  C CA    . ILE A  1 810  ? -9.582  78.366  112.743 1.00 27.57 ? 808  ILE A CA    1 
ATOM   5834  C C     . ILE A  1 810  ? -10.389 79.434  112.034 1.00 26.75 ? 808  ILE A C     1 
ATOM   5835  O O     . ILE A  1 810  ? -11.382 79.929  112.573 1.00 27.23 ? 808  ILE A O     1 
ATOM   5836  C CB    . ILE A  1 810  ? -10.475 77.174  113.115 1.00 24.89 ? 808  ILE A CB    1 
ATOM   5837  C CG1   . ILE A  1 810  ? -9.702  76.123  113.910 1.00 27.32 ? 808  ILE A CG1   1 
ATOM   5838  C CG2   . ILE A  1 810  ? -11.039 76.519  111.837 1.00 28.05 ? 808  ILE A CG2   1 
ATOM   5839  C CD1   . ILE A  1 810  ? -10.549 74.883  114.197 1.00 32.55 ? 808  ILE A CD1   1 
ATOM   5840  N N     . ALA A  1 811  ? -9.973  79.799  110.828 1.00 29.63 ? 809  ALA A N     1 
ATOM   5841  C CA    . ALA A  1 811  ? -10.627 80.869  110.085 1.00 28.29 ? 809  ALA A CA    1 
ATOM   5842  C C     . ALA A  1 811  ? -11.033 80.324  108.727 1.00 31.09 ? 809  ALA A C     1 
ATOM   5843  O O     . ALA A  1 811  ? -10.177 79.984  107.904 1.00 27.25 ? 809  ALA A O     1 
ATOM   5844  C CB    . ALA A  1 811  ? -9.716  82.087  109.940 1.00 31.41 ? 809  ALA A CB    1 
ATOM   5845  N N     . GLU A  1 812  ? -12.333 80.243  108.495 1.00 27.95 ? 810  GLU A N     1 
ATOM   5846  C CA    . GLU A  1 812  ? -12.855 79.777  107.224 1.00 26.38 ? 810  GLU A CA    1 
ATOM   5847  C C     . GLU A  1 812  ? -13.510 80.971  106.541 1.00 29.15 ? 810  GLU A C     1 
ATOM   5848  O O     . GLU A  1 812  ? -14.361 81.638  107.132 1.00 27.84 ? 810  GLU A O     1 
ATOM   5849  C CB    . GLU A  1 812  ? -13.801 78.601  107.455 1.00 30.61 ? 810  GLU A CB    1 
ATOM   5850  C CG    . GLU A  1 812  ? -13.063 77.452  108.207 1.00 31.09 ? 810  GLU A CG    1 
ATOM   5851  C CD    . GLU A  1 812  ? -11.914 76.806  107.399 1.00 35.13 ? 810  GLU A CD    1 
ATOM   5852  O OE1   . GLU A  1 812  ? -12.213 76.099  106.413 1.00 38.06 ? 810  GLU A OE1   1 
ATOM   5853  O OE2   . GLU A  1 812  ? -10.711 76.995  107.738 1.00 31.23 ? 810  GLU A OE2   1 
ATOM   5854  N N     . THR A  1 813  ? -13.048 81.287  105.337 1.00 28.11 ? 811  THR A N     1 
ATOM   5855  C CA    . THR A  1 813  ? -13.360 82.555  104.697 1.00 28.20 ? 811  THR A CA    1 
ATOM   5856  C C     . THR A  1 813  ? -13.935 82.263  103.310 1.00 31.74 ? 811  THR A C     1 
ATOM   5857  O O     . THR A  1 813  ? -14.366 81.150  102.988 1.00 30.37 ? 811  THR A O     1 
ATOM   5858  C CB    . THR A  1 813  ? -12.101 83.441  104.724 1.00 29.35 ? 811  THR A CB    1 
ATOM   5859  O OG1   . THR A  1 813  ? -10.978 82.699  104.241 1.00 31.89 ? 811  THR A OG1   1 
ATOM   5860  C CG2   . THR A  1 813  ? -11.818 83.893  106.171 1.00 27.34 ? 811  THR A CG2   1 
ATOM   5861  N N     . GLY A  1 814  ? -13.992 83.275  102.460 1.00 31.69 ? 812  GLY A N     1 
ATOM   5862  C CA    . GLY A  1 814  ? -14.735 83.149  101.226 1.00 33.69 ? 812  GLY A CA    1 
ATOM   5863  C C     . GLY A  1 814  ? -13.997 82.354  100.174 1.00 33.13 ? 812  GLY A C     1 
ATOM   5864  O O     . GLY A  1 814  ? -12.918 81.799  100.391 1.00 33.32 ? 812  GLY A O     1 
ATOM   5865  N N     . GLY A  1 815  ? -14.601 82.301  98.992  1.00 26.50 ? 813  GLY A N     1 
ATOM   5866  C CA    . GLY A  1 815  ? -13.925 81.726  97.849  1.00 28.59 ? 813  GLY A CA    1 
ATOM   5867  C C     . GLY A  1 815  ? -14.386 82.446  96.606  1.00 28.37 ? 813  GLY A C     1 
ATOM   5868  O O     . GLY A  1 815  ? -15.472 83.028  96.574  1.00 33.66 ? 813  GLY A O     1 
ATOM   5869  N N     . GLN A  1 816  ? -13.537 82.419  95.589  1.00 30.66 ? 814  GLN A N     1 
ATOM   5870  C CA    . GLN A  1 816  ? -13.891 82.896  94.257  1.00 31.39 ? 814  GLN A CA    1 
ATOM   5871  C C     . GLN A  1 816  ? -14.049 81.669  93.362  1.00 28.62 ? 814  GLN A C     1 
ATOM   5872  O O     . GLN A  1 816  ? -13.219 81.374  92.497  1.00 26.30 ? 814  GLN A O     1 
ATOM   5873  C CB    . GLN A  1 816  ? -12.817 83.878  93.741  1.00 32.86 ? 814  GLN A CB    1 
ATOM   5874  C CG    . GLN A  1 816  ? -13.233 84.754  92.564  1.00 36.18 ? 814  GLN A CG    1 
ATOM   5875  C CD    . GLN A  1 816  ? -14.233 85.838  92.956  1.00 40.98 ? 814  GLN A CD    1 
ATOM   5876  O OE1   . GLN A  1 816  ? -15.383 85.543  93.272  1.00 40.96 ? 814  GLN A OE1   1 
ATOM   5877  N NE2   . GLN A  1 816  ? -13.795 87.097  92.941  1.00 37.33 ? 814  GLN A NE2   1 
ATOM   5878  N N     . ASN A  1 817  ? -15.132 80.931  93.600  1.00 26.13 ? 815  ASN A N     1 
ATOM   5879  C CA    . ASN A  1 817  ? -15.249 79.559  93.129  1.00 24.63 ? 815  ASN A CA    1 
ATOM   5880  C C     . ASN A  1 817  ? -15.624 79.490  91.657  1.00 24.09 ? 815  ASN A C     1 
ATOM   5881  O O     . ASN A  1 817  ? -16.493 80.225  91.187  1.00 23.90 ? 815  ASN A O     1 
ATOM   5882  C CB    . ASN A  1 817  ? -16.282 78.828  93.971  1.00 22.96 ? 815  ASN A CB    1 
ATOM   5883  C CG    . ASN A  1 817  ? -16.044 79.051  95.442  1.00 24.50 ? 815  ASN A CG    1 
ATOM   5884  O OD1   . ASN A  1 817  ? -14.941 78.810  95.925  1.00 24.60 ? 815  ASN A OD1   1 
ATOM   5885  N ND2   . ASN A  1 817  ? -17.055 79.538  96.156  1.00 22.11 ? 815  ASN A ND2   1 
ATOM   5886  N N     . ALA A  1 818  ? -14.966 78.586  90.939  1.00 24.32 ? 816  ALA A N     1 
ATOM   5887  C CA    . ALA A  1 818  ? -15.130 78.449  89.507  1.00 22.23 ? 816  ALA A CA    1 
ATOM   5888  C C     . ALA A  1 818  ? -15.678 77.078  89.149  1.00 20.85 ? 816  ALA A C     1 
ATOM   5889  O O     . ALA A  1 818  ? -15.529 76.102  89.889  1.00 19.83 ? 816  ALA A O     1 
ATOM   5890  C CB    . ALA A  1 818  ? -13.796 78.664  88.779  1.00 23.89 ? 816  ALA A CB    1 
ATOM   5891  N N     . MET A  1 819  ? -16.307 77.014  87.982  1.00 22.35 ? 817  MET A N     1 
ATOM   5892  C CA    . MET A  1 819  ? -16.681 75.753  87.373  1.00 21.13 ? 817  MET A CA    1 
ATOM   5893  C C     . MET A  1 819  ? -16.206 75.785  85.932  1.00 20.73 ? 817  MET A C     1 
ATOM   5894  O O     . MET A  1 819  ? -16.409 76.786  85.239  1.00 22.83 ? 817  MET A O     1 
ATOM   5895  C CB    . MET A  1 819  ? -18.198 75.529  87.434  1.00 22.84 ? 817  MET A CB    1 
ATOM   5896  C CG    . MET A  1 819  ? -18.648 74.277  86.709  1.00 23.38 ? 817  MET A CG    1 
ATOM   5897  S SD    . MET A  1 819  ? -20.456 74.164  86.614  1.00 27.26 ? 817  MET A SD    1 
ATOM   5898  C CE    . MET A  1 819  ? -20.914 73.758  88.295  1.00 24.49 ? 817  MET A CE    1 
ATOM   5899  N N     . ILE A  1 820  ? -15.555 74.709  85.495  1.00 20.31 ? 818  ILE A N     1 
ATOM   5900  C CA    . ILE A  1 820  ? -15.076 74.577  84.121  1.00 19.31 ? 818  ILE A CA    1 
ATOM   5901  C C     . ILE A  1 820  ? -15.934 73.539  83.406  1.00 20.36 ? 818  ILE A C     1 
ATOM   5902  O O     . ILE A  1 820  ? -16.160 72.444  83.928  1.00 20.90 ? 818  ILE A O     1 
ATOM   5903  C CB    . ILE A  1 820  ? -13.588 74.191  84.070  1.00 20.24 ? 818  ILE A CB    1 
ATOM   5904  C CG1   . ILE A  1 820  ? -12.734 75.311  84.666  1.00 25.26 ? 818  ILE A CG1   1 
ATOM   5905  C CG2   . ILE A  1 820  ? -13.169 73.923  82.613  1.00 24.65 ? 818  ILE A CG2   1 
ATOM   5906  C CD1   . ILE A  1 820  ? -11.213 75.046  84.636  1.00 23.61 ? 818  ILE A CD1   1 
ATOM   5907  N N     . VAL A  1 821  ? -16.428 73.892  82.220  1.00 20.33 ? 819  VAL A N     1 
ATOM   5908  C CA    . VAL A  1 821  ? -17.326 73.049  81.444  1.00 20.98 ? 819  VAL A CA    1 
ATOM   5909  C C     . VAL A  1 821  ? -16.700 72.856  80.077  1.00 23.53 ? 819  VAL A C     1 
ATOM   5910  O O     . VAL A  1 821  ? -16.315 73.838  79.435  1.00 22.94 ? 819  VAL A O     1 
ATOM   5911  C CB    . VAL A  1 821  ? -18.714 73.707  81.297  1.00 21.83 ? 819  VAL A CB    1 
ATOM   5912  C CG1   . VAL A  1 821  ? -19.664 72.854  80.448  1.00 23.42 ? 819  VAL A CG1   1 
ATOM   5913  C CG2   . VAL A  1 821  ? -19.283 73.997  82.652  1.00 20.36 ? 819  VAL A CG2   1 
ATOM   5914  N N     . ASP A  1 822  ? -16.577 71.612  79.632  1.00 24.24 ? 820  ASP A N     1 
ATOM   5915  C CA    . ASP A  1 822  ? -16.004 71.421  78.303  1.00 24.24 ? 820  ASP A CA    1 
ATOM   5916  C C     . ASP A  1 822  ? -17.092 70.947  77.354  1.00 23.04 ? 820  ASP A C     1 
ATOM   5917  O O     . ASP A  1 822  ? -18.250 70.784  77.733  1.00 24.09 ? 820  ASP A O     1 
ATOM   5918  C CB    . ASP A  1 822  ? -14.770 70.495  78.330  1.00 25.06 ? 820  ASP A CB    1 
ATOM   5919  C CG    . ASP A  1 822  ? -15.092 69.012  78.547  1.00 26.06 ? 820  ASP A CG    1 
ATOM   5920  O OD1   . ASP A  1 822  ? -16.262 68.578  78.493  1.00 28.82 ? 820  ASP A OD1   1 
ATOM   5921  O OD2   . ASP A  1 822  ? -14.111 68.244  78.736  1.00 27.41 ? 820  ASP A OD2   1 
ATOM   5922  N N     . SER A  1 823  ? -16.708 70.736  76.095  1.00 27.13 ? 821  SER A N     1 
ATOM   5923  C CA    . SER A  1 823  ? -17.696 70.461  75.068  1.00 26.94 ? 821  SER A CA    1 
ATOM   5924  C C     . SER A  1 823  ? -18.304 69.073  75.189  1.00 27.04 ? 821  SER A C     1 
ATOM   5925  O O     . SER A  1 823  ? -19.249 68.770  74.459  1.00 30.65 ? 821  SER A O     1 
ATOM   5926  C CB    . SER A  1 823  ? -17.062 70.646  73.683  1.00 28.05 ? 821  SER A CB    1 
ATOM   5927  O OG    . SER A  1 823  ? -15.951 69.780  73.538  1.00 30.34 ? 821  SER A OG    1 
ATOM   5928  N N     . SER A  1 824  ? -17.787 68.223  76.070  1.00 23.57 ? 822  SER A N     1 
ATOM   5929  C CA    . SER A  1 824  ? -18.357 66.904  76.288  1.00 24.07 ? 822  SER A CA    1 
ATOM   5930  C C     . SER A  1 824  ? -19.472 66.897  77.326  1.00 29.16 ? 822  SER A C     1 
ATOM   5931  O O     . SER A  1 824  ? -20.208 65.905  77.407  1.00 28.36 ? 822  SER A O     1 
ATOM   5932  C CB    . SER A  1 824  ? -17.262 65.913  76.709  1.00 27.31 ? 822  SER A CB    1 
ATOM   5933  O OG    . SER A  1 824  ? -16.893 66.110  78.065  1.00 26.37 ? 822  SER A OG    1 
ATOM   5934  N N     . ALA A  1 825  ? -19.631 67.972  78.102  1.00 27.44 ? 823  ALA A N     1 
ATOM   5935  C CA    . ALA A  1 825  ? -20.658 68.016  79.136  1.00 27.64 ? 823  ALA A CA    1 
ATOM   5936  C C     . ALA A  1 825  ? -22.049 68.124  78.511  1.00 26.19 ? 823  ALA A C     1 
ATOM   5937  O O     . ALA A  1 825  ? -22.209 68.589  77.386  1.00 27.83 ? 823  ALA A O     1 
ATOM   5938  C CB    . ALA A  1 825  ? -20.420 69.205  80.072  1.00 25.66 ? 823  ALA A CB    1 
ATOM   5939  N N     . LEU A  1 826  ? -23.065 67.685  79.251  1.00 29.57 ? 824  LEU A N     1 
ATOM   5940  C CA    . LEU A  1 826  ? -24.452 67.805  78.795  1.00 29.41 ? 824  LEU A CA    1 
ATOM   5941  C C     . LEU A  1 826  ? -25.019 69.149  79.251  1.00 29.31 ? 824  LEU A C     1 
ATOM   5942  O O     . LEU A  1 826  ? -25.096 69.422  80.459  1.00 28.15 ? 824  LEU A O     1 
ATOM   5943  C CB    . LEU A  1 826  ? -25.313 66.645  79.305  1.00 29.74 ? 824  LEU A CB    1 
ATOM   5944  N N     . ALA A  1 827  ? -25.408 69.981  78.278  1.00 29.01 ? 825  ALA A N     1 
ATOM   5945  C CA    . ALA A  1 827  ? -25.833 71.349  78.558  1.00 28.66 ? 825  ALA A CA    1 
ATOM   5946  C C     . ALA A  1 827  ? -26.923 71.406  79.624  1.00 28.03 ? 825  ALA A C     1 
ATOM   5947  O O     . ALA A  1 827  ? -26.810 72.172  80.588  1.00 25.90 ? 825  ALA A O     1 
ATOM   5948  C CB    . ALA A  1 827  ? -26.299 72.027  77.266  1.00 35.08 ? 825  ALA A CB    1 
ATOM   5949  N N     . GLU A  1 828  ? -27.977 70.592  79.478  1.00 26.41 ? 826  GLU A N     1 
ATOM   5950  C CA    . GLU A  1 828  ? -29.082 70.618  80.436  1.00 27.78 ? 826  GLU A CA    1 
ATOM   5951  C C     . GLU A  1 828  ? -28.595 70.358  81.855  1.00 26.44 ? 826  GLU A C     1 
ATOM   5952  O O     . GLU A  1 828  ? -29.045 71.008  82.809  1.00 26.35 ? 826  GLU A O     1 
ATOM   5953  C CB    . GLU A  1 828  ? -30.142 69.577  80.059  1.00 33.05 ? 826  GLU A CB    1 
ATOM   5954  C CG    . GLU A  1 828  ? -31.051 69.966  78.911  1.00 36.68 ? 826  GLU A CG    1 
ATOM   5955  C CD    . GLU A  1 828  ? -30.398 69.813  77.548  1.00 38.55 ? 826  GLU A CD    1 
ATOM   5956  O OE1   . GLU A  1 828  ? -29.232 69.359  77.476  1.00 37.00 ? 826  GLU A OE1   1 
ATOM   5957  O OE2   . GLU A  1 828  ? -31.063 70.155  76.542  1.00 40.80 ? 826  GLU A OE2   1 
ATOM   5958  N N     . GLN A  1 829  ? -27.680 69.406  82.009  1.00 28.26 ? 827  GLN A N     1 
ATOM   5959  C CA    . GLN A  1 829  ? -27.132 69.080  83.320  1.00 28.79 ? 827  GLN A CA    1 
ATOM   5960  C C     . GLN A  1 829  ? -26.283 70.223  83.864  1.00 27.95 ? 827  GLN A C     1 
ATOM   5961  O O     . GLN A  1 829  ? -26.378 70.575  85.047  1.00 25.21 ? 827  GLN A O     1 
ATOM   5962  C CB    . GLN A  1 829  ? -26.305 67.800  83.202  1.00 31.52 ? 827  GLN A CB    1 
ATOM   5963  C CG    . GLN A  1 829  ? -25.808 67.223  84.497  1.00 35.22 ? 827  GLN A CG    1 
ATOM   5964  C CD    . GLN A  1 829  ? -25.046 65.926  84.272  1.00 40.40 ? 827  GLN A CD    1 
ATOM   5965  O OE1   . GLN A  1 829  ? -24.946 65.436  83.142  1.00 41.54 ? 827  GLN A OE1   1 
ATOM   5966  N NE2   . GLN A  1 829  ? -24.508 65.362  85.346  1.00 41.53 ? 827  GLN A NE2   1 
ATOM   5967  N N     . VAL A  1 830  ? -25.436 70.797  83.012  1.00 25.52 ? 828  VAL A N     1 
ATOM   5968  C CA    . VAL A  1 830  ? -24.627 71.951  83.398  1.00 26.30 ? 828  VAL A CA    1 
ATOM   5969  C C     . VAL A  1 830  ? -25.515 73.096  83.859  1.00 26.51 ? 828  VAL A C     1 
ATOM   5970  O O     . VAL A  1 830  ? -25.283 73.695  84.914  1.00 23.70 ? 828  VAL A O     1 
ATOM   5971  C CB    . VAL A  1 830  ? -23.729 72.389  82.229  1.00 22.00 ? 828  VAL A CB    1 
ATOM   5972  C CG1   . VAL A  1 830  ? -23.143 73.787  82.474  1.00 23.63 ? 828  VAL A CG1   1 
ATOM   5973  C CG2   . VAL A  1 830  ? -22.596 71.360  82.013  1.00 23.96 ? 828  VAL A CG2   1 
ATOM   5974  N N     . VAL A  1 831  ? -26.537 73.430  83.069  1.00 22.88 ? 829  VAL A N     1 
ATOM   5975  C CA    . VAL A  1 831  ? -27.329 74.617  83.387  1.00 22.18 ? 829  VAL A CA    1 
ATOM   5976  C C     . VAL A  1 831  ? -28.029 74.441  84.727  1.00 21.10 ? 829  VAL A C     1 
ATOM   5977  O O     . VAL A  1 831  ? -28.062 75.366  85.551  1.00 23.58 ? 829  VAL A O     1 
ATOM   5978  C CB    . VAL A  1 831  ? -28.324 74.926  82.258  1.00 20.83 ? 829  VAL A CB    1 
ATOM   5979  C CG1   . VAL A  1 831  ? -29.339 75.960  82.724  1.00 20.87 ? 829  VAL A CG1   1 
ATOM   5980  C CG2   . VAL A  1 831  ? -27.574 75.455  81.038  1.00 23.15 ? 829  VAL A CG2   1 
ATOM   5981  N N     . GLY A  1 832  ? -28.580 73.255  84.981  1.00 20.08 ? 830  GLY A N     1 
ATOM   5982  C CA    . GLY A  1 832  ? -29.189 73.021  86.278  1.00 21.83 ? 830  GLY A CA    1 
ATOM   5983  C C     . GLY A  1 832  ? -28.206 73.162  87.427  1.00 24.76 ? 830  GLY A C     1 
ATOM   5984  O O     . GLY A  1 832  ? -28.523 73.759  88.462  1.00 22.76 ? 830  GLY A O     1 
ATOM   5985  N N     . ASP A  1 833  ? -27.010 72.590  87.280  1.00 19.66 ? 831  ASP A N     1 
ATOM   5986  C CA    . ASP A  1 833  ? -26.049 72.692  88.375  1.00 24.26 ? 831  ASP A CA    1 
ATOM   5987  C C     . ASP A  1 833  ? -25.526 74.113  88.517  1.00 20.53 ? 831  ASP A C     1 
ATOM   5988  O O     . ASP A  1 833  ? -25.171 74.540  89.627  1.00 22.32 ? 831  ASP A O     1 
ATOM   5989  C CB    . ASP A  1 833  ? -24.888 71.725  88.156  1.00 23.26 ? 831  ASP A CB    1 
ATOM   5990  C CG    . ASP A  1 833  ? -25.314 70.274  88.263  1.00 26.32 ? 831  ASP A CG    1 
ATOM   5991  O OD1   . ASP A  1 833  ? -26.385 70.010  88.860  1.00 26.75 ? 831  ASP A OD1   1 
ATOM   5992  O OD2   . ASP A  1 833  ? -24.584 69.400  87.749  1.00 25.40 ? 831  ASP A OD2   1 
ATOM   5993  N N     . VAL A  1 834  ? -25.458 74.852  87.407  1.00 20.28 ? 832  VAL A N     1 
ATOM   5994  C CA    . VAL A  1 834  ? -24.982 76.230  87.461  1.00 20.71 ? 832  VAL A CA    1 
ATOM   5995  C C     . VAL A  1 834  ? -26.025 77.125  88.124  1.00 23.00 ? 832  VAL A C     1 
ATOM   5996  O O     . VAL A  1 834  ? -25.704 77.942  88.996  1.00 23.09 ? 832  VAL A O     1 
ATOM   5997  C CB    . VAL A  1 834  ? -24.626 76.721  86.046  1.00 23.40 ? 832  VAL A CB    1 
ATOM   5998  C CG1   . VAL A  1 834  ? -24.459 78.220  86.022  1.00 21.87 ? 832  VAL A CG1   1 
ATOM   5999  C CG2   . VAL A  1 834  ? -23.351 76.025  85.550  1.00 21.26 ? 832  VAL A CG2   1 
ATOM   6000  N N     . ILE A  1 835  ? -27.292 76.973  87.727  1.00 19.37 ? 833  ILE A N     1 
ATOM   6001  C CA    . ILE A  1 835  ? -28.375 77.745  88.333  1.00 22.57 ? 833  ILE A CA    1 
ATOM   6002  C C     . ILE A  1 835  ? -28.417 77.507  89.839  1.00 23.80 ? 833  ILE A C     1 
ATOM   6003  O O     . ILE A  1 835  ? -28.521 78.452  90.630  1.00 25.45 ? 833  ILE A O     1 
ATOM   6004  C CB    . ILE A  1 835  ? -29.725 77.399  87.670  1.00 23.93 ? 833  ILE A CB    1 
ATOM   6005  C CG1   . ILE A  1 835  ? -29.796 77.964  86.247  1.00 23.36 ? 833  ILE A CG1   1 
ATOM   6006  C CG2   . ILE A  1 835  ? -30.892 77.891  88.509  1.00 23.85 ? 833  ILE A CG2   1 
ATOM   6007  C CD1   . ILE A  1 835  ? -29.866 79.465  86.157  1.00 26.58 ? 833  ILE A CD1   1 
ATOM   6008  N N     . THR A  1 836  ? -28.329 76.240  90.259  1.00 21.38 ? 834  THR A N     1 
ATOM   6009  C CA    . THR A  1 836  ? -28.327 75.945  91.696  1.00 26.13 ? 834  THR A CA    1 
ATOM   6010  C C     . THR A  1 836  ? -27.076 76.492  92.383  1.00 24.46 ? 834  THR A C     1 
ATOM   6011  O O     . THR A  1 836  ? -27.168 77.080  93.467  1.00 25.71 ? 834  THR A O     1 
ATOM   6012  C CB    . THR A  1 836  ? -28.431 74.436  91.937  1.00 27.19 ? 834  THR A CB    1 
ATOM   6013  O OG1   . THR A  1 836  ? -29.664 73.946  91.407  1.00 29.72 ? 834  THR A OG1   1 
ATOM   6014  C CG2   . THR A  1 836  ? -28.400 74.130  93.413  1.00 26.77 ? 834  THR A CG2   1 
ATOM   6015  N N     . SER A  1 837  ? -25.897 76.318  91.772  1.00 23.33 ? 835  SER A N     1 
ATOM   6016  C CA    . SER A  1 837  ? -24.653 76.676  92.458  1.00 22.78 ? 835  SER A CA    1 
ATOM   6017  C C     . SER A  1 837  ? -24.525 78.181  92.634  1.00 24.12 ? 835  SER A C     1 
ATOM   6018  O O     . SER A  1 837  ? -24.012 78.656  93.653  1.00 22.83 ? 835  SER A O     1 
ATOM   6019  C CB    . SER A  1 837  ? -23.441 76.137  91.688  1.00 20.27 ? 835  SER A CB    1 
ATOM   6020  O OG    . SER A  1 837  ? -23.364 74.729  91.787  1.00 21.66 ? 835  SER A OG    1 
ATOM   6021  N N     . ALA A  1 838  ? -24.981 78.947  91.651  1.00 20.77 ? 836  ALA A N     1 
ATOM   6022  C CA    . ALA A  1 838  ? -24.772 80.384  91.642  1.00 22.84 ? 836  ALA A CA    1 
ATOM   6023  C C     . ALA A  1 838  ? -25.835 81.147  92.418  1.00 23.65 ? 836  ALA A C     1 
ATOM   6024  O O     . ALA A  1 838  ? -25.519 82.148  93.072  1.00 25.35 ? 836  ALA A O     1 
ATOM   6025  C CB    . ALA A  1 838  ? -24.736 80.896  90.198  1.00 22.07 ? 836  ALA A CB    1 
ATOM   6026  N N     . PHE A  1 839  ? -27.095 80.709  92.350  1.00 23.64 ? 837  PHE A N     1 
ATOM   6027  C CA    . PHE A  1 839  ? -28.212 81.516  92.823  1.00 25.79 ? 837  PHE A CA    1 
ATOM   6028  C C     . PHE A  1 839  ? -28.982 80.928  93.996  1.00 22.34 ? 837  PHE A C     1 
ATOM   6029  O O     . PHE A  1 839  ? -29.746 81.668  94.624  1.00 23.95 ? 837  PHE A O     1 
ATOM   6030  C CB    . PHE A  1 839  ? -29.188 81.789  91.665  1.00 23.13 ? 837  PHE A CB    1 
ATOM   6031  C CG    . PHE A  1 839  ? -28.510 82.353  90.447  1.00 24.75 ? 837  PHE A CG    1 
ATOM   6032  C CD1   . PHE A  1 839  ? -27.692 83.458  90.555  1.00 24.58 ? 837  PHE A CD1   1 
ATOM   6033  C CD2   . PHE A  1 839  ? -28.649 81.745  89.205  1.00 26.72 ? 837  PHE A CD2   1 
ATOM   6034  C CE1   . PHE A  1 839  ? -27.046 83.970  89.453  1.00 26.80 ? 837  PHE A CE1   1 
ATOM   6035  C CE2   . PHE A  1 839  ? -27.995 82.249  88.104  1.00 26.74 ? 837  PHE A CE2   1 
ATOM   6036  C CZ    . PHE A  1 839  ? -27.195 83.370  88.230  1.00 25.46 ? 837  PHE A CZ    1 
ATOM   6037  N N     . ASP A  1 840  ? -28.809 79.645  94.317  1.00 24.78 ? 838  ASP A N     1 
ATOM   6038  C CA    . ASP A  1 840  ? -29.380 79.097  95.545  1.00 25.65 ? 838  ASP A CA    1 
ATOM   6039  C C     . ASP A  1 840  ? -28.950 79.966  96.719  1.00 28.11 ? 838  ASP A C     1 
ATOM   6040  O O     . ASP A  1 840  ? -27.797 80.397  96.784  1.00 23.56 ? 838  ASP A O     1 
ATOM   6041  C CB    . ASP A  1 840  ? -28.895 77.657  95.740  1.00 28.36 ? 838  ASP A CB    1 
ATOM   6042  C CG    . ASP A  1 840  ? -29.384 77.019  97.026  1.00 29.87 ? 838  ASP A CG    1 
ATOM   6043  O OD1   . ASP A  1 840  ? -28.803 77.301  98.099  1.00 29.61 ? 838  ASP A OD1   1 
ATOM   6044  O OD2   . ASP A  1 840  ? -30.332 76.203  96.948  1.00 35.99 ? 838  ASP A OD2   1 
ATOM   6045  N N     . SER A  1 841  ? -29.890 80.253  97.628  1.00 24.73 ? 839  SER A N     1 
ATOM   6046  C CA    . SER A  1 841  ? -29.613 81.093  98.802  1.00 25.14 ? 839  SER A CA    1 
ATOM   6047  C C     . SER A  1 841  ? -29.103 82.466  98.391  1.00 23.51 ? 839  SER A C     1 
ATOM   6048  O O     . SER A  1 841  ? -28.281 83.085  99.086  1.00 26.65 ? 839  SER A O     1 
ATOM   6049  C CB    . SER A  1 841  ? -28.620 80.415  99.751  1.00 29.83 ? 839  SER A CB    1 
ATOM   6050  O OG    . SER A  1 841  ? -29.058 79.103  100.063 1.00 28.18 ? 839  SER A OG    1 
ATOM   6051  N N     . ALA A  1 842  ? -29.585 82.939  97.243  1.00 25.49 ? 840  ALA A N     1 
ATOM   6052  C CA    . ALA A  1 842  ? -29.195 84.235  96.692  1.00 26.46 ? 840  ALA A CA    1 
ATOM   6053  C C     . ALA A  1 842  ? -27.681 84.339  96.585  1.00 22.27 ? 840  ALA A C     1 
ATOM   6054  O O     . ALA A  1 842  ? -27.101 85.408  96.783  1.00 25.86 ? 840  ALA A O     1 
ATOM   6055  C CB    . ALA A  1 842  ? -29.777 85.395  97.517  1.00 25.92 ? 840  ALA A CB    1 
ATOM   6056  N N     . GLY A  1 843  ? -27.032 83.217  96.279  1.00 26.25 ? 841  GLY A N     1 
ATOM   6057  C CA    . GLY A  1 843  ? -25.586 83.210  96.152  1.00 21.24 ? 841  GLY A CA    1 
ATOM   6058  C C     . GLY A  1 843  ? -24.847 83.531  97.426  1.00 25.07 ? 841  GLY A C     1 
ATOM   6059  O O     . GLY A  1 843  ? -23.666 83.886  97.378  1.00 27.30 ? 841  GLY A O     1 
ATOM   6060  N N     . GLN A  1 844  ? -25.515 83.433  98.577  1.00 24.55 ? 842  GLN A N     1 
ATOM   6061  C CA    . GLN A  1 844  ? -24.881 83.745  99.849  1.00 24.29 ? 842  GLN A CA    1 
ATOM   6062  C C     . GLN A  1 844  ? -24.288 82.517  100.518 1.00 30.21 ? 842  GLN A C     1 
ATOM   6063  O O     . GLN A  1 844  ? -24.243 82.449  101.750 1.00 35.00 ? 842  GLN A O     1 
ATOM   6064  C CB    . GLN A  1 844  ? -25.878 84.440  100.777 1.00 25.88 ? 842  GLN A CB    1 
ATOM   6065  C CG    . GLN A  1 844  ? -26.380 85.752  100.210 1.00 26.62 ? 842  GLN A CG    1 
ATOM   6066  C CD    . GLN A  1 844  ? -27.369 86.462  101.125 1.00 26.56 ? 842  GLN A CD    1 
ATOM   6067  O OE1   . GLN A  1 844  ? -27.217 87.645  101.410 1.00 26.05 ? 842  GLN A OE1   1 
ATOM   6068  N NE2   . GLN A  1 844  ? -28.383 85.745  101.579 1.00 27.33 ? 842  GLN A NE2   1 
ATOM   6069  N N     . ARG A  1 845  ? -23.854 81.532  99.737  1.00 28.02 ? 843  ARG A N     1 
ATOM   6070  C CA    . ARG A  1 845  ? -23.057 80.431  100.248 1.00 27.77 ? 843  ARG A CA    1 
ATOM   6071  C C     . ARG A  1 845  ? -21.581 80.742  100.043 1.00 26.25 ? 843  ARG A C     1 
ATOM   6072  O O     . ARG A  1 845  ? -21.197 81.357  99.041  1.00 27.08 ? 843  ARG A O     1 
ATOM   6073  C CB    . ARG A  1 845  ? -23.412 79.124  99.537  1.00 27.89 ? 843  ARG A CB    1 
ATOM   6074  C CG    . ARG A  1 845  ? -24.861 78.691  99.704  1.00 29.99 ? 843  ARG A CG    1 
ATOM   6075  C CD    . ARG A  1 845  ? -25.071 77.345  99.033  1.00 28.17 ? 843  ARG A CD    1 
ATOM   6076  N NE    . ARG A  1 845  ? -26.431 76.851  99.191  1.00 29.02 ? 843  ARG A NE    1 
ATOM   6077  C CZ    . ARG A  1 845  ? -26.774 75.857  99.998  1.00 31.79 ? 843  ARG A CZ    1 
ATOM   6078  N NH1   . ARG A  1 845  ? -25.872 75.215  100.733 1.00 32.41 ? 843  ARG A NH1   1 
ATOM   6079  N NH2   . ARG A  1 845  ? -28.047 75.489  100.061 1.00 34.83 ? 843  ARG A NH2   1 
ATOM   6080  N N     . CYS A  1 846  ? -20.749 80.329  101.003 1.00 27.24 ? 844  CYS A N     1 
ATOM   6081  C CA    . CYS A  1 846  ? -19.306 80.458  100.794 1.00 28.77 ? 844  CYS A CA    1 
ATOM   6082  C C     . CYS A  1 846  ? -18.863 79.657  99.572  1.00 22.98 ? 844  CYS A C     1 
ATOM   6083  O O     . CYS A  1 846  ? -17.932 80.055  98.864  1.00 24.77 ? 844  CYS A O     1 
ATOM   6084  C CB    . CYS A  1 846  ? -18.540 79.990  102.043 1.00 30.28 ? 844  CYS A CB    1 
ATOM   6085  S SG    . CYS A  1 846  ? -19.012 80.826  103.604 1.00 45.41 ? 844  CYS A SG    1 
ATOM   6086  N N     . SER A  1 847  ? -19.546 78.553  99.300  1.00 22.35 ? 845  SER A N     1 
ATOM   6087  C CA    . SER A  1 847  ? -19.260 77.637  98.196  1.00 25.53 ? 845  SER A CA    1 
ATOM   6088  C C     . SER A  1 847  ? -19.834 78.084  96.861  1.00 25.46 ? 845  SER A C     1 
ATOM   6089  O O     . SER A  1 847  ? -19.634 77.375  95.868  1.00 24.68 ? 845  SER A O     1 
ATOM   6090  C CB    . SER A  1 847  ? -19.837 76.259  98.512  1.00 24.23 ? 845  SER A CB    1 
ATOM   6091  O OG    . SER A  1 847  ? -21.215 76.395  98.838  1.00 28.10 ? 845  SER A OG    1 
ATOM   6092  N N     . ALA A  1 848  ? -20.558 79.200  96.815  1.00 23.98 ? 846  ALA A N     1 
ATOM   6093  C CA    . ALA A  1 848  ? -21.367 79.518  95.642  1.00 24.06 ? 846  ALA A CA    1 
ATOM   6094  C C     . ALA A  1 848  ? -20.495 79.685  94.405  1.00 23.21 ? 846  ALA A C     1 
ATOM   6095  O O     . ALA A  1 848  ? -19.330 80.073  94.486  1.00 20.74 ? 846  ALA A O     1 
ATOM   6096  C CB    . ALA A  1 848  ? -22.172 80.790  95.886  1.00 21.98 ? 846  ALA A CB    1 
ATOM   6097  N N     . LEU A  1 849  ? -21.070 79.367  93.255  1.00 20.64 ? 847  LEU A N     1 
ATOM   6098  C CA    . LEU A  1 849  ? -20.365 79.487  91.986  1.00 20.60 ? 847  LEU A CA    1 
ATOM   6099  C C     . LEU A  1 849  ? -20.282 80.954  91.577  1.00 22.26 ? 847  LEU A C     1 
ATOM   6100  O O     . LEU A  1 849  ? -21.310 81.599  91.351  1.00 23.36 ? 847  LEU A O     1 
ATOM   6101  C CB    . LEU A  1 849  ? -21.093 78.683  90.917  1.00 18.48 ? 847  LEU A CB    1 
ATOM   6102  C CG    . LEU A  1 849  ? -20.554 78.826  89.500  1.00 19.86 ? 847  LEU A CG    1 
ATOM   6103  C CD1   . LEU A  1 849  ? -19.111 78.332  89.449  1.00 22.18 ? 847  LEU A CD1   1 
ATOM   6104  C CD2   . LEU A  1 849  ? -21.432 77.989  88.582  1.00 21.31 ? 847  LEU A CD2   1 
ATOM   6105  N N     . ARG A  1 850  ? -19.059 81.473  91.458  1.00 19.14 ? 848  ARG A N     1 
ATOM   6106  C CA    . ARG A  1 850  ? -18.843 82.863  91.085  1.00 24.42 ? 848  ARG A CA    1 
ATOM   6107  C C     . ARG A  1 850  ? -18.425 83.034  89.632  1.00 24.07 ? 848  ARG A C     1 
ATOM   6108  O O     . ARG A  1 850  ? -18.761 84.048  89.024  1.00 24.19 ? 848  ARG A O     1 
ATOM   6109  C CB    . ARG A  1 850  ? -17.764 83.501  91.972  1.00 24.46 ? 848  ARG A CB    1 
ATOM   6110  C CG    . ARG A  1 850  ? -17.988 83.305  93.450  1.00 23.39 ? 848  ARG A CG    1 
ATOM   6111  C CD    . ARG A  1 850  ? -19.366 83.798  93.839  1.00 26.97 ? 848  ARG A CD    1 
ATOM   6112  N NE    . ARG A  1 850  ? -19.567 83.713  95.281  1.00 28.80 ? 848  ARG A NE    1 
ATOM   6113  C CZ    . ARG A  1 850  ? -20.697 84.039  95.894  1.00 29.79 ? 848  ARG A CZ    1 
ATOM   6114  N NH1   . ARG A  1 850  ? -21.765 84.423  95.210  1.00 23.20 ? 848  ARG A NH1   1 
ATOM   6115  N NH2   . ARG A  1 850  ? -20.754 83.985  97.225  1.00 26.79 ? 848  ARG A NH2   1 
ATOM   6116  N N     . VAL A  1 851  ? -17.682 82.087  89.068  1.00 23.27 ? 849  VAL A N     1 
ATOM   6117  C CA    . VAL A  1 851  ? -17.167 82.221  87.710  1.00 25.07 ? 849  VAL A CA    1 
ATOM   6118  C C     . VAL A  1 851  ? -17.408 80.921  86.971  1.00 24.04 ? 849  VAL A C     1 
ATOM   6119  O O     . VAL A  1 851  ? -16.897 79.868  87.379  1.00 24.70 ? 849  VAL A O     1 
ATOM   6120  C CB    . VAL A  1 851  ? -15.674 82.564  87.672  1.00 24.36 ? 849  VAL A CB    1 
ATOM   6121  C CG1   . VAL A  1 851  ? -15.252 82.749  86.221  1.00 27.20 ? 849  VAL A CG1   1 
ATOM   6122  C CG2   . VAL A  1 851  ? -15.394 83.829  88.442  1.00 31.01 ? 849  VAL A CG2   1 
ATOM   6123  N N     . LEU A  1 852  ? -18.156 80.997  85.874  1.00 21.03 ? 850  LEU A N     1 
ATOM   6124  C CA    . LEU A  1 852  ? -18.387 79.855  85.000  1.00 22.45 ? 850  LEU A CA    1 
ATOM   6125  C C     . LEU A  1 852  ? -17.520 80.006  83.756  1.00 20.62 ? 850  LEU A C     1 
ATOM   6126  O O     . LEU A  1 852  ? -17.541 81.058  83.101  1.00 19.49 ? 850  LEU A O     1 
ATOM   6127  C CB    . LEU A  1 852  ? -19.871 79.767  84.621  1.00 19.58 ? 850  LEU A CB    1 
ATOM   6128  C CG    . LEU A  1 852  ? -20.309 78.687  83.633  1.00 22.85 ? 850  LEU A CG    1 
ATOM   6129  C CD1   . LEU A  1 852  ? -20.044 77.276  84.175  1.00 23.30 ? 850  LEU A CD1   1 
ATOM   6130  C CD2   . LEU A  1 852  ? -21.818 78.873  83.275  1.00 20.85 ? 850  LEU A CD2   1 
ATOM   6131  N N     . CYS A  1 853  ? -16.751 78.958  83.445  1.00 22.75 ? 851  CYS A N     1 
ATOM   6132  C CA    . CYS A  1 853  ? -15.793 78.949  82.343  1.00 24.79 ? 851  CYS A CA    1 
ATOM   6133  C C     . CYS A  1 853  ? -16.286 77.944  81.303  1.00 23.68 ? 851  CYS A C     1 
ATOM   6134  O O     . CYS A  1 853  ? -16.333 76.740  81.574  1.00 22.33 ? 851  CYS A O     1 
ATOM   6135  C CB    . CYS A  1 853  ? -14.393 78.580  82.830  1.00 24.40 ? 851  CYS A CB    1 
ATOM   6136  S SG    . CYS A  1 853  ? -13.874 79.444  84.337  1.00 28.61 ? 851  CYS A SG    1 
ATOM   6137  N N     . LEU A  1 854  ? -16.644 78.437  80.121  1.00 23.50 ? 852  LEU A N     1 
ATOM   6138  C CA    . LEU A  1 854  ? -17.300 77.645  79.089  1.00 22.65 ? 852  LEU A CA    1 
ATOM   6139  C C     . LEU A  1 854  ? -16.363 77.450  77.911  1.00 22.37 ? 852  LEU A C     1 
ATOM   6140  O O     . LEU A  1 854  ? -15.871 78.433  77.355  1.00 24.87 ? 852  LEU A O     1 
ATOM   6141  C CB    . LEU A  1 854  ? -18.575 78.342  78.611  1.00 25.41 ? 852  LEU A CB    1 
ATOM   6142  C CG    . LEU A  1 854  ? -19.665 78.515  79.671  1.00 24.21 ? 852  LEU A CG    1 
ATOM   6143  C CD1   . LEU A  1 854  ? -20.909 79.198  79.077  1.00 22.16 ? 852  LEU A CD1   1 
ATOM   6144  C CD2   . LEU A  1 854  ? -20.026 77.163  80.266  1.00 23.01 ? 852  LEU A CD2   1 
ATOM   6145  N N     . GLN A  1 855  ? -16.153 76.200  77.498  1.00 23.31 ? 853  GLN A N     1 
ATOM   6146  C CA    . GLN A  1 855  ? -15.360 75.983  76.295  1.00 23.94 ? 853  GLN A CA    1 
ATOM   6147  C C     . GLN A  1 855  ? -16.004 76.705  75.118  1.00 23.32 ? 853  GLN A C     1 
ATOM   6148  O O     . GLN A  1 855  ? -17.223 76.670  74.936  1.00 27.15 ? 853  GLN A O     1 
ATOM   6149  C CB    . GLN A  1 855  ? -15.201 74.499  75.978  1.00 23.42 ? 853  GLN A CB    1 
ATOM   6150  C CG    . GLN A  1 855  ? -14.130 74.292  74.882  1.00 26.68 ? 853  GLN A CG    1 
ATOM   6151  C CD    . GLN A  1 855  ? -13.975 72.842  74.489  1.00 29.59 ? 853  GLN A CD    1 
ATOM   6152  O OE1   . GLN A  1 855  ? -13.983 71.952  75.341  1.00 26.51 ? 853  GLN A OE1   1 
ATOM   6153  N NE2   . GLN A  1 855  ? -13.843 72.594  73.187  1.00 31.83 ? 853  GLN A NE2   1 
ATOM   6154  N N     . GLU A  1 856  ? -15.161 77.367  74.322  1.00 26.23 ? 854  GLU A N     1 
ATOM   6155  C CA    . GLU A  1 856  ? -15.651 78.324  73.338  1.00 29.86 ? 854  GLU A CA    1 
ATOM   6156  C C     . GLU A  1 856  ? -16.671 77.700  72.393  1.00 30.57 ? 854  GLU A C     1 
ATOM   6157  O O     . GLU A  1 856  ? -17.671 78.335  72.051  1.00 31.06 ? 854  GLU A O     1 
ATOM   6158  C CB    . GLU A  1 856  ? -14.470 78.906  72.558  1.00 31.43 ? 854  GLU A CB    1 
ATOM   6159  C CG    . GLU A  1 856  ? -14.883 79.797  71.395  1.00 37.60 ? 854  GLU A CG    1 
ATOM   6160  C CD    . GLU A  1 856  ? -15.742 80.982  71.825  1.00 43.16 ? 854  GLU A CD    1 
ATOM   6161  O OE1   . GLU A  1 856  ? -15.461 81.582  72.891  1.00 39.18 ? 854  GLU A OE1   1 
ATOM   6162  O OE2   . GLU A  1 856  ? -16.702 81.310  71.098  1.00 40.75 ? 854  GLU A OE2   1 
ATOM   6163  N N     . ASP A  1 857  ? -16.447 76.452  71.970  1.00 30.82 ? 855  ASP A N     1 
ATOM   6164  C CA    . ASP A  1 857  ? -17.327 75.834  70.977  1.00 31.17 ? 855  ASP A CA    1 
ATOM   6165  C C     . ASP A  1 857  ? -18.752 75.593  71.482  1.00 35.63 ? 855  ASP A C     1 
ATOM   6166  O O     . ASP A  1 857  ? -19.661 75.417  70.659  1.00 36.47 ? 855  ASP A O     1 
ATOM   6167  C CB    . ASP A  1 857  ? -16.723 74.512  70.496  1.00 40.06 ? 855  ASP A CB    1 
ATOM   6168  N N     . VAL A  1 858  ? -18.979 75.562  72.797  1.00 29.72 ? 856  VAL A N     1 
ATOM   6169  C CA    . VAL A  1 858  ? -20.317 75.358  73.340  1.00 28.66 ? 856  VAL A CA    1 
ATOM   6170  C C     . VAL A  1 858  ? -20.806 76.537  74.162  1.00 27.54 ? 856  VAL A C     1 
ATOM   6171  O O     . VAL A  1 858  ? -21.917 76.478  74.701  1.00 27.28 ? 856  VAL A O     1 
ATOM   6172  C CB    . VAL A  1 858  ? -20.417 74.059  74.172  1.00 31.33 ? 856  VAL A CB    1 
ATOM   6173  C CG1   . VAL A  1 858  ? -20.268 72.833  73.285  1.00 34.19 ? 856  VAL A CG1   1 
ATOM   6174  C CG2   . VAL A  1 858  ? -19.400 74.051  75.321  1.00 29.22 ? 856  VAL A CG2   1 
ATOM   6175  N N     . ALA A  1 859  ? -20.031 77.620  74.244  1.00 26.29 ? 857  ALA A N     1 
ATOM   6176  C CA    . ALA A  1 859  ? -20.373 78.707  75.157  1.00 24.11 ? 857  ALA A CA    1 
ATOM   6177  C C     . ALA A  1 859  ? -21.689 79.374  74.775  1.00 30.18 ? 857  ALA A C     1 
ATOM   6178  O O     . ALA A  1 859  ? -22.524 79.639  75.644  1.00 27.08 ? 857  ALA A O     1 
ATOM   6179  C CB    . ALA A  1 859  ? -19.252 79.742  75.202  1.00 27.42 ? 857  ALA A CB    1 
ATOM   6180  N N     . ASP A  1 860  ? -21.905 79.656  73.483  1.00 25.92 ? 858  ASP A N     1 
ATOM   6181  C CA    . ASP A  1 860  ? -23.102 80.412  73.125  1.00 29.76 ? 858  ASP A CA    1 
ATOM   6182  C C     . ASP A  1 860  ? -24.362 79.596  73.385  1.00 27.55 ? 858  ASP A C     1 
ATOM   6183  O O     . ASP A  1 860  ? -25.356 80.126  73.892  1.00 29.86 ? 858  ASP A O     1 
ATOM   6184  C CB    . ASP A  1 860  ? -23.037 80.873  71.671  1.00 32.86 ? 858  ASP A CB    1 
ATOM   6185  C CG    . ASP A  1 860  ? -22.142 82.094  71.479  1.00 38.88 ? 858  ASP A CG    1 
ATOM   6186  O OD1   . ASP A  1 860  ? -22.023 82.937  72.397  1.00 39.39 ? 858  ASP A OD1   1 
ATOM   6187  O OD2   . ASP A  1 860  ? -21.555 82.211  70.392  1.00 43.35 ? 858  ASP A OD2   1 
ATOM   6188  N N     . ARG A  1 861  ? -24.324 78.294  73.088  1.00 27.34 ? 859  ARG A N     1 
ATOM   6189  C CA    . ARG A  1 861  ? -25.480 77.449  73.336  1.00 28.17 ? 859  ARG A CA    1 
ATOM   6190  C C     . ARG A  1 861  ? -25.772 77.318  74.829  1.00 25.63 ? 859  ARG A C     1 
ATOM   6191  O O     . ARG A  1 861  ? -26.938 77.378  75.248  1.00 25.83 ? 859  ARG A O     1 
ATOM   6192  C CB    . ARG A  1 861  ? -25.266 76.071  72.714  1.00 31.59 ? 859  ARG A CB    1 
ATOM   6193  C CG    . ARG A  1 861  ? -26.390 75.122  73.034  1.00 35.97 ? 859  ARG A CG    1 
ATOM   6194  C CD    . ARG A  1 861  ? -26.652 74.136  71.925  1.00 44.75 ? 859  ARG A CD    1 
ATOM   6195  N NE    . ARG A  1 861  ? -27.697 73.209  72.339  1.00 51.19 ? 859  ARG A NE    1 
ATOM   6196  C CZ    . ARG A  1 861  ? -27.510 72.217  73.199  1.00 47.94 ? 859  ARG A CZ    1 
ATOM   6197  N NH1   . ARG A  1 861  ? -26.318 71.968  73.718  1.00 43.82 ? 859  ARG A NH1   1 
ATOM   6198  N NH2   . ARG A  1 861  ? -28.547 71.461  73.552  1.00 44.43 ? 859  ARG A NH2   1 
ATOM   6199  N N     . ILE A  1 862  ? -24.738 77.120  75.646  1.00 23.38 ? 860  ILE A N     1 
ATOM   6200  C CA    . ILE A  1 862  ? -24.964 76.964  77.081  1.00 23.57 ? 860  ILE A CA    1 
ATOM   6201  C C     . ILE A  1 862  ? -25.412 78.284  77.698  1.00 26.49 ? 860  ILE A C     1 
ATOM   6202  O O     . ILE A  1 862  ? -26.310 78.318  78.556  1.00 23.73 ? 860  ILE A O     1 
ATOM   6203  C CB    . ILE A  1 862  ? -23.697 76.407  77.757  1.00 26.73 ? 860  ILE A CB    1 
ATOM   6204  C CG1   . ILE A  1 862  ? -23.484 74.939  77.345  1.00 27.33 ? 860  ILE A CG1   1 
ATOM   6205  C CG2   . ILE A  1 862  ? -23.790 76.531  79.273  1.00 23.49 ? 860  ILE A CG2   1 
ATOM   6206  C CD1   . ILE A  1 862  ? -22.159 74.327  77.893  1.00 27.59 ? 860  ILE A CD1   1 
ATOM   6207  N N     . LEU A  1 863  ? -24.835 79.396  77.238  1.00 25.77 ? 861  LEU A N     1 
ATOM   6208  C CA    A LEU A  1 863  ? -25.233 80.699  77.755  0.62 26.06 ? 861  LEU A CA    1 
ATOM   6209  C CA    B LEU A  1 863  ? -25.237 80.696  77.765  0.38 26.07 ? 861  LEU A CA    1 
ATOM   6210  C C     . LEU A  1 863  ? -26.680 81.021  77.399  1.00 24.76 ? 861  LEU A C     1 
ATOM   6211  O O     . LEU A  1 863  ? -27.418 81.573  78.218  1.00 22.82 ? 861  LEU A O     1 
ATOM   6212  C CB    A LEU A  1 863  ? -24.292 81.771  77.218  0.62 26.84 ? 861  LEU A CB    1 
ATOM   6213  C CB    B LEU A  1 863  ? -24.295 81.789  77.266  0.38 26.83 ? 861  LEU A CB    1 
ATOM   6214  C CG    A LEU A  1 863  ? -24.338 83.114  77.920  0.62 27.97 ? 861  LEU A CG    1 
ATOM   6215  C CG    B LEU A  1 863  ? -23.252 82.242  78.287  0.38 28.90 ? 861  LEU A CG    1 
ATOM   6216  C CD1   A LEU A  1 863  ? -24.287 82.898  79.429  0.62 28.07 ? 861  LEU A CD1   1 
ATOM   6217  C CD1   B LEU A  1 863  ? -22.261 83.201  77.657  0.38 30.33 ? 861  LEU A CD1   1 
ATOM   6218  C CD2   A LEU A  1 863  ? -23.178 83.951  77.441  0.62 31.25 ? 861  LEU A CD2   1 
ATOM   6219  C CD2   B LEU A  1 863  ? -23.946 82.877  79.482  0.38 28.17 ? 861  LEU A CD2   1 
ATOM   6220  N N     . THR A  1 864  ? -27.107 80.681  76.179  1.00 24.85 ? 862  THR A N     1 
ATOM   6221  C CA    . THR A  1 864  ? -28.507 80.885  75.809  1.00 24.81 ? 862  THR A CA    1 
ATOM   6222  C C     . THR A  1 864  ? -29.433 80.093  76.721  1.00 23.10 ? 862  THR A C     1 
ATOM   6223  O O     . THR A  1 864  ? -30.414 80.631  77.246  1.00 25.23 ? 862  THR A O     1 
ATOM   6224  C CB    . THR A  1 864  ? -28.712 80.500  74.337  1.00 26.01 ? 862  THR A CB    1 
ATOM   6225  O OG1   . THR A  1 864  ? -28.008 81.435  73.519  1.00 26.64 ? 862  THR A OG1   1 
ATOM   6226  C CG2   . THR A  1 864  ? -30.186 80.494  73.959  1.00 24.55 ? 862  THR A CG2   1 
ATOM   6227  N N     . MET A  1 865  ? -29.115 78.810  76.948  1.00 23.01 ? 863  MET A N     1 
ATOM   6228  C CA    . MET A  1 865  ? -29.917 77.993  77.847  1.00 23.21 ? 863  MET A CA    1 
ATOM   6229  C C     . MET A  1 865  ? -29.871 78.540  79.266  1.00 22.85 ? 863  MET A C     1 
ATOM   6230  O O     . MET A  1 865  ? -30.883 78.538  79.979  1.00 22.22 ? 863  MET A O     1 
ATOM   6231  C CB    . MET A  1 865  ? -29.429 76.543  77.812  1.00 24.32 ? 863  MET A CB    1 
ATOM   6232  C CG    . MET A  1 865  ? -30.269 75.537  78.594  1.00 28.48 ? 863  MET A CG    1 
ATOM   6233  S SD    . MET A  1 865  ? -29.631 73.847  78.374  1.00 35.95 ? 863  MET A SD    1 
ATOM   6234  C CE    . MET A  1 865  ? -29.219 73.953  76.621  1.00 27.66 ? 863  MET A CE    1 
ATOM   6235  N N     . LEU A  1 866  ? -28.707 79.028  79.688  1.00 23.65 ? 864  LEU A N     1 
ATOM   6236  C CA    . LEU A  1 866  ? -28.575 79.531  81.051  1.00 22.57 ? 864  LEU A CA    1 
ATOM   6237  C C     . LEU A  1 866  ? -29.409 80.787  81.257  1.00 22.75 ? 864  LEU A C     1 
ATOM   6238  O O     . LEU A  1 866  ? -30.087 80.931  82.280  1.00 24.37 ? 864  LEU A O     1 
ATOM   6239  C CB    . LEU A  1 866  ? -27.097 79.794  81.341  1.00 22.83 ? 864  LEU A CB    1 
ATOM   6240  C CG    . LEU A  1 866  ? -26.754 80.348  82.709  1.00 25.34 ? 864  LEU A CG    1 
ATOM   6241  C CD1   . LEU A  1 866  ? -27.196 79.309  83.709  1.00 22.92 ? 864  LEU A CD1   1 
ATOM   6242  C CD2   . LEU A  1 866  ? -25.246 80.584  82.799  1.00 25.08 ? 864  LEU A CD2   1 
ATOM   6243  N N     . LYS A  1 867  ? -29.381 81.708  80.293  1.00 22.87 ? 865  LYS A N     1 
ATOM   6244  C CA    . LYS A  1 867  ? -30.179 82.920  80.435  1.00 23.11 ? 865  LYS A CA    1 
ATOM   6245  C C     . LYS A  1 867  ? -31.661 82.580  80.453  1.00 26.60 ? 865  LYS A C     1 
ATOM   6246  O O     . LYS A  1 867  ? -32.440 83.179  81.208  1.00 26.75 ? 865  LYS A O     1 
ATOM   6247  C CB    . LYS A  1 867  ? -29.854 83.899  79.300  1.00 23.45 ? 865  LYS A CB    1 
ATOM   6248  C CG    . LYS A  1 867  ? -28.420 84.436  79.357  1.00 23.17 ? 865  LYS A CG    1 
ATOM   6249  C CD    . LYS A  1 867  ? -28.079 85.278  78.129  1.00 30.31 ? 865  LYS A CD    1 
ATOM   6250  C CE    . LYS A  1 867  ? -26.634 85.795  78.224  1.00 34.33 ? 865  LYS A CE    1 
ATOM   6251  N NZ    . LYS A  1 867  ? -26.132 86.402  76.961  1.00 33.94 ? 865  LYS A NZ    1 
ATOM   6252  N N     . GLY A  1 868  ? -32.065 81.621  79.623  1.00 24.71 ? 866  GLY A N     1 
ATOM   6253  C CA    . GLY A  1 868  ? -33.461 81.222  79.601  1.00 24.59 ? 866  GLY A CA    1 
ATOM   6254  C C     . GLY A  1 868  ? -33.886 80.596  80.908  1.00 22.16 ? 866  GLY A C     1 
ATOM   6255  O O     . GLY A  1 868  ? -34.999 80.828  81.385  1.00 26.49 ? 866  GLY A O     1 
ATOM   6256  N N     . ALA A  1 869  ? -33.003 79.800  81.515  1.00 21.46 ? 867  ALA A N     1 
ATOM   6257  C CA    . ALA A  1 869  ? -33.335 79.192  82.800  1.00 21.58 ? 867  ALA A CA    1 
ATOM   6258  C C     . ALA A  1 869  ? -33.328 80.224  83.919  1.00 24.69 ? 867  ALA A C     1 
ATOM   6259  O O     . ALA A  1 869  ? -34.102 80.109  84.875  1.00 21.81 ? 867  ALA A O     1 
ATOM   6260  C CB    . ALA A  1 869  ? -32.357 78.063  83.123  1.00 22.71 ? 867  ALA A CB    1 
ATOM   6261  N N     . LEU A  1 870  ? -32.450 81.224  83.827  1.00 24.09 ? 868  LEU A N     1 
ATOM   6262  C CA    . LEU A  1 870  ? -32.453 82.309  84.809  1.00 25.55 ? 868  LEU A CA    1 
ATOM   6263  C C     . LEU A  1 870  ? -33.836 82.935  84.944  1.00 24.79 ? 868  LEU A C     1 
ATOM   6264  O O     . LEU A  1 870  ? -34.301 83.234  86.050  1.00 24.48 ? 868  LEU A O     1 
ATOM   6265  C CB    . LEU A  1 870  ? -31.448 83.376  84.384  1.00 24.27 ? 868  LEU A CB    1 
ATOM   6266  C CG    . LEU A  1 870  ? -31.243 84.557  85.322  1.00 26.22 ? 868  LEU A CG    1 
ATOM   6267  C CD1   . LEU A  1 870  ? -30.187 84.181  86.337  1.00 29.48 ? 868  LEU A CD1   1 
ATOM   6268  C CD2   . LEU A  1 870  ? -30.853 85.837  84.556  1.00 30.42 ? 868  LEU A CD2   1 
ATOM   6269  N N     . HIS A  1 871  ? -34.488 83.183  83.821  1.00 22.80 ? 869  HIS A N     1 
ATOM   6270  C CA    . HIS A  1 871  ? -35.760 83.884  83.830  1.00 26.65 ? 869  HIS A CA    1 
ATOM   6271  C C     . HIS A  1 871  ? -36.927 83.021  84.285  1.00 26.03 ? 869  HIS A C     1 
ATOM   6272  O O     . HIS A  1 871  ? -38.054 83.523  84.342  1.00 25.81 ? 869  HIS A O     1 
ATOM   6273  C CB    . HIS A  1 871  ? -36.028 84.461  82.446  1.00 25.29 ? 869  HIS A CB    1 
ATOM   6274  C CG    . HIS A  1 871  ? -35.145 85.627  82.114  1.00 30.19 ? 869  HIS A CG    1 
ATOM   6275  N ND1   . HIS A  1 871  ? -35.320 86.873  82.675  1.00 31.53 ? 869  HIS A ND1   1 
ATOM   6276  C CD2   . HIS A  1 871  ? -34.069 85.730  81.299  1.00 29.29 ? 869  HIS A CD2   1 
ATOM   6277  C CE1   . HIS A  1 871  ? -34.402 87.698  82.206  1.00 32.70 ? 869  HIS A CE1   1 
ATOM   6278  N NE2   . HIS A  1 871  ? -33.628 87.029  81.370  1.00 30.83 ? 869  HIS A NE2   1 
ATOM   6279  N N     . GLU A  1 872  ? -36.694 81.756  84.612  1.00 22.21 ? 870  GLU A N     1 
ATOM   6280  C CA    . GLU A  1 872  ? -37.741 80.894  85.147  1.00 22.09 ? 870  GLU A CA    1 
ATOM   6281  C C     . GLU A  1 872  ? -37.739 80.855  86.667  1.00 25.11 ? 870  GLU A C     1 
ATOM   6282  O O     . GLU A  1 872  ? -38.568 80.150  87.251  1.00 24.21 ? 870  GLU A O     1 
ATOM   6283  C CB    . GLU A  1 872  ? -37.598 79.475  84.589  1.00 23.71 ? 870  GLU A CB    1 
ATOM   6284  C CG    . GLU A  1 872  ? -37.845 79.401  83.077  1.00 26.11 ? 870  GLU A CG    1 
ATOM   6285  C CD    . GLU A  1 872  ? -39.257 79.836  82.700  1.00 27.84 ? 870  GLU A CD    1 
ATOM   6286  O OE1   . GLU A  1 872  ? -40.170 79.719  83.557  1.00 28.89 ? 870  GLU A OE1   1 
ATOM   6287  O OE2   . GLU A  1 872  ? -39.454 80.295  81.550  1.00 31.57 ? 870  GLU A OE2   1 
ATOM   6288  N N     . LEU A  1 873  ? -36.838 81.601  87.309  1.00 25.46 ? 871  LEU A N     1 
ATOM   6289  C CA    . LEU A  1 873  ? -36.701 81.594  88.760  1.00 25.37 ? 871  LEU A CA    1 
ATOM   6290  C C     . LEU A  1 873  ? -37.678 82.585  89.373  1.00 25.24 ? 871  LEU A C     1 
ATOM   6291  O O     . LEU A  1 873  ? -37.876 83.685  88.851  1.00 24.32 ? 871  LEU A O     1 
ATOM   6292  C CB    . LEU A  1 873  ? -35.274 81.963  89.178  1.00 24.70 ? 871  LEU A CB    1 
ATOM   6293  C CG    . LEU A  1 873  ? -34.114 81.066  88.751  1.00 24.22 ? 871  LEU A CG    1 
ATOM   6294  C CD1   . LEU A  1 873  ? -32.776 81.731  89.126  1.00 23.65 ? 871  LEU A CD1   1 
ATOM   6295  C CD2   . LEU A  1 873  ? -34.247 79.698  89.395  1.00 25.72 ? 871  LEU A CD2   1 
ATOM   6296  N N     . HIS A  1 874  ? -38.279 82.192  90.492  1.00 24.47 ? 872  HIS A N     1 
ATOM   6297  C CA    . HIS A  1 874  ? -39.217 83.038  91.218  1.00 25.83 ? 872  HIS A CA    1 
ATOM   6298  C C     . HIS A  1 874  ? -38.491 83.625  92.422  1.00 26.70 ? 872  HIS A C     1 
ATOM   6299  O O     . HIS A  1 874  ? -38.011 82.880  93.279  1.00 25.77 ? 872  HIS A O     1 
ATOM   6300  C CB    . HIS A  1 874  ? -40.439 82.229  91.652  1.00 28.11 ? 872  HIS A CB    1 
ATOM   6301  C CG    . HIS A  1 874  ? -41.470 83.020  92.399  1.00 30.01 ? 872  HIS A CG    1 
ATOM   6302  N ND1   . HIS A  1 874  ? -42.580 82.433  92.970  1.00 33.90 ? 872  HIS A ND1   1 
ATOM   6303  C CD2   . HIS A  1 874  ? -41.571 84.345  92.656  1.00 33.01 ? 872  HIS A CD2   1 
ATOM   6304  C CE1   . HIS A  1 874  ? -43.306 83.360  93.567  1.00 36.18 ? 872  HIS A CE1   1 
ATOM   6305  N NE2   . HIS A  1 874  ? -42.715 84.529  93.390  1.00 31.76 ? 872  HIS A NE2   1 
ATOM   6306  N N     . ILE A  1 875  ? -38.396 84.948  92.471  1.00 26.70 ? 873  ILE A N     1 
ATOM   6307  C CA    . ILE A  1 875  ? -37.712 85.658  93.547  1.00 29.44 ? 873  ILE A CA    1 
ATOM   6308  C C     . ILE A  1 875  ? -38.785 86.327  94.392  1.00 28.41 ? 873  ILE A C     1 
ATOM   6309  O O     . ILE A  1 875  ? -39.667 86.997  93.849  1.00 29.24 ? 873  ILE A O     1 
ATOM   6310  C CB    . ILE A  1 875  ? -36.724 86.711  93.007  1.00 30.24 ? 873  ILE A CB    1 
ATOM   6311  C CG1   . ILE A  1 875  ? -35.396 86.115  92.546  1.00 30.56 ? 873  ILE A CG1   1 
ATOM   6312  C CG2   . ILE A  1 875  ? -36.398 87.739  94.096  1.00 33.57 ? 873  ILE A CG2   1 
ATOM   6313  C CD1   . ILE A  1 875  ? -35.457 84.863  91.734  1.00 32.33 ? 873  ILE A CD1   1 
ATOM   6314  N N     . GLY A  1 876  ? -38.727 86.141  95.705  1.00 27.36 ? 874  GLY A N     1 
ATOM   6315  C CA    . GLY A  1 876  ? -39.677 86.827  96.564  1.00 29.42 ? 874  GLY A CA    1 
ATOM   6316  C C     . GLY A  1 876  ? -39.490 86.432  98.013  1.00 30.47 ? 874  GLY A C     1 
ATOM   6317  O O     . GLY A  1 876  ? -38.522 85.761  98.374  1.00 27.96 ? 874  GLY A O     1 
ATOM   6318  N N     . ARG A  1 877  ? -40.431 86.867  98.851  1.00 30.59 ? 875  ARG A N     1 
ATOM   6319  C CA    . ARG A  1 877  ? -40.379 86.493  100.259 1.00 34.02 ? 875  ARG A CA    1 
ATOM   6320  C C     . ARG A  1 877  ? -40.501 84.981  100.394 1.00 30.97 ? 875  ARG A C     1 
ATOM   6321  O O     . ARG A  1 877  ? -41.329 84.352  99.728  1.00 29.57 ? 875  ARG A O     1 
ATOM   6322  C CB    . ARG A  1 877  ? -41.494 87.189  101.042 1.00 34.17 ? 875  ARG A CB    1 
ATOM   6323  C CG    . ARG A  1 877  ? -41.196 87.315  102.527 1.00 34.50 ? 875  ARG A CG    1 
ATOM   6324  C CD    . ARG A  1 877  ? -42.264 88.142  103.224 1.00 38.00 ? 875  ARG A CD    1 
ATOM   6325  N NE    . ARG A  1 877  ? -43.439 87.365  103.595 1.00 39.82 ? 875  ARG A NE    1 
ATOM   6326  C CZ    . ARG A  1 877  ? -44.489 87.865  104.237 1.00 49.67 ? 875  ARG A CZ    1 
ATOM   6327  N NH1   . ARG A  1 877  ? -44.539 89.141  104.598 1.00 40.43 ? 875  ARG A NH1   1 
ATOM   6328  N NH2   . ARG A  1 877  ? -45.515 87.065  104.525 1.00 47.12 ? 875  ARG A NH2   1 
ATOM   6329  N N     . THR A  1 878  ? -39.675 84.392  101.265 1.00 27.08 ? 876  THR A N     1 
ATOM   6330  C CA    . THR A  1 878  ? -39.465 82.948  101.226 1.00 28.24 ? 876  THR A CA    1 
ATOM   6331  C C     . THR A  1 878  ? -40.474 82.161  102.056 1.00 30.92 ? 876  THR A C     1 
ATOM   6332  O O     . THR A  1 878  ? -40.228 80.988  102.349 1.00 33.73 ? 876  THR A O     1 
ATOM   6333  C CB    . THR A  1 878  ? -38.042 82.583  101.668 1.00 29.92 ? 876  THR A CB    1 
ATOM   6334  O OG1   . THR A  1 878  ? -37.720 83.232  102.906 1.00 31.80 ? 876  THR A OG1   1 
ATOM   6335  C CG2   . THR A  1 878  ? -37.026 82.989  100.608 1.00 29.41 ? 876  THR A CG2   1 
ATOM   6336  N N     . ASP A  1 879  ? -41.603 82.752  102.427 1.00 30.99 ? 877  ASP A N     1 
ATOM   6337  C CA    . ASP A  1 879  ? -42.626 81.970  103.103 1.00 35.15 ? 877  ASP A CA    1 
ATOM   6338  C C     . ASP A  1 879  ? -43.627 81.342  102.123 1.00 33.77 ? 877  ASP A C     1 
ATOM   6339  O O     . ASP A  1 879  ? -44.745 80.988  102.524 1.00 32.43 ? 877  ASP A O     1 
ATOM   6340  C CB    . ASP A  1 879  ? -43.323 82.814  104.177 1.00 36.79 ? 877  ASP A CB    1 
ATOM   6341  C CG    . ASP A  1 879  ? -44.148 83.958  103.609 1.00 39.16 ? 877  ASP A CG    1 
ATOM   6342  O OD1   . ASP A  1 879  ? -43.900 84.398  102.462 1.00 42.52 ? 877  ASP A OD1   1 
ATOM   6343  O OD2   . ASP A  1 879  ? -45.056 84.422  104.332 1.00 42.20 ? 877  ASP A OD2   1 
ATOM   6344  N N     . ARG A  1 880  ? -43.228 81.160  100.862 1.00 29.64 ? 878  ARG A N     1 
ATOM   6345  C CA    . ARG A  1 880  ? -43.988 80.400  99.871  1.00 29.22 ? 878  ARG A CA    1 
ATOM   6346  C C     . ARG A  1 880  ? -43.084 79.344  99.254  1.00 28.94 ? 878  ARG A C     1 
ATOM   6347  O O     . ARG A  1 880  ? -41.957 79.653  98.847  1.00 26.83 ? 878  ARG A O     1 
ATOM   6348  C CB    . ARG A  1 880  ? -44.536 81.291  98.752  1.00 31.68 ? 878  ARG A CB    1 
ATOM   6349  C CG    . ARG A  1 880  ? -45.740 82.151  99.122  1.00 35.74 ? 878  ARG A CG    1 
ATOM   6350  C CD    . ARG A  1 880  ? -45.926 83.238  98.063  1.00 36.42 ? 878  ARG A CD    1 
ATOM   6351  N NE    . ARG A  1 880  ? -47.327 83.614  97.887  1.00 50.46 ? 878  ARG A NE    1 
ATOM   6352  C CZ    . ARG A  1 880  ? -47.993 84.442  98.683  1.00 53.46 ? 878  ARG A CZ    1 
ATOM   6353  N NH1   . ARG A  1 880  ? -47.425 84.977  99.755  1.00 49.90 ? 878  ARG A NH1   1 
ATOM   6354  N NH2   . ARG A  1 880  ? -49.260 84.739  98.400  1.00 51.18 ? 878  ARG A NH2   1 
ATOM   6355  N N     . LEU A  1 881  ? -43.598 78.114  99.151  1.00 26.77 ? 879  LEU A N     1 
ATOM   6356  C CA    . LEU A  1 881  ? -42.841 77.026  98.544  1.00 28.05 ? 879  LEU A CA    1 
ATOM   6357  C C     . LEU A  1 881  ? -42.396 77.373  97.130  1.00 27.79 ? 879  LEU A C     1 
ATOM   6358  O O     . LEU A  1 881  ? -41.335 76.916  96.682  1.00 25.38 ? 879  LEU A O     1 
ATOM   6359  C CB    . LEU A  1 881  ? -43.687 75.752  98.541  1.00 25.80 ? 879  LEU A CB    1 
ATOM   6360  C CG    . LEU A  1 881  ? -43.013 74.478  98.032  1.00 28.51 ? 879  LEU A CG    1 
ATOM   6361  C CD1   . LEU A  1 881  ? -41.984 74.006  99.046  1.00 28.44 ? 879  LEU A CD1   1 
ATOM   6362  C CD2   . LEU A  1 881  ? -44.049 73.416  97.775  1.00 27.68 ? 879  LEU A CD2   1 
ATOM   6363  N N     . SER A  1 882  ? -43.169 78.201  96.427  1.00 27.52 ? 880  SER A N     1 
ATOM   6364  C CA    . SER A  1 882  ? -42.867 78.501  95.031  1.00 30.72 ? 880  SER A CA    1 
ATOM   6365  C C     . SER A  1 882  ? -41.654 79.407  94.849  1.00 27.84 ? 880  SER A C     1 
ATOM   6366  O O     . SER A  1 882  ? -41.172 79.540  93.720  1.00 29.76 ? 880  SER A O     1 
ATOM   6367  C CB    . SER A  1 882  ? -44.077 79.151  94.366  1.00 28.57 ? 880  SER A CB    1 
ATOM   6368  O OG    . SER A  1 882  ? -44.317 80.424  94.930  1.00 30.75 ? 880  SER A OG    1 
ATOM   6369  N N     . VAL A  1 883  ? -41.162 80.048  95.901  1.00 26.43 ? 881  VAL A N     1 
ATOM   6370  C CA    . VAL A  1 883  ? -40.044 80.971  95.751  1.00 26.43 ? 881  VAL A CA    1 
ATOM   6371  C C     . VAL A  1 883  ? -38.745 80.180  95.623  1.00 27.39 ? 881  VAL A C     1 
ATOM   6372  O O     . VAL A  1 883  ? -38.448 79.314  96.449  1.00 26.79 ? 881  VAL A O     1 
ATOM   6373  C CB    . VAL A  1 883  ? -39.987 81.952  96.935  1.00 26.63 ? 881  VAL A CB    1 
ATOM   6374  C CG1   . VAL A  1 883  ? -38.663 82.700  96.933  1.00 25.53 ? 881  VAL A CG1   1 
ATOM   6375  C CG2   . VAL A  1 883  ? -41.148 82.945  96.832  1.00 28.87 ? 881  VAL A CG2   1 
ATOM   6376  N N     . ASP A  1 884  ? -37.962 80.482  94.587  1.00 24.99 ? 882  ASP A N     1 
ATOM   6377  C CA    . ASP A  1 884  ? -36.688 79.795  94.397  1.00 28.13 ? 882  ASP A CA    1 
ATOM   6378  C C     . ASP A  1 884  ? -35.540 80.502  95.092  1.00 26.87 ? 882  ASP A C     1 
ATOM   6379  O O     . ASP A  1 884  ? -34.615 79.844  95.595  1.00 26.05 ? 882  ASP A O     1 
ATOM   6380  C CB    . ASP A  1 884  ? -36.366 79.688  92.907  1.00 26.73 ? 882  ASP A CB    1 
ATOM   6381  C CG    . ASP A  1 884  ? -37.441 78.948  92.140  1.00 29.26 ? 882  ASP A CG    1 
ATOM   6382  O OD1   . ASP A  1 884  ? -37.711 77.784  92.505  1.00 29.48 ? 882  ASP A OD1   1 
ATOM   6383  O OD2   . ASP A  1 884  ? -38.021 79.542  91.191  1.00 26.92 ? 882  ASP A OD2   1 
ATOM   6384  N N     . VAL A  1 885  ? -35.569 81.830  95.085  1.00 23.52 ? 883  VAL A N     1 
ATOM   6385  C CA    . VAL A  1 885  ? -34.460 82.660  95.544  1.00 25.26 ? 883  VAL A CA    1 
ATOM   6386  C C     . VAL A  1 885  ? -35.016 83.754  96.436  1.00 25.10 ? 883  VAL A C     1 
ATOM   6387  O O     . VAL A  1 885  ? -35.922 84.492  96.034  1.00 25.30 ? 883  VAL A O     1 
ATOM   6388  C CB    . VAL A  1 885  ? -33.687 83.279  94.371  1.00 28.55 ? 883  VAL A CB    1 
ATOM   6389  C CG1   . VAL A  1 885  ? -32.579 84.191  94.889  1.00 26.44 ? 883  VAL A CG1   1 
ATOM   6390  C CG2   . VAL A  1 885  ? -33.151 82.204  93.457  1.00 26.15 ? 883  VAL A CG2   1 
ATOM   6391  N N     . GLY A  1 886  ? -34.456 83.883  97.629  1.00 26.77 ? 884  GLY A N     1 
ATOM   6392  C CA    . GLY A  1 886  ? -34.940 84.860  98.566  1.00 23.14 ? 884  GLY A CA    1 
ATOM   6393  C C     . GLY A  1 886  ? -34.143 86.141  98.549  1.00 27.53 ? 884  GLY A C     1 
ATOM   6394  O O     . GLY A  1 886  ? -33.441 86.465  97.588  1.00 26.94 ? 884  GLY A O     1 
ATOM   6395  N N     . PRO A  1 887  ? -34.234 86.895  99.636  1.00 26.52 ? 885  PRO A N     1 
ATOM   6396  C CA    . PRO A  1 887  ? -33.523 88.169  99.722  1.00 27.46 ? 885  PRO A CA    1 
ATOM   6397  C C     . PRO A  1 887  ? -32.086 87.983  100.181 1.00 28.19 ? 885  PRO A C     1 
ATOM   6398  O O     . PRO A  1 887  ? -31.711 86.964  100.765 1.00 27.42 ? 885  PRO A O     1 
ATOM   6399  C CB    . PRO A  1 887  ? -34.326 88.937  100.775 1.00 30.84 ? 885  PRO A CB    1 
ATOM   6400  C CG    . PRO A  1 887  ? -34.799 87.834  101.711 1.00 27.33 ? 885  PRO A CG    1 
ATOM   6401  C CD    . PRO A  1 887  ? -35.034 86.616  100.844 1.00 28.99 ? 885  PRO A CD    1 
ATOM   6402  N N     . VAL A  1 888  ? -31.286 89.011  99.921  1.00 29.84 ? 886  VAL A N     1 
ATOM   6403  C CA    . VAL A  1 888  ? -29.977 89.086  100.541 1.00 29.49 ? 886  VAL A CA    1 
ATOM   6404  C C     . VAL A  1 888  ? -30.134 89.683  101.938 1.00 29.07 ? 886  VAL A C     1 
ATOM   6405  O O     . VAL A  1 888  ? -31.169 90.266  102.278 1.00 29.72 ? 886  VAL A O     1 
ATOM   6406  C CB    . VAL A  1 888  ? -28.981 89.876  99.669  1.00 25.21 ? 886  VAL A CB    1 
ATOM   6407  C CG1   . VAL A  1 888  ? -28.883 89.238  98.281  1.00 23.37 ? 886  VAL A CG1   1 
ATOM   6408  C CG2   . VAL A  1 888  ? -29.381 91.320  99.524  1.00 26.38 ? 886  VAL A CG2   1 
ATOM   6409  N N     . ILE A  1 889  ? -29.104 89.511  102.764 1.00 28.79 ? 887  ILE A N     1 
ATOM   6410  C CA    . ILE A  1 889  ? -29.305 89.568  104.215 1.00 30.39 ? 887  ILE A CA    1 
ATOM   6411  C C     . ILE A  1 889  ? -29.619 90.986  104.706 1.00 30.81 ? 887  ILE A C     1 
ATOM   6412  O O     . ILE A  1 889  ? -30.398 91.153  105.654 1.00 32.99 ? 887  ILE A O     1 
ATOM   6413  C CB    . ILE A  1 889  ? -28.088 88.969  104.944 1.00 30.89 ? 887  ILE A CB    1 
ATOM   6414  C CG1   . ILE A  1 889  ? -28.365 88.852  106.448 1.00 32.33 ? 887  ILE A CG1   1 
ATOM   6415  C CG2   . ILE A  1 889  ? -26.826 89.796  104.686 1.00 30.19 ? 887  ILE A CG2   1 
ATOM   6416  C CD1   . ILE A  1 889  ? -29.402 87.788  106.794 1.00 29.54 ? 887  ILE A CD1   1 
ATOM   6417  N N     . THR A  1 890  ? -29.011 92.024  104.114 1.00 29.53 ? 888  THR A N     1 
ATOM   6418  C CA    . THR A  1 890  ? -29.217 93.404  104.573 1.00 30.95 ? 888  THR A CA    1 
ATOM   6419  C C     . THR A  1 890  ? -29.238 94.382  103.405 1.00 32.00 ? 888  THR A C     1 
ATOM   6420  O O     . THR A  1 890  ? -28.822 94.072  102.284 1.00 29.55 ? 888  THR A O     1 
ATOM   6421  C CB    . THR A  1 890  ? -28.107 93.901  105.511 1.00 33.84 ? 888  THR A CB    1 
ATOM   6422  O OG1   . THR A  1 890  ? -26.860 93.835  104.805 1.00 32.48 ? 888  THR A OG1   1 
ATOM   6423  C CG2   . THR A  1 890  ? -28.037 93.088  106.798 1.00 33.49 ? 888  THR A CG2   1 
ATOM   6424  N N     . SER A  1 891  ? -29.651 95.613  103.715 1.00 32.35 ? 889  SER A N     1 
ATOM   6425  C CA    . SER A  1 891  ? -29.558 96.691  102.740 1.00 32.15 ? 889  SER A CA    1 
ATOM   6426  C C     . SER A  1 891  ? -28.111 96.981  102.364 1.00 34.69 ? 889  SER A C     1 
ATOM   6427  O O     . SER A  1 891  ? -27.840 97.374  101.225 1.00 34.22 ? 889  SER A O     1 
ATOM   6428  C CB    . SER A  1 891  ? -30.242 97.954  103.283 1.00 36.27 ? 889  SER A CB    1 
ATOM   6429  N N     . GLU A  1 892  ? -27.169 96.788  103.297 1.00 36.84 ? 890  GLU A N     1 
ATOM   6430  C CA    . GLU A  1 892  ? -25.759 97.032  103.000 1.00 37.22 ? 890  GLU A CA    1 
ATOM   6431  C C     . GLU A  1 892  ? -25.219 96.001  102.011 1.00 36.38 ? 890  GLU A C     1 
ATOM   6432  O O     . GLU A  1 892  ? -24.475 96.342  101.077 1.00 33.76 ? 890  GLU A O     1 
ATOM   6433  C CB    . GLU A  1 892  ? -24.924 97.015  104.293 1.00 36.49 ? 890  GLU A CB    1 
ATOM   6434  C CG    . GLU A  1 892  ? -25.423 97.928  105.421 1.00 46.44 ? 890  GLU A CG    1 
ATOM   6435  C CD    . GLU A  1 892  ? -26.581 97.325  106.227 1.00 44.71 ? 890  GLU A CD    1 
ATOM   6436  O OE1   . GLU A  1 892  ? -27.714 97.272  105.705 1.00 45.86 ? 890  GLU A OE1   1 
ATOM   6437  O OE2   . GLU A  1 892  ? -26.358 96.899  107.382 1.00 55.03 ? 890  GLU A OE2   1 
ATOM   6438  N N     . ALA A  1 893  ? -25.546 94.723  102.231 1.00 31.58 ? 891  ALA A N     1 
ATOM   6439  C CA    . ALA A  1 893  ? -25.158 93.684  101.280 1.00 30.01 ? 891  ALA A CA    1 
ATOM   6440  C C     . ALA A  1 893  ? -25.724 93.991  99.904  1.00 32.34 ? 891  ALA A C     1 
ATOM   6441  O O     . ALA A  1 893  ? -25.011 93.931  98.896  1.00 32.03 ? 891  ALA A O     1 
ATOM   6442  C CB    . ALA A  1 893  ? -25.639 92.317  101.766 1.00 28.34 ? 891  ALA A CB    1 
ATOM   6443  N N     . LYS A  1 894  ? -27.014 94.341  99.855  1.00 28.88 ? 892  LYS A N     1 
ATOM   6444  C CA    . LYS A  1 894  ? -27.667 94.709  98.603  1.00 32.50 ? 892  LYS A CA    1 
ATOM   6445  C C     . LYS A  1 894  ? -26.919 95.829  97.890  1.00 34.74 ? 892  LYS A C     1 
ATOM   6446  O O     . LYS A  1 894  ? -26.574 95.704  96.709  1.00 32.75 ? 892  LYS A O     1 
ATOM   6447  C CB    . LYS A  1 894  ? -29.113 95.124  98.880  1.00 27.41 ? 892  LYS A CB    1 
ATOM   6448  C CG    . LYS A  1 894  ? -29.918 95.416  97.634  1.00 28.43 ? 892  LYS A CG    1 
ATOM   6449  C CD    . LYS A  1 894  ? -31.269 96.017  97.994  1.00 33.11 ? 892  LYS A CD    1 
ATOM   6450  C CE    . LYS A  1 894  ? -32.032 96.431  96.754  1.00 33.33 ? 892  LYS A CE    1 
ATOM   6451  N NZ    . LYS A  1 894  ? -33.255 97.188  97.115  1.00 40.23 ? 892  LYS A NZ    1 
ATOM   6452  N N     . ASP A  1 895  ? -26.651 96.934  98.602  1.00 35.50 ? 893  ASP A N     1 
ATOM   6453  C CA    . ASP A  1 895  ? -25.966 98.067  97.984  1.00 36.53 ? 893  ASP A CA    1 
ATOM   6454  C C     . ASP A  1 895  ? -24.588 97.662  97.484  1.00 33.94 ? 893  ASP A C     1 
ATOM   6455  O O     . ASP A  1 895  ? -24.173 98.054  96.385  1.00 35.47 ? 893  ASP A O     1 
ATOM   6456  C CB    . ASP A  1 895  ? -25.834 99.228  98.975  1.00 38.16 ? 893  ASP A CB    1 
ATOM   6457  C CG    . ASP A  1 895  ? -27.174 99.754  99.468  1.00 48.26 ? 893  ASP A CG    1 
ATOM   6458  O OD1   . ASP A  1 895  ? -28.209 99.508  98.806  1.00 50.28 ? 893  ASP A OD1   1 
ATOM   6459  O OD2   . ASP A  1 895  ? -27.185 100.440 100.524 1.00 50.32 ? 893  ASP A OD2   1 
ATOM   6460  N N     . ASN A  1 896  ? -23.861 96.887  98.282  1.00 31.47 ? 894  ASN A N     1 
ATOM   6461  C CA    . ASN A  1 896  ? -22.539 96.441  97.867  1.00 32.11 ? 894  ASN A CA    1 
ATOM   6462  C C     . ASN A  1 896  ? -22.613 95.622  96.584  1.00 34.53 ? 894  ASN A C     1 
ATOM   6463  O O     . ASN A  1 896  ? -21.811 95.822  95.662  1.00 32.20 ? 894  ASN A O     1 
ATOM   6464  C CB    . ASN A  1 896  ? -21.894 95.636  98.991  1.00 34.59 ? 894  ASN A CB    1 
ATOM   6465  C CG    . ASN A  1 896  ? -20.521 95.115  98.620  1.00 42.42 ? 894  ASN A CG    1 
ATOM   6466  O OD1   . ASN A  1 896  ? -20.377 93.986  98.154  1.00 43.35 ? 894  ASN A OD1   1 
ATOM   6467  N ND2   . ASN A  1 896  ? -19.503 95.939  98.824  1.00 43.72 ? 894  ASN A ND2   1 
ATOM   6468  N N     . ILE A  1 897  ? -23.582 94.703  96.504  1.00 31.73 ? 895  ILE A N     1 
ATOM   6469  C CA    . ILE A  1 897  ? -23.722 93.847  95.327  1.00 32.46 ? 895  ILE A CA    1 
ATOM   6470  C C     . ILE A  1 897  ? -24.146 94.663  94.112  1.00 33.49 ? 895  ILE A C     1 
ATOM   6471  O O     . ILE A  1 897  ? -23.617 94.484  93.007  1.00 32.12 ? 895  ILE A O     1 
ATOM   6472  C CB    . ILE A  1 897  ? -24.724 92.717  95.616  1.00 29.46 ? 895  ILE A CB    1 
ATOM   6473  C CG1   . ILE A  1 897  ? -24.217 91.845  96.764  1.00 30.15 ? 895  ILE A CG1   1 
ATOM   6474  C CG2   . ILE A  1 897  ? -24.984 91.887  94.361  1.00 31.38 ? 895  ILE A CG2   1 
ATOM   6475  C CD1   . ILE A  1 897  ? -25.296 90.985  97.381  1.00 29.20 ? 895  ILE A CD1   1 
ATOM   6476  N N     . GLU A  1 898  ? -25.106 95.569  94.289  1.00 31.06 ? 896  GLU A N     1 
ATOM   6477  C CA    . GLU A  1 898  ? -25.560 96.362  93.156  1.00 33.35 ? 896  GLU A CA    1 
ATOM   6478  C C     . GLU A  1 898  ? -24.478 97.309  92.655  1.00 36.99 ? 896  GLU A C     1 
ATOM   6479  O O     . GLU A  1 898  ? -24.403 97.568  91.450  1.00 36.03 ? 896  GLU A O     1 
ATOM   6480  C CB    . GLU A  1 898  ? -26.840 97.106  93.531  1.00 35.14 ? 896  GLU A CB    1 
ATOM   6481  C CG    . GLU A  1 898  ? -28.006 96.138  93.706  1.00 35.48 ? 896  GLU A CG    1 
ATOM   6482  C CD    . GLU A  1 898  ? -29.330 96.809  94.075  1.00 42.02 ? 896  GLU A CD    1 
ATOM   6483  O OE1   . GLU A  1 898  ? -29.310 97.903  94.680  1.00 44.92 ? 896  GLU A OE1   1 
ATOM   6484  O OE2   . GLU A  1 898  ? -30.392 96.225  93.760  1.00 45.63 ? 896  GLU A OE2   1 
ATOM   6485  N N     . LYS A  1 899  ? -23.619 97.820  93.546  1.00 33.43 ? 897  LYS A N     1 
ATOM   6486  C CA    . LYS A  1 899  ? -22.535 98.678  93.090  1.00 35.23 ? 897  LYS A CA    1 
ATOM   6487  C C     . LYS A  1 899  ? -21.605 97.917  92.154  1.00 36.47 ? 897  LYS A C     1 
ATOM   6488  O O     . LYS A  1 899  ? -21.127 98.471  91.158  1.00 38.95 ? 897  LYS A O     1 
ATOM   6489  C CB    . LYS A  1 899  ? -21.761 99.247  94.287  1.00 36.94 ? 897  LYS A CB    1 
ATOM   6490  N N     . HIS A  1 900  ? -21.355 96.637  92.447  1.00 35.22 ? 898  HIS A N     1 
ATOM   6491  C CA    . HIS A  1 900  ? -20.535 95.814  91.561  1.00 36.95 ? 898  HIS A CA    1 
ATOM   6492  C C     . HIS A  1 900  ? -21.193 95.645  90.200  1.00 33.21 ? 898  HIS A C     1 
ATOM   6493  O O     . HIS A  1 900  ? -20.553 95.839  89.160  1.00 35.84 ? 898  HIS A O     1 
ATOM   6494  C CB    . HIS A  1 900  ? -20.279 94.452  92.194  1.00 36.44 ? 898  HIS A CB    1 
ATOM   6495  C CG    . HIS A  1 900  ? -19.619 93.477  91.272  1.00 36.95 ? 898  HIS A CG    1 
ATOM   6496  N ND1   . HIS A  1 900  ? -18.259 93.470  91.050  1.00 35.36 ? 898  HIS A ND1   1 
ATOM   6497  C CD2   . HIS A  1 900  ? -20.132 92.486  90.506  1.00 37.10 ? 898  HIS A CD2   1 
ATOM   6498  C CE1   . HIS A  1 900  ? -17.961 92.509  90.192  1.00 37.72 ? 898  HIS A CE1   1 
ATOM   6499  N NE2   . HIS A  1 900  ? -19.078 91.895  89.849  1.00 35.45 ? 898  HIS A NE2   1 
ATOM   6500  N N     . ILE A  1 901  ? -22.480 95.285  90.189  1.00 31.89 ? 899  ILE A N     1 
ATOM   6501  C CA    . ILE A  1 901  ? -23.184 95.068  88.927  1.00 34.39 ? 899  ILE A CA    1 
ATOM   6502  C C     . ILE A  1 901  ? -23.159 96.325  88.068  1.00 34.33 ? 899  ILE A C     1 
ATOM   6503  O O     . ILE A  1 901  ? -22.969 96.258  86.848  1.00 35.37 ? 899  ILE A O     1 
ATOM   6504  C CB    . ILE A  1 901  ? -24.629 94.604  89.193  1.00 32.95 ? 899  ILE A CB    1 
ATOM   6505  C CG1   . ILE A  1 901  ? -24.610 93.283  89.972  1.00 30.67 ? 899  ILE A CG1   1 
ATOM   6506  C CG2   . ILE A  1 901  ? -25.382 94.479  87.875  1.00 31.18 ? 899  ILE A CG2   1 
ATOM   6507  C CD1   . ILE A  1 901  ? -25.964 92.859  90.550  1.00 29.91 ? 899  ILE A CD1   1 
ATOM   6508  N N     . GLU A  1 902  ? -23.358 97.489  88.684  1.00 36.16 ? 900  GLU A N     1 
ATOM   6509  C CA    . GLU A  1 902  ? -23.382 98.714  87.895  1.00 39.50 ? 900  GLU A CA    1 
ATOM   6510  C C     . GLU A  1 902  ? -21.999 99.073  87.365  1.00 38.03 ? 900  GLU A C     1 
ATOM   6511  O O     . GLU A  1 902  ? -21.888 99.620  86.262  1.00 39.53 ? 900  GLU A O     1 
ATOM   6512  C CB    . GLU A  1 902  ? -23.981 99.851  88.718  1.00 38.62 ? 900  GLU A CB    1 
ATOM   6513  C CG    . GLU A  1 902  ? -25.475 99.659  88.928  1.00 43.87 ? 900  GLU A CG    1 
ATOM   6514  C CD    . GLU A  1 902  ? -26.205 99.327  87.623  1.00 46.97 ? 900  GLU A CD    1 
ATOM   6515  O OE1   . GLU A  1 902  ? -26.057 100.097 86.644  1.00 46.92 ? 900  GLU A OE1   1 
ATOM   6516  O OE2   . GLU A  1 902  ? -26.913 98.291  87.572  1.00 43.43 ? 900  GLU A OE2   1 
ATOM   6517  N N     . ARG A  1 903  ? -20.938 98.763  88.114  1.00 37.41 ? 901  ARG A N     1 
ATOM   6518  C CA    . ARG A  1 903  ? -19.593 98.969  87.588  1.00 40.92 ? 901  ARG A CA    1 
ATOM   6519  C C     . ARG A  1 903  ? -19.371 98.136  86.334  1.00 39.77 ? 901  ARG A C     1 
ATOM   6520  O O     . ARG A  1 903  ? -18.947 98.659  85.295  1.00 35.32 ? 901  ARG A O     1 
ATOM   6521  C CB    . ARG A  1 903  ? -18.545 98.636  88.650  1.00 42.59 ? 901  ARG A CB    1 
ATOM   6522  C CG    . ARG A  1 903  ? -18.308 99.763  89.642  1.00 46.81 ? 901  ARG A CG    1 
ATOM   6523  C CD    . ARG A  1 903  ? -17.055 99.545  90.489  1.00 48.76 ? 901  ARG A CD    1 
ATOM   6524  N NE    . ARG A  1 903  ? -17.161 98.402  91.393  1.00 55.15 ? 901  ARG A NE    1 
ATOM   6525  C CZ    . ARG A  1 903  ? -17.828 98.401  92.541  1.00 49.13 ? 901  ARG A CZ    1 
ATOM   6526  N NH1   . ARG A  1 903  ? -18.535 99.451  92.932  1.00 52.48 ? 901  ARG A NH1   1 
ATOM   6527  N NH2   . ARG A  1 903  ? -17.774 97.325  93.322  1.00 41.66 ? 901  ARG A NH2   1 
ATOM   6528  N N     . MET A  1 904  ? -19.677 96.833  86.416  1.00 36.58 ? 902  MET A N     1 
ATOM   6529  C CA    . MET A  1 904  ? -19.566 95.952  85.255  1.00 38.02 ? 902  MET A CA    1 
ATOM   6530  C C     . MET A  1 904  ? -20.427 96.443  84.102  1.00 37.47 ? 902  MET A C     1 
ATOM   6531  O O     . MET A  1 904  ? -19.997 96.406  82.943  1.00 37.29 ? 902  MET A O     1 
ATOM   6532  C CB    . MET A  1 904  ? -19.960 94.521  85.625  1.00 34.78 ? 902  MET A CB    1 
ATOM   6533  C CG    . MET A  1 904  ? -19.096 93.865  86.683  1.00 37.01 ? 902  MET A CG    1 
ATOM   6534  S SD    . MET A  1 904  ? -17.396 93.661  86.140  1.00 42.45 ? 902  MET A SD    1 
ATOM   6535  C CE    . MET A  1 904  ? -16.602 95.049  86.964  1.00 45.28 ? 902  MET A CE    1 
ATOM   6536  N N     . ARG A  1 905  ? -21.656 96.885  84.394  1.00 34.53 ? 903  ARG A N     1 
ATOM   6537  C CA    A ARG A  1 905  ? -22.501 97.422  83.335  0.53 36.56 ? 903  ARG A CA    1 
ATOM   6538  C CA    B ARG A  1 905  ? -22.500 97.419  83.334  0.47 36.57 ? 903  ARG A CA    1 
ATOM   6539  C C     . ARG A  1 905  ? -21.876 98.670  82.729  1.00 38.72 ? 903  ARG A C     1 
ATOM   6540  O O     . ARG A  1 905  ? -21.880 98.845  81.505  1.00 39.05 ? 903  ARG A O     1 
ATOM   6541  C CB    A ARG A  1 905  ? -23.903 97.726  83.867  0.53 37.71 ? 903  ARG A CB    1 
ATOM   6542  C CB    B ARG A  1 905  ? -23.907 97.708  83.867  0.47 37.71 ? 903  ARG A CB    1 
ATOM   6543  C CG    A ARG A  1 905  ? -24.951 97.823  82.774  0.53 38.49 ? 903  ARG A CG    1 
ATOM   6544  C CG    B ARG A  1 905  ? -24.975 97.761  82.785  0.47 38.49 ? 903  ARG A CG    1 
ATOM   6545  C CD    A ARG A  1 905  ? -26.270 98.388  83.285  0.53 38.30 ? 903  ARG A CD    1 
ATOM   6546  C CD    B ARG A  1 905  ? -26.387 97.910  83.360  0.47 38.41 ? 903  ARG A CD    1 
ATOM   6547  N NE    A ARG A  1 905  ? -26.727 97.742  84.510  0.53 37.91 ? 903  ARG A NE    1 
ATOM   6548  N NE    B ARG A  1 905  ? -27.236 96.757  83.071  0.47 38.17 ? 903  ARG A NE    1 
ATOM   6549  C CZ    A ARG A  1 905  ? -27.441 96.625  84.550  0.53 38.45 ? 903  ARG A CZ    1 
ATOM   6550  C CZ    B ARG A  1 905  ? -27.937 96.091  83.982  0.47 37.81 ? 903  ARG A CZ    1 
ATOM   6551  N NH1   A ARG A  1 905  ? -27.741 95.955  83.449  0.53 37.61 ? 903  ARG A NH1   1 
ATOM   6552  N NH1   B ARG A  1 905  ? -27.916 96.437  85.259  0.47 38.01 ? 903  ARG A NH1   1 
ATOM   6553  N NH2   A ARG A  1 905  ? -27.867 96.170  85.726  0.53 38.07 ? 903  ARG A NH2   1 
ATOM   6554  N NH2   B ARG A  1 905  ? -28.689 95.061  83.599  0.47 37.11 ? 903  ARG A NH2   1 
ATOM   6555  N N     . GLY A  1 906  ? -21.317 99.542  83.571  1.00 39.23 ? 904  GLY A N     1 
ATOM   6556  C CA    . GLY A  1 906  ? -20.688 100.751 83.077  1.00 38.12 ? 904  GLY A CA    1 
ATOM   6557  C C     . GLY A  1 906  ? -19.448 100.496 82.244  1.00 41.80 ? 904  GLY A C     1 
ATOM   6558  O O     . GLY A  1 906  ? -19.072 101.352 81.437  1.00 44.91 ? 904  GLY A O     1 
ATOM   6559  N N     . LEU A  1 907  ? -18.811 99.336  82.414  1.00 41.66 ? 905  LEU A N     1 
ATOM   6560  C CA    . LEU A  1 907  ? -17.670 98.951  81.589  1.00 41.91 ? 905  LEU A CA    1 
ATOM   6561  C C     . LEU A  1 907  ? -18.076 98.312  80.265  1.00 41.67 ? 905  LEU A C     1 
ATOM   6562  O O     . LEU A  1 907  ? -17.197 97.928  79.486  1.00 43.68 ? 905  LEU A O     1 
ATOM   6563  C CB    . LEU A  1 907  ? -16.766 97.995  82.359  1.00 40.29 ? 905  LEU A CB    1 
ATOM   6564  C CG    . LEU A  1 907  ? -16.116 98.588  83.604  1.00 44.05 ? 905  LEU A CG    1 
ATOM   6565  C CD1   . LEU A  1 907  ? -15.412 97.502  84.414  1.00 39.65 ? 905  LEU A CD1   1 
ATOM   6566  C CD2   . LEU A  1 907  ? -15.153 99.710  83.222  1.00 44.86 ? 905  LEU A CD2   1 
ATOM   6567  N N     . GLY A  1 908  ? -19.371 98.198  79.993  1.00 39.62 ? 906  GLY A N     1 
ATOM   6568  C CA    . GLY A  1 908  ? -19.850 97.632  78.752  1.00 41.14 ? 906  GLY A CA    1 
ATOM   6569  C C     . GLY A  1 908  ? -19.994 96.128  78.751  1.00 37.85 ? 906  GLY A C     1 
ATOM   6570  O O     . GLY A  1 908  ? -20.251 95.553  77.688  1.00 40.94 ? 906  GLY A O     1 
ATOM   6571  N N     . ARG A  1 909  ? -19.840 95.472  79.900  1.00 37.80 ? 907  ARG A N     1 
ATOM   6572  C CA    . ARG A  1 909  ? -20.062 94.033  79.980  1.00 37.82 ? 907  ARG A CA    1 
ATOM   6573  C C     . ARG A  1 909  ? -21.545 93.708  79.817  1.00 37.56 ? 907  ARG A C     1 
ATOM   6574  O O     . ARG A  1 909  ? -22.415 94.458  80.271  1.00 38.50 ? 907  ARG A O     1 
ATOM   6575  C CB    . ARG A  1 909  ? -19.551 93.498  81.318  1.00 37.80 ? 907  ARG A CB    1 
ATOM   6576  C CG    . ARG A  1 909  ? -18.132 93.911  81.639  1.00 39.44 ? 907  ARG A CG    1 
ATOM   6577  C CD    . ARG A  1 909  ? -17.138 92.984  80.972  1.00 45.94 ? 907  ARG A CD    1 
ATOM   6578  N NE    . ARG A  1 909  ? -15.803 93.566  80.859  1.00 50.50 ? 907  ARG A NE    1 
ATOM   6579  C CZ    . ARG A  1 909  ? -14.993 93.824  81.880  1.00 52.81 ? 907  ARG A CZ    1 
ATOM   6580  N NH1   . ARG A  1 909  ? -15.360 93.597  83.132  1.00 55.03 ? 907  ARG A NH1   1 
ATOM   6581  N NH2   . ARG A  1 909  ? -13.785 94.329  81.639  1.00 54.99 ? 907  ARG A NH2   1 
ATOM   6582  N N     . LYS A  1 910  ? -21.839 92.581  79.167  1.00 32.70 ? 908  LYS A N     1 
ATOM   6583  C CA    . LYS A  1 910  ? -23.225 92.150  79.037  1.00 34.70 ? 908  LYS A CA    1 
ATOM   6584  C C     . LYS A  1 910  ? -23.746 91.679  80.388  1.00 32.32 ? 908  LYS A C     1 
ATOM   6585  O O     . LYS A  1 910  ? -23.105 90.865  81.060  1.00 31.35 ? 908  LYS A O     1 
ATOM   6586  C CB    . LYS A  1 910  ? -23.363 91.027  78.008  1.00 36.96 ? 908  LYS A CB    1 
ATOM   6587  C CG    . LYS A  1 910  ? -23.233 91.459  76.567  1.00 39.36 ? 908  LYS A CG    1 
ATOM   6588  C CD    . LYS A  1 910  ? -23.595 90.318  75.615  1.00 42.87 ? 908  LYS A CD    1 
ATOM   6589  C CE    . LYS A  1 910  ? -25.063 89.945  75.729  1.00 47.75 ? 908  LYS A CE    1 
ATOM   6590  N NZ    . LYS A  1 910  ? -25.526 89.155  74.544  1.00 51.93 ? 908  LYS A NZ    1 
ATOM   6591  N N     . VAL A  1 911  ? -24.915 92.184  80.779  1.00 30.31 ? 909  VAL A N     1 
ATOM   6592  C CA    . VAL A  1 911  ? -25.507 91.897  82.083  1.00 28.40 ? 909  VAL A CA    1 
ATOM   6593  C C     . VAL A  1 911  ? -26.936 91.444  81.853  1.00 30.23 ? 909  VAL A C     1 
ATOM   6594  O O     . VAL A  1 911  ? -27.737 92.180  81.255  1.00 31.07 ? 909  VAL A O     1 
ATOM   6595  C CB    . VAL A  1 911  ? -25.483 93.118  83.021  1.00 31.76 ? 909  VAL A CB    1 
ATOM   6596  C CG1   . VAL A  1 911  ? -26.210 92.788  84.340  1.00 32.11 ? 909  VAL A CG1   1 
ATOM   6597  C CG2   . VAL A  1 911  ? -24.053 93.561  83.293  1.00 30.38 ? 909  VAL A CG2   1 
ATOM   6598  N N     . GLU A  1 912  ? -27.253 90.240  82.313  1.00 26.39 ? 910  GLU A N     1 
ATOM   6599  C CA    . GLU A  1 912  ? -28.593 89.680  82.233  1.00 29.33 ? 910  GLU A CA    1 
ATOM   6600  C C     . GLU A  1 912  ? -29.168 89.647  83.642  1.00 29.78 ? 910  GLU A C     1 
ATOM   6601  O O     . GLU A  1 912  ? -28.516 89.153  84.560  1.00 28.73 ? 910  GLU A O     1 
ATOM   6602  C CB    . GLU A  1 912  ? -28.557 88.267  81.634  1.00 30.46 ? 910  GLU A CB    1 
ATOM   6603  C CG    . GLU A  1 912  ? -29.926 87.666  81.322  1.00 30.21 ? 910  GLU A CG    1 
ATOM   6604  C CD    . GLU A  1 912  ? -30.548 88.218  80.049  1.00 32.55 ? 910  GLU A CD    1 
ATOM   6605  O OE1   . GLU A  1 912  ? -29.826 88.855  79.271  1.00 34.31 ? 910  GLU A OE1   1 
ATOM   6606  O OE2   . GLU A  1 912  ? -31.761 88.001  79.823  1.00 35.92 ? 910  GLU A OE2   1 
ATOM   6607  N N     . GLN A  1 913  ? -30.366 90.194  83.824  1.00 28.27 ? 911  GLN A N     1 
ATOM   6608  C CA    . GLN A  1 913  ? -31.006 90.166  85.133  1.00 30.35 ? 911  GLN A CA    1 
ATOM   6609  C C     . GLN A  1 913  ? -32.479 89.845  84.970  1.00 33.60 ? 911  GLN A C     1 
ATOM   6610  O O     . GLN A  1 913  ? -33.116 90.338  84.039  1.00 30.21 ? 911  GLN A O     1 
ATOM   6611  C CB    . GLN A  1 913  ? -30.885 91.514  85.860  1.00 32.37 ? 911  GLN A CB    1 
ATOM   6612  C CG    . GLN A  1 913  ? -29.477 91.998  86.090  1.00 33.63 ? 911  GLN A CG    1 
ATOM   6613  C CD    . GLN A  1 913  ? -29.452 93.197  87.008  1.00 32.93 ? 911  GLN A CD    1 
ATOM   6614  O OE1   . GLN A  1 913  ? -29.962 94.265  86.668  1.00 35.32 ? 911  GLN A OE1   1 
ATOM   6615  N NE2   . GLN A  1 913  ? -28.888 93.020  88.187  1.00 30.04 ? 911  GLN A NE2   1 
ATOM   6616  N N     . ILE A  1 914  ? -33.025 89.043  85.884  1.00 33.38 ? 912  ILE A N     1 
ATOM   6617  C CA    . ILE A  1 914  ? -34.471 88.845  85.894  1.00 35.77 ? 912  ILE A CA    1 
ATOM   6618  C C     . ILE A  1 914  ? -35.136 90.071  86.501  1.00 38.20 ? 912  ILE A C     1 
ATOM   6619  O O     . ILE A  1 914  ? -34.581 90.743  87.380  1.00 35.24 ? 912  ILE A O     1 
ATOM   6620  C CB    . ILE A  1 914  ? -34.879 87.570  86.659  1.00 36.60 ? 912  ILE A CB    1 
ATOM   6621  C CG1   . ILE A  1 914  ? -34.817 87.805  88.160  1.00 37.86 ? 912  ILE A CG1   1 
ATOM   6622  C CG2   . ILE A  1 914  ? -33.982 86.417  86.329  1.00 33.94 ? 912  ILE A CG2   1 
ATOM   6623  C CD1   . ILE A  1 914  ? -35.251 86.613  88.918  1.00 38.36 ? 912  ILE A CD1   1 
ATOM   6624  N N     . GLY A  1 915  ? -36.334 90.379  86.016  1.00 39.28 ? 913  GLY A N     1 
ATOM   6625  C CA    . GLY A  1 915  ? -37.103 91.456  86.611  1.00 38.58 ? 913  GLY A CA    1 
ATOM   6626  C C     . GLY A  1 915  ? -37.681 91.016  87.943  1.00 38.76 ? 913  GLY A C     1 
ATOM   6627  O O     . GLY A  1 915  ? -38.038 89.852  88.134  1.00 46.31 ? 913  GLY A O     1 
ATOM   6628  N N     . LEU A  1 916  ? -37.754 91.954  88.880  1.00 35.87 ? 914  LEU A N     1 
ATOM   6629  C CA    . LEU A  1 916  ? -38.255 91.677  90.220  1.00 40.67 ? 914  LEU A CA    1 
ATOM   6630  C C     . LEU A  1 916  ? -39.686 92.165  90.356  1.00 39.52 ? 914  LEU A C     1 
ATOM   6631  O O     . LEU A  1 916  ? -40.052 93.197  89.791  1.00 36.68 ? 914  LEU A O     1 
ATOM   6632  C CB    . LEU A  1 916  ? -37.388 92.344  91.286  1.00 38.32 ? 914  LEU A CB    1 
ATOM   6633  C CG    . LEU A  1 916  ? -36.000 91.732  91.452  1.00 39.84 ? 914  LEU A CG    1 
ATOM   6634  C CD1   . LEU A  1 916  ? -35.444 92.083  92.815  1.00 38.68 ? 914  LEU A CD1   1 
ATOM   6635  C CD2   . LEU A  1 916  ? -36.067 90.226  91.257  1.00 37.68 ? 914  LEU A CD2   1 
ATOM   6636  N N     . ALA A  1 917  ? -40.490 91.420  91.108  1.00 40.05 ? 915  ALA A N     1 
ATOM   6637  C CA    . ALA A  1 917  ? -41.862 91.840  91.341  1.00 44.10 ? 915  ALA A CA    1 
ATOM   6638  C C     . ALA A  1 917  ? -41.886 93.034  92.292  1.00 44.33 ? 915  ALA A C     1 
ATOM   6639  O O     . ALA A  1 917  ? -40.919 93.310  93.007  1.00 41.92 ? 915  ALA A O     1 
ATOM   6640  C CB    . ALA A  1 917  ? -42.692 90.684  91.902  1.00 49.05 ? 915  ALA A CB    1 
ATOM   6641  N N     . SER A  1 918  ? -43.015 93.754  92.291  1.00 42.49 ? 916  SER A N     1 
ATOM   6642  C CA    . SER A  1 918  ? -43.123 94.949  93.123  1.00 43.19 ? 916  SER A CA    1 
ATOM   6643  C C     . SER A  1 918  ? -43.110 94.610  94.611  1.00 43.33 ? 916  SER A C     1 
ATOM   6644  O O     . SER A  1 918  ? -42.701 95.441  95.427  1.00 43.29 ? 916  SER A O     1 
ATOM   6645  C CB    . SER A  1 918  ? -44.397 95.725  92.773  1.00 46.83 ? 916  SER A CB    1 
ATOM   6646  O OG    . SER A  1 918  ? -45.542 95.034  93.248  1.00 49.56 ? 916  SER A OG    1 
ATOM   6647  N N     . GLU A  1 919  ? -43.552 93.402  94.978  1.00 42.70 ? 917  GLU A N     1 
ATOM   6648  C CA    . GLU A  1 919  ? -43.583 93.006  96.384  1.00 46.71 ? 917  GLU A CA    1 
ATOM   6649  C C     . GLU A  1 919  ? -42.191 92.979  97.007  1.00 44.21 ? 917  GLU A C     1 
ATOM   6650  O O     . GLU A  1 919  ? -42.057 93.155  98.223  1.00 44.64 ? 917  GLU A O     1 
ATOM   6651  C CB    . GLU A  1 919  ? -44.237 91.630  96.538  1.00 49.08 ? 917  GLU A CB    1 
ATOM   6652  C CG    . GLU A  1 919  ? -45.757 91.630  96.428  1.00 52.26 ? 917  GLU A CG    1 
ATOM   6653  C CD    . GLU A  1 919  ? -46.266 91.618  94.990  1.00 57.12 ? 917  GLU A CD    1 
ATOM   6654  O OE1   . GLU A  1 919  ? -45.503 91.980  94.065  1.00 55.06 ? 917  GLU A OE1   1 
ATOM   6655  O OE2   . GLU A  1 919  ? -47.441 91.238  94.788  1.00 62.90 ? 917  GLU A OE2   1 
ATOM   6656  N N     . THR A  1 920  ? -41.145 92.753  96.211  1.00 39.96 ? 918  THR A N     1 
ATOM   6657  C CA    . THR A  1 920  ? -39.809 92.742  96.792  1.00 40.36 ? 918  THR A CA    1 
ATOM   6658  C C     . THR A  1 920  ? -39.431 94.089  97.395  1.00 38.12 ? 918  THR A C     1 
ATOM   6659  O O     . THR A  1 920  ? -38.424 94.166  98.102  1.00 37.35 ? 918  THR A O     1 
ATOM   6660  C CB    . THR A  1 920  ? -38.766 92.326  95.748  1.00 36.74 ? 918  THR A CB    1 
ATOM   6661  O OG1   . THR A  1 920  ? -38.821 93.214  94.626  1.00 37.67 ? 918  THR A OG1   1 
ATOM   6662  C CG2   . THR A  1 920  ? -39.010 90.889  95.281  1.00 33.85 ? 918  THR A CG2   1 
ATOM   6663  N N     . GLY A  1 921  ? -40.236 95.134  97.169  1.00 40.89 ? 919  GLY A N     1 
ATOM   6664  C CA    . GLY A  1 921  ? -39.880 96.465  97.631  1.00 39.46 ? 919  GLY A CA    1 
ATOM   6665  C C     . GLY A  1 921  ? -39.715 96.578  99.135  1.00 38.52 ? 919  GLY A C     1 
ATOM   6666  O O     . GLY A  1 921  ? -38.924 97.397  99.614  1.00 38.08 ? 919  GLY A O     1 
ATOM   6667  N N     . VAL A  1 922  ? -40.436 95.753  99.901  1.00 36.35 ? 920  VAL A N     1 
ATOM   6668  C CA    . VAL A  1 922  ? -40.395 95.866  101.359 1.00 36.77 ? 920  VAL A CA    1 
ATOM   6669  C C     . VAL A  1 922  ? -39.220 95.131  101.981 1.00 36.48 ? 920  VAL A C     1 
ATOM   6670  O O     . VAL A  1 922  ? -39.031 95.213  103.202 1.00 37.31 ? 920  VAL A O     1 
ATOM   6671  C CB    . VAL A  1 922  ? -41.700 95.349  101.995 1.00 38.56 ? 920  VAL A CB    1 
ATOM   6672  C CG1   . VAL A  1 922  ? -42.853 96.319  101.724 1.00 37.54 ? 920  VAL A CG1   1 
ATOM   6673  C CG2   . VAL A  1 922  ? -42.013 93.978  101.460 1.00 39.76 ? 920  VAL A CG2   1 
ATOM   6674  N N     . GLY A  1 923  ? -38.427 94.416  101.185 1.00 34.57 ? 921  GLY A N     1 
ATOM   6675  C CA    . GLY A  1 923  ? -37.236 93.747  101.673 1.00 35.63 ? 921  GLY A CA    1 
ATOM   6676  C C     . GLY A  1 923  ? -36.000 94.132  100.888 1.00 34.34 ? 921  GLY A C     1 
ATOM   6677  O O     . GLY A  1 923  ? -36.021 95.098  100.121 1.00 32.10 ? 921  GLY A O     1 
ATOM   6678  N N     . THR A  1 924  ? -34.912 93.395  101.063 1.00 32.60 ? 922  THR A N     1 
ATOM   6679  C CA    . THR A  1 924  ? -33.651 93.719  100.404 1.00 30.26 ? 922  THR A CA    1 
ATOM   6680  C C     . THR A  1 924  ? -33.334 92.595  99.411  1.00 28.58 ? 922  THR A C     1 
ATOM   6681  O O     . THR A  1 924  ? -32.766 91.566  99.785  1.00 26.44 ? 922  THR A O     1 
ATOM   6682  C CB    . THR A  1 924  ? -32.544 93.922  101.444 1.00 29.77 ? 922  THR A CB    1 
ATOM   6683  O OG1   . THR A  1 924  ? -32.468 92.776  102.298 1.00 29.94 ? 922  THR A OG1   1 
ATOM   6684  C CG2   . THR A  1 924  ? -32.834 95.149  102.302 1.00 35.11 ? 922  THR A CG2   1 
ATOM   6685  N N     . PHE A  1 925  ? -33.686 92.791  98.138  1.00 26.55 ? 923  PHE A N     1 
ATOM   6686  C CA    . PHE A  1 925  ? -33.486 91.744  97.134  1.00 28.94 ? 923  PHE A CA    1 
ATOM   6687  C C     . PHE A  1 925  ? -32.501 92.182  96.051  1.00 27.63 ? 923  PHE A C     1 
ATOM   6688  O O     . PHE A  1 925  ? -32.499 93.344  95.621  1.00 31.87 ? 923  PHE A O     1 
ATOM   6689  C CB    . PHE A  1 925  ? -34.813 91.345  96.468  1.00 30.79 ? 923  PHE A CB    1 
ATOM   6690  C CG    . PHE A  1 925  ? -35.765 90.602  97.375  1.00 29.48 ? 923  PHE A CG    1 
ATOM   6691  C CD1   . PHE A  1 925  ? -36.595 91.288  98.235  1.00 29.15 ? 923  PHE A CD1   1 
ATOM   6692  C CD2   . PHE A  1 925  ? -35.845 89.220  97.338  1.00 27.47 ? 923  PHE A CD2   1 
ATOM   6693  C CE1   . PHE A  1 925  ? -37.492 90.609  99.054  1.00 31.66 ? 923  PHE A CE1   1 
ATOM   6694  C CE2   . PHE A  1 925  ? -36.725 88.543  98.153  1.00 28.14 ? 923  PHE A CE2   1 
ATOM   6695  C CZ    . PHE A  1 925  ? -37.556 89.245  99.012  1.00 27.00 ? 923  PHE A CZ    1 
ATOM   6696  N N     . VAL A  1 926  ? -31.693 91.241  95.579  1.00 27.48 ? 924  VAL A N     1 
ATOM   6697  C CA    . VAL A  1 926  ? -30.882 91.420  94.383  1.00 29.75 ? 924  VAL A CA    1 
ATOM   6698  C C     . VAL A  1 926  ? -31.333 90.382  93.370  1.00 27.06 ? 924  VAL A C     1 
ATOM   6699  O O     . VAL A  1 926  ? -31.368 89.192  93.691  1.00 27.38 ? 924  VAL A O     1 
ATOM   6700  C CB    . VAL A  1 926  ? -29.373 91.282  94.662  1.00 26.38 ? 924  VAL A CB    1 
ATOM   6701  C CG1   . VAL A  1 926  ? -28.591 91.311  93.367  1.00 28.66 ? 924  VAL A CG1   1 
ATOM   6702  C CG2   . VAL A  1 926  ? -28.904 92.422  95.572  1.00 28.13 ? 924  VAL A CG2   1 
ATOM   6703  N N     . PRO A  1 927  ? -31.694 90.772  92.151  1.00 29.14 ? 925  PRO A N     1 
ATOM   6704  C CA    . PRO A  1 927  ? -32.105 89.780  91.153  1.00 29.58 ? 925  PRO A CA    1 
ATOM   6705  C C     . PRO A  1 927  ? -30.919 88.942  90.715  1.00 27.56 ? 925  PRO A C     1 
ATOM   6706  O O     . PRO A  1 927  ? -29.800 89.464  90.570  1.00 24.67 ? 925  PRO A O     1 
ATOM   6707  C CB    . PRO A  1 927  ? -32.647 90.638  90.002  1.00 31.25 ? 925  PRO A CB    1 
ATOM   6708  C CG    . PRO A  1 927  ? -31.957 91.945  90.151  1.00 32.37 ? 925  PRO A CG    1 
ATOM   6709  C CD    . PRO A  1 927  ? -31.721 92.145  91.621  1.00 27.99 ? 925  PRO A CD    1 
ATOM   6710  N N     . PRO A  1 928  ? -31.109 87.632  90.555  1.00 25.92 ? 926  PRO A N     1 
ATOM   6711  C CA    . PRO A  1 928  ? -30.065 86.804  89.947  1.00 26.69 ? 926  PRO A CA    1 
ATOM   6712  C C     . PRO A  1 928  ? -29.584 87.421  88.643  1.00 25.69 ? 926  PRO A C     1 
ATOM   6713  O O     . PRO A  1 928  ? -30.377 87.902  87.831  1.00 24.39 ? 926  PRO A O     1 
ATOM   6714  C CB    . PRO A  1 928  ? -30.766 85.464  89.724  1.00 25.56 ? 926  PRO A CB    1 
ATOM   6715  C CG    . PRO A  1 928  ? -31.763 85.410  90.865  1.00 28.87 ? 926  PRO A CG    1 
ATOM   6716  C CD    . PRO A  1 928  ? -32.262 86.832  91.005  1.00 28.15 ? 926  PRO A CD    1 
ATOM   6717  N N     . THR A  1 929  ? -28.264 87.425  88.467  1.00 26.87 ? 927  THR A N     1 
ATOM   6718  C CA    . THR A  1 929  ? -27.605 88.247  87.464  1.00 28.07 ? 927  THR A CA    1 
ATOM   6719  C C     . THR A  1 929  ? -26.506 87.427  86.803  1.00 23.82 ? 927  THR A C     1 
ATOM   6720  O O     . THR A  1 929  ? -25.802 86.687  87.481  1.00 25.84 ? 927  THR A O     1 
ATOM   6721  C CB    . THR A  1 929  ? -27.005 89.508  88.118  1.00 27.03 ? 927  THR A CB    1 
ATOM   6722  O OG1   . THR A  1 929  ? -28.054 90.303  88.682  1.00 29.52 ? 927  THR A OG1   1 
ATOM   6723  C CG2   . THR A  1 929  ? -26.219 90.361  87.102  1.00 29.11 ? 927  THR A CG2   1 
ATOM   6724  N N     . ILE A  1 930  ? -26.357 87.566  85.486  1.00 26.28 ? 928  ILE A N     1 
ATOM   6725  C CA    . ILE A  1 930  ? -25.265 86.944  84.742  1.00 22.70 ? 928  ILE A CA    1 
ATOM   6726  C C     . ILE A  1 930  ? -24.449 88.057  84.102  1.00 25.42 ? 928  ILE A C     1 
ATOM   6727  O O     . ILE A  1 930  ? -25.004 88.937  83.432  1.00 28.80 ? 928  ILE A O     1 
ATOM   6728  C CB    . ILE A  1 930  ? -25.780 85.946  83.683  1.00 25.75 ? 928  ILE A CB    1 
ATOM   6729  C CG1   . ILE A  1 930  ? -26.613 84.847  84.348  1.00 25.88 ? 928  ILE A CG1   1 
ATOM   6730  C CG2   . ILE A  1 930  ? -24.597 85.322  82.911  1.00 24.88 ? 928  ILE A CG2   1 
ATOM   6731  C CD1   . ILE A  1 930  ? -27.412 83.935  83.342  1.00 23.91 ? 928  ILE A CD1   1 
ATOM   6732  N N     . ILE A  1 931  ? -23.144 88.039  84.343  1.00 24.26 ? 929  ILE A N     1 
ATOM   6733  C CA    . ILE A  1 931  ? -22.234 89.047  83.823  1.00 25.68 ? 929  ILE A CA    1 
ATOM   6734  C C     . ILE A  1 931  ? -21.187 88.336  82.981  1.00 26.99 ? 929  ILE A C     1 
ATOM   6735  O O     . ILE A  1 931  ? -20.522 87.410  83.461  1.00 27.11 ? 929  ILE A O     1 
ATOM   6736  C CB    . ILE A  1 931  ? -21.580 89.853  84.955  1.00 27.18 ? 929  ILE A CB    1 
ATOM   6737  C CG1   . ILE A  1 931  ? -22.663 90.576  85.772  1.00 29.24 ? 929  ILE A CG1   1 
ATOM   6738  C CG2   . ILE A  1 931  ? -20.533 90.821  84.372  1.00 28.31 ? 929  ILE A CG2   1 
ATOM   6739  C CD1   . ILE A  1 931  ? -22.102 91.480  86.870  1.00 28.31 ? 929  ILE A CD1   1 
ATOM   6740  N N     . GLU A  1 932  ? -21.042 88.757  81.731  1.00 27.62 ? 930  GLU A N     1 
ATOM   6741  C CA    . GLU A  1 932  ? -20.081 88.139  80.828  1.00 27.45 ? 930  GLU A CA    1 
ATOM   6742  C C     . GLU A  1 932  ? -18.778 88.929  80.875  1.00 27.65 ? 930  GLU A C     1 
ATOM   6743  O O     . GLU A  1 932  ? -18.760 90.132  80.581  1.00 29.04 ? 930  GLU A O     1 
ATOM   6744  C CB    . GLU A  1 932  ? -20.649 88.067  79.412  1.00 29.81 ? 930  GLU A CB    1 
ATOM   6745  C CG    . GLU A  1 932  ? -21.831 87.089  79.312  1.00 27.57 ? 930  GLU A CG    1 
ATOM   6746  C CD    . GLU A  1 932  ? -22.585 87.198  77.997  1.00 33.12 ? 930  GLU A CD    1 
ATOM   6747  O OE1   . GLU A  1 932  ? -21.930 87.150  76.933  1.00 35.40 ? 930  GLU A OE1   1 
ATOM   6748  O OE2   . GLU A  1 932  ? -23.832 87.334  78.032  1.00 32.97 ? 930  GLU A OE2   1 
ATOM   6749  N N     . LEU A  1 933  ? -17.703 88.264  81.273  1.00 29.94 ? 931  LEU A N     1 
ATOM   6750  C CA    . LEU A  1 933  ? -16.399 88.892  81.418  1.00 29.58 ? 931  LEU A CA    1 
ATOM   6751  C C     . LEU A  1 933  ? -15.487 88.499  80.267  1.00 35.96 ? 931  LEU A C     1 
ATOM   6752  O O     . LEU A  1 933  ? -15.707 87.494  79.587  1.00 33.71 ? 931  LEU A O     1 
ATOM   6753  C CB    . LEU A  1 933  ? -15.744 88.500  82.741  1.00 30.43 ? 931  LEU A CB    1 
ATOM   6754  C CG    . LEU A  1 933  ? -16.482 88.944  84.002  1.00 31.36 ? 931  LEU A CG    1 
ATOM   6755  C CD1   . LEU A  1 933  ? -15.764 88.416  85.215  1.00 33.52 ? 931  LEU A CD1   1 
ATOM   6756  C CD2   . LEU A  1 933  ? -16.590 90.446  84.049  1.00 35.05 ? 931  LEU A CD2   1 
ATOM   6757  N N     . GLU A  1 934  ? -14.449 89.312  80.056  1.00 33.05 ? 932  GLU A N     1 
ATOM   6758  C CA    . GLU A  1 934  ? -13.445 88.965  79.054  1.00 40.59 ? 932  GLU A CA    1 
ATOM   6759  C C     . GLU A  1 934  ? -12.450 87.952  79.611  1.00 41.21 ? 932  GLU A C     1 
ATOM   6760  O O     . GLU A  1 934  ? -12.268 86.869  79.050  1.00 41.22 ? 932  GLU A O     1 
ATOM   6761  C CB    . GLU A  1 934  ? -12.724 90.227  78.570  1.00 47.03 ? 932  GLU A CB    1 
ATOM   6762  C CG    . GLU A  1 934  ? -12.395 90.224  77.092  1.00 51.49 ? 932  GLU A CG    1 
ATOM   6763  C CD    . GLU A  1 934  ? -13.634 90.335  76.214  1.00 59.28 ? 932  GLU A CD    1 
ATOM   6764  O OE1   . GLU A  1 934  ? -14.729 90.638  76.748  1.00 61.85 ? 932  GLU A OE1   1 
ATOM   6765  O OE2   . GLU A  1 934  ? -13.512 90.118  74.987  1.00 64.29 ? 932  GLU A OE2   1 
ATOM   6766  N N     . LYS A  1 935  ? -11.802 88.289  80.719  1.00 40.66 ? 933  LYS A N     1 
ATOM   6767  C CA    . LYS A  1 935  ? -10.828 87.424  81.364  1.00 41.93 ? 933  LYS A CA    1 
ATOM   6768  C C     . LYS A  1 935  ? -11.223 87.222  82.818  1.00 37.41 ? 933  LYS A C     1 
ATOM   6769  O O     . LYS A  1 935  ? -11.866 88.082  83.422  1.00 41.29 ? 933  LYS A O     1 
ATOM   6770  C CB    . LYS A  1 935  ? -9.414  88.022  81.290  1.00 38.50 ? 933  LYS A CB    1 
ATOM   6771  N N     . LEU A  1 936  ? -10.816 86.082  83.380  1.00 35.01 ? 934  LEU A N     1 
ATOM   6772  C CA    . LEU A  1 936  ? -11.035 85.842  84.803  1.00 42.51 ? 934  LEU A CA    1 
ATOM   6773  C C     . LEU A  1 936  ? -10.516 86.993  85.659  1.00 41.89 ? 934  LEU A C     1 
ATOM   6774  O O     . LEU A  1 936  ? -11.120 87.322  86.687  1.00 42.86 ? 934  LEU A O     1 
ATOM   6775  C CB    . LEU A  1 936  ? -10.377 84.523  85.212  1.00 42.23 ? 934  LEU A CB    1 
ATOM   6776  C CG    . LEU A  1 936  ? -10.578 84.005  86.640  1.00 47.10 ? 934  LEU A CG    1 
ATOM   6777  C CD1   . LEU A  1 936  ? -11.999 84.227  87.125  1.00 40.14 ? 934  LEU A CD1   1 
ATOM   6778  C CD2   . LEU A  1 936  ? -10.227 82.514  86.713  1.00 40.36 ? 934  LEU A CD2   1 
ATOM   6779  N N     . SER A  1 937  ? -9.427  87.645  85.239  1.00 44.07 ? 935  SER A N     1 
ATOM   6780  C CA    . SER A  1 937  ? -8.861  88.750  86.009  1.00 42.00 ? 935  SER A CA    1 
ATOM   6781  C C     . SER A  1 937  ? -9.731  90.010  86.006  1.00 45.12 ? 935  SER A C     1 
ATOM   6782  O O     . SER A  1 937  ? -9.443  90.933  86.774  1.00 46.24 ? 935  SER A O     1 
ATOM   6783  C CB    . SER A  1 937  ? -7.462  89.085  85.488  1.00 44.39 ? 935  SER A CB    1 
ATOM   6784  O OG    . SER A  1 937  ? -7.517  89.571  84.162  1.00 41.81 ? 935  SER A OG    1 
ATOM   6785  N N     . ASP A  1 938  ? -10.776 90.079  85.172  1.00 43.73 ? 936  ASP A N     1 
ATOM   6786  C CA    . ASP A  1 938  ? -11.737 91.180  85.259  1.00 43.80 ? 936  ASP A CA    1 
ATOM   6787  C C     . ASP A  1 938  ? -12.477 91.209  86.592  1.00 43.56 ? 936  ASP A C     1 
ATOM   6788  O O     . ASP A  1 938  ? -13.041 92.246  86.958  1.00 45.43 ? 936  ASP A O     1 
ATOM   6789  C CB    . ASP A  1 938  ? -12.773 91.088  84.132  1.00 45.89 ? 936  ASP A CB    1 
ATOM   6790  C CG    . ASP A  1 938  ? -12.177 91.329  82.756  1.00 49.42 ? 936  ASP A CG    1 
ATOM   6791  O OD1   . ASP A  1 938  ? -11.099 91.957  82.665  1.00 49.94 ? 936  ASP A OD1   1 
ATOM   6792  O OD2   . ASP A  1 938  ? -12.799 90.892  81.759  1.00 46.74 ? 936  ASP A OD2   1 
ATOM   6793  N N     . LEU A  1 939  ? -12.521 90.091  87.304  1.00 43.95 ? 937  LEU A N     1 
ATOM   6794  C CA    A LEU A  1 939  ? -13.208 89.994  88.586  0.55 44.64 ? 937  LEU A CA    1 
ATOM   6795  C CA    B LEU A  1 939  ? -13.208 89.994  88.587  0.45 44.63 ? 937  LEU A CA    1 
ATOM   6796  C C     . LEU A  1 939  ? -12.179 90.202  89.691  1.00 44.64 ? 937  LEU A C     1 
ATOM   6797  O O     . LEU A  1 939  ? -11.374 89.308  89.972  1.00 45.29 ? 937  LEU A O     1 
ATOM   6798  C CB    A LEU A  1 939  ? -13.903 88.643  88.721  0.55 40.47 ? 937  LEU A CB    1 
ATOM   6799  C CB    B LEU A  1 939  ? -13.899 88.641  88.730  0.45 40.49 ? 937  LEU A CB    1 
ATOM   6800  C CG    A LEU A  1 939  ? -14.771 88.454  89.962  0.55 41.01 ? 937  LEU A CG    1 
ATOM   6801  C CG    B LEU A  1 939  ? -15.380 88.655  89.110  0.45 40.31 ? 937  LEU A CG    1 
ATOM   6802  C CD1   A LEU A  1 939  ? -15.779 89.589  90.066  0.55 39.70 ? 937  LEU A CD1   1 
ATOM   6803  C CD1   B LEU A  1 939  ? -15.793 87.286  89.618  0.45 38.11 ? 937  LEU A CD1   1 
ATOM   6804  C CD2   A LEU A  1 939  ? -15.478 87.116  89.902  0.55 38.40 ? 937  LEU A CD2   1 
ATOM   6805  C CD2   B LEU A  1 939  ? -15.672 89.733  90.143  0.45 39.71 ? 937  LEU A CD2   1 
ATOM   6806  N N     . GLN A  1 940  ? -12.213 91.374  90.322  1.00 46.02 ? 938  GLN A N     1 
ATOM   6807  C CA    . GLN A  1 940  ? -11.162 91.779  91.248  1.00 50.04 ? 938  GLN A CA    1 
ATOM   6808  C C     . GLN A  1 940  ? -11.624 91.874  92.703  1.00 53.12 ? 938  GLN A C     1 
ATOM   6809  O O     . GLN A  1 940  ? -10.984 92.567  93.499  1.00 52.33 ? 938  GLN A O     1 
ATOM   6810  C CB    . GLN A  1 940  ? -10.570 93.114  90.792  1.00 47.45 ? 938  GLN A CB    1 
ATOM   6811  N N     . ARG A  1 941  ? -12.709 91.194  93.071  1.00 49.80 ? 939  ARG A N     1 
ATOM   6812  C CA    . ARG A  1 941  ? -13.214 91.203  94.441  1.00 48.81 ? 939  ARG A CA    1 
ATOM   6813  C C     . ARG A  1 941  ? -14.298 90.143  94.569  1.00 46.29 ? 939  ARG A C     1 
ATOM   6814  O O     . ARG A  1 941  ? -14.977 89.819  93.592  1.00 44.46 ? 939  ARG A O     1 
ATOM   6815  C CB    . ARG A  1 941  ? -13.776 92.577  94.832  1.00 49.51 ? 939  ARG A CB    1 
ATOM   6816  C CG    . ARG A  1 941  ? -14.883 93.077  93.904  1.00 50.73 ? 939  ARG A CG    1 
ATOM   6817  C CD    . ARG A  1 941  ? -15.660 94.244  94.509  1.00 54.54 ? 939  ARG A CD    1 
ATOM   6818  N NE    . ARG A  1 941  ? -16.901 93.822  95.153  1.00 54.35 ? 939  ARG A NE    1 
ATOM   6819  C CZ    . ARG A  1 941  ? -17.006 93.443  96.423  1.00 55.15 ? 939  ARG A CZ    1 
ATOM   6820  N NH1   . ARG A  1 941  ? -15.952 93.403  97.225  1.00 57.44 ? 939  ARG A NH1   1 
ATOM   6821  N NH2   . ARG A  1 941  ? -18.197 93.088  96.898  1.00 52.07 ? 939  ARG A NH2   1 
ATOM   6822  N N     . GLU A  1 942  ? -14.454 89.606  95.777  1.00 46.07 ? 940  GLU A N     1 
ATOM   6823  C CA    . GLU A  1 942  ? -15.542 88.669  96.034  1.00 45.80 ? 940  GLU A CA    1 
ATOM   6824  C C     . GLU A  1 942  ? -16.866 89.423  96.125  1.00 43.60 ? 940  GLU A C     1 
ATOM   6825  O O     . GLU A  1 942  ? -16.965 90.442  96.816  1.00 44.28 ? 940  GLU A O     1 
ATOM   6826  C CB    . GLU A  1 942  ? -15.279 87.883  97.318  1.00 45.29 ? 940  GLU A CB    1 
ATOM   6827  N N     . VAL A  1 943  ? -17.879 88.938  95.409  1.00 40.08 ? 941  VAL A N     1 
ATOM   6828  C CA    . VAL A  1 943  ? -19.201 89.559  95.374  1.00 39.17 ? 941  VAL A CA    1 
ATOM   6829  C C     . VAL A  1 943  ? -20.195 88.563  95.952  1.00 34.79 ? 941  VAL A C     1 
ATOM   6830  O O     . VAL A  1 943  ? -20.575 87.595  95.280  1.00 34.44 ? 941  VAL A O     1 
ATOM   6831  C CB    . VAL A  1 943  ? -19.607 89.973  93.954  1.00 39.36 ? 941  VAL A CB    1 
ATOM   6832  C CG1   . VAL A  1 943  ? -20.964 90.675  93.974  1.00 32.99 ? 941  VAL A CG1   1 
ATOM   6833  C CG2   . VAL A  1 943  ? -18.533 90.866  93.339  1.00 43.58 ? 941  VAL A CG2   1 
ATOM   6834  N N     . PHE A  1 944  ? -20.647 88.815  97.177  1.00 32.41 ? 942  PHE A N     1 
ATOM   6835  C CA    . PHE A  1 944  ? -21.350 87.799  97.956  1.00 31.24 ? 942  PHE A CA    1 
ATOM   6836  C C     . PHE A  1 944  ? -22.853 87.906  97.722  1.00 30.53 ? 942  PHE A C     1 
ATOM   6837  O O     . PHE A  1 944  ? -23.626 88.302  98.593  1.00 31.84 ? 942  PHE A O     1 
ATOM   6838  C CB    . PHE A  1 944  ? -21.018 87.936  99.436  1.00 33.26 ? 942  PHE A CB    1 
ATOM   6839  C CG    . PHE A  1 944  ? -21.045 86.633  100.173 1.00 34.15 ? 942  PHE A CG    1 
ATOM   6840  C CD1   . PHE A  1 944  ? -20.056 85.680  99.953  1.00 33.02 ? 942  PHE A CD1   1 
ATOM   6841  C CD2   . PHE A  1 944  ? -22.051 86.356  101.088 1.00 35.06 ? 942  PHE A CD2   1 
ATOM   6842  C CE1   . PHE A  1 944  ? -20.074 84.475  100.637 1.00 33.99 ? 942  PHE A CE1   1 
ATOM   6843  C CE2   . PHE A  1 944  ? -22.076 85.154  101.779 1.00 31.64 ? 942  PHE A CE2   1 
ATOM   6844  C CZ    . PHE A  1 944  ? -21.092 84.210  101.552 1.00 33.52 ? 942  PHE A CZ    1 
ATOM   6845  N N     . GLY A  1 945  ? -23.253 87.547  96.508  1.00 28.08 ? 943  GLY A N     1 
ATOM   6846  C CA    . GLY A  1 945  ? -24.630 87.662  96.102  1.00 27.17 ? 943  GLY A CA    1 
ATOM   6847  C C     . GLY A  1 945  ? -24.948 86.814  94.891  1.00 26.70 ? 943  GLY A C     1 
ATOM   6848  O O     . GLY A  1 945  ? -24.132 86.010  94.434  1.00 26.59 ? 943  GLY A O     1 
ATOM   6849  N N     . PRO A  1 946  ? -26.151 86.972  94.348  1.00 24.83 ? 944  PRO A N     1 
ATOM   6850  C CA    . PRO A  1 946  ? -26.585 86.112  93.231  1.00 26.13 ? 944  PRO A CA    1 
ATOM   6851  C C     . PRO A  1 946  ? -26.071 86.614  91.887  1.00 24.98 ? 944  PRO A C     1 
ATOM   6852  O O     . PRO A  1 946  ? -26.835 87.043  91.014  1.00 25.10 ? 944  PRO A O     1 
ATOM   6853  C CB    . PRO A  1 946  ? -28.116 86.180  93.341  1.00 24.86 ? 944  PRO A CB    1 
ATOM   6854  C CG    . PRO A  1 946  ? -28.397 87.528  93.894  1.00 25.42 ? 944  PRO A CG    1 
ATOM   6855  C CD    . PRO A  1 946  ? -27.212 87.888  94.808  1.00 25.87 ? 944  PRO A CD    1 
ATOM   6856  N N     . VAL A  1 947  ? -24.752 86.605  91.728  1.00 24.30 ? 945  VAL A N     1 
ATOM   6857  C CA    . VAL A  1 947  ? -24.108 87.247  90.589  1.00 25.95 ? 945  VAL A CA    1 
ATOM   6858  C C     . VAL A  1 947  ? -23.119 86.258  90.000  1.00 25.36 ? 945  VAL A C     1 
ATOM   6859  O O     . VAL A  1 947  ? -22.091 85.951  90.621  1.00 27.36 ? 945  VAL A O     1 
ATOM   6860  C CB    . VAL A  1 947  ? -23.412 88.558  90.978  1.00 28.74 ? 945  VAL A CB    1 
ATOM   6861  C CG1   . VAL A  1 947  ? -22.735 89.166  89.774  1.00 24.90 ? 945  VAL A CG1   1 
ATOM   6862  C CG2   . VAL A  1 947  ? -24.419 89.532  91.595  1.00 26.63 ? 945  VAL A CG2   1 
ATOM   6863  N N     . LEU A  1 948  ? -23.422 85.766  88.808  1.00 24.73 ? 946  LEU A N     1 
ATOM   6864  C CA    . LEU A  1 948  ? -22.618 84.765  88.126  1.00 22.05 ? 946  LEU A CA    1 
ATOM   6865  C C     . LEU A  1 948  ? -21.807 85.457  87.047  1.00 26.10 ? 946  LEU A C     1 
ATOM   6866  O O     . LEU A  1 948  ? -22.356 86.232  86.258  1.00 27.00 ? 946  LEU A O     1 
ATOM   6867  C CB    . LEU A  1 948  ? -23.497 83.686  87.489  1.00 24.15 ? 946  LEU A CB    1 
ATOM   6868  C CG    . LEU A  1 948  ? -22.666 82.671  86.691  1.00 24.74 ? 946  LEU A CG    1 
ATOM   6869  C CD1   . LEU A  1 948  ? -21.667 81.942  87.623  1.00 21.51 ? 946  LEU A CD1   1 
ATOM   6870  C CD2   . LEU A  1 948  ? -23.581 81.693  85.987  1.00 28.42 ? 946  LEU A CD2   1 
ATOM   6871  N N     . HIS A  1 949  ? -20.514 85.172  87.005  1.00 23.88 ? 947  HIS A N     1 
ATOM   6872  C CA    . HIS A  1 949  ? -19.661 85.713  85.961  1.00 25.17 ? 947  HIS A CA    1 
ATOM   6873  C C     . HIS A  1 949  ? -19.317 84.592  84.995  1.00 24.45 ? 947  HIS A C     1 
ATOM   6874  O O     . HIS A  1 949  ? -19.120 83.448  85.412  1.00 26.08 ? 947  HIS A O     1 
ATOM   6875  C CB    . HIS A  1 949  ? -18.407 86.336  86.555  1.00 24.88 ? 947  HIS A CB    1 
ATOM   6876  C CG    . HIS A  1 949  ? -18.695 87.399  87.567  1.00 29.93 ? 947  HIS A CG    1 
ATOM   6877  N ND1   . HIS A  1 949  ? -18.939 87.116  88.894  1.00 31.38 ? 947  HIS A ND1   1 
ATOM   6878  C CD2   . HIS A  1 949  ? -18.805 88.741  87.441  1.00 28.72 ? 947  HIS A CD2   1 
ATOM   6879  C CE1   . HIS A  1 949  ? -19.169 88.243  89.545  1.00 30.26 ? 947  HIS A CE1   1 
ATOM   6880  N NE2   . HIS A  1 949  ? -19.087 89.243  88.687  1.00 32.02 ? 947  HIS A NE2   1 
ATOM   6881  N N     . VAL A  1 950  ? -19.298 84.911  83.700  1.00 26.97 ? 948  VAL A N     1 
ATOM   6882  C CA    . VAL A  1 950  ? -19.102 83.912  82.654  1.00 26.13 ? 948  VAL A CA    1 
ATOM   6883  C C     . VAL A  1 950  ? -17.894 84.314  81.827  1.00 25.56 ? 948  VAL A C     1 
ATOM   6884  O O     . VAL A  1 950  ? -17.787 85.466  81.392  1.00 27.52 ? 948  VAL A O     1 
ATOM   6885  C CB    . VAL A  1 950  ? -20.344 83.757  81.754  1.00 29.24 ? 948  VAL A CB    1 
ATOM   6886  C CG1   . VAL A  1 950  ? -20.067 82.759  80.634  1.00 29.10 ? 948  VAL A CG1   1 
ATOM   6887  C CG2   . VAL A  1 950  ? -21.565 83.305  82.561  1.00 24.37 ? 948  VAL A CG2   1 
ATOM   6888  N N     . ILE A  1 951  ? -16.981 83.372  81.622  1.00 25.24 ? 949  ILE A N     1 
ATOM   6889  C CA    . ILE A  1 951  ? -15.879 83.571  80.695  1.00 30.73 ? 949  ILE A CA    1 
ATOM   6890  C C     . ILE A  1 951  ? -15.812 82.357  79.785  1.00 29.00 ? 949  ILE A C     1 
ATOM   6891  O O     . ILE A  1 951  ? -16.295 81.272  80.125  1.00 25.24 ? 949  ILE A O     1 
ATOM   6892  C CB    . ILE A  1 951  ? -14.530 83.792  81.404  1.00 29.56 ? 949  ILE A CB    1 
ATOM   6893  C CG1   . ILE A  1 951  ? -14.137 82.550  82.195  1.00 28.40 ? 949  ILE A CG1   1 
ATOM   6894  C CG2   . ILE A  1 951  ? -14.580 85.035  82.297  1.00 33.87 ? 949  ILE A CG2   1 
ATOM   6895  C CD1   . ILE A  1 951  ? -12.862 82.713  82.982  1.00 34.73 ? 949  ILE A CD1   1 
ATOM   6896  N N     . ARG A  1 952  ? -15.196 82.560  78.618  1.00 27.36 ? 950  ARG A N     1 
ATOM   6897  C CA    . ARG A  1 952  ? -15.035 81.540  77.593  1.00 28.93 ? 950  ARG A CA    1 
ATOM   6898  C C     . ARG A  1 952  ? -13.555 81.220  77.420  1.00 29.63 ? 950  ARG A C     1 
ATOM   6899  O O     . ARG A  1 952  ? -12.699 82.081  77.622  1.00 27.26 ? 950  ARG A O     1 
ATOM   6900  C CB    . ARG A  1 952  ? -15.619 82.027  76.262  1.00 32.06 ? 950  ARG A CB    1 
ATOM   6901  C CG    . ARG A  1 952  ? -16.997 82.649  76.406  1.00 31.64 ? 950  ARG A CG    1 
ATOM   6902  C CD    . ARG A  1 952  ? -17.254 83.666  75.324  1.00 39.12 ? 950  ARG A CD    1 
ATOM   6903  N NE    . ARG A  1 952  ? -17.555 83.027  74.052  1.00 36.61 ? 950  ARG A NE    1 
ATOM   6904  C CZ    . ARG A  1 952  ? -18.782 82.850  73.584  1.00 39.28 ? 950  ARG A CZ    1 
ATOM   6905  N NH1   . ARG A  1 952  ? -19.846 83.273  74.252  1.00 35.19 ? 950  ARG A NH1   1 
ATOM   6906  N NH2   . ARG A  1 952  ? -18.946 82.234  72.416  1.00 31.81 ? 950  ARG A NH2   1 
ATOM   6907  N N     . TYR A  1 953  ? -13.248 79.979  77.040  1.00 25.92 ? 951  TYR A N     1 
ATOM   6908  C CA    . TYR A  1 953  ? -11.850 79.595  76.871  1.00 26.90 ? 951  TYR A CA    1 
ATOM   6909  C C     . TYR A  1 953  ? -11.726 78.648  75.689  1.00 28.73 ? 951  TYR A C     1 
ATOM   6910  O O     . TYR A  1 953  ? -12.630 77.856  75.412  1.00 28.60 ? 951  TYR A O     1 
ATOM   6911  C CB    . TYR A  1 953  ? -11.270 78.934  78.152  1.00 26.21 ? 951  TYR A CB    1 
ATOM   6912  C CG    . TYR A  1 953  ? -11.796 77.531  78.428  1.00 26.76 ? 951  TYR A CG    1 
ATOM   6913  C CD1   . TYR A  1 953  ? -13.013 77.336  79.068  1.00 22.48 ? 951  TYR A CD1   1 
ATOM   6914  C CD2   . TYR A  1 953  ? -11.068 76.399  78.053  1.00 27.75 ? 951  TYR A CD2   1 
ATOM   6915  C CE1   . TYR A  1 953  ? -13.504 76.072  79.321  1.00 22.23 ? 951  TYR A CE1   1 
ATOM   6916  C CE2   . TYR A  1 953  ? -11.561 75.116  78.299  1.00 26.98 ? 951  TYR A CE2   1 
ATOM   6917  C CZ    . TYR A  1 953  ? -12.781 74.967  78.936  1.00 24.09 ? 951  TYR A CZ    1 
ATOM   6918  O OH    . TYR A  1 953  ? -13.289 73.715  79.190  1.00 22.86 ? 951  TYR A OH    1 
ATOM   6919  N N     . ARG A  1 954  ? -10.594 78.747  74.990  1.00 30.50 ? 952  ARG A N     1 
ATOM   6920  C CA    . ARG A  1 954  ? -10.240 77.787  73.949  1.00 32.69 ? 952  ARG A CA    1 
ATOM   6921  C C     . ARG A  1 954  ? -9.698  76.507  74.580  1.00 31.29 ? 952  ARG A C     1 
ATOM   6922  O O     . ARG A  1 954  ? -8.995  76.552  75.593  1.00 26.62 ? 952  ARG A O     1 
ATOM   6923  C CB    . ARG A  1 954  ? -9.189  78.382  73.011  1.00 35.22 ? 952  ARG A CB    1 
ATOM   6924  C CG    . ARG A  1 954  ? -9.511  79.777  72.476  1.00 40.17 ? 952  ARG A CG    1 
ATOM   6925  C CD    . ARG A  1 954  ? -10.816 79.776  71.686  1.00 43.95 ? 952  ARG A CD    1 
ATOM   6926  N NE    . ARG A  1 954  ? -10.819 78.721  70.683  1.00 47.50 ? 952  ARG A NE    1 
ATOM   6927  C CZ    . ARG A  1 954  ? -10.220 78.816  69.504  1.00 54.67 ? 952  ARG A CZ    1 
ATOM   6928  N NH1   . ARG A  1 954  ? -9.623  79.933  69.121  1.00 54.84 ? 952  ARG A NH1   1 
ATOM   6929  N NH2   . ARG A  1 954  ? -10.214 77.762  68.691  1.00 56.04 ? 952  ARG A NH2   1 
ATOM   6930  N N     . ARG A  1 955  ? -10.028 75.357  73.980  1.00 29.12 ? 953  ARG A N     1 
ATOM   6931  C CA    . ARG A  1 955  ? -9.663  74.086  74.608  1.00 29.76 ? 953  ARG A CA    1 
ATOM   6932  C C     . ARG A  1 955  ? -8.164  73.993  74.876  1.00 29.12 ? 953  ARG A C     1 
ATOM   6933  O O     . ARG A  1 955  ? -7.751  73.553  75.954  1.00 33.24 ? 953  ARG A O     1 
ATOM   6934  C CB    . ARG A  1 955  ? -10.115 72.899  73.759  1.00 32.83 ? 953  ARG A CB    1 
ATOM   6935  C CG    . ARG A  1 955  ? -9.741  71.539  74.394  1.00 40.37 ? 953  ARG A CG    1 
ATOM   6936  C CD    . ARG A  1 955  ? -10.093 71.513  75.897  1.00 41.85 ? 953  ARG A CD    1 
ATOM   6937  N NE    . ARG A  1 955  ? -9.788  70.250  76.564  1.00 41.98 ? 953  ARG A NE    1 
ATOM   6938  C CZ    . ARG A  1 955  ? -8.584  69.884  76.987  1.00 43.82 ? 953  ARG A CZ    1 
ATOM   6939  N NH1   . ARG A  1 955  ? -7.512  70.641  76.783  1.00 40.52 ? 953  ARG A NH1   1 
ATOM   6940  N NH2   . ARG A  1 955  ? -8.448  68.724  77.625  1.00 42.94 ? 953  ARG A NH2   1 
ATOM   6941  N N     . ASP A  1 956  ? -7.331  74.399  73.918  1.00 31.16 ? 954  ASP A N     1 
ATOM   6942  C CA    . ASP A  1 956  ? -5.892  74.310  74.144  1.00 33.34 ? 954  ASP A CA    1 
ATOM   6943  C C     . ASP A  1 956  ? -5.431  75.151  75.324  1.00 31.02 ? 954  ASP A C     1 
ATOM   6944  O O     . ASP A  1 956  ? -4.349  74.892  75.861  1.00 34.75 ? 954  ASP A O     1 
ATOM   6945  C CB    . ASP A  1 956  ? -5.127  74.738  72.894  1.00 33.43 ? 954  ASP A CB    1 
ATOM   6946  C CG    . ASP A  1 956  ? -5.215  73.717  71.786  1.00 37.63 ? 954  ASP A CG    1 
ATOM   6947  O OD1   . ASP A  1 956  ? -5.646  72.575  72.064  1.00 35.49 ? 954  ASP A OD1   1 
ATOM   6948  O OD2   . ASP A  1 956  ? -4.852  74.058  70.643  1.00 43.72 ? 954  ASP A OD2   1 
ATOM   6949  N N     . ASP A  1 957  ? -6.211  76.156  75.728  1.00 32.87 ? 955  ASP A N     1 
ATOM   6950  C CA    . ASP A  1 957  ? -5.851  77.031  76.837  1.00 32.95 ? 955  ASP A CA    1 
ATOM   6951  C C     . ASP A  1 957  ? -6.404  76.555  78.175  1.00 29.68 ? 955  ASP A C     1 
ATOM   6952  O O     . ASP A  1 957  ? -6.385  77.324  79.141  1.00 30.20 ? 955  ASP A O     1 
ATOM   6953  C CB    . ASP A  1 957  ? -6.341  78.464  76.589  1.00 36.12 ? 955  ASP A CB    1 
ATOM   6954  C CG    . ASP A  1 957  ? -5.648  79.138  75.419  1.00 37.97 ? 955  ASP A CG    1 
ATOM   6955  O OD1   . ASP A  1 957  ? -4.448  78.891  75.193  1.00 42.02 ? 955  ASP A OD1   1 
ATOM   6956  O OD2   . ASP A  1 957  ? -6.313  79.940  74.730  1.00 40.01 ? 955  ASP A OD2   1 
ATOM   6957  N N     . LEU A  1 958  ? -6.875  75.312  78.265  1.00 27.56 ? 956  LEU A N     1 
ATOM   6958  C CA    . LEU A  1 958  ? -7.433  74.832  79.528  1.00 26.52 ? 956  LEU A CA    1 
ATOM   6959  C C     . LEU A  1 958  ? -6.404  74.906  80.656  1.00 29.17 ? 956  LEU A C     1 
ATOM   6960  O O     . LEU A  1 958  ? -6.712  75.369  81.759  1.00 25.62 ? 956  LEU A O     1 
ATOM   6961  C CB    . LEU A  1 958  ? -7.954  73.403  79.369  1.00 28.27 ? 956  LEU A CB    1 
ATOM   6962  C CG    . LEU A  1 958  ? -8.437  72.693  80.641  1.00 28.59 ? 956  LEU A CG    1 
ATOM   6963  C CD1   . LEU A  1 958  ? -9.540  73.489  81.331  1.00 26.80 ? 956  LEU A CD1   1 
ATOM   6964  C CD2   . LEU A  1 958  ? -8.941  71.303  80.289  1.00 29.88 ? 956  LEU A CD2   1 
ATOM   6965  N N     . ASP A  1 959  ? -5.174  74.444  80.409  1.00 26.50 ? 957  ASP A N     1 
ATOM   6966  C CA    . ASP A  1 959  ? -4.204  74.430  81.500  1.00 27.20 ? 957  ASP A CA    1 
ATOM   6967  C C     . ASP A  1 959  ? -3.898  75.841  81.978  1.00 28.01 ? 957  ASP A C     1 
ATOM   6968  O O     . ASP A  1 959  ? -3.686  76.063  83.174  1.00 28.02 ? 957  ASP A O     1 
ATOM   6969  C CB    . ASP A  1 959  ? -2.909  73.731  81.084  1.00 28.94 ? 957  ASP A CB    1 
ATOM   6970  C CG    . ASP A  1 959  ? -1.984  73.489  82.265  1.00 31.36 ? 957  ASP A CG    1 
ATOM   6971  O OD1   . ASP A  1 959  ? -2.409  72.825  83.242  1.00 28.61 ? 957  ASP A OD1   1 
ATOM   6972  O OD2   . ASP A  1 959  ? -0.834  73.972  82.224  1.00 35.29 ? 957  ASP A OD2   1 
ATOM   6973  N N     . ARG A  1 960  ? -3.856  76.808  81.056  1.00 29.44 ? 958  ARG A N     1 
ATOM   6974  C CA    . ARG A  1 960  ? -3.642  78.190  81.463  1.00 26.48 ? 958  ARG A CA    1 
ATOM   6975  C C     . ARG A  1 960  ? -4.832  78.708  82.268  1.00 30.59 ? 958  ARG A C     1 
ATOM   6976  O O     . ARG A  1 960  ? -4.655  79.457  83.236  1.00 31.32 ? 958  ARG A O     1 
ATOM   6977  C CB    . ARG A  1 960  ? -3.387  79.064  80.226  1.00 32.97 ? 958  ARG A CB    1 
ATOM   6978  C CG    . ARG A  1 960  ? -3.004  80.516  80.525  1.00 36.53 ? 958  ARG A CG    1 
ATOM   6979  C CD    . ARG A  1 960  ? -2.668  81.296  79.248  1.00 43.03 ? 958  ARG A CD    1 
ATOM   6980  N NE    . ARG A  1 960  ? -3.869  81.695  78.515  1.00 52.59 ? 958  ARG A NE    1 
ATOM   6981  C CZ    . ARG A  1 960  ? -3.871  82.379  77.377  1.00 51.82 ? 958  ARG A CZ    1 
ATOM   6982  N NH1   . ARG A  1 960  ? -2.744  82.737  76.782  1.00 52.82 ? 958  ARG A NH1   1 
ATOM   6983  N NH2   . ARG A  1 960  ? -5.035  82.712  76.822  1.00 53.90 ? 958  ARG A NH2   1 
ATOM   6984  N N     . LEU A  1 961  ? -6.053  78.327  81.879  1.00 27.31 ? 959  LEU A N     1 
ATOM   6985  C CA    . LEU A  1 961  ? -7.239  78.738  82.635  1.00 26.24 ? 959  LEU A CA    1 
ATOM   6986  C C     . LEU A  1 961  ? -7.168  78.261  84.078  1.00 29.98 ? 959  LEU A C     1 
ATOM   6987  O O     . LEU A  1 961  ? -7.429  79.027  85.013  1.00 26.81 ? 959  LEU A O     1 
ATOM   6988  C CB    . LEU A  1 961  ? -8.502  78.195  81.976  1.00 26.92 ? 959  LEU A CB    1 
ATOM   6989  C CG    . LEU A  1 961  ? -9.773  78.427  82.788  1.00 27.20 ? 959  LEU A CG    1 
ATOM   6990  C CD1   . LEU A  1 961  ? -10.033 79.920  82.925  1.00 29.42 ? 959  LEU A CD1   1 
ATOM   6991  C CD2   . LEU A  1 961  ? -10.965 77.724  82.132  1.00 30.20 ? 959  LEU A CD2   1 
ATOM   6992  N N     . VAL A  1 962  ? -6.844  76.982  84.278  1.00 26.47 ? 960  VAL A N     1 
ATOM   6993  C CA    . VAL A  1 962  ? -6.684  76.472  85.638  1.00 25.88 ? 960  VAL A CA    1 
ATOM   6994  C C     . VAL A  1 962  ? -5.658  77.303  86.392  1.00 31.18 ? 960  VAL A C     1 
ATOM   6995  O O     . VAL A  1 962  ? -5.863  77.649  87.566  1.00 30.53 ? 960  VAL A O     1 
ATOM   6996  C CB    . VAL A  1 962  ? -6.309  74.978  85.611  1.00 28.74 ? 960  VAL A CB    1 
ATOM   6997  C CG1   . VAL A  1 962  ? -6.060  74.455  87.034  1.00 28.12 ? 960  VAL A CG1   1 
ATOM   6998  C CG2   . VAL A  1 962  ? -7.413  74.185  84.937  1.00 23.39 ? 960  VAL A CG2   1 
ATOM   6999  N N     . ASP A  1 963  ? -4.548  77.657  85.724  1.00 27.31 ? 961  ASP A N     1 
ATOM   7000  C CA    . ASP A  1 963  ? -3.570  78.580  86.304  1.00 32.81 ? 961  ASP A CA    1 
ATOM   7001  C C     . ASP A  1 963  ? -4.226  79.879  86.758  1.00 31.44 ? 961  ASP A C     1 
ATOM   7002  O O     . ASP A  1 963  ? -3.940  80.384  87.851  1.00 34.96 ? 961  ASP A O     1 
ATOM   7003  C CB    . ASP A  1 963  ? -2.466  78.891  85.288  1.00 33.43 ? 961  ASP A CB    1 
ATOM   7004  C CG    . ASP A  1 963  ? -1.315  77.925  85.349  1.00 39.69 ? 961  ASP A CG    1 
ATOM   7005  O OD1   . ASP A  1 963  ? -1.186  77.206  86.357  1.00 44.52 ? 961  ASP A OD1   1 
ATOM   7006  O OD2   . ASP A  1 963  ? -0.517  77.901  84.384  1.00 43.12 ? 961  ASP A OD2   1 
ATOM   7007  N N     . ASP A  1 964  ? -5.101  80.444  85.911  1.00 31.06 ? 962  ASP A N     1 
ATOM   7008  C CA    . ASP A  1 964  ? -5.796  81.688  86.240  1.00 35.76 ? 962  ASP A CA    1 
ATOM   7009  C C     . ASP A  1 964  ? -6.745  81.510  87.419  1.00 36.16 ? 962  ASP A C     1 
ATOM   7010  O O     . ASP A  1 964  ? -6.878  82.407  88.262  1.00 35.18 ? 962  ASP A O     1 
ATOM   7011  C CB    . ASP A  1 964  ? -6.578  82.194  85.031  1.00 35.99 ? 962  ASP A CB    1 
ATOM   7012  C CG    . ASP A  1 964  ? -5.684  82.612  83.886  1.00 39.05 ? 962  ASP A CG    1 
ATOM   7013  O OD1   . ASP A  1 964  ? -4.470  82.797  84.113  1.00 43.51 ? 962  ASP A OD1   1 
ATOM   7014  O OD2   . ASP A  1 964  ? -6.211  82.769  82.760  1.00 44.89 ? 962  ASP A OD2   1 
ATOM   7015  N N     . VAL A  1 965  ? -7.438  80.377  87.479  1.00 28.75 ? 963  VAL A N     1 
ATOM   7016  C CA    . VAL A  1 965  ? -8.283  80.100  88.637  1.00 31.22 ? 963  VAL A CA    1 
ATOM   7017  C C     . VAL A  1 965  ? -7.438  80.057  89.906  1.00 32.76 ? 963  VAL A C     1 
ATOM   7018  O O     . VAL A  1 965  ? -7.773  80.687  90.920  1.00 33.73 ? 963  VAL A O     1 
ATOM   7019  C CB    . VAL A  1 965  ? -9.063  78.791  88.428  1.00 28.11 ? 963  VAL A CB    1 
ATOM   7020  C CG1   . VAL A  1 965  ? -9.909  78.474  89.656  1.00 28.00 ? 963  VAL A CG1   1 
ATOM   7021  C CG2   . VAL A  1 965  ? -9.928  78.887  87.176  1.00 27.96 ? 963  VAL A CG2   1 
ATOM   7022  N N     . ASN A  1 966  ? -6.322  79.315  89.867  1.00 27.77 ? 964  ASN A N     1 
ATOM   7023  C CA    . ASN A  1 966  ? -5.451  79.229  91.033  1.00 32.01 ? 964  ASN A CA    1 
ATOM   7024  C C     . ASN A  1 966  ? -4.886  80.587  91.400  1.00 34.60 ? 964  ASN A C     1 
ATOM   7025  O O     . ASN A  1 966  ? -4.651  80.861  92.583  1.00 32.29 ? 964  ASN A O     1 
ATOM   7026  C CB    . ASN A  1 966  ? -4.288  78.261  90.786  1.00 30.69 ? 964  ASN A CB    1 
ATOM   7027  C CG    . ASN A  1 966  ? -4.718  76.803  90.756  1.00 30.17 ? 964  ASN A CG    1 
ATOM   7028  O OD1   . ASN A  1 966  ? -5.747  76.421  91.334  1.00 28.67 ? 964  ASN A OD1   1 
ATOM   7029  N ND2   . ASN A  1 966  ? -3.929  75.977  90.071  1.00 26.64 ? 964  ASN A ND2   1 
ATOM   7030  N N     . ALA A  1 967  ? -4.669  81.452  90.406  1.00 32.98 ? 965  ALA A N     1 
ATOM   7031  C CA    . ALA A  1 967  ? -3.926  82.685  90.653  1.00 39.50 ? 965  ALA A CA    1 
ATOM   7032  C C     . ALA A  1 967  ? -4.692  83.686  91.511  1.00 35.08 ? 965  ALA A C     1 
ATOM   7033  O O     . ALA A  1 967  ? -4.061  84.578  92.091  1.00 40.38 ? 965  ALA A O     1 
ATOM   7034  C CB    . ALA A  1 967  ? -3.513  83.334  89.327  1.00 38.70 ? 965  ALA A CB    1 
ATOM   7035  N N     . THR A  1 968  ? -6.018  83.561  91.626  1.00 36.26 ? 966  THR A N     1 
ATOM   7036  C CA    . THR A  1 968  ? -6.762  84.425  92.544  1.00 35.44 ? 966  THR A CA    1 
ATOM   7037  C C     . THR A  1 968  ? -6.288  84.283  93.983  1.00 34.60 ? 966  THR A C     1 
ATOM   7038  O O     . THR A  1 968  ? -6.514  85.196  94.785  1.00 34.88 ? 966  THR A O     1 
ATOM   7039  C CB    . THR A  1 968  ? -8.267  84.126  92.530  1.00 34.28 ? 966  THR A CB    1 
ATOM   7040  O OG1   . THR A  1 968  ? -8.518  82.930  93.288  1.00 31.75 ? 966  THR A OG1   1 
ATOM   7041  C CG2   . THR A  1 968  ? -8.802  83.969  91.100  1.00 35.00 ? 966  THR A CG2   1 
ATOM   7042  N N     . GLY A  1 969  ? -5.667  83.154  94.336  1.00 31.84 ? 967  GLY A N     1 
ATOM   7043  C CA    . GLY A  1 969  ? -5.251  82.893  95.704  1.00 32.66 ? 967  GLY A CA    1 
ATOM   7044  C C     . GLY A  1 969  ? -6.312  82.253  96.576  1.00 30.40 ? 967  GLY A C     1 
ATOM   7045  O O     . GLY A  1 969  ? -6.007  81.846  97.704  1.00 28.44 ? 967  GLY A O     1 
ATOM   7046  N N     . TYR A  1 970  ? -7.546  82.170  96.097  1.00 31.69 ? 968  TYR A N     1 
ATOM   7047  C CA    . TYR A  1 970  ? -8.604  81.454  96.783  1.00 29.68 ? 968  TYR A CA    1 
ATOM   7048  C C     . TYR A  1 970  ? -8.508  79.965  96.474  1.00 30.20 ? 968  TYR A C     1 
ATOM   7049  O O     . TYR A  1 970  ? -7.781  79.533  95.573  1.00 30.36 ? 968  TYR A O     1 
ATOM   7050  C CB    . TYR A  1 970  ? -9.967  82.005  96.368  1.00 29.26 ? 968  TYR A CB    1 
ATOM   7051  C CG    . TYR A  1 970  ? -10.230 83.395  96.906  1.00 31.76 ? 968  TYR A CG    1 
ATOM   7052  C CD1   . TYR A  1 970  ? -10.657 83.574  98.210  1.00 32.02 ? 968  TYR A CD1   1 
ATOM   7053  C CD2   . TYR A  1 970  ? -10.046 84.524  96.111  1.00 35.22 ? 968  TYR A CD2   1 
ATOM   7054  C CE1   . TYR A  1 970  ? -10.902 84.844  98.719  1.00 33.18 ? 968  TYR A CE1   1 
ATOM   7055  C CE2   . TYR A  1 970  ? -10.290 85.803  96.609  1.00 34.11 ? 968  TYR A CE2   1 
ATOM   7056  C CZ    . TYR A  1 970  ? -10.708 85.950  97.918  1.00 35.73 ? 968  TYR A CZ    1 
ATOM   7057  O OH    . TYR A  1 970  ? -10.957 87.204  98.437  1.00 42.07 ? 968  TYR A OH    1 
ATOM   7058  N N     . GLY A  1 971  ? -9.245  79.166  97.235  1.00 23.77 ? 969  GLY A N     1 
ATOM   7059  C CA    . GLY A  1 971  ? -9.189  77.736  97.013  1.00 27.76 ? 969  GLY A CA    1 
ATOM   7060  C C     . GLY A  1 971  ? -10.245 76.962  97.765  1.00 26.18 ? 969  GLY A C     1 
ATOM   7061  O O     . GLY A  1 971  ? -9.918  76.046  98.520  1.00 26.06 ? 969  GLY A O     1 
ATOM   7062  N N     . LEU A  1 972  ? -11.518 77.322  97.581  1.00 25.53 ? 970  LEU A N     1 
ATOM   7063  C CA    . LEU A  1 972  ? -12.581 76.698  98.361  1.00 20.55 ? 970  LEU A CA    1 
ATOM   7064  C C     . LEU A  1 972  ? -13.251 75.577  97.571  1.00 24.77 ? 970  LEU A C     1 
ATOM   7065  O O     . LEU A  1 972  ? -12.890 74.405  97.725  1.00 25.02 ? 970  LEU A O     1 
ATOM   7066  C CB    . LEU A  1 972  ? -13.617 77.745  98.790  1.00 22.29 ? 970  LEU A CB    1 
ATOM   7067  C CG    . LEU A  1 972  ? -14.609 77.279  99.858  1.00 28.13 ? 970  LEU A CG    1 
ATOM   7068  C CD1   . LEU A  1 972  ? -13.877 76.521  100.980 1.00 26.41 ? 970  LEU A CD1   1 
ATOM   7069  C CD2   . LEU A  1 972  ? -15.380 78.492  100.420 1.00 28.80 ? 970  LEU A CD2   1 
ATOM   7070  N N     . THR A  1 973  ? -14.230 75.915  96.728  1.00 23.38 ? 971  THR A N     1 
ATOM   7071  C CA    . THR A  1 973  ? -14.902 74.920  95.905  1.00 21.20 ? 971  THR A CA    1 
ATOM   7072  C C     . THR A  1 973  ? -14.553 75.131  94.438  1.00 22.15 ? 971  THR A C     1 
ATOM   7073  O O     . THR A  1 973  ? -14.234 76.238  94.002  1.00 20.41 ? 971  THR A O     1 
ATOM   7074  C CB    . THR A  1 973  ? -16.430 74.950  96.071  1.00 22.47 ? 971  THR A CB    1 
ATOM   7075  O OG1   . THR A  1 973  ? -16.934 76.236  95.710  1.00 22.83 ? 971  THR A OG1   1 
ATOM   7076  C CG2   . THR A  1 973  ? -16.841 74.642  97.525  1.00 23.15 ? 971  THR A CG2   1 
ATOM   7077  N N     . PHE A  1 974  ? -14.639 74.046  93.680  1.00 18.97 ? 972  PHE A N     1 
ATOM   7078  C CA    . PHE A  1 974  ? -14.309 74.051  92.265  1.00 19.10 ? 972  PHE A CA    1 
ATOM   7079  C C     . PHE A  1 974  ? -15.129 72.952  91.614  1.00 18.05 ? 972  PHE A C     1 
ATOM   7080  O O     . PHE A  1 974  ? -15.224 71.845  92.158  1.00 20.54 ? 972  PHE A O     1 
ATOM   7081  C CB    . PHE A  1 974  ? -12.811 73.788  92.022  1.00 21.42 ? 972  PHE A CB    1 
ATOM   7082  C CG    . PHE A  1 974  ? -12.482 73.519  90.581  1.00 18.76 ? 972  PHE A CG    1 
ATOM   7083  C CD1   . PHE A  1 974  ? -12.293 74.569  89.705  1.00 21.18 ? 972  PHE A CD1   1 
ATOM   7084  C CD2   . PHE A  1 974  ? -12.400 72.221  90.102  1.00 19.08 ? 972  PHE A CD2   1 
ATOM   7085  C CE1   . PHE A  1 974  ? -12.016 74.326  88.365  1.00 23.31 ? 972  PHE A CE1   1 
ATOM   7086  C CE2   . PHE A  1 974  ? -12.123 71.969  88.761  1.00 19.50 ? 972  PHE A CE2   1 
ATOM   7087  C CZ    . PHE A  1 974  ? -11.925 73.028  87.903  1.00 21.37 ? 972  PHE A CZ    1 
ATOM   7088  N N     . GLY A  1 975  ? -15.696 73.234  90.443  1.00 20.47 ? 973  GLY A N     1 
ATOM   7089  C CA    . GLY A  1 975  ? -16.496 72.258  89.732  1.00 18.28 ? 973  GLY A CA    1 
ATOM   7090  C C     . GLY A  1 975  ? -15.933 71.974  88.357  1.00 17.36 ? 973  GLY A C     1 
ATOM   7091  O O     . GLY A  1 975  ? -15.357 72.850  87.715  1.00 20.27 ? 973  GLY A O     1 
ATOM   7092  N N     . LEU A  1 976  ? -16.099 70.726  87.915  1.00 19.56 ? 974  LEU A N     1 
ATOM   7093  C CA    . LEU A  1 976  ? -15.728 70.338  86.562  1.00 16.94 ? 974  LEU A CA    1 
ATOM   7094  C C     . LEU A  1 976  ? -16.830 69.491  85.945  1.00 21.90 ? 974  LEU A C     1 
ATOM   7095  O O     . LEU A  1 976  ? -17.260 68.496  86.539  1.00 20.33 ? 974  LEU A O     1 
ATOM   7096  C CB    . LEU A  1 976  ? -14.406 69.563  86.564  1.00 22.57 ? 974  LEU A CB    1 
ATOM   7097  C CG    . LEU A  1 976  ? -13.984 69.034  85.205  1.00 22.10 ? 974  LEU A CG    1 
ATOM   7098  C CD1   . LEU A  1 976  ? -13.581 70.202  84.275  1.00 20.51 ? 974  LEU A CD1   1 
ATOM   7099  C CD2   . LEU A  1 976  ? -12.846 68.046  85.437  1.00 20.73 ? 974  LEU A CD2   1 
ATOM   7100  N N     . HIS A  1 977  ? -17.294 69.905  84.759  1.00 20.22 ? 975  HIS A N     1 
ATOM   7101  C CA    . HIS A  1 977  ? -18.240 69.142  83.953  1.00 21.88 ? 975  HIS A CA    1 
ATOM   7102  C C     . HIS A  1 977  ? -17.527 68.673  82.694  1.00 19.50 ? 975  HIS A C     1 
ATOM   7103  O O     . HIS A  1 977  ? -17.202 69.483  81.810  1.00 20.59 ? 975  HIS A O     1 
ATOM   7104  C CB    . HIS A  1 977  ? -19.462 69.969  83.589  1.00 21.04 ? 975  HIS A CB    1 
ATOM   7105  C CG    . HIS A  1 977  ? -20.566 69.848  84.583  1.00 22.89 ? 975  HIS A CG    1 
ATOM   7106  N ND1   . HIS A  1 977  ? -21.619 68.975  84.415  1.00 24.50 ? 975  HIS A ND1   1 
ATOM   7107  C CD2   . HIS A  1 977  ? -20.741 70.427  85.793  1.00 24.63 ? 975  HIS A CD2   1 
ATOM   7108  C CE1   . HIS A  1 977  ? -22.430 69.072  85.451  1.00 25.06 ? 975  HIS A CE1   1 
ATOM   7109  N NE2   . HIS A  1 977  ? -21.922 69.946  86.301  1.00 24.67 ? 975  HIS A NE2   1 
ATOM   7110  N N     . THR A  1 978  ? -17.292 67.372  82.631  1.00 20.26 ? 976  THR A N     1 
ATOM   7111  C CA    . THR A  1 978  ? -16.664 66.714  81.493  1.00 23.66 ? 976  THR A CA    1 
ATOM   7112  C C     . THR A  1 978  ? -16.979 65.231  81.601  1.00 22.93 ? 976  THR A C     1 
ATOM   7113  O O     . THR A  1 978  ? -17.169 64.703  82.700  1.00 21.92 ? 976  THR A O     1 
ATOM   7114  C CB    . THR A  1 978  ? -15.142 66.927  81.457  1.00 22.57 ? 976  THR A CB    1 
ATOM   7115  O OG1   . THR A  1 978  ? -14.597 66.248  80.319  1.00 21.78 ? 976  THR A OG1   1 
ATOM   7116  C CG2   . THR A  1 978  ? -14.488 66.359  82.697  1.00 21.65 ? 976  THR A CG2   1 
ATOM   7117  N N     . ARG A  1 979  ? -17.029 64.563  80.459  1.00 24.48 ? 977  ARG A N     1 
ATOM   7118  C CA    . ARG A  1 979  ? -17.094 63.109  80.454  1.00 24.42 ? 977  ARG A CA    1 
ATOM   7119  C C     . ARG A  1 979  ? -15.729 62.446  80.268  1.00 25.44 ? 977  ARG A C     1 
ATOM   7120  O O     . ARG A  1 979  ? -15.643 61.216  80.338  1.00 26.27 ? 977  ARG A O     1 
ATOM   7121  C CB    . ARG A  1 979  ? -18.041 62.634  79.358  1.00 23.98 ? 977  ARG A CB    1 
ATOM   7122  C CG    . ARG A  1 979  ? -19.477 63.009  79.617  1.00 30.09 ? 977  ARG A CG    1 
ATOM   7123  C CD    . ARG A  1 979  ? -20.304 62.779  78.390  1.00 35.43 ? 977  ARG A CD    1 
ATOM   7124  N NE    . ARG A  1 979  ? -21.721 62.908  78.689  1.00 39.88 ? 977  ARG A NE    1 
ATOM   7125  C CZ    . ARG A  1 979  ? -22.690 62.638  77.826  1.00 43.95 ? 977  ARG A CZ    1 
ATOM   7126  N NH1   . ARG A  1 979  ? -22.421 62.212  76.600  1.00 37.18 ? 977  ARG A NH1   1 
ATOM   7127  N NH2   . ARG A  1 979  ? -23.959 62.797  78.205  1.00 45.14 ? 977  ARG A NH2   1 
ATOM   7128  N N     . LEU A  1 980  ? -14.673 63.216  80.048  1.00 21.66 ? 978  LEU A N     1 
ATOM   7129  C CA    . LEU A  1 980  ? -13.401 62.676  79.571  1.00 21.91 ? 978  LEU A CA    1 
ATOM   7130  C C     . LEU A  1 980  ? -12.413 62.503  80.721  1.00 22.53 ? 978  LEU A C     1 
ATOM   7131  O O     . LEU A  1 980  ? -12.089 63.474  81.415  1.00 22.56 ? 978  LEU A O     1 
ATOM   7132  C CB    . LEU A  1 980  ? -12.809 63.588  78.509  1.00 21.18 ? 978  LEU A CB    1 
ATOM   7133  C CG    . LEU A  1 980  ? -13.787 63.915  77.390  1.00 23.59 ? 978  LEU A CG    1 
ATOM   7134  C CD1   . LEU A  1 980  ? -13.144 64.888  76.416  1.00 26.02 ? 978  LEU A CD1   1 
ATOM   7135  C CD2   . LEU A  1 980  ? -14.248 62.636  76.704  1.00 25.80 ? 978  LEU A CD2   1 
ATOM   7136  N N     . ASP A  1 981  ? -11.937 61.264  80.908  1.00 21.04 ? 979  ASP A N     1 
ATOM   7137  C CA    . ASP A  1 981  ? -10.996 60.963  81.989  1.00 21.17 ? 979  ASP A CA    1 
ATOM   7138  C C     . ASP A  1 981  ? -9.717  61.782  81.876  1.00 20.17 ? 979  ASP A C     1 
ATOM   7139  O O     . ASP A  1 981  ? -9.139  62.183  82.895  1.00 23.03 ? 979  ASP A O     1 
ATOM   7140  C CB    . ASP A  1 981  ? -10.648 59.475  81.982  1.00 21.72 ? 979  ASP A CB    1 
ATOM   7141  C CG    . ASP A  1 981  ? -11.752 58.610  82.521  1.00 25.89 ? 979  ASP A CG    1 
ATOM   7142  O OD1   . ASP A  1 981  ? -12.717 59.149  83.098  1.00 29.13 ? 979  ASP A OD1   1 
ATOM   7143  O OD2   . ASP A  1 981  ? -11.658 57.373  82.339  1.00 30.88 ? 979  ASP A OD2   1 
ATOM   7144  N N     . GLU A  1 982  ? -9.225  62.004  80.655  1.00 20.84 ? 980  GLU A N     1 
ATOM   7145  C CA    . GLU A  1 982  ? -7.976  62.751  80.532  1.00 22.88 ? 980  GLU A CA    1 
ATOM   7146  C C     . GLU A  1 982  ? -8.143  64.169  81.059  1.00 24.45 ? 980  GLU A C     1 
ATOM   7147  O O     . GLU A  1 982  ? -7.244  64.710  81.724  1.00 20.58 ? 980  GLU A O     1 
ATOM   7148  C CB    . GLU A  1 982  ? -7.484  62.773  79.083  1.00 22.37 ? 980  GLU A CB    1 
ATOM   7149  C CG    . GLU A  1 982  ? -6.291  63.717  78.922  1.00 25.99 ? 980  GLU A CG    1 
ATOM   7150  C CD    . GLU A  1 982  ? -5.999  64.108  77.471  1.00 30.73 ? 980  GLU A CD    1 
ATOM   7151  O OE1   . GLU A  1 982  ? -6.882  64.718  76.819  1.00 34.88 ? 980  GLU A OE1   1 
ATOM   7152  O OE2   . GLU A  1 982  ? -4.882  63.808  76.990  1.00 31.14 ? 980  GLU A OE2   1 
ATOM   7153  N N     . THR A  1 983  ? -9.302  64.779  80.784  1.00 22.22 ? 981  THR A N     1 
ATOM   7154  C CA    . THR A  1 983  ? -9.579  66.125  81.285  1.00 21.82 ? 981  THR A CA    1 
ATOM   7155  C C     . THR A  1 983  ? -9.785  66.120  82.795  1.00 21.83 ? 981  THR A C     1 
ATOM   7156  O O     . THR A  1 983  ? -9.330  67.039  83.492  1.00 22.58 ? 981  THR A O     1 
ATOM   7157  C CB    . THR A  1 983  ? -10.801 66.708  80.570  1.00 22.41 ? 981  THR A CB    1 
ATOM   7158  O OG1   . THR A  1 983  ? -10.550 66.756  79.158  1.00 22.99 ? 981  THR A OG1   1 
ATOM   7159  C CG2   . THR A  1 983  ? -11.110 68.123  81.070  1.00 22.71 ? 981  THR A CG2   1 
ATOM   7160  N N     . ILE A  1 984  ? -10.464 65.095  83.321  1.00 20.33 ? 982  ILE A N     1 
ATOM   7161  C CA    . ILE A  1 984  ? -10.602 64.968  84.775  1.00 22.60 ? 982  ILE A CA    1 
ATOM   7162  C C     . ILE A  1 984  ? -9.238  64.857  85.439  1.00 23.75 ? 982  ILE A C     1 
ATOM   7163  O O     . ILE A  1 984  ? -8.961  65.532  86.440  1.00 20.36 ? 982  ILE A O     1 
ATOM   7164  C CB    . ILE A  1 984  ? -11.494 63.769  85.140  1.00 17.21 ? 982  ILE A CB    1 
ATOM   7165  C CG1   . ILE A  1 984  ? -12.921 64.047  84.680  1.00 21.40 ? 982  ILE A CG1   1 
ATOM   7166  C CG2   . ILE A  1 984  ? -11.473 63.527  86.636  1.00 19.50 ? 982  ILE A CG2   1 
ATOM   7167  C CD1   . ILE A  1 984  ? -13.847 62.846  84.785  1.00 24.91 ? 982  ILE A CD1   1 
ATOM   7168  N N     . ALA A  1 985  ? -8.376  63.979  84.912  1.00 21.86 ? 983  ALA A N     1 
ATOM   7169  C CA    . ALA A  1 985  ? -7.062  63.778  85.525  1.00 25.88 ? 983  ALA A CA    1 
ATOM   7170  C C     . ALA A  1 985  ? -6.257  65.068  85.519  1.00 21.84 ? 983  ALA A C     1 
ATOM   7171  O O     . ALA A  1 985  ? -5.727  65.484  86.552  1.00 23.91 ? 983  ALA A O     1 
ATOM   7172  C CB    . ALA A  1 985  ? -6.294  62.666  84.803  1.00 23.75 ? 983  ALA A CB    1 
ATOM   7173  N N     . HIS A  1 986  ? -6.191  65.726  84.361  1.00 20.27 ? 984  HIS A N     1 
ATOM   7174  C CA    . HIS A  1 986  ? -5.464  66.982  84.201  1.00 23.39 ? 984  HIS A CA    1 
ATOM   7175  C C     . HIS A  1 986  ? -5.964  68.044  85.167  1.00 24.29 ? 984  HIS A C     1 
ATOM   7176  O O     . HIS A  1 986  ? -5.202  68.591  85.973  1.00 24.24 ? 984  HIS A O     1 
ATOM   7177  C CB    . HIS A  1 986  ? -5.622  67.455  82.752  1.00 24.87 ? 984  HIS A CB    1 
ATOM   7178  C CG    . HIS A  1 986  ? -5.096  68.829  82.472  1.00 27.76 ? 984  HIS A CG    1 
ATOM   7179  N ND1   . HIS A  1 986  ? -5.323  69.462  81.272  1.00 32.04 ? 984  HIS A ND1   1 
ATOM   7180  C CD2   . HIS A  1 986  ? -4.346  69.682  83.209  1.00 25.27 ? 984  HIS A CD2   1 
ATOM   7181  C CE1   . HIS A  1 986  ? -4.747  70.652  81.285  1.00 31.04 ? 984  HIS A CE1   1 
ATOM   7182  N NE2   . HIS A  1 986  ? -4.156  70.813  82.452  1.00 25.47 ? 984  HIS A NE2   1 
ATOM   7183  N N     . VAL A  1 987  ? -7.249  68.375  85.068  1.00 20.75 ? 985  VAL A N     1 
ATOM   7184  C CA    . VAL A  1 987  ? -7.791  69.506  85.816  1.00 23.05 ? 985  VAL A CA    1 
ATOM   7185  C C     . VAL A  1 987  ? -7.707  69.254  87.322  1.00 24.61 ? 985  VAL A C     1 
ATOM   7186  O O     . VAL A  1 987  ? -7.259  70.118  88.087  1.00 23.71 ? 985  VAL A O     1 
ATOM   7187  C CB    . VAL A  1 987  ? -9.231  69.784  85.358  1.00 20.75 ? 985  VAL A CB    1 
ATOM   7188  C CG1   . VAL A  1 987  ? -9.941  70.726  86.316  1.00 21.64 ? 985  VAL A CG1   1 
ATOM   7189  C CG2   . VAL A  1 987  ? -9.216  70.379  83.940  1.00 21.38 ? 985  VAL A CG2   1 
ATOM   7190  N N     . THR A  1 988  ? -8.145  68.078  87.774  1.00 22.16 ? 986  THR A N     1 
ATOM   7191  C CA    . THR A  1 988  ? -8.111  67.841  89.217  1.00 23.62 ? 986  THR A CA    1 
ATOM   7192  C C     . THR A  1 988  ? -6.689  67.706  89.742  1.00 28.18 ? 986  THR A C     1 
ATOM   7193  O O     . THR A  1 988  ? -6.469  67.907  90.941  1.00 25.26 ? 986  THR A O     1 
ATOM   7194  C CB    . THR A  1 988  ? -8.921  66.600  89.618  1.00 27.78 ? 986  THR A CB    1 
ATOM   7195  O OG1   . THR A  1 988  ? -8.325  65.416  89.077  1.00 24.44 ? 986  THR A OG1   1 
ATOM   7196  C CG2   . THR A  1 988  ? -10.355 66.713  89.138  1.00 28.45 ? 986  THR A CG2   1 
ATOM   7197  N N     . SER A  1 989  ? -5.707  67.404  88.888  1.00 23.16 ? 987  SER A N     1 
ATOM   7198  C CA    . SER A  1 989  ? -4.343  67.375  89.410  1.00 27.34 ? 987  SER A CA    1 
ATOM   7199  C C     . SER A  1 989  ? -3.724  68.768  89.484  1.00 28.24 ? 987  SER A C     1 
ATOM   7200  O O     . SER A  1 989  ? -2.819  68.982  90.296  1.00 30.64 ? 987  SER A O     1 
ATOM   7201  C CB    . SER A  1 989  ? -3.449  66.423  88.594  1.00 26.91 ? 987  SER A CB    1 
ATOM   7202  O OG    . SER A  1 989  ? -3.175  66.915  87.297  1.00 31.93 ? 987  SER A OG    1 
ATOM   7203  N N     . ARG A  1 990  ? -4.225  69.730  88.708  1.00 26.53 ? 988  ARG A N     1 
ATOM   7204  C CA    . ARG A  1 990  ? -3.635  71.065  88.643  1.00 25.80 ? 988  ARG A CA    1 
ATOM   7205  C C     . ARG A  1 990  ? -4.377  72.103  89.471  1.00 26.63 ? 988  ARG A C     1 
ATOM   7206  O O     . ARG A  1 990  ? -3.765  73.086  89.893  1.00 24.98 ? 988  ARG A O     1 
ATOM   7207  C CB    . ARG A  1 990  ? -3.580  71.548  87.193  1.00 27.22 ? 988  ARG A CB    1 
ATOM   7208  C CG    . ARG A  1 990  ? -2.752  70.642  86.323  1.00 32.04 ? 988  ARG A CG    1 
ATOM   7209  C CD    . ARG A  1 990  ? -1.272  70.905  86.510  1.00 34.81 ? 988  ARG A CD    1 
ATOM   7210  N NE    . ARG A  1 990  ? -0.793  71.788  85.454  1.00 33.68 ? 988  ARG A NE    1 
ATOM   7211  C CZ    . ARG A  1 990  ? 0.446   72.244  85.361  1.00 32.96 ? 988  ARG A CZ    1 
ATOM   7212  N NH1   . ARG A  1 990  ? 1.333   72.025  86.318  1.00 33.76 ? 988  ARG A NH1   1 
ATOM   7213  N NH2   . ARG A  1 990  ? 0.804   72.927  84.279  1.00 32.48 ? 988  ARG A NH2   1 
ATOM   7214  N N     . ILE A  1 991  ? -5.680  71.915  89.692  1.00 25.91 ? 989  ILE A N     1 
ATOM   7215  C CA    . ILE A  1 991  ? -6.459  72.858  90.484  1.00 24.07 ? 989  ILE A CA    1 
ATOM   7216  C C     . ILE A  1 991  ? -6.042  72.777  91.947  1.00 25.38 ? 989  ILE A C     1 
ATOM   7217  O O     . ILE A  1 991  ? -5.659  71.713  92.455  1.00 27.47 ? 989  ILE A O     1 
ATOM   7218  C CB    . ILE A  1 991  ? -7.966  72.581  90.315  1.00 25.30 ? 989  ILE A CB    1 
ATOM   7219  C CG1   . ILE A  1 991  ? -8.790  73.776  90.784  1.00 23.36 ? 989  ILE A CG1   1 
ATOM   7220  C CG2   . ILE A  1 991  ? -8.366  71.270  91.005  1.00 25.18 ? 989  ILE A CG2   1 
ATOM   7221  C CD1   . ILE A  1 991  ? -8.647  74.998  89.874  1.00 27.77 ? 989  ILE A CD1   1 
ATOM   7222  N N     . LYS A  1 992  ? -6.102  73.914  92.633  1.00 22.73 ? 990  LYS A N     1 
ATOM   7223  C CA    . LYS A  1 992  ? -5.714  73.997  94.044  1.00 27.17 ? 990  LYS A CA    1 
ATOM   7224  C C     . LYS A  1 992  ? -6.925  74.454  94.855  1.00 28.42 ? 990  LYS A C     1 
ATOM   7225  O O     . LYS A  1 992  ? -7.051  75.629  95.210  1.00 29.07 ? 990  LYS A O     1 
ATOM   7226  C CB    . LYS A  1 992  ? -4.521  74.933  94.226  1.00 25.79 ? 990  LYS A CB    1 
ATOM   7227  C CG    . LYS A  1 992  ? -3.215  74.344  93.709  1.00 29.42 ? 990  LYS A CG    1 
ATOM   7228  C CD    . LYS A  1 992  ? -2.054  75.344  93.884  1.00 37.24 ? 990  LYS A CD    1 
ATOM   7229  C CE    . LYS A  1 992  ? -0.710  74.729  93.473  1.00 44.16 ? 990  LYS A CE    1 
ATOM   7230  N NZ    . LYS A  1 992  ? 0.401   75.733  93.487  1.00 51.66 ? 990  LYS A NZ    1 
ATOM   7231  N N     . ALA A  1 993  ? -7.812  73.513  95.163  1.00 26.99 ? 991  ALA A N     1 
ATOM   7232  C CA    . ALA A  1 993  ? -9.013  73.828  95.927  1.00 27.65 ? 991  ALA A CA    1 
ATOM   7233  C C     . ALA A  1 993  ? -9.317  72.708  96.906  1.00 24.48 ? 991  ALA A C     1 
ATOM   7234  O O     . ALA A  1 993  ? -8.962  71.551  96.675  1.00 25.41 ? 991  ALA A O     1 
ATOM   7235  C CB    . ALA A  1 993  ? -10.213 74.050  95.011  1.00 23.31 ? 991  ALA A CB    1 
ATOM   7236  N N     . GLY A  1 994  ? -10.008 73.065  97.995  1.00 22.20 ? 992  GLY A N     1 
ATOM   7237  C CA    . GLY A  1 994  ? -10.292 72.102  99.042  1.00 23.68 ? 992  GLY A CA    1 
ATOM   7238  C C     . GLY A  1 994  ? -11.457 71.170  98.779  1.00 22.11 ? 992  GLY A C     1 
ATOM   7239  O O     . GLY A  1 994  ? -11.494 70.059  99.320  1.00 22.08 ? 992  GLY A O     1 
ATOM   7240  N N     . ASN A  1 995  ? -12.425 71.595  97.975  1.00 23.14 ? 993  ASN A N     1 
ATOM   7241  C CA    . ASN A  1 995  ? -13.625 70.802  97.722  1.00 24.52 ? 993  ASN A CA    1 
ATOM   7242  C C     . ASN A  1 995  ? -13.876 70.776  96.227  1.00 18.90 ? 993  ASN A C     1 
ATOM   7243  O O     . ASN A  1 995  ? -14.237 71.803  95.641  1.00 20.21 ? 993  ASN A O     1 
ATOM   7244  C CB    . ASN A  1 995  ? -14.837 71.373  98.450  1.00 21.54 ? 993  ASN A CB    1 
ATOM   7245  C CG    . ASN A  1 995  ? -14.859 70.959  99.907  1.00 23.31 ? 993  ASN A CG    1 
ATOM   7246  O OD1   . ASN A  1 995  ? -14.148 71.529  100.729 1.00 23.54 ? 993  ASN A OD1   1 
ATOM   7247  N ND2   . ASN A  1 995  ? -15.643 69.937  100.223 1.00 20.66 ? 993  ASN A ND2   1 
ATOM   7248  N N     . LEU A  1 996  ? -13.651 69.621  95.626  1.00 22.10 ? 994  LEU A N     1 
ATOM   7249  C CA    . LEU A  1 996  ? -13.803 69.442  94.194  1.00 18.74 ? 994  LEU A CA    1 
ATOM   7250  C C     . LEU A  1 996  ? -15.109 68.707  93.917  1.00 20.02 ? 994  LEU A C     1 
ATOM   7251  O O     . LEU A  1 996  ? -15.540 67.862  94.697  1.00 19.01 ? 994  LEU A O     1 
ATOM   7252  C CB    . LEU A  1 996  ? -12.629 68.644  93.627  1.00 18.01 ? 994  LEU A CB    1 
ATOM   7253  C CG    . LEU A  1 996  ? -11.255 69.214  94.027  1.00 22.21 ? 994  LEU A CG    1 
ATOM   7254  C CD1   . LEU A  1 996  ? -10.130 68.451  93.371  1.00 24.70 ? 994  LEU A CD1   1 
ATOM   7255  C CD2   . LEU A  1 996  ? -11.141 70.714  93.707  1.00 24.03 ? 994  LEU A CD2   1 
ATOM   7256  N N     . TYR A  1 997  ? -15.715 69.008  92.777  1.00 19.46 ? 995  TYR A N     1 
ATOM   7257  C CA    . TYR A  1 997  ? -17.002 68.413  92.432  1.00 18.38 ? 995  TYR A CA    1 
ATOM   7258  C C     . TYR A  1 997  ? -16.975 68.118  90.949  1.00 17.49 ? 995  TYR A C     1 
ATOM   7259  O O     . TYR A  1 997  ? -16.665 69.011  90.157  1.00 20.24 ? 995  TYR A O     1 
ATOM   7260  C CB    . TYR A  1 997  ? -18.162 69.354  92.751  1.00 19.05 ? 995  TYR A CB    1 
ATOM   7261  C CG    . TYR A  1 997  ? -18.291 69.630  94.214  1.00 19.53 ? 995  TYR A CG    1 
ATOM   7262  C CD1   . TYR A  1 997  ? -18.935 68.725  95.049  1.00 21.54 ? 995  TYR A CD1   1 
ATOM   7263  C CD2   . TYR A  1 997  ? -17.744 70.785  94.774  1.00 20.52 ? 995  TYR A CD2   1 
ATOM   7264  C CE1   . TYR A  1 997  ? -19.054 68.968  96.413  1.00 21.77 ? 995  TYR A CE1   1 
ATOM   7265  C CE2   . TYR A  1 997  ? -17.851 71.033  96.138  1.00 22.07 ? 995  TYR A CE2   1 
ATOM   7266  C CZ    . TYR A  1 997  ? -18.505 70.115  96.947  1.00 24.54 ? 995  TYR A CZ    1 
ATOM   7267  O OH    . TYR A  1 997  ? -18.624 70.346  98.306  1.00 25.77 ? 995  TYR A OH    1 
ATOM   7268  N N     . ILE A  1 998  ? -17.298 66.885  90.576  1.00 15.67 ? 996  ILE A N     1 
ATOM   7269  C CA    A ILE A  1 998  ? -17.236 66.463  89.182  0.48 18.28 ? 996  ILE A CA    1 
ATOM   7270  C CA    B ILE A  1 998  ? -17.232 66.439  89.186  0.52 18.61 ? 996  ILE A CA    1 
ATOM   7271  C C     . ILE A  1 998  ? -18.642 66.079  88.738  1.00 16.77 ? 996  ILE A C     1 
ATOM   7272  O O     . ILE A  1 998  ? -19.249 65.159  89.292  1.00 18.83 ? 996  ILE A O     1 
ATOM   7273  C CB    A ILE A  1 998  ? -16.241 65.312  88.974  0.48 20.43 ? 996  ILE A CB    1 
ATOM   7274  C CB    B ILE A  1 998  ? -16.291 65.238  89.017  0.52 20.75 ? 996  ILE A CB    1 
ATOM   7275  C CG1   A ILE A  1 998  ? -14.826 65.773  89.363  0.48 19.72 ? 996  ILE A CG1   1 
ATOM   7276  C CG1   B ILE A  1 998  ? -14.937 65.518  89.682  0.52 19.89 ? 996  ILE A CG1   1 
ATOM   7277  C CG2   A ILE A  1 998  ? -16.270 64.854  87.525  0.48 18.99 ? 996  ILE A CG2   1 
ATOM   7278  C CG2   B ILE A  1 998  ? -16.120 64.924  87.536  0.52 19.00 ? 996  ILE A CG2   1 
ATOM   7279  C CD1   A ILE A  1 998  ? -13.770 64.679  89.323  0.48 19.68 ? 996  ILE A CD1   1 
ATOM   7280  C CD1   B ILE A  1 998  ? -14.099 66.523  88.942  0.52 19.14 ? 996  ILE A CD1   1 
ATOM   7281  N N     . ASN A  1 999  ? -19.148 66.793  87.731  1.00 17.86 ? 997  ASN A N     1 
ATOM   7282  C CA    . ASN A  1 999  ? -20.435 66.515  87.089  1.00 20.37 ? 997  ASN A CA    1 
ATOM   7283  C C     . ASN A  1 999  ? -21.629 66.674  88.035  1.00 18.61 ? 997  ASN A C     1 
ATOM   7284  O O     . ASN A  1 999  ? -22.589 65.903  87.978  1.00 18.69 ? 997  ASN A O     1 
ATOM   7285  C CB    . ASN A  1 999  ? -20.405 65.132  86.430  1.00 20.94 ? 997  ASN A CB    1 
ATOM   7286  C CG    . ASN A  1 999  ? -19.432 65.084  85.250  1.00 21.36 ? 997  ASN A CG    1 
ATOM   7287  O OD1   . ASN A  1 999  ? -19.205 66.098  84.603  1.00 22.34 ? 997  ASN A OD1   1 
ATOM   7288  N ND2   . ASN A  1 999  ? -18.875 63.912  84.967  1.00 20.54 ? 997  ASN A ND2   1 
ATOM   7289  N N     . ARG A  1 1000 ? -21.572 67.688  88.900  1.00 22.59 ? 998  ARG A N     1 
ATOM   7290  C CA    . ARG A  1 1000 ? -22.640 67.998  89.849  1.00 18.78 ? 998  ARG A CA    1 
ATOM   7291  C C     . ARG A  1 1000 ? -22.488 69.461  90.257  1.00 20.47 ? 998  ARG A C     1 
ATOM   7292  O O     . ARG A  1 1000 ? -21.567 70.146  89.810  1.00 21.74 ? 998  ARG A O     1 
ATOM   7293  C CB    . ARG A  1 1000 ? -22.606 67.060  91.061  1.00 19.31 ? 998  ARG A CB    1 
ATOM   7294  C CG    . ARG A  1 1000 ? -21.196 66.871  91.698  1.00 18.59 ? 998  ARG A CG    1 
ATOM   7295  C CD    . ARG A  1 1000 ? -21.333 66.509  93.176  1.00 19.81 ? 998  ARG A CD    1 
ATOM   7296  N NE    . ARG A  1 1000 ? -21.945 67.600  93.926  1.00 21.33 ? 998  ARG A NE    1 
ATOM   7297  C CZ    . ARG A  1 1000 ? -22.187 67.553  95.233  1.00 22.42 ? 998  ARG A CZ    1 
ATOM   7298  N NH1   . ARG A  1 1000 ? -21.924 66.470  95.940  1.00 23.69 ? 998  ARG A NH1   1 
ATOM   7299  N NH2   . ARG A  1 1000 ? -22.704 68.620  95.842  1.00 22.41 ? 998  ARG A NH2   1 
ATOM   7300  N N     . ASN A  1 1001 ? -23.398 69.942  91.104  1.00 20.52 ? 999  ASN A N     1 
ATOM   7301  C CA    . ASN A  1 1001 ? -23.261 71.295  91.625  1.00 20.49 ? 999  ASN A CA    1 
ATOM   7302  C C     . ASN A  1 1001 ? -22.107 71.325  92.633  1.00 21.47 ? 999  ASN A C     1 
ATOM   7303  O O     . ASN A  1 1001 ? -21.549 70.291  92.993  1.00 21.03 ? 999  ASN A O     1 
ATOM   7304  C CB    . ASN A  1 1001 ? -24.583 71.788  92.244  1.00 19.30 ? 999  ASN A CB    1 
ATOM   7305  C CG    . ASN A  1 1001 ? -24.974 71.055  93.526  1.00 23.72 ? 999  ASN A CG    1 
ATOM   7306  O OD1   . ASN A  1 1001 ? -24.157 70.772  94.380  1.00 26.77 ? 999  ASN A OD1   1 
ATOM   7307  N ND2   . ASN A  1 1001 ? -26.256 70.777  93.663  1.00 28.51 ? 999  ASN A ND2   1 
ATOM   7308  N N     . ILE A  1 1002 ? -21.733 72.521  93.070  1.00 19.69 ? 1000 ILE A N     1 
ATOM   7309  C CA    . ILE A  1 1002 ? -20.570 72.674  93.936  1.00 23.41 ? 1000 ILE A CA    1 
ATOM   7310  C C     . ILE A  1 1002 ? -20.975 73.136  95.337  1.00 24.65 ? 1000 ILE A C     1 
ATOM   7311  O O     . ILE A  1 1002 ? -20.126 73.604  96.101  1.00 22.97 ? 1000 ILE A O     1 
ATOM   7312  C CB    . ILE A  1 1002 ? -19.520 73.617  93.311  1.00 22.87 ? 1000 ILE A CB    1 
ATOM   7313  C CG1   . ILE A  1 1002 ? -20.045 75.054  93.225  1.00 18.72 ? 1000 ILE A CG1   1 
ATOM   7314  C CG2   . ILE A  1 1002 ? -19.116 73.121  91.923  1.00 23.07 ? 1000 ILE A CG2   1 
ATOM   7315  C CD1   . ILE A  1 1002 ? -19.010 76.060  92.745  1.00 24.40 ? 1000 ILE A CD1   1 
ATOM   7316  N N     . ILE A  1 1003 ? -22.254 73.007  95.699  1.00 20.02 ? 1001 ILE A N     1 
ATOM   7317  C CA    . ILE A  1 1003 ? -22.747 73.537  96.969  1.00 23.53 ? 1001 ILE A CA    1 
ATOM   7318  C C     . ILE A  1 1003 ? -23.299 72.403  97.835  1.00 24.46 ? 1001 ILE A C     1 
ATOM   7319  O O     . ILE A  1 1003 ? -23.505 71.284  97.382  1.00 26.60 ? 1001 ILE A O     1 
ATOM   7320  C CB    . ILE A  1 1003 ? -23.815 74.639  96.781  1.00 20.89 ? 1001 ILE A CB    1 
ATOM   7321  C CG1   . ILE A  1 1003 ? -25.073 74.085  96.107  1.00 25.27 ? 1001 ILE A CG1   1 
ATOM   7322  C CG2   . ILE A  1 1003 ? -23.235 75.838  96.007  1.00 21.79 ? 1001 ILE A CG2   1 
ATOM   7323  C CD1   . ILE A  1 1003 ? -26.295 75.059  96.176  1.00 27.00 ? 1001 ILE A CD1   1 
ATOM   7324  N N     . GLY A  1 1004 ? -23.537 72.718  99.103  1.00 27.78 ? 1002 GLY A N     1 
ATOM   7325  C CA    . GLY A  1 1004 ? -24.155 71.757  100.007 1.00 27.60 ? 1002 GLY A CA    1 
ATOM   7326  C C     . GLY A  1 1004 ? -23.266 70.622  100.477 1.00 30.66 ? 1002 GLY A C     1 
ATOM   7327  O O     . GLY A  1 1004 ? -23.729 69.476  100.559 1.00 25.78 ? 1002 GLY A O     1 
ATOM   7328  N N     . ALA A  1 1005 ? -21.999 70.905  100.792 1.00 24.46 ? 1003 ALA A N     1 
ATOM   7329  C CA    . ALA A  1 1005 ? -21.104 69.867  101.288 1.00 24.84 ? 1003 ALA A CA    1 
ATOM   7330  C C     . ALA A  1 1005 ? -21.752 69.146  102.468 1.00 27.45 ? 1003 ALA A C     1 
ATOM   7331  O O     . ALA A  1 1005 ? -22.366 69.782  103.331 1.00 27.35 ? 1003 ALA A O     1 
ATOM   7332  C CB    . ALA A  1 1005 ? -19.763 70.490  101.703 1.00 25.37 ? 1003 ALA A CB    1 
ATOM   7333  N N     . VAL A  1 1006 ? -21.690 67.813  102.464 1.00 24.30 ? 1004 VAL A N     1 
ATOM   7334  C CA    . VAL A  1 1006 ? -22.337 66.995  103.497 1.00 25.68 ? 1004 VAL A CA    1 
ATOM   7335  C C     . VAL A  1 1006 ? -21.307 66.623  104.552 1.00 24.96 ? 1004 VAL A C     1 
ATOM   7336  O O     . VAL A  1 1006 ? -20.209 66.157  104.221 1.00 24.80 ? 1004 VAL A O     1 
ATOM   7337  C CB    . VAL A  1 1006 ? -22.991 65.737  102.898 1.00 24.91 ? 1004 VAL A CB    1 
ATOM   7338  C CG1   . VAL A  1 1006 ? -23.447 64.785  104.000 1.00 29.80 ? 1004 VAL A CG1   1 
ATOM   7339  C CG2   . VAL A  1 1006 ? -24.190 66.130  102.042 1.00 21.68 ? 1004 VAL A CG2   1 
ATOM   7340  N N     . VAL A  1 1007 ? -21.667 66.826  105.826 1.00 24.24 ? 1005 VAL A N     1 
ATOM   7341  C CA    . VAL A  1 1007 ? -20.784 66.503  106.939 1.00 22.35 ? 1005 VAL A CA    1 
ATOM   7342  C C     . VAL A  1 1007 ? -20.333 65.052  106.838 1.00 21.76 ? 1005 VAL A C     1 
ATOM   7343  O O     . VAL A  1 1007 ? -21.153 64.150  106.644 1.00 22.31 ? 1005 VAL A O     1 
ATOM   7344  C CB    . VAL A  1 1007 ? -21.504 66.768  108.277 1.00 23.68 ? 1005 VAL A CB    1 
ATOM   7345  C CG1   . VAL A  1 1007 ? -20.671 66.248  109.452 1.00 22.63 ? 1005 VAL A CG1   1 
ATOM   7346  C CG2   . VAL A  1 1007 ? -21.802 68.254  108.448 1.00 23.31 ? 1005 VAL A CG2   1 
ATOM   7347  N N     . GLY A  1 1008 ? -19.022 64.820  107.011 1.00 23.05 ? 1006 GLY A N     1 
ATOM   7348  C CA    . GLY A  1 1008 ? -18.477 63.473  107.029 1.00 19.85 ? 1006 GLY A CA    1 
ATOM   7349  C C     . GLY A  1 1008 ? -18.400 62.814  105.668 1.00 22.31 ? 1006 GLY A C     1 
ATOM   7350  O O     . GLY A  1 1008 ? -17.911 61.681  105.567 1.00 25.00 ? 1006 GLY A O     1 
ATOM   7351  N N     . VAL A  1 1009 ? -18.899 63.477  104.634 1.00 23.31 ? 1007 VAL A N     1 
ATOM   7352  C CA    . VAL A  1 1009 ? -18.969 62.944  103.279 1.00 25.29 ? 1007 VAL A CA    1 
ATOM   7353  C C     . VAL A  1 1009 ? -18.177 63.818  102.309 1.00 26.22 ? 1007 VAL A C     1 
ATOM   7354  O O     . VAL A  1 1009 ? -17.337 63.322  101.550 1.00 24.60 ? 1007 VAL A O     1 
ATOM   7355  C CB    . VAL A  1 1009 ? -20.439 62.790  102.807 1.00 26.25 ? 1007 VAL A CB    1 
ATOM   7356  C CG1   . VAL A  1 1009 ? -20.493 62.170  101.419 1.00 23.50 ? 1007 VAL A CG1   1 
ATOM   7357  C CG2   . VAL A  1 1009 ? -21.235 61.918  103.791 1.00 18.66 ? 1007 VAL A CG2   1 
ATOM   7358  N N     . GLN A  1 1010 ? -18.415 65.135  102.337 1.00 22.57 ? 1008 GLN A N     1 
ATOM   7359  C CA    . GLN A  1 1010 ? -17.501 66.119  101.757 1.00 24.01 ? 1008 GLN A CA    1 
ATOM   7360  C C     . GLN A  1 1010 ? -17.059 67.043  102.888 1.00 24.87 ? 1008 GLN A C     1 
ATOM   7361  O O     . GLN A  1 1010 ? -17.624 68.131  103.060 1.00 24.58 ? 1008 GLN A O     1 
ATOM   7362  C CB    . GLN A  1 1010 ? -18.132 66.913  100.615 1.00 24.67 ? 1008 GLN A CB    1 
ATOM   7363  C CG    . GLN A  1 1010 ? -18.691 66.061  99.465  1.00 26.22 ? 1008 GLN A CG    1 
ATOM   7364  C CD    . GLN A  1 1010 ? -20.194 65.878  99.566  1.00 25.99 ? 1008 GLN A CD    1 
ATOM   7365  O OE1   . GLN A  1 1010 ? -20.895 66.731  100.121 1.00 24.14 ? 1008 GLN A OE1   1 
ATOM   7366  N NE2   . GLN A  1 1010 ? -20.699 64.775  99.015  1.00 23.98 ? 1008 GLN A NE2   1 
ATOM   7367  N N     . PRO A  1 1011 ? -16.077 66.624  103.699 1.00 24.23 ? 1009 PRO A N     1 
ATOM   7368  C CA    . PRO A  1 1011 ? -15.500 67.528  104.708 1.00 23.98 ? 1009 PRO A CA    1 
ATOM   7369  C C     . PRO A  1 1011 ? -15.116 68.833  104.039 1.00 22.97 ? 1009 PRO A C     1 
ATOM   7370  O O     . PRO A  1 1011 ? -14.569 68.838  102.943 1.00 23.69 ? 1009 PRO A O     1 
ATOM   7371  C CB    . PRO A  1 1011 ? -14.266 66.763  105.210 1.00 22.61 ? 1009 PRO A CB    1 
ATOM   7372  C CG    . PRO A  1 1011 ? -14.571 65.333  104.952 1.00 24.12 ? 1009 PRO A CG    1 
ATOM   7373  C CD    . PRO A  1 1011 ? -15.396 65.317  103.667 1.00 22.91 ? 1009 PRO A CD    1 
ATOM   7374  N N     . PHE A  1 1012 ? -15.449 69.945  104.677 1.00 22.36 ? 1010 PHE A N     1 
ATOM   7375  C CA    . PHE A  1 1012 ? -15.552 71.203  103.966 1.00 23.19 ? 1010 PHE A CA    1 
ATOM   7376  C C     . PHE A  1 1012 ? -14.518 72.204  104.448 1.00 23.48 ? 1010 PHE A C     1 
ATOM   7377  O O     . PHE A  1 1012 ? -14.409 72.476  105.648 1.00 24.54 ? 1010 PHE A O     1 
ATOM   7378  C CB    . PHE A  1 1012 ? -16.958 71.796  104.099 1.00 22.49 ? 1010 PHE A CB    1 
ATOM   7379  C CG    . PHE A  1 1012 ? -17.139 73.043  103.292 1.00 25.63 ? 1010 PHE A CG    1 
ATOM   7380  C CD1   . PHE A  1 1012 ? -17.237 72.975  101.903 1.00 24.67 ? 1010 PHE A CD1   1 
ATOM   7381  C CD2   . PHE A  1 1012 ? -17.173 74.287  103.914 1.00 29.47 ? 1010 PHE A CD2   1 
ATOM   7382  C CE1   . PHE A  1 1012 ? -17.390 74.123  101.158 1.00 26.39 ? 1010 PHE A CE1   1 
ATOM   7383  C CE2   . PHE A  1 1012 ? -17.322 75.443  103.175 1.00 27.18 ? 1010 PHE A CE2   1 
ATOM   7384  C CZ    . PHE A  1 1012 ? -17.442 75.359  101.795 1.00 25.14 ? 1010 PHE A CZ    1 
ATOM   7385  N N     . GLY A  1 1013 ? -13.804 72.799  103.503 1.00 24.37 ? 1011 GLY A N     1 
ATOM   7386  C CA    . GLY A  1 1013 ? -12.813 73.789  103.863 1.00 25.60 ? 1011 GLY A CA    1 
ATOM   7387  C C     . GLY A  1 1013 ? -11.769 73.881  102.782 1.00 23.76 ? 1011 GLY A C     1 
ATOM   7388  O O     . GLY A  1 1013 ? -11.443 72.871  102.155 1.00 24.03 ? 1011 GLY A O     1 
ATOM   7389  N N     . GLY A  1 1014 ? -11.237 75.081  102.558 1.00 27.58 ? 1012 GLY A N     1 
ATOM   7390  C CA    . GLY A  1 1014 ? -10.322 75.328  101.475 1.00 29.34 ? 1012 GLY A CA    1 
ATOM   7391  C C     . GLY A  1 1014 ? -8.930  75.700  101.941 1.00 29.86 ? 1012 GLY A C     1 
ATOM   7392  O O     . GLY A  1 1014 ? -8.535  75.456  103.089 1.00 31.18 ? 1012 GLY A O     1 
ATOM   7393  N N     . ARG A  1 1015 ? -8.175  76.314  101.034 1.00 26.69 ? 1013 ARG A N     1 
ATOM   7394  C CA    A ARG A  1 1015 ? -6.785  76.688  101.261 0.56 30.35 ? 1013 ARG A CA    1 
ATOM   7395  C CA    B ARG A  1 1015 ? -6.789  76.692  101.274 0.44 30.34 ? 1013 ARG A CA    1 
ATOM   7396  C C     . ARG A  1 1015 ? -6.579  78.127  100.811 1.00 28.53 ? 1013 ARG A C     1 
ATOM   7397  O O     . ARG A  1 1015 ? -7.490  78.770  100.289 1.00 27.06 ? 1013 ARG A O     1 
ATOM   7398  C CB    A ARG A  1 1015 ? -5.830  75.755  100.506 0.56 30.94 ? 1013 ARG A CB    1 
ATOM   7399  C CB    B ARG A  1 1015 ? -5.829  75.740  100.550 0.44 30.94 ? 1013 ARG A CB    1 
ATOM   7400  C CG    A ARG A  1 1015 ? -6.094  75.720  99.004  0.56 29.82 ? 1013 ARG A CG    1 
ATOM   7401  C CG    B ARG A  1 1015 ? -6.255  75.455  99.115  0.44 29.92 ? 1013 ARG A CG    1 
ATOM   7402  C CD    A ARG A  1 1015 ? -4.802  75.602  98.198  0.56 31.11 ? 1013 ARG A CD    1 
ATOM   7403  C CD    B ARG A  1 1015 ? -5.073  75.217  98.179  0.44 31.06 ? 1013 ARG A CD    1 
ATOM   7404  N NE    A ARG A  1 1015 ? -4.121  76.885  98.052  0.56 31.22 ? 1013 ARG A NE    1 
ATOM   7405  N NE    B ARG A  1 1015 ? -3.782  75.305  98.849  0.44 32.04 ? 1013 ARG A NE    1 
ATOM   7406  C CZ    A ARG A  1 1015 ? -4.447  77.813  97.159  0.56 31.62 ? 1013 ARG A CZ    1 
ATOM   7407  C CZ    B ARG A  1 1015 ? -2.961  76.345  98.777  0.44 32.68 ? 1013 ARG A CZ    1 
ATOM   7408  N NH1   A ARG A  1 1015 ? -5.458  77.646  96.322  0.56 25.43 ? 1013 ARG A NH1   1 
ATOM   7409  N NH1   B ARG A  1 1015 ? -3.255  77.410  98.052  0.44 32.30 ? 1013 ARG A NH1   1 
ATOM   7410  N NH2   A ARG A  1 1015 ? -3.738  78.941  97.104  0.56 32.32 ? 1013 ARG A NH2   1 
ATOM   7411  N NH2   B ARG A  1 1015 ? -1.814  76.312  99.451  0.44 30.59 ? 1013 ARG A NH2   1 
ATOM   7412  N N     . GLY A  1 1016 ? -5.358  78.623  100.996 1.00 30.70 ? 1014 GLY A N     1 
ATOM   7413  C CA    . GLY A  1 1016 ? -5.042  79.966  100.539 1.00 27.72 ? 1014 GLY A CA    1 
ATOM   7414  C C     . GLY A  1 1016 ? -5.893  80.989  101.252 1.00 30.38 ? 1014 GLY A C     1 
ATOM   7415  O O     . GLY A  1 1016 ? -6.063  80.941  102.475 1.00 31.23 ? 1014 GLY A O     1 
ATOM   7416  N N     . LEU A  1 1017 ? -6.455  81.921  100.478 1.00 27.55 ? 1015 LEU A N     1 
ATOM   7417  C CA    . LEU A  1 1017 ? -7.320  82.968  101.013 1.00 30.70 ? 1015 LEU A CA    1 
ATOM   7418  C C     . LEU A  1 1017 ? -8.656  82.437  101.516 1.00 30.09 ? 1015 LEU A C     1 
ATOM   7419  O O     . LEU A  1 1017 ? -9.465  83.216  102.033 1.00 28.66 ? 1015 LEU A O     1 
ATOM   7420  C CB    . LEU A  1 1017 ? -7.568  84.031  99.945  1.00 28.22 ? 1015 LEU A CB    1 
ATOM   7421  C CG    . LEU A  1 1017 ? -6.368  84.820  99.427  1.00 34.66 ? 1015 LEU A CG    1 
ATOM   7422  C CD1   . LEU A  1 1017 ? -6.809  85.730  98.291  1.00 33.55 ? 1015 LEU A CD1   1 
ATOM   7423  C CD2   . LEU A  1 1017 ? -5.758  85.643  100.562 1.00 33.89 ? 1015 LEU A CD2   1 
ATOM   7424  N N     . SER A  1 1018 ? -8.914  81.144  101.374 1.00 27.94 ? 1016 SER A N     1 
ATOM   7425  C CA    . SER A  1 1018 ? -10.205 80.587  101.738 1.00 26.56 ? 1016 SER A CA    1 
ATOM   7426  C C     . SER A  1 1018 ? -10.236 80.010  103.140 1.00 28.91 ? 1016 SER A C     1 
ATOM   7427  O O     . SER A  1 1018 ? -11.331 79.759  103.653 1.00 28.84 ? 1016 SER A O     1 
ATOM   7428  C CB    . SER A  1 1018 ? -10.618 79.492  100.745 1.00 25.95 ? 1016 SER A CB    1 
ATOM   7429  O OG    . SER A  1 1018 ? -10.913 80.067  99.482  1.00 30.20 ? 1016 SER A OG    1 
ATOM   7430  N N     . GLY A  1 1019 ? -9.086  79.776  103.765 1.00 29.83 ? 1017 GLY A N     1 
ATOM   7431  C CA    . GLY A  1 1019 ? -9.131  79.227  105.107 1.00 31.67 ? 1017 GLY A CA    1 
ATOM   7432  C C     . GLY A  1 1019 ? -7.797  78.698  105.582 1.00 29.68 ? 1017 GLY A C     1 
ATOM   7433  O O     . GLY A  1 1019 ? -6.847  78.506  104.819 1.00 28.70 ? 1017 GLY A O     1 
ATOM   7434  N N     . THR A  1 1020 ? -7.755  78.464  106.884 1.00 26.86 ? 1018 THR A N     1 
ATOM   7435  C CA    . THR A  1 1020 ? -6.624  77.849  107.558 1.00 28.79 ? 1018 THR A CA    1 
ATOM   7436  C C     . THR A  1 1020 ? -6.735  76.343  107.605 1.00 28.64 ? 1018 THR A C     1 
ATOM   7437  O O     . THR A  1 1020 ? -5.718  75.659  107.749 1.00 30.33 ? 1018 THR A O     1 
ATOM   7438  C CB    . THR A  1 1020 ? -6.552  78.355  108.996 1.00 29.14 ? 1018 THR A CB    1 
ATOM   7439  O OG1   . THR A  1 1020 ? -7.788  78.016  109.655 1.00 25.36 ? 1018 THR A OG1   1 
ATOM   7440  C CG2   . THR A  1 1020 ? -6.370  79.867  109.014 1.00 30.82 ? 1018 THR A CG2   1 
ATOM   7441  N N     . GLY A  1 1021 ? -7.951  75.816  107.512 1.00 26.53 ? 1019 GLY A N     1 
ATOM   7442  C CA    . GLY A  1 1021 ? -8.202  74.462  107.920 1.00 23.47 ? 1019 GLY A CA    1 
ATOM   7443  C C     . GLY A  1 1021 ? -8.035  74.353  109.424 1.00 28.61 ? 1019 GLY A C     1 
ATOM   7444  O O     . GLY A  1 1021 ? -7.726  75.334  110.112 1.00 26.62 ? 1019 GLY A O     1 
ATOM   7445  N N     . PRO A  1 1022 ? -8.249  73.156  109.965 1.00 25.53 ? 1020 PRO A N     1 
ATOM   7446  C CA    . PRO A  1 1022 ? -8.663  71.938  109.259 1.00 24.59 ? 1020 PRO A CA    1 
ATOM   7447  C C     . PRO A  1 1022 ? -10.137 72.000  108.830 1.00 26.60 ? 1020 PRO A C     1 
ATOM   7448  O O     . PRO A  1 1022 ? -10.898 72.871  109.250 1.00 26.16 ? 1020 PRO A O     1 
ATOM   7449  C CB    . PRO A  1 1022 ? -8.389  70.838  110.295 1.00 24.79 ? 1020 PRO A CB    1 
ATOM   7450  C CG    . PRO A  1 1022 ? -8.598  71.541  111.630 1.00 27.52 ? 1020 PRO A CG    1 
ATOM   7451  C CD    . PRO A  1 1022 ? -8.028  72.914  111.405 1.00 27.11 ? 1020 PRO A CD    1 
ATOM   7452  N N     . LYS A  1 1023 ? -10.529 71.063  107.972 1.00 23.96 ? 1021 LYS A N     1 
ATOM   7453  C CA    . LYS A  1 1023 ? -11.870 71.045  107.399 1.00 25.08 ? 1021 LYS A CA    1 
ATOM   7454  C C     . LYS A  1 1023 ? -12.937 70.803  108.450 1.00 24.98 ? 1021 LYS A C     1 
ATOM   7455  O O     . LYS A  1 1023 ? -12.829 69.878  109.259 1.00 23.27 ? 1021 LYS A O     1 
ATOM   7456  C CB    . LYS A  1 1023 ? -11.969 69.951  106.345 1.00 25.76 ? 1021 LYS A CB    1 
ATOM   7457  C CG    . LYS A  1 1023 ? -11.317 70.274  105.024 1.00 23.38 ? 1021 LYS A CG    1 
ATOM   7458  C CD    . LYS A  1 1023 ? -11.491 69.050  104.131 1.00 23.97 ? 1021 LYS A CD    1 
ATOM   7459  C CE    . LYS A  1 1023 ? -11.057 69.312  102.683 1.00 23.99 ? 1021 LYS A CE    1 
ATOM   7460  N NZ    . LYS A  1 1023 ? -12.064 70.186  101.992 1.00 24.53 ? 1021 LYS A NZ    1 
ATOM   7461  N N     . ALA A  1 1024 ? -13.995 71.608  108.398 1.00 22.27 ? 1022 ALA A N     1 
ATOM   7462  C CA    . ALA A  1 1024 ? -15.171 71.347  109.212 1.00 21.28 ? 1022 ALA A CA    1 
ATOM   7463  C C     . ALA A  1 1024 ? -15.854 70.067  108.752 1.00 22.06 ? 1022 ALA A C     1 
ATOM   7464  O O     . ALA A  1 1024 ? -15.869 69.738  107.561 1.00 27.43 ? 1022 ALA A O     1 
ATOM   7465  C CB    . ALA A  1 1024 ? -16.133 72.535  109.145 1.00 24.26 ? 1022 ALA A CB    1 
ATOM   7466  N N     . GLY A  1 1025 ? -16.385 69.314  109.708 1.00 22.64 ? 1023 GLY A N     1 
ATOM   7467  C CA    . GLY A  1 1025 ? -17.037 68.078  109.344 1.00 21.02 ? 1023 GLY A CA    1 
ATOM   7468  C C     . GLY A  1 1025 ? -16.082 67.051  108.795 1.00 23.52 ? 1023 GLY A C     1 
ATOM   7469  O O     . GLY A  1 1025 ? -16.492 66.186  108.009 1.00 24.15 ? 1023 GLY A O     1 
ATOM   7470  N N     . GLY A  1 1026 ? -14.816 67.118  109.210 1.00 21.96 ? 1024 GLY A N     1 
ATOM   7471  C CA    . GLY A  1 1026 ? -13.799 66.172  108.827 1.00 23.08 ? 1024 GLY A CA    1 
ATOM   7472  C C     . GLY A  1 1026 ? -13.024 65.705  110.036 1.00 22.43 ? 1024 GLY A C     1 
ATOM   7473  O O     . GLY A  1 1026 ? -13.210 66.211  111.146 1.00 22.60 ? 1024 GLY A O     1 
ATOM   7474  N N     . PRO A  1 1027 ? -12.136 64.720  109.849 1.00 22.09 ? 1025 PRO A N     1 
ATOM   7475  C CA    . PRO A  1 1027 ? -11.578 63.995  110.994 1.00 23.63 ? 1025 PRO A CA    1 
ATOM   7476  C C     . PRO A  1 1027 ? -10.410 64.684  111.682 1.00 23.00 ? 1025 PRO A C     1 
ATOM   7477  O O     . PRO A  1 1027 ? -9.955  64.176  112.705 1.00 23.88 ? 1025 PRO A O     1 
ATOM   7478  C CB    . PRO A  1 1027 ? -11.117 62.665  110.368 1.00 24.30 ? 1025 PRO A CB    1 
ATOM   7479  C CG    . PRO A  1 1027 ? -10.723 63.048  108.964 1.00 24.98 ? 1025 PRO A CG    1 
ATOM   7480  C CD    . PRO A  1 1027 ? -11.718 64.136  108.558 1.00 22.91 ? 1025 PRO A CD    1 
ATOM   7481  N N     . LEU A  1 1028 ? -9.870  65.763  111.124 1.00 22.56 ? 1026 LEU A N     1 
ATOM   7482  C CA    . LEU A  1 1028 ? -8.799  66.512  111.759 1.00 24.22 ? 1026 LEU A CA    1 
ATOM   7483  C C     . LEU A  1 1028 ? -9.313  67.657  112.620 1.00 23.88 ? 1026 LEU A C     1 
ATOM   7484  O O     . LEU A  1 1028 ? -8.522  68.281  113.336 1.00 24.77 ? 1026 LEU A O     1 
ATOM   7485  C CB    . LEU A  1 1028 ? -7.856  67.069  110.691 1.00 25.13 ? 1026 LEU A CB    1 
ATOM   7486  C CG    . LEU A  1 1028 ? -6.960  66.029  110.028 1.00 25.72 ? 1026 LEU A CG    1 
ATOM   7487  C CD1   . LEU A  1 1028 ? -6.215  66.684  108.878 1.00 30.76 ? 1026 LEU A CD1   1 
ATOM   7488  C CD2   . LEU A  1 1028 ? -5.986  65.456  111.051 1.00 30.70 ? 1026 LEU A CD2   1 
ATOM   7489  N N     . TYR A  1 1029 ? -10.621 67.922  112.585 1.00 25.16 ? 1027 TYR A N     1 
ATOM   7490  C CA    . TYR A  1 1029 ? -11.178 69.133  113.185 1.00 23.48 ? 1027 TYR A CA    1 
ATOM   7491  C C     . TYR A  1 1029 ? -11.020 69.156  114.705 1.00 23.86 ? 1027 TYR A C     1 
ATOM   7492  O O     . TYR A  1 1029 ? -10.552 70.154  115.275 1.00 22.22 ? 1027 TYR A O     1 
ATOM   7493  C CB    . TYR A  1 1029 ? -12.646 69.239  112.792 1.00 22.52 ? 1027 TYR A CB    1 
ATOM   7494  C CG    . TYR A  1 1029 ? -13.295 70.610  112.871 1.00 26.06 ? 1027 TYR A CG    1 
ATOM   7495  C CD1   . TYR A  1 1029 ? -12.955 71.613  111.971 1.00 25.24 ? 1027 TYR A CD1   1 
ATOM   7496  C CD2   . TYR A  1 1029 ? -14.307 70.872  113.790 1.00 23.63 ? 1027 TYR A CD2   1 
ATOM   7497  C CE1   . TYR A  1 1029 ? -13.577 72.853  112.003 1.00 24.84 ? 1027 TYR A CE1   1 
ATOM   7498  C CE2   . TYR A  1 1029 ? -14.930 72.116  113.831 1.00 24.86 ? 1027 TYR A CE2   1 
ATOM   7499  C CZ    . TYR A  1 1029 ? -14.565 73.096  112.924 1.00 27.37 ? 1027 TYR A CZ    1 
ATOM   7500  O OH    . TYR A  1 1029 ? -15.188 74.333  112.927 1.00 28.42 ? 1027 TYR A OH    1 
ATOM   7501  N N     . LEU A  1 1030 ? -11.422 68.085  115.390 1.00 24.56 ? 1028 LEU A N     1 
ATOM   7502  C CA    . LEU A  1 1030 ? -11.341 68.114  116.850 1.00 23.59 ? 1028 LEU A CA    1 
ATOM   7503  C C     . LEU A  1 1030 ? -9.904  68.248  117.342 1.00 25.10 ? 1028 LEU A C     1 
ATOM   7504  O O     . LEU A  1 1030 ? -9.658  68.881  118.380 1.00 28.69 ? 1028 LEU A O     1 
ATOM   7505  C CB    . LEU A  1 1030 ? -11.969 66.865  117.455 1.00 21.91 ? 1028 LEU A CB    1 
ATOM   7506  C CG    . LEU A  1 1030 ? -13.448 66.683  117.138 1.00 24.20 ? 1028 LEU A CG    1 
ATOM   7507  C CD1   . LEU A  1 1030 ? -13.964 65.484  117.919 1.00 24.50 ? 1028 LEU A CD1   1 
ATOM   7508  C CD2   . LEU A  1 1030 ? -14.234 67.946  117.481 1.00 26.85 ? 1028 LEU A CD2   1 
ATOM   7509  N N     . GLY A  1 1031 ? -8.946  67.668  116.620 1.00 26.20 ? 1029 GLY A N     1 
ATOM   7510  C CA    . GLY A  1 1031 ? -7.566  67.690  117.070 1.00 27.06 ? 1029 GLY A CA    1 
ATOM   7511  C C     . GLY A  1 1031 ? -6.965  69.075  117.180 1.00 27.91 ? 1029 GLY A C     1 
ATOM   7512  O O     . GLY A  1 1031 ? -5.952  69.249  117.874 1.00 30.00 ? 1029 GLY A O     1 
ATOM   7513  N N     . ARG A  1 1032 ? -7.543  70.058  116.492 1.00 24.25 ? 1030 ARG A N     1 
ATOM   7514  C CA    . ARG A  1 1032 ? -7.111  71.444  116.598 1.00 23.01 ? 1030 ARG A CA    1 
ATOM   7515  C C     . ARG A  1 1032 ? -7.600  72.104  117.877 1.00 28.45 ? 1030 ARG A C     1 
ATOM   7516  O O     . ARG A  1 1032 ? -7.103  73.179  118.239 1.00 26.41 ? 1030 ARG A O     1 
ATOM   7517  C CB    . ARG A  1 1032 ? -7.611  72.237  115.384 1.00 24.49 ? 1030 ARG A CB    1 
ATOM   7518  C CG    . ARG A  1 1032 ? -6.983  73.629  115.241 1.00 26.16 ? 1030 ARG A CG    1 
ATOM   7519  C CD    . ARG A  1 1032 ? -5.515  73.549  114.806 1.00 28.24 ? 1030 ARG A CD    1 
ATOM   7520  N NE    . ARG A  1 1032 ? -5.012  74.848  114.363 1.00 26.06 ? 1030 ARG A NE    1 
ATOM   7521  C CZ    . ARG A  1 1032 ? -3.971  75.483  114.886 1.00 29.01 ? 1030 ARG A CZ    1 
ATOM   7522  N NH1   . ARG A  1 1032 ? -3.218  74.930  115.826 1.00 27.35 ? 1030 ARG A NH1   1 
ATOM   7523  N NH2   . ARG A  1 1032 ? -3.675  76.704  114.450 1.00 31.10 ? 1030 ARG A NH2   1 
ATOM   7524  N N     . LEU A  1 1033 ? -8.557  71.478  118.563 1.00 26.26 ? 1031 LEU A N     1 
ATOM   7525  C CA    . LEU A  1 1033 ? -9.225  72.064  119.714 1.00 27.57 ? 1031 LEU A CA    1 
ATOM   7526  C C     . LEU A  1 1033 ? -8.765  71.428  121.022 1.00 30.28 ? 1031 LEU A C     1 
ATOM   7527  O O     . LEU A  1 1033 ? -9.420  71.597  122.055 1.00 26.89 ? 1031 LEU A O     1 
ATOM   7528  C CB    . LEU A  1 1033 ? -10.743 71.947  119.540 1.00 24.54 ? 1031 LEU A CB    1 
ATOM   7529  C CG    . LEU A  1 1033 ? -11.271 72.522  118.228 1.00 26.67 ? 1031 LEU A CG    1 
ATOM   7530  C CD1   . LEU A  1 1033 ? -12.773 72.234  118.083 1.00 23.64 ? 1031 LEU A CD1   1 
ATOM   7531  C CD2   . LEU A  1 1033 ? -10.997 74.024  118.167 1.00 30.65 ? 1031 LEU A CD2   1 
ATOM   7532  N N     . VAL A  1 1034 ? -7.636  70.708  121.000 1.00 27.28 ? 1032 VAL A N     1 
ATOM   7533  C CA    . VAL A  1 1034 ? -7.019  70.158  122.205 1.00 28.68 ? 1032 VAL A CA    1 
ATOM   7534  C C     . VAL A  1 1034 ? -5.529  70.457  122.143 1.00 32.52 ? 1032 VAL A C     1 
ATOM   7535  O O     . VAL A  1 1034 ? -4.956  70.673  121.071 1.00 31.07 ? 1032 VAL A O     1 
ATOM   7536  C CB    . VAL A  1 1034 ? -7.263  68.639  122.373 1.00 30.85 ? 1032 VAL A CB    1 
ATOM   7537  C CG1   . VAL A  1 1034 ? -8.743  68.364  122.654 1.00 29.07 ? 1032 VAL A CG1   1 
ATOM   7538  C CG2   . VAL A  1 1034 ? -6.810  67.869  121.124 1.00 29.71 ? 1032 VAL A CG2   1 
ATOM   7539  N N     . THR A  1 1035 ? -4.896  70.460  123.316 1.00 31.27 ? 1033 THR A N     1 
ATOM   7540  C CA    . THR A  1 1035 ? -3.484  70.825  123.371 1.00 33.61 ? 1033 THR A CA    1 
ATOM   7541  C C     . THR A  1 1035 ? -2.605  69.781  122.688 1.00 33.78 ? 1033 THR A C     1 
ATOM   7542  O O     . THR A  1 1035 ? -1.591  70.135  122.075 1.00 34.76 ? 1033 THR A O     1 
ATOM   7543  C CB    . THR A  1 1035 ? -3.051  71.036  124.824 1.00 32.12 ? 1033 THR A CB    1 
ATOM   7544  O OG1   . THR A  1 1035 ? -3.075  69.783  125.515 1.00 41.50 ? 1033 THR A OG1   1 
ATOM   7545  C CG2   . THR A  1 1035 ? -4.006  71.992  125.520 1.00 31.84 ? 1033 THR A CG2   1 
ATOM   7546  N N     . THR A  1 1036 ? -2.983  68.506  122.763 1.00 33.57 ? 1034 THR A N     1 
ATOM   7547  C CA    . THR A  1 1036 ? -2.261  67.412  122.121 1.00 35.44 ? 1034 THR A CA    1 
ATOM   7548  C C     . THR A  1 1036 ? -3.222  66.679  121.195 1.00 34.02 ? 1034 THR A C     1 
ATOM   7549  O O     . THR A  1 1036 ? -4.223  66.121  121.654 1.00 34.62 ? 1034 THR A O     1 
ATOM   7550  C CB    . THR A  1 1036 ? -1.678  66.455  123.161 1.00 40.38 ? 1034 THR A CB    1 
ATOM   7551  O OG1   . THR A  1 1036 ? -0.758  67.168  123.995 1.00 37.33 ? 1034 THR A OG1   1 
ATOM   7552  C CG2   . THR A  1 1036 ? -0.940  65.307  122.479 1.00 41.49 ? 1034 THR A CG2   1 
ATOM   7553  N N     . ALA A  1 1037 ? -2.923  66.681  119.900 1.00 33.65 ? 1035 ALA A N     1 
ATOM   7554  C CA    . ALA A  1 1037 ? -3.875  66.158  118.930 1.00 29.84 ? 1035 ALA A CA    1 
ATOM   7555  C C     . ALA A  1 1037 ? -3.934  64.634  119.013 1.00 31.22 ? 1035 ALA A C     1 
ATOM   7556  O O     . ALA A  1 1037 ? -2.892  63.979  119.115 1.00 31.41 ? 1035 ALA A O     1 
ATOM   7557  C CB    . ALA A  1 1037 ? -3.486  66.592  117.509 1.00 30.11 ? 1035 ALA A CB    1 
ATOM   7558  N N     . PRO A  1 1038 ? -5.126  64.043  118.952 1.00 31.08 ? 1036 PRO A N     1 
ATOM   7559  C CA    . PRO A  1 1038 ? -5.231  62.586  118.853 1.00 30.44 ? 1036 PRO A CA    1 
ATOM   7560  C C     . PRO A  1 1038 ? -4.957  62.105  117.431 1.00 29.00 ? 1036 PRO A C     1 
ATOM   7561  O O     . PRO A  1 1038 ? -4.837  62.885  116.481 1.00 25.49 ? 1036 PRO A O     1 
ATOM   7562  C CB    . PRO A  1 1038 ? -6.683  62.315  119.241 1.00 31.52 ? 1036 PRO A CB    1 
ATOM   7563  C CG    . PRO A  1 1038 ? -7.406  63.503  118.703 1.00 31.36 ? 1036 PRO A CG    1 
ATOM   7564  C CD    . PRO A  1 1038 ? -6.454  64.688  118.897 1.00 26.44 ? 1036 PRO A CD    1 
ATOM   7565  N N     . VAL A  1 1039 ? -4.903  60.782  117.297 1.00 28.74 ? 1037 VAL A N     1 
ATOM   7566  C CA    . VAL A  1 1039 ? -4.772  60.127  115.997 1.00 30.01 ? 1037 VAL A CA    1 
ATOM   7567  C C     . VAL A  1 1039 ? -6.180  59.920  115.438 1.00 25.59 ? 1037 VAL A C     1 
ATOM   7568  O O     . VAL A  1 1039 ? -6.927  59.094  115.980 1.00 26.53 ? 1037 VAL A O     1 
ATOM   7569  C CB    . VAL A  1 1039 ? -4.027  58.792  116.120 1.00 30.34 ? 1037 VAL A CB    1 
ATOM   7570  C CG1   . VAL A  1 1039 ? -3.944  58.102  114.766 1.00 28.00 ? 1037 VAL A CG1   1 
ATOM   7571  C CG2   . VAL A  1 1039 ? -2.642  59.021  116.711 1.00 29.99 ? 1037 VAL A CG2   1 
ATOM   7572  N N     . PRO A  1 1040 ? -6.574  60.632  114.384 1.00 25.08 ? 1038 PRO A N     1 
ATOM   7573  C CA    . PRO A  1 1040 ? -7.927  60.491  113.850 1.00 27.75 ? 1038 PRO A CA    1 
ATOM   7574  C C     . PRO A  1 1040 ? -8.179  59.083  113.340 1.00 26.89 ? 1038 PRO A C     1 
ATOM   7575  O O     . PRO A  1 1040 ? -7.235  58.366  112.977 1.00 25.59 ? 1038 PRO A O     1 
ATOM   7576  C CB    . PRO A  1 1040 ? -7.967  61.509  112.695 1.00 26.81 ? 1038 PRO A CB    1 
ATOM   7577  C CG    . PRO A  1 1040 ? -6.822  62.431  112.921 1.00 26.06 ? 1038 PRO A CG    1 
ATOM   7578  C CD    . PRO A  1 1040 ? -5.771  61.625  113.644 1.00 28.92 ? 1038 PRO A CD    1 
ATOM   7579  N N     . PRO A  1 1041 ? -9.443  58.671  113.252 1.00 25.68 ? 1039 PRO A N     1 
ATOM   7580  C CA    . PRO A  1 1041 ? -9.763  57.399  112.595 1.00 26.68 ? 1039 PRO A CA    1 
ATOM   7581  C C     . PRO A  1 1041 ? -9.252  57.373  111.163 1.00 25.48 ? 1039 PRO A C     1 
ATOM   7582  O O     . PRO A  1 1041 ? -9.315  58.371  110.447 1.00 26.92 ? 1039 PRO A O     1 
ATOM   7583  C CB    . PRO A  1 1041 ? -11.300 57.349  112.637 1.00 25.20 ? 1039 PRO A CB    1 
ATOM   7584  C CG    . PRO A  1 1041 ? -11.685 58.310  113.704 1.00 28.33 ? 1039 PRO A CG    1 
ATOM   7585  C CD    . PRO A  1 1041 ? -10.661 59.398  113.650 1.00 26.35 ? 1039 PRO A CD    1 
ATOM   7586  N N     . GLN A  1 1042 ? -8.725  56.215  110.766 1.00 26.97 ? 1040 GLN A N     1 
ATOM   7587  C CA    . GLN A  1 1042 ? -8.227  55.928  109.425 1.00 24.59 ? 1040 GLN A CA    1 
ATOM   7588  C C     . GLN A  1 1042 ? -7.083  56.837  108.989 1.00 26.84 ? 1040 GLN A C     1 
ATOM   7589  O O     . GLN A  1 1042 ? -6.747  56.853  107.810 1.00 26.74 ? 1040 GLN A O     1 
ATOM   7590  C CB    . GLN A  1 1042 ? -9.356  56.000  108.389 1.00 30.60 ? 1040 GLN A CB    1 
ATOM   7591  C CG    . GLN A  1 1042 ? -10.491 55.034  108.666 1.00 30.97 ? 1040 GLN A CG    1 
ATOM   7592  C CD    . GLN A  1 1042 ? -11.451 54.968  107.501 1.00 33.97 ? 1040 GLN A CD    1 
ATOM   7593  O OE1   . GLN A  1 1042 ? -12.439 55.679  107.471 1.00 31.12 ? 1040 GLN A OE1   1 
ATOM   7594  N NE2   . GLN A  1 1042 ? -11.154 54.116  106.536 1.00 38.15 ? 1040 GLN A NE2   1 
ATOM   7595  N N     . HIS A  1 1043 ? -6.454  57.567  109.912 1.00 22.35 ? 1041 HIS A N     1 
ATOM   7596  C CA    . HIS A  1 1043 ? -5.451  58.580  109.579 1.00 25.38 ? 1041 HIS A CA    1 
ATOM   7597  C C     . HIS A  1 1043 ? -4.068  57.934  109.595 1.00 24.32 ? 1041 HIS A C     1 
ATOM   7598  O O     . HIS A  1 1043 ? -3.391  57.886  110.623 1.00 24.69 ? 1041 HIS A O     1 
ATOM   7599  C CB    . HIS A  1 1043 ? -5.548  59.743  110.558 1.00 24.36 ? 1041 HIS A CB    1 
ATOM   7600  C CG    . HIS A  1 1043 ? -4.622  60.878  110.260 1.00 23.81 ? 1041 HIS A CG    1 
ATOM   7601  N ND1   . HIS A  1 1043 ? -4.945  61.891  109.385 1.00 24.05 ? 1041 HIS A ND1   1 
ATOM   7602  C CD2   . HIS A  1 1043 ? -3.385  61.168  110.735 1.00 24.12 ? 1041 HIS A CD2   1 
ATOM   7603  C CE1   . HIS A  1 1043 ? -3.949  62.760  109.332 1.00 24.97 ? 1041 HIS A CE1   1 
ATOM   7604  N NE2   . HIS A  1 1043 ? -2.987  62.342  110.142 1.00 26.24 ? 1041 HIS A NE2   1 
ATOM   7605  N N     . SER A  1 1044 ? -3.644  57.428  108.439 1.00 23.91 ? 1042 SER A N     1 
ATOM   7606  C CA    . SER A  1 1044 ? -2.308  56.863  108.285 1.00 23.44 ? 1042 SER A CA    1 
ATOM   7607  C C     . SER A  1 1044 ? -2.003  56.782  106.797 1.00 26.27 ? 1042 SER A C     1 
ATOM   7608  O O     . SER A  1 1044 ? -2.892  56.941  105.959 1.00 23.06 ? 1042 SER A O     1 
ATOM   7609  C CB    . SER A  1 1044 ? -2.198  55.483  108.917 1.00 26.80 ? 1042 SER A CB    1 
ATOM   7610  O OG    . SER A  1 1044 ? -2.985  54.571  108.181 1.00 25.96 ? 1042 SER A OG    1 
ATOM   7611  N N     . SER A  1 1045 ? -0.731  56.510  106.487 1.00 23.78 ? 1043 SER A N     1 
ATOM   7612  C CA    . SER A  1 1045 ? -0.270  56.403  105.108 1.00 22.78 ? 1043 SER A CA    1 
ATOM   7613  C C     . SER A  1 1045 ? 0.954   55.503  105.059 1.00 20.89 ? 1043 SER A C     1 
ATOM   7614  O O     . SER A  1 1045 ? 1.870   55.655  105.868 1.00 24.48 ? 1043 SER A O     1 
ATOM   7615  C CB    . SER A  1 1045 ? 0.079   57.775  104.534 1.00 21.17 ? 1043 SER A CB    1 
ATOM   7616  O OG    . SER A  1 1045 ? 0.448   57.668  103.169 1.00 25.30 ? 1043 SER A OG    1 
ATOM   7617  N N     . VAL A  1 1046 ? 0.968   54.555  104.118 1.00 24.47 ? 1044 VAL A N     1 
ATOM   7618  C CA    . VAL A  1 1046 ? 2.159   53.723  103.957 1.00 24.49 ? 1044 VAL A CA    1 
ATOM   7619  C C     . VAL A  1 1046 ? 3.195   54.366  103.057 1.00 23.09 ? 1044 VAL A C     1 
ATOM   7620  O O     . VAL A  1 1046 ? 4.244   53.760  102.821 1.00 24.46 ? 1044 VAL A O     1 
ATOM   7621  C CB    . VAL A  1 1046 ? 1.824   52.330  103.385 1.00 25.02 ? 1044 VAL A CB    1 
ATOM   7622  C CG1   . VAL A  1 1046 ? 0.920   51.586  104.331 1.00 31.05 ? 1044 VAL A CG1   1 
ATOM   7623  C CG2   . VAL A  1 1046 ? 1.182   52.463  102.031 1.00 24.20 ? 1044 VAL A CG2   1 
ATOM   7624  N N     . HIS A  1 1047 ? 2.929   55.567  102.550 1.00 23.83 ? 1045 HIS A N     1 
ATOM   7625  C CA    A HIS A  1 1047 ? 3.877   56.222  101.675 0.51 25.09 ? 1045 HIS A CA    1 
ATOM   7626  C CA    B HIS A  1 1047 ? 3.831   56.303  101.660 0.49 25.08 ? 1045 HIS A CA    1 
ATOM   7627  C C     . HIS A  1 1047 ? 4.835   57.106  102.467 1.00 25.56 ? 1045 HIS A C     1 
ATOM   7628  O O     . HIS A  1 1047 ? 4.486   57.691  103.498 1.00 25.77 ? 1045 HIS A O     1 
ATOM   7629  C CB    A HIS A  1 1047 ? 3.113   57.002  100.613 0.51 24.25 ? 1045 HIS A CB    1 
ATOM   7630  C CB    B HIS A  1 1047 ? 3.051   57.265  100.752 0.49 24.03 ? 1045 HIS A CB    1 
ATOM   7631  C CG    A HIS A  1 1047 ? 2.100   56.159  99.898  0.51 23.42 ? 1045 HIS A CG    1 
ATOM   7632  C CG    B HIS A  1 1047 ? 3.890   58.344  100.120 0.49 25.98 ? 1045 HIS A CG    1 
ATOM   7633  N ND1   A HIS A  1 1047 ? 2.454   55.184  98.990  0.51 24.34 ? 1045 HIS A ND1   1 
ATOM   7634  N ND1   B HIS A  1 1047 ? 4.778   58.099  99.091  0.49 23.75 ? 1045 HIS A ND1   1 
ATOM   7635  C CD2   A HIS A  1 1047 ? 0.750   56.112  99.991  0.51 25.63 ? 1045 HIS A CD2   1 
ATOM   7636  C CD2   B HIS A  1 1047 ? 3.952   59.681  100.354 0.49 25.49 ? 1045 HIS A CD2   1 
ATOM   7637  C CE1   A HIS A  1 1047 ? 1.362   54.589  98.537  0.51 24.02 ? 1045 HIS A CE1   1 
ATOM   7638  C CE1   B HIS A  1 1047 ? 5.361   59.231  98.733  0.49 24.86 ? 1045 HIS A CE1   1 
ATOM   7639  N NE2   A HIS A  1 1047 ? 0.316   55.137  99.125  0.51 22.30 ? 1045 HIS A NE2   1 
ATOM   7640  N NE2   B HIS A  1 1047 ? 4.873   60.209  99.479  0.49 18.88 ? 1045 HIS A NE2   1 
ATOM   7641  N N     . THR A  1 1048 ? 6.071   57.160  101.985 1.00 24.82 ? 1046 THR A N     1 
ATOM   7642  C CA    . THR A  1 1048 ? 7.102   57.972  102.605 1.00 22.96 ? 1046 THR A CA    1 
ATOM   7643  C C     . THR A  1 1048 ? 7.606   58.963  101.575 1.00 27.01 ? 1046 THR A C     1 
ATOM   7644  O O     . THR A  1 1048 ? 7.945   58.579  100.453 1.00 26.90 ? 1046 THR A O     1 
ATOM   7645  C CB    . THR A  1 1048 ? 8.254   57.115  103.124 1.00 25.77 ? 1046 THR A CB    1 
ATOM   7646  O OG1   . THR A  1 1048 ? 7.717   56.037  103.895 1.00 25.07 ? 1046 THR A OG1   1 
ATOM   7647  C CG2   . THR A  1 1048 ? 9.168   57.955  104.003 1.00 24.66 ? 1046 THR A CG2   1 
ATOM   7648  N N     . ASP A  1 1049 ? 7.657   60.224  101.954 1.00 27.10 ? 1047 ASP A N     1 
ATOM   7649  C CA    . ASP A  1 1049 ? 8.145   61.227  101.029 1.00 25.19 ? 1047 ASP A CA    1 
ATOM   7650  C C     . ASP A  1 1049 ? 9.609   60.930  100.693 1.00 21.89 ? 1047 ASP A C     1 
ATOM   7651  O O     . ASP A  1 1049 ? 10.413  60.699  101.599 1.00 22.62 ? 1047 ASP A O     1 
ATOM   7652  C CB    . ASP A  1 1049 ? 7.965   62.616  101.640 1.00 21.64 ? 1047 ASP A CB    1 
ATOM   7653  C CG    . ASP A  1 1049 ? 8.393   63.710  100.702 1.00 22.85 ? 1047 ASP A CG    1 
ATOM   7654  O OD1   . ASP A  1 1049 ? 9.616   63.960  100.604 1.00 26.52 ? 1047 ASP A OD1   1 
ATOM   7655  O OD2   . ASP A  1 1049 ? 7.508   64.281  100.016 1.00 26.77 ? 1047 ASP A OD2   1 
ATOM   7656  N N     . PRO A  1 1050 ? 9.980   60.854  99.407  1.00 23.90 ? 1048 PRO A N     1 
ATOM   7657  C CA    . PRO A  1 1050 ? 11.358  60.460  99.074  1.00 23.75 ? 1048 PRO A CA    1 
ATOM   7658  C C     . PRO A  1 1050 ? 12.369  61.562  99.315  1.00 23.88 ? 1048 PRO A C     1 
ATOM   7659  O O     . PRO A  1 1050 ? 13.565  61.268  99.495  1.00 25.60 ? 1048 PRO A O     1 
ATOM   7660  C CB    . PRO A  1 1050 ? 11.269  60.101  97.580  1.00 26.50 ? 1048 PRO A CB    1 
ATOM   7661  C CG    . PRO A  1 1050 ? 10.149  60.936  97.066  1.00 27.77 ? 1048 PRO A CG    1 
ATOM   7662  C CD    . PRO A  1 1050 ? 9.174   61.137  98.208  1.00 25.93 ? 1048 PRO A CD    1 
ATOM   7663  N N     . VAL A  1 1051 ? 11.935  62.818  99.308  1.00 23.81 ? 1049 VAL A N     1 
ATOM   7664  C CA    . VAL A  1 1051 ? 12.841  63.904  99.658  1.00 24.23 ? 1049 VAL A CA    1 
ATOM   7665  C C     . VAL A  1 1051 ? 13.125  63.888  101.150 1.00 22.42 ? 1049 VAL A C     1 
ATOM   7666  O O     . VAL A  1 1051 ? 14.249  64.172  101.587 1.00 24.11 ? 1049 VAL A O     1 
ATOM   7667  C CB    . VAL A  1 1051 ? 12.251  65.242  99.202  1.00 24.38 ? 1049 VAL A CB    1 
ATOM   7668  C CG1   . VAL A  1 1051 ? 13.155  66.395  99.602  1.00 27.48 ? 1049 VAL A CG1   1 
ATOM   7669  C CG2   . VAL A  1 1051 ? 12.019  65.206  97.680  1.00 27.63 ? 1049 VAL A CG2   1 
ATOM   7670  N N     . LEU A  1 1052 ? 12.118  63.566  101.959 1.00 21.19 ? 1050 LEU A N     1 
ATOM   7671  C CA    . LEU A  1 1052 ? 12.379  63.311  103.371 1.00 20.95 ? 1050 LEU A CA    1 
ATOM   7672  C C     . LEU A  1 1052 ? 13.436  62.222  103.529 1.00 23.03 ? 1050 LEU A C     1 
ATOM   7673  O O     . LEU A  1 1052 ? 14.371  62.361  104.326 1.00 24.16 ? 1050 LEU A O     1 
ATOM   7674  C CB    . LEU A  1 1052 ? 11.066  62.935  104.076 1.00 20.56 ? 1050 LEU A CB    1 
ATOM   7675  C CG    . LEU A  1 1052 ? 11.092  62.496  105.547 1.00 21.72 ? 1050 LEU A CG    1 
ATOM   7676  C CD1   . LEU A  1 1052 ? 11.619  61.050  105.748 1.00 21.65 ? 1050 LEU A CD1   1 
ATOM   7677  C CD2   . LEU A  1 1052 ? 11.893  63.494  106.356 1.00 20.55 ? 1050 LEU A CD2   1 
ATOM   7678  N N     . LEU A  1 1053 ? 13.294  61.110  102.787 1.00 23.95 ? 1051 LEU A N     1 
ATOM   7679  C CA    . LEU A  1 1053 ? 14.269  60.027  102.891 1.00 26.19 ? 1051 LEU A CA    1 
ATOM   7680  C C     . LEU A  1 1053 ? 15.659  60.494  102.483 1.00 25.11 ? 1051 LEU A C     1 
ATOM   7681  O O     . LEU A  1 1053 ? 16.648  60.111  103.113 1.00 23.89 ? 1051 LEU A O     1 
ATOM   7682  C CB    . LEU A  1 1053 ? 13.847  58.828  102.035 1.00 24.33 ? 1051 LEU A CB    1 
ATOM   7683  C CG    . LEU A  1 1053 ? 12.609  58.050  102.494 1.00 23.64 ? 1051 LEU A CG    1 
ATOM   7684  C CD1   . LEU A  1 1053 ? 12.223  56.956  101.480 1.00 24.47 ? 1051 LEU A CD1   1 
ATOM   7685  C CD2   . LEU A  1 1053 ? 12.820  57.471  103.874 1.00 21.11 ? 1051 LEU A CD2   1 
ATOM   7686  N N     . ASP A  1 1054 ? 15.756  61.324  101.436 1.00 24.77 ? 1052 ASP A N     1 
ATOM   7687  C CA    . ASP A  1 1054 ? 17.061  61.852  101.038 1.00 27.66 ? 1052 ASP A CA    1 
ATOM   7688  C C     . ASP A  1 1054 ? 17.640  62.768  102.107 1.00 25.06 ? 1052 ASP A C     1 
ATOM   7689  O O     . ASP A  1 1054 ? 18.855  62.762  102.349 1.00 24.20 ? 1052 ASP A O     1 
ATOM   7690  C CB    . ASP A  1 1054 ? 16.956  62.616  99.720  1.00 24.72 ? 1052 ASP A CB    1 
ATOM   7691  C CG    . ASP A  1 1054 ? 16.643  61.713  98.542  1.00 30.04 ? 1052 ASP A CG    1 
ATOM   7692  O OD1   . ASP A  1 1054 ? 16.863  60.480  98.646  1.00 27.98 ? 1052 ASP A OD1   1 
ATOM   7693  O OD2   . ASP A  1 1054 ? 16.180  62.253  97.518  1.00 32.23 ? 1052 ASP A OD2   1 
ATOM   7694  N N     . PHE A  1 1055 ? 16.787  63.569  102.744 1.00 23.25 ? 1053 PHE A N     1 
ATOM   7695  C CA    . PHE A  1 1055 ? 17.242  64.449  103.819 1.00 24.12 ? 1053 PHE A CA    1 
ATOM   7696  C C     . PHE A  1 1055 ? 17.749  63.655  105.020 1.00 24.54 ? 1053 PHE A C     1 
ATOM   7697  O O     . PHE A  1 1055 ? 18.775  64.013  105.619 1.00 23.66 ? 1053 PHE A O     1 
ATOM   7698  C CB    . PHE A  1 1055 ? 16.101  65.389  104.222 1.00 24.45 ? 1053 PHE A CB    1 
ATOM   7699  C CG    . PHE A  1 1055 ? 16.459  66.343  105.334 1.00 21.96 ? 1053 PHE A CG    1 
ATOM   7700  C CD1   . PHE A  1 1055 ? 17.460  67.274  105.165 1.00 27.85 ? 1053 PHE A CD1   1 
ATOM   7701  C CD2   . PHE A  1 1055 ? 15.768  66.312  106.532 1.00 24.19 ? 1053 PHE A CD2   1 
ATOM   7702  C CE1   . PHE A  1 1055 ? 17.791  68.168  106.197 1.00 27.23 ? 1053 PHE A CE1   1 
ATOM   7703  C CE2   . PHE A  1 1055 ? 16.080  67.205  107.558 1.00 26.46 ? 1053 PHE A CE2   1 
ATOM   7704  C CZ    . PHE A  1 1055 ? 17.093  68.119  107.394 1.00 23.31 ? 1053 PHE A CZ    1 
ATOM   7705  N N     . ALA A  1 1056 ? 17.052  62.573  105.382 1.00 25.33 ? 1054 ALA A N     1 
ATOM   7706  C CA    . ALA A  1 1056 ? 17.492  61.744  106.504 1.00 21.36 ? 1054 ALA A CA    1 
ATOM   7707  C C     . ALA A  1 1056 ? 18.833  61.071  106.223 1.00 26.94 ? 1054 ALA A C     1 
ATOM   7708  O O     . ALA A  1 1056 ? 19.664  60.931  107.128 1.00 26.73 ? 1054 ALA A O     1 
ATOM   7709  C CB    . ALA A  1 1056 ? 16.424  60.694  106.838 1.00 23.06 ? 1054 ALA A CB    1 
ATOM   7710  N N     . LYS A  1 1057 ? 19.058  60.613  104.983 1.00 28.84 ? 1055 LYS A N     1 
ATOM   7711  C CA    . LYS A  1 1057 ? 20.379  60.086  104.630 1.00 32.34 ? 1055 LYS A CA    1 
ATOM   7712  C C     . LYS A  1 1057 ? 21.451  61.169  104.704 1.00 29.47 ? 1055 LYS A C     1 
ATOM   7713  O O     . LYS A  1 1057 ? 22.561  60.928  105.198 1.00 34.30 ? 1055 LYS A O     1 
ATOM   7714  C CB    . LYS A  1 1057 ? 20.340  59.462  103.230 1.00 31.52 ? 1055 LYS A CB    1 
ATOM   7715  C CG    . LYS A  1 1057 ? 19.654  58.110  103.212 1.00 33.47 ? 1055 LYS A CG    1 
ATOM   7716  C CD    . LYS A  1 1057 ? 19.741  57.433  101.858 1.00 32.45 ? 1055 LYS A CD    1 
ATOM   7717  C CE    . LYS A  1 1057 ? 19.202  58.321  100.746 1.00 32.96 ? 1055 LYS A CE    1 
ATOM   7718  N NZ    . LYS A  1 1057 ? 19.034  57.522  99.502  1.00 35.58 ? 1055 LYS A NZ    1 
ATOM   7719  N N     . TRP A  1 1058 ? 21.140  62.368  104.212 1.00 28.53 ? 1056 TRP A N     1 
ATOM   7720  C CA    . TRP A  1 1058 ? 22.074  63.483  104.318 1.00 28.36 ? 1056 TRP A CA    1 
ATOM   7721  C C     . TRP A  1 1058 ? 22.403  63.793  105.775 1.00 33.39 ? 1056 TRP A C     1 
ATOM   7722  O O     . TRP A  1 1058 ? 23.573  64.004  106.118 1.00 32.92 ? 1056 TRP A O     1 
ATOM   7723  C CB    . TRP A  1 1058 ? 21.490  64.718  103.630 1.00 30.60 ? 1056 TRP A CB    1 
ATOM   7724  C CG    . TRP A  1 1058 ? 22.348  65.957  103.734 1.00 33.65 ? 1056 TRP A CG    1 
ATOM   7725  C CD1   . TRP A  1 1058 ? 23.377  66.315  102.906 1.00 33.52 ? 1056 TRP A CD1   1 
ATOM   7726  C CD2   . TRP A  1 1058 ? 22.233  67.012  104.708 1.00 32.58 ? 1056 TRP A CD2   1 
ATOM   7727  N NE1   . TRP A  1 1058 ? 23.909  67.522  103.305 1.00 36.47 ? 1056 TRP A NE1   1 
ATOM   7728  C CE2   . TRP A  1 1058 ? 23.228  67.970  104.407 1.00 35.12 ? 1056 TRP A CE2   1 
ATOM   7729  C CE3   . TRP A  1 1058 ? 21.386  67.238  105.800 1.00 28.18 ? 1056 TRP A CE3   1 
ATOM   7730  C CZ2   . TRP A  1 1058 ? 23.405  69.137  105.163 1.00 34.46 ? 1056 TRP A CZ2   1 
ATOM   7731  C CZ3   . TRP A  1 1058 ? 21.566  68.402  106.559 1.00 31.91 ? 1056 TRP A CZ3   1 
ATOM   7732  C CH2   . TRP A  1 1058 ? 22.570  69.334  106.232 1.00 31.76 ? 1056 TRP A CH2   1 
ATOM   7733  N N     . LEU A  1 1059 ? 21.382  63.823  106.645 1.00 30.30 ? 1057 LEU A N     1 
ATOM   7734  C CA    . LEU A  1 1059 ? 21.616  64.083  108.065 1.00 29.93 ? 1057 LEU A CA    1 
ATOM   7735  C C     . LEU A  1 1059 ? 22.557  63.054  108.659 1.00 31.83 ? 1057 LEU A C     1 
ATOM   7736  O O     . LEU A  1 1059 ? 23.452  63.400  109.434 1.00 34.73 ? 1057 LEU A O     1 
ATOM   7737  C CB    . LEU A  1 1059 ? 20.293  64.076  108.841 1.00 25.48 ? 1057 LEU A CB    1 
ATOM   7738  C CG    . LEU A  1 1059 ? 19.344  65.260  108.699 1.00 29.41 ? 1057 LEU A CG    1 
ATOM   7739  C CD1   . LEU A  1 1059 ? 18.013  64.936  109.366 1.00 27.29 ? 1057 LEU A CD1   1 
ATOM   7740  C CD2   . LEU A  1 1059 ? 19.965  66.524  109.308 1.00 27.32 ? 1057 LEU A CD2   1 
ATOM   7741  N N     . ASP A  1 1060 ? 22.369  61.779  108.301 1.00 29.97 ? 1058 ASP A N     1 
ATOM   7742  C CA    . ASP A  1 1060 ? 23.270  60.723  108.765 1.00 36.15 ? 1058 ASP A CA    1 
ATOM   7743  C C     . ASP A  1 1060 ? 24.692  60.901  108.230 1.00 36.18 ? 1058 ASP A C     1 
ATOM   7744  O O     . ASP A  1 1060 ? 25.668  60.666  108.956 1.00 35.50 ? 1058 ASP A O     1 
ATOM   7745  C CB    . ASP A  1 1060 ? 22.716  59.366  108.351 1.00 39.40 ? 1058 ASP A CB    1 
ATOM   7746  C CG    . ASP A  1 1060 ? 21.872  58.741  109.424 1.00 36.51 ? 1058 ASP A CG    1 
ATOM   7747  O OD1   . ASP A  1 1060 ? 22.167  58.960  110.632 1.00 40.55 ? 1058 ASP A OD1   1 
ATOM   7748  O OD2   . ASP A  1 1060 ? 20.924  58.032  109.063 1.00 39.48 ? 1058 ASP A OD2   1 
ATOM   7749  N N     . GLY A  1 1061 ? 24.831  61.294  106.961 1.00 37.28 ? 1059 GLY A N     1 
ATOM   7750  C CA    . GLY A  1 1061 ? 26.152  61.605  106.428 1.00 34.38 ? 1059 GLY A CA    1 
ATOM   7751  C C     . GLY A  1 1061 ? 26.849  62.729  107.177 1.00 43.04 ? 1059 GLY A C     1 
ATOM   7752  O O     . GLY A  1 1061 ? 28.075  62.716  107.335 1.00 37.21 ? 1059 GLY A O     1 
ATOM   7753  N N     . LYS A  1 1062 ? 26.082  63.717  107.650 1.00 37.46 ? 1060 LYS A N     1 
ATOM   7754  C CA    . LYS A  1 1062 ? 26.646  64.809  108.439 1.00 38.17 ? 1060 LYS A CA    1 
ATOM   7755  C C     . LYS A  1 1062 ? 26.882  64.437  109.899 1.00 39.02 ? 1060 LYS A C     1 
ATOM   7756  O O     . LYS A  1 1062 ? 27.426  65.255  110.645 1.00 41.71 ? 1060 LYS A O     1 
ATOM   7757  C CB    . LYS A  1 1062 ? 25.735  66.037  108.383 1.00 40.18 ? 1060 LYS A CB    1 
ATOM   7758  C CG    . LYS A  1 1062 ? 25.615  66.699  107.016 1.00 39.42 ? 1060 LYS A CG    1 
ATOM   7759  C CD    . LYS A  1 1062 ? 26.851  67.515  106.664 1.00 45.57 ? 1060 LYS A CD    1 
ATOM   7760  C CE    . LYS A  1 1062 ? 26.726  68.124  105.273 1.00 46.94 ? 1060 LYS A CE    1 
ATOM   7761  N NZ    . LYS A  1 1062 ? 27.956  68.849  104.836 1.00 53.90 ? 1060 LYS A NZ    1 
ATOM   7762  N N     . GLY A  1 1063 ? 26.488  63.243  110.331 1.00 39.05 ? 1061 GLY A N     1 
ATOM   7763  C CA    . GLY A  1 1063 ? 26.650  62.851  111.718 1.00 37.34 ? 1061 GLY A CA    1 
ATOM   7764  C C     . GLY A  1 1063 ? 25.491  63.209  112.623 1.00 37.55 ? 1061 GLY A C     1 
ATOM   7765  O O     . GLY A  1 1063 ? 25.532  62.891  113.819 1.00 36.15 ? 1061 GLY A O     1 
ATOM   7766  N N     . ALA A  1 1064 ? 24.450  63.853  112.095 1.00 35.08 ? 1062 ALA A N     1 
ATOM   7767  C CA    . ALA A  1 1064 ? 23.307  64.269  112.905 1.00 30.66 ? 1062 ALA A CA    1 
ATOM   7768  C C     . ALA A  1 1064 ? 22.381  63.066  113.087 1.00 31.20 ? 1062 ALA A C     1 
ATOM   7769  O O     . ALA A  1 1064 ? 21.282  62.985  112.535 1.00 30.14 ? 1062 ALA A O     1 
ATOM   7770  C CB    . ALA A  1 1064 ? 22.604  65.455  112.256 1.00 33.41 ? 1062 ALA A CB    1 
ATOM   7771  N N     . ARG A  1 1065 ? 22.872  62.102  113.871 1.00 30.82 ? 1063 ARG A N     1 
ATOM   7772  C CA    . ARG A  1 1065 ? 22.206  60.805  113.976 1.00 36.07 ? 1063 ARG A CA    1 
ATOM   7773  C C     . ARG A  1 1065 ? 20.836  60.924  114.638 1.00 32.49 ? 1063 ARG A C     1 
ATOM   7774  O O     . ARG A  1 1065 ? 19.875  60.279  114.207 1.00 32.37 ? 1063 ARG A O     1 
ATOM   7775  C CB    . ARG A  1 1065 ? 23.089  59.824  114.754 1.00 36.09 ? 1063 ARG A CB    1 
ATOM   7776  N N     . ALA A  1 1066 ? 20.730  61.719  115.703 1.00 29.55 ? 1064 ALA A N     1 
ATOM   7777  C CA    . ALA A  1 1066 ? 19.450  61.860  116.383 1.00 27.80 ? 1064 ALA A CA    1 
ATOM   7778  C C     . ALA A  1 1066 ? 18.422  62.514  115.467 1.00 33.16 ? 1064 ALA A C     1 
ATOM   7779  O O     . ALA A  1 1066 ? 17.259  62.086  115.408 1.00 28.13 ? 1064 ALA A O     1 
ATOM   7780  C CB    . ALA A  1 1066 ? 19.621  62.678  117.663 1.00 31.32 ? 1064 ALA A CB    1 
ATOM   7781  N N     . GLU A  1 1067 ? 18.843  63.552  114.739 1.00 29.79 ? 1065 GLU A N     1 
ATOM   7782  C CA    . GLU A  1 1067 ? 17.944  64.233  113.816 1.00 29.51 ? 1065 GLU A CA    1 
ATOM   7783  C C     . GLU A  1 1067 ? 17.524  63.307  112.687 1.00 26.48 ? 1065 GLU A C     1 
ATOM   7784  O O     . GLU A  1 1067 ? 16.357  63.308  112.271 1.00 25.44 ? 1065 GLU A O     1 
ATOM   7785  C CB    . GLU A  1 1067 ? 18.625  65.480  113.252 1.00 29.03 ? 1065 GLU A CB    1 
ATOM   7786  C CG    . GLU A  1 1067 ? 18.746  66.645  114.238 1.00 30.03 ? 1065 GLU A CG    1 
ATOM   7787  C CD    . GLU A  1 1067 ? 19.887  66.490  115.230 1.00 37.60 ? 1065 GLU A CD    1 
ATOM   7788  O OE1   . GLU A  1 1067 ? 20.679  65.523  115.120 1.00 31.28 ? 1065 GLU A OE1   1 
ATOM   7789  O OE2   . GLU A  1 1067 ? 19.988  67.357  116.128 1.00 34.50 ? 1065 GLU A OE2   1 
ATOM   7790  N N     . ALA A  1 1068 ? 18.472  62.517  112.180 1.00 27.99 ? 1066 ALA A N     1 
ATOM   7791  C CA    . ALA A  1 1068 ? 18.166  61.593  111.095 1.00 29.07 ? 1066 ALA A CA    1 
ATOM   7792  C C     . ALA A  1 1068 ? 17.118  60.577  111.524 1.00 29.95 ? 1066 ALA A C     1 
ATOM   7793  O O     . ALA A  1 1068 ? 16.221  60.229  110.745 1.00 27.15 ? 1066 ALA A O     1 
ATOM   7794  C CB    . ALA A  1 1068 ? 19.449  60.897  110.632 1.00 29.55 ? 1066 ALA A CB    1 
ATOM   7795  N N     . GLU A  1 1069 ? 17.219  60.083  112.763 1.00 28.32 ? 1067 GLU A N     1 
ATOM   7796  C CA    . GLU A  1 1069 ? 16.204  59.172  113.282 1.00 31.73 ? 1067 GLU A CA    1 
ATOM   7797  C C     . GLU A  1 1069 ? 14.852  59.867  113.424 1.00 31.69 ? 1067 GLU A C     1 
ATOM   7798  O O     . GLU A  1 1069 ? 13.808  59.280  113.113 1.00 27.90 ? 1067 GLU A O     1 
ATOM   7799  C CB    . GLU A  1 1069 ? 16.658  58.600  114.625 1.00 36.11 ? 1067 GLU A CB    1 
ATOM   7800  C CG    . GLU A  1 1069 ? 15.558  57.922  115.413 1.00 37.44 ? 1067 GLU A CG    1 
ATOM   7801  C CD    . GLU A  1 1069 ? 15.353  56.470  115.021 1.00 44.32 ? 1067 GLU A CD    1 
ATOM   7802  O OE1   . GLU A  1 1069 ? 15.658  56.105  113.861 1.00 50.57 ? 1067 GLU A OE1   1 
ATOM   7803  O OE2   . GLU A  1 1069 ? 14.888  55.690  115.884 1.00 55.08 ? 1067 GLU A OE2   1 
ATOM   7804  N N     . ALA A  1 1070 ? 14.853  61.111  113.907 1.00 29.77 ? 1068 ALA A N     1 
ATOM   7805  C CA    . ALA A  1 1070 ? 13.617  61.882  113.990 1.00 31.16 ? 1068 ALA A CA    1 
ATOM   7806  C C     . ALA A  1 1070 ? 13.033  62.132  112.605 1.00 28.27 ? 1068 ALA A C     1 
ATOM   7807  O O     . ALA A  1 1070 ? 11.811  62.126  112.423 1.00 26.48 ? 1068 ALA A O     1 
ATOM   7808  C CB    . ALA A  1 1070 ? 13.874  63.205  114.706 1.00 27.76 ? 1068 ALA A CB    1 
ATOM   7809  N N     . ALA A  1 1071 ? 13.894  62.356  111.616 1.00 26.87 ? 1069 ALA A N     1 
ATOM   7810  C CA    . ALA A  1 1071 ? 13.403  62.538  110.257 1.00 26.55 ? 1069 ALA A CA    1 
ATOM   7811  C C     . ALA A  1 1071 ? 12.703  61.277  109.748 1.00 27.37 ? 1069 ALA A C     1 
ATOM   7812  O O     . ALA A  1 1071 ? 11.631  61.352  109.141 1.00 23.35 ? 1069 ALA A O     1 
ATOM   7813  C CB    . ALA A  1 1071 ? 14.561  62.933  109.338 1.00 21.19 ? 1069 ALA A CB    1 
ATOM   7814  N N     . ARG A  1 1072 ? 13.296  60.107  109.980 1.00 27.03 ? 1070 ARG A N     1 
ATOM   7815  C CA    . ARG A  1 1072 ? 12.656  58.873  109.531 1.00 27.64 ? 1070 ARG A CA    1 
ATOM   7816  C C     . ARG A  1 1072 ? 11.354  58.637  110.278 1.00 27.18 ? 1070 ARG A C     1 
ATOM   7817  O O     . ARG A  1 1072 ? 10.371  58.180  109.690 1.00 27.31 ? 1070 ARG A O     1 
ATOM   7818  C CB    . ARG A  1 1072 ? 13.604  57.679  109.701 1.00 25.49 ? 1070 ARG A CB    1 
ATOM   7819  C CG    . ARG A  1 1072 ? 14.816  57.722  108.779 1.00 31.92 ? 1070 ARG A CG    1 
ATOM   7820  C CD    . ARG A  1 1072 ? 15.704  56.473  108.910 1.00 33.81 ? 1070 ARG A CD    1 
ATOM   7821  N NE    . ARG A  1 1072 ? 16.416  56.422  110.183 1.00 36.34 ? 1070 ARG A NE    1 
ATOM   7822  C CZ    . ARG A  1 1072 ? 17.635  56.909  110.371 1.00 36.09 ? 1070 ARG A CZ    1 
ATOM   7823  N NH1   . ARG A  1 1072 ? 18.287  57.530  109.398 1.00 35.51 ? 1070 ARG A NH1   1 
ATOM   7824  N NH2   . ARG A  1 1072 ? 18.219  56.763  111.560 1.00 34.06 ? 1070 ARG A NH2   1 
ATOM   7825  N N     . ASN A  1 1073 ? 11.315  58.965  111.566 1.00 24.50 ? 1071 ASN A N     1 
ATOM   7826  C CA    . ASN A  1 1073 ? 10.060  58.834  112.296 1.00 28.19 ? 1071 ASN A CA    1 
ATOM   7827  C C     . ASN A  1 1073 ? 9.000   59.782  111.750 1.00 26.56 ? 1071 ASN A C     1 
ATOM   7828  O O     . ASN A  1 1073 ? 7.820   59.426  111.680 1.00 25.34 ? 1071 ASN A O     1 
ATOM   7829  C CB    . ASN A  1 1073 ? 10.292  59.090  113.779 1.00 30.76 ? 1071 ASN A CB    1 
ATOM   7830  C CG    . ASN A  1 1073 ? 11.101  57.998  114.425 1.00 34.13 ? 1071 ASN A CG    1 
ATOM   7831  O OD1   . ASN A  1 1073 ? 11.145  56.863  113.932 1.00 33.06 ? 1071 ASN A OD1   1 
ATOM   7832  N ND2   . ASN A  1 1073 ? 11.753  58.327  115.534 1.00 36.33 ? 1071 ASN A ND2   1 
ATOM   7833  N N     . ALA A  1 1074 ? 9.400   60.996  111.355 1.00 26.69 ? 1072 ALA A N     1 
ATOM   7834  C CA    . ALA A  1 1074 ? 8.443   61.899  110.720 1.00 24.23 ? 1072 ALA A CA    1 
ATOM   7835  C C     . ALA A  1 1074 ? 7.961   61.334  109.390 1.00 23.64 ? 1072 ALA A C     1 
ATOM   7836  O O     . ALA A  1 1074 ? 6.780   61.445  109.053 1.00 24.53 ? 1072 ALA A O     1 
ATOM   7837  C CB    . ALA A  1 1074 ? 9.060   63.286  110.521 1.00 23.21 ? 1072 ALA A CB    1 
ATOM   7838  N N     . GLY A  1 1075 ? 8.860   60.724  108.617 1.00 25.23 ? 1073 GLY A N     1 
ATOM   7839  C CA    . GLY A  1 1075 ? 8.445   60.132  107.350 1.00 21.60 ? 1073 GLY A CA    1 
ATOM   7840  C C     . GLY A  1 1075 ? 7.377   59.068  107.533 1.00 26.95 ? 1073 GLY A C     1 
ATOM   7841  O O     . GLY A  1 1075 ? 6.438   58.975  106.737 1.00 26.11 ? 1073 GLY A O     1 
ATOM   7842  N N     . SER A  1 1076 ? 7.497   58.262  108.598 1.00 25.60 ? 1074 SER A N     1 
ATOM   7843  C CA    . SER A  1 1076 ? 6.505   57.225  108.874 1.00 26.82 ? 1074 SER A CA    1 
ATOM   7844  C C     . SER A  1 1076 ? 5.227   57.793  109.479 1.00 25.52 ? 1074 SER A C     1 
ATOM   7845  O O     . SER A  1 1076 ? 4.129   57.328  109.150 1.00 32.26 ? 1074 SER A O     1 
ATOM   7846  C CB    . SER A  1 1076 ? 7.083   56.167  109.818 1.00 26.31 ? 1074 SER A CB    1 
ATOM   7847  O OG    . SER A  1 1076 ? 8.157   55.477  109.210 1.00 35.31 ? 1074 SER A OG    1 
ATOM   7848  N N     . SER A  1 1077 ? 5.342   58.784  110.369 1.00 24.58 ? 1075 SER A N     1 
ATOM   7849  C CA    A SER A  1 1077 ? 4.177   59.351  111.043 0.32 27.29 ? 1075 SER A CA    1 
ATOM   7850  C CA    B SER A  1 1077 ? 4.149   59.307  111.018 0.48 27.16 ? 1075 SER A CA    1 
ATOM   7851  C CA    C SER A  1 1077 ? 4.157   59.319  111.029 0.20 27.34 ? 1075 SER A CA    1 
ATOM   7852  C C     . SER A  1 1077 ? 3.328   60.213  110.112 1.00 25.70 ? 1075 SER A C     1 
ATOM   7853  O O     . SER A  1 1077 ? 2.133   60.391  110.360 1.00 26.21 ? 1075 SER A O     1 
ATOM   7854  C CB    A SER A  1 1077 ? 4.628   60.174  112.253 0.32 25.11 ? 1075 SER A CB    1 
ATOM   7855  C CB    B SER A  1 1077 ? 4.534   60.046  112.295 0.48 25.14 ? 1075 SER A CB    1 
ATOM   7856  C CB    C SER A  1 1077 ? 4.555   60.084  112.295 0.20 25.13 ? 1075 SER A CB    1 
ATOM   7857  O OG    A SER A  1 1077 ? 3.555   60.921  112.802 0.32 24.59 ? 1075 SER A OG    1 
ATOM   7858  O OG    B SER A  1 1077 ? 4.936   59.104  113.266 0.48 23.92 ? 1075 SER A OG    1 
ATOM   7859  O OG    C SER A  1 1077 ? 5.546   61.058  112.027 0.20 24.74 ? 1075 SER A OG    1 
ATOM   7860  N N     . SER A  1 1078 ? 3.927   60.780  109.073 1.00 23.97 ? 1076 SER A N     1 
ATOM   7861  C CA    . SER A  1 1078 ? 3.172   61.600  108.136 1.00 22.41 ? 1076 SER A CA    1 
ATOM   7862  C C     . SER A  1 1078 ? 2.030   60.805  107.517 1.00 27.00 ? 1076 SER A C     1 
ATOM   7863  O O     . SER A  1 1078 ? 2.167   59.619  107.212 1.00 23.77 ? 1076 SER A O     1 
ATOM   7864  C CB    . SER A  1 1078 ? 4.087   62.107  107.023 1.00 24.52 ? 1076 SER A CB    1 
ATOM   7865  O OG    . SER A  1 1078 ? 3.302   62.711  106.001 1.00 22.59 ? 1076 SER A OG    1 
ATOM   7866  N N     . ALA A  1 1079 ? 0.892   61.458  107.329 1.00 24.57 ? 1077 ALA A N     1 
ATOM   7867  C CA    . ALA A  1 1079 ? -0.230  60.821  106.661 1.00 26.92 ? 1077 ALA A CA    1 
ATOM   7868  C C     . ALA A  1 1079 ? -0.386  61.336  105.242 1.00 24.91 ? 1077 ALA A C     1 
ATOM   7869  O O     . ALA A  1 1079 ? -1.396  61.050  104.591 1.00 22.31 ? 1077 ALA A O     1 
ATOM   7870  C CB    . ALA A  1 1079 ? -1.524  61.015  107.457 1.00 25.36 ? 1077 ALA A CB    1 
ATOM   7871  N N     . LEU A  1 1080 ? 0.605   62.081  104.754 1.00 22.96 ? 1078 LEU A N     1 
ATOM   7872  C CA    . LEU A  1 1080 ? 0.673   62.432  103.342 1.00 21.90 ? 1078 LEU A CA    1 
ATOM   7873  C C     . LEU A  1 1080 ? 0.471   61.196  102.476 1.00 20.83 ? 1078 LEU A C     1 
ATOM   7874  O O     . LEU A  1 1080 ? 1.139   60.178  102.664 1.00 22.23 ? 1078 LEU A O     1 
ATOM   7875  C CB    . LEU A  1 1080 ? 2.032   63.058  103.053 1.00 22.46 ? 1078 LEU A CB    1 
ATOM   7876  C CG    . LEU A  1 1080 ? 2.317   63.292  101.574 1.00 24.80 ? 1078 LEU A CG    1 
ATOM   7877  C CD1   . LEU A  1 1080 ? 1.450   64.442  101.038 1.00 22.87 ? 1078 LEU A CD1   1 
ATOM   7878  C CD2   . LEU A  1 1080 ? 3.797   63.562  101.398 1.00 21.07 ? 1078 LEU A CD2   1 
ATOM   7879  N N     . GLY A  1 1081 ? -0.461  61.284  101.525 1.00 20.20 ? 1079 GLY A N     1 
ATOM   7880  C CA    . GLY A  1 1081 ? -0.772  60.165  100.664 1.00 24.99 ? 1079 GLY A CA    1 
ATOM   7881  C C     . GLY A  1 1081 ? -1.983  59.366  101.096 1.00 23.00 ? 1079 GLY A C     1 
ATOM   7882  O O     . GLY A  1 1081 ? -2.390  58.449  100.374 1.00 22.00 ? 1079 GLY A O     1 
ATOM   7883  N N     . LEU A  1 1082 ? -2.558  59.673  102.257 1.00 22.19 ? 1080 LEU A N     1 
ATOM   7884  C CA    . LEU A  1 1082 ? -3.823  59.056  102.628 1.00 22.40 ? 1080 LEU A CA    1 
ATOM   7885  C C     . LEU A  1 1082 ? -4.814  59.261  101.490 1.00 20.81 ? 1080 LEU A C     1 
ATOM   7886  O O     . LEU A  1 1082 ? -4.874  60.343  100.905 1.00 19.80 ? 1080 LEU A O     1 
ATOM   7887  C CB    . LEU A  1 1082 ? -4.355  59.670  103.934 1.00 22.56 ? 1080 LEU A CB    1 
ATOM   7888  C CG    . LEU A  1 1082 ? -5.697  59.210  104.512 1.00 23.05 ? 1080 LEU A CG    1 
ATOM   7889  C CD1   . LEU A  1 1082 ? -5.793  59.649  105.952 1.00 25.25 ? 1080 LEU A CD1   1 
ATOM   7890  C CD2   . LEU A  1 1082 ? -6.857  59.863  103.759 1.00 26.48 ? 1080 LEU A CD2   1 
ATOM   7891  N N     . ASP A  1 1083 ? -5.594  58.220  101.187 1.00 23.33 ? 1081 ASP A N     1 
ATOM   7892  C CA    . ASP A  1 1083 ? -6.520  58.268  100.050 1.00 23.35 ? 1081 ASP A CA    1 
ATOM   7893  C C     . ASP A  1 1083 ? -7.708  57.356  100.351 1.00 25.89 ? 1081 ASP A C     1 
ATOM   7894  O O     . ASP A  1 1083 ? -7.619  56.141  100.177 1.00 26.00 ? 1081 ASP A O     1 
ATOM   7895  C CB    . ASP A  1 1083 ? -5.803  57.856  98.775  1.00 26.52 ? 1081 ASP A CB    1 
ATOM   7896  C CG    . ASP A  1 1083 ? -6.629  58.092  97.529  1.00 33.14 ? 1081 ASP A CG    1 
ATOM   7897  O OD1   . ASP A  1 1083 ? -7.765  58.599  97.633  1.00 35.51 ? 1081 ASP A OD1   1 
ATOM   7898  O OD2   . ASP A  1 1083 ? -6.128  57.761  96.434  1.00 41.04 ? 1081 ASP A OD2   1 
ATOM   7899  N N     . LEU A  1 1084 ? -8.825  57.947  100.766 1.00 24.95 ? 1082 LEU A N     1 
ATOM   7900  C CA    . LEU A  1 1084 ? -9.945  57.175  101.269 1.00 23.69 ? 1082 LEU A CA    1 
ATOM   7901  C C     . LEU A  1 1084 ? -11.198 57.447  100.460 1.00 24.34 ? 1082 LEU A C     1 
ATOM   7902  O O     . LEU A  1 1084 ? -11.371 58.527  99.897  1.00 20.97 ? 1082 LEU A O     1 
ATOM   7903  C CB    . LEU A  1 1084 ? -10.232 57.499  102.730 1.00 25.91 ? 1082 LEU A CB    1 
ATOM   7904  C CG    . LEU A  1 1084 ? -9.168  57.135  103.744 1.00 28.58 ? 1082 LEU A CG    1 
ATOM   7905  C CD1   . LEU A  1 1084 ? -9.640  57.556  105.134 1.00 27.21 ? 1082 LEU A CD1   1 
ATOM   7906  C CD2   . LEU A  1 1084 ? -8.869  55.647  103.687 1.00 30.26 ? 1082 LEU A CD2   1 
ATOM   7907  N N     . GLU A  1 1085 ? -12.086 56.464  100.410 1.00 27.15 ? 1083 GLU A N     1 
ATOM   7908  C CA    . GLU A  1 1085 ? -13.427 56.707  99.895  1.00 24.72 ? 1083 GLU A CA    1 
ATOM   7909  C C     . GLU A  1 1085 ? -14.385 56.703  101.072 1.00 29.09 ? 1083 GLU A C     1 
ATOM   7910  O O     . GLU A  1 1085 ? -14.385 55.757  101.865 1.00 29.04 ? 1083 GLU A O     1 
ATOM   7911  C CB    . GLU A  1 1085 ? -13.846 55.678  98.848  1.00 29.85 ? 1083 GLU A CB    1 
ATOM   7912  C CG    . GLU A  1 1085 ? -15.223 56.019  98.302  1.00 29.08 ? 1083 GLU A CG    1 
ATOM   7913  C CD    . GLU A  1 1085 ? -15.692 55.140  97.157  1.00 35.19 ? 1083 GLU A CD    1 
ATOM   7914  O OE1   . GLU A  1 1085 ? -14.843 54.612  96.398  1.00 36.09 ? 1083 GLU A OE1   1 
ATOM   7915  O OE2   . GLU A  1 1085 ? -16.932 55.001  97.019  1.00 35.93 ? 1083 GLU A OE2   1 
ATOM   7916  N N     . LEU A  1 1086 ? -15.174 57.776  101.200 1.00 23.89 ? 1084 LEU A N     1 
ATOM   7917  C CA    . LEU A  1 1086 ? -16.062 57.949  102.342 1.00 26.60 ? 1084 LEU A CA    1 
ATOM   7918  C C     . LEU A  1 1086 ? -17.458 57.407  102.029 1.00 25.40 ? 1084 LEU A C     1 
ATOM   7919  O O     . LEU A  1 1086 ? -17.953 57.574  100.909 1.00 25.50 ? 1084 LEU A O     1 
ATOM   7920  C CB    . LEU A  1 1086 ? -16.155 59.421  102.731 1.00 23.54 ? 1084 LEU A CB    1 
ATOM   7921  C CG    . LEU A  1 1086 ? -14.806 60.098  103.006 1.00 25.87 ? 1084 LEU A CG    1 
ATOM   7922  C CD1   . LEU A  1 1086 ? -15.002 61.572  103.414 1.00 26.39 ? 1084 LEU A CD1   1 
ATOM   7923  C CD2   . LEU A  1 1086 ? -14.037 59.326  104.093 1.00 23.77 ? 1084 LEU A CD2   1 
ATOM   7924  N N     . PRO A  1 1087 ? -18.086 56.744  102.997 1.00 27.27 ? 1085 PRO A N     1 
ATOM   7925  C CA    . PRO A  1 1087 ? -19.452 56.239  102.787 1.00 27.79 ? 1085 PRO A CA    1 
ATOM   7926  C C     . PRO A  1 1087 ? -20.426 57.373  102.504 1.00 28.60 ? 1085 PRO A C     1 
ATOM   7927  O O     . PRO A  1 1087 ? -20.333 58.457  103.082 1.00 28.25 ? 1085 PRO A O     1 
ATOM   7928  C CB    . PRO A  1 1087 ? -19.790 55.539  104.109 1.00 28.36 ? 1085 PRO A CB    1 
ATOM   7929  C CG    . PRO A  1 1087 ? -18.508 55.383  104.838 1.00 31.72 ? 1085 PRO A CG    1 
ATOM   7930  C CD    . PRO A  1 1087 ? -17.537 56.395  104.317 1.00 26.99 ? 1085 PRO A CD    1 
ATOM   7931  N N     . GLY A  1 1088 ? -21.369 57.113  101.600 1.00 27.51 ? 1086 GLY A N     1 
ATOM   7932  C CA    . GLY A  1 1088 ? -22.349 58.101  101.209 1.00 28.03 ? 1086 GLY A CA    1 
ATOM   7933  C C     . GLY A  1 1088 ? -23.440 57.484  100.351 1.00 21.97 ? 1086 GLY A C     1 
ATOM   7934  O O     . GLY A  1 1088 ? -23.630 56.265  100.324 1.00 23.47 ? 1086 GLY A O     1 
ATOM   7935  N N     . PRO A  1 1089 ? -24.163 58.317  99.616  1.00 23.55 ? 1087 PRO A N     1 
ATOM   7936  C CA    . PRO A  1 1089 ? -25.261 57.803  98.794  1.00 22.55 ? 1087 PRO A CA    1 
ATOM   7937  C C     . PRO A  1 1089 ? -24.730 57.012  97.611  1.00 26.64 ? 1087 PRO A C     1 
ATOM   7938  O O     . PRO A  1 1089 ? -23.567 57.137  97.216  1.00 24.98 ? 1087 PRO A O     1 
ATOM   7939  C CB    . PRO A  1 1089 ? -25.968 59.079  98.324  1.00 24.97 ? 1087 PRO A CB    1 
ATOM   7940  C CG    . PRO A  1 1089 ? -24.858 60.071  98.246  1.00 29.07 ? 1087 PRO A CG    1 
ATOM   7941  C CD    . PRO A  1 1089 ? -23.976 59.768  99.431  1.00 25.83 ? 1087 PRO A CD    1 
ATOM   7942  N N     . VAL A  1 1090 ? -25.615 56.189  97.039  1.00 25.55 ? 1088 VAL A N     1 
ATOM   7943  C CA    . VAL A  1 1090 ? -25.301 55.544  95.774  1.00 22.56 ? 1088 VAL A CA    1 
ATOM   7944  C C     . VAL A  1 1090 ? -25.207 56.594  94.676  1.00 22.36 ? 1088 VAL A C     1 
ATOM   7945  O O     . VAL A  1 1090 ? -25.743 57.705  94.778  1.00 23.40 ? 1088 VAL A O     1 
ATOM   7946  C CB    . VAL A  1 1090 ? -26.344 54.473  95.411  1.00 23.75 ? 1088 VAL A CB    1 
ATOM   7947  C CG1   . VAL A  1 1090 ? -26.422 53.414  96.480  1.00 23.65 ? 1088 VAL A CG1   1 
ATOM   7948  C CG2   . VAL A  1 1090 ? -27.714 55.126  95.183  1.00 23.03 ? 1088 VAL A CG2   1 
ATOM   7949  N N     . GLY A  1 1091 ? -24.535 56.220  93.593  1.00 24.45 ? 1089 GLY A N     1 
ATOM   7950  C CA    . GLY A  1 1091 ? -24.434 57.107  92.451  1.00 24.04 ? 1089 GLY A CA    1 
ATOM   7951  C C     . GLY A  1 1091 ? -23.490 58.257  92.650  1.00 25.50 ? 1089 GLY A C     1 
ATOM   7952  O O     . GLY A  1 1091 ? -23.560 59.246  91.909  1.00 22.43 ? 1089 GLY A O     1 
ATOM   7953  N N     . GLU A  1 1092 ? -22.609 58.159  93.643  1.00 23.01 ? 1090 GLU A N     1 
ATOM   7954  C CA    . GLU A  1 1092 ? -21.662 59.211  93.942  1.00 24.23 ? 1090 GLU A CA    1 
ATOM   7955  C C     . GLU A  1 1092 ? -20.436 58.547  94.555  1.00 24.97 ? 1090 GLU A C     1 
ATOM   7956  O O     . GLU A  1 1092 ? -20.566 57.558  95.277  1.00 22.39 ? 1090 GLU A O     1 
ATOM   7957  C CB    . GLU A  1 1092 ? -22.305 60.227  94.896  1.00 25.89 ? 1090 GLU A CB    1 
ATOM   7958  C CG    . GLU A  1 1092 ? -21.602 61.575  95.004  1.00 28.30 ? 1090 GLU A CG    1 
ATOM   7959  C CD    . GLU A  1 1092 ? -22.415 62.558  95.849  1.00 32.15 ? 1090 GLU A CD    1 
ATOM   7960  O OE1   . GLU A  1 1092 ? -22.366 62.451  97.102  1.00 27.86 ? 1090 GLU A OE1   1 
ATOM   7961  O OE2   . GLU A  1 1092 ? -23.127 63.409  95.253  1.00 33.38 ? 1090 GLU A OE2   1 
ATOM   7962  N N     . ARG A  1 1093 ? -19.252 59.067  94.257  1.00 20.22 ? 1091 ARG A N     1 
ATOM   7963  C CA    . ARG A  1 1093 ? -18.031 58.601  94.909  1.00 23.11 ? 1091 ARG A CA    1 
ATOM   7964  C C     . ARG A  1 1093 ? -17.415 59.794  95.619  1.00 22.91 ? 1091 ARG A C     1 
ATOM   7965  O O     . ARG A  1 1093 ? -17.113 60.810  94.988  1.00 20.84 ? 1091 ARG A O     1 
ATOM   7966  C CB    . ARG A  1 1093 ? -17.028 57.982  93.925  1.00 26.73 ? 1091 ARG A CB    1 
ATOM   7967  C CG    . ARG A  1 1093 ? -17.358 56.566  93.481  1.00 34.90 ? 1091 ARG A CG    1 
ATOM   7968  C CD    . ARG A  1 1093 ? -16.087 55.806  93.040  1.00 42.72 ? 1091 ARG A CD    1 
ATOM   7969  N NE    . ARG A  1 1093 ? -15.416 56.480  91.936  1.00 47.24 ? 1091 ARG A NE    1 
ATOM   7970  C CZ    . ARG A  1 1093 ? -15.745 56.335  90.658  1.00 47.86 ? 1091 ARG A CZ    1 
ATOM   7971  N NH1   . ARG A  1 1093 ? -16.698 55.495  90.279  1.00 51.71 ? 1091 ARG A NH1   1 
ATOM   7972  N NH2   . ARG A  1 1093 ? -15.105 57.051  89.736  1.00 45.77 ? 1091 ARG A NH2   1 
ATOM   7973  N N     . ASN A  1 1094 ? -17.216 59.667  96.922  1.00 22.81 ? 1092 ASN A N     1 
ATOM   7974  C CA    . ASN A  1 1094 ? -16.724 60.772  97.728  1.00 21.34 ? 1092 ASN A CA    1 
ATOM   7975  C C     . ASN A  1 1094 ? -15.366 60.414  98.296  1.00 21.73 ? 1092 ASN A C     1 
ATOM   7976  O O     . ASN A  1 1094 ? -15.238 59.440  99.040  1.00 24.28 ? 1092 ASN A O     1 
ATOM   7977  C CB    . ASN A  1 1094 ? -17.725 61.104  98.820  1.00 20.43 ? 1092 ASN A CB    1 
ATOM   7978  C CG    . ASN A  1 1094 ? -18.935 61.750  98.238  1.00 21.75 ? 1092 ASN A CG    1 
ATOM   7979  O OD1   . ASN A  1 1094 ? -18.859 62.882  97.793  1.00 22.98 ? 1092 ASN A OD1   1 
ATOM   7980  N ND2   . ASN A  1 1094 ? -20.042 61.032  98.195  1.00 21.82 ? 1092 ASN A ND2   1 
ATOM   7981  N N     . LEU A  1 1095 ? -14.361 61.178  97.909  1.00 22.14 ? 1093 LEU A N     1 
ATOM   7982  C CA    . LEU A  1 1095 ? -12.976 60.836  98.175  1.00 22.46 ? 1093 LEU A CA    1 
ATOM   7983  C C     . LEU A  1 1095 ? -12.356 61.898  99.060  1.00 20.69 ? 1093 LEU A C     1 
ATOM   7984  O O     . LEU A  1 1095 ? -12.701 63.077  98.972  1.00 22.38 ? 1093 LEU A O     1 
ATOM   7985  C CB    . LEU A  1 1095 ? -12.188 60.721  96.884  1.00 20.65 ? 1093 LEU A CB    1 
ATOM   7986  C CG    . LEU A  1 1095 ? -12.871 59.817  95.854  1.00 24.61 ? 1093 LEU A CG    1 
ATOM   7987  C CD1   . LEU A  1 1095 ? -12.136 59.896  94.525  1.00 29.98 ? 1093 LEU A CD1   1 
ATOM   7988  C CD2   . LEU A  1 1095 ? -12.962 58.371  96.342  1.00 24.98 ? 1093 LEU A CD2   1 
ATOM   7989  N N     . TYR A  1 1096 ? -11.415 61.457  99.889  1.00 21.61 ? 1094 TYR A N     1 
ATOM   7990  C CA    . TYR A  1 1096 ? -10.757 62.299  100.879 1.00 21.95 ? 1094 TYR A CA    1 
ATOM   7991  C C     . TYR A  1 1096 ? -9.279  61.966  100.825 1.00 19.81 ? 1094 TYR A C     1 
ATOM   7992  O O     . TYR A  1 1096 ? -8.904  60.804  101.014 1.00 23.04 ? 1094 TYR A O     1 
ATOM   7993  C CB    . TYR A  1 1096 ? -11.326 62.024  102.274 1.00 20.95 ? 1094 TYR A CB    1 
ATOM   7994  C CG    . TYR A  1 1096 ? -10.642 62.737  103.418 1.00 23.45 ? 1094 TYR A CG    1 
ATOM   7995  C CD1   . TYR A  1 1096 ? -10.978 64.042  103.745 1.00 21.44 ? 1094 TYR A CD1   1 
ATOM   7996  C CD2   . TYR A  1 1096 ? -9.721  62.074  104.223 1.00 25.25 ? 1094 TYR A CD2   1 
ATOM   7997  C CE1   . TYR A  1 1096 ? -10.385 64.691  104.811 1.00 25.22 ? 1094 TYR A CE1   1 
ATOM   7998  C CE2   . TYR A  1 1096 ? -9.112  62.721  105.294 1.00 26.94 ? 1094 TYR A CE2   1 
ATOM   7999  C CZ    . TYR A  1 1096 ? -9.461  64.030  105.582 1.00 24.65 ? 1094 TYR A CZ    1 
ATOM   8000  O OH    . TYR A  1 1096 ? -8.871  64.696  106.627 1.00 26.84 ? 1094 TYR A OH    1 
ATOM   8001  N N     . THR A  1 1097 ? -8.446  62.970  100.562 1.00 23.13 ? 1095 THR A N     1 
ATOM   8002  C CA    . THR A  1 1097 ? -7.024  62.745  100.330 1.00 23.54 ? 1095 THR A CA    1 
ATOM   8003  C C     . THR A  1 1097 ? -6.191  63.798  101.051 1.00 21.01 ? 1095 THR A C     1 
ATOM   8004  O O     . THR A  1 1097 ? -6.616  64.946  101.209 1.00 20.77 ? 1095 THR A O     1 
ATOM   8005  C CB    . THR A  1 1097 ? -6.707  62.779  98.831  1.00 23.22 ? 1095 THR A CB    1 
ATOM   8006  O OG1   . THR A  1 1097 ? -7.156  64.024  98.281  1.00 27.22 ? 1095 THR A OG1   1 
ATOM   8007  C CG2   . THR A  1 1097 ? -7.416  61.660  98.118  1.00 23.93 ? 1095 THR A CG2   1 
ATOM   8008  N N     . LEU A  1 1098 ? -4.984  63.406  101.466 1.00 20.97 ? 1096 LEU A N     1 
ATOM   8009  C CA    . LEU A  1 1098 ? -4.047  64.304  102.140 1.00 20.84 ? 1096 LEU A CA    1 
ATOM   8010  C C     . LEU A  1 1098 ? -2.872  64.575  101.211 1.00 21.22 ? 1096 LEU A C     1 
ATOM   8011  O O     . LEU A  1 1098 ? -2.182  63.641  100.789 1.00 23.42 ? 1096 LEU A O     1 
ATOM   8012  C CB    . LEU A  1 1098 ? -3.556  63.710  103.459 1.00 21.61 ? 1096 LEU A CB    1 
ATOM   8013  C CG    . LEU A  1 1098 ? -4.609  63.527  104.554 1.00 24.09 ? 1096 LEU A CG    1 
ATOM   8014  C CD1   . LEU A  1 1098 ? -3.924  63.008  105.816 1.00 19.63 ? 1096 LEU A CD1   1 
ATOM   8015  C CD2   . LEU A  1 1098 ? -5.373  64.832  104.826 1.00 21.28 ? 1096 LEU A CD2   1 
ATOM   8016  N N     . HIS A  1 1099 ? -2.653  65.849  100.901 1.00 22.51 ? 1097 HIS A N     1 
ATOM   8017  C CA    . HIS A  1 1099 ? -1.609  66.318  100.000 1.00 21.29 ? 1097 HIS A CA    1 
ATOM   8018  C C     . HIS A  1 1099 ? -0.680  67.247  100.762 1.00 22.50 ? 1097 HIS A C     1 
ATOM   8019  O O     . HIS A  1 1099 ? -0.959  67.631  101.902 1.00 24.47 ? 1097 HIS A O     1 
ATOM   8020  C CB    . HIS A  1 1099 ? -2.208  67.081  98.814  1.00 22.83 ? 1097 HIS A CB    1 
ATOM   8021  C CG    . HIS A  1 1099 ? -3.177  66.279  98.007  1.00 27.56 ? 1097 HIS A CG    1 
ATOM   8022  N ND1   . HIS A  1 1099 ? -2.842  65.714  96.797  1.00 27.17 ? 1097 HIS A ND1   1 
ATOM   8023  C CD2   . HIS A  1 1099 ? -4.466  65.935  98.242  1.00 25.54 ? 1097 HIS A CD2   1 
ATOM   8024  C CE1   . HIS A  1 1099 ? -3.887  65.066  96.313  1.00 29.68 ? 1097 HIS A CE1   1 
ATOM   8025  N NE2   . HIS A  1 1099 ? -4.878  65.169  97.179  1.00 24.34 ? 1097 HIS A NE2   1 
ATOM   8026  N N     . ALA A  1 1100 ? 0.415   67.643  100.112 1.00 18.62 ? 1098 ALA A N     1 
ATOM   8027  C CA    . ALA A  1 1100 ? 1.245   68.691  100.702 1.00 23.38 ? 1098 ALA A CA    1 
ATOM   8028  C C     . ALA A  1 1100 ? 0.490   70.019  100.729 1.00 25.92 ? 1098 ALA A C     1 
ATOM   8029  O O     . ALA A  1 1100 ? -0.405  70.273  99.921  1.00 27.46 ? 1098 ALA A O     1 
ATOM   8030  C CB    . ALA A  1 1100 ? 2.563   68.842  99.931  1.00 22.48 ? 1098 ALA A CB    1 
ATOM   8031  N N     . ARG A  1 1101 ? 0.848   70.872  101.686 1.00 21.99 ? 1099 ARG A N     1 
ATOM   8032  C CA    . ARG A  1 1101 ? 0.215   72.178  101.791 1.00 25.26 ? 1099 ARG A CA    1 
ATOM   8033  C C     . ARG A  1 1101 ? 0.782   73.164  100.777 1.00 26.35 ? 1099 ARG A C     1 
ATOM   8034  O O     . ARG A  1 1101 ? 0.026   73.925  100.166 1.00 27.13 ? 1099 ARG A O     1 
ATOM   8035  C CB    . ARG A  1 1101 ? 0.386   72.732  103.205 1.00 27.03 ? 1099 ARG A CB    1 
ATOM   8036  C CG    . ARG A  1 1101 ? -0.585  72.173  104.203 1.00 27.90 ? 1099 ARG A CG    1 
ATOM   8037  C CD    . ARG A  1 1101 ? -0.435  72.835  105.553 1.00 29.90 ? 1099 ARG A CD    1 
ATOM   8038  N NE    . ARG A  1 1101 ? -1.293  73.996  105.757 1.00 33.26 ? 1099 ARG A NE    1 
ATOM   8039  C CZ    . ARG A  1 1101 ? -2.526  73.929  106.247 1.00 36.91 ? 1099 ARG A CZ    1 
ATOM   8040  N NH1   . ARG A  1 1101 ? -3.116  72.764  106.479 1.00 30.46 ? 1099 ARG A NH1   1 
ATOM   8041  N NH2   . ARG A  1 1101 ? -3.175  75.056  106.530 1.00 30.65 ? 1099 ARG A NH2   1 
ATOM   8042  N N     . GLY A  1 1102 ? 2.098   73.163  100.589 1.00 22.90 ? 1100 GLY A N     1 
ATOM   8043  C CA    . GLY A  1 1102 ? 2.760   74.095  99.692  1.00 26.85 ? 1100 GLY A CA    1 
ATOM   8044  C C     . GLY A  1 1102 ? 4.165   74.426  100.164 1.00 27.79 ? 1100 GLY A C     1 
ATOM   8045  O O     . GLY A  1 1102 ? 4.945   73.510  100.445 1.00 25.24 ? 1100 GLY A O     1 
ATOM   8046  N N     . ARG A  1 1103 ? 4.507   75.717  100.256 1.00 23.90 ? 1101 ARG A N     1 
ATOM   8047  C CA    . ARG A  1 1103 ? 5.794   76.151  100.791 1.00 24.60 ? 1101 ARG A CA    1 
ATOM   8048  C C     . ARG A  1 1103 ? 5.600   76.602  102.232 1.00 24.74 ? 1101 ARG A C     1 
ATOM   8049  O O     . ARG A  1 1103 ? 4.844   77.542  102.496 1.00 26.58 ? 1101 ARG A O     1 
ATOM   8050  C CB    . ARG A  1 1103 ? 6.411   77.281  99.961  1.00 31.00 ? 1101 ARG A CB    1 
ATOM   8051  C CG    . ARG A  1 1103 ? 7.889   77.573  100.357 1.00 26.36 ? 1101 ARG A CG    1 
ATOM   8052  C CD    . ARG A  1 1103 ? 8.612   78.505  99.365  1.00 32.10 ? 1101 ARG A CD    1 
ATOM   8053  N NE    . ARG A  1 1103 ? 8.641   77.945  98.015  1.00 37.71 ? 1101 ARG A NE    1 
ATOM   8054  C CZ    . ARG A  1 1103 ? 9.615   77.185  97.523  1.00 36.10 ? 1101 ARG A CZ    1 
ATOM   8055  N NH1   . ARG A  1 1103 ? 10.700  76.885  98.235  1.00 31.43 ? 1101 ARG A NH1   1 
ATOM   8056  N NH2   . ARG A  1 1103 ? 9.502   76.710  96.285  1.00 35.96 ? 1101 ARG A NH2   1 
ATOM   8057  N N     . ILE A  1 1104 ? 6.279   75.939  103.159 1.00 23.39 ? 1102 ILE A N     1 
ATOM   8058  C CA    . ILE A  1 1104 ? 6.173   76.281  104.576 1.00 24.15 ? 1102 ILE A CA    1 
ATOM   8059  C C     . ILE A  1 1104 ? 7.294   77.248  104.939 1.00 25.26 ? 1102 ILE A C     1 
ATOM   8060  O O     . ILE A  1 1104 ? 8.454   77.017  104.589 1.00 24.84 ? 1102 ILE A O     1 
ATOM   8061  C CB    . ILE A  1 1104 ? 6.242   75.016  105.448 1.00 23.42 ? 1102 ILE A CB    1 
ATOM   8062  C CG1   . ILE A  1 1104 ? 5.246   73.972  104.952 1.00 23.99 ? 1102 ILE A CG1   1 
ATOM   8063  C CG2   . ILE A  1 1104 ? 5.990   75.369  106.903 1.00 23.91 ? 1102 ILE A CG2   1 
ATOM   8064  C CD1   . ILE A  1 1104 ? 3.816   74.374  105.101 1.00 25.32 ? 1102 ILE A CD1   1 
ATOM   8065  N N     . LEU A  1 1105 ? 6.943   78.339  105.632 1.00 23.98 ? 1103 LEU A N     1 
ATOM   8066  C CA    . LEU A  1 1105 ? 7.924   79.287  106.147 1.00 25.94 ? 1103 LEU A CA    1 
ATOM   8067  C C     . LEU A  1 1105 ? 8.574   78.695  107.388 1.00 26.86 ? 1103 LEU A C     1 
ATOM   8068  O O     . LEU A  1 1105 ? 7.871   78.336  108.338 1.00 24.71 ? 1103 LEU A O     1 
ATOM   8069  C CB    . LEU A  1 1105 ? 7.247   80.614  106.499 1.00 24.56 ? 1103 LEU A CB    1 
ATOM   8070  C CG    . LEU A  1 1105 ? 8.144   81.639  107.203 1.00 27.26 ? 1103 LEU A CG    1 
ATOM   8071  C CD1   . LEU A  1 1105 ? 9.257   82.065  106.268 1.00 28.58 ? 1103 LEU A CD1   1 
ATOM   8072  C CD2   . LEU A  1 1105 ? 7.325   82.842  107.662 1.00 27.64 ? 1103 LEU A CD2   1 
ATOM   8073  N N     . LEU A  1 1106 ? 9.900   78.589  107.395 1.00 26.07 ? 1104 LEU A N     1 
ATOM   8074  C CA    . LEU A  1 1106 ? 10.614  78.035  108.538 1.00 22.87 ? 1104 LEU A CA    1 
ATOM   8075  C C     . LEU A  1 1106 ? 11.342  79.159  109.244 1.00 25.48 ? 1104 LEU A C     1 
ATOM   8076  O O     . LEU A  1 1106 ? 12.114  79.894  108.617 1.00 26.95 ? 1104 LEU A O     1 
ATOM   8077  C CB    . LEU A  1 1106 ? 11.615  76.953  108.130 1.00 24.77 ? 1104 LEU A CB    1 
ATOM   8078  C CG    . LEU A  1 1106 ? 11.058  75.664  107.532 1.00 29.30 ? 1104 LEU A CG    1 
ATOM   8079  C CD1   . LEU A  1 1106 ? 12.112  74.548  107.596 1.00 28.12 ? 1104 LEU A CD1   1 
ATOM   8080  C CD2   . LEU A  1 1106 ? 9.764   75.252  108.199 1.00 25.85 ? 1104 LEU A CD2   1 
ATOM   8081  N N     . VAL A  1 1107 ? 11.098  79.297  110.542 1.00 23.90 ? 1105 VAL A N     1 
ATOM   8082  C CA    . VAL A  1 1107 ? 11.783  80.336  111.299 1.00 24.83 ? 1105 VAL A CA    1 
ATOM   8083  C C     . VAL A  1 1107 ? 12.537  79.652  112.429 1.00 23.94 ? 1105 VAL A C     1 
ATOM   8084  O O     . VAL A  1 1107 ? 12.051  79.597  113.566 1.00 29.53 ? 1105 VAL A O     1 
ATOM   8085  C CB    . VAL A  1 1107 ? 10.807  81.407  111.814 1.00 23.72 ? 1105 VAL A CB    1 
ATOM   8086  C CG1   . VAL A  1 1107 ? 11.602  82.577  112.396 1.00 29.16 ? 1105 VAL A CG1   1 
ATOM   8087  C CG2   . VAL A  1 1107 ? 9.891   81.874  110.675 1.00 29.17 ? 1105 VAL A CG2   1 
ATOM   8088  N N     . PRO A  1 1108 ? 13.702  79.102  112.147 1.00 25.40 ? 1106 PRO A N     1 
ATOM   8089  C CA    . PRO A  1 1108 ? 14.454  78.362  113.162 1.00 27.74 ? 1106 PRO A CA    1 
ATOM   8090  C C     . PRO A  1 1108 ? 15.294  79.290  114.029 1.00 30.10 ? 1106 PRO A C     1 
ATOM   8091  O O     . PRO A  1 1108 ? 15.527  80.457  113.708 1.00 29.43 ? 1106 PRO A O     1 
ATOM   8092  C CB    . PRO A  1 1108 ? 15.347  77.457  112.320 1.00 31.01 ? 1106 PRO A CB    1 
ATOM   8093  C CG    . PRO A  1 1108 ? 15.666  78.336  111.111 1.00 27.83 ? 1106 PRO A CG    1 
ATOM   8094  C CD    . PRO A  1 1108 ? 14.353  79.053  110.823 1.00 27.15 ? 1106 PRO A CD    1 
ATOM   8095  N N     . ALA A  1 1109 ? 15.765  78.732  115.133 1.00 27.14 ? 1107 ALA A N     1 
ATOM   8096  C CA    . ALA A  1 1109 ? 16.723  79.397  116.008 1.00 30.41 ? 1107 ALA A CA    1 
ATOM   8097  C C     . ALA A  1 1109 ? 18.047  78.662  116.102 1.00 35.00 ? 1107 ALA A C     1 
ATOM   8098  O O     . ALA A  1 1109 ? 19.092  79.300  116.209 1.00 32.89 ? 1107 ALA A O     1 
ATOM   8099  C CB    . ALA A  1 1109 ? 16.144  79.566  117.427 1.00 31.18 ? 1107 ALA A CB    1 
ATOM   8100  N N     . THR A  1 1110 ? 18.030  77.334  116.082 1.00 31.43 ? 1108 THR A N     1 
ATOM   8101  C CA    . THR A  1 1110 ? 19.233  76.532  116.234 1.00 31.38 ? 1108 THR A CA    1 
ATOM   8102  C C     . THR A  1 1110 ? 19.330  75.577  115.053 1.00 29.99 ? 1108 THR A C     1 
ATOM   8103  O O     . THR A  1 1110 ? 18.333  75.263  114.409 1.00 30.55 ? 1108 THR A O     1 
ATOM   8104  C CB    . THR A  1 1110 ? 19.213  75.723  117.532 1.00 32.09 ? 1108 THR A CB    1 
ATOM   8105  O OG1   . THR A  1 1110 ? 18.114  74.802  117.489 1.00 28.88 ? 1108 THR A OG1   1 
ATOM   8106  C CG2   . THR A  1 1110 ? 19.054  76.639  118.744 1.00 34.17 ? 1108 THR A CG2   1 
ATOM   8107  N N     . GLU A  1 1111 ? 20.543  75.094  114.798 1.00 31.62 ? 1109 GLU A N     1 
ATOM   8108  C CA    . GLU A  1 1111 ? 20.747  74.126  113.724 1.00 34.47 ? 1109 GLU A CA    1 
ATOM   8109  C C     . GLU A  1 1111 ? 19.885  72.877  113.911 1.00 31.70 ? 1109 GLU A C     1 
ATOM   8110  O O     . GLU A  1 1111 ? 19.279  72.382  112.953 1.00 31.22 ? 1109 GLU A O     1 
ATOM   8111  C CB    . GLU A  1 1111 ? 22.222  73.752  113.659 1.00 35.79 ? 1109 GLU A CB    1 
ATOM   8112  C CG    . GLU A  1 1111 ? 22.494  72.521  112.851 1.00 36.32 ? 1109 GLU A CG    1 
ATOM   8113  C CD    . GLU A  1 1111 ? 23.971  72.319  112.627 1.00 38.41 ? 1109 GLU A CD    1 
ATOM   8114  O OE1   . GLU A  1 1111 ? 24.541  73.063  111.804 1.00 38.34 ? 1109 GLU A OE1   1 
ATOM   8115  O OE2   . GLU A  1 1111 ? 24.556  71.435  113.284 1.00 35.00 ? 1109 GLU A OE2   1 
ATOM   8116  N N     . SER A  1 1112 ? 19.819  72.350  115.135 1.00 28.89 ? 1110 SER A N     1 
ATOM   8117  C CA    . SER A  1 1112 ? 18.982  71.180  115.381 1.00 28.30 ? 1110 SER A CA    1 
ATOM   8118  C C     . SER A  1 1112 ? 17.516  71.501  115.152 1.00 29.23 ? 1110 SER A C     1 
ATOM   8119  O O     . SER A  1 1112 ? 16.780  70.692  114.578 1.00 25.45 ? 1110 SER A O     1 
ATOM   8120  C CB    . SER A  1 1112 ? 19.194  70.665  116.804 1.00 33.43 ? 1110 SER A CB    1 
ATOM   8121  O OG    . SER A  1 1112 ? 18.402  69.521  117.042 1.00 31.55 ? 1110 SER A OG    1 
ATOM   8122  N N     . GLY A  1 1113 ? 17.061  72.664  115.618 1.00 27.31 ? 1111 GLY A N     1 
ATOM   8123  C CA    . GLY A  1 1113 ? 15.688  73.055  115.346 1.00 26.65 ? 1111 GLY A CA    1 
ATOM   8124  C C     . GLY A  1 1113 ? 15.396  73.131  113.860 1.00 27.63 ? 1111 GLY A C     1 
ATOM   8125  O O     . GLY A  1 1113 ? 14.354  72.655  113.394 1.00 25.02 ? 1111 GLY A O     1 
ATOM   8126  N N     . LEU A  1 1114 ? 16.321  73.721  113.093 1.00 26.85 ? 1112 LEU A N     1 
ATOM   8127  C CA    . LEU A  1 1114 ? 16.148  73.773  111.644 1.00 25.34 ? 1112 LEU A CA    1 
ATOM   8128  C C     . LEU A  1 1114 ? 16.001  72.373  111.064 1.00 22.02 ? 1112 LEU A C     1 
ATOM   8129  O O     . LEU A  1 1114 ? 15.113  72.123  110.241 1.00 27.25 ? 1112 LEU A O     1 
ATOM   8130  C CB    . LEU A  1 1114 ? 17.328  74.499  110.997 1.00 27.82 ? 1112 LEU A CB    1 
ATOM   8131  C CG    . LEU A  1 1114 ? 17.407  74.368  109.471 1.00 27.60 ? 1112 LEU A CG    1 
ATOM   8132  C CD1   . LEU A  1 1114 ? 16.103  74.843  108.770 1.00 27.81 ? 1112 LEU A CD1   1 
ATOM   8133  C CD2   . LEU A  1 1114 ? 18.608  75.111  108.934 1.00 31.52 ? 1112 LEU A CD2   1 
ATOM   8134  N N     . TYR A  1 1115 ? 16.840  71.438  111.508 1.00 25.20 ? 1113 TYR A N     1 
ATOM   8135  C CA    . TYR A  1 1115 ? 16.763  70.075  110.987 1.00 26.38 ? 1113 TYR A CA    1 
ATOM   8136  C C     . TYR A  1 1115 ? 15.421  69.430  111.320 1.00 23.74 ? 1113 TYR A C     1 
ATOM   8137  O O     . TYR A  1 1115 ? 14.823  68.754  110.476 1.00 21.44 ? 1113 TYR A O     1 
ATOM   8138  C CB    . TYR A  1 1115 ? 17.904  69.238  111.547 1.00 23.45 ? 1113 TYR A CB    1 
ATOM   8139  C CG    . TYR A  1 1115 ? 19.292  69.645  111.090 1.00 29.08 ? 1113 TYR A CG    1 
ATOM   8140  C CD1   . TYR A  1 1115 ? 19.484  70.480  109.990 1.00 26.86 ? 1113 TYR A CD1   1 
ATOM   8141  C CD2   . TYR A  1 1115 ? 20.414  69.165  111.750 1.00 30.29 ? 1113 TYR A CD2   1 
ATOM   8142  C CE1   . TYR A  1 1115 ? 20.783  70.831  109.569 1.00 31.11 ? 1113 TYR A CE1   1 
ATOM   8143  C CE2   . TYR A  1 1115 ? 21.692  69.502  111.344 1.00 33.90 ? 1113 TYR A CE2   1 
ATOM   8144  C CZ    . TYR A  1 1115 ? 21.874  70.332  110.258 1.00 33.03 ? 1113 TYR A CZ    1 
ATOM   8145  O OH    . TYR A  1 1115 ? 23.159  70.658  109.876 1.00 36.94 ? 1113 TYR A OH    1 
ATOM   8146  N N     . HIS A  1 1116 ? 14.938  69.616  112.554 1.00 25.10 ? 1114 HIS A N     1 
ATOM   8147  C CA    . HIS A  1 1116 ? 13.636  69.074  112.929 1.00 26.85 ? 1114 HIS A CA    1 
ATOM   8148  C C     . HIS A  1 1116 ? 12.504  69.739  112.151 1.00 25.45 ? 1114 HIS A C     1 
ATOM   8149  O O     . HIS A  1 1116 ? 11.553  69.060  111.733 1.00 24.24 ? 1114 HIS A O     1 
ATOM   8150  C CB    . HIS A  1 1116 ? 13.412  69.241  114.440 1.00 28.56 ? 1114 HIS A CB    1 
ATOM   8151  C CG    . HIS A  1 1116 ? 14.091  68.198  115.271 1.00 28.76 ? 1114 HIS A CG    1 
ATOM   8152  N ND1   . HIS A  1 1116 ? 15.364  68.355  115.776 1.00 32.58 ? 1114 HIS A ND1   1 
ATOM   8153  C CD2   . HIS A  1 1116 ? 13.675  66.975  115.675 1.00 29.98 ? 1114 HIS A CD2   1 
ATOM   8154  C CE1   . HIS A  1 1116 ? 15.697  67.276  116.466 1.00 31.47 ? 1114 HIS A CE1   1 
ATOM   8155  N NE2   . HIS A  1 1116 ? 14.690  66.424  116.417 1.00 35.16 ? 1114 HIS A NE2   1 
ATOM   8156  N N     . GLN A  1 1117 ? 12.575  71.064  111.940 1.00 24.41 ? 1115 GLN A N     1 
ATOM   8157  C CA    . GLN A  1 1117 ? 11.538  71.730  111.148 1.00 22.15 ? 1115 GLN A CA    1 
ATOM   8158  C C     . GLN A  1 1117 ? 11.551  71.246  109.700 1.00 22.07 ? 1115 GLN A C     1 
ATOM   8159  O O     . GLN A  1 1117 ? 10.495  71.027  109.094 1.00 23.92 ? 1115 GLN A O     1 
ATOM   8160  C CB    . GLN A  1 1117 ? 11.705  73.253  111.179 1.00 24.01 ? 1115 GLN A CB    1 
ATOM   8161  C CG    . GLN A  1 1117 ? 11.542  73.909  112.558 1.00 23.89 ? 1115 GLN A CG    1 
ATOM   8162  C CD    . GLN A  1 1117 ? 11.766  75.409  112.512 1.00 27.02 ? 1115 GLN A CD    1 
ATOM   8163  O OE1   . GLN A  1 1117 ? 12.326  75.933  111.546 1.00 27.12 ? 1115 GLN A OE1   1 
ATOM   8164  N NE2   . GLN A  1 1117 ? 11.331  76.109  113.556 1.00 25.16 ? 1115 GLN A NE2   1 
ATOM   8165  N N     . LEU A  1 1118 ? 12.741  71.096  109.128 1.00 21.47 ? 1116 LEU A N     1 
ATOM   8166  C CA    . LEU A  1 1118 ? 12.843  70.639  107.748 1.00 22.41 ? 1116 LEU A CA    1 
ATOM   8167  C C     . LEU A  1 1118 ? 12.302  69.222  107.610 1.00 22.10 ? 1116 LEU A C     1 
ATOM   8168  O O     . LEU A  1 1118 ? 11.585  68.912  106.649 1.00 21.92 ? 1116 LEU A O     1 
ATOM   8169  C CB    . LEU A  1 1118 ? 14.304  70.735  107.297 1.00 23.72 ? 1116 LEU A CB    1 
ATOM   8170  C CG    . LEU A  1 1118 ? 14.696  70.618  105.826 1.00 27.57 ? 1116 LEU A CG    1 
ATOM   8171  C CD1   . LEU A  1 1118 ? 13.711  71.343  104.917 1.00 27.95 ? 1116 LEU A CD1   1 
ATOM   8172  C CD2   . LEU A  1 1118 ? 16.103  71.185  105.662 1.00 34.25 ? 1116 LEU A CD2   1 
ATOM   8173  N N     . ALA A  1 1119 ? 12.599  68.352  108.578 1.00 21.35 ? 1117 ALA A N     1 
ATOM   8174  C CA    . ALA A  1 1119 ? 12.066  66.993  108.506 1.00 23.49 ? 1117 ALA A CA    1 
ATOM   8175  C C     . ALA A  1 1119 ? 10.538  66.996  108.533 1.00 22.16 ? 1117 ALA A C     1 
ATOM   8176  O O     . ALA A  1 1119 ? 9.898   66.343  107.703 1.00 22.51 ? 1117 ALA A O     1 
ATOM   8177  C CB    . ALA A  1 1119 ? 12.634  66.136  109.637 1.00 22.15 ? 1117 ALA A CB    1 
ATOM   8178  N N     . ALA A  1 1120 ? 9.933   67.732  109.478 1.00 20.68 ? 1118 ALA A N     1 
ATOM   8179  C CA    . ALA A  1 1120 ? 8.470   67.802  109.534 1.00 22.41 ? 1118 ALA A CA    1 
ATOM   8180  C C     . ALA A  1 1120 ? 7.889   68.272  108.202 1.00 21.30 ? 1118 ALA A C     1 
ATOM   8181  O O     . ALA A  1 1120 ? 6.925   67.697  107.681 1.00 21.60 ? 1118 ALA A O     1 
ATOM   8182  C CB    . ALA A  1 1120 ? 8.036   68.746  110.658 1.00 25.55 ? 1118 ALA A CB    1 
ATOM   8183  N N     . ALA A  1 1121 ? 8.480   69.316  107.629 1.00 22.76 ? 1119 ALA A N     1 
ATOM   8184  C CA    . ALA A  1 1121 ? 7.948   69.875  106.393 1.00 22.63 ? 1119 ALA A CA    1 
ATOM   8185  C C     . ALA A  1 1121 ? 8.150   68.926  105.214 1.00 22.73 ? 1119 ALA A C     1 
ATOM   8186  O O     . ALA A  1 1121 ? 7.237   68.743  104.388 1.00 20.81 ? 1119 ALA A O     1 
ATOM   8187  C CB    . ALA A  1 1121 ? 8.602   71.232  106.124 1.00 23.90 ? 1119 ALA A CB    1 
ATOM   8188  N N     . LEU A  1 1122 ? 9.337   68.327  105.099 1.00 22.30 ? 1120 LEU A N     1 
ATOM   8189  C CA    . LEU A  1 1122 ? 9.589   67.430  103.971 1.00 20.10 ? 1120 LEU A CA    1 
ATOM   8190  C C     . LEU A  1 1122 ? 8.762   66.147  104.082 1.00 20.52 ? 1120 LEU A C     1 
ATOM   8191  O O     . LEU A  1 1122 ? 8.252   65.635  103.078 1.00 22.75 ? 1120 LEU A O     1 
ATOM   8192  C CB    . LEU A  1 1122 ? 11.082  67.095  103.894 1.00 23.21 ? 1120 LEU A CB    1 
ATOM   8193  C CG    . LEU A  1 1122 ? 12.034  68.245  103.578 1.00 21.94 ? 1120 LEU A CG    1 
ATOM   8194  C CD1   . LEU A  1 1122 ? 13.477  67.755  103.583 1.00 25.93 ? 1120 LEU A CD1   1 
ATOM   8195  C CD2   . LEU A  1 1122 ? 11.656  68.853  102.221 1.00 22.26 ? 1120 LEU A CD2   1 
ATOM   8196  N N     . ALA A  1 1123 ? 8.617   65.616  105.300 1.00 23.05 ? 1121 ALA A N     1 
ATOM   8197  C CA    . ALA A  1 1123 ? 7.845   64.393  105.502 1.00 21.85 ? 1121 ALA A CA    1 
ATOM   8198  C C     . ALA A  1 1123 ? 6.397   64.556  105.073 1.00 24.26 ? 1121 ALA A C     1 
ATOM   8199  O O     . ALA A  1 1123 ? 5.740   63.553  104.765 1.00 23.79 ? 1121 ALA A O     1 
ATOM   8200  C CB    . ALA A  1 1123 ? 7.894   63.963  106.975 1.00 21.37 ? 1121 ALA A CB    1 
ATOM   8201  N N     . THR A  1 1124 ? 5.888   65.789  105.066 1.00 21.59 ? 1122 THR A N     1 
ATOM   8202  C CA    . THR A  1 1124 ? 4.522   66.081  104.665 1.00 20.42 ? 1122 THR A CA    1 
ATOM   8203  C C     . THR A  1 1124 ? 4.451   66.628  103.238 1.00 21.93 ? 1122 THR A C     1 
ATOM   8204  O O     . THR A  1 1124 ? 3.399   67.140  102.826 1.00 21.85 ? 1122 THR A O     1 
ATOM   8205  C CB    . THR A  1 1124 ? 3.875   67.055  105.666 1.00 22.69 ? 1122 THR A CB    1 
ATOM   8206  O OG1   . THR A  1 1124 ? 4.807   68.101  106.014 1.00 22.70 ? 1122 THR A OG1   1 
ATOM   8207  C CG2   . THR A  1 1124 ? 3.480   66.302  106.934 1.00 23.59 ? 1122 THR A CG2   1 
ATOM   8208  N N     . GLY A  1 1125 ? 5.542   66.519  102.473 1.00 21.19 ? 1123 GLY A N     1 
ATOM   8209  C CA    . GLY A  1 1125 ? 5.511   66.795  101.040 1.00 21.69 ? 1123 GLY A CA    1 
ATOM   8210  C C     . GLY A  1 1125 ? 5.787   68.229  100.646 1.00 24.33 ? 1123 GLY A C     1 
ATOM   8211  O O     . GLY A  1 1125 ? 5.701   68.562  99.453  1.00 21.64 ? 1123 GLY A O     1 
ATOM   8212  N N     . ASN A  1 1126 ? 6.137   69.085  101.599 1.00 20.86 ? 1124 ASN A N     1 
ATOM   8213  C CA    . ASN A  1 1126 ? 6.227   70.516  101.365 1.00 21.89 ? 1124 ASN A CA    1 
ATOM   8214  C C     . ASN A  1 1126 ? 7.628   70.934  100.928 1.00 24.09 ? 1124 ASN A C     1 
ATOM   8215  O O     . ASN A  1 1126 ? 8.623   70.242  101.158 1.00 24.13 ? 1124 ASN A O     1 
ATOM   8216  C CB    . ASN A  1 1126 ? 5.855   71.295  102.631 1.00 20.87 ? 1124 ASN A CB    1 
ATOM   8217  C CG    . ASN A  1 1126 ? 4.460   70.988  103.110 1.00 24.55 ? 1124 ASN A CG    1 
ATOM   8218  O OD1   . ASN A  1 1126 ? 3.475   71.402  102.488 1.00 22.21 ? 1124 ASN A OD1   1 
ATOM   8219  N ND2   . ASN A  1 1126 ? 4.359   70.271  104.231 1.00 20.08 ? 1124 ASN A ND2   1 
ATOM   8220  N N     . SER A  1 1127 ? 7.677   72.089  100.278 1.00 26.57 ? 1125 SER A N     1 
ATOM   8221  C CA    . SER A  1 1127 ? 8.899   72.858  100.133 1.00 26.47 ? 1125 SER A CA    1 
ATOM   8222  C C     . SER A  1 1127 ? 8.993   73.817  101.308 1.00 26.04 ? 1125 SER A C     1 
ATOM   8223  O O     . SER A  1 1127 ? 8.044   73.971  102.086 1.00 25.22 ? 1125 SER A O     1 
ATOM   8224  C CB    . SER A  1 1127 ? 8.902   73.609  98.804  1.00 28.10 ? 1125 SER A CB    1 
ATOM   8225  O OG    . SER A  1 1127 ? 7.852   74.556  98.770  1.00 28.15 ? 1125 SER A OG    1 
ATOM   8226  N N     . VAL A  1 1128 ? 10.149  74.463  101.460 1.00 23.59 ? 1126 VAL A N     1 
ATOM   8227  C CA    . VAL A  1 1128 ? 10.330  75.351  102.599 1.00 23.67 ? 1126 VAL A CA    1 
ATOM   8228  C C     . VAL A  1 1128 ? 10.967  76.653  102.146 1.00 29.21 ? 1126 VAL A C     1 
ATOM   8229  O O     . VAL A  1 1128 ? 11.694  76.708  101.148 1.00 27.47 ? 1126 VAL A O     1 
ATOM   8230  C CB    . VAL A  1 1128 ? 11.181  74.711  103.719 1.00 26.53 ? 1126 VAL A CB    1 
ATOM   8231  C CG1   . VAL A  1 1128 ? 10.539  73.434  104.189 1.00 24.01 ? 1126 VAL A CG1   1 
ATOM   8232  C CG2   . VAL A  1 1128 ? 12.592  74.427  103.230 1.00 25.59 ? 1126 VAL A CG2   1 
ATOM   8233  N N     . ALA A  1 1129 ? 10.677  77.706  102.898 1.00 24.56 ? 1127 ALA A N     1 
ATOM   8234  C CA    . ALA A  1 1129 ? 11.417  78.961  102.842 1.00 29.78 ? 1127 ALA A CA    1 
ATOM   8235  C C     . ALA A  1 1129 ? 11.967  79.208  104.237 1.00 27.70 ? 1127 ALA A C     1 
ATOM   8236  O O     . ALA A  1 1129 ? 11.194  79.360  105.186 1.00 27.63 ? 1127 ALA A O     1 
ATOM   8237  C CB    . ALA A  1 1129 ? 10.520  80.114  102.391 1.00 28.15 ? 1127 ALA A CB    1 
ATOM   8238  N N     . ILE A  1 1130 ? 13.294  79.207  104.367 1.00 28.90 ? 1128 ILE A N     1 
ATOM   8239  C CA    . ILE A  1 1130 ? 13.958  79.310  105.662 1.00 30.64 ? 1128 ILE A CA    1 
ATOM   8240  C C     . ILE A  1 1130 ? 14.366  80.756  105.886 1.00 30.71 ? 1128 ILE A C     1 
ATOM   8241  O O     . ILE A  1 1130 ? 14.928  81.394  104.990 1.00 29.63 ? 1128 ILE A O     1 
ATOM   8242  C CB    . ILE A  1 1130 ? 15.188  78.392  105.742 1.00 29.16 ? 1128 ILE A CB    1 
ATOM   8243  C CG1   . ILE A  1 1130 ? 14.843  76.974  105.296 1.00 29.70 ? 1128 ILE A CG1   1 
ATOM   8244  C CG2   . ILE A  1 1130 ? 15.753  78.404  107.147 1.00 26.64 ? 1128 ILE A CG2   1 
ATOM   8245  C CD1   . ILE A  1 1130 ? 16.064  76.105  105.141 1.00 28.90 ? 1128 ILE A CD1   1 
ATOM   8246  N N     . ASP A  1 1131 ? 14.091  81.270  107.079 1.00 28.52 ? 1129 ASP A N     1 
ATOM   8247  C CA    . ASP A  1 1131 ? 14.445  82.645  107.396 1.00 33.52 ? 1129 ASP A CA    1 
ATOM   8248  C C     . ASP A  1 1131 ? 15.954  82.846  107.295 1.00 33.00 ? 1129 ASP A C     1 
ATOM   8249  O O     . ASP A  1 1131 ? 16.726  82.225  108.029 1.00 31.14 ? 1129 ASP A O     1 
ATOM   8250  C CB    . ASP A  1 1131 ? 13.942  82.984  108.796 1.00 29.80 ? 1129 ASP A CB    1 
ATOM   8251  C CG    . ASP A  1 1131 ? 14.318  84.381  109.224 1.00 34.46 ? 1129 ASP A CG    1 
ATOM   8252  O OD1   . ASP A  1 1131 ? 14.567  85.244  108.361 1.00 34.51 ? 1129 ASP A OD1   1 
ATOM   8253  O OD2   . ASP A  1 1131 ? 14.363  84.609  110.438 1.00 36.19 ? 1129 ASP A OD2   1 
ATOM   8254  N N     . ALA A  1 1132 ? 16.382  83.699  106.362 1.00 37.13 ? 1130 ALA A N     1 
ATOM   8255  C CA    . ALA A  1 1132 ? 17.811  83.967  106.238 1.00 35.29 ? 1130 ALA A CA    1 
ATOM   8256  C C     . ALA A  1 1132 ? 18.346  84.733  107.440 1.00 37.68 ? 1130 ALA A C     1 
ATOM   8257  O O     . ALA A  1 1132 ? 19.547  84.666  107.719 1.00 41.51 ? 1130 ALA A O     1 
ATOM   8258  C CB    . ALA A  1 1132 ? 18.100  84.730  104.946 1.00 36.80 ? 1130 ALA A CB    1 
ATOM   8259  N N     . ALA A  1 1133 ? 17.483  85.438  108.173 1.00 35.89 ? 1131 ALA A N     1 
ATOM   8260  C CA    . ALA A  1 1133 ? 17.938  86.157  109.353 1.00 42.35 ? 1131 ALA A CA    1 
ATOM   8261  C C     . ALA A  1 1133 ? 18.324  85.231  110.497 1.00 38.70 ? 1131 ALA A C     1 
ATOM   8262  O O     . ALA A  1 1133 ? 18.802  85.718  111.521 1.00 41.31 ? 1131 ALA A O     1 
ATOM   8263  C CB    . ALA A  1 1133 ? 16.861  87.144  109.817 1.00 38.14 ? 1131 ALA A CB    1 
ATOM   8264  N N     . SER A  1 1134 ? 18.132  83.920  110.351 1.00 39.05 ? 1132 SER A N     1 
ATOM   8265  C CA    . SER A  1 1134 ? 18.530  82.971  111.385 1.00 36.70 ? 1132 SER A CA    1 
ATOM   8266  C C     . SER A  1 1134 ? 20.039  82.775  111.454 1.00 38.30 ? 1132 SER A C     1 
ATOM   8267  O O     . SER A  1 1134 ? 20.540  82.281  112.470 1.00 34.95 ? 1132 SER A O     1 
ATOM   8268  C CB    . SER A  1 1134 ? 17.870  81.614  111.131 1.00 37.19 ? 1132 SER A CB    1 
ATOM   8269  O OG    . SER A  1 1134 ? 18.357  81.053  109.920 1.00 35.54 ? 1132 SER A OG    1 
ATOM   8270  N N     . GLY A  1 1135 ? 20.765  83.120  110.392 1.00 38.98 ? 1133 GLY A N     1 
ATOM   8271  C CA    . GLY A  1 1135 ? 22.191  82.859  110.343 1.00 40.84 ? 1133 GLY A CA    1 
ATOM   8272  C C     . GLY A  1 1135 ? 22.578  81.398  110.259 1.00 41.08 ? 1133 GLY A C     1 
ATOM   8273  O O     . GLY A  1 1135 ? 23.728  81.057  110.552 1.00 35.93 ? 1133 GLY A O     1 
ATOM   8274  N N     . LEU A  1 1136 ? 21.654  80.514  109.874 1.00 33.90 ? 1134 LEU A N     1 
ATOM   8275  C CA    . LEU A  1 1136 ? 21.921  79.078  109.866 1.00 38.90 ? 1134 LEU A CA    1 
ATOM   8276  C C     . LEU A  1 1136 ? 22.254  78.534  108.473 1.00 37.78 ? 1134 LEU A C     1 
ATOM   8277  O O     . LEU A  1 1136 ? 22.170  77.320  108.259 1.00 38.08 ? 1134 LEU A O     1 
ATOM   8278  C CB    . LEU A  1 1136 ? 20.729  78.314  110.454 1.00 35.40 ? 1134 LEU A CB    1 
ATOM   8279  C CG    . LEU A  1 1136 ? 20.433  78.497  111.947 1.00 35.10 ? 1134 LEU A CG    1 
ATOM   8280  C CD1   . LEU A  1 1136 ? 19.132  77.803  112.341 1.00 32.07 ? 1134 LEU A CD1   1 
ATOM   8281  C CD2   . LEU A  1 1136 ? 21.591  77.977  112.793 1.00 37.68 ? 1134 LEU A CD2   1 
ATOM   8282  N N     . GLN A  1 1137 ? 22.645  79.400  107.531 1.00 37.90 ? 1135 GLN A N     1 
ATOM   8283  C CA    . GLN A  1 1137 ? 22.911  78.952  106.162 1.00 37.39 ? 1135 GLN A CA    1 
ATOM   8284  C C     . GLN A  1 1137 ? 24.012  77.894  106.105 1.00 39.04 ? 1135 GLN A C     1 
ATOM   8285  O O     . GLN A  1 1137 ? 23.921  76.931  105.329 1.00 38.04 ? 1135 GLN A O     1 
ATOM   8286  C CB    . GLN A  1 1137 ? 23.272  80.148  105.279 1.00 39.44 ? 1135 GLN A CB    1 
ATOM   8287  C CG    . GLN A  1 1137 ? 22.086  81.065  104.953 1.00 37.80 ? 1135 GLN A CG    1 
ATOM   8288  C CD    . GLN A  1 1137 ? 21.914  82.181  105.958 1.00 36.81 ? 1135 GLN A CD    1 
ATOM   8289  O OE1   . GLN A  1 1137 ? 22.382  82.099  107.099 1.00 39.79 ? 1135 GLN A OE1   1 
ATOM   8290  N NE2   . GLN A  1 1137 ? 21.264  83.249  105.532 1.00 45.01 ? 1135 GLN A NE2   1 
ATOM   8291  N N     . ALA A  1 1138 ? 25.053  78.035  106.928 1.00 39.68 ? 1136 ALA A N     1 
ATOM   8292  C CA    . ALA A  1 1138 ? 26.116  77.039  106.902 1.00 34.71 ? 1136 ALA A CA    1 
ATOM   8293  C C     . ALA A  1 1138 ? 25.681  75.686  107.455 1.00 41.72 ? 1136 ALA A C     1 
ATOM   8294  O O     . ALA A  1 1138 ? 26.463  74.731  107.392 1.00 39.55 ? 1136 ALA A O     1 
ATOM   8295  C CB    . ALA A  1 1138 ? 27.342  77.546  107.676 1.00 38.95 ? 1136 ALA A CB    1 
ATOM   8296  N N     . SER A  1 1139 ? 24.466  75.571  107.990 1.00 40.55 ? 1137 SER A N     1 
ATOM   8297  C CA    . SER A  1 1139 ? 24.006  74.292  108.511 1.00 39.96 ? 1137 SER A CA    1 
ATOM   8298  C C     . SER A  1 1139 ? 23.479  73.364  107.426 1.00 32.79 ? 1137 SER A C     1 
ATOM   8299  O O     . SER A  1 1139 ? 23.194  72.201  107.720 1.00 34.80 ? 1137 SER A O     1 
ATOM   8300  C CB    . SER A  1 1139 ? 22.923  74.516  109.572 1.00 36.54 ? 1137 SER A CB    1 
ATOM   8301  O OG    . SER A  1 1139 ? 23.503  74.991  110.773 1.00 38.74 ? 1137 SER A OG    1 
ATOM   8302  N N     . LEU A  1 1140 ? 23.361  73.833  106.190 1.00 33.69 ? 1138 LEU A N     1 
ATOM   8303  C CA    . LEU A  1 1140 ? 22.758  73.063  105.108 1.00 36.44 ? 1138 LEU A CA    1 
ATOM   8304  C C     . LEU A  1 1140 ? 23.688  72.976  103.915 1.00 39.50 ? 1138 LEU A C     1 
ATOM   8305  O O     . LEU A  1 1140 ? 23.261  73.114  102.765 1.00 39.96 ? 1138 LEU A O     1 
ATOM   8306  C CB    . LEU A  1 1140 ? 21.425  73.671  104.674 1.00 36.30 ? 1138 LEU A CB    1 
ATOM   8307  C CG    . LEU A  1 1140 ? 20.229  73.519  105.605 1.00 31.02 ? 1138 LEU A CG    1 
ATOM   8308  C CD1   . LEU A  1 1140 ? 19.015  74.130  104.930 1.00 35.97 ? 1138 LEU A CD1   1 
ATOM   8309  C CD2   . LEU A  1 1140 ? 19.978  72.059  105.929 1.00 28.77 ? 1138 LEU A CD2   1 
ATOM   8310  N N     . LYS A  1 1141 ? 24.972  72.743  104.163 1.00 40.38 ? 1139 LYS A N     1 
ATOM   8311  C CA    . LYS A  1 1141 ? 25.939  72.631  103.082 1.00 42.69 ? 1139 LYS A CA    1 
ATOM   8312  C C     . LYS A  1 1141 ? 25.835  71.268  102.408 1.00 41.34 ? 1139 LYS A C     1 
ATOM   8313  O O     . LYS A  1 1141 ? 25.643  70.246  103.069 1.00 40.17 ? 1139 LYS A O     1 
ATOM   8314  C CB    . LYS A  1 1141 ? 27.359  72.848  103.616 1.00 44.67 ? 1139 LYS A CB    1 
ATOM   8315  N N     . ASN A  1 1142 ? 25.979  71.259  101.085 1.00 37.90 ? 1140 ASN A N     1 
ATOM   8316  C CA    . ASN A  1 1142 ? 26.025  70.016  100.317 1.00 40.43 ? 1140 ASN A CA    1 
ATOM   8317  C C     . ASN A  1 1142 ? 24.729  69.223  100.444 1.00 37.95 ? 1140 ASN A C     1 
ATOM   8318  O O     . ASN A  1 1142 ? 24.751  67.995  100.541 1.00 37.72 ? 1140 ASN A O     1 
ATOM   8319  C CB    . ASN A  1 1142 ? 27.210  69.144  100.730 1.00 46.30 ? 1140 ASN A CB    1 
ATOM   8320  C CG    . ASN A  1 1142 ? 28.526  69.865  100.612 1.00 50.32 ? 1140 ASN A CG    1 
ATOM   8321  O OD1   . ASN A  1 1142 ? 29.284  69.957  101.578 1.00 52.03 ? 1140 ASN A OD1   1 
ATOM   8322  N ND2   . ASN A  1 1142 ? 28.805  70.391  99.422  1.00 49.43 ? 1140 ASN A ND2   1 
ATOM   8323  N N     . LEU A  1 1143 ? 23.598  69.921  100.451 1.00 38.71 ? 1141 LEU A N     1 
ATOM   8324  C CA    . LEU A  1 1143 ? 22.321  69.225  100.399 1.00 39.03 ? 1141 LEU A CA    1 
ATOM   8325  C C     . LEU A  1 1143 ? 22.198  68.453  99.091  1.00 39.40 ? 1141 LEU A C     1 
ATOM   8326  O O     . LEU A  1 1143 ? 22.593  68.957  98.032  1.00 41.08 ? 1141 LEU A O     1 
ATOM   8327  C CB    . LEU A  1 1143 ? 21.147  70.196  100.513 1.00 36.93 ? 1141 LEU A CB    1 
ATOM   8328  C CG    . LEU A  1 1143 ? 20.630  70.564  101.902 1.00 38.28 ? 1141 LEU A CG    1 
ATOM   8329  C CD1   . LEU A  1 1143 ? 19.518  71.576  101.732 1.00 38.82 ? 1141 LEU A CD1   1 
ATOM   8330  C CD2   . LEU A  1 1143 ? 20.131  69.338  102.673 1.00 31.73 ? 1141 LEU A CD2   1 
ATOM   8331  N N     . PRO A  1 1144 ? 21.634  67.246  99.119  1.00 38.26 ? 1142 PRO A N     1 
ATOM   8332  C CA    . PRO A  1 1144 ? 21.306  66.561  97.864  1.00 35.70 ? 1142 PRO A CA    1 
ATOM   8333  C C     . PRO A  1 1144 ? 20.416  67.435  96.997  1.00 35.77 ? 1142 PRO A C     1 
ATOM   8334  O O     . PRO A  1 1144 ? 19.623  68.240  97.494  1.00 33.87 ? 1142 PRO A O     1 
ATOM   8335  C CB    . PRO A  1 1144 ? 20.569  65.297  98.327  1.00 36.20 ? 1142 PRO A CB    1 
ATOM   8336  C CG    . PRO A  1 1144 ? 20.958  65.118  99.760  1.00 35.08 ? 1142 PRO A CG    1 
ATOM   8337  C CD    . PRO A  1 1144 ? 21.197  66.492  100.305 1.00 37.05 ? 1142 PRO A CD    1 
ATOM   8338  N N     . GLN A  1 1145 ? 20.557  67.274  95.679  1.00 32.51 ? 1143 GLN A N     1 
ATOM   8339  C CA    . GLN A  1 1145 ? 19.803  68.118  94.761  1.00 33.23 ? 1143 GLN A CA    1 
ATOM   8340  C C     . GLN A  1 1145 ? 18.302  67.974  94.984  1.00 33.99 ? 1143 GLN A C     1 
ATOM   8341  O O     . GLN A  1 1145 ? 17.560  68.959  94.895  1.00 33.59 ? 1143 GLN A O     1 
ATOM   8342  C CB    . GLN A  1 1145 ? 20.173  67.784  93.314  1.00 38.80 ? 1143 GLN A CB    1 
ATOM   8343  N N     . THR A  1 1146 ? 17.830  66.754  95.270  1.00 32.22 ? 1144 THR A N     1 
ATOM   8344  C CA    . THR A  1 1146 ? 16.396  66.560  95.492  1.00 35.21 ? 1144 THR A CA    1 
ATOM   8345  C C     . THR A  1 1146 ? 15.899  67.417  96.645  1.00 32.07 ? 1144 THR A C     1 
ATOM   8346  O O     . THR A  1 1146 ? 14.788  67.964  96.596  1.00 30.40 ? 1144 THR A O     1 
ATOM   8347  C CB    . THR A  1 1146 ? 16.089  65.094  95.779  1.00 32.21 ? 1144 THR A CB    1 
ATOM   8348  O OG1   . THR A  1 1146 ? 17.073  64.586  96.689  1.00 34.38 ? 1144 THR A OG1   1 
ATOM   8349  C CG2   . THR A  1 1146 ? 16.107  64.281  94.501  1.00 33.07 ? 1144 THR A CG2   1 
ATOM   8350  N N     . VAL A  1 1147 ? 16.707  67.535  97.696  1.00 30.84 ? 1145 VAL A N     1 
ATOM   8351  C CA    . VAL A  1 1147 ? 16.324  68.356  98.834  1.00 26.98 ? 1145 VAL A CA    1 
ATOM   8352  C C     . VAL A  1 1147 ? 16.541  69.831  98.521  1.00 30.61 ? 1145 VAL A C     1 
ATOM   8353  O O     . VAL A  1 1147 ? 15.691  70.668  98.834  1.00 31.85 ? 1145 VAL A O     1 
ATOM   8354  C CB    . VAL A  1 1147 ? 17.095  67.906  100.092 1.00 29.12 ? 1145 VAL A CB    1 
ATOM   8355  C CG1   . VAL A  1 1147 ? 16.655  68.710  101.309 1.00 26.74 ? 1145 VAL A CG1   1 
ATOM   8356  C CG2   . VAL A  1 1147 ? 16.908  66.406  100.328 1.00 25.50 ? 1145 VAL A CG2   1 
ATOM   8357  N N     . GLY A  1 1148 ? 17.673  70.170  97.885  1.00 32.42 ? 1146 GLY A N     1 
ATOM   8358  C CA    . GLY A  1 1148 ? 17.892  71.544  97.459  1.00 30.26 ? 1146 GLY A CA    1 
ATOM   8359  C C     . GLY A  1 1148 ? 16.754  72.101  96.626  1.00 33.21 ? 1146 GLY A C     1 
ATOM   8360  O O     . GLY A  1 1148 ? 16.417  73.285  96.735  1.00 32.84 ? 1146 GLY A O     1 
ATOM   8361  N N     . LEU A  1 1149 ? 16.135  71.256  95.788  1.00 29.85 ? 1147 LEU A N     1 
ATOM   8362  C CA    . LEU A  1 1149 ? 15.010  71.714  94.976  1.00 32.26 ? 1147 LEU A CA    1 
ATOM   8363  C C     . LEU A  1 1149 ? 13.857  72.215  95.833  1.00 33.68 ? 1147 LEU A C     1 
ATOM   8364  O O     . LEU A  1 1149 ? 13.085  73.067  95.391  1.00 32.58 ? 1147 LEU A O     1 
ATOM   8365  C CB    . LEU A  1 1149 ? 14.498  70.597  94.069  1.00 36.90 ? 1147 LEU A CB    1 
ATOM   8366  C CG    . LEU A  1 1149 ? 15.389  70.166  92.904  1.00 37.54 ? 1147 LEU A CG    1 
ATOM   8367  C CD1   . LEU A  1 1149 ? 14.609  69.221  92.011  1.00 40.09 ? 1147 LEU A CD1   1 
ATOM   8368  C CD2   . LEU A  1 1149 ? 15.890  71.373  92.131  1.00 39.90 ? 1147 LEU A CD2   1 
ATOM   8369  N N     . ARG A  1 1150 ? 13.723  71.703  97.053  1.00 30.39 ? 1148 ARG A N     1 
ATOM   8370  C CA    . ARG A  1 1150 ? 12.617  72.074  97.917  1.00 27.22 ? 1148 ARG A CA    1 
ATOM   8371  C C     . ARG A  1 1150 ? 12.962  73.185  98.900  1.00 29.09 ? 1148 ARG A C     1 
ATOM   8372  O O     . ARG A  1 1150 ? 12.070  73.637  99.625  1.00 28.25 ? 1148 ARG A O     1 
ATOM   8373  C CB    . ARG A  1 1150 ? 12.137  70.849  98.689  1.00 28.60 ? 1148 ARG A CB    1 
ATOM   8374  C CG    . ARG A  1 1150 ? 11.354  69.857  97.863  1.00 30.28 ? 1148 ARG A CG    1 
ATOM   8375  C CD    . ARG A  1 1150 ? 10.236  69.295  98.699  1.00 29.16 ? 1148 ARG A CD    1 
ATOM   8376  N NE    . ARG A  1 1150 ? 9.670   68.081  98.129  1.00 27.86 ? 1148 ARG A NE    1 
ATOM   8377  C CZ    . ARG A  1 1150 ? 9.103   67.124  98.852  1.00 30.28 ? 1148 ARG A CZ    1 
ATOM   8378  N NH1   . ARG A  1 1150 ? 9.022   67.215  100.173 1.00 23.32 ? 1148 ARG A NH1   1 
ATOM   8379  N NH2   . ARG A  1 1150 ? 8.616   66.046  98.236  1.00 26.49 ? 1148 ARG A NH2   1 
ATOM   8380  N N     . VAL A  1 1151 ? 14.215  73.637  98.941  1.00 27.29 ? 1149 VAL A N     1 
ATOM   8381  C CA    . VAL A  1 1151 ? 14.689  74.573  99.959  1.00 27.02 ? 1149 VAL A CA    1 
ATOM   8382  C C     . VAL A  1 1151 ? 14.971  75.916  99.305  1.00 33.67 ? 1149 VAL A C     1 
ATOM   8383  O O     . VAL A  1 1151 ? 15.645  75.986  98.269  1.00 35.69 ? 1149 VAL A O     1 
ATOM   8384  C CB    . VAL A  1 1151 ? 15.937  74.027  100.676 1.00 31.56 ? 1149 VAL A CB    1 
ATOM   8385  C CG1   . VAL A  1 1151 ? 16.575  75.105  101.541 1.00 34.64 ? 1149 VAL A CG1   1 
ATOM   8386  C CG2   . VAL A  1 1151 ? 15.568  72.830  101.514 1.00 28.44 ? 1149 VAL A CG2   1 
ATOM   8387  N N     . SER A  1 1152 ? 14.435  76.978  99.888  1.00 30.00 ? 1150 SER A N     1 
ATOM   8388  C CA    . SER A  1 1152 ? 14.830  78.327  99.526  1.00 31.49 ? 1150 SER A CA    1 
ATOM   8389  C C     . SER A  1 1152 ? 15.109  79.092  100.802 1.00 31.87 ? 1150 SER A C     1 
ATOM   8390  O O     . SER A  1 1152 ? 14.653  78.712  101.884 1.00 30.22 ? 1150 SER A O     1 
ATOM   8391  C CB    . SER A  1 1152 ? 13.762  79.051  98.698  1.00 32.32 ? 1150 SER A CB    1 
ATOM   8392  O OG    . SER A  1 1152 ? 12.539  79.157  99.408  1.00 38.21 ? 1150 SER A OG    1 
ATOM   8393  N N     . TRP A  1 1153 ? 15.886  80.161  100.668 1.00 32.43 ? 1151 TRP A N     1 
ATOM   8394  C CA    . TRP A  1 1153 ? 16.132  81.082  101.765 1.00 32.99 ? 1151 TRP A CA    1 
ATOM   8395  C C     . TRP A  1 1153 ? 15.429  82.401  101.488 1.00 35.61 ? 1151 TRP A C     1 
ATOM   8396  O O     . TRP A  1 1153 ? 15.308  82.830  100.337 1.00 39.81 ? 1151 TRP A O     1 
ATOM   8397  C CB    . TRP A  1 1153 ? 17.624  81.300  101.965 1.00 31.92 ? 1151 TRP A CB    1 
ATOM   8398  C CG    . TRP A  1 1153 ? 18.301  80.080  102.486 1.00 32.40 ? 1151 TRP A CG    1 
ATOM   8399  C CD1   . TRP A  1 1153 ? 18.763  79.024  101.756 1.00 31.44 ? 1151 TRP A CD1   1 
ATOM   8400  C CD2   . TRP A  1 1153 ? 18.582  79.777  103.857 1.00 32.38 ? 1151 TRP A CD2   1 
ATOM   8401  N NE1   . TRP A  1 1153 ? 19.316  78.083  102.589 1.00 33.95 ? 1151 TRP A NE1   1 
ATOM   8402  C CE2   . TRP A  1 1153 ? 19.229  78.525  103.883 1.00 31.83 ? 1151 TRP A CE2   1 
ATOM   8403  C CE3   . TRP A  1 1153 ? 18.352  80.440  105.061 1.00 32.56 ? 1151 TRP A CE3   1 
ATOM   8404  C CZ2   . TRP A  1 1153 ? 19.643  77.922  105.065 1.00 34.43 ? 1151 TRP A CZ2   1 
ATOM   8405  C CZ3   . TRP A  1 1153 ? 18.789  79.844  106.243 1.00 35.26 ? 1151 TRP A CZ3   1 
ATOM   8406  C CH2   . TRP A  1 1153 ? 19.424  78.604  106.234 1.00 32.06 ? 1151 TRP A CH2   1 
ATOM   8407  N N     . SER A  1 1154 ? 14.954  83.039  102.552 1.00 33.20 ? 1152 SER A N     1 
ATOM   8408  C CA    . SER A  1 1154 ? 14.118  84.226  102.429 1.00 35.43 ? 1152 SER A CA    1 
ATOM   8409  C C     . SER A  1 1154 ? 14.600  85.283  103.409 1.00 39.45 ? 1152 SER A C     1 
ATOM   8410  O O     . SER A  1 1154 ? 14.659  85.033  104.618 1.00 36.19 ? 1152 SER A O     1 
ATOM   8411  C CB    . SER A  1 1154 ? 12.645  83.889  102.684 1.00 35.61 ? 1152 SER A CB    1 
ATOM   8412  O OG    . SER A  1 1154 ? 11.817  85.024  102.481 1.00 36.51 ? 1152 SER A OG    1 
ATOM   8413  N N     . LYS A  1 1155 ? 14.961  86.454  102.886 1.00 40.61 ? 1153 LYS A N     1 
ATOM   8414  C CA    . LYS A  1 1155 ? 15.190  87.614  103.738 1.00 41.82 ? 1153 LYS A CA    1 
ATOM   8415  C C     . LYS A  1 1155 ? 13.917  88.431  103.906 1.00 43.26 ? 1153 LYS A C     1 
ATOM   8416  O O     . LYS A  1 1155 ? 13.617  88.897  105.010 1.00 49.49 ? 1153 LYS A O     1 
ATOM   8417  C CB    . LYS A  1 1155 ? 16.309  88.489  103.163 1.00 42.24 ? 1153 LYS A CB    1 
ATOM   8418  N N     . ASP A  1 1156 ? 13.153  88.587  102.834 1.00 41.69 ? 1154 ASP A N     1 
ATOM   8419  C CA    . ASP A  1 1156 ? 11.934  89.387  102.817 1.00 42.61 ? 1154 ASP A CA    1 
ATOM   8420  C C     . ASP A  1 1156 ? 10.773  88.404  102.658 1.00 40.70 ? 1154 ASP A C     1 
ATOM   8421  O O     . ASP A  1 1156 ? 10.407  88.029  101.542 1.00 38.33 ? 1154 ASP A O     1 
ATOM   8422  C CB    . ASP A  1 1156 ? 11.999  90.427  101.685 1.00 42.25 ? 1154 ASP A CB    1 
ATOM   8423  C CG    . ASP A  1 1156 ? 10.754  91.300  101.603 1.00 51.14 ? 1154 ASP A CG    1 
ATOM   8424  O OD1   . ASP A  1 1156 ? 9.832   91.129  102.432 1.00 51.77 ? 1154 ASP A OD1   1 
ATOM   8425  O OD2   . ASP A  1 1156 ? 10.697  92.169  100.699 1.00 52.50 ? 1154 ASP A OD2   1 
ATOM   8426  N N     . TRP A  1 1157 ? 10.190  87.988  103.791 1.00 37.84 ? 1155 TRP A N     1 
ATOM   8427  C CA    . TRP A  1 1157 ? 9.167   86.941  103.751 1.00 35.09 ? 1155 TRP A CA    1 
ATOM   8428  C C     . TRP A  1 1157 ? 7.992   87.337  102.869 1.00 37.29 ? 1155 TRP A C     1 
ATOM   8429  O O     . TRP A  1 1157 ? 7.477   86.512  102.106 1.00 36.58 ? 1155 TRP A O     1 
ATOM   8430  C CB    . TRP A  1 1157 ? 8.662   86.615  105.154 1.00 33.00 ? 1155 TRP A CB    1 
ATOM   8431  C CG    . TRP A  1 1157 ? 9.706   86.184  106.117 1.00 34.73 ? 1155 TRP A CG    1 
ATOM   8432  C CD1   . TRP A  1 1157 ? 10.995  85.854  105.839 1.00 32.84 ? 1155 TRP A CD1   1 
ATOM   8433  C CD2   . TRP A  1 1157 ? 9.550   86.046  107.534 1.00 29.09 ? 1155 TRP A CD2   1 
ATOM   8434  N NE1   . TRP A  1 1157 ? 11.657  85.521  106.999 1.00 33.86 ? 1155 TRP A NE1   1 
ATOM   8435  C CE2   . TRP A  1 1157 ? 10.790  85.633  108.052 1.00 34.17 ? 1155 TRP A CE2   1 
ATOM   8436  C CE3   . TRP A  1 1157 ? 8.482   86.248  108.416 1.00 31.99 ? 1155 TRP A CE3   1 
ATOM   8437  C CZ2   . TRP A  1 1157 ? 10.993  85.404  109.412 1.00 33.90 ? 1155 TRP A CZ2   1 
ATOM   8438  C CZ3   . TRP A  1 1157 ? 8.686   86.027  109.765 1.00 29.39 ? 1155 TRP A CZ3   1 
ATOM   8439  C CH2   . TRP A  1 1157 ? 9.929   85.613  110.248 1.00 34.51 ? 1155 TRP A CH2   1 
ATOM   8440  N N     . ALA A  1 1158 ? 7.552   88.595  102.952 1.00 36.29 ? 1156 ALA A N     1 
ATOM   8441  C CA    . ALA A  1 1158 ? 6.388   89.007  102.172 1.00 38.49 ? 1156 ALA A CA    1 
ATOM   8442  C C     . ALA A  1 1158 ? 6.625   88.901  100.672 1.00 39.92 ? 1156 ALA A C     1 
ATOM   8443  O O     . ALA A  1 1158 ? 5.662   88.747  99.913  1.00 41.85 ? 1156 ALA A O     1 
ATOM   8444  C CB    . ALA A  1 1158 ? 5.983   90.436  102.529 1.00 43.78 ? 1156 ALA A CB    1 
ATOM   8445  N N     . ALA A  1 1159 ? 7.880   88.959  100.229 1.00 38.71 ? 1157 ALA A N     1 
ATOM   8446  C CA    . ALA A  1 1159 ? 8.161   88.901  98.802  1.00 44.03 ? 1157 ALA A CA    1 
ATOM   8447  C C     . ALA A  1 1159 ? 8.187   87.476  98.281  1.00 42.57 ? 1157 ALA A C     1 
ATOM   8448  O O     . ALA A  1 1159 ? 7.930   87.250  97.096  1.00 44.78 ? 1157 ALA A O     1 
ATOM   8449  C CB    . ALA A  1 1159 ? 9.497   89.587  98.498  1.00 42.91 ? 1157 ALA A CB    1 
ATOM   8450  N N     . ASP A  1 1160 ? 8.494   86.513  99.143  1.00 43.46 ? 1158 ASP A N     1 
ATOM   8451  C CA    . ASP A  1 1160 ? 8.708   85.135  98.737  1.00 39.61 ? 1158 ASP A CA    1 
ATOM   8452  C C     . ASP A  1 1160 ? 7.488   84.264  98.964  1.00 38.16 ? 1158 ASP A C     1 
ATOM   8453  O O     . ASP A  1 1160 ? 7.584   83.041  98.848  1.00 40.86 ? 1158 ASP A O     1 
ATOM   8454  C CB    . ASP A  1 1160 ? 9.918   84.575  99.476  1.00 39.92 ? 1158 ASP A CB    1 
ATOM   8455  C CG    . ASP A  1 1160 ? 11.178  85.333  99.139  1.00 44.09 ? 1158 ASP A CG    1 
ATOM   8456  O OD1   . ASP A  1 1160 ? 11.231  85.892  98.019  1.00 45.41 ? 1158 ASP A OD1   1 
ATOM   8457  O OD2   . ASP A  1 1160 ? 12.096  85.393  99.980  1.00 42.82 ? 1158 ASP A OD2   1 
ATOM   8458  N N     . GLY A  1 1161 ? 6.345   84.870  99.264  1.00 36.70 ? 1159 GLY A N     1 
ATOM   8459  C CA    . GLY A  1 1161 ? 5.125   84.141  99.480  1.00 34.86 ? 1159 GLY A CA    1 
ATOM   8460  C C     . GLY A  1 1161 ? 4.380   83.883  98.191  1.00 39.25 ? 1159 GLY A C     1 
ATOM   8461  O O     . GLY A  1 1161 ? 4.885   84.141  97.094  1.00 40.63 ? 1159 GLY A O     1 
ATOM   8462  N N     . PRO A  1 1162 ? 3.152   83.354  98.300  1.00 34.83 ? 1160 PRO A N     1 
ATOM   8463  C CA    . PRO A  1 1162 ? 2.455   83.009  99.542  1.00 34.23 ? 1160 PRO A CA    1 
ATOM   8464  C C     . PRO A  1 1162 ? 2.982   81.727  100.170 1.00 34.56 ? 1160 PRO A C     1 
ATOM   8465  O O     . PRO A  1 1162 ? 3.444   80.801  99.499  1.00 34.99 ? 1160 PRO A O     1 
ATOM   8466  C CB    . PRO A  1 1162 ? 0.994   82.859  99.088  1.00 34.93 ? 1160 PRO A CB    1 
ATOM   8467  C CG    . PRO A  1 1162 ? 1.107   82.342  97.686  1.00 37.43 ? 1160 PRO A CG    1 
ATOM   8468  C CD    . PRO A  1 1162 ? 2.353   83.005  97.111  1.00 36.77 ? 1160 PRO A CD    1 
ATOM   8469  N N     . PHE A  1 1163 ? 2.921   81.655  101.491 1.00 29.07 ? 1161 PHE A N     1 
ATOM   8470  C CA    . PHE A  1 1163 ? 3.236   80.429  102.198 1.00 24.92 ? 1161 PHE A CA    1 
ATOM   8471  C C     . PHE A  1 1163 ? 1.947   79.681  102.534 1.00 28.44 ? 1161 PHE A C     1 
ATOM   8472  O O     . PHE A  1 1163 ? 0.834   80.196  102.383 1.00 31.84 ? 1161 PHE A O     1 
ATOM   8473  C CB    . PHE A  1 1163 ? 4.071   80.753  103.439 1.00 26.55 ? 1161 PHE A CB    1 
ATOM   8474  C CG    . PHE A  1 1163 ? 5.349   81.496  103.115 1.00 28.24 ? 1161 PHE A CG    1 
ATOM   8475  C CD1   . PHE A  1 1163 ? 6.294   80.931  102.274 1.00 27.50 ? 1161 PHE A CD1   1 
ATOM   8476  C CD2   . PHE A  1 1163 ? 5.584   82.761  103.620 1.00 29.57 ? 1161 PHE A CD2   1 
ATOM   8477  C CE1   . PHE A  1 1163 ? 7.465   81.605  101.949 1.00 31.34 ? 1161 PHE A CE1   1 
ATOM   8478  C CE2   . PHE A  1 1163 ? 6.758   83.438  103.316 1.00 28.97 ? 1161 PHE A CE2   1 
ATOM   8479  C CZ    . PHE A  1 1163 ? 7.701   82.856  102.474 1.00 31.89 ? 1161 PHE A CZ    1 
ATOM   8480  N N     . ALA A  1 1164 ? 2.102   78.426  102.940 1.00 27.30 ? 1162 ALA A N     1 
ATOM   8481  C CA    . ALA A  1 1164 ? 0.957   77.598  103.297 1.00 28.70 ? 1162 ALA A CA    1 
ATOM   8482  C C     . ALA A  1 1164 ? 0.965   77.194  104.765 1.00 26.47 ? 1162 ALA A C     1 
ATOM   8483  O O     . ALA A  1 1164 ? 0.165   76.344  105.163 1.00 27.38 ? 1162 ALA A O     1 
ATOM   8484  C CB    . ALA A  1 1164 ? 0.904   76.350  102.410 1.00 27.09 ? 1162 ALA A CB    1 
ATOM   8485  N N     . GLY A  1 1165 ? 1.840   77.784  105.567 1.00 24.89 ? 1163 GLY A N     1 
ATOM   8486  C CA    . GLY A  1 1165 ? 2.009   77.431  106.962 1.00 25.78 ? 1163 GLY A CA    1 
ATOM   8487  C C     . GLY A  1 1165 ? 3.381   77.875  107.410 1.00 28.96 ? 1163 GLY A C     1 
ATOM   8488  O O     . GLY A  1 1165 ? 4.204   78.328  106.609 1.00 24.95 ? 1163 GLY A O     1 
ATOM   8489  N N     . ALA A  1 1166 ? 3.633   77.738  108.713 1.00 24.39 ? 1164 ALA A N     1 
ATOM   8490  C CA    . ALA A  1 1166 ? 4.917   78.166  109.250 1.00 22.53 ? 1164 ALA A CA    1 
ATOM   8491  C C     . ALA A  1 1166 ? 5.297   77.317  110.455 1.00 26.97 ? 1164 ALA A C     1 
ATOM   8492  O O     . ALA A  1 1166 ? 4.430   76.823  111.182 1.00 28.68 ? 1164 ALA A O     1 
ATOM   8493  C CB    . ALA A  1 1166 ? 4.894   79.652  109.651 1.00 27.23 ? 1164 ALA A CB    1 
ATOM   8494  N N     . LEU A  1 1167 ? 6.609   77.139  110.642 1.00 21.25 ? 1165 LEU A N     1 
ATOM   8495  C CA    . LEU A  1 1167 ? 7.177   76.494  111.821 1.00 25.40 ? 1165 LEU A CA    1 
ATOM   8496  C C     . LEU A  1 1167 ? 8.165   77.462  112.457 1.00 24.93 ? 1165 LEU A C     1 
ATOM   8497  O O     . LEU A  1 1167 ? 9.051   77.982  111.772 1.00 27.82 ? 1165 LEU A O     1 
ATOM   8498  C CB    . LEU A  1 1167 ? 7.874   75.178  111.450 1.00 27.24 ? 1165 LEU A CB    1 
ATOM   8499  C CG    . LEU A  1 1167 ? 6.987   74.150  110.723 1.00 28.56 ? 1165 LEU A CG    1 
ATOM   8500  C CD1   . LEU A  1 1167 ? 7.826   72.944  110.224 1.00 21.51 ? 1165 LEU A CD1   1 
ATOM   8501  C CD2   . LEU A  1 1167 ? 5.848   73.699  111.622 1.00 23.08 ? 1165 LEU A CD2   1 
ATOM   8502  N N     . VAL A  1 1168 ? 8.007   77.726  113.751 1.00 22.36 ? 1166 VAL A N     1 
ATOM   8503  C CA    . VAL A  1 1168 ? 8.817   78.719  114.450 1.00 25.16 ? 1166 VAL A CA    1 
ATOM   8504  C C     . VAL A  1 1168 ? 9.494   78.046  115.632 1.00 26.60 ? 1166 VAL A C     1 
ATOM   8505  O O     . VAL A  1 1168 ? 8.867   77.245  116.336 1.00 26.30 ? 1166 VAL A O     1 
ATOM   8506  C CB    . VAL A  1 1168 ? 7.973   79.920  114.934 1.00 25.06 ? 1166 VAL A CB    1 
ATOM   8507  C CG1   . VAL A  1 1168 ? 8.875   80.994  115.550 1.00 27.56 ? 1166 VAL A CG1   1 
ATOM   8508  C CG2   . VAL A  1 1168 ? 7.118   80.482  113.788 1.00 23.55 ? 1166 VAL A CG2   1 
ATOM   8509  N N     . GLU A  1 1169 ? 10.763  78.386  115.852 1.00 25.02 ? 1167 GLU A N     1 
ATOM   8510  C CA    . GLU A  1 1169 ? 11.521  77.992  117.040 1.00 25.43 ? 1167 GLU A CA    1 
ATOM   8511  C C     . GLU A  1 1169 ? 11.978  79.228  117.804 1.00 28.39 ? 1167 GLU A C     1 
ATOM   8512  O O     . GLU A  1 1169 ? 12.576  80.140  117.224 1.00 26.91 ? 1167 GLU A O     1 
ATOM   8513  C CB    . GLU A  1 1169 ? 12.739  77.152  116.652 1.00 27.10 ? 1167 GLU A CB    1 
ATOM   8514  C CG    . GLU A  1 1169 ? 13.594  76.691  117.822 1.00 25.57 ? 1167 GLU A CG    1 
ATOM   8515  C CD    . GLU A  1 1169 ? 14.956  76.162  117.374 1.00 31.77 ? 1167 GLU A CD    1 
ATOM   8516  O OE1   . GLU A  1 1169 ? 15.283  76.309  116.175 1.00 31.06 ? 1167 GLU A OE1   1 
ATOM   8517  O OE2   . GLU A  1 1169 ? 15.695  75.597  118.213 1.00 31.78 ? 1167 GLU A OE2   1 
ATOM   8518  N N     . GLY A  1 1170 ? 11.716  79.259  119.103 1.00 26.56 ? 1168 GLY A N     1 
ATOM   8519  C CA    . GLY A  1 1170 ? 12.242  80.348  119.893 1.00 29.69 ? 1168 GLY A CA    1 
ATOM   8520  C C     . GLY A  1 1170 ? 11.693  80.304  121.292 1.00 30.14 ? 1168 GLY A C     1 
ATOM   8521  O O     . GLY A  1 1170 ? 10.824  79.492  121.623 1.00 29.70 ? 1168 GLY A O     1 
ATOM   8522  N N     . ASP A  1 1171 ? 12.216  81.211  122.116 1.00 31.78 ? 1169 ASP A N     1 
ATOM   8523  C CA    . ASP A  1 1171 ? 11.601  81.438  123.412 1.00 30.76 ? 1169 ASP A CA    1 
ATOM   8524  C C     . ASP A  1 1171 ? 10.309  82.226  123.213 1.00 32.85 ? 1169 ASP A C     1 
ATOM   8525  O O     . ASP A  1 1171 ? 9.954   82.615  122.095 1.00 29.22 ? 1169 ASP A O     1 
ATOM   8526  C CB    . ASP A  1 1171 ? 12.591  82.116  124.368 1.00 36.34 ? 1169 ASP A CB    1 
ATOM   8527  C CG    . ASP A  1 1171 ? 13.025  83.523  123.920 1.00 40.97 ? 1169 ASP A CG    1 
ATOM   8528  O OD1   . ASP A  1 1171 ? 12.335  84.183  123.117 1.00 37.40 ? 1169 ASP A OD1   1 
ATOM   8529  O OD2   . ASP A  1 1171 ? 14.082  83.985  124.398 1.00 45.26 ? 1169 ASP A OD2   1 
ATOM   8530  N N     . ALA A  1 1172 ? 9.596   82.470  124.318 1.00 30.65 ? 1170 ALA A N     1 
ATOM   8531  C CA    . ALA A  1 1172 ? 8.250   83.036  124.228 1.00 33.26 ? 1170 ALA A CA    1 
ATOM   8532  C C     . ALA A  1 1172 ? 8.254   84.379  123.503 1.00 31.19 ? 1170 ALA A C     1 
ATOM   8533  O O     . ALA A  1 1172 ? 7.418   84.621  122.623 1.00 33.37 ? 1170 ALA A O     1 
ATOM   8534  C CB    . ALA A  1 1172 ? 7.650   83.184  125.628 1.00 31.86 ? 1170 ALA A CB    1 
ATOM   8535  N N     . GLU A  1 1173 ? 9.200   85.262  123.851 1.00 34.29 ? 1171 GLU A N     1 
ATOM   8536  C CA    . GLU A  1 1173 ? 9.240   86.589  123.236 1.00 36.03 ? 1171 GLU A CA    1 
ATOM   8537  C C     . GLU A  1 1173 ? 9.586   86.507  121.752 1.00 33.13 ? 1171 GLU A C     1 
ATOM   8538  O O     . GLU A  1 1173 ? 9.047   87.269  120.935 1.00 33.21 ? 1171 GLU A O     1 
ATOM   8539  C CB    . GLU A  1 1173 ? 10.239  87.484  123.978 1.00 37.77 ? 1171 GLU A CB    1 
ATOM   8540  N N     . ARG A  1 1174 ? 10.462  85.573  121.382 1.00 28.71 ? 1172 ARG A N     1 
ATOM   8541  C CA    . ARG A  1 1174 ? 10.783  85.388  119.972 1.00 30.81 ? 1172 ARG A CA    1 
ATOM   8542  C C     . ARG A  1 1174 ? 9.571   84.891  119.197 1.00 31.46 ? 1172 ARG A C     1 
ATOM   8543  O O     . ARG A  1 1174 ? 9.339   85.311  118.055 1.00 31.20 ? 1172 ARG A O     1 
ATOM   8544  C CB    . ARG A  1 1174 ? 11.946  84.411  119.830 1.00 31.33 ? 1172 ARG A CB    1 
ATOM   8545  C CG    . ARG A  1 1174 ? 12.263  83.992  118.399 1.00 30.52 ? 1172 ARG A CG    1 
ATOM   8546  C CD    . ARG A  1 1174 ? 12.875  85.154  117.623 1.00 35.53 ? 1172 ARG A CD    1 
ATOM   8547  N NE    . ARG A  1 1174 ? 13.192  84.804  116.241 1.00 31.74 ? 1172 ARG A NE    1 
ATOM   8548  C CZ    . ARG A  1 1174 ? 13.248  85.687  115.249 1.00 35.29 ? 1172 ARG A CZ    1 
ATOM   8549  N NH1   . ARG A  1 1174 ? 12.979  86.969  115.444 1.00 31.51 ? 1172 ARG A NH1   1 
ATOM   8550  N NH2   . ARG A  1 1174 ? 13.577  85.274  114.032 1.00 28.30 ? 1172 ARG A NH2   1 
ATOM   8551  N N     . ILE A  1 1175 ? 8.792   83.991  119.800 1.00 31.16 ? 1173 ILE A N     1 
ATOM   8552  C CA    . ILE A  1 1175 ? 7.601   83.463  119.137 1.00 28.14 ? 1173 ILE A CA    1 
ATOM   8553  C C     . ILE A  1 1175 ? 6.570   84.569  118.926 1.00 30.14 ? 1173 ILE A C     1 
ATOM   8554  O O     . ILE A  1 1175 ? 6.003   84.707  117.840 1.00 28.27 ? 1173 ILE A O     1 
ATOM   8555  C CB    . ILE A  1 1175 ? 7.011   82.290  119.942 1.00 28.21 ? 1173 ILE A CB    1 
ATOM   8556  C CG1   . ILE A  1 1175 ? 7.931   81.066  119.871 1.00 31.70 ? 1173 ILE A CG1   1 
ATOM   8557  C CG2   . ILE A  1 1175 ? 5.616   81.971  119.436 1.00 30.05 ? 1173 ILE A CG2   1 
ATOM   8558  C CD1   . ILE A  1 1175 ? 7.630   79.973  120.906 1.00 31.60 ? 1173 ILE A CD1   1 
ATOM   8559  N N     . ARG A  1 1176 ? 6.301   85.364  119.968 1.00 30.24 ? 1174 ARG A N     1 
ATOM   8560  C CA    . ARG A  1 1176 ? 5.373   86.482  119.820 1.00 28.97 ? 1174 ARG A CA    1 
ATOM   8561  C C     . ARG A  1 1176 ? 5.826   87.437  118.718 1.00 29.18 ? 1174 ARG A C     1 
ATOM   8562  O O     . ARG A  1 1176 ? 5.024   87.841  117.866 1.00 29.39 ? 1174 ARG A O     1 
ATOM   8563  C CB    . ARG A  1 1176 ? 5.232   87.222  121.147 1.00 31.53 ? 1174 ARG A CB    1 
ATOM   8564  C CG    . ARG A  1 1176 ? 3.995   88.127  121.186 1.00 34.47 ? 1174 ARG A CG    1 
ATOM   8565  C CD    . ARG A  1 1176 ? 4.077   89.171  122.291 1.00 38.55 ? 1174 ARG A CD    1 
ATOM   8566  N NE    . ARG A  1 1176 ? 4.420   88.583  123.583 1.00 42.53 ? 1174 ARG A NE    1 
ATOM   8567  C CZ    . ARG A  1 1176 ? 3.536   88.127  124.463 1.00 43.42 ? 1174 ARG A CZ    1 
ATOM   8568  N NH1   . ARG A  1 1176 ? 2.233   88.167  124.222 1.00 40.77 ? 1174 ARG A NH1   1 
ATOM   8569  N NH2   . ARG A  1 1176 ? 3.970   87.622  125.617 1.00 37.59 ? 1174 ARG A NH2   1 
ATOM   8570  N N     . ALA A  1 1177 ? 7.118   87.767  118.692 1.00 30.49 ? 1175 ALA A N     1 
ATOM   8571  C CA    . ALA A  1 1177 ? 7.653   88.664  117.668 1.00 32.75 ? 1175 ALA A CA    1 
ATOM   8572  C C     . ALA A  1 1177 ? 7.487   88.078  116.271 1.00 29.15 ? 1175 ALA A C     1 
ATOM   8573  O O     . ALA A  1 1177 ? 7.071   88.772  115.337 1.00 29.48 ? 1175 ALA A O     1 
ATOM   8574  C CB    . ALA A  1 1177 ? 9.129   88.946  117.941 1.00 29.65 ? 1175 ALA A CB    1 
ATOM   8575  N N     . VAL A  1 1178 ? 7.848   86.807  116.104 1.00 26.51 ? 1176 VAL A N     1 
ATOM   8576  C CA    . VAL A  1 1178 ? 7.712   86.167  114.803 1.00 27.65 ? 1176 VAL A CA    1 
ATOM   8577  C C     . VAL A  1 1178 ? 6.242   86.069  114.410 1.00 30.11 ? 1176 VAL A C     1 
ATOM   8578  O O     . VAL A  1 1178 ? 5.874   86.307  113.248 1.00 29.81 ? 1176 VAL A O     1 
ATOM   8579  C CB    . VAL A  1 1178 ? 8.390   84.783  114.822 1.00 28.23 ? 1176 VAL A CB    1 
ATOM   8580  C CG1   . VAL A  1 1178 ? 8.009   83.981  113.578 1.00 24.59 ? 1176 VAL A CG1   1 
ATOM   8581  C CG2   . VAL A  1 1178 ? 9.906   84.909  114.941 1.00 29.17 ? 1176 VAL A CG2   1 
ATOM   8582  N N     . ASN A  1 1179 ? 5.377   85.720  115.370 1.00 28.11 ? 1177 ASN A N     1 
ATOM   8583  C CA    . ASN A  1 1179 ? 3.946   85.572  115.093 1.00 27.98 ? 1177 ASN A CA    1 
ATOM   8584  C C     . ASN A  1 1179 ? 3.348   86.878  114.579 1.00 30.21 ? 1177 ASN A C     1 
ATOM   8585  O O     . ASN A  1 1179 ? 2.526   86.872  113.654 1.00 30.09 ? 1177 ASN A O     1 
ATOM   8586  C CB    . ASN A  1 1179 ? 3.231   85.097  116.362 1.00 29.69 ? 1177 ASN A CB    1 
ATOM   8587  C CG    . ASN A  1 1179 ? 1.947   84.351  116.088 1.00 35.72 ? 1177 ASN A CG    1 
ATOM   8588  O OD1   . ASN A  1 1179 ? 1.761   83.751  115.028 1.00 35.22 ? 1177 ASN A OD1   1 
ATOM   8589  N ND2   . ASN A  1 1179 ? 1.040   84.378  117.066 1.00 37.70 ? 1177 ASN A ND2   1 
ATOM   8590  N N     . LYS A  1 1180 ? 3.789   88.013  115.136 1.00 28.68 ? 1178 LYS A N     1 
ATOM   8591  C CA    . LYS A  1 1180 ? 3.332   89.310  114.655 1.00 31.64 ? 1178 LYS A CA    1 
ATOM   8592  C C     . LYS A  1 1180 ? 3.839   89.590  113.245 1.00 33.09 ? 1178 LYS A C     1 
ATOM   8593  O O     . LYS A  1 1180 ? 3.089   90.096  112.403 1.00 34.60 ? 1178 LYS A O     1 
ATOM   8594  C CB    . LYS A  1 1180 ? 3.778   90.408  115.622 1.00 34.39 ? 1178 LYS A CB    1 
ATOM   8595  C CG    . LYS A  1 1180 ? 3.073   90.348  116.976 1.00 33.41 ? 1178 LYS A CG    1 
ATOM   8596  C CD    . LYS A  1 1180 ? 3.802   91.208  118.010 1.00 31.97 ? 1178 LYS A CD    1 
ATOM   8597  C CE    . LYS A  1 1180 ? 3.454   92.685  117.848 1.00 47.53 ? 1178 LYS A CE    1 
ATOM   8598  N NZ    . LYS A  1 1180 ? 4.318   93.578  118.706 1.00 52.37 ? 1178 LYS A NZ    1 
ATOM   8599  N N     . ALA A  1 1181 ? 5.105   89.262  112.967 1.00 30.67 ? 1179 ALA A N     1 
ATOM   8600  C CA    . ALA A  1 1181 ? 5.634   89.437  111.617 1.00 32.72 ? 1179 ALA A CA    1 
ATOM   8601  C C     . ALA A  1 1181 ? 4.899   88.557  110.613 1.00 31.55 ? 1179 ALA A C     1 
ATOM   8602  O O     . ALA A  1 1181 ? 4.672   88.968  109.470 1.00 28.16 ? 1179 ALA A O     1 
ATOM   8603  C CB    . ALA A  1 1181 ? 7.143   89.144  111.584 1.00 26.98 ? 1179 ALA A CB    1 
ATOM   8604  N N     . ILE A  1 1182 ? 4.520   87.339  111.014 1.00 28.83 ? 1180 ILE A N     1 
ATOM   8605  C CA    . ILE A  1 1182 ? 3.791   86.462  110.098 1.00 31.01 ? 1180 ILE A CA    1 
ATOM   8606  C C     . ILE A  1 1182 ? 2.391   87.007  109.835 1.00 31.26 ? 1180 ILE A C     1 
ATOM   8607  O O     . ILE A  1 1182 ? 1.907   86.998  108.695 1.00 29.11 ? 1180 ILE A O     1 
ATOM   8608  C CB    . ILE A  1 1182 ? 3.752   85.025  110.650 1.00 32.17 ? 1180 ILE A CB    1 
ATOM   8609  C CG1   . ILE A  1 1182 ? 5.149   84.394  110.601 1.00 31.93 ? 1180 ILE A CG1   1 
ATOM   8610  C CG2   . ILE A  1 1182 ? 2.764   84.173  109.874 1.00 32.32 ? 1180 ILE A CG2   1 
ATOM   8611  C CD1   . ILE A  1 1182 ? 5.210   82.998  111.205 1.00 30.25 ? 1180 ILE A CD1   1 
ATOM   8612  N N     . ALA A  1 1183 ? 1.724   87.505  110.878 1.00 30.86 ? 1181 ALA A N     1 
ATOM   8613  C CA    . ALA A  1 1183 ? 0.393   88.070  110.692 1.00 34.74 ? 1181 ALA A CA    1 
ATOM   8614  C C     . ALA A  1 1183 ? 0.411   89.246  109.723 1.00 33.33 ? 1181 ALA A C     1 
ATOM   8615  O O     . ALA A  1 1183 ? -0.595  89.511  109.060 1.00 35.71 ? 1181 ALA A O     1 
ATOM   8616  C CB    . ALA A  1 1183 ? -0.197  88.498  112.036 1.00 29.64 ? 1181 ALA A CB    1 
ATOM   8617  N N     . ALA A  1 1184 ? 1.543   89.947  109.609 1.00 34.90 ? 1182 ALA A N     1 
ATOM   8618  C CA    . ALA A  1 1184 ? 1.642   91.086  108.702 1.00 34.94 ? 1182 ALA A CA    1 
ATOM   8619  C C     . ALA A  1 1184 ? 1.931   90.681  107.265 1.00 36.33 ? 1182 ALA A C     1 
ATOM   8620  O O     . ALA A  1 1184 ? 1.969   91.556  106.395 1.00 37.15 ? 1182 ALA A O     1 
ATOM   8621  C CB    . ALA A  1 1184 ? 2.730   92.056  109.169 1.00 35.87 ? 1182 ALA A CB    1 
ATOM   8622  N N     . LEU A  1 1185 ? 2.157   89.403  106.998 1.00 33.61 ? 1183 LEU A N     1 
ATOM   8623  C CA    . LEU A  1 1185 ? 2.367   88.962  105.625 1.00 34.35 ? 1183 LEU A CA    1 
ATOM   8624  C C     . LEU A  1 1185 ? 1.064   89.091  104.841 1.00 36.68 ? 1183 LEU A C     1 
ATOM   8625  O O     . LEU A  1 1185 ? 0.005   88.669  105.323 1.00 32.76 ? 1183 LEU A O     1 
ATOM   8626  C CB    . LEU A  1 1185 ? 2.857   87.521  105.583 1.00 33.95 ? 1183 LEU A CB    1 
ATOM   8627  C CG    . LEU A  1 1185 ? 4.188   87.207  106.263 1.00 33.36 ? 1183 LEU A CG    1 
ATOM   8628  C CD1   . LEU A  1 1185 ? 4.448   85.707  106.209 1.00 30.34 ? 1183 LEU A CD1   1 
ATOM   8629  C CD2   . LEU A  1 1185 ? 5.341   87.989  105.633 1.00 35.64 ? 1183 LEU A CD2   1 
ATOM   8630  N N     . PRO A  1 1186 ? 1.091   89.667  103.644 1.00 38.31 ? 1184 PRO A N     1 
ATOM   8631  C CA    . PRO A  1 1186 ? -0.133  89.757  102.850 1.00 34.86 ? 1184 PRO A CA    1 
ATOM   8632  C C     . PRO A  1 1186 ? -0.566  88.384  102.367 1.00 30.47 ? 1184 PRO A C     1 
ATOM   8633  O O     . PRO A  1 1186 ? 0.230   87.451  102.251 1.00 32.28 ? 1184 PRO A O     1 
ATOM   8634  C CB    . PRO A  1 1186 ? 0.273   90.652  101.676 1.00 45.28 ? 1184 PRO A CB    1 
ATOM   8635  C CG    . PRO A  1 1186 ? 1.743   90.352  101.509 1.00 48.62 ? 1184 PRO A CG    1 
ATOM   8636  C CD    . PRO A  1 1186 ? 2.268   90.166  102.912 1.00 41.92 ? 1184 PRO A CD    1 
ATOM   8637  N N     . GLY A  1 1187 ? -1.861  88.270  102.083 1.00 33.82 ? 1185 GLY A N     1 
ATOM   8638  C CA    . GLY A  1 1187 ? -2.401  87.049  101.537 1.00 33.37 ? 1185 GLY A CA    1 
ATOM   8639  C C     . GLY A  1 1187 ? -2.991  86.133  102.591 1.00 32.75 ? 1185 GLY A C     1 
ATOM   8640  O O     . GLY A  1 1187 ? -3.695  86.574  103.507 1.00 32.50 ? 1185 GLY A O     1 
ATOM   8641  N N     . PRO A  1 1188 ? -2.727  84.831  102.462 1.00 30.99 ? 1186 PRO A N     1 
ATOM   8642  C CA    . PRO A  1 1188 ? -3.423  83.844  103.300 1.00 27.27 ? 1186 PRO A CA    1 
ATOM   8643  C C     . PRO A  1 1188 ? -3.033  83.960  104.763 1.00 30.84 ? 1186 PRO A C     1 
ATOM   8644  O O     . PRO A  1 1188 ? -1.909  84.342  105.110 1.00 26.45 ? 1186 PRO A O     1 
ATOM   8645  C CB    . PRO A  1 1188 ? -2.969  82.499  102.718 1.00 33.25 ? 1186 PRO A CB    1 
ATOM   8646  C CG    . PRO A  1 1188 ? -1.626  82.801  102.115 1.00 34.75 ? 1186 PRO A CG    1 
ATOM   8647  C CD    . PRO A  1 1188 ? -1.729  84.208  101.576 1.00 30.57 ? 1186 PRO A CD    1 
ATOM   8648  N N     . LEU A  1 1189 ? -3.982  83.609  105.623 1.00 27.72 ? 1187 LEU A N     1 
ATOM   8649  C CA    . LEU A  1 1189 ? -3.716  83.498  107.051 1.00 28.49 ? 1187 LEU A CA    1 
ATOM   8650  C C     . LEU A  1 1189 ? -2.965  82.200  107.295 1.00 30.79 ? 1187 LEU A C     1 
ATOM   8651  O O     . LEU A  1 1189 ? -3.502  81.118  107.041 1.00 38.75 ? 1187 LEU A O     1 
ATOM   8652  C CB    . LEU A  1 1189 ? -5.019  83.521  107.847 1.00 32.81 ? 1187 LEU A CB    1 
ATOM   8653  C CG    . LEU A  1 1189 ? -5.691  84.871  108.124 1.00 38.85 ? 1187 LEU A CG    1 
ATOM   8654  C CD1   . LEU A  1 1189 ? -6.174  85.564  106.850 1.00 34.99 ? 1187 LEU A CD1   1 
ATOM   8655  C CD2   . LEU A  1 1189 ? -6.859  84.680  109.071 1.00 36.75 ? 1187 LEU A CD2   1 
ATOM   8656  N N     . LEU A  1 1190 ? -1.728  82.292  107.769 1.00 28.94 ? 1188 LEU A N     1 
ATOM   8657  C CA    . LEU A  1 1190 ? -0.909  81.094  107.901 1.00 29.03 ? 1188 LEU A CA    1 
ATOM   8658  C C     . LEU A  1 1190 ? -1.239  80.346  109.185 1.00 28.18 ? 1188 LEU A C     1 
ATOM   8659  O O     . LEU A  1 1190 ? -1.397  80.951  110.248 1.00 28.59 ? 1188 LEU A O     1 
ATOM   8660  C CB    . LEU A  1 1190 ? 0.574   81.448  107.887 1.00 31.00 ? 1188 LEU A CB    1 
ATOM   8661  C CG    . LEU A  1 1190 ? 1.122   82.068  106.603 1.00 33.27 ? 1188 LEU A CG    1 
ATOM   8662  C CD1   . LEU A  1 1190 ? 2.643   82.094  106.673 1.00 33.13 ? 1188 LEU A CD1   1 
ATOM   8663  C CD2   . LEU A  1 1190 ? 0.651   81.268  105.400 1.00 31.69 ? 1188 LEU A CD2   1 
ATOM   8664  N N     . LEU A  1 1191 ? -1.336  79.023  109.085 1.00 28.67 ? 1189 LEU A N     1 
ATOM   8665  C CA    . LEU A  1 1191 ? -1.361  78.171  110.276 1.00 28.75 ? 1189 LEU A CA    1 
ATOM   8666  C C     . LEU A  1 1191 ? 0.078   78.031  110.771 1.00 27.93 ? 1189 LEU A C     1 
ATOM   8667  O O     . LEU A  1 1191 ? 0.921   77.426  110.093 1.00 26.52 ? 1189 LEU A O     1 
ATOM   8668  C CB    . LEU A  1 1191 ? -1.995  76.819  109.959 1.00 27.38 ? 1189 LEU A CB    1 
ATOM   8669  C CG    . LEU A  1 1191 ? -2.563  75.954  111.093 1.00 29.30 ? 1189 LEU A CG    1 
ATOM   8670  C CD1   . LEU A  1 1191 ? -3.348  74.772  110.515 1.00 28.68 ? 1189 LEU A CD1   1 
ATOM   8671  C CD2   . LEU A  1 1191 ? -1.456  75.447  112.019 1.00 25.28 ? 1189 LEU A CD2   1 
ATOM   8672  N N     . VAL A  1 1192 ? 0.357   78.634  111.934 1.00 28.72 ? 1190 VAL A N     1 
ATOM   8673  C CA    . VAL A  1 1192 ? 1.689   78.733  112.525 1.00 26.99 ? 1190 VAL A CA    1 
ATOM   8674  C C     . VAL A  1 1192 ? 1.806   77.739  113.683 1.00 27.69 ? 1190 VAL A C     1 
ATOM   8675  O O     . VAL A  1 1192 ? 0.919   77.667  114.543 1.00 29.82 ? 1190 VAL A O     1 
ATOM   8676  C CB    . VAL A  1 1192 ? 1.957   80.167  113.030 1.00 28.31 ? 1190 VAL A CB    1 
ATOM   8677  C CG1   . VAL A  1 1192 ? 3.317   80.254  113.722 1.00 27.26 ? 1190 VAL A CG1   1 
ATOM   8678  C CG2   . VAL A  1 1192 ? 1.880   81.197  111.895 1.00 26.79 ? 1190 VAL A CG2   1 
ATOM   8679  N N     . GLN A  1 1193 ? 2.920   77.013  113.745 1.00 26.79 ? 1191 GLN A N     1 
ATOM   8680  C CA    . GLN A  1 1193 ? 3.239   76.178  114.895 1.00 21.84 ? 1191 GLN A CA    1 
ATOM   8681  C C     . GLN A  1 1193 ? 4.567   76.611  115.484 1.00 24.49 ? 1191 GLN A C     1 
ATOM   8682  O O     . GLN A  1 1193 ? 5.542   76.835  114.757 1.00 25.35 ? 1191 GLN A O     1 
ATOM   8683  C CB    . GLN A  1 1193 ? 3.317   74.703  114.524 1.00 26.83 ? 1191 GLN A CB    1 
ATOM   8684  C CG    . GLN A  1 1193 ? 2.034   74.138  113.927 1.00 26.97 ? 1191 GLN A CG    1 
ATOM   8685  C CD    . GLN A  1 1193 ? 2.125   72.638  113.797 1.00 29.77 ? 1191 GLN A CD    1 
ATOM   8686  O OE1   . GLN A  1 1193 ? 2.081   71.917  114.798 1.00 31.33 ? 1191 GLN A OE1   1 
ATOM   8687  N NE2   . GLN A  1 1193 ? 2.286   72.160  112.569 1.00 28.62 ? 1191 GLN A NE2   1 
ATOM   8688  N N     . ALA A  1 1194 ? 4.608   76.707  116.804 1.00 24.09 ? 1192 ALA A N     1 
ATOM   8689  C CA    . ALA A  1 1194 ? 5.772   77.221  117.493 1.00 26.68 ? 1192 ALA A CA    1 
ATOM   8690  C C     . ALA A  1 1194 ? 6.197   76.242  118.574 1.00 29.88 ? 1192 ALA A C     1 
ATOM   8691  O O     . ALA A  1 1194 ? 5.374   75.521  119.143 1.00 26.85 ? 1192 ALA A O     1 
ATOM   8692  C CB    . ALA A  1 1194 ? 5.498   78.596  118.117 1.00 27.44 ? 1192 ALA A CB    1 
ATOM   8693  N N     . ALA A  1 1195 ? 7.497   76.224  118.842 1.00 25.76 ? 1193 ALA A N     1 
ATOM   8694  C CA    . ALA A  1 1195 ? 8.057   75.391  119.893 1.00 27.89 ? 1193 ALA A CA    1 
ATOM   8695  C C     . ALA A  1 1195 ? 9.364   76.020  120.344 1.00 30.73 ? 1193 ALA A C     1 
ATOM   8696  O O     . ALA A  1 1195 ? 10.026  76.715  119.572 1.00 31.03 ? 1193 ALA A O     1 
ATOM   8697  C CB    . ALA A  1 1195 ? 8.287   73.955  119.408 1.00 26.59 ? 1193 ALA A CB    1 
ATOM   8698  N N     . SER A  1 1196 ? 9.714   75.794  121.607 1.00 27.64 ? 1194 SER A N     1 
ATOM   8699  C CA    . SER A  1 1196 ? 11.016  76.218  122.092 1.00 30.51 ? 1194 SER A CA    1 
ATOM   8700  C C     . SER A  1 1196 ? 12.077  75.220  121.651 1.00 29.49 ? 1194 SER A C     1 
ATOM   8701  O O     . SER A  1 1196 ? 11.775  74.098  121.244 1.00 28.95 ? 1194 SER A O     1 
ATOM   8702  C CB    . SER A  1 1196 ? 11.017  76.328  123.613 1.00 33.80 ? 1194 SER A CB    1 
ATOM   8703  O OG    . SER A  1 1196 ? 10.799  75.048  124.182 1.00 36.83 ? 1194 SER A OG    1 
ATOM   8704  N N     . SER A  1 1197 ? 13.341  75.632  121.756 1.00 28.09 ? 1195 SER A N     1 
ATOM   8705  C CA    . SER A  1 1197 ? 14.428  74.689  121.518 1.00 31.79 ? 1195 SER A CA    1 
ATOM   8706  C C     . SER A  1 1197 ? 14.321  73.489  122.445 1.00 30.64 ? 1195 SER A C     1 
ATOM   8707  O O     . SER A  1 1197 ? 14.524  72.346  122.021 1.00 28.57 ? 1195 SER A O     1 
ATOM   8708  C CB    . SER A  1 1197 ? 15.779  75.382  121.700 1.00 34.83 ? 1195 SER A CB    1 
ATOM   8709  O OG    . SER A  1 1197 ? 15.987  76.329  120.667 1.00 33.73 ? 1195 SER A OG    1 
ATOM   8710  N N     . GLY A  1 1198 ? 14.002  73.729  123.717 1.00 33.15 ? 1196 GLY A N     1 
ATOM   8711  C CA    . GLY A  1 1198 ? 13.904  72.627  124.660 1.00 33.28 ? 1196 GLY A CA    1 
ATOM   8712  C C     . GLY A  1 1198 ? 12.754  71.696  124.329 1.00 34.64 ? 1196 GLY A C     1 
ATOM   8713  O O     . GLY A  1 1198 ? 12.876  70.474  124.444 1.00 31.97 ? 1196 GLY A O     1 
ATOM   8714  N N     . GLU A  1 1199 ? 11.633  72.258  123.881 1.00 29.88 ? 1197 GLU A N     1 
ATOM   8715  C CA    . GLU A  1 1199 ? 10.498  71.428  123.501 1.00 33.60 ? 1197 GLU A CA    1 
ATOM   8716  C C     . GLU A  1 1199 ? 10.840  70.526  122.319 1.00 34.27 ? 1197 GLU A C     1 
ATOM   8717  O O     . GLU A  1 1199 ? 10.425  69.359  122.274 1.00 32.73 ? 1197 GLU A O     1 
ATOM   8718  C CB    . GLU A  1 1199 ? 9.301   72.318  123.184 1.00 33.00 ? 1197 GLU A CB    1 
ATOM   8719  C CG    . GLU A  1 1199 ? 7.999   71.555  122.920 1.00 39.57 ? 1197 GLU A CG    1 
ATOM   8720  C CD    . GLU A  1 1199 ? 7.410   70.918  124.177 1.00 49.92 ? 1197 GLU A CD    1 
ATOM   8721  O OE1   . GLU A  1 1199 ? 7.977   71.108  125.281 1.00 51.78 ? 1197 GLU A OE1   1 
ATOM   8722  O OE2   . GLU A  1 1199 ? 6.363   70.237  124.056 1.00 54.72 ? 1197 GLU A OE2   1 
ATOM   8723  N N     . ILE A  1 1200 ? 11.581  71.050  121.341 1.00 31.94 ? 1198 ILE A N     1 
ATOM   8724  C CA    . ILE A  1 1200 ? 11.981  70.222  120.210 1.00 29.18 ? 1198 ILE A CA    1 
ATOM   8725  C C     . ILE A  1 1200 ? 12.850  69.063  120.694 1.00 32.16 ? 1198 ILE A C     1 
ATOM   8726  O O     . ILE A  1 1200 ? 12.745  67.937  120.191 1.00 32.32 ? 1198 ILE A O     1 
ATOM   8727  C CB    . ILE A  1 1200 ? 12.694  71.074  119.137 1.00 29.24 ? 1198 ILE A CB    1 
ATOM   8728  C CG1   . ILE A  1 1200 ? 11.730  72.102  118.532 1.00 30.73 ? 1198 ILE A CG1   1 
ATOM   8729  C CG2   . ILE A  1 1200 ? 13.281  70.187  118.040 1.00 29.08 ? 1198 ILE A CG2   1 
ATOM   8730  C CD1   . ILE A  1 1200 ? 12.398  73.135  117.636 1.00 30.88 ? 1198 ILE A CD1   1 
ATOM   8731  N N     . ALA A  1 1201 ? 13.684  69.307  121.714 1.00 30.77 ? 1199 ALA A N     1 
ATOM   8732  C CA    . ALA A  1 1201 ? 14.533  68.244  122.242 1.00 29.99 ? 1199 ALA A CA    1 
ATOM   8733  C C     . ALA A  1 1201 ? 13.728  67.204  123.016 1.00 34.26 ? 1199 ALA A C     1 
ATOM   8734  O O     . ALA A  1 1201 ? 14.067  66.015  122.980 1.00 34.25 ? 1199 ALA A O     1 
ATOM   8735  C CB    . ALA A  1 1201 ? 15.633  68.830  123.140 1.00 34.27 ? 1199 ALA A CB    1 
ATOM   8736  N N     . ARG A  1 1202 ? 12.670  67.626  123.722 1.00 33.38 ? 1200 ARG A N     1 
ATOM   8737  C CA    . ARG A  1 1202 ? 11.938  66.742  124.623 1.00 31.89 ? 1200 ARG A CA    1 
ATOM   8738  C C     . ARG A  1 1202 ? 10.734  66.068  123.979 1.00 37.79 ? 1200 ARG A C     1 
ATOM   8739  O O     . ARG A  1 1202 ? 10.395  64.940  124.354 1.00 36.56 ? 1200 ARG A O     1 
ATOM   8740  C CB    . ARG A  1 1202 ? 11.453  67.518  125.855 1.00 34.52 ? 1200 ARG A CB    1 
ATOM   8741  C CG    . ARG A  1 1202 ? 12.547  67.924  126.819 1.00 36.46 ? 1200 ARG A CG    1 
ATOM   8742  C CD    . ARG A  1 1202 ? 11.944  68.522  128.080 1.00 37.45 ? 1200 ARG A CD    1 
ATOM   8743  N NE    . ARG A  1 1202 ? 11.028  69.600  127.744 1.00 33.94 ? 1200 ARG A NE    1 
ATOM   8744  C CZ    . ARG A  1 1202 ? 11.348  70.886  127.740 1.00 40.02 ? 1200 ARG A CZ    1 
ATOM   8745  N NH1   . ARG A  1 1202 ? 12.522  71.312  128.184 1.00 35.63 ? 1200 ARG A NH1   1 
ATOM   8746  N NH2   . ARG A  1 1202 ? 10.471  71.769  127.269 1.00 36.59 ? 1200 ARG A NH2   1 
ATOM   8747  N N     . ASN A  1 1203 ? 10.059  66.725  123.041 1.00 32.44 ? 1201 ASN A N     1 
ATOM   8748  C CA    . ASN A  1 1203 ? 8.804   66.203  122.517 1.00 35.18 ? 1201 ASN A CA    1 
ATOM   8749  C C     . ASN A  1 1203 ? 8.922   65.860  121.041 1.00 36.18 ? 1201 ASN A C     1 
ATOM   8750  O O     . ASN A  1 1203 ? 9.014   66.773  120.195 1.00 38.04 ? 1201 ASN A O     1 
ATOM   8751  C CB    . ASN A  1 1203 ? 7.685   67.216  122.748 1.00 37.17 ? 1201 ASN A CB    1 
ATOM   8752  C CG    . ASN A  1 1203 ? 6.351   66.734  122.243 1.00 37.57 ? 1201 ASN A CG    1 
ATOM   8753  O OD1   . ASN A  1 1203 ? 6.225   65.606  121.763 1.00 35.44 ? 1201 ASN A OD1   1 
ATOM   8754  N ND2   . ASN A  1 1203 ? 5.334   67.592  122.345 1.00 35.88 ? 1201 ASN A ND2   1 
ATOM   8755  N N     . PRO A  1 1204 ? 8.869   64.580  120.671 1.00 36.07 ? 1202 PRO A N     1 
ATOM   8756  C CA    . PRO A  1 1204 ? 8.897   64.232  119.242 1.00 35.15 ? 1202 PRO A CA    1 
ATOM   8757  C C     . PRO A  1 1204 ? 7.755   64.852  118.455 1.00 35.23 ? 1202 PRO A C     1 
ATOM   8758  O O     . PRO A  1 1204 ? 7.888   65.051  117.239 1.00 32.39 ? 1202 PRO A O     1 
ATOM   8759  C CB    . PRO A  1 1204 ? 8.800   62.700  119.247 1.00 38.75 ? 1202 PRO A CB    1 
ATOM   8760  C CG    . PRO A  1 1204 ? 8.152   62.368  120.553 1.00 42.80 ? 1202 PRO A CG    1 
ATOM   8761  C CD    . PRO A  1 1204 ? 8.620   63.414  121.532 1.00 36.14 ? 1202 PRO A CD    1 
ATOM   8762  N N     . ASP A  1 1205 ? 6.645   65.179  119.114 1.00 35.65 ? 1203 ASP A N     1 
ATOM   8763  C CA    . ASP A  1 1205 ? 5.499   65.805  118.470 1.00 37.09 ? 1203 ASP A CA    1 
ATOM   8764  C C     . ASP A  1 1205 ? 5.463   67.312  118.680 1.00 33.79 ? 1203 ASP A C     1 
ATOM   8765  O O     . ASP A  1 1205 ? 4.379   67.909  118.615 1.00 33.88 ? 1203 ASP A O     1 
ATOM   8766  C CB    . ASP A  1 1205 ? 4.207   65.176  118.984 1.00 38.04 ? 1203 ASP A CB    1 
ATOM   8767  C CG    . ASP A  1 1205 ? 4.167   63.686  118.754 1.00 46.08 ? 1203 ASP A CG    1 
ATOM   8768  O OD1   . ASP A  1 1205 ? 4.723   63.240  117.727 1.00 47.31 ? 1203 ASP A OD1   1 
ATOM   8769  O OD2   . ASP A  1 1205 ? 3.593   62.966  119.597 1.00 48.77 ? 1203 ASP A OD2   1 
ATOM   8770  N N     . ALA A  1 1206 ? 6.622   67.934  118.932 1.00 33.80 ? 1204 ALA A N     1 
ATOM   8771  C CA    . ALA A  1 1206 ? 6.661   69.374  119.171 1.00 31.22 ? 1204 ALA A CA    1 
ATOM   8772  C C     . ALA A  1 1206 ? 5.950   70.116  118.055 1.00 30.38 ? 1204 ALA A C     1 
ATOM   8773  O O     . ALA A  1 1206 ? 5.167   71.042  118.309 1.00 29.77 ? 1204 ALA A O     1 
ATOM   8774  C CB    . ALA A  1 1206 ? 8.104   69.854  119.294 1.00 33.99 ? 1204 ALA A CB    1 
ATOM   8775  N N     . TYR A  1 1207 ? 6.190   69.702  116.814 1.00 29.06 ? 1205 TYR A N     1 
ATOM   8776  C CA    . TYR A  1 1207 ? 5.429   70.151  115.662 1.00 28.30 ? 1205 TYR A CA    1 
ATOM   8777  C C     . TYR A  1 1207 ? 4.505   69.023  115.236 1.00 30.60 ? 1205 TYR A C     1 
ATOM   8778  O O     . TYR A  1 1207 ? 4.936   67.878  115.110 1.00 34.58 ? 1205 TYR A O     1 
ATOM   8779  C CB    . TYR A  1 1207 ? 6.361   70.536  114.511 1.00 30.47 ? 1205 TYR A CB    1 
ATOM   8780  C CG    . TYR A  1 1207 ? 7.298   71.675  114.848 1.00 28.24 ? 1205 TYR A CG    1 
ATOM   8781  C CD1   . TYR A  1 1207 ? 6.795   72.926  115.195 1.00 28.52 ? 1205 TYR A CD1   1 
ATOM   8782  C CD2   . TYR A  1 1207 ? 8.680   71.505  114.813 1.00 26.90 ? 1205 TYR A CD2   1 
ATOM   8783  C CE1   . TYR A  1 1207 ? 7.647   73.983  115.498 1.00 26.61 ? 1205 TYR A CE1   1 
ATOM   8784  C CE2   . TYR A  1 1207 ? 9.541   72.557  115.118 1.00 29.04 ? 1205 TYR A CE2   1 
ATOM   8785  C CZ    . TYR A  1 1207 ? 9.015   73.788  115.461 1.00 27.74 ? 1205 TYR A CZ    1 
ATOM   8786  O OH    . TYR A  1 1207 ? 9.856   74.831  115.757 1.00 27.13 ? 1205 TYR A OH    1 
ATOM   8787  N N     . CYS A  1 1208 ? 3.244   69.335  115.003 1.00 25.85 ? 1206 CYS A N     1 
ATOM   8788  C CA    . CYS A  1 1208 ? 2.268   68.306  114.696 1.00 29.23 ? 1206 CYS A CA    1 
ATOM   8789  C C     . CYS A  1 1208 ? 2.116   68.194  113.181 1.00 26.85 ? 1206 CYS A C     1 
ATOM   8790  O O     . CYS A  1 1208 ? 1.901   69.200  112.495 1.00 28.32 ? 1206 CYS A O     1 
ATOM   8791  C CB    . CYS A  1 1208 ? 0.937   68.633  115.370 1.00 29.33 ? 1206 CYS A CB    1 
ATOM   8792  S SG    . CYS A  1 1208 ? -0.344  67.417  115.048 1.00 32.91 ? 1206 CYS A SG    1 
ATOM   8793  N N     . LEU A  1 1209 ? 2.247   66.976  112.657 1.00 27.93 ? 1207 LEU A N     1 
ATOM   8794  C CA    . LEU A  1 1209 ? 2.201   66.822  111.207 1.00 23.79 ? 1207 LEU A CA    1 
ATOM   8795  C C     . LEU A  1 1209 ? 0.792   66.954  110.625 1.00 23.76 ? 1207 LEU A C     1 
ATOM   8796  O O     . LEU A  1 1209 ? 0.671   67.114  109.404 1.00 23.63 ? 1207 LEU A O     1 
ATOM   8797  C CB    . LEU A  1 1209 ? 2.822   65.481  110.809 1.00 22.05 ? 1207 LEU A CB    1 
ATOM   8798  C CG    . LEU A  1 1209 ? 4.274   65.268  111.281 1.00 24.12 ? 1207 LEU A CG    1 
ATOM   8799  C CD1   . LEU A  1 1209 ? 4.818   63.998  110.711 1.00 26.41 ? 1207 LEU A CD1   1 
ATOM   8800  C CD2   . LEU A  1 1209 ? 5.193   66.421  110.928 1.00 26.26 ? 1207 LEU A CD2   1 
ATOM   8801  N N     . ASN A  1 1210 ? -0.263  66.906  111.458 1.00 24.87 ? 1208 ASN A N     1 
ATOM   8802  C CA    . ASN A  1 1210 ? -1.633  67.084  110.964 1.00 29.53 ? 1208 ASN A CA    1 
ATOM   8803  C C     . ASN A  1 1210 ? -1.786  68.405  110.225 1.00 26.09 ? 1208 ASN A C     1 
ATOM   8804  O O     . ASN A  1 1210 ? -2.530  68.496  109.237 1.00 23.69 ? 1208 ASN A O     1 
ATOM   8805  C CB    . ASN A  1 1210 ? -2.646  67.063  112.115 1.00 29.42 ? 1208 ASN A CB    1 
ATOM   8806  C CG    . ASN A  1 1210 ? -2.713  65.739  112.842 1.00 31.72 ? 1208 ASN A CG    1 
ATOM   8807  O OD1   . ASN A  1 1210 ? -1.951  64.815  112.570 1.00 35.72 ? 1208 ASN A OD1   1 
ATOM   8808  N ND2   . ASN A  1 1210 ? -3.637  65.652  113.797 1.00 37.08 ? 1208 ASN A ND2   1 
ATOM   8809  N N     . TRP A  1 1211 ? -1.102  69.451  110.703 1.00 25.88 ? 1209 TRP A N     1 
ATOM   8810  C CA    . TRP A  1 1211 ? -1.306  70.800  110.194 1.00 26.59 ? 1209 TRP A CA    1 
ATOM   8811  C C     . TRP A  1 1211 ? -0.339  71.157  109.079 1.00 27.12 ? 1209 TRP A C     1 
ATOM   8812  O O     . TRP A  1 1211 ? -0.337  72.308  108.627 1.00 30.19 ? 1209 TRP A O     1 
ATOM   8813  C CB    . TRP A  1 1211 ? -1.206  71.823  111.352 1.00 23.49 ? 1209 TRP A CB    1 
ATOM   8814  C CG    . TRP A  1 1211 ? -1.836  71.317  112.639 1.00 25.22 ? 1209 TRP A CG    1 
ATOM   8815  C CD1   . TRP A  1 1211 ? -1.247  71.255  113.880 1.00 27.40 ? 1209 TRP A CD1   1 
ATOM   8816  C CD2   . TRP A  1 1211 ? -3.157  70.776  112.799 1.00 26.05 ? 1209 TRP A CD2   1 
ATOM   8817  N NE1   . TRP A  1 1211 ? -2.130  70.721  114.798 1.00 27.40 ? 1209 TRP A NE1   1 
ATOM   8818  C CE2   . TRP A  1 1211 ? -3.302  70.410  114.154 1.00 27.35 ? 1209 TRP A CE2   1 
ATOM   8819  C CE3   . TRP A  1 1211 ? -4.233  70.568  111.925 1.00 27.09 ? 1209 TRP A CE3   1 
ATOM   8820  C CZ2   . TRP A  1 1211 ? -4.479  69.849  114.653 1.00 30.96 ? 1209 TRP A CZ2   1 
ATOM   8821  C CZ3   . TRP A  1 1211 ? -5.395  70.006  112.422 1.00 26.58 ? 1209 TRP A CZ3   1 
ATOM   8822  C CH2   . TRP A  1 1211 ? -5.510  69.642  113.766 1.00 23.82 ? 1209 TRP A CH2   1 
ATOM   8823  N N     . LEU A  1 1212 ? 0.480   70.201  108.636 1.00 22.58 ? 1210 LEU A N     1 
ATOM   8824  C CA    . LEU A  1 1212 ? 1.425   70.388  107.547 1.00 23.20 ? 1210 LEU A CA    1 
ATOM   8825  C C     . LEU A  1 1212 ? 0.993   69.669  106.271 1.00 24.13 ? 1210 LEU A C     1 
ATOM   8826  O O     . LEU A  1 1212 ? 1.739   69.690  105.290 1.00 22.17 ? 1210 LEU A O     1 
ATOM   8827  C CB    . LEU A  1 1212 ? 2.828   69.923  107.970 1.00 22.16 ? 1210 LEU A CB    1 
ATOM   8828  C CG    . LEU A  1 1212 ? 3.466   70.852  109.000 1.00 22.56 ? 1210 LEU A CG    1 
ATOM   8829  C CD1   . LEU A  1 1212 ? 4.594   70.158  109.756 1.00 22.98 ? 1210 LEU A CD1   1 
ATOM   8830  C CD2   . LEU A  1 1212 ? 3.966   72.133  108.320 1.00 23.01 ? 1210 LEU A CD2   1 
ATOM   8831  N N     . VAL A  1 1213 ? -0.194  69.053  106.259 1.00 21.77 ? 1211 VAL A N     1 
ATOM   8832  C CA    . VAL A  1 1213 ? -0.785  68.484  105.051 1.00 23.58 ? 1211 VAL A CA    1 
ATOM   8833  C C     . VAL A  1 1213 ? -2.060  69.248  104.735 1.00 24.70 ? 1211 VAL A C     1 
ATOM   8834  O O     . VAL A  1 1213 ? -2.642  69.920  105.593 1.00 26.56 ? 1211 VAL A O     1 
ATOM   8835  C CB    . VAL A  1 1213 ? -1.092  66.972  105.172 1.00 24.17 ? 1211 VAL A CB    1 
ATOM   8836  C CG1   . VAL A  1 1213 ? 0.190   66.176  105.338 1.00 26.15 ? 1211 VAL A CG1   1 
ATOM   8837  C CG2   . VAL A  1 1213 ? -2.048  66.703  106.317 1.00 24.45 ? 1211 VAL A CG2   1 
ATOM   8838  N N     . GLU A  1 1214 ? -2.506  69.125  103.483 1.00 21.68 ? 1212 GLU A N     1 
ATOM   8839  C CA    . GLU A  1 1214 ? -3.741  69.753  103.028 1.00 26.11 ? 1212 GLU A CA    1 
ATOM   8840  C C     . GLU A  1 1214 ? -4.767  68.672  102.741 1.00 24.11 ? 1212 GLU A C     1 
ATOM   8841  O O     . GLU A  1 1214 ? -4.479  67.715  102.013 1.00 22.89 ? 1212 GLU A O     1 
ATOM   8842  C CB    . GLU A  1 1214 ? -3.538  70.597  101.765 1.00 26.10 ? 1212 GLU A CB    1 
ATOM   8843  C CG    . GLU A  1 1214 ? -4.857  71.277  101.304 1.00 31.30 ? 1212 GLU A CG    1 
ATOM   8844  C CD    . GLU A  1 1214 ? -4.729  72.019  99.982  1.00 39.37 ? 1212 GLU A CD    1 
ATOM   8845  O OE1   . GLU A  1 1214 ? -3.608  72.497  99.680  1.00 40.64 ? 1212 GLU A OE1   1 
ATOM   8846  O OE2   . GLU A  1 1214 ? -5.753  72.129  99.245  1.00 41.16 ? 1212 GLU A OE2   1 
ATOM   8847  N N     . GLU A  1 1215 ? -5.955  68.834  103.318 1.00 22.06 ? 1213 GLU A N     1 
ATOM   8848  C CA    . GLU A  1 1215 ? -7.088  67.965  103.047 1.00 23.16 ? 1213 GLU A CA    1 
ATOM   8849  C C     . GLU A  1 1215 ? -7.775  68.381  101.757 1.00 26.01 ? 1213 GLU A C     1 
ATOM   8850  O O     . GLU A  1 1215 ? -8.026  69.569  101.531 1.00 22.85 ? 1213 GLU A O     1 
ATOM   8851  C CB    . GLU A  1 1215 ? -8.101  68.054  104.183 1.00 22.44 ? 1213 GLU A CB    1 
ATOM   8852  C CG    . GLU A  1 1215 ? -7.630  67.552  105.529 1.00 25.75 ? 1213 GLU A CG    1 
ATOM   8853  C CD    . GLU A  1 1215 ? -8.610  67.968  106.611 1.00 25.70 ? 1213 GLU A CD    1 
ATOM   8854  O OE1   . GLU A  1 1215 ? -8.583  69.150  107.008 1.00 23.99 ? 1213 GLU A OE1   1 
ATOM   8855  O OE2   . GLU A  1 1215 ? -9.430  67.127  107.013 1.00 26.90 ? 1213 GLU A OE2   1 
ATOM   8856  N N     . VAL A  1 1216 ? -8.103  67.396  100.922 1.00 21.82 ? 1214 VAL A N     1 
ATOM   8857  C CA    . VAL A  1 1216 ? -8.859  67.620  99.694  1.00 22.28 ? 1214 VAL A CA    1 
ATOM   8858  C C     . VAL A  1 1216 ? -10.022 66.636  99.659  1.00 19.91 ? 1214 VAL A C     1 
ATOM   8859  O O     . VAL A  1 1216 ? -9.837  65.429  99.868  1.00 21.44 ? 1214 VAL A O     1 
ATOM   8860  C CB    . VAL A  1 1216 ? -7.988  67.476  98.434  1.00 24.38 ? 1214 VAL A CB    1 
ATOM   8861  C CG1   . VAL A  1 1216 ? -8.849  67.608  97.174  1.00 22.31 ? 1214 VAL A CG1   1 
ATOM   8862  C CG2   . VAL A  1 1216 ? -6.896  68.531  98.433  1.00 27.51 ? 1214 VAL A CG2   1 
ATOM   8863  N N     . SER A  1 1217 ? -11.211 67.160  99.422  1.00 20.78 ? 1215 SER A N     1 
ATOM   8864  C CA    . SER A  1 1217 ? -12.429 66.385  99.235  1.00 18.38 ? 1215 SER A CA    1 
ATOM   8865  C C     . SER A  1 1217 ? -12.808 66.442  97.768  1.00 21.04 ? 1215 SER A C     1 
ATOM   8866  O O     . SER A  1 1217 ? -12.700 67.497  97.140  1.00 22.81 ? 1215 SER A O     1 
ATOM   8867  C CB    . SER A  1 1217 ? -13.566 66.953  100.076 1.00 23.05 ? 1215 SER A CB    1 
ATOM   8868  O OG    . SER A  1 1217 ? -14.817 66.417  99.680  1.00 26.21 ? 1215 SER A OG    1 
ATOM   8869  N N     . ALA A  1 1218 ? -13.229 65.312  97.222  1.00 21.72 ? 1216 ALA A N     1 
ATOM   8870  C CA    . ALA A  1 1218 ? -13.683 65.280  95.839  1.00 22.60 ? 1216 ALA A CA    1 
ATOM   8871  C C     . ALA A  1 1218 ? -14.957 64.454  95.781  1.00 21.51 ? 1216 ALA A C     1 
ATOM   8872  O O     . ALA A  1 1218 ? -14.996 63.327  96.282  1.00 23.61 ? 1216 ALA A O     1 
ATOM   8873  C CB    . ALA A  1 1218 ? -12.611 64.701  94.909  1.00 20.12 ? 1216 ALA A CB    1 
ATOM   8874  N N     . SER A  1 1219 ? -15.998 65.032  95.199  1.00 21.11 ? 1217 SER A N     1 
ATOM   8875  C CA    . SER A  1 1219 ? -17.286 64.369  95.037  1.00 22.51 ? 1217 SER A CA    1 
ATOM   8876  C C     . SER A  1 1219 ? -17.550 64.228  93.547  1.00 19.21 ? 1217 SER A C     1 
ATOM   8877  O O     . SER A  1 1219 ? -17.646 65.236  92.839  1.00 22.02 ? 1217 SER A O     1 
ATOM   8878  C CB    . SER A  1 1219 ? -18.408 65.164  95.711  1.00 22.84 ? 1217 SER A CB    1 
ATOM   8879  O OG    . SER A  1 1219 ? -19.605 64.412  95.741  1.00 23.35 ? 1217 SER A OG    1 
ATOM   8880  N N     . ILE A  1 1220 ? -17.678 62.985  93.083  1.00 19.91 ? 1218 ILE A N     1 
ATOM   8881  C CA    . ILE A  1 1220 ? -17.882 62.670  91.668  1.00 20.53 ? 1218 ILE A CA    1 
ATOM   8882  C C     . ILE A  1 1220 ? -19.279 62.092  91.502  1.00 18.61 ? 1218 ILE A C     1 
ATOM   8883  O O     . ILE A  1 1220 ? -19.612 61.078  92.120  1.00 20.21 ? 1218 ILE A O     1 
ATOM   8884  C CB    . ILE A  1 1220 ? -16.834 61.667  91.165  1.00 22.49 ? 1218 ILE A CB    1 
ATOM   8885  C CG1   . ILE A  1 1220 ? -15.436 62.214  91.456  1.00 24.80 ? 1218 ILE A CG1   1 
ATOM   8886  C CG2   . ILE A  1 1220 ? -17.056 61.381  89.668  1.00 25.02 ? 1218 ILE A CG2   1 
ATOM   8887  C CD1   . ILE A  1 1220 ? -14.468 61.156  91.934  1.00 28.79 ? 1218 ILE A CD1   1 
ATOM   8888  N N     . ASN A  1 1221 ? -20.090 62.720  90.655  1.00 22.68 ? 1219 ASN A N     1 
ATOM   8889  C CA    . ASN A  1 1221 ? -21.405 62.175  90.341  1.00 23.32 ? 1219 ASN A CA    1 
ATOM   8890  C C     . ASN A  1 1221 ? -21.201 61.021  89.373  1.00 24.54 ? 1219 ASN A C     1 
ATOM   8891  O O     . ASN A  1 1221 ? -20.885 61.239  88.205  1.00 26.27 ? 1219 ASN A O     1 
ATOM   8892  C CB    . ASN A  1 1221 ? -22.296 63.255  89.741  1.00 22.00 ? 1219 ASN A CB    1 
ATOM   8893  C CG    . ASN A  1 1221 ? -23.658 62.727  89.291  1.00 26.67 ? 1219 ASN A CG    1 
ATOM   8894  O OD1   . ASN A  1 1221 ? -24.043 61.581  89.580  1.00 22.38 ? 1219 ASN A OD1   1 
ATOM   8895  N ND2   . ASN A  1 1221 ? -24.397 63.573  88.580  1.00 27.27 ? 1219 ASN A ND2   1 
ATOM   8896  N N     . THR A  1 1222 ? -21.378 59.794  89.845  1.00 21.97 ? 1220 THR A N     1 
ATOM   8897  C CA    . THR A  1 1222 ? -21.179 58.647  88.966  1.00 25.94 ? 1220 THR A CA    1 
ATOM   8898  C C     . THR A  1 1222 ? -22.467 58.209  88.281  1.00 29.79 ? 1220 THR A C     1 
ATOM   8899  O O     . THR A  1 1222 ? -22.448 57.238  87.522  1.00 31.83 ? 1220 THR A O     1 
ATOM   8900  C CB    . THR A  1 1222 ? -20.568 57.462  89.726  1.00 30.77 ? 1220 THR A CB    1 
ATOM   8901  O OG1   . THR A  1 1222 ? -21.410 57.091  90.817  1.00 26.80 ? 1220 THR A OG1   1 
ATOM   8902  C CG2   . THR A  1 1222 ? -19.172 57.800  90.260  1.00 27.43 ? 1220 THR A CG2   1 
ATOM   8903  N N     . ALA A  1 1223 ? -23.575 58.890  88.537  1.00 24.29 ? 1221 ALA A N     1 
ATOM   8904  C CA    . ALA A  1 1223 ? -24.820 58.672  87.816  1.00 30.60 ? 1221 ALA A CA    1 
ATOM   8905  C C     . ALA A  1 1223 ? -24.937 59.568  86.591  1.00 36.38 ? 1221 ALA A C     1 
ATOM   8906  O O     . ALA A  1 1223 ? -25.979 59.555  85.927  1.00 45.02 ? 1221 ALA A O     1 
ATOM   8907  C CB    . ALA A  1 1223 ? -26.016 58.910  88.746  1.00 28.50 ? 1221 ALA A CB    1 
ATOM   8908  N N     . ALA A  1 1224 ? -23.882 60.328  86.275  1.00 37.20 ? 1222 ALA A N     1 
ATOM   8909  C CA    . ALA A  1 1224 ? -23.994 61.440  85.333  1.00 41.40 ? 1222 ALA A CA    1 
ATOM   8910  C C     . ALA A  1 1224 ? -24.264 60.974  83.905  1.00 44.68 ? 1222 ALA A C     1 
ATOM   8911  O O     . ALA A  1 1224 ? -24.856 61.724  83.121  1.00 45.64 ? 1222 ALA A O     1 
ATOM   8912  C CB    . ALA A  1 1224 ? -22.723 62.291  85.389  1.00 38.19 ? 1222 ALA A CB    1 
ATOM   8913  N N     . ALA A  1 1225 ? -23.849 59.754  83.544  1.00 47.53 ? 1223 ALA A N     1 
ATOM   8914  C CA    . ALA A  1 1225 ? -24.080 59.252  82.191  1.00 47.41 ? 1223 ALA A CA    1 
ATOM   8915  C C     . ALA A  1 1225 ? -25.522 58.812  81.949  1.00 52.97 ? 1223 ALA A C     1 
ATOM   8916  O O     . ALA A  1 1225 ? -25.889 58.552  80.794  1.00 51.34 ? 1223 ALA A O     1 
ATOM   8917  C CB    . ALA A  1 1225 ? -23.129 58.090  81.884  1.00 44.64 ? 1223 ALA A CB    1 
ATOM   8918  N N     . GLY A  1 1226 ? -26.347 58.729  82.993  1.00 49.54 ? 1224 GLY A N     1 
ATOM   8919  C CA    . GLY A  1 1226 ? -27.738 58.353  82.821  1.00 49.91 ? 1224 GLY A CA    1 
ATOM   8920  C C     . GLY A  1 1226 ? -28.139 57.110  83.590  1.00 49.60 ? 1224 GLY A C     1 
ATOM   8921  O O     . GLY A  1 1226 ? -29.267 56.622  83.444  1.00 48.82 ? 1224 GLY A O     1 
ATOM   8922  N N     . GLY A  1 1227 ? -27.232 56.590  84.411  1.00 46.31 ? 1225 GLY A N     1 
ATOM   8923  C CA    . GLY A  1 1227 ? -27.534 55.389  85.172  1.00 47.00 ? 1225 GLY A CA    1 
ATOM   8924  C C     . GLY A  1 1227 ? -26.459 55.091  86.194  1.00 49.35 ? 1225 GLY A C     1 
ATOM   8925  O O     . GLY A  1 1227 ? -25.398 55.725  86.228  1.00 48.65 ? 1225 GLY A O     1 
ATOM   8926  N N     . ASN A  1 1228 ? -26.749 54.089  87.020  1.00 41.86 ? 1226 ASN A N     1 
ATOM   8927  C CA    . ASN A  1 1228 ? -25.891 53.692  88.131  1.00 48.55 ? 1226 ASN A CA    1 
ATOM   8928  C C     . ASN A  1 1228 ? -25.431 52.247  87.923  1.00 51.80 ? 1226 ASN A C     1 
ATOM   8929  O O     . ASN A  1 1228 ? -26.197 51.302  88.142  1.00 50.07 ? 1226 ASN A O     1 
ATOM   8930  C CB    . ASN A  1 1228 ? -26.636 53.860  89.450  1.00 47.36 ? 1226 ASN A CB    1 
ATOM   8931  C CG    . ASN A  1 1228 ? -25.740 53.686  90.654  1.00 48.61 ? 1226 ASN A CG    1 
ATOM   8932  O OD1   . ASN A  1 1228 ? -24.666 53.075  90.573  1.00 50.95 ? 1226 ASN A OD1   1 
ATOM   8933  N ND2   . ASN A  1 1228 ? -26.182 54.216  91.788  1.00 39.51 ? 1226 ASN A ND2   1 
ATOM   8934  N N     . ALA A  1 1229 ? -24.176 52.077  87.513  1.00 48.06 ? 1227 ALA A N     1 
ATOM   8935  C CA    . ALA A  1 1229 ? -23.585 50.747  87.387  1.00 49.86 ? 1227 ALA A CA    1 
ATOM   8936  C C     . ALA A  1 1229 ? -23.233 50.181  88.763  1.00 50.59 ? 1227 ALA A C     1 
ATOM   8937  O O     . ALA A  1 1229 ? -23.462 49.002  89.040  1.00 51.77 ? 1227 ALA A O     1 
ATOM   8938  C CB    . ALA A  1 1229 ? -22.348 50.797  86.498  1.00 47.85 ? 1227 ALA A CB    1 
ATOM   8939  N N     . PRO B  1 17   ? 27.224  5.277   82.972  1.00 55.28 ? 15   PRO B N     1 
ATOM   8940  C CA    . PRO B  1 17   ? 25.793  4.983   83.117  1.00 55.48 ? 15   PRO B CA    1 
ATOM   8941  C C     . PRO B  1 17   ? 24.980  5.414   81.901  1.00 54.80 ? 15   PRO B C     1 
ATOM   8942  O O     . PRO B  1 17   ? 25.076  6.575   81.494  1.00 54.90 ? 15   PRO B O     1 
ATOM   8943  C CB    . PRO B  1 17   ? 25.392  5.795   84.351  1.00 55.25 ? 15   PRO B CB    1 
ATOM   8944  C CG    . PRO B  1 17   ? 26.638  5.892   85.145  1.00 53.89 ? 15   PRO B CG    1 
ATOM   8945  C CD    . PRO B  1 17   ? 27.759  5.990   84.144  1.00 54.29 ? 15   PRO B CD    1 
ATOM   8946  N N     . ALA B  1 18   ? 24.199  4.484   81.344  1.00 54.12 ? 16   ALA B N     1 
ATOM   8947  C CA    . ALA B  1 18   ? 23.376  4.776   80.180  1.00 52.08 ? 16   ALA B CA    1 
ATOM   8948  C C     . ALA B  1 18   ? 22.381  5.893   80.502  1.00 53.07 ? 16   ALA B C     1 
ATOM   8949  O O     . ALA B  1 18   ? 21.907  6.005   81.638  1.00 52.03 ? 16   ALA B O     1 
ATOM   8950  C CB    . ALA B  1 18   ? 22.633  3.522   79.725  1.00 53.00 ? 16   ALA B CB    1 
ATOM   8951  N N     . PRO B  1 19   ? 22.062  6.746   79.527  1.00 49.29 ? 17   PRO B N     1 
ATOM   8952  C CA    . PRO B  1 19   ? 21.182  7.889   79.811  1.00 50.93 ? 17   PRO B CA    1 
ATOM   8953  C C     . PRO B  1 19   ? 19.777  7.428   80.175  1.00 47.41 ? 17   PRO B C     1 
ATOM   8954  O O     . PRO B  1 19   ? 19.185  6.587   79.494  1.00 46.32 ? 17   PRO B O     1 
ATOM   8955  C CB    . PRO B  1 19   ? 21.193  8.688   78.498  1.00 48.06 ? 17   PRO B CB    1 
ATOM   8956  C CG    . PRO B  1 19   ? 22.411  8.207   77.758  1.00 49.68 ? 17   PRO B CG    1 
ATOM   8957  C CD    . PRO B  1 19   ? 22.548  6.762   78.137  1.00 53.19 ? 17   PRO B CD    1 
ATOM   8958  N N     . PHE B  1 20   ? 19.271  7.963   81.286  1.00 48.12 ? 18   PHE B N     1 
ATOM   8959  C CA    . PHE B  1 20   ? 17.884  7.860   81.730  1.00 45.99 ? 18   PHE B CA    1 
ATOM   8960  C C     . PHE B  1 20   ? 17.476  6.453   82.139  1.00 45.64 ? 18   PHE B C     1 
ATOM   8961  O O     . PHE B  1 20   ? 16.283  6.199   82.328  1.00 47.32 ? 18   PHE B O     1 
ATOM   8962  C CB    . PHE B  1 20   ? 16.926  8.389   80.661  1.00 41.10 ? 18   PHE B CB    1 
ATOM   8963  C CG    . PHE B  1 20   ? 17.227  9.794   80.244  1.00 38.72 ? 18   PHE B CG    1 
ATOM   8964  C CD1   . PHE B  1 20   ? 16.923  10.857  81.084  1.00 39.65 ? 18   PHE B CD1   1 
ATOM   8965  C CD2   . PHE B  1 20   ? 17.824  10.057  79.024  1.00 37.86 ? 18   PHE B CD2   1 
ATOM   8966  C CE1   . PHE B  1 20   ? 17.200  12.156  80.710  1.00 37.40 ? 18   PHE B CE1   1 
ATOM   8967  C CE2   . PHE B  1 20   ? 18.107  11.365  78.644  1.00 35.74 ? 18   PHE B CE2   1 
ATOM   8968  C CZ    . PHE B  1 20   ? 17.794  12.405  79.480  1.00 36.97 ? 18   PHE B CZ    1 
ATOM   8969  N N     . ALA B  1 21   ? 18.433  5.536   82.299  1.00 52.50 ? 19   ALA B N     1 
ATOM   8970  C CA    . ALA B  1 21   ? 18.097  4.183   82.727  1.00 50.99 ? 19   ALA B CA    1 
ATOM   8971  C C     . ALA B  1 21   ? 17.445  4.181   84.107  1.00 52.54 ? 19   ALA B C     1 
ATOM   8972  O O     . ALA B  1 21   ? 16.517  3.403   84.358  1.00 58.01 ? 19   ALA B O     1 
ATOM   8973  C CB    . ALA B  1 21   ? 19.350  3.309   82.715  1.00 51.44 ? 19   ALA B CB    1 
ATOM   8974  N N     . ASP B  1 22   ? 17.901  5.054   85.011  1.00 48.46 ? 20   ASP B N     1 
ATOM   8975  C CA    . ASP B  1 22   ? 17.309  5.136   86.343  1.00 42.66 ? 20   ASP B CA    1 
ATOM   8976  C C     . ASP B  1 22   ? 16.672  6.500   86.592  1.00 37.63 ? 20   ASP B C     1 
ATOM   8977  O O     . ASP B  1 22   ? 16.896  7.109   87.641  1.00 36.44 ? 20   ASP B O     1 
ATOM   8978  C CB    . ASP B  1 22   ? 18.362  4.846   87.416  1.00 45.76 ? 20   ASP B CB    1 
ATOM   8979  N N     . PHE B  1 23   ? 15.858  6.982   85.649  1.00 37.90 ? 21   PHE B N     1 
ATOM   8980  C CA    . PHE B  1 23   ? 15.338  8.345   85.756  1.00 33.99 ? 21   PHE B CA    1 
ATOM   8981  C C     . PHE B  1 23   ? 14.438  8.505   86.976  1.00 33.24 ? 21   PHE B C     1 
ATOM   8982  O O     . PHE B  1 23   ? 14.699  9.341   87.851  1.00 29.81 ? 21   PHE B O     1 
ATOM   8983  C CB    . PHE B  1 23   ? 14.586  8.734   84.483  1.00 34.91 ? 21   PHE B CB    1 
ATOM   8984  C CG    . PHE B  1 23   ? 13.975  10.099  84.554  1.00 33.17 ? 21   PHE B CG    1 
ATOM   8985  C CD1   . PHE B  1 23   ? 14.777  11.225  84.637  1.00 29.89 ? 21   PHE B CD1   1 
ATOM   8986  C CD2   . PHE B  1 23   ? 12.598  10.257  84.552  1.00 32.27 ? 21   PHE B CD2   1 
ATOM   8987  C CE1   . PHE B  1 23   ? 14.214  12.488  84.729  1.00 33.80 ? 21   PHE B CE1   1 
ATOM   8988  C CE2   . PHE B  1 23   ? 12.032  11.512  84.635  1.00 33.92 ? 21   PHE B CE2   1 
ATOM   8989  C CZ    . PHE B  1 23   ? 12.841  12.629  84.720  1.00 34.60 ? 21   PHE B CZ    1 
ATOM   8990  N N     . ALA B  1 24   ? 13.349  7.733   87.035  1.00 30.75 ? 22   ALA B N     1 
ATOM   8991  C CA    . ALA B  1 24   ? 12.406  7.801   88.153  1.00 33.95 ? 22   ALA B CA    1 
ATOM   8992  C C     . ALA B  1 24   ? 11.685  6.468   88.312  1.00 34.79 ? 22   ALA B C     1 
ATOM   8993  O O     . ALA B  1 24   ? 10.466  6.376   88.134  1.00 33.47 ? 22   ALA B O     1 
ATOM   8994  C CB    . ALA B  1 24   ? 11.408  8.938   87.951  1.00 31.03 ? 22   ALA B CB    1 
ATOM   8995  N N     . PRO B  1 25   ? 12.408  5.414   88.685  1.00 34.41 ? 23   PRO B N     1 
ATOM   8996  C CA    . PRO B  1 25   ? 11.759  4.119   88.899  1.00 36.21 ? 23   PRO B CA    1 
ATOM   8997  C C     . PRO B  1 25   ? 10.830  4.188   90.097  1.00 37.71 ? 23   PRO B C     1 
ATOM   8998  O O     . PRO B  1 25   ? 11.185  4.768   91.134  1.00 36.07 ? 23   PRO B O     1 
ATOM   8999  C CB    . PRO B  1 25   ? 12.939  3.171   89.157  1.00 34.00 ? 23   PRO B CB    1 
ATOM   9000  C CG    . PRO B  1 25   ? 13.980  4.055   89.767  1.00 34.88 ? 23   PRO B CG    1 
ATOM   9001  C CD    . PRO B  1 25   ? 13.831  5.390   89.076  1.00 30.49 ? 23   PRO B CD    1 
ATOM   9002  N N     . PRO B  1 26   ? 9.623   3.644   89.984  1.00 35.99 ? 24   PRO B N     1 
ATOM   9003  C CA    . PRO B  1 26   ? 8.689   3.676   91.116  1.00 37.60 ? 24   PRO B CA    1 
ATOM   9004  C C     . PRO B  1 26   ? 9.220   2.904   92.318  1.00 37.84 ? 24   PRO B C     1 
ATOM   9005  O O     . PRO B  1 26   ? 10.108  2.056   92.210  1.00 38.48 ? 24   PRO B O     1 
ATOM   9006  C CB    . PRO B  1 26   ? 7.421   3.023   90.551  1.00 37.00 ? 24   PRO B CB    1 
ATOM   9007  C CG    . PRO B  1 26   ? 7.900   2.216   89.370  1.00 41.99 ? 24   PRO B CG    1 
ATOM   9008  C CD    . PRO B  1 26   ? 9.033   3.016   88.793  1.00 37.59 ? 24   PRO B CD    1 
ATOM   9009  N N     . VAL B  1 27   ? 8.658   3.218   93.489  1.00 36.77 ? 25   VAL B N     1 
ATOM   9010  C CA    . VAL B  1 27   ? 8.998   2.469   94.695  1.00 42.27 ? 25   VAL B CA    1 
ATOM   9011  C C     . VAL B  1 27   ? 8.669   0.990   94.513  1.00 40.37 ? 25   VAL B C     1 
ATOM   9012  O O     . VAL B  1 27   ? 9.435   0.112   94.933  1.00 42.66 ? 25   VAL B O     1 
ATOM   9013  C CB    . VAL B  1 27   ? 8.279   3.072   95.920  1.00 39.13 ? 25   VAL B CB    1 
ATOM   9014  C CG1   . VAL B  1 27   ? 8.504   2.204   97.142  1.00 39.47 ? 25   VAL B CG1   1 
ATOM   9015  C CG2   . VAL B  1 27   ? 8.766   4.484   96.182  1.00 35.48 ? 25   VAL B CG2   1 
ATOM   9016  N N     . ARG B  1 28   ? 7.548   0.688   93.867  1.00 37.16 ? 26   ARG B N     1 
ATOM   9017  C CA    . ARG B  1 28   ? 7.133   -0.690  93.637  1.00 40.01 ? 26   ARG B CA    1 
ATOM   9018  C C     . ARG B  1 28   ? 6.334   -0.753  92.345  1.00 40.57 ? 26   ARG B C     1 
ATOM   9019  O O     . ARG B  1 28   ? 5.863   0.278   91.852  1.00 35.34 ? 26   ARG B O     1 
ATOM   9020  C CB    . ARG B  1 28   ? 6.296   -1.227  94.810  1.00 43.87 ? 26   ARG B CB    1 
ATOM   9021  C CG    . ARG B  1 28   ? 4.940   -0.549  94.972  1.00 42.73 ? 26   ARG B CG    1 
ATOM   9022  C CD    . ARG B  1 28   ? 4.315   -0.853  96.329  1.00 46.38 ? 26   ARG B CD    1 
ATOM   9023  N NE    . ARG B  1 28   ? 5.013   -0.182  97.424  1.00 44.73 ? 26   ARG B NE    1 
ATOM   9024  C CZ    . ARG B  1 28   ? 5.770   -0.797  98.323  1.00 48.42 ? 26   ARG B CZ    1 
ATOM   9025  N NH1   . ARG B  1 28   ? 5.953   -2.108  98.291  1.00 46.91 ? 26   ARG B NH1   1 
ATOM   9026  N NH2   . ARG B  1 28   ? 6.349   -0.081  99.284  1.00 44.16 ? 26   ARG B NH2   1 
ATOM   9027  N N     . PRO B  1 29   ? 6.175   -1.943  91.758  1.00 42.55 ? 27   PRO B N     1 
ATOM   9028  C CA    . PRO B  1 29   ? 5.248   -2.070  90.626  1.00 41.35 ? 27   PRO B CA    1 
ATOM   9029  C C     . PRO B  1 29   ? 3.840   -1.655  91.030  1.00 42.03 ? 27   PRO B C     1 
ATOM   9030  O O     . PRO B  1 29   ? 3.351   -1.994  92.111  1.00 44.80 ? 27   PRO B O     1 
ATOM   9031  C CB    . PRO B  1 29   ? 5.324   -3.560  90.264  1.00 43.77 ? 27   PRO B CB    1 
ATOM   9032  C CG    . PRO B  1 29   ? 6.690   -3.987  90.754  1.00 43.93 ? 27   PRO B CG    1 
ATOM   9033  C CD    . PRO B  1 29   ? 6.915   -3.194  92.009  1.00 37.32 ? 27   PRO B CD    1 
ATOM   9034  N N     . GLN B  1 30   ? 3.191   -0.898  90.154  1.00 42.82 ? 28   GLN B N     1 
ATOM   9035  C CA    . GLN B  1 30   ? 1.863   -0.371  90.439  1.00 40.88 ? 28   GLN B CA    1 
ATOM   9036  C C     . GLN B  1 30   ? 0.815   -1.456  90.220  1.00 40.96 ? 28   GLN B C     1 
ATOM   9037  O O     . GLN B  1 30   ? 0.675   -1.980  89.108  1.00 40.55 ? 28   GLN B O     1 
ATOM   9038  C CB    . GLN B  1 30   ? 1.589   0.843   89.557  1.00 42.43 ? 28   GLN B CB    1 
ATOM   9039  C CG    . GLN B  1 30   ? 2.709   1.868   89.610  1.00 34.49 ? 28   GLN B CG    1 
ATOM   9040  C CD    . GLN B  1 30   ? 2.766   2.588   90.933  1.00 37.35 ? 28   GLN B CD    1 
ATOM   9041  O OE1   . GLN B  1 30   ? 1.977   3.495   91.186  1.00 33.34 ? 28   GLN B OE1   1 
ATOM   9042  N NE2   . GLN B  1 30   ? 3.711   2.198   91.787  1.00 37.79 ? 28   GLN B NE2   1 
ATOM   9043  N N     . SER B  1 31   ? 0.085   -1.790  91.280  1.00 38.30 ? 29   SER B N     1 
ATOM   9044  C CA    . SER B  1 31   ? -1.020  -2.728  91.190  1.00 36.78 ? 29   SER B CA    1 
ATOM   9045  C C     . SER B  1 31   ? -2.183  -2.106  90.427  1.00 40.08 ? 29   SER B C     1 
ATOM   9046  O O     . SER B  1 31   ? -2.216  -0.901  90.156  1.00 39.42 ? 29   SER B O     1 
ATOM   9047  C CB    . SER B  1 31   ? -1.489  -3.134  92.583  1.00 43.65 ? 29   SER B CB    1 
ATOM   9048  O OG    . SER B  1 31   ? -2.147  -2.044  93.210  1.00 40.32 ? 29   SER B OG    1 
ATOM   9049  N N     . THR B  1 32   ? -3.161  -2.951  90.088  1.00 39.72 ? 30   THR B N     1 
ATOM   9050  C CA    . THR B  1 32   ? -4.356  -2.447  89.421  1.00 39.72 ? 30   THR B CA    1 
ATOM   9051  C C     . THR B  1 32   ? -5.020  -1.344  90.241  1.00 35.93 ? 30   THR B C     1 
ATOM   9052  O O     . THR B  1 32   ? -5.418  -0.309  89.696  1.00 37.95 ? 30   THR B O     1 
ATOM   9053  C CB    . THR B  1 32   ? -5.324  -3.602  89.153  1.00 44.04 ? 30   THR B CB    1 
ATOM   9054  O OG1   . THR B  1 32   ? -4.698  -4.534  88.264  1.00 47.15 ? 30   THR B OG1   1 
ATOM   9055  C CG2   . THR B  1 32   ? -6.621  -3.105  88.515  1.00 44.30 ? 30   THR B CG2   1 
ATOM   9056  N N     . LEU B  1 33   ? -5.122  -1.535  91.555  1.00 35.20 ? 31   LEU B N     1 
ATOM   9057  C CA    . LEU B  1 33   ? -5.731  -0.518  92.406  1.00 36.09 ? 31   LEU B CA    1 
ATOM   9058  C C     . LEU B  1 33   ? -4.905  0.767   92.441  1.00 36.85 ? 31   LEU B C     1 
ATOM   9059  O O     . LEU B  1 33   ? -5.470  1.865   92.494  1.00 34.07 ? 31   LEU B O     1 
ATOM   9060  C CB    . LEU B  1 33   ? -5.929  -1.075  93.813  1.00 35.44 ? 31   LEU B CB    1 
ATOM   9061  C CG    . LEU B  1 33   ? -7.000  -2.153  93.871  1.00 39.35 ? 31   LEU B CG    1 
ATOM   9062  C CD1   . LEU B  1 33   ? -6.924  -2.914  95.168  1.00 39.35 ? 31   LEU B CD1   1 
ATOM   9063  C CD2   . LEU B  1 33   ? -8.360  -1.498  93.704  1.00 37.47 ? 31   LEU B CD2   1 
ATOM   9064  N N     . ARG B  1 34   ? -3.573  0.660   92.420  1.00 33.81 ? 32   ARG B N     1 
ATOM   9065  C CA    . ARG B  1 34   ? -2.755  1.871   92.406  1.00 36.15 ? 32   ARG B CA    1 
ATOM   9066  C C     . ARG B  1 34   ? -2.883  2.606   91.078  1.00 35.58 ? 32   ARG B C     1 
ATOM   9067  O O     . ARG B  1 34   ? -2.904  3.845   91.043  1.00 31.31 ? 32   ARG B O     1 
ATOM   9068  C CB    . ARG B  1 34   ? -1.293  1.529   92.696  1.00 36.27 ? 32   ARG B CB    1 
ATOM   9069  C CG    . ARG B  1 34   ? -1.045  1.101   94.127  1.00 35.18 ? 32   ARG B CG    1 
ATOM   9070  C CD    . ARG B  1 34   ? -0.997  2.304   95.071  1.00 36.29 ? 32   ARG B CD    1 
ATOM   9071  N NE    . ARG B  1 34   ? 0.072   3.239   94.737  1.00 36.99 ? 32   ARG B NE    1 
ATOM   9072  C CZ    . ARG B  1 34   ? 1.243   3.298   95.358  1.00 38.08 ? 32   ARG B CZ    1 
ATOM   9073  N NH1   . ARG B  1 34   ? 1.546   2.471   96.350  1.00 35.77 ? 32   ARG B NH1   1 
ATOM   9074  N NH2   . ARG B  1 34   ? 2.129   4.218   94.986  1.00 36.37 ? 32   ARG B NH2   1 
ATOM   9075  N N     . ARG B  1 35   ? -2.988  1.861   89.975  1.00 33.26 ? 33   ARG B N     1 
ATOM   9076  C CA    . ARG B  1 35   ? -3.162  2.495   88.671  1.00 34.56 ? 33   ARG B CA    1 
ATOM   9077  C C     . ARG B  1 35   ? -4.487  3.245   88.579  1.00 34.45 ? 33   ARG B C     1 
ATOM   9078  O O     . ARG B  1 35   ? -4.564  4.298   87.940  1.00 31.96 ? 33   ARG B O     1 
ATOM   9079  C CB    . ARG B  1 35   ? -3.089  1.453   87.553  1.00 39.00 ? 33   ARG B CB    1 
ATOM   9080  C CG    . ARG B  1 35   ? -1.747  0.780   87.400  1.00 42.37 ? 33   ARG B CG    1 
ATOM   9081  C CD    . ARG B  1 35   ? -1.741  -0.154  86.192  1.00 45.50 ? 33   ARG B CD    1 
ATOM   9082  N NE    . ARG B  1 35   ? -0.551  -0.994  86.198  1.00 52.10 ? 33   ARG B NE    1 
ATOM   9083  C CZ    . ARG B  1 35   ? 0.669   -0.550  85.932  1.00 55.33 ? 33   ARG B CZ    1 
ATOM   9084  N NH1   . ARG B  1 35   ? 0.884   0.705   85.574  1.00 51.41 ? 33   ARG B NH1   1 
ATOM   9085  N NH2   . ARG B  1 35   ? 1.701   -1.383  86.040  1.00 57.98 ? 33   ARG B NH2   1 
ATOM   9086  N N     . ALA B  1 36   ? -5.552  2.704   89.174  1.00 33.69 ? 34   ALA B N     1 
ATOM   9087  C CA    . ALA B  1 36   ? -6.835  3.397   89.107  1.00 32.41 ? 34   ALA B CA    1 
ATOM   9088  C C     . ALA B  1 36   ? -6.775  4.733   89.844  1.00 31.62 ? 34   ALA B C     1 
ATOM   9089  O O     . ALA B  1 36   ? -7.378  5.722   89.409  1.00 31.16 ? 34   ALA B O     1 
ATOM   9090  C CB    . ALA B  1 36   ? -7.945  2.505   89.658  1.00 34.98 ? 34   ALA B CB    1 
ATOM   9091  N N     . ILE B  1 37   ? -6.026  4.788   90.948  1.00 31.44 ? 35   ILE B N     1 
ATOM   9092  C CA    . ILE B  1 37   ? -5.812  6.050   91.647  1.00 31.58 ? 35   ILE B CA    1 
ATOM   9093  C C     . ILE B  1 37   ? -5.131  7.051   90.730  1.00 30.63 ? 35   ILE B C     1 
ATOM   9094  O O     . ILE B  1 37   ? -5.596  8.184   90.556  1.00 28.48 ? 35   ILE B O     1 
ATOM   9095  C CB    . ILE B  1 37   ? -4.972  5.816   92.915  1.00 31.49 ? 35   ILE B CB    1 
ATOM   9096  C CG1   . ILE B  1 37   ? -5.781  5.062   93.969  1.00 29.95 ? 35   ILE B CG1   1 
ATOM   9097  C CG2   . ILE B  1 37   ? -4.375  7.141   93.434  1.00 26.33 ? 35   ILE B CG2   1 
ATOM   9098  C CD1   . ILE B  1 37   ? -4.920  4.590   95.127  1.00 31.32 ? 35   ILE B CD1   1 
ATOM   9099  N N     . THR B  1 38   ? -3.986  6.650   90.164  1.00 27.87 ? 36   THR B N     1 
ATOM   9100  C CA    . THR B  1 38   ? -3.213  7.535   89.308  1.00 28.05 ? 36   THR B CA    1 
ATOM   9101  C C     . THR B  1 38   ? -4.030  8.000   88.109  1.00 29.14 ? 36   THR B C     1 
ATOM   9102  O O     . THR B  1 38   ? -3.949  9.165   87.706  1.00 29.67 ? 36   THR B O     1 
ATOM   9103  C CB    . THR B  1 38   ? -1.939  6.820   88.860  1.00 33.48 ? 36   THR B CB    1 
ATOM   9104  O OG1   . THR B  1 38   ? -1.196  6.399   90.021  1.00 31.78 ? 36   THR B OG1   1 
ATOM   9105  C CG2   . THR B  1 38   ? -1.082  7.757   88.007  1.00 29.92 ? 36   THR B CG2   1 
ATOM   9106  N N     . ALA B  1 39   ? -4.850  7.111   87.555  1.00 28.12 ? 37   ALA B N     1 
ATOM   9107  C CA    . ALA B  1 39   ? -5.683  7.461   86.408  1.00 31.01 ? 37   ALA B CA    1 
ATOM   9108  C C     . ALA B  1 39   ? -6.687  8.567   86.723  1.00 31.64 ? 37   ALA B C     1 
ATOM   9109  O O     . ALA B  1 39   ? -7.133  9.265   85.805  1.00 30.34 ? 37   ALA B O     1 
ATOM   9110  C CB    . ALA B  1 39   ? -6.418  6.216   85.909  1.00 30.60 ? 37   ALA B CB    1 
ATOM   9111  N N     . ALA B  1 40   ? -7.061  8.748   87.984  1.00 28.47 ? 38   ALA B N     1 
ATOM   9112  C CA    . ALA B  1 40   ? -8.048  9.762   88.319  1.00 30.04 ? 38   ALA B CA    1 
ATOM   9113  C C     . ALA B  1 40   ? -7.418  11.081  88.751  1.00 27.35 ? 38   ALA B C     1 
ATOM   9114  O O     . ALA B  1 40   ? -8.154  12.030  89.043  1.00 27.62 ? 38   ALA B O     1 
ATOM   9115  C CB    . ALA B  1 40   ? -8.980  9.252   89.421  1.00 29.02 ? 38   ALA B CB    1 
ATOM   9116  N N     . TYR B  1 41   ? -6.085  11.160  88.779  1.00 25.96 ? 39   TYR B N     1 
ATOM   9117  C CA    . TYR B  1 41   ? -5.380  12.310  89.340  1.00 26.88 ? 39   TYR B CA    1 
ATOM   9118  C C     . TYR B  1 41   ? -5.998  13.629  88.882  1.00 29.09 ? 39   TYR B C     1 
ATOM   9119  O O     . TYR B  1 41   ? -6.341  14.490  89.701  1.00 26.98 ? 39   TYR B O     1 
ATOM   9120  C CB    . TYR B  1 41   ? -3.904  12.209  88.942  1.00 27.59 ? 39   TYR B CB    1 
ATOM   9121  C CG    . TYR B  1 41   ? -2.917  12.922  89.823  1.00 27.21 ? 39   TYR B CG    1 
ATOM   9122  C CD1   . TYR B  1 41   ? -3.263  14.079  90.516  1.00 25.09 ? 39   TYR B CD1   1 
ATOM   9123  C CD2   . TYR B  1 41   ? -1.611  12.459  89.930  1.00 28.47 ? 39   TYR B CD2   1 
ATOM   9124  C CE1   . TYR B  1 41   ? -2.333  14.742  91.303  1.00 28.02 ? 39   TYR B CE1   1 
ATOM   9125  C CE2   . TYR B  1 41   ? -0.686  13.109  90.718  1.00 26.68 ? 39   TYR B CE2   1 
ATOM   9126  C CZ    . TYR B  1 41   ? -1.049  14.250  91.399  1.00 27.25 ? 39   TYR B CZ    1 
ATOM   9127  O OH    . TYR B  1 41   ? -0.119  14.918  92.162  1.00 27.22 ? 39   TYR B OH    1 
ATOM   9128  N N     . ARG B  1 42   ? -6.206  13.790  87.578  1.00 23.80 ? 40   ARG B N     1 
ATOM   9129  C CA    . ARG B  1 42   ? -6.698  15.072  87.084  1.00 24.41 ? 40   ARG B CA    1 
ATOM   9130  C C     . ARG B  1 42   ? -7.897  14.877  86.181  1.00 25.55 ? 40   ARG B C     1 
ATOM   9131  O O     . ARG B  1 42   ? -8.084  15.615  85.207  1.00 27.62 ? 40   ARG B O     1 
ATOM   9132  C CB    . ARG B  1 42   ? -5.575  15.845  86.391  1.00 28.44 ? 40   ARG B CB    1 
ATOM   9133  C CG    . ARG B  1 42   ? -4.489  16.201  87.404  1.00 26.43 ? 40   ARG B CG    1 
ATOM   9134  C CD    . ARG B  1 42   ? -3.328  16.976  86.867  1.00 28.09 ? 40   ARG B CD    1 
ATOM   9135  N NE    . ARG B  1 42   ? -2.225  16.902  87.816  1.00 27.43 ? 40   ARG B NE    1 
ATOM   9136  C CZ    . ARG B  1 42   ? -2.021  17.760  88.806  1.00 26.36 ? 40   ARG B CZ    1 
ATOM   9137  N NH1   . ARG B  1 42   ? -2.805  18.806  88.984  1.00 22.31 ? 40   ARG B NH1   1 
ATOM   9138  N NH2   . ARG B  1 42   ? -0.978  17.580  89.617  1.00 26.47 ? 40   ARG B NH2   1 
ATOM   9139  N N     . ARG B  1 43   ? -8.740  13.900  86.523  1.00 25.11 ? 41   ARG B N     1 
ATOM   9140  C CA    . ARG B  1 43   ? -9.902  13.569  85.700  1.00 28.82 ? 41   ARG B CA    1 
ATOM   9141  C C     . ARG B  1 43   ? -10.824 14.781  85.584  1.00 28.60 ? 41   ARG B C     1 
ATOM   9142  O O     . ARG B  1 43   ? -11.011 15.511  86.561  1.00 28.74 ? 41   ARG B O     1 
ATOM   9143  C CB    . ARG B  1 43   ? -10.657 12.386  86.313  1.00 29.08 ? 41   ARG B CB    1 
ATOM   9144  C CG    . ARG B  1 43   ? -11.915 11.923  85.592  1.00 29.05 ? 41   ARG B CG    1 
ATOM   9145  C CD    . ARG B  1 43   ? -12.286 10.534  86.091  1.00 31.78 ? 41   ARG B CD    1 
ATOM   9146  N NE    . ARG B  1 43   ? -11.242 9.583   85.725  1.00 33.80 ? 41   ARG B NE    1 
ATOM   9147  C CZ    . ARG B  1 43   ? -10.980 8.454   86.368  1.00 35.11 ? 41   ARG B CZ    1 
ATOM   9148  N NH1   . ARG B  1 43   ? -11.631 8.115   87.469  1.00 32.30 ? 41   ARG B NH1   1 
ATOM   9149  N NH2   . ARG B  1 43   ? -10.036 7.646   85.896  1.00 34.26 ? 41   ARG B NH2   1 
ATOM   9150  N N     . PRO B  1 44   ? -11.402 15.036  84.410  1.00 32.03 ? 42   PRO B N     1 
ATOM   9151  C CA    . PRO B  1 44   ? -12.351 16.152  84.289  1.00 31.93 ? 42   PRO B CA    1 
ATOM   9152  C C     . PRO B  1 44   ? -13.447 16.068  85.348  1.00 28.01 ? 42   PRO B C     1 
ATOM   9153  O O     . PRO B  1 44   ? -13.942 14.991  85.680  1.00 28.26 ? 42   PRO B O     1 
ATOM   9154  C CB    . PRO B  1 44   ? -12.909 15.982  82.868  1.00 32.54 ? 42   PRO B CB    1 
ATOM   9155  C CG    . PRO B  1 44   ? -11.766 15.341  82.120  1.00 35.07 ? 42   PRO B CG    1 
ATOM   9156  C CD    . PRO B  1 44   ? -11.165 14.371  83.116  1.00 32.34 ? 42   PRO B CD    1 
ATOM   9157  N N     . GLU B  1 45   ? -13.813 17.230  85.890  1.00 27.24 ? 43   GLU B N     1 
ATOM   9158  C CA    . GLU B  1 45   ? -14.818 17.291  86.946  1.00 31.49 ? 43   GLU B CA    1 
ATOM   9159  C C     . GLU B  1 45   ? -16.165 16.743  86.484  1.00 31.67 ? 43   GLU B C     1 
ATOM   9160  O O     . GLU B  1 45   ? -16.913 16.167  87.287  1.00 33.49 ? 43   GLU B O     1 
ATOM   9161  C CB    . GLU B  1 45   ? -14.930 18.742  87.435  1.00 32.17 ? 43   GLU B CB    1 
ATOM   9162  C CG    . GLU B  1 45   ? -15.384 18.896  88.868  1.00 29.51 ? 43   GLU B CG    1 
ATOM   9163  C CD    . GLU B  1 45   ? -14.893 20.189  89.524  1.00 27.06 ? 43   GLU B CD    1 
ATOM   9164  O OE1   . GLU B  1 45   ? -14.088 20.939  88.920  1.00 25.78 ? 43   GLU B OE1   1 
ATOM   9165  O OE2   . GLU B  1 45   ? -15.327 20.453  90.666  1.00 28.66 ? 43   GLU B OE2   1 
ATOM   9166  N N     . THR B  1 46   ? -16.492 16.879  85.192  1.00 28.45 ? 44   THR B N     1 
ATOM   9167  C CA    . THR B  1 46   ? -17.744 16.315  84.692  1.00 32.98 ? 44   THR B CA    1 
ATOM   9168  C C     . THR B  1 46   ? -17.722 14.790  84.623  1.00 32.44 ? 44   THR B C     1 
ATOM   9169  O O     . THR B  1 46   ? -18.792 14.173  84.558  1.00 30.21 ? 44   THR B O     1 
ATOM   9170  C CB    . THR B  1 46   ? -18.073 16.866  83.301  1.00 34.82 ? 44   THR B CB    1 
ATOM   9171  O OG1   . THR B  1 46   ? -16.920 16.721  82.462  1.00 33.49 ? 44   THR B OG1   1 
ATOM   9172  C CG2   . THR B  1 46   ? -18.466 18.335  83.374  1.00 29.53 ? 44   THR B CG2   1 
ATOM   9173  N N     . GLU B  1 47   ? -16.542 14.167  84.596  1.00 30.56 ? 45   GLU B N     1 
ATOM   9174  C CA    . GLU B  1 47   ? -16.489 12.712  84.687  1.00 29.01 ? 45   GLU B CA    1 
ATOM   9175  C C     . GLU B  1 47   ? -16.449 12.206  86.126  1.00 31.40 ? 45   GLU B C     1 
ATOM   9176  O O     . GLU B  1 47   ? -16.906 11.092  86.393  1.00 31.29 ? 45   GLU B O     1 
ATOM   9177  C CB    . GLU B  1 47   ? -15.272 12.173  83.934  1.00 34.52 ? 45   GLU B CB    1 
ATOM   9178  C CG    . GLU B  1 47   ? -15.263 12.478  82.438  1.00 37.19 ? 45   GLU B CG    1 
ATOM   9179  C CD    . GLU B  1 47   ? -13.932 12.118  81.814  1.00 44.51 ? 45   GLU B CD    1 
ATOM   9180  O OE1   . GLU B  1 47   ? -13.265 11.202  82.351  1.00 45.28 ? 45   GLU B OE1   1 
ATOM   9181  O OE2   . GLU B  1 47   ? -13.544 12.751  80.810  1.00 41.45 ? 45   GLU B OE2   1 
ATOM   9182  N N     . CYS B  1 48   ? -15.901 12.989  87.058  1.00 30.38 ? 46   CYS B N     1 
ATOM   9183  C CA    . CYS B  1 48   ? -15.838 12.539  88.447  1.00 32.75 ? 46   CYS B CA    1 
ATOM   9184  C C     . CYS B  1 48   ? -17.217 12.501  89.093  1.00 32.08 ? 46   CYS B C     1 
ATOM   9185  O O     . CYS B  1 48   ? -17.521 11.585  89.865  1.00 30.44 ? 46   CYS B O     1 
ATOM   9186  C CB    . CYS B  1 48   ? -14.926 13.452  89.259  1.00 27.47 ? 46   CYS B CB    1 
ATOM   9187  S SG    . CYS B  1 48   ? -13.222 13.471  88.739  1.00 32.55 ? 46   CYS B SG    1 
ATOM   9188  N N     . LEU B  1 49   ? -18.051 13.493  88.816  1.00 29.96 ? 47   LEU B N     1 
ATOM   9189  C CA    . LEU B  1 49   ? -19.232 13.671  89.658  1.00 34.92 ? 47   LEU B CA    1 
ATOM   9190  C C     . LEU B  1 49   ? -20.353 12.645  89.474  1.00 34.18 ? 47   LEU B C     1 
ATOM   9191  O O     . LEU B  1 49   ? -20.978 12.284  90.478  1.00 35.10 ? 47   LEU B O     1 
ATOM   9192  C CB    . LEU B  1 49   ? -19.801 15.084  89.488  1.00 34.42 ? 47   LEU B CB    1 
ATOM   9193  C CG    . LEU B  1 49   ? -19.392 16.047  90.615  1.00 32.20 ? 47   LEU B CG    1 
ATOM   9194  C CD1   . LEU B  1 49   ? -19.936 15.591  91.965  1.00 30.64 ? 47   LEU B CD1   1 
ATOM   9195  C CD2   . LEU B  1 49   ? -17.880 16.161  90.689  1.00 30.74 ? 47   LEU B CD2   1 
ATOM   9196  N N     . PRO B  1 50   ? -20.656 12.146  88.273  1.00 35.67 ? 48   PRO B N     1 
ATOM   9197  C CA    . PRO B  1 50   ? -21.839 11.260  88.126  1.00 36.44 ? 48   PRO B CA    1 
ATOM   9198  C C     . PRO B  1 50   ? -21.745 9.989   88.964  1.00 37.54 ? 48   PRO B C     1 
ATOM   9199  O O     . PRO B  1 50   ? -22.733 9.628   89.621  1.00 35.20 ? 48   PRO B O     1 
ATOM   9200  C CB    . PRO B  1 50   ? -21.880 10.962  86.618  1.00 37.30 ? 48   PRO B CB    1 
ATOM   9201  C CG    . PRO B  1 50   ? -21.283 12.174  86.001  1.00 35.73 ? 48   PRO B CG    1 
ATOM   9202  C CD    . PRO B  1 50   ? -20.169 12.591  86.947  1.00 35.77 ? 48   PRO B CD    1 
ATOM   9203  N N     . PRO B  1 51   ? -20.610 9.269   88.979  1.00 36.38 ? 49   PRO B N     1 
ATOM   9204  C CA    . PRO B  1 51   ? -20.508 8.122   89.907  1.00 37.46 ? 49   PRO B CA    1 
ATOM   9205  C C     . PRO B  1 51   ? -20.567 8.509   91.372  1.00 37.87 ? 49   PRO B C     1 
ATOM   9206  O O     . PRO B  1 51   ? -21.050 7.724   92.201  1.00 40.59 ? 49   PRO B O     1 
ATOM   9207  C CB    . PRO B  1 51   ? -19.146 7.502   89.563  1.00 37.90 ? 49   PRO B CB    1 
ATOM   9208  C CG    . PRO B  1 51   ? -18.384 8.587   88.899  1.00 37.35 ? 49   PRO B CG    1 
ATOM   9209  C CD    . PRO B  1 51   ? -19.414 9.353   88.121  1.00 37.00 ? 49   PRO B CD    1 
ATOM   9210  N N     . LEU B  1 52   ? -20.073 9.688   91.726  1.00 34.04 ? 50   LEU B N     1 
ATOM   9211  C CA    . LEU B  1 52   ? -20.164 10.125  93.112  1.00 37.11 ? 50   LEU B CA    1 
ATOM   9212  C C     . LEU B  1 52   ? -21.612 10.405  93.492  1.00 38.79 ? 50   LEU B C     1 
ATOM   9213  O O     . LEU B  1 52   ? -22.083 9.966   94.547  1.00 39.90 ? 50   LEU B O     1 
ATOM   9214  C CB    . LEU B  1 52   ? -19.294 11.365  93.330  1.00 34.96 ? 50   LEU B CB    1 
ATOM   9215  C CG    . LEU B  1 52   ? -17.773 11.218  93.173  1.00 32.80 ? 50   LEU B CG    1 
ATOM   9216  C CD1   . LEU B  1 52   ? -17.083 12.581  93.346  1.00 27.65 ? 50   LEU B CD1   1 
ATOM   9217  C CD2   . LEU B  1 52   ? -17.234 10.188  94.160  1.00 33.88 ? 50   LEU B CD2   1 
ATOM   9218  N N     . VAL B  1 53   ? -22.334 11.130  92.632  1.00 33.16 ? 51   VAL B N     1 
ATOM   9219  C CA    . VAL B  1 53   ? -23.762 11.363  92.855  1.00 38.42 ? 51   VAL B CA    1 
ATOM   9220  C C     . VAL B  1 53   ? -24.493 10.045  93.071  1.00 41.78 ? 51   VAL B C     1 
ATOM   9221  O O     . VAL B  1 53   ? -25.312 9.912   93.989  1.00 40.03 ? 51   VAL B O     1 
ATOM   9222  C CB    . VAL B  1 53   ? -24.370 12.149  91.679  1.00 37.51 ? 51   VAL B CB    1 
ATOM   9223  C CG1   . VAL B  1 53   ? -25.890 12.258  91.844  1.00 40.41 ? 51   VAL B CG1   1 
ATOM   9224  C CG2   . VAL B  1 53   ? -23.735 13.522  91.595  1.00 37.38 ? 51   VAL B CG2   1 
ATOM   9225  N N     . GLU B  1 54   ? -24.208 9.048   92.231  1.00 39.97 ? 52   GLU B N     1 
ATOM   9226  C CA    . GLU B  1 54   ? -24.910 7.774   92.361  1.00 40.94 ? 52   GLU B CA    1 
ATOM   9227  C C     . GLU B  1 54   ? -24.614 7.119   93.701  1.00 43.31 ? 52   GLU B C     1 
ATOM   9228  O O     . GLU B  1 54   ? -25.528 6.621   94.372  1.00 39.90 ? 52   GLU B O     1 
ATOM   9229  C CB    . GLU B  1 54   ? -24.540 6.843   91.205  1.00 42.04 ? 52   GLU B CB    1 
ATOM   9230  N N     . ALA B  1 55   ? -23.341 7.125   94.121  1.00 39.09 ? 53   ALA B N     1 
ATOM   9231  C CA    . ALA B  1 55   ? -22.976 6.545   95.412  1.00 43.45 ? 53   ALA B CA    1 
ATOM   9232  C C     . ALA B  1 55   ? -23.547 7.337   96.582  1.00 41.62 ? 53   ALA B C     1 
ATOM   9233  O O     . ALA B  1 55   ? -23.857 6.757   97.626  1.00 41.83 ? 53   ALA B O     1 
ATOM   9234  C CB    . ALA B  1 55   ? -21.453 6.456   95.547  1.00 40.68 ? 53   ALA B CB    1 
ATOM   9235  N N     . ALA B  1 56   ? -23.691 8.649   96.441  1.00 40.73 ? 54   ALA B N     1 
ATOM   9236  C CA    . ALA B  1 56   ? -24.165 9.481   97.536  1.00 42.19 ? 54   ALA B CA    1 
ATOM   9237  C C     . ALA B  1 56   ? -25.682 9.579   97.601  1.00 43.32 ? 54   ALA B C     1 
ATOM   9238  O O     . ALA B  1 56   ? -26.202 10.355  98.408  1.00 42.52 ? 54   ALA B O     1 
ATOM   9239  C CB    . ALA B  1 56   ? -23.565 10.880  97.431  1.00 39.49 ? 54   ALA B CB    1 
ATOM   9240  N N     . THR B  1 57   ? -26.401 8.809   96.785  1.00 43.98 ? 55   THR B N     1 
ATOM   9241  C CA    . THR B  1 57   ? -27.856 8.904   96.729  1.00 48.39 ? 55   THR B CA    1 
ATOM   9242  C C     . THR B  1 57   ? -28.489 8.180   97.909  1.00 47.65 ? 55   THR B C     1 
ATOM   9243  O O     . THR B  1 57   ? -28.132 7.037   98.209  1.00 46.50 ? 55   THR B O     1 
ATOM   9244  C CB    . THR B  1 57   ? -28.373 8.320   95.414  1.00 45.87 ? 55   THR B CB    1 
ATOM   9245  O OG1   . THR B  1 57   ? -28.082 9.234   94.348  1.00 45.32 ? 55   THR B OG1   1 
ATOM   9246  C CG2   . THR B  1 57   ? -29.870 8.079   95.479  1.00 50.11 ? 55   THR B CG2   1 
ATOM   9247  N N     . GLN B  1 58   ? -29.425 8.851   98.581  1.00 50.18 ? 56   GLN B N     1 
ATOM   9248  C CA    . GLN B  1 58   ? -30.170 8.266   99.688  1.00 54.36 ? 56   GLN B CA    1 
ATOM   9249  C C     . GLN B  1 58   ? -31.665 8.474   99.473  1.00 53.20 ? 56   GLN B C     1 
ATOM   9250  O O     . GLN B  1 58   ? -32.095 9.497   98.929  1.00 51.78 ? 56   GLN B O     1 
ATOM   9251  C CB    . GLN B  1 58   ? -29.748 8.871   101.031 1.00 52.04 ? 56   GLN B CB    1 
ATOM   9252  N N     . SER B  1 59   ? -32.453 7.497   99.928  1.00 57.89 ? 57   SER B N     1 
ATOM   9253  C CA    . SER B  1 59   ? -33.899 7.506   99.738  1.00 52.73 ? 57   SER B CA    1 
ATOM   9254  C C     . SER B  1 59   ? -34.534 8.744   100.372 1.00 57.32 ? 57   SER B C     1 
ATOM   9255  O O     . SER B  1 59   ? -33.932 9.435   101.198 1.00 57.43 ? 57   SER B O     1 
ATOM   9256  C CB    . SER B  1 59   ? -34.520 6.244   100.337 1.00 57.34 ? 57   SER B CB    1 
ATOM   9257  N N     . LYS B  1 60   ? -35.784 9.013   99.979  1.00 56.35 ? 58   LYS B N     1 
ATOM   9258  C CA    . LYS B  1 60   ? -36.481 10.198  100.474 1.00 57.22 ? 58   LYS B CA    1 
ATOM   9259  C C     . LYS B  1 60   ? -36.715 10.132  101.978 1.00 58.18 ? 58   LYS B C     1 
ATOM   9260  O O     . LYS B  1 60   ? -36.764 11.173  102.643 1.00 59.99 ? 58   LYS B O     1 
ATOM   9261  C CB    . LYS B  1 60   ? -37.813 10.379  99.742  1.00 55.73 ? 58   LYS B CB    1 
ATOM   9262  N N     . GLU B  1 61   ? -36.868 8.929   102.533 1.00 57.45 ? 59   GLU B N     1 
ATOM   9263  C CA    . GLU B  1 61   ? -37.033 8.813   103.978 1.00 56.91 ? 59   GLU B CA    1 
ATOM   9264  C C     . GLU B  1 61   ? -35.752 9.213   104.700 1.00 57.46 ? 59   GLU B C     1 
ATOM   9265  O O     . GLU B  1 61   ? -35.771 10.064  105.599 1.00 58.11 ? 59   GLU B O     1 
ATOM   9266  C CB    . GLU B  1 61   ? -37.455 7.389   104.351 1.00 62.08 ? 59   GLU B CB    1 
ATOM   9267  N N     . ILE B  1 62   ? -34.621 8.619   104.304 1.00 58.31 ? 60   ILE B N     1 
ATOM   9268  C CA    . ILE B  1 62   ? -33.335 8.979   104.899 1.00 53.10 ? 60   ILE B CA    1 
ATOM   9269  C C     . ILE B  1 62   ? -33.053 10.466  104.709 1.00 56.52 ? 60   ILE B C     1 
ATOM   9270  O O     . ILE B  1 62   ? -32.561 11.140  105.623 1.00 56.18 ? 60   ILE B O     1 
ATOM   9271  C CB    . ILE B  1 62   ? -32.212 8.103   104.308 1.00 54.32 ? 60   ILE B CB    1 
ATOM   9272  C CG1   . ILE B  1 62   ? -32.331 6.665   104.817 1.00 54.02 ? 60   ILE B CG1   1 
ATOM   9273  C CG2   . ILE B  1 62   ? -30.826 8.692   104.620 1.00 55.38 ? 60   ILE B CG2   1 
ATOM   9274  C CD1   . ILE B  1 62   ? -31.395 5.694   104.136 1.00 51.86 ? 60   ILE B CD1   1 
ATOM   9275  N N     . ARG B  1 63   ? -33.374 11.005  103.530 1.00 54.83 ? 61   ARG B N     1 
ATOM   9276  C CA    . ARG B  1 63   ? -33.100 12.416  103.261 1.00 57.35 ? 61   ARG B CA    1 
ATOM   9277  C C     . ARG B  1 63   ? -33.920 13.321  104.170 1.00 55.71 ? 61   ARG B C     1 
ATOM   9278  O O     . ARG B  1 63   ? -33.400 14.294  104.728 1.00 56.41 ? 61   ARG B O     1 
ATOM   9279  C CB    . ARG B  1 63   ? -33.380 12.747  101.795 1.00 54.27 ? 61   ARG B CB    1 
ATOM   9280  C CG    . ARG B  1 63   ? -32.237 12.485  100.845 1.00 53.11 ? 61   ARG B CG    1 
ATOM   9281  C CD    . ARG B  1 63   ? -32.614 12.973  99.468  1.00 55.30 ? 61   ARG B CD    1 
ATOM   9282  N NE    . ARG B  1 63   ? -33.408 11.996  98.734  1.00 53.70 ? 61   ARG B NE    1 
ATOM   9283  C CZ    . ARG B  1 63   ? -34.323 12.309  97.828  1.00 56.84 ? 61   ARG B CZ    1 
ATOM   9284  N NH1   . ARG B  1 63   ? -34.668 13.567  97.602  1.00 53.82 ? 61   ARG B NH1   1 
ATOM   9285  N NH2   . ARG B  1 63   ? -34.906 11.337  97.130  1.00 52.64 ? 61   ARG B NH2   1 
ATOM   9286  N N     . ASP B  1 64   ? -35.217 13.028  104.307 1.00 55.05 ? 62   ASP B N     1 
ATOM   9287  C CA    . ASP B  1 64   ? -36.075 13.831  105.174 1.00 57.49 ? 62   ASP B CA    1 
ATOM   9288  C C     . ASP B  1 64   ? -35.593 13.772  106.615 1.00 53.81 ? 62   ASP B C     1 
ATOM   9289  O O     . ASP B  1 64   ? -35.446 14.806  107.275 1.00 52.88 ? 62   ASP B O     1 
ATOM   9290  C CB    . ASP B  1 64   ? -37.526 13.353  105.072 1.00 55.44 ? 62   ASP B CB    1 
ATOM   9291  N N     . ALA B  1 65   ? -35.328 12.563  107.114 1.00 51.93 ? 63   ALA B N     1 
ATOM   9292  C CA    . ALA B  1 65   ? -34.797 12.411  108.465 1.00 53.62 ? 63   ALA B CA    1 
ATOM   9293  C C     . ALA B  1 65   ? -33.481 13.164  108.651 1.00 56.36 ? 63   ALA B C     1 
ATOM   9294  O O     . ALA B  1 65   ? -33.199 13.662  109.750 1.00 51.83 ? 63   ALA B O     1 
ATOM   9295  C CB    . ALA B  1 65   ? -34.612 10.927  108.781 1.00 54.47 ? 63   ALA B CB    1 
ATOM   9296  N N     . ALA B  1 66   ? -32.670 13.269  107.592 1.00 55.63 ? 64   ALA B N     1 
ATOM   9297  C CA    . ALA B  1 66   ? -31.376 13.936  107.712 1.00 54.15 ? 64   ALA B CA    1 
ATOM   9298  C C     . ALA B  1 66   ? -31.546 15.440  107.879 1.00 52.66 ? 64   ALA B C     1 
ATOM   9299  O O     . ALA B  1 66   ? -30.987 16.036  108.806 1.00 52.28 ? 64   ALA B O     1 
ATOM   9300  C CB    . ALA B  1 66   ? -30.504 13.625  106.492 1.00 52.88 ? 64   ALA B CB    1 
ATOM   9301  N N     . ALA B  1 67   ? -32.321 16.072  106.992 1.00 54.98 ? 65   ALA B N     1 
ATOM   9302  C CA    . ALA B  1 67   ? -32.515 17.517  107.064 1.00 56.20 ? 65   ALA B CA    1 
ATOM   9303  C C     . ALA B  1 67   ? -33.205 17.947  108.351 1.00 57.45 ? 65   ALA B C     1 
ATOM   9304  O O     . ALA B  1 67   ? -33.077 19.111  108.751 1.00 56.44 ? 65   ALA B O     1 
ATOM   9305  C CB    . ALA B  1 67   ? -33.325 18.008  105.865 1.00 55.94 ? 65   ALA B CB    1 
ATOM   9306  N N     . SER B  1 68   ? -33.942 17.043  108.999 1.00 57.82 ? 66   SER B N     1 
ATOM   9307  C CA    . SER B  1 68   ? -34.529 17.366  110.294 1.00 59.00 ? 66   SER B CA    1 
ATOM   9308  C C     . SER B  1 68   ? -33.474 17.315  111.389 1.00 55.81 ? 66   SER B C     1 
ATOM   9309  O O     . SER B  1 68   ? -33.340 18.259  112.175 1.00 56.46 ? 66   SER B O     1 
ATOM   9310  C CB    . SER B  1 68   ? -35.689 16.419  110.606 1.00 55.18 ? 66   SER B CB    1 
ATOM   9311  O OG    . SER B  1 68   ? -36.866 16.825  109.927 1.00 65.97 ? 66   SER B OG    1 
ATOM   9312  N N     . THR B  1 69   ? -32.709 16.222  111.444 1.00 57.50 ? 67   THR B N     1 
ATOM   9313  C CA    . THR B  1 69   ? -31.551 16.178  112.331 1.00 53.04 ? 67   THR B CA    1 
ATOM   9314  C C     . THR B  1 69   ? -30.634 17.376  112.102 1.00 53.04 ? 67   THR B C     1 
ATOM   9315  O O     . THR B  1 69   ? -30.137 17.977  113.061 1.00 54.42 ? 67   THR B O     1 
ATOM   9316  C CB    . THR B  1 69   ? -30.784 14.869  112.133 1.00 54.41 ? 67   THR B CB    1 
ATOM   9317  O OG1   . THR B  1 69   ? -31.627 13.759  112.469 1.00 56.53 ? 67   THR B OG1   1 
ATOM   9318  C CG2   . THR B  1 69   ? -29.526 14.838  113.015 1.00 55.71 ? 67   THR B CG2   1 
ATOM   9319  N N     . ALA B  1 70   ? -30.422 17.759  110.838 1.00 55.93 ? 68   ALA B N     1 
ATOM   9320  C CA    . ALA B  1 70   ? -29.529 18.876  110.544 1.00 52.54 ? 68   ALA B CA    1 
ATOM   9321  C C     . ALA B  1 70   ? -30.122 20.205  110.998 1.00 55.18 ? 68   ALA B C     1 
ATOM   9322  O O     . ALA B  1 70   ? -29.394 21.072  111.500 1.00 54.20 ? 68   ALA B O     1 
ATOM   9323  C CB    . ALA B  1 70   ? -29.202 18.919  109.049 1.00 54.84 ? 68   ALA B CB    1 
ATOM   9324  N N     . ARG B  1 71   ? -31.435 20.393  110.823 1.00 57.56 ? 69   ARG B N     1 
ATOM   9325  C CA    . ARG B  1 71   ? -32.072 21.627  111.282 1.00 54.78 ? 69   ARG B CA    1 
ATOM   9326  C C     . ARG B  1 71   ? -32.009 21.750  112.801 1.00 53.03 ? 69   ARG B C     1 
ATOM   9327  O O     . ARG B  1 71   ? -31.777 22.844  113.331 1.00 51.49 ? 69   ARG B O     1 
ATOM   9328  C CB    . ARG B  1 71   ? -33.522 21.688  110.797 1.00 57.78 ? 69   ARG B CB    1 
ATOM   9329  C CG    . ARG B  1 71   ? -34.421 22.632  111.595 1.00 57.54 ? 69   ARG B CG    1 
ATOM   9330  C CD    . ARG B  1 71   ? -35.531 23.228  110.723 1.00 59.54 ? 69   ARG B CD    1 
ATOM   9331  N NE    . ARG B  1 71   ? -35.293 24.641  110.443 1.00 60.26 ? 69   ARG B NE    1 
ATOM   9332  C CZ    . ARG B  1 71   ? -35.707 25.267  109.350 1.00 63.17 ? 69   ARG B CZ    1 
ATOM   9333  N NH1   . ARG B  1 71   ? -36.382 24.631  108.405 1.00 63.24 ? 69   ARG B NH1   1 
ATOM   9334  N NH2   . ARG B  1 71   ? -35.429 26.560  109.197 1.00 60.28 ? 69   ARG B NH2   1 
ATOM   9335  N N     . LYS B  1 72   ? -32.219 20.641  113.516 1.00 53.06 ? 70   LYS B N     1 
ATOM   9336  C CA    . LYS B  1 72   ? -32.093 20.668  114.967 1.00 50.63 ? 70   LYS B CA    1 
ATOM   9337  C C     . LYS B  1 72   ? -30.699 21.127  115.386 1.00 57.17 ? 70   LYS B C     1 
ATOM   9338  O O     . LYS B  1 72   ? -30.550 21.919  116.325 1.00 55.57 ? 70   LYS B O     1 
ATOM   9339  C CB    . LYS B  1 72   ? -32.405 19.288  115.545 1.00 53.92 ? 70   LYS B CB    1 
ATOM   9340  N N     . LEU B  1 73   ? -29.665 20.659  114.682 1.00 56.08 ? 71   LEU B N     1 
ATOM   9341  C CA    . LEU B  1 73   ? -28.297 21.018  115.045 1.00 55.79 ? 71   LEU B CA    1 
ATOM   9342  C C     . LEU B  1 73   ? -28.028 22.498  114.792 1.00 53.06 ? 71   LEU B C     1 
ATOM   9343  O O     . LEU B  1 73   ? -27.440 23.183  115.636 1.00 54.01 ? 71   LEU B O     1 
ATOM   9344  C CB    . LEU B  1 73   ? -27.308 20.138  114.280 1.00 54.44 ? 71   LEU B CB    1 
ATOM   9345  C CG    . LEU B  1 73   ? -27.463 18.643  114.569 1.00 53.42 ? 71   LEU B CG    1 
ATOM   9346  C CD1   . LEU B  1 73   ? -26.752 17.800  113.515 1.00 48.78 ? 71   LEU B CD1   1 
ATOM   9347  C CD2   . LEU B  1 73   ? -26.955 18.321  115.967 1.00 50.45 ? 71   LEU B CD2   1 
ATOM   9348  N N     . ILE B  1 74   ? -28.461 23.013  113.640 1.00 53.08 ? 72   ILE B N     1 
ATOM   9349  C CA    . ILE B  1 74   ? -28.206 24.415  113.325 1.00 53.33 ? 72   ILE B CA    1 
ATOM   9350  C C     . ILE B  1 74   ? -28.982 25.323  114.271 1.00 53.77 ? 72   ILE B C     1 
ATOM   9351  O O     . ILE B  1 74   ? -28.477 26.364  114.711 1.00 53.83 ? 72   ILE B O     1 
ATOM   9352  C CB    . ILE B  1 74   ? -28.537 24.706  111.849 1.00 51.46 ? 72   ILE B CB    1 
ATOM   9353  N N     . GLU B  1 75   ? -30.219 24.950  114.599 1.00 55.04 ? 73   GLU B N     1 
ATOM   9354  C CA    . GLU B  1 75   ? -30.987 25.735  115.560 1.00 57.19 ? 73   GLU B CA    1 
ATOM   9355  C C     . GLU B  1 75   ? -30.287 25.763  116.914 1.00 56.90 ? 73   GLU B C     1 
ATOM   9356  O O     . GLU B  1 75   ? -30.102 26.833  117.510 1.00 55.32 ? 73   GLU B O     1 
ATOM   9357  C CB    . GLU B  1 75   ? -32.405 25.173  115.682 1.00 49.54 ? 73   GLU B CB    1 
ATOM   9358  N N     . ALA B  1 76   ? -29.857 24.593  117.399 1.00 55.42 ? 74   ALA B N     1 
ATOM   9359  C CA    . ALA B  1 76   ? -29.158 24.534  118.680 1.00 55.75 ? 74   ALA B CA    1 
ATOM   9360  C C     . ALA B  1 76   ? -27.877 25.363  118.659 1.00 55.34 ? 74   ALA B C     1 
ATOM   9361  O O     . ALA B  1 76   ? -27.537 26.011  119.656 1.00 56.52 ? 74   ALA B O     1 
ATOM   9362  C CB    . ALA B  1 76   ? -28.855 23.081  119.050 1.00 45.89 ? 74   ALA B CB    1 
ATOM   9363  N N     . LEU B  1 77   ? -27.160 25.370  117.528 1.00 54.16 ? 75   LEU B N     1 
ATOM   9364  C CA    . LEU B  1 77   ? -25.898 26.106  117.457 1.00 55.47 ? 75   LEU B CA    1 
ATOM   9365  C C     . LEU B  1 77   ? -26.134 27.612  117.438 1.00 56.25 ? 75   LEU B C     1 
ATOM   9366  O O     . LEU B  1 77   ? -25.468 28.362  118.161 1.00 57.53 ? 75   LEU B O     1 
ATOM   9367  C CB    . LEU B  1 77   ? -25.088 25.672  116.227 1.00 47.71 ? 75   LEU B CB    1 
ATOM   9368  N N     . ARG B  1 78   ? -27.074 28.078  116.612 1.00 54.07 ? 76   ARG B N     1 
ATOM   9369  C CA    . ARG B  1 78   ? -27.355 29.508  116.534 1.00 57.03 ? 76   ARG B CA    1 
ATOM   9370  C C     . ARG B  1 78   ? -28.033 30.049  117.791 1.00 57.91 ? 76   ARG B C     1 
ATOM   9371  O O     . ARG B  1 78   ? -28.106 31.272  117.959 1.00 54.48 ? 76   ARG B O     1 
ATOM   9372  C CB    . ARG B  1 78   ? -28.221 29.809  115.307 1.00 61.00 ? 76   ARG B CB    1 
ATOM   9373  N N     . GLY B  1 79   ? -28.514 29.179  118.675 1.00 53.74 ? 77   GLY B N     1 
ATOM   9374  C CA    . GLY B  1 79   ? -29.130 29.615  119.913 1.00 58.05 ? 77   GLY B CA    1 
ATOM   9375  C C     . GLY B  1 79   ? -28.192 29.780  121.087 1.00 58.75 ? 77   GLY B C     1 
ATOM   9376  O O     . GLY B  1 79   ? -28.618 30.263  122.143 1.00 53.65 ? 77   GLY B O     1 
ATOM   9377  N N     . LYS B  1 80   ? -26.926 29.400  120.925 1.00 58.73 ? 78   LYS B N     1 
ATOM   9378  C CA    . LYS B  1 80   ? -25.946 29.452  122.002 1.00 56.53 ? 78   LYS B CA    1 
ATOM   9379  C C     . LYS B  1 80   ? -24.617 30.039  121.518 1.00 63.33 ? 78   LYS B C     1 
ATOM   9380  O O     . LYS B  1 80   ? -24.412 31.256  121.537 1.00 62.82 ? 78   LYS B O     1 
ATOM   9381  C CB    . LYS B  1 80   ? -25.729 28.051  122.584 1.00 57.22 ? 78   LYS B CB    1 
ATOM   9382  C CG    . LYS B  1 80   ? -25.158 27.043  121.594 1.00 58.14 ? 78   LYS B CG    1 
ATOM   9383  C CD    . LYS B  1 80   ? -25.160 25.623  122.159 1.00 57.80 ? 78   LYS B CD    1 
ATOM   9384  C CE    . LYS B  1 80   ? -24.373 24.666  121.257 1.00 53.61 ? 78   LYS B CE    1 
ATOM   9385  N NZ    . LYS B  1 80   ? -24.263 23.279  121.809 1.00 50.20 ? 78   LYS B NZ    1 
ATOM   9386  N N     . GLY B  1 85   ? -14.884 35.528  122.547 1.00 53.30 ? 83   GLY B N     1 
ATOM   9387  C CA    . GLY B  1 85   ? -14.884 36.657  123.459 1.00 52.67 ? 83   GLY B CA    1 
ATOM   9388  C C     . GLY B  1 85   ? -14.239 37.896  122.860 1.00 50.71 ? 83   GLY B C     1 
ATOM   9389  O O     . GLY B  1 85   ? -14.168 38.949  123.495 1.00 50.58 ? 83   GLY B O     1 
ATOM   9390  N N     . VAL B  1 86   ? -13.755 37.776  121.625 1.00 51.88 ? 84   VAL B N     1 
ATOM   9391  C CA    . VAL B  1 86   ? -13.153 38.941  120.990 1.00 52.68 ? 84   VAL B CA    1 
ATOM   9392  C C     . VAL B  1 86   ? -14.228 39.947  120.588 1.00 53.78 ? 84   VAL B C     1 
ATOM   9393  O O     . VAL B  1 86   ? -13.979 41.159  120.572 1.00 53.26 ? 84   VAL B O     1 
ATOM   9394  C CB    . VAL B  1 86   ? -12.281 38.512  119.797 1.00 51.39 ? 84   VAL B CB    1 
ATOM   9395  C CG1   . VAL B  1 86   ? -13.124 37.843  118.722 1.00 53.38 ? 84   VAL B CG1   1 
ATOM   9396  C CG2   . VAL B  1 86   ? -11.527 39.708  119.240 1.00 49.25 ? 84   VAL B CG2   1 
ATOM   9397  N N     . GLU B  1 87   ? -15.443 39.474  120.294 1.00 56.89 ? 85   GLU B N     1 
ATOM   9398  C CA    . GLU B  1 87   ? -16.539 40.385  119.973 1.00 55.56 ? 85   GLU B CA    1 
ATOM   9399  C C     . GLU B  1 87   ? -16.952 41.203  121.191 1.00 52.81 ? 85   GLU B C     1 
ATOM   9400  O O     . GLU B  1 87   ? -17.248 42.401  121.075 1.00 48.27 ? 85   GLU B O     1 
ATOM   9401  C CB    . GLU B  1 87   ? -17.730 39.597  119.427 1.00 53.46 ? 85   GLU B CB    1 
ATOM   9402  N N     . GLY B  1 88   ? -16.986 40.574  122.367 1.00 51.92 ? 86   GLY B N     1 
ATOM   9403  C CA    . GLY B  1 88   ? -17.330 41.304  123.575 1.00 52.27 ? 86   GLY B CA    1 
ATOM   9404  C C     . GLY B  1 88   ? -16.292 42.337  123.960 1.00 50.84 ? 86   GLY B C     1 
ATOM   9405  O O     . GLY B  1 88   ? -16.633 43.388  124.512 1.00 49.97 ? 86   GLY B O     1 
ATOM   9406  N N     . LEU B  1 89   ? -15.019 42.058  123.679 1.00 48.18 ? 87   LEU B N     1 
ATOM   9407  C CA    . LEU B  1 89   ? -13.964 43.033  123.934 1.00 48.94 ? 87   LEU B CA    1 
ATOM   9408  C C     . LEU B  1 89   ? -14.076 44.210  122.975 1.00 44.90 ? 87   LEU B C     1 
ATOM   9409  O O     . LEU B  1 89   ? -13.955 45.373  123.379 1.00 43.35 ? 87   LEU B O     1 
ATOM   9410  C CB    . LEU B  1 89   ? -12.594 42.360  123.805 1.00 45.85 ? 87   LEU B CB    1 
ATOM   9411  C CG    . LEU B  1 89   ? -11.411 42.937  124.587 1.00 45.81 ? 87   LEU B CG    1 
ATOM   9412  C CD1   . LEU B  1 89   ? -10.272 41.938  124.572 1.00 52.02 ? 87   LEU B CD1   1 
ATOM   9413  C CD2   . LEU B  1 89   ? -10.946 44.261  124.010 1.00 45.33 ? 87   LEU B CD2   1 
ATOM   9414  N N     . VAL B  1 90   ? -14.297 43.922  121.693 1.00 45.80 ? 88   VAL B N     1 
ATOM   9415  C CA    . VAL B  1 90   ? -14.458 44.982  120.704 1.00 46.76 ? 88   VAL B CA    1 
ATOM   9416  C C     . VAL B  1 90   ? -15.639 45.872  121.071 1.00 48.05 ? 88   VAL B C     1 
ATOM   9417  O O     . VAL B  1 90   ? -15.558 47.105  120.985 1.00 44.04 ? 88   VAL B O     1 
ATOM   9418  C CB    . VAL B  1 90   ? -14.602 44.367  119.299 1.00 43.27 ? 88   VAL B CB    1 
ATOM   9419  C CG1   . VAL B  1 90   ? -15.213 45.360  118.327 1.00 44.04 ? 88   VAL B CG1   1 
ATOM   9420  C CG2   . VAL B  1 90   ? -13.240 43.880  118.799 1.00 45.18 ? 88   VAL B CG2   1 
ATOM   9421  N N     . GLN B  1 91   ? -16.734 45.266  121.547 1.00 47.50 ? 89   GLN B N     1 
ATOM   9422  C CA    . GLN B  1 91   ? -17.919 46.042  121.893 1.00 49.36 ? 89   GLN B CA    1 
ATOM   9423  C C     . GLN B  1 91   ? -17.728 46.807  123.200 1.00 47.83 ? 89   GLN B C     1 
ATOM   9424  O O     . GLN B  1 91   ? -18.186 47.947  123.331 1.00 48.46 ? 89   GLN B O     1 
ATOM   9425  C CB    . GLN B  1 91   ? -19.140 45.123  121.973 1.00 52.52 ? 89   GLN B CB    1 
ATOM   9426  N N     . GLU B  1 92   ? -17.056 46.202  124.182 1.00 47.58 ? 90   GLU B N     1 
ATOM   9427  C CA    . GLU B  1 92   ? -16.866 46.881  125.461 1.00 45.71 ? 90   GLU B CA    1 
ATOM   9428  C C     . GLU B  1 92   ? -16.053 48.160  125.298 1.00 45.09 ? 90   GLU B C     1 
ATOM   9429  O O     . GLU B  1 92   ? -16.367 49.189  125.909 1.00 41.25 ? 90   GLU B O     1 
ATOM   9430  C CB    . GLU B  1 92   ? -16.193 45.944  126.470 1.00 46.67 ? 90   GLU B CB    1 
ATOM   9431  C CG    . GLU B  1 92   ? -15.870 46.615  127.806 1.00 51.54 ? 90   GLU B CG    1 
ATOM   9432  C CD    . GLU B  1 92   ? -15.315 45.659  128.862 1.00 47.57 ? 90   GLU B CD    1 
ATOM   9433  O OE1   . GLU B  1 92   ? -15.083 44.468  128.551 1.00 49.59 ? 90   GLU B OE1   1 
ATOM   9434  O OE2   . GLU B  1 92   ? -15.112 46.111  130.008 1.00 49.81 ? 90   GLU B OE2   1 
ATOM   9435  N N     . TYR B  1 93   ? -15.014 48.128  124.473 1.00 43.06 ? 91   TYR B N     1 
ATOM   9436  C CA    . TYR B  1 93   ? -14.166 49.298  124.311 1.00 43.38 ? 91   TYR B CA    1 
ATOM   9437  C C     . TYR B  1 93   ? -14.414 50.030  123.001 1.00 41.50 ? 91   TYR B C     1 
ATOM   9438  O O     . TYR B  1 93   ? -13.655 50.949  122.668 1.00 39.33 ? 91   TYR B O     1 
ATOM   9439  C CB    . TYR B  1 93   ? -12.698 48.898  124.444 1.00 39.64 ? 91   TYR B CB    1 
ATOM   9440  C CG    . TYR B  1 93   ? -12.351 48.571  125.874 1.00 41.34 ? 91   TYR B CG    1 
ATOM   9441  C CD1   . TYR B  1 93   ? -11.942 49.569  126.751 1.00 41.60 ? 91   TYR B CD1   1 
ATOM   9442  C CD2   . TYR B  1 93   ? -12.469 47.277  126.361 1.00 44.72 ? 91   TYR B CD2   1 
ATOM   9443  C CE1   . TYR B  1 93   ? -11.643 49.284  128.068 1.00 42.64 ? 91   TYR B CE1   1 
ATOM   9444  C CE2   . TYR B  1 93   ? -12.172 46.982  127.689 1.00 43.77 ? 91   TYR B CE2   1 
ATOM   9445  C CZ    . TYR B  1 93   ? -11.757 47.992  128.529 1.00 43.01 ? 91   TYR B CZ    1 
ATOM   9446  O OH    . TYR B  1 93   ? -11.454 47.719  129.840 1.00 45.09 ? 91   TYR B OH    1 
ATOM   9447  N N     . SER B  1 94   ? -15.464 49.658  122.268 1.00 41.59 ? 92   SER B N     1 
ATOM   9448  C CA    . SER B  1 94   ? -15.827 50.315  121.013 1.00 37.58 ? 92   SER B CA    1 
ATOM   9449  C C     . SER B  1 94   ? -14.624 50.396  120.077 1.00 38.89 ? 92   SER B C     1 
ATOM   9450  O O     . SER B  1 94   ? -14.248 51.464  119.585 1.00 37.56 ? 92   SER B O     1 
ATOM   9451  C CB    . SER B  1 94   ? -16.415 51.700  121.274 1.00 39.19 ? 92   SER B CB    1 
ATOM   9452  O OG    . SER B  1 94   ? -17.621 51.604  122.015 1.00 44.29 ? 92   SER B OG    1 
ATOM   9453  N N     . LEU B  1 95   ? -14.011 49.240  119.847 1.00 36.64 ? 93   LEU B N     1 
ATOM   9454  C CA    . LEU B  1 95   ? -12.837 49.149  119.002 1.00 34.40 ? 93   LEU B CA    1 
ATOM   9455  C C     . LEU B  1 95   ? -13.243 49.018  117.545 1.00 34.70 ? 93   LEU B C     1 
ATOM   9456  O O     . LEU B  1 95   ? -14.219 48.342  117.210 1.00 35.67 ? 93   LEU B O     1 
ATOM   9457  C CB    . LEU B  1 95   ? -11.968 47.951  119.395 1.00 34.60 ? 93   LEU B CB    1 
ATOM   9458  C CG    . LEU B  1 95   ? -11.433 47.875  120.825 1.00 38.02 ? 93   LEU B CG    1 
ATOM   9459  C CD1   . LEU B  1 95   ? -10.506 46.675  120.968 1.00 36.84 ? 93   LEU B CD1   1 
ATOM   9460  C CD2   . LEU B  1 95   ? -10.712 49.155  121.211 1.00 33.41 ? 93   LEU B CD2   1 
ATOM   9461  N N     . SER B  1 96   ? -12.482 49.676  116.681 1.00 30.79 ? 94   SER B N     1 
ATOM   9462  C CA    . SER B  1 96   ? -12.558 49.390  115.268 1.00 31.26 ? 94   SER B CA    1 
ATOM   9463  C C     . SER B  1 96   ? -11.884 48.051  114.999 1.00 34.99 ? 94   SER B C     1 
ATOM   9464  O O     . SER B  1 96   ? -11.191 47.496  115.857 1.00 33.84 ? 94   SER B O     1 
ATOM   9465  C CB    . SER B  1 96   ? -11.893 50.507  114.471 1.00 33.96 ? 94   SER B CB    1 
ATOM   9466  O OG    . SER B  1 96   ? -10.494 50.507  114.701 1.00 29.86 ? 94   SER B OG    1 
ATOM   9467  N N     . SER B  1 97   ? -12.089 47.524  113.793 1.00 28.57 ? 95   SER B N     1 
ATOM   9468  C CA    . SER B  1 97   ? -11.413 46.287  113.418 1.00 32.34 ? 95   SER B CA    1 
ATOM   9469  C C     . SER B  1 97   ? -9.897  46.442  113.501 1.00 34.90 ? 95   SER B C     1 
ATOM   9470  O O     . SER B  1 97   ? -9.209  45.601  114.093 1.00 29.28 ? 95   SER B O     1 
ATOM   9471  C CB    . SER B  1 97   ? -11.834 45.869  112.009 1.00 32.97 ? 95   SER B CB    1 
ATOM   9472  O OG    . SER B  1 97   ? -13.241 45.713  111.966 1.00 40.23 ? 95   SER B OG    1 
ATOM   9473  N N     . GLN B  1 98   ? -9.359  47.519  112.915 1.00 29.60 ? 96   GLN B N     1 
ATOM   9474  C CA    . GLN B  1 98   ? -7.917  47.742  112.975 1.00 29.75 ? 96   GLN B CA    1 
ATOM   9475  C C     . GLN B  1 98   ? -7.449  47.891  114.417 1.00 28.16 ? 96   GLN B C     1 
ATOM   9476  O O     . GLN B  1 98   ? -6.354  47.442  114.768 1.00 27.87 ? 96   GLN B O     1 
ATOM   9477  C CB    . GLN B  1 98   ? -7.525  48.979  112.162 1.00 26.64 ? 96   GLN B CB    1 
ATOM   9478  C CG    . GLN B  1 98   ? -7.487  48.759  110.650 1.00 29.86 ? 96   GLN B CG    1 
ATOM   9479  C CD    . GLN B  1 98   ? -6.522  47.664  110.264 1.00 31.84 ? 96   GLN B CD    1 
ATOM   9480  O OE1   . GLN B  1 98   ? -6.844  46.486  110.368 1.00 34.50 ? 96   GLN B OE1   1 
ATOM   9481  N NE2   . GLN B  1 98   ? -5.325  48.046  109.812 1.00 29.01 ? 96   GLN B NE2   1 
ATOM   9482  N N     . GLU B  1 99   ? -8.261  48.523  115.268 1.00 29.10 ? 97   GLU B N     1 
ATOM   9483  C CA    . GLU B  1 99   ? -7.864  48.624  116.669 1.00 31.50 ? 97   GLU B CA    1 
ATOM   9484  C C     . GLU B  1 99   ? -7.890  47.259  117.335 1.00 31.40 ? 97   GLU B C     1 
ATOM   9485  O O     . GLU B  1 99   ? -7.030  46.951  118.157 1.00 31.27 ? 97   GLU B O     1 
ATOM   9486  C CB    . GLU B  1 99   ? -8.765  49.602  117.423 1.00 30.50 ? 97   GLU B CB    1 
ATOM   9487  C CG    . GLU B  1 99   ? -8.338  51.041  117.273 1.00 27.87 ? 97   GLU B CG    1 
ATOM   9488  C CD    . GLU B  1 99   ? -9.442  52.020  117.652 1.00 32.36 ? 97   GLU B CD    1 
ATOM   9489  O OE1   . GLU B  1 99   ? -10.490 51.574  118.172 1.00 33.62 ? 97   GLU B OE1   1 
ATOM   9490  O OE2   . GLU B  1 99   ? -9.257  53.236  117.424 1.00 33.74 ? 97   GLU B OE2   1 
ATOM   9491  N N     . GLY B  1 100  ? -8.864  46.425  116.983 1.00 29.70 ? 98   GLY B N     1 
ATOM   9492  C CA    . GLY B  1 100  ? -8.918  45.100  117.568 1.00 32.36 ? 98   GLY B CA    1 
ATOM   9493  C C     . GLY B  1 100  ? -7.747  44.245  117.132 1.00 30.91 ? 98   GLY B C     1 
ATOM   9494  O O     . GLY B  1 100  ? -7.154  43.532  117.946 1.00 29.24 ? 98   GLY B O     1 
ATOM   9495  N N     . VAL B  1 101  ? -7.375  44.328  115.851 1.00 26.98 ? 99   VAL B N     1 
ATOM   9496  C CA    . VAL B  1 101  ? -6.206  43.599  115.370 1.00 29.97 ? 99   VAL B CA    1 
ATOM   9497  C C     . VAL B  1 101  ? -4.946  44.102  116.060 1.00 29.61 ? 99   VAL B C     1 
ATOM   9498  O O     . VAL B  1 101  ? -4.090  43.312  116.487 1.00 29.97 ? 99   VAL B O     1 
ATOM   9499  C CB    . VAL B  1 101  ? -6.098  43.726  113.839 1.00 28.26 ? 99   VAL B CB    1 
ATOM   9500  C CG1   . VAL B  1 101  ? -4.783  43.134  113.336 1.00 29.02 ? 99   VAL B CG1   1 
ATOM   9501  C CG2   . VAL B  1 101  ? -7.287  43.058  113.191 1.00 30.53 ? 99   VAL B CG2   1 
ATOM   9502  N N     . ALA B  1 102  ? -4.810  45.423  116.172 1.00 27.35 ? 100  ALA B N     1 
ATOM   9503  C CA    . ALA B  1 102  ? -3.619  46.008  116.775 1.00 27.79 ? 100  ALA B CA    1 
ATOM   9504  C C     . ALA B  1 102  ? -3.485  45.597  118.228 1.00 32.09 ? 100  ALA B C     1 
ATOM   9505  O O     . ALA B  1 102  ? -2.379  45.313  118.702 1.00 30.21 ? 100  ALA B O     1 
ATOM   9506  C CB    . ALA B  1 102  ? -3.665  47.534  116.674 1.00 27.27 ? 100  ALA B CB    1 
ATOM   9507  N N     . LEU B  1 103  ? -4.603  45.565  118.951 1.00 28.65 ? 101  LEU B N     1 
ATOM   9508  C CA    . LEU B  1 103  ? -4.558  45.207  120.360 1.00 30.35 ? 101  LEU B CA    1 
ATOM   9509  C C     . LEU B  1 103  ? -4.107  43.763  120.545 1.00 30.10 ? 101  LEU B C     1 
ATOM   9510  O O     . LEU B  1 103  ? -3.306  43.462  121.444 1.00 29.65 ? 101  LEU B O     1 
ATOM   9511  C CB    . LEU B  1 103  ? -5.929  45.442  120.996 1.00 27.87 ? 101  LEU B CB    1 
ATOM   9512  C CG    . LEU B  1 103  ? -6.110  45.107  122.478 1.00 30.82 ? 101  LEU B CG    1 
ATOM   9513  C CD1   . LEU B  1 103  ? -5.292  46.018  123.401 1.00 31.85 ? 101  LEU B CD1   1 
ATOM   9514  C CD2   . LEU B  1 103  ? -7.574  45.194  122.824 1.00 33.22 ? 101  LEU B CD2   1 
ATOM   9515  N N     . MET B  1 104  ? -4.609  42.856  119.706 1.00 27.37 ? 102  MET B N     1 
ATOM   9516  C CA    . MET B  1 104  ? -4.195  41.456  119.812 1.00 30.71 ? 102  MET B CA    1 
ATOM   9517  C C     . MET B  1 104  ? -2.720  41.277  119.457 1.00 33.29 ? 102  MET B C     1 
ATOM   9518  O O     . MET B  1 104  ? -2.021  40.456  120.067 1.00 30.33 ? 102  MET B O     1 
ATOM   9519  C CB    . MET B  1 104  ? -5.088  40.585  118.925 1.00 30.16 ? 102  MET B CB    1 
ATOM   9520  C CG    . MET B  1 104  ? -6.570  40.693  119.316 1.00 28.73 ? 102  MET B CG    1 
ATOM   9521  S SD    . MET B  1 104  ? -6.870  40.249  121.042 1.00 40.28 ? 102  MET B SD    1 
ATOM   9522  C CE    . MET B  1 104  ? -6.397  38.525  121.006 1.00 42.83 ? 102  MET B CE    1 
ATOM   9523  N N     . CYS B  1 105  ? -2.220  42.043  118.488 1.00 27.81 ? 103  CYS B N     1 
ATOM   9524  C CA    . CYS B  1 105  ? -0.787  42.009  118.211 1.00 31.06 ? 103  CYS B CA    1 
ATOM   9525  C C     . CYS B  1 105  ? 0.005   42.474  119.422 1.00 30.08 ? 103  CYS B C     1 
ATOM   9526  O O     . CYS B  1 105  ? 1.012   41.861  119.790 1.00 31.13 ? 103  CYS B O     1 
ATOM   9527  C CB    . CYS B  1 105  ? -0.453  42.879  117.006 1.00 26.24 ? 103  CYS B CB    1 
ATOM   9528  S SG    . CYS B  1 105  ? -1.104  42.248  115.445 1.00 30.27 ? 103  CYS B SG    1 
ATOM   9529  N N     . LEU B  1 106  ? -0.427  43.578  120.038 1.00 29.50 ? 104  LEU B N     1 
ATOM   9530  C CA    . LEU B  1 106  ? 0.221   44.042  121.258 1.00 29.90 ? 104  LEU B CA    1 
ATOM   9531  C C     . LEU B  1 106  ? 0.163   42.979  122.342 1.00 33.56 ? 104  LEU B C     1 
ATOM   9532  O O     . LEU B  1 106  ? 1.153   42.748  123.053 1.00 30.94 ? 104  LEU B O     1 
ATOM   9533  C CB    . LEU B  1 106  ? -0.440  45.325  121.757 1.00 30.62 ? 104  LEU B CB    1 
ATOM   9534  C CG    . LEU B  1 106  ? 0.063   45.691  123.153 1.00 33.24 ? 104  LEU B CG    1 
ATOM   9535  C CD1   . LEU B  1 106  ? 1.531   46.123  123.108 1.00 29.56 ? 104  LEU B CD1   1 
ATOM   9536  C CD2   . LEU B  1 106  ? -0.801  46.752  123.777 1.00 30.26 ? 104  LEU B CD2   1 
ATOM   9537  N N     . ALA B  1 107  ? -0.993  42.324  122.487 1.00 31.76 ? 105  ALA B N     1 
ATOM   9538  C CA    . ALA B  1 107  ? -1.146  41.326  123.545 1.00 32.16 ? 105  ALA B CA    1 
ATOM   9539  C C     . ALA B  1 107  ? -0.258  40.112  123.291 1.00 33.42 ? 105  ALA B C     1 
ATOM   9540  O O     . ALA B  1 107  ? 0.342   39.567  124.224 1.00 33.99 ? 105  ALA B O     1 
ATOM   9541  C CB    . ALA B  1 107  ? -2.604  40.901  123.651 1.00 31.48 ? 105  ALA B CB    1 
ATOM   9542  N N     . GLU B  1 108  ? -0.183  39.672  122.034 1.00 32.93 ? 106  GLU B N     1 
ATOM   9543  C CA    . GLU B  1 108  ? 0.724   38.601  121.639 1.00 34.15 ? 106  GLU B CA    1 
ATOM   9544  C C     . GLU B  1 108  ? 2.162   38.924  122.023 1.00 38.35 ? 106  GLU B C     1 
ATOM   9545  O O     . GLU B  1 108  ? 2.887   38.065  122.543 1.00 36.87 ? 106  GLU B O     1 
ATOM   9546  C CB    . GLU B  1 108  ? 0.610   38.375  120.127 1.00 34.65 ? 106  GLU B CB    1 
ATOM   9547  C CG    . GLU B  1 108  ? 1.617   37.396  119.537 1.00 37.24 ? 106  GLU B CG    1 
ATOM   9548  C CD    . GLU B  1 108  ? 1.831   37.602  118.045 1.00 39.08 ? 106  GLU B CD    1 
ATOM   9549  O OE1   . GLU B  1 108  ? 0.948   38.201  117.387 1.00 35.11 ? 106  GLU B OE1   1 
ATOM   9550  O OE2   . GLU B  1 108  ? 2.889   37.168  117.527 1.00 40.40 ? 106  GLU B OE2   1 
ATOM   9551  N N     . ALA B  1 109  ? 2.599   40.157  121.765 1.00 34.94 ? 107  ALA B N     1 
ATOM   9552  C CA    . ALA B  1 109  ? 3.960   40.530  122.126 1.00 39.29 ? 107  ALA B CA    1 
ATOM   9553  C C     . ALA B  1 109  ? 4.134   40.549  123.636 1.00 39.27 ? 107  ALA B C     1 
ATOM   9554  O O     . ALA B  1 109  ? 5.178   40.129  124.155 1.00 40.36 ? 107  ALA B O     1 
ATOM   9555  C CB    . ALA B  1 109  ? 4.315   41.890  121.529 1.00 36.22 ? 107  ALA B CB    1 
ATOM   9556  N N     . LEU B  1 110  ? 3.123   41.037  124.358 1.00 31.88 ? 108  LEU B N     1 
ATOM   9557  C CA    . LEU B  1 110  ? 3.219   41.072  125.814 1.00 37.08 ? 108  LEU B CA    1 
ATOM   9558  C C     . LEU B  1 110  ? 3.300   39.670  126.403 1.00 39.09 ? 108  LEU B C     1 
ATOM   9559  O O     . LEU B  1 110  ? 3.926   39.471  127.453 1.00 42.49 ? 108  LEU B O     1 
ATOM   9560  C CB    . LEU B  1 110  ? 2.033   41.834  126.411 1.00 34.04 ? 108  LEU B CB    1 
ATOM   9561  C CG    . LEU B  1 110  ? 2.180   43.353  126.277 1.00 36.50 ? 108  LEU B CG    1 
ATOM   9562  C CD1   . LEU B  1 110  ? 0.931   44.075  126.749 1.00 32.51 ? 108  LEU B CD1   1 
ATOM   9563  C CD2   . LEU B  1 110  ? 3.419   43.824  127.040 1.00 39.22 ? 108  LEU B CD2   1 
ATOM   9564  N N     . LEU B  1 111  ? 2.682   38.692  125.746 1.00 36.43 ? 109  LEU B N     1 
ATOM   9565  C CA    . LEU B  1 111  ? 2.723   37.314  126.214 1.00 40.99 ? 109  LEU B CA    1 
ATOM   9566  C C     . LEU B  1 111  ? 4.052   36.623  125.929 1.00 43.52 ? 109  LEU B C     1 
ATOM   9567  O O     . LEU B  1 111  ? 4.296   35.544  126.473 1.00 43.14 ? 109  LEU B O     1 
ATOM   9568  C CB    . LEU B  1 111  ? 1.573   36.525  125.597 1.00 39.36 ? 109  LEU B CB    1 
ATOM   9569  C CG    . LEU B  1 111  ? 0.220   36.965  126.159 1.00 37.25 ? 109  LEU B CG    1 
ATOM   9570  C CD1   . LEU B  1 111  ? -0.917  36.317  125.425 1.00 38.70 ? 109  LEU B CD1   1 
ATOM   9571  C CD2   . LEU B  1 111  ? 0.129   36.646  127.631 1.00 45.33 ? 109  LEU B CD2   1 
ATOM   9572  N N     . ARG B  1 112  ? 4.917   37.215  125.105 1.00 43.10 ? 110  ARG B N     1 
ATOM   9573  C CA    . ARG B  1 112  ? 6.274   36.698  124.969 1.00 43.42 ? 110  ARG B CA    1 
ATOM   9574  C C     . ARG B  1 112  ? 7.139   37.022  126.182 1.00 46.13 ? 110  ARG B C     1 
ATOM   9575  O O     . ARG B  1 112  ? 8.265   36.525  126.270 1.00 44.86 ? 110  ARG B O     1 
ATOM   9576  C CB    . ARG B  1 112  ? 6.924   37.238  123.689 1.00 41.82 ? 110  ARG B CB    1 
ATOM   9577  C CG    . ARG B  1 112  ? 6.189   36.844  122.402 1.00 43.59 ? 110  ARG B CG    1 
ATOM   9578  C CD    . ARG B  1 112  ? 7.037   37.062  121.140 1.00 50.21 ? 110  ARG B CD    1 
ATOM   9579  N NE    . ARG B  1 112  ? 7.431   38.455  120.955 1.00 50.36 ? 110  ARG B NE    1 
ATOM   9580  C CZ    . ARG B  1 112  ? 6.825   39.315  120.146 1.00 53.44 ? 110  ARG B CZ    1 
ATOM   9581  N NH1   . ARG B  1 112  ? 5.792   38.955  119.396 1.00 51.42 ? 110  ARG B NH1   1 
ATOM   9582  N NH2   . ARG B  1 112  ? 7.269   40.570  120.082 1.00 55.04 ? 110  ARG B NH2   1 
ATOM   9583  N N     . ILE B  1 113  ? 6.653   37.840  127.111 1.00 42.71 ? 111  ILE B N     1 
ATOM   9584  C CA    . ILE B  1 113  ? 7.316   38.052  128.394 1.00 44.76 ? 111  ILE B CA    1 
ATOM   9585  C C     . ILE B  1 113  ? 6.802   36.979  129.352 1.00 49.15 ? 111  ILE B C     1 
ATOM   9586  O O     . ILE B  1 113  ? 5.606   36.995  129.692 1.00 48.12 ? 111  ILE B O     1 
ATOM   9587  C CB    . ILE B  1 113  ? 7.058   39.461  128.941 1.00 47.15 ? 111  ILE B CB    1 
ATOM   9588  C CG1   . ILE B  1 113  ? 7.794   40.495  128.086 1.00 48.28 ? 111  ILE B CG1   1 
ATOM   9589  C CG2   . ILE B  1 113  ? 7.496   39.552  130.397 1.00 45.70 ? 111  ILE B CG2   1 
ATOM   9590  C CD1   . ILE B  1 113  ? 7.014   41.771  127.839 1.00 49.62 ? 111  ILE B CD1   1 
ATOM   9591  N N     . PRO B  1 114  ? 7.645   36.037  129.788 1.00 47.96 ? 112  PRO B N     1 
ATOM   9592  C CA    . PRO B  1 114  ? 7.125   34.863  130.514 1.00 49.04 ? 112  PRO B CA    1 
ATOM   9593  C C     . PRO B  1 114  ? 6.693   35.162  131.938 1.00 48.84 ? 112  PRO B C     1 
ATOM   9594  O O     . PRO B  1 114  ? 5.734   34.554  132.432 1.00 50.14 ? 112  PRO B O     1 
ATOM   9595  C CB    . PRO B  1 114  ? 8.309   33.882  130.483 1.00 45.76 ? 112  PRO B CB    1 
ATOM   9596  C CG    . PRO B  1 114  ? 9.235   34.412  129.415 1.00 48.88 ? 112  PRO B CG    1 
ATOM   9597  C CD    . PRO B  1 114  ? 9.069   35.895  129.454 1.00 49.35 ? 112  PRO B CD    1 
ATOM   9598  N N     . ASP B  1 115  ? 7.376   36.073  132.616 1.00 51.23 ? 113  ASP B N     1 
ATOM   9599  C CA    . ASP B  1 115  ? 7.108   36.347  134.018 1.00 55.45 ? 113  ASP B CA    1 
ATOM   9600  C C     . ASP B  1 115  ? 5.933   37.311  134.131 1.00 54.63 ? 113  ASP B C     1 
ATOM   9601  O O     . ASP B  1 115  ? 6.007   38.444  133.646 1.00 54.59 ? 113  ASP B O     1 
ATOM   9602  C CB    . ASP B  1 115  ? 8.363   36.916  134.674 1.00 52.07 ? 113  ASP B CB    1 
ATOM   9603  C CG    . ASP B  1 115  ? 8.094   37.512  136.027 1.00 58.22 ? 113  ASP B CG    1 
ATOM   9604  O OD1   . ASP B  1 115  ? 7.422   36.853  136.850 1.00 60.70 ? 113  ASP B OD1   1 
ATOM   9605  O OD2   . ASP B  1 115  ? 8.569   38.641  136.269 1.00 60.98 ? 113  ASP B OD2   1 
ATOM   9606  N N     . THR B  1 116  ? 4.854   36.861  134.775 1.00 55.06 ? 114  THR B N     1 
ATOM   9607  C CA    . THR B  1 116  ? 3.657   37.688  134.898 1.00 56.65 ? 114  THR B CA    1 
ATOM   9608  C C     . THR B  1 116  ? 3.966   39.026  135.563 1.00 57.71 ? 114  THR B C     1 
ATOM   9609  O O     . THR B  1 116  ? 3.441   40.070  135.154 1.00 54.53 ? 114  THR B O     1 
ATOM   9610  C CB    . THR B  1 116  ? 2.580   36.919  135.672 1.00 56.95 ? 114  THR B CB    1 
ATOM   9611  O OG1   . THR B  1 116  ? 1.991   35.930  134.814 1.00 58.61 ? 114  THR B OG1   1 
ATOM   9612  C CG2   . THR B  1 116  ? 1.492   37.853  136.186 1.00 57.23 ? 114  THR B CG2   1 
ATOM   9613  N N     . ALA B  1 117  ? 4.839   39.021  136.573 1.00 57.86 ? 115  ALA B N     1 
ATOM   9614  C CA    . ALA B  1 117  ? 5.177   40.261  137.262 1.00 53.39 ? 115  ALA B CA    1 
ATOM   9615  C C     . ALA B  1 117  ? 5.914   41.230  136.346 1.00 53.44 ? 115  ALA B C     1 
ATOM   9616  O O     . ALA B  1 117  ? 5.689   42.443  136.414 1.00 58.11 ? 115  ALA B O     1 
ATOM   9617  C CB    . ALA B  1 117  ? 6.015   39.958  138.506 1.00 56.40 ? 115  ALA B CB    1 
ATOM   9618  N N     . THR B  1 118  ? 6.815   40.721  135.501 1.00 53.44 ? 116  THR B N     1 
ATOM   9619  C CA    . THR B  1 118  ? 7.533   41.595  134.578 1.00 52.84 ? 116  THR B CA    1 
ATOM   9620  C C     . THR B  1 118  ? 6.593   42.156  133.521 1.00 52.63 ? 116  THR B C     1 
ATOM   9621  O O     . THR B  1 118  ? 6.693   43.332  133.152 1.00 50.75 ? 116  THR B O     1 
ATOM   9622  C CB    . THR B  1 118  ? 8.685   40.843  133.910 1.00 51.88 ? 116  THR B CB    1 
ATOM   9623  N N     . ARG B  1 119  ? 5.683   41.321  133.015 1.00 52.57 ? 117  ARG B N     1 
ATOM   9624  C CA    . ARG B  1 119  ? 4.742   41.770  131.995 1.00 52.04 ? 117  ARG B CA    1 
ATOM   9625  C C     . ARG B  1 119  ? 3.792   42.815  132.560 1.00 52.98 ? 117  ARG B C     1 
ATOM   9626  O O     . ARG B  1 119  ? 3.673   43.921  132.017 1.00 51.46 ? 117  ARG B O     1 
ATOM   9627  C CB    . ARG B  1 119  ? 3.960   40.579  131.447 1.00 51.15 ? 117  ARG B CB    1 
ATOM   9628  C CG    . ARG B  1 119  ? 2.969   40.959  130.377 1.00 45.78 ? 117  ARG B CG    1 
ATOM   9629  C CD    . ARG B  1 119  ? 1.976   39.850  130.120 1.00 47.14 ? 117  ARG B CD    1 
ATOM   9630  N NE    . ARG B  1 119  ? 2.640   38.571  129.915 1.00 47.68 ? 117  ARG B NE    1 
ATOM   9631  C CZ    . ARG B  1 119  ? 2.358   37.465  130.592 1.00 53.29 ? 117  ARG B CZ    1 
ATOM   9632  N NH1   . ARG B  1 119  ? 1.389   37.432  131.494 1.00 46.38 ? 117  ARG B NH1   1 
ATOM   9633  N NH2   . ARG B  1 119  ? 3.057   36.360  130.347 1.00 53.76 ? 117  ARG B NH2   1 
ATOM   9634  N N     . ASP B  1 120  ? 3.126   42.483  133.671 1.00 52.43 ? 118  ASP B N     1 
ATOM   9635  C CA    . ASP B  1 120  ? 2.161   43.392  134.280 1.00 55.48 ? 118  ASP B CA    1 
ATOM   9636  C C     . ASP B  1 120  ? 2.799   44.718  134.672 1.00 55.07 ? 118  ASP B C     1 
ATOM   9637  O O     . ASP B  1 120  ? 2.107   45.741  134.725 1.00 53.51 ? 118  ASP B O     1 
ATOM   9638  C CB    . ASP B  1 120  ? 1.509   42.729  135.498 1.00 55.54 ? 118  ASP B CB    1 
ATOM   9639  C CG    . ASP B  1 120  ? 0.557   41.598  135.112 1.00 58.83 ? 118  ASP B CG    1 
ATOM   9640  O OD1   . ASP B  1 120  ? 0.447   41.290  133.902 1.00 59.42 ? 118  ASP B OD1   1 
ATOM   9641  O OD2   . ASP B  1 120  ? -0.090  41.019  136.014 1.00 60.09 ? 118  ASP B OD2   1 
ATOM   9642  N N     . ALA B  1 121  ? 4.111   44.727  134.930 1.00 57.57 ? 119  ALA B N     1 
ATOM   9643  C CA    . ALA B  1 121  ? 4.803   45.971  135.254 1.00 56.08 ? 119  ALA B CA    1 
ATOM   9644  C C     . ALA B  1 121  ? 5.128   46.779  134.002 1.00 52.10 ? 119  ALA B C     1 
ATOM   9645  O O     . ALA B  1 121  ? 5.010   48.008  134.007 1.00 55.72 ? 119  ALA B O     1 
ATOM   9646  C CB    . ALA B  1 121  ? 6.079   45.678  136.046 1.00 56.69 ? 119  ALA B CB    1 
ATOM   9647  N N     . LEU B  1 122  ? 5.549   46.115  132.925 1.00 54.47 ? 120  LEU B N     1 
ATOM   9648  C CA    . LEU B  1 122  ? 5.733   46.827  131.666 1.00 53.05 ? 120  LEU B CA    1 
ATOM   9649  C C     . LEU B  1 122  ? 4.441   47.515  131.246 1.00 53.22 ? 120  LEU B C     1 
ATOM   9650  O O     . LEU B  1 122  ? 4.457   48.658  130.775 1.00 52.15 ? 120  LEU B O     1 
ATOM   9651  C CB    . LEU B  1 122  ? 6.205   45.867  130.576 1.00 49.31 ? 120  LEU B CB    1 
ATOM   9652  C CG    . LEU B  1 122  ? 6.561   46.566  129.261 1.00 52.13 ? 120  LEU B CG    1 
ATOM   9653  C CD1   . LEU B  1 122  ? 7.770   47.482  129.462 1.00 52.69 ? 120  LEU B CD1   1 
ATOM   9654  C CD2   . LEU B  1 122  ? 6.797   45.555  128.137 1.00 42.84 ? 120  LEU B CD2   1 
ATOM   9655  N N     . ILE B  1 123  ? 3.309   46.838  131.446 1.00 50.45 ? 121  ILE B N     1 
ATOM   9656  C CA    . ILE B  1 123  ? 2.018   47.381  131.039 1.00 52.48 ? 121  ILE B CA    1 
ATOM   9657  C C     . ILE B  1 123  ? 1.716   48.661  131.806 1.00 56.64 ? 121  ILE B C     1 
ATOM   9658  O O     . ILE B  1 123  ? 1.420   49.708  131.215 1.00 56.52 ? 121  ILE B O     1 
ATOM   9659  C CB    . ILE B  1 123  ? 0.915   46.326  131.247 1.00 49.25 ? 121  ILE B CB    1 
ATOM   9660  C CG1   . ILE B  1 123  ? 1.118   45.148  130.293 1.00 42.25 ? 121  ILE B CG1   1 
ATOM   9661  C CG2   . ILE B  1 123  ? -0.463  46.950  131.099 1.00 47.37 ? 121  ILE B CG2   1 
ATOM   9662  C CD1   . ILE B  1 123  ? 0.150   44.011  130.516 1.00 44.37 ? 121  ILE B CD1   1 
ATOM   9663  N N     . ARG B  1 124  ? 1.804   48.598  133.139 1.00 52.19 ? 122  ARG B N     1 
ATOM   9664  C CA    . ARG B  1 124  ? 1.360   49.706  133.977 1.00 55.45 ? 122  ARG B CA    1 
ATOM   9665  C C     . ARG B  1 124  ? 2.246   50.937  133.822 1.00 59.58 ? 122  ARG B C     1 
ATOM   9666  O O     . ARG B  1 124  ? 1.763   52.067  133.965 1.00 60.61 ? 122  ARG B O     1 
ATOM   9667  C CB    . ARG B  1 124  ? 1.320   49.267  135.443 1.00 54.27 ? 122  ARG B CB    1 
ATOM   9668  N N     . ASP B  1 125  ? 3.531   50.752  133.518 1.00 57.31 ? 123  ASP B N     1 
ATOM   9669  C CA    . ASP B  1 125  ? 4.489   51.842  133.617 1.00 58.33 ? 123  ASP B CA    1 
ATOM   9670  C C     . ASP B  1 125  ? 5.146   52.245  132.303 1.00 56.59 ? 123  ASP B C     1 
ATOM   9671  O O     . ASP B  1 125  ? 5.870   53.246  132.285 1.00 60.55 ? 123  ASP B O     1 
ATOM   9672  C CB    . ASP B  1 125  ? 5.582   51.488  134.641 1.00 57.57 ? 123  ASP B CB    1 
ATOM   9673  C CG    . ASP B  1 125  ? 5.015   51.244  136.028 1.00 59.50 ? 123  ASP B CG    1 
ATOM   9674  O OD1   . ASP B  1 125  ? 4.569   50.110  136.310 1.00 65.95 ? 123  ASP B OD1   1 
ATOM   9675  O OD2   . ASP B  1 125  ? 4.995   52.195  136.835 1.00 62.84 ? 123  ASP B OD2   1 
ATOM   9676  N N     . LYS B  1 126  ? 4.915   51.528  131.216 1.00 53.57 ? 124  LYS B N     1 
ATOM   9677  C CA    . LYS B  1 126  ? 5.535   51.935  129.960 1.00 55.53 ? 124  LYS B CA    1 
ATOM   9678  C C     . LYS B  1 126  ? 4.567   51.976  128.783 1.00 56.78 ? 124  LYS B C     1 
ATOM   9679  O O     . LYS B  1 126  ? 4.718   52.826  127.898 1.00 57.37 ? 124  LYS B O     1 
ATOM   9680  C CB    . LYS B  1 126  ? 6.709   50.997  129.639 1.00 59.64 ? 124  LYS B CB    1 
ATOM   9681  N N     . ILE B  1 127  ? 3.576   51.091  128.748 1.00 52.16 ? 125  ILE B N     1 
ATOM   9682  C CA    . ILE B  1 127  ? 2.731   50.935  127.573 1.00 52.38 ? 125  ILE B CA    1 
ATOM   9683  C C     . ILE B  1 127  ? 1.395   51.646  127.734 1.00 51.66 ? 125  ILE B C     1 
ATOM   9684  O O     . ILE B  1 127  ? 0.906   52.260  126.786 1.00 54.21 ? 125  ILE B O     1 
ATOM   9685  C CB    . ILE B  1 127  ? 2.536   49.439  127.251 1.00 49.79 ? 125  ILE B CB    1 
ATOM   9686  C CG1   . ILE B  1 127  ? 3.903   48.783  127.063 1.00 49.07 ? 125  ILE B CG1   1 
ATOM   9687  C CG2   . ILE B  1 127  ? 1.679   49.270  125.999 1.00 45.71 ? 125  ILE B CG2   1 
ATOM   9688  C CD1   . ILE B  1 127  ? 3.834   47.334  126.719 1.00 46.86 ? 125  ILE B CD1   1 
ATOM   9689  N N     . ALA B  1 128  ? 0.793   51.579  128.923 1.00 47.58 ? 126  ALA B N     1 
ATOM   9690  C CA    . ALA B  1 128  ? -0.407  52.359  129.196 1.00 50.71 ? 126  ALA B CA    1 
ATOM   9691  C C     . ALA B  1 128  ? -0.178  53.854  129.025 1.00 56.40 ? 126  ALA B C     1 
ATOM   9692  O O     . ALA B  1 128  ? -1.153  54.611  128.944 1.00 51.69 ? 126  ALA B O     1 
ATOM   9693  C CB    . ALA B  1 128  ? -0.911  52.070  130.611 1.00 51.83 ? 126  ALA B CB    1 
ATOM   9694  N N     . ASP B  1 129  ? 1.079   54.288  128.969 1.00 57.57 ? 127  ASP B N     1 
ATOM   9695  C CA    . ASP B  1 129  ? 1.439   55.670  128.699 1.00 60.71 ? 127  ASP B CA    1 
ATOM   9696  C C     . ASP B  1 129  ? 1.777   55.899  127.231 1.00 61.54 ? 127  ASP B C     1 
ATOM   9697  O O     . ASP B  1 129  ? 2.333   56.947  126.888 1.00 64.72 ? 127  ASP B O     1 
ATOM   9698  C CB    . ASP B  1 129  ? 2.612   56.089  129.591 1.00 61.00 ? 127  ASP B CB    1 
ATOM   9699  C CG    . ASP B  1 129  ? 2.285   55.977  131.073 1.00 63.54 ? 127  ASP B CG    1 
ATOM   9700  O OD1   . ASP B  1 129  ? 1.217   56.475  131.492 1.00 67.45 ? 127  ASP B OD1   1 
ATOM   9701  O OD2   . ASP B  1 129  ? 3.089   55.378  131.818 1.00 65.10 ? 127  ASP B OD2   1 
ATOM   9702  N N     . GLY B  1 130  ? 1.461   54.940  126.362 1.00 58.11 ? 128  GLY B N     1 
ATOM   9703  C CA    . GLY B  1 130  ? 1.591   55.109  124.931 1.00 56.15 ? 128  GLY B CA    1 
ATOM   9704  C C     . GLY B  1 130  ? 2.989   54.980  124.368 1.00 59.25 ? 128  GLY B C     1 
ATOM   9705  O O     . GLY B  1 130  ? 3.149   55.045  123.143 1.00 61.05 ? 128  GLY B O     1 
ATOM   9706  N N     . ASN B  1 131  ? 4.010   54.804  125.206 1.00 60.71 ? 129  ASN B N     1 
ATOM   9707  C CA    . ASN B  1 131  ? 5.383   54.661  124.719 1.00 59.93 ? 129  ASN B CA    1 
ATOM   9708  C C     . ASN B  1 131  ? 5.673   53.198  124.373 1.00 59.85 ? 129  ASN B C     1 
ATOM   9709  O O     . ASN B  1 131  ? 6.617   52.578  124.863 1.00 64.94 ? 129  ASN B O     1 
ATOM   9710  C CB    . ASN B  1 131  ? 6.367   55.199  125.753 1.00 58.38 ? 129  ASN B CB    1 
ATOM   9711  N N     . TRP B  1 132  ? 4.827   52.648  123.501 1.00 56.09 ? 130  TRP B N     1 
ATOM   9712  C CA    . TRP B  1 132  ? 4.872   51.219  123.220 1.00 52.45 ? 130  TRP B CA    1 
ATOM   9713  C C     . TRP B  1 132  ? 5.882   50.857  122.141 1.00 54.94 ? 130  TRP B C     1 
ATOM   9714  O O     . TRP B  1 132  ? 6.385   49.727  122.134 1.00 53.87 ? 130  TRP B O     1 
ATOM   9715  C CB    . TRP B  1 132  ? 3.477   50.705  122.830 1.00 50.03 ? 130  TRP B CB    1 
ATOM   9716  C CG    . TRP B  1 132  ? 2.915   51.277  121.555 1.00 43.72 ? 130  TRP B CG    1 
ATOM   9717  C CD1   . TRP B  1 132  ? 2.027   52.305  121.439 1.00 45.94 ? 130  TRP B CD1   1 
ATOM   9718  C CD2   . TRP B  1 132  ? 3.200   50.842  120.219 1.00 43.74 ? 130  TRP B CD2   1 
ATOM   9719  N NE1   . TRP B  1 132  ? 1.742   52.543  120.110 1.00 43.19 ? 130  TRP B NE1   1 
ATOM   9720  C CE2   . TRP B  1 132  ? 2.453   51.659  119.343 1.00 41.99 ? 130  TRP B CE2   1 
ATOM   9721  C CE3   . TRP B  1 132  ? 4.021   49.849  119.677 1.00 43.85 ? 130  TRP B CE3   1 
ATOM   9722  C CZ2   . TRP B  1 132  ? 2.498   51.505  117.961 1.00 37.60 ? 130  TRP B CZ2   1 
ATOM   9723  C CZ3   . TRP B  1 132  ? 4.069   49.703  118.311 1.00 41.56 ? 130  TRP B CZ3   1 
ATOM   9724  C CH2   . TRP B  1 132  ? 3.310   50.524  117.465 1.00 38.01 ? 130  TRP B CH2   1 
ATOM   9725  N N     . LYS B  1 133  ? 6.194   51.785  121.231 1.00 58.35 ? 131  LYS B N     1 
ATOM   9726  C CA    . LYS B  1 133  ? 7.174   51.491  120.189 1.00 58.66 ? 131  LYS B CA    1 
ATOM   9727  C C     . LYS B  1 133  ? 8.556   51.234  120.777 1.00 62.10 ? 131  LYS B C     1 
ATOM   9728  O O     . LYS B  1 133  ? 9.325   50.433  120.232 1.00 62.18 ? 131  LYS B O     1 
ATOM   9729  C CB    . LYS B  1 133  ? 7.226   52.639  119.181 1.00 56.62 ? 131  LYS B CB    1 
ATOM   9730  N N     . SER B  1 134  ? 8.883   51.890  121.890 1.00 63.37 ? 132  SER B N     1 
ATOM   9731  C CA    . SER B  1 134  ? 10.171  51.709  122.547 1.00 62.45 ? 132  SER B CA    1 
ATOM   9732  C C     . SER B  1 134  ? 10.256  50.350  123.230 1.00 64.38 ? 132  SER B C     1 
ATOM   9733  O O     . SER B  1 134  ? 11.054  49.493  122.832 1.00 67.65 ? 132  SER B O     1 
ATOM   9734  C CB    . SER B  1 134  ? 10.407  52.823  123.567 1.00 55.45 ? 132  SER B CB    1 
ATOM   9735  N N     . HIS B  1 135  ? 9.422   50.144  124.252 1.00 63.05 ? 133  HIS B N     1 
ATOM   9736  C CA    . HIS B  1 135  ? 9.505   48.941  125.074 1.00 61.90 ? 133  HIS B CA    1 
ATOM   9737  C C     . HIS B  1 135  ? 9.243   47.657  124.289 1.00 61.08 ? 133  HIS B C     1 
ATOM   9738  O O     . HIS B  1 135  ? 9.648   46.580  124.739 1.00 64.81 ? 133  HIS B O     1 
ATOM   9739  C CB    . HIS B  1 135  ? 8.527   49.052  126.245 1.00 58.31 ? 133  HIS B CB    1 
ATOM   9740  N N     . LEU B  1 136  ? 8.577   47.734  123.142 1.00 59.85 ? 134  LEU B N     1 
ATOM   9741  C CA    . LEU B  1 136  ? 8.343   46.544  122.327 1.00 56.53 ? 134  LEU B CA    1 
ATOM   9742  C C     . LEU B  1 136  ? 8.640   46.829  120.854 1.00 60.22 ? 134  LEU B C     1 
ATOM   9743  O O     . LEU B  1 136  ? 8.818   45.908  120.053 1.00 60.42 ? 134  LEU B O     1 
ATOM   9744  C CB    . LEU B  1 136  ? 6.901   46.046  122.488 1.00 50.64 ? 134  LEU B CB    1 
ATOM   9745  C CG    . LEU B  1 136  ? 6.397   45.667  123.884 1.00 51.04 ? 134  LEU B CG    1 
ATOM   9746  C CD1   . LEU B  1 136  ? 4.942   45.251  123.813 1.00 45.77 ? 134  LEU B CD1   1 
ATOM   9747  C CD2   . LEU B  1 136  ? 7.232   44.559  124.506 1.00 52.78 ? 134  LEU B CD2   1 
ATOM   9748  N N     . ARG B  1 140  ? 11.764  43.947  115.475 1.00 40.86 ? 138  ARG B N     1 
ATOM   9749  C CA    . ARG B  1 140  ? 10.640  43.235  114.870 1.00 42.00 ? 138  ARG B CA    1 
ATOM   9750  C C     . ARG B  1 140  ? 9.333   43.990  115.091 1.00 42.74 ? 138  ARG B C     1 
ATOM   9751  O O     . ARG B  1 140  ? 9.015   44.396  116.213 1.00 38.35 ? 138  ARG B O     1 
ATOM   9752  C CB    . ARG B  1 140  ? 10.528  41.816  115.430 1.00 43.01 ? 138  ARG B CB    1 
ATOM   9753  N N     . SER B  1 141  ? 8.584   44.184  114.010 1.00 39.41 ? 139  SER B N     1 
ATOM   9754  C CA    . SER B  1 141  ? 7.320   44.893  114.114 1.00 37.83 ? 139  SER B CA    1 
ATOM   9755  C C     . SER B  1 141  ? 6.405   44.188  115.109 1.00 36.69 ? 139  SER B C     1 
ATOM   9756  O O     . SER B  1 141  ? 6.340   42.955  115.167 1.00 32.57 ? 139  SER B O     1 
ATOM   9757  C CB    . SER B  1 141  ? 6.646   44.989  112.743 1.00 35.97 ? 139  SER B CB    1 
ATOM   9758  O OG    . SER B  1 141  ? 5.318   45.512  112.848 1.00 35.27 ? 139  SER B OG    1 
ATOM   9759  N N     . LEU B  1 142  ? 5.700   44.981  115.912 1.00 34.63 ? 140  LEU B N     1 
ATOM   9760  C CA    . LEU B  1 142  ? 4.644   44.408  116.725 1.00 30.56 ? 140  LEU B CA    1 
ATOM   9761  C C     . LEU B  1 142  ? 3.620   43.663  115.879 1.00 30.39 ? 140  LEU B C     1 
ATOM   9762  O O     . LEU B  1 142  ? 2.948   42.763  116.390 1.00 28.91 ? 140  LEU B O     1 
ATOM   9763  C CB    . LEU B  1 142  ? 3.957   45.518  117.522 1.00 30.43 ? 140  LEU B CB    1 
ATOM   9764  C CG    . LEU B  1 142  ? 3.445   45.172  118.911 1.00 35.06 ? 140  LEU B CG    1 
ATOM   9765  C CD1   . LEU B  1 142  ? 4.585   45.121  119.891 1.00 41.01 ? 140  LEU B CD1   1 
ATOM   9766  C CD2   . LEU B  1 142  ? 2.429   46.195  119.337 1.00 36.20 ? 140  LEU B CD2   1 
ATOM   9767  N N     . PHE B  1 143  ? 3.503   43.998  114.588 1.00 29.24 ? 141  PHE B N     1 
ATOM   9768  C CA    . PHE B  1 143  ? 2.386   43.550  113.766 1.00 29.27 ? 141  PHE B CA    1 
ATOM   9769  C C     . PHE B  1 143  ? 2.754   42.431  112.799 1.00 29.06 ? 141  PHE B C     1 
ATOM   9770  O O     . PHE B  1 143  ? 2.007   42.183  111.844 1.00 27.19 ? 141  PHE B O     1 
ATOM   9771  C CB    . PHE B  1 143  ? 1.790   44.754  113.031 1.00 27.67 ? 141  PHE B CB    1 
ATOM   9772  C CG    . PHE B  1 143  ? 1.506   45.907  113.943 1.00 26.08 ? 141  PHE B CG    1 
ATOM   9773  C CD1   . PHE B  1 143  ? 0.628   45.760  115.005 1.00 25.12 ? 141  PHE B CD1   1 
ATOM   9774  C CD2   . PHE B  1 143  ? 2.152   47.116  113.783 1.00 22.05 ? 141  PHE B CD2   1 
ATOM   9775  C CE1   . PHE B  1 143  ? 0.392   46.804  115.869 1.00 27.41 ? 141  PHE B CE1   1 
ATOM   9776  C CE2   . PHE B  1 143  ? 1.916   48.165  114.635 1.00 23.40 ? 141  PHE B CE2   1 
ATOM   9777  C CZ    . PHE B  1 143  ? 1.036   48.014  115.679 1.00 27.94 ? 141  PHE B CZ    1 
ATOM   9778  N N     . VAL B  1 144  ? 3.860   41.717  113.058 1.00 30.12 ? 142  VAL B N     1 
ATOM   9779  C CA    . VAL B  1 144  ? 4.317   40.639  112.177 1.00 30.96 ? 142  VAL B CA    1 
ATOM   9780  C C     . VAL B  1 144  ? 3.211   39.613  111.922 1.00 32.60 ? 142  VAL B C     1 
ATOM   9781  O O     . VAL B  1 144  ? 3.083   39.078  110.813 1.00 32.23 ? 142  VAL B O     1 
ATOM   9782  C CB    . VAL B  1 144  ? 5.580   39.977  112.767 1.00 31.28 ? 142  VAL B CB    1 
ATOM   9783  C CG1   . VAL B  1 144  ? 5.917   38.692  112.047 1.00 35.92 ? 142  VAL B CG1   1 
ATOM   9784  C CG2   . VAL B  1 144  ? 6.755   40.928  112.691 1.00 35.12 ? 142  VAL B CG2   1 
ATOM   9785  N N     . ASN B  1 145  ? 2.395   39.320  112.933 1.00 33.00 ? 143  ASN B N     1 
ATOM   9786  C CA    . ASN B  1 145  ? 1.319   38.343  112.793 1.00 32.20 ? 143  ASN B CA    1 
ATOM   9787  C C     . ASN B  1 145  ? -0.050  38.983  112.635 1.00 32.26 ? 143  ASN B C     1 
ATOM   9788  O O     . ASN B  1 145  ? -1.061  38.334  112.920 1.00 32.91 ? 143  ASN B O     1 
ATOM   9789  C CB    . ASN B  1 145  ? 1.295   37.396  113.988 1.00 34.07 ? 143  ASN B CB    1 
ATOM   9790  C CG    . ASN B  1 145  ? 2.359   36.339  113.907 1.00 37.84 ? 143  ASN B CG    1 
ATOM   9791  O OD1   . ASN B  1 145  ? 2.524   35.681  112.878 1.00 40.38 ? 143  ASN B OD1   1 
ATOM   9792  N ND2   . ASN B  1 145  ? 3.091   36.162  114.995 1.00 37.64 ? 143  ASN B ND2   1 
ATOM   9793  N N     . ALA B  1 146  ? -0.112  40.233  112.168 1.00 31.86 ? 144  ALA B N     1 
ATOM   9794  C CA    . ALA B  1 146  ? -1.394  40.933  112.136 1.00 31.15 ? 144  ALA B CA    1 
ATOM   9795  C C     . ALA B  1 146  ? -2.387  40.277  111.184 1.00 30.74 ? 144  ALA B C     1 
ATOM   9796  O O     . ALA B  1 146  ? -3.598  40.413  111.371 1.00 33.47 ? 144  ALA B O     1 
ATOM   9797  C CB    . ALA B  1 146  ? -1.188  42.394  111.754 1.00 31.03 ? 144  ALA B CB    1 
ATOM   9798  N N     . ALA B  1 147  ? -1.910  39.575  110.157 1.00 32.86 ? 145  ALA B N     1 
ATOM   9799  C CA    . ALA B  1 147  ? -2.841  38.935  109.224 1.00 33.64 ? 145  ALA B CA    1 
ATOM   9800  C C     . ALA B  1 147  ? -3.647  37.835  109.912 1.00 35.59 ? 145  ALA B C     1 
ATOM   9801  O O     . ALA B  1 147  ? -4.857  37.696  109.680 1.00 32.11 ? 145  ALA B O     1 
ATOM   9802  C CB    . ALA B  1 147  ? -2.082  38.372  108.027 1.00 32.94 ? 145  ALA B CB    1 
ATOM   9803  N N     . THR B  1 148  ? -2.991  37.048  110.766 1.00 35.80 ? 146  THR B N     1 
ATOM   9804  C CA    . THR B  1 148  ? -3.686  36.009  111.513 1.00 33.81 ? 146  THR B CA    1 
ATOM   9805  C C     . THR B  1 148  ? -4.737  36.617  112.436 1.00 35.28 ? 146  THR B C     1 
ATOM   9806  O O     . THR B  1 148  ? -5.902  36.213  112.412 1.00 35.90 ? 146  THR B O     1 
ATOM   9807  C CB    . THR B  1 148  ? -2.676  35.169  112.301 1.00 39.14 ? 146  THR B CB    1 
ATOM   9808  O OG1   . THR B  1 148  ? -1.745  34.571  111.390 1.00 36.62 ? 146  THR B OG1   1 
ATOM   9809  C CG2   . THR B  1 148  ? -3.379  34.068  113.103 1.00 38.86 ? 146  THR B CG2   1 
ATOM   9810  N N     . TRP B  1 149  ? -4.345  37.612  113.243 1.00 30.29 ? 147  TRP B N     1 
ATOM   9811  C CA    . TRP B  1 149  ? -5.312  38.293  114.098 1.00 32.90 ? 147  TRP B CA    1 
ATOM   9812  C C     . TRP B  1 149  ? -6.391  39.004  113.286 1.00 31.33 ? 147  TRP B C     1 
ATOM   9813  O O     . TRP B  1 149  ? -7.525  39.148  113.757 1.00 32.30 ? 147  TRP B O     1 
ATOM   9814  C CB    . TRP B  1 149  ? -4.598  39.283  115.012 1.00 30.95 ? 147  TRP B CB    1 
ATOM   9815  C CG    . TRP B  1 149  ? -3.718  38.632  116.012 1.00 32.56 ? 147  TRP B CG    1 
ATOM   9816  C CD1   . TRP B  1 149  ? -2.361  38.768  116.134 1.00 31.68 ? 147  TRP B CD1   1 
ATOM   9817  C CD2   . TRP B  1 149  ? -4.126  37.729  117.044 1.00 30.51 ? 147  TRP B CD2   1 
ATOM   9818  N NE1   . TRP B  1 149  ? -1.906  38.006  117.186 1.00 30.04 ? 147  TRP B NE1   1 
ATOM   9819  C CE2   . TRP B  1 149  ? -2.968  37.354  117.754 1.00 32.40 ? 147  TRP B CE2   1 
ATOM   9820  C CE3   . TRP B  1 149  ? -5.357  37.192  117.428 1.00 35.76 ? 147  TRP B CE3   1 
ATOM   9821  C CZ2   . TRP B  1 149  ? -3.006  36.478  118.842 1.00 34.76 ? 147  TRP B CZ2   1 
ATOM   9822  C CZ3   . TRP B  1 149  ? -5.395  36.321  118.515 1.00 37.08 ? 147  TRP B CZ3   1 
ATOM   9823  C CH2   . TRP B  1 149  ? -4.222  35.972  119.201 1.00 34.91 ? 147  TRP B CH2   1 
ATOM   9824  N N     . GLY B  1 150  ? -6.058  39.477  112.084 1.00 31.97 ? 148  GLY B N     1 
ATOM   9825  C CA    . GLY B  1 150  ? -7.086  40.039  111.228 1.00 32.21 ? 148  GLY B CA    1 
ATOM   9826  C C     . GLY B  1 150  ? -8.146  39.018  110.867 1.00 37.67 ? 148  GLY B C     1 
ATOM   9827  O O     . GLY B  1 150  ? -9.333  39.345  110.772 1.00 35.69 ? 148  GLY B O     1 
ATOM   9828  N N     . LEU B  1 151  ? -7.729  37.767  110.659 1.00 36.39 ? 149  LEU B N     1 
ATOM   9829  C CA    . LEU B  1 151  ? -8.682  36.679  110.478 1.00 39.26 ? 149  LEU B CA    1 
ATOM   9830  C C     . LEU B  1 151  ? -9.512  36.463  111.737 1.00 41.59 ? 149  LEU B C     1 
ATOM   9831  O O     . LEU B  1 151  ? -10.727 36.257  111.662 1.00 40.99 ? 149  LEU B O     1 
ATOM   9832  C CB    . LEU B  1 151  ? -7.939  35.397  110.103 1.00 41.67 ? 149  LEU B CB    1 
ATOM   9833  C CG    . LEU B  1 151  ? -8.130  34.839  108.700 1.00 45.86 ? 149  LEU B CG    1 
ATOM   9834  C CD1   . LEU B  1 151  ? -7.311  33.574  108.539 1.00 46.04 ? 149  LEU B CD1   1 
ATOM   9835  C CD2   . LEU B  1 151  ? -9.603  34.566  108.462 1.00 43.56 ? 149  LEU B CD2   1 
ATOM   9836  N N     . VAL B  1 152  ? -8.874  36.509  112.906 1.00 37.97 ? 150  VAL B N     1 
ATOM   9837  C CA    . VAL B  1 152  ? -9.615  36.325  114.149 1.00 41.19 ? 150  VAL B CA    1 
ATOM   9838  C C     . VAL B  1 152  ? -10.637 37.442  114.337 1.00 39.82 ? 150  VAL B C     1 
ATOM   9839  O O     . VAL B  1 152  ? -11.785 37.197  114.725 1.00 41.55 ? 150  VAL B O     1 
ATOM   9840  C CB    . VAL B  1 152  ? -8.644  36.243  115.341 1.00 36.37 ? 150  VAL B CB    1 
ATOM   9841  C CG1   . VAL B  1 152  ? -9.414  36.119  116.643 1.00 39.48 ? 150  VAL B CG1   1 
ATOM   9842  C CG2   . VAL B  1 152  ? -7.681  35.088  115.164 1.00 39.56 ? 150  VAL B CG2   1 
ATOM   9843  N N     . VAL B  1 153  ? -10.244 38.679  114.058 1.00 38.50 ? 151  VAL B N     1 
ATOM   9844  C CA    . VAL B  1 153  ? -11.057 39.841  114.405 1.00 39.77 ? 151  VAL B CA    1 
ATOM   9845  C C     . VAL B  1 153  ? -12.122 40.122  113.351 1.00 38.29 ? 151  VAL B C     1 
ATOM   9846  O O     . VAL B  1 153  ? -13.284 40.351  113.687 1.00 35.16 ? 151  VAL B O     1 
ATOM   9847  C CB    . VAL B  1 153  ? -10.139 41.064  114.638 1.00 36.68 ? 151  VAL B CB    1 
ATOM   9848  C CG1   . VAL B  1 153  ? -10.948 42.348  114.751 1.00 33.88 ? 151  VAL B CG1   1 
ATOM   9849  C CG2   . VAL B  1 153  ? -9.284  40.857  115.873 1.00 35.35 ? 151  VAL B CG2   1 
ATOM   9850  N N     . THR B  1 154  ? -11.755 40.099  112.063 1.00 39.96 ? 152  THR B N     1 
ATOM   9851  C CA    . THR B  1 154  ? -12.657 40.485  110.985 1.00 41.94 ? 152  THR B CA    1 
ATOM   9852  C C     . THR B  1 154  ? -13.158 39.325  110.145 1.00 41.40 ? 152  THR B C     1 
ATOM   9853  O O     . THR B  1 154  ? -14.142 39.495  109.425 1.00 41.25 ? 152  THR B O     1 
ATOM   9854  C CB    . THR B  1 154  ? -11.984 41.478  110.016 1.00 38.47 ? 152  THR B CB    1 
ATOM   9855  O OG1   . THR B  1 154  ? -11.078 40.770  109.159 1.00 39.29 ? 152  THR B OG1   1 
ATOM   9856  C CG2   . THR B  1 154  ? -11.223 42.562  110.764 1.00 40.50 ? 152  THR B CG2   1 
ATOM   9857  N N     . GLY B  1 155  ? -12.493 38.176  110.181 1.00 39.82 ? 153  GLY B N     1 
ATOM   9858  C CA    . GLY B  1 155  ? -12.848 37.072  109.321 1.00 37.49 ? 153  GLY B CA    1 
ATOM   9859  C C     . GLY B  1 155  ? -12.223 37.088  107.943 1.00 39.45 ? 153  GLY B C     1 
ATOM   9860  O O     . GLY B  1 155  ? -12.467 36.158  107.165 1.00 44.01 ? 153  GLY B O     1 
ATOM   9861  N N     . LYS B  1 156  ? -11.436 38.108  107.604 1.00 38.89 ? 154  LYS B N     1 
ATOM   9862  C CA    . LYS B  1 156  ? -10.778 38.189  106.306 1.00 44.27 ? 154  LYS B CA    1 
ATOM   9863  C C     . LYS B  1 156  ? -9.267  38.059  106.464 1.00 41.58 ? 154  LYS B C     1 
ATOM   9864  O O     . LYS B  1 156  ? -8.711  38.385  107.518 1.00 38.23 ? 154  LYS B O     1 
ATOM   9865  C CB    . LYS B  1 156  ? -11.114 39.506  105.595 1.00 42.32 ? 154  LYS B CB    1 
ATOM   9866  N N     . LEU B  1 157  ? -8.610  37.566  105.408 1.00 40.91 ? 155  LEU B N     1 
ATOM   9867  C CA    . LEU B  1 157  ? -7.158  37.427  105.338 1.00 46.78 ? 155  LEU B CA    1 
ATOM   9868  C C     . LEU B  1 157  ? -6.602  38.355  104.261 1.00 48.86 ? 155  LEU B C     1 
ATOM   9869  O O     . LEU B  1 157  ? -7.280  38.647  103.274 1.00 49.08 ? 155  LEU B O     1 
ATOM   9870  C CB    . LEU B  1 157  ? -6.752  35.980  105.031 1.00 45.76 ? 155  LEU B CB    1 
ATOM   9871  N N     . THR B  1 158  ? -5.351  38.810  104.435 1.00 51.77 ? 156  THR B N     1 
ATOM   9872  C CA    . THR B  1 158  ? -4.796  39.849  103.562 1.00 49.27 ? 156  THR B CA    1 
ATOM   9873  C C     . THR B  1 158  ? -3.420  39.565  102.964 1.00 47.65 ? 156  THR B C     1 
ATOM   9874  O O     . THR B  1 158  ? -3.064  40.231  101.984 1.00 52.83 ? 156  THR B O     1 
ATOM   9875  C CB    . THR B  1 158  ? -4.701  41.187  104.305 1.00 48.51 ? 156  THR B CB    1 
ATOM   9876  O OG1   . THR B  1 158  ? -3.828  41.038  105.434 1.00 46.03 ? 156  THR B OG1   1 
ATOM   9877  C CG2   . THR B  1 158  ? -6.075  41.652  104.762 1.00 46.17 ? 156  THR B CG2   1 
ATOM   9878  N N     . SER B  1 159  ? -2.632  38.646  103.525 1.00 44.89 ? 157  SER B N     1 
ATOM   9879  C CA    . SER B  1 159  ? -1.278  38.313  103.069 1.00 44.77 ? 157  SER B CA    1 
ATOM   9880  C C     . SER B  1 159  ? -0.237  39.334  103.524 1.00 43.26 ? 157  SER B C     1 
ATOM   9881  O O     . SER B  1 159  ? 0.849   38.937  103.961 1.00 46.58 ? 157  SER B O     1 
ATOM   9882  C CB    . SER B  1 159  ? -1.205  38.141  101.544 1.00 46.19 ? 157  SER B CB    1 
ATOM   9883  N N     . THR B  1 160  ? -0.516  40.635  103.415 1.00 36.14 ? 158  THR B N     1 
ATOM   9884  C CA    . THR B  1 160  ? 0.376   41.630  104.011 1.00 37.58 ? 158  THR B CA    1 
ATOM   9885  C C     . THR B  1 160  ? -0.420  42.594  104.880 1.00 34.04 ? 158  THR B C     1 
ATOM   9886  O O     . THR B  1 160  ? -1.649  42.659  104.832 1.00 33.15 ? 158  THR B O     1 
ATOM   9887  C CB    . THR B  1 160  ? 1.204   42.416  102.973 1.00 33.89 ? 158  THR B CB    1 
ATOM   9888  O OG1   . THR B  1 160  ? 0.349   43.154  102.094 1.00 34.74 ? 158  THR B OG1   1 
ATOM   9889  C CG2   . THR B  1 160  ? 2.088   41.481  102.180 1.00 35.94 ? 158  THR B CG2   1 
ATOM   9890  N N     . VAL B  1 161  ? 0.321   43.360  105.673 1.00 27.51 ? 159  VAL B N     1 
ATOM   9891  C CA    . VAL B  1 161  ? -0.208  44.063  106.830 1.00 32.02 ? 159  VAL B CA    1 
ATOM   9892  C C     . VAL B  1 161  ? 0.013   45.553  106.628 1.00 27.66 ? 159  VAL B C     1 
ATOM   9893  O O     . VAL B  1 161  ? 1.115   45.969  106.266 1.00 26.39 ? 159  VAL B O     1 
ATOM   9894  C CB    . VAL B  1 161  ? 0.488   43.550  108.103 1.00 31.94 ? 159  VAL B CB    1 
ATOM   9895  C CG1   . VAL B  1 161  ? 0.377   44.518  109.211 1.00 31.02 ? 159  VAL B CG1   1 
ATOM   9896  C CG2   . VAL B  1 161  ? -0.082  42.193  108.469 1.00 35.85 ? 159  VAL B CG2   1 
ATOM   9897  N N     . ASN B  1 162  ? -1.031  46.352  106.848 1.00 24.52 ? 160  ASN B N     1 
ATOM   9898  C CA    . ASN B  1 162  ? -0.858  47.805  106.835 1.00 26.14 ? 160  ASN B CA    1 
ATOM   9899  C C     . ASN B  1 162  ? -0.384  48.203  108.227 1.00 23.05 ? 160  ASN B C     1 
ATOM   9900  O O     . ASN B  1 162  ? -1.176  48.481  109.130 1.00 24.56 ? 160  ASN B O     1 
ATOM   9901  C CB    . ASN B  1 162  ? -2.140  48.525  106.431 1.00 25.46 ? 160  ASN B CB    1 
ATOM   9902  C CG    . ASN B  1 162  ? -1.921  50.026  106.217 1.00 28.89 ? 160  ASN B CG    1 
ATOM   9903  O OD1   . ASN B  1 162  ? -0.981  50.604  106.762 1.00 26.97 ? 160  ASN B OD1   1 
ATOM   9904  N ND2   . ASN B  1 162  ? -2.798  50.659  105.435 1.00 27.13 ? 160  ASN B ND2   1 
ATOM   9905  N N     . ASP B  1 163  ? 0.938   48.204  108.404 1.00 24.15 ? 161  ASP B N     1 
ATOM   9906  C CA    . ASP B  1 163  ? 1.512   48.477  109.715 1.00 22.19 ? 161  ASP B CA    1 
ATOM   9907  C C     . ASP B  1 163  ? 1.416   49.949  110.100 1.00 26.08 ? 161  ASP B C     1 
ATOM   9908  O O     . ASP B  1 163  ? 1.445   50.255  111.293 1.00 25.97 ? 161  ASP B O     1 
ATOM   9909  C CB    . ASP B  1 163  ? 2.959   47.984  109.776 1.00 26.78 ? 161  ASP B CB    1 
ATOM   9910  C CG    . ASP B  1 163  ? 3.812   48.496  108.625 1.00 23.28 ? 161  ASP B CG    1 
ATOM   9911  O OD1   . ASP B  1 163  ? 3.361   48.457  107.465 1.00 22.83 ? 161  ASP B OD1   1 
ATOM   9912  O OD2   . ASP B  1 163  ? 4.953   48.919  108.891 1.00 30.46 ? 161  ASP B OD2   1 
ATOM   9913  N N     . ARG B  1 164  ? 1.267   50.870  109.137 1.00 22.05 ? 162  ARG B N     1 
ATOM   9914  C CA    . ARG B  1 164  ? 1.016   52.261  109.522 1.00 23.52 ? 162  ARG B CA    1 
ATOM   9915  C C     . ARG B  1 164  ? -0.396  52.437  110.064 1.00 23.58 ? 162  ARG B C     1 
ATOM   9916  O O     . ARG B  1 164  ? -0.603  53.164  111.045 1.00 23.23 ? 162  ARG B O     1 
ATOM   9917  C CB    . ARG B  1 164  ? 1.263   53.212  108.344 1.00 24.57 ? 162  ARG B CB    1 
ATOM   9918  C CG    . ARG B  1 164  ? 2.724   53.299  107.901 1.00 26.98 ? 162  ARG B CG    1 
ATOM   9919  C CD    . ARG B  1 164  ? 3.701   53.301  109.086 1.00 28.30 ? 162  ARG B CD    1 
ATOM   9920  N NE    . ARG B  1 164  ? 3.402   54.332  110.067 1.00 35.35 ? 162  ARG B NE    1 
ATOM   9921  C CZ    . ARG B  1 164  ? 3.823   54.306  111.327 1.00 36.07 ? 162  ARG B CZ    1 
ATOM   9922  N NH1   . ARG B  1 164  ? 4.539   53.295  111.795 1.00 36.21 ? 162  ARG B NH1   1 
ATOM   9923  N NH2   . ARG B  1 164  ? 3.515   55.318  112.135 1.00 34.24 ? 162  ARG B NH2   1 
ATOM   9924  N N     . SER B  1 165  ? -1.378  51.779  109.440 1.00 23.28 ? 163  SER B N     1 
ATOM   9925  C CA    . SER B  1 165  ? -2.741  51.809  109.962 1.00 22.79 ? 163  SER B CA    1 
ATOM   9926  C C     . SER B  1 165  ? -2.813  51.162  111.342 1.00 21.16 ? 163  SER B C     1 
ATOM   9927  O O     . SER B  1 165  ? -3.467  51.684  112.251 1.00 21.91 ? 163  SER B O     1 
ATOM   9928  C CB    . SER B  1 165  ? -3.685  51.099  108.985 1.00 21.72 ? 163  SER B CB    1 
ATOM   9929  O OG    . SER B  1 165  ? -4.969  50.938  109.559 1.00 26.37 ? 163  SER B OG    1 
ATOM   9930  N N     . LEU B  1 166  ? -2.107  50.045  111.526 1.00 23.15 ? 164  LEU B N     1 
ATOM   9931  C CA    . LEU B  1 166  ? -2.118  49.372  112.822 1.00 23.30 ? 164  LEU B CA    1 
ATOM   9932  C C     . LEU B  1 166  ? -1.431  50.210  113.895 1.00 25.20 ? 164  LEU B C     1 
ATOM   9933  O O     . LEU B  1 166  ? -1.913  50.287  115.036 1.00 26.35 ? 164  LEU B O     1 
ATOM   9934  C CB    . LEU B  1 166  ? -1.470  47.998  112.689 1.00 22.38 ? 164  LEU B CB    1 
ATOM   9935  C CG    . LEU B  1 166  ? -2.370  47.074  111.875 1.00 26.94 ? 164  LEU B CG    1 
ATOM   9936  C CD1   . LEU B  1 166  ? -1.630  45.836  111.540 1.00 25.41 ? 164  LEU B CD1   1 
ATOM   9937  C CD2   . LEU B  1 166  ? -3.639  46.734  112.631 1.00 25.66 ? 164  LEU B CD2   1 
ATOM   9938  N N     . ALA B  1 167  ? -0.309  50.851  113.547 1.00 24.95 ? 165  ALA B N     1 
ATOM   9939  C CA    . ALA B  1 167  ? 0.387   51.696  114.514 1.00 27.66 ? 165  ALA B CA    1 
ATOM   9940  C C     . ALA B  1 167  ? -0.490  52.864  114.948 1.00 23.64 ? 165  ALA B C     1 
ATOM   9941  O O     . ALA B  1 167  ? -0.593  53.168  116.142 1.00 23.59 ? 165  ALA B O     1 
ATOM   9942  C CB    . ALA B  1 167  ? 1.709   52.192  113.915 1.00 23.48 ? 165  ALA B CB    1 
ATOM   9943  N N     . ALA B  1 168  ? -1.153  53.515  113.989 1.00 23.95 ? 166  ALA B N     1 
ATOM   9944  C CA    . ALA B  1 168  ? -2.124  54.559  114.316 1.00 23.34 ? 166  ALA B CA    1 
ATOM   9945  C C     . ALA B  1 168  ? -3.241  54.036  115.218 1.00 23.98 ? 166  ALA B C     1 
ATOM   9946  O O     . ALA B  1 168  ? -3.650  54.714  116.172 1.00 24.83 ? 166  ALA B O     1 
ATOM   9947  C CB    . ALA B  1 168  ? -2.717  55.130  113.020 1.00 22.97 ? 166  ALA B CB    1 
ATOM   9948  N N     . ALA B  1 169  ? -3.770  52.846  114.916 1.00 25.67 ? 167  ALA B N     1 
ATOM   9949  C CA    . ALA B  1 169  ? -4.894  52.331  115.698 1.00 24.30 ? 167  ALA B CA    1 
ATOM   9950  C C     . ALA B  1 169  ? -4.460  51.961  117.108 1.00 24.89 ? 167  ALA B C     1 
ATOM   9951  O O     . ALA B  1 169  ? -5.211  52.170  118.064 1.00 25.96 ? 167  ALA B O     1 
ATOM   9952  C CB    . ALA B  1 169  ? -5.516  51.121  115.002 1.00 25.76 ? 167  ALA B CB    1 
ATOM   9953  N N     . LEU B  1 170  ? -3.254  51.407  117.257 1.00 25.15 ? 168  LEU B N     1 
ATOM   9954  C CA    . LEU B  1 170  ? -2.805  51.052  118.596 1.00 25.07 ? 168  LEU B CA    1 
ATOM   9955  C C     . LEU B  1 170  ? -2.579  52.296  119.436 1.00 25.81 ? 168  LEU B C     1 
ATOM   9956  O O     . LEU B  1 170  ? -2.970  52.345  120.605 1.00 27.34 ? 168  LEU B O     1 
ATOM   9957  C CB    . LEU B  1 170  ? -1.537  50.208  118.517 1.00 24.49 ? 168  LEU B CB    1 
ATOM   9958  C CG    . LEU B  1 170  ? -1.005  49.720  119.862 1.00 30.25 ? 168  LEU B CG    1 
ATOM   9959  C CD1   . LEU B  1 170  ? -2.082  48.936  120.597 1.00 25.73 ? 168  LEU B CD1   1 
ATOM   9960  C CD2   . LEU B  1 170  ? 0.209   48.871  119.628 1.00 33.02 ? 168  LEU B CD2   1 
ATOM   9961  N N     . THR B  1 171  ? -1.942  53.312  118.861 1.00 27.46 ? 169  THR B N     1 
ATOM   9962  C CA    . THR B  1 171  ? -1.806  54.573  119.577 1.00 27.13 ? 169  THR B CA    1 
ATOM   9963  C C     . THR B  1 171  ? -3.170  55.136  119.951 1.00 29.68 ? 169  THR B C     1 
ATOM   9964  O O     . THR B  1 171  ? -3.379  55.583  121.082 1.00 29.92 ? 169  THR B O     1 
ATOM   9965  C CB    . THR B  1 171  ? -1.032  55.579  118.731 1.00 28.32 ? 169  THR B CB    1 
ATOM   9966  O OG1   . THR B  1 171  ? 0.278   55.073  118.490 1.00 34.89 ? 169  THR B OG1   1 
ATOM   9967  C CG2   . THR B  1 171  ? -0.956  56.940  119.438 1.00 29.43 ? 169  THR B CG2   1 
ATOM   9968  N N     . ARG B  1 172  ? -4.121  55.100  119.016 1.00 28.03 ? 170  ARG B N     1 
ATOM   9969  C CA    . ARG B  1 172  ? -5.429  55.664  119.298 1.00 29.43 ? 170  ARG B CA    1 
ATOM   9970  C C     . ARG B  1 172  ? -6.104  54.927  120.443 1.00 29.14 ? 170  ARG B C     1 
ATOM   9971  O O     . ARG B  1 172  ? -6.661  55.557  121.352 1.00 32.63 ? 170  ARG B O     1 
ATOM   9972  C CB    . ARG B  1 172  ? -6.307  55.628  118.049 1.00 28.10 ? 170  ARG B CB    1 
ATOM   9973  C CG    . ARG B  1 172  ? -7.534  56.536  118.164 1.00 27.85 ? 170  ARG B CG    1 
ATOM   9974  C CD    . ARG B  1 172  ? -8.451  56.396  116.939 1.00 28.38 ? 170  ARG B CD    1 
ATOM   9975  N NE    . ARG B  1 172  ? -7.728  56.479  115.674 1.00 26.64 ? 170  ARG B NE    1 
ATOM   9976  C CZ    . ARG B  1 172  ? -7.430  55.443  114.900 1.00 25.65 ? 170  ARG B CZ    1 
ATOM   9977  N NH1   . ARG B  1 172  ? -7.722  54.205  115.259 1.00 26.66 ? 170  ARG B NH1   1 
ATOM   9978  N NH2   . ARG B  1 172  ? -6.818  55.657  113.737 1.00 24.77 ? 170  ARG B NH2   1 
ATOM   9979  N N     . LEU B  1 173  ? -6.046  53.591  120.434 1.00 29.79 ? 171  LEU B N     1 
ATOM   9980  C CA    . LEU B  1 173  ? -6.809  52.839  121.428 1.00 31.81 ? 171  LEU B CA    1 
ATOM   9981  C C     . LEU B  1 173  ? -6.183  52.958  122.808 1.00 29.60 ? 171  LEU B C     1 
ATOM   9982  O O     . LEU B  1 173  ? -6.900  53.044  123.812 1.00 32.64 ? 171  LEU B O     1 
ATOM   9983  C CB    . LEU B  1 173  ? -6.953  51.372  121.007 1.00 30.43 ? 171  LEU B CB    1 
ATOM   9984  C CG    . LEU B  1 173  ? -5.832  50.337  121.075 1.00 28.50 ? 171  LEU B CG    1 
ATOM   9985  C CD1   . LEU B  1 173  ? -5.634  49.735  122.487 1.00 29.80 ? 171  LEU B CD1   1 
ATOM   9986  C CD2   . LEU B  1 173  ? -6.166  49.248  120.092 1.00 27.69 ? 171  LEU B CD2   1 
ATOM   9987  N N     . ILE B  1 174  ? -4.852  52.999  122.876 1.00 28.94 ? 172  ILE B N     1 
ATOM   9988  C CA    . ILE B  1 174  ? -4.197  53.166  124.168 1.00 30.19 ? 172  ILE B CA    1 
ATOM   9989  C C     . ILE B  1 174  ? -4.458  54.560  124.722 1.00 30.55 ? 172  ILE B C     1 
ATOM   9990  O O     . ILE B  1 174  ? -4.768  54.717  125.908 1.00 31.56 ? 172  ILE B O     1 
ATOM   9991  C CB    . ILE B  1 174  ? -2.688  52.874  124.058 1.00 31.82 ? 172  ILE B CB    1 
ATOM   9992  C CG1   . ILE B  1 174  ? -2.439  51.412  123.670 1.00 30.67 ? 172  ILE B CG1   1 
ATOM   9993  C CG2   . ILE B  1 174  ? -1.983  53.229  125.357 1.00 35.10 ? 172  ILE B CG2   1 
ATOM   9994  C CD1   . ILE B  1 174  ? -0.995  51.091  123.431 1.00 36.21 ? 172  ILE B CD1   1 
ATOM   9995  N N     . SER B  1 175  ? -4.343  55.598  123.882 1.00 30.23 ? 173  SER B N     1 
ATOM   9996  C CA    . SER B  1 175  ? -4.575  56.953  124.381 1.00 31.66 ? 173  SER B CA    1 
ATOM   9997  C C     . SER B  1 175  ? -6.035  57.190  124.744 1.00 31.97 ? 173  SER B C     1 
ATOM   9998  O O     . SER B  1 175  ? -6.328  58.101  125.532 1.00 36.18 ? 173  SER B O     1 
ATOM   9999  C CB    . SER B  1 175  ? -4.133  58.011  123.362 1.00 35.52 ? 173  SER B CB    1 
ATOM   10000 O OG    . SER B  1 175  ? -2.745  57.936  123.069 1.00 38.12 ? 173  SER B OG    1 
ATOM   10001 N N     . ARG B  1 176  ? -6.953  56.400  124.193 1.00 31.65 ? 174  ARG B N     1 
ATOM   10002 C CA    . ARG B  1 176  ? -8.369  56.532  124.522 1.00 34.48 ? 174  ARG B CA    1 
ATOM   10003 C C     . ARG B  1 176  ? -8.742  55.732  125.764 1.00 33.30 ? 174  ARG B C     1 
ATOM   10004 O O     . ARG B  1 176  ? -9.507  56.216  126.611 1.00 35.08 ? 174  ARG B O     1 
ATOM   10005 C CB    . ARG B  1 176  ? -9.226  56.087  123.320 1.00 31.83 ? 174  ARG B CB    1 
ATOM   10006 C CG    . ARG B  1 176  ? -10.719 56.423  123.406 1.00 34.55 ? 174  ARG B CG    1 
ATOM   10007 C CD    . ARG B  1 176  ? -11.445 56.132  122.060 1.00 32.84 ? 174  ARG B CD    1 
ATOM   10008 N NE    . ARG B  1 176  ? -11.648 54.700  121.852 1.00 32.93 ? 174  ARG B NE    1 
ATOM   10009 C CZ    . ARG B  1 176  ? -11.077 53.968  120.903 1.00 36.17 ? 174  ARG B CZ    1 
ATOM   10010 N NH1   . ARG B  1 176  ? -10.319 54.515  119.953 1.00 31.98 ? 174  ARG B NH1   1 
ATOM   10011 N NH2   . ARG B  1 176  ? -11.279 52.651  120.894 1.00 37.22 ? 174  ARG B NH2   1 
ATOM   10012 N N     . CYS B  1 177  ? -8.183  54.528  125.917 1.00 36.27 ? 175  CYS B N     1 
ATOM   10013 C CA    . CYS B  1 177  ? -8.659  53.581  126.916 1.00 33.60 ? 175  CYS B CA    1 
ATOM   10014 C C     . CYS B  1 177  ? -7.604  53.132  127.917 1.00 37.02 ? 175  CYS B C     1 
ATOM   10015 O O     . CYS B  1 177  ? -7.974  52.631  128.981 1.00 38.65 ? 175  CYS B O     1 
ATOM   10016 C CB    . CYS B  1 177  ? -9.248  52.336  126.229 1.00 39.26 ? 175  CYS B CB    1 
ATOM   10017 S SG    . CYS B  1 177  ? -10.516 52.689  124.930 1.00 45.33 ? 175  CYS B SG    1 
ATOM   10018 N N     . GLY B  1 178  ? -6.316  53.268  127.609 1.00 36.05 ? 176  GLY B N     1 
ATOM   10019 C CA    . GLY B  1 178  ? -5.307  53.042  128.632 1.00 41.82 ? 176  GLY B CA    1 
ATOM   10020 C C     . GLY B  1 178  ? -5.107  51.583  129.030 1.00 39.87 ? 176  GLY B C     1 
ATOM   10021 O O     . GLY B  1 178  ? -5.416  50.643  128.289 1.00 42.01 ? 176  GLY B O     1 
ATOM   10022 N N     . GLU B  1 179  ? -4.559  51.416  130.236 1.00 43.02 ? 177  GLU B N     1 
ATOM   10023 C CA    . GLU B  1 179  ? -4.264  50.087  130.770 1.00 43.47 ? 177  GLU B CA    1 
ATOM   10024 C C     . GLU B  1 179  ? -5.450  49.130  130.783 1.00 40.44 ? 177  GLU B C     1 
ATOM   10025 O O     . GLU B  1 179  ? -5.239  47.940  130.491 1.00 40.07 ? 177  GLU B O     1 
ATOM   10026 C CB    . GLU B  1 179  ? -3.690  50.204  132.195 1.00 45.54 ? 177  GLU B CB    1 
ATOM   10027 C CG    . GLU B  1 179  ? -4.237  49.149  133.171 1.00 53.09 ? 177  GLU B CG    1 
ATOM   10028 C CD    . GLU B  1 179  ? -3.151  48.389  133.923 1.00 64.29 ? 177  GLU B CD    1 
ATOM   10029 O OE1   . GLU B  1 179  ? -2.206  49.035  134.434 1.00 64.12 ? 177  GLU B OE1   1 
ATOM   10030 O OE2   . GLU B  1 179  ? -3.250  47.140  134.005 1.00 63.33 ? 177  GLU B OE2   1 
ATOM   10031 N N     . PRO B  1 180  ? -6.679  49.534  131.130 1.00 40.76 ? 178  PRO B N     1 
ATOM   10032 C CA    . PRO B  1 180  ? -7.754  48.535  131.195 1.00 39.44 ? 178  PRO B CA    1 
ATOM   10033 C C     . PRO B  1 180  ? -7.977  47.789  129.892 1.00 41.59 ? 178  PRO B C     1 
ATOM   10034 O O     . PRO B  1 180  ? -8.300  46.596  129.938 1.00 40.04 ? 178  PRO B O     1 
ATOM   10035 C CB    . PRO B  1 180  ? -8.978  49.368  131.601 1.00 40.83 ? 178  PRO B CB    1 
ATOM   10036 C CG    . PRO B  1 180  ? -8.404  50.471  132.413 1.00 41.41 ? 178  PRO B CG    1 
ATOM   10037 C CD    . PRO B  1 180  ? -7.135  50.834  131.658 1.00 38.95 ? 178  PRO B CD    1 
ATOM   10038 N N     . VAL B  1 181  ? -7.804  48.433  128.731 1.00 34.86 ? 179  VAL B N     1 
ATOM   10039 C CA    . VAL B  1 181  ? -8.025  47.695  127.493 1.00 37.75 ? 179  VAL B CA    1 
ATOM   10040 C C     . VAL B  1 181  ? -6.836  46.792  127.199 1.00 38.58 ? 179  VAL B C     1 
ATOM   10041 O O     . VAL B  1 181  ? -7.006  45.697  126.648 1.00 35.73 ? 179  VAL B O     1 
ATOM   10042 C CB    . VAL B  1 181  ? -8.322  48.639  126.309 1.00 37.91 ? 179  VAL B CB    1 
ATOM   10043 C CG1   . VAL B  1 181  ? -7.074  49.408  125.867 1.00 36.38 ? 179  VAL B CG1   1 
ATOM   10044 C CG2   . VAL B  1 181  ? -8.894  47.860  125.138 1.00 38.83 ? 179  VAL B CG2   1 
ATOM   10045 N N     . ILE B  1 182  ? -5.627  47.220  127.576 1.00 36.84 ? 180  ILE B N     1 
ATOM   10046 C CA    . ILE B  1 182  ? -4.452  46.372  127.414 1.00 38.30 ? 180  ILE B CA    1 
ATOM   10047 C C     . ILE B  1 182  ? -4.607  45.100  128.239 1.00 38.74 ? 180  ILE B C     1 
ATOM   10048 O O     . ILE B  1 182  ? -4.447  43.986  127.726 1.00 38.28 ? 180  ILE B O     1 
ATOM   10049 C CB    . ILE B  1 182  ? -3.174  47.152  127.779 1.00 37.53 ? 180  ILE B CB    1 
ATOM   10050 C CG1   . ILE B  1 182  ? -2.975  48.322  126.809 1.00 36.54 ? 180  ILE B CG1   1 
ATOM   10051 C CG2   . ILE B  1 182  ? -1.953  46.251  127.707 1.00 38.25 ? 180  ILE B CG2   1 
ATOM   10052 C CD1   . ILE B  1 182  ? -1.984  49.358  127.283 1.00 39.98 ? 180  ILE B CD1   1 
ATOM   10053 N N     . ARG B  1 183  ? -4.967  45.243  129.523 1.00 38.44 ? 181  ARG B N     1 
ATOM   10054 C CA    . ARG B  1 183  ? -5.152  44.063  130.365 1.00 43.02 ? 181  ARG B CA    1 
ATOM   10055 C C     . ARG B  1 183  ? -6.203  43.117  129.785 1.00 43.09 ? 181  ARG B C     1 
ATOM   10056 O O     . ARG B  1 183  ? -5.991  41.899  129.744 1.00 42.73 ? 181  ARG B O     1 
ATOM   10057 C CB    . ARG B  1 183  ? -5.514  44.487  131.792 1.00 47.61 ? 181  ARG B CB    1 
ATOM   10058 C CG    . ARG B  1 183  ? -6.059  43.374  132.698 1.00 53.97 ? 181  ARG B CG    1 
ATOM   10059 C CD    . ARG B  1 183  ? -5.157  42.140  132.742 1.00 55.17 ? 181  ARG B CD    1 
ATOM   10060 N NE    . ARG B  1 183  ? -3.750  42.482  132.885 1.00 56.04 ? 181  ARG B NE    1 
ATOM   10061 C CZ    . ARG B  1 183  ? -2.756  41.626  132.695 1.00 57.65 ? 181  ARG B CZ    1 
ATOM   10062 N NH1   . ARG B  1 183  ? -2.985  40.373  132.341 1.00 59.07 ? 181  ARG B NH1   1 
ATOM   10063 N NH2   . ARG B  1 183  ? -1.503  42.041  132.860 1.00 60.93 ? 181  ARG B NH2   1 
ATOM   10064 N N     . ARG B  1 184  ? -7.330  43.654  129.313 1.00 43.25 ? 182  ARG B N     1 
ATOM   10065 C CA    . ARG B  1 184  ? -8.346  42.807  128.693 1.00 42.56 ? 182  ARG B CA    1 
ATOM   10066 C C     . ARG B  1 184  ? -7.805  42.093  127.459 1.00 43.53 ? 182  ARG B C     1 
ATOM   10067 O O     . ARG B  1 184  ? -8.106  40.915  127.236 1.00 46.14 ? 182  ARG B O     1 
ATOM   10068 C CB    . ARG B  1 184  ? -9.580  43.637  128.338 1.00 44.11 ? 182  ARG B CB    1 
ATOM   10069 C CG    . ARG B  1 184  ? -10.476 43.934  129.534 1.00 48.45 ? 182  ARG B CG    1 
ATOM   10070 C CD    . ARG B  1 184  ? -11.427 42.768  129.839 1.00 51.51 ? 182  ARG B CD    1 
ATOM   10071 N NE    . ARG B  1 184  ? -12.690 42.898  129.122 1.00 49.92 ? 182  ARG B NE    1 
ATOM   10072 C CZ    . ARG B  1 184  ? -13.104 42.095  128.150 1.00 51.65 ? 182  ARG B CZ    1 
ATOM   10073 N NH1   . ARG B  1 184  ? -12.418 41.017  127.798 1.00 50.81 ? 182  ARG B NH1   1 
ATOM   10074 N NH2   . ARG B  1 184  ? -14.237 42.381  127.514 1.00 51.03 ? 182  ARG B NH2   1 
ATOM   10075 N N     . GLY B  1 185  ? -7.015  42.790  126.639 1.00 40.18 ? 183  GLY B N     1 
ATOM   10076 C CA    . GLY B  1 185  ? -6.468  42.159  125.449 1.00 39.30 ? 183  GLY B CA    1 
ATOM   10077 C C     . GLY B  1 185  ? -5.501  41.036  125.774 1.00 40.27 ? 183  GLY B C     1 
ATOM   10078 O O     . GLY B  1 185  ? -5.557  39.963  125.168 1.00 38.64 ? 183  GLY B O     1 
ATOM   10079 N N     . VAL B  1 186  ? -4.601  41.268  126.735 1.00 37.51 ? 184  VAL B N     1 
ATOM   10080 C CA    . VAL B  1 186  ? -3.670  40.228  127.167 1.00 43.41 ? 184  VAL B CA    1 
ATOM   10081 C C     . VAL B  1 186  ? -4.430  39.002  127.672 1.00 41.89 ? 184  VAL B C     1 
ATOM   10082 O O     . VAL B  1 186  ? -4.157  37.868  127.261 1.00 40.96 ? 184  VAL B O     1 
ATOM   10083 C CB    . VAL B  1 186  ? -2.712  40.790  128.232 1.00 40.19 ? 184  VAL B CB    1 
ATOM   10084 C CG1   . VAL B  1 186  ? -1.956  39.668  128.943 1.00 43.29 ? 184  VAL B CG1   1 
ATOM   10085 C CG2   . VAL B  1 186  ? -1.752  41.783  127.591 1.00 39.28 ? 184  VAL B CG2   1 
ATOM   10086 N N     . ASP B  1 187  ? -5.409  39.217  128.554 1.00 43.08 ? 185  ASP B N     1 
ATOM   10087 C CA    . ASP B  1 187  ? -6.180  38.099  129.095 1.00 44.17 ? 185  ASP B CA    1 
ATOM   10088 C C     . ASP B  1 187  ? -6.919  37.352  127.997 1.00 44.52 ? 185  ASP B C     1 
ATOM   10089 O O     . ASP B  1 187  ? -7.056  36.125  128.056 1.00 42.02 ? 185  ASP B O     1 
ATOM   10090 C CB    . ASP B  1 187  ? -7.167  38.601  130.143 1.00 45.52 ? 185  ASP B CB    1 
ATOM   10091 C CG    . ASP B  1 187  ? -6.477  39.205  131.344 1.00 52.32 ? 185  ASP B CG    1 
ATOM   10092 O OD1   . ASP B  1 187  ? -5.239  39.048  131.462 1.00 52.37 ? 185  ASP B OD1   1 
ATOM   10093 O OD2   . ASP B  1 187  ? -7.175  39.839  132.164 1.00 44.54 ? 185  ASP B OD2   1 
ATOM   10094 N N     . MET B  1 188  ? -7.408  38.081  126.990 1.00 45.53 ? 186  MET B N     1 
ATOM   10095 C CA    . MET B  1 188  ? -8.099  37.460  125.869 1.00 40.75 ? 186  MET B CA    1 
ATOM   10096 C C     . MET B  1 188  ? -7.140  36.634  125.018 1.00 44.13 ? 186  MET B C     1 
ATOM   10097 O O     . MET B  1 188  ? -7.449  35.501  124.637 1.00 44.95 ? 186  MET B O     1 
ATOM   10098 C CB    . MET B  1 188  ? -8.771  38.545  125.029 1.00 45.07 ? 186  MET B CB    1 
ATOM   10099 C CG    . MET B  1 188  ? -9.572  38.040  123.854 1.00 49.78 ? 186  MET B CG    1 
ATOM   10100 S SD    . MET B  1 188  ? -11.030 37.163  124.420 1.00 56.99 ? 186  MET B SD    1 
ATOM   10101 C CE    . MET B  1 188  ? -11.653 38.281  125.684 1.00 54.09 ? 186  MET B CE    1 
ATOM   10102 N N     . ALA B  1 189  ? -5.975  37.191  124.691 1.00 42.74 ? 187  ALA B N     1 
ATOM   10103 C CA    . ALA B  1 189  ? -5.027  36.460  123.859 1.00 42.78 ? 187  ALA B CA    1 
ATOM   10104 C C     . ALA B  1 189  ? -4.485  35.235  124.590 1.00 43.51 ? 187  ALA B C     1 
ATOM   10105 O O     . ALA B  1 189  ? -4.285  34.177  123.978 1.00 44.44 ? 187  ALA B O     1 
ATOM   10106 C CB    . ALA B  1 189  ? -3.887  37.384  123.422 1.00 38.73 ? 187  ALA B CB    1 
ATOM   10107 N N     . MET B  1 190  ? -4.231  35.361  125.893 1.00 42.88 ? 188  MET B N     1 
ATOM   10108 C CA    . MET B  1 190  ? -3.812  34.209  126.685 1.00 45.83 ? 188  MET B CA    1 
ATOM   10109 C C     . MET B  1 190  ? -4.813  33.064  126.556 1.00 44.98 ? 188  MET B C     1 
ATOM   10110 O O     . MET B  1 190  ? -4.436  31.921  126.267 1.00 42.91 ? 188  MET B O     1 
ATOM   10111 C CB    . MET B  1 190  ? -3.639  34.614  128.152 1.00 42.35 ? 188  MET B CB    1 
ATOM   10112 C CG    . MET B  1 190  ? -2.435  33.982  128.836 1.00 47.44 ? 188  MET B CG    1 
ATOM   10113 S SD    . MET B  1 190  ? -2.476  34.217  130.625 1.00 62.01 ? 188  MET B SD    1 
ATOM   10114 C CE    . MET B  1 190  ? -2.145  35.972  130.772 1.00 43.83 ? 188  MET B CE    1 
ATOM   10115 N N     . ARG B  1 191  ? -6.100  33.354  126.756 1.00 44.76 ? 189  ARG B N     1 
ATOM   10116 C CA    . ARG B  1 191  ? -7.115  32.308  126.652 1.00 45.53 ? 189  ARG B CA    1 
ATOM   10117 C C     . ARG B  1 191  ? -7.146  31.708  125.249 1.00 44.39 ? 189  ARG B C     1 
ATOM   10118 O O     . ARG B  1 191  ? -7.125  30.481  125.085 1.00 44.09 ? 189  ARG B O     1 
ATOM   10119 C CB    . ARG B  1 191  ? -8.489  32.863  127.040 1.00 43.89 ? 189  ARG B CB    1 
ATOM   10120 N N     . MET B  1 192  ? -7.171  32.558  124.221 1.00 42.33 ? 190  MET B N     1 
ATOM   10121 C CA    . MET B  1 192  ? -7.248  32.048  122.857 1.00 42.27 ? 190  MET B CA    1 
ATOM   10122 C C     . MET B  1 192  ? -6.019  31.214  122.517 1.00 44.53 ? 190  MET B C     1 
ATOM   10123 O O     . MET B  1 192  ? -6.135  30.064  122.073 1.00 42.92 ? 190  MET B O     1 
ATOM   10124 C CB    . MET B  1 192  ? -7.405  33.202  121.866 1.00 43.55 ? 190  MET B CB    1 
ATOM   10125 C CG    . MET B  1 192  ? -8.625  34.069  122.125 1.00 48.59 ? 190  MET B CG    1 
ATOM   10126 S SD    . MET B  1 192  ? -8.904  35.280  120.820 1.00 53.90 ? 190  MET B SD    1 
ATOM   10127 C CE    . MET B  1 192  ? -9.409  34.193  119.491 1.00 43.21 ? 190  MET B CE    1 
ATOM   10128 N N     . MET B  1 193  ? -4.826  31.777  122.727 1.00 40.21 ? 191  MET B N     1 
ATOM   10129 C CA    . MET B  1 193  ? -3.615  31.071  122.337 1.00 41.16 ? 191  MET B CA    1 
ATOM   10130 C C     . MET B  1 193  ? -3.278  29.931  123.283 1.00 45.16 ? 191  MET B C     1 
ATOM   10131 O O     . MET B  1 193  ? -2.492  29.052  122.914 1.00 40.23 ? 191  MET B O     1 
ATOM   10132 C CB    . MET B  1 193  ? -2.434  32.037  122.262 1.00 45.76 ? 191  MET B CB    1 
ATOM   10133 C CG    . MET B  1 193  ? -2.461  32.955  121.054 1.00 45.31 ? 191  MET B CG    1 
ATOM   10134 S SD    . MET B  1 193  ? -0.907  33.855  120.877 1.00 49.37 ? 191  MET B SD    1 
ATOM   10135 C CE    . MET B  1 193  ? -0.843  34.728  122.419 1.00 39.42 ? 191  MET B CE    1 
ATOM   10136 N N     . GLY B  1 194  ? -3.852  29.920  124.485 1.00 44.07 ? 192  GLY B N     1 
ATOM   10137 C CA    . GLY B  1 194  ? -3.485  28.929  125.477 1.00 42.13 ? 192  GLY B CA    1 
ATOM   10138 C C     . GLY B  1 194  ? -4.463  27.781  125.600 1.00 44.41 ? 192  GLY B C     1 
ATOM   10139 O O     . GLY B  1 194  ? -4.074  26.683  126.011 1.00 44.85 ? 192  GLY B O     1 
ATOM   10140 N N     . GLU B  1 195  ? -5.730  28.015  125.244 1.00 43.63 ? 193  GLU B N     1 
ATOM   10141 C CA    . GLU B  1 195  ? -6.796  27.055  125.526 1.00 44.85 ? 193  GLU B CA    1 
ATOM   10142 C C     . GLU B  1 195  ? -7.765  26.834  124.376 1.00 44.75 ? 193  GLU B C     1 
ATOM   10143 O O     . GLU B  1 195  ? -8.429  25.791  124.354 1.00 37.24 ? 193  GLU B O     1 
ATOM   10144 C CB    . GLU B  1 195  ? -7.599  27.490  126.763 1.00 45.97 ? 193  GLU B CB    1 
ATOM   10145 N N     . GLN B  1 196  ? -7.878  27.757  123.422 1.00 46.98 ? 194  GLN B N     1 
ATOM   10146 C CA    . GLN B  1 196  ? -8.781  27.602  122.290 1.00 44.88 ? 194  GLN B CA    1 
ATOM   10147 C C     . GLN B  1 196  ? -8.056  27.135  121.034 1.00 45.53 ? 194  GLN B C     1 
ATOM   10148 O O     . GLN B  1 196  ? -8.457  26.144  120.416 1.00 47.35 ? 194  GLN B O     1 
ATOM   10149 C CB    . GLN B  1 196  ? -9.520  28.919  122.018 1.00 45.19 ? 194  GLN B CB    1 
ATOM   10150 N N     . PHE B  1 197  ? -6.989  27.827  120.639 1.00 42.06 ? 195  PHE B N     1 
ATOM   10151 C CA    . PHE B  1 197  ? -6.252  27.401  119.456 1.00 44.92 ? 195  PHE B CA    1 
ATOM   10152 C C     . PHE B  1 197  ? -5.477  26.117  119.722 1.00 42.39 ? 195  PHE B C     1 
ATOM   10153 O O     . PHE B  1 197  ? -5.347  25.268  118.833 1.00 42.29 ? 195  PHE B O     1 
ATOM   10154 C CB    . PHE B  1 197  ? -5.328  28.527  118.992 1.00 42.07 ? 195  PHE B CB    1 
ATOM   10155 C CG    . PHE B  1 197  ? -6.067  29.755  118.538 1.00 41.85 ? 195  PHE B CG    1 
ATOM   10156 C CD1   . PHE B  1 197  ? -7.295  29.639  117.911 1.00 46.72 ? 195  PHE B CD1   1 
ATOM   10157 C CD2   . PHE B  1 197  ? -5.545  31.020  118.752 1.00 46.26 ? 195  PHE B CD2   1 
ATOM   10158 C CE1   . PHE B  1 197  ? -7.985  30.760  117.490 1.00 48.33 ? 195  PHE B CE1   1 
ATOM   10159 C CE2   . PHE B  1 197  ? -6.235  32.149  118.338 1.00 45.31 ? 195  PHE B CE2   1 
ATOM   10160 C CZ    . PHE B  1 197  ? -7.453  32.015  117.710 1.00 47.54 ? 195  PHE B CZ    1 
ATOM   10161 N N     . VAL B  1 198  ? -4.982  25.940  120.937 1.00 37.97 ? 196  VAL B N     1 
ATOM   10162 C CA    . VAL B  1 198  ? -4.362  24.682  121.317 1.00 39.35 ? 196  VAL B CA    1 
ATOM   10163 C C     . VAL B  1 198  ? -5.095  24.152  122.533 1.00 41.76 ? 196  VAL B C     1 
ATOM   10164 O O     . VAL B  1 198  ? -5.664  24.911  123.326 1.00 42.61 ? 196  VAL B O     1 
ATOM   10165 C CB    . VAL B  1 198  ? -2.851  24.820  121.606 1.00 35.68 ? 196  VAL B CB    1 
ATOM   10166 C CG1   . VAL B  1 198  ? -2.110  25.263  120.345 1.00 39.25 ? 196  VAL B CG1   1 
ATOM   10167 C CG2   . VAL B  1 198  ? -2.617  25.775  122.738 1.00 37.26 ? 196  VAL B CG2   1 
ATOM   10168 N N     . THR B  1 199  ? -5.095  22.830  122.665 1.00 39.56 ? 197  THR B N     1 
ATOM   10169 C CA    . THR B  1 199  ? -5.619  22.226  123.881 1.00 38.44 ? 197  THR B CA    1 
ATOM   10170 C C     . THR B  1 199  ? -4.661  22.427  125.046 1.00 40.94 ? 197  THR B C     1 
ATOM   10171 O O     . THR B  1 199  ? -5.092  22.465  126.201 1.00 40.43 ? 197  THR B O     1 
ATOM   10172 C CB    . THR B  1 199  ? -5.903  20.753  123.621 1.00 38.45 ? 197  THR B CB    1 
ATOM   10173 O OG1   . THR B  1 199  ? -6.583  20.647  122.357 1.00 37.68 ? 197  THR B OG1   1 
ATOM   10174 C CG2   . THR B  1 199  ? -6.792  20.188  124.701 1.00 40.91 ? 197  THR B CG2   1 
ATOM   10175 N N     . GLY B  1 200  ? -3.373  22.579  124.762 1.00 38.13 ? 198  GLY B N     1 
ATOM   10176 C CA    . GLY B  1 200  ? -2.407  22.943  125.776 1.00 40.36 ? 198  GLY B CA    1 
ATOM   10177 C C     . GLY B  1 200  ? -1.061  23.207  125.139 1.00 39.94 ? 198  GLY B C     1 
ATOM   10178 O O     . GLY B  1 200  ? -0.804  22.802  124.002 1.00 38.72 ? 198  GLY B O     1 
ATOM   10179 N N     . GLU B  1 201  ? -0.204  23.902  125.893 1.00 44.88 ? 199  GLU B N     1 
ATOM   10180 C CA    . GLU B  1 201  ? 1.133   24.221  125.397 1.00 46.27 ? 199  GLU B CA    1 
ATOM   10181 C C     . GLU B  1 201  ? 2.040   22.997  125.393 1.00 41.05 ? 199  GLU B C     1 
ATOM   10182 O O     . GLU B  1 201  ? 2.933   22.890  124.546 1.00 43.55 ? 199  GLU B O     1 
ATOM   10183 C CB    . GLU B  1 201  ? 1.757   25.339  126.235 1.00 42.59 ? 199  GLU B CB    1 
ATOM   10184 N N     . THR B  1 202  ? 1.823   22.070  126.317 1.00 40.61 ? 200  THR B N     1 
ATOM   10185 C CA    . THR B  1 202  ? 2.576   20.827  126.390 1.00 43.10 ? 200  THR B CA    1 
ATOM   10186 C C     . THR B  1 202  ? 1.594   19.664  126.402 1.00 44.50 ? 200  THR B C     1 
ATOM   10187 O O     . THR B  1 202  ? 0.411   19.835  126.711 1.00 41.47 ? 200  THR B O     1 
ATOM   10188 C CB    . THR B  1 202  ? 3.440   20.766  127.642 1.00 44.13 ? 200  THR B CB    1 
ATOM   10189 O OG1   . THR B  1 202  ? 2.587   20.731  128.790 1.00 46.22 ? 200  THR B OG1   1 
ATOM   10190 C CG2   . THR B  1 202  ? 4.334   21.989  127.737 1.00 49.09 ? 200  THR B CG2   1 
ATOM   10191 N N     . ILE B  1 203  ? 2.097   18.474  126.059 1.00 42.20 ? 201  ILE B N     1 
ATOM   10192 C CA    . ILE B  1 203  ? 1.250   17.284  126.085 1.00 42.35 ? 201  ILE B CA    1 
ATOM   10193 C C     . ILE B  1 203  ? 0.733   17.034  127.497 1.00 41.18 ? 201  ILE B C     1 
ATOM   10194 O O     . ILE B  1 203  ? -0.397  16.566  127.682 1.00 38.28 ? 201  ILE B O     1 
ATOM   10195 C CB    . ILE B  1 203  ? 2.011   16.064  125.522 1.00 39.95 ? 201  ILE B CB    1 
ATOM   10196 C CG1   . ILE B  1 203  ? 1.048   14.893  125.292 1.00 38.09 ? 201  ILE B CG1   1 
ATOM   10197 C CG2   . ILE B  1 203  ? 3.138   15.639  126.465 1.00 37.72 ? 201  ILE B CG2   1 
ATOM   10198 C CD1   . ILE B  1 203  ? -0.058  15.209  124.284 1.00 34.74 ? 201  ILE B CD1   1 
ATOM   10199 N N     . ARG B  1 204  ? 1.527   17.381  128.511 1.00 43.39 ? 202  ARG B N     1 
ATOM   10200 C CA    . ARG B  1 204  ? 1.098   17.225  129.896 1.00 43.80 ? 202  ARG B CA    1 
ATOM   10201 C C     . ARG B  1 204  ? -0.133  18.075  130.188 1.00 42.52 ? 202  ARG B C     1 
ATOM   10202 O O     . ARG B  1 204  ? -1.110  17.598  130.781 1.00 42.73 ? 202  ARG B O     1 
ATOM   10203 C CB    . ARG B  1 204  ? 2.247   17.606  130.828 1.00 46.00 ? 202  ARG B CB    1 
ATOM   10204 C CG    . ARG B  1 204  ? 2.247   16.894  132.146 1.00 48.13 ? 202  ARG B CG    1 
ATOM   10205 C CD    . ARG B  1 204  ? 3.476   17.295  132.947 1.00 50.25 ? 202  ARG B CD    1 
ATOM   10206 N NE    . ARG B  1 204  ? 3.496   18.732  133.188 1.00 50.49 ? 202  ARG B NE    1 
ATOM   10207 C CZ    . ARG B  1 204  ? 2.874   19.325  134.197 1.00 50.56 ? 202  ARG B CZ    1 
ATOM   10208 N NH1   . ARG B  1 204  ? 2.186   18.631  135.089 1.00 53.66 ? 202  ARG B NH1   1 
ATOM   10209 N NH2   . ARG B  1 204  ? 2.944   20.648  134.314 1.00 52.75 ? 202  ARG B NH2   1 
ATOM   10210 N N     . GLU B  1 205  ? -0.104  19.344  129.775 1.00 42.92 ? 203  GLU B N     1 
ATOM   10211 C CA    . GLU B  1 205  ? -1.247  20.213  130.018 1.00 44.17 ? 203  GLU B CA    1 
ATOM   10212 C C     . GLU B  1 205  ? -2.451  19.766  129.199 1.00 41.87 ? 203  GLU B C     1 
ATOM   10213 O O     . GLU B  1 205  ? -3.588  19.806  129.681 1.00 42.06 ? 203  GLU B O     1 
ATOM   10214 C CB    . GLU B  1 205  ? -0.879  21.659  129.699 1.00 44.86 ? 203  GLU B CB    1 
ATOM   10215 C CG    . GLU B  1 205  ? -1.762  22.688  130.371 1.00 50.10 ? 203  GLU B CG    1 
ATOM   10216 C CD    . GLU B  1 205  ? -1.376  24.111  129.991 1.00 55.71 ? 203  GLU B CD    1 
ATOM   10217 O OE1   . GLU B  1 205  ? -1.262  24.392  128.781 1.00 51.66 ? 203  GLU B OE1   1 
ATOM   10218 O OE2   . GLU B  1 205  ? -1.175  24.945  130.904 1.00 62.86 ? 203  GLU B OE2   1 
ATOM   10219 N N     . ALA B  1 206  ? -2.217  19.325  127.964 1.00 40.19 ? 204  ALA B N     1 
ATOM   10220 C CA    . ALA B  1 206  ? -3.323  18.935  127.100 1.00 40.68 ? 204  ALA B CA    1 
ATOM   10221 C C     . ALA B  1 206  ? -3.988  17.657  127.596 1.00 42.02 ? 204  ALA B C     1 
ATOM   10222 O O     . ALA B  1 206  ? -5.209  17.502  127.479 1.00 42.35 ? 204  ALA B O     1 
ATOM   10223 C CB    . ALA B  1 206  ? -2.835  18.774  125.658 1.00 34.53 ? 204  ALA B CB    1 
ATOM   10224 N N     . LEU B  1 207  ? -3.207  16.732  128.155 1.00 40.55 ? 205  LEU B N     1 
ATOM   10225 C CA    . LEU B  1 207  ? -3.787  15.495  128.668 1.00 40.30 ? 205  LEU B CA    1 
ATOM   10226 C C     . LEU B  1 207  ? -4.665  15.759  129.881 1.00 44.14 ? 205  LEU B C     1 
ATOM   10227 O O     . LEU B  1 207  ? -5.743  15.167  130.010 1.00 45.81 ? 205  LEU B O     1 
ATOM   10228 C CB    . LEU B  1 207  ? -2.685  14.497  129.013 1.00 40.98 ? 205  LEU B CB    1 
ATOM   10229 C CG    . LEU B  1 207  ? -1.964  13.830  127.843 1.00 39.45 ? 205  LEU B CG    1 
ATOM   10230 C CD1   . LEU B  1 207  ? -0.711  13.116  128.354 1.00 40.83 ? 205  LEU B CD1   1 
ATOM   10231 C CD2   . LEU B  1 207  ? -2.890  12.865  127.102 1.00 35.12 ? 205  LEU B CD2   1 
ATOM   10232 N N     . LYS B  1 208  ? -4.223  16.637  130.788 1.00 44.17 ? 206  LYS B N     1 
ATOM   10233 C CA    . LYS B  1 208  ? -5.051  16.969  131.945 1.00 49.61 ? 206  LYS B CA    1 
ATOM   10234 C C     . LYS B  1 208  ? -6.309  17.732  131.534 1.00 45.72 ? 206  LYS B C     1 
ATOM   10235 O O     . LYS B  1 208  ? -7.351  17.609  132.186 1.00 46.53 ? 206  LYS B O     1 
ATOM   10236 C CB    . LYS B  1 208  ? -4.241  17.773  132.965 1.00 48.82 ? 206  LYS B CB    1 
ATOM   10237 N N     . ARG B  1 209  ? -6.241  18.510  130.458 1.00 45.25 ? 207  ARG B N     1 
ATOM   10238 C CA    . ARG B  1 209  ? -7.416  19.239  130.009 1.00 45.72 ? 207  ARG B CA    1 
ATOM   10239 C C     . ARG B  1 209  ? -8.372  18.371  129.206 1.00 48.07 ? 207  ARG B C     1 
ATOM   10240 O O     . ARG B  1 209  ? -9.496  18.803  128.931 1.00 47.57 ? 207  ARG B O     1 
ATOM   10241 C CB    . ARG B  1 209  ? -6.992  20.455  129.187 1.00 46.82 ? 207  ARG B CB    1 
ATOM   10242 C CG    . ARG B  1 209  ? -6.322  21.534  130.024 1.00 45.18 ? 207  ARG B CG    1 
ATOM   10243 C CD    . ARG B  1 209  ? -6.006  22.740  129.183 1.00 45.02 ? 207  ARG B CD    1 
ATOM   10244 N NE    . ARG B  1 209  ? -5.323  23.777  129.945 1.00 50.45 ? 207  ARG B NE    1 
ATOM   10245 C CZ    . ARG B  1 209  ? -4.800  24.870  129.408 1.00 50.36 ? 207  ARG B CZ    1 
ATOM   10246 N NH1   . ARG B  1 209  ? -4.850  25.091  128.103 1.00 44.30 ? 207  ARG B NH1   1 
ATOM   10247 N NH2   . ARG B  1 209  ? -4.214  25.765  130.200 1.00 53.98 ? 207  ARG B NH2   1 
ATOM   10248 N N     . SER B  1 210  ? -7.967  17.155  128.849 1.00 48.48 ? 208  SER B N     1 
ATOM   10249 C CA    . SER B  1 210  ? -8.816  16.265  128.070 1.00 44.42 ? 208  SER B CA    1 
ATOM   10250 C C     . SER B  1 210  ? -9.778  15.451  128.924 1.00 46.23 ? 208  SER B C     1 
ATOM   10251 O O     . SER B  1 210  ? -10.775 14.946  128.394 1.00 45.33 ? 208  SER B O     1 
ATOM   10252 C CB    . SER B  1 210  ? -7.947  15.321  127.235 1.00 41.82 ? 208  SER B CB    1 
ATOM   10253 O OG    . SER B  1 210  ? -7.150  16.064  126.309 1.00 40.97 ? 208  SER B OG    1 
ATOM   10254 N N     . LYS B  1 211  ? -9.518  15.324  130.228 1.00 44.55 ? 209  LYS B N     1 
ATOM   10255 C CA    . LYS B  1 211  ? -10.336 14.442  131.061 1.00 45.46 ? 209  LYS B CA    1 
ATOM   10256 C C     . LYS B  1 211  ? -11.796 14.879  131.077 1.00 44.89 ? 209  LYS B C     1 
ATOM   10257 O O     . LYS B  1 211  ? -12.697 14.035  131.104 1.00 46.07 ? 209  LYS B O     1 
ATOM   10258 C CB    . LYS B  1 211  ? -9.788  14.395  132.485 1.00 45.17 ? 209  LYS B CB    1 
ATOM   10259 C CG    . LYS B  1 211  ? -8.277  14.214  132.581 1.00 56.02 ? 209  LYS B CG    1 
ATOM   10260 C CD    . LYS B  1 211  ? -7.838  12.837  132.102 1.00 57.58 ? 209  LYS B CD    1 
ATOM   10261 C CE    . LYS B  1 211  ? -6.336  12.655  132.288 1.00 59.79 ? 209  LYS B CE    1 
ATOM   10262 N NZ    . LYS B  1 211  ? -5.887  11.298  131.885 1.00 56.85 ? 209  LYS B NZ    1 
ATOM   10263 N N     . GLU B  1 212  ? -12.050 16.192  131.051 1.00 45.93 ? 210  GLU B N     1 
ATOM   10264 C CA    . GLU B  1 212  ? -13.417 16.686  131.213 1.00 46.20 ? 210  GLU B CA    1 
ATOM   10265 C C     . GLU B  1 212  ? -14.318 16.211  130.079 1.00 47.33 ? 210  GLU B C     1 
ATOM   10266 O O     . GLU B  1 212  ? -15.423 15.715  130.321 1.00 49.55 ? 210  GLU B O     1 
ATOM   10267 C CB    . GLU B  1 212  ? -13.427 18.214  131.303 1.00 44.99 ? 210  GLU B CB    1 
ATOM   10268 N N     . LEU B  1 213  ? -13.868 16.358  128.830 1.00 44.56 ? 211  LEU B N     1 
ATOM   10269 C CA    . LEU B  1 213  ? -14.701 15.930  127.710 1.00 48.39 ? 211  LEU B CA    1 
ATOM   10270 C C     . LEU B  1 213  ? -14.620 14.425  127.476 1.00 47.18 ? 211  LEU B C     1 
ATOM   10271 O O     . LEU B  1 213  ? -15.588 13.834  126.986 1.00 47.00 ? 211  LEU B O     1 
ATOM   10272 C CB    . LEU B  1 213  ? -14.333 16.709  126.443 1.00 43.39 ? 211  LEU B CB    1 
ATOM   10273 C CG    . LEU B  1 213  ? -14.881 18.143  126.404 1.00 42.02 ? 211  LEU B CG    1 
ATOM   10274 C CD1   . LEU B  1 213  ? -14.504 18.882  125.116 1.00 43.64 ? 211  LEU B CD1   1 
ATOM   10275 C CD2   . LEU B  1 213  ? -16.390 18.148  126.581 1.00 48.50 ? 211  LEU B CD2   1 
ATOM   10276 N N     . GLU B  1 214  ? -13.508 13.780  127.844 1.00 43.14 ? 212  GLU B N     1 
ATOM   10277 C CA    . GLU B  1 214  ? -13.453 12.318  127.782 1.00 42.61 ? 212  GLU B CA    1 
ATOM   10278 C C     . GLU B  1 214  ? -14.501 11.679  128.688 1.00 45.18 ? 212  GLU B C     1 
ATOM   10279 O O     . GLU B  1 214  ? -15.119 10.672  128.320 1.00 43.49 ? 212  GLU B O     1 
ATOM   10280 C CB    . GLU B  1 214  ? -12.063 11.816  128.164 1.00 45.55 ? 212  GLU B CB    1 
ATOM   10281 C CG    . GLU B  1 214  ? -10.991 12.029  127.102 1.00 43.34 ? 212  GLU B CG    1 
ATOM   10282 C CD    . GLU B  1 214  ? -9.659  11.414  127.520 1.00 42.50 ? 212  GLU B CD    1 
ATOM   10283 O OE1   . GLU B  1 214  ? -9.534  11.025  128.699 1.00 45.38 ? 212  GLU B OE1   1 
ATOM   10284 O OE2   . GLU B  1 214  ? -8.751  11.310  126.675 1.00 45.62 ? 212  GLU B OE2   1 
ATOM   10285 N N     . GLU B  1 215  ? -14.706 12.237  129.884 1.00 43.21 ? 213  GLU B N     1 
ATOM   10286 C CA    . GLU B  1 215  ? -15.716 11.696  130.785 1.00 44.02 ? 213  GLU B CA    1 
ATOM   10287 C C     . GLU B  1 215  ? -17.124 11.882  130.233 1.00 46.41 ? 213  GLU B C     1 
ATOM   10288 O O     . GLU B  1 215  ? -18.033 11.144  130.621 1.00 51.09 ? 213  GLU B O     1 
ATOM   10289 C CB    . GLU B  1 215  ? -15.595 12.347  132.163 1.00 48.80 ? 213  GLU B CB    1 
ATOM   10290 N N     . LYS B  1 216  ? -17.317 12.838  129.327 1.00 51.11 ? 214  LYS B N     1 
ATOM   10291 C CA    . LYS B  1 216  ? -18.588 13.031  128.652 1.00 48.38 ? 214  LYS B CA    1 
ATOM   10292 C C     . LYS B  1 216  ? -18.724 12.161  127.406 1.00 51.85 ? 214  LYS B C     1 
ATOM   10293 O O     . LYS B  1 216  ? -19.797 12.149  126.794 1.00 52.38 ? 214  LYS B O     1 
ATOM   10294 C CB    . LYS B  1 216  ? -18.764 14.510  128.280 1.00 48.50 ? 214  LYS B CB    1 
ATOM   10295 N N     . GLY B  1 217  ? -17.672 11.438  127.018 1.00 42.56 ? 215  GLY B N     1 
ATOM   10296 C CA    . GLY B  1 217  ? -17.720 10.518  125.899 1.00 43.47 ? 215  GLY B CA    1 
ATOM   10297 C C     . GLY B  1 217  ? -16.842 10.894  124.721 1.00 43.86 ? 215  GLY B C     1 
ATOM   10298 O O     . GLY B  1 217  ? -16.780 10.124  123.754 1.00 45.32 ? 215  GLY B O     1 
ATOM   10299 N N     . PHE B  1 218  ? -16.175 12.047  124.750 1.00 42.19 ? 216  PHE B N     1 
ATOM   10300 C CA    . PHE B  1 218  ? -15.272 12.383  123.660 1.00 41.19 ? 216  PHE B CA    1 
ATOM   10301 C C     . PHE B  1 218  ? -13.989 11.570  123.767 1.00 39.87 ? 216  PHE B C     1 
ATOM   10302 O O     . PHE B  1 218  ? -13.653 11.025  124.817 1.00 43.13 ? 216  PHE B O     1 
ATOM   10303 C CB    . PHE B  1 218  ? -14.930 13.876  123.667 1.00 42.55 ? 216  PHE B CB    1 
ATOM   10304 C CG    . PHE B  1 218  ? -16.063 14.766  123.248 1.00 44.47 ? 216  PHE B CG    1 
ATOM   10305 C CD1   . PHE B  1 218  ? -17.015 15.176  124.167 1.00 47.36 ? 216  PHE B CD1   1 
ATOM   10306 C CD2   . PHE B  1 218  ? -16.171 15.202  121.937 1.00 45.28 ? 216  PHE B CD2   1 
ATOM   10307 C CE1   . PHE B  1 218  ? -18.056 15.998  123.784 1.00 47.22 ? 216  PHE B CE1   1 
ATOM   10308 C CE2   . PHE B  1 218  ? -17.211 16.028  121.550 1.00 46.15 ? 216  PHE B CE2   1 
ATOM   10309 C CZ    . PHE B  1 218  ? -18.155 16.424  122.477 1.00 48.54 ? 216  PHE B CZ    1 
ATOM   10310 N N     . SER B  1 219  ? -13.257 11.501  122.659 1.00 41.95 ? 217  SER B N     1 
ATOM   10311 C CA    . SER B  1 219  ? -11.898 10.978  122.671 1.00 39.23 ? 217  SER B CA    1 
ATOM   10312 C C     . SER B  1 219  ? -11.006 12.009  121.993 1.00 37.49 ? 217  SER B C     1 
ATOM   10313 O O     . SER B  1 219  ? -11.479 13.051  121.524 1.00 38.58 ? 217  SER B O     1 
ATOM   10314 C CB    . SER B  1 219  ? -11.812 9.602   121.998 1.00 37.45 ? 217  SER B CB    1 
ATOM   10315 O OG    . SER B  1 219  ? -12.005 9.698   120.596 1.00 41.82 ? 217  SER B OG    1 
ATOM   10316 N N     . TYR B  1 220  ? -9.703  11.733  121.947 1.00 37.08 ? 218  TYR B N     1 
ATOM   10317 C CA    . TYR B  1 220  ? -8.751  12.733  121.494 1.00 34.87 ? 218  TYR B CA    1 
ATOM   10318 C C     . TYR B  1 220  ? -7.731  12.127  120.541 1.00 32.92 ? 218  TYR B C     1 
ATOM   10319 O O     . TYR B  1 220  ? -7.423  10.937  120.594 1.00 36.56 ? 218  TYR B O     1 
ATOM   10320 C CB    . TYR B  1 220  ? -8.026  13.384  122.685 1.00 35.65 ? 218  TYR B CB    1 
ATOM   10321 C CG    . TYR B  1 220  ? -8.816  14.501  123.333 1.00 34.20 ? 218  TYR B CG    1 
ATOM   10322 C CD1   . TYR B  1 220  ? -9.800  14.229  124.274 1.00 38.14 ? 218  TYR B CD1   1 
ATOM   10323 C CD2   . TYR B  1 220  ? -8.575  15.826  122.999 1.00 33.09 ? 218  TYR B CD2   1 
ATOM   10324 C CE1   . TYR B  1 220  ? -10.525 15.245  124.861 1.00 38.45 ? 218  TYR B CE1   1 
ATOM   10325 C CE2   . TYR B  1 220  ? -9.286  16.848  123.579 1.00 36.10 ? 218  TYR B CE2   1 
ATOM   10326 C CZ    . TYR B  1 220  ? -10.261 16.553  124.512 1.00 37.23 ? 218  TYR B CZ    1 
ATOM   10327 O OH    . TYR B  1 220  ? -10.975 17.579  125.089 1.00 41.10 ? 218  TYR B OH    1 
ATOM   10328 N N     . SER B  1 221  ? -7.214  12.981  119.667 1.00 34.17 ? 219  SER B N     1 
ATOM   10329 C CA    . SER B  1 221  ? -6.051  12.688  118.840 1.00 31.05 ? 219  SER B CA    1 
ATOM   10330 C C     . SER B  1 221  ? -5.191  13.938  118.870 1.00 30.18 ? 219  SER B C     1 
ATOM   10331 O O     . SER B  1 221  ? -5.652  15.007  118.467 1.00 31.11 ? 219  SER B O     1 
ATOM   10332 C CB    . SER B  1 221  ? -6.458  12.336  117.404 1.00 34.16 ? 219  SER B CB    1 
ATOM   10333 O OG    . SER B  1 221  ? -5.316  12.151  116.580 1.00 33.15 ? 219  SER B OG    1 
ATOM   10334 N N     . TYR B  1 222  ? -3.966  13.822  119.373 1.00 31.89 ? 220  TYR B N     1 
ATOM   10335 C CA    . TYR B  1 222  ? -3.137  14.993  119.632 1.00 31.59 ? 220  TYR B CA    1 
ATOM   10336 C C     . TYR B  1 222  ? -2.237  15.301  118.447 1.00 32.83 ? 220  TYR B C     1 
ATOM   10337 O O     . TYR B  1 222  ? -1.598  14.405  117.888 1.00 31.95 ? 220  TYR B O     1 
ATOM   10338 C CB    . TYR B  1 222  ? -2.300  14.789  120.887 1.00 29.95 ? 220  TYR B CB    1 
ATOM   10339 C CG    . TYR B  1 222  ? -3.176  14.643  122.092 1.00 30.98 ? 220  TYR B CG    1 
ATOM   10340 C CD1   . TYR B  1 222  ? -3.769  15.757  122.669 1.00 31.20 ? 220  TYR B CD1   1 
ATOM   10341 C CD2   . TYR B  1 222  ? -3.463  13.394  122.621 1.00 31.94 ? 220  TYR B CD2   1 
ATOM   10342 C CE1   . TYR B  1 222  ? -4.595  15.635  123.770 1.00 32.06 ? 220  TYR B CE1   1 
ATOM   10343 C CE2   . TYR B  1 222  ? -4.296  13.262  123.723 1.00 33.36 ? 220  TYR B CE2   1 
ATOM   10344 C CZ    . TYR B  1 222  ? -4.856  14.387  124.291 1.00 33.00 ? 220  TYR B CZ    1 
ATOM   10345 O OH    . TYR B  1 222  ? -5.691  14.265  125.385 1.00 34.07 ? 220  TYR B OH    1 
ATOM   10346 N N     . ASP B  1 223  ? -2.177  16.573  118.102 1.00 29.50 ? 221  ASP B N     1 
ATOM   10347 C CA    . ASP B  1 223  ? -1.426  17.088  116.963 1.00 33.62 ? 221  ASP B CA    1 
ATOM   10348 C C     . ASP B  1 223  ? -0.293  17.934  117.533 1.00 36.13 ? 221  ASP B C     1 
ATOM   10349 O O     . ASP B  1 223  ? -0.518  19.051  118.009 1.00 34.48 ? 221  ASP B O     1 
ATOM   10350 C CB    . ASP B  1 223  ? -2.356  17.890  116.063 1.00 36.33 ? 221  ASP B CB    1 
ATOM   10351 C CG    . ASP B  1 223  ? -1.615  18.686  115.006 1.00 43.64 ? 221  ASP B CG    1 
ATOM   10352 O OD1   . ASP B  1 223  ? -0.454  18.342  114.686 1.00 41.91 ? 221  ASP B OD1   1 
ATOM   10353 O OD2   . ASP B  1 223  ? -2.213  19.659  114.493 1.00 41.51 ? 221  ASP B OD2   1 
ATOM   10354 N N     . MET B  1 224  ? 0.924   17.400  117.496 1.00 33.89 ? 222  MET B N     1 
ATOM   10355 C CA    . MET B  1 224  ? 2.043   18.049  118.167 1.00 37.76 ? 222  MET B CA    1 
ATOM   10356 C C     . MET B  1 224  ? 2.565   19.275  117.419 1.00 40.92 ? 222  MET B C     1 
ATOM   10357 O O     . MET B  1 224  ? 3.649   19.761  117.749 1.00 48.43 ? 222  MET B O     1 
ATOM   10358 C CB    . MET B  1 224  ? 3.162   17.033  118.395 1.00 35.44 ? 222  MET B CB    1 
ATOM   10359 C CG    . MET B  1 224  ? 2.729   15.874  119.285 1.00 38.57 ? 222  MET B CG    1 
ATOM   10360 S SD    . MET B  1 224  ? 2.024   16.465  120.844 1.00 45.01 ? 222  MET B SD    1 
ATOM   10361 C CE    . MET B  1 224  ? 3.421   17.396  121.473 1.00 34.96 ? 222  MET B CE    1 
ATOM   10362 N N     . LEU B  1 225  ? 1.802   19.788  116.459 1.00 40.98 ? 223  LEU B N     1 
ATOM   10363 C CA    . LEU B  1 225  ? 2.121   20.994  115.701 1.00 46.26 ? 223  LEU B CA    1 
ATOM   10364 C C     . LEU B  1 225  ? 3.569   21.003  115.235 1.00 53.92 ? 223  LEU B C     1 
ATOM   10365 O O     . LEU B  1 225  ? 4.434   21.642  115.847 1.00 54.19 ? 223  LEU B O     1 
ATOM   10366 C CB    . LEU B  1 225  ? 1.793   22.244  116.519 1.00 44.63 ? 223  LEU B CB    1 
ATOM   10367 C CG    . LEU B  1 225  ? 0.268   22.404  116.641 1.00 45.95 ? 223  LEU B CG    1 
ATOM   10368 C CD1   . LEU B  1 225  ? -0.127  23.646  117.437 1.00 46.98 ? 223  LEU B CD1   1 
ATOM   10369 C CD2   . LEU B  1 225  ? -0.395  22.396  115.265 1.00 42.57 ? 223  LEU B CD2   1 
ATOM   10370 N N     . GLY B  1 226  ? 3.823   20.264  114.159 1.00 51.77 ? 224  GLY B N     1 
ATOM   10371 C CA    . GLY B  1 226  ? 5.077   20.259  113.436 1.00 45.47 ? 224  GLY B CA    1 
ATOM   10372 C C     . GLY B  1 226  ? 4.789   19.832  112.013 1.00 44.92 ? 224  GLY B C     1 
ATOM   10373 O O     . GLY B  1 226  ? 3.947   18.957  111.788 1.00 45.25 ? 224  GLY B O     1 
ATOM   10374 N N     . GLU B  1 227  ? 5.438   20.463  111.042 1.00 46.83 ? 225  GLU B N     1 
ATOM   10375 C CA    . GLU B  1 227  ? 5.287   20.057  109.650 1.00 43.43 ? 225  GLU B CA    1 
ATOM   10376 C C     . GLU B  1 227  ? 6.354   20.758  108.832 1.00 41.02 ? 225  GLU B C     1 
ATOM   10377 O O     . GLU B  1 227  ? 6.959   21.738  109.278 1.00 45.22 ? 225  GLU B O     1 
ATOM   10378 C CB    . GLU B  1 227  ? 3.895   20.384  109.097 1.00 43.41 ? 225  GLU B CB    1 
ATOM   10379 C CG    . GLU B  1 227  ? 3.507   21.839  109.225 1.00 45.65 ? 225  GLU B CG    1 
ATOM   10380 C CD    . GLU B  1 227  ? 2.066   22.086  108.810 1.00 50.79 ? 225  GLU B CD    1 
ATOM   10381 O OE1   . GLU B  1 227  ? 1.719   21.776  107.649 1.00 50.18 ? 225  GLU B OE1   1 
ATOM   10382 O OE2   . GLU B  1 227  ? 1.281   22.581  109.649 1.00 54.03 ? 225  GLU B OE2   1 
ATOM   10383 N N     . ALA B  1 228  ? 6.572   20.235  107.628 1.00 38.27 ? 226  ALA B N     1 
ATOM   10384 C CA    . ALA B  1 228  ? 7.515   20.798  106.670 1.00 34.51 ? 226  ALA B CA    1 
ATOM   10385 C C     . ALA B  1 228  ? 8.861   21.090  107.339 1.00 37.98 ? 226  ALA B C     1 
ATOM   10386 O O     . ALA B  1 228  ? 9.283   22.237  107.502 1.00 37.74 ? 226  ALA B O     1 
ATOM   10387 C CB    . ALA B  1 228  ? 6.934   22.054  106.016 1.00 33.08 ? 226  ALA B CB    1 
ATOM   10388 N N     . ALA B  1 229  ? 9.509   20.004  107.752 1.00 33.08 ? 227  ALA B N     1 
ATOM   10389 C CA    . ALA B  1 229  ? 10.895  20.086  108.190 1.00 32.93 ? 227  ALA B CA    1 
ATOM   10390 C C     . ALA B  1 229  ? 11.757  20.697  107.084 1.00 30.61 ? 227  ALA B C     1 
ATOM   10391 O O     . ALA B  1 229  ? 11.716  20.254  105.935 1.00 32.82 ? 227  ALA B O     1 
ATOM   10392 C CB    . ALA B  1 229  ? 11.401  18.695  108.555 1.00 25.56 ? 227  ALA B CB    1 
ATOM   10393 N N     . THR B  1 230  ? 12.509  21.741  107.427 1.00 30.10 ? 228  THR B N     1 
ATOM   10394 C CA    . THR B  1 230  ? 13.440  22.371  106.497 1.00 32.45 ? 228  THR B CA    1 
ATOM   10395 C C     . THR B  1 230  ? 14.835  21.748  106.550 1.00 32.31 ? 228  THR B C     1 
ATOM   10396 O O     . THR B  1 230  ? 15.502  21.618  105.516 1.00 30.38 ? 228  THR B O     1 
ATOM   10397 C CB    . THR B  1 230  ? 13.531  23.871  106.795 1.00 34.23 ? 228  THR B CB    1 
ATOM   10398 O OG1   . THR B  1 230  ? 12.216  24.432  106.779 1.00 36.10 ? 228  THR B OG1   1 
ATOM   10399 C CG2   . THR B  1 230  ? 14.385  24.579  105.750 1.00 29.72 ? 228  THR B CG2   1 
ATOM   10400 N N     . THR B  1 231  ? 15.293  21.361  107.735 1.00 25.66 ? 229  THR B N     1 
ATOM   10401 C CA    . THR B  1 231  ? 16.630  20.826  107.918 1.00 28.97 ? 229  THR B CA    1 
ATOM   10402 C C     . THR B  1 231  ? 16.555  19.442  108.546 1.00 29.98 ? 229  THR B C     1 
ATOM   10403 O O     . THR B  1 231  ? 15.526  19.040  109.101 1.00 25.88 ? 229  THR B O     1 
ATOM   10404 C CB    . THR B  1 231  ? 17.483  21.731  108.815 1.00 30.36 ? 229  THR B CB    1 
ATOM   10405 O OG1   . THR B  1 231  ? 16.993  21.648  110.163 1.00 31.25 ? 229  THR B OG1   1 
ATOM   10406 C CG2   . THR B  1 231  ? 17.441  23.187  108.335 1.00 30.20 ? 229  THR B CG2   1 
ATOM   10407 N N     . ALA B  1 232  ? 17.673  18.715  108.464 1.00 26.09 ? 230  ALA B N     1 
ATOM   10408 C CA    . ALA B  1 232  ? 17.752  17.429  109.149 1.00 30.70 ? 230  ALA B CA    1 
ATOM   10409 C C     . ALA B  1 232  ? 17.480  17.590  110.641 1.00 28.54 ? 230  ALA B C     1 
ATOM   10410 O O     . ALA B  1 232  ? 16.818  16.745  111.252 1.00 30.20 ? 230  ALA B O     1 
ATOM   10411 C CB    . ALA B  1 232  ? 19.124  16.786  108.920 1.00 31.06 ? 230  ALA B CB    1 
ATOM   10412 N N     . ALA B  1 233  ? 17.984  18.671  111.247 1.00 29.50 ? 231  ALA B N     1 
ATOM   10413 C CA    . ALA B  1 233  ? 17.815  18.852  112.689 1.00 31.45 ? 231  ALA B CA    1 
ATOM   10414 C C     . ALA B  1 233  ? 16.350  19.089  113.046 1.00 31.95 ? 231  ALA B C     1 
ATOM   10415 O O     . ALA B  1 233  ? 15.877  18.613  114.087 1.00 32.28 ? 231  ALA B O     1 
ATOM   10416 C CB    . ALA B  1 233  ? 18.687  20.007  113.187 1.00 30.70 ? 231  ALA B CB    1 
ATOM   10417 N N     . ASP B  1 234  ? 15.625  19.835  112.202 1.00 27.01 ? 232  ASP B N     1 
ATOM   10418 C CA    . ASP B  1 234  ? 14.185  19.991  112.387 1.00 30.25 ? 232  ASP B CA    1 
ATOM   10419 C C     . ASP B  1 234  ? 13.498  18.630  112.418 1.00 31.87 ? 232  ASP B C     1 
ATOM   10420 O O     . ASP B  1 234  ? 12.694  18.339  113.312 1.00 31.41 ? 232  ASP B O     1 
ATOM   10421 C CB    . ASP B  1 234  ? 13.576  20.829  111.249 1.00 28.47 ? 232  ASP B CB    1 
ATOM   10422 C CG    . ASP B  1 234  ? 14.025  22.278  111.253 1.00 35.47 ? 232  ASP B CG    1 
ATOM   10423 O OD1   . ASP B  1 234  ? 14.503  22.781  112.290 1.00 35.74 ? 232  ASP B OD1   1 
ATOM   10424 O OD2   . ASP B  1 234  ? 13.862  22.923  110.195 1.00 38.05 ? 232  ASP B OD2   1 
ATOM   10425 N N     . ALA B  1 235  ? 13.797  17.790  111.426 1.00 28.81 ? 233  ALA B N     1 
ATOM   10426 C CA    . ALA B  1 235  ? 13.127  16.503  111.313 1.00 28.80 ? 233  ALA B CA    1 
ATOM   10427 C C     . ALA B  1 235  ? 13.467  15.601  112.489 1.00 29.95 ? 233  ALA B C     1 
ATOM   10428 O O     . ALA B  1 235  ? 12.595  14.899  113.008 1.00 25.75 ? 233  ALA B O     1 
ATOM   10429 C CB    . ALA B  1 235  ? 13.501  15.834  109.990 1.00 30.26 ? 233  ALA B CB    1 
ATOM   10430 N N     . GLU B  1 236  ? 14.721  15.628  112.946 1.00 27.68 ? 234  GLU B N     1 
ATOM   10431 C CA    . GLU B  1 236  ? 15.083  14.809  114.093 1.00 31.27 ? 234  GLU B CA    1 
ATOM   10432 C C     . GLU B  1 236  ? 14.366  15.284  115.351 1.00 28.11 ? 234  GLU B C     1 
ATOM   10433 O O     . GLU B  1 236  ? 13.921  14.467  116.166 1.00 30.91 ? 234  GLU B O     1 
ATOM   10434 C CB    . GLU B  1 236  ? 16.603  14.816  114.290 1.00 31.66 ? 234  GLU B CB    1 
ATOM   10435 C CG    . GLU B  1 236  ? 17.096  13.696  115.174 1.00 31.59 ? 234  GLU B CG    1 
ATOM   10436 C CD    . GLU B  1 236  ? 18.611  13.683  115.292 1.00 44.16 ? 234  GLU B CD    1 
ATOM   10437 O OE1   . GLU B  1 236  ? 19.273  14.497  114.604 1.00 40.34 ? 234  GLU B OE1   1 
ATOM   10438 O OE2   . GLU B  1 236  ? 19.134  12.855  116.072 1.00 41.08 ? 234  GLU B OE2   1 
ATOM   10439 N N     . ARG B  1 237  ? 14.215  16.595  115.510 1.00 28.49 ? 235  ARG B N     1 
ATOM   10440 C CA    . ARG B  1 237  ? 13.500  17.110  116.668 1.00 31.85 ? 235  ARG B CA    1 
ATOM   10441 C C     . ARG B  1 237  ? 12.023  16.737  116.613 1.00 29.97 ? 235  ARG B C     1 
ATOM   10442 O O     . ARG B  1 237  ? 11.455  16.304  117.623 1.00 28.44 ? 235  ARG B O     1 
ATOM   10443 C CB    . ARG B  1 237  ? 13.670  18.625  116.764 1.00 34.94 ? 235  ARG B CB    1 
ATOM   10444 C CG    . ARG B  1 237  ? 12.607  19.270  117.607 1.00 36.42 ? 235  ARG B CG    1 
ATOM   10445 C CD    . ARG B  1 237  ? 12.833  20.730  117.814 1.00 40.11 ? 235  ARG B CD    1 
ATOM   10446 N NE    . ARG B  1 237  ? 12.203  21.141  119.061 1.00 44.92 ? 235  ARG B NE    1 
ATOM   10447 C CZ    . ARG B  1 237  ? 12.224  22.377  119.536 1.00 44.79 ? 235  ARG B CZ    1 
ATOM   10448 N NH1   . ARG B  1 237  ? 12.834  23.353  118.882 1.00 42.79 ? 235  ARG B NH1   1 
ATOM   10449 N NH2   . ARG B  1 237  ? 11.622  22.636  120.696 1.00 40.97 ? 235  ARG B NH2   1 
ATOM   10450 N N     . TYR B  1 238  ? 11.386  16.893  115.442 1.00 29.05 ? 236  TYR B N     1 
ATOM   10451 C CA    . TYR B  1 238  ? 9.985   16.493  115.306 1.00 30.69 ? 236  TYR B CA    1 
ATOM   10452 C C     . TYR B  1 238  ? 9.813   15.019  115.643 1.00 28.41 ? 236  TYR B C     1 
ATOM   10453 O O     . TYR B  1 238  ? 8.859   14.638  116.333 1.00 25.56 ? 236  TYR B O     1 
ATOM   10454 C CB    . TYR B  1 238  ? 9.453   16.790  113.892 1.00 28.39 ? 236  TYR B CB    1 
ATOM   10455 C CG    . TYR B  1 238  ? 9.262   18.264  113.595 1.00 32.47 ? 236  TYR B CG    1 
ATOM   10456 C CD1   . TYR B  1 238  ? 8.753   19.130  114.558 1.00 37.17 ? 236  TYR B CD1   1 
ATOM   10457 C CD2   . TYR B  1 238  ? 9.626   18.800  112.361 1.00 30.41 ? 236  TYR B CD2   1 
ATOM   10458 C CE1   . TYR B  1 238  ? 8.599   20.488  114.295 1.00 44.50 ? 236  TYR B CE1   1 
ATOM   10459 C CE2   . TYR B  1 238  ? 9.479   20.156  112.090 1.00 38.50 ? 236  TYR B CE2   1 
ATOM   10460 C CZ    . TYR B  1 238  ? 8.966   20.998  113.060 1.00 45.02 ? 236  TYR B CZ    1 
ATOM   10461 O OH    . TYR B  1 238  ? 8.824   22.350  112.792 1.00 44.35 ? 236  TYR B OH    1 
ATOM   10462 N N     . TYR B  1 239  ? 10.741  14.175  115.195 1.00 27.83 ? 237  TYR B N     1 
ATOM   10463 C CA    . TYR B  1 239  ? 10.649  12.759  115.537 1.00 27.41 ? 237  TYR B CA    1 
ATOM   10464 C C     . TYR B  1 239  ? 10.725  12.556  117.044 1.00 31.83 ? 237  TYR B C     1 
ATOM   10465 O O     . TYR B  1 239  ? 9.942   11.793  117.628 1.00 27.36 ? 237  TYR B O     1 
ATOM   10466 C CB    . TYR B  1 239  ? 11.755  11.969  114.842 1.00 27.86 ? 237  TYR B CB    1 
ATOM   10467 C CG    . TYR B  1 239  ? 11.838  10.546  115.319 1.00 32.75 ? 237  TYR B CG    1 
ATOM   10468 C CD1   . TYR B  1 239  ? 11.021  9.571   114.786 1.00 31.01 ? 237  TYR B CD1   1 
ATOM   10469 C CD2   . TYR B  1 239  ? 12.716  10.178  116.326 1.00 35.06 ? 237  TYR B CD2   1 
ATOM   10470 C CE1   . TYR B  1 239  ? 11.084  8.269   115.230 1.00 31.51 ? 237  TYR B CE1   1 
ATOM   10471 C CE2   . TYR B  1 239  ? 12.781  8.877   116.777 1.00 34.92 ? 237  TYR B CE2   1 
ATOM   10472 C CZ    . TYR B  1 239  ? 11.967  7.927   116.221 1.00 33.45 ? 237  TYR B CZ    1 
ATOM   10473 O OH    . TYR B  1 239  ? 12.034  6.628   116.662 1.00 41.57 ? 237  TYR B OH    1 
ATOM   10474 N N     . ARG B  1 240  ? 11.678  13.226  117.694 1.00 29.80 ? 238  ARG B N     1 
ATOM   10475 C CA    . ARG B  1 240  ? 11.821  13.065  119.133 1.00 30.07 ? 238  ARG B CA    1 
ATOM   10476 C C     . ARG B  1 240  ? 10.621  13.623  119.885 1.00 29.24 ? 238  ARG B C     1 
ATOM   10477 O O     . ARG B  1 240  ? 10.251  13.089  120.937 1.00 29.79 ? 238  ARG B O     1 
ATOM   10478 C CB    . ARG B  1 240  ? 13.113  13.734  119.606 1.00 32.74 ? 238  ARG B CB    1 
ATOM   10479 C CG    . ARG B  1 240  ? 14.357  13.064  119.061 1.00 35.35 ? 238  ARG B CG    1 
ATOM   10480 C CD    . ARG B  1 240  ? 14.483  11.641  119.582 1.00 32.79 ? 238  ARG B CD    1 
ATOM   10481 N NE    . ARG B  1 240  ? 15.590  10.934  118.951 1.00 38.18 ? 238  ARG B NE    1 
ATOM   10482 C CZ    . ARG B  1 240  ? 15.864  9.653   119.142 1.00 43.88 ? 238  ARG B CZ    1 
ATOM   10483 N NH1   . ARG B  1 240  ? 15.125  8.899   119.941 1.00 42.24 ? 238  ARG B NH1   1 
ATOM   10484 N NH2   . ARG B  1 240  ? 16.908  9.114   118.520 1.00 44.35 ? 238  ARG B NH2   1 
ATOM   10485 N N     . ASP B  1 241  ? 10.017  14.694  119.371 1.00 29.61 ? 239  ASP B N     1 
ATOM   10486 C CA    . ASP B  1 241  ? 8.788   15.217  119.960 1.00 32.36 ? 239  ASP B CA    1 
ATOM   10487 C C     . ASP B  1 241  ? 7.621   14.239  119.810 1.00 30.36 ? 239  ASP B C     1 
ATOM   10488 O O     . ASP B  1 241  ? 6.832   14.067  120.744 1.00 28.85 ? 239  ASP B O     1 
ATOM   10489 C CB    . ASP B  1 241  ? 8.441   16.558  119.330 1.00 31.69 ? 239  ASP B CB    1 
ATOM   10490 C CG    . ASP B  1 241  ? 9.374   17.676  119.781 1.00 36.94 ? 239  ASP B CG    1 
ATOM   10491 O OD1   . ASP B  1 241  ? 10.187  17.458  120.713 1.00 41.42 ? 239  ASP B OD1   1 
ATOM   10492 O OD2   . ASP B  1 241  ? 9.299   18.771  119.191 1.00 39.68 ? 239  ASP B OD2   1 
ATOM   10493 N N     . TYR B  1 242  ? 7.482   13.601  118.644 1.00 30.71 ? 240  TYR B N     1 
ATOM   10494 C CA    . TYR B  1 242  ? 6.432   12.594  118.480 1.00 29.09 ? 240  TYR B CA    1 
ATOM   10495 C C     . TYR B  1 242  ? 6.656   11.410  119.414 1.00 29.69 ? 240  TYR B C     1 
ATOM   10496 O O     . TYR B  1 242  ? 5.719   10.924  120.066 1.00 29.43 ? 240  TYR B O     1 
ATOM   10497 C CB    . TYR B  1 242  ? 6.389   12.113  117.033 1.00 27.29 ? 240  TYR B CB    1 
ATOM   10498 C CG    . TYR B  1 242  ? 5.777   13.054  116.010 1.00 28.36 ? 240  TYR B CG    1 
ATOM   10499 C CD1   . TYR B  1 242  ? 4.654   13.832  116.303 1.00 31.50 ? 240  TYR B CD1   1 
ATOM   10500 C CD2   . TYR B  1 242  ? 6.287   13.108  114.721 1.00 26.25 ? 240  TYR B CD2   1 
ATOM   10501 C CE1   . TYR B  1 242  ? 4.076   14.671  115.323 1.00 32.44 ? 240  TYR B CE1   1 
ATOM   10502 C CE2   . TYR B  1 242  ? 5.738   13.935  113.757 1.00 30.33 ? 240  TYR B CE2   1 
ATOM   10503 C CZ    . TYR B  1 242  ? 4.636   14.716  114.055 1.00 29.83 ? 240  TYR B CZ    1 
ATOM   10504 O OH    . TYR B  1 242  ? 4.103   15.515  113.057 1.00 30.55 ? 240  TYR B OH    1 
ATOM   10505 N N     . GLU B  1 243  ? 7.903   10.925  119.479 1.00 28.85 ? 241  GLU B N     1 
ATOM   10506 C CA    . GLU B  1 243  ? 8.247   9.809   120.353 1.00 29.80 ? 241  GLU B CA    1 
ATOM   10507 C C     . GLU B  1 243  ? 7.932   10.130  121.808 1.00 31.01 ? 241  GLU B C     1 
ATOM   10508 O O     . GLU B  1 243  ? 7.348   9.309   122.530 1.00 31.30 ? 241  GLU B O     1 
ATOM   10509 C CB    . GLU B  1 243  ? 9.728   9.469   120.188 1.00 30.34 ? 241  GLU B CB    1 
ATOM   10510 C CG    . GLU B  1 243  ? 10.177  8.248   120.946 1.00 35.79 ? 241  GLU B CG    1 
ATOM   10511 C CD    . GLU B  1 243  ? 11.691  8.191   121.092 1.00 37.21 ? 241  GLU B CD    1 
ATOM   10512 O OE1   . GLU B  1 243  ? 12.352  9.252   120.990 1.00 36.37 ? 241  GLU B OE1   1 
ATOM   10513 O OE2   . GLU B  1 243  ? 12.220  7.087   121.306 1.00 42.69 ? 241  GLU B OE2   1 
ATOM   10514 N N     . SER B  1 244  ? 8.331   11.322  122.261 1.00 30.02 ? 242  SER B N     1 
ATOM   10515 C CA    . SER B  1 244  ? 8.028   11.732  123.624 1.00 30.61 ? 242  SER B CA    1 
ATOM   10516 C C     . SER B  1 244  ? 6.521   11.791  123.867 1.00 30.93 ? 242  SER B C     1 
ATOM   10517 O O     . SER B  1 244  ? 6.032   11.327  124.906 1.00 31.83 ? 242  SER B O     1 
ATOM   10518 C CB    . SER B  1 244  ? 8.681   13.087  123.907 1.00 30.06 ? 242  SER B CB    1 
ATOM   10519 O OG    . SER B  1 244  ? 8.479   13.452  125.258 1.00 37.26 ? 242  SER B OG    1 
ATOM   10520 N N     . ALA B  1 245  ? 5.767   12.345  122.914 1.00 30.26 ? 243  ALA B N     1 
ATOM   10521 C CA    . ALA B  1 245  ? 4.323   12.472  123.093 1.00 31.14 ? 243  ALA B CA    1 
ATOM   10522 C C     . ALA B  1 245  ? 3.644   11.105  123.112 1.00 31.36 ? 243  ALA B C     1 
ATOM   10523 O O     . ALA B  1 245  ? 2.700   10.885  123.885 1.00 32.11 ? 243  ALA B O     1 
ATOM   10524 C CB    . ALA B  1 245  ? 3.733   13.358  121.992 1.00 30.91 ? 243  ALA B CB    1 
ATOM   10525 N N     . ILE B  1 246  ? 4.117   10.167  122.288 1.00 31.27 ? 244  ILE B N     1 
ATOM   10526 C CA    . ILE B  1 246  ? 3.524   8.829   122.289 1.00 32.83 ? 244  ILE B CA    1 
ATOM   10527 C C     . ILE B  1 246  ? 3.678   8.184   123.663 1.00 33.17 ? 244  ILE B C     1 
ATOM   10528 O O     . ILE B  1 246  ? 2.758   7.517   124.158 1.00 34.39 ? 244  ILE B O     1 
ATOM   10529 C CB    . ILE B  1 246  ? 4.131   7.959   121.169 1.00 31.83 ? 244  ILE B CB    1 
ATOM   10530 C CG1   . ILE B  1 246  ? 3.704   8.478   119.801 1.00 32.57 ? 244  ILE B CG1   1 
ATOM   10531 C CG2   . ILE B  1 246  ? 3.735   6.485   121.336 1.00 33.17 ? 244  ILE B CG2   1 
ATOM   10532 C CD1   . ILE B  1 246  ? 4.305   7.702   118.639 1.00 30.67 ? 244  ILE B CD1   1 
ATOM   10533 N N     . HIS B  1 247  ? 4.828   8.387   124.316 1.00 33.20 ? 245  HIS B N     1 
ATOM   10534 C CA    . HIS B  1 247  ? 5.003   7.849   125.665 1.00 34.24 ? 245  HIS B CA    1 
ATOM   10535 C C     . HIS B  1 247  ? 4.002   8.458   126.634 1.00 34.71 ? 245  HIS B C     1 
ATOM   10536 O O     . HIS B  1 247  ? 3.426   7.751   127.466 1.00 35.73 ? 245  HIS B O     1 
ATOM   10537 C CB    . HIS B  1 247  ? 6.426   8.097   126.166 1.00 34.15 ? 245  HIS B CB    1 
ATOM   10538 C CG    . HIS B  1 247  ? 7.440   7.166   125.585 1.00 34.15 ? 245  HIS B CG    1 
ATOM   10539 N ND1   . HIS B  1 247  ? 7.448   5.814   125.854 1.00 35.93 ? 245  HIS B ND1   1 
ATOM   10540 C CD2   . HIS B  1 247  ? 8.477   7.392   124.746 1.00 34.30 ? 245  HIS B CD2   1 
ATOM   10541 C CE1   . HIS B  1 247  ? 8.451   5.247   125.207 1.00 39.62 ? 245  HIS B CE1   1 
ATOM   10542 N NE2   . HIS B  1 247  ? 9.093   6.183   124.530 1.00 38.09 ? 245  HIS B NE2   1 
ATOM   10543 N N     . ALA B  1 248  ? 3.790   9.770   126.548 1.00 34.02 ? 246  ALA B N     1 
ATOM   10544 C CA    . ALA B  1 248  ? 2.830   10.424  127.430 1.00 34.47 ? 246  ALA B CA    1 
ATOM   10545 C C     . ALA B  1 248  ? 1.406   9.967   127.133 1.00 34.87 ? 246  ALA B C     1 
ATOM   10546 O O     . ALA B  1 248  ? 0.659   9.602   128.045 1.00 35.85 ? 246  ALA B O     1 
ATOM   10547 C CB    . ALA B  1 248  ? 2.937   11.943  127.292 1.00 33.63 ? 246  ALA B CB    1 
ATOM   10548 N N     . ILE B  1 249  ? 1.014   10.003  125.858 1.00 34.15 ? 247  ILE B N     1 
ATOM   10549 C CA    . ILE B  1 249  ? -0.348  9.633   125.473 1.00 35.70 ? 247  ILE B CA    1 
ATOM   10550 C C     . ILE B  1 249  ? -0.616  8.178   125.815 1.00 35.54 ? 247  ILE B C     1 
ATOM   10551 O O     . ILE B  1 249  ? -1.652  7.839   126.397 1.00 39.62 ? 247  ILE B O     1 
ATOM   10552 C CB    . ILE B  1 249  ? -0.568  9.901   123.974 1.00 33.51 ? 247  ILE B CB    1 
ATOM   10553 C CG1   . ILE B  1 249  ? -0.491  11.395  123.682 1.00 32.57 ? 247  ILE B CG1   1 
ATOM   10554 C CG2   . ILE B  1 249  ? -1.906  9.290   123.509 1.00 34.51 ? 247  ILE B CG2   1 
ATOM   10555 C CD1   . ILE B  1 249  ? -0.186  11.720  122.238 1.00 31.49 ? 247  ILE B CD1   1 
ATOM   10556 N N     . GLY B  1 250  ? 0.325   7.297   125.464 1.00 36.44 ? 248  GLY B N     1 
ATOM   10557 C CA    . GLY B  1 250  ? 0.158   5.887   125.764 1.00 36.57 ? 248  GLY B CA    1 
ATOM   10558 C C     . GLY B  1 250  ? -0.001  5.614   127.246 1.00 38.30 ? 248  GLY B C     1 
ATOM   10559 O O     . GLY B  1 250  ? -0.830  4.790   127.651 1.00 41.41 ? 248  GLY B O     1 
ATOM   10560 N N     . LYS B  1 251  ? 0.791   6.291   128.083 1.00 37.61 ? 249  LYS B N     1 
ATOM   10561 C CA    . LYS B  1 251  ? 0.635   6.103   129.523 1.00 38.71 ? 249  LYS B CA    1 
ATOM   10562 C C     . LYS B  1 251  ? -0.693  6.676   130.012 1.00 39.13 ? 249  LYS B C     1 
ATOM   10563 O O     . LYS B  1 251  ? -1.341  6.096   130.895 1.00 40.28 ? 249  LYS B O     1 
ATOM   10564 C CB    . LYS B  1 251  ? 1.814   6.740   130.268 1.00 39.54 ? 249  LYS B CB    1 
ATOM   10565 N N     . ALA B  1 252  ? -1.105  7.824   129.465 1.00 38.71 ? 250  ALA B N     1 
ATOM   10566 C CA    . ALA B  1 252  ? -2.414  8.381   129.796 1.00 40.04 ? 250  ALA B CA    1 
ATOM   10567 C C     . ALA B  1 252  ? -3.538  7.445   129.364 1.00 41.73 ? 250  ALA B C     1 
ATOM   10568 O O     . ALA B  1 252  ? -4.514  7.254   130.101 1.00 40.79 ? 250  ALA B O     1 
ATOM   10569 C CB    . ALA B  1 252  ? -2.583  9.751   129.140 1.00 41.58 ? 250  ALA B CB    1 
ATOM   10570 N N     . SER B  1 253  ? -3.417  6.857   128.169 1.00 41.48 ? 251  SER B N     1 
ATOM   10571 C CA    . SER B  1 253  ? -4.440  5.938   127.673 1.00 41.08 ? 251  SER B CA    1 
ATOM   10572 C C     . SER B  1 253  ? -4.730  4.828   128.675 1.00 42.48 ? 251  SER B C     1 
ATOM   10573 O O     . SER B  1 253  ? -5.885  4.422   128.845 1.00 44.33 ? 251  SER B O     1 
ATOM   10574 C CB    . SER B  1 253  ? -4.003  5.340   126.335 1.00 38.95 ? 251  SER B CB    1 
ATOM   10575 O OG    . SER B  1 253  ? -4.942  4.390   125.867 1.00 41.09 ? 251  SER B OG    1 
ATOM   10576 N N     . ALA B  1 254  ? -3.690  4.316   129.334 1.00 43.06 ? 252  ALA B N     1 
ATOM   10577 C CA    . ALA B  1 254  ? -3.822  3.304   130.384 1.00 47.22 ? 252  ALA B CA    1 
ATOM   10578 C C     . ALA B  1 254  ? -4.623  2.096   129.902 1.00 46.70 ? 252  ALA B C     1 
ATOM   10579 O O     . ALA B  1 254  ? -5.474  1.557   130.618 1.00 46.18 ? 252  ALA B O     1 
ATOM   10580 C CB    . ALA B  1 254  ? -4.438  3.901   131.651 1.00 48.11 ? 252  ALA B CB    1 
ATOM   10581 N N     . GLY B  1 255  ? -4.345  1.671   128.669 1.00 48.17 ? 253  GLY B N     1 
ATOM   10582 C CA    . GLY B  1 255  ? -4.947  0.469   128.128 1.00 47.19 ? 253  GLY B CA    1 
ATOM   10583 C C     . GLY B  1 255  ? -6.393  0.604   127.713 1.00 46.94 ? 253  GLY B C     1 
ATOM   10584 O O     . GLY B  1 255  ? -7.063  -0.409  127.505 1.00 49.21 ? 253  GLY B O     1 
ATOM   10585 N N     . ARG B  1 256  ? -6.900  1.830   127.592 1.00 45.66 ? 254  ARG B N     1 
ATOM   10586 C CA    . ARG B  1 256  ? -8.274  2.048   127.155 1.00 46.11 ? 254  ARG B CA    1 
ATOM   10587 C C     . ARG B  1 256  ? -8.495  1.663   125.699 1.00 46.42 ? 254  ARG B C     1 
ATOM   10588 O O     . ARG B  1 256  ? -9.651  1.602   125.265 1.00 46.02 ? 254  ARG B O     1 
ATOM   10589 C CB    . ARG B  1 256  ? -8.669  3.517   127.368 1.00 42.33 ? 254  ARG B CB    1 
ATOM   10590 C CG    . ARG B  1 256  ? -8.987  3.874   128.823 1.00 43.41 ? 254  ARG B CG    1 
ATOM   10591 C CD    . ARG B  1 256  ? -9.369  5.340   128.928 1.00 46.38 ? 254  ARG B CD    1 
ATOM   10592 N NE    . ARG B  1 256  ? -8.207  6.208   128.797 1.00 44.38 ? 254  ARG B NE    1 
ATOM   10593 C CZ    . ARG B  1 256  ? -8.262  7.526   128.664 1.00 45.57 ? 254  ARG B CZ    1 
ATOM   10594 N NH1   . ARG B  1 256  ? -9.417  8.162   128.555 1.00 44.18 ? 254  ARG B NH1   1 
ATOM   10595 N NH2   . ARG B  1 256  ? -7.128  8.223   128.651 1.00 44.26 ? 254  ARG B NH2   1 
ATOM   10596 N N     . GLY B  1 257  ? -7.428  1.417   124.941 1.00 46.10 ? 255  GLY B N     1 
ATOM   10597 C CA    . GLY B  1 257  ? -7.543  0.950   123.577 1.00 42.74 ? 255  GLY B CA    1 
ATOM   10598 C C     . GLY B  1 257  ? -7.747  2.080   122.588 1.00 43.46 ? 255  GLY B C     1 
ATOM   10599 O O     . GLY B  1 257  ? -7.955  3.243   122.942 1.00 42.88 ? 255  GLY B O     1 
ATOM   10600 N N     . ILE B  1 258  ? -7.709  1.715   121.303 1.00 42.30 ? 256  ILE B N     1 
ATOM   10601 C CA    . ILE B  1 258  ? -7.622  2.726   120.248 1.00 43.02 ? 256  ILE B CA    1 
ATOM   10602 C C     . ILE B  1 258  ? -8.929  3.454   119.969 1.00 41.97 ? 256  ILE B C     1 
ATOM   10603 O O     . ILE B  1 258  ? -8.909  4.461   119.250 1.00 40.60 ? 256  ILE B O     1 
ATOM   10604 C CB    . ILE B  1 258  ? -7.120  2.116   118.928 1.00 41.76 ? 256  ILE B CB    1 
ATOM   10605 C CG1   . ILE B  1 258  ? -8.066  1.030   118.440 1.00 43.56 ? 256  ILE B CG1   1 
ATOM   10606 C CG2   . ILE B  1 258  ? -5.711  1.553   119.086 1.00 40.97 ? 256  ILE B CG2   1 
ATOM   10607 C CD1   . ILE B  1 258  ? -7.612  0.423   117.142 1.00 40.71 ? 256  ILE B CD1   1 
ATOM   10608 N N     . TYR B  1 259  ? -10.062 2.990   120.507 1.00 42.82 ? 257  TYR B N     1 
ATOM   10609 C CA    . TYR B  1 259  ? -11.328 3.683   120.276 1.00 40.55 ? 257  TYR B CA    1 
ATOM   10610 C C     . TYR B  1 259  ? -11.713 4.593   121.435 1.00 43.44 ? 257  TYR B C     1 
ATOM   10611 O O     . TYR B  1 259  ? -12.095 5.747   121.216 1.00 43.42 ? 257  TYR B O     1 
ATOM   10612 C CB    . TYR B  1 259  ? -12.454 2.674   119.987 1.00 43.66 ? 257  TYR B CB    1 
ATOM   10613 C CG    . TYR B  1 259  ? -12.089 1.720   118.875 1.00 42.62 ? 257  TYR B CG    1 
ATOM   10614 C CD1   . TYR B  1 259  ? -11.928 2.177   117.568 1.00 43.62 ? 257  TYR B CD1   1 
ATOM   10615 C CD2   . TYR B  1 259  ? -11.882 0.371   119.130 1.00 42.45 ? 257  TYR B CD2   1 
ATOM   10616 C CE1   . TYR B  1 259  ? -11.572 1.317   116.545 1.00 40.43 ? 257  TYR B CE1   1 
ATOM   10617 C CE2   . TYR B  1 259  ? -11.530 -0.499  118.113 1.00 44.83 ? 257  TYR B CE2   1 
ATOM   10618 C CZ    . TYR B  1 259  ? -11.376 -0.019  116.822 1.00 44.12 ? 257  TYR B CZ    1 
ATOM   10619 O OH    . TYR B  1 259  ? -11.017 -0.878  115.808 1.00 45.92 ? 257  TYR B OH    1 
ATOM   10620 N N     . GLU B  1 260  ? -11.626 4.100   122.669 1.00 41.36 ? 258  GLU B N     1 
ATOM   10621 C CA    . GLU B  1 260  ? -11.927 4.960   123.807 1.00 46.15 ? 258  GLU B CA    1 
ATOM   10622 C C     . GLU B  1 260  ? -10.740 5.845   124.164 1.00 46.27 ? 258  GLU B C     1 
ATOM   10623 O O     . GLU B  1 260  ? -10.920 7.016   124.524 1.00 46.63 ? 258  GLU B O     1 
ATOM   10624 C CB    . GLU B  1 260  ? -12.352 4.118   125.012 1.00 42.22 ? 258  GLU B CB    1 
ATOM   10625 N N     . GLY B  1 261  ? -9.525  5.318   124.038 1.00 47.27 ? 259  GLY B N     1 
ATOM   10626 C CA    . GLY B  1 261  ? -8.340  6.031   124.463 1.00 44.53 ? 259  GLY B CA    1 
ATOM   10627 C C     . GLY B  1 261  ? -7.860  7.042   123.445 1.00 42.54 ? 259  GLY B C     1 
ATOM   10628 O O     . GLY B  1 261  ? -8.327  7.110   122.296 1.00 40.97 ? 259  GLY B O     1 
ATOM   10629 N N     . PRO B  1 262  ? -6.896  7.856   123.860 1.00 39.68 ? 260  PRO B N     1 
ATOM   10630 C CA    . PRO B  1 262  ? -6.364  8.881   122.962 1.00 36.27 ? 260  PRO B CA    1 
ATOM   10631 C C     . PRO B  1 262  ? -5.351  8.302   121.989 1.00 34.86 ? 260  PRO B C     1 
ATOM   10632 O O     . PRO B  1 262  ? -4.784  7.226   122.190 1.00 40.39 ? 260  PRO B O     1 
ATOM   10633 C CB    . PRO B  1 262  ? -5.703  9.883   123.917 1.00 36.85 ? 260  PRO B CB    1 
ATOM   10634 C CG    . PRO B  1 262  ? -5.304  9.057   125.100 1.00 36.24 ? 260  PRO B CG    1 
ATOM   10635 C CD    . PRO B  1 262  ? -6.303  7.932   125.209 1.00 39.73 ? 260  PRO B CD    1 
ATOM   10636 N N     . GLY B  1 263  ? -5.119  9.063   120.920 1.00 33.77 ? 261  GLY B N     1 
ATOM   10637 C CA    . GLY B  1 263  ? -4.167  8.695   119.897 1.00 32.98 ? 261  GLY B CA    1 
ATOM   10638 C C     . GLY B  1 263  ? -3.331  9.899   119.523 1.00 31.90 ? 261  GLY B C     1 
ATOM   10639 O O     . GLY B  1 263  ? -3.454  10.973  120.123 1.00 32.32 ? 261  GLY B O     1 
ATOM   10640 N N     . ILE B  1 264  ? -2.487  9.706   118.512 1.00 31.17 ? 262  ILE B N     1 
ATOM   10641 C CA    . ILE B  1 264  ? -1.611  10.756  118.015 1.00 30.70 ? 262  ILE B CA    1 
ATOM   10642 C C     . ILE B  1 264  ? -1.772  10.838  116.508 1.00 30.12 ? 262  ILE B C     1 
ATOM   10643 O O     . ILE B  1 264  ? -2.052  9.836   115.840 1.00 29.68 ? 262  ILE B O     1 
ATOM   10644 C CB    . ILE B  1 264  ? -0.128  10.522  118.403 1.00 30.53 ? 262  ILE B CB    1 
ATOM   10645 C CG1   . ILE B  1 264  ? 0.691   11.805  118.233 1.00 30.34 ? 262  ILE B CG1   1 
ATOM   10646 C CG2   . ILE B  1 264  ? 0.503   9.415   117.582 1.00 30.03 ? 262  ILE B CG2   1 
ATOM   10647 C CD1   . ILE B  1 264  ? 2.098   11.668  118.807 1.00 29.77 ? 262  ILE B CD1   1 
ATOM   10648 N N     . SER B  1 265  ? -1.636  12.058  115.987 1.00 28.77 ? 263  SER B N     1 
ATOM   10649 C CA    . SER B  1 265  ? -1.602  12.349  114.560 1.00 30.72 ? 263  SER B CA    1 
ATOM   10650 C C     . SER B  1 265  ? -0.235  12.917  114.210 1.00 30.48 ? 263  SER B C     1 
ATOM   10651 O O     . SER B  1 265  ? 0.281   13.776  114.927 1.00 31.75 ? 263  SER B O     1 
ATOM   10652 C CB    . SER B  1 265  ? -2.674  13.368  114.169 1.00 29.93 ? 263  SER B CB    1 
ATOM   10653 O OG    . SER B  1 265  ? -3.976  12.825  114.294 1.00 33.22 ? 263  SER B OG    1 
ATOM   10654 N N     . ILE B  1 266  ? 0.337   12.463  113.095 1.00 27.63 ? 264  ILE B N     1 
ATOM   10655 C CA    . ILE B  1 266  ? 1.648   12.926  112.662 1.00 25.81 ? 264  ILE B CA    1 
ATOM   10656 C C     . ILE B  1 266  ? 1.546   13.397  111.215 1.00 29.33 ? 264  ILE B C     1 
ATOM   10657 O O     . ILE B  1 266  ? 0.625   13.042  110.477 1.00 25.76 ? 264  ILE B O     1 
ATOM   10658 C CB    . ILE B  1 266  ? 2.740   11.838  112.799 1.00 27.34 ? 264  ILE B CB    1 
ATOM   10659 C CG1   . ILE B  1 266  ? 2.439   10.656  111.883 1.00 31.75 ? 264  ILE B CG1   1 
ATOM   10660 C CG2   . ILE B  1 266  ? 2.862   11.337  114.257 1.00 27.01 ? 264  ILE B CG2   1 
ATOM   10661 C CD1   . ILE B  1 266  ? 3.642   9.767   111.620 1.00 33.29 ? 264  ILE B CD1   1 
ATOM   10662 N N     . LYS B  1 267  ? 2.500   14.223  110.817 1.00 26.85 ? 265  LYS B N     1 
ATOM   10663 C CA    . LYS B  1 267  ? 2.628   14.630  109.422 1.00 26.22 ? 265  LYS B CA    1 
ATOM   10664 C C     . LYS B  1 267  ? 3.950   14.105  108.883 1.00 24.89 ? 265  LYS B C     1 
ATOM   10665 O O     . LYS B  1 267  ? 4.999   14.298  109.509 1.00 26.60 ? 265  LYS B O     1 
ATOM   10666 C CB    . LYS B  1 267  ? 2.537   16.151  109.276 1.00 29.67 ? 265  LYS B CB    1 
ATOM   10667 C CG    . LYS B  1 267  ? 1.101   16.675  109.343 1.00 32.54 ? 265  LYS B CG    1 
ATOM   10668 C CD    . LYS B  1 267  ? 1.021   18.170  109.034 1.00 38.79 ? 265  LYS B CD    1 
ATOM   10669 C CE    . LYS B  1 267  ? -0.375  18.719  109.338 1.00 42.17 ? 265  LYS B CE    1 
ATOM   10670 N NZ    . LYS B  1 267  ? -0.905  18.261  110.656 1.00 44.42 ? 265  LYS B NZ    1 
ATOM   10671 N N     . LEU B  1 268  ? 3.900   13.436  107.729 1.00 25.43 ? 266  LEU B N     1 
ATOM   10672 C CA    . LEU B  1 268  ? 5.117   12.861  107.174 1.00 25.74 ? 266  LEU B CA    1 
ATOM   10673 C C     . LEU B  1 268  ? 6.122   13.940  106.790 1.00 25.92 ? 266  LEU B C     1 
ATOM   10674 O O     . LEU B  1 268  ? 7.330   13.717  106.899 1.00 25.54 ? 266  LEU B O     1 
ATOM   10675 C CB    . LEU B  1 268  ? 4.779   11.968  105.976 1.00 23.54 ? 266  LEU B CB    1 
ATOM   10676 C CG    . LEU B  1 268  ? 3.965   10.698  106.282 1.00 26.49 ? 266  LEU B CG    1 
ATOM   10677 C CD1   . LEU B  1 268  ? 3.819   9.847   105.052 1.00 28.17 ? 266  LEU B CD1   1 
ATOM   10678 C CD2   . LEU B  1 268  ? 4.613   9.878   107.368 1.00 24.99 ? 266  LEU B CD2   1 
ATOM   10679 N N     . SER B  1 269  ? 5.653   15.118  106.360 1.00 24.09 ? 267  SER B N     1 
ATOM   10680 C CA    . SER B  1 269  ? 6.586   16.187  106.017 1.00 25.85 ? 267  SER B CA    1 
ATOM   10681 C C     . SER B  1 269  ? 7.369   16.677  107.231 1.00 24.04 ? 267  SER B C     1 
ATOM   10682 O O     . SER B  1 269  ? 8.446   17.267  107.071 1.00 26.96 ? 267  SER B O     1 
ATOM   10683 C CB    . SER B  1 269  ? 5.838   17.340  105.342 1.00 25.03 ? 267  SER B CB    1 
ATOM   10684 O OG    . SER B  1 269  ? 4.992   18.020  106.255 1.00 28.43 ? 267  SER B OG    1 
ATOM   10685 N N     . ALA B  1 270  ? 6.881   16.415  108.441 1.00 24.69 ? 268  ALA B N     1 
ATOM   10686 C CA    . ALA B  1 270  ? 7.644   16.792  109.625 1.00 25.04 ? 268  ALA B CA    1 
ATOM   10687 C C     . ALA B  1 270  ? 8.850   15.894  109.849 1.00 27.73 ? 268  ALA B C     1 
ATOM   10688 O O     . ALA B  1 270  ? 9.775   16.288  110.569 1.00 27.28 ? 268  ALA B O     1 
ATOM   10689 C CB    . ALA B  1 270  ? 6.759   16.754  110.874 1.00 30.14 ? 268  ALA B CB    1 
ATOM   10690 N N     . LEU B  1 271  ? 8.864   14.705  109.251 1.00 25.42 ? 269  LEU B N     1 
ATOM   10691 C CA    . LEU B  1 271  ? 9.833   13.681  109.600 1.00 24.29 ? 269  LEU B CA    1 
ATOM   10692 C C     . LEU B  1 271  ? 10.995  13.594  108.625 1.00 27.65 ? 269  LEU B C     1 
ATOM   10693 O O     . LEU B  1 271  ? 11.874  12.757  108.818 1.00 28.30 ? 269  LEU B O     1 
ATOM   10694 C CB    . LEU B  1 271  ? 9.138   12.324  109.691 1.00 24.48 ? 269  LEU B CB    1 
ATOM   10695 C CG    . LEU B  1 271  ? 8.190   12.193  110.870 1.00 29.88 ? 269  LEU B CG    1 
ATOM   10696 C CD1   . LEU B  1 271  ? 7.434   10.865  110.784 1.00 31.16 ? 269  LEU B CD1   1 
ATOM   10697 C CD2   . LEU B  1 271  ? 8.981   12.284  112.159 1.00 28.57 ? 269  LEU B CD2   1 
ATOM   10698 N N     . HIS B  1 272  ? 11.017  14.426  107.577 1.00 24.17 ? 270  HIS B N     1 
ATOM   10699 C CA    . HIS B  1 272  ? 12.121  14.371  106.634 1.00 28.13 ? 270  HIS B CA    1 
ATOM   10700 C C     . HIS B  1 272  ? 12.133  15.675  105.862 1.00 30.45 ? 270  HIS B C     1 
ATOM   10701 O O     . HIS B  1 272  ? 11.059  16.145  105.469 1.00 26.74 ? 270  HIS B O     1 
ATOM   10702 C CB    . HIS B  1 272  ? 11.978  13.191  105.666 1.00 30.39 ? 270  HIS B CB    1 
ATOM   10703 C CG    . HIS B  1 272  ? 13.225  12.908  104.905 1.00 31.39 ? 270  HIS B CG    1 
ATOM   10704 N ND1   . HIS B  1 272  ? 13.623  13.670  103.830 1.00 28.24 ? 270  HIS B ND1   1 
ATOM   10705 C CD2   . HIS B  1 272  ? 14.199  11.986  105.100 1.00 33.21 ? 270  HIS B CD2   1 
ATOM   10706 C CE1   . HIS B  1 272  ? 14.777  13.214  103.375 1.00 33.88 ? 270  HIS B CE1   1 
ATOM   10707 N NE2   . HIS B  1 272  ? 15.147  12.191  104.128 1.00 38.70 ? 270  HIS B NE2   1 
ATOM   10708 N N     . PRO B  1 273  ? 13.300  16.288  105.631 1.00 27.47 ? 271  PRO B N     1 
ATOM   10709 C CA    . PRO B  1 273  ? 13.325  17.574  104.914 1.00 27.22 ? 271  PRO B CA    1 
ATOM   10710 C C     . PRO B  1 273  ? 13.039  17.470  103.423 1.00 29.23 ? 271  PRO B C     1 
ATOM   10711 O O     . PRO B  1 273  ? 12.785  18.508  102.801 1.00 28.17 ? 271  PRO B O     1 
ATOM   10712 C CB    . PRO B  1 273  ? 14.748  18.096  105.163 1.00 26.85 ? 271  PRO B CB    1 
ATOM   10713 C CG    . PRO B  1 273  ? 15.555  16.875  105.477 1.00 30.24 ? 271  PRO B CG    1 
ATOM   10714 C CD    . PRO B  1 273  ? 14.625  15.907  106.153 1.00 31.30 ? 271  PRO B CD    1 
ATOM   10715 N N     . ARG B  1 274  ? 13.075  16.275  102.823 1.00 26.61 ? 272  ARG B N     1 
ATOM   10716 C CA    . ARG B  1 274  ? 12.855  16.121  101.385 1.00 24.62 ? 272  ARG B CA    1 
ATOM   10717 C C     . ARG B  1 274  ? 11.737  15.100  101.146 1.00 25.04 ? 272  ARG B C     1 
ATOM   10718 O O     . ARG B  1 274  ? 11.898  14.100  100.447 1.00 24.93 ? 272  ARG B O     1 
ATOM   10719 C CB    . ARG B  1 274  ? 14.125  15.685  100.651 1.00 26.73 ? 272  ARG B CB    1 
ATOM   10720 C CG    . ARG B  1 274  ? 15.297  16.679  100.712 1.00 26.34 ? 272  ARG B CG    1 
ATOM   10721 C CD    . ARG B  1 274  ? 14.907  18.062  100.166 1.00 25.92 ? 272  ARG B CD    1 
ATOM   10722 N NE    . ARG B  1 274  ? 14.386  17.971  98.804  1.00 28.66 ? 272  ARG B NE    1 
ATOM   10723 C CZ    . ARG B  1 274  ? 15.143  17.913  97.716  1.00 30.43 ? 272  ARG B CZ    1 
ATOM   10724 N NH1   . ARG B  1 274  ? 16.468  17.900  97.792  1.00 28.82 ? 272  ARG B NH1   1 
ATOM   10725 N NH2   . ARG B  1 274  ? 14.557  17.839  96.523  1.00 30.96 ? 272  ARG B NH2   1 
ATOM   10726 N N     . TYR B  1 275  ? 10.587  15.342  101.753 1.00 23.75 ? 273  TYR B N     1 
ATOM   10727 C CA    . TYR B  1 275  ? 9.457   14.431  101.592 1.00 26.28 ? 273  TYR B CA    1 
ATOM   10728 C C     . TYR B  1 275  ? 8.760   14.757  100.276 1.00 26.10 ? 273  TYR B C     1 
ATOM   10729 O O     . TYR B  1 275  ? 7.917   15.655  100.215 1.00 26.15 ? 273  TYR B O     1 
ATOM   10730 C CB    . TYR B  1 275  ? 8.514   14.552  102.782 1.00 24.83 ? 273  TYR B CB    1 
ATOM   10731 C CG    . TYR B  1 275  ? 7.254   13.738  102.616 1.00 24.74 ? 273  TYR B CG    1 
ATOM   10732 C CD1   . TYR B  1 275  ? 7.313   12.397  102.271 1.00 26.74 ? 273  TYR B CD1   1 
ATOM   10733 C CD2   . TYR B  1 275  ? 6.012   14.318  102.814 1.00 24.67 ? 273  TYR B CD2   1 
ATOM   10734 C CE1   . TYR B  1 275  ? 6.159   11.656  102.109 1.00 26.15 ? 273  TYR B CE1   1 
ATOM   10735 C CE2   . TYR B  1 275  ? 4.866   13.595  102.667 1.00 27.24 ? 273  TYR B CE2   1 
ATOM   10736 C CZ    . TYR B  1 275  ? 4.938   12.269  102.309 1.00 27.32 ? 273  TYR B CZ    1 
ATOM   10737 O OH    . TYR B  1 275  ? 3.782   11.557  102.164 1.00 27.96 ? 273  TYR B OH    1 
ATOM   10738 N N     . SER B  1 276  ? 9.111   14.030  99.213  1.00 26.99 ? 274  SER B N     1 
ATOM   10739 C CA    . SER B  1 276  ? 8.525   14.292  97.899  1.00 26.90 ? 274  SER B CA    1 
ATOM   10740 C C     . SER B  1 276  ? 8.805   13.117  96.972  1.00 25.97 ? 274  SER B C     1 
ATOM   10741 O O     . SER B  1 276  ? 9.752   12.354  97.172  1.00 28.52 ? 274  SER B O     1 
ATOM   10742 C CB    . SER B  1 276  ? 9.065   15.582  97.276  1.00 27.65 ? 274  SER B CB    1 
ATOM   10743 O OG    . SER B  1 276  ? 10.407  15.413  96.855  1.00 28.32 ? 274  SER B OG    1 
ATOM   10744 N N     . ARG B  1 277  ? 7.968   12.992  95.942  1.00 25.79 ? 275  ARG B N     1 
ATOM   10745 C CA    . ARG B  1 277  ? 8.144   11.915  94.974  1.00 27.54 ? 275  ARG B CA    1 
ATOM   10746 C C     . ARG B  1 277  ? 9.523   11.954  94.333  1.00 27.01 ? 275  ARG B C     1 
ATOM   10747 O O     . ARG B  1 277  ? 10.113  10.899  94.081  1.00 28.30 ? 275  ARG B O     1 
ATOM   10748 C CB    . ARG B  1 277  ? 7.052   11.983  93.906  1.00 24.58 ? 275  ARG B CB    1 
ATOM   10749 C CG    . ARG B  1 277  ? 7.205   10.982  92.779  1.00 28.08 ? 275  ARG B CG    1 
ATOM   10750 C CD    . ARG B  1 277  ? 7.236   9.555   93.301  1.00 29.93 ? 275  ARG B CD    1 
ATOM   10751 N NE    . ARG B  1 277  ? 7.409   8.580   92.229  1.00 30.13 ? 275  ARG B NE    1 
ATOM   10752 C CZ    . ARG B  1 277  ? 8.581   8.265   91.697  1.00 31.25 ? 275  ARG B CZ    1 
ATOM   10753 N NH1   . ARG B  1 277  ? 9.703   8.841   92.107  1.00 31.32 ? 275  ARG B NH1   1 
ATOM   10754 N NH2   . ARG B  1 277  ? 8.627   7.369   90.717  1.00 30.26 ? 275  ARG B NH2   1 
ATOM   10755 N N     . ALA B  1 278  ? 10.077  13.151  94.103  1.00 27.30 ? 276  ALA B N     1 
ATOM   10756 C CA    . ALA B  1 278  ? 11.389  13.234  93.465  1.00 28.20 ? 276  ALA B CA    1 
ATOM   10757 C C     . ALA B  1 278  ? 12.482  12.599  94.313  1.00 28.87 ? 276  ALA B C     1 
ATOM   10758 O O     . ALA B  1 278  ? 13.499  12.156  93.765  1.00 30.77 ? 276  ALA B O     1 
ATOM   10759 C CB    . ALA B  1 278  ? 11.750  14.689  93.153  1.00 28.12 ? 276  ALA B CB    1 
ATOM   10760 N N     . GLN B  1 279  ? 12.285  12.515  95.629  1.00 27.61 ? 277  GLN B N     1 
ATOM   10761 C CA    . GLN B  1 279  ? 13.254  11.924  96.544  1.00 26.48 ? 277  GLN B CA    1 
ATOM   10762 C C     . GLN B  1 279  ? 12.722  10.649  97.188  1.00 29.90 ? 277  GLN B C     1 
ATOM   10763 O O     . GLN B  1 279  ? 13.068  10.332  98.332  1.00 28.52 ? 277  GLN B O     1 
ATOM   10764 C CB    . GLN B  1 279  ? 13.650  12.934  97.618  1.00 29.35 ? 277  GLN B CB    1 
ATOM   10765 C CG    . GLN B  1 279  ? 14.256  14.217  97.063  1.00 28.48 ? 277  GLN B CG    1 
ATOM   10766 C CD    . GLN B  1 279  ? 15.580  13.969  96.378  1.00 32.00 ? 277  GLN B CD    1 
ATOM   10767 O OE1   . GLN B  1 279  ? 16.313  13.038  96.730  1.00 35.51 ? 277  GLN B OE1   1 
ATOM   10768 N NE2   . GLN B  1 279  ? 15.892  14.786  95.383  1.00 28.31 ? 277  GLN B NE2   1 
ATOM   10769 N N     . ALA B  1 280  ? 11.894  9.902   96.446  1.00 28.84 ? 278  ALA B N     1 
ATOM   10770 C CA    . ALA B  1 280  ? 11.247  8.702   96.974  1.00 28.96 ? 278  ALA B CA    1 
ATOM   10771 C C     . ALA B  1 280  ? 12.250  7.703   97.540  1.00 31.14 ? 278  ALA B C     1 
ATOM   10772 O O     . ALA B  1 280  ? 11.942  7.004   98.516  1.00 29.29 ? 278  ALA B O     1 
ATOM   10773 C CB    . ALA B  1 280  ? 10.405  8.034   95.877  1.00 26.24 ? 278  ALA B CB    1 
ATOM   10774 N N     . ALA B  1 281  ? 13.440  7.604   96.938  1.00 29.79 ? 279  ALA B N     1 
ATOM   10775 C CA    . ALA B  1 281  ? 14.456  6.705   97.480  1.00 33.32 ? 279  ALA B CA    1 
ATOM   10776 C C     . ALA B  1 281  ? 14.822  7.100   98.904  1.00 32.48 ? 279  ALA B C     1 
ATOM   10777 O O     . ALA B  1 281  ? 14.846  6.256   99.807  1.00 32.55 ? 279  ALA B O     1 
ATOM   10778 C CB    . ALA B  1 281  ? 15.700  6.704   96.593  1.00 34.60 ? 279  ALA B CB    1 
ATOM   10779 N N     . ARG B  1 282  ? 15.100  8.389   99.125  1.00 30.67 ? 280  ARG B N     1 
ATOM   10780 C CA    . ARG B  1 282  ? 15.424  8.851   100.469 1.00 33.90 ? 280  ARG B CA    1 
ATOM   10781 C C     . ARG B  1 282  ? 14.233  8.700   101.409 1.00 31.85 ? 280  ARG B C     1 
ATOM   10782 O O     . ARG B  1 282  ? 14.402  8.418   102.600 1.00 35.39 ? 280  ARG B O     1 
ATOM   10783 C CB    . ARG B  1 282  ? 15.894  10.305  100.424 1.00 32.97 ? 280  ARG B CB    1 
ATOM   10784 C CG    . ARG B  1 282  ? 17.203  10.512  99.691  1.00 32.89 ? 280  ARG B CG    1 
ATOM   10785 C CD    . ARG B  1 282  ? 17.773  11.883  99.992  1.00 34.22 ? 280  ARG B CD    1 
ATOM   10786 N NE    . ARG B  1 282  ? 18.022  12.055  101.418 1.00 33.38 ? 280  ARG B NE    1 
ATOM   10787 C CZ    . ARG B  1 282  ? 18.176  13.228  102.015 1.00 36.16 ? 280  ARG B CZ    1 
ATOM   10788 N NH1   . ARG B  1 282  ? 18.143  14.365  101.328 1.00 31.98 ? 280  ARG B NH1   1 
ATOM   10789 N NH2   . ARG B  1 282  ? 18.344  13.263  103.337 1.00 30.67 ? 280  ARG B NH2   1 
ATOM   10790 N N     . VAL B  1 283  ? 13.023  8.907   100.897 1.00 29.86 ? 281  VAL B N     1 
ATOM   10791 C CA    . VAL B  1 283  ? 11.837  8.804   101.739 1.00 28.87 ? 281  VAL B CA    1 
ATOM   10792 C C     . VAL B  1 283  ? 11.673  7.376   102.240 1.00 31.21 ? 281  VAL B C     1 
ATOM   10793 O O     . VAL B  1 283  ? 11.478  7.142   103.439 1.00 31.90 ? 281  VAL B O     1 
ATOM   10794 C CB    . VAL B  1 283  ? 10.595  9.299   100.972 1.00 27.01 ? 281  VAL B CB    1 
ATOM   10795 C CG1   . VAL B  1 283  ? 9.308   8.875   101.686 1.00 28.69 ? 281  VAL B CG1   1 
ATOM   10796 C CG2   . VAL B  1 283  ? 10.663  10.813  100.827 1.00 27.06 ? 281  VAL B CG2   1 
ATOM   10797 N N     . MET B  1 284  ? 11.793  6.394   101.342 1.00 28.36 ? 282  MET B N     1 
ATOM   10798 C CA    . MET B  1 284  ? 11.629  5.008   101.781 1.00 30.62 ? 282  MET B CA    1 
ATOM   10799 C C     . MET B  1 284  ? 12.777  4.548   102.676 1.00 34.05 ? 282  MET B C     1 
ATOM   10800 O O     . MET B  1 284  ? 12.573  3.705   103.556 1.00 33.24 ? 282  MET B O     1 
ATOM   10801 C CB    . MET B  1 284  ? 11.498  4.075   100.581 1.00 32.87 ? 282  MET B CB    1 
ATOM   10802 C CG    . MET B  1 284  ? 10.290  4.366   99.705  1.00 31.76 ? 282  MET B CG    1 
ATOM   10803 S SD    . MET B  1 284  ? 8.742   4.363   100.618 1.00 37.80 ? 282  MET B SD    1 
ATOM   10804 C CE    . MET B  1 284  ? 8.458   2.607   100.844 1.00 36.26 ? 282  MET B CE    1 
ATOM   10805 N N     . GLY B  1 285  ? 13.979  5.085   102.481 1.00 34.38 ? 283  GLY B N     1 
ATOM   10806 C CA    . GLY B  1 285  ? 15.131  4.619   103.230 1.00 33.53 ? 283  GLY B CA    1 
ATOM   10807 C C     . GLY B  1 285  ? 15.360  5.323   104.551 1.00 34.77 ? 283  GLY B C     1 
ATOM   10808 O O     . GLY B  1 285  ? 15.973  4.752   105.463 1.00 35.32 ? 283  GLY B O     1 
ATOM   10809 N N     . GLU B  1 286  ? 14.861  6.551   104.680 1.00 32.65 ? 284  GLU B N     1 
ATOM   10810 C CA    . GLU B  1 286  ? 15.134  7.384   105.844 1.00 34.13 ? 284  GLU B CA    1 
ATOM   10811 C C     . GLU B  1 286  ? 13.872  7.770   106.599 1.00 34.18 ? 284  GLU B C     1 
ATOM   10812 O O     . GLU B  1 286  ? 13.845  7.704   107.833 1.00 35.18 ? 284  GLU B O     1 
ATOM   10813 C CB    . GLU B  1 286  ? 15.892  8.650   105.409 1.00 33.43 ? 284  GLU B CB    1 
ATOM   10814 C CG    . GLU B  1 286  ? 17.201  8.368   104.684 1.00 37.20 ? 284  GLU B CG    1 
ATOM   10815 C CD    . GLU B  1 286  ? 17.747  9.590   103.948 1.00 40.08 ? 284  GLU B CD    1 
ATOM   10816 O OE1   . GLU B  1 286  ? 17.418  10.726  104.349 1.00 36.48 ? 284  GLU B OE1   1 
ATOM   10817 O OE2   . GLU B  1 286  ? 18.500  9.418   102.961 1.00 45.34 ? 284  GLU B OE2   1 
ATOM   10818 N N     . LEU B  1 287  ? 12.837  8.210   105.887 1.00 30.01 ? 285  LEU B N     1 
ATOM   10819 C CA    . LEU B  1 287  ? 11.585  8.595   106.527 1.00 31.93 ? 285  LEU B CA    1 
ATOM   10820 C C     . LEU B  1 287  ? 10.842  7.375   107.059 1.00 32.12 ? 285  LEU B C     1 
ATOM   10821 O O     . LEU B  1 287  ? 10.415  7.355   108.219 1.00 27.55 ? 285  LEU B O     1 
ATOM   10822 C CB    . LEU B  1 287  ? 10.720  9.364   105.526 1.00 26.23 ? 285  LEU B CB    1 
ATOM   10823 C CG    . LEU B  1 287  ? 9.711   10.388  106.064 1.00 28.11 ? 285  LEU B CG    1 
ATOM   10824 C CD1   . LEU B  1 287  ? 9.153   11.219  104.945 1.00 25.97 ? 285  LEU B CD1   1 
ATOM   10825 C CD2   . LEU B  1 287  ? 8.575   9.705   106.795 1.00 31.59 ? 285  LEU B CD2   1 
ATOM   10826 N N     . LEU B  1 288  ? 10.692  6.339   106.228 1.00 29.82 ? 286  LEU B N     1 
ATOM   10827 C CA    . LEU B  1 288  ? 9.900   5.176   106.630 1.00 32.15 ? 286  LEU B CA    1 
ATOM   10828 C C     . LEU B  1 288  ? 10.371  4.534   107.930 1.00 33.53 ? 286  LEU B C     1 
ATOM   10829 O O     . LEU B  1 288  ? 9.515   4.229   108.780 1.00 33.39 ? 286  LEU B O     1 
ATOM   10830 C CB    . LEU B  1 288  ? 9.861   4.152   105.489 1.00 31.96 ? 286  LEU B CB    1 
ATOM   10831 C CG    . LEU B  1 288  ? 9.155   2.837   105.830 1.00 36.99 ? 286  LEU B CG    1 
ATOM   10832 C CD1   . LEU B  1 288  ? 7.661   3.059   105.948 1.00 34.41 ? 286  LEU B CD1   1 
ATOM   10833 C CD2   . LEU B  1 288  ? 9.470   1.730   104.831 1.00 36.93 ? 286  LEU B CD2   1 
ATOM   10834 N N     . PRO B  1 289  ? 11.669  4.269   108.151 1.00 34.77 ? 287  PRO B N     1 
ATOM   10835 C CA    . PRO B  1 289  ? 12.066  3.679   109.445 1.00 30.26 ? 287  PRO B CA    1 
ATOM   10836 C C     . PRO B  1 289  ? 11.675  4.527   110.636 1.00 32.18 ? 287  PRO B C     1 
ATOM   10837 O O     . PRO B  1 289  ? 11.420  3.988   111.725 1.00 34.20 ? 287  PRO B O     1 
ATOM   10838 C CB    . PRO B  1 289  ? 13.586  3.545   109.313 1.00 36.82 ? 287  PRO B CB    1 
ATOM   10839 C CG    . PRO B  1 289  ? 13.797  3.375   107.836 1.00 36.52 ? 287  PRO B CG    1 
ATOM   10840 C CD    . PRO B  1 289  ? 12.793  4.273   107.193 1.00 36.20 ? 287  PRO B CD    1 
ATOM   10841 N N     . ARG B  1 290  ? 11.630  5.846   110.466 1.00 33.22 ? 288  ARG B N     1 
ATOM   10842 C CA    A ARG B  1 290  ? 11.173  6.704   111.552 0.57 31.03 ? 288  ARG B CA    1 
ATOM   10843 C CA    B ARG B  1 290  ? 11.172  6.712   111.545 0.43 31.05 ? 288  ARG B CA    1 
ATOM   10844 C C     . ARG B  1 290  ? 9.690   6.490   111.836 1.00 30.89 ? 288  ARG B C     1 
ATOM   10845 O O     . ARG B  1 290  ? 9.290   6.371   113.001 1.00 31.00 ? 288  ARG B O     1 
ATOM   10846 C CB    A ARG B  1 290  ? 11.465  8.164   111.219 0.57 31.91 ? 288  ARG B CB    1 
ATOM   10847 C CB    B ARG B  1 290  ? 11.463  8.169   111.190 0.43 31.91 ? 288  ARG B CB    1 
ATOM   10848 C CG    A ARG B  1 290  ? 12.918  8.581   111.473 0.57 32.37 ? 288  ARG B CG    1 
ATOM   10849 C CG    B ARG B  1 290  ? 12.960  8.498   111.183 0.43 32.39 ? 288  ARG B CG    1 
ATOM   10850 C CD    A ARG B  1 290  ? 13.165  9.989   110.938 0.57 33.76 ? 288  ARG B CD    1 
ATOM   10851 C CD    B ARG B  1 290  ? 13.221  9.951   110.792 0.43 33.71 ? 288  ARG B CD    1 
ATOM   10852 N NE    A ARG B  1 290  ? 14.444  10.540  111.369 0.57 35.24 ? 288  ARG B NE    1 
ATOM   10853 N NE    B ARG B  1 290  ? 14.442  10.462  111.406 0.43 35.20 ? 288  ARG B NE    1 
ATOM   10854 C CZ    A ARG B  1 290  ? 14.946  11.685  110.926 0.57 32.80 ? 288  ARG B CZ    1 
ATOM   10855 C CZ    B ARG B  1 290  ? 15.586  10.669  110.766 0.43 34.90 ? 288  ARG B CZ    1 
ATOM   10856 N NH1   A ARG B  1 290  ? 14.311  12.415  110.024 0.57 32.31 ? 288  ARG B NH1   1 
ATOM   10857 N NH1   B ARG B  1 290  ? 15.707  10.444  109.467 0.43 34.36 ? 288  ARG B NH1   1 
ATOM   10858 N NH2   A ARG B  1 290  ? 16.110  12.107  111.400 0.57 33.12 ? 288  ARG B NH2   1 
ATOM   10859 N NH2   B ARG B  1 290  ? 16.634  11.120  111.447 0.43 34.73 ? 288  ARG B NH2   1 
ATOM   10860 N N     . VAL B  1 291  ? 8.856   6.417   110.784 1.00 28.42 ? 289  VAL B N     1 
ATOM   10861 C CA    . VAL B  1 291  ? 7.435   6.147   110.997 1.00 31.96 ? 289  VAL B CA    1 
ATOM   10862 C C     . VAL B  1 291  ? 7.255   4.794   111.660 1.00 29.29 ? 289  VAL B C     1 
ATOM   10863 O O     . VAL B  1 291  ? 6.418   4.632   112.557 1.00 30.96 ? 289  VAL B O     1 
ATOM   10864 C CB    . VAL B  1 291  ? 6.644   6.207   109.673 1.00 32.85 ? 289  VAL B CB    1 
ATOM   10865 C CG1   . VAL B  1 291  ? 5.156   6.256   109.954 1.00 31.08 ? 289  VAL B CG1   1 
ATOM   10866 C CG2   . VAL B  1 291  ? 7.062   7.388   108.847 1.00 30.81 ? 289  VAL B CG2   1 
ATOM   10867 N N     . LYS B  1 292  ? 8.028   3.797   111.228 1.00 31.38 ? 290  LYS B N     1 
ATOM   10868 C CA    . LYS B  1 292  ? 7.853   2.459   111.781 1.00 33.36 ? 290  LYS B CA    1 
ATOM   10869 C C     . LYS B  1 292  ? 8.148   2.455   113.275 1.00 31.83 ? 290  LYS B C     1 
ATOM   10870 O O     . LYS B  1 292  ? 7.425   1.829   114.063 1.00 34.43 ? 290  LYS B O     1 
ATOM   10871 C CB    . LYS B  1 292  ? 8.755   1.463   111.052 1.00 34.18 ? 290  LYS B CB    1 
ATOM   10872 N N     . ALA B  1 293  ? 9.207   3.152   113.678 1.00 34.03 ? 291  ALA B N     1 
ATOM   10873 C CA    . ALA B  1 293  ? 9.567   3.201   115.091 1.00 32.82 ? 291  ALA B CA    1 
ATOM   10874 C C     . ALA B  1 293  ? 8.456   3.836   115.915 1.00 33.88 ? 291  ALA B C     1 
ATOM   10875 O O     . ALA B  1 293  ? 8.105   3.336   116.995 1.00 36.09 ? 291  ALA B O     1 
ATOM   10876 C CB    . ALA B  1 293  ? 10.882  3.960   115.272 1.00 32.56 ? 291  ALA B CB    1 
ATOM   10877 N N     . LEU B  1 294  ? 7.893   4.942   115.426 1.00 31.92 ? 292  LEU B N     1 
ATOM   10878 C CA    . LEU B  1 294  ? 6.791   5.586   116.129 1.00 30.68 ? 292  LEU B CA    1 
ATOM   10879 C C     . LEU B  1 294  ? 5.583   4.673   116.200 1.00 32.39 ? 292  LEU B C     1 
ATOM   10880 O O     . LEU B  1 294  ? 4.935   4.565   117.245 1.00 32.81 ? 292  LEU B O     1 
ATOM   10881 C CB    . LEU B  1 294  ? 6.411   6.895   115.436 1.00 29.36 ? 292  LEU B CB    1 
ATOM   10882 C CG    . LEU B  1 294  ? 7.462   8.002   115.497 1.00 30.45 ? 292  LEU B CG    1 
ATOM   10883 C CD1   . LEU B  1 294  ? 7.079   9.118   114.548 1.00 28.06 ? 292  LEU B CD1   1 
ATOM   10884 C CD2   . LEU B  1 294  ? 7.601   8.513   116.926 1.00 30.51 ? 292  LEU B CD2   1 
ATOM   10885 N N     . ALA B  1 295  ? 5.249   4.027   115.083 1.00 31.11 ? 293  ALA B N     1 
ATOM   10886 C CA    . ALA B  1 295  ? 4.122   3.105   115.070 1.00 33.11 ? 293  ALA B CA    1 
ATOM   10887 C C     . ALA B  1 295  ? 4.366   1.922   116.003 1.00 35.01 ? 293  ALA B C     1 
ATOM   10888 O O     . ALA B  1 295  ? 3.436   1.427   116.652 1.00 34.88 ? 293  ALA B O     1 
ATOM   10889 C CB    . ALA B  1 295  ? 3.869   2.632   113.640 1.00 31.66 ? 293  ALA B CB    1 
ATOM   10890 N N     . LEU B  1 296  ? 5.614   1.458   116.082 1.00 37.43 ? 294  LEU B N     1 
ATOM   10891 C CA    . LEU B  1 296  ? 5.962   0.402   117.030 1.00 37.35 ? 294  LEU B CA    1 
ATOM   10892 C C     . LEU B  1 296  ? 5.665   0.829   118.466 1.00 38.26 ? 294  LEU B C     1 
ATOM   10893 O O     . LEU B  1 296  ? 5.140   0.041   119.263 1.00 39.29 ? 294  LEU B O     1 
ATOM   10894 C CB    . LEU B  1 296  ? 7.437   0.038   116.866 1.00 39.51 ? 294  LEU B CB    1 
ATOM   10895 C CG    . LEU B  1 296  ? 7.907   -1.403  117.062 1.00 49.78 ? 294  LEU B CG    1 
ATOM   10896 C CD1   . LEU B  1 296  ? 6.797   -2.301  117.596 1.00 47.50 ? 294  LEU B CD1   1 
ATOM   10897 C CD2   . LEU B  1 296  ? 8.454   -1.940  115.744 1.00 49.67 ? 294  LEU B CD2   1 
ATOM   10898 N N     . LEU B  1 297  ? 5.993   2.074   118.815 1.00 33.91 ? 295  LEU B N     1 
ATOM   10899 C CA    . LEU B  1 297  ? 5.693   2.569   120.155 1.00 37.99 ? 295  LEU B CA    1 
ATOM   10900 C C     . LEU B  1 297  ? 4.187   2.718   120.367 1.00 35.91 ? 295  LEU B C     1 
ATOM   10901 O O     . LEU B  1 297  ? 3.671   2.360   121.431 1.00 35.43 ? 295  LEU B O     1 
ATOM   10902 C CB    . LEU B  1 297  ? 6.411   3.899   120.400 1.00 33.43 ? 295  LEU B CB    1 
ATOM   10903 N N     . ALA B  1 298  ? 3.466   3.244   119.370 1.00 36.44 ? 296  ALA B N     1 
ATOM   10904 C CA    . ALA B  1 298  ? 2.013   3.365   119.499 1.00 34.56 ? 296  ALA B CA    1 
ATOM   10905 C C     . ALA B  1 298  ? 1.362   1.998   119.683 1.00 40.17 ? 296  ALA B C     1 
ATOM   10906 O O     . ALA B  1 298  ? 0.387   1.855   120.435 1.00 39.09 ? 296  ALA B O     1 
ATOM   10907 C CB    . ALA B  1 298  ? 1.419   4.072   118.280 1.00 37.12 ? 296  ALA B CB    1 
ATOM   10908 N N     . LYS B  1 299  ? 1.894   0.980   119.007 1.00 36.20 ? 297  LYS B N     1 
ATOM   10909 C CA    . LYS B  1 299  ? 1.372   -0.369  119.177 1.00 36.71 ? 297  LYS B CA    1 
ATOM   10910 C C     . LYS B  1 299  ? 1.627   -0.880  120.591 1.00 40.63 ? 297  LYS B C     1 
ATOM   10911 O O     . LYS B  1 299  ? 0.752   -1.510  121.197 1.00 38.97 ? 297  LYS B O     1 
ATOM   10912 C CB    . LYS B  1 299  ? 1.992   -1.307  118.141 1.00 36.70 ? 297  LYS B CB    1 
ATOM   10913 N N     . ASN B  1 300  ? 2.810   -0.606  121.143 1.00 40.12 ? 298  ASN B N     1 
ATOM   10914 C CA    . ASN B  1 300  ? 3.114   -1.100  122.483 1.00 42.07 ? 298  ASN B CA    1 
ATOM   10915 C C     . ASN B  1 300  ? 2.182   -0.498  123.523 1.00 39.51 ? 298  ASN B C     1 
ATOM   10916 O O     . ASN B  1 300  ? 1.890   -1.140  124.536 1.00 40.48 ? 298  ASN B O     1 
ATOM   10917 C CB    . ASN B  1 300  ? 4.575   -0.821  122.825 1.00 47.55 ? 298  ASN B CB    1 
ATOM   10918 C CG    . ASN B  1 300  ? 5.536   -1.645  121.979 1.00 48.18 ? 298  ASN B CG    1 
ATOM   10919 O OD1   . ASN B  1 300  ? 5.168   -2.695  121.451 1.00 48.29 ? 298  ASN B OD1   1 
ATOM   10920 N ND2   . ASN B  1 300  ? 6.772   -1.174  121.850 1.00 47.81 ? 298  ASN B ND2   1 
ATOM   10921 N N     . TYR B  1 301  ? 1.672   0.706   123.278 1.00 37.98 ? 299  TYR B N     1 
ATOM   10922 C CA    . TYR B  1 301  ? 0.698   1.322   124.167 1.00 39.43 ? 299  TYR B CA    1 
ATOM   10923 C C     . TYR B  1 301  ? -0.747  1.084   123.739 1.00 41.60 ? 299  TYR B C     1 
ATOM   10924 O O     . TYR B  1 301  ? -1.663  1.470   124.473 1.00 41.98 ? 299  TYR B O     1 
ATOM   10925 C CB    . TYR B  1 301  ? 0.962   2.827   124.270 1.00 39.54 ? 299  TYR B CB    1 
ATOM   10926 C CG    . TYR B  1 301  ? 2.208   3.185   125.059 1.00 37.23 ? 299  TYR B CG    1 
ATOM   10927 C CD1   . TYR B  1 301  ? 2.274   2.970   126.427 1.00 39.26 ? 299  TYR B CD1   1 
ATOM   10928 C CD2   . TYR B  1 301  ? 3.303   3.775   124.433 1.00 39.69 ? 299  TYR B CD2   1 
ATOM   10929 C CE1   . TYR B  1 301  ? 3.404   3.305   127.149 1.00 38.13 ? 299  TYR B CE1   1 
ATOM   10930 C CE2   . TYR B  1 301  ? 4.444   4.122   125.149 1.00 37.14 ? 299  TYR B CE2   1 
ATOM   10931 C CZ    . TYR B  1 301  ? 4.483   3.879   126.503 1.00 38.80 ? 299  TYR B CZ    1 
ATOM   10932 O OH    . TYR B  1 301  ? 5.604   4.217   127.210 1.00 37.14 ? 299  TYR B OH    1 
ATOM   10933 N N     . ASP B  1 302  ? -0.963  0.450   122.589 1.00 41.16 ? 300  ASP B N     1 
ATOM   10934 C CA    . ASP B  1 302  ? -2.281  0.254   121.983 1.00 39.77 ? 300  ASP B CA    1 
ATOM   10935 C C     . ASP B  1 302  ? -3.044  1.571   121.840 1.00 38.02 ? 300  ASP B C     1 
ATOM   10936 O O     . ASP B  1 302  ? -4.178  1.729   122.297 1.00 41.34 ? 300  ASP B O     1 
ATOM   10937 C CB    . ASP B  1 302  ? -3.105  -0.778  122.761 1.00 40.81 ? 300  ASP B CB    1 
ATOM   10938 C CG    . ASP B  1 302  ? -4.300  -1.268  121.964 1.00 50.08 ? 300  ASP B CG    1 
ATOM   10939 O OD1   . ASP B  1 302  ? -4.119  -1.515  120.748 1.00 46.37 ? 300  ASP B OD1   1 
ATOM   10940 O OD2   . ASP B  1 302  ? -5.409  -1.384  122.533 1.00 49.64 ? 300  ASP B OD2   1 
ATOM   10941 N N     . ILE B  1 303  ? -2.409  2.522   121.157 1.00 36.78 ? 301  ILE B N     1 
ATOM   10942 C CA    . ILE B  1 303  ? -3.053  3.773   120.802 1.00 35.99 ? 301  ILE B CA    1 
ATOM   10943 C C     . ILE B  1 303  ? -3.050  3.900   119.284 1.00 35.11 ? 301  ILE B C     1 
ATOM   10944 O O     . ILE B  1 303  ? -2.290  3.235   118.573 1.00 34.94 ? 301  ILE B O     1 
ATOM   10945 C CB    . ILE B  1 303  ? -2.368  4.999   121.438 1.00 35.35 ? 301  ILE B CB    1 
ATOM   10946 C CG1   . ILE B  1 303  ? -0.970  5.176   120.844 1.00 35.08 ? 301  ILE B CG1   1 
ATOM   10947 C CG2   . ILE B  1 303  ? -2.287  4.850   122.957 1.00 36.27 ? 301  ILE B CG2   1 
ATOM   10948 C CD1   . ILE B  1 303  ? -0.317  6.512   121.191 1.00 34.80 ? 301  ILE B CD1   1 
ATOM   10949 N N     . GLY B  1 304  ? -3.899  4.794   118.799 1.00 34.58 ? 302  GLY B N     1 
ATOM   10950 C CA    . GLY B  1 304  ? -3.927  5.081   117.391 1.00 33.71 ? 302  GLY B CA    1 
ATOM   10951 C C     . GLY B  1 304  ? -2.792  5.999   116.985 1.00 35.87 ? 302  GLY B C     1 
ATOM   10952 O O     . GLY B  1 304  ? -2.355  6.870   117.738 1.00 32.31 ? 302  GLY B O     1 
ATOM   10953 N N     . LEU B  1 305  ? -2.287  5.769   115.778 1.00 32.01 ? 303  LEU B N     1 
ATOM   10954 C CA    . LEU B  1 305  ? -1.305  6.654   115.161 1.00 30.93 ? 303  LEU B CA    1 
ATOM   10955 C C     . LEU B  1 305  ? -1.826  6.972   113.778 1.00 30.28 ? 303  LEU B C     1 
ATOM   10956 O O     . LEU B  1 305  ? -1.948  6.065   112.952 1.00 31.99 ? 303  LEU B O     1 
ATOM   10957 C CB    . LEU B  1 305  ? 0.078   6.009   115.075 1.00 30.92 ? 303  LEU B CB    1 
ATOM   10958 C CG    . LEU B  1 305  ? 1.184   6.939   114.568 1.00 31.83 ? 303  LEU B CG    1 
ATOM   10959 C CD1   . LEU B  1 305  ? 2.525   6.582   115.189 1.00 31.31 ? 303  LEU B CD1   1 
ATOM   10960 C CD2   . LEU B  1 305  ? 1.308   6.917   113.062 1.00 33.76 ? 303  LEU B CD2   1 
ATOM   10961 N N     . ASN B  1 306  ? -2.128  8.241   113.536 1.00 29.66 ? 304  ASN B N     1 
ATOM   10962 C CA    . ASN B  1 306  ? -2.764  8.691   112.304 1.00 31.93 ? 304  ASN B CA    1 
ATOM   10963 C C     . ASN B  1 306  ? -1.793  9.504   111.457 1.00 29.88 ? 304  ASN B C     1 
ATOM   10964 O O     . ASN B  1 306  ? -1.095  10.385  111.968 1.00 30.18 ? 304  ASN B O     1 
ATOM   10965 C CB    . ASN B  1 306  ? -3.998  9.544   112.603 1.00 31.54 ? 304  ASN B CB    1 
ATOM   10966 C CG    . ASN B  1 306  ? -4.583  10.152  111.355 1.00 31.41 ? 304  ASN B CG    1 
ATOM   10967 O OD1   . ASN B  1 306  ? -4.418  11.355  111.076 1.00 36.54 ? 304  ASN B OD1   1 
ATOM   10968 N ND2   . ASN B  1 306  ? -5.221  9.318   110.561 1.00 30.05 ? 304  ASN B ND2   1 
ATOM   10969 N N     . ILE B  1 307  ? -1.777  9.219   110.156 1.00 27.94 ? 305  ILE B N     1 
ATOM   10970 C CA    . ILE B  1 307  ? -0.985  9.966   109.187 1.00 31.11 ? 305  ILE B CA    1 
ATOM   10971 C C     . ILE B  1 307  ? -1.897  10.997  108.527 1.00 30.51 ? 305  ILE B C     1 
ATOM   10972 O O     . ILE B  1 307  ? -2.803  10.640  107.761 1.00 28.64 ? 305  ILE B O     1 
ATOM   10973 C CB    . ILE B  1 307  ? -0.345  9.040   108.143 1.00 26.60 ? 305  ILE B CB    1 
ATOM   10974 C CG1   . ILE B  1 307  ? 0.658   8.107   108.819 1.00 33.76 ? 305  ILE B CG1   1 
ATOM   10975 C CG2   . ILE B  1 307  ? 0.345   9.857   107.055 1.00 26.59 ? 305  ILE B CG2   1 
ATOM   10976 C CD1   . ILE B  1 307  ? 0.850   6.795   108.094 1.00 34.75 ? 305  ILE B CD1   1 
ATOM   10977 N N     . ASP B  1 308  ? -1.660  12.273  108.841 1.00 26.43 ? 306  ASP B N     1 
ATOM   10978 C CA    . ASP B  1 308  ? -2.374  13.371  108.208 1.00 29.08 ? 306  ASP B CA    1 
ATOM   10979 C C     . ASP B  1 308  ? -2.077  13.387  106.715 1.00 28.19 ? 306  ASP B C     1 
ATOM   10980 O O     . ASP B  1 308  ? -1.011  12.963  106.268 1.00 27.72 ? 306  ASP B O     1 
ATOM   10981 C CB    . ASP B  1 308  ? -1.959  14.720  108.815 1.00 28.46 ? 306  ASP B CB    1 
ATOM   10982 C CG    . ASP B  1 308  ? -2.459  14.926  110.240 1.00 36.12 ? 306  ASP B CG    1 
ATOM   10983 O OD1   . ASP B  1 308  ? -3.328  14.154  110.714 1.00 32.56 ? 306  ASP B OD1   1 
ATOM   10984 O OD2   . ASP B  1 308  ? -1.972  15.881  110.886 1.00 32.29 ? 306  ASP B OD2   1 
ATOM   10985 N N     . ALA B  1 309  ? -3.032  13.887  105.942 1.00 27.00 ? 307  ALA B N     1 
ATOM   10986 C CA    . ALA B  1 309  ? -2.870  14.035  104.504 1.00 27.70 ? 307  ALA B CA    1 
ATOM   10987 C C     . ALA B  1 309  ? -2.507  15.476  104.177 1.00 27.21 ? 307  ALA B C     1 
ATOM   10988 O O     . ALA B  1 309  ? -3.058  16.410  104.766 1.00 26.05 ? 307  ALA B O     1 
ATOM   10989 C CB    . ALA B  1 309  ? -4.151  13.639  103.771 1.00 26.55 ? 307  ALA B CB    1 
ATOM   10990 N N     . GLU B  1 310  ? -1.569  15.649  103.238 1.00 23.52 ? 308  GLU B N     1 
ATOM   10991 C CA    . GLU B  1 310  ? -1.015  16.961  102.934 1.00 27.86 ? 308  GLU B CA    1 
ATOM   10992 C C     . GLU B  1 310  ? -1.301  17.358  101.482 1.00 24.33 ? 308  GLU B C     1 
ATOM   10993 O O     . GLU B  1 310  ? -2.446  17.250  101.038 1.00 24.24 ? 308  GLU B O     1 
ATOM   10994 C CB    . GLU B  1 310  ? 0.484   16.970  103.259 1.00 23.34 ? 308  GLU B CB    1 
ATOM   10995 C CG    . GLU B  1 310  ? 0.730   16.540  104.711 1.00 25.34 ? 308  GLU B CG    1 
ATOM   10996 C CD    . GLU B  1 310  ? 2.172   16.685  105.176 1.00 25.01 ? 308  GLU B CD    1 
ATOM   10997 O OE1   . GLU B  1 310  ? 2.677   17.823  105.245 1.00 28.56 ? 308  GLU B OE1   1 
ATOM   10998 O OE2   . GLU B  1 310  ? 2.789   15.655  105.499 1.00 24.65 ? 308  GLU B OE2   1 
ATOM   10999 N N     . GLU B  1 311  ? -0.298  17.862  100.759 1.00 22.68 ? 309  GLU B N     1 
ATOM   11000 C CA    . GLU B  1 311  ? -0.513  18.330  99.393  1.00 25.09 ? 309  GLU B CA    1 
ATOM   11001 C C     . GLU B  1 311  ? -0.869  17.172  98.465  1.00 23.71 ? 309  GLU B C     1 
ATOM   11002 O O     . GLU B  1 311  ? -0.543  16.015  98.728  1.00 26.39 ? 309  GLU B O     1 
ATOM   11003 C CB    . GLU B  1 311  ? 0.733   19.041  98.864  1.00 24.80 ? 309  GLU B CB    1 
ATOM   11004 C CG    . GLU B  1 311  ? 1.079   20.361  99.603  1.00 26.37 ? 309  GLU B CG    1 
ATOM   11005 C CD    . GLU B  1 311  ? 1.892   20.158  100.890 1.00 28.78 ? 309  GLU B CD    1 
ATOM   11006 O OE1   . GLU B  1 311  ? 2.141   19.007  101.313 1.00 26.54 ? 309  GLU B OE1   1 
ATOM   11007 O OE2   . GLU B  1 311  ? 2.283   21.172  101.492 1.00 32.85 ? 309  GLU B OE2   1 
ATOM   11008 N N     . ALA B  1 312  ? -1.509  17.507  97.337  1.00 20.37 ? 310  ALA B N     1 
ATOM   11009 C CA    . ALA B  1 312  ? -1.936  16.465  96.408  1.00 24.35 ? 310  ALA B CA    1 
ATOM   11010 C C     . ALA B  1 312  ? -0.751  15.675  95.867  1.00 25.46 ? 310  ALA B C     1 
ATOM   11011 O O     . ALA B  1 312  ? -0.871  14.468  95.625  1.00 21.70 ? 310  ALA B O     1 
ATOM   11012 C CB    . ALA B  1 312  ? -2.732  17.073  95.248  1.00 24.11 ? 310  ALA B CB    1 
ATOM   11013 N N     . ASP B  1 313  ? 0.413   16.312  95.705  1.00 22.26 ? 311  ASP B N     1 
ATOM   11014 C CA    . ASP B  1 313  ? 1.513   15.561  95.114  1.00 25.25 ? 311  ASP B CA    1 
ATOM   11015 C C     . ASP B  1 313  ? 2.246   14.682  96.124  1.00 24.80 ? 311  ASP B C     1 
ATOM   11016 O O     . ASP B  1 313  ? 3.254   14.069  95.768  1.00 27.04 ? 311  ASP B O     1 
ATOM   11017 C CB    . ASP B  1 313  ? 2.482   16.503  94.378  1.00 24.49 ? 311  ASP B CB    1 
ATOM   11018 C CG    . ASP B  1 313  ? 3.167   17.502  95.286  1.00 28.26 ? 311  ASP B CG    1 
ATOM   11019 O OD1   . ASP B  1 313  ? 2.978   17.464  96.522  1.00 27.03 ? 311  ASP B OD1   1 
ATOM   11020 O OD2   . ASP B  1 313  ? 3.923   18.342  94.737  1.00 26.79 ? 311  ASP B OD2   1 
ATOM   11021 N N     . ARG B  1 314  ? 1.749   14.574  97.355  1.00 23.98 ? 312  ARG B N     1 
ATOM   11022 C CA    . ARG B  1 314  ? 2.288   13.630  98.327  1.00 24.15 ? 312  ARG B CA    1 
ATOM   11023 C C     . ARG B  1 314  ? 1.352   12.462  98.612  1.00 24.19 ? 312  ARG B C     1 
ATOM   11024 O O     . ARG B  1 314  ? 1.735   11.536  99.340  1.00 25.24 ? 312  ARG B O     1 
ATOM   11025 C CB    . ARG B  1 314  ? 2.630   14.370  99.622  1.00 23.80 ? 312  ARG B CB    1 
ATOM   11026 C CG    . ARG B  1 314  ? 3.891   15.236  99.472  1.00 24.48 ? 312  ARG B CG    1 
ATOM   11027 C CD    . ARG B  1 314  ? 3.934   16.409  100.440 1.00 25.66 ? 312  ARG B CD    1 
ATOM   11028 N NE    . ARG B  1 314  ? 5.316   16.809  100.701 1.00 22.35 ? 312  ARG B NE    1 
ATOM   11029 C CZ    . ARG B  1 314  ? 5.688   17.804  101.492 1.00 29.01 ? 312  ARG B CZ    1 
ATOM   11030 N NH1   . ARG B  1 314  ? 4.799   18.600  102.075 1.00 23.95 ? 312  ARG B NH1   1 
ATOM   11031 N NH2   . ARG B  1 314  ? 6.990   18.007  101.703 1.00 24.38 ? 312  ARG B NH2   1 
ATOM   11032 N N     . LEU B  1 315  ? 0.145   12.466  98.044  1.00 24.34 ? 313  LEU B N     1 
ATOM   11033 C CA    . LEU B  1 315  ? -0.841  11.439  98.373  1.00 28.47 ? 313  LEU B CA    1 
ATOM   11034 C C     . LEU B  1 315  ? -0.330  10.045  98.015  1.00 29.33 ? 313  LEU B C     1 
ATOM   11035 O O     . LEU B  1 315  ? -0.261  9.147   98.872  1.00 27.45 ? 313  LEU B O     1 
ATOM   11036 C CB    . LEU B  1 315  ? -2.162  11.738  97.653  1.00 24.93 ? 313  LEU B CB    1 
ATOM   11037 C CG    . LEU B  1 315  ? -3.457  11.109  98.191  1.00 29.06 ? 313  LEU B CG    1 
ATOM   11038 C CD1   . LEU B  1 315  ? -4.676  11.724  97.481  1.00 26.77 ? 313  LEU B CD1   1 
ATOM   11039 C CD2   . LEU B  1 315  ? -3.495  9.588   98.075  1.00 28.04 ? 313  LEU B CD2   1 
ATOM   11040 N N     . GLU B  1 316  ? 0.026   9.838   96.748  1.00 25.34 ? 314  GLU B N     1 
ATOM   11041 C CA    . GLU B  1 316  ? 0.404   8.489   96.332  1.00 29.62 ? 314  GLU B CA    1 
ATOM   11042 C C     . GLU B  1 316  ? 1.712   8.047   96.980  1.00 31.51 ? 314  GLU B C     1 
ATOM   11043 O O     . GLU B  1 316  ? 1.859   6.868   97.329  1.00 32.51 ? 314  GLU B O     1 
ATOM   11044 C CB    . GLU B  1 316  ? 0.456   8.413   94.805  1.00 30.25 ? 314  GLU B CB    1 
ATOM   11045 C CG    . GLU B  1 316  ? -0.950  8.578   94.235  1.00 29.10 ? 314  GLU B CG    1 
ATOM   11046 C CD    . GLU B  1 316  ? -1.046  8.386   92.734  1.00 32.35 ? 314  GLU B CD    1 
ATOM   11047 O OE1   . GLU B  1 316  ? -0.457  7.415   92.199  1.00 35.45 ? 314  GLU B OE1   1 
ATOM   11048 O OE2   . GLU B  1 316  ? -1.733  9.211   92.098  1.00 32.18 ? 314  GLU B OE2   1 
ATOM   11049 N N     . LEU B  1 317  ? 2.648   8.975   97.185  1.00 31.28 ? 315  LEU B N     1 
ATOM   11050 C CA    . LEU B  1 317  ? 3.875   8.631   97.894  1.00 31.59 ? 315  LEU B CA    1 
ATOM   11051 C C     . LEU B  1 317  ? 3.565   8.092   99.283  1.00 29.86 ? 315  LEU B C     1 
ATOM   11052 O O     . LEU B  1 317  ? 4.141   7.085   99.704  1.00 28.61 ? 315  LEU B O     1 
ATOM   11053 C CB    . LEU B  1 317  ? 4.793   9.847   97.980  1.00 28.60 ? 315  LEU B CB    1 
ATOM   11054 C CG    . LEU B  1 317  ? 6.092   9.656   98.771  1.00 31.11 ? 315  LEU B CG    1 
ATOM   11055 C CD1   . LEU B  1 317  ? 6.921   8.505   98.220  1.00 32.44 ? 315  LEU B CD1   1 
ATOM   11056 C CD2   . LEU B  1 317  ? 6.893   10.942  98.762  1.00 28.67 ? 315  LEU B CD2   1 
ATOM   11057 N N     . SER B  1 318  ? 2.632   8.728   100.000 1.00 27.11 ? 316  SER B N     1 
ATOM   11058 C CA    . SER B  1 318  ? 2.300   8.267   101.346 1.00 28.82 ? 316  SER B CA    1 
ATOM   11059 C C     . SER B  1 318  ? 1.697   6.862   101.331 1.00 30.91 ? 316  SER B C     1 
ATOM   11060 O O     . SER B  1 318  ? 1.831   6.122   102.313 1.00 32.94 ? 316  SER B O     1 
ATOM   11061 C CB    . SER B  1 318  ? 1.344   9.249   102.036 1.00 27.37 ? 316  SER B CB    1 
ATOM   11062 O OG    . SER B  1 318  ? 0.053   9.242   101.455 1.00 28.91 ? 316  SER B OG    1 
ATOM   11063 N N     . LEU B  1 319  ? 1.047   6.469   100.232 1.00 27.88 ? 317  LEU B N     1 
ATOM   11064 C CA    . LEU B  1 319  ? 0.478   5.123   100.170 1.00 27.77 ? 317  LEU B CA    1 
ATOM   11065 C C     . LEU B  1 319  ? 1.558   4.050   100.169 1.00 29.35 ? 317  LEU B C     1 
ATOM   11066 O O     . LEU B  1 319  ? 1.330   2.947   100.674 1.00 34.32 ? 317  LEU B O     1 
ATOM   11067 C CB    . LEU B  1 319  ? -0.400  4.960   98.926  1.00 30.41 ? 317  LEU B CB    1 
ATOM   11068 C CG    . LEU B  1 319  ? -1.661  5.822   98.840  1.00 31.86 ? 317  LEU B CG    1 
ATOM   11069 C CD1   . LEU B  1 319  ? -2.354  5.571   97.511  1.00 32.73 ? 317  LEU B CD1   1 
ATOM   11070 C CD2   . LEU B  1 319  ? -2.610  5.523   99.992  1.00 30.02 ? 317  LEU B CD2   1 
ATOM   11071 N N     . ASP B  1 320  ? 2.731   4.345   99.604  1.00 32.97 ? 318  ASP B N     1 
ATOM   11072 C CA    . ASP B  1 320  ? 3.817   3.375   99.655  1.00 35.16 ? 318  ASP B CA    1 
ATOM   11073 C C     . ASP B  1 320  ? 4.296   3.156   101.082 1.00 34.74 ? 318  ASP B C     1 
ATOM   11074 O O     . ASP B  1 320  ? 4.733   2.055   101.425 1.00 35.98 ? 318  ASP B O     1 
ATOM   11075 C CB    . ASP B  1 320  ? 4.962   3.827   98.754  1.00 32.92 ? 318  ASP B CB    1 
ATOM   11076 C CG    . ASP B  1 320  ? 4.648   3.629   97.277  1.00 33.24 ? 318  ASP B CG    1 
ATOM   11077 O OD1   . ASP B  1 320  ? 4.321   2.487   96.899  1.00 38.72 ? 318  ASP B OD1   1 
ATOM   11078 O OD2   . ASP B  1 320  ? 4.708   4.615   96.506  1.00 34.41 ? 318  ASP B OD2   1 
ATOM   11079 N N     . LEU B  1 321  ? 4.223   4.184   101.927 1.00 31.82 ? 319  LEU B N     1 
ATOM   11080 C CA    . LEU B  1 321  ? 4.564   3.990   103.330 1.00 32.90 ? 319  LEU B CA    1 
ATOM   11081 C C     . LEU B  1 321  ? 3.478   3.203   104.041 1.00 32.67 ? 319  LEU B C     1 
ATOM   11082 O O     . LEU B  1 321  ? 3.773   2.305   104.835 1.00 34.56 ? 319  LEU B O     1 
ATOM   11083 C CB    . LEU B  1 321  ? 4.791   5.338   104.014 1.00 28.39 ? 319  LEU B CB    1 
ATOM   11084 C CG    . LEU B  1 321  ? 6.158   5.954   103.740 1.00 33.30 ? 319  LEU B CG    1 
ATOM   11085 C CD1   . LEU B  1 321  ? 6.082   6.905   102.551 1.00 33.07 ? 319  LEU B CD1   1 
ATOM   11086 C CD2   . LEU B  1 321  ? 6.675   6.661   104.979 1.00 34.21 ? 319  LEU B CD2   1 
ATOM   11087 N N     . LEU B  1 322  ? 2.215   3.524   103.759 1.00 31.53 ? 320  LEU B N     1 
ATOM   11088 C CA    . LEU B  1 322  ? 1.112   2.784   104.354 1.00 32.76 ? 320  LEU B CA    1 
ATOM   11089 C C     . LEU B  1 322  ? 1.212   1.306   104.019 1.00 33.64 ? 320  LEU B C     1 
ATOM   11090 O O     . LEU B  1 322  ? 0.969   0.454   104.876 1.00 31.71 ? 320  LEU B O     1 
ATOM   11091 C CB    . LEU B  1 322  ? -0.222  3.345   103.866 1.00 32.95 ? 320  LEU B CB    1 
ATOM   11092 C CG    . LEU B  1 322  ? -1.446  2.682   104.490 1.00 36.07 ? 320  LEU B CG    1 
ATOM   11093 C CD1   . LEU B  1 322  ? -1.407  2.868   105.995 1.00 36.39 ? 320  LEU B CD1   1 
ATOM   11094 C CD2   . LEU B  1 322  ? -2.742  3.229   103.912 1.00 33.37 ? 320  LEU B CD2   1 
ATOM   11095 N N     . GLU B  1 323  ? 1.598   0.990   102.780 1.00 34.08 ? 321  GLU B N     1 
ATOM   11096 C CA    . GLU B  1 323  ? 1.722   -0.403  102.358 1.00 36.12 ? 321  GLU B CA    1 
ATOM   11097 C C     . GLU B  1 323  ? 2.722   -1.153  103.229 1.00 38.15 ? 321  GLU B C     1 
ATOM   11098 O O     . GLU B  1 323  ? 2.433   -2.247  103.724 1.00 40.29 ? 321  GLU B O     1 
ATOM   11099 C CB    . GLU B  1 323  ? 2.131   -0.457  100.881 1.00 38.24 ? 321  GLU B CB    1 
ATOM   11100 C CG    . GLU B  1 323  ? 2.354   -1.859  100.328 1.00 42.49 ? 321  GLU B CG    1 
ATOM   11101 C CD    . GLU B  1 323  ? 1.098   -2.502  99.742  1.00 44.33 ? 321  GLU B CD    1 
ATOM   11102 O OE1   . GLU B  1 323  ? 0.199   -1.788  99.248  1.00 44.26 ? 321  GLU B OE1   1 
ATOM   11103 O OE2   . GLU B  1 323  ? 1.010   -3.743  99.763  1.00 49.15 ? 321  GLU B OE2   1 
ATOM   11104 N N     . VAL B  1 324  ? 3.903   -0.567  103.449 1.00 36.99 ? 322  VAL B N     1 
ATOM   11105 C CA    . VAL B  1 324  ? 4.932   -1.272  104.210 1.00 38.29 ? 322  VAL B CA    1 
ATOM   11106 C C     . VAL B  1 324  ? 4.520   -1.426  105.669 1.00 37.54 ? 322  VAL B C     1 
ATOM   11107 O O     . VAL B  1 324  ? 4.708   -2.493  106.268 1.00 40.22 ? 322  VAL B O     1 
ATOM   11108 C CB    . VAL B  1 324  ? 6.285   -0.552  104.079 1.00 38.99 ? 322  VAL B CB    1 
ATOM   11109 C CG1   . VAL B  1 324  ? 7.306   -1.192  105.009 1.00 34.48 ? 322  VAL B CG1   1 
ATOM   11110 C CG2   . VAL B  1 324  ? 6.758   -0.593  102.627 1.00 39.81 ? 322  VAL B CG2   1 
ATOM   11111 N N     . LEU B  1 325  ? 3.962   -0.369  106.268 1.00 35.76 ? 323  LEU B N     1 
ATOM   11112 C CA    . LEU B  1 325  ? 3.567   -0.442  107.673 1.00 35.60 ? 323  LEU B CA    1 
ATOM   11113 C C     . LEU B  1 325  ? 2.495   -1.500  107.892 1.00 36.05 ? 323  LEU B C     1 
ATOM   11114 O O     . LEU B  1 325  ? 2.515   -2.209  108.902 1.00 38.15 ? 323  LEU B O     1 
ATOM   11115 C CB    . LEU B  1 325  ? 3.080   0.925   108.155 1.00 34.82 ? 323  LEU B CB    1 
ATOM   11116 C CG    . LEU B  1 325  ? 4.158   2.014   108.103 1.00 34.39 ? 323  LEU B CG    1 
ATOM   11117 C CD1   . LEU B  1 325  ? 3.573   3.393   108.309 1.00 32.29 ? 323  LEU B CD1   1 
ATOM   11118 C CD2   . LEU B  1 325  ? 5.238   1.736   109.150 1.00 33.78 ? 323  LEU B CD2   1 
ATOM   11119 N N     . CYS B  1 326  ? 1.558   -1.640  106.945 1.00 34.04 ? 324  CYS B N     1 
ATOM   11120 C CA    . CYS B  1 326  ? 0.468   -2.586  107.154 1.00 36.34 ? 324  CYS B CA    1 
ATOM   11121 C C     . CYS B  1 326  ? 0.920   -4.031  106.972 1.00 40.39 ? 324  CYS B C     1 
ATOM   11122 O O     . CYS B  1 326  ? 0.320   -4.943  107.561 1.00 36.39 ? 324  CYS B O     1 
ATOM   11123 C CB    . CYS B  1 326  ? -0.703  -2.254  106.222 1.00 36.06 ? 324  CYS B CB    1 
ATOM   11124 S SG    . CYS B  1 326  ? -1.612  -0.778  106.756 1.00 41.89 ? 324  CYS B SG    1 
ATOM   11125 N N     . LEU B  1 327  ? 1.972   -4.264  106.182 1.00 35.81 ? 325  LEU B N     1 
ATOM   11126 C CA    . LEU B  1 327  ? 2.520   -5.608  106.008 1.00 38.68 ? 325  LEU B CA    1 
ATOM   11127 C C     . LEU B  1 327  ? 3.668   -5.913  106.967 1.00 39.22 ? 325  LEU B C     1 
ATOM   11128 O O     . LEU B  1 327  ? 4.153   -7.053  107.002 1.00 39.47 ? 325  LEU B O     1 
ATOM   11129 C CB    . LEU B  1 327  ? 2.980   -5.801  104.558 1.00 38.63 ? 325  LEU B CB    1 
ATOM   11130 C CG    . LEU B  1 327  ? 1.863   -5.577  103.528 1.00 42.76 ? 325  LEU B CG    1 
ATOM   11131 C CD1   . LEU B  1 327  ? 2.396   -5.605  102.100 1.00 44.65 ? 325  LEU B CD1   1 
ATOM   11132 C CD2   . LEU B  1 327  ? 0.764   -6.607  103.705 1.00 45.43 ? 325  LEU B CD2   1 
ATOM   11133 N N     . ASP B  1 328  ? 4.098   -4.936  107.759 1.00 38.03 ? 326  ASP B N     1 
ATOM   11134 C CA    . ASP B  1 328  ? 5.213   -5.133  108.682 1.00 39.34 ? 326  ASP B CA    1 
ATOM   11135 C C     . ASP B  1 328  ? 4.756   -5.975  109.873 1.00 39.80 ? 326  ASP B C     1 
ATOM   11136 O O     . ASP B  1 328  ? 4.003   -5.497  110.728 1.00 40.79 ? 326  ASP B O     1 
ATOM   11137 C CB    . ASP B  1 328  ? 5.746   -3.771  109.127 1.00 36.11 ? 326  ASP B CB    1 
ATOM   11138 C CG    . ASP B  1 328  ? 7.044   -3.873  109.927 1.00 44.33 ? 326  ASP B CG    1 
ATOM   11139 O OD1   . ASP B  1 328  ? 7.350   -4.963  110.454 1.00 41.46 ? 326  ASP B OD1   1 
ATOM   11140 O OD2   . ASP B  1 328  ? 7.756   -2.849  110.040 1.00 47.62 ? 326  ASP B OD2   1 
ATOM   11141 N N     . GLY B  1 329  ? 5.238   -7.217  109.953 1.00 39.03 ? 327  GLY B N     1 
ATOM   11142 C CA    . GLY B  1 329  ? 4.865   -8.126  111.032 1.00 39.12 ? 327  GLY B CA    1 
ATOM   11143 C C     . GLY B  1 329  ? 5.247   -7.660  112.431 1.00 39.88 ? 327  GLY B C     1 
ATOM   11144 O O     . GLY B  1 329  ? 4.723   -8.207  113.410 1.00 42.99 ? 327  GLY B O     1 
ATOM   11145 N N     . ASP B  1 330  ? 6.144   -6.680  112.555 1.00 38.55 ? 328  ASP B N     1 
ATOM   11146 C CA    . ASP B  1 330  ? 6.424   -6.117  113.871 1.00 41.19 ? 328  ASP B CA    1 
ATOM   11147 C C     . ASP B  1 330  ? 5.197   -5.429  114.455 1.00 42.91 ? 328  ASP B C     1 
ATOM   11148 O O     . ASP B  1 330  ? 5.062   -5.346  115.682 1.00 43.13 ? 328  ASP B O     1 
ATOM   11149 C CB    . ASP B  1 330  ? 7.609   -5.146  113.796 1.00 42.70 ? 328  ASP B CB    1 
ATOM   11150 C CG    . ASP B  1 330  ? 8.935   -5.863  113.563 1.00 49.06 ? 328  ASP B CG    1 
ATOM   11151 O OD1   . ASP B  1 330  ? 8.955   -7.108  113.668 1.00 51.09 ? 328  ASP B OD1   1 
ATOM   11152 O OD2   . ASP B  1 330  ? 9.955   -5.199  113.270 1.00 45.17 ? 328  ASP B OD2   1 
ATOM   11153 N N     . LEU B  1 331  ? 4.278   -4.962  113.601 1.00 40.75 ? 329  LEU B N     1 
ATOM   11154 C CA    . LEU B  1 331  ? 3.045   -4.324  114.046 1.00 39.83 ? 329  LEU B CA    1 
ATOM   11155 C C     . LEU B  1 331  ? 1.859   -5.283  114.067 1.00 40.75 ? 329  LEU B C     1 
ATOM   11156 O O     . LEU B  1 331  ? 0.708   -4.831  114.095 1.00 39.00 ? 329  LEU B O     1 
ATOM   11157 C CB    . LEU B  1 331  ? 2.729   -3.124  113.159 1.00 38.26 ? 329  LEU B CB    1 
ATOM   11158 C CG    . LEU B  1 331  ? 3.900   -2.165  112.978 1.00 38.20 ? 329  LEU B CG    1 
ATOM   11159 C CD1   . LEU B  1 331  ? 3.592   -1.177  111.879 1.00 34.77 ? 329  LEU B CD1   1 
ATOM   11160 C CD2   . LEU B  1 331  ? 4.195   -1.453  114.288 1.00 40.57 ? 329  LEU B CD2   1 
ATOM   11161 N N     . SER B  1 332  ? 2.122   -6.588  114.059 1.00 43.19 ? 330  SER B N     1 
ATOM   11162 C CA    . SER B  1 332  ? 1.091   -7.616  113.970 1.00 40.21 ? 330  SER B CA    1 
ATOM   11163 C C     . SER B  1 332  ? -0.027  -7.411  114.987 1.00 44.90 ? 330  SER B C     1 
ATOM   11164 O O     . SER B  1 332  ? 0.219   -7.338  116.193 1.00 47.40 ? 330  SER B O     1 
ATOM   11165 C CB    . SER B  1 332  ? 1.737   -8.989  114.178 1.00 42.20 ? 330  SER B CB    1 
ATOM   11166 O OG    . SER B  1 332  ? 0.765   -10.020 114.181 1.00 46.20 ? 330  SER B OG    1 
ATOM   11167 N N     . GLY B  1 333  ? -1.265  -7.336  114.494 1.00 41.96 ? 331  GLY B N     1 
ATOM   11168 C CA    . GLY B  1 333  ? -2.429  -7.261  115.351 1.00 45.94 ? 331  GLY B CA    1 
ATOM   11169 C C     . GLY B  1 333  ? -2.816  -5.873  115.815 1.00 47.58 ? 331  GLY B C     1 
ATOM   11170 O O     . GLY B  1 333  ? -3.912  -5.707  116.366 1.00 46.00 ? 331  GLY B O     1 
ATOM   11171 N N     . TRP B  1 334  ? -1.959  -4.877  115.605 1.00 43.91 ? 332  TRP B N     1 
ATOM   11172 C CA    . TRP B  1 334  ? -2.243  -3.493  115.969 1.00 43.13 ? 332  TRP B CA    1 
ATOM   11173 C C     . TRP B  1 334  ? -3.175  -2.871  114.937 1.00 42.90 ? 332  TRP B C     1 
ATOM   11174 O O     . TRP B  1 334  ? -2.799  -2.690  113.775 1.00 46.26 ? 332  TRP B O     1 
ATOM   11175 C CB    . TRP B  1 334  ? -0.934  -2.718  116.072 1.00 39.46 ? 332  TRP B CB    1 
ATOM   11176 C CG    . TRP B  1 334  ? -1.087  -1.256  116.307 1.00 40.78 ? 332  TRP B CG    1 
ATOM   11177 C CD1   . TRP B  1 334  ? -1.731  -0.653  117.346 1.00 40.55 ? 332  TRP B CD1   1 
ATOM   11178 C CD2   . TRP B  1 334  ? -0.562  -0.203  115.494 1.00 35.93 ? 332  TRP B CD2   1 
ATOM   11179 N NE1   . TRP B  1 334  ? -1.652  0.714   117.224 1.00 39.80 ? 332  TRP B NE1   1 
ATOM   11180 C CE2   . TRP B  1 334  ? -0.938  1.017   116.094 1.00 34.86 ? 332  TRP B CE2   1 
ATOM   11181 C CE3   . TRP B  1 334  ? 0.182   -0.172  114.314 1.00 40.62 ? 332  TRP B CE3   1 
ATOM   11182 C CZ2   . TRP B  1 334  ? -0.582  2.250   115.565 1.00 33.69 ? 332  TRP B CZ2   1 
ATOM   11183 C CZ3   . TRP B  1 334  ? 0.528   1.057   113.782 1.00 36.28 ? 332  TRP B CZ3   1 
ATOM   11184 C CH2   . TRP B  1 334  ? 0.143   2.249   114.407 1.00 35.69 ? 332  TRP B CH2   1 
ATOM   11185 N N     . ASN B  1 335  ? -4.391  -2.531  115.358 1.00 39.89 ? 333  ASN B N     1 
ATOM   11186 C CA    . ASN B  1 335  ? -5.354  -1.868  114.495 1.00 40.64 ? 333  ASN B CA    1 
ATOM   11187 C C     . ASN B  1 335  ? -5.306  -0.356  114.625 1.00 39.06 ? 333  ASN B C     1 
ATOM   11188 O O     . ASN B  1 335  ? -6.269  0.322   114.257 1.00 39.33 ? 333  ASN B O     1 
ATOM   11189 C CB    . ASN B  1 335  ? -6.765  -2.378  114.797 1.00 43.01 ? 333  ASN B CB    1 
ATOM   11190 C CG    . ASN B  1 335  ? -6.903  -3.853  114.542 1.00 43.89 ? 333  ASN B CG    1 
ATOM   11191 O OD1   . ASN B  1 335  ? -6.416  -4.353  113.528 1.00 43.97 ? 333  ASN B OD1   1 
ATOM   11192 N ND2   . ASN B  1 335  ? -7.537  -4.575  115.477 1.00 43.60 ? 333  ASN B ND2   1 
ATOM   11193 N N     . GLY B  1 336  ? -4.213  0.187   115.143 1.00 40.33 ? 334  GLY B N     1 
ATOM   11194 C CA    . GLY B  1 336  ? -4.183  1.604   115.397 1.00 35.12 ? 334  GLY B CA    1 
ATOM   11195 C C     . GLY B  1 336  ? -3.630  2.452   114.289 1.00 36.20 ? 334  GLY B C     1 
ATOM   11196 O O     . GLY B  1 336  ? -3.578  3.675   114.445 1.00 34.45 ? 334  GLY B O     1 
ATOM   11197 N N     . MET B  1 337  ? -3.197  1.863   113.178 1.00 38.55 ? 335  MET B N     1 
ATOM   11198 C CA    . MET B  1 337  ? -2.709  2.677   112.074 1.00 35.24 ? 335  MET B CA    1 
ATOM   11199 C C     . MET B  1 337  ? -3.847  3.506   111.499 1.00 40.65 ? 335  MET B C     1 
ATOM   11200 O O     . MET B  1 337  ? -4.909  2.968   111.164 1.00 36.87 ? 335  MET B O     1 
ATOM   11201 C CB    . MET B  1 337  ? -2.105  1.806   110.979 1.00 41.33 ? 335  MET B CB    1 
ATOM   11202 C CG    . MET B  1 337  ? -1.511  2.619   109.815 1.00 38.91 ? 335  MET B CG    1 
ATOM   11203 S SD    . MET B  1 337  ? 0.230   2.977   110.089 1.00 51.59 ? 335  MET B SD    1 
ATOM   11204 C CE    . MET B  1 337  ? 0.110   4.545   110.923 1.00 44.09 ? 335  MET B CE    1 
ATOM   11205 N N     . GLY B  1 338  ? -3.624  4.815   111.383 1.00 36.58 ? 336  GLY B N     1 
ATOM   11206 C CA    . GLY B  1 338  ? -4.621  5.723   110.849 1.00 33.18 ? 336  GLY B CA    1 
ATOM   11207 C C     . GLY B  1 338  ? -4.118  6.413   109.595 1.00 33.42 ? 336  GLY B C     1 
ATOM   11208 O O     . GLY B  1 338  ? -2.921  6.638   109.428 1.00 31.70 ? 336  GLY B O     1 
ATOM   11209 N N     . PHE B  1 339  ? -5.051  6.773   108.721 1.00 31.71 ? 337  PHE B N     1 
ATOM   11210 C CA    . PHE B  1 339  ? -4.691  7.364   107.441 1.00 30.24 ? 337  PHE B CA    1 
ATOM   11211 C C     . PHE B  1 339  ? -5.824  8.277   107.002 1.00 30.56 ? 337  PHE B C     1 
ATOM   11212 O O     . PHE B  1 339  ? -6.983  7.854   106.975 1.00 28.77 ? 337  PHE B O     1 
ATOM   11213 C CB    . PHE B  1 339  ? -4.448  6.271   106.392 1.00 28.72 ? 337  PHE B CB    1 
ATOM   11214 C CG    . PHE B  1 339  ? -3.769  6.756   105.150 1.00 29.68 ? 337  PHE B CG    1 
ATOM   11215 C CD1   . PHE B  1 339  ? -2.384  6.818   105.073 1.00 29.78 ? 337  PHE B CD1   1 
ATOM   11216 C CD2   . PHE B  1 339  ? -4.512  7.146   104.053 1.00 29.42 ? 337  PHE B CD2   1 
ATOM   11217 C CE1   . PHE B  1 339  ? -1.761  7.262   103.897 1.00 30.29 ? 337  PHE B CE1   1 
ATOM   11218 C CE2   . PHE B  1 339  ? -3.893  7.582   102.884 1.00 32.20 ? 337  PHE B CE2   1 
ATOM   11219 C CZ    . PHE B  1 339  ? -2.518  7.647   102.818 1.00 29.49 ? 337  PHE B CZ    1 
ATOM   11220 N N     . VAL B  1 340  ? -5.487  9.510   106.656 1.00 27.52 ? 338  VAL B N     1 
ATOM   11221 C CA    . VAL B  1 340  ? -6.456  10.505  106.207 1.00 30.31 ? 338  VAL B CA    1 
ATOM   11222 C C     . VAL B  1 340  ? -6.600  10.421  104.697 1.00 28.92 ? 338  VAL B C     1 
ATOM   11223 O O     . VAL B  1 340  ? -5.602  10.282  103.979 1.00 29.42 ? 338  VAL B O     1 
ATOM   11224 C CB    . VAL B  1 340  ? -6.014  11.920  106.630 1.00 26.92 ? 338  VAL B CB    1 
ATOM   11225 C CG1   . VAL B  1 340  ? -7.001  12.947  106.103 1.00 29.71 ? 338  VAL B CG1   1 
ATOM   11226 C CG2   . VAL B  1 340  ? -5.919  12.004  108.157 1.00 28.25 ? 338  VAL B CG2   1 
ATOM   11227 N N     . VAL B  1 341  ? -7.839  10.520  104.207 1.00 26.87 ? 339  VAL B N     1 
ATOM   11228 C CA    . VAL B  1 341  ? -8.116  10.698  102.788 1.00 26.40 ? 339  VAL B CA    1 
ATOM   11229 C C     . VAL B  1 341  ? -8.977  11.946  102.626 1.00 25.89 ? 339  VAL B C     1 
ATOM   11230 O O     . VAL B  1 341  ? -9.881  12.199  103.429 1.00 29.78 ? 339  VAL B O     1 
ATOM   11231 C CB    . VAL B  1 341  ? -8.798  9.460   102.171 1.00 28.81 ? 339  VAL B CB    1 
ATOM   11232 C CG1   . VAL B  1 341  ? -8.782  9.560   100.648 1.00 32.54 ? 339  VAL B CG1   1 
ATOM   11233 C CG2   . VAL B  1 341  ? -8.084  8.212   102.602 1.00 29.92 ? 339  VAL B CG2   1 
ATOM   11234 N N     . GLN B  1 342  ? -8.694  12.722  101.585 1.00 29.51 ? 340  GLN B N     1 
ATOM   11235 C CA    . GLN B  1 342  ? -9.292  14.039  101.387 1.00 26.98 ? 340  GLN B CA    1 
ATOM   11236 C C     . GLN B  1 342  ? -10.390 13.937  100.330 1.00 29.61 ? 340  GLN B C     1 
ATOM   11237 O O     . GLN B  1 342  ? -10.106 13.688  99.152  1.00 24.98 ? 340  GLN B O     1 
ATOM   11238 C CB    . GLN B  1 342  ? -8.213  15.046  100.982 1.00 26.77 ? 340  GLN B CB    1 
ATOM   11239 C CG    . GLN B  1 342  ? -7.155  15.280  102.048 1.00 25.81 ? 340  GLN B CG    1 
ATOM   11240 C CD    . GLN B  1 342  ? -5.785  15.631  101.474 1.00 25.18 ? 340  GLN B CD    1 
ATOM   11241 O OE1   . GLN B  1 342  ? -5.322  15.001  100.522 1.00 25.84 ? 340  GLN B OE1   1 
ATOM   11242 N NE2   . GLN B  1 342  ? -5.140  16.650  102.046 1.00 23.04 ? 340  GLN B NE2   1 
ATOM   11243 N N     . ALA B  1 343  ? -11.644 14.137  100.755 1.00 27.48 ? 341  ALA B N     1 
ATOM   11244 C CA    . ALA B  1 343  ? -12.779 14.047  99.839  1.00 27.61 ? 341  ALA B CA    1 
ATOM   11245 C C     . ALA B  1 343  ? -12.750 15.124  98.759  1.00 25.42 ? 341  ALA B C     1 
ATOM   11246 O O     . ALA B  1 343  ? -13.340 14.919  97.693  1.00 27.89 ? 341  ALA B O     1 
ATOM   11247 C CB    . ALA B  1 343  ? -14.093 14.141  100.605 1.00 26.26 ? 341  ALA B CB    1 
ATOM   11248 N N     . TYR B  1 344  ? -12.065 16.255  98.990  1.00 25.35 ? 342  TYR B N     1 
ATOM   11249 C CA    . TYR B  1 344  ? -12.018 17.223  97.892  1.00 25.91 ? 342  TYR B CA    1 
ATOM   11250 C C     . TYR B  1 344  ? -11.113 16.772  96.755  1.00 26.66 ? 342  TYR B C     1 
ATOM   11251 O O     . TYR B  1 344  ? -11.074 17.436  95.714  1.00 26.20 ? 342  TYR B O     1 
ATOM   11252 C CB    . TYR B  1 344  ? -11.612 18.623  98.384  1.00 24.09 ? 342  TYR B CB    1 
ATOM   11253 C CG    . TYR B  1 344  ? -10.165 18.920  98.775  1.00 23.23 ? 342  TYR B CG    1 
ATOM   11254 C CD1   . TYR B  1 344  ? -9.174  17.942  98.830  1.00 23.92 ? 342  TYR B CD1   1 
ATOM   11255 C CD2   . TYR B  1 344  ? -9.804  20.227  99.089  1.00 21.50 ? 342  TYR B CD2   1 
ATOM   11256 C CE1   . TYR B  1 344  ? -7.860  18.280  99.198  1.00 24.26 ? 342  TYR B CE1   1 
ATOM   11257 C CE2   . TYR B  1 344  ? -8.534  20.560  99.469  1.00 25.35 ? 342  TYR B CE2   1 
ATOM   11258 C CZ    . TYR B  1 344  ? -7.563  19.595  99.522  1.00 24.12 ? 342  TYR B CZ    1 
ATOM   11259 O OH    . TYR B  1 344  ? -6.310  19.988  99.909  1.00 24.44 ? 342  TYR B OH    1 
ATOM   11260 N N     . GLY B  1 345  ? -10.424 15.645  96.914  1.00 28.91 ? 343  GLY B N     1 
ATOM   11261 C CA    . GLY B  1 345  ? -9.540  15.143  95.880  1.00 28.11 ? 343  GLY B CA    1 
ATOM   11262 C C     . GLY B  1 345  ? -10.265 14.178  94.955  1.00 26.14 ? 343  GLY B C     1 
ATOM   11263 O O     . GLY B  1 345  ? -11.117 13.395  95.384  1.00 24.71 ? 343  GLY B O     1 
ATOM   11264 N N     . LYS B  1 346  ? -9.907  14.246  93.672  1.00 25.24 ? 344  LYS B N     1 
ATOM   11265 C CA    . LYS B  1 346  ? -10.582 13.428  92.677  1.00 24.21 ? 344  LYS B CA    1 
ATOM   11266 C C     . LYS B  1 346  ? -10.230 11.957  92.830  1.00 27.16 ? 344  LYS B C     1 
ATOM   11267 O O     . LYS B  1 346  ? -10.961 11.096  92.341  1.00 26.62 ? 344  LYS B O     1 
ATOM   11268 C CB    . LYS B  1 346  ? -10.227 13.922  91.270  1.00 25.01 ? 344  LYS B CB    1 
ATOM   11269 C CG    . LYS B  1 346  ? -10.542 15.405  91.045  1.00 25.13 ? 344  LYS B CG    1 
ATOM   11270 C CD    . LYS B  1 346  ? -10.213 15.857  89.620  1.00 28.65 ? 344  LYS B CD    1 
ATOM   11271 C CE    . LYS B  1 346  ? -10.996 17.114  89.245  1.00 28.08 ? 344  LYS B CE    1 
ATOM   11272 N NZ    . LYS B  1 346  ? -10.439 17.801  88.046  1.00 27.26 ? 344  LYS B NZ    1 
ATOM   11273 N N     . ARG B  1 347  ? -9.136  11.646  93.508  1.00 27.01 ? 345  ARG B N     1 
ATOM   11274 C CA    . ARG B  1 347  ? -8.723  10.262  93.634  1.00 29.46 ? 345  ARG B CA    1 
ATOM   11275 C C     . ARG B  1 347  ? -9.332  9.567   94.842  1.00 28.26 ? 345  ARG B C     1 
ATOM   11276 O O     . ARG B  1 347  ? -9.173  8.352   94.978  1.00 31.30 ? 345  ARG B O     1 
ATOM   11277 C CB    . ARG B  1 347  ? -7.199  10.195  93.695  1.00 26.72 ? 345  ARG B CB    1 
ATOM   11278 C CG    . ARG B  1 347  ? -6.561  10.588  92.376  1.00 24.57 ? 345  ARG B CG    1 
ATOM   11279 C CD    . ARG B  1 347  ? -5.070  10.863  92.555  1.00 23.29 ? 345  ARG B CD    1 
ATOM   11280 N NE    . ARG B  1 347  ? -4.819  12.091  93.313  1.00 25.01 ? 345  ARG B NE    1 
ATOM   11281 C CZ    . ARG B  1 347  ? -3.628  12.442  93.777  1.00 24.82 ? 345  ARG B CZ    1 
ATOM   11282 N NH1   . ARG B  1 347  ? -2.569  11.662  93.612  1.00 22.66 ? 345  ARG B NH1   1 
ATOM   11283 N NH2   . ARG B  1 347  ? -3.496  13.595  94.439  1.00 24.38 ? 345  ARG B NH2   1 
ATOM   11284 N N     . CYS B  1 348  ? -10.031 10.312  95.696  1.00 27.09 ? 346  CYS B N     1 
ATOM   11285 C CA    . CYS B  1 348  ? -10.471 9.819   97.001  1.00 31.65 ? 346  CYS B CA    1 
ATOM   11286 C C     . CYS B  1 348  ? -11.197 8.477   96.959  1.00 30.38 ? 346  CYS B C     1 
ATOM   11287 O O     . CYS B  1 348  ? -10.833 7.591   97.747  1.00 28.83 ? 346  CYS B O     1 
ATOM   11288 C CB    . CYS B  1 348  ? -11.334 10.897  97.670  1.00 26.85 ? 346  CYS B CB    1 
ATOM   11289 S SG    . CYS B  1 348  ? -11.856 10.507  99.402  1.00 37.31 ? 346  CYS B SG    1 
ATOM   11290 N N     . PRO B  1 349  ? -12.199 8.242   96.095  1.00 28.20 ? 347  PRO B N     1 
ATOM   11291 C CA    . PRO B  1 349  ? -12.853 6.924   96.121  1.00 34.87 ? 347  PRO B CA    1 
ATOM   11292 C C     . PRO B  1 349  ? -11.919 5.798   95.714  1.00 32.84 ? 347  PRO B C     1 
ATOM   11293 O O     . PRO B  1 349  ? -12.019 4.689   96.252  1.00 33.40 ? 347  PRO B O     1 
ATOM   11294 C CB    . PRO B  1 349  ? -14.030 7.082   95.136  1.00 30.43 ? 347  PRO B CB    1 
ATOM   11295 C CG    . PRO B  1 349  ? -13.664 8.215   94.274  1.00 29.88 ? 347  PRO B CG    1 
ATOM   11296 C CD    . PRO B  1 349  ? -12.824 9.143   95.110  1.00 30.92 ? 347  PRO B CD    1 
ATOM   11297 N N     . PHE B  1 350  ? -11.002 6.055   94.787  1.00 30.44 ? 348  PHE B N     1 
ATOM   11298 C CA    . PHE B  1 350  ? -10.070 5.014   94.380  1.00 31.90 ? 348  PHE B CA    1 
ATOM   11299 C C     . PHE B  1 350  ? -9.009  4.774   95.446  1.00 33.65 ? 348  PHE B C     1 
ATOM   11300 O O     . PHE B  1 350  ? -8.549  3.638   95.612  1.00 31.80 ? 348  PHE B O     1 
ATOM   11301 C CB    . PHE B  1 350  ? -9.443  5.402   93.048  1.00 31.04 ? 348  PHE B CB    1 
ATOM   11302 C CG    . PHE B  1 350  ? -10.458 5.810   92.032  1.00 31.42 ? 348  PHE B CG    1 
ATOM   11303 C CD1   . PHE B  1 350  ? -11.163 4.851   91.321  1.00 38.63 ? 348  PHE B CD1   1 
ATOM   11304 C CD2   . PHE B  1 350  ? -10.747 7.149   91.821  1.00 32.26 ? 348  PHE B CD2   1 
ATOM   11305 C CE1   . PHE B  1 350  ? -12.124 5.218   90.400  1.00 37.59 ? 348  PHE B CE1   1 
ATOM   11306 C CE2   . PHE B  1 350  ? -11.707 7.519   90.898  1.00 33.12 ? 348  PHE B CE2   1 
ATOM   11307 C CZ    . PHE B  1 350  ? -12.389 6.556   90.189  1.00 38.22 ? 348  PHE B CZ    1 
ATOM   11308 N N     . VAL B  1 351  ? -8.619  5.821   96.180  1.00 31.58 ? 349  VAL B N     1 
ATOM   11309 C CA    . VAL B  1 351  ? -7.705  5.631   97.304  1.00 30.12 ? 349  VAL B CA    1 
ATOM   11310 C C     . VAL B  1 351  ? -8.361  4.773   98.376  1.00 33.58 ? 349  VAL B C     1 
ATOM   11311 O O     . VAL B  1 351  ? -7.717  3.907   98.978  1.00 32.11 ? 349  VAL B O     1 
ATOM   11312 C CB    . VAL B  1 351  ? -7.248  6.989   97.869  1.00 30.16 ? 349  VAL B CB    1 
ATOM   11313 C CG1   . VAL B  1 351  ? -6.317  6.790   99.107  1.00 27.07 ? 349  VAL B CG1   1 
ATOM   11314 C CG2   . VAL B  1 351  ? -6.550  7.790   96.804  1.00 29.99 ? 349  VAL B CG2   1 
ATOM   11315 N N     . LEU B  1 352  ? -9.656  4.989   98.618  1.00 31.84 ? 350  LEU B N     1 
ATOM   11316 C CA    . LEU B  1 352  ? -10.375 4.174   99.589  1.00 30.91 ? 350  LEU B CA    1 
ATOM   11317 C C     . LEU B  1 352  ? -10.473 2.720   99.138  1.00 35.89 ? 350  LEU B C     1 
ATOM   11318 O O     . LEU B  1 352  ? -10.357 1.805   99.962  1.00 36.86 ? 350  LEU B O     1 
ATOM   11319 C CB    . LEU B  1 352  ? -11.762 4.764   99.827  1.00 35.30 ? 350  LEU B CB    1 
ATOM   11320 C CG    . LEU B  1 352  ? -11.756 6.070   100.610 1.00 32.69 ? 350  LEU B CG    1 
ATOM   11321 C CD1   . LEU B  1 352  ? -13.151 6.619   100.728 1.00 32.71 ? 350  LEU B CD1   1 
ATOM   11322 C CD2   . LEU B  1 352  ? -11.173 5.801   101.992 1.00 33.89 ? 350  LEU B CD2   1 
ATOM   11323 N N     . ASP B  1 353  ? -10.704 2.486   97.839  1.00 35.49 ? 351  ASP B N     1 
ATOM   11324 C CA    . ASP B  1 353  ? -10.641 1.128   97.297  1.00 36.64 ? 351  ASP B CA    1 
ATOM   11325 C C     . ASP B  1 353  ? -9.311  0.466   97.644  1.00 37.00 ? 351  ASP B C     1 
ATOM   11326 O O     . ASP B  1 353  ? -9.267  -0.694  98.085  1.00 35.26 ? 351  ASP B O     1 
ATOM   11327 C CB    . ASP B  1 353  ? -10.830 1.156   95.774  1.00 33.24 ? 351  ASP B CB    1 
ATOM   11328 C CG    . ASP B  1 353  ? -12.266 1.421   95.358  1.00 40.75 ? 351  ASP B CG    1 
ATOM   11329 O OD1   . ASP B  1 353  ? -13.187 1.158   96.158  1.00 40.50 ? 351  ASP B OD1   1 
ATOM   11330 O OD2   . ASP B  1 353  ? -12.471 1.889   94.215  1.00 41.66 ? 351  ASP B OD2   1 
ATOM   11331 N N     . PHE B  1 354  ? -8.214  1.204   97.456  1.00 32.41 ? 352  PHE B N     1 
ATOM   11332 C CA    . PHE B  1 354  ? -6.882  0.681   97.755  1.00 35.19 ? 352  PHE B CA    1 
ATOM   11333 C C     . PHE B  1 354  ? -6.701  0.423   99.246  1.00 37.00 ? 352  PHE B C     1 
ATOM   11334 O O     . PHE B  1 354  ? -6.156  -0.618  99.636  1.00 38.13 ? 352  PHE B O     1 
ATOM   11335 C CB    . PHE B  1 354  ? -5.813  1.646   97.242  1.00 35.65 ? 352  PHE B CB    1 
ATOM   11336 C CG    . PHE B  1 354  ? -4.429  1.321   97.724  1.00 34.81 ? 352  PHE B CG    1 
ATOM   11337 C CD1   . PHE B  1 354  ? -3.637  0.428   97.035  1.00 35.27 ? 352  PHE B CD1   1 
ATOM   11338 C CD2   . PHE B  1 354  ? -3.932  1.898   98.879  1.00 34.32 ? 352  PHE B CD2   1 
ATOM   11339 C CE1   . PHE B  1 354  ? -2.374  0.117   97.485  1.00 36.80 ? 352  PHE B CE1   1 
ATOM   11340 C CE2   . PHE B  1 354  ? -2.674  1.587   99.340  1.00 37.25 ? 352  PHE B CE2   1 
ATOM   11341 C CZ    . PHE B  1 354  ? -1.889  0.702   98.638  1.00 39.32 ? 352  PHE B CZ    1 
ATOM   11342 N N     . ILE B  1 355  ? -7.131  1.362   100.097 1.00 32.96 ? 353  ILE B N     1 
ATOM   11343 C CA    . ILE B  1 355  ? -6.972  1.180   101.540 1.00 34.31 ? 353  ILE B CA    1 
ATOM   11344 C C     . ILE B  1 355  ? -7.818  0.015   102.039 1.00 39.39 ? 353  ILE B C     1 
ATOM   11345 O O     . ILE B  1 355  ? -7.363  -0.787  102.861 1.00 39.53 ? 353  ILE B O     1 
ATOM   11346 C CB    . ILE B  1 355  ? -7.310  2.479   102.293 1.00 35.59 ? 353  ILE B CB    1 
ATOM   11347 C CG1   . ILE B  1 355  ? -6.292  3.563   101.943 1.00 33.97 ? 353  ILE B CG1   1 
ATOM   11348 C CG2   . ILE B  1 355  ? -7.369  2.222   103.803 1.00 37.86 ? 353  ILE B CG2   1 
ATOM   11349 C CD1   . ILE B  1 355  ? -6.616  4.938   102.524 1.00 32.03 ? 353  ILE B CD1   1 
ATOM   11350 N N     . ILE B  1 356  ? -9.062  -0.095  101.559 1.00 33.74 ? 354  ILE B N     1 
ATOM   11351 C CA    . ILE B  1 356  ? -9.934  -1.183  101.997 1.00 41.10 ? 354  ILE B CA    1 
ATOM   11352 C C     . ILE B  1 356  ? -9.361  -2.526  101.567 1.00 39.11 ? 354  ILE B C     1 
ATOM   11353 O O     . ILE B  1 356  ? -9.397  -3.504  102.323 1.00 42.11 ? 354  ILE B O     1 
ATOM   11354 C CB    . ILE B  1 356  ? -11.367 -0.968  101.474 1.00 38.22 ? 354  ILE B CB    1 
ATOM   11355 C CG1   . ILE B  1 356  ? -12.022 0.195   102.220 1.00 38.94 ? 354  ILE B CG1   1 
ATOM   11356 C CG2   . ILE B  1 356  ? -12.205 -2.235  101.625 1.00 39.94 ? 354  ILE B CG2   1 
ATOM   11357 C CD1   . ILE B  1 356  ? -13.258 0.757   101.535 1.00 39.21 ? 354  ILE B CD1   1 
ATOM   11358 N N     . ASP B  1 357  ? -8.779  -2.586  100.372 1.00 37.35 ? 355  ASP B N     1 
ATOM   11359 C CA    . ASP B  1 357  ? -8.156  -3.834  99.950  1.00 41.43 ? 355  ASP B CA    1 
ATOM   11360 C C     . ASP B  1 357  ? -6.890  -4.123  100.750 1.00 41.18 ? 355  ASP B C     1 
ATOM   11361 O O     . ASP B  1 357  ? -6.627  -5.280  101.102 1.00 40.64 ? 355  ASP B O     1 
ATOM   11362 C CB    . ASP B  1 357  ? -7.858  -3.791  98.453  1.00 42.92 ? 355  ASP B CB    1 
ATOM   11363 C CG    . ASP B  1 357  ? -7.015  -4.953  98.000  1.00 43.23 ? 355  ASP B CG    1 
ATOM   11364 O OD1   . ASP B  1 357  ? -7.538  -6.079  97.952  1.00 43.37 ? 355  ASP B OD1   1 
ATOM   11365 O OD2   . ASP B  1 357  ? -5.821  -4.749  97.705  1.00 41.96 ? 355  ASP B OD2   1 
ATOM   11366 N N     . LEU B  1 358  ? -6.091  -3.087  101.048 1.00 38.74 ? 356  LEU B N     1 
ATOM   11367 C CA    . LEU B  1 358  ? -4.901  -3.283  101.872 1.00 39.63 ? 356  LEU B CA    1 
ATOM   11368 C C     . LEU B  1 358  ? -5.270  -3.858  103.234 1.00 40.48 ? 356  LEU B C     1 
ATOM   11369 O O     . LEU B  1 358  ? -4.578  -4.737  103.756 1.00 39.31 ? 356  LEU B O     1 
ATOM   11370 C CB    . LEU B  1 358  ? -4.142  -1.961  102.032 1.00 36.75 ? 356  LEU B CB    1 
ATOM   11371 C CG    . LEU B  1 358  ? -2.841  -1.914  102.863 1.00 37.80 ? 356  LEU B CG    1 
ATOM   11372 C CD1   . LEU B  1 358  ? -1.854  -2.980  102.439 1.00 35.58 ? 356  LEU B CD1   1 
ATOM   11373 C CD2   . LEU B  1 358  ? -2.183  -0.532  102.779 1.00 35.86 ? 356  LEU B CD2   1 
ATOM   11374 N N     . ALA B  1 359  ? -6.365  -3.375  103.821 1.00 39.05 ? 357  ALA B N     1 
ATOM   11375 C CA    . ALA B  1 359  ? -6.753  -3.834  105.145 1.00 42.24 ? 357  ALA B CA    1 
ATOM   11376 C C     . ALA B  1 359  ? -7.220  -5.283  105.106 1.00 45.93 ? 357  ALA B C     1 
ATOM   11377 O O     . ALA B  1 359  ? -6.974  -6.049  106.048 1.00 43.32 ? 357  ALA B O     1 
ATOM   11378 C CB    . ALA B  1 359  ? -7.842  -2.926  105.706 1.00 40.34 ? 357  ALA B CB    1 
ATOM   11379 N N     . ARG B  1 360  ? -7.886  -5.679  104.021 1.00 45.54 ? 358  ARG B N     1 
ATOM   11380 C CA    . ARG B  1 360  ? -8.348  -7.058  103.900 1.00 47.48 ? 358  ARG B CA    1 
ATOM   11381 C C     . ARG B  1 360  ? -7.180  -8.029  103.825 1.00 46.54 ? 358  ARG B C     1 
ATOM   11382 O O     . ARG B  1 360  ? -7.137  -9.020  104.565 1.00 47.61 ? 358  ARG B O     1 
ATOM   11383 C CB    . ARG B  1 360  ? -9.237  -7.214  102.670 1.00 50.63 ? 358  ARG B CB    1 
ATOM   11384 C CG    . ARG B  1 360  ? -10.660 -6.771  102.880 1.00 52.08 ? 358  ARG B CG    1 
ATOM   11385 C CD    . ARG B  1 360  ? -11.574 -7.486  101.904 1.00 57.11 ? 358  ARG B CD    1 
ATOM   11386 N NE    . ARG B  1 360  ? -12.858 -6.812  101.779 1.00 53.63 ? 358  ARG B NE    1 
ATOM   11387 C CZ    . ARG B  1 360  ? -13.111 -5.861  100.893 1.00 56.21 ? 358  ARG B CZ    1 
ATOM   11388 N NH1   . ARG B  1 360  ? -12.181 -5.441  100.048 1.00 58.82 ? 358  ARG B NH1   1 
ATOM   11389 N NH2   . ARG B  1 360  ? -14.328 -5.323  100.847 1.00 55.17 ? 358  ARG B NH2   1 
ATOM   11390 N N     . ARG B  1 361  ? -6.221  -7.761  102.936 1.00 44.29 ? 359  ARG B N     1 
ATOM   11391 C CA    . ARG B  1 361  ? -5.139  -8.708  102.708 1.00 46.49 ? 359  ARG B CA    1 
ATOM   11392 C C     . ARG B  1 361  ? -4.064  -8.653  103.781 1.00 45.07 ? 359  ARG B C     1 
ATOM   11393 O O     . ARG B  1 361  ? -3.252  -9.578  103.864 1.00 43.48 ? 359  ARG B O     1 
ATOM   11394 C CB    . ARG B  1 361  ? -4.503  -8.474  101.334 1.00 45.53 ? 359  ARG B CB    1 
ATOM   11395 C CG    . ARG B  1 361  ? -3.946  -7.094  101.103 1.00 44.65 ? 359  ARG B CG    1 
ATOM   11396 C CD    . ARG B  1 361  ? -3.514  -6.918  99.638  1.00 46.60 ? 359  ARG B CD    1 
ATOM   11397 N NE    . ARG B  1 361  ? -3.325  -5.510  99.288  1.00 44.20 ? 359  ARG B NE    1 
ATOM   11398 C CZ    . ARG B  1 361  ? -2.164  -4.866  99.318  1.00 41.43 ? 359  ARG B CZ    1 
ATOM   11399 N NH1   . ARG B  1 361  ? -1.042  -5.475  99.660  1.00 42.28 ? 359  ARG B NH1   1 
ATOM   11400 N NH2   . ARG B  1 361  ? -2.129  -3.573  98.998  1.00 37.05 ? 359  ARG B NH2   1 
ATOM   11401 N N     . SER B  1 362  ? -4.021  -7.593  104.590 1.00 44.27 ? 360  SER B N     1 
ATOM   11402 C CA    . SER B  1 362  ? -3.015  -7.491  105.638 1.00 41.09 ? 360  SER B CA    1 
ATOM   11403 C C     . SER B  1 362  ? -3.543  -7.856  107.017 1.00 41.62 ? 360  SER B C     1 
ATOM   11404 O O     . SER B  1 362  ? -2.743  -8.020  107.943 1.00 43.61 ? 360  SER B O     1 
ATOM   11405 C CB    . SER B  1 362  ? -2.434  -6.072  105.687 1.00 42.42 ? 360  SER B CB    1 
ATOM   11406 O OG    . SER B  1 362  ? -3.427  -5.152  106.088 1.00 39.46 ? 360  SER B OG    1 
ATOM   11407 N N     . GLY B  1 363  ? -4.854  -7.977  107.189 1.00 39.74 ? 361  GLY B N     1 
ATOM   11408 C CA    . GLY B  1 363  ? -5.364  -8.339  108.499 1.00 40.63 ? 361  GLY B CA    1 
ATOM   11409 C C     . GLY B  1 363  ? -5.317  -7.214  109.509 1.00 42.90 ? 361  GLY B C     1 
ATOM   11410 O O     . GLY B  1 363  ? -5.232  -7.473  110.712 1.00 45.14 ? 361  GLY B O     1 
ATOM   11411 N N     . ARG B  1 364  ? -5.365  -5.968  109.045 1.00 41.75 ? 362  ARG B N     1 
ATOM   11412 C CA    . ARG B  1 364  ? -5.357  -4.787  109.899 1.00 45.97 ? 362  ARG B CA    1 
ATOM   11413 C C     . ARG B  1 364  ? -6.635  -4.003  109.671 1.00 43.18 ? 362  ARG B C     1 
ATOM   11414 O O     . ARG B  1 364  ? -6.950  -3.646  108.532 1.00 46.12 ? 362  ARG B O     1 
ATOM   11415 C CB    . ARG B  1 364  ? -4.171  -3.866  109.596 1.00 40.98 ? 362  ARG B CB    1 
ATOM   11416 C CG    . ARG B  1 364  ? -2.839  -4.536  109.605 1.00 39.70 ? 362  ARG B CG    1 
ATOM   11417 C CD    . ARG B  1 364  ? -2.310  -4.711  111.019 1.00 42.91 ? 362  ARG B CD    1 
ATOM   11418 N NE    . ARG B  1 364  ? -1.015  -5.375  110.988 1.00 41.23 ? 362  ARG B NE    1 
ATOM   11419 C CZ    . ARG B  1 364  ? 0.134   -4.752  110.768 1.00 39.71 ? 362  ARG B CZ    1 
ATOM   11420 N NH1   . ARG B  1 364  ? 0.189   -3.441  110.618 1.00 37.83 ? 362  ARG B NH1   1 
ATOM   11421 N NH2   . ARG B  1 364  ? 1.255   -5.465  110.698 1.00 40.01 ? 362  ARG B NH2   1 
ATOM   11422 N N     . ARG B  1 365  ? -7.361  -3.722  110.743 1.00 39.50 ? 363  ARG B N     1 
ATOM   11423 C CA    . ARG B  1 365  ? -8.390  -2.700  110.654 1.00 43.36 ? 363  ARG B CA    1 
ATOM   11424 C C     . ARG B  1 365  ? -7.699  -1.345  110.627 1.00 38.10 ? 363  ARG B C     1 
ATOM   11425 O O     . ARG B  1 365  ? -7.121  -0.915  111.629 1.00 41.91 ? 363  ARG B O     1 
ATOM   11426 C CB    . ARG B  1 365  ? -9.370  -2.802  111.815 1.00 44.78 ? 363  ARG B CB    1 
ATOM   11427 C CG    . ARG B  1 365  ? -10.581 -1.914  111.628 1.00 43.52 ? 363  ARG B CG    1 
ATOM   11428 C CD    . ARG B  1 365  ? -11.739 -2.419  112.470 1.00 47.14 ? 363  ARG B CD    1 
ATOM   11429 N NE    . ARG B  1 365  ? -12.992 -1.762  112.116 1.00 46.24 ? 363  ARG B NE    1 
ATOM   11430 C CZ    . ARG B  1 365  ? -13.689 -0.990  112.937 1.00 45.95 ? 363  ARG B CZ    1 
ATOM   11431 N NH1   . ARG B  1 365  ? -13.298 -0.776  114.184 1.00 42.63 ? 363  ARG B NH1   1 
ATOM   11432 N NH2   . ARG B  1 365  ? -14.817 -0.431  112.503 1.00 45.60 ? 363  ARG B NH2   1 
ATOM   11433 N N     . ILE B  1 366  ? -7.709  -0.708  109.479 1.00 38.92 ? 364  ILE B N     1 
ATOM   11434 C CA    . ILE B  1 366  ? -7.112  0.606   109.295 1.00 37.03 ? 364  ILE B CA    1 
ATOM   11435 C C     . ILE B  1 366  ? -8.141  1.660   109.676 1.00 40.27 ? 364  ILE B C     1 
ATOM   11436 O O     . ILE B  1 366  ? -9.320  1.566   109.304 1.00 38.73 ? 364  ILE B O     1 
ATOM   11437 C CB    . ILE B  1 366  ? -6.636  0.784   107.840 1.00 36.37 ? 364  ILE B CB    1 
ATOM   11438 C CG1   . ILE B  1 366  ? -5.584  -0.267  107.486 1.00 39.16 ? 364  ILE B CG1   1 
ATOM   11439 C CG2   . ILE B  1 366  ? -6.110  2.197   107.613 1.00 32.31 ? 364  ILE B CG2   1 
ATOM   11440 C CD1   . ILE B  1 366  ? -5.052  -0.151  106.062 1.00 41.02 ? 364  ILE B CD1   1 
ATOM   11441 N N     . MET B  1 367  ? -7.701  2.664   110.431 1.00 38.47 ? 365  MET B N     1 
ATOM   11442 C CA    . MET B  1 367  ? -8.549  3.788   110.803 1.00 35.08 ? 365  MET B CA    1 
ATOM   11443 C C     . MET B  1 367  ? -8.484  4.820   109.688 1.00 36.80 ? 365  MET B C     1 
ATOM   11444 O O     . MET B  1 367  ? -7.396  5.291   109.344 1.00 33.88 ? 365  MET B O     1 
ATOM   11445 C CB    . MET B  1 367  ? -8.097  4.379   112.137 1.00 36.73 ? 365  MET B CB    1 
ATOM   11446 C CG    . MET B  1 367  ? -7.959  3.317   113.227 1.00 36.35 ? 365  MET B CG    1 
ATOM   11447 S SD    . MET B  1 367  ? -7.295  3.952   114.779 1.00 40.11 ? 365  MET B SD    1 
ATOM   11448 C CE    . MET B  1 367  ? -8.698  4.846   115.435 1.00 43.10 ? 365  MET B CE    1 
ATOM   11449 N N     . VAL B  1 368  ? -9.633  5.160   109.110 1.00 33.02 ? 366  VAL B N     1 
ATOM   11450 C CA    . VAL B  1 368  ? -9.664  6.042   107.949 1.00 31.22 ? 366  VAL B CA    1 
ATOM   11451 C C     . VAL B  1 368  ? -10.362 7.335   108.327 1.00 30.85 ? 366  VAL B C     1 
ATOM   11452 O O     . VAL B  1 368  ? -11.585 7.364   108.512 1.00 32.48 ? 366  VAL B O     1 
ATOM   11453 C CB    . VAL B  1 368  ? -10.341 5.400   106.738 1.00 31.47 ? 366  VAL B CB    1 
ATOM   11454 C CG1   . VAL B  1 368  ? -10.122 6.306   105.540 1.00 30.94 ? 366  VAL B CG1   1 
ATOM   11455 C CG2   . VAL B  1 368  ? -9.750  4.046   106.476 1.00 36.10 ? 366  VAL B CG2   1 
ATOM   11456 N N     . ARG B  1 369  ? -9.602  8.424   108.403 1.00 29.93 ? 367  ARG B N     1 
ATOM   11457 C CA    . ARG B  1 369  ? -10.191 9.728   108.660 1.00 29.53 ? 367  ARG B CA    1 
ATOM   11458 C C     . ARG B  1 369  ? -10.564 10.331  107.320 1.00 32.04 ? 367  ARG B C     1 
ATOM   11459 O O     . ARG B  1 369  ? -9.686  10.665  106.514 1.00 30.15 ? 367  ARG B O     1 
ATOM   11460 C CB    . ARG B  1 369  ? -9.251  10.659  109.424 1.00 32.50 ? 367  ARG B CB    1 
ATOM   11461 C CG    . ARG B  1 369  ? -9.933  11.980  109.760 1.00 32.28 ? 367  ARG B CG    1 
ATOM   11462 C CD    . ARG B  1 369  ? -8.953  13.050  110.172 1.00 34.47 ? 367  ARG B CD    1 
ATOM   11463 N NE    . ARG B  1 369  ? -8.278  12.694  111.408 1.00 31.87 ? 367  ARG B NE    1 
ATOM   11464 C CZ    . ARG B  1 369  ? -7.084  13.139  111.758 1.00 35.89 ? 367  ARG B CZ    1 
ATOM   11465 N NH1   . ARG B  1 369  ? -6.388  13.943  110.963 1.00 36.19 ? 367  ARG B NH1   1 
ATOM   11466 N NH2   . ARG B  1 369  ? -6.568  12.754  112.925 1.00 32.58 ? 367  ARG B NH2   1 
ATOM   11467 N N     . LEU B  1 370  ? -11.862 10.460  107.082 1.00 29.25 ? 368  LEU B N     1 
ATOM   11468 C CA    . LEU B  1 370  ? -12.362 11.138  105.901 1.00 29.60 ? 368  LEU B CA    1 
ATOM   11469 C C     . LEU B  1 370  ? -12.497 12.618  106.215 1.00 29.68 ? 368  LEU B C     1 
ATOM   11470 O O     . LEU B  1 370  ? -13.243 13.001  107.117 1.00 33.83 ? 368  LEU B O     1 
ATOM   11471 C CB    . LEU B  1 370  ? -13.697 10.544  105.472 1.00 29.47 ? 368  LEU B CB    1 
ATOM   11472 C CG    . LEU B  1 370  ? -14.267 11.151  104.203 1.00 34.50 ? 368  LEU B CG    1 
ATOM   11473 C CD1   . LEU B  1 370  ? -13.309 10.931  103.036 1.00 29.05 ? 368  LEU B CD1   1 
ATOM   11474 C CD2   . LEU B  1 370  ? -15.616 10.512  103.940 1.00 31.86 ? 368  LEU B CD2   1 
ATOM   11475 N N     . VAL B  1 371  ? -11.760 13.450  105.488 1.00 28.45 ? 369  VAL B N     1 
ATOM   11476 C CA    . VAL B  1 371  ? -11.846 14.890  105.635 1.00 26.48 ? 369  VAL B CA    1 
ATOM   11477 C C     . VAL B  1 371  ? -12.208 15.455  104.278 1.00 27.86 ? 369  VAL B C     1 
ATOM   11478 O O     . VAL B  1 371  ? -12.171 14.759  103.262 1.00 27.33 ? 369  VAL B O     1 
ATOM   11479 C CB    . VAL B  1 371  ? -10.532 15.503  106.144 1.00 29.02 ? 369  VAL B CB    1 
ATOM   11480 C CG1   . VAL B  1 371  ? -10.056 14.748  107.369 1.00 29.05 ? 369  VAL B CG1   1 
ATOM   11481 C CG2   . VAL B  1 371  ? -9.489  15.435  105.053 1.00 27.99 ? 369  VAL B CG2   1 
ATOM   11482 N N     . LYS B  1 372  ? -12.545 16.739  104.254 1.00 27.10 ? 370  LYS B N     1 
ATOM   11483 C CA    . LYS B  1 372  ? -12.689 17.362  102.946 1.00 27.20 ? 370  LYS B CA    1 
ATOM   11484 C C     . LYS B  1 372  ? -11.325 17.789  102.401 1.00 24.80 ? 370  LYS B C     1 
ATOM   11485 O O     . LYS B  1 372  ? -10.897 17.313  101.348 1.00 27.02 ? 370  LYS B O     1 
ATOM   11486 C CB    . LYS B  1 372  ? -13.704 18.502  103.024 1.00 24.84 ? 370  LYS B CB    1 
ATOM   11487 C CG    . LYS B  1 372  ? -15.108 17.905  103.324 1.00 26.78 ? 370  LYS B CG    1 
ATOM   11488 C CD    . LYS B  1 372  ? -16.216 18.904  103.415 1.00 32.15 ? 370  LYS B CD    1 
ATOM   11489 C CE    . LYS B  1 372  ? -17.522 18.203  103.821 1.00 34.50 ? 370  LYS B CE    1 
ATOM   11490 N NZ    . LYS B  1 372  ? -18.594 19.190  104.113 1.00 30.72 ? 370  LYS B NZ    1 
ATOM   11491 N N     . GLY B  1 373  ? -10.600 18.631  103.116 1.00 24.64 ? 371  GLY B N     1 
ATOM   11492 C CA    . GLY B  1 373  ? -9.205  18.884  102.787 1.00 23.86 ? 371  GLY B CA    1 
ATOM   11493 C C     . GLY B  1 373  ? -8.796  20.322  103.018 1.00 26.82 ? 371  GLY B C     1 
ATOM   11494 O O     . GLY B  1 373  ? -9.572  21.254  102.816 1.00 26.14 ? 371  GLY B O     1 
ATOM   11495 N N     . ALA B  1 374  ? -7.535  20.510  103.417 1.00 24.37 ? 372  ALA B N     1 
ATOM   11496 C CA    . ALA B  1 374  ? -7.098  21.765  104.004 1.00 25.90 ? 372  ALA B CA    1 
ATOM   11497 C C     . ALA B  1 374  ? -6.294  22.664  103.058 1.00 23.46 ? 372  ALA B C     1 
ATOM   11498 O O     . ALA B  1 374  ? -5.968  23.792  103.445 1.00 24.78 ? 372  ALA B O     1 
ATOM   11499 C CB    . ALA B  1 374  ? -6.281  21.475  105.272 1.00 27.77 ? 372  ALA B CB    1 
ATOM   11500 N N     . TYR B  1 375  ? -6.010  22.231  101.817 1.00 22.11 ? 373  TYR B N     1 
ATOM   11501 C CA    . TYR B  1 375  ? -5.041  22.910  100.956 1.00 25.97 ? 373  TYR B CA    1 
ATOM   11502 C C     . TYR B  1 375  ? -5.656  23.432  99.661  1.00 23.49 ? 373  TYR B C     1 
ATOM   11503 O O     . TYR B  1 375  ? -4.951  23.581  98.664  1.00 21.46 ? 373  TYR B O     1 
ATOM   11504 C CB    . TYR B  1 375  ? -3.873  21.992  100.608 1.00 22.13 ? 373  TYR B CB    1 
ATOM   11505 C CG    . TYR B  1 375  ? -3.158  21.428  101.811 1.00 26.49 ? 373  TYR B CG    1 
ATOM   11506 C CD1   . TYR B  1 375  ? -3.694  20.357  102.511 1.00 26.33 ? 373  TYR B CD1   1 
ATOM   11507 C CD2   . TYR B  1 375  ? -1.945  21.969  102.246 1.00 28.66 ? 373  TYR B CD2   1 
ATOM   11508 C CE1   . TYR B  1 375  ? -3.053  19.838  103.614 1.00 28.18 ? 373  TYR B CE1   1 
ATOM   11509 C CE2   . TYR B  1 375  ? -1.293  21.449  103.346 1.00 29.28 ? 373  TYR B CE2   1 
ATOM   11510 C CZ    . TYR B  1 375  ? -1.856  20.382  104.023 1.00 30.43 ? 373  TYR B CZ    1 
ATOM   11511 O OH    . TYR B  1 375  ? -1.232  19.844  105.117 1.00 29.81 ? 373  TYR B OH    1 
ATOM   11512 N N     . TRP B  1 376  ? -6.945  23.764  99.675  1.00 23.06 ? 374  TRP B N     1 
ATOM   11513 C CA    . TRP B  1 376  ? -7.664  23.973  98.422  1.00 20.85 ? 374  TRP B CA    1 
ATOM   11514 C C     . TRP B  1 376  ? -7.083  25.121  97.601  1.00 24.35 ? 374  TRP B C     1 
ATOM   11515 O O     . TRP B  1 376  ? -6.779  24.938  96.425  1.00 22.02 ? 374  TRP B O     1 
ATOM   11516 C CB    . TRP B  1 376  ? -9.157  24.196  98.688  1.00 22.17 ? 374  TRP B CB    1 
ATOM   11517 C CG    . TRP B  1 376  ? -9.904  24.319  97.440  1.00 24.46 ? 374  TRP B CG    1 
ATOM   11518 C CD1   . TRP B  1 376  ? -10.294 23.306  96.629  1.00 23.21 ? 374  TRP B CD1   1 
ATOM   11519 C CD2   . TRP B  1 376  ? -10.329 25.534  96.805  1.00 25.51 ? 374  TRP B CD2   1 
ATOM   11520 N NE1   . TRP B  1 376  ? -10.960 23.804  95.534  1.00 24.50 ? 374  TRP B NE1   1 
ATOM   11521 C CE2   . TRP B  1 376  ? -10.993 25.171  95.617  1.00 28.07 ? 374  TRP B CE2   1 
ATOM   11522 C CE3   . TRP B  1 376  ? -10.227 26.892  97.134  1.00 28.07 ? 374  TRP B CE3   1 
ATOM   11523 C CZ2   . TRP B  1 376  ? -11.547 26.114  94.752  1.00 22.19 ? 374  TRP B CZ2   1 
ATOM   11524 C CZ3   . TRP B  1 376  ? -10.776 27.828  96.274  1.00 24.24 ? 374  TRP B CZ3   1 
ATOM   11525 C CH2   . TRP B  1 376  ? -11.436 27.433  95.099  1.00 25.01 ? 374  TRP B CH2   1 
ATOM   11526 N N     . ASP B  1 377  ? -6.961  26.321  98.187  1.00 23.26 ? 375  ASP B N     1 
ATOM   11527 C CA    . ASP B  1 377  ? -6.437  27.470  97.438  1.00 24.88 ? 375  ASP B CA    1 
ATOM   11528 C C     . ASP B  1 377  ? -5.054  27.178  96.877  1.00 25.63 ? 375  ASP B C     1 
ATOM   11529 O O     . ASP B  1 377  ? -4.731  27.557  95.741  1.00 24.78 ? 375  ASP B O     1 
ATOM   11530 C CB    . ASP B  1 377  ? -6.359  28.709  98.340  1.00 30.54 ? 375  ASP B CB    1 
ATOM   11531 C CG    . ASP B  1 377  ? -7.717  29.267  98.691  1.00 38.75 ? 375  ASP B CG    1 
ATOM   11532 O OD1   . ASP B  1 377  ? -8.433  29.703  97.764  1.00 43.18 ? 375  ASP B OD1   1 
ATOM   11533 O OD2   . ASP B  1 377  ? -8.072  29.267  99.889  1.00 44.80 ? 375  ASP B OD2   1 
ATOM   11534 N N     . ALA B  1 378  ? -4.218  26.509  97.672  1.00 23.55 ? 376  ALA B N     1 
ATOM   11535 C CA    . ALA B  1 378  ? -2.867  26.186  97.233  1.00 23.02 ? 376  ALA B CA    1 
ATOM   11536 C C     . ALA B  1 378  ? -2.888  25.234  96.044  1.00 24.13 ? 376  ALA B C     1 
ATOM   11537 O O     . ALA B  1 378  ? -2.065  25.357  95.129  1.00 24.85 ? 376  ALA B O     1 
ATOM   11538 C CB    . ALA B  1 378  ? -2.074  25.578  98.396  1.00 21.36 ? 376  ALA B CB    1 
ATOM   11539 N N     . GLU B  1 379  ? -3.831  24.285  96.027  1.00 20.75 ? 377  GLU B N     1 
ATOM   11540 C CA    . GLU B  1 379  ? -3.845  23.314  94.935  1.00 23.48 ? 377  GLU B CA    1 
ATOM   11541 C C     . GLU B  1 379  ? -4.287  23.971  93.632  1.00 21.93 ? 377  GLU B C     1 
ATOM   11542 O O     . GLU B  1 379  ? -3.780  23.640  92.554  1.00 24.18 ? 377  GLU B O     1 
ATOM   11543 C CB    . GLU B  1 379  ? -4.758  22.131  95.262  1.00 24.95 ? 377  GLU B CB    1 
ATOM   11544 C CG    . GLU B  1 379  ? -4.388  21.294  96.479  1.00 25.13 ? 377  GLU B CG    1 
ATOM   11545 C CD    . GLU B  1 379  ? -3.071  20.524  96.349  1.00 27.72 ? 377  GLU B CD    1 
ATOM   11546 O OE1   . GLU B  1 379  ? -2.460  20.509  95.254  1.00 27.36 ? 377  GLU B OE1   1 
ATOM   11547 O OE2   . GLU B  1 379  ? -2.655  19.914  97.363  1.00 23.02 ? 377  GLU B OE2   1 
ATOM   11548 N N     . ILE B  1 380  ? -5.239  24.900  93.710  1.00 23.26 ? 378  ILE B N     1 
ATOM   11549 C CA    . ILE B  1 380  ? -5.641  25.642  92.519  1.00 23.20 ? 378  ILE B CA    1 
ATOM   11550 C C     . ILE B  1 380  ? -4.458  26.417  91.960  1.00 20.68 ? 378  ILE B C     1 
ATOM   11551 O O     . ILE B  1 380  ? -4.174  26.380  90.754  1.00 21.49 ? 378  ILE B O     1 
ATOM   11552 C CB    . ILE B  1 380  ? -6.809  26.589  92.843  1.00 21.22 ? 378  ILE B CB    1 
ATOM   11553 C CG1   . ILE B  1 380  ? -7.975  25.817  93.467  1.00 21.20 ? 378  ILE B CG1   1 
ATOM   11554 C CG2   . ILE B  1 380  ? -7.242  27.311  91.572  1.00 22.57 ? 378  ILE B CG2   1 
ATOM   11555 C CD1   . ILE B  1 380  ? -8.588  24.754  92.543  1.00 20.04 ? 378  ILE B CD1   1 
ATOM   11556 N N     . LYS B  1 381  ? -3.783  27.171  92.826  1.00 19.67 ? 379  LYS B N     1 
ATOM   11557 C CA    . LYS B  1 381  ? -2.636  27.962  92.393  1.00 21.76 ? 379  LYS B CA    1 
ATOM   11558 C C     . LYS B  1 381  ? -1.549  27.081  91.784  1.00 20.36 ? 379  LYS B C     1 
ATOM   11559 O O     . LYS B  1 381  ? -1.038  27.371  90.697  1.00 19.65 ? 379  LYS B O     1 
ATOM   11560 C CB    . LYS B  1 381  ? -2.090  28.774  93.564  1.00 19.38 ? 379  LYS B CB    1 
ATOM   11561 C CG    . LYS B  1 381  ? -0.855  29.579  93.171  1.00 19.73 ? 379  LYS B CG    1 
ATOM   11562 C CD    . LYS B  1 381  ? -0.414  30.531  94.268  1.00 23.80 ? 379  LYS B CD    1 
ATOM   11563 C CE    . LYS B  1 381  ? 0.650   31.509  93.758  1.00 25.43 ? 379  LYS B CE    1 
ATOM   11564 N NZ    . LYS B  1 381  ? 1.275   32.255  94.904  1.00 23.72 ? 379  LYS B NZ    1 
ATOM   11565 N N     . ARG B  1 382  ? -1.221  25.964  92.441  1.00 17.70 ? 380  ARG B N     1 
ATOM   11566 C CA    . ARG B  1 382  ? -0.132  25.114  91.954  1.00 23.80 ? 380  ARG B CA    1 
ATOM   11567 C C     . ARG B  1 382  ? -0.438  24.539  90.570  1.00 23.34 ? 380  ARG B C     1 
ATOM   11568 O O     . ARG B  1 382  ? 0.429   24.519  89.680  1.00 22.99 ? 380  ARG B O     1 
ATOM   11569 C CB    . ARG B  1 382  ? 0.125   23.976  92.946  1.00 26.84 ? 380  ARG B CB    1 
ATOM   11570 C CG    . ARG B  1 382  ? 1.321   23.095  92.581  1.00 29.85 ? 380  ARG B CG    1 
ATOM   11571 C CD    . ARG B  1 382  ? 2.618   23.767  92.978  1.00 38.16 ? 380  ARG B CD    1 
ATOM   11572 N NE    . ARG B  1 382  ? 3.397   24.248  91.842  1.00 38.87 ? 380  ARG B NE    1 
ATOM   11573 C CZ    . ARG B  1 382  ? 4.286   25.234  91.915  1.00 42.01 ? 380  ARG B CZ    1 
ATOM   11574 N NH1   . ARG B  1 382  ? 4.469   25.920  93.035  1.00 40.66 ? 380  ARG B NH1   1 
ATOM   11575 N NH2   . ARG B  1 382  ? 5.014   25.539  90.840  1.00 38.64 ? 380  ARG B NH2   1 
ATOM   11576 N N     . ALA B  1 383  ? -1.655  24.027  90.383  1.00 22.45 ? 381  ALA B N     1 
ATOM   11577 C CA    . ALA B  1 383  ? -2.026  23.474  89.081  1.00 21.47 ? 381  ALA B CA    1 
ATOM   11578 C C     . ALA B  1 383  ? -1.962  24.529  87.987  1.00 22.42 ? 381  ALA B C     1 
ATOM   11579 O O     . ALA B  1 383  ? -1.552  24.232  86.851  1.00 20.48 ? 381  ALA B O     1 
ATOM   11580 C CB    . ALA B  1 383  ? -3.421  22.864  89.139  1.00 20.13 ? 381  ALA B CB    1 
ATOM   11581 N N     . GLN B  1 384  ? -2.375  25.764  88.301  1.00 20.45 ? 382  GLN B N     1 
ATOM   11582 C CA    . GLN B  1 384  ? -2.323  26.816  87.295  1.00 22.28 ? 382  GLN B CA    1 
ATOM   11583 C C     . GLN B  1 384  ? -0.888  27.198  86.983  1.00 21.53 ? 382  GLN B C     1 
ATOM   11584 O O     . GLN B  1 384  ? -0.535  27.383  85.811  1.00 23.36 ? 382  GLN B O     1 
ATOM   11585 C CB    . GLN B  1 384  ? -3.120  28.042  87.741  1.00 17.49 ? 382  GLN B CB    1 
ATOM   11586 C CG    . GLN B  1 384  ? -4.653  27.820  87.811  1.00 20.30 ? 382  GLN B CG    1 
ATOM   11587 C CD    . GLN B  1 384  ? -5.356  29.102  88.197  1.00 21.27 ? 382  GLN B CD    1 
ATOM   11588 O OE1   . GLN B  1 384  ? -4.742  29.986  88.776  1.00 22.30 ? 382  GLN B OE1   1 
ATOM   11589 N NE2   . GLN B  1 384  ? -6.642  29.209  87.887  1.00 18.84 ? 382  GLN B NE2   1 
ATOM   11590 N N     . LEU B  1 385  ? -0.043  27.308  88.014  1.00 19.83 ? 383  LEU B N     1 
ATOM   11591 C CA    . LEU B  1 385  ? 1.362   27.644  87.790  1.00 23.37 ? 383  LEU B CA    1 
ATOM   11592 C C     . LEU B  1 385  ? 2.044   26.608  86.915  1.00 23.70 ? 383  LEU B C     1 
ATOM   11593 O O     . LEU B  1 385  ? 2.858   26.946  86.045  1.00 20.78 ? 383  LEU B O     1 
ATOM   11594 C CB    . LEU B  1 385  ? 2.097   27.754  89.125  1.00 23.36 ? 383  LEU B CB    1 
ATOM   11595 C CG    . LEU B  1 385  ? 1.892   29.074  89.858  1.00 25.02 ? 383  LEU B CG    1 
ATOM   11596 C CD1   . LEU B  1 385  ? 2.656   29.054  91.182  1.00 26.40 ? 383  LEU B CD1   1 
ATOM   11597 C CD2   . LEU B  1 385  ? 2.378   30.223  88.974  1.00 26.64 ? 383  LEU B CD2   1 
ATOM   11598 N N     . ASP B  1 386  ? 1.719   25.339  87.129  1.00 22.42 ? 384  ASP B N     1 
ATOM   11599 C CA    . ASP B  1 386  ? 2.422   24.247  86.485  1.00 22.18 ? 384  ASP B CA    1 
ATOM   11600 C C     . ASP B  1 386  ? 1.824   23.877  85.139  1.00 23.37 ? 384  ASP B C     1 
ATOM   11601 O O     . ASP B  1 386  ? 2.347   22.975  84.472  1.00 25.14 ? 384  ASP B O     1 
ATOM   11602 C CB    . ASP B  1 386  ? 2.456   23.031  87.430  1.00 24.69 ? 384  ASP B CB    1 
ATOM   11603 C CG    . ASP B  1 386  ? 3.428   23.228  88.610  1.00 31.05 ? 384  ASP B CG    1 
ATOM   11604 O OD1   . ASP B  1 386  ? 4.139   24.261  88.649  1.00 33.61 ? 384  ASP B OD1   1 
ATOM   11605 O OD2   . ASP B  1 386  ? 3.484   22.348  89.500  1.00 31.91 ? 384  ASP B OD2   1 
ATOM   11606 N N     . GLY B  1 387  ? 0.749   24.546  84.723  1.00 24.00 ? 385  GLY B N     1 
ATOM   11607 C CA    . GLY B  1 387  ? 0.153   24.281  83.426  1.00 21.27 ? 385  GLY B CA    1 
ATOM   11608 C C     . GLY B  1 387  ? -0.375  22.869  83.275  1.00 28.06 ? 385  GLY B C     1 
ATOM   11609 O O     . GLY B  1 387  ? -0.295  22.290  82.184  1.00 26.18 ? 385  GLY B O     1 
ATOM   11610 N N     . LEU B  1 388  ? -0.906  22.287  84.345  1.00 23.11 ? 386  LEU B N     1 
ATOM   11611 C CA    . LEU B  1 388  ? -1.251  20.876  84.230  1.00 22.54 ? 386  LEU B CA    1 
ATOM   11612 C C     . LEU B  1 388  ? -2.663  20.701  83.662  1.00 24.60 ? 386  LEU B C     1 
ATOM   11613 O O     . LEU B  1 388  ? -3.419  21.657  83.476  1.00 26.23 ? 386  LEU B O     1 
ATOM   11614 C CB    . LEU B  1 388  ? -1.077  20.185  85.578  1.00 23.96 ? 386  LEU B CB    1 
ATOM   11615 C CG    . LEU B  1 388  ? 0.376   20.347  86.049  1.00 25.25 ? 386  LEU B CG    1 
ATOM   11616 C CD1   . LEU B  1 388  ? 0.596   19.789  87.435  1.00 24.84 ? 386  LEU B CD1   1 
ATOM   11617 C CD2   . LEU B  1 388  ? 1.363   19.714  85.049  1.00 26.75 ? 386  LEU B CD2   1 
ATOM   11618 N N     . ALA B  1 389  ? -3.008  19.448  83.361  1.00 22.92 ? 387  ALA B N     1 
ATOM   11619 C CA    . ALA B  1 389  ? -4.217  19.176  82.584  1.00 24.07 ? 387  ALA B CA    1 
ATOM   11620 C C     . ALA B  1 389  ? -5.480  19.654  83.293  1.00 27.09 ? 387  ALA B C     1 
ATOM   11621 O O     . ALA B  1 389  ? -6.396  20.199  82.667  1.00 27.79 ? 387  ALA B O     1 
ATOM   11622 C CB    . ALA B  1 389  ? -4.310  17.679  82.277  1.00 30.31 ? 387  ALA B CB    1 
ATOM   11623 N N     . ASP B  1 390  ? -5.553  19.470  84.597  1.00 27.70 ? 388  ASP B N     1 
ATOM   11624 C CA    . ASP B  1 390  ? -6.741  19.872  85.328  1.00 25.40 ? 388  ASP B CA    1 
ATOM   11625 C C     . ASP B  1 390  ? -6.315  19.990  86.780  1.00 22.06 ? 388  ASP B C     1 
ATOM   11626 O O     . ASP B  1 390  ? -5.150  19.775  87.110  1.00 21.64 ? 388  ASP B O     1 
ATOM   11627 C CB    . ASP B  1 390  ? -7.868  18.858  85.131  1.00 25.20 ? 388  ASP B CB    1 
ATOM   11628 C CG    . ASP B  1 390  ? -9.243  19.453  85.330  1.00 31.08 ? 388  ASP B CG    1 
ATOM   11629 O OD1   . ASP B  1 390  ? -9.433  20.237  86.280  1.00 28.15 ? 388  ASP B OD1   1 
ATOM   11630 O OD2   . ASP B  1 390  ? -10.146 19.117  84.528  1.00 34.08 ? 388  ASP B OD2   1 
ATOM   11631 N N     . PHE B  1 391  ? -7.282  20.272  87.651  1.00 22.00 ? 389  PHE B N     1 
ATOM   11632 C CA    . PHE B  1 391  ? -6.942  20.324  89.065  1.00 22.93 ? 389  PHE B CA    1 
ATOM   11633 C C     . PHE B  1 391  ? -7.002  18.930  89.678  1.00 20.68 ? 389  PHE B C     1 
ATOM   11634 O O     . PHE B  1 391  ? -7.717  18.058  89.187  1.00 22.63 ? 389  PHE B O     1 
ATOM   11635 C CB    . PHE B  1 391  ? -7.901  21.254  89.790  1.00 21.56 ? 389  PHE B CB    1 
ATOM   11636 C CG    . PHE B  1 391  ? -7.861  22.643  89.249  1.00 19.49 ? 389  PHE B CG    1 
ATOM   11637 C CD1   . PHE B  1 391  ? -6.821  23.494  89.593  1.00 20.91 ? 389  PHE B CD1   1 
ATOM   11638 C CD2   . PHE B  1 391  ? -8.827  23.084  88.377  1.00 21.58 ? 389  PHE B CD2   1 
ATOM   11639 C CE1   . PHE B  1 391  ? -6.757  24.773  89.081  1.00 22.73 ? 389  PHE B CE1   1 
ATOM   11640 C CE2   . PHE B  1 391  ? -8.776  24.369  87.869  1.00 22.28 ? 389  PHE B CE2   1 
ATOM   11641 C CZ    . PHE B  1 391  ? -7.736  25.207  88.213  1.00 22.11 ? 389  PHE B CZ    1 
ATOM   11642 N N     . PRO B  1 392  ? -6.250  18.690  90.750  1.00 22.16 ? 390  PRO B N     1 
ATOM   11643 C CA    . PRO B  1 392  ? -6.394  17.432  91.482  1.00 22.14 ? 390  PRO B CA    1 
ATOM   11644 C C     . PRO B  1 392  ? -7.494  17.485  92.527  1.00 27.48 ? 390  PRO B C     1 
ATOM   11645 O O     . PRO B  1 392  ? -7.681  16.509  93.253  1.00 23.55 ? 390  PRO B O     1 
ATOM   11646 C CB    . PRO B  1 392  ? -5.020  17.283  92.141  1.00 22.63 ? 390  PRO B CB    1 
ATOM   11647 C CG    . PRO B  1 392  ? -4.653  18.720  92.486  1.00 22.10 ? 390  PRO B CG    1 
ATOM   11648 C CD    . PRO B  1 392  ? -5.173  19.539  91.303  1.00 21.80 ? 390  PRO B CD    1 
ATOM   11649 N N     . VAL B  1 393  ? -8.208  18.605  92.620  1.00 24.11 ? 391  VAL B N     1 
ATOM   11650 C CA    . VAL B  1 393  ? -9.288  18.783  93.576  1.00 25.08 ? 391  VAL B CA    1 
ATOM   11651 C C     . VAL B  1 393  ? -10.477 19.353  92.815  1.00 23.89 ? 391  VAL B C     1 
ATOM   11652 O O     . VAL B  1 393  ? -10.338 19.871  91.705  1.00 25.34 ? 391  VAL B O     1 
ATOM   11653 C CB    . VAL B  1 393  ? -8.884  19.706  94.752  1.00 22.38 ? 391  VAL B CB    1 
ATOM   11654 C CG1   . VAL B  1 393  ? -7.703  19.107  95.547  1.00 23.10 ? 391  VAL B CG1   1 
ATOM   11655 C CG2   . VAL B  1 393  ? -8.531  21.096  94.238  1.00 22.28 ? 391  VAL B CG2   1 
ATOM   11656 N N     . PHE B  1 394  ? -11.658 19.221  93.412  1.00 22.73 ? 392  PHE B N     1 
ATOM   11657 C CA    . PHE B  1 394  ? -12.851 19.831  92.838  1.00 22.33 ? 392  PHE B CA    1 
ATOM   11658 C C     . PHE B  1 394  ? -12.751 21.350  92.925  1.00 23.24 ? 392  PHE B C     1 
ATOM   11659 O O     . PHE B  1 394  ? -11.977 21.900  93.712  1.00 25.85 ? 392  PHE B O     1 
ATOM   11660 C CB    . PHE B  1 394  ? -14.110 19.296  93.531  1.00 23.66 ? 392  PHE B CB    1 
ATOM   11661 C CG    . PHE B  1 394  ? -14.251 17.818  93.399  1.00 27.06 ? 392  PHE B CG    1 
ATOM   11662 C CD1   . PHE B  1 394  ? -14.510 17.248  92.157  1.00 23.66 ? 392  PHE B CD1   1 
ATOM   11663 C CD2   . PHE B  1 394  ? -14.040 16.987  94.484  1.00 23.95 ? 392  PHE B CD2   1 
ATOM   11664 C CE1   . PHE B  1 394  ? -14.595 15.875  92.024  1.00 25.02 ? 392  PHE B CE1   1 
ATOM   11665 C CE2   . PHE B  1 394  ? -14.103 15.616  94.350  1.00 26.26 ? 392  PHE B CE2   1 
ATOM   11666 C CZ    . PHE B  1 394  ? -14.386 15.062  93.113  1.00 24.57 ? 392  PHE B CZ    1 
ATOM   11667 N N     . THR B  1 395  ? -13.490 22.031  92.043  1.00 23.43 ? 393  THR B N     1 
ATOM   11668 C CA    . THR B  1 395  ? -13.506 23.485  92.012  1.00 25.57 ? 393  THR B CA    1 
ATOM   11669 C C     . THR B  1 395  ? -14.794 24.101  92.543  1.00 26.68 ? 393  THR B C     1 
ATOM   11670 O O     . THR B  1 395  ? -14.830 25.320  92.738  1.00 28.22 ? 393  THR B O     1 
ATOM   11671 C CB    . THR B  1 395  ? -13.255 23.998  90.582  1.00 24.50 ? 393  THR B CB    1 
ATOM   11672 O OG1   . THR B  1 395  ? -14.312 23.569  89.717  1.00 24.30 ? 393  THR B OG1   1 
ATOM   11673 C CG2   . THR B  1 395  ? -11.934 23.462  90.078  1.00 27.14 ? 393  THR B CG2   1 
ATOM   11674 N N     . ARG B  1 396  ? -15.849 23.313  92.760  1.00 26.83 ? 394  ARG B N     1 
ATOM   11675 C CA    . ARG B  1 396  ? -17.066 23.774  93.428  1.00 28.01 ? 394  ARG B CA    1 
ATOM   11676 C C     . ARG B  1 396  ? -17.176 23.128  94.799  1.00 29.28 ? 394  ARG B C     1 
ATOM   11677 O O     . ARG B  1 396  ? -17.050 21.906  94.926  1.00 29.28 ? 394  ARG B O     1 
ATOM   11678 C CB    . ARG B  1 396  ? -18.325 23.442  92.621  1.00 25.98 ? 394  ARG B CB    1 
ATOM   11679 C CG    . ARG B  1 396  ? -18.343 24.086  91.261  1.00 29.24 ? 394  ARG B CG    1 
ATOM   11680 C CD    . ARG B  1 396  ? -19.717 23.995  90.588  1.00 29.26 ? 394  ARG B CD    1 
ATOM   11681 N NE    . ARG B  1 396  ? -19.613 24.554  89.247  1.00 33.52 ? 394  ARG B NE    1 
ATOM   11682 C CZ    . ARG B  1 396  ? -20.565 25.231  88.618  1.00 36.96 ? 394  ARG B CZ    1 
ATOM   11683 N NH1   . ARG B  1 396  ? -21.759 25.420  89.166  1.00 37.72 ? 394  ARG B NH1   1 
ATOM   11684 N NH2   . ARG B  1 396  ? -20.308 25.741  87.412  1.00 33.79 ? 394  ARG B NH2   1 
ATOM   11685 N N     . LYS B  1 397  ? -17.463 23.942  95.815  1.00 29.02 ? 395  LYS B N     1 
ATOM   11686 C CA    . LYS B  1 397  ? -17.559 23.406  97.168  1.00 28.54 ? 395  LYS B CA    1 
ATOM   11687 C C     . LYS B  1 397  ? -18.625 22.313  97.276  1.00 28.52 ? 395  LYS B C     1 
ATOM   11688 O O     . LYS B  1 397  ? -18.460 21.351  98.036  1.00 31.03 ? 395  LYS B O     1 
ATOM   11689 C CB    . LYS B  1 397  ? -17.842 24.546  98.147  1.00 32.67 ? 395  LYS B CB    1 
ATOM   11690 C CG    . LYS B  1 397  ? -17.494 24.229  99.590  1.00 32.09 ? 395  LYS B CG    1 
ATOM   11691 C CD    . LYS B  1 397  ? -18.652 23.592  100.314 1.00 35.83 ? 395  LYS B CD    1 
ATOM   11692 C CE    . LYS B  1 397  ? -18.368 23.454  101.804 1.00 36.84 ? 395  LYS B CE    1 
ATOM   11693 N NZ    . LYS B  1 397  ? -19.573 22.950  102.522 1.00 35.84 ? 395  LYS B NZ    1 
ATOM   11694 N N     . ILE B  1 398  ? -19.704 22.416  96.504  1.00 31.11 ? 396  ILE B N     1 
ATOM   11695 C CA    . ILE B  1 398  ? -20.750 21.410  96.589  1.00 29.94 ? 396  ILE B CA    1 
ATOM   11696 C C     . ILE B  1 398  ? -20.274 20.063  96.038  1.00 29.87 ? 396  ILE B C     1 
ATOM   11697 O O     . ILE B  1 398  ? -20.729 19.003  96.488  1.00 29.55 ? 396  ILE B O     1 
ATOM   11698 C CB    . ILE B  1 398  ? -22.006 21.936  95.872  1.00 34.11 ? 396  ILE B CB    1 
ATOM   11699 C CG1   . ILE B  1 398  ? -23.234 21.173  96.308  1.00 38.23 ? 396  ILE B CG1   1 
ATOM   11700 C CG2   . ILE B  1 398  ? -21.844 21.906  94.346  1.00 31.94 ? 396  ILE B CG2   1 
ATOM   11701 C CD1   . ILE B  1 398  ? -24.486 21.844  95.851  1.00 41.97 ? 396  ILE B CD1   1 
ATOM   11702 N N     . HIS B  1 399  ? -19.348 20.073  95.080  1.00 29.35 ? 397  HIS B N     1 
ATOM   11703 C CA    . HIS B  1 399  ? -18.769 18.824  94.585  1.00 30.01 ? 397  HIS B CA    1 
ATOM   11704 C C     . HIS B  1 399  ? -18.011 18.087  95.681  1.00 28.37 ? 397  HIS B C     1 
ATOM   11705 O O     . HIS B  1 399  ? -18.104 16.860  95.793  1.00 29.23 ? 397  HIS B O     1 
ATOM   11706 C CB    . HIS B  1 399  ? -17.844 19.121  93.402  1.00 30.03 ? 397  HIS B CB    1 
ATOM   11707 C CG    . HIS B  1 399  ? -18.573 19.609  92.185  1.00 29.56 ? 397  HIS B CG    1 
ATOM   11708 N ND1   . HIS B  1 399  ? -17.931 20.164  91.097  1.00 26.48 ? 397  HIS B ND1   1 
ATOM   11709 C CD2   . HIS B  1 399  ? -19.895 19.619  91.888  1.00 30.97 ? 397  HIS B CD2   1 
ATOM   11710 C CE1   . HIS B  1 399  ? -18.827 20.499  90.185  1.00 29.04 ? 397  HIS B CE1   1 
ATOM   11711 N NE2   . HIS B  1 399  ? -20.026 20.178  90.639  1.00 28.08 ? 397  HIS B NE2   1 
ATOM   11712 N N     . THR B  1 400  ? -17.232 18.817  96.484  1.00 26.98 ? 398  THR B N     1 
ATOM   11713 C CA    . THR B  1 400  ? -16.540 18.190  97.603  1.00 28.81 ? 398  THR B CA    1 
ATOM   11714 C C     . THR B  1 400  ? -17.539 17.597  98.583  1.00 29.00 ? 398  THR B C     1 
ATOM   11715 O O     . THR B  1 400  ? -17.312 16.512  99.132  1.00 30.20 ? 398  THR B O     1 
ATOM   11716 C CB    . THR B  1 400  ? -15.624 19.205  98.296  1.00 27.32 ? 398  THR B CB    1 
ATOM   11717 O OG1   . THR B  1 400  ? -14.517 19.526  97.434  1.00 25.93 ? 398  THR B OG1   1 
ATOM   11718 C CG2   . THR B  1 400  ? -15.082 18.646  99.599  1.00 27.41 ? 398  THR B CG2   1 
ATOM   11719 N N     . ASP B  1 401  ? -18.674 18.271  98.789  1.00 28.15 ? 399  ASP B N     1 
ATOM   11720 C CA    . ASP B  1 401  ? -19.658 17.746  99.735  1.00 30.49 ? 399  ASP B CA    1 
ATOM   11721 C C     . ASP B  1 401  ? -20.267 16.445  99.229  1.00 30.84 ? 399  ASP B C     1 
ATOM   11722 O O     . ASP B  1 401  ? -20.483 15.514  100.005 1.00 31.02 ? 399  ASP B O     1 
ATOM   11723 C CB    . ASP B  1 401  ? -20.752 18.782  100.007 1.00 32.86 ? 399  ASP B CB    1 
ATOM   11724 C CG    . ASP B  1 401  ? -20.257 19.966  100.838 1.00 37.31 ? 399  ASP B CG    1 
ATOM   11725 O OD1   . ASP B  1 401  ? -19.264 19.813  101.598 1.00 34.45 ? 399  ASP B OD1   1 
ATOM   11726 O OD2   . ASP B  1 401  ? -20.868 21.055  100.733 1.00 34.26 ? 399  ASP B OD2   1 
ATOM   11727 N N     . VAL B  1 402  ? -20.522 16.351  97.923  1.00 32.04 ? 400  VAL B N     1 
ATOM   11728 C CA    . VAL B  1 402  ? -21.039 15.110  97.358  1.00 31.28 ? 400  VAL B CA    1 
ATOM   11729 C C     . VAL B  1 402  ? -19.980 14.016  97.416  1.00 33.90 ? 400  VAL B C     1 
ATOM   11730 O O     . VAL B  1 402  ? -20.276 12.862  97.757  1.00 34.19 ? 400  VAL B O     1 
ATOM   11731 C CB    . VAL B  1 402  ? -21.527 15.357  95.919  1.00 32.75 ? 400  VAL B CB    1 
ATOM   11732 C CG1   . VAL B  1 402  ? -22.006 14.062  95.301  1.00 34.78 ? 400  VAL B CG1   1 
ATOM   11733 C CG2   . VAL B  1 402  ? -22.616 16.423  95.913  1.00 35.51 ? 400  VAL B CG2   1 
ATOM   11734 N N     . SER B  1 403  ? -18.728 14.367  97.098  1.00 28.68 ? 401  SER B N     1 
ATOM   11735 C CA    . SER B  1 403  ? -17.624 13.417  97.196  1.00 31.81 ? 401  SER B CA    1 
ATOM   11736 C C     . SER B  1 403  ? -17.525 12.836  98.602  1.00 32.15 ? 401  SER B C     1 
ATOM   11737 O O     . SER B  1 403  ? -17.427 11.619  98.780  1.00 32.03 ? 401  SER B O     1 
ATOM   11738 C CB    . SER B  1 403  ? -16.312 14.111  96.809  1.00 27.66 ? 401  SER B CB    1 
ATOM   11739 O OG    . SER B  1 403  ? -15.192 13.247  96.933  1.00 28.56 ? 401  SER B OG    1 
ATOM   11740 N N     . TYR B  1 404  ? -17.555 13.702  99.611  1.00 30.31 ? 402  TYR B N     1 
ATOM   11741 C CA    . TYR B  1 404  ? -17.509 13.250  100.998 1.00 31.18 ? 402  TYR B CA    1 
ATOM   11742 C C     . TYR B  1 404  ? -18.615 12.246  101.290 1.00 33.26 ? 402  TYR B C     1 
ATOM   11743 O O     . TYR B  1 404  ? -18.371 11.177  101.867 1.00 36.23 ? 402  TYR B O     1 
ATOM   11744 C CB    . TYR B  1 404  ? -17.621 14.458  101.917 1.00 33.29 ? 402  TYR B CB    1 
ATOM   11745 C CG    . TYR B  1 404  ? -17.220 14.188  103.343 1.00 32.80 ? 402  TYR B CG    1 
ATOM   11746 C CD1   . TYR B  1 404  ? -18.107 13.593  104.227 1.00 34.18 ? 402  TYR B CD1   1 
ATOM   11747 C CD2   . TYR B  1 404  ? -15.957 14.538  103.807 1.00 30.32 ? 402  TYR B CD2   1 
ATOM   11748 C CE1   . TYR B  1 404  ? -17.754 13.351  105.529 1.00 34.22 ? 402  TYR B CE1   1 
ATOM   11749 C CE2   . TYR B  1 404  ? -15.591 14.298  105.118 1.00 29.95 ? 402  TYR B CE2   1 
ATOM   11750 C CZ    . TYR B  1 404  ? -16.491 13.706  105.972 1.00 32.37 ? 402  TYR B CZ    1 
ATOM   11751 O OH    . TYR B  1 404  ? -16.145 13.459  107.287 1.00 34.37 ? 402  TYR B OH    1 
ATOM   11752 N N     . ILE B  1 405  ? -19.846 12.573  100.902 1.00 32.51 ? 403  ILE B N     1 
ATOM   11753 C CA    . ILE B  1 405  ? -20.967 11.697  101.227 1.00 35.10 ? 403  ILE B CA    1 
ATOM   11754 C C     . ILE B  1 405  ? -20.833 10.368  100.493 1.00 34.25 ? 403  ILE B C     1 
ATOM   11755 O O     . ILE B  1 405  ? -21.073 9.299   101.069 1.00 36.24 ? 403  ILE B O     1 
ATOM   11756 C CB    . ILE B  1 405  ? -22.296 12.418  100.928 1.00 36.58 ? 403  ILE B CB    1 
ATOM   11757 C CG1   . ILE B  1 405  ? -22.421 13.637  101.847 1.00 42.43 ? 403  ILE B CG1   1 
ATOM   11758 C CG2   . ILE B  1 405  ? -23.474 11.499  101.129 1.00 38.03 ? 403  ILE B CG2   1 
ATOM   11759 C CD1   . ILE B  1 405  ? -23.705 14.406  101.707 1.00 45.81 ? 403  ILE B CD1   1 
ATOM   11760 N N     . ALA B  1 406  ? -20.402 10.408  99.226  1.00 34.43 ? 404  ALA B N     1 
ATOM   11761 C CA    . ALA B  1 406  ? -20.199 9.178   98.462  1.00 35.82 ? 404  ALA B CA    1 
ATOM   11762 C C     . ALA B  1 406  ? -19.093 8.321   99.067  1.00 37.83 ? 404  ALA B C     1 
ATOM   11763 O O     . ALA B  1 406  ? -19.209 7.091   99.127  1.00 37.11 ? 404  ALA B O     1 
ATOM   11764 C CB    . ALA B  1 406  ? -19.870 9.512   97.004  1.00 36.74 ? 404  ALA B CB    1 
ATOM   11765 N N     . CYS B  1 407  ? -17.999 8.949   99.501  1.00 35.42 ? 405  CYS B N     1 
ATOM   11766 C CA    . CYS B  1 407  ? -16.936 8.183   100.128 1.00 37.35 ? 405  CYS B CA    1 
ATOM   11767 C C     . CYS B  1 407  ? -17.359 7.674   101.501 1.00 36.21 ? 405  CYS B C     1 
ATOM   11768 O O     . CYS B  1 407  ? -16.943 6.585   101.913 1.00 36.37 ? 405  CYS B O     1 
ATOM   11769 C CB    . CYS B  1 407  ? -15.676 9.038   100.197 1.00 34.67 ? 405  CYS B CB    1 
ATOM   11770 S SG    . CYS B  1 407  ? -15.048 9.400   98.513  1.00 38.26 ? 405  CYS B SG    1 
ATOM   11771 N N     . ALA B  1 408  ? -18.202 8.428   102.208 1.00 36.19 ? 406  ALA B N     1 
ATOM   11772 C CA    . ALA B  1 408  ? -18.762 7.927   103.459 1.00 38.43 ? 406  ALA B CA    1 
ATOM   11773 C C     . ALA B  1 408  ? -19.587 6.666   103.224 1.00 40.20 ? 406  ALA B C     1 
ATOM   11774 O O     . ALA B  1 408  ? -19.552 5.733   104.032 1.00 42.63 ? 406  ALA B O     1 
ATOM   11775 C CB    . ALA B  1 408  ? -19.607 9.011   104.127 1.00 37.36 ? 406  ALA B CB    1 
ATOM   11776 N N     . ALA B  1 409  ? -20.319 6.605   102.110 1.00 41.59 ? 407  ALA B N     1 
ATOM   11777 C CA    . ALA B  1 409  ? -21.084 5.398   101.826 1.00 41.79 ? 407  ALA B CA    1 
ATOM   11778 C C     . ALA B  1 409  ? -20.163 4.207   101.586 1.00 38.93 ? 407  ALA B C     1 
ATOM   11779 O O     . ALA B  1 409  ? -20.438 3.098   102.058 1.00 42.06 ? 407  ALA B O     1 
ATOM   11780 C CB    . ALA B  1 409  ? -22.012 5.627   100.630 1.00 41.62 ? 407  ALA B CB    1 
ATOM   11781 N N     . LYS B  1 410  ? -19.055 4.427   100.876 1.00 40.58 ? 408  LYS B N     1 
ATOM   11782 C CA    . LYS B  1 410  ? -18.121 3.343   100.598 1.00 38.63 ? 408  LYS B CA    1 
ATOM   11783 C C     . LYS B  1 410  ? -17.483 2.819   101.879 1.00 40.75 ? 408  LYS B C     1 
ATOM   11784 O O     . LYS B  1 410  ? -17.336 1.605   102.055 1.00 44.42 ? 408  LYS B O     1 
ATOM   11785 C CB    . LYS B  1 410  ? -17.053 3.829   99.622  1.00 35.70 ? 408  LYS B CB    1 
ATOM   11786 C CG    . LYS B  1 410  ? -16.000 2.807   99.290  1.00 38.32 ? 408  LYS B CG    1 
ATOM   11787 C CD    . LYS B  1 410  ? -14.864 3.436   98.493  1.00 39.67 ? 408  LYS B CD    1 
ATOM   11788 C CE    . LYS B  1 410  ? -15.301 3.878   97.105  1.00 41.93 ? 408  LYS B CE    1 
ATOM   11789 N NZ    . LYS B  1 410  ? -15.537 2.706   96.208  1.00 40.30 ? 408  LYS B NZ    1 
ATOM   11790 N N     . LEU B  1 411  ? -17.115 3.721   102.794 1.00 41.66 ? 409  LEU B N     1 
ATOM   11791 C CA    . LEU B  1 411  ? -16.466 3.309   104.039 1.00 40.84 ? 409  LEU B CA    1 
ATOM   11792 C C     . LEU B  1 411  ? -17.428 2.559   104.945 1.00 42.97 ? 409  LEU B C     1 
ATOM   11793 O O     . LEU B  1 411  ? -17.055 1.556   105.564 1.00 43.80 ? 409  LEU B O     1 
ATOM   11794 C CB    . LEU B  1 411  ? -15.900 4.530   104.771 1.00 42.26 ? 409  LEU B CB    1 
ATOM   11795 C CG    . LEU B  1 411  ? -14.578 5.100   104.250 1.00 41.90 ? 409  LEU B CG    1 
ATOM   11796 C CD1   . LEU B  1 411  ? -14.367 6.508   104.768 1.00 41.53 ? 409  LEU B CD1   1 
ATOM   11797 C CD2   . LEU B  1 411  ? -13.412 4.212   104.637 1.00 37.19 ? 409  LEU B CD2   1 
ATOM   11798 N N     . LEU B  1 412  ? -18.667 3.041   105.050 1.00 43.89 ? 410  LEU B N     1 
ATOM   11799 C CA    . LEU B  1 412  ? -19.648 2.389   105.904 1.00 44.19 ? 410  LEU B CA    1 
ATOM   11800 C C     . LEU B  1 412  ? -19.941 0.961   105.466 1.00 45.10 ? 410  LEU B C     1 
ATOM   11801 O O     . LEU B  1 412  ? -20.373 0.148   106.288 1.00 47.58 ? 410  LEU B O     1 
ATOM   11802 C CB    . LEU B  1 412  ? -20.927 3.224   105.938 1.00 41.54 ? 410  LEU B CB    1 
ATOM   11803 C CG    . LEU B  1 412  ? -20.754 4.514   106.746 1.00 43.89 ? 410  LEU B CG    1 
ATOM   11804 C CD1   . LEU B  1 412  ? -21.945 5.439   106.603 1.00 44.93 ? 410  LEU B CD1   1 
ATOM   11805 C CD2   . LEU B  1 412  ? -20.531 4.164   108.211 1.00 49.49 ? 410  LEU B CD2   1 
ATOM   11806 N N     . ALA B  1 413  ? -19.709 0.626   104.201 1.00 44.49 ? 411  ALA B N     1 
ATOM   11807 C CA    . ALA B  1 413  ? -19.928 -0.741  103.756 1.00 47.28 ? 411  ALA B CA    1 
ATOM   11808 C C     . ALA B  1 413  ? -18.721 -1.634  103.997 1.00 50.39 ? 411  ALA B C     1 
ATOM   11809 O O     . ALA B  1 413  ? -18.761 -2.811  103.627 1.00 50.20 ? 411  ALA B O     1 
ATOM   11810 C CB    . ALA B  1 413  ? -20.299 -0.761  102.271 1.00 44.89 ? 411  ALA B CB    1 
ATOM   11811 N N     . ALA B  1 414  ? -17.661 -1.112  104.624 1.00 41.27 ? 412  ALA B N     1 
ATOM   11812 C CA    . ALA B  1 414  ? -16.425 -1.861  104.828 1.00 46.65 ? 412  ALA B CA    1 
ATOM   11813 C C     . ALA B  1 414  ? -15.947 -1.796  106.276 1.00 47.12 ? 412  ALA B C     1 
ATOM   11814 O O     . ALA B  1 414  ? -14.759 -2.010  106.541 1.00 46.31 ? 412  ALA B O     1 
ATOM   11815 C CB    . ALA B  1 414  ? -15.325 -1.355  103.888 1.00 42.64 ? 412  ALA B CB    1 
ATOM   11816 N N     . THR B  1 415  ? -16.852 -1.520  107.219 1.00 47.22 ? 413  THR B N     1 
ATOM   11817 C CA    . THR B  1 415  ? -16.485 -1.376  108.624 1.00 48.32 ? 413  THR B CA    1 
ATOM   11818 C C     . THR B  1 415  ? -15.868 -2.635  109.219 1.00 50.36 ? 413  THR B C     1 
ATOM   11819 O O     . THR B  1 415  ? -15.325 -2.570  110.330 1.00 48.70 ? 413  THR B O     1 
ATOM   11820 C CB    . THR B  1 415  ? -17.706 -0.974  109.443 1.00 45.75 ? 413  THR B CB    1 
ATOM   11821 O OG1   . THR B  1 415  ? -18.706 -1.989  109.325 1.00 53.33 ? 413  THR B OG1   1 
ATOM   11822 C CG2   . THR B  1 415  ? -18.267 0.334   108.927 1.00 42.60 ? 413  THR B CG2   1 
ATOM   11823 N N     . ASP B  1 416  ? -15.933 -3.771  108.521 1.00 49.03 ? 414  ASP B N     1 
ATOM   11824 C CA    . ASP B  1 416  ? -15.215 -4.952  108.981 1.00 44.57 ? 414  ASP B CA    1 
ATOM   11825 C C     . ASP B  1 416  ? -13.714 -4.800  108.778 1.00 51.27 ? 414  ASP B C     1 
ATOM   11826 O O     . ASP B  1 416  ? -12.923 -5.275  109.603 1.00 55.75 ? 414  ASP B O     1 
ATOM   11827 C CB    . ASP B  1 416  ? -15.725 -6.192  108.248 1.00 56.89 ? 414  ASP B CB    1 
ATOM   11828 N N     . VAL B  1 417  ? -13.309 -4.126  107.701 1.00 42.91 ? 415  VAL B N     1 
ATOM   11829 C CA    . VAL B  1 417  ? -11.900 -3.978  107.364 1.00 47.16 ? 415  VAL B CA    1 
ATOM   11830 C C     . VAL B  1 417  ? -11.332 -2.613  107.744 1.00 45.44 ? 415  VAL B C     1 
ATOM   11831 O O     . VAL B  1 417  ? -10.106 -2.484  107.866 1.00 49.76 ? 415  VAL B O     1 
ATOM   11832 C CB    . VAL B  1 417  ? -11.674 -4.236  105.857 1.00 44.92 ? 415  VAL B CB    1 
ATOM   11833 N N     . VAL B  1 418  ? -12.172 -1.589  107.918 1.00 44.17 ? 416  VAL B N     1 
ATOM   11834 C CA    . VAL B  1 418  ? -11.691 -0.249  108.236 1.00 42.67 ? 416  VAL B CA    1 
ATOM   11835 C C     . VAL B  1 418  ? -12.567 0.375   109.311 1.00 42.25 ? 416  VAL B C     1 
ATOM   11836 O O     . VAL B  1 418  ? -13.738 0.029   109.476 1.00 43.45 ? 416  VAL B O     1 
ATOM   11837 C CB    . VAL B  1 418  ? -11.648 0.696   107.007 1.00 40.45 ? 416  VAL B CB    1 
ATOM   11838 C CG1   . VAL B  1 418  ? -10.713 0.155   105.932 1.00 37.89 ? 416  VAL B CG1   1 
ATOM   11839 C CG2   . VAL B  1 418  ? -13.059 0.945   106.465 1.00 40.37 ? 416  VAL B CG2   1 
ATOM   11840 N N     . PHE B  1 419  ? -11.981 1.331   110.033 1.00 39.12 ? 417  PHE B N     1 
ATOM   11841 C CA    . PHE B  1 419  ? -12.693 2.101   111.048 1.00 40.64 ? 417  PHE B CA    1 
ATOM   11842 C C     . PHE B  1 419  ? -12.905 3.519   110.534 1.00 40.10 ? 417  PHE B C     1 
ATOM   11843 O O     . PHE B  1 419  ? -11.969 4.340   110.565 1.00 36.79 ? 417  PHE B O     1 
ATOM   11844 C CB    . PHE B  1 419  ? -11.918 2.108   112.372 1.00 37.66 ? 417  PHE B CB    1 
ATOM   11845 C CG    . PHE B  1 419  ? -12.570 2.918   113.458 1.00 39.15 ? 417  PHE B CG    1 
ATOM   11846 C CD1   . PHE B  1 419  ? -13.800 2.548   113.978 1.00 39.41 ? 417  PHE B CD1   1 
ATOM   11847 C CD2   . PHE B  1 419  ? -11.941 4.043   113.974 1.00 37.22 ? 417  PHE B CD2   1 
ATOM   11848 C CE1   . PHE B  1 419  ? -14.407 3.294   114.973 1.00 39.81 ? 417  PHE B CE1   1 
ATOM   11849 C CE2   . PHE B  1 419  ? -12.533 4.788   114.976 1.00 37.00 ? 417  PHE B CE2   1 
ATOM   11850 C CZ    . PHE B  1 419  ? -13.777 4.423   115.473 1.00 37.53 ? 417  PHE B CZ    1 
ATOM   11851 N N     . PRO B  1 420  ? -14.096 3.857   110.036 1.00 37.76 ? 418  PRO B N     1 
ATOM   11852 C CA    . PRO B  1 420  ? -14.300 5.185   109.439 1.00 36.57 ? 418  PRO B CA    1 
ATOM   11853 C C     . PRO B  1 420  ? -14.416 6.265   110.506 1.00 39.02 ? 418  PRO B C     1 
ATOM   11854 O O     . PRO B  1 420  ? -15.151 6.122   111.488 1.00 36.84 ? 418  PRO B O     1 
ATOM   11855 C CB    . PRO B  1 420  ? -15.613 5.030   108.656 1.00 35.93 ? 418  PRO B CB    1 
ATOM   11856 C CG    . PRO B  1 420  ? -15.788 3.571   108.475 1.00 37.23 ? 418  PRO B CG    1 
ATOM   11857 C CD    . PRO B  1 420  ? -15.233 2.969   109.757 1.00 39.95 ? 418  PRO B CD    1 
ATOM   11858 N N     . GLN B  1 421  ? -13.694 7.362   110.284 1.00 35.27 ? 419  GLN B N     1 
ATOM   11859 C CA    . GLN B  1 421  ? -13.658 8.518   111.174 1.00 37.31 ? 419  GLN B CA    1 
ATOM   11860 C C     . GLN B  1 421  ? -14.058 9.730   110.345 1.00 36.15 ? 419  GLN B C     1 
ATOM   11861 O O     . GLN B  1 421  ? -13.297 10.164  109.471 1.00 33.03 ? 419  GLN B O     1 
ATOM   11862 C CB    . GLN B  1 421  ? -12.259 8.687   111.779 1.00 32.58 ? 419  GLN B CB    1 
ATOM   11863 C CG    . GLN B  1 421  ? -11.715 7.407   112.417 1.00 34.01 ? 419  GLN B CG    1 
ATOM   11864 C CD    . GLN B  1 421  ? -10.220 7.448   112.682 1.00 35.97 ? 419  GLN B CD    1 
ATOM   11865 O OE1   . GLN B  1 421  ? -9.408  7.470   111.752 1.00 32.11 ? 419  GLN B OE1   1 
ATOM   11866 N NE2   . GLN B  1 421  ? -9.847  7.424   113.962 1.00 32.93 ? 419  GLN B NE2   1 
ATOM   11867 N N     . PHE B  1 422  ? -15.243 10.279  110.601 1.00 38.06 ? 420  PHE B N     1 
ATOM   11868 C CA    . PHE B  1 422  ? -15.786 11.342  109.751 1.00 34.98 ? 420  PHE B CA    1 
ATOM   11869 C C     . PHE B  1 422  ? -15.513 12.694  110.401 1.00 37.42 ? 420  PHE B C     1 
ATOM   11870 O O     . PHE B  1 422  ? -16.221 13.112  111.320 1.00 36.36 ? 420  PHE B O     1 
ATOM   11871 C CB    . PHE B  1 422  ? -17.273 11.129  109.490 1.00 36.36 ? 420  PHE B CB    1 
ATOM   11872 C CG    . PHE B  1 422  ? -17.588 9.803   108.888 1.00 37.77 ? 420  PHE B CG    1 
ATOM   11873 C CD1   . PHE B  1 422  ? -17.198 9.506   107.596 1.00 37.16 ? 420  PHE B CD1   1 
ATOM   11874 C CD2   . PHE B  1 422  ? -18.286 8.850   109.612 1.00 34.92 ? 420  PHE B CD2   1 
ATOM   11875 C CE1   . PHE B  1 422  ? -17.494 8.283   107.036 1.00 38.07 ? 420  PHE B CE1   1 
ATOM   11876 C CE2   . PHE B  1 422  ? -18.588 7.624   109.056 1.00 38.64 ? 420  PHE B CE2   1 
ATOM   11877 C CZ    . PHE B  1 422  ? -18.186 7.343   107.762 1.00 41.22 ? 420  PHE B CZ    1 
ATOM   11878 N N     . ALA B  1 423  ? -14.486 13.384  109.908 1.00 31.59 ? 421  ALA B N     1 
ATOM   11879 C CA    . ALA B  1 423  ? -14.108 14.691  110.423 1.00 34.75 ? 421  ALA B CA    1 
ATOM   11880 C C     . ALA B  1 423  ? -14.866 15.756  109.648 1.00 35.26 ? 421  ALA B C     1 
ATOM   11881 O O     . ALA B  1 423  ? -14.618 15.961  108.454 1.00 35.58 ? 421  ALA B O     1 
ATOM   11882 C CB    . ALA B  1 423  ? -12.600 14.903  110.305 1.00 29.98 ? 421  ALA B CB    1 
ATOM   11883 N N     . THR B  1 424  ? -15.768 16.453  110.330 1.00 36.01 ? 422  THR B N     1 
ATOM   11884 C CA    . THR B  1 424  ? -16.463 17.564  109.705 1.00 34.12 ? 422  THR B CA    1 
ATOM   11885 C C     . THR B  1 424  ? -17.125 18.413  110.778 1.00 35.04 ? 422  THR B C     1 
ATOM   11886 O O     . THR B  1 424  ? -17.544 17.908  111.825 1.00 35.67 ? 422  THR B O     1 
ATOM   11887 C CB    . THR B  1 424  ? -17.510 17.084  108.691 1.00 37.65 ? 422  THR B CB    1 
ATOM   11888 O OG1   . THR B  1 424  ? -18.124 18.219  108.072 1.00 34.56 ? 422  THR B OG1   1 
ATOM   11889 C CG2   . THR B  1 424  ? -18.588 16.229  109.384 1.00 35.93 ? 422  THR B CG2   1 
ATOM   11890 N N     . HIS B  1 425  ? -17.218 19.709  110.494 1.00 35.40 ? 423  HIS B N     1 
ATOM   11891 C CA    . HIS B  1 425  ? -17.944 20.665  111.318 1.00 36.33 ? 423  HIS B CA    1 
ATOM   11892 C C     . HIS B  1 425  ? -19.282 21.053  110.706 1.00 39.75 ? 423  HIS B C     1 
ATOM   11893 O O     . HIS B  1 425  ? -19.954 21.953  111.220 1.00 38.60 ? 423  HIS B O     1 
ATOM   11894 C CB    . HIS B  1 425  ? -17.091 21.913  111.531 1.00 32.79 ? 423  HIS B CB    1 
ATOM   11895 C CG    . HIS B  1 425  ? -15.822 21.646  112.272 1.00 38.47 ? 423  HIS B CG    1 
ATOM   11896 N ND1   . HIS B  1 425  ? -14.633 22.280  111.975 1.00 39.91 ? 423  HIS B ND1   1 
ATOM   11897 C CD2   . HIS B  1 425  ? -15.560 20.818  113.312 1.00 37.88 ? 423  HIS B CD2   1 
ATOM   11898 C CE1   . HIS B  1 425  ? -13.693 21.848  112.796 1.00 37.65 ? 423  HIS B CE1   1 
ATOM   11899 N NE2   . HIS B  1 425  ? -14.231 20.965  113.620 1.00 34.78 ? 423  HIS B NE2   1 
ATOM   11900 N N     . ASN B  1 426  ? -19.670 20.405  109.616 1.00 35.10 ? 424  ASN B N     1 
ATOM   11901 C CA    . ASN B  1 426  ? -20.850 20.771  108.847 1.00 39.46 ? 424  ASN B CA    1 
ATOM   11902 C C     . ASN B  1 426  ? -22.008 19.883  109.299 1.00 38.47 ? 424  ASN B C     1 
ATOM   11903 O O     . ASN B  1 426  ? -21.982 18.663  109.101 1.00 36.46 ? 424  ASN B O     1 
ATOM   11904 C CB    . ASN B  1 426  ? -20.550 20.637  107.353 1.00 38.79 ? 424  ASN B CB    1 
ATOM   11905 C CG    . ASN B  1 426  ? -21.643 21.209  106.477 1.00 41.54 ? 424  ASN B CG    1 
ATOM   11906 O OD1   . ASN B  1 426  ? -22.829 21.015  106.746 1.00 43.84 ? 424  ASN B OD1   1 
ATOM   11907 N ND2   . ASN B  1 426  ? -21.249 21.918  105.417 1.00 37.25 ? 424  ASN B ND2   1 
ATOM   11908 N N     . ALA B  1 427  ? -23.021 20.503  109.914 1.00 43.85 ? 425  ALA B N     1 
ATOM   11909 C CA    . ALA B  1 427  ? -24.151 19.749  110.451 1.00 44.91 ? 425  ALA B CA    1 
ATOM   11910 C C     . ALA B  1 427  ? -24.923 19.027  109.357 1.00 40.45 ? 425  ALA B C     1 
ATOM   11911 O O     . ALA B  1 427  ? -25.450 17.931  109.589 1.00 40.73 ? 425  ALA B O     1 
ATOM   11912 C CB    . ALA B  1 427  ? -25.082 20.680  111.231 1.00 45.58 ? 425  ALA B CB    1 
ATOM   11913 N N     . GLN B  1 428  ? -24.995 19.612  108.159 1.00 43.60 ? 426  GLN B N     1 
ATOM   11914 C CA    . GLN B  1 428  ? -25.673 18.928  107.064 1.00 45.83 ? 426  GLN B CA    1 
ATOM   11915 C C     . GLN B  1 428  ? -24.927 17.660  106.679 1.00 43.35 ? 426  GLN B C     1 
ATOM   11916 O O     . GLN B  1 428  ? -25.538 16.594  106.523 1.00 43.11 ? 426  GLN B O     1 
ATOM   11917 C CB    . GLN B  1 428  ? -25.831 19.859  105.863 1.00 46.70 ? 426  GLN B CB    1 
ATOM   11918 C CG    . GLN B  1 428  ? -26.823 19.349  104.822 1.00 47.07 ? 426  GLN B CG    1 
ATOM   11919 C CD    . GLN B  1 428  ? -26.281 18.197  103.988 1.00 47.25 ? 426  GLN B CD    1 
ATOM   11920 O OE1   . GLN B  1 428  ? -25.092 18.149  103.672 1.00 47.84 ? 426  GLN B OE1   1 
ATOM   11921 N NE2   . GLN B  1 428  ? -27.154 17.266  103.629 1.00 42.97 ? 426  GLN B NE2   1 
ATOM   11922 N N     . THR B  1 429  ? -23.600 17.760  106.518 1.00 43.21 ? 427  THR B N     1 
ATOM   11923 C CA    . THR B  1 429  ? -22.786 16.576  106.252 1.00 41.40 ? 427  THR B CA    1 
ATOM   11924 C C     . THR B  1 429  ? -22.939 15.545  107.367 1.00 40.16 ? 427  THR B C     1 
ATOM   11925 O O     . THR B  1 429  ? -23.086 14.344  107.107 1.00 38.68 ? 427  THR B O     1 
ATOM   11926 C CB    . THR B  1 429  ? -21.308 16.964  106.099 1.00 38.74 ? 427  THR B CB    1 
ATOM   11927 O OG1   . THR B  1 429  ? -21.172 18.066  105.185 1.00 39.32 ? 427  THR B OG1   1 
ATOM   11928 C CG2   . THR B  1 429  ? -20.518 15.775  105.589 1.00 36.99 ? 427  THR B CG2   1 
ATOM   11929 N N     . LEU B  1 430  ? -22.874 16.000  108.621 1.00 41.31 ? 428  LEU B N     1 
ATOM   11930 C CA    . LEU B  1 430  ? -22.958 15.096  109.765 1.00 39.55 ? 428  LEU B CA    1 
ATOM   11931 C C     . LEU B  1 430  ? -24.286 14.340  109.777 1.00 45.23 ? 428  LEU B C     1 
ATOM   11932 O O     . LEU B  1 430  ? -24.323 13.114  109.943 1.00 44.09 ? 428  LEU B O     1 
ATOM   11933 C CB    . LEU B  1 430  ? -22.774 15.910  111.048 1.00 41.02 ? 428  LEU B CB    1 
ATOM   11934 C CG    . LEU B  1 430  ? -22.615 15.279  112.437 1.00 41.59 ? 428  LEU B CG    1 
ATOM   11935 C CD1   . LEU B  1 430  ? -22.110 16.354  113.360 1.00 43.79 ? 428  LEU B CD1   1 
ATOM   11936 C CD2   . LEU B  1 430  ? -23.922 14.708  112.984 1.00 47.30 ? 428  LEU B CD2   1 
ATOM   11937 N N     . ALA B  1 431  ? -25.394 15.062  109.609 1.00 44.50 ? 429  ALA B N     1 
ATOM   11938 C CA    . ALA B  1 431  ? -26.702 14.414  109.658 1.00 45.84 ? 429  ALA B CA    1 
ATOM   11939 C C     . ALA B  1 431  ? -26.838 13.360  108.563 1.00 44.71 ? 429  ALA B C     1 
ATOM   11940 O O     . ALA B  1 431  ? -27.365 12.266  108.805 1.00 48.51 ? 429  ALA B O     1 
ATOM   11941 C CB    . ALA B  1 431  ? -27.804 15.464  109.544 1.00 45.93 ? 429  ALA B CB    1 
ATOM   11942 N N     . ALA B  1 432  ? -26.345 13.668  107.357 1.00 44.44 ? 430  ALA B N     1 
ATOM   11943 C CA    . ALA B  1 432  ? -26.424 12.721  106.250 1.00 42.51 ? 430  ALA B CA    1 
ATOM   11944 C C     . ALA B  1 432  ? -25.725 11.412  106.585 1.00 44.08 ? 430  ALA B C     1 
ATOM   11945 O O     . ALA B  1 432  ? -26.255 10.332  106.309 1.00 43.68 ? 430  ALA B O     1 
ATOM   11946 C CB    . ALA B  1 432  ? -25.819 13.343  104.989 1.00 43.09 ? 430  ALA B CB    1 
ATOM   11947 N N     . ILE B  1 433  ? -24.522 11.484  107.164 1.00 45.22 ? 431  ILE B N     1 
ATOM   11948 C CA    . ILE B  1 433  ? -23.809 10.260  107.517 1.00 48.25 ? 431  ILE B CA    1 
ATOM   11949 C C     . ILE B  1 433  ? -24.488 9.569   108.688 1.00 42.85 ? 431  ILE B C     1 
ATOM   11950 O O     . ILE B  1 433  ? -24.604 8.340   108.719 1.00 44.44 ? 431  ILE B O     1 
ATOM   11951 C CB    . ILE B  1 433  ? -22.334 10.569  107.823 1.00 45.56 ? 431  ILE B CB    1 
ATOM   11952 C CG1   . ILE B  1 433  ? -21.672 11.183  106.596 1.00 47.50 ? 431  ILE B CG1   1 
ATOM   11953 C CG2   . ILE B  1 433  ? -21.596 9.308   108.258 1.00 44.90 ? 431  ILE B CG2   1 
ATOM   11954 C CD1   . ILE B  1 433  ? -20.206 11.418  106.784 1.00 46.20 ? 431  ILE B CD1   1 
ATOM   11955 N N     . TYR B  1 434  ? -24.951 10.352  109.663 1.00 47.44 ? 432  TYR B N     1 
ATOM   11956 C CA    . TYR B  1 434  ? -25.597 9.795   110.850 1.00 47.02 ? 432  TYR B CA    1 
ATOM   11957 C C     . TYR B  1 434  ? -26.780 8.902   110.481 1.00 50.22 ? 432  TYR B C     1 
ATOM   11958 O O     . TYR B  1 434  ? -27.000 7.853   111.102 1.00 50.71 ? 432  TYR B O     1 
ATOM   11959 C CB    . TYR B  1 434  ? -26.029 10.945  111.763 1.00 46.68 ? 432  TYR B CB    1 
ATOM   11960 C CG    . TYR B  1 434  ? -26.964 10.569  112.890 1.00 48.64 ? 432  TYR B CG    1 
ATOM   11961 C CD1   . TYR B  1 434  ? -26.509 9.854   113.995 1.00 48.48 ? 432  TYR B CD1   1 
ATOM   11962 C CD2   . TYR B  1 434  ? -28.303 10.953  112.860 1.00 52.79 ? 432  TYR B CD2   1 
ATOM   11963 C CE1   . TYR B  1 434  ? -27.370 9.519   115.032 1.00 51.98 ? 432  TYR B CE1   1 
ATOM   11964 C CE2   . TYR B  1 434  ? -29.169 10.626  113.890 1.00 52.15 ? 432  TYR B CE2   1 
ATOM   11965 C CZ    . TYR B  1 434  ? -28.699 9.909   114.972 1.00 53.33 ? 432  TYR B CZ    1 
ATOM   11966 O OH    . TYR B  1 434  ? -29.557 9.582   115.993 1.00 50.15 ? 432  TYR B OH    1 
ATOM   11967 N N     . HIS B  1 435  ? -27.538 9.286   109.461 1.00 50.54 ? 433  HIS B N     1 
ATOM   11968 C CA    . HIS B  1 435  ? -28.681 8.491   109.038 1.00 50.84 ? 433  HIS B CA    1 
ATOM   11969 C C     . HIS B  1 435  ? -28.318 7.432   108.009 1.00 51.67 ? 433  HIS B C     1 
ATOM   11970 O O     . HIS B  1 435  ? -29.022 6.425   107.897 1.00 52.34 ? 433  HIS B O     1 
ATOM   11971 C CB    . HIS B  1 435  ? -29.771 9.412   108.490 1.00 53.03 ? 433  HIS B CB    1 
ATOM   11972 C CG    . HIS B  1 435  ? -30.529 10.134  109.560 1.00 54.65 ? 433  HIS B CG    1 
ATOM   11973 N ND1   . HIS B  1 435  ? -31.385 9.488   110.424 1.00 52.34 ? 433  HIS B ND1   1 
ATOM   11974 C CD2   . HIS B  1 435  ? -30.545 11.439  109.919 1.00 53.56 ? 433  HIS B CD2   1 
ATOM   11975 C CE1   . HIS B  1 435  ? -31.901 10.364  111.267 1.00 53.09 ? 433  HIS B CE1   1 
ATOM   11976 N NE2   . HIS B  1 435  ? -31.412 11.557  110.979 1.00 52.42 ? 433  HIS B NE2   1 
ATOM   11977 N N     . MET B  1 436  ? -27.227 7.632   107.272 1.00 52.03 ? 434  MET B N     1 
ATOM   11978 C CA    . MET B  1 436  ? -26.779 6.646   106.300 1.00 47.76 ? 434  MET B CA    1 
ATOM   11979 C C     . MET B  1 436  ? -26.219 5.406   106.980 1.00 50.82 ? 434  MET B C     1 
ATOM   11980 O O     . MET B  1 436  ? -26.264 4.310   106.408 1.00 49.59 ? 434  MET B O     1 
ATOM   11981 C CB    . MET B  1 436  ? -25.737 7.301   105.390 1.00 49.41 ? 434  MET B CB    1 
ATOM   11982 C CG    . MET B  1 436  ? -24.925 6.376   104.518 1.00 49.96 ? 434  MET B CG    1 
ATOM   11983 S SD    . MET B  1 436  ? -23.697 7.350   103.625 1.00 55.03 ? 434  MET B SD    1 
ATOM   11984 C CE    . MET B  1 436  ? -24.755 8.479   102.721 1.00 43.64 ? 434  MET B CE    1 
ATOM   11985 N N     . ALA B  1 437  ? -25.701 5.558   108.203 1.00 50.87 ? 435  ALA B N     1 
ATOM   11986 C CA    . ALA B  1 437  ? -25.081 4.450   108.916 1.00 50.77 ? 435  ALA B CA    1 
ATOM   11987 C C     . ALA B  1 437  ? -26.091 3.472   109.501 1.00 56.05 ? 435  ALA B C     1 
ATOM   11988 O O     . ALA B  1 437  ? -25.717 2.334   109.806 1.00 58.38 ? 435  ALA B O     1 
ATOM   11989 C CB    . ALA B  1 437  ? -24.183 4.988   110.027 1.00 45.83 ? 435  ALA B CB    1 
ATOM   11990 N N     . GLY B  1 438  ? -27.351 3.880   109.666 1.00 55.44 ? 436  GLY B N     1 
ATOM   11991 C CA    . GLY B  1 438  ? -28.379 2.989   110.178 1.00 58.59 ? 436  GLY B CA    1 
ATOM   11992 C C     . GLY B  1 438  ? -28.579 3.083   111.679 1.00 64.62 ? 436  GLY B C     1 
ATOM   11993 O O     . GLY B  1 438  ? -28.288 4.122   112.284 1.00 58.74 ? 436  GLY B O     1 
ATOM   11994 N N     . LYS B  1 439  ? -29.064 1.996   112.295 1.00 62.13 ? 437  LYS B N     1 
ATOM   11995 C CA    . LYS B  1 439  ? -29.343 1.973   113.725 1.00 58.36 ? 437  LYS B CA    1 
ATOM   11996 C C     . LYS B  1 439  ? -28.441 1.046   114.527 1.00 62.31 ? 437  LYS B C     1 
ATOM   11997 O O     . LYS B  1 439  ? -28.413 1.157   115.757 1.00 66.11 ? 437  LYS B O     1 
ATOM   11998 C CB    . LYS B  1 439  ? -30.804 1.562   113.975 1.00 64.12 ? 437  LYS B CB    1 
ATOM   11999 C CG    . LYS B  1 439  ? -31.798 2.310   113.111 1.00 61.13 ? 437  LYS B CG    1 
ATOM   12000 C CD    . LYS B  1 439  ? -32.998 2.766   113.916 1.00 62.47 ? 437  LYS B CD    1 
ATOM   12001 C CE    . LYS B  1 439  ? -33.370 4.205   113.576 1.00 69.23 ? 437  LYS B CE    1 
ATOM   12002 N NZ    . LYS B  1 439  ? -32.734 5.179   114.507 1.00 68.79 ? 437  LYS B NZ    1 
ATOM   12003 N N     . ASP B  1 440  ? -27.717 0.132   113.882 1.00 60.92 ? 438  ASP B N     1 
ATOM   12004 C CA    . ASP B  1 440  ? -26.897 -0.843  114.603 1.00 64.31 ? 438  ASP B CA    1 
ATOM   12005 C C     . ASP B  1 440  ? -25.560 -0.221  115.023 1.00 69.28 ? 438  ASP B C     1 
ATOM   12006 O O     . ASP B  1 440  ? -24.482 -0.722  114.705 1.00 72.62 ? 438  ASP B O     1 
ATOM   12007 C CB    . ASP B  1 440  ? -26.680 -2.086  113.750 1.00 61.19 ? 438  ASP B CB    1 
ATOM   12008 N N     . PHE B  1 441  ? -25.654 0.883   115.772 1.00 68.61 ? 439  PHE B N     1 
ATOM   12009 C CA    . PHE B  1 441  ? -24.494 1.705   116.112 1.00 60.92 ? 439  PHE B CA    1 
ATOM   12010 C C     . PHE B  1 441  ? -23.849 1.247   117.415 1.00 60.17 ? 439  PHE B C     1 
ATOM   12011 O O     . PHE B  1 441  ? -24.534 0.933   118.393 1.00 59.21 ? 439  PHE B O     1 
ATOM   12012 C CB    . PHE B  1 441  ? -24.893 3.180   116.222 1.00 56.45 ? 439  PHE B CB    1 
ATOM   12013 N N     . HIS B  1 442  ? -22.518 1.211   117.421 1.00 61.66 ? 440  HIS B N     1 
ATOM   12014 C CA    . HIS B  1 442  ? -21.768 0.875   118.622 1.00 57.09 ? 440  HIS B CA    1 
ATOM   12015 C C     . HIS B  1 442  ? -20.396 1.522   118.523 1.00 52.14 ? 440  HIS B C     1 
ATOM   12016 O O     . HIS B  1 442  ? -20.026 2.074   117.485 1.00 53.20 ? 440  HIS B O     1 
ATOM   12017 C CB    . HIS B  1 442  ? -21.653 -0.644  118.817 1.00 58.86 ? 440  HIS B CB    1 
ATOM   12018 C CG    . HIS B  1 442  ? -20.816 -1.334  117.781 1.00 60.25 ? 440  HIS B CG    1 
ATOM   12019 N ND1   . HIS B  1 442  ? -19.452 -1.486  117.908 1.00 59.44 ? 440  HIS B ND1   1 
ATOM   12020 C CD2   . HIS B  1 442  ? -21.151 -1.919  116.606 1.00 59.21 ? 440  HIS B CD2   1 
ATOM   12021 C CE1   . HIS B  1 442  ? -18.983 -2.140  116.860 1.00 57.52 ? 440  HIS B CE1   1 
ATOM   12022 N NE2   . HIS B  1 442  ? -19.994 -2.414  116.055 1.00 61.29 ? 440  HIS B NE2   1 
ATOM   12023 N N     . VAL B  1 443  ? -19.650 1.466   119.622 1.00 50.18 ? 441  VAL B N     1 
ATOM   12024 C CA    . VAL B  1 443  ? -18.299 2.022   119.645 1.00 50.26 ? 441  VAL B CA    1 
ATOM   12025 C C     . VAL B  1 443  ? -17.345 1.021   119.008 1.00 49.52 ? 441  VAL B C     1 
ATOM   12026 O O     . VAL B  1 443  ? -17.379 -0.176  119.317 1.00 52.59 ? 441  VAL B O     1 
ATOM   12027 C CB    . VAL B  1 443  ? -17.871 2.378   121.077 1.00 52.01 ? 441  VAL B CB    1 
ATOM   12028 C CG1   . VAL B  1 443  ? -16.469 2.966   121.071 1.00 53.35 ? 441  VAL B CG1   1 
ATOM   12029 C CG2   . VAL B  1 443  ? -18.847 3.374   121.684 1.00 53.35 ? 441  VAL B CG2   1 
ATOM   12030 N N     . GLY B  1 444  ? -16.497 1.508   118.107 1.00 50.06 ? 442  GLY B N     1 
ATOM   12031 C CA    . GLY B  1 444  ? -15.699 0.659   117.256 1.00 45.07 ? 442  GLY B CA    1 
ATOM   12032 C C     . GLY B  1 444  ? -16.235 0.523   115.845 1.00 48.65 ? 442  GLY B C     1 
ATOM   12033 O O     . GLY B  1 444  ? -15.503 0.051   114.968 1.00 46.20 ? 442  GLY B O     1 
ATOM   12034 N N     . LYS B  1 445  ? -17.490 0.919   115.607 1.00 50.13 ? 443  LYS B N     1 
ATOM   12035 C CA    . LYS B  1 445  ? -18.068 0.857   114.267 1.00 47.12 ? 443  LYS B CA    1 
ATOM   12036 C C     . LYS B  1 445  ? -17.585 2.022   113.410 1.00 45.77 ? 443  LYS B C     1 
ATOM   12037 O O     . LYS B  1 445  ? -16.980 1.820   112.352 1.00 45.10 ? 443  LYS B O     1 
ATOM   12038 C CB    . LYS B  1 445  ? -19.597 0.849   114.354 1.00 51.47 ? 443  LYS B CB    1 
ATOM   12039 N N     . TYR B  1 446  ? -17.862 3.246   113.851 1.00 45.11 ? 444  TYR B N     1 
ATOM   12040 C CA    . TYR B  1 446  ? -17.342 4.459   113.235 1.00 43.80 ? 444  TYR B CA    1 
ATOM   12041 C C     . TYR B  1 446  ? -17.358 5.547   114.302 1.00 43.37 ? 444  TYR B C     1 
ATOM   12042 O O     . TYR B  1 446  ? -17.849 5.340   115.417 1.00 45.68 ? 444  TYR B O     1 
ATOM   12043 C CB    . TYR B  1 446  ? -18.158 4.856   111.990 1.00 39.92 ? 444  TYR B CB    1 
ATOM   12044 C CG    . TYR B  1 446  ? -19.589 5.253   112.268 1.00 45.22 ? 444  TYR B CG    1 
ATOM   12045 C CD1   . TYR B  1 446  ? -19.925 6.572   112.550 1.00 45.36 ? 444  TYR B CD1   1 
ATOM   12046 C CD2   . TYR B  1 446  ? -20.609 4.310   112.230 1.00 44.79 ? 444  TYR B CD2   1 
ATOM   12047 C CE1   . TYR B  1 446  ? -21.236 6.933   112.810 1.00 49.49 ? 444  TYR B CE1   1 
ATOM   12048 C CE2   . TYR B  1 446  ? -21.912 4.661   112.487 1.00 48.33 ? 444  TYR B CE2   1 
ATOM   12049 C CZ    . TYR B  1 446  ? -22.223 5.975   112.773 1.00 50.02 ? 444  TYR B CZ    1 
ATOM   12050 O OH    . TYR B  1 446  ? -23.531 6.323   113.021 1.00 57.78 ? 444  TYR B OH    1 
ATOM   12051 N N     . GLU B  1 447  ? -16.805 6.706   113.958 1.00 43.28 ? 445  GLU B N     1 
ATOM   12052 C CA    . GLU B  1 447  ? -16.834 7.839   114.868 1.00 42.19 ? 445  GLU B CA    1 
ATOM   12053 C C     . GLU B  1 447  ? -16.859 9.117   114.053 1.00 38.41 ? 445  GLU B C     1 
ATOM   12054 O O     . GLU B  1 447  ? -16.564 9.117   112.859 1.00 36.32 ? 445  GLU B O     1 
ATOM   12055 C CB    . GLU B  1 447  ? -15.634 7.832   115.827 1.00 38.43 ? 445  GLU B CB    1 
ATOM   12056 C CG    . GLU B  1 447  ? -14.318 8.288   115.196 1.00 37.15 ? 445  GLU B CG    1 
ATOM   12057 C CD    . GLU B  1 447  ? -13.135 8.157   116.145 1.00 35.99 ? 445  GLU B CD    1 
ATOM   12058 O OE1   . GLU B  1 447  ? -13.339 7.689   117.286 1.00 36.06 ? 445  GLU B OE1   1 
ATOM   12059 O OE2   . GLU B  1 447  ? -12.000 8.506   115.743 1.00 35.12 ? 445  GLU B OE2   1 
ATOM   12060 N N     . PHE B  1 448  ? -17.241 10.208  114.705 1.00 37.36 ? 446  PHE B N     1 
ATOM   12061 C CA    . PHE B  1 448  ? -17.061 11.535  114.141 1.00 40.55 ? 446  PHE B CA    1 
ATOM   12062 C C     . PHE B  1 448  ? -15.802 12.161  114.736 1.00 39.55 ? 446  PHE B C     1 
ATOM   12063 O O     . PHE B  1 448  ? -15.267 11.687  115.741 1.00 37.98 ? 446  PHE B O     1 
ATOM   12064 C CB    . PHE B  1 448  ? -18.279 12.419  114.410 1.00 41.31 ? 446  PHE B CB    1 
ATOM   12065 N N     . GLN B  1 449  ? -15.315 13.223  114.090 1.00 35.59 ? 447  GLN B N     1 
ATOM   12066 C CA    . GLN B  1 449  ? -14.149 13.939  114.592 1.00 37.14 ? 447  GLN B CA    1 
ATOM   12067 C C     . GLN B  1 449  ? -14.333 15.432  114.376 1.00 38.17 ? 447  GLN B C     1 
ATOM   12068 O O     . GLN B  1 449  ? -15.022 15.866  113.449 1.00 36.56 ? 447  GLN B O     1 
ATOM   12069 C CB    . GLN B  1 449  ? -12.842 13.484  113.923 1.00 31.06 ? 447  GLN B CB    1 
ATOM   12070 C CG    . GLN B  1 449  ? -12.551 12.000  114.032 1.00 33.32 ? 447  GLN B CG    1 
ATOM   12071 C CD    . GLN B  1 449  ? -11.080 11.681  113.813 1.00 34.72 ? 447  GLN B CD    1 
ATOM   12072 O OE1   . GLN B  1 449  ? -10.318 12.514  113.303 1.00 33.87 ? 447  GLN B OE1   1 
ATOM   12073 N NE2   . GLN B  1 449  ? -10.675 10.471  114.184 1.00 31.83 ? 447  GLN B NE2   1 
ATOM   12074 N N     . CYS B  1 450  ? -13.725 16.218  115.258 1.00 32.54 ? 448  CYS B N     1 
ATOM   12075 C CA    . CYS B  1 450  ? -13.769 17.661  115.124 1.00 35.61 ? 448  CYS B CA    1 
ATOM   12076 C C     . CYS B  1 450  ? -12.457 18.238  115.621 1.00 33.71 ? 448  CYS B C     1 
ATOM   12077 O O     . CYS B  1 450  ? -11.608 17.535  116.177 1.00 36.00 ? 448  CYS B O     1 
ATOM   12078 C CB    . CYS B  1 450  ? -14.943 18.275  115.892 1.00 38.79 ? 448  CYS B CB    1 
ATOM   12079 S SG    . CYS B  1 450  ? -14.721 18.220  117.690 1.00 38.88 ? 448  CYS B SG    1 
ATOM   12080 N N     . LEU B  1 451  ? -12.315 19.536  115.416 1.00 32.74 ? 449  LEU B N     1 
ATOM   12081 C CA    . LEU B  1 451  ? -11.141 20.278  115.839 1.00 37.24 ? 449  LEU B CA    1 
ATOM   12082 C C     . LEU B  1 451  ? -11.403 20.909  117.200 1.00 39.11 ? 449  LEU B C     1 
ATOM   12083 O O     . LEU B  1 451  ? -12.486 21.445  117.453 1.00 37.34 ? 449  LEU B O     1 
ATOM   12084 C CB    . LEU B  1 451  ? -10.805 21.350  114.798 1.00 38.72 ? 449  LEU B CB    1 
ATOM   12085 C CG    . LEU B  1 451  ? -9.613  22.257  115.060 1.00 43.54 ? 449  LEU B CG    1 
ATOM   12086 C CD1   . LEU B  1 451  ? -8.316  21.448  115.032 1.00 44.46 ? 449  LEU B CD1   1 
ATOM   12087 C CD2   . LEU B  1 451  ? -9.584  23.374  114.031 1.00 45.28 ? 449  LEU B CD2   1 
ATOM   12088 N N     . HIS B  1 452  ? -10.415 20.811  118.085 1.00 32.71 ? 450  HIS B N     1 
ATOM   12089 C CA    . HIS B  1 452  ? -10.523 21.431  119.395 1.00 40.92 ? 450  HIS B CA    1 
ATOM   12090 C C     . HIS B  1 452  ? -10.877 22.902  119.252 1.00 38.99 ? 450  HIS B C     1 
ATOM   12091 O O     . HIS B  1 452  ? -10.367 23.593  118.368 1.00 40.34 ? 450  HIS B O     1 
ATOM   12092 C CB    . HIS B  1 452  ? -9.206  21.269  120.160 1.00 35.34 ? 450  HIS B CB    1 
ATOM   12093 C CG    . HIS B  1 452  ? -9.099  22.145  121.365 1.00 37.70 ? 450  HIS B CG    1 
ATOM   12094 N ND1   . HIS B  1 452  ? -9.533  21.753  122.612 1.00 38.03 ? 450  HIS B ND1   1 
ATOM   12095 C CD2   . HIS B  1 452  ? -8.618  23.402  121.511 1.00 38.77 ? 450  HIS B CD2   1 
ATOM   12096 C CE1   . HIS B  1 452  ? -9.318  22.729  123.477 1.00 39.88 ? 450  HIS B CE1   1 
ATOM   12097 N NE2   . HIS B  1 452  ? -8.768  23.743  122.832 1.00 39.09 ? 450  HIS B NE2   1 
ATOM   12098 N N     . GLY B  1 453  ? -11.775 23.370  120.115 1.00 41.71 ? 451  GLY B N     1 
ATOM   12099 C CA    . GLY B  1 453  ? -12.136 24.779  120.123 1.00 45.17 ? 451  GLY B CA    1 
ATOM   12100 C C     . GLY B  1 453  ? -12.783 25.250  118.844 1.00 47.27 ? 451  GLY B C     1 
ATOM   12101 O O     . GLY B  1 453  ? -12.599 26.406  118.443 1.00 47.30 ? 451  GLY B O     1 
ATOM   12102 N N     . MET B  1 454  ? -13.520 24.374  118.177 1.00 45.00 ? 452  MET B N     1 
ATOM   12103 C CA    . MET B  1 454  ? -14.217 24.742  116.955 1.00 41.35 ? 452  MET B CA    1 
ATOM   12104 C C     . MET B  1 454  ? -15.429 23.847  116.805 1.00 43.75 ? 452  MET B C     1 
ATOM   12105 O O     . MET B  1 454  ? -16.553 24.329  116.640 1.00 43.96 ? 452  MET B O     1 
ATOM   12106 C CB    . MET B  1 454  ? -13.303 24.611  115.733 1.00 44.31 ? 452  MET B CB    1 
ATOM   12107 C CG    . MET B  1 454  ? -14.039 24.823  114.423 1.00 46.65 ? 452  MET B CG    1 
ATOM   12108 S SD    . MET B  1 454  ? -14.865 26.420  114.442 1.00 55.69 ? 452  MET B SD    1 
ATOM   12109 C CE    . MET B  1 454  ? -13.432 27.506  114.501 1.00 45.51 ? 452  MET B CE    1 
ATOM   12110 N N     . GLY B  1 455  ? -15.202 22.540  116.865 1.00 39.92 ? 453  GLY B N     1 
ATOM   12111 C CA    . GLY B  1 455  ? -16.281 21.594  116.710 1.00 40.92 ? 453  GLY B CA    1 
ATOM   12112 C C     . GLY B  1 455  ? -17.046 21.294  117.971 1.00 44.81 ? 453  GLY B C     1 
ATOM   12113 O O     . GLY B  1 455  ? -18.065 20.604  117.900 1.00 43.66 ? 453  GLY B O     1 
ATOM   12114 N N     . GLU B  1 456  ? -16.578 21.794  119.122 1.00 48.61 ? 454  GLU B N     1 
ATOM   12115 C CA    . GLU B  1 456  ? -17.223 21.455  120.388 1.00 50.60 ? 454  GLU B CA    1 
ATOM   12116 C C     . GLU B  1 456  ? -18.679 21.906  120.443 1.00 45.47 ? 454  GLU B C     1 
ATOM   12117 O O     . GLU B  1 456  ? -19.530 21.092  120.836 1.00 49.07 ? 454  GLU B O     1 
ATOM   12118 C CB    . GLU B  1 456  ? -16.404 22.014  121.559 1.00 50.92 ? 454  GLU B CB    1 
ATOM   12119 N N     . PRO B  1 457  ? -19.044 23.146  120.070 1.00 47.38 ? 455  PRO B N     1 
ATOM   12120 C CA    . PRO B  1 457  ? -20.477 23.492  120.035 1.00 51.10 ? 455  PRO B CA    1 
ATOM   12121 C C     . PRO B  1 457  ? -21.333 22.502  119.261 1.00 49.06 ? 455  PRO B C     1 
ATOM   12122 O O     . PRO B  1 457  ? -22.390 22.091  119.755 1.00 50.62 ? 455  PRO B O     1 
ATOM   12123 C CB    . PRO B  1 457  ? -20.470 24.883  119.389 1.00 49.15 ? 455  PRO B CB    1 
ATOM   12124 C CG    . PRO B  1 457  ? -19.192 25.479  119.862 1.00 49.20 ? 455  PRO B CG    1 
ATOM   12125 C CD    . PRO B  1 457  ? -18.208 24.334  119.797 1.00 50.64 ? 455  PRO B CD    1 
ATOM   12126 N N     . LEU B  1 458  ? -20.897 22.091  118.066 1.00 47.18 ? 456  LEU B N     1 
ATOM   12127 C CA    . LEU B  1 458  ? -21.692 21.157  117.272 1.00 46.87 ? 456  LEU B CA    1 
ATOM   12128 C C     . LEU B  1 458  ? -21.787 19.798  117.951 1.00 44.84 ? 456  LEU B C     1 
ATOM   12129 O O     . LEU B  1 458  ? -22.882 19.249  118.118 1.00 46.16 ? 456  LEU B O     1 
ATOM   12130 C CB    . LEU B  1 458  ? -21.102 21.014  115.863 1.00 42.98 ? 456  LEU B CB    1 
ATOM   12131 N N     . TYR B  1 459  ? -20.654 19.236  118.359 1.00 47.02 ? 457  TYR B N     1 
ATOM   12132 C CA    . TYR B  1 459  ? -20.684 17.871  118.863 1.00 45.22 ? 457  TYR B CA    1 
ATOM   12133 C C     . TYR B  1 459  ? -21.132 17.786  120.323 1.00 42.92 ? 457  TYR B C     1 
ATOM   12134 O O     . TYR B  1 459  ? -21.434 16.681  120.784 1.00 43.36 ? 457  TYR B O     1 
ATOM   12135 C CB    . TYR B  1 459  ? -19.320 17.211  118.644 1.00 44.27 ? 457  TYR B CB    1 
ATOM   12136 C CG    . TYR B  1 459  ? -19.112 16.871  117.184 1.00 42.83 ? 457  TYR B CG    1 
ATOM   12137 C CD1   . TYR B  1 459  ? -19.623 15.696  116.650 1.00 44.13 ? 457  TYR B CD1   1 
ATOM   12138 C CD2   . TYR B  1 459  ? -18.458 17.747  116.335 1.00 40.85 ? 457  TYR B CD2   1 
ATOM   12139 C CE1   . TYR B  1 459  ? -19.470 15.391  115.318 1.00 43.70 ? 457  TYR B CE1   1 
ATOM   12140 C CE2   . TYR B  1 459  ? -18.284 17.449  114.993 1.00 42.37 ? 457  TYR B CE2   1 
ATOM   12141 C CZ    . TYR B  1 459  ? -18.795 16.262  114.492 1.00 44.55 ? 457  TYR B CZ    1 
ATOM   12142 O OH    . TYR B  1 459  ? -18.647 15.942  113.161 1.00 42.74 ? 457  TYR B OH    1 
ATOM   12143 N N     . GLU B  1 460  ? -21.226 18.927  121.027 1.00 42.09 ? 458  GLU B N     1 
ATOM   12144 C CA    . GLU B  1 460  ? -21.915 18.960  122.308 1.00 47.42 ? 458  GLU B CA    1 
ATOM   12145 C C     . GLU B  1 460  ? -23.401 18.663  122.129 1.00 50.53 ? 458  GLU B C     1 
ATOM   12146 O O     . GLU B  1 460  ? -24.045 18.208  123.076 1.00 54.06 ? 458  GLU B O     1 
ATOM   12147 C CB    . GLU B  1 460  ? -21.695 20.308  123.010 1.00 46.32 ? 458  GLU B CB    1 
ATOM   12148 N N     . GLU B  1 461  ? -23.943 18.887  120.939 1.00 51.08 ? 459  GLU B N     1 
ATOM   12149 C CA    . GLU B  1 461  ? -25.281 18.477  120.589 1.00 54.66 ? 459  GLU B CA    1 
ATOM   12150 C C     . GLU B  1 461  ? -25.321 17.118  119.875 1.00 53.25 ? 459  GLU B C     1 
ATOM   12151 O O     . GLU B  1 461  ? -26.357 16.766  119.295 1.00 51.31 ? 459  GLU B O     1 
ATOM   12152 C CB    . GLU B  1 461  ? -25.900 19.574  119.724 1.00 64.51 ? 459  GLU B CB    1 
ATOM   12153 N N     . VAL B  1 462  ? -24.234 16.334  119.934 1.00 51.02 ? 460  VAL B N     1 
ATOM   12154 C CA    . VAL B  1 462  ? -24.114 15.044  119.263 1.00 48.95 ? 460  VAL B CA    1 
ATOM   12155 C C     . VAL B  1 462  ? -23.710 13.938  120.243 1.00 51.54 ? 460  VAL B C     1 
ATOM   12156 O O     . VAL B  1 462  ? -24.245 12.833  120.187 1.00 53.33 ? 460  VAL B O     1 
ATOM   12157 C CB    . VAL B  1 462  ? -23.100 15.122  118.089 1.00 49.84 ? 460  VAL B CB    1 
ATOM   12158 C CG1   . VAL B  1 462  ? -22.788 13.735  117.476 1.00 48.17 ? 460  VAL B CG1   1 
ATOM   12159 C CG2   . VAL B  1 462  ? -23.477 16.097  117.053 1.00 47.72 ? 460  VAL B CG2   1 
ATOM   12160 N N     . VAL B  1 463  ? -22.674 14.188  121.093 1.00 50.26 ? 461  VAL B N     1 
ATOM   12161 C CA    . VAL B  1 463  ? -22.221 13.177  122.054 1.00 47.85 ? 461  VAL B CA    1 
ATOM   12162 C C     . VAL B  1 463  ? -23.163 13.167  123.246 1.00 53.43 ? 461  VAL B C     1 
ATOM   12163 O O     . VAL B  1 463  ? -23.604 14.224  123.728 1.00 51.15 ? 461  VAL B O     1 
ATOM   12164 C CB    . VAL B  1 463  ? -20.771 13.434  122.512 1.00 50.86 ? 461  VAL B CB    1 
ATOM   12165 N N     . GLY B  1 464  ? -23.439 11.979  123.744 1.00 50.29 ? 462  GLY B N     1 
ATOM   12166 C CA    . GLY B  1 464  ? -24.282 11.855  124.915 1.00 54.71 ? 462  GLY B CA    1 
ATOM   12167 C C     . GLY B  1 464  ? -25.617 11.171  124.609 1.00 56.28 ? 462  GLY B C     1 
ATOM   12168 O O     . GLY B  1 464  ? -26.167 11.274  123.502 1.00 55.91 ? 462  GLY B O     1 
ATOM   12169 N N     . ARG B  1 465  ? -26.145 10.449  125.611 1.00 57.27 ? 463  ARG B N     1 
ATOM   12170 C CA    . ARG B  1 465  ? -27.404 9.727   125.419 1.00 57.17 ? 463  ARG B CA    1 
ATOM   12171 C C     . ARG B  1 465  ? -28.564 10.679  125.145 1.00 61.95 ? 463  ARG B C     1 
ATOM   12172 O O     . ARG B  1 465  ? -29.487 10.342  124.387 1.00 61.58 ? 463  ARG B O     1 
ATOM   12173 C CB    . ARG B  1 465  ? -27.705 8.851   126.642 1.00 63.63 ? 463  ARG B CB    1 
ATOM   12174 N N     . GLY B  1 466  ? -28.527 11.871  125.734 1.00 59.39 ? 464  GLY B N     1 
ATOM   12175 C CA    . GLY B  1 466  ? -29.545 12.885  125.567 1.00 59.21 ? 464  GLY B CA    1 
ATOM   12176 C C     . GLY B  1 466  ? -29.441 13.673  124.286 1.00 60.58 ? 464  GLY B C     1 
ATOM   12177 O O     . GLY B  1 466  ? -30.154 14.669  124.122 1.00 62.88 ? 464  GLY B O     1 
ATOM   12178 N N     . LYS B  1 467  ? -28.559 13.258  123.377 1.00 59.36 ? 465  LYS B N     1 
ATOM   12179 C CA    . LYS B  1 467  ? -28.361 13.938  122.109 1.00 58.69 ? 465  LYS B CA    1 
ATOM   12180 C C     . LYS B  1 467  ? -28.497 12.933  120.970 1.00 61.74 ? 465  LYS B C     1 
ATOM   12181 O O     . LYS B  1 467  ? -29.612 12.491  120.670 1.00 62.73 ? 465  LYS B O     1 
ATOM   12182 C CB    . LYS B  1 467  ? -27.004 14.640  122.105 1.00 58.20 ? 465  LYS B CB    1 
ATOM   12183 C CG    . LYS B  1 467  ? -26.955 15.842  123.040 1.00 54.50 ? 465  LYS B CG    1 
ATOM   12184 C CD    . LYS B  1 467  ? -27.873 16.945  122.534 1.00 58.65 ? 465  LYS B CD    1 
ATOM   12185 C CE    . LYS B  1 467  ? -28.190 17.962  123.616 1.00 54.85 ? 465  LYS B CE    1 
ATOM   12186 N NZ    . LYS B  1 467  ? -27.023 18.197  124.502 1.00 63.27 ? 465  LYS B NZ    1 
ATOM   12187 N N     . LEU B  1 468  ? -27.385 12.555  120.333 1.00 55.20 ? 466  LEU B N     1 
ATOM   12188 C CA    . LEU B  1 468  ? -27.414 11.542  119.284 1.00 50.93 ? 466  LEU B CA    1 
ATOM   12189 C C     . LEU B  1 468  ? -26.674 10.271  119.664 1.00 51.49 ? 466  LEU B C     1 
ATOM   12190 O O     . LEU B  1 468  ? -26.681 9.311   118.884 1.00 49.01 ? 466  LEU B O     1 
ATOM   12191 C CB    . LEU B  1 468  ? -26.830 12.100  117.979 1.00 54.08 ? 466  LEU B CB    1 
ATOM   12192 C CG    . LEU B  1 468  ? -27.533 13.336  117.420 1.00 52.87 ? 466  LEU B CG    1 
ATOM   12193 C CD1   . LEU B  1 468  ? -26.854 13.804  116.149 1.00 53.03 ? 466  LEU B CD1   1 
ATOM   12194 C CD2   . LEU B  1 468  ? -29.013 13.046  117.181 1.00 57.26 ? 466  LEU B CD2   1 
ATOM   12195 N N     . ASP B  1 469  ? -26.042 10.242  120.837 1.00 55.01 ? 467  ASP B N     1 
ATOM   12196 C CA    . ASP B  1 469  ? -25.208 9.129   121.296 1.00 56.13 ? 467  ASP B CA    1 
ATOM   12197 C C     . ASP B  1 469  ? -24.250 8.652   120.206 1.00 50.97 ? 467  ASP B C     1 
ATOM   12198 O O     . ASP B  1 469  ? -24.170 7.465   119.884 1.00 50.97 ? 467  ASP B O     1 
ATOM   12199 C CB    . ASP B  1 469  ? -26.062 7.977   121.826 1.00 58.67 ? 467  ASP B CB    1 
ATOM   12200 C CG    . ASP B  1 469  ? -25.440 7.319   123.030 1.00 64.48 ? 467  ASP B CG    1 
ATOM   12201 O OD1   . ASP B  1 469  ? -24.983 8.061   123.924 1.00 64.13 ? 467  ASP B OD1   1 
ATOM   12202 O OD2   . ASP B  1 469  ? -25.405 6.070   123.086 1.00 74.48 ? 467  ASP B OD2   1 
ATOM   12203 N N     . ARG B  1 470  ? -23.507 9.603   119.639 1.00 52.09 ? 468  ARG B N     1 
ATOM   12204 C CA    . ARG B  1 470  ? -22.454 9.262   118.702 1.00 49.52 ? 468  ARG B CA    1 
ATOM   12205 C C     . ARG B  1 470  ? -21.117 9.790   119.208 1.00 49.31 ? 468  ARG B C     1 
ATOM   12206 O O     . ARG B  1 470  ? -21.046 10.915  119.719 1.00 46.43 ? 468  ARG B O     1 
ATOM   12207 C CB    . ARG B  1 470  ? -22.735 9.827   117.301 1.00 49.07 ? 468  ARG B CB    1 
ATOM   12208 C CG    . ARG B  1 470  ? -23.901 9.153   116.579 1.00 45.85 ? 468  ARG B CG    1 
ATOM   12209 C CD    . ARG B  1 470  ? -23.774 7.625   116.613 1.00 49.67 ? 468  ARG B CD    1 
ATOM   12210 N NE    . ARG B  1 470  ? -24.927 6.939   116.033 1.00 50.24 ? 468  ARG B NE    1 
ATOM   12211 C CZ    . ARG B  1 470  ? -25.971 6.488   116.721 1.00 55.46 ? 468  ARG B CZ    1 
ATOM   12212 N NH1   . ARG B  1 470  ? -26.074 6.673   118.030 1.00 45.49 ? 468  ARG B NH1   1 
ATOM   12213 N NH2   . ARG B  1 470  ? -26.938 5.834   116.079 1.00 48.73 ? 468  ARG B NH2   1 
ATOM   12214 N N     . PRO B  1 471  ? -20.052 9.006   119.096 1.00 42.84 ? 469  PRO B N     1 
ATOM   12215 C CA    . PRO B  1 471  ? -18.756 9.434   119.623 1.00 48.24 ? 469  PRO B CA    1 
ATOM   12216 C C     . PRO B  1 471  ? -18.060 10.415  118.692 1.00 45.88 ? 469  PRO B C     1 
ATOM   12217 O O     . PRO B  1 471  ? -18.326 10.488  117.488 1.00 41.25 ? 469  PRO B O     1 
ATOM   12218 C CB    . PRO B  1 471  ? -17.971 8.124   119.730 1.00 43.72 ? 469  PRO B CB    1 
ATOM   12219 C CG    . PRO B  1 471  ? -18.563 7.274   118.685 1.00 44.23 ? 469  PRO B CG    1 
ATOM   12220 C CD    . PRO B  1 471  ? -20.029 7.596   118.676 1.00 45.79 ? 469  PRO B CD    1 
ATOM   12221 N N     . CYS B  1 472  ? -17.155 11.183  119.284 1.00 42.89 ? 470  CYS B N     1 
ATOM   12222 C CA    . CYS B  1 472  ? -16.409 12.195  118.553 1.00 43.11 ? 470  CYS B CA    1 
ATOM   12223 C C     . CYS B  1 472  ? -14.986 12.235  119.085 1.00 42.87 ? 470  CYS B C     1 
ATOM   12224 O O     . CYS B  1 472  ? -14.781 12.319  120.301 1.00 42.12 ? 470  CYS B O     1 
ATOM   12225 C CB    . CYS B  1 472  ? -17.060 13.573  118.686 1.00 41.14 ? 470  CYS B CB    1 
ATOM   12226 S SG    . CYS B  1 472  ? -16.243 14.839  117.715 1.00 45.74 ? 470  CYS B SG    1 
ATOM   12227 N N     . ARG B  1 473  ? -14.013 12.166  118.179 1.00 39.82 ? 471  ARG B N     1 
ATOM   12228 C CA    . ARG B  1 473  ? -12.605 12.311  118.529 1.00 37.27 ? 471  ARG B CA    1 
ATOM   12229 C C     . ARG B  1 473  ? -12.178 13.737  118.219 1.00 36.26 ? 471  ARG B C     1 
ATOM   12230 O O     . ARG B  1 473  ? -12.316 14.203  117.080 1.00 35.60 ? 471  ARG B O     1 
ATOM   12231 C CB    . ARG B  1 473  ? -11.722 11.314  117.778 1.00 37.17 ? 471  ARG B CB    1 
ATOM   12232 C CG    . ARG B  1 473  ? -10.228 11.412  118.153 1.00 34.19 ? 471  ARG B CG    1 
ATOM   12233 C CD    . ARG B  1 473  ? -9.435  10.253  117.576 1.00 34.19 ? 471  ARG B CD    1 
ATOM   12234 N NE    . ARG B  1 473  ? -10.138 8.981   117.721 1.00 34.57 ? 471  ARG B NE    1 
ATOM   12235 C CZ    . ARG B  1 473  ? -9.992  8.140   118.737 1.00 35.47 ? 471  ARG B CZ    1 
ATOM   12236 N NH1   . ARG B  1 473  ? -9.138  8.381   119.723 1.00 35.16 ? 471  ARG B NH1   1 
ATOM   12237 N NH2   . ARG B  1 473  ? -10.714 7.022   118.759 1.00 39.73 ? 471  ARG B NH2   1 
ATOM   12238 N N     . ILE B  1 474  ? -11.676 14.423  119.234 1.00 36.48 ? 472  ILE B N     1 
ATOM   12239 C CA    . ILE B  1 474  ? -11.237 15.805  119.111 1.00 35.05 ? 472  ILE B CA    1 
ATOM   12240 C C     . ILE B  1 474  ? -9.779  15.812  118.668 1.00 33.74 ? 472  ILE B C     1 
ATOM   12241 O O     . ILE B  1 474  ? -8.915  15.224  119.325 1.00 32.03 ? 472  ILE B O     1 
ATOM   12242 C CB    . ILE B  1 474  ? -11.420 16.553  120.440 1.00 35.76 ? 472  ILE B CB    1 
ATOM   12243 C CG1   . ILE B  1 474  ? -12.898 16.537  120.843 1.00 36.34 ? 472  ILE B CG1   1 
ATOM   12244 C CG2   . ILE B  1 474  ? -10.894 17.971  120.323 1.00 36.22 ? 472  ILE B CG2   1 
ATOM   12245 C CD1   . ILE B  1 474  ? -13.168 16.990  122.269 1.00 38.53 ? 472  ILE B CD1   1 
ATOM   12246 N N     . TYR B  1 475  ? -9.519  16.438  117.528 1.00 33.96 ? 473  TYR B N     1 
ATOM   12247 C CA    . TYR B  1 475  ? -8.165  16.683  117.055 1.00 31.86 ? 473  TYR B CA    1 
ATOM   12248 C C     . TYR B  1 475  ? -7.629  17.876  117.828 1.00 36.04 ? 473  TYR B C     1 
ATOM   12249 O O     . TYR B  1 475  ? -8.159  18.985  117.709 1.00 37.52 ? 473  TYR B O     1 
ATOM   12250 C CB    . TYR B  1 475  ? -8.199  16.944  115.555 1.00 33.88 ? 473  TYR B CB    1 
ATOM   12251 C CG    . TYR B  1 475  ? -6.875  17.081  114.854 1.00 32.95 ? 473  TYR B CG    1 
ATOM   12252 C CD1   . TYR B  1 475  ? -6.264  15.985  114.258 1.00 36.51 ? 473  TYR B CD1   1 
ATOM   12253 C CD2   . TYR B  1 475  ? -6.262  18.323  114.737 1.00 42.65 ? 473  TYR B CD2   1 
ATOM   12254 C CE1   . TYR B  1 475  ? -5.067  16.110  113.585 1.00 36.68 ? 473  TYR B CE1   1 
ATOM   12255 C CE2   . TYR B  1 475  ? -5.052  18.464  114.064 1.00 43.02 ? 473  TYR B CE2   1 
ATOM   12256 C CZ    . TYR B  1 475  ? -4.468  17.347  113.483 1.00 39.72 ? 473  TYR B CZ    1 
ATOM   12257 O OH    . TYR B  1 475  ? -3.272  17.479  112.813 1.00 41.39 ? 473  TYR B OH    1 
ATOM   12258 N N     . ALA B  1 476  ? -6.594  17.650  118.633 1.00 33.68 ? 474  ALA B N     1 
ATOM   12259 C CA    . ALA B  1 476  ? -6.177  18.599  119.665 1.00 32.39 ? 474  ALA B CA    1 
ATOM   12260 C C     . ALA B  1 476  ? -4.767  19.110  119.405 1.00 36.66 ? 474  ALA B C     1 
ATOM   12261 O O     . ALA B  1 476  ? -3.785  18.392  119.669 1.00 31.83 ? 474  ALA B O     1 
ATOM   12262 C CB    . ALA B  1 476  ? -6.261  17.934  121.037 1.00 31.54 ? 474  ALA B CB    1 
ATOM   12263 N N     . PRO B  1 477  ? -4.614  20.332  118.895 1.00 34.78 ? 475  PRO B N     1 
ATOM   12264 C CA    . PRO B  1 477  ? -3.274  20.909  118.750 1.00 34.69 ? 475  PRO B CA    1 
ATOM   12265 C C     . PRO B  1 477  ? -2.588  21.056  120.096 1.00 35.10 ? 475  PRO B C     1 
ATOM   12266 O O     . PRO B  1 477  ? -3.210  21.406  121.100 1.00 34.04 ? 475  PRO B O     1 
ATOM   12267 C CB    . PRO B  1 477  ? -3.546  22.273  118.110 1.00 35.71 ? 475  PRO B CB    1 
ATOM   12268 C CG    . PRO B  1 477  ? -4.875  22.113  117.427 1.00 33.46 ? 475  PRO B CG    1 
ATOM   12269 C CD    . PRO B  1 477  ? -5.654  21.205  118.330 1.00 35.02 ? 475  PRO B CD    1 
ATOM   12270 N N     . VAL B  1 478  ? -1.287  20.789  120.104 1.00 33.23 ? 476  VAL B N     1 
ATOM   12271 C CA    . VAL B  1 478  ? -0.461  20.925  121.294 1.00 33.09 ? 476  VAL B CA    1 
ATOM   12272 C C     . VAL B  1 478  ? 0.813   21.648  120.887 1.00 38.81 ? 476  VAL B C     1 
ATOM   12273 O O     . VAL B  1 478  ? 1.508   21.209  119.964 1.00 37.60 ? 476  VAL B O     1 
ATOM   12274 C CB    . VAL B  1 478  ? -0.130  19.565  121.926 1.00 35.08 ? 476  VAL B CB    1 
ATOM   12275 C CG1   . VAL B  1 478  ? 0.694   19.776  123.169 1.00 34.96 ? 476  VAL B CG1   1 
ATOM   12276 C CG2   . VAL B  1 478  ? -1.421  18.784  122.238 1.00 29.71 ? 476  VAL B CG2   1 
ATOM   12277 N N     . GLY B  1 479  ? 1.112   22.751  121.552 1.00 39.78 ? 477  GLY B N     1 
ATOM   12278 C CA    . GLY B  1 479  ? 2.325   23.468  121.223 1.00 38.65 ? 477  GLY B CA    1 
ATOM   12279 C C     . GLY B  1 479  ? 2.313   24.892  121.724 1.00 43.55 ? 477  GLY B C     1 
ATOM   12280 O O     . GLY B  1 479  ? 1.315   25.403  122.238 1.00 40.75 ? 477  GLY B O     1 
ATOM   12281 N N     . THR B  1 480  ? 3.464   25.532  121.537 1.00 41.62 ? 478  THR B N     1 
ATOM   12282 C CA    . THR B  1 480  ? 3.708   26.903  121.946 1.00 48.04 ? 478  THR B CA    1 
ATOM   12283 C C     . THR B  1 480  ? 2.913   27.881  121.079 1.00 51.19 ? 478  THR B C     1 
ATOM   12284 O O     . THR B  1 480  ? 2.188   27.504  120.150 1.00 51.12 ? 478  THR B O     1 
ATOM   12285 C CB    . THR B  1 480  ? 5.203   27.207  121.854 1.00 46.47 ? 478  THR B CB    1 
ATOM   12286 O OG1   . THR B  1 480  ? 5.647   27.009  120.501 1.00 49.53 ? 478  THR B OG1   1 
ATOM   12287 C CG2   . THR B  1 480  ? 5.983   26.292  122.782 1.00 43.28 ? 478  THR B CG2   1 
ATOM   12288 N N     . HIS B  1 481  ? 3.071   29.170  121.383 1.00 53.89 ? 479  HIS B N     1 
ATOM   12289 C CA    . HIS B  1 481  ? 2.417   30.202  120.583 1.00 53.23 ? 479  HIS B CA    1 
ATOM   12290 C C     . HIS B  1 481  ? 3.083   30.352  119.222 1.00 53.38 ? 479  HIS B C     1 
ATOM   12291 O O     . HIS B  1 481  ? 2.402   30.601  118.220 1.00 56.72 ? 479  HIS B O     1 
ATOM   12292 C CB    . HIS B  1 481  ? 2.424   31.529  121.337 1.00 47.16 ? 479  HIS B CB    1 
ATOM   12293 C CG    . HIS B  1 481  ? 1.678   31.483  122.632 1.00 47.54 ? 479  HIS B CG    1 
ATOM   12294 N ND1   . HIS B  1 481  ? 1.582   32.570  123.476 1.00 49.60 ? 479  HIS B ND1   1 
ATOM   12295 C CD2   . HIS B  1 481  ? 0.989   30.480  123.228 1.00 48.79 ? 479  HIS B CD2   1 
ATOM   12296 C CE1   . HIS B  1 481  ? 0.869   32.237  124.538 1.00 49.97 ? 479  HIS B CE1   1 
ATOM   12297 N NE2   . HIS B  1 481  ? 0.498   30.975  124.413 1.00 52.04 ? 479  HIS B NE2   1 
ATOM   12298 N N     . GLU B  1 482  ? 4.410   30.197  119.163 1.00 55.25 ? 480  GLU B N     1 
ATOM   12299 C CA    . GLU B  1 482  ? 5.116   30.323  117.891 1.00 52.38 ? 480  GLU B CA    1 
ATOM   12300 C C     . GLU B  1 482  ? 4.656   29.267  116.898 1.00 54.67 ? 480  GLU B C     1 
ATOM   12301 O O     . GLU B  1 482  ? 4.429   29.568  115.719 1.00 58.08 ? 480  GLU B O     1 
ATOM   12302 C CB    . GLU B  1 482  ? 6.624   30.227  118.117 1.00 56.39 ? 480  GLU B CB    1 
ATOM   12303 N N     . THR B  1 483  ? 4.511   28.022  117.358 1.00 54.91 ? 481  THR B N     1 
ATOM   12304 C CA    . THR B  1 483  ? 4.044   26.953  116.479 1.00 55.64 ? 481  THR B CA    1 
ATOM   12305 C C     . THR B  1 483  ? 2.598   27.177  116.054 1.00 55.25 ? 481  THR B C     1 
ATOM   12306 O O     . THR B  1 483  ? 2.262   27.011  114.875 1.00 58.23 ? 481  THR B O     1 
ATOM   12307 C CB    . THR B  1 483  ? 4.192   25.595  117.171 1.00 53.56 ? 481  THR B CB    1 
ATOM   12308 N N     . LEU B  1 484  ? 1.730   27.560  116.997 1.00 56.54 ? 482  LEU B N     1 
ATOM   12309 C CA    . LEU B  1 484  ? 0.315   27.745  116.681 1.00 54.22 ? 482  LEU B CA    1 
ATOM   12310 C C     . LEU B  1 484  ? 0.128   28.802  115.599 1.00 54.43 ? 482  LEU B C     1 
ATOM   12311 O O     . LEU B  1 484  ? -0.510  28.551  114.569 1.00 52.98 ? 482  LEU B O     1 
ATOM   12312 C CB    . LEU B  1 484  ? -0.463  28.123  117.944 1.00 50.18 ? 482  LEU B CB    1 
ATOM   12313 N N     . LEU B  1 485  ? 0.696   29.990  115.809 1.00 53.33 ? 483  LEU B N     1 
ATOM   12314 C CA    . LEU B  1 485  ? 0.532   31.073  114.848 1.00 55.33 ? 483  LEU B CA    1 
ATOM   12315 C C     . LEU B  1 485  ? 1.080   30.719  113.469 1.00 54.69 ? 483  LEU B C     1 
ATOM   12316 O O     . LEU B  1 485  ? 0.653   31.318  112.474 1.00 52.02 ? 483  LEU B O     1 
ATOM   12317 C CB    . LEU B  1 485  ? 1.207   32.335  115.385 1.00 52.40 ? 483  LEU B CB    1 
ATOM   12318 C CG    . LEU B  1 485  ? 0.494   32.975  116.576 1.00 49.87 ? 483  LEU B CG    1 
ATOM   12319 C CD1   . LEU B  1 485  ? 1.425   33.916  117.322 1.00 50.92 ? 483  LEU B CD1   1 
ATOM   12320 C CD2   . LEU B  1 485  ? -0.747  33.708  116.102 1.00 46.92 ? 483  LEU B CD2   1 
ATOM   12321 N N     . ALA B  1 486  ? 1.989   29.740  113.387 1.00 51.47 ? 484  ALA B N     1 
ATOM   12322 C CA    . ALA B  1 486  ? 2.633   29.413  112.119 1.00 51.17 ? 484  ALA B CA    1 
ATOM   12323 C C     . ALA B  1 486  ? 1.676   28.766  111.118 1.00 53.36 ? 484  ALA B C     1 
ATOM   12324 O O     . ALA B  1 486  ? 1.892   28.880  109.905 1.00 52.40 ? 484  ALA B O     1 
ATOM   12325 C CB    . ALA B  1 486  ? 3.832   28.500  112.369 1.00 52.86 ? 484  ALA B CB    1 
ATOM   12326 N N     . TYR B  1 487  ? 0.626   28.078  111.588 1.00 51.65 ? 485  TYR B N     1 
ATOM   12327 C CA    . TYR B  1 487  ? -0.306  27.390  110.699 1.00 50.98 ? 485  TYR B CA    1 
ATOM   12328 C C     . TYR B  1 487  ? -1.755  27.748  111.009 1.00 53.80 ? 485  TYR B C     1 
ATOM   12329 O O     . TYR B  1 487  ? -2.675  27.060  110.546 1.00 48.43 ? 485  TYR B O     1 
ATOM   12330 C CB    . TYR B  1 487  ? -0.119  25.868  110.775 1.00 50.70 ? 485  TYR B CB    1 
ATOM   12331 N N     . LEU B  1 488  ? -1.981  28.813  111.781 1.00 54.25 ? 486  LEU B N     1 
ATOM   12332 C CA    . LEU B  1 488  ? -3.345  29.149  112.173 1.00 53.92 ? 486  LEU B CA    1 
ATOM   12333 C C     . LEU B  1 488  ? -4.138  29.737  111.011 1.00 53.65 ? 486  LEU B C     1 
ATOM   12334 O O     . LEU B  1 488  ? -5.361  29.545  110.933 1.00 45.78 ? 486  LEU B O     1 
ATOM   12335 C CB    . LEU B  1 488  ? -3.325  30.115  113.357 1.00 48.51 ? 486  LEU B CB    1 
ATOM   12336 C CG    . LEU B  1 488  ? -4.726  30.319  113.922 1.00 48.90 ? 486  LEU B CG    1 
ATOM   12337 C CD1   . LEU B  1 488  ? -5.383  28.957  114.120 1.00 52.28 ? 486  LEU B CD1   1 
ATOM   12338 C CD2   . LEU B  1 488  ? -4.698  31.118  115.219 1.00 43.54 ? 486  LEU B CD2   1 
ATOM   12339 N N     . VAL B  1 489  ? -3.464  30.449  110.101 1.00 52.77 ? 487  VAL B N     1 
ATOM   12340 C CA    . VAL B  1 489  ? -4.142  30.983  108.921 1.00 50.21 ? 487  VAL B CA    1 
ATOM   12341 C C     . VAL B  1 489  ? -4.875  29.868  108.185 1.00 49.75 ? 487  VAL B C     1 
ATOM   12342 O O     . VAL B  1 489  ? -6.075  29.968  107.907 1.00 56.17 ? 487  VAL B O     1 
ATOM   12343 C CB    . VAL B  1 489  ? -3.136  31.704  108.005 1.00 52.20 ? 487  VAL B CB    1 
ATOM   12344 N N     . ARG B  1 490  ? -4.168  28.770  107.893 1.00 53.73 ? 488  ARG B N     1 
ATOM   12345 C CA    . ARG B  1 490  ? -4.788  27.662  107.169 1.00 53.25 ? 488  ARG B CA    1 
ATOM   12346 C C     . ARG B  1 490  ? -5.916  27.028  107.976 1.00 55.90 ? 488  ARG B C     1 
ATOM   12347 O O     . ARG B  1 490  ? -6.951  26.648  107.414 1.00 54.44 ? 488  ARG B O     1 
ATOM   12348 C CB    . ARG B  1 490  ? -3.741  26.606  106.798 1.00 47.92 ? 488  ARG B CB    1 
ATOM   12349 C CG    . ARG B  1 490  ? -4.301  25.537  105.859 1.00 46.47 ? 488  ARG B CG    1 
ATOM   12350 C CD    . ARG B  1 490  ? -3.250  24.568  105.326 1.00 48.50 ? 488  ARG B CD    1 
ATOM   12351 N NE    . ARG B  1 490  ? -2.828  23.585  106.318 1.00 44.33 ? 488  ARG B NE    1 
ATOM   12352 C CZ    . ARG B  1 490  ? -1.567  23.372  106.667 1.00 50.65 ? 488  ARG B CZ    1 
ATOM   12353 N NH1   . ARG B  1 490  ? -0.573  24.037  106.100 1.00 45.80 ? 488  ARG B NH1   1 
ATOM   12354 N NH2   . ARG B  1 490  ? -1.295  22.466  107.605 1.00 49.44 ? 488  ARG B NH2   1 
ATOM   12355 N N     . ARG B  1 491  ? -5.738  26.908  109.296 1.00 51.20 ? 489  ARG B N     1 
ATOM   12356 C CA    . ARG B  1 491  ? -6.752  26.262  110.121 1.00 52.68 ? 489  ARG B CA    1 
ATOM   12357 C C     . ARG B  1 491  ? -8.035  27.083  110.163 1.00 57.59 ? 489  ARG B C     1 
ATOM   12358 O O     . ARG B  1 491  ? -9.139  26.525  110.112 1.00 55.24 ? 489  ARG B O     1 
ATOM   12359 C CB    . ARG B  1 491  ? -6.212  26.039  111.533 1.00 54.53 ? 489  ARG B CB    1 
ATOM   12360 N N     . LEU B  1 492  ? -7.907  28.411  110.239 1.00 57.78 ? 490  LEU B N     1 
ATOM   12361 C CA    . LEU B  1 492  ? -9.077  29.281  110.343 1.00 58.59 ? 490  LEU B CA    1 
ATOM   12362 C C     . LEU B  1 492  ? -9.841  29.348  109.024 1.00 58.43 ? 490  LEU B C     1 
ATOM   12363 O O     . LEU B  1 492  ? -11.068 29.191  108.997 1.00 55.05 ? 490  LEU B O     1 
ATOM   12364 C CB    . LEU B  1 492  ? -8.640  30.677  110.785 1.00 53.64 ? 490  LEU B CB    1 
ATOM   12365 C CG    . LEU B  1 492  ? -8.005  30.732  112.171 1.00 54.12 ? 490  LEU B CG    1 
ATOM   12366 C CD1   . LEU B  1 492  ? -7.369  32.095  112.428 1.00 51.78 ? 490  LEU B CD1   1 
ATOM   12367 C CD2   . LEU B  1 492  ? -9.062  30.410  113.224 1.00 53.39 ? 490  LEU B CD2   1 
ATOM   12368 N N     . LEU B  1 493  ? -9.134  29.599  107.925 1.00 61.10 ? 491  LEU B N     1 
ATOM   12369 C CA    . LEU B  1 493  ? -9.748  29.662  106.604 1.00 56.01 ? 491  LEU B CA    1 
ATOM   12370 C C     . LEU B  1 493  ? -10.572 28.419  106.300 1.00 58.27 ? 491  LEU B C     1 
ATOM   12371 O O     . LEU B  1 493  ? -11.523 28.477  105.525 1.00 63.20 ? 491  LEU B O     1 
ATOM   12372 C CB    . LEU B  1 493  ? -8.683  29.839  105.530 1.00 53.81 ? 491  LEU B CB    1 
ATOM   12373 C CG    . LEU B  1 493  ? -8.426  31.265  105.073 1.00 55.59 ? 491  LEU B CG    1 
ATOM   12374 C CD1   . LEU B  1 493  ? -7.560  31.224  103.821 1.00 55.12 ? 491  LEU B CD1   1 
ATOM   12375 C CD2   . LEU B  1 493  ? -9.744  32.003  104.831 1.00 54.03 ? 491  LEU B CD2   1 
ATOM   12376 N N     . GLY B  1 496  ? -13.364 29.538  107.874 1.00 58.52 ? 494  GLY B N     1 
ATOM   12377 C CA    . GLY B  1 496  ? -13.451 30.987  107.914 1.00 57.30 ? 494  GLY B CA    1 
ATOM   12378 C C     . GLY B  1 496  ? -13.797 31.658  106.592 1.00 62.39 ? 494  GLY B C     1 
ATOM   12379 O O     . GLY B  1 496  ? -14.317 32.775  106.585 1.00 62.52 ? 494  GLY B O     1 
ATOM   12380 N N     . ALA B  1 497  ? -13.501 30.989  105.476 1.00 61.63 ? 495  ALA B N     1 
ATOM   12381 C CA    . ALA B  1 497  ? -13.851 31.516  104.163 1.00 58.43 ? 495  ALA B CA    1 
ATOM   12382 C C     . ALA B  1 497  ? -15.367 31.533  103.979 1.00 53.91 ? 495  ALA B C     1 
ATOM   12383 O O     . ALA B  1 497  ? -16.108 30.791  104.630 1.00 58.04 ? 495  ALA B O     1 
ATOM   12384 C CB    . ALA B  1 497  ? -13.196 30.692  103.055 1.00 52.40 ? 495  ALA B CB    1 
ATOM   12385 N N     . ASN B  1 498  ? -15.822 32.385  103.055 1.00 55.43 ? 496  ASN B N     1 
ATOM   12386 C CA    . ASN B  1 498  ? -17.250 32.679  102.942 1.00 53.89 ? 496  ASN B CA    1 
ATOM   12387 C C     . ASN B  1 498  ? -18.072 31.418  102.701 1.00 52.51 ? 496  ASN B C     1 
ATOM   12388 O O     . ASN B  1 498  ? -19.156 31.259  103.273 1.00 51.91 ? 496  ASN B O     1 
ATOM   12389 C CB    . ASN B  1 498  ? -17.491 33.696  101.827 1.00 51.16 ? 496  ASN B CB    1 
ATOM   12390 N N     . SER B  1 499  ? -17.574 30.507  101.869 1.00 49.05 ? 497  SER B N     1 
ATOM   12391 C CA    . SER B  1 499  ? -18.317 29.296  101.542 1.00 47.24 ? 497  SER B CA    1 
ATOM   12392 C C     . SER B  1 499  ? -18.279 28.238  102.642 1.00 47.79 ? 497  SER B C     1 
ATOM   12393 O O     . SER B  1 499  ? -18.940 27.204  102.504 1.00 41.99 ? 497  SER B O     1 
ATOM   12394 C CB    . SER B  1 499  ? -17.772 28.683  100.255 1.00 45.64 ? 497  SER B CB    1 
ATOM   12395 O OG    . SER B  1 499  ? -16.440 28.246  100.458 1.00 44.55 ? 497  SER B OG    1 
ATOM   12396 N N     . SER B  1 500  ? -17.512 28.443  103.707 1.00 49.49 ? 498  SER B N     1 
ATOM   12397 C CA    . SER B  1 500  ? -17.398 27.416  104.729 1.00 49.12 ? 498  SER B CA    1 
ATOM   12398 C C     . SER B  1 500  ? -18.552 27.512  105.722 1.00 50.85 ? 498  SER B C     1 
ATOM   12399 O O     . SER B  1 500  ? -19.068 28.597  106.005 1.00 50.38 ? 498  SER B O     1 
ATOM   12400 C CB    . SER B  1 500  ? -16.062 27.528  105.464 1.00 49.58 ? 498  SER B CB    1 
ATOM   12401 O OG    . SER B  1 500  ? -16.036 28.683  106.280 1.00 55.12 ? 498  SER B OG    1 
ATOM   12402 N N     . PHE B  1 501  ? -18.960 26.353  106.246 1.00 45.67 ? 499  PHE B N     1 
ATOM   12403 C CA    . PHE B  1 501  ? -20.065 26.323  107.201 1.00 50.44 ? 499  PHE B CA    1 
ATOM   12404 C C     . PHE B  1 501  ? -19.731 27.122  108.455 1.00 53.23 ? 499  PHE B C     1 
ATOM   12405 O O     . PHE B  1 501  ? -20.599 27.804  109.014 1.00 55.42 ? 499  PHE B O     1 
ATOM   12406 C CB    . PHE B  1 501  ? -20.410 24.879  107.564 1.00 45.81 ? 499  PHE B CB    1 
ATOM   12407 N N     . VAL B  1 502  ? -18.470 27.073  108.894 1.00 53.65 ? 500  VAL B N     1 
ATOM   12408 C CA    . VAL B  1 502  ? -18.075 27.715  110.143 1.00 58.36 ? 500  VAL B CA    1 
ATOM   12409 C C     . VAL B  1 502  ? -18.112 29.236  110.047 1.00 58.97 ? 500  VAL B C     1 
ATOM   12410 O O     . VAL B  1 502  ? -18.097 29.914  111.080 1.00 61.73 ? 500  VAL B O     1 
ATOM   12411 C CB    . VAL B  1 502  ? -16.677 27.233  110.573 1.00 58.62 ? 500  VAL B CB    1 
ATOM   12412 N N     . HIS B  1 503  ? -18.136 29.796  108.837 1.00 55.69 ? 501  HIS B N     1 
ATOM   12413 C CA    . HIS B  1 503  ? -18.431 31.212  108.658 1.00 54.68 ? 501  HIS B CA    1 
ATOM   12414 C C     . HIS B  1 503  ? -19.893 31.475  108.308 1.00 56.27 ? 501  HIS B C     1 
ATOM   12415 O O     . HIS B  1 503  ? -20.393 32.575  108.574 1.00 59.48 ? 501  HIS B O     1 
ATOM   12416 C CB    . HIS B  1 503  ? -17.532 31.812  107.568 1.00 54.39 ? 501  HIS B CB    1 
ATOM   12417 N N     . ARG B  1 504  ? -20.595 30.481  107.754 1.00 50.97 ? 502  ARG B N     1 
ATOM   12418 C CA    . ARG B  1 504  ? -21.971 30.670  107.311 1.00 51.03 ? 502  ARG B CA    1 
ATOM   12419 C C     . ARG B  1 504  ? -22.965 30.587  108.465 1.00 54.29 ? 502  ARG B C     1 
ATOM   12420 O O     . ARG B  1 504  ? -23.968 31.310  108.475 1.00 54.69 ? 502  ARG B O     1 
ATOM   12421 C CB    . ARG B  1 504  ? -22.316 29.634  106.243 1.00 45.12 ? 502  ARG B CB    1 
ATOM   12422 C CG    . ARG B  1 504  ? -21.679 29.921  104.894 1.00 49.58 ? 502  ARG B CG    1 
ATOM   12423 C CD    . ARG B  1 504  ? -21.730 28.700  103.980 1.00 47.24 ? 502  ARG B CD    1 
ATOM   12424 N NE    . ARG B  1 504  ? -23.086 28.210  103.772 1.00 42.93 ? 502  ARG B NE    1 
ATOM   12425 C CZ    . ARG B  1 504  ? -23.945 28.731  102.907 1.00 48.13 ? 502  ARG B CZ    1 
ATOM   12426 N NH1   . ARG B  1 504  ? -23.645 29.808  102.200 1.00 53.33 ? 502  ARG B NH1   1 
ATOM   12427 N NH2   . ARG B  1 504  ? -25.134 28.157  102.748 1.00 50.07 ? 502  ARG B NH2   1 
ATOM   12428 N N     . ILE B  1 505  ? -22.719 29.704  109.435 1.00 53.75 ? 503  ILE B N     1 
ATOM   12429 C CA    . ILE B  1 505  ? -23.601 29.611  110.590 1.00 51.69 ? 503  ILE B CA    1 
ATOM   12430 C C     . ILE B  1 505  ? -23.625 30.922  111.364 1.00 54.49 ? 503  ILE B C     1 
ATOM   12431 O O     . ILE B  1 505  ? -24.574 31.186  112.112 1.00 51.95 ? 503  ILE B O     1 
ATOM   12432 C CB    . ILE B  1 505  ? -23.178 28.435  111.492 1.00 54.02 ? 503  ILE B CB    1 
ATOM   12433 N N     . ASN B  1 506  ? -22.604 31.758  111.192 1.00 56.67 ? 504  ASN B N     1 
ATOM   12434 C CA    . ASN B  1 506  ? -22.536 33.076  111.803 1.00 57.09 ? 504  ASN B CA    1 
ATOM   12435 C C     . ASN B  1 506  ? -22.983 34.186  110.859 1.00 60.13 ? 504  ASN B C     1 
ATOM   12436 O O     . ASN B  1 506  ? -22.931 35.361  111.234 1.00 61.35 ? 504  ASN B O     1 
ATOM   12437 C CB    . ASN B  1 506  ? -21.112 33.355  112.298 1.00 55.95 ? 504  ASN B CB    1 
ATOM   12438 N N     . ASP B  1 507  ? -23.400 33.851  109.640 1.00 57.67 ? 505  ASP B N     1 
ATOM   12439 C CA    . ASP B  1 507  ? -23.988 34.838  108.745 1.00 59.73 ? 505  ASP B CA    1 
ATOM   12440 C C     . ASP B  1 507  ? -25.493 34.825  108.965 1.00 61.79 ? 505  ASP B C     1 
ATOM   12441 O O     . ASP B  1 507  ? -26.144 33.814  108.654 1.00 62.23 ? 505  ASP B O     1 
ATOM   12442 C CB    . ASP B  1 507  ? -23.653 34.531  107.293 1.00 55.85 ? 505  ASP B CB    1 
ATOM   12443 N N     . PRO B  1 508  ? -26.083 35.888  109.519 1.00 64.53 ? 506  PRO B N     1 
ATOM   12444 C CA    . PRO B  1 508  ? -27.532 35.871  109.774 1.00 62.04 ? 506  PRO B CA    1 
ATOM   12445 C C     . PRO B  1 508  ? -28.357 35.799  108.507 1.00 64.35 ? 506  PRO B C     1 
ATOM   12446 O O     . PRO B  1 508  ? -29.536 35.427  108.575 1.00 65.34 ? 506  PRO B O     1 
ATOM   12447 C CB    . PRO B  1 508  ? -27.778 37.190  110.524 1.00 64.69 ? 506  PRO B CB    1 
ATOM   12448 C CG    . PRO B  1 508  ? -26.418 37.670  110.954 1.00 61.79 ? 506  PRO B CG    1 
ATOM   12449 C CD    . PRO B  1 508  ? -25.462 37.157  109.931 1.00 61.64 ? 506  PRO B CD    1 
ATOM   12450 N N     . LYS B  1 509  ? -27.775 36.146  107.353 1.00 61.97 ? 507  LYS B N     1 
ATOM   12451 C CA    . LYS B  1 509  ? -28.505 36.068  106.094 1.00 65.88 ? 507  LYS B CA    1 
ATOM   12452 C C     . LYS B  1 509  ? -28.715 34.625  105.647 1.00 68.25 ? 507  LYS B C     1 
ATOM   12453 O O     . LYS B  1 509  ? -29.740 34.314  105.030 1.00 66.03 ? 507  LYS B O     1 
ATOM   12454 C CB    . LYS B  1 509  ? -27.768 36.860  105.013 1.00 57.30 ? 507  LYS B CB    1 
ATOM   12455 N N     . VAL B  1 510  ? -27.770 33.733  105.941 1.00 63.87 ? 508  VAL B N     1 
ATOM   12456 C CA    . VAL B  1 510  ? -27.919 32.339  105.535 1.00 60.74 ? 508  VAL B CA    1 
ATOM   12457 C C     . VAL B  1 510  ? -28.993 31.691  106.398 1.00 61.49 ? 508  VAL B C     1 
ATOM   12458 O O     . VAL B  1 510  ? -28.858 31.602  107.623 1.00 61.22 ? 508  VAL B O     1 
ATOM   12459 C CB    . VAL B  1 510  ? -26.588 31.585  105.636 1.00 54.91 ? 508  VAL B CB    1 
ATOM   12460 N N     . SER B  1 511  ? -30.068 31.244  105.760 1.00 60.07 ? 509  SER B N     1 
ATOM   12461 C CA    . SER B  1 511  ? -31.153 30.578  106.455 1.00 60.72 ? 509  SER B CA    1 
ATOM   12462 C C     . SER B  1 511  ? -30.755 29.157  106.829 1.00 59.73 ? 509  SER B C     1 
ATOM   12463 O O     . SER B  1 511  ? -29.834 28.570  106.255 1.00 62.64 ? 509  SER B O     1 
ATOM   12464 C CB    . SER B  1 511  ? -32.408 30.544  105.583 1.00 58.74 ? 509  SER B CB    1 
ATOM   12465 N N     . ILE B  1 512  ? -31.469 28.599  107.807 1.00 58.42 ? 510  ILE B N     1 
ATOM   12466 C CA    . ILE B  1 512  ? -31.297 27.184  108.114 1.00 61.50 ? 510  ILE B CA    1 
ATOM   12467 C C     . ILE B  1 512  ? -31.644 26.340  106.895 1.00 62.18 ? 510  ILE B C     1 
ATOM   12468 O O     . ILE B  1 512  ? -31.000 25.320  106.626 1.00 61.28 ? 510  ILE B O     1 
ATOM   12469 C CB    . ILE B  1 512  ? -32.134 26.789  109.347 1.00 58.61 ? 510  ILE B CB    1 
ATOM   12470 C CG1   . ILE B  1 512  ? -31.552 27.431  110.607 1.00 58.32 ? 510  ILE B CG1   1 
ATOM   12471 C CG2   . ILE B  1 512  ? -32.208 25.267  109.501 1.00 56.64 ? 510  ILE B CG2   1 
ATOM   12472 C CD1   . ILE B  1 512  ? -32.014 26.782  111.895 1.00 55.00 ? 510  ILE B CD1   1 
ATOM   12473 N N     . ASP B  1 513  ? -32.650 26.767  106.123 1.00 61.23 ? 511  ASP B N     1 
ATOM   12474 C CA    . ASP B  1 513  ? -32.996 26.050  104.899 1.00 59.77 ? 511  ASP B CA    1 
ATOM   12475 C C     . ASP B  1 513  ? -31.820 26.017  103.928 1.00 58.19 ? 511  ASP B C     1 
ATOM   12476 O O     . ASP B  1 513  ? -31.569 24.990  103.288 1.00 57.13 ? 511  ASP B O     1 
ATOM   12477 C CB    . ASP B  1 513  ? -34.223 26.684  104.236 1.00 60.16 ? 511  ASP B CB    1 
ATOM   12478 C CG    . ASP B  1 513  ? -35.540 26.212  104.844 1.00 62.87 ? 511  ASP B CG    1 
ATOM   12479 O OD1   . ASP B  1 513  ? -35.521 25.398  105.792 1.00 70.31 ? 511  ASP B OD1   1 
ATOM   12480 O OD2   . ASP B  1 513  ? -36.605 26.655  104.365 1.00 64.40 ? 511  ASP B OD2   1 
ATOM   12481 N N     . GLU B  1 514  ? -31.084 27.128  103.809 1.00 54.78 ? 512  GLU B N     1 
ATOM   12482 C CA    . GLU B  1 514  ? -29.921 27.152  102.925 1.00 58.34 ? 512  GLU B CA    1 
ATOM   12483 C C     . GLU B  1 514  ? -28.832 26.202  103.418 1.00 58.67 ? 512  GLU B C     1 
ATOM   12484 O O     . GLU B  1 514  ? -28.228 25.472  102.624 1.00 54.05 ? 512  GLU B O     1 
ATOM   12485 C CB    . GLU B  1 514  ? -29.379 28.578  102.803 1.00 56.53 ? 512  GLU B CB    1 
ATOM   12486 N N     . LEU B  1 515  ? -28.589 26.178  104.733 1.00 59.65 ? 513  LEU B N     1 
ATOM   12487 C CA    . LEU B  1 515  ? -27.545 25.326  105.298 1.00 52.91 ? 513  LEU B CA    1 
ATOM   12488 C C     . LEU B  1 515  ? -27.886 23.841  105.202 1.00 54.01 ? 513  LEU B C     1 
ATOM   12489 O O     . LEU B  1 515  ? -26.979 23.015  105.052 1.00 53.10 ? 513  LEU B O     1 
ATOM   12490 C CB    . LEU B  1 515  ? -27.298 25.707  106.760 1.00 51.18 ? 513  LEU B CB    1 
ATOM   12491 C CG    . LEU B  1 515  ? -26.884 27.151  107.052 1.00 52.65 ? 513  LEU B CG    1 
ATOM   12492 C CD1   . LEU B  1 515  ? -26.993 27.432  108.546 1.00 56.70 ? 513  LEU B CD1   1 
ATOM   12493 C CD2   . LEU B  1 515  ? -25.471 27.442  106.552 1.00 48.78 ? 513  LEU B CD2   1 
ATOM   12494 N N     . ILE B  1 516  ? -29.169 23.477  105.289 1.00 51.59 ? 514  ILE B N     1 
ATOM   12495 C CA    . ILE B  1 516  ? -29.562 22.069  105.293 1.00 50.75 ? 514  ILE B CA    1 
ATOM   12496 C C     . ILE B  1 516  ? -29.879 21.589  103.881 1.00 48.88 ? 514  ILE B C     1 
ATOM   12497 O O     . ILE B  1 516  ? -30.401 20.483  103.697 1.00 49.68 ? 514  ILE B O     1 
ATOM   12498 C CB    . ILE B  1 516  ? -30.761 21.815  106.228 1.00 53.54 ? 514  ILE B CB    1 
ATOM   12499 C CG1   . ILE B  1 516  ? -32.021 22.518  105.701 1.00 53.60 ? 514  ILE B CG1   1 
ATOM   12500 C CG2   . ILE B  1 516  ? -30.430 22.236  107.653 1.00 51.90 ? 514  ILE B CG2   1 
ATOM   12501 C CD1   . ILE B  1 516  ? -33.257 22.322  106.576 1.00 55.62 ? 514  ILE B CD1   1 
ATOM   12502 N N     . ALA B  1 517  ? -29.578 22.415  102.881 1.00 50.67 ? 515  ALA B N     1 
ATOM   12503 C CA    . ALA B  1 517  ? -29.723 21.991  101.492 1.00 49.19 ? 515  ALA B CA    1 
ATOM   12504 C C     . ALA B  1 517  ? -28.872 20.754  101.222 1.00 49.59 ? 515  ALA B C     1 
ATOM   12505 O O     . ALA B  1 517  ? -27.703 20.692  101.617 1.00 49.97 ? 515  ALA B O     1 
ATOM   12506 C CB    . ALA B  1 517  ? -29.324 23.122  100.547 1.00 47.25 ? 515  ALA B CB    1 
ATOM   12507 N N     . ASP B  1 518  ? -29.471 19.763  100.559 1.00 48.01 ? 516  ASP B N     1 
ATOM   12508 C CA    . ASP B  1 518  ? -28.820 18.499  100.241 1.00 43.82 ? 516  ASP B CA    1 
ATOM   12509 C C     . ASP B  1 518  ? -27.921 18.696  99.025  1.00 45.70 ? 516  ASP B C     1 
ATOM   12510 O O     . ASP B  1 518  ? -28.418 18.895  97.910  1.00 47.33 ? 516  ASP B O     1 
ATOM   12511 C CB    . ASP B  1 518  ? -29.874 17.414  99.990  1.00 48.17 ? 516  ASP B CB    1 
ATOM   12512 C CG    . ASP B  1 518  ? -29.268 16.050  99.702  1.00 49.75 ? 516  ASP B CG    1 
ATOM   12513 O OD1   . ASP B  1 518  ? -28.028 15.945  99.563  1.00 44.47 ? 516  ASP B OD1   1 
ATOM   12514 O OD2   . ASP B  1 518  ? -30.041 15.069  99.612  1.00 50.38 ? 516  ASP B OD2   1 
ATOM   12515 N N     . PRO B  1 519  ? -26.598 18.642  99.192  1.00 42.05 ? 517  PRO B N     1 
ATOM   12516 C CA    . PRO B  1 519  ? -25.713 18.854  98.036  1.00 41.09 ? 517  PRO B CA    1 
ATOM   12517 C C     . PRO B  1 519  ? -25.916 17.829  96.938  1.00 41.64 ? 517  PRO B C     1 
ATOM   12518 O O     . PRO B  1 519  ? -25.791 18.170  95.758  1.00 41.11 ? 517  PRO B O     1 
ATOM   12519 C CB    . PRO B  1 519  ? -24.302 18.766  98.646  1.00 40.57 ? 517  PRO B CB    1 
ATOM   12520 C CG    . PRO B  1 519  ? -24.481 18.011  99.939  1.00 41.63 ? 517  PRO B CG    1 
ATOM   12521 C CD    . PRO B  1 519  ? -25.848 18.393  100.437 1.00 44.50 ? 517  PRO B CD    1 
ATOM   12522 N N     . VAL B  1 520  ? -26.242 16.587  97.291  1.00 38.08 ? 518  VAL B N     1 
ATOM   12523 C CA    . VAL B  1 520  ? -26.401 15.541  96.285  1.00 43.19 ? 518  VAL B CA    1 
ATOM   12524 C C     . VAL B  1 520  ? -27.522 15.896  95.317  1.00 46.42 ? 518  VAL B C     1 
ATOM   12525 O O     . VAL B  1 520  ? -27.373 15.771  94.092  1.00 45.56 ? 518  VAL B O     1 
ATOM   12526 C CB    . VAL B  1 520  ? -26.651 14.187  96.971  1.00 45.94 ? 518  VAL B CB    1 
ATOM   12527 C CG1   . VAL B  1 520  ? -26.783 13.083  95.937  1.00 46.89 ? 518  VAL B CG1   1 
ATOM   12528 C CG2   . VAL B  1 520  ? -25.525 13.895  97.954  1.00 40.90 ? 518  VAL B CG2   1 
ATOM   12529 N N     . GLU B  1 521  ? -28.650 16.371  95.845  1.00 45.93 ? 519  GLU B N     1 
ATOM   12530 C CA    . GLU B  1 521  ? -29.770 16.737  94.987  1.00 45.95 ? 519  GLU B CA    1 
ATOM   12531 C C     . GLU B  1 521  ? -29.533 18.049  94.252  1.00 47.09 ? 519  GLU B C     1 
ATOM   12532 O O     . GLU B  1 521  ? -30.025 18.220  93.130  1.00 45.89 ? 519  GLU B O     1 
ATOM   12533 C CB    . GLU B  1 521  ? -31.059 16.817  95.807  1.00 46.73 ? 519  GLU B CB    1 
ATOM   12534 C CG    . GLU B  1 521  ? -31.383 15.536  96.554  1.00 47.10 ? 519  GLU B CG    1 
ATOM   12535 C CD    . GLU B  1 521  ? -31.451 14.321  95.641  1.00 51.82 ? 519  GLU B CD    1 
ATOM   12536 O OE1   . GLU B  1 521  ? -31.806 14.479  94.454  1.00 52.95 ? 519  GLU B OE1   1 
ATOM   12537 O OE2   . GLU B  1 521  ? -31.146 13.203  96.114  1.00 53.75 ? 519  GLU B OE2   1 
ATOM   12538 N N     . VAL B  1 522  ? -28.789 18.984  94.843  1.00 46.62 ? 520  VAL B N     1 
ATOM   12539 C CA    . VAL B  1 522  ? -28.499 20.215  94.119  1.00 44.00 ? 520  VAL B CA    1 
ATOM   12540 C C     . VAL B  1 522  ? -27.594 19.926  92.926  1.00 46.68 ? 520  VAL B C     1 
ATOM   12541 O O     . VAL B  1 522  ? -27.815 20.446  91.828  1.00 45.35 ? 520  VAL B O     1 
ATOM   12542 C CB    . VAL B  1 522  ? -27.887 21.274  95.055  1.00 44.07 ? 520  VAL B CB    1 
ATOM   12543 C CG1   . VAL B  1 522  ? -27.631 22.567  94.292  1.00 41.27 ? 520  VAL B CG1   1 
ATOM   12544 C CG2   . VAL B  1 522  ? -28.803 21.531  96.254  1.00 47.72 ? 520  VAL B CG2   1 
ATOM   12545 N N     . VAL B  1 523  ? -26.577 19.078  93.113  1.00 43.43 ? 521  VAL B N     1 
ATOM   12546 C CA    . VAL B  1 523  ? -25.708 18.713  91.995  1.00 42.92 ? 521  VAL B CA    1 
ATOM   12547 C C     . VAL B  1 523  ? -26.489 17.952  90.933  1.00 45.42 ? 521  VAL B C     1 
ATOM   12548 O O     . VAL B  1 523  ? -26.308 18.177  89.731  1.00 46.11 ? 521  VAL B O     1 
ATOM   12549 C CB    . VAL B  1 523  ? -24.505 17.893  92.491  1.00 43.89 ? 521  VAL B CB    1 
ATOM   12550 C CG1   . VAL B  1 523  ? -23.771 17.270  91.314  1.00 40.05 ? 521  VAL B CG1   1 
ATOM   12551 C CG2   . VAL B  1 523  ? -23.573 18.766  93.302  1.00 40.52 ? 521  VAL B CG2   1 
ATOM   12552 N N     . ARG B  1 524  ? -27.357 17.032  91.359  1.00 44.58 ? 522  ARG B N     1 
ATOM   12553 C CA    . ARG B  1 524  ? -28.070 16.172  90.418  1.00 47.96 ? 522  ARG B CA    1 
ATOM   12554 C C     . ARG B  1 524  ? -28.954 16.977  89.474  1.00 48.22 ? 522  ARG B C     1 
ATOM   12555 O O     . ARG B  1 524  ? -29.189 16.559  88.333  1.00 51.29 ? 522  ARG B O     1 
ATOM   12556 C CB    . ARG B  1 524  ? -28.910 15.147  91.187  1.00 46.69 ? 522  ARG B CB    1 
ATOM   12557 C CG    . ARG B  1 524  ? -29.546 14.061  90.320  1.00 46.37 ? 522  ARG B CG    1 
ATOM   12558 C CD    . ARG B  1 524  ? -30.730 13.388  91.004  1.00 50.50 ? 522  ARG B CD    1 
ATOM   12559 N NE    . ARG B  1 524  ? -30.368 12.793  92.284  1.00 48.68 ? 522  ARG B NE    1 
ATOM   12560 C CZ    . ARG B  1 524  ? -29.720 11.644  92.425  1.00 52.21 ? 522  ARG B CZ    1 
ATOM   12561 N NH1   . ARG B  1 524  ? -29.358 10.917  91.379  1.00 50.78 ? 522  ARG B NH1   1 
ATOM   12562 N NH2   . ARG B  1 524  ? -29.417 11.216  93.648  1.00 52.23 ? 522  ARG B NH2   1 
ATOM   12563 N N     . ALA B  1 525  ? -29.442 18.131  89.919  1.00 46.68 ? 523  ALA B N     1 
ATOM   12564 C CA    . ALA B  1 525  ? -30.365 18.929  89.127  1.00 47.89 ? 523  ALA B CA    1 
ATOM   12565 C C     . ALA B  1 525  ? -29.670 19.966  88.257  1.00 48.79 ? 523  ALA B C     1 
ATOM   12566 O O     . ALA B  1 525  ? -30.342 20.651  87.484  1.00 47.90 ? 523  ALA B O     1 
ATOM   12567 C CB    . ALA B  1 525  ? -31.382 19.627  90.040  1.00 48.83 ? 523  ALA B CB    1 
ATOM   12568 N N     . MET B  1 526  ? -28.354 20.101  88.358  1.00 45.39 ? 524  MET B N     1 
ATOM   12569 C CA    A MET B  1 526  ? -27.656 21.076  87.542  0.45 46.99 ? 524  MET B CA    1 
ATOM   12570 C CA    B MET B  1 526  ? -27.639 21.068  87.542  0.55 46.99 ? 524  MET B CA    1 
ATOM   12571 C C     . MET B  1 526  ? -27.749 20.694  86.064  1.00 48.43 ? 524  MET B C     1 
ATOM   12572 O O     . MET B  1 526  ? -27.904 19.518  85.725  1.00 45.67 ? 524  MET B O     1 
ATOM   12573 C CB    A MET B  1 526  ? -26.199 21.185  87.977  0.45 45.96 ? 524  MET B CB    1 
ATOM   12574 C CB    B MET B  1 526  ? -26.172 21.136  87.961  0.55 45.95 ? 524  MET B CB    1 
ATOM   12575 C CG    A MET B  1 526  ? -26.061 21.607  89.426  0.45 47.10 ? 524  MET B CG    1 
ATOM   12576 C CG    B MET B  1 526  ? -25.956 21.793  89.309  0.55 47.10 ? 524  MET B CG    1 
ATOM   12577 S SD    A MET B  1 526  ? -24.433 22.227  89.874  0.45 45.31 ? 524  MET B SD    1 
ATOM   12578 S SD    B MET B  1 526  ? -26.579 23.486  89.354  0.55 47.50 ? 524  MET B SD    1 
ATOM   12579 C CE    A MET B  1 526  ? -24.693 22.574  91.610  0.45 43.33 ? 524  MET B CE    1 
ATOM   12580 C CE    B MET B  1 526  ? -25.456 24.305  88.223  0.55 46.26 ? 524  MET B CE    1 
ATOM   12581 N N     . PRO B  1 527  ? -27.681 21.679  85.159  1.00 48.63 ? 525  PRO B N     1 
ATOM   12582 C CA    . PRO B  1 527  ? -27.789 21.353  83.726  1.00 51.13 ? 525  PRO B CA    1 
ATOM   12583 C C     . PRO B  1 527  ? -26.628 20.515  83.217  1.00 45.37 ? 525  PRO B C     1 
ATOM   12584 O O     . PRO B  1 527  ? -26.819 19.667  82.337  1.00 42.78 ? 525  PRO B O     1 
ATOM   12585 C CB    . PRO B  1 527  ? -27.833 22.734  83.054  1.00 47.45 ? 525  PRO B CB    1 
ATOM   12586 C CG    . PRO B  1 527  ? -27.133 23.636  84.017  1.00 49.58 ? 525  PRO B CG    1 
ATOM   12587 C CD    . PRO B  1 527  ? -27.509 23.125  85.383  1.00 49.41 ? 525  PRO B CD    1 
ATOM   12588 N N     . VAL B  1 528  ? -25.429 20.730  83.737  1.00 42.96 ? 526  VAL B N     1 
ATOM   12589 C CA    . VAL B  1 528  ? -24.274 19.895  83.442  1.00 41.16 ? 526  VAL B CA    1 
ATOM   12590 C C     . VAL B  1 528  ? -23.756 19.403  84.783  1.00 36.57 ? 526  VAL B C     1 
ATOM   12591 O O     . VAL B  1 528  ? -23.206 20.187  85.565  1.00 39.17 ? 526  VAL B O     1 
ATOM   12592 C CB    . VAL B  1 528  ? -23.190 20.660  82.672  1.00 40.22 ? 526  VAL B CB    1 
ATOM   12593 C CG1   . VAL B  1 528  ? -21.890 19.849  82.604  1.00 39.33 ? 526  VAL B CG1   1 
ATOM   12594 C CG2   . VAL B  1 528  ? -23.682 21.025  81.273  1.00 40.22 ? 526  VAL B CG2   1 
ATOM   12595 N N     . VAL B  1 529  ? -23.946 18.118  85.063  1.00 34.35 ? 527  VAL B N     1 
ATOM   12596 C CA    . VAL B  1 529  ? -23.467 17.583  86.329  1.00 35.02 ? 527  VAL B CA    1 
ATOM   12597 C C     . VAL B  1 529  ? -21.949 17.681  86.366  1.00 34.36 ? 527  VAL B C     1 
ATOM   12598 O O     . VAL B  1 529  ? -21.255 17.251  85.436  1.00 34.91 ? 527  VAL B O     1 
ATOM   12599 C CB    . VAL B  1 529  ? -23.946 16.140  86.525  1.00 38.31 ? 527  VAL B CB    1 
ATOM   12600 C CG1   . VAL B  1 529  ? -23.340 15.570  87.792  1.00 38.28 ? 527  VAL B CG1   1 
ATOM   12601 C CG2   . VAL B  1 529  ? -25.476 16.084  86.586  1.00 38.46 ? 527  VAL B CG2   1 
ATOM   12602 N N     . GLY B  1 530  ? -21.427 18.282  87.432  1.00 32.63 ? 528  GLY B N     1 
ATOM   12603 C CA    . GLY B  1 530  ? -19.997 18.364  87.616  1.00 32.64 ? 528  GLY B CA    1 
ATOM   12604 C C     . GLY B  1 530  ? -19.283 19.437  86.831  1.00 29.88 ? 528  GLY B C     1 
ATOM   12605 O O     . GLY B  1 530  ? -18.053 19.385  86.740  1.00 30.11 ? 528  GLY B O     1 
ATOM   12606 N N     . ALA B  1 531  ? -19.996 20.414  86.267  1.00 26.21 ? 529  ALA B N     1 
ATOM   12607 C CA    . ALA B  1 531  ? -19.318 21.509  85.590  1.00 28.28 ? 529  ALA B CA    1 
ATOM   12608 C C     . ALA B  1 531  ? -18.336 22.192  86.533  1.00 30.19 ? 529  ALA B C     1 
ATOM   12609 O O     . ALA B  1 531  ? -18.635 22.410  87.711  1.00 31.63 ? 529  ALA B O     1 
ATOM   12610 C CB    . ALA B  1 531  ? -20.326 22.527  85.064  1.00 33.05 ? 529  ALA B CB    1 
ATOM   12611 N N     . LYS B  1 532  ? -17.145 22.491  86.008  1.00 23.75 ? 530  LYS B N     1 
ATOM   12612 C CA    . LYS B  1 532  ? -16.145 23.276  86.722  1.00 27.64 ? 530  LYS B CA    1 
ATOM   12613 C C     . LYS B  1 532  ? -16.724 24.621  87.141  1.00 29.16 ? 530  LYS B C     1 
ATOM   12614 O O     . LYS B  1 532  ? -17.632 25.151  86.501  1.00 28.06 ? 530  LYS B O     1 
ATOM   12615 C CB    . LYS B  1 532  ? -14.919 23.495  85.823  1.00 29.39 ? 530  LYS B CB    1 
ATOM   12616 C CG    . LYS B  1 532  ? -13.886 24.479  86.347  1.00 31.48 ? 530  LYS B CG    1 
ATOM   12617 C CD    . LYS B  1 532  ? -12.780 24.727  85.324  1.00 30.18 ? 530  LYS B CD    1 
ATOM   12618 C CE    . LYS B  1 532  ? -13.313 25.470  84.115  1.00 31.17 ? 530  LYS B CE    1 
ATOM   12619 N NZ    . LYS B  1 532  ? -13.625 26.893  84.436  1.00 30.63 ? 530  LYS B NZ    1 
ATOM   12620 N N     . HIS B  1 533  ? -16.205 25.161  88.240  1.00 28.46 ? 531  HIS B N     1 
ATOM   12621 C CA    . HIS B  1 533  ? -16.589 26.495  88.686  1.00 28.18 ? 531  HIS B CA    1 
ATOM   12622 C C     . HIS B  1 533  ? -16.408 27.507  87.561  1.00 31.39 ? 531  HIS B C     1 
ATOM   12623 O O     . HIS B  1 533  ? -15.363 27.542  86.904  1.00 26.32 ? 531  HIS B O     1 
ATOM   12624 C CB    . HIS B  1 533  ? -15.732 26.899  89.888  1.00 30.30 ? 531  HIS B CB    1 
ATOM   12625 C CG    . HIS B  1 533  ? -16.282 28.050  90.672  1.00 32.15 ? 531  HIS B CG    1 
ATOM   12626 N ND1   . HIS B  1 533  ? -16.374 29.326  90.159  1.00 28.74 ? 531  HIS B ND1   1 
ATOM   12627 C CD2   . HIS B  1 533  ? -16.753 28.119  91.940  1.00 34.42 ? 531  HIS B CD2   1 
ATOM   12628 C CE1   . HIS B  1 533  ? -16.889 30.130  91.072  1.00 33.00 ? 531  HIS B CE1   1 
ATOM   12629 N NE2   . HIS B  1 533  ? -17.130 29.422  92.162  1.00 38.20 ? 531  HIS B NE2   1 
ATOM   12630 N N     . ASP B  1 534  ? -17.429 28.349  87.358  1.00 29.98 ? 532  ASP B N     1 
ATOM   12631 C CA    . ASP B  1 534  ? -17.406 29.311  86.258  1.00 30.37 ? 532  ASP B CA    1 
ATOM   12632 C C     . ASP B  1 534  ? -16.289 30.344  86.395  1.00 30.19 ? 532  ASP B C     1 
ATOM   12633 O O     . ASP B  1 534  ? -15.873 30.925  85.390  1.00 29.19 ? 532  ASP B O     1 
ATOM   12634 C CB    . ASP B  1 534  ? -18.761 30.019  86.171  1.00 28.17 ? 532  ASP B CB    1 
ATOM   12635 N N     . ARG B  1 535  ? -15.791 30.578  87.604  1.00 29.18 ? 533  ARG B N     1 
ATOM   12636 C CA    . ARG B  1 535  ? -14.865 31.669  87.869  1.00 28.63 ? 533  ARG B CA    1 
ATOM   12637 C C     . ARG B  1 535  ? -13.460 31.178  88.188  1.00 29.91 ? 533  ARG B C     1 
ATOM   12638 O O     . ARG B  1 535  ? -12.632 31.961  88.654  1.00 30.17 ? 533  ARG B O     1 
ATOM   12639 C CB    . ARG B  1 535  ? -15.398 32.539  89.015  1.00 34.12 ? 533  ARG B CB    1 
ATOM   12640 N N     . ILE B  1 536  ? -13.164 29.901  87.954  1.00 27.12 ? 534  ILE B N     1 
ATOM   12641 C CA    . ILE B  1 536  ? -11.816 29.368  88.138  1.00 25.51 ? 534  ILE B CA    1 
ATOM   12642 C C     . ILE B  1 536  ? -11.336 28.851  86.790  1.00 27.75 ? 534  ILE B C     1 
ATOM   12643 O O     . ILE B  1 536  ? -11.955 27.948  86.208  1.00 25.30 ? 534  ILE B O     1 
ATOM   12644 C CB    . ILE B  1 536  ? -11.779 28.260  89.195  1.00 24.34 ? 534  ILE B CB    1 
ATOM   12645 C CG1   . ILE B  1 536  ? -12.302 28.804  90.531  1.00 26.20 ? 534  ILE B CG1   1 
ATOM   12646 C CG2   . ILE B  1 536  ? -10.359 27.732  89.347  1.00 25.09 ? 534  ILE B CG2   1 
ATOM   12647 C CD1   . ILE B  1 536  ? -12.310 27.768  91.646  1.00 30.31 ? 534  ILE B CD1   1 
ATOM   12648 N N     . ALA B  1 537  ? -10.244 29.417  86.294  1.00 25.01 ? 535  ALA B N     1 
ATOM   12649 C CA    . ALA B  1 537  ? -9.745  29.032  84.978  1.00 28.21 ? 535  ALA B CA    1 
ATOM   12650 C C     . ALA B  1 537  ? -8.978  27.715  85.035  1.00 22.91 ? 535  ALA B C     1 
ATOM   12651 O O     . ALA B  1 537  ? -8.143  27.509  85.916  1.00 22.98 ? 535  ALA B O     1 
ATOM   12652 C CB    . ALA B  1 537  ? -8.838  30.128  84.423  1.00 24.66 ? 535  ALA B CB    1 
ATOM   12653 N N     . LEU B  1 538  ? -9.250  26.824  84.076  1.00 24.59 ? 536  LEU B N     1 
ATOM   12654 C CA    . LEU B  1 538  ? -8.323  25.720  83.857  1.00 25.73 ? 536  LEU B CA    1 
ATOM   12655 C C     . LEU B  1 538  ? -6.943  26.294  83.541  1.00 23.32 ? 536  LEU B C     1 
ATOM   12656 O O     . LEU B  1 538  ? -6.833  27.405  83.018  1.00 22.72 ? 536  LEU B O     1 
ATOM   12657 C CB    . LEU B  1 538  ? -8.792  24.827  82.710  1.00 24.92 ? 536  LEU B CB    1 
ATOM   12658 C CG    . LEU B  1 538  ? -9.963  23.879  82.926  1.00 29.81 ? 536  LEU B CG    1 
ATOM   12659 C CD1   . LEU B  1 538  ? -10.275 23.173  81.604  1.00 29.89 ? 536  LEU B CD1   1 
ATOM   12660 C CD2   . LEU B  1 538  ? -9.625  22.881  84.021  1.00 26.50 ? 536  LEU B CD2   1 
ATOM   12661 N N     . PRO B  1 539  ? -5.865  25.589  83.891  1.00 23.42 ? 537  PRO B N     1 
ATOM   12662 C CA    . PRO B  1 539  ? -4.528  26.144  83.603  1.00 23.50 ? 537  PRO B CA    1 
ATOM   12663 C C     . PRO B  1 539  ? -4.355  26.506  82.134  1.00 22.25 ? 537  PRO B C     1 
ATOM   12664 O O     . PRO B  1 539  ? -3.752  27.540  81.812  1.00 22.62 ? 537  PRO B O     1 
ATOM   12665 C CB    . PRO B  1 539  ? -3.582  25.021  84.056  1.00 23.21 ? 537  PRO B CB    1 
ATOM   12666 C CG    . PRO B  1 539  ? -4.353  24.299  85.141  1.00 20.36 ? 537  PRO B CG    1 
ATOM   12667 C CD    . PRO B  1 539  ? -5.809  24.331  84.658  1.00 23.77 ? 537  PRO B CD    1 
ATOM   12668 N N     . ALA B  1 540  ? -4.918  25.703  81.233  1.00 21.19 ? 538  ALA B N     1 
ATOM   12669 C CA    . ALA B  1 540  ? -4.788  25.979  79.808  1.00 26.28 ? 538  ALA B CA    1 
ATOM   12670 C C     . ALA B  1 540  ? -5.520  27.247  79.395  1.00 28.23 ? 538  ALA B C     1 
ATOM   12671 O O     . ALA B  1 540  ? -5.207  27.818  78.336  1.00 24.48 ? 538  ALA B O     1 
ATOM   12672 C CB    . ALA B  1 540  ? -5.321  24.798  78.993  1.00 27.20 ? 538  ALA B CB    1 
ATOM   12673 N N     . GLU B  1 541  ? -6.476  27.697  80.211  1.00 26.17 ? 539  GLU B N     1 
ATOM   12674 C CA    . GLU B  1 541  ? -7.357  28.812  79.884  1.00 27.14 ? 539  GLU B CA    1 
ATOM   12675 C C     . GLU B  1 541  ? -7.027  30.072  80.693  1.00 27.28 ? 539  GLU B C     1 
ATOM   12676 O O     . GLU B  1 541  ? -7.841  31.005  80.741  1.00 24.86 ? 539  GLU B O     1 
ATOM   12677 C CB    . GLU B  1 541  ? -8.819  28.379  80.084  1.00 24.70 ? 539  GLU B CB    1 
ATOM   12678 C CG    . GLU B  1 541  ? -9.272  27.353  79.008  1.00 27.20 ? 539  GLU B CG    1 
ATOM   12679 C CD    . GLU B  1 541  ? -10.615 26.647  79.278  1.00 40.47 ? 539  GLU B CD    1 
ATOM   12680 O OE1   . GLU B  1 541  ? -11.399 27.091  80.144  1.00 39.91 ? 539  GLU B OE1   1 
ATOM   12681 O OE2   . GLU B  1 541  ? -10.888 25.630  78.596  1.00 41.35 ? 539  GLU B OE2   1 
ATOM   12682 N N     . LEU B  1 542  ? -5.826  30.131  81.288  1.00 23.28 ? 540  LEU B N     1 
ATOM   12683 C CA    . LEU B  1 542  ? -5.445  31.259  82.144  1.00 24.03 ? 540  LEU B CA    1 
ATOM   12684 C C     . LEU B  1 542  ? -5.529  32.590  81.413  1.00 26.36 ? 540  LEU B C     1 
ATOM   12685 O O     . LEU B  1 542  ? -5.757  33.630  82.047  1.00 25.48 ? 540  LEU B O     1 
ATOM   12686 C CB    . LEU B  1 542  ? -4.012  31.092  82.678  1.00 25.90 ? 540  LEU B CB    1 
ATOM   12687 C CG    . LEU B  1 542  ? -3.690  30.303  83.945  1.00 27.97 ? 540  LEU B CG    1 
ATOM   12688 C CD1   . LEU B  1 542  ? -2.266  30.587  84.425  1.00 25.23 ? 540  LEU B CD1   1 
ATOM   12689 C CD2   . LEU B  1 542  ? -4.703  30.542  85.060  1.00 25.60 ? 540  LEU B CD2   1 
ATOM   12690 N N     . PHE B  1 543  ? -5.338  32.589  80.093  1.00 22.81 ? 541  PHE B N     1 
ATOM   12691 C CA    . PHE B  1 543  ? -5.317  33.835  79.338  1.00 25.06 ? 541  PHE B CA    1 
ATOM   12692 C C     . PHE B  1 543  ? -6.555  33.994  78.474  1.00 24.36 ? 541  PHE B C     1 
ATOM   12693 O O     . PHE B  1 543  ? -6.615  34.911  77.650  1.00 24.96 ? 541  PHE B O     1 
ATOM   12694 C CB    . PHE B  1 543  ? -4.027  33.927  78.518  1.00 21.38 ? 541  PHE B CB    1 
ATOM   12695 C CG    . PHE B  1 543  ? -2.809  33.659  79.336  1.00 22.33 ? 541  PHE B CG    1 
ATOM   12696 C CD1   . PHE B  1 543  ? -2.506  34.476  80.423  1.00 22.60 ? 541  PHE B CD1   1 
ATOM   12697 C CD2   . PHE B  1 543  ? -1.998  32.575  79.074  1.00 21.85 ? 541  PHE B CD2   1 
ATOM   12698 C CE1   . PHE B  1 543  ? -1.406  34.223  81.209  1.00 21.64 ? 541  PHE B CE1   1 
ATOM   12699 C CE2   . PHE B  1 543  ? -0.872  32.318  79.859  1.00 23.71 ? 541  PHE B CE2   1 
ATOM   12700 C CZ    . PHE B  1 543  ? -0.575  33.150  80.929  1.00 24.62 ? 541  PHE B CZ    1 
ATOM   12701 N N     . GLY B  1 544  ? -7.549  33.129  78.663  1.00 27.45 ? 542  GLY B N     1 
ATOM   12702 C CA    . GLY B  1 544  ? -8.839  33.322  78.024  1.00 26.77 ? 542  GLY B CA    1 
ATOM   12703 C C     . GLY B  1 544  ? -8.744  33.174  76.519  1.00 33.22 ? 542  GLY B C     1 
ATOM   12704 O O     . GLY B  1 544  ? -8.057  32.292  75.989  1.00 29.38 ? 542  GLY B O     1 
ATOM   12705 N N     . ASP B  1 545  ? -9.448  34.052  75.814  1.00 28.23 ? 543  ASP B N     1 
ATOM   12706 C CA    . ASP B  1 545  ? -9.463  33.989  74.363  1.00 33.56 ? 543  ASP B CA    1 
ATOM   12707 C C     . ASP B  1 545  ? -8.188  34.529  73.728  1.00 29.13 ? 543  ASP B C     1 
ATOM   12708 O O     . ASP B  1 545  ? -8.008  34.362  72.516  1.00 29.94 ? 543  ASP B O     1 
ATOM   12709 C CB    . ASP B  1 545  ? -10.676 34.752  73.834  1.00 36.77 ? 543  ASP B CB    1 
ATOM   12710 C CG    . ASP B  1 545  ? -11.983 34.179  74.345  1.00 42.65 ? 543  ASP B CG    1 
ATOM   12711 O OD1   . ASP B  1 545  ? -12.062 32.943  74.551  1.00 41.94 ? 543  ASP B OD1   1 
ATOM   12712 O OD2   . ASP B  1 545  ? -12.934 34.964  74.536  1.00 54.25 ? 543  ASP B OD2   1 
ATOM   12713 N N     . ALA B  1 546  ? -7.303  35.155  74.511  1.00 27.46 ? 544  ALA B N     1 
ATOM   12714 C CA    . ALA B  1 546  ? -6.086  35.735  73.946  1.00 26.34 ? 544  ALA B CA    1 
ATOM   12715 C C     . ALA B  1 546  ? -5.166  34.663  73.378  1.00 28.91 ? 544  ALA B C     1 
ATOM   12716 O O     . ALA B  1 546  ? -4.601  34.837  72.291  1.00 24.47 ? 544  ALA B O     1 
ATOM   12717 C CB    . ALA B  1 546  ? -5.339  36.548  75.005  1.00 25.92 ? 544  ALA B CB    1 
ATOM   12718 N N     . ARG B  1 547  ? -4.980  33.565  74.105  1.00 24.76 ? 545  ARG B N     1 
ATOM   12719 C CA    . ARG B  1 547  ? -4.028  32.543  73.690  1.00 24.16 ? 545  ARG B CA    1 
ATOM   12720 C C     . ARG B  1 547  ? -4.123  31.378  74.656  1.00 24.54 ? 545  ARG B C     1 
ATOM   12721 O O     . ARG B  1 547  ? -4.577  31.525  75.795  1.00 25.40 ? 545  ARG B O     1 
ATOM   12722 C CB    . ARG B  1 547  ? -2.581  33.068  73.644  1.00 26.05 ? 545  ARG B CB    1 
ATOM   12723 C CG    . ARG B  1 547  ? -2.002  33.410  74.987  1.00 24.32 ? 545  ARG B CG    1 
ATOM   12724 C CD    . ARG B  1 547  ? -0.534  33.811  74.876  1.00 25.78 ? 545  ARG B CD    1 
ATOM   12725 N NE    . ARG B  1 547  ? -0.158  34.647  76.006  1.00 24.51 ? 545  ARG B NE    1 
ATOM   12726 C CZ    . ARG B  1 547  ? 0.585   34.271  77.039  1.00 25.16 ? 545  ARG B CZ    1 
ATOM   12727 N NH1   . ARG B  1 547  ? 1.199   33.095  77.068  1.00 21.60 ? 545  ARG B NH1   1 
ATOM   12728 N NH2   . ARG B  1 547  ? 0.737   35.109  78.061  1.00 26.10 ? 545  ARG B NH2   1 
ATOM   12729 N N     . THR B  1 548  ? -3.670  30.223  74.192  1.00 23.14 ? 546  THR B N     1 
ATOM   12730 C CA    . THR B  1 548  ? -3.668  29.014  75.002  1.00 23.75 ? 546  THR B CA    1 
ATOM   12731 C C     . THR B  1 548  ? -2.381  28.943  75.821  1.00 24.55 ? 546  THR B C     1 
ATOM   12732 O O     . THR B  1 548  ? -1.283  29.052  75.277  1.00 22.44 ? 546  THR B O     1 
ATOM   12733 C CB    . THR B  1 548  ? -3.806  27.791  74.098  1.00 24.29 ? 546  THR B CB    1 
ATOM   12734 O OG1   . THR B  1 548  ? -5.003  27.917  73.312  1.00 29.54 ? 546  THR B OG1   1 
ATOM   12735 C CG2   . THR B  1 548  ? -3.859  26.514  74.912  1.00 25.87 ? 546  THR B CG2   1 
ATOM   12736 N N     . ASN B  1 549  ? -2.524  28.779  77.130  1.00 20.58 ? 547  ASN B N     1 
ATOM   12737 C CA    . ASN B  1 549  ? -1.370  28.626  77.999  1.00 21.84 ? 547  ASN B CA    1 
ATOM   12738 C C     . ASN B  1 549  ? -0.624  27.339  77.647  1.00 21.10 ? 547  ASN B C     1 
ATOM   12739 O O     . ASN B  1 549  ? -1.236  26.323  77.309  1.00 26.20 ? 547  ASN B O     1 
ATOM   12740 C CB    . ASN B  1 549  ? -1.845  28.615  79.463  1.00 21.61 ? 547  ASN B CB    1 
ATOM   12741 C CG    . ASN B  1 549  ? -0.700  28.682  80.454  1.00 23.39 ? 547  ASN B CG    1 
ATOM   12742 O OD1   . ASN B  1 549  ? 0.410   29.080  80.104  1.00 22.75 ? 547  ASN B OD1   1 
ATOM   12743 N ND2   . ASN B  1 549  ? -0.969  28.311  81.708  1.00 22.52 ? 547  ASN B ND2   1 
ATOM   12744 N N     . SER B  1 550  ? 0.707   27.393  77.675  1.00 20.67 ? 548  SER B N     1 
ATOM   12745 C CA    . SER B  1 550  ? 1.487   26.170  77.508  1.00 23.86 ? 548  SER B CA    1 
ATOM   12746 C C     . SER B  1 550  ? 1.143   25.159  78.592  1.00 23.07 ? 548  SER B C     1 
ATOM   12747 O O     . SER B  1 550  ? 0.717   25.517  79.693  1.00 23.88 ? 548  SER B O     1 
ATOM   12748 C CB    . SER B  1 550  ? 2.981   26.459  77.561  1.00 22.06 ? 548  SER B CB    1 
ATOM   12749 O OG    . SER B  1 550  ? 3.340   26.950  78.839  1.00 24.51 ? 548  SER B OG    1 
ATOM   12750 N N     . ALA B  1 551  ? 1.352   23.882  78.280  1.00 25.64 ? 549  ALA B N     1 
ATOM   12751 C CA    . ALA B  1 551  ? 1.111   22.801  79.221  1.00 24.67 ? 549  ALA B CA    1 
ATOM   12752 C C     . ALA B  1 551  ? 2.437   22.214  79.690  1.00 26.14 ? 549  ALA B C     1 
ATOM   12753 O O     . ALA B  1 551  ? 3.378   22.076  78.902  1.00 26.05 ? 549  ALA B O     1 
ATOM   12754 C CB    . ALA B  1 551  ? 0.250   21.706  78.593  1.00 27.95 ? 549  ALA B CB    1 
ATOM   12755 N N     . GLY B  1 552  ? 2.503   21.879  80.974  1.00 26.32 ? 550  GLY B N     1 
ATOM   12756 C CA    . GLY B  1 552  ? 3.646   21.213  81.549  1.00 26.13 ? 550  GLY B CA    1 
ATOM   12757 C C     . GLY B  1 552  ? 3.415   19.726  81.705  1.00 24.79 ? 550  GLY B C     1 
ATOM   12758 O O     . GLY B  1 552  ? 2.537   19.133  81.071  1.00 28.28 ? 550  GLY B O     1 
ATOM   12759 N N     . LEU B  1 553  ? 4.212   19.116  82.581  1.00 25.99 ? 551  LEU B N     1 
ATOM   12760 C CA    . LEU B  1 553  ? 4.157   17.684  82.846  1.00 30.99 ? 551  LEU B CA    1 
ATOM   12761 C C     . LEU B  1 553  ? 4.238   17.488  84.351  1.00 26.52 ? 551  LEU B C     1 
ATOM   12762 O O     . LEU B  1 553  ? 4.983   18.195  85.025  1.00 28.61 ? 551  LEU B O     1 
ATOM   12763 C CB    . LEU B  1 553  ? 5.302   16.921  82.147  1.00 28.29 ? 551  LEU B CB    1 
ATOM   12764 C CG    . LEU B  1 553  ? 5.253   16.874  80.612  1.00 27.68 ? 551  LEU B CG    1 
ATOM   12765 C CD1   . LEU B  1 553  ? 6.504   16.280  80.031  1.00 30.88 ? 551  LEU B CD1   1 
ATOM   12766 C CD2   . LEU B  1 553  ? 4.029   16.106  80.122  1.00 30.87 ? 551  LEU B CD2   1 
ATOM   12767 N N     . ASP B  1 554  ? 3.467   16.538  84.867  1.00 26.21 ? 552  ASP B N     1 
ATOM   12768 C CA    . ASP B  1 554  ? 3.318   16.340  86.306  1.00 26.85 ? 552  ASP B CA    1 
ATOM   12769 C C     . ASP B  1 554  ? 4.337   15.295  86.744  1.00 27.71 ? 552  ASP B C     1 
ATOM   12770 O O     . ASP B  1 554  ? 4.151   14.103  86.491  1.00 25.85 ? 552  ASP B O     1 
ATOM   12771 C CB    . ASP B  1 554  ? 1.890   15.899  86.614  1.00 31.18 ? 552  ASP B CB    1 
ATOM   12772 C CG    . ASP B  1 554  ? 1.624   15.708  88.094  1.00 28.01 ? 552  ASP B CG    1 
ATOM   12773 O OD1   . ASP B  1 554  ? 2.532   15.930  88.933  1.00 27.13 ? 552  ASP B OD1   1 
ATOM   12774 O OD2   . ASP B  1 554  ? 0.471   15.335  88.404  1.00 30.30 ? 552  ASP B OD2   1 
ATOM   12775 N N     . LEU B  1 555  ? 5.414   15.735  87.395  1.00 24.24 ? 553  LEU B N     1 
ATOM   12776 C CA    . LEU B  1 555  ? 6.459   14.787  87.764  1.00 26.43 ? 553  LEU B CA    1 
ATOM   12777 C C     . LEU B  1 555  ? 6.136   14.025  89.039  1.00 28.14 ? 553  LEU B C     1 
ATOM   12778 O O     . LEU B  1 555  ? 6.998   13.311  89.550  1.00 24.40 ? 553  LEU B O     1 
ATOM   12779 C CB    . LEU B  1 555  ? 7.813   15.500  87.886  1.00 28.15 ? 553  LEU B CB    1 
ATOM   12780 C CG    . LEU B  1 555  ? 8.321   16.038  86.538  1.00 30.99 ? 553  LEU B CG    1 
ATOM   12781 C CD1   . LEU B  1 555  ? 9.681   16.704  86.664  1.00 29.83 ? 553  LEU B CD1   1 
ATOM   12782 C CD2   . LEU B  1 555  ? 8.362   14.939  85.461  1.00 30.66 ? 553  LEU B CD2   1 
ATOM   12783 N N     . SER B  1 556  ? 4.914   14.148  89.551  1.00 30.09 ? 554  SER B N     1 
ATOM   12784 C CA    . SER B  1 556  ? 4.419   13.297  90.624  1.00 30.06 ? 554  SER B CA    1 
ATOM   12785 C C     . SER B  1 556  ? 3.480   12.219  90.107  1.00 29.88 ? 554  SER B C     1 
ATOM   12786 O O     . SER B  1 556  ? 3.013   11.389  90.891  1.00 29.43 ? 554  SER B O     1 
ATOM   12787 C CB    . SER B  1 556  ? 3.692   14.140  91.688  1.00 30.69 ? 554  SER B CB    1 
ATOM   12788 O OG    . SER B  1 556  ? 2.388   14.519  91.228  1.00 28.63 ? 554  SER B OG    1 
ATOM   12789 N N     . ASN B  1 557  ? 3.199   12.214  88.807  1.00 29.11 ? 555  ASN B N     1 
ATOM   12790 C CA    . ASN B  1 557  ? 2.278   11.263  88.202  1.00 28.70 ? 555  ASN B CA    1 
ATOM   12791 C C     . ASN B  1 557  ? 3.061   10.064  87.676  1.00 31.35 ? 555  ASN B C     1 
ATOM   12792 O O     . ASN B  1 557  ? 3.906   10.214  86.784  1.00 28.85 ? 555  ASN B O     1 
ATOM   12793 C CB    . ASN B  1 557  ? 1.494   11.946  87.077  1.00 28.09 ? 555  ASN B CB    1 
ATOM   12794 C CG    . ASN B  1 557  ? 0.448   11.046  86.467  1.00 30.72 ? 555  ASN B CG    1 
ATOM   12795 O OD1   . ASN B  1 557  ? 0.734   9.908   86.087  1.00 31.27 ? 555  ASN B OD1   1 
ATOM   12796 N ND2   . ASN B  1 557  ? -0.782  11.550  86.365  1.00 31.79 ? 555  ASN B ND2   1 
ATOM   12797 N N     . GLU B  1 558  ? 2.764   8.873   88.212  1.00 31.51 ? 556  GLU B N     1 
ATOM   12798 C CA    . GLU B  1 558  ? 3.535   7.688   87.842  1.00 32.24 ? 556  GLU B CA    1 
ATOM   12799 C C     . GLU B  1 558  ? 3.374   7.333   86.369  1.00 31.27 ? 556  GLU B C     1 
ATOM   12800 O O     . GLU B  1 558  ? 4.317   6.808   85.772  1.00 30.61 ? 556  GLU B O     1 
ATOM   12801 C CB    . GLU B  1 558  ? 3.141   6.479   88.696  1.00 32.64 ? 556  GLU B CB    1 
ATOM   12802 C CG    . GLU B  1 558  ? 3.540   6.538   90.156  1.00 33.30 ? 556  GLU B CG    1 
ATOM   12803 C CD    . GLU B  1 558  ? 5.051   6.598   90.414  1.00 32.86 ? 556  GLU B CD    1 
ATOM   12804 O OE1   . GLU B  1 558  ? 5.880   6.295   89.522  1.00 32.87 ? 556  GLU B OE1   1 
ATOM   12805 O OE2   . GLU B  1 558  ? 5.407   6.946   91.550  1.00 35.89 ? 556  GLU B OE2   1 
ATOM   12806 N N     . GLU B  1 559  ? 2.192   7.571   85.777  1.00 33.09 ? 557  GLU B N     1 
ATOM   12807 C CA    . GLU B  1 559  ? 2.028   7.333   84.339  1.00 32.84 ? 557  GLU B CA    1 
ATOM   12808 C C     . GLU B  1 559  ? 2.943   8.256   83.546  1.00 31.37 ? 557  GLU B C     1 
ATOM   12809 O O     . GLU B  1 559  ? 3.603   7.834   82.585  1.00 32.39 ? 557  GLU B O     1 
ATOM   12810 C CB    . GLU B  1 559  ? 0.577   7.557   83.889  1.00 36.63 ? 557  GLU B CB    1 
ATOM   12811 C CG    . GLU B  1 559  ? -0.513  6.649   84.456  1.00 37.59 ? 557  GLU B CG    1 
ATOM   12812 C CD    . GLU B  1 559  ? -1.918  7.076   83.991  1.00 42.89 ? 557  GLU B CD    1 
ATOM   12813 O OE1   . GLU B  1 559  ? -2.030  8.041   83.204  1.00 49.21 ? 557  GLU B OE1   1 
ATOM   12814 O OE2   . GLU B  1 559  ? -2.914  6.454   84.415  1.00 42.20 ? 557  GLU B OE2   1 
ATOM   12815 N N     . THR B  1 560  ? 2.969   9.533   83.931  1.00 27.68 ? 558  THR B N     1 
ATOM   12816 C CA    . THR B  1 560  ? 3.818   10.520  83.282  1.00 30.29 ? 558  THR B CA    1 
ATOM   12817 C C     . THR B  1 560  ? 5.295   10.158  83.424  1.00 30.83 ? 558  THR B C     1 
ATOM   12818 O O     . THR B  1 560  ? 6.054   10.233  82.451  1.00 29.94 ? 558  THR B O     1 
ATOM   12819 C CB    . THR B  1 560  ? 3.538   11.912  83.878  1.00 27.68 ? 558  THR B CB    1 
ATOM   12820 O OG1   . THR B  1 560  ? 2.152   12.244  83.711  1.00 27.84 ? 558  THR B OG1   1 
ATOM   12821 C CG2   . THR B  1 560  ? 4.384   12.979  83.189  1.00 29.07 ? 558  THR B CG2   1 
ATOM   12822 N N     . LEU B  1 561  ? 5.727   9.759   84.630  1.00 29.21 ? 559  LEU B N     1 
ATOM   12823 C CA    . LEU B  1 561  ? 7.128   9.378   84.810  1.00 31.68 ? 559  LEU B CA    1 
ATOM   12824 C C     . LEU B  1 561  ? 7.485   8.154   83.972  1.00 30.69 ? 559  LEU B C     1 
ATOM   12825 O O     . LEU B  1 561  ? 8.580   8.079   83.404  1.00 29.99 ? 559  LEU B O     1 
ATOM   12826 C CB    . LEU B  1 561  ? 7.424   9.116   86.287  1.00 29.66 ? 559  LEU B CB    1 
ATOM   12827 C CG    . LEU B  1 561  ? 7.353   10.345  87.200  1.00 26.61 ? 559  LEU B CG    1 
ATOM   12828 C CD1   . LEU B  1 561  ? 7.526   9.912   88.664  1.00 26.75 ? 559  LEU B CD1   1 
ATOM   12829 C CD2   . LEU B  1 561  ? 8.423   11.363  86.824  1.00 25.28 ? 559  LEU B CD2   1 
ATOM   12830 N N     . ALA B  1 562  ? 6.582   7.180   83.890  1.00 29.98 ? 560  ALA B N     1 
ATOM   12831 C CA    . ALA B  1 562  ? 6.880   5.976   83.122  1.00 32.06 ? 560  ALA B CA    1 
ATOM   12832 C C     . ALA B  1 562  ? 6.991   6.284   81.630  1.00 32.93 ? 560  ALA B C     1 
ATOM   12833 O O     . ALA B  1 562  ? 7.884   5.771   80.949  1.00 34.20 ? 560  ALA B O     1 
ATOM   12834 C CB    . ALA B  1 562  ? 5.813   4.904   83.376  1.00 30.64 ? 560  ALA B CB    1 
ATOM   12835 N N     . SER B  1 563  ? 6.108   7.130   81.103  1.00 32.69 ? 561  SER B N     1 
ATOM   12836 C CA    . SER B  1 563  ? 6.178   7.426   79.676  1.00 33.94 ? 561  SER B CA    1 
ATOM   12837 C C     . SER B  1 563  ? 7.304   8.403   79.363  1.00 33.12 ? 561  SER B C     1 
ATOM   12838 O O     . SER B  1 563  ? 7.906   8.323   78.288  1.00 31.80 ? 561  SER B O     1 
ATOM   12839 C CB    . SER B  1 563  ? 4.841   7.969   79.180  1.00 32.69 ? 561  SER B CB    1 
ATOM   12840 O OG    . SER B  1 563  ? 4.658   9.305   79.585  1.00 38.62 ? 561  SER B OG    1 
ATOM   12841 N N     . LEU B  1 564  ? 7.596   9.327   80.285  1.00 30.04 ? 562  LEU B N     1 
ATOM   12842 C CA    . LEU B  1 564  ? 8.727   10.227  80.108  1.00 33.30 ? 562  LEU B CA    1 
ATOM   12843 C C     . LEU B  1 564  ? 10.051  9.464   80.130  1.00 35.56 ? 562  LEU B C     1 
ATOM   12844 O O     . LEU B  1 564  ? 10.960  9.767   79.353  1.00 34.36 ? 562  LEU B O     1 
ATOM   12845 C CB    . LEU B  1 564  ? 8.696   11.300  81.197  1.00 34.40 ? 562  LEU B CB    1 
ATOM   12846 C CG    . LEU B  1 564  ? 9.683   12.451  81.114  1.00 39.75 ? 562  LEU B CG    1 
ATOM   12847 C CD1   . LEU B  1 564  ? 9.550   13.096  79.759  1.00 35.05 ? 562  LEU B CD1   1 
ATOM   12848 C CD2   . LEU B  1 564  ? 9.420   13.466  82.243  1.00 35.49 ? 562  LEU B CD2   1 
ATOM   12849 N N     . THR B  1 565  ? 10.181  8.481   81.025  1.00 30.71 ? 563  THR B N     1 
ATOM   12850 C CA    . THR B  1 565  ? 11.367  7.636   81.043  1.00 33.41 ? 563  THR B CA    1 
ATOM   12851 C C     . THR B  1 565  ? 11.638  7.047   79.662  1.00 37.63 ? 563  THR B C     1 
ATOM   12852 O O     . THR B  1 565  ? 12.763  7.111   79.155  1.00 37.96 ? 563  THR B O     1 
ATOM   12853 C CB    . THR B  1 565  ? 11.195  6.521   82.081  1.00 33.81 ? 563  THR B CB    1 
ATOM   12854 O OG1   . THR B  1 565  ? 11.110  7.091   83.399  1.00 32.58 ? 563  THR B OG1   1 
ATOM   12855 C CG2   . THR B  1 565  ? 12.370  5.538   82.022  1.00 37.15 ? 563  THR B CG2   1 
ATOM   12856 N N     . GLU B  1 566  ? 10.609  6.479   79.031  1.00 35.03 ? 564  GLU B N     1 
ATOM   12857 C CA    . GLU B  1 566  ? 10.816  5.837   77.735  1.00 39.84 ? 564  GLU B CA    1 
ATOM   12858 C C     . GLU B  1 566  ? 11.099  6.858   76.641  1.00 35.30 ? 564  GLU B C     1 
ATOM   12859 O O     . GLU B  1 566  ? 11.926  6.614   75.758  1.00 35.69 ? 564  GLU B O     1 
ATOM   12860 C CB    . GLU B  1 566  ? 9.611   4.978   77.363  1.00 42.25 ? 564  GLU B CB    1 
ATOM   12861 C CG    . GLU B  1 566  ? 9.427   3.762   78.259  1.00 46.53 ? 564  GLU B CG    1 
ATOM   12862 C CD    . GLU B  1 566  ? 10.737  3.071   78.602  1.00 53.90 ? 564  GLU B CD    1 
ATOM   12863 O OE1   . GLU B  1 566  ? 11.524  2.760   77.677  1.00 60.51 ? 564  GLU B OE1   1 
ATOM   12864 O OE2   . GLU B  1 566  ? 10.982  2.836   79.807  1.00 56.78 ? 564  GLU B OE2   1 
ATOM   12865 N N     . ALA B  1 567  ? 10.419  7.998   76.668  1.00 32.55 ? 565  ALA B N     1 
ATOM   12866 C CA    . ALA B  1 567  ? 10.695  9.015   75.661  1.00 36.33 ? 565  ALA B CA    1 
ATOM   12867 C C     . ALA B  1 567  ? 12.091  9.601   75.825  1.00 37.93 ? 565  ALA B C     1 
ATOM   12868 O O     . ALA B  1 567  ? 12.728  9.962   74.826  1.00 32.47 ? 565  ALA B O     1 
ATOM   12869 C CB    . ALA B  1 567  ? 9.640   10.118  75.721  1.00 34.94 ? 565  ALA B CB    1 
ATOM   12870 N N     . LEU B  1 568  ? 12.582  9.710   77.067  1.00 29.95 ? 566  LEU B N     1 
ATOM   12871 C CA    . LEU B  1 568  ? 13.924  10.239  77.283  1.00 34.23 ? 566  LEU B CA    1 
ATOM   12872 C C     . LEU B  1 568  ? 14.981  9.259   76.789  1.00 36.65 ? 566  LEU B C     1 
ATOM   12873 O O     . LEU B  1 568  ? 15.984  9.667   76.193  1.00 33.89 ? 566  LEU B O     1 
ATOM   12874 C CB    . LEU B  1 568  ? 14.142  10.556  78.764  1.00 31.64 ? 566  LEU B CB    1 
ATOM   12875 C CG    . LEU B  1 568  ? 13.318  11.675  79.404  1.00 34.31 ? 566  LEU B CG    1 
ATOM   12876 C CD1   . LEU B  1 568  ? 13.625  11.776  80.891  1.00 34.48 ? 566  LEU B CD1   1 
ATOM   12877 C CD2   . LEU B  1 568  ? 13.563  13.010  78.717  1.00 32.76 ? 566  LEU B CD2   1 
ATOM   12878 N N     . ARG B  1 569  ? 14.778  7.961   77.034  1.00 36.17 ? 567  ARG B N     1 
ATOM   12879 C CA    . ARG B  1 569  ? 15.700  6.959   76.509  1.00 40.59 ? 567  ARG B CA    1 
ATOM   12880 C C     . ARG B  1 569  ? 15.748  6.994   74.986  1.00 40.04 ? 567  ARG B C     1 
ATOM   12881 O O     . ARG B  1 569  ? 16.830  6.919   74.388  1.00 41.03 ? 567  ARG B O     1 
ATOM   12882 C CB    . ARG B  1 569  ? 15.294  5.563   76.977  1.00 42.23 ? 567  ARG B CB    1 
ATOM   12883 C CG    . ARG B  1 569  ? 15.332  5.357   78.463  1.00 45.35 ? 567  ARG B CG    1 
ATOM   12884 C CD    . ARG B  1 569  ? 15.135  3.892   78.777  1.00 50.14 ? 567  ARG B CD    1 
ATOM   12885 N NE    . ARG B  1 569  ? 14.938  3.682   80.203  1.00 54.28 ? 567  ARG B NE    1 
ATOM   12886 C CZ    . ARG B  1 569  ? 14.886  2.489   80.775  1.00 58.67 ? 567  ARG B CZ    1 
ATOM   12887 N NH1   . ARG B  1 569  ? 15.037  1.380   80.069  1.00 60.19 ? 567  ARG B NH1   1 
ATOM   12888 N NH2   . ARG B  1 569  ? 14.687  2.406   82.089  1.00 60.08 ? 567  ARG B NH2   1 
ATOM   12889 N N     . GLU B  1 570  ? 14.580  7.081   74.343  1.00 36.92 ? 568  GLU B N     1 
ATOM   12890 C CA    . GLU B  1 570  ? 14.533  7.130   72.886  1.00 40.09 ? 568  GLU B CA    1 
ATOM   12891 C C     . GLU B  1 570  ? 15.283  8.343   72.351  1.00 38.05 ? 568  GLU B C     1 
ATOM   12892 O O     . GLU B  1 570  ? 15.988  8.247   71.341  1.00 38.80 ? 568  GLU B O     1 
ATOM   12893 C CB    . GLU B  1 570  ? 13.081  7.154   72.407  1.00 38.50 ? 568  GLU B CB    1 
ATOM   12894 C CG    . GLU B  1 570  ? 12.319  5.875   72.686  1.00 45.78 ? 568  GLU B CG    1 
ATOM   12895 C CD    . GLU B  1 570  ? 10.822  6.016   72.453  1.00 51.33 ? 568  GLU B CD    1 
ATOM   12896 O OE1   . GLU B  1 570  ? 10.360  7.132   72.121  1.00 57.23 ? 568  GLU B OE1   1 
ATOM   12897 O OE2   . GLU B  1 570  ? 10.105  5.004   72.609  1.00 58.10 ? 568  GLU B OE2   1 
ATOM   12898 N N     . SER B  1 571  ? 15.141  9.492   73.017  1.00 37.76 ? 569  SER B N     1 
ATOM   12899 C CA    . SER B  1 571  ? 15.797  10.711  72.558  1.00 38.07 ? 569  SER B CA    1 
ATOM   12900 C C     . SER B  1 571  ? 17.311  10.579  72.622  1.00 41.14 ? 569  SER B C     1 
ATOM   12901 O O     . SER B  1 571  ? 18.022  11.157  71.790  1.00 39.52 ? 569  SER B O     1 
ATOM   12902 C CB    . SER B  1 571  ? 15.351  11.904  73.405  1.00 37.52 ? 569  SER B CB    1 
ATOM   12903 O OG    . SER B  1 571  ? 16.120  11.972  74.609  1.00 39.90 ? 569  SER B OG    1 
ATOM   12904 N N     . ALA B  1 572  ? 17.819  9.835   73.608  1.00 36.23 ? 570  ALA B N     1 
ATOM   12905 C CA    . ALA B  1 572  ? 19.255  9.639   73.736  1.00 37.79 ? 570  ALA B CA    1 
ATOM   12906 C C     . ALA B  1 572  ? 19.821  8.771   72.619  1.00 43.39 ? 570  ALA B C     1 
ATOM   12907 O O     . ALA B  1 572  ? 21.024  8.847   72.338  1.00 41.99 ? 570  ALA B O     1 
ATOM   12908 C CB    . ALA B  1 572  ? 19.569  9.019   75.097  1.00 38.27 ? 570  ALA B CB    1 
ATOM   12909 N N     . ALA B  1 573  ? 18.988  7.958   71.977  1.00 38.65 ? 571  ALA B N     1 
ATOM   12910 C CA    . ALA B  1 573  ? 19.425  7.101   70.885  1.00 43.31 ? 571  ALA B CA    1 
ATOM   12911 C C     . ALA B  1 573  ? 19.318  7.766   69.512  1.00 41.94 ? 571  ALA B C     1 
ATOM   12912 O O     . ALA B  1 573  ? 19.729  7.161   68.516  1.00 40.02 ? 571  ALA B O     1 
ATOM   12913 C CB    . ALA B  1 573  ? 18.621  5.793   70.896  1.00 40.16 ? 571  ALA B CB    1 
ATOM   12914 N N     . MET B  1 574  ? 18.794  8.986   69.429  1.00 39.88 ? 572  MET B N     1 
ATOM   12915 C CA    . MET B  1 574  ? 18.674  9.650   68.139  1.00 39.66 ? 572  MET B CA    1 
ATOM   12916 C C     . MET B  1 574  ? 19.997  10.296  67.736  1.00 40.01 ? 572  MET B C     1 
ATOM   12917 O O     . MET B  1 574  ? 20.848  10.608  68.571  1.00 36.59 ? 572  MET B O     1 
ATOM   12918 C CB    . MET B  1 574  ? 17.561  10.695  68.178  1.00 37.17 ? 572  MET B CB    1 
ATOM   12919 C CG    . MET B  1 574  ? 16.194  10.098  68.476  1.00 38.97 ? 572  MET B CG    1 
ATOM   12920 S SD    . MET B  1 574  ? 14.943  11.346  68.821  1.00 49.39 ? 572  MET B SD    1 
ATOM   12921 C CE    . MET B  1 574  ? 13.530  10.323  69.242  1.00 45.21 ? 572  MET B CE    1 
ATOM   12922 N N     . LYS B  1 575  ? 20.178  10.486  66.429  1.00 33.32 ? 573  LYS B N     1 
ATOM   12923 C CA    . LYS B  1 575  ? 21.364  11.187  65.936  1.00 34.85 ? 573  LYS B CA    1 
ATOM   12924 C C     . LYS B  1 575  ? 21.071  12.682  65.904  1.00 33.28 ? 573  LYS B C     1 
ATOM   12925 O O     . LYS B  1 575  ? 20.424  13.172  64.977  1.00 33.76 ? 573  LYS B O     1 
ATOM   12926 C CB    . LYS B  1 575  ? 21.765  10.690  64.556  1.00 33.58 ? 573  LYS B CB    1 
ATOM   12927 C CG    . LYS B  1 575  ? 23.069  11.308  64.071  1.00 39.12 ? 573  LYS B CG    1 
ATOM   12928 C CD    . LYS B  1 575  ? 23.395  10.832  62.675  1.00 39.54 ? 573  LYS B CD    1 
ATOM   12929 C CE    . LYS B  1 575  ? 24.783  11.278  62.240  1.00 45.65 ? 573  LYS B CE    1 
ATOM   12930 N NZ    . LYS B  1 575  ? 25.070  10.771  60.876  1.00 45.97 ? 573  LYS B NZ    1 
ATOM   12931 N N     . TRP B  1 576  ? 21.555  13.413  66.913  1.00 33.61 ? 574  TRP B N     1 
ATOM   12932 C CA    . TRP B  1 576  ? 21.368  14.857  66.987  1.00 30.53 ? 574  TRP B CA    1 
ATOM   12933 C C     . TRP B  1 576  ? 22.514  15.585  66.296  1.00 32.21 ? 574  TRP B C     1 
ATOM   12934 O O     . TRP B  1 576  ? 23.686  15.358  66.612  1.00 31.13 ? 574  TRP B O     1 
ATOM   12935 C CB    . TRP B  1 576  ? 21.267  15.322  68.441  1.00 29.62 ? 574  TRP B CB    1 
ATOM   12936 C CG    . TRP B  1 576  ? 20.102  14.703  69.156  1.00 32.74 ? 574  TRP B CG    1 
ATOM   12937 C CD1   . TRP B  1 576  ? 20.148  13.683  70.069  1.00 35.91 ? 574  TRP B CD1   1 
ATOM   12938 C CD2   . TRP B  1 576  ? 18.718  15.052  69.009  1.00 32.75 ? 574  TRP B CD2   1 
ATOM   12939 N NE1   . TRP B  1 576  ? 18.875  13.383  70.505  1.00 36.57 ? 574  TRP B NE1   1 
ATOM   12940 C CE2   . TRP B  1 576  ? 17.982  14.208  69.869  1.00 35.75 ? 574  TRP B CE2   1 
ATOM   12941 C CE3   . TRP B  1 576  ? 18.031  15.994  68.235  1.00 33.68 ? 574  TRP B CE3   1 
ATOM   12942 C CZ2   . TRP B  1 576  ? 16.592  14.278  69.977  1.00 38.74 ? 574  TRP B CZ2   1 
ATOM   12943 C CZ3   . TRP B  1 576  ? 16.640  16.065  68.343  1.00 34.66 ? 574  TRP B CZ3   1 
ATOM   12944 C CH2   . TRP B  1 576  ? 15.940  15.212  69.207  1.00 37.58 ? 574  TRP B CH2   1 
ATOM   12945 N N     . THR B  1 577  ? 22.166  16.470  65.366  1.00 30.61 ? 575  THR B N     1 
ATOM   12946 C CA    . THR B  1 577  ? 23.145  17.217  64.595  1.00 29.06 ? 575  THR B CA    1 
ATOM   12947 C C     . THR B  1 577  ? 22.730  18.675  64.532  1.00 30.83 ? 575  THR B C     1 
ATOM   12948 O O     . THR B  1 577  ? 21.563  19.029  64.723  1.00 29.18 ? 575  THR B O     1 
ATOM   12949 C CB    . THR B  1 577  ? 23.286  16.697  63.160  1.00 29.61 ? 575  THR B CB    1 
ATOM   12950 O OG1   . THR B  1 577  ? 22.010  16.803  62.505  1.00 33.90 ? 575  THR B OG1   1 
ATOM   12951 C CG2   . THR B  1 577  ? 23.764  15.258  63.146  1.00 34.63 ? 575  THR B CG2   1 
ATOM   12952 N N     . ALA B  1 578  ? 23.705  19.524  64.237  1.00 27.18 ? 576  ALA B N     1 
ATOM   12953 C CA    . ALA B  1 578  ? 23.434  20.934  64.002  1.00 26.81 ? 576  ALA B CA    1 
ATOM   12954 C C     . ALA B  1 578  ? 24.367  21.367  62.891  1.00 28.82 ? 576  ALA B C     1 
ATOM   12955 O O     . ALA B  1 578  ? 25.581  21.157  62.979  1.00 34.04 ? 576  ALA B O     1 
ATOM   12956 C CB    . ALA B  1 578  ? 23.626  21.784  65.265  1.00 24.61 ? 576  ALA B CB    1 
ATOM   12957 N N     . LEU B  1 579  ? 23.790  21.896  61.826  1.00 28.58 ? 577  LEU B N     1 
ATOM   12958 C CA    . LEU B  1 579  ? 24.489  22.240  60.606  1.00 28.52 ? 577  LEU B CA    1 
ATOM   12959 C C     . LEU B  1 579  ? 24.269  23.711  60.301  1.00 26.46 ? 577  LEU B C     1 
ATOM   12960 O O     . LEU B  1 579  ? 23.261  24.293  60.713  1.00 26.14 ? 577  LEU B O     1 
ATOM   12961 C CB    . LEU B  1 579  ? 23.965  21.398  59.431  1.00 27.70 ? 577  LEU B CB    1 
ATOM   12962 C CG    . LEU B  1 579  ? 23.866  19.894  59.686  1.00 31.97 ? 577  LEU B CG    1 
ATOM   12963 C CD1   . LEU B  1 579  ? 23.330  19.179  58.458  1.00 33.25 ? 577  LEU B CD1   1 
ATOM   12964 C CD2   . LEU B  1 579  ? 25.223  19.336  60.092  1.00 30.87 ? 577  LEU B CD2   1 
ATOM   12965 N N     . PRO B  1 580  ? 25.164  24.334  59.546  1.00 27.57 ? 578  PRO B N     1 
ATOM   12966 C CA    . PRO B  1 580  ? 24.821  25.631  58.951  1.00 26.71 ? 578  PRO B CA    1 
ATOM   12967 C C     . PRO B  1 580  ? 23.725  25.462  57.911  1.00 26.84 ? 578  PRO B C     1 
ATOM   12968 O O     . PRO B  1 580  ? 23.989  25.092  56.762  1.00 30.46 ? 578  PRO B O     1 
ATOM   12969 C CB    . PRO B  1 580  ? 26.137  26.103  58.318  1.00 28.10 ? 578  PRO B CB    1 
ATOM   12970 C CG    . PRO B  1 580  ? 27.202  25.128  58.808  1.00 29.67 ? 578  PRO B CG    1 
ATOM   12971 C CD    . PRO B  1 580  ? 26.482  23.852  59.100  1.00 29.31 ? 578  PRO B CD    1 
ATOM   12972 N N     . GLN B  1 581  ? 22.484  25.695  58.323  1.00 28.58 ? 579  GLN B N     1 
ATOM   12973 C CA    . GLN B  1 581  ? 21.308  25.558  57.460  1.00 31.23 ? 579  GLN B CA    1 
ATOM   12974 C C     . GLN B  1 581  ? 21.048  26.870  56.736  1.00 26.81 ? 579  GLN B C     1 
ATOM   12975 O O     . GLN B  1 581  ? 20.359  27.751  57.240  1.00 28.70 ? 579  GLN B O     1 
ATOM   12976 C CB    . GLN B  1 581  ? 20.094  25.153  58.286  1.00 29.06 ? 579  GLN B CB    1 
ATOM   12977 C CG    . GLN B  1 581  ? 20.274  23.817  58.948  1.00 32.72 ? 579  GLN B CG    1 
ATOM   12978 C CD    . GLN B  1 581  ? 20.190  22.652  57.980  1.00 37.32 ? 579  GLN B CD    1 
ATOM   12979 O OE1   . GLN B  1 581  ? 19.944  22.827  56.778  1.00 35.30 ? 579  GLN B OE1   1 
ATOM   12980 N NE2   . GLN B  1 581  ? 20.381  21.444  58.507  1.00 38.94 ? 579  GLN B NE2   1 
ATOM   12981 N N     . LEU B  1 582  ? 21.610  27.008  55.547  1.00 27.44 ? 580  LEU B N     1 
ATOM   12982 C CA    . LEU B  1 582  ? 21.312  28.161  54.716  1.00 27.20 ? 580  LEU B CA    1 
ATOM   12983 C C     . LEU B  1 582  ? 20.059  27.875  53.877  1.00 33.18 ? 580  LEU B C     1 
ATOM   12984 O O     . LEU B  1 582  ? 19.543  26.755  53.849  1.00 32.43 ? 580  LEU B O     1 
ATOM   12985 C CB    . LEU B  1 582  ? 22.519  28.508  53.837  1.00 31.65 ? 580  LEU B CB    1 
ATOM   12986 C CG    . LEU B  1 582  ? 23.670  29.291  54.510  1.00 35.01 ? 580  LEU B CG    1 
ATOM   12987 C CD1   . LEU B  1 582  ? 24.329  28.514  55.646  1.00 32.40 ? 580  LEU B CD1   1 
ATOM   12988 C CD2   . LEU B  1 582  ? 24.715  29.736  53.491  1.00 38.86 ? 580  LEU B CD2   1 
ATOM   12989 N N     . ALA B  1 583  ? 19.546  28.917  53.222  1.00 30.74 ? 581  ALA B N     1 
ATOM   12990 C CA    . ALA B  1 583  ? 18.369  28.744  52.374  1.00 36.50 ? 581  ALA B CA    1 
ATOM   12991 C C     . ALA B  1 583  ? 18.594  27.657  51.325  1.00 37.52 ? 581  ALA B C     1 
ATOM   12992 O O     . ALA B  1 583  ? 17.700  26.843  51.055  1.00 42.44 ? 581  ALA B O     1 
ATOM   12993 C CB    . ALA B  1 583  ? 18.012  30.073  51.709  1.00 34.97 ? 581  ALA B CB    1 
ATOM   12994 N N     . THR B  1 584  ? 19.785  27.607  50.747  1.00 35.36 ? 582  THR B N     1 
ATOM   12995 C CA    . THR B  1 584  ? 20.098  26.642  49.697  1.00 34.12 ? 582  THR B CA    1 
ATOM   12996 C C     . THR B  1 584  ? 20.421  25.254  50.231  1.00 35.22 ? 582  THR B C     1 
ATOM   12997 O O     . THR B  1 584  ? 20.766  24.371  49.443  1.00 34.16 ? 582  THR B O     1 
ATOM   12998 C CB    . THR B  1 584  ? 21.275  27.144  48.870  1.00 36.17 ? 582  THR B CB    1 
ATOM   12999 O OG1   . THR B  1 584  ? 22.331  27.523  49.761  1.00 41.03 ? 582  THR B OG1   1 
ATOM   13000 C CG2   . THR B  1 584  ? 20.870  28.345  48.040  1.00 40.75 ? 582  THR B CG2   1 
ATOM   13001 N N     . GLY B  1 585  ? 20.338  25.034  51.539  1.00 33.93 ? 583  GLY B N     1 
ATOM   13002 C CA    . GLY B  1 585  ? 20.612  23.732  52.087  1.00 32.97 ? 583  GLY B CA    1 
ATOM   13003 C C     . GLY B  1 585  ? 21.772  23.799  53.050  1.00 35.25 ? 583  GLY B C     1 
ATOM   13004 O O     . GLY B  1 585  ? 22.376  24.858  53.245  1.00 32.98 ? 583  GLY B O     1 
ATOM   13005 N N     . PRO B  1 586  ? 22.101  22.672  53.681  1.00 34.73 ? 584  PRO B N     1 
ATOM   13006 C CA    . PRO B  1 586  ? 23.184  22.677  54.670  1.00 33.94 ? 584  PRO B CA    1 
ATOM   13007 C C     . PRO B  1 586  ? 24.546  22.877  54.024  1.00 33.98 ? 584  PRO B C     1 
ATOM   13008 O O     . PRO B  1 586  ? 24.862  22.296  52.982  1.00 33.41 ? 584  PRO B O     1 
ATOM   13009 C CB    . PRO B  1 586  ? 23.071  21.299  55.336  1.00 33.51 ? 584  PRO B CB    1 
ATOM   13010 C CG    . PRO B  1 586  ? 22.364  20.447  54.311  1.00 36.73 ? 584  PRO B CG    1 
ATOM   13011 C CD    . PRO B  1 586  ? 21.393  21.379  53.640  1.00 30.86 ? 584  PRO B CD    1 
ATOM   13012 N N     . ALA B  1 587  ? 25.354  23.713  54.665  1.00 32.41 ? 585  ALA B N     1 
ATOM   13013 C CA    . ALA B  1 587  ? 26.703  24.027  54.215  1.00 33.99 ? 585  ALA B CA    1 
ATOM   13014 C C     . ALA B  1 587  ? 27.726  23.144  54.917  1.00 32.29 ? 585  ALA B C     1 
ATOM   13015 O O     . ALA B  1 587  ? 27.540  22.732  56.065  1.00 34.15 ? 585  ALA B O     1 
ATOM   13016 C CB    . ALA B  1 587  ? 27.028  25.500  54.488  1.00 31.03 ? 585  ALA B CB    1 
ATOM   13017 N N     . ALA B  1 588  ? 28.817  22.867  54.218  1.00 32.47 ? 586  ALA B N     1 
ATOM   13018 C CA    . ALA B  1 588  ? 29.933  22.151  54.815  1.00 34.98 ? 586  ALA B CA    1 
ATOM   13019 C C     . ALA B  1 588  ? 30.672  23.056  55.799  1.00 36.30 ? 586  ALA B C     1 
ATOM   13020 O O     . ALA B  1 588  ? 30.548  24.282  55.762  1.00 36.57 ? 586  ALA B O     1 
ATOM   13021 C CB    . ALA B  1 588  ? 30.884  21.644  53.732  1.00 37.70 ? 586  ALA B CB    1 
ATOM   13022 N N     . GLY B  1 589  ? 31.433  22.437  56.694  1.00 34.80 ? 587  GLY B N     1 
ATOM   13023 C CA    . GLY B  1 589  ? 32.193  23.197  57.672  1.00 39.07 ? 587  GLY B CA    1 
ATOM   13024 C C     . GLY B  1 589  ? 32.938  22.281  58.619  1.00 40.08 ? 587  GLY B C     1 
ATOM   13025 O O     . GLY B  1 589  ? 32.988  21.066  58.425  1.00 38.65 ? 587  GLY B O     1 
ATOM   13026 N N     . GLU B  1 590  ? 33.517  22.886  59.660  1.00 39.33 ? 588  GLU B N     1 
ATOM   13027 C CA    . GLU B  1 590  ? 34.281  22.139  60.653  1.00 37.15 ? 588  GLU B CA    1 
ATOM   13028 C C     . GLU B  1 590  ? 33.331  21.496  61.658  1.00 37.02 ? 588  GLU B C     1 
ATOM   13029 O O     . GLU B  1 590  ? 32.431  22.155  62.178  1.00 33.75 ? 588  GLU B O     1 
ATOM   13030 C CB    . GLU B  1 590  ? 35.261  23.063  61.373  1.00 36.75 ? 588  GLU B CB    1 
ATOM   13031 N N     . THR B  1 591  ? 33.535  20.214  61.940  1.00 39.76 ? 589  THR B N     1 
ATOM   13032 C CA    . THR B  1 591  ? 32.606  19.440  62.753  1.00 40.37 ? 589  THR B CA    1 
ATOM   13033 C C     . THR B  1 591  ? 33.262  19.006  64.059  1.00 41.40 ? 589  THR B C     1 
ATOM   13034 O O     . THR B  1 591  ? 34.434  18.614  64.074  1.00 39.51 ? 589  THR B O     1 
ATOM   13035 C CB    . THR B  1 591  ? 32.112  18.217  61.972  1.00 42.31 ? 589  THR B CB    1 
ATOM   13036 O OG1   . THR B  1 591  ? 31.417  18.661  60.799  1.00 40.45 ? 589  THR B OG1   1 
ATOM   13037 C CG2   . THR B  1 591  ? 31.161  17.375  62.819  1.00 39.64 ? 589  THR B CG2   1 
ATOM   13038 N N     . ARG B  1 592  ? 32.509  19.083  65.156  1.00 38.10 ? 590  ARG B N     1 
ATOM   13039 C CA    . ARG B  1 592  ? 33.006  18.605  66.437  1.00 37.35 ? 590  ARG B CA    1 
ATOM   13040 C C     . ARG B  1 592  ? 31.861  18.009  67.242  1.00 38.11 ? 590  ARG B C     1 
ATOM   13041 O O     . ARG B  1 592  ? 30.686  18.227  66.944  1.00 37.95 ? 590  ARG B O     1 
ATOM   13042 C CB    . ARG B  1 592  ? 33.684  19.723  67.228  1.00 43.52 ? 590  ARG B CB    1 
ATOM   13043 C CG    . ARG B  1 592  ? 32.758  20.839  67.607  1.00 41.21 ? 590  ARG B CG    1 
ATOM   13044 C CD    . ARG B  1 592  ? 33.306  21.632  68.789  1.00 49.16 ? 590  ARG B CD    1 
ATOM   13045 N NE    . ARG B  1 592  ? 32.424  22.738  69.148  1.00 45.26 ? 590  ARG B NE    1 
ATOM   13046 C CZ    . ARG B  1 592  ? 31.395  22.647  69.981  1.00 48.91 ? 590  ARG B CZ    1 
ATOM   13047 N NH1   . ARG B  1 592  ? 31.105  21.514  70.606  1.00 43.59 ? 590  ARG B NH1   1 
ATOM   13048 N NH2   . ARG B  1 592  ? 30.639  23.721  70.194  1.00 43.55 ? 590  ARG B NH2   1 
ATOM   13049 N N     . THR B  1 593  ? 32.216  17.263  68.285  1.00 38.86 ? 591  THR B N     1 
ATOM   13050 C CA    . THR B  1 593  ? 31.199  16.657  69.126  1.00 38.12 ? 591  THR B CA    1 
ATOM   13051 C C     . THR B  1 593  ? 30.683  17.639  70.174  1.00 36.68 ? 591  THR B C     1 
ATOM   13052 O O     . THR B  1 593  ? 31.402  18.515  70.662  1.00 37.56 ? 591  THR B O     1 
ATOM   13053 C CB    . THR B  1 593  ? 31.738  15.400  69.809  1.00 39.29 ? 591  THR B CB    1 
ATOM   13054 O OG1   . THR B  1 593  ? 32.827  15.752  70.669  1.00 41.71 ? 591  THR B OG1   1 
ATOM   13055 C CG2   . THR B  1 593  ? 32.204  14.405  68.766  1.00 40.51 ? 591  THR B CG2   1 
ATOM   13056 N N     . VAL B  1 594  ? 29.410  17.491  70.500  1.00 35.43 ? 592  VAL B N     1 
ATOM   13057 C CA    . VAL B  1 594  ? 28.770  18.213  71.588  1.00 33.19 ? 592  VAL B CA    1 
ATOM   13058 C C     . VAL B  1 594  ? 28.708  17.255  72.765  1.00 36.13 ? 592  VAL B C     1 
ATOM   13059 O O     . VAL B  1 594  ? 28.264  16.109  72.616  1.00 31.80 ? 592  VAL B O     1 
ATOM   13060 C CB    . VAL B  1 594  ? 27.371  18.703  71.174  1.00 34.55 ? 592  VAL B CB    1 
ATOM   13061 C CG1   . VAL B  1 594  ? 26.716  19.528  72.277  1.00 27.57 ? 592  VAL B CG1   1 
ATOM   13062 C CG2   . VAL B  1 594  ? 27.461  19.523  69.892  1.00 32.79 ? 592  VAL B CG2   1 
ATOM   13063 N N     . LEU B  1 595  ? 29.189  17.697  73.924  1.00 36.63 ? 593  LEU B N     1 
ATOM   13064 C CA    . LEU B  1 595  ? 29.318  16.817  75.074  1.00 35.13 ? 593  LEU B CA    1 
ATOM   13065 C C     . LEU B  1 595  ? 28.359  17.238  76.180  1.00 31.73 ? 593  LEU B C     1 
ATOM   13066 O O     . LEU B  1 595  ? 27.965  18.402  76.278  1.00 34.70 ? 593  LEU B O     1 
ATOM   13067 C CB    . LEU B  1 595  ? 30.756  16.807  75.610  1.00 36.70 ? 593  LEU B CB    1 
ATOM   13068 C CG    . LEU B  1 595  ? 31.883  16.351  74.683  1.00 36.10 ? 593  LEU B CG    1 
ATOM   13069 C CD1   . LEU B  1 595  ? 33.197  16.299  75.461  1.00 41.50 ? 593  LEU B CD1   1 
ATOM   13070 C CD2   . LEU B  1 595  ? 31.566  15.004  74.056  1.00 37.91 ? 593  LEU B CD2   1 
ATOM   13071 N N     . ASN B  1 596  ? 27.971  16.263  76.987  1.00 32.59 ? 594  ASN B N     1 
ATOM   13072 C CA    . ASN B  1 596  ? 27.129  16.487  78.169  1.00 30.83 ? 594  ASN B CA    1 
ATOM   13073 C C     . ASN B  1 596  ? 27.953  17.179  79.250  1.00 29.88 ? 594  ASN B C     1 
ATOM   13074 O O     . ASN B  1 596  ? 28.961  16.615  79.694  1.00 29.75 ? 594  ASN B O     1 
ATOM   13075 C CB    . ASN B  1 596  ? 26.611  15.126  78.652  1.00 31.61 ? 594  ASN B CB    1 
ATOM   13076 C CG    . ASN B  1 596  ? 25.502  15.226  79.666  1.00 32.66 ? 594  ASN B CG    1 
ATOM   13077 O OD1   . ASN B  1 596  ? 25.474  16.136  80.509  1.00 29.19 ? 594  ASN B OD1   1 
ATOM   13078 N ND2   . ASN B  1 596  ? 24.559  14.275  79.588  1.00 33.47 ? 594  ASN B ND2   1 
ATOM   13079 N N     . PRO B  1 597  ? 27.585  18.386  79.693  1.00 29.85 ? 595  PRO B N     1 
ATOM   13080 C CA    . PRO B  1 597  ? 28.390  19.054  80.732  1.00 30.37 ? 595  PRO B CA    1 
ATOM   13081 C C     . PRO B  1 597  ? 28.430  18.290  82.045  1.00 31.28 ? 595  PRO B C     1 
ATOM   13082 O O     . PRO B  1 597  ? 29.374  18.480  82.820  1.00 29.11 ? 595  PRO B O     1 
ATOM   13083 C CB    . PRO B  1 597  ? 27.714  20.427  80.895  1.00 28.50 ? 595  PRO B CB    1 
ATOM   13084 C CG    . PRO B  1 597  ? 26.372  20.310  80.239  1.00 29.58 ? 595  PRO B CG    1 
ATOM   13085 C CD    . PRO B  1 597  ? 26.484  19.228  79.192  1.00 26.24 ? 595  PRO B CD    1 
ATOM   13086 N N     . GLY B  1 598  ? 27.445  17.426  82.319  1.00 30.69 ? 596  GLY B N     1 
ATOM   13087 C CA    . GLY B  1 598  ? 27.471  16.605  83.516  1.00 30.16 ? 596  GLY B CA    1 
ATOM   13088 C C     . GLY B  1 598  ? 28.300  15.345  83.405  1.00 34.54 ? 596  GLY B C     1 
ATOM   13089 O O     . GLY B  1 598  ? 28.528  14.670  84.411  1.00 37.02 ? 596  GLY B O     1 
ATOM   13090 N N     . ASP B  1 599  ? 28.768  15.026  82.203  1.00 31.72 ? 597  ASP B N     1 
ATOM   13091 C CA    . ASP B  1 599  ? 29.512  13.800  81.955  1.00 35.29 ? 597  ASP B CA    1 
ATOM   13092 C C     . ASP B  1 599  ? 30.054  13.849  80.536  1.00 35.74 ? 597  ASP B C     1 
ATOM   13093 O O     . ASP B  1 599  ? 29.337  13.524  79.588  1.00 34.15 ? 597  ASP B O     1 
ATOM   13094 C CB    . ASP B  1 599  ? 28.624  12.569  82.153  1.00 37.47 ? 597  ASP B CB    1 
ATOM   13095 C CG    . ASP B  1 599  ? 29.412  11.269  82.143  1.00 42.13 ? 597  ASP B CG    1 
ATOM   13096 O OD1   . ASP B  1 599  ? 30.576  11.264  81.670  1.00 40.24 ? 597  ASP B OD1   1 
ATOM   13097 O OD2   . ASP B  1 599  ? 28.861  10.246  82.610  1.00 42.15 ? 597  ASP B OD2   1 
ATOM   13098 N N     . HIS B  1 600  ? 31.317  14.249  80.383  1.00 35.54 ? 598  HIS B N     1 
ATOM   13099 C CA    . HIS B  1 600  ? 31.886  14.458  79.058  1.00 36.37 ? 598  HIS B CA    1 
ATOM   13100 C C     . HIS B  1 600  ? 32.025  13.176  78.256  1.00 36.60 ? 598  HIS B C     1 
ATOM   13101 O O     . HIS B  1 600  ? 32.265  13.250  77.045  1.00 36.99 ? 598  HIS B O     1 
ATOM   13102 C CB    . HIS B  1 600  ? 33.238  15.176  79.182  1.00 37.28 ? 598  HIS B CB    1 
ATOM   13103 C CG    . HIS B  1 600  ? 33.101  16.628  79.523  1.00 36.75 ? 598  HIS B CG    1 
ATOM   13104 N ND1   . HIS B  1 600  ? 34.173  17.493  79.570  1.00 34.51 ? 598  HIS B ND1   1 
ATOM   13105 C CD2   . HIS B  1 600  ? 32.010  17.364  79.846  1.00 31.77 ? 598  HIS B CD2   1 
ATOM   13106 C CE1   . HIS B  1 600  ? 33.749  18.701  79.897  1.00 34.82 ? 598  HIS B CE1   1 
ATOM   13107 N NE2   . HIS B  1 600  ? 32.441  18.649  80.076  1.00 37.31 ? 598  HIS B NE2   1 
ATOM   13108 N N     . ARG B  1 601  ? 31.869  12.010  78.885  1.00 38.35 ? 599  ARG B N     1 
ATOM   13109 C CA    . ARG B  1 601  ? 31.845  10.768  78.132  1.00 38.11 ? 599  ARG B CA    1 
ATOM   13110 C C     . ARG B  1 601  ? 30.556  10.614  77.330  1.00 33.86 ? 599  ARG B C     1 
ATOM   13111 O O     . ARG B  1 601  ? 30.518  9.813   76.390  1.00 37.39 ? 599  ARG B O     1 
ATOM   13112 C CB    . ARG B  1 601  ? 32.015  9.575   79.072  1.00 40.82 ? 599  ARG B CB    1 
ATOM   13113 C CG    . ARG B  1 601  ? 33.263  9.617   79.942  1.00 41.52 ? 599  ARG B CG    1 
ATOM   13114 C CD    . ARG B  1 601  ? 33.169  8.601   81.075  1.00 45.30 ? 599  ARG B CD    1 
ATOM   13115 N NE    . ARG B  1 601  ? 32.050  8.876   81.970  1.00 44.00 ? 599  ARG B NE    1 
ATOM   13116 C CZ    . ARG B  1 601  ? 31.703  8.112   82.999  1.00 45.13 ? 599  ARG B CZ    1 
ATOM   13117 N NH1   . ARG B  1 601  ? 32.373  7.012   83.300  1.00 44.69 ? 599  ARG B NH1   1 
ATOM   13118 N NH2   . ARG B  1 601  ? 30.660  8.466   83.750  1.00 44.60 ? 599  ARG B NH2   1 
ATOM   13119 N N     . ASP B  1 602  ? 29.507  11.344  77.696  1.00 37.62 ? 600  ASP B N     1 
ATOM   13120 C CA    . ASP B  1 602  ? 28.202  11.264  77.040  1.00 36.33 ? 600  ASP B CA    1 
ATOM   13121 C C     . ASP B  1 602  ? 28.235  12.213  75.851  1.00 35.91 ? 600  ASP B C     1 
ATOM   13122 O O     . ASP B  1 602  ? 28.111  13.431  76.008  1.00 37.31 ? 600  ASP B O     1 
ATOM   13123 C CB    . ASP B  1 602  ? 27.088  11.612  78.025  1.00 37.62 ? 600  ASP B CB    1 
ATOM   13124 C CG    . ASP B  1 602  ? 25.698  11.510  77.414  1.00 38.21 ? 600  ASP B CG    1 
ATOM   13125 O OD1   . ASP B  1 602  ? 25.526  10.797  76.403  1.00 39.00 ? 600  ASP B OD1   1 
ATOM   13126 O OD2   . ASP B  1 602  ? 24.775  12.157  77.945  1.00 39.92 ? 600  ASP B OD2   1 
ATOM   13127 N N     . VAL B  1 603  ? 28.428  11.655  74.659  1.00 35.85 ? 601  VAL B N     1 
ATOM   13128 C CA    . VAL B  1 603  ? 28.400  12.432  73.423  1.00 32.95 ? 601  VAL B CA    1 
ATOM   13129 C C     . VAL B  1 603  ? 26.945  12.644  73.007  1.00 36.27 ? 601  VAL B C     1 
ATOM   13130 O O     . VAL B  1 603  ? 26.225  11.685  72.707  1.00 38.88 ? 601  VAL B O     1 
ATOM   13131 C CB    . VAL B  1 603  ? 29.193  11.724  72.317  1.00 35.41 ? 601  VAL B CB    1 
ATOM   13132 C CG1   . VAL B  1 603  ? 29.050  12.471  70.997  1.00 36.42 ? 601  VAL B CG1   1 
ATOM   13133 C CG2   . VAL B  1 603  ? 30.674  11.577  72.731  1.00 36.27 ? 601  VAL B CG2   1 
ATOM   13134 N N     . VAL B  1 604  ? 26.517  13.900  72.975  1.00 31.84 ? 602  VAL B N     1 
ATOM   13135 C CA    . VAL B  1 604  ? 25.117  14.217  72.726  1.00 32.03 ? 602  VAL B CA    1 
ATOM   13136 C C     . VAL B  1 604  ? 24.846  14.325  71.239  1.00 33.26 ? 602  VAL B C     1 
ATOM   13137 O O     . VAL B  1 604  ? 23.782  13.924  70.768  1.00 36.00 ? 602  VAL B O     1 
ATOM   13138 C CB    . VAL B  1 604  ? 24.717  15.514  73.456  1.00 33.54 ? 602  VAL B CB    1 
ATOM   13139 C CG1   . VAL B  1 604  ? 23.236  15.767  73.286  1.00 29.81 ? 602  VAL B CG1   1 
ATOM   13140 C CG2   . VAL B  1 604  ? 25.101  15.448  74.938  1.00 32.79 ? 602  VAL B CG2   1 
ATOM   13141 N N     . GLY B  1 605  ? 25.801  14.861  70.491  1.00 31.34 ? 603  GLY B N     1 
ATOM   13142 C CA    . GLY B  1 605  ? 25.626  14.969  69.059  1.00 33.65 ? 603  GLY B CA    1 
ATOM   13143 C C     . GLY B  1 605  ? 26.836  15.590  68.411  1.00 35.18 ? 603  GLY B C     1 
ATOM   13144 O O     . GLY B  1 605  ? 27.923  15.612  68.986  1.00 32.37 ? 603  GLY B O     1 
ATOM   13145 N N     . SER B  1 606  ? 26.628  16.092  67.198  1.00 34.47 ? 604  SER B N     1 
ATOM   13146 C CA    . SER B  1 606  ? 27.676  16.677  66.379  1.00 33.34 ? 604  SER B CA    1 
ATOM   13147 C C     . SER B  1 606  ? 27.197  18.019  65.861  1.00 31.72 ? 604  SER B C     1 
ATOM   13148 O O     . SER B  1 606  ? 26.042  18.155  65.451  1.00 33.14 ? 604  SER B O     1 
ATOM   13149 C CB    . SER B  1 606  ? 28.043  15.766  65.190  1.00 29.90 ? 604  SER B CB    1 
ATOM   13150 O OG    . SER B  1 606  ? 28.560  14.524  65.647  1.00 40.39 ? 604  SER B OG    1 
ATOM   13151 N N     . VAL B  1 607  ? 28.081  19.011  65.873  1.00 31.48 ? 605  VAL B N     1 
ATOM   13152 C CA    . VAL B  1 607  ? 27.767  20.317  65.308  1.00 30.14 ? 605  VAL B CA    1 
ATOM   13153 C C     . VAL B  1 607  ? 28.777  20.613  64.213  1.00 34.25 ? 605  VAL B C     1 
ATOM   13154 O O     . VAL B  1 607  ? 29.979  20.366  64.367  1.00 33.60 ? 605  VAL B O     1 
ATOM   13155 C CB    . VAL B  1 607  ? 27.748  21.446  66.363  1.00 30.73 ? 605  VAL B CB    1 
ATOM   13156 C CG1   . VAL B  1 607  ? 29.069  21.531  67.131  1.00 33.31 ? 605  VAL B CG1   1 
ATOM   13157 C CG2   . VAL B  1 607  ? 27.425  22.791  65.708  1.00 27.86 ? 605  VAL B CG2   1 
ATOM   13158 N N     . THR B  1 608  ? 28.274  21.107  63.095  1.00 31.35 ? 606  THR B N     1 
ATOM   13159 C CA    . THR B  1 608  ? 29.088  21.581  61.991  1.00 29.29 ? 606  THR B CA    1 
ATOM   13160 C C     . THR B  1 608  ? 29.017  23.103  61.995  1.00 28.85 ? 606  THR B C     1 
ATOM   13161 O O     . THR B  1 608  ? 27.924  23.679  61.942  1.00 29.13 ? 606  THR B O     1 
ATOM   13162 C CB    . THR B  1 608  ? 28.577  20.994  60.678  1.00 32.90 ? 606  THR B CB    1 
ATOM   13163 O OG1   . THR B  1 608  ? 28.720  19.564  60.721  1.00 33.31 ? 606  THR B OG1   1 
ATOM   13164 C CG2   . THR B  1 608  ? 29.348  21.551  59.488  1.00 30.20 ? 606  THR B CG2   1 
ATOM   13165 N N     . GLU B  1 609  ? 30.166  23.762  62.062  1.00 30.64 ? 607  GLU B N     1 
ATOM   13166 C CA    . GLU B  1 609  ? 30.112  25.193  62.330  1.00 31.99 ? 607  GLU B CA    1 
ATOM   13167 C C     . GLU B  1 609  ? 30.307  26.007  61.052  1.00 28.22 ? 607  GLU B C     1 
ATOM   13168 O O     . GLU B  1 609  ? 30.859  25.533  60.052  1.00 29.21 ? 607  GLU B O     1 
ATOM   13169 C CB    . GLU B  1 609  ? 31.118  25.572  63.426  1.00 32.99 ? 607  GLU B CB    1 
ATOM   13170 C CG    . GLU B  1 609  ? 30.683  24.973  64.768  1.00 35.24 ? 607  GLU B CG    1 
ATOM   13171 C CD    . GLU B  1 609  ? 31.486  25.450  65.974  1.00 43.34 ? 607  GLU B CD    1 
ATOM   13172 O OE1   . GLU B  1 609  ? 32.705  25.689  65.827  1.00 44.66 ? 607  GLU B OE1   1 
ATOM   13173 O OE2   . GLU B  1 609  ? 30.885  25.575  67.073  1.00 40.13 ? 607  GLU B OE2   1 
ATOM   13174 N N     . THR B  1 610  ? 29.779  27.233  61.090  1.00 32.40 ? 608  THR B N     1 
ATOM   13175 C CA    . THR B  1 610  ? 29.633  28.067  59.904  1.00 31.89 ? 608  THR B CA    1 
ATOM   13176 C C     . THR B  1 610  ? 30.932  28.808  59.612  1.00 32.61 ? 608  THR B C     1 
ATOM   13177 O O     . THR B  1 610  ? 31.529  29.396  60.515  1.00 35.96 ? 608  THR B O     1 
ATOM   13178 C CB    . THR B  1 610  ? 28.495  29.075  60.106  1.00 34.01 ? 608  THR B CB    1 
ATOM   13179 O OG1   . THR B  1 610  ? 27.319  28.401  60.569  1.00 31.78 ? 608  THR B OG1   1 
ATOM   13180 C CG2   . THR B  1 610  ? 28.171  29.789  58.803  1.00 34.91 ? 608  THR B CG2   1 
ATOM   13181 N N     . SER B  1 611  ? 31.367  28.790  58.356  1.00 30.19 ? 609  SER B N     1 
ATOM   13182 C CA    . SER B  1 611  ? 32.458  29.673  57.976  1.00 36.12 ? 609  SER B CA    1 
ATOM   13183 C C     . SER B  1 611  ? 31.968  31.116  57.922  1.00 37.82 ? 609  SER B C     1 
ATOM   13184 O O     . SER B  1 611  ? 30.772  31.392  57.766  1.00 36.27 ? 609  SER B O     1 
ATOM   13185 C CB    . SER B  1 611  ? 33.053  29.258  56.626  1.00 36.93 ? 609  SER B CB    1 
ATOM   13186 O OG    . SER B  1 611  ? 32.117  29.435  55.579  1.00 36.59 ? 609  SER B OG    1 
ATOM   13187 N N     . GLU B  1 612  ? 32.908  32.053  58.075  1.00 38.78 ? 610  GLU B N     1 
ATOM   13188 C CA    . GLU B  1 612  ? 32.543  33.466  57.978  1.00 42.76 ? 610  GLU B CA    1 
ATOM   13189 C C     . GLU B  1 612  ? 31.996  33.798  56.594  1.00 40.24 ? 610  GLU B C     1 
ATOM   13190 O O     . GLU B  1 612  ? 31.055  34.590  56.462  1.00 39.13 ? 610  GLU B O     1 
ATOM   13191 C CB    . GLU B  1 612  ? 33.749  34.354  58.298  1.00 47.60 ? 610  GLU B CB    1 
ATOM   13192 C CG    . GLU B  1 612  ? 34.026  34.547  59.777  1.00 48.33 ? 610  GLU B CG    1 
ATOM   13193 C CD    . GLU B  1 612  ? 35.189  35.509  60.032  1.00 54.92 ? 610  GLU B CD    1 
ATOM   13194 O OE1   . GLU B  1 612  ? 35.333  36.493  59.273  1.00 59.83 ? 610  GLU B OE1   1 
ATOM   13195 O OE2   . GLU B  1 612  ? 35.958  35.278  60.989  1.00 50.94 ? 610  GLU B OE2   1 
ATOM   13196 N N     . GLU B  1 613  ? 32.581  33.212  55.544  1.00 40.70 ? 611  GLU B N     1 
ATOM   13197 C CA    . GLU B  1 613  ? 32.074  33.463  54.198  1.00 35.71 ? 611  GLU B CA    1 
ATOM   13198 C C     . GLU B  1 613  ? 30.628  32.997  54.069  1.00 40.34 ? 611  GLU B C     1 
ATOM   13199 O O     . GLU B  1 613  ? 29.808  33.679  53.448  1.00 39.38 ? 611  GLU B O     1 
ATOM   13200 C CB    . GLU B  1 613  ? 32.960  32.781  53.150  1.00 41.08 ? 611  GLU B CB    1 
ATOM   13201 N N     . ASP B  1 614  ? 30.297  31.844  54.664  1.00 38.03 ? 612  ASP B N     1 
ATOM   13202 C CA    . ASP B  1 614  ? 28.927  31.344  54.600  1.00 36.37 ? 612  ASP B CA    1 
ATOM   13203 C C     . ASP B  1 614  ? 27.992  32.175  55.464  1.00 38.47 ? 612  ASP B C     1 
ATOM   13204 O O     . ASP B  1 614  ? 26.791  32.255  55.174  1.00 35.13 ? 612  ASP B O     1 
ATOM   13205 C CB    . ASP B  1 614  ? 28.871  29.872  55.022  1.00 36.42 ? 612  ASP B CB    1 
ATOM   13206 C CG    . ASP B  1 614  ? 29.296  28.923  53.913  1.00 42.02 ? 612  ASP B CG    1 
ATOM   13207 O OD1   . ASP B  1 614  ? 29.246  29.317  52.720  1.00 41.48 ? 612  ASP B OD1   1 
ATOM   13208 O OD2   . ASP B  1 614  ? 29.675  27.772  54.233  1.00 42.83 ? 612  ASP B OD2   1 
ATOM   13209 N N     . ALA B  1 615  ? 28.510  32.795  56.530  1.00 33.26 ? 613  ALA B N     1 
ATOM   13210 C CA    . ALA B  1 615  ? 27.651  33.673  57.316  1.00 35.82 ? 613  ALA B CA    1 
ATOM   13211 C C     . ALA B  1 615  ? 27.242  34.887  56.498  1.00 37.59 ? 613  ALA B C     1 
ATOM   13212 O O     . ALA B  1 615  ? 26.069  35.283  56.498  1.00 32.35 ? 613  ALA B O     1 
ATOM   13213 C CB    . ALA B  1 615  ? 28.351  34.098  58.603  1.00 32.50 ? 613  ALA B CB    1 
ATOM   13214 N N     . ARG B  1 616  ? 28.195  35.474  55.772  1.00 33.64 ? 614  ARG B N     1 
ATOM   13215 C CA    . ARG B  1 616  ? 27.859  36.575  54.877  1.00 37.30 ? 614  ARG B CA    1 
ATOM   13216 C C     . ARG B  1 616  ? 26.896  36.126  53.783  1.00 36.97 ? 614  ARG B C     1 
ATOM   13217 O O     . ARG B  1 616  ? 25.960  36.855  53.435  1.00 38.01 ? 614  ARG B O     1 
ATOM   13218 C CB    . ARG B  1 616  ? 29.138  37.176  54.290  1.00 41.03 ? 614  ARG B CB    1 
ATOM   13219 C CG    . ARG B  1 616  ? 29.927  37.971  55.330  1.00 40.96 ? 614  ARG B CG    1 
ATOM   13220 C CD    . ARG B  1 616  ? 31.122  38.707  54.734  1.00 45.59 ? 614  ARG B CD    1 
ATOM   13221 N NE    . ARG B  1 616  ? 32.231  37.805  54.460  1.00 51.25 ? 614  ARG B NE    1 
ATOM   13222 C CZ    . ARG B  1 616  ? 33.125  37.429  55.363  1.00 50.63 ? 614  ARG B CZ    1 
ATOM   13223 N NH1   . ARG B  1 616  ? 33.090  37.890  56.605  1.00 50.66 ? 614  ARG B NH1   1 
ATOM   13224 N NH2   . ARG B  1 616  ? 34.063  36.553  55.020  1.00 47.95 ? 614  ARG B NH2   1 
ATOM   13225 N N     . ARG B  1 617  ? 27.089  34.918  53.248  1.00 37.32 ? 615  ARG B N     1 
ATOM   13226 C CA    . ARG B  1 617  ? 26.188  34.426  52.210  1.00 38.67 ? 615  ARG B CA    1 
ATOM   13227 C C     . ARG B  1 617  ? 24.774  34.257  52.753  1.00 33.00 ? 615  ARG B C     1 
ATOM   13228 O O     . ARG B  1 617  ? 23.800  34.615  52.086  1.00 32.82 ? 615  ARG B O     1 
ATOM   13229 C CB    . ARG B  1 617  ? 26.717  33.111  51.630  1.00 37.56 ? 615  ARG B CB    1 
ATOM   13230 C CG    . ARG B  1 617  ? 25.834  32.484  50.548  1.00 38.02 ? 615  ARG B CG    1 
ATOM   13231 C CD    . ARG B  1 617  ? 26.628  31.546  49.620  1.00 45.20 ? 615  ARG B CD    1 
ATOM   13232 N NE    . ARG B  1 617  ? 26.937  30.259  50.241  1.00 44.11 ? 615  ARG B NE    1 
ATOM   13233 C CZ    . ARG B  1 617  ? 26.069  29.261  50.372  1.00 48.91 ? 615  ARG B CZ    1 
ATOM   13234 N NH1   . ARG B  1 617  ? 24.814  29.371  49.956  1.00 46.27 ? 615  ARG B NH1   1 
ATOM   13235 N NH2   . ARG B  1 617  ? 26.465  28.126  50.941  1.00 44.75 ? 615  ARG B NH2   1 
ATOM   13236 N N     . ALA B  1 618  ? 24.646  33.752  53.982  1.00 35.25 ? 616  ALA B N     1 
ATOM   13237 C CA    . ALA B  1 618  ? 23.336  33.639  54.625  1.00 31.25 ? 616  ALA B CA    1 
ATOM   13238 C C     . ALA B  1 618  ? 22.606  34.975  54.658  1.00 31.31 ? 616  ALA B C     1 
ATOM   13239 O O     . ALA B  1 618  ? 21.396  35.043  54.402  1.00 29.43 ? 616  ALA B O     1 
ATOM   13240 C CB    . ALA B  1 618  ? 23.509  33.111  56.050  1.00 29.15 ? 616  ALA B CB    1 
ATOM   13241 N N     . VAL B  1 619  ? 23.319  36.044  55.018  1.00 34.18 ? 617  VAL B N     1 
ATOM   13242 C CA    . VAL B  1 619  ? 22.683  37.351  55.122  1.00 35.08 ? 617  VAL B CA    1 
ATOM   13243 C C     . VAL B  1 619  ? 22.230  37.834  53.747  1.00 34.60 ? 617  VAL B C     1 
ATOM   13244 O O     . VAL B  1 619  ? 21.159  38.439  53.610  1.00 38.31 ? 617  VAL B O     1 
ATOM   13245 C CB    . VAL B  1 619  ? 23.627  38.358  55.805  1.00 34.61 ? 617  VAL B CB    1 
ATOM   13246 C CG1   . VAL B  1 619  ? 22.953  39.708  55.897  1.00 34.62 ? 617  VAL B CG1   1 
ATOM   13247 C CG2   . VAL B  1 619  ? 24.009  37.870  57.200  1.00 31.44 ? 617  VAL B CG2   1 
ATOM   13248 N N     . ARG B  1 620  ? 23.014  37.553  52.704  1.00 37.45 ? 618  ARG B N     1 
ATOM   13249 C CA    . ARG B  1 620  ? 22.588  37.930  51.359  1.00 35.07 ? 618  ARG B CA    1 
ATOM   13250 C C     . ARG B  1 620  ? 21.369  37.129  50.922  1.00 36.47 ? 618  ARG B C     1 
ATOM   13251 O O     . ARG B  1 620  ? 20.465  37.671  50.276  1.00 35.58 ? 618  ARG B O     1 
ATOM   13252 C CB    . ARG B  1 620  ? 23.737  37.759  50.366  1.00 40.75 ? 618  ARG B CB    1 
ATOM   13253 C CG    . ARG B  1 620  ? 24.713  38.922  50.390  1.00 45.16 ? 618  ARG B CG    1 
ATOM   13254 C CD    . ARG B  1 620  ? 25.630  38.931  49.175  1.00 46.91 ? 618  ARG B CD    1 
ATOM   13255 N NE    . ARG B  1 620  ? 26.334  37.664  49.028  1.00 54.79 ? 618  ARG B NE    1 
ATOM   13256 C CZ    . ARG B  1 620  ? 27.412  37.319  49.721  1.00 52.86 ? 618  ARG B CZ    1 
ATOM   13257 N NH1   . ARG B  1 620  ? 27.947  38.132  50.620  1.00 52.29 ? 618  ARG B NH1   1 
ATOM   13258 N NH2   . ARG B  1 620  ? 27.959  36.125  49.514  1.00 50.13 ? 618  ARG B NH2   1 
ATOM   13259 N N     . LEU B  1 621  ? 21.323  35.835  51.261  1.00 34.29 ? 619  LEU B N     1 
ATOM   13260 C CA    . LEU B  1 621  ? 20.137  35.040  50.948  1.00 32.40 ? 619  LEU B CA    1 
ATOM   13261 C C     . LEU B  1 621  ? 18.918  35.547  51.715  1.00 32.94 ? 619  LEU B C     1 
ATOM   13262 O O     . LEU B  1 621  ? 17.790  35.530  51.196  1.00 31.56 ? 619  LEU B O     1 
ATOM   13263 C CB    . LEU B  1 621  ? 20.397  33.564  51.254  1.00 34.36 ? 619  LEU B CB    1 
ATOM   13264 C CG    . LEU B  1 621  ? 21.342  32.774  50.341  1.00 35.31 ? 619  LEU B CG    1 
ATOM   13265 C CD1   . LEU B  1 621  ? 21.781  31.486  51.012  1.00 36.40 ? 619  LEU B CD1   1 
ATOM   13266 C CD2   . LEU B  1 621  ? 20.673  32.458  49.002  1.00 36.02 ? 619  LEU B CD2   1 
ATOM   13267 N N     . ALA B  1 622  ? 19.122  35.989  52.959  1.00 32.19 ? 620  ALA B N     1 
ATOM   13268 C CA    . ALA B  1 622  ? 18.017  36.571  53.715  1.00 33.02 ? 620  ALA B CA    1 
ATOM   13269 C C     . ALA B  1 622  ? 17.569  37.891  53.100  1.00 31.57 ? 620  ALA B C     1 
ATOM   13270 O O     . ALA B  1 622  ? 16.369  38.172  53.027  1.00 33.77 ? 620  ALA B O     1 
ATOM   13271 C CB    . ALA B  1 622  ? 18.417  36.762  55.180  1.00 31.12 ? 620  ALA B CB    1 
ATOM   13272 N N     . ALA B  1 623  ? 18.514  38.707  52.626  1.00 31.93 ? 621  ALA B N     1 
ATOM   13273 C CA    . ALA B  1 623  ? 18.128  39.983  52.033  1.00 33.84 ? 621  ALA B CA    1 
ATOM   13274 C C     . ALA B  1 623  ? 17.332  39.786  50.746  1.00 35.24 ? 621  ALA B C     1 
ATOM   13275 O O     . ALA B  1 623  ? 16.334  40.484  50.512  1.00 34.20 ? 621  ALA B O     1 
ATOM   13276 C CB    . ALA B  1 623  ? 19.368  40.834  51.777  1.00 32.00 ? 621  ALA B CB    1 
ATOM   13277 N N     . ASP B  1 624  ? 17.738  38.825  49.914  1.00 33.02 ? 622  ASP B N     1 
ATOM   13278 C CA    . ASP B  1 624  ? 17.045  38.609  48.646  1.00 34.10 ? 622  ASP B CA    1 
ATOM   13279 C C     . ASP B  1 624  ? 15.632  38.096  48.863  1.00 36.55 ? 622  ASP B C     1 
ATOM   13280 O O     . ASP B  1 624  ? 14.742  38.388  48.061  1.00 36.59 ? 622  ASP B O     1 
ATOM   13281 C CB    . ASP B  1 624  ? 17.830  37.639  47.768  1.00 42.25 ? 622  ASP B CB    1 
ATOM   13282 C CG    . ASP B  1 624  ? 19.196  38.175  47.387  1.00 47.62 ? 622  ASP B CG    1 
ATOM   13283 O OD1   . ASP B  1 624  ? 19.397  39.410  47.470  1.00 53.35 ? 622  ASP B OD1   1 
ATOM   13284 O OD2   . ASP B  1 624  ? 20.072  37.364  47.010  1.00 55.59 ? 622  ASP B OD2   1 
ATOM   13285 N N     . ALA B  1 625  ? 15.395  37.368  49.951  1.00 34.10 ? 623  ALA B N     1 
ATOM   13286 C CA    . ALA B  1 625  ? 14.074  36.838  50.256  1.00 36.80 ? 623  ALA B CA    1 
ATOM   13287 C C     . ALA B  1 625  ? 13.273  37.711  51.216  1.00 34.07 ? 623  ALA B C     1 
ATOM   13288 O O     . ALA B  1 625  ? 12.121  37.378  51.514  1.00 33.46 ? 623  ALA B O     1 
ATOM   13289 C CB    . ALA B  1 625  ? 14.194  35.432  50.839  1.00 38.58 ? 623  ALA B CB    1 
ATOM   13290 N N     . ALA B  1 626  ? 13.851  38.802  51.718  1.00 30.95 ? 624  ALA B N     1 
ATOM   13291 C CA    . ALA B  1 626  ? 13.124  39.646  52.666  1.00 32.90 ? 624  ALA B CA    1 
ATOM   13292 C C     . ALA B  1 626  ? 11.772  40.132  52.145  1.00 31.30 ? 624  ALA B C     1 
ATOM   13293 O O     . ALA B  1 626  ? 10.804  40.117  52.925  1.00 33.82 ? 624  ALA B O     1 
ATOM   13294 C CB    . ALA B  1 626  ? 14.004  40.836  53.084  1.00 27.57 ? 624  ALA B CB    1 
ATOM   13295 N N     . PRO B  1 627  ? 11.624  40.587  50.895  1.00 31.63 ? 625  PRO B N     1 
ATOM   13296 C CA    . PRO B  1 627  ? 10.291  41.047  50.477  1.00 32.02 ? 625  PRO B CA    1 
ATOM   13297 C C     . PRO B  1 627  ? 9.259   39.933  50.421  1.00 33.43 ? 625  PRO B C     1 
ATOM   13298 O O     . PRO B  1 627  ? 8.088   40.182  50.720  1.00 31.39 ? 625  PRO B O     1 
ATOM   13299 C CB    . PRO B  1 627  ? 10.551  41.669  49.094  1.00 37.01 ? 625  PRO B CB    1 
ATOM   13300 C CG    . PRO B  1 627  ? 12.001  41.945  49.053  1.00 34.75 ? 625  PRO B CG    1 
ATOM   13301 C CD    . PRO B  1 627  ? 12.639  40.866  49.862  1.00 34.65 ? 625  PRO B CD    1 
ATOM   13302 N N     . ASP B  1 628  ? 9.652   38.709  50.042  1.00 31.76 ? 626  ASP B N     1 
ATOM   13303 C CA    . ASP B  1 628  ? 8.687   37.612  49.993  1.00 30.93 ? 626  ASP B CA    1 
ATOM   13304 C C     . ASP B  1 628  ? 8.143   37.283  51.379  1.00 32.75 ? 626  ASP B C     1 
ATOM   13305 O O     . ASP B  1 628  ? 6.952   36.987  51.536  1.00 29.36 ? 626  ASP B O     1 
ATOM   13306 C CB    . ASP B  1 628  ? 9.325   36.372  49.380  1.00 31.15 ? 626  ASP B CB    1 
ATOM   13307 C CG    . ASP B  1 628  ? 9.539   36.507  47.890  1.00 39.89 ? 626  ASP B CG    1 
ATOM   13308 O OD1   . ASP B  1 628  ? 9.015   37.472  47.291  1.00 40.99 ? 626  ASP B OD1   1 
ATOM   13309 O OD2   . ASP B  1 628  ? 10.237  35.643  47.329  1.00 44.40 ? 626  ASP B OD2   1 
ATOM   13310 N N     . TRP B  1 629  ? 9.001   37.310  52.394  1.00 28.74 ? 627  TRP B N     1 
ATOM   13311 C CA    . TRP B  1 629  ? 8.522   37.028  53.743  1.00 28.52 ? 627  TRP B CA    1 
ATOM   13312 C C     . TRP B  1 629  ? 7.683   38.185  54.279  1.00 28.45 ? 627  TRP B C     1 
ATOM   13313 O O     . TRP B  1 629  ? 6.656   37.967  54.932  1.00 27.68 ? 627  TRP B O     1 
ATOM   13314 C CB    . TRP B  1 629  ? 9.712   36.716  54.669  1.00 28.72 ? 627  TRP B CB    1 
ATOM   13315 C CG    . TRP B  1 629  ? 9.269   36.433  56.063  1.00 24.75 ? 627  TRP B CG    1 
ATOM   13316 C CD1   . TRP B  1 629  ? 9.599   37.128  57.192  1.00 24.60 ? 627  TRP B CD1   1 
ATOM   13317 C CD2   . TRP B  1 629  ? 8.367   35.404  56.472  1.00 26.24 ? 627  TRP B CD2   1 
ATOM   13318 N NE1   . TRP B  1 629  ? 8.956   36.592  58.278  1.00 21.48 ? 627  TRP B NE1   1 
ATOM   13319 C CE2   . TRP B  1 629  ? 8.198   35.528  57.868  1.00 20.79 ? 627  TRP B CE2   1 
ATOM   13320 C CE3   . TRP B  1 629  ? 7.686   34.383  55.798  1.00 25.16 ? 627  TRP B CE3   1 
ATOM   13321 C CZ2   . TRP B  1 629  ? 7.380   34.666  58.609  1.00 24.88 ? 627  TRP B CZ2   1 
ATOM   13322 C CZ3   . TRP B  1 629  ? 6.848   33.533  56.540  1.00 24.88 ? 627  TRP B CZ3   1 
ATOM   13323 C CH2   . TRP B  1 629  ? 6.709   33.681  57.926  1.00 27.30 ? 627  TRP B CH2   1 
ATOM   13324 N N     . ALA B  1 630  ? 8.080   39.424  53.984  1.00 29.79 ? 628  ALA B N     1 
ATOM   13325 C CA    . ALA B  1 630  ? 7.301   40.571  54.455  1.00 30.35 ? 628  ALA B CA    1 
ATOM   13326 C C     . ALA B  1 630  ? 5.883   40.561  53.893  1.00 31.56 ? 628  ALA B C     1 
ATOM   13327 O O     . ALA B  1 630  ? 4.946   41.039  54.552  1.00 30.62 ? 628  ALA B O     1 
ATOM   13328 C CB    . ALA B  1 630  ? 8.009   41.875  54.077  1.00 30.99 ? 628  ALA B CB    1 
ATOM   13329 N N     . ALA B  1 631  ? 5.706   40.020  52.682  1.00 28.70 ? 629  ALA B N     1 
ATOM   13330 C CA    . ALA B  1 631  ? 4.411   39.975  52.013  1.00 31.76 ? 629  ALA B CA    1 
ATOM   13331 C C     . ALA B  1 631  ? 3.512   38.852  52.519  1.00 31.94 ? 629  ALA B C     1 
ATOM   13332 O O     . ALA B  1 631  ? 2.351   38.773  52.099  1.00 26.86 ? 629  ALA B O     1 
ATOM   13333 C CB    . ALA B  1 631  ? 4.612   39.828  50.498  1.00 33.73 ? 629  ALA B CB    1 
ATOM   13334 N N     . VAL B  1 632  ? 4.014   37.969  53.373  1.00 26.94 ? 630  VAL B N     1 
ATOM   13335 C CA    . VAL B  1 632  ? 3.111   37.028  54.035  1.00 27.29 ? 630  VAL B CA    1 
ATOM   13336 C C     . VAL B  1 632  ? 2.290   37.801  55.053  1.00 29.22 ? 630  VAL B C     1 
ATOM   13337 O O     . VAL B  1 632  ? 2.873   38.524  55.883  1.00 29.13 ? 630  VAL B O     1 
ATOM   13338 C CB    . VAL B  1 632  ? 3.889   35.896  54.708  1.00 27.92 ? 630  VAL B CB    1 
ATOM   13339 C CG1   . VAL B  1 632  ? 2.923   34.968  55.448  1.00 25.53 ? 630  VAL B CG1   1 
ATOM   13340 C CG2   . VAL B  1 632  ? 4.693   35.108  53.688  1.00 26.52 ? 630  VAL B CG2   1 
ATOM   13341 N N     . PRO B  1 633  ? 0.963   37.714  54.998  1.00 26.46 ? 631  PRO B N     1 
ATOM   13342 C CA    . PRO B  1 633  ? 0.105   38.495  55.900  1.00 26.39 ? 631  PRO B CA    1 
ATOM   13343 C C     . PRO B  1 633  ? 0.471   38.255  57.351  1.00 29.42 ? 631  PRO B C     1 
ATOM   13344 O O     . PRO B  1 633  ? 0.790   37.118  57.727  1.00 27.62 ? 631  PRO B O     1 
ATOM   13345 C CB    . PRO B  1 633  ? -1.296  37.959  55.588  1.00 25.49 ? 631  PRO B CB    1 
ATOM   13346 C CG    . PRO B  1 633  ? -1.203  37.596  54.127  1.00 29.65 ? 631  PRO B CG    1 
ATOM   13347 C CD    . PRO B  1 633  ? 0.191   37.023  53.952  1.00 29.32 ? 631  PRO B CD    1 
ATOM   13348 N N     . PRO B  1 634  ? 0.420   39.298  58.193  1.00 30.42 ? 632  PRO B N     1 
ATOM   13349 C CA    . PRO B  1 634  ? 0.784   39.124  59.614  1.00 27.74 ? 632  PRO B CA    1 
ATOM   13350 C C     . PRO B  1 634  ? 0.071   37.971  60.288  1.00 24.32 ? 632  PRO B C     1 
ATOM   13351 O O     . PRO B  1 634  ? 0.687   37.231  61.066  1.00 23.09 ? 632  PRO B O     1 
ATOM   13352 C CB    . PRO B  1 634  ? 0.380   40.467  60.243  1.00 27.54 ? 632  PRO B CB    1 
ATOM   13353 C CG    . PRO B  1 634  ? 0.449   41.447  59.120  1.00 29.67 ? 632  PRO B CG    1 
ATOM   13354 C CD    . PRO B  1 634  ? 0.125   40.704  57.855  1.00 26.67 ? 632  PRO B CD    1 
ATOM   13355 N N     . SER B  1 635  ? -1.221  37.801  60.012  1.00 24.02 ? 633  SER B N     1 
ATOM   13356 C CA    . SER B  1 635  ? -1.978  36.707  60.616  1.00 24.56 ? 633  SER B CA    1 
ATOM   13357 C C     . SER B  1 635  ? -1.488  35.342  60.140  1.00 24.25 ? 633  SER B C     1 
ATOM   13358 O O     . SER B  1 635  ? -1.568  34.365  60.892  1.00 24.87 ? 633  SER B O     1 
ATOM   13359 C CB    . SER B  1 635  ? -3.469  36.853  60.290  1.00 30.91 ? 633  SER B CB    1 
ATOM   13360 O OG    . SER B  1 635  ? -3.668  36.690  58.891  1.00 35.69 ? 633  SER B OG    1 
ATOM   13361 N N     . GLU B  1 636  ? -0.999  35.238  58.901  1.00 22.99 ? 634  GLU B N     1 
ATOM   13362 C CA    . GLU B  1 636  ? -0.443  33.964  58.457  1.00 24.16 ? 634  GLU B CA    1 
ATOM   13363 C C     . GLU B  1 636  ? 0.948   33.716  59.046  1.00 25.98 ? 634  GLU B C     1 
ATOM   13364 O O     . GLU B  1 636  ? 1.307   32.562  59.306  1.00 23.77 ? 634  GLU B O     1 
ATOM   13365 C CB    . GLU B  1 636  ? -0.393  33.893  56.927  1.00 26.69 ? 634  GLU B CB    1 
ATOM   13366 C CG    . GLU B  1 636  ? 0.213   32.592  56.363  1.00 34.48 ? 634  GLU B CG    1 
ATOM   13367 C CD    . GLU B  1 636  ? -0.378  31.299  56.966  1.00 40.77 ? 634  GLU B CD    1 
ATOM   13368 O OE1   . GLU B  1 636  ? -1.630  31.175  57.046  1.00 35.50 ? 634  GLU B OE1   1 
ATOM   13369 O OE2   . GLU B  1 636  ? 0.422   30.403  57.364  1.00 36.99 ? 634  GLU B OE2   1 
ATOM   13370 N N     . ARG B  1 637  ? 1.743   34.769  59.252  1.00 21.47 ? 635  ARG B N     1 
ATOM   13371 C CA    . ARG B  1 637  ? 2.995   34.593  59.986  1.00 20.91 ? 635  ARG B CA    1 
ATOM   13372 C C     . ARG B  1 637  ? 2.718   34.172  61.424  1.00 23.96 ? 635  ARG B C     1 
ATOM   13373 O O     . ARG B  1 637  ? 3.410   33.302  61.977  1.00 19.66 ? 635  ARG B O     1 
ATOM   13374 C CB    . ARG B  1 637  ? 3.829   35.878  59.947  1.00 22.64 ? 635  ARG B CB    1 
ATOM   13375 C CG    . ARG B  1 637  ? 4.095   36.398  58.533  1.00 22.33 ? 635  ARG B CG    1 
ATOM   13376 C CD    . ARG B  1 637  ? 5.137   37.515  58.533  1.00 23.03 ? 635  ARG B CD    1 
ATOM   13377 N NE    . ARG B  1 637  ? 4.763   38.651  59.379  1.00 24.39 ? 635  ARG B NE    1 
ATOM   13378 C CZ    . ARG B  1 637  ? 4.480   39.858  58.909  1.00 26.81 ? 635  ARG B CZ    1 
ATOM   13379 N NH1   . ARG B  1 637  ? 4.450   40.105  57.609  1.00 30.88 ? 635  ARG B NH1   1 
ATOM   13380 N NH2   . ARG B  1 637  ? 4.245   40.848  59.760  1.00 23.99 ? 635  ARG B NH2   1 
ATOM   13381 N N     . ALA B  1 638  ? 1.713   34.787  62.049  1.00 21.42 ? 636  ALA B N     1 
ATOM   13382 C CA    . ALA B  1 638  ? 1.330   34.381  63.396  1.00 19.82 ? 636  ALA B CA    1 
ATOM   13383 C C     . ALA B  1 638  ? 0.862   32.935  63.418  1.00 19.89 ? 636  ALA B C     1 
ATOM   13384 O O     . ALA B  1 638  ? 1.077   32.226  64.406  1.00 22.39 ? 636  ALA B O     1 
ATOM   13385 C CB    . ALA B  1 638  ? 0.236   35.320  63.936  1.00 19.51 ? 636  ALA B CB    1 
ATOM   13386 N N     . ALA B  1 639  ? 0.231   32.478  62.333  1.00 21.14 ? 637  ALA B N     1 
ATOM   13387 C CA    . ALA B  1 639  ? -0.217  31.089  62.260  1.00 23.16 ? 637  ALA B CA    1 
ATOM   13388 C C     . ALA B  1 639  ? 0.962   30.124  62.267  1.00 24.60 ? 637  ALA B C     1 
ATOM   13389 O O     . ALA B  1 639  ? 0.865   29.026  62.835  1.00 22.48 ? 637  ALA B O     1 
ATOM   13390 C CB    . ALA B  1 639  ? -1.080  30.872  61.011  1.00 23.13 ? 637  ALA B CB    1 
ATOM   13391 N N     . CYS B  1 640  ? 2.079   30.513  61.634  1.00 20.77 ? 638  CYS B N     1 
ATOM   13392 C CA    . CYS B  1 640  ? 3.288   29.704  61.678  1.00 21.28 ? 638  CYS B CA    1 
ATOM   13393 C C     . CYS B  1 640  ? 3.776   29.548  63.104  1.00 20.10 ? 638  CYS B C     1 
ATOM   13394 O O     . CYS B  1 640  ? 4.152   28.451  63.535  1.00 19.58 ? 638  CYS B O     1 
ATOM   13395 C CB    . CYS B  1 640  ? 4.389   30.346  60.825  1.00 22.42 ? 638  CYS B CB    1 
ATOM   13396 S SG    . CYS B  1 640  ? 4.104   30.272  59.058  1.00 26.83 ? 638  CYS B SG    1 
ATOM   13397 N N     . LEU B  1 641  ? 3.803   30.654  63.847  1.00 19.89 ? 639  LEU B N     1 
ATOM   13398 C CA    . LEU B  1 641  ? 4.235   30.583  65.233  1.00 20.27 ? 639  LEU B CA    1 
ATOM   13399 C C     . LEU B  1 641  ? 3.321   29.670  66.035  1.00 22.23 ? 639  LEU B C     1 
ATOM   13400 O O     . LEU B  1 641  ? 3.795   28.837  66.824  1.00 22.94 ? 639  LEU B O     1 
ATOM   13401 C CB    . LEU B  1 641  ? 4.277   31.987  65.840  1.00 20.22 ? 639  LEU B CB    1 
ATOM   13402 C CG    . LEU B  1 641  ? 5.543   32.827  65.666  1.00 18.77 ? 639  LEU B CG    1 
ATOM   13403 C CD1   . LEU B  1 641  ? 5.973   33.001  64.206  1.00 23.03 ? 639  LEU B CD1   1 
ATOM   13404 C CD2   . LEU B  1 641  ? 5.369   34.184  66.381  1.00 20.72 ? 639  LEU B CD2   1 
ATOM   13405 N N     . ASP B  1 642  ? 2.005   29.804  65.841  1.00 21.04 ? 640  ASP B N     1 
ATOM   13406 C CA    . ASP B  1 642  ? 1.075   28.943  66.565  1.00 20.57 ? 640  ASP B CA    1 
ATOM   13407 C C     . ASP B  1 642  ? 1.281   27.475  66.208  1.00 20.81 ? 640  ASP B C     1 
ATOM   13408 O O     . ASP B  1 642  ? 1.205   26.605  67.085  1.00 23.35 ? 640  ASP B O     1 
ATOM   13409 C CB    . ASP B  1 642  ? -0.369  29.377  66.314  1.00 21.59 ? 640  ASP B CB    1 
ATOM   13410 C CG    . ASP B  1 642  ? -0.779  30.555  67.185  1.00 26.17 ? 640  ASP B CG    1 
ATOM   13411 O OD1   . ASP B  1 642  ? -0.118  30.791  68.224  1.00 24.65 ? 640  ASP B OD1   1 
ATOM   13412 O OD2   . ASP B  1 642  ? -1.748  31.256  66.836  1.00 26.36 ? 640  ASP B OD2   1 
ATOM   13413 N N     . ARG B  1 643  ? 1.555   27.172  64.936  1.00 20.17 ? 641  ARG B N     1 
ATOM   13414 C CA    . ARG B  1 643  ? 1.813   25.775  64.579  1.00 20.32 ? 641  ARG B CA    1 
ATOM   13415 C C     . ARG B  1 643  ? 3.106   25.276  65.214  1.00 23.37 ? 641  ARG B C     1 
ATOM   13416 O O     . ARG B  1 643  ? 3.165   24.144  65.712  1.00 22.98 ? 641  ARG B O     1 
ATOM   13417 C CB    . ARG B  1 643  ? 1.860   25.607  63.061  1.00 21.36 ? 641  ARG B CB    1 
ATOM   13418 C CG    . ARG B  1 643  ? 0.485   25.671  62.397  1.00 24.29 ? 641  ARG B CG    1 
ATOM   13419 C CD    . ARG B  1 643  ? 0.581   25.234  60.928  1.00 30.10 ? 641  ARG B CD    1 
ATOM   13420 N NE    . ARG B  1 643  ? 1.310   26.211  60.122  1.00 25.21 ? 641  ARG B NE    1 
ATOM   13421 C CZ    . ARG B  1 643  ? 0.737   27.241  59.517  1.00 27.99 ? 641  ARG B CZ    1 
ATOM   13422 N NH1   . ARG B  1 643  ? -0.566  27.450  59.601  1.00 26.87 ? 641  ARG B NH1   1 
ATOM   13423 N NH2   . ARG B  1 643  ? 1.485   28.068  58.796  1.00 28.82 ? 641  ARG B NH2   1 
ATOM   13424 N N     . ALA B  1 644  ? 4.141   26.114  65.228  1.00 19.95 ? 642  ALA B N     1 
ATOM   13425 C CA    . ALA B  1 644  ? 5.372   25.739  65.912  1.00 22.41 ? 642  ALA B CA    1 
ATOM   13426 C C     . ALA B  1 644  ? 5.101   25.406  67.373  1.00 26.58 ? 642  ALA B C     1 
ATOM   13427 O O     . ALA B  1 644  ? 5.623   24.412  67.900  1.00 21.45 ? 642  ALA B O     1 
ATOM   13428 C CB    . ALA B  1 644  ? 6.395   26.862  65.800  1.00 22.46 ? 642  ALA B CB    1 
ATOM   13429 N N     . ALA B  1 645  ? 4.275   26.222  68.040  1.00 20.27 ? 643  ALA B N     1 
ATOM   13430 C CA    . ALA B  1 645  ? 3.975   25.979  69.448  1.00 18.69 ? 643  ALA B CA    1 
ATOM   13431 C C     . ALA B  1 645  ? 3.315   24.621  69.646  1.00 21.68 ? 643  ALA B C     1 
ATOM   13432 O O     . ALA B  1 645  ? 3.673   23.883  70.581  1.00 21.53 ? 643  ALA B O     1 
ATOM   13433 C CB    . ALA B  1 645  ? 3.104   27.118  69.997  1.00 19.33 ? 643  ALA B CB    1 
ATOM   13434 N N     . GLU B  1 646  ? 2.370   24.257  68.760  1.00 23.36 ? 644  GLU B N     1 
ATOM   13435 C CA    . GLU B  1 646  ? 1.737   22.940  68.846  1.00 26.70 ? 644  GLU B CA    1 
ATOM   13436 C C     . GLU B  1 646  ? 2.769   21.833  68.682  1.00 27.63 ? 644  GLU B C     1 
ATOM   13437 O O     . GLU B  1 646  ? 2.722   20.823  69.391  1.00 25.78 ? 644  GLU B O     1 
ATOM   13438 C CB    . GLU B  1 646  ? 0.641   22.775  67.775  1.00 25.03 ? 644  GLU B CB    1 
ATOM   13439 C CG    . GLU B  1 646  ? -0.529  23.719  67.896  1.00 28.68 ? 644  GLU B CG    1 
ATOM   13440 C CD    . GLU B  1 646  ? -1.244  23.579  69.234  1.00 34.63 ? 644  GLU B CD    1 
ATOM   13441 O OE1   . GLU B  1 646  ? -1.471  22.433  69.683  1.00 40.84 ? 644  GLU B OE1   1 
ATOM   13442 O OE2   . GLU B  1 646  ? -1.556  24.615  69.848  1.00 38.28 ? 644  GLU B OE2   1 
ATOM   13443 N N     . LEU B  1 647  ? 3.687   21.991  67.722  1.00 22.64 ? 645  LEU B N     1 
ATOM   13444 C CA    . LEU B  1 647  ? 4.722   20.980  67.529  1.00 26.48 ? 645  LEU B CA    1 
ATOM   13445 C C     . LEU B  1 647  ? 5.615   20.842  68.758  1.00 24.03 ? 645  LEU B C     1 
ATOM   13446 O O     . LEU B  1 647  ? 5.933   19.720  69.175  1.00 24.55 ? 645  LEU B O     1 
ATOM   13447 C CB    . LEU B  1 647  ? 5.547   21.308  66.285  1.00 25.75 ? 645  LEU B CB    1 
ATOM   13448 C CG    . LEU B  1 647  ? 4.837   21.150  64.946  1.00 32.14 ? 645  LEU B CG    1 
ATOM   13449 C CD1   . LEU B  1 647  ? 5.745   21.586  63.797  1.00 26.82 ? 645  LEU B CD1   1 
ATOM   13450 C CD2   . LEU B  1 647  ? 4.360   19.726  64.728  1.00 28.42 ? 645  LEU B CD2   1 
ATOM   13451 N N     . MET B  1 648  ? 6.011   21.963  69.375  1.00 24.27 ? 646  MET B N     1 
ATOM   13452 C CA    . MET B  1 648  ? 6.870   21.875  70.562  1.00 21.84 ? 646  MET B CA    1 
ATOM   13453 C C     . MET B  1 648  ? 6.136   21.265  71.749  1.00 25.56 ? 646  MET B C     1 
ATOM   13454 O O     . MET B  1 648  ? 6.738   20.549  72.556  1.00 23.70 ? 646  MET B O     1 
ATOM   13455 C CB    . MET B  1 648  ? 7.415   23.245  70.952  1.00 21.66 ? 646  MET B CB    1 
ATOM   13456 C CG    . MET B  1 648  ? 8.527   23.760  70.060  1.00 28.71 ? 646  MET B CG    1 
ATOM   13457 S SD    . MET B  1 648  ? 9.275   25.233  70.780  1.00 26.48 ? 646  MET B SD    1 
ATOM   13458 C CE    . MET B  1 648  ? 10.193  25.818  69.361  1.00 26.33 ? 646  MET B CE    1 
ATOM   13459 N N     . GLN B  1 649  ? 4.845   21.557  71.883  1.00 23.77 ? 647  GLN B N     1 
ATOM   13460 C CA    . GLN B  1 649  ? 4.055   20.940  72.940  1.00 25.96 ? 647  GLN B CA    1 
ATOM   13461 C C     . GLN B  1 649  ? 3.989   19.429  72.755  1.00 23.63 ? 647  GLN B C     1 
ATOM   13462 O O     . GLN B  1 649  ? 4.217   18.667  73.701  1.00 28.29 ? 647  GLN B O     1 
ATOM   13463 C CB    . GLN B  1 649  ? 2.657   21.555  72.961  1.00 25.21 ? 647  GLN B CB    1 
ATOM   13464 C CG    . GLN B  1 649  ? 1.781   21.069  74.102  1.00 24.80 ? 647  GLN B CG    1 
ATOM   13465 C CD    . GLN B  1 649  ? 2.189   21.697  75.409  1.00 25.92 ? 647  GLN B CD    1 
ATOM   13466 O OE1   . GLN B  1 649  ? 1.916   22.877  75.656  1.00 24.66 ? 647  GLN B OE1   1 
ATOM   13467 N NE2   . GLN B  1 649  ? 2.885   20.929  76.242  1.00 24.43 ? 647  GLN B NE2   1 
ATOM   13468 N N     . ALA B  1 650  ? 3.677   18.974  71.537  1.00 25.62 ? 648  ALA B N     1 
ATOM   13469 C CA    . ALA B  1 650  ? 3.572   17.542  71.270  1.00 25.85 ? 648  ALA B CA    1 
ATOM   13470 C C     . ALA B  1 650  ? 4.899   16.814  71.478  1.00 26.27 ? 648  ALA B C     1 
ATOM   13471 O O     . ALA B  1 650  ? 4.912   15.658  71.919  1.00 30.15 ? 648  ALA B O     1 
ATOM   13472 C CB    . ALA B  1 650  ? 3.072   17.312  69.843  1.00 26.41 ? 648  ALA B CB    1 
ATOM   13473 N N     . ARG B  1 651  ? 6.013   17.460  71.163  1.00 24.58 ? 649  ARG B N     1 
ATOM   13474 C CA    . ARG B  1 651  ? 7.332   16.847  71.216  1.00 27.10 ? 649  ARG B CA    1 
ATOM   13475 C C     . ARG B  1 651  ? 8.113   17.213  72.468  1.00 28.79 ? 649  ARG B C     1 
ATOM   13476 O O     . ARG B  1 651  ? 9.309   16.923  72.545  1.00 29.36 ? 649  ARG B O     1 
ATOM   13477 C CB    . ARG B  1 651  ? 8.118   17.236  69.970  1.00 27.61 ? 649  ARG B CB    1 
ATOM   13478 C CG    . ARG B  1 651  ? 7.331   16.873  68.740  1.00 28.98 ? 649  ARG B CG    1 
ATOM   13479 C CD    . ARG B  1 651  ? 7.992   17.278  67.454  1.00 32.97 ? 649  ARG B CD    1 
ATOM   13480 N NE    . ARG B  1 651  ? 7.097   16.965  66.345  1.00 33.30 ? 649  ARG B NE    1 
ATOM   13481 C CZ    . ARG B  1 651  ? 7.323   17.301  65.084  1.00 35.46 ? 649  ARG B CZ    1 
ATOM   13482 N NH1   . ARG B  1 651  ? 8.432   17.937  64.727  1.00 27.60 ? 649  ARG B NH1   1 
ATOM   13483 N NH2   . ARG B  1 651  ? 6.415   16.991  64.161  1.00 33.38 ? 649  ARG B NH2   1 
ATOM   13484 N N     . MET B  1 652  ? 7.455   17.814  73.456  1.00 26.27 ? 650  MET B N     1 
ATOM   13485 C CA    . MET B  1 652  ? 8.139   18.218  74.682  1.00 26.63 ? 650  MET B CA    1 
ATOM   13486 C C     . MET B  1 652  ? 8.973   17.109  75.316  1.00 28.62 ? 650  MET B C     1 
ATOM   13487 O O     . MET B  1 652  ? 10.115  17.395  75.702  1.00 31.06 ? 650  MET B O     1 
ATOM   13488 C CB    . MET B  1 652  ? 7.118   18.775  75.690  1.00 24.49 ? 650  MET B CB    1 
ATOM   13489 C CG    . MET B  1 652  ? 7.748   19.148  77.040  1.00 28.35 ? 650  MET B CG    1 
ATOM   13490 S SD    . MET B  1 652  ? 6.519   19.742  78.221  1.00 30.09 ? 650  MET B SD    1 
ATOM   13491 C CE    . MET B  1 652  ? 6.253   21.432  77.701  1.00 26.25 ? 650  MET B CE    1 
ATOM   13492 N N     . PRO B  1 653  ? 8.507   15.858  75.446  1.00 27.31 ? 651  PRO B N     1 
ATOM   13493 C CA    . PRO B  1 653  ? 9.386   14.833  76.043  1.00 32.14 ? 651  PRO B CA    1 
ATOM   13494 C C     . PRO B  1 653  ? 10.713  14.667  75.316  1.00 29.79 ? 651  PRO B C     1 
ATOM   13495 O O     . PRO B  1 653  ? 11.749  14.497  75.968  1.00 31.95 ? 651  PRO B O     1 
ATOM   13496 C CB    . PRO B  1 653  ? 8.536   13.553  75.972  1.00 29.40 ? 651  PRO B CB    1 
ATOM   13497 C CG    . PRO B  1 653  ? 7.146   14.021  75.915  1.00 32.59 ? 651  PRO B CG    1 
ATOM   13498 C CD    . PRO B  1 653  ? 7.167   15.312  75.146  1.00 29.84 ? 651  PRO B CD    1 
ATOM   13499 N N     . THR B  1 654  ? 10.716  14.709  73.981  1.00 32.17 ? 652  THR B N     1 
ATOM   13500 C CA    . THR B  1 654  ? 11.969  14.564  73.244  1.00 31.04 ? 652  THR B CA    1 
ATOM   13501 C C     . THR B  1 654  ? 12.863  15.782  73.431  1.00 33.73 ? 652  THR B C     1 
ATOM   13502 O O     . THR B  1 654  ? 14.083  15.645  73.607  1.00 31.50 ? 652  THR B O     1 
ATOM   13503 C CB    . THR B  1 654  ? 11.680  14.345  71.763  1.00 29.33 ? 652  THR B CB    1 
ATOM   13504 O OG1   . THR B  1 654  ? 10.955  13.118  71.605  1.00 35.15 ? 652  THR B OG1   1 
ATOM   13505 C CG2   . THR B  1 654  ? 12.964  14.293  70.964  1.00 35.10 ? 652  THR B CG2   1 
ATOM   13506 N N     . LEU B  1 655  ? 12.271  16.978  73.397  1.00 28.50 ? 653  LEU B N     1 
ATOM   13507 C CA    . LEU B  1 655  ? 13.035  18.203  73.614  1.00 27.49 ? 653  LEU B CA    1 
ATOM   13508 C C     . LEU B  1 655  ? 13.656  18.220  74.999  1.00 31.08 ? 653  LEU B C     1 
ATOM   13509 O O     . LEU B  1 655  ? 14.794  18.673  75.164  1.00 29.73 ? 653  LEU B O     1 
ATOM   13510 C CB    . LEU B  1 655  ? 12.147  19.432  73.435  1.00 24.93 ? 653  LEU B CB    1 
ATOM   13511 C CG    . LEU B  1 655  ? 11.464  19.569  72.070  1.00 29.39 ? 653  LEU B CG    1 
ATOM   13512 C CD1   . LEU B  1 655  ? 10.604  20.840  71.977  1.00 25.83 ? 653  LEU B CD1   1 
ATOM   13513 C CD2   . LEU B  1 655  ? 12.524  19.533  70.984  1.00 30.17 ? 653  LEU B CD2   1 
ATOM   13514 N N     . LEU B  1 656  ? 12.913  17.751  76.007  1.00 29.03 ? 654  LEU B N     1 
ATOM   13515 C CA    . LEU B  1 656  ? 13.458  17.621  77.358  1.00 30.12 ? 654  LEU B CA    1 
ATOM   13516 C C     . LEU B  1 656  ? 14.762  16.850  77.368  1.00 30.50 ? 654  LEU B C     1 
ATOM   13517 O O     . LEU B  1 656  ? 15.740  17.273  77.992  1.00 32.13 ? 654  LEU B O     1 
ATOM   13518 C CB    . LEU B  1 656  ? 12.467  16.898  78.264  1.00 32.14 ? 654  LEU B CB    1 
ATOM   13519 C CG    . LEU B  1 656  ? 11.179  17.644  78.453  1.00 29.21 ? 654  LEU B CG    1 
ATOM   13520 C CD1   . LEU B  1 656  ? 10.243  16.873  79.383  1.00 32.18 ? 654  LEU B CD1   1 
ATOM   13521 C CD2   . LEU B  1 656  ? 11.508  19.019  78.985  1.00 28.60 ? 654  LEU B CD2   1 
ATOM   13522 N N     . GLY B  1 657  ? 14.765  15.675  76.735  1.00 30.49 ? 655  GLY B N     1 
ATOM   13523 C CA    . GLY B  1 657  ? 15.944  14.835  76.750  1.00 34.61 ? 655  GLY B CA    1 
ATOM   13524 C C     . GLY B  1 657  ? 17.148  15.542  76.171  1.00 33.78 ? 655  GLY B C     1 
ATOM   13525 O O     . GLY B  1 657  ? 18.263  15.403  76.676  1.00 33.61 ? 655  GLY B O     1 
ATOM   13526 N N     . LEU B  1 658  ? 16.933  16.334  75.122  1.00 31.07 ? 656  LEU B N     1 
ATOM   13527 C CA    . LEU B  1 658  ? 18.038  17.077  74.530  1.00 27.41 ? 656  LEU B CA    1 
ATOM   13528 C C     . LEU B  1 658  ? 18.483  18.216  75.437  1.00 32.05 ? 656  LEU B C     1 
ATOM   13529 O O     . LEU B  1 658  ? 19.689  18.445  75.612  1.00 32.55 ? 656  LEU B O     1 
ATOM   13530 C CB    . LEU B  1 658  ? 17.630  17.598  73.150  1.00 32.85 ? 656  LEU B CB    1 
ATOM   13531 C CG    . LEU B  1 658  ? 18.755  18.127  72.265  1.00 33.09 ? 656  LEU B CG    1 
ATOM   13532 C CD1   . LEU B  1 658  ? 19.823  17.059  72.099  1.00 28.16 ? 656  LEU B CD1   1 
ATOM   13533 C CD2   . LEU B  1 658  ? 18.205  18.562  70.922  1.00 31.05 ? 656  LEU B CD2   1 
ATOM   13534 N N     . ILE B  1 659  ? 17.529  18.937  76.037  1.00 28.18 ? 657  ILE B N     1 
ATOM   13535 C CA    . ILE B  1 659  ? 17.899  20.045  76.911  1.00 27.86 ? 657  ILE B CA    1 
ATOM   13536 C C     . ILE B  1 659  ? 18.635  19.521  78.132  1.00 30.69 ? 657  ILE B C     1 
ATOM   13537 O O     . ILE B  1 659  ? 19.611  20.126  78.599  1.00 28.37 ? 657  ILE B O     1 
ATOM   13538 C CB    . ILE B  1 659  ? 16.648  20.856  77.301  1.00 24.67 ? 657  ILE B CB    1 
ATOM   13539 C CG1   . ILE B  1 659  ? 16.082  21.554  76.068  1.00 28.62 ? 657  ILE B CG1   1 
ATOM   13540 C CG2   . ILE B  1 659  ? 16.945  21.854  78.431  1.00 26.14 ? 657  ILE B CG2   1 
ATOM   13541 C CD1   . ILE B  1 659  ? 14.680  22.079  76.287  1.00 28.34 ? 657  ILE B CD1   1 
ATOM   13542 N N     . ILE B  1 660  ? 18.180  18.387  78.664  1.00 26.34 ? 658  ILE B N     1 
ATOM   13543 C CA    . ILE B  1 660  ? 18.805  17.819  79.853  1.00 27.34 ? 658  ILE B CA    1 
ATOM   13544 C C     . ILE B  1 660  ? 20.258  17.474  79.571  1.00 27.26 ? 658  ILE B C     1 
ATOM   13545 O O     . ILE B  1 660  ? 21.150  17.778  80.373  1.00 31.45 ? 658  ILE B O     1 
ATOM   13546 C CB    . ILE B  1 660  ? 18.012  16.583  80.321  1.00 26.25 ? 658  ILE B CB    1 
ATOM   13547 C CG1   . ILE B  1 660  ? 16.694  17.000  80.979  1.00 27.73 ? 658  ILE B CG1   1 
ATOM   13548 C CG2   . ILE B  1 660  ? 18.877  15.690  81.228  1.00 26.02 ? 658  ILE B CG2   1 
ATOM   13549 C CD1   . ILE B  1 660  ? 15.751  15.818  81.200  1.00 28.70 ? 658  ILE B CD1   1 
ATOM   13550 N N     . ARG B  1 661  ? 20.523  16.864  78.416  1.00 28.18 ? 659  ARG B N     1 
ATOM   13551 C CA    . ARG B  1 661  ? 21.854  16.336  78.135  1.00 30.07 ? 659  ARG B CA    1 
ATOM   13552 C C     . ARG B  1 661  ? 22.785  17.366  77.505  1.00 31.71 ? 659  ARG B C     1 
ATOM   13553 O O     . ARG B  1 661  ? 23.988  17.353  77.774  1.00 30.35 ? 659  ARG B O     1 
ATOM   13554 C CB    . ARG B  1 661  ? 21.752  15.111  77.229  1.00 30.42 ? 659  ARG B CB    1 
ATOM   13555 C CG    . ARG B  1 661  ? 21.332  13.861  77.961  1.00 33.70 ? 659  ARG B CG    1 
ATOM   13556 C CD    . ARG B  1 661  ? 21.072  12.713  77.003  1.00 34.44 ? 659  ARG B CD    1 
ATOM   13557 N NE    . ARG B  1 661  ? 22.280  12.195  76.368  1.00 37.53 ? 659  ARG B NE    1 
ATOM   13558 C CZ    . ARG B  1 661  ? 22.452  12.095  75.056  1.00 39.30 ? 659  ARG B CZ    1 
ATOM   13559 N NH1   . ARG B  1 661  ? 21.532  12.510  74.206  1.00 38.95 ? 659  ARG B NH1   1 
ATOM   13560 N NH2   . ARG B  1 661  ? 23.562  11.531  74.583  1.00 33.59 ? 659  ARG B NH2   1 
ATOM   13561 N N     . GLU B  1 662  ? 22.269  18.251  76.658  1.00 29.43 ? 660  GLU B N     1 
ATOM   13562 C CA    . GLU B  1 662  ? 23.151  19.230  76.044  1.00 28.50 ? 660  GLU B CA    1 
ATOM   13563 C C     . GLU B  1 662  ? 23.423  20.393  76.984  1.00 28.88 ? 660  GLU B C     1 
ATOM   13564 O O     . GLU B  1 662  ? 24.545  20.902  77.023  1.00 26.84 ? 660  GLU B O     1 
ATOM   13565 C CB    . GLU B  1 662  ? 22.564  19.741  74.727  1.00 30.73 ? 660  GLU B CB    1 
ATOM   13566 C CG    . GLU B  1 662  ? 23.377  20.873  74.096  1.00 30.86 ? 660  GLU B CG    1 
ATOM   13567 C CD    . GLU B  1 662  ? 22.862  21.313  72.721  1.00 31.25 ? 660  GLU B CD    1 
ATOM   13568 O OE1   . GLU B  1 662  ? 21.644  21.575  72.569  1.00 28.75 ? 660  GLU B OE1   1 
ATOM   13569 O OE2   . GLU B  1 662  ? 23.689  21.390  71.787  1.00 30.63 ? 660  GLU B OE2   1 
ATOM   13570 N N     . ALA B  1 663  ? 22.426  20.819  77.758  1.00 28.03 ? 661  ALA B N     1 
ATOM   13571 C CA    . ALA B  1 663  ? 22.544  22.047  78.525  1.00 27.40 ? 661  ALA B CA    1 
ATOM   13572 C C     . ALA B  1 663  ? 22.726  21.813  80.014  1.00 28.08 ? 661  ALA B C     1 
ATOM   13573 O O     . ALA B  1 663  ? 22.930  22.780  80.753  1.00 30.61 ? 661  ALA B O     1 
ATOM   13574 C CB    . ALA B  1 663  ? 21.326  22.944  78.281  1.00 27.98 ? 661  ALA B CB    1 
ATOM   13575 N N     . GLY B  1 664  ? 22.694  20.565  80.470  1.00 32.22 ? 662  GLY B N     1 
ATOM   13576 C CA    . GLY B  1 664  ? 22.912  20.286  81.876  1.00 29.57 ? 662  GLY B CA    1 
ATOM   13577 C C     . GLY B  1 664  ? 21.722  20.541  82.770  1.00 31.64 ? 662  GLY B C     1 
ATOM   13578 O O     . GLY B  1 664  ? 21.891  20.639  83.991  1.00 31.68 ? 662  GLY B O     1 
ATOM   13579 N N     . LYS B  1 665  ? 20.515  20.630  82.208  1.00 27.66 ? 663  LYS B N     1 
ATOM   13580 C CA    . LYS B  1 665  ? 19.356  21.055  82.977  1.00 29.62 ? 663  LYS B CA    1 
ATOM   13581 C C     . LYS B  1 665  ? 18.673  19.866  83.630  1.00 27.17 ? 663  LYS B C     1 
ATOM   13582 O O     . LYS B  1 665  ? 18.754  18.734  83.151  1.00 27.50 ? 663  LYS B O     1 
ATOM   13583 C CB    . LYS B  1 665  ? 18.343  21.799  82.105  1.00 27.37 ? 663  LYS B CB    1 
ATOM   13584 C CG    . LYS B  1 665  ? 18.865  23.119  81.587  1.00 32.81 ? 663  LYS B CG    1 
ATOM   13585 C CD    . LYS B  1 665  ? 17.747  24.093  81.281  1.00 29.54 ? 663  LYS B CD    1 
ATOM   13586 C CE    . LYS B  1 665  ? 18.343  25.468  81.008  1.00 30.12 ? 663  LYS B CE    1 
ATOM   13587 N NZ    . LYS B  1 665  ? 17.330  26.559  81.000  1.00 32.05 ? 663  LYS B NZ    1 
ATOM   13588 N N     . SER B  1 666  ? 17.997  20.142  84.739  1.00 29.05 ? 664  SER B N     1 
ATOM   13589 C CA    . SER B  1 666  ? 17.119  19.144  85.319  1.00 33.08 ? 664  SER B CA    1 
ATOM   13590 C C     . SER B  1 666  ? 15.854  19.011  84.476  1.00 29.82 ? 664  SER B C     1 
ATOM   13591 O O     . SER B  1 666  ? 15.495  19.904  83.703  1.00 27.97 ? 664  SER B O     1 
ATOM   13592 C CB    . SER B  1 666  ? 16.749  19.530  86.743  1.00 33.40 ? 664  SER B CB    1 
ATOM   13593 O OG    . SER B  1 666  ? 15.872  20.630  86.714  1.00 32.11 ? 664  SER B OG    1 
ATOM   13594 N N     . ALA B  1 667  ? 15.178  17.868  84.623  1.00 28.19 ? 665  ALA B N     1 
ATOM   13595 C CA    . ALA B  1 667  ? 13.943  17.656  83.873  1.00 29.85 ? 665  ALA B CA    1 
ATOM   13596 C C     . ALA B  1 667  ? 12.914  18.722  84.214  1.00 29.74 ? 665  ALA B C     1 
ATOM   13597 O O     . ALA B  1 667  ? 12.213  19.228  83.331  1.00 27.09 ? 665  ALA B O     1 
ATOM   13598 C CB    . ALA B  1 667  ? 13.383  16.262  84.151  1.00 30.71 ? 665  ALA B CB    1 
ATOM   13599 N N     . LEU B  1 668  ? 12.844  19.101  85.488  1.00 28.14 ? 666  LEU B N     1 
ATOM   13600 C CA    . LEU B  1 668  ? 11.894  20.119  85.919  1.00 28.00 ? 666  LEU B CA    1 
ATOM   13601 C C     . LEU B  1 668  ? 12.166  21.450  85.230  1.00 30.24 ? 666  LEU B C     1 
ATOM   13602 O O     . LEU B  1 668  ? 11.244  22.096  84.714  1.00 27.36 ? 666  LEU B O     1 
ATOM   13603 C CB    . LEU B  1 668  ? 11.977  20.264  87.436  1.00 35.28 ? 666  LEU B CB    1 
ATOM   13604 C CG    . LEU B  1 668  ? 10.835  20.941  88.176  1.00 39.45 ? 666  LEU B CG    1 
ATOM   13605 C CD1   . LEU B  1 668  ? 9.528   20.153  88.011  1.00 38.36 ? 666  LEU B CD1   1 
ATOM   13606 C CD2   . LEU B  1 668  ? 11.244  21.019  89.632  1.00 39.80 ? 666  LEU B CD2   1 
ATOM   13607 N N     . ASN B  1 669  ? 13.436  21.876  85.204  1.00 25.77 ? 667  ASN B N     1 
ATOM   13608 C CA    . ASN B  1 669  ? 13.775  23.128  84.533  1.00 24.71 ? 667  ASN B CA    1 
ATOM   13609 C C     . ASN B  1 669  ? 13.669  23.008  83.011  1.00 25.61 ? 667  ASN B C     1 
ATOM   13610 O O     . ASN B  1 669  ? 13.376  24.001  82.331  1.00 24.88 ? 667  ASN B O     1 
ATOM   13611 C CB    . ASN B  1 669  ? 15.187  23.567  84.918  1.00 29.11 ? 667  ASN B CB    1 
ATOM   13612 C CG    . ASN B  1 669  ? 15.301  23.975  86.388  1.00 28.37 ? 667  ASN B CG    1 
ATOM   13613 O OD1   . ASN B  1 669  ? 16.286  23.654  87.047  1.00 36.75 ? 667  ASN B OD1   1 
ATOM   13614 N ND2   . ASN B  1 669  ? 14.293  24.685  86.899  1.00 29.66 ? 667  ASN B ND2   1 
ATOM   13615 N N     . ALA B  1 670  ? 13.950  21.830  82.455  1.00 22.32 ? 668  ALA B N     1 
ATOM   13616 C CA    . ALA B  1 670  ? 13.797  21.674  81.012  1.00 26.68 ? 668  ALA B CA    1 
ATOM   13617 C C     . ALA B  1 670  ? 12.332  21.804  80.602  1.00 23.99 ? 668  ALA B C     1 
ATOM   13618 O O     . ALA B  1 670  ? 12.027  22.355  79.538  1.00 21.88 ? 668  ALA B O     1 
ATOM   13619 C CB    . ALA B  1 670  ? 14.373  20.335  80.557  1.00 25.51 ? 668  ALA B CB    1 
ATOM   13620 N N     . ILE B  1 671  ? 11.410  21.275  81.417  1.00 25.13 ? 669  ILE B N     1 
ATOM   13621 C CA    . ILE B  1 671  ? 9.982   21.442  81.126  1.00 23.92 ? 669  ILE B CA    1 
ATOM   13622 C C     . ILE B  1 671  ? 9.629   22.922  81.072  1.00 21.87 ? 669  ILE B C     1 
ATOM   13623 O O     . ILE B  1 671  ? 8.970   23.384  80.137  1.00 25.01 ? 669  ILE B O     1 
ATOM   13624 C CB    . ILE B  1 671  ? 9.124   20.698  82.164  1.00 27.07 ? 669  ILE B CB    1 
ATOM   13625 C CG1   . ILE B  1 671  ? 9.284   19.188  81.976  1.00 26.37 ? 669  ILE B CG1   1 
ATOM   13626 C CG2   . ILE B  1 671  ? 7.659   21.101  82.026  1.00 26.32 ? 669  ILE B CG2   1 
ATOM   13627 C CD1   . ILE B  1 671  ? 8.751   18.345  83.112  1.00 32.11 ? 669  ILE B CD1   1 
ATOM   13628 N N     . ALA B  1 672  ? 10.091  23.691  82.065  1.00 22.15 ? 670  ALA B N     1 
ATOM   13629 C CA    . ALA B  1 672  ? 9.795   25.116  82.104  1.00 24.21 ? 670  ALA B CA    1 
ATOM   13630 C C     . ALA B  1 672  ? 10.350  25.827  80.877  1.00 24.03 ? 670  ALA B C     1 
ATOM   13631 O O     . ALA B  1 672  ? 9.731   26.763  80.361  1.00 24.85 ? 670  ALA B O     1 
ATOM   13632 C CB    . ALA B  1 672  ? 10.373  25.744  83.380  1.00 26.93 ? 670  ALA B CB    1 
ATOM   13633 N N     . GLU B  1 673  ? 11.523  25.406  80.408  1.00 21.18 ? 671  GLU B N     1 
ATOM   13634 C CA    . GLU B  1 673  ? 12.113  26.039  79.239  1.00 25.40 ? 671  GLU B CA    1 
ATOM   13635 C C     . GLU B  1 673  ? 11.262  25.797  78.000  1.00 21.83 ? 671  GLU B C     1 
ATOM   13636 O O     . GLU B  1 673  ? 10.970  26.735  77.253  1.00 23.15 ? 671  GLU B O     1 
ATOM   13637 C CB    . GLU B  1 673  ? 13.533  25.533  79.016  1.00 25.20 ? 671  GLU B CB    1 
ATOM   13638 C CG    . GLU B  1 673  ? 14.074  25.941  77.657  1.00 26.22 ? 671  GLU B CG    1 
ATOM   13639 C CD    . GLU B  1 673  ? 15.488  26.446  77.721  1.00 32.73 ? 671  GLU B CD    1 
ATOM   13640 O OE1   . GLU B  1 673  ? 16.244  25.996  78.622  1.00 33.74 ? 671  GLU B OE1   1 
ATOM   13641 O OE2   . GLU B  1 673  ? 15.841  27.290  76.861  1.00 27.45 ? 671  GLU B OE2   1 
ATOM   13642 N N     . VAL B  1 674  ? 10.827  24.551  77.790  1.00 20.10 ? 672  VAL B N     1 
ATOM   13643 C CA    . VAL B  1 674  ? 9.963   24.250  76.650  1.00 23.73 ? 672  VAL B CA    1 
ATOM   13644 C C     . VAL B  1 674  ? 8.639   25.015  76.764  1.00 22.36 ? 672  VAL B C     1 
ATOM   13645 O O     . VAL B  1 674  ? 8.157   25.594  75.787  1.00 20.61 ? 672  VAL B O     1 
ATOM   13646 C CB    . VAL B  1 674  ? 9.751   22.727  76.520  1.00 22.29 ? 672  VAL B CB    1 
ATOM   13647 C CG1   . VAL B  1 674  ? 8.832   22.405  75.354  1.00 23.41 ? 672  VAL B CG1   1 
ATOM   13648 C CG2   . VAL B  1 674  ? 11.089  22.015  76.305  1.00 25.17 ? 672  VAL B CG2   1 
ATOM   13649 N N     . ARG B  1 675  ? 8.045   25.057  77.959  1.00 21.32 ? 673  ARG B N     1 
ATOM   13650 C CA    . ARG B  1 675  ? 6.828   25.852  78.113  1.00 22.52 ? 673  ARG B CA    1 
ATOM   13651 C C     . ARG B  1 675  ? 7.077   27.316  77.767  1.00 20.85 ? 673  ARG B C     1 
ATOM   13652 O O     . ARG B  1 675  ? 6.213   27.977  77.180  1.00 21.26 ? 673  ARG B O     1 
ATOM   13653 C CB    . ARG B  1 675  ? 6.277   25.757  79.538  1.00 20.24 ? 673  ARG B CB    1 
ATOM   13654 C CG    . ARG B  1 675  ? 5.777   24.380  79.987  1.00 20.42 ? 673  ARG B CG    1 
ATOM   13655 C CD    . ARG B  1 675  ? 5.049   24.564  81.344  1.00 25.54 ? 673  ARG B CD    1 
ATOM   13656 N NE    . ARG B  1 675  ? 3.932   25.490  81.201  1.00 23.76 ? 673  ARG B NE    1 
ATOM   13657 C CZ    . ARG B  1 675  ? 3.347   26.122  82.210  1.00 24.89 ? 673  ARG B CZ    1 
ATOM   13658 N NH1   . ARG B  1 675  ? 3.759   25.957  83.457  1.00 21.13 ? 673  ARG B NH1   1 
ATOM   13659 N NH2   . ARG B  1 675  ? 2.320   26.932  81.961  1.00 23.75 ? 673  ARG B NH2   1 
ATOM   13660 N N     . GLU B  1 676  ? 8.221   27.859  78.180  1.00 21.37 ? 674  GLU B N     1 
ATOM   13661 C CA    . GLU B  1 676  ? 8.504   29.257  77.873  1.00 22.19 ? 674  GLU B CA    1 
ATOM   13662 C C     . GLU B  1 676  ? 8.635   29.478  76.368  1.00 20.96 ? 674  GLU B C     1 
ATOM   13663 O O     . GLU B  1 676  ? 8.133   30.473  75.850  1.00 20.45 ? 674  GLU B O     1 
ATOM   13664 C CB    . GLU B  1 676  ? 9.767   29.724  78.605  1.00 24.26 ? 674  GLU B CB    1 
ATOM   13665 C CG    . GLU B  1 676  ? 10.105  31.196  78.410  1.00 25.42 ? 674  GLU B CG    1 
ATOM   13666 C CD    . GLU B  1 676  ? 11.329  31.630  79.269  1.00 38.49 ? 674  GLU B CD    1 
ATOM   13667 O OE1   . GLU B  1 676  ? 11.790  30.824  80.122  1.00 39.81 ? 674  GLU B OE1   1 
ATOM   13668 O OE2   . GLU B  1 676  ? 11.827  32.767  79.088  1.00 38.29 ? 674  GLU B OE2   1 
ATOM   13669 N N     . ALA B  1 677  ? 9.286   28.554  75.649  1.00 19.54 ? 675  ALA B N     1 
ATOM   13670 C CA    . ALA B  1 677  ? 9.345   28.652  74.187  1.00 21.55 ? 675  ALA B CA    1 
ATOM   13671 C C     . ALA B  1 677  ? 7.952   28.672  73.565  1.00 21.21 ? 675  ALA B C     1 
ATOM   13672 O O     . ALA B  1 677  ? 7.663   29.497  72.686  1.00 20.16 ? 675  ALA B O     1 
ATOM   13673 C CB    . ALA B  1 677  ? 10.154  27.491  73.605  1.00 20.99 ? 675  ALA B CB    1 
ATOM   13674 N N     . ILE B  1 678  ? 7.090   27.734  73.978  1.00 21.74 ? 676  ILE B N     1 
ATOM   13675 C CA    . ILE B  1 678  ? 5.702   27.695  73.498  1.00 16.35 ? 676  ILE B CA    1 
ATOM   13676 C C     . ILE B  1 678  ? 5.004   29.015  73.802  1.00 19.36 ? 676  ILE B C     1 
ATOM   13677 O O     . ILE B  1 678  ? 4.313   29.581  72.957  1.00 19.40 ? 676  ILE B O     1 
ATOM   13678 C CB    . ILE B  1 678  ? 4.962   26.505  74.136  1.00 18.96 ? 676  ILE B CB    1 
ATOM   13679 C CG1   . ILE B  1 678  ? 5.590   25.179  73.684  1.00 23.71 ? 676  ILE B CG1   1 
ATOM   13680 C CG2   . ILE B  1 678  ? 3.446   26.532  73.827  1.00 18.04 ? 676  ILE B CG2   1 
ATOM   13681 C CD1   . ILE B  1 678  ? 5.251   24.014  74.591  1.00 20.14 ? 676  ILE B CD1   1 
ATOM   13682 N N     . ASP B  1 679  ? 5.166   29.521  75.029  1.00 18.72 ? 677  ASP B N     1 
ATOM   13683 C CA    . ASP B  1 679  ? 4.537   30.785  75.409  1.00 21.95 ? 677  ASP B CA    1 
ATOM   13684 C C     . ASP B  1 679  ? 5.007   31.957  74.543  1.00 19.55 ? 677  ASP B C     1 
ATOM   13685 O O     . ASP B  1 679  ? 4.195   32.791  74.141  1.00 18.25 ? 677  ASP B O     1 
ATOM   13686 C CB    . ASP B  1 679  ? 4.818   31.079  76.885  1.00 19.37 ? 677  ASP B CB    1 
ATOM   13687 C CG    . ASP B  1 679  ? 4.053   30.149  77.820  1.00 23.98 ? 677  ASP B CG    1 
ATOM   13688 O OD1   . ASP B  1 679  ? 3.001   29.636  77.406  1.00 24.89 ? 677  ASP B OD1   1 
ATOM   13689 O OD2   . ASP B  1 679  ? 4.516   29.922  78.961  1.00 27.07 ? 677  ASP B OD2   1 
ATOM   13690 N N     . PHE B  1 680  ? 6.317   32.068  74.287  1.00 18.96 ? 678  PHE B N     1 
ATOM   13691 C CA    . PHE B  1 680  ? 6.810   33.137  73.418  1.00 19.91 ? 678  PHE B CA    1 
ATOM   13692 C C     . PHE B  1 680  ? 6.153   33.075  72.049  1.00 19.68 ? 678  PHE B C     1 
ATOM   13693 O O     . PHE B  1 680  ? 5.725   34.098  71.500  1.00 19.13 ? 678  PHE B O     1 
ATOM   13694 C CB    . PHE B  1 680  ? 8.321   33.028  73.239  1.00 16.85 ? 678  PHE B CB    1 
ATOM   13695 C CG    . PHE B  1 680  ? 9.134   33.702  74.309  1.00 19.49 ? 678  PHE B CG    1 
ATOM   13696 C CD1   . PHE B  1 680  ? 8.880   35.007  74.698  1.00 18.71 ? 678  PHE B CD1   1 
ATOM   13697 C CD2   . PHE B  1 680  ? 10.195  33.030  74.885  1.00 20.54 ? 678  PHE B CD2   1 
ATOM   13698 C CE1   . PHE B  1 680  ? 9.675   35.627  75.688  1.00 21.46 ? 678  PHE B CE1   1 
ATOM   13699 C CE2   . PHE B  1 680  ? 10.978  33.628  75.869  1.00 21.59 ? 678  PHE B CE2   1 
ATOM   13700 C CZ    . PHE B  1 680  ? 10.718  34.930  76.266  1.00 22.08 ? 678  PHE B CZ    1 
ATOM   13701 N N     . LEU B  1 681  ? 6.097   31.878  71.469  1.00 18.55 ? 679  LEU B N     1 
ATOM   13702 C CA    . LEU B  1 681  ? 5.495   31.719  70.144  1.00 17.49 ? 679  LEU B CA    1 
ATOM   13703 C C     . LEU B  1 681  ? 4.041   32.171  70.145  1.00 21.69 ? 679  LEU B C     1 
ATOM   13704 O O     . LEU B  1 681  ? 3.609   32.911  69.253  1.00 18.58 ? 679  LEU B O     1 
ATOM   13705 C CB    . LEU B  1 681  ? 5.583   30.257  69.691  1.00 20.40 ? 679  LEU B CB    1 
ATOM   13706 C CG    . LEU B  1 681  ? 6.972   29.709  69.399  1.00 23.56 ? 679  LEU B CG    1 
ATOM   13707 C CD1   . LEU B  1 681  ? 6.969   28.194  69.531  1.00 20.87 ? 679  LEU B CD1   1 
ATOM   13708 C CD2   . LEU B  1 681  ? 7.437   30.139  68.010  1.00 20.29 ? 679  LEU B CD2   1 
ATOM   13709 N N     . ARG B  1 682  ? 3.262   31.720  71.139  1.00 17.83 ? 680  ARG B N     1 
ATOM   13710 C CA    . ARG B  1 682  ? 1.842   32.059  71.174  1.00 21.28 ? 680  ARG B CA    1 
ATOM   13711 C C     . ARG B  1 682  ? 1.630   33.505  71.580  1.00 19.86 ? 680  ARG B C     1 
ATOM   13712 O O     . ARG B  1 682  ? 0.695   34.151  71.103  1.00 21.65 ? 680  ARG B O     1 
ATOM   13713 C CB    . ARG B  1 682  ? 1.090   31.123  72.127  1.00 18.43 ? 680  ARG B CB    1 
ATOM   13714 C CG    . ARG B  1 682  ? 0.931   29.689  71.574  1.00 20.54 ? 680  ARG B CG    1 
ATOM   13715 C CD    . ARG B  1 682  ? 0.279   28.797  72.599  1.00 21.64 ? 680  ARG B CD    1 
ATOM   13716 N NE    . ARG B  1 682  ? 0.074   27.458  72.076  1.00 20.09 ? 680  ARG B NE    1 
ATOM   13717 C CZ    . ARG B  1 682  ? -0.094  26.392  72.833  1.00 21.77 ? 680  ARG B CZ    1 
ATOM   13718 N NH1   . ARG B  1 682  ? -0.167  26.491  74.153  1.00 22.28 ? 680  ARG B NH1   1 
ATOM   13719 N NH2   . ARG B  1 682  ? -0.140  25.198  72.258  1.00 21.43 ? 680  ARG B NH2   1 
ATOM   13720 N N     . TYR B  1 683  ? 2.484   34.035  72.454  1.00 21.20 ? 681  TYR B N     1 
ATOM   13721 C CA    . TYR B  1 683  ? 2.330   35.432  72.846  1.00 20.86 ? 681  TYR B CA    1 
ATOM   13722 C C     . TYR B  1 683  ? 2.602   36.369  71.673  1.00 19.96 ? 681  TYR B C     1 
ATOM   13723 O O     . TYR B  1 683  ? 1.789   37.254  71.375  1.00 19.75 ? 681  TYR B O     1 
ATOM   13724 C CB    . TYR B  1 683  ? 3.246   35.752  74.025  1.00 21.44 ? 681  TYR B CB    1 
ATOM   13725 C CG    . TYR B  1 683  ? 3.195   37.209  74.418  1.00 20.07 ? 681  TYR B CG    1 
ATOM   13726 C CD1   . TYR B  1 683  ? 2.154   37.693  75.194  1.00 20.74 ? 681  TYR B CD1   1 
ATOM   13727 C CD2   . TYR B  1 683  ? 4.201   38.102  74.017  1.00 18.81 ? 681  TYR B CD2   1 
ATOM   13728 C CE1   . TYR B  1 683  ? 2.084   39.024  75.547  1.00 21.33 ? 681  TYR B CE1   1 
ATOM   13729 C CE2   . TYR B  1 683  ? 4.141   39.437  74.368  1.00 19.80 ? 681  TYR B CE2   1 
ATOM   13730 C CZ    . TYR B  1 683  ? 3.064   39.893  75.138  1.00 22.55 ? 681  TYR B CZ    1 
ATOM   13731 O OH    . TYR B  1 683  ? 2.954   41.215  75.512  1.00 21.10 ? 681  TYR B OH    1 
ATOM   13732 N N     . TYR B  1 684  ? 3.718   36.169  70.959  1.00 19.46 ? 682  TYR B N     1 
ATOM   13733 C CA    . TYR B  1 684  ? 4.030   37.097  69.874  1.00 20.51 ? 682  TYR B CA    1 
ATOM   13734 C C     . TYR B  1 684  ? 3.081   36.898  68.693  1.00 21.78 ? 682  TYR B C     1 
ATOM   13735 O O     . TYR B  1 684  ? 2.796   37.849  67.961  1.00 20.62 ? 682  TYR B O     1 
ATOM   13736 C CB    . TYR B  1 684  ? 5.493   36.955  69.433  1.00 22.10 ? 682  TYR B CB    1 
ATOM   13737 C CG    . TYR B  1 684  ? 6.511   37.342  70.495  1.00 20.64 ? 682  TYR B CG    1 
ATOM   13738 C CD1   . TYR B  1 684  ? 6.363   38.495  71.265  1.00 21.35 ? 682  TYR B CD1   1 
ATOM   13739 C CD2   . TYR B  1 684  ? 7.625   36.550  70.721  1.00 19.74 ? 682  TYR B CD2   1 
ATOM   13740 C CE1   . TYR B  1 684  ? 7.305   38.830  72.252  1.00 21.17 ? 682  TYR B CE1   1 
ATOM   13741 C CE2   . TYR B  1 684  ? 8.562   36.884  71.691  1.00 19.36 ? 682  TYR B CE2   1 
ATOM   13742 C CZ    . TYR B  1 684  ? 8.386   38.010  72.456  1.00 19.80 ? 682  TYR B CZ    1 
ATOM   13743 O OH    . TYR B  1 684  ? 9.345   38.304  73.410  1.00 21.11 ? 682  TYR B OH    1 
ATOM   13744 N N     . ALA B  1 685  ? 2.546   35.687  68.526  1.00 19.31 ? 683  ALA B N     1 
ATOM   13745 C CA    . ALA B  1 685  ? 1.471   35.464  67.563  1.00 21.72 ? 683  ALA B CA    1 
ATOM   13746 C C     . ALA B  1 685  ? 0.247   36.317  67.896  1.00 22.54 ? 683  ALA B C     1 
ATOM   13747 O O     . ALA B  1 685  ? -0.265  37.052  67.046  1.00 18.73 ? 683  ALA B O     1 
ATOM   13748 C CB    . ALA B  1 685  ? 1.115   33.978  67.530  1.00 18.52 ? 683  ALA B CB    1 
ATOM   13749 N N     . GLU B  1 686  ? -0.207  36.271  69.147  1.00 19.14 ? 684  GLU B N     1 
ATOM   13750 C CA    . GLU B  1 686  ? -1.385  37.055  69.520  1.00 22.62 ? 684  GLU B CA    1 
ATOM   13751 C C     . GLU B  1 686  ? -1.105  38.553  69.443  1.00 22.74 ? 684  GLU B C     1 
ATOM   13752 O O     . GLU B  1 686  ? -1.933  39.317  68.937  1.00 22.09 ? 684  GLU B O     1 
ATOM   13753 C CB    . GLU B  1 686  ? -1.850  36.667  70.919  1.00 25.55 ? 684  GLU B CB    1 
ATOM   13754 C CG    . GLU B  1 686  ? -2.926  37.597  71.469  1.00 26.98 ? 684  GLU B CG    1 
ATOM   13755 C CD    . GLU B  1 686  ? -4.258  37.542  70.675  1.00 33.96 ? 684  GLU B CD    1 
ATOM   13756 O OE1   . GLU B  1 686  ? -4.427  36.698  69.746  1.00 35.36 ? 684  GLU B OE1   1 
ATOM   13757 O OE2   . GLU B  1 686  ? -5.156  38.353  71.002  1.00 32.22 ? 684  GLU B OE2   1 
ATOM   13758 N N     . GLN B  1 687  ? 0.068   38.993  69.910  1.00 20.05 ? 685  GLN B N     1 
ATOM   13759 C CA    . GLN B  1 687  ? 0.417   40.413  69.803  1.00 20.37 ? 685  GLN B CA    1 
ATOM   13760 C C     . GLN B  1 687  ? 0.429   40.877  68.350  1.00 21.04 ? 685  GLN B C     1 
ATOM   13761 O O     . GLN B  1 687  ? -0.037  41.981  68.037  1.00 21.01 ? 685  GLN B O     1 
ATOM   13762 C CB    . GLN B  1 687  ? 1.771   40.680  70.466  1.00 22.62 ? 685  GLN B CB    1 
ATOM   13763 C CG    . GLN B  1 687  ? 1.713   40.496  71.992  1.00 19.85 ? 685  GLN B CG    1 
ATOM   13764 C CD    . GLN B  1 687  ? 0.674   41.391  72.633  1.00 23.36 ? 685  GLN B CD    1 
ATOM   13765 O OE1   . GLN B  1 687  ? 0.697   42.603  72.452  1.00 23.60 ? 685  GLN B OE1   1 
ATOM   13766 N NE2   . GLN B  1 687  ? -0.257  40.793  73.364  1.00 24.46 ? 685  GLN B NE2   1 
ATOM   13767 N N     . THR B  1 688  ? 0.931   40.035  67.443  1.00 18.46 ? 686  THR B N     1 
ATOM   13768 C CA    . THR B  1 688  ? 0.829   40.338  66.018  1.00 21.08 ? 686  THR B CA    1 
ATOM   13769 C C     . THR B  1 688  ? -0.624  40.473  65.570  1.00 20.08 ? 686  THR B C     1 
ATOM   13770 O O     . THR B  1 688  ? -0.997  41.456  64.918  1.00 21.80 ? 686  THR B O     1 
ATOM   13771 C CB    . THR B  1 688  ? 1.537   39.255  65.207  1.00 20.92 ? 686  THR B CB    1 
ATOM   13772 O OG1   . THR B  1 688  ? 2.917   39.247  65.547  1.00 22.11 ? 686  THR B OG1   1 
ATOM   13773 C CG2   . THR B  1 688  ? 1.380   39.540  63.716  1.00 22.12 ? 686  THR B CG2   1 
ATOM   13774 N N     . ARG B  1 689  ? -1.465  39.486  65.892  1.00 21.23 ? 687  ARG B N     1 
ATOM   13775 C CA    . ARG B  1 689  ? -2.875  39.580  65.498  1.00 23.05 ? 687  ARG B CA    1 
ATOM   13776 C C     . ARG B  1 689  ? -3.546  40.842  66.045  1.00 24.80 ? 687  ARG B C     1 
ATOM   13777 O O     . ARG B  1 689  ? -4.501  41.349  65.443  1.00 23.76 ? 687  ARG B O     1 
ATOM   13778 C CB    . ARG B  1 689  ? -3.633  38.335  65.958  1.00 22.60 ? 687  ARG B CB    1 
ATOM   13779 C CG    . ARG B  1 689  ? -3.433  37.121  65.048  1.00 23.53 ? 687  ARG B CG    1 
ATOM   13780 C CD    . ARG B  1 689  ? -4.291  35.957  65.487  1.00 27.33 ? 687  ARG B CD    1 
ATOM   13781 N NE    . ARG B  1 689  ? -4.059  35.576  66.877  1.00 23.98 ? 687  ARG B NE    1 
ATOM   13782 C CZ    . ARG B  1 689  ? -3.247  34.600  67.256  1.00 26.12 ? 687  ARG B CZ    1 
ATOM   13783 N NH1   . ARG B  1 689  ? -2.513  33.936  66.381  1.00 25.69 ? 687  ARG B NH1   1 
ATOM   13784 N NH2   . ARG B  1 689  ? -3.188  34.269  68.540  1.00 25.70 ? 687  ARG B NH2   1 
ATOM   13785 N N     . ARG B  1 690  ? -3.062  41.370  67.173  1.00 21.14 ? 688  ARG B N     1 
ATOM   13786 C CA    . ARG B  1 690  ? -3.647  42.585  67.735  1.00 23.69 ? 688  ARG B CA    1 
ATOM   13787 C C     . ARG B  1 690  ? -3.108  43.878  67.118  1.00 24.71 ? 688  ARG B C     1 
ATOM   13788 O O     . ARG B  1 690  ? -3.757  44.920  67.255  1.00 25.32 ? 688  ARG B O     1 
ATOM   13789 C CB    . ARG B  1 690  ? -3.409  42.638  69.247  1.00 21.16 ? 688  ARG B CB    1 
ATOM   13790 C CG    . ARG B  1 690  ? -4.120  41.551  70.054  1.00 26.83 ? 688  ARG B CG    1 
ATOM   13791 C CD    . ARG B  1 690  ? -5.613  41.822  70.211  1.00 28.22 ? 688  ARG B CD    1 
ATOM   13792 N NE    . ARG B  1 690  ? -5.819  43.056  70.962  1.00 28.79 ? 688  ARG B NE    1 
ATOM   13793 C CZ    . ARG B  1 690  ? -6.395  44.140  70.464  1.00 32.04 ? 688  ARG B CZ    1 
ATOM   13794 N NH1   . ARG B  1 690  ? -6.920  44.146  69.243  1.00 31.18 ? 688  ARG B NH1   1 
ATOM   13795 N NH2   . ARG B  1 690  ? -6.466  45.240  71.214  1.00 28.25 ? 688  ARG B NH2   1 
ATOM   13796 N N     . THR B  1 691  ? -1.948  43.863  66.454  1.00 22.92 ? 689  THR B N     1 
ATOM   13797 C CA    . THR B  1 691  ? -1.307  45.142  66.146  1.00 25.68 ? 689  THR B CA    1 
ATOM   13798 C C     . THR B  1 691  ? -0.865  45.358  64.701  1.00 27.47 ? 689  THR B C     1 
ATOM   13799 O O     . THR B  1 691  ? -1.077  46.448  64.164  1.00 29.71 ? 689  THR B O     1 
ATOM   13800 C CB    . THR B  1 691  ? -0.081  45.366  67.040  1.00 24.44 ? 689  THR B CB    1 
ATOM   13801 O OG1   . THR B  1 691  ? 0.859   44.302  66.856  1.00 22.12 ? 689  THR B OG1   1 
ATOM   13802 C CG2   . THR B  1 691  ? -0.488  45.429  68.538  1.00 24.76 ? 689  THR B CG2   1 
ATOM   13803 N N     . LEU B  1 692  ? -0.221  44.379  64.067  1.00 27.50 ? 690  LEU B N     1 
ATOM   13804 C CA    . LEU B  1 692  ? 0.513   44.667  62.840  1.00 23.17 ? 690  LEU B CA    1 
ATOM   13805 C C     . LEU B  1 692  ? -0.407  44.823  61.637  1.00 25.29 ? 690  LEU B C     1 
ATOM   13806 O O     . LEU B  1 692  ? -1.242  43.958  61.352  1.00 24.67 ? 690  LEU B O     1 
ATOM   13807 C CB    . LEU B  1 692  ? 1.562   43.580  62.556  1.00 23.50 ? 690  LEU B CB    1 
ATOM   13808 C CG    . LEU B  1 692  ? 2.665   43.500  63.620  1.00 25.36 ? 690  LEU B CG    1 
ATOM   13809 C CD1   . LEU B  1 692  ? 3.846   42.644  63.201  1.00 23.94 ? 690  LEU B CD1   1 
ATOM   13810 C CD2   . LEU B  1 692  ? 3.131   44.877  64.072  1.00 22.71 ? 690  LEU B CD2   1 
ATOM   13811 N N     . GLY B  1 693  ? -0.224  45.921  60.918  1.00 28.06 ? 691  GLY B N     1 
ATOM   13812 C CA    . GLY B  1 693  ? -0.924  46.176  59.683  1.00 29.11 ? 691  GLY B CA    1 
ATOM   13813 C C     . GLY B  1 693  ? 0.066   46.559  58.599  1.00 31.68 ? 691  GLY B C     1 
ATOM   13814 O O     . GLY B  1 693  ? 1.282   46.474  58.789  1.00 29.67 ? 691  GLY B O     1 
ATOM   13815 N N     . PRO B  1 694  ? -0.434  47.021  57.451  1.00 31.80 ? 692  PRO B N     1 
ATOM   13816 C CA    . PRO B  1 694  ? 0.465   47.230  56.304  1.00 32.23 ? 692  PRO B CA    1 
ATOM   13817 C C     . PRO B  1 694  ? 1.483   48.350  56.503  1.00 33.67 ? 692  PRO B C     1 
ATOM   13818 O O     . PRO B  1 694  ? 2.590   48.270  55.949  1.00 33.73 ? 692  PRO B O     1 
ATOM   13819 C CB    . PRO B  1 694  ? -0.497  47.520  55.140  1.00 34.67 ? 692  PRO B CB    1 
ATOM   13820 C CG    . PRO B  1 694  ? -1.839  47.823  55.754  1.00 35.63 ? 692  PRO B CG    1 
ATOM   13821 C CD    . PRO B  1 694  ? -1.861  47.210  57.126  1.00 32.79 ? 692  PRO B CD    1 
ATOM   13822 N N     . GLY B  1 695  ? 1.167   49.372  57.293  1.00 32.92 ? 693  GLY B N     1 
ATOM   13823 C CA    . GLY B  1 695  ? 2.118   50.435  57.554  1.00 29.60 ? 693  GLY B CA    1 
ATOM   13824 C C     . GLY B  1 695  ? 3.234   50.126  58.536  1.00 33.95 ? 693  GLY B C     1 
ATOM   13825 O O     . GLY B  1 695  ? 4.100   50.982  58.746  1.00 31.28 ? 693  GLY B O     1 
ATOM   13826 N N     . HIS B  1 696  ? 3.246   48.941  59.155  1.00 30.61 ? 694  HIS B N     1 
ATOM   13827 C CA    . HIS B  1 696  ? 4.311   48.560  60.086  1.00 30.83 ? 694  HIS B CA    1 
ATOM   13828 C C     . HIS B  1 696  ? 5.292   47.665  59.335  1.00 33.29 ? 694  HIS B C     1 
ATOM   13829 O O     . HIS B  1 696  ? 5.277   46.436  59.435  1.00 31.98 ? 694  HIS B O     1 
ATOM   13830 C CB    . HIS B  1 696  ? 3.729   47.886  61.321  1.00 29.08 ? 694  HIS B CB    1 
ATOM   13831 C CG    . HIS B  1 696  ? 2.591   48.647  61.916  1.00 29.36 ? 694  HIS B CG    1 
ATOM   13832 N ND1   . HIS B  1 696  ? 1.290   48.189  61.891  1.00 29.37 ? 694  HIS B ND1   1 
ATOM   13833 C CD2   . HIS B  1 696  ? 2.551   49.864  62.505  1.00 26.67 ? 694  HIS B CD2   1 
ATOM   13834 C CE1   . HIS B  1 696  ? 0.504   49.081  62.462  1.00 28.40 ? 694  HIS B CE1   1 
ATOM   13835 N NE2   . HIS B  1 696  ? 1.243   50.111  62.834  1.00 27.60 ? 694  HIS B NE2   1 
ATOM   13836 N N     . GLY B  1 697  ? 6.165   48.313  58.572  1.00 33.02 ? 695  GLY B N     1 
ATOM   13837 C CA    . GLY B  1 697  ? 7.077   47.616  57.699  1.00 31.59 ? 695  GLY B CA    1 
ATOM   13838 C C     . GLY B  1 697  ? 8.204   46.954  58.456  1.00 28.35 ? 695  GLY B C     1 
ATOM   13839 O O     . GLY B  1 697  ? 8.660   47.450  59.494  1.00 28.47 ? 695  GLY B O     1 
ATOM   13840 N N     . PRO B  1 698  ? 8.676   45.818  57.949  1.00 30.45 ? 696  PRO B N     1 
ATOM   13841 C CA    . PRO B  1 698  ? 9.782   45.117  58.605  1.00 28.63 ? 696  PRO B CA    1 
ATOM   13842 C C     . PRO B  1 698  ? 11.082  45.881  58.473  1.00 26.50 ? 696  PRO B C     1 
ATOM   13843 O O     . PRO B  1 698  ? 11.255  46.739  57.607  1.00 25.13 ? 696  PRO B O     1 
ATOM   13844 C CB    . PRO B  1 698  ? 9.867   43.796  57.839  1.00 30.61 ? 696  PRO B CB    1 
ATOM   13845 C CG    . PRO B  1 698  ? 9.419   44.166  56.487  1.00 30.36 ? 696  PRO B CG    1 
ATOM   13846 C CD    . PRO B  1 698  ? 8.243   45.103  56.740  1.00 31.75 ? 696  PRO B CD    1 
ATOM   13847 N N     . LEU B  1 699  ? 12.025  45.518  59.339  1.00 24.91 ? 697  LEU B N     1 
ATOM   13848 C CA    . LEU B  1 699  ? 13.370  46.073  59.229  1.00 25.49 ? 697  LEU B CA    1 
ATOM   13849 C C     . LEU B  1 699  ? 14.143  45.422  58.095  1.00 26.37 ? 697  LEU B C     1 
ATOM   13850 O O     . LEU B  1 699  ? 14.866  46.105  57.361  1.00 27.61 ? 697  LEU B O     1 
ATOM   13851 C CB    . LEU B  1 699  ? 14.126  45.884  60.543  1.00 25.72 ? 697  LEU B CB    1 
ATOM   13852 C CG    . LEU B  1 699  ? 13.514  46.449  61.826  1.00 30.01 ? 697  LEU B CG    1 
ATOM   13853 C CD1   . LEU B  1 699  ? 14.394  46.024  63.012  1.00 27.75 ? 697  LEU B CD1   1 
ATOM   13854 C CD2   . LEU B  1 699  ? 13.394  47.970  61.761  1.00 30.85 ? 697  LEU B CD2   1 
ATOM   13855 N N     . GLY B  1 700  ? 14.012  44.105  57.942  1.00 27.09 ? 698  GLY B N     1 
ATOM   13856 C CA    . GLY B  1 700  ? 14.851  43.342  57.042  1.00 24.42 ? 698  GLY B CA    1 
ATOM   13857 C C     . GLY B  1 700  ? 15.551  42.243  57.816  1.00 26.82 ? 698  GLY B C     1 
ATOM   13858 O O     . GLY B  1 700  ? 15.135  41.899  58.923  1.00 27.47 ? 698  GLY B O     1 
ATOM   13859 N N     . PRO B  1 701  ? 16.640  41.693  57.276  1.00 28.06 ? 699  PRO B N     1 
ATOM   13860 C CA    . PRO B  1 701  ? 17.329  40.588  57.965  1.00 27.35 ? 699  PRO B CA    1 
ATOM   13861 C C     . PRO B  1 701  ? 17.711  40.954  59.393  1.00 26.31 ? 699  PRO B C     1 
ATOM   13862 O O     . PRO B  1 701  ? 18.304  41.999  59.648  1.00 27.53 ? 699  PRO B O     1 
ATOM   13863 C CB    . PRO B  1 701  ? 18.567  40.351  57.094  1.00 30.45 ? 699  PRO B CB    1 
ATOM   13864 C CG    . PRO B  1 701  ? 18.164  40.831  55.732  1.00 29.09 ? 699  PRO B CG    1 
ATOM   13865 C CD    . PRO B  1 701  ? 17.262  42.012  55.979  1.00 29.39 ? 699  PRO B CD    1 
ATOM   13866 N N     . ILE B  1 702  ? 17.350  40.088  60.333  1.00 25.83 ? 700  ILE B N     1 
ATOM   13867 C CA    . ILE B  1 702  ? 17.659  40.281  61.742  1.00 24.12 ? 700  ILE B CA    1 
ATOM   13868 C C     . ILE B  1 702  ? 18.579  39.165  62.172  1.00 25.99 ? 700  ILE B C     1 
ATOM   13869 O O     . ILE B  1 702  ? 18.286  37.987  61.939  1.00 25.21 ? 700  ILE B O     1 
ATOM   13870 C CB    . ILE B  1 702  ? 16.404  40.282  62.633  1.00 25.47 ? 700  ILE B CB    1 
ATOM   13871 C CG1   . ILE B  1 702  ? 15.440  41.396  62.222  1.00 30.00 ? 700  ILE B CG1   1 
ATOM   13872 C CG2   . ILE B  1 702  ? 16.814  40.369  64.107  1.00 23.14 ? 700  ILE B CG2   1 
ATOM   13873 C CD1   . ILE B  1 702  ? 16.004  42.766  62.307  1.00 27.86 ? 700  ILE B CD1   1 
ATOM   13874 N N     . VAL B  1 703  ? 19.675  39.536  62.813  1.00 25.63 ? 701  VAL B N     1 
ATOM   13875 C CA    . VAL B  1 703  ? 20.602  38.582  63.395  1.00 25.93 ? 701  VAL B CA    1 
ATOM   13876 C C     . VAL B  1 703  ? 20.141  38.348  64.826  1.00 25.05 ? 701  VAL B C     1 
ATOM   13877 O O     . VAL B  1 703  ? 19.987  39.303  65.597  1.00 23.40 ? 701  VAL B O     1 
ATOM   13878 C CB    . VAL B  1 703  ? 22.039  39.119  63.336  1.00 24.31 ? 701  VAL B CB    1 
ATOM   13879 C CG1   . VAL B  1 703  ? 22.987  38.235  64.128  1.00 27.33 ? 701  VAL B CG1   1 
ATOM   13880 C CG2   . VAL B  1 703  ? 22.486  39.244  61.862  1.00 23.38 ? 701  VAL B CG2   1 
ATOM   13881 N N     . CYS B  1 704  ? 19.893  37.086  65.178  1.00 20.19 ? 702  CYS B N     1 
ATOM   13882 C CA    . CYS B  1 704  ? 19.433  36.717  66.513  1.00 21.07 ? 702  CYS B CA    1 
ATOM   13883 C C     . CYS B  1 704  ? 20.520  35.892  67.179  1.00 22.89 ? 702  CYS B C     1 
ATOM   13884 O O     . CYS B  1 704  ? 20.789  34.769  66.750  1.00 24.78 ? 702  CYS B O     1 
ATOM   13885 C CB    . CYS B  1 704  ? 18.128  35.923  66.433  1.00 23.38 ? 702  CYS B CB    1 
ATOM   13886 S SG    . CYS B  1 704  ? 16.709  36.853  65.815  1.00 26.23 ? 702  CYS B SG    1 
ATOM   13887 N N     . ILE B  1 705  ? 21.151  36.444  68.220  1.00 24.50 ? 703  ILE B N     1 
ATOM   13888 C CA    . ILE B  1 705  ? 22.269  35.789  68.905  1.00 22.13 ? 703  ILE B CA    1 
ATOM   13889 C C     . ILE B  1 705  ? 21.793  35.383  70.292  1.00 21.69 ? 703  ILE B C     1 
ATOM   13890 O O     . ILE B  1 705  ? 21.378  36.236  71.088  1.00 23.50 ? 703  ILE B O     1 
ATOM   13891 C CB    . ILE B  1 705  ? 23.503  36.708  68.983  1.00 25.18 ? 703  ILE B CB    1 
ATOM   13892 C CG1   . ILE B  1 705  ? 24.030  37.006  67.573  1.00 25.20 ? 703  ILE B CG1   1 
ATOM   13893 C CG2   . ILE B  1 705  ? 24.596  36.065  69.848  1.00 24.59 ? 703  ILE B CG2   1 
ATOM   13894 C CD1   . ILE B  1 705  ? 25.210  37.988  67.521  1.00 28.55 ? 703  ILE B CD1   1 
ATOM   13895 N N     . SER B  1 706  ? 21.825  34.092  70.580  1.00 22.58 ? 704  SER B N     1 
ATOM   13896 C CA    . SER B  1 706  ? 21.212  33.582  71.795  1.00 25.43 ? 704  SER B CA    1 
ATOM   13897 C C     . SER B  1 706  ? 22.244  32.963  72.742  1.00 23.55 ? 704  SER B C     1 
ATOM   13898 O O     . SER B  1 706  ? 23.345  32.585  72.326  1.00 22.61 ? 704  SER B O     1 
ATOM   13899 C CB    . SER B  1 706  ? 20.134  32.547  71.440  1.00 23.50 ? 704  SER B CB    1 
ATOM   13900 O OG    . SER B  1 706  ? 20.667  31.571  70.569  1.00 22.87 ? 704  SER B OG    1 
ATOM   13901 N N     . PRO B  1 707  ? 21.910  32.833  74.020  1.00 26.07 ? 705  PRO B N     1 
ATOM   13902 C CA    . PRO B  1 707  ? 22.853  32.277  74.995  1.00 23.29 ? 705  PRO B CA    1 
ATOM   13903 C C     . PRO B  1 707  ? 22.673  30.774  75.198  1.00 27.17 ? 705  PRO B C     1 
ATOM   13904 O O     . PRO B  1 707  ? 21.765  30.141  74.657  1.00 28.24 ? 705  PRO B O     1 
ATOM   13905 C CB    . PRO B  1 707  ? 22.484  33.042  76.279  1.00 26.95 ? 705  PRO B CB    1 
ATOM   13906 C CG    . PRO B  1 707  ? 21.040  33.282  76.155  1.00 27.03 ? 705  PRO B CG    1 
ATOM   13907 C CD    . PRO B  1 707  ? 20.748  33.464  74.673  1.00 26.27 ? 705  PRO B CD    1 
ATOM   13908 N N     . TRP B  1 708  ? 23.577  30.206  75.994  1.00 26.66 ? 706  TRP B N     1 
ATOM   13909 C CA    . TRP B  1 708  ? 23.538  28.776  76.289  1.00 28.69 ? 706  TRP B CA    1 
ATOM   13910 C C     . TRP B  1 708  ? 22.668  28.432  77.486  1.00 24.05 ? 706  TRP B C     1 
ATOM   13911 O O     . TRP B  1 708  ? 22.392  27.248  77.706  1.00 25.85 ? 706  TRP B O     1 
ATOM   13912 C CB    . TRP B  1 708  ? 24.950  28.242  76.542  1.00 27.17 ? 706  TRP B CB    1 
ATOM   13913 C CG    . TRP B  1 708  ? 25.695  29.095  77.516  1.00 30.01 ? 706  TRP B CG    1 
ATOM   13914 C CD1   . TRP B  1 708  ? 26.585  30.083  77.222  1.00 29.61 ? 706  TRP B CD1   1 
ATOM   13915 C CD2   . TRP B  1 708  ? 25.582  29.066  78.943  1.00 22.51 ? 706  TRP B CD2   1 
ATOM   13916 N NE1   . TRP B  1 708  ? 27.049  30.656  78.379  1.00 28.84 ? 706  TRP B NE1   1 
ATOM   13917 C CE2   . TRP B  1 708  ? 26.435  30.058  79.448  1.00 29.49 ? 706  TRP B CE2   1 
ATOM   13918 C CE3   . TRP B  1 708  ? 24.853  28.281  79.841  1.00 27.78 ? 706  TRP B CE3   1 
ATOM   13919 C CZ2   . TRP B  1 708  ? 26.572  30.303  80.816  1.00 29.95 ? 706  TRP B CZ2   1 
ATOM   13920 C CZ3   . TRP B  1 708  ? 24.983  28.526  81.196  1.00 25.43 ? 706  TRP B CZ3   1 
ATOM   13921 C CH2   . TRP B  1 708  ? 25.847  29.519  81.670  1.00 30.10 ? 706  TRP B CH2   1 
ATOM   13922 N N     . ASN B  1 709  ? 22.238  29.421  78.271  1.00 22.39 ? 707  ASN B N     1 
ATOM   13923 C CA    . ASN B  1 709  ? 21.559  29.111  79.521  1.00 28.47 ? 707  ASN B CA    1 
ATOM   13924 C C     . ASN B  1 709  ? 20.053  28.949  79.362  1.00 28.04 ? 707  ASN B C     1 
ATOM   13925 O O     . ASN B  1 709  ? 19.425  28.275  80.182  1.00 29.54 ? 707  ASN B O     1 
ATOM   13926 C CB    . ASN B  1 709  ? 21.882  30.180  80.577  1.00 25.47 ? 707  ASN B CB    1 
ATOM   13927 C CG    . ASN B  1 709  ? 21.319  31.551  80.222  1.00 30.36 ? 707  ASN B CG    1 
ATOM   13928 O OD1   . ASN B  1 709  ? 21.180  31.896  79.049  1.00 34.92 ? 707  ASN B OD1   1 
ATOM   13929 N ND2   . ASN B  1 709  ? 20.997  32.335  81.235  1.00 29.55 ? 707  ASN B ND2   1 
ATOM   13930 N N     . PHE B  1 710  ? 19.462  29.528  78.327  1.00 29.04 ? 708  PHE B N     1 
ATOM   13931 C CA    . PHE B  1 710  ? 18.094  29.211  77.916  1.00 29.07 ? 708  PHE B CA    1 
ATOM   13932 C C     . PHE B  1 710  ? 18.143  28.909  76.434  1.00 25.45 ? 708  PHE B C     1 
ATOM   13933 O O     . PHE B  1 710  ? 17.647  29.678  75.607  1.00 24.13 ? 708  PHE B O     1 
ATOM   13934 C CB    . PHE B  1 710  ? 17.125  30.346  78.236  1.00 28.32 ? 708  PHE B CB    1 
ATOM   13935 C CG    . PHE B  1 710  ? 16.940  30.546  79.698  1.00 31.83 ? 708  PHE B CG    1 
ATOM   13936 C CD1   . PHE B  1 710  ? 16.206  29.627  80.438  1.00 33.52 ? 708  PHE B CD1   1 
ATOM   13937 C CD2   . PHE B  1 710  ? 17.555  31.603  80.347  1.00 32.51 ? 708  PHE B CD2   1 
ATOM   13938 C CE1   . PHE B  1 710  ? 16.051  29.786  81.807  1.00 36.48 ? 708  PHE B CE1   1 
ATOM   13939 C CE2   . PHE B  1 710  ? 17.403  31.778  81.713  1.00 37.87 ? 708  PHE B CE2   1 
ATOM   13940 C CZ    . PHE B  1 710  ? 16.657  30.865  82.446  1.00 37.48 ? 708  PHE B CZ    1 
ATOM   13941 N N     . PRO B  1 711  ? 18.757  27.779  76.069  1.00 26.79 ? 709  PRO B N     1 
ATOM   13942 C CA    . PRO B  1 711  ? 19.126  27.549  74.676  1.00 25.41 ? 709  PRO B CA    1 
ATOM   13943 C C     . PRO B  1 711  ? 17.940  27.245  73.766  1.00 24.35 ? 709  PRO B C     1 
ATOM   13944 O O     . PRO B  1 711  ? 18.109  27.270  72.538  1.00 25.90 ? 709  PRO B O     1 
ATOM   13945 C CB    . PRO B  1 711  ? 20.086  26.355  74.779  1.00 25.23 ? 709  PRO B CB    1 
ATOM   13946 C CG    . PRO B  1 711  ? 19.553  25.590  75.945  1.00 25.46 ? 709  PRO B CG    1 
ATOM   13947 C CD    . PRO B  1 711  ? 19.129  26.641  76.932  1.00 24.67 ? 709  PRO B CD    1 
ATOM   13948 N N     . LEU B  1 712  ? 16.753  26.983  74.304  1.00 25.25 ? 710  LEU B N     1 
ATOM   13949 C CA    . LEU B  1 712  ? 15.547  26.940  73.481  1.00 24.47 ? 710  LEU B CA    1 
ATOM   13950 C C     . LEU B  1 712  ? 14.637  28.138  73.689  1.00 24.96 ? 710  LEU B C     1 
ATOM   13951 O O     . LEU B  1 712  ? 14.117  28.683  72.715  1.00 24.85 ? 710  LEU B O     1 
ATOM   13952 C CB    . LEU B  1 712  ? 14.736  25.659  73.738  1.00 22.36 ? 710  LEU B CB    1 
ATOM   13953 C CG    . LEU B  1 712  ? 13.494  25.477  72.837  1.00 22.62 ? 710  LEU B CG    1 
ATOM   13954 C CD1   . LEU B  1 712  ? 13.857  25.203  71.369  1.00 23.36 ? 710  LEU B CD1   1 
ATOM   13955 C CD2   . LEU B  1 712  ? 12.558  24.362  73.374  1.00 25.47 ? 710  LEU B CD2   1 
ATOM   13956 N N     . ALA B  1 713  ? 14.422  28.566  74.936  1.00 22.96 ? 711  ALA B N     1 
ATOM   13957 C CA    . ALA B  1 713  ? 13.399  29.571  75.195  1.00 24.05 ? 711  ALA B CA    1 
ATOM   13958 C C     . ALA B  1 713  ? 13.807  30.933  74.654  1.00 22.74 ? 711  ALA B C     1 
ATOM   13959 O O     . ALA B  1 713  ? 13.022  31.594  73.965  1.00 22.98 ? 711  ALA B O     1 
ATOM   13960 C CB    . ALA B  1 713  ? 13.100  29.660  76.699  1.00 26.01 ? 711  ALA B CB    1 
ATOM   13961 N N     . ILE B  1 714  ? 15.011  31.401  74.990  1.00 21.32 ? 712  ILE B N     1 
ATOM   13962 C CA    . ILE B  1 714  ? 15.418  32.722  74.502  1.00 21.54 ? 712  ILE B CA    1 
ATOM   13963 C C     . ILE B  1 714  ? 15.705  32.658  73.009  1.00 23.85 ? 712  ILE B C     1 
ATOM   13964 O O     . ILE B  1 714  ? 15.364  33.572  72.245  1.00 22.92 ? 712  ILE B O     1 
ATOM   13965 C CB    . ILE B  1 714  ? 16.626  33.238  75.299  1.00 26.91 ? 712  ILE B CB    1 
ATOM   13966 C CG1   . ILE B  1 714  ? 16.184  33.662  76.701  1.00 26.47 ? 712  ILE B CG1   1 
ATOM   13967 C CG2   . ILE B  1 714  ? 17.295  34.402  74.584  1.00 26.62 ? 712  ILE B CG2   1 
ATOM   13968 C CD1   . ILE B  1 714  ? 17.342  34.208  77.530  1.00 36.76 ? 712  ILE B CD1   1 
ATOM   13969 N N     . PHE B  1 715  ? 16.350  31.579  72.580  1.00 24.13 ? 713  PHE B N     1 
ATOM   13970 C CA    . PHE B  1 715  ? 16.504  31.294  71.164  1.00 22.85 ? 713  PHE B CA    1 
ATOM   13971 C C     . PHE B  1 715  ? 15.180  31.465  70.422  1.00 25.06 ? 713  PHE B C     1 
ATOM   13972 O O     . PHE B  1 715  ? 15.093  32.226  69.451  1.00 24.59 ? 713  PHE B O     1 
ATOM   13973 C CB    . PHE B  1 715  ? 17.043  29.878  71.021  1.00 22.83 ? 713  PHE B CB    1 
ATOM   13974 C CG    . PHE B  1 715  ? 17.213  29.432  69.613  1.00 23.57 ? 713  PHE B CG    1 
ATOM   13975 C CD1   . PHE B  1 715  ? 18.365  29.739  68.924  1.00 21.93 ? 713  PHE B CD1   1 
ATOM   13976 C CD2   . PHE B  1 715  ? 16.215  28.717  68.978  1.00 23.84 ? 713  PHE B CD2   1 
ATOM   13977 C CE1   . PHE B  1 715  ? 18.532  29.334  67.598  1.00 23.16 ? 713  PHE B CE1   1 
ATOM   13978 C CE2   . PHE B  1 715  ? 16.367  28.305  67.646  1.00 23.97 ? 713  PHE B CE2   1 
ATOM   13979 C CZ    . PHE B  1 715  ? 17.530  28.614  66.966  1.00 26.02 ? 713  PHE B CZ    1 
ATOM   13980 N N     . THR B  1 716  ? 14.134  30.772  70.887  1.00 22.96 ? 714  THR B N     1 
ATOM   13981 C CA    . THR B  1 716  ? 12.844  30.790  70.198  1.00 21.83 ? 714  THR B CA    1 
ATOM   13982 C C     . THR B  1 716  ? 12.179  32.155  70.282  1.00 21.63 ? 714  THR B C     1 
ATOM   13983 O O     . THR B  1 716  ? 11.587  32.617  69.297  1.00 23.36 ? 714  THR B O     1 
ATOM   13984 C CB    . THR B  1 716  ? 11.924  29.703  70.773  1.00 19.31 ? 714  THR B CB    1 
ATOM   13985 O OG1   . THR B  1 716  ? 12.534  28.416  70.559  1.00 24.43 ? 714  THR B OG1   1 
ATOM   13986 C CG2   . THR B  1 716  ? 10.544  29.717  70.084  1.00 20.17 ? 714  THR B CG2   1 
ATOM   13987 N N     . GLY B  1 717  ? 12.270  32.819  71.437  1.00 21.21 ? 715  GLY B N     1 
ATOM   13988 C CA    . GLY B  1 717  ? 11.562  34.078  71.608  1.00 20.36 ? 715  GLY B CA    1 
ATOM   13989 C C     . GLY B  1 717  ? 12.092  35.177  70.703  1.00 22.68 ? 715  GLY B C     1 
ATOM   13990 O O     . GLY B  1 717  ? 11.318  35.916  70.086  1.00 22.02 ? 715  GLY B O     1 
ATOM   13991 N N     . GLN B  1 718  ? 13.422  35.320  70.625  1.00 21.03 ? 716  GLN B N     1 
ATOM   13992 C CA    . GLN B  1 718  ? 13.976  36.355  69.756  1.00 20.05 ? 716  GLN B CA    1 
ATOM   13993 C C     . GLN B  1 718  ? 13.633  36.065  68.304  1.00 21.03 ? 716  GLN B C     1 
ATOM   13994 O O     . GLN B  1 718  ? 13.232  36.965  67.555  1.00 20.32 ? 716  GLN B O     1 
ATOM   13995 C CB    . GLN B  1 718  ? 15.508  36.458  69.924  1.00 19.39 ? 716  GLN B CB    1 
ATOM   13996 C CG    . GLN B  1 718  ? 15.983  36.779  71.380  1.00 21.92 ? 716  GLN B CG    1 
ATOM   13997 C CD    . GLN B  1 718  ? 17.482  37.042  71.459  1.00 19.15 ? 716  GLN B CD    1 
ATOM   13998 O OE1   . GLN B  1 718  ? 17.926  37.992  72.116  1.00 24.81 ? 716  GLN B OE1   1 
ATOM   13999 N NE2   . GLN B  1 718  ? 18.272  36.199  70.793  1.00 21.01 ? 716  GLN B NE2   1 
ATOM   14000 N N     . ILE B  1 719  ? 13.765  34.801  67.898  1.00 20.41 ? 717  ILE B N     1 
ATOM   14001 C CA    . ILE B  1 719  ? 13.528  34.433  66.508  1.00 20.85 ? 717  ILE B CA    1 
ATOM   14002 C C     . ILE B  1 719  ? 12.060  34.601  66.152  1.00 20.24 ? 717  ILE B C     1 
ATOM   14003 O O     . ILE B  1 719  ? 11.726  35.155  65.097  1.00 20.52 ? 717  ILE B O     1 
ATOM   14004 C CB    . ILE B  1 719  ? 14.020  33.000  66.261  1.00 20.39 ? 717  ILE B CB    1 
ATOM   14005 C CG1   . ILE B  1 719  ? 15.550  32.965  66.307  1.00 22.80 ? 717  ILE B CG1   1 
ATOM   14006 C CG2   . ILE B  1 719  ? 13.520  32.480  64.937  1.00 25.25 ? 717  ILE B CG2   1 
ATOM   14007 C CD1   . ILE B  1 719  ? 16.086  31.593  66.393  1.00 25.31 ? 717  ILE B CD1   1 
ATOM   14008 N N     . ALA B  1 720  ? 11.163  34.139  67.031  1.00 20.76 ? 718  ALA B N     1 
ATOM   14009 C CA    . ALA B  1 720  ? 9.726   34.222  66.758  1.00 24.75 ? 718  ALA B CA    1 
ATOM   14010 C C     . ALA B  1 720  ? 9.271   35.667  66.612  1.00 23.29 ? 718  ALA B C     1 
ATOM   14011 O O     . ALA B  1 720  ? 8.471   35.992  65.720  1.00 21.13 ? 718  ALA B O     1 
ATOM   14012 C CB    . ALA B  1 720  ? 8.933   33.522  67.868  1.00 21.12 ? 718  ALA B CB    1 
ATOM   14013 N N     . ALA B  1 721  ? 9.784   36.552  67.470  1.00 19.70 ? 719  ALA B N     1 
ATOM   14014 C CA    . ALA B  1 721  ? 9.411   37.962  67.402  1.00 18.74 ? 719  ALA B CA    1 
ATOM   14015 C C     . ALA B  1 721  ? 9.896   38.607  66.107  1.00 24.41 ? 719  ALA B C     1 
ATOM   14016 O O     . ALA B  1 721  ? 9.153   39.353  65.460  1.00 24.34 ? 719  ALA B O     1 
ATOM   14017 C CB    . ALA B  1 721  ? 9.966   38.701  68.613  1.00 21.84 ? 719  ALA B CB    1 
ATOM   14018 N N     . ALA B  1 722  ? 11.154  38.353  65.724  1.00 22.20 ? 720  ALA B N     1 
ATOM   14019 C CA    . ALA B  1 722  ? 11.669  38.934  64.488  1.00 20.91 ? 720  ALA B CA    1 
ATOM   14020 C C     . ALA B  1 722  ? 10.902  38.394  63.280  1.00 20.50 ? 720  ALA B C     1 
ATOM   14021 O O     . ALA B  1 722  ? 10.521  39.159  62.383  1.00 21.70 ? 720  ALA B O     1 
ATOM   14022 C CB    . ALA B  1 722  ? 13.175  38.652  64.362  1.00 19.70 ? 720  ALA B CB    1 
ATOM   14023 N N     . LEU B  1 723  ? 10.642  37.084  63.257  1.00 17.59 ? 721  LEU B N     1 
ATOM   14024 C CA    . LEU B  1 723  ? 9.919   36.487  62.132  1.00 21.42 ? 721  LEU B CA    1 
ATOM   14025 C C     . LEU B  1 723  ? 8.504   37.030  62.025  1.00 23.16 ? 721  LEU B C     1 
ATOM   14026 O O     . LEU B  1 723  ? 8.041   37.368  60.928  1.00 24.40 ? 721  LEU B O     1 
ATOM   14027 C CB    . LEU B  1 723  ? 9.860   34.966  62.272  1.00 21.07 ? 721  LEU B CB    1 
ATOM   14028 C CG    . LEU B  1 723  ? 11.160  34.192  62.046  1.00 23.96 ? 721  LEU B CG    1 
ATOM   14029 C CD1   . LEU B  1 723  ? 10.923  32.739  62.447  1.00 26.16 ? 721  LEU B CD1   1 
ATOM   14030 C CD2   . LEU B  1 723  ? 11.606  34.290  60.601  1.00 20.96 ? 721  LEU B CD2   1 
ATOM   14031 N N     . VAL B  1 724  ? 7.772   37.065  63.146  1.00 19.77 ? 722  VAL B N     1 
ATOM   14032 C CA    . VAL B  1 724  ? 6.358   37.403  63.050  1.00 20.81 ? 722  VAL B CA    1 
ATOM   14033 C C     . VAL B  1 724  ? 6.187   38.876  62.692  1.00 22.13 ? 722  VAL B C     1 
ATOM   14034 O O     . VAL B  1 724  ? 5.203   39.255  62.044  1.00 25.41 ? 722  VAL B O     1 
ATOM   14035 C CB    . VAL B  1 724  ? 5.629   37.014  64.351  1.00 21.10 ? 722  VAL B CB    1 
ATOM   14036 C CG1   . VAL B  1 724  ? 5.829   38.075  65.454  1.00 22.19 ? 722  VAL B CG1   1 
ATOM   14037 C CG2   . VAL B  1 724  ? 4.138   36.719  64.075  1.00 19.81 ? 722  VAL B CG2   1 
ATOM   14038 N N     . ALA B  1 725  ? 7.172   39.711  63.024  1.00 23.15 ? 723  ALA B N     1 
ATOM   14039 C CA    . ALA B  1 725  ? 7.164   41.099  62.592  1.00 23.34 ? 723  ALA B CA    1 
ATOM   14040 C C     . ALA B  1 725  ? 7.511   41.255  61.115  1.00 26.39 ? 723  ALA B C     1 
ATOM   14041 O O     . ALA B  1 725  ? 7.544   42.389  60.632  1.00 26.52 ? 723  ALA B O     1 
ATOM   14042 C CB    . ALA B  1 725  ? 8.123   41.923  63.454  1.00 24.32 ? 723  ALA B CB    1 
ATOM   14043 N N     . GLY B  1 726  ? 7.764   40.167  60.390  1.00 24.70 ? 724  GLY B N     1 
ATOM   14044 C CA    . GLY B  1 726  ? 8.003   40.232  58.957  1.00 21.33 ? 724  GLY B CA    1 
ATOM   14045 C C     . GLY B  1 726  ? 9.467   40.283  58.532  1.00 25.36 ? 724  GLY B C     1 
ATOM   14046 O O     . GLY B  1 726  ? 9.740   40.609  57.371  1.00 25.48 ? 724  GLY B O     1 
ATOM   14047 N N     . ASN B  1 727  ? 10.418  39.950  59.428  1.00 22.23 ? 725  ASN B N     1 
ATOM   14048 C CA    . ASN B  1 727  ? 11.854  39.974  59.149  1.00 23.13 ? 725  ASN B CA    1 
ATOM   14049 C C     . ASN B  1 727  ? 12.392  38.567  58.953  1.00 22.38 ? 725  ASN B C     1 
ATOM   14050 O O     . ASN B  1 727  ? 12.078  37.672  59.750  1.00 26.30 ? 725  ASN B O     1 
ATOM   14051 C CB    . ASN B  1 727  ? 12.607  40.639  60.297  1.00 25.56 ? 725  ASN B CB    1 
ATOM   14052 C CG    . ASN B  1 727  ? 12.040  42.000  60.651  1.00 26.04 ? 725  ASN B CG    1 
ATOM   14053 O OD1   . ASN B  1 727  ? 12.255  42.981  59.935  1.00 26.26 ? 725  ASN B OD1   1 
ATOM   14054 N ND2   . ASN B  1 727  ? 11.315  42.069  61.764  1.00 22.59 ? 725  ASN B ND2   1 
ATOM   14055 N N     . PRO B  1 728  ? 13.200  38.310  57.930  1.00 24.82 ? 726  PRO B N     1 
ATOM   14056 C CA    . PRO B  1 728  ? 13.931  37.042  57.894  1.00 23.12 ? 726  PRO B CA    1 
ATOM   14057 C C     . PRO B  1 728  ? 15.038  37.066  58.937  1.00 26.12 ? 726  PRO B C     1 
ATOM   14058 O O     . PRO B  1 728  ? 15.562  38.128  59.288  1.00 25.00 ? 726  PRO B O     1 
ATOM   14059 C CB    . PRO B  1 728  ? 14.487  36.988  56.464  1.00 26.51 ? 726  PRO B CB    1 
ATOM   14060 C CG    . PRO B  1 728  ? 14.630  38.441  56.071  1.00 25.49 ? 726  PRO B CG    1 
ATOM   14061 C CD    . PRO B  1 728  ? 13.674  39.261  56.906  1.00 26.21 ? 726  PRO B CD    1 
ATOM   14062 N N     . VAL B  1 729  ? 15.370  35.881  59.453  1.00 26.25 ? 727  VAL B N     1 
ATOM   14063 C CA    . VAL B  1 729  ? 16.212  35.740  60.634  1.00 24.77 ? 727  VAL B CA    1 
ATOM   14064 C C     . VAL B  1 729  ? 17.454  34.918  60.319  1.00 25.76 ? 727  VAL B C     1 
ATOM   14065 O O     . VAL B  1 729  ? 17.379  33.857  59.679  1.00 25.48 ? 727  VAL B O     1 
ATOM   14066 C CB    . VAL B  1 729  ? 15.445  35.113  61.807  1.00 25.56 ? 727  VAL B CB    1 
ATOM   14067 C CG1   . VAL B  1 729  ? 16.422  34.640  62.875  1.00 20.03 ? 727  VAL B CG1   1 
ATOM   14068 C CG2   . VAL B  1 729  ? 14.448  36.110  62.356  1.00 22.09 ? 727  VAL B CG2   1 
ATOM   14069 N N     . LEU B  1 730  ? 18.589  35.419  60.772  1.00 21.86 ? 728  LEU B N     1 
ATOM   14070 C CA    . LEU B  1 730  ? 19.845  34.681  60.847  1.00 26.00 ? 728  LEU B CA    1 
ATOM   14071 C C     . LEU B  1 730  ? 20.032  34.300  62.310  1.00 24.02 ? 728  LEU B C     1 
ATOM   14072 O O     . LEU B  1 730  ? 20.247  35.174  63.151  1.00 26.72 ? 728  LEU B O     1 
ATOM   14073 C CB    . LEU B  1 730  ? 21.011  35.537  60.362  1.00 23.55 ? 728  LEU B CB    1 
ATOM   14074 C CG    . LEU B  1 730  ? 21.027  36.011  58.906  1.00 25.11 ? 728  LEU B CG    1 
ATOM   14075 C CD1   . LEU B  1 730  ? 20.625  34.870  57.962  1.00 24.34 ? 728  LEU B CD1   1 
ATOM   14076 C CD2   . LEU B  1 730  ? 20.121  37.225  58.713  1.00 27.42 ? 728  LEU B CD2   1 
ATOM   14077 N N     . ALA B  1 731  ? 19.921  33.018  62.621  1.00 24.96 ? 729  ALA B N     1 
ATOM   14078 C CA    . ALA B  1 731  ? 19.947  32.559  64.005  1.00 22.54 ? 729  ALA B CA    1 
ATOM   14079 C C     . ALA B  1 731  ? 21.338  32.018  64.333  1.00 24.20 ? 729  ALA B C     1 
ATOM   14080 O O     . ALA B  1 731  ? 21.771  31.026  63.748  1.00 24.70 ? 729  ALA B O     1 
ATOM   14081 C CB    . ALA B  1 731  ? 18.878  31.489  64.240  1.00 22.65 ? 729  ALA B CB    1 
ATOM   14082 N N     . LYS B  1 732  ? 22.038  32.676  65.263  1.00 22.86 ? 730  LYS B N     1 
ATOM   14083 C CA    . LYS B  1 732  ? 23.361  32.231  65.686  1.00 21.37 ? 730  LYS B CA    1 
ATOM   14084 C C     . LYS B  1 732  ? 23.268  31.749  67.125  1.00 25.41 ? 730  LYS B C     1 
ATOM   14085 O O     . LYS B  1 732  ? 23.319  32.571  68.053  1.00 23.91 ? 730  LYS B O     1 
ATOM   14086 C CB    . LYS B  1 732  ? 24.383  33.365  65.569  1.00 22.98 ? 730  LYS B CB    1 
ATOM   14087 C CG    . LYS B  1 732  ? 25.813  32.930  65.195  1.00 26.56 ? 730  LYS B CG    1 
ATOM   14088 C CD    . LYS B  1 732  ? 26.494  32.095  66.271  1.00 27.80 ? 730  LYS B CD    1 
ATOM   14089 C CE    . LYS B  1 732  ? 26.783  32.895  67.534  1.00 25.97 ? 730  LYS B CE    1 
ATOM   14090 N NZ    . LYS B  1 732  ? 27.470  32.020  68.508  1.00 29.80 ? 730  LYS B NZ    1 
ATOM   14091 N N     . PRO B  1 733  ? 23.162  30.444  67.367  1.00 25.76 ? 731  PRO B N     1 
ATOM   14092 C CA    . PRO B  1 733  ? 23.027  29.946  68.738  1.00 24.67 ? 731  PRO B CA    1 
ATOM   14093 C C     . PRO B  1 733  ? 24.373  29.889  69.436  1.00 24.65 ? 731  PRO B C     1 
ATOM   14094 O O     . PRO B  1 733  ? 25.430  29.962  68.813  1.00 25.88 ? 731  PRO B O     1 
ATOM   14095 C CB    . PRO B  1 733  ? 22.472  28.536  68.539  1.00 23.34 ? 731  PRO B CB    1 
ATOM   14096 C CG    . PRO B  1 733  ? 23.163  28.091  67.273  1.00 25.42 ? 731  PRO B CG    1 
ATOM   14097 C CD    . PRO B  1 733  ? 23.229  29.341  66.393  1.00 24.87 ? 731  PRO B CD    1 
ATOM   14098 N N     . ALA B  1 734  ? 24.309  29.752  70.759  1.00 26.33 ? 732  ALA B N     1 
ATOM   14099 C CA    . ALA B  1 734  ? 25.527  29.688  71.554  1.00 25.13 ? 732  ALA B CA    1 
ATOM   14100 C C     . ALA B  1 734  ? 26.383  28.497  71.134  1.00 27.43 ? 732  ALA B C     1 
ATOM   14101 O O     . ALA B  1 734  ? 25.872  27.423  70.801  1.00 23.97 ? 732  ALA B O     1 
ATOM   14102 C CB    . ALA B  1 734  ? 25.174  29.601  73.042  1.00 26.40 ? 732  ALA B CB    1 
ATOM   14103 N N     . GLU B  1 735  ? 27.702  28.696  71.151  1.00 25.24 ? 733  GLU B N     1 
ATOM   14104 C CA    . GLU B  1 735  ? 28.627  27.628  70.796  1.00 25.10 ? 733  GLU B CA    1 
ATOM   14105 C C     . GLU B  1 735  ? 28.361  26.357  71.596  1.00 29.32 ? 733  GLU B C     1 
ATOM   14106 O O     . GLU B  1 735  ? 28.539  25.246  71.087  1.00 26.76 ? 733  GLU B O     1 
ATOM   14107 C CB    . GLU B  1 735  ? 30.062  28.111  71.035  1.00 34.04 ? 733  GLU B CB    1 
ATOM   14108 C CG    . GLU B  1 735  ? 31.121  27.274  70.382  1.00 39.10 ? 733  GLU B CG    1 
ATOM   14109 C CD    . GLU B  1 735  ? 32.515  27.868  70.574  1.00 42.46 ? 733  GLU B CD    1 
ATOM   14110 O OE1   . GLU B  1 735  ? 32.610  29.068  70.936  1.00 43.48 ? 733  GLU B OE1   1 
ATOM   14111 O OE2   . GLU B  1 735  ? 33.496  27.124  70.373  1.00 45.75 ? 733  GLU B OE2   1 
ATOM   14112 N N     . GLU B  1 736  ? 27.927  26.501  72.846  1.00 24.63 ? 734  GLU B N     1 
ATOM   14113 C CA    . GLU B  1 736  ? 27.785  25.353  73.733  1.00 27.28 ? 734  GLU B CA    1 
ATOM   14114 C C     . GLU B  1 736  ? 26.545  24.515  73.446  1.00 26.18 ? 734  GLU B C     1 
ATOM   14115 O O     . GLU B  1 736  ? 26.554  23.308  73.709  1.00 28.31 ? 734  GLU B O     1 
ATOM   14116 C CB    . GLU B  1 736  ? 27.735  25.830  75.177  1.00 26.67 ? 734  GLU B CB    1 
ATOM   14117 C CG    . GLU B  1 736  ? 29.037  26.444  75.654  1.00 31.54 ? 734  GLU B CG    1 
ATOM   14118 C CD    . GLU B  1 736  ? 29.122  27.948  75.455  1.00 36.01 ? 734  GLU B CD    1 
ATOM   14119 O OE1   . GLU B  1 736  ? 28.364  28.518  74.645  1.00 28.68 ? 734  GLU B OE1   1 
ATOM   14120 O OE2   . GLU B  1 736  ? 29.968  28.572  76.122  1.00 39.34 ? 734  GLU B OE2   1 
ATOM   14121 N N     . THR B  1 737  ? 25.480  25.117  72.918  1.00 26.86 ? 735  THR B N     1 
ATOM   14122 C CA    . THR B  1 737  ? 24.172  24.460  72.828  1.00 27.46 ? 735  THR B CA    1 
ATOM   14123 C C     . THR B  1 737  ? 23.575  24.561  71.422  1.00 28.76 ? 735  THR B C     1 
ATOM   14124 O O     . THR B  1 737  ? 22.464  25.064  71.241  1.00 30.66 ? 735  THR B O     1 
ATOM   14125 C CB    . THR B  1 737  ? 23.215  25.053  73.866  1.00 26.55 ? 735  THR B CB    1 
ATOM   14126 O OG1   . THR B  1 737  ? 23.084  26.472  73.669  1.00 24.02 ? 735  THR B OG1   1 
ATOM   14127 C CG2   . THR B  1 737  ? 23.733  24.783  75.287  1.00 24.11 ? 735  THR B CG2   1 
ATOM   14128 N N     . PRO B  1 738  ? 24.281  24.075  70.394  1.00 28.89 ? 736  PRO B N     1 
ATOM   14129 C CA    . PRO B  1 738  ? 23.732  24.177  69.028  1.00 25.73 ? 736  PRO B CA    1 
ATOM   14130 C C     . PRO B  1 738  ? 22.664  23.146  68.697  1.00 26.77 ? 736  PRO B C     1 
ATOM   14131 O O     . PRO B  1 738  ? 21.878  23.382  67.775  1.00 26.20 ? 736  PRO B O     1 
ATOM   14132 C CB    . PRO B  1 738  ? 24.964  23.957  68.148  1.00 25.32 ? 736  PRO B CB    1 
ATOM   14133 C CG    . PRO B  1 738  ? 25.732  22.956  68.948  1.00 26.09 ? 736  PRO B CG    1 
ATOM   14134 C CD    . PRO B  1 738  ? 25.600  23.418  70.389  1.00 28.04 ? 736  PRO B CD    1 
ATOM   14135 N N     . LEU B  1 739  ? 22.622  22.009  69.394  1.00 23.64 ? 737  LEU B N     1 
ATOM   14136 C CA    . LEU B  1 739  ? 21.716  20.940  68.993  1.00 27.40 ? 737  LEU B CA    1 
ATOM   14137 C C     . LEU B  1 739  ? 20.261  21.310  69.258  1.00 26.66 ? 737  LEU B C     1 
ATOM   14138 O O     . LEU B  1 739  ? 19.397  21.074  68.410  1.00 24.12 ? 737  LEU B O     1 
ATOM   14139 C CB    . LEU B  1 739  ? 22.077  19.649  69.718  1.00 27.75 ? 737  LEU B CB    1 
ATOM   14140 C CG    . LEU B  1 739  ? 23.508  19.151  69.548  1.00 25.78 ? 737  LEU B CG    1 
ATOM   14141 C CD1   . LEU B  1 739  ? 23.715  17.966  70.470  1.00 28.25 ? 737  LEU B CD1   1 
ATOM   14142 C CD2   . LEU B  1 739  ? 23.804  18.756  68.099  1.00 26.97 ? 737  LEU B CD2   1 
ATOM   14143 N N     . ILE B  1 740  ? 19.960  21.878  70.427  1.00 26.42 ? 738  ILE B N     1 
ATOM   14144 C CA    . ILE B  1 740  ? 18.567  22.230  70.680  1.00 24.39 ? 738  ILE B CA    1 
ATOM   14145 C C     . ILE B  1 740  ? 18.142  23.374  69.774  1.00 23.16 ? 738  ILE B C     1 
ATOM   14146 O O     . ILE B  1 740  ? 16.978  23.449  69.366  1.00 22.78 ? 738  ILE B O     1 
ATOM   14147 C CB    . ILE B  1 740  ? 18.335  22.561  72.168  1.00 27.30 ? 738  ILE B CB    1 
ATOM   14148 C CG1   . ILE B  1 740  ? 16.843  22.825  72.420  1.00 25.36 ? 738  ILE B CG1   1 
ATOM   14149 C CG2   . ILE B  1 740  ? 19.146  23.770  72.589  1.00 26.42 ? 738  ILE B CG2   1 
ATOM   14150 C CD1   . ILE B  1 740  ? 15.978  21.570  72.318  1.00 29.73 ? 738  ILE B CD1   1 
ATOM   14151 N N     . ALA B  1 741  ? 19.073  24.267  69.424  1.00 25.19 ? 739  ALA B N     1 
ATOM   14152 C CA    . ALA B  1 741  ? 18.755  25.346  68.492  1.00 24.41 ? 739  ALA B CA    1 
ATOM   14153 C C     . ALA B  1 741  ? 18.414  24.803  67.111  1.00 23.04 ? 739  ALA B C     1 
ATOM   14154 O O     . ALA B  1 741  ? 17.453  25.266  66.469  1.00 23.70 ? 739  ALA B O     1 
ATOM   14155 C CB    . ALA B  1 741  ? 19.929  26.314  68.387  1.00 23.49 ? 739  ALA B CB    1 
ATOM   14156 N N     . ALA B  1 742  ? 19.190  23.821  66.634  1.00 22.72 ? 740  ALA B N     1 
ATOM   14157 C CA    . ALA B  1 742  ? 18.892  23.201  65.342  1.00 24.23 ? 740  ALA B CA    1 
ATOM   14158 C C     . ALA B  1 742  ? 17.508  22.558  65.349  1.00 28.52 ? 740  ALA B C     1 
ATOM   14159 O O     . ALA B  1 742  ? 16.778  22.619  64.349  1.00 25.62 ? 740  ALA B O     1 
ATOM   14160 C CB    . ALA B  1 742  ? 19.960  22.157  64.998  1.00 26.42 ? 740  ALA B CB    1 
ATOM   14161 N N     . GLU B  1 743  ? 17.146  21.913  66.462  1.00 24.83 ? 741  GLU B N     1 
ATOM   14162 C CA    . GLU B  1 743  ? 15.822  21.313  66.588  1.00 24.56 ? 741  GLU B CA    1 
ATOM   14163 C C     . GLU B  1 743  ? 14.741  22.382  66.582  1.00 24.74 ? 741  GLU B C     1 
ATOM   14164 O O     . GLU B  1 743  ? 13.692  22.208  65.945  1.00 24.57 ? 741  GLU B O     1 
ATOM   14165 C CB    . GLU B  1 743  ? 15.757  20.479  67.874  1.00 31.10 ? 741  GLU B CB    1 
ATOM   14166 C CG    . GLU B  1 743  ? 14.431  19.793  68.113  1.00 28.43 ? 741  GLU B CG    1 
ATOM   14167 C CD    . GLU B  1 743  ? 14.109  18.730  67.076  1.00 31.33 ? 741  GLU B CD    1 
ATOM   14168 O OE1   . GLU B  1 743  ? 15.009  18.336  66.278  1.00 30.14 ? 741  GLU B OE1   1 
ATOM   14169 O OE2   . GLU B  1 743  ? 12.943  18.286  67.061  1.00 31.41 ? 741  GLU B OE2   1 
ATOM   14170 N N     . GLY B  1 744  ? 14.995  23.502  67.270  1.00 21.94 ? 742  GLY B N     1 
ATOM   14171 C CA    . GLY B  1 744  ? 14.081  24.637  67.212  1.00 22.80 ? 742  GLY B CA    1 
ATOM   14172 C C     . GLY B  1 744  ? 13.843  25.143  65.798  1.00 22.44 ? 742  GLY B C     1 
ATOM   14173 O O     . GLY B  1 744  ? 12.703  25.454  65.430  1.00 24.17 ? 742  GLY B O     1 
ATOM   14174 N N     . VAL B  1 745  ? 14.912  25.224  64.984  1.00 22.30 ? 743  VAL B N     1 
ATOM   14175 C CA    . VAL B  1 745  ? 14.771  25.629  63.584  1.00 24.40 ? 743  VAL B CA    1 
ATOM   14176 C C     . VAL B  1 745  ? 14.005  24.574  62.779  1.00 26.61 ? 743  VAL B C     1 
ATOM   14177 O O     . VAL B  1 745  ? 13.149  24.918  61.943  1.00 23.33 ? 743  VAL B O     1 
ATOM   14178 C CB    . VAL B  1 745  ? 16.153  25.934  62.973  1.00 27.79 ? 743  VAL B CB    1 
ATOM   14179 C CG1   . VAL B  1 745  ? 16.083  26.112  61.434  1.00 24.49 ? 743  VAL B CG1   1 
ATOM   14180 C CG2   . VAL B  1 745  ? 16.744  27.196  63.626  1.00 23.78 ? 743  VAL B CG2   1 
ATOM   14181 N N     . ARG B  1 746  ? 14.289  23.281  63.002  1.00 22.55 ? 744  ARG B N     1 
ATOM   14182 C CA    . ARG B  1 746  ? 13.502  22.251  62.312  1.00 27.32 ? 744  ARG B CA    1 
ATOM   14183 C C     . ARG B  1 746  ? 12.011  22.444  62.544  1.00 25.22 ? 744  ARG B C     1 
ATOM   14184 O O     . ARG B  1 746  ? 11.204  22.308  61.618  1.00 23.23 ? 744  ARG B O     1 
ATOM   14185 C CB    . ARG B  1 746  ? 13.883  20.847  62.773  1.00 24.09 ? 744  ARG B CB    1 
ATOM   14186 C CG    . ARG B  1 746  ? 15.305  20.443  62.469  1.00 27.20 ? 744  ARG B CG    1 
ATOM   14187 C CD    . ARG B  1 746  ? 15.558  19.033  62.953  1.00 27.16 ? 744  ARG B CD    1 
ATOM   14188 N NE    . ARG B  1 746  ? 16.963  18.727  62.768  1.00 31.32 ? 744  ARG B NE    1 
ATOM   14189 C CZ    . ARG B  1 746  ? 17.858  18.666  63.737  1.00 28.94 ? 744  ARG B CZ    1 
ATOM   14190 N NH1   . ARG B  1 746  ? 17.502  18.702  65.016  1.00 26.33 ? 744  ARG B NH1   1 
ATOM   14191 N NH2   . ARG B  1 746  ? 19.144  18.560  63.415  1.00 28.29 ? 744  ARG B NH2   1 
ATOM   14192 N N     . ILE B  1 747  ? 11.629  22.718  63.791  1.00 21.35 ? 745  ILE B N     1 
ATOM   14193 C CA    . ILE B  1 747  ? 10.221  22.847  64.146  1.00 23.53 ? 745  ILE B CA    1 
ATOM   14194 C C     . ILE B  1 747  ? 9.606   24.090  63.508  1.00 24.19 ? 745  ILE B C     1 
ATOM   14195 O O     . ILE B  1 747  ? 8.484   24.051  62.982  1.00 21.46 ? 745  ILE B O     1 
ATOM   14196 C CB    . ILE B  1 747  ? 10.097  22.868  65.682  1.00 22.30 ? 745  ILE B CB    1 
ATOM   14197 C CG1   . ILE B  1 747  ? 10.483  21.484  66.235  1.00 23.61 ? 745  ILE B CG1   1 
ATOM   14198 C CG2   . ILE B  1 747  ? 8.690   23.320  66.116  1.00 23.76 ? 745  ILE B CG2   1 
ATOM   14199 C CD1   . ILE B  1 747  ? 10.241  21.311  67.714  1.00 23.41 ? 745  ILE B CD1   1 
ATOM   14200 N N     . LEU B  1 748  ? 10.323  25.213  63.550  1.00 22.94 ? 746  LEU B N     1 
ATOM   14201 C CA    . LEU B  1 748  ? 9.817   26.439  62.946  1.00 21.62 ? 746  LEU B CA    1 
ATOM   14202 C C     . LEU B  1 748  ? 9.669   26.293  61.436  1.00 21.52 ? 746  LEU B C     1 
ATOM   14203 O O     . LEU B  1 748  ? 8.694   26.773  60.844  1.00 20.63 ? 746  LEU B O     1 
ATOM   14204 C CB    . LEU B  1 748  ? 10.739  27.607  63.314  1.00 20.71 ? 746  LEU B CB    1 
ATOM   14205 C CG    . LEU B  1 748  ? 10.389  28.215  64.677  1.00 24.82 ? 746  LEU B CG    1 
ATOM   14206 C CD1   . LEU B  1 748  ? 11.494  29.175  65.167  1.00 21.99 ? 746  LEU B CD1   1 
ATOM   14207 C CD2   . LEU B  1 748  ? 9.090   28.928  64.547  1.00 25.14 ? 746  LEU B CD2   1 
ATOM   14208 N N     . ARG B  1 749  ? 10.588  25.580  60.797  1.00 21.57 ? 747  ARG B N     1 
ATOM   14209 C CA    . ARG B  1 749  ? 10.438  25.355  59.361  1.00 22.30 ? 747  ARG B CA    1 
ATOM   14210 C C     . ARG B  1 749  ? 9.290   24.398  59.066  1.00 22.91 ? 747  ARG B C     1 
ATOM   14211 O O     . ARG B  1 749  ? 8.523   24.609  58.114  1.00 24.47 ? 747  ARG B O     1 
ATOM   14212 C CB    . ARG B  1 749  ? 11.743  24.820  58.779  1.00 25.01 ? 747  ARG B CB    1 
ATOM   14213 C CG    . ARG B  1 749  ? 12.858  25.853  58.667  1.00 26.56 ? 747  ARG B CG    1 
ATOM   14214 C CD    . ARG B  1 749  ? 13.986  25.283  57.810  1.00 31.83 ? 747  ARG B CD    1 
ATOM   14215 N NE    . ARG B  1 749  ? 15.069  26.227  57.575  1.00 29.53 ? 747  ARG B NE    1 
ATOM   14216 C CZ    . ARG B  1 749  ? 16.123  25.962  56.812  1.00 35.51 ? 747  ARG B CZ    1 
ATOM   14217 N NH1   . ARG B  1 749  ? 16.266  24.792  56.212  1.00 35.78 ? 747  ARG B NH1   1 
ATOM   14218 N NH2   . ARG B  1 749  ? 17.067  26.888  56.658  1.00 36.40 ? 747  ARG B NH2   1 
ATOM   14219 N N     . GLU B  1 750  ? 9.164   23.336  59.862  1.00 22.39 ? 748  GLU B N     1 
ATOM   14220 C CA    . GLU B  1 750  ? 8.059   22.397  59.665  1.00 24.15 ? 748  GLU B CA    1 
ATOM   14221 C C     . GLU B  1 750  ? 6.712   23.087  59.834  1.00 22.18 ? 748  GLU B C     1 
ATOM   14222 O O     . GLU B  1 750  ? 5.745   22.741  59.151  1.00 23.43 ? 748  GLU B O     1 
ATOM   14223 C CB    . GLU B  1 750  ? 8.196   21.218  60.634  1.00 25.79 ? 748  GLU B CB    1 
ATOM   14224 C CG    . GLU B  1 750  ? 7.118   20.128  60.499  1.00 29.26 ? 748  GLU B CG    1 
ATOM   14225 C CD    . GLU B  1 750  ? 7.342   18.967  61.475  1.00 34.40 ? 748  GLU B CD    1 
ATOM   14226 O OE1   . GLU B  1 750  ? 8.440   18.897  62.089  1.00 30.30 ? 748  GLU B OE1   1 
ATOM   14227 O OE2   . GLU B  1 750  ? 6.421   18.134  61.633  1.00 33.01 ? 748  GLU B OE2   1 
ATOM   14228 N N     . ALA B  1 751  ? 6.635   24.072  60.730  1.00 21.39 ? 749  ALA B N     1 
ATOM   14229 C CA    . ALA B  1 751  ? 5.425   24.839  60.969  1.00 21.66 ? 749  ALA B CA    1 
ATOM   14230 C C     . ALA B  1 751  ? 5.113   25.841  59.870  1.00 23.17 ? 749  ALA B C     1 
ATOM   14231 O O     . ALA B  1 751  ? 4.019   26.412  59.875  1.00 23.61 ? 749  ALA B O     1 
ATOM   14232 C CB    . ALA B  1 751  ? 5.533   25.595  62.292  1.00 20.19 ? 749  ALA B CB    1 
ATOM   14233 N N     . GLY B  1 752  ? 6.034   26.091  58.945  1.00 24.08 ? 750  GLY B N     1 
ATOM   14234 C CA    . GLY B  1 752  ? 5.710   26.987  57.853  1.00 23.72 ? 750  GLY B CA    1 
ATOM   14235 C C     . GLY B  1 752  ? 6.728   28.072  57.558  1.00 26.08 ? 750  GLY B C     1 
ATOM   14236 O O     . GLY B  1 752  ? 6.621   28.747  56.532  1.00 22.29 ? 750  GLY B O     1 
ATOM   14237 N N     . ILE B  1 753  ? 7.721   28.258  58.421  1.00 25.37 ? 751  ILE B N     1 
ATOM   14238 C CA    . ILE B  1 753  ? 8.718   29.296  58.159  1.00 26.58 ? 751  ILE B CA    1 
ATOM   14239 C C     . ILE B  1 753  ? 9.598   28.852  56.995  1.00 24.70 ? 751  ILE B C     1 
ATOM   14240 O O     . ILE B  1 753  ? 10.261  27.801  57.076  1.00 26.24 ? 751  ILE B O     1 
ATOM   14241 C CB    . ILE B  1 753  ? 9.569   29.608  59.394  1.00 25.50 ? 751  ILE B CB    1 
ATOM   14242 C CG1   . ILE B  1 753  ? 8.693   30.024  60.586  1.00 27.64 ? 751  ILE B CG1   1 
ATOM   14243 C CG2   . ILE B  1 753  ? 10.586  30.681  59.023  1.00 26.36 ? 751  ILE B CG2   1 
ATOM   14244 C CD1   . ILE B  1 753  ? 7.803   31.225  60.340  1.00 24.56 ? 751  ILE B CD1   1 
ATOM   14245 N N     . PRO B  1 754  ? 9.658   29.625  55.911  1.00 23.96 ? 752  PRO B N     1 
ATOM   14246 C CA    . PRO B  1 754  ? 10.433  29.200  54.741  1.00 24.86 ? 752  PRO B CA    1 
ATOM   14247 C C     . PRO B  1 754  ? 11.926  29.176  55.032  1.00 27.86 ? 752  PRO B C     1 
ATOM   14248 O O     . PRO B  1 754  ? 12.431  29.915  55.876  1.00 25.93 ? 752  PRO B O     1 
ATOM   14249 C CB    . PRO B  1 754  ? 10.093  30.258  53.680  1.00 29.17 ? 752  PRO B CB    1 
ATOM   14250 C CG    . PRO B  1 754  ? 8.855   30.943  54.171  1.00 31.21 ? 752  PRO B CG    1 
ATOM   14251 C CD    . PRO B  1 754  ? 8.904   30.866  55.668  1.00 24.62 ? 752  PRO B CD    1 
ATOM   14252 N N     . ALA B  1 755  ? 12.627  28.304  54.310  1.00 29.80 ? 753  ALA B N     1 
ATOM   14253 C CA    . ALA B  1 755  ? 14.063  28.136  54.517  1.00 29.94 ? 753  ALA B CA    1 
ATOM   14254 C C     . ALA B  1 755  ? 14.810  29.464  54.401  1.00 31.76 ? 753  ALA B C     1 
ATOM   14255 O O     . ALA B  1 755  ? 15.713  29.750  55.192  1.00 28.53 ? 753  ALA B O     1 
ATOM   14256 C CB    . ALA B  1 755  ? 14.607  27.116  53.519  1.00 36.31 ? 753  ALA B CB    1 
ATOM   14257 N N     . SER B  1 756  ? 14.423  30.311  53.448  1.00 29.38 ? 754  SER B N     1 
ATOM   14258 C CA    . SER B  1 756  ? 15.128  31.579  53.285  1.00 27.55 ? 754  SER B CA    1 
ATOM   14259 C C     . SER B  1 756  ? 14.804  32.577  54.388  1.00 28.69 ? 754  SER B C     1 
ATOM   14260 O O     . SER B  1 756  ? 15.574  33.517  54.597  1.00 30.23 ? 754  SER B O     1 
ATOM   14261 C CB    . SER B  1 756  ? 14.791  32.187  51.928  1.00 30.43 ? 754  SER B CB    1 
ATOM   14262 O OG    . SER B  1 756  ? 13.413  32.512  51.878  1.00 34.29 ? 754  SER B OG    1 
ATOM   14263 N N     . ALA B  1 757  ? 13.694  32.402  55.099  1.00 25.41 ? 755  ALA B N     1 
ATOM   14264 C CA    . ALA B  1 757  ? 13.374  33.314  56.188  1.00 24.12 ? 755  ALA B CA    1 
ATOM   14265 C C     . ALA B  1 757  ? 14.027  32.932  57.508  1.00 24.08 ? 755  ALA B C     1 
ATOM   14266 O O     . ALA B  1 757  ? 14.008  33.747  58.444  1.00 22.81 ? 755  ALA B O     1 
ATOM   14267 C CB    . ALA B  1 757  ? 11.854  33.395  56.394  1.00 26.51 ? 755  ALA B CB    1 
ATOM   14268 N N     . LEU B  1 758  ? 14.572  31.717  57.625  1.00 23.35 ? 756  LEU B N     1 
ATOM   14269 C CA    . LEU B  1 758  ? 15.125  31.249  58.899  1.00 25.60 ? 756  LEU B CA    1 
ATOM   14270 C C     . LEU B  1 758  ? 16.318  30.350  58.596  1.00 26.42 ? 756  LEU B C     1 
ATOM   14271 O O     . LEU B  1 758  ? 16.156  29.187  58.213  1.00 26.81 ? 756  LEU B O     1 
ATOM   14272 C CB    . LEU B  1 758  ? 14.087  30.520  59.738  1.00 22.23 ? 756  LEU B CB    1 
ATOM   14273 C CG    . LEU B  1 758  ? 14.581  29.936  61.068  1.00 27.68 ? 756  LEU B CG    1 
ATOM   14274 C CD1   . LEU B  1 758  ? 15.181  31.001  61.963  1.00 25.20 ? 756  LEU B CD1   1 
ATOM   14275 C CD2   . LEU B  1 758  ? 13.461  29.237  61.788  1.00 23.53 ? 756  LEU B CD2   1 
ATOM   14276 N N     . GLN B  1 759  ? 17.506  30.900  58.769  1.00 26.97 ? 757  GLN B N     1 
ATOM   14277 C CA    . GLN B  1 759  ? 18.740  30.175  58.537  1.00 23.24 ? 757  GLN B CA    1 
ATOM   14278 C C     . GLN B  1 759  ? 19.458  30.022  59.868  1.00 24.93 ? 757  GLN B C     1 
ATOM   14279 O O     . GLN B  1 759  ? 19.468  30.952  60.677  1.00 27.63 ? 757  GLN B O     1 
ATOM   14280 C CB    . GLN B  1 759  ? 19.601  30.914  57.529  1.00 26.94 ? 757  GLN B CB    1 
ATOM   14281 C CG    . GLN B  1 759  ? 18.948  30.984  56.160  1.00 24.63 ? 757  GLN B CG    1 
ATOM   14282 C CD    . GLN B  1 759  ? 19.733  31.815  55.205  1.00 25.14 ? 757  GLN B CD    1 
ATOM   14283 O OE1   . GLN B  1 759  ? 20.499  31.286  54.399  1.00 30.00 ? 757  GLN B OE1   1 
ATOM   14284 N NE2   . GLN B  1 759  ? 19.554  33.122  55.270  1.00 25.95 ? 757  GLN B NE2   1 
ATOM   14285 N N     . LEU B  1 760  ? 20.051  28.850  60.086  1.00 25.99 ? 758  LEU B N     1 
ATOM   14286 C CA    . LEU B  1 760  ? 20.775  28.548  61.315  1.00 26.45 ? 758  LEU B CA    1 
ATOM   14287 C C     . LEU B  1 760  ? 22.269  28.566  61.031  1.00 25.01 ? 758  LEU B C     1 
ATOM   14288 O O     . LEU B  1 760  ? 22.736  27.859  60.134  1.00 24.99 ? 758  LEU B O     1 
ATOM   14289 C CB    . LEU B  1 760  ? 20.367  27.185  61.874  1.00 24.25 ? 758  LEU B CB    1 
ATOM   14290 C CG    . LEU B  1 760  ? 21.088  26.774  63.149  1.00 25.15 ? 758  LEU B CG    1 
ATOM   14291 C CD1   . LEU B  1 760  ? 20.450  27.484  64.336  1.00 23.55 ? 758  LEU B CD1   1 
ATOM   14292 C CD2   . LEU B  1 760  ? 21.086  25.261  63.324  1.00 26.43 ? 758  LEU B CD2   1 
ATOM   14293 N N     . LEU B  1 761  ? 23.024  29.342  61.817  1.00 26.09 ? 759  LEU B N     1 
ATOM   14294 C CA    . LEU B  1 761  ? 24.474  29.484  61.633  1.00 28.05 ? 759  LEU B CA    1 
ATOM   14295 C C     . LEU B  1 761  ? 25.200  29.153  62.931  1.00 24.76 ? 759  LEU B C     1 
ATOM   14296 O O     . LEU B  1 761  ? 25.553  30.052  63.704  1.00 26.97 ? 759  LEU B O     1 
ATOM   14297 C CB    . LEU B  1 761  ? 24.852  30.895  61.175  1.00 31.03 ? 759  LEU B CB    1 
ATOM   14298 C CG    . LEU B  1 761  ? 24.324  31.453  59.849  1.00 27.47 ? 759  LEU B CG    1 
ATOM   14299 C CD1   . LEU B  1 761  ? 24.505  30.432  58.725  1.00 30.98 ? 759  LEU B CD1   1 
ATOM   14300 C CD2   . LEU B  1 761  ? 22.892  31.915  59.966  1.00 28.45 ? 759  LEU B CD2   1 
ATOM   14301 N N     . PRO B  1 762  ? 25.465  27.880  63.188  1.00 28.01 ? 760  PRO B N     1 
ATOM   14302 C CA    . PRO B  1 762  ? 26.218  27.517  64.395  1.00 28.23 ? 760  PRO B CA    1 
ATOM   14303 C C     . PRO B  1 762  ? 27.651  28.031  64.344  1.00 28.64 ? 760  PRO B C     1 
ATOM   14304 O O     . PRO B  1 762  ? 28.256  28.156  63.279  1.00 25.81 ? 760  PRO B O     1 
ATOM   14305 C CB    . PRO B  1 762  ? 26.183  25.981  64.390  1.00 30.98 ? 760  PRO B CB    1 
ATOM   14306 C CG    . PRO B  1 762  ? 25.039  25.610  63.441  1.00 27.35 ? 760  PRO B CG    1 
ATOM   14307 C CD    . PRO B  1 762  ? 25.080  26.698  62.400  1.00 25.08 ? 760  PRO B CD    1 
ATOM   14308 N N     . GLY B  1 763  ? 28.195  28.335  65.519  1.00 29.96 ? 761  GLY B N     1 
ATOM   14309 C CA    . GLY B  1 763  ? 29.602  28.669  65.621  1.00 29.81 ? 761  GLY B CA    1 
ATOM   14310 C C     . GLY B  1 763  ? 29.867  29.588  66.796  1.00 30.51 ? 761  GLY B C     1 
ATOM   14311 O O     . GLY B  1 763  ? 29.027  29.765  67.679  1.00 30.74 ? 761  GLY B O     1 
ATOM   14312 N N     . ASP B  1 764  ? 31.065  30.169  66.787  1.00 36.40 ? 762  ASP B N     1 
ATOM   14313 C CA    . ASP B  1 764  ? 31.526  30.984  67.895  1.00 38.28 ? 762  ASP B CA    1 
ATOM   14314 C C     . ASP B  1 764  ? 31.276  32.463  67.607  1.00 37.53 ? 762  ASP B C     1 
ATOM   14315 O O     . ASP B  1 764  ? 30.512  32.831  66.704  1.00 31.90 ? 762  ASP B O     1 
ATOM   14316 C CB    . ASP B  1 764  ? 33.005  30.688  68.196  1.00 37.59 ? 762  ASP B CB    1 
ATOM   14317 C CG    . ASP B  1 764  ? 33.941  31.026  67.040  1.00 41.98 ? 762  ASP B CG    1 
ATOM   14318 O OD1   . ASP B  1 764  ? 33.543  31.730  66.089  1.00 41.73 ? 762  ASP B OD1   1 
ATOM   14319 O OD2   . ASP B  1 764  ? 35.108  30.568  67.080  1.00 48.69 ? 762  ASP B OD2   1 
ATOM   14320 N N     . GLY B  1 765  ? 31.929  33.325  68.392  1.00 35.36 ? 763  GLY B N     1 
ATOM   14321 C CA    . GLY B  1 765  ? 31.717  34.756  68.285  1.00 32.66 ? 763  GLY B CA    1 
ATOM   14322 C C     . GLY B  1 765  ? 32.199  35.355  66.986  1.00 33.04 ? 763  GLY B C     1 
ATOM   14323 O O     . GLY B  1 765  ? 31.732  36.432  66.610  1.00 35.79 ? 763  GLY B O     1 
ATOM   14324 N N     . ARG B  1 766  ? 33.129  34.687  66.294  1.00 30.13 ? 764  ARG B N     1 
ATOM   14325 C CA    . ARG B  1 766  ? 33.502  35.117  64.951  1.00 34.90 ? 764  ARG B CA    1 
ATOM   14326 C C     . ARG B  1 766  ? 32.338  34.984  63.974  1.00 33.34 ? 764  ARG B C     1 
ATOM   14327 O O     . ARG B  1 766  ? 32.212  35.790  63.041  1.00 33.04 ? 764  ARG B O     1 
ATOM   14328 C CB    . ARG B  1 766  ? 34.694  34.308  64.449  1.00 33.98 ? 764  ARG B CB    1 
ATOM   14329 N N     . VAL B  1 767  ? 31.498  33.962  64.152  1.00 35.80 ? 765  VAL B N     1 
ATOM   14330 C CA    . VAL B  1 767  ? 30.310  33.829  63.312  1.00 33.18 ? 765  VAL B CA    1 
ATOM   14331 C C     . VAL B  1 767  ? 29.316  34.941  63.627  1.00 30.71 ? 765  VAL B C     1 
ATOM   14332 O O     . VAL B  1 767  ? 28.807  35.619  62.725  1.00 32.49 ? 765  VAL B O     1 
ATOM   14333 C CB    . VAL B  1 767  ? 29.685  32.432  63.488  1.00 30.63 ? 765  VAL B CB    1 
ATOM   14334 C CG1   . VAL B  1 767  ? 28.363  32.317  62.690  1.00 28.87 ? 765  VAL B CG1   1 
ATOM   14335 C CG2   . VAL B  1 767  ? 30.673  31.352  63.026  1.00 29.96 ? 765  VAL B CG2   1 
ATOM   14336 N N     . GLY B  1 768  ? 29.026  35.148  64.910  1.00 29.41 ? 766  GLY B N     1 
ATOM   14337 C CA    . GLY B  1 768  ? 28.167  36.260  65.285  1.00 30.08 ? 766  GLY B CA    1 
ATOM   14338 C C     . GLY B  1 768  ? 28.675  37.591  64.761  1.00 29.23 ? 766  GLY B C     1 
ATOM   14339 O O     . GLY B  1 768  ? 27.906  38.397  64.234  1.00 30.44 ? 766  GLY B O     1 
ATOM   14340 N N     . ALA B  1 769  ? 29.980  37.836  64.892  1.00 31.35 ? 767  ALA B N     1 
ATOM   14341 C CA    . ALA B  1 769  ? 30.536  39.118  64.471  1.00 31.48 ? 767  ALA B CA    1 
ATOM   14342 C C     . ALA B  1 769  ? 30.398  39.307  62.968  1.00 32.19 ? 767  ALA B C     1 
ATOM   14343 O O     . ALA B  1 769  ? 30.027  40.393  62.505  1.00 31.85 ? 767  ALA B O     1 
ATOM   14344 C CB    . ALA B  1 769  ? 32.010  39.216  64.893  1.00 32.07 ? 767  ALA B CB    1 
ATOM   14345 N N     . ALA B  1 770  ? 30.690  38.253  62.195  1.00 27.93 ? 768  ALA B N     1 
ATOM   14346 C CA    . ALA B  1 770  ? 30.489  38.303  60.752  1.00 31.69 ? 768  ALA B CA    1 
ATOM   14347 C C     . ALA B  1 770  ? 29.038  38.605  60.398  1.00 31.81 ? 768  ALA B C     1 
ATOM   14348 O O     . ALA B  1 770  ? 28.767  39.351  59.451  1.00 30.37 ? 768  ALA B O     1 
ATOM   14349 C CB    . ALA B  1 770  ? 30.936  36.987  60.112  1.00 31.55 ? 768  ALA B CB    1 
ATOM   14350 N N     . LEU B  1 771  ? 28.083  38.024  61.131  1.00 29.40 ? 769  LEU B N     1 
ATOM   14351 C CA    . LEU B  1 771  ? 26.684  38.304  60.835  1.00 28.72 ? 769  LEU B CA    1 
ATOM   14352 C C     . LEU B  1 771  ? 26.359  39.762  61.129  1.00 28.73 ? 769  LEU B C     1 
ATOM   14353 O O     . LEU B  1 771  ? 25.753  40.451  60.304  1.00 31.83 ? 769  LEU B O     1 
ATOM   14354 C CB    . LEU B  1 771  ? 25.758  37.371  61.631  1.00 26.51 ? 769  LEU B CB    1 
ATOM   14355 C CG    . LEU B  1 771  ? 25.805  35.881  61.259  1.00 26.57 ? 769  LEU B CG    1 
ATOM   14356 C CD1   . LEU B  1 771  ? 25.012  35.035  62.244  1.00 28.61 ? 769  LEU B CD1   1 
ATOM   14357 C CD2   . LEU B  1 771  ? 25.293  35.656  59.839  1.00 26.39 ? 769  LEU B CD2   1 
ATOM   14358 N N     . VAL B  1 772  ? 26.755  40.243  62.309  1.00 27.39 ? 770  VAL B N     1 
ATOM   14359 C CA    . VAL B  1 772  ? 26.448  41.612  62.717  1.00 30.98 ? 770  VAL B CA    1 
ATOM   14360 C C     . VAL B  1 772  ? 27.018  42.622  61.728  1.00 31.63 ? 770  VAL B C     1 
ATOM   14361 O O     . VAL B  1 772  ? 26.393  43.652  61.445  1.00 32.22 ? 770  VAL B O     1 
ATOM   14362 C CB    . VAL B  1 772  ? 26.968  41.859  64.143  1.00 28.99 ? 770  VAL B CB    1 
ATOM   14363 C CG1   . VAL B  1 772  ? 26.980  43.362  64.462  1.00 31.39 ? 770  VAL B CG1   1 
ATOM   14364 C CG2   . VAL B  1 772  ? 26.083  41.102  65.147  1.00 28.61 ? 770  VAL B CG2   1 
ATOM   14365 N N     . ALA B  1 773  ? 28.205  42.345  61.188  1.00 33.31 ? 771  ALA B N     1 
ATOM   14366 C CA    . ALA B  1 773  ? 28.895  43.297  60.323  1.00 33.61 ? 771  ALA B CA    1 
ATOM   14367 C C     . ALA B  1 773  ? 28.421  43.250  58.873  1.00 38.69 ? 771  ALA B C     1 
ATOM   14368 O O     . ALA B  1 773  ? 28.751  44.159  58.107  1.00 40.79 ? 771  ALA B O     1 
ATOM   14369 C CB    . ALA B  1 773  ? 30.405  43.056  60.382  1.00 36.67 ? 771  ALA B CB    1 
ATOM   14370 N N     . ALA B  1 774  ? 27.654  42.232  58.485  1.00 35.69 ? 772  ALA B N     1 
ATOM   14371 C CA    . ALA B  1 774  ? 27.188  42.116  57.108  1.00 38.25 ? 772  ALA B CA    1 
ATOM   14372 C C     . ALA B  1 774  ? 26.377  43.340  56.691  1.00 38.30 ? 772  ALA B C     1 
ATOM   14373 O O     . ALA B  1 774  ? 25.618  43.910  57.479  1.00 36.81 ? 772  ALA B O     1 
ATOM   14374 C CB    . ALA B  1 774  ? 26.344  40.848  56.936  1.00 38.19 ? 772  ALA B CB    1 
ATOM   14375 N N     . ALA B  1 775  ? 26.528  43.722  55.420  1.00 40.09 ? 773  ALA B N     1 
ATOM   14376 C CA    . ALA B  1 775  ? 25.938  44.966  54.935  1.00 42.01 ? 773  ALA B CA    1 
ATOM   14377 C C     . ALA B  1 775  ? 24.414  44.963  55.046  1.00 38.97 ? 773  ALA B C     1 
ATOM   14378 O O     . ALA B  1 775  ? 23.807  45.984  55.398  1.00 39.18 ? 773  ALA B O     1 
ATOM   14379 C CB    . ALA B  1 775  ? 26.387  45.211  53.491  1.00 37.37 ? 773  ALA B CB    1 
ATOM   14380 N N     . GLU B  1 776  ? 23.775  43.823  54.784  1.00 36.54 ? 774  GLU B N     1 
ATOM   14381 C CA    . GLU B  1 776  ? 22.315  43.755  54.720  1.00 34.59 ? 774  GLU B CA    1 
ATOM   14382 C C     . GLU B  1 776  ? 21.653  43.513  56.079  1.00 32.75 ? 774  GLU B C     1 
ATOM   14383 O O     . GLU B  1 776  ? 20.420  43.421  56.152  1.00 32.34 ? 774  GLU B O     1 
ATOM   14384 C CB    . GLU B  1 776  ? 21.901  42.663  53.726  1.00 34.49 ? 774  GLU B CB    1 
ATOM   14385 C CG    . GLU B  1 776  ? 22.526  42.823  52.337  1.00 40.47 ? 774  GLU B CG    1 
ATOM   14386 C CD    . GLU B  1 776  ? 23.849  42.062  52.157  1.00 43.89 ? 774  GLU B CD    1 
ATOM   14387 O OE1   . GLU B  1 776  ? 24.432  41.575  53.156  1.00 42.76 ? 774  GLU B OE1   1 
ATOM   14388 O OE2   . GLU B  1 776  ? 24.315  41.961  50.999  1.00 46.56 ? 774  GLU B OE2   1 
ATOM   14389 N N     . THR B  1 777  ? 22.427  43.427  57.153  1.00 31.14 ? 775  THR B N     1 
ATOM   14390 C CA    . THR B  1 777  ? 21.858  43.238  58.483  1.00 29.61 ? 775  THR B CA    1 
ATOM   14391 C C     . THR B  1 777  ? 21.122  44.501  58.922  1.00 31.72 ? 775  THR B C     1 
ATOM   14392 O O     . THR B  1 777  ? 21.695  45.595  58.924  1.00 33.05 ? 775  THR B O     1 
ATOM   14393 C CB    . THR B  1 777  ? 22.962  42.881  59.469  1.00 29.17 ? 775  THR B CB    1 
ATOM   14394 O OG1   . THR B  1 777  ? 23.467  41.577  59.154  1.00 31.83 ? 775  THR B OG1   1 
ATOM   14395 C CG2   . THR B  1 777  ? 22.444  42.882  60.901  1.00 26.31 ? 775  THR B CG2   1 
ATOM   14396 N N     . ALA B  1 778  ? 19.848  44.350  59.282  1.00 29.12 ? 776  ALA B N     1 
ATOM   14397 C CA    . ALA B  1 778  ? 18.960  45.477  59.547  1.00 27.82 ? 776  ALA B CA    1 
ATOM   14398 C C     . ALA B  1 778  ? 18.607  45.603  61.021  1.00 26.45 ? 776  ALA B C     1 
ATOM   14399 O O     . ALA B  1 778  ? 17.927  46.557  61.406  1.00 28.14 ? 776  ALA B O     1 
ATOM   14400 C CB    . ALA B  1 778  ? 17.679  45.346  58.720  1.00 29.02 ? 776  ALA B CB    1 
ATOM   14401 N N     . GLY B  1 779  ? 19.058  44.674  61.845  1.00 26.69 ? 777  GLY B N     1 
ATOM   14402 C CA    . GLY B  1 779  ? 18.744  44.692  63.258  1.00 25.76 ? 777  GLY B CA    1 
ATOM   14403 C C     . GLY B  1 779  ? 19.418  43.501  63.904  1.00 24.58 ? 777  GLY B C     1 
ATOM   14404 O O     . GLY B  1 779  ? 19.742  42.507  63.249  1.00 24.99 ? 777  GLY B O     1 
ATOM   14405 N N     . VAL B  1 780  ? 19.617  43.611  65.207  1.00 23.78 ? 778  VAL B N     1 
ATOM   14406 C CA    . VAL B  1 780  ? 20.299  42.562  65.944  1.00 24.48 ? 778  VAL B CA    1 
ATOM   14407 C C     . VAL B  1 780  ? 19.576  42.379  67.256  1.00 21.64 ? 778  VAL B C     1 
ATOM   14408 O O     . VAL B  1 780  ? 19.239  43.364  67.923  1.00 23.60 ? 778  VAL B O     1 
ATOM   14409 C CB    . VAL B  1 780  ? 21.787  42.881  66.204  1.00 23.85 ? 778  VAL B CB    1 
ATOM   14410 C CG1   . VAL B  1 780  ? 22.391  41.812  67.081  1.00 23.67 ? 778  VAL B CG1   1 
ATOM   14411 C CG2   . VAL B  1 780  ? 22.571  42.978  64.893  1.00 24.52 ? 778  VAL B CG2   1 
ATOM   14412 N N     . MET B  1 781  ? 19.323  41.125  67.615  1.00 21.90 ? 779  MET B N     1 
ATOM   14413 C CA    . MET B  1 781  ? 18.729  40.767  68.900  1.00 23.56 ? 779  MET B CA    1 
ATOM   14414 C C     . MET B  1 781  ? 19.746  39.903  69.624  1.00 25.44 ? 779  MET B C     1 
ATOM   14415 O O     . MET B  1 781  ? 20.168  38.871  69.096  1.00 25.21 ? 779  MET B O     1 
ATOM   14416 C CB    . MET B  1 781  ? 17.406  40.030  68.695  1.00 22.58 ? 779  MET B CB    1 
ATOM   14417 C CG    . MET B  1 781  ? 16.436  40.849  67.891  1.00 23.71 ? 779  MET B CG    1 
ATOM   14418 S SD    . MET B  1 781  ? 14.955  39.925  67.513  1.00 26.81 ? 779  MET B SD    1 
ATOM   14419 C CE    . MET B  1 781  ? 14.236  39.798  69.144  1.00 25.25 ? 779  MET B CE    1 
ATOM   14420 N N     . PHE B  1 782  ? 20.179  40.347  70.797  1.00 24.74 ? 780  PHE B N     1 
ATOM   14421 C CA    . PHE B  1 782  ? 21.312  39.738  71.478  1.00 21.40 ? 780  PHE B CA    1 
ATOM   14422 C C     . PHE B  1 782  ? 20.986  39.528  72.948  1.00 25.11 ? 780  PHE B C     1 
ATOM   14423 O O     . PHE B  1 782  ? 20.488  40.440  73.605  1.00 26.41 ? 780  PHE B O     1 
ATOM   14424 C CB    . PHE B  1 782  ? 22.555  40.623  71.385  1.00 24.57 ? 780  PHE B CB    1 
ATOM   14425 C CG    . PHE B  1 782  ? 23.691  40.133  72.237  1.00 24.81 ? 780  PHE B CG    1 
ATOM   14426 C CD1   . PHE B  1 782  ? 24.473  39.069  71.810  1.00 24.41 ? 780  PHE B CD1   1 
ATOM   14427 C CD2   . PHE B  1 782  ? 23.933  40.682  73.488  1.00 25.73 ? 780  PHE B CD2   1 
ATOM   14428 C CE1   . PHE B  1 782  ? 25.504  38.585  72.591  1.00 26.98 ? 780  PHE B CE1   1 
ATOM   14429 C CE2   . PHE B  1 782  ? 24.977  40.198  74.280  1.00 24.11 ? 780  PHE B CE2   1 
ATOM   14430 C CZ    . PHE B  1 782  ? 25.762  39.157  73.829  1.00 27.69 ? 780  PHE B CZ    1 
ATOM   14431 N N     . THR B  1 783  ? 21.320  38.351  73.469  1.00 23.15 ? 781  THR B N     1 
ATOM   14432 C CA    . THR B  1 783  ? 21.186  38.060  74.888  1.00 25.09 ? 781  THR B CA    1 
ATOM   14433 C C     . THR B  1 783  ? 22.469  37.382  75.328  1.00 25.52 ? 781  THR B C     1 
ATOM   14434 O O     . THR B  1 783  ? 22.845  36.338  74.782  1.00 27.46 ? 781  THR B O     1 
ATOM   14435 C CB    . THR B  1 783  ? 19.950  37.187  75.183  1.00 24.47 ? 781  THR B CB    1 
ATOM   14436 O OG1   . THR B  1 783  ? 18.774  37.889  74.773  1.00 24.36 ? 781  THR B OG1   1 
ATOM   14437 C CG2   . THR B  1 783  ? 19.830  36.899  76.684  1.00 27.46 ? 781  THR B CG2   1 
ATOM   14438 N N     . GLY B  1 784  ? 23.174  38.007  76.268  1.00 25.28 ? 782  GLY B N     1 
ATOM   14439 C CA    . GLY B  1 784  ? 24.482  37.498  76.648  1.00 24.70 ? 782  GLY B CA    1 
ATOM   14440 C C     . GLY B  1 784  ? 25.226  38.533  77.471  1.00 26.53 ? 782  GLY B C     1 
ATOM   14441 O O     . GLY B  1 784  ? 24.613  39.353  78.155  1.00 25.58 ? 782  GLY B O     1 
ATOM   14442 N N     . SER B  1 785  ? 26.547  38.501  77.364  1.00 28.54 ? 783  SER B N     1 
ATOM   14443 C CA    . SER B  1 785  ? 27.391  39.303  78.239  1.00 30.42 ? 783  SER B CA    1 
ATOM   14444 C C     . SER B  1 785  ? 27.392  40.776  77.837  1.00 33.18 ? 783  SER B C     1 
ATOM   14445 O O     . SER B  1 785  ? 27.235  41.127  76.666  1.00 27.97 ? 783  SER B O     1 
ATOM   14446 C CB    . SER B  1 785  ? 28.816  38.779  78.229  1.00 30.53 ? 783  SER B CB    1 
ATOM   14447 O OG    . SER B  1 785  ? 29.431  39.071  76.995  1.00 32.78 ? 783  SER B OG    1 
ATOM   14448 N N     . THR B  1 786  ? 27.581  41.639  78.839  1.00 33.08 ? 784  THR B N     1 
ATOM   14449 C CA    . THR B  1 786  ? 27.713  43.071  78.592  1.00 33.33 ? 784  THR B CA    1 
ATOM   14450 C C     . THR B  1 786  ? 28.819  43.366  77.585  1.00 31.70 ? 784  THR B C     1 
ATOM   14451 O O     . THR B  1 786  ? 28.672  44.245  76.725  1.00 33.01 ? 784  THR B O     1 
ATOM   14452 C CB    . THR B  1 786  ? 27.996  43.798  79.912  1.00 34.04 ? 784  THR B CB    1 
ATOM   14453 O OG1   . THR B  1 786  ? 26.797  43.863  80.692  1.00 36.25 ? 784  THR B OG1   1 
ATOM   14454 C CG2   . THR B  1 786  ? 28.495  45.198  79.645  1.00 34.78 ? 784  THR B CG2   1 
ATOM   14455 N N     . GLU B  1 787  ? 29.932  42.634  77.670  1.00 32.05 ? 785  GLU B N     1 
ATOM   14456 C CA    . GLU B  1 787  ? 31.094  42.943  76.846  1.00 32.99 ? 785  GLU B CA    1 
ATOM   14457 C C     . GLU B  1 787  ? 30.817  42.694  75.365  1.00 32.48 ? 785  GLU B C     1 
ATOM   14458 O O     . GLU B  1 787  ? 31.177  43.516  74.517  1.00 31.66 ? 785  GLU B O     1 
ATOM   14459 C CB    . GLU B  1 787  ? 32.299  42.124  77.319  1.00 36.60 ? 785  GLU B CB    1 
ATOM   14460 N N     . VAL B  1 788  ? 30.180  41.567  75.030  1.00 28.24 ? 786  VAL B N     1 
ATOM   14461 C CA    . VAL B  1 788  ? 29.846  41.306  73.629  1.00 28.67 ? 786  VAL B CA    1 
ATOM   14462 C C     . VAL B  1 788  ? 28.791  42.293  73.135  1.00 25.27 ? 786  VAL B C     1 
ATOM   14463 O O     . VAL B  1 788  ? 28.839  42.750  71.989  1.00 31.37 ? 786  VAL B O     1 
ATOM   14464 C CB    . VAL B  1 788  ? 29.389  39.846  73.455  1.00 30.19 ? 786  VAL B CB    1 
ATOM   14465 C CG1   . VAL B  1 788  ? 28.823  39.607  72.047  1.00 28.89 ? 786  VAL B CG1   1 
ATOM   14466 C CG2   . VAL B  1 788  ? 30.535  38.897  73.745  1.00 33.52 ? 786  VAL B CG2   1 
ATOM   14467 N N     . ALA B  1 789  ? 27.829  42.643  73.985  1.00 28.26 ? 787  ALA B N     1 
ATOM   14468 C CA    . ALA B  1 789  ? 26.804  43.600  73.577  1.00 28.69 ? 787  ALA B CA    1 
ATOM   14469 C C     . ALA B  1 789  ? 27.416  44.937  73.181  1.00 28.63 ? 787  ALA B C     1 
ATOM   14470 O O     . ALA B  1 789  ? 26.971  45.575  72.218  1.00 26.62 ? 787  ALA B O     1 
ATOM   14471 C CB    . ALA B  1 789  ? 25.786  43.799  74.695  1.00 29.24 ? 787  ALA B CB    1 
ATOM   14472 N N     . ARG B  1 790  ? 28.420  45.394  73.933  1.00 28.33 ? 788  ARG B N     1 
ATOM   14473 C CA    . ARG B  1 790  ? 29.095  46.638  73.577  1.00 27.50 ? 788  ARG B CA    1 
ATOM   14474 C C     . ARG B  1 790  ? 29.858  46.490  72.268  1.00 27.34 ? 788  ARG B C     1 
ATOM   14475 O O     . ARG B  1 790  ? 29.917  47.425  71.463  1.00 31.11 ? 788  ARG B O     1 
ATOM   14476 C CB    . ARG B  1 790  ? 30.029  47.067  74.713  1.00 33.66 ? 788  ARG B CB    1 
ATOM   14477 N N     . LEU B  1 791  ? 30.449  45.321  72.027  1.00 27.00 ? 789  LEU B N     1 
ATOM   14478 C CA    . LEU B  1 791  ? 31.137  45.118  70.759  1.00 29.98 ? 789  LEU B CA    1 
ATOM   14479 C C     . LEU B  1 791  ? 30.158  45.183  69.595  1.00 32.10 ? 789  LEU B C     1 
ATOM   14480 O O     . LEU B  1 791  ? 30.450  45.787  68.558  1.00 29.92 ? 789  LEU B O     1 
ATOM   14481 C CB    . LEU B  1 791  ? 31.859  43.777  70.756  1.00 30.00 ? 789  LEU B CB    1 
ATOM   14482 C CG    . LEU B  1 791  ? 33.047  43.666  71.713  1.00 34.29 ? 789  LEU B CG    1 
ATOM   14483 C CD1   . LEU B  1 791  ? 33.590  42.259  71.680  1.00 35.17 ? 789  LEU B CD1   1 
ATOM   14484 C CD2   . LEU B  1 791  ? 34.141  44.669  71.368  1.00 37.57 ? 789  LEU B CD2   1 
ATOM   14485 N N     . ILE B  1 792  ? 29.004  44.532  69.745  1.00 28.21 ? 790  ILE B N     1 
ATOM   14486 C CA    . ILE B  1 792  ? 27.980  44.555  68.703  1.00 27.54 ? 790  ILE B CA    1 
ATOM   14487 C C     . ILE B  1 792  ? 27.512  45.982  68.459  1.00 30.35 ? 790  ILE B C     1 
ATOM   14488 O O     . ILE B  1 792  ? 27.396  46.435  67.312  1.00 32.18 ? 790  ILE B O     1 
ATOM   14489 C CB    . ILE B  1 792  ? 26.808  43.638  69.100  1.00 26.82 ? 790  ILE B CB    1 
ATOM   14490 C CG1   . ILE B  1 792  ? 27.269  42.179  69.090  1.00 27.94 ? 790  ILE B CG1   1 
ATOM   14491 C CG2   . ILE B  1 792  ? 25.609  43.855  68.164  1.00 27.72 ? 790  ILE B CG2   1 
ATOM   14492 C CD1   . ILE B  1 792  ? 26.292  41.214  69.731  1.00 28.50 ? 790  ILE B CD1   1 
ATOM   14493 N N     . GLN B  1 793  ? 27.233  46.706  69.543  1.00 27.17 ? 791  GLN B N     1 
ATOM   14494 C CA    . GLN B  1 793  ? 26.781  48.086  69.440  1.00 29.14 ? 791  GLN B CA    1 
ATOM   14495 C C     . GLN B  1 793  ? 27.776  48.935  68.657  1.00 29.53 ? 791  GLN B C     1 
ATOM   14496 O O     . GLN B  1 793  ? 27.379  49.791  67.858  1.00 31.21 ? 791  GLN B O     1 
ATOM   14497 C CB    . GLN B  1 793  ? 26.562  48.646  70.847  1.00 31.16 ? 791  GLN B CB    1 
ATOM   14498 C CG    . GLN B  1 793  ? 26.052  50.090  70.919  1.00 32.13 ? 791  GLN B CG    1 
ATOM   14499 C CD    . GLN B  1 793  ? 26.488  50.774  72.215  1.00 36.57 ? 791  GLN B CD    1 
ATOM   14500 O OE1   . GLN B  1 793  ? 27.567  50.485  72.753  1.00 35.30 ? 791  GLN B OE1   1 
ATOM   14501 N NE2   . GLN B  1 793  ? 25.649  51.666  72.729  1.00 34.88 ? 791  GLN B NE2   1 
ATOM   14502 N N     . ALA B  1 794  ? 29.077  48.679  68.837  1.00 30.68 ? 792  ALA B N     1 
ATOM   14503 C CA    . ALA B  1 794  ? 30.080  49.456  68.115  1.00 32.34 ? 792  ALA B CA    1 
ATOM   14504 C C     . ALA B  1 794  ? 30.122  49.086  66.635  1.00 35.41 ? 792  ALA B C     1 
ATOM   14505 O O     . ALA B  1 794  ? 30.232  49.974  65.780  1.00 37.14 ? 792  ALA B O     1 
ATOM   14506 C CB    . ALA B  1 794  ? 31.455  49.270  68.758  1.00 32.61 ? 792  ALA B CB    1 
ATOM   14507 N N     . GLN B  1 795  ? 30.077  47.785  66.306  1.00 34.38 ? 793  GLN B N     1 
ATOM   14508 C CA    . GLN B  1 795  ? 29.980  47.402  64.895  1.00 29.70 ? 793  GLN B CA    1 
ATOM   14509 C C     . GLN B  1 795  ? 28.772  48.064  64.238  1.00 32.30 ? 793  GLN B C     1 
ATOM   14510 O O     . GLN B  1 795  ? 28.853  48.535  63.096  1.00 32.45 ? 793  GLN B O     1 
ATOM   14511 C CB    . GLN B  1 795  ? 29.877  45.879  64.737  1.00 32.90 ? 793  GLN B CB    1 
ATOM   14512 C CG    . GLN B  1 795  ? 31.081  45.037  65.122  1.00 41.56 ? 793  GLN B CG    1 
ATOM   14513 C CD    . GLN B  1 795  ? 30.811  43.529  64.993  1.00 42.08 ? 793  GLN B CD    1 
ATOM   14514 O OE1   . GLN B  1 795  ? 30.968  42.942  63.915  1.00 41.46 ? 793  GLN B OE1   1 
ATOM   14515 N NE2   . GLN B  1 795  ? 30.398  42.902  66.097  1.00 39.31 ? 793  GLN B NE2   1 
ATOM   14516 N N     . LEU B  1 796  ? 27.634  48.108  64.945  1.00 31.24 ? 794  LEU B N     1 
ATOM   14517 C CA    . LEU B  1 796  ? 26.408  48.601  64.319  1.00 32.19 ? 794  LEU B CA    1 
ATOM   14518 C C     . LEU B  1 796  ? 26.446  50.109  64.119  1.00 34.54 ? 794  LEU B C     1 
ATOM   14519 O O     . LEU B  1 796  ? 25.868  50.616  63.151  1.00 34.82 ? 794  LEU B O     1 
ATOM   14520 C CB    . LEU B  1 796  ? 25.185  48.217  65.146  1.00 31.77 ? 794  LEU B CB    1 
ATOM   14521 C CG    . LEU B  1 796  ? 24.870  46.729  65.163  1.00 29.20 ? 794  LEU B CG    1 
ATOM   14522 C CD1   . LEU B  1 796  ? 23.664  46.448  66.073  1.00 27.87 ? 794  LEU B CD1   1 
ATOM   14523 C CD2   . LEU B  1 796  ? 24.638  46.240  63.743  1.00 30.94 ? 794  LEU B CD2   1 
ATOM   14524 N N     . ALA B  1 797  ? 27.134  50.832  65.004  1.00 30.99 ? 795  ALA B N     1 
ATOM   14525 C CA    . ALA B  1 797  ? 27.129  52.289  64.960  1.00 38.49 ? 795  ALA B CA    1 
ATOM   14526 C C     . ALA B  1 797  ? 27.892  52.849  63.770  1.00 37.49 ? 795  ALA B C     1 
ATOM   14527 O O     . ALA B  1 797  ? 27.718  54.023  63.448  1.00 39.93 ? 795  ALA B O     1 
ATOM   14528 C CB    . ALA B  1 797  ? 27.714  52.863  66.252  1.00 37.46 ? 795  ALA B CB    1 
ATOM   14529 N N     . ASP B  1 798  ? 28.742  52.060  63.120  1.00 37.16 ? 796  ASP B N     1 
ATOM   14530 C CA    . ASP B  1 798  ? 29.392  52.549  61.914  1.00 41.46 ? 796  ASP B CA    1 
ATOM   14531 C C     . ASP B  1 798  ? 28.489  52.487  60.689  1.00 43.88 ? 796  ASP B C     1 
ATOM   14532 O O     . ASP B  1 798  ? 28.827  53.078  59.659  1.00 43.35 ? 796  ASP B O     1 
ATOM   14533 C CB    . ASP B  1 798  ? 30.673  51.762  61.644  1.00 47.24 ? 796  ASP B CB    1 
ATOM   14534 C CG    . ASP B  1 798  ? 31.523  52.393  60.560  1.00 57.56 ? 796  ASP B CG    1 
ATOM   14535 O OD1   . ASP B  1 798  ? 31.646  53.639  60.556  1.00 61.25 ? 796  ASP B OD1   1 
ATOM   14536 O OD2   . ASP B  1 798  ? 32.066  51.648  59.714  1.00 62.34 ? 796  ASP B OD2   1 
ATOM   14537 N N     . ARG B  1 799  ? 27.358  51.797  60.772  1.00 42.15 ? 797  ARG B N     1 
ATOM   14538 C CA    . ARG B  1 799  ? 26.459  51.611  59.643  1.00 43.55 ? 797  ARG B CA    1 
ATOM   14539 C C     . ARG B  1 799  ? 25.149  52.349  59.897  1.00 39.35 ? 797  ARG B C     1 
ATOM   14540 O O     . ARG B  1 799  ? 24.797  52.664  61.037  1.00 38.67 ? 797  ARG B O     1 
ATOM   14541 C CB    . ARG B  1 799  ? 26.171  50.117  59.400  1.00 42.59 ? 797  ARG B CB    1 
ATOM   14542 C CG    . ARG B  1 799  ? 27.375  49.176  59.540  1.00 45.02 ? 797  ARG B CG    1 
ATOM   14543 C CD    . ARG B  1 799  ? 27.169  47.827  58.806  1.00 48.27 ? 797  ARG B CD    1 
ATOM   14544 N NE    . ARG B  1 799  ? 26.400  46.842  59.567  1.00 41.08 ? 797  ARG B NE    1 
ATOM   14545 C CZ    . ARG B  1 799  ? 25.108  46.599  59.384  1.00 42.43 ? 797  ARG B CZ    1 
ATOM   14546 N NH1   . ARG B  1 799  ? 24.416  47.208  58.433  1.00 43.92 ? 797  ARG B NH1   1 
ATOM   14547 N NH2   . ARG B  1 799  ? 24.494  45.720  60.172  1.00 42.59 ? 797  ARG B NH2   1 
ATOM   14548 N N     . LEU B  1 800  ? 24.427  52.631  58.818  1.00 36.17 ? 798  LEU B N     1 
ATOM   14549 C CA    . LEU B  1 800  ? 23.049  53.098  58.906  1.00 40.23 ? 798  LEU B CA    1 
ATOM   14550 C C     . LEU B  1 800  ? 22.158  52.184  58.076  1.00 39.91 ? 798  LEU B C     1 
ATOM   14551 O O     . LEU B  1 800  ? 22.629  51.475  57.185  1.00 42.58 ? 798  LEU B O     1 
ATOM   14552 C CB    . LEU B  1 800  ? 22.904  54.541  58.418  1.00 42.51 ? 798  LEU B CB    1 
ATOM   14553 C CG    . LEU B  1 800  ? 23.425  55.661  59.316  1.00 39.77 ? 798  LEU B CG    1 
ATOM   14554 C CD1   . LEU B  1 800  ? 23.196  57.012  58.639  1.00 41.32 ? 798  LEU B CD1   1 
ATOM   14555 C CD2   . LEU B  1 800  ? 22.755  55.615  60.665  1.00 38.39 ? 798  LEU B CD2   1 
ATOM   14556 N N     . SER B  1 801  ? 20.863  52.193  58.391  1.00 41.67 ? 799  SER B N     1 
ATOM   14557 C CA    . SER B  1 801  ? 19.895  51.490  57.571  1.00 45.40 ? 799  SER B CA    1 
ATOM   14558 C C     . SER B  1 801  ? 19.837  52.137  56.192  1.00 50.67 ? 799  SER B C     1 
ATOM   14559 O O     . SER B  1 801  ? 20.330  53.251  56.001  1.00 47.89 ? 799  SER B O     1 
ATOM   14560 C CB    . SER B  1 801  ? 18.519  51.512  58.232  1.00 44.30 ? 799  SER B CB    1 
ATOM   14561 O OG    . SER B  1 801  ? 17.953  52.812  58.218  1.00 43.50 ? 799  SER B OG    1 
ATOM   14562 N N     . PRO B  1 802  ? 19.266  51.447  55.200  1.00 55.23 ? 800  PRO B N     1 
ATOM   14563 C CA    . PRO B  1 802  ? 19.104  52.084  53.883  1.00 51.14 ? 800  PRO B CA    1 
ATOM   14564 C C     . PRO B  1 802  ? 18.404  53.431  53.959  1.00 52.96 ? 800  PRO B C     1 
ATOM   14565 O O     . PRO B  1 802  ? 18.749  54.347  53.200  1.00 57.66 ? 800  PRO B O     1 
ATOM   14566 C CB    . PRO B  1 802  ? 18.284  51.051  53.100  1.00 55.82 ? 800  PRO B CB    1 
ATOM   14567 C CG    . PRO B  1 802  ? 18.623  49.747  53.741  1.00 57.49 ? 800  PRO B CG    1 
ATOM   14568 C CD    . PRO B  1 802  ? 18.807  50.046  55.197  1.00 49.54 ? 800  PRO B CD    1 
ATOM   14569 N N     . ALA B  1 803  ? 17.448  53.587  54.876  1.00 49.40 ? 801  ALA B N     1 
ATOM   14570 C CA    . ALA B  1 803  ? 16.754  54.849  55.096  1.00 48.29 ? 801  ALA B CA    1 
ATOM   14571 C C     . ALA B  1 803  ? 17.543  55.827  55.965  1.00 49.90 ? 801  ALA B C     1 
ATOM   14572 O O     . ALA B  1 803  ? 16.992  56.865  56.349  1.00 48.31 ? 801  ALA B O     1 
ATOM   14573 C CB    . ALA B  1 803  ? 15.388  54.592  55.734  1.00 45.72 ? 801  ALA B CB    1 
ATOM   14574 N N     . GLY B  1 804  ? 18.791  55.510  56.309  1.00 44.67 ? 802  GLY B N     1 
ATOM   14575 C CA    . GLY B  1 804  ? 19.633  56.445  57.029  1.00 43.86 ? 802  GLY B CA    1 
ATOM   14576 C C     . GLY B  1 804  ? 19.329  56.584  58.501  1.00 40.66 ? 802  GLY B C     1 
ATOM   14577 O O     . GLY B  1 804  ? 19.476  57.675  59.058  1.00 36.79 ? 802  GLY B O     1 
ATOM   14578 N N     . ARG B  1 805  ? 18.901  55.507  59.150  1.00 41.16 ? 803  ARG B N     1 
ATOM   14579 C CA    . ARG B  1 805  ? 18.557  55.528  60.557  1.00 37.68 ? 803  ARG B CA    1 
ATOM   14580 C C     . ARG B  1 805  ? 19.382  54.485  61.303  1.00 36.33 ? 803  ARG B C     1 
ATOM   14581 O O     . ARG B  1 805  ? 19.871  53.530  60.694  1.00 38.02 ? 803  ARG B O     1 
ATOM   14582 C CB    . ARG B  1 805  ? 17.059  55.262  60.762  1.00 43.36 ? 803  ARG B CB    1 
ATOM   14583 C CG    . ARG B  1 805  ? 16.152  56.327  60.128  1.00 42.94 ? 803  ARG B CG    1 
ATOM   14584 C CD    . ARG B  1 805  ? 16.442  57.727  60.691  1.00 43.36 ? 803  ARG B CD    1 
ATOM   14585 N NE    . ARG B  1 805  ? 15.484  58.727  60.216  1.00 50.23 ? 803  ARG B NE    1 
ATOM   14586 C CZ    . ARG B  1 805  ? 15.761  59.688  59.342  1.00 47.44 ? 803  ARG B CZ    1 
ATOM   14587 N NH1   . ARG B  1 805  ? 16.972  59.825  58.822  1.00 46.96 ? 803  ARG B NH1   1 
ATOM   14588 N NH2   . ARG B  1 805  ? 14.802  60.548  58.995  1.00 47.85 ? 803  ARG B NH2   1 
ATOM   14589 N N     . PRO B  1 806  ? 19.594  54.660  62.605  1.00 35.06 ? 804  PRO B N     1 
ATOM   14590 C CA    . PRO B  1 806  ? 20.425  53.700  63.343  1.00 35.20 ? 804  PRO B CA    1 
ATOM   14591 C C     . PRO B  1 806  ? 19.838  52.296  63.295  1.00 31.97 ? 804  PRO B C     1 
ATOM   14592 O O     . PRO B  1 806  ? 18.617  52.103  63.319  1.00 29.98 ? 804  PRO B O     1 
ATOM   14593 C CB    . PRO B  1 806  ? 20.429  54.262  64.766  1.00 33.91 ? 804  PRO B CB    1 
ATOM   14594 C CG    . PRO B  1 806  ? 20.179  55.725  64.583  1.00 36.19 ? 804  PRO B CG    1 
ATOM   14595 C CD    . PRO B  1 806  ? 19.227  55.819  63.437  1.00 35.95 ? 804  PRO B CD    1 
ATOM   14596 N N     . ILE B  1 807  ? 20.721  51.313  63.212  1.00 31.71 ? 805  ILE B N     1 
ATOM   14597 C CA    . ILE B  1 807  ? 20.280  49.920  63.151  1.00 29.53 ? 805  ILE B CA    1 
ATOM   14598 C C     . ILE B  1 807  ? 19.880  49.471  64.552  1.00 31.50 ? 805  ILE B C     1 
ATOM   14599 O O     . ILE B  1 807  ? 20.683  49.611  65.487  1.00 28.64 ? 805  ILE B O     1 
ATOM   14600 C CB    . ILE B  1 807  ? 21.381  49.037  62.585  1.00 34.08 ? 805  ILE B CB    1 
ATOM   14601 C CG1   . ILE B  1 807  ? 21.664  49.453  61.144  1.00 33.53 ? 805  ILE B CG1   1 
ATOM   14602 C CG2   . ILE B  1 807  ? 20.973  47.562  62.667  1.00 28.58 ? 805  ILE B CG2   1 
ATOM   14603 C CD1   . ILE B  1 807  ? 22.838  48.800  60.588  1.00 41.07 ? 805  ILE B CD1   1 
ATOM   14604 N N     . PRO B  1 808  ? 18.675  48.930  64.737  1.00 29.73 ? 806  PRO B N     1 
ATOM   14605 C CA    . PRO B  1 808  ? 18.204  48.635  66.093  1.00 28.96 ? 806  PRO B CA    1 
ATOM   14606 C C     . PRO B  1 808  ? 18.969  47.488  66.718  1.00 30.72 ? 806  PRO B C     1 
ATOM   14607 O O     . PRO B  1 808  ? 19.336  46.518  66.052  1.00 28.89 ? 806  PRO B O     1 
ATOM   14608 C CB    . PRO B  1 808  ? 16.732  48.264  65.886  1.00 28.58 ? 806  PRO B CB    1 
ATOM   14609 C CG    . PRO B  1 808  ? 16.366  48.887  64.585  1.00 33.22 ? 806  PRO B CG    1 
ATOM   14610 C CD    . PRO B  1 808  ? 17.599  48.792  63.743  1.00 27.83 ? 806  PRO B CD    1 
ATOM   14611 N N     . LEU B  1 809  ? 19.184  47.596  68.023  1.00 28.50 ? 807  LEU B N     1 
ATOM   14612 C CA    . LEU B  1 809  ? 19.845  46.555  68.789  1.00 26.88 ? 807  LEU B CA    1 
ATOM   14613 C C     . LEU B  1 809  ? 19.015  46.311  70.030  1.00 26.49 ? 807  LEU B C     1 
ATOM   14614 O O     . LEU B  1 809  ? 18.763  47.248  70.794  1.00 28.47 ? 807  LEU B O     1 
ATOM   14615 C CB    . LEU B  1 809  ? 21.270  46.962  69.178  1.00 27.36 ? 807  LEU B CB    1 
ATOM   14616 C CG    . LEU B  1 809  ? 21.927  46.103  70.261  1.00 25.33 ? 807  LEU B CG    1 
ATOM   14617 C CD1   . LEU B  1 809  ? 21.977  44.622  69.855  1.00 29.10 ? 807  LEU B CD1   1 
ATOM   14618 C CD2   . LEU B  1 809  ? 23.341  46.620  70.597  1.00 28.95 ? 807  LEU B CD2   1 
ATOM   14619 N N     . ILE B  1 810  ? 18.578  45.068  70.229  1.00 23.36 ? 808  ILE B N     1 
ATOM   14620 C CA    . ILE B  1 810  ? 17.945  44.670  71.478  1.00 26.01 ? 808  ILE B CA    1 
ATOM   14621 C C     . ILE B  1 810  ? 18.923  43.770  72.203  1.00 27.05 ? 808  ILE B C     1 
ATOM   14622 O O     . ILE B  1 810  ? 19.255  42.680  71.715  1.00 28.41 ? 808  ILE B O     1 
ATOM   14623 C CB    . ILE B  1 810  ? 16.606  43.958  71.261  1.00 26.32 ? 808  ILE B CB    1 
ATOM   14624 C CG1   . ILE B  1 810  ? 15.645  44.850  70.493  1.00 22.50 ? 808  ILE B CG1   1 
ATOM   14625 C CG2   . ILE B  1 810  ? 16.016  43.569  72.612  1.00 26.14 ? 808  ILE B CG2   1 
ATOM   14626 C CD1   . ILE B  1 810  ? 14.276  44.166  70.273  1.00 28.59 ? 808  ILE B CD1   1 
ATOM   14627 N N     . ALA B  1 811  ? 19.376  44.219  73.372  1.00 26.51 ? 809  ALA B N     1 
ATOM   14628 C CA    . ALA B  1 811  ? 20.451  43.565  74.103  1.00 24.79 ? 809  ALA B CA    1 
ATOM   14629 C C     . ALA B  1 811  ? 19.999  43.355  75.541  1.00 30.06 ? 809  ALA B C     1 
ATOM   14630 O O     . ALA B  1 811  ? 19.754  44.325  76.261  1.00 33.43 ? 809  ALA B O     1 
ATOM   14631 C CB    . ALA B  1 811  ? 21.732  44.401  74.048  1.00 26.92 ? 809  ALA B CB    1 
ATOM   14632 N N     . GLU B  1 812  ? 19.874  42.101  75.950  1.00 26.53 ? 810  GLU B N     1 
ATOM   14633 C CA    . GLU B  1 812  ? 19.588  41.747  77.334  1.00 28.22 ? 810  GLU B CA    1 
ATOM   14634 C C     . GLU B  1 812  ? 20.863  41.180  77.948  1.00 29.26 ? 810  GLU B C     1 
ATOM   14635 O O     . GLU B  1 812  ? 21.460  40.250  77.393  1.00 25.90 ? 810  GLU B O     1 
ATOM   14636 C CB    . GLU B  1 812  ? 18.425  40.747  77.418  1.00 28.51 ? 810  GLU B CB    1 
ATOM   14637 N N     . THR B  1 813  ? 21.305  41.758  79.071  1.00 26.31 ? 811  THR B N     1 
ATOM   14638 C CA    . THR B  1 813  ? 22.656  41.509  79.545  1.00 26.63 ? 811  THR B CA    1 
ATOM   14639 C C     . THR B  1 813  ? 22.724  41.282  81.056  1.00 33.85 ? 811  THR B C     1 
ATOM   14640 O O     . THR B  1 813  ? 23.704  41.664  81.701  1.00 32.60 ? 811  THR B O     1 
ATOM   14641 C CB    . THR B  1 813  ? 23.598  42.653  79.156  1.00 32.11 ? 811  THR B CB    1 
ATOM   14642 O OG1   . THR B  1 813  ? 23.012  43.907  79.528  1.00 28.21 ? 811  THR B OG1   1 
ATOM   14643 C CG2   . THR B  1 813  ? 23.865  42.651  77.644  1.00 30.91 ? 811  THR B CG2   1 
ATOM   14644 N N     . GLY B  1 814  ? 21.731  40.631  81.645  1.00 31.26 ? 812  GLY B N     1 
ATOM   14645 C CA    . GLY B  1 814  ? 22.005  40.124  82.997  1.00 35.50 ? 812  GLY B CA    1 
ATOM   14646 C C     . GLY B  1 814  ? 21.990  41.185  84.095  1.00 35.04 ? 812  GLY B C     1 
ATOM   14647 O O     . GLY B  1 814  ? 21.632  42.336  83.879  1.00 35.72 ? 812  GLY B O     1 
ATOM   14648 N N     . GLY B  1 815  ? 22.375  40.763  85.301  1.00 34.54 ? 813  GLY B N     1 
ATOM   14649 C CA    . GLY B  1 815  ? 22.225  41.632  86.458  1.00 33.55 ? 813  GLY B CA    1 
ATOM   14650 C C     . GLY B  1 815  ? 22.910  41.068  87.684  1.00 32.73 ? 813  GLY B C     1 
ATOM   14651 O O     . GLY B  1 815  ? 23.340  39.913  87.711  1.00 38.39 ? 813  GLY B O     1 
ATOM   14652 N N     . GLN B  1 816  ? 22.989  41.915  88.708  1.00 31.14 ? 814  GLN B N     1 
ATOM   14653 C CA    . GLN B  1 816  ? 23.523  41.580  90.027  1.00 29.70 ? 814  GLN B CA    1 
ATOM   14654 C C     . GLN B  1 816  ? 22.352  41.620  91.010  1.00 26.32 ? 814  GLN B C     1 
ATOM   14655 O O     . GLN B  1 816  ? 22.198  42.566  91.783  1.00 27.72 ? 814  GLN B O     1 
ATOM   14656 C CB    . GLN B  1 816  ? 24.639  42.595  90.413  1.00 32.10 ? 814  GLN B CB    1 
ATOM   14657 C CG    . GLN B  1 816  ? 25.610  42.124  91.477  1.00 37.72 ? 814  GLN B CG    1 
ATOM   14658 C CD    . GLN B  1 816  ? 26.473  40.984  90.998  1.00 38.22 ? 814  GLN B CD    1 
ATOM   14659 O OE1   . GLN B  1 816  ? 26.018  39.842  90.939  1.00 36.77 ? 814  GLN B OE1   1 
ATOM   14660 N NE2   . GLN B  1 816  ? 27.734  41.281  90.653  1.00 36.82 ? 814  GLN B NE2   1 
ATOM   14661 N N     . ASN B  1 817  ? 21.536  40.571  90.995  1.00 23.87 ? 815  ASN B N     1 
ATOM   14662 C CA    . ASN B  1 817  ? 20.184  40.645  91.547  1.00 22.81 ? 815  ASN B CA    1 
ATOM   14663 C C     . ASN B  1 817  ? 20.197  40.409  93.054  1.00 24.02 ? 815  ASN B C     1 
ATOM   14664 O O     . ASN B  1 817  ? 20.804  39.444  93.534  1.00 24.42 ? 815  ASN B O     1 
ATOM   14665 C CB    . ASN B  1 817  ? 19.295  39.614  90.841  1.00 21.33 ? 815  ASN B CB    1 
ATOM   14666 C CG    . ASN B  1 817  ? 19.419  39.712  89.335  1.00 24.27 ? 815  ASN B CG    1 
ATOM   14667 O OD1   . ASN B  1 817  ? 19.224  40.787  88.767  1.00 22.89 ? 815  ASN B OD1   1 
ATOM   14668 N ND2   . ASN B  1 817  ? 19.777  38.604  88.687  1.00 23.39 ? 815  ASN B ND2   1 
ATOM   14669 N N     . ALA B  1 818  ? 19.538  41.293  93.792  1.00 22.42 ? 816  ALA B N     1 
ATOM   14670 C CA    . ALA B  1 818  ? 19.482  41.253  95.244  1.00 21.91 ? 816  ALA B CA    1 
ATOM   14671 C C     . ALA B  1 818  ? 18.097  40.824  95.705  1.00 21.08 ? 816  ALA B C     1 
ATOM   14672 O O     . ALA B  1 818  ? 17.092  40.981  95.003  1.00 21.43 ? 816  ALA B O     1 
ATOM   14673 C CB    . ALA B  1 818  ? 19.824  42.625  95.855  1.00 21.21 ? 816  ALA B CB    1 
ATOM   14674 N N     . MET B  1 819  ? 18.048  40.281  96.916  1.00 19.81 ? 817  MET B N     1 
ATOM   14675 C CA    . MET B  1 819  ? 16.793  40.082  97.614  1.00 19.04 ? 817  MET B CA    1 
ATOM   14676 C C     . MET B  1 819  ? 16.973  40.652  99.008  1.00 23.25 ? 817  MET B C     1 
ATOM   14677 O O     . MET B  1 819  ? 18.000  40.404  99.648  1.00 23.40 ? 817  MET B O     1 
ATOM   14678 C CB    . MET B  1 819  ? 16.387  38.604  97.679  1.00 23.29 ? 817  MET B CB    1 
ATOM   14679 C CG    . MET B  1 819  ? 15.152  38.387  98.531  1.00 24.81 ? 817  MET B CG    1 
ATOM   14680 S SD    . MET B  1 819  ? 14.880  36.654  98.900  1.00 28.08 ? 817  MET B SD    1 
ATOM   14681 C CE    . MET B  1 819  ? 14.401  36.055  97.280  1.00 24.68 ? 817  MET B CE    1 
ATOM   14682 N N     . ILE B  1 820  ? 16.000  41.439  99.459  1.00 21.92 ? 818  ILE B N     1 
ATOM   14683 C CA    . ILE B  1 820  ? 16.035  42.060  100.780 1.00 19.78 ? 818  ILE B CA    1 
ATOM   14684 C C     . ILE B  1 820  ? 14.987  41.374  101.649 1.00 21.95 ? 818  ILE B C     1 
ATOM   14685 O O     . ILE B  1 820  ? 13.841  41.207  101.226 1.00 21.92 ? 818  ILE B O     1 
ATOM   14686 C CB    . ILE B  1 820  ? 15.781  43.579  100.698 1.00 19.27 ? 818  ILE B CB    1 
ATOM   14687 C CG1   . ILE B  1 820  ? 16.951  44.274  99.985  1.00 24.40 ? 818  ILE B CG1   1 
ATOM   14688 C CG2   . ILE B  1 820  ? 15.601  44.173  102.116 1.00 21.32 ? 818  ILE B CG2   1 
ATOM   14689 C CD1   . ILE B  1 820  ? 16.780  45.789  99.830  1.00 27.28 ? 818  ILE B CD1   1 
ATOM   14690 N N     . VAL B  1 821  ? 15.383  40.998  102.869 1.00 22.99 ? 819  VAL B N     1 
ATOM   14691 C CA    . VAL B  1 821  ? 14.551  40.243  103.800 1.00 22.88 ? 819  VAL B CA    1 
ATOM   14692 C C     . VAL B  1 821  ? 14.563  40.995  105.126 1.00 22.47 ? 819  VAL B C     1 
ATOM   14693 O O     . VAL B  1 821  ? 15.640  41.286  105.652 1.00 24.11 ? 819  VAL B O     1 
ATOM   14694 C CB    . VAL B  1 821  ? 15.100  38.814  103.995 1.00 22.80 ? 819  VAL B CB    1 
ATOM   14695 C CG1   . VAL B  1 821  ? 14.277  38.021  105.006 1.00 22.38 ? 819  VAL B CG1   1 
ATOM   14696 C CG2   . VAL B  1 821  ? 15.179  38.065  102.649 1.00 20.30 ? 819  VAL B CG2   1 
ATOM   14697 N N     . ASP B  1 822  ? 13.389  41.327  105.659 1.00 24.76 ? 820  ASP B N     1 
ATOM   14698 C CA    . ASP B  1 822  ? 13.353  41.972  106.970 1.00 25.03 ? 820  ASP B CA    1 
ATOM   14699 C C     . ASP B  1 822  ? 12.883  40.976  108.032 1.00 27.18 ? 820  ASP B C     1 
ATOM   14700 O O     . ASP B  1 822  ? 12.591  39.814  107.747 1.00 24.74 ? 820  ASP B O     1 
ATOM   14701 C CB    . ASP B  1 822  ? 12.512  43.258  106.932 1.00 25.09 ? 820  ASP B CB    1 
ATOM   14702 C CG    . ASP B  1 822  ? 10.984  43.028  106.870 1.00 28.19 ? 820  ASP B CG    1 
ATOM   14703 O OD1   . ASP B  1 822  ? 10.466  41.906  107.033 1.00 24.71 ? 820  ASP B OD1   1 
ATOM   14704 O OD2   . ASP B  1 822  ? 10.281  44.048  106.666 1.00 29.76 ? 820  ASP B OD2   1 
ATOM   14705 N N     . SER B  1 823  ? 12.828  41.439  109.281 1.00 25.94 ? 821  SER B N     1 
ATOM   14706 C CA    . SER B  1 823  ? 12.527  40.537  110.384 1.00 28.23 ? 821  SER B CA    1 
ATOM   14707 C C     . SER B  1 823  ? 11.078  40.062  110.402 1.00 30.02 ? 821  SER B C     1 
ATOM   14708 O O     . SER B  1 823  ? 10.747  39.180  111.201 1.00 30.00 ? 821  SER B O     1 
ATOM   14709 C CB    . SER B  1 823  ? 12.878  41.214  111.717 1.00 29.39 ? 821  SER B CB    1 
ATOM   14710 O OG    . SER B  1 823  ? 12.205  42.457  111.864 1.00 31.40 ? 821  SER B OG    1 
ATOM   14711 N N     . SER B  1 824  ? 10.207  40.607  109.559 1.00 25.25 ? 822  SER B N     1 
ATOM   14712 C CA    . SER B  1 824  ? 8.827   40.150  109.531 1.00 26.39 ? 822  SER B CA    1 
ATOM   14713 C C     . SER B  1 824  ? 8.621   38.962  108.602 1.00 29.84 ? 822  SER B C     1 
ATOM   14714 O O     . SER B  1 824  ? 7.579   38.302  108.689 1.00 29.12 ? 822  SER B O     1 
ATOM   14715 C CB    . SER B  1 824  ? 7.885   41.296  109.124 1.00 27.16 ? 822  SER B CB    1 
ATOM   14716 O OG    . SER B  1 824  ? 7.870   41.498  107.720 1.00 26.51 ? 822  SER B OG    1 
ATOM   14717 N N     . ALA B  1 825  ? 9.582   38.675  107.726 1.00 25.04 ? 823  ALA B N     1 
ATOM   14718 C CA    . ALA B  1 825  ? 9.417   37.609  106.747 1.00 30.50 ? 823  ALA B CA    1 
ATOM   14719 C C     . ALA B  1 825  ? 9.412   36.250  107.434 1.00 30.55 ? 823  ALA B C     1 
ATOM   14720 O O     . ALA B  1 825  ? 10.005  36.067  108.501 1.00 29.44 ? 823  ALA B O     1 
ATOM   14721 C CB    . ALA B  1 825  ? 10.542  37.664  105.704 1.00 26.98 ? 823  ALA B CB    1 
ATOM   14722 N N     . LEU B  1 826  ? 8.741   35.287  106.807 1.00 29.83 ? 824  LEU B N     1 
ATOM   14723 C CA    . LEU B  1 826  ? 8.723   33.924  107.330 1.00 31.32 ? 824  LEU B CA    1 
ATOM   14724 C C     . LEU B  1 826  ? 9.975   33.190  106.859 1.00 29.51 ? 824  LEU B C     1 
ATOM   14725 O O     . LEU B  1 826  ? 10.173  32.990  105.652 1.00 29.26 ? 824  LEU B O     1 
ATOM   14726 C CB    . LEU B  1 826  ? 7.462   33.180  106.896 1.00 32.59 ? 824  LEU B CB    1 
ATOM   14727 C CG    . LEU B  1 826  ? 7.338   31.732  107.400 1.00 37.81 ? 824  LEU B CG    1 
ATOM   14728 C CD1   . LEU B  1 826  ? 7.205   31.676  108.912 1.00 36.90 ? 824  LEU B CD1   1 
ATOM   14729 C CD2   . LEU B  1 826  ? 6.168   31.024  106.756 1.00 40.72 ? 824  LEU B CD2   1 
ATOM   14730 N N     . ALA B  1 827  ? 10.804  32.767  107.817 1.00 28.31 ? 825  ALA B N     1 
ATOM   14731 C CA    . ALA B  1 827  ? 12.124  32.234  107.488 1.00 29.22 ? 825  ALA B CA    1 
ATOM   14732 C C     . ALA B  1 827  ? 12.043  31.033  106.550 1.00 28.97 ? 825  ALA B C     1 
ATOM   14733 O O     . ALA B  1 827  ? 12.825  30.930  105.598 1.00 28.86 ? 825  ALA B O     1 
ATOM   14734 C CB    . ALA B  1 827  ? 12.859  31.853  108.766 1.00 29.66 ? 825  ALA B CB    1 
ATOM   14735 N N     . GLU B  1 828  ? 11.126  30.101  106.816 1.00 27.01 ? 826  GLU B N     1 
ATOM   14736 C CA    . GLU B  1 828  ? 11.014  28.921  105.960 1.00 29.03 ? 826  GLU B CA    1 
ATOM   14737 C C     . GLU B  1 828  ? 10.680  29.310  104.529 1.00 31.14 ? 826  GLU B C     1 
ATOM   14738 O O     . GLU B  1 828  ? 11.181  28.704  103.567 1.00 30.72 ? 826  GLU B O     1 
ATOM   14739 C CB    . GLU B  1 828  ? 9.952   27.975  106.503 1.00 29.94 ? 826  GLU B CB    1 
ATOM   14740 C CG    . GLU B  1 828  ? 10.357  27.203  107.764 1.00 36.40 ? 826  GLU B CG    1 
ATOM   14741 C CD    . GLU B  1 828  ? 10.295  28.029  109.050 1.00 40.46 ? 826  GLU B CD    1 
ATOM   14742 O OE1   . GLU B  1 828  ? 9.833   29.200  109.024 1.00 35.57 ? 826  GLU B OE1   1 
ATOM   14743 O OE2   . GLU B  1 828  ? 10.732  27.497  110.097 1.00 41.88 ? 826  GLU B OE2   1 
ATOM   14744 N N     . GLN B  1 829  ? 9.821   30.308  104.363 1.00 27.40 ? 827  GLN B N     1 
ATOM   14745 C CA    . GLN B  1 829  ? 9.445   30.701  103.013 1.00 28.93 ? 827  GLN B CA    1 
ATOM   14746 C C     . GLN B  1 829  ? 10.613  31.383  102.328 1.00 28.48 ? 827  GLN B C     1 
ATOM   14747 O O     . GLN B  1 829  ? 10.881  31.132  101.148 1.00 25.02 ? 827  GLN B O     1 
ATOM   14748 C CB    . GLN B  1 829  ? 8.216   31.608  103.054 1.00 30.88 ? 827  GLN B CB    1 
ATOM   14749 C CG    . GLN B  1 829  ? 7.756   32.112  101.696 1.00 34.95 ? 827  GLN B CG    1 
ATOM   14750 C CD    . GLN B  1 829  ? 6.563   33.046  101.821 1.00 38.66 ? 827  GLN B CD    1 
ATOM   14751 O OE1   . GLN B  1 829  ? 6.299   33.587  102.896 1.00 40.33 ? 827  GLN B OE1   1 
ATOM   14752 N NE2   . GLN B  1 829  ? 5.829   33.229  100.727 1.00 40.04 ? 827  GLN B NE2   1 
ATOM   14753 N N     . VAL B  1 830  ? 11.320  32.235  103.072 1.00 26.30 ? 828  VAL B N     1 
ATOM   14754 C CA    . VAL B  1 830  ? 12.538  32.872  102.579 1.00 26.94 ? 828  VAL B CA    1 
ATOM   14755 C C     . VAL B  1 830  ? 13.551  31.823  102.141 1.00 26.61 ? 828  VAL B C     1 
ATOM   14756 O O     . VAL B  1 830  ? 14.142  31.925  101.062 1.00 23.36 ? 828  VAL B O     1 
ATOM   14757 C CB    . VAL B  1 830  ? 13.132  33.797  103.660 1.00 23.59 ? 828  VAL B CB    1 
ATOM   14758 C CG1   . VAL B  1 830  ? 14.602  34.107  103.368 1.00 25.23 ? 828  VAL B CG1   1 
ATOM   14759 C CG2   . VAL B  1 830  ? 12.346  35.083  103.749 1.00 27.69 ? 828  VAL B CG2   1 
ATOM   14760 N N     . VAL B  1 831  ? 13.788  30.808  102.978 1.00 24.35 ? 829  VAL B N     1 
ATOM   14761 C CA    . VAL B  1 831  ? 14.834  29.846  102.639 1.00 22.89 ? 829  VAL B CA    1 
ATOM   14762 C C     . VAL B  1 831  ? 14.486  29.103  101.357 1.00 22.72 ? 829  VAL B C     1 
ATOM   14763 O O     . VAL B  1 831  ? 15.342  28.921  100.479 1.00 25.70 ? 829  VAL B O     1 
ATOM   14764 C CB    . VAL B  1 831  ? 15.102  28.883  103.808 1.00 24.35 ? 829  VAL B CB    1 
ATOM   14765 C CG1   . VAL B  1 831  ? 15.864  27.645  103.319 1.00 26.01 ? 829  VAL B CG1   1 
ATOM   14766 C CG2   . VAL B  1 831  ? 15.919  29.602  104.872 1.00 23.69 ? 829  VAL B CG2   1 
ATOM   14767 N N     . GLY B  1 832  ? 13.234  28.665  101.222 1.00 24.78 ? 830  GLY B N     1 
ATOM   14768 C CA    . GLY B  1 832  ? 12.827  28.008  99.995  1.00 28.82 ? 830  GLY B CA    1 
ATOM   14769 C C     . GLY B  1 832  ? 13.008  28.898  98.779  1.00 28.67 ? 830  GLY B C     1 
ATOM   14770 O O     . GLY B  1 832  ? 13.467  28.446  97.728  1.00 27.17 ? 830  GLY B O     1 
ATOM   14771 N N     . ASP B  1 833  ? 12.665  30.181  98.913  1.00 23.41 ? 831  ASP B N     1 
ATOM   14772 C CA    . ASP B  1 833  ? 12.760  31.085  97.768  1.00 24.00 ? 831  ASP B CA    1 
ATOM   14773 C C     . ASP B  1 833  ? 14.206  31.441  97.460  1.00 26.18 ? 831  ASP B C     1 
ATOM   14774 O O     . ASP B  1 833  ? 14.556  31.647  96.295  1.00 26.85 ? 831  ASP B O     1 
ATOM   14775 C CB    . ASP B  1 833  ? 11.910  32.330  98.030  1.00 21.68 ? 831  ASP B CB    1 
ATOM   14776 C CG    . ASP B  1 833  ? 10.399  32.021  97.985  1.00 26.83 ? 831  ASP B CG    1 
ATOM   14777 O OD1   . ASP B  1 833  ? 10.017  30.917  97.529  1.00 28.05 ? 831  ASP B OD1   1 
ATOM   14778 O OD2   . ASP B  1 833  ? 9.593   32.863  98.411  1.00 27.05 ? 831  ASP B OD2   1 
ATOM   14779 N N     . VAL B  1 834  ? 15.071  31.477  98.474  1.00 18.43 ? 832  VAL B N     1 
ATOM   14780 C CA    . VAL B  1 834  ? 16.482  31.749  98.228  1.00 24.49 ? 832  VAL B CA    1 
ATOM   14781 C C     . VAL B  1 834  ? 17.145  30.563  97.539  1.00 25.88 ? 832  VAL B C     1 
ATOM   14782 O O     . VAL B  1 834  ? 17.906  30.731  96.578  1.00 26.89 ? 832  VAL B O     1 
ATOM   14783 C CB    . VAL B  1 834  ? 17.186  32.105  99.549  1.00 25.80 ? 832  VAL B CB    1 
ATOM   14784 C CG1   . VAL B  1 834  ? 18.684  32.014  99.388  1.00 23.53 ? 832  VAL B CG1   1 
ATOM   14785 C CG2   . VAL B  1 834  ? 16.765  33.498  99.993  1.00 23.95 ? 832  VAL B CG2   1 
ATOM   14786 N N     . ILE B  1 835  ? 16.907  29.351  98.054  1.00 25.42 ? 833  ILE B N     1 
ATOM   14787 C CA    . ILE B  1 835  ? 17.516  28.151  97.481  1.00 28.42 ? 833  ILE B CA    1 
ATOM   14788 C C     . ILE B  1 835  ? 17.171  28.035  96.006  1.00 30.13 ? 833  ILE B C     1 
ATOM   14789 O O     . ILE B  1 835  ? 18.031  27.723  95.173  1.00 28.20 ? 833  ILE B O     1 
ATOM   14790 C CB    . ILE B  1 835  ? 17.071  26.895  98.255  1.00 30.89 ? 833  ILE B CB    1 
ATOM   14791 C CG1   . ILE B  1 835  ? 17.653  26.881  99.673  1.00 30.32 ? 833  ILE B CG1   1 
ATOM   14792 C CG2   . ILE B  1 835  ? 17.469  25.617  97.498  1.00 31.71 ? 833  ILE B CG2   1 
ATOM   14793 C CD1   . ILE B  1 835  ? 18.886  26.046  99.832  1.00 34.72 ? 833  ILE B CD1   1 
ATOM   14794 N N     . THR B  1 836  ? 15.906  28.275  95.664  1.00 24.66 ? 834  THR B N     1 
ATOM   14795 C CA    . THR B  1 836  ? 15.485  28.249  94.273  1.00 26.06 ? 834  THR B CA    1 
ATOM   14796 C C     . THR B  1 836  ? 16.141  29.372  93.487  1.00 26.09 ? 834  THR B C     1 
ATOM   14797 O O     . THR B  1 836  ? 16.732  29.136  92.433  1.00 27.60 ? 834  THR B O     1 
ATOM   14798 C CB    . THR B  1 836  ? 13.956  28.358  94.195  1.00 29.64 ? 834  THR B CB    1 
ATOM   14799 O OG1   . THR B  1 836  ? 13.369  27.246  94.881  1.00 33.48 ? 834  THR B OG1   1 
ATOM   14800 C CG2   . THR B  1 836  ? 13.495  28.336  92.768  1.00 31.09 ? 834  THR B CG2   1 
ATOM   14801 N N     . SER B  1 837  ? 16.067  30.603  93.998  1.00 22.79 ? 835  SER B N     1 
ATOM   14802 C CA    . SER B  1 837  ? 16.544  31.750  93.232  1.00 23.15 ? 835  SER B CA    1 
ATOM   14803 C C     . SER B  1 837  ? 18.051  31.689  92.990  1.00 21.42 ? 835  SER B C     1 
ATOM   14804 O O     . SER B  1 837  ? 18.523  32.023  91.899  1.00 19.90 ? 835  SER B O     1 
ATOM   14805 C CB    . SER B  1 837  ? 16.162  33.044  93.950  1.00 20.81 ? 835  SER B CB    1 
ATOM   14806 O OG    . SER B  1 837  ? 14.752  33.146  94.000  1.00 24.00 ? 835  SER B OG    1 
ATOM   14807 N N     . ALA B  1 838  ? 18.823  31.245  93.987  1.00 21.37 ? 836  ALA B N     1 
ATOM   14808 C CA    . ALA B  1 838  ? 20.276  31.276  93.863  1.00 22.58 ? 836  ALA B CA    1 
ATOM   14809 C C     . ALA B  1 838  ? 20.862  30.069  93.138  1.00 25.17 ? 836  ALA B C     1 
ATOM   14810 O O     . ALA B  1 838  ? 21.895  30.203  92.477  1.00 26.50 ? 836  ALA B O     1 
ATOM   14811 C CB    . ALA B  1 838  ? 20.917  31.369  95.247  1.00 22.91 ? 836  ALA B CB    1 
ATOM   14812 N N     . PHE B  1 839  ? 20.277  28.882  93.291  1.00 26.18 ? 837  PHE B N     1 
ATOM   14813 C CA    . PHE B  1 839  ? 20.972  27.657  92.907  1.00 26.89 ? 837  PHE B CA    1 
ATOM   14814 C C     . PHE B  1 839  ? 20.247  26.824  91.863  1.00 27.26 ? 837  PHE B C     1 
ATOM   14815 O O     . PHE B  1 839  ? 20.865  25.918  91.292  1.00 27.04 ? 837  PHE B O     1 
ATOM   14816 C CB    . PHE B  1 839  ? 21.246  26.783  94.142  1.00 25.85 ? 837  PHE B CB    1 
ATOM   14817 C CG    . PHE B  1 839  ? 21.951  27.516  95.254  1.00 25.86 ? 837  PHE B CG    1 
ATOM   14818 C CD1   . PHE B  1 839  ? 23.202  28.089  95.045  1.00 30.48 ? 837  PHE B CD1   1 
ATOM   14819 C CD2   . PHE B  1 839  ? 21.366  27.638  96.506  1.00 30.78 ? 837  PHE B CD2   1 
ATOM   14820 C CE1   . PHE B  1 839  ? 23.858  28.771  96.057  1.00 29.41 ? 837  PHE B CE1   1 
ATOM   14821 C CE2   . PHE B  1 839  ? 22.013  28.328  97.533  1.00 28.67 ? 837  PHE B CE2   1 
ATOM   14822 C CZ    . PHE B  1 839  ? 23.268  28.891  97.310  1.00 30.27 ? 837  PHE B CZ    1 
ATOM   14823 N N     . ASP B  1 840  ? 18.969  27.086  91.606  1.00 24.44 ? 838  ASP B N     1 
ATOM   14824 C CA    . ASP B  1 840  ? 18.297  26.460  90.474  1.00 27.27 ? 838  ASP B CA    1 
ATOM   14825 C C     . ASP B  1 840  ? 19.091  26.727  89.207  1.00 28.02 ? 838  ASP B C     1 
ATOM   14826 O O     . ASP B  1 840  ? 19.595  27.835  88.993  1.00 27.69 ? 838  ASP B O     1 
ATOM   14827 C CB    . ASP B  1 840  ? 16.870  27.005  90.338  1.00 26.79 ? 838  ASP B CB    1 
ATOM   14828 C CG    . ASP B  1 840  ? 16.105  26.403  89.174  1.00 32.36 ? 838  ASP B CG    1 
ATOM   14829 O OD1   . ASP B  1 840  ? 16.397  26.756  88.010  1.00 33.30 ? 838  ASP B OD1   1 
ATOM   14830 O OD2   . ASP B  1 840  ? 15.189  25.588  89.427  1.00 34.60 ? 838  ASP B OD2   1 
ATOM   14831 N N     . SER B  1 841  ? 19.220  25.693  88.377  1.00 27.12 ? 839  SER B N     1 
ATOM   14832 C CA    . SER B  1 841  ? 20.001  25.773  87.146  1.00 28.56 ? 839  SER B CA    1 
ATOM   14833 C C     . SER B  1 841  ? 21.439  26.154  87.441  1.00 26.02 ? 839  SER B C     1 
ATOM   14834 O O     . SER B  1 841  ? 22.099  26.812  86.630  1.00 24.27 ? 839  SER B O     1 
ATOM   14835 C CB    . SER B  1 841  ? 19.378  26.760  86.158  1.00 29.62 ? 839  SER B CB    1 
ATOM   14836 O OG    . SER B  1 841  ? 18.037  26.400  85.901  1.00 28.03 ? 839  SER B OG    1 
ATOM   14837 N N     . ALA B  1 842  ? 21.912  25.747  88.621  1.00 26.97 ? 840  ALA B N     1 
ATOM   14838 C CA    . ALA B  1 842  ? 23.261  26.051  89.085  1.00 26.29 ? 840  ALA B CA    1 
ATOM   14839 C C     . ALA B  1 842  ? 23.534  27.548  89.010  1.00 26.45 ? 840  ALA B C     1 
ATOM   14840 O O     . ALA B  1 842  ? 24.639  27.982  88.689  1.00 24.97 ? 840  ALA B O     1 
ATOM   14841 C CB    . ALA B  1 842  ? 24.308  25.257  88.301  1.00 29.41 ? 840  ALA B CB    1 
ATOM   14842 N N     . GLY B  1 843  ? 22.504  28.342  89.301  1.00 25.21 ? 841  GLY B N     1 
ATOM   14843 C CA    . GLY B  1 843  ? 22.647  29.785  89.290  1.00 25.17 ? 841  GLY B CA    1 
ATOM   14844 C C     . GLY B  1 843  ? 22.949  30.380  87.933  1.00 27.61 ? 841  GLY B C     1 
ATOM   14845 O O     . GLY B  1 843  ? 23.457  31.503  87.862  1.00 28.40 ? 841  GLY B O     1 
ATOM   14846 N N     . GLN B  1 844  ? 22.678  29.652  86.849  1.00 25.69 ? 842  GLN B N     1 
ATOM   14847 C CA    . GLN B  1 844  ? 22.965  30.136  85.498  1.00 26.47 ? 842  GLN B CA    1 
ATOM   14848 C C     . GLN B  1 844  ? 21.738  30.779  84.864  1.00 24.66 ? 842  GLN B C     1 
ATOM   14849 O O     . GLN B  1 844  ? 21.503  30.645  83.670  1.00 30.55 ? 842  GLN B O     1 
ATOM   14850 C CB    . GLN B  1 844  ? 23.497  29.012  84.624  1.00 21.74 ? 842  GLN B CB    1 
ATOM   14851 C CG    . GLN B  1 844  ? 24.753  28.354  85.217  1.00 27.47 ? 842  GLN B CG    1 
ATOM   14852 C CD    . GLN B  1 844  ? 25.270  27.208  84.370  1.00 24.97 ? 842  GLN B CD    1 
ATOM   14853 O OE1   . GLN B  1 844  ? 26.442  27.171  84.044  1.00 25.76 ? 842  GLN B OE1   1 
ATOM   14854 N NE2   . GLN B  1 844  ? 24.392  26.270  84.010  1.00 28.15 ? 842  GLN B NE2   1 
ATOM   14855 N N     . ARG B  1 845  ? 20.937  31.466  85.661  1.00 25.54 ? 843  ARG B N     1 
ATOM   14856 C CA    . ARG B  1 845  ? 19.869  32.317  85.159  1.00 24.99 ? 843  ARG B CA    1 
ATOM   14857 C C     . ARG B  1 845  ? 20.329  33.761  85.263  1.00 26.47 ? 843  ARG B C     1 
ATOM   14858 O O     . ARG B  1 845  ? 20.929  34.158  86.264  1.00 26.66 ? 843  ARG B O     1 
ATOM   14859 C CB    . ARG B  1 845  ? 18.588  32.124  85.964  1.00 26.16 ? 843  ARG B CB    1 
ATOM   14860 C CG    . ARG B  1 845  ? 18.045  30.728  85.931  1.00 26.35 ? 843  ARG B CG    1 
ATOM   14861 C CD    . ARG B  1 845  ? 16.826  30.662  86.819  1.00 26.91 ? 843  ARG B CD    1 
ATOM   14862 N NE    . ARG B  1 845  ? 16.215  29.344  86.802  1.00 30.83 ? 843  ARG B NE    1 
ATOM   14863 C CZ    . ARG B  1 845  ? 15.129  29.047  86.102  1.00 31.97 ? 843  ARG B CZ    1 
ATOM   14864 N NH1   . ARG B  1 845  ? 14.527  29.949  85.348  1.00 30.66 ? 843  ARG B NH1   1 
ATOM   14865 N NH2   . ARG B  1 845  ? 14.634  27.813  86.161  1.00 32.56 ? 843  ARG B NH2   1 
ATOM   14866 N N     . CYS B  1 846  ? 20.057  34.549  84.225  1.00 27.02 ? 844  CYS B N     1 
ATOM   14867 C CA    . CYS B  1 846  ? 20.297  35.984  84.339  1.00 25.71 ? 844  CYS B CA    1 
ATOM   14868 C C     . CYS B  1 846  ? 19.533  36.584  85.518  1.00 24.91 ? 844  CYS B C     1 
ATOM   14869 O O     . CYS B  1 846  ? 19.962  37.594  86.081  1.00 24.82 ? 844  CYS B O     1 
ATOM   14870 C CB    . CYS B  1 846  ? 19.902  36.685  83.038  1.00 34.43 ? 844  CYS B CB    1 
ATOM   14871 S SG    . CYS B  1 846  ? 20.861  36.107  81.586  1.00 53.84 ? 844  CYS B SG    1 
ATOM   14872 N N     . SER B  1 847  ? 18.408  35.977  85.893  1.00 24.69 ? 845  SER B N     1 
ATOM   14873 C CA    . SER B  1 847  ? 17.585  36.425  87.013  1.00 25.05 ? 845  SER B CA    1 
ATOM   14874 C C     . SER B  1 847  ? 18.064  35.910  88.367  1.00 24.56 ? 845  SER B C     1 
ATOM   14875 O O     . SER B  1 847  ? 17.467  36.274  89.386  1.00 21.87 ? 845  SER B O     1 
ATOM   14876 C CB    . SER B  1 847  ? 16.143  35.968  86.797  1.00 23.58 ? 845  SER B CB    1 
ATOM   14877 O OG    . SER B  1 847  ? 16.145  34.560  86.582  1.00 26.53 ? 845  SER B OG    1 
ATOM   14878 N N     . ALA B  1 848  ? 19.108  35.082  88.410  1.00 23.11 ? 846  ALA B N     1 
ATOM   14879 C CA    . ALA B  1 848  ? 19.448  34.375  89.640  1.00 21.63 ? 846  ALA B CA    1 
ATOM   14880 C C     . ALA B  1 848  ? 19.782  35.355  90.761  1.00 23.26 ? 846  ALA B C     1 
ATOM   14881 O O     . ALA B  1 848  ? 20.335  36.439  90.534  1.00 21.44 ? 846  ALA B O     1 
ATOM   14882 C CB    . ALA B  1 848  ? 20.629  33.430  89.401  1.00 22.67 ? 846  ALA B CB    1 
ATOM   14883 N N     . LEU B  1 849  ? 19.430  34.962  91.985  1.00 21.57 ? 847  LEU B N     1 
ATOM   14884 C CA    . LEU B  1 849  ? 19.786  35.742  93.170  1.00 20.68 ? 847  LEU B CA    1 
ATOM   14885 C C     . LEU B  1 849  ? 21.298  35.720  93.394  1.00 22.48 ? 847  LEU B C     1 
ATOM   14886 O O     . LEU B  1 849  ? 21.899  34.651  93.508  1.00 25.06 ? 847  LEU B O     1 
ATOM   14887 C CB    . LEU B  1 849  ? 19.063  35.173  94.384  1.00 23.66 ? 847  LEU B CB    1 
ATOM   14888 C CG    . LEU B  1 849  ? 19.395  35.780  95.752  1.00 23.49 ? 847  LEU B CG    1 
ATOM   14889 C CD1   . LEU B  1 849  ? 19.136  37.269  95.735  1.00 22.13 ? 847  LEU B CD1   1 
ATOM   14890 C CD2   . LEU B  1 849  ? 18.525  35.101  96.821  1.00 23.42 ? 847  LEU B CD2   1 
ATOM   14891 N N     . ARG B  1 850  ? 21.907  36.900  93.477  1.00 22.40 ? 848  ARG B N     1 
ATOM   14892 C CA    . ARG B  1 850  ? 23.342  37.021  93.675  1.00 22.53 ? 848  ARG B CA    1 
ATOM   14893 C C     . ARG B  1 850  ? 23.699  37.542  95.050  1.00 20.15 ? 848  ARG B C     1 
ATOM   14894 O O     . ARG B  1 850  ? 24.738  37.171  95.582  1.00 27.07 ? 848  ARG B O     1 
ATOM   14895 C CB    . ARG B  1 850  ? 23.955  37.952  92.621  1.00 23.54 ? 848  ARG B CB    1 
ATOM   14896 C CG    . ARG B  1 850  ? 23.657  37.536  91.191  1.00 26.16 ? 848  ARG B CG    1 
ATOM   14897 C CD    . ARG B  1 850  ? 23.997  36.095  90.936  1.00 23.87 ? 848  ARG B CD    1 
ATOM   14898 N NE    . ARG B  1 850  ? 23.880  35.770  89.513  1.00 27.54 ? 848  ARG B NE    1 
ATOM   14899 C CZ    . ARG B  1 850  ? 24.003  34.546  89.023  1.00 27.71 ? 848  ARG B CZ    1 
ATOM   14900 N NH1   . ARG B  1 850  ? 24.239  33.512  89.817  1.00 25.44 ? 848  ARG B NH1   1 
ATOM   14901 N NH2   . ARG B  1 850  ? 23.848  34.346  87.707  1.00 24.46 ? 848  ARG B NH2   1 
ATOM   14902 N N     . VAL B  1 851  ? 22.850  38.383  95.637  1.00 23.65 ? 849  VAL B N     1 
ATOM   14903 C CA    . VAL B  1 851  ? 23.125  38.992  96.931  1.00 25.34 ? 849  VAL B CA    1 
ATOM   14904 C C     . VAL B  1 851  ? 21.878  38.906  97.788  1.00 25.53 ? 849  VAL B C     1 
ATOM   14905 O O     . VAL B  1 851  ? 20.838  39.489  97.447  1.00 26.20 ? 849  VAL B O     1 
ATOM   14906 C CB    . VAL B  1 851  ? 23.561  40.456  96.810  1.00 26.91 ? 849  VAL B CB    1 
ATOM   14907 C CG1   . VAL B  1 851  ? 23.974  40.958  98.192  1.00 27.62 ? 849  VAL B CG1   1 
ATOM   14908 C CG2   . VAL B  1 851  ? 24.679  40.583  95.817  1.00 28.13 ? 849  VAL B CG2   1 
ATOM   14909 N N     . LEU B  1 852  ? 21.983  38.204  98.903  1.00 25.71 ? 850  LEU B N     1 
ATOM   14910 C CA    . LEU B  1 852  ? 20.889  38.096  99.847  1.00 26.18 ? 850  LEU B CA    1 
ATOM   14911 C C     . LEU B  1 852  ? 21.166  39.073  100.980 1.00 25.82 ? 850  LEU B C     1 
ATOM   14912 O O     . LEU B  1 852  ? 22.256  39.056  101.554 1.00 24.87 ? 850  LEU B O     1 
ATOM   14913 C CB    . LEU B  1 852  ? 20.762  36.665  100.372 1.00 22.50 ? 850  LEU B CB    1 
ATOM   14914 C CG    . LEU B  1 852  ? 19.731  36.416  101.478 1.00 23.28 ? 850  LEU B CG    1 
ATOM   14915 C CD1   . LEU B  1 852  ? 18.293  36.729  101.026 1.00 23.95 ? 850  LEU B CD1   1 
ATOM   14916 C CD2   . LEU B  1 852  ? 19.831  34.979  101.961 1.00 24.27 ? 850  LEU B CD2   1 
ATOM   14917 N N     . CYS B  1 853  ? 20.193  39.938  101.275 1.00 23.25 ? 851  CYS B N     1 
ATOM   14918 C CA    . CYS B  1 853  ? 20.343  40.993  102.275 1.00 23.96 ? 851  CYS B CA    1 
ATOM   14919 C C     . CYS B  1 853  ? 19.398  40.696  103.428 1.00 23.66 ? 851  CYS B C     1 
ATOM   14920 O O     . CYS B  1 853  ? 18.178  40.765  103.266 1.00 23.69 ? 851  CYS B O     1 
ATOM   14921 C CB    . CYS B  1 853  ? 20.039  42.366  101.694 1.00 21.72 ? 851  CYS B CB    1 
ATOM   14922 S SG    . CYS B  1 853  ? 21.020  42.750  100.231 1.00 28.86 ? 851  CYS B SG    1 
ATOM   14923 N N     . LEU B  1 854  ? 19.966  40.401  104.592 1.00 23.16 ? 852  LEU B N     1 
ATOM   14924 C CA    . LEU B  1 854  ? 19.213  39.925  105.742 1.00 23.39 ? 852  LEU B CA    1 
ATOM   14925 C C     . LEU B  1 854  ? 19.270  40.955  106.858 1.00 22.48 ? 852  LEU B C     1 
ATOM   14926 O O     . LEU B  1 854  ? 20.361  41.407  107.232 1.00 25.25 ? 852  LEU B O     1 
ATOM   14927 C CB    . LEU B  1 854  ? 19.788  38.601  106.252 1.00 24.04 ? 852  LEU B CB    1 
ATOM   14928 C CG    . LEU B  1 854  ? 19.740  37.426  105.274 1.00 25.73 ? 852  LEU B CG    1 
ATOM   14929 C CD1   . LEU B  1 854  ? 20.455  36.242  105.882 1.00 24.40 ? 852  LEU B CD1   1 
ATOM   14930 C CD2   . LEU B  1 854  ? 18.288  37.098  104.964 1.00 24.94 ? 852  LEU B CD2   1 
ATOM   14931 N N     . GLN B  1 855  ? 18.106  41.321  107.384 1.00 27.33 ? 853  GLN B N     1 
ATOM   14932 C CA    . GLN B  1 855  ? 18.084  42.198  108.544 1.00 27.54 ? 853  GLN B CA    1 
ATOM   14933 C C     . GLN B  1 855  ? 18.882  41.562  109.674 1.00 28.10 ? 853  GLN B C     1 
ATOM   14934 O O     . GLN B  1 855  ? 18.745  40.365  109.947 1.00 26.57 ? 853  GLN B O     1 
ATOM   14935 C CB    . GLN B  1 855  ? 16.648  42.487  108.989 1.00 23.12 ? 853  GLN B CB    1 
ATOM   14936 C CG    . GLN B  1 855  ? 16.603  43.669  109.965 1.00 26.76 ? 853  GLN B CG    1 
ATOM   14937 C CD    . GLN B  1 855  ? 15.218  43.961  110.495 1.00 31.67 ? 853  GLN B CD    1 
ATOM   14938 O OE1   . GLN B  1 855  ? 14.238  43.932  109.751 1.00 29.36 ? 853  GLN B OE1   1 
ATOM   14939 N NE2   . GLN B  1 855  ? 15.133  44.266  111.789 1.00 29.97 ? 853  GLN B NE2   1 
ATOM   14940 N N     . GLU B  1 856  ? 19.733  42.377  110.308 1.00 27.67 ? 854  GLU B N     1 
ATOM   14941 C CA    . GLU B  1 856  ? 20.694  41.887  111.291 1.00 29.22 ? 854  GLU B CA    1 
ATOM   14942 C C     . GLU B  1 856  ? 20.048  40.979  112.333 1.00 29.96 ? 854  GLU B C     1 
ATOM   14943 O O     . GLU B  1 856  ? 20.629  39.963  112.720 1.00 28.99 ? 854  GLU B O     1 
ATOM   14944 C CB    . GLU B  1 856  ? 21.377  43.079  111.971 1.00 32.97 ? 854  GLU B CB    1 
ATOM   14945 C CG    . GLU B  1 856  ? 22.251  42.713  113.160 1.00 36.62 ? 854  GLU B CG    1 
ATOM   14946 C CD    . GLU B  1 856  ? 23.495  41.909  112.771 1.00 44.47 ? 854  GLU B CD    1 
ATOM   14947 O OE1   . GLU B  1 856  ? 23.970  42.057  111.625 1.00 43.38 ? 854  GLU B OE1   1 
ATOM   14948 O OE2   . GLU B  1 856  ? 24.006  41.134  113.618 1.00 44.63 ? 854  GLU B OE2   1 
ATOM   14949 N N     . ASP B  1 857  ? 18.846  41.326  112.797 1.00 29.38 ? 855  ASP B N     1 
ATOM   14950 C CA    . ASP B  1 857  ? 18.240  40.618  113.926 1.00 28.33 ? 855  ASP B CA    1 
ATOM   14951 C C     . ASP B  1 857  ? 17.828  39.192  113.587 1.00 34.08 ? 855  ASP B C     1 
ATOM   14952 O O     . ASP B  1 857  ? 17.702  38.371  114.503 1.00 35.23 ? 855  ASP B O     1 
ATOM   14953 C CB    . ASP B  1 857  ? 17.019  41.382  114.442 1.00 32.69 ? 855  ASP B CB    1 
ATOM   14954 N N     . VAL B  1 858  ? 17.583  38.876  112.311 1.00 27.18 ? 856  VAL B N     1 
ATOM   14955 C CA    . VAL B  1 858  ? 17.208  37.522  111.921 1.00 28.16 ? 856  VAL B CA    1 
ATOM   14956 C C     . VAL B  1 858  ? 18.267  36.839  111.069 1.00 24.97 ? 856  VAL B C     1 
ATOM   14957 O O     . VAL B  1 858  ? 18.063  35.690  110.662 1.00 26.53 ? 856  VAL B O     1 
ATOM   14958 C CB    . VAL B  1 858  ? 15.839  37.492  111.207 1.00 27.43 ? 856  VAL B CB    1 
ATOM   14959 C CG1   . VAL B  1 858  ? 14.739  37.971  112.163 1.00 27.47 ? 856  VAL B CG1   1 
ATOM   14960 C CG2   . VAL B  1 858  ? 15.858  38.331  109.956 1.00 27.33 ? 856  VAL B CG2   1 
ATOM   14961 N N     . ALA B  1 859  ? 19.407  37.485  110.825 1.00 26.37 ? 857  ALA B N     1 
ATOM   14962 C CA    . ALA B  1 859  ? 20.371  36.955  109.862 1.00 26.20 ? 857  ALA B CA    1 
ATOM   14963 C C     . ALA B  1 859  ? 20.911  35.592  110.280 1.00 24.78 ? 857  ALA B C     1 
ATOM   14964 O O     . ALA B  1 859  ? 20.971  34.666  109.465 1.00 23.53 ? 857  ALA B O     1 
ATOM   14965 C CB    . ALA B  1 859  ? 21.509  37.955  109.658 1.00 26.33 ? 857  ALA B CB    1 
ATOM   14966 N N     . ASP B  1 860  ? 21.315  35.439  111.549 1.00 28.83 ? 858  ASP B N     1 
ATOM   14967 C CA    . ASP B  1 860  ? 21.932  34.174  111.954 1.00 29.41 ? 858  ASP B CA    1 
ATOM   14968 C C     . ASP B  1 860  ? 20.963  33.007  111.834 1.00 25.42 ? 858  ASP B C     1 
ATOM   14969 O O     . ASP B  1 860  ? 21.353  31.915  111.408 1.00 28.00 ? 858  ASP B O     1 
ATOM   14970 C CB    . ASP B  1 860  ? 22.466  34.248  113.387 1.00 28.99 ? 858  ASP B CB    1 
ATOM   14971 C CG    . ASP B  1 860  ? 23.613  35.213  113.524 1.00 34.49 ? 858  ASP B CG    1 
ATOM   14972 O OD1   . ASP B  1 860  ? 24.403  35.353  112.560 1.00 35.30 ? 858  ASP B OD1   1 
ATOM   14973 O OD2   . ASP B  1 860  ? 23.710  35.842  114.592 1.00 38.40 ? 858  ASP B OD2   1 
ATOM   14974 N N     . ARG B  1 861  ? 19.702  33.201  112.237 1.00 26.99 ? 859  ARG B N     1 
ATOM   14975 C CA    . ARG B  1 861  ? 18.768  32.085  112.205 1.00 27.86 ? 859  ARG B CA    1 
ATOM   14976 C C     . ARG B  1 861  ? 18.449  31.673  110.771 1.00 28.94 ? 859  ARG B C     1 
ATOM   14977 O O     . ARG B  1 861  ? 18.423  30.479  110.448 1.00 26.72 ? 859  ARG B O     1 
ATOM   14978 C CB    . ARG B  1 861  ? 17.488  32.450  112.954 1.00 34.96 ? 859  ARG B CB    1 
ATOM   14979 C CG    . ARG B  1 861  ? 16.391  31.430  112.747 1.00 38.61 ? 859  ARG B CG    1 
ATOM   14980 C CD    . ARG B  1 861  ? 15.336  31.457  113.827 1.00 45.10 ? 859  ARG B CD    1 
ATOM   14981 N NE    . ARG B  1 861  ? 14.295  30.476  113.535 1.00 47.38 ? 859  ARG B NE    1 
ATOM   14982 C CZ    . ARG B  1 861  ? 13.227  30.730  112.790 1.00 42.45 ? 859  ARG B CZ    1 
ATOM   14983 N NH1   . ARG B  1 861  ? 13.011  31.933  112.278 1.00 40.55 ? 859  ARG B NH1   1 
ATOM   14984 N NH2   . ARG B  1 861  ? 12.355  29.751  112.549 1.00 46.20 ? 859  ARG B NH2   1 
ATOM   14985 N N     . ILE B  1 862  ? 18.201  32.647  109.896 1.00 26.34 ? 860  ILE B N     1 
ATOM   14986 C CA    . ILE B  1 862  ? 17.956  32.328  108.488 1.00 22.33 ? 860  ILE B CA    1 
ATOM   14987 C C     . ILE B  1 862  ? 19.187  31.676  107.864 1.00 21.95 ? 860  ILE B C     1 
ATOM   14988 O O     . ILE B  1 862  ? 19.076  30.716  107.089 1.00 24.18 ? 860  ILE B O     1 
ATOM   14989 C CB    . ILE B  1 862  ? 17.519  33.603  107.744 1.00 23.76 ? 860  ILE B CB    1 
ATOM   14990 C CG1   . ILE B  1 862  ? 16.143  34.039  108.261 1.00 26.75 ? 860  ILE B CG1   1 
ATOM   14991 C CG2   . ILE B  1 862  ? 17.521  33.398  106.224 1.00 26.95 ? 860  ILE B CG2   1 
ATOM   14992 C CD1   . ILE B  1 862  ? 15.632  35.379  107.702 1.00 26.90 ? 860  ILE B CD1   1 
ATOM   14993 N N     . LEU B  1 863  ? 20.382  32.168  108.200 1.00 23.97 ? 861  LEU B N     1 
ATOM   14994 C CA    . LEU B  1 863  ? 21.591  31.539  107.670 1.00 25.72 ? 861  LEU B CA    1 
ATOM   14995 C C     . LEU B  1 863  ? 21.698  30.086  108.113 1.00 27.70 ? 861  LEU B C     1 
ATOM   14996 O O     . LEU B  1 863  ? 22.044  29.206  107.311 1.00 26.33 ? 861  LEU B O     1 
ATOM   14997 C CB    . LEU B  1 863  ? 22.832  32.318  108.101 1.00 27.83 ? 861  LEU B CB    1 
ATOM   14998 C CG    . LEU B  1 863  ? 23.147  33.515  107.213 1.00 33.77 ? 861  LEU B CG    1 
ATOM   14999 C CD1   . LEU B  1 863  ? 24.239  34.388  107.840 1.00 36.88 ? 861  LEU B CD1   1 
ATOM   15000 C CD2   . LEU B  1 863  ? 23.556  33.011  105.837 1.00 32.79 ? 861  LEU B CD2   1 
ATOM   15001 N N     . THR B  1 864  ? 21.409  29.807  109.388 1.00 26.73 ? 862  THR B N     1 
ATOM   15002 C CA    . THR B  1 864  ? 21.440  28.418  109.836 1.00 27.64 ? 862  THR B CA    1 
ATOM   15003 C C     . THR B  1 864  ? 20.465  27.566  109.035 1.00 28.61 ? 862  THR B C     1 
ATOM   15004 O O     . THR B  1 864  ? 20.810  26.462  108.594 1.00 28.37 ? 862  THR B O     1 
ATOM   15005 C CB    . THR B  1 864  ? 21.135  28.341  111.327 1.00 34.06 ? 862  THR B CB    1 
ATOM   15006 O OG1   . THR B  1 864  ? 22.183  28.999  112.029 1.00 30.26 ? 862  THR B OG1   1 
ATOM   15007 C CG2   . THR B  1 864  ? 21.057  26.898  111.786 1.00 37.09 ? 862  THR B CG2   1 
ATOM   15008 N N     . MET B  1 865  ? 19.240  28.070  108.835 1.00 24.67 ? 863  MET B N     1 
ATOM   15009 C CA    . MET B  1 865  ? 18.230  27.318  108.092 1.00 29.70 ? 863  MET B CA    1 
ATOM   15010 C C     . MET B  1 865  ? 18.648  27.149  106.643 1.00 26.41 ? 863  MET B C     1 
ATOM   15011 O O     . MET B  1 865  ? 18.492  26.068  106.061 1.00 23.62 ? 863  MET B O     1 
ATOM   15012 C CB    . MET B  1 865  ? 16.882  28.036  108.169 1.00 24.45 ? 863  MET B CB    1 
ATOM   15013 C CG    . MET B  1 865  ? 15.682  27.234  107.716 1.00 27.95 ? 863  MET B CG    1 
ATOM   15014 S SD    . MET B  1 865  ? 14.145  28.164  108.014 1.00 33.90 ? 863  MET B SD    1 
ATOM   15015 C CE    . MET B  1 865  ? 14.578  28.859  109.618 1.00 29.82 ? 863  MET B CE    1 
ATOM   15016 N N     . LEU B  1 866  ? 19.197  28.212  106.059 1.00 26.23 ? 864  LEU B N     1 
ATOM   15017 C CA    . LEU B  1 866  ? 19.665  28.157  104.679 1.00 26.26 ? 864  LEU B CA    1 
ATOM   15018 C C     . LEU B  1 866  ? 20.734  27.086  104.517 1.00 27.27 ? 864  LEU B C     1 
ATOM   15019 O O     . LEU B  1 866  ? 20.688  26.272  103.586 1.00 28.02 ? 864  LEU B O     1 
ATOM   15020 C CB    . LEU B  1 866  ? 20.194  29.534  104.270 1.00 26.89 ? 864  LEU B CB    1 
ATOM   15021 C CG    . LEU B  1 866  ? 20.725  29.658  102.848 1.00 27.37 ? 864  LEU B CG    1 
ATOM   15022 C CD1   . LEU B  1 866  ? 19.626  29.237  101.896 1.00 29.04 ? 864  LEU B CD1   1 
ATOM   15023 C CD2   . LEU B  1 866  ? 21.147  31.103  102.571 1.00 30.99 ? 864  LEU B CD2   1 
ATOM   15024 N N     . LYS B  1 867  ? 21.685  27.042  105.449 1.00 25.89 ? 865  LYS B N     1 
ATOM   15025 C CA    . LYS B  1 867  ? 22.755  26.056  105.365 1.00 27.20 ? 865  LYS B CA    1 
ATOM   15026 C C     . LYS B  1 867  ? 22.226  24.643  105.585 1.00 33.05 ? 865  LYS B C     1 
ATOM   15027 O O     . LYS B  1 867  ? 22.661  23.702  104.913 1.00 29.45 ? 865  LYS B O     1 
ATOM   15028 C CB    . LYS B  1 867  ? 23.852  26.407  106.370 1.00 28.93 ? 865  LYS B CB    1 
ATOM   15029 C CG    . LYS B  1 867  ? 24.678  27.618  105.928 1.00 30.82 ? 865  LYS B CG    1 
ATOM   15030 C CD    . LYS B  1 867  ? 25.408  28.264  107.090 1.00 35.44 ? 865  LYS B CD    1 
ATOM   15031 C CE    . LYS B  1 867  ? 26.291  29.420  106.603 1.00 38.86 ? 865  LYS B CE    1 
ATOM   15032 N NZ    . LYS B  1 867  ? 27.028  30.092  107.713 1.00 43.29 ? 865  LYS B NZ    1 
ATOM   15033 N N     . GLY B  1 868  ? 21.270  24.472  106.500 1.00 29.18 ? 866  GLY B N     1 
ATOM   15034 C CA    . GLY B  1 868  ? 20.672  23.156  106.678 1.00 27.45 ? 866  GLY B CA    1 
ATOM   15035 C C     . GLY B  1 868  ? 19.929  22.678  105.444 1.00 28.57 ? 866  GLY B C     1 
ATOM   15036 O O     . GLY B  1 868  ? 20.038  21.514  105.053 1.00 30.43 ? 866  GLY B O     1 
ATOM   15037 N N     . ALA B  1 869  ? 19.168  23.572  104.811 1.00 29.47 ? 867  ALA B N     1 
ATOM   15038 C CA    . ALA B  1 869  ? 18.472  23.222  103.576 1.00 31.67 ? 867  ALA B CA    1 
ATOM   15039 C C     . ALA B  1 869  ? 19.449  22.930  102.445 1.00 28.25 ? 867  ALA B C     1 
ATOM   15040 O O     . ALA B  1 869  ? 19.192  22.061  101.603 1.00 29.55 ? 867  ALA B O     1 
ATOM   15041 C CB    . ALA B  1 869  ? 17.530  24.351  103.166 1.00 28.12 ? 867  ALA B CB    1 
ATOM   15042 N N     . LEU B  1 870  ? 20.546  23.683  102.374 1.00 27.43 ? 868  LEU B N     1 
ATOM   15043 C CA    . LEU B  1 870  ? 21.510  23.465  101.300 1.00 31.44 ? 868  LEU B CA    1 
ATOM   15044 C C     . LEU B  1 870  ? 22.067  22.054  101.337 1.00 31.86 ? 868  LEU B C     1 
ATOM   15045 O O     . LEU B  1 870  ? 22.259  21.424  100.291 1.00 31.28 ? 868  LEU B O     1 
ATOM   15046 C CB    . LEU B  1 870  ? 22.649  24.477  101.401 1.00 32.14 ? 868  LEU B CB    1 
ATOM   15047 C CG    . LEU B  1 870  ? 23.322  24.732  100.063 1.00 39.21 ? 868  LEU B CG    1 
ATOM   15048 C CD1   . LEU B  1 870  ? 22.324  25.466  99.176  1.00 36.19 ? 868  LEU B CD1   1 
ATOM   15049 C CD2   . LEU B  1 870  ? 24.616  25.512  100.216 1.00 43.80 ? 868  LEU B CD2   1 
ATOM   15050 N N     . HIS B  1 871  ? 22.330  21.532  102.529 1.00 28.48 ? 869  HIS B N     1 
ATOM   15051 C CA    . HIS B  1 871  ? 22.950  20.217  102.593 1.00 30.57 ? 869  HIS B CA    1 
ATOM   15052 C C     . HIS B  1 871  ? 21.999  19.088  102.222 1.00 31.63 ? 869  HIS B C     1 
ATOM   15053 O O     . HIS B  1 871  ? 22.440  17.937  102.127 1.00 30.14 ? 869  HIS B O     1 
ATOM   15054 C CB    . HIS B  1 871  ? 23.547  20.004  103.981 1.00 37.67 ? 869  HIS B CB    1 
ATOM   15055 C CG    . HIS B  1 871  ? 24.748  20.860  104.241 1.00 40.72 ? 869  HIS B CG    1 
ATOM   15056 N ND1   . HIS B  1 871  ? 25.961  20.647  103.618 1.00 47.65 ? 869  HIS B ND1   1 
ATOM   15057 C CD2   . HIS B  1 871  ? 24.922  21.936  105.045 1.00 40.41 ? 869  HIS B CD2   1 
ATOM   15058 C CE1   . HIS B  1 871  ? 26.830  21.552  104.032 1.00 45.43 ? 869  HIS B CE1   1 
ATOM   15059 N NE2   . HIS B  1 871  ? 26.223  22.349  104.894 1.00 45.30 ? 869  HIS B NE2   1 
ATOM   15060 N N     . GLU B  1 872  ? 20.729  19.388  101.981 1.00 26.97 ? 870  GLU B N     1 
ATOM   15061 C CA    . GLU B  1 872  ? 19.771  18.394  101.531 1.00 28.66 ? 870  GLU B CA    1 
ATOM   15062 C C     . GLU B  1 872  ? 19.666  18.331  100.014 1.00 29.18 ? 870  GLU B C     1 
ATOM   15063 O O     . GLU B  1 872  ? 18.900  17.511  99.501  1.00 30.92 ? 870  GLU B O     1 
ATOM   15064 C CB    . GLU B  1 872  ? 18.389  18.678  102.138 1.00 29.57 ? 870  GLU B CB    1 
ATOM   15065 C CG    . GLU B  1 872  ? 18.351  18.636  103.669 1.00 25.23 ? 870  GLU B CG    1 
ATOM   15066 C CD    . GLU B  1 872  ? 18.728  17.275  104.231 1.00 31.32 ? 870  GLU B CD    1 
ATOM   15067 O OE1   . GLU B  1 872  ? 18.555  16.263  103.515 1.00 35.07 ? 870  GLU B OE1   1 
ATOM   15068 O OE2   . GLU B  1 872  ? 19.210  17.213  105.383 1.00 33.54 ? 870  GLU B OE2   1 
ATOM   15069 N N     . LEU B  1 873  ? 20.403  19.178  99.291  1.00 27.11 ? 871  LEU B N     1 
ATOM   15070 C CA    . LEU B  1 873  ? 20.339  19.197  97.831  1.00 28.36 ? 871  LEU B CA    1 
ATOM   15071 C C     . LEU B  1 873  ? 21.169  18.069  97.243  1.00 30.19 ? 871  LEU B C     1 
ATOM   15072 O O     . LEU B  1 873  ? 22.204  17.683  97.790  1.00 29.96 ? 871  LEU B O     1 
ATOM   15073 C CB    . LEU B  1 873  ? 20.854  20.527  97.271  1.00 27.61 ? 871  LEU B CB    1 
ATOM   15074 C CG    . LEU B  1 873  ? 20.112  21.833  97.574  1.00 35.10 ? 871  LEU B CG    1 
ATOM   15075 C CD1   . LEU B  1 873  ? 20.765  23.003  96.829  1.00 29.40 ? 871  LEU B CD1   1 
ATOM   15076 C CD2   . LEU B  1 873  ? 18.618  21.731  97.251  1.00 32.62 ? 871  LEU B CD2   1 
ATOM   15077 N N     . HIS B  1 874  ? 20.719  17.551  96.100  1.00 28.71 ? 872  HIS B N     1 
ATOM   15078 C CA    . HIS B  1 874  ? 21.419  16.493  95.379  1.00 32.32 ? 872  HIS B CA    1 
ATOM   15079 C C     . HIS B  1 874  ? 22.012  17.105  94.113  1.00 32.20 ? 872  HIS B C     1 
ATOM   15080 O O     . HIS B  1 874  ? 21.272  17.642  93.280  1.00 28.97 ? 872  HIS B O     1 
ATOM   15081 C CB    . HIS B  1 874  ? 20.459  15.343  95.049  1.00 28.93 ? 872  HIS B CB    1 
ATOM   15082 C CG    . HIS B  1 874  ? 21.084  14.213  94.288  1.00 30.25 ? 872  HIS B CG    1 
ATOM   15083 N ND1   . HIS B  1 874  ? 22.441  14.114  94.064  1.00 37.53 ? 872  HIS B ND1   1 
ATOM   15084 C CD2   . HIS B  1 874  ? 20.527  13.133  93.690  1.00 32.68 ? 872  HIS B CD2   1 
ATOM   15085 C CE1   . HIS B  1 874  ? 22.691  13.029  93.354  1.00 33.74 ? 872  HIS B CE1   1 
ATOM   15086 N NE2   . HIS B  1 874  ? 21.546  12.415  93.117  1.00 37.60 ? 872  HIS B NE2   1 
ATOM   15087 N N     . ILE B  1 875  ? 23.337  17.051  93.986  1.00 30.33 ? 873  ILE B N     1 
ATOM   15088 C CA    . ILE B  1 875  ? 24.054  17.602  92.841  1.00 31.84 ? 873  ILE B CA    1 
ATOM   15089 C C     . ILE B  1 875  ? 24.608  16.445  92.019  1.00 33.54 ? 873  ILE B C     1 
ATOM   15090 O O     . ILE B  1 875  ? 25.247  15.541  92.567  1.00 27.31 ? 873  ILE B O     1 
ATOM   15091 C CB    . ILE B  1 875  ? 25.189  18.538  93.287  1.00 33.47 ? 873  ILE B CB    1 
ATOM   15092 C CG1   . ILE B  1 875  ? 24.637  19.678  94.137  1.00 34.38 ? 873  ILE B CG1   1 
ATOM   15093 C CG2   . ILE B  1 875  ? 25.941  19.081  92.082  1.00 32.79 ? 873  ILE B CG2   1 
ATOM   15094 C CD1   . ILE B  1 875  ? 25.361  19.817  95.466  1.00 40.83 ? 873  ILE B CD1   1 
ATOM   15095 N N     . GLY B  1 876  ? 24.363  16.463  90.714  1.00 31.59 ? 874  GLY B N     1 
ATOM   15096 C CA    . GLY B  1 876  ? 24.886  15.409  89.869  1.00 29.95 ? 874  GLY B CA    1 
ATOM   15097 C C     . GLY B  1 876  ? 24.319  15.501  88.467  1.00 31.84 ? 874  GLY B C     1 
ATOM   15098 O O     . GLY B  1 876  ? 23.630  16.461  88.117  1.00 27.26 ? 874  GLY B O     1 
ATOM   15099 N N     . ARG B  1 877  ? 24.634  14.477  87.674  1.00 31.78 ? 875  ARG B N     1 
ATOM   15100 C CA    . ARG B  1 877  ? 24.164  14.418  86.300  1.00 34.58 ? 875  ARG B CA    1 
ATOM   15101 C C     . ARG B  1 877  ? 22.643  14.359  86.291  1.00 33.67 ? 875  ARG B C     1 
ATOM   15102 O O     . ARG B  1 877  ? 22.037  13.585  87.038  1.00 33.78 ? 875  ARG B O     1 
ATOM   15103 C CB    . ARG B  1 877  ? 24.755  13.198  85.592  1.00 35.63 ? 875  ARG B CB    1 
ATOM   15104 C CG    . ARG B  1 877  ? 24.549  13.215  84.086  1.00 38.65 ? 875  ARG B CG    1 
ATOM   15105 C CD    . ARG B  1 877  ? 25.318  12.080  83.431  1.00 42.78 ? 875  ARG B CD    1 
ATOM   15106 N NE    . ARG B  1 877  ? 24.474  10.920  83.178  1.00 44.57 ? 875  ARG B NE    1 
ATOM   15107 C CZ    . ARG B  1 877  ? 24.877  9.840   82.520  1.00 52.82 ? 875  ARG B CZ    1 
ATOM   15108 N NH1   . ARG B  1 877  ? 26.118  9.728   82.070  1.00 45.72 ? 875  ARG B NH1   1 
ATOM   15109 N NH2   . ARG B  1 877  ? 24.015  8.848   82.308  1.00 51.80 ? 875  ARG B NH2   1 
ATOM   15110 N N     . THR B  1 878  ? 22.027  15.175  85.437  1.00 30.50 ? 876  THR B N     1 
ATOM   15111 C CA    . THR B  1 878  ? 20.609  15.495  85.551  1.00 30.55 ? 876  THR B CA    1 
ATOM   15112 C C     . THR B  1 878  ? 19.685  14.523  84.833  1.00 32.20 ? 876  THR B C     1 
ATOM   15113 O O     . THR B  1 878  ? 18.541  14.890  84.542  1.00 37.63 ? 876  THR B O     1 
ATOM   15114 C CB    . THR B  1 878  ? 20.344  16.907  85.032  1.00 30.44 ? 876  THR B CB    1 
ATOM   15115 O OG1   . THR B  1 878  ? 20.899  17.050  83.715  1.00 32.97 ? 876  THR B OG1   1 
ATOM   15116 C CG2   . THR B  1 878  ? 20.957  17.921  85.952  1.00 26.82 ? 876  THR B CG2   1 
ATOM   15117 N N     . ASP B  1 879  ? 20.115  13.292  84.569  1.00 35.75 ? 877  ASP B N     1 
ATOM   15118 C CA    . ASP B  1 879  ? 19.185  12.303  84.039  1.00 36.93 ? 877  ASP B CA    1 
ATOM   15119 C C     . ASP B  1 879  ? 18.580  11.440  85.143  1.00 33.63 ? 877  ASP B C     1 
ATOM   15120 O O     . ASP B  1 879  ? 18.162  10.303  84.898  1.00 31.69 ? 877  ASP B O     1 
ATOM   15121 C CB    . ASP B  1 879  ? 19.854  11.457  82.952  1.00 37.75 ? 877  ASP B CB    1 
ATOM   15122 C CG    . ASP B  1 879  ? 20.971  10.588  83.472  1.00 40.82 ? 877  ASP B CG    1 
ATOM   15123 O OD1   . ASP B  1 879  ? 21.585  10.922  84.510  1.00 42.49 ? 877  ASP B OD1   1 
ATOM   15124 O OD2   . ASP B  1 879  ? 21.237  9.557   82.816  1.00 47.13 ? 877  ASP B OD2   1 
ATOM   15125 N N     . ARG B  1 880  ? 18.495  11.987  86.351  1.00 33.13 ? 878  ARG B N     1 
ATOM   15126 C CA    . ARG B  1 880  ? 17.795  11.384  87.475  1.00 33.20 ? 878  ARG B CA    1 
ATOM   15127 C C     . ARG B  1 880  ? 16.843  12.422  88.051  1.00 30.73 ? 878  ARG B C     1 
ATOM   15128 O O     . ARG B  1 880  ? 17.243  13.566  88.283  1.00 29.84 ? 878  ARG B O     1 
ATOM   15129 C CB    . ARG B  1 880  ? 18.782  10.910  88.550  1.00 29.13 ? 878  ARG B CB    1 
ATOM   15130 N N     . LEU B  1 881  ? 15.588  12.013  88.283  1.00 30.28 ? 879  LEU B N     1 
ATOM   15131 C CA    . LEU B  1 881  ? 14.587  12.900  88.868  1.00 27.70 ? 879  LEU B CA    1 
ATOM   15132 C C     . LEU B  1 881  ? 15.020  13.448  90.225  1.00 30.82 ? 879  LEU B C     1 
ATOM   15133 O O     . LEU B  1 881  ? 14.690  14.593  90.566  1.00 29.08 ? 879  LEU B O     1 
ATOM   15134 C CB    . LEU B  1 881  ? 13.262  12.151  89.010  1.00 28.51 ? 879  LEU B CB    1 
ATOM   15135 C CG    . LEU B  1 881  ? 12.093  13.004  89.523  1.00 30.63 ? 879  LEU B CG    1 
ATOM   15136 C CD1   . LEU B  1 881  ? 11.696  14.016  88.479  1.00 31.69 ? 879  LEU B CD1   1 
ATOM   15137 C CD2   . LEU B  1 881  ? 10.915  12.125  89.899  1.00 29.03 ? 879  LEU B CD2   1 
ATOM   15138 N N     . SER B  1 882  ? 15.754  12.650  91.008  1.00 29.84 ? 880  SER B N     1 
ATOM   15139 C CA    . SER B  1 882  ? 16.222  13.047  92.335  1.00 31.38 ? 880  SER B CA    1 
ATOM   15140 C C     . SER B  1 882  ? 17.277  14.148  92.319  1.00 32.30 ? 880  SER B C     1 
ATOM   15141 O O     . SER B  1 882  ? 17.639  14.643  93.390  1.00 33.68 ? 880  SER B O     1 
ATOM   15142 C CB    . SER B  1 882  ? 16.799  11.835  93.055  1.00 30.00 ? 880  SER B CB    1 
ATOM   15143 O OG    . SER B  1 882  ? 17.950  11.372  92.371  1.00 33.92 ? 880  SER B OG    1 
ATOM   15144 N N     . VAL B  1 883  ? 17.790  14.543  91.162  1.00 29.33 ? 881  VAL B N     1 
ATOM   15145 C CA    . VAL B  1 883  ? 18.861  15.531  91.132  1.00 28.22 ? 881  VAL B CA    1 
ATOM   15146 C C     . VAL B  1 883  ? 18.257  16.927  91.170  1.00 29.77 ? 881  VAL B C     1 
ATOM   15147 O O     . VAL B  1 883  ? 17.344  17.247  90.397  1.00 29.65 ? 881  VAL B O     1 
ATOM   15148 C CB    . VAL B  1 883  ? 19.755  15.338  89.898  1.00 31.06 ? 881  VAL B CB    1 
ATOM   15149 C CG1   . VAL B  1 883  ? 20.706  16.518  89.746  1.00 26.83 ? 881  VAL B CG1   1 
ATOM   15150 C CG2   . VAL B  1 883  ? 20.526  14.029  90.023  1.00 35.08 ? 881  VAL B CG2   1 
ATOM   15151 N N     . ASP B  1 884  ? 18.762  17.757  92.075  1.00 28.21 ? 882  ASP B N     1 
ATOM   15152 C CA    . ASP B  1 884  ? 18.265  19.115  92.244  1.00 30.08 ? 882  ASP B CA    1 
ATOM   15153 C C     . ASP B  1 884  ? 19.051  20.130  91.427  1.00 29.92 ? 882  ASP B C     1 
ATOM   15154 O O     . ASP B  1 884  ? 18.462  21.057  90.861  1.00 32.23 ? 882  ASP B O     1 
ATOM   15155 C CB    . ASP B  1 884  ? 18.311  19.490  93.727  1.00 28.00 ? 882  ASP B CB    1 
ATOM   15156 C CG    . ASP B  1 884  ? 17.435  18.573  94.583  1.00 30.49 ? 882  ASP B CG    1 
ATOM   15157 O OD1   . ASP B  1 884  ? 16.241  18.420  94.239  1.00 31.52 ? 882  ASP B OD1   1 
ATOM   15158 O OD2   . ASP B  1 884  ? 17.937  17.986  95.573  1.00 29.54 ? 882  ASP B OD2   1 
ATOM   15159 N N     . VAL B  1 885  ? 20.371  19.979  91.372  1.00 28.88 ? 883  VAL B N     1 
ATOM   15160 C CA    . VAL B  1 885  ? 21.271  20.950  90.756  1.00 31.14 ? 883  VAL B CA    1 
ATOM   15161 C C     . VAL B  1 885  ? 22.236  20.196  89.852  1.00 28.64 ? 883  VAL B C     1 
ATOM   15162 O O     . VAL B  1 885  ? 22.897  19.254  90.296  1.00 28.61 ? 883  VAL B O     1 
ATOM   15163 C CB    . VAL B  1 885  ? 22.052  21.756  91.810  1.00 35.02 ? 883  VAL B CB    1 
ATOM   15164 C CG1   . VAL B  1 885  ? 23.162  22.590  91.146  1.00 34.80 ? 883  VAL B CG1   1 
ATOM   15165 C CG2   . VAL B  1 885  ? 21.113  22.628  92.638  1.00 34.18 ? 883  VAL B CG2   1 
ATOM   15166 N N     . GLY B  1 886  ? 22.303  20.596  88.587  1.00 25.77 ? 884  GLY B N     1 
ATOM   15167 C CA    . GLY B  1 886  ? 23.210  19.974  87.660  1.00 27.26 ? 884  GLY B CA    1 
ATOM   15168 C C     . GLY B  1 886  ? 24.519  20.725  87.543  1.00 27.70 ? 884  GLY B C     1 
ATOM   15169 O O     . GLY B  1 886  ? 24.894  21.533  88.400  1.00 26.38 ? 884  GLY B O     1 
ATOM   15170 N N     . PRO B  1 887  ? 25.231  20.464  86.456  1.00 29.19 ? 885  PRO B N     1 
ATOM   15171 C CA    . PRO B  1 887  ? 26.568  21.036  86.260  1.00 26.62 ? 885  PRO B CA    1 
ATOM   15172 C C     . PRO B  1 887  ? 26.502  22.468  85.748  1.00 24.89 ? 885  PRO B C     1 
ATOM   15173 O O     . PRO B  1 887  ? 25.467  22.927  85.275  1.00 23.36 ? 885  PRO B O     1 
ATOM   15174 C CB    . PRO B  1 887  ? 27.158  20.120  85.190  1.00 25.27 ? 885  PRO B CB    1 
ATOM   15175 C CG    . PRO B  1 887  ? 25.933  19.713  84.372  1.00 28.49 ? 885  PRO B CG    1 
ATOM   15176 C CD    . PRO B  1 887  ? 24.863  19.507  85.396  1.00 28.03 ? 885  PRO B CD    1 
ATOM   15177 N N     . VAL B  1 888  ? 27.653  23.158  85.800  1.00 24.84 ? 886  VAL B N     1 
ATOM   15178 C CA    . VAL B  1 888  ? 27.779  24.408  85.051  1.00 29.16 ? 886  VAL B CA    1 
ATOM   15179 C C     . VAL B  1 888  ? 28.208  24.059  83.631  1.00 22.97 ? 886  VAL B C     1 
ATOM   15180 O O     . VAL B  1 888  ? 28.594  22.919  83.352  1.00 24.12 ? 886  VAL B O     1 
ATOM   15181 C CB    . VAL B  1 888  ? 28.740  25.428  85.699  1.00 27.63 ? 886  VAL B CB    1 
ATOM   15182 C CG1   . VAL B  1 888  ? 28.204  25.876  87.058  1.00 27.16 ? 886  VAL B CG1   1 
ATOM   15183 C CG2   . VAL B  1 888  ? 30.170  24.902  85.794  1.00 24.86 ? 886  VAL B CG2   1 
ATOM   15184 N N     . ILE B  1 889  ? 28.121  25.034  82.721  1.00 24.48 ? 887  ILE B N     1 
ATOM   15185 C CA    . ILE B  1 889  ? 28.023  24.678  81.305  1.00 24.82 ? 887  ILE B CA    1 
ATOM   15186 C C     . ILE B  1 889  ? 29.356  24.189  80.730  1.00 28.88 ? 887  ILE B C     1 
ATOM   15187 O O     . ILE B  1 889  ? 29.368  23.322  79.841  1.00 25.98 ? 887  ILE B O     1 
ATOM   15188 C CB    . ILE B  1 889  ? 27.438  25.861  80.515  1.00 23.37 ? 887  ILE B CB    1 
ATOM   15189 C CG1   . ILE B  1 889  ? 27.168  25.467  79.056  1.00 27.83 ? 887  ILE B CG1   1 
ATOM   15190 C CG2   . ILE B  1 889  ? 28.348  27.081  80.601  1.00 26.74 ? 887  ILE B CG2   1 
ATOM   15191 C CD1   . ILE B  1 889  ? 26.209  24.305  78.888  1.00 24.03 ? 887  ILE B CD1   1 
ATOM   15192 N N     . THR B  1 890  ? 30.489  24.712  81.205  1.00 27.32 ? 888  THR B N     1 
ATOM   15193 C CA    . THR B  1 890  ? 31.791  24.366  80.642  1.00 26.76 ? 888  THR B CA    1 
ATOM   15194 C C     . THR B  1 890  ? 32.861  24.406  81.722  1.00 26.99 ? 888  THR B C     1 
ATOM   15195 O O     . THR B  1 890  ? 32.667  24.978  82.795  1.00 26.15 ? 888  THR B O     1 
ATOM   15196 C CB    . THR B  1 890  ? 32.229  25.331  79.528  1.00 32.21 ? 888  THR B CB    1 
ATOM   15197 O OG1   . THR B  1 890  ? 32.297  26.657  80.067  1.00 27.83 ? 888  THR B OG1   1 
ATOM   15198 C CG2   . THR B  1 890  ? 31.257  25.286  78.318  1.00 29.40 ? 888  THR B CG2   1 
ATOM   15199 N N     . SER B  1 891  ? 34.029  23.853  81.377  1.00 29.64 ? 889  SER B N     1 
ATOM   15200 C CA    . SER B  1 891  ? 35.206  23.965  82.242  1.00 29.71 ? 889  SER B CA    1 
ATOM   15201 C C     . SER B  1 891  ? 35.594  25.416  82.446  1.00 31.78 ? 889  SER B C     1 
ATOM   15202 O O     . SER B  1 891  ? 36.010  25.803  83.543  1.00 32.29 ? 889  SER B O     1 
ATOM   15203 C CB    . SER B  1 891  ? 36.396  23.207  81.648  1.00 31.13 ? 889  SER B CB    1 
ATOM   15204 O OG    . SER B  1 891  ? 36.118  21.832  81.511  1.00 42.94 ? 889  SER B OG    1 
ATOM   15205 N N     . GLU B  1 892  ? 35.492  26.230  81.390  1.00 29.44 ? 890  GLU B N     1 
ATOM   15206 C CA    . GLU B  1 892  ? 35.878  27.635  81.504  1.00 34.79 ? 890  GLU B CA    1 
ATOM   15207 C C     . GLU B  1 892  ? 34.964  28.373  82.472  1.00 32.55 ? 890  GLU B C     1 
ATOM   15208 O O     . GLU B  1 892  ? 35.434  29.135  83.329  1.00 33.63 ? 890  GLU B O     1 
ATOM   15209 C CB    . GLU B  1 892  ? 35.862  28.302  80.127  1.00 40.88 ? 890  GLU B CB    1 
ATOM   15210 C CG    . GLU B  1 892  ? 36.078  29.809  80.162  1.00 44.83 ? 890  GLU B CG    1 
ATOM   15211 C CD    . GLU B  1 892  ? 36.045  30.442  78.778  1.00 54.66 ? 890  GLU B CD    1 
ATOM   15212 O OE1   . GLU B  1 892  ? 35.989  29.691  77.781  1.00 62.25 ? 890  GLU B OE1   1 
ATOM   15213 O OE2   . GLU B  1 892  ? 36.082  31.689  78.685  1.00 59.69 ? 890  GLU B OE2   1 
ATOM   15214 N N     . ALA B  1 893  ? 33.650  28.153  82.356  1.00 29.48 ? 891  ALA B N     1 
ATOM   15215 C CA    . ALA B  1 893  ? 32.716  28.745  83.309  1.00 29.75 ? 891  ALA B CA    1 
ATOM   15216 C C     . ALA B  1 893  ? 33.049  28.297  84.724  1.00 30.60 ? 891  ALA B C     1 
ATOM   15217 O O     . ALA B  1 893  ? 33.103  29.115  85.652  1.00 29.29 ? 891  ALA B O     1 
ATOM   15218 C CB    . ALA B  1 893  ? 31.274  28.367  82.948  1.00 26.46 ? 891  ALA B CB    1 
ATOM   15219 N N     . LYS B  1 894  ? 33.295  26.998  84.903  1.00 27.99 ? 892  LYS B N     1 
ATOM   15220 C CA    . LYS B  1 894  ? 33.640  26.485  86.225  1.00 29.30 ? 892  LYS B CA    1 
ATOM   15221 C C     . LYS B  1 894  ? 34.904  27.148  86.768  1.00 33.39 ? 892  LYS B C     1 
ATOM   15222 O O     . LYS B  1 894  ? 34.953  27.536  87.943  1.00 31.72 ? 892  LYS B O     1 
ATOM   15223 C CB    . LYS B  1 894  ? 33.817  24.967  86.179  1.00 31.05 ? 892  LYS B CB    1 
ATOM   15224 C CG    . LYS B  1 894  ? 34.348  24.394  87.490  1.00 33.59 ? 892  LYS B CG    1 
ATOM   15225 C CD    . LYS B  1 894  ? 34.523  22.889  87.426  1.00 33.91 ? 892  LYS B CD    1 
ATOM   15226 C CE    . LYS B  1 894  ? 35.050  22.348  88.753  1.00 36.96 ? 892  LYS B CE    1 
ATOM   15227 N NZ    . LYS B  1 894  ? 35.407  20.905  88.669  1.00 37.52 ? 892  LYS B NZ    1 
ATOM   15228 N N     . ASP B  1 895  ? 35.941  27.287  85.934  1.00 28.83 ? 893  ASP B N     1 
ATOM   15229 C CA    . ASP B  1 895  ? 37.164  27.920  86.420  1.00 33.33 ? 893  ASP B CA    1 
ATOM   15230 C C     . ASP B  1 895  ? 36.939  29.386  86.768  1.00 33.91 ? 893  ASP B C     1 
ATOM   15231 O O     . ASP B  1 895  ? 37.538  29.894  87.722  1.00 31.68 ? 893  ASP B O     1 
ATOM   15232 C CB    . ASP B  1 895  ? 38.282  27.779  85.381  1.00 34.12 ? 893  ASP B CB    1 
ATOM   15233 C CG    . ASP B  1 895  ? 38.732  26.348  85.214  1.00 39.00 ? 893  ASP B CG    1 
ATOM   15234 O OD1   . ASP B  1 895  ? 38.565  25.569  86.181  1.00 45.00 ? 893  ASP B OD1   1 
ATOM   15235 O OD2   . ASP B  1 895  ? 39.263  26.001  84.133  1.00 43.78 ? 893  ASP B OD2   1 
ATOM   15236 N N     . ASN B  1 896  ? 36.077  30.070  86.013  1.00 28.04 ? 894  ASN B N     1 
ATOM   15237 C CA    . ASN B  1 896  ? 35.806  31.478  86.265  1.00 31.61 ? 894  ASN B CA    1 
ATOM   15238 C C     . ASN B  1 896  ? 35.107  31.656  87.612  1.00 34.55 ? 894  ASN B C     1 
ATOM   15239 O O     . ASN B  1 896  ? 35.469  32.543  88.400  1.00 32.16 ? 894  ASN B O     1 
ATOM   15240 C CB    . ASN B  1 896  ? 34.974  32.028  85.097  1.00 36.43 ? 894  ASN B CB    1 
ATOM   15241 C CG    . ASN B  1 896  ? 34.564  33.495  85.265  1.00 44.05 ? 894  ASN B CG    1 
ATOM   15242 O OD1   . ASN B  1 896  ? 33.987  33.891  86.273  1.00 44.55 ? 894  ASN B OD1   1 
ATOM   15243 N ND2   . ASN B  1 896  ? 34.832  34.295  84.239  1.00 52.45 ? 894  ASN B ND2   1 
ATOM   15244 N N     . ILE B  1 897  ? 34.130  30.790  87.900  1.00 30.30 ? 895  ILE B N     1 
ATOM   15245 C CA    . ILE B  1 897  ? 33.407  30.834  89.166  1.00 32.62 ? 895  ILE B CA    1 
ATOM   15246 C C     . ILE B  1 897  ? 34.351  30.545  90.330  1.00 35.52 ? 895  ILE B C     1 
ATOM   15247 O O     . ILE B  1 897  ? 34.377  31.274  91.331  1.00 33.23 ? 895  ILE B O     1 
ATOM   15248 C CB    . ILE B  1 897  ? 32.230  29.841  89.130  1.00 26.95 ? 895  ILE B CB    1 
ATOM   15249 C CG1   . ILE B  1 897  ? 31.217  30.261  88.060  1.00 30.77 ? 895  ILE B CG1   1 
ATOM   15250 C CG2   . ILE B  1 897  ? 31.567  29.734  90.503  1.00 27.92 ? 895  ILE B CG2   1 
ATOM   15251 C CD1   . ILE B  1 897  ? 30.409  29.086  87.493  1.00 25.89 ? 895  ILE B CD1   1 
ATOM   15252 N N     . GLU B  1 898  ? 35.136  29.473  90.221  1.00 34.98 ? 896  GLU B N     1 
ATOM   15253 C CA    . GLU B  1 898  ? 36.036  29.113  91.314  1.00 35.28 ? 896  GLU B CA    1 
ATOM   15254 C C     . GLU B  1 898  ? 37.122  30.162  91.533  1.00 37.17 ? 896  GLU B C     1 
ATOM   15255 O O     . GLU B  1 898  ? 37.539  30.385  92.675  1.00 35.30 ? 896  GLU B O     1 
ATOM   15256 C CB    . GLU B  1 898  ? 36.646  27.738  91.053  1.00 40.25 ? 896  GLU B CB    1 
ATOM   15257 C CG    . GLU B  1 898  ? 35.601  26.640  91.123  1.00 39.16 ? 896  GLU B CG    1 
ATOM   15258 C CD    . GLU B  1 898  ? 36.156  25.280  90.766  1.00 44.25 ? 896  GLU B CD    1 
ATOM   15259 O OE1   . GLU B  1 898  ? 37.157  25.227  90.019  1.00 48.06 ? 896  GLU B OE1   1 
ATOM   15260 O OE2   . GLU B  1 898  ? 35.593  24.266  91.236  1.00 47.86 ? 896  GLU B OE2   1 
ATOM   15261 N N     . LYS B  1 899  ? 37.579  30.819  90.463  1.00 35.04 ? 897  LYS B N     1 
ATOM   15262 C CA    . LYS B  1 899  ? 38.518  31.927  90.616  1.00 36.10 ? 897  LYS B CA    1 
ATOM   15263 C C     . LYS B  1 899  ? 37.942  33.008  91.524  1.00 36.91 ? 897  LYS B C     1 
ATOM   15264 O O     . LYS B  1 899  ? 38.649  33.553  92.382  1.00 36.32 ? 897  LYS B O     1 
ATOM   15265 C CB    . LYS B  1 899  ? 38.864  32.498  89.241  1.00 39.43 ? 897  LYS B CB    1 
ATOM   15266 C CG    . LYS B  1 899  ? 39.726  33.754  89.237  1.00 40.94 ? 897  LYS B CG    1 
ATOM   15267 C CD    . LYS B  1 899  ? 39.854  34.274  87.804  1.00 45.33 ? 897  LYS B CD    1 
ATOM   15268 C CE    . LYS B  1 899  ? 40.462  35.673  87.725  1.00 49.10 ? 897  LYS B CE    1 
ATOM   15269 N NZ    . LYS B  1 899  ? 40.200  36.308  86.389  1.00 47.18 ? 897  LYS B NZ    1 
ATOM   15270 N N     . HIS B  1 900  ? 36.651  33.317  91.365  1.00 33.53 ? 898  HIS B N     1 
ATOM   15271 C CA    . HIS B  1 900  ? 36.005  34.279  92.255  1.00 34.85 ? 898  HIS B CA    1 
ATOM   15272 C C     . HIS B  1 900  ? 35.904  33.746  93.676  1.00 35.05 ? 898  HIS B C     1 
ATOM   15273 O O     . HIS B  1 900  ? 36.135  34.485  94.643  1.00 36.86 ? 898  HIS B O     1 
ATOM   15274 C CB    . HIS B  1 900  ? 34.614  34.622  91.742  1.00 34.31 ? 898  HIS B CB    1 
ATOM   15275 C CG    . HIS B  1 900  ? 33.764  35.319  92.752  1.00 33.66 ? 898  HIS B CG    1 
ATOM   15276 N ND1   . HIS B  1 900  ? 33.952  36.641  93.091  1.00 34.15 ? 898  HIS B ND1   1 
ATOM   15277 C CD2   . HIS B  1 900  ? 32.726  34.879  93.501  1.00 31.48 ? 898  HIS B CD2   1 
ATOM   15278 C CE1   . HIS B  1 900  ? 33.051  36.991  93.992  1.00 35.85 ? 898  HIS B CE1   1 
ATOM   15279 N NE2   . HIS B  1 900  ? 32.293  35.942  94.254  1.00 31.47 ? 898  HIS B NE2   1 
ATOM   15280 N N     . ILE B  1 901  ? 35.534  32.474  93.822  1.00 32.32 ? 899  ILE B N     1 
ATOM   15281 C CA    . ILE B  1 901  ? 35.346  31.897  95.147  1.00 33.87 ? 899  ILE B CA    1 
ATOM   15282 C C     . ILE B  1 901  ? 36.667  31.868  95.893  1.00 41.30 ? 899  ILE B C     1 
ATOM   15283 O O     . ILE B  1 901  ? 36.754  32.262  97.065  1.00 41.06 ? 899  ILE B O     1 
ATOM   15284 C CB    . ILE B  1 901  ? 34.733  30.492  95.038  1.00 34.55 ? 899  ILE B CB    1 
ATOM   15285 C CG1   . ILE B  1 901  ? 33.300  30.572  94.499  1.00 34.60 ? 899  ILE B CG1   1 
ATOM   15286 C CG2   . ILE B  1 901  ? 34.761  29.792  96.394  1.00 37.70 ? 899  ILE B CG2   1 
ATOM   15287 C CD1   . ILE B  1 901  ? 32.696  29.224  94.199  1.00 29.44 ? 899  ILE B CD1   1 
ATOM   15288 N N     . GLU B  1 902  ? 37.724  31.431  95.211  1.00 37.09 ? 900  GLU B N     1 
ATOM   15289 C CA    . GLU B  1 902  ? 39.040  31.391  95.841  1.00 40.04 ? 900  GLU B CA    1 
ATOM   15290 C C     . GLU B  1 902  ? 39.554  32.785  96.159  1.00 40.39 ? 900  GLU B C     1 
ATOM   15291 O O     . GLU B  1 902  ? 40.253  32.967  97.159  1.00 42.12 ? 900  GLU B O     1 
ATOM   15292 C CB    . GLU B  1 902  ? 40.023  30.644  94.944  1.00 41.89 ? 900  GLU B CB    1 
ATOM   15293 C CG    . GLU B  1 902  ? 39.796  29.148  94.975  1.00 43.83 ? 900  GLU B CG    1 
ATOM   15294 C CD    . GLU B  1 902  ? 39.799  28.621  96.401  1.00 51.28 ? 900  GLU B CD    1 
ATOM   15295 O OE1   . GLU B  1 902  ? 40.748  28.948  97.155  1.00 47.80 ? 900  GLU B OE1   1 
ATOM   15296 O OE2   . GLU B  1 902  ? 38.837  27.909  96.772  1.00 52.74 ? 900  GLU B OE2   1 
ATOM   15297 N N     . ARG B  1 903  ? 39.221  33.776  95.335  1.00 36.67 ? 901  ARG B N     1 
ATOM   15298 C CA    . ARG B  1 903  ? 39.592  35.146  95.659  1.00 40.13 ? 901  ARG B CA    1 
ATOM   15299 C C     . ARG B  1 903  ? 38.873  35.630  96.918  1.00 44.70 ? 901  ARG B C     1 
ATOM   15300 O O     . ARG B  1 903  ? 39.469  36.334  97.745  1.00 46.08 ? 901  ARG B O     1 
ATOM   15301 C CB    . ARG B  1 903  ? 39.301  36.058  94.470  1.00 40.80 ? 901  ARG B CB    1 
ATOM   15302 C CG    . ARG B  1 903  ? 39.761  37.481  94.673  1.00 45.79 ? 901  ARG B CG    1 
ATOM   15303 C CD    . ARG B  1 903  ? 39.674  38.288  93.393  1.00 49.85 ? 901  ARG B CD    1 
ATOM   15304 N NE    . ARG B  1 903  ? 40.126  39.654  93.626  1.00 55.60 ? 901  ARG B NE    1 
ATOM   15305 C CZ    . ARG B  1 903  ? 39.340  40.634  94.056  1.00 56.79 ? 901  ARG B CZ    1 
ATOM   15306 N NH1   . ARG B  1 903  ? 38.047  40.442  94.259  1.00 57.28 ? 901  ARG B NH1   1 
ATOM   15307 N NH2   . ARG B  1 903  ? 39.866  41.834  94.291  1.00 56.95 ? 901  ARG B NH2   1 
ATOM   15308 N N     . MET B  1 904  ? 37.601  35.249  97.088  1.00 39.41 ? 902  MET B N     1 
ATOM   15309 C CA    . MET B  1 904  ? 36.861  35.596  98.301  1.00 41.87 ? 902  MET B CA    1 
ATOM   15310 C C     . MET B  1 904  ? 37.385  34.825  99.503  1.00 46.13 ? 902  MET B C     1 
ATOM   15311 O O     . MET B  1 904  ? 37.546  35.387  100.592 1.00 47.77 ? 902  MET B O     1 
ATOM   15312 C CB    . MET B  1 904  ? 35.365  35.318  98.114  1.00 39.48 ? 902  MET B CB    1 
ATOM   15313 C CG    . MET B  1 904  ? 34.719  36.148  97.039  1.00 32.18 ? 902  MET B CG    1 
ATOM   15314 S SD    . MET B  1 904  ? 34.698  37.903  97.425  1.00 47.26 ? 902  MET B SD    1 
ATOM   15315 C CE    . MET B  1 904  ? 35.910  38.513  96.252  1.00 46.98 ? 902  MET B CE    1 
ATOM   15316 N N     . ARG B  1 905  ? 37.601  33.519  99.335  1.00 46.05 ? 903  ARG B N     1 
ATOM   15317 C CA    . ARG B  1 905  ? 38.248  32.724  100.374 1.00 49.89 ? 903  ARG B CA    1 
ATOM   15318 C C     . ARG B  1 905  ? 39.591  33.328  100.753 1.00 49.40 ? 903  ARG B C     1 
ATOM   15319 O O     . ARG B  1 905  ? 39.924  33.440  101.938 1.00 51.05 ? 903  ARG B O     1 
ATOM   15320 C CB    . ARG B  1 905  ? 38.430  31.283  99.888  1.00 48.49 ? 903  ARG B CB    1 
ATOM   15321 C CG    . ARG B  1 905  ? 37.930  30.218  100.835 1.00 49.56 ? 903  ARG B CG    1 
ATOM   15322 C CD    . ARG B  1 905  ? 38.359  28.832  100.366 1.00 46.74 ? 903  ARG B CD    1 
ATOM   15323 N NE    . ARG B  1 905  ? 37.327  28.110  99.629  1.00 45.97 ? 903  ARG B NE    1 
ATOM   15324 C CZ    . ARG B  1 905  ? 36.404  27.338  100.189 1.00 45.70 ? 903  ARG B CZ    1 
ATOM   15325 N NH1   . ARG B  1 905  ? 36.288  27.239  101.503 1.00 50.62 ? 903  ARG B NH1   1 
ATOM   15326 N NH2   . ARG B  1 905  ? 35.583  26.637  99.411  1.00 45.52 ? 903  ARG B NH2   1 
ATOM   15327 N N     . GLY B  1 906  ? 40.369  33.741  99.752  1.00 47.10 ? 904  GLY B N     1 
ATOM   15328 C CA    . GLY B  1 906  ? 41.647  34.364  100.034 1.00 49.11 ? 904  GLY B CA    1 
ATOM   15329 C C     . GLY B  1 906  ? 41.504  35.617  100.872 1.00 53.63 ? 904  GLY B C     1 
ATOM   15330 O O     . GLY B  1 906  ? 42.337  35.893  101.738 1.00 54.97 ? 904  GLY B O     1 
ATOM   15331 N N     . LEU B  1 907  ? 40.440  36.386  100.640 1.00 52.22 ? 905  LEU B N     1 
ATOM   15332 C CA    . LEU B  1 907  ? 40.224  37.608  101.405 1.00 50.10 ? 905  LEU B CA    1 
ATOM   15333 C C     . LEU B  1 907  ? 39.643  37.345  102.792 1.00 50.20 ? 905  LEU B C     1 
ATOM   15334 O O     . LEU B  1 907  ? 39.374  38.302  103.522 1.00 53.22 ? 905  LEU B O     1 
ATOM   15335 C CB    . LEU B  1 907  ? 39.317  38.560  100.625 1.00 45.88 ? 905  LEU B CB    1 
ATOM   15336 N N     . GLY B  1 908  ? 39.439  36.086  103.175 1.00 49.85 ? 906  GLY B N     1 
ATOM   15337 C CA    . GLY B  1 908  ? 39.021  35.759  104.520 1.00 49.03 ? 906  GLY B CA    1 
ATOM   15338 C C     . GLY B  1 908  ? 37.528  35.670  104.746 1.00 52.15 ? 906  GLY B C     1 
ATOM   15339 O O     . GLY B  1 908  ? 37.108  35.459  105.892 1.00 51.89 ? 906  GLY B O     1 
ATOM   15340 N N     . ARG B  1 909  ? 36.712  35.816  103.701 1.00 49.25 ? 907  ARG B N     1 
ATOM   15341 C CA    . ARG B  1 909  ? 35.264  35.776  103.865 1.00 44.33 ? 907  ARG B CA    1 
ATOM   15342 C C     . ARG B  1 909  ? 34.800  34.359  104.173 1.00 47.05 ? 907  ARG B C     1 
ATOM   15343 O O     . ARG B  1 909  ? 35.369  33.383  103.677 1.00 53.55 ? 907  ARG B O     1 
ATOM   15344 C CB    . ARG B  1 909  ? 34.579  36.299  102.602 1.00 46.70 ? 907  ARG B CB    1 
ATOM   15345 N N     . LYS B  1 910  ? 33.773  34.240  105.012 1.00 44.86 ? 908  LYS B N     1 
ATOM   15346 C CA    . LYS B  1 910  ? 33.223  32.926  105.322 1.00 46.66 ? 908  LYS B CA    1 
ATOM   15347 C C     . LYS B  1 910  ? 32.586  32.318  104.077 1.00 48.52 ? 908  LYS B C     1 
ATOM   15348 O O     . LYS B  1 910  ? 31.860  32.994  103.343 1.00 48.39 ? 908  LYS B O     1 
ATOM   15349 C CB    . LYS B  1 910  ? 32.198  33.025  106.451 1.00 47.99 ? 908  LYS B CB    1 
ATOM   15350 N N     . VAL B  1 911  ? 32.868  31.033  103.838 1.00 48.48 ? 909  VAL B N     1 
ATOM   15351 C CA    . VAL B  1 911  ? 32.454  30.333  102.621 1.00 46.92 ? 909  VAL B CA    1 
ATOM   15352 C C     . VAL B  1 911  ? 31.935  28.951  102.995 1.00 44.57 ? 909  VAL B C     1 
ATOM   15353 O O     . VAL B  1 911  ? 32.697  28.111  103.482 1.00 51.69 ? 909  VAL B O     1 
ATOM   15354 C CB    . VAL B  1 911  ? 33.605  30.195  101.609 1.00 47.73 ? 909  VAL B CB    1 
ATOM   15355 C CG1   . VAL B  1 911  ? 33.146  29.389  100.397 1.00 42.72 ? 909  VAL B CG1   1 
ATOM   15356 C CG2   . VAL B  1 911  ? 34.128  31.554  101.188 1.00 43.19 ? 909  VAL B CG2   1 
ATOM   15357 N N     . GLU B  1 912  ? 30.654  28.706  102.753 1.00 43.65 ? 910  GLU B N     1 
ATOM   15358 C CA    . GLU B  1 912  ? 30.040  27.400  102.946 1.00 43.37 ? 910  GLU B CA    1 
ATOM   15359 C C     . GLU B  1 912  ? 29.816  26.748  101.585 1.00 45.57 ? 910  GLU B C     1 
ATOM   15360 O O     . GLU B  1 912  ? 29.419  27.423  100.627 1.00 39.25 ? 910  GLU B O     1 
ATOM   15361 C CB    . GLU B  1 912  ? 28.712  27.538  103.702 1.00 46.63 ? 910  GLU B CB    1 
ATOM   15362 C CG    . GLU B  1 912  ? 27.946  26.233  103.953 1.00 46.85 ? 910  GLU B CG    1 
ATOM   15363 C CD    . GLU B  1 912  ? 28.220  25.640  105.335 1.00 48.01 ? 910  GLU B CD    1 
ATOM   15364 O OE1   . GLU B  1 912  ? 28.895  26.304  106.155 1.00 46.59 ? 910  GLU B OE1   1 
ATOM   15365 O OE2   . GLU B  1 912  ? 27.763  24.505  105.597 1.00 48.14 ? 910  GLU B OE2   1 
ATOM   15366 N N     . GLN B  1 913  ? 30.075  25.437  101.495 1.00 40.82 ? 911  GLN B N     1 
ATOM   15367 C CA    . GLN B  1 913  ? 29.853  24.697  100.259 1.00 42.40 ? 911  GLN B CA    1 
ATOM   15368 C C     . GLN B  1 913  ? 29.302  23.309  100.545 1.00 46.54 ? 911  GLN B C     1 
ATOM   15369 O O     . GLN B  1 913  ? 29.717  22.649  101.502 1.00 47.68 ? 911  GLN B O     1 
ATOM   15370 C CB    . GLN B  1 913  ? 31.142  24.565  99.435  1.00 40.97 ? 911  GLN B CB    1 
ATOM   15371 C CG    . GLN B  1 913  ? 31.618  25.862  98.810  1.00 38.19 ? 911  GLN B CG    1 
ATOM   15372 C CD    . GLN B  1 913  ? 32.752  25.653  97.826  1.00 43.33 ? 911  GLN B CD    1 
ATOM   15373 O OE1   . GLN B  1 913  ? 33.751  24.997  98.137  1.00 45.06 ? 911  GLN B OE1   1 
ATOM   15374 N NE2   . GLN B  1 913  ? 32.602  26.204  96.626  1.00 35.54 ? 911  GLN B NE2   1 
ATOM   15375 N N     . ILE B  1 914  ? 28.373  22.867  99.692  1.00 43.42 ? 912  ILE B N     1 
ATOM   15376 C CA    . ILE B  1 914  ? 27.927  21.480  99.707  1.00 44.19 ? 912  ILE B CA    1 
ATOM   15377 C C     . ILE B  1 914  ? 29.046  20.564  99.203  1.00 51.73 ? 912  ILE B C     1 
ATOM   15378 O O     . ILE B  1 914  ? 29.897  20.960  98.392  1.00 47.70 ? 912  ILE B O     1 
ATOM   15379 C CB    . ILE B  1 914  ? 26.652  21.322  98.857  1.00 44.33 ? 912  ILE B CB    1 
ATOM   15380 N N     . GLY B  1 915  ? 29.053  19.326  99.692  1.00 51.07 ? 913  GLY B N     1 
ATOM   15381 C CA    . GLY B  1 915  ? 30.009  18.342  99.204  1.00 48.47 ? 913  GLY B CA    1 
ATOM   15382 C C     . GLY B  1 915  ? 29.550  17.744  97.882  1.00 50.20 ? 913  GLY B C     1 
ATOM   15383 O O     . GLY B  1 915  ? 28.360  17.530  97.651  1.00 55.61 ? 913  GLY B O     1 
ATOM   15384 N N     . LEU B  1 916  ? 30.512  17.488  96.999  1.00 46.53 ? 914  LEU B N     1 
ATOM   15385 C CA    . LEU B  1 916  ? 30.226  16.927  95.680  1.00 48.29 ? 914  LEU B CA    1 
ATOM   15386 C C     . LEU B  1 916  ? 30.576  15.448  95.659  1.00 49.47 ? 914  LEU B C     1 
ATOM   15387 O O     . LEU B  1 916  ? 31.667  15.061  96.089  1.00 47.12 ? 914  LEU B O     1 
ATOM   15388 C CB    . LEU B  1 916  ? 31.005  17.650  94.584  1.00 47.07 ? 914  LEU B CB    1 
ATOM   15389 C CG    . LEU B  1 916  ? 30.696  19.129  94.383  1.00 46.03 ? 914  LEU B CG    1 
ATOM   15390 C CD1   . LEU B  1 916  ? 31.578  19.703  93.279  1.00 42.97 ? 914  LEU B CD1   1 
ATOM   15391 C CD2   . LEU B  1 916  ? 29.209  19.342  94.092  1.00 41.22 ? 914  LEU B CD2   1 
ATOM   15392 N N     . ALA B  1 917  ? 29.653  14.628  95.152  1.00 45.91 ? 915  ALA B N     1 
ATOM   15393 C CA    . ALA B  1 917  ? 29.898  13.198  95.039  1.00 49.83 ? 915  ALA B CA    1 
ATOM   15394 C C     . ALA B  1 917  ? 31.016  12.923  94.036  1.00 47.03 ? 915  ALA B C     1 
ATOM   15395 O O     . ALA B  1 917  ? 31.323  13.742  93.166  1.00 46.14 ? 915  ALA B O     1 
ATOM   15396 C CB    . ALA B  1 917  ? 28.627  12.461  94.618  1.00 50.60 ? 915  ALA B CB    1 
ATOM   15397 N N     . SER B  1 918  ? 31.631  11.746  94.173  1.00 51.89 ? 916  SER B N     1 
ATOM   15398 C CA    . SER B  1 918  ? 32.733  11.382  93.286  1.00 53.28 ? 916  SER B CA    1 
ATOM   15399 C C     . SER B  1 918  ? 32.282  11.362  91.830  1.00 50.06 ? 916  SER B C     1 
ATOM   15400 O O     . SER B  1 918  ? 33.033  11.772  90.935  1.00 46.97 ? 916  SER B O     1 
ATOM   15401 C CB    . SER B  1 918  ? 33.313  10.024  93.695  1.00 47.99 ? 916  SER B CB    1 
ATOM   15402 N N     . GLU B  1 919  ? 31.044  10.920  91.580  1.00 50.38 ? 917  GLU B N     1 
ATOM   15403 C CA    . GLU B  1 919  ? 30.517  10.785  90.224  1.00 50.62 ? 917  GLU B CA    1 
ATOM   15404 C C     . GLU B  1 919  ? 30.489  12.098  89.453  1.00 49.26 ? 917  GLU B C     1 
ATOM   15405 O O     . GLU B  1 919  ? 30.313  12.069  88.231  1.00 49.66 ? 917  GLU B O     1 
ATOM   15406 C CB    . GLU B  1 919  ? 29.101  10.200  90.259  1.00 48.85 ? 917  GLU B CB    1 
ATOM   15407 N N     . THR B  1 920  ? 30.644  13.239  90.120  1.00 47.84 ? 918  THR B N     1 
ATOM   15408 C CA    . THR B  1 920  ? 30.659  14.514  89.416  1.00 41.09 ? 918  THR B CA    1 
ATOM   15409 C C     . THR B  1 920  ? 31.995  14.815  88.744  1.00 43.28 ? 918  THR B C     1 
ATOM   15410 O O     . THR B  1 920  ? 32.065  15.767  87.962  1.00 38.95 ? 918  THR B O     1 
ATOM   15411 C CB    . THR B  1 920  ? 30.313  15.654  90.381  1.00 43.81 ? 918  THR B CB    1 
ATOM   15412 O OG1   . THR B  1 920  ? 31.344  15.779  91.368  1.00 40.04 ? 918  THR B OG1   1 
ATOM   15413 C CG2   . THR B  1 920  ? 28.986  15.385  91.073  1.00 40.56 ? 918  THR B CG2   1 
ATOM   15414 N N     . GLY B  1 921  ? 33.049  14.038  89.026  1.00 39.69 ? 919  GLY B N     1 
ATOM   15415 C CA    . GLY B  1 921  ? 34.358  14.308  88.451  1.00 42.79 ? 919  GLY B CA    1 
ATOM   15416 C C     . GLY B  1 921  ? 34.417  14.181  86.939  1.00 41.38 ? 919  GLY B C     1 
ATOM   15417 O O     . GLY B  1 921  ? 35.313  14.756  86.312  1.00 42.52 ? 919  GLY B O     1 
ATOM   15418 N N     . VAL B  1 922  ? 33.480  13.448  86.333  1.00 38.03 ? 920  VAL B N     1 
ATOM   15419 C CA    . VAL B  1 922  ? 33.458  13.326  84.878  1.00 38.60 ? 920  VAL B CA    1 
ATOM   15420 C C     . VAL B  1 922  ? 32.803  14.514  84.188  1.00 37.60 ? 920  VAL B C     1 
ATOM   15421 O O     . VAL B  1 922  ? 32.876  14.614  82.959  1.00 37.18 ? 920  VAL B O     1 
ATOM   15422 C CB    . VAL B  1 922  ? 32.768  12.009  84.479  1.00 38.07 ? 920  VAL B CB    1 
ATOM   15423 C CG1   . VAL B  1 922  ? 33.546  10.839  85.048  1.00 38.88 ? 920  VAL B CG1   1 
ATOM   15424 C CG2   . VAL B  1 922  ? 31.333  11.982  84.981  1.00 39.07 ? 920  VAL B CG2   1 
ATOM   15425 N N     . GLY B  1 923  ? 32.190  15.429  84.939  1.00 35.31 ? 921  GLY B N     1 
ATOM   15426 C CA    . GLY B  1 923  ? 31.556  16.608  84.366  1.00 35.16 ? 921  GLY B CA    1 
ATOM   15427 C C     . GLY B  1 923  ? 32.070  17.888  85.001  1.00 30.33 ? 921  GLY B C     1 
ATOM   15428 O O     . GLY B  1 923  ? 33.003  17.830  85.803  1.00 37.14 ? 921  GLY B O     1 
ATOM   15429 N N     . THR B  1 924  ? 31.487  19.045  84.679  1.00 29.52 ? 922  THR B N     1 
ATOM   15430 C CA    . THR B  1 924  ? 31.919  20.325  85.249  1.00 28.99 ? 922  THR B CA    1 
ATOM   15431 C C     . THR B  1 924  ? 30.883  20.801  86.265  1.00 29.57 ? 922  THR B C     1 
ATOM   15432 O O     . THR B  1 924  ? 29.875  21.411  85.898  1.00 27.65 ? 922  THR B O     1 
ATOM   15433 C CB    . THR B  1 924  ? 32.136  21.366  84.157  1.00 29.32 ? 922  THR B CB    1 
ATOM   15434 O OG1   . THR B  1 924  ? 30.953  21.477  83.363  1.00 33.28 ? 922  THR B OG1   1 
ATOM   15435 C CG2   . THR B  1 924  ? 33.298  20.959  83.257  1.00 28.52 ? 922  THR B CG2   1 
ATOM   15436 N N     . PHE B  1 925  ? 31.150  20.561  87.544  1.00 29.16 ? 923  PHE B N     1 
ATOM   15437 C CA    . PHE B  1 925  ? 30.235  20.932  88.613  1.00 29.01 ? 923  PHE B CA    1 
ATOM   15438 C C     . PHE B  1 925  ? 30.867  21.955  89.546  1.00 27.51 ? 923  PHE B C     1 
ATOM   15439 O O     . PHE B  1 925  ? 32.073  21.912  89.818  1.00 31.23 ? 923  PHE B O     1 
ATOM   15440 C CB    . PHE B  1 925  ? 29.819  19.698  89.423  1.00 32.63 ? 923  PHE B CB    1 
ATOM   15441 C CG    . PHE B  1 925  ? 28.951  18.744  88.666  1.00 30.95 ? 923  PHE B CG    1 
ATOM   15442 C CD1   . PHE B  1 925  ? 29.503  17.825  87.789  1.00 29.71 ? 923  PHE B CD1   1 
ATOM   15443 C CD2   . PHE B  1 925  ? 27.570  18.772  88.825  1.00 28.51 ? 923  PHE B CD2   1 
ATOM   15444 C CE1   . PHE B  1 925  ? 28.701  16.939  87.091  1.00 31.38 ? 923  PHE B CE1   1 
ATOM   15445 C CE2   . PHE B  1 925  ? 26.756  17.903  88.113  1.00 31.10 ? 923  PHE B CE2   1 
ATOM   15446 C CZ    . PHE B  1 925  ? 27.323  16.978  87.248  1.00 32.60 ? 923  PHE B CZ    1 
ATOM   15447 N N     . VAL B  1 926  ? 30.036  22.863  90.045  1.00 27.60 ? 924  VAL B N     1 
ATOM   15448 C CA    . VAL B  1 926  ? 30.395  23.780  91.120  1.00 26.64 ? 924  VAL B CA    1 
ATOM   15449 C C     . VAL B  1 926  ? 29.364  23.605  92.223  1.00 27.54 ? 924  VAL B C     1 
ATOM   15450 O O     . VAL B  1 926  ? 28.168  23.746  91.961  1.00 28.04 ? 924  VAL B O     1 
ATOM   15451 C CB    . VAL B  1 926  ? 30.424  25.248  90.657  1.00 26.57 ? 924  VAL B CB    1 
ATOM   15452 C CG1   . VAL B  1 926  ? 30.728  26.171  91.847  1.00 27.07 ? 924  VAL B CG1   1 
ATOM   15453 C CG2   . VAL B  1 926  ? 31.449  25.429  89.554  1.00 29.00 ? 924  VAL B CG2   1 
ATOM   15454 N N     . PRO B  1 927  ? 29.767  23.325  93.461  1.00 30.11 ? 925  PRO B N     1 
ATOM   15455 C CA    . PRO B  1 927  ? 28.783  23.128  94.512  1.00 31.06 ? 925  PRO B CA    1 
ATOM   15456 C C     . PRO B  1 927  ? 28.100  24.437  94.859  1.00 30.20 ? 925  PRO B C     1 
ATOM   15457 O O     . PRO B  1 927  ? 28.710  25.517  94.764  1.00 29.14 ? 925  PRO B O     1 
ATOM   15458 C CB    . PRO B  1 927  ? 29.621  22.604  95.691  1.00 36.35 ? 925  PRO B CB    1 
ATOM   15459 C CG    . PRO B  1 927  ? 30.982  23.167  95.461  1.00 33.05 ? 925  PRO B CG    1 
ATOM   15460 C CD    . PRO B  1 927  ? 31.151  23.195  93.958  1.00 31.04 ? 925  PRO B CD    1 
ATOM   15461 N N     . PRO B  1 928  ? 26.826  24.395  95.226  1.00 31.98 ? 926  PRO B N     1 
ATOM   15462 C CA    . PRO B  1 928  ? 26.182  25.584  95.780  1.00 31.54 ? 926  PRO B CA    1 
ATOM   15463 C C     . PRO B  1 928  ? 27.034  26.177  96.891  1.00 31.19 ? 926  PRO B C     1 
ATOM   15464 O O     . PRO B  1 928  ? 27.504  25.467  97.780  1.00 37.22 ? 926  PRO B O     1 
ATOM   15465 C CB    . PRO B  1 928  ? 24.851  25.043  96.299  1.00 30.97 ? 926  PRO B CB    1 
ATOM   15466 C CG    . PRO B  1 928  ? 24.543  23.926  95.357  1.00 36.40 ? 926  PRO B CG    1 
ATOM   15467 C CD    . PRO B  1 928  ? 25.875  23.292  95.013  1.00 30.76 ? 926  PRO B CD    1 
ATOM   15468 N N     . THR B  1 929  ? 27.262  27.486  96.809  1.00 30.44 ? 927  THR B N     1 
ATOM   15469 C CA    . THR B  1 929  ? 28.200  28.185  97.678  1.00 30.35 ? 927  THR B CA    1 
ATOM   15470 C C     . THR B  1 929  ? 27.543  29.417  98.276  1.00 31.51 ? 927  THR B C     1 
ATOM   15471 O O     . THR B  1 929  ? 26.841  30.153  97.582  1.00 32.05 ? 927  THR B O     1 
ATOM   15472 C CB    . THR B  1 929  ? 29.454  28.601  96.900  1.00 33.24 ? 927  THR B CB    1 
ATOM   15473 O OG1   . THR B  1 929  ? 30.053  27.433  96.332  1.00 31.49 ? 927  THR B OG1   1 
ATOM   15474 C CG2   . THR B  1 929  ? 30.470  29.295  97.815  1.00 34.01 ? 927  THR B CG2   1 
ATOM   15475 N N     . ILE B  1 930  ? 27.787  29.647  99.562  1.00 37.61 ? 928  ILE B N     1 
ATOM   15476 C CA    . ILE B  1 930  ? 27.363  30.859  100.255 1.00 32.04 ? 928  ILE B CA    1 
ATOM   15477 C C     . ILE B  1 930  ? 28.608  31.610  100.699 1.00 36.10 ? 928  ILE B C     1 
ATOM   15478 O O     . ILE B  1 930  ? 29.511  31.021  101.305 1.00 39.96 ? 928  ILE B O     1 
ATOM   15479 C CB    . ILE B  1 930  ? 26.470  30.537  101.468 1.00 34.53 ? 928  ILE B CB    1 
ATOM   15480 C CG1   . ILE B  1 930  ? 25.247  29.729  101.032 1.00 36.29 ? 928  ILE B CG1   1 
ATOM   15481 C CG2   . ILE B  1 930  ? 26.107  31.834  102.206 1.00 32.60 ? 928  ILE B CG2   1 
ATOM   15482 C CD1   . ILE B  1 930  ? 24.323  29.329  102.153 1.00 34.66 ? 928  ILE B CD1   1 
ATOM   15483 N N     . ILE B  1 931  ? 28.666  32.901  100.390 1.00 34.33 ? 929  ILE B N     1 
ATOM   15484 C CA    . ILE B  1 931  ? 29.792  33.749  100.758 1.00 35.54 ? 929  ILE B CA    1 
ATOM   15485 C C     . ILE B  1 931  ? 29.243  34.966  101.493 1.00 38.31 ? 929  ILE B C     1 
ATOM   15486 O O     . ILE B  1 931  ? 28.396  35.690  100.959 1.00 33.58 ? 929  ILE B O     1 
ATOM   15487 C CB    . ILE B  1 931  ? 30.612  34.188  99.534  1.00 33.95 ? 929  ILE B CB    1 
ATOM   15488 C CG1   . ILE B  1 931  ? 31.168  32.970  98.788  1.00 35.83 ? 929  ILE B CG1   1 
ATOM   15489 C CG2   . ILE B  1 931  ? 31.741  35.137  99.938  1.00 33.45 ? 929  ILE B CG2   1 
ATOM   15490 C CD1   . ILE B  1 931  ? 31.914  33.342  97.530  1.00 34.23 ? 929  ILE B CD1   1 
ATOM   15491 N N     . GLU B  1 932  ? 29.727  35.203  102.706 1.00 39.80 ? 930  GLU B N     1 
ATOM   15492 C CA    . GLU B  1 932  ? 29.252  36.333  103.493 1.00 39.39 ? 930  GLU B CA    1 
ATOM   15493 C C     . GLU B  1 932  ? 30.174  37.522  103.270 1.00 35.85 ? 930  GLU B C     1 
ATOM   15494 O O     . GLU B  1 932  ? 31.394  37.405  103.421 1.00 39.92 ? 930  GLU B O     1 
ATOM   15495 C CB    . GLU B  1 932  ? 29.158  35.948  104.972 1.00 41.89 ? 930  GLU B CB    1 
ATOM   15496 C CG    . GLU B  1 932  ? 28.202  34.770  105.162 1.00 44.74 ? 930  GLU B CG    1 
ATOM   15497 C CD    . GLU B  1 932  ? 28.008  34.356  106.605 1.00 53.14 ? 930  GLU B CD    1 
ATOM   15498 O OE1   . GLU B  1 932  ? 27.965  35.245  107.483 1.00 56.27 ? 930  GLU B OE1   1 
ATOM   15499 O OE2   . GLU B  1 932  ? 27.893  33.133  106.855 1.00 52.82 ? 930  GLU B OE2   1 
ATOM   15500 N N     . LEU B  1 933  ? 29.589  38.650  102.870 1.00 34.04 ? 931  LEU B N     1 
ATOM   15501 C CA    . LEU B  1 933  ? 30.325  39.866  102.565 1.00 37.43 ? 931  LEU B CA    1 
ATOM   15502 C C     . LEU B  1 933  ? 30.072  40.917  103.639 1.00 41.43 ? 931  LEU B C     1 
ATOM   15503 O O     . LEU B  1 933  ? 29.086  40.863  104.372 1.00 41.61 ? 931  LEU B O     1 
ATOM   15504 C CB    . LEU B  1 933  ? 29.925  40.431  101.194 1.00 38.35 ? 931  LEU B CB    1 
ATOM   15505 C CG    . LEU B  1 933  ? 29.971  39.519  99.960  1.00 35.66 ? 931  LEU B CG    1 
ATOM   15506 C CD1   . LEU B  1 933  ? 29.562  40.305  98.725  1.00 34.95 ? 931  LEU B CD1   1 
ATOM   15507 C CD2   . LEU B  1 933  ? 31.360  38.920  99.776  1.00 40.39 ? 931  LEU B CD2   1 
ATOM   15508 N N     . GLU B  1 934  ? 30.974  41.892  103.709 1.00 44.97 ? 932  GLU B N     1 
ATOM   15509 C CA    . GLU B  1 934  ? 30.789  43.009  104.628 1.00 43.28 ? 932  GLU B CA    1 
ATOM   15510 C C     . GLU B  1 934  ? 29.900  44.075  104.013 1.00 48.03 ? 932  GLU B C     1 
ATOM   15511 O O     . GLU B  1 934  ? 28.969  44.564  104.659 1.00 53.82 ? 932  GLU B O     1 
ATOM   15512 C CB    . GLU B  1 934  ? 32.144  43.606  105.021 1.00 47.61 ? 932  GLU B CB    1 
ATOM   15513 N N     . LYS B  1 935  ? 30.173  44.443  102.763 1.00 44.20 ? 933  LYS B N     1 
ATOM   15514 C CA    . LYS B  1 935  ? 29.387  45.422  102.033 1.00 45.73 ? 933  LYS B CA    1 
ATOM   15515 C C     . LYS B  1 935  ? 29.078  44.871  100.649 1.00 44.93 ? 933  LYS B C     1 
ATOM   15516 O O     . LYS B  1 935  ? 29.792  44.012  100.125 1.00 40.16 ? 933  LYS B O     1 
ATOM   15517 C CB    . LYS B  1 935  ? 30.123  46.764  101.911 1.00 42.58 ? 933  LYS B CB    1 
ATOM   15518 N N     . LEU B  1 936  ? 27.995  45.382  100.063 1.00 40.87 ? 934  LEU B N     1 
ATOM   15519 C CA    . LEU B  1 936  ? 27.615  44.974  98.717  1.00 43.79 ? 934  LEU B CA    1 
ATOM   15520 C C     . LEU B  1 936  ? 28.727  45.278  97.717  1.00 47.33 ? 934  LEU B C     1 
ATOM   15521 O O     . LEU B  1 936  ? 29.022  44.460  96.836  1.00 44.28 ? 934  LEU B O     1 
ATOM   15522 C CB    . LEU B  1 936  ? 26.311  45.673  98.323  1.00 45.59 ? 934  LEU B CB    1 
ATOM   15523 C CG    . LEU B  1 936  ? 25.421  45.030  97.264  1.00 42.37 ? 934  LEU B CG    1 
ATOM   15524 C CD1   . LEU B  1 936  ? 25.905  43.647  96.938  1.00 46.62 ? 934  LEU B CD1   1 
ATOM   15525 C CD2   . LEU B  1 936  ? 23.982  44.982  97.741  1.00 42.13 ? 934  LEU B CD2   1 
ATOM   15526 N N     . SER B  1 937  ? 29.382  46.434  97.859  1.00 44.59 ? 935  SER B N     1 
ATOM   15527 C CA    . SER B  1 937  ? 30.429  46.824  96.920  1.00 46.13 ? 935  SER B CA    1 
ATOM   15528 C C     . SER B  1 937  ? 31.656  45.916  96.979  1.00 45.62 ? 935  SER B C     1 
ATOM   15529 O O     . SER B  1 937  ? 32.569  46.092  96.163  1.00 46.74 ? 935  SER B O     1 
ATOM   15530 C CB    . SER B  1 937  ? 30.833  48.279  97.167  1.00 42.80 ? 935  SER B CB    1 
ATOM   15531 O OG    . SER B  1 937  ? 31.267  48.466  98.500  1.00 47.67 ? 935  SER B OG    1 
ATOM   15532 N N     . ASP B  1 938  ? 31.705  44.955  97.908  1.00 42.86 ? 936  ASP B N     1 
ATOM   15533 C CA    . ASP B  1 938  ? 32.748  43.931  97.871  1.00 44.82 ? 936  ASP B CA    1 
ATOM   15534 C C     . ASP B  1 938  ? 32.599  42.996  96.674  1.00 48.57 ? 936  ASP B C     1 
ATOM   15535 O O     . ASP B  1 938  ? 33.577  42.350  96.279  1.00 44.03 ? 936  ASP B O     1 
ATOM   15536 C CB    . ASP B  1 938  ? 32.740  43.108  99.160  1.00 43.99 ? 936  ASP B CB    1 
ATOM   15537 C CG    . ASP B  1 938  ? 33.080  43.940  100.391 1.00 50.38 ? 936  ASP B CG    1 
ATOM   15538 O OD1   . ASP B  1 938  ? 33.765  44.981  100.246 1.00 45.00 ? 936  ASP B OD1   1 
ATOM   15539 O OD2   . ASP B  1 938  ? 32.663  43.545  101.506 1.00 49.17 ? 936  ASP B OD2   1 
ATOM   15540 N N     . LEU B  1 939  ? 31.399  42.904  96.102  1.00 42.81 ? 937  LEU B N     1 
ATOM   15541 C CA    . LEU B  1 939  ? 31.149  42.124  94.895  1.00 44.40 ? 937  LEU B CA    1 
ATOM   15542 C C     . LEU B  1 939  ? 31.378  43.046  93.702  1.00 45.42 ? 937  LEU B C     1 
ATOM   15543 O O     . LEU B  1 939  ? 30.613  43.991  93.487  1.00 49.31 ? 937  LEU B O     1 
ATOM   15544 C CB    . LEU B  1 939  ? 29.726  41.564  94.914  1.00 40.90 ? 937  LEU B CB    1 
ATOM   15545 C CG    . LEU B  1 939  ? 29.326  40.545  93.843  1.00 41.52 ? 937  LEU B CG    1 
ATOM   15546 C CD1   . LEU B  1 939  ? 30.223  39.311  93.912  1.00 38.93 ? 937  LEU B CD1   1 
ATOM   15547 C CD2   . LEU B  1 939  ? 27.857  40.154  93.976  1.00 39.19 ? 937  LEU B CD2   1 
ATOM   15548 N N     . GLN B  1 940  ? 32.430  42.778  92.931  1.00 43.50 ? 938  GLN B N     1 
ATOM   15549 C CA    . GLN B  1 940  ? 32.900  43.702  91.907  1.00 45.55 ? 938  GLN B CA    1 
ATOM   15550 C C     . GLN B  1 940  ? 32.771  43.156  90.489  1.00 51.54 ? 938  GLN B C     1 
ATOM   15551 O O     . GLN B  1 940  ? 33.354  43.737  89.565  1.00 50.70 ? 938  GLN B O     1 
ATOM   15552 C CB    . GLN B  1 940  ? 34.354  44.091  92.186  1.00 51.25 ? 938  GLN B CB    1 
ATOM   15553 N N     . ARG B  1 941  ? 32.042  42.056  90.292  1.00 44.94 ? 939  ARG B N     1 
ATOM   15554 C CA    . ARG B  1 941  ? 31.761  41.530  88.957  1.00 46.05 ? 939  ARG B CA    1 
ATOM   15555 C C     . ARG B  1 941  ? 30.665  40.478  89.062  1.00 41.30 ? 939  ARG B C     1 
ATOM   15556 O O     . ARG B  1 941  ? 30.396  39.944  90.140  1.00 37.39 ? 939  ARG B O     1 
ATOM   15557 C CB    . ARG B  1 941  ? 33.012  40.935  88.291  1.00 46.65 ? 939  ARG B CB    1 
ATOM   15558 C CG    . ARG B  1 941  ? 33.611  39.719  88.990  1.00 44.91 ? 939  ARG B CG    1 
ATOM   15559 C CD    . ARG B  1 941  ? 34.739  39.135  88.150  1.00 45.67 ? 939  ARG B CD    1 
ATOM   15560 N NE    . ARG B  1 941  ? 35.252  37.870  88.668  1.00 44.55 ? 939  ARG B NE    1 
ATOM   15561 C CZ    . ARG B  1 941  ? 34.934  36.676  88.183  1.00 42.48 ? 939  ARG B CZ    1 
ATOM   15562 N NH1   . ARG B  1 941  ? 34.057  36.541  87.201  1.00 46.58 ? 939  ARG B NH1   1 
ATOM   15563 N NH2   . ARG B  1 941  ? 35.511  35.592  88.694  1.00 37.22 ? 939  ARG B NH2   1 
ATOM   15564 N N     . GLU B  1 942  ? 30.030  40.191  87.927  1.00 39.39 ? 940  GLU B N     1 
ATOM   15565 C CA    . GLU B  1 942  ? 29.013  39.152  87.904  1.00 41.02 ? 940  GLU B CA    1 
ATOM   15566 C C     . GLU B  1 942  ? 29.677  37.781  87.986  1.00 36.50 ? 940  GLU B C     1 
ATOM   15567 O O     . GLU B  1 942  ? 30.636  37.498  87.264  1.00 40.40 ? 940  GLU B O     1 
ATOM   15568 C CB    . GLU B  1 942  ? 28.161  39.266  86.639  1.00 45.53 ? 940  GLU B CB    1 
ATOM   15569 C CG    . GLU B  1 942  ? 26.713  38.786  86.815  1.00 43.47 ? 940  GLU B CG    1 
ATOM   15570 C CD    . GLU B  1 942  ? 25.965  38.665  85.489  1.00 46.90 ? 940  GLU B CD    1 
ATOM   15571 O OE1   . GLU B  1 942  ? 26.628  38.581  84.428  1.00 50.57 ? 940  GLU B OE1   1 
ATOM   15572 O OE2   . GLU B  1 942  ? 24.715  38.657  85.505  1.00 43.85 ? 940  GLU B OE2   1 
ATOM   15573 N N     . VAL B  1 943  ? 29.181  36.936  88.886  1.00 33.98 ? 941  VAL B N     1 
ATOM   15574 C CA    . VAL B  1 943  ? 29.649  35.563  89.024  1.00 32.24 ? 941  VAL B CA    1 
ATOM   15575 C C     . VAL B  1 943  ? 28.494  34.664  88.618  1.00 31.45 ? 941  VAL B C     1 
ATOM   15576 O O     . VAL B  1 943  ? 27.518  34.504  89.363  1.00 29.19 ? 941  VAL B O     1 
ATOM   15577 C CB    . VAL B  1 943  ? 30.133  35.261  90.446  1.00 33.62 ? 941  VAL B CB    1 
ATOM   15578 C CG1   . VAL B  1 943  ? 30.636  33.825  90.540  1.00 31.48 ? 941  VAL B CG1   1 
ATOM   15579 C CG2   . VAL B  1 943  ? 31.225  36.240  90.814  1.00 35.44 ? 941  VAL B CG2   1 
ATOM   15580 N N     . PHE B  1 944  ? 28.608  34.077  87.431  1.00 26.40 ? 942  PHE B N     1 
ATOM   15581 C CA    . PHE B  1 944  ? 27.470  33.439  86.774  1.00 28.93 ? 942  PHE B CA    1 
ATOM   15582 C C     . PHE B  1 944  ? 27.432  31.952  87.124  1.00 30.36 ? 942  PHE B C     1 
ATOM   15583 O O     . PHE B  1 944  ? 27.690  31.068  86.309  1.00 27.96 ? 942  PHE B O     1 
ATOM   15584 C CB    . PHE B  1 944  ? 27.544  33.666  85.272  1.00 28.88 ? 942  PHE B CB    1 
ATOM   15585 C CG    . PHE B  1 944  ? 26.200  33.666  84.610  1.00 33.68 ? 942  PHE B CG    1 
ATOM   15586 C CD1   . PHE B  1 944  ? 25.355  34.769  84.731  1.00 31.12 ? 942  PHE B CD1   1 
ATOM   15587 C CD2   . PHE B  1 944  ? 25.766  32.566  83.897  1.00 31.88 ? 942  PHE B CD2   1 
ATOM   15588 C CE1   . PHE B  1 944  ? 24.104  34.770  84.131  1.00 33.16 ? 942  PHE B CE1   1 
ATOM   15589 C CE2   . PHE B  1 944  ? 24.506  32.571  83.283  1.00 29.38 ? 942  PHE B CE2   1 
ATOM   15590 C CZ    . PHE B  1 944  ? 23.681  33.675  83.409  1.00 28.30 ? 942  PHE B CZ    1 
ATOM   15591 N N     . GLY B  1 945  ? 27.079  31.686  88.372  1.00 26.34 ? 943  GLY B N     1 
ATOM   15592 C CA    . GLY B  1 945  ? 27.101  30.339  88.882  1.00 24.22 ? 943  GLY B CA    1 
ATOM   15593 C C     . GLY B  1 945  ? 26.404  30.253  90.215  1.00 29.68 ? 943  GLY B C     1 
ATOM   15594 O O     . GLY B  1 945  ? 25.789  31.217  90.675  1.00 27.12 ? 943  GLY B O     1 
ATOM   15595 N N     . PRO B  1 946  ? 26.477  29.092  90.862  1.00 29.02 ? 944  PRO B N     1 
ATOM   15596 C CA    . PRO B  1 946  ? 25.678  28.858  92.080  1.00 26.31 ? 944  PRO B CA    1 
ATOM   15597 C C     . PRO B  1 946  ? 26.361  29.427  93.321  1.00 25.54 ? 944  PRO B C     1 
ATOM   15598 O O     . PRO B  1 946  ? 26.783  28.708  94.230  1.00 28.88 ? 944  PRO B O     1 
ATOM   15599 C CB    . PRO B  1 946  ? 25.560  27.328  92.100  1.00 26.07 ? 944  PRO B CB    1 
ATOM   15600 C CG    . PRO B  1 946  ? 26.866  26.854  91.478  1.00 29.46 ? 944  PRO B CG    1 
ATOM   15601 C CD    . PRO B  1 946  ? 27.226  27.896  90.436  1.00 27.66 ? 944  PRO B CD    1 
ATOM   15602 N N     . VAL B  1 947  ? 26.511  30.745  93.343  1.00 24.67 ? 945  VAL B N     1 
ATOM   15603 C CA    . VAL B  1 947  ? 27.309  31.424  94.354  1.00 25.56 ? 945  VAL B CA    1 
ATOM   15604 C C     . VAL B  1 947  ? 26.454  32.529  94.949  1.00 30.88 ? 945  VAL B C     1 
ATOM   15605 O O     . VAL B  1 947  ? 26.204  33.551  94.300  1.00 27.65 ? 945  VAL B O     1 
ATOM   15606 C CB    . VAL B  1 947  ? 28.620  31.987  93.788  1.00 30.55 ? 945  VAL B CB    1 
ATOM   15607 C CG1   . VAL B  1 947  ? 29.404  32.705  94.880  1.00 30.92 ? 945  VAL B CG1   1 
ATOM   15608 C CG2   . VAL B  1 947  ? 29.469  30.856  93.212  1.00 29.84 ? 945  VAL B CG2   1 
ATOM   15609 N N     . LEU B  1 948  ? 26.011  32.331  96.178  1.00 30.06 ? 946  LEU B N     1 
ATOM   15610 C CA    . LEU B  1 948  ? 25.156  33.293  96.850  1.00 26.42 ? 946  LEU B CA    1 
ATOM   15611 C C     . LEU B  1 948  ? 25.982  34.128  97.814  1.00 27.73 ? 946  LEU B C     1 
ATOM   15612 O O     . LEU B  1 948  ? 26.649  33.581  98.693  1.00 30.45 ? 946  LEU B O     1 
ATOM   15613 C CB    . LEU B  1 948  ? 24.045  32.581  97.610  1.00 25.97 ? 946  LEU B CB    1 
ATOM   15614 C CG    . LEU B  1 948  ? 23.117  33.524  98.380  1.00 27.36 ? 946  LEU B CG    1 
ATOM   15615 C CD1   . LEU B  1 948  ? 22.339  34.397  97.399  1.00 25.20 ? 946  LEU B CD1   1 
ATOM   15616 C CD2   . LEU B  1 948  ? 22.187  32.695  99.249  1.00 26.83 ? 946  LEU B CD2   1 
ATOM   15617 N N     . HIS B  1 949  ? 25.916  35.444  97.661  1.00 28.11 ? 947  HIS B N     1 
ATOM   15618 C CA    . HIS B  1 949  ? 26.561  36.379  98.571  1.00 30.23 ? 947  HIS B CA    1 
ATOM   15619 C C     . HIS B  1 949  ? 25.537  36.867  99.585  1.00 29.09 ? 947  HIS B C     1 
ATOM   15620 O O     . HIS B  1 949  ? 24.373  37.081  99.246  1.00 27.53 ? 947  HIS B O     1 
ATOM   15621 C CB    . HIS B  1 949  ? 27.168  37.543  97.793  1.00 27.96 ? 947  HIS B CB    1 
ATOM   15622 C CG    . HIS B  1 949  ? 28.121  37.099  96.728  1.00 31.62 ? 947  HIS B CG    1 
ATOM   15623 N ND1   . HIS B  1 949  ? 27.704  36.676  95.484  1.00 29.38 ? 947  HIS B ND1   1 
ATOM   15624 C CD2   . HIS B  1 949  ? 29.469  36.965  96.740  1.00 33.04 ? 947  HIS B CD2   1 
ATOM   15625 C CE1   . HIS B  1 949  ? 28.756  36.311  94.770  1.00 29.08 ? 947  HIS B CE1   1 
ATOM   15626 N NE2   . HIS B  1 949  ? 29.839  36.476  95.508  1.00 34.27 ? 947  HIS B NE2   1 
ATOM   15627 N N     . VAL B  1 950  ? 25.957  37.017  100.837 1.00 31.42 ? 948  VAL B N     1 
ATOM   15628 C CA    . VAL B  1 950  ? 25.035  37.383  101.908 1.00 29.22 ? 948  VAL B CA    1 
ATOM   15629 C C     . VAL B  1 950  ? 25.590  38.591  102.641 1.00 28.09 ? 948  VAL B C     1 
ATOM   15630 O O     . VAL B  1 950  ? 26.770  38.607  103.021 1.00 30.22 ? 948  VAL B O     1 
ATOM   15631 C CB    . VAL B  1 950  ? 24.801  36.223  102.894 1.00 30.77 ? 948  VAL B CB    1 
ATOM   15632 C CG1   . VAL B  1 950  ? 23.918  36.693  104.054 1.00 29.88 ? 948  VAL B CG1   1 
ATOM   15633 C CG2   . VAL B  1 950  ? 24.154  35.050  102.198 1.00 31.17 ? 948  VAL B CG2   1 
ATOM   15634 N N     . ILE B  1 951  ? 24.751  39.609  102.824 1.00 25.56 ? 949  ILE B N     1 
ATOM   15635 C CA    . ILE B  1 951  ? 25.108  40.759  103.640 1.00 27.56 ? 949  ILE B CA    1 
ATOM   15636 C C     . ILE B  1 951  ? 24.014  40.992  104.669 1.00 28.26 ? 949  ILE B C     1 
ATOM   15637 O O     . ILE B  1 951  ? 22.849  40.623  104.469 1.00 26.20 ? 949  ILE B O     1 
ATOM   15638 C CB    . ILE B  1 951  ? 25.340  42.038  102.806 1.00 34.71 ? 949  ILE B CB    1 
ATOM   15639 C CG1   . ILE B  1 951  ? 24.087  42.417  102.047 1.00 30.06 ? 949  ILE B CG1   1 
ATOM   15640 C CG2   . ILE B  1 951  ? 26.527  41.881  101.857 1.00 37.71 ? 949  ILE B CG2   1 
ATOM   15641 C CD1   . ILE B  1 951  ? 24.283  43.639  101.173 1.00 40.62 ? 949  ILE B CD1   1 
ATOM   15642 N N     . ARG B  1 952  ? 24.409  41.596  105.785 1.00 24.87 ? 950  ARG B N     1 
ATOM   15643 C CA    . ARG B  1 952  ? 23.528  41.924  106.898 1.00 28.02 ? 950  ARG B CA    1 
ATOM   15644 C C     . ARG B  1 952  ? 23.352  43.435  106.958 1.00 27.70 ? 950  ARG B C     1 
ATOM   15645 O O     . ARG B  1 952  ? 24.291  44.191  106.679 1.00 29.80 ? 950  ARG B O     1 
ATOM   15646 C CB    . ARG B  1 952  ? 24.113  41.402  108.225 1.00 26.15 ? 950  ARG B CB    1 
ATOM   15647 C CG    . ARG B  1 952  ? 24.607  39.961  108.115 1.00 33.35 ? 950  ARG B CG    1 
ATOM   15648 C CD    . ARG B  1 952  ? 25.666  39.605  109.143 1.00 38.45 ? 950  ARG B CD    1 
ATOM   15649 N NE    . ARG B  1 952  ? 25.101  39.413  110.472 1.00 42.97 ? 950  ARG B NE    1 
ATOM   15650 C CZ    . ARG B  1 952  ? 24.862  38.232  111.031 1.00 37.77 ? 950  ARG B CZ    1 
ATOM   15651 N NH1   . ARG B  1 952  ? 25.106  37.096  110.390 1.00 35.44 ? 950  ARG B NH1   1 
ATOM   15652 N NH2   . ARG B  1 952  ? 24.363  38.191  112.266 1.00 38.03 ? 950  ARG B NH2   1 
ATOM   15653 N N     . TYR B  1 953  ? 22.152  43.884  107.312 1.00 26.54 ? 951  TYR B N     1 
ATOM   15654 C CA    . TYR B  1 953  ? 21.900  45.316  107.385 1.00 24.90 ? 951  TYR B CA    1 
ATOM   15655 C C     . TYR B  1 953  ? 21.064  45.632  108.619 1.00 26.04 ? 951  TYR B C     1 
ATOM   15656 O O     . TYR B  1 953  ? 20.288  44.803  109.090 1.00 24.16 ? 951  TYR B O     1 
ATOM   15657 C CB    . TYR B  1 953  ? 21.206  45.816  106.115 1.00 26.78 ? 951  TYR B CB    1 
ATOM   15658 C CG    . TYR B  1 953  ? 19.759  45.402  105.999 1.00 25.27 ? 951  TYR B CG    1 
ATOM   15659 C CD1   . TYR B  1 953  ? 19.396  44.172  105.445 1.00 24.10 ? 951  TYR B CD1   1 
ATOM   15660 C CD2   . TYR B  1 953  ? 18.751  46.243  106.439 1.00 24.26 ? 951  TYR B CD2   1 
ATOM   15661 C CE1   . TYR B  1 953  ? 18.065  43.810  105.346 1.00 25.14 ? 951  TYR B CE1   1 
ATOM   15662 C CE2   . TYR B  1 953  ? 17.432  45.883  106.351 1.00 24.57 ? 951  TYR B CE2   1 
ATOM   15663 C CZ    . TYR B  1 953  ? 17.090  44.668  105.797 1.00 24.22 ? 951  TYR B CZ    1 
ATOM   15664 O OH    . TYR B  1 953  ? 15.754  44.335  105.721 1.00 24.44 ? 951  TYR B OH    1 
ATOM   15665 N N     . ARG B  1 954  ? 21.246  46.839  109.152 1.00 28.62 ? 952  ARG B N     1 
ATOM   15666 C CA    . ARG B  1 954  ? 20.418  47.331  110.243 1.00 29.64 ? 952  ARG B CA    1 
ATOM   15667 C C     . ARG B  1 954  ? 19.160  47.946  109.646 1.00 31.23 ? 952  ARG B C     1 
ATOM   15668 O O     . ARG B  1 954  ? 19.216  48.565  108.579 1.00 27.63 ? 952  ARG B O     1 
ATOM   15669 C CB    . ARG B  1 954  ? 21.186  48.358  111.084 1.00 34.52 ? 952  ARG B CB    1 
ATOM   15670 N N     . ARG B  1 955  ? 18.013  47.742  110.310 1.00 30.94 ? 953  ARG B N     1 
ATOM   15671 C CA    . ARG B  1 955  ? 16.757  48.196  109.708 1.00 33.15 ? 953  ARG B CA    1 
ATOM   15672 C C     . ARG B  1 955  ? 16.789  49.690  109.405 1.00 34.49 ? 953  ARG B C     1 
ATOM   15673 O O     . ARG B  1 955  ? 16.217  50.135  108.396 1.00 31.85 ? 953  ARG B O     1 
ATOM   15674 C CB    . ARG B  1 955  ? 15.570  47.857  110.613 1.00 32.36 ? 953  ARG B CB    1 
ATOM   15675 C CG    . ARG B  1 955  ? 14.213  48.360  110.093 1.00 40.19 ? 953  ARG B CG    1 
ATOM   15676 C CD    . ARG B  1 955  ? 13.966  47.994  108.620 1.00 39.47 ? 953  ARG B CD    1 
ATOM   15677 N NE    . ARG B  1 955  ? 12.654  48.413  108.135 1.00 45.94 ? 953  ARG B NE    1 
ATOM   15678 C CZ    . ARG B  1 955  ? 12.357  49.632  107.697 1.00 48.16 ? 953  ARG B CZ    1 
ATOM   15679 N NH1   . ARG B  1 955  ? 13.260  50.604  107.683 1.00 43.05 ? 953  ARG B NH1   1 
ATOM   15680 N NH2   . ARG B  1 955  ? 11.122  49.882  107.263 1.00 43.79 ? 953  ARG B NH2   1 
ATOM   15681 N N     . ASP B  1 956  ? 17.477  50.471  110.242 1.00 32.67 ? 954  ASP B N     1 
ATOM   15682 C CA    . ASP B  1 956  ? 17.591  51.910  110.016 1.00 39.69 ? 954  ASP B CA    1 
ATOM   15683 C C     . ASP B  1 956  ? 18.277  52.247  108.699 1.00 38.31 ? 954  ASP B C     1 
ATOM   15684 O O     . ASP B  1 956  ? 18.078  53.346  108.169 1.00 38.12 ? 954  ASP B O     1 
ATOM   15685 C CB    . ASP B  1 956  ? 18.363  52.564  111.164 1.00 42.09 ? 954  ASP B CB    1 
ATOM   15686 C CG    . ASP B  1 956  ? 17.554  52.631  112.439 1.00 48.72 ? 954  ASP B CG    1 
ATOM   15687 O OD1   . ASP B  1 956  ? 16.337  52.353  112.370 1.00 48.53 ? 954  ASP B OD1   1 
ATOM   15688 O OD2   . ASP B  1 956  ? 18.131  52.950  113.503 1.00 52.49 ? 954  ASP B OD2   1 
ATOM   15689 N N     . ASP B  1 957  ? 19.092  51.340  108.174 1.00 34.20 ? 955  ASP B N     1 
ATOM   15690 C CA    . ASP B  1 957  ? 19.883  51.594  106.978 1.00 34.32 ? 955  ASP B CA    1 
ATOM   15691 C C     . ASP B  1 957  ? 19.227  51.043  105.720 1.00 28.41 ? 955  ASP B C     1 
ATOM   15692 O O     . ASP B  1 957  ? 19.885  50.964  104.678 1.00 29.59 ? 955  ASP B O     1 
ATOM   15693 C CB    . ASP B  1 957  ? 21.284  50.998  107.135 1.00 32.24 ? 955  ASP B CB    1 
ATOM   15694 C CG    . ASP B  1 957  ? 22.098  51.697  108.205 1.00 40.56 ? 955  ASP B CG    1 
ATOM   15695 O OD1   . ASP B  1 957  ? 21.946  52.931  108.358 1.00 41.07 ? 955  ASP B OD1   1 
ATOM   15696 O OD2   . ASP B  1 957  ? 22.891  51.006  108.891 1.00 42.42 ? 955  ASP B OD2   1 
ATOM   15697 N N     . LEU B  1 958  ? 17.947  50.675  105.796 1.00 27.47 ? 956  LEU B N     1 
ATOM   15698 C CA    . LEU B  1 958  ? 17.262  50.105  104.641 1.00 26.39 ? 956  LEU B CA    1 
ATOM   15699 C C     . LEU B  1 958  ? 17.349  51.027  103.428 1.00 26.08 ? 956  LEU B C     1 
ATOM   15700 O O     . LEU B  1 958  ? 17.671  50.582  102.321 1.00 25.49 ? 956  LEU B O     1 
ATOM   15701 C CB    . LEU B  1 958  ? 15.807  49.822  105.000 1.00 28.07 ? 956  LEU B CB    1 
ATOM   15702 C CG    . LEU B  1 958  ? 14.953  49.205  103.896 1.00 28.49 ? 956  LEU B CG    1 
ATOM   15703 C CD1   . LEU B  1 958  ? 15.576  47.896  103.434 1.00 26.28 ? 956  LEU B CD1   1 
ATOM   15704 C CD2   . LEU B  1 958  ? 13.543  48.997  104.417 1.00 33.27 ? 956  LEU B CD2   1 
ATOM   15705 N N     . ASP B  1 959  ? 17.095  52.324  103.616 1.00 28.27 ? 957  ASP B N     1 
ATOM   15706 C CA    . ASP B  1 959  ? 17.118  53.217  102.465 1.00 27.27 ? 957  ASP B CA    1 
ATOM   15707 C C     . ASP B  1 959  ? 18.516  53.306  101.862 1.00 27.38 ? 957  ASP B C     1 
ATOM   15708 O O     . ASP B  1 959  ? 18.664  53.392  100.643 1.00 28.98 ? 957  ASP B O     1 
ATOM   15709 C CB    . ASP B  1 959  ? 16.599  54.606  102.836 1.00 29.18 ? 957  ASP B CB    1 
ATOM   15710 C CG    . ASP B  1 959  ? 16.249  55.429  101.610 1.00 28.05 ? 957  ASP B CG    1 
ATOM   15711 O OD1   . ASP B  1 959  ? 15.590  54.888  100.696 1.00 28.07 ? 957  ASP B OD1   1 
ATOM   15712 O OD2   . ASP B  1 959  ? 16.627  56.613  101.551 1.00 30.31 ? 957  ASP B OD2   1 
ATOM   15713 N N     . ARG B  1 960  ? 19.559  53.281  102.695 1.00 29.55 ? 958  ARG B N     1 
ATOM   15714 C CA    . ARG B  1 960  ? 20.913  53.262  102.149 1.00 26.67 ? 958  ARG B CA    1 
ATOM   15715 C C     . ARG B  1 960  ? 21.232  51.924  101.482 1.00 29.54 ? 958  ARG B C     1 
ATOM   15716 O O     . ARG B  1 960  ? 22.015  51.877  100.521 1.00 29.70 ? 958  ARG B O     1 
ATOM   15717 C CB    . ARG B  1 960  ? 21.935  53.573  103.252 1.00 28.26 ? 958  ARG B CB    1 
ATOM   15718 N N     . LEU B  1 961  ? 20.650  50.827  101.973 1.00 24.04 ? 959  LEU B N     1 
ATOM   15719 C CA    . LEU B  1 961  ? 20.878  49.540  101.318 1.00 25.65 ? 959  LEU B CA    1 
ATOM   15720 C C     . LEU B  1 961  ? 20.262  49.520  99.920  1.00 27.90 ? 959  LEU B C     1 
ATOM   15721 O O     . LEU B  1 961  ? 20.858  48.983  98.978  1.00 27.48 ? 959  LEU B O     1 
ATOM   15722 C CB    . LEU B  1 961  ? 20.314  48.400  102.172 1.00 22.94 ? 959  LEU B CB    1 
ATOM   15723 C CG    . LEU B  1 961  ? 20.347  46.990  101.552 1.00 26.45 ? 959  LEU B CG    1 
ATOM   15724 C CD1   . LEU B  1 961  ? 21.775  46.493  101.401 1.00 32.62 ? 959  LEU B CD1   1 
ATOM   15725 C CD2   . LEU B  1 961  ? 19.497  45.993  102.343 1.00 26.21 ? 959  LEU B CD2   1 
ATOM   15726 N N     . VAL B  1 962  ? 19.081  50.127  99.760  1.00 24.09 ? 960  VAL B N     1 
ATOM   15727 C CA    . VAL B  1 962  ? 18.484  50.233  98.437  1.00 25.12 ? 960  VAL B CA    1 
ATOM   15728 C C     . VAL B  1 962  ? 19.386  51.050  97.514  1.00 29.07 ? 960  VAL B C     1 
ATOM   15729 O O     . VAL B  1 962  ? 19.607  50.670  96.361  1.00 25.81 ? 960  VAL B O     1 
ATOM   15730 C CB    . VAL B  1 962  ? 17.061  50.816  98.543  1.00 28.33 ? 960  VAL B CB    1 
ATOM   15731 C CG1   . VAL B  1 962  ? 16.533  51.202  97.172  1.00 25.32 ? 960  VAL B CG1   1 
ATOM   15732 C CG2   . VAL B  1 962  ? 16.123  49.794  99.209  1.00 22.64 ? 960  VAL B CG2   1 
ATOM   15733 N N     . ASP B  1 963  ? 19.951  52.161  98.015  1.00 28.70 ? 961  ASP B N     1 
ATOM   15734 C CA    . ASP B  1 963  ? 20.979  52.895  97.267  1.00 33.18 ? 961  ASP B CA    1 
ATOM   15735 C C     . ASP B  1 963  ? 22.115  51.990  96.826  1.00 29.93 ? 961  ASP B C     1 
ATOM   15736 O O     . ASP B  1 963  ? 22.551  52.035  95.667  1.00 32.73 ? 961  ASP B O     1 
ATOM   15737 C CB    . ASP B  1 963  ? 21.570  54.025  98.106  1.00 32.94 ? 961  ASP B CB    1 
ATOM   15738 C CG    . ASP B  1 963  ? 20.647  55.175  98.244  1.00 35.65 ? 961  ASP B CG    1 
ATOM   15739 O OD1   . ASP B  1 963  ? 19.750  55.298  97.386  1.00 38.29 ? 961  ASP B OD1   1 
ATOM   15740 O OD2   . ASP B  1 963  ? 20.827  55.966  99.206  1.00 39.49 ? 961  ASP B OD2   1 
ATOM   15741 N N     . ASP B  1 964  ? 22.629  51.184  97.755  1.00 28.40 ? 962  ASP B N     1 
ATOM   15742 C CA    . ASP B  1 964  ? 23.752  50.306  97.458  1.00 30.27 ? 962  ASP B CA    1 
ATOM   15743 C C     . ASP B  1 964  ? 23.403  49.303  96.366  1.00 31.72 ? 962  ASP B C     1 
ATOM   15744 O O     . ASP B  1 964  ? 24.230  49.019  95.492  1.00 28.00 ? 962  ASP B O     1 
ATOM   15745 C CB    . ASP B  1 964  ? 24.195  49.574  98.724  1.00 31.68 ? 962  ASP B CB    1 
ATOM   15746 C CG    . ASP B  1 964  ? 24.868  50.491  99.727  1.00 36.17 ? 962  ASP B CG    1 
ATOM   15747 O OD1   . ASP B  1 964  ? 25.021  51.699  99.424  1.00 36.95 ? 962  ASP B OD1   1 
ATOM   15748 O OD2   . ASP B  1 964  ? 25.248  50.001  100.817 1.00 39.46 ? 962  ASP B OD2   1 
ATOM   15749 N N     . VAL B  1 965  ? 22.184  48.752  96.399  1.00 27.39 ? 963  VAL B N     1 
ATOM   15750 C CA    . VAL B  1 965  ? 21.773  47.827  95.346  1.00 25.99 ? 963  VAL B CA    1 
ATOM   15751 C C     . VAL B  1 965  ? 21.676  48.553  94.008  1.00 27.03 ? 963  VAL B C     1 
ATOM   15752 O O     . VAL B  1 965  ? 22.151  48.048  92.985  1.00 30.47 ? 963  VAL B O     1 
ATOM   15753 C CB    . VAL B  1 965  ? 20.450  47.126  95.720  1.00 28.91 ? 963  VAL B CB    1 
ATOM   15754 C CG1   . VAL B  1 965  ? 19.911  46.305  94.525  1.00 24.27 ? 963  VAL B CG1   1 
ATOM   15755 C CG2   . VAL B  1 965  ? 20.666  46.211  96.932  1.00 26.25 ? 963  VAL B CG2   1 
ATOM   15756 N N     . ASN B  1 966  ? 21.076  49.749  93.993  1.00 26.99 ? 964  ASN B N     1 
ATOM   15757 C CA    . ASN B  1 966  ? 20.981  50.525  92.755  1.00 29.79 ? 964  ASN B CA    1 
ATOM   15758 C C     . ASN B  1 966  ? 22.355  50.924  92.233  1.00 33.63 ? 964  ASN B C     1 
ATOM   15759 O O     . ASN B  1 966  ? 22.535  51.093  91.020  1.00 32.70 ? 964  ASN B O     1 
ATOM   15760 C CB    . ASN B  1 966  ? 20.148  51.792  92.975  1.00 31.00 ? 964  ASN B CB    1 
ATOM   15761 C CG    . ASN B  1 966  ? 18.664  51.511  93.141  1.00 30.47 ? 964  ASN B CG    1 
ATOM   15762 O OD1   . ASN B  1 966  ? 18.150  50.501  92.657  1.00 28.16 ? 964  ASN B OD1   1 
ATOM   15763 N ND2   . ASN B  1 966  ? 17.964  52.419  93.816  1.00 26.51 ? 964  ASN B ND2   1 
ATOM   15764 N N     . ALA B  1 967  ? 23.329  51.094  93.132  1.00 29.32 ? 965  ALA B N     1 
ATOM   15765 C CA    . ALA B  1 967  ? 24.613  51.671  92.759  1.00 31.00 ? 965  ALA B CA    1 
ATOM   15766 C C     . ALA B  1 967  ? 25.425  50.784  91.824  1.00 32.09 ? 965  ALA B C     1 
ATOM   15767 O O     . ALA B  1 967  ? 26.376  51.278  91.208  1.00 34.54 ? 965  ALA B O     1 
ATOM   15768 C CB    . ALA B  1 967  ? 25.441  51.963  94.014  1.00 31.98 ? 965  ALA B CB    1 
ATOM   15769 N N     . THR B  1 968  ? 25.111  49.486  91.728  1.00 31.42 ? 966  THR B N     1 
ATOM   15770 C CA    . THR B  1 968  ? 25.851  48.625  90.809  1.00 33.56 ? 966  THR B CA    1 
ATOM   15771 C C     . THR B  1 968  ? 25.615  48.993  89.350  1.00 34.66 ? 966  THR B C     1 
ATOM   15772 O O     . THR B  1 968  ? 26.389  48.568  88.484  1.00 35.22 ? 966  THR B O     1 
ATOM   15773 C CB    . THR B  1 968  ? 25.465  47.162  90.995  1.00 34.18 ? 966  THR B CB    1 
ATOM   15774 O OG1   . THR B  1 968  ? 24.172  46.944  90.398  1.00 32.86 ? 966  THR B OG1   1 
ATOM   15775 C CG2   . THR B  1 968  ? 25.413  46.806  92.473  1.00 36.19 ? 966  THR B CG2   1 
ATOM   15776 N N     . GLY B  1 969  ? 24.553  49.747  89.052  1.00 33.99 ? 967  GLY B N     1 
ATOM   15777 C CA    . GLY B  1 969  ? 24.205  50.061  87.682  1.00 32.48 ? 967  GLY B CA    1 
ATOM   15778 C C     . GLY B  1 969  ? 23.344  49.026  86.980  1.00 34.22 ? 967  GLY B C     1 
ATOM   15779 O O     . GLY B  1 969  ? 22.801  49.320  85.905  1.00 33.72 ? 967  GLY B O     1 
ATOM   15780 N N     . TYR B  1 970  ? 23.216  47.825  87.537  1.00 30.07 ? 968  TYR B N     1 
ATOM   15781 C CA    . TYR B  1 970  ? 22.306  46.831  86.993  1.00 29.74 ? 968  TYR B CA    1 
ATOM   15782 C C     . TYR B  1 970  ? 20.903  47.063  87.535  1.00 30.89 ? 968  TYR B C     1 
ATOM   15783 O O     . TYR B  1 970  ? 20.700  47.765  88.524  1.00 31.85 ? 968  TYR B O     1 
ATOM   15784 C CB    . TYR B  1 970  ? 22.753  45.418  87.358  1.00 29.15 ? 968  TYR B CB    1 
ATOM   15785 C CG    . TYR B  1 970  ? 24.091  45.016  86.796  1.00 39.16 ? 968  TYR B CG    1 
ATOM   15786 C CD1   . TYR B  1 970  ? 24.209  44.580  85.480  1.00 38.69 ? 968  TYR B CD1   1 
ATOM   15787 C CD2   . TYR B  1 970  ? 25.231  45.045  87.584  1.00 36.12 ? 968  TYR B CD2   1 
ATOM   15788 C CE1   . TYR B  1 970  ? 25.436  44.199  84.963  1.00 37.74 ? 968  TYR B CE1   1 
ATOM   15789 C CE2   . TYR B  1 970  ? 26.452  44.669  87.080  1.00 43.24 ? 968  TYR B CE2   1 
ATOM   15790 C CZ    . TYR B  1 970  ? 26.549  44.244  85.771  1.00 44.66 ? 968  TYR B CZ    1 
ATOM   15791 O OH    . TYR B  1 970  ? 27.769  43.863  85.272  1.00 50.61 ? 968  TYR B OH    1 
ATOM   15792 N N     . GLY B  1 971  ? 19.926  46.457  86.879  1.00 28.81 ? 969  GLY B N     1 
ATOM   15793 C CA    . GLY B  1 971  ? 18.572  46.592  87.364  1.00 27.07 ? 969  GLY B CA    1 
ATOM   15794 C C     . GLY B  1 971  ? 17.700  45.536  86.738  1.00 25.64 ? 969  GLY B C     1 
ATOM   15795 O O     . GLY B  1 971  ? 16.741  45.864  86.033  1.00 28.01 ? 969  GLY B O     1 
ATOM   15796 N N     . LEU B  1 972  ? 18.023  44.266  86.977  1.00 26.16 ? 970  LEU B N     1 
ATOM   15797 C CA    . LEU B  1 972  ? 17.262  43.202  86.334  1.00 25.19 ? 970  LEU B CA    1 
ATOM   15798 C C     . LEU B  1 972  ? 16.165  42.684  87.262  1.00 24.04 ? 970  LEU B C     1 
ATOM   15799 O O     . LEU B  1 972  ? 15.031  43.150  87.175  1.00 24.71 ? 970  LEU B O     1 
ATOM   15800 C CB    . LEU B  1 972  ? 18.183  42.080  85.881  1.00 25.86 ? 970  LEU B CB    1 
ATOM   15801 C CG    . LEU B  1 972  ? 17.486  41.040  84.999  1.00 24.83 ? 970  LEU B CG    1 
ATOM   15802 C CD1   . LEU B  1 972  ? 16.664  41.707  83.869  1.00 28.95 ? 970  LEU B CD1   1 
ATOM   15803 C CD2   . LEU B  1 972  ? 18.515  40.088  84.434  1.00 25.77 ? 970  LEU B CD2   1 
ATOM   15804 N N     . THR B  1 973  ? 16.459  41.722  88.135  1.00 20.07 ? 971  THR B N     1 
ATOM   15805 C CA    . THR B  1 973  ? 15.453  41.253  89.074  1.00 19.93 ? 971  THR B CA    1 
ATOM   15806 C C     . THR B  1 973  ? 15.791  41.722  90.483  1.00 20.81 ? 971  THR B C     1 
ATOM   15807 O O     . THR B  1 973  ? 16.943  42.006  90.806  1.00 19.72 ? 971  THR B O     1 
ATOM   15808 C CB    . THR B  1 973  ? 15.314  39.729  89.063  1.00 22.54 ? 971  THR B CB    1 
ATOM   15809 O OG1   . THR B  1 973  ? 16.578  39.125  89.383  1.00 21.77 ? 971  THR B OG1   1 
ATOM   15810 C CG2   . THR B  1 973  ? 14.823  39.228  87.688  1.00 23.16 ? 971  THR B CG2   1 
ATOM   15811 N N     . PHE B  1 974  ? 14.753  41.800  91.311  1.00 20.81 ? 972  PHE B N     1 
ATOM   15812 C CA    . PHE B  1 974  ? 14.902  42.229  92.695  1.00 21.66 ? 972  PHE B CA    1 
ATOM   15813 C C     . PHE B  1 974  ? 13.798  41.572  93.503  1.00 19.92 ? 972  PHE B C     1 
ATOM   15814 O O     . PHE B  1 974  ? 12.640  41.588  93.080  1.00 18.87 ? 972  PHE B O     1 
ATOM   15815 C CB    . PHE B  1 974  ? 14.803  43.748  92.834  1.00 18.04 ? 972  PHE B CB    1 
ATOM   15816 C CG    . PHE B  1 974  ? 14.728  44.199  94.249  1.00 20.71 ? 972  PHE B CG    1 
ATOM   15817 C CD1   . PHE B  1 974  ? 15.883  44.300  95.005  1.00 23.20 ? 972  PHE B CD1   1 
ATOM   15818 C CD2   . PHE B  1 974  ? 13.510  44.487  94.842  1.00 21.49 ? 972  PHE B CD2   1 
ATOM   15819 C CE1   . PHE B  1 974  ? 15.832  44.699  96.324  1.00 25.45 ? 972  PHE B CE1   1 
ATOM   15820 C CE2   . PHE B  1 974  ? 13.448  44.879  96.165  1.00 21.55 ? 972  PHE B CE2   1 
ATOM   15821 C CZ    . PHE B  1 974  ? 14.607  44.987  96.910  1.00 22.47 ? 972  PHE B CZ    1 
ATOM   15822 N N     . GLY B  1 975  ? 14.139  41.019  94.666  1.00 19.58 ? 973  GLY B N     1 
ATOM   15823 C CA    . GLY B  1 975  ? 13.156  40.398  95.533  1.00 22.58 ? 973  GLY B CA    1 
ATOM   15824 C C     . GLY B  1 975  ? 13.049  41.110  96.868  1.00 21.51 ? 973  GLY B C     1 
ATOM   15825 O O     . GLY B  1 975  ? 14.021  41.665  97.365  1.00 21.20 ? 973  GLY B O     1 
ATOM   15826 N N     . LEU B  1 976  ? 11.846  41.081  97.448  1.00 19.62 ? 974  LEU B N     1 
ATOM   15827 C CA    . LEU B  1 976  ? 11.611  41.647  98.777  1.00 21.57 ? 974  LEU B CA    1 
ATOM   15828 C C     . LEU B  1 976  ? 10.732  40.694  99.562  1.00 21.88 ? 974  LEU B C     1 
ATOM   15829 O O     . LEU B  1 976  ? 9.674   40.286  99.079  1.00 21.63 ? 974  LEU B O     1 
ATOM   15830 C CB    . LEU B  1 976  ? 10.944  43.020  98.695  1.00 22.60 ? 974  LEU B CB    1 
ATOM   15831 C CG    . LEU B  1 976  ? 10.527  43.652  100.028 1.00 22.68 ? 974  LEU B CG    1 
ATOM   15832 C CD1   . LEU B  1 976  ? 11.755  43.980  100.898 1.00 20.47 ? 974  LEU B CD1   1 
ATOM   15833 C CD2   . LEU B  1 976  ? 9.709   44.898  99.757  1.00 22.87 ? 974  LEU B CD2   1 
ATOM   15834 N N     . HIS B  1 977  ? 11.177  40.318  100.761 1.00 22.59 ? 975  HIS B N     1 
ATOM   15835 C CA    . HIS B  1 977  ? 10.393  39.459  101.640 1.00 21.11 ? 975  HIS B CA    1 
ATOM   15836 C C     . HIS B  1 977  ? 10.069  40.265  102.886 1.00 20.86 ? 975  HIS B C     1 
ATOM   15837 O O     . HIS B  1 977  ? 10.965  40.572  103.681 1.00 22.04 ? 975  HIS B O     1 
ATOM   15838 C CB    . HIS B  1 977  ? 11.143  38.170  101.988 1.00 22.03 ? 975  HIS B CB    1 
ATOM   15839 C CG    . HIS B  1 977  ? 10.889  37.064  101.018 1.00 24.83 ? 975  HIS B CG    1 
ATOM   15840 N ND1   . HIS B  1 977  ? 10.061  35.999  101.305 1.00 28.53 ? 975  HIS B ND1   1 
ATOM   15841 C CD2   . HIS B  1 977  ? 11.291  36.896  99.737  1.00 27.04 ? 975  HIS B CD2   1 
ATOM   15842 C CE1   . HIS B  1 977  ? 10.004  35.198  100.256 1.00 27.59 ? 975  HIS B CE1   1 
ATOM   15843 N NE2   . HIS B  1 977  ? 10.738  35.721  99.291  1.00 26.65 ? 975  HIS B NE2   1 
ATOM   15844 N N     . THR B  1 978  ? 8.795   40.615  103.032 1.00 19.96 ? 976  THR B N     1 
ATOM   15845 C CA    . THR B  1 978  ? 8.317   41.377  104.179 1.00 23.67 ? 976  THR B CA    1 
ATOM   15846 C C     . THR B  1 978  ? 6.807   41.231  104.242 1.00 25.38 ? 976  THR B C     1 
ATOM   15847 O O     . THR B  1 978  ? 6.141   41.054  103.220 1.00 24.47 ? 976  THR B O     1 
ATOM   15848 C CB    . THR B  1 978  ? 8.695   42.865  104.100 1.00 24.65 ? 976  THR B CB    1 
ATOM   15849 O OG1   . THR B  1 978  ? 8.160   43.564  105.232 1.00 24.87 ? 976  THR B OG1   1 
ATOM   15850 C CG2   . THR B  1 978  ? 8.140   43.496  102.843 1.00 25.34 ? 976  THR B CG2   1 
ATOM   15851 N N     . ARG B  1 979  ? 6.276   41.287  105.454 1.00 25.28 ? 977  ARG B N     1 
ATOM   15852 C CA    . ARG B  1 979  ? 4.836   41.329  105.610 1.00 26.37 ? 977  ARG B CA    1 
ATOM   15853 C C     . ARG B  1 979  ? 4.298   42.750  105.717 1.00 26.26 ? 977  ARG B C     1 
ATOM   15854 O O     . ARG B  1 979  ? 3.088   42.917  105.805 1.00 25.68 ? 977  ARG B O     1 
ATOM   15855 C CB    . ARG B  1 979  ? 4.415   40.531  106.850 1.00 27.70 ? 977  ARG B CB    1 
ATOM   15856 C CG    . ARG B  1 979  ? 4.412   39.031  106.643 1.00 34.56 ? 977  ARG B CG    1 
ATOM   15857 C CD    . ARG B  1 979  ? 4.435   38.321  107.988 1.00 38.10 ? 977  ARG B CD    1 
ATOM   15858 N NE    . ARG B  1 979  ? 4.371   36.875  107.820 1.00 42.07 ? 977  ARG B NE    1 
ATOM   15859 C CZ    . ARG B  1 979  ? 4.084   36.020  108.791 1.00 44.05 ? 977  ARG B CZ    1 
ATOM   15860 N NH1   . ARG B  1 979  ? 3.768   36.436  110.008 1.00 39.37 ? 977  ARG B NH1   1 
ATOM   15861 N NH2   . ARG B  1 979  ? 4.114   34.714  108.533 1.00 47.91 ? 977  ARG B NH2   1 
ATOM   15862 N N     . LEU B  1 980  ? 5.158   43.767  105.687 1.00 24.39 ? 978  LEU B N     1 
ATOM   15863 C CA    . LEU B  1 980  ? 4.788   45.120  106.087 1.00 23.86 ? 978  LEU B CA    1 
ATOM   15864 C C     . LEU B  1 980  ? 4.572   46.015  104.873 1.00 23.66 ? 978  LEU B C     1 
ATOM   15865 O O     . LEU B  1 980  ? 5.510   46.260  104.105 1.00 23.80 ? 978  LEU B O     1 
ATOM   15866 C CB    . LEU B  1 980  ? 5.866   45.721  106.985 1.00 23.10 ? 978  LEU B CB    1 
ATOM   15867 C CG    . LEU B  1 980  ? 6.204   44.864  108.203 1.00 28.66 ? 978  LEU B CG    1 
ATOM   15868 C CD1   . LEU B  1 980  ? 7.301   45.524  109.054 1.00 25.97 ? 978  LEU B CD1   1 
ATOM   15869 C CD2   . LEU B  1 980  ? 4.964   44.604  109.020 1.00 26.40 ? 978  LEU B CD2   1 
ATOM   15870 N N     . ASP B  1 981  ? 3.353   46.545  104.737 1.00 23.69 ? 979  ASP B N     1 
ATOM   15871 C CA    . ASP B  1 981  ? 3.025   47.382  103.583 1.00 25.20 ? 979  ASP B CA    1 
ATOM   15872 C C     . ASP B  1 981  ? 3.920   48.609  103.474 1.00 24.20 ? 979  ASP B C     1 
ATOM   15873 O O     . ASP B  1 981  ? 4.215   49.057  102.361 1.00 23.32 ? 979  ASP B O     1 
ATOM   15874 C CB    . ASP B  1 981  ? 1.570   47.833  103.642 1.00 24.21 ? 979  ASP B CB    1 
ATOM   15875 C CG    . ASP B  1 981  ? 0.612   46.741  103.252 1.00 27.63 ? 979  ASP B CG    1 
ATOM   15876 O OD1   . ASP B  1 981  ? 1.041   45.770  102.590 1.00 29.52 ? 979  ASP B OD1   1 
ATOM   15877 O OD2   . ASP B  1 981  ? -0.568  46.869  103.603 1.00 29.67 ? 979  ASP B OD2   1 
ATOM   15878 N N     . GLU B  1 982  ? 4.307   49.209  104.609 1.00 22.49 ? 980  GLU B N     1 
ATOM   15879 C CA    . GLU B  1 982  ? 5.149   50.402  104.550 1.00 25.96 ? 980  GLU B CA    1 
ATOM   15880 C C     . GLU B  1 982  ? 6.520   50.058  103.994 1.00 25.21 ? 980  GLU B C     1 
ATOM   15881 O O     . GLU B  1 982  ? 7.108   50.825  103.222 1.00 23.81 ? 980  GLU B O     1 
ATOM   15882 C CB    . GLU B  1 982  ? 5.295   51.046  105.933 1.00 25.41 ? 980  GLU B CB    1 
ATOM   15883 C CG    . GLU B  1 982  ? 6.332   52.169  105.952 1.00 27.85 ? 980  GLU B CG    1 
ATOM   15884 C CD    . GLU B  1 982  ? 6.706   52.643  107.355 1.00 36.42 ? 980  GLU B CD    1 
ATOM   15885 O OE1   . GLU B  1 982  ? 6.938   51.795  108.249 1.00 37.64 ? 980  GLU B OE1   1 
ATOM   15886 O OE2   . GLU B  1 982  ? 6.768   53.874  107.561 1.00 33.30 ? 980  GLU B OE2   1 
ATOM   15887 N N     . THR B  1 983  ? 7.027   48.887  104.352 1.00 24.99 ? 981  THR B N     1 
ATOM   15888 C CA    . THR B  1 983  ? 8.308   48.464  103.816 1.00 23.31 ? 981  THR B CA    1 
ATOM   15889 C C     . THR B  1 983  ? 8.184   48.109  102.341 1.00 24.03 ? 981  THR B C     1 
ATOM   15890 O O     . THR B  1 983  ? 9.094   48.393  101.556 1.00 23.45 ? 981  THR B O     1 
ATOM   15891 C CB    . THR B  1 983  ? 8.843   47.290  104.627 1.00 25.52 ? 981  THR B CB    1 
ATOM   15892 O OG1   . THR B  1 983  ? 9.060   47.717  105.983 1.00 29.67 ? 981  THR B OG1   1 
ATOM   15893 C CG2   . THR B  1 983  ? 10.136  46.785  104.019 1.00 24.23 ? 981  THR B CG2   1 
ATOM   15894 N N     . ILE B  1 984  ? 7.055   47.520  101.937 1.00 19.02 ? 982  ILE B N     1 
ATOM   15895 C CA    . ILE B  1 984  ? 6.842   47.263  100.511 1.00 22.55 ? 982  ILE B CA    1 
ATOM   15896 C C     . ILE B  1 984  ? 6.803   48.575  99.732  1.00 23.74 ? 982  ILE B C     1 
ATOM   15897 O O     . ILE B  1 984  ? 7.461   48.720  98.694  1.00 24.82 ? 982  ILE B O     1 
ATOM   15898 C CB    . ILE B  1 984  ? 5.561   46.444  100.288 1.00 22.97 ? 982  ILE B CB    1 
ATOM   15899 C CG1   . ILE B  1 984  ? 5.720   45.040  100.875 1.00 27.22 ? 982  ILE B CG1   1 
ATOM   15900 C CG2   . ILE B  1 984  ? 5.214   46.358  98.799  1.00 23.74 ? 982  ILE B CG2   1 
ATOM   15901 C CD1   . ILE B  1 984  ? 4.504   44.168  100.650 1.00 26.56 ? 982  ILE B CD1   1 
ATOM   15902 N N     . ALA B  1 985  ? 6.019   49.545  100.208 1.00 22.62 ? 983  ALA B N     1 
ATOM   15903 C CA    . ALA B  1 985  ? 5.906   50.813  99.486  1.00 23.89 ? 983  ALA B CA    1 
ATOM   15904 C C     . ALA B  1 985  ? 7.250   51.531  99.420  1.00 24.35 ? 983  ALA B C     1 
ATOM   15905 O O     . ALA B  1 985  ? 7.627   52.083  98.382  1.00 23.74 ? 983  ALA B O     1 
ATOM   15906 C CB    . ALA B  1 985  ? 4.859   51.708  100.156 1.00 23.15 ? 983  ALA B CB    1 
ATOM   15907 N N     . HIS B  1 986  ? 7.988   51.535  100.525 1.00 22.57 ? 984  HIS B N     1 
ATOM   15908 C CA    . HIS B  1 986  ? 9.283   52.207  100.546 1.00 25.12 ? 984  HIS B CA    1 
ATOM   15909 C C     . HIS B  1 986  ? 10.229  51.577  99.528  1.00 23.56 ? 984  HIS B C     1 
ATOM   15910 O O     . HIS B  1 986  ? 10.733  52.252  98.623  1.00 25.15 ? 984  HIS B O     1 
ATOM   15911 C CB    . HIS B  1 986  ? 9.839   52.145  101.972 1.00 22.82 ? 984  HIS B CB    1 
ATOM   15912 C CG    . HIS B  1 986  ? 11.237  52.664  102.136 1.00 29.57 ? 984  HIS B CG    1 
ATOM   15913 N ND1   . HIS B  1 986  ? 11.813  52.824  103.378 1.00 29.42 ? 984  HIS B ND1   1 
ATOM   15914 C CD2   . HIS B  1 986  ? 12.179  53.040  101.237 1.00 29.26 ? 984  HIS B CD2   1 
ATOM   15915 C CE1   . HIS B  1 986  ? 13.044  53.284  103.238 1.00 32.49 ? 984  HIS B CE1   1 
ATOM   15916 N NE2   . HIS B  1 986  ? 13.296  53.413  101.946 1.00 30.00 ? 984  HIS B NE2   1 
ATOM   15917 N N     . VAL B  1 987  ? 10.439  50.267  99.638  1.00 20.84 ? 985  VAL B N     1 
ATOM   15918 C CA    . VAL B  1 987  ? 11.461  49.584  98.849  1.00 23.43 ? 985  VAL B CA    1 
ATOM   15919 C C     . VAL B  1 987  ? 11.116  49.589  97.362  1.00 25.33 ? 985  VAL B C     1 
ATOM   15920 O O     . VAL B  1 987  ? 11.994  49.832  96.519  1.00 26.98 ? 985  VAL B O     1 
ATOM   15921 C CB    . VAL B  1 987  ? 11.659  48.159  99.392  1.00 22.68 ? 985  VAL B CB    1 
ATOM   15922 C CG1   . VAL B  1 987  ? 12.524  47.353  98.483  1.00 23.35 ? 985  VAL B CG1   1 
ATOM   15923 C CG2   . VAL B  1 987  ? 12.291  48.227  100.783 1.00 21.67 ? 985  VAL B CG2   1 
ATOM   15924 N N     . THR B  1 988  ? 9.845   49.335  97.008  1.00 23.93 ? 986  THR B N     1 
ATOM   15925 C CA    . THR B  1 988  ? 9.485   49.284  95.587  1.00 24.89 ? 986  THR B CA    1 
ATOM   15926 C C     . THR B  1 988  ? 9.478   50.665  94.936  1.00 26.36 ? 986  THR B C     1 
ATOM   15927 O O     . THR B  1 988  ? 9.668   50.761  93.722  1.00 26.84 ? 986  THR B O     1 
ATOM   15928 C CB    . THR B  1 988  ? 8.115   48.613  95.367  1.00 25.47 ? 986  THR B CB    1 
ATOM   15929 O OG1   . THR B  1 988  ? 7.072   49.402  95.948  1.00 27.18 ? 986  THR B OG1   1 
ATOM   15930 C CG2   . THR B  1 988  ? 8.083   47.211  95.954  1.00 26.68 ? 986  THR B CG2   1 
ATOM   15931 N N     . SER B  1 989  ? 9.289   51.731  95.705  1.00 27.34 ? 987  SER B N     1 
ATOM   15932 C CA    . SER B  1 989  ? 9.393   53.072  95.141  1.00 29.74 ? 987  SER B CA    1 
ATOM   15933 C C     . SER B  1 989  ? 10.836  53.526  94.942  1.00 28.76 ? 987  SER B C     1 
ATOM   15934 O O     . SER B  1 989  ? 11.078  54.427  94.132  1.00 30.99 ? 987  SER B O     1 
ATOM   15935 C CB    . SER B  1 989  ? 8.662   54.084  96.029  1.00 27.42 ? 987  SER B CB    1 
ATOM   15936 O OG    . SER B  1 989  ? 9.400   54.387  97.212  1.00 34.50 ? 987  SER B OG    1 
ATOM   15937 N N     . ARG B  1 990  ? 11.801  52.927  95.636  1.00 24.21 ? 988  ARG B N     1 
ATOM   15938 C CA    . ARG B  1 990  ? 13.183  53.394  95.561  1.00 24.98 ? 988  ARG B CA    1 
ATOM   15939 C C     . ARG B  1 990  ? 14.081  52.495  94.720  1.00 27.19 ? 988  ARG B C     1 
ATOM   15940 O O     . ARG B  1 990  ? 15.067  52.979  94.157  1.00 27.66 ? 988  ARG B O     1 
ATOM   15941 C CB    . ARG B  1 990  ? 13.775  53.525  96.971  1.00 25.82 ? 988  ARG B CB    1 
ATOM   15942 C CG    . ARG B  1 990  ? 12.935  54.400  97.908  1.00 30.28 ? 988  ARG B CG    1 
ATOM   15943 C CD    . ARG B  1 990  ? 13.179  55.853  97.673  1.00 31.95 ? 988  ARG B CD    1 
ATOM   15944 N NE    . ARG B  1 990  ? 14.317  56.356  98.437  1.00 28.32 ? 988  ARG B NE    1 
ATOM   15945 C CZ    . ARG B  1 990  ? 14.726  57.615  98.386  1.00 29.28 ? 988  ARG B CZ    1 
ATOM   15946 N NH1   . ARG B  1 990  ? 14.176  58.480  97.553  1.00 31.23 ? 988  ARG B NH1   1 
ATOM   15947 N NH2   . ARG B  1 990  ? 15.704  58.018  99.193  1.00 30.72 ? 988  ARG B NH2   1 
ATOM   15948 N N     . ILE B  1 991  ? 13.764  51.198  94.620  1.00 25.24 ? 989  ILE B N     1 
ATOM   15949 C CA    . ILE B  1 991  ? 14.596  50.281  93.860  1.00 24.77 ? 989  ILE B CA    1 
ATOM   15950 C C     . ILE B  1 991  ? 14.449  50.579  92.373  1.00 25.80 ? 989  ILE B C     1 
ATOM   15951 O O     . ILE B  1 991  ? 13.392  51.004  91.900  1.00 25.66 ? 989  ILE B O     1 
ATOM   15952 C CB    . ILE B  1 991  ? 14.221  48.822  94.177  1.00 23.90 ? 989  ILE B CB    1 
ATOM   15953 C CG1   . ILE B  1 991  ? 15.360  47.869  93.798  1.00 24.47 ? 989  ILE B CG1   1 
ATOM   15954 C CG2   . ILE B  1 991  ? 12.912  48.443  93.487  1.00 25.86 ? 989  ILE B CG2   1 
ATOM   15955 C CD1   . ILE B  1 991  ? 16.547  47.954  94.761  1.00 26.27 ? 989  ILE B CD1   1 
ATOM   15956 N N     . LYS B  1 992  ? 15.520  50.366  91.627  1.00 26.60 ? 990  LYS B N     1 
ATOM   15957 C CA    . LYS B  1 992  ? 15.505  50.555  90.178  1.00 30.10 ? 990  LYS B CA    1 
ATOM   15958 C C     . LYS B  1 992  ? 15.819  49.201  89.555  1.00 28.59 ? 990  LYS B C     1 
ATOM   15959 O O     . LYS B  1 992  ? 16.978  48.875  89.293  1.00 33.21 ? 990  LYS B O     1 
ATOM   15960 C CB    . LYS B  1 992  ? 16.513  51.642  89.752  1.00 28.75 ? 990  LYS B CB    1 
ATOM   15961 C CG    . LYS B  1 992  ? 16.173  53.016  90.321  1.00 32.95 ? 990  LYS B CG    1 
ATOM   15962 C CD    . LYS B  1 992  ? 17.358  53.948  90.242  1.00 35.95 ? 990  LYS B CD    1 
ATOM   15963 C CE    . LYS B  1 992  ? 17.120  55.193  91.104  1.00 40.74 ? 990  LYS B CE    1 
ATOM   15964 N NZ    . LYS B  1 992  ? 18.388  55.756  91.652  1.00 46.27 ? 990  LYS B NZ    1 
ATOM   15965 N N     . ALA B  1 993  ? 14.787  48.394  89.353  1.00 27.22 ? 991  ALA B N     1 
ATOM   15966 C CA    . ALA B  1 993  ? 14.945  47.112  88.696  1.00 25.52 ? 991  ALA B CA    1 
ATOM   15967 C C     . ALA B  1 993  ? 13.738  46.880  87.796  1.00 26.38 ? 991  ALA B C     1 
ATOM   15968 O O     . ALA B  1 993  ? 12.638  47.364  88.077  1.00 23.93 ? 991  ALA B O     1 
ATOM   15969 C CB    . ALA B  1 993  ? 15.105  45.972  89.715  1.00 22.23 ? 991  ALA B CB    1 
ATOM   15970 N N     . GLY B  1 994  ? 13.959  46.148  86.697  1.00 22.76 ? 992  GLY B N     1 
ATOM   15971 C CA    . GLY B  1 994  ? 12.875  45.914  85.757  1.00 22.73 ? 992  GLY B CA    1 
ATOM   15972 C C     . GLY B  1 994  ? 11.840  44.895  86.209  1.00 22.82 ? 992  GLY B C     1 
ATOM   15973 O O     . GLY B  1 994  ? 10.693  44.929  85.752  1.00 22.06 ? 992  GLY B O     1 
ATOM   15974 N N     . ASN B  1 995  ? 12.226  43.951  87.062  1.00 21.00 ? 993  ASN B N     1 
ATOM   15975 C CA    . ASN B  1 995  ? 11.354  42.856  87.464  1.00 19.12 ? 993  ASN B CA    1 
ATOM   15976 C C     . ASN B  1 995  ? 11.427  42.717  88.974  1.00 21.00 ? 993  ASN B C     1 
ATOM   15977 O O     . ASN B  1 995  ? 12.450  42.274  89.501  1.00 21.27 ? 993  ASN B O     1 
ATOM   15978 C CB    . ASN B  1 995  ? 11.758  41.548  86.788  1.00 19.29 ? 993  ASN B CB    1 
ATOM   15979 C CG    . ASN B  1 995  ? 11.227  41.450  85.368  1.00 18.24 ? 993  ASN B CG    1 
ATOM   15980 O OD1   . ASN B  1 995  ? 11.814  41.979  84.438  1.00 22.81 ? 993  ASN B OD1   1 
ATOM   15981 N ND2   . ASN B  1 995  ? 10.102  40.775  85.211  1.00 20.04 ? 993  ASN B ND2   1 
ATOM   15982 N N     . LEU B  1 996  ? 10.339  43.077  89.649  1.00 21.84 ? 994  LEU B N     1 
ATOM   15983 C CA    . LEU B  1 996  ? 10.246  43.061  91.102  1.00 17.74 ? 994  LEU B CA    1 
ATOM   15984 C C     . LEU B  1 996  ? 9.412   41.865  91.548  1.00 18.86 ? 994  LEU B C     1 
ATOM   15985 O O     . LEU B  1 996  ? 8.437   41.500  90.890  1.00 21.16 ? 994  LEU B O     1 
ATOM   15986 C CB    . LEU B  1 996  ? 9.603   44.359  91.601  1.00 16.75 ? 994  LEU B CB    1 
ATOM   15987 C CG    . LEU B  1 996  ? 10.123  45.684  91.038  1.00 22.88 ? 994  LEU B CG    1 
ATOM   15988 C CD1   . LEU B  1 996  ? 9.419   46.849  91.713  1.00 27.34 ? 994  LEU B CD1   1 
ATOM   15989 C CD2   . LEU B  1 996  ? 11.643  45.813  91.201  1.00 22.89 ? 994  LEU B CD2   1 
ATOM   15990 N N     . TYR B  1 997  ? 9.779   41.271  92.683  1.00 19.67 ? 995  TYR B N     1 
ATOM   15991 C CA    . TYR B  1 997  ? 9.110   40.082  93.195  1.00 18.57 ? 995  TYR B CA    1 
ATOM   15992 C C     . TYR B  1 997  ? 8.935   40.237  94.696  1.00 20.34 ? 995  TYR B C     1 
ATOM   15993 O O     . TYR B  1 997  ? 9.915   40.485  95.402  1.00 22.51 ? 995  TYR B O     1 
ATOM   15994 C CB    . TYR B  1 997  ? 9.932   38.825  92.897  1.00 19.95 ? 995  TYR B CB    1 
ATOM   15995 C CG    . TYR B  1 997  ? 10.051  38.546  91.427  1.00 22.48 ? 995  TYR B CG    1 
ATOM   15996 C CD1   . TYR B  1 997  ? 9.047   37.865  90.756  1.00 24.88 ? 995  TYR B CD1   1 
ATOM   15997 C CD2   . TYR B  1 997  ? 11.147  38.988  90.700  1.00 23.17 ? 995  TYR B CD2   1 
ATOM   15998 C CE1   . TYR B  1 997  ? 9.147   37.596  89.401  1.00 24.51 ? 995  TYR B CE1   1 
ATOM   15999 C CE2   . TYR B  1 997  ? 11.243  38.730  89.334  1.00 23.89 ? 995  TYR B CE2   1 
ATOM   16000 C CZ    . TYR B  1 997  ? 10.240  38.043  88.701  1.00 25.81 ? 995  TYR B CZ    1 
ATOM   16001 O OH    . TYR B  1 997  ? 10.324  37.781  87.350  1.00 31.55 ? 995  TYR B OH    1 
ATOM   16002 N N     . ILE B  1 998  ? 7.708   40.074  95.184  1.00 20.29 ? 996  ILE B N     1 
ATOM   16003 C CA    . ILE B  1 998  ? 7.407   40.295  96.593  1.00 21.39 ? 996  ILE B CA    1 
ATOM   16004 C C     . ILE B  1 998  ? 6.931   38.982  97.193  1.00 19.16 ? 996  ILE B C     1 
ATOM   16005 O O     . ILE B  1 998  ? 5.903   38.437  96.768  1.00 22.76 ? 996  ILE B O     1 
ATOM   16006 C CB    . ILE B  1 998  ? 6.348   41.389  96.794  1.00 21.76 ? 996  ILE B CB    1 
ATOM   16007 C CG1   . ILE B  1 998  ? 6.763   42.696  96.087  1.00 21.20 ? 996  ILE B CG1   1 
ATOM   16008 C CG2   . ILE B  1 998  ? 6.067   41.572  98.310  1.00 21.55 ? 996  ILE B CG2   1 
ATOM   16009 C CD1   . ILE B  1 998  ? 8.019   43.297  96.573  1.00 27.95 ? 996  ILE B CD1   1 
ATOM   16010 N N     . ASN B  1 999  ? 7.673   38.488  98.193  1.00 18.15 ? 997  ASN B N     1 
ATOM   16011 C CA    . ASN B  1 999  ? 7.308   37.288  98.955  1.00 20.49 ? 997  ASN B CA    1 
ATOM   16012 C C     . ASN B  1 999  ? 7.253   36.033  98.085  1.00 20.45 ? 997  ASN B C     1 
ATOM   16013 O O     . ASN B  1 999  ? 6.406   35.159  98.285  1.00 22.70 ? 997  ASN B O     1 
ATOM   16014 C CB    . ASN B  1 999  ? 5.988   37.513  99.709  1.00 23.43 ? 997  ASN B CB    1 
ATOM   16015 C CG    . ASN B  1 999  ? 6.147   38.556  100.794 1.00 22.20 ? 997  ASN B CG    1 
ATOM   16016 O OD1   . ASN B  1 999  ? 7.228   38.678  101.342 1.00 22.74 ? 997  ASN B OD1   1 
ATOM   16017 N ND2   . ASN B  1 999  ? 5.108   39.349  101.058 1.00 22.17 ? 997  ASN B ND2   1 
ATOM   16018 N N     . ARG B  1 1000 ? 8.187   35.935  97.136  1.00 21.89 ? 998  ARG B N     1 
ATOM   16019 C CA    . ARG B  1 1000 ? 8.323   34.770  96.273  1.00 20.68 ? 998  ARG B CA    1 
ATOM   16020 C C     . ARG B  1 1000 ? 9.742   34.752  95.719  1.00 21.98 ? 998  ARG B C     1 
ATOM   16021 O O     . ARG B  1 1000 ? 10.560  35.627  96.019  1.00 22.22 ? 998  ARG B O     1 
ATOM   16022 C CB    . ARG B  1 1000 ? 7.278   34.778  95.148  1.00 20.86 ? 998  ARG B CB    1 
ATOM   16023 C CG    . ARG B  1 1000 ? 7.239   36.102  94.387  1.00 19.59 ? 998  ARG B CG    1 
ATOM   16024 C CD    . ARG B  1 1000 ? 6.754   35.896  92.956  1.00 21.36 ? 998  ARG B CD    1 
ATOM   16025 N NE    . ARG B  1 1000 ? 7.711   35.119  92.183  1.00 21.95 ? 998  ARG B NE    1 
ATOM   16026 C CZ    . ARG B  1 1000 ? 7.515   34.771  90.918  1.00 25.30 ? 998  ARG B CZ    1 
ATOM   16027 N NH1   . ARG B  1 1000 ? 6.405   35.092  90.285  1.00 22.71 ? 998  ARG B NH1   1 
ATOM   16028 N NH2   . ARG B  1 1000 ? 8.455   34.083  90.276  1.00 23.11 ? 998  ARG B NH2   1 
ATOM   16029 N N     . ASN B  1 1001 ? 10.042  33.742  94.906  1.00 21.04 ? 999  ASN B N     1 
ATOM   16030 C CA    . ASN B  1 1001 ? 11.376  33.712  94.328  1.00 20.70 ? 999  ASN B CA    1 
ATOM   16031 C C     . ASN B  1 1001 ? 11.468  34.755  93.210  1.00 21.98 ? 999  ASN B C     1 
ATOM   16032 O O     . ASN B  1 1001 ? 10.484  35.401  92.850  1.00 22.12 ? 999  ASN B O     1 
ATOM   16033 C CB    . ASN B  1 1001 ? 11.732  32.299  93.858  1.00 21.02 ? 999  ASN B CB    1 
ATOM   16034 C CG    . ASN B  1 1001 ? 10.945  31.857  92.629  1.00 26.64 ? 999  ASN B CG    1 
ATOM   16035 O OD1   . ASN B  1 1001 ? 10.761  32.620  91.696  1.00 24.40 ? 999  ASN B OD1   1 
ATOM   16036 N ND2   . ASN B  1 1001 ? 10.467  30.608  92.640  1.00 28.36 ? 999  ASN B ND2   1 
ATOM   16037 N N     . ILE B  1 1002 ? 12.667  34.949  92.675  1.00 18.95 ? 1000 ILE B N     1 
ATOM   16038 C CA    . ILE B  1 1002 ? 12.873  36.018  91.709  1.00 21.65 ? 1000 ILE B CA    1 
ATOM   16039 C C     . ILE B  1 1002 ? 13.206  35.474  90.319  1.00 23.04 ? 1000 ILE B C     1 
ATOM   16040 O O     . ILE B  1 1002 ? 13.699  36.219  89.468  1.00 24.06 ? 1000 ILE B O     1 
ATOM   16041 C CB    . ILE B  1 1002 ? 13.940  37.011  92.193  1.00 23.17 ? 1000 ILE B CB    1 
ATOM   16042 C CG1   . ILE B  1 1002 ? 15.334  36.353  92.261  1.00 18.82 ? 1000 ILE B CG1   1 
ATOM   16043 C CG2   . ILE B  1 1002 ? 13.512  37.599  93.532  1.00 21.07 ? 1000 ILE B CG2   1 
ATOM   16044 C CD1   . ILE B  1 1002 ? 16.417  37.312  92.592  1.00 20.96 ? 1000 ILE B CD1   1 
ATOM   16045 N N     . ILE B  1 1003 ? 12.933  34.194  90.064  1.00 23.26 ? 1001 ILE B N     1 
ATOM   16046 C CA    . ILE B  1 1003 ? 13.317  33.567  88.805  1.00 21.98 ? 1001 ILE B CA    1 
ATOM   16047 C C     . ILE B  1 1003 ? 12.073  33.118  88.045  1.00 26.92 ? 1001 ILE B C     1 
ATOM   16048 O O     . ILE B  1 1003 ? 10.966  33.062  88.586  1.00 27.92 ? 1001 ILE B O     1 
ATOM   16049 C CB    . ILE B  1 1003 ? 14.272  32.379  89.019  1.00 25.07 ? 1001 ILE B CB    1 
ATOM   16050 C CG1   . ILE B  1 1003 ? 13.597  31.279  89.840  1.00 25.85 ? 1001 ILE B CG1   1 
ATOM   16051 C CG2   . ILE B  1 1003 ? 15.514  32.848  89.712  1.00 24.32 ? 1001 ILE B CG2   1 
ATOM   16052 C CD1   . ILE B  1 1003 ? 14.393  29.973  89.849  1.00 28.10 ? 1001 ILE B CD1   1 
ATOM   16053 N N     . GLY B  1 1004 ? 12.272  32.801  86.766  1.00 25.56 ? 1002 GLY B N     1 
ATOM   16054 C CA    . GLY B  1 1004 ? 11.231  32.114  86.023  1.00 29.88 ? 1002 GLY B CA    1 
ATOM   16055 C C     . GLY B  1 1004 ? 10.131  33.030  85.550  1.00 28.08 ? 1002 GLY B C     1 
ATOM   16056 O O     . GLY B  1 1004 ? 8.939   32.671  85.629  1.00 28.37 ? 1002 GLY B O     1 
ATOM   16057 N N     . ALA B  1 1005 ? 10.491  34.222  85.086  1.00 24.66 ? 1003 ALA B N     1 
ATOM   16058 C CA    . ALA B  1 1005 ? 9.496   35.165  84.605  1.00 22.10 ? 1003 ALA B CA    1 
ATOM   16059 C C     . ALA B  1 1005 ? 8.655   34.520  83.512  1.00 27.13 ? 1003 ALA B C     1 
ATOM   16060 O O     . ALA B  1 1005 ? 9.173   33.832  82.632  1.00 27.39 ? 1003 ALA B O     1 
ATOM   16061 C CB    . ALA B  1 1005 ? 10.182  36.422  84.073  1.00 26.36 ? 1003 ALA B CB    1 
ATOM   16062 N N     . VAL B  1 1006 ? 7.350   34.723  83.590  1.00 20.86 ? 1004 VAL B N     1 
ATOM   16063 C CA    . VAL B  1 1006 ? 6.400   34.056  82.712  1.00 23.66 ? 1004 VAL B CA    1 
ATOM   16064 C C     . VAL B  1 1006 ? 5.997   35.025  81.614  1.00 21.06 ? 1004 VAL B C     1 
ATOM   16065 O O     . VAL B  1 1006 ? 5.603   36.165  81.888  1.00 20.78 ? 1004 VAL B O     1 
ATOM   16066 C CB    . VAL B  1 1006 ? 5.182   33.550  83.503  1.00 23.19 ? 1004 VAL B CB    1 
ATOM   16067 C CG1   . VAL B  1 1006 ? 4.077   33.030  82.576  1.00 23.02 ? 1004 VAL B CG1   1 
ATOM   16068 C CG2   . VAL B  1 1006 ? 5.638   32.458  84.473  1.00 25.62 ? 1004 VAL B CG2   1 
ATOM   16069 N N     . VAL B  1 1007 ? 6.102   34.561  80.368  1.00 20.63 ? 1005 VAL B N     1 
ATOM   16070 C CA    . VAL B  1 1007 ? 5.732   35.359  79.206  1.00 23.29 ? 1005 VAL B CA    1 
ATOM   16071 C C     . VAL B  1 1007 ? 4.355   35.986  79.380  1.00 22.78 ? 1005 VAL B C     1 
ATOM   16072 O O     . VAL B  1 1007 ? 3.358   35.298  79.638  1.00 21.46 ? 1005 VAL B O     1 
ATOM   16073 C CB    . VAL B  1 1007 ? 5.781   34.477  77.949  1.00 23.28 ? 1005 VAL B CB    1 
ATOM   16074 C CG1   . VAL B  1 1007 ? 5.211   35.235  76.761  1.00 22.49 ? 1005 VAL B CG1   1 
ATOM   16075 C CG2   . VAL B  1 1007 ? 7.217   34.034  77.696  1.00 23.10 ? 1005 VAL B CG2   1 
ATOM   16076 N N     . GLY B  1 1008 ? 4.288   37.299  79.180  1.00 23.27 ? 1006 GLY B N     1 
ATOM   16077 C CA    . GLY B  1 1008 ? 3.027   38.000  79.218  1.00 24.92 ? 1006 GLY B CA    1 
ATOM   16078 C C     . GLY B  1 1008 ? 2.455   38.193  80.603  1.00 23.99 ? 1006 GLY B C     1 
ATOM   16079 O O     . GLY B  1 1008 ? 1.427   38.859  80.743  1.00 22.73 ? 1006 GLY B O     1 
ATOM   16080 N N     . VAL B  1 1009 ? 3.081   37.632  81.627  1.00 19.78 ? 1007 VAL B N     1 
ATOM   16081 C CA    . VAL B  1 1009 ? 2.640   37.775  83.009  1.00 21.98 ? 1007 VAL B CA    1 
ATOM   16082 C C     . VAL B  1 1009 ? 3.651   38.581  83.820  1.00 21.13 ? 1007 VAL B C     1 
ATOM   16083 O O     . VAL B  1 1009 ? 3.278   39.494  84.562  1.00 21.67 ? 1007 VAL B O     1 
ATOM   16084 C CB    . VAL B  1 1009 ? 2.381   36.395  83.652  1.00 22.90 ? 1007 VAL B CB    1 
ATOM   16085 C CG1   . VAL B  1 1009 ? 1.826   36.547  85.083  1.00 21.82 ? 1007 VAL B CG1   1 
ATOM   16086 C CG2   . VAL B  1 1009 ? 1.429   35.579  82.776  1.00 21.66 ? 1007 VAL B CG2   1 
ATOM   16087 N N     . GLN B  1 1010 ? 4.942   38.248  83.688  1.00 21.94 ? 1008 GLN B N     1 
ATOM   16088 C CA    . GLN B  1 1010 ? 6.059   39.100  84.102  1.00 21.72 ? 1008 GLN B CA    1 
ATOM   16089 C C     . GLN B  1 1010 ? 6.912   39.357  82.862  1.00 22.61 ? 1008 GLN B C     1 
ATOM   16090 O O     . GLN B  1 1010 ? 7.946   38.700  82.666  1.00 24.34 ? 1008 GLN B O     1 
ATOM   16091 C CB    . GLN B  1 1010 ? 6.899   38.479  85.227  1.00 21.27 ? 1008 GLN B CB    1 
ATOM   16092 C CG    . GLN B  1 1010 ? 6.127   38.158  86.495  1.00 22.22 ? 1008 GLN B CG    1 
ATOM   16093 C CD    . GLN B  1 1010 ? 5.730   36.700  86.570  1.00 22.59 ? 1008 GLN B CD    1 
ATOM   16094 O OE1   . GLN B  1 1010 ? 6.434   35.826  86.047  1.00 24.81 ? 1008 GLN B OE1   1 
ATOM   16095 N NE2   . GLN B  1 1010 ? 4.599   36.420  87.224  1.00 21.63 ? 1008 GLN B NE2   1 
ATOM   16096 N N     . PRO B  1 1011 ? 6.498   40.285  81.992  1.00 21.70 ? 1009 PRO B N     1 
ATOM   16097 C CA    . PRO B  1 1011 ? 7.380   40.736  80.899  1.00 21.83 ? 1009 PRO B CA    1 
ATOM   16098 C C     . PRO B  1 1011 ? 8.764   41.050  81.446  1.00 23.05 ? 1009 PRO B C     1 
ATOM   16099 O O     . PRO B  1 1011 ? 8.903   41.751  82.448  1.00 21.03 ? 1009 PRO B O     1 
ATOM   16100 C CB    . PRO B  1 1011 ? 6.688   42.001  80.381  1.00 21.64 ? 1009 PRO B CB    1 
ATOM   16101 C CG    . PRO B  1 1011 ? 5.250   41.846  80.796  1.00 23.17 ? 1009 PRO B CG    1 
ATOM   16102 C CD    . PRO B  1 1011 ? 5.260   41.083  82.082  1.00 21.92 ? 1009 PRO B CD    1 
ATOM   16103 N N     . PHE B  1 1012 ? 9.791   40.516  80.788  1.00 19.22 ? 1010 PHE B N     1 
ATOM   16104 C CA    . PHE B  1 1012 ? 11.094  40.340  81.408  1.00 23.63 ? 1010 PHE B CA    1 
ATOM   16105 C C     . PHE B  1 1012 ? 12.135  41.257  80.787  1.00 21.61 ? 1010 PHE B C     1 
ATOM   16106 O O     . PHE B  1 1012 ? 12.324  41.267  79.570  1.00 22.59 ? 1010 PHE B O     1 
ATOM   16107 C CB    . PHE B  1 1012 ? 11.566  38.889  81.300  1.00 23.06 ? 1010 PHE B CB    1 
ATOM   16108 C CG    . PHE B  1 1012 ? 12.848  38.638  82.031  1.00 23.04 ? 1010 PHE B CG    1 
ATOM   16109 C CD1   . PHE B  1 1012 ? 12.870  38.608  83.413  1.00 24.56 ? 1010 PHE B CD1   1 
ATOM   16110 C CD2   . PHE B  1 1012 ? 14.034  38.446  81.337  1.00 27.78 ? 1010 PHE B CD2   1 
ATOM   16111 C CE1   . PHE B  1 1012 ? 14.050  38.372  84.101  1.00 21.71 ? 1010 PHE B CE1   1 
ATOM   16112 C CE2   . PHE B  1 1012 ? 15.232  38.223  82.009  1.00 27.05 ? 1010 PHE B CE2   1 
ATOM   16113 C CZ    . PHE B  1 1012 ? 15.244  38.191  83.396  1.00 25.29 ? 1010 PHE B CZ    1 
ATOM   16114 N N     . GLY B  1 1013 ? 12.836  41.980  81.629  1.00 21.28 ? 1011 GLY B N     1 
ATOM   16115 C CA    . GLY B  1 1013 ? 13.995  42.736  81.203  1.00 22.40 ? 1011 GLY B CA    1 
ATOM   16116 C C     . GLY B  1 1013 ? 14.159  43.952  82.073  1.00 26.10 ? 1011 GLY B C     1 
ATOM   16117 O O     . GLY B  1 1013 ? 13.225  44.428  82.712  1.00 24.63 ? 1011 GLY B O     1 
ATOM   16118 N N     . GLY B  1 1014 ? 15.381  44.471  82.084  1.00 28.10 ? 1012 GLY B N     1 
ATOM   16119 C CA    . GLY B  1 1014 ? 15.705  45.551  82.978  1.00 27.39 ? 1012 GLY B CA    1 
ATOM   16120 C C     . GLY B  1 1014 ? 16.271  46.762  82.288  1.00 31.23 ? 1012 GLY B C     1 
ATOM   16121 O O     . GLY B  1 1014 ? 16.221  46.885  81.058  1.00 36.51 ? 1012 GLY B O     1 
ATOM   16122 N N     . ARG B  1 1015 ? 16.853  47.636  83.096  1.00 32.22 ? 1013 ARG B N     1 
ATOM   16123 C CA    A ARG B  1 1015 ? 17.400  48.929  82.723  0.59 35.62 ? 1013 ARG B CA    1 
ATOM   16124 C CA    B ARG B  1 1015 ? 17.417  48.900  82.648  0.41 35.57 ? 1013 ARG B CA    1 
ATOM   16125 C C     . ARG B  1 1015 ? 18.899  48.952  83.003  1.00 32.29 ? 1013 ARG B C     1 
ATOM   16126 O O     . ARG B  1 1015 ? 19.469  47.998  83.528  1.00 31.27 ? 1013 ARG B O     1 
ATOM   16127 C CB    A ARG B  1 1015 ? 16.700  50.037  83.513  0.59 36.00 ? 1013 ARG B CB    1 
ATOM   16128 C CB    B ARG B  1 1015 ? 16.664  50.078  83.270  0.41 36.00 ? 1013 ARG B CB    1 
ATOM   16129 C CG    A ARG B  1 1015 ? 16.596  49.698  85.005  0.59 36.08 ? 1013 ARG B CG    1 
ATOM   16130 C CG    B ARG B  1 1015 ? 16.276  49.853  84.727  0.41 36.60 ? 1013 ARG B CG    1 
ATOM   16131 C CD    A ARG B  1 1015 ? 16.539  50.938  85.890  0.59 38.12 ? 1013 ARG B CD    1 
ATOM   16132 C CD    B ARG B  1 1015 ? 16.552  51.078  85.592  0.41 38.01 ? 1013 ARG B CD    1 
ATOM   16133 N NE    A ARG B  1 1015 ? 17.798  51.680  85.889  0.59 39.66 ? 1013 ARG B NE    1 
ATOM   16134 N NE    B ARG B  1 1015 ? 17.938  51.133  86.053  0.41 38.45 ? 1013 ARG B NE    1 
ATOM   16135 C CZ    A ARG B  1 1015 ? 18.845  51.400  86.655  0.59 36.79 ? 1013 ARG B CZ    1 
ATOM   16136 C CZ    B ARG B  1 1015 ? 18.850  51.989  85.607  0.41 37.60 ? 1013 ARG B CZ    1 
ATOM   16137 N NH1   A ARG B  1 1015 ? 18.841  50.371  87.490  0.59 34.84 ? 1013 ARG B NH1   1 
ATOM   16138 N NH1   B ARG B  1 1015 ? 18.565  52.881  84.673  0.41 38.08 ? 1013 ARG B NH1   1 
ATOM   16139 N NH2   A ARG B  1 1015 ? 19.929  52.169  86.578  0.59 38.02 ? 1013 ARG B NH2   1 
ATOM   16140 N NH2   B ARG B  1 1015 ? 20.079  51.950  86.115  0.41 37.83 ? 1013 ARG B NH2   1 
ATOM   16141 N N     . GLY B  1 1016 ? 19.525  50.079  82.688  1.00 31.81 ? 1014 GLY B N     1 
ATOM   16142 C CA    . GLY B  1 1016 ? 20.930  50.243  83.032  1.00 30.39 ? 1014 GLY B CA    1 
ATOM   16143 C C     . GLY B  1 1016 ? 21.816  49.242  82.319  1.00 30.98 ? 1014 GLY B C     1 
ATOM   16144 O O     . GLY B  1 1016 ? 21.678  48.998  81.115  1.00 34.06 ? 1014 GLY B O     1 
ATOM   16145 N N     . LEU B  1 1017 ? 22.747  48.648  83.067  1.00 28.46 ? 1015 LEU B N     1 
ATOM   16146 C CA    . LEU B  1 1017 ? 23.650  47.643  82.526  1.00 29.70 ? 1015 LEU B CA    1 
ATOM   16147 C C     . LEU B  1 1017 ? 22.954  46.324  82.242  1.00 29.99 ? 1015 LEU B C     1 
ATOM   16148 O O     . LEU B  1 1017 ? 23.601  45.396  81.743  1.00 31.37 ? 1015 LEU B O     1 
ATOM   16149 C CB    . LEU B  1 1017 ? 24.811  47.421  83.505  1.00 33.07 ? 1015 LEU B CB    1 
ATOM   16150 C CG    . LEU B  1 1017 ? 25.737  48.625  83.748  1.00 36.42 ? 1015 LEU B CG    1 
ATOM   16151 C CD1   . LEU B  1 1017 ? 26.624  48.415  84.974  1.00 35.93 ? 1015 LEU B CD1   1 
ATOM   16152 C CD2   . LEU B  1 1017 ? 26.587  48.879  82.516  1.00 34.11 ? 1015 LEU B CD2   1 
ATOM   16153 N N     . SER B  1 1018 ? 21.664  46.211  82.568  1.00 27.71 ? 1016 SER B N     1 
ATOM   16154 C CA    . SER B  1 1018 ? 20.910  44.983  82.371  1.00 29.37 ? 1016 SER B CA    1 
ATOM   16155 C C     . SER B  1 1018 ? 20.273  44.898  80.993  1.00 30.39 ? 1016 SER B C     1 
ATOM   16156 O O     . SER B  1 1018 ? 19.883  43.804  80.576  1.00 30.80 ? 1016 SER B O     1 
ATOM   16157 C CB    . SER B  1 1018 ? 19.829  44.846  83.457  1.00 30.80 ? 1016 SER B CB    1 
ATOM   16158 O OG    . SER B  1 1018 ? 20.446  44.609  84.723  1.00 31.75 ? 1016 SER B OG    1 
ATOM   16159 N N     . GLY B  1 1019 ? 20.137  46.008  80.287  1.00 31.69 ? 1017 GLY B N     1 
ATOM   16160 C CA    . GLY B  1 1019 ? 19.830  45.907  78.878  1.00 30.94 ? 1017 GLY B CA    1 
ATOM   16161 C C     . GLY B  1 1019 ? 19.221  47.170  78.318  1.00 28.70 ? 1017 GLY B C     1 
ATOM   16162 O O     . GLY B  1 1019 ? 19.083  48.183  78.990  1.00 29.81 ? 1017 GLY B O     1 
ATOM   16163 N N     . THR B  1 1020 ? 18.858  47.068  77.045  1.00 28.75 ? 1018 THR B N     1 
ATOM   16164 C CA    . THR B  1 1020 ? 18.230  48.154  76.313  1.00 24.78 ? 1018 THR B CA    1 
ATOM   16165 C C     . THR B  1 1020 ? 16.715  48.177  76.472  1.00 26.99 ? 1018 THR B C     1 
ATOM   16166 O O     . THR B  1 1020 ? 16.095  49.237  76.334  1.00 28.73 ? 1018 THR B O     1 
ATOM   16167 C CB    . THR B  1 1020 ? 18.556  48.008  74.828  1.00 28.84 ? 1018 THR B CB    1 
ATOM   16168 O OG1   . THR B  1 1020 ? 18.026  46.752  74.375  1.00 22.11 ? 1018 THR B OG1   1 
ATOM   16169 C CG2   . THR B  1 1020 ? 20.080  48.022  74.585  1.00 25.15 ? 1018 THR B CG2   1 
ATOM   16170 N N     . GLY B  1 1021 ? 16.100  47.031  76.705  1.00 25.67 ? 1019 GLY B N     1 
ATOM   16171 C CA    . GLY B  1 1021 ? 14.682  46.904  76.471  1.00 25.09 ? 1019 GLY B CA    1 
ATOM   16172 C C     . GLY B  1 1021 ? 14.396  46.955  74.980  1.00 22.90 ? 1019 GLY B C     1 
ATOM   16173 O O     . GLY B  1 1021 ? 15.318  47.020  74.160  1.00 26.72 ? 1019 GLY B O     1 
ATOM   16174 N N     . PRO B  1 1022 ? 13.105  46.879  74.591  1.00 22.63 ? 1020 PRO B N     1 
ATOM   16175 C CA    . PRO B  1 1022 ? 11.931  46.702  75.451  1.00 21.35 ? 1020 PRO B CA    1 
ATOM   16176 C C     . PRO B  1 1022 ? 11.910  45.302  76.045  1.00 23.74 ? 1020 PRO B C     1 
ATOM   16177 O O     . PRO B  1 1022 ? 12.669  44.428  75.615  1.00 23.29 ? 1020 PRO B O     1 
ATOM   16178 C CB    . PRO B  1 1022 ? 10.757  46.924  74.485  1.00 24.52 ? 1020 PRO B CB    1 
ATOM   16179 C CG    . PRO B  1 1022 ? 11.287  46.402  73.169  1.00 23.98 ? 1020 PRO B CG    1 
ATOM   16180 C CD    . PRO B  1 1022 ? 12.754  46.783  73.159  1.00 23.04 ? 1020 PRO B CD    1 
ATOM   16181 N N     . LYS B  1 1023 ? 11.040  45.061  77.020  1.00 21.24 ? 1021 LYS B N     1 
ATOM   16182 C CA    . LYS B  1 1023 ? 10.979  43.759  77.675  1.00 22.85 ? 1021 LYS B CA    1 
ATOM   16183 C C     . LYS B  1 1023 ? 10.535  42.656  76.725  1.00 22.08 ? 1021 LYS B C     1 
ATOM   16184 O O     . LYS B  1 1023 ? 9.576   42.815  75.972  1.00 19.97 ? 1021 LYS B O     1 
ATOM   16185 C CB    . LYS B  1 1023 ? 10.001  43.800  78.837  1.00 22.67 ? 1021 LYS B CB    1 
ATOM   16186 C CG    . LYS B  1 1023 ? 10.448  44.613  80.025  1.00 21.53 ? 1021 LYS B CG    1 
ATOM   16187 C CD    . LYS B  1 1023 ? 9.292   44.682  81.015  1.00 20.93 ? 1021 LYS B CD    1 
ATOM   16188 C CE    . LYS B  1 1023 ? 9.752   45.156  82.401  1.00 23.99 ? 1021 LYS B CE    1 
ATOM   16189 N NZ    . LYS B  1 1023 ? 10.432  44.054  83.143  1.00 23.20 ? 1021 LYS B NZ    1 
ATOM   16190 N N     . ALA B  1 1024 ? 11.207  41.506  76.823  1.00 22.79 ? 1022 ALA B N     1 
ATOM   16191 C CA    . ALA B  1 1024 ? 10.771  40.302  76.130  1.00 23.86 ? 1022 ALA B CA    1 
ATOM   16192 C C     . ALA B  1 1024 ? 9.474   39.773  76.730  1.00 24.40 ? 1022 ALA B C     1 
ATOM   16193 O O     . ALA B  1 1024 ? 9.250   39.841  77.944  1.00 25.27 ? 1022 ALA B O     1 
ATOM   16194 C CB    . ALA B  1 1024 ? 11.856  39.223  76.198  1.00 24.74 ? 1022 ALA B CB    1 
ATOM   16195 N N     . GLY B  1 1025 ? 8.615   39.235  75.870  1.00 21.96 ? 1023 GLY B N     1 
ATOM   16196 C CA    . GLY B  1 1025 ? 7.341   38.744  76.353  1.00 19.41 ? 1023 GLY B CA    1 
ATOM   16197 C C     . GLY B  1 1025 ? 6.479   39.847  76.913  1.00 20.40 ? 1023 GLY B C     1 
ATOM   16198 O O     . GLY B  1 1025 ? 5.660   39.599  77.798  1.00 20.62 ? 1023 GLY B O     1 
ATOM   16199 N N     . GLY B  1 1026 ? 6.666   41.068  76.432  1.00 21.32 ? 1024 GLY B N     1 
ATOM   16200 C CA    . GLY B  1 1026 ? 5.834   42.189  76.794  1.00 22.34 ? 1024 GLY B CA    1 
ATOM   16201 C C     . GLY B  1 1026 ? 5.377   42.912  75.544  1.00 21.52 ? 1024 GLY B C     1 
ATOM   16202 O O     . GLY B  1 1026 ? 5.830   42.621  74.433  1.00 21.93 ? 1024 GLY B O     1 
ATOM   16203 N N     . PRO B  1 1027 ? 4.472   43.882  75.708  1.00 22.49 ? 1025 PRO B N     1 
ATOM   16204 C CA    . PRO B  1 1027 ? 3.741   44.418  74.554  1.00 21.12 ? 1025 PRO B CA    1 
ATOM   16205 C C     . PRO B  1 1027 ? 4.502   45.449  73.745  1.00 21.88 ? 1025 PRO B C     1 
ATOM   16206 O O     . PRO B  1 1027 ? 4.024   45.823  72.671  1.00 20.19 ? 1025 PRO B O     1 
ATOM   16207 C CB    . PRO B  1 1027 ? 2.495   45.047  75.197  1.00 21.31 ? 1025 PRO B CB    1 
ATOM   16208 C CG    . PRO B  1 1027 ? 2.975   45.435  76.596  1.00 22.34 ? 1025 PRO B CG    1 
ATOM   16209 C CD    . PRO B  1 1027 ? 3.910   44.339  76.995  1.00 22.87 ? 1025 PRO B CD    1 
ATOM   16210 N N     . LEU B  1 1028 ? 5.649   45.931  74.205  1.00 21.76 ? 1026 LEU B N     1 
ATOM   16211 C CA    . LEU B  1 1028 ? 6.440   46.832  73.374  1.00 21.05 ? 1026 LEU B CA    1 
ATOM   16212 C C     . LEU B  1 1028 ? 7.420   46.112  72.470  1.00 22.94 ? 1026 LEU B C     1 
ATOM   16213 O O     . LEU B  1 1028 ? 8.075   46.765  71.654  1.00 22.61 ? 1026 LEU B O     1 
ATOM   16214 C CB    . LEU B  1 1028 ? 7.222   47.811  74.245  1.00 23.60 ? 1026 LEU B CB    1 
ATOM   16215 C CG    . LEU B  1 1028 ? 6.357   48.628  75.203  1.00 25.44 ? 1026 LEU B CG    1 
ATOM   16216 C CD1   . LEU B  1 1028 ? 7.200   49.679  75.931  1.00 23.89 ? 1026 LEU B CD1   1 
ATOM   16217 C CD2   . LEU B  1 1028 ? 5.217   49.261  74.444  1.00 29.07 ? 1026 LEU B CD2   1 
ATOM   16218 N N     . TYR B  1 1029 ? 7.553   44.795  72.606  1.00 23.55 ? 1027 TYR B N     1 
ATOM   16219 C CA    . TYR B  1 1029 ? 8.672   44.092  71.992  1.00 20.84 ? 1027 TYR B CA    1 
ATOM   16220 C C     . TYR B  1 1029 ? 8.600   44.150  70.472  1.00 22.18 ? 1027 TYR B C     1 
ATOM   16221 O O     . TYR B  1 1029 ? 9.581   44.503  69.808  1.00 21.87 ? 1027 TYR B O     1 
ATOM   16222 C CB    . TYR B  1 1029 ? 8.668   42.646  72.468  1.00 21.37 ? 1027 TYR B CB    1 
ATOM   16223 C CG    . TYR B  1 1029 ? 9.987   41.906  72.367  1.00 22.59 ? 1027 TYR B CG    1 
ATOM   16224 C CD1   . TYR B  1 1029 ? 11.071  42.247  73.177  1.00 22.45 ? 1027 TYR B CD1   1 
ATOM   16225 C CD2   . TYR B  1 1029 ? 10.120  40.812  71.528  1.00 21.72 ? 1027 TYR B CD2   1 
ATOM   16226 C CE1   . TYR B  1 1029 ? 12.243  41.551  73.112  1.00 20.70 ? 1027 TYR B CE1   1 
ATOM   16227 C CE2   . TYR B  1 1029 ? 11.298  40.097  71.460  1.00 20.48 ? 1027 TYR B CE2   1 
ATOM   16228 C CZ    . TYR B  1 1029 ? 12.356  40.467  72.260  1.00 24.97 ? 1027 TYR B CZ    1 
ATOM   16229 O OH    . TYR B  1 1029 ? 13.520  39.736  72.222  1.00 25.57 ? 1027 TYR B OH    1 
ATOM   16230 N N     . LEU B  1 1030 ? 7.441   43.795  69.902  1.00 23.22 ? 1028 LEU B N     1 
ATOM   16231 C CA    . LEU B  1 1030 ? 7.338   43.703  68.446  1.00 23.44 ? 1028 LEU B CA    1 
ATOM   16232 C C     . LEU B  1 1030 ? 7.545   45.055  67.780  1.00 24.55 ? 1028 LEU B C     1 
ATOM   16233 O O     . LEU B  1 1030 ? 8.098   45.120  66.678  1.00 23.86 ? 1028 LEU B O     1 
ATOM   16234 C CB    . LEU B  1 1030 ? 5.987   43.119  68.033  1.00 22.96 ? 1028 LEU B CB    1 
ATOM   16235 C CG    . LEU B  1 1030 ? 5.716   41.655  68.395  1.00 26.17 ? 1028 LEU B CG    1 
ATOM   16236 C CD1   . LEU B  1 1030 ? 4.415   41.204  67.750  1.00 23.36 ? 1028 LEU B CD1   1 
ATOM   16237 C CD2   . LEU B  1 1030 ? 6.910   40.734  68.010  1.00 23.63 ? 1028 LEU B CD2   1 
ATOM   16238 N N     . GLY B  1 1031 ? 7.120   46.140  68.435  1.00 24.26 ? 1029 GLY B N     1 
ATOM   16239 C CA    . GLY B  1 1031 ? 7.281   47.471  67.869  1.00 25.15 ? 1029 GLY B CA    1 
ATOM   16240 C C     . GLY B  1 1031 ? 8.720   47.853  67.576  1.00 24.24 ? 1029 GLY B C     1 
ATOM   16241 O O     . GLY B  1 1031 ? 8.964   48.744  66.761  1.00 24.60 ? 1029 GLY B O     1 
ATOM   16242 N N     . ARG B  1 1032 ? 9.682   47.190  68.207  1.00 22.62 ? 1030 ARG B N     1 
ATOM   16243 C CA    . ARG B  1 1032 ? 11.071  47.495  67.940  1.00 24.04 ? 1030 ARG B CA    1 
ATOM   16244 C C     . ARG B  1 1032 ? 11.584  46.810  66.684  1.00 24.37 ? 1030 ARG B C     1 
ATOM   16245 O O     . ARG B  1 1032 ? 12.678  47.139  66.213  1.00 26.01 ? 1030 ARG B O     1 
ATOM   16246 C CB    . ARG B  1 1032 ? 11.915  47.076  69.144  1.00 28.30 ? 1030 ARG B CB    1 
ATOM   16247 C CG    . ARG B  1 1032 ? 13.325  47.570  69.089  1.00 27.83 ? 1030 ARG B CG    1 
ATOM   16248 C CD    . ARG B  1 1032 ? 13.417  49.044  69.421  1.00 26.32 ? 1030 ARG B CD    1 
ATOM   16249 N NE    . ARG B  1 1032 ? 14.820  49.417  69.597  1.00 29.47 ? 1030 ARG B NE    1 
ATOM   16250 C CZ    . ARG B  1 1032 ? 15.463  50.322  68.872  1.00 31.46 ? 1030 ARG B CZ    1 
ATOM   16251 N NH1   . ARG B  1 1032 ? 14.857  50.997  67.905  1.00 32.55 ? 1030 ARG B NH1   1 
ATOM   16252 N NH2   . ARG B  1 1032 ? 16.750  50.545  69.110  1.00 31.82 ? 1030 ARG B NH2   1 
ATOM   16253 N N     . LEU B  1 1033 ? 10.831  45.855  66.150  1.00 24.16 ? 1031 LEU B N     1 
ATOM   16254 C CA    . LEU B  1 1033 ? 11.276  45.047  65.026  1.00 24.39 ? 1031 LEU B CA    1 
ATOM   16255 C C     . LEU B  1 1033 ? 10.606  45.454  63.724  1.00 25.78 ? 1031 LEU B C     1 
ATOM   16256 O O     . LEU B  1 1033 ? 10.662  44.699  62.750  1.00 24.57 ? 1031 LEU B O     1 
ATOM   16257 C CB    . LEU B  1 1033 ? 11.027  43.573  65.327  1.00 23.16 ? 1031 LEU B CB    1 
ATOM   16258 C CG    . LEU B  1 1033 ? 11.655  43.193  66.674  1.00 25.19 ? 1031 LEU B CG    1 
ATOM   16259 C CD1   . LEU B  1 1033 ? 11.298  41.769  67.058  1.00 26.50 ? 1031 LEU B CD1   1 
ATOM   16260 C CD2   . LEU B  1 1033 ? 13.156  43.385  66.687  1.00 24.38 ? 1031 LEU B CD2   1 
ATOM   16261 N N     . VAL B  1 1034 ? 9.962   46.626  63.701  1.00 23.15 ? 1032 VAL B N     1 
ATOM   16262 C CA    . VAL B  1 1034 ? 9.329   47.206  62.520  1.00 25.75 ? 1032 VAL B CA    1 
ATOM   16263 C C     . VAL B  1 1034 ? 9.775   48.659  62.445  1.00 27.44 ? 1032 VAL B C     1 
ATOM   16264 O O     . VAL B  1 1034 ? 10.264  49.228  63.421  1.00 27.74 ? 1032 VAL B O     1 
ATOM   16265 C CB    . VAL B  1 1034 ? 7.783   47.114  62.553  1.00 27.06 ? 1032 VAL B CB    1 
ATOM   16266 C CG1   . VAL B  1 1034 ? 7.309   45.687  62.286  1.00 25.73 ? 1032 VAL B CG1   1 
ATOM   16267 C CG2   . VAL B  1 1034 ? 7.238   47.607  63.891  1.00 22.35 ? 1032 VAL B CG2   1 
ATOM   16268 N N     . THR B  1 1035 ? 9.622   49.266  61.267  1.00 26.98 ? 1033 THR B N     1 
ATOM   16269 C CA    . THR B  1 1035 ? 10.149  50.618  61.106  1.00 31.19 ? 1033 THR B CA    1 
ATOM   16270 C C     . THR B  1 1035 ? 9.184   51.688  61.588  1.00 32.50 ? 1033 THR B C     1 
ATOM   16271 O O     . THR B  1 1035 ? 9.612   52.820  61.836  1.00 34.49 ? 1033 THR B O     1 
ATOM   16272 C CB    . THR B  1 1035 ? 10.526  50.877  59.646  1.00 34.07 ? 1033 THR B CB    1 
ATOM   16273 O OG1   . THR B  1 1035 ? 9.498   50.363  58.799  1.00 34.91 ? 1033 THR B OG1   1 
ATOM   16274 C CG2   . THR B  1 1035 ? 11.848  50.198  59.313  1.00 36.43 ? 1033 THR B CG2   1 
ATOM   16275 N N     . THR B  1 1036 ? 7.903   51.355  61.722  1.00 31.40 ? 1034 THR B N     1 
ATOM   16276 C CA    . THR B  1 1036 ? 6.918   52.188  62.399  1.00 30.13 ? 1034 THR B CA    1 
ATOM   16277 C C     . THR B  1 1036 ? 6.234   51.335  63.452  1.00 29.72 ? 1034 THR B C     1 
ATOM   16278 O O     . THR B  1 1036 ? 5.543   50.373  63.110  1.00 27.05 ? 1034 THR B O     1 
ATOM   16279 C CB    . THR B  1 1036 ? 5.875   52.734  61.423  1.00 33.52 ? 1034 THR B CB    1 
ATOM   16280 O OG1   . THR B  1 1036 ? 6.533   53.428  60.358  1.00 38.68 ? 1034 THR B OG1   1 
ATOM   16281 C CG2   . THR B  1 1036 ? 4.932   53.689  62.148  1.00 33.59 ? 1034 THR B CG2   1 
ATOM   16282 N N     . ALA B  1 1037 ? 6.402   51.692  64.717  1.00 28.42 ? 1035 ALA B N     1 
ATOM   16283 C CA    . ALA B  1 1037 ? 5.847   50.868  65.782  1.00 26.85 ? 1035 ALA B CA    1 
ATOM   16284 C C     . ALA B  1 1037 ? 4.329   51.040  65.866  1.00 29.92 ? 1035 ALA B C     1 
ATOM   16285 O O     . ALA B  1 1037 ? 3.819   52.159  65.766  1.00 31.14 ? 1035 ALA B O     1 
ATOM   16286 C CB    . ALA B  1 1037 ? 6.495   51.218  67.121  1.00 27.22 ? 1035 ALA B CB    1 
ATOM   16287 N N     . PRO B  1 1038 ? 3.583   49.955  66.039  1.00 23.44 ? 1036 PRO B N     1 
ATOM   16288 C CA    . PRO B  1 1038 ? 2.142   50.079  66.284  1.00 26.50 ? 1036 PRO B CA    1 
ATOM   16289 C C     . PRO B  1 1038 ? 1.877   50.560  67.703  1.00 26.70 ? 1036 PRO B C     1 
ATOM   16290 O O     . PRO B  1 1038 ? 2.777   50.676  68.538  1.00 23.04 ? 1036 PRO B O     1 
ATOM   16291 C CB    . PRO B  1 1038 ? 1.619   48.658  66.094  1.00 24.63 ? 1036 PRO B CB    1 
ATOM   16292 C CG    . PRO B  1 1038 ? 2.792   47.799  66.571  1.00 27.01 ? 1036 PRO B CG    1 
ATOM   16293 C CD    . PRO B  1 1038 ? 4.053   48.560  66.151  1.00 25.45 ? 1036 PRO B CD    1 
ATOM   16294 N N     . VAL B  1 1039 ? 0.602   50.822  67.969  1.00 26.96 ? 1037 VAL B N     1 
ATOM   16295 C CA    . VAL B  1 1039 ? 0.118   51.097  69.320  1.00 21.70 ? 1037 VAL B CA    1 
ATOM   16296 C C     . VAL B  1 1039 ? -0.160  49.750  69.981  1.00 22.57 ? 1037 VAL B C     1 
ATOM   16297 O O     . VAL B  1 1039 ? -1.079  49.041  69.543  1.00 22.45 ? 1037 VAL B O     1 
ATOM   16298 C CB    . VAL B  1 1039 ? -1.141  51.974  69.287  1.00 28.48 ? 1037 VAL B CB    1 
ATOM   16299 C CG1   . VAL B  1 1039 ? -1.696  52.227  70.715  1.00 25.53 ? 1037 VAL B CG1   1 
ATOM   16300 C CG2   . VAL B  1 1039 ? -0.837  53.284  68.575  1.00 27.32 ? 1037 VAL B CG2   1 
ATOM   16301 N N     . PRO B  1 1040 ? 0.587   49.358  71.005  1.00 22.73 ? 1038 PRO B N     1 
ATOM   16302 C CA    . PRO B  1 1040 ? 0.360   48.040  71.631  1.00 23.78 ? 1038 PRO B CA    1 
ATOM   16303 C C     . PRO B  1 1040 ? -1.010  47.971  72.290  1.00 23.01 ? 1038 PRO B C     1 
ATOM   16304 O O     . PRO B  1 1040 ? -1.591  49.012  72.622  1.00 24.51 ? 1038 PRO B O     1 
ATOM   16305 C CB    . PRO B  1 1040 ? 1.486   47.946  72.671  1.00 24.47 ? 1038 PRO B CB    1 
ATOM   16306 C CG    . PRO B  1 1040 ? 2.500   48.998  72.257  1.00 23.33 ? 1038 PRO B CG    1 
ATOM   16307 C CD    . PRO B  1 1040 ? 1.710   50.092  71.608  1.00 24.69 ? 1038 PRO B CD    1 
ATOM   16308 N N     . PRO B  1 1041 ? -1.555  46.765  72.512  1.00 22.68 ? 1039 PRO B N     1 
ATOM   16309 C CA    . PRO B  1 1041 ? -2.795  46.638  73.285  1.00 24.90 ? 1039 PRO B CA    1 
ATOM   16310 C C     . PRO B  1 1041 ? -2.670  47.302  74.646  1.00 25.42 ? 1039 PRO B C     1 
ATOM   16311 O O     . PRO B  1 1041 ? -1.632  47.214  75.303  1.00 24.75 ? 1039 PRO B O     1 
ATOM   16312 C CB    . PRO B  1 1041 ? -2.972  45.120  73.428  1.00 25.75 ? 1039 PRO B CB    1 
ATOM   16313 C CG    . PRO B  1 1041 ? -2.175  44.542  72.328  1.00 24.49 ? 1039 PRO B CG    1 
ATOM   16314 C CD    . PRO B  1 1041 ? -1.018  45.450  72.129  1.00 26.42 ? 1039 PRO B CD    1 
ATOM   16315 N N     . GLN B  1 1042 ? -3.740  47.982  75.056  1.00 23.19 ? 1040 GLN B N     1 
ATOM   16316 C CA    . GLN B  1 1042 ? -3.865  48.581  76.384  1.00 27.96 ? 1040 GLN B CA    1 
ATOM   16317 C C     . GLN B  1 1042 ? -2.822  49.660  76.647  1.00 24.66 ? 1040 GLN B C     1 
ATOM   16318 O O     . GLN B  1 1042 ? -2.640  50.091  77.786  1.00 20.84 ? 1040 GLN B O     1 
ATOM   16319 C CB    . GLN B  1 1042 ? -3.781  47.518  77.486  1.00 28.47 ? 1040 GLN B CB    1 
ATOM   16320 C CG    . GLN B  1 1042 ? -4.765  46.386  77.327  1.00 29.02 ? 1040 GLN B CG    1 
ATOM   16321 C CD    . GLN B  1 1042 ? -4.794  45.517  78.561  1.00 37.06 ? 1040 GLN B CD    1 
ATOM   16322 O OE1   . GLN B  1 1042 ? -3.889  44.723  78.786  1.00 40.75 ? 1040 GLN B OE1   1 
ATOM   16323 N NE2   . GLN B  1 1042 ? -5.819  45.694  79.385  1.00 42.29 ? 1040 GLN B NE2   1 
ATOM   16324 N N     . HIS B  1 1043 ? -2.140  50.142  75.620  1.00 20.46 ? 1041 HIS B N     1 
ATOM   16325 C CA    . HIS B  1 1043 ? -1.024  51.072  75.815  1.00 22.99 ? 1041 HIS B CA    1 
ATOM   16326 C C     . HIS B  1 1043 ? -1.528  52.510  75.718  1.00 24.40 ? 1041 HIS B C     1 
ATOM   16327 O O     . HIS B  1 1043 ? -1.593  53.103  74.640  1.00 26.40 ? 1041 HIS B O     1 
ATOM   16328 C CB    . HIS B  1 1043 ? 0.069   50.778  74.801  1.00 21.39 ? 1041 HIS B CB    1 
ATOM   16329 C CG    . HIS B  1 1043 ? 1.257   51.680  74.889  1.00 26.70 ? 1041 HIS B CG    1 
ATOM   16330 N ND1   . HIS B  1 1043 ? 2.357   51.381  75.660  1.00 22.23 ? 1041 HIS B ND1   1 
ATOM   16331 C CD2   . HIS B  1 1043 ? 1.533   52.856  74.275  1.00 25.52 ? 1041 HIS B CD2   1 
ATOM   16332 C CE1   . HIS B  1 1043 ? 3.257   52.341  75.529  1.00 24.90 ? 1041 HIS B CE1   1 
ATOM   16333 N NE2   . HIS B  1 1043 ? 2.780   53.249  74.695  1.00 24.96 ? 1041 HIS B NE2   1 
ATOM   16334 N N     . SER B  1 1044 ? -1.861  53.090  76.866  1.00 21.55 ? 1042 SER B N     1 
ATOM   16335 C CA    . SER B  1 1044 ? -2.327  54.473  76.918  1.00 23.10 ? 1042 SER B CA    1 
ATOM   16336 C C     . SER B  1 1044 ? -2.343  54.895  78.378  1.00 24.16 ? 1042 SER B C     1 
ATOM   16337 O O     . SER B  1 1044 ? -2.268  54.059  79.278  1.00 25.87 ? 1042 SER B O     1 
ATOM   16338 C CB    . SER B  1 1044 ? -3.723  54.624  76.305  1.00 21.65 ? 1042 SER B CB    1 
ATOM   16339 O OG    . SER B  1 1044 ? -4.674  54.101  77.209  1.00 24.87 ? 1042 SER B OG    1 
ATOM   16340 N N     . SER B  1 1045 ? -2.480  56.198  78.603  1.00 21.10 ? 1043 SER B N     1 
ATOM   16341 C CA    . SER B  1 1045 ? -2.491  56.736  79.957  1.00 19.36 ? 1043 SER B CA    1 
ATOM   16342 C C     . SER B  1 1045 ? -3.331  58.002  79.973  1.00 20.79 ? 1043 SER B C     1 
ATOM   16343 O O     . SER B  1 1045 ? -3.272  58.792  79.031  1.00 22.99 ? 1043 SER B O     1 
ATOM   16344 C CB    . SER B  1 1045 ? -1.065  57.052  80.421  1.00 21.09 ? 1043 SER B CB    1 
ATOM   16345 O OG    . SER B  1 1045 ? -1.047  57.622  81.714  1.00 22.53 ? 1043 SER B OG    1 
ATOM   16346 N N     . VAL B  1 1046 ? -4.097  58.203  81.054  1.00 20.18 ? 1044 VAL B N     1 
ATOM   16347 C CA    . VAL B  1 1046 ? -4.892  59.425  81.190  1.00 25.22 ? 1044 VAL B CA    1 
ATOM   16348 C C     . VAL B  1 1046 ? -4.109  60.546  81.855  1.00 21.62 ? 1044 VAL B C     1 
ATOM   16349 O O     . VAL B  1 1046 ? -4.612  61.673  81.941  1.00 26.16 ? 1044 VAL B O     1 
ATOM   16350 C CB    . VAL B  1 1046 ? -6.203  59.221  81.991  1.00 21.92 ? 1044 VAL B CB    1 
ATOM   16351 C CG1   . VAL B  1 1046 ? -7.155  58.306  81.245  1.00 27.91 ? 1044 VAL B CG1   1 
ATOM   16352 C CG2   . VAL B  1 1046 ? -5.916  58.671  83.378  1.00 25.37 ? 1044 VAL B CG2   1 
ATOM   16353 N N     . HIS B  1 1047 ? -2.890  60.283  82.307  1.00 23.67 ? 1045 HIS B N     1 
ATOM   16354 C CA    A HIS B  1 1047 ? -2.126  61.320  82.960  0.45 23.70 ? 1045 HIS B CA    1 
ATOM   16355 C CA    B HIS B  1 1047 ? -2.036  61.266  82.979  0.55 23.72 ? 1045 HIS B CA    1 
ATOM   16356 C C     . HIS B  1 1047 ? -1.270  62.083  81.953  1.00 23.25 ? 1045 HIS B C     1 
ATOM   16357 O O     . HIS B  1 1047 ? -0.790  61.534  80.954  1.00 25.69 ? 1045 HIS B O     1 
ATOM   16358 C CB    A HIS B  1 1047 ? -1.306  60.690  84.079  0.45 24.10 ? 1045 HIS B CB    1 
ATOM   16359 C CB    B HIS B  1 1047 ? -1.033  60.550  83.901  0.55 23.81 ? 1045 HIS B CB    1 
ATOM   16360 C CG    A HIS B  1 1047 ? -2.145  59.858  85.001  0.45 23.73 ? 1045 HIS B CG    1 
ATOM   16361 C CG    B HIS B  1 1047 ? 0.172   61.371  84.286  0.55 23.91 ? 1045 HIS B CG    1 
ATOM   16362 N ND1   A HIS B  1 1047 ? -3.034  60.413  85.900  0.45 24.76 ? 1045 HIS B ND1   1 
ATOM   16363 N ND1   B HIS B  1 1047 ? 0.123   62.374  85.237  0.55 23.16 ? 1045 HIS B ND1   1 
ATOM   16364 C CD2   A HIS B  1 1047 ? -2.280  58.515  85.119  0.45 22.98 ? 1045 HIS B CD2   1 
ATOM   16365 C CD2   B HIS B  1 1047 ? 1.467   61.304  83.878  0.55 23.89 ? 1045 HIS B CD2   1 
ATOM   16366 C CE1   A HIS B  1 1047 ? -3.656  59.447  86.552  0.45 22.17 ? 1045 HIS B CE1   1 
ATOM   16367 C CE1   B HIS B  1 1047 ? 1.329   62.902  85.378  0.55 26.58 ? 1045 HIS B CE1   1 
ATOM   16368 N NE2   A HIS B  1 1047 ? -3.215  58.286  86.098  0.45 23.55 ? 1045 HIS B NE2   1 
ATOM   16369 N NE2   B HIS B  1 1047 ? 2.163   62.271  84.564  0.55 20.47 ? 1045 HIS B NE2   1 
ATOM   16370 N N     . THR B  1 1048 ? -1.146  63.378  82.195  1.00 22.24 ? 1046 THR B N     1 
ATOM   16371 C CA    . THR B  1 1048 ? -0.317  64.256  81.379  1.00 22.37 ? 1046 THR B CA    1 
ATOM   16372 C C     . THR B  1 1048 ? 0.787   64.817  82.262  1.00 21.08 ? 1046 THR B C     1 
ATOM   16373 O O     . THR B  1 1048 ? 0.512   65.348  83.345  1.00 24.07 ? 1046 THR B O     1 
ATOM   16374 C CB    . THR B  1 1048 ? -1.121  65.403  80.765  1.00 27.86 ? 1046 THR B CB    1 
ATOM   16375 O OG1   . THR B  1 1048 ? -2.329  64.893  80.208  1.00 27.36 ? 1046 THR B OG1   1 
ATOM   16376 C CG2   . THR B  1 1048 ? -0.316  66.087  79.639  1.00 28.35 ? 1046 THR B CG2   1 
ATOM   16377 N N     . ASP B  1 1049 ? 2.022   64.690  81.811  1.00 21.30 ? 1047 ASP B N     1 
ATOM   16378 C CA    . ASP B  1 1049 ? 3.132   65.202  82.592  1.00 22.18 ? 1047 ASP B CA    1 
ATOM   16379 C C     . ASP B  1 1049 ? 2.931   66.699  82.821  1.00 22.94 ? 1047 ASP B C     1 
ATOM   16380 O O     . ASP B  1 1049 ? 2.629   67.430  81.873  1.00 25.12 ? 1047 ASP B O     1 
ATOM   16381 C CB    . ASP B  1 1049 ? 4.447   64.910  81.869  1.00 23.53 ? 1047 ASP B CB    1 
ATOM   16382 C CG    . ASP B  1 1049 ? 5.646   65.340  82.657  1.00 24.52 ? 1047 ASP B CG    1 
ATOM   16383 O OD1   . ASP B  1 1049 ? 6.001   66.532  82.566  1.00 27.60 ? 1047 ASP B OD1   1 
ATOM   16384 O OD2   . ASP B  1 1049 ? 6.216   64.494  83.374  1.00 26.07 ? 1047 ASP B OD2   1 
ATOM   16385 N N     . PRO B  1 1050 ? 3.028   67.185  84.060  1.00 20.99 ? 1048 PRO B N     1 
ATOM   16386 C CA    . PRO B  1 1050 ? 2.762   68.618  84.290  1.00 26.08 ? 1048 PRO B CA    1 
ATOM   16387 C C     . PRO B  1 1050 ? 3.847   69.537  83.745  1.00 26.41 ? 1048 PRO B C     1 
ATOM   16388 O O     . PRO B  1 1050 ? 3.547   70.682  83.385  1.00 26.73 ? 1048 PRO B O     1 
ATOM   16389 C CB    . PRO B  1 1050 ? 2.653   68.710  85.820  1.00 25.60 ? 1048 PRO B CB    1 
ATOM   16390 C CG    . PRO B  1 1050 ? 3.460   67.576  86.318  1.00 27.41 ? 1048 PRO B CG    1 
ATOM   16391 C CD    . PRO B  1 1050 ? 3.271   66.455  85.313  1.00 25.04 ? 1048 PRO B CD    1 
ATOM   16392 N N     . VAL B  1 1051 ? 5.096   69.071  83.674  1.00 25.38 ? 1049 VAL B N     1 
ATOM   16393 C CA    . VAL B  1 1051 ? 6.165   69.888  83.103  1.00 28.05 ? 1049 VAL B CA    1 
ATOM   16394 C C     . VAL B  1 1051 ? 5.980   70.032  81.597  1.00 26.24 ? 1049 VAL B C     1 
ATOM   16395 O O     . VAL B  1 1051 ? 6.197   71.113  81.032  1.00 27.63 ? 1049 VAL B O     1 
ATOM   16396 C CB    . VAL B  1 1051 ? 7.541   69.299  83.462  1.00 26.08 ? 1049 VAL B CB    1 
ATOM   16397 C CG1   . VAL B  1 1051 ? 8.650   70.152  82.835  1.00 26.67 ? 1049 VAL B CG1   1 
ATOM   16398 C CG2   . VAL B  1 1051 ? 7.714   69.243  84.980  1.00 27.28 ? 1049 VAL B CG2   1 
ATOM   16399 N N     . LEU B  1 1052 ? 5.568   68.955  80.920  1.00 26.96 ? 1050 LEU B N     1 
ATOM   16400 C CA    . LEU B  1 1052 ? 5.183   69.057  79.511  1.00 25.11 ? 1050 LEU B CA    1 
ATOM   16401 C C     . LEU B  1 1052 ? 4.140   70.152  79.308  1.00 28.61 ? 1050 LEU B C     1 
ATOM   16402 O O     . LEU B  1 1052 ? 4.226   70.943  78.361  1.00 24.56 ? 1050 LEU B O     1 
ATOM   16403 C CB    . LEU B  1 1052 ? 4.659   67.709  79.001  1.00 22.67 ? 1050 LEU B CB    1 
ATOM   16404 C CG    . LEU B  1 1052 ? 4.155   67.527  77.546  1.00 22.81 ? 1050 LEU B CG    1 
ATOM   16405 C CD1   . LEU B  1 1052 ? 2.722   68.048  77.343  1.00 25.50 ? 1050 LEU B CD1   1 
ATOM   16406 C CD2   . LEU B  1 1052 ? 5.130   68.157  76.516  1.00 22.31 ? 1050 LEU B CD2   1 
ATOM   16407 N N     . LEU B  1 1053 ? 3.128   70.193  80.180  1.00 25.03 ? 1051 LEU B N     1 
ATOM   16408 C CA    . LEU B  1 1053 ? 2.105   71.230  80.090  1.00 27.92 ? 1051 LEU B CA    1 
ATOM   16409 C C     . LEU B  1 1053 ? 2.715   72.621  80.210  1.00 29.06 ? 1051 LEU B C     1 
ATOM   16410 O O     . LEU B  1 1053 ? 2.364   73.531  79.450  1.00 29.44 ? 1051 LEU B O     1 
ATOM   16411 C CB    . LEU B  1 1053 ? 1.037   71.008  81.170  1.00 29.75 ? 1051 LEU B CB    1 
ATOM   16412 C CG    . LEU B  1 1053 ? 0.101   69.810  80.927  1.00 29.46 ? 1051 LEU B CG    1 
ATOM   16413 C CD1   . LEU B  1 1053 ? -0.746  69.469  82.149  1.00 30.85 ? 1051 LEU B CD1   1 
ATOM   16414 C CD2   . LEU B  1 1053 ? -0.784  70.066  79.729  1.00 27.85 ? 1051 LEU B CD2   1 
ATOM   16415 N N     . ASP B  1 1054 ? 3.622   72.810  81.172  1.00 29.14 ? 1052 ASP B N     1 
ATOM   16416 C CA    . ASP B  1 1054 ? 4.265   74.116  81.330  1.00 28.86 ? 1052 ASP B CA    1 
ATOM   16417 C C     . ASP B  1 1054 ? 5.077   74.479  80.091  1.00 28.09 ? 1052 ASP B C     1 
ATOM   16418 O O     . ASP B  1 1054 ? 5.102   75.642  79.673  1.00 27.22 ? 1052 ASP B O     1 
ATOM   16419 C CB    . ASP B  1 1054 ? 5.162   74.124  82.568  1.00 32.18 ? 1052 ASP B CB    1 
ATOM   16420 C CG    . ASP B  1 1054 ? 4.379   74.057  83.868  1.00 34.90 ? 1052 ASP B CG    1 
ATOM   16421 O OD1   . ASP B  1 1054 ? 3.189   74.420  83.869  1.00 32.67 ? 1052 ASP B OD1   1 
ATOM   16422 O OD2   . ASP B  1 1054 ? 4.964   73.650  84.898  1.00 37.15 ? 1052 ASP B OD2   1 
ATOM   16423 N N     . PHE B  1 1055 ? 5.759   73.492  79.502  1.00 30.17 ? 1053 PHE B N     1 
ATOM   16424 C CA    . PHE B  1 1055 ? 6.512   73.721  78.271  1.00 26.26 ? 1053 PHE B CA    1 
ATOM   16425 C C     . PHE B  1 1055 ? 5.592   74.127  77.126  1.00 31.73 ? 1053 PHE B C     1 
ATOM   16426 O O     . PHE B  1 1055 ? 5.908   75.049  76.365  1.00 28.96 ? 1053 PHE B O     1 
ATOM   16427 C CB    . PHE B  1 1055 ? 7.305   72.459  77.921  1.00 26.88 ? 1053 PHE B CB    1 
ATOM   16428 C CG    . PHE B  1 1055 ? 8.205   72.608  76.727  1.00 26.19 ? 1053 PHE B CG    1 
ATOM   16429 C CD1   . PHE B  1 1055 ? 9.181   73.596  76.692  1.00 27.23 ? 1053 PHE B CD1   1 
ATOM   16430 C CD2   . PHE B  1 1055 ? 8.099   71.735  75.657  1.00 27.38 ? 1053 PHE B CD2   1 
ATOM   16431 C CE1   . PHE B  1 1055 ? 10.015  73.716  75.587  1.00 29.13 ? 1053 PHE B CE1   1 
ATOM   16432 C CE2   . PHE B  1 1055 ? 8.928   71.847  74.551  1.00 26.16 ? 1053 PHE B CE2   1 
ATOM   16433 C CZ    . PHE B  1 1055 ? 9.885   72.841  74.515  1.00 27.60 ? 1053 PHE B CZ    1 
ATOM   16434 N N     . ALA B  1 1056 ? 4.437   73.460  76.995  1.00 29.53 ? 1054 ALA B N     1 
ATOM   16435 C CA    . ALA B  1 1056 ? 3.484   73.812  75.941  1.00 30.30 ? 1054 ALA B CA    1 
ATOM   16436 C C     . ALA B  1 1056 ? 3.001   75.253  76.072  1.00 29.32 ? 1054 ALA B C     1 
ATOM   16437 O O     . ALA B  1 1056 ? 2.840   75.954  75.067  1.00 31.41 ? 1054 ALA B O     1 
ATOM   16438 C CB    . ALA B  1 1056 ? 2.290   72.858  75.965  1.00 31.59 ? 1054 ALA B CB    1 
ATOM   16439 N N     . LYS B  1 1057 ? 2.741   75.708  77.297  1.00 29.91 ? 1055 LYS B N     1 
ATOM   16440 C CA    . LYS B  1 1057 ? 2.277   77.085  77.469  1.00 33.46 ? 1055 LYS B CA    1 
ATOM   16441 C C     . LYS B  1 1057 ? 3.378   78.078  77.127  1.00 32.39 ? 1055 LYS B C     1 
ATOM   16442 O O     . LYS B  1 1057 ? 3.118   79.123  76.516  1.00 35.33 ? 1055 LYS B O     1 
ATOM   16443 C CB    . LYS B  1 1057 ? 1.799   77.316  78.901  1.00 34.60 ? 1055 LYS B CB    1 
ATOM   16444 C CG    . LYS B  1 1057 ? 0.490   76.634  79.240  1.00 34.83 ? 1055 LYS B CG    1 
ATOM   16445 C CD    . LYS B  1 1057 ? 0.070   76.932  80.670  1.00 35.43 ? 1055 LYS B CD    1 
ATOM   16446 C CE    . LYS B  1 1057 ? 1.056   76.359  81.669  1.00 33.32 ? 1055 LYS B CE    1 
ATOM   16447 N NZ    . LYS B  1 1057 ? 0.517   76.459  83.067  1.00 35.14 ? 1055 LYS B NZ    1 
ATOM   16448 N N     . TRP B  1 1058 ? 4.610   77.775  77.540  1.00 31.00 ? 1056 TRP B N     1 
ATOM   16449 C CA    . TRP B  1 1058 ? 5.756   78.589  77.150  1.00 31.46 ? 1056 TRP B CA    1 
ATOM   16450 C C     . TRP B  1 1058 ? 5.876   78.683  75.632  1.00 31.57 ? 1056 TRP B C     1 
ATOM   16451 O O     . TRP B  1 1058 ? 6.102   79.769  75.088  1.00 34.21 ? 1056 TRP B O     1 
ATOM   16452 C CB    . TRP B  1 1058 ? 7.025   77.997  77.767  1.00 31.46 ? 1056 TRP B CB    1 
ATOM   16453 C CG    . TRP B  1 1058 ? 8.287   78.752  77.475  1.00 36.13 ? 1056 TRP B CG    1 
ATOM   16454 C CD1   . TRP B  1 1058 ? 8.692   79.918  78.046  1.00 36.49 ? 1056 TRP B CD1   1 
ATOM   16455 C CD2   . TRP B  1 1058 ? 9.324   78.368  76.565  1.00 35.03 ? 1056 TRP B CD2   1 
ATOM   16456 N NE1   . TRP B  1 1058 ? 9.911   80.299  77.536  1.00 39.08 ? 1056 TRP B NE1   1 
ATOM   16457 C CE2   . TRP B  1 1058 ? 10.321  79.366  76.622  1.00 38.48 ? 1056 TRP B CE2   1 
ATOM   16458 C CE3   . TRP B  1 1058 ? 9.504   77.286  75.699  1.00 35.77 ? 1056 TRP B CE3   1 
ATOM   16459 C CZ2   . TRP B  1 1058 ? 11.484  79.309  75.854  1.00 36.61 ? 1056 TRP B CZ2   1 
ATOM   16460 C CZ3   . TRP B  1 1058 ? 10.666  77.235  74.923  1.00 38.20 ? 1056 TRP B CZ3   1 
ATOM   16461 C CH2   . TRP B  1 1058 ? 11.635  78.240  75.010  1.00 36.47 ? 1056 TRP B CH2   1 
ATOM   16462 N N     . LEU B  1 1059 ? 5.720   77.559  74.927  1.00 31.99 ? 1057 LEU B N     1 
ATOM   16463 C CA    . LEU B  1 1059 ? 5.773   77.595  73.466  1.00 33.75 ? 1057 LEU B CA    1 
ATOM   16464 C C     . LEU B  1 1059 ? 4.653   78.458  72.886  1.00 38.19 ? 1057 LEU B C     1 
ATOM   16465 O O     . LEU B  1 1059 ? 4.873   79.207  71.923  1.00 40.38 ? 1057 LEU B O     1 
ATOM   16466 C CB    . LEU B  1 1059 ? 5.715   76.178  72.905  1.00 29.09 ? 1057 LEU B CB    1 
ATOM   16467 C CG    . LEU B  1 1059 ? 6.896   75.277  73.276  1.00 31.29 ? 1057 LEU B CG    1 
ATOM   16468 C CD1   . LEU B  1 1059 ? 6.613   73.866  72.809  1.00 29.87 ? 1057 LEU B CD1   1 
ATOM   16469 C CD2   . LEU B  1 1059 ? 8.207   75.805  72.649  1.00 31.49 ? 1057 LEU B CD2   1 
ATOM   16470 N N     . ASP B  1 1060 ? 3.443   78.365  73.456  1.00 35.74 ? 1058 ASP B N     1 
ATOM   16471 C CA    . ASP B  1 1060 ? 2.348   79.241  73.039  1.00 38.53 ? 1058 ASP B CA    1 
ATOM   16472 C C     . ASP B  1 1060 ? 2.708   80.709  73.235  1.00 39.08 ? 1058 ASP B C     1 
ATOM   16473 O O     . ASP B  1 1060 ? 2.382   81.554  72.392  1.00 40.25 ? 1058 ASP B O     1 
ATOM   16474 C CB    . ASP B  1 1060 ? 1.069   78.918  73.824  1.00 40.99 ? 1058 ASP B CB    1 
ATOM   16475 C CG    . ASP B  1 1060 ? 0.360   77.671  73.323  1.00 40.56 ? 1058 ASP B CG    1 
ATOM   16476 O OD1   . ASP B  1 1060 ? 0.358   77.438  72.101  1.00 47.17 ? 1058 ASP B OD1   1 
ATOM   16477 O OD2   . ASP B  1 1060 ? -0.209  76.937  74.162  1.00 42.91 ? 1058 ASP B OD2   1 
ATOM   16478 N N     . GLY B  1 1061 ? 3.359   81.032  74.356  1.00 37.34 ? 1059 GLY B N     1 
ATOM   16479 C CA    . GLY B  1 1061 ? 3.732   82.413  74.614  1.00 44.14 ? 1059 GLY B CA    1 
ATOM   16480 C C     . GLY B  1 1061 ? 4.674   82.968  73.564  1.00 43.61 ? 1059 GLY B C     1 
ATOM   16481 O O     . GLY B  1 1061 ? 4.588   84.140  73.199  1.00 44.52 ? 1059 GLY B O     1 
ATOM   16482 N N     . LYS B  1 1062 ? 5.579   82.130  73.059  1.00 42.55 ? 1060 LYS B N     1 
ATOM   16483 C CA    . LYS B  1 1062 ? 6.562   82.544  72.063  1.00 45.22 ? 1060 LYS B CA    1 
ATOM   16484 C C     . LYS B  1 1062 ? 5.999   82.595  70.654  1.00 46.73 ? 1060 LYS B C     1 
ATOM   16485 O O     . LYS B  1 1062 ? 6.692   83.073  69.749  1.00 47.90 ? 1060 LYS B O     1 
ATOM   16486 C CB    . LYS B  1 1062 ? 7.748   81.587  72.070  1.00 43.62 ? 1060 LYS B CB    1 
ATOM   16487 C CG    . LYS B  1 1062 ? 8.577   81.624  73.315  1.00 43.62 ? 1060 LYS B CG    1 
ATOM   16488 C CD    . LYS B  1 1062 ? 9.399   80.361  73.387  1.00 41.62 ? 1060 LYS B CD    1 
ATOM   16489 C CE    . LYS B  1 1062 ? 10.103  80.093  72.065  1.00 44.48 ? 1060 LYS B CE    1 
ATOM   16490 N NZ    . LYS B  1 1062 ? 11.215  81.044  71.819  1.00 41.72 ? 1060 LYS B NZ    1 
ATOM   16491 N N     . GLY B  1 1063 ? 4.781   82.105  70.446  1.00 43.45 ? 1061 GLY B N     1 
ATOM   16492 C CA    . GLY B  1 1063 ? 4.234   81.996  69.115  1.00 42.01 ? 1061 GLY B CA    1 
ATOM   16493 C C     . GLY B  1 1063 ? 4.666   80.766  68.359  1.00 43.96 ? 1061 GLY B C     1 
ATOM   16494 O O     . GLY B  1 1063 ? 4.330   80.636  67.175  1.00 43.74 ? 1061 GLY B O     1 
ATOM   16495 N N     . ALA B  1 1064 ? 5.394   79.852  69.005  1.00 40.60 ? 1062 ALA B N     1 
ATOM   16496 C CA    . ALA B  1 1064 ? 5.835   78.610  68.371  1.00 37.18 ? 1062 ALA B CA    1 
ATOM   16497 C C     . ALA B  1 1064 ? 4.656   77.639  68.318  1.00 37.83 ? 1062 ALA B C     1 
ATOM   16498 O O     . ALA B  1 1064 ? 4.588   76.641  69.041  1.00 34.49 ? 1062 ALA B O     1 
ATOM   16499 C CB    . ALA B  1 1064 ? 7.019   78.022  69.123  1.00 35.92 ? 1062 ALA B CB    1 
ATOM   16500 N N     . ARG B  1 1065 ? 3.719   77.942  67.414  1.00 40.08 ? 1063 ARG B N     1 
ATOM   16501 C CA    . ARG B  1 1065 ? 2.413   77.282  67.439  1.00 38.85 ? 1063 ARG B CA    1 
ATOM   16502 C C     . ARG B  1 1065 ? 2.509   75.816  67.027  1.00 37.20 ? 1063 ARG B C     1 
ATOM   16503 O O     . ARG B  1 1065 ? 1.899   74.950  67.666  1.00 37.13 ? 1063 ARG B O     1 
ATOM   16504 C CB    . ARG B  1 1065 ? 1.425   78.031  66.537  1.00 37.76 ? 1063 ARG B CB    1 
ATOM   16505 N N     . ALA B  1 1066 ? 3.253   75.516  65.957  1.00 37.29 ? 1064 ALA B N     1 
ATOM   16506 C CA    . ALA B  1 1066 ? 3.395   74.126  65.525  1.00 35.51 ? 1064 ALA B CA    1 
ATOM   16507 C C     . ALA B  1 1066 ? 4.028   73.268  66.614  1.00 34.40 ? 1064 ALA B C     1 
ATOM   16508 O O     . ALA B  1 1066 ? 3.653   72.100  66.793  1.00 33.29 ? 1064 ALA B O     1 
ATOM   16509 C CB    . ALA B  1 1066 ? 4.232   74.048  64.254  1.00 34.38 ? 1064 ALA B CB    1 
ATOM   16510 N N     . GLU B  1 1067 ? 5.000   73.831  67.337  1.00 31.77 ? 1065 GLU B N     1 
ATOM   16511 C CA    . GLU B  1 1067 ? 5.673   73.094  68.403  1.00 33.27 ? 1065 GLU B CA    1 
ATOM   16512 C C     . GLU B  1 1067 ? 4.767   72.928  69.621  1.00 30.93 ? 1065 GLU B C     1 
ATOM   16513 O O     . GLU B  1 1067 ? 4.740   71.859  70.241  1.00 32.67 ? 1065 GLU B O     1 
ATOM   16514 C CB    . GLU B  1 1067 ? 6.976   73.806  68.787  1.00 31.13 ? 1065 GLU B CB    1 
ATOM   16515 C CG    . GLU B  1 1067 ? 8.071   73.769  67.705  1.00 32.45 ? 1065 GLU B CG    1 
ATOM   16516 C CD    . GLU B  1 1067 ? 7.821   74.730  66.546  1.00 37.78 ? 1065 GLU B CD    1 
ATOM   16517 O OE1   . GLU B  1 1067 ? 6.894   75.563  66.647  1.00 37.75 ? 1065 GLU B OE1   1 
ATOM   16518 O OE2   . GLU B  1 1067 ? 8.560   74.658  65.537  1.00 37.34 ? 1065 GLU B OE2   1 
ATOM   16519 N N     . ALA B  1 1068 ? 4.033   73.980  69.991  1.00 33.92 ? 1066 ALA B N     1 
ATOM   16520 C CA    . ALA B  1 1068 ? 3.072   73.857  71.086  1.00 34.67 ? 1066 ALA B CA    1 
ATOM   16521 C C     . ALA B  1 1068 ? 2.057   72.756  70.804  1.00 31.00 ? 1066 ALA B C     1 
ATOM   16522 O O     . ALA B  1 1068 ? 1.730   71.958  71.690  1.00 33.54 ? 1066 ALA B O     1 
ATOM   16523 C CB    . ALA B  1 1068 ? 2.365   75.189  71.316  1.00 33.86 ? 1066 ALA B CB    1 
ATOM   16524 N N     . GLU B  1 1069 ? 1.559   72.690  69.572  1.00 32.29 ? 1067 GLU B N     1 
ATOM   16525 C CA    . GLU B  1 1069 ? 0.653   71.613  69.197  1.00 33.57 ? 1067 GLU B CA    1 
ATOM   16526 C C     . GLU B  1 1069 ? 1.335   70.252  69.306  1.00 33.64 ? 1067 GLU B C     1 
ATOM   16527 O O     . GLU B  1 1069 ? 0.739   69.287  69.800  1.00 32.48 ? 1067 GLU B O     1 
ATOM   16528 C CB    . GLU B  1 1069 ? 0.132   71.858  67.778  1.00 37.66 ? 1067 GLU B CB    1 
ATOM   16529 C CG    . GLU B  1 1069 ? -0.712  70.734  67.211  1.00 40.43 ? 1067 GLU B CG    1 
ATOM   16530 C CD    . GLU B  1 1069 ? -2.145  70.760  67.726  1.00 46.26 ? 1067 GLU B CD    1 
ATOM   16531 O OE1   . GLU B  1 1069 ? -2.509  71.731  68.426  1.00 45.54 ? 1067 GLU B OE1   1 
ATOM   16532 O OE2   . GLU B  1 1069 ? -2.901  69.804  67.439  1.00 48.00 ? 1067 GLU B OE2   1 
ATOM   16533 N N     . ALA B  1 1070 ? 2.591   70.153  68.868  1.00 32.78 ? 1068 ALA B N     1 
ATOM   16534 C CA    . ALA B  1 1070 ? 3.285   68.874  68.950  1.00 32.05 ? 1068 ALA B CA    1 
ATOM   16535 C C     . ALA B  1 1070 ? 3.504   68.466  70.399  1.00 26.79 ? 1068 ALA B C     1 
ATOM   16536 O O     . ALA B  1 1070 ? 3.412   67.281  70.736  1.00 29.50 ? 1068 ALA B O     1 
ATOM   16537 C CB    . ALA B  1 1070 ? 4.618   68.944  68.201  1.00 32.60 ? 1068 ALA B CB    1 
ATOM   16538 N N     . ALA B  1 1071 ? 3.773   69.436  71.271  1.00 27.06 ? 1069 ALA B N     1 
ATOM   16539 C CA    . ALA B  1 1071 ? 3.940   69.127  72.685  1.00 25.39 ? 1069 ALA B CA    1 
ATOM   16540 C C     . ALA B  1 1071 ? 2.640   68.617  73.297  1.00 27.87 ? 1069 ALA B C     1 
ATOM   16541 O O     . ALA B  1 1071 ? 2.643   67.663  74.088  1.00 25.93 ? 1069 ALA B O     1 
ATOM   16542 C CB    . ALA B  1 1071 ? 4.419   70.364  73.432  1.00 26.24 ? 1069 ALA B CB    1 
ATOM   16543 N N     . ARG B  1 1072 ? 1.516   69.254  72.968  1.00 24.97 ? 1070 ARG B N     1 
ATOM   16544 C CA    . ARG B  1 1072 ? 0.260   68.776  73.534  1.00 23.70 ? 1070 ARG B CA    1 
ATOM   16545 C C     . ARG B  1 1072 ? -0.076  67.393  73.010  1.00 27.52 ? 1070 ARG B C     1 
ATOM   16546 O O     . ARG B  1 1072 ? -0.539  66.529  73.764  1.00 25.37 ? 1070 ARG B O     1 
ATOM   16547 C CB    . ARG B  1 1072 ? -0.862  69.770  73.250  1.00 33.25 ? 1070 ARG B CB    1 
ATOM   16548 C CG    . ARG B  1 1072 ? -0.947  70.834  74.320  1.00 36.67 ? 1070 ARG B CG    1 
ATOM   16549 C CD    . ARG B  1 1072 ? -2.171  71.707  74.136  1.00 35.61 ? 1070 ARG B CD    1 
ATOM   16550 N NE    . ARG B  1 1072 ? -1.790  73.054  73.747  1.00 38.99 ? 1070 ARG B NE    1 
ATOM   16551 C CZ    . ARG B  1 1072 ? -1.755  73.488  72.494  1.00 41.33 ? 1070 ARG B CZ    1 
ATOM   16552 N NH1   . ARG B  1 1072 ? -2.136  72.721  71.483  1.00 39.69 ? 1070 ARG B NH1   1 
ATOM   16553 N NH2   . ARG B  1 1072 ? -1.320  74.719  72.249  1.00 40.52 ? 1070 ARG B NH2   1 
ATOM   16554 N N     . ASN B  1 1073 ? 0.201   67.142  71.735  1.00 27.05 ? 1071 ASN B N     1 
ATOM   16555 C CA    . ASN B  1 1073 ? -0.053  65.819  71.186  1.00 26.34 ? 1071 ASN B CA    1 
ATOM   16556 C C     . ASN B  1 1073 ? 0.840   64.771  71.835  1.00 26.84 ? 1071 ASN B C     1 
ATOM   16557 O O     . ASN B  1 1073 ? 0.419   63.629  72.038  1.00 25.94 ? 1071 ASN B O     1 
ATOM   16558 C CB    . ASN B  1 1073 ? 0.138   65.852  69.673  1.00 29.45 ? 1071 ASN B CB    1 
ATOM   16559 C CG    . ASN B  1 1073 ? -1.011  66.551  68.972  1.00 33.57 ? 1071 ASN B CG    1 
ATOM   16560 O OD1   . ASN B  1 1073 ? -2.126  66.589  69.490  1.00 38.31 ? 1071 ASN B OD1   1 
ATOM   16561 N ND2   . ASN B  1 1073 ? -0.748  67.117  67.803  1.00 39.61 ? 1071 ASN B ND2   1 
ATOM   16562 N N     . ALA B  1 1074 ? 2.080   65.136  72.161  1.00 27.88 ? 1072 ALA B N     1 
ATOM   16563 C CA    . ALA B  1 1074 ? 2.962   64.203  72.852  1.00 25.63 ? 1072 ALA B CA    1 
ATOM   16564 C C     . ALA B  1 1074 ? 2.464   63.933  74.265  1.00 25.13 ? 1072 ALA B C     1 
ATOM   16565 O O     . ALA B  1 1074 ? 2.541   62.797  74.753  1.00 21.83 ? 1072 ALA B O     1 
ATOM   16566 C CB    . ALA B  1 1074 ? 4.388   64.759  72.887  1.00 25.64 ? 1072 ALA B CB    1 
ATOM   16567 N N     . GLY B  1 1075 ? 2.000   64.979  74.949  1.00 25.34 ? 1073 GLY B N     1 
ATOM   16568 C CA    . GLY B  1 1075 ? 1.490   64.803  76.300  1.00 26.40 ? 1073 GLY B CA    1 
ATOM   16569 C C     . GLY B  1 1075 ? 0.304   63.852  76.346  1.00 29.73 ? 1073 GLY B C     1 
ATOM   16570 O O     . GLY B  1 1075 ? 0.152   63.074  77.294  1.00 28.87 ? 1073 GLY B O     1 
ATOM   16571 N N     . SER B  1 1076 ? -0.535  63.879  75.309  1.00 24.67 ? 1074 SER B N     1 
ATOM   16572 C CA    . SER B  1 1076 ? -1.682  62.974  75.286  1.00 26.57 ? 1074 SER B CA    1 
ATOM   16573 C C     . SER B  1 1076 ? -1.282  61.562  74.885  1.00 29.06 ? 1074 SER B C     1 
ATOM   16574 O O     . SER B  1 1076 ? -1.752  60.591  75.491  1.00 31.83 ? 1074 SER B O     1 
ATOM   16575 C CB    . SER B  1 1076 ? -2.774  63.510  74.351  1.00 30.41 ? 1074 SER B CB    1 
ATOM   16576 O OG    . SER B  1 1076 ? -3.406  64.646  74.916  1.00 31.54 ? 1074 SER B OG    1 
ATOM   16577 N N     . SER B  1 1077 ? -0.418  61.413  73.881  1.00 26.38 ? 1075 SER B N     1 
ATOM   16578 C CA    . SER B  1 1077 ? -0.149  60.067  73.396  1.00 28.35 ? 1075 SER B CA    1 
ATOM   16579 C C     . SER B  1 1077 ? 0.872   59.334  74.255  1.00 26.66 ? 1075 SER B C     1 
ATOM   16580 O O     . SER B  1 1077 ? 0.996   58.111  74.128  1.00 28.93 ? 1075 SER B O     1 
ATOM   16581 C CB    . SER B  1 1077 ? 0.310   60.099  71.930  1.00 33.59 ? 1075 SER B CB    1 
ATOM   16582 O OG    . SER B  1 1077 ? 1.605   60.633  71.802  1.00 31.77 ? 1075 SER B OG    1 
ATOM   16583 N N     . SER B  1 1078 ? 1.591   60.045  75.125  1.00 23.61 ? 1076 SER B N     1 
ATOM   16584 C CA    . SER B  1 1078 ? 2.467   59.389  76.091  1.00 24.89 ? 1076 SER B CA    1 
ATOM   16585 C C     . SER B  1 1078 ? 1.669   58.375  76.897  1.00 24.73 ? 1076 SER B C     1 
ATOM   16586 O O     . SER B  1 1078 ? 0.524   58.628  77.270  1.00 26.20 ? 1076 SER B O     1 
ATOM   16587 C CB    . SER B  1 1078 ? 3.096   60.430  77.033  1.00 21.15 ? 1076 SER B CB    1 
ATOM   16588 O OG    . SER B  1 1078 ? 3.808   59.796  78.090  1.00 20.92 ? 1076 SER B OG    1 
ATOM   16589 N N     . ALA B  1 1079 ? 2.273   57.220  77.152  1.00 22.65 ? 1077 ALA B N     1 
ATOM   16590 C CA    . ALA B  1 1079 ? 1.673   56.208  78.006  1.00 22.27 ? 1077 ALA B CA    1 
ATOM   16591 C C     . ALA B  1 1079 ? 2.284   56.211  79.398  1.00 23.59 ? 1077 ALA B C     1 
ATOM   16592 O O     . ALA B  1 1079 ? 2.044   55.279  80.176  1.00 21.52 ? 1077 ALA B O     1 
ATOM   16593 C CB    . ALA B  1 1079 ? 1.802   54.824  77.367  1.00 24.81 ? 1077 ALA B CB    1 
ATOM   16594 N N     . LEU B  1 1080 ? 3.079   57.232  79.715  1.00 22.04 ? 1078 LEU B N     1 
ATOM   16595 C CA    . LEU B  1 1080 ? 3.589   57.429  81.070  1.00 21.01 ? 1078 LEU B CA    1 
ATOM   16596 C C     . LEU B  1 1080 ? 2.461   57.369  82.101  1.00 23.47 ? 1078 LEU B C     1 
ATOM   16597 O O     . LEU B  1 1080 ? 1.447   58.068  81.982  1.00 22.27 ? 1078 LEU B O     1 
ATOM   16598 C CB    . LEU B  1 1080 ? 4.299   58.779  81.148  1.00 22.29 ? 1078 LEU B CB    1 
ATOM   16599 C CG    . LEU B  1 1080 ? 4.752   59.211  82.540  1.00 22.59 ? 1078 LEU B CG    1 
ATOM   16600 C CD1   . LEU B  1 1080 ? 5.903   58.326  83.045  1.00 19.79 ? 1078 LEU B CD1   1 
ATOM   16601 C CD2   . LEU B  1 1080 ? 5.124   60.708  82.601  1.00 19.95 ? 1078 LEU B CD2   1 
ATOM   16602 N N     . GLY B  1 1081 ? 2.652   56.534  83.125  1.00 20.45 ? 1079 GLY B N     1 
ATOM   16603 C CA    . GLY B  1 1081 ? 1.658   56.361  84.166  1.00 22.35 ? 1079 GLY B CA    1 
ATOM   16604 C C     . GLY B  1 1081 ? 0.676   55.230  83.925  1.00 26.03 ? 1079 GLY B C     1 
ATOM   16605 O O     . GLY B  1 1081 ? -0.222  55.028  84.750  1.00 20.00 ? 1079 GLY B O     1 
ATOM   16606 N N     . LEU B  1 1082 ? 0.789   54.519  82.795  1.00 23.94 ? 1080 LEU B N     1 
ATOM   16607 C CA    . LEU B  1 1082 ? 0.055   53.274  82.596  1.00 24.94 ? 1080 LEU B CA    1 
ATOM   16608 C C     . LEU B  1 1082 ? 0.271   52.355  83.787  1.00 25.37 ? 1080 LEU B C     1 
ATOM   16609 O O     . LEU B  1 1082 ? 1.389   52.216  84.280  1.00 23.91 ? 1080 LEU B O     1 
ATOM   16610 C CB    . LEU B  1 1082 ? 0.526   52.587  81.307  1.00 21.69 ? 1080 LEU B CB    1 
ATOM   16611 C CG    . LEU B  1 1082 ? -0.068  51.225  80.932  1.00 21.64 ? 1080 LEU B CG    1 
ATOM   16612 C CD1   . LEU B  1 1082 ? -1.583  51.313  81.053  1.00 28.64 ? 1080 LEU B CD1   1 
ATOM   16613 C CD2   . LEU B  1 1082 ? 0.297   50.832  79.491  1.00 21.05 ? 1080 LEU B CD2   1 
ATOM   16614 N N     . ASP B  1 1083 ? -0.802  51.715  84.251  1.00 22.89 ? 1081 ASP B N     1 
ATOM   16615 C CA    . ASP B  1 1083 ? -0.700  50.899  85.463  1.00 23.34 ? 1081 ASP B CA    1 
ATOM   16616 C C     . ASP B  1 1083 ? -1.733  49.776  85.370  1.00 27.14 ? 1081 ASP B C     1 
ATOM   16617 O O     . ASP B  1 1083 ? -2.895  49.983  85.705  1.00 27.36 ? 1081 ASP B O     1 
ATOM   16618 C CB    . ASP B  1 1083 ? -0.916  51.770  86.694  1.00 28.66 ? 1081 ASP B CB    1 
ATOM   16619 C CG    . ASP B  1 1083 ? -0.849  50.986  87.994  1.00 37.40 ? 1081 ASP B CG    1 
ATOM   16620 O OD1   . ASP B  1 1083 ? -0.275  49.874  88.007  1.00 39.35 ? 1081 ASP B OD1   1 
ATOM   16621 O OD2   . ASP B  1 1083 ? -1.380  51.493  89.010  1.00 41.14 ? 1081 ASP B OD2   1 
ATOM   16622 N N     . LEU B  1 1084 ? -1.298  48.597  84.939  1.00 26.13 ? 1082 LEU B N     1 
ATOM   16623 C CA    . LEU B  1 1084 ? -2.184  47.497  84.579  1.00 24.91 ? 1082 LEU B CA    1 
ATOM   16624 C C     . LEU B  1 1084 ? -1.962  46.304  85.495  1.00 28.43 ? 1082 LEU B C     1 
ATOM   16625 O O     . LEU B  1 1084 ? -0.833  46.041  85.924  1.00 24.75 ? 1082 LEU B O     1 
ATOM   16626 C CB    . LEU B  1 1084 ? -1.923  47.050  83.141  1.00 24.07 ? 1082 LEU B CB    1 
ATOM   16627 C CG    . LEU B  1 1084 ? -2.322  48.069  82.088  1.00 26.91 ? 1082 LEU B CG    1 
ATOM   16628 C CD1   . LEU B  1 1084 ? -2.034  47.513  80.708  1.00 28.86 ? 1082 LEU B CD1   1 
ATOM   16629 C CD2   . LEU B  1 1084 ? -3.803  48.424  82.263  1.00 34.48 ? 1082 LEU B CD2   1 
ATOM   16630 N N     . GLU B  1 1085 ? -3.032  45.561  85.769  1.00 23.98 ? 1083 GLU B N     1 
ATOM   16631 C CA    . GLU B  1 1085 ? -2.885  44.221  86.316  1.00 26.83 ? 1083 GLU B CA    1 
ATOM   16632 C C     . GLU B  1 1085 ? -3.039  43.229  85.169  1.00 26.47 ? 1083 GLU B C     1 
ATOM   16633 O O     . GLU B  1 1085 ? -3.997  43.315  84.397  1.00 30.20 ? 1083 GLU B O     1 
ATOM   16634 C CB    . GLU B  1 1085 ? -3.887  43.921  87.436  1.00 25.51 ? 1083 GLU B CB    1 
ATOM   16635 C CG    . GLU B  1 1085 ? -3.774  42.466  87.906  1.00 30.52 ? 1083 GLU B CG    1 
ATOM   16636 C CD    . GLU B  1 1085 ? -4.338  42.193  89.295  1.00 33.15 ? 1083 GLU B CD    1 
ATOM   16637 O OE1   . GLU B  1 1085 ? -4.841  43.128  89.954  1.00 34.62 ? 1083 GLU B OE1   1 
ATOM   16638 O OE2   . GLU B  1 1085 ? -4.243  41.028  89.745  1.00 34.69 ? 1083 GLU B OE2   1 
ATOM   16639 N N     . LEU B  1 1086 ? -2.075  42.326  85.035  1.00 25.52 ? 1084 LEU B N     1 
ATOM   16640 C CA    . LEU B  1 1086 ? -2.019  41.317  83.978  1.00 26.71 ? 1084 LEU B CA    1 
ATOM   16641 C C     . LEU B  1 1086 ? -2.699  40.019  84.421  1.00 28.16 ? 1084 LEU B C     1 
ATOM   16642 O O     . LEU B  1 1086 ? -2.553  39.599  85.582  1.00 27.25 ? 1084 LEU B O     1 
ATOM   16643 C CB    . LEU B  1 1086 ? -0.573  41.027  83.591  1.00 25.59 ? 1084 LEU B CB    1 
ATOM   16644 C CG    . LEU B  1 1086 ? 0.218   42.226  83.072  1.00 25.18 ? 1084 LEU B CG    1 
ATOM   16645 C CD1   . LEU B  1 1086 ? 1.566   41.798  82.486  1.00 27.03 ? 1084 LEU B CD1   1 
ATOM   16646 C CD2   . LEU B  1 1086 ? -0.596  42.969  82.019  1.00 28.62 ? 1084 LEU B CD2   1 
ATOM   16647 N N     . PRO B  1 1087 ? -3.460  39.399  83.512  1.00 27.40 ? 1085 PRO B N     1 
ATOM   16648 C CA    . PRO B  1 1087 ? -4.043  38.083  83.800  1.00 26.82 ? 1085 PRO B CA    1 
ATOM   16649 C C     . PRO B  1 1087 ? -2.962  37.068  84.128  1.00 24.96 ? 1085 PRO B C     1 
ATOM   16650 O O     . PRO B  1 1087 ? -1.924  37.019  83.476  1.00 30.37 ? 1085 PRO B O     1 
ATOM   16651 C CB    . PRO B  1 1087 ? -4.751  37.712  82.490  1.00 29.83 ? 1085 PRO B CB    1 
ATOM   16652 C CG    . PRO B  1 1087 ? -4.970  38.975  81.779  1.00 27.49 ? 1085 PRO B CG    1 
ATOM   16653 C CD    . PRO B  1 1087 ? -3.865  39.911  82.187  1.00 28.44 ? 1085 PRO B CD    1 
ATOM   16654 N N     . GLY B  1 1088 ? -3.235  36.230  85.125  1.00 23.44 ? 1086 GLY B N     1 
ATOM   16655 C CA    . GLY B  1 1088 ? -2.310  35.205  85.544  1.00 26.21 ? 1086 GLY B CA    1 
ATOM   16656 C C     . GLY B  1 1088 ? -2.954  34.254  86.532  1.00 25.50 ? 1086 GLY B C     1 
ATOM   16657 O O     . GLY B  1 1088 ? -4.180  34.176  86.645  1.00 23.63 ? 1086 GLY B O     1 
ATOM   16658 N N     . PRO B  1 1089 ? -2.132  33.527  87.281  1.00 24.82 ? 1087 PRO B N     1 
ATOM   16659 C CA    . PRO B  1 1089 ? -2.664  32.566  88.253  1.00 24.16 ? 1087 PRO B CA    1 
ATOM   16660 C C     . PRO B  1 1089 ? -3.291  33.251  89.457  1.00 25.19 ? 1087 PRO B C     1 
ATOM   16661 O O     . PRO B  1 1089 ? -2.985  34.398  89.791  1.00 22.31 ? 1087 PRO B O     1 
ATOM   16662 C CB    . PRO B  1 1089 ? -1.422  31.771  88.673  1.00 26.19 ? 1087 PRO B CB    1 
ATOM   16663 C CG    . PRO B  1 1089 ? -0.287  32.790  88.514  1.00 28.16 ? 1087 PRO B CG    1 
ATOM   16664 C CD    . PRO B  1 1089 ? -0.655  33.602  87.307  1.00 26.48 ? 1087 PRO B CD    1 
ATOM   16665 N N     . VAL B  1 1090 ? -4.181  32.509  90.124  1.00 23.89 ? 1088 VAL B N     1 
ATOM   16666 C CA    . VAL B  1 1090 ? -4.696  32.950  91.417  1.00 22.06 ? 1088 VAL B CA    1 
ATOM   16667 C C     . VAL B  1 1090 ? -3.552  33.008  92.431  1.00 25.43 ? 1088 VAL B C     1 
ATOM   16668 O O     . VAL B  1 1090 ? -2.490  32.404  92.256  1.00 21.49 ? 1088 VAL B O     1 
ATOM   16669 C CB    . VAL B  1 1090 ? -5.831  32.048  91.927  1.00 24.31 ? 1088 VAL B CB    1 
ATOM   16670 C CG1   . VAL B  1 1090 ? -6.958  31.957  90.890  1.00 21.09 ? 1088 VAL B CG1   1 
ATOM   16671 C CG2   . VAL B  1 1090 ? -5.319  30.650  92.329  1.00 24.02 ? 1088 VAL B CG2   1 
ATOM   16672 N N     . GLY B  1 1091 ? -3.782  33.749  93.510  1.00 21.95 ? 1089 GLY B N     1 
ATOM   16673 C CA    . GLY B  1 1091 ? -2.782  33.821  94.564  1.00 24.00 ? 1089 GLY B CA    1 
ATOM   16674 C C     . GLY B  1 1091 ? -1.578  34.652  94.210  1.00 25.92 ? 1089 GLY B C     1 
ATOM   16675 O O     . GLY B  1 1091 ? -0.584  34.620  94.933  1.00 22.85 ? 1089 GLY B O     1 
ATOM   16676 N N     . GLU B  1 1092 ? -1.653  35.406  93.116  1.00 23.97 ? 1090 GLU B N     1 
ATOM   16677 C CA    . GLU B  1 1092 ? -0.579  36.264  92.659  1.00 25.32 ? 1090 GLU B CA    1 
ATOM   16678 C C     . GLU B  1 1092 ? -1.218  37.509  92.070  1.00 25.24 ? 1090 GLU B C     1 
ATOM   16679 O O     . GLU B  1 1092 ? -2.297  37.439  91.479  1.00 23.92 ? 1090 GLU B O     1 
ATOM   16680 C CB    . GLU B  1 1092 ? 0.280   35.551  91.588  1.00 24.42 ? 1090 GLU B CB    1 
ATOM   16681 C CG    . GLU B  1 1092 ? 1.775   35.764  91.692  1.00 29.25 ? 1090 GLU B CG    1 
ATOM   16682 C CD    . GLU B  1 1092 ? 2.553   34.870  90.735  1.00 31.73 ? 1090 GLU B CD    1 
ATOM   16683 O OE1   . GLU B  1 1092 ? 2.283   34.925  89.508  1.00 27.61 ? 1090 GLU B OE1   1 
ATOM   16684 O OE2   . GLU B  1 1092 ? 3.426   34.101  91.209  1.00 35.92 ? 1090 GLU B OE2   1 
ATOM   16685 N N     . ARG B  1 1093 ? -0.555  38.645  92.227  1.00 25.93 ? 1091 ARG B N     1 
ATOM   16686 C CA    . ARG B  1 1093 ? -0.961  39.873  91.557  1.00 22.39 ? 1091 ARG B CA    1 
ATOM   16687 C C     . ARG B  1 1093 ? 0.209   40.321  90.695  1.00 25.40 ? 1091 ARG B C     1 
ATOM   16688 O O     . ARG B  1 1093 ? 1.307   40.552  91.205  1.00 22.38 ? 1091 ARG B O     1 
ATOM   16689 C CB    . ARG B  1 1093 ? -1.365  40.957  92.562  1.00 25.57 ? 1091 ARG B CB    1 
ATOM   16690 C CG    . ARG B  1 1093 ? -2.128  42.119  91.946  1.00 37.83 ? 1091 ARG B CG    1 
ATOM   16691 C CD    . ARG B  1 1093 ? -2.388  43.264  92.952  1.00 41.32 ? 1091 ARG B CD    1 
ATOM   16692 N NE    . ARG B  1 1093 ? -2.773  42.787  94.276  1.00 40.61 ? 1091 ARG B NE    1 
ATOM   16693 C CZ    . ARG B  1 1093 ? -2.136  43.106  95.397  1.00 48.98 ? 1091 ARG B CZ    1 
ATOM   16694 N NH1   . ARG B  1 1093 ? -1.071  43.896  95.389  1.00 47.54 ? 1091 ARG B NH1   1 
ATOM   16695 N NH2   . ARG B  1 1093 ? -2.583  42.629  96.557  1.00 49.34 ? 1091 ARG B NH2   1 
ATOM   16696 N N     . ASN B  1 1094 ? -0.016  40.409  89.391  1.00 24.94 ? 1092 ASN B N     1 
ATOM   16697 C CA    . ASN B  1 1094 ? 1.048   40.690  88.440  1.00 23.02 ? 1092 ASN B CA    1 
ATOM   16698 C C     . ASN B  1 1094 ? 0.757   42.031  87.789  1.00 21.90 ? 1092 ASN B C     1 
ATOM   16699 O O     . ASN B  1 1094 ? -0.286  42.195  87.143  1.00 23.01 ? 1092 ASN B O     1 
ATOM   16700 C CB    . ASN B  1 1094 ? 1.156   39.558  87.410  1.00 21.87 ? 1092 ASN B CB    1 
ATOM   16701 C CG    . ASN B  1 1094 ? 1.772   38.305  88.025  1.00 21.31 ? 1092 ASN B CG    1 
ATOM   16702 O OD1   . ASN B  1 1094 ? 2.965   38.267  88.273  1.00 21.50 ? 1092 ASN B OD1   1 
ATOM   16703 N ND2   . ASN B  1 1094 ? 0.960   37.299  88.291  1.00 23.55 ? 1092 ASN B ND2   1 
ATOM   16704 N N     . LEU B  1 1095 ? 1.670   42.981  87.979  1.00 20.64 ? 1093 LEU B N     1 
ATOM   16705 C CA    . LEU B  1 1095 ? 1.459   44.381  87.656  1.00 22.92 ? 1093 LEU B CA    1 
ATOM   16706 C C     . LEU B  1 1095 ? 2.462   44.826  86.598  1.00 19.40 ? 1093 LEU B C     1 
ATOM   16707 O O     . LEU B  1 1095 ? 3.594   44.345  86.559  1.00 20.93 ? 1093 LEU B O     1 
ATOM   16708 C CB    . LEU B  1 1095 ? 1.595   45.239  88.926  1.00 23.82 ? 1093 LEU B CB    1 
ATOM   16709 C CG    . LEU B  1 1095 ? 0.679   44.814  90.101  1.00 25.32 ? 1093 LEU B CG    1 
ATOM   16710 C CD1   . LEU B  1 1095 ? 0.854   45.704  91.340  1.00 32.71 ? 1093 LEU B CD1   1 
ATOM   16711 C CD2   . LEU B  1 1095 ? -0.772  44.783  89.701  1.00 27.89 ? 1093 LEU B CD2   1 
ATOM   16712 N N     . TYR B  1 1096 ? 2.034   45.759  85.749  1.00 18.53 ? 1094 TYR B N     1 
ATOM   16713 C CA    . TYR B  1 1096 ? 2.858   46.276  84.665  1.00 19.52 ? 1094 TYR B CA    1 
ATOM   16714 C C     . TYR B  1 1096 ? 2.648   47.780  84.618  1.00 19.57 ? 1094 TYR B C     1 
ATOM   16715 O O     . TYR B  1 1096 ? 1.516   48.244  84.475  1.00 18.55 ? 1094 TYR B O     1 
ATOM   16716 C CB    . TYR B  1 1096 ? 2.474   45.602  83.343  1.00 18.12 ? 1094 TYR B CB    1 
ATOM   16717 C CG    . TYR B  1 1096 ? 3.158   46.119  82.115  1.00 20.07 ? 1094 TYR B CG    1 
ATOM   16718 C CD1   . TYR B  1 1096 ? 4.403   45.641  81.740  1.00 20.32 ? 1094 TYR B CD1   1 
ATOM   16719 C CD2   . TYR B  1 1096 ? 2.539   47.055  81.299  1.00 24.14 ? 1094 TYR B CD2   1 
ATOM   16720 C CE1   . TYR B  1 1096 ? 5.033   46.108  80.604  1.00 20.56 ? 1094 TYR B CE1   1 
ATOM   16721 C CE2   . TYR B  1 1096 ? 3.148   47.510  80.145  1.00 21.88 ? 1094 TYR B CE2   1 
ATOM   16722 C CZ    . TYR B  1 1096 ? 4.393   47.042  79.809  1.00 20.95 ? 1094 TYR B CZ    1 
ATOM   16723 O OH    . TYR B  1 1096 ? 5.009   47.492  78.662  1.00 21.50 ? 1094 TYR B OH    1 
ATOM   16724 N N     . THR B  1 1097 ? 3.726   48.543  84.785  1.00 21.61 ? 1095 THR B N     1 
ATOM   16725 C CA    . THR B  1 1097 ? 3.626   49.992  84.894  1.00 22.23 ? 1095 THR B CA    1 
ATOM   16726 C C     . THR B  1 1097 ? 4.671   50.659  84.011  1.00 20.09 ? 1095 THR B C     1 
ATOM   16727 O O     . THR B  1 1097 ? 5.743   50.118  83.780  1.00 20.84 ? 1095 THR B O     1 
ATOM   16728 C CB    . THR B  1 1097 ? 3.818   50.454  86.335  1.00 23.19 ? 1095 THR B CB    1 
ATOM   16729 O OG1   . THR B  1 1097 ? 5.077   49.973  86.800  1.00 26.82 ? 1095 THR B OG1   1 
ATOM   16730 C CG2   . THR B  1 1097 ? 2.743   49.870  87.229  1.00 23.57 ? 1095 THR B CG2   1 
ATOM   16731 N N     . LEU B  1 1098 ? 4.354   51.848  83.520  1.00 21.24 ? 1096 LEU B N     1 
ATOM   16732 C CA    . LEU B  1 1098 ? 5.295   52.588  82.697  1.00 20.44 ? 1096 LEU B CA    1 
ATOM   16733 C C     . LEU B  1 1098 ? 5.695   53.860  83.429  1.00 19.92 ? 1096 LEU B C     1 
ATOM   16734 O O     . LEU B  1 1098 ? 4.834   54.672  83.786  1.00 21.34 ? 1096 LEU B O     1 
ATOM   16735 C CB    . LEU B  1 1098 ? 4.702   52.913  81.330  1.00 20.69 ? 1096 LEU B CB    1 
ATOM   16736 C CG    . LEU B  1 1098 ? 4.346   51.734  80.425  1.00 21.31 ? 1096 LEU B CG    1 
ATOM   16737 C CD1   . LEU B  1 1098 ? 3.770   52.274  79.117  1.00 21.68 ? 1096 LEU B CD1   1 
ATOM   16738 C CD2   . LEU B  1 1098 ? 5.573   50.908  80.163  1.00 18.29 ? 1096 LEU B CD2   1 
ATOM   16739 N N     . HIS B  1 1099 ? 7.004   54.039  83.617  1.00 19.88 ? 1097 HIS B N     1 
ATOM   16740 C CA    . HIS B  1 1099 ? 7.587   55.150  84.362  1.00 19.38 ? 1097 HIS B CA    1 
ATOM   16741 C C     . HIS B  1 1099 ? 8.490   55.978  83.452  1.00 21.07 ? 1097 HIS B C     1 
ATOM   16742 O O     . HIS B  1 1099 ? 8.849   55.563  82.349  1.00 23.17 ? 1097 HIS B O     1 
ATOM   16743 C CB    . HIS B  1 1099 ? 8.426   54.650  85.544  1.00 24.08 ? 1097 HIS B CB    1 
ATOM   16744 C CG    . HIS B  1 1099 ? 7.676   53.797  86.514  1.00 23.81 ? 1097 HIS B CG    1 
ATOM   16745 N ND1   . HIS B  1 1099 ? 7.263   54.264  87.745  1.00 25.30 ? 1097 HIS B ND1   1 
ATOM   16746 C CD2   . HIS B  1 1099 ? 7.285   52.504  86.451  1.00 23.81 ? 1097 HIS B CD2   1 
ATOM   16747 C CE1   . HIS B  1 1099 ? 6.631   53.298  88.388  1.00 27.58 ? 1097 HIS B CE1   1 
ATOM   16748 N NE2   . HIS B  1 1099 ? 6.633   52.219  87.626  1.00 25.73 ? 1097 HIS B NE2   1 
ATOM   16749 N N     . ALA B  1 1100 ? 8.890   57.146  83.945  1.00 21.76 ? 1098 ALA B N     1 
ATOM   16750 C CA    . ALA B  1 1100 ? 9.931   57.906  83.264  1.00 24.47 ? 1098 ALA B CA    1 
ATOM   16751 C C     . ALA B  1 1100 ? 11.213  57.078  83.200  1.00 25.92 ? 1098 ALA B C     1 
ATOM   16752 O O     . ALA B  1 1100 ? 11.465  56.214  84.046  1.00 24.06 ? 1098 ALA B O     1 
ATOM   16753 C CB    . ALA B  1 1100 ? 10.174  59.232  83.982  1.00 28.73 ? 1098 ALA B CB    1 
ATOM   16754 N N     . ARG B  1 1101 ? 11.996  57.296  82.142  1.00 26.17 ? 1099 ARG B N     1 
ATOM   16755 C CA    . ARG B  1 1101 ? 13.244  56.552  82.002  1.00 28.92 ? 1099 ARG B CA    1 
ATOM   16756 C C     . ARG B  1 1101 ? 14.379  57.192  82.792  1.00 28.45 ? 1099 ARG B C     1 
ATOM   16757 O O     . ARG B  1 1101 ? 15.154  56.491  83.451  1.00 30.25 ? 1099 ARG B O     1 
ATOM   16758 C CB    . ARG B  1 1101 ? 13.636  56.440  80.531  1.00 30.83 ? 1099 ARG B CB    1 
ATOM   16759 C CG    . ARG B  1 1101 ? 13.109  55.212  79.846  1.00 30.84 ? 1099 ARG B CG    1 
ATOM   16760 C CD    . ARG B  1 1101 ? 13.667  55.066  78.438  1.00 32.78 ? 1099 ARG B CD    1 
ATOM   16761 N NE    . ARG B  1 1101 ? 14.744  54.085  78.326  1.00 38.76 ? 1099 ARG B NE    1 
ATOM   16762 C CZ    . ARG B  1 1101 ? 14.581  52.829  77.926  1.00 42.60 ? 1099 ARG B CZ    1 
ATOM   16763 N NH1   . ARG B  1 1101 ? 13.382  52.338  77.670  1.00 37.00 ? 1099 ARG B NH1   1 
ATOM   16764 N NH2   . ARG B  1 1101 ? 15.651  52.048  77.772  1.00 37.82 ? 1099 ARG B NH2   1 
ATOM   16765 N N     . GLY B  1 1102 ? 14.503  58.510  82.736  1.00 26.24 ? 1100 GLY B N     1 
ATOM   16766 C CA    . GLY B  1 1102 ? 15.629  59.166  83.376  1.00 30.26 ? 1100 GLY B CA    1 
ATOM   16767 C C     . GLY B  1 1102 ? 15.995  60.472  82.701  1.00 26.77 ? 1100 GLY B C     1 
ATOM   16768 O O     . GLY B  1 1102 ? 15.130  61.313  82.448  1.00 25.88 ? 1100 GLY B O     1 
ATOM   16769 N N     . ARG B  1 1103 ? 17.281  60.682  82.434  1.00 25.69 ? 1101 ARG B N     1 
ATOM   16770 C CA    . ARG B  1 1103 ? 17.720  61.836  81.670  1.00 23.70 ? 1101 ARG B CA    1 
ATOM   16771 C C     . ARG B  1 1103 ? 18.009  61.398  80.242  1.00 24.59 ? 1101 ARG B C     1 
ATOM   16772 O O     . ARG B  1 1103 ? 18.790  60.468  80.015  1.00 26.62 ? 1101 ARG B O     1 
ATOM   16773 C CB    . ARG B  1 1103 ? 18.959  62.481  82.297  1.00 25.97 ? 1101 ARG B CB    1 
ATOM   16774 C CG    . ARG B  1 1103 ? 19.307  63.853  81.698  1.00 28.45 ? 1101 ARG B CG    1 
ATOM   16775 C CD    . ARG B  1 1103 ? 20.371  64.600  82.523  1.00 27.48 ? 1101 ARG B CD    1 
ATOM   16776 N NE    . ARG B  1 1103 ? 19.972  64.802  83.915  1.00 36.57 ? 1101 ARG B NE    1 
ATOM   16777 C CZ    . ARG B  1 1103 ? 19.367  65.889  84.389  1.00 39.04 ? 1101 ARG B CZ    1 
ATOM   16778 N NH1   . ARG B  1 1103 ? 19.025  66.904  83.596  1.00 34.36 ? 1101 ARG B NH1   1 
ATOM   16779 N NH2   . ARG B  1 1103 ? 19.106  65.967  85.693  1.00 37.41 ? 1101 ARG B NH2   1 
ATOM   16780 N N     . ILE B  1 1104 ? 17.385  62.069  79.286  1.00 22.86 ? 1102 ILE B N     1 
ATOM   16781 C CA    . ILE B  1 1104 ? 17.504  61.723  77.874  1.00 26.22 ? 1102 ILE B CA    1 
ATOM   16782 C C     . ILE B  1 1104 ? 18.540  62.646  77.252  1.00 22.71 ? 1102 ILE B C     1 
ATOM   16783 O O     . ILE B  1 1104 ? 18.487  63.862  77.449  1.00 22.49 ? 1102 ILE B O     1 
ATOM   16784 C CB    . ILE B  1 1104 ? 16.147  61.855  77.162  1.00 23.14 ? 1102 ILE B CB    1 
ATOM   16785 C CG1   . ILE B  1 1104 ? 15.083  61.054  77.934  1.00 21.69 ? 1102 ILE B CG1   1 
ATOM   16786 C CG2   . ILE B  1 1104 ? 16.258  61.386  75.710  1.00 25.32 ? 1102 ILE B CG2   1 
ATOM   16787 C CD1   . ILE B  1 1104 ? 15.366  59.570  78.009  1.00 23.00 ? 1102 ILE B CD1   1 
ATOM   16788 N N     . LEU B  1 1105 ? 19.485  62.081  76.511  1.00 23.43 ? 1103 LEU B N     1 
ATOM   16789 C CA    . LEU B  1 1105 ? 20.449  62.924  75.811  1.00 25.41 ? 1103 LEU B CA    1 
ATOM   16790 C C     . LEU B  1 1105 ? 19.788  63.495  74.561  1.00 22.76 ? 1103 LEU B C     1 
ATOM   16791 O O     . LEU B  1 1105 ? 19.327  62.747  73.697  1.00 24.82 ? 1103 LEU B O     1 
ATOM   16792 C CB    . LEU B  1 1105 ? 21.702  62.126  75.451  1.00 23.59 ? 1103 LEU B CB    1 
ATOM   16793 C CG    . LEU B  1 1105 ? 22.706  62.836  74.546  1.00 28.56 ? 1103 LEU B CG    1 
ATOM   16794 C CD1   . LEU B  1 1105 ? 23.368  63.980  75.311  1.00 26.59 ? 1103 LEU B CD1   1 
ATOM   16795 C CD2   . LEU B  1 1105 ? 23.754  61.831  74.039  1.00 27.69 ? 1103 LEU B CD2   1 
ATOM   16796 N N     . LEU B  1 1106 ? 19.741  64.810  74.460  1.00 24.02 ? 1104 LEU B N     1 
ATOM   16797 C CA    . LEU B  1 1106 ? 19.196  65.470  73.288  1.00 27.67 ? 1104 LEU B CA    1 
ATOM   16798 C C     . LEU B  1 1106 ? 20.345  65.991  72.442  1.00 24.69 ? 1104 LEU B C     1 
ATOM   16799 O O     . LEU B  1 1106 ? 21.204  66.725  72.936  1.00 25.31 ? 1104 LEU B O     1 
ATOM   16800 C CB    . LEU B  1 1106 ? 18.268  66.618  73.684  1.00 23.14 ? 1104 LEU B CB    1 
ATOM   16801 C CG    . LEU B  1 1106 ? 16.770  66.343  73.798  1.00 28.60 ? 1104 LEU B CG    1 
ATOM   16802 C CD1   . LEU B  1 1106 ? 16.476  65.018  74.475  1.00 27.01 ? 1104 LEU B CD1   1 
ATOM   16803 C CD2   . LEU B  1 1106 ? 16.086  67.526  74.507  1.00 25.14 ? 1104 LEU B CD2   1 
ATOM   16804 N N     . VAL B  1 1107 ? 20.346  65.628  71.166  1.00 26.03 ? 1105 VAL B N     1 
ATOM   16805 C CA    . VAL B  1 1107 ? 21.344  66.154  70.242  1.00 28.68 ? 1105 VAL B CA    1 
ATOM   16806 C C     . VAL B  1 1107 ? 20.600  66.864  69.119  1.00 28.10 ? 1105 VAL B C     1 
ATOM   16807 O O     . VAL B  1 1107 ? 20.443  66.300  68.026  1.00 28.62 ? 1105 VAL B O     1 
ATOM   16808 C CB    . VAL B  1 1107 ? 22.259  65.033  69.726  1.00 28.07 ? 1105 VAL B CB    1 
ATOM   16809 C CG1   . VAL B  1 1107 ? 23.485  65.616  68.998  1.00 26.69 ? 1105 VAL B CG1   1 
ATOM   16810 C CG2   . VAL B  1 1107 ? 22.703  64.169  70.885  1.00 27.08 ? 1105 VAL B CG2   1 
ATOM   16811 N N     . PRO B  1 1108 ? 20.117  68.083  69.350  1.00 25.20 ? 1106 PRO B N     1 
ATOM   16812 C CA    . PRO B  1 1108 ? 19.423  68.824  68.296  1.00 30.49 ? 1106 PRO B CA    1 
ATOM   16813 C C     . PRO B  1 1108 ? 20.388  69.453  67.299  1.00 29.08 ? 1106 PRO B C     1 
ATOM   16814 O O     . PRO B  1 1108 ? 21.575  69.659  67.563  1.00 31.28 ? 1106 PRO B O     1 
ATOM   16815 C CB    . PRO B  1 1108 ? 18.683  69.910  69.076  1.00 26.47 ? 1106 PRO B CB    1 
ATOM   16816 C CG    . PRO B  1 1108 ? 19.662  70.202  70.212  1.00 29.98 ? 1106 PRO B CG    1 
ATOM   16817 C CD    . PRO B  1 1108 ? 20.167  68.847  70.613  1.00 27.84 ? 1106 PRO B CD    1 
ATOM   16818 N N     . ALA B  1 1109 ? 19.834  69.764  66.139  1.00 28.26 ? 1107 ALA B N     1 
ATOM   16819 C CA    . ALA B  1 1109 ? 20.489  70.565  65.121  1.00 32.13 ? 1107 ALA B CA    1 
ATOM   16820 C C     . ALA B  1 1109 ? 19.859  71.939  64.965  1.00 31.38 ? 1107 ALA B C     1 
ATOM   16821 O O     . ALA B  1 1109 ? 20.580  72.920  64.761  1.00 32.95 ? 1107 ALA B O     1 
ATOM   16822 C CB    . ALA B  1 1109 ? 20.462  69.820  63.778  1.00 32.90 ? 1107 ALA B CB    1 
ATOM   16823 N N     . THR B  1 1110 ? 18.534  72.035  65.089  1.00 30.23 ? 1108 THR B N     1 
ATOM   16824 C CA    . THR B  1 1110 ? 17.777  73.268  64.912  1.00 31.79 ? 1108 THR B CA    1 
ATOM   16825 C C     . THR B  1 1110 ? 16.943  73.570  66.155  1.00 32.35 ? 1108 THR B C     1 
ATOM   16826 O O     . THR B  1 1110 ? 16.643  72.685  66.969  1.00 29.61 ? 1108 THR B O     1 
ATOM   16827 C CB    . THR B  1 1110 ? 16.826  73.188  63.698  1.00 31.81 ? 1108 THR B CB    1 
ATOM   16828 O OG1   . THR B  1 1110 ? 15.805  72.205  63.937  1.00 32.47 ? 1108 THR B OG1   1 
ATOM   16829 C CG2   . THR B  1 1110 ? 17.583  72.828  62.423  1.00 34.82 ? 1108 THR B CG2   1 
ATOM   16830 N N     . GLU B  1 1111 ? 16.526  74.837  66.266  1.00 32.13 ? 1109 GLU B N     1 
ATOM   16831 C CA    . GLU B  1 1111 ? 15.671  75.240  67.381  1.00 33.74 ? 1109 GLU B CA    1 
ATOM   16832 C C     . GLU B  1 1111 ? 14.360  74.456  67.384  1.00 30.94 ? 1109 GLU B C     1 
ATOM   16833 O O     . GLU B  1 1111 ? 13.940  73.940  68.424  1.00 30.26 ? 1109 GLU B O     1 
ATOM   16834 C CB    . GLU B  1 1111 ? 15.395  76.746  67.332  1.00 33.26 ? 1109 GLU B CB    1 
ATOM   16835 C CG    . GLU B  1 1111 ? 14.352  77.194  68.366  1.00 32.83 ? 1109 GLU B CG    1 
ATOM   16836 C CD    . GLU B  1 1111 ? 14.135  78.695  68.401  1.00 37.84 ? 1109 GLU B CD    1 
ATOM   16837 O OE1   . GLU B  1 1111 ? 14.918  79.401  69.075  1.00 37.21 ? 1109 GLU B OE1   1 
ATOM   16838 O OE2   . GLU B  1 1111 ? 13.172  79.172  67.763  1.00 42.64 ? 1109 GLU B OE2   1 
ATOM   16839 N N     . SER B  1 1112 ? 13.691  74.364  66.230  1.00 30.31 ? 1110 SER B N     1 
ATOM   16840 C CA    . SER B  1 1112 ? 12.431  73.624  66.184  1.00 29.92 ? 1110 SER B CA    1 
ATOM   16841 C C     . SER B  1 1112 ? 12.649  72.152  66.505  1.00 31.82 ? 1110 SER B C     1 
ATOM   16842 O O     . SER B  1 1112 ? 11.819  71.522  67.175  1.00 29.28 ? 1110 SER B O     1 
ATOM   16843 C CB    . SER B  1 1112 ? 11.772  73.780  64.818  1.00 32.46 ? 1110 SER B CB    1 
ATOM   16844 O OG    . SER B  1 1112 ? 10.533  73.091  64.784  1.00 35.42 ? 1110 SER B OG    1 
ATOM   16845 N N     . GLY B  1 1113 ? 13.759  71.584  66.026  1.00 31.45 ? 1111 GLY B N     1 
ATOM   16846 C CA    . GLY B  1 1113 ? 14.097  70.218  66.390  1.00 31.36 ? 1111 GLY B CA    1 
ATOM   16847 C C     . GLY B  1 1113 ? 14.270  70.053  67.887  1.00 27.38 ? 1111 GLY B C     1 
ATOM   16848 O O     . GLY B  1 1113 ? 13.791  69.077  68.473  1.00 28.01 ? 1111 GLY B O     1 
ATOM   16849 N N     . LEU B  1 1114 ? 14.945  71.011  68.526  1.00 26.26 ? 1112 LEU B N     1 
ATOM   16850 C CA    . LEU B  1 1114 ? 15.123  70.963  69.976  1.00 29.25 ? 1112 LEU B CA    1 
ATOM   16851 C C     . LEU B  1 1114 ? 13.778  70.998  70.691  1.00 28.77 ? 1112 LEU B C     1 
ATOM   16852 O O     . LEU B  1 1114 ? 13.558  70.248  71.651  1.00 27.15 ? 1112 LEU B O     1 
ATOM   16853 C CB    . LEU B  1 1114 ? 15.991  72.132  70.437  1.00 29.16 ? 1112 LEU B CB    1 
ATOM   16854 C CG    . LEU B  1 1114 ? 16.108  72.389  71.942  1.00 27.40 ? 1112 LEU B CG    1 
ATOM   16855 C CD1   . LEU B  1 1114 ? 16.603  71.131  72.674  1.00 28.17 ? 1112 LEU B CD1   1 
ATOM   16856 C CD2   . LEU B  1 1114 ? 17.044  73.547  72.169  1.00 29.65 ? 1112 LEU B CD2   1 
ATOM   16857 N N     . TYR B  1 1115 ? 12.867  71.859  70.230  1.00 27.85 ? 1113 TYR B N     1 
ATOM   16858 C CA    . TYR B  1 1115 ? 11.551  71.948  70.861  1.00 30.70 ? 1113 TYR B CA    1 
ATOM   16859 C C     . TYR B  1 1115 ? 10.797  70.630  70.753  1.00 24.78 ? 1113 TYR B C     1 
ATOM   16860 O O     . TYR B  1 1115 ? 10.200  70.164  71.727  1.00 27.26 ? 1113 TYR B O     1 
ATOM   16861 C CB    . TYR B  1 1115 ? 10.735  73.079  70.233  1.00 29.17 ? 1113 TYR B CB    1 
ATOM   16862 C CG    . TYR B  1 1115 ? 11.253  74.467  70.533  1.00 28.95 ? 1113 TYR B CG    1 
ATOM   16863 C CD1   . TYR B  1 1115 ? 12.133  74.698  71.585  1.00 31.18 ? 1113 TYR B CD1   1 
ATOM   16864 C CD2   . TYR B  1 1115 ? 10.860  75.543  69.760  1.00 32.56 ? 1113 TYR B CD2   1 
ATOM   16865 C CE1   . TYR B  1 1115 ? 12.620  75.976  71.844  1.00 36.19 ? 1113 TYR B CE1   1 
ATOM   16866 C CE2   . TYR B  1 1115 ? 11.323  76.822  70.016  1.00 35.72 ? 1113 TYR B CE2   1 
ATOM   16867 C CZ    . TYR B  1 1115 ? 12.205  77.034  71.055  1.00 35.55 ? 1113 TYR B CZ    1 
ATOM   16868 O OH    . TYR B  1 1115 ? 12.661  78.311  71.294  1.00 36.98 ? 1113 TYR B OH    1 
ATOM   16869 N N     . HIS B  1 1116 ? 10.808  70.013  69.567  1.00 24.90 ? 1114 HIS B N     1 
ATOM   16870 C CA    . HIS B  1 1116 ? 10.157  68.716  69.411  1.00 27.20 ? 1114 HIS B CA    1 
ATOM   16871 C C     . HIS B  1 1116 ? 10.807  67.660  70.301  1.00 25.88 ? 1114 HIS B C     1 
ATOM   16872 O O     . HIS B  1 1116 ? 10.106  66.855  70.927  1.00 24.78 ? 1114 HIS B O     1 
ATOM   16873 C CB    . HIS B  1 1116 ? 10.187  68.267  67.946  1.00 26.39 ? 1114 HIS B CB    1 
ATOM   16874 C CG    . HIS B  1 1116 ? 9.181   68.948  67.070  1.00 27.10 ? 1114 HIS B CG    1 
ATOM   16875 N ND1   . HIS B  1 1116 ? 9.358   70.223  66.574  1.00 30.79 ? 1114 HIS B ND1   1 
ATOM   16876 C CD2   . HIS B  1 1116 ? 7.992   68.516  66.584  1.00 31.82 ? 1114 HIS B CD2   1 
ATOM   16877 C CE1   . HIS B  1 1116 ? 8.316   70.551  65.829  1.00 31.06 ? 1114 HIS B CE1   1 
ATOM   16878 N NE2   . HIS B  1 1116 ? 7.474   69.531  65.817  1.00 33.96 ? 1114 HIS B NE2   1 
ATOM   16879 N N     . GLN B  1 1117 ? 12.148  67.634  70.370  1.00 27.11 ? 1115 GLN B N     1 
ATOM   16880 C CA    . GLN B  1 1117 ? 12.811  66.643  71.220  1.00 24.50 ? 1115 GLN B CA    1 
ATOM   16881 C C     . GLN B  1 1117 ? 12.457  66.847  72.688  1.00 24.27 ? 1115 GLN B C     1 
ATOM   16882 O O     . GLN B  1 1117 ? 12.214  65.877  73.416  1.00 23.81 ? 1115 GLN B O     1 
ATOM   16883 C CB    . GLN B  1 1117 ? 14.336  66.698  71.048  1.00 22.70 ? 1115 GLN B CB    1 
ATOM   16884 C CG    . GLN B  1 1117 ? 14.855  66.237  69.698  1.00 26.08 ? 1115 GLN B CG    1 
ATOM   16885 C CD    . GLN B  1 1117 ? 16.370  66.418  69.575  1.00 27.37 ? 1115 GLN B CD    1 
ATOM   16886 O OE1   . GLN B  1 1117 ? 17.005  67.046  70.428  1.00 25.64 ? 1115 GLN B OE1   1 
ATOM   16887 N NE2   . GLN B  1 1117 ? 16.954  65.850  68.525  1.00 24.90 ? 1115 GLN B NE2   1 
ATOM   16888 N N     . LEU B  1 1118 ? 12.474  68.095  73.151  1.00 24.78 ? 1116 LEU B N     1 
ATOM   16889 C CA    . LEU B  1 1118 ? 12.089  68.373  74.530  1.00 26.44 ? 1116 LEU B CA    1 
ATOM   16890 C C     . LEU B  1 1118 ? 10.677  67.908  74.807  1.00 23.82 ? 1116 LEU B C     1 
ATOM   16891 O O     . LEU B  1 1118 ? 10.411  67.324  75.865  1.00 24.32 ? 1116 LEU B O     1 
ATOM   16892 C CB    . LEU B  1 1118 ? 12.195  69.865  74.826  1.00 27.81 ? 1116 LEU B CB    1 
ATOM   16893 C CG    . LEU B  1 1118 ? 13.549  70.291  75.366  1.00 29.59 ? 1116 LEU B CG    1 
ATOM   16894 C CD1   . LEU B  1 1118 ? 13.669  71.813  75.294  1.00 29.94 ? 1116 LEU B CD1   1 
ATOM   16895 C CD2   . LEU B  1 1118 ? 13.649  69.790  76.807  1.00 32.43 ? 1116 LEU B CD2   1 
ATOM   16896 N N     . ALA B  1 1119 ? 9.753   68.181  73.876  1.00 24.57 ? 1117 ALA B N     1 
ATOM   16897 C CA    . ALA B  1 1119 ? 8.360   67.787  74.073  1.00 25.18 ? 1117 ALA B CA    1 
ATOM   16898 C C     . ALA B  1 1119 ? 8.244   66.282  74.252  1.00 27.11 ? 1117 ALA B C     1 
ATOM   16899 O O     . ALA B  1 1119 ? 7.570   65.810  75.170  1.00 23.20 ? 1117 ALA B O     1 
ATOM   16900 C CB    . ALA B  1 1119 ? 7.501   68.252  72.897  1.00 24.05 ? 1117 ALA B CB    1 
ATOM   16901 N N     . ALA B  1 1120 ? 8.912   65.514  73.384  1.00 25.10 ? 1118 ALA B N     1 
ATOM   16902 C CA    . ALA B  1 1120 ? 8.907   64.058  73.503  1.00 24.64 ? 1118 ALA B CA    1 
ATOM   16903 C C     . ALA B  1 1120 ? 9.436   63.609  74.858  1.00 25.86 ? 1118 ALA B C     1 
ATOM   16904 O O     . ALA B  1 1120 ? 8.855   62.730  75.502  1.00 22.99 ? 1118 ALA B O     1 
ATOM   16905 C CB    . ALA B  1 1120 ? 9.743   63.442  72.379  1.00 26.19 ? 1118 ALA B CB    1 
ATOM   16906 N N     . ALA B  1 1121 ? 10.551  64.192  75.308  1.00 22.51 ? 1119 ALA B N     1 
ATOM   16907 C CA    . ALA B  1 1121 ? 11.159  63.719  76.551  1.00 20.95 ? 1119 ALA B CA    1 
ATOM   16908 C C     . ALA B  1 1121 ? 10.375  64.182  77.774  1.00 22.44 ? 1119 ALA B C     1 
ATOM   16909 O O     . ALA B  1 1121 ? 10.259  63.444  78.764  1.00 22.23 ? 1119 ALA B O     1 
ATOM   16910 C CB    . ALA B  1 1121 ? 12.603  64.202  76.640  1.00 24.40 ? 1119 ALA B CB    1 
ATOM   16911 N N     . LEU B  1 1122 ? 9.865   65.410  77.745  1.00 21.92 ? 1120 LEU B N     1 
ATOM   16912 C CA    . LEU B  1 1122 ? 9.081   65.896  78.875  1.00 25.14 ? 1120 LEU B CA    1 
ATOM   16913 C C     . LEU B  1 1122 ? 7.755   65.154  78.992  1.00 24.99 ? 1120 LEU B C     1 
ATOM   16914 O O     . LEU B  1 1122 ? 7.320   64.825  80.103  1.00 24.37 ? 1120 LEU B O     1 
ATOM   16915 C CB    . LEU B  1 1122 ? 8.845   67.396  78.744  1.00 22.64 ? 1120 LEU B CB    1 
ATOM   16916 C CG    . LEU B  1 1122 ? 10.082  68.300  78.868  1.00 26.11 ? 1120 LEU B CG    1 
ATOM   16917 C CD1   . LEU B  1 1122 ? 9.708   69.753  78.552  1.00 27.15 ? 1120 LEU B CD1   1 
ATOM   16918 C CD2   . LEU B  1 1122 ? 10.721  68.195  80.247  1.00 23.44 ? 1120 LEU B CD2   1 
ATOM   16919 N N     . ALA B  1 1123 ? 7.101   64.871  77.860  1.00 22.31 ? 1121 ALA B N     1 
ATOM   16920 C CA    . ALA B  1 1123 ? 5.817   64.175  77.909  1.00 23.21 ? 1121 ALA B CA    1 
ATOM   16921 C C     . ALA B  1 1123 ? 5.946   62.774  78.488  1.00 25.53 ? 1121 ALA B C     1 
ATOM   16922 O O     . ALA B  1 1123 ? 4.952   62.215  78.974  1.00 22.32 ? 1121 ALA B O     1 
ATOM   16923 C CB    . ALA B  1 1123 ? 5.199   64.085  76.511  1.00 24.65 ? 1121 ALA B CB    1 
ATOM   16924 N N     . THR B  1 1124 ? 7.139   62.189  78.436  1.00 21.98 ? 1122 THR B N     1 
ATOM   16925 C CA    . THR B  1 1124 ? 7.366   60.870  78.998  1.00 22.24 ? 1122 THR B CA    1 
ATOM   16926 C C     . THR B  1 1124 ? 8.010   60.946  80.381  1.00 21.72 ? 1122 THR B C     1 
ATOM   16927 O O     . THR B  1 1124 ? 8.538   59.947  80.874  1.00 24.78 ? 1122 THR B O     1 
ATOM   16928 C CB    . THR B  1 1124 ? 8.185   60.010  78.020  1.00 23.72 ? 1122 THR B CB    1 
ATOM   16929 O OG1   . THR B  1 1124 ? 9.285   60.761  77.492  1.00 24.00 ? 1122 THR B OG1   1 
ATOM   16930 C CG2   . THR B  1 1124 ? 7.281   59.586  76.836  1.00 22.71 ? 1122 THR B CG2   1 
ATOM   16931 N N     . GLY B  1 1125 ? 7.952   62.109  81.024  1.00 21.69 ? 1123 GLY B N     1 
ATOM   16932 C CA    . GLY B  1 1125 ? 8.414   62.260  82.388  1.00 20.08 ? 1123 GLY B CA    1 
ATOM   16933 C C     . GLY B  1 1125 ? 9.910   62.405  82.553  1.00 22.14 ? 1123 GLY B C     1 
ATOM   16934 O O     . GLY B  1 1125 ? 10.392  62.350  83.684  1.00 23.15 ? 1123 GLY B O     1 
ATOM   16935 N N     . ASN B  1 1126 ? 10.667  62.593  81.477  1.00 21.65 ? 1124 ASN B N     1 
ATOM   16936 C CA    . ASN B  1 1126 ? 12.121  62.579  81.615  1.00 23.69 ? 1124 ASN B CA    1 
ATOM   16937 C C     . ASN B  1 1126 ? 12.703  63.975  81.811  1.00 24.34 ? 1124 ASN B C     1 
ATOM   16938 O O     . ASN B  1 1126 ? 12.077  64.992  81.513  1.00 26.04 ? 1124 ASN B O     1 
ATOM   16939 C CB    . ASN B  1 1126 ? 12.767  61.941  80.393  1.00 22.77 ? 1124 ASN B CB    1 
ATOM   16940 C CG    . ASN B  1 1126 ? 12.269  60.542  80.147  1.00 20.54 ? 1124 ASN B CG    1 
ATOM   16941 O OD1   . ASN B  1 1126 ? 12.566  59.606  80.909  1.00 24.01 ? 1124 ASN B OD1   1 
ATOM   16942 N ND2   . ASN B  1 1126 ? 11.516  60.382  79.087  1.00 21.91 ? 1124 ASN B ND2   1 
ATOM   16943 N N     . SER B  1 1127 ? 13.924  64.004  82.346  1.00 25.34 ? 1125 SER B N     1 
ATOM   16944 C CA    . SER B  1 1127 ? 14.765  65.178  82.250  1.00 22.73 ? 1125 SER B CA    1 
ATOM   16945 C C     . SER B  1 1127 ? 15.617  65.042  80.995  1.00 25.40 ? 1125 SER B C     1 
ATOM   16946 O O     . SER B  1 1127 ? 15.590  64.018  80.311  1.00 22.82 ? 1125 SER B O     1 
ATOM   16947 C CB    . SER B  1 1127 ? 15.638  65.337  83.501  1.00 26.21 ? 1125 SER B CB    1 
ATOM   16948 O OG    . SER B  1 1127 ? 16.534  64.240  83.653  1.00 27.24 ? 1125 SER B OG    1 
ATOM   16949 N N     . VAL B  1 1128 ? 16.354  66.096  80.664  1.00 24.57 ? 1126 VAL B N     1 
ATOM   16950 C CA    . VAL B  1 1128 ? 17.178  66.066  79.461  1.00 27.11 ? 1126 VAL B CA    1 
ATOM   16951 C C     . VAL B  1 1128 ? 18.548  66.646  79.753  1.00 27.71 ? 1126 VAL B C     1 
ATOM   16952 O O     . VAL B  1 1128 ? 18.737  67.432  80.683  1.00 29.29 ? 1126 VAL B O     1 
ATOM   16953 C CB    . VAL B  1 1128 ? 16.536  66.821  78.276  1.00 26.79 ? 1126 VAL B CB    1 
ATOM   16954 C CG1   . VAL B  1 1128 ? 15.151  66.254  77.981  1.00 23.63 ? 1126 VAL B CG1   1 
ATOM   16955 C CG2   . VAL B  1 1128 ? 16.465  68.326  78.553  1.00 26.32 ? 1126 VAL B CG2   1 
ATOM   16956 N N     . ALA B  1 1129 ? 19.512  66.219  78.940  1.00 24.45 ? 1127 ALA B N     1 
ATOM   16957 C CA    . ALA B  1 1129 ? 20.804  66.877  78.799  1.00 24.33 ? 1127 ALA B CA    1 
ATOM   16958 C C     . ALA B  1 1129 ? 20.933  67.257  77.335  1.00 26.53 ? 1127 ALA B C     1 
ATOM   16959 O O     . ALA B  1 1129 ? 20.907  66.379  76.467  1.00 23.83 ? 1127 ALA B O     1 
ATOM   16960 C CB    . ALA B  1 1129 ? 21.939  65.956  79.217  1.00 26.13 ? 1127 ALA B CB    1 
ATOM   16961 N N     . ILE B  1 1130 ? 21.014  68.555  77.060  1.00 23.74 ? 1128 ILE B N     1 
ATOM   16962 C CA    . ILE B  1 1130 ? 21.107  69.046  75.695  1.00 26.10 ? 1128 ILE B CA    1 
ATOM   16963 C C     . ILE B  1 1130 ? 22.574  69.223  75.326  1.00 24.10 ? 1128 ILE B C     1 
ATOM   16964 O O     . ILE B  1 1130 ? 23.345  69.867  76.051  1.00 28.07 ? 1128 ILE B O     1 
ATOM   16965 C CB    . ILE B  1 1130 ? 20.331  70.362  75.520  1.00 27.10 ? 1128 ILE B CB    1 
ATOM   16966 C CG1   . ILE B  1 1130 ? 18.902  70.213  76.081  1.00 25.06 ? 1128 ILE B CG1   1 
ATOM   16967 C CG2   . ILE B  1 1130 ? 20.254  70.719  74.049  1.00 26.89 ? 1128 ILE B CG2   1 
ATOM   16968 C CD1   . ILE B  1 1130 ? 18.155  71.525  76.138  1.00 25.12 ? 1128 ILE B CD1   1 
ATOM   16969 N N     . ASP B  1 1131 ? 22.952  68.675  74.175  1.00 26.40 ? 1129 ASP B N     1 
ATOM   16970 C CA    . ASP B  1 1131 ? 24.318  68.818  73.685  1.00 28.58 ? 1129 ASP B CA    1 
ATOM   16971 C C     . ASP B  1 1131 ? 24.692  70.287  73.526  1.00 28.07 ? 1129 ASP B C     1 
ATOM   16972 O O     . ASP B  1 1131 ? 24.113  70.991  72.692  1.00 29.99 ? 1129 ASP B O     1 
ATOM   16973 C CB    . ASP B  1 1131 ? 24.461  68.071  72.359  1.00 30.25 ? 1129 ASP B CB    1 
ATOM   16974 C CG    . ASP B  1 1131 ? 25.795  68.295  71.700  1.00 30.15 ? 1129 ASP B CG    1 
ATOM   16975 O OD1   . ASP B  1 1131 ? 26.824  68.324  72.410  1.00 30.09 ? 1129 ASP B OD1   1 
ATOM   16976 O OD2   . ASP B  1 1131 ? 25.802  68.422  70.460  1.00 31.39 ? 1129 ASP B OD2   1 
ATOM   16977 N N     . ALA B  1 1132 ? 25.654  70.763  74.324  1.00 31.19 ? 1130 ALA B N     1 
ATOM   16978 C CA    . ALA B  1 1132 ? 26.029  72.174  74.272  1.00 31.05 ? 1130 ALA B CA    1 
ATOM   16979 C C     . ALA B  1 1132 ? 26.604  72.562  72.920  1.00 31.07 ? 1130 ALA B C     1 
ATOM   16980 O O     . ALA B  1 1132 ? 26.573  73.742  72.556  1.00 32.64 ? 1130 ALA B O     1 
ATOM   16981 C CB    . ALA B  1 1132 ? 27.038  72.498  75.375  1.00 31.12 ? 1130 ALA B CB    1 
ATOM   16982 N N     . ALA B  1 1133 ? 27.108  71.596  72.157  1.00 32.32 ? 1131 ALA B N     1 
ATOM   16983 C CA    . ALA B  1 1133 ? 27.717  71.911  70.873  1.00 34.28 ? 1131 ALA B CA    1 
ATOM   16984 C C     . ALA B  1 1133 ? 26.692  72.277  69.813  1.00 33.66 ? 1131 ALA B C     1 
ATOM   16985 O O     . ALA B  1 1133 ? 27.083  72.764  68.744  1.00 35.93 ? 1131 ALA B O     1 
ATOM   16986 C CB    . ALA B  1 1133 ? 28.573  70.731  70.395  1.00 37.06 ? 1131 ALA B CB    1 
ATOM   16987 N N     . SER B  1 1134 ? 25.399  72.052  70.074  1.00 31.24 ? 1132 SER B N     1 
ATOM   16988 C CA    . SER B  1 1134 ? 24.370  72.464  69.133  1.00 30.46 ? 1132 SER B CA    1 
ATOM   16989 C C     . SER B  1 1134 ? 24.306  73.977  68.996  1.00 31.12 ? 1132 SER B C     1 
ATOM   16990 O O     . SER B  1 1134 ? 23.784  74.470  67.994  1.00 33.01 ? 1132 SER B O     1 
ATOM   16991 C CB    . SER B  1 1134 ? 22.995  71.926  69.565  1.00 28.63 ? 1132 SER B CB    1 
ATOM   16992 O OG    . SER B  1 1134 ? 22.625  72.455  70.831  1.00 30.26 ? 1132 SER B OG    1 
ATOM   16993 N N     . GLY B  1 1135 ? 24.820  74.721  69.972  1.00 28.52 ? 1133 GLY B N     1 
ATOM   16994 C CA    . GLY B  1 1135 ? 24.809  76.168  69.875  1.00 32.78 ? 1133 GLY B CA    1 
ATOM   16995 C C     . GLY B  1 1135 ? 23.450  76.807  70.068  1.00 32.10 ? 1133 GLY B C     1 
ATOM   16996 O O     . GLY B  1 1135 ? 23.268  77.979  69.730  1.00 35.41 ? 1133 GLY B O     1 
ATOM   16997 N N     . LEU B  1 1136 ? 22.501  76.079  70.643  1.00 33.34 ? 1134 LEU B N     1 
ATOM   16998 C CA    . LEU B  1 1136 ? 21.107  76.501  70.718  1.00 34.27 ? 1134 LEU B CA    1 
ATOM   16999 C C     . LEU B  1 1136 ? 20.730  77.041  72.095  1.00 33.79 ? 1134 LEU B C     1 
ATOM   17000 O O     . LEU B  1 1136 ? 19.541  77.101  72.421  1.00 36.57 ? 1134 LEU B O     1 
ATOM   17001 C CB    . LEU B  1 1136 ? 20.202  75.332  70.338  1.00 31.85 ? 1134 LEU B CB    1 
ATOM   17002 C CG    . LEU B  1 1136 ? 20.321  74.881  68.884  1.00 33.53 ? 1134 LEU B CG    1 
ATOM   17003 C CD1   . LEU B  1 1136 ? 19.553  73.591  68.654  1.00 33.03 ? 1134 LEU B CD1   1 
ATOM   17004 C CD2   . LEU B  1 1136 ? 19.828  75.979  67.947  1.00 35.77 ? 1134 LEU B CD2   1 
ATOM   17005 N N     . GLN B  1 1137 ? 21.713  77.467  72.895  1.00 34.97 ? 1135 GLN B N     1 
ATOM   17006 C CA    . GLN B  1 1137 ? 21.429  77.826  74.283  1.00 36.37 ? 1135 GLN B CA    1 
ATOM   17007 C C     . GLN B  1 1137 ? 20.500  79.030  74.385  1.00 40.31 ? 1135 GLN B C     1 
ATOM   17008 O O     . GLN B  1 1137 ? 19.752  79.152  75.362  1.00 43.62 ? 1135 GLN B O     1 
ATOM   17009 C CB    . GLN B  1 1137 ? 22.731  78.096  75.045  1.00 38.71 ? 1135 GLN B CB    1 
ATOM   17010 C CG    . GLN B  1 1137 ? 23.578  76.851  75.340  1.00 40.47 ? 1135 GLN B CG    1 
ATOM   17011 C CD    . GLN B  1 1137 ? 24.520  76.492  74.204  1.00 35.57 ? 1135 GLN B CD    1 
ATOM   17012 O OE1   . GLN B  1 1137 ? 24.371  76.967  73.082  1.00 34.96 ? 1135 GLN B OE1   1 
ATOM   17013 N NE2   . GLN B  1 1137 ? 25.501  75.648  74.496  1.00 37.48 ? 1135 GLN B NE2   1 
ATOM   17014 N N     . ALA B  1 1138 ? 20.512  79.919  73.393  1.00 37.77 ? 1136 ALA B N     1 
ATOM   17015 C CA    . ALA B  1 1138 ? 19.624  81.071  73.434  1.00 37.94 ? 1136 ALA B CA    1 
ATOM   17016 C C     . ALA B  1 1138 ? 18.185  80.727  73.069  1.00 38.82 ? 1136 ALA B C     1 
ATOM   17017 O O     . ALA B  1 1138 ? 17.322  81.611  73.125  1.00 38.95 ? 1136 ALA B O     1 
ATOM   17018 C CB    . ALA B  1 1138 ? 20.133  82.166  72.503  1.00 35.24 ? 1136 ALA B CB    1 
ATOM   17019 N N     . SER B  1 1139 ? 17.907  79.480  72.693  1.00 36.56 ? 1137 SER B N     1 
ATOM   17020 C CA    . SER B  1 1139 ? 16.562  79.070  72.308  1.00 38.39 ? 1137 SER B CA    1 
ATOM   17021 C C     . SER B  1 1139 ? 15.655  78.807  73.499  1.00 38.17 ? 1137 SER B C     1 
ATOM   17022 O O     . SER B  1 1139 ? 14.442  78.646  73.309  1.00 36.71 ? 1137 SER B O     1 
ATOM   17023 C CB    . SER B  1 1139 ? 16.619  77.811  71.438  1.00 34.65 ? 1137 SER B CB    1 
ATOM   17024 O OG    . SER B  1 1139 ? 17.116  78.116  70.145  1.00 35.41 ? 1137 SER B OG    1 
ATOM   17025 N N     . LEU B  1 1140 ? 16.209  78.750  74.707  1.00 37.24 ? 1138 LEU B N     1 
ATOM   17026 C CA    . LEU B  1 1140 ? 15.425  78.460  75.896  1.00 39.42 ? 1138 LEU B CA    1 
ATOM   17027 C C     . LEU B  1 1140 ? 15.442  79.647  76.848  1.00 40.05 ? 1138 LEU B C     1 
ATOM   17028 O O     . LEU B  1 1140 ? 15.632  79.483  78.056  1.00 43.39 ? 1138 LEU B O     1 
ATOM   17029 C CB    . LEU B  1 1140 ? 15.949  77.194  76.575  1.00 39.18 ? 1138 LEU B CB    1 
ATOM   17030 C CG    . LEU B  1 1140 ? 15.918  75.964  75.662  1.00 39.01 ? 1138 LEU B CG    1 
ATOM   17031 C CD1   . LEU B  1 1140 ? 16.355  74.688  76.388  1.00 34.78 ? 1138 LEU B CD1   1 
ATOM   17032 C CD2   . LEU B  1 1140 ? 14.536  75.783  75.051  1.00 40.25 ? 1138 LEU B CD2   1 
ATOM   17033 N N     . LYS B  1 1141 ? 15.224  80.843  76.310  1.00 39.83 ? 1139 LYS B N     1 
ATOM   17034 C CA    . LYS B  1 1141 ? 15.186  82.050  77.118  1.00 40.30 ? 1139 LYS B CA    1 
ATOM   17035 C C     . LYS B  1 1141 ? 13.821  82.197  77.780  1.00 45.39 ? 1139 LYS B C     1 
ATOM   17036 O O     . LYS B  1 1141 ? 12.783  81.999  77.141  1.00 45.86 ? 1139 LYS B O     1 
ATOM   17037 C CB    . LYS B  1 1141 ? 15.493  83.276  76.253  1.00 42.22 ? 1139 LYS B CB    1 
ATOM   17038 N N     . ASN B  1 1142 ? 13.833  82.532  79.075  1.00 45.58 ? 1140 ASN B N     1 
ATOM   17039 C CA    . ASN B  1 1142 ? 12.617  82.777  79.855  1.00 45.85 ? 1140 ASN B CA    1 
ATOM   17040 C C     . ASN B  1 1142 ? 11.795  81.499  80.033  1.00 42.79 ? 1140 ASN B C     1 
ATOM   17041 O O     . ASN B  1 1142 ? 10.564  81.532  80.074  1.00 43.90 ? 1140 ASN B O     1 
ATOM   17042 C CB    . ASN B  1 1142 ? 11.765  83.885  79.231  1.00 47.01 ? 1140 ASN B CB    1 
ATOM   17043 N N     . LEU B  1 1143 ? 12.486  80.368  80.149  1.00 41.41 ? 1141 LEU B N     1 
ATOM   17044 C CA    . LEU B  1 1143 ? 11.827  79.083  80.358  1.00 41.35 ? 1141 LEU B CA    1 
ATOM   17045 C C     . LEU B  1 1143 ? 11.238  79.019  81.767  1.00 37.87 ? 1141 LEU B C     1 
ATOM   17046 O O     . LEU B  1 1143 ? 11.867  79.479  82.719  1.00 40.44 ? 1141 LEU B O     1 
ATOM   17047 C CB    . LEU B  1 1143 ? 12.841  77.947  80.165  1.00 36.99 ? 1141 LEU B CB    1 
ATOM   17048 C CG    . LEU B  1 1143 ? 12.385  76.540  79.820  1.00 36.34 ? 1141 LEU B CG    1 
ATOM   17049 C CD1   . LEU B  1 1143 ? 11.744  76.486  78.441  1.00 36.92 ? 1141 LEU B CD1   1 
ATOM   17050 C CD2   . LEU B  1 1143 ? 13.567  75.565  79.918  1.00 38.65 ? 1141 LEU B CD2   1 
ATOM   17051 N N     . PRO B  1 1144 ? 10.041  78.454  81.938  1.00 39.59 ? 1142 PRO B N     1 
ATOM   17052 C CA    . PRO B  1 1144 ? 9.505   78.285  83.296  1.00 39.48 ? 1142 PRO B CA    1 
ATOM   17053 C C     . PRO B  1 1144 ? 10.440  77.448  84.156  1.00 37.28 ? 1142 PRO B C     1 
ATOM   17054 O O     . PRO B  1 1144 ? 11.027  76.465  83.694  1.00 36.92 ? 1142 PRO B O     1 
ATOM   17055 C CB    . PRO B  1 1144 ? 8.164   77.576  83.066  1.00 38.39 ? 1142 PRO B CB    1 
ATOM   17056 C CG    . PRO B  1 1144 ? 7.791   77.939  81.667  1.00 40.19 ? 1142 PRO B CG    1 
ATOM   17057 C CD    . PRO B  1 1144 ? 9.082   78.017  80.908  1.00 38.51 ? 1142 PRO B CD    1 
ATOM   17058 N N     . GLN B  1 1145 ? 10.583  77.855  85.422  1.00 40.06 ? 1143 GLN B N     1 
ATOM   17059 C CA    . GLN B  1 1145 ? 11.464  77.143  86.340  1.00 37.34 ? 1143 GLN B CA    1 
ATOM   17060 C C     . GLN B  1 1145 ? 11.125  75.662  86.421  1.00 36.30 ? 1143 GLN B C     1 
ATOM   17061 O O     . GLN B  1 1145 ? 12.022  74.834  86.608  1.00 36.68 ? 1143 GLN B O     1 
ATOM   17062 C CB    . GLN B  1 1145 ? 11.396  77.771  87.734  1.00 36.87 ? 1143 GLN B CB    1 
ATOM   17063 N N     . THR B  1 1146 ? 9.842   75.308  86.285  1.00 35.35 ? 1144 THR B N     1 
ATOM   17064 C CA    . THR B  1 1146 ? 9.456   73.896  86.290  1.00 37.36 ? 1144 THR B CA    1 
ATOM   17065 C C     . THR B  1 1146 ? 10.111  73.144  85.147  1.00 34.35 ? 1144 THR B C     1 
ATOM   17066 O O     . THR B  1 1146 ? 10.544  71.996  85.312  1.00 36.51 ? 1144 THR B O     1 
ATOM   17067 C CB    . THR B  1 1146 ? 7.934   73.750  86.187  1.00 35.83 ? 1144 THR B CB    1 
ATOM   17068 O OG1   . THR B  1 1146 ? 7.448   74.638  85.174  1.00 37.98 ? 1144 THR B OG1   1 
ATOM   17069 C CG2   . THR B  1 1146 ? 7.272   74.085  87.505  1.00 40.63 ? 1144 THR B CG2   1 
ATOM   17070 N N     . VAL B  1 1147 ? 10.174  73.762  83.972  1.00 32.63 ? 1145 VAL B N     1 
ATOM   17071 C CA    . VAL B  1 1147 ? 10.848  73.109  82.860  1.00 31.68 ? 1145 VAL B CA    1 
ATOM   17072 C C     . VAL B  1 1147 ? 12.359  73.196  83.029  1.00 33.82 ? 1145 VAL B C     1 
ATOM   17073 O O     . VAL B  1 1147 ? 13.075  72.211  82.817  1.00 34.35 ? 1145 VAL B O     1 
ATOM   17074 C CB    . VAL B  1 1147 ? 10.383  73.715  81.526  1.00 31.92 ? 1145 VAL B CB    1 
ATOM   17075 C CG1   . VAL B  1 1147 ? 10.969  72.922  80.365  1.00 35.83 ? 1145 VAL B CG1   1 
ATOM   17076 C CG2   . VAL B  1 1147 ? 8.858   73.729  81.456  1.00 28.86 ? 1145 VAL B CG2   1 
ATOM   17077 N N     . GLY B  1 1148 ? 12.862  74.362  83.439  1.00 32.44 ? 1146 GLY B N     1 
ATOM   17078 C CA    . GLY B  1 1148 ? 14.300  74.540  83.567  1.00 34.23 ? 1146 GLY B CA    1 
ATOM   17079 C C     . GLY B  1 1148 ? 14.944  73.556  84.518  1.00 34.68 ? 1146 GLY B C     1 
ATOM   17080 O O     . GLY B  1 1148 ? 16.080  73.124  84.292  1.00 31.84 ? 1146 GLY B O     1 
ATOM   17081 N N     . LEU B  1 1149 ? 14.227  73.170  85.583  1.00 33.63 ? 1147 LEU B N     1 
ATOM   17082 C CA    . LEU B  1 1149 ? 14.753  72.194  86.529  1.00 34.35 ? 1147 LEU B CA    1 
ATOM   17083 C C     . LEU B  1 1149 ? 14.952  70.832  85.890  1.00 32.51 ? 1147 LEU B C     1 
ATOM   17084 O O     . LEU B  1 1149 ? 15.693  70.005  86.430  1.00 35.05 ? 1147 LEU B O     1 
ATOM   17085 C CB    . LEU B  1 1149 ? 13.829  72.060  87.742  1.00 35.05 ? 1147 LEU B CB    1 
ATOM   17086 N N     . ARG B  1 1150 ? 14.332  70.580  84.748  1.00 29.11 ? 1148 ARG B N     1 
ATOM   17087 C CA    . ARG B  1 1150 ? 14.544  69.324  84.054  1.00 31.61 ? 1148 ARG B CA    1 
ATOM   17088 C C     . ARG B  1 1150 ? 15.598  69.420  82.970  1.00 30.39 ? 1148 ARG B C     1 
ATOM   17089 O O     . ARG B  1 1150 ? 15.882  68.413  82.314  1.00 31.84 ? 1148 ARG B O     1 
ATOM   17090 C CB    . ARG B  1 1150 ? 13.241  68.842  83.435  1.00 29.82 ? 1148 ARG B CB    1 
ATOM   17091 C CG    . ARG B  1 1150 ? 12.270  68.274  84.433  1.00 30.78 ? 1148 ARG B CG    1 
ATOM   17092 C CD    . ARG B  1 1150 ? 11.546  67.142  83.776  1.00 30.22 ? 1148 ARG B CD    1 
ATOM   17093 N NE    . ARG B  1 1150 ? 10.377  66.743  84.538  1.00 31.20 ? 1148 ARG B NE    1 
ATOM   17094 C CZ    . ARG B  1 1150 ? 9.322   66.147  84.009  1.00 29.01 ? 1148 ARG B CZ    1 
ATOM   17095 N NH1   . ARG B  1 1150 ? 9.283   65.826  82.723  1.00 24.57 ? 1148 ARG B NH1   1 
ATOM   17096 N NH2   . ARG B  1 1150 ? 8.276   65.874  84.785  1.00 27.84 ? 1148 ARG B NH2   1 
ATOM   17097 N N     . VAL B  1 1151 ? 16.171  70.600  82.757  1.00 31.97 ? 1149 VAL B N     1 
ATOM   17098 C CA    . VAL B  1 1151 ? 17.018  70.872  81.605  1.00 28.88 ? 1149 VAL B CA    1 
ATOM   17099 C C     . VAL B  1 1151 ? 18.443  71.089  82.082  1.00 33.85 ? 1149 VAL B C     1 
ATOM   17100 O O     . VAL B  1 1151 ? 18.696  71.927  82.953  1.00 31.66 ? 1149 VAL B O     1 
ATOM   17101 C CB    . VAL B  1 1151 ? 16.516  72.087  80.810  1.00 32.56 ? 1149 VAL B CB    1 
ATOM   17102 C CG1   . VAL B  1 1151 ? 17.584  72.555  79.795  1.00 32.60 ? 1149 VAL B CG1   1 
ATOM   17103 C CG2   . VAL B  1 1151 ? 15.220  71.740  80.103  1.00 31.16 ? 1149 VAL B CG2   1 
ATOM   17104 N N     . SER B  1 1152 ? 19.369  70.327  81.521  1.00 30.99 ? 1150 SER B N     1 
ATOM   17105 C CA    . SER B  1 1152 ? 20.780  70.609  81.693  1.00 29.13 ? 1150 SER B CA    1 
ATOM   17106 C C     . SER B  1 1152 ? 21.426  70.656  80.316  1.00 30.86 ? 1150 SER B C     1 
ATOM   17107 O O     . SER B  1 1152 ? 20.861  70.196  79.318  1.00 30.29 ? 1150 SER B O     1 
ATOM   17108 C CB    . SER B  1 1152 ? 21.452  69.572  82.598  1.00 31.19 ? 1150 SER B CB    1 
ATOM   17109 O OG    . SER B  1 1152 ? 21.431  68.286  82.013  1.00 33.69 ? 1150 SER B OG    1 
ATOM   17110 N N     . TRP B  1 1153 ? 22.606  71.253  80.263  1.00 28.38 ? 1151 TRP B N     1 
ATOM   17111 C CA    . TRP B  1 1153 ? 23.393  71.293  79.049  1.00 29.41 ? 1151 TRP B CA    1 
ATOM   17112 C C     . TRP B  1 1153 ? 24.675  70.517  79.299  1.00 32.80 ? 1151 TRP B C     1 
ATOM   17113 O O     . TRP B  1 1153 ? 25.282  70.639  80.366  1.00 33.43 ? 1151 TRP B O     1 
ATOM   17114 C CB    . TRP B  1 1153 ? 23.705  72.732  78.650  1.00 32.87 ? 1151 TRP B CB    1 
ATOM   17115 C CG    . TRP B  1 1153 ? 22.492  73.498  78.233  1.00 33.96 ? 1151 TRP B CG    1 
ATOM   17116 C CD1   . TRP B  1 1153 ? 21.611  74.146  79.047  1.00 31.08 ? 1151 TRP B CD1   1 
ATOM   17117 C CD2   . TRP B  1 1153 ? 22.023  73.694  76.891  1.00 33.18 ? 1151 TRP B CD2   1 
ATOM   17118 N NE1   . TRP B  1 1153 ? 20.617  74.734  78.291  1.00 33.50 ? 1151 TRP B NE1   1 
ATOM   17119 C CE2   . TRP B  1 1153 ? 20.853  74.474  76.966  1.00 35.58 ? 1151 TRP B CE2   1 
ATOM   17120 C CE3   . TRP B  1 1153 ? 22.486  73.292  75.632  1.00 31.59 ? 1151 TRP B CE3   1 
ATOM   17121 C CZ2   . TRP B  1 1153 ? 20.145  74.864  75.830  1.00 36.56 ? 1151 TRP B CZ2   1 
ATOM   17122 C CZ3   . TRP B  1 1153 ? 21.779  73.683  74.506  1.00 31.92 ? 1151 TRP B CZ3   1 
ATOM   17123 C CH2   . TRP B  1 1153 ? 20.618  74.454  74.615  1.00 34.68 ? 1151 TRP B CH2   1 
ATOM   17124 N N     . SER B  1 1154 ? 25.088  69.719  78.321  1.00 30.24 ? 1152 SER B N     1 
ATOM   17125 C CA    . SER B  1 1154 ? 26.277  68.896  78.467  1.00 30.05 ? 1152 SER B CA    1 
ATOM   17126 C C     . SER B  1 1154 ? 27.286  69.223  77.380  1.00 26.42 ? 1152 SER B C     1 
ATOM   17127 O O     . SER B  1 1154 ? 26.954  69.175  76.190  1.00 29.46 ? 1152 SER B O     1 
ATOM   17128 C CB    . SER B  1 1154 ? 25.931  67.413  78.404  1.00 29.11 ? 1152 SER B CB    1 
ATOM   17129 O OG    . SER B  1 1154 ? 27.125  66.652  78.486  1.00 29.57 ? 1152 SER B OG    1 
ATOM   17130 N N     . LYS B  1 1155 ? 28.516  69.523  77.799  1.00 31.42 ? 1153 LYS B N     1 
ATOM   17131 C CA    . LYS B  1 1155 ? 29.669  69.634  76.917  1.00 31.54 ? 1153 LYS B CA    1 
ATOM   17132 C C     . LYS B  1 1155 ? 30.545  68.394  76.990  1.00 31.07 ? 1153 LYS B C     1 
ATOM   17133 O O     . LYS B  1 1155 ? 31.637  68.377  76.418  1.00 37.99 ? 1153 LYS B O     1 
ATOM   17134 C CB    . LYS B  1 1155 ? 30.498  70.877  77.275  1.00 34.59 ? 1153 LYS B CB    1 
ATOM   17135 N N     . ASP B  1 1156 ? 30.095  67.366  77.707  1.00 30.16 ? 1154 ASP B N     1 
ATOM   17136 C CA    . ASP B  1 1156 ? 30.918  66.188  77.985  1.00 27.51 ? 1154 ASP B CA    1 
ATOM   17137 C C     . ASP B  1 1156 ? 29.926  65.047  78.236  1.00 28.34 ? 1154 ASP B C     1 
ATOM   17138 O O     . ASP B  1 1156 ? 29.550  64.781  79.379  1.00 28.43 ? 1154 ASP B O     1 
ATOM   17139 C CB    . ASP B  1 1156 ? 31.827  66.413  79.173  1.00 27.50 ? 1154 ASP B CB    1 
ATOM   17140 C CG    . ASP B  1 1156 ? 32.850  65.293  79.358  1.00 25.64 ? 1154 ASP B CG    1 
ATOM   17141 O OD1   . ASP B  1 1156 ? 32.571  64.146  78.945  1.00 28.27 ? 1154 ASP B OD1   1 
ATOM   17142 O OD2   . ASP B  1 1156 ? 33.941  65.574  79.893  1.00 32.06 ? 1154 ASP B OD2   1 
ATOM   17143 N N     . TRP B  1 1157 ? 29.514  64.390  77.154  1.00 24.32 ? 1155 TRP B N     1 
ATOM   17144 C CA    . TRP B  1 1157 ? 28.431  63.420  77.282  1.00 25.94 ? 1155 TRP B CA    1 
ATOM   17145 C C     . TRP B  1 1157 ? 28.843  62.252  78.165  1.00 29.23 ? 1155 TRP B C     1 
ATOM   17146 O O     . TRP B  1 1157 ? 28.016  61.700  78.897  1.00 27.33 ? 1155 TRP B O     1 
ATOM   17147 C CB    . TRP B  1 1157 ? 28.008  62.897  75.918  1.00 24.83 ? 1155 TRP B CB    1 
ATOM   17148 C CG    . TRP B  1 1157 ? 27.513  63.911  74.934  1.00 28.07 ? 1155 TRP B CG    1 
ATOM   17149 C CD1   . TRP B  1 1157 ? 27.247  65.232  75.150  1.00 27.16 ? 1155 TRP B CD1   1 
ATOM   17150 C CD2   . TRP B  1 1157 ? 27.214  63.656  73.563  1.00 27.59 ? 1155 TRP B CD2   1 
ATOM   17151 N NE1   . TRP B  1 1157 ? 26.821  65.822  73.976  1.00 26.55 ? 1155 TRP B NE1   1 
ATOM   17152 C CE2   . TRP B  1 1157 ? 26.783  64.866  72.992  1.00 27.27 ? 1155 TRP B CE2   1 
ATOM   17153 C CE3   . TRP B  1 1157 ? 27.271  62.510  72.760  1.00 29.38 ? 1155 TRP B CE3   1 
ATOM   17154 C CZ2   . TRP B  1 1157 ? 26.412  64.966  71.649  1.00 29.92 ? 1155 TRP B CZ2   1 
ATOM   17155 C CZ3   . TRP B  1 1157 ? 26.896  62.607  71.436  1.00 28.68 ? 1155 TRP B CZ3   1 
ATOM   17156 C CH2   . TRP B  1 1157 ? 26.485  63.833  70.889  1.00 30.58 ? 1155 TRP B CH2   1 
ATOM   17157 N N     . ALA B  1 1158 ? 30.112  61.838  78.093  1.00 26.87 ? 1156 ALA B N     1 
ATOM   17158 C CA    . ALA B  1 1158 ? 30.505  60.667  78.864  1.00 30.79 ? 1156 ALA B CA    1 
ATOM   17159 C C     . ALA B  1 1158 ? 30.571  60.971  80.349  1.00 29.22 ? 1156 ALA B C     1 
ATOM   17160 O O     . ALA B  1 1158 ? 30.313  60.081  81.168  1.00 31.35 ? 1156 ALA B O     1 
ATOM   17161 C CB    . ALA B  1 1158 ? 31.845  60.121  78.382  1.00 25.45 ? 1156 ALA B CB    1 
ATOM   17162 N N     . ALA B  1 1159 ? 30.940  62.203  80.715  1.00 28.95 ? 1157 ALA B N     1 
ATOM   17163 C CA    . ALA B  1 1159 ? 31.047  62.574  82.118  1.00 28.31 ? 1157 ALA B CA    1 
ATOM   17164 C C     . ALA B  1 1159 ? 29.700  62.927  82.736  1.00 29.93 ? 1157 ALA B C     1 
ATOM   17165 O O     . ALA B  1 1159 ? 29.543  62.818  83.953  1.00 30.06 ? 1157 ALA B O     1 
ATOM   17166 C CB    . ALA B  1 1159 ? 32.001  63.751  82.285  1.00 28.52 ? 1157 ALA B CB    1 
ATOM   17167 N N     . ASP B  1 1160 ? 28.736  63.342  81.934  1.00 28.87 ? 1158 ASP B N     1 
ATOM   17168 C CA    . ASP B  1 1160 ? 27.441  63.774  82.444  1.00 30.01 ? 1158 ASP B CA    1 
ATOM   17169 C C     . ASP B  1 1160 ? 26.399  62.667  82.459  1.00 30.41 ? 1158 ASP B C     1 
ATOM   17170 O O     . ASP B  1 1160 ? 25.278  62.894  82.929  1.00 30.18 ? 1158 ASP B O     1 
ATOM   17171 C CB    . ASP B  1 1160 ? 26.952  64.966  81.625  1.00 28.49 ? 1158 ASP B CB    1 
ATOM   17172 C CG    . ASP B  1 1160 ? 27.830  66.184  81.814  1.00 31.77 ? 1158 ASP B CG    1 
ATOM   17173 O OD1   . ASP B  1 1160 ? 28.550  66.234  82.846  1.00 35.21 ? 1158 ASP B OD1   1 
ATOM   17174 O OD2   . ASP B  1 1160 ? 27.815  67.088  80.943  1.00 34.22 ? 1158 ASP B OD2   1 
ATOM   17175 N N     . GLY B  1 1161 ? 26.733  61.481  81.967  1.00 27.86 ? 1159 GLY B N     1 
ATOM   17176 C CA    . GLY B  1 1161 ? 25.817  60.370  82.003  1.00 28.25 ? 1159 GLY B CA    1 
ATOM   17177 C C     . GLY B  1 1161 ? 25.774  59.762  83.389  1.00 33.66 ? 1159 GLY B C     1 
ATOM   17178 O O     . GLY B  1 1161 ? 26.353  60.299  84.338  1.00 35.24 ? 1159 GLY B O     1 
ATOM   17179 N N     . PRO B  1 1162 ? 25.112  58.613  83.532  1.00 34.00 ? 1160 PRO B N     1 
ATOM   17180 C CA    . PRO B  1 1162 ? 24.487  57.798  82.488  1.00 31.37 ? 1160 PRO B CA    1 
ATOM   17181 C C     . PRO B  1 1162 ? 23.205  58.439  82.022  1.00 30.35 ? 1160 PRO B C     1 
ATOM   17182 O O     . PRO B  1 1162 ? 22.506  59.092  82.792  1.00 32.14 ? 1160 PRO B O     1 
ATOM   17183 C CB    . PRO B  1 1162 ? 24.221  56.469  83.205  1.00 35.37 ? 1160 PRO B CB    1 
ATOM   17184 C CG    . PRO B  1 1162 ? 23.882  56.912  84.614  1.00 31.44 ? 1160 PRO B CG    1 
ATOM   17185 C CD    . PRO B  1 1162 ? 24.826  58.074  84.879  1.00 38.58 ? 1160 PRO B CD    1 
ATOM   17186 N N     . PHE B  1 1163 ? 22.900  58.291  80.743  1.00 26.08 ? 1161 PHE B N     1 
ATOM   17187 C CA    . PHE B  1 1163 ? 21.622  58.699  80.191  1.00 27.77 ? 1161 PHE B CA    1 
ATOM   17188 C C     . PHE B  1 1163 ? 20.739  57.467  80.010  1.00 26.21 ? 1161 PHE B C     1 
ATOM   17189 O O     . PHE B  1 1163 ? 21.177  56.325  80.158  1.00 28.10 ? 1161 PHE B O     1 
ATOM   17190 C CB    . PHE B  1 1163 ? 21.830  59.453  78.866  1.00 26.59 ? 1161 PHE B CB    1 
ATOM   17191 C CG    . PHE B  1 1163 ? 22.733  60.641  78.997  1.00 28.15 ? 1161 PHE B CG    1 
ATOM   17192 C CD1   . PHE B  1 1163 ? 22.348  61.743  79.751  1.00 27.28 ? 1161 PHE B CD1   1 
ATOM   17193 C CD2   . PHE B  1 1163 ? 23.977  60.657  78.386  1.00 27.84 ? 1161 PHE B CD2   1 
ATOM   17194 C CE1   . PHE B  1 1163 ? 23.189  62.832  79.895  1.00 30.13 ? 1161 PHE B CE1   1 
ATOM   17195 C CE2   . PHE B  1 1163 ? 24.818  61.751  78.524  1.00 27.19 ? 1161 PHE B CE2   1 
ATOM   17196 C CZ    . PHE B  1 1163 ? 24.424  62.840  79.282  1.00 30.82 ? 1161 PHE B CZ    1 
ATOM   17197 N N     . ALA B  1 1164 ? 19.470  57.712  79.710  1.00 27.98 ? 1162 ALA B N     1 
ATOM   17198 C CA    . ALA B  1 1164 ? 18.486  56.650  79.576  1.00 27.22 ? 1162 ALA B CA    1 
ATOM   17199 C C     . ALA B  1 1164 ? 17.975  56.510  78.152  1.00 29.02 ? 1162 ALA B C     1 
ATOM   17200 O O     . ALA B  1 1164 ? 17.097  55.682  77.900  1.00 29.43 ? 1162 ALA B O     1 
ATOM   17201 C CB    . ALA B  1 1164 ? 17.306  56.900  80.530  1.00 27.24 ? 1162 ALA B CB    1 
ATOM   17202 N N     . GLY B  1 1165 ? 18.500  57.297  77.223  1.00 26.23 ? 1163 GLY B N     1 
ATOM   17203 C CA    . GLY B  1 1165 ? 18.030  57.308  75.850  1.00 25.09 ? 1163 GLY B CA    1 
ATOM   17204 C C     . GLY B  1 1165 ? 18.671  58.483  75.151  1.00 25.63 ? 1163 GLY B C     1 
ATOM   17205 O O     . GLY B  1 1165 ? 19.351  59.303  75.764  1.00 25.05 ? 1163 GLY B O     1 
ATOM   17206 N N     . ALA B  1 1166 ? 18.451  58.556  73.846  1.00 26.07 ? 1164 ALA B N     1 
ATOM   17207 C CA    . ALA B  1 1166 ? 18.995  59.672  73.100  1.00 26.11 ? 1164 ALA B CA    1 
ATOM   17208 C C     . ALA B  1 1166 ? 18.085  59.987  71.927  1.00 22.53 ? 1164 ALA B C     1 
ATOM   17209 O O     . ALA B  1 1166 ? 17.585  59.083  71.255  1.00 26.99 ? 1164 ALA B O     1 
ATOM   17210 C CB    . ALA B  1 1166 ? 20.412  59.377  72.605  1.00 25.30 ? 1164 ALA B CB    1 
ATOM   17211 N N     . LEU B  1 1167 ? 17.875  61.275  71.698  1.00 21.93 ? 1165 LEU B N     1 
ATOM   17212 C CA    . LEU B  1 1167 ? 17.146  61.775  70.541  1.00 27.52 ? 1165 LEU B CA    1 
ATOM   17213 C C     . LEU B  1 1167 ? 18.116  62.593  69.701  1.00 26.71 ? 1165 LEU B C     1 
ATOM   17214 O O     . LEU B  1 1167 ? 18.812  63.467  70.231  1.00 27.28 ? 1165 LEU B O     1 
ATOM   17215 C CB    . LEU B  1 1167 ? 15.948  62.632  70.969  1.00 23.97 ? 1165 LEU B CB    1 
ATOM   17216 C CG    . LEU B  1 1167 ? 14.889  61.980  71.874  1.00 24.86 ? 1165 LEU B CG    1 
ATOM   17217 C CD1   . LEU B  1 1167 ? 13.698  62.911  72.038  1.00 24.33 ? 1165 LEU B CD1   1 
ATOM   17218 C CD2   . LEU B  1 1167 ? 14.420  60.682  71.279  1.00 23.21 ? 1165 LEU B CD2   1 
ATOM   17219 N N     . VAL B  1 1168 ? 18.190  62.299  68.401  1.00 27.20 ? 1166 VAL B N     1 
ATOM   17220 C CA    . VAL B  1 1168 ? 19.178  62.932  67.530  1.00 28.46 ? 1166 VAL B CA    1 
ATOM   17221 C C     . VAL B  1 1168 ? 18.468  63.535  66.324  1.00 28.12 ? 1166 VAL B C     1 
ATOM   17222 O O     . VAL B  1 1168 ? 17.592  62.899  65.731  1.00 28.46 ? 1166 VAL B O     1 
ATOM   17223 C CB    . VAL B  1 1168 ? 20.255  61.927  67.067  1.00 26.99 ? 1166 VAL B CB    1 
ATOM   17224 C CG1   . VAL B  1 1168 ? 21.312  62.616  66.208  1.00 30.60 ? 1166 VAL B CG1   1 
ATOM   17225 C CG2   . VAL B  1 1168 ? 20.897  61.195  68.271  1.00 26.29 ? 1166 VAL B CG2   1 
ATOM   17226 N N     . GLU B  1 1169 ? 18.861  64.756  65.954  1.00 27.98 ? 1167 GLU B N     1 
ATOM   17227 C CA    . GLU B  1 1169 ? 18.390  65.428  64.747  1.00 30.17 ? 1167 GLU B CA    1 
ATOM   17228 C C     . GLU B  1 1169 ? 19.589  65.682  63.840  1.00 31.61 ? 1167 GLU B C     1 
ATOM   17229 O O     . GLU B  1 1169 ? 20.594  66.224  64.296  1.00 31.52 ? 1167 GLU B O     1 
ATOM   17230 C CB    . GLU B  1 1169 ? 17.713  66.758  65.095  1.00 30.94 ? 1167 GLU B CB    1 
ATOM   17231 C CG    . GLU B  1 1169 ? 17.255  67.575  63.898  1.00 31.39 ? 1167 GLU B CG    1 
ATOM   17232 C CD    . GLU B  1 1169 ? 16.886  69.015  64.266  1.00 32.23 ? 1167 GLU B CD    1 
ATOM   17233 O OE1   . GLU B  1 1169 ? 17.169  69.443  65.408  1.00 29.85 ? 1167 GLU B OE1   1 
ATOM   17234 O OE2   . GLU B  1 1169 ? 16.323  69.727  63.404  1.00 36.22 ? 1167 GLU B OE2   1 
ATOM   17235 N N     . GLY B  1 1170 ? 19.496  65.291  62.574  1.00 33.44 ? 1168 GLY B N     1 
ATOM   17236 C CA    . GLY B  1 1170 ? 20.562  65.617  61.645  1.00 33.37 ? 1168 GLY B CA    1 
ATOM   17237 C C     . GLY B  1 1170 ? 20.409  64.866  60.341  1.00 34.61 ? 1168 GLY B C     1 
ATOM   17238 O O     . GLY B  1 1170 ? 19.508  64.041  60.170  1.00 35.11 ? 1168 GLY B O     1 
ATOM   17239 N N     . ASP B  1 1171 ? 21.311  65.179  59.407  1.00 38.10 ? 1169 ASP B N     1 
ATOM   17240 C CA    . ASP B  1 1171 ? 21.347  64.410  58.176  1.00 38.39 ? 1169 ASP B CA    1 
ATOM   17241 C C     . ASP B  1 1171 ? 22.029  63.068  58.429  1.00 38.48 ? 1169 ASP B C     1 
ATOM   17242 O O     . ASP B  1 1171 ? 22.469  62.764  59.540  1.00 37.09 ? 1169 ASP B O     1 
ATOM   17243 C CB    . ASP B  1 1171 ? 22.036  65.193  57.055  1.00 41.25 ? 1169 ASP B CB    1 
ATOM   17244 C CG    . ASP B  1 1171 ? 23.477  65.576  57.373  1.00 45.54 ? 1169 ASP B CG    1 
ATOM   17245 O OD1   . ASP B  1 1171 ? 24.073  65.094  58.366  1.00 40.70 ? 1169 ASP B OD1   1 
ATOM   17246 O OD2   . ASP B  1 1171 ? 24.032  66.385  56.593  1.00 45.32 ? 1169 ASP B OD2   1 
ATOM   17247 N N     . ALA B  1 1172 ? 22.132  62.258  57.374  1.00 38.26 ? 1170 ALA B N     1 
ATOM   17248 C CA    . ALA B  1 1172 ? 22.676  60.915  57.528  1.00 37.34 ? 1170 ALA B CA    1 
ATOM   17249 C C     . ALA B  1 1172 ? 24.088  60.939  58.109  1.00 38.49 ? 1170 ALA B C     1 
ATOM   17250 O O     . ALA B  1 1172 ? 24.407  60.138  58.995  1.00 40.47 ? 1170 ALA B O     1 
ATOM   17251 C CB    . ALA B  1 1172 ? 22.651  60.187  56.185  1.00 41.29 ? 1170 ALA B CB    1 
ATOM   17252 N N     . GLU B  1 1173 ? 24.947  61.850  57.633  1.00 37.25 ? 1171 GLU B N     1 
ATOM   17253 C CA    . GLU B  1 1173 ? 26.317  61.907  58.136  1.00 37.99 ? 1171 GLU B CA    1 
ATOM   17254 C C     . GLU B  1 1173 ? 26.342  62.274  59.617  1.00 36.63 ? 1171 GLU B C     1 
ATOM   17255 O O     . GLU B  1 1173 ? 27.050  61.645  60.413  1.00 37.06 ? 1171 GLU B O     1 
ATOM   17256 C CB    . GLU B  1 1173 ? 27.147  62.905  57.322  1.00 43.59 ? 1171 GLU B CB    1 
ATOM   17257 N N     . ARG B  1 1174 ? 25.580  63.303  60.001  1.00 35.46 ? 1172 ARG B N     1 
ATOM   17258 C CA    . ARG B  1 1174 ? 25.503  63.693  61.407  1.00 34.66 ? 1172 ARG B CA    1 
ATOM   17259 C C     . ARG B  1 1174 ? 25.008  62.543  62.275  1.00 32.80 ? 1172 ARG B C     1 
ATOM   17260 O O     . ARG B  1 1174 ? 25.551  62.296  63.356  1.00 34.75 ? 1172 ARG B O     1 
ATOM   17261 C CB    . ARG B  1 1174 ? 24.590  64.912  61.555  1.00 37.41 ? 1172 ARG B CB    1 
ATOM   17262 C CG    . ARG B  1 1174 ? 24.366  65.379  62.981  1.00 35.74 ? 1172 ARG B CG    1 
ATOM   17263 C CD    . ARG B  1 1174 ? 25.656  65.888  63.590  1.00 39.19 ? 1172 ARG B CD    1 
ATOM   17264 N NE    . ARG B  1 1174 ? 25.453  66.308  64.969  1.00 39.10 ? 1172 ARG B NE    1 
ATOM   17265 C CZ    . ARG B  1 1174 ? 26.427  66.467  65.853  1.00 39.70 ? 1172 ARG B CZ    1 
ATOM   17266 N NH1   . ARG B  1 1174 ? 27.693  66.256  65.531  1.00 35.56 ? 1172 ARG B NH1   1 
ATOM   17267 N NH2   . ARG B  1 1174 ? 26.121  66.824  67.098  1.00 38.13 ? 1172 ARG B NH2   1 
ATOM   17268 N N     . ILE B  1 1175 ? 23.995  61.812  61.805  1.00 29.18 ? 1173 ILE B N     1 
ATOM   17269 C CA    . ILE B  1 1175 ? 23.411  60.743  62.612  1.00 36.16 ? 1173 ILE B CA    1 
ATOM   17270 C C     . ILE B  1 1175 ? 24.434  59.639  62.850  1.00 34.97 ? 1173 ILE B C     1 
ATOM   17271 O O     . ILE B  1 1175 ? 24.587  59.147  63.975  1.00 32.63 ? 1173 ILE B O     1 
ATOM   17272 C CB    . ILE B  1 1175 ? 22.134  60.207  61.941  1.00 36.65 ? 1173 ILE B CB    1 
ATOM   17273 C CG1   . ILE B  1 1175 ? 21.004  61.234  62.046  1.00 36.64 ? 1173 ILE B CG1   1 
ATOM   17274 C CG2   . ILE B  1 1175 ? 21.707  58.881  62.558  1.00 35.10 ? 1173 ILE B CG2   1 
ATOM   17275 C CD1   . ILE B  1 1175 ? 19.827  60.906  61.151  1.00 37.63 ? 1173 ILE B CD1   1 
ATOM   17276 N N     . ARG B  1 1176 ? 25.169  59.252  61.801  1.00 32.38 ? 1174 ARG B N     1 
ATOM   17277 C CA    . ARG B  1 1176 ? 26.189  58.215  61.951  1.00 34.74 ? 1174 ARG B CA    1 
ATOM   17278 C C     . ARG B  1 1176 ? 27.255  58.629  62.959  1.00 31.83 ? 1174 ARG B C     1 
ATOM   17279 O O     . ARG B  1 1176 ? 27.634  57.837  63.828  1.00 33.58 ? 1174 ARG B O     1 
ATOM   17280 C CB    . ARG B  1 1176 ? 26.821  57.900  60.591  1.00 35.21 ? 1174 ARG B CB    1 
ATOM   17281 C CG    . ARG B  1 1176 ? 27.910  56.819  60.632  1.00 38.99 ? 1174 ARG B CG    1 
ATOM   17282 C CD    . ARG B  1 1176 ? 28.692  56.719  59.307  1.00 43.20 ? 1174 ARG B CD    1 
ATOM   17283 N NE    . ARG B  1 1176 ? 27.824  56.824  58.135  1.00 51.37 ? 1174 ARG B NE    1 
ATOM   17284 C CZ    . ARG B  1 1176 ? 27.224  55.799  57.535  1.00 53.34 ? 1174 ARG B CZ    1 
ATOM   17285 N NH1   . ARG B  1 1176 ? 27.433  54.551  57.923  1.00 53.27 ? 1174 ARG B NH1   1 
ATOM   17286 N NH2   . ARG B  1 1176 ? 26.390  56.034  56.522  1.00 51.11 ? 1174 ARG B NH2   1 
ATOM   17287 N N     . ALA B  1 1177 ? 27.729  59.876  62.876  1.00 31.93 ? 1175 ALA B N     1 
ATOM   17288 C CA    . ALA B  1 1177 ? 28.768  60.352  63.786  1.00 34.63 ? 1175 ALA B CA    1 
ATOM   17289 C C     . ALA B  1 1177 ? 28.271  60.418  65.224  1.00 30.00 ? 1175 ALA B C     1 
ATOM   17290 O O     . ALA B  1 1177 ? 29.009  60.086  66.159  1.00 31.75 ? 1175 ALA B O     1 
ATOM   17291 C CB    . ALA B  1 1177 ? 29.272  61.723  63.336  1.00 31.96 ? 1175 ALA B CB    1 
ATOM   17292 N N     . VAL B  1 1178 ? 27.033  60.867  65.424  1.00 30.26 ? 1176 VAL B N     1 
ATOM   17293 C CA    . VAL B  1 1178 ? 26.490  60.944  66.775  1.00 29.31 ? 1176 VAL B CA    1 
ATOM   17294 C C     . VAL B  1 1178 ? 26.253  59.546  67.321  1.00 31.57 ? 1176 VAL B C     1 
ATOM   17295 O O     . VAL B  1 1178 ? 26.549  59.256  68.487  1.00 31.25 ? 1176 VAL B O     1 
ATOM   17296 C CB    . VAL B  1 1178 ? 25.208  61.802  66.766  1.00 28.67 ? 1176 VAL B CB    1 
ATOM   17297 C CG1   . VAL B  1 1178 ? 24.540  61.825  68.129  1.00 31.20 ? 1176 VAL B CG1   1 
ATOM   17298 C CG2   . VAL B  1 1178 ? 25.546  63.229  66.320  1.00 32.05 ? 1176 VAL B CG2   1 
ATOM   17299 N N     . ASN B  1 1179 ? 25.724  58.656  66.479  1.00 30.90 ? 1177 ASN B N     1 
ATOM   17300 C CA    . ASN B  1 1179 ? 25.501  57.269  66.869  1.00 31.19 ? 1177 ASN B CA    1 
ATOM   17301 C C     . ASN B  1 1179 ? 26.811  56.593  67.260  1.00 32.12 ? 1177 ASN B C     1 
ATOM   17302 O O     . ASN B  1 1179 ? 26.855  55.796  68.208  1.00 28.98 ? 1177 ASN B O     1 
ATOM   17303 C CB    . ASN B  1 1179 ? 24.826  56.538  65.708  1.00 31.57 ? 1177 ASN B CB    1 
ATOM   17304 C CG    . ASN B  1 1179 ? 24.154  55.265  66.128  1.00 35.19 ? 1177 ASN B CG    1 
ATOM   17305 O OD1   . ASN B  1 1179 ? 23.605  55.166  67.224  1.00 34.21 ? 1177 ASN B OD1   1 
ATOM   17306 N ND2   . ASN B  1 1179 ? 24.187  54.273  65.250  1.00 34.69 ? 1177 ASN B ND2   1 
ATOM   17307 N N     . LYS B  1 1180 ? 27.898  56.919  66.553  1.00 31.65 ? 1178 LYS B N     1 
ATOM   17308 C CA    . LYS B  1 1180 ? 29.207  56.366  66.891  1.00 31.83 ? 1178 LYS B CA    1 
ATOM   17309 C C     . LYS B  1 1180 ? 29.717  56.915  68.219  1.00 29.41 ? 1178 LYS B C     1 
ATOM   17310 O O     . LYS B  1 1180 ? 30.294  56.174  69.021  1.00 30.36 ? 1178 LYS B O     1 
ATOM   17311 C CB    . LYS B  1 1180 ? 30.212  56.657  65.773  1.00 32.11 ? 1178 LYS B CB    1 
ATOM   17312 C CG    . LYS B  1 1180 ? 30.017  55.809  64.529  1.00 38.72 ? 1178 LYS B CG    1 
ATOM   17313 C CD    . LYS B  1 1180 ? 30.981  56.233  63.402  1.00 44.24 ? 1178 LYS B CD    1 
ATOM   17314 C CE    . LYS B  1 1180 ? 32.405  55.835  63.713  1.00 52.29 ? 1178 LYS B CE    1 
ATOM   17315 N NZ    . LYS B  1 1180 ? 32.522  54.351  63.811  1.00 54.45 ? 1178 LYS B NZ    1 
ATOM   17316 N N     . ALA B  1 1181 ? 29.510  58.205  68.473  1.00 30.82 ? 1179 ALA B N     1 
ATOM   17317 C CA    . ALA B  1 1181 ? 29.916  58.770  69.756  1.00 29.73 ? 1179 ALA B CA    1 
ATOM   17318 C C     . ALA B  1 1181 ? 29.085  58.191  70.896  1.00 28.71 ? 1179 ALA B C     1 
ATOM   17319 O O     . ALA B  1 1181 ? 29.612  57.926  71.982  1.00 28.09 ? 1179 ALA B O     1 
ATOM   17320 C CB    . ALA B  1 1181 ? 29.803  60.296  69.716  1.00 32.48 ? 1179 ALA B CB    1 
ATOM   17321 N N     . ILE B  1 1182 ? 27.785  57.966  70.665  1.00 26.88 ? 1180 ILE B N     1 
ATOM   17322 C CA    . ILE B  1 1182 ? 26.944  57.404  71.717  1.00 30.29 ? 1180 ILE B CA    1 
ATOM   17323 C C     . ILE B  1 1182 ? 27.349  55.969  72.015  1.00 30.63 ? 1180 ILE B C     1 
ATOM   17324 O O     . ILE B  1 1182 ? 27.426  55.557  73.178  1.00 30.29 ? 1180 ILE B O     1 
ATOM   17325 C CB    . ILE B  1 1182 ? 25.458  57.510  71.323  1.00 30.89 ? 1180 ILE B CB    1 
ATOM   17326 C CG1   . ILE B  1 1182 ? 25.015  58.978  71.373  1.00 28.85 ? 1180 ILE B CG1   1 
ATOM   17327 C CG2   . ILE B  1 1182 ? 24.592  56.615  72.225  1.00 32.15 ? 1180 ILE B CG2   1 
ATOM   17328 C CD1   . ILE B  1 1182 ? 23.671  59.239  70.739  1.00 29.26 ? 1180 ILE B CD1   1 
ATOM   17329 N N     . ALA B  1 1183 ? 27.628  55.186  70.975  1.00 32.67 ? 1181 ALA B N     1 
ATOM   17330 C CA    . ALA B  1 1183 ? 28.062  53.814  71.193  1.00 33.26 ? 1181 ALA B CA    1 
ATOM   17331 C C     . ALA B  1 1183 ? 29.346  53.732  72.006  1.00 31.67 ? 1181 ALA B C     1 
ATOM   17332 O O     . ALA B  1 1183 ? 29.604  52.696  72.622  1.00 32.30 ? 1181 ALA B O     1 
ATOM   17333 C CB    . ALA B  1 1183 ? 28.246  53.097  69.853  1.00 32.71 ? 1181 ALA B CB    1 
ATOM   17334 N N     . ALA B  1 1184 ? 30.155  54.794  72.035  1.00 29.71 ? 1182 ALA B N     1 
ATOM   17335 C CA    . ALA B  1 1184 ? 31.397  54.805  72.798  1.00 33.34 ? 1182 ALA B CA    1 
ATOM   17336 C C     . ALA B  1 1184 ? 31.226  55.296  74.233  1.00 32.18 ? 1182 ALA B C     1 
ATOM   17337 O O     . ALA B  1 1184 ? 32.209  55.333  74.974  1.00 30.90 ? 1182 ALA B O     1 
ATOM   17338 C CB    . ALA B  1 1184 ? 32.449  55.672  72.089  1.00 28.89 ? 1182 ALA B CB    1 
ATOM   17339 N N     . LEU B  1 1185 ? 30.026  55.697  74.640  1.00 30.01 ? 1183 LEU B N     1 
ATOM   17340 C CA    . LEU B  1 1185 ? 29.846  56.179  76.001  1.00 32.55 ? 1183 LEU B CA    1 
ATOM   17341 C C     . LEU B  1 1185 ? 29.936  55.017  76.986  1.00 32.94 ? 1183 LEU B C     1 
ATOM   17342 O O     . LEU B  1 1185 ? 29.563  53.884  76.663  1.00 31.76 ? 1183 LEU B O     1 
ATOM   17343 C CB    . LEU B  1 1185 ? 28.499  56.875  76.166  1.00 31.93 ? 1183 LEU B CB    1 
ATOM   17344 C CG    . LEU B  1 1185 ? 28.230  58.110  75.314  1.00 31.87 ? 1183 LEU B CG    1 
ATOM   17345 C CD1   . LEU B  1 1185 ? 26.773  58.548  75.511  1.00 25.63 ? 1183 LEU B CD1   1 
ATOM   17346 C CD2   . LEU B  1 1185 ? 29.190  59.207  75.700  1.00 31.09 ? 1183 LEU B CD2   1 
ATOM   17347 N N     . PRO B  1 1186 ? 30.434  55.268  78.190  1.00 33.99 ? 1184 PRO B N     1 
ATOM   17348 C CA    . PRO B  1 1186 ? 30.472  54.217  79.204  1.00 37.23 ? 1184 PRO B CA    1 
ATOM   17349 C C     . PRO B  1 1186 ? 29.091  53.969  79.789  1.00 30.29 ? 1184 PRO B C     1 
ATOM   17350 O O     . PRO B  1 1186 ? 28.188  54.806  79.722  1.00 32.78 ? 1184 PRO B O     1 
ATOM   17351 C CB    . PRO B  1 1186 ? 31.427  54.780  80.263  1.00 34.60 ? 1184 PRO B CB    1 
ATOM   17352 C CG    . PRO B  1 1186 ? 31.278  56.257  80.135  1.00 36.93 ? 1184 PRO B CG    1 
ATOM   17353 C CD    . PRO B  1 1186 ? 31.048  56.519  78.665  1.00 34.71 ? 1184 PRO B CD    1 
ATOM   17354 N N     . GLY B  1 1187 ? 28.938  52.787  80.373  1.00 31.90 ? 1185 GLY B N     1 
ATOM   17355 C CA    . GLY B  1 1187 ? 27.709  52.450  81.050  1.00 32.25 ? 1185 GLY B CA    1 
ATOM   17356 C C     . GLY B  1 1187 ? 26.694  51.792  80.138  1.00 31.63 ? 1185 GLY B C     1 
ATOM   17357 O O     . GLY B  1 1187 ? 27.037  50.982  79.270  1.00 33.65 ? 1185 GLY B O     1 
ATOM   17358 N N     . PRO B  1 1188 ? 25.422  52.139  80.305  1.00 34.77 ? 1186 PRO B N     1 
ATOM   17359 C CA    . PRO B  1 1188 ? 24.368  51.409  79.592  1.00 31.57 ? 1186 PRO B CA    1 
ATOM   17360 C C     . PRO B  1 1188 ? 24.375  51.724  78.107  1.00 32.21 ? 1186 PRO B C     1 
ATOM   17361 O O     . PRO B  1 1188 ? 24.763  52.812  77.684  1.00 30.21 ? 1186 PRO B O     1 
ATOM   17362 C CB    . PRO B  1 1188 ? 23.081  51.919  80.248  1.00 33.85 ? 1186 PRO B CB    1 
ATOM   17363 C CG    . PRO B  1 1188 ? 23.416  53.317  80.621  1.00 37.56 ? 1186 PRO B CG    1 
ATOM   17364 C CD    . PRO B  1 1188 ? 24.886  53.305  81.030  1.00 34.63 ? 1186 PRO B CD    1 
ATOM   17365 N N     . LEU B  1 1189 ? 23.888  50.764  77.318  1.00 31.02 ? 1187 LEU B N     1 
ATOM   17366 C CA    . LEU B  1 1189 ? 23.720  50.957  75.881  1.00 32.96 ? 1187 LEU B CA    1 
ATOM   17367 C C     . LEU B  1 1189 ? 22.470  51.795  75.636  1.00 32.30 ? 1187 LEU B C     1 
ATOM   17368 O O     . LEU B  1 1189 ? 21.369  51.381  76.009  1.00 32.53 ? 1187 LEU B O     1 
ATOM   17369 C CB    . LEU B  1 1189 ? 23.607  49.608  75.168  1.00 32.47 ? 1187 LEU B CB    1 
ATOM   17370 C CG    . LEU B  1 1189 ? 24.855  48.721  75.026  1.00 32.39 ? 1187 LEU B CG    1 
ATOM   17371 C CD1   . LEU B  1 1189 ? 25.298  48.148  76.366  1.00 39.28 ? 1187 LEU B CD1   1 
ATOM   17372 C CD2   . LEU B  1 1189 ? 24.586  47.591  74.053  1.00 32.02 ? 1187 LEU B CD2   1 
ATOM   17373 N N     . LEU B  1 1190 ? 22.630  52.970  75.027  1.00 28.35 ? 1188 LEU B N     1 
ATOM   17374 C CA    . LEU B  1 1190 ? 21.497  53.874  74.844  1.00 31.03 ? 1188 LEU B CA    1 
ATOM   17375 C C     . LEU B  1 1190 ? 20.640  53.469  73.652  1.00 29.51 ? 1188 LEU B C     1 
ATOM   17376 O O     . LEU B  1 1190 ? 21.147  53.100  72.585  1.00 29.87 ? 1188 LEU B O     1 
ATOM   17377 C CB    . LEU B  1 1190 ? 21.965  55.319  74.655  1.00 28.79 ? 1188 LEU B CB    1 
ATOM   17378 C CG    . LEU B  1 1190 ? 22.783  55.963  75.777  1.00 31.65 ? 1188 LEU B CG    1 
ATOM   17379 C CD1   . LEU B  1 1190 ? 22.846  57.484  75.606  1.00 29.13 ? 1188 LEU B CD1   1 
ATOM   17380 C CD2   . LEU B  1 1190 ? 22.274  55.572  77.164  1.00 28.30 ? 1188 LEU B CD2   1 
ATOM   17381 N N     . LEU B  1 1191 ? 19.328  53.552  73.835  1.00 31.10 ? 1189 LEU B N     1 
ATOM   17382 C CA    . LEU B  1 1191 ? 18.394  53.420  72.730  1.00 29.98 ? 1189 LEU B CA    1 
ATOM   17383 C C     . LEU B  1 1191 ? 18.364  54.753  71.988  1.00 32.61 ? 1189 LEU B C     1 
ATOM   17384 O O     . LEU B  1 1191 ? 17.857  55.751  72.508  1.00 30.77 ? 1189 LEU B O     1 
ATOM   17385 C CB    . LEU B  1 1191 ? 17.021  53.023  73.260  1.00 34.98 ? 1189 LEU B CB    1 
ATOM   17386 C CG    . LEU B  1 1191 ? 16.023  52.358  72.318  1.00 38.29 ? 1189 LEU B CG    1 
ATOM   17387 C CD1   . LEU B  1 1191 ? 14.909  51.731  73.141  1.00 34.96 ? 1189 LEU B CD1   1 
ATOM   17388 C CD2   . LEU B  1 1191 ? 15.469  53.369  71.331  1.00 32.67 ? 1189 LEU B CD2   1 
ATOM   17389 N N     . VAL B  1 1192 ? 18.919  54.781  70.784  1.00 29.84 ? 1190 VAL B N     1 
ATOM   17390 C CA    . VAL B  1 1192 ? 19.071  56.014  70.019  1.00 31.14 ? 1190 VAL B CA    1 
ATOM   17391 C C     . VAL B  1 1192 ? 17.938  56.102  69.011  1.00 30.73 ? 1190 VAL B C     1 
ATOM   17392 O O     . VAL B  1 1192 ? 17.668  55.138  68.283  1.00 31.74 ? 1190 VAL B O     1 
ATOM   17393 C CB    . VAL B  1 1192 ? 20.442  56.064  69.324  1.00 32.00 ? 1190 VAL B CB    1 
ATOM   17394 C CG1   . VAL B  1 1192 ? 20.564  57.281  68.417  1.00 28.63 ? 1190 VAL B CG1   1 
ATOM   17395 C CG2   . VAL B  1 1192 ? 21.567  56.070  70.372  1.00 29.72 ? 1190 VAL B CG2   1 
ATOM   17396 N N     . GLN B  1 1193 ? 17.250  57.240  68.987  1.00 27.08 ? 1191 GLN B N     1 
ATOM   17397 C CA    . GLN B  1 1193 ? 16.264  57.534  67.957  1.00 28.21 ? 1191 GLN B CA    1 
ATOM   17398 C C     . GLN B  1 1193 ? 16.716  58.750  67.175  1.00 28.47 ? 1191 GLN B C     1 
ATOM   17399 O O     . GLN B  1 1193 ? 17.120  59.756  67.766  1.00 28.50 ? 1191 GLN B O     1 
ATOM   17400 C CB    . GLN B  1 1193 ? 14.896  57.838  68.530  1.00 25.23 ? 1191 GLN B CB    1 
ATOM   17401 C CG    . GLN B  1 1193 ? 14.315  56.756  69.356  1.00 24.94 ? 1191 GLN B CG    1 
ATOM   17402 C CD    . GLN B  1 1193 ? 12.875  57.067  69.663  1.00 30.19 ? 1191 GLN B CD    1 
ATOM   17403 O OE1   . GLN B  1 1193 ? 12.033  57.098  68.761  1.00 30.36 ? 1191 GLN B OE1   1 
ATOM   17404 N NE2   . GLN B  1 1193 ? 12.587  57.334  70.926  1.00 25.27 ? 1191 GLN B NE2   1 
ATOM   17405 N N     . ALA B  1 1194 ? 16.613  58.675  65.854  1.00 26.37 ? 1192 ALA B N     1 
ATOM   17406 C CA    . ALA B  1 1194 ? 17.122  59.748  65.015  1.00 29.88 ? 1192 ALA B CA    1 
ATOM   17407 C C     . ALA B  1 1194 ? 16.095  60.130  63.967  1.00 30.28 ? 1192 ALA B C     1 
ATOM   17408 O O     . ALA B  1 1194 ? 15.294  59.302  63.525  1.00 29.98 ? 1192 ALA B O     1 
ATOM   17409 C CB    . ALA B  1 1194 ? 18.437  59.361  64.328  1.00 29.55 ? 1192 ALA B CB    1 
ATOM   17410 N N     . ALA B  1 1195 ? 16.138  61.400  63.576  1.00 29.75 ? 1193 ALA B N     1 
ATOM   17411 C CA    . ALA B  1 1195 ? 15.309  61.924  62.503  1.00 33.04 ? 1193 ALA B CA    1 
ATOM   17412 C C     . ALA B  1 1195 ? 16.041  63.093  61.862  1.00 35.64 ? 1193 ALA B C     1 
ATOM   17413 O O     . ALA B  1 1195 ? 16.907  63.718  62.477  1.00 31.85 ? 1193 ALA B O     1 
ATOM   17414 C CB    . ALA B  1 1195 ? 13.939  62.382  63.010  1.00 33.88 ? 1193 ALA B CB    1 
ATOM   17415 N N     . SER B  1 1196 ? 15.685  63.385  60.619  1.00 36.94 ? 1194 SER B N     1 
ATOM   17416 C CA    . SER B  1 1196 ? 16.134  64.607  59.974  1.00 36.13 ? 1194 SER B CA    1 
ATOM   17417 C C     . SER B  1 1196 ? 15.206  65.757  60.343  1.00 36.57 ? 1194 SER B C     1 
ATOM   17418 O O     . SER B  1 1196 ? 14.073  65.550  60.796  1.00 38.53 ? 1194 SER B O     1 
ATOM   17419 C CB    . SER B  1 1196 ? 16.152  64.440  58.459  1.00 38.38 ? 1194 SER B CB    1 
ATOM   17420 O OG    . SER B  1 1196 ? 14.822  64.315  57.994  1.00 40.29 ? 1194 SER B OG    1 
ATOM   17421 N N     . SER B  1 1197 ? 15.693  66.982  60.128  1.00 36.30 ? 1195 SER B N     1 
ATOM   17422 C CA    . SER B  1 1197 ? 14.852  68.155  60.358  1.00 38.93 ? 1195 SER B CA    1 
ATOM   17423 C C     . SER B  1 1197 ? 13.573  68.082  59.541  1.00 37.56 ? 1195 SER B C     1 
ATOM   17424 O O     . SER B  1 1197 ? 12.516  68.534  59.991  1.00 36.70 ? 1195 SER B O     1 
ATOM   17425 C CB    . SER B  1 1197 ? 15.611  69.432  60.012  1.00 36.60 ? 1195 SER B CB    1 
ATOM   17426 O OG    . SER B  1 1197 ? 16.832  69.496  60.717  1.00 34.31 ? 1195 SER B OG    1 
ATOM   17427 N N     . GLY B  1 1198 ? 13.658  67.527  58.331  1.00 39.20 ? 1196 GLY B N     1 
ATOM   17428 C CA    . GLY B  1 1198 ? 12.481  67.435  57.485  1.00 40.97 ? 1196 GLY B CA    1 
ATOM   17429 C C     . GLY B  1 1198 ? 11.468  66.427  57.988  1.00 41.33 ? 1196 GLY B C     1 
ATOM   17430 O O     . GLY B  1 1198 ? 10.258  66.626  57.842  1.00 43.98 ? 1196 GLY B O     1 
ATOM   17431 N N     . GLU B  1 1199 ? 11.939  65.326  58.577  1.00 40.13 ? 1197 GLU B N     1 
ATOM   17432 C CA    . GLU B  1 1199 ? 10.998  64.368  59.152  1.00 41.92 ? 1197 GLU B CA    1 
ATOM   17433 C C     . GLU B  1 1199 ? 10.329  64.937  60.396  1.00 40.89 ? 1197 GLU B C     1 
ATOM   17434 O O     . GLU B  1 1199 ? 9.117   64.771  60.585  1.00 38.89 ? 1197 GLU B O     1 
ATOM   17435 C CB    . GLU B  1 1199 ? 11.695  63.046  59.472  1.00 43.39 ? 1197 GLU B CB    1 
ATOM   17436 C CG    . GLU B  1 1199 ? 10.739  62.044  60.102  1.00 49.11 ? 1197 GLU B CG    1 
ATOM   17437 C CD    . GLU B  1 1199 ? 11.250  60.616  60.077  1.00 55.85 ? 1197 GLU B CD    1 
ATOM   17438 O OE1   . GLU B  1 1199 ? 12.490  60.415  60.013  1.00 54.11 ? 1197 GLU B OE1   1 
ATOM   17439 O OE2   . GLU B  1 1199 ? 10.395  59.697  60.123  1.00 58.57 ? 1197 GLU B OE2   1 
ATOM   17440 N N     . ILE B  1 1200 ? 11.098  65.619  61.251  1.00 35.99 ? 1198 ILE B N     1 
ATOM   17441 C CA    . ILE B  1 1200 ? 10.521  66.281  62.421  1.00 36.40 ? 1198 ILE B CA    1 
ATOM   17442 C C     . ILE B  1 1200 ? 9.387   67.211  62.007  1.00 39.33 ? 1198 ILE B C     1 
ATOM   17443 O O     . ILE B  1 1200 ? 8.352   67.297  62.682  1.00 34.19 ? 1198 ILE B O     1 
ATOM   17444 C CB    . ILE B  1 1200 ? 11.617  67.042  63.192  1.00 36.07 ? 1198 ILE B CB    1 
ATOM   17445 C CG1   . ILE B  1 1200 ? 12.610  66.064  63.821  1.00 33.38 ? 1198 ILE B CG1   1 
ATOM   17446 C CG2   . ILE B  1 1200 ? 11.009  67.923  64.263  1.00 35.52 ? 1198 ILE B CG2   1 
ATOM   17447 C CD1   . ILE B  1 1200 ? 13.772  66.750  64.508  1.00 29.86 ? 1198 ILE B CD1   1 
ATOM   17448 N N     . ALA B  1 1201 ? 9.556   67.913  60.884  1.00 36.75 ? 1199 ALA B N     1 
ATOM   17449 C CA    . ALA B  1 1201 ? 8.519   68.835  60.418  1.00 40.04 ? 1199 ALA B CA    1 
ATOM   17450 C C     . ALA B  1 1201 ? 7.327   68.104  59.797  1.00 42.75 ? 1199 ALA B C     1 
ATOM   17451 O O     . ALA B  1 1201 ? 6.173   68.514  59.990  1.00 39.80 ? 1199 ALA B O     1 
ATOM   17452 C CB    . ALA B  1 1201 ? 9.114   69.823  59.415  1.00 38.31 ? 1199 ALA B CB    1 
ATOM   17453 N N     . ARG B  1 1202 ? 7.579   67.016  59.068  1.00 43.57 ? 1200 ARG B N     1 
ATOM   17454 C CA    . ARG B  1 1202 ? 6.533   66.336  58.311  1.00 41.89 ? 1200 ARG B CA    1 
ATOM   17455 C C     . ARG B  1 1202 ? 5.838   65.223  59.085  1.00 42.63 ? 1200 ARG B C     1 
ATOM   17456 O O     . ARG B  1 1202 ? 4.659   64.951  58.829  1.00 40.38 ? 1200 ARG B O     1 
ATOM   17457 C CB    . ARG B  1 1202 ? 7.120   65.754  57.021  1.00 43.76 ? 1200 ARG B CB    1 
ATOM   17458 N N     . ASN B  1 1203 ? 6.526   64.566  60.011  1.00 39.76 ? 1201 ASN B N     1 
ATOM   17459 C CA    . ASN B  1 1203 ? 6.004   63.352  60.643  1.00 42.40 ? 1201 ASN B CA    1 
ATOM   17460 C C     . ASN B  1 1203 ? 5.836   63.562  62.140  1.00 42.02 ? 1201 ASN B C     1 
ATOM   17461 O O     . ASN B  1 1203 ? 6.845   63.670  62.864  1.00 41.23 ? 1201 ASN B O     1 
ATOM   17462 C CB    . ASN B  1 1203 ? 6.937   62.171  60.360  1.00 42.44 ? 1201 ASN B CB    1 
ATOM   17463 C CG    . ASN B  1 1203 ? 6.471   60.872  61.010  1.00 46.60 ? 1201 ASN B CG    1 
ATOM   17464 O OD1   . ASN B  1 1203 ? 5.353   60.775  61.535  1.00 44.81 ? 1201 ASN B OD1   1 
ATOM   17465 N ND2   . ASN B  1 1203 ? 7.332   59.858  60.968  1.00 46.13 ? 1201 ASN B ND2   1 
ATOM   17466 N N     . PRO B  1 1204 ? 4.604   63.612  62.658  1.00 43.80 ? 1202 PRO B N     1 
ATOM   17467 C CA    . PRO B  1 1204 ? 4.428   63.782  64.110  1.00 37.93 ? 1202 PRO B CA    1 
ATOM   17468 C C     . PRO B  1 1204 ? 4.930   62.600  64.925  1.00 40.59 ? 1202 PRO B C     1 
ATOM   17469 O O     . PRO B  1 1204 ? 5.124   62.744  66.140  1.00 40.81 ? 1202 PRO B O     1 
ATOM   17470 C CB    . PRO B  1 1204 ? 2.910   63.969  64.268  1.00 42.66 ? 1202 PRO B CB    1 
ATOM   17471 C CG    . PRO B  1 1204 ? 2.321   63.322  63.065  1.00 40.76 ? 1202 PRO B CG    1 
ATOM   17472 C CD    . PRO B  1 1204 ? 3.320   63.483  61.947  1.00 43.49 ? 1202 PRO B CD    1 
ATOM   17473 N N     . ASP B  1 1205 ? 5.159   61.443  64.304  1.00 37.27 ? 1203 ASP B N     1 
ATOM   17474 C CA    . ASP B  1 1205 ? 5.753   60.300  64.986  1.00 40.92 ? 1203 ASP B CA    1 
ATOM   17475 C C     . ASP B  1 1205 ? 7.238   60.126  64.659  1.00 37.37 ? 1203 ASP B C     1 
ATOM   17476 O O     . ASP B  1 1205 ? 7.762   59.012  64.776  1.00 36.20 ? 1203 ASP B O     1 
ATOM   17477 C CB    . ASP B  1 1205 ? 4.973   59.023  64.656  1.00 42.04 ? 1203 ASP B CB    1 
ATOM   17478 C CG    . ASP B  1 1205 ? 3.643   58.936  65.411  1.00 45.79 ? 1203 ASP B CG    1 
ATOM   17479 O OD1   . ASP B  1 1205 ? 3.362   59.844  66.218  1.00 43.68 ? 1203 ASP B OD1   1 
ATOM   17480 O OD2   . ASP B  1 1205 ? 2.881   57.962  65.201  1.00 50.07 ? 1203 ASP B OD2   1 
ATOM   17481 N N     . ALA B  1 1206 ? 7.920   61.204  64.255  1.00 35.77 ? 1204 ALA B N     1 
ATOM   17482 C CA    . ALA B  1 1206 ? 9.364   61.145  64.016  1.00 36.21 ? 1204 ALA B CA    1 
ATOM   17483 C C     . ALA B  1 1206 ? 10.111  60.486  65.168  1.00 35.63 ? 1204 ALA B C     1 
ATOM   17484 O O     . ALA B  1 1206 ? 11.016  59.674  64.942  1.00 34.49 ? 1204 ALA B O     1 
ATOM   17485 C CB    . ALA B  1 1206 ? 9.921   62.548  63.779  1.00 36.60 ? 1204 ALA B CB    1 
ATOM   17486 N N     . TYR B  1 1207 ? 9.753   60.821  66.409  1.00 32.29 ? 1205 TYR B N     1 
ATOM   17487 C CA    . TYR B  1 1207 ? 10.314  60.172  67.591  1.00 32.96 ? 1205 TYR B CA    1 
ATOM   17488 C C     . TYR B  1 1207 ? 9.219   59.382  68.298  1.00 28.85 ? 1205 TYR B C     1 
ATOM   17489 O O     . TYR B  1 1207 ? 8.117   59.890  68.511  1.00 34.88 ? 1205 TYR B O     1 
ATOM   17490 C CB    . TYR B  1 1207 ? 10.940  61.182  68.561  1.00 29.20 ? 1205 TYR B CB    1 
ATOM   17491 C CG    . TYR B  1 1207 ? 12.111  61.960  67.991  1.00 28.23 ? 1205 TYR B CG    1 
ATOM   17492 C CD1   . TYR B  1 1207 ? 13.292  61.320  67.629  1.00 29.32 ? 1205 TYR B CD1   1 
ATOM   17493 C CD2   . TYR B  1 1207 ? 12.037  63.337  67.832  1.00 28.35 ? 1205 TYR B CD2   1 
ATOM   17494 C CE1   . TYR B  1 1207 ? 14.361  62.036  67.114  1.00 28.24 ? 1205 TYR B CE1   1 
ATOM   17495 C CE2   . TYR B  1 1207 ? 13.103  64.064  67.306  1.00 28.55 ? 1205 TYR B CE2   1 
ATOM   17496 C CZ    . TYR B  1 1207 ? 14.261  63.412  66.956  1.00 27.79 ? 1205 TYR B CZ    1 
ATOM   17497 O OH    . TYR B  1 1207 ? 15.319  64.131  66.439  1.00 28.77 ? 1205 TYR B OH    1 
ATOM   17498 N N     . CYS B  1 1208 ? 9.530   58.147  68.664  1.00 25.58 ? 1206 CYS B N     1 
ATOM   17499 C CA    . CYS B  1 1208 ? 8.545   57.233  69.225  1.00 26.50 ? 1206 CYS B CA    1 
ATOM   17500 C C     . CYS B  1 1208 ? 8.549   57.314  70.750  1.00 27.75 ? 1206 CYS B C     1 
ATOM   17501 O O     . CYS B  1 1208 ? 9.583   57.081  71.385  1.00 26.50 ? 1206 CYS B O     1 
ATOM   17502 C CB    . CYS B  1 1208 ? 8.843   55.806  68.787  1.00 26.27 ? 1206 CYS B CB    1 
ATOM   17503 S SG    . CYS B  1 1208 ? 7.551   54.686  69.308  1.00 31.29 ? 1206 CYS B SG    1 
ATOM   17504 N N     . LEU B  1 1209 ? 7.385   57.603  71.342  1.00 25.75 ? 1207 LEU B N     1 
ATOM   17505 C CA    . LEU B  1 1209 ? 7.345   57.705  72.798  1.00 24.63 ? 1207 LEU B CA    1 
ATOM   17506 C C     . LEU B  1 1209 ? 7.409   56.346  73.482  1.00 24.11 ? 1207 LEU B C     1 
ATOM   17507 O O     . LEU B  1 1209 ? 7.665   56.299  74.695  1.00 25.15 ? 1207 LEU B O     1 
ATOM   17508 C CB    . LEU B  1 1209 ? 6.090   58.461  73.249  1.00 22.56 ? 1207 LEU B CB    1 
ATOM   17509 C CG    . LEU B  1 1209 ? 5.904   59.873  72.660  1.00 25.22 ? 1207 LEU B CG    1 
ATOM   17510 C CD1   . LEU B  1 1209 ? 4.670   60.569  73.266  1.00 26.44 ? 1207 LEU B CD1   1 
ATOM   17511 C CD2   . LEU B  1 1209 ? 7.142   60.735  72.815  1.00 23.92 ? 1207 LEU B CD2   1 
ATOM   17512 N N     . ASN B  1 1210 ? 7.196   55.246  72.745  1.00 24.07 ? 1208 ASN B N     1 
ATOM   17513 C CA    . ASN B  1 1210 ? 7.304   53.919  73.350  1.00 27.00 ? 1208 ASN B CA    1 
ATOM   17514 C C     . ASN B  1 1210 ? 8.660   53.711  74.019  1.00 28.41 ? 1208 ASN B C     1 
ATOM   17515 O O     . ASN B  1 1210 ? 8.751   53.042  75.057  1.00 25.92 ? 1208 ASN B O     1 
ATOM   17516 C CB    . ASN B  1 1210 ? 7.080   52.827  72.297  1.00 29.40 ? 1208 ASN B CB    1 
ATOM   17517 C CG    . ASN B  1 1210 ? 5.672   52.839  71.706  1.00 30.29 ? 1208 ASN B CG    1 
ATOM   17518 O OD1   . ASN B  1 1210 ? 4.894   53.762  71.931  1.00 33.66 ? 1208 ASN B OD1   1 
ATOM   17519 N ND2   . ASN B  1 1210 ? 5.358   51.814  70.919  1.00 33.33 ? 1208 ASN B ND2   1 
ATOM   17520 N N     . TRP B  1 1211 ? 9.729   54.259  73.431  1.00 24.09 ? 1209 TRP B N     1 
ATOM   17521 C CA    . TRP B  1 1211 ? 11.089  54.006  73.889  1.00 24.81 ? 1209 TRP B CA    1 
ATOM   17522 C C     . TRP B  1 1211 ? 11.570  55.013  74.927  1.00 24.21 ? 1209 TRP B C     1 
ATOM   17523 O O     . TRP B  1 1211 ? 12.695  54.887  75.405  1.00 26.57 ? 1209 TRP B O     1 
ATOM   17524 C CB    . TRP B  1 1211 ? 12.059  53.987  72.684  1.00 26.10 ? 1209 TRP B CB    1 
ATOM   17525 C CG    . TRP B  1 1211 ? 11.469  53.279  71.486  1.00 29.16 ? 1209 TRP B CG    1 
ATOM   17526 C CD1   . TRP B  1 1211 ? 11.354  53.770  70.212  1.00 28.75 ? 1209 TRP B CD1   1 
ATOM   17527 C CD2   . TRP B  1 1211 ? 10.867  51.982  71.469  1.00 24.76 ? 1209 TRP B CD2   1 
ATOM   17528 N NE1   . TRP B  1 1211 ? 10.751  52.847  69.403  1.00 29.03 ? 1209 TRP B NE1   1 
ATOM   17529 C CE2   . TRP B  1 1211 ? 10.432  51.742  70.148  1.00 30.63 ? 1209 TRP B CE2   1 
ATOM   17530 C CE3   . TRP B  1 1211 ? 10.673  50.988  72.442  1.00 27.92 ? 1209 TRP B CE3   1 
ATOM   17531 C CZ2   . TRP B  1 1211 ? 9.793   50.551  69.769  1.00 27.44 ? 1209 TRP B CZ2   1 
ATOM   17532 C CZ3   . TRP B  1 1211 ? 10.038  49.804  72.071  1.00 28.42 ? 1209 TRP B CZ3   1 
ATOM   17533 C CH2   . TRP B  1 1211 ? 9.603   49.600  70.739  1.00 30.32 ? 1209 TRP B CH2   1 
ATOM   17534 N N     . LEU B  1 1212 ? 10.750  56.000  75.291  1.00 24.41 ? 1210 LEU B N     1 
ATOM   17535 C CA    . LEU B  1 1212 ? 11.124  57.026  76.261  1.00 21.03 ? 1210 LEU B CA    1 
ATOM   17536 C C     . LEU B  1 1212 ? 10.513  56.778  77.636  1.00 22.24 ? 1210 LEU B C     1 
ATOM   17537 O O     . LEU B  1 1212 ? 10.650  57.612  78.533  1.00 22.55 ? 1210 LEU B O     1 
ATOM   17538 C CB    . LEU B  1 1212 ? 10.728  58.408  75.725  1.00 22.81 ? 1210 LEU B CB    1 
ATOM   17539 C CG    . LEU B  1 1212 ? 11.596  58.876  74.549  1.00 22.24 ? 1210 LEU B CG    1 
ATOM   17540 C CD1   . LEU B  1 1212 ? 11.015  60.123  73.880  1.00 21.91 ? 1210 LEU B CD1   1 
ATOM   17541 C CD2   . LEU B  1 1212 ? 13.043  59.126  75.024  1.00 21.32 ? 1210 LEU B CD2   1 
ATOM   17542 N N     . VAL B  1 1213 ? 9.850   55.646  77.828  1.00 25.07 ? 1211 VAL B N     1 
ATOM   17543 C CA    . VAL B  1 1213 ? 9.350   55.249  79.135  1.00 24.28 ? 1211 VAL B CA    1 
ATOM   17544 C C     . VAL B  1 1213 ? 10.061  53.967  79.534  1.00 26.44 ? 1211 VAL B C     1 
ATOM   17545 O O     . VAL B  1 1213 ? 10.644  53.270  78.703  1.00 24.08 ? 1211 VAL B O     1 
ATOM   17546 C CB    . VAL B  1 1213 ? 7.821   55.048  79.150  1.00 24.15 ? 1211 VAL B CB    1 
ATOM   17547 C CG1   . VAL B  1 1213 ? 7.111   56.389  79.004  1.00 22.58 ? 1211 VAL B CG1   1 
ATOM   17548 C CG2   . VAL B  1 1213 ? 7.390   54.097  78.033  1.00 24.08 ? 1211 VAL B CG2   1 
ATOM   17549 N N     . GLU B  1 1214 ? 10.010  53.663  80.829  1.00 23.60 ? 1212 GLU B N     1 
ATOM   17550 C CA    . GLU B  1 1214 ? 10.619  52.458  81.382  1.00 28.11 ? 1212 GLU B CA    1 
ATOM   17551 C C     . GLU B  1 1214 ? 9.527   51.518  81.869  1.00 20.43 ? 1212 GLU B C     1 
ATOM   17552 O O     . GLU B  1 1214 ? 8.668   51.918  82.658  1.00 23.08 ? 1212 GLU B O     1 
ATOM   17553 C CB    . GLU B  1 1214 ? 11.551  52.799  82.542  1.00 23.37 ? 1212 GLU B CB    1 
ATOM   17554 C CG    . GLU B  1 1214 ? 12.255  51.591  83.168  1.00 34.42 ? 1212 GLU B CG    1 
ATOM   17555 C CD    . GLU B  1 1214 ? 13.018  51.965  84.440  1.00 39.92 ? 1212 GLU B CD    1 
ATOM   17556 O OE1   . GLU B  1 1214 ? 13.656  53.042  84.461  1.00 44.01 ? 1212 GLU B OE1   1 
ATOM   17557 O OE2   . GLU B  1 1214 ? 12.960  51.195  85.428  1.00 46.76 ? 1212 GLU B OE2   1 
ATOM   17558 N N     . GLU B  1 1215 ? 9.560   50.279  81.390  1.00 17.91 ? 1213 GLU B N     1 
ATOM   17559 C CA    . GLU B  1 1215 ? 8.619   49.259  81.834  1.00 19.40 ? 1213 GLU B CA    1 
ATOM   17560 C C     . GLU B  1 1215 ? 9.067   48.665  83.161  1.00 19.56 ? 1213 GLU B C     1 
ATOM   17561 O O     . GLU B  1 1215 ? 10.245  48.344  83.340  1.00 21.52 ? 1213 GLU B O     1 
ATOM   17562 C CB    . GLU B  1 1215 ? 8.540   48.134  80.803  1.00 24.22 ? 1213 GLU B CB    1 
ATOM   17563 C CG    . GLU B  1 1215 ? 8.157   48.547  79.406  1.00 24.65 ? 1213 GLU B CG    1 
ATOM   17564 C CD    . GLU B  1 1215 ? 8.338   47.387  78.430  1.00 23.59 ? 1213 GLU B CD    1 
ATOM   17565 O OE1   . GLU B  1 1215 ? 9.477   47.170  77.988  1.00 22.19 ? 1213 GLU B OE1   1 
ATOM   17566 O OE2   . GLU B  1 1215 ? 7.357   46.671  78.164  1.00 24.54 ? 1213 GLU B OE2   1 
ATOM   17567 N N     . VAL B  1 1216 ? 8.124   48.470  84.073  1.00 21.09 ? 1214 VAL B N     1 
ATOM   17568 C CA    . VAL B  1 1216 ? 8.409   47.777  85.319  1.00 17.52 ? 1214 VAL B CA    1 
ATOM   17569 C C     . VAL B  1 1216 ? 7.345   46.716  85.550  1.00 20.66 ? 1214 VAL B C     1 
ATOM   17570 O O     . VAL B  1 1216 ? 6.145   47.004  85.474  1.00 22.57 ? 1214 VAL B O     1 
ATOM   17571 C CB    . VAL B  1 1216 ? 8.480   48.745  86.514  1.00 21.65 ? 1214 VAL B CB    1 
ATOM   17572 C CG1   . VAL B  1 1216 ? 8.614   47.959  87.791  1.00 23.69 ? 1214 VAL B CG1   1 
ATOM   17573 C CG2   . VAL B  1 1216 ? 9.671   49.703  86.341  1.00 24.57 ? 1214 VAL B CG2   1 
ATOM   17574 N N     . SER B  1 1217 ? 7.794   45.499  85.841  1.00 19.04 ? 1215 SER B N     1 
ATOM   17575 C CA    . SER B  1 1217 ? 6.947   44.377  86.189  1.00 17.43 ? 1215 SER B CA    1 
ATOM   17576 C C     . SER B  1 1217 ? 7.107   44.083  87.673  1.00 19.12 ? 1215 SER B C     1 
ATOM   17577 O O     . SER B  1 1217 ? 8.224   44.112  88.191  1.00 20.83 ? 1215 SER B O     1 
ATOM   17578 C CB    . SER B  1 1217 ? 7.326   43.146  85.372  1.00 20.65 ? 1215 SER B CB    1 
ATOM   17579 O OG    . SER B  1 1217 ? 6.755   41.974  85.938  1.00 26.06 ? 1215 SER B OG    1 
ATOM   17580 N N     . ALA B  1 1218 ? 5.989   43.828  88.353  1.00 20.47 ? 1216 ALA B N     1 
ATOM   17581 C CA    . ALA B  1 1218 ? 6.030   43.439  89.757  1.00 22.15 ? 1216 ALA B CA    1 
ATOM   17582 C C     . ALA B  1 1218 ? 5.069   42.290  89.984  1.00 20.08 ? 1216 ALA B C     1 
ATOM   17583 O O     . ALA B  1 1218 ? 3.912   42.340  89.556  1.00 23.39 ? 1216 ALA B O     1 
ATOM   17584 C CB    . ALA B  1 1218 ? 5.682   44.610  90.690  1.00 21.52 ? 1216 ALA B CB    1 
ATOM   17585 N N     . SER B  1 1219 ? 5.559   41.253  90.645  1.00 19.31 ? 1217 SER B N     1 
ATOM   17586 C CA    . SER B  1 1219 ? 4.789   40.043  90.876  1.00 19.52 ? 1217 SER B CA    1 
ATOM   17587 C C     . SER B  1 1219 ? 4.718   39.843  92.379  1.00 19.34 ? 1217 SER B C     1 
ATOM   17588 O O     . SER B  1 1219 ? 5.749   39.646  93.019  1.00 20.02 ? 1217 SER B O     1 
ATOM   17589 C CB    . SER B  1 1219 ? 5.441   38.845  90.189  1.00 20.92 ? 1217 SER B CB    1 
ATOM   17590 O OG    . SER B  1 1219 ? 4.723   37.664  90.485  1.00 24.87 ? 1217 SER B OG    1 
ATOM   17591 N N     . ILE B  1 1220 ? 3.514   39.927  92.934  1.00 22.10 ? 1218 ILE B N     1 
ATOM   17592 C CA    . ILE B  1 1220 ? 3.304   39.867  94.377  1.00 23.25 ? 1218 ILE B CA    1 
ATOM   17593 C C     . ILE B  1 1220 ? 2.592   38.562  94.698  1.00 23.30 ? 1218 ILE B C     1 
ATOM   17594 O O     . ILE B  1 1220 ? 1.491   38.314  94.195  1.00 25.41 ? 1218 ILE B O     1 
ATOM   17595 C CB    . ILE B  1 1220 ? 2.478   41.065  94.878  1.00 28.81 ? 1218 ILE B CB    1 
ATOM   17596 C CG1   . ILE B  1 1220 ? 3.187   42.373  94.538  1.00 27.69 ? 1218 ILE B CG1   1 
ATOM   17597 C CG2   . ILE B  1 1220 ? 2.237   40.952  96.381  1.00 25.51 ? 1218 ILE B CG2   1 
ATOM   17598 C CD1   . ILE B  1 1220 ? 2.743   42.976  93.226  1.00 31.21 ? 1218 ILE B CD1   1 
ATOM   17599 N N     . ASN B  1 1221 ? 3.206   37.741  95.549  1.00 22.06 ? 1219 ASN B N     1 
ATOM   17600 C CA    . ASN B  1 1221 ? 2.585   36.511  96.025  1.00 23.12 ? 1219 ASN B CA    1 
ATOM   17601 C C     . ASN B  1 1221 ? 1.547   36.879  97.076  1.00 26.64 ? 1219 ASN B C     1 
ATOM   17602 O O     . ASN B  1 1221 ? 1.907   37.245  98.194  1.00 25.43 ? 1219 ASN B O     1 
ATOM   17603 C CB    . ASN B  1 1221 ? 3.653   35.577  96.597  1.00 22.23 ? 1219 ASN B CB    1 
ATOM   17604 C CG    . ASN B  1 1221 ? 3.070   34.329  97.231  1.00 27.07 ? 1219 ASN B CG    1 
ATOM   17605 O OD1   . ASN B  1 1221 ? 1.869   34.071  97.153  1.00 24.88 ? 1219 ASN B OD1   1 
ATOM   17606 N ND2   . ASN B  1 1221 ? 3.927   33.542  97.868  1.00 28.99 ? 1219 ASN B ND2   1 
ATOM   17607 N N     . THR B  1 1222 ? 0.262   36.763  96.743  1.00 24.05 ? 1220 THR B N     1 
ATOM   17608 C CA    . THR B  1 1222 ? -0.790  37.118  97.688  1.00 26.64 ? 1220 THR B CA    1 
ATOM   17609 C C     . THR B  1 1222 ? -1.329  35.923  98.459  1.00 28.55 ? 1220 THR B C     1 
ATOM   17610 O O     . THR B  1 1222 ? -2.296  36.069  99.217  1.00 30.59 ? 1220 THR B O     1 
ATOM   17611 C CB    . THR B  1 1222 ? -1.933  37.837  96.973  1.00 27.35 ? 1220 THR B CB    1 
ATOM   17612 O OG1   . THR B  1 1222 ? -2.460  36.998  95.934  1.00 27.57 ? 1220 THR B OG1   1 
ATOM   17613 C CG2   . THR B  1 1222 ? -1.424  39.143  96.372  1.00 28.24 ? 1220 THR B CG2   1 
ATOM   17614 N N     . ALA B  1 1223 ? -0.741  34.751  98.279  1.00 30.50 ? 1221 ALA B N     1 
ATOM   17615 C CA    . ALA B  1 1223 ? -1.061  33.617  99.124  1.00 32.19 ? 1221 ALA B CA    1 
ATOM   17616 C C     . ALA B  1 1223 ? -0.115  33.516  100.306 1.00 40.38 ? 1221 ALA B C     1 
ATOM   17617 O O     . ALA B  1 1223 ? -0.369  32.722  101.216 1.00 46.83 ? 1221 ALA B O     1 
ATOM   17618 C CB    . ALA B  1 1223 ? -1.011  32.322  98.313  1.00 31.52 ? 1221 ALA B CB    1 
ATOM   17619 N N     . ALA B  1 1224 ? 0.938   34.333  100.320 1.00 37.51 ? 1222 ALA B N     1 
ATOM   17620 C CA    . ALA B  1 1224 ? 2.094   34.134  101.186 1.00 41.98 ? 1222 ALA B CA    1 
ATOM   17621 C C     . ALA B  1 1224 ? 1.737   34.123  102.669 1.00 44.38 ? 1222 ALA B C     1 
ATOM   17622 O O     . ALA B  1 1224 ? 2.476   33.560  103.480 1.00 41.79 ? 1222 ALA B O     1 
ATOM   17623 C CB    . ALA B  1 1224 ? 3.146   35.212  100.905 1.00 36.80 ? 1222 ALA B CB    1 
HETATM 17624 C C1    . PGE C  2 .    ? 1.840   59.993  97.095  1.00 37.58 ? 1301 PGE A C1    1 
HETATM 17625 O O1    . PGE C  2 .    ? 3.014   60.055  96.293  1.00 46.08 ? 1301 PGE A O1    1 
HETATM 17626 C C2    . PGE C  2 .    ? 1.717   61.301  97.852  1.00 33.31 ? 1301 PGE A C2    1 
HETATM 17627 O O2    . PGE C  2 .    ? 0.755   62.111  97.222  1.00 36.63 ? 1301 PGE A O2    1 
HETATM 17628 C C3    . PGE C  2 .    ? -0.236  62.559  98.127  1.00 30.27 ? 1301 PGE A C3    1 
HETATM 17629 C C4    . PGE C  2 .    ? -1.627  62.404  97.559  1.00 28.91 ? 1301 PGE A C4    1 
HETATM 17630 O O4    . PGE C  2 .    ? -4.191  59.490  94.997  1.00 48.15 ? 1301 PGE A O4    1 
HETATM 17631 C C6    . PGE C  2 .    ? -3.222  59.507  96.042  1.00 36.71 ? 1301 PGE A C6    1 
HETATM 17632 C C5    . PGE C  2 .    ? -3.216  60.872  96.718  1.00 36.00 ? 1301 PGE A C5    1 
HETATM 17633 O O3    . PGE C  2 .    ? -1.981  61.055  97.404  1.00 41.77 ? 1301 PGE A O3    1 
HETATM 17634 C C1    . PEG D  3 .    ? -51.965 77.192  73.859  1.00 37.69 ? 1302 PEG A C1    1 
HETATM 17635 O O1    . PEG D  3 .    ? -52.112 77.546  75.222  1.00 42.83 ? 1302 PEG A O1    1 
HETATM 17636 C C2    . PEG D  3 .    ? -50.738 76.371  73.608  1.00 39.64 ? 1302 PEG A C2    1 
HETATM 17637 O O2    . PEG D  3 .    ? -49.633 77.235  73.389  1.00 44.34 ? 1302 PEG A O2    1 
HETATM 17638 C C3    . PEG D  3 .    ? -48.732 76.753  72.407  1.00 38.28 ? 1302 PEG A C3    1 
HETATM 17639 C C4    . PEG D  3 .    ? -47.419 76.435  73.065  1.00 36.62 ? 1302 PEG A C4    1 
HETATM 17640 O O4    . PEG D  3 .    ? -47.081 77.406  74.042  1.00 37.69 ? 1302 PEG A O4    1 
HETATM 17641 N N1    . PYS E  4 .    ? -15.324 91.647  114.154 1.00 41.98 ? 1303 PYS A N1    1 
HETATM 17642 C C2    . PYS E  4 .    ? -15.150 90.661  115.015 1.00 37.53 ? 1303 PYS A C2    1 
HETATM 17643 C C3    . PYS E  4 .    ? -13.993 90.486  115.769 1.00 35.74 ? 1303 PYS A C3    1 
HETATM 17644 C C4    . PYS E  4 .    ? -12.982 91.410  115.597 1.00 39.37 ? 1303 PYS A C4    1 
HETATM 17645 C C5    . PYS E  4 .    ? -13.146 92.455  114.692 1.00 38.60 ? 1303 PYS A C5    1 
HETATM 17646 C C6    . PYS E  4 .    ? -14.334 92.527  113.997 1.00 39.38 ? 1303 PYS A C6    1 
HETATM 17647 S S2    . PYS E  4 .    ? -16.452 89.492  115.229 1.00 42.93 ? 1303 PYS A S2    1 
HETATM 17648 C C1    . PEG F  3 .    ? -28.097 63.189  90.265  1.00 36.75 ? 1304 PEG A C1    1 
HETATM 17649 O O1    . PEG F  3 .    ? -27.382 61.969  90.058  1.00 26.10 ? 1304 PEG A O1    1 
HETATM 17650 C C2    . PEG F  3 .    ? -28.109 63.613  91.707  1.00 31.35 ? 1304 PEG A C2    1 
HETATM 17651 O O2    . PEG F  3 .    ? -27.260 64.729  91.883  1.00 45.68 ? 1304 PEG A O2    1 
HETATM 17652 C C3    . PEG F  3 .    ? -26.205 64.491  92.811  1.00 36.60 ? 1304 PEG A C3    1 
HETATM 17653 C C4    . PEG F  3 .    ? -24.885 64.503  92.105  1.00 34.03 ? 1304 PEG A C4    1 
HETATM 17654 O O4    . PEG F  3 .    ? -24.005 63.512  92.623  1.00 27.37 ? 1304 PEG A O4    1 
HETATM 17655 C C1    . PEG G  3 .    ? -26.673 70.966  96.909  1.00 36.01 ? 1305 PEG A C1    1 
HETATM 17656 O O1    . PEG G  3 .    ? -27.901 71.091  97.623  1.00 44.10 ? 1305 PEG A O1    1 
HETATM 17657 C C2    . PEG G  3 .    ? -26.250 69.538  96.768  1.00 32.81 ? 1305 PEG A C2    1 
HETATM 17658 O O2    . PEG G  3 .    ? -27.205 68.847  95.962  1.00 40.24 ? 1305 PEG A O2    1 
HETATM 17659 C C3    . PEG G  3 .    ? -26.652 67.747  95.246  1.00 38.05 ? 1305 PEG A C3    1 
HETATM 17660 C C4    . PEG G  3 .    ? -27.623 67.300  94.188  1.00 34.37 ? 1305 PEG A C4    1 
HETATM 17661 O O4    . PEG G  3 .    ? -28.958 67.291  94.666  1.00 43.52 ? 1305 PEG A O4    1 
HETATM 17662 C C1    . PEG H  3 .    ? 4.027   71.802  97.339  1.00 38.96 ? 1306 PEG A C1    1 
HETATM 17663 O O1    . PEG H  3 .    ? 3.096   71.340  96.365  1.00 43.15 ? 1306 PEG A O1    1 
HETATM 17664 C C2    . PEG H  3 .    ? 5.252   70.949  97.390  1.00 35.25 ? 1306 PEG A C2    1 
HETATM 17665 O O2    . PEG H  3 .    ? 6.285   71.550  96.625  1.00 42.46 ? 1306 PEG A O2    1 
HETATM 17666 C C3    . PEG H  3 .    ? 7.409   70.700  96.434  1.00 37.15 ? 1306 PEG A C3    1 
HETATM 17667 C C4    . PEG H  3 .    ? 8.095   71.048  95.147  1.00 41.87 ? 1306 PEG A C4    1 
HETATM 17668 O O4    . PEG H  3 .    ? 8.953   72.178  95.286  1.00 44.66 ? 1306 PEG A O4    1 
HETATM 17669 C C     . FMT I  5 .    ? -40.373 61.431  103.885 0.80 23.15 ? 1307 FMT A C     1 
HETATM 17670 O O1    . FMT I  5 .    ? -39.689 60.959  104.788 0.80 33.26 ? 1307 FMT A O1    1 
HETATM 17671 O O2    . FMT I  5 .    ? -41.534 61.094  103.649 0.80 34.17 ? 1307 FMT A O2    1 
HETATM 17672 C C1    . PEG J  3 .    ? -26.027 53.354  114.666 1.00 41.61 ? 1308 PEG A C1    1 
HETATM 17673 O O1    . PEG J  3 .    ? -26.661 52.103  114.887 1.00 50.13 ? 1308 PEG A O1    1 
HETATM 17674 C C2    . PEG J  3 .    ? -26.759 54.454  115.365 1.00 41.05 ? 1308 PEG A C2    1 
HETATM 17675 O O2    . PEG J  3 .    ? -25.843 55.452  115.784 1.00 45.70 ? 1308 PEG A O2    1 
HETATM 17676 C C3    . PEG J  3 .    ? -24.814 54.950  116.624 1.00 43.08 ? 1308 PEG A C3    1 
HETATM 17677 C C4    . PEG J  3 .    ? -24.188 56.088  117.371 1.00 43.87 ? 1308 PEG A C4    1 
HETATM 17678 O O4    . PEG J  3 .    ? -24.522 56.043  118.751 1.00 49.14 ? 1308 PEG A O4    1 
HETATM 17679 S S     . SO4 K  6 .    ? -9.366  52.860  112.190 1.00 29.43 ? 1309 SO4 A S     1 
HETATM 17680 O O1    . SO4 K  6 .    ? -8.293  53.055  111.247 1.00 29.53 ? 1309 SO4 A O1    1 
HETATM 17681 O O2    . SO4 K  6 .    ? -10.426 52.073  111.581 1.00 31.46 ? 1309 SO4 A O2    1 
HETATM 17682 O O3    . SO4 K  6 .    ? -8.886  52.122  113.368 1.00 27.52 ? 1309 SO4 A O3    1 
HETATM 17683 O O4    . SO4 K  6 .    ? -9.796  54.195  112.560 1.00 28.48 ? 1309 SO4 A O4    1 
HETATM 17684 S S     . SO4 L  6 .    ? -12.575 75.471  71.066  0.77 36.56 ? 1310 SO4 A S     1 
HETATM 17685 O O1    . SO4 L  6 .    ? -11.450 75.930  71.856  0.77 37.79 ? 1310 SO4 A O1    1 
HETATM 17686 O O2    . SO4 L  6 .    ? -12.916 76.515  70.103  0.77 42.33 ? 1310 SO4 A O2    1 
HETATM 17687 O O3    . SO4 L  6 .    ? -12.185 74.236  70.389  0.77 43.83 ? 1310 SO4 A O3    1 
HETATM 17688 O O4    . SO4 L  6 .    ? -13.746 75.228  71.901  0.77 32.44 ? 1310 SO4 A O4    1 
HETATM 17689 S S     . SO4 M  6 .    ? 12.288  75.300  127.363 0.78 44.89 ? 1311 SO4 A S     1 
HETATM 17690 O O1    . SO4 M  6 .    ? 12.962  75.941  126.235 0.78 44.79 ? 1311 SO4 A O1    1 
HETATM 17691 O O2    . SO4 M  6 .    ? 10.916  74.950  127.015 0.78 42.26 ? 1311 SO4 A O2    1 
HETATM 17692 O O3    . SO4 M  6 .    ? 13.022  74.082  127.710 0.78 43.27 ? 1311 SO4 A O3    1 
HETATM 17693 O O4    . SO4 M  6 .    ? 12.259  76.232  128.486 0.78 53.14 ? 1311 SO4 A O4    1 
HETATM 17694 S S     . SO4 N  6 .    ? 29.686  70.981  107.152 0.94 58.19 ? 1312 SO4 A S     1 
HETATM 17695 O O1    . SO4 N  6 .    ? 30.464  70.402  106.059 0.94 60.96 ? 1312 SO4 A O1    1 
HETATM 17696 O O2    . SO4 N  6 .    ? 28.286  71.089  106.764 0.94 56.38 ? 1312 SO4 A O2    1 
HETATM 17697 O O3    . SO4 N  6 .    ? 29.810  70.111  108.318 0.94 57.13 ? 1312 SO4 A O3    1 
HETATM 17698 O O4    . SO4 N  6 .    ? 30.193  72.318  107.456 0.94 60.75 ? 1312 SO4 A O4    1 
HETATM 17699 P PA    . FAD O  7 .    ? -38.001 43.307  83.282  1.00 37.07 ? 1313 FAD A PA    1 
HETATM 17700 O O1A   . FAD O  7 .    ? -36.562 42.721  83.211  1.00 38.22 ? 1313 FAD A O1A   1 
HETATM 17701 O O2A   . FAD O  7 .    ? -39.092 42.415  83.609  1.00 39.97 ? 1313 FAD A O2A   1 
HETATM 17702 O O5B   . FAD O  7 .    ? -38.219 44.367  84.297  1.00 34.90 ? 1313 FAD A O5B   1 
HETATM 17703 C C5B   . FAD O  7 .    ? -37.149 45.255  84.641  1.00 33.91 ? 1313 FAD A C5B   1 
HETATM 17704 C C4B   . FAD O  7 .    ? -37.650 46.355  85.582  1.00 34.68 ? 1313 FAD A C4B   1 
HETATM 17705 O O4B   . FAD O  7 .    ? -37.626 45.961  86.929  1.00 32.05 ? 1313 FAD A O4B   1 
HETATM 17706 C C3B   . FAD O  7 .    ? -36.894 47.652  85.535  1.00 35.57 ? 1313 FAD A C3B   1 
HETATM 17707 O O3B   . FAD O  7 .    ? -37.164 48.484  84.456  1.00 32.62 ? 1313 FAD A O3B   1 
HETATM 17708 C C2B   . FAD O  7 .    ? -37.319 48.281  86.809  1.00 31.28 ? 1313 FAD A C2B   1 
HETATM 17709 O O2B   . FAD O  7 .    ? -38.532 48.941  86.710  1.00 31.65 ? 1313 FAD A O2B   1 
HETATM 17710 C C1B   . FAD O  7 .    ? -37.495 47.116  87.714  1.00 33.51 ? 1313 FAD A C1B   1 
HETATM 17711 N N9A   . FAD O  7 .    ? -36.397 46.889  88.619  1.00 36.04 ? 1313 FAD A N9A   1 
HETATM 17712 C C8A   . FAD O  7 .    ? -35.097 46.573  88.271  1.00 36.93 ? 1313 FAD A C8A   1 
HETATM 17713 N N7A   . FAD O  7 .    ? -34.359 46.414  89.383  1.00 35.51 ? 1313 FAD A N7A   1 
HETATM 17714 C C5A   . FAD O  7 .    ? -35.156 46.618  90.496  1.00 32.67 ? 1313 FAD A C5A   1 
HETATM 17715 C C6A   . FAD O  7 .    ? -34.941 46.585  91.862  1.00 29.73 ? 1313 FAD A C6A   1 
HETATM 17716 N N6A   . FAD O  7 .    ? -33.637 46.265  92.400  1.00 34.47 ? 1313 FAD A N6A   1 
HETATM 17717 N N1A   . FAD O  7 .    ? -35.964 46.832  92.703  1.00 32.17 ? 1313 FAD A N1A   1 
HETATM 17718 C C2A   . FAD O  7 .    ? -37.214 47.112  92.248  1.00 33.11 ? 1313 FAD A C2A   1 
HETATM 17719 N N3A   . FAD O  7 .    ? -37.453 47.158  90.906  1.00 35.87 ? 1313 FAD A N3A   1 
HETATM 17720 C C4A   . FAD O  7 .    ? -36.465 46.926  90.025  1.00 32.65 ? 1313 FAD A C4A   1 
HETATM 17721 N N1    . FAD O  7 .    ? -40.958 53.644  82.137  1.00 29.16 ? 1313 FAD A N1    1 
HETATM 17722 C C2    . FAD O  7 .    ? -41.454 54.778  82.874  1.00 24.62 ? 1313 FAD A C2    1 
HETATM 17723 O O2    . FAD O  7 .    ? -40.967 55.094  84.081  1.00 23.68 ? 1313 FAD A O2    1 
HETATM 17724 N N3    . FAD O  7 .    ? -42.347 55.657  82.315  1.00 27.67 ? 1313 FAD A N3    1 
HETATM 17725 C C4    . FAD O  7 .    ? -42.889 55.405  81.080  1.00 27.62 ? 1313 FAD A C4    1 
HETATM 17726 O O4    . FAD O  7 .    ? -43.782 56.314  80.575  1.00 28.85 ? 1313 FAD A O4    1 
HETATM 17727 C C4X   . FAD O  7 .    ? -42.596 54.116  80.375  1.00 27.98 ? 1313 FAD A C4X   1 
HETATM 17728 N N5    . FAD O  7 .    ? -43.267 53.717  79.219  1.00 32.15 ? 1313 FAD A N5    1 
HETATM 17729 C C5X   . FAD O  7 .    ? -42.970 52.480  78.624  1.00 34.36 ? 1313 FAD A C5X   1 
HETATM 17730 C C6    . FAD O  7 .    ? -43.650 52.074  77.453  1.00 30.60 ? 1313 FAD A C6    1 
HETATM 17731 C C7    . FAD O  7 .    ? -43.341 50.844  76.874  1.00 30.53 ? 1313 FAD A C7    1 
HETATM 17732 C C7M   . FAD O  7 .    ? -44.041 50.369  75.623  1.00 31.70 ? 1313 FAD A C7M   1 
HETATM 17733 C C8    . FAD O  7 .    ? -42.377 50.022  77.423  1.00 31.49 ? 1313 FAD A C8    1 
HETATM 17734 C C8M   . FAD O  7 .    ? -42.073 48.715  76.760  1.00 30.20 ? 1313 FAD A C8M   1 
HETATM 17735 C C9    . FAD O  7 .    ? -41.695 50.406  78.578  1.00 31.49 ? 1313 FAD A C9    1 
HETATM 17736 C C9A   . FAD O  7 .    ? -41.991 51.632  79.178  1.00 32.97 ? 1313 FAD A C9A   1 
HETATM 17737 N N10   . FAD O  7 .    ? -41.298 52.017  80.367  1.00 33.06 ? 1313 FAD A N10   1 
HETATM 17738 C C10   . FAD O  7 .    ? -41.592 53.256  80.970  1.00 29.24 ? 1313 FAD A C10   1 
HETATM 17739 C "C1'" . FAD O  7 .    ? -40.232 51.143  80.934  1.00 37.22 ? 1313 FAD A "C1'" 1 
HETATM 17740 C "C2'" . FAD O  7 .    ? -40.719 50.095  81.906  1.00 35.42 ? 1313 FAD A "C2'" 1 
HETATM 17741 O "O2'" . FAD O  7 .    ? -41.118 50.793  83.009  1.00 37.13 ? 1313 FAD A "O2'" 1 
HETATM 17742 C "C3'" . FAD O  7 .    ? -39.665 49.032  82.326  1.00 33.67 ? 1313 FAD A "C3'" 1 
HETATM 17743 O "O3'" . FAD O  7 .    ? -38.783 49.587  83.226  1.00 41.92 ? 1313 FAD A "O3'" 1 
HETATM 17744 C "C4'" . FAD O  7 .    ? -38.824 48.373  81.239  1.00 37.67 ? 1313 FAD A "C4'" 1 
HETATM 17745 O "O4'" . FAD O  7 .    ? -39.445 48.411  80.012  1.00 44.32 ? 1313 FAD A "O4'" 1 
HETATM 17746 C "C5'" . FAD O  7 .    ? -38.460 46.924  81.588  1.00 36.46 ? 1313 FAD A "C5'" 1 
HETATM 17747 O "O5'" . FAD O  7 .    ? -39.530 46.211  82.190  1.00 38.37 ? 1313 FAD A "O5'" 1 
HETATM 17748 P P     . FAD O  7 .    ? -39.913 44.696  81.769  1.00 35.42 ? 1313 FAD A P     1 
HETATM 17749 O O1P   . FAD O  7 .    ? -41.284 44.097  82.262  1.00 40.37 ? 1313 FAD A O1P   1 
HETATM 17750 O O2P   . FAD O  7 .    ? -39.766 44.848  80.213  1.00 34.42 ? 1313 FAD A O2P   1 
HETATM 17751 O O3P   . FAD O  7 .    ? -38.535 43.869  82.003  1.00 37.33 ? 1313 FAD A O3P   1 
HETATM 17752 C C1    . PGE P  2 .    ? 1.600   60.424  88.503  1.00 38.09 ? 1301 PGE B C1    1 
HETATM 17753 O O1    . PGE P  2 .    ? 0.269   60.030  88.188  1.00 39.11 ? 1301 PGE B O1    1 
HETATM 17754 C C2    . PGE P  2 .    ? 2.508   60.150  87.319  1.00 39.21 ? 1301 PGE B C2    1 
HETATM 17755 O O2    . PGE P  2 .    ? 3.294   59.003  87.577  1.00 36.97 ? 1301 PGE B O2    1 
HETATM 17756 C C3    . PGE P  2 .    ? 3.923   58.496  86.414  1.00 31.48 ? 1301 PGE B C3    1 
HETATM 17757 C C4    . PGE P  2 .    ? 4.454   57.111  86.743  1.00 31.09 ? 1301 PGE B C4    1 
HETATM 17758 O O4    . PGE P  2 .    ? 1.693   54.490  88.874  1.00 39.34 ? 1301 PGE B O4    1 
HETATM 17759 C C6    . PGE P  2 .    ? 2.425   54.177  87.687  1.00 35.22 ? 1301 PGE B C6    1 
HETATM 17760 C C5    . PGE P  2 .    ? 3.679   55.027  87.558  1.00 32.06 ? 1301 PGE B C5    1 
HETATM 17761 O O3    . PGE P  2 .    ? 3.340   56.279  86.991  1.00 33.99 ? 1301 PGE B O3    1 
HETATM 17762 C C1    . PEG Q  3 .    ? 4.737   32.742  93.857  1.00 33.53 ? 1302 PEG B C1    1 
HETATM 17763 O O1    . PEG Q  3 .    ? 3.572   33.566  93.856  1.00 29.60 ? 1302 PEG B O1    1 
HETATM 17764 C C2    . PEG Q  3 .    ? 4.422   31.307  93.543  1.00 36.41 ? 1302 PEG B C2    1 
HETATM 17765 O O2    . PEG Q  3 .    ? 4.571   30.503  94.713  1.00 46.00 ? 1302 PEG B O2    1 
HETATM 17766 C C3    . PEG Q  3 .    ? 3.410   29.749  95.038  1.00 34.83 ? 1302 PEG B C3    1 
HETATM 17767 C C4    . PEG Q  3 .    ? 3.107   29.875  96.504  1.00 34.54 ? 1302 PEG B C4    1 
HETATM 17768 O O4    . PEG Q  3 .    ? 1.879   30.547  96.766  1.00 26.85 ? 1302 PEG B O4    1 
HETATM 17769 N N1    . PYS R  4 .    ? 30.623  37.835  69.552  1.00 33.53 ? 1303 PYS B N1    1 
HETATM 17770 C C2    . PYS R  4 .    ? 29.485  37.934  68.867  1.00 33.59 ? 1303 PYS B C2    1 
HETATM 17771 C C3    . PYS R  4 .    ? 29.166  39.017  68.045  1.00 30.38 ? 1303 PYS B C3    1 
HETATM 17772 C C4    . PYS R  4 .    ? 30.107  40.032  67.955  1.00 34.13 ? 1303 PYS B C4    1 
HETATM 17773 C C5    . PYS R  4 .    ? 31.298  39.944  68.671  1.00 34.98 ? 1303 PYS B C5    1 
HETATM 17774 C C6    . PYS R  4 .    ? 31.510  38.821  69.454  1.00 31.82 ? 1303 PYS B C6    1 
HETATM 17775 S S2    . PYS R  4 .    ? 28.316  36.621  68.997  1.00 39.62 ? 1303 PYS B S2    1 
HETATM 17776 C C1    . PEG S  3 .    ? -5.428  31.323  69.018  1.00 40.06 ? 1304 PEG B C1    1 
HETATM 17777 O O1    . PEG S  3 .    ? -6.271  32.190  68.275  1.00 43.63 ? 1304 PEG B O1    1 
HETATM 17778 C C2    . PEG S  3 .    ? -5.597  31.540  70.491  1.00 34.96 ? 1304 PEG B C2    1 
HETATM 17779 O O2    . PEG S  3 .    ? -6.929  31.202  70.867  1.00 38.56 ? 1304 PEG B O2    1 
HETATM 17780 C C3    . PEG S  3 .    ? -6.987  30.290  71.953  1.00 33.34 ? 1304 PEG B C3    1 
HETATM 17781 C C4    . PEG S  3 .    ? -7.972  30.784  72.967  1.00 34.25 ? 1304 PEG B C4    1 
HETATM 17782 O O4    . PEG S  3 .    ? -9.307  30.588  72.516  1.00 42.76 ? 1304 PEG B O4    1 
HETATM 17783 C C1    . PEG T  3 .    ? 14.819  66.968  54.690  1.00 47.67 ? 1305 PEG B C1    1 
HETATM 17784 O O1    . PEG T  3 .    ? 15.594  66.734  55.864  1.00 46.88 ? 1305 PEG B O1    1 
HETATM 17785 C C2    . PEG T  3 .    ? 13.693  65.988  54.553  1.00 48.76 ? 1305 PEG B C2    1 
HETATM 17786 O O2    . PEG T  3 .    ? 14.195  64.756  54.059  1.00 50.07 ? 1305 PEG B O2    1 
HETATM 17787 C C3    . PEG T  3 .    ? 14.259  63.742  55.048  1.00 46.32 ? 1305 PEG B C3    1 
HETATM 17788 C C4    . PEG T  3 .    ? 15.431  62.848  54.775  1.00 46.23 ? 1305 PEG B C4    1 
HETATM 17789 O O4    . PEG T  3 .    ? 15.488  61.778  55.703  1.00 48.79 ? 1305 PEG B O4    1 
HETATM 17790 C C     . FMT U  5 .    ? 5.113   12.460  78.375  0.76 38.47 ? 1306 FMT B C     1 
HETATM 17791 O O1    . FMT U  5 .    ? 5.751   11.403  78.340  0.76 38.66 ? 1306 FMT B O1    1 
HETATM 17792 O O2    . FMT U  5 .    ? 3.988   12.586  78.871  0.76 40.76 ? 1306 FMT B O2    1 
HETATM 17793 C C     . FMT V  5 .    ? 29.410  65.053  67.924  1.00 48.24 ? 1307 FMT B C     1 
HETATM 17794 O O1    . FMT V  5 .    ? 30.126  64.054  67.871  1.00 53.03 ? 1307 FMT B O1    1 
HETATM 17795 O O2    . FMT V  5 .    ? 29.496  65.902  68.813  1.00 49.63 ? 1307 FMT B O2    1 
HETATM 17796 S S     . SO4 W  6 .    ? -7.225  47.487  74.022  1.00 25.43 ? 1308 SO4 B S     1 
HETATM 17797 O O1    . SO4 W  6 .    ? -6.022  46.745  73.644  1.00 28.15 ? 1308 SO4 B O1    1 
HETATM 17798 O O2    . SO4 W  6 .    ? -7.927  47.894  72.814  1.00 23.43 ? 1308 SO4 B O2    1 
HETATM 17799 O O3    . SO4 W  6 .    ? -8.118  46.637  74.786  1.00 26.64 ? 1308 SO4 B O3    1 
HETATM 17800 O O4    . SO4 W  6 .    ? -6.855  48.633  74.811  1.00 26.37 ? 1308 SO4 B O4    1 
HETATM 17801 S S     . SO4 X  6 .    ? 18.124  45.269  113.641 0.66 36.76 ? 1309 SO4 B S     1 
HETATM 17802 O O1    . SO4 X  6 .    ? 18.874  46.182  112.794 0.66 33.33 ? 1309 SO4 B O1    1 
HETATM 17803 O O2    . SO4 X  6 .    ? 16.886  45.925  114.055 0.66 40.21 ? 1309 SO4 B O2    1 
HETATM 17804 O O3    . SO4 X  6 .    ? 17.800  44.029  112.933 0.66 31.44 ? 1309 SO4 B O3    1 
HETATM 17805 O O4    . SO4 X  6 .    ? 18.935  44.927  114.812 0.66 36.79 ? 1309 SO4 B O4    1 
HETATM 17806 P PA    . FAD Y  7 .    ? -17.218 22.908  105.205 1.00 31.32 ? 1310 FAD B PA    1 
HETATM 17807 O O1A   . FAD Y  7 .    ? -17.463 24.421  105.223 1.00 34.15 ? 1310 FAD B O1A   1 
HETATM 17808 O O2A   . FAD Y  7 .    ? -18.345 22.016  105.012 1.00 35.41 ? 1310 FAD B O2A   1 
HETATM 17809 O O5B   . FAD Y  7 .    ? -16.293 22.408  104.138 1.00 33.46 ? 1310 FAD B O5B   1 
HETATM 17810 C C5B   . FAD Y  7 .    ? -15.275 23.309  103.714 1.00 28.97 ? 1310 FAD B C5B   1 
HETATM 17811 C C4B   . FAD Y  7 .    ? -14.292 22.617  102.766 1.00 29.43 ? 1310 FAD B C4B   1 
HETATM 17812 O O4B   . FAD Y  7 .    ? -14.813 22.557  101.472 1.00 29.98 ? 1310 FAD B O4B   1 
HETATM 17813 C C3B   . FAD Y  7 .    ? -12.968 23.300  102.625 1.00 28.57 ? 1310 FAD B C3B   1 
HETATM 17814 O O3B   . FAD Y  7 .    ? -12.065 23.023  103.641 1.00 27.46 ? 1310 FAD B O3B   1 
HETATM 17815 C C2B   . FAD Y  7 .    ? -12.487 22.711  101.344 1.00 27.23 ? 1310 FAD B C2B   1 
HETATM 17816 O O2B   . FAD Y  7 .    ? -11.976 21.452  101.534 1.00 28.30 ? 1310 FAD B O2B   1 
HETATM 17817 C C1B   . FAD Y  7 .    ? -13.735 22.537  100.573 1.00 30.70 ? 1310 FAD B C1B   1 
HETATM 17818 N N9A   . FAD Y  7 .    ? -13.954 23.576  99.608  1.00 28.98 ? 1310 FAD B N9A   1 
HETATM 17819 C C8A   . FAD Y  7 .    ? -14.126 24.920  99.846  1.00 27.64 ? 1310 FAD B C8A   1 
HETATM 17820 N N7A   . FAD Y  7 .    ? -14.301 25.563  98.680  1.00 28.72 ? 1310 FAD B N7A   1 
HETATM 17821 C C5A   . FAD Y  7 .    ? -14.247 24.652  97.639  1.00 27.46 ? 1310 FAD B C5A   1 
HETATM 17822 C C6A   . FAD Y  7 .    ? -14.380 24.727  96.263  1.00 28.17 ? 1310 FAD B C6A   1 
HETATM 17823 N N6A   . FAD Y  7 .    ? -14.621 25.980  95.615  1.00 23.96 ? 1310 FAD B N6A   1 
HETATM 17824 N N1A   . FAD Y  7 .    ? -14.269 23.617  95.529  1.00 26.21 ? 1310 FAD B N1A   1 
HETATM 17825 C C2A   . FAD Y  7 .    ? -14.065 22.399  96.086  1.00 28.52 ? 1310 FAD B C2A   1 
HETATM 17826 N N3A   . FAD Y  7 .    ? -13.940 22.289  97.434  1.00 29.21 ? 1310 FAD B N3A   1 
HETATM 17827 C C4A   . FAD Y  7 .    ? -14.026 23.375  98.211  1.00 27.73 ? 1310 FAD B C4A   1 
HETATM 17828 N N1    . FAD Y  7 .    ? -7.572  18.339  105.981 1.00 28.39 ? 1310 FAD B N1    1 
HETATM 17829 C C2    . FAD Y  7 .    ? -6.417  17.823  105.322 1.00 23.99 ? 1310 FAD B C2    1 
HETATM 17830 O O2    . FAD Y  7 .    ? -6.169  18.227  104.055 1.00 24.66 ? 1310 FAD B O2    1 
HETATM 17831 N N3    . FAD Y  7 .    ? -5.585  16.939  105.956 1.00 26.09 ? 1310 FAD B N3    1 
HETATM 17832 C C4    . FAD Y  7 .    ? -5.845  16.547  107.257 1.00 25.71 ? 1310 FAD B C4    1 
HETATM 17833 O O4    . FAD Y  7 .    ? -5.020  15.657  107.870 1.00 28.53 ? 1310 FAD B O4    1 
HETATM 17834 C C4X   . FAD Y  7 .    ? -7.055  17.017  107.974 1.00 32.49 ? 1310 FAD B C4X   1 
HETATM 17835 N N5    . FAD Y  7 .    ? -7.379  16.569  109.257 1.00 32.16 ? 1310 FAD B N5    1 
HETATM 17836 C C5X   . FAD Y  7 .    ? -8.550  17.019  109.859 1.00 32.28 ? 1310 FAD B C5X   1 
HETATM 17837 C C6    . FAD Y  7 .    ? -8.896  16.578  111.156 1.00 30.61 ? 1310 FAD B C6    1 
HETATM 17838 C C7    . FAD Y  7 .    ? -10.075 17.049  111.739 1.00 33.46 ? 1310 FAD B C7    1 
HETATM 17839 C C7M   . FAD Y  7 .    ? -10.487 16.605  113.118 1.00 36.32 ? 1310 FAD B C7M   1 
HETATM 17840 C C8    . FAD Y  7 .    ? -10.906 17.920  111.074 1.00 35.64 ? 1310 FAD B C8    1 
HETATM 17841 C C8M   . FAD Y  7 .    ? -12.177 18.403  111.721 1.00 33.59 ? 1310 FAD B C8M   1 
HETATM 17842 C C9    . FAD Y  7 .    ? -10.574 18.348  109.788 1.00 33.40 ? 1310 FAD B C9    1 
HETATM 17843 C C9A   . FAD Y  7 .    ? -9.402  17.905  109.190 1.00 32.03 ? 1310 FAD B C9A   1 
HETATM 17844 N N10   . FAD Y  7 .    ? -9.084  18.370  107.871 1.00 34.85 ? 1310 FAD B N10   1 
HETATM 17845 C C10   . FAD Y  7 .    ? -7.911  17.918  107.253 1.00 28.83 ? 1310 FAD B C10   1 
HETATM 17846 C "C1'" . FAD Y  7 .    ? -10.028 19.250  107.136 1.00 29.28 ? 1310 FAD B "C1'" 1 
HETATM 17847 C "C2'" . FAD Y  7 .    ? -9.681  20.707  107.039 1.00 35.58 ? 1310 FAD B "C2'" 1 
HETATM 17848 O "O2'" . FAD Y  7 .    ? -8.728  21.007  107.987 1.00 35.25 ? 1310 FAD B "O2'" 1 
HETATM 17849 C "C3'" . FAD Y  7 .    ? -10.991 21.487  107.253 1.00 33.11 ? 1310 FAD B "C3'" 1 
HETATM 17850 O "O3'" . FAD Y  7 .    ? -11.318 21.451  108.594 1.00 35.64 ? 1310 FAD B "O3'" 1 
HETATM 17851 C "C4'" . FAD Y  7 .    ? -12.188 20.958  106.474 1.00 34.79 ? 1310 FAD B "C4'" 1 
HETATM 17852 O "O4'" . FAD Y  7 .    ? -11.982 21.029  105.106 1.00 31.68 ? 1310 FAD B "O4'" 1 
HETATM 17853 C "C5'" . FAD Y  7 .    ? -13.453 21.726  106.844 1.00 30.55 ? 1310 FAD B "C5'" 1 
HETATM 17854 O "O5'" . FAD Y  7 .    ? -14.532 21.107  106.177 1.00 31.97 ? 1310 FAD B "O5'" 1 
HETATM 17855 P P     . FAD Y  7 .    ? -15.993 20.931  106.825 1.00 33.09 ? 1310 FAD B P     1 
HETATM 17856 O O1P   . FAD Y  7 .    ? -16.763 19.589  106.504 1.00 39.41 ? 1310 FAD B O1P   1 
HETATM 17857 O O2P   . FAD Y  7 .    ? -15.646 21.262  108.329 1.00 33.63 ? 1310 FAD B O2P   1 
HETATM 17858 O O3P   . FAD Y  7 .    ? -16.683 22.352  106.495 1.00 33.55 ? 1310 FAD B O3P   1 
HETATM 17859 O O     . HOH Z  8 .    ? -30.546 49.959  105.457 1.00 35.77 ? 1401 HOH A O     1 
HETATM 17860 O O     . HOH Z  8 .    ? -21.499 73.998  105.241 1.00 46.30 ? 1402 HOH A O     1 
HETATM 17861 O O     . HOH Z  8 .    ? -12.987 59.033  123.702 1.00 38.60 ? 1403 HOH A O     1 
HETATM 17862 O O     . HOH Z  8 .    ? -27.904 69.776  75.039  1.00 41.20 ? 1404 HOH A O     1 
HETATM 17863 O O     . HOH Z  8 .    ? -0.729  63.568  111.014 1.00 31.67 ? 1405 HOH A O     1 
HETATM 17864 O O     . HOH Z  8 .    ? -57.762 67.261  62.474  1.00 34.39 ? 1406 HOH A O     1 
HETATM 17865 O O     . HOH Z  8 .    ? -14.008 54.922  113.117 1.00 37.77 ? 1407 HOH A O     1 
HETATM 17866 O O     . HOH Z  8 .    ? -52.883 61.034  102.763 1.00 28.94 ? 1408 HOH A O     1 
HETATM 17867 O O     . HOH Z  8 .    ? -24.141 72.712  73.095  1.00 43.32 ? 1409 HOH A O     1 
HETATM 17868 O O     . HOH Z  8 .    ? -5.207  70.445  77.391  1.00 42.68 ? 1410 HOH A O     1 
HETATM 17869 O O     . HOH Z  8 .    ? -27.984 55.770  91.503  1.00 35.66 ? 1411 HOH A O     1 
HETATM 17870 O O     . HOH Z  8 .    ? -29.206 57.388  116.577 1.00 37.95 ? 1412 HOH A O     1 
HETATM 17871 O O     . HOH Z  8 .    ? -32.320 79.869  100.723 1.00 30.99 ? 1413 HOH A O     1 
HETATM 17872 O O     . HOH Z  8 .    ? -15.047 64.059  100.230 1.00 28.64 ? 1414 HOH A O     1 
HETATM 17873 O O     . HOH Z  8 .    ? -43.659 80.432  90.969  1.00 37.15 ? 1415 HOH A O     1 
HETATM 17874 O O     . HOH Z  8 .    ? -16.942 55.590  113.509 1.00 39.93 ? 1416 HOH A O     1 
HETATM 17875 O O     . HOH Z  8 .    ? -2.430  74.347  100.764 1.00 38.63 ? 1417 HOH A O     1 
HETATM 17876 O O     . HOH Z  8 .    ? -7.228  80.781  129.090 1.00 37.29 ? 1418 HOH A O     1 
HETATM 17877 O O     . HOH Z  8 .    ? -38.483 62.182  106.536 1.00 33.21 ? 1419 HOH A O     1 
HETATM 17878 O O     . HOH Z  8 .    ? -14.269 74.810  106.770 1.00 27.58 ? 1420 HOH A O     1 
HETATM 17879 O O     . HOH Z  8 .    ? 17.375  78.125  121.629 1.00 40.50 ? 1421 HOH A O     1 
HETATM 17880 O O     . HOH Z  8 .    ? -30.472 99.067  99.692  1.00 41.37 ? 1422 HOH A O     1 
HETATM 17881 O O     . HOH Z  8 .    ? -23.381 63.712  98.970  1.00 27.74 ? 1423 HOH A O     1 
HETATM 17882 O O     . HOH Z  8 .    ? -55.322 56.393  65.547  1.00 26.90 ? 1424 HOH A O     1 
HETATM 17883 O O     . HOH Z  8 .    ? -58.656 49.286  96.384  1.00 46.99 ? 1425 HOH A O     1 
HETATM 17884 O O     . HOH Z  8 .    ? -48.335 72.174  114.311 1.00 41.29 ? 1426 HOH A O     1 
HETATM 17885 O O     . HOH Z  8 .    ? -5.933  53.397  111.934 1.00 23.92 ? 1427 HOH A O     1 
HETATM 17886 O O     . HOH Z  8 .    ? -41.656 86.100  115.154 1.00 37.79 ? 1428 HOH A O     1 
HETATM 17887 O O     . HOH Z  8 .    ? -6.840  58.433  121.218 1.00 32.98 ? 1429 HOH A O     1 
HETATM 17888 O O     . HOH Z  8 .    ? -7.410  42.622  62.786  1.00 34.09 ? 1430 HOH A O     1 
HETATM 17889 O O     . HOH Z  8 .    ? -62.152 56.826  64.594  1.00 35.01 ? 1431 HOH A O     1 
HETATM 17890 O O     . HOH Z  8 .    ? -59.838 54.105  75.667  1.00 27.19 ? 1432 HOH A O     1 
HETATM 17891 O O     . HOH Z  8 .    ? -39.105 64.921  97.303  1.00 35.67 ? 1433 HOH A O     1 
HETATM 17892 O O     . HOH Z  8 .    ? 16.580  57.784  104.029 1.00 28.39 ? 1434 HOH A O     1 
HETATM 17893 O O     . HOH Z  8 .    ? -38.030 69.380  125.023 1.00 46.50 ? 1435 HOH A O     1 
HETATM 17894 O O     . HOH Z  8 .    ? -7.146  50.431  77.538  1.00 29.57 ? 1436 HOH A O     1 
HETATM 17895 O O     . HOH Z  8 .    ? -25.533 58.271  119.293 1.00 40.99 ? 1437 HOH A O     1 
HETATM 17896 O O     . HOH Z  8 .    ? 6.547   80.948  97.930  1.00 41.89 ? 1438 HOH A O     1 
HETATM 17897 O O     . HOH Z  8 .    ? -32.664 75.817  96.102  1.00 41.29 ? 1439 HOH A O     1 
HETATM 17898 O O     . HOH Z  8 .    ? -0.577  65.902  95.705  1.00 34.37 ? 1440 HOH A O     1 
HETATM 17899 O O     . HOH Z  8 .    ? -43.245 77.680  68.845  1.00 33.38 ? 1441 HOH A O     1 
HETATM 17900 O O     . HOH Z  8 .    ? -13.389 55.529  82.513  1.00 38.37 ? 1442 HOH A O     1 
HETATM 17901 O O     . HOH Z  8 .    ? -26.640 49.956  97.534  1.00 33.49 ? 1443 HOH A O     1 
HETATM 17902 O O     . HOH Z  8 .    ? 19.287  82.049  114.667 1.00 36.21 ? 1444 HOH A O     1 
HETATM 17903 O O     . HOH Z  8 .    ? 20.194  58.369  112.555 1.00 39.51 ? 1445 HOH A O     1 
HETATM 17904 O O     . HOH Z  8 .    ? -20.247 59.191  77.129  1.00 28.07 ? 1446 HOH A O     1 
HETATM 17905 O O     . HOH Z  8 .    ? -55.628 33.200  72.220  1.00 45.87 ? 1447 HOH A O     1 
HETATM 17906 O O     . HOH Z  8 .    ? 6.797   53.909  102.636 1.00 21.62 ? 1448 HOH A O     1 
HETATM 17907 O O     . HOH Z  8 .    ? 1.491   72.849  117.113 1.00 35.57 ? 1449 HOH A O     1 
HETATM 17908 O O     . HOH Z  8 .    ? -12.191 77.251  104.122 1.00 30.37 ? 1450 HOH A O     1 
HETATM 17909 O O     . HOH Z  8 .    ? -10.826 63.023  73.497  1.00 32.58 ? 1451 HOH A O     1 
HETATM 17910 O O     . HOH Z  8 .    ? -66.041 58.599  76.648  1.00 27.47 ? 1452 HOH A O     1 
HETATM 17911 O O     . HOH Z  8 .    ? -39.840 78.618  101.446 1.00 32.60 ? 1453 HOH A O     1 
HETATM 17912 O O     . HOH Z  8 .    ? -9.396  64.929  77.299  1.00 28.71 ? 1454 HOH A O     1 
HETATM 17913 O O     . HOH Z  8 .    ? -25.111 88.971  100.775 1.00 31.66 ? 1455 HOH A O     1 
HETATM 17914 O O     . HOH Z  8 .    ? -21.612 47.060  58.736  1.00 39.79 ? 1456 HOH A O     1 
HETATM 17915 O O     . HOH Z  8 .    ? -60.881 59.415  91.361  1.00 26.54 ? 1457 HOH A O     1 
HETATM 17916 O O     . HOH Z  8 .    ? -11.943 73.018  129.668 1.00 35.16 ? 1458 HOH A O     1 
HETATM 17917 O O     . HOH Z  8 .    ? -48.267 57.516  87.044  1.00 22.68 ? 1459 HOH A O     1 
HETATM 17918 O O     . HOH Z  8 .    ? -38.747 49.414  103.507 1.00 38.06 ? 1460 HOH A O     1 
HETATM 17919 O O     . HOH Z  8 .    ? -34.148 90.787  123.723 1.00 38.69 ? 1461 HOH A O     1 
HETATM 17920 O O     . HOH Z  8 .    ? 3.737   72.651  86.991  1.00 38.01 ? 1462 HOH A O     1 
HETATM 17921 O O     . HOH Z  8 .    ? -18.178 39.188  68.809  1.00 41.31 ? 1463 HOH A O     1 
HETATM 17922 O O     . HOH Z  8 .    ? 8.922   74.361  93.915  1.00 38.78 ? 1464 HOH A O     1 
HETATM 17923 O O     . HOH Z  8 .    ? 7.562   91.301  115.239 1.00 34.84 ? 1465 HOH A O     1 
HETATM 17924 O O     . HOH Z  8 .    ? -20.589 91.167  98.239  1.00 42.00 ? 1466 HOH A O     1 
HETATM 17925 O O     . HOH Z  8 .    ? -52.568 78.250  88.648  1.00 34.99 ? 1467 HOH A O     1 
HETATM 17926 O O     . HOH Z  8 .    ? -55.645 75.162  75.663  1.00 31.66 ? 1468 HOH A O     1 
HETATM 17927 O O     . HOH Z  8 .    ? -19.224 70.200  88.723  1.00 30.03 ? 1469 HOH A O     1 
HETATM 17928 O O     . HOH Z  8 .    ? -38.540 37.892  88.824  1.00 42.49 ? 1470 HOH A O     1 
HETATM 17929 O O     . HOH Z  8 .    ? -10.675 69.300  134.855 1.00 39.40 ? 1471 HOH A O     1 
HETATM 17930 O O     . HOH Z  8 .    ? -40.062 57.168  88.916  1.00 22.98 ? 1472 HOH A O     1 
HETATM 17931 O O     . HOH Z  8 .    ? -52.274 47.076  69.538  1.00 37.64 ? 1473 HOH A O     1 
HETATM 17932 O O     . HOH Z  8 .    ? -46.856 66.332  95.040  1.00 27.98 ? 1474 HOH A O     1 
HETATM 17933 O O     . HOH Z  8 .    ? -6.537  54.733  106.340 1.00 33.48 ? 1475 HOH A O     1 
HETATM 17934 O O     . HOH Z  8 .    ? -25.053 65.106  95.629  1.00 33.39 ? 1476 HOH A O     1 
HETATM 17935 O O     . HOH Z  8 .    ? -26.264 50.691  106.288 1.00 38.63 ? 1477 HOH A O     1 
HETATM 17936 O O     . HOH Z  8 .    ? -39.318 78.300  98.676  1.00 33.43 ? 1478 HOH A O     1 
HETATM 17937 O O     . HOH Z  8 .    ? -24.581 92.727  128.379 1.00 42.06 ? 1479 HOH A O     1 
HETATM 17938 O O     . HOH Z  8 .    ? -5.302  54.359  109.345 1.00 26.38 ? 1480 HOH A O     1 
HETATM 17939 O O     . HOH Z  8 .    ? 21.145  57.245  106.593 1.00 40.61 ? 1481 HOH A O     1 
HETATM 17940 O O     . HOH Z  8 .    ? -20.628 47.552  55.586  1.00 42.29 ? 1482 HOH A O     1 
HETATM 17941 O O     . HOH Z  8 .    ? -15.090 56.584  85.873  1.00 42.87 ? 1483 HOH A O     1 
HETATM 17942 O O     . HOH Z  8 .    ? -37.357 63.649  68.286  1.00 39.27 ? 1484 HOH A O     1 
HETATM 17943 O O     . HOH Z  8 .    ? -34.651 70.001  77.196  1.00 41.72 ? 1485 HOH A O     1 
HETATM 17944 O O     . HOH Z  8 .    ? -51.676 55.134  76.669  1.00 24.83 ? 1486 HOH A O     1 
HETATM 17945 O O     . HOH Z  8 .    ? -11.826 68.533  77.511  1.00 34.10 ? 1487 HOH A O     1 
HETATM 17946 O O     . HOH Z  8 .    ? -47.234 48.672  94.008  1.00 27.46 ? 1488 HOH A O     1 
HETATM 17947 O O     . HOH Z  8 .    ? 13.630  81.979  115.701 1.00 30.08 ? 1489 HOH A O     1 
HETATM 17948 O O     . HOH Z  8 .    ? -4.322  69.672  107.747 1.00 31.85 ? 1490 HOH A O     1 
HETATM 17949 O O     . HOH Z  8 .    ? -15.061 48.729  52.295  1.00 44.27 ? 1491 HOH A O     1 
HETATM 17950 O O     . HOH Z  8 .    ? -14.566 75.927  110.950 1.00 23.17 ? 1492 HOH A O     1 
HETATM 17951 O O     . HOH Z  8 .    ? -49.628 66.655  94.940  1.00 31.16 ? 1493 HOH A O     1 
HETATM 17952 O O     . HOH Z  8 .    ? -29.287 54.834  113.004 1.00 38.74 ? 1494 HOH A O     1 
HETATM 17953 O O     . HOH Z  8 .    ? -1.807  80.098  98.440  1.00 40.61 ? 1495 HOH A O     1 
HETATM 17954 O O     . HOH Z  8 .    ? 17.182  69.106  119.321 1.00 35.38 ? 1496 HOH A O     1 
HETATM 17955 O O     . HOH Z  8 .    ? -2.379  53.572  105.836 1.00 30.47 ? 1497 HOH A O     1 
HETATM 17956 O O     . HOH Z  8 .    ? -69.145 56.385  83.655  1.00 32.09 ? 1498 HOH A O     1 
HETATM 17957 O O     . HOH Z  8 .    ? -59.618 51.697  66.688  1.00 25.81 ? 1499 HOH A O     1 
HETATM 17958 O O     . HOH Z  8 .    ? -35.642 66.198  95.852  1.00 46.88 ? 1500 HOH A O     1 
HETATM 17959 O O     . HOH Z  8 .    ? -51.177 51.797  64.734  1.00 29.01 ? 1501 HOH A O     1 
HETATM 17960 O O     . HOH Z  8 .    ? -62.033 36.255  79.241  1.00 44.93 ? 1502 HOH A O     1 
HETATM 17961 O O     . HOH Z  8 .    ? -3.066  93.370  122.403 1.00 49.96 ? 1503 HOH A O     1 
HETATM 17962 O O     . HOH Z  8 .    ? -50.093 48.830  100.742 1.00 33.66 ? 1504 HOH A O     1 
HETATM 17963 O O     . HOH Z  8 .    ? -23.056 97.349  79.693  1.00 42.27 ? 1505 HOH A O     1 
HETATM 17964 O O     . HOH Z  8 .    ? -43.782 75.529  115.168 1.00 38.73 ? 1506 HOH A O     1 
HETATM 17965 O O     . HOH Z  8 .    ? -19.997 54.854  108.198 1.00 31.59 ? 1507 HOH A O     1 
HETATM 17966 O O     . HOH Z  8 .    ? -52.462 48.776  63.429  1.00 38.30 ? 1508 HOH A O     1 
HETATM 17967 O O     . HOH Z  8 .    ? -3.690  70.463  118.775 1.00 31.30 ? 1509 HOH A O     1 
HETATM 17968 O O     . HOH Z  8 .    ? -14.496 61.300  109.047 1.00 29.66 ? 1510 HOH A O     1 
HETATM 17969 O O     . HOH Z  8 .    ? -44.757 73.758  76.086  1.00 31.38 ? 1511 HOH A O     1 
HETATM 17970 O O     . HOH Z  8 .    ? -4.027  54.823  62.466  1.00 38.32 ? 1512 HOH A O     1 
HETATM 17971 O O     . HOH Z  8 .    ? -23.303 60.468  116.996 1.00 27.19 ? 1513 HOH A O     1 
HETATM 17972 O O     . HOH Z  8 .    ? -9.758  87.407  89.129  1.00 45.22 ? 1514 HOH A O     1 
HETATM 17973 O O     . HOH Z  8 .    ? 25.563  79.761  109.176 1.00 42.21 ? 1515 HOH A O     1 
HETATM 17974 O O     . HOH Z  8 .    ? -19.114 61.468  86.268  1.00 30.11 ? 1516 HOH A O     1 
HETATM 17975 O O     . HOH Z  8 .    ? -17.489 91.786  112.657 1.00 45.24 ? 1517 HOH A O     1 
HETATM 17976 O O     . HOH Z  8 .    ? -35.768 76.316  93.514  1.00 35.71 ? 1518 HOH A O     1 
HETATM 17977 O O     . HOH Z  8 .    ? -48.471 66.001  58.594  1.00 36.75 ? 1519 HOH A O     1 
HETATM 17978 O O     . HOH Z  8 .    ? -56.578 34.412  87.562  1.00 40.28 ? 1520 HOH A O     1 
HETATM 17979 O O     . HOH Z  8 .    ? -26.071 61.805  76.975  1.00 43.44 ? 1521 HOH A O     1 
HETATM 17980 O O     . HOH Z  8 .    ? -10.890 49.496  111.257 1.00 27.05 ? 1522 HOH A O     1 
HETATM 17981 O O     . HOH Z  8 .    ? -23.144 58.859  76.662  1.00 33.23 ? 1523 HOH A O     1 
HETATM 17982 O O     . HOH Z  8 .    ? -45.251 63.426  85.176  1.00 27.86 ? 1524 HOH A O     1 
HETATM 17983 O O     . HOH Z  8 .    ? -41.158 48.771  64.714  1.00 34.53 ? 1525 HOH A O     1 
HETATM 17984 O O     . HOH Z  8 .    ? -38.325 40.550  72.338  1.00 39.92 ? 1526 HOH A O     1 
HETATM 17985 O O     . HOH Z  8 .    ? -29.135 75.370  103.070 1.00 32.34 ? 1527 HOH A O     1 
HETATM 17986 O O     . HOH Z  8 .    ? -11.741 63.200  114.390 1.00 27.80 ? 1528 HOH A O     1 
HETATM 17987 O O     . HOH Z  8 .    ? -44.893 63.166  82.245  1.00 24.79 ? 1529 HOH A O     1 
HETATM 17988 O O     . HOH Z  8 .    ? -19.640 72.806  98.575  1.00 23.95 ? 1530 HOH A O     1 
HETATM 17989 O O     . HOH Z  8 .    ? -50.975 50.482  58.112  1.00 39.82 ? 1531 HOH A O     1 
HETATM 17990 O O     . HOH Z  8 .    ? -51.093 69.771  101.313 1.00 26.39 ? 1532 HOH A O     1 
HETATM 17991 O O     . HOH Z  8 .    ? -27.367 53.691  110.865 1.00 35.82 ? 1533 HOH A O     1 
HETATM 17992 O O     . HOH Z  8 .    ? -5.972  64.980  115.325 1.00 29.30 ? 1534 HOH A O     1 
HETATM 17993 O O     . HOH Z  8 .    ? -56.346 55.593  96.045  1.00 27.96 ? 1535 HOH A O     1 
HETATM 17994 O O     . HOH Z  8 .    ? -32.034 82.510  76.309  1.00 27.08 ? 1536 HOH A O     1 
HETATM 17995 O O     . HOH Z  8 .    ? -50.248 68.484  93.035  1.00 32.38 ? 1537 HOH A O     1 
HETATM 17996 O O     . HOH Z  8 .    ? -34.709 76.945  97.435  1.00 39.20 ? 1538 HOH A O     1 
HETATM 17997 O O     . HOH Z  8 .    ? -57.693 64.644  92.044  1.00 37.92 ? 1539 HOH A O     1 
HETATM 17998 O O     . HOH Z  8 .    ? -39.404 76.629  94.192  1.00 31.16 ? 1540 HOH A O     1 
HETATM 17999 O O     . HOH Z  8 .    ? -36.898 63.401  96.882  1.00 34.34 ? 1541 HOH A O     1 
HETATM 18000 O O     . HOH Z  8 .    ? -47.834 48.944  96.933  1.00 24.96 ? 1542 HOH A O     1 
HETATM 18001 O O     . HOH Z  8 .    ? 0.313   85.397  104.107 1.00 31.21 ? 1543 HOH A O     1 
HETATM 18002 O O     . HOH Z  8 .    ? -32.284 86.827  77.498  1.00 39.82 ? 1544 HOH A O     1 
HETATM 18003 O O     . HOH Z  8 .    ? -46.692 54.027  90.542  1.00 25.38 ? 1545 HOH A O     1 
HETATM 18004 O O     . HOH Z  8 .    ? -51.521 64.712  95.735  1.00 29.92 ? 1546 HOH A O     1 
HETATM 18005 O O     . HOH Z  8 .    ? -43.233 48.101  60.698  1.00 36.66 ? 1547 HOH A O     1 
HETATM 18006 O O     . HOH Z  8 .    ? -20.803 54.773  91.969  1.00 41.98 ? 1548 HOH A O     1 
HETATM 18007 O O     . HOH Z  8 .    ? -13.103 87.498  99.983  1.00 46.52 ? 1549 HOH A O     1 
HETATM 18008 O O     . HOH Z  8 .    ? -60.585 61.220  93.634  1.00 28.39 ? 1550 HOH A O     1 
HETATM 18009 O O     . HOH Z  8 .    ? -31.438 71.608  83.812  1.00 32.32 ? 1551 HOH A O     1 
HETATM 18010 O O     . HOH Z  8 .    ? -17.581 87.024  93.540  1.00 35.99 ? 1552 HOH A O     1 
HETATM 18011 O O     . HOH Z  8 .    ? -14.353 64.534  52.010  1.00 43.11 ? 1553 HOH A O     1 
HETATM 18012 O O     . HOH Z  8 .    ? -34.650 82.645  119.950 1.00 30.78 ? 1554 HOH A O     1 
HETATM 18013 O O     . HOH Z  8 .    ? -14.996 48.790  76.816  1.00 34.77 ? 1555 HOH A O     1 
HETATM 18014 O O     . HOH Z  8 .    ? -20.904 84.891  70.968  1.00 44.12 ? 1556 HOH A O     1 
HETATM 18015 O O     . HOH Z  8 .    ? -5.478  67.994  79.050  1.00 39.68 ? 1557 HOH A O     1 
HETATM 18016 O O     . HOH Z  8 .    ? -46.985 59.656  103.063 1.00 29.89 ? 1558 HOH A O     1 
HETATM 18017 O O     . HOH Z  8 .    ? -41.808 71.385  65.135  1.00 33.15 ? 1559 HOH A O     1 
HETATM 18018 O O     . HOH Z  8 .    ? -22.982 67.434  98.609  1.00 29.15 ? 1560 HOH A O     1 
HETATM 18019 O O     . HOH Z  8 .    ? -61.970 70.154  83.990  1.00 27.26 ? 1561 HOH A O     1 
HETATM 18020 O O     . HOH Z  8 .    ? -60.080 60.606  76.733  1.00 24.24 ? 1562 HOH A O     1 
HETATM 18021 O O     . HOH Z  8 .    ? -41.142 90.924  99.808  1.00 39.85 ? 1563 HOH A O     1 
HETATM 18022 O O     . HOH Z  8 .    ? -6.370  82.580  104.564 1.00 31.89 ? 1564 HOH A O     1 
HETATM 18023 O O     . HOH Z  8 .    ? -26.567 56.400  109.068 1.00 28.54 ? 1565 HOH A O     1 
HETATM 18024 O O     . HOH Z  8 .    ? -4.690  60.013  126.513 1.00 40.03 ? 1566 HOH A O     1 
HETATM 18025 O O     . HOH Z  8 .    ? -18.248 57.333  98.261  1.00 26.27 ? 1567 HOH A O     1 
HETATM 18026 O O     . HOH Z  8 .    ? -25.737 62.567  111.083 1.00 27.93 ? 1568 HOH A O     1 
HETATM 18027 O O     . HOH Z  8 .    ? -25.234 88.428  80.036  1.00 30.36 ? 1569 HOH A O     1 
HETATM 18028 O O     . HOH Z  8 .    ? -32.149 84.140  100.534 1.00 29.12 ? 1570 HOH A O     1 
HETATM 18029 O O     . HOH Z  8 .    ? -40.178 85.911  124.521 1.00 47.58 ? 1571 HOH A O     1 
HETATM 18030 O O     . HOH Z  8 .    ? -24.073 101.472 85.476  1.00 43.80 ? 1572 HOH A O     1 
HETATM 18031 O O     . HOH Z  8 .    ? -46.933 80.892  94.571  1.00 41.48 ? 1573 HOH A O     1 
HETATM 18032 O O     . HOH Z  8 .    ? -20.824 73.284  69.518  1.00 45.09 ? 1574 HOH A O     1 
HETATM 18033 O O     . HOH Z  8 .    ? -32.799 60.581  74.321  1.00 45.07 ? 1575 HOH A O     1 
HETATM 18034 O O     . HOH Z  8 .    ? -30.971 91.120  108.278 1.00 31.33 ? 1576 HOH A O     1 
HETATM 18035 O O     . HOH Z  8 .    ? -59.048 37.879  77.399  1.00 40.01 ? 1577 HOH A O     1 
HETATM 18036 O O     . HOH Z  8 .    ? 18.239  58.961  96.909  1.00 40.90 ? 1578 HOH A O     1 
HETATM 18037 O O     . HOH Z  8 .    ? -20.184 78.866  71.257  1.00 28.70 ? 1579 HOH A O     1 
HETATM 18038 O O     . HOH Z  8 .    ? -62.463 61.703  68.835  1.00 32.01 ? 1580 HOH A O     1 
HETATM 18039 O O     . HOH Z  8 .    ? -23.609 54.253  102.445 1.00 29.97 ? 1581 HOH A O     1 
HETATM 18040 O O     . HOH Z  8 .    ? -37.312 80.592  79.950  1.00 25.84 ? 1582 HOH A O     1 
HETATM 18041 O O     . HOH Z  8 .    ? -59.165 33.753  73.469  1.00 48.38 ? 1583 HOH A O     1 
HETATM 18042 O O     . HOH Z  8 .    ? 7.948   89.569  121.795 1.00 33.13 ? 1584 HOH A O     1 
HETATM 18043 O O     . HOH Z  8 .    ? -53.224 63.589  99.299  1.00 30.45 ? 1585 HOH A O     1 
HETATM 18044 O O     . HOH Z  8 .    ? -0.344  84.965  108.184 1.00 33.20 ? 1586 HOH A O     1 
HETATM 18045 O O     . HOH Z  8 .    ? 0.026   79.996  82.785  1.00 40.57 ? 1587 HOH A O     1 
HETATM 18046 O O     . HOH Z  8 .    ? -2.866  55.875  101.005 1.00 35.42 ? 1588 HOH A O     1 
HETATM 18047 O O     . HOH Z  8 .    ? 9.226   56.884  98.798  1.00 31.53 ? 1589 HOH A O     1 
HETATM 18048 O O     . HOH Z  8 .    ? -46.863 67.232  60.439  1.00 30.83 ? 1590 HOH A O     1 
HETATM 18049 O O     . HOH Z  8 .    ? -25.952 94.211  79.339  1.00 36.52 ? 1591 HOH A O     1 
HETATM 18050 O O     . HOH Z  8 .    ? -27.759 72.978  130.849 1.00 38.45 ? 1592 HOH A O     1 
HETATM 18051 O O     . HOH Z  8 .    ? -57.105 45.725  72.031  1.00 30.81 ? 1593 HOH A O     1 
HETATM 18052 O O     . HOH Z  8 .    ? -27.109 80.770  135.358 1.00 46.74 ? 1594 HOH A O     1 
HETATM 18053 O O     . HOH Z  8 .    ? -32.687 59.698  110.834 1.00 35.95 ? 1595 HOH A O     1 
HETATM 18054 O O     . HOH Z  8 .    ? -42.058 79.851  81.008  1.00 36.88 ? 1596 HOH A O     1 
HETATM 18055 O O     . HOH Z  8 .    ? -28.811 61.844  118.011 1.00 27.84 ? 1597 HOH A O     1 
HETATM 18056 O O     . HOH Z  8 .    ? -58.390 57.475  63.800  1.00 27.86 ? 1598 HOH A O     1 
HETATM 18057 O O     . HOH Z  8 .    ? -6.203  76.120  112.303 1.00 24.19 ? 1599 HOH A O     1 
HETATM 18058 O O     . HOH Z  8 .    ? -67.758 59.940  70.702  1.00 34.68 ? 1600 HOH A O     1 
HETATM 18059 O O     . HOH Z  8 .    ? -7.121  70.490  95.011  1.00 31.32 ? 1601 HOH A O     1 
HETATM 18060 O O     . HOH Z  8 .    ? -1.592  76.909  89.009  1.00 36.78 ? 1602 HOH A O     1 
HETATM 18061 O O     . HOH Z  8 .    ? -48.706 54.262  62.065  1.00 32.56 ? 1603 HOH A O     1 
HETATM 18062 O O     . HOH Z  8 .    ? -0.709  77.332  118.435 1.00 35.56 ? 1604 HOH A O     1 
HETATM 18063 O O     . HOH Z  8 .    ? 12.143  75.444  96.258  1.00 38.43 ? 1605 HOH A O     1 
HETATM 18064 O O     . HOH Z  8 .    ? -32.559 79.348  97.274  1.00 28.75 ? 1606 HOH A O     1 
HETATM 18065 O O     . HOH Z  8 .    ? -32.558 82.368  98.812  1.00 28.05 ? 1607 HOH A O     1 
HETATM 18066 O O     . HOH Z  8 .    ? 13.309  86.599  122.401 1.00 39.52 ? 1608 HOH A O     1 
HETATM 18067 O O     . HOH Z  8 .    ? 1.797   85.806  119.455 1.00 35.04 ? 1609 HOH A O     1 
HETATM 18068 O O     . HOH Z  8 .    ? -57.959 57.650  102.089 1.00 35.13 ? 1610 HOH A O     1 
HETATM 18069 O O     . HOH Z  8 .    ? 6.339   90.677  108.202 1.00 37.23 ? 1611 HOH A O     1 
HETATM 18070 O O     . HOH Z  8 .    ? -51.415 69.865  94.917  1.00 34.99 ? 1612 HOH A O     1 
HETATM 18071 O O     . HOH Z  8 .    ? -19.101 59.174  105.380 1.00 28.88 ? 1613 HOH A O     1 
HETATM 18072 O O     . HOH Z  8 .    ? -1.372  78.191  115.882 1.00 35.48 ? 1614 HOH A O     1 
HETATM 18073 O O     . HOH Z  8 .    ? -9.668  56.030  83.586  1.00 36.23 ? 1615 HOH A O     1 
HETATM 18074 O O     . HOH Z  8 .    ? -26.135 70.129  132.616 1.00 44.68 ? 1616 HOH A O     1 
HETATM 18075 O O     . HOH Z  8 .    ? -8.959  60.053  108.358 1.00 29.60 ? 1617 HOH A O     1 
HETATM 18076 O O     . HOH Z  8 .    ? -1.912  77.754  122.445 1.00 34.91 ? 1618 HOH A O     1 
HETATM 18077 O O     . HOH Z  8 .    ? -62.140 57.922  70.927  1.00 26.62 ? 1619 HOH A O     1 
HETATM 18078 O O     . HOH Z  8 .    ? -16.602 60.328  107.514 1.00 35.73 ? 1620 HOH A O     1 
HETATM 18079 O O     . HOH Z  8 .    ? -30.853 95.936  106.122 1.00 35.12 ? 1621 HOH A O     1 
HETATM 18080 O O     . HOH Z  8 .    ? -12.289 79.295  95.652  1.00 26.45 ? 1622 HOH A O     1 
HETATM 18081 O O     . HOH Z  8 .    ? 12.580  73.924  92.870  1.00 39.92 ? 1623 HOH A O     1 
HETATM 18082 O O     . HOH Z  8 .    ? -46.017 65.097  92.813  1.00 26.54 ? 1624 HOH A O     1 
HETATM 18083 O O     . HOH Z  8 .    ? -32.463 75.051  127.701 1.00 34.70 ? 1625 HOH A O     1 
HETATM 18084 O O     . HOH Z  8 .    ? -24.285 83.284  113.344 1.00 26.65 ? 1626 HOH A O     1 
HETATM 18085 O O     . HOH Z  8 .    ? -10.347 81.181  92.303  1.00 30.38 ? 1627 HOH A O     1 
HETATM 18086 O O     . HOH Z  8 .    ? -15.583 43.883  77.697  1.00 40.59 ? 1628 HOH A O     1 
HETATM 18087 O O     . HOH Z  8 .    ? -53.970 42.885  65.998  1.00 38.94 ? 1629 HOH A O     1 
HETATM 18088 O O     . HOH Z  8 .    ? 10.959  67.213  118.277 1.00 34.96 ? 1630 HOH A O     1 
HETATM 18089 O O     . HOH Z  8 .    ? -48.954 78.482  75.705  1.00 35.15 ? 1631 HOH A O     1 
HETATM 18090 O O     . HOH Z  8 .    ? -7.369  62.379  108.259 1.00 26.77 ? 1632 HOH A O     1 
HETATM 18091 O O     . HOH Z  8 .    ? -44.125 88.529  117.023 1.00 52.56 ? 1633 HOH A O     1 
HETATM 18092 O O     . HOH Z  8 .    ? -6.968  41.816  67.051  1.00 32.33 ? 1634 HOH A O     1 
HETATM 18093 O O     . HOH Z  8 .    ? -10.890 67.811  109.206 1.00 24.30 ? 1635 HOH A O     1 
HETATM 18094 O O     . HOH Z  8 .    ? -38.629 61.378  92.891  1.00 24.54 ? 1636 HOH A O     1 
HETATM 18095 O O     . HOH Z  8 .    ? -47.158 82.244  102.624 1.00 34.96 ? 1637 HOH A O     1 
HETATM 18096 O O     . HOH Z  8 .    ? 3.841   57.660  106.143 1.00 25.39 ? 1638 HOH A O     1 
HETATM 18097 O O     . HOH Z  8 .    ? -42.217 67.736  92.158  1.00 26.14 ? 1639 HOH A O     1 
HETATM 18098 O O     . HOH Z  8 .    ? -52.761 53.830  101.181 1.00 31.03 ? 1640 HOH A O     1 
HETATM 18099 O O     . HOH Z  8 .    ? -3.810  57.412  73.704  1.00 30.55 ? 1641 HOH A O     1 
HETATM 18100 O O     . HOH Z  8 .    ? -27.650 82.487  130.962 1.00 36.71 ? 1642 HOH A O     1 
HETATM 18101 O O     . HOH Z  8 .    ? -48.169 64.082  97.840  1.00 29.83 ? 1643 HOH A O     1 
HETATM 18102 O O     . HOH Z  8 .    ? -35.765 73.339  84.537  1.00 29.96 ? 1644 HOH A O     1 
HETATM 18103 O O     . HOH Z  8 .    ? -54.862 47.198  68.280  1.00 33.45 ? 1645 HOH A O     1 
HETATM 18104 O O     . HOH Z  8 .    ? -8.436  59.780  95.268  1.00 40.14 ? 1646 HOH A O     1 
HETATM 18105 O O     . HOH Z  8 .    ? -41.817 27.378  71.269  1.00 48.85 ? 1647 HOH A O     1 
HETATM 18106 O O     . HOH Z  8 .    ? -32.623 64.828  123.385 1.00 34.07 ? 1648 HOH A O     1 
HETATM 18107 O O     . HOH Z  8 .    ? -49.732 78.120  78.402  1.00 33.97 ? 1649 HOH A O     1 
HETATM 18108 O O     . HOH Z  8 .    ? -20.304 66.062  82.104  1.00 31.58 ? 1650 HOH A O     1 
HETATM 18109 O O     . HOH Z  8 .    ? -54.112 55.257  69.332  1.00 26.53 ? 1651 HOH A O     1 
HETATM 18110 O O     . HOH Z  8 .    ? -28.406 77.797  102.567 1.00 34.13 ? 1652 HOH A O     1 
HETATM 18111 O O     . HOH Z  8 .    ? -46.159 76.045  95.457  1.00 34.08 ? 1653 HOH A O     1 
HETATM 18112 O O     . HOH Z  8 .    ? -23.799 63.812  107.238 1.00 24.71 ? 1654 HOH A O     1 
HETATM 18113 O O     . HOH Z  8 .    ? -28.450 62.019  103.285 1.00 25.19 ? 1655 HOH A O     1 
HETATM 18114 O O     . HOH Z  8 .    ? -41.632 71.603  115.529 1.00 35.59 ? 1656 HOH A O     1 
HETATM 18115 O O     . HOH Z  8 .    ? -34.098 83.864  124.676 1.00 36.51 ? 1657 HOH A O     1 
HETATM 18116 O O     . HOH Z  8 .    ? -24.504 59.621  122.911 1.00 42.45 ? 1658 HOH A O     1 
HETATM 18117 O O     . HOH Z  8 .    ? 10.645  57.062  107.206 1.00 29.64 ? 1659 HOH A O     1 
HETATM 18118 O O     . HOH Z  8 .    ? -31.406 91.388  81.590  1.00 31.74 ? 1660 HOH A O     1 
HETATM 18119 O O     . HOH Z  8 .    ? -54.040 68.551  94.255  1.00 38.38 ? 1661 HOH A O     1 
HETATM 18120 O O     . HOH Z  8 .    ? -34.805 75.725  84.102  1.00 34.53 ? 1662 HOH A O     1 
HETATM 18121 O O     . HOH Z  8 .    ? -30.684 86.546  103.272 1.00 28.44 ? 1663 HOH A O     1 
HETATM 18122 O O     . HOH Z  8 .    ? -45.586 62.505  93.584  1.00 25.12 ? 1664 HOH A O     1 
HETATM 18123 O O     . HOH Z  8 .    ? -60.573 46.947  89.440  1.00 29.67 ? 1665 HOH A O     1 
HETATM 18124 O O     . HOH Z  8 .    ? 0.924   74.744  108.554 1.00 33.06 ? 1666 HOH A O     1 
HETATM 18125 O O     . HOH Z  8 .    ? -28.826 56.708  60.782  1.00 44.17 ? 1667 HOH A O     1 
HETATM 18126 O O     . HOH Z  8 .    ? -20.503 86.962  113.992 1.00 34.62 ? 1668 HOH A O     1 
HETATM 18127 O O     . HOH Z  8 .    ? 16.155  65.102  121.448 1.00 38.81 ? 1669 HOH A O     1 
HETATM 18128 O O     . HOH Z  8 .    ? 5.091   66.905  97.350  1.00 31.28 ? 1670 HOH A O     1 
HETATM 18129 O O     . HOH Z  8 .    ? -36.827 58.855  95.289  1.00 25.73 ? 1671 HOH A O     1 
HETATM 18130 O O     . HOH Z  8 .    ? -19.089 59.685  70.777  1.00 27.36 ? 1672 HOH A O     1 
HETATM 18131 O O     . HOH Z  8 .    ? -47.526 60.125  86.069  1.00 22.28 ? 1673 HOH A O     1 
HETATM 18132 O O     . HOH Z  8 .    ? -44.489 41.209  105.234 1.00 40.12 ? 1674 HOH A O     1 
HETATM 18133 O O     . HOH Z  8 .    ? -8.704  52.913  106.217 1.00 43.28 ? 1675 HOH A O     1 
HETATM 18134 O O     . HOH Z  8 .    ? -42.835 78.078  76.765  1.00 31.15 ? 1676 HOH A O     1 
HETATM 18135 O O     . HOH Z  8 .    ? -68.085 63.870  86.104  1.00 36.99 ? 1677 HOH A O     1 
HETATM 18136 O O     . HOH Z  8 .    ? -3.309  89.859  110.386 1.00 37.27 ? 1678 HOH A O     1 
HETATM 18137 O O     . HOH Z  8 .    ? -52.699 61.841  95.731  1.00 27.26 ? 1679 HOH A O     1 
HETATM 18138 O O     . HOH Z  8 .    ? -18.412 54.692  87.965  1.00 47.78 ? 1680 HOH A O     1 
HETATM 18139 O O     . HOH Z  8 .    ? -1.508  79.243  101.301 1.00 33.06 ? 1681 HOH A O     1 
HETATM 18140 O O     . HOH Z  8 .    ? 16.997  80.448  98.168  1.00 37.04 ? 1682 HOH A O     1 
HETATM 18141 O O     . HOH Z  8 .    ? -44.420 55.524  95.921  1.00 23.29 ? 1683 HOH A O     1 
HETATM 18142 O O     . HOH Z  8 .    ? -34.804 66.596  102.767 1.00 28.60 ? 1684 HOH A O     1 
HETATM 18143 O O     . HOH Z  8 .    ? -26.182 63.593  105.689 1.00 28.96 ? 1685 HOH A O     1 
HETATM 18144 O O     . HOH Z  8 .    ? -27.112 51.853  99.845  1.00 30.98 ? 1686 HOH A O     1 
HETATM 18145 O O     . HOH Z  8 .    ? 15.779  61.430  117.640 1.00 42.87 ? 1687 HOH A O     1 
HETATM 18146 O O     . HOH Z  8 .    ? -21.163 57.984  98.269  1.00 28.67 ? 1688 HOH A O     1 
HETATM 18147 O O     . HOH Z  8 .    ? -46.124 78.256  97.103  1.00 24.72 ? 1689 HOH A O     1 
HETATM 18148 O O     . HOH Z  8 .    ? -20.177 52.369  79.224  1.00 33.37 ? 1690 HOH A O     1 
HETATM 18149 O O     . HOH Z  8 .    ? -35.718 51.691  86.276  1.00 22.90 ? 1691 HOH A O     1 
HETATM 18150 O O     . HOH Z  8 .    ? -27.855 70.914  91.014  1.00 28.59 ? 1692 HOH A O     1 
HETATM 18151 O O     . HOH Z  8 .    ? -4.351  72.999  118.117 1.00 33.85 ? 1693 HOH A O     1 
HETATM 18152 O O     . HOH Z  8 .    ? -52.190 73.061  106.595 1.00 39.51 ? 1694 HOH A O     1 
HETATM 18153 O O     . HOH Z  8 .    ? -4.123  79.272  105.084 1.00 32.28 ? 1695 HOH A O     1 
HETATM 18154 O O     . HOH Z  8 .    ? -11.282 92.225  126.035 1.00 41.22 ? 1696 HOH A O     1 
HETATM 18155 O O     . HOH Z  8 .    ? -65.825 71.444  81.157  1.00 32.08 ? 1697 HOH A O     1 
HETATM 18156 O O     . HOH Z  8 .    ? -26.591 80.275  102.878 1.00 38.95 ? 1698 HOH A O     1 
HETATM 18157 O O     . HOH Z  8 .    ? 8.193   67.913  116.169 1.00 38.05 ? 1699 HOH A O     1 
HETATM 18158 O O     . HOH Z  8 .    ? 13.221  56.835  117.766 1.00 49.26 ? 1700 HOH A O     1 
HETATM 18159 O O     . HOH Z  8 .    ? -38.654 50.282  99.339  1.00 33.72 ? 1701 HOH A O     1 
HETATM 18160 O O     . HOH Z  8 .    ? 10.116  81.365  126.798 1.00 35.59 ? 1702 HOH A O     1 
HETATM 18161 O O     . HOH Z  8 .    ? -42.979 61.244  101.264 1.00 30.99 ? 1703 HOH A O     1 
HETATM 18162 O O     . HOH Z  8 .    ? -9.716  63.775  97.265  1.00 25.20 ? 1704 HOH A O     1 
HETATM 18163 O O     . HOH Z  8 .    ? 6.604   60.935  104.528 1.00 27.13 ? 1705 HOH A O     1 
HETATM 18164 O O     . HOH Z  8 .    ? -24.279 67.649  106.233 1.00 30.00 ? 1706 HOH A O     1 
HETATM 18165 O O     . HOH Z  8 .    ? 5.666   62.904  98.472  1.00 26.76 ? 1707 HOH A O     1 
HETATM 18166 O O     . HOH Z  8 .    ? -43.469 85.390  98.308  1.00 39.46 ? 1708 HOH A O     1 
HETATM 18167 O O     . HOH Z  8 .    ? -65.876 64.552  82.191  1.00 28.73 ? 1709 HOH A O     1 
HETATM 18168 O O     . HOH Z  8 .    ? -32.081 89.301  109.936 1.00 32.45 ? 1710 HOH A O     1 
HETATM 18169 O O     . HOH Z  8 .    ? -44.648 31.061  84.786  1.00 40.24 ? 1711 HOH A O     1 
HETATM 18170 O O     . HOH Z  8 .    ? -40.632 64.509  63.111  1.00 35.76 ? 1712 HOH A O     1 
HETATM 18171 O O     . HOH Z  8 .    ? -18.494 60.967  67.792  1.00 34.37 ? 1713 HOH A O     1 
HETATM 18172 O O     . HOH Z  8 .    ? -7.553  50.735  53.939  1.00 38.88 ? 1714 HOH A O     1 
HETATM 18173 O O     . HOH Z  8 .    ? -8.663  80.804  75.923  1.00 33.30 ? 1715 HOH A O     1 
HETATM 18174 O O     . HOH Z  8 .    ? -66.610 61.509  76.641  1.00 24.97 ? 1716 HOH A O     1 
HETATM 18175 O O     . HOH Z  8 .    ? -35.225 95.192  97.465  1.00 32.77 ? 1717 HOH A O     1 
HETATM 18176 O O     . HOH Z  8 .    ? -21.391 56.618  54.222  1.00 42.63 ? 1718 HOH A O     1 
HETATM 18177 O O     . HOH Z  8 .    ? -15.073 67.186  73.987  1.00 32.11 ? 1719 HOH A O     1 
HETATM 18178 O O     . HOH Z  8 .    ? -16.803 76.682  109.784 1.00 29.80 ? 1720 HOH A O     1 
HETATM 18179 O O     . HOH Z  8 .    ? -0.235  52.745  63.834  1.00 32.81 ? 1721 HOH A O     1 
HETATM 18180 O O     . HOH Z  8 .    ? -4.172  78.279  123.742 1.00 29.70 ? 1722 HOH A O     1 
HETATM 18181 O O     . HOH Z  8 .    ? -30.537 81.206  124.420 1.00 34.81 ? 1723 HOH A O     1 
HETATM 18182 O O     . HOH Z  8 .    ? -29.118 76.774  73.635  1.00 32.09 ? 1724 HOH A O     1 
HETATM 18183 O O     . HOH Z  8 .    ? -26.634 82.712  114.161 1.00 29.33 ? 1725 HOH A O     1 
HETATM 18184 O O     . HOH Z  8 .    ? -31.930 59.944  106.736 1.00 31.01 ? 1726 HOH A O     1 
HETATM 18185 O O     . HOH Z  8 .    ? -3.513  57.516  69.061  1.00 39.34 ? 1727 HOH A O     1 
HETATM 18186 O O     . HOH Z  8 .    ? -48.131 59.020  83.680  1.00 23.77 ? 1728 HOH A O     1 
HETATM 18187 O O     . HOH Z  8 .    ? -61.318 68.491  69.314  1.00 31.15 ? 1729 HOH A O     1 
HETATM 18188 O O     . HOH Z  8 .    ? -4.422  73.077  77.971  1.00 35.30 ? 1730 HOH A O     1 
HETATM 18189 O O     . HOH Z  8 .    ? -12.878 65.962  113.900 1.00 24.83 ? 1731 HOH A O     1 
HETATM 18190 O O     . HOH Z  8 .    ? -18.612 79.584  128.445 1.00 33.07 ? 1732 HOH A O     1 
HETATM 18191 O O     . HOH Z  8 .    ? -32.521 61.503  112.670 1.00 28.78 ? 1733 HOH A O     1 
HETATM 18192 O O     . HOH Z  8 .    ? -37.227 68.326  84.161  1.00 38.63 ? 1734 HOH A O     1 
HETATM 18193 O O     . HOH Z  8 .    ? -13.522 94.513  85.410  1.00 50.46 ? 1735 HOH A O     1 
HETATM 18194 O O     . HOH Z  8 .    ? -46.506 55.786  88.267  1.00 21.79 ? 1736 HOH A O     1 
HETATM 18195 O O     . HOH Z  8 .    ? 2.364   64.663  114.209 1.00 35.43 ? 1737 HOH A O     1 
HETATM 18196 O O     . HOH Z  8 .    ? -18.067 82.813  97.574  1.00 34.06 ? 1738 HOH A O     1 
HETATM 18197 O O     . HOH Z  8 .    ? -27.133 62.797  87.406  1.00 29.31 ? 1739 HOH A O     1 
HETATM 18198 O O     . HOH Z  8 .    ? -36.968 82.962  122.288 1.00 33.93 ? 1740 HOH A O     1 
HETATM 18199 O O     . HOH Z  8 .    ? -57.539 60.032  61.813  1.00 28.88 ? 1741 HOH A O     1 
HETATM 18200 O O     . HOH Z  8 .    ? -3.082  85.679  126.160 1.00 40.41 ? 1742 HOH A O     1 
HETATM 18201 O O     . HOH Z  8 .    ? -17.889 72.817  112.278 1.00 27.18 ? 1743 HOH A O     1 
HETATM 18202 O O     . HOH Z  8 .    ? -3.016  62.387  78.507  1.00 27.09 ? 1744 HOH A O     1 
HETATM 18203 O O     . HOH Z  8 .    ? -33.508 78.299  75.036  1.00 31.04 ? 1745 HOH A O     1 
HETATM 18204 O O     . HOH Z  8 .    ? -61.584 52.577  91.822  1.00 32.59 ? 1746 HOH A O     1 
HETATM 18205 O O     . HOH Z  8 .    ? 25.705  64.186  104.319 1.00 36.01 ? 1747 HOH A O     1 
HETATM 18206 O O     . HOH Z  8 .    ? -2.450  85.282  114.939 1.00 29.44 ? 1748 HOH A O     1 
HETATM 18207 O O     . HOH Z  8 .    ? -22.094 90.429  113.019 1.00 42.33 ? 1749 HOH A O     1 
HETATM 18208 O O     . HOH Z  8 .    ? -20.304 86.852  92.574  1.00 31.56 ? 1750 HOH A O     1 
HETATM 18209 O O     . HOH Z  8 .    ? -28.150 71.440  100.387 1.00 42.58 ? 1751 HOH A O     1 
HETATM 18210 O O     . HOH Z  8 .    ? -42.141 88.853  97.870  1.00 36.40 ? 1752 HOH A O     1 
HETATM 18211 O O     . HOH Z  8 .    ? -50.180 75.881  102.426 1.00 34.22 ? 1753 HOH A O     1 
HETATM 18212 O O     . HOH Z  8 .    ? -41.903 23.748  81.924  1.00 52.32 ? 1754 HOH A O     1 
HETATM 18213 O O     . HOH Z  8 .    ? -0.794  67.220  91.106  1.00 41.22 ? 1755 HOH A O     1 
HETATM 18214 O O     . HOH Z  8 .    ? -39.594 27.196  87.218  1.00 47.91 ? 1756 HOH A O     1 
HETATM 18215 O O     . HOH Z  8 .    ? -25.228 79.448  96.053  1.00 27.08 ? 1757 HOH A O     1 
HETATM 18216 O O     . HOH Z  8 .    ? -16.437 95.696  91.250  1.00 45.98 ? 1758 HOH A O     1 
HETATM 18217 O O     . HOH Z  8 .    ? -42.396 56.664  90.344  1.00 22.79 ? 1759 HOH A O     1 
HETATM 18218 O O     . HOH Z  8 .    ? -11.758 59.889  85.629  1.00 32.76 ? 1760 HOH A O     1 
HETATM 18219 O O     . HOH Z  8 .    ? -33.822 70.281  101.462 1.00 36.06 ? 1761 HOH A O     1 
HETATM 18220 O O     . HOH Z  8 .    ? -32.004 88.539  96.347  1.00 30.93 ? 1762 HOH A O     1 
HETATM 18221 O O     . HOH Z  8 .    ? 15.224  83.091  112.777 1.00 33.61 ? 1763 HOH A O     1 
HETATM 18222 O O     . HOH Z  8 .    ? -20.221 78.984  116.152 1.00 28.03 ? 1764 HOH A O     1 
HETATM 18223 O O     . HOH Z  8 .    ? -21.090 81.562  117.289 1.00 27.03 ? 1765 HOH A O     1 
HETATM 18224 O O     . HOH Z  8 .    ? -16.040 68.118  97.803  1.00 22.90 ? 1766 HOH A O     1 
HETATM 18225 O O     . HOH Z  8 .    ? 14.006  78.207  122.675 1.00 35.64 ? 1767 HOH A O     1 
HETATM 18226 O O     . HOH Z  8 .    ? -64.189 52.668  90.807  1.00 38.52 ? 1768 HOH A O     1 
HETATM 18227 O O     . HOH Z  8 .    ? 9.724   68.052  95.314  1.00 40.72 ? 1769 HOH A O     1 
HETATM 18228 O O     . HOH Z  8 .    ? -25.020 69.473  104.220 1.00 38.66 ? 1770 HOH A O     1 
HETATM 18229 O O     . HOH Z  8 .    ? 1.224   66.297  97.774  1.00 24.11 ? 1771 HOH A O     1 
HETATM 18230 O O     . HOH Z  8 .    ? -1.135  83.934  119.329 1.00 31.92 ? 1772 HOH A O     1 
HETATM 18231 O O     . HOH Z  8 .    ? -49.072 28.970  74.695  1.00 46.05 ? 1773 HOH A O     1 
HETATM 18232 O O     . HOH Z  8 .    ? -27.631 58.895  77.205  1.00 46.09 ? 1774 HOH A O     1 
HETATM 18233 O O     . HOH Z  8 .    ? -29.020 95.101  90.085  1.00 33.42 ? 1775 HOH A O     1 
HETATM 18234 O O     . HOH Z  8 .    ? -13.853 78.034  112.291 1.00 23.67 ? 1776 HOH A O     1 
HETATM 18235 O O     . HOH Z  8 .    ? -8.781  65.077  115.109 1.00 27.83 ? 1777 HOH A O     1 
HETATM 18236 O O     . HOH Z  8 .    ? 1.039   62.113  112.326 1.00 35.62 ? 1778 HOH A O     1 
HETATM 18237 O O     . HOH Z  8 .    ? -50.495 56.782  72.613  1.00 30.67 ? 1779 HOH A O     1 
HETATM 18238 O O     . HOH Z  8 .    ? -5.250  55.661  102.337 1.00 35.99 ? 1780 HOH A O     1 
HETATM 18239 O O     . HOH Z  8 .    ? -30.446 72.954  99.795  1.00 40.51 ? 1781 HOH A O     1 
HETATM 18240 O O     . HOH Z  8 .    ? -39.950 61.552  95.513  1.00 28.64 ? 1782 HOH A O     1 
HETATM 18241 O O     . HOH Z  8 .    ? -38.784 70.566  82.768  1.00 29.19 ? 1783 HOH A O     1 
HETATM 18242 O O     . HOH Z  8 .    ? -20.975 71.003  76.577  1.00 31.55 ? 1784 HOH A O     1 
HETATM 18243 O O     . HOH Z  8 .    ? -46.530 30.184  86.602  1.00 40.13 ? 1785 HOH A O     1 
HETATM 18244 O O     . HOH Z  8 .    ? -28.359 61.018  85.478  1.00 41.07 ? 1786 HOH A O     1 
HETATM 18245 O O     . HOH Z  8 .    ? -45.054 60.932  86.446  1.00 25.82 ? 1787 HOH A O     1 
HETATM 18246 O O     . HOH Z  8 .    ? -39.513 86.319  90.258  1.00 33.32 ? 1788 HOH A O     1 
HETATM 18247 O O     . HOH Z  8 .    ? -12.239 81.013  68.999  1.00 53.09 ? 1789 HOH A O     1 
HETATM 18248 O O     . HOH Z  8 .    ? -15.173 59.045  127.796 1.00 33.63 ? 1790 HOH A O     1 
HETATM 18249 O O     . HOH Z  8 .    ? -31.218 84.007  124.753 1.00 28.30 ? 1791 HOH A O     1 
HETATM 18250 O O     . HOH Z  8 .    ? -55.329 26.220  92.900  1.00 46.97 ? 1792 HOH A O     1 
HETATM 18251 O O     . HOH Z  8 .    ? -50.327 72.245  102.210 1.00 33.13 ? 1793 HOH A O     1 
HETATM 18252 O O     . HOH Z  8 .    ? -39.017 60.959  75.682  1.00 47.67 ? 1794 HOH A O     1 
HETATM 18253 O O     . HOH Z  8 .    ? -25.656 88.844  117.592 1.00 32.96 ? 1795 HOH A O     1 
HETATM 18254 O O     . HOH Z  8 .    ? 25.104  77.332  110.700 1.00 42.73 ? 1796 HOH A O     1 
HETATM 18255 O O     . HOH Z  8 .    ? 12.939  88.637  117.739 1.00 32.50 ? 1797 HOH A O     1 
HETATM 18256 O O     . HOH Z  8 .    ? -57.055 73.436  97.269  1.00 40.92 ? 1798 HOH A O     1 
HETATM 18257 O O     . HOH Z  8 .    ? 2.499   84.079  102.912 1.00 30.73 ? 1799 HOH A O     1 
HETATM 18258 O O     . HOH Z  8 .    ? -0.580  82.190  114.630 1.00 38.60 ? 1800 HOH A O     1 
HETATM 18259 O O     . HOH Z  8 .    ? -37.323 45.130  105.172 1.00 37.39 ? 1801 HOH A O     1 
HETATM 18260 O O     . HOH Z  8 .    ? -32.571 93.019  105.129 1.00 33.38 ? 1802 HOH A O     1 
HETATM 18261 O O     . HOH Z  8 .    ? -27.404 64.870  101.302 1.00 27.02 ? 1803 HOH A O     1 
HETATM 18262 O O     . HOH Z  8 .    ? -35.219 64.736  67.058  1.00 36.33 ? 1804 HOH A O     1 
HETATM 18263 O O     . HOH Z  8 .    ? -47.847 70.607  112.306 1.00 42.30 ? 1805 HOH A O     1 
HETATM 18264 O O     . HOH Z  8 .    ? -49.777 54.015  74.865  1.00 28.70 ? 1806 HOH A O     1 
HETATM 18265 O O     . HOH Z  8 .    ? -27.098 89.404  78.669  1.00 36.25 ? 1807 HOH A O     1 
HETATM 18266 O O     . HOH Z  8 .    ? 5.170   55.124  98.138  1.00 29.71 ? 1808 HOH A O     1 
HETATM 18267 O O     . HOH Z  8 .    ? -28.242 60.381  126.040 1.00 43.10 ? 1809 HOH A O     1 
HETATM 18268 O O     . HOH Z  8 .    ? -42.554 47.275  82.095  1.00 30.23 ? 1810 HOH A O     1 
HETATM 18269 O O     . HOH Z  8 .    ? 12.701  67.214  94.799  1.00 40.59 ? 1811 HOH A O     1 
HETATM 18270 O O     . HOH Z  8 .    ? -26.553 84.373  74.993  1.00 35.27 ? 1812 HOH A O     1 
HETATM 18271 O O     . HOH Z  8 .    ? -43.054 49.732  56.712  1.00 42.65 ? 1813 HOH A O     1 
HETATM 18272 O O     . HOH Z  8 .    ? -22.115 54.402  87.378  1.00 41.04 ? 1814 HOH A O     1 
HETATM 18273 O O     . HOH Z  8 .    ? -41.721 64.104  104.648 1.00 27.77 ? 1815 HOH A O     1 
HETATM 18274 O O     . HOH Z  8 .    ? -4.805  59.043  119.569 1.00 32.56 ? 1816 HOH A O     1 
HETATM 18275 O O     . HOH Z  8 .    ? -59.415 58.266  77.768  1.00 24.11 ? 1817 HOH A O     1 
HETATM 18276 O O     . HOH Z  8 .    ? -8.028  77.318  93.112  1.00 30.44 ? 1818 HOH A O     1 
HETATM 18277 O O     . HOH Z  8 .    ? -46.233 72.634  65.091  1.00 27.44 ? 1819 HOH A O     1 
HETATM 18278 O O     . HOH Z  8 .    ? -4.194  76.351  125.705 1.00 36.87 ? 1820 HOH A O     1 
HETATM 18279 O O     . HOH Z  8 .    ? -22.942 53.837  93.583  1.00 34.90 ? 1821 HOH A O     1 
HETATM 18280 O O     . HOH Z  8 .    ? -37.078 51.430  61.684  1.00 38.90 ? 1822 HOH A O     1 
HETATM 18281 O O     . HOH Z  8 .    ? -3.315  82.370  98.542  1.00 33.32 ? 1823 HOH A O     1 
HETATM 18282 O O     . HOH Z  8 .    ? -24.572 69.464  75.580  1.00 36.55 ? 1824 HOH A O     1 
HETATM 18283 O O     . HOH Z  8 .    ? -23.255 72.823  103.485 1.00 43.05 ? 1825 HOH A O     1 
HETATM 18284 O O     . HOH Z  8 .    ? -61.539 55.223  68.349  1.00 24.68 ? 1826 HOH A O     1 
HETATM 18285 O O     . HOH Z  8 .    ? -50.613 66.272  107.515 1.00 30.58 ? 1827 HOH A O     1 
HETATM 18286 O O     . HOH Z  8 .    ? 7.203   89.042  124.136 1.00 37.79 ? 1828 HOH A O     1 
HETATM 18287 O O     . HOH Z  8 .    ? -37.038 60.434  97.358  1.00 29.37 ? 1829 HOH A O     1 
HETATM 18288 O O     . HOH Z  8 .    ? -25.561 59.217  115.588 1.00 28.93 ? 1830 HOH A O     1 
HETATM 18289 O O     . HOH Z  8 .    ? -12.628 39.890  68.955  1.00 42.85 ? 1831 HOH A O     1 
HETATM 18290 O O     . HOH Z  8 .    ? -13.107 53.042  111.968 1.00 38.07 ? 1832 HOH A O     1 
HETATM 18291 O O     . HOH Z  8 .    ? -8.111  75.317  71.305  1.00 35.73 ? 1833 HOH A O     1 
HETATM 18292 O O     . HOH Z  8 .    ? -20.431 59.547  79.893  1.00 38.93 ? 1834 HOH A O     1 
HETATM 18293 O O     . HOH Z  8 .    ? -41.817 70.901  96.322  1.00 27.42 ? 1835 HOH A O     1 
HETATM 18294 O O     . HOH Z  8 .    ? -23.067 83.578  92.589  1.00 27.79 ? 1836 HOH A O     1 
HETATM 18295 O O     . HOH Z  8 .    ? 18.711  73.027  119.678 1.00 30.13 ? 1837 HOH A O     1 
HETATM 18296 O O     . HOH Z  8 .    ? 16.869  71.442  120.612 1.00 36.09 ? 1838 HOH A O     1 
HETATM 18297 O O     . HOH Z  8 .    ? 13.972  87.189  111.661 1.00 40.89 ? 1839 HOH A O     1 
HETATM 18298 O O     . HOH Z  8 .    ? -39.063 71.196  85.190  1.00 33.09 ? 1840 HOH A O     1 
HETATM 18299 O O     . HOH Z  8 .    ? -48.818 61.519  57.606  1.00 30.12 ? 1841 HOH A O     1 
HETATM 18300 O O     . HOH Z  8 .    ? -25.667 68.299  91.784  1.00 28.10 ? 1842 HOH A O     1 
HETATM 18301 O O     . HOH Z  8 .    ? -31.290 61.027  91.566  1.00 26.78 ? 1843 HOH A O     1 
HETATM 18302 O O     . HOH Z  8 .    ? -2.132  78.247  76.788  1.00 38.84 ? 1844 HOH A O     1 
HETATM 18303 O O     . HOH Z  8 .    ? -25.785 66.892  88.519  1.00 38.83 ? 1845 HOH A O     1 
HETATM 18304 O O     . HOH Z  8 .    ? 23.232  65.671  116.456 1.00 38.96 ? 1846 HOH A O     1 
HETATM 18305 O O     . HOH Z  8 .    ? -55.448 47.343  70.558  1.00 29.61 ? 1847 HOH A O     1 
HETATM 18306 O O     . HOH Z  8 .    ? 24.883  58.218  111.268 1.00 41.89 ? 1848 HOH A O     1 
HETATM 18307 O O     . HOH Z  8 .    ? -13.145 43.016  77.046  1.00 45.05 ? 1849 HOH A O     1 
HETATM 18308 O O     . HOH Z  8 .    ? -14.056 96.089  121.539 1.00 43.17 ? 1850 HOH A O     1 
HETATM 18309 O O     . HOH Z  8 .    ? -6.652  71.188  104.842 1.00 36.36 ? 1851 HOH A O     1 
HETATM 18310 O O     . HOH Z  8 .    ? -54.578 37.238  90.306  1.00 42.38 ? 1852 HOH A O     1 
HETATM 18311 O O     . HOH Z  8 .    ? -39.273 66.709  95.372  1.00 33.54 ? 1853 HOH A O     1 
HETATM 18312 O O     . HOH Z  8 .    ? -35.034 80.660  121.652 1.00 31.90 ? 1854 HOH A O     1 
HETATM 18313 O O     . HOH Z  8 .    ? -20.070 89.237  76.194  1.00 32.95 ? 1855 HOH A O     1 
HETATM 18314 O O     . HOH Z  8 .    ? -37.602 66.046  110.510 1.00 33.82 ? 1856 HOH A O     1 
HETATM 18315 O O     . HOH Z  8 .    ? -11.821 88.787  130.309 1.00 38.46 ? 1857 HOH A O     1 
HETATM 18316 O O     . HOH Z  8 .    ? -28.632 69.577  87.086  1.00 35.07 ? 1858 HOH A O     1 
HETATM 18317 O O     . HOH Z  8 .    ? -21.077 101.338 90.745  1.00 40.78 ? 1859 HOH A O     1 
HETATM 18318 O O     . HOH Z  8 .    ? -19.846 85.171  76.562  1.00 35.95 ? 1860 HOH A O     1 
HETATM 18319 O O     . HOH Z  8 .    ? -12.514 77.395  91.977  1.00 22.01 ? 1861 HOH A O     1 
HETATM 18320 O O     . HOH Z  8 .    ? -41.221 80.094  88.564  1.00 28.40 ? 1862 HOH A O     1 
HETATM 18321 O O     . HOH Z  8 .    ? -48.628 75.128  96.557  1.00 29.75 ? 1863 HOH A O     1 
HETATM 18322 O O     . HOH Z  8 .    ? 20.815  61.858  100.411 1.00 31.22 ? 1864 HOH A O     1 
HETATM 18323 O O     . HOH Z  8 .    ? -1.827  80.429  113.069 1.00 35.50 ? 1865 HOH A O     1 
HETATM 18324 O O     . HOH Z  8 .    ? -39.913 88.965  120.485 1.00 41.04 ? 1866 HOH A O     1 
HETATM 18325 O O     . HOH Z  8 .    ? 0.368   64.060  108.502 1.00 26.29 ? 1867 HOH A O     1 
HETATM 18326 O O     . HOH Z  8 .    ? -28.895 83.913  105.463 1.00 32.12 ? 1868 HOH A O     1 
HETATM 18327 O O     . HOH Z  8 .    ? 7.918   92.986  100.488 1.00 49.77 ? 1869 HOH A O     1 
HETATM 18328 O O     . HOH Z  8 .    ? -38.267 72.899  88.306  1.00 31.93 ? 1870 HOH A O     1 
HETATM 18329 O O     . HOH Z  8 .    ? -38.735 73.204  91.293  1.00 36.41 ? 1871 HOH A O     1 
HETATM 18330 O O     . HOH Z  8 .    ? -34.575 56.363  106.435 1.00 31.86 ? 1872 HOH A O     1 
HETATM 18331 O O     . HOH Z  8 .    ? -25.195 83.022  73.687  1.00 35.14 ? 1873 HOH A O     1 
HETATM 18332 O O     . HOH Z  8 .    ? -38.743 86.336  84.606  1.00 43.89 ? 1874 HOH A O     1 
HETATM 18333 O O     . HOH Z  8 .    ? -58.617 34.547  85.591  1.00 41.80 ? 1875 HOH A O     1 
HETATM 18334 O O     . HOH Z  8 .    ? -6.238  70.862  107.203 1.00 35.44 ? 1876 HOH A O     1 
HETATM 18335 O O     . HOH Z  8 .    ? -11.196 53.807  101.198 1.00 30.20 ? 1877 HOH A O     1 
HETATM 18336 O O     . HOH Z  8 .    ? -19.669 91.138  77.870  1.00 37.19 ? 1878 HOH A O     1 
HETATM 18337 O O     . HOH Z  8 .    ? -4.846  82.430  126.599 1.00 42.11 ? 1879 HOH A O     1 
HETATM 18338 O O     . HOH Z  8 .    ? -49.409 47.518  98.391  1.00 31.56 ? 1880 HOH A O     1 
HETATM 18339 O O     . HOH Z  8 .    ? 2.138   76.030  118.197 1.00 31.46 ? 1881 HOH A O     1 
HETATM 18340 O O     . HOH Z  8 .    ? -32.015 94.287  128.906 1.00 48.42 ? 1882 HOH A O     1 
HETATM 18341 O O     . HOH Z  8 .    ? -9.974  74.283  105.338 1.00 34.73 ? 1883 HOH A O     1 
HETATM 18342 O O     . HOH Z  8 .    ? -45.394 57.604  103.167 1.00 36.52 ? 1884 HOH A O     1 
HETATM 18343 O O     . HOH Z  8 .    ? -13.614 55.252  104.634 1.00 38.35 ? 1885 HOH A O     1 
HETATM 18344 O O     . HOH Z  8 .    ? -31.574 58.205  116.754 1.00 39.19 ? 1886 HOH A O     1 
HETATM 18345 O O     . HOH Z  8 .    ? -64.833 42.816  87.514  1.00 40.96 ? 1887 HOH A O     1 
HETATM 18346 O O     . HOH Z  8 .    ? -42.983 65.836  64.535  1.00 34.17 ? 1888 HOH A O     1 
HETATM 18347 O O     . HOH Z  8 .    ? -53.749 72.288  68.847  1.00 33.54 ? 1889 HOH A O     1 
HETATM 18348 O O     . HOH Z  8 .    ? -29.483 59.961  89.684  1.00 25.79 ? 1890 HOH A O     1 
HETATM 18349 O O     . HOH Z  8 .    ? -18.884 86.266  110.544 1.00 36.77 ? 1891 HOH A O     1 
HETATM 18350 O O     . HOH Z  8 .    ? -38.414 75.802  99.455  1.00 38.52 ? 1892 HOH A O     1 
HETATM 18351 O O     . HOH Z  8 .    ? -26.076 62.623  62.419  1.00 48.55 ? 1893 HOH A O     1 
HETATM 18352 O O     . HOH Z  8 .    ? -44.196 59.293  88.462  1.00 21.86 ? 1894 HOH A O     1 
HETATM 18353 O O     . HOH Z  8 .    ? -45.956 54.786  93.038  1.00 25.19 ? 1895 HOH A O     1 
HETATM 18354 O O     . HOH Z  8 .    ? -1.988  77.856  106.464 1.00 31.95 ? 1896 HOH A O     1 
HETATM 18355 O O     . HOH Z  8 .    ? -14.024 41.721  72.067  1.00 36.14 ? 1897 HOH A O     1 
HETATM 18356 O O     . HOH Z  8 .    ? -33.239 60.194  83.669  1.00 45.71 ? 1898 HOH A O     1 
HETATM 18357 O O     . HOH Z  8 .    ? -8.318  93.395  107.349 1.00 36.21 ? 1899 HOH A O     1 
HETATM 18358 O O     . HOH Z  8 .    ? -54.548 79.456  82.422  1.00 44.48 ? 1900 HOH A O     1 
HETATM 18359 O O     . HOH Z  8 .    ? 22.694  76.073  116.545 1.00 30.56 ? 1901 HOH A O     1 
HETATM 18360 O O     . HOH Z  8 .    ? -15.213 78.688  104.352 1.00 35.25 ? 1902 HOH A O     1 
HETATM 18361 O O     . HOH Z  8 .    ? -65.761 54.204  91.616  1.00 36.68 ? 1903 HOH A O     1 
HETATM 18362 O O     . HOH Z  8 .    ? -10.485 63.631  116.752 1.00 31.43 ? 1904 HOH A O     1 
HETATM 18363 O O     . HOH Z  8 .    ? -1.416  70.066  117.575 1.00 29.47 ? 1905 HOH A O     1 
HETATM 18364 O O     . HOH Z  8 .    ? -14.528 85.349  77.933  1.00 36.11 ? 1906 HOH A O     1 
HETATM 18365 O O     . HOH Z  8 .    ? -22.050 89.858  110.725 1.00 39.22 ? 1907 HOH A O     1 
HETATM 18366 O O     . HOH Z  8 .    ? -23.756 63.993  74.297  1.00 45.05 ? 1908 HOH A O     1 
HETATM 18367 O O     . HOH Z  8 .    ? 4.590   85.921  102.089 1.00 35.12 ? 1909 HOH A O     1 
HETATM 18368 O O     . HOH Z  8 .    ? -37.987 65.306  89.356  1.00 35.34 ? 1910 HOH A O     1 
HETATM 18369 O O     . HOH Z  8 .    ? -66.671 68.558  84.842  1.00 40.06 ? 1911 HOH A O     1 
HETATM 18370 O O     . HOH Z  8 .    ? 2.732   77.941  99.407  1.00 28.36 ? 1912 HOH A O     1 
HETATM 18371 O O     . HOH Z  8 .    ? 2.599   74.352  110.621 1.00 32.78 ? 1913 HOH A O     1 
HETATM 18372 O O     . HOH Z  8 .    ? -36.551 80.908  76.740  1.00 27.44 ? 1914 HOH A O     1 
HETATM 18373 O O     . HOH Z  8 .    ? -11.576 43.193  74.947  1.00 34.66 ? 1915 HOH A O     1 
HETATM 18374 O O     . HOH Z  8 .    ? -6.898  93.967  114.854 1.00 37.95 ? 1916 HOH A O     1 
HETATM 18375 O O     . HOH Z  8 .    ? -59.869 62.799  78.308  1.00 29.62 ? 1917 HOH A O     1 
HETATM 18376 O O     . HOH Z  8 .    ? -53.704 49.192  61.020  1.00 36.28 ? 1918 HOH A O     1 
HETATM 18377 O O     . HOH Z  8 .    ? 2.261   86.165  127.535 1.00 39.62 ? 1919 HOH A O     1 
HETATM 18378 O O     . HOH Z  8 .    ? -66.285 64.265  89.099  1.00 36.96 ? 1920 HOH A O     1 
HETATM 18379 O O     . HOH Z  8 .    ? -34.905 77.491  85.985  1.00 30.73 ? 1921 HOH A O     1 
HETATM 18380 O O     . HOH Z  8 .    ? -37.740 86.185  103.060 1.00 35.12 ? 1922 HOH A O     1 
HETATM 18381 O O     . HOH Z  8 .    ? -39.176 74.988  97.287  1.00 35.23 ? 1923 HOH A O     1 
HETATM 18382 O O     . HOH Z  8 .    ? -27.507 90.769  117.268 1.00 40.42 ? 1924 HOH A O     1 
HETATM 18383 O O     . HOH Z  8 .    ? -1.543  95.995  118.777 1.00 42.30 ? 1925 HOH A O     1 
HETATM 18384 O O     . HOH Z  8 .    ? -9.412  60.501  85.318  1.00 24.39 ? 1926 HOH A O     1 
HETATM 18385 O O     . HOH Z  8 .    ? -38.165 67.868  99.242  1.00 29.96 ? 1927 HOH A O     1 
HETATM 18386 O O     . HOH Z  8 .    ? 21.769  72.818  117.319 1.00 39.88 ? 1928 HOH A O     1 
HETATM 18387 O O     . HOH Z  8 .    ? -14.364 93.230  89.473  1.00 46.55 ? 1929 HOH A O     1 
HETATM 18388 O O     . HOH Z  8 .    ? -12.357 93.867  79.078  1.00 53.22 ? 1930 HOH A O     1 
HETATM 18389 O O     . HOH Z  8 .    ? -21.208 50.187  109.724 1.00 40.79 ? 1931 HOH A O     1 
HETATM 18390 O O     . HOH Z  8 .    ? -45.554 63.718  106.830 1.00 38.63 ? 1932 HOH A O     1 
HETATM 18391 O O     . HOH Z  8 .    ? -17.926 85.840  78.446  1.00 32.27 ? 1933 HOH A O     1 
HETATM 18392 O O     . HOH Z  8 .    ? -33.867 95.277  93.821  1.00 44.75 ? 1934 HOH A O     1 
HETATM 18393 O O     . HOH Z  8 .    ? -58.619 65.039  95.056  1.00 38.28 ? 1935 HOH A O     1 
HETATM 18394 O O     . HOH Z  8 .    ? -19.912 76.793  68.031  1.00 41.81 ? 1936 HOH A O     1 
HETATM 18395 O O     . HOH Z  8 .    ? 14.717  82.462  121.087 1.00 34.26 ? 1937 HOH A O     1 
HETATM 18396 O O     . HOH Z  8 .    ? -2.389  62.554  114.463 1.00 35.96 ? 1938 HOH A O     1 
HETATM 18397 O O     . HOH Z  8 .    ? -62.605 54.230  64.032  1.00 38.22 ? 1939 HOH A O     1 
HETATM 18398 O O     . HOH Z  8 .    ? -0.384  67.890  118.891 1.00 39.03 ? 1940 HOH A O     1 
HETATM 18399 O O     . HOH Z  8 .    ? -32.601 92.283  111.708 1.00 38.54 ? 1941 HOH A O     1 
HETATM 18400 O O     . HOH Z  8 .    ? -42.997 77.760  79.517  1.00 31.59 ? 1942 HOH A O     1 
HETATM 18401 O O     . HOH Z  8 .    ? 6.937   87.939  125.822 1.00 38.08 ? 1943 HOH A O     1 
HETATM 18402 O O     . HOH Z  8 .    ? -12.890 69.179  75.076  1.00 38.57 ? 1944 HOH A O     1 
HETATM 18403 O O     . HOH Z  8 .    ? -36.740 95.314  95.093  1.00 38.07 ? 1945 HOH A O     1 
HETATM 18404 O O     . HOH Z  8 .    ? 2.405   58.817  114.839 1.00 43.00 ? 1946 HOH A O     1 
HETATM 18405 O O     . HOH Z  8 .    ? -35.302 65.532  75.514  1.00 44.25 ? 1947 HOH A O     1 
HETATM 18406 O O     . HOH Z  8 .    ? 8.981   64.693  95.589  1.00 36.80 ? 1948 HOH A O     1 
HETATM 18407 O O     . HOH Z  8 .    ? -52.658 29.684  73.657  1.00 50.03 ? 1949 HOH A O     1 
HETATM 18408 O O     . HOH Z  8 .    ? -50.090 72.924  63.650  1.00 31.68 ? 1950 HOH A O     1 
HETATM 18409 O O     . HOH Z  8 .    ? 1.215   70.054  88.577  1.00 42.36 ? 1951 HOH A O     1 
HETATM 18410 O O     . HOH Z  8 .    ? -14.605 55.162  51.627  1.00 49.23 ? 1952 HOH A O     1 
HETATM 18411 O O     . HOH Z  8 .    ? -57.387 53.370  97.332  1.00 27.49 ? 1953 HOH A O     1 
HETATM 18412 O O     . HOH Z  8 .    ? -43.333 56.185  92.955  1.00 23.81 ? 1954 HOH A O     1 
HETATM 18413 O O     . HOH Z  8 .    ? -41.837 64.339  59.386  1.00 32.27 ? 1955 HOH A O     1 
HETATM 18414 O O     . HOH Z  8 .    ? -45.748 89.570  107.711 1.00 43.53 ? 1956 HOH A O     1 
HETATM 18415 O O     . HOH Z  8 .    ? 1.092   56.991  108.834 1.00 26.13 ? 1957 HOH A O     1 
HETATM 18416 O O     . HOH Z  8 .    ? -35.308 40.376  93.118  1.00 31.22 ? 1958 HOH A O     1 
HETATM 18417 O O     . HOH Z  8 .    ? -47.172 77.215  93.040  1.00 30.32 ? 1959 HOH A O     1 
HETATM 18418 O O     . HOH Z  8 .    ? -65.203 54.923  81.774  1.00 31.05 ? 1960 HOH A O     1 
HETATM 18419 O O     . HOH Z  8 .    ? 7.004   55.075  100.011 1.00 24.38 ? 1961 HOH A O     1 
HETATM 18420 O O     . HOH Z  8 .    ? -21.031 90.221  106.243 1.00 45.54 ? 1962 HOH A O     1 
HETATM 18421 O O     . HOH Z  8 .    ? -22.405 76.987  71.148  1.00 30.88 ? 1963 HOH A O     1 
HETATM 18422 O O     . HOH Z  8 .    ? -32.218 44.665  104.480 1.00 44.70 ? 1964 HOH A O     1 
HETATM 18423 O O     . HOH Z  8 .    ? -2.887  75.895  78.319  1.00 29.94 ? 1965 HOH A O     1 
HETATM 18424 O O     . HOH Z  8 .    ? -26.419 60.617  59.053  1.00 44.74 ? 1966 HOH A O     1 
HETATM 18425 O O     . HOH Z  8 .    ? -10.923 66.600  128.758 1.00 40.38 ? 1967 HOH A O     1 
HETATM 18426 O O     . HOH Z  8 .    ? -9.184  51.660  108.704 1.00 34.26 ? 1968 HOH A O     1 
HETATM 18427 O O     . HOH Z  8 .    ? -13.630 54.168  77.938  1.00 26.18 ? 1969 HOH A O     1 
HETATM 18428 O O     . HOH Z  8 .    ? 10.688  64.503  116.204 1.00 41.72 ? 1970 HOH A O     1 
HETATM 18429 O O     . HOH Z  8 .    ? -23.532 76.009  134.744 1.00 42.65 ? 1971 HOH A O     1 
HETATM 18430 O O     . HOH Z  8 .    ? -8.592  82.213  106.056 1.00 34.45 ? 1972 HOH A O     1 
HETATM 18431 O O     . HOH Z  8 .    ? -44.226 66.174  108.108 1.00 39.39 ? 1973 HOH A O     1 
HETATM 18432 O O     . HOH Z  8 .    ? -32.464 56.108  86.979  1.00 29.48 ? 1974 HOH A O     1 
HETATM 18433 O O     . HOH Z  8 .    ? 11.072  85.062  126.237 1.00 35.86 ? 1975 HOH A O     1 
HETATM 18434 O O     . HOH Z  8 .    ? -7.700  68.000  74.764  1.00 49.27 ? 1976 HOH A O     1 
HETATM 18435 O O     . HOH Z  8 .    ? -0.525  52.333  59.940  1.00 42.33 ? 1977 HOH A O     1 
HETATM 18436 O O     . HOH Z  8 .    ? -16.482 42.946  72.985  1.00 42.98 ? 1978 HOH A O     1 
HETATM 18437 O O     . HOH Z  8 .    ? -31.584 41.074  99.228  1.00 45.14 ? 1979 HOH A O     1 
HETATM 18438 O O     . HOH Z  8 .    ? -18.380 68.708  105.970 1.00 28.04 ? 1980 HOH A O     1 
HETATM 18439 O O     . HOH Z  8 .    ? -10.802 94.781  83.820  1.00 46.11 ? 1981 HOH A O     1 
HETATM 18440 O O     . HOH Z  8 .    ? -5.346  70.393  74.199  1.00 46.13 ? 1982 HOH A O     1 
HETATM 18441 O O     . HOH Z  8 .    ? -6.935  38.138  64.108  1.00 40.52 ? 1983 HOH A O     1 
HETATM 18442 O O     . HOH Z  8 .    ? -20.413 54.688  99.982  1.00 34.52 ? 1984 HOH A O     1 
HETATM 18443 O O     . HOH Z  8 .    ? -52.650 75.570  69.388  1.00 37.15 ? 1985 HOH A O     1 
HETATM 18444 O O     . HOH Z  8 .    ? -17.573 88.546  108.666 1.00 39.51 ? 1986 HOH A O     1 
HETATM 18445 O O     . HOH Z  8 .    ? -63.382 62.146  98.720  1.00 38.25 ? 1987 HOH A O     1 
HETATM 18446 O O     . HOH Z  8 .    ? -37.380 54.412  54.957  1.00 51.84 ? 1988 HOH A O     1 
HETATM 18447 O O     . HOH Z  8 .    ? -57.196 31.911  89.161  1.00 43.95 ? 1989 HOH A O     1 
HETATM 18448 O O     . HOH Z  8 .    ? -37.920 40.276  75.331  1.00 40.27 ? 1990 HOH A O     1 
HETATM 18449 O O     . HOH Z  8 .    ? -33.457 42.386  93.420  1.00 37.55 ? 1991 HOH A O     1 
HETATM 18450 O O     . HOH Z  8 .    ? -6.146  61.828  94.476  1.00 45.92 ? 1992 HOH A O     1 
HETATM 18451 O O     . HOH Z  8 .    ? -33.450 84.139  129.456 1.00 39.68 ? 1993 HOH A O     1 
HETATM 18452 O O     . HOH Z  8 .    ? -62.316 59.960  96.790  1.00 31.26 ? 1994 HOH A O     1 
HETATM 18453 O O     . HOH Z  8 .    ? -0.071  87.212  126.172 1.00 38.90 ? 1995 HOH A O     1 
HETATM 18454 O O     . HOH Z  8 .    ? -1.896  54.411  102.903 1.00 32.97 ? 1996 HOH A O     1 
HETATM 18455 O O     . HOH Z  8 .    ? -63.049 67.545  67.404  1.00 35.33 ? 1997 HOH A O     1 
HETATM 18456 O O     . HOH Z  8 .    ? -3.593  59.719  69.746  1.00 45.61 ? 1998 HOH A O     1 
HETATM 18457 O O     . HOH Z  8 .    ? -31.472 34.567  73.414  1.00 50.55 ? 1999 HOH A O     1 
HETATM 18458 O O     . HOH Z  8 .    ? -9.300  83.840  81.829  1.00 42.27 ? 2000 HOH A O     1 
HETATM 18459 O O     . HOH Z  8 .    ? -52.065 54.888  71.136  1.00 32.85 ? 2001 HOH A O     1 
HETATM 18460 O O     . HOH Z  8 .    ? -17.268 88.029  76.927  1.00 43.23 ? 2002 HOH A O     1 
HETATM 18461 O O     . HOH Z  8 .    ? -44.074 90.411  101.365 1.00 41.81 ? 2003 HOH A O     1 
HETATM 18462 O O     . HOH Z  8 .    ? -10.925 63.041  69.752  1.00 33.91 ? 2004 HOH A O     1 
HETATM 18463 O O     . HOH Z  8 .    ? -26.108 74.537  134.174 1.00 41.73 ? 2005 HOH A O     1 
HETATM 18464 O O     . HOH Z  8 .    ? -48.025 79.862  96.676  1.00 42.56 ? 2006 HOH A O     1 
HETATM 18465 O O     . HOH Z  8 .    ? -18.503 59.610  112.451 1.00 42.41 ? 2007 HOH A O     1 
HETATM 18466 O O     . HOH Z  8 .    ? 19.821  64.326  94.656  1.00 35.96 ? 2008 HOH A O     1 
HETATM 18467 O O     . HOH Z  8 .    ? -42.026 88.905  94.867  1.00 42.55 ? 2009 HOH A O     1 
HETATM 18468 O O     . HOH Z  8 .    ? -53.351 66.161  103.055 1.00 43.88 ? 2010 HOH A O     1 
HETATM 18469 O O     . HOH Z  8 .    ? -28.971 95.991  109.003 1.00 46.04 ? 2011 HOH A O     1 
HETATM 18470 O O     . HOH Z  8 .    ? -41.181 70.054  93.948  1.00 33.15 ? 2012 HOH A O     1 
HETATM 18471 O O     . HOH Z  8 .    ? -8.887  41.087  70.205  1.00 38.33 ? 2013 HOH A O     1 
HETATM 18472 O O     . HOH Z  8 .    ? -53.025 56.702  74.736  1.00 29.06 ? 2014 HOH A O     1 
HETATM 18473 O O     . HOH Z  8 .    ? -34.345 59.056  107.439 1.00 32.24 ? 2015 HOH A O     1 
HETATM 18474 O O     . HOH Z  8 .    ? 10.995  89.762  106.657 1.00 44.12 ? 2016 HOH A O     1 
HETATM 18475 O O     . HOH Z  8 .    ? -46.235 78.380  91.093  1.00 30.41 ? 2017 HOH A O     1 
HETATM 18476 O O     . HOH Z  8 .    ? -47.615 32.621  86.693  1.00 42.20 ? 2018 HOH A O     1 
HETATM 18477 O O     . HOH Z  8 .    ? -18.065 54.029  99.890  1.00 40.10 ? 2019 HOH A O     1 
HETATM 18478 O O     . HOH Z  8 .    ? -2.120  83.528  116.786 1.00 34.89 ? 2020 HOH A O     1 
HETATM 18479 O O     . HOH Z  8 .    ? -60.244 63.790  93.177  1.00 39.11 ? 2021 HOH A O     1 
HETATM 18480 O O     . HOH Z  8 .    ? -29.648 58.683  80.051  1.00 47.24 ? 2022 HOH A O     1 
HETATM 18481 O O     . HOH Z  8 .    ? -39.637 47.102  105.163 1.00 35.74 ? 2023 HOH A O     1 
HETATM 18482 O O     . HOH Z  8 .    ? -22.783 74.374  70.638  1.00 40.80 ? 2024 HOH A O     1 
HETATM 18483 O O     . HOH Z  8 .    ? -66.358 54.687  79.028  1.00 36.66 ? 2025 HOH A O     1 
HETATM 18484 O O     . HOH Z  8 .    ? -28.382 82.843  103.141 1.00 33.88 ? 2026 HOH A O     1 
HETATM 18485 O O     . HOH Z  8 .    ? -27.288 60.425  123.899 1.00 38.67 ? 2027 HOH A O     1 
HETATM 18486 O O     . HOH Z  8 .    ? 22.567  64.719  95.048  1.00 48.25 ? 2028 HOH A O     1 
HETATM 18487 O O     . HOH Z  8 .    ? 18.871  75.214  98.326  1.00 43.68 ? 2029 HOH A O     1 
HETATM 18488 O O     . HOH Z  8 .    ? -51.070 80.146  72.698  1.00 38.22 ? 2030 HOH A O     1 
HETATM 18489 O O     . HOH Z  8 .    ? -40.023 67.834  90.298  1.00 34.51 ? 2031 HOH A O     1 
HETATM 18490 O O     . HOH Z  8 .    ? -31.581 78.198  91.935  1.00 37.49 ? 2032 HOH A O     1 
HETATM 18491 O O     . HOH Z  8 .    ? -21.526 53.117  89.396  1.00 43.78 ? 2033 HOH A O     1 
HETATM 18492 O O     . HOH Z  8 .    ? 6.374   91.197  119.956 1.00 34.52 ? 2034 HOH A O     1 
HETATM 18493 O O     . HOH Z  8 .    ? -63.223 60.720  94.382  1.00 39.08 ? 2035 HOH A O     1 
HETATM 18494 O O     . HOH Z  8 .    ? -64.661 62.792  68.991  1.00 42.02 ? 2036 HOH A O     1 
HETATM 18495 O O     . HOH Z  8 .    ? 20.633  75.513  100.791 1.00 43.00 ? 2037 HOH A O     1 
HETATM 18496 O O     . HOH Z  8 .    ? -21.099 86.969  109.045 1.00 35.37 ? 2038 HOH A O     1 
HETATM 18497 O O     . HOH Z  8 .    ? -29.460 57.280  86.920  1.00 43.81 ? 2039 HOH A O     1 
HETATM 18498 O O     . HOH Z  8 .    ? -55.456 57.117  103.245 1.00 36.81 ? 2040 HOH A O     1 
HETATM 18499 O O     . HOH Z  8 .    ? -27.781 51.348  111.077 1.00 42.05 ? 2041 HOH A O     1 
HETATM 18500 O O     . HOH Z  8 .    ? 16.762  83.923  114.780 1.00 45.04 ? 2042 HOH A O     1 
HETATM 18501 O O     . HOH Z  8 .    ? -21.417 102.422 88.380  1.00 44.09 ? 2043 HOH A O     1 
HETATM 18502 O O     . HOH Z  8 .    ? -24.430 46.994  58.685  1.00 45.12 ? 2044 HOH A O     1 
HETATM 18503 O O     . HOH Z  8 .    ? -27.154 65.541  104.139 1.00 37.32 ? 2045 HOH A O     1 
HETATM 18504 O O     . HOH Z  8 .    ? -33.424 84.337  77.749  1.00 31.17 ? 2046 HOH A O     1 
HETATM 18505 O O     . HOH Z  8 .    ? -28.840 57.699  89.517  1.00 34.89 ? 2047 HOH A O     1 
HETATM 18506 O O     . HOH Z  8 .    ? -45.143 69.488  112.983 1.00 41.99 ? 2048 HOH A O     1 
HETATM 18507 O O     . HOH Z  8 .    ? -56.278 24.571  91.313  1.00 50.40 ? 2049 HOH A O     1 
HETATM 18508 O O     . HOH Z  8 .    ? 20.271  61.478  98.108  1.00 33.90 ? 2050 HOH A O     1 
HETATM 18509 O O     . HOH Z  8 .    ? -45.644 85.018  91.339  1.00 47.53 ? 2051 HOH A O     1 
HETATM 18510 O O     . HOH Z  8 .    ? 12.390  88.495  120.332 1.00 40.22 ? 2052 HOH A O     1 
HETATM 18511 O O     . HOH Z  8 .    ? -52.679 73.938  62.779  1.00 33.38 ? 2053 HOH A O     1 
HETATM 18512 O O     . HOH Z  8 .    ? -67.199 65.952  84.139  1.00 34.54 ? 2054 HOH A O     1 
HETATM 18513 O O     . HOH Z  8 .    ? 6.667   66.773  95.261  1.00 38.49 ? 2055 HOH A O     1 
HETATM 18514 O O     . HOH Z  8 .    ? -1.676  75.864  126.405 1.00 43.76 ? 2056 HOH A O     1 
HETATM 18515 O O     . HOH Z  8 .    ? -9.041  62.286  71.281  1.00 41.62 ? 2057 HOH A O     1 
HETATM 18516 O O     . HOH Z  8 .    ? -42.333 63.920  107.232 1.00 37.11 ? 2058 HOH A O     1 
HETATM 18517 O O     . HOH Z  8 .    ? -29.424 60.532  122.121 1.00 39.15 ? 2059 HOH A O     1 
HETATM 18518 O O     . HOH Z  8 .    ? -15.529 57.663  107.071 1.00 36.84 ? 2060 HOH A O     1 
HETATM 18519 O O     . HOH Z  8 .    ? -21.499 63.118  82.454  1.00 42.32 ? 2061 HOH A O     1 
HETATM 18520 O O     . HOH Z  8 .    ? -34.819 76.253  88.338  1.00 33.96 ? 2062 HOH A O     1 
HETATM 18521 O O     . HOH Z  8 .    ? -10.718 78.724  93.270  1.00 27.36 ? 2063 HOH A O     1 
HETATM 18522 O O     . HOH Z  8 .    ? -32.965 98.604  100.561 1.00 41.99 ? 2064 HOH A O     1 
HETATM 18523 O O     . HOH Z  8 .    ? -30.658 82.130  101.825 1.00 32.63 ? 2065 HOH A O     1 
HETATM 18524 O O     . HOH Z  8 .    ? -24.977 66.104  98.104  1.00 33.08 ? 2066 HOH A O     1 
HETATM 18525 O O     . HOH Z  8 .    ? -33.601 62.567  90.521  1.00 38.71 ? 2067 HOH A O     1 
HETATM 18526 O O     . HOH Z  8 .    ? -53.317 45.294  95.715  1.00 43.92 ? 2068 HOH A O     1 
HETATM 18527 O O     . HOH Z  8 .    ? -23.208 43.287  57.035  1.00 46.25 ? 2069 HOH A O     1 
HETATM 18528 O O     . HOH Z  8 .    ? -52.899 64.095  101.826 1.00 35.18 ? 2070 HOH A O     1 
HETATM 18529 O O     . HOH Z  8 .    ? -45.020 82.462  90.063  1.00 43.49 ? 2071 HOH A O     1 
HETATM 18530 O O     . HOH Z  8 .    ? -36.127 63.289  91.422  1.00 42.08 ? 2072 HOH A O     1 
HETATM 18531 O O     . HOH Z  8 .    ? -32.443 68.254  102.657 1.00 37.21 ? 2073 HOH A O     1 
HETATM 18532 O O     . HOH Z  8 .    ? -30.449 84.271  74.366  1.00 44.75 ? 2074 HOH A O     1 
HETATM 18533 O O     . HOH Z  8 .    ? -11.477 59.700  107.553 1.00 38.08 ? 2075 HOH A O     1 
HETATM 18534 O O     . HOH Z  8 .    ? -45.626 28.933  88.532  1.00 50.02 ? 2076 HOH A O     1 
HETATM 18535 O O     . HOH Z  8 .    ? -28.379 61.817  59.156  1.00 49.67 ? 2077 HOH A O     1 
HETATM 18536 O O     . HOH Z  8 .    ? -33.903 80.930  75.571  1.00 32.58 ? 2078 HOH A O     1 
HETATM 18537 O O     . HOH Z  8 .    ? -45.049 88.263  100.164 1.00 49.05 ? 2079 HOH A O     1 
HETATM 18538 O O     . HOH Z  8 .    ? -27.252 59.126  117.628 1.00 34.36 ? 2080 HOH A O     1 
HETATM 18539 O O     . HOH Z  8 .    ? 23.206  62.313  100.895 1.00 41.51 ? 2081 HOH A O     1 
HETATM 18540 O O     . HOH Z  8 .    ? -17.368 57.487  111.048 1.00 42.64 ? 2082 HOH A O     1 
HETATM 18541 O O     . HOH Z  8 .    ? -23.044 90.316  101.914 1.00 35.14 ? 2083 HOH A O     1 
HETATM 18542 O O     . HOH Z  8 .    ? -16.770 50.270  77.814  1.00 40.76 ? 2084 HOH A O     1 
HETATM 18543 O O     . HOH Z  8 .    ? -36.527 66.951  88.327  1.00 43.74 ? 2085 HOH A O     1 
HETATM 18544 O O     . HOH Z  8 .    ? 24.870  66.888  114.623 1.00 39.68 ? 2086 HOH A O     1 
HETATM 18545 O O     . HOH Z  8 .    ? -34.053 81.252  123.980 1.00 39.16 ? 2087 HOH A O     1 
HETATM 18546 O O     . HOH Z  8 .    ? -26.184 83.605  70.702  1.00 39.96 ? 2088 HOH A O     1 
HETATM 18547 O O     . HOH Z  8 .    ? -23.943 77.803  69.115  1.00 44.49 ? 2089 HOH A O     1 
HETATM 18548 O O     . HOH Z  8 .    ? 12.946  87.445  126.119 1.00 45.46 ? 2090 HOH A O     1 
HETATM 18549 O O     . HOH Z  8 .    ? -22.444 45.571  56.300  1.00 51.89 ? 2091 HOH A O     1 
HETATM 18550 O O     . HOH Z  8 .    ? 3.829   64.735  97.560  1.00 27.27 ? 2092 HOH A O     1 
HETATM 18551 O O     . HOH Z  8 .    ? -9.064  62.138  95.217  1.00 42.57 ? 2093 HOH A O     1 
HETATM 18552 O O     . HOH Z  8 .    ? -27.160 58.074  58.807  1.00 47.42 ? 2094 HOH A O     1 
HETATM 18553 O O     . HOH Z  8 .    ? -22.756 91.755  104.467 1.00 40.11 ? 2095 HOH A O     1 
HETATM 18554 O O     . HOH Z  8 .    ? -36.472 37.476  87.463  1.00 44.69 ? 2096 HOH A O     1 
HETATM 18555 O O     . HOH Z  8 .    ? -34.855 98.535  102.665 1.00 51.55 ? 2097 HOH A O     1 
HETATM 18556 O O     . HOH Z  8 .    ? -25.688 62.354  103.428 1.00 34.56 ? 2098 HOH A O     1 
HETATM 18557 O O     . HOH Z  8 .    ? -30.322 58.691  120.847 1.00 48.05 ? 2099 HOH A O     1 
HETATM 18558 O O     . HOH Z  8 .    ? -8.840  52.604  101.987 1.00 45.56 ? 2100 HOH A O     1 
HETATM 18559 O O     . HOH Z  8 .    ? -18.778 74.674  110.377 1.00 32.51 ? 2101 HOH A O     1 
HETATM 18560 O O     . HOH Z  8 .    ? -4.230  80.050  126.141 1.00 39.82 ? 2102 HOH A O     1 
HETATM 18561 O O     . HOH Z  8 .    ? -27.171 66.582  99.466  1.00 32.89 ? 2103 HOH A O     1 
HETATM 18562 O O     . HOH Z  8 .    ? -56.801 76.160  77.516  1.00 38.06 ? 2104 HOH A O     1 
HETATM 18563 O O     . HOH Z  8 .    ? -0.844  60.943  113.750 1.00 38.04 ? 2105 HOH A O     1 
HETATM 18564 O O     . HOH Z  8 .    ? -37.181 82.580  78.239  1.00 37.58 ? 2106 HOH A O     1 
HETATM 18565 O O     . HOH Z  8 .    ? -53.538 68.992  101.880 1.00 38.89 ? 2107 HOH A O     1 
HETATM 18566 O O     . HOH Z  8 .    ? -38.271 73.845  94.131  1.00 43.09 ? 2108 HOH A O     1 
HETATM 18567 O O     . HOH Z  8 .    ? -32.751 65.788  125.992 1.00 40.38 ? 2109 HOH A O     1 
HETATM 18568 O O     . HOH Z  8 .    ? -16.784 75.707  107.228 1.00 31.58 ? 2110 HOH A O     1 
HETATM 18569 O O     . HOH Z  8 .    ? -29.148 77.835  71.434  1.00 33.82 ? 2111 HOH A O     1 
HETATM 18570 O O     . HOH Z  8 .    ? -24.435 50.243  96.387  1.00 35.58 ? 2112 HOH A O     1 
HETATM 18571 O O     . HOH Z  8 .    ? -25.383 98.278  79.043  1.00 47.81 ? 2113 HOH A O     1 
HETATM 18572 O O     . HOH Z  8 .    ? -56.975 48.770  98.855  1.00 49.90 ? 2114 HOH A O     1 
HETATM 18573 O O     . HOH Z  8 .    ? 12.782  62.697  94.865  1.00 38.53 ? 2115 HOH A O     1 
HETATM 18574 O O     . HOH Z  8 .    ? -3.480  83.082  113.530 1.00 35.43 ? 2116 HOH A O     1 
HETATM 18575 O O     . HOH Z  8 .    ? -18.877 74.229  107.706 1.00 36.03 ? 2117 HOH A O     1 
HETATM 18576 O O     . HOH Z  8 .    ? -57.088 36.680  89.063  1.00 42.41 ? 2118 HOH A O     1 
HETATM 18577 O O     . HOH Z  8 .    ? 23.064  70.091  117.548 1.00 41.91 ? 2119 HOH A O     1 
HETATM 18578 O O     . HOH Z  8 .    ? -52.558 72.927  103.596 1.00 37.68 ? 2120 HOH A O     1 
HETATM 18579 O O     . HOH Z  8 .    ? 6.866   62.618  96.012  1.00 33.99 ? 2121 HOH A O     1 
HETATM 18580 O O     . HOH Z  8 .    ? -63.516 57.207  97.797  1.00 37.82 ? 2122 HOH A O     1 
HETATM 18581 O O     . HOH Z  8 .    ? -63.116 55.331  70.663  1.00 34.00 ? 2123 HOH A O     1 
HETATM 18582 O O     . HOH Z  8 .    ? -24.645 52.020  101.181 1.00 40.45 ? 2124 HOH A O     1 
HETATM 18583 O O     . HOH Z  8 .    ? -21.049 52.714  102.241 1.00 39.61 ? 2125 HOH A O     1 
HETATM 18584 O O     . HOH Z  8 .    ? -29.930 92.723  110.031 1.00 43.09 ? 2126 HOH A O     1 
HETATM 18585 O O     . HOH Z  8 .    ? -62.007 70.594  86.491  1.00 38.02 ? 2127 HOH A O     1 
HETATM 18586 O O     . HOH Z  8 .    ? -33.715 76.342  90.965  1.00 44.51 ? 2128 HOH A O     1 
HETATM 18587 O O     . HOH Z  8 .    ? -49.337 77.940  94.843  1.00 38.63 ? 2129 HOH A O     1 
HETATM 18588 O O     . HOH Z  8 .    ? 18.653  60.021  94.457  1.00 45.18 ? 2130 HOH A O     1 
HETATM 18589 O O     . HOH Z  8 .    ? -58.641 59.373  104.115 1.00 39.12 ? 2131 HOH A O     1 
HETATM 18590 O O     . HOH Z  8 .    ? -2.501  84.790  97.793  1.00 39.40 ? 2132 HOH A O     1 
HETATM 18591 O O     . HOH Z  8 .    ? -12.582 61.775  106.279 1.00 32.25 ? 2133 HOH A O     1 
HETATM 18592 O O     . HOH Z  8 .    ? -32.964 58.498  85.715  1.00 37.79 ? 2134 HOH A O     1 
HETATM 18593 O O     . HOH Z  8 .    ? -52.094 47.004  97.658  1.00 37.93 ? 2135 HOH A O     1 
HETATM 18594 O O     . HOH Z  8 .    ? -46.186 38.874  105.566 1.00 43.65 ? 2136 HOH A O     1 
HETATM 18595 O O     . HOH Z  8 .    ? -24.963 62.661  101.263 1.00 39.14 ? 2137 HOH A O     1 
HETATM 18596 O O     . HOH Z  8 .    ? 11.022  64.223  94.580  1.00 43.87 ? 2138 HOH A O     1 
HETATM 18597 O O     . HOH Z  8 .    ? -23.769 48.320  95.406  1.00 44.79 ? 2139 HOH A O     1 
HETATM 18598 O O     . HOH Z  8 .    ? -35.545 39.116  74.593  1.00 48.96 ? 2140 HOH A O     1 
HETATM 18599 O O     . HOH Z  8 .    ? -2.181  88.248  127.075 1.00 41.43 ? 2141 HOH A O     1 
HETATM 18600 O O     . HOH Z  8 .    ? -55.321 52.507  101.486 1.00 36.10 ? 2142 HOH A O     1 
HETATM 18601 O O     . HOH Z  8 .    ? -56.078 78.983  77.760  1.00 38.17 ? 2143 HOH A O     1 
HETATM 18602 O O     . HOH Z  8 .    ? -33.408 57.154  112.317 1.00 36.81 ? 2144 HOH A O     1 
HETATM 18603 O O     . HOH Z  8 .    ? -39.238 72.189  96.656  1.00 37.88 ? 2145 HOH A O     1 
HETATM 18604 O O     . HOH Z  8 .    ? -47.873 37.560  103.820 1.00 44.19 ? 2146 HOH A O     1 
HETATM 18605 O O     . HOH Z  8 .    ? -54.295 71.452  103.370 1.00 41.31 ? 2147 HOH A O     1 
HETATM 18606 O O     . HOH Z  8 .    ? -53.959 47.408  99.525  1.00 35.47 ? 2148 HOH A O     1 
HETATM 18607 O O     . HOH AA 8 .    ? -11.333 27.510  82.218  1.00 30.27 ? 1401 HOH B O     1 
HETATM 18608 O O     . HOH AA 8 .    ? 7.664   19.203  117.775 1.00 41.22 ? 1402 HOH B O     1 
HETATM 18609 O O     . HOH AA 8 .    ? -1.172  74.315  75.477  1.00 37.83 ? 1403 HOH B O     1 
HETATM 18610 O O     . HOH AA 8 .    ? 31.630  62.918  66.660  1.00 48.33 ? 1404 HOH B O     1 
HETATM 18611 O O     . HOH AA 8 .    ? -8.271  24.104  117.736 1.00 45.11 ? 1405 HOH B O     1 
HETATM 18612 O O     . HOH AA 8 .    ? -1.065  14.598  86.915  1.00 26.64 ? 1406 HOH B O     1 
HETATM 18613 O O     . HOH AA 8 .    ? -6.475  11.940  126.667 1.00 40.05 ? 1407 HOH B O     1 
HETATM 18614 O O     . HOH AA 8 .    ? 18.615  38.219  116.683 1.00 39.28 ? 1408 HOH B O     1 
HETATM 18615 O O     . HOH AA 8 .    ? 11.470  5.788   123.148 1.00 43.02 ? 1409 HOH B O     1 
HETATM 18616 O O     . HOH AA 8 .    ? -1.826  51.021  91.299  1.00 44.66 ? 1410 HOH B O     1 
HETATM 18617 O O     . HOH AA 8 .    ? -1.282  21.991  72.019  1.00 35.08 ? 1411 HOH B O     1 
HETATM 18618 O O     . HOH AA 8 .    ? 23.832  52.758  71.613  1.00 39.09 ? 1412 HOH B O     1 
HETATM 18619 O O     . HOH AA 8 .    ? 10.906  46.206  107.532 1.00 33.09 ? 1413 HOH B O     1 
HETATM 18620 O O     . HOH AA 8 .    ? 16.988  14.164  110.497 1.00 37.70 ? 1414 HOH B O     1 
HETATM 18621 O O     . HOH AA 8 .    ? 25.472  54.770  62.961  1.00 36.57 ? 1415 HOH B O     1 
HETATM 18622 O O     . HOH AA 8 .    ? -10.277 -2.930  116.870 1.00 40.59 ? 1416 HOH B O     1 
HETATM 18623 O O     . HOH AA 8 .    ? 10.687  24.469  104.894 1.00 40.97 ? 1417 HOH B O     1 
HETATM 18624 O O     . HOH AA 8 .    ? 16.447  15.671  85.527  1.00 33.06 ? 1418 HOH B O     1 
HETATM 18625 O O     . HOH AA 8 .    ? -5.545  -6.636  113.502 1.00 42.94 ? 1419 HOH B O     1 
HETATM 18626 O O     . HOH AA 8 .    ? 30.073  26.992  56.515  1.00 33.48 ? 1420 HOH B O     1 
HETATM 18627 O O     . HOH AA 8 .    ? -2.469  29.239  58.299  1.00 39.17 ? 1421 HOH B O     1 
HETATM 18628 O O     . HOH AA 8 .    ? 11.158  17.978  65.402  1.00 35.99 ? 1422 HOH B O     1 
HETATM 18629 O O     . HOH AA 8 .    ? 1.116   41.959  76.967  1.00 27.77 ? 1423 HOH B O     1 
HETATM 18630 O O     . HOH AA 8 .    ? 10.893  19.119  62.032  1.00 34.79 ? 1424 HOH B O     1 
HETATM 18631 O O     . HOH AA 8 .    ? 4.053   55.185  73.759  1.00 30.95 ? 1425 HOH B O     1 
HETATM 18632 O O     . HOH AA 8 .    ? -7.527  34.185  67.542  1.00 47.54 ? 1426 HOH B O     1 
HETATM 18633 O O     . HOH AA 8 .    ? -7.154  8.315   112.307 1.00 31.62 ? 1427 HOH B O     1 
HETATM 18634 O O     . HOH AA 8 .    ? -11.118 19.702  123.833 1.00 39.22 ? 1428 HOH B O     1 
HETATM 18635 O O     . HOH AA 8 .    ? 10.162  50.404  91.326  1.00 31.46 ? 1429 HOH B O     1 
HETATM 18636 O O     . HOH AA 8 .    ? 15.632  52.555  59.062  1.00 36.27 ? 1430 HOH B O     1 
HETATM 18637 O O     . HOH AA 8 .    ? 27.828  67.720  69.118  1.00 35.53 ? 1431 HOH B O     1 
HETATM 18638 O O     . HOH AA 8 .    ? 18.515  48.047  91.066  1.00 31.68 ? 1432 HOH B O     1 
HETATM 18639 O O     . HOH AA 8 .    ? 27.533  37.868  90.882  1.00 36.00 ? 1433 HOH B O     1 
HETATM 18640 O O     . HOH AA 8 .    ? 24.428  52.331  110.342 1.00 46.02 ? 1434 HOH B O     1 
HETATM 18641 O O     . HOH AA 8 .    ? -4.735  27.064  70.983  1.00 33.64 ? 1435 HOH B O     1 
HETATM 18642 O O     . HOH AA 8 .    ? 33.220  29.116  62.333  1.00 34.44 ? 1436 HOH B O     1 
HETATM 18643 O O     . HOH AA 8 .    ? 0.816   -0.443  97.228  1.00 44.15 ? 1437 HOH B O     1 
HETATM 18644 O O     . HOH AA 8 .    ? 15.169  40.291  74.025  1.00 25.14 ? 1438 HOH B O     1 
HETATM 18645 O O     . HOH AA 8 .    ? -5.210  42.573  73.349  1.00 33.23 ? 1439 HOH B O     1 
HETATM 18646 O O     . HOH AA 8 .    ? 27.695  41.730  83.947  1.00 48.14 ? 1440 HOH B O     1 
HETATM 18647 O O     . HOH AA 8 .    ? -15.526 47.196  115.390 1.00 41.71 ? 1441 HOH B O     1 
HETATM 18648 O O     . HOH AA 8 .    ? 16.676  52.637  64.831  1.00 39.73 ? 1442 HOH B O     1 
HETATM 18649 O O     . HOH AA 8 .    ? 3.602   14.000  73.289  1.00 43.35 ? 1443 HOH B O     1 
HETATM 18650 O O     . HOH AA 8 .    ? 9.168   25.927  55.797  1.00 31.53 ? 1444 HOH B O     1 
HETATM 18651 O O     . HOH AA 8 .    ? 13.397  9.956   92.541  1.00 30.96 ? 1445 HOH B O     1 
HETATM 18652 O O     . HOH AA 8 .    ? -5.887  37.185  78.456  1.00 29.68 ? 1446 HOH B O     1 
HETATM 18653 O O     . HOH AA 8 .    ? 3.757   7.701   93.299  1.00 32.17 ? 1447 HOH B O     1 
HETATM 18654 O O     . HOH AA 8 .    ? 5.972   25.178  87.182  1.00 32.61 ? 1448 HOH B O     1 
HETATM 18655 O O     . HOH AA 8 .    ? 1.509   57.281  88.409  1.00 39.96 ? 1449 HOH B O     1 
HETATM 18656 O O     . HOH AA 8 .    ? -7.340  -1.514  120.910 1.00 44.74 ? 1450 HOH B O     1 
HETATM 18657 O O     . HOH AA 8 .    ? 5.055   32.247  90.650  1.00 34.33 ? 1451 HOH B O     1 
HETATM 18658 O O     . HOH AA 8 .    ? -3.287  10.205  85.475  1.00 35.26 ? 1452 HOH B O     1 
HETATM 18659 O O     . HOH AA 8 .    ? 18.806  12.667  96.339  1.00 33.80 ? 1453 HOH B O     1 
HETATM 18660 O O     . HOH AA 8 .    ? 15.741  3.869   99.706  1.00 40.55 ? 1454 HOH B O     1 
HETATM 18661 O O     . HOH AA 8 .    ? 6.206   43.869  59.037  1.00 38.34 ? 1455 HOH B O     1 
HETATM 18662 O O     . HOH AA 8 .    ? -5.625  -7.486  117.019 1.00 39.50 ? 1456 HOH B O     1 
HETATM 18663 O O     . HOH AA 8 .    ? 22.863  34.811  116.772 1.00 35.80 ? 1457 HOH B O     1 
HETATM 18664 O O     . HOH AA 8 .    ? -17.054 4.824   117.791 1.00 40.41 ? 1458 HOH B O     1 
HETATM 18665 O O     . HOH AA 8 .    ? -4.296  64.210  81.993  1.00 22.88 ? 1459 HOH B O     1 
HETATM 18666 O O     . HOH AA 8 .    ? 29.170  69.239  80.665  1.00 29.29 ? 1460 HOH B O     1 
HETATM 18667 O O     . HOH AA 8 .    ? 7.080   33.760  87.409  1.00 28.11 ? 1461 HOH B O     1 
HETATM 18668 O O     . HOH AA 8 .    ? -6.340  50.970  73.907  1.00 20.91 ? 1462 HOH B O     1 
HETATM 18669 O O     . HOH AA 8 .    ? 10.109  50.708  65.584  1.00 32.49 ? 1463 HOH B O     1 
HETATM 18670 O O     . HOH AA 8 .    ? 31.619  54.013  68.658  1.00 32.65 ? 1464 HOH B O     1 
HETATM 18671 O O     . HOH AA 8 .    ? -13.300 53.844  123.612 1.00 39.98 ? 1465 HOH B O     1 
HETATM 18672 O O     . HOH AA 8 .    ? -2.749  62.923  86.329  1.00 28.46 ? 1466 HOH B O     1 
HETATM 18673 O O     . HOH AA 8 .    ? -2.695  4.552   86.119  1.00 36.97 ? 1467 HOH B O     1 
HETATM 18674 O O     . HOH AA 8 .    ? -2.380  42.003  62.558  1.00 31.92 ? 1468 HOH B O     1 
HETATM 18675 O O     . HOH AA 8 .    ? -5.548  5.059   123.464 1.00 38.68 ? 1469 HOH B O     1 
HETATM 18676 O O     . HOH AA 8 .    ? 2.852   17.990  90.431  1.00 36.99 ? 1470 HOH B O     1 
HETATM 18677 O O     . HOH AA 8 .    ? 4.155   -9.097  105.447 1.00 43.09 ? 1471 HOH B O     1 
HETATM 18678 O O     . HOH AA 8 .    ? 15.121  53.261  82.362  1.00 39.51 ? 1472 HOH B O     1 
HETATM 18679 O O     . HOH AA 8 .    ? -1.176  55.899  123.143 1.00 37.42 ? 1473 HOH B O     1 
HETATM 18680 O O     . HOH AA 8 .    ? 15.411  21.257  89.166  1.00 36.64 ? 1474 HOH B O     1 
HETATM 18681 O O     . HOH AA 8 .    ? 6.877   7.558   76.056  1.00 33.69 ? 1475 HOH B O     1 
HETATM 18682 O O     . HOH AA 8 .    ? 4.259   42.086  85.318  1.00 24.66 ? 1476 HOH B O     1 
HETATM 18683 O O     . HOH AA 8 .    ? 18.902  24.470  55.082  1.00 39.22 ? 1477 HOH B O     1 
HETATM 18684 O O     . HOH AA 8 .    ? -0.498  26.919  69.346  1.00 23.37 ? 1478 HOH B O     1 
HETATM 18685 O O     . HOH AA 8 .    ? 14.426  38.873  45.542  1.00 49.11 ? 1479 HOH B O     1 
HETATM 18686 O O     . HOH AA 8 .    ? 18.750  7.083   101.879 1.00 41.55 ? 1480 HOH B O     1 
HETATM 18687 O O     . HOH AA 8 .    ? 10.634  16.157  122.905 1.00 42.65 ? 1481 HOH B O     1 
HETATM 18688 O O     . HOH AA 8 .    ? 19.960  19.277  106.754 1.00 26.18 ? 1482 HOH B O     1 
HETATM 18689 O O     . HOH AA 8 .    ? 2.532   43.954  71.222  1.00 25.47 ? 1483 HOH B O     1 
HETATM 18690 O O     . HOH AA 8 .    ? 8.274   30.185  85.917  1.00 38.05 ? 1484 HOH B O     1 
HETATM 18691 O O     . HOH AA 8 .    ? -4.811  5.949   82.726  1.00 45.70 ? 1485 HOH B O     1 
HETATM 18692 O O     . HOH AA 8 .    ? 20.998  4.909   68.684  1.00 44.20 ? 1486 HOH B O     1 
HETATM 18693 O O     . HOH AA 8 .    ? 18.086  12.395  118.396 1.00 32.93 ? 1487 HOH B O     1 
HETATM 18694 O O     . HOH AA 8 .    ? -1.325  5.114   93.014  1.00 29.20 ? 1488 HOH B O     1 
HETATM 18695 O O     . HOH AA 8 .    ? 1.657   13.332  105.693 1.00 27.44 ? 1489 HOH B O     1 
HETATM 18696 O O     . HOH AA 8 .    ? -14.488 6.697   121.546 1.00 42.44 ? 1490 HOH B O     1 
HETATM 18697 O O     . HOH AA 8 .    ? -5.816  12.356  85.449  1.00 34.78 ? 1491 HOH B O     1 
HETATM 18698 O O     . HOH AA 8 .    ? 22.466  45.492  91.712  1.00 30.07 ? 1492 HOH B O     1 
HETATM 18699 O O     . HOH AA 8 .    ? 1.542   5.915   92.909  1.00 33.11 ? 1493 HOH B O     1 
HETATM 18700 O O     . HOH AA 8 .    ? 10.199  51.640  76.727  1.00 35.36 ? 1494 HOH B O     1 
HETATM 18701 O O     . HOH AA 8 .    ? 14.909  20.390  93.188  1.00 36.29 ? 1495 HOH B O     1 
HETATM 18702 O O     . HOH AA 8 .    ? -5.882  40.347  63.479  1.00 39.16 ? 1496 HOH B O     1 
HETATM 18703 O O     . HOH AA 8 .    ? -12.942 35.421  120.819 1.00 49.17 ? 1497 HOH B O     1 
HETATM 18704 O O     . HOH AA 8 .    ? -13.744 12.299  94.990  1.00 28.21 ? 1498 HOH B O     1 
HETATM 18705 O O     . HOH AA 8 .    ? 26.860  21.481  75.977  1.00 32.21 ? 1499 HOH B O     1 
HETATM 18706 O O     . HOH AA 8 .    ? 0.177   4.002   89.370  1.00 33.87 ? 1500 HOH B O     1 
HETATM 18707 O O     . HOH AA 8 .    ? -8.325  2.127   93.497  1.00 30.45 ? 1501 HOH B O     1 
HETATM 18708 O O     . HOH AA 8 .    ? 5.437   6.892   95.452  1.00 35.51 ? 1502 HOH B O     1 
HETATM 18709 O O     . HOH AA 8 .    ? -5.493  55.176  79.446  1.00 28.52 ? 1503 HOH B O     1 
HETATM 18710 O O     . HOH AA 8 .    ? 31.076  21.079  80.782  1.00 29.67 ? 1504 HOH B O     1 
HETATM 18711 O O     . HOH AA 8 .    ? 28.204  29.454  84.317  1.00 28.13 ? 1505 HOH B O     1 
HETATM 18712 O O     . HOH AA 8 .    ? 6.329   5.391   87.109  1.00 32.55 ? 1506 HOH B O     1 
HETATM 18713 O O     . HOH AA 8 .    ? 20.498  52.544  70.110  1.00 34.96 ? 1507 HOH B O     1 
HETATM 18714 O O     . HOH AA 8 .    ? -0.397  -10.480 116.482 1.00 39.01 ? 1508 HOH B O     1 
HETATM 18715 O O     . HOH AA 8 .    ? 17.338  40.536  72.350  1.00 23.89 ? 1509 HOH B O     1 
HETATM 18716 O O     . HOH AA 8 .    ? 25.180  35.199  74.421  1.00 32.03 ? 1510 HOH B O     1 
HETATM 18717 O O     . HOH AA 8 .    ? 7.579   48.952  107.766 1.00 26.82 ? 1511 HOH B O     1 
HETATM 18718 O O     . HOH AA 8 .    ? 0.014   18.491  81.431  1.00 30.88 ? 1512 HOH B O     1 
HETATM 18719 O O     . HOH AA 8 .    ? -0.903  50.099  58.742  1.00 36.35 ? 1513 HOH B O     1 
HETATM 18720 O O     . HOH AA 8 .    ? 5.391   35.912  49.713  1.00 38.14 ? 1514 HOH B O     1 
HETATM 18721 O O     . HOH AA 8 .    ? -6.733  52.435  108.308 1.00 34.28 ? 1515 HOH B O     1 
HETATM 18722 O O     . HOH AA 8 .    ? -12.695 19.692  84.848  1.00 31.56 ? 1516 HOH B O     1 
HETATM 18723 O O     . HOH AA 8 .    ? -2.389  39.398  88.202  1.00 22.51 ? 1517 HOH B O     1 
HETATM 18724 O O     . HOH AA 8 .    ? 6.456   15.082  125.690 1.00 39.25 ? 1518 HOH B O     1 
HETATM 18725 O O     . HOH AA 8 .    ? 1.667   12.910  102.964 1.00 29.79 ? 1519 HOH B O     1 
HETATM 18726 O O     . HOH AA 8 .    ? 6.638   5.434   93.324  1.00 34.93 ? 1520 HOH B O     1 
HETATM 18727 O O     . HOH AA 8 .    ? -2.346  23.935  77.185  1.00 27.80 ? 1521 HOH B O     1 
HETATM 18728 O O     . HOH AA 8 .    ? 1.167   -1.052  93.568  1.00 40.99 ? 1522 HOH B O     1 
HETATM 18729 O O     . HOH AA 8 .    ? -21.374 15.209  83.772  1.00 32.53 ? 1523 HOH B O     1 
HETATM 18730 O O     . HOH AA 8 .    ? -10.363 10.911  131.201 1.00 46.89 ? 1524 HOH B O     1 
HETATM 18731 O O     . HOH AA 8 .    ? 22.868  48.440  78.825  1.00 29.63 ? 1525 HOH B O     1 
HETATM 18732 O O     . HOH AA 8 .    ? -2.342  48.762  64.308  1.00 27.26 ? 1526 HOH B O     1 
HETATM 18733 O O     . HOH AA 8 .    ? -4.538  -2.461  98.014  1.00 38.80 ? 1527 HOH B O     1 
HETATM 18734 O O     . HOH AA 8 .    ? 28.197  13.096  87.028  1.00 44.04 ? 1528 HOH B O     1 
HETATM 18735 O O     . HOH AA 8 .    ? -3.406  -11.720 102.325 1.00 38.77 ? 1529 HOH B O     1 
HETATM 18736 O O     . HOH AA 8 .    ? -13.901 45.956  109.418 1.00 44.11 ? 1530 HOH B O     1 
HETATM 18737 O O     . HOH AA 8 .    ? 19.832  32.617  67.950  1.00 22.25 ? 1531 HOH B O     1 
HETATM 18738 O O     . HOH AA 8 .    ? 3.449   33.591  87.546  1.00 27.18 ? 1532 HOH B O     1 
HETATM 18739 O O     . HOH AA 8 .    ? 28.819  9.065   74.301  1.00 42.06 ? 1533 HOH B O     1 
HETATM 18740 O O     . HOH AA 8 .    ? 19.022  7.804   84.775  1.00 42.21 ? 1534 HOH B O     1 
HETATM 18741 O O     . HOH AA 8 .    ? 34.548  62.390  79.073  1.00 27.90 ? 1535 HOH B O     1 
HETATM 18742 O O     . HOH AA 8 .    ? 5.658   55.589  105.872 1.00 27.47 ? 1536 HOH B O     1 
HETATM 18743 O O     . HOH AA 8 .    ? 20.886  22.555  87.499  1.00 30.95 ? 1537 HOH B O     1 
HETATM 18744 O O     . HOH AA 8 .    ? 23.088  37.264  87.070  1.00 30.47 ? 1538 HOH B O     1 
HETATM 18745 O O     . HOH AA 8 .    ? 19.367  79.263  69.333  1.00 38.21 ? 1539 HOH B O     1 
HETATM 18746 O O     . HOH AA 8 .    ? -5.300  39.790  73.229  1.00 31.76 ? 1540 HOH B O     1 
HETATM 18747 O O     . HOH AA 8 .    ? 12.148  10.848  72.291  1.00 38.36 ? 1541 HOH B O     1 
HETATM 18748 O O     . HOH AA 8 .    ? 10.076  48.901  56.613  1.00 39.86 ? 1542 HOH B O     1 
HETATM 18749 O O     . HOH AA 8 .    ? -0.292  75.831  68.881  1.00 38.56 ? 1543 HOH B O     1 
HETATM 18750 O O     . HOH AA 8 .    ? 19.564  4.763   77.601  1.00 44.92 ? 1544 HOH B O     1 
HETATM 18751 O O     . HOH AA 8 .    ? -5.018  30.664  78.271  1.00 24.32 ? 1545 HOH B O     1 
HETATM 18752 O O     . HOH AA 8 .    ? 23.378  51.963  63.173  1.00 34.03 ? 1546 HOH B O     1 
HETATM 18753 O O     . HOH AA 8 .    ? 27.116  35.045  91.936  1.00 31.64 ? 1547 HOH B O     1 
HETATM 18754 O O     . HOH AA 8 .    ? 22.816  23.030  85.467  1.00 31.25 ? 1548 HOH B O     1 
HETATM 18755 O O     . HOH AA 8 .    ? -10.311 32.222  89.928  1.00 29.31 ? 1549 HOH B O     1 
HETATM 18756 O O     . HOH AA 8 .    ? 10.009  71.421  62.780  1.00 38.52 ? 1550 HOH B O     1 
HETATM 18757 O O     . HOH AA 8 .    ? -4.726  10.515  101.477 1.00 28.13 ? 1551 HOH B O     1 
HETATM 18758 O O     . HOH AA 8 .    ? 20.952  62.931  85.534  1.00 41.12 ? 1552 HOH B O     1 
HETATM 18759 O O     . HOH AA 8 .    ? 33.416  25.893  59.407  1.00 30.37 ? 1553 HOH B O     1 
HETATM 18760 O O     . HOH AA 8 .    ? 18.276  43.594  92.477  1.00 23.55 ? 1554 HOH B O     1 
HETATM 18761 O O     . HOH AA 8 .    ? 8.995   5.729   86.010  1.00 37.03 ? 1555 HOH B O     1 
HETATM 18762 O O     . HOH AA 8 .    ? -4.814  36.923  90.775  1.00 35.84 ? 1556 HOH B O     1 
HETATM 18763 O O     . HOH AA 8 .    ? 12.630  36.528  86.885  1.00 23.56 ? 1557 HOH B O     1 
HETATM 18764 O O     . HOH AA 8 .    ? 16.746  26.813  83.606  1.00 35.14 ? 1558 HOH B O     1 
HETATM 18765 O O     . HOH AA 8 .    ? 15.586  9.629   90.349  1.00 29.97 ? 1559 HOH B O     1 
HETATM 18766 O O     . HOH AA 8 .    ? 3.841   29.363  85.491  1.00 25.96 ? 1560 HOH B O     1 
HETATM 18767 O O     . HOH AA 8 .    ? 11.492  16.155  67.754  1.00 42.23 ? 1561 HOH B O     1 
HETATM 18768 O O     . HOH AA 8 .    ? -7.738  29.714  76.605  1.00 30.16 ? 1562 HOH B O     1 
HETATM 18769 O O     . HOH AA 8 .    ? 23.770  17.087  82.336  1.00 40.16 ? 1563 HOH B O     1 
HETATM 18770 O O     . HOH AA 8 .    ? 14.944  25.207  111.257 1.00 41.46 ? 1564 HOH B O     1 
HETATM 18771 O O     . HOH AA 8 .    ? 31.671  60.310  66.009  1.00 33.21 ? 1565 HOH B O     1 
HETATM 18772 O O     . HOH AA 8 .    ? 28.538  18.253  58.395  1.00 38.96 ? 1566 HOH B O     1 
HETATM 18773 O O     . HOH AA 8 .    ? 7.531   65.968  64.855  1.00 37.14 ? 1567 HOH B O     1 
HETATM 18774 O O     . HOH AA 8 .    ? 11.555  17.718  96.122  1.00 35.97 ? 1568 HOH B O     1 
HETATM 18775 O O     . HOH AA 8 .    ? -10.420 31.511  81.253  1.00 34.75 ? 1569 HOH B O     1 
HETATM 18776 O O     . HOH AA 8 .    ? -2.590  45.113  103.541 1.00 36.86 ? 1570 HOH B O     1 
HETATM 18777 O O     . HOH AA 8 .    ? 4.875   63.043  85.183  1.00 25.77 ? 1571 HOH B O     1 
HETATM 18778 O O     . HOH AA 8 .    ? -1.313  60.521  78.437  1.00 26.92 ? 1572 HOH B O     1 
HETATM 18779 O O     . HOH AA 8 .    ? 30.325  34.962  51.153  1.00 45.89 ? 1573 HOH B O     1 
HETATM 18780 O O     . HOH AA 8 .    ? 0.821   28.600  83.846  1.00 23.25 ? 1574 HOH B O     1 
HETATM 18781 O O     . HOH AA 8 .    ? 1.417   20.247  105.177 1.00 36.70 ? 1575 HOH B O     1 
HETATM 18782 O O     . HOH AA 8 .    ? -36.896 7.415   98.136  1.00 53.17 ? 1576 HOH B O     1 
HETATM 18783 O O     . HOH AA 8 .    ? -5.059  16.000  98.046  1.00 24.97 ? 1577 HOH B O     1 
HETATM 18784 O O     . HOH AA 8 .    ? 27.346  42.065  106.023 1.00 33.07 ? 1578 HOH B O     1 
HETATM 18785 O O     . HOH AA 8 .    ? 21.782  29.539  72.042  1.00 27.81 ? 1579 HOH B O     1 
HETATM 18786 O O     . HOH AA 8 .    ? 33.051  28.005  53.509  1.00 46.46 ? 1580 HOH B O     1 
HETATM 18787 O O     . HOH AA 8 .    ? -11.789 18.134  127.703 1.00 39.84 ? 1581 HOH B O     1 
HETATM 18788 O O     . HOH AA 8 .    ? -10.735 46.334  75.311  1.00 23.37 ? 1582 HOH B O     1 
HETATM 18789 O O     . HOH AA 8 .    ? 3.770   10.297  93.226  1.00 27.00 ? 1583 HOH B O     1 
HETATM 18790 O O     . HOH AA 8 .    ? 2.622   5.665   81.339  1.00 37.43 ? 1584 HOH B O     1 
HETATM 18791 O O     . HOH AA 8 .    ? 14.646  22.110  103.017 1.00 34.86 ? 1585 HOH B O     1 
HETATM 18792 O O     . HOH AA 8 .    ? 29.442  67.828  72.771  1.00 34.88 ? 1586 HOH B O     1 
HETATM 18793 O O     . HOH AA 8 .    ? 22.387  24.564  109.664 1.00 34.38 ? 1587 HOH B O     1 
HETATM 18794 O O     . HOH AA 8 .    ? -25.079 9.901   88.333  1.00 39.22 ? 1588 HOH B O     1 
HETATM 18795 O O     . HOH AA 8 .    ? 21.952  53.205  68.039  1.00 40.92 ? 1589 HOH B O     1 
HETATM 18796 O O     . HOH AA 8 .    ? -1.161  38.233  81.138  1.00 27.99 ? 1590 HOH B O     1 
HETATM 18797 O O     . HOH AA 8 .    ? -4.784  37.703  94.772  1.00 40.00 ? 1591 HOH B O     1 
HETATM 18798 O O     . HOH AA 8 .    ? -13.536 17.762  106.770 1.00 33.96 ? 1592 HOH B O     1 
HETATM 18799 O O     . HOH AA 8 .    ? 7.555   56.783  88.653  1.00 36.11 ? 1593 HOH B O     1 
HETATM 18800 O O     . HOH AA 8 .    ? 1.534   46.355  100.005 1.00 34.69 ? 1594 HOH B O     1 
HETATM 18801 O O     . HOH AA 8 .    ? 17.210  34.030  56.679  1.00 24.97 ? 1595 HOH B O     1 
HETATM 18802 O O     . HOH AA 8 .    ? -2.097  2.450   127.186 1.00 35.84 ? 1596 HOH B O     1 
HETATM 18803 O O     . HOH AA 8 .    ? 7.591   44.902  76.134  1.00 21.13 ? 1597 HOH B O     1 
HETATM 18804 O O     . HOH AA 8 .    ? 5.398   23.835  120.698 1.00 47.59 ? 1598 HOH B O     1 
HETATM 18805 O O     . HOH AA 8 .    ? -6.664  13.907  92.522  1.00 25.64 ? 1599 HOH B O     1 
HETATM 18806 O O     . HOH AA 8 .    ? 11.324  41.359  55.274  1.00 25.78 ? 1600 HOH B O     1 
HETATM 18807 O O     . HOH AA 8 .    ? -5.214  51.555  76.459  1.00 24.33 ? 1601 HOH B O     1 
HETATM 18808 O O     . HOH AA 8 .    ? 0.176   47.582  77.286  1.00 25.71 ? 1602 HOH B O     1 
HETATM 18809 O O     . HOH AA 8 .    ? 2.682   39.314  99.761  1.00 29.40 ? 1603 HOH B O     1 
HETATM 18810 O O     . HOH AA 8 .    ? -3.917  24.601  71.179  1.00 39.85 ? 1604 HOH B O     1 
HETATM 18811 O O     . HOH AA 8 .    ? 12.665  5.775   85.288  1.00 33.08 ? 1605 HOH B O     1 
HETATM 18812 O O     . HOH AA 8 .    ? 13.929  81.343  70.689  1.00 42.33 ? 1606 HOH B O     1 
HETATM 18813 O O     . HOH AA 8 .    ? -7.829  26.868  101.133 1.00 36.96 ? 1607 HOH B O     1 
HETATM 18814 O O     . HOH AA 8 .    ? 18.021  23.116  89.148  1.00 28.66 ? 1608 HOH B O     1 
HETATM 18815 O O     . HOH AA 8 .    ? 4.670   46.546  70.134  1.00 23.77 ? 1609 HOH B O     1 
HETATM 18816 O O     . HOH AA 8 .    ? 19.980  43.395  88.842  1.00 27.59 ? 1610 HOH B O     1 
HETATM 18817 O O     . HOH AA 8 .    ? 8.302   13.441  72.092  1.00 33.85 ? 1611 HOH B O     1 
HETATM 18818 O O     . HOH AA 8 .    ? 11.792  37.138  73.196  1.00 23.01 ? 1612 HOH B O     1 
HETATM 18819 O O     . HOH AA 8 .    ? 7.136   42.712  50.425  1.00 40.00 ? 1613 HOH B O     1 
HETATM 18820 O O     . HOH AA 8 .    ? 24.890  57.546  79.045  1.00 28.85 ? 1614 HOH B O     1 
HETATM 18821 O O     . HOH AA 8 .    ? 24.057  25.771  51.310  1.00 31.86 ? 1615 HOH B O     1 
HETATM 18822 O O     . HOH AA 8 .    ? 30.601  40.163  57.612  1.00 38.94 ? 1616 HOH B O     1 
HETATM 18823 O O     . HOH AA 8 .    ? 5.867   14.816  95.621  1.00 26.50 ? 1617 HOH B O     1 
HETATM 18824 O O     . HOH AA 8 .    ? -1.406  32.523  69.885  1.00 22.16 ? 1618 HOH B O     1 
HETATM 18825 O O     . HOH AA 8 .    ? -9.755  5.455   88.103  1.00 35.41 ? 1619 HOH B O     1 
HETATM 18826 O O     . HOH AA 8 .    ? 13.989  26.542  83.107  1.00 33.64 ? 1620 HOH B O     1 
HETATM 18827 O O     . HOH AA 8 .    ? 0.342   -7.631  108.023 1.00 40.94 ? 1621 HOH B O     1 
HETATM 18828 O O     . HOH AA 8 .    ? 33.848  67.806  81.460  1.00 30.34 ? 1622 HOH B O     1 
HETATM 18829 O O     . HOH AA 8 .    ? -13.652 11.508  92.151  1.00 28.78 ? 1623 HOH B O     1 
HETATM 18830 O O     . HOH AA 8 .    ? -6.116  39.197  107.756 1.00 39.41 ? 1624 HOH B O     1 
HETATM 18831 O O     . HOH AA 8 .    ? 20.694  27.228  71.662  1.00 22.97 ? 1625 HOH B O     1 
HETATM 18832 O O     . HOH AA 8 .    ? -8.860  23.943  77.894  1.00 35.36 ? 1626 HOH B O     1 
HETATM 18833 O O     . HOH AA 8 .    ? -6.675  11.358  129.270 1.00 47.74 ? 1627 HOH B O     1 
HETATM 18834 O O     . HOH AA 8 .    ? 0.880   55.546  111.447 1.00 32.93 ? 1628 HOH B O     1 
HETATM 18835 O O     . HOH AA 8 .    ? 11.314  20.090  121.641 1.00 42.92 ? 1629 HOH B O     1 
HETATM 18836 O O     . HOH AA 8 .    ? 12.574  1.609   112.418 1.00 39.16 ? 1630 HOH B O     1 
HETATM 18837 O O     . HOH AA 8 .    ? 11.720  26.055  103.148 1.00 34.56 ? 1631 HOH B O     1 
HETATM 18838 O O     . HOH AA 8 .    ? 22.845  67.342  65.377  1.00 37.46 ? 1632 HOH B O     1 
HETATM 18839 O O     . HOH AA 8 .    ? 4.877   49.351  69.688  1.00 29.06 ? 1633 HOH B O     1 
HETATM 18840 O O     . HOH AA 8 .    ? 31.414  28.887  78.745  1.00 41.24 ? 1634 HOH B O     1 
HETATM 18841 O O     . HOH AA 8 .    ? 28.388  25.309  68.167  1.00 29.14 ? 1635 HOH B O     1 
HETATM 18842 O O     . HOH AA 8 .    ? 2.272   41.635  54.757  1.00 33.82 ? 1636 HOH B O     1 
HETATM 18843 O O     . HOH AA 8 .    ? 0.392   19.908  70.523  1.00 28.10 ? 1637 HOH B O     1 
HETATM 18844 O O     . HOH AA 8 .    ? 9.705   43.429  111.264 1.00 35.28 ? 1638 HOH B O     1 
HETATM 18845 O O     . HOH AA 8 .    ? 1.062   30.444  75.627  1.00 26.18 ? 1639 HOH B O     1 
HETATM 18846 O O     . HOH AA 8 .    ? 18.279  14.821  98.620  1.00 32.22 ? 1640 HOH B O     1 
HETATM 18847 O O     . HOH AA 8 .    ? 0.796   38.631  109.352 1.00 34.54 ? 1641 HOH B O     1 
HETATM 18848 O O     . HOH AA 8 .    ? -29.030 17.165  118.778 1.00 46.55 ? 1642 HOH B O     1 
HETATM 18849 O O     . HOH AA 8 .    ? 2.778   11.371  95.509  1.00 31.69 ? 1643 HOH B O     1 
HETATM 18850 O O     . HOH AA 8 .    ? 15.271  55.850  75.294  1.00 32.32 ? 1644 HOH B O     1 
HETATM 18851 O O     . HOH AA 8 .    ? -10.609 1.305   92.274  1.00 33.66 ? 1645 HOH B O     1 
HETATM 18852 O O     . HOH AA 8 .    ? 35.147  16.065  63.316  1.00 46.41 ? 1646 HOH B O     1 
HETATM 18853 O O     . HOH AA 8 .    ? -1.249  55.390  73.145  1.00 33.69 ? 1647 HOH B O     1 
HETATM 18854 O O     . HOH AA 8 .    ? 23.532  2.110   82.570  1.00 52.72 ? 1648 HOH B O     1 
HETATM 18855 O O     . HOH AA 8 .    ? -11.446 20.178  89.085  1.00 27.57 ? 1649 HOH B O     1 
HETATM 18856 O O     . HOH AA 8 .    ? 18.313  23.531  111.681 1.00 36.67 ? 1650 HOH B O     1 
HETATM 18857 O O     . HOH AA 8 .    ? 17.365  42.684  80.608  1.00 32.72 ? 1651 HOH B O     1 
HETATM 18858 O O     . HOH AA 8 .    ? 24.235  68.923  68.246  1.00 32.67 ? 1652 HOH B O     1 
HETATM 18859 O O     . HOH AA 8 .    ? 19.033  30.538  89.626  1.00 25.77 ? 1653 HOH B O     1 
HETATM 18860 O O     . HOH AA 8 .    ? 2.598   30.447  81.094  1.00 25.94 ? 1654 HOH B O     1 
HETATM 18861 O O     . HOH AA 8 .    ? 14.727  40.821  78.279  1.00 27.39 ? 1655 HOH B O     1 
HETATM 18862 O O     . HOH AA 8 .    ? 12.527  37.125  108.908 1.00 31.17 ? 1656 HOH B O     1 
HETATM 18863 O O     . HOH AA 8 .    ? 2.340   70.351  65.100  1.00 40.19 ? 1657 HOH B O     1 
HETATM 18864 O O     . HOH AA 8 .    ? 23.277  11.934  68.531  1.00 32.78 ? 1658 HOH B O     1 
HETATM 18865 O O     . HOH AA 8 .    ? 33.330  19.059  88.353  1.00 32.63 ? 1659 HOH B O     1 
HETATM 18866 O O     . HOH AA 8 .    ? 18.663  13.057  74.749  1.00 37.46 ? 1660 HOH B O     1 
HETATM 18867 O O     . HOH AA 8 .    ? -2.573  21.148  92.488  1.00 22.32 ? 1661 HOH B O     1 
HETATM 18868 O O     . HOH AA 8 .    ? 9.404   29.010  99.444  1.00 36.74 ? 1662 HOH B O     1 
HETATM 18869 O O     . HOH AA 8 .    ? 5.036   57.787  69.879  1.00 29.05 ? 1663 HOH B O     1 
HETATM 18870 O O     . HOH AA 8 .    ? 12.426  21.247  102.547 1.00 38.84 ? 1664 HOH B O     1 
HETATM 18871 O O     . HOH AA 8 .    ? -8.036  12.143  98.137  1.00 27.07 ? 1665 HOH B O     1 
HETATM 18872 O O     . HOH AA 8 .    ? -4.164  18.324  99.139  1.00 23.43 ? 1666 HOH B O     1 
HETATM 18873 O O     . HOH AA 8 .    ? 13.467  25.708  97.259  1.00 38.37 ? 1667 HOH B O     1 
HETATM 18874 O O     . HOH AA 8 .    ? 23.562  32.642  92.550  1.00 25.74 ? 1668 HOH B O     1 
HETATM 18875 O O     . HOH AA 8 .    ? -5.034  9.408   116.239 1.00 37.50 ? 1669 HOH B O     1 
HETATM 18876 O O     . HOH AA 8 .    ? 37.659  37.379  86.047  1.00 47.79 ? 1670 HOH B O     1 
HETATM 18877 O O     . HOH AA 8 .    ? 26.503  39.743  53.474  1.00 37.91 ? 1671 HOH B O     1 
HETATM 18878 O O     . HOH AA 8 .    ? -1.180  50.936  65.834  1.00 27.73 ? 1672 HOH B O     1 
HETATM 18879 O O     . HOH AA 8 .    ? 34.660  24.896  71.569  1.00 52.66 ? 1673 HOH B O     1 
HETATM 18880 O O     . HOH AA 8 .    ? 17.205  54.786  98.395  1.00 30.95 ? 1674 HOH B O     1 
HETATM 18881 O O     . HOH AA 8 .    ? 1.667   76.272  85.597  1.00 44.58 ? 1675 HOH B O     1 
HETATM 18882 O O     . HOH AA 8 .    ? 10.313  52.458  105.697 1.00 41.85 ? 1676 HOH B O     1 
HETATM 18883 O O     . HOH AA 8 .    ? 8.195   31.657  94.850  1.00 32.61 ? 1677 HOH B O     1 
HETATM 18884 O O     . HOH AA 8 .    ? 2.690   48.978  77.031  1.00 25.93 ? 1678 HOH B O     1 
HETATM 18885 O O     . HOH AA 8 .    ? 27.322  22.733  89.424  1.00 26.02 ? 1679 HOH B O     1 
HETATM 18886 O O     . HOH AA 8 .    ? -6.243  -0.005  87.051  1.00 37.00 ? 1680 HOH B O     1 
HETATM 18887 O O     . HOH AA 8 .    ? 30.757  35.718  71.362  1.00 45.03 ? 1681 HOH B O     1 
HETATM 18888 O O     . HOH AA 8 .    ? 2.383   63.256  79.282  1.00 21.08 ? 1682 HOH B O     1 
HETATM 18889 O O     . HOH AA 8 .    ? 2.737   32.562  79.339  1.00 21.96 ? 1683 HOH B O     1 
HETATM 18890 O O     . HOH AA 8 .    ? 19.850  18.725  66.910  1.00 23.94 ? 1684 HOH B O     1 
HETATM 18891 O O     . HOH AA 8 .    ? -5.733  35.298  88.680  1.00 37.07 ? 1685 HOH B O     1 
HETATM 18892 O O     . HOH AA 8 .    ? 26.976  49.367  95.883  1.00 40.73 ? 1686 HOH B O     1 
HETATM 18893 O O     . HOH AA 8 .    ? 39.895  29.015  88.949  1.00 37.34 ? 1687 HOH B O     1 
HETATM 18894 O O     . HOH AA 8 .    ? -7.154  27.823  75.101  1.00 36.24 ? 1688 HOH B O     1 
HETATM 18895 O O     . HOH AA 8 .    ? -24.965 16.352  83.142  1.00 42.62 ? 1689 HOH B O     1 
HETATM 18896 O O     . HOH AA 8 .    ? 19.651  28.387  82.972  1.00 34.88 ? 1690 HOH B O     1 
HETATM 18897 O O     . HOH AA 8 .    ? -1.956  10.935  102.428 1.00 28.03 ? 1691 HOH B O     1 
HETATM 18898 O O     . HOH AA 8 .    ? -23.867 22.907  85.421  1.00 44.15 ? 1692 HOH B O     1 
HETATM 18899 O O     . HOH AA 8 .    ? 16.139  48.363  71.835  1.00 25.11 ? 1693 HOH B O     1 
HETATM 18900 O O     . HOH AA 8 .    ? -14.708 5.620   118.596 1.00 39.99 ? 1694 HOH B O     1 
HETATM 18901 O O     . HOH AA 8 .    ? -6.292  12.286  100.202 1.00 25.63 ? 1695 HOH B O     1 
HETATM 18902 O O     . HOH AA 8 .    ? 16.509  21.553  100.952 1.00 33.38 ? 1696 HOH B O     1 
HETATM 18903 O O     . HOH AA 8 .    ? 19.463  54.924  94.617  1.00 37.63 ? 1697 HOH B O     1 
HETATM 18904 O O     . HOH AA 8 .    ? -1.858  25.018  80.704  1.00 29.87 ? 1698 HOH B O     1 
HETATM 18905 O O     . HOH AA 8 .    ? 18.628  22.994  85.639  1.00 28.51 ? 1699 HOH B O     1 
HETATM 18906 O O     . HOH AA 8 .    ? 4.689   47.475  88.031  1.00 22.62 ? 1700 HOH B O     1 
HETATM 18907 O O     . HOH AA 8 .    ? -0.630  23.747  74.839  1.00 25.08 ? 1701 HOH B O     1 
HETATM 18908 O O     . HOH AA 8 .    ? 6.086   57.417  61.597  1.00 46.03 ? 1702 HOH B O     1 
HETATM 18909 O O     . HOH AA 8 .    ? 29.373  9.373   93.231  1.00 48.36 ? 1703 HOH B O     1 
HETATM 18910 O O     . HOH AA 8 .    ? 9.928   1.930   118.611 1.00 36.26 ? 1704 HOH B O     1 
HETATM 18911 O O     . HOH AA 8 .    ? 12.987  16.750  89.958  1.00 38.28 ? 1705 HOH B O     1 
HETATM 18912 O O     . HOH AA 8 .    ? -2.384  18.051  106.956 1.00 35.35 ? 1706 HOH B O     1 
HETATM 18913 O O     . HOH AA 8 .    ? -9.483  18.843  81.805  1.00 41.57 ? 1707 HOH B O     1 
HETATM 18914 O O     . HOH AA 8 .    ? 6.557   16.121  122.652 1.00 39.67 ? 1708 HOH B O     1 
HETATM 18915 O O     . HOH AA 8 .    ? 24.637  15.965  96.237  1.00 38.98 ? 1709 HOH B O     1 
HETATM 18916 O O     . HOH AA 8 .    ? 4.710   18.466  125.004 1.00 38.82 ? 1710 HOH B O     1 
HETATM 18917 O O     . HOH AA 8 .    ? -9.345  9.832   124.350 1.00 37.51 ? 1711 HOH B O     1 
HETATM 18918 O O     . HOH AA 8 .    ? 17.494  48.929  59.946  1.00 28.76 ? 1712 HOH B O     1 
HETATM 18919 O O     . HOH AA 8 .    ? -19.695 28.474  89.030  1.00 34.32 ? 1713 HOH B O     1 
HETATM 18920 O O     . HOH AA 8 .    ? 1.821   40.334  115.501 1.00 35.82 ? 1714 HOH B O     1 
HETATM 18921 O O     . HOH AA 8 .    ? 5.239   42.612  71.675  1.00 21.00 ? 1715 HOH B O     1 
HETATM 18922 O O     . HOH AA 8 .    ? 4.878   17.728  92.154  1.00 31.03 ? 1716 HOH B O     1 
HETATM 18923 O O     . HOH AA 8 .    ? 11.956  11.568  122.593 1.00 36.33 ? 1717 HOH B O     1 
HETATM 18924 O O     . HOH AA 8 .    ? -1.152  66.874  85.039  1.00 32.46 ? 1718 HOH B O     1 
HETATM 18925 O O     . HOH AA 8 .    ? 36.195  38.122  92.226  1.00 40.26 ? 1719 HOH B O     1 
HETATM 18926 O O     . HOH AA 8 .    ? 18.296  67.116  59.040  1.00 34.39 ? 1720 HOH B O     1 
HETATM 18927 O O     . HOH AA 8 .    ? -8.896  23.826  101.864 1.00 23.01 ? 1721 HOH B O     1 
HETATM 18928 O O     . HOH AA 8 .    ? 33.123  46.250  67.769  1.00 36.75 ? 1722 HOH B O     1 
HETATM 18929 O O     . HOH AA 8 .    ? 31.899  59.310  72.897  1.00 32.21 ? 1723 HOH B O     1 
HETATM 18930 O O     . HOH AA 8 .    ? -1.449  67.298  76.327  1.00 33.73 ? 1724 HOH B O     1 
HETATM 18931 O O     . HOH AA 8 .    ? 4.851   21.695  84.758  1.00 26.83 ? 1725 HOH B O     1 
HETATM 18932 O O     . HOH AA 8 .    ? 5.367   43.060  56.485  1.00 35.18 ? 1726 HOH B O     1 
HETATM 18933 O O     . HOH AA 8 .    ? 13.020  48.064  82.867  1.00 32.86 ? 1727 HOH B O     1 
HETATM 18934 O O     . HOH AA 8 .    ? -1.950  36.597  88.341  1.00 26.67 ? 1728 HOH B O     1 
HETATM 18935 O O     . HOH AA 8 .    ? -7.525  23.912  126.268 1.00 41.14 ? 1729 HOH B O     1 
HETATM 18936 O O     . HOH AA 8 .    ? 23.342  48.421  107.825 1.00 35.90 ? 1730 HOH B O     1 
HETATM 18937 O O     . HOH AA 8 .    ? -3.444  52.331  83.436  1.00 30.32 ? 1731 HOH B O     1 
HETATM 18938 O O     . HOH AA 8 .    ? 22.549  54.359  94.046  1.00 36.45 ? 1732 HOH B O     1 
HETATM 18939 O O     . HOH AA 8 .    ? 1.120   38.529  106.752 1.00 38.94 ? 1733 HOH B O     1 
HETATM 18940 O O     . HOH AA 8 .    ? 23.340  72.898  82.453  1.00 37.24 ? 1734 HOH B O     1 
HETATM 18941 O O     . HOH AA 8 .    ? 27.216  59.004  79.261  1.00 30.09 ? 1735 HOH B O     1 
HETATM 18942 O O     . HOH AA 8 .    ? 31.854  62.220  75.888  1.00 29.03 ? 1736 HOH B O     1 
HETATM 18943 O O     . HOH AA 8 .    ? 14.710  16.535  92.774  1.00 33.85 ? 1737 HOH B O     1 
HETATM 18944 O O     . HOH AA 8 .    ? 18.148  22.835  61.875  1.00 28.37 ? 1738 HOH B O     1 
HETATM 18945 O O     . HOH AA 8 .    ? -22.506 20.491  89.298  1.00 39.90 ? 1739 HOH B O     1 
HETATM 18946 O O     . HOH AA 8 .    ? 10.696  29.266  95.323  1.00 31.28 ? 1740 HOH B O     1 
HETATM 18947 O O     . HOH AA 8 .    ? 3.037   35.236  122.366 1.00 37.44 ? 1741 HOH B O     1 
HETATM 18948 O O     . HOH AA 8 .    ? 18.296  52.478  67.513  1.00 37.49 ? 1742 HOH B O     1 
HETATM 18949 O O     . HOH AA 8 .    ? 3.886   19.269  61.041  1.00 39.85 ? 1743 HOH B O     1 
HETATM 18950 O O     . HOH AA 8 .    ? 20.166  50.768  78.508  1.00 32.29 ? 1744 HOH B O     1 
HETATM 18951 O O     . HOH AA 8 .    ? -14.357 54.293  119.338 1.00 33.73 ? 1745 HOH B O     1 
HETATM 18952 O O     . HOH AA 8 .    ? 6.559   11.631  127.682 1.00 29.35 ? 1746 HOH B O     1 
HETATM 18953 O O     . HOH AA 8 .    ? 9.136   62.121  86.223  1.00 29.58 ? 1747 HOH B O     1 
HETATM 18954 O O     . HOH AA 8 .    ? 33.196  57.996  75.084  1.00 37.12 ? 1748 HOH B O     1 
HETATM 18955 O O     . HOH AA 8 .    ? 4.794   -0.080  87.953  1.00 43.90 ? 1749 HOH B O     1 
HETATM 18956 O O     . HOH AA 8 .    ? 1.079   42.364  99.461  1.00 40.36 ? 1750 HOH B O     1 
HETATM 18957 O O     . HOH AA 8 .    ? 25.781  33.170  70.979  1.00 35.01 ? 1751 HOH B O     1 
HETATM 18958 O O     . HOH AA 8 .    ? 0.275   12.029  94.714  1.00 23.38 ? 1752 HOH B O     1 
HETATM 18959 O O     . HOH AA 8 .    ? 8.443   37.357  80.208  1.00 23.88 ? 1753 HOH B O     1 
HETATM 18960 O O     . HOH AA 8 .    ? 5.115   69.454  64.229  1.00 40.74 ? 1754 HOH B O     1 
HETATM 18961 O O     . HOH AA 8 .    ? 11.669  45.074  110.195 1.00 40.78 ? 1755 HOH B O     1 
HETATM 18962 O O     . HOH AA 8 .    ? 28.317  31.285  73.975  1.00 38.85 ? 1756 HOH B O     1 
HETATM 18963 O O     . HOH AA 8 .    ? -2.521  14.244  99.758  1.00 25.60 ? 1757 HOH B O     1 
HETATM 18964 O O     . HOH AA 8 .    ? -0.130  17.753  92.433  1.00 30.63 ? 1758 HOH B O     1 
HETATM 18965 O O     . HOH AA 8 .    ? -3.659  45.832  107.828 1.00 31.99 ? 1759 HOH B O     1 
HETATM 18966 O O     . HOH AA 8 .    ? 21.066  37.272  113.721 1.00 30.43 ? 1760 HOH B O     1 
HETATM 18967 O O     . HOH AA 8 .    ? 8.446   40.683  87.839  1.00 20.70 ? 1761 HOH B O     1 
HETATM 18968 O O     . HOH AA 8 .    ? 18.703  62.117  58.223  1.00 40.65 ? 1762 HOH B O     1 
HETATM 18969 O O     . HOH AA 8 .    ? 6.562   31.748  80.222  1.00 28.13 ? 1763 HOH B O     1 
HETATM 18970 O O     . HOH AA 8 .    ? 7.651   39.979  47.239  1.00 42.71 ? 1764 HOH B O     1 
HETATM 18971 O O     . HOH AA 8 .    ? 7.777   62.810  67.193  1.00 42.18 ? 1765 HOH B O     1 
HETATM 18972 O O     . HOH AA 8 .    ? -2.873  30.988  64.225  1.00 31.28 ? 1766 HOH B O     1 
HETATM 18973 O O     . HOH AA 8 .    ? -2.931  10.736  104.883 1.00 27.81 ? 1767 HOH B O     1 
HETATM 18974 O O     . HOH AA 8 .    ? 8.996   3.304   81.870  1.00 38.23 ? 1768 HOH B O     1 
HETATM 18975 O O     . HOH AA 8 .    ? 0.058   19.185  94.972  1.00 23.12 ? 1769 HOH B O     1 
HETATM 18976 O O     . HOH AA 8 .    ? -1.114  20.508  90.539  1.00 25.75 ? 1770 HOH B O     1 
HETATM 18977 O O     . HOH AA 8 .    ? -5.633  46.383  84.910  1.00 31.15 ? 1771 HOH B O     1 
HETATM 18978 O O     . HOH AA 8 .    ? 7.814   58.077  86.426  1.00 26.53 ? 1772 HOH B O     1 
HETATM 18979 O O     . HOH AA 8 .    ? -0.176  28.701  97.509  1.00 29.82 ? 1773 HOH B O     1 
HETATM 18980 O O     . HOH AA 8 .    ? -4.275  -0.628  111.674 1.00 37.92 ? 1774 HOH B O     1 
HETATM 18981 O O     . HOH AA 8 .    ? -12.184 7.480   128.814 1.00 46.08 ? 1775 HOH B O     1 
HETATM 18982 O O     . HOH AA 8 .    ? -9.037  33.478  69.996  1.00 45.76 ? 1776 HOH B O     1 
HETATM 18983 O O     . HOH AA 8 .    ? -6.365  34.348  84.750  1.00 31.01 ? 1777 HOH B O     1 
HETATM 18984 O O     . HOH AA 8 .    ? 12.216  7.425   91.397  1.00 30.36 ? 1778 HOH B O     1 
HETATM 18985 O O     . HOH AA 8 .    ? 4.461   77.952  81.237  1.00 34.08 ? 1779 HOH B O     1 
HETATM 18986 O O     . HOH AA 8 .    ? 28.870  22.590  77.119  1.00 28.00 ? 1780 HOH B O     1 
HETATM 18987 O O     . HOH AA 8 .    ? 1.601   15.015  83.248  1.00 28.72 ? 1781 HOH B O     1 
HETATM 18988 O O     . HOH AA 8 .    ? 16.026  53.283  106.173 1.00 33.93 ? 1782 HOH B O     1 
HETATM 18989 O O     . HOH AA 8 .    ? 1.242   9.140   90.625  1.00 32.86 ? 1783 HOH B O     1 
HETATM 18990 O O     . HOH AA 8 .    ? 4.098   19.485  98.217  1.00 37.11 ? 1784 HOH B O     1 
HETATM 18991 O O     . HOH AA 8 .    ? 14.633  42.363  75.921  1.00 25.91 ? 1785 HOH B O     1 
HETATM 18992 O O     . HOH AA 8 .    ? -6.651  6.162   119.735 1.00 35.15 ? 1786 HOH B O     1 
HETATM 18993 O O     . HOH AA 8 .    ? 19.564  15.768  64.109  1.00 30.53 ? 1787 HOH B O     1 
HETATM 18994 O O     . HOH AA 8 .    ? 0.637   -8.253  110.415 1.00 42.94 ? 1788 HOH B O     1 
HETATM 18995 O O     . HOH AA 8 .    ? 24.770  50.965  67.629  1.00 33.31 ? 1789 HOH B O     1 
HETATM 18996 O O     . HOH AA 8 .    ? 3.154   40.634  118.325 1.00 39.02 ? 1790 HOH B O     1 
HETATM 18997 O O     . HOH AA 8 .    ? 21.299  53.974  84.483  1.00 41.29 ? 1791 HOH B O     1 
HETATM 18998 O O     . HOH AA 8 .    ? -7.139  45.069  81.859  1.00 48.04 ? 1792 HOH B O     1 
HETATM 18999 O O     . HOH AA 8 .    ? 4.534   32.119  131.491 1.00 51.70 ? 1793 HOH B O     1 
HETATM 19000 O O     . HOH AA 8 .    ? 26.403  12.509  88.803  1.00 41.28 ? 1794 HOH B O     1 
HETATM 19001 O O     . HOH AA 8 .    ? 15.646  48.792  58.039  1.00 30.10 ? 1795 HOH B O     1 
HETATM 19002 O O     . HOH AA 8 .    ? 37.681  30.821  82.698  1.00 39.43 ? 1796 HOH B O     1 
HETATM 19003 O O     . HOH AA 8 .    ? -2.606  59.920  120.987 1.00 35.68 ? 1797 HOH B O     1 
HETATM 19004 O O     . HOH AA 8 .    ? 17.105  33.570  49.199  1.00 34.19 ? 1798 HOH B O     1 
HETATM 19005 O O     . HOH AA 8 .    ? 5.889   18.475  88.152  1.00 31.91 ? 1799 HOH B O     1 
HETATM 19006 O O     . HOH AA 8 .    ? 32.824  36.990  105.890 1.00 44.52 ? 1800 HOH B O     1 
HETATM 19007 O O     . HOH AA 8 .    ? 0.334   26.818  95.785  1.00 25.60 ? 1801 HOH B O     1 
HETATM 19008 O O     . HOH AA 8 .    ? 29.114  31.138  71.755  1.00 37.21 ? 1802 HOH B O     1 
HETATM 19009 O O     . HOH AA 8 .    ? -15.398 9.907   90.867  1.00 30.43 ? 1803 HOH B O     1 
HETATM 19010 O O     . HOH AA 8 .    ? 23.005  51.223  66.087  1.00 31.93 ? 1804 HOH B O     1 
HETATM 19011 O O     . HOH AA 8 .    ? -7.528  8.539   83.036  1.00 46.88 ? 1805 HOH B O     1 
HETATM 19012 O O     . HOH AA 8 .    ? 3.021   31.144  99.354  1.00 32.33 ? 1806 HOH B O     1 
HETATM 19013 O O     . HOH AA 8 .    ? 26.566  27.206  67.626  1.00 27.78 ? 1807 HOH B O     1 
HETATM 19014 O O     . HOH AA 8 .    ? 0.819   28.492  125.865 1.00 52.14 ? 1808 HOH B O     1 
HETATM 19015 O O     . HOH AA 8 .    ? 11.964  20.673  59.353  1.00 26.35 ? 1809 HOH B O     1 
HETATM 19016 O O     . HOH AA 8 .    ? 11.778  49.671  89.600  1.00 29.22 ? 1810 HOH B O     1 
HETATM 19017 O O     . HOH AA 8 .    ? 35.345  32.350  55.590  1.00 40.19 ? 1811 HOH B O     1 
HETATM 19018 O O     . HOH AA 8 .    ? 34.057  18.212  71.779  1.00 43.60 ? 1812 HOH B O     1 
HETATM 19019 O O     . HOH AA 8 .    ? 10.546  33.613  110.577 1.00 38.15 ? 1813 HOH B O     1 
HETATM 19020 O O     . HOH AA 8 .    ? -2.982  33.750  63.347  1.00 29.82 ? 1814 HOH B O     1 
HETATM 19021 O O     . HOH AA 8 .    ? 25.109  23.663  82.489  1.00 26.54 ? 1815 HOH B O     1 
HETATM 19022 O O     . HOH AA 8 .    ? 1.214   10.670  130.688 1.00 37.04 ? 1816 HOH B O     1 
HETATM 19023 O O     . HOH AA 8 .    ? 33.782  36.982  83.898  1.00 48.38 ? 1817 HOH B O     1 
HETATM 19024 O O     . HOH AA 8 .    ? 35.660  12.652  91.810  1.00 47.87 ? 1818 HOH B O     1 
HETATM 19025 O O     . HOH AA 8 .    ? 7.862   65.842  69.380  1.00 38.52 ? 1819 HOH B O     1 
HETATM 19026 O O     . HOH AA 8 .    ? 22.336  14.106  81.456  1.00 36.06 ? 1820 HOH B O     1 
HETATM 19027 O O     . HOH AA 8 .    ? 17.615  33.644  69.144  1.00 21.35 ? 1821 HOH B O     1 
HETATM 19028 O O     . HOH AA 8 .    ? 9.968   66.944  87.412  1.00 44.65 ? 1822 HOH B O     1 
HETATM 19029 O O     . HOH AA 8 .    ? -8.725  31.394  87.796  1.00 23.24 ? 1823 HOH B O     1 
HETATM 19030 O O     . HOH AA 8 .    ? -5.562  22.824  81.724  1.00 29.41 ? 1824 HOH B O     1 
HETATM 19031 O O     . HOH AA 8 .    ? 15.952  38.035  75.477  1.00 24.79 ? 1825 HOH B O     1 
HETATM 19032 O O     . HOH AA 8 .    ? -14.200 9.102   88.449  1.00 34.03 ? 1826 HOH B O     1 
HETATM 19033 O O     . HOH AA 8 .    ? -2.892  39.801  58.688  1.00 32.00 ? 1827 HOH B O     1 
HETATM 19034 O O     . HOH AA 8 .    ? 14.989  57.214  72.589  1.00 35.52 ? 1828 HOH B O     1 
HETATM 19035 O O     . HOH AA 8 .    ? -2.162  57.733  75.965  1.00 24.52 ? 1829 HOH B O     1 
HETATM 19036 O O     . HOH AA 8 .    ? 8.669   35.385  103.807 1.00 35.22 ? 1830 HOH B O     1 
HETATM 19037 O O     . HOH AA 8 .    ? -0.814  13.214  101.797 1.00 26.84 ? 1831 HOH B O     1 
HETATM 19038 O O     . HOH AA 8 .    ? 7.858   20.375  103.192 1.00 37.23 ? 1832 HOH B O     1 
HETATM 19039 O O     . HOH AA 8 .    ? -11.163 35.991  77.191  1.00 40.72 ? 1833 HOH B O     1 
HETATM 19040 O O     . HOH AA 8 .    ? 33.560  33.362  70.830  1.00 43.50 ? 1834 HOH B O     1 
HETATM 19041 O O     . HOH AA 8 .    ? 16.391  69.560  55.920  1.00 48.88 ? 1835 HOH B O     1 
HETATM 19042 O O     . HOH AA 8 .    ? 2.654   53.427  70.060  1.00 34.28 ? 1836 HOH B O     1 
HETATM 19043 O O     . HOH AA 8 .    ? 5.361   3.036   94.116  1.00 37.13 ? 1837 HOH B O     1 
HETATM 19044 O O     . HOH AA 8 .    ? -16.156 4.120   93.705  1.00 46.99 ? 1838 HOH B O     1 
HETATM 19045 O O     . HOH AA 8 .    ? 14.606  8.795   94.515  1.00 29.28 ? 1839 HOH B O     1 
HETATM 19046 O O     . HOH AA 8 .    ? 31.111  34.091  85.690  1.00 40.47 ? 1840 HOH B O     1 
HETATM 19047 O O     . HOH AA 8 .    ? 3.008   44.836  68.795  1.00 26.97 ? 1841 HOH B O     1 
HETATM 19048 O O     . HOH AA 8 .    ? 19.213  54.596  105.313 1.00 32.73 ? 1842 HOH B O     1 
HETATM 19049 O O     . HOH AA 8 .    ? 21.237  47.663  56.864  1.00 42.64 ? 1843 HOH B O     1 
HETATM 19050 O O     . HOH AA 8 .    ? -2.576  30.405  71.452  1.00 23.13 ? 1844 HOH B O     1 
HETATM 19051 O O     . HOH AA 8 .    ? 19.342  58.710  83.210  1.00 32.38 ? 1845 HOH B O     1 
HETATM 19052 O O     . HOH AA 8 .    ? 20.233  18.539  60.663  1.00 30.45 ? 1846 HOH B O     1 
HETATM 19053 O O     . HOH AA 8 .    ? 2.412   48.909  100.018 1.00 27.61 ? 1847 HOH B O     1 
HETATM 19054 O O     . HOH AA 8 .    ? 25.642  53.821  74.780  1.00 31.08 ? 1848 HOH B O     1 
HETATM 19055 O O     . HOH AA 8 .    ? 34.105  22.257  78.883  1.00 32.18 ? 1849 HOH B O     1 
HETATM 19056 O O     . HOH AA 8 .    ? -5.802  15.131  95.496  1.00 25.55 ? 1850 HOH B O     1 
HETATM 19057 O O     . HOH AA 8 .    ? 2.413   29.995  55.204  1.00 39.34 ? 1851 HOH B O     1 
HETATM 19058 O O     . HOH AA 8 .    ? 12.208  28.770  83.920  1.00 37.68 ? 1852 HOH B O     1 
HETATM 19059 O O     . HOH AA 8 .    ? 20.807  21.779  61.426  1.00 26.49 ? 1853 HOH B O     1 
HETATM 19060 O O     . HOH AA 8 .    ? 32.881  28.526  64.957  1.00 35.41 ? 1854 HOH B O     1 
HETATM 19061 O O     . HOH AA 8 .    ? -13.991 48.781  111.882 1.00 37.51 ? 1855 HOH B O     1 
HETATM 19062 O O     . HOH AA 8 .    ? 25.142  53.630  69.317  1.00 38.69 ? 1856 HOH B O     1 
HETATM 19063 O O     . HOH AA 8 .    ? 1.722   67.319  66.154  1.00 44.87 ? 1857 HOH B O     1 
HETATM 19064 O O     . HOH AA 8 .    ? 15.827  56.045  64.698  1.00 28.36 ? 1858 HOH B O     1 
HETATM 19065 O O     . HOH AA 8 .    ? 20.439  20.116  110.354 1.00 28.08 ? 1859 HOH B O     1 
HETATM 19066 O O     . HOH AA 8 .    ? 16.614  10.311  114.322 1.00 42.26 ? 1860 HOH B O     1 
HETATM 19067 O O     . HOH AA 8 .    ? 22.288  25.666  80.327  1.00 31.92 ? 1861 HOH B O     1 
HETATM 19068 O O     . HOH AA 8 .    ? 1.416   22.340  64.096  1.00 26.45 ? 1862 HOH B O     1 
HETATM 19069 O O     . HOH AA 8 .    ? -1.912  -1.326  110.405 1.00 35.58 ? 1863 HOH B O     1 
HETATM 19070 O O     . HOH AA 8 .    ? 1.660   20.392  90.841  1.00 35.94 ? 1864 HOH B O     1 
HETATM 19071 O O     . HOH AA 8 .    ? -6.965  43.880  74.610  1.00 36.44 ? 1865 HOH B O     1 
HETATM 19072 O O     . HOH AA 8 .    ? -2.248  -8.012  111.689 1.00 35.80 ? 1866 HOH B O     1 
HETATM 19073 O O     . HOH AA 8 .    ? -2.895  64.566  84.316  1.00 25.87 ? 1867 HOH B O     1 
HETATM 19074 O O     . HOH AA 8 .    ? -19.708 23.737  113.616 1.00 37.59 ? 1868 HOH B O     1 
HETATM 19075 O O     . HOH AA 8 .    ? 7.702   77.351  86.774  1.00 40.92 ? 1869 HOH B O     1 
HETATM 19076 O O     . HOH AA 8 .    ? 29.682  58.030  83.263  1.00 44.70 ? 1870 HOH B O     1 
HETATM 19077 O O     . HOH AA 8 .    ? -16.268 21.465  83.329  1.00 35.97 ? 1871 HOH B O     1 
HETATM 19078 O O     . HOH AA 8 .    ? 34.261  37.804  62.178  1.00 37.26 ? 1872 HOH B O     1 
HETATM 19079 O O     . HOH AA 8 .    ? 32.857  19.358  96.899  1.00 49.48 ? 1873 HOH B O     1 
HETATM 19080 O O     . HOH AA 8 .    ? -4.461  26.470  100.665 1.00 32.04 ? 1874 HOH B O     1 
HETATM 19081 O O     . HOH AA 8 .    ? -3.104  -3.140  86.134  1.00 48.50 ? 1875 HOH B O     1 
HETATM 19082 O O     . HOH AA 8 .    ? 14.858  18.935  90.263  1.00 34.79 ? 1876 HOH B O     1 
HETATM 19083 O O     . HOH AA 8 .    ? 4.770   56.135  75.873  1.00 23.00 ? 1877 HOH B O     1 
HETATM 19084 O O     . HOH AA 8 .    ? 17.945  76.825  64.505  1.00 35.19 ? 1878 HOH B O     1 
HETATM 19085 O O     . HOH AA 8 .    ? -7.559  10.125  114.010 1.00 29.43 ? 1879 HOH B O     1 
HETATM 19086 O O     . HOH AA 8 .    ? -2.837  -5.903  90.593  1.00 46.09 ? 1880 HOH B O     1 
HETATM 19087 O O     . HOH AA 8 .    ? 35.621  25.239  78.545  1.00 29.31 ? 1881 HOH B O     1 
HETATM 19088 O O     . HOH AA 8 .    ? 18.983  35.328  114.251 1.00 30.27 ? 1882 HOH B O     1 
HETATM 19089 O O     . HOH AA 8 .    ? -2.390  60.036  125.208 1.00 39.99 ? 1883 HOH B O     1 
HETATM 19090 O O     . HOH AA 8 .    ? 29.843  29.151  106.495 1.00 38.45 ? 1884 HOH B O     1 
HETATM 19091 O O     . HOH AA 8 .    ? 13.993  75.901  63.644  1.00 34.99 ? 1885 HOH B O     1 
HETATM 19092 O O     . HOH AA 8 .    ? 8.918   14.932  91.234  1.00 28.59 ? 1886 HOH B O     1 
HETATM 19093 O O     . HOH AA 8 .    ? 6.929   66.343  87.455  1.00 41.37 ? 1887 HOH B O     1 
HETATM 19094 O O     . HOH AA 8 .    ? 25.598  52.678  56.026  1.00 48.55 ? 1888 HOH B O     1 
HETATM 19095 O O     . HOH AA 8 .    ? 18.544  66.403  56.468  1.00 39.62 ? 1889 HOH B O     1 
HETATM 19096 O O     . HOH AA 8 .    ? 38.326  22.638  86.927  1.00 50.91 ? 1890 HOH B O     1 
HETATM 19097 O O     . HOH AA 8 .    ? -7.408  12.893  95.672  1.00 25.26 ? 1891 HOH B O     1 
HETATM 19098 O O     . HOH AA 8 .    ? 2.750   57.084  71.868  1.00 32.93 ? 1892 HOH B O     1 
HETATM 19099 O O     . HOH AA 8 .    ? -5.465  70.000  69.067  1.00 46.21 ? 1893 HOH B O     1 
HETATM 19100 O O     . HOH AA 8 .    ? 12.691  29.442  51.101  1.00 33.62 ? 1894 HOH B O     1 
HETATM 19101 O O     . HOH AA 8 .    ? -18.387 26.747  95.035  1.00 31.92 ? 1895 HOH B O     1 
HETATM 19102 O O     . HOH AA 8 .    ? -12.100 21.715  86.511  1.00 31.90 ? 1896 HOH B O     1 
HETATM 19103 O O     . HOH AA 8 .    ? -2.820  22.624  80.479  1.00 28.51 ? 1897 HOH B O     1 
HETATM 19104 O O     . HOH AA 8 .    ? -4.799  -4.312  92.828  1.00 37.70 ? 1898 HOH B O     1 
HETATM 19105 O O     . HOH AA 8 .    ? 25.963  75.351  77.521  1.00 39.04 ? 1899 HOH B O     1 
HETATM 19106 O O     . HOH AA 8 .    ? 6.695   26.063  84.398  1.00 35.25 ? 1900 HOH B O     1 
HETATM 19107 O O     . HOH AA 8 .    ? 30.890  19.401  56.788  1.00 37.54 ? 1901 HOH B O     1 
HETATM 19108 O O     . HOH AA 8 .    ? 31.522  51.112  80.113  1.00 41.50 ? 1902 HOH B O     1 
HETATM 19109 O O     . HOH AA 8 .    ? 15.795  49.667  79.762  1.00 40.54 ? 1903 HOH B O     1 
HETATM 19110 O O     . HOH AA 8 .    ? -0.175  11.142  81.987  1.00 41.63 ? 1904 HOH B O     1 
HETATM 19111 O O     . HOH AA 8 .    ? -6.212  35.668  93.670  1.00 34.83 ? 1905 HOH B O     1 
HETATM 19112 O O     . HOH AA 8 .    ? -12.988 31.464  84.375  1.00 41.62 ? 1906 HOH B O     1 
HETATM 19113 O O     . HOH AA 8 .    ? 15.335  37.083  116.059 1.00 46.89 ? 1907 HOH B O     1 
HETATM 19114 O O     . HOH AA 8 .    ? 31.438  67.309  83.285  1.00 40.62 ? 1908 HOH B O     1 
HETATM 19115 O O     . HOH AA 8 .    ? -4.369  30.648  95.853  1.00 30.23 ? 1909 HOH B O     1 
HETATM 19116 O O     . HOH AA 8 .    ? 13.172  53.580  106.761 1.00 42.85 ? 1910 HOH B O     1 
HETATM 19117 O O     . HOH AA 8 .    ? 7.996   54.245  65.527  1.00 33.08 ? 1911 HOH B O     1 
HETATM 19118 O O     . HOH AA 8 .    ? 3.798   18.015  76.875  1.00 38.35 ? 1912 HOH B O     1 
HETATM 19119 O O     . HOH AA 8 .    ? -15.215 19.200  83.540  1.00 33.25 ? 1913 HOH B O     1 
HETATM 19120 O O     . HOH AA 8 .    ? -6.148  41.149  85.052  1.00 37.75 ? 1914 HOH B O     1 
HETATM 19121 O O     . HOH AA 8 .    ? 37.870  36.745  90.384  1.00 36.41 ? 1915 HOH B O     1 
HETATM 19122 O O     . HOH AA 8 .    ? -3.142  -2.745  96.090  1.00 40.32 ? 1916 HOH B O     1 
HETATM 19123 O O     . HOH AA 8 .    ? 22.828  67.822  60.109  1.00 36.62 ? 1917 HOH B O     1 
HETATM 19124 O O     . HOH AA 8 .    ? 7.847   26.666  110.979 1.00 47.59 ? 1918 HOH B O     1 
HETATM 19125 O O     . HOH AA 8 .    ? -2.102  28.368  63.581  1.00 36.41 ? 1919 HOH B O     1 
HETATM 19126 O O     . HOH AA 8 .    ? 9.164   57.426  96.501  1.00 38.22 ? 1920 HOH B O     1 
HETATM 19127 O O     . HOH AA 8 .    ? 35.652  31.027  59.205  1.00 39.79 ? 1921 HOH B O     1 
HETATM 19128 O O     . HOH AA 8 .    ? 14.303  6.235   69.617  1.00 45.23 ? 1922 HOH B O     1 
HETATM 19129 O O     . HOH AA 8 .    ? -1.801  -9.911  110.275 1.00 42.98 ? 1923 HOH B O     1 
HETATM 19130 O O     . HOH AA 8 .    ? 29.806  41.543  84.649  1.00 49.52 ? 1924 HOH B O     1 
HETATM 19131 O O     . HOH AA 8 .    ? -20.558 25.294  95.541  1.00 30.70 ? 1925 HOH B O     1 
HETATM 19132 O O     . HOH AA 8 .    ? 17.928  49.259  113.122 1.00 39.60 ? 1926 HOH B O     1 
HETATM 19133 O O     . HOH AA 8 .    ? 15.977  9.836   96.453  1.00 33.82 ? 1927 HOH B O     1 
HETATM 19134 O O     . HOH AA 8 .    ? 28.400  33.920  70.864  1.00 43.98 ? 1928 HOH B O     1 
HETATM 19135 O O     . HOH AA 8 .    ? 9.974   53.288  66.357  1.00 34.28 ? 1929 HOH B O     1 
HETATM 19136 O O     . HOH AA 8 .    ? 28.038  10.163  85.680  1.00 46.48 ? 1930 HOH B O     1 
HETATM 19137 O O     . HOH AA 8 .    ? 31.038  41.226  80.322  1.00 40.42 ? 1931 HOH B O     1 
HETATM 19138 O O     . HOH AA 8 .    ? 8.948   80.389  86.516  1.00 47.07 ? 1932 HOH B O     1 
HETATM 19139 O O     . HOH AA 8 .    ? 12.297  57.805  95.025  1.00 37.67 ? 1933 HOH B O     1 
HETATM 19140 O O     . HOH AA 8 .    ? 21.357  26.478  82.925  1.00 32.39 ? 1934 HOH B O     1 
HETATM 19141 O O     . HOH AA 8 .    ? 9.373   30.378  89.442  1.00 34.52 ? 1935 HOH B O     1 
HETATM 19142 O O     . HOH AA 8 .    ? 38.975  35.256  83.553  1.00 50.72 ? 1936 HOH B O     1 
HETATM 19143 O O     . HOH AA 8 .    ? 2.386   3.634   85.527  1.00 40.06 ? 1937 HOH B O     1 
HETATM 19144 O O     . HOH AA 8 .    ? 18.651  39.941  80.693  1.00 33.39 ? 1938 HOH B O     1 
HETATM 19145 O O     . HOH AA 8 .    ? 6.197   48.243  115.643 1.00 32.27 ? 1939 HOH B O     1 
HETATM 19146 O O     . HOH AA 8 .    ? -22.436 25.499  92.406  1.00 41.68 ? 1940 HOH B O     1 
HETATM 19147 O O     . HOH AA 8 .    ? -6.634  7.828   117.595 1.00 32.97 ? 1941 HOH B O     1 
HETATM 19148 O O     . HOH AA 8 .    ? -5.577  37.728  86.987  1.00 39.62 ? 1942 HOH B O     1 
HETATM 19149 O O     . HOH AA 8 .    ? -19.936 27.612  92.380  1.00 41.39 ? 1943 HOH B O     1 
HETATM 19150 O O     . HOH AA 8 .    ? 6.258   17.305  97.376  1.00 34.98 ? 1944 HOH B O     1 
HETATM 19151 O O     . HOH AA 8 .    ? 32.840  58.974  68.087  1.00 40.58 ? 1945 HOH B O     1 
HETATM 19152 O O     . HOH AA 8 .    ? 16.554  13.700  107.743 1.00 36.96 ? 1946 HOH B O     1 
HETATM 19153 O O     . HOH AA 8 .    ? -7.302  36.748  67.139  1.00 35.38 ? 1947 HOH B O     1 
HETATM 19154 O O     . HOH AA 8 .    ? -10.411 29.897  76.841  1.00 38.91 ? 1948 HOH B O     1 
HETATM 19155 O O     . HOH AA 8 .    ? 18.340  63.724  56.041  1.00 43.37 ? 1949 HOH B O     1 
HETATM 19156 O O     . HOH AA 8 .    ? 28.556  41.269  54.002  1.00 41.45 ? 1950 HOH B O     1 
HETATM 19157 O O     . HOH AA 8 .    ? -2.608  29.630  97.865  1.00 32.21 ? 1951 HOH B O     1 
HETATM 19158 O O     . HOH AA 8 .    ? 23.635  68.396  62.781  1.00 42.52 ? 1952 HOH B O     1 
HETATM 19159 O O     . HOH AA 8 .    ? -4.890  51.568  102.740 1.00 40.99 ? 1953 HOH B O     1 
HETATM 19160 O O     . HOH AA 8 .    ? 19.997  45.282  90.966  1.00 29.75 ? 1954 HOH B O     1 
HETATM 19161 O O     . HOH AA 8 .    ? 0.653   46.582  96.986  1.00 49.34 ? 1955 HOH B O     1 
HETATM 19162 O O     . HOH AA 8 .    ? 4.944   43.320  51.523  1.00 40.41 ? 1956 HOH B O     1 
HETATM 19163 O O     . HOH AA 8 .    ? 33.391  40.269  60.987  1.00 45.13 ? 1957 HOH B O     1 
HETATM 19164 O O     . HOH AA 8 .    ? 8.992   16.926  124.448 1.00 43.02 ? 1958 HOH B O     1 
HETATM 19165 O O     . HOH AA 8 .    ? 26.048  32.800  75.591  1.00 35.48 ? 1959 HOH B O     1 
HETATM 19166 O O     . HOH AA 8 .    ? -13.210 9.174   131.118 1.00 49.38 ? 1960 HOH B O     1 
HETATM 19167 O O     . HOH AA 8 .    ? -1.053  16.432  83.944  1.00 25.07 ? 1961 HOH B O     1 
HETATM 19168 O O     . HOH AA 8 .    ? -13.050 4.812   86.829  1.00 47.65 ? 1962 HOH B O     1 
HETATM 19169 O O     . HOH AA 8 .    ? 20.967  24.394  84.138  1.00 32.91 ? 1963 HOH B O     1 
HETATM 19170 O O     . HOH AA 8 .    ? 32.918  62.401  69.576  1.00 44.52 ? 1964 HOH B O     1 
HETATM 19171 O O     . HOH AA 8 .    ? -7.884  -3.267  118.896 1.00 44.61 ? 1965 HOH B O     1 
HETATM 19172 O O     . HOH AA 8 .    ? -0.215  44.971  78.421  1.00 33.54 ? 1966 HOH B O     1 
HETATM 19173 O O     . HOH AA 8 .    ? 0.488   4.074   87.054  1.00 38.57 ? 1967 HOH B O     1 
HETATM 19174 O O     . HOH AA 8 .    ? 11.054  9.909   124.413 1.00 35.68 ? 1968 HOH B O     1 
HETATM 19175 O O     . HOH AA 8 .    ? -4.019  39.910  61.343  1.00 37.84 ? 1969 HOH B O     1 
HETATM 19176 O O     . HOH AA 8 .    ? -12.154 29.831  82.629  1.00 38.27 ? 1970 HOH B O     1 
HETATM 19177 O O     . HOH AA 8 .    ? 5.440   44.766  54.524  1.00 37.52 ? 1971 HOH B O     1 
HETATM 19178 O O     . HOH AA 8 .    ? 15.924  35.054  114.747 1.00 41.85 ? 1972 HOH B O     1 
HETATM 19179 O O     . HOH AA 8 .    ? 6.216   60.876  89.071  1.00 43.41 ? 1973 HOH B O     1 
HETATM 19180 O O     . HOH AA 8 .    ? 17.102  25.883  111.064 1.00 36.19 ? 1974 HOH B O     1 
HETATM 19181 O O     . HOH AA 8 .    ? -4.534  45.618  105.607 1.00 47.39 ? 1975 HOH B O     1 
HETATM 19182 O O     . HOH AA 8 .    ? 0.170   17.874  72.473  1.00 35.07 ? 1976 HOH B O     1 
HETATM 19183 O O     . HOH AA 8 .    ? 14.790  21.740  98.635  1.00 37.09 ? 1977 HOH B O     1 
HETATM 19184 O O     . HOH AA 8 .    ? -2.367  51.711  101.808 1.00 33.39 ? 1978 HOH B O     1 
HETATM 19185 O O     . HOH AA 8 .    ? 6.818   23.767  84.334  1.00 34.50 ? 1979 HOH B O     1 
HETATM 19186 O O     . HOH AA 8 .    ? -17.801 6.459   93.870  1.00 40.82 ? 1980 HOH B O     1 
HETATM 19187 O O     . HOH AA 8 .    ? 1.702   44.521  98.009  1.00 39.44 ? 1981 HOH B O     1 
HETATM 19188 O O     . HOH AA 8 .    ? -2.942  29.209  100.131 1.00 40.20 ? 1982 HOH B O     1 
HETATM 19189 O O     . HOH AA 8 .    ? 1.335   55.042  71.102  1.00 37.95 ? 1983 HOH B O     1 
HETATM 19190 O O     . HOH AA 8 .    ? 6.147   -10.344 106.489 1.00 42.08 ? 1984 HOH B O     1 
HETATM 19191 O O     . HOH AA 8 .    ? 9.545   74.870  90.140  1.00 45.79 ? 1985 HOH B O     1 
HETATM 19192 O O     . HOH AA 8 .    ? -2.898  28.306  69.617  1.00 31.63 ? 1986 HOH B O     1 
HETATM 19193 O O     . HOH AA 8 .    ? 34.679  25.671  57.129  1.00 38.43 ? 1987 HOH B O     1 
HETATM 19194 O O     . HOH AA 8 .    ? 21.065  69.124  59.267  1.00 44.30 ? 1988 HOH B O     1 
HETATM 19195 O O     . HOH AA 8 .    ? 40.286  38.074  90.002  1.00 39.23 ? 1989 HOH B O     1 
HETATM 19196 O O     . HOH AA 8 .    ? 20.747  22.711  110.844 1.00 42.96 ? 1990 HOH B O     1 
HETATM 19197 O O     . HOH AA 8 .    ? -15.363 6.730   87.503  1.00 46.62 ? 1991 HOH B O     1 
HETATM 19198 O O     . HOH AA 8 .    ? 13.900  24.799  101.912 1.00 36.15 ? 1992 HOH B O     1 
HETATM 19199 O O     . HOH AA 8 .    ? 9.492   64.036  88.110  1.00 41.72 ? 1993 HOH B O     1 
HETATM 19200 O O     . HOH AA 8 .    ? 7.797   77.037  89.248  1.00 44.93 ? 1994 HOH B O     1 
HETATM 19201 O O     . HOH AA 8 .    ? -7.455  22.309  79.435  1.00 33.41 ? 1995 HOH B O     1 
HETATM 19202 O O     . HOH AA 8 .    ? 9.995   28.211  89.462  1.00 45.08 ? 1996 HOH B O     1 
HETATM 19203 O O     . HOH AA 8 .    ? 6.664   2.008   80.300  1.00 45.16 ? 1997 HOH B O     1 
HETATM 19204 O O     . HOH AA 8 .    ? 32.506  42.948  80.743  1.00 46.21 ? 1998 HOH B O     1 
HETATM 19205 O O     . HOH AA 8 .    ? 11.998  0.542   114.942 1.00 50.28 ? 1999 HOH B O     1 
HETATM 19206 O O     . HOH AA 8 .    ? 13.800  36.183  74.894  1.00 28.15 ? 2000 HOH B O     1 
HETATM 19207 O O     . HOH AA 8 .    ? 13.318  36.397  78.059  1.00 29.32 ? 2001 HOH B O     1 
HETATM 19208 O O     . HOH AA 8 .    ? -9.065  41.971  73.156  1.00 42.47 ? 2002 HOH B O     1 
HETATM 19209 O O     . HOH AA 8 .    ? 30.636  30.841  80.293  1.00 40.30 ? 2003 HOH B O     1 
HETATM 19210 O O     . HOH AA 8 .    ? -12.410 19.923  81.227  1.00 45.19 ? 2004 HOH B O     1 
HETATM 19211 O O     . HOH AA 8 .    ? 31.076  61.482  73.383  1.00 33.44 ? 2005 HOH B O     1 
HETATM 19212 O O     . HOH AA 8 .    ? 20.132  33.936  116.241 1.00 33.84 ? 2006 HOH B O     1 
HETATM 19213 O O     . HOH AA 8 .    ? 1.667   21.557  95.951  1.00 43.44 ? 2007 HOH B O     1 
HETATM 19214 O O     . HOH AA 8 .    ? 6.686   60.944  86.138  1.00 26.87 ? 2008 HOH B O     1 
HETATM 19215 O O     . HOH AA 8 .    ? 29.373  31.258  82.490  1.00 32.74 ? 2009 HOH B O     1 
HETATM 19216 O O     . HOH AA 8 .    ? 5.243   49.822  114.025 1.00 38.74 ? 2010 HOH B O     1 
HETATM 19217 O O     . HOH AA 8 .    ? 21.985  19.625  108.260 1.00 37.56 ? 2011 HOH B O     1 
HETATM 19218 O O     . HOH AA 8 .    ? -8.287  33.441  86.156  1.00 37.86 ? 2012 HOH B O     1 
HETATM 19219 O O     . HOH AA 8 .    ? 4.376   64.151  87.605  1.00 37.98 ? 2013 HOH B O     1 
HETATM 19220 O O     . HOH AA 8 .    ? 5.821   29.716  87.192  1.00 31.64 ? 2014 HOH B O     1 
HETATM 19221 O O     . HOH AA 8 .    ? 8.634   64.866  67.123  1.00 40.48 ? 2015 HOH B O     1 
HETATM 19222 O O     . HOH AA 8 .    ? 31.936  69.502  80.874  1.00 36.82 ? 2016 HOH B O     1 
HETATM 19223 O O     . HOH AA 8 .    ? 19.756  2.573   78.212  1.00 48.97 ? 2017 HOH B O     1 
HETATM 19224 O O     . HOH AA 8 .    ? 5.086   2.737   86.768  1.00 43.47 ? 2018 HOH B O     1 
HETATM 19225 O O     . HOH AA 8 .    ? -11.525 1.550   90.070  1.00 39.80 ? 2019 HOH B O     1 
HETATM 19226 O O     . HOH AA 8 .    ? 14.391  51.584  63.696  1.00 36.10 ? 2020 HOH B O     1 
HETATM 19227 O O     . HOH AA 8 .    ? -21.758 26.020  97.647  1.00 44.40 ? 2021 HOH B O     1 
HETATM 19228 O O     . HOH AA 8 .    ? -25.262 12.420  87.460  1.00 38.89 ? 2022 HOH B O     1 
HETATM 19229 O O     . HOH AA 8 .    ? 9.324   3.325   84.655  1.00 35.47 ? 2023 HOH B O     1 
HETATM 19230 O O     . HOH AA 8 .    ? 23.568  71.630  84.498  1.00 47.22 ? 2024 HOH B O     1 
HETATM 19231 O O     . HOH AA 8 .    ? 14.146  24.436  99.300  1.00 40.04 ? 2025 HOH B O     1 
HETATM 19232 O O     . HOH AA 8 .    ? -7.277  24.849  75.866  1.00 39.70 ? 2026 HOH B O     1 
HETATM 19233 O O     . HOH AA 8 .    ? -11.298 46.719  77.862  1.00 44.56 ? 2027 HOH B O     1 
HETATM 19234 O O     . HOH AA 8 .    ? -10.668 33.577  84.828  1.00 44.44 ? 2028 HOH B O     1 
HETATM 19235 O O     . HOH AA 8 .    ? 15.516  38.475  77.795  1.00 29.49 ? 2029 HOH B O     1 
HETATM 19236 O O     . HOH AA 8 .    ? -23.471 14.026  83.235  1.00 37.01 ? 2030 HOH B O     1 
HETATM 19237 O O     . HOH AA 8 .    ? -4.336  22.908  73.180  1.00 39.87 ? 2031 HOH B O     1 
HETATM 19238 O O     . HOH AA 8 .    ? 30.921  23.370  75.178  1.00 37.30 ? 2032 HOH B O     1 
HETATM 19239 O O     . HOH AA 8 .    ? 9.906   16.730  90.630  1.00 34.73 ? 2033 HOH B O     1 
HETATM 19240 O O     . HOH AA 8 .    ? -6.582  36.387  62.479  1.00 38.67 ? 2034 HOH B O     1 
HETATM 19241 O O     . HOH AA 8 .    ? 2.087   21.381  62.128  1.00 34.09 ? 2035 HOH B O     1 
HETATM 19242 O O     . HOH AA 8 .    ? -1.207  23.064  64.535  1.00 34.43 ? 2036 HOH B O     1 
HETATM 19243 O O     . HOH AA 8 .    ? -9.577  34.682  90.918  1.00 44.09 ? 2037 HOH B O     1 
HETATM 19244 O O     . HOH AA 8 .    ? 27.095  35.425  71.929  1.00 38.23 ? 2038 HOH B O     1 
HETATM 19245 O O     . HOH AA 8 .    ? 2.106   31.869  85.842  1.00 31.01 ? 2039 HOH B O     1 
HETATM 19246 O O     . HOH AA 8 .    ? 17.611  37.749  79.458  1.00 37.27 ? 2040 HOH B O     1 
HETATM 19247 O O     . HOH AA 8 .    ? -15.867 7.146   91.643  1.00 41.17 ? 2041 HOH B O     1 
HETATM 19248 O O     . HOH AA 8 .    ? -5.006  23.366  75.642  1.00 35.35 ? 2042 HOH B O     1 
HETATM 19249 O O     . HOH AA 8 .    ? -2.607  23.367  62.057  1.00 46.68 ? 2043 HOH B O     1 
HETATM 19250 O O     . HOH AA 8 .    ? 29.080  33.939  81.872  1.00 42.34 ? 2044 HOH B O     1 
HETATM 19251 O O     . HOH AA 8 .    ? -15.874 5.374   89.621  1.00 43.11 ? 2045 HOH B O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1     N N   . PRO A 17   ? 0.7211 0.7667 0.8269 0.1180  0.0088  -0.1261 15   PRO A N   
2     C CA  . PRO A 17   ? 0.6406 0.6959 0.7335 0.1139  0.0155  -0.1165 15   PRO A CA  
3     C C   . PRO A 17   ? 0.6125 0.6815 0.6913 0.1134  0.0202  -0.1186 15   PRO A C   
4     O O   . PRO A 17   ? 0.6272 0.6918 0.7018 0.1127  0.0186  -0.1212 15   PRO A O   
5     C CB  . PRO A 17   ? 0.6386 0.6777 0.7277 0.1064  0.0148  -0.1024 15   PRO A CB  
6     C CG  . PRO A 17   ? 0.6583 0.6814 0.7614 0.1074  0.0079  -0.1039 15   PRO A CG  
7     C CD  . PRO A 17   ? 0.6279 0.6533 0.7380 0.1133  0.0043  -0.1179 15   PRO A CD  
8     N N   . ALA A 18   ? 0.5709 0.6569 0.6430 0.1138  0.0258  -0.1173 16   ALA A N   
9     C CA  . ALA A 18   ? 0.5335 0.6343 0.5924 0.1134  0.0304  -0.1185 16   ALA A CA  
10    C C   . ALA A 18   ? 0.5476 0.6391 0.5946 0.1061  0.0318  -0.1071 16   ALA A C   
11    O O   . ALA A 18   ? 0.5102 0.5913 0.5557 0.1008  0.0322  -0.0957 16   ALA A O   
12    C CB  . ALA A 18   ? 0.5780 0.6988 0.6328 0.1145  0.0361  -0.1174 16   ALA A CB  
13    N N   . PRO A 19   ? 0.5214 0.6165 0.5600 0.1060  0.0322  -0.1101 17   PRO A N   
14    C CA  . PRO A 19   ? 0.5197 0.6057 0.5478 0.0994  0.0332  -0.0998 17   PRO A CA  
15    C C   . PRO A 19   ? 0.4926 0.5849 0.5111 0.0944  0.0385  -0.0879 17   PRO A C   
16    O O   . PRO A 19   ? 0.4930 0.6029 0.5077 0.0958  0.0426  -0.0888 17   PRO A O   
17    C CB  . PRO A 19   ? 0.5134 0.6068 0.5350 0.1016  0.0330  -0.1072 17   PRO A CB  
18    C CG  . PRO A 19   ? 0.4889 0.5864 0.5216 0.1089  0.0294  -0.1221 17   PRO A CG  
19    C CD  . PRO A 19   ? 0.5069 0.6131 0.5469 0.1120  0.0310  -0.1239 17   PRO A CD  
20    N N   . PHE A 20   ? 0.4621 0.5403 0.4778 0.0883  0.0380  -0.0769 18   PHE A N   
21    C CA  . PHE A 20   ? 0.4503 0.5309 0.4574 0.0827  0.0421  -0.0650 18   PHE A CA  
22    C C   . PHE A 20   ? 0.4604 0.5497 0.4711 0.0829  0.0449  -0.0620 18   PHE A C   
23    O O   . PHE A 20   ? 0.4565 0.5512 0.4606 0.0788  0.0486  -0.0531 18   PHE A O   
24    C CB  . PHE A 20   ? 0.4203 0.5124 0.4154 0.0813  0.0455  -0.0633 18   PHE A CB  
25    C CG  . PHE A 20   ? 0.4143 0.4981 0.4047 0.0803  0.0430  -0.0648 18   PHE A CG  
26    C CD1 . PHE A 20   ? 0.4081 0.4762 0.3958 0.0751  0.0414  -0.0566 18   PHE A CD1 
27    C CD2 . PHE A 20   ? 0.3712 0.4635 0.3603 0.0847  0.0421  -0.0749 18   PHE A CD2 
28    C CE1 . PHE A 20   ? 0.4278 0.4888 0.4116 0.0742  0.0392  -0.0580 18   PHE A CE1 
29    C CE2 . PHE A 20   ? 0.3811 0.4659 0.3661 0.0837  0.0397  -0.0762 18   PHE A CE2 
30    C CZ  . PHE A 20   ? 0.4252 0.4944 0.4076 0.0784  0.0383  -0.0676 18   PHE A CZ  
31    N N   . ALA A 21   ? 0.4677 0.5583 0.4893 0.0877  0.0430  -0.0690 19   ALA A N   
32    C CA  . ALA A 21   ? 0.5208 0.6196 0.5465 0.0880  0.0455  -0.0663 19   ALA A CA  
33    C C   . ALA A 21   ? 0.5278 0.6141 0.5545 0.0825  0.0450  -0.0551 19   ALA A C   
34    O O   . ALA A 21   ? 0.6048 0.6981 0.6320 0.0809  0.0478  -0.0500 19   ALA A O   
35    C CB  . ALA A 21   ? 0.5218 0.6251 0.5598 0.0949  0.0431  -0.0773 19   ALA A CB  
36    N N   . ASP A 22   ? 0.4823 0.5513 0.5095 0.0794  0.0416  -0.0512 20   ASP A N   
37    C CA  . ASP A 22   ? 0.4875 0.5451 0.5152 0.0743  0.0409  -0.0411 20   ASP A CA  
38    C C   . ASP A 22   ? 0.4198 0.4684 0.4384 0.0687  0.0410  -0.0337 20   ASP A C   
39    O O   . ASP A 22   ? 0.3653 0.4003 0.3853 0.0654  0.0385  -0.0284 20   ASP A O   
40    C CB  . ASP A 22   ? 0.4816 0.5270 0.5208 0.0760  0.0360  -0.0430 20   ASP A CB  
41    N N   . PHE A 23   ? 0.3986 0.4552 0.4076 0.0676  0.0439  -0.0331 21   PHE A N   
42    C CA  . PHE A 23   ? 0.3754 0.4233 0.3764 0.0634  0.0435  -0.0279 21   PHE A CA  
43    C C   . PHE A 23   ? 0.3759 0.4160 0.3745 0.0575  0.0440  -0.0172 21   PHE A C   
44    O O   . PHE A 23   ? 0.3566 0.3834 0.3555 0.0548  0.0413  -0.0139 21   PHE A O   
45    C CB  . PHE A 23   ? 0.3730 0.4324 0.3646 0.0634  0.0464  -0.0287 21   PHE A CB  
46    C CG  . PHE A 23   ? 0.3954 0.4468 0.3789 0.0590  0.0461  -0.0228 21   PHE A CG  
47    C CD1 . PHE A 23   ? 0.4076 0.4475 0.3916 0.0592  0.0426  -0.0257 21   PHE A CD1 
48    C CD2 . PHE A 23   ? 0.4145 0.4698 0.3908 0.0546  0.0490  -0.0142 21   PHE A CD2 
49    C CE1 . PHE A 23   ? 0.3641 0.3972 0.3409 0.0553  0.0423  -0.0206 21   PHE A CE1 
50    C CE2 . PHE A 23   ? 0.3857 0.4335 0.3554 0.0508  0.0483  -0.0091 21   PHE A CE2 
51    C CZ  . PHE A 23   ? 0.4240 0.4610 0.3939 0.0513  0.0451  -0.0126 21   PHE A CZ  
52    N N   . ALA A 24   ? 0.3441 0.3929 0.3407 0.0555  0.0474  -0.0119 22   ALA A N   
53    C CA  . ALA A 24   ? 0.3882 0.4307 0.3822 0.0499  0.0479  -0.0023 22   ALA A CA  
54    C C   . ALA A 24   ? 0.3548 0.4070 0.3511 0.0489  0.0507  0.0016  22   ALA A C   
55    O O   . ALA A 24   ? 0.3698 0.4268 0.3611 0.0452  0.0532  0.0081  22   ALA A O   
56    C CB  . ALA A 24   ? 0.3862 0.4270 0.3710 0.0461  0.0489  0.0026  22   ALA A CB  
57    N N   . PRO A 25   ? 0.3740 0.4290 0.3786 0.0520  0.0501  -0.0018 23   PRO A N   
58    C CA  . PRO A 25   ? 0.3596 0.4244 0.3669 0.0512  0.0527  0.0016  23   PRO A CA  
59    C C   . PRO A 25   ? 0.3690 0.4266 0.3752 0.0455  0.0525  0.0107  23   PRO A C   
60    O O   . PRO A 25   ? 0.3632 0.4078 0.3709 0.0437  0.0495  0.0127  23   PRO A O   
61    C CB  . PRO A 25   ? 0.3559 0.4217 0.3733 0.0559  0.0509  -0.0047 23   PRO A CB  
62    C CG  . PRO A 25   ? 0.4049 0.4555 0.4254 0.0565  0.0464  -0.0068 23   PRO A CG  
63    C CD  . PRO A 25   ? 0.3576 0.4043 0.3702 0.0555  0.0463  -0.0076 23   PRO A CD  
64    N N   . PRO A 26   ? 0.3850 0.4512 0.3888 0.0424  0.0555  0.0165  24   PRO A N   
65    C CA  . PRO A 26   ? 0.3608 0.4205 0.3644 0.0371  0.0550  0.0245  24   PRO A CA  
66    C C   . PRO A 26   ? 0.3842 0.4395 0.3957 0.0376  0.0530  0.0246  24   PRO A C   
67    O O   . PRO A 26   ? 0.3664 0.4271 0.3841 0.0418  0.0529  0.0197  24   PRO A O   
68    C CB  . PRO A 26   ? 0.3459 0.4181 0.3473 0.0345  0.0587  0.0296  24   PRO A CB  
69    C CG  . PRO A 26   ? 0.3824 0.4698 0.3853 0.0392  0.0612  0.0237  24   PRO A CG  
70    C CD  . PRO A 26   ? 0.3903 0.4729 0.3913 0.0433  0.0594  0.0161  24   PRO A CD  
71    N N   . VAL A 27   ? 0.3696 0.4153 0.3810 0.0335  0.0512  0.0301  25   VAL A N   
72    C CA  . VAL A 27   ? 0.3925 0.4345 0.4107 0.0333  0.0492  0.0314  25   VAL A CA  
73    C C   . VAL A 27   ? 0.4095 0.4635 0.4328 0.0341  0.0514  0.0320  25   VAL A C   
74    O O   . VAL A 27   ? 0.3800 0.4355 0.4105 0.0370  0.0502  0.0292  25   VAL A O   
75    C CB  . VAL A 27   ? 0.4119 0.4442 0.4280 0.0283  0.0473  0.0373  25   VAL A CB  
76    C CG1 . VAL A 27   ? 0.4101 0.4419 0.4327 0.0274  0.0458  0.0397  25   VAL A CG1 
77    C CG2 . VAL A 27   ? 0.3300 0.3508 0.3430 0.0282  0.0447  0.0360  25   VAL A CG2 
78    N N   . ARG A 28   ? 0.3856 0.4486 0.4058 0.0316  0.0545  0.0357  26   ARG A N   
79    C CA  . ARG A 28   ? 0.4301 0.5060 0.4548 0.0316  0.0571  0.0371  26   ARG A CA  
80    C C   . ARG A 28   ? 0.4440 0.5318 0.4639 0.0309  0.0608  0.0384  26   ARG A C   
81    O O   . ARG A 28   ? 0.4260 0.5102 0.4391 0.0290  0.0610  0.0403  26   ARG A O   
82    C CB  . ARG A 28   ? 0.4459 0.5192 0.4736 0.0270  0.0563  0.0435  26   ARG A CB  
83    C CG  . ARG A 28   ? 0.4442 0.5165 0.4669 0.0215  0.0573  0.0501  26   ARG A CG  
84    C CD  . ARG A 28   ? 0.5024 0.5720 0.5289 0.0171  0.0560  0.0556  26   ARG A CD  
85    N NE  . ARG A 28   ? 0.5005 0.5568 0.5267 0.0161  0.0524  0.0555  26   ARG A NE  
86    C CZ  . ARG A 28   ? 0.5114 0.5644 0.5425 0.0180  0.0502  0.0535  26   ARG A CZ  
87    N NH1 . ARG A 28   ? 0.4636 0.5248 0.5010 0.0208  0.0509  0.0515  26   ARG A NH1 
88    N NH2 . ARG A 28   ? 0.4727 0.5147 0.5026 0.0170  0.0470  0.0537  26   ARG A NH2 
89    N N   . PRO A 29   ? 0.4380 0.5408 0.4614 0.0322  0.0637  0.0380  27   PRO A N   
90    C CA  . PRO A 29   ? 0.4324 0.5482 0.4513 0.0308  0.0674  0.0407  27   PRO A CA  
91    C C   . PRO A 29   ? 0.4165 0.5288 0.4324 0.0242  0.0675  0.0499  27   PRO A C   
92    O O   . PRO A 29   ? 0.4254 0.5323 0.4451 0.0208  0.0661  0.0542  27   PRO A O   
93    C CB  . PRO A 29   ? 0.4374 0.5697 0.4623 0.0331  0.0701  0.0391  27   PRO A CB  
94    C CG  . PRO A 29   ? 0.4191 0.5469 0.4510 0.0378  0.0677  0.0325  27   PRO A CG  
95    C CD  . PRO A 29   ? 0.4476 0.5571 0.4794 0.0353  0.0638  0.0350  27   PRO A CD  
96    N N   . GLN A 30   ? 0.4152 0.5303 0.4244 0.0225  0.0689  0.0526  28   GLN A N   
97    C CA  . GLN A 30   ? 0.4311 0.5406 0.4376 0.0166  0.0682  0.0608  28   GLN A CA  
98    C C   . GLN A 30   ? 0.4293 0.5513 0.4392 0.0128  0.0707  0.0678  28   GLN A C   
99    O O   . GLN A 30   ? 0.3952 0.5324 0.4035 0.0134  0.0739  0.0689  28   GLN A O   
100   C CB  . GLN A 30   ? 0.4105 0.5175 0.4090 0.0163  0.0683  0.0612  28   GLN A CB  
101   C CG  . GLN A 30   ? 0.3678 0.4626 0.3631 0.0197  0.0657  0.0546  28   GLN A CG  
102   C CD  . GLN A 30   ? 0.3879 0.4660 0.3847 0.0174  0.0622  0.0559  28   GLN A CD  
103   O OE1 . GLN A 30   ? 0.3906 0.4608 0.3845 0.0136  0.0608  0.0605  28   GLN A OE1 
104   N NE2 . GLN A 30   ? 0.3970 0.4705 0.3989 0.0197  0.0605  0.0519  28   GLN A NE2 
105   N N   . SER A 31   ? 0.3746 0.4911 0.3896 0.0089  0.0691  0.0724  29   SER A N   
106   C CA  . SER A 31   ? 0.3475 0.4740 0.3670 0.0045  0.0708  0.0797  29   SER A CA  
107   C C   . SER A 31   ? 0.3565 0.4850 0.3721 0.0000  0.0714  0.0872  29   SER A C   
108   O O   . SER A 31   ? 0.3453 0.4648 0.3551 -0.0002 0.0699  0.0871  29   SER A O   
109   C CB  . SER A 31   ? 0.3417 0.4599 0.3677 0.0014  0.0682  0.0821  29   SER A CB  
110   O OG  . SER A 31   ? 0.3508 0.4552 0.3748 -0.0024 0.0652  0.0855  29   SER A OG  
111   N N   . THR A 32   ? 0.3249 0.4656 0.3444 -0.0038 0.0735  0.0942  30   THR A N   
112   C CA  . THR A 32   ? 0.3228 0.4655 0.3404 -0.0087 0.0736  0.1029  30   THR A CA  
113   C C   . THR A 32   ? 0.3094 0.4340 0.3270 -0.0123 0.0694  0.1057  30   THR A C   
114   O O   . THR A 32   ? 0.3225 0.4427 0.3355 -0.0139 0.0685  0.1090  30   THR A O   
115   C CB  . THR A 32   ? 0.3399 0.4969 0.3639 -0.0130 0.0757  0.1107  30   THR A CB  
116   O OG1 . THR A 32   ? 0.3367 0.5124 0.3600 -0.0095 0.0799  0.1080  30   THR A OG1 
117   C CG2 . THR A 32   ? 0.3751 0.5330 0.3988 -0.0188 0.0751  0.1209  30   THR A CG2 
118   N N   . LEU A 33   ? 0.2892 0.4038 0.3120 -0.0134 0.0668  0.1043  31   LEU A N   
119   C CA  . LEU A 33   ? 0.3239 0.4224 0.3471 -0.0164 0.0627  0.1060  31   LEU A CA  
120   C C   . LEU A 33   ? 0.3396 0.4266 0.3554 -0.0130 0.0612  0.1002  31   LEU A C   
121   O O   . LEU A 33   ? 0.3229 0.4011 0.3361 -0.0151 0.0591  0.1026  31   LEU A O   
122   C CB  . LEU A 33   ? 0.3581 0.4502 0.3882 -0.0181 0.0603  0.1052  31   LEU A CB  
123   C CG  . LEU A 33   ? 0.3720 0.4720 0.4104 -0.0231 0.0606  0.1125  31   LEU A CG  
124   C CD1 . LEU A 33   ? 0.3189 0.4176 0.3641 -0.0233 0.0592  0.1100  31   LEU A CD1 
125   C CD2 . LEU A 33   ? 0.3485 0.4412 0.3887 -0.0284 0.0578  0.1192  31   LEU A CD2 
126   N N   . ARG A 34   ? 0.3015 0.3886 0.3147 -0.0078 0.0620  0.0926  32   ARG A N   
127   C CA  . ARG A 34   ? 0.3535 0.4306 0.3604 -0.0047 0.0606  0.0872  32   ARG A CA  
128   C C   . ARG A 34   ? 0.3226 0.4044 0.3229 -0.0040 0.0622  0.0886  32   ARG A C   
129   O O   . ARG A 34   ? 0.3346 0.4069 0.3303 -0.0041 0.0603  0.0878  32   ARG A O   
130   C CB  . ARG A 34   ? 0.3666 0.4435 0.3736 0.0006  0.0609  0.0792  32   ARG A CB  
131   C CG  . ARG A 34   ? 0.3840 0.4531 0.3961 0.0004  0.0585  0.0773  32   ARG A CG  
132   C CD  . ARG A 34   ? 0.3021 0.3559 0.3119 -0.0008 0.0550  0.0764  32   ARG A CD  
133   N NE  . ARG A 34   ? 0.3727 0.4204 0.3771 0.0028  0.0543  0.0710  32   ARG A NE  
134   C CZ  . ARG A 34   ? 0.3974 0.4412 0.4026 0.0063  0.0532  0.0657  32   ARG A CZ  
135   N NH1 . ARG A 34   ? 0.3927 0.4380 0.4037 0.0069  0.0527  0.0648  32   ARG A NH1 
136   N NH2 . ARG A 34   ? 0.3653 0.4033 0.3660 0.0091  0.0525  0.0614  32   ARG A NH2 
137   N N   . ARG A 35   ? 0.3066 0.4041 0.3065 -0.0035 0.0656  0.0906  33   ARG A N   
138   C CA  . ARG A 35   ? 0.3295 0.4335 0.3229 -0.0029 0.0671  0.0923  33   ARG A CA  
139   C C   . ARG A 35   ? 0.3551 0.4543 0.3480 -0.0081 0.0654  0.1007  33   ARG A C   
140   O O   . ARG A 35   ? 0.3291 0.4258 0.3161 -0.0077 0.0648  0.1012  33   ARG A O   
141   C CB  . ARG A 35   ? 0.3529 0.4767 0.3461 -0.0014 0.0712  0.0929  33   ARG A CB  
142   C CG  . ARG A 35   ? 0.4055 0.5347 0.3986 0.0048  0.0728  0.0833  33   ARG A CG  
143   C CD  . ARG A 35   ? 0.5195 0.6698 0.5134 0.0065  0.0769  0.0832  33   ARG A CD  
144   N NE  . ARG A 35   ? 0.6008 0.7548 0.5953 0.0129  0.0777  0.0730  33   ARG A NE  
145   C CZ  . ARG A 35   ? 0.6239 0.7788 0.6132 0.0176  0.0779  0.0658  33   ARG A CZ  
146   N NH1 . ARG A 35   ? 0.6358 0.7902 0.6181 0.0168  0.0777  0.0678  33   ARG A NH1 
147   N NH2 . ARG A 35   ? 0.5330 0.6892 0.5246 0.0233  0.0779  0.0563  33   ARG A NH2 
148   N N   . ALA A 36   ? 0.2905 0.3884 0.2901 -0.0130 0.0642  0.1073  34   ALA A N   
149   C CA  . ALA A 36   ? 0.3241 0.4158 0.3248 -0.0179 0.0618  0.1150  34   ALA A CA  
150   C C   . ALA A 36   ? 0.3221 0.3962 0.3203 -0.0174 0.0580  0.1114  34   ALA A C   
151   O O   . ALA A 36   ? 0.3254 0.3945 0.3215 -0.0192 0.0562  0.1152  34   ALA A O   
152   C CB  . ALA A 36   ? 0.2975 0.3906 0.3073 -0.0231 0.0608  0.1219  34   ALA A CB  
153   N N   . ILE A 37   ? 0.3198 0.3851 0.3189 -0.0149 0.0567  0.1045  35   ILE A N   
154   C CA  . ILE A 37   ? 0.3427 0.3931 0.3390 -0.0140 0.0535  0.1005  35   ILE A CA  
155   C C   . ILE A 37   ? 0.3140 0.3641 0.3021 -0.0107 0.0543  0.0972  35   ILE A C   
156   O O   . ILE A 37   ? 0.3023 0.3452 0.2875 -0.0118 0.0522  0.0989  35   ILE A O   
157   C CB  . ILE A 37   ? 0.3240 0.3674 0.3225 -0.0120 0.0523  0.0941  35   ILE A CB  
158   C CG1 . ILE A 37   ? 0.2868 0.3295 0.2933 -0.0156 0.0509  0.0974  35   ILE A CG1 
159   C CG2 . ILE A 37   ? 0.2609 0.2912 0.2556 -0.0105 0.0496  0.0895  35   ILE A CG2 
160   C CD1 . ILE A 37   ? 0.2797 0.3186 0.2886 -0.0136 0.0501  0.0919  35   ILE A CD1 
161   N N   . THR A 38   ? 0.3488 0.4066 0.3336 -0.0064 0.0569  0.0920  36   THR A N   
162   C CA  . THR A 38   ? 0.3281 0.3858 0.3056 -0.0030 0.0573  0.0877  36   THR A CA  
163   C C   . THR A 38   ? 0.3475 0.4118 0.3213 -0.0049 0.0581  0.0938  36   THR A C   
164   O O   . THR A 38   ? 0.3384 0.3972 0.3072 -0.0041 0.0567  0.0929  36   THR A O   
165   C CB  . THR A 38   ? 0.3153 0.3814 0.2914 0.0020  0.0599  0.0808  36   THR A CB  
166   O OG1 . THR A 38   ? 0.3367 0.3972 0.3174 0.0033  0.0589  0.0766  36   THR A OG1 
167   C CG2 . THR A 38   ? 0.3656 0.4292 0.3352 0.0058  0.0596  0.0749  36   THR A CG2 
168   N N   . ALA A 39   ? 0.3235 0.3998 0.3002 -0.0076 0.0601  0.1006  37   ALA A N   
169   C CA  . ALA A 39   ? 0.3422 0.4262 0.3160 -0.0099 0.0608  0.1078  37   ALA A CA  
170   C C   . ALA A 39   ? 0.3534 0.4249 0.3279 -0.0133 0.0570  0.1127  37   ALA A C   
171   O O   . ALA A 39   ? 0.3490 0.4228 0.3193 -0.0140 0.0566  0.1165  37   ALA A O   
172   C CB  . ALA A 39   ? 0.3292 0.4281 0.3073 -0.0130 0.0633  0.1152  37   ALA A CB  
173   N N   . ALA A 40   ? 0.3232 0.3818 0.3030 -0.0154 0.0540  0.1123  38   ALA A N   
174   C CA  . ALA A 40   ? 0.3172 0.3642 0.2993 -0.0185 0.0502  0.1164  38   ALA A CA  
175   C C   . ALA A 40   ? 0.3257 0.3602 0.3033 -0.0158 0.0479  0.1099  38   ALA A C   
176   O O   . ALA A 40   ? 0.3431 0.3678 0.3225 -0.0178 0.0446  0.1121  38   ALA A O   
177   C CB  . ALA A 40   ? 0.2962 0.3370 0.2874 -0.0223 0.0479  0.1192  38   ALA A CB  
178   N N   . TYR A 41   ? 0.3252 0.3602 0.2976 -0.0113 0.0495  0.1019  39   TYR A N   
179   C CA  . TYR A 41   ? 0.3141 0.3372 0.2835 -0.0088 0.0473  0.0952  39   TYR A CA  
180   C C   . TYR A 41   ? 0.3708 0.3876 0.3373 -0.0098 0.0449  0.0976  39   TYR A C   
181   O O   . TYR A 41   ? 0.3537 0.3590 0.3221 -0.0106 0.0418  0.0962  39   TYR A O   
182   C CB  . TYR A 41   ? 0.3130 0.3401 0.2773 -0.0040 0.0495  0.0876  39   TYR A CB  
183   C CG  . TYR A 41   ? 0.3495 0.3659 0.3128 -0.0015 0.0478  0.0802  39   TYR A CG  
184   C CD1 . TYR A 41   ? 0.3118 0.3164 0.2751 -0.0027 0.0446  0.0798  39   TYR A CD1 
185   C CD2 . TYR A 41   ? 0.3490 0.3677 0.3117 0.0022  0.0491  0.0738  39   TYR A CD2 
186   C CE1 . TYR A 41   ? 0.3545 0.3508 0.3167 -0.0006 0.0432  0.0737  39   TYR A CE1 
187   C CE2 . TYR A 41   ? 0.3277 0.3372 0.2899 0.0041  0.0474  0.0681  39   TYR A CE2 
188   C CZ  . TYR A 41   ? 0.3640 0.3627 0.3258 0.0026  0.0446  0.0682  39   TYR A CZ  
189   O OH  . TYR A 41   ? 0.3292 0.3200 0.2907 0.0042  0.0430  0.0631  39   TYR A OH  
190   N N   . ARG A 42   ? 0.3416 0.3666 0.3037 -0.0095 0.0461  0.1012  40   ARG A N   
191   C CA  . ARG A 42   ? 0.3520 0.3721 0.3112 -0.0100 0.0438  0.1035  40   ARG A CA  
192   C C   . ARG A 42   ? 0.3941 0.4220 0.3546 -0.0134 0.0438  0.1134  40   ARG A C   
193   O O   . ARG A 42   ? 0.3869 0.4183 0.3429 -0.0130 0.0435  0.1162  40   ARG A O   
194   C CB  . ARG A 42   ? 0.4039 0.4250 0.3553 -0.0058 0.0446  0.0970  40   ARG A CB  
195   C CG  . ARG A 42   ? 0.3608 0.3717 0.3118 -0.0032 0.0436  0.0885  40   ARG A CG  
196   C CD  . ARG A 42   ? 0.3876 0.3996 0.3324 0.0010  0.0444  0.0815  40   ARG A CD  
197   N NE  . ARG A 42   ? 0.3744 0.3801 0.3206 0.0031  0.0442  0.0744  40   ARG A NE  
198   C CZ  . ARG A 42   ? 0.3681 0.3623 0.3156 0.0029  0.0417  0.0716  40   ARG A CZ  
199   N NH1 . ARG A 42   ? 0.3644 0.3517 0.3118 0.0011  0.0391  0.0740  40   ARG A NH1 
200   N NH2 . ARG A 42   ? 0.3595 0.3499 0.3088 0.0044  0.0416  0.0663  40   ARG A NH2 
201   N N   . ARG A 43   ? 0.3631 0.3939 0.3306 -0.0170 0.0438  0.1193  41   ARG A N   
202   C CA  . ARG A 43   ? 0.4127 0.4517 0.3827 -0.0208 0.0438  0.1298  41   ARG A CA  
203   C C   . ARG A 43   ? 0.4223 0.4521 0.3943 -0.0230 0.0396  0.1346  41   ARG A C   
204   O O   . ARG A 43   ? 0.3913 0.4075 0.3671 -0.0233 0.0363  0.1315  41   ARG A O   
205   C CB  . ARG A 43   ? 0.3744 0.4167 0.3528 -0.0245 0.0442  0.1347  41   ARG A CB  
206   C CG  . ARG A 43   ? 0.3815 0.4304 0.3650 -0.0294 0.0433  0.1466  41   ARG A CG  
207   C CD  . ARG A 43   ? 0.4261 0.4804 0.4173 -0.0325 0.0445  0.1503  41   ARG A CD  
208   N NE  . ARG A 43   ? 0.3945 0.4618 0.3819 -0.0298 0.0492  0.1463  41   ARG A NE  
209   C CZ  . ARG A 43   ? 0.3891 0.4591 0.3815 -0.0304 0.0506  0.1447  41   ARG A CZ  
210   N NH1 . ARG A 43   ? 0.3849 0.4458 0.3860 -0.0336 0.0477  0.1463  41   ARG A NH1 
211   N NH2 . ARG A 43   ? 0.3793 0.4618 0.3684 -0.0276 0.0548  0.1410  41   ARG A NH2 
212   N N   . PRO A 44   ? 0.4228 0.4602 0.3925 -0.0243 0.0395  0.1421  42   PRO A N   
213   C CA  . PRO A 44   ? 0.4303 0.4589 0.4024 -0.0262 0.0352  0.1471  42   PRO A CA  
214   C C   . PRO A 44   ? 0.4470 0.4652 0.4302 -0.0302 0.0313  0.1510  42   PRO A C   
215   O O   . PRO A 44   ? 0.4010 0.4236 0.3907 -0.0333 0.0320  0.1555  42   PRO A O   
216   C CB  . PRO A 44   ? 0.4817 0.5239 0.4510 -0.0279 0.0363  0.1567  42   PRO A CB  
217   C CG  . PRO A 44   ? 0.4910 0.5475 0.4520 -0.0246 0.0413  0.1521  42   PRO A CG  
218   C CD  . PRO A 44   ? 0.4831 0.5381 0.4472 -0.0237 0.0434  0.1457  42   PRO A CD  
219   N N   . GLU A 45   ? 0.4611 0.4658 0.4469 -0.0299 0.0270  0.1487  43   GLU A N   
220   C CA  . GLU A 45   ? 0.4352 0.4285 0.4316 -0.0328 0.0228  0.1499  43   GLU A CA  
221   C C   . GLU A 45   ? 0.4457 0.4425 0.4510 -0.0380 0.0206  0.1620  43   GLU A C   
222   O O   . GLU A 45   ? 0.4218 0.4139 0.4369 -0.0410 0.0183  0.1634  43   GLU A O   
223   C CB  . GLU A 45   ? 0.4646 0.4445 0.4612 -0.0308 0.0188  0.1444  43   GLU A CB  
224   C CG  . GLU A 45   ? 0.4624 0.4303 0.4672 -0.0315 0.0154  0.1394  43   GLU A CG  
225   C CD  . GLU A 45   ? 0.4066 0.3641 0.4086 -0.0282 0.0131  0.1308  43   GLU A CD  
226   O OE1 . GLU A 45   ? 0.4117 0.3711 0.4049 -0.0251 0.0147  0.1279  43   GLU A OE1 
227   O OE2 . GLU A 45   ? 0.4139 0.3620 0.4227 -0.0286 0.0097  0.1268  43   GLU A OE2 
228   N N   . THR A 46   ? 0.4273 0.4325 0.4295 -0.0386 0.0207  0.1678  44   THR A N   
229   C CA  . THR A 46   ? 0.4466 0.4566 0.4569 -0.0426 0.0184  0.1754  44   THR A CA  
230   C C   . THR A 46   ? 0.4660 0.4871 0.4786 -0.0446 0.0217  0.1776  44   THR A C   
231   O O   . THR A 46   ? 0.4349 0.4570 0.4571 -0.0484 0.0194  0.1827  44   THR A O   
232   C CB  . THR A 46   ? 0.4911 0.5090 0.4967 -0.0424 0.0179  0.1807  44   THR A CB  
233   O OG1 . THR A 46   ? 0.4227 0.4532 0.4166 -0.0394 0.0232  0.1786  44   THR A OG1 
234   C CG2 . THR A 46   ? 0.4211 0.4272 0.4269 -0.0410 0.0136  0.1795  44   THR A CG2 
235   N N   . GLU A 47   ? 0.4406 0.4704 0.4454 -0.0421 0.0271  0.1737  45   GLU A N   
236   C CA  . GLU A 47   ? 0.4786 0.5191 0.4859 -0.0437 0.0303  0.1751  45   GLU A CA  
237   C C   . GLU A 47   ? 0.4566 0.4884 0.4708 -0.0447 0.0296  0.1715  45   GLU A C   
238   O O   . GLU A 47   ? 0.4139 0.4513 0.4346 -0.0475 0.0302  0.1742  45   GLU A O   
239   C CB  . GLU A 47   ? 0.4668 0.5213 0.4636 -0.0403 0.0363  0.1721  45   GLU A CB  
240   C CG  . GLU A 47   ? 0.5614 0.6267 0.5512 -0.0392 0.0371  0.1753  45   GLU A CG  
241   C CD  . GLU A 47   ? 0.6361 0.7150 0.6155 -0.0352 0.0427  0.1708  45   GLU A CD  
242   O OE1 . GLU A 47   ? 0.6418 0.7250 0.6210 -0.0340 0.0462  0.1670  45   GLU A OE1 
243   O OE2 . GLU A 47   ? 0.7133 0.7988 0.6851 -0.0331 0.0434  0.1709  45   GLU A OE2 
244   N N   . CYS A 48   ? 0.4327 0.4517 0.4461 -0.0427 0.0282  0.1656  46   CYS A N   
245   C CA  . CYS A 48   ? 0.4123 0.4242 0.4317 -0.0432 0.0274  0.1604  46   CYS A CA  
246   C C   . CYS A 48   ? 0.4222 0.4257 0.4543 -0.0476 0.0222  0.1648  46   CYS A C   
247   O O   . CYS A 48   ? 0.3723 0.3765 0.4117 -0.0499 0.0221  0.1650  46   CYS A O   
248   C CB  . CYS A 48   ? 0.4008 0.4022 0.4148 -0.0386 0.0269  0.1486  46   CYS A CB  
249   S SG  . CYS A 48   ? 0.4403 0.4494 0.4409 -0.0329 0.0322  0.1406  46   CYS A SG  
250   N N   . LEU A 49   ? 0.3948 0.3906 0.4302 -0.0483 0.0176  0.1669  47   LEU A N   
251   C CA  . LEU A 49   ? 0.4436 0.4285 0.4913 -0.0512 0.0118  0.1675  47   LEU A CA  
252   C C   . LEU A 49   ? 0.3756 0.3665 0.4331 -0.0556 0.0103  0.1740  47   LEU A C   
253   O O   . LEU A 49   ? 0.4652 0.4504 0.5323 -0.0577 0.0077  0.1725  47   LEU A O   
254   C CB  . LEU A 49   ? 0.4155 0.3905 0.4644 -0.0503 0.0072  0.1675  47   LEU A CB  
255   C CG  . LEU A 49   ? 0.4317 0.3936 0.4803 -0.0477 0.0051  0.1597  47   LEU A CG  
256   C CD1 . LEU A 49   ? 0.4303 0.3849 0.4895 -0.0497 0.0022  0.1562  47   LEU A CD1 
257   C CD2 . LEU A 49   ? 0.3846 0.3503 0.4206 -0.0432 0.0101  0.1520  47   LEU A CD2 
258   N N   . PRO A 50   ? 0.4588 0.4609 0.5151 -0.0571 0.0115  0.1811  48   PRO A N   
259   C CA  . PRO A 50   ? 0.4487 0.4556 0.5160 -0.0616 0.0092  0.1878  48   PRO A CA  
260   C C   . PRO A 50   ? 0.4036 0.4136 0.4758 -0.0633 0.0109  0.1862  48   PRO A C   
261   O O   . PRO A 50   ? 0.4667 0.4712 0.5508 -0.0664 0.0068  0.1874  48   PRO A O   
262   C CB  . PRO A 50   ? 0.4369 0.4587 0.4988 -0.0621 0.0120  0.1948  48   PRO A CB  
263   C CG  . PRO A 50   ? 0.4906 0.5098 0.5430 -0.0587 0.0124  0.1928  48   PRO A CG  
264   C CD  . PRO A 50   ? 0.4452 0.4558 0.4916 -0.0551 0.0141  0.1837  48   PRO A CD  
265   N N   . PRO A 51   ? 0.4168 0.4354 0.4811 -0.0613 0.0166  0.1833  49   PRO A N   
266   C CA  . PRO A 51   ? 0.4526 0.4735 0.5225 -0.0629 0.0179  0.1817  49   PRO A CA  
267   C C   . PRO A 51   ? 0.4037 0.4105 0.4794 -0.0628 0.0146  0.1753  49   PRO A C   
268   O O   . PRO A 51   ? 0.4482 0.4543 0.5329 -0.0654 0.0131  0.1752  49   PRO A O   
269   C CB  . PRO A 51   ? 0.4455 0.4785 0.5051 -0.0600 0.0246  0.1792  49   PRO A CB  
270   C CG  . PRO A 51   ? 0.4381 0.4691 0.4867 -0.0560 0.0261  0.1762  49   PRO A CG  
271   C CD  . PRO A 51   ? 0.4224 0.4494 0.4733 -0.0574 0.0220  0.1810  49   PRO A CD  
272   N N   . LEU A 52   ? 0.4163 0.4125 0.4874 -0.0598 0.0133  0.1699  50   LEU A N   
273   C CA  . LEU A 52   ? 0.3871 0.3704 0.4644 -0.0598 0.0097  0.1639  50   LEU A CA  
274   C C   . LEU A 52   ? 0.4444 0.4191 0.5346 -0.0629 0.0029  0.1659  50   LEU A C   
275   O O   . LEU A 52   ? 0.3918 0.3611 0.4917 -0.0649 -0.0002 0.1633  50   LEU A O   
276   C CB  . LEU A 52   ? 0.3598 0.3354 0.4280 -0.0551 0.0101  0.1559  50   LEU A CB  
277   C CG  . LEU A 52   ? 0.3746 0.3577 0.4300 -0.0506 0.0160  0.1499  50   LEU A CG  
278   C CD1 . LEU A 52   ? 0.3770 0.3546 0.4223 -0.0459 0.0163  0.1433  50   LEU A CD1 
279   C CD2 . LEU A 52   ? 0.3597 0.3437 0.4162 -0.0496 0.0173  0.1429  50   LEU A CD2 
280   N N   . VAL A 53   ? 0.4389 0.4125 0.5298 -0.0633 0.0004  0.1703  51   VAL A N   
281   C CA  . VAL A 53   ? 0.4761 0.4426 0.5802 -0.0662 -0.0062 0.1729  51   VAL A CA  
282   C C   . VAL A 53   ? 0.4465 0.4193 0.5606 -0.0704 -0.0070 0.1776  51   VAL A C   
283   O O   . VAL A 53   ? 0.4598 0.4253 0.5860 -0.0726 -0.0119 0.1758  51   VAL A O   
284   C CB  . VAL A 53   ? 0.4743 0.4410 0.5771 -0.0660 -0.0082 0.1782  51   VAL A CB  
285   C CG1 . VAL A 53   ? 0.5050 0.4660 0.6225 -0.0693 -0.0150 0.1820  51   VAL A CG1 
286   C CG2 . VAL A 53   ? 0.3920 0.3507 0.4869 -0.0620 -0.0084 0.1728  51   VAL A CG2 
287   N N   . GLU A 54   ? 0.4528 0.4396 0.5623 -0.0715 -0.0023 0.1831  52   GLU A N   
288   C CA  . GLU A 54   ? 0.4460 0.4396 0.5650 -0.0755 -0.0029 0.1879  52   GLU A CA  
289   C C   . GLU A 54   ? 0.4555 0.4459 0.5789 -0.0759 -0.0027 0.1820  52   GLU A C   
290   O O   . GLU A 54   ? 0.4701 0.4576 0.6058 -0.0792 -0.0067 0.1828  52   GLU A O   
291   C CB  . GLU A 54   ? 0.4324 0.4428 0.5452 -0.0762 0.0024  0.1945  52   GLU A CB  
292   N N   . ALA A 55   ? 0.4416 0.4326 0.5556 -0.0728 0.0017  0.1760  53   ALA A N   
293   C CA  . ALA A 55   ? 0.4269 0.4161 0.5447 -0.0732 0.0021  0.1709  53   ALA A CA  
294   C C   . ALA A 55   ? 0.4412 0.4157 0.5677 -0.0735 -0.0039 0.1647  53   ALA A C   
295   O O   . ALA A 55   ? 0.4251 0.3977 0.5598 -0.0753 -0.0057 0.1618  53   ALA A O   
296   C CB  . ALA A 55   ? 0.4190 0.4132 0.5248 -0.0696 0.0082  0.1666  53   ALA A CB  
297   N N   . ALA A 56   ? 0.4370 0.4017 0.5624 -0.0716 -0.0072 0.1623  54   ALA A N   
298   C CA  . ALA A 56   ? 0.4316 0.3829 0.5651 -0.0713 -0.0130 0.1555  54   ALA A CA  
299   C C   . ALA A 56   ? 0.4945 0.4404 0.6425 -0.0744 -0.0197 0.1580  54   ALA A C   
300   O O   . ALA A 56   ? 0.4879 0.4232 0.6444 -0.0742 -0.0252 0.1517  54   ALA A O   
301   C CB  . ALA A 56   ? 0.3918 0.3352 0.5172 -0.0673 -0.0132 0.1508  54   ALA A CB  
302   N N   . THR A 57   ? 0.5532 0.5067 0.7047 -0.0772 -0.0197 0.1666  55   THR A N   
303   C CA  . THR A 57   ? 0.5173 0.4663 0.6828 -0.0801 -0.0263 0.1700  55   THR A CA  
304   C C   . THR A 57   ? 0.4889 0.4353 0.6675 -0.0829 -0.0300 0.1670  55   THR A C   
305   O O   . THR A 57   ? 0.4878 0.4421 0.6657 -0.0844 -0.0265 0.1680  55   THR A O   
306   C CB  . THR A 57   ? 0.5262 0.4857 0.6916 -0.0824 -0.0249 0.1808  55   THR A CB  
307   O OG1 . THR A 57   ? 0.5008 0.4630 0.6542 -0.0798 -0.0217 0.1831  55   THR A OG1 
308   C CG2 . THR A 57   ? 0.6115 0.5663 0.7919 -0.0855 -0.0319 0.1851  55   THR A CG2 
309   N N   . GLN A 58   ? 0.4618 0.3974 0.6526 -0.0833 -0.0372 0.1629  56   GLN A N   
310   C CA  . GLN A 58   ? 0.5137 0.4463 0.7183 -0.0860 -0.0417 0.1596  56   GLN A CA  
311   C C   . GLN A 58   ? 0.5638 0.4922 0.7829 -0.0883 -0.0487 0.1637  56   GLN A C   
312   O O   . GLN A 58   ? 0.5314 0.4570 0.7503 -0.0874 -0.0507 0.1671  56   GLN A O   
313   C CB  . GLN A 58   ? 0.4968 0.4200 0.7033 -0.0837 -0.0442 0.1475  56   GLN A CB  
314   C CG  . GLN A 58   ? 0.4644 0.3907 0.6573 -0.0812 -0.0380 0.1432  56   GLN A CG  
315   C CD  . GLN A 58   ? 0.4894 0.4094 0.6867 -0.0803 -0.0406 0.1324  56   GLN A CD  
316   O OE1 . GLN A 58   ? 0.4569 0.3793 0.6624 -0.0828 -0.0420 0.1306  56   GLN A OE1 
317   N NE2 . GLN A 58   ? 0.4671 0.3806 0.6577 -0.0759 -0.0411 0.1238  56   GLN A NE2 
318   N N   . SER A 59   ? 0.5060 0.4342 0.7384 -0.0914 -0.0526 0.1631  57   SER A N   
319   C CA  . SER A 59   ? 0.5226 0.4480 0.7698 -0.0941 -0.0592 0.1680  57   SER A CA  
320   C C   . SER A 59   ? 0.5741 0.4870 0.8284 -0.0915 -0.0659 0.1616  57   SER A C   
321   O O   . SER A 59   ? 0.5304 0.4362 0.7803 -0.0880 -0.0662 0.1517  57   SER A O   
322   C CB  . SER A 59   ? 0.5271 0.4543 0.7874 -0.0976 -0.0622 0.1676  57   SER A CB  
323   O OG  . SER A 59   ? 0.5293 0.4491 0.7939 -0.0960 -0.0651 0.1556  57   SER A OG  
324   N N   . LYS A 60   ? 0.5582 0.4690 0.8238 -0.0932 -0.0713 0.1675  58   LYS A N   
325   C CA  . LYS A 60   ? 0.5673 0.4667 0.8425 -0.0909 -0.0786 0.1614  58   LYS A CA  
326   C C   . LYS A 60   ? 0.5679 0.4596 0.8522 -0.0897 -0.0832 0.1489  58   LYS A C   
327   O O   . LYS A 60   ? 0.5411 0.4246 0.8250 -0.0858 -0.0857 0.1388  58   LYS A O   
328   C CB  . LYS A 60   ? 0.5815 0.4807 0.8701 -0.0936 -0.0843 0.1703  58   LYS A CB  
329   C CG  . LYS A 60   ? 0.5702 0.4580 0.8716 -0.0915 -0.0927 0.1641  58   LYS A CG  
330   C CD  . LYS A 60   ? 0.6111 0.4939 0.9029 -0.0871 -0.0917 0.1600  58   LYS A CD  
331   C CE  . LYS A 60   ? 0.6255 0.4979 0.9311 -0.0848 -0.1003 0.1539  58   LYS A CE  
332   N NZ  . LYS A 60   ? 0.6251 0.4924 0.9221 -0.0804 -0.0997 0.1489  58   LYS A NZ  
333   N N   . GLU A 61   ? 0.4851 0.3801 0.7777 -0.0928 -0.0842 0.1490  59   GLU A N   
334   C CA  . GLU A 61   ? 0.5360 0.4248 0.8381 -0.0918 -0.0889 0.1370  59   GLU A CA  
335   C C   . GLU A 61   ? 0.5325 0.4198 0.8229 -0.0885 -0.0850 0.1265  59   GLU A C   
336   O O   . GLU A 61   ? 0.5299 0.4097 0.8248 -0.0855 -0.0893 0.1145  59   GLU A O   
337   C CB  . GLU A 61   ? 0.4706 0.3647 0.7825 -0.0960 -0.0900 0.1400  59   GLU A CB  
338   N N   . ILE A 62   ? 0.4706 0.3654 0.7460 -0.0888 -0.0770 0.1307  60   ILE A N   
339   C CA  . ILE A 62   ? 0.5319 0.4257 0.7963 -0.0859 -0.0732 0.1217  60   ILE A CA  
340   C C   . ILE A 62   ? 0.5161 0.4032 0.7732 -0.0815 -0.0734 0.1171  60   ILE A C   
341   O O   . ILE A 62   ? 0.5097 0.3916 0.7647 -0.0784 -0.0746 0.1059  60   ILE A O   
342   C CB  . ILE A 62   ? 0.5084 0.4126 0.7598 -0.0873 -0.0647 0.1277  60   ILE A CB  
343   C CG1 . ILE A 62   ? 0.5097 0.4193 0.7684 -0.0906 -0.0649 0.1271  60   ILE A CG1 
344   C CG2 . ILE A 62   ? 0.4780 0.3812 0.7153 -0.0837 -0.0600 0.1215  60   ILE A CG2 
345   C CD1 . ILE A 62   ? 0.4983 0.4186 0.7455 -0.0917 -0.0569 0.1320  60   ILE A CD1 
346   N N   . ARG A 63   ? 0.5150 0.4028 0.7678 -0.0811 -0.0723 0.1254  61   ARG A N   
347   C CA  . ARG A 63   ? 0.5099 0.3915 0.7560 -0.0770 -0.0727 0.1214  61   ARG A CA  
348   C C   . ARG A 63   ? 0.5519 0.4236 0.8105 -0.0746 -0.0807 0.1110  61   ARG A C   
349   O O   . ARG A 63   ? 0.5149 0.3813 0.7693 -0.0707 -0.0813 0.1012  61   ARG A O   
350   C CB  . ARG A 63   ? 0.5342 0.4191 0.7749 -0.0775 -0.0706 0.1326  61   ARG A CB  
351   C CG  . ARG A 63   ? 0.5703 0.4651 0.7954 -0.0782 -0.0620 0.1400  61   ARG A CG  
352   C CD  . ARG A 63   ? 0.6185 0.5174 0.8375 -0.0783 -0.0600 0.1500  61   ARG A CD  
353   N NE  . ARG A 63   ? 0.6455 0.5486 0.8753 -0.0823 -0.0630 0.1594  61   ARG A NE  
354   C CZ  . ARG A 63   ? 0.6426 0.5424 0.8801 -0.0826 -0.0679 0.1638  61   ARG A CZ  
355   N NH1 . ARG A 63   ? 0.6367 0.5292 0.8723 -0.0792 -0.0703 0.1596  61   ARG A NH1 
356   N NH2 . ARG A 63   ? 0.6140 0.5183 0.8618 -0.0865 -0.0706 0.1729  61   ARG A NH2 
357   N N   . ASP A 64   ? 0.5342 0.4038 0.8087 -0.0767 -0.0871 0.1128  62   ASP A N   
358   C CA  . ASP A 64   ? 0.5608 0.4220 0.8487 -0.0742 -0.0951 0.1020  62   ASP A CA  
359   C C   . ASP A 64   ? 0.5549 0.4146 0.8437 -0.0725 -0.0959 0.0885  62   ASP A C   
360   O O   . ASP A 64   ? 0.5397 0.3939 0.8295 -0.0684 -0.0990 0.0768  62   ASP A O   
361   C CB  . ASP A 64   ? 0.5271 0.3874 0.8326 -0.0772 -0.1016 0.1071  62   ASP A CB  
362   C CG  . ASP A 64   ? 0.5907 0.4513 0.8978 -0.0783 -0.1027 0.1186  62   ASP A CG  
363   O OD1 . ASP A 64   ? 0.5629 0.4239 0.8579 -0.0763 -0.0988 0.1215  62   ASP A OD1 
364   O OD2 . ASP A 64   ? 0.5858 0.4465 0.9066 -0.0812 -0.1075 0.1249  62   ASP A OD2 
365   N N   . ALA A 65   ? 0.4911 0.3565 0.7795 -0.0757 -0.0932 0.0899  63   ALA A N   
366   C CA  . ALA A 65   ? 0.5010 0.3664 0.7902 -0.0746 -0.0940 0.0775  63   ALA A CA  
367   C C   . ALA A 65   ? 0.5318 0.3967 0.8066 -0.0711 -0.0895 0.0709  63   ALA A C   
368   O O   . ALA A 65   ? 0.5416 0.4036 0.8181 -0.0682 -0.0923 0.0575  63   ALA A O   
369   C CB  . ALA A 65   ? 0.4768 0.3495 0.7673 -0.0789 -0.0912 0.0818  63   ALA A CB  
370   N N   . ALA A 66   ? 0.5036 0.3719 0.7642 -0.0714 -0.0825 0.0798  64   ALA A N   
371   C CA  . ALA A 66   ? 0.5375 0.4053 0.7845 -0.0682 -0.0782 0.0744  64   ALA A CA  
372   C C   . ALA A 66   ? 0.5674 0.4277 0.8145 -0.0636 -0.0818 0.0672  64   ALA A C   
373   O O   . ALA A 66   ? 0.5331 0.3950 0.7723 -0.0588 -0.0809 0.0552  64   ALA A O   
374   C CB  . ALA A 66   ? 0.5202 0.3954 0.7511 -0.0688 -0.0697 0.0854  64   ALA A CB  
375   N N   . ALA A 67   ? 0.4957 0.3531 0.7474 -0.0634 -0.0845 0.0733  65   ALA A N   
376   C CA  . ALA A 67   ? 0.5811 0.4318 0.8349 -0.0590 -0.0886 0.0665  65   ALA A CA  
377   C C   . ALA A 67   ? 0.5674 0.4142 0.8326 -0.0564 -0.0952 0.0514  65   ALA A C   
378   O O   . ALA A 67   ? 0.5671 0.4106 0.8301 -0.0520 -0.0969 0.0409  65   ALA A O   
379   C CB  . ALA A 67   ? 0.5307 0.3794 0.7905 -0.0599 -0.0914 0.0759  65   ALA A CB  
380   N N   . SER A 68   ? 0.5437 0.3917 0.8212 -0.0589 -0.0991 0.0495  66   SER A N   
381   C CA  . SER A 68   ? 0.5635 0.4093 0.8521 -0.0562 -0.1056 0.0346  66   SER A CA  
382   C C   . SER A 68   ? 0.5422 0.3912 0.8228 -0.0544 -0.1031 0.0230  66   SER A C   
383   O O   . SER A 68   ? 0.5534 0.4011 0.8354 -0.0501 -0.1063 0.0093  66   SER A O   
384   C CB  . SER A 68   ? 0.5155 0.3622 0.8194 -0.0594 -0.1104 0.0361  66   SER A CB  
385   O OG  . SER A 68   ? 0.5713 0.4170 0.8856 -0.0566 -0.1166 0.0211  66   SER A OG  
386   N N   . THR A 69   ? 0.5285 0.3841 0.7993 -0.0571 -0.0969 0.0280  67   THR A N   
387   C CA  . THR A 69   ? 0.5361 0.4016 0.7929 -0.0534 -0.0924 0.0175  67   THR A CA  
388   C C   . THR A 69   ? 0.4987 0.3660 0.7397 -0.0482 -0.0881 0.0135  67   THR A C   
389   O O   . THR A 69   ? 0.4875 0.3591 0.7237 -0.0438 -0.0884 0.0006  67   THR A O   
390   C CB  . THR A 69   ? 0.5115 0.3860 0.7589 -0.0563 -0.0858 0.0248  67   THR A CB  
391   O OG1 . THR A 69   ? 0.5250 0.3993 0.7875 -0.0606 -0.0903 0.0255  67   THR A OG1 
392   C CG2 . THR A 69   ? 0.4338 0.3185 0.6650 -0.0523 -0.0805 0.0160  67   THR A CG2 
393   N N   . ALA A 70   ? 0.5230 0.3877 0.7562 -0.0486 -0.0842 0.0243  68   ALA A N   
394   C CA  . ALA A 70   ? 0.5395 0.4056 0.7581 -0.0440 -0.0802 0.0212  68   ALA A CA  
395   C C   . ALA A 70   ? 0.5860 0.4458 0.8130 -0.0401 -0.0865 0.0108  68   ALA A C   
396   O O   . ALA A 70   ? 0.5460 0.4100 0.7638 -0.0354 -0.0848 0.0010  68   ALA A O   
397   C CB  . ALA A 70   ? 0.5002 0.3650 0.7099 -0.0455 -0.0752 0.0350  68   ALA A CB  
398   N N   . ARG A 71   ? 0.6201 0.4701 0.8652 -0.0421 -0.0939 0.0130  69   ARG A N   
399   C CA  . ARG A 71   ? 0.5953 0.4391 0.8512 -0.0383 -0.1010 0.0019  69   ARG A CA  
400   C C   . ARG A 71   ? 0.5802 0.4301 0.8385 -0.0351 -0.1034 -0.0147 69   ARG A C   
401   O O   . ARG A 71   ? 0.6333 0.4855 0.8880 -0.0301 -0.1043 -0.0262 69   ARG A O   
402   C CB  . ARG A 71   ? 0.5845 0.4216 0.8576 -0.0403 -0.1076 0.0075  69   ARG A CB  
403   C CG  . ARG A 71   ? 0.6641 0.4993 0.9500 -0.0359 -0.1152 -0.0057 69   ARG A CG  
404   C CD  . ARG A 71   ? 0.6433 0.4740 0.9425 -0.0366 -0.1205 0.0015  69   ARG A CD  
405   N NE  . ARG A 71   ? 0.6759 0.5034 0.9686 -0.0356 -0.1186 0.0096  69   ARG A NE  
406   C CZ  . ARG A 71   ? 0.6484 0.4741 0.9396 -0.0307 -0.1202 0.0020  69   ARG A CZ  
407   N NH1 . ARG A 71   ? 0.6630 0.4902 0.9585 -0.0261 -0.1237 -0.0141 69   ARG A NH1 
408   N NH2 . ARG A 71   ? 0.6455 0.4686 0.9302 -0.0303 -0.1181 0.0105  69   ARG A NH2 
409   N N   . LYS A 72   ? 0.5449 0.3987 0.8087 -0.0380 -0.1044 -0.0162 70   LYS A N   
410   C CA  . LYS A 72   ? 0.5588 0.4196 0.8247 -0.0352 -0.1069 -0.0318 70   LYS A CA  
411   C C   . LYS A 72   ? 0.6175 0.4898 0.8631 -0.0312 -0.0999 -0.0378 70   LYS A C   
412   O O   . LYS A 72   ? 0.6020 0.4792 0.8468 -0.0266 -0.1018 -0.0515 70   LYS A O   
413   C CB  . LYS A 72   ? 0.5199 0.3834 0.7944 -0.0394 -0.1087 -0.0309 70   LYS A CB  
414   C CG  . LYS A 72   ? 0.5848 0.4566 0.8617 -0.0365 -0.1116 -0.0472 70   LYS A CG  
415   C CD  . LYS A 72   ? 0.5811 0.4594 0.8589 -0.0401 -0.1104 -0.0457 70   LYS A CD  
416   C CE  . LYS A 72   ? 0.6655 0.5369 0.9659 -0.0437 -0.1189 -0.0471 70   LYS A CE  
417   N NZ  . LYS A 72   ? 0.6794 0.5596 0.9815 -0.0454 -0.1192 -0.0521 70   LYS A NZ  
418   N N   . LEU A 73   ? 0.5746 0.4519 0.8043 -0.0328 -0.0917 -0.0277 71   LEU A N   
419   C CA  . LEU A 73   ? 0.5325 0.4202 0.7435 -0.0294 -0.0851 -0.0321 71   LEU A CA  
420   C C   . LEU A 73   ? 0.5971 0.4833 0.8022 -0.0249 -0.0847 -0.0366 71   LEU A C   
421   O O   . LEU A 73   ? 0.5639 0.4583 0.7612 -0.0210 -0.0833 -0.0469 71   LEU A O   
422   C CB  . LEU A 73   ? 0.5191 0.4109 0.7160 -0.0320 -0.0771 -0.0197 71   LEU A CB  
423   C CG  . LEU A 73   ? 0.4846 0.3799 0.6847 -0.0363 -0.0761 -0.0144 71   LEU A CG  
424   C CD1 . LEU A 73   ? 0.4980 0.3968 0.6840 -0.0381 -0.0682 -0.0022 71   LEU A CD1 
425   C CD2 . LEU A 73   ? 0.4757 0.3804 0.6752 -0.0347 -0.0772 -0.0258 71   LEU A CD2 
426   N N   . ILE A 74   ? 0.5495 0.4262 0.7581 -0.0256 -0.0858 -0.0287 72   ILE A N   
427   C CA  . ILE A 74   ? 0.6060 0.4810 0.8095 -0.0214 -0.0855 -0.0323 72   ILE A CA  
428   C C   . ILE A 74   ? 0.6045 0.4780 0.8206 -0.0177 -0.0928 -0.0468 72   ILE A C   
429   O O   . ILE A 74   ? 0.5871 0.4643 0.7973 -0.0132 -0.0922 -0.0548 72   ILE A O   
430   C CB  . ILE A 74   ? 0.5635 0.4293 0.7675 -0.0234 -0.0848 -0.0191 72   ILE A CB  
431   C CG1 . ILE A 74   ? 0.5805 0.4505 0.7696 -0.0261 -0.0767 -0.0068 72   ILE A CG1 
432   C CG2 . ILE A 74   ? 0.6058 0.4686 0.8071 -0.0191 -0.0857 -0.0230 72   ILE A CG2 
433   C CD1 . ILE A 74   ? 0.6272 0.4901 0.8164 -0.0287 -0.0756 0.0071  72   ILE A CD1 
434   N N   . GLU A 75   ? 0.6199 0.4888 0.8537 -0.0193 -0.1000 -0.0511 73   GLU A N   
435   C CA  . GLU A 75   ? 0.6478 0.5162 0.8943 -0.0154 -0.1073 -0.0665 73   GLU A CA  
436   C C   . GLU A 75   ? 0.6646 0.5471 0.9015 -0.0117 -0.1049 -0.0799 73   GLU A C   
437   O O   . GLU A 75   ? 0.6312 0.5176 0.8679 -0.0068 -0.1067 -0.0913 73   GLU A O   
438   C CB  . GLU A 75   ? 0.6371 0.4981 0.9051 -0.0182 -0.1155 -0.0683 73   GLU A CB  
439   N N   . ALA A 76   ? 0.6255 0.5167 0.8542 -0.0138 -0.1007 -0.0783 74   ALA A N   
440   C CA  . ALA A 76   ? 0.6178 0.5235 0.8372 -0.0107 -0.0983 -0.0898 74   ALA A CA  
441   C C   . ALA A 76   ? 0.5868 0.4995 0.7874 -0.0080 -0.0913 -0.0884 74   ALA A C   
442   O O   . ALA A 76   ? 0.6570 0.5797 0.8528 -0.0039 -0.0911 -0.0997 74   ALA A O   
443   C CB  . ALA A 76   ? 0.6113 0.5239 0.8277 -0.0140 -0.0961 -0.0875 74   ALA A CB  
444   N N   . LEU A 77   ? 0.5836 0.4920 0.7739 -0.0102 -0.0855 -0.0746 75   LEU A N   
445   C CA  . LEU A 77   ? 0.5905 0.5047 0.7640 -0.0078 -0.0791 -0.0726 75   LEU A CA  
446   C C   . LEU A 77   ? 0.6181 0.5307 0.7943 -0.0034 -0.0819 -0.0805 75   LEU A C   
447   O O   . LEU A 77   ? 0.6396 0.5613 0.8051 -0.0002 -0.0785 -0.0860 75   LEU A O   
448   C CB  . LEU A 77   ? 0.5693 0.4778 0.7335 -0.0109 -0.0734 -0.0569 75   LEU A CB  
449   C CG  . LEU A 77   ? 0.5199 0.4345 0.6737 -0.0139 -0.0676 -0.0494 75   LEU A CG  
450   C CD1 . LEU A 77   ? 0.5348 0.4432 0.6817 -0.0165 -0.0629 -0.0350 75   LEU A CD1 
451   C CD2 . LEU A 77   ? 0.5532 0.4807 0.6934 -0.0114 -0.0631 -0.0553 75   LEU A CD2 
452   N N   . ARG A 78   ? 0.6186 0.5199 0.8096 -0.0033 -0.0881 -0.0809 76   ARG A N   
453   C CA  . ARG A 78   ? 0.6373 0.5365 0.8323 0.0011  -0.0912 -0.0885 76   ARG A CA  
454   C C   . ARG A 78   ? 0.6284 0.5343 0.8334 0.0050  -0.0970 -0.1059 76   ARG A C   
455   O O   . ARG A 78   ? 0.6551 0.5635 0.8610 0.0095  -0.0988 -0.1145 76   ARG A O   
456   C CB  . ARG A 78   ? 0.5708 0.4550 0.7771 -0.0002 -0.0954 -0.0804 76   ARG A CB  
457   C CG  . ARG A 78   ? 0.6116 0.4923 0.8049 -0.0016 -0.0892 -0.0668 76   ARG A CG  
458   C CD  . ARG A 78   ? 0.5535 0.4206 0.7567 -0.0036 -0.0928 -0.0568 76   ARG A CD  
459   N NE  . ARG A 78   ? 0.5985 0.4643 0.7886 -0.0037 -0.0872 -0.0467 76   ARG A NE  
460   C CZ  . ARG A 78   ? 0.6128 0.4689 0.8071 -0.0049 -0.0889 -0.0371 76   ARG A CZ  
461   N NH1 . ARG A 78   ? 0.6347 0.4806 0.8466 -0.0063 -0.0961 -0.0351 76   ARG A NH1 
462   N NH2 . ARG A 78   ? 0.6351 0.4919 0.8162 -0.0046 -0.0835 -0.0293 76   ARG A NH2 
463   N N   . GLY A 79   ? 0.6301 0.5400 0.8422 0.0037  -0.1000 -0.1116 77   GLY A N   
464   C CA  . GLY A 79   ? 0.6433 0.5620 0.8635 0.0075  -0.1050 -0.1289 77   GLY A CA  
465   C C   . GLY A 79   ? 0.6792 0.6154 0.8854 0.0087  -0.1001 -0.1349 77   GLY A C   
466   O O   . GLY A 79   ? 0.6887 0.6335 0.9006 0.0098  -0.1035 -0.1463 77   GLY A O   
467   N N   . LYS A 80   ? 0.7436 0.6855 0.9317 0.0083  -0.0922 -0.1273 78   LYS A N   
468   C CA  . LYS A 80   ? 0.7353 0.6939 0.9096 0.0090  -0.0872 -0.1310 78   LYS A CA  
469   C C   . LYS A 80   ? 0.6994 0.6628 0.8566 0.0100  -0.0800 -0.1248 78   LYS A C   
470   O O   . LYS A 80   ? 0.7458 0.7082 0.9028 0.0131  -0.0804 -0.1282 78   LYS A O   
471   C CB  . LYS A 80   ? 0.6569 0.6173 0.8282 0.0047  -0.0850 -0.1242 78   LYS A CB  
472   N N   . GLY A 85   ? 0.6034 0.6390 0.6674 0.0218  -0.0428 -0.1193 83   GLY A N   
473   C CA  . GLY A 85   ? 0.5525 0.6043 0.6049 0.0209  -0.0382 -0.1176 83   GLY A CA  
474   C C   . GLY A 85   ? 0.5066 0.5631 0.5526 0.0221  -0.0351 -0.1161 83   GLY A C   
475   O O   . GLY A 85   ? 0.5136 0.5833 0.5604 0.0251  -0.0359 -0.1255 83   GLY A O   
476   N N   . VAL A 86   ? 0.5069 0.5531 0.5466 0.0199  -0.0315 -0.1045 84   VAL A N   
477   C CA  . VAL A 86   ? 0.5214 0.5691 0.5567 0.0210  -0.0292 -0.1029 84   VAL A CA  
478   C C   . VAL A 86   ? 0.4852 0.5277 0.5303 0.0248  -0.0336 -0.1114 84   VAL A C   
479   O O   . VAL A 86   ? 0.4675 0.5175 0.5115 0.0272  -0.0331 -0.1161 84   VAL A O   
480   C CB  . VAL A 86   ? 0.5362 0.5721 0.5642 0.0181  -0.0253 -0.0894 84   VAL A CB  
481   N N   . GLU A 87   ? 0.5189 0.5487 0.5742 0.0254  -0.0381 -0.1136 85   GLU A N   
482   C CA  . GLU A 87   ? 0.5111 0.5346 0.5772 0.0290  -0.0430 -0.1212 85   GLU A CA  
483   C C   . GLU A 87   ? 0.5134 0.5523 0.5851 0.0330  -0.0460 -0.1362 85   GLU A C   
484   O O   . GLU A 87   ? 0.4706 0.5111 0.5473 0.0365  -0.0482 -0.1432 85   GLU A O   
485   C CB  . GLU A 87   ? 0.5818 0.5885 0.6584 0.0282  -0.0474 -0.1191 85   GLU A CB  
486   N N   . GLY A 88   ? 0.4605 0.5116 0.5317 0.0327  -0.0463 -0.1418 86   GLY A N   
487   C CA  . GLY A 88   ? 0.4655 0.5333 0.5415 0.0366  -0.0490 -0.1567 86   GLY A CA  
488   C C   . GLY A 88   ? 0.4504 0.5353 0.5171 0.0376  -0.0448 -0.1582 86   GLY A C   
489   O O   . GLY A 88   ? 0.4167 0.5133 0.4879 0.0416  -0.0469 -0.1699 86   GLY A O   
490   N N   . LEU A 89   ? 0.4723 0.5594 0.5267 0.0340  -0.0390 -0.1464 87   LEU A N   
491   C CA  . LEU A 89   ? 0.4445 0.5464 0.4903 0.0342  -0.0349 -0.1456 87   LEU A CA  
492   C C   . LEU A 89   ? 0.4104 0.5048 0.4590 0.0365  -0.0354 -0.1459 87   LEU A C   
493   O O   . LEU A 89   ? 0.3904 0.4976 0.4406 0.0397  -0.0359 -0.1546 87   LEU A O   
494   C CB  . LEU A 89   ? 0.4551 0.5584 0.4886 0.0295  -0.0293 -0.1322 87   LEU A CB  
495   C CG  . LEU A 89   ? 0.4581 0.5809 0.4817 0.0283  -0.0248 -0.1299 87   LEU A CG  
496   C CD1 . LEU A 89   ? 0.4658 0.5838 0.4799 0.0235  -0.0205 -0.1155 87   LEU A CD1 
497   C CD2 . LEU A 89   ? 0.4493 0.5762 0.4723 0.0302  -0.0237 -0.1319 87   LEU A CD2 
498   N N   . VAL A 90   ? 0.4058 0.4804 0.4552 0.0349  -0.0354 -0.1367 88   VAL A N   
499   C CA  . VAL A 90   ? 0.4098 0.4758 0.4624 0.0370  -0.0364 -0.1365 88   VAL A CA  
500   C C   . VAL A 90   ? 0.4321 0.5014 0.4969 0.0422  -0.0419 -0.1507 88   VAL A C   
501   O O   . VAL A 90   ? 0.4277 0.5032 0.4939 0.0451  -0.0421 -0.1558 88   VAL A O   
502   C CB  . VAL A 90   ? 0.3931 0.4373 0.4465 0.0348  -0.0367 -0.1254 88   VAL A CB  
503   C CG1 . VAL A 90   ? 0.4365 0.4713 0.4955 0.0374  -0.0390 -0.1265 88   VAL A CG1 
504   C CG2 . VAL A 90   ? 0.4157 0.4580 0.4569 0.0304  -0.0310 -0.1123 88   VAL A CG2 
505   N N   . GLN A 91   ? 0.4391 0.5049 0.5135 0.0435  -0.0467 -0.1579 89   GLN A N   
506   C CA  . GLN A 91   ? 0.4316 0.5001 0.5192 0.0486  -0.0526 -0.1724 89   GLN A CA  
507   C C   . GLN A 91   ? 0.4395 0.5322 0.5254 0.0517  -0.0518 -0.1844 89   GLN A C   
508   O O   . GLN A 91   ? 0.4357 0.5344 0.5272 0.0560  -0.0539 -0.1935 89   GLN A O   
509   C CB  . GLN A 91   ? 0.4816 0.5407 0.5804 0.0489  -0.0582 -0.1769 89   GLN A CB  
510   N N   . GLU A 92   ? 0.4199 0.5276 0.4981 0.0497  -0.0488 -0.1845 90   GLU A N   
511   C CA  . GLU A 92   ? 0.4574 0.5897 0.5348 0.0526  -0.0485 -0.1968 90   GLU A CA  
512   C C   . GLU A 92   ? 0.4220 0.5658 0.4931 0.0536  -0.0448 -0.1959 90   GLU A C   
513   O O   . GLU A 92   ? 0.4098 0.5691 0.4852 0.0579  -0.0463 -0.2083 90   GLU A O   
514   C CB  . GLU A 92   ? 0.4234 0.5699 0.4926 0.0497  -0.0457 -0.1950 90   GLU A CB  
515   C CG  . GLU A 92   ? 0.5039 0.6778 0.5723 0.0527  -0.0456 -0.2079 90   GLU A CG  
516   C CD  . GLU A 92   ? 0.5491 0.7378 0.6097 0.0498  -0.0432 -0.2060 90   GLU A CD  
517   O OE1 . GLU A 92   ? 0.4980 0.6746 0.5549 0.0458  -0.0421 -0.1955 90   GLU A OE1 
518   O OE2 . GLU A 92   ? 0.5203 0.7334 0.5784 0.0517  -0.0425 -0.2150 90   GLU A OE2 
519   N N   . TYR A 93   ? 0.4192 0.5556 0.4808 0.0498  -0.0401 -0.1819 91   TYR A N   
520   C CA  . TYR A 93   ? 0.3653 0.5129 0.4206 0.0501  -0.0362 -0.1799 91   TYR A CA  
521   C C   . TYR A 93   ? 0.3468 0.4783 0.4056 0.0512  -0.0371 -0.1759 91   TYR A C   
522   O O   . TYR A 93   ? 0.3521 0.4892 0.4049 0.0504  -0.0336 -0.1714 91   TYR A O   
523   C CB  . TYR A 93   ? 0.3663 0.5219 0.4079 0.0449  -0.0300 -0.1677 91   TYR A CB  
524   C CG  . TYR A 93   ? 0.3951 0.5720 0.4329 0.0443  -0.0289 -0.1726 91   TYR A CG  
525   C CD1 . TYR A 93   ? 0.4123 0.5854 0.4499 0.0423  -0.0300 -0.1709 91   TYR A CD1 
526   C CD2 . TYR A 93   ? 0.4015 0.6032 0.4362 0.0458  -0.0270 -0.1792 91   TYR A CD2 
527   C CE1 . TYR A 93   ? 0.4407 0.6340 0.4747 0.0419  -0.0292 -0.1755 91   TYR A CE1 
528   C CE2 . TYR A 93   ? 0.4163 0.6391 0.4473 0.0453  -0.0261 -0.1836 91   TYR A CE2 
529   C CZ  . TYR A 93   ? 0.4108 0.6292 0.4413 0.0434  -0.0273 -0.1818 91   TYR A CZ  
530   O OH  . TYR A 93   ? 0.4378 0.6777 0.4645 0.0429  -0.0265 -0.1862 91   TYR A OH  
531   N N   . SER A 94   ? 0.3613 0.4734 0.4298 0.0528  -0.0419 -0.1770 92   SER A N   
532   C CA  . SER A 94   ? 0.3656 0.4626 0.4385 0.0542  -0.0436 -0.1737 92   SER A CA  
533   C C   . SER A 94   ? 0.3574 0.4483 0.4189 0.0500  -0.0382 -0.1590 92   SER A C   
534   O O   . SER A 94   ? 0.3326 0.4247 0.3926 0.0510  -0.0370 -0.1577 92   SER A O   
535   C CB  . SER A 94   ? 0.3581 0.4658 0.4386 0.0596  -0.0462 -0.1863 92   SER A CB  
536   O OG  . SER A 94   ? 0.4134 0.5286 0.5045 0.0637  -0.0512 -0.2011 92   SER A OG  
537   N N   . LEU A 95   ? 0.3292 0.4140 0.3832 0.0454  -0.0353 -0.1484 93   LEU A N   
538   C CA  . LEU A 95   ? 0.3613 0.4401 0.4050 0.0413  -0.0305 -0.1348 93   LEU A CA  
539   C C   . LEU A 95   ? 0.3171 0.3744 0.3640 0.0411  -0.0323 -0.1278 93   LEU A C   
540   O O   . LEU A 95   ? 0.3600 0.4042 0.4143 0.0417  -0.0361 -0.1284 93   LEU A O   
541   C CB  . LEU A 95   ? 0.3540 0.4341 0.3893 0.0368  -0.0270 -0.1264 93   LEU A CB  
542   C CG  . LEU A 95   ? 0.3319 0.4335 0.3631 0.0364  -0.0251 -0.1315 93   LEU A CG  
543   C CD1 . LEU A 95   ? 0.3948 0.4953 0.4183 0.0318  -0.0220 -0.1219 93   LEU A CD1 
544   C CD2 . LEU A 95   ? 0.3195 0.4385 0.3460 0.0369  -0.0221 -0.1333 93   LEU A CD2 
545   N N   . SER A 96   ? 0.3029 0.3573 0.3443 0.0401  -0.0295 -0.1209 94   SER A N   
546   C CA  . SER A 96   ? 0.3407 0.3761 0.3817 0.0386  -0.0299 -0.1113 94   SER A CA  
547   C C   . SER A 96   ? 0.3257 0.3539 0.3591 0.0340  -0.0267 -0.1004 94   SER A C   
548   O O   . SER A 96   ? 0.2989 0.3370 0.3266 0.0318  -0.0239 -0.0992 94   SER A O   
549   C CB  . SER A 96   ? 0.3319 0.3678 0.3689 0.0389  -0.0278 -0.1077 94   SER A CB  
550   O OG  . SER A 96   ? 0.3015 0.3476 0.3282 0.0357  -0.0226 -0.1021 94   SER A OG  
551   N N   . SER A 97   ? 0.3061 0.3176 0.3394 0.0326  -0.0272 -0.0920 95   SER A N   
552   C CA  . SER A 97   ? 0.3645 0.3693 0.3910 0.0286  -0.0242 -0.0817 95   SER A CA  
553   C C   . SER A 97   ? 0.3349 0.3483 0.3508 0.0259  -0.0189 -0.0760 95   SER A C   
554   O O   . SER A 97   ? 0.3048 0.3223 0.3155 0.0232  -0.0164 -0.0721 95   SER A O   
555   C CB  . SER A 97   ? 0.3977 0.3852 0.4256 0.0277  -0.0253 -0.0738 95   SER A CB  
556   O OG  . SER A 97   ? 0.5271 0.5064 0.5651 0.0293  -0.0302 -0.0775 95   SER A OG  
557   N N   . GLN A 98   ? 0.2641 0.2803 0.2773 0.0266  -0.0176 -0.0751 96   GLN A N   
558   C CA  . GLN A 98   ? 0.2689 0.2929 0.2733 0.0238  -0.0130 -0.0695 96   GLN A CA  
559   C C   . GLN A 98   ? 0.2698 0.3118 0.2722 0.0234  -0.0115 -0.0742 96   GLN A C   
560   O O   . GLN A 98   ? 0.2654 0.3129 0.2611 0.0202  -0.0081 -0.0683 96   GLN A O   
561   C CB  . GLN A 98   ? 0.3022 0.3259 0.3051 0.0247  -0.0123 -0.0682 96   GLN A CB  
562   C CG  . GLN A 98   ? 0.3161 0.3234 0.3179 0.0241  -0.0127 -0.0608 96   GLN A CG  
563   C CD  . GLN A 98   ? 0.2574 0.2592 0.2520 0.0203  -0.0094 -0.0510 96   GLN A CD  
564   O OE1 . GLN A 98   ? 0.3307 0.3266 0.3256 0.0191  -0.0096 -0.0483 96   GLN A OE1 
565   N NE2 . GLN A 98   ? 0.3169 0.3210 0.3057 0.0185  -0.0065 -0.0460 96   GLN A NE2 
566   N N   . GLU A 99   ? 0.2854 0.3373 0.2938 0.0266  -0.0141 -0.0849 97   GLU A N   
567   C CA  . GLU A 99   ? 0.2617 0.3323 0.2681 0.0262  -0.0127 -0.0897 97   GLU A CA  
568   C C   . GLU A 99   ? 0.2820 0.3522 0.2868 0.0241  -0.0124 -0.0874 97   GLU A C   
569   O O   . GLU A 99   ? 0.2968 0.3782 0.2957 0.0215  -0.0096 -0.0842 97   GLU A O   
570   C CB  . GLU A 99   ? 0.2451 0.3273 0.2587 0.0305  -0.0157 -0.1028 97   GLU A CB  
571   C CG  . GLU A 99   ? 0.2378 0.3254 0.2518 0.0323  -0.0151 -0.1049 97   GLU A CG  
572   C CD  . GLU A 99   ? 0.2725 0.3690 0.2952 0.0373  -0.0187 -0.1183 97   GLU A CD  
573   O OE1 . GLU A 99   ? 0.3040 0.4005 0.3332 0.0396  -0.0221 -0.1262 97   GLU A OE1 
574   O OE2 . GLU A 99   ? 0.2734 0.3766 0.2970 0.0390  -0.0183 -0.1211 97   GLU A OE2 
575   N N   . GLY A 100  ? 0.2783 0.3358 0.2886 0.0249  -0.0155 -0.0887 98   GLY A N   
576   C CA  . GLY A 100  ? 0.3018 0.3582 0.3110 0.0229  -0.0153 -0.0863 98   GLY A CA  
577   C C   . GLY A 100  ? 0.2946 0.3465 0.2954 0.0187  -0.0114 -0.0743 98   GLY A C   
578   O O   . GLY A 100  ? 0.2759 0.3361 0.2726 0.0165  -0.0096 -0.0719 98   GLY A O   
579   N N   . VAL A 101  ? 0.2524 0.2916 0.2510 0.0178  -0.0103 -0.0669 99   VAL A N   
580   C CA  . VAL A 101  ? 0.2759 0.3110 0.2671 0.0142  -0.0067 -0.0562 99   VAL A CA  
581   C C   . VAL A 101  ? 0.2933 0.3432 0.2787 0.0125  -0.0036 -0.0542 99   VAL A C   
582   O O   . VAL A 101  ? 0.2965 0.3505 0.2774 0.0097  -0.0015 -0.0487 99   VAL A O   
583   C CB  . VAL A 101  ? 0.2871 0.3073 0.2772 0.0140  -0.0063 -0.0499 99   VAL A CB  
584   C CG1 . VAL A 101  ? 0.2620 0.2795 0.2451 0.0107  -0.0027 -0.0402 99   VAL A CG1 
585   C CG2 . VAL A 101  ? 0.3318 0.3380 0.3276 0.0150  -0.0092 -0.0501 99   VAL A CG2 
586   N N   . ALA A 102  ? 0.2581 0.3166 0.2440 0.0139  -0.0034 -0.0583 100  ALA A N   
587   C CA  . ALA A 102  ? 0.2689 0.3417 0.2497 0.0119  -0.0005 -0.0554 100  ALA A CA  
588   C C   . ALA A 102  ? 0.2525 0.3411 0.2322 0.0111  -0.0002 -0.0584 100  ALA A C   
589   O O   . ALA A 102  ? 0.2824 0.3789 0.2572 0.0080  0.0023  -0.0520 100  ALA A O   
590   C CB  . ALA A 102  ? 0.2401 0.3205 0.2223 0.0138  -0.0006 -0.0601 100  ALA A CB  
591   N N   . LEU A 103  ? 0.2862 0.3798 0.2710 0.0139  -0.0029 -0.0681 101  LEU A N   
592   C CA  . LEU A 103  ? 0.2839 0.3934 0.2680 0.0135  -0.0030 -0.0721 101  LEU A CA  
593   C C   . LEU A 103  ? 0.2883 0.3926 0.2691 0.0105  -0.0020 -0.0645 101  LEU A C   
594   O O   . LEU A 103  ? 0.2862 0.4028 0.2625 0.0081  -0.0001 -0.0605 101  LEU A O   
595   C CB  . LEU A 103  ? 0.2962 0.4096 0.2875 0.0175  -0.0068 -0.0847 101  LEU A CB  
596   C CG  . LEU A 103  ? 0.2724 0.4029 0.2638 0.0178  -0.0075 -0.0908 101  LEU A CG  
597   C CD1 . LEU A 103  ? 0.2784 0.4317 0.2653 0.0171  -0.0050 -0.0920 101  LEU A CD1 
598   C CD2 . LEU A 103  ? 0.3068 0.4365 0.3069 0.0218  -0.0119 -0.1033 101  LEU A CD2 
599   N N   . MET A 104  ? 0.2571 0.3437 0.2403 0.0106  -0.0033 -0.0619 102  MET A N   
600   C CA  . MET A 104  ? 0.3002 0.3819 0.2806 0.0078  -0.0023 -0.0548 102  MET A CA  
601   C C   . MET A 104  ? 0.2945 0.3762 0.2685 0.0045  0.0011  -0.0439 102  MET A C   
602   O O   . MET A 104  ? 0.2983 0.3848 0.2691 0.0020  0.0023  -0.0388 102  MET A O   
603   C CB  . MET A 104  ? 0.2543 0.3176 0.2388 0.0085  -0.0042 -0.0538 102  MET A CB  
604   C CG  . MET A 104  ? 0.2752 0.3380 0.2676 0.0115  -0.0082 -0.0641 102  MET A CG  
605   S SD  . MET A 104  ? 0.4003 0.4823 0.3935 0.0119  -0.0094 -0.0719 102  MET A SD  
606   C CE  . MET A 104  ? 0.3704 0.4477 0.3599 0.0083  -0.0079 -0.0626 102  MET A CE  
607   N N   . CYS A 105  ? 0.2702 0.3468 0.2426 0.0043  0.0024  -0.0405 103  CYS A N   
608   C CA  . CYS A 105  ? 0.2889 0.3660 0.2563 0.0011  0.0052  -0.0308 103  CYS A CA  
609   C C   . CYS A 105  ? 0.3278 0.4245 0.2924 -0.0006 0.0066  -0.0301 103  CYS A C   
610   O O   . CYS A 105  ? 0.3361 0.4363 0.2974 -0.0037 0.0082  -0.0223 103  CYS A O   
611   C CB  . CYS A 105  ? 0.2696 0.3376 0.2366 0.0014  0.0060  -0.0282 103  CYS A CB  
612   S SG  . CYS A 105  ? 0.3176 0.3635 0.2863 0.0025  0.0050  -0.0258 103  CYS A SG  
613   N N   . LEU A 106  ? 0.2713 0.3814 0.2374 0.0012  0.0060  -0.0378 104  LEU A N   
614   C CA  . LEU A 106  ? 0.2976 0.4289 0.2611 -0.0004 0.0073  -0.0376 104  LEU A CA  
615   C C   . LEU A 106  ? 0.3046 0.4436 0.2669 -0.0014 0.0068  -0.0372 104  LEU A C   
616   O O   . LEU A 106  ? 0.3265 0.4756 0.2852 -0.0046 0.0084  -0.0301 104  LEU A O   
617   C CB  . LEU A 106  ? 0.3086 0.4536 0.2745 0.0025  0.0064  -0.0477 104  LEU A CB  
618   C CG  . LEU A 106  ? 0.3076 0.4775 0.2711 0.0012  0.0076  -0.0489 104  LEU A CG  
619   C CD1 . LEU A 106  ? 0.3423 0.5184 0.3019 -0.0028 0.0103  -0.0383 104  LEU A CD1 
620   C CD2 . LEU A 106  ? 0.2953 0.4787 0.2621 0.0049  0.0064  -0.0610 104  LEU A CD2 
621   N N   . ALA A 107  ? 0.2662 0.4009 0.2320 0.0010  0.0044  -0.0445 105  ALA A N   
622   C CA  . ALA A 107  ? 0.3109 0.4526 0.2761 0.0002  0.0037  -0.0448 105  ALA A CA  
623   C C   . ALA A 107  ? 0.3657 0.4993 0.3277 -0.0032 0.0052  -0.0333 105  ALA A C   
624   O O   . ALA A 107  ? 0.3394 0.4847 0.2984 -0.0055 0.0059  -0.0289 105  ALA A O   
625   C CB  . ALA A 107  ? 0.2905 0.4248 0.2611 0.0032  0.0006  -0.0540 105  ALA A CB  
626   N N   . GLU A 108  ? 0.3224 0.4363 0.2852 -0.0034 0.0054  -0.0285 106  GLU A N   
627   C CA  . GLU A 108  ? 0.3344 0.4400 0.2947 -0.0062 0.0068  -0.0181 106  GLU A CA  
628   C C   . GLU A 108  ? 0.4049 0.5216 0.3615 -0.0093 0.0088  -0.0101 106  GLU A C   
629   O O   . GLU A 108  ? 0.3984 0.5195 0.3532 -0.0117 0.0092  -0.0037 106  GLU A O   
630   C CB  . GLU A 108  ? 0.3510 0.4363 0.3125 -0.0057 0.0070  -0.0149 106  GLU A CB  
631   C CG  . GLU A 108  ? 0.3489 0.4245 0.3086 -0.0081 0.0083  -0.0051 106  GLU A CG  
632   C CD  . GLU A 108  ? 0.4504 0.5104 0.4100 -0.0079 0.0092  -0.0012 106  GLU A CD  
633   O OE1 . GLU A 108  ? 0.4232 0.4758 0.3848 -0.0057 0.0084  -0.0062 106  GLU A OE1 
634   O OE2 . GLU A 108  ? 0.4652 0.5208 0.4232 -0.0099 0.0105  0.0067  106  GLU A OE2 
635   N N   . ALA A 109  ? 0.3414 0.4631 0.2973 -0.0095 0.0097  -0.0102 107  ALA A N   
636   C CA  . ALA A 109  ? 0.3731 0.5041 0.3264 -0.0128 0.0114  -0.0018 107  ALA A CA  
637   C C   . ALA A 109  ? 0.4122 0.5653 0.3637 -0.0143 0.0115  -0.0019 107  ALA A C   
638   O O   . ALA A 109  ? 0.4518 0.6109 0.4014 -0.0175 0.0122  0.0071  107  ALA A O   
639   C CB  . ALA A 109  ? 0.3957 0.5269 0.3494 -0.0126 0.0123  -0.0023 107  ALA A CB  
640   N N   . LEU A 110  ? 0.3598 0.5257 0.3120 -0.0118 0.0107  -0.0119 108  LEU A N   
641   C CA  . LEU A 110  ? 0.4015 0.5893 0.3516 -0.0127 0.0106  -0.0134 108  LEU A CA  
642   C C   . LEU A 110  ? 0.4254 0.6117 0.3747 -0.0139 0.0097  -0.0094 108  LEU A C   
643   O O   . LEU A 110  ? 0.4418 0.6434 0.3886 -0.0164 0.0101  -0.0041 108  LEU A O   
644   C CB  . LEU A 110  ? 0.3726 0.5720 0.3246 -0.0090 0.0092  -0.0269 108  LEU A CB  
645   C CG  . LEU A 110  ? 0.3721 0.5791 0.3247 -0.0079 0.0102  -0.0309 108  LEU A CG  
646   C CD1 . LEU A 110  ? 0.3536 0.5677 0.3096 -0.0034 0.0083  -0.0453 108  LEU A CD1 
647   C CD2 . LEU A 110  ? 0.4141 0.6419 0.3633 -0.0113 0.0121  -0.0242 108  LEU A CD2 
648   N N   . LEU A 111  ? 0.4631 0.6318 0.4148 -0.0123 0.0085  -0.0115 109  LEU A N   
649   C CA  . LEU A 111  ? 0.4704 0.6375 0.4217 -0.0134 0.0076  -0.0081 109  LEU A CA  
650   C C   . LEU A 111  ? 0.5095 0.6711 0.4592 -0.0168 0.0088  0.0049  109  LEU A C   
651   O O   . LEU A 111  ? 0.5474 0.7117 0.4964 -0.0182 0.0082  0.0093  109  LEU A O   
652   C CB  . LEU A 111  ? 0.4313 0.5819 0.3862 -0.0108 0.0060  -0.0139 109  LEU A CB  
653   C CG  . LEU A 111  ? 0.3792 0.5378 0.3370 -0.0076 0.0038  -0.0269 109  LEU A CG  
654   C CD1 . LEU A 111  ? 0.3900 0.5322 0.3523 -0.0055 0.0019  -0.0318 109  LEU A CD1 
655   C CD2 . LEU A 111  ? 0.4124 0.5923 0.3682 -0.0082 0.0031  -0.0294 109  LEU A CD2 
656   N N   . ARG A 112  ? 0.4967 0.6506 0.4463 -0.0182 0.0102  0.0110  110  ARG A N   
657   C CA  . ARG A 112  ? 0.5200 0.6704 0.4689 -0.0215 0.0109  0.0230  110  ARG A CA  
658   C C   . ARG A 112  ? 0.5493 0.7203 0.4962 -0.0246 0.0113  0.0291  110  ARG A C   
659   O O   . ARG A 112  ? 0.5624 0.7326 0.5095 -0.0276 0.0114  0.0396  110  ARG A O   
660   C CB  . ARG A 112  ? 0.5493 0.6851 0.4995 -0.0219 0.0119  0.0269  110  ARG A CB  
661   C CG  . ARG A 112  ? 0.5093 0.6248 0.4612 -0.0192 0.0116  0.0228  110  ARG A CG  
662   C CD  . ARG A 112  ? 0.5821 0.6879 0.5347 -0.0187 0.0124  0.0228  110  ARG A CD  
663   N NE  . ARG A 112  ? 0.6132 0.7154 0.5662 -0.0215 0.0131  0.0325  110  ARG A NE  
664   C CZ  . ARG A 112  ? 0.6854 0.7722 0.6397 -0.0217 0.0130  0.0374  110  ARG A CZ  
665   N NH1 . ARG A 112  ? 0.7017 0.7761 0.6567 -0.0196 0.0127  0.0342  110  ARG A NH1 
666   N NH2 . ARG A 112  ? 0.6997 0.7842 0.6554 -0.0242 0.0132  0.0455  110  ARG A NH2 
667   N N   . ILE A 113  ? 0.5626 0.7524 0.5078 -0.0239 0.0114  0.0228  111  ILE A N   
668   C CA  . ILE A 113  ? 0.5794 0.7919 0.5223 -0.0268 0.0117  0.0281  111  ILE A CA  
669   C C   . ILE A 113  ? 0.5746 0.7955 0.5162 -0.0268 0.0104  0.0276  111  ILE A C   
670   O O   . ILE A 113  ? 0.5654 0.7898 0.5071 -0.0238 0.0094  0.0171  111  ILE A O   
671   C CB  . ILE A 113  ? 0.5422 0.7730 0.4838 -0.0259 0.0126  0.0212  111  ILE A CB  
672   C CG1 . ILE A 113  ? 0.5139 0.7363 0.4569 -0.0263 0.0139  0.0228  111  ILE A CG1 
673   C CG2 . ILE A 113  ? 0.5654 0.8220 0.5042 -0.0289 0.0130  0.0265  111  ILE A CG2 
674   C CD1 . ILE A 113  ? 0.4943 0.7338 0.4367 -0.0252 0.0148  0.0159  111  ILE A CD1 
675   N N   . PRO A 114  ? 0.6216 0.8460 0.5628 -0.0300 0.0100  0.0386  112  PRO A N   
676   C CA  . PRO A 114  ? 0.6396 0.8675 0.5802 -0.0298 0.0085  0.0386  112  PRO A CA  
677   C C   . PRO A 114  ? 0.6152 0.8675 0.5529 -0.0292 0.0079  0.0322  112  PRO A C   
678   O O   . PRO A 114  ? 0.6082 0.8613 0.5461 -0.0270 0.0064  0.0252  112  PRO A O   
679   C CB  . PRO A 114  ? 0.5829 0.8086 0.5243 -0.0335 0.0081  0.0530  112  PRO A CB  
680   C CG  . PRO A 114  ? 0.6324 0.8456 0.5760 -0.0349 0.0093  0.0590  112  PRO A CG  
681   C CD  . PRO A 114  ? 0.6150 0.8365 0.5572 -0.0338 0.0106  0.0517  112  PRO A CD  
682   N N   . ASP A 115  ? 0.6236 0.8966 0.5589 -0.0310 0.0089  0.0343  113  ASP A N   
683   C CA  . ASP A 115  ? 0.6254 0.9247 0.5576 -0.0307 0.0084  0.0294  113  ASP A CA  
684   C C   . ASP A 115  ? 0.6214 0.9277 0.5536 -0.0268 0.0085  0.0142  113  ASP A C   
685   O O   . ASP A 115  ? 0.6174 0.9234 0.5502 -0.0263 0.0099  0.0118  113  ASP A O   
686   C CB  . ASP A 115  ? 0.6160 0.9364 0.5456 -0.0350 0.0093  0.0404  113  ASP A CB  
687   C CG  . ASP A 115  ? 0.6480 0.9985 0.5738 -0.0346 0.0092  0.0343  113  ASP A CG  
688   O OD1 . ASP A 115  ? 0.6319 0.9911 0.5563 -0.0337 0.0076  0.0313  113  ASP A OD1 
689   O OD2 . ASP A 115  ? 0.6399 1.0062 0.5645 -0.0349 0.0107  0.0322  113  ASP A OD2 
690   N N   . THR A 116  ? 0.5762 0.8897 0.5083 -0.0240 0.0068  0.0037  114  THR A N   
691   C CA  . THR A 116  ? 0.5972 0.9153 0.5308 -0.0197 0.0062  -0.0120 114  THR A CA  
692   C C   . THR A 116  ? 0.6156 0.9579 0.5468 -0.0198 0.0077  -0.0150 114  THR A C   
693   O O   . THR A 116  ? 0.5976 0.9372 0.5308 -0.0175 0.0083  -0.0225 114  THR A O   
694   C CB  . THR A 116  ? 0.5762 0.8999 0.5108 -0.0170 0.0036  -0.0221 114  THR A CB  
695   O OG1 . THR A 116  ? 0.6173 0.9176 0.5549 -0.0167 0.0024  -0.0201 114  THR A OG1 
696   C CG2 . THR A 116  ? 0.5900 0.9197 0.5272 -0.0124 0.0025  -0.0388 114  THR A CG2 
697   N N   . ALA A 117  ? 0.5801 0.9471 0.5072 -0.0226 0.0081  -0.0091 115  ALA A N   
698   C CA  . ALA A 117  ? 0.5611 0.9533 0.4865 -0.0229 0.0096  -0.0117 115  ALA A CA  
699   C C   . ALA A 117  ? 0.5651 0.9511 0.4910 -0.0249 0.0119  -0.0048 115  ALA A C   
700   O O   . ALA A 117  ? 0.5892 0.9833 0.5173 -0.0230 0.0127  -0.0121 115  ALA A O   
701   C CB  . ALA A 117  ? 0.5537 0.9665 0.4811 -0.0258 0.0089  -0.0040 115  ALA A CB  
702   N N   . THR A 118  ? 0.5420 0.9116 0.4684 -0.0286 0.0125  0.0091  116  THR A N   
703   C CA  . THR A 118  ? 0.5897 0.9506 0.5177 -0.0305 0.0143  0.0154  116  THR A CA  
704   C C   . THR A 118  ? 0.5722 0.9149 0.5035 -0.0262 0.0142  0.0043  116  THR A C   
705   O O   . THR A 118  ? 0.5358 0.8832 0.4680 -0.0257 0.0156  0.0013  116  THR A O   
706   C CB  . THR A 118  ? 0.5629 0.9063 0.4922 -0.0345 0.0142  0.0308  116  THR A CB  
707   O OG1 . THR A 118  ? 0.6747 1.0329 0.6024 -0.0381 0.0136  0.0413  116  THR A OG1 
708   C CG2 . THR A 118  ? 0.5291 0.8668 0.4603 -0.0369 0.0158  0.0377  116  THR A CG2 
709   N N   . ARG A 119  ? 0.5353 0.8574 0.4688 -0.0233 0.0126  -0.0015 117  ARG A N   
710   C CA  . ARG A 119  ? 0.5601 0.8640 0.4972 -0.0194 0.0121  -0.0114 117  ARG A CA  
711   C C   . ARG A 119  ? 0.5579 0.8782 0.4958 -0.0156 0.0118  -0.0257 117  ARG A C   
712   O O   . ARG A 119  ? 0.5320 0.8501 0.4718 -0.0141 0.0127  -0.0298 117  ARG A O   
713   C CB  . ARG A 119  ? 0.4749 0.7573 0.4144 -0.0174 0.0102  -0.0145 117  ARG A CB  
714   C CG  . ARG A 119  ? 0.4803 0.7401 0.4237 -0.0142 0.0096  -0.0211 117  ARG A CG  
715   C CD  . ARG A 119  ? 0.4828 0.7267 0.4289 -0.0119 0.0074  -0.0262 117  ARG A CD  
716   N NE  . ARG A 119  ? 0.5229 0.7582 0.4678 -0.0147 0.0074  -0.0157 117  ARG A NE  
717   C CZ  . ARG A 119  ? 0.5092 0.7482 0.4539 -0.0147 0.0059  -0.0168 117  ARG A CZ  
718   N NH1 . ARG A 119  ? 0.4827 0.7338 0.4284 -0.0120 0.0041  -0.0281 117  ARG A NH1 
719   N NH2 . ARG A 119  ? 0.5947 0.8250 0.5387 -0.0172 0.0060  -0.0067 117  ARG A NH2 
720   N N   . ASP A 120  ? 0.5525 0.8902 0.4894 -0.0139 0.0105  -0.0336 118  ASP A N   
721   C CA  . ASP A 120  ? 0.5732 0.9281 0.5114 -0.0098 0.0099  -0.0484 118  ASP A CA  
722   C C   . ASP A 120  ? 0.5488 0.9241 0.4850 -0.0112 0.0123  -0.0464 118  ASP A C   
723   O O   . ASP A 120  ? 0.5346 0.9157 0.4733 -0.0078 0.0122  -0.0572 118  ASP A O   
724   C CB  . ASP A 120  ? 0.5374 0.9101 0.4743 -0.0083 0.0080  -0.0560 118  ASP A CB  
725   C CG  . ASP A 120  ? 0.6063 0.9592 0.5460 -0.0067 0.0054  -0.0590 118  ASP A CG  
726   O OD1 . ASP A 120  ? 0.5800 0.9063 0.5225 -0.0068 0.0052  -0.0551 118  ASP A OD1 
727   O OD2 . ASP A 120  ? 0.6396 1.0044 0.5790 -0.0054 0.0035  -0.0655 118  ASP A OD2 
728   N N   . ALA A 121  ? 0.5491 0.9353 0.4814 -0.0164 0.0142  -0.0323 119  ALA A N   
729   C CA  . ALA A 121  ? 0.5828 0.9844 0.5171 -0.0184 0.0159  -0.0281 119  ALA A CA  
730   C C   . ALA A 121  ? 0.5698 0.9567 0.5039 -0.0183 0.0176  -0.0269 119  ALA A C   
731   O O   . ALA A 121  ? 0.5417 0.9376 0.4786 -0.0166 0.0182  -0.0330 119  ALA A O   
732   C CB  . ALA A 121  ? 0.5785 0.9901 0.5127 -0.0240 0.0162  -0.0122 119  ALA A CB  
733   N N   . LEU A 122  ? 0.5492 0.9089 0.4848 -0.0199 0.0173  -0.0186 120  LEU A N   
734   C CA  . LEU A 122  ? 0.5356 0.8770 0.4742 -0.0196 0.0179  -0.0174 120  LEU A CA  
735   C C   . LEU A 122  ? 0.5625 0.8977 0.5046 -0.0138 0.0168  -0.0329 120  LEU A C   
736   O O   . LEU A 122  ? 0.5412 0.8785 0.4852 -0.0127 0.0177  -0.0363 120  LEU A O   
737   C CB  . LEU A 122  ? 0.5183 0.8320 0.4579 -0.0216 0.0174  -0.0076 120  LEU A CB  
738   C CG  . LEU A 122  ? 0.5374 0.8349 0.4795 -0.0224 0.0183  -0.0032 120  LEU A CG  
739   C CD1 . LEU A 122  ? 0.5583 0.8738 0.4996 -0.0264 0.0203  0.0046  120  LEU A CD1 
740   C CD2 . LEU A 122  ? 0.5511 0.8231 0.4941 -0.0242 0.0178  0.0058  120  LEU A CD2 
741   N N   . ILE A 123  ? 0.5655 0.8936 0.5092 -0.0102 0.0145  -0.0425 121  ILE A N   
742   C CA  . ILE A 123  ? 0.5117 0.8339 0.4599 -0.0046 0.0127  -0.0574 121  ILE A CA  
743   C C   . ILE A 123  ? 0.5389 0.8877 0.4875 -0.0023 0.0133  -0.0673 121  ILE A C   
744   O O   . ILE A 123  ? 0.5011 0.8486 0.4527 -0.0001 0.0135  -0.0729 121  ILE A O   
745   C CB  . ILE A 123  ? 0.4881 0.8008 0.4385 -0.0017 0.0098  -0.0652 121  ILE A CB  
746   C CG1 . ILE A 123  ? 0.4488 0.7337 0.3996 -0.0034 0.0093  -0.0566 121  ILE A CG1 
747   C CG2 . ILE A 123  ? 0.4513 0.7631 0.4073 0.0041  0.0074  -0.0816 121  ILE A CG2 
748   C CD1 . ILE A 123  ? 0.4646 0.7438 0.4164 -0.0023 0.0070  -0.0601 121  ILE A CD1 
749   N N   . ARG A 124  ? 0.5353 0.9093 0.4809 -0.0028 0.0134  -0.0697 122  ARG A N   
750   C CA  . ARG A 124  ? 0.5501 0.9490 0.4982 0.0001  0.0133  -0.0805 122  ARG A CA  
751   C C   . ARG A 124  ? 0.5788 0.9886 0.5279 -0.0025 0.0156  -0.0738 122  ARG A C   
752   O O   . ARG A 124  ? 0.6544 1.0711 0.6084 0.0008  0.0152  -0.0830 122  ARG A O   
753   C CB  . ARG A 124  ? 0.5125 0.9312 0.4621 -0.0004 0.0120  -0.0814 122  ARG A CB  
754   N N   . ASP A 125  ? 0.6092 1.0202 0.5546 -0.0083 0.0176  -0.0579 123  ASP A N   
755   C CA  . ASP A 125  ? 0.6144 1.0386 0.5615 -0.0115 0.0193  -0.0506 123  ASP A CA  
756   C C   . ASP A 125  ? 0.6176 1.0262 0.5637 -0.0124 0.0212  -0.0465 123  ASP A C   
757   O O   . ASP A 125  ? 0.6916 1.1092 0.6408 -0.0121 0.0219  -0.0483 123  ASP A O   
758   C CB  . ASP A 125  ? 0.6572 1.0922 0.6027 -0.0175 0.0197  -0.0352 123  ASP A CB  
759   C CG  . ASP A 125  ? 0.6508 1.1042 0.5976 -0.0169 0.0180  -0.0384 123  ASP A CG  
760   O OD1 . ASP A 125  ? 0.6475 1.1140 0.5981 -0.0125 0.0166  -0.0519 123  ASP A OD1 
761   O OD2 . ASP A 125  ? 0.6721 1.1271 0.6168 -0.0208 0.0177  -0.0274 123  ASP A OD2 
762   N N   . LYS A 126  ? 0.5642 0.9477 0.5081 -0.0134 0.0213  -0.0409 124  LYS A N   
763   C CA  . LYS A 126  ? 0.5946 0.9597 0.5407 -0.0153 0.0221  -0.0335 124  LYS A CA  
764   C C   . LYS A 126  ? 0.6193 0.9565 0.5691 -0.0111 0.0202  -0.0407 124  LYS A C   
765   O O   . LYS A 126  ? 0.6372 0.9665 0.5897 -0.0103 0.0206  -0.0416 124  LYS A O   
766   C CB  . LYS A 126  ? 0.6004 0.9569 0.5444 -0.0212 0.0229  -0.0164 124  LYS A CB  
767   N N   . ILE A 127  ? 0.5787 0.9010 0.5291 -0.0086 0.0181  -0.0452 125  ILE A N   
768   C CA  . ILE A 127  ? 0.5651 0.8614 0.5193 -0.0051 0.0162  -0.0508 125  ILE A CA  
769   C C   . ILE A 127  ? 0.5695 0.8718 0.5280 0.0005  0.0148  -0.0661 125  ILE A C   
770   O O   . ILE A 127  ? 0.6056 0.8985 0.5672 0.0023  0.0146  -0.0688 125  ILE A O   
771   C CB  . ILE A 127  ? 0.5552 0.8339 0.5092 -0.0045 0.0144  -0.0501 125  ILE A CB  
772   C CG1 . ILE A 127  ? 0.5792 0.8513 0.5297 -0.0097 0.0156  -0.0352 125  ILE A CG1 
773   C CG2 . ILE A 127  ? 0.5141 0.7671 0.4722 -0.0012 0.0125  -0.0551 125  ILE A CG2 
774   C CD1 . ILE A 127  ? 0.5430 0.8027 0.4937 -0.0127 0.0169  -0.0251 125  ILE A CD1 
775   N N   . ALA A 128  ? 0.5224 0.8407 0.4814 0.0034  0.0135  -0.0766 126  ALA A N   
776   C CA  . ALA A 128  ? 0.4775 0.8010 0.4418 0.0092  0.0115  -0.0923 126  ALA A CA  
777   C C   . ALA A 128  ? 0.6059 0.9446 0.5715 0.0098  0.0131  -0.0950 126  ALA A C   
778   O O   . ALA A 128  ? 0.5318 0.8683 0.5027 0.0146  0.0114  -0.1063 126  ALA A O   
779   C CB  . ALA A 128  ? 0.4341 0.7760 0.3989 0.0119  0.0099  -0.1031 126  ALA A CB  
780   N N   . ASP A 129  ? 0.6527 1.0067 0.6140 0.0051  0.0163  -0.0846 127  ASP A N   
781   C CA  . ASP A 129  ? 0.6512 1.0214 0.6136 0.0051  0.0181  -0.0861 127  ASP A CA  
782   C C   . ASP A 129  ? 0.6540 1.0035 0.6183 0.0037  0.0186  -0.0792 127  ASP A C   
783   O O   . ASP A 129  ? 0.7496 1.1090 0.7135 0.0011  0.0207  -0.0737 127  ASP A O   
784   C CB  . ASP A 129  ? 0.6158 1.0137 0.5734 0.0002  0.0211  -0.0776 127  ASP A CB  
785   N N   . GLY A 130  ? 0.6905 1.0119 0.6569 0.0054  0.0165  -0.0794 128  GLY A N   
786   C CA  . GLY A 130  ? 0.6661 0.9667 0.6337 0.0042  0.0166  -0.0730 128  GLY A CA  
787   C C   . GLY A 130  ? 0.7156 1.0110 0.6792 -0.0021 0.0187  -0.0569 128  GLY A C   
788   O O   . GLY A 130  ? 0.7291 1.0346 0.6889 -0.0056 0.0198  -0.0500 128  GLY A O   
789   N N   . ASN A 131  ? 0.6629 0.9422 0.6278 -0.0034 0.0190  -0.0512 129  ASN A N   
790   C CA  . ASN A 131  ? 0.6942 0.9659 0.6568 -0.0090 0.0204  -0.0367 129  ASN A CA  
791   C C   . ASN A 131  ? 0.6438 0.9039 0.6034 -0.0109 0.0199  -0.0302 129  ASN A C   
792   O O   . ASN A 131  ? 0.6767 0.9445 0.6338 -0.0154 0.0211  -0.0201 129  ASN A O   
793   C CB  . ASN A 131  ? 0.6716 0.9671 0.6330 -0.0133 0.0228  -0.0298 129  ASN A CB  
794   N N   . TRP A 132  ? 0.6339 0.8759 0.5946 -0.0073 0.0179  -0.0359 130  TRP A N   
795   C CA  . TRP A 132  ? 0.5803 0.8088 0.5389 -0.0089 0.0173  -0.0300 130  TRP A CA  
796   C C   . TRP A 132  ? 0.5738 0.7871 0.5316 -0.0128 0.0180  -0.0176 130  TRP A C   
797   O O   . TRP A 132  ? 0.5837 0.7920 0.5394 -0.0156 0.0182  -0.0096 130  TRP A O   
798   C CB  . TRP A 132  ? 0.5656 0.7772 0.5263 -0.0044 0.0149  -0.0384 130  TRP A CB  
799   C CG  . TRP A 132  ? 0.4678 0.6612 0.4315 -0.0019 0.0138  -0.0413 130  TRP A CG  
800   C CD1 . TRP A 132  ? 0.4162 0.6117 0.3836 0.0021  0.0126  -0.0512 130  TRP A CD1 
801   C CD2 . TRP A 132  ? 0.4340 0.6050 0.3974 -0.0031 0.0137  -0.0343 130  TRP A CD2 
802   N NE1 . TRP A 132  ? 0.4119 0.5877 0.3812 0.0033  0.0117  -0.0502 130  TRP A NE1 
803   C CE2 . TRP A 132  ? 0.4066 0.5677 0.3732 0.0001  0.0124  -0.0400 130  TRP A CE2 
804   C CE3 . TRP A 132  ? 0.4453 0.6044 0.4063 -0.0065 0.0144  -0.0240 130  TRP A CE3 
805   C CZ2 . TRP A 132  ? 0.3441 0.4847 0.3110 0.0000  0.0120  -0.0356 130  TRP A CZ2 
806   C CZ3 . TRP A 132  ? 0.4507 0.5896 0.4123 -0.0064 0.0140  -0.0203 130  TRP A CZ3 
807   C CH2 . TRP A 132  ? 0.4210 0.5511 0.3852 -0.0032 0.0128  -0.0261 130  TRP A CH2 
808   N N   . LYS A 133  ? 0.5981 0.8037 0.5577 -0.0129 0.0183  -0.0164 131  LYS A N   
809   C CA  . LYS A 133  ? 0.6276 0.8184 0.5872 -0.0163 0.0187  -0.0059 131  LYS A CA  
810   C C   . LYS A 133  ? 0.6864 0.8899 0.6448 -0.0217 0.0200  0.0052  131  LYS A C   
811   O O   . LYS A 133  ? 0.7540 0.9472 0.7120 -0.0246 0.0198  0.0142  131  LYS A O   
812   C CB  . LYS A 133  ? 0.5882 0.7708 0.5502 -0.0152 0.0185  -0.0077 131  LYS A CB  
813   N N   . SER A 134  ? 0.6973 0.9241 0.6557 -0.0232 0.0212  0.0047  132  SER A N   
814   C CA  . SER A 134  ? 0.6841 0.9248 0.6422 -0.0288 0.0224  0.0161  132  SER A CA  
815   C C   . SER A 134  ? 0.7016 0.9430 0.6573 -0.0308 0.0221  0.0223  132  SER A C   
816   O O   . SER A 134  ? 0.7474 0.9879 0.7037 -0.0354 0.0221  0.0340  132  SER A O   
817   C CB  . SER A 134  ? 0.6773 0.9455 0.6354 -0.0295 0.0239  0.0133  132  SER A CB  
818   N N   . HIS A 135  ? 0.6927 0.9350 0.6463 -0.0274 0.0214  0.0146  133  HIS A N   
819   C CA  . HIS A 135  ? 0.6832 0.9295 0.6344 -0.0292 0.0210  0.0196  133  HIS A CA  
820   C C   . HIS A 135  ? 0.6928 0.9151 0.6441 -0.0282 0.0197  0.0215  133  HIS A C   
821   O O   . HIS A 135  ? 0.6838 0.9062 0.6341 -0.0305 0.0193  0.0286  133  HIS A O   
822   C CB  . HIS A 135  ? 0.6553 0.9207 0.6044 -0.0265 0.0210  0.0102  133  HIS A CB  
823   C CG  . HIS A 135  ? 0.6690 0.9592 0.6181 -0.0266 0.0224  0.0063  133  HIS A CG  
824   N ND1 . HIS A 135  ? 0.6415 0.9331 0.5926 -0.0228 0.0224  -0.0044 133  HIS A ND1 
825   C CD2 . HIS A 135  ? 0.6432 0.9585 0.5907 -0.0302 0.0237  0.0119  133  HIS A CD2 
826   C CE1 . HIS A 135  ? 0.6802 0.9968 0.6310 -0.0238 0.0239  -0.0058 133  HIS A CE1 
827   N NE2 . HIS A 135  ? 0.7100 1.0419 0.6585 -0.0284 0.0248  0.0042  133  HIS A NE2 
828   N N   . LEU A 136  ? 0.6996 0.9026 0.6524 -0.0248 0.0190  0.0156  134  LEU A N   
829   C CA  . LEU A 136  ? 0.6561 0.8374 0.6089 -0.0237 0.0179  0.0171  134  LEU A CA  
830   C C   . LEU A 136  ? 0.7273 0.8885 0.6822 -0.0230 0.0176  0.0181  134  LEU A C   
831   O O   . LEU A 136  ? 0.7457 0.8914 0.7011 -0.0242 0.0172  0.0243  134  LEU A O   
832   C CB  . LEU A 136  ? 0.6337 0.8124 0.5859 -0.0196 0.0168  0.0072  134  LEU A CB  
833   C CG  . LEU A 136  ? 0.6314 0.8270 0.5816 -0.0199 0.0166  0.0056  134  LEU A CG  
834   C CD1 . LEU A 136  ? 0.5164 0.7108 0.4674 -0.0154 0.0151  -0.0066 134  LEU A CD1 
835   C CD2 . LEU A 136  ? 0.5914 0.7822 0.5405 -0.0229 0.0163  0.0154  134  LEU A CD2 
836   N N   . SER A 139  ? 0.5856 0.6875 0.5502 -0.0334 0.0153  0.0551  137  SER A N   
837   C CA  . SER A 139  ? 0.5840 0.6675 0.5510 -0.0332 0.0143  0.0584  137  SER A CA  
838   C C   . SER A 139  ? 0.6010 0.6708 0.5654 -0.0290 0.0144  0.0517  137  SER A C   
839   O O   . SER A 139  ? 0.5873 0.6421 0.5529 -0.0280 0.0137  0.0528  137  SER A O   
840   C CB  . SER A 139  ? 0.5485 0.6327 0.5183 -0.0365 0.0132  0.0682  137  SER A CB  
841   N N   . ARG A 140  ? 0.5456 0.6213 0.5069 -0.0265 0.0150  0.0447  138  ARG A N   
842   C CA  . ARG A 140  ? 0.5179 0.5819 0.4775 -0.0229 0.0149  0.0386  138  ARG A CA  
843   C C   . ARG A 140  ? 0.5091 0.5782 0.4671 -0.0200 0.0151  0.0296  138  ARG A C   
844   O O   . ARG A 140  ? 0.4691 0.5535 0.4263 -0.0204 0.0154  0.0271  138  ARG A O   
845   C CB  . ARG A 140  ? 0.5042 0.5679 0.4629 -0.0229 0.0147  0.0406  138  ARG A CB  
846   C CG  . ARG A 140  ? 0.5464 0.5976 0.5040 -0.0197 0.0145  0.0356  138  ARG A CG  
847   C CD  . ARG A 140  ? 0.5573 0.6138 0.5140 -0.0193 0.0143  0.0345  138  ARG A CD  
848   N NE  . ARG A 140  ? 0.6217 0.6656 0.5788 -0.0185 0.0140  0.0365  138  ARG A NE  
849   C CZ  . ARG A 140  ? 0.6462 0.6886 0.6027 -0.0171 0.0137  0.0335  138  ARG A CZ  
850   N NH1 . ARG A 140  ? 0.6943 0.7462 0.6501 -0.0161 0.0134  0.0277  138  ARG A NH1 
851   N NH2 . ARG A 140  ? 0.6293 0.6610 0.5867 -0.0165 0.0137  0.0359  138  ARG A NH2 
852   N N   . SER A 141  ? 0.4367 0.4938 0.3946 -0.0171 0.0148  0.0246  139  SER A N   
853   C CA  . SER A 141  ? 0.3940 0.4541 0.3515 -0.0141 0.0144  0.0160  139  SER A CA  
854   C C   . SER A 141  ? 0.3936 0.4597 0.3505 -0.0128 0.0141  0.0119  139  SER A C   
855   O O   . SER A 141  ? 0.3842 0.4449 0.3405 -0.0131 0.0139  0.0144  139  SER A O   
856   C CB  . SER A 141  ? 0.3848 0.4295 0.3426 -0.0114 0.0138  0.0128  139  SER A CB  
857   O OG  . SER A 141  ? 0.3833 0.4293 0.3417 -0.0083 0.0130  0.0048  139  SER A OG  
858   N N   . LEU A 142  ? 0.3843 0.4624 0.3415 -0.0113 0.0138  0.0052  140  LEU A N   
859   C CA  . LEU A 142  ? 0.3409 0.4233 0.2984 -0.0094 0.0129  -0.0008 140  LEU A CA  
860   C C   . LEU A 142  ? 0.3362 0.4025 0.2947 -0.0069 0.0117  -0.0038 140  LEU A C   
861   O O   . LEU A 142  ? 0.3403 0.4064 0.2993 -0.0061 0.0109  -0.0063 140  LEU A O   
862   C CB  . LEU A 142  ? 0.3796 0.4757 0.3383 -0.0074 0.0124  -0.0093 140  LEU A CB  
863   C CG  . LEU A 142  ? 0.4262 0.5420 0.3838 -0.0086 0.0128  -0.0104 140  LEU A CG  
864   C CD1 . LEU A 142  ? 0.4983 0.6241 0.4543 -0.0125 0.0144  -0.0021 140  LEU A CD1 
865   C CD2 . LEU A 142  ? 0.4284 0.5558 0.3880 -0.0054 0.0118  -0.0211 140  LEU A CD2 
866   N N   . PHE A 143  ? 0.3145 0.3680 0.2736 -0.0058 0.0115  -0.0035 141  PHE A N   
867   C CA  . PHE A 143  ? 0.3280 0.3686 0.2887 -0.0030 0.0102  -0.0073 141  PHE A CA  
868   C C   . PHE A 143  ? 0.3104 0.3367 0.2700 -0.0038 0.0107  -0.0014 141  PHE A C   
869   O O   . PHE A 143  ? 0.3306 0.3453 0.2910 -0.0020 0.0099  -0.0026 141  PHE A O   
870   C CB  . PHE A 143  ? 0.2959 0.3341 0.2582 -0.0008 0.0093  -0.0121 141  PHE A CB  
871   C CG  . PHE A 143  ? 0.3136 0.3672 0.2773 0.0001  0.0090  -0.0181 141  PHE A CG  
872   C CD1 . PHE A 143  ? 0.2394 0.3014 0.2052 0.0018  0.0077  -0.0249 141  PHE A CD1 
873   C CD2 . PHE A 143  ? 0.2838 0.3444 0.2471 -0.0007 0.0099  -0.0172 141  PHE A CD2 
874   C CE1 . PHE A 143  ? 0.2946 0.3720 0.2618 0.0029  0.0074  -0.0312 141  PHE A CE1 
875   C CE2 . PHE A 143  ? 0.3098 0.3859 0.2745 0.0001  0.0098  -0.0228 141  PHE A CE2 
876   C CZ  . PHE A 143  ? 0.2948 0.3797 0.2613 0.0021  0.0086  -0.0300 141  PHE A CZ  
877   N N   . VAL A 144  ? 0.3217 0.3492 0.2796 -0.0064 0.0118  0.0052  142  VAL A N   
878   C CA  A VAL A 144  ? 0.3532 0.3683 0.3104 -0.0069 0.0123  0.0104  142  VAL A CA  
879   C CA  B VAL A 144  ? 0.3533 0.3684 0.3105 -0.0069 0.0123  0.0104  142  VAL A CA  
880   C C   . VAL A 144  ? 0.3513 0.3587 0.3095 -0.0052 0.0115  0.0079  142  VAL A C   
881   O O   . VAL A 144  ? 0.3695 0.3655 0.3276 -0.0044 0.0116  0.0095  142  VAL A O   
882   C CB  A VAL A 144  ? 0.3686 0.3877 0.3251 -0.0097 0.0132  0.0172  142  VAL A CB  
883   C CB  B VAL A 144  ? 0.3686 0.3875 0.3250 -0.0097 0.0132  0.0172  142  VAL A CB  
884   C CG1 A VAL A 144  ? 0.3694 0.3768 0.3259 -0.0098 0.0136  0.0215  142  VAL A CG1 
885   C CG1 B VAL A 144  ? 0.3827 0.4064 0.3392 -0.0117 0.0138  0.0208  142  VAL A CG1 
886   C CG2 A VAL A 144  ? 0.3828 0.4070 0.3392 -0.0117 0.0138  0.0208  142  VAL A CG2 
887   C CG2 B VAL A 144  ? 0.3608 0.3911 0.3173 -0.0106 0.0130  0.0166  142  VAL A CG2 
888   N N   . ASN A 145  ? 0.3180 0.3322 0.2775 -0.0048 0.0106  0.0040  143  ASN A N   
889   C CA  . ASN A 145  ? 0.3405 0.3479 0.3019 -0.0036 0.0096  0.0021  143  ASN A CA  
890   C C   . ASN A 145  ? 0.3148 0.3200 0.2793 -0.0011 0.0076  -0.0049 143  ASN A C   
891   O O   . ASN A 145  ? 0.3290 0.3317 0.2964 -0.0003 0.0062  -0.0078 143  ASN A O   
892   C CB  . ASN A 145  ? 0.3608 0.3756 0.3224 -0.0048 0.0095  0.0026  143  ASN A CB  
893   C CG  . ASN A 145  ? 0.3931 0.4064 0.3529 -0.0069 0.0109  0.0101  143  ASN A CG  
894   O OD1 . ASN A 145  ? 0.4244 0.4271 0.3839 -0.0069 0.0116  0.0138  143  ASN A OD1 
895   N ND2 . ASN A 145  ? 0.3757 0.4001 0.3344 -0.0088 0.0113  0.0124  143  ASN A ND2 
896   N N   . ALA A 146  ? 0.3202 0.3261 0.2850 0.0002  0.0072  -0.0078 144  ALA A N   
897   C CA  . ALA A 146  ? 0.3009 0.3061 0.2696 0.0028  0.0049  -0.0149 144  ALA A CA  
898   C C   . ALA A 146  ? 0.3412 0.3332 0.3125 0.0039  0.0035  -0.0144 144  ALA A C   
899   O O   . ALA A 146  ? 0.3417 0.3321 0.3176 0.0057  0.0010  -0.0198 144  ALA A O   
900   C CB  . ALA A 146  ? 0.2949 0.3034 0.2634 0.0039  0.0049  -0.0174 144  ALA A CB  
901   N N   . ALA A 147  ? 0.3318 0.3145 0.3005 0.0030  0.0049  -0.0081 145  ALA A N   
902   C CA  . ALA A 147  ? 0.3829 0.3545 0.3537 0.0037  0.0038  -0.0066 145  ALA A CA  
903   C C   . ALA A 147  ? 0.3678 0.3396 0.3420 0.0033  0.0026  -0.0081 145  ALA A C   
904   O O   . ALA A 147  ? 0.3700 0.3365 0.3489 0.0045  0.0002  -0.0106 145  ALA A O   
905   C CB  . ALA A 147  ? 0.4159 0.3800 0.3829 0.0027  0.0058  0.0001  145  ALA A CB  
906   N N   . THR A 148  ? 0.3349 0.3129 0.3073 0.0017  0.0039  -0.0065 146  THR A N   
907   C CA  . THR A 148  ? 0.3673 0.3468 0.3430 0.0013  0.0027  -0.0081 146  THR A CA  
908   C C   . THR A 148  ? 0.3427 0.3284 0.3231 0.0029  -0.0001 -0.0163 146  THR A C   
909   O O   . THR A 148  ? 0.3495 0.3308 0.3353 0.0036  -0.0025 -0.0193 146  THR A O   
910   C CB  . THR A 148  ? 0.3798 0.3655 0.3523 -0.0008 0.0046  -0.0043 146  THR A CB  
911   O OG1 . THR A 148  ? 0.3497 0.3287 0.3190 -0.0018 0.0068  0.0026  146  THR A OG1 
912   C CG2 . THR A 148  ? 0.3765 0.3643 0.3522 -0.0013 0.0033  -0.0060 146  THR A CG2 
913   N N   . TRP A 149  ? 0.3427 0.3390 0.3219 0.0035  0.0001  -0.0204 147  TRP A N   
914   C CA  . TRP A 149  ? 0.3295 0.3328 0.3135 0.0055  -0.0026 -0.0294 147  TRP A CA  
915   C C   . TRP A 149  ? 0.2961 0.2908 0.2853 0.0079  -0.0053 -0.0331 147  TRP A C   
916   O O   . TRP A 149  ? 0.3379 0.3329 0.3337 0.0096  -0.0085 -0.0397 147  TRP A O   
917   C CB  . TRP A 149  ? 0.3169 0.3346 0.2981 0.0057  -0.0016 -0.0326 147  TRP A CB  
918   C CG  . TRP A 149  ? 0.3361 0.3638 0.3135 0.0035  0.0003  -0.0296 147  TRP A CG  
919   C CD1 . TRP A 149  ? 0.3328 0.3656 0.3049 0.0013  0.0030  -0.0234 147  TRP A CD1 
920   C CD2 . TRP A 149  ? 0.3438 0.3776 0.3230 0.0031  -0.0009 -0.0323 147  TRP A CD2 
921   N NE1 . TRP A 149  ? 0.3768 0.4185 0.3472 -0.0004 0.0036  -0.0216 147  TRP A NE1 
922   C CE2 . TRP A 149  ? 0.3414 0.3843 0.3157 0.0007  0.0014  -0.0271 147  TRP A CE2 
923   C CE3 . TRP A 149  ? 0.3293 0.3618 0.3143 0.0044  -0.0038 -0.0385 147  TRP A CE3 
924   C CZ2 . TRP A 149  ? 0.3482 0.3994 0.3226 -0.0002 0.0009  -0.0280 147  TRP A CZ2 
925   C CZ3 . TRP A 149  ? 0.3933 0.4338 0.3785 0.0035  -0.0043 -0.0398 147  TRP A CZ3 
926   C CH2 . TRP A 149  ? 0.3830 0.4331 0.3627 0.0012  -0.0019 -0.0346 147  TRP A CH2 
927   N N   . GLY A 150  ? 0.3228 0.3102 0.3098 0.0081  -0.0044 -0.0291 148  GLY A N   
928   C CA  . GLY A 150  ? 0.3146 0.2929 0.3065 0.0101  -0.0070 -0.0310 148  GLY A CA  
929   C C   . GLY A 150  ? 0.3560 0.3252 0.3533 0.0098  -0.0093 -0.0300 148  GLY A C   
930   O O   . GLY A 150  ? 0.4023 0.3682 0.4069 0.0116  -0.0130 -0.0350 148  GLY A O   
931   N N   . LEU A 151  ? 0.3850 0.3502 0.3793 0.0075  -0.0074 -0.0234 149  LEU A N   
932   C CA  . LEU A 151  ? 0.3768 0.3347 0.3765 0.0068  -0.0093 -0.0219 149  LEU A CA  
933   C C   . LEU A 151  ? 0.3667 0.3303 0.3726 0.0074  -0.0122 -0.0293 149  LEU A C   
934   O O   . LEU A 151  ? 0.4205 0.3786 0.4345 0.0082  -0.0159 -0.0321 149  LEU A O   
935   C CB  . LEU A 151  ? 0.4056 0.3606 0.4008 0.0043  -0.0064 -0.0141 149  LEU A CB  
936   C CG  . LEU A 151  ? 0.5025 0.4469 0.4978 0.0035  -0.0061 -0.0073 149  LEU A CG  
937   C CD1 . LEU A 151  ? 0.5030 0.4468 0.4952 0.0013  -0.0035 -0.0014 149  LEU A CD1 
938   C CD2 . LEU A 151  ? 0.4479 0.3857 0.4517 0.0041  -0.0100 -0.0089 149  LEU A CD2 
939   N N   . VAL A 152  ? 0.3539 0.3289 0.3568 0.0071  -0.0109 -0.0324 150  VAL A N   
940   C CA  . VAL A 152  ? 0.3341 0.3165 0.3424 0.0079  -0.0136 -0.0401 150  VAL A CA  
941   C C   . VAL A 152  ? 0.3740 0.3575 0.3894 0.0109  -0.0174 -0.0491 150  VAL A C   
942   O O   . VAL A 152  ? 0.3805 0.3621 0.4043 0.0119  -0.0213 -0.0548 150  VAL A O   
943   C CB  . VAL A 152  ? 0.3406 0.3368 0.3433 0.0070  -0.0112 -0.0413 150  VAL A CB  
944   C CG1 . VAL A 152  ? 0.3852 0.3915 0.3929 0.0083  -0.0141 -0.0508 150  VAL A CG1 
945   C CG2 . VAL A 152  ? 0.3626 0.3572 0.3604 0.0042  -0.0084 -0.0332 150  VAL A CG2 
946   N N   . VAL A 153  ? 0.3500 0.3369 0.3628 0.0125  -0.0166 -0.0510 151  VAL A N   
947   C CA  . VAL A 153  ? 0.3323 0.3224 0.3516 0.0158  -0.0200 -0.0603 151  VAL A CA  
948   C C   . VAL A 153  ? 0.3750 0.3515 0.4014 0.0171  -0.0234 -0.0595 151  VAL A C   
949   O O   . VAL A 153  ? 0.4036 0.3781 0.4396 0.0192  -0.0279 -0.0665 151  VAL A O   
950   C CB  . VAL A 153  ? 0.3403 0.3408 0.3542 0.0169  -0.0177 -0.0625 151  VAL A CB  
951   C CG1 . VAL A 153  ? 0.3761 0.3782 0.3968 0.0205  -0.0211 -0.0712 151  VAL A CG1 
952   C CG2 . VAL A 153  ? 0.3249 0.3411 0.3341 0.0159  -0.0155 -0.0648 151  VAL A CG2 
953   N N   . THR A 154  ? 0.3931 0.3605 0.4153 0.0159  -0.0215 -0.0509 152  THR A N   
954   C CA  . THR A 154  ? 0.4035 0.3595 0.4316 0.0172  -0.0245 -0.0494 152  THR A CA  
955   C C   . THR A 154  ? 0.4651 0.4093 0.4959 0.0150  -0.0254 -0.0419 152  THR A C   
956   O O   . THR A 154  ? 0.4472 0.3824 0.4850 0.0159  -0.0288 -0.0409 152  THR A O   
957   C CB  . THR A 154  ? 0.4406 0.3950 0.4629 0.0177  -0.0223 -0.0455 152  THR A CB  
958   O OG1 . THR A 154  ? 0.4511 0.4007 0.4656 0.0151  -0.0186 -0.0357 152  THR A OG1 
959   C CG2 . THR A 154  ? 0.3840 0.3509 0.4021 0.0191  -0.0205 -0.0510 152  THR A CG2 
960   N N   . GLY A 155  ? 0.4670 0.4116 0.4930 0.0122  -0.0224 -0.0363 153  GLY A N   
961   C CA  . GLY A 155  ? 0.4275 0.3624 0.4551 0.0100  -0.0226 -0.0283 153  GLY A CA  
962   C C   . GLY A 155  ? 0.4794 0.4083 0.5007 0.0091  -0.0199 -0.0197 153  GLY A C   
963   O O   . GLY A 155  ? 0.5514 0.4736 0.5732 0.0072  -0.0195 -0.0126 153  GLY A O   
964   N N   . LYS A 156  ? 0.4715 0.4035 0.4869 0.0103  -0.0179 -0.0201 154  LYS A N   
965   C CA  . LYS A 156  ? 0.4810 0.4080 0.4907 0.0099  -0.0158 -0.0131 154  LYS A CA  
966   C C   . LYS A 156  ? 0.4763 0.4088 0.4763 0.0087  -0.0110 -0.0103 154  LYS A C   
967   O O   . LYS A 156  ? 0.4063 0.3474 0.4039 0.0090  -0.0098 -0.0146 154  LYS A O   
968   C CB  . LYS A 156  ? 0.4849 0.4098 0.4971 0.0124  -0.0181 -0.0158 154  LYS A CB  
969   N N   . LEU A 157  ? 0.4453 0.3735 0.4401 0.0075  -0.0086 -0.0030 155  LEU A N   
970   C CA  . LEU A 157  ? 0.5231 0.4551 0.5098 0.0064  -0.0045 0.0001  155  LEU A CA  
971   C C   . LEU A 157  ? 0.5484 0.4799 0.5307 0.0075  -0.0035 0.0010  155  LEU A C   
972   O O   . LEU A 157  ? 0.5452 0.4709 0.5284 0.0083  -0.0048 0.0035  155  LEU A O   
973   C CB  . LEU A 157  ? 0.5487 0.4774 0.5328 0.0044  -0.0023 0.0068  155  LEU A CB  
974   N N   . THR A 158  ? 0.5450 0.4829 0.5229 0.0074  -0.0015 -0.0007 156  THR A N   
975   C CA  . THR A 158  ? 0.5576 0.4958 0.5310 0.0080  -0.0002 0.0005  156  THR A CA  
976   C C   . THR A 158  ? 0.5752 0.5154 0.5430 0.0063  0.0031  0.0045  156  THR A C   
977   O O   . THR A 158  ? 0.5952 0.5406 0.5623 0.0051  0.0043  0.0040  156  THR A O   
978   C CB  . THR A 158  ? 0.5814 0.5260 0.5562 0.0094  -0.0013 -0.0054 156  THR A CB  
979   N N   . SER A 159  ? 0.4719 0.4083 0.4359 0.0063  0.0044  0.0083  157  SER A N   
980   C CA  . SER A 159  ? 0.5078 0.4452 0.4675 0.0050  0.0071  0.0117  157  SER A CA  
981   C C   . SER A 159  ? 0.4792 0.4231 0.4374 0.0044  0.0080  0.0099  157  SER A C   
982   O O   . SER A 159  ? 0.5659 0.5130 0.5226 0.0029  0.0096  0.0118  157  SER A O   
983   C CB  . SER A 159  ? 0.5595 0.4917 0.5161 0.0055  0.0079  0.0153  157  SER A CB  
984   O OG  . SER A 159  ? 0.5577 0.4869 0.5154 0.0070  0.0059  0.0142  157  SER A OG  
985   N N   . THR A 160  ? 0.4965 0.4429 0.4554 0.0055  0.0068  0.0065  158  THR A N   
986   C CA  . THR A 160  ? 0.4261 0.3795 0.3839 0.0047  0.0076  0.0051  158  THR A CA  
987   C C   . THR A 160  ? 0.4109 0.3711 0.3720 0.0057  0.0061  -0.0004 158  THR A C   
988   O O   . THR A 160  ? 0.4277 0.3857 0.3921 0.0073  0.0040  -0.0035 158  THR A O   
989   C CB  . THR A 160  ? 0.4478 0.3991 0.4034 0.0050  0.0080  0.0063  158  THR A CB  
990   O OG1 . THR A 160  ? 0.4856 0.4330 0.4423 0.0070  0.0062  0.0044  158  THR A OG1 
991   C CG2 . THR A 160  ? 0.4650 0.4113 0.4178 0.0042  0.0095  0.0108  158  THR A CG2 
992   N N   . VAL A 161  ? 0.3488 0.3178 0.3093 0.0046  0.0069  -0.0015 159  VAL A N   
993   C CA  . VAL A 161  ? 0.3302 0.3087 0.2933 0.0052  0.0060  -0.0068 159  VAL A CA  
994   C C   . VAL A 161  ? 0.3110 0.2936 0.2746 0.0062  0.0055  -0.0096 159  VAL A C   
995   O O   . VAL A 161  ? 0.2892 0.2731 0.2505 0.0049  0.0068  -0.0067 159  VAL A O   
996   C CB  . VAL A 161  ? 0.3253 0.3129 0.2871 0.0030  0.0075  -0.0053 159  VAL A CB  
997   C CG1 . VAL A 161  ? 0.3499 0.3501 0.3136 0.0034  0.0070  -0.0105 159  VAL A CG1 
998   C CG2 . VAL A 161  ? 0.3886 0.3727 0.3507 0.0023  0.0077  -0.0034 159  VAL A CG2 
999   N N   . ASN A 162  ? 0.2898 0.2745 0.2570 0.0086  0.0034  -0.0155 160  ASN A N   
1000  C CA  . ASN A 162  ? 0.3193 0.3101 0.2876 0.0096  0.0029  -0.0189 160  ASN A CA  
1001  C C   . ASN A 162  ? 0.2473 0.2524 0.2158 0.0085  0.0040  -0.0214 160  ASN A C   
1002  O O   . ASN A 162  ? 0.2539 0.2663 0.2257 0.0101  0.0027  -0.0276 160  ASN A O   
1003  C CB  . ASN A 162  ? 0.2756 0.2629 0.2483 0.0129  0.0000  -0.0241 160  ASN A CB  
1004  C CG  . ASN A 162  ? 0.3522 0.3455 0.3262 0.0142  -0.0005 -0.0275 160  ASN A CG  
1005  O OD1 . ASN A 162  ? 0.2770 0.2803 0.2495 0.0126  0.0012  -0.0275 160  ASN A OD1 
1006  N ND2 . ASN A 162  ? 0.3237 0.3111 0.3008 0.0168  -0.0030 -0.0300 160  ASN A ND2 
1007  N N   . ASP A 163  ? 0.2502 0.2599 0.2157 0.0056  0.0062  -0.0166 161  ASP A N   
1008  C CA  . ASP A 163  ? 0.2663 0.2904 0.2315 0.0039  0.0074  -0.0171 161  ASP A CA  
1009  C C   . ASP A 163  ? 0.2849 0.3206 0.2522 0.0050  0.0070  -0.0223 161  ASP A C   
1010  O O   . ASP A 163  ? 0.2764 0.3258 0.2446 0.0048  0.0074  -0.0256 161  ASP A O   
1011  C CB  . ASP A 163  ? 0.2807 0.3058 0.2429 0.0003  0.0094  -0.0095 161  ASP A CB  
1012  C CG  . ASP A 163  ? 0.3372 0.3561 0.2985 -0.0007 0.0098  -0.0055 161  ASP A CG  
1013  O OD1 . ASP A 163  ? 0.2781 0.2866 0.2394 0.0012  0.0089  -0.0064 161  ASP A OD1 
1014  O OD2 . ASP A 163  ? 0.3449 0.3699 0.3058 -0.0035 0.0110  -0.0013 161  ASP A OD2 
1015  N N   . ARG A 164  ? 0.2509 0.2823 0.2193 0.0064  0.0062  -0.0236 162  ARG A N   
1016  C CA  . ARG A 164  ? 0.2485 0.2913 0.2196 0.0078  0.0056  -0.0291 162  ARG A CA  
1017  C C   . ARG A 164  ? 0.2526 0.2980 0.2279 0.0116  0.0034  -0.0377 162  ARG A C   
1018  O O   . ARG A 164  ? 0.2552 0.3146 0.2327 0.0126  0.0033  -0.0434 162  ARG A O   
1019  C CB  . ARG A 164  ? 0.2570 0.2948 0.2285 0.0083  0.0052  -0.0281 162  ARG A CB  
1020  C CG  . ARG A 164  ? 0.3164 0.3535 0.2850 0.0047  0.0070  -0.0208 162  ARG A CG  
1021  C CD  . ARG A 164  ? 0.3923 0.4420 0.3599 0.0014  0.0090  -0.0175 162  ARG A CD  
1022  N NE  . ARG A 164  ? 0.4017 0.4680 0.3714 0.0018  0.0092  -0.0223 162  ARG A NE  
1023  C CZ  . ARG A 164  ? 0.4353 0.5158 0.4046 -0.0001 0.0106  -0.0217 162  ARG A CZ  
1024  N NH1 . ARG A 164  ? 0.4637 0.5431 0.4306 -0.0028 0.0116  -0.0161 162  ARG A NH1 
1025  N NH2 . ARG A 164  ? 0.4130 0.5097 0.3843 0.0007  0.0108  -0.0268 162  ARG A NH2 
1026  N N   . SER A 165  ? 0.2625 0.2950 0.2395 0.0136  0.0014  -0.0387 163  SER A N   
1027  C CA  . SER A 165  ? 0.2770 0.3106 0.2591 0.0170  -0.0013 -0.0466 163  SER A CA  
1028  C C   . SER A 165  ? 0.2760 0.3198 0.2583 0.0163  -0.0008 -0.0495 163  SER A C   
1029  O O   . SER A 165  ? 0.2332 0.2870 0.2196 0.0187  -0.0022 -0.0576 163  SER A O   
1030  C CB  . SER A 165  ? 0.3069 0.3244 0.2911 0.0185  -0.0036 -0.0454 163  SER A CB  
1031  O OG  . SER A 165  ? 0.2638 0.2816 0.2540 0.0214  -0.0066 -0.0526 163  SER A OG  
1032  N N   . LEU A 166  ? 0.2531 0.2947 0.2314 0.0133  0.0011  -0.0433 164  LEU A N   
1033  C CA  . LEU A 166  ? 0.2473 0.2989 0.2254 0.0126  0.0015  -0.0455 164  LEU A CA  
1034  C C   . LEU A 166  ? 0.2571 0.3277 0.2338 0.0114  0.0033  -0.0472 164  LEU A C   
1035  O O   . LEU A 166  ? 0.2320 0.3152 0.2106 0.0126  0.0027  -0.0536 164  LEU A O   
1036  C CB  . LEU A 166  ? 0.2552 0.2996 0.2297 0.0098  0.0029  -0.0381 164  LEU A CB  
1037  C CG  . LEU A 166  ? 0.2642 0.2920 0.2403 0.0108  0.0013  -0.0367 164  LEU A CG  
1038  C CD1 . LEU A 166  ? 0.3007 0.3226 0.2729 0.0079  0.0031  -0.0288 164  LEU A CD1 
1039  C CD2 . LEU A 166  ? 0.2347 0.2627 0.2163 0.0134  -0.0016 -0.0441 164  LEU A CD2 
1040  N N   . ALA A 167  ? 0.2318 0.3056 0.2056 0.0090  0.0053  -0.0417 165  ALA A N   
1041  C CA  . ALA A 167  ? 0.2901 0.3830 0.2631 0.0076  0.0069  -0.0427 165  ALA A CA  
1042  C C   . ALA A 167  ? 0.2682 0.3716 0.2457 0.0112  0.0054  -0.0527 165  ALA A C   
1043  O O   . ALA A 167  ? 0.2302 0.3511 0.2082 0.0116  0.0059  -0.0574 165  ALA A O   
1044  C CB  . ALA A 167  ? 0.2918 0.3853 0.2621 0.0042  0.0090  -0.0347 165  ALA A CB  
1045  N N   . ALA A 168  ? 0.2291 0.3225 0.2099 0.0142  0.0035  -0.0562 166  ALA A N   
1046  C CA  . ALA A 168  ? 0.2836 0.3860 0.2696 0.0181  0.0016  -0.0663 166  ALA A CA  
1047  C C   . ALA A 168  ? 0.2534 0.3595 0.2433 0.0210  -0.0007 -0.0748 166  ALA A C   
1048  O O   . ALA A 168  ? 0.2451 0.3676 0.2376 0.0230  -0.0011 -0.0829 166  ALA A O   
1049  C CB  . ALA A 168  ? 0.2611 0.3507 0.2503 0.0207  -0.0005 -0.0675 166  ALA A CB  
1050  N N   . ALA A 169  ? 0.2675 0.3594 0.2579 0.0212  -0.0021 -0.0730 167  ALA A N   
1051  C CA  . ALA A 169  ? 0.2598 0.3535 0.2547 0.0238  -0.0047 -0.0810 167  ALA A CA  
1052  C C   . ALA A 169  ? 0.2338 0.3452 0.2260 0.0222  -0.0030 -0.0828 167  ALA A C   
1053  O O   . ALA A 169  ? 0.2202 0.3433 0.2165 0.0250  -0.0047 -0.0925 167  ALA A O   
1054  C CB  . ALA A 169  ? 0.2452 0.3200 0.2410 0.0234  -0.0064 -0.0772 167  ALA A CB  
1055  N N   . LEU A 170  ? 0.2704 0.3848 0.2562 0.0179  0.0002  -0.0735 168  LEU A N   
1056  C CA  . LEU A 170  ? 0.2521 0.3835 0.2349 0.0160  0.0018  -0.0737 168  LEU A CA  
1057  C C   . LEU A 170  ? 0.2534 0.4069 0.2367 0.0169  0.0028  -0.0793 168  LEU A C   
1058  O O   . LEU A 170  ? 0.2434 0.4130 0.2277 0.0181  0.0023  -0.0863 168  LEU A O   
1059  C CB  . LEU A 170  ? 0.2756 0.4041 0.2521 0.0111  0.0046  -0.0616 168  LEU A CB  
1060  C CG  . LEU A 170  ? 0.2559 0.4011 0.2293 0.0089  0.0060  -0.0602 168  LEU A CG  
1061  C CD1 . LEU A 170  ? 0.2615 0.4064 0.2376 0.0111  0.0037  -0.0673 168  LEU A CD1 
1062  C CD2 . LEU A 170  ? 0.3573 0.4976 0.3257 0.0042  0.0083  -0.0478 168  LEU A CD2 
1063  N N   . THR A 171  ? 0.2405 0.3960 0.2232 0.0162  0.0041  -0.0765 169  THR A N   
1064  C CA  . THR A 171  ? 0.2828 0.4595 0.2666 0.0171  0.0051  -0.0820 169  THR A CA  
1065  C C   . THR A 171  ? 0.2862 0.4683 0.2767 0.0227  0.0020  -0.0960 169  THR A C   
1066  O O   . THR A 171  ? 0.2552 0.4576 0.2468 0.0242  0.0021  -0.1037 169  THR A O   
1067  C CB  . THR A 171  ? 0.2546 0.4293 0.2376 0.0155  0.0066  -0.0765 169  THR A CB  
1068  O OG1 . THR A 171  ? 0.3178 0.4889 0.2955 0.0103  0.0091  -0.0641 169  THR A OG1 
1069  C CG2 . THR A 171  ? 0.3035 0.5005 0.2883 0.0166  0.0076  -0.0823 169  THR A CG2 
1070  N N   . ARG A 172  ? 0.2436 0.4078 0.2391 0.0259  -0.0010 -0.0995 170  ARG A N   
1071  C CA  . ARG A 172  ? 0.2725 0.4395 0.2759 0.0314  -0.0046 -0.1127 170  ARG A CA  
1072  C C   . ARG A 172  ? 0.2510 0.4258 0.2564 0.0329  -0.0063 -0.1201 170  ARG A C   
1073  O O   . ARG A 172  ? 0.2708 0.4625 0.2802 0.0362  -0.0075 -0.1312 170  ARG A O   
1074  C CB  . ARG A 172  ? 0.2584 0.4028 0.2668 0.0339  -0.0079 -0.1129 170  ARG A CB  
1075  C CG  . ARG A 172  ? 0.2726 0.4190 0.2906 0.0397  -0.0120 -0.1258 170  ARG A CG  
1076  C CD  . ARG A 172  ? 0.2736 0.3968 0.2968 0.0418  -0.0157 -0.1248 170  ARG A CD  
1077  N NE  . ARG A 172  ? 0.2376 0.3479 0.2563 0.0391  -0.0139 -0.1142 170  ARG A NE  
1078  C CZ  . ARG A 172  ? 0.2307 0.3251 0.2451 0.0360  -0.0131 -0.1043 170  ARG A CZ  
1079  N NH1 . ARG A 172  ? 0.2597 0.3484 0.2736 0.0348  -0.0136 -0.1030 170  ARG A NH1 
1080  N NH2 . ARG A 172  ? 0.2524 0.3368 0.2632 0.0341  -0.0117 -0.0960 170  ARG A NH2 
1081  N N   . LEU A 173  ? 0.2490 0.4122 0.2519 0.0306  -0.0064 -0.1145 171  LEU A N   
1082  C CA  . LEU A 173  ? 0.2673 0.4361 0.2731 0.0323  -0.0086 -0.1220 171  LEU A CA  
1083  C C   . LEU A 173  ? 0.2659 0.4598 0.2672 0.0308  -0.0061 -0.1238 171  LEU A C   
1084  O O   . LEU A 173  ? 0.2329 0.4402 0.2379 0.0338  -0.0080 -0.1347 171  LEU A O   
1085  C CB  . LEU A 173  ? 0.2724 0.4227 0.2770 0.0302  -0.0094 -0.1154 171  LEU A CB  
1086  C CG  . LEU A 173  ? 0.2625 0.4108 0.2588 0.0249  -0.0059 -0.1029 171  LEU A CG  
1087  C CD1 . LEU A 173  ? 0.2876 0.4514 0.2818 0.0240  -0.0055 -0.1056 171  LEU A CD1 
1088  C CD2 . LEU A 173  ? 0.2750 0.3996 0.2711 0.0234  -0.0066 -0.0951 171  LEU A CD2 
1089  N N   . ILE A 174  ? 0.2549 0.4560 0.2487 0.0263  -0.0020 -0.1133 172  ILE A N   
1090  C CA  . ILE A 174  ? 0.2866 0.5128 0.2760 0.0244  0.0003  -0.1137 172  ILE A CA  
1091  C C   . ILE A 174  ? 0.2498 0.4971 0.2424 0.0277  0.0003  -0.1239 172  ILE A C   
1092  O O   . ILE A 174  ? 0.3052 0.5727 0.2987 0.0296  -0.0002 -0.1328 172  ILE A O   
1093  C CB  . ILE A 174  ? 0.2940 0.5217 0.2756 0.0185  0.0042  -0.0989 172  ILE A CB  
1094  C CG1 . ILE A 174  ? 0.2919 0.5044 0.2705 0.0157  0.0042  -0.0907 172  ILE A CG1 
1095  C CG2 . ILE A 174  ? 0.3146 0.5705 0.2922 0.0164  0.0068  -0.0985 172  ILE A CG2 
1096  C CD1 . ILE A 174  ? 0.3204 0.5293 0.2930 0.0103  0.0073  -0.0761 172  ILE A CD1 
1097  N N   . SER A 175  ? 0.2812 0.5246 0.2757 0.0286  0.0007  -0.1234 173  SER A N   
1098  C CA  . SER A 175  ? 0.2814 0.5451 0.2794 0.0317  0.0008  -0.1330 173  SER A CA  
1099  C C   . SER A 175  ? 0.3177 0.5835 0.3242 0.0381  -0.0035 -0.1491 173  SER A C   
1100  O O   . SER A 175  ? 0.3073 0.5953 0.3165 0.0412  -0.0037 -0.1597 173  SER A O   
1101  C CB  . SER A 175  ? 0.2930 0.5500 0.2919 0.0314  0.0018  -0.1288 173  SER A CB  
1102  O OG  . SER A 175  ? 0.3522 0.6113 0.3442 0.0256  0.0056  -0.1152 173  SER A OG  
1103  N N   . ARG A 176  ? 0.2811 0.5248 0.2922 0.0401  -0.0071 -0.1512 174  ARG A N   
1104  C CA  . ARG A 176  ? 0.3313 0.5741 0.3522 0.0461  -0.0119 -0.1661 174  ARG A CA  
1105  C C   . ARG A 176  ? 0.3247 0.5799 0.3458 0.0469  -0.0131 -0.1732 174  ARG A C   
1106  O O   . ARG A 176  ? 0.3332 0.6052 0.3597 0.0513  -0.0151 -0.1870 174  ARG A O   
1107  C CB  . ARG A 176  ? 0.3537 0.5676 0.3803 0.0476  -0.0156 -0.1646 174  ARG A CB  
1108  C CG  . ARG A 176  ? 0.3422 0.5531 0.3810 0.0540  -0.0212 -0.1796 174  ARG A CG  
1109  C CD  . ARG A 176  ? 0.3030 0.4858 0.3480 0.0552  -0.0250 -0.1766 174  ARG A CD  
1110  N NE  . ARG A 176  ? 0.3002 0.4668 0.3434 0.0522  -0.0257 -0.1697 174  ARG A NE  
1111  C CZ  . ARG A 176  ? 0.3241 0.4735 0.3615 0.0480  -0.0236 -0.1561 174  ARG A CZ  
1112  N NH1 . ARG A 176  ? 0.2933 0.4381 0.3259 0.0461  -0.0209 -0.1475 174  ARG A NH1 
1113  N NH2 . ARG A 176  ? 0.3340 0.4710 0.3708 0.0459  -0.0245 -0.1514 174  ARG A NH2 
1114  N N   . CYS A 177  ? 0.3180 0.5660 0.3335 0.0428  -0.0118 -0.1642 175  CYS A N   
1115  C CA  . CYS A 177  ? 0.3181 0.5740 0.3344 0.0435  -0.0136 -0.1706 175  CYS A CA  
1116  C C   . CYS A 177  ? 0.3690 0.6441 0.3761 0.0393  -0.0098 -0.1641 175  CYS A C   
1117  O O   . CYS A 177  ? 0.3735 0.6608 0.3812 0.0403  -0.0111 -0.1710 175  CYS A O   
1118  C CB  . CYS A 177  ? 0.3219 0.5528 0.3414 0.0429  -0.0165 -0.1673 175  CYS A CB  
1119  S SG  . CYS A 177  ? 0.4130 0.6163 0.4425 0.0464  -0.0209 -0.1700 175  CYS A SG  
1120  N N   . GLY A 178  ? 0.3648 0.6416 0.3639 0.0343  -0.0054 -0.1505 176  GLY A N   
1121  C CA  . GLY A 178  ? 0.3421 0.6405 0.3333 0.0304  -0.0019 -0.1444 176  GLY A CA  
1122  C C   . GLY A 178  ? 0.3403 0.6351 0.3276 0.0276  -0.0021 -0.1390 176  GLY A C   
1123  O O   . GLY A 178  ? 0.3169 0.5889 0.3054 0.0268  -0.0035 -0.1344 176  GLY A O   
1124  N N   . GLU A 179  ? 0.3375 0.6568 0.3202 0.0260  -0.0004 -0.1393 177  GLU A N   
1125  C CA  . GLU A 179  ? 0.3296 0.6485 0.3077 0.0228  -0.0002 -0.1326 177  GLU A CA  
1126  C C   . GLU A 179  ? 0.3177 0.6219 0.3012 0.0256  -0.0043 -0.1402 177  GLU A C   
1127  O O   . GLU A 179  ? 0.3663 0.6552 0.3476 0.0226  -0.0042 -0.1313 177  GLU A O   
1128  C CB  . GLU A 179  ? 0.3329 0.6836 0.3057 0.0213  0.0018  -0.1334 177  GLU A CB  
1129  C CG  . GLU A 179  ? 0.4293 0.7825 0.3964 0.0173  0.0025  -0.1243 177  GLU A CG  
1130  C CD  . GLU A 179  ? 0.5658 0.9340 0.5345 0.0201  -0.0001 -0.1360 177  GLU A CD  
1131  O OE1 . GLU A 179  ? 0.5712 0.9280 0.5471 0.0244  -0.0039 -0.1476 177  GLU A OE1 
1132  O OE2 . GLU A 179  ? 0.6652 1.0536 0.6320 0.0177  0.0011  -0.1314 177  GLU A OE2 
1133  N N   . PRO A 180  ? 0.2802 0.5882 0.2716 0.0310  -0.0080 -0.1561 178  PRO A N   
1134  C CA  . PRO A 180  ? 0.3341 0.6277 0.3314 0.0330  -0.0122 -0.1624 178  PRO A CA  
1135  C C   . PRO A 180  ? 0.3349 0.5971 0.3341 0.0314  -0.0130 -0.1536 178  PRO A C   
1136  O O   . PRO A 180  ? 0.3617 0.6133 0.3614 0.0300  -0.0145 -0.1509 178  PRO A O   
1137  C CB  . PRO A 180  ? 0.3493 0.6498 0.3561 0.0394  -0.0162 -0.1805 178  PRO A CB  
1138  C CG  . PRO A 180  ? 0.3481 0.6771 0.3525 0.0400  -0.0137 -0.1837 178  PRO A CG  
1139  C CD  . PRO A 180  ? 0.3307 0.6592 0.3260 0.0355  -0.0088 -0.1697 178  PRO A CD  
1140  N N   . VAL A 181  ? 0.3251 0.5729 0.3254 0.0314  -0.0122 -0.1489 179  VAL A N   
1141  C CA  . VAL A 181  ? 0.3235 0.5429 0.3256 0.0300  -0.0130 -0.1409 179  VAL A CA  
1142  C C   . VAL A 181  ? 0.3223 0.5355 0.3158 0.0244  -0.0094 -0.1251 179  VAL A C   
1143  O O   . VAL A 181  ? 0.2929 0.4880 0.2869 0.0228  -0.0102 -0.1193 179  VAL A O   
1144  C CB  . VAL A 181  ? 0.3084 0.5144 0.3147 0.0321  -0.0137 -0.1415 179  VAL A CB  
1145  C CG1 . VAL A 181  ? 0.3077 0.5199 0.3072 0.0294  -0.0094 -0.1326 179  VAL A CG1 
1146  C CG2 . VAL A 181  ? 0.3063 0.4843 0.3166 0.0317  -0.0158 -0.1365 179  VAL A CG2 
1147  N N   . ILE A 182  ? 0.3373 0.5658 0.3234 0.0213  -0.0056 -0.1179 180  ILE A N   
1148  C CA  . ILE A 182  ? 0.2851 0.5094 0.2641 0.0162  -0.0026 -0.1033 180  ILE A CA  
1149  C C   . ILE A 182  ? 0.3236 0.5519 0.3013 0.0150  -0.0036 -0.1031 180  ILE A C   
1150  O O   . ILE A 182  ? 0.3220 0.5353 0.2980 0.0124  -0.0033 -0.0944 180  ILE A O   
1151  C CB  . ILE A 182  ? 0.3082 0.5501 0.2810 0.0132  0.0012  -0.0962 180  ILE A CB  
1152  C CG1 . ILE A 182  ? 0.3218 0.5609 0.2964 0.0144  0.0020  -0.0971 180  ILE A CG1 
1153  C CG2 . ILE A 182  ? 0.3090 0.5445 0.2757 0.0079  0.0037  -0.0808 180  ILE A CG2 
1154  C CD1 . ILE A 182  ? 0.3892 0.6483 0.3591 0.0117  0.0054  -0.0918 180  ILE A CD1 
1155  N N   . ARG A 183  ? 0.3259 0.5756 0.3043 0.0169  -0.0048 -0.1128 181  ARG A N   
1156  C CA  . ARG A 183  ? 0.3725 0.6279 0.3502 0.0162  -0.0062 -0.1142 181  ARG A CA  
1157  C C   . ARG A 183  ? 0.3793 0.6124 0.3631 0.0176  -0.0095 -0.1168 181  ARG A C   
1158  O O   . ARG A 183  ? 0.3510 0.5758 0.3328 0.0149  -0.0094 -0.1096 181  ARG A O   
1159  C CB  . ARG A 183  ? 0.3403 0.6224 0.3191 0.0191  -0.0076 -0.1270 181  ARG A CB  
1160  C CG  . ARG A 183  ? 0.4656 0.7551 0.4450 0.0194  -0.0099 -0.1319 181  ARG A CG  
1161  C CD  . ARG A 183  ? 0.4823 0.7876 0.4533 0.0150  -0.0072 -0.1215 181  ARG A CD  
1162  N NE  . ARG A 183  ? 0.4865 0.7729 0.4547 0.0111  -0.0061 -0.1079 181  ARG A NE  
1163  C CZ  . ARG A 183  ? 0.5090 0.7952 0.4709 0.0068  -0.0028 -0.0934 181  ARG A CZ  
1164  N NH1 . ARG A 183  ? 0.4548 0.7584 0.4122 0.0052  0.0000  -0.0894 181  ARG A NH1 
1165  N NH2 . ARG A 183  ? 0.4768 0.7454 0.4375 0.0039  -0.0023 -0.0828 181  ARG A NH2 
1166  N N   . ARG A 184  ? 0.3672 0.5902 0.3590 0.0216  -0.0126 -0.1268 182  ARG A N   
1167  C CA  . ARG A 184  ? 0.3843 0.5863 0.3829 0.0226  -0.0160 -0.1290 182  ARG A CA  
1168  C C   . ARG A 184  ? 0.3176 0.4970 0.3136 0.0193  -0.0141 -0.1153 182  ARG A C   
1169  O O   . ARG A 184  ? 0.3795 0.5462 0.3772 0.0180  -0.0153 -0.1118 182  ARG A O   
1170  C CB  . ARG A 184  ? 0.3706 0.5667 0.3791 0.0275  -0.0200 -0.1416 182  ARG A CB  
1171  C CG  . ARG A 184  ? 0.3979 0.6107 0.4125 0.0314  -0.0236 -0.1574 182  ARG A CG  
1172  C CD  . ARG A 184  ? 0.4018 0.6029 0.4238 0.0321  -0.0280 -0.1621 182  ARG A CD  
1173  N NE  . ARG A 184  ? 0.4170 0.6003 0.4501 0.0353  -0.0323 -0.1688 182  ARG A NE  
1174  C CZ  . ARG A 184  ? 0.4347 0.5949 0.4724 0.0341  -0.0342 -0.1633 182  ARG A CZ  
1175  N NH1 . ARG A 184  ? 0.4596 0.6111 0.4922 0.0299  -0.0321 -0.1518 182  ARG A NH1 
1176  N NH2 . ARG A 184  ? 0.4279 0.5741 0.4762 0.0371  -0.0384 -0.1694 182  ARG A NH2 
1177  N N   . GLY A 185  ? 0.3012 0.4759 0.2935 0.0181  -0.0113 -0.1080 183  GLY A N   
1178  C CA  . GLY A 185  ? 0.3372 0.4923 0.3265 0.0151  -0.0094 -0.0955 183  GLY A CA  
1179  C C   . GLY A 185  ? 0.3417 0.4991 0.3247 0.0111  -0.0071 -0.0851 183  GLY A C   
1180  O O   . GLY A 185  ? 0.3337 0.4755 0.3170 0.0095  -0.0072 -0.0788 183  GLY A O   
1181  N N   . VAL A 186  ? 0.3298 0.5074 0.3074 0.0095  -0.0051 -0.0833 184  VAL A N   
1182  C CA  . VAL A 186  ? 0.3514 0.5323 0.3234 0.0056  -0.0031 -0.0731 184  VAL A CA  
1183  C C   . VAL A 186  ? 0.3454 0.5237 0.3202 0.0060  -0.0056 -0.0763 184  VAL A C   
1184  O O   . VAL A 186  ? 0.3650 0.5321 0.3386 0.0036  -0.0051 -0.0681 184  VAL A O   
1185  C CB  . VAL A 186  ? 0.3899 0.5949 0.3563 0.0038  -0.0010 -0.0707 184  VAL A CB  
1186  C CG1 . VAL A 186  ? 0.3645 0.5751 0.3265 0.0003  0.0000  -0.0616 184  VAL A CG1 
1187  C CG2 . VAL A 186  ? 0.2648 0.4698 0.2284 0.0024  0.0018  -0.0643 184  VAL A CG2 
1188  N N   . ASP A 187  ? 0.3685 0.5576 0.3477 0.0090  -0.0085 -0.0888 185  ASP A N   
1189  C CA  . ASP A 187  ? 0.3808 0.5684 0.3635 0.0093  -0.0113 -0.0930 185  ASP A CA  
1190  C C   . ASP A 187  ? 0.3987 0.5617 0.3871 0.0096  -0.0131 -0.0915 185  ASP A C   
1191  O O   . ASP A 187  ? 0.4234 0.5792 0.4122 0.0078  -0.0136 -0.0870 185  ASP A O   
1192  C CB  . ASP A 187  ? 0.3733 0.5778 0.3604 0.0129  -0.0144 -0.1080 185  ASP A CB  
1193  C CG  . ASP A 187  ? 0.4624 0.6940 0.4434 0.0123  -0.0125 -0.1089 185  ASP A CG  
1194  O OD1 . ASP A 187  ? 0.5013 0.7379 0.4751 0.0085  -0.0094 -0.0971 185  ASP A OD1 
1195  O OD2 . ASP A 187  ? 0.4141 0.6622 0.3977 0.0155  -0.0142 -0.1212 185  ASP A OD2 
1196  N N   . MET A 188  ? 0.3887 0.5392 0.3818 0.0118  -0.0142 -0.0949 186  MET A N   
1197  C CA  . MET A 188  ? 0.3633 0.4907 0.3613 0.0117  -0.0155 -0.0917 186  MET A CA  
1198  C C   . MET A 188  ? 0.3718 0.4877 0.3640 0.0080  -0.0123 -0.0776 186  MET A C   
1199  O O   . MET A 188  ? 0.4227 0.5279 0.4168 0.0066  -0.0130 -0.0735 186  MET A O   
1200  C CB  . MET A 188  ? 0.3857 0.5036 0.3885 0.0144  -0.0168 -0.0962 186  MET A CB  
1201  C CG  . MET A 188  ? 0.4645 0.5598 0.4732 0.0144  -0.0187 -0.0934 186  MET A CG  
1202  S SD  . MET A 188  ? 0.6763 0.7678 0.6953 0.0159  -0.0240 -0.1025 186  MET A SD  
1203  C CE  . MET A 188  ? 0.4835 0.5892 0.5090 0.0207  -0.0276 -0.1189 186  MET A CE  
1204  N N   . ALA A 189  ? 0.3487 0.4668 0.3347 0.0066  -0.0089 -0.0703 187  ALA A N   
1205  C CA  . ALA A 189  ? 0.3538 0.4613 0.3352 0.0035  -0.0061 -0.0577 187  ALA A CA  
1206  C C   . ALA A 189  ? 0.3365 0.4501 0.3149 0.0010  -0.0054 -0.0526 187  ALA A C   
1207  O O   . ALA A 189  ? 0.3688 0.4706 0.3465 -0.0008 -0.0046 -0.0448 187  ALA A O   
1208  C CB  . ALA A 189  ? 0.3461 0.4569 0.3220 0.0023  -0.0030 -0.0515 187  ALA A CB  
1209  N N   . MET A 190  ? 0.3421 0.4751 0.3188 0.0011  -0.0059 -0.0569 188  MET A N   
1210  C CA  . MET A 190  ? 0.4259 0.5665 0.3999 -0.0012 -0.0056 -0.0521 188  MET A CA  
1211  C C   . MET A 190  ? 0.4036 0.5346 0.3827 -0.0008 -0.0081 -0.0549 188  MET A C   
1212  O O   . MET A 190  ? 0.4273 0.5525 0.4051 -0.0029 -0.0073 -0.0471 188  MET A O   
1213  C CB  . MET A 190  ? 0.3491 0.5141 0.3203 -0.0010 -0.0059 -0.0570 188  MET A CB  
1214  C CG  . MET A 190  ? 0.4685 0.6433 0.4359 -0.0036 -0.0053 -0.0504 188  MET A CG  
1215  S SD  . MET A 190  ? 0.6004 0.8059 0.5639 -0.0035 -0.0055 -0.0555 188  MET A SD  
1216  C CE  . MET A 190  ? 0.5136 0.7272 0.4732 -0.0040 -0.0026 -0.0522 188  MET A CE  
1217  N N   . ARG A 191  ? 0.3928 0.5219 0.3786 0.0020  -0.0114 -0.0658 189  ARG A N   
1218  C CA  . ARG A 191  ? 0.4071 0.5263 0.3990 0.0021  -0.0141 -0.0684 189  ARG A CA  
1219  C C   . ARG A 191  ? 0.4346 0.5323 0.4282 0.0010  -0.0132 -0.0605 189  ARG A C   
1220  O O   . ARG A 191  ? 0.4095 0.5001 0.4045 -0.0006 -0.0135 -0.0560 189  ARG A O   
1221  C CB  . ARG A 191  ? 0.3744 0.4961 0.3744 0.0053  -0.0183 -0.0820 189  ARG A CB  
1222  N N   . MET A 192  ? 0.3766 0.4647 0.3701 0.0018  -0.0121 -0.0590 190  MET A N   
1223  C CA  . MET A 192  ? 0.3824 0.4513 0.3776 0.0010  -0.0115 -0.0523 190  MET A CA  
1224  C C   . MET A 192  ? 0.4079 0.4731 0.3973 -0.0018 -0.0082 -0.0408 190  MET A C   
1225  O O   . MET A 192  ? 0.4045 0.4596 0.3958 -0.0031 -0.0082 -0.0361 190  MET A O   
1226  C CB  . MET A 192  ? 0.4224 0.4833 0.4182 0.0025  -0.0111 -0.0531 190  MET A CB  
1227  C CG  . MET A 192  ? 0.4283 0.4886 0.4316 0.0055  -0.0148 -0.0639 190  MET A CG  
1228  S SD  . MET A 192  ? 0.5250 0.5740 0.5286 0.0070  -0.0141 -0.0624 190  MET A SD  
1229  C CE  . MET A 192  ? 0.5069 0.5352 0.5154 0.0059  -0.0153 -0.0565 190  MET A CE  
1230  N N   . MET A 193  ? 0.3502 0.4239 0.3331 -0.0029 -0.0055 -0.0360 191  MET A N   
1231  C CA  . MET A 193  ? 0.4367 0.5065 0.4148 -0.0053 -0.0027 -0.0252 191  MET A CA  
1232  C C   . MET A 193  ? 0.4141 0.4920 0.3911 -0.0069 -0.0029 -0.0222 191  MET A C   
1233  O O   . MET A 193  ? 0.4264 0.4985 0.4016 -0.0086 -0.0013 -0.0139 191  MET A O   
1234  C CB  . MET A 193  ? 0.4181 0.4935 0.3909 -0.0059 -0.0003 -0.0210 191  MET A CB  
1235  C CG  . MET A 193  ? 0.4053 0.4708 0.3785 -0.0046 0.0003  -0.0217 191  MET A CG  
1236  S SD  . MET A 193  ? 0.5414 0.6101 0.5089 -0.0062 0.0034  -0.0141 191  MET A SD  
1237  C CE  . MET A 193  ? 0.4215 0.5128 0.3869 -0.0063 0.0031  -0.0188 191  MET A CE  
1238  N N   . GLY A 194  ? 0.4255 0.5170 0.4039 -0.0063 -0.0049 -0.0291 192  GLY A N   
1239  C CA  . GLY A 194  ? 0.3873 0.4880 0.3645 -0.0078 -0.0053 -0.0265 192  GLY A CA  
1240  C C   . GLY A 194  ? 0.4574 0.5536 0.4403 -0.0075 -0.0079 -0.0308 192  GLY A C   
1241  O O   . GLY A 194  ? 0.4397 0.5383 0.4223 -0.0090 -0.0080 -0.0265 192  GLY A O   
1242  N N   . GLU A 195  ? 0.4134 0.5030 0.4023 -0.0056 -0.0104 -0.0389 193  GLU A N   
1243  C CA  . GLU A 195  ? 0.4160 0.5023 0.4118 -0.0053 -0.0135 -0.0441 193  GLU A CA  
1244  C C   . GLU A 195  ? 0.3661 0.4344 0.3682 -0.0050 -0.0146 -0.0441 193  GLU A C   
1245  O O   . GLU A 195  ? 0.3335 0.3971 0.3412 -0.0056 -0.0167 -0.0452 193  GLU A O   
1246  C CB  . GLU A 195  ? 0.4108 0.5104 0.4102 -0.0033 -0.0168 -0.0562 193  GLU A CB  
1247  C CG  . GLU A 195  ? 0.5368 0.6567 0.5305 -0.0037 -0.0162 -0.0572 193  GLU A CG  
1248  C CD  . GLU A 195  ? 0.5766 0.7102 0.5730 -0.0010 -0.0189 -0.0699 193  GLU A CD  
1249  O OE1 . GLU A 195  ? 0.5846 0.7160 0.5886 0.0004  -0.0227 -0.0788 193  GLU A OE1 
1250  O OE2 . GLU A 195  ? 0.6263 0.7726 0.6177 -0.0004 -0.0174 -0.0710 193  GLU A OE2 
1251  N N   . GLN A 196  ? 0.3885 0.4472 0.3901 -0.0041 -0.0135 -0.0427 194  GLN A N   
1252  C CA  . GLN A 196  ? 0.3857 0.4286 0.3936 -0.0037 -0.0149 -0.0430 194  GLN A CA  
1253  C C   . GLN A 196  ? 0.4079 0.4383 0.4126 -0.0051 -0.0118 -0.0326 194  GLN A C   
1254  O O   . GLN A 196  ? 0.4221 0.4427 0.4307 -0.0062 -0.0122 -0.0290 194  GLN A O   
1255  C CB  . GLN A 196  ? 0.4329 0.4746 0.4444 -0.0011 -0.0170 -0.0508 194  GLN A CB  
1256  C CG  . GLN A 196  ? 0.5023 0.5564 0.5185 0.0009  -0.0206 -0.0628 194  GLN A CG  
1257  C CD  . GLN A 196  ? 0.5011 0.5551 0.5212 0.0038  -0.0227 -0.0711 194  GLN A CD  
1258  O OE1 . GLN A 196  ? 0.5831 0.6251 0.6044 0.0043  -0.0223 -0.0683 194  GLN A OE1 
1259  N NE2 . GLN A 196  ? 0.4998 0.5678 0.5219 0.0059  -0.0250 -0.0816 194  GLN A NE2 
1260  N N   . PHE A 197  ? 0.4118 0.4430 0.4098 -0.0052 -0.0087 -0.0278 195  PHE A N   
1261  C CA  . PHE A 197  ? 0.3768 0.3972 0.3716 -0.0063 -0.0059 -0.0187 195  PHE A CA  
1262  C C   . PHE A 197  ? 0.3916 0.4141 0.3840 -0.0082 -0.0042 -0.0120 195  PHE A C   
1263  O O   . PHE A 197  ? 0.3899 0.4030 0.3822 -0.0091 -0.0026 -0.0057 195  PHE A O   
1264  C CB  . PHE A 197  ? 0.3933 0.4139 0.3825 -0.0058 -0.0035 -0.0161 195  PHE A CB  
1265  C CG  . PHE A 197  ? 0.4564 0.4732 0.4482 -0.0038 -0.0050 -0.0216 195  PHE A CG  
1266  C CD1 . PHE A 197  ? 0.4949 0.5012 0.4929 -0.0031 -0.0072 -0.0237 195  PHE A CD1 
1267  C CD2 . PHE A 197  ? 0.4554 0.4795 0.4440 -0.0027 -0.0043 -0.0245 195  PHE A CD2 
1268  C CE1 . PHE A 197  ? 0.5652 0.5677 0.5664 -0.0012 -0.0089 -0.0286 195  PHE A CE1 
1269  C CE2 . PHE A 197  ? 0.4997 0.5204 0.4911 -0.0007 -0.0059 -0.0298 195  PHE A CE2 
1270  C CZ  . PHE A 197  ? 0.4510 0.4606 0.4488 0.0002  -0.0083 -0.0319 195  PHE A CZ  
1271  N N   . VAL A 198  ? 0.3435 0.3786 0.3341 -0.0087 -0.0046 -0.0134 196  VAL A N   
1272  C CA  . VAL A 198  ? 0.3621 0.3999 0.3516 -0.0103 -0.0038 -0.0078 196  VAL A CA  
1273  C C   . VAL A 198  ? 0.3565 0.4036 0.3497 -0.0105 -0.0066 -0.0138 196  VAL A C   
1274  O O   . VAL A 198  ? 0.3748 0.4299 0.3697 -0.0092 -0.0088 -0.0219 196  VAL A O   
1275  C CB  . VAL A 198  ? 0.3340 0.3787 0.3171 -0.0113 -0.0013 -0.0013 196  VAL A CB  
1276  C CG1 . VAL A 198  ? 0.3452 0.3805 0.3253 -0.0111 0.0012  0.0040  196  VAL A CG1 
1277  C CG2 . VAL A 198  ? 0.3927 0.4527 0.3730 -0.0110 -0.0021 -0.0056 196  VAL A CG2 
1278  N N   . THR A 199  ? 0.3434 0.3897 0.3385 -0.0118 -0.0068 -0.0101 197  THR A N   
1279  C CA  . THR A 199  ? 0.3405 0.3973 0.3386 -0.0120 -0.0094 -0.0152 197  THR A CA  
1280  C C   . THR A 199  ? 0.3729 0.4454 0.3654 -0.0123 -0.0090 -0.0145 197  THR A C   
1281  O O   . THR A 199  ? 0.4258 0.5107 0.4192 -0.0118 -0.0113 -0.0214 197  THR A O   
1282  C CB  . THR A 199  ? 0.3863 0.4380 0.3882 -0.0134 -0.0098 -0.0112 197  THR A CB  
1283  O OG1 . THR A 199  ? 0.3752 0.4133 0.3824 -0.0134 -0.0102 -0.0113 197  THR A OG1 
1284  C CG2 . THR A 199  ? 0.3745 0.4366 0.3800 -0.0137 -0.0128 -0.0167 197  THR A CG2 
1285  N N   . GLY A 200  ? 0.3625 0.4353 0.3495 -0.0131 -0.0062 -0.0064 198  GLY A N   
1286  C CA  . GLY A 200  ? 0.4037 0.4912 0.3855 -0.0137 -0.0057 -0.0043 198  GLY A CA  
1287  C C   . GLY A 200  ? 0.3975 0.4810 0.3748 -0.0146 -0.0028 0.0046  198  GLY A C   
1288  O O   . GLY A 200  ? 0.4012 0.4712 0.3793 -0.0146 -0.0012 0.0093  198  GLY A O   
1289  N N   . GLU A 201  ? 0.3617 0.4579 0.3346 -0.0152 -0.0023 0.0068  199  GLU A N   
1290  C CA  . GLU A 201  ? 0.3900 0.4837 0.3594 -0.0163 0.0000  0.0151  199  GLU A CA  
1291  C C   . GLU A 201  ? 0.3997 0.4902 0.3694 -0.0176 0.0005  0.0241  199  GLU A C   
1292  O O   . GLU A 201  ? 0.3759 0.4572 0.3452 -0.0180 0.0021  0.0305  199  GLU A O   
1293  C CB  . GLU A 201  ? 0.4347 0.5442 0.4000 -0.0170 0.0001  0.0151  199  GLU A CB  
1294  C CG  . GLU A 201  ? 0.5108 0.6200 0.4733 -0.0185 0.0019  0.0243  199  GLU A CG  
1295  C CD  . GLU A 201  ? 0.5632 0.6902 0.5221 -0.0196 0.0020  0.0247  199  GLU A CD  
1296  O OE1 . GLU A 201  ? 0.6036 0.7458 0.5614 -0.0197 0.0005  0.0211  199  GLU A OE1 
1297  O OE2 . GLU A 201  ? 0.6225 0.7488 0.5796 -0.0204 0.0034  0.0285  199  GLU A OE2 
1298  N N   . THR A 202  ? 0.3655 0.4638 0.3366 -0.0182 -0.0011 0.0242  200  THR A N   
1299  C CA  . THR A 202  ? 0.3422 0.4387 0.3145 -0.0192 -0.0011 0.0320  200  THR A CA  
1300  C C   . THR A 202  ? 0.3577 0.4507 0.3343 -0.0187 -0.0025 0.0286  200  THR A C   
1301  O O   . THR A 202  ? 0.3501 0.4457 0.3285 -0.0180 -0.0040 0.0204  200  THR A O   
1302  C CB  . THR A 202  ? 0.3652 0.4775 0.3348 -0.0208 -0.0020 0.0371  200  THR A CB  
1303  O OG1 . THR A 202  ? 0.3819 0.5081 0.3512 -0.0206 -0.0040 0.0302  200  THR A OG1 
1304  C CG2 . THR A 202  ? 0.4002 0.5174 0.3662 -0.0217 -0.0008 0.0408  200  THR A CG2 
1305  N N   . ILE A 203  ? 0.3114 0.3986 0.2902 -0.0192 -0.0021 0.0347  201  ILE A N   
1306  C CA  . ILE A 203  ? 0.3191 0.4032 0.3024 -0.0189 -0.0033 0.0320  201  ILE A CA  
1307  C C   . ILE A 203  ? 0.3201 0.4189 0.3038 -0.0194 -0.0059 0.0274  201  ILE A C   
1308  O O   . ILE A 203  ? 0.3336 0.4321 0.3209 -0.0190 -0.0076 0.0205  201  ILE A O   
1309  C CB  . ILE A 203  ? 0.3533 0.4303 0.3391 -0.0191 -0.0025 0.0394  201  ILE A CB  
1310  C CG1 . ILE A 203  ? 0.2480 0.3208 0.2390 -0.0190 -0.0033 0.0366  201  ILE A CG1 
1311  C CG2 . ILE A 203  ? 0.3499 0.4368 0.3343 -0.0201 -0.0033 0.0463  201  ILE A CG2 
1312  C CD1 . ILE A 203  ? 0.3095 0.3720 0.3028 -0.0183 -0.0028 0.0310  201  ILE A CD1 
1313  N N   . ARG A 204  ? 0.3092 0.4218 0.2894 -0.0203 -0.0066 0.0308  202  ARG A N   
1314  C CA  . ARG A 204  ? 0.3274 0.4558 0.3074 -0.0206 -0.0092 0.0264  202  ARG A CA  
1315  C C   . ARG A 204  ? 0.3611 0.4944 0.3412 -0.0195 -0.0104 0.0154  202  ARG A C   
1316  O O   . ARG A 204  ? 0.3736 0.5119 0.3568 -0.0192 -0.0127 0.0084  202  ARG A O   
1317  C CB  . ARG A 204  ? 0.3431 0.4862 0.3188 -0.0219 -0.0095 0.0329  202  ARG A CB  
1318  C CG  . ARG A 204  ? 0.4677 0.6143 0.4451 -0.0228 -0.0106 0.0400  202  ARG A CG  
1319  C CD  . ARG A 204  ? 0.5216 0.6776 0.4956 -0.0243 -0.0106 0.0496  202  ARG A CD  
1320  N NE  . ARG A 204  ? 0.5078 0.6621 0.4848 -0.0249 -0.0115 0.0577  202  ARG A NE  
1321  C CZ  . ARG A 204  ? 0.4947 0.6341 0.4751 -0.0244 -0.0103 0.0628  202  ARG A CZ  
1322  N NH1 . ARG A 204  ? 0.4456 0.5708 0.4264 -0.0235 -0.0080 0.0614  202  ARG A NH1 
1323  N NH2 . ARG A 204  ? 0.4405 0.5800 0.4242 -0.0246 -0.0115 0.0693  202  ARG A NH2 
1324  N N   . GLU A 205  ? 0.3744 0.5064 0.3517 -0.0190 -0.0090 0.0134  203  GLU A N   
1325  C CA  . GLU A 205  ? 0.3382 0.4744 0.3162 -0.0176 -0.0103 0.0025  203  GLU A CA  
1326  C C   . GLU A 205  ? 0.3788 0.5007 0.3628 -0.0165 -0.0111 -0.0033 203  GLU A C   
1327  O O   . GLU A 205  ? 0.3746 0.5004 0.3623 -0.0156 -0.0137 -0.0126 203  GLU A O   
1328  C CB  . GLU A 205  ? 0.4208 0.5590 0.3946 -0.0172 -0.0085 0.0027  203  GLU A CB  
1329  C CG  . GLU A 205  ? 0.4583 0.5973 0.4336 -0.0153 -0.0094 -0.0081 203  GLU A CG  
1330  C CD  . GLU A 205  ? 0.5270 0.6686 0.4980 -0.0151 -0.0074 -0.0069 203  GLU A CD  
1331  O OE1 . GLU A 205  ? 0.5649 0.7218 0.5314 -0.0161 -0.0069 -0.0039 203  GLU A OE1 
1332  O OE2 . GLU A 205  ? 0.5355 0.6643 0.5079 -0.0141 -0.0064 -0.0085 203  GLU A OE2 
1333  N N   . ALA A 206  ? 0.3231 0.4289 0.3086 -0.0167 -0.0092 0.0021  204  ALA A N   
1334  C CA  . ALA A 206  ? 0.3565 0.4488 0.3478 -0.0162 -0.0099 -0.0016 204  ALA A CA  
1335  C C   . ALA A 206  ? 0.3561 0.4513 0.3526 -0.0168 -0.0123 -0.0041 204  ALA A C   
1336  O O   . ALA A 206  ? 0.3071 0.3993 0.3092 -0.0163 -0.0146 -0.0115 204  ALA A O   
1337  C CB  . ALA A 206  ? 0.3145 0.3916 0.3056 -0.0164 -0.0071 0.0058  204  ALA A CB  
1338  N N   . LEU A 207  ? 0.3094 0.4106 0.3047 -0.0178 -0.0122 0.0019  205  LEU A N   
1339  C CA  . LEU A 207  ? 0.3338 0.4386 0.3339 -0.0185 -0.0146 -0.0001 205  LEU A CA  
1340  C C   . LEU A 207  ? 0.3851 0.5041 0.3864 -0.0180 -0.0179 -0.0097 205  LEU A C   
1341  O O   . LEU A 207  ? 0.3666 0.4849 0.3741 -0.0180 -0.0206 -0.0158 205  LEU A O   
1342  C CB  . LEU A 207  ? 0.3278 0.4366 0.3263 -0.0195 -0.0138 0.0087  205  LEU A CB  
1343  C CG  . LEU A 207  ? 0.3443 0.4393 0.3439 -0.0198 -0.0112 0.0169  205  LEU A CG  
1344  C CD1 . LEU A 207  ? 0.3111 0.4112 0.3081 -0.0204 -0.0104 0.0258  205  LEU A CD1 
1345  C CD2 . LEU A 207  ? 0.2772 0.3643 0.2838 -0.0202 -0.0120 0.0152  205  LEU A CD2 
1346  N N   . LYS A 208  ? 0.3546 0.4872 0.3503 -0.0175 -0.0179 -0.0113 206  LYS A N   
1347  C CA  . LYS A 208  ? 0.3670 0.5144 0.3636 -0.0166 -0.0210 -0.0214 206  LYS A CA  
1348  C C   . LYS A 208  ? 0.3523 0.4925 0.3545 -0.0151 -0.0228 -0.0318 206  LYS A C   
1349  O O   . LYS A 208  ? 0.3753 0.5206 0.3829 -0.0145 -0.0263 -0.0408 206  LYS A O   
1350  C CB  . LYS A 208  ? 0.3665 0.5305 0.3558 -0.0165 -0.0203 -0.0208 206  LYS A CB  
1351  N N   . ARG A 209  ? 0.3604 0.4885 0.3621 -0.0145 -0.0208 -0.0306 207  ARG A N   
1352  C CA  . ARG A 209  ? 0.3991 0.5199 0.4064 -0.0130 -0.0227 -0.0397 207  ARG A CA  
1353  C C   . ARG A 209  ? 0.4105 0.5166 0.4261 -0.0137 -0.0242 -0.0401 207  ARG A C   
1354  O O   . ARG A 209  ? 0.4203 0.5205 0.4424 -0.0126 -0.0266 -0.0478 207  ARG A O   
1355  C CB  . ARG A 209  ? 0.4047 0.5189 0.4083 -0.0121 -0.0202 -0.0381 207  ARG A CB  
1356  C CG  . ARG A 209  ? 0.4617 0.5916 0.4583 -0.0115 -0.0191 -0.0388 207  ARG A CG  
1357  C CD  . ARG A 209  ? 0.4406 0.5638 0.4337 -0.0108 -0.0165 -0.0363 207  ARG A CD  
1358  N NE  . ARG A 209  ? 0.4889 0.6281 0.4759 -0.0104 -0.0155 -0.0373 207  ARG A NE  
1359  C CZ  . ARG A 209  ? 0.5357 0.6732 0.5187 -0.0101 -0.0131 -0.0345 207  ARG A CZ  
1360  N NH1 . ARG A 209  ? 0.4879 0.6085 0.4720 -0.0100 -0.0115 -0.0308 207  ARG A NH1 
1361  N NH2 . ARG A 209  ? 0.5608 0.7147 0.5386 -0.0101 -0.0124 -0.0353 207  ARG A NH2 
1362  N N   . SER A 210  ? 0.4121 0.5128 0.4284 -0.0154 -0.0230 -0.0321 208  SER A N   
1363  C CA  . SER A 210  ? 0.3821 0.4700 0.4063 -0.0164 -0.0241 -0.0314 208  SER A CA  
1364  C C   . SER A 210  ? 0.3909 0.4851 0.4222 -0.0170 -0.0281 -0.0379 208  SER A C   
1365  O O   . SER A 210  ? 0.3855 0.4701 0.4251 -0.0178 -0.0300 -0.0395 208  SER A O   
1366  C CB  . SER A 210  ? 0.3631 0.4424 0.3851 -0.0178 -0.0207 -0.0201 208  SER A CB  
1367  O OG  . SER A 210  ? 0.3957 0.4680 0.4123 -0.0173 -0.0173 -0.0148 208  SER A OG  
1368  N N   . LYS A 211  ? 0.4197 0.5304 0.4481 -0.0166 -0.0296 -0.0414 209  LYS A N   
1369  C CA  . LYS A 211  ? 0.4138 0.5314 0.4487 -0.0172 -0.0336 -0.0476 209  LYS A CA  
1370  C C   . LYS A 211  ? 0.4284 0.5422 0.4725 -0.0162 -0.0378 -0.0589 209  LYS A C   
1371  O O   . LYS A 211  ? 0.4515 0.5619 0.5045 -0.0173 -0.0409 -0.0620 209  LYS A O   
1372  C CB  . LYS A 211  ? 0.4069 0.5445 0.4362 -0.0168 -0.0346 -0.0497 209  LYS A CB  
1373  N N   . GLU A 212  ? 0.4356 0.5495 0.4786 -0.0142 -0.0381 -0.0650 210  GLU A N   
1374  C CA  . GLU A 212  ? 0.4765 0.5871 0.5291 -0.0129 -0.0425 -0.0764 210  GLU A CA  
1375  C C   . GLU A 212  ? 0.4536 0.5463 0.5159 -0.0145 -0.0437 -0.0735 210  GLU A C   
1376  O O   . GLU A 212  ? 0.4237 0.5150 0.4959 -0.0153 -0.0479 -0.0792 210  GLU A O   
1377  C CB  . GLU A 212  ? 0.4936 0.6055 0.5432 -0.0104 -0.0420 -0.0818 210  GLU A CB  
1378  C CG  . GLU A 212  ? 0.4878 0.5974 0.5480 -0.0085 -0.0471 -0.0946 210  GLU A CG  
1379  C CD  . GLU A 212  ? 0.6097 0.7203 0.6674 -0.0057 -0.0466 -0.1000 210  GLU A CD  
1380  O OE1 . GLU A 212  ? 0.6755 0.7877 0.7235 -0.0057 -0.0422 -0.0931 210  GLU A OE1 
1381  O OE2 . GLU A 212  ? 0.6972 0.8072 0.7634 -0.0036 -0.0509 -0.1113 210  GLU A OE2 
1382  N N   . LEU A 213  ? 0.4279 0.5071 0.4875 -0.0152 -0.0401 -0.0647 211  LEU A N   
1383  C CA  . LEU A 213  ? 0.4444 0.5075 0.5130 -0.0168 -0.0412 -0.0616 211  LEU A CA  
1384  C C   . LEU A 213  ? 0.4198 0.4802 0.4912 -0.0196 -0.0405 -0.0542 211  LEU A C   
1385  O O   . LEU A 213  ? 0.4367 0.4875 0.5178 -0.0213 -0.0426 -0.0535 211  LEU A O   
1386  C CB  . LEU A 213  ? 0.4403 0.4913 0.5053 -0.0165 -0.0378 -0.0553 211  LEU A CB  
1387  C CG  . LEU A 213  ? 0.4012 0.4510 0.4680 -0.0140 -0.0399 -0.0636 211  LEU A CG  
1388  C CD1 . LEU A 213  ? 0.4318 0.4682 0.4970 -0.0138 -0.0373 -0.0575 211  LEU A CD1 
1389  C CD2 . LEU A 213  ? 0.4423 0.4910 0.5219 -0.0135 -0.0460 -0.0742 211  LEU A CD2 
1390  N N   . GLU A 214  ? 0.4057 0.4748 0.4697 -0.0201 -0.0378 -0.0487 212  GLU A N   
1391  C CA  . GLU A 214  ? 0.4250 0.4931 0.4926 -0.0224 -0.0377 -0.0430 212  GLU A CA  
1392  C C   . GLU A 214  ? 0.4389 0.5129 0.5160 -0.0232 -0.0429 -0.0514 212  GLU A C   
1393  O O   . GLU A 214  ? 0.4360 0.5043 0.5213 -0.0254 -0.0443 -0.0490 212  GLU A O   
1394  C CB  . GLU A 214  ? 0.4080 0.4843 0.4662 -0.0226 -0.0341 -0.0355 212  GLU A CB  
1395  C CG  . GLU A 214  ? 0.3764 0.4438 0.4281 -0.0226 -0.0291 -0.0254 212  GLU A CG  
1396  C CD  . GLU A 214  ? 0.4138 0.4885 0.4578 -0.0227 -0.0262 -0.0181 212  GLU A CD  
1397  O OE1 . GLU A 214  ? 0.4072 0.4954 0.4487 -0.0223 -0.0278 -0.0211 212  GLU A OE1 
1398  O OE2 . GLU A 214  ? 0.4179 0.4852 0.4586 -0.0230 -0.0225 -0.0095 212  GLU A OE2 
1399  N N   . GLU A 215  ? 0.4155 0.5017 0.4921 -0.0213 -0.0460 -0.0615 213  GLU A N   
1400  C CA  . GLU A 215  ? 0.4550 0.5472 0.5412 -0.0216 -0.0515 -0.0712 213  GLU A CA  
1401  C C   . GLU A 215  ? 0.4799 0.5595 0.5791 -0.0223 -0.0554 -0.0762 213  GLU A C   
1402  O O   . GLU A 215  ? 0.5568 0.6368 0.6665 -0.0236 -0.0599 -0.0811 213  GLU A O   
1403  C CB  . GLU A 215  ? 0.4769 0.5860 0.5592 -0.0191 -0.0538 -0.0817 213  GLU A CB  
1404  N N   . LYS A 216  ? 0.5100 0.5784 0.6091 -0.0215 -0.0541 -0.0746 214  LYS A N   
1405  C CA  . LYS A 216  ? 0.4948 0.5500 0.6062 -0.0222 -0.0578 -0.0778 214  LYS A CA  
1406  C C   . LYS A 216  ? 0.5015 0.5431 0.6169 -0.0253 -0.0557 -0.0664 214  LYS A C   
1407  O O   . LYS A 216  ? 0.5481 0.5783 0.6741 -0.0265 -0.0586 -0.0669 214  LYS A O   
1408  C CB  . LYS A 216  ? 0.4176 0.4686 0.5275 -0.0195 -0.0579 -0.0824 214  LYS A CB  
1409  N N   . GLY A 217  ? 0.4579 0.5007 0.5656 -0.0267 -0.0509 -0.0561 215  GLY A N   
1410  C CA  . GLY A 217  ? 0.4495 0.4821 0.5611 -0.0296 -0.0488 -0.0458 215  GLY A CA  
1411  C C   . GLY A 217  ? 0.4644 0.4894 0.5673 -0.0294 -0.0432 -0.0358 215  GLY A C   
1412  O O   . GLY A 217  ? 0.4783 0.4956 0.5840 -0.0317 -0.0413 -0.0273 215  GLY A O   
1413  N N   . PHE A 218  ? 0.4004 0.4280 0.4932 -0.0268 -0.0406 -0.0366 216  PHE A N   
1414  C CA  . PHE A 218  ? 0.3768 0.3983 0.4610 -0.0265 -0.0353 -0.0275 216  PHE A CA  
1415  C C   . PHE A 218  ? 0.3520 0.3800 0.4278 -0.0268 -0.0312 -0.0205 216  PHE A C   
1416  O O   . PHE A 218  ? 0.3680 0.4065 0.4429 -0.0268 -0.0324 -0.0229 216  PHE A O   
1417  C CB  . PHE A 218  ? 0.3414 0.3626 0.4190 -0.0238 -0.0344 -0.0311 216  PHE A CB  
1418  C CG  . PHE A 218  ? 0.3822 0.3945 0.4676 -0.0233 -0.0377 -0.0360 216  PHE A CG  
1419  C CD1 . PHE A 218  ? 0.3915 0.4070 0.4853 -0.0224 -0.0432 -0.0470 216  PHE A CD1 
1420  C CD2 . PHE A 218  ? 0.3720 0.3731 0.4565 -0.0235 -0.0356 -0.0299 216  PHE A CD2 
1421  C CE1 . PHE A 218  ? 0.4226 0.4295 0.5244 -0.0217 -0.0466 -0.0515 216  PHE A CE1 
1422  C CE2 . PHE A 218  ? 0.4333 0.4260 0.5251 -0.0229 -0.0389 -0.0339 216  PHE A CE2 
1423  C CZ  . PHE A 218  ? 0.3714 0.3667 0.4723 -0.0220 -0.0445 -0.0446 216  PHE A CZ  
1424  N N   . SER A 219  ? 0.3227 0.3446 0.3927 -0.0269 -0.0267 -0.0117 217  SER A N   
1425  C CA  . SER A 219  ? 0.3142 0.3409 0.3757 -0.0264 -0.0227 -0.0051 217  SER A CA  
1426  C C   . SER A 219  ? 0.3328 0.3561 0.3853 -0.0246 -0.0193 -0.0022 217  SER A C   
1427  O O   . SER A 219  ? 0.3159 0.3335 0.3689 -0.0238 -0.0199 -0.0052 217  SER A O   
1428  C CB  . SER A 219  ? 0.3681 0.3911 0.4330 -0.0284 -0.0207 0.0028  217  SER A CB  
1429  O OG  . SER A 219  ? 0.3685 0.3809 0.4345 -0.0290 -0.0187 0.0077  217  SER A OG  
1430  N N   . TYR A 220  ? 0.3090 0.3359 0.3538 -0.0239 -0.0158 0.0035  218  TYR A N   
1431  C CA  . TYR A 220  ? 0.3115 0.3366 0.3479 -0.0223 -0.0129 0.0058  218  TYR A CA  
1432  C C   . TYR A 220  ? 0.3529 0.3739 0.3851 -0.0222 -0.0089 0.0145  218  TYR A C   
1433  O O   . TYR A 220  ? 0.3273 0.3514 0.3608 -0.0230 -0.0081 0.0184  218  TYR A O   
1434  C CB  . TYR A 220  ? 0.3206 0.3568 0.3510 -0.0210 -0.0135 0.0023  218  TYR A CB  
1435  C CG  . TYR A 220  ? 0.3357 0.3753 0.3677 -0.0200 -0.0165 -0.0068 218  TYR A CG  
1436  C CD1 . TYR A 220  ? 0.3411 0.3868 0.3795 -0.0204 -0.0206 -0.0142 218  TYR A CD1 
1437  C CD2 . TYR A 220  ? 0.3045 0.3415 0.3321 -0.0186 -0.0155 -0.0085 218  TYR A CD2 
1438  C CE1 . TYR A 220  ? 0.3804 0.4296 0.4210 -0.0191 -0.0237 -0.0235 218  TYR A CE1 
1439  C CE2 . TYR A 220  ? 0.3696 0.4102 0.3992 -0.0173 -0.0183 -0.0173 218  TYR A CE2 
1440  C CZ  . TYR A 220  ? 0.3670 0.4138 0.4032 -0.0175 -0.0224 -0.0250 218  TYR A CZ  
1441  O OH  . TYR A 220  ? 0.3628 0.4135 0.4015 -0.0159 -0.0254 -0.0346 218  TYR A OH  
1442  N N   . SER A 221  ? 0.3358 0.3501 0.3636 -0.0212 -0.0064 0.0171  219  SER A N   
1443  C CA  . SER A 221  ? 0.3012 0.3128 0.3238 -0.0205 -0.0027 0.0240  219  SER A CA  
1444  C C   . SER A 221  ? 0.3410 0.3529 0.3564 -0.0190 -0.0014 0.0235  219  SER A C   
1445  O O   . SER A 221  ? 0.3549 0.3625 0.3697 -0.0184 -0.0019 0.0203  219  SER A O   
1446  C CB  . SER A 221  ? 0.3377 0.3400 0.3627 -0.0210 -0.0007 0.0282  219  SER A CB  
1447  O OG  . SER A 221  ? 0.3706 0.3710 0.3907 -0.0200 0.0027  0.0338  219  SER A OG  
1448  N N   . TYR A 222  ? 0.2997 0.3167 0.3104 -0.0184 -0.0001 0.0269  220  TYR A N   
1449  C CA  . TYR A 222  ? 0.3082 0.3276 0.3128 -0.0174 0.0006  0.0265  220  TYR A CA  
1450  C C   . TYR A 222  ? 0.3556 0.3674 0.3566 -0.0165 0.0036  0.0315  220  TYR A C   
1451  O O   . TYR A 222  ? 0.3117 0.3214 0.3131 -0.0163 0.0053  0.0365  220  TYR A O   
1452  C CB  . TYR A 222  ? 0.2885 0.3190 0.2905 -0.0175 -0.0002 0.0276  220  TYR A CB  
1453  C CG  . TYR A 222  ? 0.2825 0.3217 0.2876 -0.0182 -0.0033 0.0217  220  TYR A CG  
1454  C CD1 . TYR A 222  ? 0.3156 0.3593 0.3196 -0.0177 -0.0051 0.0150  220  TYR A CD1 
1455  C CD2 . TYR A 222  ? 0.2802 0.3231 0.2895 -0.0191 -0.0047 0.0223  220  TYR A CD2 
1456  C CE1 . TYR A 222  ? 0.3122 0.3645 0.3195 -0.0180 -0.0082 0.0086  220  TYR A CE1 
1457  C CE2 . TYR A 222  ? 0.2864 0.3374 0.2990 -0.0196 -0.0078 0.0163  220  TYR A CE2 
1458  C CZ  . TYR A 222  ? 0.3074 0.3631 0.3189 -0.0190 -0.0096 0.0093  220  TYR A CZ  
1459  O OH  . TYR A 222  ? 0.3330 0.3974 0.3481 -0.0193 -0.0130 0.0024  220  TYR A OH  
1460  N N   . ASP A 223  ? 0.3447 0.3530 0.3427 -0.0157 0.0041  0.0295  221  ASP A N   
1461  C CA  . ASP A 223  ? 0.3882 0.3894 0.3827 -0.0148 0.0066  0.0331  221  ASP A CA  
1462  C C   . ASP A 223  ? 0.4122 0.4182 0.4018 -0.0143 0.0070  0.0341  221  ASP A C   
1463  O O   . ASP A 223  ? 0.3773 0.3869 0.3649 -0.0142 0.0060  0.0302  221  ASP A O   
1464  C CB  . ASP A 223  ? 0.4056 0.3992 0.4007 -0.0144 0.0067  0.0304  221  ASP A CB  
1465  C CG  . ASP A 223  ? 0.4884 0.4758 0.4795 -0.0133 0.0089  0.0330  221  ASP A CG  
1466  O OD1 . ASP A 223  ? 0.4781 0.4654 0.4667 -0.0128 0.0106  0.0371  221  ASP A OD1 
1467  O OD2 . ASP A 223  ? 0.5421 0.5246 0.5329 -0.0128 0.0087  0.0307  221  ASP A OD2 
1468  N N   . MET A 224  ? 0.3862 0.3927 0.3745 -0.0142 0.0083  0.0394  222  MET A N   
1469  C CA  . MET A 224  ? 0.4587 0.4702 0.4435 -0.0142 0.0083  0.0416  222  MET A CA  
1470  C C   . MET A 224  ? 0.4910 0.4966 0.4726 -0.0134 0.0097  0.0419  222  MET A C   
1471  O O   . MET A 224  ? 0.5479 0.5559 0.5272 -0.0136 0.0100  0.0449  222  MET A O   
1472  C CB  . MET A 224  ? 0.4655 0.4795 0.4514 -0.0144 0.0084  0.0474  222  MET A CB  
1473  C CG  . MET A 224  ? 0.4267 0.4476 0.4157 -0.0151 0.0068  0.0471  222  MET A CG  
1474  S SD  . MET A 224  ? 0.4357 0.4690 0.4234 -0.0162 0.0044  0.0421  222  MET A SD  
1475  C CE  . MET A 224  ? 0.4010 0.4407 0.3843 -0.0167 0.0045  0.0463  222  MET A CE  
1476  N N   . LEU A 225  ? 0.4763 0.4746 0.4581 -0.0128 0.0104  0.0391  223  LEU A N   
1477  C CA  . LEU A 225  ? 0.5343 0.5273 0.5132 -0.0120 0.0114  0.0384  223  LEU A CA  
1478  C C   . LEU A 225  ? 0.5811 0.5707 0.5584 -0.0114 0.0129  0.0431  223  LEU A C   
1479  O O   . LEU A 225  ? 0.5979 0.5858 0.5726 -0.0111 0.0133  0.0431  223  LEU A O   
1480  C CB  . LEU A 225  ? 0.4808 0.4798 0.4575 -0.0122 0.0102  0.0345  223  LEU A CB  
1481  C CG  . LEU A 225  ? 0.4812 0.4822 0.4600 -0.0122 0.0084  0.0282  223  LEU A CG  
1482  C CD1 . LEU A 225  ? 0.4588 0.4677 0.4355 -0.0121 0.0073  0.0240  223  LEU A CD1 
1483  C CD2 . LEU A 225  ? 0.4264 0.4177 0.4070 -0.0114 0.0087  0.0265  223  LEU A CD2 
1484  N N   . GLY A 226  ? 0.5599 0.5484 0.5394 -0.0112 0.0134  0.0468  224  GLY A N   
1485  C CA  . GLY A 226  ? 0.5210 0.5049 0.5003 -0.0102 0.0146  0.0504  224  GLY A CA  
1486  C C   . GLY A 226  ? 0.5023 0.4781 0.4813 -0.0089 0.0162  0.0495  224  GLY A C   
1487  O O   . GLY A 226  ? 0.4957 0.4698 0.4761 -0.0088 0.0167  0.0481  224  GLY A O   
1488  N N   . GLU A 227  ? 0.5001 0.4717 0.4776 -0.0079 0.0170  0.0504  225  GLU A N   
1489  C CA  . GLU A 227  ? 0.4832 0.4483 0.4596 -0.0065 0.0185  0.0492  225  GLU A CA  
1490  C C   . GLU A 227  ? 0.5106 0.4722 0.4861 -0.0054 0.0190  0.0502  225  GLU A C   
1491  O O   . GLU A 227  ? 0.4801 0.4430 0.4546 -0.0060 0.0181  0.0507  225  GLU A O   
1492  C CB  . GLU A 227  ? 0.5955 0.5591 0.5698 -0.0069 0.0183  0.0459  225  GLU A CB  
1493  C CG  . GLU A 227  ? 0.6160 0.5741 0.5895 -0.0059 0.0196  0.0452  225  GLU A CG  
1494  C CD  . GLU A 227  ? 0.6379 0.5947 0.6109 -0.0065 0.0188  0.0424  225  GLU A CD  
1495  O OE1 . GLU A 227  ? 0.5912 0.5517 0.5650 -0.0075 0.0172  0.0404  225  GLU A OE1 
1496  O OE2 . GLU A 227  ? 0.6521 0.6046 0.6240 -0.0058 0.0195  0.0422  225  GLU A OE2 
1497  N N   . ALA A 228  ? 0.4759 0.4334 0.4518 -0.0037 0.0203  0.0502  226  ALA A N   
1498  C CA  . ALA A 228  ? 0.4200 0.3734 0.3951 -0.0022 0.0207  0.0498  226  ALA A CA  
1499  C C   . ALA A 228  ? 0.4218 0.3761 0.3991 -0.0025 0.0193  0.0520  226  ALA A C   
1500  O O   . ALA A 228  ? 0.4307 0.3844 0.4066 -0.0032 0.0185  0.0519  226  ALA A O   
1501  C CB  . ALA A 228  ? 0.5363 0.4870 0.5076 -0.0023 0.0210  0.0473  226  ALA A CB  
1502  N N   . ALA A 229  ? 0.3409 0.2967 0.3222 -0.0021 0.0188  0.0543  227  ALA A N   
1503  C CA  . ALA A 229  ? 0.3975 0.3533 0.3823 -0.0022 0.0171  0.0570  227  ALA A CA  
1504  C C   . ALA A 229  ? 0.3817 0.3320 0.3670 -0.0005 0.0171  0.0554  227  ALA A C   
1505  O O   . ALA A 229  ? 0.3705 0.3179 0.3555 0.0016  0.0184  0.0527  227  ALA A O   
1506  C CB  . ALA A 229  ? 0.3347 0.2924 0.3245 -0.0014 0.0164  0.0595  227  ALA A CB  
1507  N N   . THR A 230  ? 0.3563 0.3059 0.3426 -0.0016 0.0155  0.0570  228  THR A N   
1508  C CA  . THR A 230  ? 0.4239 0.3685 0.4116 -0.0004 0.0149  0.0555  228  THR A CA  
1509  C C   . THR A 230  ? 0.3720 0.3147 0.3668 0.0005  0.0128  0.0578  228  THR A C   
1510  O O   . THR A 230  ? 0.3284 0.2665 0.3259 0.0026  0.0123  0.0554  228  THR A O   
1511  C CB  . THR A 230  ? 0.4516 0.3964 0.4364 -0.0022 0.0143  0.0555  228  THR A CB  
1512  O OG1 . THR A 230  ? 0.4847 0.4312 0.4638 -0.0027 0.0160  0.0530  228  THR A OG1 
1513  C CG2 . THR A 230  ? 0.4306 0.3702 0.4169 -0.0010 0.0137  0.0534  228  THR A CG2 
1514  N N   . THR A 231  ? 0.3408 0.2870 0.3392 -0.0010 0.0112  0.0624  229  THR A N   
1515  C CA  . THR A 231  ? 0.3151 0.2594 0.3213 -0.0005 0.0086  0.0655  229  THR A CA  
1516  C C   . THR A 231  ? 0.2954 0.2430 0.3048 0.0000  0.0082  0.0681  229  THR A C   
1517  O O   . THR A 231  ? 0.3121 0.2644 0.3177 -0.0009 0.0096  0.0682  229  THR A O   
1518  C CB  . THR A 231  ? 0.3436 0.2891 0.3522 -0.0033 0.0061  0.0704  229  THR A CB  
1519  O OG1 . THR A 231  ? 0.3524 0.3053 0.3590 -0.0060 0.0060  0.0746  229  THR A OG1 
1520  C CG2 . THR A 231  ? 0.3427 0.2864 0.3472 -0.0043 0.0067  0.0680  229  THR A CG2 
1521  N N   . ALA A 232  ? 0.3247 0.2697 0.3419 0.0016  0.0060  0.0696  230  ALA A N   
1522  C CA  . ALA A 232  ? 0.3244 0.2728 0.3460 0.0019  0.0049  0.0729  230  ALA A CA  
1523  C C   . ALA A 232  ? 0.3597 0.3149 0.3795 -0.0016 0.0039  0.0786  230  ALA A C   
1524  O O   . ALA A 232  ? 0.3743 0.3346 0.3925 -0.0020 0.0047  0.0795  230  ALA A O   
1525  C CB  . ALA A 232  ? 0.3415 0.2858 0.3730 0.0040  0.0018  0.0742  230  ALA A CB  
1526  N N   . ALA A 233  ? 0.3530 0.3090 0.3728 -0.0042 0.0023  0.0822  231  ALA A N   
1527  C CA  . ALA A 233  ? 0.3909 0.3550 0.4088 -0.0076 0.0014  0.0876  231  ALA A CA  
1528  C C   . ALA A 233  ? 0.3812 0.3508 0.3908 -0.0085 0.0041  0.0844  231  ALA A C   
1529  O O   . ALA A 233  ? 0.3686 0.3453 0.3768 -0.0098 0.0039  0.0866  231  ALA A O   
1530  C CB  . ALA A 233  ? 0.3879 0.3530 0.4074 -0.0103 -0.0006 0.0921  231  ALA A CB  
1531  N N   . ASP A 234  ? 0.3353 0.3015 0.3397 -0.0077 0.0064  0.0790  232  ASP A N   
1532  C CA  . ASP A 234  ? 0.3677 0.3379 0.3653 -0.0084 0.0086  0.0755  232  ASP A CA  
1533  C C   . ASP A 234  ? 0.3594 0.3308 0.3573 -0.0070 0.0096  0.0739  232  ASP A C   
1534  O O   . ASP A 234  ? 0.3559 0.3333 0.3511 -0.0083 0.0100  0.0736  232  ASP A O   
1535  C CB  . ASP A 234  ? 0.4246 0.3901 0.4177 -0.0075 0.0105  0.0702  232  ASP A CB  
1536  C CG  . ASP A 234  ? 0.4736 0.4400 0.4647 -0.0093 0.0100  0.0710  232  ASP A CG  
1537  O OD1 . ASP A 234  ? 0.4850 0.4578 0.4768 -0.0117 0.0085  0.0753  232  ASP A OD1 
1538  O OD2 . ASP A 234  ? 0.5723 0.5338 0.5611 -0.0083 0.0110  0.0674  232  ASP A OD2 
1539  N N   . ALA A 235  ? 0.3167 0.2829 0.3180 -0.0044 0.0101  0.0722  233  ALA A N   
1540  C CA  . ALA A 235  ? 0.3352 0.3033 0.3373 -0.0032 0.0112  0.0710  233  ALA A CA  
1541  C C   . ALA A 235  ? 0.3586 0.3327 0.3642 -0.0044 0.0092  0.0755  233  ALA A C   
1542  O O   . ALA A 235  ? 0.3100 0.2888 0.3143 -0.0049 0.0098  0.0750  233  ALA A O   
1543  C CB  . ALA A 235  ? 0.3247 0.2876 0.3302 0.0000  0.0121  0.0684  233  ALA A CB  
1544  N N   . GLU A 236  ? 0.3404 0.3147 0.3507 -0.0048 0.0067  0.0803  234  GLU A N   
1545  C CA  . GLU A 236  ? 0.3569 0.3377 0.3707 -0.0061 0.0045  0.0855  234  GLU A CA  
1546  C C   . GLU A 236  ? 0.3526 0.3418 0.3609 -0.0090 0.0045  0.0865  234  GLU A C   
1547  O O   . GLU A 236  ? 0.3441 0.3397 0.3525 -0.0096 0.0040  0.0875  234  GLU A O   
1548  C CB  . GLU A 236  ? 0.4066 0.3857 0.4269 -0.0064 0.0013  0.0912  234  GLU A CB  
1549  C CG  . GLU A 236  ? 0.5098 0.4833 0.5382 -0.0033 0.0000  0.0912  234  GLU A CG  
1550  C CD  . GLU A 236  ? 0.6170 0.5841 0.6514 -0.0028 -0.0023 0.0932  234  GLU A CD  
1551  O OE1 . GLU A 236  ? 0.6770 0.6458 0.7114 -0.0055 -0.0041 0.0977  234  GLU A OE1 
1552  O OE2 . GLU A 236  ? 0.6506 0.6113 0.6902 0.0005  -0.0026 0.0899  234  GLU A OE2 
1553  N N   . ARG A 237  ? 0.3472 0.3373 0.3512 -0.0106 0.0049  0.0858  235  ARG A N   
1554  C CA  . ARG A 237  ? 0.3793 0.3783 0.3783 -0.0130 0.0051  0.0855  235  ARG A CA  
1555  C C   . ARG A 237  ? 0.3799 0.3802 0.3755 -0.0124 0.0068  0.0800  235  ARG A C   
1556  O O   . ARG A 237  ? 0.3400 0.3484 0.3343 -0.0136 0.0062  0.0801  235  ARG A O   
1557  C CB  . ARG A 237  ? 0.3812 0.3805 0.3765 -0.0144 0.0055  0.0848  235  ARG A CB  
1558  C CG  . ARG A 237  ? 0.4829 0.4897 0.4723 -0.0158 0.0064  0.0813  235  ARG A CG  
1559  C CD  . ARG A 237  ? 0.6034 0.6154 0.5904 -0.0180 0.0059  0.0832  235  ARG A CD  
1560  N NE  . ARG A 237  ? 0.6680 0.6716 0.6562 -0.0174 0.0063  0.0832  235  ARG A NE  
1561  C CZ  . ARG A 237  ? 0.6660 0.6630 0.6515 -0.0160 0.0081  0.0777  235  ARG A CZ  
1562  N NH1 . ARG A 237  ? 0.6084 0.6056 0.5901 -0.0151 0.0096  0.0721  235  ARG A NH1 
1563  N NH2 . ARG A 237  ? 0.6622 0.6523 0.6491 -0.0156 0.0080  0.0781  235  ARG A NH2 
1564  N N   . TYR A 238  ? 0.3265 0.3193 0.3210 -0.0105 0.0089  0.0754  236  TYR A N   
1565  C CA  . TYR A 238  ? 0.3164 0.3098 0.3087 -0.0102 0.0103  0.0709  236  TYR A CA  
1566  C C   . TYR A 238  ? 0.2907 0.2871 0.2867 -0.0097 0.0097  0.0722  236  TYR A C   
1567  O O   . TYR A 238  ? 0.3184 0.3198 0.3134 -0.0106 0.0096  0.0702  236  TYR A O   
1568  C CB  . TYR A 238  ? 0.3204 0.3057 0.3112 -0.0085 0.0124  0.0668  236  TYR A CB  
1569  C CG  . TYR A 238  ? 0.3364 0.3197 0.3229 -0.0091 0.0131  0.0643  236  TYR A CG  
1570  C CD1 . TYR A 238  ? 0.4175 0.4068 0.4008 -0.0108 0.0125  0.0626  236  TYR A CD1 
1571  C CD2 . TYR A 238  ? 0.3733 0.3495 0.3590 -0.0078 0.0141  0.0630  236  TYR A CD2 
1572  C CE1 . TYR A 238  ? 0.4252 0.4132 0.4049 -0.0111 0.0130  0.0601  236  TYR A CE1 
1573  C CE2 . TYR A 238  ? 0.4066 0.3813 0.3886 -0.0083 0.0145  0.0607  236  TYR A CE2 
1574  C CZ  . TYR A 238  ? 0.5132 0.4938 0.4924 -0.0099 0.0140  0.0594  236  TYR A CZ  
1575  O OH  . TYR A 238  ? 0.5104 0.4899 0.4863 -0.0102 0.0144  0.0568  236  TYR A OH  
1576  N N   . TYR A 239  ? 0.2632 0.2569 0.2641 -0.0083 0.0091  0.0753  237  TYR A N   
1577  C CA  . TYR A 239  ? 0.3212 0.3184 0.3262 -0.0077 0.0084  0.0769  237  TYR A CA  
1578  C C   . TYR A 239  ? 0.3327 0.3395 0.3376 -0.0098 0.0062  0.0799  237  TYR A C   
1579  O O   . TYR A 239  ? 0.2855 0.2974 0.2903 -0.0104 0.0061  0.0784  237  TYR A O   
1580  C CB  . TYR A 239  ? 0.3240 0.3170 0.3351 -0.0055 0.0076  0.0795  237  TYR A CB  
1581  C CG  . TYR A 239  ? 0.3167 0.3140 0.3326 -0.0048 0.0067  0.0814  237  TYR A CG  
1582  C CD1 . TYR A 239  ? 0.3348 0.3383 0.3534 -0.0060 0.0039  0.0864  237  TYR A CD1 
1583  C CD2 . TYR A 239  ? 0.3296 0.3255 0.3472 -0.0032 0.0084  0.0784  237  TYR A CD2 
1584  C CE1 . TYR A 239  ? 0.3964 0.4040 0.4194 -0.0053 0.0028  0.0882  237  TYR A CE1 
1585  C CE2 . TYR A 239  ? 0.3180 0.3183 0.3403 -0.0026 0.0075  0.0800  237  TYR A CE2 
1586  C CZ  . TYR A 239  ? 0.3703 0.3762 0.3953 -0.0036 0.0046  0.0847  237  TYR A CZ  
1587  O OH  . TYR A 239  ? 0.3612 0.3718 0.3910 -0.0030 0.0034  0.0865  237  TYR A OH  
1588  N N   . ARG A 240  ? 0.3018 0.3118 0.3067 -0.0111 0.0044  0.0844  238  ARG A N   
1589  C CA  . ARG A 240  ? 0.3299 0.3507 0.3345 -0.0131 0.0023  0.0878  238  ARG A CA  
1590  C C   . ARG A 240  ? 0.2953 0.3226 0.2943 -0.0147 0.0029  0.0833  238  ARG A C   
1591  O O   . ARG A 240  ? 0.3441 0.3804 0.3428 -0.0157 0.0016  0.0835  238  ARG A O   
1592  C CB  . ARG A 240  ? 0.3574 0.3812 0.3638 -0.0145 0.0001  0.0946  238  ARG A CB  
1593  C CG  . ARG A 240  ? 0.3732 0.3963 0.3759 -0.0158 0.0006  0.0944  238  ARG A CG  
1594  C CD  . ARG A 240  ? 0.3803 0.4071 0.3860 -0.0175 -0.0019 0.1023  238  ARG A CD  
1595  N NE  . ARG A 240  ? 0.4160 0.4408 0.4191 -0.0187 -0.0013 0.1022  238  ARG A NE  
1596  C CZ  . ARG A 240  ? 0.4178 0.4335 0.4243 -0.0179 -0.0015 0.1034  238  ARG A CZ  
1597  N NH1 . ARG A 240  ? 0.4095 0.4175 0.4225 -0.0158 -0.0025 0.1050  238  ARG A NH1 
1598  N NH2 . ARG A 240  ? 0.4721 0.4866 0.4758 -0.0190 -0.0007 0.1024  238  ARG A NH2 
1599  N N   . ASP A 241  ? 0.3191 0.3422 0.3142 -0.0146 0.0047  0.0787  239  ASP A N   
1600  C CA  A ASP A 241  ? 0.3422 0.3705 0.3332 -0.0156 0.0050  0.0734  239  ASP A CA  
1601  C CA  B ASP A 241  ? 0.3422 0.3704 0.3332 -0.0156 0.0051  0.0735  239  ASP A CA  
1602  C C   . ASP A 241  ? 0.3442 0.3719 0.3368 -0.0149 0.0054  0.0696  239  ASP A C   
1603  O O   . ASP A 241  ? 0.3354 0.3709 0.3273 -0.0159 0.0043  0.0670  239  ASP A O   
1604  C CB  A ASP A 241  ? 0.3896 0.4126 0.3768 -0.0154 0.0066  0.0695  239  ASP A CB  
1605  C CB  B ASP A 241  ? 0.3895 0.4124 0.3768 -0.0154 0.0066  0.0696  239  ASP A CB  
1606  C CG  A ASP A 241  ? 0.3892 0.4139 0.3749 -0.0164 0.0062  0.0731  239  ASP A CG  
1607  C CG  B ASP A 241  ? 0.3894 0.4183 0.3732 -0.0162 0.0065  0.0641  239  ASP A CG  
1608  O OD1 A ASP A 241  ? 0.3995 0.4323 0.3860 -0.0178 0.0045  0.0782  239  ASP A OD1 
1609  O OD1 B ASP A 241  ? 0.4300 0.4688 0.4116 -0.0176 0.0054  0.0648  239  ASP A OD1 
1610  O OD2 A ASP A 241  ? 0.4397 0.4580 0.4237 -0.0158 0.0075  0.0712  239  ASP A OD2 
1611  O OD2 B ASP A 241  ? 0.4523 0.4762 0.4360 -0.0154 0.0074  0.0590  239  ASP A OD2 
1612  N N   . TYR A 242  ? 0.2951 0.3142 0.2904 -0.0133 0.0069  0.0690  240  TYR A N   
1613  C CA  . TYR A 242  ? 0.2996 0.3184 0.2974 -0.0130 0.0073  0.0662  240  TYR A CA  
1614  C C   . TYR A 242  ? 0.2841 0.3102 0.2854 -0.0134 0.0054  0.0692  240  TYR A C   
1615  O O   . TYR A 242  ? 0.2640 0.2950 0.2663 -0.0142 0.0046  0.0665  240  TYR A O   
1616  C CB  . TYR A 242  ? 0.2523 0.2621 0.2523 -0.0112 0.0094  0.0658  240  TYR A CB  
1617  C CG  . TYR A 242  ? 0.3068 0.3095 0.3038 -0.0108 0.0112  0.0623  240  TYR A CG  
1618  C CD1 . TYR A 242  ? 0.3342 0.3378 0.3286 -0.0119 0.0111  0.0581  240  TYR A CD1 
1619  C CD2 . TYR A 242  ? 0.3178 0.3132 0.3152 -0.0091 0.0129  0.0630  240  TYR A CD2 
1620  C CE1 . TYR A 242  ? 0.3728 0.3698 0.3649 -0.0114 0.0125  0.0554  240  TYR A CE1 
1621  C CE2 . TYR A 242  ? 0.3036 0.2931 0.2981 -0.0086 0.0145  0.0601  240  TYR A CE2 
1622  C CZ  . TYR A 242  ? 0.3404 0.3306 0.3323 -0.0098 0.0143  0.0567  240  TYR A CZ  
1623  O OH  . TYR A 242  ? 0.3144 0.2987 0.3039 -0.0094 0.0156  0.0544  240  TYR A OH  
1624  N N   . GLU A 243  ? 0.2762 0.3026 0.2802 -0.0128 0.0046  0.0746  241  GLU A N   
1625  C CA  . GLU A 243  ? 0.3038 0.3373 0.3115 -0.0130 0.0025  0.0780  241  GLU A CA  
1626  C C   . GLU A 243  ? 0.3204 0.3652 0.3253 -0.0150 0.0006  0.0777  241  GLU A C   
1627  O O   . GLU A 243  ? 0.2707 0.3218 0.2773 -0.0155 -0.0007 0.0765  241  GLU A O   
1628  C CB  . GLU A 243  ? 0.2977 0.3293 0.3091 -0.0120 0.0014  0.0842  241  GLU A CB  
1629  C CG  . GLU A 243  ? 0.3503 0.3878 0.3668 -0.0117 -0.0008 0.0884  241  GLU A CG  
1630  C CD  . GLU A 243  ? 0.3840 0.4205 0.4046 -0.0111 -0.0028 0.0951  241  GLU A CD  
1631  O OE1 . GLU A 243  ? 0.5165 0.5508 0.5351 -0.0118 -0.0030 0.0973  241  GLU A OE1 
1632  O OE2 . GLU A 243  ? 0.4524 0.4902 0.4787 -0.0099 -0.0043 0.0984  241  GLU A OE2 
1633  N N   . SER A 244  ? 0.3060 0.3542 0.3067 -0.0162 0.0002  0.0783  242  SER A N   
1634  C CA  . SER A 244  ? 0.2952 0.3561 0.2931 -0.0179 -0.0016 0.0778  242  SER A CA  
1635  C C   . SER A 244  ? 0.2979 0.3612 0.2940 -0.0183 -0.0014 0.0700  242  SER A C   
1636  O O   . SER A 244  ? 0.3045 0.3780 0.3005 -0.0192 -0.0032 0.0682  242  SER A O   
1637  C CB  . SER A 244  ? 0.3226 0.3877 0.3167 -0.0192 -0.0020 0.0807  242  SER A CB  
1638  O OG  . SER A 244  ? 0.3819 0.4423 0.3725 -0.0190 -0.0002 0.0754  242  SER A OG  
1639  N N   . ALA A 245  ? 0.2712 0.3255 0.2664 -0.0175 0.0006  0.0652  243  ALA A N   
1640  C CA  . ALA A 245  ? 0.2888 0.3440 0.2840 -0.0178 0.0003  0.0581  243  ALA A CA  
1641  C C   . ALA A 245  ? 0.2627 0.3181 0.2627 -0.0177 -0.0004 0.0574  243  ALA A C   
1642  O O   . ALA A 245  ? 0.2634 0.3252 0.2645 -0.0185 -0.0020 0.0530  243  ALA A O   
1643  C CB  . ALA A 245  ? 0.2931 0.3381 0.2870 -0.0171 0.0023  0.0543  243  ALA A CB  
1644  N N   . ILE A 246  ? 0.2583 0.3073 0.2617 -0.0167 0.0008  0.0613  244  ILE A N   
1645  C CA  . ILE A 246  ? 0.2825 0.3324 0.2910 -0.0167 0.0002  0.0609  244  ILE A CA  
1646  C C   . ILE A 246  ? 0.2855 0.3471 0.2951 -0.0176 -0.0025 0.0622  244  ILE A C   
1647  O O   . ILE A 246  ? 0.2899 0.3560 0.3021 -0.0184 -0.0038 0.0586  244  ILE A O   
1648  C CB  . ILE A 246  ? 0.2486 0.2911 0.2606 -0.0152 0.0020  0.0649  244  ILE A CB  
1649  C CG1 . ILE A 246  ? 0.2666 0.2988 0.2777 -0.0144 0.0046  0.0626  244  ILE A CG1 
1650  C CG2 . ILE A 246  ? 0.2974 0.3432 0.3149 -0.0152 0.0012  0.0654  244  ILE A CG2 
1651  C CD1 . ILE A 246  ? 0.2963 0.3224 0.3103 -0.0126 0.0064  0.0657  244  ILE A CD1 
1652  N N   . HIS A 247  ? 0.2666 0.3339 0.2746 -0.0177 -0.0036 0.0674  245  HIS A N   
1653  C CA  . HIS A 247  ? 0.3031 0.3831 0.3115 -0.0187 -0.0063 0.0690  245  HIS A CA  
1654  C C   . HIS A 247  ? 0.2891 0.3776 0.2946 -0.0199 -0.0077 0.0624  245  HIS A C   
1655  O O   . HIS A 247  ? 0.3364 0.4323 0.3442 -0.0204 -0.0096 0.0597  245  HIS A O   
1656  C CB  . HIS A 247  ? 0.2927 0.3775 0.2995 -0.0189 -0.0074 0.0763  245  HIS A CB  
1657  C CG  . HIS A 247  ? 0.2644 0.3432 0.2758 -0.0176 -0.0073 0.0827  245  HIS A CG  
1658  N ND1 . HIS A 247  ? 0.3021 0.3829 0.3188 -0.0169 -0.0084 0.0847  245  HIS A ND1 
1659  C CD2 . HIS A 247  ? 0.2808 0.3521 0.2930 -0.0167 -0.0064 0.0872  245  HIS A CD2 
1660  C CE1 . HIS A 247  ? 0.3056 0.3803 0.3262 -0.0154 -0.0083 0.0899  245  HIS A CE1 
1661  N NE2 . HIS A 247  ? 0.2821 0.3508 0.3002 -0.0153 -0.0071 0.0914  245  HIS A NE2 
1662  N N   . ALA A 248  ? 0.2796 0.3675 0.2806 -0.0201 -0.0069 0.0594  246  ALA A N   
1663  C CA  . ALA A 248  ? 0.2933 0.3903 0.2919 -0.0208 -0.0084 0.0525  246  ALA A CA  
1664  C C   . ALA A 248  ? 0.3043 0.3973 0.3068 -0.0207 -0.0088 0.0452  246  ALA A C   
1665  O O   . ALA A 248  ? 0.2869 0.3890 0.2907 -0.0213 -0.0112 0.0403  246  ALA A O   
1666  C CB  . ALA A 248  ? 0.3380 0.4348 0.3317 -0.0208 -0.0072 0.0505  246  ALA A CB  
1667  N N   . ILE A 249  ? 0.2701 0.3499 0.2749 -0.0201 -0.0068 0.0446  247  ILE A N   
1668  C CA  . ILE A 249  ? 0.2727 0.3479 0.2822 -0.0204 -0.0074 0.0391  247  ILE A CA  
1669  C C   . ILE A 249  ? 0.2855 0.3644 0.3002 -0.0210 -0.0088 0.0405  247  ILE A C   
1670  O O   . ILE A 249  ? 0.3008 0.3835 0.3193 -0.0218 -0.0109 0.0351  247  ILE A O   
1671  C CB  . ILE A 249  ? 0.2288 0.2900 0.2392 -0.0198 -0.0047 0.0396  247  ILE A CB  
1672  C CG1 . ILE A 249  ? 0.2414 0.2995 0.2470 -0.0193 -0.0037 0.0373  247  ILE A CG1 
1673  C CG2 . ILE A 249  ? 0.2328 0.2893 0.2491 -0.0205 -0.0054 0.0353  247  ILE A CG2 
1674  C CD1 . ILE A 249  ? 0.2197 0.2649 0.2246 -0.0184 -0.0007 0.0401  247  ILE A CD1 
1675  N N   . GLY A 250  ? 0.2790 0.3570 0.2948 -0.0205 -0.0078 0.0473  248  GLY A N   
1676  C CA  . GLY A 250  ? 0.2820 0.3638 0.3030 -0.0208 -0.0091 0.0489  248  GLY A CA  
1677  C C   . GLY A 250  ? 0.2950 0.3909 0.3157 -0.0216 -0.0124 0.0473  248  GLY A C   
1678  O O   . GLY A 250  ? 0.2974 0.3976 0.3227 -0.0224 -0.0143 0.0443  248  GLY A O   
1679  N N   . LYS A 251  ? 0.2864 0.3902 0.3018 -0.0216 -0.0131 0.0493  249  LYS A N   
1680  C CA  . LYS A 251  ? 0.3104 0.4294 0.3245 -0.0224 -0.0162 0.0472  249  LYS A CA  
1681  C C   . LYS A 251  ? 0.3296 0.4522 0.3447 -0.0229 -0.0179 0.0374  249  LYS A C   
1682  O O   . LYS A 251  ? 0.3362 0.4677 0.3542 -0.0235 -0.0207 0.0336  249  LYS A O   
1683  C CB  . LYS A 251  ? 0.3303 0.4576 0.3383 -0.0225 -0.0164 0.0513  249  LYS A CB  
1684  C CG  . LYS A 251  ? 0.3526 0.4794 0.3605 -0.0222 -0.0160 0.0614  249  LYS A CG  
1685  C CD  . LYS A 251  ? 0.3669 0.5020 0.3691 -0.0228 -0.0162 0.0652  249  LYS A CD  
1686  C CE  . LYS A 251  ? 0.3615 0.4933 0.3643 -0.0227 -0.0158 0.0753  249  LYS A CE  
1687  N NZ  . LYS A 251  ? 0.3261 0.4644 0.3235 -0.0237 -0.0158 0.0788  249  LYS A NZ  
1688  N N   . ALA A 252  ? 0.3062 0.4221 0.3193 -0.0226 -0.0166 0.0329  250  ALA A N   
1689  C CA  . ALA A 252  ? 0.3319 0.4502 0.3469 -0.0228 -0.0185 0.0231  250  ALA A CA  
1690  C C   . ALA A 252  ? 0.3159 0.4274 0.3387 -0.0234 -0.0195 0.0200  250  ALA A C   
1691  O O   . ALA A 252  ? 0.3673 0.4850 0.3940 -0.0240 -0.0225 0.0129  250  ALA A O   
1692  C CB  . ALA A 252  ? 0.2980 0.4096 0.3098 -0.0221 -0.0169 0.0197  250  ALA A CB  
1693  N N   . SER A 253  ? 0.2999 0.3994 0.3254 -0.0234 -0.0171 0.0249  251  SER A N   
1694  C CA  . SER A 253  ? 0.3342 0.4277 0.3674 -0.0244 -0.0177 0.0231  251  SER A CA  
1695  C C   . SER A 253  ? 0.3319 0.4354 0.3695 -0.0252 -0.0206 0.0219  251  SER A C   
1696  O O   . SER A 253  ? 0.2921 0.3962 0.3360 -0.0263 -0.0231 0.0163  251  SER A O   
1697  C CB  . SER A 253  ? 0.2974 0.3796 0.3320 -0.0241 -0.0143 0.0297  251  SER A CB  
1698  O OG  . SER A 253  ? 0.3016 0.3787 0.3436 -0.0253 -0.0147 0.0286  251  SER A OG  
1699  N N   . ALA A 254  ? 0.2783 0.3900 0.3132 -0.0248 -0.0207 0.0274  252  ALA A N   
1700  C CA  . ALA A 254  ? 0.3233 0.4466 0.3612 -0.0255 -0.0238 0.0268  252  ALA A CA  
1701  C C   . ALA A 254  ? 0.3501 0.4692 0.3967 -0.0266 -0.0245 0.0260  252  ALA A C   
1702  O O   . ALA A 254  ? 0.2915 0.4177 0.3428 -0.0276 -0.0277 0.0209  252  ALA A O   
1703  C CB  . ALA A 254  ? 0.3662 0.5021 0.4022 -0.0257 -0.0271 0.0191  252  ALA A CB  
1704  N N   . GLY A 255  ? 0.3393 0.4474 0.3882 -0.0264 -0.0215 0.0310  253  GLY A N   
1705  C CA  . GLY A 255  ? 0.3379 0.4427 0.3950 -0.0276 -0.0217 0.0313  253  GLY A CA  
1706  C C   . GLY A 255  ? 0.3686 0.4668 0.4314 -0.0292 -0.0226 0.0256  253  GLY A C   
1707  O O   . GLY A 255  ? 0.3514 0.4491 0.4220 -0.0307 -0.0235 0.0254  253  GLY A O   
1708  N N   . ARG A 256  ? 0.3102 0.4033 0.3703 -0.0290 -0.0225 0.0213  254  ARG A N   
1709  C CA  . ARG A 256  ? 0.3005 0.3862 0.3672 -0.0305 -0.0236 0.0165  254  ARG A CA  
1710  C C   . ARG A 256  ? 0.3508 0.4255 0.4207 -0.0312 -0.0204 0.0220  254  ARG A C   
1711  O O   . ARG A 256  ? 0.3379 0.4068 0.4147 -0.0330 -0.0215 0.0197  254  ARG A O   
1712  C CB  . ARG A 256  ? 0.3151 0.3985 0.3785 -0.0298 -0.0246 0.0103  254  ARG A CB  
1713  C CG  . ARG A 256  ? 0.3581 0.4525 0.4219 -0.0296 -0.0289 0.0017  254  ARG A CG  
1714  C CD  . ARG A 256  ? 0.3794 0.4722 0.4392 -0.0284 -0.0293 -0.0042 254  ARG A CD  
1715  N NE  . ARG A 256  ? 0.3378 0.4342 0.3876 -0.0267 -0.0267 -0.0005 254  ARG A NE  
1716  C CZ  . ARG A 256  ? 0.3668 0.4624 0.4117 -0.0255 -0.0262 -0.0039 254  ARG A CZ  
1717  N NH1 . ARG A 256  ? 0.4169 0.5072 0.4658 -0.0254 -0.0280 -0.0109 254  ARG A NH1 
1718  N NH2 . ARG A 256  ? 0.3464 0.4468 0.3827 -0.0244 -0.0241 0.0000  254  ARG A NH2 
1719  N N   . GLY A 257  ? 0.3155 0.3875 0.3810 -0.0299 -0.0167 0.0290  255  GLY A N   
1720  C CA  . GLY A 257  ? 0.3055 0.3691 0.3739 -0.0304 -0.0136 0.0339  255  GLY A CA  
1721  C C   . GLY A 257  ? 0.3338 0.3875 0.3987 -0.0299 -0.0115 0.0339  255  GLY A C   
1722  O O   . GLY A 257  ? 0.3132 0.3658 0.3740 -0.0293 -0.0124 0.0298  255  GLY A O   
1723  N N   . ILE A 258  ? 0.2903 0.3375 0.3571 -0.0303 -0.0085 0.0386  256  ILE A N   
1724  C CA  . ILE A 258  ? 0.2956 0.3341 0.3579 -0.0294 -0.0059 0.0399  256  ILE A CA  
1725  C C   . ILE A 258  ? 0.3342 0.3666 0.4004 -0.0311 -0.0078 0.0361  256  ILE A C   
1726  O O   . ILE A 258  ? 0.2908 0.3166 0.3530 -0.0303 -0.0064 0.0361  256  ILE A O   
1727  C CB  . ILE A 258  ? 0.3045 0.3393 0.3668 -0.0289 -0.0019 0.0462  256  ILE A CB  
1728  C CG1 . ILE A 258  ? 0.2987 0.3333 0.3697 -0.0314 -0.0021 0.0480  256  ILE A CG1 
1729  C CG2 . ILE A 258  ? 0.3011 0.3408 0.3602 -0.0268 -0.0003 0.0497  256  ILE A CG2 
1730  C CD1 . ILE A 258  ? 0.2616 0.2950 0.3327 -0.0308 0.0020  0.0539  256  ILE A CD1 
1731  N N   . TYR A 259  ? 0.3215 0.3558 0.3960 -0.0334 -0.0111 0.0329  257  TYR A N   
1732  C CA  . TYR A 259  ? 0.3086 0.3365 0.3883 -0.0350 -0.0134 0.0295  257  TYR A CA  
1733  C C   . TYR A 259  ? 0.3368 0.3675 0.4164 -0.0344 -0.0174 0.0211  257  TYR A C   
1734  O O   . TYR A 259  ? 0.3742 0.3996 0.4522 -0.0337 -0.0181 0.0179  257  TYR A O   
1735  C CB  . TYR A 259  ? 0.3500 0.3769 0.4404 -0.0381 -0.0148 0.0314  257  TYR A CB  
1736  C CG  . TYR A 259  ? 0.3248 0.3510 0.4157 -0.0387 -0.0108 0.0394  257  TYR A CG  
1737  C CD1 . TYR A 259  ? 0.3336 0.3533 0.4210 -0.0382 -0.0074 0.0440  257  TYR A CD1 
1738  C CD2 . TYR A 259  ? 0.3301 0.3633 0.4252 -0.0396 -0.0104 0.0420  257  TYR A CD2 
1739  C CE1 . TYR A 259  ? 0.3127 0.3334 0.4005 -0.0386 -0.0037 0.0507  257  TYR A CE1 
1740  C CE2 . TYR A 259  ? 0.3191 0.3529 0.4150 -0.0399 -0.0067 0.0487  257  TYR A CE2 
1741  C CZ  . TYR A 259  ? 0.3183 0.3462 0.4104 -0.0393 -0.0033 0.0529  257  TYR A CZ  
1742  O OH  . TYR A 259  ? 0.3256 0.3557 0.4184 -0.0393 0.0005  0.0589  257  TYR A OH  
1743  N N   . GLU A 260  ? 0.2999 0.3397 0.3812 -0.0345 -0.0201 0.0173  258  GLU A N   
1744  C CA  . GLU A 260  ? 0.3462 0.3912 0.4269 -0.0336 -0.0238 0.0088  258  GLU A CA  
1745  C C   . GLU A 260  ? 0.3487 0.3975 0.4184 -0.0310 -0.0219 0.0083  258  GLU A C   
1746  O O   . GLU A 260  ? 0.3930 0.4427 0.4607 -0.0299 -0.0237 0.0022  258  GLU A O   
1747  C CB  . GLU A 260  ? 0.3914 0.4461 0.4775 -0.0347 -0.0274 0.0049  258  GLU A CB  
1748  C CG  . GLU A 260  ? 0.4522 0.5158 0.5358 -0.0333 -0.0308 -0.0038 258  GLU A CG  
1749  C CD  . GLU A 260  ? 0.5154 0.5883 0.6057 -0.0344 -0.0350 -0.0090 258  GLU A CD  
1750  O OE1 . GLU A 260  ? 0.5318 0.6053 0.6280 -0.0363 -0.0351 -0.0051 258  GLU A OE1 
1751  O OE2 . GLU A 260  ? 0.6073 0.6878 0.6972 -0.0334 -0.0384 -0.0175 258  GLU A OE2 
1752  N N   . GLY A 261  ? 0.3470 0.3982 0.4105 -0.0299 -0.0186 0.0148  259  GLY A N   
1753  C CA  . GLY A 261  ? 0.2896 0.3459 0.3439 -0.0279 -0.0173 0.0151  259  GLY A CA  
1754  C C   . GLY A 261  ? 0.3027 0.3508 0.3508 -0.0266 -0.0139 0.0185  259  GLY A C   
1755  O O   . GLY A 261  ? 0.3430 0.3818 0.3932 -0.0271 -0.0120 0.0215  259  GLY A O   
1756  N N   . PRO A 262  ? 0.2890 0.3412 0.3295 -0.0250 -0.0132 0.0182  260  PRO A N   
1757  C CA  . PRO A 262  ? 0.2965 0.3415 0.3312 -0.0238 -0.0104 0.0204  260  PRO A CA  
1758  C C   . PRO A 262  ? 0.3073 0.3477 0.3394 -0.0232 -0.0067 0.0283  260  PRO A C   
1759  O O   . PRO A 262  ? 0.2999 0.3446 0.3331 -0.0232 -0.0063 0.0323  260  PRO A O   
1760  C CB  . PRO A 262  ? 0.3144 0.3676 0.3427 -0.0226 -0.0112 0.0176  260  PRO A CB  
1761  C CG  . PRO A 262  ? 0.2773 0.3421 0.3060 -0.0230 -0.0129 0.0181  260  PRO A CG  
1762  C CD  . PRO A 262  ? 0.3052 0.3697 0.3422 -0.0245 -0.0150 0.0160  260  PRO A CD  
1763  N N   . GLY A 263  ? 0.3036 0.3355 0.3327 -0.0224 -0.0043 0.0302  261  GLY A N   
1764  C CA  . GLY A 263  ? 0.2932 0.3208 0.3196 -0.0214 -0.0009 0.0367  261  GLY A CA  
1765  C C   . GLY A 263  ? 0.2865 0.3104 0.3061 -0.0200 0.0008  0.0375  261  GLY A C   
1766  O O   . GLY A 263  ? 0.2551 0.2812 0.2720 -0.0198 -0.0005 0.0333  261  GLY A O   
1767  N N   . ILE A 264  ? 0.2769 0.2960 0.2943 -0.0188 0.0037  0.0423  262  ILE A N   
1768  C CA  . ILE A 264  ? 0.2803 0.2955 0.2920 -0.0175 0.0053  0.0435  262  ILE A CA  
1769  C C   . ILE A 264  ? 0.3109 0.3172 0.3226 -0.0170 0.0078  0.0452  262  ILE A C   
1770  O O   . ILE A 264  ? 0.2610 0.2654 0.2765 -0.0173 0.0088  0.0473  262  ILE A O   
1771  C CB  . ILE A 264  ? 0.2256 0.2444 0.2345 -0.0165 0.0060  0.0478  262  ILE A CB  
1772  C CG1 . ILE A 264  ? 0.2711 0.2877 0.2746 -0.0157 0.0068  0.0481  262  ILE A CG1 
1773  C CG2 . ILE A 264  ? 0.2471 0.2630 0.2588 -0.0156 0.0079  0.0523  262  ILE A CG2 
1774  C CD1 . ILE A 264  ? 0.3086 0.3291 0.3101 -0.0151 0.0067  0.0525  262  ILE A CD1 
1775  N N   . SER A 265  ? 0.2705 0.2721 0.2779 -0.0162 0.0087  0.0443  263  SER A N   
1776  C CA  . SER A 265  ? 0.3080 0.3019 0.3143 -0.0154 0.0111  0.0461  263  SER A CA  
1777  C C   . SER A 265  ? 0.3033 0.2956 0.3049 -0.0137 0.0127  0.0484  263  SER A C   
1778  O O   . SER A 265  ? 0.3621 0.3570 0.3605 -0.0136 0.0117  0.0475  263  SER A O   
1779  C CB  . SER A 265  ? 0.3238 0.3129 0.3299 -0.0159 0.0104  0.0428  263  SER A CB  
1780  O OG  . SER A 265  ? 0.4268 0.4161 0.4386 -0.0175 0.0086  0.0410  263  SER A OG  
1781  N N   . ILE A 266  ? 0.2976 0.2860 0.2990 -0.0125 0.0149  0.0513  264  ILE A N   
1782  C CA  . ILE A 266  ? 0.3197 0.3059 0.3178 -0.0108 0.0162  0.0531  264  ILE A CA  
1783  C C   . ILE A 266  ? 0.2877 0.2675 0.2838 -0.0098 0.0182  0.0531  264  ILE A C   
1784  O O   . ILE A 266  ? 0.2907 0.2688 0.2886 -0.0102 0.0191  0.0531  264  ILE A O   
1785  C CB  . ILE A 266  ? 0.3099 0.2989 0.3106 -0.0098 0.0165  0.0564  264  ILE A CB  
1786  C CG1 . ILE A 266  ? 0.3132 0.3016 0.3174 -0.0092 0.0182  0.0576  264  ILE A CG1 
1787  C CG2 . ILE A 266  ? 0.3117 0.3078 0.3143 -0.0108 0.0143  0.0570  264  ILE A CG2 
1788  C CD1 . ILE A 266  ? 0.3519 0.3420 0.3587 -0.0073 0.0188  0.0602  264  ILE A CD1 
1789  N N   . LYS A 267  ? 0.3109 0.2879 0.3035 -0.0086 0.0188  0.0532  265  LYS A N   
1790  C CA  . LYS A 267  ? 0.2609 0.2327 0.2513 -0.0072 0.0206  0.0532  265  LYS A CA  
1791  C C   . LYS A 267  ? 0.2814 0.2528 0.2725 -0.0052 0.0217  0.0550  265  LYS A C   
1792  O O   . LYS A 267  ? 0.2831 0.2555 0.2742 -0.0049 0.0206  0.0559  265  LYS A O   
1793  C CB  . LYS A 267  ? 0.3414 0.3099 0.3277 -0.0073 0.0202  0.0511  265  LYS A CB  
1794  C CG  . LYS A 267  ? 0.3989 0.3660 0.3853 -0.0086 0.0194  0.0489  265  LYS A CG  
1795  C CD  . LYS A 267  ? 0.4448 0.4085 0.4276 -0.0083 0.0191  0.0468  265  LYS A CD  
1796  C CE  . LYS A 267  ? 0.4319 0.3939 0.4161 -0.0094 0.0178  0.0445  265  LYS A CE  
1797  N NZ  . LYS A 267  ? 0.4373 0.4038 0.4243 -0.0107 0.0156  0.0422  265  LYS A NZ  
1798  N N   . LEU A 268  ? 0.2524 0.2229 0.2446 -0.0039 0.0236  0.0554  266  LEU A N   
1799  C CA  . LEU A 268  ? 0.2632 0.2337 0.2571 -0.0015 0.0243  0.0562  266  LEU A CA  
1800  C C   . LEU A 268  ? 0.2772 0.2436 0.2683 -0.0003 0.0240  0.0553  266  LEU A C   
1801  O O   . LEU A 268  ? 0.2932 0.2594 0.2866 0.0011  0.0233  0.0560  266  LEU A O   
1802  C CB  . LEU A 268  ? 0.2681 0.2398 0.2633 -0.0002 0.0266  0.0562  266  LEU A CB  
1803  C CG  . LEU A 268  ? 0.2954 0.2719 0.2945 -0.0015 0.0270  0.0576  266  LEU A CG  
1804  C CD1 . LEU A 268  ? 0.2646 0.2434 0.2647 -0.0005 0.0295  0.0580  266  LEU A CD1 
1805  C CD2 . LEU A 268  ? 0.3116 0.2917 0.3150 -0.0012 0.0256  0.0589  266  LEU A CD2 
1806  N N   . SER A 269  ? 0.2851 0.2483 0.2720 -0.0009 0.0242  0.0537  267  SER A N   
1807  C CA  . SER A 269  ? 0.3033 0.2629 0.2880 0.0002  0.0239  0.0527  267  SER A CA  
1808  C C   . SER A 269  ? 0.3295 0.2900 0.3149 -0.0008 0.0218  0.0540  267  SER A C   
1809  O O   . SER A 269  ? 0.3259 0.2839 0.3113 0.0000  0.0211  0.0541  267  SER A O   
1810  C CB  . SER A 269  ? 0.3428 0.2992 0.3230 -0.0003 0.0244  0.0509  267  SER A CB  
1811  O OG  . SER A 269  ? 0.3442 0.3013 0.3230 -0.0023 0.0231  0.0505  267  SER A OG  
1812  N N   . ALA A 270  ? 0.2770 0.2415 0.2632 -0.0027 0.0206  0.0551  268  ALA A N   
1813  C CA  . ALA A 270  ? 0.3096 0.2770 0.2966 -0.0038 0.0187  0.0571  268  ALA A CA  
1814  C C   . ALA A 270  ? 0.2950 0.2632 0.2865 -0.0027 0.0178  0.0600  268  ALA A C   
1815  O O   . ALA A 270  ? 0.2765 0.2457 0.2692 -0.0033 0.0161  0.0624  268  ALA A O   
1816  C CB  . ALA A 270  ? 0.3038 0.2766 0.2904 -0.0059 0.0176  0.0570  268  ALA A CB  
1817  N N   . LEU A 271  ? 0.3289 0.2972 0.3236 -0.0012 0.0187  0.0600  269  LEU A N   
1818  C CA  . LEU A 271  ? 0.3039 0.2740 0.3039 -0.0001 0.0175  0.0625  269  LEU A CA  
1819  C C   . LEU A 271  ? 0.3063 0.2722 0.3093 0.0026  0.0176  0.0618  269  LEU A C   
1820  O O   . LEU A 271  ? 0.3018 0.2683 0.3103 0.0039  0.0162  0.0637  269  LEU A O   
1821  C CB  . LEU A 271  ? 0.2682 0.2423 0.2709 0.0000  0.0182  0.0627  269  LEU A CB  
1822  C CG  . LEU A 271  ? 0.2827 0.2618 0.2842 -0.0026 0.0171  0.0636  269  LEU A CG  
1823  C CD1 . LEU A 271  ? 0.3040 0.2870 0.3086 -0.0027 0.0177  0.0637  269  LEU A CD1 
1824  C CD2 . LEU A 271  ? 0.2818 0.2641 0.2846 -0.0035 0.0146  0.0670  269  LEU A CD2 
1825  N N   . HIS A 272  ? 0.2840 0.2457 0.2841 0.0037  0.0189  0.0589  270  HIS A N   
1826  C CA  . HIS A 272  ? 0.2827 0.2406 0.2858 0.0063  0.0186  0.0574  270  HIS A CA  
1827  C C   . HIS A 272  ? 0.3341 0.2879 0.3328 0.0063  0.0192  0.0550  270  HIS A C   
1828  O O   . HIS A 272  ? 0.3189 0.2728 0.3126 0.0056  0.0210  0.0533  270  HIS A O   
1829  C CB  . HIS A 272  ? 0.3055 0.2650 0.3112 0.0091  0.0204  0.0551  270  HIS A CB  
1830  C CG  . HIS A 272  ? 0.3465 0.3034 0.3573 0.0123  0.0194  0.0532  270  HIS A CG  
1831  N ND1 . HIS A 272  ? 0.3758 0.3288 0.3854 0.0138  0.0195  0.0500  270  HIS A ND1 
1832  C CD2 . HIS A 272  ? 0.3643 0.3222 0.3824 0.0144  0.0179  0.0537  270  HIS A CD2 
1833  C CE1 . HIS A 272  ? 0.3856 0.3372 0.4016 0.0167  0.0181  0.0482  270  HIS A CE1 
1834  N NE2 . HIS A 272  ? 0.3820 0.3363 0.4033 0.0172  0.0171  0.0504  270  HIS A NE2 
1835  N N   . PRO A 273  ? 0.2948 0.2449 0.2959 0.0071  0.0175  0.0549  271  PRO A N   
1836  C CA  . PRO A 273  ? 0.2896 0.2361 0.2866 0.0069  0.0179  0.0525  271  PRO A CA  
1837  C C   . PRO A 273  ? 0.3529 0.2978 0.3482 0.0096  0.0197  0.0481  271  PRO A C   
1838  O O   . PRO A 273  ? 0.3350 0.2775 0.3262 0.0095  0.0202  0.0460  271  PRO A O   
1839  C CB  . PRO A 273  ? 0.3289 0.2724 0.3304 0.0067  0.0150  0.0543  271  PRO A CB  
1840  C CG  . PRO A 273  ? 0.3321 0.2759 0.3411 0.0085  0.0136  0.0556  271  PRO A CG  
1841  C CD  . PRO A 273  ? 0.3256 0.2745 0.3337 0.0079  0.0148  0.0572  271  PRO A CD  
1842  N N   . ARG A 274  ? 0.3103 0.2572 0.3086 0.0121  0.0207  0.0465  272  ARG A N   
1843  C CA  . ARG A 274  ? 0.3147 0.2621 0.3110 0.0147  0.0227  0.0422  272  ARG A CA  
1844  C C   . ARG A 274  ? 0.3505 0.3030 0.3451 0.0148  0.0252  0.0424  272  ARG A C   
1845  O O   . ARG A 274  ? 0.3187 0.2745 0.3161 0.0174  0.0263  0.0404  272  ARG A O   
1846  C CB  . ARG A 274  ? 0.2999 0.2458 0.3021 0.0181  0.0214  0.0390  272  ARG A CB  
1847  C CG  . ARG A 274  ? 0.3120 0.2524 0.3171 0.0179  0.0184  0.0388  272  ARG A CG  
1848  C CD  . ARG A 274  ? 0.3546 0.2926 0.3535 0.0169  0.0191  0.0370  272  ARG A CD  
1849  N NE  . ARG A 274  ? 0.3339 0.2741 0.3287 0.0191  0.0214  0.0326  272  ARG A NE  
1850  C CZ  . ARG A 274  ? 0.3423 0.2821 0.3393 0.0223  0.0210  0.0277  272  ARG A CZ  
1851  N NH1 . ARG A 274  ? 0.3314 0.2676 0.3354 0.0238  0.0181  0.0261  272  ARG A NH1 
1852  N NH2 . ARG A 274  ? 0.3142 0.2576 0.3065 0.0240  0.0233  0.0243  272  ARG A NH2 
1853  N N   . TYR A 275  ? 0.2955 0.2492 0.2862 0.0120  0.0260  0.0449  273  TYR A N   
1854  C CA  . TYR A 275  ? 0.2949 0.2532 0.2849 0.0114  0.0281  0.0458  273  TYR A CA  
1855  C C   . TYR A 275  ? 0.2941 0.2534 0.2795 0.0121  0.0302  0.0440  273  TYR A C   
1856  O O   . TYR A 275  ? 0.3167 0.2743 0.2977 0.0102  0.0304  0.0447  273  TYR A O   
1857  C CB  . TYR A 275  ? 0.3305 0.2896 0.3196 0.0082  0.0275  0.0489  273  TYR A CB  
1858  C CG  . TYR A 275  ? 0.2810 0.2440 0.2696 0.0071  0.0293  0.0501  273  TYR A CG  
1859  C CD1 . TYR A 275  ? 0.3279 0.2957 0.3202 0.0084  0.0305  0.0503  273  TYR A CD1 
1860  C CD2 . TYR A 275  ? 0.3033 0.2655 0.2886 0.0046  0.0294  0.0510  273  TYR A CD2 
1861  C CE1 . TYR A 275  ? 0.3214 0.2933 0.3140 0.0070  0.0320  0.0519  273  TYR A CE1 
1862  C CE2 . TYR A 275  ? 0.3278 0.2933 0.3139 0.0032  0.0306  0.0525  273  TYR A CE2 
1863  C CZ  . TYR A 275  ? 0.3219 0.2924 0.3115 0.0043  0.0320  0.0532  273  TYR A CZ  
1864  O OH  . TYR A 275  ? 0.3451 0.3193 0.3361 0.0026  0.0331  0.0552  273  TYR A OH  
1865  N N   . SER A 276  ? 0.3313 0.2941 0.3179 0.0150  0.0317  0.0415  274  SER A N   
1866  C CA  . SER A 276  ? 0.3247 0.2899 0.3069 0.0158  0.0337  0.0400  274  SER A CA  
1867  C C   . SER A 276  ? 0.3266 0.2988 0.3111 0.0187  0.0356  0.0379  274  SER A C   
1868  O O   . SER A 276  ? 0.3109 0.2844 0.3008 0.0208  0.0349  0.0363  274  SER A O   
1869  C CB  . SER A 276  ? 0.3613 0.3221 0.3403 0.0168  0.0327  0.0371  274  SER A CB  
1870  O OG  . SER A 276  ? 0.3500 0.3107 0.3328 0.0201  0.0318  0.0332  274  SER A OG  
1871  N N   . ARG A 277  ? 0.3066 0.2839 0.2873 0.0187  0.0379  0.0381  275  ARG A N   
1872  C CA  . ARG A 277  ? 0.2921 0.2782 0.2746 0.0214  0.0401  0.0360  275  ARG A CA  
1873  C C   . ARG A 277  ? 0.3318 0.3182 0.3168 0.0257  0.0393  0.0301  275  ARG A C   
1874  O O   . ARG A 277  ? 0.3075 0.2995 0.2970 0.0285  0.0400  0.0274  275  ARG A O   
1875  C CB  . ARG A 277  ? 0.3262 0.3185 0.3037 0.0205  0.0426  0.0378  275  ARG A CB  
1876  C CG  . ARG A 277  ? 0.3166 0.3198 0.2948 0.0235  0.0451  0.0353  275  ARG A CG  
1877  C CD  . ARG A 277  ? 0.3182 0.3272 0.3024 0.0238  0.0461  0.0364  275  ARG A CD  
1878  N NE  . ARG A 277  ? 0.3078 0.3285 0.2929 0.0269  0.0486  0.0335  275  ARG A NE  
1879  C CZ  . ARG A 277  ? 0.3296 0.3531 0.3176 0.0314  0.0483  0.0270  275  ARG A CZ  
1880  N NH1 . ARG A 277  ? 0.3240 0.3389 0.3147 0.0332  0.0455  0.0233  275  ARG A NH1 
1881  N NH2 . ARG A 277  ? 0.3456 0.3813 0.3344 0.0342  0.0509  0.0242  275  ARG A NH2 
1882  N N   . ALA A 278  ? 0.3188 0.2993 0.3013 0.0262  0.0377  0.0276  276  ALA A N   
1883  C CA  . ALA A 278  ? 0.3611 0.3409 0.3466 0.0301  0.0364  0.0215  276  ALA A CA  
1884  C C   . ALA A 278  ? 0.3303 0.3069 0.3238 0.0314  0.0341  0.0207  276  ALA A C   
1885  O O   . ALA A 278  ? 0.3206 0.2991 0.3192 0.0352  0.0333  0.0156  276  ALA A O   
1886  C CB  . ALA A 278  ? 0.3230 0.2963 0.3050 0.0297  0.0346  0.0199  276  ALA A CB  
1887  N N   . GLN A 279  ? 0.3148 0.2867 0.3100 0.0284  0.0328  0.0254  277  GLN A N   
1888  C CA  . GLN A 279  ? 0.3179 0.2869 0.3207 0.0292  0.0304  0.0259  277  GLN A CA  
1889  C C   . GLN A 279  ? 0.3399 0.3141 0.3457 0.0286  0.0316  0.0288  277  GLN A C   
1890  O O   . GLN A 279  ? 0.3523 0.3239 0.3625 0.0275  0.0297  0.0317  277  GLN A O   
1891  C CB  . GLN A 279  ? 0.3085 0.2693 0.3112 0.0264  0.0277  0.0291  277  GLN A CB  
1892  C CG  . GLN A 279  ? 0.3380 0.2936 0.3389 0.0269  0.0262  0.0262  277  GLN A CG  
1893  C CD  . GLN A 279  ? 0.3917 0.3466 0.3990 0.0310  0.0244  0.0207  277  GLN A CD  
1894  O OE1 . GLN A 279  ? 0.4646 0.4190 0.4794 0.0325  0.0226  0.0206  277  GLN A OE1 
1895  N NE2 . GLN A 279  ? 0.3326 0.2876 0.3373 0.0329  0.0246  0.0159  277  GLN A NE2 
1896  N N   . ALA A 280  ? 0.3548 0.3373 0.3587 0.0294  0.0346  0.0281  278  ALA A N   
1897  C CA  . ALA A 280  ? 0.3453 0.3333 0.3515 0.0281  0.0360  0.0315  278  ALA A CA  
1898  C C   . ALA A 280  ? 0.3331 0.3217 0.3477 0.0305  0.0343  0.0305  278  ALA A C   
1899  O O   . ALA A 280  ? 0.3262 0.3156 0.3436 0.0286  0.0339  0.0343  278  ALA A O   
1900  C CB  . ALA A 280  ? 0.3127 0.3104 0.3162 0.0288  0.0396  0.0309  278  ALA A CB  
1901  N N   . ALA A 281  ? 0.2906 0.2793 0.3100 0.0347  0.0331  0.0252  279  ALA A N   
1902  C CA  . ALA A 281  ? 0.3438 0.3327 0.3723 0.0372  0.0309  0.0240  279  ALA A CA  
1903  C C   . ALA A 281  ? 0.3478 0.3287 0.3793 0.0348  0.0275  0.0286  279  ALA A C   
1904  O O   . ALA A 281  ? 0.3024 0.2846 0.3391 0.0345  0.0264  0.0314  279  ALA A O   
1905  C CB  . ALA A 281  ? 0.3553 0.3448 0.3890 0.0424  0.0296  0.0168  279  ALA A CB  
1906  N N   . ARG A 282  ? 0.2876 0.2610 0.3161 0.0331  0.0257  0.0294  280  ARG A N   
1907  C CA  . ARG A 282  ? 0.3394 0.3066 0.3698 0.0303  0.0227  0.0343  280  ARG A CA  
1908  C C   . ARG A 282  ? 0.3301 0.2996 0.3564 0.0262  0.0240  0.0397  280  ARG A C   
1909  O O   . ARG A 282  ? 0.3228 0.2915 0.3524 0.0246  0.0220  0.0437  280  ARG A O   
1910  C CB  . ARG A 282  ? 0.3136 0.2735 0.3411 0.0290  0.0210  0.0342  280  ARG A CB  
1911  C CG  . ARG A 282  ? 0.3609 0.3171 0.3943 0.0325  0.0186  0.0293  280  ARG A CG  
1912  C CD  . ARG A 282  ? 0.3365 0.2853 0.3683 0.0302  0.0163  0.0309  280  ARG A CD  
1913  N NE  . ARG A 282  ? 0.3407 0.2867 0.3750 0.0271  0.0138  0.0373  280  ARG A NE  
1914  C CZ  . ARG A 282  ? 0.3715 0.3132 0.4037 0.0240  0.0123  0.0407  280  ARG A CZ  
1915  N NH1 . ARG A 282  ? 0.3274 0.2661 0.3551 0.0235  0.0126  0.0383  280  ARG A NH1 
1916  N NH2 . ARG A 282  ? 0.3381 0.2794 0.3725 0.0212  0.0103  0.0468  280  ARG A NH2 
1917  N N   . VAL A 283  ? 0.3007 0.2731 0.3200 0.0245  0.0270  0.0398  281  VAL A N   
1918  C CA  . VAL A 283  ? 0.3188 0.2931 0.3348 0.0208  0.0278  0.0442  281  VAL A CA  
1919  C C   . VAL A 283  ? 0.3199 0.2999 0.3411 0.0212  0.0281  0.0458  281  VAL A C   
1920  O O   . VAL A 283  ? 0.3097 0.2897 0.3326 0.0190  0.0266  0.0494  281  VAL A O   
1921  C CB  . VAL A 283  ? 0.3280 0.3041 0.3369 0.0192  0.0306  0.0439  281  VAL A CB  
1922  C CG1 . VAL A 283  ? 0.3101 0.2894 0.3178 0.0159  0.0316  0.0477  281  VAL A CG1 
1923  C CG2 . VAL A 283  ? 0.3194 0.2893 0.3231 0.0179  0.0298  0.0434  281  VAL A CG2 
1924  N N   . MET A 284  ? 0.2912 0.2771 0.3153 0.0242  0.0300  0.0428  282  MET A N   
1925  C CA  . MET A 284  ? 0.3373 0.3295 0.3668 0.0248  0.0304  0.0440  282  MET A CA  
1926  C C   . MET A 284  ? 0.3254 0.3152 0.3625 0.0264  0.0270  0.0449  282  MET A C   
1927  O O   . MET A 284  ? 0.3254 0.3182 0.3660 0.0253  0.0262  0.0479  282  MET A O   
1928  C CB  . MET A 284  ? 0.3134 0.3136 0.3445 0.0279  0.0333  0.0403  282  MET A CB  
1929  C CG  . MET A 284  ? 0.3169 0.3208 0.3410 0.0260  0.0366  0.0407  282  MET A CG  
1930  S SD  . MET A 284  ? 0.3598 0.3640 0.3805 0.0205  0.0372  0.0467  282  MET A SD  
1931  C CE  . MET A 284  ? 0.3683 0.3814 0.3962 0.0209  0.0380  0.0481  282  MET A CE  
1932  N N   . GLY A 285  ? 0.3454 0.3300 0.3855 0.0288  0.0247  0.0424  283  GLY A N   
1933  C CA  . GLY A 285  ? 0.3247 0.3068 0.3731 0.0304  0.0211  0.0437  283  GLY A CA  
1934  C C   . GLY A 285  ? 0.3546 0.3316 0.4020 0.0268  0.0183  0.0492  283  GLY A C   
1935  O O   . GLY A 285  ? 0.3573 0.3347 0.4106 0.0268  0.0156  0.0525  283  GLY A O   
1936  N N   . GLU A 286  ? 0.3385 0.3118 0.3787 0.0239  0.0187  0.0503  284  GLU A N   
1937  C CA  . GLU A 286  ? 0.3370 0.3065 0.3765 0.0208  0.0160  0.0551  284  GLU A CA  
1938  C C   . GLU A 286  ? 0.3601 0.3319 0.3928 0.0167  0.0173  0.0581  284  GLU A C   
1939  O O   . GLU A 286  ? 0.3686 0.3413 0.4020 0.0144  0.0152  0.0623  284  GLU A O   
1940  C CB  . GLU A 286  ? 0.3470 0.3098 0.3854 0.0209  0.0145  0.0539  284  GLU A CB  
1941  C CG  . GLU A 286  ? 0.3706 0.3302 0.4167 0.0250  0.0125  0.0504  284  GLU A CG  
1942  C CD  . GLU A 286  ? 0.3983 0.3519 0.4425 0.0251  0.0117  0.0480  284  GLU A CD  
1943  O OE1 . GLU A 286  ? 0.3938 0.3447 0.4331 0.0218  0.0112  0.0511  284  GLU A OE1 
1944  O OE2 . GLU A 286  ? 0.3858 0.3379 0.4335 0.0287  0.0115  0.0426  284  GLU A OE2 
1945  N N   . LEU A 287  ? 0.2907 0.2636 0.3171 0.0158  0.0203  0.0560  285  LEU A N   
1946  C CA  . LEU A 287  ? 0.3446 0.3191 0.3656 0.0121  0.0210  0.0581  285  LEU A CA  
1947  C C   . LEU A 287  ? 0.3201 0.3007 0.3435 0.0113  0.0217  0.0596  285  LEU A C   
1948  O O   . LEU A 287  ? 0.3369 0.3196 0.3598 0.0088  0.0204  0.0624  285  LEU A O   
1949  C CB  . LEU A 287  ? 0.2945 0.2672 0.3088 0.0113  0.0234  0.0557  285  LEU A CB  
1950  C CG  . LEU A 287  ? 0.3544 0.3289 0.3640 0.0082  0.0246  0.0568  285  LEU A CG  
1951  C CD1 . LEU A 287  ? 0.3394 0.3144 0.3485 0.0054  0.0225  0.0594  285  LEU A CD1 
1952  C CD2 . LEU A 287  ? 0.3717 0.3428 0.3752 0.0077  0.0261  0.0547  285  LEU A CD2 
1953  N N   . LEU A 288  ? 0.3246 0.3089 0.3510 0.0136  0.0236  0.0577  286  LEU A N   
1954  C CA  . LEU A 288  ? 0.3462 0.3368 0.3756 0.0129  0.0243  0.0590  286  LEU A CA  
1955  C C   . LEU A 288  ? 0.3295 0.3221 0.3637 0.0123  0.0215  0.0622  286  LEU A C   
1956  O O   . LEU A 288  ? 0.3076 0.3036 0.3411 0.0095  0.0211  0.0643  286  LEU A O   
1957  C CB  . LEU A 288  ? 0.3524 0.3475 0.3852 0.0160  0.0267  0.0563  286  LEU A CB  
1958  C CG  . LEU A 288  ? 0.4432 0.4459 0.4804 0.0158  0.0276  0.0574  286  LEU A CG  
1959  C CD1 . LEU A 288  ? 0.3871 0.3918 0.4207 0.0118  0.0287  0.0595  286  LEU A CD1 
1960  C CD2 . LEU A 288  ? 0.4603 0.4682 0.5003 0.0192  0.0302  0.0542  286  LEU A CD2 
1961  N N   . PRO A 289  ? 0.3145 0.3054 0.3540 0.0145  0.0191  0.0629  287  PRO A N   
1962  C CA  . PRO A 289  ? 0.3242 0.3178 0.3683 0.0137  0.0161  0.0668  287  PRO A CA  
1963  C C   . PRO A 289  ? 0.3074 0.3006 0.3470 0.0100  0.0145  0.0700  287  PRO A C   
1964  O O   . PRO A 289  ? 0.3175 0.3154 0.3589 0.0085  0.0129  0.0728  287  PRO A O   
1965  C CB  . PRO A 289  ? 0.3344 0.3247 0.3851 0.0169  0.0136  0.0670  287  PRO A CB  
1966  C CG  . PRO A 289  ? 0.3871 0.3756 0.4384 0.0202  0.0158  0.0619  287  PRO A CG  
1967  C CD  . PRO A 289  ? 0.3159 0.3028 0.3585 0.0181  0.0185  0.0603  287  PRO A CD  
1968  N N   . ARG A 290  ? 0.3265 0.3153 0.3604 0.0086  0.0148  0.0694  288  ARG A N   
1969  C CA  . ARG A 290  ? 0.3250 0.3147 0.3545 0.0053  0.0135  0.0717  288  ARG A CA  
1970  C C   . ARG A 290  ? 0.2949 0.2885 0.3209 0.0029  0.0149  0.0706  288  ARG A C   
1971  O O   . ARG A 290  ? 0.2719 0.2698 0.2973 0.0007  0.0132  0.0725  288  ARG A O   
1972  C CB  . ARG A 290  ? 0.2995 0.2837 0.3242 0.0046  0.0135  0.0708  288  ARG A CB  
1973  C CG  . ARG A 290  ? 0.3626 0.3424 0.3915 0.0068  0.0118  0.0717  288  ARG A CG  
1974  C CD  . ARG A 290  ? 0.3608 0.3355 0.3853 0.0060  0.0119  0.0707  288  ARG A CD  
1975  N NE  . ARG A 290  ? 0.4161 0.3865 0.4459 0.0077  0.0097  0.0719  288  ARG A NE  
1976  C CZ  . ARG A 290  ? 0.4272 0.3922 0.4558 0.0085  0.0098  0.0698  288  ARG A CZ  
1977  N NH1 . ARG A 290  ? 0.3708 0.3340 0.3926 0.0078  0.0122  0.0666  288  ARG A NH1 
1978  N NH2 . ARG A 290  ? 0.4758 0.4368 0.5107 0.0100  0.0072  0.0709  288  ARG A NH2 
1979  N N   . VAL A 291  ? 0.2556 0.2479 0.2794 0.0032  0.0176  0.0676  289  VAL A N   
1980  C CA  . VAL A 291  ? 0.2947 0.2903 0.3168 0.0008  0.0186  0.0668  289  VAL A CA  
1981  C C   . VAL A 291  ? 0.2987 0.3005 0.3262 0.0007  0.0178  0.0683  289  VAL A C   
1982  O O   . VAL A 291  ? 0.2655 0.2711 0.2928 -0.0017 0.0168  0.0687  289  VAL A O   
1983  C CB  . VAL A 291  ? 0.3040 0.2974 0.3236 0.0011  0.0215  0.0643  289  VAL A CB  
1984  C CG1 . VAL A 291  ? 0.3005 0.2968 0.3198 -0.0016 0.0220  0.0641  289  VAL A CG1 
1985  C CG2 . VAL A 291  ? 0.3218 0.3094 0.3361 0.0012  0.0220  0.0628  289  VAL A CG2 
1986  N N   . LYS A 292  ? 0.2604 0.2636 0.2931 0.0034  0.0181  0.0688  290  LYS A N   
1987  C CA  . LYS A 292  ? 0.2509 0.2603 0.2892 0.0036  0.0173  0.0702  290  LYS A CA  
1988  C C   . LYS A 292  ? 0.2751 0.2875 0.3145 0.0022  0.0139  0.0732  290  LYS A C   
1989  O O   . LYS A 292  ? 0.2267 0.2446 0.2678 0.0005  0.0130  0.0740  290  LYS A O   
1990  C CB  . LYS A 292  ? 0.2528 0.2632 0.2970 0.0072  0.0179  0.0697  290  LYS A CB  
1991  C CG  . LYS A 292  ? 0.2666 0.2837 0.3174 0.0077  0.0168  0.0714  290  LYS A CG  
1992  C CD  . LYS A 292  ? 0.2941 0.3127 0.3516 0.0118  0.0170  0.0705  290  LYS A CD  
1993  C CE  . LYS A 292  ? 0.3064 0.3323 0.3705 0.0120  0.0158  0.0722  290  LYS A CE  
1994  N NZ  . LYS A 292  ? 0.3374 0.3663 0.4081 0.0160  0.0169  0.0702  290  LYS A NZ  
1995  N N   . ALA A 293  ? 0.2752 0.2846 0.3138 0.0027  0.0120  0.0751  291  ALA A N   
1996  C CA  . ALA A 293  ? 0.2886 0.3022 0.3280 0.0011  0.0088  0.0787  291  ALA A CA  
1997  C C   . ALA A 293  ? 0.2809 0.2976 0.3149 -0.0022 0.0085  0.0778  291  ALA A C   
1998  O O   . ALA A 293  ? 0.3013 0.3245 0.3363 -0.0037 0.0064  0.0794  291  ALA A O   
1999  C CB  . ALA A 293  ? 0.2970 0.3069 0.3369 0.0020  0.0068  0.0815  291  ALA A CB  
2000  N N   . LEU A 294  ? 0.2689 0.2815 0.2974 -0.0032 0.0102  0.0749  292  LEU A N   
2001  C CA  . LEU A 294  ? 0.2485 0.2640 0.2729 -0.0060 0.0098  0.0731  292  LEU A CA  
2002  C C   . LEU A 294  ? 0.2434 0.2627 0.2705 -0.0071 0.0103  0.0713  292  LEU A C   
2003  O O   . LEU A 294  ? 0.2558 0.2808 0.2831 -0.0089 0.0084  0.0708  292  LEU A O   
2004  C CB  . LEU A 294  ? 0.2176 0.2274 0.2364 -0.0065 0.0113  0.0703  292  LEU A CB  
2005  C CG  . LEU A 294  ? 0.2644 0.2709 0.2806 -0.0060 0.0107  0.0720  292  LEU A CG  
2006  C CD1 . LEU A 294  ? 0.2685 0.2693 0.2795 -0.0063 0.0124  0.0689  292  LEU A CD1 
2007  C CD2 . LEU A 294  ? 0.2554 0.2683 0.2705 -0.0077 0.0080  0.0747  292  LEU A CD2 
2008  N N   . ALA A 295  ? 0.2380 0.2548 0.2675 -0.0059 0.0126  0.0702  293  ALA A N   
2009  C CA  . ALA A 295  ? 0.2701 0.2907 0.3030 -0.0072 0.0131  0.0692  293  ALA A CA  
2010  C C   . ALA A 295  ? 0.2512 0.2789 0.2891 -0.0072 0.0109  0.0712  293  ALA A C   
2011  O O   . ALA A 295  ? 0.2768 0.3093 0.3166 -0.0092 0.0098  0.0702  293  ALA A O   
2012  C CB  . ALA A 295  ? 0.2301 0.2483 0.2649 -0.0059 0.0161  0.0685  293  ALA A CB  
2013  N N   . LEU A 296  ? 0.2508 0.2794 0.2916 -0.0049 0.0101  0.0740  294  LEU A N   
2014  C CA  . LEU A 296  ? 0.2575 0.2930 0.3034 -0.0048 0.0078  0.0763  294  LEU A CA  
2015  C C   . LEU A 296  ? 0.2655 0.3064 0.3090 -0.0072 0.0049  0.0768  294  LEU A C   
2016  O O   . LEU A 296  ? 0.2322 0.2799 0.2788 -0.0083 0.0032  0.0770  294  LEU A O   
2017  C CB  . LEU A 296  ? 0.2484 0.2833 0.2982 -0.0019 0.0068  0.0795  294  LEU A CB  
2018  C CG  . LEU A 296  ? 0.3094 0.3423 0.3640 0.0012  0.0089  0.0786  294  LEU A CG  
2019  C CD1 . LEU A 296  ? 0.3337 0.3639 0.3918 0.0042  0.0074  0.0809  294  LEU A CD1 
2020  C CD2 . LEU A 296  ? 0.3024 0.3420 0.3629 0.0012  0.0090  0.0786  294  LEU A CD2 
2021  N N   . LEU A 297  ? 0.2694 0.3082 0.3074 -0.0080 0.0043  0.0769  295  LEU A N   
2022  C CA  . LEU A 297  ? 0.2688 0.3140 0.3038 -0.0101 0.0018  0.0767  295  LEU A CA  
2023  C C   . LEU A 297  ? 0.2694 0.3162 0.3032 -0.0123 0.0020  0.0719  295  LEU A C   
2024  O O   . LEU A 297  ? 0.2612 0.3155 0.2962 -0.0138 -0.0002 0.0709  295  LEU A O   
2025  C CB  . LEU A 297  ? 0.2955 0.3383 0.3252 -0.0103 0.0014  0.0780  295  LEU A CB  
2026  C CG  . LEU A 297  ? 0.2906 0.3416 0.3169 -0.0122 -0.0012 0.0789  295  LEU A CG  
2027  C CD1 . LEU A 297  ? 0.3319 0.3914 0.3621 -0.0122 -0.0040 0.0831  295  LEU A CD1 
2028  C CD2 . LEU A 297  ? 0.3433 0.3913 0.3653 -0.0122 -0.0010 0.0809  295  LEU A CD2 
2029  N N   . ALA A 298  ? 0.2795 0.3195 0.3116 -0.0125 0.0044  0.0690  296  ALA A N   
2030  C CA  . ALA A 298  ? 0.2780 0.3186 0.3105 -0.0145 0.0042  0.0648  296  ALA A CA  
2031  C C   . ALA A 298  ? 0.2911 0.3364 0.3301 -0.0152 0.0036  0.0648  296  ALA A C   
2032  O O   . ALA A 298  ? 0.2559 0.3056 0.2966 -0.0172 0.0017  0.0620  296  ALA A O   
2033  C CB  . ALA A 298  ? 0.2850 0.3173 0.3155 -0.0145 0.0068  0.0627  296  ALA A CB  
2034  N N   . LYS A 299  ? 0.2315 0.2760 0.2743 -0.0136 0.0051  0.0677  297  LYS A N   
2035  C CA  . LYS A 299  ? 0.2927 0.3426 0.3421 -0.0141 0.0046  0.0681  297  LYS A CA  
2036  C C   . LYS A 299  ? 0.3023 0.3608 0.3533 -0.0148 0.0012  0.0687  297  LYS A C   
2037  O O   . LYS A 299  ? 0.2705 0.3341 0.3252 -0.0167 -0.0004 0.0668  297  LYS A O   
2038  C CB  . LYS A 299  ? 0.2850 0.3339 0.3382 -0.0116 0.0067  0.0709  297  LYS A CB  
2039  C CG  . LYS A 299  ? 0.2692 0.3251 0.3295 -0.0117 0.0058  0.0721  297  LYS A CG  
2040  C CD  . LYS A 299  ? 0.2680 0.3233 0.3322 -0.0089 0.0081  0.0740  297  LYS A CD  
2041  C CE  . LYS A 299  ? 0.3093 0.3725 0.3807 -0.0084 0.0066  0.0757  297  LYS A CE  
2042  N NZ  . LYS A 299  ? 0.3489 0.4124 0.4247 -0.0053 0.0088  0.0768  297  LYS A NZ  
2043  N N   . ASN A 300  ? 0.2446 0.3052 0.2932 -0.0136 -0.0002 0.0716  298  ASN A N   
2044  C CA  . ASN A 300  ? 0.2869 0.3569 0.3371 -0.0142 -0.0036 0.0730  298  ASN A CA  
2045  C C   . ASN A 300  ? 0.2781 0.3533 0.3255 -0.0166 -0.0057 0.0688  298  ASN A C   
2046  O O   . ASN A 300  ? 0.3132 0.3964 0.3637 -0.0177 -0.0081 0.0678  298  ASN A O   
2047  C CB  . ASN A 300  ? 0.3090 0.3805 0.3574 -0.0127 -0.0049 0.0778  298  ASN A CB  
2048  C CG  . ASN A 300  ? 0.3591 0.4407 0.4104 -0.0129 -0.0083 0.0806  298  ASN A CG  
2049  O OD1 . ASN A 300  ? 0.4430 0.5271 0.5004 -0.0118 -0.0087 0.0827  298  ASN A OD1 
2050  N ND2 . ASN A 300  ? 0.3233 0.4118 0.3704 -0.0144 -0.0106 0.0805  298  ASN A ND2 
2051  N N   . TYR A 301  ? 0.2753 0.3462 0.3173 -0.0173 -0.0049 0.0660  299  TYR A N   
2052  C CA  . TYR A 301  ? 0.3111 0.3866 0.3512 -0.0192 -0.0069 0.0608  299  TYR A CA  
2053  C C   . TYR A 301  ? 0.2852 0.3571 0.3292 -0.0207 -0.0065 0.0562  299  TYR A C   
2054  O O   . TYR A 301  ? 0.3104 0.3860 0.3547 -0.0222 -0.0087 0.0511  299  TYR A O   
2055  C CB  . TYR A 301  ? 0.2730 0.3463 0.3061 -0.0192 -0.0065 0.0593  299  TYR A CB  
2056  C CG  . TYR A 301  ? 0.2453 0.3245 0.2745 -0.0186 -0.0077 0.0633  299  TYR A CG  
2057  C CD1 . TYR A 301  ? 0.2752 0.3663 0.3035 -0.0195 -0.0108 0.0631  299  TYR A CD1 
2058  C CD2 . TYR A 301  ? 0.2791 0.3523 0.3055 -0.0173 -0.0060 0.0675  299  TYR A CD2 
2059  C CE1 . TYR A 301  ? 0.2885 0.3860 0.3131 -0.0194 -0.0120 0.0676  299  TYR A CE1 
2060  C CE2 . TYR A 301  ? 0.2924 0.3711 0.3159 -0.0172 -0.0074 0.0720  299  TYR A CE2 
2061  C CZ  . TYR A 301  ? 0.3273 0.4183 0.3498 -0.0183 -0.0103 0.0724  299  TYR A CZ  
2062  O OH  . TYR A 301  ? 0.3351 0.4325 0.3548 -0.0186 -0.0118 0.0778  299  TYR A OH  
2063  N N   . ASP A 302  ? 0.2783 0.3435 0.3256 -0.0203 -0.0039 0.0579  300  ASP A N   
2064  C CA  . ASP A 302  ? 0.3051 0.3665 0.3568 -0.0220 -0.0034 0.0550  300  ASP A CA  
2065  C C   . ASP A 302  ? 0.2804 0.3367 0.3289 -0.0229 -0.0036 0.0505  300  ASP A C   
2066  O O   . ASP A 302  ? 0.2464 0.3044 0.2980 -0.0248 -0.0059 0.0459  300  ASP A O   
2067  C CB  . ASP A 302  ? 0.2951 0.3638 0.3536 -0.0237 -0.0060 0.0533  300  ASP A CB  
2068  C CG  . ASP A 302  ? 0.3217 0.3866 0.3867 -0.0254 -0.0049 0.0528  300  ASP A CG  
2069  O OD1 . ASP A 302  ? 0.3092 0.3680 0.3740 -0.0247 -0.0017 0.0556  300  ASP A OD1 
2070  O OD2 . ASP A 302  ? 0.3636 0.4321 0.4341 -0.0276 -0.0075 0.0496  300  ASP A OD2 
2071  N N   . ILE A 303  ? 0.2812 0.3312 0.3242 -0.0216 -0.0014 0.0517  301  ILE A N   
2072  C CA  . ILE A 303  ? 0.2596 0.3041 0.2997 -0.0222 -0.0013 0.0479  301  ILE A CA  
2073  C C   . ILE A 303  ? 0.2579 0.2932 0.2974 -0.0216 0.0019  0.0501  301  ILE A C   
2074  O O   . ILE A 303  ? 0.2653 0.2990 0.3051 -0.0203 0.0043  0.0542  301  ILE A O   
2075  C CB  . ILE A 303  ? 0.2734 0.3200 0.3066 -0.0213 -0.0021 0.0466  301  ILE A CB  
2076  C CG1 . ILE A 303  ? 0.2625 0.3056 0.2914 -0.0193 0.0004  0.0515  301  ILE A CG1 
2077  C CG2 . ILE A 303  ? 0.2523 0.3100 0.2857 -0.0218 -0.0052 0.0451  301  ILE A CG2 
2078  C CD1 . ILE A 303  ? 0.2368 0.2810 0.2592 -0.0188 0.0000  0.0508  301  ILE A CD1 
2079  N N   . GLY A 304  ? 0.2934 0.3233 0.3323 -0.0225 0.0017  0.0470  302  GLY A N   
2080  C CA  . GLY A 304  ? 0.2756 0.2974 0.3131 -0.0220 0.0046  0.0491  302  GLY A CA  
2081  C C   . GLY A 304  ? 0.2629 0.2817 0.2935 -0.0198 0.0066  0.0509  302  GLY A C   
2082  O O   . GLY A 304  ? 0.2653 0.2863 0.2917 -0.0192 0.0054  0.0493  302  GLY A O   
2083  N N   . LEU A 305  ? 0.2807 0.2952 0.3107 -0.0186 0.0095  0.0542  303  LEU A N   
2084  C CA  . LEU A 305  ? 0.2691 0.2792 0.2934 -0.0166 0.0115  0.0554  303  LEU A CA  
2085  C C   . LEU A 305  ? 0.2647 0.2685 0.2884 -0.0165 0.0137  0.0560  303  LEU A C   
2086  O O   . LEU A 305  ? 0.2644 0.2683 0.2910 -0.0163 0.0157  0.0584  303  LEU A O   
2087  C CB  . LEU A 305  ? 0.2549 0.2674 0.2792 -0.0146 0.0125  0.0588  303  LEU A CB  
2088  C CG  . LEU A 305  ? 0.3446 0.3527 0.3641 -0.0125 0.0139  0.0600  303  LEU A CG  
2089  C CD1 . LEU A 305  ? 0.3074 0.3192 0.3272 -0.0111 0.0128  0.0625  303  LEU A CD1 
2090  C CD2 . LEU A 305  ? 0.3531 0.3568 0.3728 -0.0110 0.0168  0.0611  303  LEU A CD2 
2091  N N   . ASN A 306  ? 0.2742 0.2733 0.2945 -0.0167 0.0134  0.0538  304  ASN A N   
2092  C CA  . ASN A 306  ? 0.2787 0.2720 0.2983 -0.0170 0.0150  0.0543  304  ASN A CA  
2093  C C   . ASN A 306  ? 0.2927 0.2821 0.3068 -0.0148 0.0172  0.0553  304  ASN A C   
2094  O O   . ASN A 306  ? 0.2870 0.2757 0.2970 -0.0138 0.0165  0.0539  304  ASN A O   
2095  C CB  . ASN A 306  ? 0.2913 0.2817 0.3118 -0.0186 0.0128  0.0509  304  ASN A CB  
2096  C CG  . ASN A 306  ? 0.2928 0.2769 0.3123 -0.0187 0.0140  0.0519  304  ASN A CG  
2097  O OD1 . ASN A 306  ? 0.3555 0.3358 0.3703 -0.0176 0.0143  0.0505  304  ASN A OD1 
2098  N ND2 . ASN A 306  ? 0.2978 0.2817 0.3219 -0.0202 0.0147  0.0546  304  ASN A ND2 
2099  N N   . ILE A 307  ? 0.2818 0.2691 0.2958 -0.0140 0.0197  0.0575  305  ILE A N   
2100  C CA  . ILE A 307  ? 0.2997 0.2831 0.3087 -0.0120 0.0216  0.0578  305  ILE A CA  
2101  C C   . ILE A 307  ? 0.2927 0.2711 0.2996 -0.0128 0.0215  0.0569  305  ILE A C   
2102  O O   . ILE A 307  ? 0.2672 0.2451 0.2764 -0.0139 0.0223  0.0587  305  ILE A O   
2103  C CB  . ILE A 307  ? 0.3221 0.3074 0.3321 -0.0103 0.0243  0.0602  305  ILE A CB  
2104  C CG1 . ILE A 307  ? 0.3107 0.3008 0.3237 -0.0092 0.0240  0.0610  305  ILE A CG1 
2105  C CG2 . ILE A 307  ? 0.3353 0.3167 0.3403 -0.0080 0.0260  0.0597  305  ILE A CG2 
2106  C CD1 . ILE A 307  ? 0.3053 0.2982 0.3203 -0.0073 0.0264  0.0625  305  ILE A CD1 
2107  N N   . ASP A 308  ? 0.2916 0.2667 0.2943 -0.0122 0.0206  0.0546  306  ASP A N   
2108  C CA  . ASP A 308  ? 0.3000 0.2703 0.3007 -0.0126 0.0202  0.0535  306  ASP A CA  
2109  C C   . ASP A 308  ? 0.2953 0.2632 0.2934 -0.0114 0.0227  0.0555  306  ASP A C   
2110  O O   . ASP A 308  ? 0.2823 0.2516 0.2787 -0.0095 0.0246  0.0565  306  ASP A O   
2111  C CB  . ASP A 308  ? 0.3368 0.3053 0.3337 -0.0121 0.0188  0.0503  306  ASP A CB  
2112  C CG  . ASP A 308  ? 0.4255 0.3969 0.4248 -0.0134 0.0160  0.0473  306  ASP A CG  
2113  O OD1 . ASP A 308  ? 0.4197 0.3931 0.4240 -0.0150 0.0148  0.0473  306  ASP A OD1 
2114  O OD2 . ASP A 308  ? 0.4656 0.4378 0.4620 -0.0130 0.0149  0.0447  306  ASP A OD2 
2115  N N   . ALA A 309  ? 0.2909 0.2555 0.2889 -0.0123 0.0225  0.0561  307  ALA A N   
2116  C CA  . ALA A 309  ? 0.2851 0.2484 0.2803 -0.0112 0.0247  0.0582  307  ALA A CA  
2117  C C   . ALA A 309  ? 0.3359 0.2949 0.3259 -0.0098 0.0244  0.0560  307  ALA A C   
2118  O O   . ALA A 309  ? 0.2915 0.2477 0.2813 -0.0104 0.0223  0.0536  307  ALA A O   
2119  C CB  . ALA A 309  ? 0.2727 0.2359 0.2714 -0.0133 0.0246  0.0613  307  ALA A CB  
2120  N N   . GLU A 310  ? 0.2791 0.2380 0.2652 -0.0078 0.0265  0.0564  308  GLU A N   
2121  C CA  . GLU A 310  ? 0.2958 0.2509 0.2772 -0.0063 0.0262  0.0542  308  GLU A CA  
2122  C C   . GLU A 310  ? 0.2917 0.2457 0.2702 -0.0056 0.0275  0.0556  308  GLU A C   
2123  O O   . GLU A 310  ? 0.2985 0.2525 0.2789 -0.0071 0.0273  0.0581  308  GLU A O   
2124  C CB  . GLU A 310  ? 0.3144 0.2703 0.2940 -0.0045 0.0267  0.0527  308  GLU A CB  
2125  C CG  . GLU A 310  ? 0.3323 0.2902 0.3145 -0.0055 0.0251  0.0520  308  GLU A CG  
2126  C CD  . GLU A 310  ? 0.3208 0.2792 0.3020 -0.0041 0.0250  0.0513  308  GLU A CD  
2127  O OE1 . GLU A 310  ? 0.3569 0.3129 0.3351 -0.0038 0.0242  0.0498  308  GLU A OE1 
2128  O OE2 . GLU A 310  ? 0.3144 0.2757 0.2981 -0.0034 0.0254  0.0524  308  GLU A OE2 
2129  N N   . GLU A 311  ? 0.3014 0.2548 0.2759 -0.0034 0.0287  0.0543  309  GLU A N   
2130  C CA  . GLU A 311  ? 0.3151 0.2680 0.2864 -0.0027 0.0296  0.0552  309  GLU A CA  
2131  C C   . GLU A 311  ? 0.2923 0.2505 0.2646 -0.0026 0.0318  0.0583  309  GLU A C   
2132  O O   . GLU A 311  ? 0.2916 0.2539 0.2666 -0.0024 0.0329  0.0589  309  GLU A O   
2133  C CB  . GLU A 311  ? 0.3369 0.2881 0.3039 -0.0003 0.0300  0.0524  309  GLU A CB  
2134  C CG  . GLU A 311  ? 0.3374 0.2840 0.3030 -0.0005 0.0280  0.0498  309  GLU A CG  
2135  C CD  . GLU A 311  ? 0.4123 0.3593 0.3796 -0.0004 0.0273  0.0484  309  GLU A CD  
2136  O OE1 . GLU A 311  ? 0.3743 0.3243 0.3446 -0.0006 0.0279  0.0495  309  GLU A OE1 
2137  O OE2 . GLU A 311  ? 0.4369 0.3817 0.4028 -0.0002 0.0261  0.0464  309  GLU A OE2 
2138  N N   . ALA A 312  ? 0.3027 0.2617 0.2730 -0.0029 0.0323  0.0606  310  ALA A N   
2139  C CA  . ALA A 312  ? 0.2878 0.2534 0.2590 -0.0033 0.0344  0.0642  310  ALA A CA  
2140  C C   . ALA A 312  ? 0.3093 0.2805 0.2790 -0.0006 0.0369  0.0623  310  ALA A C   
2141  O O   . ALA A 312  ? 0.3164 0.2942 0.2886 -0.0008 0.0387  0.0643  310  ALA A O   
2142  C CB  . ALA A 312  ? 0.2887 0.2548 0.2575 -0.0039 0.0344  0.0673  310  ALA A CB  
2143  N N   . ASP A 313  ? 0.2987 0.2677 0.2651 0.0021  0.0369  0.0581  311  ASP A N   
2144  C CA  . ASP A 313  ? 0.3055 0.2798 0.2715 0.0050  0.0388  0.0556  311  ASP A CA  
2145  C C   . ASP A 313  ? 0.3119 0.2866 0.2823 0.0056  0.0387  0.0541  311  ASP A C   
2146  O O   . ASP A 313  ? 0.2956 0.2737 0.2668 0.0083  0.0398  0.0514  311  ASP A O   
2147  C CB  . ASP A 313  ? 0.3219 0.2941 0.2837 0.0077  0.0386  0.0515  311  ASP A CB  
2148  C CG  . ASP A 313  ? 0.3696 0.3341 0.3315 0.0078  0.0363  0.0487  311  ASP A CG  
2149  O OD1 . ASP A 313  ? 0.3667 0.3283 0.3315 0.0061  0.0351  0.0496  311  ASP A OD1 
2150  O OD2 . ASP A 313  ? 0.4157 0.3776 0.3747 0.0095  0.0357  0.0457  311  ASP A OD2 
2151  N N   . ARG A 314  ? 0.3057 0.2771 0.2791 0.0033  0.0371  0.0556  312  ARG A N   
2152  C CA  . ARG A 314  ? 0.3112 0.2840 0.2891 0.0034  0.0368  0.0551  312  ARG A CA  
2153  C C   . ARG A 314  ? 0.3023 0.2799 0.2843 0.0013  0.0375  0.0585  312  ARG A C   
2154  O O   . ARG A 314  ? 0.3040 0.2839 0.2899 0.0016  0.0374  0.0584  312  ARG A O   
2155  C CB  . ARG A 314  ? 0.3053 0.2722 0.2837 0.0025  0.0343  0.0539  312  ARG A CB  
2156  C CG  . ARG A 314  ? 0.3129 0.2761 0.2887 0.0046  0.0336  0.0508  312  ARG A CG  
2157  C CD  . ARG A 314  ? 0.3715 0.3295 0.3464 0.0032  0.0313  0.0501  312  ARG A CD  
2158  N NE  . ARG A 314  ? 0.3409 0.2967 0.3158 0.0049  0.0304  0.0480  312  ARG A NE  
2159  C CZ  . ARG A 314  ? 0.3449 0.2972 0.3188 0.0041  0.0286  0.0474  312  ARG A CZ  
2160  N NH1 . ARG A 314  ? 0.3112 0.2621 0.2836 0.0020  0.0276  0.0478  312  ARG A NH1 
2161  N NH2 . ARG A 314  ? 0.3377 0.2885 0.3129 0.0053  0.0277  0.0464  312  ARG A NH2 
2162  N N   . LEU A 315  ? 0.3060 0.2853 0.2879 -0.0008 0.0380  0.0619  313  LEU A N   
2163  C CA  . LEU A 315  ? 0.2939 0.2774 0.2806 -0.0033 0.0383  0.0655  313  LEU A CA  
2164  C C   . LEU A 315  ? 0.3119 0.3035 0.3013 -0.0017 0.0406  0.0656  313  LEU A C   
2165  O O   . LEU A 315  ? 0.2930 0.2867 0.2870 -0.0024 0.0403  0.0660  313  LEU A O   
2166  C CB  . LEU A 315  ? 0.3051 0.2894 0.2917 -0.0058 0.0384  0.0697  313  LEU A CB  
2167  C CG  . LEU A 315  ? 0.3068 0.2922 0.2993 -0.0095 0.0373  0.0738  313  LEU A CG  
2168  C CD1 . LEU A 315  ? 0.3057 0.2906 0.2980 -0.0118 0.0368  0.0782  313  LEU A CD1 
2169  C CD2 . LEU A 315  ? 0.3389 0.3325 0.3358 -0.0100 0.0392  0.0758  313  LEU A CD2 
2170  N N   . GLU A 316  ? 0.2971 0.2944 0.2839 0.0005  0.0430  0.0651  314  GLU A N   
2171  C CA  . GLU A 316  ? 0.3322 0.3389 0.3221 0.0019  0.0454  0.0653  314  GLU A CA  
2172  C C   . GLU A 316  ? 0.3245 0.3304 0.3168 0.0049  0.0449  0.0610  314  GLU A C   
2173  O O   . GLU A 316  ? 0.3143 0.3257 0.3114 0.0052  0.0456  0.0614  314  GLU A O   
2174  C CB  . GLU A 316  ? 0.3228 0.3377 0.3095 0.0035  0.0481  0.0656  314  GLU A CB  
2175  C CG  . GLU A 316  ? 0.3086 0.3256 0.2943 0.0000  0.0485  0.0714  314  GLU A CG  
2176  C CD  . GLU A 316  ? 0.3362 0.3626 0.3183 0.0011  0.0511  0.0727  314  GLU A CD  
2177  O OE1 . GLU A 316  ? 0.3705 0.4062 0.3530 0.0039  0.0535  0.0702  314  GLU A OE1 
2178  O OE2 . GLU A 316  ? 0.3531 0.3783 0.3321 -0.0007 0.0506  0.0762  314  GLU A OE2 
2179  N N   . LEU A 317  ? 0.3182 0.3174 0.3079 0.0068  0.0433  0.0574  315  LEU A N   
2180  C CA  . LEU A 317  ? 0.3305 0.3278 0.3235 0.0091  0.0421  0.0543  315  LEU A CA  
2181  C C   . LEU A 317  ? 0.3316 0.3273 0.3288 0.0068  0.0405  0.0565  315  LEU A C   
2182  O O   . LEU A 317  ? 0.3014 0.3001 0.3032 0.0082  0.0403  0.0558  315  LEU A O   
2183  C CB  . LEU A 317  ? 0.3204 0.3102 0.3103 0.0107  0.0404  0.0511  315  LEU A CB  
2184  C CG  . LEU A 317  ? 0.3419 0.3291 0.3356 0.0130  0.0387  0.0485  315  LEU A CG  
2185  C CD1 . LEU A 317  ? 0.3280 0.3222 0.3262 0.0163  0.0400  0.0462  315  LEU A CD1 
2186  C CD2 . LEU A 317  ? 0.3837 0.3643 0.3748 0.0144  0.0370  0.0457  315  LEU A CD2 
2187  N N   . SER A 318  ? 0.3225 0.3137 0.3186 0.0035  0.0389  0.0587  316  SER A N   
2188  C CA  . SER A 318  ? 0.3025 0.2929 0.3024 0.0013  0.0371  0.0602  316  SER A CA  
2189  C C   . SER A 318  ? 0.3203 0.3180 0.3252 0.0002  0.0384  0.0626  316  SER A C   
2190  O O   . SER A 318  ? 0.2891 0.2883 0.2982 -0.0004 0.0372  0.0631  316  SER A O   
2191  C CB  . SER A 318  ? 0.2745 0.2593 0.2725 -0.0017 0.0352  0.0611  316  SER A CB  
2192  O OG  . SER A 318  ? 0.3253 0.3117 0.3236 -0.0041 0.0359  0.0639  316  SER A OG  
2193  N N   . LEU A 319  ? 0.2626 0.2656 0.2671 -0.0002 0.0407  0.0645  317  LEU A N   
2194  C CA  . LEU A 319  ? 0.2574 0.2688 0.2670 -0.0012 0.0422  0.0671  317  LEU A CA  
2195  C C   . LEU A 319  ? 0.2631 0.2797 0.2759 0.0021  0.0432  0.0647  317  LEU A C   
2196  O O   . LEU A 319  ? 0.2857 0.3075 0.3039 0.0014  0.0433  0.0660  317  LEU A O   
2197  C CB  . LEU A 319  ? 0.2639 0.2812 0.2721 -0.0023 0.0447  0.0700  317  LEU A CB  
2198  C CG  . LEU A 319  ? 0.3429 0.3553 0.3495 -0.0059 0.0434  0.0733  317  LEU A CG  
2199  C CD1 . LEU A 319  ? 0.2992 0.3184 0.3044 -0.0069 0.0458  0.0771  317  LEU A CD1 
2200  C CD2 . LEU A 319  ? 0.2926 0.3033 0.3048 -0.0095 0.0412  0.0756  317  LEU A CD2 
2201  N N   . ASP A 320  ? 0.3431 0.3586 0.3535 0.0058  0.0436  0.0609  318  ASP A N   
2202  C CA  . ASP A 320  ? 0.3380 0.3580 0.3527 0.0094  0.0440  0.0582  318  ASP A CA  
2203  C C   . ASP A 320  ? 0.3217 0.3379 0.3403 0.0092  0.0413  0.0582  318  ASP A C   
2204  O O   . ASP A 320  ? 0.3334 0.3548 0.3575 0.0106  0.0414  0.0579  318  ASP A O   
2205  C CB  . ASP A 320  ? 0.3196 0.3388 0.3317 0.0135  0.0446  0.0537  318  ASP A CB  
2206  C CG  . ASP A 320  ? 0.3831 0.4110 0.3932 0.0149  0.0478  0.0530  318  ASP A CG  
2207  O OD1 . ASP A 320  ? 0.3849 0.4225 0.3987 0.0152  0.0498  0.0540  318  ASP A OD1 
2208  O OD2 . ASP A 320  ? 0.4218 0.4479 0.4266 0.0156  0.0484  0.0515  318  ASP A OD2 
2209  N N   . LEU A 321  ? 0.2947 0.3028 0.3107 0.0075  0.0388  0.0586  319  LEU A N   
2210  C CA  . LEU A 321  ? 0.3082 0.3140 0.3275 0.0068  0.0362  0.0593  319  LEU A CA  
2211  C C   . LEU A 321  ? 0.3006 0.3104 0.3234 0.0036  0.0358  0.0622  319  LEU A C   
2212  O O   . LEU A 321  ? 0.2611 0.2740 0.2888 0.0039  0.0347  0.0628  319  LEU A O   
2213  C CB  . LEU A 321  ? 0.2746 0.2724 0.2901 0.0057  0.0338  0.0589  319  LEU A CB  
2214  C CG  . LEU A 321  ? 0.3201 0.3132 0.3333 0.0086  0.0333  0.0563  319  LEU A CG  
2215  C CD1 . LEU A 321  ? 0.3896 0.3764 0.3971 0.0071  0.0325  0.0560  319  LEU A CD1 
2216  C CD2 . LEU A 321  ? 0.3977 0.3897 0.4152 0.0102  0.0309  0.0563  319  LEU A CD2 
2217  N N   . LEU A 322  ? 0.3008 0.3102 0.3217 0.0004  0.0364  0.0641  320  LEU A N   
2218  C CA  . LEU A 322  ? 0.2944 0.3072 0.3194 -0.0029 0.0358  0.0666  320  LEU A CA  
2219  C C   . LEU A 322  ? 0.2948 0.3165 0.3254 -0.0020 0.0376  0.0677  320  LEU A C   
2220  O O   . LEU A 322  ? 0.2995 0.3246 0.3351 -0.0034 0.0364  0.0689  320  LEU A O   
2221  C CB  . LEU A 322  ? 0.2797 0.2906 0.3029 -0.0061 0.0361  0.0687  320  LEU A CB  
2222  C CG  . LEU A 322  ? 0.2467 0.2607 0.2753 -0.0098 0.0350  0.0712  320  LEU A CG  
2223  C CD1 . LEU A 322  ? 0.2880 0.2982 0.3177 -0.0112 0.0316  0.0698  320  LEU A CD1 
2224  C CD2 . LEU A 322  ? 0.2794 0.2927 0.3079 -0.0128 0.0355  0.0740  320  LEU A CD2 
2225  N N   . GLU A 323  ? 0.2749 0.3014 0.3047 0.0004  0.0404  0.0671  321  GLU A N   
2226  C CA  . GLU A 323  ? 0.3298 0.3663 0.3650 0.0015  0.0425  0.0677  321  GLU A CA  
2227  C C   . GLU A 323  ? 0.3189 0.3568 0.3587 0.0044  0.0411  0.0657  321  GLU A C   
2228  O O   . GLU A 323  ? 0.3196 0.3631 0.3650 0.0036  0.0408  0.0671  321  GLU A O   
2229  C CB  . GLU A 323  ? 0.3473 0.3895 0.3801 0.0038  0.0458  0.0667  321  GLU A CB  
2230  C CG  . GLU A 323  ? 0.3819 0.4354 0.4200 0.0063  0.0480  0.0659  321  GLU A CG  
2231  C CD  . GLU A 323  ? 0.4141 0.4776 0.4537 0.0038  0.0509  0.0696  321  GLU A CD  
2232  O OE1 . GLU A 323  ? 0.4364 0.4984 0.4722 0.0011  0.0516  0.0724  321  GLU A OE1 
2233  O OE2 . GLU A 323  ? 0.4513 0.5248 0.4965 0.0046  0.0525  0.0699  321  GLU A OE2 
2234  N N   . VAL A 324  ? 0.2875 0.3203 0.3253 0.0076  0.0399  0.0627  322  VAL A N   
2235  C CA  . VAL A 324  ? 0.2511 0.2850 0.2941 0.0105  0.0383  0.0612  322  VAL A CA  
2236  C C   . VAL A 324  ? 0.2805 0.3129 0.3261 0.0079  0.0354  0.0636  322  VAL A C   
2237  O O   . VAL A 324  ? 0.3273 0.3649 0.3789 0.0085  0.0347  0.0643  322  VAL A O   
2238  C CB  . VAL A 324  ? 0.3552 0.3832 0.3965 0.0141  0.0371  0.0580  322  VAL A CB  
2239  C CG1 . VAL A 324  ? 0.3561 0.3845 0.4038 0.0167  0.0346  0.0574  322  VAL A CG1 
2240  C CG2 . VAL A 324  ? 0.3447 0.3760 0.3844 0.0172  0.0398  0.0547  322  VAL A CG2 
2241  N N   . LEU A 325  ? 0.2423 0.2681 0.2836 0.0050  0.0337  0.0646  323  LEU A N   
2242  C CA  . LEU A 325  ? 0.2946 0.3198 0.3378 0.0026  0.0308  0.0663  323  LEU A CA  
2243  C C   . LEU A 325  ? 0.2881 0.3199 0.3360 -0.0001 0.0312  0.0682  323  LEU A C   
2244  O O   . LEU A 325  ? 0.2641 0.2995 0.3166 -0.0004 0.0294  0.0691  323  LEU A O   
2245  C CB  . LEU A 325  ? 0.2556 0.2737 0.2931 0.0001  0.0291  0.0663  323  LEU A CB  
2246  C CG  . LEU A 325  ? 0.3102 0.3219 0.3436 0.0020  0.0281  0.0649  323  LEU A CG  
2247  C CD1 . LEU A 325  ? 0.2962 0.3025 0.3239 -0.0006 0.0274  0.0646  323  LEU A CD1 
2248  C CD2 . LEU A 325  ? 0.2727 0.2846 0.3089 0.0031  0.0254  0.0657  323  LEU A CD2 
2249  N N   . CYS A 326  ? 0.3126 0.3462 0.3597 -0.0022 0.0333  0.0692  324  CYS A N   
2250  C CA  . CYS A 326  ? 0.2780 0.3178 0.3304 -0.0052 0.0335  0.0715  324  CYS A CA  
2251  C C   . CYS A 326  ? 0.2971 0.3459 0.3556 -0.0031 0.0350  0.0718  324  CYS A C   
2252  O O   . CYS A 326  ? 0.2579 0.3123 0.3221 -0.0052 0.0343  0.0735  324  CYS A O   
2253  C CB  . CYS A 326  ? 0.2915 0.3309 0.3422 -0.0082 0.0351  0.0734  324  CYS A CB  
2254  S SG  . CYS A 326  ? 0.3651 0.3949 0.4113 -0.0114 0.0323  0.0729  324  CYS A SG  
2255  N N   . LEU A 327  ? 0.2784 0.3292 0.3365 0.0009  0.0369  0.0699  325  LEU A N   
2256  C CA  . LEU A 327  ? 0.2814 0.3412 0.3456 0.0036  0.0383  0.0694  325  LEU A CA  
2257  C C   . LEU A 327  ? 0.2955 0.3545 0.3635 0.0065  0.0356  0.0680  325  LEU A C   
2258  O O   . LEU A 327  ? 0.3001 0.3664 0.3743 0.0088  0.0361  0.0675  325  LEU A O   
2259  C CB  . LEU A 327  ? 0.3210 0.3849 0.3836 0.0068  0.0416  0.0673  325  LEU A CB  
2260  C CG  . LEU A 327  ? 0.3444 0.4117 0.4041 0.0039  0.0445  0.0696  325  LEU A CG  
2261  C CD1 . LEU A 327  ? 0.3556 0.4282 0.4129 0.0074  0.0478  0.0672  325  LEU A CD1 
2262  C CD2 . LEU A 327  ? 0.3534 0.4289 0.4188 0.0004  0.0453  0.0732  325  LEU A CD2 
2263  N N   . ASP A 328  ? 0.2692 0.3202 0.3342 0.0062  0.0326  0.0679  326  ASP A N   
2264  C CA  . ASP A 328  ? 0.2946 0.3445 0.3630 0.0089  0.0298  0.0675  326  ASP A CA  
2265  C C   . ASP A 328  ? 0.2901 0.3444 0.3634 0.0068  0.0275  0.0697  326  ASP A C   
2266  O O   . ASP A 328  ? 0.2830 0.3350 0.3538 0.0033  0.0257  0.0711  326  ASP A O   
2267  C CB  . ASP A 328  ? 0.2930 0.3336 0.3561 0.0091  0.0276  0.0672  326  ASP A CB  
2268  C CG  . ASP A 328  ? 0.3408 0.3801 0.4080 0.0120  0.0246  0.0674  326  ASP A CG  
2269  O OD1 . ASP A 328  ? 0.3252 0.3696 0.3982 0.0123  0.0229  0.0689  326  ASP A OD1 
2270  O OD2 . ASP A 328  ? 0.3489 0.3819 0.4137 0.0139  0.0237  0.0665  326  ASP A OD2 
2271  N N   . GLY A 329  ? 0.2699 0.3310 0.3504 0.0093  0.0273  0.0697  327  GLY A N   
2272  C CA  . GLY A 329  ? 0.2536 0.3201 0.3392 0.0075  0.0252  0.0717  327  GLY A CA  
2273  C C   . GLY A 329  ? 0.3043 0.3667 0.3882 0.0061  0.0212  0.0732  327  GLY A C   
2274  O O   . GLY A 329  ? 0.2671 0.3329 0.3526 0.0031  0.0194  0.0746  327  GLY A O   
2275  N N   . ASP A 330  ? 0.2728 0.3286 0.3535 0.0080  0.0196  0.0731  328  ASP A N   
2276  C CA  . ASP A 330  ? 0.3264 0.3796 0.4052 0.0066  0.0159  0.0751  328  ASP A CA  
2277  C C   . ASP A 330  ? 0.2585 0.3099 0.3316 0.0022  0.0155  0.0751  328  ASP A C   
2278  O O   . ASP A 330  ? 0.2814 0.3341 0.3537 0.0005  0.0125  0.0765  328  ASP A O   
2279  C CB  . ASP A 330  ? 0.3147 0.3610 0.3910 0.0090  0.0146  0.0753  328  ASP A CB  
2280  C CG  . ASP A 330  ? 0.3442 0.3917 0.4276 0.0135  0.0137  0.0752  328  ASP A CG  
2281  O OD1 . ASP A 330  ? 0.3759 0.4302 0.4660 0.0146  0.0132  0.0757  328  ASP A OD1 
2282  O OD2 . ASP A 330  ? 0.3076 0.3492 0.3904 0.0160  0.0133  0.0744  328  ASP A OD2 
2283  N N   . LEU A 331  ? 0.2501 0.2990 0.3195 0.0006  0.0181  0.0736  329  LEU A N   
2284  C CA  . LEU A 331  ? 0.2523 0.2991 0.3174 -0.0033 0.0175  0.0731  329  LEU A CA  
2285  C C   . LEU A 331  ? 0.2766 0.3288 0.3458 -0.0063 0.0178  0.0732  329  LEU A C   
2286  O O   . LEU A 331  ? 0.2724 0.3228 0.3395 -0.0095 0.0172  0.0723  329  LEU A O   
2287  C CB  . LEU A 331  ? 0.2505 0.2902 0.3092 -0.0036 0.0195  0.0717  329  LEU A CB  
2288  C CG  . LEU A 331  ? 0.2458 0.2793 0.2998 -0.0015 0.0189  0.0713  329  LEU A CG  
2289  C CD1 . LEU A 331  ? 0.2432 0.2707 0.2917 -0.0016 0.0213  0.0697  329  LEU A CD1 
2290  C CD2 . LEU A 331  ? 0.2674 0.3002 0.3187 -0.0031 0.0157  0.0721  329  LEU A CD2 
2291  N N   . SER A 332  ? 0.3050 0.3640 0.3808 -0.0052 0.0186  0.0741  330  SER A N   
2292  C CA  . SER A 332  ? 0.3173 0.3817 0.3978 -0.0083 0.0190  0.0745  330  SER A CA  
2293  C C   . SER A 332  ? 0.2694 0.3362 0.3515 -0.0111 0.0154  0.0744  330  SER A C   
2294  O O   . SER A 332  ? 0.2545 0.3215 0.3353 -0.0101 0.0126  0.0745  330  SER A O   
2295  C CB  . SER A 332  ? 0.2838 0.3561 0.3714 -0.0064 0.0208  0.0755  330  SER A CB  
2296  O OG  . SER A 332  ? 0.2965 0.3726 0.3881 -0.0039 0.0186  0.0760  330  SER A OG  
2297  N N   . GLY A 333  ? 0.2577 0.3266 0.3428 -0.0147 0.0151  0.0741  331  GLY A N   
2298  C CA  . GLY A 333  ? 0.3131 0.3843 0.4000 -0.0175 0.0115  0.0729  331  GLY A CA  
2299  C C   . GLY A 333  ? 0.2763 0.3415 0.3576 -0.0194 0.0098  0.0705  331  GLY A C   
2300  O O   . GLY A 333  ? 0.2966 0.3641 0.3795 -0.0217 0.0067  0.0685  331  GLY A O   
2301  N N   . TRP A 334  ? 0.2688 0.3269 0.3439 -0.0183 0.0116  0.0701  332  TRP A N   
2302  C CA  . TRP A 334  ? 0.2718 0.3243 0.3414 -0.0196 0.0102  0.0677  332  TRP A CA  
2303  C C   . TRP A 334  ? 0.2787 0.3253 0.3470 -0.0209 0.0125  0.0676  332  TRP A C   
2304  O O   . TRP A 334  ? 0.2674 0.3120 0.3340 -0.0192 0.0157  0.0694  332  TRP A O   
2305  C CB  . TRP A 334  ? 0.2657 0.3153 0.3288 -0.0170 0.0098  0.0676  332  TRP A CB  
2306  C CG  . TRP A 334  ? 0.2523 0.2959 0.3090 -0.0176 0.0094  0.0654  332  TRP A CG  
2307  C CD1 . TRP A 334  ? 0.2665 0.3106 0.3215 -0.0194 0.0067  0.0624  332  TRP A CD1 
2308  C CD2 . TRP A 334  ? 0.2291 0.2659 0.2802 -0.0159 0.0116  0.0657  332  TRP A CD2 
2309  N NE1 . TRP A 334  ? 0.2646 0.3027 0.3134 -0.0190 0.0072  0.0609  332  TRP A NE1 
2310  C CE2 . TRP A 334  ? 0.2523 0.2857 0.2986 -0.0170 0.0102  0.0631  332  TRP A CE2 
2311  C CE3 . TRP A 334  ? 0.2821 0.3161 0.3322 -0.0134 0.0146  0.0675  332  TRP A CE3 
2312  C CZ2 . TRP A 334  ? 0.2771 0.3040 0.3176 -0.0159 0.0116  0.0627  332  TRP A CZ2 
2313  C CZ3 . TRP A 334  ? 0.2985 0.3259 0.3426 -0.0123 0.0159  0.0668  332  TRP A CZ3 
2314  C CH2 . TRP A 334  ? 0.2668 0.2906 0.3063 -0.0137 0.0144  0.0646  332  TRP A CH2 
2315  N N   . ASN A 335  ? 0.2417 0.2860 0.3111 -0.0239 0.0106  0.0656  333  ASN A N   
2316  C CA  . ASN A 335  ? 0.2414 0.2802 0.3106 -0.0255 0.0121  0.0660  333  ASN A CA  
2317  C C   . ASN A 335  ? 0.2557 0.2876 0.3185 -0.0252 0.0112  0.0633  333  ASN A C   
2318  O O   . ASN A 335  ? 0.2575 0.2845 0.3206 -0.0269 0.0112  0.0630  333  ASN A O   
2319  C CB  . ASN A 335  ? 0.2622 0.3030 0.3393 -0.0293 0.0103  0.0660  333  ASN A CB  
2320  C CG  . ASN A 335  ? 0.2941 0.3413 0.3778 -0.0301 0.0122  0.0697  333  ASN A CG  
2321  O OD1 . ASN A 335  ? 0.2733 0.3219 0.3554 -0.0281 0.0157  0.0725  333  ASN A OD1 
2322  N ND2 . ASN A 335  ? 0.2579 0.3094 0.3495 -0.0331 0.0099  0.0695  333  ASN A ND2 
2323  N N   . GLY A 336  ? 0.2883 0.3199 0.3456 -0.0231 0.0104  0.0618  334  GLY A N   
2324  C CA  . GLY A 336  ? 0.2609 0.2875 0.3124 -0.0228 0.0094  0.0590  334  GLY A CA  
2325  C C   . GLY A 336  ? 0.2791 0.2992 0.3250 -0.0212 0.0122  0.0601  334  GLY A C   
2326  O O   . GLY A 336  ? 0.2666 0.2821 0.3083 -0.0212 0.0115  0.0578  334  GLY A O   
2327  N N   . MET A 337  ? 0.2914 0.3116 0.3374 -0.0196 0.0153  0.0632  335  MET A N   
2328  C CA  A MET A 337  ? 0.2824 0.2972 0.3232 -0.0179 0.0178  0.0639  335  MET A CA  
2329  C CA  B MET A 337  ? 0.2824 0.2972 0.3231 -0.0179 0.0178  0.0638  335  MET A CA  
2330  C C   . MET A 337  ? 0.2465 0.2566 0.2871 -0.0199 0.0181  0.0637  335  MET A C   
2331  O O   . MET A 337  ? 0.2676 0.2795 0.3136 -0.0221 0.0183  0.0654  335  MET A O   
2332  C CB  A MET A 337  ? 0.2819 0.2993 0.3236 -0.0157 0.0208  0.0664  335  MET A CB  
2333  C CB  B MET A 337  ? 0.2821 0.2993 0.3236 -0.0156 0.0208  0.0664  335  MET A CB  
2334  C CG  A MET A 337  ? 0.2953 0.3080 0.3316 -0.0136 0.0233  0.0666  335  MET A CG  
2335  C CG  B MET A 337  ? 0.2953 0.3077 0.3317 -0.0140 0.0233  0.0666  335  MET A CG  
2336  S SD  A MET A 337  ? 0.3342 0.3425 0.3644 -0.0112 0.0222  0.0648  335  MET A SD  
2337  S SD  B MET A 337  ? 0.3185 0.3320 0.3532 -0.0097 0.0251  0.0669  335  MET A SD  
2338  C CE  A MET A 337  ? 0.3092 0.3226 0.3428 -0.0087 0.0218  0.0661  335  MET A CE  
2339  C CE  B MET A 337  ? 0.3063 0.3169 0.3375 -0.0091 0.0222  0.0654  335  MET A CE  
2340  N N   . GLY A 338  ? 0.2603 0.2646 0.2955 -0.0192 0.0180  0.0620  336  GLY A N   
2341  C CA  . GLY A 338  ? 0.2628 0.2622 0.2979 -0.0208 0.0179  0.0619  336  GLY A CA  
2342  C C   . GLY A 338  ? 0.2652 0.2602 0.2943 -0.0188 0.0203  0.0627  336  GLY A C   
2343  O O   . GLY A 338  ? 0.2590 0.2538 0.2837 -0.0163 0.0215  0.0623  336  GLY A O   
2344  N N   . PHE A 339  ? 0.2317 0.2234 0.2613 -0.0202 0.0208  0.0641  337  PHE A N   
2345  C CA  . PHE A 339  ? 0.3154 0.3040 0.3399 -0.0186 0.0232  0.0654  337  PHE A CA  
2346  C C   . PHE A 339  ? 0.2764 0.2597 0.3013 -0.0205 0.0218  0.0656  337  PHE A C   
2347  O O   . PHE A 339  ? 0.2721 0.2558 0.3030 -0.0232 0.0205  0.0673  337  PHE A O   
2348  C CB  . PHE A 339  ? 0.3059 0.2994 0.3316 -0.0179 0.0264  0.0689  337  PHE A CB  
2349  C CG  . PHE A 339  ? 0.2901 0.2822 0.3100 -0.0155 0.0290  0.0693  337  PHE A CG  
2350  C CD1 . PHE A 339  ? 0.3238 0.3159 0.3398 -0.0122 0.0301  0.0673  337  PHE A CD1 
2351  C CD2 . PHE A 339  ? 0.2629 0.2541 0.2820 -0.0166 0.0302  0.0719  337  PHE A CD2 
2352  C CE1 . PHE A 339  ? 0.2902 0.2813 0.3015 -0.0099 0.0323  0.0670  337  PHE A CE1 
2353  C CE2 . PHE A 339  ? 0.2976 0.2885 0.3113 -0.0143 0.0325  0.0720  337  PHE A CE2 
2354  C CZ  . PHE A 339  ? 0.2747 0.2655 0.2845 -0.0109 0.0335  0.0691  337  PHE A CZ  
2355  N N   . VAL A 340  ? 0.2803 0.2588 0.2997 -0.0190 0.0220  0.0640  338  VAL A N   
2356  C CA  . VAL A 340  ? 0.2961 0.2692 0.3155 -0.0203 0.0205  0.0640  338  VAL A CA  
2357  C C   . VAL A 340  ? 0.2710 0.2443 0.2887 -0.0202 0.0230  0.0682  338  VAL A C   
2358  O O   . VAL A 340  ? 0.2957 0.2711 0.3087 -0.0179 0.0258  0.0688  338  VAL A O   
2359  C CB  . VAL A 340  ? 0.2917 0.2603 0.3061 -0.0187 0.0192  0.0598  338  VAL A CB  
2360  C CG1 . VAL A 340  ? 0.3069 0.2700 0.3218 -0.0196 0.0175  0.0596  338  VAL A CG1 
2361  C CG2 . VAL A 340  ? 0.2734 0.2438 0.2892 -0.0188 0.0168  0.0558  338  VAL A CG2 
2362  N N   . VAL A 341  ? 0.2913 0.2627 0.3132 -0.0226 0.0217  0.0710  339  VAL A N   
2363  C CA  . VAL A 341  ? 0.2512 0.2227 0.2711 -0.0229 0.0235  0.0754  339  VAL A CA  
2364  C C   . VAL A 341  ? 0.2913 0.2559 0.3117 -0.0237 0.0208  0.0751  339  VAL A C   
2365  O O   . VAL A 341  ? 0.3122 0.2733 0.3384 -0.0256 0.0174  0.0737  339  VAL A O   
2366  C CB  . VAL A 341  ? 0.3325 0.3101 0.3581 -0.0254 0.0248  0.0811  339  VAL A CB  
2367  C CG1 . VAL A 341  ? 0.3256 0.3103 0.3515 -0.0242 0.0272  0.0807  339  VAL A CG1 
2368  C CG2 . VAL A 341  ? 0.3679 0.3432 0.4022 -0.0290 0.0213  0.0824  339  VAL A CG2 
2369  N N   . GLN A 342  ? 0.3099 0.2728 0.3245 -0.0222 0.0222  0.0760  340  GLN A N   
2370  C CA  . GLN A 342  ? 0.2853 0.2416 0.2995 -0.0223 0.0197  0.0753  340  GLN A CA  
2371  C C   . GLN A 342  ? 0.3229 0.2793 0.3407 -0.0247 0.0193  0.0817  340  GLN A C   
2372  O O   . GLN A 342  ? 0.3023 0.2632 0.3163 -0.0242 0.0221  0.0857  340  GLN A O   
2373  C CB  . GLN A 342  ? 0.2593 0.2136 0.2651 -0.0191 0.0211  0.0722  340  GLN A CB  
2374  C CG  . GLN A 342  ? 0.2729 0.2275 0.2753 -0.0170 0.0215  0.0668  340  GLN A CG  
2375  C CD  . GLN A 342  ? 0.3012 0.2569 0.2962 -0.0140 0.0242  0.0655  340  GLN A CD  
2376  O OE1 . GLN A 342  ? 0.2832 0.2431 0.2761 -0.0132 0.0269  0.0680  340  GLN A OE1 
2377  N NE2 . GLN A 342  ? 0.3086 0.2610 0.3000 -0.0124 0.0233  0.0613  340  GLN A NE2 
2378  N N   . ALA A 343  ? 0.3166 0.2686 0.3421 -0.0272 0.0154  0.0827  341  ALA A N   
2379  C CA  . ALA A 343  ? 0.3197 0.2715 0.3501 -0.0300 0.0144  0.0898  341  ALA A CA  
2380  C C   . ALA A 343  ? 0.3295 0.2788 0.3548 -0.0287 0.0145  0.0918  341  ALA A C   
2381  O O   . ALA A 343  ? 0.3327 0.2838 0.3601 -0.0307 0.0145  0.0988  341  ALA A O   
2382  C CB  . ALA A 343  ? 0.3040 0.2507 0.3452 -0.0329 0.0095  0.0898  341  ALA A CB  
2383  N N   . TYR A 344  ? 0.3084 0.2539 0.3273 -0.0256 0.0146  0.0862  342  TYR A N   
2384  C CA  . TYR A 344  ? 0.3371 0.2809 0.3511 -0.0244 0.0148  0.0883  342  TYR A CA  
2385  C C   . TYR A 344  ? 0.3342 0.2854 0.3409 -0.0231 0.0193  0.0913  342  TYR A C   
2386  O O   . TYR A 344  ? 0.3444 0.2959 0.3466 -0.0221 0.0198  0.0936  342  TYR A O   
2387  C CB  . TYR A 344  ? 0.3419 0.2797 0.3521 -0.0217 0.0131  0.0816  342  TYR A CB  
2388  C CG  . TYR A 344  ? 0.3135 0.2525 0.3158 -0.0186 0.0156  0.0756  342  TYR A CG  
2389  C CD1 . TYR A 344  ? 0.2887 0.2335 0.2879 -0.0178 0.0190  0.0752  342  TYR A CD1 
2390  C CD2 . TYR A 344  ? 0.3199 0.2545 0.3189 -0.0164 0.0142  0.0704  342  TYR A CD2 
2391  C CE1 . TYR A 344  ? 0.3320 0.2772 0.3252 -0.0151 0.0206  0.0701  342  TYR A CE1 
2392  C CE2 . TYR A 344  ? 0.3278 0.2635 0.3205 -0.0140 0.0161  0.0656  342  TYR A CE2 
2393  C CZ  . TYR A 344  ? 0.3059 0.2466 0.2960 -0.0134 0.0191  0.0657  342  TYR A CZ  
2394  O OH  . TYR A 344  ? 0.3232 0.2646 0.3082 -0.0112 0.0205  0.0615  342  TYR A OH  
2395  N N   . GLY A 345  ? 0.3119 0.2695 0.3175 -0.0228 0.0223  0.0910  343  GLY A N   
2396  C CA  . GLY A 345  ? 0.3127 0.2781 0.3120 -0.0211 0.0264  0.0927  343  GLY A CA  
2397  C C   . GLY A 345  ? 0.3419 0.3150 0.3444 -0.0238 0.0278  0.1006  343  GLY A C   
2398  O O   . GLY A 345  ? 0.3130 0.2873 0.3231 -0.0268 0.0267  0.1040  343  GLY A O   
2399  N N   . LYS A 346  ? 0.2978 0.2769 0.2947 -0.0226 0.0302  0.1035  344  LYS A N   
2400  C CA  . LYS A 346  ? 0.3334 0.3219 0.3322 -0.0250 0.0320  0.1115  344  LYS A CA  
2401  C C   . LYS A 346  ? 0.3419 0.3392 0.3431 -0.0255 0.0349  0.1122  344  LYS A C   
2402  O O   . LYS A 346  ? 0.3498 0.3542 0.3557 -0.0287 0.0356  0.1193  344  LYS A O   
2403  C CB  . LYS A 346  ? 0.3139 0.3081 0.3048 -0.0229 0.0341  0.1130  344  LYS A CB  
2404  C CG  . LYS A 346  ? 0.3670 0.3538 0.3567 -0.0232 0.0310  0.1145  344  LYS A CG  
2405  C CD  . LYS A 346  ? 0.3562 0.3476 0.3369 -0.0202 0.0329  0.1134  344  LYS A CD  
2406  C CE  . LYS A 346  ? 0.3904 0.3771 0.3710 -0.0212 0.0299  0.1175  344  LYS A CE  
2407  N NZ  . LYS A 346  ? 0.4022 0.3940 0.3740 -0.0183 0.0316  0.1164  344  LYS A NZ  
2408  N N   . ARG A 347  ? 0.3200 0.3172 0.3187 -0.0226 0.0364  0.1054  345  ARG A N   
2409  C CA  . ARG A 347  ? 0.3234 0.3292 0.3243 -0.0225 0.0392  0.1053  345  ARG A CA  
2410  C C   . ARG A 347  ? 0.3160 0.3188 0.3251 -0.0252 0.0371  0.1055  345  ARG A C   
2411  O O   . ARG A 347  ? 0.3288 0.3389 0.3410 -0.0255 0.0391  0.1062  345  ARG A O   
2412  C CB  . ARG A 347  ? 0.3081 0.3156 0.3031 -0.0179 0.0415  0.0980  345  ARG A CB  
2413  C CG  . ARG A 347  ? 0.2783 0.2919 0.2658 -0.0150 0.0441  0.0974  345  ARG A CG  
2414  C CD  . ARG A 347  ? 0.3095 0.3214 0.2920 -0.0104 0.0452  0.0895  345  ARG A CD  
2415  N NE  . ARG A 347  ? 0.3301 0.3303 0.3108 -0.0096 0.0424  0.0853  345  ARG A NE  
2416  C CZ  . ARG A 347  ? 0.3130 0.3093 0.2909 -0.0065 0.0423  0.0790  345  ARG A CZ  
2417  N NH1 . ARG A 347  ? 0.2963 0.2984 0.2733 -0.0036 0.0445  0.0756  345  ARG A NH1 
2418  N NH2 . ARG A 347  ? 0.3312 0.3179 0.3078 -0.0063 0.0398  0.0761  345  ARG A NH2 
2419  N N   . CYS A 348  ? 0.3108 0.3035 0.3238 -0.0269 0.0331  0.1046  346  CYS A N   
2420  C CA  . CYS A 348  ? 0.3035 0.2927 0.3239 -0.0289 0.0307  0.1030  346  CYS A CA  
2421  C C   . CYS A 348  ? 0.3404 0.3372 0.3682 -0.0322 0.0315  0.1085  346  CYS A C   
2422  O O   . CYS A 348  ? 0.3126 0.3121 0.3431 -0.0319 0.0320  0.1058  346  CYS A O   
2423  C CB  . CYS A 348  ? 0.3532 0.3319 0.3777 -0.0305 0.0260  0.1020  346  CYS A CB  
2424  S SG  . CYS A 348  ? 0.4139 0.3881 0.4455 -0.0317 0.0228  0.0970  346  CYS A SG  
2425  N N   . PRO A 349  ? 0.3290 0.3298 0.3609 -0.0356 0.0313  0.1164  347  PRO A N   
2426  C CA  . PRO A 349  ? 0.3450 0.3536 0.3847 -0.0390 0.0320  0.1217  347  PRO A CA  
2427  C C   . PRO A 349  ? 0.3346 0.3549 0.3710 -0.0369 0.0367  0.1209  347  PRO A C   
2428  O O   . PRO A 349  ? 0.3184 0.3436 0.3604 -0.0383 0.0372  0.1215  347  PRO A O   
2429  C CB  . PRO A 349  ? 0.3214 0.3324 0.3652 -0.0430 0.0310  0.1311  347  PRO A CB  
2430  C CG  . PRO A 349  ? 0.3761 0.3838 0.4120 -0.0407 0.0311  0.1307  347  PRO A CG  
2431  C CD  . PRO A 349  ? 0.3249 0.3232 0.3557 -0.0368 0.0300  0.1214  347  PRO A CD  
2432  N N   . PHE A 350  ? 0.3240 0.3487 0.3516 -0.0333 0.0399  0.1189  348  PHE A N   
2433  C CA  . PHE A 350  ? 0.3337 0.3698 0.3585 -0.0307 0.0441  0.1173  348  PHE A CA  
2434  C C   . PHE A 350  ? 0.2867 0.3194 0.3106 -0.0274 0.0441  0.1095  348  PHE A C   
2435  O O   . PHE A 350  ? 0.2743 0.3148 0.3007 -0.0267 0.0462  0.1086  348  PHE A O   
2436  C CB  . PHE A 350  ? 0.2772 0.3195 0.2937 -0.0279 0.0471  0.1175  348  PHE A CB  
2437  C CG  . PHE A 350  ? 0.3026 0.3482 0.3197 -0.0311 0.0467  0.1257  348  PHE A CG  
2438  C CD1 . PHE A 350  ? 0.3658 0.4232 0.3877 -0.0346 0.0484  0.1336  348  PHE A CD1 
2439  C CD2 . PHE A 350  ? 0.3650 0.4019 0.3786 -0.0311 0.0443  0.1261  348  PHE A CD2 
2440  C CE1 . PHE A 350  ? 0.3450 0.4058 0.3682 -0.0380 0.0477  0.1424  348  PHE A CE1 
2441  C CE2 . PHE A 350  ? 0.3736 0.4133 0.3884 -0.0343 0.0435  0.1345  348  PHE A CE2 
2442  C CZ  . PHE A 350  ? 0.3774 0.4289 0.3970 -0.0378 0.0451  0.1428  348  PHE A CZ  
2443  N N   . VAL A 351  ? 0.2857 0.3073 0.3063 -0.0256 0.0417  0.1040  349  VAL A N   
2444  C CA  . VAL A 351  ? 0.2777 0.2953 0.2986 -0.0233 0.0409  0.0976  349  VAL A CA  
2445  C C   . VAL A 351  ? 0.2928 0.3109 0.3222 -0.0265 0.0390  0.0991  349  VAL A C   
2446  O O   . VAL A 351  ? 0.2932 0.3153 0.3247 -0.0252 0.0399  0.0966  349  VAL A O   
2447  C CB  . VAL A 351  ? 0.2869 0.2932 0.3034 -0.0217 0.0383  0.0927  349  VAL A CB  
2448  C CG1 . VAL A 351  ? 0.2814 0.2842 0.2983 -0.0199 0.0371  0.0871  349  VAL A CG1 
2449  C CG2 . VAL A 351  ? 0.3040 0.3100 0.3124 -0.0186 0.0401  0.0910  349  VAL A CG2 
2450  N N   . LEU A 352  ? 0.2981 0.3120 0.3332 -0.0305 0.0361  0.1028  350  LEU A N   
2451  C CA  . LEU A 352  ? 0.2989 0.3130 0.3428 -0.0336 0.0338  0.1039  350  LEU A CA  
2452  C C   . LEU A 352  ? 0.3088 0.3348 0.3570 -0.0349 0.0367  0.1081  350  LEU A C   
2453  O O   . LEU A 352  ? 0.2985 0.3275 0.3510 -0.0351 0.0365  0.1063  350  LEU A O   
2454  C CB  . LEU A 352  ? 0.2862 0.2935 0.3363 -0.0377 0.0298  0.1072  350  LEU A CB  
2455  C CG  . LEU A 352  ? 0.3366 0.3325 0.3848 -0.0365 0.0262  0.1017  350  LEU A CG  
2456  C CD1 . LEU A 352  ? 0.3460 0.3356 0.4009 -0.0402 0.0223  0.1051  350  LEU A CD1 
2457  C CD2 . LEU A 352  ? 0.2824 0.2762 0.3319 -0.0354 0.0246  0.0953  350  LEU A CD2 
2458  N N   . ASP A 353  ? 0.3157 0.3495 0.3628 -0.0359 0.0394  0.1139  351  ASP A N   
2459  C CA  . ASP A 353  ? 0.2949 0.3420 0.3456 -0.0368 0.0426  0.1177  351  ASP A CA  
2460  C C   . ASP A 353  ? 0.2730 0.3249 0.3205 -0.0324 0.0451  0.1118  351  ASP A C   
2461  O O   . ASP A 353  ? 0.2877 0.3464 0.3407 -0.0330 0.0459  0.1121  351  ASP A O   
2462  C CB  . ASP A 353  ? 0.3315 0.3877 0.3790 -0.0374 0.0457  0.1238  351  ASP A CB  
2463  C CG  . ASP A 353  ? 0.3418 0.3966 0.3949 -0.0427 0.0434  0.1321  351  ASP A CG  
2464  O OD1 . ASP A 353  ? 0.3825 0.4306 0.4437 -0.0463 0.0396  0.1336  351  ASP A OD1 
2465  O OD2 . ASP A 353  ? 0.4034 0.4644 0.4533 -0.0433 0.0453  0.1374  351  ASP A OD2 
2466  N N   . PHE A 354  ? 0.2881 0.3363 0.3276 -0.0279 0.0460  0.1063  352  PHE A N   
2467  C CA  . PHE A 354  ? 0.2819 0.3335 0.3190 -0.0234 0.0479  0.1006  352  PHE A CA  
2468  C C   . PHE A 354  ? 0.2682 0.3142 0.3093 -0.0234 0.0451  0.0969  352  PHE A C   
2469  O O   . PHE A 354  ? 0.2906 0.3430 0.3351 -0.0221 0.0462  0.0955  352  PHE A O   
2470  C CB  . PHE A 354  ? 0.2726 0.3202 0.3010 -0.0190 0.0488  0.0959  352  PHE A CB  
2471  C CG  . PHE A 354  ? 0.2972 0.3452 0.3240 -0.0145 0.0495  0.0897  352  PHE A CG  
2472  C CD1 . PHE A 354  ? 0.3129 0.3718 0.3400 -0.0115 0.0527  0.0883  352  PHE A CD1 
2473  C CD2 . PHE A 354  ? 0.3051 0.3432 0.3309 -0.0133 0.0467  0.0853  352  PHE A CD2 
2474  C CE1 . PHE A 354  ? 0.3551 0.4139 0.3821 -0.0072 0.0528  0.0826  352  PHE A CE1 
2475  C CE2 . PHE A 354  ? 0.3242 0.3626 0.3496 -0.0094 0.0470  0.0805  352  PHE A CE2 
2476  C CZ  . PHE A 354  ? 0.3420 0.3901 0.3683 -0.0063 0.0498  0.0791  352  PHE A CZ  
2477  N N   . ILE A 355  ? 0.2593 0.2944 0.3002 -0.0247 0.0416  0.0953  353  ILE A N   
2478  C CA  . ILE A 355  ? 0.2519 0.2827 0.2960 -0.0247 0.0388  0.0916  353  ILE A CA  
2479  C C   . ILE A 355  ? 0.2740 0.3101 0.3270 -0.0282 0.0379  0.0946  353  ILE A C   
2480  O O   . ILE A 355  ? 0.2728 0.3116 0.3290 -0.0273 0.0373  0.0923  353  ILE A O   
2481  C CB  . ILE A 355  ? 0.2584 0.2777 0.3002 -0.0254 0.0352  0.0889  353  ILE A CB  
2482  C CG1 . ILE A 355  ? 0.2674 0.2816 0.3006 -0.0218 0.0360  0.0853  353  ILE A CG1 
2483  C CG2 . ILE A 355  ? 0.2750 0.2916 0.3208 -0.0261 0.0321  0.0856  353  ILE A CG2 
2484  C CD1 . ILE A 355  ? 0.2926 0.2968 0.3236 -0.0225 0.0329  0.0830  353  ILE A CD1 
2485  N N   . ILE A 356  ? 0.2613 0.2989 0.3191 -0.0323 0.0373  0.1001  354  ILE A N   
2486  C CA  . ILE A 356  ? 0.2593 0.3022 0.3266 -0.0361 0.0362  0.1035  354  ILE A CA  
2487  C C   . ILE A 356  ? 0.2922 0.3476 0.3615 -0.0348 0.0399  0.1049  354  ILE A C   
2488  O O   . ILE A 356  ? 0.2756 0.3351 0.3508 -0.0356 0.0391  0.1043  354  ILE A O   
2489  C CB  . ILE A 356  ? 0.2890 0.3309 0.3616 -0.0410 0.0348  0.1099  354  ILE A CB  
2490  C CG1 . ILE A 356  ? 0.2827 0.3120 0.3557 -0.0424 0.0303  0.1076  354  ILE A CG1 
2491  C CG2 . ILE A 356  ? 0.3327 0.3820 0.4155 -0.0452 0.0343  0.1146  354  ILE A CG2 
2492  C CD1 . ILE A 356  ? 0.3428 0.3694 0.4202 -0.0465 0.0286  0.1139  354  ILE A CD1 
2493  N N   . ASP A 357  ? 0.2854 0.3474 0.3497 -0.0325 0.0437  0.1062  355  ASP A N   
2494  C CA  . ASP A 357  ? 0.3075 0.3821 0.3734 -0.0304 0.0473  0.1062  355  ASP A CA  
2495  C C   . ASP A 357  ? 0.2987 0.3719 0.3632 -0.0260 0.0469  0.0997  355  ASP A C   
2496  O O   . ASP A 357  ? 0.2712 0.3522 0.3408 -0.0253 0.0478  0.0993  355  ASP A O   
2497  C CB  . ASP A 357  ? 0.2547 0.3372 0.3151 -0.0283 0.0513  0.1078  355  ASP A CB  
2498  C CG  . ASP A 357  ? 0.2834 0.3792 0.3452 -0.0253 0.0549  0.1065  355  ASP A CG  
2499  O OD1 . ASP A 357  ? 0.3068 0.4129 0.3754 -0.0282 0.0561  0.1111  355  ASP A OD1 
2500  O OD2 . ASP A 357  ? 0.3265 0.4228 0.3836 -0.0201 0.0563  0.1008  355  ASP A OD2 
2501  N N   . LEU A 358  ? 0.2719 0.3356 0.3298 -0.0229 0.0457  0.0950  356  LEU A N   
2502  C CA  . LEU A 358  ? 0.2651 0.3268 0.3220 -0.0191 0.0449  0.0896  356  LEU A CA  
2503  C C   . LEU A 358  ? 0.2696 0.3295 0.3326 -0.0213 0.0417  0.0892  356  LEU A C   
2504  O O   . LEU A 358  ? 0.2885 0.3528 0.3547 -0.0193 0.0416  0.0873  356  LEU A O   
2505  C CB  . LEU A 358  ? 0.2592 0.3109 0.3084 -0.0162 0.0438  0.0855  356  LEU A CB  
2506  C CG  . LEU A 358  ? 0.3052 0.3533 0.3534 -0.0127 0.0423  0.0808  356  LEU A CG  
2507  C CD1 . LEU A 358  ? 0.2939 0.3506 0.3438 -0.0087 0.0448  0.0790  356  LEU A CD1 
2508  C CD2 . LEU A 358  ? 0.2996 0.3376 0.3407 -0.0109 0.0409  0.0777  356  LEU A CD2 
2509  N N   . ALA A 359  ? 0.2727 0.3263 0.3379 -0.0252 0.0387  0.0908  357  ALA A N   
2510  C CA  . ALA A 359  ? 0.2805 0.3335 0.3521 -0.0276 0.0355  0.0901  357  ALA A CA  
2511  C C   . ALA A 359  ? 0.2491 0.3128 0.3286 -0.0293 0.0367  0.0932  357  ALA A C   
2512  O O   . ALA A 359  ? 0.3032 0.3700 0.3869 -0.0288 0.0354  0.0915  357  ALA A O   
2513  C CB  . ALA A 359  ? 0.3136 0.3587 0.3870 -0.0315 0.0320  0.0909  357  ALA A CB  
2514  N N   . ARG A 360  ? 0.2768 0.3473 0.3586 -0.0313 0.0394  0.0981  358  ARG A N   
2515  C CA  . ARG A 360  ? 0.2596 0.3420 0.3492 -0.0331 0.0410  0.1014  358  ARG A CA  
2516  C C   . ARG A 360  ? 0.2906 0.3808 0.3795 -0.0283 0.0435  0.0984  358  ARG A C   
2517  O O   . ARG A 360  ? 0.2930 0.3892 0.3882 -0.0285 0.0428  0.0980  358  ARG A O   
2518  C CB  . ARG A 360  ? 0.3304 0.4196 0.4219 -0.0362 0.0435  0.1078  358  ARG A CB  
2519  C CG  . ARG A 360  ? 0.3311 0.4141 0.4268 -0.0416 0.0405  0.1121  358  ARG A CG  
2520  C CD  . ARG A 360  ? 0.4240 0.5161 0.5236 -0.0454 0.0429  0.1199  358  ARG A CD  
2521  N NE  . ARG A 360  ? 0.4355 0.5195 0.5375 -0.0498 0.0400  0.1239  358  ARG A NE  
2522  C CZ  . ARG A 360  ? 0.4728 0.5533 0.5840 -0.0545 0.0361  0.1262  358  ARG A CZ  
2523  N NH1 . ARG A 360  ? 0.3968 0.4820 0.5156 -0.0559 0.0349  0.1254  358  ARG A NH1 
2524  N NH2 . ARG A 360  ? 0.4829 0.5549 0.5963 -0.0578 0.0330  0.1291  358  ARG A NH2 
2525  N N   . ARG A 361  ? 0.2492 0.3396 0.3311 -0.0239 0.0461  0.0959  359  ARG A N   
2526  C CA  . ARG A 361  ? 0.2668 0.3646 0.3489 -0.0190 0.0482  0.0926  359  ARG A CA  
2527  C C   . ARG A 361  ? 0.3186 0.4112 0.4017 -0.0167 0.0452  0.0884  359  ARG A C   
2528  O O   . ARG A 361  ? 0.3099 0.4096 0.3982 -0.0148 0.0454  0.0873  359  ARG A O   
2529  C CB  . ARG A 361  ? 0.3036 0.4014 0.3783 -0.0148 0.0509  0.0900  359  ARG A CB  
2530  C CG  . ARG A 361  ? 0.3033 0.4088 0.3763 -0.0164 0.0543  0.0940  359  ARG A CG  
2531  C CD  . ARG A 361  ? 0.3515 0.4586 0.4175 -0.0115 0.0569  0.0904  359  ARG A CD  
2532  N NE  . ARG A 361  ? 0.3175 0.4125 0.3762 -0.0113 0.0554  0.0891  359  ARG A NE  
2533  C CZ  . ARG A 361  ? 0.3627 0.4504 0.4165 -0.0072 0.0545  0.0837  359  ARG A CZ  
2534  N NH1 . ARG A 361  ? 0.3520 0.4423 0.4077 -0.0027 0.0546  0.0792  359  ARG A NH1 
2535  N NH2 . ARG A 361  ? 0.3048 0.3825 0.3522 -0.0075 0.0532  0.0831  359  ARG A NH2 
2536  N N   . SER A 362  ? 0.2604 0.3414 0.3388 -0.0166 0.0424  0.0862  360  SER A N   
2537  C CA  . SER A 362  ? 0.2854 0.3618 0.3638 -0.0145 0.0394  0.0828  360  SER A CA  
2538  C C   . SER A 362  ? 0.3039 0.3808 0.3884 -0.0180 0.0362  0.0838  360  SER A C   
2539  O O   . SER A 362  ? 0.2931 0.3703 0.3796 -0.0163 0.0341  0.0818  360  SER A O   
2540  C CB  . SER A 362  ? 0.3003 0.3655 0.3711 -0.0131 0.0378  0.0802  360  SER A CB  
2541  O OG  . SER A 362  ? 0.2715 0.3302 0.3408 -0.0171 0.0360  0.0815  360  SER A OG  
2542  N N   . GLY A 363  ? 0.2852 0.3625 0.3731 -0.0227 0.0356  0.0869  361  GLY A N   
2543  C CA  . GLY A 363  ? 0.2749 0.3516 0.3686 -0.0262 0.0320  0.0871  361  GLY A CA  
2544  C C   . GLY A 363  ? 0.3080 0.3752 0.3979 -0.0264 0.0282  0.0838  361  GLY A C   
2545  O O   . GLY A 363  ? 0.3238 0.3916 0.4179 -0.0281 0.0250  0.0826  361  GLY A O   
2546  N N   . ARG A 364  ? 0.2845 0.3440 0.3665 -0.0245 0.0286  0.0821  362  ARG A N   
2547  C CA  . ARG A 364  ? 0.3089 0.3601 0.3868 -0.0248 0.0254  0.0790  362  ARG A CA  
2548  C C   . ARG A 364  ? 0.3064 0.3519 0.3843 -0.0283 0.0243  0.0799  362  ARG A C   
2549  O O   . ARG A 364  ? 0.3345 0.3791 0.4106 -0.0287 0.0267  0.0824  362  ARG A O   
2550  C CB  . ARG A 364  ? 0.3431 0.3893 0.4130 -0.0208 0.0262  0.0767  362  ARG A CB  
2551  C CG  . ARG A 364  ? 0.3761 0.4274 0.4464 -0.0168 0.0279  0.0764  362  ARG A CG  
2552  C CD  . ARG A 364  ? 0.3116 0.3608 0.3801 -0.0147 0.0252  0.0742  362  ARG A CD  
2553  N NE  . ARG A 364  ? 0.2848 0.3396 0.3563 -0.0113 0.0262  0.0744  362  ARG A NE  
2554  C CZ  . ARG A 364  ? 0.3311 0.3835 0.3995 -0.0074 0.0268  0.0733  362  ARG A CZ  
2555  N NH1 . ARG A 364  ? 0.2483 0.2930 0.3100 -0.0067 0.0265  0.0720  362  ARG A NH1 
2556  N NH2 . ARG A 364  ? 0.2567 0.3144 0.3293 -0.0042 0.0275  0.0732  362  ARG A NH2 
2557  N N   . ARG A 365  ? 0.3071 0.3495 0.3877 -0.0307 0.0204  0.0777  363  ARG A N   
2558  C CA  . ARG A 365  ? 0.2997 0.3360 0.3816 -0.0338 0.0185  0.0779  363  ARG A CA  
2559  C C   . ARG A 365  ? 0.3148 0.3432 0.3884 -0.0318 0.0183  0.0751  363  ARG A C   
2560  O O   . ARG A 365  ? 0.3132 0.3382 0.3847 -0.0314 0.0154  0.0710  363  ARG A O   
2561  C CB  . ARG A 365  ? 0.2718 0.3088 0.3611 -0.0370 0.0143  0.0758  363  ARG A CB  
2562  C CG  . ARG A 365  ? 0.2664 0.2970 0.3590 -0.0402 0.0116  0.0755  363  ARG A CG  
2563  C CD  . ARG A 365  ? 0.3180 0.3513 0.4211 -0.0441 0.0085  0.0759  363  ARG A CD  
2564  N NE  . ARG A 365  ? 0.3734 0.4003 0.4813 -0.0473 0.0059  0.0765  363  ARG A NE  
2565  C CZ  . ARG A 365  ? 0.3054 0.3269 0.4153 -0.0480 0.0015  0.0713  363  ARG A CZ  
2566  N NH1 . ARG A 365  ? 0.3150 0.3378 0.4220 -0.0461 -0.0006 0.0653  363  ARG A NH1 
2567  N NH2 . ARG A 365  ? 0.3111 0.3263 0.4259 -0.0506 -0.0009 0.0722  363  ARG A NH2 
2568  N N   . ILE A 366  ? 0.2847 0.3108 0.3534 -0.0304 0.0213  0.0772  364  ILE A N   
2569  C CA  . ILE A 366  ? 0.2939 0.3132 0.3544 -0.0281 0.0214  0.0747  364  ILE A CA  
2570  C C   . ILE A 366  ? 0.2587 0.2712 0.3200 -0.0303 0.0182  0.0725  364  ILE A C   
2571  O O   . ILE A 366  ? 0.2527 0.2638 0.3194 -0.0334 0.0170  0.0748  364  ILE A O   
2572  C CB  . ILE A 366  ? 0.2681 0.2873 0.3238 -0.0262 0.0253  0.0772  364  ILE A CB  
2573  C CG1 . ILE A 366  ? 0.2832 0.3093 0.3386 -0.0233 0.0281  0.0778  364  ILE A CG1 
2574  C CG2 . ILE A 366  ? 0.2515 0.2630 0.2992 -0.0242 0.0251  0.0746  364  ILE A CG2 
2575  C CD1 . ILE A 366  ? 0.3105 0.3395 0.3629 -0.0216 0.0320  0.0801  364  ILE A CD1 
2576  N N   . MET A 367  ? 0.2848 0.2934 0.3412 -0.0286 0.0164  0.0682  365  MET A N   
2577  C CA  . MET A 367  ? 0.3069 0.3094 0.3636 -0.0300 0.0133  0.0652  365  MET A CA  
2578  C C   . MET A 367  ? 0.3098 0.3064 0.3611 -0.0290 0.0151  0.0665  365  MET A C   
2579  O O   . MET A 367  ? 0.3258 0.3212 0.3699 -0.0262 0.0170  0.0657  365  MET A O   
2580  C CB  . MET A 367  ? 0.2720 0.2746 0.3258 -0.0287 0.0108  0.0600  365  MET A CB  
2581  C CG  . MET A 367  ? 0.2883 0.2979 0.3464 -0.0292 0.0093  0.0590  365  MET A CG  
2582  S SD  . MET A 367  ? 0.3337 0.3461 0.3885 -0.0279 0.0062  0.0535  365  MET A SD  
2583  C CE  . MET A 367  ? 0.3417 0.3514 0.4019 -0.0304 0.0018  0.0483  365  MET A CE  
2584  N N   . VAL A 368  ? 0.2850 0.2784 0.3403 -0.0315 0.0143  0.0689  366  VAL A N   
2585  C CA  . VAL A 368  ? 0.2491 0.2379 0.3000 -0.0308 0.0159  0.0710  366  VAL A CA  
2586  C C   . VAL A 368  ? 0.2704 0.2522 0.3216 -0.0313 0.0124  0.0674  366  VAL A C   
2587  O O   . VAL A 368  ? 0.2998 0.2793 0.3585 -0.0341 0.0093  0.0675  366  VAL A O   
2588  C CB  . VAL A 368  ? 0.2909 0.2820 0.3458 -0.0331 0.0176  0.0774  366  VAL A CB  
2589  C CG1 . VAL A 368  ? 0.3429 0.3300 0.3925 -0.0322 0.0191  0.0795  366  VAL A CG1 
2590  C CG2 . VAL A 368  ? 0.3009 0.3004 0.3562 -0.0324 0.0209  0.0802  366  VAL A CG2 
2591  N N   . ARG A 369  ? 0.2644 0.2429 0.3082 -0.0286 0.0128  0.0641  367  ARG A N   
2592  C CA  . ARG A 369  ? 0.2656 0.2379 0.3092 -0.0287 0.0099  0.0604  367  ARG A CA  
2593  C C   . ARG A 369  ? 0.3055 0.2731 0.3472 -0.0288 0.0109  0.0639  367  ARG A C   
2594  O O   . ARG A 369  ? 0.2982 0.2655 0.3326 -0.0266 0.0138  0.0650  367  ARG A O   
2595  C CB  . ARG A 369  ? 0.2815 0.2536 0.3187 -0.0260 0.0095  0.0551  367  ARG A CB  
2596  C CG  . ARG A 369  ? 0.3077 0.2744 0.3449 -0.0258 0.0066  0.0509  367  ARG A CG  
2597  C CD  . ARG A 369  ? 0.3578 0.3245 0.3871 -0.0231 0.0074  0.0473  367  ARG A CD  
2598  N NE  . ARG A 369  ? 0.3430 0.3154 0.3712 -0.0224 0.0068  0.0442  367  ARG A NE  
2599  C CZ  . ARG A 369  ? 0.4172 0.3918 0.4388 -0.0204 0.0081  0.0430  367  ARG A CZ  
2600  N NH1 . ARG A 369  ? 0.4090 0.3804 0.4247 -0.0188 0.0100  0.0439  367  ARG A NH1 
2601  N NH2 . ARG A 369  ? 0.3499 0.3306 0.3714 -0.0203 0.0072  0.0412  367  ARG A NH2 
2602  N N   . LEU A 370  ? 0.2788 0.2428 0.3275 -0.0313 0.0082  0.0655  368  LEU A N   
2603  C CA  . LEU A 370  ? 0.2969 0.2566 0.3451 -0.0318 0.0084  0.0694  368  LEU A CA  
2604  C C   . LEU A 370  ? 0.2810 0.2344 0.3267 -0.0301 0.0060  0.0645  368  LEU A C   
2605  O O   . LEU A 370  ? 0.3035 0.2541 0.3547 -0.0308 0.0020  0.0599  368  LEU A O   
2606  C CB  . LEU A 370  ? 0.2922 0.2511 0.3504 -0.0356 0.0062  0.0744  368  LEU A CB  
2607  C CG  . LEU A 370  ? 0.2958 0.2514 0.3539 -0.0366 0.0065  0.0801  368  LEU A CG  
2608  C CD1 . LEU A 370  ? 0.3067 0.2677 0.3568 -0.0350 0.0116  0.0844  368  LEU A CD1 
2609  C CD2 . LEU A 370  ? 0.3419 0.2963 0.4112 -0.0408 0.0036  0.0855  368  LEU A CD2 
2610  N N   . VAL A 371  ? 0.2862 0.2379 0.3240 -0.0279 0.0083  0.0650  369  VAL A N   
2611  C CA  . VAL A 371  ? 0.2783 0.2245 0.3133 -0.0262 0.0063  0.0608  369  VAL A CA  
2612  C C   . VAL A 371  ? 0.3211 0.2639 0.3544 -0.0263 0.0071  0.0656  369  VAL A C   
2613  O O   . VAL A 371  ? 0.3129 0.2588 0.3453 -0.0272 0.0097  0.0717  369  VAL A O   
2614  C CB  . VAL A 371  ? 0.3483 0.2962 0.3750 -0.0231 0.0080  0.0560  369  VAL A CB  
2615  C CG1 . VAL A 371  ? 0.3434 0.2961 0.3714 -0.0232 0.0076  0.0526  369  VAL A CG1 
2616  C CG2 . VAL A 371  ? 0.3278 0.2775 0.3467 -0.0214 0.0122  0.0593  369  VAL A CG2 
2617  N N   . LYS A 372  ? 0.3276 0.2650 0.3605 -0.0252 0.0047  0.0628  370  LYS A N   
2618  C CA  . LYS A 372  ? 0.3229 0.2575 0.3532 -0.0250 0.0054  0.0673  370  LYS A CA  
2619  C C   . LYS A 372  ? 0.3354 0.2721 0.3551 -0.0221 0.0093  0.0668  370  LYS A C   
2620  O O   . LYS A 372  ? 0.3383 0.2785 0.3544 -0.0221 0.0124  0.0718  370  LYS A O   
2621  C CB  . LYS A 372  ? 0.3872 0.3150 0.4226 -0.0250 0.0009  0.0650  370  LYS A CB  
2622  C CG  . LYS A 372  ? 0.3598 0.2854 0.4071 -0.0283 -0.0029 0.0674  370  LYS A CG  
2623  C CD  . LYS A 372  ? 0.4056 0.3239 0.4605 -0.0287 -0.0080 0.0659  370  LYS A CD  
2624  C CE  . LYS A 372  ? 0.4418 0.3583 0.5095 -0.0323 -0.0118 0.0688  370  LYS A CE  
2625  N NZ  . LYS A 372  ? 0.4153 0.3246 0.4933 -0.0326 -0.0179 0.0656  370  LYS A NZ  
2626  N N   . GLY A 373  ? 0.2978 0.2335 0.3128 -0.0198 0.0091  0.0609  371  GLY A N   
2627  C CA  . GLY A 373  ? 0.2844 0.2223 0.2905 -0.0173 0.0125  0.0599  371  GLY A CA  
2628  C C   . GLY A 373  ? 0.3516 0.2863 0.3538 -0.0152 0.0113  0.0548  371  GLY A C   
2629  O O   . GLY A 373  ? 0.3273 0.2576 0.3322 -0.0152 0.0085  0.0534  371  GLY A O   
2630  N N   . ALA A 374  ? 0.3242 0.2612 0.3203 -0.0133 0.0133  0.0521  372  ALA A N   
2631  C CA  . ALA A 374  ? 0.3520 0.2875 0.3451 -0.0117 0.0122  0.0470  372  ALA A CA  
2632  C C   . ALA A 374  ? 0.3484 0.2827 0.3349 -0.0098 0.0140  0.0473  372  ALA A C   
2633  O O   . ALA A 374  ? 0.3794 0.3130 0.3633 -0.0085 0.0133  0.0435  372  ALA A O   
2634  C CB  . ALA A 374  ? 0.3201 0.2598 0.3122 -0.0113 0.0125  0.0435  372  ALA A CB  
2635  N N   . TYR A 375  ? 0.3277 0.2626 0.3114 -0.0095 0.0163  0.0515  373  TYR A N   
2636  C CA  . TYR A 375  ? 0.3322 0.2669 0.3096 -0.0075 0.0181  0.0512  373  TYR A CA  
2637  C C   . TYR A 375  ? 0.3014 0.2339 0.2776 -0.0073 0.0178  0.0542  373  TYR A C   
2638  O O   . TYR A 375  ? 0.3007 0.2346 0.2721 -0.0060 0.0198  0.0554  373  TYR A O   
2639  C CB  . TYR A 375  ? 0.3327 0.2712 0.3070 -0.0066 0.0211  0.0524  373  TYR A CB  
2640  C CG  . TYR A 375  ? 0.3127 0.2536 0.2881 -0.0067 0.0213  0.0503  373  TYR A CG  
2641  C CD1 . TYR A 375  ? 0.3087 0.2522 0.2888 -0.0083 0.0210  0.0516  373  TYR A CD1 
2642  C CD2 . TYR A 375  ? 0.3642 0.3054 0.3366 -0.0054 0.0215  0.0474  373  TYR A CD2 
2643  C CE1 . TYR A 375  ? 0.3472 0.2934 0.3283 -0.0083 0.0210  0.0500  373  TYR A CE1 
2644  C CE2 . TYR A 375  ? 0.3898 0.3339 0.3634 -0.0057 0.0214  0.0463  373  TYR A CE2 
2645  C CZ  . TYR A 375  ? 0.3895 0.3361 0.3673 -0.0070 0.0211  0.0475  373  TYR A CZ  
2646  O OH  . TYR A 375  ? 0.4025 0.3524 0.3813 -0.0073 0.0209  0.0468  373  TYR A OH  
2647  N N   . TRP A 376  ? 0.2989 0.2282 0.2798 -0.0086 0.0151  0.0553  374  TRP A N   
2648  C CA  . TRP A 376  ? 0.2888 0.2169 0.2698 -0.0090 0.0147  0.0600  374  TRP A CA  
2649  C C   . TRP A 376  ? 0.3575 0.2846 0.3327 -0.0069 0.0152  0.0588  374  TRP A C   
2650  O O   . TRP A 376  ? 0.3354 0.2652 0.3065 -0.0063 0.0172  0.0619  374  TRP A O   
2651  C CB  . TRP A 376  ? 0.3379 0.2620 0.3265 -0.0108 0.0110  0.0614  374  TRP A CB  
2652  C CG  . TRP A 376  ? 0.3227 0.2461 0.3122 -0.0116 0.0103  0.0674  374  TRP A CG  
2653  C CD1 . TRP A 376  ? 0.3367 0.2635 0.3277 -0.0135 0.0116  0.0741  374  TRP A CD1 
2654  C CD2 . TRP A 376  ? 0.3586 0.2783 0.3473 -0.0106 0.0082  0.0678  374  TRP A CD2 
2655  N NE1 . TRP A 376  ? 0.3574 0.2832 0.3486 -0.0139 0.0103  0.0790  374  TRP A NE1 
2656  C CE2 . TRP A 376  ? 0.3675 0.2886 0.3573 -0.0121 0.0082  0.0752  374  TRP A CE2 
2657  C CE3 . TRP A 376  ? 0.3953 0.3113 0.3826 -0.0087 0.0064  0.0627  374  TRP A CE3 
2658  C CZ2 . TRP A 376  ? 0.3774 0.2960 0.3671 -0.0116 0.0061  0.0779  374  TRP A CZ2 
2659  C CZ3 . TRP A 376  ? 0.3959 0.3092 0.3834 -0.0080 0.0044  0.0649  374  TRP A CZ3 
2660  C CH2 . TRP A 376  ? 0.3792 0.2936 0.3678 -0.0095 0.0041  0.0725  374  TRP A CH2 
2661  N N   . ASP A 377  ? 0.3245 0.2484 0.2992 -0.0058 0.0134  0.0541  375  ASP A N   
2662  C CA  . ASP A 377  ? 0.3596 0.2825 0.3291 -0.0038 0.0136  0.0527  375  ASP A CA  
2663  C C   . ASP A 377  ? 0.3517 0.2782 0.3150 -0.0025 0.0169  0.0525  375  ASP A C   
2664  O O   . ASP A 377  ? 0.3709 0.2984 0.3301 -0.0014 0.0177  0.0538  375  ASP A O   
2665  C CB  . ASP A 377  ? 0.3919 0.3127 0.3617 -0.0028 0.0117  0.0469  375  ASP A CB  
2666  C CG  . ASP A 377  ? 0.5220 0.4395 0.4985 -0.0035 0.0082  0.0453  375  ASP A CG  
2667  O OD1 . ASP A 377  ? 0.5708 0.4857 0.5512 -0.0044 0.0063  0.0489  375  ASP A OD1 
2668  O OD2 . ASP A 377  ? 0.5927 0.5106 0.5707 -0.0031 0.0070  0.0401  375  ASP A OD2 
2669  N N   . ALA A 378  ? 0.3408 0.2696 0.3038 -0.0025 0.0184  0.0506  376  ALA A N   
2670  C CA  . ALA A 378  ? 0.3329 0.2645 0.2914 -0.0010 0.0210  0.0497  376  ALA A CA  
2671  C C   . ALA A 378  ? 0.3389 0.2743 0.2959 -0.0009 0.0231  0.0536  376  ALA A C   
2672  O O   . ALA A 378  ? 0.3206 0.2581 0.2733 0.0009  0.0246  0.0529  376  ALA A O   
2673  C CB  . ALA A 378  ? 0.3402 0.2732 0.2998 -0.0012 0.0217  0.0475  376  ALA A CB  
2674  N N   . GLU A 379  ? 0.3098 0.2468 0.2705 -0.0027 0.0232  0.0574  377  GLU A N   
2675  C CA  . GLU A 379  ? 0.3119 0.2541 0.2714 -0.0027 0.0253  0.0614  377  GLU A CA  
2676  C C   . GLU A 379  ? 0.3109 0.2538 0.2673 -0.0022 0.0250  0.0639  377  GLU A C   
2677  O O   . GLU A 379  ? 0.3222 0.2703 0.2747 -0.0010 0.0271  0.0650  377  GLU A O   
2678  C CB  . GLU A 379  ? 0.3177 0.2618 0.2826 -0.0052 0.0252  0.0656  377  GLU A CB  
2679  C CG  . GLU A 379  ? 0.2978 0.2426 0.2661 -0.0058 0.0257  0.0636  377  GLU A CG  
2680  C CD  . GLU A 379  ? 0.3169 0.2659 0.2823 -0.0039 0.0284  0.0616  377  GLU A CD  
2681  O OE1 . GLU A 379  ? 0.3127 0.2655 0.2743 -0.0022 0.0303  0.0619  377  GLU A OE1 
2682  O OE2 . GLU A 379  ? 0.3329 0.2820 0.3005 -0.0040 0.0284  0.0596  377  GLU A OE2 
2683  N N   . ILE A 380  ? 0.3130 0.2511 0.2713 -0.0030 0.0222  0.0648  378  ILE A N   
2684  C CA  . ILE A 380  ? 0.3239 0.2625 0.2796 -0.0026 0.0214  0.0675  378  ILE A CA  
2685  C C   . ILE A 380  ? 0.3588 0.2984 0.3081 0.0001  0.0225  0.0635  378  ILE A C   
2686  O O   . ILE A 380  ? 0.3270 0.2716 0.2721 0.0012  0.0239  0.0652  378  ILE A O   
2687  C CB  . ILE A 380  ? 0.3481 0.2806 0.3082 -0.0036 0.0177  0.0685  378  ILE A CB  
2688  C CG1 . ILE A 380  ? 0.3512 0.2825 0.3188 -0.0064 0.0161  0.0724  378  ILE A CG1 
2689  C CG2 . ILE A 380  ? 0.3497 0.2826 0.3070 -0.0029 0.0165  0.0713  378  ILE A CG2 
2690  C CD1 . ILE A 380  ? 0.3533 0.2904 0.3216 -0.0082 0.0176  0.0795  378  ILE A CD1 
2691  N N   . LYS A 381  ? 0.3237 0.2594 0.2726 0.0012  0.0217  0.0581  379  LYS A N   
2692  C CA  . LYS A 381  ? 0.3545 0.2904 0.2984 0.0034  0.0223  0.0542  379  LYS A CA  
2693  C C   . LYS A 381  ? 0.3521 0.2934 0.2930 0.0049  0.0251  0.0531  379  LYS A C   
2694  O O   . LYS A 381  ? 0.3163 0.2605 0.2529 0.0066  0.0258  0.0521  379  LYS A O   
2695  C CB  . LYS A 381  ? 0.3267 0.2583 0.2717 0.0037  0.0211  0.0494  379  LYS A CB  
2696  C CG  . LYS A 381  ? 0.3311 0.2628 0.2722 0.0057  0.0215  0.0454  379  LYS A CG  
2697  C CD  . LYS A 381  ? 0.3674 0.2958 0.3101 0.0055  0.0200  0.0416  379  LYS A CD  
2698  C CE  . LYS A 381  ? 0.3357 0.2639 0.2754 0.0070  0.0200  0.0382  379  LYS A CE  
2699  N NZ  . LYS A 381  ? 0.3503 0.2767 0.2917 0.0065  0.0190  0.0351  379  LYS A NZ  
2700  N N   . ARG A 382  ? 0.3338 0.2767 0.2771 0.0043  0.0265  0.0531  380  ARG A N   
2701  C CA  . ARG A 382  ? 0.3339 0.2815 0.2754 0.0060  0.0289  0.0512  380  ARG A CA  
2702  C C   . ARG A 382  ? 0.3304 0.2852 0.2693 0.0067  0.0306  0.0541  380  ARG A C   
2703  O O   . ARG A 382  ? 0.3357 0.2945 0.2710 0.0090  0.0318  0.0513  380  ARG A O   
2704  C CB  . ARG A 382  ? 0.3764 0.3244 0.3217 0.0053  0.0298  0.0510  380  ARG A CB  
2705  C CG  . ARG A 382  ? 0.4283 0.3816 0.3732 0.0071  0.0320  0.0493  380  ARG A CG  
2706  C CD  . ARG A 382  ? 0.5863 0.5368 0.5317 0.0086  0.0316  0.0447  380  ARG A CD  
2707  N NE  . ARG A 382  ? 0.5647 0.5126 0.5071 0.0100  0.0305  0.0416  380  ARG A NE  
2708  C CZ  . ARG A 382  ? 0.6245 0.5684 0.5678 0.0104  0.0292  0.0385  380  ARG A CZ  
2709  N NH1 . ARG A 382  ? 0.7079 0.6499 0.6547 0.0096  0.0288  0.0383  380  ARG A NH1 
2710  N NH2 . ARG A 382  ? 0.6334 0.5754 0.5743 0.0115  0.0282  0.0358  380  ARG A NH2 
2711  N N   . ALA A 383  ? 0.3158 0.2729 0.2565 0.0046  0.0306  0.0597  381  ALA A N   
2712  C CA  . ALA A 383  ? 0.3290 0.2944 0.2672 0.0048  0.0323  0.0634  381  ALA A CA  
2713  C C   . ALA A 383  ? 0.3335 0.3001 0.2666 0.0063  0.0315  0.0629  381  ALA A C   
2714  O O   . ALA A 383  ? 0.3589 0.3334 0.2880 0.0080  0.0332  0.0625  381  ALA A O   
2715  C CB  . ALA A 383  ? 0.3203 0.2873 0.2623 0.0018  0.0319  0.0705  381  ALA A CB  
2716  N N   . GLN A 384  ? 0.3368 0.2965 0.2703 0.0058  0.0288  0.0627  382  GLN A N   
2717  C CA  . GLN A 384  ? 0.3375 0.2981 0.2665 0.0072  0.0278  0.0621  382  GLN A CA  
2718  C C   . GLN A 384  ? 0.3403 0.3021 0.2656 0.0101  0.0286  0.0553  382  GLN A C   
2719  O O   . GLN A 384  ? 0.3577 0.3258 0.2786 0.0119  0.0294  0.0544  382  GLN A O   
2720  C CB  . GLN A 384  ? 0.3408 0.2937 0.2720 0.0062  0.0246  0.0630  382  GLN A CB  
2721  C CG  . GLN A 384  ? 0.3067 0.2584 0.2421 0.0035  0.0230  0.0699  382  GLN A CG  
2722  C CD  . GLN A 384  ? 0.3464 0.2909 0.2844 0.0030  0.0194  0.0700  382  GLN A CD  
2723  O OE1 . GLN A 384  ? 0.3839 0.3236 0.3214 0.0043  0.0184  0.0646  382  GLN A OE1 
2724  N NE2 . GLN A 384  ? 0.3639 0.3078 0.3053 0.0012  0.0174  0.0763  382  GLN A NE2 
2725  N N   . LEU A 385  ? 0.3159 0.2721 0.2433 0.0106  0.0283  0.0506  383  LEU A N   
2726  C CA  . LEU A 385  ? 0.3318 0.2885 0.2572 0.0131  0.0287  0.0445  383  LEU A CA  
2727  C C   . LEU A 385  ? 0.3546 0.3196 0.2784 0.0150  0.0311  0.0430  383  LEU A C   
2728  O O   . LEU A 385  ? 0.3771 0.3455 0.2977 0.0174  0.0312  0.0389  383  LEU A O   
2729  C CB  . LEU A 385  ? 0.3704 0.3208 0.2994 0.0127  0.0280  0.0411  383  LEU A CB  
2730  C CG  . LEU A 385  ? 0.3599 0.3034 0.2900 0.0117  0.0257  0.0402  383  LEU A CG  
2731  C CD1 . LEU A 385  ? 0.4095 0.3490 0.3430 0.0111  0.0254  0.0376  383  LEU A CD1 
2732  C CD2 . LEU A 385  ? 0.4192 0.3625 0.3459 0.0132  0.0245  0.0375  383  LEU A CD2 
2733  N N   . ASP A 386  ? 0.3277 0.2964 0.2537 0.0141  0.0329  0.0458  384  ASP A N   
2734  C CA  . ASP A 386  ? 0.3488 0.3257 0.2741 0.0162  0.0352  0.0435  384  ASP A CA  
2735  C C   . ASP A 386  ? 0.3508 0.3381 0.2722 0.0166  0.0367  0.0467  384  ASP A C   
2736  O O   . ASP A 386  ? 0.3599 0.3560 0.2803 0.0186  0.0388  0.0446  384  ASP A O   
2737  C CB  . ASP A 386  ? 0.3351 0.3123 0.2651 0.0152  0.0366  0.0448  384  ASP A CB  
2738  C CG  . ASP A 386  ? 0.4718 0.4413 0.4056 0.0154  0.0354  0.0408  384  ASP A CG  
2739  O OD1 . ASP A 386  ? 0.4856 0.4503 0.4185 0.0165  0.0338  0.0369  384  ASP A OD1 
2740  O OD2 . ASP A 386  ? 0.4578 0.4265 0.3955 0.0144  0.0360  0.0421  384  ASP A OD2 
2741  N N   . GLY A 387  ? 0.3486 0.3355 0.2679 0.0149  0.0355  0.0517  385  GLY A N   
2742  C CA  . GLY A 387  ? 0.3638 0.3613 0.2792 0.0150  0.0366  0.0557  385  GLY A CA  
2743  C C   . GLY A 387  ? 0.3704 0.3765 0.2874 0.0137  0.0391  0.0605  385  GLY A C   
2744  O O   . GLY A 387  ? 0.3475 0.3657 0.2612 0.0150  0.0411  0.0610  385  GLY A O   
2745  N N   . LEU A 388  ? 0.3586 0.3597 0.2809 0.0111  0.0390  0.0640  386  LEU A N   
2746  C CA  . LEU A 388  ? 0.3786 0.3880 0.3033 0.0098  0.0414  0.0680  386  LEU A CA  
2747  C C   . LEU A 388  ? 0.3811 0.3954 0.3059 0.0067  0.0412  0.0773  386  LEU A C   
2748  O O   . LEU A 388  ? 0.3919 0.4015 0.3159 0.0054  0.0388  0.0808  386  LEU A O   
2749  C CB  . LEU A 388  ? 0.3239 0.3266 0.2545 0.0086  0.0414  0.0671  386  LEU A CB  
2750  C CG  . LEU A 388  ? 0.3595 0.3588 0.2901 0.0118  0.0416  0.0586  386  LEU A CG  
2751  C CD1 . LEU A 388  ? 0.3583 0.3516 0.2944 0.0107  0.0413  0.0578  386  LEU A CD1 
2752  C CD2 . LEU A 388  ? 0.3681 0.3782 0.2960 0.0151  0.0439  0.0543  386  LEU A CD2 
2753  N N   . ALA A 389  ? 0.3991 0.4235 0.3255 0.0055  0.0436  0.0816  387  ALA A N   
2754  C CA  . ALA A 389  ? 0.3743 0.4063 0.3005 0.0026  0.0437  0.0910  387  ALA A CA  
2755  C C   . ALA A 389  ? 0.3899 0.4115 0.3217 -0.0013 0.0406  0.0974  387  ALA A C   
2756  O O   . ALA A 389  ? 0.3826 0.4050 0.3141 -0.0032 0.0388  0.1040  387  ALA A O   
2757  C CB  . ALA A 389  ? 0.4322 0.4777 0.3598 0.0019  0.0471  0.0942  387  ALA A CB  
2758  N N   . ASP A 390  ? 0.3769 0.3888 0.3142 -0.0023 0.0395  0.0951  388  ASP A N   
2759  C CA  . ASP A 390  ? 0.3544 0.3571 0.2980 -0.0058 0.0365  0.1003  388  ASP A CA  
2760  C C   . ASP A 390  ? 0.3465 0.3383 0.2939 -0.0055 0.0353  0.0943  388  ASP A C   
2761  O O   . ASP A 390  ? 0.3060 0.2971 0.2511 -0.0028 0.0367  0.0872  388  ASP A O   
2762  C CB  . ASP A 390  ? 0.3608 0.3705 0.3093 -0.0096 0.0371  0.1093  388  ASP A CB  
2763  C CG  . ASP A 390  ? 0.4078 0.4106 0.3623 -0.0132 0.0333  0.1165  388  ASP A CG  
2764  O OD1 . ASP A 390  ? 0.3998 0.3903 0.3576 -0.0133 0.0302  0.1132  388  ASP A OD1 
2765  O OD2 . ASP A 390  ? 0.4816 0.4915 0.4377 -0.0159 0.0331  0.1255  388  ASP A OD2 
2766  N N   . PHE A 391  ? 0.3131 0.2970 0.2668 -0.0082 0.0324  0.0973  389  PHE A N   
2767  C CA  . PHE A 391  ? 0.3284 0.3038 0.2855 -0.0080 0.0314  0.0917  389  PHE A CA  
2768  C C   . PHE A 391  ? 0.3444 0.3234 0.3063 -0.0096 0.0330  0.0931  389  PHE A C   
2769  O O   . PHE A 391  ? 0.3479 0.3337 0.3125 -0.0120 0.0339  0.0997  389  PHE A O   
2770  C CB  . PHE A 391  ? 0.3302 0.2951 0.2918 -0.0095 0.0273  0.0923  389  PHE A CB  
2771  C CG  . PHE A 391  ? 0.2937 0.2551 0.2513 -0.0079 0.0255  0.0911  389  PHE A CG  
2772  C CD1 . PHE A 391  ? 0.3153 0.2730 0.2685 -0.0051 0.0256  0.0838  389  PHE A CD1 
2773  C CD2 . PHE A 391  ? 0.3717 0.3341 0.3302 -0.0094 0.0236  0.0976  389  PHE A CD2 
2774  C CE1 . PHE A 391  ? 0.3406 0.2956 0.2903 -0.0036 0.0239  0.0825  389  PHE A CE1 
2775  C CE2 . PHE A 391  ? 0.3599 0.3194 0.3148 -0.0078 0.0218  0.0965  389  PHE A CE2 
2776  C CZ  . PHE A 391  ? 0.3246 0.2805 0.2750 -0.0048 0.0221  0.0887  389  PHE A CZ  
2777  N N   . PRO A 392  ? 0.3351 0.3105 0.2981 -0.0084 0.0334  0.0874  390  PRO A N   
2778  C CA  . PRO A 392  ? 0.3228 0.3010 0.2910 -0.0101 0.0344  0.0886  390  PRO A CA  
2779  C C   . PRO A 392  ? 0.3628 0.3339 0.3383 -0.0131 0.0312  0.0902  390  PRO A C   
2780  O O   . PRO A 392  ? 0.3349 0.3071 0.3152 -0.0145 0.0315  0.0904  390  PRO A O   
2781  C CB  . PRO A 392  ? 0.2802 0.2578 0.2461 -0.0071 0.0359  0.0814  390  PRO A CB  
2782  C CG  . PRO A 392  ? 0.3388 0.3080 0.3016 -0.0055 0.0337  0.0767  390  PRO A CG  
2783  C CD  . PRO A 392  ? 0.3290 0.2988 0.2885 -0.0056 0.0330  0.0799  390  PRO A CD  
2784  N N   . VAL A 393  ? 0.3583 0.3222 0.3350 -0.0138 0.0280  0.0908  391  VAL A N   
2785  C CA  . VAL A 393  ? 0.3559 0.3126 0.3400 -0.0163 0.0244  0.0915  391  VAL A CA  
2786  C C   . VAL A 393  ? 0.3197 0.2748 0.3067 -0.0183 0.0220  0.0977  391  VAL A C   
2787  O O   . VAL A 393  ? 0.3403 0.2984 0.3223 -0.0172 0.0228  0.1001  391  VAL A O   
2788  C CB  . VAL A 393  ? 0.3260 0.2748 0.3097 -0.0146 0.0223  0.0842  391  VAL A CB  
2789  C CG1 . VAL A 393  ? 0.3212 0.2715 0.3034 -0.0132 0.0242  0.0790  391  VAL A CG1 
2790  C CG2 . VAL A 393  ? 0.3284 0.2745 0.3058 -0.0121 0.0220  0.0817  391  VAL A CG2 
2791  N N   . PHE A 394  ? 0.3207 0.2712 0.3164 -0.0212 0.0186  0.1004  392  PHE A N   
2792  C CA  . PHE A 394  ? 0.3414 0.2887 0.3416 -0.0232 0.0153  0.1064  392  PHE A CA  
2793  C C   . PHE A 394  ? 0.3519 0.2918 0.3495 -0.0208 0.0128  0.1019  392  PHE A C   
2794  O O   . PHE A 394  ? 0.3457 0.2820 0.3402 -0.0184 0.0130  0.0942  392  PHE A O   
2795  C CB  . PHE A 394  ? 0.3253 0.2688 0.3367 -0.0268 0.0119  0.1096  392  PHE A CB  
2796  C CG  . PHE A 394  ? 0.3623 0.3134 0.3768 -0.0293 0.0142  0.1144  392  PHE A CG  
2797  C CD1 . PHE A 394  ? 0.3827 0.3425 0.3960 -0.0311 0.0164  0.1228  392  PHE A CD1 
2798  C CD2 . PHE A 394  ? 0.3734 0.3242 0.3918 -0.0299 0.0145  0.1104  392  PHE A CD2 
2799  C CE1 . PHE A 394  ? 0.3754 0.3435 0.3917 -0.0334 0.0188  0.1271  392  PHE A CE1 
2800  C CE2 . PHE A 394  ? 0.3282 0.2865 0.3497 -0.0322 0.0166  0.1147  392  PHE A CE2 
2801  C CZ  . PHE A 394  ? 0.3787 0.3456 0.3992 -0.0339 0.0189  0.1230  392  PHE A CZ  
2802  N N   . THR A 395  ? 0.3523 0.2907 0.3513 -0.0217 0.0105  0.1073  393  THR A N   
2803  C CA  . THR A 395  ? 0.3932 0.3250 0.3906 -0.0195 0.0078  0.1037  393  THR A CA  
2804  C C   . THR A 395  ? 0.3871 0.3104 0.3947 -0.0211 0.0023  0.1046  393  THR A C   
2805  O O   . THR A 395  ? 0.4074 0.3251 0.4150 -0.0192 -0.0004 0.1010  393  THR A O   
2806  C CB  . THR A 395  ? 0.3813 0.3176 0.3720 -0.0185 0.0089  0.1081  393  THR A CB  
2807  O OG1 . THR A 395  ? 0.3853 0.3263 0.3799 -0.0216 0.0083  0.1183  393  THR A OG1 
2808  C CG2 . THR A 395  ? 0.3901 0.3336 0.3706 -0.0159 0.0136  0.1046  393  THR A CG2 
2809  N N   . ARG A 396  ? 0.4041 0.3265 0.4210 -0.0244 0.0002  0.1092  394  ARG A N   
2810  C CA  . ARG A 396  ? 0.4261 0.3400 0.4544 -0.0258 -0.0055 0.1089  394  ARG A CA  
2811  C C   . ARG A 396  ? 0.4216 0.3335 0.4559 -0.0268 -0.0062 0.1038  394  ARG A C   
2812  O O   . ARG A 396  ? 0.4352 0.3525 0.4700 -0.0288 -0.0037 0.1066  394  ARG A O   
2813  C CB  . ARG A 396  ? 0.4182 0.3320 0.4544 -0.0294 -0.0084 0.1197  394  ARG A CB  
2814  C CG  . ARG A 396  ? 0.4541 0.3703 0.4854 -0.0287 -0.0084 0.1257  394  ARG A CG  
2815  C CD  . ARG A 396  ? 0.4517 0.3662 0.4931 -0.0324 -0.0126 0.1365  394  ARG A CD  
2816  N NE  . ARG A 396  ? 0.5350 0.4542 0.5705 -0.0320 -0.0120 0.1434  394  ARG A NE  
2817  C CZ  . ARG A 396  ? 0.5836 0.4993 0.6257 -0.0335 -0.0166 0.1507  394  ARG A CZ  
2818  N NH1 . ARG A 396  ? 0.6074 0.5151 0.6625 -0.0351 -0.0222 0.1507  394  ARG A NH1 
2819  N NH2 . ARG A 396  ? 0.5123 0.4341 0.5473 -0.0326 -0.0155 0.1558  394  ARG A NH2 
2820  N N   . LYS A 397  ? 0.3778 0.2829 0.4167 -0.0253 -0.0097 0.0960  395  LYS A N   
2821  C CA  . LYS A 397  ? 0.4196 0.3234 0.4639 -0.0259 -0.0108 0.0901  395  LYS A CA  
2822  C C   . LYS A 397  ? 0.4127 0.3166 0.4677 -0.0300 -0.0129 0.0965  395  LYS A C   
2823  O O   . LYS A 397  ? 0.3841 0.2911 0.4409 -0.0313 -0.0116 0.0950  395  LYS A O   
2824  C CB  . LYS A 397  ? 0.4561 0.3533 0.5050 -0.0237 -0.0150 0.0812  395  LYS A CB  
2825  C CG  . LYS A 397  ? 0.4952 0.3928 0.5467 -0.0232 -0.0155 0.0730  395  LYS A CG  
2826  C CD  . LYS A 397  ? 0.4874 0.3811 0.5526 -0.0258 -0.0204 0.0732  395  LYS A CD  
2827  C CE  . LYS A 397  ? 0.4925 0.3880 0.5597 -0.0252 -0.0208 0.0645  395  LYS A CE  
2828  N NZ  . LYS A 397  ? 0.4937 0.3867 0.5740 -0.0282 -0.0250 0.0653  395  LYS A NZ  
2829  N N   . ILE A 398  ? 0.3999 0.3005 0.4623 -0.0323 -0.0164 0.1041  396  ILE A N   
2830  C CA  . ILE A 398  ? 0.4045 0.3048 0.4784 -0.0366 -0.0190 0.1107  396  ILE A CA  
2831  C C   . ILE A 398  ? 0.3678 0.2778 0.4371 -0.0389 -0.0139 0.1174  396  ILE A C   
2832  O O   . ILE A 398  ? 0.3821 0.2939 0.4590 -0.0421 -0.0146 0.1202  396  ILE A O   
2833  C CB  . ILE A 398  ? 0.4344 0.3290 0.5180 -0.0386 -0.0243 0.1180  396  ILE A CB  
2834  C CG1 . ILE A 398  ? 0.4592 0.3507 0.5579 -0.0429 -0.0287 0.1227  396  ILE A CG1 
2835  C CG2 . ILE A 398  ? 0.4161 0.3164 0.4925 -0.0392 -0.0215 0.1278  396  ILE A CG2 
2836  C CD1 . ILE A 398  ? 0.4996 0.3831 0.6103 -0.0444 -0.0354 0.1279  396  ILE A CD1 
2837  N N   . HIS A 399  ? 0.3738 0.2906 0.4312 -0.0373 -0.0089 0.1198  397  HIS A N   
2838  C CA  . HIS A 399  ? 0.3725 0.2996 0.4252 -0.0387 -0.0039 0.1248  397  HIS A CA  
2839  C C   . HIS A 399  ? 0.3558 0.2851 0.4066 -0.0378 -0.0014 0.1175  397  HIS A C   
2840  O O   . HIS A 399  ? 0.3536 0.2881 0.4081 -0.0403 0.0000  0.1208  397  HIS A O   
2841  C CB  . HIS A 399  ? 0.3823 0.3162 0.4226 -0.0365 0.0006  0.1271  397  HIS A CB  
2842  C CG  . HIS A 399  ? 0.3805 0.3150 0.4220 -0.0379 -0.0012 0.1360  397  HIS A CG  
2843  N ND1 . HIS A 399  ? 0.4431 0.3825 0.4743 -0.0357 0.0015  0.1376  397  HIS A ND1 
2844  C CD2 . HIS A 399  ? 0.4245 0.3556 0.4765 -0.0415 -0.0057 0.1442  397  HIS A CD2 
2845  C CE1 . HIS A 399  ? 0.4346 0.3742 0.4696 -0.0377 -0.0011 0.1465  397  HIS A CE1 
2846  N NE2 . HIS A 399  ? 0.4108 0.3451 0.4586 -0.0413 -0.0056 0.1509  397  HIS A NE2 
2847  N N   . THR A 400  ? 0.3280 0.2539 0.3733 -0.0342 -0.0010 0.1079  398  THR A N   
2848  C CA  . THR A 400  ? 0.3317 0.2594 0.3757 -0.0332 0.0006  0.1010  398  THR A CA  
2849  C C   . THR A 400  ? 0.3531 0.2777 0.4092 -0.0360 -0.0033 0.1002  398  THR A C   
2850  O O   . THR A 400  ? 0.3669 0.2959 0.4243 -0.0371 -0.0016 0.0993  398  THR A O   
2851  C CB  . THR A 400  ? 0.3494 0.2736 0.3867 -0.0293 0.0008  0.0917  398  THR A CB  
2852  O OG1 . THR A 400  ? 0.3697 0.2977 0.3961 -0.0268 0.0047  0.0923  398  THR A OG1 
2853  C CG2 . THR A 400  ? 0.3031 0.2290 0.3403 -0.0285 0.0016  0.0848  398  THR A CG2 
2854  N N   . ASP A 401  ? 0.3654 0.2824 0.4308 -0.0372 -0.0087 0.1001  399  ASP A N   
2855  C CA  . ASP A 401  ? 0.3420 0.2557 0.4201 -0.0399 -0.0131 0.0991  399  ASP A CA  
2856  C C   . ASP A 401  ? 0.3729 0.2918 0.4572 -0.0443 -0.0123 0.1086  399  ASP A C   
2857  O O   . ASP A 401  ? 0.3665 0.2876 0.4563 -0.0462 -0.0126 0.1072  399  ASP A O   
2858  C CB  . ASP A 401  ? 0.3788 0.2832 0.4667 -0.0401 -0.0195 0.0975  399  ASP A CB  
2859  C CG  . ASP A 401  ? 0.4478 0.3478 0.5324 -0.0360 -0.0211 0.0864  399  ASP A CG  
2860  O OD1 . ASP A 401  ? 0.4354 0.3390 0.5136 -0.0339 -0.0185 0.0792  399  ASP A OD1 
2861  O OD2 . ASP A 401  ? 0.4597 0.3531 0.5486 -0.0349 -0.0251 0.0851  399  ASP A OD2 
2862  N N   . VAL A 402  ? 0.3836 0.3050 0.4672 -0.0462 -0.0113 0.1184  400  VAL A N   
2863  C CA  . VAL A 402  ? 0.3514 0.2796 0.4404 -0.0505 -0.0100 0.1281  400  VAL A CA  
2864  C C   . VAL A 402  ? 0.3488 0.2866 0.4298 -0.0497 -0.0042 0.1268  400  VAL A C   
2865  O O   . VAL A 402  ? 0.3408 0.2828 0.4281 -0.0525 -0.0039 0.1291  400  VAL A O   
2866  C CB  . VAL A 402  ? 0.3802 0.3111 0.4687 -0.0525 -0.0098 0.1392  400  VAL A CB  
2867  C CG1 . VAL A 402  ? 0.3387 0.2789 0.4320 -0.0571 -0.0078 0.1496  400  VAL A CG1 
2868  C CG2 . VAL A 402  ? 0.4063 0.3271 0.5046 -0.0536 -0.0163 0.1412  400  VAL A CG2 
2869  N N   . SER A 403  ? 0.3320 0.2735 0.4000 -0.0458 0.0003  0.1230  401  SER A N   
2870  C CA  . SER A 403  ? 0.3657 0.3159 0.4266 -0.0444 0.0056  0.1210  401  SER A CA  
2871  C C   . SER A 403  ? 0.4003 0.3491 0.4654 -0.0444 0.0045  0.1141  401  SER A C   
2872  O O   . SER A 403  ? 0.3211 0.2768 0.3878 -0.0457 0.0068  0.1157  401  SER A O   
2873  C CB  . SER A 403  ? 0.3513 0.3034 0.3989 -0.0399 0.0094  0.1165  401  SER A CB  
2874  O OG  . SER A 403  ? 0.3367 0.2964 0.3783 -0.0382 0.0140  0.1140  401  SER A OG  
2875  N N   . TYR A 404  ? 0.3284 0.2692 0.3952 -0.0426 0.0010  0.1061  402  TYR A N   
2876  C CA  . TYR A 404  ? 0.3704 0.3104 0.4411 -0.0425 -0.0005 0.0992  402  TYR A CA  
2877  C C   . TYR A 404  ? 0.3538 0.2947 0.4372 -0.0469 -0.0033 0.1034  402  TYR A C   
2878  O O   . TYR A 404  ? 0.3283 0.2745 0.4133 -0.0478 -0.0019 0.1024  402  TYR A O   
2879  C CB  . TYR A 404  ? 0.3401 0.2723 0.4112 -0.0400 -0.0042 0.0904  402  TYR A CB  
2880  C CG  . TYR A 404  ? 0.3584 0.2917 0.4304 -0.0389 -0.0050 0.0820  402  TYR A CG  
2881  C CD1 . TYR A 404  ? 0.3399 0.2722 0.4230 -0.0415 -0.0089 0.0804  402  TYR A CD1 
2882  C CD2 . TYR A 404  ? 0.3522 0.2878 0.4144 -0.0354 -0.0023 0.0759  402  TYR A CD2 
2883  C CE1 . TYR A 404  ? 0.3711 0.3054 0.4546 -0.0403 -0.0097 0.0727  402  TYR A CE1 
2884  C CE2 . TYR A 404  ? 0.3075 0.2449 0.3702 -0.0344 -0.0031 0.0690  402  TYR A CE2 
2885  C CZ  . TYR A 404  ? 0.2948 0.2319 0.3678 -0.0368 -0.0068 0.0673  402  TYR A CZ  
2886  O OH  . TYR A 404  ? 0.2848 0.2250 0.3578 -0.0358 -0.0076 0.0603  402  TYR A OH  
2887  N N   . ILE A 405  ? 0.3401 0.2759 0.4331 -0.0498 -0.0076 0.1085  403  ILE A N   
2888  C CA  . ILE A 405  ? 0.3714 0.3071 0.4779 -0.0543 -0.0110 0.1124  403  ILE A CA  
2889  C C   . ILE A 405  ? 0.3495 0.2952 0.4558 -0.0572 -0.0069 0.1212  403  ILE A C   
2890  O O   . ILE A 405  ? 0.3334 0.2829 0.4464 -0.0597 -0.0073 0.1216  403  ILE A O   
2891  C CB  . ILE A 405  ? 0.3977 0.3248 0.5154 -0.0567 -0.0170 0.1160  403  ILE A CB  
2892  C CG1 . ILE A 405  ? 0.4361 0.3542 0.5557 -0.0537 -0.0215 0.1054  403  ILE A CG1 
2893  C CG2 . ILE A 405  ? 0.4056 0.3327 0.5381 -0.0619 -0.0207 0.1219  403  ILE A CG2 
2894  C CD1 . ILE A 405  ? 0.4502 0.3591 0.5782 -0.0544 -0.0271 0.1076  403  ILE A CD1 
2895  N N   . ALA A 406  ? 0.3679 0.3191 0.4661 -0.0567 -0.0027 0.1277  404  ALA A N   
2896  C CA  . ALA A 406  ? 0.3664 0.3292 0.4634 -0.0589 0.0017  0.1353  404  ALA A CA  
2897  C C   . ALA A 406  ? 0.3413 0.3106 0.4325 -0.0566 0.0057  0.1296  404  ALA A C   
2898  O O   . ALA A 406  ? 0.3754 0.3526 0.4710 -0.0590 0.0074  0.1333  404  ALA A O   
2899  C CB  . ALA A 406  ? 0.3714 0.3399 0.4596 -0.0580 0.0055  0.1419  404  ALA A CB  
2900  N N   . CYS A 407  ? 0.3643 0.3313 0.4458 -0.0519 0.0073  0.1212  405  CYS A N   
2901  C CA  . CYS A 407  ? 0.3333 0.3060 0.4097 -0.0495 0.0107  0.1160  405  CYS A CA  
2902  C C   . CYS A 407  ? 0.3646 0.3351 0.4494 -0.0511 0.0074  0.1114  405  CYS A C   
2903  O O   . CYS A 407  ? 0.3440 0.3214 0.4296 -0.0513 0.0095  0.1109  405  CYS A O   
2904  C CB  . CYS A 407  ? 0.3314 0.3017 0.3960 -0.0445 0.0128  0.1090  405  CYS A CB  
2905  S SG  . CYS A 407  ? 0.4294 0.4058 0.4835 -0.0425 0.0178  0.1139  405  CYS A SG  
2906  N N   . ALA A 408  ? 0.3703 0.3320 0.4623 -0.0520 0.0020  0.1079  406  ALA A N   
2907  C CA  . ALA A 408  ? 0.3869 0.3472 0.4882 -0.0538 -0.0016 0.1036  406  ALA A CA  
2908  C C   . ALA A 408  ? 0.3442 0.3096 0.4559 -0.0586 -0.0022 0.1112  406  ALA A C   
2909  O O   . ALA A 408  ? 0.3425 0.3121 0.4588 -0.0597 -0.0025 0.1090  406  ALA A O   
2910  C CB  . ALA A 408  ? 0.3741 0.3243 0.4815 -0.0537 -0.0075 0.0980  406  ALA A CB  
2911  N N   . ALA A 409  ? 0.3568 0.3229 0.4726 -0.0617 -0.0023 0.1205  407  ALA A N   
2912  C CA  . ALA A 409  ? 0.3940 0.3662 0.5198 -0.0667 -0.0026 0.1288  407  ALA A CA  
2913  C C   . ALA A 409  ? 0.3729 0.3572 0.4930 -0.0660 0.0032  0.1307  407  ALA A C   
2914  O O   . ALA A 409  ? 0.3451 0.3350 0.4729 -0.0688 0.0030  0.1325  407  ALA A O   
2915  C CB  . ALA A 409  ? 0.3857 0.3573 0.5164 -0.0702 -0.0037 0.1393  407  ALA A CB  
2916  N N   . LYS A 410  ? 0.3279 0.3167 0.4353 -0.0622 0.0083  0.1299  408  LYS A N   
2917  C CA  . LYS A 410  ? 0.2899 0.2902 0.3922 -0.0608 0.0136  0.1307  408  LYS A CA  
2918  C C   . LYS A 410  ? 0.3396 0.3399 0.4418 -0.0588 0.0132  0.1225  408  LYS A C   
2919  O O   . LYS A 410  ? 0.3448 0.3535 0.4503 -0.0599 0.0150  0.1239  408  LYS A O   
2920  C CB  . LYS A 410  ? 0.3056 0.3097 0.3949 -0.0568 0.0184  0.1306  408  LYS A CB  
2921  C CG  . LYS A 410  ? 0.3320 0.3486 0.4163 -0.0550 0.0239  0.1314  408  LYS A CG  
2922  C CD  . LYS A 410  ? 0.3771 0.3955 0.4487 -0.0501 0.0278  0.1284  408  LYS A CD  
2923  C CE  . LYS A 410  ? 0.3729 0.3940 0.4413 -0.0511 0.0291  0.1354  408  LYS A CE  
2924  N NZ  . LYS A 410  ? 0.3511 0.3855 0.4234 -0.0541 0.0321  0.1436  408  LYS A NZ  
2925  N N   . LEU A 411  ? 0.3145 0.3065 0.4129 -0.0558 0.0108  0.1141  409  LEU A N   
2926  C CA  . LEU A 411  ? 0.2953 0.2878 0.3931 -0.0539 0.0102  0.1066  409  LEU A CA  
2927  C C   . LEU A 411  ? 0.3140 0.3068 0.4244 -0.0577 0.0062  0.1065  409  LEU A C   
2928  O O   . LEU A 411  ? 0.2939 0.2927 0.4061 -0.0577 0.0071  0.1046  409  LEU A O   
2929  C CB  . LEU A 411  ? 0.2989 0.2834 0.3903 -0.0503 0.0084  0.0983  409  LEU A CB  
2930  C CG  . LEU A 411  ? 0.3154 0.3010 0.3941 -0.0457 0.0125  0.0960  409  LEU A CG  
2931  C CD1 . LEU A 411  ? 0.3377 0.3148 0.4114 -0.0431 0.0102  0.0897  409  LEU A CD1 
2932  C CD2 . LEU A 411  ? 0.2762 0.2690 0.3509 -0.0434 0.0155  0.0934  409  LEU A CD2 
2933  N N   . LEU A 412  ? 0.3200 0.3061 0.4397 -0.0610 0.0015  0.1083  410  LEU A N   
2934  C CA  . LEU A 412  ? 0.3199 0.3053 0.4527 -0.0648 -0.0031 0.1078  410  LEU A CA  
2935  C C   . LEU A 412  ? 0.3291 0.3239 0.4689 -0.0687 -0.0011 0.1157  410  LEU A C   
2936  O O   . LEU A 412  ? 0.3479 0.3446 0.4974 -0.0714 -0.0039 0.1147  410  LEU A O   
2937  C CB  . LEU A 412  ? 0.3411 0.3166 0.4833 -0.0673 -0.0090 0.1079  410  LEU A CB  
2938  C CG  . LEU A 412  ? 0.3310 0.2982 0.4702 -0.0639 -0.0124 0.0977  410  LEU A CG  
2939  C CD1 . LEU A 412  ? 0.3417 0.2992 0.4902 -0.0659 -0.0180 0.0983  410  LEU A CD1 
2940  C CD2 . LEU A 412  ? 0.3407 0.3099 0.4823 -0.0629 -0.0145 0.0892  410  LEU A CD2 
2941  N N   . ALA A 413  ? 0.2845 0.2859 0.4197 -0.0691 0.0035  0.1235  411  ALA A N   
2942  C CA  . ALA A 413  ? 0.3399 0.3525 0.4803 -0.0722 0.0062  0.1305  411  ALA A CA  
2943  C C   . ALA A 413  ? 0.3491 0.3705 0.4832 -0.0689 0.0104  0.1266  411  ALA A C   
2944  O O   . ALA A 413  ? 0.3506 0.3823 0.4890 -0.0710 0.0128  0.1314  411  ALA A O   
2945  C CB  . ALA A 413  ? 0.3066 0.3248 0.4451 -0.0741 0.0095  0.1406  411  ALA A CB  
2946  N N   . ALA A 414  ? 0.3738 0.3918 0.4985 -0.0640 0.0112  0.1183  412  ALA A N   
2947  C CA  . ALA A 414  ? 0.3557 0.3814 0.4745 -0.0606 0.0149  0.1150  412  ALA A CA  
2948  C C   . ALA A 414  ? 0.3527 0.3748 0.4711 -0.0584 0.0121  0.1062  412  ALA A C   
2949  O O   . ALA A 414  ? 0.2897 0.3153 0.4009 -0.0546 0.0147  0.1023  412  ALA A O   
2950  C CB  . ALA A 414  ? 0.3406 0.3687 0.4470 -0.0563 0.0198  0.1149  412  ALA A CB  
2951  N N   . THR A 415  ? 0.3258 0.3414 0.4521 -0.0609 0.0067  0.1031  413  THR A N   
2952  C CA  . THR A 415  ? 0.3094 0.3230 0.4355 -0.0590 0.0038  0.0947  413  THR A CA  
2953  C C   . THR A 415  ? 0.3618 0.3846 0.4896 -0.0586 0.0053  0.0939  413  THR A C   
2954  O O   . THR A 415  ? 0.3448 0.3680 0.4696 -0.0561 0.0040  0.0875  413  THR A O   
2955  C CB  . THR A 415  ? 0.3490 0.3559 0.4853 -0.0620 -0.0025 0.0914  413  THR A CB  
2956  O OG1 . THR A 415  ? 0.3483 0.3585 0.4971 -0.0670 -0.0043 0.0970  413  THR A OG1 
2957  C CG2 . THR A 415  ? 0.3328 0.3296 0.4673 -0.0616 -0.0047 0.0906  413  THR A CG2 
2958  N N   . ASP A 416  ? 0.3577 0.3888 0.4904 -0.0609 0.0078  0.1004  414  ASP A N   
2959  C CA  . ASP A 416  ? 0.3993 0.4395 0.5337 -0.0601 0.0093  0.0995  414  ASP A CA  
2960  C C   . ASP A 416  ? 0.3695 0.4133 0.4929 -0.0549 0.0136  0.0973  414  ASP A C   
2961  O O   . ASP A 416  ? 0.3844 0.4327 0.5071 -0.0528 0.0136  0.0938  414  ASP A O   
2962  C CB  . ASP A 416  ? 0.4272 0.4763 0.5709 -0.0642 0.0107  0.1069  414  ASP A CB  
2963  C CG  . ASP A 416  ? 0.4692 0.5231 0.6084 -0.0639 0.0157  0.1137  414  ASP A CG  
2964  O OD1 . ASP A 416  ? 0.4719 0.5194 0.6062 -0.0635 0.0160  0.1152  414  ASP A OD1 
2965  O OD2 . ASP A 416  ? 0.5365 0.6013 0.6768 -0.0638 0.0194  0.1173  414  ASP A OD2 
2966  N N   . VAL A 417  ? 0.3593 0.4008 0.4741 -0.0525 0.0168  0.0989  415  VAL A N   
2967  C CA  . VAL A 417  ? 0.3804 0.4251 0.4858 -0.0475 0.0206  0.0968  415  VAL A CA  
2968  C C   . VAL A 417  ? 0.3252 0.3614 0.4210 -0.0440 0.0201  0.0919  415  VAL A C   
2969  O O   . VAL A 417  ? 0.3303 0.3680 0.4195 -0.0400 0.0221  0.0890  415  VAL A O   
2970  C CB  . VAL A 417  ? 0.3813 0.4337 0.4846 -0.0470 0.0256  0.1024  415  VAL A CB  
2971  C CG1 . VAL A 417  ? 0.4359 0.4989 0.5483 -0.0500 0.0266  0.1069  415  VAL A CG1 
2972  C CG2 . VAL A 417  ? 0.3879 0.4358 0.4889 -0.0486 0.0262  0.1064  415  VAL A CG2 
2973  N N   . VAL A 418  ? 0.3123 0.3398 0.4075 -0.0453 0.0176  0.0910  416  VAL A N   
2974  C CA  . VAL A 418  ? 0.2859 0.3058 0.3729 -0.0422 0.0166  0.0859  416  VAL A CA  
2975  C C   . VAL A 418  ? 0.2793 0.2930 0.3707 -0.0440 0.0115  0.0815  416  VAL A C   
2976  O O   . VAL A 418  ? 0.3166 0.3299 0.4174 -0.0478 0.0085  0.0829  416  VAL A O   
2977  C CB  . VAL A 418  ? 0.2785 0.2940 0.3586 -0.0409 0.0189  0.0881  416  VAL A CB  
2978  C CG1 . VAL A 418  ? 0.2989 0.3210 0.3735 -0.0382 0.0239  0.0907  416  VAL A CG1 
2979  C CG2 . VAL A 418  ? 0.2824 0.2944 0.3682 -0.0449 0.0172  0.0927  416  VAL A CG2 
2980  N N   . PHE A 419  ? 0.2609 0.2700 0.3458 -0.0413 0.0103  0.0759  417  PHE A N   
2981  C CA  . PHE A 419  ? 0.2698 0.2737 0.3575 -0.0421 0.0056  0.0705  417  PHE A CA  
2982  C C   . PHE A 419  ? 0.2547 0.2507 0.3379 -0.0412 0.0052  0.0696  417  PHE A C   
2983  O O   . PHE A 419  ? 0.2741 0.2681 0.3483 -0.0380 0.0067  0.0669  417  PHE A O   
2984  C CB  . PHE A 419  ? 0.2798 0.2866 0.3638 -0.0397 0.0044  0.0647  417  PHE A CB  
2985  C CG  . PHE A 419  ? 0.3040 0.3071 0.3896 -0.0400 -0.0001 0.0581  417  PHE A CG  
2986  C CD1 . PHE A 419  ? 0.2935 0.2957 0.3892 -0.0431 -0.0043 0.0563  417  PHE A CD1 
2987  C CD2 . PHE A 419  ? 0.2735 0.2747 0.3511 -0.0371 -0.0003 0.0536  417  PHE A CD2 
2988  C CE1 . PHE A 419  ? 0.3077 0.3074 0.4054 -0.0430 -0.0087 0.0492  417  PHE A CE1 
2989  C CE2 . PHE A 419  ? 0.2524 0.2519 0.3316 -0.0371 -0.0044 0.0470  417  PHE A CE2 
2990  C CZ  . PHE A 419  ? 0.3096 0.3084 0.3988 -0.0398 -0.0086 0.0444  417  PHE A CZ  
2991  N N   . PRO A 420  ? 0.2698 0.2609 0.3591 -0.0440 0.0031  0.0719  418  PRO A N   
2992  C CA  . PRO A 420  ? 0.2785 0.2621 0.3636 -0.0429 0.0026  0.0713  418  PRO A CA  
2993  C C   . PRO A 420  ? 0.2911 0.2703 0.3753 -0.0415 -0.0011 0.0633  418  PRO A C   
2994  O O   . PRO A 420  ? 0.2567 0.2367 0.3477 -0.0428 -0.0050 0.0590  418  PRO A O   
2995  C CB  . PRO A 420  ? 0.2399 0.2204 0.3337 -0.0468 0.0009  0.0769  418  PRO A CB  
2996  C CG  . PRO A 420  ? 0.2811 0.2686 0.3822 -0.0497 0.0017  0.0817  418  PRO A CG  
2997  C CD  . PRO A 420  ? 0.2895 0.2817 0.3902 -0.0484 0.0010  0.0761  418  PRO A CD  
2998  N N   . GLN A 421  ? 0.2489 0.2241 0.3248 -0.0387 0.0000  0.0613  419  GLN A N   
2999  C CA  . GLN A 421  ? 0.2659 0.2378 0.3394 -0.0368 -0.0028 0.0539  419  GLN A CA  
3000  C C   . GLN A 421  ? 0.2757 0.2403 0.3475 -0.0363 -0.0034 0.0546  419  GLN A C   
3001  O O   . GLN A 421  ? 0.2898 0.2533 0.3535 -0.0344 0.0000  0.0572  419  GLN A O   
3002  C CB  . GLN A 421  ? 0.2774 0.2535 0.3415 -0.0336 -0.0005 0.0508  419  GLN A CB  
3003  C CG  . GLN A 421  ? 0.2918 0.2755 0.3574 -0.0340 0.0002  0.0512  419  GLN A CG  
3004  C CD  . GLN A 421  ? 0.3014 0.2890 0.3581 -0.0310 0.0031  0.0506  419  GLN A CD  
3005  O OE1 . GLN A 421  ? 0.2830 0.2700 0.3341 -0.0295 0.0067  0.0543  419  GLN A OE1 
3006  N NE2 . GLN A 421  ? 0.3151 0.3070 0.3707 -0.0301 0.0012  0.0459  419  GLN A NE2 
3007  N N   . PHE A 422  ? 0.2756 0.2352 0.3556 -0.0379 -0.0078 0.0523  420  PHE A N   
3008  C CA  . PHE A 422  ? 0.3226 0.2750 0.4031 -0.0378 -0.0089 0.0539  420  PHE A CA  
3009  C C   . PHE A 422  ? 0.3042 0.2539 0.3800 -0.0348 -0.0106 0.0463  420  PHE A C   
3010  O O   . PHE A 422  ? 0.3129 0.2608 0.3949 -0.0348 -0.0150 0.0398  420  PHE A O   
3011  C CB  . PHE A 422  ? 0.3416 0.2897 0.4349 -0.0413 -0.0132 0.0565  420  PHE A CB  
3012  C CG  . PHE A 422  ? 0.3002 0.2519 0.3980 -0.0446 -0.0113 0.0646  420  PHE A CG  
3013  C CD1 . PHE A 422  ? 0.3264 0.2797 0.4190 -0.0448 -0.0071 0.0725  420  PHE A CD1 
3014  C CD2 . PHE A 422  ? 0.3123 0.2672 0.4193 -0.0473 -0.0137 0.0642  420  PHE A CD2 
3015  C CE1 . PHE A 422  ? 0.3377 0.2961 0.4342 -0.0477 -0.0051 0.0799  420  PHE A CE1 
3016  C CE2 . PHE A 422  ? 0.3422 0.3016 0.4537 -0.0504 -0.0118 0.0719  420  PHE A CE2 
3017  C CZ  . PHE A 422  ? 0.3201 0.2815 0.4262 -0.0506 -0.0074 0.0799  420  PHE A CZ  
3018  N N   . ALA A 423  ? 0.3075 0.2574 0.3727 -0.0321 -0.0070 0.0469  421  ALA A N   
3019  C CA  . ALA A 423  ? 0.3359 0.2846 0.3958 -0.0293 -0.0079 0.0403  421  ALA A CA  
3020  C C   . ALA A 423  ? 0.3358 0.2770 0.3983 -0.0291 -0.0101 0.0406  421  ALA A C   
3021  O O   . ALA A 423  ? 0.3529 0.2914 0.4116 -0.0290 -0.0077 0.0464  421  ALA A O   
3022  C CB  . ALA A 423  ? 0.3274 0.2795 0.3758 -0.0268 -0.0034 0.0412  421  ALA A CB  
3023  N N   . THR A 424  ? 0.3260 0.2643 0.3952 -0.0289 -0.0148 0.0343  422  THR A N   
3024  C CA  . THR A 424  ? 0.3358 0.2669 0.4082 -0.0284 -0.0172 0.0343  422  THR A CA  
3025  C C   . THR A 424  ? 0.3933 0.3229 0.4721 -0.0271 -0.0224 0.0249  422  THR A C   
3026  O O   . THR A 424  ? 0.3275 0.2601 0.4128 -0.0280 -0.0252 0.0200  422  THR A O   
3027  C CB  . THR A 424  ? 0.3867 0.3128 0.4670 -0.0315 -0.0185 0.0423  422  THR A CB  
3028  O OG1 . THR A 424  ? 0.4157 0.3348 0.4989 -0.0309 -0.0211 0.0427  422  THR A OG1 
3029  C CG2 . THR A 424  ? 0.3799 0.3061 0.4726 -0.0344 -0.0225 0.0413  422  THR A CG2 
3030  N N   . HIS A 425  ? 0.3479 0.2735 0.4250 -0.0249 -0.0236 0.0219  423  HIS A N   
3031  C CA  . HIS A 425  ? 0.3976 0.3211 0.4819 -0.0234 -0.0287 0.0130  423  HIS A CA  
3032  C C   . HIS A 425  ? 0.4198 0.3344 0.5154 -0.0246 -0.0333 0.0152  423  HIS A C   
3033  O O   . HIS A 425  ? 0.4639 0.3757 0.5672 -0.0232 -0.0382 0.0077  423  HIS A O   
3034  C CB  . HIS A 425  ? 0.3583 0.2843 0.4341 -0.0198 -0.0274 0.0073  423  HIS A CB  
3035  C CG  . HIS A 425  ? 0.3797 0.3146 0.4455 -0.0187 -0.0235 0.0052  423  HIS A CG  
3036  N ND1 . HIS A 425  ? 0.4169 0.3539 0.4713 -0.0172 -0.0191 0.0077  423  HIS A ND1 
3037  C CD2 . HIS A 425  ? 0.4085 0.3508 0.4744 -0.0190 -0.0237 0.0011  423  HIS A CD2 
3038  C CE1 . HIS A 425  ? 0.4174 0.3624 0.4659 -0.0167 -0.0168 0.0057  423  HIS A CE1 
3039  N NE2 . HIS A 425  ? 0.3871 0.3358 0.4420 -0.0178 -0.0195 0.0018  423  HIS A NE2 
3040  N N   . ASN A 426  ? 0.4057 0.3164 0.5027 -0.0272 -0.0320 0.0253  424  ASN A N   
3041  C CA  . ASN A 426  ? 0.4632 0.3655 0.5706 -0.0288 -0.0361 0.0295  424  ASN A CA  
3042  C C   . ASN A 426  ? 0.4571 0.3574 0.5788 -0.0319 -0.0409 0.0293  424  ASN A C   
3043  O O   . ASN A 426  ? 0.4684 0.3711 0.5916 -0.0351 -0.0391 0.0359  424  ASN A O   
3044  C CB  . ASN A 426  ? 0.4604 0.3612 0.5622 -0.0303 -0.0323 0.0410  424  ASN A CB  
3045  C CG  . ASN A 426  ? 0.4606 0.3534 0.5719 -0.0319 -0.0364 0.0466  424  ASN A CG  
3046  O OD1 . ASN A 426  ? 0.4525 0.3410 0.5774 -0.0341 -0.0416 0.0466  424  ASN A OD1 
3047  N ND2 . ASN A 426  ? 0.4305 0.3214 0.5351 -0.0308 -0.0343 0.0516  424  ASN A ND2 
3048  N N   . ALA A 427  ? 0.4281 0.3240 0.5610 -0.0310 -0.0472 0.0215  425  ALA A N   
3049  C CA  . ALA A 427  ? 0.4087 0.3027 0.5563 -0.0337 -0.0524 0.0195  425  ALA A CA  
3050  C C   . ALA A 427  ? 0.4527 0.3411 0.6098 -0.0381 -0.0541 0.0311  425  ALA A C   
3051  O O   . ALA A 427  ? 0.4384 0.3271 0.6054 -0.0414 -0.0566 0.0325  425  ALA A O   
3052  C CB  . ALA A 427  ? 0.5136 0.4039 0.6720 -0.0312 -0.0593 0.0081  425  ALA A CB  
3053  N N   . GLN A 428  ? 0.4623 0.3462 0.6166 -0.0385 -0.0528 0.0395  426  GLN A N   
3054  C CA  . GLN A 428  ? 0.4709 0.3513 0.6326 -0.0429 -0.0536 0.0519  426  GLN A CA  
3055  C C   . GLN A 428  ? 0.4568 0.3449 0.6108 -0.0455 -0.0475 0.0597  426  GLN A C   
3056  O O   . GLN A 428  ? 0.4569 0.3456 0.6197 -0.0497 -0.0487 0.0663  426  GLN A O   
3057  C CB  . GLN A 428  ? 0.4360 0.3110 0.5960 -0.0424 -0.0538 0.0587  426  GLN A CB  
3058  C CG  . GLN A 428  ? 0.4792 0.3495 0.6506 -0.0470 -0.0568 0.0710  426  GLN A CG  
3059  C CD  . GLN A 428  ? 0.5226 0.3999 0.6875 -0.0505 -0.0510 0.0825  426  GLN A CD  
3060  O OE1 . GLN A 428  ? 0.5287 0.4127 0.6785 -0.0487 -0.0444 0.0833  426  GLN A OE1 
3061  N NE2 . GLN A 428  ? 0.4884 0.3646 0.6652 -0.0554 -0.0537 0.0913  426  GLN A NE2 
3062  N N   . THR A 429  ? 0.4827 0.3769 0.6208 -0.0429 -0.0411 0.0592  427  THR A N   
3063  C CA  . THR A 429  ? 0.4828 0.3850 0.6130 -0.0445 -0.0353 0.0647  427  THR A CA  
3064  C C   . THR A 429  ? 0.4549 0.3613 0.5907 -0.0459 -0.0365 0.0601  427  THR A C   
3065  O O   . THR A 429  ? 0.4281 0.3381 0.5678 -0.0494 -0.0353 0.0666  427  THR A O   
3066  C CB  . THR A 429  ? 0.4314 0.3384 0.5449 -0.0408 -0.0292 0.0627  427  THR A CB  
3067  O OG1 . THR A 429  ? 0.4709 0.3737 0.5798 -0.0391 -0.0289 0.0653  427  THR A OG1 
3068  C CG2 . THR A 429  ? 0.4225 0.3372 0.5284 -0.0421 -0.0233 0.0695  427  THR A CG2 
3069  N N   . LEU A 430  ? 0.4133 0.3203 0.5496 -0.0432 -0.0389 0.0487  428  LEU A N   
3070  C CA  . LEU A 430  ? 0.4342 0.3455 0.5761 -0.0443 -0.0408 0.0430  428  LEU A CA  
3071  C C   . LEU A 430  ? 0.4618 0.3693 0.6200 -0.0487 -0.0457 0.0470  428  LEU A C   
3072  O O   . LEU A 430  ? 0.4111 0.3234 0.5723 -0.0517 -0.0445 0.0511  428  LEU A O   
3073  C CB  . LEU A 430  ? 0.4240 0.3360 0.5657 -0.0407 -0.0438 0.0298  428  LEU A CB  
3074  C CG  . LEU A 430  ? 0.4365 0.3560 0.5784 -0.0402 -0.0444 0.0220  428  LEU A CG  
3075  C CD1 . LEU A 430  ? 0.4739 0.3955 0.6123 -0.0360 -0.0462 0.0100  428  LEU A CD1 
3076  C CD2 . LEU A 430  ? 0.4017 0.3198 0.5590 -0.0436 -0.0495 0.0212  428  LEU A CD2 
3077  N N   . ALA A 431  ? 0.4431 0.3422 0.6130 -0.0492 -0.0517 0.0458  429  ALA A N   
3078  C CA  . ALA A 431  ? 0.4455 0.3399 0.6330 -0.0534 -0.0576 0.0490  429  ALA A CA  
3079  C C   . ALA A 431  ? 0.4280 0.3242 0.6170 -0.0581 -0.0547 0.0631  429  ALA A C   
3080  O O   . ALA A 431  ? 0.4180 0.3161 0.6170 -0.0620 -0.0565 0.0662  429  ALA A O   
3081  C CB  . ALA A 431  ? 0.4628 0.3470 0.6617 -0.0528 -0.0643 0.0465  429  ALA A CB  
3082  N N   . ALA A 432  ? 0.4141 0.3108 0.5935 -0.0578 -0.0501 0.0716  430  ALA A N   
3083  C CA  . ALA A 432  ? 0.4749 0.3751 0.6549 -0.0620 -0.0470 0.0851  430  ALA A CA  
3084  C C   . ALA A 432  ? 0.4229 0.3329 0.5979 -0.0632 -0.0423 0.0863  430  ALA A C   
3085  O O   . ALA A 432  ? 0.4418 0.3548 0.6250 -0.0677 -0.0426 0.0939  430  ALA A O   
3086  C CB  . ALA A 432  ? 0.4196 0.3202 0.5880 -0.0605 -0.0426 0.0921  430  ALA A CB  
3087  N N   . ILE A 433  ? 0.4345 0.3497 0.5969 -0.0593 -0.0382 0.0790  431  ILE A N   
3088  C CA  . ILE A 433  ? 0.4208 0.3454 0.5779 -0.0599 -0.0337 0.0798  431  ILE A CA  
3089  C C   . ILE A 433  ? 0.4138 0.3395 0.5823 -0.0620 -0.0380 0.0744  431  ILE A C   
3090  O O   . ILE A 433  ? 0.4304 0.3620 0.6027 -0.0650 -0.0366 0.0791  431  ILE A O   
3091  C CB  . ILE A 433  ? 0.4094 0.3386 0.5500 -0.0551 -0.0285 0.0741  431  ILE A CB  
3092  C CG1 . ILE A 433  ? 0.4194 0.3487 0.5494 -0.0537 -0.0239 0.0805  431  ILE A CG1 
3093  C CG2 . ILE A 433  ? 0.3811 0.3194 0.5176 -0.0552 -0.0249 0.0730  431  ILE A CG2 
3094  C CD1 . ILE A 433  ? 0.4077 0.3393 0.5233 -0.0490 -0.0199 0.0749  431  ILE A CD1 
3095  N N   . TYR A 434  ? 0.3978 0.3184 0.5725 -0.0602 -0.0435 0.0642  432  TYR A N   
3096  C CA  . TYR A 434  ? 0.4230 0.3447 0.6091 -0.0619 -0.0482 0.0578  432  TYR A CA  
3097  C C   . TYR A 434  ? 0.4311 0.3506 0.6328 -0.0676 -0.0517 0.0661  432  TYR A C   
3098  O O   . TYR A 434  ? 0.4259 0.3509 0.6331 -0.0703 -0.0519 0.0669  432  TYR A O   
3099  C CB  . TYR A 434  ? 0.4194 0.3358 0.6103 -0.0589 -0.0540 0.0455  432  TYR A CB  
3100  C CG  . TYR A 434  ? 0.4521 0.3683 0.6576 -0.0606 -0.0604 0.0381  432  TYR A CG  
3101  C CD1 . TYR A 434  ? 0.4297 0.3543 0.6329 -0.0603 -0.0594 0.0325  432  TYR A CD1 
3102  C CD2 . TYR A 434  ? 0.4657 0.3731 0.6877 -0.0625 -0.0678 0.0364  432  TYR A CD2 
3103  C CE1 . TYR A 434  ? 0.4606 0.3854 0.6772 -0.0618 -0.0656 0.0252  432  TYR A CE1 
3104  C CE2 . TYR A 434  ? 0.4607 0.3676 0.6969 -0.0639 -0.0742 0.0289  432  TYR A CE2 
3105  C CZ  . TYR A 434  ? 0.5010 0.4169 0.7343 -0.0636 -0.0730 0.0231  432  TYR A CZ  
3106  O OH  . TYR A 434  ? 0.4998 0.4157 0.7474 -0.0650 -0.0795 0.0152  432  TYR A OH  
3107  N N   . HIS A 435  ? 0.4400 0.3521 0.6495 -0.0697 -0.0546 0.0728  433  HIS A N   
3108  C CA  . HIS A 435  ? 0.4272 0.3373 0.6522 -0.0756 -0.0581 0.0819  433  HIS A CA  
3109  C C   . HIS A 435  ? 0.4603 0.3786 0.6799 -0.0787 -0.0519 0.0946  433  HIS A C   
3110  O O   . HIS A 435  ? 0.4258 0.3474 0.6559 -0.0835 -0.0531 0.1006  433  HIS A O   
3111  C CB  . HIS A 435  ? 0.4805 0.3799 0.7167 -0.0769 -0.0638 0.0855  433  HIS A CB  
3112  C CG  . HIS A 435  ? 0.4914 0.3829 0.7386 -0.0750 -0.0715 0.0734  433  HIS A CG  
3113  N ND1 . HIS A 435  ? 0.5060 0.3943 0.7712 -0.0781 -0.0784 0.0702  433  HIS A ND1 
3114  C CD2 . HIS A 435  ? 0.5020 0.3889 0.7448 -0.0699 -0.0734 0.0630  433  HIS A CD2 
3115  C CE1 . HIS A 435  ? 0.5254 0.4075 0.7970 -0.0749 -0.0844 0.0579  433  HIS A CE1 
3116  N NE2 . HIS A 435  ? 0.4722 0.3538 0.7304 -0.0699 -0.0813 0.0534  433  HIS A NE2 
3117  N N   . MET A 436  ? 0.4416 0.3637 0.6456 -0.0761 -0.0454 0.0985  434  MET A N   
3118  C CA  . MET A 436  ? 0.4333 0.3648 0.6309 -0.0782 -0.0390 0.1089  434  MET A CA  
3119  C C   . MET A 436  ? 0.4278 0.3682 0.6239 -0.0785 -0.0364 0.1057  434  MET A C   
3120  O O   . MET A 436  ? 0.4745 0.4222 0.6743 -0.0822 -0.0341 0.1140  434  MET A O   
3121  C CB  . MET A 436  ? 0.4243 0.3584 0.6050 -0.0744 -0.0329 0.1110  434  MET A CB  
3122  C CG  . MET A 436  ? 0.4600 0.4046 0.6334 -0.0759 -0.0262 0.1206  434  MET A CG  
3123  S SD  . MET A 436  ? 0.4465 0.3945 0.5999 -0.0707 -0.0192 0.1205  434  MET A SD  
3124  C CE  . MET A 436  ? 0.4513 0.3907 0.6072 -0.0713 -0.0224 0.1263  434  MET A CE  
3125  N N   . ALA A 437  ? 0.4038 0.3446 0.5946 -0.0746 -0.0368 0.0941  435  ALA A N   
3126  C CA  . ALA A 437  ? 0.4626 0.4121 0.6513 -0.0745 -0.0345 0.0909  435  ALA A CA  
3127  C C   . ALA A 437  ? 0.4899 0.4401 0.6951 -0.0792 -0.0394 0.0914  435  ALA A C   
3128  O O   . ALA A 437  ? 0.4390 0.3974 0.6446 -0.0805 -0.0372 0.0923  435  ALA A O   
3129  C CB  . ALA A 437  ? 0.4348 0.3849 0.6139 -0.0694 -0.0340 0.0789  435  ALA A CB  
3130  N N   . GLY A 438  ? 0.4908 0.4323 0.7102 -0.0818 -0.0462 0.0909  436  GLY A N   
3131  C CA  . GLY A 438  ? 0.5210 0.4626 0.7576 -0.0866 -0.0514 0.0921  436  GLY A CA  
3132  C C   . GLY A 438  ? 0.5121 0.4547 0.7524 -0.0849 -0.0552 0.0793  436  GLY A C   
3133  O O   . GLY A 438  ? 0.4341 0.3770 0.6644 -0.0799 -0.0544 0.0694  436  GLY A O   
3134  N N   . LYS A 439  ? 0.5440 0.4884 0.7989 -0.0892 -0.0592 0.0801  437  LYS A N   
3135  C CA  . LYS A 439  ? 0.5111 0.4553 0.7740 -0.0885 -0.0648 0.0680  437  LYS A CA  
3136  C C   . LYS A 439  ? 0.5283 0.4832 0.7819 -0.0862 -0.0611 0.0626  437  LYS A C   
3137  O O   . LYS A 439  ? 0.5446 0.5005 0.7979 -0.0833 -0.0642 0.0506  437  LYS A O   
3138  C CB  . LYS A 439  ? 0.5704 0.5112 0.8548 -0.0944 -0.0717 0.0710  437  LYS A CB  
3139  N N   . ASP A 440  ? 0.4912 0.4547 0.7376 -0.0872 -0.0548 0.0708  438  ASP A N   
3140  C CA  . ASP A 440  ? 0.5088 0.4824 0.7478 -0.0853 -0.0516 0.0665  438  ASP A CA  
3141  C C   . ASP A 440  ? 0.5060 0.4814 0.7268 -0.0792 -0.0471 0.0609  438  ASP A C   
3142  O O   . ASP A 440  ? 0.4715 0.4465 0.6814 -0.0775 -0.0419 0.0666  438  ASP A O   
3143  C CB  . ASP A 440  ? 0.4815 0.4638 0.7204 -0.0884 -0.0466 0.0772  438  ASP A CB  
3144  C CG  . ASP A 440  ? 0.5657 0.5478 0.8230 -0.0949 -0.0509 0.0833  438  ASP A CG  
3145  O OD1 . ASP A 440  ? 0.5196 0.4957 0.7900 -0.0965 -0.0582 0.0770  438  ASP A OD1 
3146  O OD2 . ASP A 440  ? 0.5602 0.5486 0.8194 -0.0982 -0.0472 0.0939  438  ASP A OD2 
3147  N N   . PHE A 441  ? 0.4280 0.4063 0.6459 -0.0761 -0.0493 0.0498  439  PHE A N   
3148  C CA  . PHE A 441  ? 0.4384 0.4196 0.6397 -0.0708 -0.0452 0.0450  439  PHE A CA  
3149  C C   . PHE A 441  ? 0.4303 0.4207 0.6279 -0.0690 -0.0451 0.0383  439  PHE A C   
3150  O O   . PHE A 441  ? 0.3687 0.3613 0.5766 -0.0706 -0.0503 0.0322  439  PHE A O   
3151  C CB  . PHE A 441  ? 0.4248 0.3984 0.6234 -0.0676 -0.0481 0.0374  439  PHE A CB  
3152  C CG  . PHE A 441  ? 0.4063 0.3829 0.5880 -0.0626 -0.0437 0.0337  439  PHE A CG  
3153  C CD1 . PHE A 441  ? 0.4102 0.3853 0.5807 -0.0610 -0.0380 0.0406  439  PHE A CD1 
3154  C CD2 . PHE A 441  ? 0.3774 0.3593 0.5546 -0.0595 -0.0453 0.0236  439  PHE A CD2 
3155  C CE1 . PHE A 441  ? 0.3430 0.3208 0.4990 -0.0566 -0.0342 0.0374  439  PHE A CE1 
3156  C CE2 . PHE A 441  ? 0.3966 0.3819 0.5590 -0.0553 -0.0413 0.0212  439  PHE A CE2 
3157  C CZ  . PHE A 441  ? 0.3836 0.3663 0.5358 -0.0539 -0.0358 0.0282  439  PHE A CZ  
3158  N N   . HIS A 442  ? 0.3744 0.3705 0.5578 -0.0657 -0.0395 0.0395  440  HIS A N   
3159  C CA  . HIS A 442  ? 0.3439 0.3487 0.5214 -0.0631 -0.0392 0.0333  440  HIS A CA  
3160  C C   . HIS A 442  ? 0.4145 0.4200 0.5760 -0.0585 -0.0348 0.0320  440  HIS A C   
3161  O O   . HIS A 442  ? 0.3585 0.3599 0.5133 -0.0576 -0.0307 0.0381  440  HIS A O   
3162  C CB  . HIS A 442  ? 0.3771 0.3905 0.5569 -0.0650 -0.0368 0.0387  440  HIS A CB  
3163  C CG  . HIS A 442  ? 0.3527 0.3677 0.5256 -0.0649 -0.0303 0.0486  440  HIS A CG  
3164  N ND1 . HIS A 442  ? 0.3805 0.4002 0.5404 -0.0612 -0.0253 0.0496  440  HIS A ND1 
3165  C CD2 . HIS A 442  ? 0.3601 0.3735 0.5379 -0.0681 -0.0281 0.0578  440  HIS A CD2 
3166  C CE1 . HIS A 442  ? 0.3442 0.3649 0.5013 -0.0617 -0.0204 0.0582  440  HIS A CE1 
3167  N NE2 . HIS A 442  ? 0.4089 0.4264 0.5762 -0.0659 -0.0218 0.0633  440  HIS A NE2 
3168  N N   . VAL A 443  ? 0.4132 0.4242 0.5689 -0.0556 -0.0360 0.0242  441  VAL A N   
3169  C CA  . VAL A 443  ? 0.4141 0.4265 0.5553 -0.0515 -0.0321 0.0235  441  VAL A CA  
3170  C C   . VAL A 443  ? 0.3983 0.4146 0.5325 -0.0509 -0.0262 0.0318  441  VAL A C   
3171  O O   . VAL A 443  ? 0.3748 0.3978 0.5127 -0.0523 -0.0258 0.0342  441  VAL A O   
3172  C CB  . VAL A 443  ? 0.4545 0.4738 0.5917 -0.0489 -0.0347 0.0142  441  VAL A CB  
3173  C CG1 . VAL A 443  ? 0.4171 0.4412 0.5403 -0.0455 -0.0301 0.0160  441  VAL A CG1 
3174  C CG2 . VAL A 443  ? 0.4735 0.4882 0.6136 -0.0479 -0.0390 0.0058  441  VAL A CG2 
3175  N N   . GLY A 444  ? 0.3757 0.3881 0.5006 -0.0489 -0.0219 0.0359  442  GLY A N   
3176  C CA  . GLY A 444  ? 0.3558 0.3707 0.4751 -0.0483 -0.0165 0.0436  442  GLY A CA  
3177  C C   . GLY A 444  ? 0.3235 0.3340 0.4467 -0.0506 -0.0143 0.0513  442  GLY A C   
3178  O O   . GLY A 444  ? 0.3155 0.3279 0.4331 -0.0496 -0.0095 0.0572  442  GLY A O   
3179  N N   . LYS A 445  ? 0.3251 0.3302 0.4581 -0.0538 -0.0178 0.0516  443  LYS A N   
3180  C CA  . LYS A 445  ? 0.2949 0.2965 0.4317 -0.0563 -0.0159 0.0598  443  LYS A CA  
3181  C C   . LYS A 445  ? 0.3254 0.3208 0.4532 -0.0540 -0.0132 0.0615  443  LYS A C   
3182  O O   . LYS A 445  ? 0.2845 0.2811 0.4071 -0.0536 -0.0087 0.0681  443  LYS A O   
3183  C CB  . LYS A 445  ? 0.3631 0.3604 0.5142 -0.0606 -0.0210 0.0602  443  LYS A CB  
3184  C CG  . LYS A 445  ? 0.3878 0.3843 0.5447 -0.0643 -0.0192 0.0702  443  LYS A CG  
3185  C CD  . LYS A 445  ? 0.4078 0.3990 0.5796 -0.0687 -0.0248 0.0712  443  LYS A CD  
3186  C CE  . LYS A 445  ? 0.4824 0.4746 0.6601 -0.0728 -0.0228 0.0825  443  LYS A CE  
3187  N NZ  . LYS A 445  ? 0.4586 0.4463 0.6529 -0.0779 -0.0286 0.0848  443  LYS A NZ  
3188  N N   . TYR A 446  ? 0.3090 0.2983 0.4352 -0.0525 -0.0163 0.0553  444  TYR A N   
3189  C CA  . TYR A 446  ? 0.2905 0.2745 0.4074 -0.0497 -0.0142 0.0552  444  TYR A CA  
3190  C C   . TYR A 446  ? 0.3217 0.3030 0.4368 -0.0474 -0.0178 0.0459  444  TYR A C   
3191  O O   . TYR A 446  ? 0.3196 0.3030 0.4413 -0.0481 -0.0220 0.0397  444  TYR A O   
3192  C CB  . TYR A 446  ? 0.2965 0.2740 0.4172 -0.0518 -0.0141 0.0616  444  TYR A CB  
3193  C CG  . TYR A 446  ? 0.3508 0.3218 0.4837 -0.0545 -0.0202 0.0592  444  TYR A CG  
3194  C CD1 . TYR A 446  ? 0.3722 0.3365 0.5046 -0.0526 -0.0234 0.0531  444  TYR A CD1 
3195  C CD2 . TYR A 446  ? 0.4271 0.3988 0.5728 -0.0588 -0.0229 0.0630  444  TYR A CD2 
3196  C CE1 . TYR A 446  ? 0.4356 0.3935 0.5804 -0.0548 -0.0294 0.0505  444  TYR A CE1 
3197  C CE2 . TYR A 446  ? 0.3823 0.3476 0.5405 -0.0613 -0.0289 0.0609  444  TYR A CE2 
3198  C CZ  . TYR A 446  ? 0.4361 0.3944 0.5940 -0.0592 -0.0322 0.0544  444  TYR A CZ  
3199  O OH  . TYR A 446  ? 0.5663 0.5179 0.7380 -0.0615 -0.0387 0.0519  444  TYR A OH  
3200  N N   . GLU A 447  ? 0.3052 0.2826 0.4117 -0.0446 -0.0162 0.0445  445  GLU A N   
3201  C CA  . GLU A 447  ? 0.3034 0.2788 0.4083 -0.0424 -0.0194 0.0358  445  GLU A CA  
3202  C C   . GLU A 447  ? 0.3123 0.2803 0.4130 -0.0409 -0.0187 0.0366  445  GLU A C   
3203  O O   . GLU A 447  ? 0.3218 0.2873 0.4187 -0.0412 -0.0152 0.0437  445  GLU A O   
3204  C CB  . GLU A 447  ? 0.2711 0.2537 0.3670 -0.0395 -0.0178 0.0312  445  GLU A CB  
3205  C CG  . GLU A 447  ? 0.3048 0.2881 0.3885 -0.0369 -0.0125 0.0351  445  GLU A CG  
3206  C CD  . GLU A 447  ? 0.2970 0.2874 0.3728 -0.0344 -0.0113 0.0318  445  GLU A CD  
3207  O OE1 . GLU A 447  ? 0.2989 0.2953 0.3779 -0.0348 -0.0139 0.0274  445  GLU A OE1 
3208  O OE2 . GLU A 447  ? 0.3581 0.3483 0.4246 -0.0322 -0.0078 0.0338  445  GLU A OE2 
3209  N N   . PHE A 448  ? 0.2836 0.2488 0.3853 -0.0393 -0.0223 0.0290  446  PHE A N   
3210  C CA  . PHE A 448  ? 0.3178 0.2775 0.4140 -0.0371 -0.0216 0.0280  446  PHE A CA  
3211  C C   . PHE A 448  ? 0.3246 0.2893 0.4092 -0.0337 -0.0191 0.0238  446  PHE A C   
3212  O O   . PHE A 448  ? 0.3445 0.3166 0.4266 -0.0331 -0.0188 0.0208  446  PHE A O   
3213  C CB  . PHE A 448  ? 0.3415 0.2952 0.4470 -0.0373 -0.0273 0.0221  446  PHE A CB  
3214  C CG  . PHE A 448  ? 0.3308 0.2785 0.4487 -0.0409 -0.0304 0.0270  446  PHE A CG  
3215  C CD1 . PHE A 448  ? 0.3613 0.3029 0.4791 -0.0419 -0.0289 0.0349  446  PHE A CD1 
3216  C CD2 . PHE A 448  ? 0.3458 0.2944 0.4758 -0.0433 -0.0349 0.0240  446  PHE A CD2 
3217  C CE1 . PHE A 448  ? 0.3695 0.3062 0.4992 -0.0456 -0.0318 0.0406  446  PHE A CE1 
3218  C CE2 . PHE A 448  ? 0.3691 0.3121 0.5115 -0.0470 -0.0380 0.0292  446  PHE A CE2 
3219  C CZ  . PHE A 448  ? 0.4092 0.3463 0.5515 -0.0483 -0.0365 0.0379  446  PHE A CZ  
3220  N N   . GLN A 449  ? 0.3182 0.2791 0.3958 -0.0316 -0.0172 0.0243  447  GLN A N   
3221  C CA  . GLN A 449  ? 0.2951 0.2600 0.3624 -0.0286 -0.0152 0.0206  447  GLN A CA  
3222  C C   . GLN A 449  ? 0.3453 0.3052 0.4110 -0.0267 -0.0166 0.0168  447  GLN A C   
3223  O O   . GLN A 449  ? 0.3163 0.2688 0.3859 -0.0274 -0.0175 0.0196  447  GLN A O   
3224  C CB  . GLN A 449  ? 0.2949 0.2619 0.3526 -0.0277 -0.0098 0.0269  447  GLN A CB  
3225  C CG  . GLN A 449  ? 0.2894 0.2618 0.3483 -0.0291 -0.0081 0.0309  447  GLN A CG  
3226  C CD  . GLN A 449  ? 0.3244 0.3000 0.3742 -0.0275 -0.0034 0.0350  447  GLN A CD  
3227  O OE1 . GLN A 449  ? 0.3441 0.3170 0.3869 -0.0257 -0.0012 0.0361  447  GLN A OE1 
3228  N NE2 . GLN A 449  ? 0.3190 0.3004 0.3693 -0.0280 -0.0023 0.0370  447  GLN A NE2 
3229  N N   . CYS A 450  ? 0.3449 0.3096 0.4047 -0.0243 -0.0166 0.0107  448  CYS A N   
3230  C CA  . CYS A 450  ? 0.3415 0.3031 0.3994 -0.0221 -0.0178 0.0062  448  CYS A CA  
3231  C C   . CYS A 450  ? 0.3484 0.3163 0.3957 -0.0199 -0.0149 0.0045  448  CYS A C   
3232  O O   . CYS A 450  ? 0.3378 0.3124 0.3804 -0.0200 -0.0128 0.0061  448  CYS A O   
3233  C CB  . CYS A 450  ? 0.3363 0.2977 0.4035 -0.0218 -0.0233 -0.0025 448  CYS A CB  
3234  S SG  . CYS A 450  ? 0.4139 0.3876 0.4805 -0.0206 -0.0254 -0.0119 448  CYS A SG  
3235  N N   . LEU A 451  ? 0.3095 0.2753 0.3534 -0.0179 -0.0150 0.0017  449  LEU A N   
3236  C CA  . LEU A 451  ? 0.3327 0.3046 0.3674 -0.0160 -0.0126 0.0001  449  LEU A CA  
3237  C C   . LEU A 451  ? 0.3489 0.3292 0.3851 -0.0147 -0.0155 -0.0091 449  LEU A C   
3238  O O   . LEU A 451  ? 0.3655 0.3442 0.4091 -0.0143 -0.0195 -0.0155 449  LEU A O   
3239  C CB  . LEU A 451  ? 0.3505 0.3167 0.3805 -0.0145 -0.0109 0.0018  449  LEU A CB  
3240  N N   . HIS A 452  ? 0.3461 0.3358 0.3756 -0.0142 -0.0137 -0.0095 450  HIS A N   
3241  C CA  . HIS A 452  ? 0.3719 0.3721 0.4012 -0.0129 -0.0159 -0.0178 450  HIS A CA  
3242  C C   . HIS A 452  ? 0.3882 0.3872 0.4178 -0.0108 -0.0174 -0.0238 450  HIS A C   
3243  O O   . HIS A 452  ? 0.3548 0.3486 0.3799 -0.0101 -0.0151 -0.0203 450  HIS A O   
3244  C CB  . HIS A 452  ? 0.3758 0.3862 0.3966 -0.0128 -0.0132 -0.0153 450  HIS A CB  
3245  C CG  . HIS A 452  ? 0.3655 0.3878 0.3840 -0.0113 -0.0146 -0.0227 450  HIS A CG  
3246  N ND1 . HIS A 452  ? 0.4013 0.4338 0.4229 -0.0113 -0.0174 -0.0291 450  HIS A ND1 
3247  C CD2 . HIS A 452  ? 0.3822 0.4085 0.3958 -0.0098 -0.0137 -0.0251 450  HIS A CD2 
3248  C CE1 . HIS A 452  ? 0.3895 0.4327 0.4079 -0.0097 -0.0180 -0.0350 450  HIS A CE1 
3249  N NE2 . HIS A 452  ? 0.3669 0.4064 0.3805 -0.0089 -0.0157 -0.0326 450  HIS A NE2 
3250  N N   . GLY A 453  ? 0.4372 0.4417 0.4724 -0.0096 -0.0213 -0.0333 451  GLY A N   
3251  C CA  . GLY A 453  ? 0.4490 0.4544 0.4852 -0.0072 -0.0230 -0.0403 451  GLY A CA  
3252  C C   . GLY A 453  ? 0.5231 0.5152 0.5644 -0.0068 -0.0243 -0.0389 451  GLY A C   
3253  O O   . GLY A 453  ? 0.5816 0.5722 0.6203 -0.0051 -0.0237 -0.0402 451  GLY A O   
3254  N N   . MET A 454  ? 0.4880 0.4712 0.5369 -0.0086 -0.0261 -0.0359 452  MET A N   
3255  C CA  . MET A 454  ? 0.4936 0.4642 0.5468 -0.0088 -0.0269 -0.0320 452  MET A CA  
3256  C C   . MET A 454  ? 0.5051 0.4690 0.5694 -0.0109 -0.0304 -0.0311 452  MET A C   
3257  O O   . MET A 454  ? 0.5022 0.4605 0.5763 -0.0102 -0.0349 -0.0357 452  MET A O   
3258  C CB  . MET A 454  ? 0.4704 0.4364 0.5150 -0.0097 -0.0219 -0.0219 452  MET A CB  
3259  C CG  . MET A 454  ? 0.4952 0.4493 0.5434 -0.0106 -0.0222 -0.0157 452  MET A CG  
3260  S SD  . MET A 454  ? 0.6487 0.5973 0.7004 -0.0080 -0.0251 -0.0206 452  MET A SD  
3261  C CE  . MET A 454  ? 0.5886 0.5449 0.6280 -0.0059 -0.0210 -0.0217 452  MET A CE  
3262  N N   . GLY A 455  ? 0.4448 0.4098 0.5085 -0.0133 -0.0288 -0.0255 453  GLY A N   
3263  C CA  . GLY A 455  ? 0.4535 0.4130 0.5277 -0.0157 -0.0318 -0.0236 453  GLY A CA  
3264  C C   . GLY A 455  ? 0.4622 0.4273 0.5448 -0.0159 -0.0363 -0.0321 453  GLY A C   
3265  O O   . GLY A 455  ? 0.4681 0.4276 0.5617 -0.0178 -0.0400 -0.0320 453  GLY A O   
3266  N N   . GLU A 456  ? 0.4494 0.4259 0.5275 -0.0141 -0.0363 -0.0393 454  GLU A N   
3267  C CA  . GLU A 456  ? 0.4548 0.4380 0.5408 -0.0141 -0.0407 -0.0482 454  GLU A CA  
3268  C C   . GLU A 456  ? 0.4919 0.4687 0.5912 -0.0133 -0.0469 -0.0557 454  GLU A C   
3269  O O   . GLU A 456  ? 0.5135 0.4886 0.6234 -0.0151 -0.0508 -0.0580 454  GLU A O   
3270  C CB  . GLU A 456  ? 0.5072 0.5050 0.5858 -0.0119 -0.0399 -0.0554 454  GLU A CB  
3271  C CG  . GLU A 456  ? 0.5202 0.5251 0.5875 -0.0129 -0.0349 -0.0483 454  GLU A CG  
3272  C CD  . GLU A 456  ? 0.4858 0.4912 0.5423 -0.0117 -0.0304 -0.0439 454  GLU A CD  
3273  O OE1 . GLU A 456  ? 0.4982 0.4955 0.5557 -0.0106 -0.0305 -0.0435 454  GLU A OE1 
3274  O OE2 . GLU A 456  ? 0.4665 0.4803 0.5139 -0.0117 -0.0271 -0.0407 454  GLU A OE2 
3275  N N   . PRO A 457  ? 0.4954 0.4684 0.5960 -0.0108 -0.0484 -0.0599 455  PRO A N   
3276  C CA  . PRO A 457  ? 0.5273 0.4927 0.6424 -0.0102 -0.0548 -0.0663 455  PRO A CA  
3277  C C   . PRO A 457  ? 0.5047 0.4590 0.6299 -0.0137 -0.0569 -0.0589 455  PRO A C   
3278  O O   . PRO A 457  ? 0.4773 0.4302 0.6150 -0.0147 -0.0622 -0.0642 455  PRO A O   
3279  C CB  . PRO A 457  ? 0.5317 0.4925 0.6443 -0.0076 -0.0543 -0.0671 455  PRO A CB  
3280  C CG  . PRO A 457  ? 0.5001 0.4714 0.5984 -0.0058 -0.0492 -0.0675 455  PRO A CG  
3281  C CD  . PRO A 457  ? 0.4962 0.4713 0.5863 -0.0085 -0.0447 -0.0590 455  PRO A CD  
3282  N N   . LEU A 458  ? 0.4852 0.4323 0.6055 -0.0159 -0.0529 -0.0467 456  LEU A N   
3283  C CA  . LEU A 458  ? 0.4625 0.4003 0.5921 -0.0195 -0.0546 -0.0387 456  LEU A CA  
3284  C C   . LEU A 458  ? 0.4587 0.4015 0.5916 -0.0222 -0.0550 -0.0380 456  LEU A C   
3285  O O   . LEU A 458  ? 0.4942 0.4328 0.6404 -0.0243 -0.0598 -0.0392 456  LEU A O   
3286  C CB  . LEU A 458  ? 0.4440 0.3758 0.5660 -0.0210 -0.0496 -0.0260 456  LEU A CB  
3287  C CG  . LEU A 458  ? 0.4688 0.3933 0.5986 -0.0251 -0.0503 -0.0161 456  LEU A CG  
3288  C CD1 . LEU A 458  ? 0.4651 0.3804 0.6113 -0.0261 -0.0573 -0.0182 456  LEU A CD1 
3289  C CD2 . LEU A 458  ? 0.4455 0.3667 0.5660 -0.0261 -0.0448 -0.0044 456  LEU A CD2 
3290  N N   . TYR A 459  ? 0.4350 0.3870 0.5566 -0.0222 -0.0502 -0.0361 457  TYR A N   
3291  C CA  . TYR A 459  ? 0.4779 0.4341 0.6019 -0.0249 -0.0499 -0.0334 457  TYR A CA  
3292  C C   . TYR A 459  ? 0.4800 0.4442 0.6106 -0.0241 -0.0545 -0.0447 457  TYR A C   
3293  O O   . TYR A 459  ? 0.4742 0.4406 0.6106 -0.0266 -0.0559 -0.0437 457  TYR A O   
3294  C CB  . TYR A 459  ? 0.4125 0.3745 0.5229 -0.0253 -0.0432 -0.0259 457  TYR A CB  
3295  C CG  . TYR A 459  ? 0.3769 0.3310 0.4848 -0.0272 -0.0396 -0.0140 457  TYR A CG  
3296  C CD1 . TYR A 459  ? 0.3640 0.3147 0.4787 -0.0308 -0.0398 -0.0067 457  TYR A CD1 
3297  C CD2 . TYR A 459  ? 0.3862 0.3367 0.4856 -0.0255 -0.0363 -0.0102 457  TYR A CD2 
3298  C CE1 . TYR A 459  ? 0.3639 0.3089 0.4763 -0.0325 -0.0364 0.0040  457  TYR A CE1 
3299  C CE2 . TYR A 459  ? 0.3789 0.3232 0.4758 -0.0272 -0.0331 0.0002  457  TYR A CE2 
3300  C CZ  . TYR A 459  ? 0.4054 0.3474 0.5087 -0.0306 -0.0331 0.0072  457  TYR A CZ  
3301  O OH  . TYR A 459  ? 0.4154 0.3530 0.5163 -0.0322 -0.0298 0.0174  457  TYR A OH  
3302  N N   . GLU A 460  ? 0.4690 0.4382 0.5996 -0.0207 -0.0571 -0.0558 458  GLU A N   
3303  C CA  . GLU A 460  ? 0.4981 0.4743 0.6375 -0.0200 -0.0625 -0.0673 458  GLU A CA  
3304  C C   . GLU A 460  ? 0.5101 0.4765 0.6672 -0.0217 -0.0692 -0.0700 458  GLU A C   
3305  O O   . GLU A 460  ? 0.5208 0.4916 0.6875 -0.0218 -0.0742 -0.0788 458  GLU A O   
3306  C CB  . GLU A 460  ? 0.5465 0.5323 0.6813 -0.0158 -0.0635 -0.0790 458  GLU A CB  
3307  C CG  . GLU A 460  ? 0.5482 0.5453 0.6665 -0.0146 -0.0574 -0.0763 458  GLU A CG  
3308  C CD  . GLU A 460  ? 0.6001 0.6118 0.7149 -0.0113 -0.0589 -0.0883 458  GLU A CD  
3309  O OE1 . GLU A 460  ? 0.6769 0.6957 0.7990 -0.0110 -0.0633 -0.0973 458  GLU A OE1 
3310  O OE2 . GLU A 460  ? 0.6941 0.7109 0.7990 -0.0090 -0.0557 -0.0888 458  GLU A OE2 
3311  N N   . GLU A 461  ? 0.4877 0.4414 0.6498 -0.0231 -0.0695 -0.0624 459  GLU A N   
3312  C CA  . GLU A 461  ? 0.5374 0.4808 0.7164 -0.0259 -0.0752 -0.0610 459  GLU A CA  
3313  C C   . GLU A 461  ? 0.5227 0.4632 0.7035 -0.0307 -0.0730 -0.0490 459  GLU A C   
3314  O O   . GLU A 461  ? 0.4789 0.4106 0.6732 -0.0337 -0.0770 -0.0449 459  GLU A O   
3315  C CB  . GLU A 461  ? 0.5426 0.4744 0.7268 -0.0250 -0.0773 -0.0586 459  GLU A CB  
3316  C CG  . GLU A 461  ? 0.5360 0.4708 0.7168 -0.0201 -0.0785 -0.0691 459  GLU A CG  
3317  C CD  . GLU A 461  ? 0.6111 0.5511 0.8027 -0.0176 -0.0851 -0.0847 459  GLU A CD  
3318  O OE1 . GLU A 461  ? 0.5916 0.5281 0.7977 -0.0198 -0.0906 -0.0872 459  GLU A OE1 
3319  O OE2 . GLU A 461  ? 0.6537 0.6020 0.8396 -0.0134 -0.0850 -0.0947 459  GLU A OE2 
3320  N N   . VAL A 462  ? 0.4866 0.4345 0.6545 -0.0313 -0.0668 -0.0431 460  VAL A N   
3321  C CA  . VAL A 462  ? 0.5012 0.4477 0.6691 -0.0354 -0.0637 -0.0315 460  VAL A CA  
3322  C C   . VAL A 462  ? 0.5119 0.4688 0.6782 -0.0363 -0.0631 -0.0341 460  VAL A C   
3323  O O   . VAL A 462  ? 0.4982 0.4543 0.6743 -0.0397 -0.0654 -0.0314 460  VAL A O   
3324  C CB  . VAL A 462  ? 0.4809 0.4257 0.6354 -0.0354 -0.0566 -0.0204 460  VAL A CB  
3325  C CG1 . VAL A 462  ? 0.4548 0.4005 0.6087 -0.0391 -0.0531 -0.0095 460  VAL A CG1 
3326  C CG2 . VAL A 462  ? 0.4815 0.4160 0.6382 -0.0349 -0.0574 -0.0168 460  VAL A CG2 
3327  N N   . VAL A 463  ? 0.4303 0.3977 0.5846 -0.0334 -0.0601 -0.0390 461  VAL A N   
3328  C CA  . VAL A 463  ? 0.4820 0.4600 0.6328 -0.0341 -0.0589 -0.0402 461  VAL A CA  
3329  C C   . VAL A 463  ? 0.5162 0.4984 0.6793 -0.0343 -0.0656 -0.0513 461  VAL A C   
3330  O O   . VAL A 463  ? 0.5323 0.5136 0.7012 -0.0320 -0.0703 -0.0615 461  VAL A O   
3331  C CB  . VAL A 463  ? 0.4378 0.4259 0.5727 -0.0311 -0.0542 -0.0417 461  VAL A CB  
3332  C CG1 . VAL A 463  ? 0.4633 0.4630 0.5951 -0.0317 -0.0533 -0.0427 461  VAL A CG1 
3333  C CG2 . VAL A 463  ? 0.4202 0.4038 0.5440 -0.0308 -0.0479 -0.0313 461  VAL A CG2 
3334  N N   . GLY A 464  ? 0.4791 0.4660 0.6464 -0.0368 -0.0664 -0.0498 462  GLY A N   
3335  C CA  . GLY A 464  ? 0.5323 0.5255 0.7095 -0.0368 -0.0724 -0.0609 462  GLY A CA  
3336  C C   . GLY A 464  ? 0.5553 0.5400 0.7508 -0.0403 -0.0782 -0.0605 462  GLY A C   
3337  O O   . GLY A 464  ? 0.5413 0.5140 0.7434 -0.0420 -0.0790 -0.0545 462  GLY A O   
3338  N N   . ARG A 465  ? 0.5603 0.5513 0.7643 -0.0415 -0.0824 -0.0670 463  ARG A N   
3339  C CA  . ARG A 465  ? 0.5443 0.5280 0.7668 -0.0453 -0.0884 -0.0669 463  ARG A CA  
3340  C C   . ARG A 465  ? 0.5782 0.5524 0.8136 -0.0442 -0.0948 -0.0744 463  ARG A C   
3341  O O   . ARG A 465  ? 0.6424 0.6064 0.8928 -0.0476 -0.0990 -0.0706 463  ARG A O   
3342  C CB  . ARG A 465  ? 0.5305 0.5242 0.7593 -0.0463 -0.0920 -0.0740 463  ARG A CB  
3343  N N   . GLY A 466  ? 0.5528 0.5301 0.7830 -0.0396 -0.0958 -0.0845 464  GLY A N   
3344  C CA  . GLY A 466  ? 0.5899 0.5585 0.8321 -0.0378 -0.1019 -0.0923 464  GLY A CA  
3345  C C   . GLY A 466  ? 0.6115 0.5676 0.8525 -0.0382 -0.0997 -0.0829 464  GLY A C   
3346  O O   . GLY A 466  ? 0.6605 0.6075 0.9133 -0.0373 -0.1051 -0.0875 464  GLY A O   
3347  N N   . LYS A 467  ? 0.6148 0.5704 0.8419 -0.0393 -0.0920 -0.0702 465  LYS A N   
3348  C CA  . LYS A 467  ? 0.5550 0.4997 0.7802 -0.0398 -0.0895 -0.0604 465  LYS A CA  
3349  C C   . LYS A 467  ? 0.5423 0.4813 0.7703 -0.0450 -0.0869 -0.0454 465  LYS A C   
3350  O O   . LYS A 467  ? 0.5674 0.5031 0.8102 -0.0486 -0.0916 -0.0442 465  LYS A O   
3351  C CB  . LYS A 467  ? 0.5093 0.4585 0.7156 -0.0362 -0.0829 -0.0589 465  LYS A CB  
3352  C CG  . LYS A 467  ? 0.5526 0.5092 0.7554 -0.0313 -0.0850 -0.0733 465  LYS A CG  
3353  C CD  . LYS A 467  ? 0.5842 0.5322 0.8014 -0.0297 -0.0921 -0.0814 465  LYS A CD  
3354  C CE  . LYS A 467  ? 0.5969 0.5513 0.8081 -0.0243 -0.0926 -0.0932 465  LYS A CE  
3355  N NZ  . LYS A 467  ? 0.5976 0.5417 0.8211 -0.0224 -0.0983 -0.0985 465  LYS A NZ  
3356  N N   . LEU A 468  ? 0.5683 0.5068 0.7831 -0.0453 -0.0798 -0.0343 466  LEU A N   
3357  C CA  . LEU A 468  ? 0.4976 0.4330 0.7136 -0.0498 -0.0766 -0.0202 466  LEU A CA  
3358  C C   . LEU A 468  ? 0.5291 0.4746 0.7387 -0.0513 -0.0726 -0.0172 466  LEU A C   
3359  O O   . LEU A 468  ? 0.4950 0.4397 0.7074 -0.0552 -0.0704 -0.0068 466  LEU A O   
3360  C CB  . LEU A 468  ? 0.5126 0.4431 0.7182 -0.0493 -0.0711 -0.0099 466  LEU A CB  
3361  C CG  . LEU A 468  ? 0.5341 0.4545 0.7445 -0.0478 -0.0743 -0.0110 466  LEU A CG  
3362  C CD1 . LEU A 468  ? 0.5123 0.4300 0.7101 -0.0470 -0.0682 -0.0013 466  LEU A CD1 
3363  C CD2 . LEU A 468  ? 0.5256 0.4365 0.7558 -0.0515 -0.0812 -0.0085 466  LEU A CD2 
3364  N N   . ASP A 469  ? 0.5370 0.4926 0.7383 -0.0482 -0.0716 -0.0260 467  ASP A N   
3365  C CA  . ASP A 469  ? 0.5084 0.4744 0.7032 -0.0490 -0.0681 -0.0240 467  ASP A CA  
3366  C C   . ASP A 469  ? 0.4583 0.4248 0.6416 -0.0500 -0.0606 -0.0112 467  ASP A C   
3367  O O   . ASP A 469  ? 0.4363 0.4057 0.6215 -0.0530 -0.0585 -0.0041 467  ASP A O   
3368  C CB  . ASP A 469  ? 0.5321 0.4995 0.7415 -0.0527 -0.0729 -0.0254 467  ASP A CB  
3369  C CG  . ASP A 469  ? 0.5695 0.5496 0.7737 -0.0521 -0.0718 -0.0297 467  ASP A CG  
3370  O OD1 . ASP A 469  ? 0.5755 0.5632 0.7660 -0.0485 -0.0684 -0.0332 467  ASP A OD1 
3371  O OD2 . ASP A 469  ? 0.6269 0.6095 0.8411 -0.0552 -0.0745 -0.0292 467  ASP A OD2 
3372  N N   . ARG A 470  ? 0.4882 0.4523 0.6600 -0.0473 -0.0565 -0.0089 468  ARG A N   
3373  C CA  . ARG A 470  ? 0.4208 0.3864 0.5804 -0.0473 -0.0494 0.0011  468  ARG A CA  
3374  C C   . ARG A 470  ? 0.4240 0.3958 0.5686 -0.0431 -0.0457 -0.0030 468  ARG A C   
3375  O O   . ARG A 470  ? 0.4645 0.4351 0.6069 -0.0403 -0.0475 -0.0102 468  ARG A O   
3376  C CB  . ARG A 470  ? 0.3935 0.3495 0.5540 -0.0485 -0.0479 0.0098  468  ARG A CB  
3377  C CG  . ARG A 470  ? 0.4406 0.3908 0.6161 -0.0532 -0.0513 0.0159  468  ARG A CG  
3378  C CD  . ARG A 470  ? 0.4381 0.3942 0.6147 -0.0564 -0.0484 0.0236  468  ARG A CD  
3379  N NE  . ARG A 470  ? 0.4531 0.4045 0.6444 -0.0612 -0.0517 0.0300  468  ARG A NE  
3380  C CZ  . ARG A 470  ? 0.4793 0.4313 0.6843 -0.0639 -0.0570 0.0263  468  ARG A CZ  
3381  N NH1 . ARG A 470  ? 0.4442 0.4021 0.6499 -0.0622 -0.0596 0.0160  468  ARG A NH1 
3382  N NH2 . ARG A 470  ? 0.4124 0.3598 0.6310 -0.0687 -0.0598 0.0335  468  ARG A NH2 
3383  N N   . PRO A 471  ? 0.4578 0.4367 0.5927 -0.0426 -0.0408 0.0013  469  PRO A N   
3384  C CA  . PRO A 471  ? 0.3245 0.3100 0.4462 -0.0391 -0.0378 -0.0022 469  PRO A CA  
3385  C C   . PRO A 471  ? 0.3867 0.3669 0.4991 -0.0371 -0.0339 0.0019  469  PRO A C   
3386  O O   . PRO A 471  ? 0.3328 0.3058 0.4463 -0.0385 -0.0321 0.0094  469  PRO A O   
3387  C CB  . PRO A 471  ? 0.3964 0.3899 0.5131 -0.0397 -0.0343 0.0025  469  PRO A CB  
3388  C CG  . PRO A 471  ? 0.3677 0.3564 0.4897 -0.0428 -0.0326 0.0119  469  PRO A CG  
3389  C CD  . PRO A 471  ? 0.4133 0.3949 0.5492 -0.0454 -0.0378 0.0100  469  PRO A CD  
3390  N N   . CYS A 472  ? 0.3651 0.3499 0.4680 -0.0340 -0.0326 -0.0029 470  CYS A N   
3391  C CA  . CYS A 472  ? 0.3439 0.3249 0.4372 -0.0319 -0.0290 0.0001  470  CYS A CA  
3392  C C   . CYS A 472  ? 0.3060 0.2953 0.3874 -0.0297 -0.0254 0.0000  470  CYS A C   
3393  O O   . CYS A 472  ? 0.3667 0.3644 0.4468 -0.0286 -0.0272 -0.0065 470  CYS A O   
3394  C CB  . CYS A 472  ? 0.3451 0.3213 0.4410 -0.0301 -0.0322 -0.0066 470  CYS A CB  
3395  S SG  . CYS A 472  ? 0.4034 0.3746 0.4886 -0.0278 -0.0281 -0.0029 470  CYS A SG  
3396  N N   . ARG A 473  ? 0.3095 0.2969 0.3828 -0.0292 -0.0205 0.0073  471  ARG A N   
3397  C CA  . ARG A 473  ? 0.3328 0.3265 0.3953 -0.0272 -0.0172 0.0081  471  ARG A CA  
3398  C C   . ARG A 473  ? 0.3274 0.3183 0.3833 -0.0249 -0.0162 0.0061  471  ARG A C   
3399  O O   . ARG A 473  ? 0.3301 0.3131 0.3854 -0.0248 -0.0148 0.0097  471  ARG A O   
3400  C CB  . ARG A 473  ? 0.3339 0.3277 0.3921 -0.0277 -0.0128 0.0168  471  ARG A CB  
3401  C CG  . ARG A 473  ? 0.3047 0.3052 0.3537 -0.0258 -0.0102 0.0179  471  ARG A CG  
3402  C CD  . ARG A 473  ? 0.3198 0.3205 0.3665 -0.0262 -0.0065 0.0255  471  ARG A CD  
3403  N NE  . ARG A 473  ? 0.3261 0.3287 0.3806 -0.0283 -0.0077 0.0271  471  ARG A NE  
3404  C CZ  . ARG A 473  ? 0.3544 0.3648 0.4111 -0.0288 -0.0092 0.0255  471  ARG A CZ  
3405  N NH1 . ARG A 473  ? 0.3194 0.3369 0.3706 -0.0273 -0.0094 0.0233  471  ARG A NH1 
3406  N NH2 . ARG A 473  ? 0.2939 0.3055 0.3589 -0.0311 -0.0108 0.0263  471  ARG A NH2 
3407  N N   . ILE A 474  ? 0.3307 0.3291 0.3816 -0.0231 -0.0167 0.0008  472  ILE A N   
3408  C CA  . ILE A 474  ? 0.2895 0.2872 0.3341 -0.0209 -0.0158 -0.0017 472  ILE A CA  
3409  C C   . ILE A 474  ? 0.3222 0.3208 0.3573 -0.0202 -0.0112 0.0049  472  ILE A C   
3410  O O   . ILE A 474  ? 0.3631 0.3689 0.3944 -0.0202 -0.0099 0.0069  472  ILE A O   
3411  C CB  . ILE A 474  ? 0.3014 0.3084 0.3456 -0.0195 -0.0187 -0.0107 472  ILE A CB  
3412  C CG1 . ILE A 474  ? 0.3464 0.3519 0.4013 -0.0199 -0.0238 -0.0183 472  ILE A CG1 
3413  C CG2 . ILE A 474  ? 0.3212 0.3291 0.3585 -0.0174 -0.0173 -0.0127 472  ILE A CG2 
3414  C CD1 . ILE A 474  ? 0.3447 0.3614 0.4003 -0.0184 -0.0270 -0.0284 472  ILE A CD1 
3415  N N   . TYR A 475  ? 0.2932 0.2842 0.3250 -0.0195 -0.0090 0.0084  473  TYR A N   
3416  C CA  . TYR A 475  ? 0.3463 0.3372 0.3696 -0.0185 -0.0051 0.0135  473  TYR A CA  
3417  C C   . TYR A 475  ? 0.3680 0.3646 0.3857 -0.0168 -0.0053 0.0091  473  TYR A C   
3418  O O   . TYR A 475  ? 0.3365 0.3305 0.3547 -0.0158 -0.0066 0.0049  473  TYR A O   
3419  C CB  . TYR A 475  ? 0.3755 0.3568 0.3980 -0.0184 -0.0030 0.0182  473  TYR A CB  
3420  C CG  . TYR A 475  ? 0.4303 0.4102 0.4455 -0.0175 0.0009  0.0239  473  TYR A CG  
3421  C CD1 . TYR A 475  ? 0.4310 0.4128 0.4452 -0.0179 0.0032  0.0290  473  TYR A CD1 
3422  C CD2 . TYR A 475  ? 0.5141 0.4905 0.5244 -0.0161 0.0022  0.0238  473  TYR A CD2 
3423  C CE1 . TYR A 475  ? 0.4519 0.4321 0.4605 -0.0168 0.0064  0.0334  473  TYR A CE1 
3424  C CE2 . TYR A 475  ? 0.5491 0.5239 0.5536 -0.0152 0.0053  0.0283  473  TYR A CE2 
3425  C CZ  . TYR A 475  ? 0.5371 0.5136 0.5410 -0.0155 0.0074  0.0329  473  TYR A CZ  
3426  O OH  . TYR A 475  ? 0.5728 0.5476 0.5718 -0.0143 0.0101  0.0367  473  TYR A OH  
3427  N N   . ALA A 476  ? 0.3816 0.3865 0.3947 -0.0166 -0.0043 0.0104  474  ALA A N   
3428  C CA  . ALA A 476  ? 0.3531 0.3671 0.3622 -0.0156 -0.0051 0.0061  474  ALA A CA  
3429  C C   . ALA A 476  ? 0.3479 0.3624 0.3496 -0.0150 -0.0020 0.0111  474  ALA A C   
3430  O O   . ALA A 476  ? 0.3056 0.3235 0.3047 -0.0155 -0.0006 0.0162  474  ALA A O   
3431  C CB  . ALA A 476  ? 0.3340 0.3591 0.3444 -0.0163 -0.0070 0.0035  474  ALA A CB  
3432  N N   . PRO A 477  ? 0.3311 0.3423 0.3297 -0.0139 -0.0013 0.0098  475  PRO A N   
3433  C CA  . PRO A 477  ? 0.3159 0.3280 0.3082 -0.0135 0.0013  0.0142  475  PRO A CA  
3434  C C   . PRO A 477  ? 0.3190 0.3438 0.3082 -0.0138 0.0007  0.0134  475  PRO A C   
3435  O O   . PRO A 477  ? 0.3277 0.3608 0.3182 -0.0136 -0.0015 0.0073  475  PRO A O   
3436  C CB  . PRO A 477  ? 0.3572 0.3639 0.3482 -0.0123 0.0015  0.0115  475  PRO A CB  
3437  C CG  . PRO A 477  ? 0.3791 0.3789 0.3760 -0.0122 -0.0004 0.0080  475  PRO A CG  
3438  C CD  . PRO A 477  ? 0.3747 0.3803 0.3764 -0.0131 -0.0029 0.0046  475  PRO A CD  
3439  N N   . VAL A 478  ? 0.2923 0.3189 0.2777 -0.0142 0.0025  0.0197  476  VAL A N   
3440  C CA  . VAL A 478  ? 0.3234 0.3622 0.3059 -0.0148 0.0021  0.0210  476  VAL A CA  
3441  C C   . VAL A 478  ? 0.3822 0.4196 0.3603 -0.0148 0.0041  0.0258  476  VAL A C   
3442  O O   . VAL A 478  ? 0.4075 0.4361 0.3855 -0.0146 0.0058  0.0308  476  VAL A O   
3443  C CB  . VAL A 478  ? 0.3759 0.4192 0.3599 -0.0158 0.0016  0.0251  476  VAL A CB  
3444  C CG1 . VAL A 478  ? 0.3156 0.3724 0.2964 -0.0166 0.0010  0.0273  476  VAL A CG1 
3445  C CG2 . VAL A 478  ? 0.3326 0.3766 0.3216 -0.0159 -0.0004 0.0203  476  VAL A CG2 
3446  N N   . GLY A 479  ? 0.3895 0.4358 0.3646 -0.0149 0.0038  0.0240  477  GLY A N   
3447  C CA  . GLY A 479  ? 0.3898 0.4355 0.3616 -0.0153 0.0054  0.0288  477  GLY A CA  
3448  C C   . GLY A 479  ? 0.3808 0.4362 0.3498 -0.0153 0.0050  0.0253  477  GLY A C   
3449  O O   . GLY A 479  ? 0.3168 0.3779 0.2865 -0.0145 0.0037  0.0179  477  GLY A O   
3450  N N   . THR A 480  ? 0.3672 0.4247 0.3336 -0.0162 0.0062  0.0306  478  THR A N   
3451  C CA  . THR A 480  ? 0.3819 0.4490 0.3456 -0.0165 0.0063  0.0285  478  THR A CA  
3452  C C   . THR A 480  ? 0.4347 0.4941 0.3985 -0.0149 0.0068  0.0231  478  THR A C   
3453  O O   . THR A 480  ? 0.4474 0.4937 0.4129 -0.0138 0.0072  0.0223  478  THR A O   
3454  C CB  . THR A 480  ? 0.4378 0.5083 0.3997 -0.0183 0.0072  0.0367  478  THR A CB  
3455  O OG1 . THR A 480  ? 0.4641 0.5203 0.4269 -0.0179 0.0084  0.0403  478  THR A OG1 
3456  C CG2 . THR A 480  ? 0.4219 0.5000 0.3843 -0.0200 0.0063  0.0428  478  THR A CG2 
3457  N N   . HIS A 481  ? 0.4416 0.5101 0.4034 -0.0148 0.0068  0.0199  479  HIS A N   
3458  C CA  . HIS A 481  ? 0.4899 0.5523 0.4518 -0.0133 0.0072  0.0153  479  HIS A CA  
3459  C C   . HIS A 481  ? 0.4921 0.5415 0.4535 -0.0135 0.0088  0.0207  479  HIS A C   
3460  O O   . HIS A 481  ? 0.5110 0.5494 0.4736 -0.0120 0.0089  0.0180  479  HIS A O   
3461  C CB  . HIS A 481  ? 0.4267 0.5029 0.3865 -0.0134 0.0072  0.0120  479  HIS A CB  
3462  C CG  . HIS A 481  ? 0.4900 0.5800 0.4505 -0.0127 0.0056  0.0049  479  HIS A CG  
3463  N ND1 . HIS A 481  ? 0.4475 0.5528 0.4063 -0.0126 0.0055  0.0008  479  HIS A ND1 
3464  C CD2 . HIS A 481  ? 0.4690 0.5604 0.4318 -0.0120 0.0039  0.0006  479  HIS A CD2 
3465  C CE1 . HIS A 481  ? 0.5218 0.6376 0.4817 -0.0116 0.0037  -0.0061 479  HIS A CE1 
3466  N NE2 . HIS A 481  ? 0.4974 0.6046 0.4599 -0.0113 0.0026  -0.0064 479  HIS A NE2 
3467  N N   . GLU A 482  ? 0.5141 0.5649 0.4744 -0.0153 0.0096  0.0283  480  GLU A N   
3468  C CA  . GLU A 482  ? 0.5344 0.5733 0.4948 -0.0153 0.0108  0.0330  480  GLU A CA  
3469  C C   . GLU A 482  ? 0.5822 0.6080 0.5444 -0.0140 0.0110  0.0330  480  GLU A C   
3470  O O   . GLU A 482  ? 0.6093 0.6250 0.5715 -0.0128 0.0117  0.0315  480  GLU A O   
3471  C CB  . GLU A 482  ? 0.5860 0.6287 0.5464 -0.0175 0.0110  0.0413  480  GLU A CB  
3472  N N   . THR A 483  ? 0.5329 0.5597 0.4966 -0.0144 0.0105  0.0349  481  THR A N   
3473  C CA  . THR A 483  ? 0.5373 0.5534 0.5030 -0.0135 0.0109  0.0354  481  THR A CA  
3474  C C   . THR A 483  ? 0.5141 0.5247 0.4809 -0.0120 0.0105  0.0293  481  THR A C   
3475  O O   . THR A 483  ? 0.5531 0.5534 0.5205 -0.0110 0.0113  0.0295  481  THR A O   
3476  C CB  . THR A 483  ? 0.5106 0.5307 0.4781 -0.0142 0.0102  0.0382  481  THR A CB  
3477  O OG1 . THR A 483  ? 0.5497 0.5750 0.5168 -0.0157 0.0102  0.0445  481  THR A OG1 
3478  C CG2 . THR A 483  ? 0.5418 0.5517 0.5115 -0.0134 0.0108  0.0393  481  THR A CG2 
3479  N N   . LEU A 484  ? 0.5224 0.5405 0.4899 -0.0118 0.0090  0.0237  482  LEU A N   
3480  C CA  . LEU A 484  ? 0.5178 0.5309 0.4879 -0.0105 0.0079  0.0177  482  LEU A CA  
3481  C C   . LEU A 484  ? 0.5481 0.5530 0.5174 -0.0093 0.0086  0.0164  482  LEU A C   
3482  O O   . LEU A 484  ? 0.5561 0.5515 0.5273 -0.0085 0.0084  0.0158  482  LEU A O   
3483  C CB  . LEU A 484  ? 0.5221 0.5457 0.4934 -0.0102 0.0060  0.0110  482  LEU A CB  
3484  N N   . LEU A 485  ? 0.4979 0.5069 0.4645 -0.0093 0.0092  0.0165  483  LEU A N   
3485  C CA  . LEU A 485  ? 0.5581 0.5612 0.5241 -0.0081 0.0094  0.0144  483  LEU A CA  
3486  C C   . LEU A 485  ? 0.5660 0.5579 0.5311 -0.0079 0.0108  0.0190  483  LEU A C   
3487  O O   . LEU A 485  ? 0.5637 0.5492 0.5287 -0.0067 0.0108  0.0173  483  LEU A O   
3488  C CB  . LEU A 485  ? 0.4794 0.4913 0.4432 -0.0084 0.0097  0.0134  483  LEU A CB  
3489  C CG  . LEU A 485  ? 0.5544 0.5778 0.5191 -0.0079 0.0082  0.0068  483  LEU A CG  
3490  C CD1 . LEU A 485  ? 0.5463 0.5811 0.5083 -0.0088 0.0089  0.0074  483  LEU A CD1 
3491  C CD2 . LEU A 485  ? 0.5033 0.5216 0.4710 -0.0057 0.0066  0.0001  483  LEU A CD2 
3492  N N   . ALA A 486  ? 0.5592 0.5490 0.5238 -0.0088 0.0119  0.0244  484  ALA A N   
3493  C CA  . ALA A 486  ? 0.5748 0.5557 0.5385 -0.0083 0.0133  0.0281  484  ALA A CA  
3494  C C   . ALA A 486  ? 0.6298 0.6020 0.5947 -0.0072 0.0134  0.0271  484  ALA A C   
3495  O O   . ALA A 486  ? 0.6435 0.6093 0.6072 -0.0063 0.0141  0.0279  484  ALA A O   
3496  C CB  . ALA A 486  ? 0.5494 0.5308 0.5133 -0.0092 0.0141  0.0336  484  ALA A CB  
3497  N N   . TYR A 487  ? 0.5854 0.5577 0.5530 -0.0073 0.0125  0.0255  485  TYR A N   
3498  C CA  . TYR A 487  ? 0.6119 0.5767 0.5814 -0.0066 0.0124  0.0253  485  TYR A CA  
3499  C C   . TYR A 487  ? 0.6052 0.5707 0.5783 -0.0064 0.0101  0.0206  485  TYR A C   
3500  O O   . TYR A 487  ? 0.5753 0.5359 0.5515 -0.0065 0.0095  0.0210  485  TYR A O   
3501  C CB  . TYR A 487  ? 0.6723 0.6349 0.6431 -0.0071 0.0135  0.0293  485  TYR A CB  
3502  C CG  . TYR A 487  ? 0.6870 0.6478 0.6553 -0.0069 0.0153  0.0334  485  TYR A CG  
3503  C CD1 . TYR A 487  ? 0.6980 0.6535 0.6641 -0.0058 0.0163  0.0341  485  TYR A CD1 
3504  C CD2 . TYR A 487  ? 0.6524 0.6172 0.6212 -0.0075 0.0157  0.0362  485  TYR A CD2 
3505  C CE1 . TYR A 487  ? 0.7451 0.6990 0.7098 -0.0053 0.0176  0.0369  485  TYR A CE1 
3506  C CE2 . TYR A 487  ? 0.6910 0.6536 0.6587 -0.0071 0.0169  0.0394  485  TYR A CE2 
3507  C CZ  . TYR A 487  ? 0.7546 0.7118 0.7205 -0.0059 0.0178  0.0395  485  TYR A CZ  
3508  O OH  . TYR A 487  ? 0.7605 0.7156 0.7262 -0.0053 0.0186  0.0419  485  TYR A OH  
3509  N N   . LEU A 488  ? 0.5983 0.5700 0.5716 -0.0062 0.0087  0.0159  486  LEU A N   
3510  C CA  . LEU A 488  ? 0.5964 0.5689 0.5742 -0.0056 0.0062  0.0104  486  LEU A CA  
3511  C C   . LEU A 488  ? 0.5810 0.5450 0.5607 -0.0045 0.0052  0.0096  486  LEU A C   
3512  O O   . LEU A 488  ? 0.5333 0.4940 0.5182 -0.0044 0.0030  0.0073  486  LEU A O   
3513  C CB  . LEU A 488  ? 0.5318 0.5140 0.5092 -0.0051 0.0050  0.0050  486  LEU A CB  
3514  C CG  . LEU A 488  ? 0.5496 0.5345 0.5323 -0.0043 0.0019  -0.0022 486  LEU A CG  
3515  C CD1 . LEU A 488  ? 0.5252 0.5092 0.5120 -0.0053 0.0007  -0.0020 486  LEU A CD1 
3516  C CD2 . LEU A 488  ? 0.4886 0.4856 0.4702 -0.0037 0.0012  -0.0076 486  LEU A CD2 
3517  N N   . VAL A 489  ? 0.5423 0.5026 0.5185 -0.0038 0.0066  0.0116  487  VAL A N   
3518  C CA  . VAL A 489  ? 0.5717 0.5244 0.5493 -0.0028 0.0057  0.0117  487  VAL A CA  
3519  C C   . VAL A 489  ? 0.5866 0.5331 0.5668 -0.0036 0.0057  0.0156  487  VAL A C   
3520  O O   . VAL A 489  ? 0.5579 0.5003 0.5431 -0.0035 0.0035  0.0144  487  VAL A O   
3521  C CB  . VAL A 489  ? 0.5806 0.5311 0.5535 -0.0021 0.0073  0.0137  487  VAL A CB  
3522  C CG1 . VAL A 489  ? 0.5776 0.5203 0.5513 -0.0013 0.0067  0.0154  487  VAL A CG1 
3523  C CG2 . VAL A 489  ? 0.5441 0.5008 0.5158 -0.0013 0.0068  0.0094  487  VAL A CG2 
3524  N N   . ARG A 490  ? 0.6031 0.5491 0.5807 -0.0045 0.0081  0.0205  488  ARG A N   
3525  C CA  . ARG A 490  ? 0.5860 0.5278 0.5660 -0.0053 0.0085  0.0244  488  ARG A CA  
3526  C C   . ARG A 490  ? 0.5985 0.5413 0.5847 -0.0064 0.0062  0.0224  488  ARG A C   
3527  O O   . ARG A 490  ? 0.5561 0.4943 0.5466 -0.0070 0.0048  0.0240  488  ARG A O   
3528  C CB  . ARG A 490  ? 0.5580 0.5009 0.5346 -0.0058 0.0113  0.0289  488  ARG A CB  
3529  C CG  . ARG A 490  ? 0.5977 0.5372 0.5759 -0.0064 0.0123  0.0333  488  ARG A CG  
3530  C CD  . ARG A 490  ? 0.5631 0.5046 0.5389 -0.0065 0.0150  0.0368  488  ARG A CD  
3531  N NE  . ARG A 490  ? 0.5937 0.5399 0.5713 -0.0074 0.0148  0.0363  488  ARG A NE  
3532  C CZ  . ARG A 490  ? 0.6325 0.5819 0.6077 -0.0071 0.0161  0.0371  488  ARG A CZ  
3533  N NH1 . ARG A 490  ? 0.5395 0.4875 0.5110 -0.0059 0.0176  0.0383  488  ARG A NH1 
3534  N NH2 . ARG A 490  ? 0.5646 0.5188 0.5417 -0.0079 0.0156  0.0369  488  ARG A NH2 
3535  N N   . ARG A 491  ? 0.5751 0.5242 0.5622 -0.0067 0.0054  0.0189  489  ARG A N   
3536  C CA  . ARG A 491  ? 0.5770 0.5276 0.5702 -0.0076 0.0030  0.0165  489  ARG A CA  
3537  C C   . ARG A 491  ? 0.5997 0.5475 0.5987 -0.0069 -0.0005 0.0116  489  ARG A C   
3538  O O   . ARG A 491  ? 0.5781 0.5230 0.5837 -0.0079 -0.0028 0.0113  489  ARG A O   
3539  C CB  . ARG A 491  ? 0.5553 0.5146 0.5476 -0.0080 0.0030  0.0138  489  ARG A CB  
3540  N N   . LEU A 492  ? 0.6142 0.5627 0.6115 -0.0053 -0.0012 0.0078  490  LEU A N   
3541  C CA  . LEU A 492  ? 0.6195 0.5653 0.6230 -0.0042 -0.0049 0.0027  490  LEU A CA  
3542  C C   . LEU A 492  ? 0.6327 0.5692 0.6394 -0.0045 -0.0058 0.0070  490  LEU A C   
3543  O O   . LEU A 492  ? 0.6118 0.5443 0.6263 -0.0047 -0.0093 0.0053  490  LEU A O   
3544  C CB  . LEU A 492  ? 0.5725 0.5225 0.5733 -0.0022 -0.0052 -0.0025 490  LEU A CB  
3545  C CG  . LEU A 492  ? 0.5540 0.5149 0.5526 -0.0019 -0.0049 -0.0075 490  LEU A CG  
3546  C CD1 . LEU A 492  ? 0.5817 0.5467 0.5758 -0.0004 -0.0039 -0.0098 490  LEU A CD1 
3547  C CD2 . LEU A 492  ? 0.5160 0.4808 0.5218 -0.0013 -0.0086 -0.0149 490  LEU A CD2 
3548  N N   . LEU A 493  ? 0.6053 0.5388 0.6064 -0.0045 -0.0030 0.0127  491  LEU A N   
3549  C CA  . LEU A 493  ? 0.6165 0.5427 0.6196 -0.0049 -0.0036 0.0175  491  LEU A CA  
3550  C C   . LEU A 493  ? 0.6230 0.5470 0.6312 -0.0070 -0.0042 0.0218  491  LEU A C   
3551  O O   . LEU A 493  ? 0.6438 0.5629 0.6590 -0.0077 -0.0071 0.0230  491  LEU A O   
3552  C CB  . LEU A 493  ? 0.6147 0.5398 0.6101 -0.0044 -0.0003 0.0222  491  LEU A CB  
3553  C CG  . LEU A 493  ? 0.6194 0.5457 0.6104 -0.0024 0.0000  0.0190  491  LEU A CG  
3554  C CD1 . LEU A 493  ? 0.6206 0.5457 0.6048 -0.0021 0.0031  0.0237  491  LEU A CD1 
3555  C CD2 . LEU A 493  ? 0.5903 0.5128 0.5864 -0.0011 -0.0035 0.0158  491  LEU A CD2 
3556  N N   . GLY A 496  ? 0.6839 0.6020 0.7159 -0.0052 -0.0169 0.0065  494  GLY A N   
3557  C CA  . GLY A 496  ? 0.6518 0.5695 0.6837 -0.0026 -0.0186 0.0014  494  GLY A CA  
3558  C C   . GLY A 496  ? 0.7325 0.6432 0.7648 -0.0021 -0.0193 0.0064  494  GLY A C   
3559  O O   . GLY A 496  ? 0.7580 0.6668 0.7932 0.0000  -0.0220 0.0023  494  GLY A O   
3560  N N   . ALA A 497  ? 0.7325 0.6401 0.7618 -0.0040 -0.0170 0.0151  495  ALA A N   
3561  C CA  . ALA A 497  ? 0.7005 0.6024 0.7299 -0.0038 -0.0177 0.0208  495  ALA A CA  
3562  C C   . ALA A 497  ? 0.6787 0.5742 0.7201 -0.0042 -0.0232 0.0208  495  ALA A C   
3563  O O   . ALA A 497  ? 0.6844 0.5790 0.7340 -0.0054 -0.0260 0.0185  495  ALA A O   
3564  C CB  . ALA A 497  ? 0.6326 0.5345 0.6563 -0.0058 -0.0139 0.0298  495  ALA A CB  
3565  N N   . ASN A 498  ? 0.6564 0.5471 0.6992 -0.0033 -0.0251 0.0237  496  ASN A N   
3566  C CA  . ASN A 498  ? 0.6780 0.5619 0.7330 -0.0036 -0.0308 0.0244  496  ASN A CA  
3567  C C   . ASN A 498  ? 0.6950 0.5762 0.7568 -0.0071 -0.0320 0.0311  496  ASN A C   
3568  O O   . ASN A 498  ? 0.6659 0.5428 0.7398 -0.0078 -0.0370 0.0291  496  ASN A O   
3569  C CB  . ASN A 498  ? 0.7032 0.5828 0.7575 -0.0024 -0.0321 0.0288  496  ASN A CB  
3570  N N   . SER A 499  ? 0.6785 0.5626 0.7333 -0.0093 -0.0275 0.0385  497  SER A N   
3571  C CA  . SER A 499  ? 0.6708 0.5537 0.7312 -0.0128 -0.0280 0.0456  497  SER A CA  
3572  C C   . SER A 499  ? 0.6249 0.5112 0.6881 -0.0141 -0.0276 0.0413  497  SER A C   
3573  O O   . SER A 499  ? 0.6151 0.5002 0.6854 -0.0171 -0.0290 0.0459  497  SER A O   
3574  C CB  . SER A 499  ? 0.6483 0.5342 0.7002 -0.0144 -0.0233 0.0552  497  SER A CB  
3575  O OG  . SER A 499  ? 0.5865 0.4787 0.6269 -0.0133 -0.0179 0.0529  497  SER A OG  
3576  N N   . SER A 500  ? 0.6088 0.4998 0.6670 -0.0120 -0.0260 0.0329  498  SER A N   
3577  C CA  . SER A 500  ? 0.5978 0.4932 0.6573 -0.0130 -0.0254 0.0290  498  SER A CA  
3578  C C   . SER A 500  ? 0.6250 0.5172 0.6980 -0.0136 -0.0312 0.0240  498  SER A C   
3579  O O   . SER A 500  ? 0.5971 0.4850 0.6772 -0.0119 -0.0357 0.0193  498  SER A O   
3580  C CB  . SER A 500  ? 0.6098 0.5120 0.6605 -0.0106 -0.0224 0.0219  498  SER A CB  
3581  O OG  . SER A 500  ? 0.6567 0.5617 0.6959 -0.0102 -0.0173 0.0263  498  SER A OG  
3582  N N   . PHE A 501  ? 0.5490 0.4435 0.6260 -0.0159 -0.0313 0.0244  499  PHE A N   
3583  C CA  . PHE A 501  ? 0.5979 0.4894 0.6886 -0.0168 -0.0371 0.0196  499  PHE A CA  
3584  C C   . PHE A 501  ? 0.6307 0.5253 0.7233 -0.0136 -0.0397 0.0071  499  PHE A C   
3585  O O   . PHE A 501  ? 0.6309 0.5211 0.7344 -0.0124 -0.0454 0.0016  499  PHE A O   
3586  C CB  . PHE A 501  ? 0.5269 0.4213 0.6208 -0.0200 -0.0363 0.0227  499  PHE A CB  
3587  C CG  . PHE A 501  ? 0.5380 0.4291 0.6468 -0.0213 -0.0425 0.0182  499  PHE A CG  
3588  C CD1 . PHE A 501  ? 0.5428 0.4265 0.6635 -0.0240 -0.0466 0.0244  499  PHE A CD1 
3589  C CD2 . PHE A 501  ? 0.5279 0.4239 0.6393 -0.0200 -0.0444 0.0078  499  PHE A CD2 
3590  C CE1 . PHE A 501  ? 0.5387 0.4189 0.6744 -0.0253 -0.0528 0.0202  499  PHE A CE1 
3591  C CE2 . PHE A 501  ? 0.5145 0.4077 0.6403 -0.0210 -0.0504 0.0029  499  PHE A CE2 
3592  C CZ  . PHE A 501  ? 0.5305 0.4153 0.6688 -0.0237 -0.0547 0.0090  499  PHE A CZ  
3593  N N   . VAL A 502  ? 0.6084 0.5112 0.6910 -0.0120 -0.0359 0.0025  500  VAL A N   
3594  C CA  . VAL A 502  ? 0.6372 0.5450 0.7215 -0.0092 -0.0382 -0.0093 500  VAL A CA  
3595  C C   . VAL A 502  ? 0.6690 0.5744 0.7536 -0.0060 -0.0400 -0.0134 500  VAL A C   
3596  O O   . VAL A 502  ? 0.7124 0.6193 0.8035 -0.0036 -0.0441 -0.0233 500  VAL A O   
3597  C CB  . VAL A 502  ? 0.5897 0.5078 0.6634 -0.0087 -0.0338 -0.0122 500  VAL A CB  
3598  C CG1 . VAL A 502  ? 0.5525 0.4725 0.6243 -0.0118 -0.0311 -0.0057 500  VAL A CG1 
3599  C CG2 . VAL A 502  ? 0.6455 0.5667 0.7071 -0.0068 -0.0294 -0.0109 500  VAL A CG2 
3600  N N   . HIS A 503  ? 0.6238 0.5257 0.7016 -0.0059 -0.0373 -0.0065 501  HIS A N   
3601  C CA  . HIS A 503  ? 0.6418 0.5404 0.7209 -0.0031 -0.0394 -0.0094 501  HIS A CA  
3602  C C   . HIS A 503  ? 0.6924 0.5823 0.7861 -0.0032 -0.0459 -0.0098 501  HIS A C   
3603  O O   . HIS A 503  ? 0.6922 0.5806 0.7920 -0.0003 -0.0499 -0.0171 501  HIS A O   
3604  C CB  . HIS A 503  ? 0.6494 0.5465 0.7182 -0.0032 -0.0350 -0.0013 501  HIS A CB  
3605  C CG  . HIS A 503  ? 0.6722 0.5664 0.7415 -0.0005 -0.0368 -0.0035 501  HIS A CG  
3606  N ND1 . HIS A 503  ? 0.6883 0.5741 0.7662 -0.0005 -0.0411 -0.0001 501  HIS A ND1 
3607  C CD2 . HIS A 503  ? 0.6638 0.5626 0.7262 0.0023  -0.0351 -0.0085 501  HIS A CD2 
3608  C CE1 . HIS A 503  ? 0.6801 0.5654 0.7565 0.0024  -0.0420 -0.0032 501  HIS A CE1 
3609  N NE2 . HIS A 503  ? 0.6601 0.5534 0.7271 0.0041  -0.0383 -0.0085 501  HIS A NE2 
3610  N N   . ARG A 504  ? 0.6667 0.5510 0.7668 -0.0066 -0.0473 -0.0021 502  ARG A N   
3611  C CA  . ARG A 504  ? 0.6493 0.5247 0.7640 -0.0072 -0.0537 -0.0006 502  ARG A CA  
3612  C C   . ARG A 504  ? 0.6631 0.5380 0.7910 -0.0069 -0.0594 -0.0098 502  ARG A C   
3613  O O   . ARG A 504  ? 0.6405 0.5101 0.7804 -0.0051 -0.0655 -0.0150 502  ARG A O   
3614  C CB  . ARG A 504  ? 0.6488 0.5191 0.7650 -0.0113 -0.0529 0.0128  502  ARG A CB  
3615  C CG  . ARG A 504  ? 0.6901 0.5601 0.7953 -0.0111 -0.0486 0.0212  502  ARG A CG  
3616  C CD  . ARG A 504  ? 0.6882 0.5578 0.7908 -0.0150 -0.0457 0.0338  502  ARG A CD  
3617  N NE  . ARG A 504  ? 0.6917 0.5555 0.8086 -0.0182 -0.0507 0.0386  502  ARG A NE  
3618  C CZ  . ARG A 504  ? 0.7146 0.5710 0.8414 -0.0189 -0.0556 0.0434  502  ARG A CZ  
3619  N NH1 . ARG A 504  ? 0.6695 0.5233 0.7933 -0.0165 -0.0562 0.0443  502  ARG A NH1 
3620  N NH2 . ARG A 504  ? 0.6952 0.5466 0.8360 -0.0221 -0.0603 0.0478  502  ARG A NH2 
3621  N N   . ILE A 505  ? 0.6575 0.5384 0.7839 -0.0084 -0.0577 -0.0124 503  ILE A N   
3622  C CA  . ILE A 505  ? 0.6465 0.5284 0.7848 -0.0078 -0.0631 -0.0225 503  ILE A CA  
3623  C C   . ILE A 505  ? 0.6891 0.5753 0.8283 -0.0030 -0.0654 -0.0355 503  ILE A C   
3624  O O   . ILE A 505  ? 0.6673 0.5514 0.8197 -0.0014 -0.0717 -0.0444 503  ILE A O   
3625  C CB  . ILE A 505  ? 0.6033 0.4926 0.7380 -0.0099 -0.0604 -0.0234 503  ILE A CB  
3626  N N   . ASN A 506  ? 0.6903 0.5827 0.8162 -0.0008 -0.0605 -0.0367 504  ASN A N   
3627  C CA  . ASN A 506  ? 0.6977 0.5959 0.8230 0.0037  -0.0619 -0.0482 504  ASN A CA  
3628  C C   . ASN A 506  ? 0.7341 0.6259 0.8614 0.0060  -0.0637 -0.0469 504  ASN A C   
3629  O O   . ASN A 506  ? 0.7945 0.6918 0.9185 0.0096  -0.0634 -0.0547 504  ASN A O   
3630  C CB  . ASN A 506  ? 0.7175 0.6277 0.8277 0.0046  -0.0557 -0.0506 504  ASN A CB  
3631  N N   . ASP A 507  ? 0.7440 0.6252 0.8768 0.0039  -0.0656 -0.0372 505  ASP A N   
3632  C CA  . ASP A 507  ? 0.7188 0.5934 0.8549 0.0059  -0.0681 -0.0353 505  ASP A CA  
3633  C C   . ASP A 507  ? 0.7746 0.6401 0.9297 0.0063  -0.0765 -0.0382 505  ASP A C   
3634  O O   . ASP A 507  ? 0.7222 0.5806 0.8853 0.0027  -0.0789 -0.0305 505  ASP A O   
3635  C CB  . ASP A 507  ? 0.7345 0.6049 0.8621 0.0034  -0.0641 -0.0214 505  ASP A CB  
3636  N N   . PRO A 508  ? 0.7818 0.6472 0.9451 0.0106  -0.0813 -0.0489 506  PRO A N   
3637  C CA  . PRO A 508  ? 0.7918 0.6483 0.9748 0.0113  -0.0900 -0.0529 506  PRO A CA  
3638  C C   . PRO A 508  ? 0.7323 0.5766 0.9228 0.0092  -0.0933 -0.0409 506  PRO A C   
3639  O O   . PRO A 508  ? 0.7777 0.6133 0.9852 0.0084  -0.1005 -0.0409 506  PRO A O   
3640  C CB  . PRO A 508  ? 0.7765 0.6376 0.9641 0.0170  -0.0933 -0.0676 506  PRO A CB  
3641  C CG  . PRO A 508  ? 0.8135 0.6883 0.9843 0.0185  -0.0862 -0.0726 506  PRO A CG  
3642  C CD  . PRO A 508  ? 0.7966 0.6712 0.9523 0.0150  -0.0791 -0.0589 506  PRO A CD  
3643  N N   . LYS A 509  ? 0.7699 0.6136 0.9485 0.0082  -0.0885 -0.0305 507  LYS A N   
3644  C CA  . LYS A 509  ? 0.7819 0.6156 0.9664 0.0060  -0.0912 -0.0181 507  LYS A CA  
3645  C C   . LYS A 509  ? 0.7634 0.5931 0.9508 0.0004  -0.0908 -0.0061 507  LYS A C   
3646  O O   . LYS A 509  ? 0.7738 0.5957 0.9679 -0.0020 -0.0937 0.0049  507  LYS A O   
3647  C CB  . LYS A 509  ? 0.7688 0.6046 0.9393 0.0070  -0.0862 -0.0115 507  LYS A CB  
3648  N N   . VAL A 510  ? 0.7521 0.5876 0.9351 -0.0017 -0.0874 -0.0078 508  VAL A N   
3649  C CA  . VAL A 510  ? 0.7096 0.5433 0.8933 -0.0071 -0.0858 0.0034  508  VAL A CA  
3650  C C   . VAL A 510  ? 0.6617 0.4922 0.8617 -0.0085 -0.0919 -0.0020 508  VAL A C   
3651  O O   . VAL A 510  ? 0.6737 0.5101 0.8735 -0.0068 -0.0918 -0.0136 508  VAL A O   
3652  C CB  . VAL A 510  ? 0.6874 0.5305 0.8532 -0.0086 -0.0770 0.0067  508  VAL A CB  
3653  C CG1 . VAL A 510  ? 0.6680 0.5100 0.8343 -0.0139 -0.0752 0.0189  508  VAL A CG1 
3654  C CG2 . VAL A 510  ? 0.6769 0.5236 0.8272 -0.0066 -0.0715 0.0098  508  VAL A CG2 
3655  N N   . SER A 511  ? 0.6160 0.4375 0.8302 -0.0119 -0.0973 0.0065  509  SER A N   
3656  C CA  . SER A 511  ? 0.6173 0.4379 0.8464 -0.0136 -0.1026 0.0025  509  SER A CA  
3657  C C   . SER A 511  ? 0.6166 0.4397 0.8425 -0.0180 -0.0991 0.0069  509  SER A C   
3658  O O   . SER A 511  ? 0.6129 0.4412 0.8241 -0.0200 -0.0918 0.0157  509  SER A O   
3659  C CB  . SER A 511  ? 0.6683 0.4858 0.9096 -0.0155 -0.1075 0.0111  509  SER A CB  
3660  O OG  . SER A 511  ? 0.6298 0.4474 0.8650 -0.0201 -0.1037 0.0272  509  SER A OG  
3661  N N   . ILE A 512  ? 0.6390 0.4631 0.8763 -0.0189 -0.1032 0.0003  510  ILE A N   
3662  C CA  . ILE A 512  ? 0.6213 0.4478 0.8577 -0.0234 -0.1006 0.0049  510  ILE A CA  
3663  C C   . ILE A 512  ? 0.6558 0.4818 0.8913 -0.0283 -0.0984 0.0222  510  ILE A C   
3664  O O   . ILE A 512  ? 0.6364 0.4652 0.8628 -0.0317 -0.0928 0.0303  510  ILE A O   
3665  C CB  . ILE A 512  ? 0.6047 0.4327 0.8550 -0.0234 -0.1062 -0.0053 510  ILE A CB  
3666  C CG1 . ILE A 512  ? 0.5905 0.4220 0.8404 -0.0181 -0.1080 -0.0232 510  ILE A CG1 
3667  C CG2 . ILE A 512  ? 0.6027 0.4336 0.8524 -0.0282 -0.1037 -0.0004 510  ILE A CG2 
3668  C CD1 . ILE A 512  ? 0.6306 0.4656 0.8914 -0.0180 -0.1125 -0.0344 510  ILE A CD1 
3669  N N   . ASP A 513  ? 0.6355 0.4586 0.8804 -0.0287 -0.1027 0.0280  511  ASP A N   
3670  C CA  . ASP A 513  ? 0.5893 0.4133 0.8338 -0.0333 -0.1009 0.0441  511  ASP A CA  
3671  C C   . ASP A 513  ? 0.6202 0.4468 0.8474 -0.0341 -0.0934 0.0534  511  ASP A C   
3672  O O   . ASP A 513  ? 0.6311 0.4618 0.8531 -0.0382 -0.0892 0.0646  511  ASP A O   
3673  C CB  . ASP A 513  ? 0.6556 0.4762 0.9123 -0.0330 -0.1071 0.0478  511  ASP A CB  
3674  N N   . GLU A 514  ? 0.6145 0.4397 0.8329 -0.0301 -0.0916 0.0486  512  GLU A N   
3675  C CA  . GLU A 514  ? 0.6289 0.4568 0.8306 -0.0304 -0.0845 0.0560  512  GLU A CA  
3676  C C   . GLU A 514  ? 0.6298 0.4647 0.8203 -0.0313 -0.0782 0.0540  512  GLU A C   
3677  O O   . GLU A 514  ? 0.6151 0.4558 0.7927 -0.0329 -0.0716 0.0625  512  GLU A O   
3678  C CB  . GLU A 514  ? 0.6545 0.4799 0.8498 -0.0255 -0.0843 0.0502  512  GLU A CB  
3679  C CG  . GLU A 514  ? 0.6766 0.4992 0.8778 -0.0243 -0.0885 0.0540  512  GLU A CG  
3680  C CD  . GLU A 514  ? 0.7108 0.5311 0.9074 -0.0191 -0.0890 0.0465  512  GLU A CD  
3681  O OE1 . GLU A 514  ? 0.7622 0.5855 0.9490 -0.0163 -0.0854 0.0379  512  GLU A OE1 
3682  O OE2 . GLU A 514  ? 0.7667 0.5848 0.9681 -0.0177 -0.0925 0.0489  512  GLU A OE2 
3683  N N   . LEU A 515  ? 0.6282 0.4655 0.8219 -0.0299 -0.0795 0.0421  513  LEU A N   
3684  C CA  . LEU A 515  ? 0.6720 0.5188 0.8527 -0.0297 -0.0730 0.0385  513  LEU A CA  
3685  C C   . LEU A 515  ? 0.6082 0.4576 0.7926 -0.0347 -0.0717 0.0461  513  LEU A C   
3686  O O   . LEU A 515  ? 0.5841 0.4412 0.7561 -0.0355 -0.0651 0.0489  513  LEU A O   
3687  C CB  . LEU A 515  ? 0.6416 0.4918 0.8230 -0.0259 -0.0746 0.0227  513  LEU A CB  
3688  C CG  . LEU A 515  ? 0.6187 0.4708 0.7918 -0.0207 -0.0735 0.0139  513  LEU A CG  
3689  C CD1 . LEU A 515  ? 0.6036 0.4603 0.7797 -0.0175 -0.0759 -0.0014 513  LEU A CD1 
3690  C CD2 . LEU A 515  ? 0.5924 0.4512 0.7462 -0.0199 -0.0653 0.0186  513  LEU A CD2 
3691  N N   . ILE A 516  ? 0.5753 0.4182 0.7770 -0.0380 -0.0780 0.0494  514  ILE A N   
3692  C CA  . ILE A 516  ? 0.5935 0.4388 0.8004 -0.0431 -0.0774 0.0570  514  ILE A CA  
3693  C C   . ILE A 516  ? 0.5932 0.4381 0.8002 -0.0472 -0.0757 0.0733  514  ILE A C   
3694  O O   . ILE A 516  ? 0.5787 0.4273 0.7913 -0.0512 -0.0758 0.0802  514  ILE A O   
3695  C CB  . ILE A 516  ? 0.5616 0.4019 0.7876 -0.0448 -0.0851 0.0508  514  ILE A CB  
3696  C CG1 . ILE A 516  ? 0.6090 0.4447 0.8470 -0.0441 -0.0913 0.0529  514  ILE A CG1 
3697  C CG2 . ILE A 516  ? 0.5943 0.4381 0.8188 -0.0404 -0.0862 0.0341  514  ILE A CG2 
3698  C CD1 . ILE A 516  ? 0.5818 0.4161 0.8370 -0.0452 -0.0981 0.0477  514  ILE A CD1 
3699  N N   . ALA A 517  ? 0.5819 0.4263 0.7804 -0.0454 -0.0735 0.0783  515  ALA A N   
3700  C CA  . ALA A 517  ? 0.6145 0.4636 0.8092 -0.0481 -0.0708 0.0921  515  ALA A CA  
3701  C C   . ALA A 517  ? 0.5650 0.4221 0.7497 -0.0511 -0.0638 0.0996  515  ALA A C   
3702  O O   . ALA A 517  ? 0.5421 0.4026 0.7152 -0.0493 -0.0588 0.0952  515  ALA A O   
3703  C CB  . ALA A 517  ? 0.6297 0.4773 0.8162 -0.0452 -0.0697 0.0946  515  ALA A CB  
3704  N N   . ASP A 518  ? 0.5829 0.4456 0.7708 -0.0549 -0.0631 0.1099  516  ASP A N   
3705  C CA  . ASP A 518  ? 0.5652 0.4370 0.7447 -0.0577 -0.0566 0.1172  516  ASP A CA  
3706  C C   . ASP A 518  ? 0.5215 0.3987 0.6856 -0.0565 -0.0505 0.1238  516  ASP A C   
3707  O O   . ASP A 518  ? 0.5007 0.3806 0.6642 -0.0572 -0.0508 0.1316  516  ASP A O   
3708  C CB  . ASP A 518  ? 0.5630 0.4396 0.7522 -0.0622 -0.0583 0.1253  516  ASP A CB  
3709  C CG  . ASP A 518  ? 0.5821 0.4687 0.7640 -0.0649 -0.0519 0.1316  516  ASP A CG  
3710  O OD1 . ASP A 518  ? 0.5348 0.4246 0.7047 -0.0634 -0.0463 0.1293  516  ASP A OD1 
3711  O OD2 . ASP A 518  ? 0.6144 0.5063 0.8034 -0.0686 -0.0526 0.1387  516  ASP A OD2 
3712  N N   . PRO A 519  ? 0.5122 0.3920 0.6638 -0.0547 -0.0450 0.1210  517  PRO A N   
3713  C CA  . PRO A 519  ? 0.5191 0.4046 0.6563 -0.0532 -0.0393 0.1266  517  PRO A CA  
3714  C C   . PRO A 519  ? 0.5080 0.4044 0.6416 -0.0562 -0.0353 0.1373  517  PRO A C   
3715  O O   . PRO A 519  ? 0.4932 0.3943 0.6183 -0.0555 -0.0325 0.1431  517  PRO A O   
3716  C CB  . PRO A 519  ? 0.5171 0.4069 0.6405 -0.0492 -0.0339 0.1169  517  PRO A CB  
3717  C CG  . PRO A 519  ? 0.5197 0.4102 0.6496 -0.0504 -0.0350 0.1108  517  PRO A CG  
3718  C CD  . PRO A 519  ? 0.5249 0.4068 0.6726 -0.0528 -0.0429 0.1106  517  PRO A CD  
3719  N N   . VAL A 520  ? 0.5244 0.4253 0.6644 -0.0596 -0.0351 0.1399  518  VAL A N   
3720  C CA  . VAL A 520  ? 0.5293 0.4413 0.6670 -0.0626 -0.0316 0.1497  518  VAL A CA  
3721  C C   . VAL A 520  ? 0.5242 0.4366 0.6684 -0.0641 -0.0353 0.1568  518  VAL A C   
3722  O O   . VAL A 520  ? 0.4932 0.4135 0.6301 -0.0644 -0.0322 0.1642  518  VAL A O   
3723  C CB  . VAL A 520  ? 0.5216 0.4379 0.6665 -0.0659 -0.0312 0.1504  518  VAL A CB  
3724  C CG1 . VAL A 520  ? 0.5148 0.4437 0.6574 -0.0688 -0.0274 0.1602  518  VAL A CG1 
3725  C CG2 . VAL A 520  ? 0.5148 0.4308 0.6541 -0.0644 -0.0278 0.1433  518  VAL A CG2 
3726  N N   . GLU A 521  ? 0.5368 0.4409 0.6950 -0.0650 -0.0424 0.1546  519  GLU A N   
3727  C CA  . GLU A 521  ? 0.5732 0.4774 0.7389 -0.0666 -0.0465 0.1618  519  GLU A CA  
3728  C C   . GLU A 521  ? 0.5879 0.4893 0.7466 -0.0635 -0.0467 0.1620  519  GLU A C   
3729  O O   . GLU A 521  ? 0.5545 0.4608 0.7124 -0.0646 -0.0469 0.1704  519  GLU A O   
3730  C CB  . GLU A 521  ? 0.5440 0.4402 0.7275 -0.0682 -0.0543 0.1590  519  GLU A CB  
3731  C CG  . GLU A 521  ? 0.6066 0.5064 0.7983 -0.0717 -0.0546 0.1599  519  GLU A CG  
3732  C CD  . GLU A 521  ? 0.6687 0.5813 0.8566 -0.0751 -0.0501 0.1708  519  GLU A CD  
3733  O OE1 . GLU A 521  ? 0.6159 0.5331 0.8023 -0.0760 -0.0501 0.1792  519  GLU A OE1 
3734  O OE2 . GLU A 521  ? 0.6582 0.5766 0.8447 -0.0768 -0.0467 0.1709  519  GLU A OE2 
3735  N N   . VAL A 522  ? 0.5188 0.4127 0.6722 -0.0596 -0.0467 0.1532  520  VAL A N   
3736  C CA  . VAL A 522  ? 0.5447 0.4364 0.6906 -0.0564 -0.0465 0.1532  520  VAL A CA  
3737  C C   . VAL A 522  ? 0.5955 0.4978 0.7265 -0.0563 -0.0397 0.1597  520  VAL A C   
3738  O O   . VAL A 522  ? 0.5631 0.4686 0.6909 -0.0561 -0.0398 0.1657  520  VAL A O   
3739  C CB  . VAL A 522  ? 0.5433 0.4258 0.6865 -0.0523 -0.0476 0.1420  520  VAL A CB  
3740  C CG1 . VAL A 522  ? 0.5727 0.4532 0.7082 -0.0491 -0.0474 0.1422  520  VAL A CG1 
3741  C CG2 . VAL A 522  ? 0.5402 0.4132 0.6986 -0.0521 -0.0547 0.1345  520  VAL A CG2 
3742  N N   . VAL A 523  ? 0.4963 0.4048 0.6184 -0.0563 -0.0338 0.1586  521  VAL A N   
3743  C CA  . VAL A 523  ? 0.5105 0.4300 0.6191 -0.0559 -0.0274 0.1639  521  VAL A CA  
3744  C C   . VAL A 523  ? 0.5452 0.4749 0.6569 -0.0595 -0.0269 0.1742  521  VAL A C   
3745  O O   . VAL A 523  ? 0.5344 0.4715 0.6387 -0.0591 -0.0246 0.1799  521  VAL A O   
3746  C CB  . VAL A 523  ? 0.5058 0.4294 0.6054 -0.0548 -0.0216 0.1597  521  VAL A CB  
3747  C CG1 . VAL A 523  ? 0.4640 0.4010 0.5521 -0.0550 -0.0152 0.1655  521  VAL A CG1 
3748  C CG2 . VAL A 523  ? 0.4823 0.3979 0.5760 -0.0509 -0.0213 0.1509  521  VAL A CG2 
3749  N N   . ARG A 524  ? 0.5226 0.4536 0.6453 -0.0630 -0.0291 0.1768  522  ARG A N   
3750  C CA  . ARG A 524  ? 0.5696 0.5112 0.6958 -0.0667 -0.0286 0.1870  522  ARG A CA  
3751  C C   . ARG A 524  ? 0.5897 0.5309 0.7196 -0.0672 -0.0325 0.1934  522  ARG A C   
3752  O O   . ARG A 524  ? 0.6156 0.5678 0.7420 -0.0688 -0.0303 0.2018  522  ARG A O   
3753  C CB  . ARG A 524  ? 0.5763 0.5176 0.7159 -0.0704 -0.0315 0.1884  522  ARG A CB  
3754  C CG  . ARG A 524  ? 0.5881 0.5409 0.7320 -0.0744 -0.0312 0.1993  522  ARG A CG  
3755  C CD  . ARG A 524  ? 0.5837 0.5334 0.7441 -0.0782 -0.0365 0.2013  522  ARG A CD  
3756  N NE  . ARG A 524  ? 0.5939 0.5382 0.7575 -0.0779 -0.0364 0.1933  522  ARG A NE  
3757  C CZ  . ARG A 524  ? 0.5611 0.5131 0.7207 -0.0789 -0.0317 0.1931  522  ARG A CZ  
3758  N NH1 . ARG A 524  ? 0.5864 0.5520 0.7383 -0.0800 -0.0263 0.1997  522  ARG A NH1 
3759  N NH2 . ARG A 524  ? 0.6163 0.5627 0.7801 -0.0788 -0.0324 0.1858  522  ARG A NH2 
3760  N N   . ALA A 525  ? 0.5687 0.4981 0.7057 -0.0657 -0.0382 0.1893  523  ALA A N   
3761  C CA  . ALA A 525  ? 0.5712 0.4991 0.7143 -0.0663 -0.0429 0.1952  523  ALA A CA  
3762  C C   . ALA A 525  ? 0.6302 0.5575 0.7621 -0.0628 -0.0413 0.1943  523  ALA A C   
3763  O O   . ALA A 525  ? 0.6340 0.5598 0.7702 -0.0630 -0.0452 0.1988  523  ALA A O   
3764  C CB  . ALA A 525  ? 0.5986 0.5142 0.7577 -0.0667 -0.0507 0.1913  523  ALA A CB  
3765  N N   . MET A 526  ? 0.5804 0.5089 0.6986 -0.0596 -0.0359 0.1887  524  MET A N   
3766  C CA  . MET A 526  ? 0.6099 0.5386 0.7173 -0.0563 -0.0343 0.1880  524  MET A CA  
3767  C C   . MET A 526  ? 0.6377 0.5798 0.7386 -0.0579 -0.0313 0.1977  524  MET A C   
3768  O O   . MET A 526  ? 0.5588 0.5113 0.6597 -0.0607 -0.0285 0.2031  524  MET A O   
3769  C CB  . MET A 526  ? 0.6291 0.5561 0.7242 -0.0527 -0.0295 0.1798  524  MET A CB  
3770  C CG  . MET A 526  ? 0.6128 0.5264 0.7129 -0.0504 -0.0329 0.1699  524  MET A CG  
3771  S SD  . MET A 526  ? 0.8571 0.7684 0.9431 -0.0459 -0.0280 0.1610  524  MET A SD  
3772  C CE  . MET A 526  ? 0.6541 0.5786 0.7302 -0.0473 -0.0203 0.1640  524  MET A CE  
3773  N N   . PRO A 527  ? 0.6147 0.5574 0.7104 -0.0560 -0.0321 0.1999  525  PRO A N   
3774  C CA  . PRO A 527  ? 0.6285 0.5846 0.7192 -0.0576 -0.0299 0.2094  525  PRO A CA  
3775  C C   . PRO A 527  ? 0.6186 0.5877 0.6966 -0.0573 -0.0225 0.2098  525  PRO A C   
3776  O O   . PRO A 527  ? 0.5692 0.5505 0.6480 -0.0602 -0.0206 0.2169  525  PRO A O   
3777  C CB  . PRO A 527  ? 0.6271 0.5799 0.7131 -0.0548 -0.0319 0.2093  525  PRO A CB  
3778  C CG  . PRO A 527  ? 0.6159 0.5529 0.7097 -0.0528 -0.0369 0.2018  525  PRO A CG  
3779  C CD  . PRO A 527  ? 0.6114 0.5437 0.7054 -0.0523 -0.0349 0.1941  525  PRO A CD  
3780  N N   . VAL A 528  ? 0.5645 0.5317 0.6314 -0.0537 -0.0185 0.2022  526  VAL A N   
3781  C CA  . VAL A 528  ? 0.5412 0.5196 0.5968 -0.0528 -0.0117 0.2009  526  VAL A CA  
3782  C C   . VAL A 528  ? 0.5697 0.5413 0.6263 -0.0521 -0.0102 0.1931  526  VAL A C   
3783  O O   . VAL A 528  ? 0.5505 0.5123 0.6041 -0.0491 -0.0106 0.1856  526  VAL A O   
3784  C CB  . VAL A 528  ? 0.5736 0.5571 0.6151 -0.0492 -0.0082 0.1989  526  VAL A CB  
3785  C CG1 . VAL A 528  ? 0.5427 0.5375 0.5732 -0.0479 -0.0013 0.1965  526  VAL A CG1 
3786  C CG2 . VAL A 528  ? 0.5591 0.5499 0.6001 -0.0501 -0.0100 0.2069  526  VAL A CG2 
3787  N N   . VAL A 529  ? 0.4893 0.4665 0.5506 -0.0549 -0.0086 0.1951  527  VAL A N   
3788  C CA  . VAL A 529  ? 0.5573 0.5289 0.6204 -0.0545 -0.0073 0.1883  527  VAL A CA  
3789  C C   . VAL A 529  ? 0.4990 0.4734 0.5487 -0.0508 -0.0018 0.1822  527  VAL A C   
3790  O O   . VAL A 529  ? 0.4820 0.4687 0.5222 -0.0499 0.0031  0.1843  527  VAL A O   
3791  C CB  . VAL A 529  ? 0.4673 0.4462 0.5374 -0.0583 -0.0063 0.1924  527  VAL A CB  
3792  C CG1 . VAL A 529  ? 0.4643 0.4396 0.5344 -0.0577 -0.0041 0.1856  527  VAL A CG1 
3793  C CG2 . VAL A 529  ? 0.5298 0.5038 0.6148 -0.0619 -0.0126 0.1975  527  VAL A CG2 
3794  N N   . GLY A 530  ? 0.4518 0.4151 0.5009 -0.0484 -0.0027 0.1744  528  GLY A N   
3795  C CA  . GLY A 530  ? 0.4917 0.4569 0.5296 -0.0451 0.0022  0.1685  528  GLY A CA  
3796  C C   . GLY A 530  ? 0.4467 0.4136 0.4738 -0.0417 0.0038  0.1674  528  GLY A C   
3797  O O   . GLY A 530  ? 0.4364 0.4083 0.4535 -0.0390 0.0084  0.1639  528  GLY A O   
3798  N N   . ALA A 531  ? 0.4827 0.4457 0.5117 -0.0415 -0.0001 0.1703  529  ALA A N   
3799  C CA  . ALA A 531  ? 0.4726 0.4364 0.4916 -0.0382 0.0009  0.1689  529  ALA A CA  
3800  C C   . ALA A 531  ? 0.4433 0.3983 0.4580 -0.0348 0.0015  0.1605  529  ALA A C   
3801  O O   . ALA A 531  ? 0.5048 0.4492 0.5265 -0.0346 -0.0016 0.1546  529  ALA A O   
3802  C CB  . ALA A 531  ? 0.4652 0.4249 0.4890 -0.0387 -0.0042 0.1732  529  ALA A CB  
3803  N N   . LYS A 532  ? 0.3922 0.3529 0.3947 -0.0311 0.0055  0.1554  530  LYS A N   
3804  C CA  . LYS A 532  ? 0.4645 0.4187 0.4613 -0.0268 0.0061  0.1435  530  LYS A CA  
3805  C C   . LYS A 532  ? 0.4580 0.4003 0.4601 -0.0259 0.0007  0.1410  530  LYS A C   
3806  O O   . LYS A 532  ? 0.4280 0.3684 0.4349 -0.0275 -0.0030 0.1484  530  LYS A O   
3807  C CB  . LYS A 532  ? 0.4747 0.4374 0.4588 -0.0235 0.0102  0.1405  530  LYS A CB  
3808  C CG  . LYS A 532  ? 0.5319 0.4885 0.5101 -0.0192 0.0105  0.1294  530  LYS A CG  
3809  C CD  . LYS A 532  ? 0.4654 0.4302 0.4322 -0.0161 0.0140  0.1266  530  LYS A CD  
3810  C CE  . LYS A 532  ? 0.5182 0.4864 0.4824 -0.0161 0.0121  0.1329  530  LYS A CE  
3811  N NZ  . LYS A 532  ? 0.4841 0.4414 0.4517 -0.0151 0.0075  0.1307  530  LYS A NZ  
3812  N N   . HIS A 533  ? 0.4432 0.3779 0.4446 -0.0232 0.0002  0.1306  531  HIS A N   
3813  C CA  . HIS A 533  ? 0.4643 0.3892 0.4696 -0.0215 -0.0043 0.1263  531  HIS A CA  
3814  C C   . HIS A 533  ? 0.4663 0.3934 0.4648 -0.0194 -0.0045 0.1281  531  HIS A C   
3815  O O   . HIS A 533  ? 0.4338 0.3676 0.4218 -0.0173 -0.0005 0.1256  531  HIS A O   
3816  C CB  . HIS A 533  ? 0.4405 0.3601 0.4441 -0.0188 -0.0036 0.1147  531  HIS A CB  
3817  C CG  . HIS A 533  ? 0.4979 0.4077 0.5079 -0.0175 -0.0085 0.1096  531  HIS A CG  
3818  N ND1 . HIS A 533  ? 0.5154 0.4226 0.5225 -0.0151 -0.0103 0.1078  531  HIS A ND1 
3819  C CD2 . HIS A 533  ? 0.5077 0.4104 0.5271 -0.0181 -0.0120 0.1053  531  HIS A CD2 
3820  C CE1 . HIS A 533  ? 0.5311 0.4301 0.5458 -0.0141 -0.0146 0.1027  531  HIS A CE1 
3821  N NE2 . HIS A 533  ? 0.5560 0.4523 0.5781 -0.0159 -0.0158 0.1009  531  HIS A NE2 
3822  N N   . ASP A 534  ? 0.4866 0.4078 0.4915 -0.0199 -0.0096 0.1321  532  ASP A N   
3823  C CA  . ASP A 534  ? 0.5105 0.4344 0.5100 -0.0183 -0.0104 0.1352  532  ASP A CA  
3824  C C   . ASP A 534  ? 0.5026 0.4248 0.4938 -0.0140 -0.0089 0.1252  532  ASP A C   
3825  O O   . ASP A 534  ? 0.4888 0.4160 0.4722 -0.0123 -0.0078 0.1263  532  ASP A O   
3826  C CB  . ASP A 534  ? 0.5298 0.4467 0.5394 -0.0195 -0.0167 0.1413  532  ASP A CB  
3827  C CG  . ASP A 534  ? 0.6486 0.5687 0.6658 -0.0241 -0.0185 0.1537  532  ASP A CG  
3828  O OD1 . ASP A 534  ? 0.6852 0.6157 0.6971 -0.0259 -0.0143 0.1591  532  ASP A OD1 
3829  O OD2 . ASP A 534  ? 0.7737 0.6865 0.8025 -0.0256 -0.0241 0.1573  532  ASP A OD2 
3830  N N   . ARG A 535  ? 0.4472 0.3631 0.4402 -0.0124 -0.0091 0.1156  533  ARG A N   
3831  C CA  . ARG A 535  ? 0.4576 0.3714 0.4446 -0.0088 -0.0084 0.1065  533  ARG A CA  
3832  C C   . ARG A 535  ? 0.4680 0.3866 0.4463 -0.0074 -0.0031 0.1002  533  ARG A C   
3833  O O   . ARG A 535  ? 0.4832 0.3998 0.4575 -0.0048 -0.0024 0.0922  533  ARG A O   
3834  C CB  . ARG A 535  ? 0.4784 0.3826 0.4733 -0.0077 -0.0125 0.1000  533  ARG A CB  
3835  N N   . ILE A 536  ? 0.4039 0.3292 0.3796 -0.0090 0.0004  0.1037  534  ILE A N   
3836  C CA  . ILE A 536  ? 0.4525 0.3829 0.4205 -0.0075 0.0051  0.0983  534  ILE A CA  
3837  C C   . ILE A 536  ? 0.4292 0.3697 0.3897 -0.0072 0.0081  0.1030  534  ILE A C   
3838  O O   . ILE A 536  ? 0.4784 0.4243 0.4408 -0.0096 0.0085  0.1111  534  ILE A O   
3839  C CB  . ILE A 536  ? 0.4099 0.3402 0.3815 -0.0091 0.0068  0.0968  534  ILE A CB  
3840  C CG1 . ILE A 536  ? 0.4667 0.3883 0.4459 -0.0093 0.0036  0.0919  534  ILE A CG1 
3841  C CG2 . ILE A 536  ? 0.4560 0.3917 0.4203 -0.0074 0.0114  0.0918  534  ILE A CG2 
3842  C CD1 . ILE A 536  ? 0.4528 0.3744 0.4356 -0.0107 0.0049  0.0898  534  ILE A CD1 
3843  N N   . ALA A 537  ? 0.3932 0.3367 0.3456 -0.0043 0.0102  0.0978  535  ALA A N   
3844  C CA  . ALA A 537  ? 0.4426 0.3965 0.3876 -0.0036 0.0129  0.1008  535  ALA A CA  
3845  C C   . ALA A 537  ? 0.4042 0.3651 0.3464 -0.0035 0.0172  0.0991  535  ALA A C   
3846  O O   . ALA A 537  ? 0.3883 0.3459 0.3305 -0.0024 0.0186  0.0923  535  ALA A O   
3847  C CB  . ALA A 537  ? 0.4307 0.3850 0.3690 -0.0004 0.0128  0.0955  535  ALA A CB  
3848  N N   . LEU A 538  ? 0.4084 0.3796 0.3485 -0.0047 0.0193  0.1054  536  LEU A N   
3849  C CA  . LEU A 538  ? 0.3604 0.3400 0.2967 -0.0037 0.0236  0.1026  536  LEU A CA  
3850  C C   . LEU A 538  ? 0.3549 0.3363 0.2839 0.0001  0.0251  0.0944  536  LEU A C   
3851  O O   . LEU A 538  ? 0.3804 0.3605 0.3059 0.0016  0.0234  0.0932  536  LEU A O   
3852  C CB  . LEU A 538  ? 0.4152 0.4075 0.3499 -0.0053 0.0256  0.1107  536  LEU A CB  
3853  C CG  . LEU A 538  ? 0.3926 0.3855 0.3349 -0.0095 0.0248  0.1193  536  LEU A CG  
3854  C CD1 . LEU A 538  ? 0.4542 0.4607 0.3944 -0.0112 0.0262  0.1285  536  LEU A CD1 
3855  C CD2 . LEU A 538  ? 0.3891 0.3814 0.3350 -0.0101 0.0270  0.1160  536  LEU A CD2 
3856  N N   . PRO A 539  ? 0.3496 0.3336 0.2767 0.0018  0.0280  0.0885  537  PRO A N   
3857  C CA  . PRO A 539  ? 0.3800 0.3650 0.3015 0.0053  0.0290  0.0805  537  PRO A CA  
3858  C C   . PRO A 539  ? 0.3519 0.3463 0.2671 0.0070  0.0294  0.0815  537  PRO A C   
3859  O O   . PRO A 539  ? 0.3871 0.3791 0.2988 0.0092  0.0283  0.0766  537  PRO A O   
3860  C CB  . PRO A 539  ? 0.3433 0.3316 0.2653 0.0064  0.0320  0.0760  537  PRO A CB  
3861  C CG  . PRO A 539  ? 0.3354 0.3183 0.2641 0.0035  0.0316  0.0793  537  PRO A CG  
3862  C CD  . PRO A 539  ? 0.3483 0.3326 0.2796 0.0005  0.0299  0.0883  537  PRO A CD  
3863  N N   . ALA A 540  ? 0.3900 0.3955 0.3036 0.0058  0.0310  0.0880  538  ALA A N   
3864  C CA  . ALA A 540  ? 0.3992 0.4154 0.3063 0.0074  0.0314  0.0894  538  ALA A CA  
3865  C C   . ALA A 540  ? 0.4450 0.4564 0.3515 0.0068  0.0278  0.0929  538  ALA A C   
3866  O O   . ALA A 540  ? 0.4159 0.4332 0.3167 0.0088  0.0274  0.0915  538  ALA A O   
3867  C CB  . ALA A 540  ? 0.4693 0.4997 0.3753 0.0058  0.0338  0.0967  538  ALA A CB  
3868  N N   . GLU A 541  ? 0.3994 0.4006 0.3121 0.0042  0.0250  0.0974  539  GLU A N   
3869  C CA  . GLU A 541  ? 0.4288 0.4255 0.3425 0.0035  0.0212  0.1017  539  GLU A CA  
3870  C C   . GLU A 541  ? 0.4216 0.4059 0.3370 0.0050  0.0187  0.0949  539  GLU A C   
3871  O O   . GLU A 541  ? 0.4453 0.4230 0.3641 0.0042  0.0151  0.0980  539  GLU A O   
3872  C CB  . GLU A 541  ? 0.4417 0.4365 0.3622 -0.0003 0.0191  0.1119  539  GLU A CB  
3873  C CG  . GLU A 541  ? 0.5337 0.5427 0.4522 -0.0021 0.0213  0.1204  539  GLU A CG  
3874  C CD  . GLU A 541  ? 0.6272 0.6343 0.5539 -0.0064 0.0199  0.1299  539  GLU A CD  
3875  O OE1 . GLU A 541  ? 0.6217 0.6163 0.5557 -0.0076 0.0173  0.1290  539  GLU A OE1 
3876  O OE2 . GLU A 541  ? 0.6516 0.6703 0.5777 -0.0085 0.0213  0.1383  539  GLU A OE2 
3877  N N   . LEU A 542  ? 0.4038 0.3853 0.3173 0.0072  0.0203  0.0859  540  LEU A N   
3878  C CA  . LEU A 542  ? 0.3919 0.3626 0.3074 0.0083  0.0183  0.0796  540  LEU A CA  
3879  C C   . LEU A 542  ? 0.4138 0.3836 0.3265 0.0097  0.0156  0.0792  540  LEU A C   
3880  O O   . LEU A 542  ? 0.4064 0.3675 0.3227 0.0096  0.0128  0.0776  540  LEU A O   
3881  C CB  . LEU A 542  ? 0.3705 0.3401 0.2840 0.0103  0.0205  0.0708  540  LEU A CB  
3882  C CG  . LEU A 542  ? 0.4230 0.3853 0.3415 0.0094  0.0210  0.0677  540  LEU A CG  
3883  C CD1 . LEU A 542  ? 0.3906 0.3505 0.3074 0.0116  0.0219  0.0592  540  LEU A CD1 
3884  C CD2 . LEU A 542  ? 0.4064 0.3597 0.3310 0.0075  0.0181  0.0699  540  LEU A CD2 
3885  N N   . PHE A 543  ? 0.3591 0.3386 0.2658 0.0110  0.0163  0.0803  541  PHE A N   
3886  C CA  . PHE A 543  ? 0.3946 0.3743 0.2982 0.0126  0.0137  0.0795  541  PHE A CA  
3887  C C   . PHE A 543  ? 0.4499 0.4338 0.3538 0.0111  0.0115  0.0891  541  PHE A C   
3888  O O   . PHE A 543  ? 0.4273 0.4134 0.3281 0.0124  0.0094  0.0896  541  PHE A O   
3889  C CB  . PHE A 543  ? 0.4170 0.4044 0.3136 0.0155  0.0155  0.0730  541  PHE A CB  
3890  C CG  . PHE A 543  ? 0.3694 0.3530 0.2666 0.0168  0.0175  0.0644  541  PHE A CG  
3891  C CD1 . PHE A 543  ? 0.4223 0.3950 0.3237 0.0166  0.0161  0.0602  541  PHE A CD1 
3892  C CD2 . PHE A 543  ? 0.4096 0.4010 0.3038 0.0182  0.0206  0.0607  541  PHE A CD2 
3893  C CE1 . PHE A 543  ? 0.4117 0.3810 0.3141 0.0175  0.0176  0.0533  541  PHE A CE1 
3894  C CE2 . PHE A 543  ? 0.3959 0.3830 0.2917 0.0194  0.0219  0.0533  541  PHE A CE2 
3895  C CZ  . PHE A 543  ? 0.3897 0.3658 0.2896 0.0189  0.0204  0.0501  541  PHE A CZ  
3896  N N   . GLY A 544  ? 0.4286 0.4136 0.3366 0.0083  0.0116  0.0971  542  GLY A N   
3897  C CA  . GLY A 544  ? 0.4591 0.4465 0.3693 0.0063  0.0088  0.1072  542  GLY A CA  
3898  C C   . GLY A 544  ? 0.4789 0.4801 0.3815 0.0073  0.0096  0.1108  542  GLY A C   
3899  O O   . GLY A 544  ? 0.4461 0.4583 0.3434 0.0081  0.0132  0.1093  542  GLY A O   
3900  N N   . ASP A 545  ? 0.4384 0.4399 0.3407 0.0075  0.0061  0.1153  543  ASP A N   
3901  C CA  . ASP A 545  ? 0.4926 0.5081 0.3878 0.0082  0.0064  0.1197  543  ASP A CA  
3902  C C   . ASP A 545  ? 0.4735 0.4950 0.3605 0.0119  0.0080  0.1101  543  ASP A C   
3903  O O   . ASP A 545  ? 0.5255 0.5608 0.4058 0.0129  0.0090  0.1121  543  ASP A O   
3904  C CB  . ASP A 545  ? 0.5116 0.5253 0.4097 0.0071  0.0016  0.1284  543  ASP A CB  
3905  C CG  . ASP A 545  ? 0.6701 0.6816 0.5762 0.0031  -0.0002 0.1399  543  ASP A CG  
3906  O OD1 . ASP A 545  ? 0.6380 0.6537 0.5453 0.0011  0.0028  0.1426  543  ASP A OD1 
3907  O OD2 . ASP A 545  ? 0.8209 0.8266 0.7327 0.0020  -0.0048 0.1464  543  ASP A OD2 
3908  N N   . ALA A 546  ? 0.4629 0.4751 0.3507 0.0139  0.0082  0.0998  544  ALA A N   
3909  C CA  . ALA A 546  ? 0.4805 0.4970 0.3618 0.0173  0.0088  0.0908  544  ALA A CA  
3910  C C   . ALA A 546  ? 0.4878 0.5166 0.3635 0.0187  0.0129  0.0868  544  ALA A C   
3911  O O   . ALA A 546  ? 0.4450 0.4852 0.3142 0.0208  0.0133  0.0843  544  ALA A O   
3912  C CB  . ALA A 546  ? 0.4650 0.4688 0.3496 0.0186  0.0080  0.0816  544  ALA A CB  
3913  N N   . ARG A 547  ? 0.4134 0.4406 0.2918 0.0177  0.0158  0.0855  545  ARG A N   
3914  C CA  . ARG A 547  ? 0.4425 0.4810 0.3167 0.0194  0.0195  0.0810  545  ARG A CA  
3915  C C   . ARG A 547  ? 0.3875 0.4228 0.2665 0.0174  0.0220  0.0824  545  ARG A C   
3916  O O   . ARG A 547  ? 0.3624 0.3853 0.2476 0.0154  0.0208  0.0843  545  ARG A O   
3917  C CB  . ARG A 547  ? 0.4531 0.4906 0.3245 0.0229  0.0200  0.0688  545  ARG A CB  
3918  C CG  . ARG A 547  ? 0.4493 0.4721 0.3260 0.0228  0.0195  0.0630  545  ARG A CG  
3919  C CD  . ARG A 547  ? 0.4650 0.4865 0.3400 0.0259  0.0195  0.0519  545  ARG A CD  
3920  N NE  . ARG A 547  ? 0.4551 0.4623 0.3353 0.0253  0.0178  0.0483  545  ARG A NE  
3921  C CZ  . ARG A 547  ? 0.4170 0.4174 0.3009 0.0254  0.0191  0.0432  545  ARG A CZ  
3922  N NH1 . ARG A 547  ? 0.4633 0.4690 0.3469 0.0263  0.0218  0.0400  545  ARG A NH1 
3923  N NH2 . ARG A 547  ? 0.4344 0.4231 0.3227 0.0245  0.0174  0.0412  545  ARG A NH2 
3924  N N   . THR A 548  ? 0.3824 0.4295 0.2585 0.0183  0.0255  0.0810  546  THR A N   
3925  C CA  . THR A 548  ? 0.3815 0.4276 0.2617 0.0168  0.0281  0.0822  546  THR A CA  
3926  C C   . THR A 548  ? 0.3712 0.4097 0.2534 0.0189  0.0292  0.0717  546  THR A C   
3927  O O   . THR A 548  ? 0.3487 0.3921 0.2273 0.0222  0.0300  0.0633  546  THR A O   
3928  C CB  . THR A 548  ? 0.4153 0.4789 0.2920 0.0166  0.0313  0.0861  546  THR A CB  
3929  O OG1 . THR A 548  ? 0.4319 0.5031 0.3070 0.0143  0.0300  0.0969  546  THR A OG1 
3930  C CG2 . THR A 548  ? 0.3825 0.4450 0.2643 0.0148  0.0339  0.0878  546  THR A CG2 
3931  N N   . ASN A 549  ? 0.3595 0.3860 0.2479 0.0171  0.0289  0.0720  547  ASN A N   
3932  C CA  . ASN A 549  ? 0.3616 0.3814 0.2524 0.0187  0.0299  0.0633  547  ASN A CA  
3933  C C   . ASN A 549  ? 0.3137 0.3444 0.2030 0.0205  0.0333  0.0598  547  ASN A C   
3934  O O   . ASN A 549  ? 0.3692 0.4104 0.2576 0.0193  0.0353  0.0655  547  ASN A O   
3935  C CB  . ASN A 549  ? 0.3308 0.3378 0.2283 0.0162  0.0291  0.0653  547  ASN A CB  
3936  C CG  . ASN A 549  ? 0.3669 0.3659 0.2671 0.0176  0.0293  0.0571  547  ASN A CG  
3937  O OD1 . ASN A 549  ? 0.3744 0.3748 0.2721 0.0204  0.0295  0.0497  547  ASN A OD1 
3938  N ND2 . ASN A 549  ? 0.3320 0.3222 0.2376 0.0156  0.0291  0.0583  547  ASN A ND2 
3939  N N   . SER A 550  ? 0.3475 0.3764 0.2370 0.0234  0.0338  0.0503  548  SER A N   
3940  C CA  . SER A 550  ? 0.3484 0.3862 0.2380 0.0253  0.0368  0.0460  548  SER A CA  
3941  C C   . SER A 550  ? 0.3418 0.3749 0.2371 0.0231  0.0382  0.0492  548  SER A C   
3942  O O   . SER A 550  ? 0.3547 0.3755 0.2541 0.0209  0.0367  0.0513  548  SER A O   
3943  C CB  . SER A 550  ? 0.3605 0.3964 0.2502 0.0290  0.0363  0.0349  548  SER A CB  
3944  O OG  . SER A 550  ? 0.3455 0.3667 0.2401 0.0283  0.0346  0.0321  548  SER A OG  
3945  N N   . ALA A 551  ? 0.3595 0.4035 0.2548 0.0238  0.0411  0.0496  549  ALA A N   
3946  C CA  . ALA A 551  ? 0.3799 0.4215 0.2806 0.0219  0.0427  0.0524  549  ALA A CA  
3947  C C   . ALA A 551  ? 0.3510 0.3901 0.2549 0.0247  0.0435  0.0437  549  ALA A C   
3948  O O   . ALA A 551  ? 0.3796 0.4263 0.2814 0.0283  0.0443  0.0366  549  ALA A O   
3949  C CB  . ALA A 551  ? 0.4028 0.4585 0.3026 0.0204  0.0454  0.0592  549  ALA A CB  
3950  N N   . GLY A 552  ? 0.3592 0.3881 0.2686 0.0231  0.0431  0.0443  550  GLY A N   
3951  C CA  . GLY A 552  ? 0.3389 0.3654 0.2524 0.0252  0.0437  0.0376  550  GLY A CA  
3952  C C   . GLY A 552  ? 0.3590 0.3938 0.2753 0.0251  0.0465  0.0395  550  GLY A C   
3953  O O   . GLY A 552  ? 0.3848 0.4308 0.2990 0.0240  0.0484  0.0447  550  GLY A O   
3954  N N   . LEU A 553  ? 0.3609 0.3905 0.2824 0.0259  0.0465  0.0357  551  LEU A N   
3955  C CA  . LEU A 553  ? 0.3480 0.3842 0.2733 0.0259  0.0488  0.0369  551  LEU A CA  
3956  C C   . LEU A 553  ? 0.3333 0.3580 0.2644 0.0241  0.0477  0.0379  551  LEU A C   
3957  O O   . LEU A 553  ? 0.3648 0.3793 0.2977 0.0248  0.0455  0.0339  551  LEU A O   
3958  C CB  . LEU A 553  ? 0.3601 0.4058 0.2861 0.0305  0.0502  0.0289  551  LEU A CB  
3959  C CG  . LEU A 553  ? 0.3417 0.4023 0.2624 0.0331  0.0518  0.0264  551  LEU A CG  
3960  C CD1 . LEU A 553  ? 0.3831 0.4508 0.3063 0.0380  0.0525  0.0167  551  LEU A CD1 
3961  C CD2 . LEU A 553  ? 0.3695 0.4424 0.2876 0.0306  0.0544  0.0346  551  LEU A CD2 
3962  N N   . ASP A 554  ? 0.3542 0.3815 0.2885 0.0216  0.0491  0.0432  552  ASP A N   
3963  C CA  . ASP A 554  ? 0.3674 0.3850 0.3071 0.0196  0.0479  0.0447  552  ASP A CA  
3964  C C   . ASP A 554  ? 0.3513 0.3715 0.2955 0.0223  0.0488  0.0396  552  ASP A C   
3965  O O   . ASP A 554  ? 0.3268 0.3568 0.2728 0.0227  0.0511  0.0408  552  ASP A O   
3966  C CB  . ASP A 554  ? 0.3564 0.3747 0.2978 0.0154  0.0484  0.0529  552  ASP A CB  
3967  C CG  . ASP A 554  ? 0.3887 0.3973 0.3353 0.0131  0.0469  0.0543  552  ASP A CG  
3968  O OD1 . ASP A 554  ? 0.4022 0.4041 0.3508 0.0147  0.0456  0.0495  552  ASP A OD1 
3969  O OD2 . ASP A 554  ? 0.4071 0.4151 0.3559 0.0097  0.0467  0.0604  552  ASP A OD2 
3970  N N   . LEU A 555  ? 0.3379 0.3498 0.2846 0.0241  0.0468  0.0343  553  LEU A N   
3971  C CA  . LEU A 555  ? 0.3329 0.3465 0.2849 0.0268  0.0471  0.0296  553  LEU A CA  
3972  C C   . LEU A 555  ? 0.3581 0.3679 0.3153 0.0245  0.0469  0.0333  553  LEU A C   
3973  O O   . LEU A 555  ? 0.3319 0.3413 0.2942 0.0265  0.0466  0.0300  553  LEU A O   
3974  C CB  . LEU A 555  ? 0.3387 0.3454 0.2923 0.0297  0.0447  0.0228  553  LEU A CB  
3975  C CG  . LEU A 555  ? 0.3755 0.3869 0.3246 0.0324  0.0447  0.0179  553  LEU A CG  
3976  C CD1 . LEU A 555  ? 0.3912 0.3958 0.3433 0.0352  0.0420  0.0109  553  LEU A CD1 
3977  C CD2 . LEU A 555  ? 0.3967 0.4230 0.3446 0.0351  0.0475  0.0157  553  LEU A CD2 
3978  N N   . SER A 556  ? 0.3694 0.3762 0.3259 0.0205  0.0469  0.0398  554  SER A N   
3979  C CA  . SER A 556  ? 0.3642 0.3698 0.3255 0.0181  0.0469  0.0436  554  SER A CA  
3980  C C   . SER A 556  ? 0.3683 0.3843 0.3303 0.0166  0.0495  0.0482  554  SER A C   
3981  O O   . SER A 556  ? 0.3637 0.3799 0.3300 0.0145  0.0497  0.0515  554  SER A O   
3982  C CB  . SER A 556  ? 0.3784 0.3738 0.3396 0.0145  0.0447  0.0471  554  SER A CB  
3983  O OG  . SER A 556  ? 0.4135 0.4101 0.3718 0.0118  0.0450  0.0521  554  SER A OG  
3984  N N   . ASN A 557  ? 0.3632 0.3887 0.3214 0.0176  0.0514  0.0486  555  ASN A N   
3985  C CA  . ASN A 557  ? 0.3272 0.3640 0.2857 0.0158  0.0540  0.0538  555  ASN A CA  
3986  C C   . ASN A 557  ? 0.3441 0.3927 0.3048 0.0194  0.0564  0.0496  555  ASN A C   
3987  O O   . ASN A 557  ? 0.3351 0.3892 0.2931 0.0232  0.0571  0.0439  555  ASN A O   
3988  C CB  . ASN A 557  ? 0.3372 0.3784 0.2900 0.0146  0.0545  0.0576  555  ASN A CB  
3989  C CG  . ASN A 557  ? 0.3582 0.4122 0.3115 0.0123  0.0570  0.0642  555  ASN A CG  
3990  O OD1 . ASN A 557  ? 0.3610 0.4265 0.3160 0.0140  0.0596  0.0628  555  ASN A OD1 
3991  N ND2 . ASN A 557  ? 0.4016 0.4536 0.3539 0.0083  0.0561  0.0716  555  ASN A ND2 
3992  N N   . GLU A 558  ? 0.3799 0.4332 0.3458 0.0182  0.0577  0.0521  556  GLU A N   
3993  C CA  . GLU A 558  ? 0.3364 0.4006 0.3054 0.0219  0.0597  0.0474  556  GLU A CA  
3994  C C   . GLU A 558  ? 0.3253 0.4049 0.2902 0.0238  0.0626  0.0467  556  GLU A C   
3995  O O   . GLU A 558  ? 0.3657 0.4529 0.3310 0.0284  0.0636  0.0396  556  GLU A O   
3996  C CB  . GLU A 558  ? 0.3657 0.4330 0.3412 0.0200  0.0606  0.0509  556  GLU A CB  
3997  C CG  . GLU A 558  ? 0.3797 0.4346 0.3599 0.0193  0.0579  0.0500  556  GLU A CG  
3998  C CD  . GLU A 558  ? 0.3757 0.4261 0.3583 0.0239  0.0563  0.0421  556  GLU A CD  
3999  O OE1 . GLU A 558  ? 0.3468 0.4046 0.3290 0.0282  0.0575  0.0363  556  GLU A OE1 
4000  O OE2 . GLU A 558  ? 0.3567 0.3962 0.3421 0.0232  0.0538  0.0419  556  GLU A OE2 
4001  N N   . GLU A 559  ? 0.3196 0.4047 0.2810 0.0202  0.0638  0.0540  557  GLU A N   
4002  C CA  . GLU A 559  ? 0.3766 0.4779 0.3336 0.0218  0.0665  0.0539  557  GLU A CA  
4003  C C   . GLU A 559  ? 0.3483 0.4483 0.2998 0.0256  0.0656  0.0470  557  GLU A C   
4004  O O   . GLU A 559  ? 0.3282 0.4410 0.2776 0.0295  0.0674  0.0416  557  GLU A O   
4005  C CB  . GLU A 559  ? 0.3466 0.4534 0.3012 0.0169  0.0675  0.0642  557  GLU A CB  
4006  C CG  . GLU A 559  ? 0.3667 0.4723 0.3270 0.0121  0.0676  0.0721  557  GLU A CG  
4007  C CD  . GLU A 559  ? 0.5042 0.6146 0.4629 0.0072  0.0679  0.0825  557  GLU A CD  
4008  O OE1 . GLU A 559  ? 0.5366 0.6502 0.4893 0.0075  0.0679  0.0838  557  GLU A OE1 
4009  O OE2 . GLU A 559  ? 0.4820 0.5932 0.4460 0.0030  0.0680  0.0896  557  GLU A OE2 
4010  N N   . THR A 560  ? 0.3291 0.4144 0.2784 0.0245  0.0626  0.0469  558  THR A N   
4011  C CA  . THR A 560  ? 0.3827 0.4658 0.3276 0.0280  0.0613  0.0402  558  THR A CA  
4012  C C   . THR A 560  ? 0.3374 0.4196 0.2862 0.0330  0.0607  0.0302  558  THR A C   
4013  O O   . THR A 560  ? 0.3240 0.4141 0.2706 0.0372  0.0612  0.0232  558  THR A O   
4014  C CB  . THR A 560  ? 0.3665 0.4340 0.3091 0.0256  0.0583  0.0424  558  THR A CB  
4015  O OG1 . THR A 560  ? 0.3800 0.4487 0.3200 0.0212  0.0585  0.0515  558  THR A OG1 
4016  C CG2 . THR A 560  ? 0.3293 0.3945 0.2676 0.0289  0.0568  0.0356  558  THR A CG2 
4017  N N   . LEU A 561  ? 0.3229 0.3959 0.2779 0.0328  0.0594  0.0293  559  LEU A N   
4018  C CA  . LEU A 561  ? 0.2891 0.3608 0.2491 0.0375  0.0584  0.0205  559  LEU A CA  
4019  C C   . LEU A 561  ? 0.3686 0.4573 0.3305 0.0413  0.0612  0.0159  559  LEU A C   
4020  O O   . LEU A 561  ? 0.3471 0.4391 0.3108 0.0462  0.0605  0.0068  559  LEU A O   
4021  C CB  . LEU A 561  ? 0.3134 0.3735 0.2799 0.0361  0.0565  0.0218  559  LEU A CB  
4022  C CG  . LEU A 561  ? 0.2994 0.3438 0.2641 0.0330  0.0536  0.0247  559  LEU A CG  
4023  C CD1 . LEU A 561  ? 0.3517 0.3866 0.3222 0.0311  0.0519  0.0271  559  LEU A CD1 
4024  C CD2 . LEU A 561  ? 0.3180 0.3565 0.2811 0.0360  0.0513  0.0180  559  LEU A CD2 
4025  N N   . ALA A 562  ? 0.3353 0.4353 0.2975 0.0390  0.0641  0.0218  560  ALA A N   
4026  C CA  . ALA A 562  ? 0.3497 0.4673 0.3140 0.0426  0.0670  0.0175  560  ALA A CA  
4027  C C   . ALA A 562  ? 0.3641 0.4950 0.3220 0.0453  0.0686  0.0136  560  ALA A C   
4028  O O   . ALA A 562  ? 0.3335 0.4745 0.2931 0.0506  0.0693  0.0046  560  ALA A O   
4029  C CB  . ALA A 562  ? 0.3717 0.4986 0.3381 0.0390  0.0698  0.0256  560  ALA A CB  
4030  N N   . SER A 563  ? 0.3673 0.4985 0.3182 0.0419  0.0688  0.0199  561  SER A N   
4031  C CA  A SER A 563  ? 0.3528 0.4966 0.2969 0.0442  0.0700  0.0169  561  SER A CA  
4032  C CA  B SER A 563  ? 0.3528 0.4969 0.2970 0.0443  0.0701  0.0168  561  SER A CA  
4033  C C   . SER A 563  ? 0.3947 0.5311 0.3380 0.0485  0.0672  0.0068  561  SER A C   
4034  O O   . SER A 563  ? 0.3855 0.5341 0.3268 0.0531  0.0680  -0.0011 561  SER A O   
4035  C CB  A SER A 563  ? 0.3592 0.5033 0.2969 0.0391  0.0704  0.0273  561  SER A CB  
4036  C CB  B SER A 563  ? 0.3592 0.5050 0.2968 0.0393  0.0707  0.0270  561  SER A CB  
4037  O OG  A SER A 563  ? 0.3845 0.5397 0.3152 0.0411  0.0711  0.0248  561  SER A OG  
4038  O OG  B SER A 563  ? 0.3496 0.4764 0.2866 0.0363  0.0676  0.0306  561  SER A OG  
4039  N N   . LEU A 564  ? 0.3435 0.4606 0.2884 0.0471  0.0639  0.0070  562  LEU A N   
4040  C CA  . LEU A 564  ? 0.3724 0.4815 0.3175 0.0508  0.0609  -0.0020 562  LEU A CA  
4041  C C   . LEU A 564  ? 0.3991 0.5113 0.3516 0.0563  0.0602  -0.0124 562  LEU A C   
4042  O O   . LEU A 564  ? 0.3817 0.4983 0.3341 0.0609  0.0591  -0.0219 562  LEU A O   
4043  C CB  . LEU A 564  ? 0.3718 0.4604 0.3177 0.0476  0.0576  0.0014  562  LEU A CB  
4044  C CG  . LEU A 564  ? 0.4445 0.5236 0.3890 0.0495  0.0544  -0.0046 562  LEU A CG  
4045  C CD1 . LEU A 564  ? 0.3810 0.4699 0.3175 0.0501  0.0552  -0.0052 562  LEU A CD1 
4046  C CD2 . LEU A 564  ? 0.4559 0.5172 0.4009 0.0454  0.0518  0.0008  562  LEU A CD2 
4047  N N   . THR A 565  ? 0.3148 0.4252 0.2741 0.0560  0.0607  -0.0110 563  THR A N   
4048  C CA  . THR A 565  ? 0.3839 0.4979 0.3512 0.0614  0.0600  -0.0205 563  THR A CA  
4049  C C   . THR A 565  ? 0.3875 0.5216 0.3530 0.0662  0.0623  -0.0282 563  THR A C   
4050  O O   . THR A 565  ? 0.3962 0.5319 0.3655 0.0716  0.0604  -0.0392 563  THR A O   
4051  C CB  . THR A 565  ? 0.3637 0.4765 0.3377 0.0600  0.0608  -0.0165 563  THR A CB  
4052  O OG1 . THR A 565  ? 0.4049 0.4992 0.3811 0.0563  0.0581  -0.0111 563  THR A OG1 
4053  C CG2 . THR A 565  ? 0.4018 0.5204 0.3845 0.0660  0.0601  -0.0263 563  THR A CG2 
4054  N N   . GLU A 566  ? 0.3790 0.5292 0.3391 0.0644  0.0662  -0.0227 564  GLU A N   
4055  C CA  . GLU A 566  ? 0.4013 0.5730 0.3591 0.0688  0.0688  -0.0296 564  GLU A CA  
4056  C C   . GLU A 566  ? 0.4402 0.6140 0.3920 0.0712  0.0673  -0.0357 564  GLU A C   
4057  O O   . GLU A 566  ? 0.4615 0.6451 0.4151 0.0771  0.0668  -0.0472 564  GLU A O   
4058  C CB  . GLU A 566  ? 0.4460 0.6350 0.3993 0.0655  0.0733  -0.0207 564  GLU A CB  
4059  C CG  . GLU A 566  ? 0.5129 0.7018 0.4726 0.0633  0.0748  -0.0152 564  GLU A CG  
4060  C CD  . GLU A 566  ? 0.6036 0.7967 0.5725 0.0691  0.0744  -0.0254 564  GLU A CD  
4061  O OE1 . GLU A 566  ? 0.6294 0.8386 0.5984 0.0745  0.0756  -0.0348 564  GLU A OE1 
4062  O OE2 . GLU A 566  ? 0.5515 0.7321 0.5278 0.0684  0.0726  -0.0244 564  GLU A OE2 
4063  N N   . ALA A 567  ? 0.4044 0.5694 0.3494 0.0670  0.0663  -0.0286 565  ALA A N   
4064  C CA  . ALA A 567  ? 0.4245 0.5919 0.3635 0.0690  0.0649  -0.0339 565  ALA A CA  
4065  C C   . ALA A 567  ? 0.4300 0.5857 0.3750 0.0735  0.0607  -0.0454 565  ALA A C   
4066  O O   . ALA A 567  ? 0.4240 0.5884 0.3681 0.0782  0.0598  -0.0556 565  ALA A O   
4067  C CB  . ALA A 567  ? 0.4183 0.5770 0.3499 0.0635  0.0643  -0.0237 565  ALA A CB  
4068  N N   . LEU A 568  ? 0.3388 0.4753 0.2903 0.0719  0.0580  -0.0440 566  LEU A N   
4069  C CA  . LEU A 568  ? 0.3935 0.5180 0.3517 0.0755  0.0536  -0.0535 566  LEU A CA  
4070  C C   . LEU A 568  ? 0.4038 0.5388 0.3697 0.0821  0.0533  -0.0655 566  LEU A C   
4071  O O   . LEU A 568  ? 0.4235 0.5590 0.3920 0.0867  0.0506  -0.0764 566  LEU A O   
4072  C CB  . LEU A 568  ? 0.3343 0.4379 0.2981 0.0721  0.0510  -0.0482 566  LEU A CB  
4073  C CG  . LEU A 568  ? 0.3502 0.4421 0.3077 0.0660  0.0506  -0.0377 566  LEU A CG  
4074  C CD1 . LEU A 568  ? 0.3598 0.4344 0.3232 0.0629  0.0486  -0.0325 566  LEU A CD1 
4075  C CD2 . LEU A 568  ? 0.4121 0.4999 0.3645 0.0664  0.0484  -0.0409 566  LEU A CD2 
4076  N N   . ARG A 569  ? 0.3760 0.5196 0.3460 0.0829  0.0559  -0.0642 567  ARG A N   
4077  C CA  . ARG A 569  ? 0.4357 0.5917 0.4129 0.0894  0.0559  -0.0757 567  ARG A CA  
4078  C C   . ARG A 569  ? 0.4509 0.6269 0.4223 0.0935  0.0577  -0.0837 567  ARG A C   
4079  O O   . ARG A 569  ? 0.4426 0.6234 0.4194 0.0997  0.0554  -0.0969 567  ARG A O   
4080  C CB  . ARG A 569  ? 0.4155 0.5799 0.3968 0.0890  0.0591  -0.0716 567  ARG A CB  
4081  C CG  . ARG A 569  ? 0.4950 0.6420 0.4845 0.0867  0.0569  -0.0668 567  ARG A CG  
4082  C CD  . ARG A 569  ? 0.5269 0.6838 0.5187 0.0855  0.0604  -0.0613 567  ARG A CD  
4083  N NE  . ARG A 569  ? 0.5698 0.7114 0.5682 0.0826  0.0587  -0.0553 567  ARG A NE  
4084  C CZ  . ARG A 569  ? 0.6288 0.7723 0.6366 0.0852  0.0583  -0.0581 567  ARG A CZ  
4085  N NH1 . ARG A 569  ? 0.5547 0.7142 0.5672 0.0911  0.0596  -0.0674 567  ARG A NH1 
4086  N NH2 . ARG A 569  ? 0.6371 0.7669 0.6498 0.0821  0.0567  -0.0516 567  ARG A NH2 
4087  N N   . GLU A 570  ? 0.4499 0.6384 0.4108 0.0902  0.0614  -0.0761 568  GLU A N   
4088  C CA  . GLU A 570  ? 0.4454 0.6549 0.3999 0.0937  0.0632  -0.0828 568  GLU A CA  
4089  C C   . GLU A 570  ? 0.5128 0.7154 0.4648 0.0957  0.0595  -0.0901 568  GLU A C   
4090  O O   . GLU A 570  ? 0.4249 0.6418 0.3762 0.1011  0.0591  -0.1015 568  GLU A O   
4091  C CB  . GLU A 570  ? 0.4679 0.6919 0.4121 0.0891  0.0679  -0.0711 568  GLU A CB  
4092  C CG  . GLU A 570  ? 0.5704 0.8087 0.5172 0.0885  0.0720  -0.0668 568  GLU A CG  
4093  C CD  . GLU A 570  ? 0.5937 0.8399 0.5325 0.0821  0.0758  -0.0519 568  GLU A CD  
4094  O OE1 . GLU A 570  ? 0.6701 0.9041 0.6034 0.0772  0.0746  -0.0432 568  GLU A OE1 
4095  O OE2 . GLU A 570  ? 0.6838 0.9485 0.6226 0.0819  0.0798  -0.0490 568  GLU A OE2 
4096  N N   . SER A 571  ? 0.4376 0.6192 0.3887 0.0916  0.0566  -0.0842 569  SER A N   
4097  C CA  . SER A 571  ? 0.4715 0.6455 0.4213 0.0933  0.0527  -0.0910 569  SER A CA  
4098  C C   . SER A 571  ? 0.4546 0.6234 0.4155 0.0993  0.0486  -0.1053 569  SER A C   
4099  O O   . SER A 571  ? 0.4438 0.6165 0.4044 0.1032  0.0462  -0.1155 569  SER A O   
4100  C CB  . SER A 571  ? 0.4450 0.5980 0.3921 0.0874  0.0506  -0.0813 569  SER A CB  
4101  O OG  . SER A 571  ? 0.4145 0.5482 0.3713 0.0869  0.0474  -0.0818 569  SER A OG  
4102  N N   . ALA A 572  ? 0.4518 0.6119 0.4231 0.1003  0.0474  -0.1063 570  ALA A N   
4103  C CA  . ALA A 572  ? 0.4452 0.5993 0.4286 0.1060  0.0430  -0.1192 570  ALA A CA  
4104  C C   . ALA A 572  ? 0.4678 0.6428 0.4546 0.1131  0.0441  -0.1322 570  ALA A C   
4105  O O   . ALA A 572  ? 0.4803 0.6522 0.4778 0.1186  0.0400  -0.1446 570  ALA A O   
4106  C CB  . ALA A 572  ? 0.4783 0.6154 0.4720 0.1044  0.0409  -0.1151 570  ALA A CB  
4107  N N   . ALA A 573  ? 0.4745 0.6711 0.4533 0.1132  0.0492  -0.1296 571  ALA A N   
4108  C CA  . ALA A 573  ? 0.4915 0.7116 0.4719 0.1198  0.0509  -0.1417 571  ALA A CA  
4109  C C   . ALA A 573  ? 0.5313 0.7659 0.5030 0.1222  0.0511  -0.1485 571  ALA A C   
4110  O O   . ALA A 573  ? 0.5783 0.8332 0.5501 0.1267  0.0520  -0.1575 571  ALA A O   
4111  C CB  . ALA A 573  ? 0.4618 0.6992 0.4390 0.1186  0.0566  -0.1349 571  ALA A CB  
4112  N N   . MET A 574  ? 0.4970 0.7208 0.4617 0.1183  0.0495  -0.1431 572  MET A N   
4113  C CA  . MET A 574  ? 0.5443 0.7815 0.5003 0.1200  0.0494  -0.1485 572  MET A CA  
4114  C C   . MET A 574  ? 0.5219 0.7507 0.4858 0.1250  0.0436  -0.1631 572  MET A C   
4115  O O   . MET A 574  ? 0.4730 0.6791 0.4456 0.1239  0.0392  -0.1633 572  MET A O   
4116  C CB  . MET A 574  ? 0.5248 0.7559 0.4690 0.1131  0.0508  -0.1345 572  MET A CB  
4117  C CG  . MET A 574  ? 0.5380 0.7765 0.4752 0.1077  0.0561  -0.1194 572  MET A CG  
4118  S SD  . MET A 574  ? 0.6120 0.8396 0.5379 0.0998  0.0564  -0.1037 572  MET A SD  
4119  C CE  . MET A 574  ? 0.6267 0.8636 0.5477 0.0942  0.0621  -0.0876 572  MET A CE  
4120  N N   . LYS A 575  ? 0.4628 0.7055 0.4255 0.1272  0.0415  -0.1711 573  LYS A N   
4121  C CA  . LYS A 575  ? 0.4824 0.7175 0.4531 0.1306  0.0350  -0.1837 573  LYS A CA  
4122  C C   . LYS A 575  ? 0.4650 0.6938 0.4273 0.1279  0.0336  -0.1809 573  LYS A C   
4123  O O   . LYS A 575  ? 0.4702 0.7117 0.4261 0.1280  0.0328  -0.1833 573  LYS A O   
4124  C CB  . LYS A 575  ? 0.5237 0.7774 0.4982 0.1346  0.0331  -0.1942 573  LYS A CB  
4125  C CG  . LYS A 575  ? 0.5884 0.8473 0.5729 0.1378  0.0335  -0.1989 573  LYS A CG  
4126  C CD  . LYS A 575  ? 0.5875 0.8244 0.5861 0.1397  0.0295  -0.2033 573  LYS A CD  
4127  C CE  . LYS A 575  ? 0.6347 0.8775 0.6454 0.1440  0.0280  -0.2113 573  LYS A CE  
4128  N NZ  . LYS A 575  ? 0.7104 0.9315 0.7351 0.1454  0.0240  -0.2139 573  LYS A NZ  
4129  N N   . TRP A 576  ? 0.4285 0.6375 0.3909 0.1256  0.0331  -0.1756 574  TRP A N   
4130  C CA  . TRP A 576  ? 0.4035 0.6037 0.3590 0.1227  0.0313  -0.1724 574  TRP A CA  
4131  C C   . TRP A 576  ? 0.4047 0.6020 0.3669 0.1258  0.0251  -0.1851 574  TRP A C   
4132  O O   . TRP A 576  ? 0.4093 0.5985 0.3850 0.1290  0.0206  -0.1945 574  TRP A O   
4133  C CB  . TRP A 576  ? 0.4194 0.5934 0.3780 0.1165  0.0297  -0.1603 574  TRP A CB  
4134  C CG  . TRP A 576  ? 0.4012 0.5733 0.3547 0.1111  0.0343  -0.1449 574  TRP A CG  
4135  C CD1 . TRP A 576  ? 0.4050 0.5693 0.3660 0.1101  0.0352  -0.1407 574  TRP A CD1 
4136  C CD2 . TRP A 576  ? 0.3579 0.5354 0.2986 0.1057  0.0383  -0.1315 574  TRP A CD2 
4137  N NE1 . TRP A 576  ? 0.3886 0.5533 0.3422 0.1046  0.0395  -0.1261 574  TRP A NE1 
4138  C CE2 . TRP A 576  ? 0.3632 0.5358 0.3047 0.1018  0.0414  -0.1201 574  TRP A CE2 
4139  C CE3 . TRP A 576  ? 0.3681 0.5544 0.2973 0.1040  0.0393  -0.1280 574  TRP A CE3 
4140  C CZ2 . TRP A 576  ? 0.3947 0.5702 0.3266 0.0962  0.0452  -0.1058 574  TRP A CZ2 
4141  C CZ3 . TRP A 576  ? 0.4290 0.6181 0.3485 0.0984  0.0430  -0.1132 574  TRP A CZ3 
4142  C CH2 . TRP A 576  ? 0.4672 0.6508 0.3885 0.0945  0.0459  -0.1024 574  TRP A CH2 
4143  N N   . THR A 577  ? 0.3726 0.5768 0.3259 0.1245  0.0244  -0.1847 575  THR A N   
4144  C CA  . THR A 577  ? 0.3688 0.5688 0.3279 0.1265  0.0182  -0.1952 575  THR A CA  
4145  C C   . THR A 577  ? 0.3921 0.5853 0.3423 0.1232  0.0175  -0.1902 575  THR A C   
4146  O O   . THR A 577  ? 0.3985 0.5939 0.3367 0.1196  0.0218  -0.1789 575  THR A O   
4147  C CB  . THR A 577  ? 0.4440 0.6650 0.4039 0.1298  0.0168  -0.2041 575  THR A CB  
4148  O OG1 . THR A 577  ? 0.4028 0.6418 0.3485 0.1276  0.0208  -0.1967 575  THR A OG1 
4149  C CG2 . THR A 577  ? 0.4427 0.6719 0.4115 0.1333  0.0172  -0.2099 575  THR A CG2 
4150  N N   . ALA A 578  ? 0.3795 0.5640 0.3366 0.1244  0.0117  -0.1987 576  ALA A N   
4151  C CA  . ALA A 578  ? 0.3626 0.5417 0.3129 0.1219  0.0099  -0.1963 576  ALA A CA  
4152  C C   . ALA A 578  ? 0.4215 0.6072 0.3777 0.1248  0.0045  -0.2081 576  ALA A C   
4153  O O   . ALA A 578  ? 0.4042 0.5829 0.3743 0.1275  -0.0002 -0.2179 576  ALA A O   
4154  C CB  . ALA A 578  ? 0.3565 0.5112 0.3110 0.1196  0.0078  -0.1931 576  ALA A CB  
4155  N N   . LEU A 579  ? 0.4601 0.6592 0.4063 0.1240  0.0050  -0.2070 577  LEU A N   
4156  C CA  . LEU A 579  ? 0.4436 0.6529 0.3939 0.1269  0.0005  -0.2177 577  LEU A CA  
4157  C C   . LEU A 579  ? 0.4159 0.6213 0.3596 0.1245  -0.0015 -0.2155 577  LEU A C   
4158  O O   . LEU A 579  ? 0.4594 0.6612 0.3922 0.1208  0.0018  -0.2045 577  LEU A O   
4159  C CB  . LEU A 579  ? 0.4430 0.6787 0.3879 0.1292  0.0031  -0.2195 577  LEU A CB  
4160  C CG  . LEU A 579  ? 0.5059 0.7500 0.4533 0.1308  0.0067  -0.2187 577  LEU A CG  
4161  C CD1 . LEU A 579  ? 0.5329 0.8039 0.4726 0.1320  0.0096  -0.2181 577  LEU A CD1 
4162  C CD2 . LEU A 579  ? 0.5209 0.7571 0.4848 0.1347  0.0022  -0.2304 577  LEU A CD2 
4163  N N   . PRO A 580  ? 0.4425 0.6490 0.3930 0.1266  -0.0070 -0.2257 578  PRO A N   
4164  C CA  . PRO A 580  ? 0.4482 0.6554 0.3916 0.1247  -0.0087 -0.2240 578  PRO A CA  
4165  C C   . PRO A 580  ? 0.4607 0.6903 0.3903 0.1243  -0.0047 -0.2182 578  PRO A C   
4166  O O   . PRO A 580  ? 0.5023 0.7508 0.4330 0.1275  -0.0056 -0.2251 578  PRO A O   
4167  C CB  . PRO A 580  ? 0.4650 0.6708 0.4208 0.1277  -0.0156 -0.2375 578  PRO A CB  
4168  C CG  . PRO A 580  ? 0.4320 0.6311 0.4025 0.1305  -0.0179 -0.2451 578  PRO A CG  
4169  C CD  . PRO A 580  ? 0.3983 0.6060 0.3636 0.1308  -0.0122 -0.2393 578  PRO A CD  
4170  N N   . GLN A 581  ? 0.4314 0.6597 0.3487 0.1204  -0.0004 -0.2053 579  GLN A N   
4171  C CA  . GLN A 581  ? 0.4318 0.6802 0.3362 0.1192  0.0037  -0.1970 579  GLN A CA  
4172  C C   . GLN A 581  ? 0.4684 0.7197 0.3666 0.1179  0.0012  -0.1960 579  GLN A C   
4173  O O   . GLN A 581  ? 0.4155 0.6577 0.3060 0.1142  0.0023  -0.1866 579  GLN A O   
4174  C CB  . GLN A 581  ? 0.4406 0.6859 0.3362 0.1154  0.0095  -0.1827 579  GLN A CB  
4175  C CG  . GLN A 581  ? 0.4279 0.6707 0.3295 0.1166  0.0122  -0.1830 579  GLN A CG  
4176  C CD  . GLN A 581  ? 0.5048 0.7698 0.4075 0.1195  0.0139  -0.1870 579  GLN A CD  
4177  O OE1 . GLN A 581  ? 0.4914 0.7565 0.4009 0.1213  0.0151  -0.1901 579  GLN A OE1 
4178  N NE2 . GLN A 581  ? 0.4562 0.7406 0.3525 0.1199  0.0139  -0.1868 579  GLN A NE2 
4179  N N   . LEU A 582  ? 0.4639 0.7282 0.3658 0.1211  -0.0023 -0.2061 580  LEU A N   
4180  C CA  . LEU A 582  ? 0.4817 0.7502 0.3785 0.1204  -0.0049 -0.2062 580  LEU A CA  
4181  C C   . LEU A 582  ? 0.4741 0.7620 0.3576 0.1186  -0.0010 -0.1957 580  LEU A C   
4182  O O   . LEU A 582  ? 0.4468 0.7469 0.3261 0.1182  0.0034  -0.1897 580  LEU A O   
4183  C CB  . LEU A 582  ? 0.4646 0.7397 0.3714 0.1246  -0.0104 -0.2212 580  LEU A CB  
4184  C CG  . LEU A 582  ? 0.5417 0.7960 0.4601 0.1249  -0.0160 -0.2295 580  LEU A CG  
4185  C CD1 . LEU A 582  ? 0.5554 0.7927 0.4840 0.1252  -0.0161 -0.2316 580  LEU A CD1 
4186  C CD2 . LEU A 582  ? 0.5011 0.7646 0.4281 0.1288  -0.0214 -0.2432 580  LEU A CD2 
4187  N N   . ALA A 583  ? 0.4571 0.7476 0.3345 0.1172  -0.0028 -0.1930 581  ALA A N   
4188  C CA  . ALA A 583  ? 0.4788 0.7875 0.3445 0.1154  0.0001  -0.1829 581  ALA A CA  
4189  C C   . ALA A 583  ? 0.5287 0.8624 0.3953 0.1186  0.0013  -0.1877 581  ALA A C   
4190  O O   . ALA A 583  ? 0.5450 0.8937 0.4039 0.1170  0.0053  -0.1779 581  ALA A O   
4191  C CB  . ALA A 583  ? 0.5451 0.8536 0.4062 0.1143  -0.0030 -0.1818 581  ALA A CB  
4192  N N   . THR A 584  ? 0.5091 0.8476 0.3856 0.1232  -0.0025 -0.2028 582  THR A N   
4193  C CA  . THR A 584  ? 0.5601 0.9232 0.4386 0.1270  -0.0023 -0.2096 582  THR A CA  
4194  C C   . THR A 584  ? 0.5194 0.8870 0.4015 0.1282  0.0009  -0.2100 582  THR A C   
4195  O O   . THR A 584  ? 0.5633 0.9533 0.4443 0.1303  0.0026  -0.2117 582  THR A O   
4196  C CB  . THR A 584  ? 0.5954 0.9615 0.4842 0.1316  -0.0081 -0.2262 582  THR A CB  
4197  O OG1 . THR A 584  ? 0.5842 0.9276 0.4840 0.1323  -0.0113 -0.2337 582  THR A OG1 
4198  C CG2 . THR A 584  ? 0.5821 0.9516 0.4663 0.1309  -0.0110 -0.2261 582  THR A CG2 
4199  N N   . GLY A 585  ? 0.5412 0.8887 0.4278 0.1269  0.0019  -0.2084 583  GLY A N   
4200  C CA  . GLY A 585  ? 0.5359 0.8855 0.4267 0.1280  0.0047  -0.2089 583  GLY A CA  
4201  C C   . GLY A 585  ? 0.5393 0.8671 0.4418 0.1294  0.0021  -0.2167 583  GLY A C   
4202  O O   . GLY A 585  ? 0.5847 0.8959 0.4923 0.1293  -0.0020 -0.2217 583  GLY A O   
4203  N N   . PRO A 586  ? 0.5445 0.8717 0.4518 0.1305  0.0044  -0.2176 584  PRO A N   
4204  C CA  . PRO A 586  ? 0.5047 0.8124 0.4246 0.1322  0.0015  -0.2255 584  PRO A CA  
4205  C C   . PRO A 586  ? 0.5543 0.8626 0.4861 0.1365  -0.0050 -0.2413 584  PRO A C   
4206  O O   . PRO A 586  ? 0.5231 0.8515 0.4552 0.1396  -0.0065 -0.2483 584  PRO A O   
4207  C CB  . PRO A 586  ? 0.5175 0.8317 0.4399 0.1333  0.0052  -0.2242 584  PRO A CB  
4208  C CG  . PRO A 586  ? 0.5390 0.8801 0.4529 0.1337  0.0085  -0.2203 584  PRO A CG  
4209  C CD  . PRO A 586  ? 0.5272 0.8719 0.4295 0.1302  0.0095  -0.2111 584  PRO A CD  
4210  N N   . ALA A 587  ? 0.5216 0.8078 0.4638 0.1366  -0.0091 -0.2465 585  ALA A N   
4211  C CA  . ALA A 587  ? 0.5214 0.8048 0.4766 0.1401  -0.0158 -0.2608 585  ALA A CA  
4212  C C   . ALA A 587  ? 0.5567 0.8286 0.5266 0.1425  -0.0183 -0.2682 585  ALA A C   
4213  O O   . ALA A 587  ? 0.5863 0.8455 0.5567 0.1406  -0.0155 -0.2616 585  ALA A O   
4214  C CB  . ALA A 587  ? 0.5484 0.8155 0.5046 0.1378  -0.0197 -0.2606 585  ALA A CB  
4215  N N   . ALA A 588  ? 0.5536 0.8305 0.5360 0.1468  -0.0238 -0.2820 586  ALA A N   
4216  C CA  . ALA A 588  ? 0.5784 0.8451 0.5762 0.1493  -0.0272 -0.2899 586  ALA A CA  
4217  C C   . ALA A 588  ? 0.6264 0.8667 0.6349 0.1474  -0.0321 -0.2910 586  ALA A C   
4218  O O   . ALA A 588  ? 0.5962 0.8287 0.6018 0.1449  -0.0339 -0.2888 586  ALA A O   
4219  C CB  . ALA A 588  ? 0.6296 0.9140 0.6371 0.1549  -0.0314 -0.3044 586  ALA A CB  
4220  N N   . GLY A 589  ? 0.6034 0.8303 0.6249 0.1483  -0.0343 -0.2941 587  GLY A N   
4221  C CA  . GLY A 589  ? 0.5634 0.7658 0.5966 0.1463  -0.0393 -0.2947 587  GLY A CA  
4222  C C   . GLY A 589  ? 0.5971 0.7868 0.6431 0.1472  -0.0406 -0.2958 587  GLY A C   
4223  O O   . GLY A 589  ? 0.5898 0.7905 0.6368 0.1500  -0.0384 -0.2982 587  GLY A O   
4224  N N   . GLU A 590  ? 0.5832 0.7497 0.6392 0.1446  -0.0444 -0.2936 588  GLU A N   
4225  C CA  . GLU A 590  ? 0.5526 0.7044 0.6219 0.1449  -0.0464 -0.2935 588  GLU A CA  
4226  C C   . GLU A 590  ? 0.5808 0.7287 0.6406 0.1427  -0.0395 -0.2820 588  GLU A C   
4227  O O   . GLU A 590  ? 0.5422 0.6812 0.5921 0.1386  -0.0361 -0.2717 588  GLU A O   
4228  C CB  . GLU A 590  ? 0.6378 0.7667 0.7204 0.1421  -0.0525 -0.2932 588  GLU A CB  
4229  N N   . THR A 591  ? 0.4961 0.6508 0.5596 0.1454  -0.0378 -0.2840 589  THR A N   
4230  C CA  . THR A 591  ? 0.5252 0.6799 0.5804 0.1441  -0.0311 -0.2742 589  THR A CA  
4231  C C   . THR A 591  ? 0.5357 0.6717 0.6042 0.1436  -0.0333 -0.2721 589  THR A C   
4232  O O   . THR A 591  ? 0.5371 0.6714 0.6208 0.1466  -0.0385 -0.2806 589  THR A O   
4233  C CB  . THR A 591  ? 0.5289 0.7078 0.5772 0.1475  -0.0268 -0.2771 589  THR A CB  
4234  O OG1 . THR A 591  ? 0.5370 0.7341 0.5734 0.1478  -0.0252 -0.2787 589  THR A OG1 
4235  C CG2 . THR A 591  ? 0.4467 0.6262 0.4861 0.1457  -0.0198 -0.2664 589  THR A CG2 
4236  N N   . ARG A 592  ? 0.4907 0.6135 0.5542 0.1400  -0.0297 -0.2607 590  ARG A N   
4237  C CA  . ARG A 592  ? 0.4962 0.6026 0.5711 0.1393  -0.0310 -0.2570 590  ARG A CA  
4238  C C   . ARG A 592  ? 0.4911 0.5973 0.5550 0.1374  -0.0238 -0.2458 590  ARG A C   
4239  O O   . ARG A 592  ? 0.4639 0.5786 0.5120 0.1357  -0.0184 -0.2398 590  ARG A O   
4240  C CB  . ARG A 592  ? 0.5703 0.6537 0.6561 0.1361  -0.0368 -0.2547 590  ARG A CB  
4241  C CG  . ARG A 592  ? 0.5643 0.6392 0.6387 0.1315  -0.0341 -0.2455 590  ARG A CG  
4242  C CD  . ARG A 592  ? 0.6475 0.6989 0.7328 0.1278  -0.0389 -0.2407 590  ARG A CD  
4243  N NE  . ARG A 592  ? 0.6385 0.6827 0.7125 0.1236  -0.0362 -0.2321 590  ARG A NE  
4244  C CZ  . ARG A 592  ? 0.6224 0.6614 0.6877 0.1212  -0.0311 -0.2219 590  ARG A CZ  
4245  N NH1 . ARG A 592  ? 0.5972 0.6365 0.6643 0.1224  -0.0281 -0.2184 590  ARG A NH1 
4246  N NH2 . ARG A 592  ? 0.6100 0.6441 0.6649 0.1178  -0.0291 -0.2153 590  ARG A NH2 
4247  N N   . THR A 593  ? 0.4826 0.5790 0.5555 0.1377  -0.0239 -0.2428 591  THR A N   
4248  C CA  . THR A 593  ? 0.4755 0.5724 0.5396 0.1363  -0.0173 -0.2327 591  THR A CA  
4249  C C   . THR A 593  ? 0.4897 0.5687 0.5500 0.1316  -0.0164 -0.2223 591  THR A C   
4250  O O   . THR A 593  ? 0.4532 0.5166 0.5209 0.1294  -0.0215 -0.2223 591  THR A O   
4251  C CB  . THR A 593  ? 0.5158 0.6108 0.5909 0.1386  -0.0176 -0.2336 591  THR A CB  
4252  O OG1 . THR A 593  ? 0.5231 0.5980 0.6147 0.1378  -0.0242 -0.2342 591  THR A OG1 
4253  C CG2 . THR A 593  ? 0.5193 0.6337 0.5971 0.1433  -0.0181 -0.2439 591  THR A CG2 
4254  N N   . VAL A 594  ? 0.4196 0.5018 0.4684 0.1301  -0.0098 -0.2131 592  VAL A N   
4255  C CA  . VAL A 594  ? 0.4371 0.5036 0.4814 0.1238  -0.0086 -0.1992 592  VAL A CA  
4256  C C   . VAL A 594  ? 0.4653 0.5240 0.5150 0.1219  -0.0070 -0.1905 592  VAL A C   
4257  O O   . VAL A 594  ? 0.4313 0.5030 0.4776 0.1241  -0.0027 -0.1902 592  VAL A O   
4258  C CB  . VAL A 594  ? 0.3860 0.4613 0.4115 0.1196  -0.0031 -0.1896 592  VAL A CB  
4259  C CG1 . VAL A 594  ? 0.3394 0.3982 0.3607 0.1118  -0.0021 -0.1735 592  VAL A CG1 
4260  C CG2 . VAL A 594  ? 0.4098 0.4939 0.4301 0.1217  -0.0049 -0.1987 592  VAL A CG2 
4261  N N   . LEU A 595  ? 0.4697 0.5084 0.5285 0.1181  -0.0106 -0.1836 593  LEU A N   
4262  C CA  . LEU A 595  ? 0.4288 0.4591 0.4953 0.1168  -0.0105 -0.1766 593  LEU A CA  
4263  C C   . LEU A 595  ? 0.4020 0.4231 0.4595 0.1091  -0.0070 -0.1592 593  LEU A C   
4264  O O   . LEU A 595  ? 0.4106 0.4251 0.4612 0.1045  -0.0071 -0.1531 593  LEU A O   
4265  C CB  . LEU A 595  ? 0.4708 0.4858 0.5564 0.1186  -0.0178 -0.1821 593  LEU A CB  
4266  C CG  . LEU A 595  ? 0.4850 0.5066 0.5829 0.1264  -0.0226 -0.2003 593  LEU A CG  
4267  C CD1 . LEU A 595  ? 0.5750 0.5791 0.6919 0.1258  -0.0304 -0.2017 593  LEU A CD1 
4268  C CD2 . LEU A 595  ? 0.4073 0.4460 0.5047 0.1315  -0.0192 -0.2063 593  LEU A CD2 
4269  N N   . ASN A 596  ? 0.3768 0.3982 0.4346 0.1080  -0.0040 -0.1519 594  ASN A N   
4270  C CA  . ASN A 596  ? 0.4128 0.4256 0.4638 0.1011  -0.0010 -0.1362 594  ASN A CA  
4271  C C   . ASN A 596  ? 0.3760 0.3692 0.4374 0.0976  -0.0061 -0.1310 594  ASN A C   
4272  O O   . ASN A 596  ? 0.3990 0.3858 0.4748 0.1003  -0.0103 -0.1352 594  ASN A O   
4273  C CB  . ASN A 596  ? 0.3735 0.3937 0.4231 0.1016  0.0032  -0.1315 594  ASN A CB  
4274  C CG  . ASN A 596  ? 0.3996 0.4122 0.4426 0.0949  0.0063  -0.1160 594  ASN A CG  
4275  O OD1 . ASN A 596  ? 0.4104 0.4090 0.4545 0.0903  0.0041  -0.1088 594  ASN A OD1 
4276  N ND2 . ASN A 596  ? 0.4224 0.4452 0.4590 0.0945  0.0113  -0.1111 594  ASN A ND2 
4277  N N   . PRO A 597  ? 0.3796 0.3635 0.4350 0.0918  -0.0061 -0.1220 595  PRO A N   
4278  C CA  . PRO A 597  ? 0.3693 0.3360 0.4349 0.0884  -0.0111 -0.1172 595  PRO A CA  
4279  C C   . PRO A 597  ? 0.3992 0.3588 0.4709 0.0862  -0.0111 -0.1085 595  PRO A C   
4280  O O   . PRO A 597  ? 0.3829 0.3300 0.4665 0.0848  -0.0159 -0.1063 595  PRO A O   
4281  C CB  . PRO A 597  ? 0.4031 0.3650 0.4583 0.0828  -0.0098 -0.1093 595  PRO A CB  
4282  C CG  . PRO A 597  ? 0.4163 0.3908 0.4559 0.0821  -0.0035 -0.1060 595  PRO A CG  
4283  C CD  . PRO A 597  ? 0.3406 0.3297 0.3803 0.0884  -0.0021 -0.1166 595  PRO A CD  
4284  N N   . GLY A 598  ? 0.3770 0.3447 0.4417 0.0860  -0.0060 -0.1037 596  GLY A N   
4285  C CA  . GLY A 598  ? 0.3783 0.3407 0.4486 0.0844  -0.0060 -0.0961 596  GLY A CA  
4286  C C   . GLY A 598  ? 0.4169 0.3824 0.4998 0.0900  -0.0083 -0.1039 596  GLY A C   
4287  O O   . GLY A 598  ? 0.3916 0.3515 0.4818 0.0891  -0.0094 -0.0984 596  GLY A O   
4288  N N   . ASP A 599  ? 0.3852 0.3600 0.4710 0.0960  -0.0091 -0.1170 597  ASP A N   
4289  C CA  . ASP A 599  ? 0.4136 0.3935 0.5113 0.1023  -0.0111 -0.1262 597  ASP A CA  
4290  C C   . ASP A 599  ? 0.3981 0.3871 0.4984 0.1084  -0.0130 -0.1415 597  ASP A C   
4291  O O   . ASP A 599  ? 0.4108 0.4155 0.5009 0.1109  -0.0085 -0.1463 597  ASP A O   
4292  C CB  . ASP A 599  ? 0.4109 0.4024 0.5027 0.1031  -0.0056 -0.1227 597  ASP A CB  
4293  C CG  . ASP A 599  ? 0.4590 0.4545 0.5642 0.1091  -0.0078 -0.1304 597  ASP A CG  
4294  O OD1 . ASP A 599  ? 0.4395 0.4308 0.5583 0.1136  -0.0135 -0.1406 597  ASP A OD1 
4295  O OD2 . ASP A 599  ? 0.4961 0.4990 0.5986 0.1092  -0.0040 -0.1263 597  ASP A OD2 
4296  N N   . HIS A 600  ? 0.4081 0.3878 0.5222 0.1108  -0.0197 -0.1491 598  HIS A N   
4297  C CA  . HIS A 600  ? 0.4716 0.4586 0.5891 0.1164  -0.0223 -0.1643 598  HIS A CA  
4298  C C   . HIS A 600  ? 0.4873 0.4903 0.6083 0.1239  -0.0209 -0.1764 598  HIS A C   
4299  O O   . HIS A 600  ? 0.5320 0.5460 0.6522 0.1288  -0.0215 -0.1893 598  HIS A O   
4300  C CB  . HIS A 600  ? 0.4515 0.4236 0.5852 0.1169  -0.0305 -0.1693 598  HIS A CB  
4301  C CG  . HIS A 600  ? 0.4466 0.4076 0.5755 0.1106  -0.0318 -0.1615 598  HIS A CG  
4302  N ND1 . HIS A 600  ? 0.4969 0.4461 0.6380 0.1104  -0.0387 -0.1657 598  HIS A ND1 
4303  C CD2 . HIS A 600  ? 0.4649 0.4252 0.5787 0.1045  -0.0272 -0.1499 598  HIS A CD2 
4304  C CE1 . HIS A 600  ? 0.5048 0.4472 0.6381 0.1043  -0.0381 -0.1571 598  HIS A CE1 
4305  N NE2 . HIS A 600  ? 0.5079 0.4567 0.6246 0.1008  -0.0312 -0.1476 598  HIS A NE2 
4306  N N   . ARG A 601  ? 0.4819 0.4875 0.6066 0.1250  -0.0190 -0.1728 599  ARG A N   
4307  C CA  . ARG A 601  ? 0.5073 0.5301 0.6337 0.1318  -0.0167 -0.1832 599  ARG A CA  
4308  C C   . ARG A 601  ? 0.4790 0.5209 0.5873 0.1315  -0.0091 -0.1823 599  ARG A C   
4309  O O   . ARG A 601  ? 0.4473 0.5066 0.5552 0.1374  -0.0073 -0.1934 599  ARG A O   
4310  C CB  . ARG A 601  ? 0.4676 0.4879 0.6025 0.1324  -0.0166 -0.1782 599  ARG A CB  
4311  C CG  . ARG A 601  ? 0.4573 0.4596 0.6110 0.1327  -0.0242 -0.1778 599  ARG A CG  
4312  C CD  . ARG A 601  ? 0.4329 0.4321 0.5920 0.1318  -0.0234 -0.1694 599  ARG A CD  
4313  N NE  . ARG A 601  ? 0.4838 0.4816 0.6285 0.1245  -0.0178 -0.1536 599  ARG A NE  
4314  C CZ  . ARG A 601  ? 0.5380 0.5328 0.6842 0.1221  -0.0164 -0.1439 599  ARG A CZ  
4315  N NH1 . ARG A 601  ? 0.5209 0.5135 0.6822 0.1261  -0.0201 -0.1473 599  ARG A NH1 
4316  N NH2 . ARG A 601  ? 0.5045 0.4986 0.6374 0.1156  -0.0115 -0.1306 599  ARG A NH2 
4317  N N   . ASP A 602  ? 0.4503 0.4897 0.5441 0.1247  -0.0049 -0.1694 600  ASP A N   
4318  C CA  . ASP A 602  ? 0.4500 0.5060 0.5268 0.1234  0.0020  -0.1663 600  ASP A CA  
4319  C C   . ASP A 602  ? 0.4708 0.5328 0.5406 0.1245  0.0014  -0.1736 600  ASP A C   
4320  O O   . ASP A 602  ? 0.4752 0.5265 0.5402 0.1199  0.0001  -0.1678 600  ASP A O   
4321  C CB  . ASP A 602  ? 0.4644 0.5142 0.5305 0.1157  0.0062  -0.1492 600  ASP A CB  
4322  C CG  . ASP A 602  ? 0.4859 0.5514 0.5353 0.1138  0.0128  -0.1446 600  ASP A CG  
4323  O OD1 . ASP A 602  ? 0.4823 0.5661 0.5289 0.1186  0.0152  -0.1534 600  ASP A OD1 
4324  O OD2 . ASP A 602  ? 0.4471 0.5071 0.4865 0.1074  0.0155  -0.1321 600  ASP A OD2 
4325  N N   . VAL A 603  ? 0.4644 0.5442 0.5338 0.1308  0.0022  -0.1866 601  VAL A N   
4326  C CA  . VAL A 603  ? 0.4635 0.5523 0.5255 0.1324  0.0020  -0.1942 601  VAL A CA  
4327  C C   . VAL A 603  ? 0.4667 0.5680 0.5099 0.1284  0.0089  -0.1847 601  VAL A C   
4328  O O   . VAL A 603  ? 0.4728 0.5896 0.5103 0.1294  0.0140  -0.1826 601  VAL A O   
4329  C CB  . VAL A 603  ? 0.4589 0.5619 0.5277 0.1392  -0.0005 -0.2101 601  VAL A CB  
4330  C CG1 . VAL A 603  ? 0.4815 0.5943 0.5412 0.1390  -0.0009 -0.2151 601  VAL A CG1 
4331  C CG2 . VAL A 603  ? 0.4802 0.5685 0.5677 0.1407  -0.0082 -0.2159 601  VAL A CG2 
4332  N N   . VAL A 604  ? 0.4157 0.5104 0.4500 0.1238  0.0087  -0.1786 602  VAL A N   
4333  C CA  . VAL A 604  ? 0.3919 0.4961 0.4094 0.1194  0.0145  -0.1683 602  VAL A CA  
4334  C C   . VAL A 604  ? 0.4261 0.5509 0.4348 0.1232  0.0163  -0.1771 602  VAL A C   
4335  O O   . VAL A 604  ? 0.4161 0.5565 0.4130 0.1218  0.0218  -0.1714 602  VAL A O   
4336  C CB  . VAL A 604  ? 0.4011 0.4881 0.4133 0.1123  0.0136  -0.1564 602  VAL A CB  
4337  C CG1 . VAL A 604  ? 0.3932 0.4888 0.3893 0.1078  0.0191  -0.1452 602  VAL A CG1 
4338  C CG2 . VAL A 604  ? 0.4135 0.4815 0.4344 0.1087  0.0117  -0.1479 602  VAL A CG2 
4339  N N   . GLY A 605  ? 0.4195 0.5453 0.4342 0.1277  0.0117  -0.1907 603  GLY A N   
4340  C CA  . GLY A 605  ? 0.4042 0.5499 0.4106 0.1311  0.0129  -0.1993 603  GLY A CA  
4341  C C   . GLY A 605  ? 0.4184 0.5583 0.4337 0.1328  0.0059  -0.2098 603  GLY A C   
4342  O O   . GLY A 605  ? 0.4312 0.5556 0.4608 0.1338  0.0005  -0.2142 603  GLY A O   
4343  N N   . SER A 606  ? 0.3834 0.5366 0.3905 0.1330  0.0058  -0.2133 604  SER A N   
4344  C CA  . SER A 606  ? 0.4213 0.5733 0.4363 0.1349  -0.0007 -0.2240 604  SER A CA  
4345  C C   . SER A 606  ? 0.4315 0.5844 0.4361 0.1324  -0.0010 -0.2219 604  SER A C   
4346  O O   . SER A 606  ? 0.4662 0.6323 0.4562 0.1307  0.0039  -0.2156 604  SER A O   
4347  C CB  . SER A 606  ? 0.4289 0.6005 0.4473 0.1392  -0.0016 -0.2338 604  SER A CB  
4348  O OG  . SER A 606  ? 0.5672 0.7377 0.5959 0.1416  -0.0018 -0.2362 604  SER A OG  
4349  N N   . VAL A 607  ? 0.3959 0.5352 0.4085 0.1319  -0.0069 -0.2268 605  VAL A N   
4350  C CA  . VAL A 607  ? 0.4333 0.5722 0.4379 0.1297  -0.0080 -0.2258 605  VAL A CA  
4351  C C   . VAL A 607  ? 0.4213 0.5670 0.4335 0.1325  -0.0138 -0.2378 605  VAL A C   
4352  O O   . VAL A 607  ? 0.4391 0.5766 0.4667 0.1346  -0.0192 -0.2456 605  VAL A O   
4353  C CB  . VAL A 607  ? 0.4495 0.5657 0.4559 0.1259  -0.0098 -0.2195 605  VAL A CB  
4354  C CG1 . VAL A 607  ? 0.4380 0.5357 0.4628 0.1264  -0.0159 -0.2239 605  VAL A CG1 
4355  C CG2 . VAL A 607  ? 0.4126 0.5290 0.4119 0.1239  -0.0116 -0.2196 605  VAL A CG2 
4356  N N   . THR A 608  ? 0.4106 0.5716 0.4123 0.1326  -0.0128 -0.2390 606  THR A N   
4357  C CA  . THR A 608  ? 0.4415 0.6093 0.4488 0.1350  -0.0182 -0.2497 606  THR A CA  
4358  C C   . THR A 608  ? 0.4700 0.6265 0.4740 0.1317  -0.0206 -0.2470 606  THR A C   
4359  O O   . THR A 608  ? 0.4397 0.6004 0.4295 0.1290  -0.0167 -0.2389 606  THR A O   
4360  C CB  . THR A 608  ? 0.5047 0.6990 0.5033 0.1375  -0.0157 -0.2533 606  THR A CB  
4361  O OG1 . THR A 608  ? 0.4863 0.6913 0.4880 0.1403  -0.0133 -0.2554 606  THR A OG1 
4362  C CG2 . THR A 608  ? 0.5033 0.7054 0.5083 0.1403  -0.0215 -0.2651 606  THR A CG2 
4363  N N   . GLU A 609  ? 0.4861 0.6283 0.5035 0.1318  -0.0271 -0.2533 607  GLU A N   
4364  C CA  . GLU A 609  ? 0.5183 0.6468 0.5345 0.1282  -0.0295 -0.2498 607  GLU A CA  
4365  C C   . GLU A 609  ? 0.5060 0.6466 0.5190 0.1294  -0.0323 -0.2563 607  GLU A C   
4366  O O   . GLU A 609  ? 0.5286 0.6835 0.5464 0.1332  -0.0347 -0.2661 607  GLU A O   
4367  C CB  . GLU A 609  ? 0.5600 0.6657 0.5925 0.1268  -0.0350 -0.2511 607  GLU A CB  
4368  C CG  . GLU A 609  ? 0.5793 0.6732 0.6145 0.1256  -0.0320 -0.2435 607  GLU A CG  
4369  C CD  . GLU A 609  ? 0.6631 0.7329 0.7112 0.1226  -0.0365 -0.2404 607  GLU A CD  
4370  O OE1 . GLU A 609  ? 0.7621 0.8252 0.8249 0.1233  -0.0430 -0.2474 607  GLU A OE1 
4371  O OE2 . GLU A 609  ? 0.6298 0.6880 0.6736 0.1194  -0.0335 -0.2305 607  GLU A OE2 
4372  N N   . THR A 610  ? 0.5115 0.6471 0.5160 0.1260  -0.0319 -0.2507 608  THR A N   
4373  C CA  . THR A 610  ? 0.4961 0.6438 0.4951 0.1266  -0.0337 -0.2549 608  THR A CA  
4374  C C   . THR A 610  ? 0.5066 0.6460 0.5203 0.1275  -0.0413 -0.2645 608  THR A C   
4375  O O   . THR A 610  ? 0.4832 0.6027 0.5068 0.1250  -0.0446 -0.2630 608  THR A O   
4376  C CB  . THR A 610  ? 0.5141 0.6590 0.4984 0.1226  -0.0304 -0.2446 608  THR A CB  
4377  O OG1 . THR A 610  ? 0.4772 0.6265 0.4496 0.1213  -0.0237 -0.2345 608  THR A OG1 
4378  C CG2 . THR A 610  ? 0.4761 0.6369 0.4525 0.1234  -0.0313 -0.2475 608  THR A CG2 
4379  N N   . SER A 611  ? 0.4799 0.6353 0.4953 0.1307  -0.0440 -0.2740 609  SER A N   
4380  C CA  . SER A 611  ? 0.4880 0.6376 0.5162 0.1314  -0.0512 -0.2828 609  SER A CA  
4381  C C   . SER A 611  ? 0.5130 0.6564 0.5342 0.1278  -0.0519 -0.2780 609  SER A C   
4382  O O   . SER A 611  ? 0.4969 0.6471 0.5022 0.1260  -0.0472 -0.2701 609  SER A O   
4383  C CB  . SER A 611  ? 0.5120 0.6816 0.5446 0.1364  -0.0540 -0.2951 609  SER A CB  
4384  O OG  . SER A 611  ? 0.5196 0.7068 0.5386 0.1368  -0.0516 -0.2942 609  SER A OG  
4385  N N   . GLU A 612  ? 0.5343 0.6646 0.5682 0.1266  -0.0581 -0.2824 610  GLU A N   
4386  C CA  . GLU A 612  ? 0.5176 0.6421 0.5464 0.1233  -0.0594 -0.2788 610  GLU A CA  
4387  C C   . GLU A 612  ? 0.4933 0.6383 0.5115 0.1253  -0.0586 -0.2822 610  GLU A C   
4388  O O   . GLU A 612  ? 0.5076 0.6536 0.5139 0.1227  -0.0565 -0.2757 610  GLU A O   
4389  C CB  . GLU A 612  ? 0.5905 0.6993 0.6364 0.1218  -0.0666 -0.2836 610  GLU A CB  
4390  C CG  . GLU A 612  ? 0.6179 0.7039 0.6720 0.1180  -0.0673 -0.2765 610  GLU A CG  
4391  C CD  . GLU A 612  ? 0.7152 0.7865 0.7863 0.1159  -0.0745 -0.2801 610  GLU A CD  
4392  O OE1 . GLU A 612  ? 0.7643 0.8431 0.8409 0.1178  -0.0789 -0.2887 610  GLU A OE1 
4393  O OE2 . GLU A 612  ? 0.7125 0.7653 0.7918 0.1124  -0.0757 -0.2740 610  GLU A OE2 
4394  N N   . GLU A 613  ? 0.4978 0.6600 0.5203 0.1301  -0.0602 -0.2924 611  GLU A N   
4395  C CA  . GLU A 613  ? 0.5334 0.7169 0.5459 0.1322  -0.0593 -0.2955 611  GLU A CA  
4396  C C   . GLU A 613  ? 0.4695 0.6648 0.4631 0.1312  -0.0519 -0.2853 611  GLU A C   
4397  O O   . GLU A 613  ? 0.4824 0.6856 0.4642 0.1298  -0.0503 -0.2806 611  GLU A O   
4398  C CB  . GLU A 613  ? 0.4827 0.6828 0.5045 0.1377  -0.0627 -0.3088 611  GLU A CB  
4399  N N   . ASP A 614  ? 0.5293 0.7258 0.5204 0.1316  -0.0476 -0.2812 612  ASP A N   
4400  C CA  . ASP A 614  ? 0.5060 0.7143 0.4802 0.1305  -0.0407 -0.2710 612  ASP A CA  
4401  C C   . ASP A 614  ? 0.4918 0.6864 0.4557 0.1254  -0.0378 -0.2584 612  ASP A C   
4402  O O   . ASP A 614  ? 0.4385 0.6435 0.3878 0.1239  -0.0337 -0.2502 612  ASP A O   
4403  C CB  . ASP A 614  ? 0.5135 0.7266 0.4886 0.1322  -0.0371 -0.2701 612  ASP A CB  
4404  C CG  . ASP A 614  ? 0.5438 0.7779 0.5235 0.1373  -0.0383 -0.2807 612  ASP A CG  
4405  O OD1 . ASP A 614  ? 0.6141 0.8624 0.5923 0.1393  -0.0407 -0.2867 612  ASP A OD1 
4406  O OD2 . ASP A 614  ? 0.5108 0.7477 0.4957 0.1395  -0.0371 -0.2833 612  ASP A OD2 
4407  N N   . ALA A 615  ? 0.4700 0.6419 0.4418 0.1227  -0.0400 -0.2564 613  ALA A N   
4408  C CA  . ALA A 615  ? 0.4399 0.5991 0.4030 0.1181  -0.0380 -0.2456 613  ALA A CA  
4409  C C   . ALA A 615  ? 0.4450 0.6095 0.4020 0.1171  -0.0401 -0.2457 613  ALA A C   
4410  O O   . ALA A 615  ? 0.4339 0.6008 0.3775 0.1145  -0.0369 -0.2362 613  ALA A O   
4411  C CB  . ALA A 615  ? 0.4301 0.5648 0.4044 0.1155  -0.0407 -0.2444 613  ALA A CB  
4412  N N   . ARG A 616  ? 0.4757 0.6428 0.4427 0.1191  -0.0457 -0.2562 614  ARG A N   
4413  C CA  . ARG A 616  ? 0.4824 0.6561 0.4439 0.1185  -0.0478 -0.2568 614  ARG A CA  
4414  C C   . ARG A 616  ? 0.4389 0.6366 0.3871 0.1204  -0.0442 -0.2547 614  ARG A C   
4415  O O   . ARG A 616  ? 0.4207 0.6232 0.3574 0.1184  -0.0428 -0.2479 614  ARG A O   
4416  C CB  . ARG A 616  ? 0.5214 0.6925 0.4978 0.1203  -0.0548 -0.2688 614  ARG A CB  
4417  C CG  . ARG A 616  ? 0.5729 0.7217 0.5582 0.1165  -0.0587 -0.2673 614  ARG A CG  
4418  C CD  . ARG A 616  ? 0.5732 0.7110 0.5779 0.1178  -0.0639 -0.2760 614  ARG A CD  
4419  N NE  . ARG A 616  ? 0.6604 0.8134 0.6726 0.1225  -0.0674 -0.2883 614  ARG A NE  
4420  C CZ  . ARG A 616  ? 0.6771 0.8256 0.7062 0.1248  -0.0721 -0.2975 614  ARG A CZ  
4421  N NH1 . ARG A 616  ? 0.7059 0.8347 0.7469 0.1225  -0.0743 -0.2955 614  ARG A NH1 
4422  N NH2 . ARG A 616  ? 0.6672 0.8318 0.7019 0.1295  -0.0750 -0.3087 614  ARG A NH2 
4423  N N   . ARG A 617  ? 0.4509 0.6640 0.4006 0.1241  -0.0428 -0.2600 615  ARG A N   
4424  C CA  . ARG A 617  ? 0.4403 0.6770 0.3776 0.1256  -0.0390 -0.2568 615  ARG A CA  
4425  C C   . ARG A 617  ? 0.4197 0.6558 0.3422 0.1221  -0.0329 -0.2419 615  ARG A C   
4426  O O   . ARG A 617  ? 0.4208 0.6696 0.3313 0.1210  -0.0307 -0.2352 615  ARG A O   
4427  C CB  . ARG A 617  ? 0.4339 0.6863 0.3765 0.1301  -0.0385 -0.2647 615  ARG A CB  
4428  N N   . ALA A 618  ? 0.4158 0.6372 0.3394 0.1201  -0.0304 -0.2362 616  ALA A N   
4429  C CA  . ALA A 618  ? 0.4091 0.6292 0.3198 0.1168  -0.0247 -0.2222 616  ALA A CA  
4430  C C   . ALA A 618  ? 0.4012 0.6144 0.3033 0.1132  -0.0252 -0.2141 616  ALA A C   
4431  O O   . ALA A 618  ? 0.4098 0.6324 0.2991 0.1113  -0.0215 -0.2038 616  ALA A O   
4432  C CB  . ALA A 618  ? 0.4171 0.6211 0.3323 0.1155  -0.0226 -0.2188 616  ALA A CB  
4433  N N   . VAL A 619  ? 0.4047 0.6018 0.3143 0.1120  -0.0297 -0.2183 617  VAL A N   
4434  C CA  . VAL A 619  ? 0.4250 0.6163 0.3269 0.1087  -0.0305 -0.2112 617  VAL A CA  
4435  C C   . VAL A 619  ? 0.4074 0.6180 0.3013 0.1098  -0.0309 -0.2111 617  VAL A C   
4436  O O   . VAL A 619  ? 0.4166 0.6316 0.2985 0.1075  -0.0287 -0.2008 617  VAL A O   
4437  C CB  . VAL A 619  ? 0.4285 0.6001 0.3410 0.1072  -0.0356 -0.2162 617  VAL A CB  
4438  C CG1 . VAL A 619  ? 0.4145 0.5816 0.3187 0.1039  -0.0365 -0.2090 617  VAL A CG1 
4439  C CG2 . VAL A 619  ? 0.4124 0.5646 0.3325 0.1056  -0.0350 -0.2147 617  VAL A CG2 
4440  N N   . ARG A 620  ? 0.4111 0.6339 0.3119 0.1135  -0.0340 -0.2223 618  ARG A N   
4441  C CA  . ARG A 620  ? 0.4355 0.6775 0.3293 0.1148  -0.0346 -0.2228 618  ARG A CA  
4442  C C   . ARG A 620  ? 0.4605 0.7206 0.3420 0.1146  -0.0292 -0.2133 618  ARG A C   
4443  O O   . ARG A 620  ? 0.5002 0.7707 0.3715 0.1133  -0.0283 -0.2061 618  ARG A O   
4444  C CB  . ARG A 620  ? 0.4712 0.7235 0.3757 0.1191  -0.0391 -0.2375 618  ARG A CB  
4445  N N   . LEU A 621  ? 0.4273 0.6911 0.3098 0.1156  -0.0257 -0.2126 619  LEU A N   
4446  C CA  . LEU A 621  ? 0.4334 0.7131 0.3049 0.1149  -0.0204 -0.2023 619  LEU A CA  
4447  C C   . LEU A 621  ? 0.4588 0.7296 0.3197 0.1102  -0.0173 -0.1870 619  LEU A C   
4448  O O   . LEU A 621  ? 0.4663 0.7498 0.3168 0.1086  -0.0149 -0.1771 619  LEU A O   
4449  C CB  . LEU A 621  ? 0.4279 0.7118 0.3038 0.1168  -0.0175 -0.2049 619  LEU A CB  
4450  C CG  . LEU A 621  ? 0.4274 0.7247 0.3129 0.1218  -0.0202 -0.2193 619  LEU A CG  
4451  C CD1 . LEU A 621  ? 0.4393 0.7351 0.3316 0.1235  -0.0182 -0.2228 619  LEU A CD1 
4452  C CD2 . LEU A 621  ? 0.4513 0.7749 0.3299 0.1235  -0.0193 -0.2187 619  LEU A CD2 
4453  N N   . ALA A 622  ? 0.4095 0.6585 0.2733 0.1080  -0.0174 -0.1846 620  ALA A N   
4454  C CA  . ALA A 622  ? 0.4359 0.6749 0.2907 0.1038  -0.0152 -0.1711 620  ALA A CA  
4455  C C   . ALA A 622  ? 0.4320 0.6735 0.2810 0.1023  -0.0179 -0.1676 620  ALA A C   
4456  O O   . ALA A 622  ? 0.4374 0.6839 0.2761 0.0997  -0.0157 -0.1553 620  ALA A O   
4457  C CB  . ALA A 622  ? 0.3877 0.6032 0.2485 0.1022  -0.0158 -0.1715 620  ALA A CB  
4458  N N   . ALA A 623  ? 0.4187 0.6563 0.2748 0.1039  -0.0229 -0.1781 621  ALA A N   
4459  C CA  . ALA A 623  ? 0.4401 0.6808 0.2914 0.1029  -0.0257 -0.1759 621  ALA A CA  
4460  C C   . ALA A 623  ? 0.4901 0.7539 0.3327 0.1036  -0.0240 -0.1710 621  ALA A C   
4461  O O   . ALA A 623  ? 0.4518 0.7191 0.2855 0.1013  -0.0235 -0.1606 621  ALA A O   
4462  C CB  . ALA A 623  ? 0.4162 0.6511 0.2782 0.1048  -0.0314 -0.1893 621  ALA A CB  
4463  N N   . ASP A 624  ? 0.4842 0.7645 0.3298 0.1069  -0.0232 -0.1780 622  ASP A N   
4464  C CA  . ASP A 624  ? 0.5592 0.8631 0.3976 0.1079  -0.0217 -0.1741 622  ASP A CA  
4465  C C   . ASP A 624  ? 0.5448 0.8544 0.3729 0.1047  -0.0167 -0.1580 622  ASP A C   
4466  O O   . ASP A 624  ? 0.5366 0.8603 0.3569 0.1036  -0.0160 -0.1499 622  ASP A O   
4467  C CB  . ASP A 624  ? 0.5507 0.8711 0.3954 0.1123  -0.0220 -0.1858 622  ASP A CB  
4468  C CG  . ASP A 624  ? 0.6506 0.9712 0.5048 0.1156  -0.0275 -0.2008 622  ASP A CG  
4469  O OD1 . ASP A 624  ? 0.7322 1.0457 0.5859 0.1144  -0.0308 -0.2010 622  ASP A OD1 
4470  O OD2 . ASP A 624  ? 0.7471 1.0755 0.6097 0.1194  -0.0286 -0.2125 622  ASP A OD2 
4471  N N   . ALA A 625  ? 0.5518 0.8508 0.3801 0.1030  -0.0134 -0.1527 623  ALA A N   
4472  C CA  . ALA A 625  ? 0.5672 0.8711 0.3872 0.0999  -0.0088 -0.1375 623  ALA A CA  
4473  C C   . ALA A 625  ? 0.5310 0.8193 0.3452 0.0957  -0.0086 -0.1251 623  ALA A C   
4474  O O   . ALA A 625  ? 0.5225 0.8145 0.3299 0.0926  -0.0053 -0.1112 623  ALA A O   
4475  C CB  . ALA A 625  ? 0.5744 0.8773 0.3979 0.1004  -0.0051 -0.1382 623  ALA A CB  
4476  N N   . ALA A 626  ? 0.5181 0.7895 0.3354 0.0953  -0.0121 -0.1296 624  ALA A N   
4477  C CA  . ALA A 626  ? 0.4989 0.7552 0.3114 0.0917  -0.0122 -0.1187 624  ALA A CA  
4478  C C   . ALA A 626  ? 0.4969 0.7630 0.3003 0.0890  -0.0116 -0.1047 624  ALA A C   
4479  O O   . ALA A 626  ? 0.5253 0.7853 0.3240 0.0858  -0.0092 -0.0916 624  ALA A O   
4480  C CB  . ALA A 626  ? 0.5107 0.7509 0.3286 0.0920  -0.0169 -0.1270 624  ALA A CB  
4481  N N   . PRO A 627  ? 0.5103 0.7909 0.3113 0.0901  -0.0138 -0.1061 625  PRO A N   
4482  C CA  . PRO A 627  ? 0.5536 0.8427 0.3465 0.0874  -0.0133 -0.0916 625  PRO A CA  
4483  C C   . PRO A 627  ? 0.4697 0.7680 0.2587 0.0852  -0.0086 -0.0794 625  PRO A C   
4484  O O   . PRO A 627  ? 0.5140 0.8084 0.2983 0.0816  -0.0077 -0.0648 625  PRO A O   
4485  C CB  . PRO A 627  ? 0.5069 0.8130 0.2992 0.0898  -0.0160 -0.0978 625  PRO A CB  
4486  C CG  . PRO A 627  ? 0.5588 0.8575 0.3588 0.0929  -0.0195 -0.1142 625  PRO A CG  
4487  C CD  . PRO A 627  ? 0.5622 0.8509 0.3681 0.0937  -0.0173 -0.1203 625  PRO A CD  
4488  N N   . ASP A 628  ? 0.4565 0.7668 0.2481 0.0872  -0.0059 -0.0849 626  ASP A N   
4489  C CA  . ASP A 628  ? 0.5096 0.8302 0.2982 0.0851  -0.0015 -0.0736 626  ASP A CA  
4490  C C   . ASP A 628  ? 0.5015 0.8053 0.2898 0.0818  0.0010  -0.0642 626  ASP A C   
4491  O O   . ASP A 628  ? 0.5171 0.8228 0.3017 0.0782  0.0031  -0.0494 626  ASP A O   
4492  C CB  . ASP A 628  ? 0.5360 0.8720 0.3285 0.0883  0.0006  -0.0832 626  ASP A CB  
4493  C CG  . ASP A 628  ? 0.6103 0.9638 0.4037 0.0919  -0.0020 -0.0932 626  ASP A CG  
4494  O OD1 . ASP A 628  ? 0.6279 0.9885 0.4167 0.0908  -0.0039 -0.0877 626  ASP A OD1 
4495  O OD2 . ASP A 628  ? 0.6745 1.0348 0.4735 0.0957  -0.0023 -0.1067 626  ASP A OD2 
4496  N N   . TRP A 629  ? 0.5032 0.7905 0.2961 0.0830  0.0007  -0.0725 627  TRP A N   
4497  C CA  . TRP A 629  ? 0.4037 0.6756 0.1965 0.0802  0.0032  -0.0641 627  TRP A CA  
4498  C C   . TRP A 629  ? 0.4868 0.7455 0.2760 0.0771  0.0011  -0.0538 627  TRP A C   
4499  O O   . TRP A 629  ? 0.4482 0.7011 0.2350 0.0736  0.0031  -0.0405 627  TRP A O   
4500  C CB  . TRP A 629  ? 0.4274 0.6864 0.2268 0.0825  0.0034  -0.0761 627  TRP A CB  
4501  C CG  . TRP A 629  ? 0.4289 0.6717 0.2283 0.0800  0.0057  -0.0686 627  TRP A CG  
4502  C CD1 . TRP A 629  ? 0.4205 0.6416 0.2247 0.0791  0.0040  -0.0707 627  TRP A CD1 
4503  C CD2 . TRP A 629  ? 0.4249 0.6700 0.2223 0.0772  0.0100  -0.0566 627  TRP A CD2 
4504  N NE1 . TRP A 629  ? 0.4220 0.6301 0.2298 0.0754  0.0068  -0.0605 627  TRP A NE1 
4505  C CE2 . TRP A 629  ? 0.3788 0.6024 0.1807 0.0747  0.0105  -0.0523 627  TRP A CE2 
4506  C CE3 . TRP A 629  ? 0.4391 0.7005 0.2345 0.0758  0.0131  -0.0486 627  TRP A CE3 
4507  C CZ2 . TRP A 629  ? 0.4161 0.6351 0.2192 0.0713  0.0141  -0.0409 627  TRP A CZ2 
4508  C CZ3 . TRP A 629  ? 0.4348 0.6928 0.2299 0.0726  0.0167  -0.0374 627  TRP A CZ3 
4509  C CH2 . TRP A 629  ? 0.4161 0.6549 0.2126 0.0710  0.0173  -0.0341 627  TRP A CH2 
4510  N N   . ALA A 630  ? 0.4496 0.7035 0.2388 0.0783  -0.0032 -0.0596 628  ALA A N   
4511  C CA  . ALA A 630  ? 0.5037 0.7469 0.2895 0.0757  -0.0056 -0.0499 628  ALA A CA  
4512  C C   . ALA A 630  ? 0.4858 0.7397 0.2666 0.0727  -0.0050 -0.0346 628  ALA A C   
4513  O O   . ALA A 630  ? 0.4715 0.7160 0.2504 0.0698  -0.0060 -0.0231 628  ALA A O   
4514  C CB  . ALA A 630  ? 0.4561 0.6946 0.2434 0.0776  -0.0104 -0.0597 628  ALA A CB  
4515  N N   . ALA A 631  ? 0.4705 0.7439 0.2500 0.0734  -0.0036 -0.0343 629  ALA A N   
4516  C CA  . ALA A 631  ? 0.5181 0.8029 0.2937 0.0705  -0.0033 -0.0199 629  ALA A CA  
4517  C C   . ALA A 631  ? 0.5135 0.7974 0.2893 0.0669  0.0005  -0.0067 629  ALA A C   
4518  O O   . ALA A 631  ? 0.5404 0.8281 0.3143 0.0636  0.0003  0.0075  629  ALA A O   
4519  C CB  . ALA A 631  ? 0.4962 0.8035 0.2706 0.0727  -0.0033 -0.0248 629  ALA A CB  
4520  N N   . VAL A 632  ? 0.4831 0.7624 0.2618 0.0674  0.0038  -0.0108 630  VAL A N   
4521  C CA  . VAL A 632  ? 0.4962 0.7720 0.2757 0.0638  0.0072  0.0015  630  VAL A CA  
4522  C C   . VAL A 632  ? 0.4526 0.7099 0.2321 0.0608  0.0054  0.0118  630  VAL A C   
4523  O O   . VAL A 632  ? 0.4610 0.7030 0.2414 0.0622  0.0037  0.0053  630  VAL A O   
4524  C CB  . VAL A 632  ? 0.4430 0.7168 0.2260 0.0654  0.0108  -0.0063 630  VAL A CB  
4525  C CG1 . VAL A 632  ? 0.3983 0.6668 0.1827 0.0615  0.0141  0.0065  630  VAL A CG1 
4526  C CG2 . VAL A 632  ? 0.4422 0.7355 0.2261 0.0686  0.0123  -0.0162 630  VAL A CG2 
4527  N N   . PRO A 633  ? 0.4344 0.6924 0.2135 0.0567  0.0053  0.0276  631  PRO A N   
4528  C CA  . PRO A 633  ? 0.4434 0.6842 0.2235 0.0540  0.0030  0.0376  631  PRO A CA  
4529  C C   . PRO A 633  ? 0.4847 0.7086 0.2674 0.0538  0.0048  0.0357  631  PRO A C   
4530  O O   . PRO A 633  ? 0.4478 0.6741 0.2323 0.0538  0.0086  0.0335  631  PRO A O   
4531  C CB  . PRO A 633  ? 0.4655 0.7120 0.2469 0.0496  0.0035  0.0543  631  PRO A CB  
4532  C CG  . PRO A 633  ? 0.4641 0.7329 0.2431 0.0506  0.0043  0.0523  631  PRO A CG  
4533  C CD  . PRO A 633  ? 0.4653 0.7411 0.2438 0.0547  0.0068  0.0366  631  PRO A CD  
4534  N N   . PRO A 634  ? 0.4243 0.6270 0.2133 0.0527  0.0020  0.0353  632  PRO A N   
4535  C CA  . PRO A 634  ? 0.4044 0.5862 0.2019 0.0513  0.0034  0.0325  632  PRO A CA  
4536  C C   . PRO A 634  ? 0.4485 0.6289 0.2483 0.0481  0.0069  0.0424  632  PRO A C   
4537  O O   . PRO A 634  ? 0.3925 0.5654 0.1969 0.0481  0.0096  0.0374  632  PRO A O   
4538  C CB  . PRO A 634  ? 0.4284 0.5919 0.2309 0.0497  -0.0004 0.0355  632  PRO A CB  
4539  C CG  . PRO A 634  ? 0.4440 0.6172 0.2413 0.0520  -0.0040 0.0318  632  PRO A CG  
4540  C CD  . PRO A 634  ? 0.4569 0.6547 0.2454 0.0529  -0.0027 0.0362  632  PRO A CD  
4541  N N   . SER A 635  ? 0.4454 0.6330 0.2428 0.0453  0.0065  0.0567  633  SER A N   
4542  C CA  . SER A 635  ? 0.4326 0.6196 0.2329 0.0419  0.0095  0.0670  633  SER A CA  
4543  C C   . SER A 635  ? 0.4339 0.6362 0.2310 0.0435  0.0140  0.0618  633  SER A C   
4544  O O   . SER A 635  ? 0.4302 0.6261 0.2319 0.0421  0.0169  0.0626  633  SER A O   
4545  C CB  . SER A 635  ? 0.4992 0.6933 0.2976 0.0386  0.0077  0.0834  633  SER A CB  
4546  O OG  . SER A 635  ? 0.6127 0.8179 0.4125 0.0360  0.0109  0.0905  633  SER A OG  
4547  N N   . GLU A 636  ? 0.4164 0.6380 0.2076 0.0464  0.0144  0.0555  634  GLU A N   
4548  C CA  . GLU A 636  ? 0.4311 0.6663 0.2226 0.0478  0.0183  0.0493  634  GLU A CA  
4549  C C   . GLU A 636  ? 0.4478 0.6774 0.2396 0.0518  0.0198  0.0344  634  GLU A C   
4550  O O   . GLU A 636  ? 0.4264 0.6587 0.2206 0.0522  0.0233  0.0316  634  GLU A O   
4551  C CB  . GLU A 636  ? 0.4669 0.7229 0.2557 0.0491  0.0178  0.0470  634  GLU A CB  
4552  C CG  . GLU A 636  ? 0.5562 0.8287 0.3459 0.0506  0.0215  0.0416  634  GLU A CG  
4553  C CD  . GLU A 636  ? 0.5774 0.8477 0.3711 0.0472  0.0250  0.0502  634  GLU A CD  
4554  O OE1 . GLU A 636  ? 0.6037 0.8709 0.3995 0.0427  0.0246  0.0648  634  GLU A OE1 
4555  O OE2 . GLU A 636  ? 0.5480 0.8195 0.3435 0.0492  0.0280  0.0423  634  GLU A OE2 
4556  N N   . ARG A 637  ? 0.4036 0.6220 0.1968 0.0541  0.0166  0.0246  635  ARG A N   
4557  C CA  . ARG A 637  ? 0.3955 0.6012 0.1949 0.0564  0.0171  0.0113  635  ARG A CA  
4558  C C   . ARG A 637  ? 0.3778 0.5646 0.1850 0.0532  0.0187  0.0163  635  ARG A C   
4559  O O   . ARG A 637  ? 0.3771 0.5609 0.1883 0.0544  0.0211  0.0097  635  ARG A O   
4560  C CB  . ARG A 637  ? 0.3792 0.5748 0.1802 0.0584  0.0129  0.0020  635  ARG A CB  
4561  C CG  . ARG A 637  ? 0.3783 0.5930 0.1716 0.0615  0.0109  -0.0028 635  ARG A CG  
4562  C CD  . ARG A 637  ? 0.4186 0.6256 0.2143 0.0643  0.0072  -0.0155 635  ARG A CD  
4563  N NE  . ARG A 637  ? 0.4233 0.6089 0.2245 0.0617  0.0044  -0.0117 635  ARG A NE  
4564  C CZ  . ARG A 637  ? 0.4453 0.6294 0.2445 0.0614  0.0007  -0.0096 635  ARG A CZ  
4565  N NH1 . ARG A 637  ? 0.4299 0.6323 0.2215 0.0632  -0.0009 -0.0095 635  ARG A NH1 
4566  N NH2 . ARG A 637  ? 0.3884 0.5530 0.1936 0.0594  -0.0016 -0.0078 635  ARG A NH2 
4567  N N   . ALA A 638  ? 0.3506 0.5251 0.1602 0.0493  0.0172  0.0280  636  ALA A N   
4568  C CA  . ALA A 638  ? 0.3755 0.5330 0.1922 0.0461  0.0185  0.0334  636  ALA A CA  
4569  C C   . ALA A 638  ? 0.3770 0.5445 0.1934 0.0446  0.0226  0.0396  636  ALA A C   
4570  O O   . ALA A 638  ? 0.3341 0.4924 0.1560 0.0438  0.0247  0.0379  636  ALA A O   
4571  C CB  . ALA A 638  ? 0.3615 0.5057 0.1810 0.0426  0.0157  0.0441  636  ALA A CB  
4572  N N   . ALA A 639  ? 0.4219 0.6089 0.2319 0.0440  0.0236  0.0473  637  ALA A N   
4573  C CA  . ALA A 639  ? 0.3901 0.5898 0.1994 0.0427  0.0276  0.0530  637  ALA A CA  
4574  C C   . ALA A 639  ? 0.4015 0.6078 0.2115 0.0464  0.0306  0.0401  637  ALA A C   
4575  O O   . ALA A 639  ? 0.3840 0.5902 0.1974 0.0453  0.0338  0.0418  637  ALA A O   
4576  C CB  . ALA A 639  ? 0.3863 0.6073 0.1895 0.0416  0.0278  0.0622  637  ALA A CB  
4577  N N   . CYS A 640  ? 0.4097 0.6219 0.2169 0.0510  0.0295  0.0269  638  CYS A N   
4578  C CA  . CYS A 640  ? 0.3555 0.5716 0.1649 0.0549  0.0315  0.0133  638  CYS A CA  
4579  C C   . CYS A 640  ? 0.3920 0.5861 0.2104 0.0540  0.0317  0.0100  638  CYS A C   
4580  O O   . CYS A 640  ? 0.3788 0.5747 0.2008 0.0549  0.0345  0.0060  638  CYS A O   
4581  C CB  . CYS A 640  ? 0.3997 0.6222 0.2065 0.0597  0.0291  -0.0007 638  CYS A CB  
4582  S SG  . CYS A 640  ? 0.4358 0.6859 0.2347 0.0617  0.0290  -0.0013 638  CYS A SG  
4583  N N   . LEU A 641  ? 0.3348 0.5090 0.1572 0.0523  0.0286  0.0109  639  LEU A N   
4584  C CA  . LEU A 641  ? 0.3346 0.4886 0.1653 0.0512  0.0286  0.0082  639  LEU A CA  
4585  C C   . LEU A 641  ? 0.3504 0.5003 0.1842 0.0474  0.0313  0.0188  639  LEU A C   
4586  O O   . LEU A 641  ? 0.3588 0.5023 0.1980 0.0476  0.0331  0.0154  639  LEU A O   
4587  C CB  . LEU A 641  ? 0.3231 0.4587 0.1568 0.0500  0.0249  0.0079  639  LEU A CB  
4588  C CG  . LEU A 641  ? 0.3225 0.4527 0.1584 0.0533  0.0223  -0.0054 639  LEU A CG  
4589  C CD1 . LEU A 641  ? 0.3680 0.5165 0.1972 0.0569  0.0214  -0.0119 639  LEU A CD1 
4590  C CD2 . LEU A 641  ? 0.3661 0.4791 0.2049 0.0511  0.0190  -0.0027 639  LEU A CD2 
4591  N N   . ASP A 642  ? 0.3855 0.5388 0.2165 0.0439  0.0312  0.0319  640  ASP A N   
4592  C CA  . ASP A 642  ? 0.3422 0.4922 0.1769 0.0401  0.0334  0.0422  640  ASP A CA  
4593  C C   . ASP A 642  ? 0.3472 0.5136 0.1807 0.0413  0.0375  0.0409  640  ASP A C   
4594  O O   . ASP A 642  ? 0.3469 0.5081 0.1854 0.0396  0.0396  0.0431  640  ASP A O   
4595  C CB  . ASP A 642  ? 0.3794 0.5305 0.2123 0.0361  0.0320  0.0566  640  ASP A CB  
4596  C CG  . ASP A 642  ? 0.3933 0.5242 0.2303 0.0342  0.0283  0.0594  640  ASP A CG  
4597  O OD1 . ASP A 642  ? 0.3834 0.4983 0.2258 0.0346  0.0277  0.0529  640  ASP A OD1 
4598  O OD2 . ASP A 642  ? 0.4301 0.5617 0.2653 0.0322  0.0258  0.0681  640  ASP A OD2 
4599  N N   . ARG A 643  ? 0.3701 0.5575 0.1969 0.0442  0.0386  0.0372  641  ARG A N   
4600  C CA  . ARG A 643  ? 0.3555 0.5601 0.1813 0.0458  0.0426  0.0346  641  ARG A CA  
4601  C C   . ARG A 643  ? 0.3722 0.5694 0.2038 0.0492  0.0434  0.0215  641  ARG A C   
4602  O O   . ARG A 643  ? 0.4047 0.6050 0.2398 0.0490  0.0464  0.0216  641  ARG A O   
4603  C CB  . ARG A 643  ? 0.3982 0.6281 0.2156 0.0486  0.0434  0.0324  641  ARG A CB  
4604  C CG  . ARG A 643  ? 0.3910 0.6315 0.2060 0.0442  0.0434  0.0473  641  ARG A CG  
4605  C CD  . ARG A 643  ? 0.3844 0.6468 0.1971 0.0458  0.0434  0.0443  641  ARG A CD  
4606  N NE  . ARG A 643  ? 0.4247 0.6898 0.2332 0.0496  0.0406  0.0345  641  ARG A NE  
4607  C CZ  . ARG A 643  ? 0.4253 0.6917 0.2306 0.0484  0.0375  0.0397  641  ARG A CZ  
4608  N NH1 . ARG A 643  ? 0.4113 0.6754 0.2174 0.0435  0.0365  0.0547  641  ARG A NH1 
4609  N NH2 . ARG A 643  ? 0.3879 0.6576 0.1898 0.0521  0.0350  0.0295  641  ARG A NH2 
4610  N N   . ALA A 644  ? 0.3350 0.5222 0.1681 0.0522  0.0406  0.0104  642  ALA A N   
4611  C CA  . ALA A 644  ? 0.3554 0.5339 0.1951 0.0552  0.0407  -0.0014 642  ALA A CA  
4612  C C   . ALA A 644  ? 0.3798 0.5395 0.2268 0.0519  0.0412  0.0037  642  ALA A C   
4613  O O   . ALA A 644  ? 0.3390 0.4974 0.1910 0.0531  0.0431  -0.0007 642  ALA A O   
4614  C CB  . ALA A 644  ? 0.3799 0.5503 0.2206 0.0583  0.0371  -0.0129 642  ALA A CB  
4615  N N   . ALA A 645  ? 0.3546 0.5001 0.2026 0.0478  0.0394  0.0129  643  ALA A N   
4616  C CA  . ALA A 645  ? 0.3236 0.4523 0.1784 0.0446  0.0397  0.0177  643  ALA A CA  
4617  C C   . ALA A 645  ? 0.3847 0.5221 0.2407 0.0428  0.0433  0.0245  643  ALA A C   
4618  O O   . ALA A 645  ? 0.3854 0.5157 0.2472 0.0426  0.0446  0.0224  643  ALA A O   
4619  C CB  . ALA A 645  ? 0.3399 0.4542 0.1953 0.0408  0.0371  0.0264  643  ALA A CB  
4620  N N   . GLU A 646  ? 0.3694 0.5225 0.2201 0.0412  0.0449  0.0330  644  GLU A N   
4621  C CA  . GLU A 646  ? 0.4148 0.5783 0.2667 0.0392  0.0484  0.0400  644  GLU A CA  
4622  C C   . GLU A 646  ? 0.3635 0.5375 0.2169 0.0432  0.0511  0.0298  644  GLU A C   
4623  O O   . GLU A 646  ? 0.3770 0.5495 0.2354 0.0422  0.0533  0.0315  644  GLU A O   
4624  C CB  . GLU A 646  ? 0.3869 0.5677 0.2326 0.0371  0.0493  0.0505  644  GLU A CB  
4625  C CG  . GLU A 646  ? 0.4752 0.6458 0.3208 0.0328  0.0465  0.0619  644  GLU A CG  
4626  C CD  . GLU A 646  ? 0.5416 0.6973 0.3944 0.0285  0.0464  0.0700  644  GLU A CD  
4627  O OE1 . GLU A 646  ? 0.5896 0.7526 0.4449 0.0268  0.0493  0.0745  644  GLU A OE1 
4628  O OE2 . GLU A 646  ? 0.5788 0.7160 0.4350 0.0268  0.0434  0.0715  644  GLU A OE2 
4629  N N   . LEU A 647  ? 0.3345 0.5189 0.1845 0.0480  0.0507  0.0188  645  LEU A N   
4630  C CA  . LEU A 647  ? 0.3642 0.5592 0.2163 0.0525  0.0529  0.0078  645  LEU A CA  
4631  C C   . LEU A 647  ? 0.3626 0.5395 0.2232 0.0536  0.0519  0.0007  645  LEU A C   
4632  O O   . LEU A 647  ? 0.3460 0.5267 0.2111 0.0550  0.0541  -0.0026 645  LEU A O   
4633  C CB  . LEU A 647  ? 0.3562 0.5652 0.2032 0.0576  0.0519  -0.0032 645  LEU A CB  
4634  C CG  . LEU A 647  ? 0.4089 0.6426 0.2473 0.0576  0.0537  0.0017  645  LEU A CG  
4635  C CD1 . LEU A 647  ? 0.4043 0.6501 0.2377 0.0627  0.0520  -0.0100 645  LEU A CD1 
4636  C CD2 . LEU A 647  ? 0.4231 0.6749 0.2618 0.0577  0.0582  0.0045  645  LEU A CD2 
4637  N N   . MET A 648  ? 0.3426 0.5007 0.2057 0.0531  0.0484  -0.0019 646  MET A N   
4638  C CA  . MET A 648  ? 0.3488 0.4897 0.2201 0.0538  0.0472  -0.0076 646  MET A CA  
4639  C C   . MET A 648  ? 0.3738 0.5058 0.2495 0.0497  0.0488  0.0016  646  MET A C   
4640  O O   . MET A 648  ? 0.3914 0.5179 0.2734 0.0507  0.0495  -0.0023 646  MET A O   
4641  C CB  . MET A 648  ? 0.3406 0.4646 0.2133 0.0536  0.0432  -0.0111 646  MET A CB  
4642  C CG  . MET A 648  ? 0.3829 0.5122 0.2541 0.0582  0.0410  -0.0229 646  MET A CG  
4643  S SD  . MET A 648  ? 0.4030 0.5102 0.2796 0.0581  0.0365  -0.0286 646  MET A SD  
4644  C CE  . MET A 648  ? 0.4072 0.5265 0.2811 0.0634  0.0343  -0.0419 646  MET A CE  
4645  N N   . GLN A 649  ? 0.3641 0.4942 0.2371 0.0451  0.0490  0.0138  647  GLN A N   
4646  C CA  . GLN A 649  ? 0.3459 0.4684 0.2233 0.0410  0.0503  0.0227  647  GLN A CA  
4647  C C   . GLN A 649  ? 0.3836 0.5205 0.2626 0.0417  0.0540  0.0233  647  GLN A C   
4648  O O   . GLN A 649  ? 0.3793 0.5096 0.2643 0.0410  0.0549  0.0234  647  GLN A O   
4649  C CB  . GLN A 649  ? 0.3492 0.4688 0.2240 0.0363  0.0495  0.0353  647  GLN A CB  
4650  C CG  . GLN A 649  ? 0.3678 0.4775 0.2481 0.0320  0.0500  0.0438  647  GLN A CG  
4651  C CD  . GLN A 649  ? 0.3540 0.4427 0.2396 0.0311  0.0475  0.0411  647  GLN A CD  
4652  O OE1 . GLN A 649  ? 0.3647 0.4428 0.2496 0.0295  0.0448  0.0438  647  GLN A OE1 
4653  N NE2 . GLN A 649  ? 0.3903 0.4736 0.2813 0.0323  0.0483  0.0360  647  GLN A NE2 
4654  N N   . ALA A 650  ? 0.3657 0.5232 0.2392 0.0431  0.0561  0.0240  648  ALA A N   
4655  C CA  . ALA A 650  ? 0.3831 0.5565 0.2578 0.0438  0.0599  0.0246  648  ALA A CA  
4656  C C   . ALA A 650  ? 0.4123 0.5869 0.2917 0.0489  0.0604  0.0115  648  ALA A C   
4657  O O   . ALA A 650  ? 0.4053 0.5849 0.2891 0.0492  0.0628  0.0112  648  ALA A O   
4658  C CB  . ALA A 650  ? 0.3910 0.5878 0.2584 0.0441  0.0620  0.0285  648  ALA A CB  
4659  N N   . ARG A 651  ? 0.4046 0.5743 0.2839 0.0529  0.0579  0.0006  649  ARG A N   
4660  C CA  . ARG A 651  ? 0.3709 0.5419 0.2553 0.0581  0.0576  -0.0126 649  ARG A CA  
4661  C C   . ARG A 651  ? 0.3897 0.5386 0.2821 0.0578  0.0551  -0.0158 649  ARG A C   
4662  O O   . ARG A 651  ? 0.3869 0.5339 0.2849 0.0619  0.0540  -0.0264 649  ARG A O   
4663  C CB  . ARG A 651  ? 0.3803 0.5608 0.2608 0.0628  0.0560  -0.0233 649  ARG A CB  
4664  C CG  . ARG A 651  ? 0.4540 0.6453 0.3386 0.0689  0.0566  -0.0370 649  ARG A CG  
4665  C CD  . ARG A 651  ? 0.4940 0.7068 0.3719 0.0730  0.0571  -0.0441 649  ARG A CD  
4666  N NE  . ARG A 651  ? 0.4797 0.6988 0.3630 0.0794  0.0563  -0.0595 649  ARG A NE  
4667  C CZ  . ARG A 651  ? 0.5755 0.8065 0.4630 0.0823  0.0589  -0.0640 649  ARG A CZ  
4668  N NH1 . ARG A 651  ? 0.5337 0.7721 0.4204 0.0791  0.0627  -0.0541 649  ARG A NH1 
4669  N NH2 . ARG A 651  ? 0.5342 0.7697 0.4275 0.0885  0.0574  -0.0790 649  ARG A NH2 
4670  N N   . MET A 652  ? 0.3594 0.4922 0.2529 0.0530  0.0539  -0.0068 650  MET A N   
4671  C CA  . MET A 652  ? 0.3712 0.4839 0.2716 0.0524  0.0513  -0.0093 650  MET A CA  
4672  C C   . MET A 652  ? 0.4182 0.5302 0.3263 0.0548  0.0522  -0.0149 650  MET A C   
4673  O O   . MET A 652  ? 0.4240 0.5265 0.3376 0.0575  0.0496  -0.0232 650  MET A O   
4674  C CB  . MET A 652  ? 0.3645 0.4630 0.2650 0.0469  0.0506  0.0016  650  MET A CB  
4675  C CG  . MET A 652  ? 0.3754 0.4549 0.2827 0.0460  0.0482  -0.0003 650  MET A CG  
4676  S SD  . MET A 652  ? 0.4110 0.4763 0.3188 0.0399  0.0475  0.0116  650  MET A SD  
4677  C CE  . MET A 652  ? 0.3995 0.4601 0.3013 0.0390  0.0448  0.0129  650  MET A CE  
4678  N N   . PRO A 653  ? 0.3927 0.5142 0.3023 0.0540  0.0553  -0.0107 651  PRO A N   
4679  C CA  . PRO A 653  ? 0.3744 0.4945 0.2920 0.0566  0.0557  -0.0164 651  PRO A CA  
4680  C C   . PRO A 653  ? 0.3935 0.5200 0.3141 0.0628  0.0545  -0.0301 651  PRO A C   
4681  O O   . PRO A 653  ? 0.3886 0.5047 0.3170 0.0650  0.0523  -0.0363 651  PRO A O   
4682  C CB  . PRO A 653  ? 0.3574 0.4914 0.2746 0.0550  0.0597  -0.0099 651  PRO A CB  
4683  C CG  . PRO A 653  ? 0.4098 0.5434 0.3211 0.0496  0.0605  0.0022  651  PRO A CG  
4684  C CD  . PRO A 653  ? 0.3697 0.5020 0.2748 0.0503  0.0584  0.0001  651  PRO A CD  
4685  N N   . THR A 654  ? 0.3723 0.5157 0.2874 0.0658  0.0557  -0.0348 652  THR A N   
4686  C CA  . THR A 654  ? 0.3798 0.5298 0.2982 0.0721  0.0541  -0.0489 652  THR A CA  
4687  C C   . THR A 654  ? 0.4162 0.5506 0.3369 0.0731  0.0496  -0.0550 652  THR A C   
4688  O O   . THR A 654  ? 0.3861 0.5147 0.3148 0.0769  0.0470  -0.0649 652  THR A O   
4689  C CB  . THR A 654  ? 0.4279 0.6015 0.3393 0.0749  0.0565  -0.0525 652  THR A CB  
4690  O OG1 . THR A 654  ? 0.4019 0.5907 0.3117 0.0736  0.0608  -0.0461 652  THR A OG1 
4691  C CG2 . THR A 654  ? 0.4309 0.6123 0.3465 0.0819  0.0548  -0.0684 652  THR A CG2 
4692  N N   . LEU A 655  ? 0.3836 0.5111 0.2982 0.0697  0.0484  -0.0490 653  LEU A N   
4693  C CA  . LEU A 655  ? 0.3497 0.4621 0.2666 0.0700  0.0441  -0.0537 653  LEU A CA  
4694  C C   . LEU A 655  ? 0.4087 0.5023 0.3346 0.0686  0.0420  -0.0530 653  LEU A C   
4695  O O   . LEU A 655  ? 0.3896 0.4739 0.3218 0.0709  0.0384  -0.0609 653  LEU A O   
4696  C CB  . LEU A 655  ? 0.4045 0.5130 0.3136 0.0662  0.0435  -0.0461 653  LEU A CB  
4697  C CG  . LEU A 655  ? 0.3943 0.5212 0.2941 0.0672  0.0452  -0.0455 653  LEU A CG  
4698  C CD1 . LEU A 655  ? 0.3622 0.4833 0.2554 0.0635  0.0438  -0.0382 653  LEU A CD1 
4699  C CD2 . LEU A 655  ? 0.4087 0.5476 0.3092 0.0732  0.0440  -0.0592 653  LEU A CD2 
4700  N N   . LEU A 656  ? 0.3812 0.4694 0.3082 0.0647  0.0439  -0.0436 654  LEU A N   
4701  C CA  . LEU A 656  ? 0.3861 0.4579 0.3213 0.0632  0.0419  -0.0422 654  LEU A CA  
4702  C C   . LEU A 656  ? 0.4196 0.4917 0.3640 0.0680  0.0403  -0.0525 654  LEU A C   
4703  O O   . LEU A 656  ? 0.3892 0.4482 0.3405 0.0687  0.0366  -0.0566 654  LEU A O   
4704  C CB  . LEU A 656  ? 0.4013 0.4709 0.3365 0.0591  0.0445  -0.0319 654  LEU A CB  
4705  C CG  . LEU A 656  ? 0.3727 0.4400 0.3008 0.0540  0.0457  -0.0209 654  LEU A CG  
4706  C CD1 . LEU A 656  ? 0.3395 0.4030 0.2701 0.0504  0.0474  -0.0124 654  LEU A CD1 
4707  C CD2 . LEU A 656  ? 0.3597 0.4134 0.2867 0.0522  0.0425  -0.0203 654  LEU A CD2 
4708  N N   . GLY A 657  ? 0.3674 0.4547 0.3126 0.0713  0.0428  -0.0565 655  GLY A N   
4709  C CA  . GLY A 657  ? 0.4067 0.4953 0.3617 0.0762  0.0413  -0.0664 655  GLY A CA  
4710  C C   . GLY A 657  ? 0.3688 0.4552 0.3275 0.0805  0.0374  -0.0781 655  GLY A C   
4711  O O   . GLY A 657  ? 0.3567 0.4336 0.3255 0.0828  0.0339  -0.0842 655  GLY A O   
4712  N N   . LEU A 658  ? 0.3773 0.4725 0.3285 0.0815  0.0376  -0.0811 656  LEU A N   
4713  C CA  . LEU A 658  ? 0.3827 0.4757 0.3376 0.0852  0.0335  -0.0923 656  LEU A CA  
4714  C C   . LEU A 658  ? 0.3620 0.4342 0.3212 0.0822  0.0295  -0.0898 656  LEU A C   
4715  O O   . LEU A 658  ? 0.3703 0.4340 0.3392 0.0848  0.0254  -0.0977 656  LEU A O   
4716  C CB  . LEU A 658  ? 0.3713 0.4792 0.3164 0.0867  0.0347  -0.0954 656  LEU A CB  
4717  C CG  . LEU A 658  ? 0.3513 0.4592 0.2993 0.0908  0.0306  -0.1077 656  LEU A CG  
4718  C CD1 . LEU A 658  ? 0.3709 0.4820 0.3301 0.0968  0.0283  -0.1208 656  LEU A CD1 
4719  C CD2 . LEU A 658  ? 0.3494 0.4747 0.2866 0.0920  0.0323  -0.1097 656  LEU A CD2 
4720  N N   . ILE A 659  ? 0.3775 0.4416 0.3304 0.0767  0.0304  -0.0788 657  ILE A N   
4721  C CA  . ILE A 659  ? 0.3604 0.4063 0.3169 0.0736  0.0268  -0.0761 657  ILE A CA  
4722  C C   . ILE A 659  ? 0.3847 0.4184 0.3519 0.0731  0.0250  -0.0752 657  ILE A C   
4723  O O   . ILE A 659  ? 0.3436 0.3655 0.3185 0.0733  0.0208  -0.0788 657  ILE A O   
4724  C CB  . ILE A 659  ? 0.3698 0.4109 0.3176 0.0680  0.0285  -0.0646 657  ILE A CB  
4725  C CG1 . ILE A 659  ? 0.3835 0.4362 0.3215 0.0687  0.0296  -0.0655 657  ILE A CG1 
4726  C CG2 . ILE A 659  ? 0.3755 0.3990 0.3272 0.0647  0.0252  -0.0612 657  ILE A CG2 
4727  C CD1 . ILE A 659  ? 0.3841 0.4320 0.3144 0.0637  0.0306  -0.0550 657  ILE A CD1 
4728  N N   . ILE A 660  ? 0.3477 0.3844 0.3157 0.0722  0.0278  -0.0700 658  ILE A N   
4729  C CA  . ILE A 660  ? 0.3476 0.3740 0.3255 0.0719  0.0261  -0.0687 658  ILE A CA  
4730  C C   . ILE A 660  ? 0.3843 0.4099 0.3733 0.0771  0.0224  -0.0803 658  ILE A C   
4731  O O   . ILE A 660  ? 0.4062 0.4186 0.4041 0.0766  0.0184  -0.0812 658  ILE A O   
4732  C CB  . ILE A 660  ? 0.3815 0.4142 0.3584 0.0708  0.0300  -0.0625 658  ILE A CB  
4733  C CG1 . ILE A 660  ? 0.3812 0.4108 0.3499 0.0650  0.0326  -0.0505 658  ILE A CG1 
4734  C CG2 . ILE A 660  ? 0.3492 0.3743 0.3375 0.0718  0.0280  -0.0634 658  ILE A CG2 
4735  C CD1 . ILE A 660  ? 0.4186 0.4570 0.3852 0.0639  0.0367  -0.0446 658  ILE A CD1 
4736  N N   . ARG A 661  ? 0.3594 0.3996 0.3484 0.0822  0.0234  -0.0895 659  ARG A N   
4737  C CA  . ARG A 661  ? 0.4004 0.4405 0.4012 0.0877  0.0198  -0.1011 659  ARG A CA  
4738  C C   . ARG A 661  ? 0.4041 0.4392 0.4083 0.0896  0.0152  -0.1097 659  ARG A C   
4739  O O   . ARG A 661  ? 0.3913 0.4178 0.4078 0.0920  0.0106  -0.1160 659  ARG A O   
4740  C CB  . ARG A 661  ? 0.4123 0.4708 0.4129 0.0929  0.0226  -0.1085 659  ARG A CB  
4741  C CG  . ARG A 661  ? 0.3927 0.4545 0.3947 0.0919  0.0259  -0.1021 659  ARG A CG  
4742  C CD  . ARG A 661  ? 0.4489 0.5314 0.4492 0.0965  0.0294  -0.1082 659  ARG A CD  
4743  N NE  . ARG A 661  ? 0.4190 0.5073 0.4287 0.1034  0.0263  -0.1230 659  ARG A NE  
4744  C CZ  . ARG A 661  ? 0.4035 0.5079 0.4097 0.1080  0.0271  -0.1329 659  ARG A CZ  
4745  N NH1 . ARG A 661  ? 0.4207 0.5379 0.4139 0.1063  0.0310  -0.1293 659  ARG A NH1 
4746  N NH2 . ARG A 661  ? 0.4560 0.5644 0.4724 0.1145  0.0237  -0.1470 659  ARG A NH2 
4747  N N   . GLU A 662  ? 0.3414 0.3816 0.3359 0.0886  0.0161  -0.1098 660  GLU A N   
4748  C CA  . GLU A 662  ? 0.4038 0.4405 0.4018 0.0907  0.0117  -0.1187 660  GLU A CA  
4749  C C   . GLU A 662  ? 0.3531 0.3716 0.3544 0.0860  0.0083  -0.1126 660  GLU A C   
4750  O O   . GLU A 662  ? 0.3786 0.3882 0.3900 0.0874  0.0033  -0.1191 660  GLU A O   
4751  C CB  . GLU A 662  ? 0.4311 0.4821 0.4178 0.0920  0.0137  -0.1222 660  GLU A CB  
4752  C CG  . GLU A 662  ? 0.4154 0.4630 0.4053 0.0939  0.0090  -0.1314 660  GLU A CG  
4753  C CD  . GLU A 662  ? 0.4451 0.5080 0.4241 0.0956  0.0106  -0.1356 660  GLU A CD  
4754  O OE1 . GLU A 662  ? 0.4754 0.5447 0.4424 0.0925  0.0147  -0.1265 660  GLU A OE1 
4755  O OE2 . GLU A 662  ? 0.4254 0.4938 0.4082 0.1001  0.0075  -0.1480 660  GLU A OE2 
4756  N N   . ALA A 663  ? 0.3734 0.3864 0.3669 0.0804  0.0109  -0.1004 661  ALA A N   
4757  C CA  . ALA A 663  ? 0.3590 0.3570 0.3540 0.0758  0.0082  -0.0945 661  ALA A CA  
4758  C C   . ALA A 663  ? 0.3771 0.3629 0.3790 0.0725  0.0074  -0.0865 661  ALA A C   
4759  O O   . ALA A 663  ? 0.3864 0.3601 0.3908 0.0687  0.0050  -0.0815 661  ALA A O   
4760  C CB  . ALA A 663  ? 0.3627 0.3626 0.3449 0.0719  0.0108  -0.0870 661  ALA A CB  
4761  N N   . GLY A 664  ? 0.3686 0.3578 0.3735 0.0738  0.0093  -0.0853 662  GLY A N   
4762  C CA  . GLY A 664  ? 0.3728 0.3515 0.3843 0.0710  0.0085  -0.0780 662  GLY A CA  
4763  C C   . GLY A 664  ? 0.3578 0.3328 0.3613 0.0653  0.0115  -0.0656 662  GLY A C   
4764  O O   . GLY A 664  ? 0.4088 0.3735 0.4171 0.0621  0.0101  -0.0591 662  GLY A O   
4765  N N   . LYS A 665  ? 0.3708 0.3541 0.3627 0.0641  0.0155  -0.0622 663  LYS A N   
4766  C CA  . LYS A 665  ? 0.3671 0.3468 0.3514 0.0589  0.0180  -0.0514 663  LYS A CA  
4767  C C   . LYS A 665  ? 0.3566 0.3403 0.3402 0.0580  0.0213  -0.0456 663  LYS A C   
4768  O O   . LYS A 665  ? 0.3521 0.3454 0.3370 0.0614  0.0230  -0.0496 663  LYS A O   
4769  C CB  . LYS A 665  ? 0.3973 0.3837 0.3704 0.0579  0.0202  -0.0500 663  LYS A CB  
4770  C CG  . LYS A 665  ? 0.4517 0.4348 0.4246 0.0585  0.0171  -0.0550 663  LYS A CG  
4771  C CD  . LYS A 665  ? 0.4182 0.4000 0.3818 0.0547  0.0184  -0.0484 663  LYS A CD  
4772  C CE  . LYS A 665  ? 0.4362 0.4148 0.3999 0.0551  0.0153  -0.0532 663  LYS A CE  
4773  N NZ  . LYS A 665  ? 0.4831 0.4587 0.4392 0.0512  0.0161  -0.0462 663  LYS A NZ  
4774  N N   . SER A 666  ? 0.3777 0.3544 0.3592 0.0533  0.0221  -0.0364 664  SER A N   
4775  C CA  . SER A 666  ? 0.3613 0.3422 0.3406 0.0518  0.0254  -0.0302 664  SER A CA  
4776  C C   . SER A 666  ? 0.4028 0.3941 0.3721 0.0513  0.0291  -0.0277 664  SER A C   
4777  O O   . SER A 666  ? 0.3865 0.3796 0.3497 0.0509  0.0291  -0.0285 664  SER A O   
4778  C CB  . SER A 666  ? 0.4054 0.3766 0.3854 0.0471  0.0249  -0.0216 664  SER A CB  
4779  O OG  . SER A 666  ? 0.3969 0.3654 0.3694 0.0438  0.0254  -0.0172 664  SER A OG  
4780  N N   . ALA A 667  ? 0.3619 0.3605 0.3301 0.0510  0.0322  -0.0243 665  ALA A N   
4781  C CA  . ALA A 667  ? 0.3934 0.4024 0.3531 0.0501  0.0357  -0.0206 665  ALA A CA  
4782  C C   . ALA A 667  ? 0.3785 0.3817 0.3318 0.0455  0.0359  -0.0130 665  ALA A C   
4783  O O   . ALA A 667  ? 0.3880 0.3969 0.3342 0.0450  0.0371  -0.0118 665  ALA A O   
4784  C CB  . ALA A 667  ? 0.3623 0.3789 0.3236 0.0500  0.0387  -0.0174 665  ALA A CB  
4785  N N   . LEU A 668  ? 0.3594 0.3518 0.3154 0.0421  0.0347  -0.0079 666  LEU A N   
4786  C CA  . LEU A 668  ? 0.3830 0.3691 0.3340 0.0382  0.0344  -0.0018 666  LEU A CA  
4787  C C   . LEU A 668  ? 0.3977 0.3818 0.3453 0.0389  0.0326  -0.0053 666  LEU A C   
4788  O O   . LEU A 668  ? 0.3817 0.3685 0.3228 0.0375  0.0334  -0.0023 666  LEU A O   
4789  C CB  . LEU A 668  ? 0.4541 0.4296 0.4097 0.0353  0.0327  0.0021  666  LEU A CB  
4790  C CG  . LEU A 668  ? 0.4774 0.4486 0.4291 0.0311  0.0332  0.0094  666  LEU A CG  
4791  C CD1 . LEU A 668  ? 0.4887 0.4680 0.4361 0.0301  0.0361  0.0136  666  LEU A CD1 
4792  C CD2 . LEU A 668  ? 0.5405 0.5047 0.4972 0.0288  0.0321  0.0127  666  LEU A CD2 
4793  N N   . ASN A 669  ? 0.4083 0.3877 0.3608 0.0409  0.0298  -0.0114 667  ASN A N   
4794  C CA  . ASN A 669  ? 0.3684 0.3457 0.3184 0.0415  0.0278  -0.0150 667  ASN A CA  
4795  C C   . ASN A 669  ? 0.3728 0.3614 0.3179 0.0447  0.0290  -0.0199 667  ASN A C   
4796  O O   . ASN A 669  ? 0.3927 0.3821 0.3327 0.0444  0.0282  -0.0205 667  ASN A O   
4797  C CB  . ASN A 669  ? 0.3790 0.3483 0.3367 0.0427  0.0242  -0.0202 667  ASN A CB  
4798  C CG  . ASN A 669  ? 0.4222 0.3810 0.3842 0.0392  0.0227  -0.0148 667  ASN A CG  
4799  O OD1 . ASN A 669  ? 0.4685 0.4223 0.4385 0.0398  0.0206  -0.0166 667  ASN A OD1 
4800  N ND2 . ASN A 669  ? 0.4245 0.3805 0.3817 0.0355  0.0237  -0.0082 667  ASN A ND2 
4801  N N   . ALA A 670  ? 0.3123 0.3104 0.2587 0.0478  0.0307  -0.0236 668  ALA A N   
4802  C CA  . ALA A 670  ? 0.3426 0.3538 0.2838 0.0508  0.0321  -0.0280 668  ALA A CA  
4803  C C   . ALA A 670  ? 0.3572 0.3749 0.2897 0.0481  0.0347  -0.0205 668  ALA A C   
4804  O O   . ALA A 670  ? 0.3307 0.3547 0.2572 0.0489  0.0348  -0.0217 668  ALA A O   
4805  C CB  . ALA A 670  ? 0.4026 0.4237 0.3477 0.0548  0.0334  -0.0339 668  ALA A CB  
4806  N N   . ILE A 671  ? 0.3350 0.3513 0.2672 0.0450  0.0367  -0.0124 669  ILE A N   
4807  C CA  . ILE A 671  ? 0.3348 0.3553 0.2601 0.0419  0.0386  -0.0044 669  ILE A CA  
4808  C C   . ILE A 671  ? 0.3670 0.3802 0.2887 0.0399  0.0365  -0.0022 669  ILE A C   
4809  O O   . ILE A 671  ? 0.3269 0.3464 0.2424 0.0396  0.0370  -0.0001 669  ILE A O   
4810  C CB  . ILE A 671  ? 0.3822 0.3998 0.3097 0.0386  0.0403  0.0034  669  ILE A CB  
4811  C CG1 . ILE A 671  ? 0.3815 0.4088 0.3121 0.0406  0.0427  0.0018  669  ILE A CG1 
4812  C CG2 . ILE A 671  ? 0.3696 0.3885 0.2917 0.0350  0.0412  0.0120  669  ILE A CG2 
4813  C CD1 . ILE A 671  ? 0.4115 0.4337 0.3466 0.0379  0.0435  0.0072  669  ILE A CD1 
4814  N N   . ALA A 672  ? 0.3715 0.3719 0.2970 0.0384  0.0342  -0.0024 670  ALA A N   
4815  C CA  . ALA A 672  ? 0.3865 0.3802 0.3092 0.0366  0.0322  -0.0006 670  ALA A CA  
4816  C C   . ALA A 672  ? 0.3647 0.3630 0.2844 0.0394  0.0307  -0.0071 670  ALA A C   
4817  O O   . ALA A 672  ? 0.3803 0.3797 0.2948 0.0385  0.0301  -0.0049 670  ALA A O   
4818  C CB  . ALA A 672  ? 0.3865 0.3673 0.3144 0.0347  0.0300  -0.0003 670  ALA A CB  
4819  N N   . GLU A 673  ? 0.3325 0.3340 0.2559 0.0430  0.0300  -0.0153 671  GLU A N   
4820  C CA  . GLU A 673  ? 0.3403 0.3469 0.2614 0.0460  0.0284  -0.0224 671  GLU A CA  
4821  C C   . GLU A 673  ? 0.3848 0.4058 0.2982 0.0472  0.0305  -0.0214 671  GLU A C   
4822  O O   . GLU A 673  ? 0.3435 0.3679 0.2521 0.0478  0.0294  -0.0228 671  GLU A O   
4823  C CB  . GLU A 673  ? 0.3375 0.3444 0.2654 0.0497  0.0268  -0.0321 671  GLU A CB  
4824  C CG  . GLU A 673  ? 0.3999 0.4153 0.3252 0.0534  0.0254  -0.0405 671  GLU A CG  
4825  C CD  . GLU A 673  ? 0.4455 0.4545 0.3786 0.0558  0.0217  -0.0495 671  GLU A CD  
4826  O OE1 . GLU A 673  ? 0.4866 0.4888 0.4278 0.0560  0.0208  -0.0507 671  GLU A OE1 
4827  O OE2 . GLU A 673  ? 0.4137 0.4247 0.3454 0.0574  0.0195  -0.0552 671  GLU A OE2 
4828  N N   . VAL A 674  ? 0.3492 0.3797 0.2615 0.0476  0.0336  -0.0188 672  VAL A N   
4829  C CA  . VAL A 674  ? 0.3322 0.3775 0.2372 0.0484  0.0357  -0.0167 672  VAL A CA  
4830  C C   . VAL A 674  ? 0.3249 0.3676 0.2246 0.0444  0.0358  -0.0068 672  VAL A C   
4831  O O   . VAL A 674  ? 0.3216 0.3724 0.2151 0.0447  0.0357  -0.0054 672  VAL A O   
4832  C CB  . VAL A 674  ? 0.3628 0.4201 0.2684 0.0496  0.0390  -0.0160 672  VAL A CB  
4833  C CG1 . VAL A 674  ? 0.3242 0.3986 0.2220 0.0500  0.0413  -0.0128 672  VAL A CG1 
4834  C CG2 . VAL A 674  ? 0.3145 0.3745 0.2261 0.0541  0.0384  -0.0267 672  VAL A CG2 
4835  N N   . ARG A 675  ? 0.3010 0.3326 0.2036 0.0408  0.0357  -0.0001 673  ARG A N   
4836  C CA  . ARG A 675  ? 0.3334 0.3607 0.2326 0.0373  0.0351  0.0083  673  ARG A CA  
4837  C C   . ARG A 675  ? 0.3309 0.3537 0.2277 0.0377  0.0323  0.0055  673  ARG A C   
4838  O O   . ARG A 675  ? 0.3239 0.3507 0.2155 0.0368  0.0318  0.0099  673  ARG A O   
4839  C CB  . ARG A 675  ? 0.2863 0.3018 0.1900 0.0338  0.0350  0.0138  673  ARG A CB  
4840  C CG  . ARG A 675  ? 0.3212 0.3413 0.2267 0.0324  0.0377  0.0190  673  ARG A CG  
4841  C CD  . ARG A 675  ? 0.3881 0.3967 0.2972 0.0286  0.0370  0.0250  673  ARG A CD  
4842  N NE  . ARG A 675  ? 0.3564 0.3631 0.2626 0.0260  0.0360  0.0318  673  ARG A NE  
4843  C CZ  . ARG A 675  ? 0.3771 0.3737 0.2858 0.0232  0.0345  0.0360  673  ARG A CZ  
4844  N NH1 . ARG A 675  ? 0.3403 0.3281 0.2538 0.0223  0.0340  0.0344  673  ARG A NH1 
4845  N NH2 . ARG A 675  ? 0.3251 0.3207 0.2317 0.0212  0.0333  0.0418  673  ARG A NH2 
4846  N N   . GLU A 676  ? 0.3457 0.3600 0.2466 0.0389  0.0301  -0.0012 674  GLU A N   
4847  C CA  . GLU A 676  ? 0.3406 0.3505 0.2401 0.0393  0.0273  -0.0043 674  GLU A CA  
4848  C C   . GLU A 676  ? 0.3468 0.3691 0.2407 0.0421  0.0271  -0.0084 674  GLU A C   
4849  O O   . GLU A 676  ? 0.3386 0.3619 0.2282 0.0416  0.0256  -0.0064 674  GLU A O   
4850  C CB  . GLU A 676  ? 0.3566 0.3568 0.2625 0.0402  0.0251  -0.0110 674  GLU A CB  
4851  C CG  . GLU A 676  ? 0.4704 0.4636 0.3765 0.0395  0.0221  -0.0129 674  GLU A CG  
4852  C CD  . GLU A 676  ? 0.5881 0.5707 0.5016 0.0391  0.0200  -0.0171 674  GLU A CD  
4853  O OE1 . GLU A 676  ? 0.6648 0.6441 0.5833 0.0389  0.0208  -0.0169 674  GLU A OE1 
4854  O OE2 . GLU A 676  ? 0.5888 0.5668 0.5035 0.0390  0.0174  -0.0201 674  GLU A OE2 
4855  N N   . ALA A 677  ? 0.3589 0.3916 0.2528 0.0454  0.0285  -0.0142 675  ALA A N   
4856  C CA  . ALA A 677  ? 0.3167 0.3628 0.2050 0.0483  0.0283  -0.0187 675  ALA A CA  
4857  C C   . ALA A 677  ? 0.3167 0.3727 0.1978 0.0466  0.0299  -0.0099 675  ALA A C   
4858  O O   . ALA A 677  ? 0.3517 0.4132 0.2275 0.0471  0.0286  -0.0096 675  ALA A O   
4859  C CB  . ALA A 677  ? 0.2967 0.3528 0.1872 0.0524  0.0294  -0.0275 675  ALA A CB  
4860  N N   . ILE A 678  ? 0.3144 0.3725 0.1956 0.0443  0.0326  -0.0022 676  ILE A N   
4861  C CA  . ILE A 678  ? 0.3291 0.3950 0.2050 0.0419  0.0338  0.0077  676  ILE A CA  
4862  C C   . ILE A 678  ? 0.3419 0.3976 0.2167 0.0392  0.0312  0.0133  676  ILE A C   
4863  O O   . ILE A 678  ? 0.2896 0.3521 0.1591 0.0386  0.0305  0.0181  676  ILE A O   
4864  C CB  . ILE A 678  ? 0.3035 0.3710 0.1816 0.0395  0.0366  0.0149  676  ILE A CB  
4865  C CG1 . ILE A 678  ? 0.3541 0.4350 0.2324 0.0425  0.0394  0.0098  676  ILE A CG1 
4866  C CG2 . ILE A 678  ? 0.3314 0.4030 0.2059 0.0361  0.0371  0.0266  676  ILE A CG2 
4867  C CD1 . ILE A 678  ? 0.3481 0.4260 0.2317 0.0407  0.0417  0.0135  676  ILE A CD1 
4868  N N   . ASP A 679  ? 0.3125 0.3525 0.1924 0.0375  0.0297  0.0134  677  ASP A N   
4869  C CA  . ASP A 679  ? 0.3326 0.3631 0.2124 0.0351  0.0272  0.0182  677  ASP A CA  
4870  C C   . ASP A 679  ? 0.3581 0.3903 0.2347 0.0371  0.0247  0.0131  677  ASP A C   
4871  O O   . ASP A 679  ? 0.3255 0.3590 0.1986 0.0360  0.0232  0.0182  677  ASP A O   
4872  C CB  . ASP A 679  ? 0.3503 0.3654 0.2365 0.0331  0.0264  0.0182  677  ASP A CB  
4873  C CG  . ASP A 679  ? 0.4039 0.4163 0.2933 0.0305  0.0284  0.0246  677  ASP A CG  
4874  O OD1 . ASP A 679  ? 0.3815 0.4011 0.2685 0.0292  0.0298  0.0315  677  ASP A OD1 
4875  O OD2 . ASP A 679  ? 0.4173 0.4204 0.3119 0.0297  0.0284  0.0230  677  ASP A OD2 
4876  N N   . PHE A 680  ? 0.3300 0.3623 0.2080 0.0400  0.0238  0.0032  678  PHE A N   
4877  C CA  . PHE A 680  ? 0.3091 0.3444 0.1843 0.0420  0.0213  -0.0025 678  PHE A CA  
4878  C C   . PHE A 680  ? 0.3523 0.4029 0.2200 0.0432  0.0218  0.0003  678  PHE A C   
4879  O O   . PHE A 680  ? 0.3289 0.3807 0.1931 0.0429  0.0197  0.0025  678  PHE A O   
4880  C CB  . PHE A 680  ? 0.3117 0.3471 0.1904 0.0453  0.0204  -0.0139 678  PHE A CB  
4881  C CG  . PHE A 680  ? 0.3376 0.3582 0.2232 0.0443  0.0183  -0.0174 678  PHE A CG  
4882  C CD1 . PHE A 680  ? 0.3275 0.3398 0.2134 0.0425  0.0158  -0.0156 678  PHE A CD1 
4883  C CD2 . PHE A 680  ? 0.3497 0.3657 0.2415 0.0452  0.0187  -0.0226 678  PHE A CD2 
4884  C CE1 . PHE A 680  ? 0.3567 0.3569 0.2490 0.0414  0.0140  -0.0185 678  PHE A CE1 
4885  C CE2 . PHE A 680  ? 0.3639 0.3671 0.2624 0.0440  0.0166  -0.0250 678  PHE A CE2 
4886  C CZ  . PHE A 680  ? 0.3838 0.3796 0.2823 0.0420  0.0144  -0.0229 678  PHE A CZ  
4887  N N   . LEU A 681  ? 0.3493 0.4126 0.2146 0.0445  0.0245  0.0002  679  LEU A N   
4888  C CA  . LEU A 681  ? 0.3444 0.4247 0.2024 0.0456  0.0252  0.0029  679  LEU A CA  
4889  C C   . LEU A 681  ? 0.3782 0.4576 0.2333 0.0421  0.0247  0.0152  679  LEU A C   
4890  O O   . LEU A 681  ? 0.3343 0.4202 0.1845 0.0424  0.0230  0.0175  679  LEU A O   
4891  C CB  . LEU A 681  ? 0.3033 0.3977 0.1600 0.0472  0.0287  0.0017  679  LEU A CB  
4892  C CG  . LEU A 681  ? 0.3915 0.4905 0.2506 0.0515  0.0290  -0.0113 679  LEU A CG  
4893  C CD1 . LEU A 681  ? 0.3266 0.4352 0.1870 0.0524  0.0326  -0.0115 679  LEU A CD1 
4894  C CD2 . LEU A 681  ? 0.3512 0.4630 0.2050 0.0550  0.0273  -0.0187 679  LEU A CD2 
4895  N N   . ARG A 682  ? 0.3339 0.4049 0.1929 0.0388  0.0258  0.0229  680  ARG A N   
4896  C CA  . ARG A 682  ? 0.3544 0.4243 0.2121 0.0356  0.0250  0.0346  680  ARG A CA  
4897  C C   . ARG A 682  ? 0.3573 0.4149 0.2166 0.0346  0.0214  0.0353  680  ARG A C   
4898  O O   . ARG A 682  ? 0.3458 0.4059 0.2024 0.0335  0.0196  0.0421  680  ARG A O   
4899  C CB  . ARG A 682  ? 0.2953 0.3603 0.1574 0.0324  0.0269  0.0421  680  ARG A CB  
4900  C CG  . ARG A 682  ? 0.3428 0.4229 0.2025 0.0326  0.0303  0.0449  680  ARG A CG  
4901  C CD  . ARG A 682  ? 0.3746 0.4488 0.2397 0.0296  0.0322  0.0509  680  ARG A CD  
4902  N NE  . ARG A 682  ? 0.3308 0.4201 0.1941 0.0296  0.0355  0.0537  680  ARG A NE  
4903  C CZ  . ARG A 682  ? 0.3889 0.4766 0.2566 0.0277  0.0377  0.0570  680  ARG A CZ  
4904  N NH1 . ARG A 682  ? 0.3459 0.4178 0.2199 0.0258  0.0369  0.0576  680  ARG A NH1 
4905  N NH2 . ARG A 682  ? 0.3938 0.4969 0.2597 0.0279  0.0409  0.0594  680  ARG A NH2 
4906  N N   . TYR A 683  ? 0.3629 0.4077 0.2268 0.0351  0.0203  0.0286  681  TYR A N   
4907  C CA  . TYR A 683  ? 0.3590 0.3930 0.2247 0.0343  0.0171  0.0285  681  TYR A CA  
4908  C C   . TYR A 683  ? 0.3593 0.4007 0.2201 0.0366  0.0148  0.0249  681  TYR A C   
4909  O O   . TYR A 683  ? 0.3412 0.3813 0.2007 0.0357  0.0124  0.0299  681  TYR A O   
4910  C CB  . TYR A 683  ? 0.3485 0.3695 0.2202 0.0343  0.0166  0.0220  681  TYR A CB  
4911  C CG  . TYR A 683  ? 0.3588 0.3700 0.2325 0.0336  0.0135  0.0213  681  TYR A CG  
4912  C CD1 . TYR A 683  ? 0.3518 0.3548 0.2282 0.0311  0.0123  0.0282  681  TYR A CD1 
4913  C CD2 . TYR A 683  ? 0.3465 0.3573 0.2199 0.0357  0.0115  0.0133  681  TYR A CD2 
4914  C CE1 . TYR A 683  ? 0.3226 0.3176 0.2012 0.0307  0.0095  0.0272  681  TYR A CE1 
4915  C CE2 . TYR A 683  ? 0.3406 0.3435 0.2161 0.0350  0.0088  0.0128  681  TYR A CE2 
4916  C CZ  . TYR A 683  ? 0.3643 0.3595 0.2423 0.0326  0.0079  0.0196  681  TYR A CZ  
4917  O OH  . TYR A 683  ? 0.3351 0.3233 0.2155 0.0322  0.0052  0.0186  681  TYR A OH  
4918  N N   . TYR A 684  ? 0.3212 0.3705 0.1798 0.0397  0.0152  0.0158  682  TYR A N   
4919  C CA  . TYR A 684  ? 0.3511 0.4073 0.2052 0.0419  0.0128  0.0115  682  TYR A CA  
4920  C C   . TYR A 684  ? 0.3948 0.4657 0.2422 0.0419  0.0129  0.0187  682  TYR A C   
4921  O O   . TYR A 684  ? 0.3663 0.4411 0.2102 0.0426  0.0103  0.0194  682  TYR A O   
4922  C CB  . TYR A 684  ? 0.3436 0.4049 0.1980 0.0454  0.0128  -0.0007 682  TYR A CB  
4923  C CG  . TYR A 684  ? 0.3480 0.3949 0.2096 0.0453  0.0118  -0.0075 682  TYR A CG  
4924  C CD1 . TYR A 684  ? 0.3407 0.3749 0.2058 0.0433  0.0095  -0.0055 682  TYR A CD1 
4925  C CD2 . TYR A 684  ? 0.2981 0.3449 0.1634 0.0471  0.0129  -0.0154 682  TYR A CD2 
4926  C CE1 . TYR A 684  ? 0.3442 0.3664 0.2160 0.0428  0.0086  -0.0108 682  TYR A CE1 
4927  C CE2 . TYR A 684  ? 0.3030 0.3371 0.1753 0.0467  0.0117  -0.0205 682  TYR A CE2 
4928  C CZ  . TYR A 684  ? 0.3646 0.3867 0.2400 0.0444  0.0097  -0.0178 682  TYR A CZ  
4929  O OH  . TYR A 684  ? 0.3355 0.3461 0.2179 0.0436  0.0086  -0.0221 682  TYR A OH  
4930  N N   . ALA A 685  ? 0.3509 0.4307 0.1964 0.0410  0.0159  0.0244  683  ALA A N   
4931  C CA  . ALA A 685  ? 0.3513 0.4447 0.1909 0.0402  0.0160  0.0334  683  ALA A CA  
4932  C C   . ALA A 685  ? 0.3519 0.4368 0.1933 0.0372  0.0134  0.0438  683  ALA A C   
4933  O O   . ALA A 685  ? 0.3299 0.4213 0.1673 0.0374  0.0110  0.0479  683  ALA A O   
4934  C CB  . ALA A 685  ? 0.3568 0.4609 0.1953 0.0393  0.0197  0.0383  683  ALA A CB  
4935  N N   . GLU A 686  ? 0.3707 0.4412 0.2185 0.0345  0.0135  0.0479  684  GLU A N   
4936  C CA  . GLU A 686  ? 0.3879 0.4497 0.2386 0.0319  0.0108  0.0568  684  GLU A CA  
4937  C C   . GLU A 686  ? 0.3595 0.4148 0.2104 0.0333  0.0072  0.0524  684  GLU A C   
4938  O O   . GLU A 686  ? 0.3572 0.4139 0.2069 0.0327  0.0043  0.0587  684  GLU A O   
4939  C CB  . GLU A 686  ? 0.4126 0.4605 0.2705 0.0292  0.0115  0.0603  684  GLU A CB  
4940  C CG  . GLU A 686  ? 0.4903 0.5272 0.3529 0.0270  0.0082  0.0675  684  GLU A CG  
4941  C CD  . GLU A 686  ? 0.5106 0.5551 0.3718 0.0251  0.0067  0.0795  684  GLU A CD  
4942  O OE1 . GLU A 686  ? 0.5433 0.6019 0.3999 0.0249  0.0087  0.0838  684  GLU A OE1 
4943  O OE2 . GLU A 686  ? 0.4966 0.5331 0.3617 0.0238  0.0033  0.0849  684  GLU A OE2 
4944  N N   . GLN A 687  ? 0.3499 0.3983 0.2028 0.0350  0.0070  0.0419  685  GLN A N   
4945  C CA  . GLN A 687  ? 0.3450 0.3879 0.1985 0.0361  0.0036  0.0375  685  GLN A CA  
4946  C C   . GLN A 687  ? 0.3378 0.3943 0.1846 0.0382  0.0020  0.0367  685  GLN A C   
4947  O O   . GLN A 687  ? 0.3158 0.3707 0.1622 0.0384  -0.0013 0.0389  685  GLN A O   
4948  C CB  . GLN A 687  ? 0.3502 0.3847 0.2075 0.0373  0.0039  0.0267  685  GLN A CB  
4949  C CG  . GLN A 687  ? 0.3473 0.3682 0.2113 0.0352  0.0050  0.0278  685  GLN A CG  
4950  C CD  . GLN A 687  ? 0.3800 0.3914 0.2477 0.0331  0.0027  0.0341  685  GLN A CD  
4951  O OE1 . GLN A 687  ? 0.3854 0.3934 0.2538 0.0337  -0.0002 0.0321  685  GLN A OE1 
4952  N NE2 . GLN A 687  ? 0.4198 0.4272 0.2904 0.0308  0.0037  0.0415  685  GLN A NE2 
4953  N N   . THR A 688  ? 0.3417 0.4125 0.1832 0.0400  0.0041  0.0339  686  THR A N   
4954  C CA  . THR A 688  ? 0.3445 0.4307 0.1789 0.0420  0.0027  0.0337  686  THR A CA  
4955  C C   . THR A 688  ? 0.3777 0.4693 0.2097 0.0399  0.0012  0.0468  686  THR A C   
4956  O O   . THR A 688  ? 0.3863 0.4821 0.2155 0.0407  -0.0019 0.0487  686  THR A O   
4957  C CB  . THR A 688  ? 0.3698 0.4713 0.1995 0.0443  0.0056  0.0279  686  THR A CB  
4958  O OG1 . THR A 688  ? 0.3476 0.4443 0.1800 0.0467  0.0057  0.0150  686  THR A OG1 
4959  C CG2 . THR A 688  ? 0.3514 0.4717 0.1729 0.0461  0.0045  0.0295  686  THR A CG2 
4960  N N   . ARG A 689  ? 0.3636 0.4555 0.1972 0.0373  0.0033  0.0560  687  ARG A N   
4961  C CA  . ARG A 689  ? 0.3628 0.4592 0.1954 0.0350  0.0016  0.0693  687  ARG A CA  
4962  C C   . ARG A 689  ? 0.3780 0.4603 0.2159 0.0338  -0.0025 0.0731  687  ARG A C   
4963  O O   . ARG A 689  ? 0.3876 0.4739 0.2244 0.0330  -0.0054 0.0818  687  ARG A O   
4964  C CB  . ARG A 689  ? 0.3772 0.4750 0.2121 0.0320  0.0044  0.0783  687  ARG A CB  
4965  C CG  . ARG A 689  ? 0.3912 0.5063 0.2205 0.0331  0.0083  0.0764  687  ARG A CG  
4966  C CD  . ARG A 689  ? 0.3608 0.4790 0.1924 0.0298  0.0106  0.0872  687  ARG A CD  
4967  N NE  . ARG A 689  ? 0.3954 0.4978 0.2344 0.0282  0.0120  0.0853  687  ARG A NE  
4968  C CZ  . ARG A 689  ? 0.4208 0.5242 0.2607 0.0290  0.0156  0.0790  687  ARG A CZ  
4969  N NH1 . ARG A 689  ? 0.4313 0.5505 0.2655 0.0315  0.0183  0.0735  687  ARG A NH1 
4970  N NH2 . ARG A 689  ? 0.4016 0.4903 0.2482 0.0275  0.0164  0.0781  687  ARG A NH2 
4971  N N   . ARG A 690  ? 0.3428 0.4091 0.1866 0.0338  -0.0028 0.0667  688  ARG A N   
4972  C CA  . ARG A 690  ? 0.3992 0.4527 0.2484 0.0331  -0.0065 0.0688  688  ARG A CA  
4973  C C   . ARG A 690  ? 0.4006 0.4563 0.2473 0.0355  -0.0096 0.0631  688  ARG A C   
4974  O O   . ARG A 690  ? 0.3826 0.4322 0.2325 0.0351  -0.0132 0.0670  688  ARG A O   
4975  C CB  . ARG A 690  ? 0.3590 0.3962 0.2155 0.0321  -0.0056 0.0642  688  ARG A CB  
4976  C CG  . ARG A 690  ? 0.3901 0.4221 0.2511 0.0294  -0.0034 0.0704  688  ARG A CG  
4977  C CD  . ARG A 690  ? 0.4609 0.4897 0.3259 0.0271  -0.0062 0.0821  688  ARG A CD  
4978  N NE  . ARG A 690  ? 0.4448 0.4611 0.3158 0.0272  -0.0097 0.0808  688  ARG A NE  
4979  C CZ  . ARG A 690  ? 0.4658 0.4828 0.3370 0.0279  -0.0137 0.0841  688  ARG A CZ  
4980  N NH1 . ARG A 690  ? 0.4158 0.4451 0.2815 0.0283  -0.0149 0.0900  688  ARG A NH1 
4981  N NH2 . ARG A 690  ? 0.4156 0.4214 0.2925 0.0284  -0.0165 0.0814  688  ARG A NH2 
4982  N N   . THR A 691  ? 0.3817 0.4459 0.2233 0.0381  -0.0086 0.0537  689  THR A N   
4983  C CA  . THR A 691  ? 0.3758 0.4384 0.2170 0.0402  -0.0116 0.0464  689  THR A CA  
4984  C C   . THR A 691  ? 0.4541 0.5330 0.2877 0.0427  -0.0127 0.0434  689  THR A C   
4985  O O   . THR A 691  ? 0.4599 0.5409 0.2922 0.0435  -0.0163 0.0446  689  THR A O   
4986  C CB  . THR A 691  ? 0.4251 0.4777 0.2705 0.0410  -0.0105 0.0350  689  THR A CB  
4987  O OG1 . THR A 691  ? 0.4022 0.4611 0.2452 0.0420  -0.0072 0.0289  689  THR A OG1 
4988  C CG2 . THR A 691  ? 0.4189 0.4554 0.2720 0.0387  -0.0102 0.0374  689  THR A CG2 
4989  N N   . LEU A 692  ? 0.4610 0.5519 0.2895 0.0440  -0.0099 0.0390  690  LEU A N   
4990  C CA  . LEU A 692  ? 0.4410 0.5456 0.2635 0.0471  -0.0110 0.0312  690  LEU A CA  
4991  C C   . LEU A 692  ? 0.4771 0.5974 0.2927 0.0474  -0.0128 0.0394  690  LEU A C   
4992  O O   . LEU A 692  ? 0.4108 0.5393 0.2237 0.0458  -0.0112 0.0492  690  LEU A O   
4993  C CB  . LEU A 692  ? 0.4209 0.5331 0.2412 0.0489  -0.0075 0.0224  690  LEU A CB  
4994  C CG  . LEU A 692  ? 0.4362 0.5338 0.2634 0.0491  -0.0065 0.0129  690  LEU A CG  
4995  C CD1 . LEU A 692  ? 0.4135 0.5188 0.2394 0.0513  -0.0038 0.0037  690  LEU A CD1 
4996  C CD2 . LEU A 692  ? 0.4671 0.5562 0.2977 0.0500  -0.0101 0.0059  690  LEU A CD2 
4997  N N   . GLY A 693  ? 0.4083 0.5329 0.2214 0.0493  -0.0164 0.0356  691  GLY A N   
4998  C CA  . GLY A 693  ? 0.4536 0.5944 0.2599 0.0500  -0.0185 0.0421  691  GLY A CA  
4999  C C   . GLY A 693  ? 0.4856 0.6397 0.2861 0.0535  -0.0198 0.0311  691  GLY A C   
5000  O O   . GLY A 693  ? 0.4511 0.6029 0.2532 0.0554  -0.0188 0.0184  691  GLY A O   
5001  N N   . PRO A 694  ? 0.4942 0.6628 0.2885 0.0544  -0.0225 0.0360  692  PRO A N   
5002  C CA  . PRO A 694  ? 0.5028 0.6868 0.2910 0.0579  -0.0238 0.0256  692  PRO A CA  
5003  C C   . PRO A 694  ? 0.5416 0.7155 0.3342 0.0596  -0.0268 0.0138  692  PRO A C   
5004  O O   . PRO A 694  ? 0.5391 0.7206 0.3296 0.0625  -0.0270 0.0013  692  PRO A O   
5005  C CB  . PRO A 694  ? 0.5340 0.7343 0.3153 0.0578  -0.0264 0.0361  692  PRO A CB  
5006  C CG  . PRO A 694  ? 0.4994 0.6976 0.2819 0.0543  -0.0248 0.0516  692  PRO A CG  
5007  C CD  . PRO A 694  ? 0.4595 0.6338 0.2518 0.0521  -0.0239 0.0517  692  PRO A CD  
5008  N N   . GLY A 695  ? 0.4991 0.6565 0.2982 0.0580  -0.0292 0.0172  693  GLY A N   
5009  C CA  . GLY A 695  ? 0.5371 0.6850 0.3409 0.0592  -0.0319 0.0068  693  GLY A CA  
5010  C C   . GLY A 695  ? 0.5249 0.6606 0.3351 0.0592  -0.0297 -0.0038 693  GLY A C   
5011  O O   . GLY A 695  ? 0.5314 0.6596 0.3461 0.0600  -0.0319 -0.0125 693  GLY A O   
5012  N N   . HIS A 696  ? 0.4947 0.6280 0.3057 0.0583  -0.0256 -0.0029 694  HIS A N   
5013  C CA  . HIS A 696  ? 0.4563 0.5780 0.2736 0.0583  -0.0236 -0.0122 694  HIS A CA  
5014  C C   . HIS A 696  ? 0.4876 0.6220 0.3014 0.0611  -0.0219 -0.0225 694  HIS A C   
5015  O O   . HIS A 696  ? 0.5269 0.6635 0.3403 0.0610  -0.0183 -0.0225 694  HIS A O   
5016  C CB  . HIS A 696  ? 0.5020 0.6107 0.3241 0.0553  -0.0205 -0.0049 694  HIS A CB  
5017  C CG  . HIS A 696  ? 0.4643 0.5635 0.2891 0.0529  -0.0221 0.0061  694  HIS A CG  
5018  N ND1 . HIS A 696  ? 0.4653 0.5670 0.2882 0.0510  -0.0210 0.0185  694  HIS A ND1 
5019  C CD2 . HIS A 696  ? 0.4572 0.5451 0.2872 0.0521  -0.0250 0.0064  694  HIS A CD2 
5020  C CE1 . HIS A 696  ? 0.4569 0.5486 0.2840 0.0493  -0.0234 0.0256  694  HIS A CE1 
5021  N NE2 . HIS A 696  ? 0.4691 0.5526 0.3004 0.0501  -0.0257 0.0182  694  HIS A NE2 
5022  N N   . GLY A 697  ? 0.4978 0.6410 0.3095 0.0638  -0.0248 -0.0318 695  GLY A N   
5023  C CA  . GLY A 697  ? 0.4532 0.6103 0.2616 0.0670  -0.0241 -0.0426 695  GLY A CA  
5024  C C   . GLY A 697  ? 0.4440 0.5910 0.2595 0.0674  -0.0222 -0.0519 695  GLY A C   
5025  O O   . GLY A 697  ? 0.4387 0.5685 0.2623 0.0657  -0.0229 -0.0537 695  GLY A O   
5026  N N   . PRO A 698  ? 0.4624 0.6207 0.2754 0.0697  -0.0198 -0.0578 696  PRO A N   
5027  C CA  . PRO A 698  ? 0.4267 0.5762 0.2471 0.0705  -0.0183 -0.0671 696  PRO A CA  
5028  C C   . PRO A 698  ? 0.4339 0.5779 0.2608 0.0722  -0.0222 -0.0803 696  PRO A C   
5029  O O   . PRO A 698  ? 0.4370 0.5892 0.2612 0.0739  -0.0256 -0.0851 696  PRO A O   
5030  C CB  . PRO A 698  ? 0.4643 0.6313 0.2795 0.0733  -0.0155 -0.0709 696  PRO A CB  
5031  C CG  . PRO A 698  ? 0.5056 0.6868 0.3112 0.0723  -0.0141 -0.0587 696  PRO A CG  
5032  C CD  . PRO A 698  ? 0.5071 0.6873 0.3107 0.0716  -0.0181 -0.0554 696  PRO A CD  
5033  N N   . LEU A 699  ? 0.4119 0.5419 0.2479 0.0716  -0.0217 -0.0859 697  LEU A N   
5034  C CA  . LEU A 699  ? 0.4076 0.5321 0.2513 0.0731  -0.0253 -0.0988 697  LEU A CA  
5035  C C   . LEU A 699  ? 0.4104 0.5509 0.2522 0.0777  -0.0264 -0.1116 697  LEU A C   
5036  O O   . LEU A 699  ? 0.4073 0.5519 0.2509 0.0797  -0.0305 -0.1213 697  LEU A O   
5037  C CB  . LEU A 699  ? 0.3948 0.5010 0.2490 0.0710  -0.0245 -0.1003 697  LEU A CB  
5038  C CG  . LEU A 699  ? 0.4309 0.5199 0.2895 0.0667  -0.0244 -0.0911 697  LEU A CG  
5039  C CD1 . LEU A 699  ? 0.4061 0.4803 0.2749 0.0652  -0.0236 -0.0939 697  LEU A CD1 
5040  C CD2 . LEU A 699  ? 0.4512 0.5376 0.3111 0.0659  -0.0284 -0.0920 697  LEU A CD2 
5041  N N   . GLY A 700  ? 0.4055 0.5557 0.2441 0.0795  -0.0230 -0.1123 698  GLY A N   
5042  C CA  . GLY A 700  ? 0.3843 0.5483 0.2229 0.0841  -0.0237 -0.1258 698  GLY A CA  
5043  C C   . GLY A 700  ? 0.3938 0.5517 0.2391 0.0848  -0.0211 -0.1297 698  GLY A C   
5044  O O   . GLY A 700  ? 0.4228 0.5692 0.2701 0.0817  -0.0180 -0.1201 698  GLY A O   
5045  N N   . PRO A 701  ? 0.4218 0.5872 0.2712 0.0890  -0.0226 -0.1439 699  PRO A N   
5046  C CA  . PRO A 701  ? 0.3949 0.5545 0.2518 0.0901  -0.0206 -0.1484 699  PRO A CA  
5047  C C   . PRO A 701  ? 0.4021 0.5375 0.2695 0.0863  -0.0213 -0.1446 699  PRO A C   
5048  O O   . PRO A 701  ? 0.4021 0.5264 0.2761 0.0851  -0.0252 -0.1482 699  PRO A O   
5049  C CB  . PRO A 701  ? 0.4105 0.5802 0.2724 0.0952  -0.0238 -0.1658 699  PRO A CB  
5050  C CG  . PRO A 701  ? 0.4377 0.6246 0.2933 0.0960  -0.0249 -0.1652 699  PRO A CG  
5051  C CD  . PRO A 701  ? 0.4019 0.5836 0.2496 0.0930  -0.0258 -0.1558 699  PRO A CD  
5052  N N   . ILE A 702  ? 0.4047 0.5327 0.2735 0.0843  -0.0174 -0.1369 700  ILE A N   
5053  C CA  . ILE A 702  ? 0.3855 0.4923 0.2636 0.0807  -0.0175 -0.1323 700  ILE A CA  
5054  C C   . ILE A 702  ? 0.3978 0.5010 0.2843 0.0826  -0.0167 -0.1392 700  ILE A C   
5055  O O   . ILE A 702  ? 0.3765 0.4903 0.2590 0.0847  -0.0133 -0.1390 700  ILE A O   
5056  C CB  . ILE A 702  ? 0.3759 0.4756 0.2489 0.0762  -0.0140 -0.1163 700  ILE A CB  
5057  C CG1 . ILE A 702  ? 0.3749 0.4748 0.2424 0.0741  -0.0157 -0.1100 700  ILE A CG1 
5058  C CG2 . ILE A 702  ? 0.3757 0.4568 0.2578 0.0731  -0.0133 -0.1124 700  ILE A CG2 
5059  C CD1 . ILE A 702  ? 0.4339 0.5237 0.2992 0.0696  -0.0135 -0.0958 700  ILE A CD1 
5060  N N   . VAL A 703  ? 0.3605 0.4493 0.2589 0.0820  -0.0200 -0.1451 701  VAL A N   
5061  C CA  . VAL A 703  ? 0.3536 0.4366 0.2617 0.0836  -0.0199 -0.1509 701  VAL A CA  
5062  C C   . VAL A 703  ? 0.3903 0.4587 0.3009 0.0792  -0.0170 -0.1389 701  VAL A C   
5063  O O   . VAL A 703  ? 0.3599 0.4152 0.2730 0.0751  -0.0181 -0.1322 701  VAL A O   
5064  C CB  . VAL A 703  ? 0.3709 0.4460 0.2919 0.0852  -0.0255 -0.1633 701  VAL A CB  
5065  C CG1 . VAL A 703  ? 0.3624 0.4286 0.2947 0.0861  -0.0257 -0.1671 701  VAL A CG1 
5066  C CG2 . VAL A 703  ? 0.3685 0.4594 0.2877 0.0902  -0.0285 -0.1769 701  VAL A CG2 
5067  N N   . CYS A 704  ? 0.3632 0.4348 0.2727 0.0800  -0.0132 -0.1362 702  CYS A N   
5068  C CA  . CYS A 704  ? 0.3859 0.4450 0.2978 0.0762  -0.0104 -0.1255 702  CYS A CA  
5069  C C   . CYS A 704  ? 0.3713 0.4227 0.2950 0.0777  -0.0116 -0.1318 702  CYS A C   
5070  O O   . CYS A 704  ? 0.3439 0.4051 0.2686 0.0817  -0.0106 -0.1389 702  CYS A O   
5071  C CB  . CYS A 704  ? 0.3502 0.4185 0.2520 0.0754  -0.0052 -0.1158 702  CYS A CB  
5072  S SG  . CYS A 704  ? 0.4105 0.4871 0.2995 0.0734  -0.0042 -0.1067 702  CYS A SG  
5073  N N   . ILE A 705  ? 0.3629 0.3975 0.2958 0.0745  -0.0137 -0.1291 703  ILE A N   
5074  C CA  . ILE A 705  ? 0.3829 0.4084 0.3283 0.0754  -0.0155 -0.1341 703  ILE A CA  
5075  C C   . ILE A 705  ? 0.3617 0.3767 0.3078 0.0713  -0.0124 -0.1223 703  ILE A C   
5076  O O   . ILE A 705  ? 0.3447 0.3503 0.2899 0.0669  -0.0123 -0.1136 703  ILE A O   
5077  C CB  . ILE A 705  ? 0.4043 0.4196 0.3612 0.0749  -0.0213 -0.1412 703  ILE A CB  
5078  C CG1 . ILE A 705  ? 0.3934 0.4200 0.3501 0.0794  -0.0246 -0.1542 703  ILE A CG1 
5079  C CG2 . ILE A 705  ? 0.3552 0.3593 0.3259 0.0750  -0.0234 -0.1439 703  ILE A CG2 
5080  C CD1 . ILE A 705  ? 0.4212 0.4390 0.3869 0.0781  -0.0303 -0.1595 703  ILE A CD1 
5081  N N   . SER A 706  ? 0.3519 0.3697 0.2994 0.0729  -0.0098 -0.1220 704  SER A N   
5082  C CA  . SER A 706  ? 0.3551 0.3657 0.3016 0.0694  -0.0064 -0.1108 704  SER A CA  
5083  C C   . SER A 706  ? 0.3230 0.3235 0.2818 0.0696  -0.0080 -0.1129 704  SER A C   
5084  O O   . SER A 706  ? 0.3432 0.3453 0.3105 0.0734  -0.0110 -0.1236 704  SER A O   
5085  C CB  . SER A 706  ? 0.3524 0.3757 0.2889 0.0705  -0.0014 -0.1063 704  SER A CB  
5086  O OG  . SER A 706  ? 0.3826 0.4180 0.3205 0.0757  -0.0013 -0.1164 704  SER A OG  
5087  N N   . PRO A 707  ? 0.3334 0.3238 0.2942 0.0656  -0.0064 -0.1031 705  PRO A N   
5088  C CA  . PRO A 707  ? 0.3889 0.3689 0.3617 0.0652  -0.0083 -0.1036 705  PRO A CA  
5089  C C   . PRO A 707  ? 0.3702 0.3551 0.3434 0.0673  -0.0052 -0.1031 705  PRO A C   
5090  O O   . PRO A 707  ? 0.3752 0.3711 0.3391 0.0685  -0.0012 -0.1010 705  PRO A O   
5091  C CB  . PRO A 707  ? 0.3338 0.3020 0.3068 0.0595  -0.0079 -0.0925 705  PRO A CB  
5092  C CG  . PRO A 707  ? 0.3882 0.3627 0.3482 0.0578  -0.0035 -0.0846 705  PRO A CG  
5093  C CD  . PRO A 707  ? 0.3639 0.3517 0.3163 0.0613  -0.0031 -0.0909 705  PRO A CD  
5094  N N   . TRP A 708  ? 0.3723 0.3489 0.3570 0.0677  -0.0074 -0.1048 706  TRP A N   
5095  C CA  . TRP A 708  ? 0.3581 0.3383 0.3452 0.0698  -0.0051 -0.1047 706  TRP A CA  
5096  C C   . TRP A 708  ? 0.3735 0.3490 0.3567 0.0656  -0.0014 -0.0922 706  TRP A C   
5097  O O   . TRP A 708  ? 0.4169 0.3975 0.3991 0.0669  0.0015  -0.0907 706  TRP A O   
5098  C CB  . TRP A 708  ? 0.3980 0.3715 0.4002 0.0723  -0.0094 -0.1120 706  TRP A CB  
5099  C CG  . TRP A 708  ? 0.4061 0.3644 0.4178 0.0684  -0.0134 -0.1079 706  TRP A CG  
5100  C CD1 . TRP A 708  ? 0.4492 0.4015 0.4683 0.0681  -0.0184 -0.1132 706  TRP A CD1 
5101  C CD2 . TRP A 708  ? 0.3297 0.2778 0.3443 0.0638  -0.0127 -0.0971 706  TRP A CD2 
5102  N NE1 . TRP A 708  ? 0.4242 0.3634 0.4508 0.0636  -0.0207 -0.1059 706  TRP A NE1 
5103  C CE2 . TRP A 708  ? 0.3890 0.3258 0.4126 0.0610  -0.0173 -0.0961 706  TRP A CE2 
5104  C CE3 . TRP A 708  ? 0.3261 0.2741 0.3368 0.0619  -0.0088 -0.0883 706  TRP A CE3 
5105  C CZ2 . TRP A 708  ? 0.3924 0.3190 0.4208 0.0563  -0.0178 -0.0863 706  TRP A CZ2 
5106  C CZ3 . TRP A 708  ? 0.4134 0.3507 0.4286 0.0574  -0.0095 -0.0792 706  TRP A CZ3 
5107  C CH2 . TRP A 708  ? 0.3927 0.3199 0.4165 0.0547  -0.0139 -0.0782 706  TRP A CH2 
5108  N N   . ASN A 709  ? 0.3621 0.3287 0.3431 0.0607  -0.0015 -0.0837 707  ASN A N   
5109  C CA  . ASN A 709  ? 0.3990 0.3605 0.3781 0.0568  0.0013  -0.0729 707  ASN A CA  
5110  C C   . ASN A 709  ? 0.3991 0.3684 0.3659 0.0556  0.0060  -0.0663 707  ASN A C   
5111  O O   . ASN A 709  ? 0.4302 0.3984 0.3954 0.0536  0.0087  -0.0592 707  ASN A O   
5112  C CB  . ASN A 709  ? 0.4041 0.3534 0.3873 0.0522  -0.0009 -0.0666 707  ASN A CB  
5113  C CG  . ASN A 709  ? 0.4474 0.3968 0.4237 0.0500  -0.0012 -0.0648 707  ASN A CG  
5114  O OD1 . ASN A 709  ? 0.4482 0.4054 0.4189 0.0524  -0.0010 -0.0699 707  ASN A OD1 
5115  N ND2 . ASN A 709  ? 0.4362 0.3777 0.4130 0.0455  -0.0016 -0.0574 707  ASN A ND2 
5116  N N   . PHE A 710  ? 0.3892 0.3663 0.3478 0.0566  0.0067  -0.0684 708  PHE A N   
5117  C CA  . PHE A 710  ? 0.3845 0.3712 0.3322 0.0561  0.0108  -0.0631 708  PHE A CA  
5118  C C   . PHE A 710  ? 0.4312 0.4315 0.3745 0.0605  0.0111  -0.0712 708  PHE A C   
5119  O O   . PHE A 710  ? 0.3876 0.3934 0.3240 0.0605  0.0110  -0.0715 708  PHE A O   
5120  C CB  . PHE A 710  ? 0.4089 0.3914 0.3499 0.0520  0.0115  -0.0549 708  PHE A CB  
5121  C CG  . PHE A 710  ? 0.4396 0.4120 0.3831 0.0479  0.0122  -0.0464 708  PHE A CG  
5122  C CD1 . PHE A 710  ? 0.4967 0.4711 0.4375 0.0466  0.0155  -0.0399 708  PHE A CD1 
5123  C CD2 . PHE A 710  ? 0.4890 0.4507 0.4380 0.0454  0.0094  -0.0452 708  PHE A CD2 
5124  C CE1 . PHE A 710  ? 0.5173 0.4832 0.4605 0.0431  0.0160  -0.0328 708  PHE A CE1 
5125  C CE2 . PHE A 710  ? 0.4885 0.4424 0.4396 0.0417  0.0101  -0.0377 708  PHE A CE2 
5126  C CZ  . PHE A 710  ? 0.5095 0.4656 0.4576 0.0407  0.0133  -0.0318 708  PHE A CZ  
5127  N N   . PRO A 711  ? 0.3616 0.3688 0.3090 0.0644  0.0115  -0.0779 709  PRO A N   
5128  C CA  . PRO A 711  ? 0.3512 0.3717 0.2967 0.0693  0.0110  -0.0881 709  PRO A CA  
5129  C C   . PRO A 711  ? 0.3502 0.3857 0.2841 0.0697  0.0148  -0.0848 709  PRO A C   
5130  O O   . PRO A 711  ? 0.3473 0.3957 0.2779 0.0735  0.0146  -0.0925 709  PRO A O   
5131  C CB  . PRO A 711  ? 0.3232 0.3454 0.2778 0.0731  0.0104  -0.0954 709  PRO A CB  
5132  C CG  . PRO A 711  ? 0.3361 0.3530 0.2918 0.0701  0.0131  -0.0860 709  PRO A CG  
5133  C CD  . PRO A 711  ? 0.3548 0.3586 0.3090 0.0647  0.0125  -0.0765 709  PRO A CD  
5134  N N   . LEU A 712  ? 0.3699 0.4049 0.2980 0.0661  0.0182  -0.0737 710  LEU A N   
5135  C CA  . LEU A 712  ? 0.3463 0.3946 0.2637 0.0658  0.0213  -0.0688 710  LEU A CA  
5136  C C   . LEU A 712  ? 0.3566 0.3994 0.2678 0.0618  0.0210  -0.0605 710  LEU A C   
5137  O O   . LEU A 712  ? 0.3320 0.3841 0.2359 0.0624  0.0210  -0.0605 710  LEU A O   
5138  C CB  . LEU A 712  ? 0.3095 0.3641 0.2252 0.0650  0.0255  -0.0626 710  LEU A CB  
5139  C CG  . LEU A 712  ? 0.3661 0.4343 0.2716 0.0639  0.0287  -0.0558 710  LEU A CG  
5140  C CD1 . LEU A 712  ? 0.3730 0.4584 0.2743 0.0683  0.0287  -0.0644 710  LEU A CD1 
5141  C CD2 . LEU A 712  ? 0.3800 0.4526 0.2845 0.0620  0.0325  -0.0479 710  LEU A CD2 
5142  N N   . ALA A 713  ? 0.3563 0.3846 0.2707 0.0578  0.0203  -0.0538 711  ALA A N   
5143  C CA  . ALA A 713  ? 0.3293 0.3533 0.2380 0.0541  0.0204  -0.0452 711  ALA A CA  
5144  C C   . ALA A 713  ? 0.3558 0.3765 0.2639 0.0544  0.0170  -0.0493 711  ALA A C   
5145  O O   . ALA A 713  ? 0.3577 0.3841 0.2586 0.0539  0.0171  -0.0465 711  ALA A O   
5146  C CB  . ALA A 713  ? 0.3341 0.3452 0.2464 0.0501  0.0210  -0.0372 711  ALA A CB  
5147  N N   . ILE A 714  ? 0.3704 0.3817 0.2862 0.0548  0.0139  -0.0552 712  ILE A N   
5148  C CA  . ILE A 714  ? 0.3458 0.3543 0.2616 0.0549  0.0105  -0.0593 712  ILE A CA  
5149  C C   . ILE A 714  ? 0.3604 0.3823 0.2726 0.0591  0.0097  -0.0679 712  ILE A C   
5150  O O   . ILE A 714  ? 0.3641 0.3903 0.2709 0.0592  0.0085  -0.0683 712  ILE A O   
5151  C CB  . ILE A 714  ? 0.3800 0.3755 0.3059 0.0540  0.0072  -0.0630 712  ILE A CB  
5152  C CG1 . ILE A 714  ? 0.3934 0.3774 0.3210 0.0495  0.0080  -0.0536 712  ILE A CG1 
5153  C CG2 . ILE A 714  ? 0.3473 0.3419 0.2746 0.0549  0.0034  -0.0696 712  ILE A CG2 
5154  C CD1 . ILE A 714  ? 0.4659 0.4379 0.4035 0.0478  0.0051  -0.0552 712  ILE A CD1 
5155  N N   . PHE A 715  ? 0.3537 0.3832 0.2685 0.0628  0.0104  -0.0749 713  PHE A N   
5156  C CA  . PHE A 715  ? 0.3900 0.4350 0.3007 0.0671  0.0102  -0.0833 713  PHE A CA  
5157  C C   . PHE A 715  ? 0.3905 0.4477 0.2897 0.0663  0.0127  -0.0766 713  PHE A C   
5158  O O   . PHE A 715  ? 0.3686 0.4329 0.2628 0.0675  0.0111  -0.0796 713  PHE A O   
5159  C CB  . PHE A 715  ? 0.3626 0.4149 0.2777 0.0708  0.0115  -0.0899 713  PHE A CB  
5160  C CG  . PHE A 715  ? 0.3737 0.4447 0.2841 0.0755  0.0120  -0.0983 713  PHE A CG  
5161  C CD1 . PHE A 715  ? 0.3546 0.4286 0.2699 0.0796  0.0083  -0.1113 713  PHE A CD1 
5162  C CD2 . PHE A 715  ? 0.3701 0.4563 0.2714 0.0758  0.0160  -0.0933 713  PHE A CD2 
5163  C CE1 . PHE A 715  ? 0.4080 0.5006 0.3189 0.0842  0.0087  -0.1201 713  PHE A CE1 
5164  C CE2 . PHE A 715  ? 0.3761 0.4815 0.2726 0.0801  0.0166  -0.1010 713  PHE A CE2 
5165  C CZ  . PHE A 715  ? 0.4096 0.5185 0.3108 0.0845  0.0130  -0.1148 713  PHE A CZ  
5166  N N   . THR A 716  ? 0.3535 0.4130 0.2489 0.0641  0.0164  -0.0671 714  THR A N   
5167  C CA  . THR A 716  ? 0.3487 0.4192 0.2342 0.0628  0.0187  -0.0592 714  THR A CA  
5168  C C   . THR A 716  ? 0.3672 0.4306 0.2492 0.0598  0.0168  -0.0531 714  THR A C   
5169  O O   . THR A 716  ? 0.3527 0.4260 0.2276 0.0605  0.0164  -0.0522 714  THR A O   
5170  C CB  . THR A 716  ? 0.3759 0.4477 0.2601 0.0605  0.0226  -0.0498 714  THR A CB  
5171  O OG1 . THR A 716  ? 0.3894 0.4706 0.2761 0.0637  0.0246  -0.0557 714  THR A OG1 
5172  C CG2 . THR A 716  ? 0.3699 0.4514 0.2452 0.0584  0.0246  -0.0399 714  THR A CG2 
5173  N N   . GLY A 717  ? 0.3522 0.3994 0.2391 0.0566  0.0157  -0.0489 715  GLY A N   
5174  C CA  . GLY A 717  ? 0.3369 0.3777 0.2210 0.0538  0.0141  -0.0429 715  GLY A CA  
5175  C C   . GLY A 717  ? 0.3761 0.4198 0.2586 0.0557  0.0107  -0.0498 715  GLY A C   
5176  O O   . GLY A 717  ? 0.3461 0.3951 0.2224 0.0551  0.0101  -0.0460 715  GLY A O   
5177  N N   . GLN A 718  ? 0.3355 0.3759 0.2244 0.0579  0.0083  -0.0600 716  GLN A N   
5178  C CA  . GLN A 718  ? 0.3409 0.3842 0.2294 0.0597  0.0048  -0.0673 716  GLN A CA  
5179  C C   . GLN A 718  ? 0.3932 0.4546 0.2736 0.0628  0.0053  -0.0704 716  GLN A C   
5180  O O   . GLN A 718  ? 0.3430 0.4094 0.2181 0.0629  0.0037  -0.0696 716  GLN A O   
5181  C CB  . GLN A 718  ? 0.3368 0.3735 0.2349 0.0615  0.0017  -0.0779 716  GLN A CB  
5182  C CG  . GLN A 718  ? 0.3258 0.3451 0.2325 0.0582  0.0006  -0.0748 716  GLN A CG  
5183  C CD  . GLN A 718  ? 0.4039 0.4173 0.3209 0.0598  -0.0031 -0.0849 716  GLN A CD  
5184  O OE1 . GLN A 718  ? 0.4076 0.4096 0.3308 0.0574  -0.0056 -0.0843 716  GLN A OE1 
5185  N NE2 . GLN A 718  ? 0.3722 0.3936 0.2916 0.0640  -0.0036 -0.0943 716  GLN A NE2 
5186  N N   . ILE A 719  ? 0.3420 0.4144 0.2212 0.0655  0.0077  -0.0737 717  ILE A N   
5187  C CA  . ILE A 719  ? 0.3814 0.4733 0.2530 0.0688  0.0084  -0.0775 717  ILE A CA  
5188  C C   . ILE A 719  ? 0.3634 0.4629 0.2255 0.0664  0.0105  -0.0656 717  ILE A C   
5189  O O   . ILE A 719  ? 0.4043 0.5157 0.2596 0.0676  0.0095  -0.0660 717  ILE A O   
5190  C CB  . ILE A 719  ? 0.3709 0.4730 0.2444 0.0723  0.0105  -0.0844 717  ILE A CB  
5191  C CG1 . ILE A 719  ? 0.3525 0.4495 0.2355 0.0756  0.0072  -0.0980 717  ILE A CG1 
5192  C CG2 . ILE A 719  ? 0.4313 0.5557 0.2957 0.0750  0.0125  -0.0853 717  ILE A CG2 
5193  C CD1 . ILE A 719  ? 0.4320 0.5327 0.3203 0.0783  0.0089  -0.1037 717  ILE A CD1 
5194  N N   . ALA A 720  ? 0.3829 0.4760 0.2450 0.0629  0.0132  -0.0548 718  ALA A N   
5195  C CA  . ALA A 720  ? 0.3605 0.4599 0.2151 0.0604  0.0149  -0.0429 718  ALA A CA  
5196  C C   . ALA A 720  ? 0.3271 0.4213 0.1792 0.0587  0.0119  -0.0391 718  ALA A C   
5197  O O   . ALA A 720  ? 0.3469 0.4518 0.1919 0.0585  0.0118  -0.0339 718  ALA A O   
5198  C CB  . ALA A 720  ? 0.3260 0.4173 0.1829 0.0569  0.0177  -0.0329 718  ALA A CB  
5199  N N   . ALA A 721  ? 0.3540 0.4319 0.2122 0.0572  0.0096  -0.0408 719  ALA A N   
5200  C CA  . ALA A 721  ? 0.3109 0.3836 0.1676 0.0557  0.0067  -0.0375 719  ALA A CA  
5201  C C   . ALA A 721  ? 0.3561 0.4403 0.2087 0.0587  0.0041  -0.0451 719  ALA A C   
5202  O O   . ALA A 721  ? 0.3949 0.4855 0.2416 0.0583  0.0029  -0.0402 719  ALA A O   
5203  C CB  . ALA A 721  ? 0.3352 0.3898 0.1998 0.0536  0.0049  -0.0389 719  ALA A CB  
5204  N N   . ALA A 722  ? 0.3445 0.4312 0.2007 0.0619  0.0028  -0.0572 720  ALA A N   
5205  C CA  . ALA A 722  ? 0.3518 0.4495 0.2048 0.0651  0.0000  -0.0658 720  ALA A CA  
5206  C C   . ALA A 722  ? 0.3591 0.4771 0.2024 0.0668  0.0017  -0.0630 720  ALA A C   
5207  O O   . ALA A 722  ? 0.3761 0.5026 0.2136 0.0674  -0.0003 -0.0621 720  ALA A O   
5208  C CB  . ALA A 722  ? 0.3278 0.4248 0.1877 0.0684  -0.0017 -0.0798 720  ALA A CB  
5209  N N   . LEU A 723  ? 0.3436 0.4702 0.1850 0.0675  0.0054  -0.0609 721  LEU A N   
5210  C CA  . LEU A 723  ? 0.3456 0.4933 0.1780 0.0689  0.0074  -0.0578 721  LEU A CA  
5211  C C   . LEU A 723  ? 0.3686 0.5179 0.1948 0.0655  0.0076  -0.0436 721  LEU A C   
5212  O O   . LEU A 723  ? 0.3493 0.5138 0.1680 0.0665  0.0069  -0.0414 721  LEU A O   
5213  C CB  . LEU A 723  ? 0.3542 0.5094 0.1870 0.0698  0.0114  -0.0577 721  LEU A CB  
5214  C CG  . LEU A 723  ? 0.3602 0.5208 0.1975 0.0742  0.0115  -0.0720 721  LEU A CG  
5215  C CD1 . LEU A 723  ? 0.3662 0.5315 0.2048 0.0743  0.0157  -0.0694 721  LEU A CD1 
5216  C CD2 . LEU A 723  ? 0.3615 0.5422 0.1929 0.0785  0.0100  -0.0812 721  LEU A CD2 
5217  N N   . VAL A 724  ? 0.3993 0.5340 0.2290 0.0616  0.0087  -0.0336 722  VAL A N   
5218  C CA  . VAL A 724  ? 0.3602 0.4968 0.1851 0.0585  0.0088  -0.0199 722  VAL A CA  
5219  C C   . VAL A 724  ? 0.3803 0.5132 0.2037 0.0583  0.0048  -0.0194 722  VAL A C   
5220  O O   . VAL A 724  ? 0.3674 0.5080 0.1853 0.0572  0.0039  -0.0106 722  VAL A O   
5221  C CB  . VAL A 724  ? 0.3280 0.4504 0.1575 0.0546  0.0108  -0.0101 722  VAL A CB  
5222  C CG1 . VAL A 724  ? 0.3736 0.4752 0.2102 0.0528  0.0085  -0.0110 722  VAL A CG1 
5223  C CG2 . VAL A 724  ? 0.3581 0.4874 0.1830 0.0518  0.0117  0.0041  722  VAL A CG2 
5224  N N   . ALA A 725  ? 0.3848 0.5068 0.2134 0.0593  0.0021  -0.0285 723  ALA A N   
5225  C CA  . ALA A 725  ? 0.3853 0.5054 0.2129 0.0596  -0.0019 -0.0300 723  ALA A CA  
5226  C C   . ALA A 725  ? 0.4082 0.5467 0.2293 0.0631  -0.0036 -0.0369 723  ALA A C   
5227  O O   . ALA A 725  ? 0.4138 0.5521 0.2341 0.0636  -0.0071 -0.0391 723  ALA A O   
5228  C CB  . ALA A 725  ? 0.3692 0.4726 0.2051 0.0593  -0.0042 -0.0375 723  ALA A CB  
5229  N N   . GLY A 726  ? 0.3965 0.5515 0.2134 0.0656  -0.0013 -0.0408 724  GLY A N   
5230  C CA  . GLY A 726  ? 0.3980 0.5729 0.2081 0.0691  -0.0027 -0.0473 724  GLY A CA  
5231  C C   . GLY A 726  ? 0.4024 0.5800 0.2160 0.0731  -0.0045 -0.0640 724  GLY A C   
5232  O O   . GLY A 726  ? 0.4142 0.6076 0.2227 0.0762  -0.0064 -0.0709 724  GLY A O   
5233  N N   . ASN A 727  ? 0.3898 0.5530 0.2122 0.0732  -0.0043 -0.0706 725  ASN A N   
5234  C CA  . ASN A 727  ? 0.4056 0.5694 0.2334 0.0768  -0.0066 -0.0864 725  ASN A CA  
5235  C C   . ASN A 727  ? 0.3781 0.5527 0.2064 0.0799  -0.0038 -0.0935 725  ASN A C   
5236  O O   . ASN A 727  ? 0.4113 0.5815 0.2413 0.0783  -0.0003 -0.0875 725  ASN A O   
5237  C CB  . ASN A 727  ? 0.3811 0.5223 0.2195 0.0749  -0.0086 -0.0896 725  ASN A CB  
5238  C CG  . ASN A 727  ? 0.3606 0.4908 0.1994 0.0718  -0.0111 -0.0827 725  ASN A CG  
5239  O OD1 . ASN A 727  ? 0.3999 0.5345 0.2370 0.0730  -0.0145 -0.0872 725  ASN A OD1 
5240  N ND2 . ASN A 727  ? 0.3748 0.4912 0.2158 0.0680  -0.0094 -0.0720 725  ASN A ND2 
5241  N N   . PRO A 728  ? 0.3642 0.5531 0.1916 0.0845  -0.0054 -0.1066 726  PRO A N   
5242  C CA  . PRO A 728  ? 0.3662 0.5619 0.1973 0.0879  -0.0036 -0.1162 726  PRO A CA  
5243  C C   . PRO A 728  ? 0.3940 0.5693 0.2376 0.0876  -0.0052 -0.1228 726  PRO A C   
5244  O O   . PRO A 728  ? 0.3918 0.5529 0.2413 0.0863  -0.0088 -0.1254 726  PRO A O   
5245  C CB  . PRO A 728  ? 0.3751 0.5892 0.2050 0.0921  -0.0059 -0.1277 726  PRO A CB  
5246  C CG  . PRO A 728  ? 0.3784 0.5879 0.2074 0.0915  -0.0104 -0.1295 726  PRO A CG  
5247  C CD  . PRO A 728  ? 0.3868 0.5838 0.2117 0.0869  -0.0097 -0.1148 726  PRO A CD  
5248  N N   . VAL A 729  ? 0.3851 0.5601 0.2332 0.0888  -0.0025 -0.1254 727  VAL A N   
5249  C CA  . VAL A 729  ? 0.3927 0.5480 0.2525 0.0878  -0.0033 -0.1283 727  VAL A CA  
5250  C C   . VAL A 729  ? 0.3949 0.5557 0.2619 0.0927  -0.0044 -0.1434 727  VAL A C   
5251  O O   . VAL A 729  ? 0.4188 0.5974 0.2818 0.0961  -0.0020 -0.1475 727  VAL A O   
5252  C CB  . VAL A 729  ? 0.3714 0.5169 0.2314 0.0838  0.0008  -0.1152 727  VAL A CB  
5253  C CG1 . VAL A 729  ? 0.3697 0.4991 0.2415 0.0836  0.0003  -0.1195 727  VAL A CG1 
5254  C CG2 . VAL A 729  ? 0.3664 0.5018 0.2227 0.0790  0.0007  -0.1023 727  VAL A CG2 
5255  N N   . LEU A 730  ? 0.3571 0.5029 0.2355 0.0932  -0.0083 -0.1516 728  LEU A N   
5256  C CA  . LEU A 730  ? 0.3598 0.5046 0.2485 0.0971  -0.0099 -0.1645 728  LEU A CA  
5257  C C   . LEU A 730  ? 0.3978 0.5230 0.2953 0.0938  -0.0089 -0.1581 728  LEU A C   
5258  O O   . LEU A 730  ? 0.3930 0.5006 0.2959 0.0902  -0.0111 -0.1539 728  LEU A O   
5259  C CB  . LEU A 730  ? 0.3674 0.5097 0.2641 0.0999  -0.0158 -0.1787 728  LEU A CB  
5260  C CG  . LEU A 730  ? 0.3960 0.5535 0.2880 0.1018  -0.0185 -0.1845 728  LEU A CG  
5261  C CD1 . LEU A 730  ? 0.4320 0.6122 0.3182 0.1042  -0.0155 -0.1843 728  LEU A CD1 
5262  C CD2 . LEU A 730  ? 0.3779 0.5323 0.2608 0.0987  -0.0191 -0.1764 728  LEU A CD2 
5263  N N   . ALA A 731  ? 0.4081 0.5371 0.3069 0.0951  -0.0055 -0.1573 729  ALA A N   
5264  C CA  . ALA A 731  ? 0.4014 0.5143 0.3067 0.0920  -0.0038 -0.1497 729  ALA A CA  
5265  C C   . ALA A 731  ? 0.3741 0.4792 0.2933 0.0950  -0.0069 -0.1611 729  ALA A C   
5266  O O   . ALA A 731  ? 0.4587 0.5755 0.3802 0.0997  -0.0063 -0.1703 729  ALA A O   
5267  C CB  . ALA A 731  ? 0.4042 0.5259 0.3024 0.0910  0.0019  -0.1403 729  ALA A CB  
5268  N N   . LYS A 732  ? 0.4267 0.5126 0.3558 0.0923  -0.0103 -0.1604 730  LYS A N   
5269  C CA  . LYS A 732  ? 0.4099 0.4863 0.3536 0.0944  -0.0138 -0.1696 730  LYS A CA  
5270  C C   . LYS A 732  ? 0.4009 0.4632 0.3495 0.0909  -0.0116 -0.1596 730  LYS A C   
5271  O O   . LYS A 732  ? 0.3545 0.4011 0.3063 0.0862  -0.0128 -0.1518 730  LYS A O   
5272  C CB  . LYS A 732  ? 0.4083 0.4739 0.3610 0.0939  -0.0198 -0.1764 730  LYS A CB  
5273  C CG  . LYS A 732  ? 0.4679 0.5336 0.4338 0.0989  -0.0247 -0.1923 730  LYS A CG  
5274  C CD  . LYS A 732  ? 0.4416 0.4969 0.4191 0.0992  -0.0249 -0.1921 730  LYS A CD  
5275  C CE  . LYS A 732  ? 0.4971 0.5313 0.4823 0.0935  -0.0265 -0.1823 730  LYS A CE  
5276  N NZ  . LYS A 732  ? 0.4886 0.5125 0.4870 0.0941  -0.0280 -0.1836 730  LYS A NZ  
5277  N N   . PRO A 733  ? 0.3581 0.4259 0.3074 0.0929  -0.0085 -0.1596 731  PRO A N   
5278  C CA  . PRO A 733  ? 0.3695 0.4246 0.3233 0.0895  -0.0066 -0.1501 731  PRO A CA  
5279  C C   . PRO A 733  ? 0.3747 0.4150 0.3443 0.0900  -0.0112 -0.1556 731  PRO A C   
5280  O O   . PRO A 733  ? 0.4060 0.4478 0.3842 0.0939  -0.0156 -0.1684 731  PRO A O   
5281  C CB  . PRO A 733  ? 0.3528 0.4214 0.3024 0.0922  -0.0020 -0.1498 731  PRO A CB  
5282  C CG  . PRO A 733  ? 0.3504 0.4352 0.3007 0.0985  -0.0036 -0.1645 731  PRO A CG  
5283  C CD  . PRO A 733  ? 0.3811 0.4684 0.3272 0.0984  -0.0066 -0.1685 731  PRO A CD  
5284  N N   . ALA A 734  ? 0.3584 0.3845 0.3323 0.0857  -0.0104 -0.1457 732  ALA A N   
5285  C CA  . ALA A 734  ? 0.4101 0.4223 0.3992 0.0857  -0.0147 -0.1491 732  ALA A CA  
5286  C C   . ALA A 734  ? 0.4245 0.4438 0.4218 0.0916  -0.0159 -0.1606 732  ALA A C   
5287  O O   . ALA A 734  ? 0.3989 0.4311 0.3902 0.0944  -0.0119 -0.1615 732  ALA A O   
5288  C CB  . ALA A 734  ? 0.3607 0.3597 0.3518 0.0806  -0.0129 -0.1363 732  ALA A CB  
5289  N N   . GLU A 735  ? 0.4383 0.4492 0.4501 0.0936  -0.0216 -0.1696 733  GLU A N   
5290  C CA  . GLU A 735  ? 0.4334 0.4498 0.4551 0.0996  -0.0238 -0.1820 733  GLU A CA  
5291  C C   . GLU A 735  ? 0.4390 0.4543 0.4631 0.0998  -0.0207 -0.1765 733  GLU A C   
5292  O O   . GLU A 735  ? 0.3848 0.4109 0.4114 0.1050  -0.0198 -0.1847 733  GLU A O   
5293  C CB  . GLU A 735  ? 0.4891 0.4936 0.5277 0.1007  -0.0312 -0.1908 733  GLU A CB  
5294  C CG  . GLU A 735  ? 0.6064 0.6157 0.6575 0.1074  -0.0348 -0.2055 733  GLU A CG  
5295  C CD  . GLU A 735  ? 0.6422 0.6383 0.7110 0.1072  -0.0426 -0.2116 733  GLU A CD  
5296  O OE1 . GLU A 735  ? 0.6739 0.6578 0.7446 0.1028  -0.0451 -0.2066 733  GLU A OE1 
5297  O OE2 . GLU A 735  ? 0.6904 0.6892 0.7711 0.1100  -0.0462 -0.2189 733  GLU A OE2 
5298  N N   . GLU A 736  ? 0.3997 0.4031 0.4230 0.0943  -0.0189 -0.1629 734  GLU A N   
5299  C CA  . GLU A 736  ? 0.3835 0.3850 0.4100 0.0941  -0.0164 -0.1574 734  GLU A CA  
5300  C C   . GLU A 736  ? 0.3710 0.3865 0.3840 0.0944  -0.0096 -0.1522 734  GLU A C   
5301  O O   . GLU A 736  ? 0.4115 0.4300 0.4273 0.0961  -0.0076 -0.1514 734  GLU A O   
5302  C CB  . GLU A 736  ? 0.4224 0.4067 0.4533 0.0881  -0.0172 -0.1450 734  GLU A CB  
5303  C CG  . GLU A 736  ? 0.4529 0.4227 0.4991 0.0872  -0.0239 -0.1484 734  GLU A CG  
5304  C CD  . GLU A 736  ? 0.5119 0.4756 0.5556 0.0834  -0.0261 -0.1460 734  GLU A CD  
5305  O OE1 . GLU A 736  ? 0.4171 0.3899 0.4488 0.0834  -0.0237 -0.1468 734  GLU A OE1 
5306  O OE2 . GLU A 736  ? 0.5193 0.4693 0.5735 0.0802  -0.0304 -0.1428 734  GLU A OE2 
5307  N N   . THR A 737  ? 0.3966 0.4208 0.3956 0.0928  -0.0064 -0.1483 735  THR A N   
5308  C CA  . THR A 737  ? 0.3925 0.4281 0.3791 0.0917  -0.0001 -0.1404 735  THR A CA  
5309  C C   . THR A 737  ? 0.3753 0.4288 0.3504 0.0942  0.0021  -0.1449 735  THR A C   
5310  O O   . THR A 737  ? 0.3965 0.4540 0.3598 0.0908  0.0053  -0.1360 735  THR A O   
5311  C CB  . THR A 737  ? 0.3836 0.4088 0.3641 0.0850  0.0023  -0.1251 735  THR A CB  
5312  O OG1 . THR A 737  ? 0.3725 0.3925 0.3489 0.0822  0.0004  -0.1231 735  THR A OG1 
5313  C CG2 . THR A 737  ? 0.3626 0.3724 0.3534 0.0824  0.0007  -0.1197 735  THR A CG2 
5314  N N   . PRO A 738  ? 0.4027 0.4682 0.3812 0.1002  0.0003  -0.1588 736  PRO A N   
5315  C CA  . PRO A 738  ? 0.4033 0.4881 0.3706 0.1028  0.0024  -0.1633 736  PRO A CA  
5316  C C   . PRO A 738  ? 0.3989 0.5003 0.3564 0.1033  0.0084  -0.1581 736  PRO A C   
5317  O O   . PRO A 738  ? 0.3511 0.4672 0.2970 0.1034  0.0110  -0.1566 736  PRO A O   
5318  C CB  . PRO A 738  ? 0.4001 0.4920 0.3763 0.1094  -0.0019 -0.1810 736  PRO A CB  
5319  C CG  . PRO A 738  ? 0.3651 0.4495 0.3545 0.1115  -0.0033 -0.1844 736  PRO A CG  
5320  C CD  . PRO A 738  ? 0.3871 0.4509 0.3799 0.1053  -0.0035 -0.1710 736  PRO A CD  
5321  N N   . LEU A 739  ? 0.3317 0.4318 0.2939 0.1035  0.0107  -0.1549 737  LEU A N   
5322  C CA  . LEU A 739  ? 0.3648 0.4824 0.3192 0.1045  0.0162  -0.1516 737  LEU A CA  
5323  C C   . LEU A 739  ? 0.3444 0.4634 0.2862 0.0988  0.0204  -0.1364 737  LEU A C   
5324  O O   . LEU A 739  ? 0.3367 0.4732 0.2682 0.0993  0.0237  -0.1345 737  LEU A O   
5325  C CB  . LEU A 739  ? 0.3591 0.4742 0.3225 0.1060  0.0172  -0.1518 737  LEU A CB  
5326  C CG  . LEU A 739  ? 0.3993 0.5152 0.3761 0.1123  0.0133  -0.1671 737  LEU A CG  
5327  C CD1 . LEU A 739  ? 0.4179 0.5304 0.4029 0.1131  0.0145  -0.1652 737  LEU A CD1 
5328  C CD2 . LEU A 739  ? 0.3441 0.4825 0.3176 0.1187  0.0136  -0.1807 737  LEU A CD2 
5329  N N   . ILE A 740  ? 0.3211 0.4222 0.2640 0.0933  0.0201  -0.1253 738  ILE A N   
5330  C CA  . ILE A 740  ? 0.3739 0.4753 0.3061 0.0880  0.0235  -0.1114 738  ILE A CA  
5331  C C   . ILE A 740  ? 0.3652 0.4714 0.2889 0.0874  0.0224  -0.1116 738  ILE A C   
5332  O O   . ILE A 740  ? 0.3779 0.4931 0.2913 0.0850  0.0254  -0.1034 738  ILE A O   
5333  C CB  . ILE A 740  ? 0.3978 0.4794 0.3338 0.0827  0.0232  -0.1007 738  ILE A CB  
5334  C CG1 . ILE A 740  ? 0.3944 0.4767 0.3206 0.0775  0.0268  -0.0867 738  ILE A CG1 
5335  C CG2 . ILE A 740  ? 0.3883 0.4532 0.3304 0.0814  0.0184  -0.1032 738  ILE A CG2 
5336  C CD1 . ILE A 740  ? 0.3932 0.4907 0.3145 0.0778  0.0316  -0.0822 738  ILE A CD1 
5337  N N   . ALA A 741  ? 0.3929 0.4940 0.3213 0.0896  0.0179  -0.1212 739  ALA A N   
5338  C CA  . ALA A 741  ? 0.3810 0.4880 0.3017 0.0895  0.0166  -0.1225 739  ALA A CA  
5339  C C   . ALA A 741  ? 0.3786 0.5096 0.2911 0.0932  0.0191  -0.1274 739  ALA A C   
5340  O O   . ALA A 741  ? 0.3416 0.4820 0.2434 0.0913  0.0210  -0.1207 739  ALA A O   
5341  C CB  . ALA A 741  ? 0.3930 0.4905 0.3217 0.0913  0.0110  -0.1327 739  ALA A CB  
5342  N N   . ALA A 742  ? 0.3468 0.4886 0.2646 0.0986  0.0190  -0.1388 740  ALA A N   
5343  C CA  . ALA A 742  ? 0.3765 0.5432 0.2869 0.1027  0.0214  -0.1446 740  ALA A CA  
5344  C C   . ALA A 742  ? 0.3891 0.5671 0.2897 0.0995  0.0270  -0.1316 740  ALA A C   
5345  O O   . ALA A 742  ? 0.3965 0.5918 0.2867 0.0996  0.0290  -0.1291 740  ALA A O   
5346  C CB  . ALA A 742  ? 0.3723 0.5478 0.2916 0.1091  0.0204  -0.1593 740  ALA A CB  
5347  N N   . GLU A 743  ? 0.3820 0.5508 0.2863 0.0965  0.0293  -0.1231 741  GLU A N   
5348  C CA  . GLU A 743  ? 0.3967 0.5739 0.2931 0.0929  0.0343  -0.1099 741  GLU A CA  
5349  C C   . GLU A 743  ? 0.3917 0.5640 0.2794 0.0876  0.0345  -0.0976 741  GLU A C   
5350  O O   . GLU A 743  ? 0.3512 0.5376 0.2298 0.0859  0.0376  -0.0895 741  GLU A O   
5351  C CB  . GLU A 743  ? 0.4084 0.5746 0.3118 0.0908  0.0360  -0.1041 741  GLU A CB  
5352  C CG  . GLU A 743  ? 0.4043 0.5760 0.3013 0.0863  0.0406  -0.0897 741  GLU A CG  
5353  C CD  . GLU A 743  ? 0.4448 0.6424 0.3355 0.0886  0.0446  -0.0905 741  GLU A CD  
5354  O OE1 . GLU A 743  ? 0.4493 0.6618 0.3407 0.0943  0.0440  -0.1031 741  GLU A OE1 
5355  O OE2 . GLU A 743  ? 0.4973 0.7013 0.3827 0.0847  0.0482  -0.0783 741  GLU A OE2 
5356  N N   . GLY A 744  ? 0.3760 0.5285 0.2669 0.0851  0.0311  -0.0959 742  GLY A N   
5357  C CA  . GLY A 744  ? 0.3623 0.5099 0.2458 0.0807  0.0307  -0.0857 742  GLY A CA  
5358  C C   . GLY A 744  ? 0.3694 0.5341 0.2441 0.0827  0.0302  -0.0889 742  GLY A C   
5359  O O   . GLY A 744  ? 0.3908 0.5634 0.2567 0.0799  0.0321  -0.0788 742  GLY A O   
5360  N N   . VAL A 745  ? 0.3350 0.5058 0.2123 0.0877  0.0274  -0.1031 743  VAL A N   
5361  C CA  . VAL A 745  ? 0.3426 0.5314 0.2116 0.0902  0.0268  -0.1075 743  VAL A CA  
5362  C C   . VAL A 745  ? 0.3809 0.5939 0.2422 0.0913  0.0312  -0.1042 743  VAL A C   
5363  O O   . VAL A 745  ? 0.3851 0.6120 0.2366 0.0902  0.0323  -0.0983 743  VAL A O   
5364  C CB  . VAL A 745  ? 0.3472 0.5379 0.2219 0.0956  0.0226  -0.1247 743  VAL A CB  
5365  C CG1 . VAL A 745  ? 0.4043 0.6191 0.2706 0.0994  0.0226  -0.1315 743  VAL A CG1 
5366  C CG2 . VAL A 745  ? 0.3518 0.5209 0.2322 0.0935  0.0180  -0.1258 743  VAL A CG2 
5367  N N   . ARG A 746  ? 0.3984 0.6176 0.2643 0.0935  0.0338  -0.1077 744  ARG A N   
5368  C CA  . ARG A 746  ? 0.3795 0.6226 0.2385 0.0944  0.0384  -0.1042 744  ARG A CA  
5369  C C   . ARG A 746  ? 0.3879 0.6315 0.2393 0.0883  0.0412  -0.0861 744  ARG A C   
5370  O O   . ARG A 746  ? 0.3883 0.6494 0.2324 0.0871  0.0427  -0.0802 744  ARG A O   
5371  C CB  . ARG A 746  ? 0.3901 0.6368 0.2565 0.0971  0.0407  -0.1094 744  ARG A CB  
5372  C CG  . ARG A 746  ? 0.3916 0.6609 0.2562 0.0969  0.0435  -0.1062 744  ARG A CG  
5373  C CD  . ARG A 746  ? 0.4008 0.6725 0.2716 0.0981  0.0465  -0.1071 744  ARG A CD  
5374  N NE  . ARG A 746  ? 0.4772 0.7374 0.3461 0.0942  0.0497  -0.0954 744  ARG A NE  
5375  C CZ  . ARG A 746  ? 0.4882 0.7551 0.3506 0.0893  0.0532  -0.0806 744  ARG A CZ  
5376  N NH1 . ARG A 746  ? 0.4598 0.7445 0.3170 0.0876  0.0539  -0.0752 744  ARG A NH1 
5377  N NH2 . ARG A 746  ? 0.4622 0.7126 0.3278 0.0843  0.0541  -0.0693 744  ARG A NH2 
5378  N N   . ILE A 747  ? 0.3720 0.5945 0.2275 0.0836  0.0411  -0.0764 745  ILE A N   
5379  C CA  . ILE A 747  ? 0.3993 0.6196 0.2495 0.0777  0.0432  -0.0595 745  ILE A CA  
5380  C C   . ILE A 747  ? 0.3775 0.5985 0.2203 0.0757  0.0410  -0.0541 745  ILE A C   
5381  O O   . ILE A 747  ? 0.3653 0.5984 0.2006 0.0730  0.0429  -0.0434 745  ILE A O   
5382  C CB  . ILE A 747  ? 0.3625 0.5594 0.2200 0.0737  0.0430  -0.0526 745  ILE A CB  
5383  C CG1 . ILE A 747  ? 0.4152 0.6155 0.2786 0.0750  0.0459  -0.0548 745  ILE A CG1 
5384  C CG2 . ILE A 747  ? 0.3618 0.5520 0.2150 0.0677  0.0436  -0.0367 745  ILE A CG2 
5385  C CD1 . ILE A 747  ? 0.3858 0.5636 0.2581 0.0728  0.0449  -0.0530 745  ILE A CD1 
5386  N N   . LEU A 748  ? 0.3887 0.5968 0.2338 0.0768  0.0369  -0.0610 746  LEU A N   
5387  C CA  . LEU A 748  ? 0.3771 0.5865 0.2155 0.0754  0.0345  -0.0570 746  LEU A CA  
5388  C C   . LEU A 748  ? 0.3821 0.6178 0.2118 0.0784  0.0354  -0.0603 746  LEU A C   
5389  O O   . LEU A 748  ? 0.3775 0.6218 0.1994 0.0759  0.0357  -0.0505 746  LEU A O   
5390  C CB  . LEU A 748  ? 0.3453 0.5380 0.1886 0.0765  0.0299  -0.0655 746  LEU A CB  
5391  C CG  . LEU A 748  ? 0.3954 0.5630 0.2445 0.0721  0.0286  -0.0582 746  LEU A CG  
5392  C CD1 . LEU A 748  ? 0.3995 0.5518 0.2550 0.0736  0.0243  -0.0679 746  LEU A CD1 
5393  C CD2 . LEU A 748  ? 0.3630 0.5277 0.2062 0.0675  0.0287  -0.0441 746  LEU A CD2 
5394  N N   . ARG A 749  ? 0.3734 0.6225 0.2047 0.0838  0.0356  -0.0741 747  ARG A N   
5395  C CA  . ARG A 749  ? 0.3980 0.6679 0.2272 0.0849  0.0351  -0.0756 747  ARG A CA  
5396  C C   . ARG A 749  ? 0.4092 0.6936 0.2354 0.0815  0.0389  -0.0629 747  ARG A C   
5397  O O   . ARG A 749  ? 0.4134 0.7110 0.2347 0.0796  0.0387  -0.0558 747  ARG A O   
5398  C CB  . ARG A 749  ? 0.4291 0.7066 0.2655 0.0903  0.0334  -0.0923 747  ARG A CB  
5399  C CG  . ARG A 749  ? 0.4616 0.7312 0.3007 0.0933  0.0284  -0.1043 747  ARG A CG  
5400  C CD  . ARG A 749  ? 0.5261 0.7995 0.3745 0.0984  0.0264  -0.1206 747  ARG A CD  
5401  N NE  . ARG A 749  ? 0.4857 0.7533 0.3379 0.1010  0.0213  -0.1320 747  ARG A NE  
5402  C CZ  . ARG A 749  ? 0.5046 0.7806 0.3638 0.1054  0.0184  -0.1455 747  ARG A CZ  
5403  N NH1 . ARG A 749  ? 0.5061 0.7966 0.3690 0.1079  0.0201  -0.1499 747  ARG A NH1 
5404  N NH2 . ARG A 749  ? 0.4548 0.7249 0.3178 0.1072  0.0136  -0.1548 747  ARG A NH2 
5405  N N   . GLU A 750  ? 0.3667 0.6489 0.1961 0.0807  0.0423  -0.0598 748  GLU A N   
5406  C CA  . GLU A 750  ? 0.3874 0.6815 0.2148 0.0769  0.0458  -0.0467 748  GLU A CA  
5407  C C   . GLU A 750  ? 0.4056 0.6943 0.2273 0.0713  0.0456  -0.0306 748  GLU A C   
5408  O O   . GLU A 750  ? 0.4391 0.7410 0.2582 0.0683  0.0466  -0.0203 748  GLU A O   
5409  C CB  . GLU A 750  ? 0.4321 0.7219 0.2645 0.0766  0.0492  -0.0457 748  GLU A CB  
5410  C CG  . GLU A 750  ? 0.4931 0.7961 0.3247 0.0726  0.0526  -0.0330 748  GLU A CG  
5411  C CD  . GLU A 750  ? 0.5626 0.8615 0.3994 0.0721  0.0559  -0.0315 748  GLU A CD  
5412  O OE1 . GLU A 750  ? 0.5620 0.8537 0.4039 0.0762  0.0558  -0.0431 748  GLU A OE1 
5413  O OE2 . GLU A 750  ? 0.6074 0.9099 0.4438 0.0676  0.0584  -0.0184 748  GLU A OE2 
5414  N N   . ALA A 751  ? 0.3687 0.6381 0.1891 0.0701  0.0441  -0.0284 749  ALA A N   
5415  C CA  . ALA A 751  ? 0.3696 0.6321 0.1856 0.0651  0.0434  -0.0135 749  ALA A CA  
5416  C C   . ALA A 751  ? 0.3797 0.6501 0.1911 0.0649  0.0403  -0.0121 749  ALA A C   
5417  O O   . ALA A 751  ? 0.4231 0.6900 0.2314 0.0609  0.0393  0.0005  749  ALA A O   
5418  C CB  . ALA A 751  ? 0.3575 0.5936 0.1778 0.0631  0.0416  -0.0118 749  ALA A CB  
5419  N N   . GLY A 752  ? 0.4071 0.6879 0.2187 0.0693  0.0385  -0.0248 750  GLY A N   
5420  C CA  . GLY A 752  ? 0.4224 0.7138 0.2298 0.0693  0.0359  -0.0238 750  GLY A CA  
5421  C C   . GLY A 752  ? 0.3914 0.6760 0.1982 0.0728  0.0319  -0.0355 750  GLY A C   
5422  O O   . GLY A 752  ? 0.3886 0.6828 0.1924 0.0733  0.0296  -0.0360 750  GLY A O   
5423  N N   . ILE A 753  ? 0.4212 0.6898 0.2314 0.0750  0.0310  -0.0449 751  ILE A N   
5424  C CA  . ILE A 753  ? 0.4102 0.6722 0.2212 0.0783  0.0269  -0.0569 751  ILE A CA  
5425  C C   . ILE A 753  ? 0.3990 0.6775 0.2132 0.0826  0.0258  -0.0697 751  ILE A C   
5426  O O   . ILE A 753  ? 0.4081 0.6904 0.2276 0.0852  0.0274  -0.0776 751  ILE A O   
5427  C CB  . ILE A 753  ? 0.3999 0.6410 0.2156 0.0795  0.0259  -0.0640 751  ILE A CB  
5428  C CG1 . ILE A 753  ? 0.3638 0.5851 0.1819 0.0738  0.0262  -0.0496 751  ILE A CG1 
5429  C CG2 . ILE A 753  ? 0.4538 0.6879 0.2721 0.0823  0.0213  -0.0759 751  ILE A CG2 
5430  C CD1 . ILE A 753  ? 0.3853 0.6012 0.1993 0.0710  0.0234  -0.0416 751  ILE A CD1 
5431  N N   . PRO A 754  ? 0.4074 0.6962 0.2189 0.0836  0.0230  -0.0722 752  PRO A N   
5432  C CA  . PRO A 754  ? 0.4674 0.7728 0.2822 0.0879  0.0218  -0.0845 752  PRO A CA  
5433  C C   . PRO A 754  ? 0.4586 0.7539 0.2814 0.0921  0.0194  -0.1011 752  PRO A C   
5434  O O   . PRO A 754  ? 0.4147 0.6909 0.2394 0.0920  0.0173  -0.1042 752  PRO A O   
5435  C CB  . PRO A 754  ? 0.4843 0.7991 0.2942 0.0877  0.0189  -0.0829 752  PRO A CB  
5436  C CG  . PRO A 754  ? 0.4426 0.7480 0.2464 0.0827  0.0191  -0.0671 752  PRO A CG  
5437  C CD  . PRO A 754  ? 0.3906 0.6756 0.1963 0.0811  0.0206  -0.0643 752  PRO A CD  
5438  N N   . ALA A 755  ? 0.4227 0.7313 0.2508 0.0960  0.0194  -0.1118 753  ALA A N   
5439  C CA  . ALA A 755  ? 0.4354 0.7355 0.2729 0.1002  0.0167  -0.1277 753  ALA A CA  
5440  C C   . ALA A 755  ? 0.4509 0.7421 0.2905 0.1016  0.0116  -0.1361 753  ALA A C   
5441  O O   . ALA A 755  ? 0.4717 0.7471 0.3189 0.1032  0.0090  -0.1454 753  ALA A O   
5442  C CB  . ALA A 755  ? 0.4996 0.8186 0.3423 0.1042  0.0170  -0.1373 753  ALA A CB  
5443  N N   . SER A 756  ? 0.3977 0.6988 0.2314 0.1008  0.0100  -0.1328 754  SER A N   
5444  C CA  . SER A 756  ? 0.4614 0.7543 0.2971 0.1019  0.0052  -0.1402 754  SER A CA  
5445  C C   . SER A 756  ? 0.4376 0.7089 0.2710 0.0986  0.0043  -0.1336 754  SER A C   
5446  O O   . SER A 756  ? 0.4729 0.7323 0.3103 0.0995  0.0002  -0.1412 754  SER A O   
5447  C CB  . SER A 756  ? 0.5125 0.8232 0.3427 0.1022  0.0037  -0.1386 754  SER A CB  
5448  O OG  . SER A 756  ? 0.4613 0.7762 0.2820 0.0980  0.0062  -0.1225 754  SER A OG  
5449  N N   . ALA A 757  ? 0.4384 0.7044 0.2657 0.0949  0.0079  -0.1199 755  ALA A N   
5450  C CA  . ALA A 757  ? 0.3899 0.6362 0.2149 0.0919  0.0073  -0.1133 755  ALA A CA  
5451  C C   . ALA A 757  ? 0.4057 0.6341 0.2376 0.0925  0.0077  -0.1182 755  ALA A C   
5452  O O   . ALA A 757  ? 0.4044 0.6144 0.2378 0.0904  0.0061  -0.1155 755  ALA A O   
5453  C CB  . ALA A 757  ? 0.4006 0.6493 0.2169 0.0875  0.0104  -0.0957 755  ALA A CB  
5454  N N   . LEU A 758  ? 0.4027 0.6350 0.2407 0.0948  0.0096  -0.1246 756  LEU A N   
5455  C CA  . LEU A 758  ? 0.4425 0.6585 0.2873 0.0953  0.0103  -0.1280 756  LEU A CA  
5456  C C   . LEU A 758  ? 0.4306 0.6512 0.2856 0.0995  0.0092  -0.1416 756  LEU A C   
5457  O O   . LEU A 758  ? 0.4002 0.6345 0.2554 0.1006  0.0122  -0.1410 756  LEU A O   
5458  C CB  . LEU A 758  ? 0.4019 0.6139 0.2438 0.0914  0.0149  -0.1139 756  LEU A CB  
5459  C CG  . LEU A 758  ? 0.4079 0.6027 0.2604 0.0908  0.0156  -0.1152 756  LEU A CG  
5460  C CD1 . LEU A 758  ? 0.4056 0.5766 0.2663 0.0886  0.0116  -0.1163 756  LEU A CD1 
5461  C CD2 . LEU A 758  ? 0.4293 0.6226 0.2792 0.0867  0.0200  -0.1008 756  LEU A CD2 
5462  N N   . GLN A 759  ? 0.3709 0.5798 0.2351 0.1016  0.0047  -0.1532 757  GLN A N   
5463  C CA  . GLN A 759  ? 0.4314 0.6421 0.3073 0.1056  0.0024  -0.1666 757  GLN A CA  
5464  C C   . GLN A 759  ? 0.4202 0.6107 0.3056 0.1057  0.0017  -0.1700 757  GLN A C   
5465  O O   . GLN A 759  ? 0.4092 0.5819 0.2961 0.1035  -0.0002 -0.1676 757  GLN A O   
5466  C CB  . GLN A 759  ? 0.4423 0.6567 0.3233 0.1079  -0.0029 -0.1776 757  GLN A CB  
5467  C CG  . GLN A 759  ? 0.3875 0.6241 0.2607 0.1085  -0.0025 -0.1759 757  GLN A CG  
5468  C CD  . GLN A 759  ? 0.4230 0.6628 0.3010 0.1107  -0.0078 -0.1865 757  GLN A CD  
5469  O OE1 . GLN A 759  ? 0.4085 0.6583 0.2940 0.1145  -0.0101 -0.1976 757  GLN A OE1 
5470  N NE2 . GLN A 759  ? 0.3921 0.6239 0.2662 0.1085  -0.0101 -0.1833 757  GLN A NE2 
5471  N N   . LEU A 760  ? 0.4609 0.6542 0.3534 0.1081  0.0030  -0.1748 758  LEU A N   
5472  C CA  . LEU A 760  ? 0.4254 0.6008 0.3283 0.1086  0.0021  -0.1781 758  LEU A CA  
5473  C C   . LEU A 760  ? 0.4056 0.5765 0.3228 0.1119  -0.0036 -0.1922 758  LEU A C   
5474  O O   . LEU A 760  ? 0.4488 0.6346 0.3693 0.1150  -0.0047 -0.1999 758  LEU A O   
5475  C CB  . LEU A 760  ? 0.3966 0.5767 0.2993 0.1091  0.0069  -0.1738 758  LEU A CB  
5476  C CG  . LEU A 760  ? 0.3975 0.5586 0.3123 0.1087  0.0059  -0.1746 758  LEU A CG  
5477  C CD1 . LEU A 760  ? 0.3782 0.5199 0.2921 0.1018  0.0071  -0.1588 758  LEU A CD1 
5478  C CD2 . LEU A 760  ? 0.4137 0.5849 0.3313 0.1118  0.0092  -0.1776 758  LEU A CD2 
5479  N N   . LEU A 761  ? 0.3929 0.5436 0.3191 0.1109  -0.0074 -0.1953 759  LEU A N   
5480  C CA  . LEU A 761  ? 0.4171 0.5610 0.3583 0.1133  -0.0135 -0.2074 759  LEU A CA  
5481  C C   . LEU A 761  ? 0.4116 0.5359 0.3647 0.1128  -0.0149 -0.2080 759  LEU A C   
5482  O O   . LEU A 761  ? 0.4280 0.5345 0.3860 0.1104  -0.0178 -0.2065 759  LEU A O   
5483  C CB  . LEU A 761  ? 0.3897 0.5287 0.3317 0.1120  -0.0182 -0.2106 759  LEU A CB  
5484  C CG  . LEU A 761  ? 0.4701 0.6264 0.4026 0.1125  -0.0184 -0.2113 759  LEU A CG  
5485  C CD1 . LEU A 761  ? 0.4439 0.6218 0.3766 0.1164  -0.0176 -0.2177 759  LEU A CD1 
5486  C CD2 . LEU A 761  ? 0.4489 0.6081 0.3656 0.1092  -0.0142 -0.1988 759  LEU A CD2 
5487  N N   . PRO A 762  ? 0.4286 0.5560 0.3873 0.1151  -0.0132 -0.2100 760  PRO A N   
5488  C CA  . PRO A 762  ? 0.4591 0.5684 0.4308 0.1149  -0.0151 -0.2107 760  PRO A CA  
5489  C C   . PRO A 762  ? 0.4909 0.5894 0.4788 0.1158  -0.0224 -0.2202 760  PRO A C   
5490  O O   . PRO A 762  ? 0.4615 0.5701 0.4528 0.1181  -0.0257 -0.2289 760  PRO A O   
5491  C CB  . PRO A 762  ? 0.4514 0.5710 0.4248 0.1177  -0.0118 -0.2117 760  PRO A CB  
5492  C CG  . PRO A 762  ? 0.4155 0.5577 0.3745 0.1183  -0.0070 -0.2087 760  PRO A CG  
5493  C CD  . PRO A 762  ? 0.3995 0.5478 0.3539 0.1179  -0.0098 -0.2117 760  PRO A CD  
5494  N N   . GLY A 763  ? 0.4184 0.4966 0.4168 0.1138  -0.0251 -0.2181 761  GLY A N   
5495  C CA  . GLY A 763  ? 0.5031 0.5698 0.5180 0.1139  -0.0321 -0.2254 761  GLY A CA  
5496  C C   . GLY A 763  ? 0.5401 0.5849 0.5610 0.1096  -0.0346 -0.2192 761  GLY A C   
5497  O O   . GLY A 763  ? 0.5239 0.5621 0.5368 0.1055  -0.0308 -0.2070 761  GLY A O   
5498  N N   . ASP A 764  ? 0.5662 0.6004 0.6022 0.1089  -0.0412 -0.2244 762  ASP A N   
5499  C CA  . ASP A 764  ? 0.6022 0.6156 0.6473 0.1046  -0.0446 -0.2188 762  ASP A CA  
5500  C C   . ASP A 764  ? 0.5789 0.5896 0.6184 0.1016  -0.0461 -0.2172 762  ASP A C   
5501  O O   . ASP A 764  ? 0.5254 0.5489 0.5508 0.1024  -0.0432 -0.2175 762  ASP A O   
5502  C CB  . ASP A 764  ? 0.6140 0.6175 0.6794 0.1050  -0.0509 -0.2237 762  ASP A CB  
5503  C CG  . ASP A 764  ? 0.6419 0.6554 0.7146 0.1080  -0.0557 -0.2353 762  ASP A CG  
5504  O OD1 . ASP A 764  ? 0.6261 0.6483 0.6913 0.1082  -0.0560 -0.2386 762  ASP A OD1 
5505  O OD2 . ASP A 764  ? 0.6831 0.6962 0.7696 0.1105  -0.0594 -0.2413 762  ASP A OD2 
5506  N N   . GLY A 765  ? 0.6120 0.6064 0.6628 0.0979  -0.0510 -0.2150 763  GLY A N   
5507  C CA  . GLY A 765  ? 0.5888 0.5797 0.6355 0.0944  -0.0526 -0.2126 763  GLY A CA  
5508  C C   . GLY A 765  ? 0.5357 0.5380 0.5829 0.0967  -0.0560 -0.2225 763  GLY A C   
5509  O O   . GLY A 765  ? 0.5719 0.5764 0.6115 0.0950  -0.0562 -0.2215 763  GLY A O   
5510  N N   . ARG A 766  ? 0.5657 0.5757 0.6222 0.1005  -0.0588 -0.2316 764  ARG A N   
5511  C CA  . ARG A 766  ? 0.5600 0.5833 0.6165 0.1032  -0.0617 -0.2411 764  ARG A CA  
5512  C C   . ARG A 766  ? 0.5336 0.5745 0.5711 0.1050  -0.0565 -0.2406 764  ARG A C   
5513  O O   . ARG A 766  ? 0.4980 0.5460 0.5302 0.1049  -0.0578 -0.2433 764  ARG A O   
5514  C CB  . ARG A 766  ? 0.5631 0.5929 0.6323 0.1074  -0.0652 -0.2512 764  ARG A CB  
5515  C CG  . ARG A 766  ? 0.6486 0.6637 0.7381 0.1060  -0.0717 -0.2532 764  ARG A CG  
5516  C CD  . ARG A 766  ? 0.7042 0.7274 0.8041 0.1108  -0.0741 -0.2626 764  ARG A CD  
5517  N NE  . ARG A 766  ? 0.7040 0.7324 0.7972 0.1129  -0.0687 -0.2596 764  ARG A NE  
5518  C CZ  . ARG A 766  ? 0.6921 0.7321 0.7888 0.1176  -0.0687 -0.2670 764  ARG A CZ  
5519  N NH1 . ARG A 766  ? 0.6620 0.7103 0.7691 0.1210  -0.0738 -0.2783 764  ARG A NH1 
5520  N NH2 . ARG A 766  ? 0.7144 0.7582 0.8046 0.1189  -0.0635 -0.2632 764  ARG A NH2 
5521  N N   . VAL A 767  ? 0.5463 0.5949 0.5736 0.1066  -0.0507 -0.2368 765  VAL A N   
5522  C CA  . VAL A 767  ? 0.5265 0.5918 0.5356 0.1077  -0.0454 -0.2340 765  VAL A CA  
5523  C C   . VAL A 767  ? 0.4690 0.5274 0.4673 0.1036  -0.0436 -0.2253 765  VAL A C   
5524  O O   . VAL A 767  ? 0.4642 0.5324 0.4527 0.1035  -0.0433 -0.2254 765  VAL A O   
5525  C CB  . VAL A 767  ? 0.4839 0.5580 0.4858 0.1098  -0.0396 -0.2307 765  VAL A CB  
5526  C CG1 . VAL A 767  ? 0.4607 0.5537 0.4449 0.1108  -0.0345 -0.2275 765  VAL A CG1 
5527  C CG2 . VAL A 767  ? 0.5521 0.6310 0.5663 0.1137  -0.0419 -0.2394 765  VAL A CG2 
5528  N N   . GLY A 768  ? 0.4804 0.5222 0.4808 0.1004  -0.0427 -0.2177 766  GLY A N   
5529  C CA  . GLY A 768  ? 0.4547 0.4898 0.4470 0.0947  -0.0410 -0.2051 766  GLY A CA  
5530  C C   . GLY A 768  ? 0.4346 0.4664 0.4308 0.0936  -0.0462 -0.2103 766  GLY A C   
5531  O O   . GLY A 768  ? 0.4100 0.4471 0.3956 0.0918  -0.0449 -0.2057 766  GLY A O   
5532  N N   . ALA A 769  ? 0.4278 0.4513 0.4402 0.0946  -0.0523 -0.2195 767  ALA A N   
5533  C CA  . ALA A 769  ? 0.4343 0.4538 0.4523 0.0925  -0.0574 -0.2227 767  ALA A CA  
5534  C C   . ALA A 769  ? 0.4671 0.5047 0.4788 0.0956  -0.0581 -0.2299 767  ALA A C   
5535  O O   . ALA A 769  ? 0.4486 0.4881 0.4557 0.0940  -0.0596 -0.2296 767  ALA A O   
5536  C CB  . ALA A 769  ? 0.4028 0.4090 0.4413 0.0912  -0.0635 -0.2265 767  ALA A CB  
5537  N N   . ALA A 770  ? 0.4523 0.5038 0.4641 0.1001  -0.0572 -0.2364 768  ALA A N   
5538  C CA  . ALA A 770  ? 0.4766 0.5470 0.4820 0.1032  -0.0576 -0.2429 768  ALA A CA  
5539  C C   . ALA A 770  ? 0.4358 0.5162 0.4219 0.1023  -0.0528 -0.2356 768  ALA A C   
5540  O O   . ALA A 770  ? 0.4674 0.5571 0.4480 0.1025  -0.0541 -0.2376 768  ALA A O   
5541  C CB  . ALA A 770  ? 0.4723 0.5566 0.4811 0.1080  -0.0570 -0.2505 768  ALA A CB  
5542  N N   . LEU A 771  ? 0.4127 0.4916 0.3888 0.1012  -0.0473 -0.2268 769  LEU A N   
5543  C CA  . LEU A 771  ? 0.4173 0.5056 0.3755 0.1002  -0.0427 -0.2187 769  LEU A CA  
5544  C C   . LEU A 771  ? 0.4245 0.5025 0.3795 0.0964  -0.0444 -0.2136 769  LEU A C   
5545  O O   . LEU A 771  ? 0.4608 0.5484 0.4056 0.0961  -0.0441 -0.2116 769  LEU A O   
5546  C CB  . LEU A 771  ? 0.3955 0.4839 0.3452 0.1000  -0.0367 -0.2105 769  LEU A CB  
5547  C CG  . LEU A 771  ? 0.3989 0.5004 0.3484 0.1036  -0.0335 -0.2133 769  LEU A CG  
5548  C CD1 . LEU A 771  ? 0.4115 0.5080 0.3562 0.1022  -0.0282 -0.2039 769  LEU A CD1 
5549  C CD2 . LEU A 771  ? 0.4232 0.5476 0.3622 0.1060  -0.0317 -0.2147 769  LEU A CD2 
5550  N N   . VAL A 772  ? 0.4142 0.4729 0.3791 0.0922  -0.0460 -0.2081 770  VAL A N   
5551  C CA  . VAL A 772  ? 0.3983 0.4471 0.3625 0.0872  -0.0473 -0.1999 770  VAL A CA  
5552  C C   . VAL A 772  ? 0.4004 0.4538 0.3680 0.0888  -0.0529 -0.2107 770  VAL A C   
5553  O O   . VAL A 772  ? 0.4258 0.4812 0.3865 0.0866  -0.0532 -0.2060 770  VAL A O   
5554  C CB  . VAL A 772  ? 0.3688 0.3975 0.3445 0.0824  -0.0482 -0.1925 770  VAL A CB  
5555  C CG1 . VAL A 772  ? 0.3843 0.4039 0.3619 0.0776  -0.0505 -0.1866 770  VAL A CG1 
5556  C CG2 . VAL A 772  ? 0.4269 0.4521 0.3969 0.0802  -0.0423 -0.1801 770  VAL A CG2 
5557  N N   . ALA A 773  ? 0.4317 0.4871 0.4112 0.0919  -0.0572 -0.2227 771  ALA A N   
5558  C CA  . ALA A 773  ? 0.4106 0.4693 0.3965 0.0920  -0.0624 -0.2297 771  ALA A CA  
5559  C C   . ALA A 773  ? 0.4989 0.5782 0.4739 0.0951  -0.0614 -0.2330 771  ALA A C   
5560  O O   . ALA A 773  ? 0.4805 0.5636 0.4583 0.0952  -0.0653 -0.2377 771  ALA A O   
5561  C CB  . ALA A 773  ? 0.4349 0.4880 0.4397 0.0933  -0.0675 -0.2386 771  ALA A CB  
5562  N N   . ALA A 774  ? 0.4408 0.5337 0.4041 0.0976  -0.0564 -0.2304 772  ALA A N   
5563  C CA  . ALA A 774  ? 0.4661 0.5799 0.4205 0.1006  -0.0556 -0.2334 772  ALA A CA  
5564  C C   . ALA A 774  ? 0.4389 0.5562 0.3822 0.0985  -0.0555 -0.2277 772  ALA A C   
5565  O O   . ALA A 774  ? 0.4185 0.5286 0.3533 0.0955  -0.0529 -0.2180 772  ALA A O   
5566  C CB  . ALA A 774  ? 0.4378 0.5652 0.3825 0.1031  -0.0500 -0.2303 772  ALA A CB  
5567  N N   . ALA A 775  ? 0.4223 0.5514 0.3660 0.1003  -0.0586 -0.2338 773  ALA A N   
5568  C CA  . ALA A 775  ? 0.4277 0.5593 0.3632 0.0983  -0.0596 -0.2294 773  ALA A CA  
5569  C C   . ALA A 775  ? 0.4418 0.5820 0.3598 0.0975  -0.0544 -0.2181 773  ALA A C   
5570  O O   . ALA A 775  ? 0.4612 0.5970 0.3722 0.0947  -0.0545 -0.2110 773  ALA A O   
5571  C CB  . ALA A 775  ? 0.4658 0.6109 0.4045 0.1009  -0.0635 -0.2383 773  ALA A CB  
5572  N N   . GLU A 776  ? 0.4312 0.5835 0.3424 0.0996  -0.0501 -0.2158 774  GLU A N   
5573  C CA  . GLU A 776  ? 0.4427 0.6046 0.3380 0.0987  -0.0453 -0.2045 774  GLU A CA  
5574  C C   . GLU A 776  ? 0.4435 0.5930 0.3342 0.0961  -0.0415 -0.1948 774  GLU A C   
5575  O O   . GLU A 776  ? 0.4350 0.5903 0.3132 0.0949  -0.0378 -0.1842 774  GLU A O   
5576  C CB  . GLU A 776  ? 0.4414 0.6246 0.3311 0.1020  -0.0424 -0.2056 774  GLU A CB  
5577  C CG  . GLU A 776  ? 0.5745 0.7716 0.4690 0.1051  -0.0461 -0.2160 774  GLU A CG  
5578  C CD  . GLU A 776  ? 0.5931 0.7924 0.5001 0.1085  -0.0478 -0.2278 774  GLU A CD  
5579  O OE1 . GLU A 776  ? 0.5230 0.7058 0.4405 0.1078  -0.0491 -0.2312 774  GLU A OE1 
5580  O OE2 . GLU A 776  ? 0.6581 0.8759 0.5645 0.1120  -0.0478 -0.2335 774  GLU A OE2 
5581  N N   . THR A 777  ? 0.4346 0.5676 0.3356 0.0953  -0.0424 -0.1978 775  THR A N   
5582  C CA  . THR A 777  ? 0.4207 0.5397 0.3202 0.0917  -0.0389 -0.1864 775  THR A CA  
5583  C C   . THR A 777  ? 0.4267 0.5363 0.3235 0.0869  -0.0393 -0.1753 775  THR A C   
5584  O O   . THR A 777  ? 0.4329 0.5335 0.3373 0.0854  -0.0436 -0.1790 775  THR A O   
5585  C CB  . THR A 777  ? 0.4109 0.5134 0.3249 0.0909  -0.0402 -0.1904 775  THR A CB  
5586  O OG1 . THR A 777  ? 0.4300 0.5413 0.3466 0.0954  -0.0393 -0.1997 775  THR A OG1 
5587  C CG2 . THR A 777  ? 0.3762 0.4631 0.2911 0.0858  -0.0367 -0.1758 775  THR A CG2 
5588  N N   . ALA A 778  ? 0.4019 0.5140 0.2885 0.0846  -0.0351 -0.1618 776  ALA A N   
5589  C CA  . ALA A 778  ? 0.4075 0.5139 0.2900 0.0808  -0.0354 -0.1514 776  ALA A CA  
5590  C C   . ALA A 778  ? 0.3922 0.4803 0.2795 0.0760  -0.0333 -0.1403 776  ALA A C   
5591  O O   . ALA A 778  ? 0.4605 0.5422 0.3461 0.0729  -0.0337 -0.1322 776  ALA A O   
5592  C CB  . ALA A 778  ? 0.4180 0.5400 0.2864 0.0814  -0.0328 -0.1434 776  ALA A CB  
5593  N N   . GLY A 779  ? 0.4082 0.4884 0.3014 0.0756  -0.0311 -0.1401 777  GLY A N   
5594  C CA  . GLY A 779  ? 0.3635 0.4279 0.2608 0.0713  -0.0289 -0.1299 777  GLY A CA  
5595  C C   . GLY A 779  ? 0.3576 0.4166 0.2616 0.0721  -0.0272 -0.1326 777  GLY A C   
5596  O O   . GLY A 779  ? 0.3939 0.4640 0.2958 0.0758  -0.0261 -0.1390 777  GLY A O   
5597  N N   . VAL A 780  ? 0.3729 0.4159 0.2850 0.0686  -0.0270 -0.1280 778  VAL A N   
5598  C CA  . VAL A 780  ? 0.3891 0.4256 0.3087 0.0690  -0.0257 -0.1297 778  VAL A CA  
5599  C C   . VAL A 780  ? 0.3553 0.3818 0.2738 0.0648  -0.0220 -0.1168 778  VAL A C   
5600  O O   . VAL A 780  ? 0.3598 0.3774 0.2792 0.0611  -0.0226 -0.1099 778  VAL A O   
5601  C CB  . VAL A 780  ? 0.3617 0.3881 0.2954 0.0690  -0.0304 -0.1386 778  VAL A CB  
5602  C CG1 . VAL A 780  ? 0.3994 0.4189 0.3414 0.0694  -0.0293 -0.1397 778  VAL A CG1 
5603  C CG2 . VAL A 780  ? 0.3676 0.4038 0.3032 0.0731  -0.0345 -0.1521 778  VAL A CG2 
5604  N N   . MET A 781  ? 0.3762 0.4048 0.2928 0.0656  -0.0184 -0.1138 779  MET A N   
5605  C CA  . MET A 781  ? 0.3743 0.3931 0.2915 0.0620  -0.0152 -0.1031 779  MET A CA  
5606  C C   . MET A 781  ? 0.3803 0.3915 0.3079 0.0625  -0.0156 -0.1071 779  MET A C   
5607  O O   . MET A 781  ? 0.3612 0.3798 0.2894 0.0660  -0.0148 -0.1132 779  MET A O   
5608  C CB  . MET A 781  ? 0.3782 0.4058 0.2849 0.0621  -0.0107 -0.0950 779  MET A CB  
5609  C CG  . MET A 781  ? 0.3831 0.4186 0.2801 0.0617  -0.0106 -0.0904 779  MET A CG  
5610  S SD  . MET A 781  ? 0.3924 0.4416 0.2778 0.0624  -0.0060 -0.0823 779  MET A SD  
5611  C CE  . MET A 781  ? 0.3524 0.3880 0.2390 0.0575  -0.0033 -0.0691 779  MET A CE  
5612  N N   . PHE A 782  ? 0.3586 0.3558 0.2946 0.0591  -0.0171 -0.1038 780  PHE A N   
5613  C CA  . PHE A 782  ? 0.3749 0.3640 0.3221 0.0592  -0.0184 -0.1072 780  PHE A CA  
5614  C C   . PHE A 782  ? 0.3789 0.3580 0.3276 0.0552  -0.0158 -0.0966 780  PHE A C   
5615  O O   . PHE A 782  ? 0.3467 0.3202 0.2934 0.0515  -0.0154 -0.0890 780  PHE A O   
5616  C CB  . PHE A 782  ? 0.3573 0.3392 0.3158 0.0589  -0.0238 -0.1145 780  PHE A CB  
5617  C CG  . PHE A 782  ? 0.3709 0.3429 0.3422 0.0584  -0.0257 -0.1166 780  PHE A CG  
5618  C CD1 . PHE A 782  ? 0.3568 0.3326 0.3339 0.0626  -0.0269 -0.1259 780  PHE A CD1 
5619  C CD2 . PHE A 782  ? 0.3583 0.3180 0.3363 0.0537  -0.0263 -0.1090 780  PHE A CD2 
5620  C CE1 . PHE A 782  ? 0.3966 0.3630 0.3862 0.0623  -0.0291 -0.1274 780  PHE A CE1 
5621  C CE2 . PHE A 782  ? 0.3819 0.3329 0.3719 0.0531  -0.0283 -0.1100 780  PHE A CE2 
5622  C CZ  . PHE A 782  ? 0.4164 0.3702 0.4125 0.0574  -0.0298 -0.1190 780  PHE A CZ  
5623  N N   . THR A 783  ? 0.3544 0.3321 0.3067 0.0562  -0.0141 -0.0963 781  THR A N   
5624  C CA  . THR A 783  ? 0.3893 0.3571 0.3453 0.0527  -0.0124 -0.0878 781  THR A CA  
5625  C C   . THR A 783  ? 0.3533 0.3154 0.3214 0.0540  -0.0149 -0.0933 781  THR A C   
5626  O O   . THR A 783  ? 0.3810 0.3494 0.3502 0.0579  -0.0145 -0.0998 781  THR A O   
5627  C CB  . THR A 783  ? 0.3645 0.3368 0.3121 0.0523  -0.0074 -0.0802 781  THR A CB  
5628  O OG1 . THR A 783  ? 0.3590 0.3369 0.2961 0.0514  -0.0056 -0.0752 781  THR A OG1 
5629  C CG2 . THR A 783  ? 0.3906 0.3527 0.3424 0.0486  -0.0060 -0.0717 781  THR A CG2 
5630  N N   . GLY A 784  ? 0.3704 0.3213 0.3478 0.0507  -0.0175 -0.0906 782  GLY A N   
5631  C CA  . GLY A 784  ? 0.3728 0.3173 0.3632 0.0516  -0.0207 -0.0954 782  GLY A CA  
5632  C C   . GLY A 784  ? 0.4097 0.3430 0.4094 0.0472  -0.0239 -0.0912 782  GLY A C   
5633  O O   . GLY A 784  ? 0.3803 0.3107 0.3758 0.0432  -0.0224 -0.0830 782  GLY A O   
5634  N N   . SER A 785  ? 0.4154 0.3430 0.4284 0.0479  -0.0284 -0.0969 783  SER A N   
5635  C CA  . SER A 785  ? 0.4555 0.3729 0.4785 0.0434  -0.0317 -0.0923 783  SER A CA  
5636  C C   . SER A 785  ? 0.4355 0.3532 0.4573 0.0414  -0.0338 -0.0934 783  SER A C   
5637  O O   . SER A 785  ? 0.4019 0.3265 0.4189 0.0444  -0.0346 -0.1008 783  SER A O   
5638  C CB  . SER A 785  ? 0.4494 0.3604 0.4882 0.0447  -0.0366 -0.0980 783  SER A CB  
5639  O OG  . SER A 785  ? 0.4779 0.3922 0.5210 0.0483  -0.0405 -0.1099 783  SER A OG  
5640  N N   . THR A 786  ? 0.4305 0.3414 0.4567 0.0363  -0.0348 -0.0857 784  THR A N   
5641  C CA  . THR A 786  ? 0.4558 0.3664 0.4831 0.0340  -0.0373 -0.0864 784  THR A CA  
5642  C C   . THR A 786  ? 0.4503 0.3592 0.4888 0.0358  -0.0431 -0.0967 784  THR A C   
5643  O O   . THR A 786  ? 0.4482 0.3609 0.4847 0.0366  -0.0450 -0.1020 784  THR A O   
5644  C CB  . THR A 786  ? 0.4907 0.3953 0.5218 0.0281  -0.0372 -0.0762 784  THR A CB  
5645  O OG1 . THR A 786  ? 0.5182 0.4247 0.5390 0.0267  -0.0320 -0.0676 784  THR A OG1 
5646  C CG2 . THR A 786  ? 0.5361 0.4415 0.5676 0.0257  -0.0394 -0.0767 784  THR A CG2 
5647  N N   . GLU A 787  ? 0.4494 0.3525 0.5005 0.0367  -0.0464 -0.0998 785  GLU A N   
5648  C CA  . GLU A 787  ? 0.4804 0.3809 0.5443 0.0385  -0.0526 -0.1100 785  GLU A CA  
5649  C C   . GLU A 787  ? 0.4319 0.3418 0.4895 0.0442  -0.0529 -0.1219 785  GLU A C   
5650  O O   . GLU A 787  ? 0.4267 0.3382 0.4879 0.0449  -0.0567 -0.1292 785  GLU A O   
5651  C CB  . GLU A 787  ? 0.5028 0.3957 0.5810 0.0391  -0.0558 -0.1111 785  GLU A CB  
5652  C CG  . GLU A 787  ? 0.6354 0.5228 0.7144 0.0352  -0.0531 -0.0986 785  GLU A CG  
5653  C CD  . GLU A 787  ? 0.7348 0.6170 0.8250 0.0371  -0.0552 -0.1001 785  GLU A CD  
5654  O OE1 . GLU A 787  ? 0.7018 0.5806 0.8051 0.0395  -0.0608 -0.1090 785  GLU A OE1 
5655  O OE2 . GLU A 787  ? 0.7762 0.6578 0.8625 0.0362  -0.0516 -0.0925 785  GLU A OE2 
5656  N N   . VAL A 788  ? 0.4504 0.3674 0.4987 0.0482  -0.0489 -0.1240 786  VAL A N   
5657  C CA  . VAL A 788  ? 0.4194 0.3473 0.4610 0.0537  -0.0489 -0.1350 786  VAL A CA  
5658  C C   . VAL A 788  ? 0.3866 0.3217 0.4152 0.0527  -0.0466 -0.1328 786  VAL A C   
5659  O O   . VAL A 788  ? 0.4307 0.3722 0.4581 0.0553  -0.0491 -0.1416 786  VAL A O   
5660  C CB  . VAL A 788  ? 0.4304 0.3650 0.4659 0.0579  -0.0450 -0.1369 786  VAL A CB  
5661  C CG1 . VAL A 788  ? 0.4294 0.3780 0.4556 0.0631  -0.0440 -0.1466 786  VAL A CG1 
5662  C CG2 . VAL A 788  ? 0.4944 0.4227 0.5444 0.0597  -0.0483 -0.1414 786  VAL A CG2 
5663  N N   . ALA A 789  ? 0.3750 0.3093 0.3943 0.0492  -0.0421 -0.1213 787  ALA A N   
5664  C CA  . ALA A 789  ? 0.4265 0.3667 0.4345 0.0481  -0.0403 -0.1183 787  ALA A CA  
5665  C C   . ALA A 789  ? 0.3918 0.3292 0.4067 0.0462  -0.0451 -0.1219 787  ALA A C   
5666  O O   . ALA A 789  ? 0.3893 0.3340 0.3978 0.0478  -0.0458 -0.1264 787  ALA A O   
5667  C CB  . ALA A 789  ? 0.3813 0.3189 0.3816 0.0442  -0.0357 -0.1054 787  ALA A CB  
5668  N N   A ARG A 790  ? 0.4146 0.3419 0.4427 0.0427  -0.0485 -0.1198 788  ARG A N   
5669  N N   B ARG A 790  ? 0.4148 0.3421 0.4430 0.0427  -0.0485 -0.1198 788  ARG A N   
5670  C CA  A ARG A 790  ? 0.4336 0.3582 0.4697 0.0404  -0.0533 -0.1230 788  ARG A CA  
5671  C CA  B ARG A 790  ? 0.4337 0.3581 0.4699 0.0404  -0.0533 -0.1229 788  ARG A CA  
5672  C C   A ARG A 790  ? 0.4361 0.3644 0.4784 0.0447  -0.0582 -0.1370 788  ARG A C   
5673  C C   B ARG A 790  ? 0.4360 0.3641 0.4786 0.0447  -0.0583 -0.1369 788  ARG A C   
5674  O O   A ARG A 790  ? 0.4311 0.3624 0.4739 0.0447  -0.0612 -0.1419 788  ARG A O   
5675  O O   B ARG A 790  ? 0.4311 0.3620 0.4745 0.0445  -0.0613 -0.1417 788  ARG A O   
5676  C CB  A ARG A 790  ? 0.4647 0.3782 0.5140 0.0352  -0.0558 -0.1163 788  ARG A CB  
5677  C CB  B ARG A 790  ? 0.4647 0.3781 0.5140 0.0352  -0.0557 -0.1160 788  ARG A CB  
5678  C CG  A ARG A 790  ? 0.4947 0.4054 0.5522 0.0317  -0.0601 -0.1169 788  ARG A CG  
5679  C CG  B ARG A 790  ? 0.4947 0.4051 0.5517 0.0313  -0.0598 -0.1158 788  ARG A CG  
5680  C CD  A ARG A 790  ? 0.5041 0.4048 0.5753 0.0264  -0.0626 -0.1095 788  ARG A CD  
5681  C CD  B ARG A 790  ? 0.5054 0.4063 0.5745 0.0257  -0.0614 -0.1070 788  ARG A CD  
5682  N NE  A ARG A 790  ? 0.5147 0.4135 0.5803 0.0232  -0.0577 -0.0973 788  ARG A NE  
5683  N NE  B ARG A 790  ? 0.5163 0.4171 0.5773 0.0221  -0.0564 -0.0947 788  ARG A NE  
5684  C CZ  A ARG A 790  ? 0.5091 0.4101 0.5673 0.0197  -0.0547 -0.0891 788  ARG A CZ  
5685  C CZ  B ARG A 790  ? 0.5082 0.4050 0.5703 0.0206  -0.0540 -0.0873 788  ARG A CZ  
5686  N NH1 A ARG A 790  ? 0.4953 0.4003 0.5504 0.0190  -0.0557 -0.0912 788  ARG A NH1 
5687  N NH1 B ARG A 790  ? 0.5256 0.4177 0.5965 0.0223  -0.0560 -0.0902 788  ARG A NH1 
5688  N NH2 A ARG A 790  ? 0.5134 0.4128 0.5677 0.0171  -0.0507 -0.0791 788  ARG A NH2 
5689  N NH2 B ARG A 790  ? 0.5138 0.4115 0.5686 0.0174  -0.0497 -0.0771 788  ARG A NH2 
5690  N N   . LEU A 791  ? 0.4004 0.3290 0.4478 0.0487  -0.0592 -0.1440 789  LEU A N   
5691  C CA  . LEU A 791  ? 0.4311 0.3649 0.4838 0.0536  -0.0637 -0.1586 789  LEU A CA  
5692  C C   . LEU A 791  ? 0.4013 0.3491 0.4390 0.0575  -0.0612 -0.1637 789  LEU A C   
5693  O O   . LEU A 791  ? 0.4009 0.3544 0.4401 0.0598  -0.0649 -0.1736 789  LEU A O   
5694  C CB  . LEU A 791  ? 0.4456 0.3772 0.5073 0.0573  -0.0652 -0.1651 789  LEU A CB  
5695  C CG  . LEU A 791  ? 0.4522 0.3705 0.5327 0.0546  -0.0700 -0.1639 789  LEU A CG  
5696  C CD1 . LEU A 791  ? 0.4468 0.3645 0.5336 0.0588  -0.0704 -0.1692 789  LEU A CD1 
5697  C CD2 . LEU A 791  ? 0.4644 0.3786 0.5588 0.0538  -0.0773 -0.1721 789  LEU A CD2 
5698  N N   . ILE A 792  ? 0.3780 0.3320 0.4015 0.0582  -0.0551 -0.1570 790  ILE A N   
5699  C CA  . ILE A 792  ? 0.4228 0.3905 0.4318 0.0613  -0.0526 -0.1599 790  ILE A CA  
5700  C C   . ILE A 792  ? 0.4093 0.3779 0.4139 0.0584  -0.0535 -0.1565 790  ILE A C   
5701  O O   . ILE A 792  ? 0.3890 0.3669 0.3890 0.0610  -0.0554 -0.1638 790  ILE A O   
5702  C CB  . ILE A 792  ? 0.3881 0.3615 0.3842 0.0621  -0.0461 -0.1522 790  ILE A CB  
5703  C CG1 . ILE A 792  ? 0.3869 0.3635 0.3864 0.0664  -0.0455 -0.1587 790  ILE A CG1 
5704  C CG2 . ILE A 792  ? 0.3692 0.3554 0.3501 0.0637  -0.0434 -0.1513 790  ILE A CG2 
5705  C CD1 . ILE A 792  ? 0.3911 0.3679 0.3834 0.0657  -0.0397 -0.1492 790  ILE A CD1 
5706  N N   . GLN A 793  ? 0.3665 0.3261 0.3725 0.0531  -0.0524 -0.1456 791  GLN A N   
5707  C CA  . GLN A 793  ? 0.4091 0.3691 0.4122 0.0502  -0.0534 -0.1421 791  GLN A CA  
5708  C C   . GLN A 793  ? 0.3866 0.3470 0.3992 0.0509  -0.0596 -0.1525 791  GLN A C   
5709  O O   . GLN A 793  ? 0.3956 0.3633 0.4023 0.0518  -0.0608 -0.1556 791  GLN A O   
5710  C CB  . GLN A 793  ? 0.3866 0.3366 0.3930 0.0444  -0.0518 -0.1301 791  GLN A CB  
5711  C CG  . GLN A 793  ? 0.3978 0.3481 0.4022 0.0412  -0.0528 -0.1262 791  GLN A CG  
5712  C CD  . GLN A 793  ? 0.4577 0.3989 0.4679 0.0355  -0.0521 -0.1160 791  GLN A CD  
5713  O OE1 . GLN A 793  ? 0.5160 0.4490 0.5379 0.0333  -0.0540 -0.1150 791  GLN A OE1 
5714  N NE2 . GLN A 793  ? 0.4921 0.4352 0.4945 0.0333  -0.0494 -0.1084 791  GLN A NE2 
5715  N N   . ALA A 794  ? 0.4185 0.3711 0.4463 0.0505  -0.0640 -0.1579 792  ALA A N   
5716  C CA  . ALA A 794  ? 0.4294 0.3816 0.4679 0.0510  -0.0705 -0.1681 792  ALA A CA  
5717  C C   . ALA A 794  ? 0.4003 0.3648 0.4337 0.0572  -0.0721 -0.1813 792  ALA A C   
5718  O O   . ALA A 794  ? 0.4245 0.3941 0.4583 0.0579  -0.0757 -0.1879 792  ALA A O   
5719  C CB  . ALA A 794  ? 0.4167 0.3573 0.4738 0.0493  -0.0751 -0.1706 792  ALA A CB  
5720  N N   . GLN A 795  ? 0.3872 0.3576 0.4157 0.0616  -0.0696 -0.1853 793  GLN A N   
5721  C CA  . GLN A 795  ? 0.4171 0.4018 0.4391 0.0676  -0.0704 -0.1973 793  GLN A CA  
5722  C C   . GLN A 795  ? 0.3999 0.3956 0.4065 0.0678  -0.0679 -0.1939 793  GLN A C   
5723  O O   . GLN A 795  ? 0.4272 0.4318 0.4324 0.0703  -0.0712 -0.2030 793  GLN A O   
5724  C CB  . GLN A 795  ? 0.4401 0.4308 0.4576 0.0719  -0.0669 -0.1998 793  GLN A CB  
5725  C CG  . GLN A 795  ? 0.4692 0.4530 0.5018 0.0739  -0.0702 -0.2074 793  GLN A CG  
5726  C CD  . GLN A 795  ? 0.4909 0.4833 0.5174 0.0787  -0.0664 -0.2107 793  GLN A CD  
5727  O OE1 . GLN A 795  ? 0.5595 0.5465 0.5852 0.0772  -0.0626 -0.2021 793  GLN A OE1 
5728  N NE2 . GLN A 795  ? 0.4470 0.4541 0.4697 0.0842  -0.0673 -0.2221 793  GLN A NE2 
5729  N N   . LEU A 796  ? 0.3953 0.3907 0.3908 0.0652  -0.0624 -0.1809 794  LEU A N   
5730  C CA  . LEU A 796  ? 0.3924 0.3983 0.3731 0.0657  -0.0598 -0.1768 794  LEU A CA  
5731  C C   . LEU A 796  ? 0.4449 0.4490 0.4282 0.0629  -0.0634 -0.1766 794  LEU A C   
5732  O O   . LEU A 796  ? 0.3841 0.3990 0.3585 0.0648  -0.0638 -0.1790 794  LEU A O   
5733  C CB  . LEU A 796  ? 0.4107 0.4151 0.3810 0.0633  -0.0536 -0.1629 794  LEU A CB  
5734  C CG  . LEU A 796  ? 0.3896 0.3999 0.3536 0.0663  -0.0493 -0.1623 794  LEU A CG  
5735  C CD1 . LEU A 796  ? 0.3670 0.3741 0.3225 0.0633  -0.0438 -0.1481 794  LEU A CD1 
5736  C CD2 . LEU A 796  ? 0.4153 0.4428 0.3699 0.0715  -0.0493 -0.1704 794  LEU A CD2 
5737  N N   . ALA A 797  ? 0.4062 0.3975 0.4013 0.0585  -0.0658 -0.1733 795  ALA A N   
5738  C CA  . ALA A 797  ? 0.4313 0.4211 0.4296 0.0556  -0.0692 -0.1728 795  ALA A CA  
5739  C C   . ALA A 797  ? 0.4292 0.4258 0.4325 0.0587  -0.0749 -0.1867 795  ALA A C   
5740  O O   . ALA A 797  ? 0.4356 0.4344 0.4391 0.0573  -0.0776 -0.1876 795  ALA A O   
5741  C CB  . ALA A 797  ? 0.4447 0.4204 0.4556 0.0500  -0.0706 -0.1663 795  ALA A CB  
5742  N N   . ASP A 798  ? 0.4213 0.4216 0.4290 0.0631  -0.0770 -0.1980 796  ASP A N   
5743  C CA  . ASP A 798  ? 0.4386 0.4476 0.4501 0.0669  -0.0824 -0.2126 796  ASP A CA  
5744  C C   . ASP A 798  ? 0.4743 0.5000 0.4699 0.0705  -0.0806 -0.2148 796  ASP A C   
5745  O O   . ASP A 798  ? 0.4539 0.4877 0.4508 0.0728  -0.0850 -0.2249 796  ASP A O   
5746  C CB  . ASP A 798  ? 0.4994 0.5088 0.5198 0.0711  -0.0848 -0.2244 796  ASP A CB  
5747  C CG  . ASP A 798  ? 0.6171 0.6124 0.6578 0.0681  -0.0896 -0.2261 796  ASP A CG  
5748  O OD1 . ASP A 798  ? 0.6306 0.6166 0.6785 0.0634  -0.0925 -0.2224 796  ASP A OD1 
5749  O OD2 . ASP A 798  ? 0.5575 0.5517 0.6076 0.0704  -0.0905 -0.2305 796  ASP A OD2 
5750  N N   . ARG A 799  ? 0.4557 0.4869 0.4368 0.0708  -0.0746 -0.2053 797  ARG A N   
5751  C CA  . ARG A 799  ? 0.4586 0.5071 0.4248 0.0748  -0.0727 -0.2074 797  ARG A CA  
5752  C C   . ARG A 799  ? 0.4442 0.4947 0.3989 0.0720  -0.0696 -0.1948 797  ARG A C   
5753  O O   . ARG A 799  ? 0.4165 0.4557 0.3726 0.0675  -0.0673 -0.1835 797  ARG A O   
5754  C CB  . ARG A 799  ? 0.4914 0.5483 0.4504 0.0787  -0.0686 -0.2086 797  ARG A CB  
5755  C CG  . ARG A 799  ? 0.4664 0.5229 0.4364 0.0821  -0.0712 -0.2210 797  ARG A CG  
5756  C CD  . ARG A 799  ? 0.4423 0.5131 0.4042 0.0864  -0.0670 -0.2224 797  ARG A CD  
5757  N NE  . ARG A 799  ? 0.5177 0.5841 0.4733 0.0857  -0.0618 -0.2141 797  ARG A NE  
5758  C CZ  . ARG A 799  ? 0.4846 0.5588 0.4257 0.0852  -0.0565 -0.2037 797  ARG A CZ  
5759  N NH1 . ARG A 799  ? 0.4597 0.5469 0.3893 0.0863  -0.0563 -0.2026 797  ARG A NH1 
5760  N NH2 . ARG A 799  ? 0.4549 0.5235 0.3935 0.0835  -0.0516 -0.1939 797  ARG A NH2 
5761  N N   . LEU A 800  ? 0.4547 0.5203 0.3981 0.0749  -0.0697 -0.1971 798  LEU A N   
5762  C CA  . LEU A 800  ? 0.4655 0.5355 0.3967 0.0733  -0.0667 -0.1855 798  LEU A CA  
5763  C C   . LEU A 800  ? 0.4361 0.5227 0.3533 0.0772  -0.0634 -0.1850 798  LEU A C   
5764  O O   . LEU A 800  ? 0.4542 0.5514 0.3709 0.0815  -0.0645 -0.1958 798  LEU A O   
5765  C CB  . LEU A 800  ? 0.4944 0.5668 0.4261 0.0721  -0.0708 -0.1870 798  LEU A CB  
5766  C CG  . LEU A 800  ? 0.5068 0.5650 0.4514 0.0677  -0.0741 -0.1860 798  LEU A CG  
5767  C CD1 . LEU A 800  ? 0.5019 0.5661 0.4469 0.0677  -0.0788 -0.1905 798  LEU A CD1 
5768  C CD2 . LEU A 800  ? 0.4506 0.4970 0.3948 0.0631  -0.0701 -0.1718 798  LEU A CD2 
5769  N N   . SER A 801  ? 0.4749 0.5640 0.3814 0.0757  -0.0596 -0.1724 799  SER A N   
5770  C CA  . SER A 801  ? 0.5197 0.6256 0.4126 0.0788  -0.0569 -0.1701 799  SER A CA  
5771  C C   . SER A 801  ? 0.5797 0.7003 0.4677 0.0815  -0.0609 -0.1776 799  SER A C   
5772  O O   . SER A 801  ? 0.5670 0.6831 0.4615 0.0804  -0.0653 -0.1818 799  SER A O   
5773  C CB  . SER A 801  ? 0.5553 0.6586 0.4396 0.0759  -0.0525 -0.1541 799  SER A CB  
5774  O OG  . SER A 801  ? 0.5780 0.6800 0.4603 0.0739  -0.0545 -0.1487 799  SER A OG  
5775  N N   . PRO A 802  ? 0.5646 0.7039 0.4415 0.0851  -0.0597 -0.1792 800  PRO A N   
5776  C CA  . PRO A 802  ? 0.5515 0.7052 0.4247 0.0871  -0.0629 -0.1837 800  PRO A CA  
5777  C C   . PRO A 802  ? 0.6255 0.7764 0.4945 0.0848  -0.0651 -0.1766 800  PRO A C   
5778  O O   . PRO A 802  ? 0.5849 0.7411 0.4562 0.0854  -0.0691 -0.1817 800  PRO A O   
5779  C CB  . PRO A 802  ? 0.5515 0.7237 0.4147 0.0896  -0.0591 -0.1799 800  PRO A CB  
5780  C CG  . PRO A 802  ? 0.6418 0.8092 0.4995 0.0887  -0.0542 -0.1717 800  PRO A CG  
5781  C CD  . PRO A 802  ? 0.5761 0.7243 0.4451 0.0870  -0.0548 -0.1756 800  PRO A CD  
5782  N N   . ALA A 803  ? 0.6145 0.7549 0.4814 0.0811  -0.0617 -0.1623 801  ALA A N   
5783  C CA  . ALA A 803  ? 0.6185 0.7530 0.4850 0.0782  -0.0631 -0.1537 801  ALA A CA  
5784  C C   . ALA A 803  ? 0.6345 0.7529 0.5140 0.0752  -0.0661 -0.1571 801  ALA A C   
5785  O O   . ALA A 803  ? 0.6565 0.7700 0.5370 0.0728  -0.0676 -0.1512 801  ALA A O   
5786  C CB  . ALA A 803  ? 0.6071 0.7363 0.4677 0.0756  -0.0585 -0.1378 801  ALA A CB  
5787  N N   . GLY A 804  ? 0.5926 0.7032 0.4825 0.0752  -0.0671 -0.1661 802  GLY A N   
5788  C CA  . GLY A 804  ? 0.5435 0.6396 0.4465 0.0721  -0.0701 -0.1688 802  GLY A CA  
5789  C C   . GLY A 804  ? 0.5486 0.6283 0.4562 0.0676  -0.0668 -0.1578 802  GLY A C   
5790  O O   . GLY A 804  ? 0.5554 0.6256 0.4703 0.0644  -0.0687 -0.1555 802  GLY A O   
5791  N N   . ARG A 805  ? 0.5449 0.6217 0.4486 0.0674  -0.0620 -0.1512 803  ARG A N   
5792  C CA  . ARG A 805  ? 0.4951 0.5578 0.4021 0.0635  -0.0586 -0.1407 803  ARG A CA  
5793  C C   . ARG A 805  ? 0.4174 0.4722 0.3310 0.0632  -0.0566 -0.1433 803  ARG A C   
5794  O O   . ARG A 805  ? 0.4580 0.5199 0.3708 0.0666  -0.0567 -0.1513 803  ARG A O   
5795  C CB  . ARG A 805  ? 0.5177 0.5840 0.4135 0.0631  -0.0545 -0.1283 803  ARG A CB  
5796  C CG  . ARG A 805  ? 0.5531 0.6265 0.4428 0.0633  -0.0566 -0.1245 803  ARG A CG  
5797  C CD  . ARG A 805  ? 0.5436 0.6085 0.4423 0.0606  -0.0599 -0.1258 803  ARG A CD  
5798  N NE  . ARG A 805  ? 0.5758 0.6431 0.4699 0.0598  -0.0607 -0.1183 803  ARG A NE  
5799  C CZ  . ARG A 805  ? 0.5200 0.5947 0.4132 0.0609  -0.0647 -0.1221 803  ARG A CZ  
5800  N NH1 . ARG A 805  ? 0.6071 0.6884 0.5034 0.0629  -0.0685 -0.1339 803  ARG A NH1 
5801  N NH2 . ARG A 805  ? 0.5921 0.6677 0.4819 0.0601  -0.0653 -0.1144 803  ARG A NH2 
5802  N N   . PRO A 806  ? 0.4340 0.4747 0.3547 0.0594  -0.0550 -0.1370 804  PRO A N   
5803  C CA  . PRO A 806  ? 0.4428 0.4756 0.3707 0.0590  -0.0536 -0.1392 804  PRO A CA  
5804  C C   . PRO A 806  ? 0.4518 0.4903 0.3711 0.0612  -0.0491 -0.1359 804  PRO A C   
5805  O O   . PRO A 806  ? 0.4084 0.4520 0.3175 0.0613  -0.0460 -0.1274 804  PRO A O   
5806  C CB  . PRO A 806  ? 0.4537 0.4722 0.3886 0.0541  -0.0524 -0.1307 804  PRO A CB  
5807  C CG  . PRO A 806  ? 0.4808 0.4995 0.4158 0.0522  -0.0547 -0.1282 804  PRO A CG  
5808  C CD  . PRO A 806  ? 0.4437 0.4757 0.3667 0.0554  -0.0547 -0.1282 804  PRO A CD  
5809  N N   . ILE A 807  ? 0.4052 0.4429 0.3295 0.0631  -0.0489 -0.1426 805  ILE A N   
5810  C CA  . ILE A 807  ? 0.4082 0.4509 0.3264 0.0651  -0.0447 -0.1404 805  ILE A CA  
5811  C C   . ILE A 807  ? 0.4364 0.4674 0.3558 0.0615  -0.0408 -0.1291 805  ILE A C   
5812  O O   . ILE A 807  ? 0.4162 0.4350 0.3459 0.0590  -0.0417 -0.1291 805  ILE A O   
5813  C CB  . ILE A 807  ? 0.4301 0.4757 0.3545 0.0686  -0.0462 -0.1522 805  ILE A CB  
5814  C CG1 . ILE A 807  ? 0.4400 0.4969 0.3648 0.0723  -0.0508 -0.1650 805  ILE A CG1 
5815  C CG2 . ILE A 807  ? 0.3716 0.4236 0.2894 0.0708  -0.0416 -0.1497 805  ILE A CG2 
5816  C CD1 . ILE A 807  ? 0.4326 0.5067 0.3436 0.0750  -0.0498 -0.1643 805  ILE A CD1 
5817  N N   . PRO A 808  ? 0.4217 0.4562 0.3313 0.0610  -0.0367 -0.1193 806  PRO A N   
5818  C CA  . PRO A 808  ? 0.3866 0.4104 0.2974 0.0576  -0.0332 -0.1090 806  PRO A CA  
5819  C C   . PRO A 808  ? 0.4133 0.4318 0.3304 0.0580  -0.0317 -0.1116 806  PRO A C   
5820  O O   . PRO A 808  ? 0.4059 0.4326 0.3212 0.0614  -0.0310 -0.1177 806  PRO A O   
5821  C CB  . PRO A 808  ? 0.3957 0.4271 0.2948 0.0579  -0.0296 -0.0999 806  PRO A CB  
5822  C CG  . PRO A 808  ? 0.4245 0.4684 0.3168 0.0603  -0.0320 -0.1034 806  PRO A CG  
5823  C CD  . PRO A 808  ? 0.3712 0.4198 0.2686 0.0632  -0.0355 -0.1168 806  PRO A CD  
5824  N N   . LEU A 809  ? 0.4256 0.4310 0.3502 0.0545  -0.0311 -0.1068 807  LEU A N   
5825  C CA  . LEU A 809  ? 0.3896 0.3886 0.3206 0.0543  -0.0297 -0.1075 807  LEU A CA  
5826  C C   . LEU A 809  ? 0.3920 0.3837 0.3210 0.0510  -0.0259 -0.0959 807  LEU A C   
5827  O O   . LEU A 809  ? 0.3480 0.3325 0.2792 0.0475  -0.0262 -0.0902 807  LEU A O   
5828  C CB  . LEU A 809  ? 0.3932 0.3831 0.3376 0.0531  -0.0337 -0.1139 807  LEU A CB  
5829  C CG  . LEU A 809  ? 0.4176 0.3988 0.3700 0.0521  -0.0326 -0.1124 807  LEU A CG  
5830  C CD1 . LEU A 809  ? 0.3720 0.3604 0.3225 0.0563  -0.0311 -0.1183 807  LEU A CD1 
5831  C CD2 . LEU A 809  ? 0.4447 0.4160 0.4111 0.0500  -0.0368 -0.1163 807  LEU A CD2 
5832  N N   . ILE A 810  ? 0.3508 0.3452 0.2757 0.0520  -0.0222 -0.0928 808  ILE A N   
5833  C CA  . ILE A 810  ? 0.3786 0.3655 0.3034 0.0491  -0.0189 -0.0832 808  ILE A CA  
5834  C C   . ILE A 810  ? 0.3674 0.3474 0.3015 0.0490  -0.0191 -0.0862 808  ILE A C   
5835  O O   . ILE A 810  ? 0.3717 0.3568 0.3060 0.0520  -0.0184 -0.0915 808  ILE A O   
5836  C CB  . ILE A 810  ? 0.3457 0.3396 0.2605 0.0499  -0.0148 -0.0766 808  ILE A CB  
5837  C CG1 . ILE A 810  ? 0.3769 0.3782 0.2830 0.0502  -0.0150 -0.0732 808  ILE A CG1 
5838  C CG2 . ILE A 810  ? 0.3882 0.3736 0.3040 0.0467  -0.0118 -0.0672 808  ILE A CG2 
5839  C CD1 . ILE A 810  ? 0.4440 0.4514 0.3412 0.0503  -0.0114 -0.0653 808  ILE A CD1 
5840  N N   . ALA A 811  ? 0.4048 0.3740 0.3469 0.0455  -0.0201 -0.0829 809  ALA A N   
5841  C CA  . ALA A 811  ? 0.3870 0.3489 0.3390 0.0450  -0.0210 -0.0851 809  ALA A CA  
5842  C C   . ALA A 811  ? 0.4247 0.3792 0.3775 0.0414  -0.0182 -0.0753 809  ALA A C   
5843  O O   . ALA A 811  ? 0.3773 0.3265 0.3316 0.0379  -0.0185 -0.0699 809  ALA A O   
5844  C CB  . ALA A 811  ? 0.4246 0.3810 0.3877 0.0441  -0.0259 -0.0913 809  ALA A CB  
5845  N N   . GLU A 812  ? 0.3851 0.3399 0.3370 0.0424  -0.0155 -0.0733 810  GLU A N   
5846  C CA  . GLU A 812  ? 0.3670 0.3154 0.3197 0.0393  -0.0129 -0.0647 810  GLU A CA  
5847  C C   . GLU A 812  ? 0.4008 0.3429 0.3641 0.0390  -0.0143 -0.0669 810  GLU A C   
5848  O O   . GLU A 812  ? 0.3823 0.3274 0.3480 0.0423  -0.0148 -0.0730 810  GLU A O   
5849  C CB  . GLU A 812  ? 0.4219 0.3759 0.3652 0.0402  -0.0086 -0.0595 810  GLU A CB  
5850  C CG  . GLU A 812  ? 0.4291 0.3893 0.3629 0.0404  -0.0079 -0.0572 810  GLU A CG  
5851  C CD  . GLU A 812  ? 0.4821 0.4369 0.4160 0.0369  -0.0085 -0.0514 810  GLU A CD  
5852  O OE1 . GLU A 812  ? 0.5207 0.4713 0.4540 0.0344  -0.0063 -0.0442 810  GLU A OE1 
5853  O OE2 . GLU A 812  ? 0.4322 0.3874 0.3671 0.0367  -0.0112 -0.0544 810  GLU A OE2 
5854  N N   . THR A 813  ? 0.3880 0.3219 0.3582 0.0352  -0.0155 -0.0623 811  THR A N   
5855  C CA  . THR A 813  ? 0.3873 0.3146 0.3694 0.0345  -0.0181 -0.0642 811  THR A CA  
5856  C C   . THR A 813  ? 0.4334 0.3554 0.4171 0.0313  -0.0159 -0.0553 811  THR A C   
5857  O O   . THR A 813  ? 0.4180 0.3422 0.3938 0.0305  -0.0122 -0.0494 811  THR A O   
5858  C CB  . THR A 813  ? 0.4004 0.3240 0.3907 0.0330  -0.0227 -0.0680 811  THR A CB  
5859  O OG1 . THR A 813  ? 0.4339 0.3570 0.4207 0.0296  -0.0222 -0.0624 811  THR A OG1 
5860  C CG2 . THR A 813  ? 0.3732 0.3027 0.3629 0.0371  -0.0252 -0.0785 811  THR A CG2 
5861  N N   . GLY A 814  ? 0.4314 0.3467 0.4259 0.0293  -0.0184 -0.0543 812  GLY A N   
5862  C CA  . GLY A 814  ? 0.4574 0.3688 0.4540 0.0268  -0.0165 -0.0467 812  GLY A CA  
5863  C C   . GLY A 814  ? 0.4517 0.3619 0.4453 0.0225  -0.0150 -0.0384 812  GLY A C   
5864  O O   . GLY A 814  ? 0.4547 0.3670 0.4442 0.0215  -0.0151 -0.0381 812  GLY A O   
5865  N N   . GLY A 815  ? 0.3679 0.2752 0.3639 0.0201  -0.0136 -0.0318 813  GLY A N   
5866  C CA  . GLY A 815  ? 0.3950 0.3016 0.3899 0.0159  -0.0126 -0.0243 813  GLY A CA  
5867  C C   . GLY A 815  ? 0.3908 0.2932 0.3939 0.0131  -0.0136 -0.0190 813  GLY A C   
5868  O O   . GLY A 815  ? 0.4571 0.3574 0.4644 0.0147  -0.0139 -0.0198 813  GLY A O   
5869  N N   . GLN A 816  ? 0.4191 0.3209 0.4249 0.0089  -0.0141 -0.0134 814  GLN A N   
5870  C CA  . GLN A 816  ? 0.4269 0.3265 0.4392 0.0056  -0.0146 -0.0065 814  GLN A CA  
5871  C C   . GLN A 816  ? 0.3932 0.2968 0.3976 0.0038  -0.0108 -0.0005 814  GLN A C   
5872  O O   . GLN A 816  ? 0.3630 0.2688 0.3674 0.0004  -0.0105 0.0042  814  GLN A O   
5873  C CB  . GLN A 816  ? 0.4429 0.3403 0.4652 0.0019  -0.0183 -0.0044 814  GLN A CB  
5874  C CG  . GLN A 816  ? 0.4827 0.3775 0.5146 -0.0013 -0.0201 0.0022  814  GLN A CG  
5875  C CD  . GLN A 816  ? 0.5425 0.4319 0.5827 0.0011  -0.0228 -0.0012 814  GLN A CD  
5876  O OE1 . GLN A 816  ? 0.5435 0.4331 0.5797 0.0044  -0.0208 -0.0033 814  GLN A OE1 
5877  N NE2 . GLN A 816  ? 0.4937 0.3786 0.5463 -0.0004 -0.0275 -0.0018 814  GLN A NE2 
5878  N N   . ASN A 817  ? 0.3633 0.2682 0.3611 0.0063  -0.0079 -0.0009 815  ASN A N   
5879  C CA  . ASN A 817  ? 0.3461 0.2547 0.3352 0.0057  -0.0044 0.0026  815  ASN A CA  
5880  C C   . ASN A 817  ? 0.3382 0.2476 0.3294 0.0026  -0.0035 0.0096  815  ASN A C   
5881  O O   . ASN A 817  ? 0.3347 0.2420 0.3315 0.0022  -0.0043 0.0117  815  ASN A O   
5882  C CB  . ASN A 817  ? 0.3268 0.2367 0.3089 0.0093  -0.0019 -0.0001 815  ASN A CB  
5883  C CG  . ASN A 817  ? 0.3467 0.2569 0.3272 0.0126  -0.0030 -0.0071 815  ASN A CG  
5884  O OD1 . ASN A 817  ? 0.3483 0.2598 0.3267 0.0125  -0.0039 -0.0092 815  ASN A OD1 
5885  N ND2 . ASN A 817  ? 0.3162 0.2260 0.2978 0.0157  -0.0030 -0.0109 815  ASN A ND2 
5886  N N   . ALA A 818  ? 0.3413 0.2546 0.3284 0.0004  -0.0020 0.0129  816  ALA A N   
5887  C CA  . ALA A 818  ? 0.3133 0.2293 0.3019 -0.0027 -0.0012 0.0191  816  ALA A CA  
5888  C C   . ALA A 818  ? 0.2974 0.2166 0.2782 -0.0020 0.0020  0.0204  816  ALA A C   
5889  O O   . ALA A 818  ? 0.2864 0.2063 0.2607 0.0001  0.0034  0.0173  816  ALA A O   
5890  C CB  . ALA A 818  ? 0.3321 0.2515 0.3240 -0.0063 -0.0025 0.0219  816  ALA A CB  
5891  N N   . MET A 819  ? 0.3153 0.2368 0.2973 -0.0039 0.0028  0.0252  817  MET A N   
5892  C CA  . MET A 819  ? 0.3005 0.2258 0.2765 -0.0040 0.0053  0.0267  817  MET A CA  
5893  C C   . MET A 819  ? 0.2929 0.2237 0.2711 -0.0076 0.0052  0.0315  817  MET A C   
5894  O O   . MET A 819  ? 0.3173 0.2484 0.3015 -0.0098 0.0038  0.0355  817  MET A O   
5895  C CB  . MET A 819  ? 0.3233 0.2469 0.2977 -0.0023 0.0067  0.0272  817  MET A CB  
5896  C CG  . MET A 819  ? 0.3304 0.2578 0.3000 -0.0026 0.0089  0.0289  817  MET A CG  
5897  S SD  . MET A 819  ? 0.3801 0.3062 0.3493 -0.0012 0.0102  0.0303  817  MET A SD  
5898  C CE  . MET A 819  ? 0.3476 0.2703 0.3128 0.0025  0.0112  0.0255  817  MET A CE  
5899  N N   . ILE A 820  ? 0.2873 0.2231 0.2612 -0.0081 0.0065  0.0311  818  ILE A N   
5900  C CA  . ILE A 820  ? 0.2718 0.2150 0.2469 -0.0112 0.0067  0.0349  818  ILE A CA  
5901  C C   . ILE A 820  ? 0.2853 0.2319 0.2563 -0.0107 0.0086  0.0356  818  ILE A C   
5902  O O   . ILE A 820  ? 0.2943 0.2394 0.2605 -0.0084 0.0098  0.0322  818  ILE A O   
5903  C CB  . ILE A 820  ? 0.2824 0.2301 0.2567 -0.0121 0.0064  0.0333  818  ILE A CB  
5904  C CG1 . ILE A 820  ? 0.3452 0.2901 0.3246 -0.0131 0.0042  0.0330  818  ILE A CG1 
5905  C CG2 . ILE A 820  ? 0.3347 0.2922 0.3096 -0.0150 0.0071  0.0367  818  ILE A CG2 
5906  C CD1 . ILE A 820  ? 0.3226 0.2724 0.3021 -0.0143 0.0038  0.0316  818  ILE A CD1 
5907  N N   . VAL A 821  ? 0.2827 0.2339 0.2560 -0.0130 0.0086  0.0401  819  VAL A N   
5908  C CA  . VAL A 821  ? 0.2906 0.2455 0.2609 -0.0127 0.0101  0.0409  819  VAL A CA  
5909  C C   . VAL A 821  ? 0.3193 0.2846 0.2901 -0.0155 0.0103  0.0435  819  VAL A C   
5910  O O   . VAL A 821  ? 0.3092 0.2783 0.2843 -0.0183 0.0091  0.0480  819  VAL A O   
5911  C CB  . VAL A 821  ? 0.3017 0.2533 0.2745 -0.0126 0.0099  0.0440  819  VAL A CB  
5912  C CG1 . VAL A 821  ? 0.3213 0.2773 0.2914 -0.0126 0.0112  0.0448  819  VAL A CG1 
5913  C CG2 . VAL A 821  ? 0.2859 0.2288 0.2588 -0.0098 0.0097  0.0410  819  VAL A CG2 
5914  N N   . ASP A 822  ? 0.3280 0.2983 0.2947 -0.0147 0.0115  0.0407  820  ASP A N   
5915  C CA  . ASP A 822  ? 0.3241 0.3060 0.2911 -0.0170 0.0117  0.0424  820  ASP A CA  
5916  C C   . ASP A 822  ? 0.3078 0.2942 0.2734 -0.0172 0.0124  0.0437  820  ASP A C   
5917  O O   . ASP A 822  ? 0.3234 0.3037 0.2882 -0.0157 0.0127  0.0434  820  ASP A O   
5918  C CB  . ASP A 822  ? 0.3335 0.3202 0.2984 -0.0162 0.0121  0.0378  820  ASP A CB  
5919  C CG  . ASP A 822  ? 0.3479 0.3333 0.3089 -0.0133 0.0128  0.0324  820  ASP A CG  
5920  O OD1 . ASP A 822  ? 0.3843 0.3667 0.3440 -0.0122 0.0133  0.0323  820  ASP A OD1 
5921  O OD2 . ASP A 822  ? 0.3645 0.3523 0.3245 -0.0121 0.0127  0.0282  820  ASP A OD2 
5922  N N   . SER A 823  ? 0.3557 0.3540 0.3212 -0.0191 0.0127  0.0450  821  SER A N   
5923  C CA  . SER A 823  ? 0.3516 0.3559 0.3162 -0.0197 0.0130  0.0467  821  SER A CA  
5924  C C   . SER A 823  ? 0.3545 0.3571 0.3158 -0.0170 0.0137  0.0411  821  SER A C   
5925  O O   . SER A 823  ? 0.3991 0.4055 0.3599 -0.0171 0.0139  0.0418  821  SER A O   
5926  C CB  . SER A 823  ? 0.3604 0.3796 0.3257 -0.0226 0.0130  0.0497  821  SER A CB  
5927  O OG  . SER A 823  ? 0.3878 0.4136 0.3512 -0.0218 0.0136  0.0445  821  SER A OG  
5928  N N   . SER A 824  ? 0.3129 0.3102 0.2725 -0.0146 0.0139  0.0357  822  SER A N   
5929  C CA  . SER A 824  ? 0.3209 0.3154 0.2785 -0.0121 0.0141  0.0309  822  SER A CA  
5930  C C   . SER A 824  ? 0.3892 0.3724 0.3464 -0.0105 0.0143  0.0314  822  SER A C   
5931  O O   . SER A 824  ? 0.3801 0.3611 0.3364 -0.0090 0.0144  0.0288  822  SER A O   
5932  C CB  . SER A 824  ? 0.3620 0.3568 0.3187 -0.0102 0.0139  0.0252  822  SER A CB  
5933  O OG  . SER A 824  ? 0.3536 0.3386 0.3099 -0.0090 0.0137  0.0247  822  SER A OG  
5934  N N   . ALA A 825  ? 0.3692 0.3458 0.3277 -0.0108 0.0142  0.0346  823  ALA A N   
5935  C CA  . ALA A 825  ? 0.3750 0.3421 0.3331 -0.0091 0.0146  0.0347  823  ALA A CA  
5936  C C   . ALA A 825  ? 0.3559 0.3242 0.3149 -0.0097 0.0148  0.0373  823  ALA A C   
5937  O O   . ALA A 825  ? 0.3740 0.3493 0.3343 -0.0116 0.0145  0.0403  823  ALA A O   
5938  C CB  . ALA A 825  ? 0.3514 0.3124 0.3112 -0.0091 0.0142  0.0366  823  ALA A CB  
5939  N N   . LEU A 826  ? 0.4010 0.3632 0.3593 -0.0080 0.0154  0.0364  824  LEU A N   
5940  C CA  . LEU A 826  ? 0.3984 0.3611 0.3579 -0.0083 0.0156  0.0387  824  LEU A CA  
5941  C C   . LEU A 826  ? 0.3978 0.3561 0.3598 -0.0083 0.0154  0.0423  824  LEU A C   
5942  O O   . LEU A 826  ? 0.3854 0.3370 0.3473 -0.0067 0.0157  0.0412  824  LEU A O   
5943  C CB  . LEU A 826  ? 0.4041 0.3634 0.3624 -0.0067 0.0162  0.0363  824  LEU A CB  
5944  N N   . ALA A 827  ? 0.3916 0.3544 0.3562 -0.0101 0.0148  0.0464  825  ALA A N   
5945  C CA  . ALA A 827  ? 0.3871 0.3461 0.3556 -0.0103 0.0140  0.0499  825  ALA A CA  
5946  C C   . ALA A 827  ? 0.3813 0.3334 0.3503 -0.0079 0.0146  0.0486  825  ALA A C   
5947  O O   . ALA A 827  ? 0.3557 0.3022 0.3264 -0.0067 0.0143  0.0480  825  ALA A O   
5948  C CB  . ALA A 827  ? 0.4653 0.4307 0.4368 -0.0126 0.0129  0.0551  825  ALA A CB  
5949  N N   . GLU A 828  ? 0.3608 0.3139 0.3286 -0.0072 0.0155  0.0480  826  GLU A N   
5950  C CA  . GLU A 828  ? 0.3796 0.3277 0.3480 -0.0052 0.0164  0.0471  826  GLU A CA  
5951  C C   . GLU A 828  ? 0.3653 0.3080 0.3314 -0.0032 0.0171  0.0437  826  GLU A C   
5952  O O   . GLU A 828  ? 0.3649 0.3037 0.3324 -0.0015 0.0174  0.0430  826  GLU A O   
5953  C CB  . GLU A 828  ? 0.4460 0.3965 0.4133 -0.0051 0.0172  0.0467  826  GLU A CB  
5954  C CG  . GLU A 828  ? 0.4894 0.4446 0.4595 -0.0064 0.0165  0.0501  826  GLU A CG  
5955  C CD  . GLU A 828  ? 0.5109 0.4735 0.4804 -0.0086 0.0155  0.0515  826  GLU A CD  
5956  O OE1 . GLU A 828  ? 0.4915 0.4556 0.4586 -0.0092 0.0155  0.0494  826  GLU A OE1 
5957  O OE2 . GLU A 828  ? 0.5370 0.5046 0.5085 -0.0099 0.0147  0.0547  826  GLU A OE2 
5958  N N   . GLN A 829  ? 0.3892 0.3324 0.3520 -0.0033 0.0174  0.0412  827  GLN A N   
5959  C CA  . GLN A 829  ? 0.3982 0.3371 0.3584 -0.0016 0.0179  0.0383  827  GLN A CA  
5960  C C   . GLN A 829  ? 0.3880 0.3243 0.3496 -0.0012 0.0170  0.0379  827  GLN A C   
5961  O O   . GLN A 829  ? 0.3547 0.2873 0.3160 0.0007  0.0173  0.0361  827  GLN A O   
5962  C CB  . GLN A 829  ? 0.4333 0.3737 0.3907 -0.0019 0.0179  0.0361  827  GLN A CB  
5963  C CG  . GLN A 829  ? 0.4823 0.4189 0.4370 -0.0002 0.0183  0.0337  827  GLN A CG  
5964  C CD  . GLN A 829  ? 0.5480 0.4858 0.5010 -0.0004 0.0178  0.0317  827  GLN A CD  
5965  O OE1 . GLN A 829  ? 0.5609 0.5027 0.5147 -0.0016 0.0173  0.0315  827  GLN A OE1 
5966  N NE2 . GLN A 829  ? 0.5641 0.4989 0.5149 0.0009  0.0177  0.0301  827  GLN A NE2 
5967  N N   . VAL A 830  ? 0.3557 0.2947 0.3191 -0.0031 0.0159  0.0394  828  VAL A N   
5968  C CA  . VAL A 830  ? 0.3655 0.3021 0.3315 -0.0033 0.0146  0.0395  828  VAL A CA  
5969  C C   . VAL A 830  ? 0.3680 0.3010 0.3382 -0.0021 0.0140  0.0403  828  VAL A C   
5970  O O   . VAL A 830  ? 0.3335 0.2625 0.3047 -0.0004 0.0135  0.0379  828  VAL A O   
5971  C CB  . VAL A 830  ? 0.3088 0.2502 0.2770 -0.0061 0.0134  0.0423  828  VAL A CB  
5972  C CG1 . VAL A 830  ? 0.3288 0.2675 0.3017 -0.0068 0.0116  0.0436  828  VAL A CG1 
5973  C CG2 . VAL A 830  ? 0.3337 0.2786 0.2982 -0.0066 0.0139  0.0400  828  VAL A CG2 
5974  N N   . VAL A 831  ? 0.3205 0.2553 0.2936 -0.0028 0.0138  0.0435  829  VAL A N   
5975  C CA  . VAL A 831  ? 0.3109 0.2425 0.2893 -0.0016 0.0127  0.0444  829  VAL A CA  
5976  C C   . VAL A 831  ? 0.2989 0.2272 0.2757 0.0015  0.0140  0.0405  829  VAL A C   
5977  O O   . VAL A 831  ? 0.3304 0.2552 0.3105 0.0034  0.0130  0.0383  829  VAL A O   
5978  C CB  . VAL A 831  ? 0.2917 0.2264 0.2734 -0.0029 0.0122  0.0488  829  VAL A CB  
5979  C CG1 . VAL A 831  ? 0.2916 0.2227 0.2788 -0.0010 0.0112  0.0489  829  VAL A CG1 
5980  C CG2 . VAL A 831  ? 0.3190 0.2575 0.3033 -0.0061 0.0105  0.0533  829  VAL A CG2 
5981  N N   . GLY A 832  ? 0.2870 0.2169 0.2592 0.0023  0.0160  0.0394  830  GLY A N   
5982  C CA  . GLY A 832  ? 0.3103 0.2386 0.2807 0.0050  0.0173  0.0363  830  GLY A CA  
5983  C C   . GLY A 832  ? 0.3488 0.2747 0.3171 0.0064  0.0171  0.0326  830  GLY A C   
5984  O O   . GLY A 832  ? 0.3236 0.2482 0.2931 0.0088  0.0171  0.0297  830  GLY A O   
5985  N N   . ASP A 833  ? 0.2852 0.2113 0.2504 0.0051  0.0168  0.0323  831  ASP A N   
5986  C CA  . ASP A 833  ? 0.3448 0.2691 0.3080 0.0065  0.0164  0.0289  831  ASP A CA  
5987  C C   . ASP A 833  ? 0.2967 0.2185 0.2650 0.0067  0.0143  0.0277  831  ASP A C   
5988  O O   . ASP A 833  ? 0.3199 0.2401 0.2880 0.0087  0.0138  0.0239  831  ASP A O   
5989  C CB  . ASP A 833  ? 0.3330 0.2584 0.2924 0.0051  0.0165  0.0288  831  ASP A CB  
5990  C CG  . ASP A 833  ? 0.3727 0.2995 0.3279 0.0053  0.0180  0.0292  831  ASP A CG  
5991  O OD1 . ASP A 833  ? 0.3783 0.3054 0.3327 0.0067  0.0193  0.0292  831  ASP A OD1 
5992  O OD2 . ASP A 833  ? 0.3613 0.2894 0.3146 0.0041  0.0178  0.0294  831  ASP A OD2 
5993  N N   . VAL A 834  ? 0.2918 0.2137 0.2650 0.0046  0.0129  0.0309  832  VAL A N   
5994  C CA  . VAL A 834  ? 0.2962 0.2152 0.2757 0.0044  0.0103  0.0306  832  VAL A CA  
5995  C C   . VAL A 834  ? 0.3244 0.2410 0.3084 0.0071  0.0097  0.0284  832  VAL A C   
5996  O O   . VAL A 834  ? 0.3254 0.2393 0.3125 0.0088  0.0082  0.0245  832  VAL A O   
5997  C CB  . VAL A 834  ? 0.3283 0.2489 0.3120 0.0010  0.0088  0.0358  832  VAL A CB  
5998  C CG1 . VAL A 834  ? 0.3072 0.2245 0.2993 0.0006  0.0058  0.0366  832  VAL A CG1 
5999  C CG2 . VAL A 834  ? 0.3013 0.2250 0.2814 -0.0013 0.0091  0.0367  832  VAL A CG2 
6000  N N   . ILE A 835  ? 0.2778 0.1958 0.2625 0.0075  0.0107  0.0304  833  ILE A N   
6001  C CA  . ILE A 835  ? 0.3172 0.2339 0.3064 0.0104  0.0103  0.0280  833  ILE A CA  
6002  C C   . ILE A 835  ? 0.3339 0.2511 0.3194 0.0137  0.0116  0.0221  833  ILE A C   
6003  O O   . ILE A 835  ? 0.3539 0.2694 0.3437 0.0162  0.0101  0.0179  833  ILE A O   
6004  C CB  . ILE A 835  ? 0.3335 0.2528 0.3231 0.0103  0.0116  0.0311  833  ILE A CB  
6005  C CG1 . ILE A 835  ? 0.3244 0.2437 0.3192 0.0075  0.0097  0.0367  833  ILE A CG1 
6006  C CG2 . ILE A 835  ? 0.3313 0.2508 0.3239 0.0138  0.0120  0.0277  833  ILE A CG2 
6007  C CD1 . ILE A 835  ? 0.3634 0.2790 0.3676 0.0081  0.0064  0.0371  833  ILE A CD1 
6008  N N   . THR A 836  ? 0.3048 0.2248 0.2827 0.0137  0.0140  0.0218  834  THR A N   
6009  C CA  . THR A 836  ? 0.3658 0.2875 0.3395 0.0165  0.0153  0.0171  834  THR A CA  
6010  C C   . THR A 836  ? 0.3452 0.2648 0.3193 0.0171  0.0134  0.0133  834  THR A C   
6011  O O   . THR A 836  ? 0.3605 0.2808 0.3357 0.0201  0.0129  0.0082  834  THR A O   
6012  C CB  . THR A 836  ? 0.3807 0.3056 0.3469 0.0159  0.0179  0.0187  834  THR A CB  
6013  O OG1 . THR A 836  ? 0.4119 0.3389 0.3783 0.0155  0.0194  0.0217  834  THR A OG1 
6014  C CG2 . THR A 836  ? 0.3759 0.3036 0.3378 0.0185  0.0190  0.0148  834  THR A CG2 
6015  N N   . SER A 837  ? 0.3318 0.2496 0.3052 0.0145  0.0124  0.0153  835  SER A N   
6016  C CA  . SER A 837  ? 0.3253 0.2417 0.2985 0.0149  0.0107  0.0118  835  SER A CA  
6017  C C   . SER A 837  ? 0.3406 0.2537 0.3220 0.0159  0.0077  0.0089  835  SER A C   
6018  O O   . SER A 837  ? 0.3242 0.2370 0.3062 0.0180  0.0065  0.0037  835  SER A O   
6019  C CB  . SER A 837  ? 0.2943 0.2104 0.2655 0.0118  0.0103  0.0148  835  SER A CB  
6020  O OG  . SER A 837  ? 0.3134 0.2320 0.2775 0.0115  0.0125  0.0160  835  SER A OG  
6021  N N   . ALA A 838  ? 0.2967 0.2077 0.2850 0.0145  0.0063  0.0122  836  ALA A N   
6022  C CA  . ALA A 838  ? 0.3210 0.2280 0.3187 0.0148  0.0027  0.0105  836  ALA A CA  
6023  C C   . ALA A 838  ? 0.3299 0.2365 0.3323 0.0187  0.0020  0.0056  836  ALA A C   
6024  O O   . ALA A 838  ? 0.3503 0.2543 0.3586 0.0206  -0.0007 0.0006  836  ALA A O   
6025  C CB  . ALA A 838  ? 0.3099 0.2150 0.3137 0.0113  0.0010  0.0171  836  ALA A CB  
6026  N N   . PHE A 839  ? 0.3295 0.2389 0.3298 0.0201  0.0043  0.0066  837  PHE A N   
6027  C CA  . PHE A 839  ? 0.3547 0.2642 0.3609 0.0235  0.0035  0.0028  837  PHE A CA  
6028  C C   . PHE A 839  ? 0.3112 0.2263 0.3115 0.0271  0.0064  -0.0020 837  PHE A C   
6029  O O   . PHE A 839  ? 0.3295 0.2459 0.3347 0.0307  0.0056  -0.0071 837  PHE A O   
6030  C CB  . PHE A 839  ? 0.3196 0.2281 0.3310 0.0222  0.0031  0.0083  837  PHE A CB  
6031  C CG  . PHE A 839  ? 0.3396 0.2441 0.3567 0.0184  0.0003  0.0141  837  PHE A CG  
6032  C CD1 . PHE A 839  ? 0.3364 0.2363 0.3613 0.0181  -0.0035 0.0124  837  PHE A CD1 
6033  C CD2 . PHE A 839  ? 0.3648 0.2709 0.3793 0.0150  0.0015  0.0213  837  PHE A CD2 
6034  C CE1 . PHE A 839  ? 0.3636 0.2608 0.3940 0.0142  -0.0060 0.0185  837  PHE A CE1 
6035  C CE2 . PHE A 839  ? 0.3642 0.2683 0.3835 0.0114  -0.0008 0.0270  837  PHE A CE2 
6036  C CZ  . PHE A 839  ? 0.3468 0.2465 0.3741 0.0108  -0.0046 0.0260  837  PHE A CZ  
6037  N N   . ASP A 840  ? 0.3439 0.2630 0.3345 0.0264  0.0095  -0.0006 838  ASP A N   
6038  C CA  . ASP A 840  ? 0.3548 0.2802 0.3397 0.0294  0.0121  -0.0047 838  ASP A CA  
6039  C C   . ASP A 840  ? 0.3848 0.3110 0.3722 0.0328  0.0102  -0.0127 838  ASP A C   
6040  O O   . ASP A 840  ? 0.3278 0.2504 0.3170 0.0320  0.0077  -0.0144 838  ASP A O   
6041  C CB  . ASP A 840  ? 0.3914 0.3197 0.3666 0.0276  0.0147  -0.0016 838  ASP A CB  
6042  C CG  . ASP A 840  ? 0.4102 0.3457 0.3792 0.0302  0.0173  -0.0046 838  ASP A CG  
6043  O OD1 . ASP A 840  ? 0.4067 0.3445 0.3739 0.0324  0.0165  -0.0099 838  ASP A OD1 
6044  O OD2 . ASP A 840  ? 0.4874 0.4268 0.4532 0.0299  0.0199  -0.0013 838  ASP A OD2 
6045  N N   . SER A 841  ? 0.3399 0.2716 0.3281 0.0367  0.0111  -0.0179 839  SER A N   
6046  C CA  . SER A 841  ? 0.3434 0.2775 0.3343 0.0406  0.0092  -0.0267 839  SER A CA  
6047  C C   . SER A 841  ? 0.3216 0.2482 0.3234 0.0407  0.0046  -0.0296 839  SER A C   
6048  O O   . SER A 841  ? 0.3609 0.2866 0.3651 0.0422  0.0021  -0.0356 839  SER A O   
6049  C CB  . SER A 841  ? 0.4044 0.3423 0.3869 0.0406  0.0102  -0.0288 839  SER A CB  
6050  O OG  . SER A 841  ? 0.3845 0.3286 0.3576 0.0400  0.0141  -0.0249 839  SER A OG  
6051  N N   . ALA A 842  ? 0.3461 0.2675 0.3550 0.0390  0.0032  -0.0249 840  ALA A N   
6052  C CA  . ALA A 842  ? 0.3570 0.2709 0.3776 0.0385  -0.0015 -0.0258 840  ALA A CA  
6053  C C   . ALA A 842  ? 0.3055 0.2149 0.3257 0.0357  -0.0036 -0.0250 840  ALA A C   
6054  O O   . ALA A 842  ? 0.3495 0.2546 0.3784 0.0365  -0.0077 -0.0292 840  ALA A O   
6055  C CB  . ALA A 842  ? 0.3469 0.2616 0.3764 0.0435  -0.0042 -0.0349 840  ALA A CB  
6056  N N   . GLY A 843  ? 0.3586 0.2693 0.3696 0.0326  -0.0011 -0.0198 841  GLY A N   
6057  C CA  . GLY A 843  ? 0.2964 0.2040 0.3067 0.0299  -0.0027 -0.0188 841  GLY A CA  
6058  C C   . GLY A 843  ? 0.3446 0.2538 0.3540 0.0325  -0.0042 -0.0269 841  GLY A C   
6059  O O   . GLY A 843  ? 0.3731 0.2790 0.3851 0.0307  -0.0067 -0.0274 841  GLY A O   
6060  N N   . GLN A 844  ? 0.3371 0.2524 0.3433 0.0368  -0.0027 -0.0334 842  GLN A N   
6061  C CA  . GLN A 844  ? 0.3331 0.2516 0.3381 0.0397  -0.0042 -0.0418 842  GLN A CA  
6062  C C   . GLN A 844  ? 0.4103 0.3345 0.4031 0.0392  -0.0012 -0.0409 842  GLN A C   
6063  O O   . GLN A 844  ? 0.4701 0.4008 0.4588 0.0425  -0.0008 -0.0474 842  GLN A O   
6064  C CB  . GLN A 844  ? 0.3503 0.2736 0.3594 0.0449  -0.0047 -0.0502 842  GLN A CB  
6065  C CG  . GLN A 844  ? 0.3573 0.2743 0.3801 0.0458  -0.0085 -0.0521 842  GLN A CG  
6066  C CD  . GLN A 844  ? 0.3531 0.2753 0.3809 0.0515  -0.0093 -0.0614 842  GLN A CD  
6067  O OE1 . GLN A 844  ? 0.3442 0.2630 0.3826 0.0539  -0.0137 -0.0684 842  GLN A OE1 
6068  N NE2 . GLN A 844  ? 0.3624 0.2931 0.3829 0.0536  -0.0052 -0.0617 842  GLN A NE2 
6069  N N   . ARG A 845  ? 0.3850 0.3076 0.3722 0.0354  0.0008  -0.0330 843  ARG A N   
6070  C CA  . ARG A 845  ? 0.3837 0.3101 0.3612 0.0345  0.0026  -0.0317 843  ARG A CA  
6071  C C   . ARG A 845  ? 0.3652 0.2870 0.3450 0.0323  -0.0003 -0.0319 843  ARG A C   
6072  O O   . ARG A 845  ? 0.3754 0.2910 0.3624 0.0296  -0.0024 -0.0289 843  ARG A O   
6073  C CB  . ARG A 845  ? 0.3873 0.3145 0.3579 0.0319  0.0060  -0.0236 843  ARG A CB  
6074  C CG  . ARG A 845  ? 0.4131 0.3451 0.3812 0.0335  0.0090  -0.0225 843  ARG A CG  
6075  C CD  . ARG A 845  ? 0.3919 0.3245 0.3538 0.0307  0.0119  -0.0149 843  ARG A CD  
6076  N NE  . ARG A 845  ? 0.4018 0.3393 0.3614 0.0319  0.0147  -0.0132 843  ARG A NE  
6077  C CZ  . ARG A 845  ? 0.4372 0.3812 0.3895 0.0327  0.0173  -0.0123 843  ARG A CZ  
6078  N NH1 . ARG A 845  ? 0.4462 0.3927 0.3925 0.0326  0.0174  -0.0127 843  ARG A NH1 
6079  N NH2 . ARG A 845  ? 0.4745 0.4230 0.4259 0.0335  0.0198  -0.0104 843  ARG A NH2 
6080  N N   . CYS A 846  ? 0.3784 0.3041 0.3524 0.0333  -0.0003 -0.0353 844  CYS A N   
6081  C CA  . CYS A 846  ? 0.3985 0.3207 0.3740 0.0310  -0.0027 -0.0350 844  CYS A CA  
6082  C C   . CYS A 846  ? 0.3269 0.2460 0.3003 0.0267  -0.0014 -0.0266 844  CYS A C   
6083  O O   . CYS A 846  ? 0.3493 0.2642 0.3275 0.0239  -0.0035 -0.0246 844  CYS A O   
6084  C CB  . CYS A 846  ? 0.4181 0.3459 0.3867 0.0329  -0.0028 -0.0394 844  CYS A CB  
6085  S SG  . CYS A 846  ? 0.6071 0.5414 0.5769 0.0383  -0.0042 -0.0504 844  CYS A SG  
6086  N N   . SER A 847  ? 0.3202 0.2419 0.2871 0.0262  0.0020  -0.0218 845  SER A N   
6087  C CA  . SER A 847  ? 0.3619 0.2819 0.3261 0.0228  0.0035  -0.0146 845  SER A CA  
6088  C C   . SER A 847  ? 0.3604 0.2764 0.3306 0.0204  0.0034  -0.0100 845  SER A C   
6089  O O   . SER A 847  ? 0.3512 0.2667 0.3196 0.0176  0.0045  -0.0045 845  SER A O   
6090  C CB  . SER A 847  ? 0.3469 0.2711 0.3025 0.0234  0.0068  -0.0117 845  SER A CB  
6091  O OG  . SER A 847  ? 0.3951 0.3219 0.3506 0.0255  0.0084  -0.0126 845  SER A OG  
6092  N N   . ALA A 848  ? 0.3400 0.2539 0.3174 0.0217  0.0019  -0.0123 846  ALA A N   
6093  C CA  . ALA A 848  ? 0.3402 0.2515 0.3226 0.0199  0.0020  -0.0075 846  ALA A CA  
6094  C C   . ALA A 848  ? 0.3291 0.2374 0.3152 0.0158  0.0006  -0.0022 846  ALA A C   
6095  O O   . ALA A 848  ? 0.2975 0.2044 0.2861 0.0145  -0.0016 -0.0035 846  ALA A O   
6096  C CB  . ALA A 848  ? 0.3117 0.2210 0.3025 0.0223  -0.0001 -0.0113 846  ALA A CB  
6097  N N   . LEU A 849  ? 0.2965 0.2049 0.2830 0.0136  0.0019  0.0037  847  LEU A N   
6098  C CA  . LEU A 849  ? 0.2953 0.2027 0.2849 0.0096  0.0008  0.0092  847  LEU A CA  
6099  C C   . LEU A 849  ? 0.3139 0.2173 0.3144 0.0084  -0.0028 0.0099  847  LEU A C   
6100  O O   . LEU A 849  ? 0.3268 0.2284 0.3325 0.0094  -0.0035 0.0106  847  LEU A O   
6101  C CB  . LEU A 849  ? 0.2686 0.1783 0.2551 0.0079  0.0032  0.0148  847  LEU A CB  
6102  C CG  . LEU A 849  ? 0.2848 0.1954 0.2745 0.0038  0.0024  0.0208  847  LEU A CG  
6103  C CD1 . LEU A 849  ? 0.3145 0.2271 0.3013 0.0020  0.0022  0.0207  847  LEU A CD1 
6104  C CD2 . LEU A 849  ? 0.3033 0.2169 0.2894 0.0029  0.0047  0.0251  847  LEU A CD2 
6105  N N   . ARG A 850  ? 0.2735 0.1756 0.2780 0.0063  -0.0052 0.0101  848  ARG A N   
6106  C CA  . ARG A 850  ? 0.3379 0.2359 0.3539 0.0047  -0.0091 0.0113  848  ARG A CA  
6107  C C   . ARG A 850  ? 0.3319 0.2312 0.3517 0.0000  -0.0098 0.0195  848  ARG A C   
6108  O O   . ARG A 850  ? 0.3312 0.2277 0.3602 -0.0015 -0.0125 0.0230  848  ARG A O   
6109  C CB  . ARG A 850  ? 0.3379 0.2338 0.3578 0.0053  -0.0120 0.0059  848  ARG A CB  
6110  C CG  . ARG A 850  ? 0.3257 0.2221 0.3410 0.0099  -0.0114 -0.0025 848  ARG A CG  
6111  C CD  . ARG A 850  ? 0.3705 0.2655 0.3889 0.0133  -0.0115 -0.0056 848  ARG A CD  
6112  N NE  . ARG A 850  ? 0.3941 0.2912 0.4088 0.0178  -0.0111 -0.0140 848  ARG A NE  
6113  C CZ  . ARG A 850  ? 0.4060 0.3038 0.4221 0.0215  -0.0108 -0.0184 848  ARG A CZ  
6114  N NH1 . ARG A 850  ? 0.3215 0.2175 0.3425 0.0216  -0.0109 -0.0153 848  ARG A NH1 
6115  N NH2 . ARG A 850  ? 0.3680 0.2692 0.3806 0.0255  -0.0106 -0.0262 848  ARG A NH2 
6116  N N   . VAL A 851  ? 0.3223 0.2261 0.3356 -0.0024 -0.0077 0.0226  849  VAL A N   
6117  C CA  . VAL A 851  ? 0.3429 0.2500 0.3594 -0.0069 -0.0082 0.0300  849  VAL A CA  
6118  C C   . VAL A 851  ? 0.3310 0.2438 0.3388 -0.0076 -0.0046 0.0329  849  VAL A C   
6119  O O   . VAL A 851  ? 0.3410 0.2563 0.3411 -0.0066 -0.0025 0.0300  849  VAL A O   
6120  C CB  . VAL A 851  ? 0.3325 0.2407 0.3524 -0.0096 -0.0102 0.0304  849  VAL A CB  
6121  C CG1 . VAL A 851  ? 0.3657 0.2787 0.3890 -0.0145 -0.0106 0.0387  849  VAL A CG1 
6122  C CG2 . VAL A 851  ? 0.4156 0.3178 0.4448 -0.0089 -0.0142 0.0269  849  VAL A CG2 
6123  N N   . LEU A 852  ? 0.2915 0.2065 0.3009 -0.0094 -0.0042 0.0386  850  LEU A N   
6124  C CA  . LEU A 852  ? 0.3098 0.2309 0.3123 -0.0104 -0.0013 0.0415  850  LEU A CA  
6125  C C   . LEU A 852  ? 0.2837 0.2111 0.2886 -0.0148 -0.0019 0.0475  850  LEU A C   
6126  O O   . LEU A 852  ? 0.2668 0.1942 0.2796 -0.0175 -0.0043 0.0527  850  LEU A O   
6127  C CB  . LEU A 852  ? 0.2736 0.1944 0.2758 -0.0092 -0.0003 0.0434  850  LEU A CB  
6128  C CG  . LEU A 852  ? 0.3150 0.2420 0.3113 -0.0103 0.0023  0.0464  850  LEU A CG  
6129  C CD1 . LEU A 852  ? 0.3231 0.2516 0.3106 -0.0084 0.0049  0.0419  850  LEU A CD1 
6130  C CD2 . LEU A 852  ? 0.2894 0.2154 0.2873 -0.0093 0.0026  0.0486  850  LEU A CD2 
6131  N N   . CYS A 853  ? 0.3109 0.2440 0.3095 -0.0156 0.0001  0.0468  851  CYS A N   
6132  C CA  . CYS A 853  ? 0.3337 0.2748 0.3335 -0.0195 -0.0001 0.0514  851  CYS A CA  
6133  C C   . CYS A 853  ? 0.3190 0.2674 0.3133 -0.0200 0.0023  0.0535  851  CYS A C   
6134  O O   . CYS A 853  ? 0.3038 0.2533 0.2912 -0.0178 0.0045  0.0493  851  CYS A O   
6135  C CB  . CYS A 853  ? 0.3287 0.2716 0.3266 -0.0197 0.0000  0.0479  851  CYS A CB  
6136  S SG  . CYS A 853  ? 0.3836 0.3176 0.3859 -0.0178 -0.0026 0.0429  851  CYS A SG  
6137  N N   . LEU A 854  ? 0.3138 0.2675 0.3117 -0.0229 0.0017  0.0600  852  LEU A N   
6138  C CA  . LEU A 854  ? 0.3021 0.2629 0.2956 -0.0233 0.0036  0.0621  852  LEU A CA  
6139  C C   . LEU A 854  ? 0.2948 0.2674 0.2879 -0.0268 0.0039  0.0658  852  LEU A C   
6140  O O   . LEU A 854  ? 0.3233 0.2993 0.3225 -0.0303 0.0021  0.0716  852  LEU A O   
6141  C CB  . LEU A 854  ? 0.3364 0.2954 0.3339 -0.0238 0.0025  0.0667  852  LEU A CB  
6142  C CG  . LEU A 854  ? 0.3243 0.2733 0.3224 -0.0201 0.0024  0.0630  852  LEU A CG  
6143  C CD1 . LEU A 854  ? 0.2970 0.2453 0.2996 -0.0206 0.0012  0.0678  852  LEU A CD1 
6144  C CD2 . LEU A 854  ? 0.3122 0.2601 0.3021 -0.0169 0.0051  0.0569  852  LEU A CD2 
6145  N N   . GLN A 855  ? 0.3065 0.2858 0.2932 -0.0260 0.0061  0.0626  853  GLN A N   
6146  C CA  . GLN A 855  ? 0.3103 0.3027 0.2965 -0.0290 0.0067  0.0656  853  GLN A CA  
6147  C C   . GLN A 855  ? 0.2991 0.2981 0.2888 -0.0320 0.0058  0.0734  853  GLN A C   
6148  O O   . GLN A 855  ? 0.3487 0.3451 0.3378 -0.0309 0.0059  0.0745  853  GLN A O   
6149  C CB  . GLN A 855  ? 0.3039 0.3027 0.2833 -0.0271 0.0089  0.0602  853  GLN A CB  
6150  C CG  . GLN A 855  ? 0.3404 0.3538 0.3196 -0.0298 0.0094  0.0619  853  GLN A CG  
6151  C CD  . GLN A 855  ? 0.3768 0.3972 0.3504 -0.0277 0.0111  0.0559  853  GLN A CD  
6152  O OE1 . GLN A 855  ? 0.3411 0.3546 0.3115 -0.0244 0.0117  0.0495  853  GLN A OE1 
6153  N NE2 . GLN A 855  ? 0.4007 0.4353 0.3734 -0.0296 0.0118  0.0579  853  GLN A NE2 
6154  N N   . GLU A 856  ? 0.3317 0.3398 0.3253 -0.0360 0.0048  0.0793  854  GLU A N   
6155  C CA  . GLU A 856  ? 0.3742 0.3875 0.3729 -0.0395 0.0032  0.0883  854  GLU A CA  
6156  C C   . GLU A 856  ? 0.3822 0.4026 0.3766 -0.0390 0.0045  0.0893  854  GLU A C   
6157  O O   . GLU A 856  ? 0.3880 0.4064 0.3856 -0.0397 0.0031  0.0944  854  GLU A O   
6158  C CB  . GLU A 856  ? 0.3889 0.4136 0.3915 -0.0441 0.0024  0.0944  854  GLU A CB  
6159  C CG  . GLU A 856  ? 0.4627 0.4956 0.4702 -0.0482 0.0008  0.1049  854  GLU A CG  
6160  C CD  . GLU A 856  ? 0.5346 0.5555 0.5498 -0.0484 -0.0022 0.1096  854  GLU A CD  
6161  O OE1 . GLU A 856  ? 0.4865 0.4955 0.5065 -0.0475 -0.0039 0.1073  854  GLU A OE1 
6162  O OE2 . GLU A 856  ? 0.5027 0.5262 0.5194 -0.0494 -0.0031 0.1152  854  GLU A OE2 
6163  N N   . ASP A 857  ? 0.3849 0.4137 0.3726 -0.0376 0.0068  0.0841  855  ASP A N   
6164  C CA  . ASP A 857  ? 0.3878 0.4250 0.3717 -0.0374 0.0077  0.0847  855  ASP A CA  
6165  C C   . ASP A 857  ? 0.4482 0.4749 0.4309 -0.0344 0.0077  0.0823  855  ASP A C   
6166  O O   . ASP A 857  ? 0.4573 0.4897 0.4388 -0.0347 0.0078  0.0845  855  ASP A O   
6167  C CB  . ASP A 857  ? 0.4988 0.5467 0.4767 -0.0362 0.0098  0.0783  855  ASP A CB  
6168  N N   . VAL A 858  ? 0.3779 0.3906 0.3609 -0.0315 0.0077  0.0777  856  VAL A N   
6169  C CA  . VAL A 858  ? 0.3677 0.3713 0.3499 -0.0286 0.0078  0.0755  856  VAL A CA  
6170  C C   . VAL A 858  ? 0.3555 0.3476 0.3435 -0.0282 0.0060  0.0782  856  VAL A C   
6171  O O   . VAL A 858  ? 0.3546 0.3392 0.3427 -0.0258 0.0061  0.0764  856  VAL A O   
6172  C CB  . VAL A 858  ? 0.4051 0.4034 0.3818 -0.0250 0.0097  0.0670  856  VAL A CB  
6173  C CG1 . VAL A 858  ? 0.4395 0.4484 0.4113 -0.0248 0.0110  0.0637  856  VAL A CG1 
6174  C CG2 . VAL A 858  ? 0.3807 0.3721 0.3573 -0.0237 0.0097  0.0629  856  VAL A CG2 
6175  N N   . ALA A 859  ? 0.3380 0.3291 0.3318 -0.0306 0.0041  0.0825  857  ALA A N   
6176  C CA  . ALA A 859  ? 0.3121 0.2915 0.3123 -0.0297 0.0020  0.0834  857  ALA A CA  
6177  C C   . ALA A 859  ? 0.3884 0.3656 0.3929 -0.0297 0.0005  0.0881  857  ALA A C   
6178  O O   . ALA A 859  ? 0.3517 0.3192 0.3582 -0.0268 0.0000  0.0853  857  ALA A O   
6179  C CB  . ALA A 859  ? 0.3518 0.3313 0.3585 -0.0327 -0.0002 0.0874  857  ALA A CB  
6180  N N   . ASP A 860  ? 0.3307 0.3175 0.3368 -0.0328 -0.0003 0.0953  858  ASP A N   
6181  C CA  . ASP A 860  ? 0.3783 0.3628 0.3897 -0.0329 -0.0022 0.1005  858  ASP A CA  
6182  C C   . ASP A 860  ? 0.3529 0.3344 0.3595 -0.0293 -0.0004 0.0957  858  ASP A C   
6183  O O   . ASP A 860  ? 0.3834 0.3569 0.3942 -0.0273 -0.0016 0.0956  858  ASP A O   
6184  C CB  . ASP A 860  ? 0.4127 0.4092 0.4266 -0.0371 -0.0036 0.1099  858  ASP A CB  
6185  C CG  . ASP A 860  ? 0.4860 0.4831 0.5082 -0.0409 -0.0065 0.1171  858  ASP A CG  
6186  O OD1 . ASP A 860  ? 0.4939 0.4797 0.5229 -0.0400 -0.0087 0.1163  858  ASP A OD1 
6187  O OD2 . ASP A 860  ? 0.5383 0.5479 0.5607 -0.0448 -0.0068 0.1237  858  ASP A OD2 
6188  N N   . ARG A 861  ? 0.3508 0.3385 0.3494 -0.0285 0.0022  0.0913  859  ARG A N   
6189  C CA  . ARG A 861  ? 0.3636 0.3487 0.3582 -0.0255 0.0038  0.0868  859  ARG A CA  
6190  C C   . ARG A 861  ? 0.3355 0.3084 0.3298 -0.0219 0.0045  0.0805  859  ARG A C   
6191  O O   . ARG A 861  ? 0.3393 0.3071 0.3348 -0.0196 0.0046  0.0793  859  ARG A O   
6192  C CB  . ARG A 861  ? 0.4063 0.4004 0.3935 -0.0255 0.0061  0.0830  859  ARG A CB  
6193  C CG  . ARG A 861  ? 0.4641 0.4550 0.4477 -0.0226 0.0075  0.0782  859  ARG A CG  
6194  C CD  . ARG A 861  ? 0.5730 0.5749 0.5524 -0.0234 0.0084  0.0774  859  ARG A CD  
6195  N NE  . ARG A 861  ? 0.6568 0.6546 0.6337 -0.0208 0.0096  0.0726  859  ARG A NE  
6196  C CZ  . ARG A 861  ? 0.6185 0.6111 0.5919 -0.0185 0.0111  0.0661  859  ARG A CZ  
6197  N NH1 . ARG A 861  ? 0.5675 0.5585 0.5391 -0.0183 0.0116  0.0631  859  ARG A NH1 
6198  N NH2 . ARG A 861  ? 0.5756 0.5648 0.5478 -0.0166 0.0119  0.0630  859  ARG A NH2 
6199  N N   . ILE A 862  ? 0.3088 0.2782 0.3014 -0.0212 0.0052  0.0763  860  ILE A N   
6200  C CA  . ILE A 862  ? 0.3148 0.2741 0.3065 -0.0178 0.0059  0.0703  860  ILE A CA  
6201  C C   . ILE A 862  ? 0.3519 0.3034 0.3511 -0.0169 0.0036  0.0720  860  ILE A C   
6202  O O   . ILE A 862  ? 0.3189 0.2640 0.3186 -0.0139 0.0040  0.0686  860  ILE A O   
6203  C CB  . ILE A 862  ? 0.3565 0.3148 0.3444 -0.0174 0.0069  0.0656  860  ILE A CB  
6204  C CG1 . ILE A 862  ? 0.3643 0.3288 0.3453 -0.0171 0.0091  0.0623  860  ILE A CG1 
6205  C CG2 . ILE A 862  ? 0.3186 0.2673 0.3067 -0.0142 0.0070  0.0604  860  ILE A CG2 
6206  C CD1 . ILE A 862  ? 0.3687 0.3332 0.3463 -0.0167 0.0098  0.0579  860  ILE A CD1 
6207  N N   . LEU A 863  ? 0.3403 0.2926 0.3460 -0.0196 0.0010  0.0773  861  LEU A N   
6208  C CA  A LEU A 863  ? 0.3438 0.2884 0.3582 -0.0188 -0.0018 0.0788  861  LEU A CA  
6209  C CA  B LEU A 863  ? 0.3439 0.2884 0.3583 -0.0188 -0.0018 0.0788  861  LEU A CA  
6210  C C   . LEU A 863  ? 0.3265 0.2703 0.3442 -0.0176 -0.0026 0.0815  861  LEU A C   
6211  O O   . LEU A 863  ? 0.3028 0.2393 0.3249 -0.0148 -0.0036 0.0788  861  LEU A O   
6212  C CB  A LEU A 863  ? 0.3506 0.2968 0.3722 -0.0224 -0.0048 0.0849  861  LEU A CB  
6213  C CB  B LEU A 863  ? 0.3507 0.2965 0.3724 -0.0223 -0.0048 0.0847  861  LEU A CB  
6214  C CG  A LEU A 863  ? 0.3646 0.3017 0.3963 -0.0217 -0.0083 0.0852  861  LEU A CG  
6215  C CG  B LEU A 863  ? 0.3780 0.3175 0.4024 -0.0218 -0.0059 0.0808  861  LEU A CG  
6216  C CD1 A LEU A 863  ? 0.3693 0.2984 0.3988 -0.0176 -0.0073 0.0761  861  LEU A CD1 
6217  C CD1 B LEU A 863  ? 0.3928 0.3350 0.4245 -0.0261 -0.0088 0.0874  861  LEU A CD1 
6218  C CD2 A LEU A 863  ? 0.4034 0.3425 0.4414 -0.0258 -0.0109 0.0909  861  LEU A CD2 
6219  C CD2 B LEU A 863  ? 0.3706 0.3000 0.3998 -0.0181 -0.0073 0.0758  861  LEU A CD2 
6220  N N   . THR A 864  ? 0.3255 0.2775 0.3413 -0.0197 -0.0022 0.0865  862  THR A N   
6221  C CA  . THR A 864  ? 0.3240 0.2761 0.3426 -0.0186 -0.0028 0.0889  862  THR A CA  
6222  C C   . THR A 864  ? 0.3053 0.2531 0.3193 -0.0146 -0.0004 0.0819  862  THR A C   
6223  O O   . THR A 864  ? 0.3325 0.2750 0.3512 -0.0121 -0.0013 0.0808  862  THR A O   
6224  C CB  . THR A 864  ? 0.3363 0.2994 0.3523 -0.0215 -0.0026 0.0948  862  THR A CB  
6225  O OG1 . THR A 864  ? 0.3411 0.3085 0.3627 -0.0253 -0.0053 0.1026  862  THR A OG1 
6226  C CG2 . THR A 864  ? 0.3171 0.2811 0.3346 -0.0202 -0.0029 0.0965  862  THR A CG2 
6227  N N   . MET A 865  ? 0.3060 0.2564 0.3117 -0.0140 0.0026  0.0772  863  MET A N   
6228  C CA  . MET A 865  ? 0.3112 0.2581 0.3127 -0.0107 0.0049  0.0713  863  MET A CA  
6229  C C   . MET A 865  ? 0.3086 0.2470 0.3127 -0.0078 0.0046  0.0666  863  MET A C   
6230  O O   . MET A 865  ? 0.3014 0.2365 0.3064 -0.0049 0.0052  0.0636  863  MET A O   
6231  C CB  . MET A 865  ? 0.3267 0.2775 0.3199 -0.0109 0.0075  0.0676  863  MET A CB  
6232  C CG  . MET A 865  ? 0.3816 0.3300 0.3705 -0.0082 0.0098  0.0627  863  MET A CG  
6233  S SD  . MET A 865  ? 0.4773 0.4304 0.4582 -0.0089 0.0120  0.0591  863  MET A SD  
6234  C CE  . MET A 865  ? 0.3688 0.3319 0.3502 -0.0124 0.0108  0.0643  863  MET A CE  
6235  N N   . LEU A 866  ? 0.3192 0.2548 0.3248 -0.0085 0.0035  0.0656  864  LEU A N   
6236  C CA  . LEU A 866  ? 0.3070 0.2354 0.3149 -0.0056 0.0030  0.0604  864  LEU A CA  
6237  C C   . LEU A 866  ? 0.3079 0.2317 0.3249 -0.0040 0.0003  0.0615  864  LEU A C   
6238  O O   . LEU A 866  ? 0.3293 0.2493 0.3474 -0.0005 0.0008  0.0565  864  LEU A O   
6239  C CB  . LEU A 866  ? 0.3108 0.2379 0.3189 -0.0070 0.0020  0.0595  864  LEU A CB  
6240  C CG  . LEU A 866  ? 0.3439 0.2644 0.3544 -0.0044 0.0011  0.0538  864  LEU A CG  
6241  C CD1 . LEU A 866  ? 0.3158 0.2359 0.3190 -0.0013 0.0042  0.0480  864  LEU A CD1 
6242  C CD2 . LEU A 866  ? 0.3406 0.2607 0.3515 -0.0064 0.0000  0.0537  864  LEU A CD2 
6243  N N   . LYS A 867  ? 0.3067 0.2315 0.3307 -0.0065 -0.0026 0.0679  865  LYS A N   
6244  C CA  . LYS A 867  ? 0.3080 0.2281 0.3420 -0.0049 -0.0056 0.0691  865  LYS A CA  
6245  C C   . LYS A 867  ? 0.3521 0.2734 0.3853 -0.0024 -0.0043 0.0681  865  LYS A C   
6246  O O   . LYS A 867  ? 0.3537 0.2706 0.3921 0.0010  -0.0053 0.0645  865  LYS A O   
6247  C CB  . LYS A 867  ? 0.3092 0.2308 0.3511 -0.0086 -0.0092 0.0776  865  LYS A CB  
6248  C CG  . LYS A 867  ? 0.3052 0.2252 0.3501 -0.0112 -0.0111 0.0790  865  LYS A CG  
6249  C CD  . LYS A 867  ? 0.3920 0.3153 0.4442 -0.0155 -0.0144 0.0888  865  LYS A CD  
6250  C CE  . LYS A 867  ? 0.4422 0.3643 0.4978 -0.0184 -0.0163 0.0902  865  LYS A CE  
6251  N NZ  . LYS A 867  ? 0.4336 0.3614 0.4945 -0.0234 -0.0188 0.1005  865  LYS A NZ  
6252  N N   . GLY A 868  ? 0.3280 0.2558 0.3551 -0.0039 -0.0021 0.0708  866  GLY A N   
6253  C CA  . GLY A 868  ? 0.3262 0.2557 0.3524 -0.0018 -0.0008 0.0699  866  GLY A CA  
6254  C C   . GLY A 868  ? 0.2976 0.2248 0.3195 0.0018  0.0020  0.0625  866  GLY A C   
6255  O O   . GLY A 868  ? 0.3518 0.2778 0.3768 0.0047  0.0021  0.0602  866  GLY A O   
6256  N N   . ALA A 869  ? 0.2911 0.2181 0.3060 0.0017  0.0041  0.0587  867  ALA A N   
6257  C CA  . ALA A 869  ? 0.2946 0.2201 0.3051 0.0048  0.0066  0.0522  867  ALA A CA  
6258  C C   . ALA A 869  ? 0.3338 0.2542 0.3500 0.0080  0.0050  0.0477  867  ALA A C   
6259  O O   . ALA A 869  ? 0.2975 0.2179 0.3132 0.0113  0.0064  0.0430  867  ALA A O   
6260  C CB  . ALA A 869  ? 0.3114 0.2382 0.3134 0.0038  0.0089  0.0500  867  ALA A CB  
6261  N N   . LEU A 870  ? 0.3255 0.2422 0.3474 0.0070  0.0020  0.0487  868  LEU A N   
6262  C CA  . LEU A 870  ? 0.3435 0.2551 0.3723 0.0100  -0.0002 0.0439  868  LEU A CA  
6263  C C   . LEU A 870  ? 0.3318 0.2429 0.3674 0.0130  -0.0012 0.0428  868  LEU A C   
6264  O O   . LEU A 870  ? 0.3275 0.2375 0.3650 0.0170  -0.0010 0.0364  868  LEU A O   
6265  C CB  . LEU A 870  ? 0.3260 0.2337 0.3623 0.0078  -0.0041 0.0469  868  LEU A CB  
6266  C CG  . LEU A 870  ? 0.3499 0.2518 0.3947 0.0105  -0.0073 0.0417  868  LEU A CG  
6267  C CD1 . LEU A 870  ? 0.3933 0.2943 0.4326 0.0112  -0.0060 0.0360  868  LEU A CD1 
6268  C CD2 . LEU A 870  ? 0.4006 0.2985 0.4569 0.0081  -0.0121 0.0471  868  LEU A CD2 
6269  N N   . HIS A 871  ? 0.3047 0.2174 0.3444 0.0114  -0.0025 0.0490  869  HIS A N   
6270  C CA  . HIS A 871  ? 0.3510 0.2631 0.3985 0.0141  -0.0041 0.0486  869  HIS A CA  
6271  C C   . HIS A 871  ? 0.3434 0.2600 0.3857 0.0166  -0.0005 0.0455  869  HIS A C   
6272  O O   . HIS A 871  ? 0.3384 0.2555 0.3868 0.0192  -0.0015 0.0447  869  HIS A O   
6273  C CB  . HIS A 871  ? 0.3315 0.2441 0.3853 0.0113  -0.0070 0.0570  869  HIS A CB  
6274  C CG  . HIS A 871  ? 0.3922 0.3000 0.4548 0.0095  -0.0115 0.0603  869  HIS A CG  
6275  N ND1 . HIS A 871  ? 0.4074 0.3093 0.4814 0.0122  -0.0153 0.0574  869  HIS A ND1 
6276  C CD2 . HIS A 871  ? 0.3808 0.2891 0.4431 0.0051  -0.0128 0.0663  869  HIS A CD2 
6277  C CE1 . HIS A 871  ? 0.4212 0.3195 0.5019 0.0094  -0.0190 0.0619  869  HIS A CE1 
6278  N NE2 . HIS A 871  ? 0.3984 0.3009 0.4719 0.0049  -0.0174 0.0676  869  HIS A NE2 
6279  N N   . GLU A 872  ? 0.2974 0.2174 0.3293 0.0159  0.0033  0.0439  870  GLU A N   
6280  C CA  . GLU A 872  ? 0.2959 0.2204 0.3232 0.0179  0.0066  0.0411  870  GLU A CA  
6281  C C   . GLU A 872  ? 0.3347 0.2593 0.3600 0.0215  0.0083  0.0336  870  GLU A C   
6282  O O   . GLU A 872  ? 0.3232 0.2522 0.3446 0.0232  0.0112  0.0313  870  GLU A O   
6283  C CB  . GLU A 872  ? 0.3181 0.2466 0.3363 0.0149  0.0095  0.0442  870  GLU A CB  
6284  C CG  . GLU A 872  ? 0.3472 0.2779 0.3668 0.0117  0.0083  0.0510  870  GLU A CG  
6285  C CD  . GLU A 872  ? 0.3665 0.2993 0.3922 0.0132  0.0074  0.0527  870  GLU A CD  
6286  O OE1 . GLU A 872  ? 0.3790 0.3133 0.4053 0.0163  0.0091  0.0486  870  GLU A OE1 
6287  O OE2 . GLU A 872  ? 0.4119 0.3456 0.4420 0.0113  0.0051  0.0582  870  GLU A OE2 
6288  N N   . LEU A 873  ? 0.3396 0.2601 0.3676 0.0226  0.0063  0.0299  871  LEU A N   
6289  C CA  . LEU A 873  ? 0.3389 0.2604 0.3646 0.0260  0.0076  0.0224  871  LEU A CA  
6290  C C   . LEU A 873  ? 0.3343 0.2563 0.3684 0.0305  0.0062  0.0174  871  LEU A C   
6291  O O   . LEU A 873  ? 0.3207 0.2387 0.3647 0.0310  0.0025  0.0186  871  LEU A O   
6292  C CB  . LEU A 873  ? 0.3321 0.2493 0.3573 0.0254  0.0059  0.0201  871  LEU A CB  
6293  C CG  . LEU A 873  ? 0.3287 0.2456 0.3461 0.0215  0.0071  0.0236  871  LEU A CG  
6294  C CD1 . LEU A 873  ? 0.3221 0.2346 0.3417 0.0211  0.0046  0.0211  871  LEU A CD1 
6295  C CD2 . LEU A 873  ? 0.3495 0.2711 0.3567 0.0218  0.0112  0.0222  871  LEU A CD2 
6296  N N   . HIS A 874  ? 0.3240 0.2513 0.3545 0.0337  0.0089  0.0119  872  HIS A N   
6297  C CA  . HIS A 874  ? 0.3380 0.2677 0.3758 0.0386  0.0080  0.0058  872  HIS A CA  
6298  C C   . HIS A 874  ? 0.3489 0.2778 0.3877 0.0416  0.0069  -0.0022 872  HIS A C   
6299  O O   . HIS A 874  ? 0.3388 0.2715 0.3690 0.0418  0.0095  -0.0049 872  HIS A O   
6300  C CB  . HIS A 874  ? 0.3655 0.3036 0.3990 0.0402  0.0120  0.0049  872  HIS A CB  
6301  C CG  . HIS A 874  ? 0.3858 0.3281 0.4265 0.0453  0.0115  -0.0017 872  HIS A CG  
6302  N ND1 . HIS A 874  ? 0.4329 0.3843 0.4708 0.0473  0.0150  -0.0035 872  HIS A ND1 
6303  C CD2 . HIS A 874  ? 0.4213 0.3606 0.4726 0.0489  0.0077  -0.0070 872  HIS A CD2 
6304  C CE1 . HIS A 874  ? 0.4581 0.4125 0.5040 0.0522  0.0137  -0.0101 872  HIS A CE1 
6305  N NE2 . HIS A 874  ? 0.4018 0.3487 0.4562 0.0534  0.0091  -0.0126 872  HIS A NE2 
6306  N N   . ILE A 875  ? 0.3468 0.2709 0.3966 0.0439  0.0026  -0.0060 873  ILE A N   
6307  C CA  . ILE A 875  ? 0.3810 0.3040 0.4337 0.0470  0.0006  -0.0143 873  ILE A CA  
6308  C C   . ILE A 875  ? 0.3641 0.2920 0.4233 0.0528  0.0002  -0.0225 873  ILE A C   
6309  O O   . ILE A 875  ? 0.3719 0.2984 0.4405 0.0543  -0.0020 -0.0216 873  ILE A O   
6310  C CB  . ILE A 875  ? 0.3913 0.3048 0.4528 0.0454  -0.0046 -0.0131 873  ILE A CB  
6311  C CG1 . ILE A 875  ? 0.3988 0.3089 0.4533 0.0405  -0.0041 -0.0077 873  ILE A CG1 
6312  C CG2 . ILE A 875  ? 0.4315 0.3437 0.5003 0.0498  -0.0078 -0.0232 873  ILE A CG2 
6313  C CD1 . ILE A 875  ? 0.4236 0.3364 0.4684 0.0364  -0.0005 0.0003  873  ILE A CD1 
6314  N N   . GLY A 876  ? 0.3501 0.2848 0.4048 0.0562  0.0021  -0.0305 874  GLY A N   
6315  C CA  . GLY A 876  ? 0.3720 0.3128 0.4332 0.0620  0.0016  -0.0394 874  GLY A CA  
6316  C C   . GLY A 876  ? 0.3847 0.3348 0.4383 0.0651  0.0044  -0.0473 874  GLY A C   
6317  O O   . GLY A 876  ? 0.3558 0.3062 0.4002 0.0628  0.0060  -0.0461 874  GLY A O   
6318  N N   . ARG A 877  ? 0.3820 0.3406 0.4398 0.0705  0.0050  -0.0555 875  ARG A N   
6319  C CA  . ARG A 877  ? 0.4240 0.3940 0.4744 0.0737  0.0079  -0.0631 875  ARG A CA  
6320  C C   . ARG A 877  ? 0.3877 0.3649 0.4241 0.0703  0.0135  -0.0562 875  ARG A C   
6321  O O   . ARG A 877  ? 0.3700 0.3488 0.4047 0.0681  0.0159  -0.0493 875  ARG A O   
6322  C CB  . ARG A 877  ? 0.4205 0.4000 0.4780 0.0801  0.0077  -0.0728 875  ARG A CB  
6323  C CG  . ARG A 877  ? 0.4224 0.4124 0.4761 0.0844  0.0086  -0.0835 875  ARG A CG  
6324  C CD  . ARG A 877  ? 0.4606 0.4601 0.5232 0.0912  0.0078  -0.0942 875  ARG A CD  
6325  N NE  . ARG A 877  ? 0.4809 0.4945 0.5376 0.0923  0.0131  -0.0928 875  ARG A NE  
6326  C CZ  . ARG A 877  ? 0.6000 0.6249 0.6624 0.0980  0.0137  -0.1014 875  ARG A CZ  
6327  N NH1 . ARG A 877  ? 0.4793 0.5030 0.5539 0.1036  0.0091  -0.1127 875  ARG A NH1 
6328  N NH2 . ARG A 877  ? 0.5652 0.6034 0.6217 0.0981  0.0188  -0.0988 875  ARG A NH2 
6329  N N   . THR A 878  ? 0.3400 0.3217 0.3670 0.0697  0.0153  -0.0580 876  THR A N   
6330  C CA  . THR A 878  ? 0.3578 0.3427 0.3724 0.0655  0.0195  -0.0499 876  THR A CA  
6331  C C   . THR A 878  ? 0.3890 0.3886 0.3973 0.0671  0.0243  -0.0504 876  THR A C   
6332  O O   . THR A 878  ? 0.4264 0.4305 0.4245 0.0642  0.0275  -0.0451 876  THR A O   
6333  C CB  . THR A 878  ? 0.3824 0.3646 0.3898 0.0635  0.0190  -0.0499 876  THR A CB  
6334  O OG1 . THR A 878  ? 0.4038 0.3923 0.4121 0.0680  0.0178  -0.0603 876  THR A OG1 
6335  C CG2 . THR A 878  ? 0.3793 0.3472 0.3909 0.0601  0.0153  -0.0459 876  THR A CG2 
6336  N N   . ASP A 879  ? 0.3851 0.3927 0.3997 0.0714  0.0246  -0.0561 877  ASP A N   
6337  C CA  . ASP A 879  ? 0.4348 0.4570 0.4438 0.0724  0.0293  -0.0554 877  ASP A CA  
6338  C C   . ASP A 879  ? 0.4173 0.4385 0.4272 0.0694  0.0314  -0.0467 877  ASP A C   
6339  O O   . ASP A 879  ? 0.3967 0.4297 0.4059 0.0708  0.0346  -0.0469 877  ASP A O   
6340  C CB  . ASP A 879  ? 0.4498 0.4843 0.4638 0.0790  0.0293  -0.0668 877  ASP A CB  
6341  C CG  . ASP A 879  ? 0.4767 0.5073 0.5040 0.0825  0.0263  -0.0714 877  ASP A CG  
6342  O OD1 . ASP A 879  ? 0.5217 0.5382 0.5556 0.0803  0.0229  -0.0672 877  ASP A OD1 
6343  O OD2 . ASP A 879  ? 0.5098 0.5523 0.5413 0.0876  0.0272  -0.0792 877  ASP A OD2 
6344  N N   . ARG A 880  ? 0.3688 0.3772 0.3800 0.0651  0.0296  -0.0392 878  ARG A N   
6345  C CA  . ARG A 880  ? 0.3643 0.3712 0.3748 0.0614  0.0314  -0.0304 878  ARG A CA  
6346  C C   . ARG A 880  ? 0.3658 0.3654 0.3686 0.0557  0.0320  -0.0219 878  ARG A C   
6347  O O   . ARG A 880  ? 0.3422 0.3319 0.3452 0.0542  0.0292  -0.0215 878  ARG A O   
6348  C CB  . ARG A 880  ? 0.3944 0.3935 0.4158 0.0620  0.0282  -0.0296 878  ARG A CB  
6349  C CG  . ARG A 880  ? 0.4404 0.4469 0.4706 0.0673  0.0278  -0.0364 878  ARG A CG  
6350  C CD  . ARG A 880  ? 0.4486 0.4447 0.4906 0.0681  0.0232  -0.0362 878  ARG A CD  
6351  N NE  . ARG A 880  ? 0.6217 0.6239 0.6715 0.0710  0.0235  -0.0378 878  ARG A NE  
6352  C CZ  . ARG A 880  ? 0.6549 0.6647 0.7116 0.0769  0.0229  -0.0471 878  ARG A CZ  
6353  N NH1 . ARG A 880  ? 0.6086 0.6218 0.6654 0.0807  0.0220  -0.0562 878  ARG A NH1 
6354  N NH2 . ARG A 880  ? 0.6219 0.6367 0.6860 0.0793  0.0231  -0.0477 878  ARG A NH2 
6355  N N   . LEU A 881  ? 0.3385 0.3432 0.3353 0.0526  0.0354  -0.0152 879  LEU A N   
6356  C CA  . LEU A 881  ? 0.3590 0.3574 0.3492 0.0474  0.0359  -0.0075 879  LEU A CA  
6357  C C   . LEU A 881  ? 0.3584 0.3443 0.3530 0.0448  0.0328  -0.0037 879  LEU A C   
6358  O O   . LEU A 881  ? 0.3317 0.3105 0.3221 0.0416  0.0318  -0.0002 879  LEU A O   
6359  C CB  . LEU A 881  ? 0.3296 0.3351 0.3154 0.0447  0.0394  -0.0011 879  LEU A CB  
6360  C CG  . LEU A 881  ? 0.3678 0.3682 0.3471 0.0396  0.0400  0.0065  879  LEU A CG  
6361  C CD1 . LEU A 881  ? 0.3687 0.3713 0.3406 0.0395  0.0407  0.0054  879  LEU A CD1 
6362  C CD2 . LEU A 881  ? 0.3558 0.3617 0.3342 0.0370  0.0426  0.0126  879  LEU A CD2 
6363  N N   . SER A 882  ? 0.3529 0.3367 0.3560 0.0463  0.0310  -0.0044 880  SER A N   
6364  C CA  . SER A 882  ? 0.3955 0.3690 0.4028 0.0435  0.0282  0.0002  880  SER A CA  
6365  C C   . SER A 882  ? 0.3609 0.3256 0.3712 0.0438  0.0245  -0.0023 880  SER A C   
6366  O O   . SER A 882  ? 0.3872 0.3440 0.3996 0.0408  0.0222  0.0024  880  SER A O   
6367  C CB  . SER A 882  ? 0.3651 0.3395 0.3811 0.0451  0.0271  0.0006  880  SER A CB  
6368  O OG  . SER A 882  ? 0.3897 0.3650 0.4136 0.0499  0.0249  -0.0069 880  SER A OG  
6369  N N   . VAL A 883  ? 0.3424 0.3086 0.3533 0.0471  0.0236  -0.0095 881  VAL A N   
6370  C CA  . VAL A 883  ? 0.3438 0.3016 0.3589 0.0473  0.0198  -0.0121 881  VAL A CA  
6371  C C   . VAL A 883  ? 0.3601 0.3138 0.3670 0.0435  0.0202  -0.0084 881  VAL A C   
6372  O O   . VAL A 883  ? 0.3534 0.3124 0.3521 0.0433  0.0229  -0.0090 881  VAL A O   
6373  C CB  . VAL A 883  ? 0.3438 0.3050 0.3631 0.0525  0.0183  -0.0221 881  VAL A CB  
6374  C CG1 . VAL A 883  ? 0.3316 0.2845 0.3538 0.0521  0.0146  -0.0247 881  VAL A CG1 
6375  C CG2 . VAL A 883  ? 0.3680 0.3310 0.3979 0.0563  0.0167  -0.0260 881  VAL A CG2 
6376  N N   . ASP A 884  ? 0.3316 0.2765 0.3413 0.0405  0.0175  -0.0044 882  ASP A N   
6377  C CA  . ASP A 884  ? 0.3749 0.3162 0.3779 0.0371  0.0176  -0.0012 882  ASP A CA  
6378  C C   . ASP A 884  ? 0.3595 0.2977 0.3637 0.0385  0.0153  -0.0067 882  ASP A C   
6379  O O   . ASP A 884  ? 0.3514 0.2902 0.3483 0.0373  0.0163  -0.0069 882  ASP A O   
6380  C CB  . ASP A 884  ? 0.3586 0.2937 0.3633 0.0329  0.0162  0.0060  882  ASP A CB  
6381  C CG  . ASP A 884  ? 0.3900 0.3282 0.3935 0.0313  0.0182  0.0112  882  ASP A CG  
6382  O OD1 . ASP A 884  ? 0.3936 0.3365 0.3899 0.0304  0.0214  0.0126  882  ASP A OD1 
6383  O OD2 . ASP A 884  ? 0.3589 0.2947 0.3691 0.0308  0.0164  0.0141  882  ASP A OD2 
6384  N N   . VAL A 885  ? 0.3152 0.2496 0.3290 0.0408  0.0117  -0.0108 883  VAL A N   
6385  C CA  . VAL A 885  ? 0.3375 0.2674 0.3547 0.0417  0.0085  -0.0157 883  VAL A CA  
6386  C C   . VAL A 885  ? 0.3321 0.2645 0.3571 0.0469  0.0066  -0.0246 883  VAL A C   
6387  O O   . VAL A 885  ? 0.3322 0.2634 0.3659 0.0487  0.0049  -0.0252 883  VAL A O   
6388  C CB  . VAL A 885  ? 0.3802 0.3011 0.4036 0.0383  0.0049  -0.0108 883  VAL A CB  
6389  C CG1 . VAL A 885  ? 0.3532 0.2697 0.3815 0.0392  0.0013  -0.0160 883  VAL A CG1 
6390  C CG2 . VAL A 885  ? 0.3526 0.2725 0.3686 0.0335  0.0068  -0.0028 883  VAL A CG2 
6391  N N   . GLY A 886  ? 0.3530 0.2888 0.3753 0.0496  0.0065  -0.0319 884  GLY A N   
6392  C CA  . GLY A 886  ? 0.3035 0.2430 0.3327 0.0549  0.0047  -0.0416 884  GLY A CA  
6393  C C   . GLY A 886  ? 0.3583 0.2899 0.3979 0.0559  -0.0007 -0.0464 884  GLY A C   
6394  O O   . GLY A 886  ? 0.3524 0.2750 0.3963 0.0523  -0.0034 -0.0410 884  GLY A O   
6395  N N   . PRO A 887  ? 0.3426 0.2782 0.3867 0.0609  -0.0024 -0.0570 885  PRO A N   
6396  C CA  . PRO A 887  ? 0.3533 0.2815 0.4087 0.0622  -0.0081 -0.0627 885  PRO A CA  
6397  C C   . PRO A 887  ? 0.3648 0.2911 0.4151 0.0604  -0.0089 -0.0642 885  PRO A C   
6398  O O   . PRO A 887  ? 0.3570 0.2896 0.3951 0.0596  -0.0053 -0.0635 885  PRO A O   
6399  C CB  . PRO A 887  ? 0.3917 0.3267 0.4535 0.0689  -0.0092 -0.0745 885  PRO A CB  
6400  C CG  . PRO A 887  ? 0.3472 0.2955 0.3958 0.0704  -0.0035 -0.0762 885  PRO A CG  
6401  C CD  . PRO A 887  ? 0.3714 0.3193 0.4108 0.0655  0.0007  -0.0643 885  PRO A CD  
6402  N N   . VAL A 888  ? 0.3852 0.3027 0.4458 0.0597  -0.0142 -0.0662 886  VAL A N   
6403  C CA  . VAL A 888  ? 0.3820 0.2983 0.4402 0.0591  -0.0159 -0.0702 886  VAL A CA  
6404  C C   . VAL A 888  ? 0.3734 0.2966 0.4344 0.0651  -0.0174 -0.0836 886  VAL A C   
6405  O O   . VAL A 888  ? 0.3782 0.3051 0.4459 0.0696  -0.0181 -0.0899 886  VAL A O   
6406  C CB  . VAL A 888  ? 0.3284 0.2331 0.3965 0.0553  -0.0209 -0.0661 886  VAL A CB  
6407  C CG1 . VAL A 888  ? 0.3077 0.2080 0.3723 0.0495  -0.0191 -0.0531 886  VAL A CG1 
6408  C CG2 . VAL A 888  ? 0.3396 0.2382 0.4247 0.0579  -0.0266 -0.0711 886  VAL A CG2 
6409  N N   . ILE A 889  ? 0.3708 0.2966 0.4264 0.0653  -0.0177 -0.0883 887  ILE A N   
6410  C CA  . ILE A 889  ? 0.3885 0.3255 0.4406 0.0707  -0.0169 -0.0997 887  ILE A CA  
6411  C C   . ILE A 889  ? 0.3894 0.3250 0.4561 0.0759  -0.0222 -0.1116 887  ILE A C   
6412  O O   . ILE A 889  ? 0.4137 0.3597 0.4802 0.0814  -0.0212 -0.1209 887  ILE A O   
6413  C CB  . ILE A 889  ? 0.3971 0.3375 0.4392 0.0694  -0.0161 -0.1011 887  ILE A CB  
6414  C CG1 . ILE A 889  ? 0.4126 0.3669 0.4488 0.0748  -0.0145 -0.1118 887  ILE A CG1 
6415  C CG2 . ILE A 889  ? 0.3886 0.3190 0.4396 0.0673  -0.0216 -0.1027 887  ILE A CG2 
6416  C CD1 . ILE A 889  ? 0.3770 0.3431 0.4020 0.0758  -0.0084 -0.1085 887  ILE A CD1 
6417  N N   . THR A 890  ? 0.3727 0.2965 0.4528 0.0744  -0.0281 -0.1119 888  THR A N   
6418  C CA  . THR A 890  ? 0.3863 0.3077 0.4821 0.0793  -0.0339 -0.1235 888  THR A CA  
6419  C C   . THR A 890  ? 0.3989 0.3063 0.5105 0.0768  -0.0392 -0.1183 888  THR A C   
6420  O O   . THR A 890  ? 0.3708 0.2706 0.4814 0.0710  -0.0388 -0.1061 888  THR A O   
6421  C CB  . THR A 890  ? 0.4220 0.3440 0.5200 0.0809  -0.0377 -0.1333 888  THR A CB  
6422  O OG1 . THR A 890  ? 0.4078 0.3199 0.5062 0.0749  -0.0396 -0.1253 888  THR A OG1 
6423  C CG2 . THR A 890  ? 0.4174 0.3541 0.5010 0.0839  -0.0334 -0.1398 888  THR A CG2 
6424  N N   . SER A 891  ? 0.3991 0.3038 0.5264 0.0815  -0.0447 -0.1281 889  SER A N   
6425  C CA  . SER A 891  ? 0.3953 0.2865 0.5400 0.0794  -0.0509 -0.1241 889  SER A CA  
6426  C C   . SER A 891  ? 0.4292 0.3111 0.5777 0.0743  -0.0547 -0.1198 889  SER A C   
6427  O O   . SER A 891  ? 0.4239 0.2954 0.5809 0.0695  -0.0576 -0.1099 889  SER A O   
6428  C CB  . SER A 891  ? 0.4420 0.3324 0.6037 0.0860  -0.0566 -0.1369 889  SER A CB  
6429  N N   . GLU A 892  ? 0.4570 0.3432 0.5995 0.0750  -0.0547 -0.1268 890  GLU A N   
6430  C CA  . GLU A 892  ? 0.4634 0.3417 0.6093 0.0701  -0.0581 -0.1231 890  GLU A CA  
6431  C C   . GLU A 892  ? 0.4572 0.3337 0.5914 0.0632  -0.0537 -0.1081 890  GLU A C   
6432  O O   . GLU A 892  ? 0.4247 0.2921 0.5658 0.0578  -0.0567 -0.0996 890  GLU A O   
6433  C CB  . GLU A 892  ? 0.4534 0.3381 0.5949 0.0729  -0.0589 -0.1347 890  GLU A CB  
6434  C CG  . GLU A 892  ? 0.5746 0.4640 0.7258 0.0804  -0.0629 -0.1515 890  GLU A CG  
6435  C CD  . GLU A 892  ? 0.5516 0.4550 0.6922 0.0860  -0.0575 -0.1578 890  GLU A CD  
6436  O OE1 . GLU A 892  ? 0.5654 0.4691 0.7078 0.0871  -0.0556 -0.1539 890  GLU A OE1 
6437  O OE2 . GLU A 892  ? 0.6818 0.5967 0.8125 0.0893  -0.0552 -0.1664 890  GLU A OE2 
6438  N N   . ALA A 893  ? 0.3991 0.2848 0.5159 0.0631  -0.0467 -0.1049 891  ALA A N   
6439  C CA  . ALA A 893  ? 0.3833 0.2678 0.4892 0.0571  -0.0424 -0.0915 891  ALA A CA  
6440  C C   . ALA A 893  ? 0.4126 0.2897 0.5263 0.0538  -0.0435 -0.0810 891  ALA A C   
6441  O O   . ALA A 893  ? 0.4102 0.2813 0.5253 0.0481  -0.0443 -0.0710 891  ALA A O   
6442  C CB  . ALA A 893  ? 0.3644 0.2599 0.4524 0.0583  -0.0352 -0.0903 891  ALA A CB  
6443  N N   . LYS A 894  ? 0.3667 0.2450 0.4857 0.0575  -0.0435 -0.0833 892  LYS A N   
6444  C CA  . LYS A 894  ? 0.4118 0.2837 0.5392 0.0550  -0.0450 -0.0741 892  LYS A CA  
6445  C C   . LYS A 894  ? 0.4387 0.2993 0.5820 0.0516  -0.0518 -0.0703 892  LYS A C   
6446  O O   . LYS A 894  ? 0.4148 0.2708 0.5589 0.0459  -0.0519 -0.0582 892  LYS A O   
6447  C CB  . LYS A 894  ? 0.3444 0.2194 0.4778 0.0606  -0.0452 -0.0799 892  LYS A CB  
6448  C CG  . LYS A 894  ? 0.3565 0.2261 0.4974 0.0584  -0.0464 -0.0703 892  LYS A CG  
6449  C CD  . LYS A 894  ? 0.4121 0.2842 0.5617 0.0645  -0.0477 -0.0777 892  LYS A CD  
6450  C CE  . LYS A 894  ? 0.4138 0.2800 0.5728 0.0625  -0.0498 -0.0682 892  LYS A CE  
6451  N NZ  . LYS A 894  ? 0.4969 0.3644 0.6671 0.0687  -0.0523 -0.0762 892  LYS A NZ  
6452  N N   . ASP A 895  ? 0.4452 0.3020 0.6018 0.0550  -0.0577 -0.0806 893  ASP A N   
6453  C CA  . ASP A 895  ? 0.4561 0.3020 0.6297 0.0517  -0.0648 -0.0772 893  ASP A CA  
6454  C C   . ASP A 895  ? 0.4258 0.2694 0.5942 0.0452  -0.0643 -0.0689 893  ASP A C   
6455  O O   . ASP A 895  ? 0.4449 0.2817 0.6210 0.0398  -0.0671 -0.0582 893  ASP A O   
6456  C CB  . ASP A 895  ? 0.4730 0.3158 0.6612 0.0567  -0.0713 -0.0912 893  ASP A CB  
6457  C CG  . ASP A 895  ? 0.5976 0.4428 0.7933 0.0637  -0.0725 -0.1004 893  ASP A CG  
6458  O OD1 . ASP A 895  ? 0.6233 0.4695 0.8176 0.0638  -0.0701 -0.0941 893  ASP A OD1 
6459  O OD2 . ASP A 895  ? 0.6204 0.4698 0.8217 0.0681  -0.0754 -0.1130 893  ASP A OD2 
6460  N N   . ASN A 896  ? 0.3968 0.2467 0.5522 0.0455  -0.0608 -0.0735 894  ASN A N   
6461  C CA  . ASN A 896  ? 0.4072 0.2559 0.5570 0.0397  -0.0600 -0.0664 894  ASN A CA  
6462  C C   . ASN A 896  ? 0.4404 0.2898 0.5820 0.0343  -0.0558 -0.0520 894  ASN A C   
6463  O O   . ASN A 896  ? 0.4108 0.2557 0.5569 0.0286  -0.0578 -0.0427 894  ASN A O   
6464  C CB  . ASN A 896  ? 0.4406 0.2970 0.5768 0.0417  -0.0566 -0.0739 894  ASN A CB  
6465  C CG  . ASN A 896  ? 0.5419 0.3978 0.6720 0.0361  -0.0556 -0.0673 894  ASN A CG  
6466  O OD1 . ASN A 896  ? 0.5567 0.4170 0.6733 0.0332  -0.0502 -0.0596 894  ASN A OD1 
6467  N ND2 . ASN A 896  ? 0.5565 0.4074 0.6973 0.0345  -0.0610 -0.0705 894  ASN A ND2 
6468  N N   . ILE A 897  ? 0.4067 0.2622 0.5366 0.0360  -0.0502 -0.0500 895  ILE A N   
6469  C CA  . ILE A 897  ? 0.4183 0.2754 0.5398 0.0314  -0.0461 -0.0375 895  ILE A CA  
6470  C C   . ILE A 897  ? 0.4291 0.2797 0.5635 0.0285  -0.0498 -0.0286 895  ILE A C   
6471  O O   . ILE A 897  ? 0.4124 0.2618 0.5464 0.0228  -0.0496 -0.0176 895  ILE A O   
6472  C CB  . ILE A 897  ? 0.3823 0.2474 0.4897 0.0342  -0.0397 -0.0384 895  ILE A CB  
6473  C CG1 . ILE A 897  ? 0.3931 0.2652 0.4874 0.0364  -0.0361 -0.0454 895  ILE A CG1 
6474  C CG2 . ILE A 897  ? 0.4085 0.2751 0.5086 0.0298  -0.0360 -0.0262 895  ILE A CG2 
6475  C CD1 . ILE A 897  ? 0.3819 0.2621 0.4653 0.0404  -0.0309 -0.0490 895  ILE A CD1 
6476  N N   . GLU A 898  ? 0.3955 0.2427 0.5419 0.0324  -0.0534 -0.0332 896  GLU A N   
6477  C CA  . GLU A 898  ? 0.4222 0.2634 0.5816 0.0298  -0.0574 -0.0244 896  GLU A CA  
6478  C C   . GLU A 898  ? 0.4664 0.3000 0.6392 0.0252  -0.0634 -0.0195 896  GLU A C   
6479  O O   . GLU A 898  ? 0.4533 0.2842 0.6317 0.0203  -0.0651 -0.0077 896  GLU A O   
6480  C CB  . GLU A 898  ? 0.4420 0.2813 0.6117 0.0356  -0.0600 -0.0312 896  GLU A CB  
6481  C CG  . GLU A 898  ? 0.4479 0.2953 0.6049 0.0388  -0.0538 -0.0325 896  GLU A CG  
6482  C CD  . GLU A 898  ? 0.5277 0.3747 0.6943 0.0448  -0.0560 -0.0394 896  GLU A CD  
6483  O OE1 . GLU A 898  ? 0.5612 0.4035 0.7419 0.0483  -0.0616 -0.0481 896  GLU A OE1 
6484  O OE2 . GLU A 898  ? 0.5739 0.4257 0.7341 0.0460  -0.0521 -0.0365 896  GLU A OE2 
6485  N N   . LYS A 899  ? 0.4204 0.2514 0.5986 0.0265  -0.0668 -0.0281 897  LYS A N   
6486  C CA  . LYS A 899  ? 0.4411 0.2654 0.6322 0.0216  -0.0725 -0.0232 897  LYS A CA  
6487  C C   . LYS A 899  ? 0.4588 0.2864 0.6404 0.0147  -0.0691 -0.0113 897  LYS A C   
6488  O O   . LYS A 899  ? 0.4884 0.3122 0.6794 0.0093  -0.0726 -0.0009 897  LYS A O   
6489  C CB  . LYS A 899  ? 0.4615 0.2833 0.6587 0.0244  -0.0764 -0.0355 897  LYS A CB  
6490  N N   . HIS A 900  ? 0.4466 0.2819 0.6097 0.0150  -0.0625 -0.0124 898  HIS A N   
6491  C CA  . HIS A 900  ? 0.4703 0.3099 0.6237 0.0090  -0.0589 -0.0020 898  HIS A CA  
6492  C C   . HIS A 900  ? 0.4225 0.2634 0.5758 0.0057  -0.0576 0.0102  898  HIS A C   
6493  O O   . HIS A 900  ? 0.4546 0.2954 0.6118 -0.0002 -0.0590 0.0208  898  HIS A O   
6494  C CB  . HIS A 900  ? 0.4676 0.3149 0.6022 0.0107  -0.0524 -0.0064 898  HIS A CB  
6495  C CG  . HIS A 900  ? 0.4759 0.3284 0.5998 0.0055  -0.0483 0.0033  898  HIS A CG  
6496  N ND1 . HIS A 900  ? 0.4553 0.3085 0.5798 0.0011  -0.0493 0.0066  898  HIS A ND1 
6497  C CD2 . HIS A 900  ? 0.4796 0.3376 0.5926 0.0042  -0.0433 0.0100  898  HIS A CD2 
6498  C CE1 . HIS A 900  ? 0.4867 0.3458 0.6008 -0.0025 -0.0450 0.0147  898  HIS A CE1 
6499  N NE2 . HIS A 900  ? 0.4594 0.3213 0.5664 -0.0007 -0.0414 0.0167  898  HIS A NE2 
6500  N N   . ILE A 901  ? 0.4067 0.2497 0.5554 0.0093  -0.0548 0.0090  899  ILE A N   
6501  C CA  . ILE A 901  ? 0.4380 0.2831 0.5857 0.0064  -0.0534 0.0200  899  ILE A CA  
6502  C C   . ILE A 901  ? 0.4334 0.2722 0.5989 0.0031  -0.0599 0.0280  899  ILE A C   
6503  O O   . ILE A 901  ? 0.4457 0.2867 0.6115 -0.0022 -0.0598 0.0401  899  ILE A O   
6504  C CB  . ILE A 901  ? 0.4207 0.2685 0.5626 0.0114  -0.0501 0.0160  899  ILE A CB  
6505  C CG1 . ILE A 901  ? 0.3954 0.2501 0.5196 0.0139  -0.0437 0.0098  899  ILE A CG1 
6506  C CG2 . ILE A 901  ? 0.3976 0.2473 0.5399 0.0086  -0.0494 0.0272  899  ILE A CG2 
6507  C CD1 . ILE A 901  ? 0.3865 0.2445 0.5054 0.0193  -0.0406 0.0037  899  ILE A CD1 
6508  N N   . GLU A 902  ? 0.4539 0.2851 0.6347 0.0061  -0.0659 0.0216  900  GLU A N   
6509  C CA  . GLU A 902  ? 0.4924 0.3168 0.6915 0.0030  -0.0726 0.0295  900  GLU A CA  
6510  C C   . GLU A 902  ? 0.4722 0.2966 0.6760 -0.0036 -0.0751 0.0371  900  GLU A C   
6511  O O   . GLU A 902  ? 0.4882 0.3157 0.6981 -0.0085 -0.0772 0.0482  900  GLU A O   
6512  C CB  . GLU A 902  ? 0.4783 0.2979 0.6911 0.0082  -0.0778 0.0195  900  GLU A CB  
6513  C CG  . GLU A 902  ? 0.5453 0.3652 0.7565 0.0139  -0.0761 0.0151  900  GLU A CG  
6514  C CD  . GLU A 902  ? 0.5845 0.4077 0.7926 0.0108  -0.0741 0.0277  900  GLU A CD  
6515  O OE1 . GLU A 902  ? 0.5806 0.4050 0.7972 0.0062  -0.0774 0.0375  900  GLU A OE1 
6516  O OE2 . GLU A 902  ? 0.5423 0.3706 0.7373 0.0127  -0.0684 0.0275  900  GLU A OE2 
6517  N N   . ARG A 903  ? 0.4659 0.2904 0.6653 -0.0038 -0.0743 0.0309  901  ARG A N   
6518  C CA  . ARG A 903  ? 0.5089 0.3339 0.7119 -0.0103 -0.0762 0.0385  901  ARG A CA  
6519  C C   . ARG A 903  ? 0.4951 0.3285 0.6875 -0.0157 -0.0716 0.0513  901  ARG A C   
6520  O O   . ARG A 903  ? 0.4356 0.2715 0.6349 -0.0213 -0.0739 0.0625  901  ARG A O   
6521  C CB  . ARG A 903  ? 0.5316 0.3576 0.7289 -0.0091 -0.0751 0.0288  901  ARG A CB  
6522  C CG  . ARG A 903  ? 0.5827 0.4012 0.7947 -0.0061 -0.0815 0.0187  901  ARG A CG  
6523  C CD  . ARG A 903  ? 0.6083 0.4272 0.8171 -0.0065 -0.0815 0.0116  901  ARG A CD  
6524  N NE  . ARG A 903  ? 0.6932 0.5185 0.8838 -0.0020 -0.0752 0.0024  901  ARG A NE  
6525  C CZ  . ARG A 903  ? 0.6179 0.4426 0.8064 0.0048  -0.0749 -0.0104 901  ARG A CZ  
6526  N NH1 . ARG A 903  ? 0.6577 0.4758 0.8607 0.0085  -0.0803 -0.0166 901  ARG A NH1 
6527  N NH2 . ARG A 903  ? 0.5266 0.3581 0.6984 0.0079  -0.0693 -0.0172 901  ARG A NH2 
6528  N N   . MET A 904  ? 0.4584 0.2992 0.6324 -0.0137 -0.0645 0.0489  902  MET A N   
6529  C CA  . MET A 904  ? 0.4773 0.3269 0.6405 -0.0181 -0.0599 0.0595  902  MET A CA  
6530  C C   . MET A 904  ? 0.4678 0.3173 0.6384 -0.0203 -0.0620 0.0701  902  MET A C   
6531  O O   . MET A 904  ? 0.4637 0.3186 0.6346 -0.0260 -0.0619 0.0819  902  MET A O   
6532  C CB  . MET A 904  ? 0.4405 0.2965 0.5846 -0.0147 -0.0527 0.0539  902  MET A CB  
6533  C CG  . MET A 904  ? 0.4713 0.3288 0.6062 -0.0128 -0.0501 0.0447  902  MET A CG  
6534  S SD  . MET A 904  ? 0.5390 0.4014 0.6724 -0.0193 -0.0499 0.0511  902  MET A SD  
6535  C CE  . MET A 904  ? 0.5721 0.4256 0.7227 -0.0194 -0.0571 0.0458  902  MET A CE  
6536  N N   . ARG A 905  ? 0.4303 0.2748 0.6067 -0.0158 -0.0638 0.0663  903  ARG A N   
6537  C CA  A ARG A 905  ? 0.4534 0.2982 0.6375 -0.0176 -0.0662 0.0761  903  ARG A CA  
6538  C CA  B ARG A 905  ? 0.4535 0.2983 0.6376 -0.0176 -0.0662 0.0761  903  ARG A CA  
6539  C C   . ARG A 905  ? 0.4758 0.3222 0.6732 -0.0220 -0.0715 0.0826  903  ARG A C   
6540  O O   . ARG A 905  ? 0.4773 0.3308 0.6756 -0.0265 -0.0718 0.0939  903  ARG A O   
6541  C CB  A ARG A 905  ? 0.4682 0.3084 0.6563 -0.0113 -0.0673 0.0691  903  ARG A CB  
6542  C CB  B ARG A 905  ? 0.4683 0.3085 0.6562 -0.0113 -0.0672 0.0691  903  ARG A CB  
6543  C CG  A ARG A 905  ? 0.4762 0.3211 0.6650 -0.0123 -0.0670 0.0777  903  ARG A CG  
6544  C CG  B ARG A 905  ? 0.4764 0.3214 0.6646 -0.0122 -0.0668 0.0776  903  ARG A CG  
6545  C CD  A ARG A 905  ? 0.4729 0.3133 0.6690 -0.0064 -0.0693 0.0710  903  ARG A CD  
6546  C CD  B ARG A 905  ? 0.4758 0.3167 0.6668 -0.0057 -0.0672 0.0702  903  ARG A CD  
6547  N NE  A ARG A 905  ? 0.4713 0.3077 0.6613 -0.0001 -0.0665 0.0588  903  ARG A NE  
6548  N NE  B ARG A 905  ? 0.4754 0.3216 0.6531 -0.0041 -0.0615 0.0714  903  ARG A NE  
6549  C CZ  A ARG A 905  ? 0.4809 0.3240 0.6559 0.0022  -0.0602 0.0565  903  ARG A CZ  
6550  C CZ  B ARG A 905  ? 0.4735 0.3211 0.6421 0.0014  -0.0575 0.0609  903  ARG A CZ  
6551  N NH1 A ARG A 905  ? 0.4707 0.3205 0.6377 -0.0011 -0.0571 0.0662  903  ARG A NH1 
6552  N NH1 B ARG A 905  ? 0.4764 0.3193 0.6486 0.0063  -0.0588 0.0489  903  ARG A NH1 
6553  N NH2 A ARG A 905  ? 0.4781 0.3218 0.6463 0.0079  -0.0572 0.0443  903  ARG A NH2 
6554  N NH2 B ARG A 905  ? 0.4664 0.3211 0.6225 0.0021  -0.0522 0.0626  903  ARG A NH2 
6555  N N   . GLY A 906  ? 0.4807 0.3212 0.6885 -0.0207 -0.0759 0.0756  904  GLY A N   
6556  C CA  . GLY A 906  ? 0.4617 0.3034 0.6835 -0.0248 -0.0814 0.0815  904  GLY A CA  
6557  C C   . GLY A 906  ? 0.5069 0.3558 0.7254 -0.0316 -0.0802 0.0914  904  GLY A C   
6558  O O   . GLY A 906  ? 0.5418 0.3946 0.7700 -0.0360 -0.0839 0.1001  904  GLY A O   
6559  N N   . LEU A 907  ? 0.5088 0.3601 0.7141 -0.0327 -0.0753 0.0903  905  LEU A N   
6560  C CA  . LEU A 907  ? 0.5107 0.3704 0.7114 -0.0390 -0.0734 0.0995  905  LEU A CA  
6561  C C   . LEU A 907  ? 0.5071 0.3771 0.6990 -0.0421 -0.0696 0.1103  905  LEU A C   
6562  O O   . LEU A 907  ? 0.5311 0.4101 0.7183 -0.0472 -0.0676 0.1180  905  LEU A O   
6563  C CB  . LEU A 907  ? 0.4939 0.3521 0.6850 -0.0388 -0.0700 0.0934  905  LEU A CB  
6564  C CG  . LEU A 907  ? 0.5415 0.3915 0.7408 -0.0365 -0.0737 0.0830  905  LEU A CG  
6565  C CD1 . LEU A 907  ? 0.4897 0.3402 0.6765 -0.0351 -0.0695 0.0753  905  LEU A CD1 
6566  C CD2 . LEU A 907  ? 0.5467 0.3987 0.7592 -0.0413 -0.0788 0.0886  905  LEU A CD2 
6567  N N   . GLY A 908  ? 0.4819 0.3516 0.6718 -0.0391 -0.0687 0.1107  906  GLY A N   
6568  C CA  . GLY A 908  ? 0.5005 0.3802 0.6825 -0.0416 -0.0655 0.1201  906  GLY A CA  
6569  C C   . GLY A 908  ? 0.4631 0.3465 0.6285 -0.0407 -0.0591 0.1186  906  GLY A C   
6570  O O   . GLY A 908  ? 0.5015 0.3947 0.6593 -0.0431 -0.0561 0.1261  906  GLY A O   
6571  N N   . ARG A 909  ? 0.4668 0.3429 0.6266 -0.0372 -0.0570 0.1091  907  ARG A N   
6572  C CA  . ARG A 909  ? 0.4707 0.3540 0.6121 -0.0348 -0.0500 0.1041  907  ARG A CA  
6573  C C   . ARG A 909  ? 0.4688 0.3520 0.6062 -0.0310 -0.0483 0.1031  907  ARG A C   
6574  O O   . ARG A 909  ? 0.4804 0.3555 0.6271 -0.0276 -0.0517 0.0999  907  ARG A O   
6575  C CB  . ARG A 909  ? 0.4740 0.3539 0.6083 -0.0308 -0.0477 0.0914  907  ARG A CB  
6576  C CG  . ARG A 909  ? 0.4933 0.3721 0.6329 -0.0339 -0.0500 0.0910  907  ARG A CG  
6577  C CD  . ARG A 909  ? 0.5755 0.4653 0.7045 -0.0380 -0.0459 0.0955  907  ARG A CD  
6578  N NE  . ARG A 909  ? 0.6304 0.5212 0.7671 -0.0427 -0.0488 0.0994  907  ARG A NE  
6579  C CZ  . ARG A 909  ? 0.6603 0.5458 0.8002 -0.0415 -0.0505 0.0918  907  ARG A CZ  
6580  N NH1 . ARG A 909  ? 0.6919 0.5710 0.8280 -0.0357 -0.0497 0.0797  907  ARG A NH1 
6581  N NH2 . ARG A 909  ? 0.6849 0.5725 0.8322 -0.0465 -0.0530 0.0966  907  ARG A NH2 
6582  N N   . LYS A 910  ? 0.4087 0.3011 0.5327 -0.0315 -0.0431 0.1054  908  LYS A N   
6583  C CA  . LYS A 910  ? 0.4354 0.3284 0.5546 -0.0279 -0.0411 0.1039  908  LYS A CA  
6584  C C   . LYS A 910  ? 0.4091 0.2965 0.5226 -0.0216 -0.0387 0.0910  908  LYS A C   
6585  O O   . LYS A 910  ? 0.3994 0.2885 0.5033 -0.0205 -0.0353 0.0842  908  LYS A O   
6586  C CB  . LYS A 910  ? 0.4644 0.3690 0.5710 -0.0301 -0.0364 0.1090  908  LYS A CB  
6587  C CG  . LYS A 910  ? 0.4906 0.4028 0.6021 -0.0357 -0.0384 0.1223  908  LYS A CG  
6588  C CD  . LYS A 910  ? 0.5353 0.4592 0.6342 -0.0367 -0.0338 0.1255  908  LYS A CD  
6589  C CE  . LYS A 910  ? 0.5990 0.5209 0.6945 -0.0324 -0.0324 0.1220  908  LYS A CE  
6590  N NZ  . LYS A 910  ? 0.6508 0.5842 0.7380 -0.0343 -0.0296 0.1277  908  LYS A NZ  
6591  N N   . VAL A 911  ? 0.3834 0.2651 0.5032 -0.0176 -0.0406 0.0877  909  VAL A N   
6592  C CA  . VAL A 911  ? 0.3620 0.2392 0.4780 -0.0115 -0.0389 0.0756  909  VAL A CA  
6593  C C   . VAL A 911  ? 0.3857 0.2653 0.4976 -0.0085 -0.0366 0.0754  909  VAL A C   
6594  O O   . VAL A 911  ? 0.3938 0.2716 0.5151 -0.0087 -0.0398 0.0808  909  VAL A O   
6595  C CB  . VAL A 911  ? 0.4031 0.2706 0.5330 -0.0086 -0.0441 0.0695  909  VAL A CB  
6596  C CG1 . VAL A 911  ? 0.4099 0.2750 0.5353 -0.0020 -0.0420 0.0569  909  VAL A CG1 
6597  C CG2 . VAL A 911  ? 0.3849 0.2499 0.5194 -0.0116 -0.0466 0.0692  909  VAL A CG2 
6598  N N   . GLU A 912  ? 0.3402 0.2239 0.4387 -0.0060 -0.0312 0.0696  910  GLU A N   
6599  C CA  . GLU A 912  ? 0.3782 0.2646 0.4718 -0.0031 -0.0285 0.0684  910  GLU A CA  
6600  C C   . GLU A 912  ? 0.3854 0.2680 0.4782 0.0028  -0.0275 0.0571  910  GLU A C   
6601  O O   . GLU A 912  ? 0.3743 0.2569 0.4605 0.0042  -0.0254 0.0503  910  GLU A O   
6602  C CB  . GLU A 912  ? 0.3943 0.2892 0.4737 -0.0050 -0.0233 0.0709  910  GLU A CB  
6603  C CG  . GLU A 912  ? 0.3915 0.2900 0.4664 -0.0029 -0.0208 0.0712  910  GLU A CG  
6604  C CD  . GLU A 912  ? 0.4181 0.3190 0.4998 -0.0054 -0.0235 0.0808  910  GLU A CD  
6605  O OE1 . GLU A 912  ? 0.4382 0.3396 0.5258 -0.0095 -0.0265 0.0882  910  GLU A OE1 
6606  O OE2 . GLU A 912  ? 0.4603 0.3631 0.5414 -0.0034 -0.0225 0.0811  910  GLU A OE2 
6607  N N   . GLN A 913  ? 0.3647 0.2448 0.4645 0.0063  -0.0292 0.0551  911  GLN A N   
6608  C CA  . GLN A 913  ? 0.3919 0.2704 0.4910 0.0121  -0.0281 0.0443  911  GLN A CA  
6609  C C   . GLN A 913  ? 0.4324 0.3141 0.5301 0.0148  -0.0262 0.0442  911  GLN A C   
6610  O O   . GLN A 913  ? 0.3872 0.2686 0.4919 0.0136  -0.0286 0.0509  911  GLN A O   
6611  C CB  . GLN A 913  ? 0.4153 0.2861 0.5285 0.0148  -0.0335 0.0387  911  GLN A CB  
6612  C CG  . GLN A 913  ? 0.4313 0.2982 0.5484 0.0123  -0.0362 0.0383  911  GLN A CG  
6613  C CD  . GLN A 913  ? 0.4203 0.2802 0.5507 0.0160  -0.0412 0.0304  911  GLN A CD  
6614  O OE1 . GLN A 913  ? 0.4476 0.3025 0.5920 0.0166  -0.0462 0.0327  911  GLN A OE1 
6615  N NE2 . GLN A 913  ? 0.3851 0.2448 0.5114 0.0186  -0.0402 0.0209  911  GLN A NE2 
6616  N N   . ILE A 914  ? 0.4313 0.3165 0.5204 0.0185  -0.0220 0.0368  912  ILE A N   
6617  C CA  . ILE A 914  ? 0.4605 0.3488 0.5496 0.0216  -0.0205 0.0356  912  ILE A CA  
6618  C C   . ILE A 914  ? 0.4883 0.3721 0.5909 0.0262  -0.0246 0.0299  912  ILE A C   
6619  O O   . ILE A 914  ? 0.4504 0.3300 0.5584 0.0284  -0.0271 0.0231  912  ILE A O   
6620  C CB  . ILE A 914  ? 0.4733 0.3677 0.5495 0.0237  -0.0147 0.0303  912  ILE A CB  
6621  C CG1 . ILE A 914  ? 0.4894 0.3831 0.5659 0.0283  -0.0144 0.0196  912  ILE A CG1 
6622  C CG2 . ILE A 914  ? 0.4426 0.3401 0.5067 0.0198  -0.0113 0.0337  912  ILE A CG2 
6623  C CD1 . ILE A 914  ? 0.4975 0.3978 0.5622 0.0302  -0.0091 0.0155  912  ILE A CD1 
6624  N N   . GLY A 915  ? 0.4998 0.3845 0.6083 0.0277  -0.0257 0.0323  913  GLY A N   
6625  C CA  . GLY A 915  ? 0.4878 0.3691 0.6090 0.0327  -0.0294 0.0261  913  GLY A CA  
6626  C C   . GLY A 915  ? 0.4904 0.3763 0.6062 0.0380  -0.0259 0.0152  913  GLY A C   
6627  O O   . GLY A 915  ? 0.5878 0.4804 0.6913 0.0379  -0.0205 0.0147  913  GLY A O   
6628  N N   . LEU A 916  ? 0.4515 0.3343 0.5769 0.0426  -0.0291 0.0062  914  LEU A N   
6629  C CA  . LEU A 916  ? 0.5119 0.4003 0.6332 0.0480  -0.0261 -0.0050 914  LEU A CA  
6630  C C   . LEU A 916  ? 0.4937 0.3847 0.6234 0.0528  -0.0271 -0.0087 914  LEU A C   
6631  O O   . LEU A 916  ? 0.4548 0.3403 0.5985 0.0536  -0.0323 -0.0065 914  LEU A O   
6632  C CB  . LEU A 916  ? 0.4817 0.3667 0.6075 0.0505  -0.0288 -0.0142 914  LEU A CB  
6633  C CG  . LEU A 916  ? 0.5046 0.3888 0.6204 0.0467  -0.0270 -0.0128 914  LEU A CG  
6634  C CD1 . LEU A 916  ? 0.4895 0.3742 0.6061 0.0505  -0.0279 -0.0243 914  LEU A CD1 
6635  C CD2 . LEU A 916  ? 0.4804 0.3716 0.5797 0.0440  -0.0206 -0.0081 914  LEU A CD2 
6636  N N   . ALA A 917  ? 0.5001 0.3999 0.6218 0.0560  -0.0223 -0.0142 915  ALA A N   
6637  C CA  . ALA A 917  ? 0.5474 0.4513 0.6768 0.0610  -0.0228 -0.0187 915  ALA A CA  
6638  C C   . ALA A 917  ? 0.5469 0.4484 0.6888 0.0668  -0.0272 -0.0300 915  ALA A C   
6639  O O   . ALA A 917  ? 0.5173 0.4163 0.6591 0.0673  -0.0286 -0.0358 915  ALA A O   
6640  C CB  . ALA A 917  ? 0.6104 0.5254 0.7278 0.0624  -0.0163 -0.0210 915  ALA A CB  
6641  N N   . SER A 918  ? 0.5194 0.4220 0.6729 0.0713  -0.0297 -0.0336 916  SER A N   
6642  C CA  . SER A 918  ? 0.5245 0.4248 0.6919 0.0772  -0.0346 -0.0449 916  SER A CA  
6643  C C   . SER A 918  ? 0.5255 0.4351 0.6858 0.0818  -0.0310 -0.0573 916  SER A C   
6644  O O   . SER A 918  ? 0.5230 0.4306 0.6913 0.0857  -0.0346 -0.0674 916  SER A O   
6645  C CB  . SER A 918  ? 0.5659 0.4662 0.7473 0.0813  -0.0379 -0.0461 916  SER A CB  
6646  O OG  . SER A 918  ? 0.5987 0.5108 0.7734 0.0846  -0.0327 -0.0499 916  SER A OG  
6647  N N   . GLU A 919  ? 0.5189 0.4392 0.6645 0.0813  -0.0241 -0.0567 917  GLU A N   
6648  C CA  . GLU A 919  ? 0.5687 0.4995 0.7065 0.0853  -0.0204 -0.0673 917  GLU A CA  
6649  C C   . GLU A 919  ? 0.5397 0.4675 0.6724 0.0839  -0.0210 -0.0708 917  GLU A C   
6650  O O   . GLU A 919  ? 0.5434 0.4777 0.6751 0.0883  -0.0205 -0.0819 917  GLU A O   
6651  C CB  . GLU A 919  ? 0.5999 0.5420 0.7229 0.0838  -0.0130 -0.0634 917  GLU A CB  
6652  C CG  . GLU A 919  ? 0.6361 0.5859 0.7636 0.0871  -0.0115 -0.0643 917  GLU A CG  
6653  C CD  . GLU A 919  ? 0.6983 0.6418 0.8301 0.0835  -0.0130 -0.0531 917  GLU A CD  
6654  O OE1 . GLU A 919  ? 0.6747 0.6069 0.8103 0.0795  -0.0167 -0.0460 917  GLU A OE1 
6655  O OE2 . GLU A 919  ? 0.7693 0.7199 0.9006 0.0846  -0.0104 -0.0513 917  GLU A OE2 
6656  N N   . THR A 920  ? 0.4901 0.4090 0.6193 0.0779  -0.0220 -0.0617 918  THR A N   
6657  C CA  . THR A 920  ? 0.4976 0.4137 0.6224 0.0765  -0.0228 -0.0650 918  THR A CA  
6658  C C   . THR A 920  ? 0.4660 0.3771 0.6052 0.0808  -0.0290 -0.0754 918  THR A C   
6659  O O   . THR A 920  ? 0.4574 0.3678 0.5939 0.0809  -0.0299 -0.0807 918  THR A O   
6660  C CB  . THR A 920  ? 0.4560 0.3639 0.5759 0.0694  -0.0231 -0.0533 918  THR A CB  
6661  O OG1 . THR A 920  ? 0.4667 0.3648 0.5997 0.0674  -0.0283 -0.0469 918  THR A OG1 
6662  C CG2 . THR A 920  ? 0.4226 0.3361 0.5274 0.0654  -0.0168 -0.0446 918  THR A CG2 
6663  N N   . GLY A 921  ? 0.4970 0.4048 0.6518 0.0846  -0.0336 -0.0788 919  GLY A N   
6664  C CA  . GLY A 921  ? 0.4756 0.3772 0.6464 0.0885  -0.0405 -0.0883 919  GLY A CA  
6665  C C   . GLY A 921  ? 0.4617 0.3719 0.6301 0.0941  -0.0397 -0.1031 919  GLY A C   
6666  O O   . GLY A 921  ? 0.4550 0.3600 0.6319 0.0957  -0.0446 -0.1105 919  GLY A O   
6667  N N   . VAL A 922  ? 0.4333 0.3574 0.5902 0.0970  -0.0336 -0.1075 920  VAL A N   
6668  C CA  . VAL A 922  ? 0.4359 0.3707 0.5904 0.1027  -0.0326 -0.1218 920  VAL A CA  
6669  C C   . VAL A 922  ? 0.4359 0.3736 0.5765 0.0998  -0.0298 -0.1219 920  VAL A C   
6670  O O   . VAL A 922  ? 0.4443 0.3911 0.5821 0.1041  -0.0292 -0.1334 920  VAL A O   
6671  C CB  . VAL A 922  ? 0.4553 0.4058 0.6042 0.1072  -0.0274 -0.1267 920  VAL A CB  
6672  C CG1 . VAL A 922  ? 0.4372 0.3868 0.6026 0.1123  -0.0313 -0.1315 920  VAL A CG1 
6673  C CG2 . VAL A 922  ? 0.4741 0.4291 0.6076 0.1021  -0.0207 -0.1144 920  VAL A CG2 
6674  N N   . GLY A 923  ? 0.4168 0.3478 0.5488 0.0929  -0.0280 -0.1097 921  GLY A N   
6675  C CA  . GLY A 923  ? 0.4339 0.3662 0.5537 0.0899  -0.0259 -0.1090 921  GLY A CA  
6676  C C   . GLY A 923  ? 0.4205 0.3390 0.5451 0.0847  -0.0302 -0.1025 921  GLY A C   
6677  O O   . GLY A 923  ? 0.3909 0.2989 0.5300 0.0840  -0.0356 -0.1002 921  GLY A O   
6678  N N   . THR A 924  ? 0.4023 0.3210 0.5154 0.0808  -0.0279 -0.0990 922  THR A N   
6679  C CA  . THR A 924  ? 0.3752 0.2824 0.4921 0.0759  -0.0316 -0.0933 922  THR A CA  
6680  C C   . THR A 924  ? 0.3585 0.2638 0.4637 0.0693  -0.0274 -0.0793 922  THR A C   
6681  O O   . THR A 924  ? 0.3342 0.2447 0.4255 0.0673  -0.0232 -0.0774 922  THR A O   
6682  C CB  . THR A 924  ? 0.3691 0.2778 0.4843 0.0772  -0.0334 -0.1022 922  THR A CB  
6683  O OG1 . THR A 924  ? 0.3730 0.2933 0.4714 0.0778  -0.0274 -0.1039 922  THR A OG1 
6684  C CG2 . THR A 924  ? 0.4319 0.3414 0.5609 0.0838  -0.0385 -0.1165 922  THR A CG2 
6685  N N   . PHE A 925  ? 0.3331 0.2315 0.4443 0.0660  -0.0288 -0.0697 923  PHE A N   
6686  C CA  . PHE A 925  ? 0.3670 0.2646 0.4679 0.0601  -0.0250 -0.0570 923  PHE A CA  
6687  C C   . PHE A 925  ? 0.3518 0.2390 0.4588 0.0546  -0.0288 -0.0485 923  PHE A C   
6688  O O   . PHE A 925  ? 0.4031 0.2827 0.5251 0.0549  -0.0345 -0.0485 923  PHE A O   
6689  C CB  . PHE A 925  ? 0.3898 0.2906 0.4895 0.0603  -0.0222 -0.0515 923  PHE A CB  
6690  C CG  . PHE A 925  ? 0.3722 0.2848 0.4631 0.0642  -0.0172 -0.0570 923  PHE A CG  
6691  C CD1 . PHE A 925  ? 0.3639 0.2816 0.4619 0.0705  -0.0184 -0.0674 923  PHE A CD1 
6692  C CD2 . PHE A 925  ? 0.3496 0.2685 0.4256 0.0616  -0.0113 -0.0514 923  PHE A CD2 
6693  C CE1 . PHE A 925  ? 0.3943 0.3243 0.4843 0.0739  -0.0136 -0.0719 923  PHE A CE1 
6694  C CE2 . PHE A 925  ? 0.3568 0.2869 0.4254 0.0647  -0.0068 -0.0554 923  PHE A CE2 
6695  C CZ  . PHE A 925  ? 0.3381 0.2742 0.4135 0.0708  -0.0078 -0.0655 923  PHE A CZ  
6696  N N   . VAL A 926  ? 0.3535 0.2410 0.4495 0.0496  -0.0258 -0.0409 924  VAL A N   
6697  C CA  . VAL A 926  ? 0.3835 0.2638 0.4830 0.0438  -0.0281 -0.0309 924  VAL A CA  
6698  C C   . VAL A 926  ? 0.3515 0.2348 0.4417 0.0402  -0.0238 -0.0207 924  VAL A C   
6699  O O   . VAL A 926  ? 0.3579 0.2476 0.4348 0.0399  -0.0187 -0.0204 924  VAL A O   
6700  C CB  . VAL A 926  ? 0.3428 0.2211 0.4386 0.0410  -0.0289 -0.0314 924  VAL A CB  
6701  C CG1 . VAL A 926  ? 0.3727 0.2458 0.4706 0.0347  -0.0304 -0.0202 924  VAL A CG1 
6702  C CG2 . VAL A 926  ? 0.3625 0.2370 0.4693 0.0443  -0.0340 -0.0415 924  VAL A CG2 
6703  N N   . PRO A 927  ? 0.3769 0.2562 0.4741 0.0374  -0.0259 -0.0122 925  PRO A N   
6704  C CA  . PRO A 927  ? 0.3842 0.2671 0.4727 0.0340  -0.0220 -0.0029 925  PRO A CA  
6705  C C   . PRO A 927  ? 0.3615 0.2452 0.4404 0.0290  -0.0199 0.0027  925  PRO A C   
6706  O O   . PRO A 927  ? 0.3250 0.2041 0.4083 0.0265  -0.0229 0.0039  925  PRO A O   
6707  C CB  . PRO A 927  ? 0.4029 0.2812 0.5034 0.0323  -0.0260 0.0042  925  PRO A CB  
6708  C CG  . PRO A 927  ? 0.4150 0.2858 0.5292 0.0325  -0.0321 0.0019  925  PRO A CG  
6709  C CD  . PRO A 927  ? 0.3592 0.2309 0.4732 0.0372  -0.0323 -0.0104 925  PRO A CD  
6710  N N   . PRO A 928  ? 0.3431 0.2325 0.4092 0.0277  -0.0148 0.0056  926  PRO A N   
6711  C CA  . PRO A 928  ? 0.3553 0.2457 0.4131 0.0230  -0.0129 0.0114  926  PRO A CA  
6712  C C   . PRO A 928  ? 0.3415 0.2281 0.4066 0.0185  -0.0162 0.0201  926  PRO A C   
6713  O O   . PRO A 928  ? 0.3230 0.2087 0.3948 0.0180  -0.0179 0.0250  926  PRO A O   
6714  C CB  . PRO A 928  ? 0.3426 0.2392 0.3892 0.0227  -0.0078 0.0141  926  PRO A CB  
6715  C CG  . PRO A 928  ? 0.3839 0.2838 0.4293 0.0278  -0.0062 0.0064  926  PRO A CG  
6716  C CD  . PRO A 928  ? 0.3716 0.2672 0.4306 0.0307  -0.0106 0.0029  926  PRO A CD  
6717  N N   . THR A 929  ? 0.3571 0.2424 0.4213 0.0153  -0.0172 0.0222  927  THR A N   
6718  C CA  . THR A 929  ? 0.3706 0.2524 0.4437 0.0111  -0.0211 0.0294  927  THR A CA  
6719  C C   . THR A 929  ? 0.3183 0.2037 0.3831 0.0065  -0.0190 0.0348  927  THR A C   
6720  O O   . THR A 929  ? 0.3460 0.2333 0.4024 0.0070  -0.0165 0.0305  927  THR A O   
6721  C CB  . THR A 929  ? 0.3556 0.2309 0.4404 0.0123  -0.0262 0.0247  927  THR A CB  
6722  O OG1 . THR A 929  ? 0.3853 0.2576 0.4789 0.0169  -0.0285 0.0191  927  THR A OG1 
6723  C CG2 . THR A 929  ? 0.3797 0.2516 0.4745 0.0073  -0.0305 0.0330  927  THR A CG2 
6724  N N   . ILE A 930  ? 0.3480 0.2351 0.4156 0.0021  -0.0200 0.0442  928  ILE A N   
6725  C CA  . ILE A 930  ? 0.3031 0.1946 0.3647 -0.0024 -0.0185 0.0495  928  ILE A CA  
6726  C C   . ILE A 930  ? 0.3347 0.2237 0.4074 -0.0063 -0.0231 0.0556  928  ILE A C   
6727  O O   . ILE A 930  ? 0.3750 0.2619 0.4574 -0.0074 -0.0264 0.0611  928  ILE A O   
6728  C CB  . ILE A 930  ? 0.3422 0.2406 0.3957 -0.0043 -0.0152 0.0554  928  ILE A CB  
6729  C CG1 . ILE A 930  ? 0.3463 0.2469 0.3900 -0.0007 -0.0109 0.0497  928  ILE A CG1 
6730  C CG2 . ILE A 930  ? 0.3311 0.2352 0.3789 -0.0087 -0.0138 0.0600  928  ILE A CG2 
6731  C CD1 . ILE A 930  ? 0.3214 0.2281 0.3589 -0.0020 -0.0081 0.0546  928  ILE A CD1 
6732  N N   . ILE A 931  ? 0.3203 0.2094 0.3920 -0.0083 -0.0236 0.0546  929  ILE A N   
6733  C CA  . ILE A 931  ? 0.3355 0.2226 0.4178 -0.0124 -0.0279 0.0603  929  ILE A CA  
6734  C C   . ILE A 931  ? 0.3518 0.2465 0.4272 -0.0170 -0.0256 0.0661  929  ILE A C   
6735  O O   . ILE A 931  ? 0.3555 0.2532 0.4213 -0.0164 -0.0224 0.0615  929  ILE A O   
6736  C CB  . ILE A 931  ? 0.3542 0.2345 0.4439 -0.0106 -0.0313 0.0531  929  ILE A CB  
6737  C CG1 . ILE A 931  ? 0.3801 0.2538 0.4771 -0.0056 -0.0336 0.0466  929  ILE A CG1 
6738  C CG2 . ILE A 931  ? 0.3653 0.2440 0.4662 -0.0156 -0.0357 0.0597  929  ILE A CG2 
6739  C CD1 . ILE A 931  ? 0.3675 0.2346 0.4735 -0.0035 -0.0376 0.0387  929  ILE A CD1 
6740  N N   . GLU A 932  ? 0.3567 0.2554 0.4373 -0.0216 -0.0273 0.0761  930  GLU A N   
6741  C CA  . GLU A 932  ? 0.3535 0.2613 0.4283 -0.0261 -0.0252 0.0819  930  GLU A CA  
6742  C C   . GLU A 932  ? 0.3537 0.2603 0.4366 -0.0296 -0.0285 0.0843  930  GLU A C   
6743  O O   . GLU A 932  ? 0.3683 0.2710 0.4641 -0.0319 -0.0332 0.0897  930  GLU A O   
6744  C CB  . GLU A 932  ? 0.3811 0.2961 0.4556 -0.0292 -0.0248 0.0916  930  GLU A CB  
6745  C CG  . GLU A 932  ? 0.3549 0.2725 0.4201 -0.0260 -0.0211 0.0889  930  GLU A CG  
6746  C CD  . GLU A 932  ? 0.4227 0.3465 0.4894 -0.0284 -0.0215 0.0979  930  GLU A CD  
6747  O OE1 . GLU A 932  ? 0.4488 0.3813 0.5150 -0.0330 -0.0215 0.1054  930  GLU A OE1 
6748  O OE2 . GLU A 932  ? 0.4211 0.3419 0.4895 -0.0258 -0.0219 0.0974  930  GLU A OE2 
6749  N N   . LEU A 933  ? 0.3839 0.2936 0.4601 -0.0300 -0.0263 0.0804  931  LEU A N   
6750  C CA  . LEU A 933  ? 0.3773 0.2865 0.4603 -0.0332 -0.0291 0.0817  931  LEU A CA  
6751  C C   . LEU A 933  ? 0.4553 0.3757 0.5353 -0.0385 -0.0275 0.0896  931  LEU A C   
6752  O O   . LEU A 933  ? 0.4274 0.3561 0.4975 -0.0387 -0.0236 0.0912  931  LEU A O   
6753  C CB  . LEU A 933  ? 0.3908 0.2961 0.4693 -0.0300 -0.0281 0.0713  931  LEU A CB  
6754  C CG  . LEU A 933  ? 0.4048 0.3003 0.4866 -0.0248 -0.0298 0.0624  931  LEU A CG  
6755  C CD1 . LEU A 933  ? 0.4347 0.3288 0.5103 -0.0219 -0.0285 0.0530  931  LEU A CD1 
6756  C CD2 . LEU A 933  ? 0.4485 0.3367 0.5464 -0.0259 -0.0357 0.0647  931  LEU A CD2 
6757  N N   . GLU A 934  ? 0.4151 0.3364 0.5043 -0.0427 -0.0307 0.0943  932  GLU A N   
6758  C CA  . GLU A 934  ? 0.5074 0.4407 0.5941 -0.0477 -0.0292 0.1013  932  GLU A CA  
6759  C C   . GLU A 934  ? 0.5173 0.4544 0.5942 -0.0464 -0.0258 0.0941  932  GLU A C   
6760  O O   . GLU A 934  ? 0.5176 0.4642 0.5843 -0.0466 -0.0218 0.0942  932  GLU A O   
6761  C CB  . GLU A 934  ? 0.5841 0.5177 0.6849 -0.0533 -0.0340 0.1101  932  GLU A CB  
6762  C CG  . GLU A 934  ? 0.6361 0.5830 0.7373 -0.0590 -0.0333 0.1219  932  GLU A CG  
6763  C CD  . GLU A 934  ? 0.7339 0.6830 0.8353 -0.0591 -0.0334 0.1285  932  GLU A CD  
6764  O OE1 . GLU A 934  ? 0.7690 0.7079 0.8729 -0.0552 -0.0349 0.1248  932  GLU A OE1 
6765  O OE2 . GLU A 934  ? 0.7940 0.7558 0.8930 -0.0630 -0.0321 0.1373  932  GLU A OE2 
6766  N N   . LYS A 935  ? 0.5115 0.4415 0.5920 -0.0449 -0.0277 0.0875  933  LYS A N   
6767  C CA  . LYS A 935  ? 0.5293 0.4621 0.6018 -0.0434 -0.0252 0.0806  933  LYS A CA  
6768  C C   . LYS A 935  ? 0.4764 0.3995 0.5456 -0.0377 -0.0251 0.0697  933  LYS A C   
6769  O O   . LYS A 935  ? 0.5261 0.4400 0.6028 -0.0358 -0.0282 0.0673  933  LYS A O   
6770  C CB  . LYS A 935  ? 0.4822 0.4181 0.5623 -0.0478 -0.0277 0.0836  933  LYS A CB  
6771  N N   . LEU A 936  ? 0.4487 0.3745 0.5071 -0.0350 -0.0217 0.0630  934  LEU A N   
6772  C CA  . LEU A 936  ? 0.5474 0.4657 0.6021 -0.0299 -0.0216 0.0530  934  LEU A CA  
6773  C C   . LEU A 936  ? 0.5384 0.4494 0.6037 -0.0299 -0.0262 0.0497  934  LEU A C   
6774  O O   . LEU A 936  ? 0.5528 0.4562 0.6195 -0.0259 -0.0275 0.0429  934  LEU A O   
6775  C CB  . LEU A 936  ? 0.5461 0.4693 0.5893 -0.0279 -0.0180 0.0479  934  LEU A CB  
6776  C CG  . LEU A 936  ? 0.6116 0.5294 0.6485 -0.0227 -0.0171 0.0383  934  LEU A CG  
6777  C CD1 . LEU A 936  ? 0.5256 0.4371 0.5624 -0.0191 -0.0171 0.0355  934  LEU A CD1 
6778  C CD2 . LEU A 936  ? 0.5284 0.4519 0.5534 -0.0211 -0.0131 0.0356  934  LEU A CD2 
6779  N N   . SER A 937  ? 0.5625 0.4761 0.6359 -0.0345 -0.0288 0.0543  935  SER A N   
6780  C CA  . SER A 937  ? 0.5349 0.4416 0.6195 -0.0350 -0.0336 0.0511  935  SER A CA  
6781  C C   . SER A 937  ? 0.5730 0.4714 0.6700 -0.0349 -0.0380 0.0530  935  SER A C   
6782  O O   . SER A 937  ? 0.5863 0.4776 0.6931 -0.0343 -0.0424 0.0486  935  SER A O   
6783  C CB  . SER A 937  ? 0.5612 0.4737 0.6518 -0.0404 -0.0352 0.0563  935  SER A CB  
6784  O OG  . SER A 937  ? 0.5247 0.4423 0.6217 -0.0456 -0.0361 0.0675  935  SER A OG  
6785  N N   . ASP A 938  ? 0.5550 0.4540 0.6524 -0.0354 -0.0373 0.0590  936  ASP A N   
6786  C CA  . ASP A 938  ? 0.5550 0.4455 0.6636 -0.0344 -0.0414 0.0598  936  ASP A CA  
6787  C C   . ASP A 938  ? 0.5551 0.4379 0.6619 -0.0279 -0.0418 0.0484  936  ASP A C   
6788  O O   . ASP A 938  ? 0.5777 0.4527 0.6957 -0.0264 -0.0461 0.0463  936  ASP A O   
6789  C CB  . ASP A 938  ? 0.5809 0.4745 0.6884 -0.0356 -0.0400 0.0680  936  ASP A CB  
6790  C CG  . ASP A 938  ? 0.6215 0.5231 0.7333 -0.0422 -0.0406 0.0803  936  ASP A CG  
6791  O OD1 . ASP A 938  ? 0.6250 0.5273 0.7453 -0.0462 -0.0436 0.0835  936  ASP A OD1 
6792  O OD2 . ASP A 938  ? 0.5871 0.4949 0.6940 -0.0434 -0.0381 0.0868  936  ASP A OD2 
6793  N N   . LEU A 939  ? 0.5636 0.4491 0.6571 -0.0241 -0.0375 0.0412  937  LEU A N   
6794  C CA  A LEU A 939  ? 0.5752 0.4556 0.6653 -0.0180 -0.0372 0.0307  937  LEU A CA  
6795  C CA  B LEU A 939  ? 0.5750 0.4555 0.6651 -0.0180 -0.0372 0.0307  937  LEU A CA  
6796  C C   . LEU A 939  ? 0.5752 0.4537 0.6670 -0.0169 -0.0392 0.0228  937  LEU A C   
6797  O O   . LEU A 939  ? 0.5849 0.4684 0.6674 -0.0169 -0.0364 0.0207  937  LEU A O   
6798  C CB  A LEU A 939  ? 0.5259 0.4108 0.6009 -0.0148 -0.0315 0.0284  937  LEU A CB  
6799  C CB  B LEU A 939  ? 0.5261 0.4111 0.6011 -0.0148 -0.0315 0.0283  937  LEU A CB  
6800  C CG  A LEU A 939  ? 0.5353 0.4170 0.6059 -0.0087 -0.0306 0.0187  937  LEU A CG  
6801  C CG  B LEU A 939  ? 0.5255 0.4072 0.5991 -0.0103 -0.0307 0.0247  937  LEU A CG  
6802  C CD1 A LEU A 939  ? 0.5170 0.3923 0.5989 -0.0068 -0.0343 0.0175  937  LEU A CD1 
6803  C CD1 B LEU A 939  ? 0.5011 0.3871 0.5599 -0.0069 -0.0255 0.0205  937  LEU A CD1 
6804  C CD2 A LEU A 939  ? 0.5053 0.3918 0.5621 -0.0066 -0.0252 0.0186  937  LEU A CD2 
6805  C CD2 B LEU A 939  ? 0.5169 0.3915 0.6003 -0.0069 -0.0349 0.0170  937  LEU A CD2 
6806  N N   . GLN A 940  ? 0.5910 0.4625 0.6951 -0.0156 -0.0444 0.0181  938  GLN A N   
6807  C CA  . GLN A 940  ? 0.6411 0.5106 0.7496 -0.0153 -0.0474 0.0113  938  GLN A CA  
6808  C C   . GLN A 940  ? 0.6818 0.5482 0.7885 -0.0090 -0.0482 -0.0012 938  GLN A C   
6809  O O   . GLN A 940  ? 0.6704 0.5335 0.7846 -0.0082 -0.0522 -0.0078 938  GLN A O   
6810  C CB  . GLN A 940  ? 0.6040 0.4688 0.7299 -0.0197 -0.0535 0.0159  938  GLN A CB  
6811  N N   . ARG A 941  ? 0.6424 0.5104 0.7395 -0.0046 -0.0445 -0.0047 939  ARG A N   
6812  C CA  . ARG A 941  ? 0.6312 0.4982 0.7253 0.0015  -0.0446 -0.0163 939  ARG A CA  
6813  C C   . ARG A 941  ? 0.6023 0.4735 0.6832 0.0049  -0.0392 -0.0168 939  ARG A C   
6814  O O   . ARG A 941  ? 0.5794 0.4515 0.6583 0.0032  -0.0369 -0.0093 939  ARG A O   
6815  C CB  . ARG A 941  ? 0.6374 0.4973 0.7465 0.0037  -0.0502 -0.0215 939  ARG A CB  
6816  C CG  . ARG A 941  ? 0.6516 0.5080 0.7679 0.0030  -0.0511 -0.0150 939  ARG A CG  
6817  C CD  . ARG A 941  ? 0.6976 0.5477 0.8268 0.0070  -0.0560 -0.0225 939  ARG A CD  
6818  N NE  . ARG A 941  ? 0.6968 0.5495 0.8187 0.0128  -0.0529 -0.0289 939  ARG A NE  
6819  C CZ  . ARG A 941  ? 0.7082 0.5647 0.8227 0.0178  -0.0513 -0.0396 939  ARG A CZ  
6820  N NH1 . ARG A 941  ? 0.7372 0.5952 0.8499 0.0180  -0.0525 -0.0456 939  ARG A NH1 
6821  N NH2 . ARG A 941  ? 0.6700 0.5298 0.7786 0.0225  -0.0484 -0.0441 939  ARG A NH2 
6822  N N   . GLU A 942  ? 0.6012 0.4755 0.6736 0.0095  -0.0373 -0.0256 940  GLU A N   
6823  C CA  . GLU A 942  ? 0.6001 0.4786 0.6613 0.0128  -0.0325 -0.0265 940  GLU A CA  
6824  C C   . GLU A 942  ? 0.5710 0.4463 0.6394 0.0160  -0.0340 -0.0293 940  GLU A C   
6825  O O   . GLU A 942  ? 0.5775 0.4494 0.6555 0.0187  -0.0382 -0.0368 940  GLU A O   
6826  C CB  . GLU A 942  ? 0.5955 0.4793 0.6458 0.0165  -0.0302 -0.0343 940  GLU A CB  
6827  N N   . VAL A 943  ? 0.5273 0.4038 0.5917 0.0158  -0.0309 -0.0236 941  VAL A N   
6828  C CA  . VAL A 943  ? 0.5144 0.3886 0.5852 0.0187  -0.0320 -0.0253 941  VAL A CA  
6829  C C   . VAL A 943  ? 0.4609 0.3411 0.5198 0.0225  -0.0270 -0.0282 941  VAL A C   
6830  O O   . VAL A 943  ? 0.4584 0.3416 0.5088 0.0208  -0.0230 -0.0216 941  VAL A O   
6831  C CB  . VAL A 943  ? 0.5155 0.3862 0.5937 0.0149  -0.0331 -0.0153 941  VAL A CB  
6832  C CG1 . VAL A 943  ? 0.4332 0.3012 0.5191 0.0182  -0.0347 -0.0175 941  VAL A CG1 
6833  C CG2 . VAL A 943  ? 0.5668 0.4327 0.6563 0.0103  -0.0378 -0.0108 941  VAL A CG2 
6834  N N   . PHE A 944  ? 0.4301 0.3124 0.4888 0.0276  -0.0275 -0.0381 942  PHE A N   
6835  C CA  . PHE A 944  ? 0.4169 0.3066 0.4633 0.0310  -0.0227 -0.0414 942  PHE A CA  
6836  C C   . PHE A 944  ? 0.4070 0.2977 0.4554 0.0335  -0.0214 -0.0409 942  PHE A C   
6837  O O   . PHE A 944  ? 0.4219 0.3154 0.4725 0.0382  -0.0218 -0.0488 942  PHE A O   
6838  C CB  . PHE A 944  ? 0.4420 0.3359 0.4860 0.0353  -0.0236 -0.0522 942  PHE A CB  
6839  C CG  . PHE A 944  ? 0.4553 0.3575 0.4845 0.0366  -0.0188 -0.0530 942  PHE A CG  
6840  C CD1 . PHE A 944  ? 0.4435 0.3468 0.4642 0.0334  -0.0169 -0.0480 942  PHE A CD1 
6841  C CD2 . PHE A 944  ? 0.4662 0.3754 0.4904 0.0412  -0.0164 -0.0585 942  PHE A CD2 
6842  C CE1 . PHE A 944  ? 0.4577 0.3682 0.4656 0.0346  -0.0129 -0.0482 942  PHE A CE1 
6843  C CE2 . PHE A 944  ? 0.4248 0.3418 0.4357 0.0421  -0.0122 -0.0583 942  PHE A CE2 
6844  C CZ  . PHE A 944  ? 0.4511 0.3683 0.4542 0.0388  -0.0106 -0.0530 942  PHE A CZ  
6845  N N   . GLY A 945  ? 0.3768 0.2658 0.4245 0.0301  -0.0197 -0.0315 943  GLY A N   
6846  C CA  . GLY A 945  ? 0.3642 0.2537 0.4146 0.0317  -0.0187 -0.0297 943  GLY A CA  
6847  C C   . GLY A 945  ? 0.3599 0.2501 0.4046 0.0279  -0.0156 -0.0194 943  GLY A C   
6848  O O   . GLY A 945  ? 0.3605 0.2517 0.3982 0.0244  -0.0137 -0.0143 943  GLY A O   
6849  N N   . PRO A 946  ? 0.3350 0.2252 0.3832 0.0288  -0.0151 -0.0167 944  PRO A N   
6850  C CA  . PRO A 946  ? 0.3528 0.2447 0.3952 0.0256  -0.0120 -0.0077 944  PRO A CA  
6851  C C   . PRO A 946  ? 0.3374 0.2249 0.3867 0.0208  -0.0147 0.0007  944  PRO A C   
6852  O O   . PRO A 946  ? 0.3375 0.2234 0.3929 0.0199  -0.0158 0.0057  944  PRO A O   
6853  C CB  . PRO A 946  ? 0.3353 0.2297 0.3794 0.0289  -0.0107 -0.0092 944  PRO A CB  
6854  C CG  . PRO A 946  ? 0.3396 0.2304 0.3959 0.0324  -0.0150 -0.0160 944  PRO A CG  
6855  C CD  . PRO A 946  ? 0.3455 0.2349 0.4025 0.0331  -0.0172 -0.0225 944  PRO A CD  
6856  N N   . VAL A 947  ? 0.3295 0.2155 0.3782 0.0177  -0.0158 0.0024  945  VAL A N   
6857  C CA  . VAL A 947  ? 0.3490 0.2316 0.4055 0.0132  -0.0189 0.0099  945  VAL A CA  
6858  C C   . VAL A 947  ? 0.3433 0.2295 0.3909 0.0092  -0.0163 0.0150  945  VAL A C   
6859  O O   . VAL A 947  ? 0.3696 0.2566 0.4131 0.0090  -0.0160 0.0115  945  VAL A O   
6860  C CB  . VAL A 947  ? 0.3822 0.2589 0.4510 0.0133  -0.0243 0.0064  945  VAL A CB  
6861  C CG1 . VAL A 947  ? 0.3317 0.2058 0.4085 0.0080  -0.0274 0.0154  945  VAL A CG1 
6862  C CG2 . VAL A 947  ? 0.3533 0.2266 0.4318 0.0178  -0.0272 0.0001  945  VAL A CG2 
6863  N N   . LEU A 948  ? 0.3352 0.2242 0.3801 0.0062  -0.0146 0.0229  946  LEU A N   
6864  C CA  . LEU A 948  ? 0.3025 0.1962 0.3392 0.0027  -0.0120 0.0276  946  LEU A CA  
6865  C C   . LEU A 948  ? 0.3515 0.2448 0.3955 -0.0021 -0.0149 0.0348  946  LEU A C   
6866  O O   . LEU A 948  ? 0.3607 0.2524 0.4129 -0.0036 -0.0173 0.0402  946  LEU A O   
6867  C CB  . LEU A 948  ? 0.3301 0.2285 0.3588 0.0025  -0.0082 0.0311  946  LEU A CB  
6868  C CG  . LEU A 948  ? 0.3384 0.2419 0.3596 -0.0009 -0.0059 0.0355  946  LEU A CG  
6869  C CD1 . LEU A 948  ? 0.2996 0.2039 0.3138 0.0001  -0.0045 0.0302  946  LEU A CD1 
6870  C CD2 . LEU A 948  ? 0.3857 0.2936 0.4007 -0.0011 -0.0028 0.0387  946  LEU A CD2 
6871  N N   . HIS A 949  ? 0.3235 0.2188 0.3649 -0.0046 -0.0148 0.0354  947  HIS A N   
6872  C CA  . HIS A 949  ? 0.3374 0.2342 0.3849 -0.0095 -0.0170 0.0428  947  HIS A CA  
6873  C C   . HIS A 949  ? 0.3286 0.2332 0.3672 -0.0123 -0.0136 0.0477  947  HIS A C   
6874  O O   . HIS A 949  ? 0.3516 0.2591 0.3802 -0.0107 -0.0102 0.0439  947  HIS A O   
6875  C CB  . HIS A 949  ? 0.3329 0.2269 0.3857 -0.0105 -0.0199 0.0399  947  HIS A CB  
6876  C CG  . HIS A 949  ? 0.3963 0.2829 0.4579 -0.0074 -0.0235 0.0336  947  HIS A CG  
6877  N ND1 . HIS A 949  ? 0.4167 0.3016 0.4738 -0.0027 -0.0225 0.0242  947  HIS A ND1 
6878  C CD2 . HIS A 949  ? 0.3782 0.2593 0.4536 -0.0083 -0.0284 0.0352  947  HIS A CD2 
6879  C CE1 . HIS A 949  ? 0.4011 0.2802 0.4685 -0.0005 -0.0265 0.0195  947  HIS A CE1 
6880  N NE2 . HIS A 949  ? 0.4205 0.2966 0.4995 -0.0038 -0.0303 0.0259  947  HIS A NE2 
6881  N N   . VAL A 950  ? 0.3579 0.2664 0.4005 -0.0163 -0.0145 0.0562  948  VAL A N   
6882  C CA  . VAL A 950  ? 0.3469 0.2640 0.3818 -0.0188 -0.0115 0.0608  948  VAL A CA  
6883  C C   . VAL A 950  ? 0.3367 0.2589 0.3758 -0.0236 -0.0130 0.0669  948  VAL A C   
6884  O O   . VAL A 950  ? 0.3586 0.2790 0.4080 -0.0264 -0.0166 0.0724  948  VAL A O   
6885  C CB  . VAL A 950  ? 0.3857 0.3056 0.4199 -0.0189 -0.0105 0.0656  948  VAL A CB  
6886  C CG1 . VAL A 950  ? 0.3830 0.3128 0.4098 -0.0215 -0.0078 0.0697  948  VAL A CG1 
6887  C CG2 . VAL A 950  ? 0.3266 0.2425 0.3567 -0.0142 -0.0088 0.0597  948  VAL A CG2 
6888  N N   . ILE A 951  ? 0.3328 0.2616 0.3645 -0.0248 -0.0105 0.0660  949  ILE A N   
6889  C CA  . ILE A 951  ? 0.3990 0.3354 0.4333 -0.0295 -0.0112 0.0721  949  ILE A CA  
6890  C C   . ILE A 951  ? 0.3766 0.3233 0.4018 -0.0304 -0.0076 0.0736  949  ILE A C   
6891  O O   . ILE A 951  ? 0.3319 0.2784 0.3486 -0.0272 -0.0048 0.0684  949  ILE A O   
6892  C CB  . ILE A 951  ? 0.3839 0.3188 0.4203 -0.0303 -0.0124 0.0687  949  ILE A CB  
6893  C CG1 . ILE A 951  ? 0.3724 0.3080 0.3986 -0.0270 -0.0093 0.0608  949  ILE A CG1 
6894  C CG2 . ILE A 951  ? 0.4385 0.3634 0.4849 -0.0293 -0.0165 0.0665  949  ILE A CG2 
6895  C CD1 . ILE A 951  ? 0.4525 0.3866 0.4804 -0.0272 -0.0105 0.0569  949  ILE A CD1 
6896  N N   . ARG A 952  ? 0.3519 0.3081 0.3794 -0.0348 -0.0080 0.0807  950  ARG A N   
6897  C CA  . ARG A 952  ? 0.3704 0.3383 0.3906 -0.0361 -0.0050 0.0824  950  ARG A CA  
6898  C C   . ARG A 952  ? 0.3771 0.3527 0.3959 -0.0383 -0.0043 0.0820  950  ARG A C   
6899  O O   . ARG A 952  ? 0.3452 0.3196 0.3710 -0.0408 -0.0067 0.0843  950  ARG A O   
6900  C CB  . ARG A 952  ? 0.4064 0.3817 0.4300 -0.0394 -0.0059 0.0915  950  ARG A CB  
6901  C CG  . ARG A 952  ? 0.4024 0.3697 0.4302 -0.0378 -0.0076 0.0932  950  ARG A CG  
6902  C CD  . ARG A 952  ? 0.4929 0.4649 0.5286 -0.0419 -0.0102 0.1037  950  ARG A CD  
6903  N NE  . ARG A 952  ? 0.4586 0.4433 0.4890 -0.0437 -0.0082 0.1081  950  ARG A NE  
6904  C CZ  . ARG A 952  ? 0.4928 0.4782 0.5214 -0.0425 -0.0079 0.1097  950  ARG A CZ  
6905  N NH1 . ARG A 952  ? 0.4435 0.4180 0.4755 -0.0395 -0.0092 0.1077  950  ARG A NH1 
6906  N NH2 . ARG A 952  ? 0.3957 0.3938 0.4192 -0.0441 -0.0061 0.1131  950  ARG A NH2 
6907  N N   . TYR A 953  ? 0.3302 0.3139 0.3408 -0.0374 -0.0013 0.0787  951  TYR A N   
6908  C CA  . TYR A 953  ? 0.3403 0.3322 0.3496 -0.0390 -0.0005 0.0775  951  TYR A CA  
6909  C C   . TYR A 953  ? 0.3607 0.3667 0.3643 -0.0400 0.0020  0.0785  951  TYR A C   
6910  O O   . TYR A 953  ? 0.3607 0.3674 0.3587 -0.0378 0.0036  0.0762  951  TYR A O   
6911  C CB  . TYR A 953  ? 0.3351 0.3202 0.3404 -0.0354 0.0002  0.0687  951  TYR A CB  
6912  C CG  . TYR A 953  ? 0.3454 0.3297 0.3418 -0.0313 0.0029  0.0621  951  TYR A CG  
6913  C CD1 . TYR A 953  ? 0.2950 0.2701 0.2890 -0.0281 0.0032  0.0594  951  TYR A CD1 
6914  C CD2 . TYR A 953  ? 0.3568 0.3497 0.3478 -0.0308 0.0049  0.0587  951  TYR A CD2 
6915  C CE1 . TYR A 953  ? 0.2945 0.2689 0.2813 -0.0248 0.0054  0.0542  951  TYR A CE1 
6916  C CE2 . TYR A 953  ? 0.3498 0.3413 0.3339 -0.0272 0.0068  0.0530  951  TYR A CE2 
6917  C CZ  . TYR A 953  ? 0.3170 0.2990 0.2991 -0.0244 0.0070  0.0511  951  TYR A CZ  
6918  O OH  . TYR A 953  ? 0.3039 0.2845 0.2801 -0.0212 0.0086  0.0461  951  TYR A OH  
6919  N N   . ARG A 954  ? 0.3787 0.3964 0.3839 -0.0434 0.0021  0.0817  952  ARG A N   
6920  C CA  . ARG A 954  ? 0.4032 0.4358 0.4030 -0.0439 0.0045  0.0810  952  ARG A CA  
6921  C C   . ARG A 954  ? 0.3879 0.4197 0.3814 -0.0400 0.0064  0.0714  952  ARG A C   
6922  O O   . ARG A 954  ? 0.3307 0.3555 0.3253 -0.0387 0.0058  0.0674  952  ARG A O   
6923  C CB  . ARG A 954  ? 0.4290 0.4758 0.4333 -0.0489 0.0041  0.0878  952  ARG A CB  
6924  C CG  . ARG A 954  ? 0.4889 0.5362 0.5014 -0.0535 0.0015  0.0985  952  ARG A CG  
6925  C CD  . ARG A 954  ? 0.5366 0.5861 0.5473 -0.0534 0.0017  0.1025  952  ARG A CD  
6926  N NE  . ARG A 954  ? 0.5789 0.6433 0.5824 -0.0530 0.0044  0.1006  952  ARG A NE  
6927  C CZ  . ARG A 954  ? 0.6637 0.7459 0.6677 -0.0568 0.0050  0.1062  952  ARG A CZ  
6928  N NH1 . ARG A 954  ? 0.6616 0.7490 0.6731 -0.0618 0.0031  0.1155  952  ARG A NH1 
6929  N NH2 . ARG A 954  ? 0.6788 0.7745 0.6761 -0.0556 0.0074  0.1025  952  ARG A NH2 
6930  N N   . ARG A 955  ? 0.3600 0.3990 0.3474 -0.0381 0.0085  0.0676  953  ARG A N   
6931  C CA  . ARG A 955  ? 0.3707 0.4073 0.3529 -0.0340 0.0098  0.0585  953  ARG A CA  
6932  C C   . ARG A 955  ? 0.3604 0.4019 0.3439 -0.0346 0.0097  0.0561  953  ARG A C   
6933  O O   . ARG A 955  ? 0.4158 0.4490 0.3980 -0.0318 0.0095  0.0503  953  ARG A O   
6934  C CB  . ARG A 955  ? 0.4083 0.4538 0.3852 -0.0323 0.0115  0.0549  953  ARG A CB  
6935  C CG  . ARG A 955  ? 0.5061 0.5487 0.4789 -0.0280 0.0124  0.0457  953  ARG A CG  
6936  C CD  . ARG A 955  ? 0.5307 0.5563 0.5029 -0.0252 0.0116  0.0426  953  ARG A CD  
6937  N NE  . ARG A 955  ? 0.5348 0.5568 0.5035 -0.0213 0.0120  0.0349  953  ARG A NE  
6938  C CZ  . ARG A 955  ? 0.5573 0.5812 0.5263 -0.0204 0.0118  0.0311  953  ARG A CZ  
6939  N NH1 . ARG A 955  ? 0.5123 0.5427 0.4848 -0.0231 0.0114  0.0339  953  ARG A NH1 
6940  N NH2 . ARG A 955  ? 0.5485 0.5682 0.5149 -0.0167 0.0118  0.0247  953  ARG A NH2 
6941  N N   . ASP A 956  ? 0.3806 0.4363 0.3669 -0.0384 0.0099  0.0606  954  ASP A N   
6942  C CA  . ASP A 956  ? 0.4058 0.4672 0.3939 -0.0390 0.0099  0.0583  954  ASP A CA  
6943  C C   . ASP A 956  ? 0.3789 0.4282 0.3715 -0.0395 0.0079  0.0588  954  ASP A C   
6944  O O   . ASP A 956  ? 0.4257 0.4758 0.4188 -0.0387 0.0078  0.0548  954  ASP A O   
6945  C CB  . ASP A 956  ? 0.3998 0.4796 0.3908 -0.0435 0.0104  0.0642  954  ASP A CB  
6946  C CG  . ASP A 956  ? 0.4496 0.5444 0.4357 -0.0425 0.0125  0.0612  954  ASP A CG  
6947  O OD1 . ASP A 956  ? 0.4256 0.5162 0.4068 -0.0380 0.0134  0.0535  954  ASP A OD1 
6948  O OD2 . ASP A 956  ? 0.5208 0.6321 0.5085 -0.0461 0.0132  0.0666  954  ASP A OD2 
6949  N N   . ASP A 957  ? 0.4046 0.4432 0.4009 -0.0406 0.0062  0.0633  955  ASP A N   
6950  C CA  . ASP A 957  ? 0.4078 0.4350 0.4092 -0.0409 0.0039  0.0633  955  ASP A CA  
6951  C C   . ASP A 957  ? 0.3725 0.3850 0.3701 -0.0360 0.0037  0.0562  955  ASP A C   
6952  O O   . ASP A 957  ? 0.3813 0.3835 0.3827 -0.0358 0.0017  0.0558  955  ASP A O   
6953  C CB  . ASP A 957  ? 0.4467 0.4702 0.4556 -0.0446 0.0016  0.0716  955  ASP A CB  
6954  C CG  . ASP A 957  ? 0.4637 0.5012 0.4779 -0.0501 0.0011  0.0800  955  ASP A CG  
6955  O OD1 . ASP A 957  ? 0.5114 0.5589 0.5261 -0.0516 0.0018  0.0792  955  ASP A OD1 
6956  O OD2 . ASP A 957  ? 0.4877 0.5266 0.5060 -0.0531 0.0000  0.0878  955  ASP A OD2 
6957  N N   . LEU A 958  ? 0.3482 0.3602 0.3388 -0.0323 0.0056  0.0507  956  LEU A N   
6958  C CA  . LEU A 958  ? 0.3405 0.3398 0.3275 -0.0280 0.0055  0.0449  956  LEU A CA  
6959  C C   . LEU A 958  ? 0.3752 0.3697 0.3634 -0.0268 0.0043  0.0408  956  LEU A C   
6960  O O   . LEU A 958  ? 0.3335 0.3172 0.3226 -0.0252 0.0030  0.0389  956  LEU A O   
6961  C CB  . LEU A 958  ? 0.3643 0.3651 0.3446 -0.0247 0.0075  0.0402  956  LEU A CB  
6962  C CG  . LEU A 958  ? 0.3735 0.3630 0.3496 -0.0204 0.0075  0.0345  956  LEU A CG  
6963  C CD1 . LEU A 958  ? 0.3541 0.3329 0.3315 -0.0198 0.0067  0.0363  956  LEU A CD1 
6964  C CD2 . LEU A 958  ? 0.3907 0.3828 0.3618 -0.0178 0.0091  0.0309  956  LEU A CD2 
6965  N N   . ASP A 959  ? 0.3385 0.3416 0.3266 -0.0274 0.0047  0.0388  957  ASP A N   
6966  C CA  . ASP A 959  ? 0.3486 0.3474 0.3375 -0.0260 0.0035  0.0346  957  ASP A CA  
6967  C C   . ASP A 959  ? 0.3582 0.3519 0.3540 -0.0287 0.0010  0.0378  957  ASP A C   
6968  O O   . ASP A 959  ? 0.3611 0.3463 0.3574 -0.0268 -0.0005 0.0341  957  ASP A O   
6969  C CB  . ASP A 959  ? 0.3671 0.3769 0.3556 -0.0263 0.0042  0.0321  957  ASP A CB  
6970  C CG  . ASP A 959  ? 0.3994 0.4045 0.3877 -0.0240 0.0030  0.0269  957  ASP A CG  
6971  O OD1 . ASP A 959  ? 0.3689 0.3654 0.3529 -0.0201 0.0029  0.0224  957  ASP A OD1 
6972  O OD2 . ASP A 959  ? 0.4458 0.4565 0.4386 -0.0263 0.0020  0.0277  957  ASP A OD2 
6973  N N   . ARG A 960  ? 0.3726 0.3719 0.3743 -0.0331 0.0003  0.0447  958  ARG A N   
6974  C CA  . ARG A 960  ? 0.3343 0.3280 0.3440 -0.0358 -0.0026 0.0481  958  ARG A CA  
6975  C C   . ARG A 960  ? 0.3906 0.3710 0.4008 -0.0336 -0.0038 0.0470  958  ARG A C   
6976  O O   . ARG A 960  ? 0.4010 0.3733 0.4156 -0.0331 -0.0063 0.0450  958  ARG A O   
6977  C CB  . ARG A 960  ? 0.4110 0.4141 0.4274 -0.0413 -0.0032 0.0569  958  ARG A CB  
6978  C CG  . ARG A 960  ? 0.4543 0.4527 0.4809 -0.0449 -0.0067 0.0612  958  ARG A CG  
6979  C CD  . ARG A 960  ? 0.5307 0.5399 0.5642 -0.0508 -0.0074 0.0709  958  ARG A CD  
6980  N NE  . ARG A 960  ? 0.6518 0.6601 0.6862 -0.0519 -0.0074 0.0769  958  ARG A NE  
6981  C CZ  . ARG A 960  ? 0.6372 0.6544 0.6771 -0.0569 -0.0081 0.0863  958  ARG A CZ  
6982  N NH1 . ARG A 960  ? 0.6445 0.6730 0.6894 -0.0614 -0.0086 0.0913  958  ARG A NH1 
6983  N NH2 . ARG A 960  ? 0.6641 0.6793 0.7046 -0.0573 -0.0084 0.0912  958  ARG A NH2 
6984  N N   . LEU A 961  ? 0.3508 0.3298 0.3570 -0.0321 -0.0023 0.0480  959  LEU A N   
6985  C CA  . LEU A 961  ? 0.3411 0.3086 0.3474 -0.0296 -0.0032 0.0466  959  LEU A CA  
6986  C C   . LEU A 961  ? 0.3924 0.3520 0.3946 -0.0253 -0.0033 0.0389  959  LEU A C   
6987  O O   . LEU A 961  ? 0.3539 0.3050 0.3596 -0.0241 -0.0054 0.0368  959  LEU A O   
6988  C CB  . LEU A 961  ? 0.3509 0.3194 0.3527 -0.0285 -0.0012 0.0483  959  LEU A CB  
6989  C CG  . LEU A 961  ? 0.3582 0.3159 0.3593 -0.0254 -0.0016 0.0460  959  LEU A CG  
6990  C CD1 . LEU A 961  ? 0.3852 0.3372 0.3954 -0.0273 -0.0047 0.0496  959  LEU A CD1 
6991  C CD2 . LEU A 961  ? 0.3972 0.3568 0.3933 -0.0243 0.0005  0.0473  959  LEU A CD2 
6992  N N   . VAL A 962  ? 0.3494 0.3120 0.3444 -0.0228 -0.0013 0.0346  960  VAL A N   
6993  C CA  . VAL A 962  ? 0.3454 0.3017 0.3364 -0.0189 -0.0015 0.0281  960  VAL A CA  
6994  C C   . VAL A 962  ? 0.4114 0.3655 0.4077 -0.0198 -0.0042 0.0263  960  VAL A C   
6995  O O   . VAL A 962  ? 0.4057 0.3523 0.4020 -0.0175 -0.0056 0.0223  960  VAL A O   
6996  C CB  . VAL A 962  ? 0.3824 0.3431 0.3664 -0.0166 0.0005  0.0246  960  VAL A CB  
6997  C CG1 . VAL A 962  ? 0.3778 0.3329 0.3579 -0.0129 -0.0001 0.0188  960  VAL A CG1 
6998  C CG2 . VAL A 962  ? 0.3157 0.2778 0.2953 -0.0156 0.0026  0.0259  960  VAL A CG2 
6999  N N   . ASP A 963  ? 0.3585 0.3198 0.3594 -0.0234 -0.0049 0.0291  961  ASP A N   
7000  C CA  . ASP A 963  ? 0.4264 0.3860 0.4340 -0.0250 -0.0078 0.0283  961  ASP A CA  
7001  C C   . ASP A 963  ? 0.4098 0.3609 0.4241 -0.0256 -0.0105 0.0293  961  ASP A C   
7002  O O   . ASP A 963  ? 0.4554 0.4006 0.4723 -0.0241 -0.0128 0.0248  961  ASP A O   
7003  C CB  . ASP A 963  ? 0.4292 0.3989 0.4420 -0.0296 -0.0081 0.0330  961  ASP A CB  
7004  C CG  . ASP A 963  ? 0.5074 0.4843 0.5165 -0.0287 -0.0069 0.0295  961  ASP A CG  
7005  O OD1 . ASP A 963  ? 0.5717 0.5445 0.5756 -0.0248 -0.0068 0.0235  961  ASP A OD1 
7006  O OD2 . ASP A 963  ? 0.5464 0.5340 0.5581 -0.0319 -0.0063 0.0331  961  ASP A OD2 
7007  N N   . ASP A 964  ? 0.4039 0.3546 0.4216 -0.0277 -0.0105 0.0349  962  ASP A N   
7008  C CA  . ASP A 964  ? 0.4636 0.4062 0.4889 -0.0281 -0.0133 0.0361  962  ASP A CA  
7009  C C   . ASP A 964  ? 0.4729 0.4070 0.4939 -0.0231 -0.0132 0.0297  962  ASP A C   
7010  O O   . ASP A 964  ? 0.4610 0.3881 0.4875 -0.0220 -0.0161 0.0265  962  ASP A O   
7011  C CB  . ASP A 964  ? 0.4644 0.4092 0.4937 -0.0311 -0.0132 0.0438  962  ASP A CB  
7012  C CG  . ASP A 964  ? 0.4983 0.4523 0.5333 -0.0365 -0.0139 0.0511  962  ASP A CG  
7013  O OD1 . ASP A 964  ? 0.5526 0.5096 0.5910 -0.0383 -0.0151 0.0503  962  ASP A OD1 
7014  O OD2 . ASP A 964  ? 0.5701 0.5289 0.6065 -0.0391 -0.0132 0.0580  962  ASP A OD2 
7015  N N   . VAL A 965  ? 0.3820 0.3168 0.3937 -0.0201 -0.0101 0.0277  963  VAL A N   
7016  C CA  . VAL A 965  ? 0.4170 0.3454 0.4240 -0.0155 -0.0096 0.0220  963  VAL A CA  
7017  C C   . VAL A 965  ? 0.4375 0.3639 0.4434 -0.0134 -0.0110 0.0155  963  VAL A C   
7018  O O   . VAL A 965  ? 0.4509 0.3717 0.4590 -0.0110 -0.0129 0.0111  963  VAL A O   
7019  C CB  . VAL A 965  ? 0.3799 0.3104 0.3775 -0.0132 -0.0061 0.0218  963  VAL A CB  
7020  C CG1 . VAL A 965  ? 0.3820 0.3070 0.3747 -0.0088 -0.0055 0.0164  963  VAL A CG1 
7021  C CG2 . VAL A 965  ? 0.3768 0.3097 0.3758 -0.0153 -0.0049 0.0278  963  VAL A CG2 
7022  N N   . ASN A 966  ? 0.3737 0.3053 0.3762 -0.0139 -0.0103 0.0147  964  ASN A N   
7023  C CA  . ASN A 966  ? 0.4281 0.3587 0.4295 -0.0119 -0.0118 0.0089  964  ASN A CA  
7024  C C   . ASN A 966  ? 0.4587 0.3862 0.4697 -0.0137 -0.0156 0.0077  964  ASN A C   
7025  O O   . ASN A 966  ? 0.4305 0.3547 0.4417 -0.0113 -0.0175 0.0018  964  ASN A O   
7026  C CB  . ASN A 966  ? 0.4104 0.3478 0.4080 -0.0125 -0.0106 0.0087  964  ASN A CB  
7027  C CG  . ASN A 966  ? 0.4062 0.3456 0.3945 -0.0098 -0.0076 0.0079  964  ASN A CG  
7028  O OD1 . ASN A 966  ? 0.3902 0.3255 0.3737 -0.0069 -0.0065 0.0061  964  ASN A OD1 
7029  N ND2 . ASN A 966  ? 0.3599 0.3060 0.3463 -0.0109 -0.0064 0.0091  964  ASN A ND2 
7030  N N   . ALA A 967  ? 0.4350 0.3638 0.4544 -0.0180 -0.0170 0.0134  965  ALA A N   
7031  C CA  . ALA A 967  ? 0.5148 0.4414 0.5448 -0.0205 -0.0211 0.0130  965  ALA A CA  
7032  C C   . ALA A 967  ? 0.4598 0.3779 0.4952 -0.0183 -0.0239 0.0089  965  ALA A C   
7033  O O   . ALA A 967  ? 0.5253 0.4405 0.5685 -0.0190 -0.0277 0.0058  965  ALA A O   
7034  C CB  . ALA A 967  ? 0.5005 0.4314 0.5387 -0.0261 -0.0219 0.0213  965  ALA A CB  
7035  N N   . THR A 968  ? 0.4771 0.3916 0.5090 -0.0155 -0.0225 0.0082  966  THR A N   
7036  C CA  . THR A 968  ? 0.4675 0.3750 0.5040 -0.0126 -0.0251 0.0029  966  THR A CA  
7037  C C   . THR A 968  ? 0.4583 0.3649 0.4915 -0.0090 -0.0262 -0.0059 966  THR A C   
7038  O O   . THR A 968  ? 0.4613 0.3632 0.5006 -0.0071 -0.0294 -0.0113 966  THR A O   
7039  C CB  . THR A 968  ? 0.4552 0.3604 0.4870 -0.0097 -0.0228 0.0030  966  THR A CB  
7040  O OG1 . THR A 968  ? 0.4263 0.3337 0.4462 -0.0059 -0.0196 -0.0013 966  THR A OG1 
7041  C CG2 . THR A 968  ? 0.4634 0.3709 0.4956 -0.0128 -0.0209 0.0116  966  THR A CG2 
7042  N N   . GLY A 969  ? 0.4248 0.3362 0.4487 -0.0077 -0.0239 -0.0076 967  GLY A N   
7043  C CA  . GLY A 969  ? 0.4366 0.3482 0.4560 -0.0041 -0.0248 -0.0154 967  GLY A CA  
7044  C C   . GLY A 969  ? 0.4110 0.3222 0.4216 0.0007  -0.0225 -0.0195 967  GLY A C   
7045  O O   . GLY A 969  ? 0.3875 0.3005 0.3926 0.0037  -0.0227 -0.0251 967  GLY A O   
7046  N N   . TYR A 970  ? 0.4284 0.3379 0.4376 0.0013  -0.0205 -0.0165 968  TYR A N   
7047  C CA  . TYR A 970  ? 0.4057 0.3158 0.4064 0.0053  -0.0179 -0.0191 968  TYR A CA  
7048  C C   . TYR A 970  ? 0.4142 0.3284 0.4048 0.0053  -0.0142 -0.0157 968  TYR A C   
7049  O O   . TYR A 970  ? 0.4154 0.3320 0.4062 0.0024  -0.0135 -0.0112 968  TYR A O   
7050  C CB  . TYR A 970  ? 0.4003 0.3069 0.4045 0.0058  -0.0174 -0.0174 968  TYR A CB  
7051  C CG  . TYR A 970  ? 0.4303 0.3325 0.4441 0.0070  -0.0213 -0.0224 968  TYR A CG  
7052  C CD1 . TYR A 970  ? 0.4341 0.3368 0.4458 0.0115  -0.0220 -0.0304 968  TYR A CD1 
7053  C CD2 . TYR A 970  ? 0.4715 0.3697 0.4971 0.0037  -0.0244 -0.0192 968  TYR A CD2 
7054  C CE1 . TYR A 970  ? 0.4469 0.3458 0.4681 0.0130  -0.0258 -0.0361 968  TYR A CE1 
7055  C CE2 . TYR A 970  ? 0.4556 0.3491 0.4914 0.0050  -0.0285 -0.0242 968  TYR A CE2 
7056  C CZ  . TYR A 970  ? 0.4767 0.3705 0.5103 0.0098  -0.0292 -0.0331 968  TYR A CZ  
7057  O OH  . TYR A 970  ? 0.5549 0.4445 0.5991 0.0115  -0.0335 -0.0392 968  TYR A OH  
7058  N N   . GLY A 971  ? 0.3350 0.2506 0.3175 0.0087  -0.0120 -0.0178 969  GLY A N   
7059  C CA  . GLY A 971  ? 0.3873 0.3062 0.3613 0.0089  -0.0090 -0.0147 969  GLY A CA  
7060  C C   . GLY A 971  ? 0.3695 0.2895 0.3359 0.0122  -0.0067 -0.0159 969  GLY A C   
7061  O O   . GLY A 971  ? 0.3692 0.2922 0.3289 0.0141  -0.0060 -0.0171 969  GLY A O   
7062  N N   . LEU A 972  ? 0.3614 0.2795 0.3291 0.0130  -0.0057 -0.0151 970  LEU A N   
7063  C CA  . LEU A 972  ? 0.2998 0.2199 0.2610 0.0161  -0.0035 -0.0163 970  LEU A CA  
7064  C C   . LEU A 972  ? 0.3546 0.2753 0.3113 0.0151  -0.0005 -0.0106 970  LEU A C   
7065  O O   . LEU A 972  ? 0.3589 0.2819 0.3098 0.0153  0.0007  -0.0090 970  LEU A O   
7066  C CB  . LEU A 972  ? 0.3210 0.2396 0.2864 0.0181  -0.0042 -0.0198 970  LEU A CB  
7067  C CG  . LEU A 972  ? 0.3958 0.3181 0.3548 0.0217  -0.0023 -0.0224 970  LEU A CG  
7068  C CD1 . LEU A 972  ? 0.3748 0.3019 0.3268 0.0234  -0.0023 -0.0249 970  LEU A CD1 
7069  C CD2 . LEU A 972  ? 0.4026 0.3244 0.3671 0.0242  -0.0038 -0.0279 970  LEU A CD2 
7070  N N   . THR A 973  ? 0.3365 0.2553 0.2965 0.0140  0.0005  -0.0077 971  THR A N   
7071  C CA  . THR A 973  ? 0.3098 0.2292 0.2663 0.0130  0.0031  -0.0027 971  THR A CA  
7072  C C   . THR A 973  ? 0.3206 0.2391 0.2818 0.0095  0.0028  0.0015  971  THR A C   
7073  O O   . THR A 973  ? 0.2969 0.2136 0.2648 0.0078  0.0008  0.0016  971  THR A O   
7074  C CB  . THR A 973  ? 0.3262 0.2456 0.2819 0.0146  0.0048  -0.0023 971  THR A CB  
7075  O OG1 . THR A 973  ? 0.3293 0.2460 0.2922 0.0143  0.0034  -0.0031 971  THR A OG1 
7076  C CG2 . THR A 973  ? 0.3356 0.2580 0.2860 0.0180  0.0055  -0.0060 971  THR A CG2 
7077  N N   . PHE A 974  ? 0.2809 0.2012 0.2386 0.0083  0.0046  0.0051  972  PHE A N   
7078  C CA  . PHE A 974  ? 0.2812 0.2026 0.2420 0.0051  0.0046  0.0091  972  PHE A CA  
7079  C C   . PHE A 974  ? 0.2686 0.1916 0.2257 0.0050  0.0069  0.0120  972  PHE A C   
7080  O O   . PHE A 974  ? 0.3016 0.2254 0.2535 0.0066  0.0080  0.0113  972  PHE A O   
7081  C CB  . PHE A 974  ? 0.3096 0.2335 0.2707 0.0036  0.0036  0.0087  972  PHE A CB  
7082  C CG  . PHE A 974  ? 0.2741 0.2015 0.2371 0.0007  0.0041  0.0126  972  PHE A CG  
7083  C CD1 . PHE A 974  ? 0.3024 0.2306 0.2717 -0.0022 0.0030  0.0154  972  PHE A CD1 
7084  C CD2 . PHE A 974  ? 0.2786 0.2090 0.2375 0.0008  0.0056  0.0135  972  PHE A CD2 
7085  C CE1 . PHE A 974  ? 0.3273 0.2603 0.2978 -0.0049 0.0036  0.0192  972  PHE A CE1 
7086  C CE2 . PHE A 974  ? 0.2818 0.2168 0.2422 -0.0016 0.0061  0.0163  972  PHE A CE2 
7087  C CZ  . PHE A 974  ? 0.3030 0.2399 0.2689 -0.0045 0.0053  0.0192  972  PHE A CZ  
7088  N N   . GLY A 975  ? 0.2979 0.2216 0.2581 0.0030  0.0074  0.0156  973  GLY A N   
7089  C CA  . GLY A 975  ? 0.2706 0.1960 0.2280 0.0027  0.0092  0.0181  973  GLY A CA  
7090  C C   . GLY A 975  ? 0.2570 0.1867 0.2159 0.0000  0.0093  0.0208  973  GLY A C   
7091  O O   . GLY A 975  ? 0.2919 0.2231 0.2551 -0.0022 0.0081  0.0225  973  GLY A O   
7092  N N   . LEU A 976  ? 0.2852 0.2172 0.2407 0.0002  0.0105  0.0211  974  LEU A N   
7093  C CA  . LEU A 976  ? 0.2499 0.1873 0.2064 -0.0020 0.0108  0.0230  974  LEU A CA  
7094  C C   . LEU A 976  ? 0.3129 0.2515 0.2677 -0.0018 0.0121  0.0242  974  LEU A C   
7095  O O   . LEU A 976  ? 0.2947 0.2312 0.2464 0.0000  0.0127  0.0228  974  LEU A O   
7096  C CB  . LEU A 976  ? 0.3207 0.2612 0.2757 -0.0018 0.0103  0.0206  974  LEU A CB  
7097  C CG  . LEU A 976  ? 0.3121 0.2596 0.2679 -0.0036 0.0106  0.0215  974  LEU A CG  
7098  C CD1 . LEU A 976  ? 0.2890 0.2411 0.2491 -0.0067 0.0101  0.0247  974  LEU A CD1 
7099  C CD2 . LEU A 976  ? 0.2945 0.2443 0.2488 -0.0024 0.0101  0.0181  974  LEU A CD2 
7100  N N   . HIS A 977  ? 0.2897 0.2318 0.2469 -0.0038 0.0123  0.0272  975  HIS A N   
7101  C CA  . HIS A 977  ? 0.3102 0.2548 0.2663 -0.0040 0.0133  0.0283  975  HIS A CA  
7102  C C   . HIS A 977  ? 0.2774 0.2298 0.2339 -0.0058 0.0132  0.0284  975  HIS A C   
7103  O O   . HIS A 977  ? 0.2886 0.2460 0.2478 -0.0081 0.0128  0.0312  975  HIS A O   
7104  C CB  . HIS A 977  ? 0.2991 0.2427 0.2576 -0.0048 0.0135  0.0316  975  HIS A CB  
7105  C CG  . HIS A 977  ? 0.3249 0.2630 0.2820 -0.0026 0.0142  0.0308  975  HIS A CG  
7106  N ND1 . HIS A 977  ? 0.3457 0.2840 0.3012 -0.0020 0.0153  0.0310  975  HIS A ND1 
7107  C CD2 . HIS A 977  ? 0.3484 0.2817 0.3056 -0.0009 0.0141  0.0295  975  HIS A CD2 
7108  C CE1 . HIS A 977  ? 0.3545 0.2886 0.3092 -0.0002 0.0159  0.0305  975  HIS A CE1 
7109  N NE2 . HIS A 977  ? 0.3501 0.2814 0.3057 0.0007  0.0152  0.0293  975  HIS A NE2 
7110  N N   . THR A 978  ? 0.2871 0.2411 0.2415 -0.0046 0.0134  0.0254  976  THR A N   
7111  C CA  . THR A 978  ? 0.3274 0.2895 0.2821 -0.0055 0.0132  0.0240  976  THR A CA  
7112  C C   . THR A 978  ? 0.3190 0.2800 0.2723 -0.0035 0.0132  0.0206  976  THR A C   
7113  O O   . THR A 978  ? 0.3089 0.2633 0.2608 -0.0016 0.0130  0.0194  976  THR A O   
7114  C CB  . THR A 978  ? 0.3119 0.2781 0.2674 -0.0060 0.0126  0.0226  976  THR A CB  
7115  O OG1 . THR A 978  ? 0.2987 0.2742 0.2547 -0.0066 0.0126  0.0207  976  THR A OG1 
7116  C CG2 . THR A 978  ? 0.3027 0.2633 0.2567 -0.0038 0.0120  0.0193  976  THR A CG2 
7117  N N   . ARG A 979  ? 0.3361 0.3040 0.2900 -0.0040 0.0131  0.0191  977  ARG A N   
7118  C CA  . ARG A 979  ? 0.3354 0.3029 0.2894 -0.0022 0.0124  0.0151  977  ARG A CA  
7119  C C   . ARG A 979  ? 0.3466 0.3187 0.3014 -0.0012 0.0114  0.0108  977  ARG A C   
7120  O O   . ARG A 979  ? 0.3571 0.3283 0.3129 0.0006  0.0103  0.0070  977  ARG A O   
7121  C CB  . ARG A 979  ? 0.3279 0.3002 0.2828 -0.0028 0.0125  0.0148  977  ARG A CB  
7122  C CG  . ARG A 979  ? 0.4071 0.3744 0.3617 -0.0033 0.0132  0.0183  977  ARG A CG  
7123  C CD  . ARG A 979  ? 0.4724 0.4460 0.4280 -0.0043 0.0132  0.0184  977  ARG A CD  
7124  N NE  . ARG A 979  ? 0.5303 0.4989 0.4860 -0.0044 0.0138  0.0212  977  ARG A NE  
7125  C CZ  . ARG A 979  ? 0.5803 0.5527 0.5370 -0.0051 0.0137  0.0215  977  ARG A CZ  
7126  N NH1 . ARG A 979  ? 0.4912 0.4727 0.4486 -0.0057 0.0131  0.0190  977  ARG A NH1 
7127  N NH2 . ARG A 979  ? 0.5968 0.5645 0.5539 -0.0051 0.0142  0.0241  977  ARG A NH2 
7128  N N   . LEU A 980  ? 0.2969 0.2740 0.2520 -0.0023 0.0116  0.0114  978  LEU A N   
7129  C CA  . LEU A 980  ? 0.2972 0.2817 0.2535 -0.0017 0.0109  0.0073  978  LEU A CA  
7130  C C   . LEU A 980  ? 0.3069 0.2861 0.2630 -0.0001 0.0100  0.0055  978  LEU A C   
7131  O O   . LEU A 980  ? 0.3087 0.2845 0.2641 -0.0010 0.0103  0.0082  978  LEU A O   
7132  C CB  . LEU A 980  ? 0.2841 0.2793 0.2412 -0.0043 0.0116  0.0092  978  LEU A CB  
7133  C CG  . LEU A 980  ? 0.3127 0.3137 0.2697 -0.0062 0.0124  0.0120  978  LEU A CG  
7134  C CD1 . LEU A 980  ? 0.3395 0.3517 0.2974 -0.0091 0.0130  0.0151  978  LEU A CD1 
7135  C CD2 . LEU A 980  ? 0.3393 0.3442 0.2967 -0.0045 0.0119  0.0072  978  LEU A CD2 
7136  N N   . ASP A 981  ? 0.2878 0.2666 0.2451 0.0023  0.0086  0.0009  979  ASP A N   
7137  C CA  . ASP A 981  ? 0.2909 0.2652 0.2483 0.0041  0.0075  -0.0008 979  ASP A CA  
7138  C C   . ASP A 981  ? 0.2761 0.2562 0.2340 0.0030  0.0077  -0.0008 979  ASP A C   
7139  O O   . ASP A 981  ? 0.3142 0.2897 0.2713 0.0034  0.0072  0.0000  979  ASP A O   
7140  C CB  . ASP A 981  ? 0.2970 0.2712 0.2569 0.0068  0.0055  -0.0058 979  ASP A CB  
7141  C CG  . ASP A 981  ? 0.3526 0.3186 0.3127 0.0080  0.0047  -0.0051 979  ASP A CG  
7142  O OD1 . ASP A 981  ? 0.3963 0.3564 0.3540 0.0070  0.0058  -0.0009 979  ASP A OD1 
7143  O OD2 . ASP A 981  ? 0.4146 0.3805 0.3780 0.0099  0.0028  -0.0090 979  ASP A OD2 
7144  N N   . GLU A 982  ? 0.2804 0.2717 0.2398 0.0015  0.0083  -0.0018 980  GLU A N   
7145  C CA  . GLU A 982  ? 0.3037 0.3014 0.2642 0.0002  0.0084  -0.0015 980  GLU A CA  
7146  C C   . GLU A 982  ? 0.3253 0.3186 0.2850 -0.0022 0.0091  0.0039  980  GLU A C   
7147  O O   . GLU A 982  ? 0.2766 0.2685 0.2369 -0.0025 0.0085  0.0042  980  GLU A O   
7148  C CB  . GLU A 982  ? 0.2919 0.3039 0.2540 -0.0013 0.0092  -0.0029 980  GLU A CB  
7149  C CG  . GLU A 982  ? 0.3348 0.3542 0.2984 -0.0035 0.0096  -0.0011 980  GLU A CG  
7150  C CD  . GLU A 982  ? 0.3894 0.4240 0.3541 -0.0061 0.0108  0.0001  980  GLU A CD  
7151  O OE1 . GLU A 982  ? 0.4415 0.4781 0.4055 -0.0084 0.0117  0.0045  980  GLU A OE1 
7152  O OE2 . GLU A 982  ? 0.3903 0.4357 0.3570 -0.0057 0.0107  -0.0032 980  GLU A OE2 
7153  N N   . THR A 983  ? 0.2983 0.2890 0.2570 -0.0038 0.0100  0.0079  981  THR A N   
7154  C CA  . THR A 983  ? 0.2947 0.2805 0.2537 -0.0058 0.0102  0.0126  981  THR A CA  
7155  C C   . THR A 983  ? 0.2992 0.2737 0.2565 -0.0038 0.0095  0.0120  981  THR A C   
7156  O O   . THR A 983  ? 0.3094 0.2808 0.2676 -0.0045 0.0090  0.0133  981  THR A O   
7157  C CB  . THR A 983  ? 0.3021 0.2884 0.2610 -0.0077 0.0111  0.0167  981  THR A CB  
7158  O OG1 . THR A 983  ? 0.3050 0.3033 0.2652 -0.0097 0.0117  0.0177  981  THR A OG1 
7159  C CG2 . THR A 983  ? 0.3072 0.2881 0.2676 -0.0095 0.0109  0.0213  981  THR A CG2 
7160  N N   . ILE A 984  ? 0.2827 0.2517 0.2380 -0.0014 0.0094  0.0100  982  ILE A N   
7161  C CA  . ILE A 984  ? 0.3151 0.2752 0.2685 0.0006  0.0087  0.0096  982  ILE A CA  
7162  C C   . ILE A 984  ? 0.3293 0.2899 0.2831 0.0017  0.0075  0.0070  982  ILE A C   
7163  O O   . ILE A 984  ? 0.2881 0.2445 0.2412 0.0019  0.0069  0.0075  982  ILE A O   
7164  C CB  . ILE A 984  ? 0.2489 0.2043 0.2007 0.0027  0.0086  0.0086  982  ILE A CB  
7165  C CG1 . ILE A 984  ? 0.3026 0.2566 0.2539 0.0017  0.0099  0.0114  982  ILE A CG1 
7166  C CG2 . ILE A 984  ? 0.2810 0.2292 0.2307 0.0047  0.0079  0.0084  982  ILE A CG2 
7167  C CD1 . ILE A 984  ? 0.3483 0.2991 0.2991 0.0031  0.0097  0.0107  982  ILE A CD1 
7168  N N   . ALA A 985  ? 0.3030 0.2693 0.2582 0.0025  0.0068  0.0038  983  ALA A N   
7169  C CA  . ALA A 985  ? 0.3533 0.3206 0.3093 0.0038  0.0055  0.0011  983  ALA A CA  
7170  C C   . ALA A 985  ? 0.3006 0.2711 0.2582 0.0015  0.0055  0.0026  983  ALA A C   
7171  O O   . ALA A 985  ? 0.3282 0.2948 0.2854 0.0020  0.0045  0.0023  983  ALA A O   
7172  C CB  . ALA A 985  ? 0.3234 0.2974 0.2816 0.0051  0.0047  -0.0030 983  ALA A CB  
7173  N N   . HIS A 986  ? 0.2776 0.2553 0.2372 -0.0013 0.0065  0.0046  984  HIS A N   
7174  C CA  . HIS A 986  ? 0.3149 0.2964 0.2773 -0.0041 0.0064  0.0069  984  HIS A CA  
7175  C C   . HIS A 986  ? 0.3293 0.3022 0.2914 -0.0047 0.0059  0.0094  984  HIS A C   
7176  O O   . HIS A 986  ? 0.3290 0.2998 0.2924 -0.0047 0.0046  0.0085  984  HIS A O   
7177  C CB  . HIS A 986  ? 0.3300 0.3207 0.2944 -0.0072 0.0075  0.0099  984  HIS A CB  
7178  C CG  . HIS A 986  ? 0.3642 0.3584 0.3322 -0.0107 0.0073  0.0140  984  HIS A CG  
7179  N ND1 . HIS A 986  ? 0.4151 0.4171 0.3853 -0.0140 0.0081  0.0183  984  HIS A ND1 
7180  C CD2 . HIS A 986  ? 0.3327 0.3241 0.3032 -0.0118 0.0060  0.0146  984  HIS A CD2 
7181  C CE1 . HIS A 986  ? 0.4006 0.4040 0.3749 -0.0170 0.0073  0.0219  984  HIS A CE1 
7182  N NE2 . HIS A 986  ? 0.3321 0.3289 0.3068 -0.0157 0.0060  0.0194  984  HIS A NE2 
7183  N N   . VAL A 987  ? 0.2862 0.2548 0.2474 -0.0051 0.0067  0.0120  985  VAL A N   
7184  C CA  . VAL A 987  ? 0.3174 0.2791 0.2794 -0.0056 0.0062  0.0140  985  VAL A CA  
7185  C C   . VAL A 987  ? 0.3403 0.2949 0.2997 -0.0028 0.0052  0.0111  985  VAL A C   
7186  O O   . VAL A 987  ? 0.3294 0.2812 0.2904 -0.0030 0.0040  0.0105  985  VAL A O   
7187  C CB  . VAL A 987  ? 0.2892 0.2484 0.2507 -0.0063 0.0072  0.0171  985  VAL A CB  
7188  C CG1 . VAL A 987  ? 0.3029 0.2542 0.2650 -0.0057 0.0066  0.0178  985  VAL A CG1 
7189  C CG2 . VAL A 987  ? 0.2936 0.2604 0.2584 -0.0096 0.0077  0.0209  985  VAL A CG2 
7190  N N   . THR A 988  ? 0.3115 0.2634 0.2671 -0.0002 0.0056  0.0092  986  THR A N   
7191  C CA  . THR A 988  ? 0.3327 0.2791 0.2856 0.0024  0.0047  0.0072  986  THR A CA  
7192  C C   . THR A 988  ? 0.3896 0.3381 0.3431 0.0031  0.0032  0.0046  986  THR A C   
7193  O O   . THR A 988  ? 0.3542 0.2992 0.3062 0.0046  0.0021  0.0031  986  THR A O   
7194  C CB  . THR A 988  ? 0.3877 0.3310 0.3369 0.0047  0.0053  0.0069  986  THR A CB  
7195  O OG1 . THR A 988  ? 0.3440 0.2908 0.2936 0.0055  0.0049  0.0053  986  THR A OG1 
7196  C CG2 . THR A 988  ? 0.3970 0.3384 0.3457 0.0041  0.0068  0.0095  986  THR A CG2 
7197  N N   . SER A 989  ? 0.3230 0.2780 0.2790 0.0020  0.0030  0.0037  987  SER A N   
7198  C CA  . SER A 989  ? 0.3748 0.3321 0.3319 0.0026  0.0014  0.0012  987  SER A CA  
7199  C C   . SER A 989  ? 0.3845 0.3430 0.3453 0.0002  0.0005  0.0020  987  SER A C   
7200  O O   . SER A 989  ? 0.4149 0.3730 0.3763 0.0009  -0.0011 -0.0002 987  SER A O   
7201  C CB  . SER A 989  ? 0.3665 0.3309 0.3252 0.0030  0.0013  -0.0008 987  SER A CB  
7202  O OG  . SER A 989  ? 0.4264 0.3984 0.3883 0.0002  0.0023  0.0007  987  SER A OG  
7203  N N   . ARG A 990  ? 0.3616 0.3211 0.3252 -0.0026 0.0013  0.0051  988  ARG A N   
7204  C CA  . ARG A 990  ? 0.3503 0.3109 0.3189 -0.0054 0.0001  0.0065  988  ARG A CA  
7205  C C   . ARG A 990  ? 0.3631 0.3163 0.3325 -0.0052 -0.0008 0.0069  988  ARG A C   
7206  O O   . ARG A 990  ? 0.3410 0.2933 0.3146 -0.0065 -0.0026 0.0063  988  ARG A O   
7207  C CB  . ARG A 990  ? 0.3647 0.3323 0.3372 -0.0090 0.0010  0.0105  988  ARG A CB  
7208  C CG  . ARG A 990  ? 0.4228 0.3997 0.3951 -0.0092 0.0018  0.0095  988  ARG A CG  
7209  C CD  . ARG A 990  ? 0.4550 0.4370 0.4308 -0.0102 0.0005  0.0079  988  ARG A CD  
7210  N NE  . ARG A 990  ? 0.4363 0.4262 0.4173 -0.0145 0.0006  0.0120  988  ARG A NE  
7211  C CZ  . ARG A 990  ? 0.4236 0.4196 0.4091 -0.0166 -0.0004 0.0121  988  ARG A CZ  
7212  N NH1 . ARG A 990  ? 0.4344 0.4286 0.4199 -0.0148 -0.0019 0.0082  988  ARG A NH1 
7213  N NH2 . ARG A 990  ? 0.4131 0.4179 0.4032 -0.0207 0.0000  0.0166  988  ARG A NH2 
7214  N N   . ILE A 991  ? 0.3566 0.3049 0.3229 -0.0037 0.0003  0.0075  989  ILE A N   
7215  C CA  . ILE A 991  ? 0.3351 0.2772 0.3024 -0.0031 -0.0005 0.0072  989  ILE A CA  
7216  C C   . ILE A 991  ? 0.3535 0.2925 0.3183 -0.0003 -0.0019 0.0029  989  ILE A C   
7217  O O   . ILE A 991  ? 0.3811 0.3211 0.3415 0.0018  -0.0017 0.0009  989  ILE A O   
7218  C CB  . ILE A 991  ? 0.3527 0.2916 0.3171 -0.0020 0.0012  0.0089  989  ILE A CB  
7219  C CG1 . ILE A 991  ? 0.3288 0.2627 0.2962 -0.0019 0.0004  0.0090  989  ILE A CG1 
7220  C CG2 . ILE A 991  ? 0.3537 0.2912 0.3117 0.0011  0.0023  0.0070  989  ILE A CG2 
7221  C CD1 . ILE A 991  ? 0.3819 0.3167 0.3566 -0.0054 -0.0008 0.0124  989  ILE A CD1 
7222  N N   . LYS A 992  ? 0.3200 0.2556 0.2881 -0.0004 -0.0036 0.0012  990  LYS A N   
7223  C CA  . LYS A 992  ? 0.3775 0.3112 0.3436 0.0022  -0.0052 -0.0033 990  LYS A CA  
7224  C C   . LYS A 992  ? 0.3953 0.3246 0.3599 0.0044  -0.0050 -0.0050 990  LYS A C   
7225  O O   . LYS A 992  ? 0.4028 0.3295 0.3721 0.0042  -0.0068 -0.0069 990  LYS A O   
7226  C CB  . LYS A 992  ? 0.3577 0.2925 0.3297 0.0005  -0.0079 -0.0052 990  LYS A CB  
7227  C CG  . LYS A 992  ? 0.4016 0.3418 0.3743 -0.0009 -0.0080 -0.0046 990  LYS A CG  
7228  C CD  . LYS A 992  ? 0.4981 0.4396 0.4774 -0.0030 -0.0108 -0.0061 990  LYS A CD  
7229  C CE  . LYS A 992  ? 0.5833 0.5313 0.5633 -0.0041 -0.0110 -0.0060 990  LYS A CE  
7230  N NZ  . LYS A 992  ? 0.6752 0.6253 0.6626 -0.0068 -0.0135 -0.0067 990  LYS A NZ  
7231  N N   . ALA A 993  ? 0.3794 0.3081 0.3378 0.0066  -0.0031 -0.0044 991  ALA A N   
7232  C CA  . ALA A 993  ? 0.3893 0.3155 0.3459 0.0088  -0.0025 -0.0059 991  ALA A CA  
7233  C C   . ALA A 993  ? 0.3513 0.2787 0.3004 0.0117  -0.0014 -0.0069 991  ALA A C   
7234  O O   . ALA A 993  ? 0.3636 0.2927 0.3094 0.0118  -0.0007 -0.0050 991  ALA A O   
7235  C CB  . ALA A 993  ? 0.3343 0.2587 0.2926 0.0076  -0.0009 -0.0024 991  ALA A CB  
7236  N N   . GLY A 994  ? 0.3231 0.2502 0.2701 0.0142  -0.0015 -0.0097 992  GLY A N   
7237  C CA  . GLY A 994  ? 0.3434 0.2728 0.2835 0.0168  -0.0007 -0.0101 992  GLY A CA  
7238  C C   . GLY A 994  ? 0.3247 0.2540 0.2612 0.0171  0.0018  -0.0063 992  GLY A C   
7239  O O   . GLY A 994  ? 0.3255 0.2566 0.2569 0.0183  0.0024  -0.0047 992  GLY A O   
7240  N N   . ASN A 995  ? 0.3376 0.2649 0.2769 0.0160  0.0031  -0.0044 993  ASN A N   
7241  C CA  . ASN A 995  ? 0.3560 0.2832 0.2924 0.0162  0.0054  -0.0010 993  ASN A CA  
7242  C C   . ASN A 995  ? 0.2842 0.2097 0.2242 0.0137  0.0062  0.0023  993  ASN A C   
7243  O O   . ASN A 995  ? 0.2998 0.2237 0.2444 0.0125  0.0060  0.0023  993  ASN A O   
7244  C CB  . ASN A 995  ? 0.3183 0.2463 0.2539 0.0181  0.0064  -0.0025 993  ASN A CB  
7245  C CG  . ASN A 995  ? 0.3412 0.2731 0.2714 0.0208  0.0064  -0.0045 993  ASN A CG  
7246  O OD1 . ASN A 995  ? 0.3436 0.2771 0.2736 0.0221  0.0047  -0.0086 993  ASN A OD1 
7247  N ND2 . ASN A 995  ? 0.3084 0.2425 0.2342 0.0214  0.0082  -0.0012 993  ASN A ND2 
7248  N N   . LEU A 996  ? 0.3251 0.2512 0.2635 0.0128  0.0069  0.0049  994  LEU A N   
7249  C CA  . LEU A 996  ? 0.2816 0.2076 0.2228 0.0105  0.0076  0.0077  994  LEU A CA  
7250  C C   . LEU A 996  ? 0.2986 0.2241 0.2380 0.0107  0.0095  0.0104  994  LEU A C   
7251  O O   . LEU A 996  ? 0.2869 0.2127 0.2226 0.0122  0.0100  0.0110  994  LEU A O   
7252  C CB  . LEU A 996  ? 0.2717 0.1995 0.2130 0.0096  0.0068  0.0078  994  LEU A CB  
7253  C CG  . LEU A 996  ? 0.3241 0.2529 0.2670 0.0095  0.0049  0.0051  994  LEU A CG  
7254  C CD1 . LEU A 996  ? 0.3544 0.2859 0.2981 0.0087  0.0042  0.0050  994  LEU A CD1 
7255  C CD2 . LEU A 996  ? 0.3458 0.2738 0.2935 0.0079  0.0041  0.0044  994  LEU A CD2 
7256  N N   . TYR A 997  ? 0.2906 0.2160 0.2328 0.0090  0.0102  0.0124  995  TYR A N   
7257  C CA  . TYR A 997  ? 0.2773 0.2025 0.2186 0.0090  0.0119  0.0149  995  TYR A CA  
7258  C C   . TYR A 997  ? 0.2647 0.1914 0.2084 0.0068  0.0121  0.0168  995  TYR A C   
7259  O O   . TYR A 997  ? 0.2981 0.2257 0.2452 0.0051  0.0116  0.0174  995  TYR A O   
7260  C CB  . TYR A 997  ? 0.2858 0.2099 0.2283 0.0096  0.0126  0.0150  995  TYR A CB  
7261  C CG  . TYR A 997  ? 0.2926 0.2168 0.2326 0.0121  0.0126  0.0125  995  TYR A CG  
7262  C CD1 . TYR A 997  ? 0.3190 0.2446 0.2549 0.0135  0.0137  0.0134  995  TYR A CD1 
7263  C CD2 . TYR A 997  ? 0.3046 0.2282 0.2466 0.0128  0.0111  0.0092  995  TYR A CD2 
7264  C CE1 . TYR A 997  ? 0.3222 0.2496 0.2553 0.0158  0.0138  0.0112  995  TYR A CE1 
7265  C CE2 . TYR A 997  ? 0.3247 0.2496 0.2642 0.0153  0.0110  0.0061  995  TYR A CE2 
7266  C CZ  . TYR A 997  ? 0.3568 0.2842 0.2915 0.0168  0.0124  0.0072  995  TYR A CZ  
7267  O OH  . TYR A 997  ? 0.3723 0.3027 0.3040 0.0193  0.0124  0.0043  995  TYR A OH  
7268  N N   . ILE A 998  ? 0.2419 0.1693 0.1843 0.0068  0.0126  0.0180  996  ILE A N   
7269  C CA  A ILE A 998  ? 0.2735 0.2035 0.2178 0.0050  0.0127  0.0189  996  ILE A CA  
7270  C CA  B ILE A 998  ? 0.2776 0.2076 0.2219 0.0050  0.0127  0.0189  996  ILE A CA  
7271  C C   . ILE A 998  ? 0.2544 0.1841 0.1989 0.0047  0.0139  0.0210  996  ILE A C   
7272  O O   . ILE A 998  ? 0.2815 0.2097 0.2243 0.0057  0.0143  0.0216  996  ILE A O   
7273  C CB  A ILE A 998  ? 0.3002 0.2319 0.2441 0.0054  0.0118  0.0173  996  ILE A CB  
7274  C CB  B ILE A 998  ? 0.3044 0.2359 0.2482 0.0055  0.0118  0.0174  996  ILE A CB  
7275  C CG1 A ILE A 998  ? 0.2909 0.2235 0.2350 0.0055  0.0105  0.0152  996  ILE A CG1 
7276  C CG1 B ILE A 998  ? 0.2937 0.2253 0.2369 0.0061  0.0105  0.0152  996  ILE A CG1 
7277  C CG2 A ILE A 998  ? 0.2801 0.2156 0.2260 0.0039  0.0119  0.0175  996  ILE A CG2 
7278  C CG2 B ILE A 998  ? 0.2800 0.2158 0.2260 0.0039  0.0118  0.0173  996  ILE A CG2 
7279  C CD1 A ILE A 998  ? 0.2899 0.2241 0.2339 0.0064  0.0093  0.0132  996  ILE A CD1 
7280  C CD1 B ILE A 998  ? 0.2822 0.2169 0.2282 0.0044  0.0101  0.0148  996  ILE A CD1 
7281  N N   . ASN A 999  ? 0.2667 0.1982 0.2137 0.0031  0.0144  0.0226  997  ASN A N   
7282  C CA  . ASN A 999  ? 0.2981 0.2302 0.2458 0.0026  0.0153  0.0246  997  ASN A CA  
7283  C C   . ASN A 999  ? 0.2771 0.2063 0.2238 0.0039  0.0164  0.0256  997  ASN A C   
7284  O O   . ASN A 999  ? 0.2782 0.2074 0.2245 0.0040  0.0171  0.0267  997  ASN A O   
7285  C CB  . ASN A 999  ? 0.3046 0.2387 0.2522 0.0023  0.0151  0.0240  997  ASN A CB  
7286  C CG  . ASN A 999  ? 0.3079 0.2470 0.2569 0.0009  0.0143  0.0229  997  ASN A CG  
7287  O OD1 . ASN A 999  ? 0.3188 0.2606 0.2694 -0.0005 0.0144  0.0241  997  ASN A OD1 
7288  N ND2 . ASN A 999  ? 0.2968 0.2376 0.2459 0.0014  0.0136  0.0206  997  ASN A ND2 
7289  N N   . ARG A 1000 ? 0.3281 0.2555 0.2748 0.0049  0.0163  0.0248  998  ARG A N   
7290  C CA  . ARG A 1000 ? 0.2804 0.2066 0.2264 0.0065  0.0173  0.0249  998  ARG A CA  
7291  C C   . ARG A 1000 ? 0.3015 0.2265 0.2497 0.0072  0.0167  0.0234  998  ARG A C   
7292  O O   . ARG A 1000 ? 0.3169 0.2417 0.2674 0.0061  0.0154  0.0229  998  ARG A O   
7293  C CB  . ARG A 1000 ? 0.2885 0.2144 0.2308 0.0081  0.0177  0.0243  998  ARG A CB  
7294  C CG  . ARG A 1000 ? 0.2802 0.2056 0.2204 0.0088  0.0165  0.0222  998  ARG A CG  
7295  C CD  . ARG A 1000 ? 0.2967 0.2225 0.2334 0.0107  0.0168  0.0217  998  ARG A CD  
7296  N NE  . ARG A 1000 ? 0.3157 0.2421 0.2525 0.0122  0.0175  0.0202  998  ARG A NE  
7297  C CZ  . ARG A 1000 ? 0.3299 0.2583 0.2636 0.0141  0.0180  0.0193  998  ARG A CZ  
7298  N NH1 . ARG A 1000 ? 0.3467 0.2764 0.2770 0.0145  0.0179  0.0207  998  ARG A NH1 
7299  N NH2 . ARG A 1000 ? 0.3291 0.2589 0.2636 0.0157  0.0184  0.0168  998  ARG A NH2 
7300  N N   . ASN A 1001 ? 0.3022 0.2268 0.2505 0.0090  0.0174  0.0226  999  ASN A N   
7301  C CA  . ASN A 1001 ? 0.3014 0.2247 0.2525 0.0101  0.0164  0.0201  999  ASN A CA  
7302  C C   . ASN A 1001 ? 0.3147 0.2377 0.2634 0.0113  0.0154  0.0169  999  ASN A C   
7303  O O   . ASN A 1001 ? 0.3102 0.2341 0.2549 0.0114  0.0157  0.0171  999  ASN A O   
7304  C CB  . ASN A 1001 ? 0.2857 0.2098 0.2379 0.0121  0.0174  0.0193  999  ASN A CB  
7305  C CG  . ASN A 1001 ? 0.3424 0.2691 0.2898 0.0142  0.0189  0.0180  999  ASN A CG  
7306  O OD1 . ASN A 1001 ? 0.3819 0.3091 0.3260 0.0151  0.0184  0.0161  999  ASN A OD1 
7307  N ND2 . ASN A 1001 ? 0.4025 0.3313 0.3496 0.0149  0.0205  0.0194  999  ASN A ND2 
7308  N N   . ILE A 1002 ? 0.2916 0.2132 0.2434 0.0122  0.0139  0.0140  1000 ILE A N   
7309  C CA  . ILE A 1002 ? 0.3392 0.2608 0.2895 0.0131  0.0126  0.0107  1000 ILE A CA  
7310  C C   . ILE A 1002 ? 0.3549 0.2778 0.3039 0.0162  0.0126  0.0066  1000 ILE A C   
7311  O O   . ILE A 1002 ? 0.3336 0.2566 0.2826 0.0173  0.0111  0.0029  1000 ILE A O   
7312  C CB  . ILE A 1002 ? 0.3313 0.2509 0.2867 0.0113  0.0103  0.0103  1000 ILE A CB  
7313  C CG1 . ILE A 1002 ? 0.2774 0.1947 0.2394 0.0117  0.0089  0.0091  1000 ILE A CG1 
7314  C CG2 . ILE A 1002 ? 0.3335 0.2537 0.2896 0.0083  0.0105  0.0143  1000 ILE A CG2 
7315  C CD1 . ILE A 1002 ? 0.3479 0.2631 0.3159 0.0098  0.0063  0.0090  1000 ILE A CD1 
7316  N N   . ILE A 1003 ? 0.2959 0.2209 0.2439 0.0177  0.0143  0.0068  1001 ILE A N   
7317  C CA  . ILE A 1003 ? 0.3396 0.2675 0.2868 0.0208  0.0145  0.0025  1001 ILE A CA  
7318  C C   . ILE A 1003 ? 0.3520 0.2848 0.2927 0.0220  0.0167  0.0038  1001 ILE A C   
7319  O O   . ILE A 1003 ? 0.3799 0.3128 0.3180 0.0204  0.0180  0.0082  1001 ILE A O   
7320  C CB  . ILE A 1003 ? 0.3045 0.2318 0.2575 0.0221  0.0143  0.0008  1001 ILE A CB  
7321  C CG1 . ILE A 1003 ? 0.3597 0.2880 0.3125 0.0212  0.0164  0.0050  1001 ILE A CG1 
7322  C CG2 . ILE A 1003 ? 0.3151 0.2374 0.2755 0.0208  0.0115  0.0000  1001 ILE A CG2 
7323  C CD1 . ILE A 1003 ? 0.3795 0.3087 0.3375 0.0233  0.0165  0.0030  1001 ILE A CD1 
7324  N N   . GLY A 1004 ? 0.3931 0.3306 0.3317 0.0248  0.0170  -0.0002 1002 GLY A N   
7325  C CA  . GLY A 1004 ? 0.3907 0.3343 0.3236 0.0259  0.0191  0.0015  1002 GLY A CA  
7326  C C   . GLY A 1004 ? 0.4309 0.3758 0.3583 0.0251  0.0190  0.0039  1002 GLY A C   
7327  O O   . GLY A 1004 ? 0.3695 0.3165 0.2936 0.0242  0.0205  0.0086  1002 GLY A O   
7328  N N   . ALA A 1005 ? 0.3530 0.2965 0.2798 0.0254  0.0169  0.0011  1003 ALA A N   
7329  C CA  . ALA A 1005 ? 0.3590 0.3038 0.2810 0.0250  0.0164  0.0031  1003 ALA A CA  
7330  C C   . ALA A 1005 ? 0.3914 0.3436 0.3079 0.0264  0.0180  0.0049  1003 ALA A C   
7331  O O   . ALA A 1005 ? 0.3885 0.3465 0.3041 0.0288  0.0187  0.0014  1003 ALA A O   
7332  C CB  . ALA A 1005 ? 0.3659 0.3098 0.2882 0.0258  0.0139  -0.0014 1003 ALA A CB  
7333  N N   . VAL A 1006 ? 0.3524 0.3050 0.2661 0.0250  0.0184  0.0104  1004 VAL A N   
7334  C CA  . VAL A 1006 ? 0.3689 0.3288 0.2780 0.0257  0.0199  0.0139  1004 VAL A CA  
7335  C C   . VAL A 1006 ? 0.3600 0.3237 0.2646 0.0267  0.0183  0.0134  1004 VAL A C   
7336  O O   . VAL A 1006 ? 0.3593 0.3185 0.2643 0.0257  0.0164  0.0143  1004 VAL A O   
7337  C CB  . VAL A 1006 ? 0.3595 0.3176 0.2693 0.0233  0.0209  0.0208  1004 VAL A CB  
7338  C CG1 . VAL A 1006 ? 0.4204 0.3859 0.3259 0.0234  0.0218  0.0255  1004 VAL A CG1 
7339  C CG2 . VAL A 1006 ? 0.3179 0.2743 0.2315 0.0225  0.0226  0.0211  1004 VAL A CG2 
7340  N N   . VAL A 1007 ? 0.3492 0.3221 0.2497 0.0288  0.0191  0.0120  1005 VAL A N   
7341  C CA  . VAL A 1007 ? 0.3251 0.3034 0.2208 0.0301  0.0177  0.0117  1005 VAL A CA  
7342  C C   . VAL A 1007 ? 0.3187 0.2948 0.2131 0.0280  0.0168  0.0190  1005 VAL A C   
7343  O O   . VAL A 1007 ? 0.3254 0.3019 0.2202 0.0264  0.0181  0.0252  1005 VAL A O   
7344  C CB  . VAL A 1007 ? 0.3393 0.3299 0.2305 0.0324  0.0192  0.0102  1005 VAL A CB  
7345  C CG1 . VAL A 1007 ? 0.3255 0.3231 0.2111 0.0334  0.0177  0.0114  1005 VAL A CG1 
7346  C CG2 . VAL A 1007 ? 0.3332 0.3260 0.2266 0.0350  0.0194  0.0015  1005 VAL A CG2 
7347  N N   . GLY A 1008 ? 0.3362 0.3100 0.2296 0.0282  0.0142  0.0182  1006 GLY A N   
7348  C CA  . GLY A 1008 ? 0.2965 0.2686 0.1893 0.0267  0.0128  0.0245  1006 GLY A CA  
7349  C C   . GLY A 1008 ? 0.3291 0.2917 0.2270 0.0244  0.0123  0.0273  1006 GLY A C   
7350  O O   . GLY A 1008 ? 0.3638 0.3238 0.2624 0.0234  0.0106  0.0319  1006 GLY A O   
7351  N N   . VAL A 1009 ? 0.3420 0.3000 0.2436 0.0237  0.0135  0.0246  1007 VAL A N   
7352  C CA  . VAL A 1009 ? 0.3681 0.3186 0.2744 0.0216  0.0134  0.0267  1007 VAL A CA  
7353  C C   . VAL A 1009 ? 0.3806 0.3256 0.2901 0.0214  0.0125  0.0216  1007 VAL A C   
7354  O O   . VAL A 1009 ? 0.3607 0.3013 0.2727 0.0204  0.0110  0.0219  1007 VAL A O   
7355  C CB  . VAL A 1009 ? 0.3796 0.3303 0.2876 0.0204  0.0157  0.0296  1007 VAL A CB  
7356  C CG1 . VAL A 1009 ? 0.3454 0.2892 0.2582 0.0184  0.0153  0.0314  1007 VAL A CG1 
7357  C CG2 . VAL A 1009 ? 0.2823 0.2393 0.1875 0.0203  0.0166  0.0354  1007 VAL A CG2 
7358  N N   . GLN A 1010 ? 0.3339 0.2799 0.2440 0.0224  0.0133  0.0168  1008 GLN A N   
7359  C CA  . GLN A 1010 ? 0.3522 0.2947 0.2652 0.0223  0.0119  0.0120  1008 GLN A CA  
7360  C C   . GLN A 1010 ? 0.3625 0.3093 0.2733 0.0246  0.0111  0.0071  1008 GLN A C   
7361  O O   . GLN A 1010 ? 0.3579 0.3061 0.2700 0.0257  0.0117  0.0034  1008 GLN A O   
7362  C CB  . GLN A 1010 ? 0.3604 0.2991 0.2779 0.0212  0.0130  0.0109  1008 GLN A CB  
7363  C CG  . GLN A 1010 ? 0.3803 0.3158 0.3001 0.0191  0.0139  0.0152  1008 GLN A CG  
7364  C CD  . GLN A 1010 ? 0.3768 0.3144 0.2962 0.0191  0.0160  0.0179  1008 GLN A CD  
7365  O OE1 . GLN A 1010 ? 0.3525 0.2932 0.2715 0.0205  0.0171  0.0157  1008 GLN A OE1 
7366  N NE2 . GLN A 1010 ? 0.3515 0.2878 0.2717 0.0175  0.0166  0.0222  1008 GLN A NE2 
7367  N N   . PRO A 1011 ? 0.3545 0.3038 0.2622 0.0255  0.0094  0.0068  1009 PRO A N   
7368  C CA  . PRO A 1011 ? 0.3506 0.3041 0.2565 0.0276  0.0081  0.0013  1009 PRO A CA  
7369  C C   . PRO A 1011 ? 0.3375 0.2868 0.2486 0.0273  0.0071  -0.0039 1009 PRO A C   
7370  O O   . PRO A 1011 ? 0.3470 0.2908 0.2621 0.0253  0.0065  -0.0031 1009 PRO A O   
7371  C CB  . PRO A 1011 ? 0.3337 0.2883 0.2371 0.0278  0.0059  0.0025  1009 PRO A CB  
7372  C CG  . PRO A 1011 ? 0.3535 0.3071 0.2560 0.0266  0.0064  0.0093  1009 PRO A CG  
7373  C CD  . PRO A 1011 ? 0.3386 0.2868 0.2451 0.0247  0.0082  0.0111  1009 PRO A CD  
7374  N N   . PHE A 1012 ? 0.3284 0.2808 0.2402 0.0292  0.0070  -0.0092 1010 PHE A N   
7375  C CA  . PHE A 1012 ? 0.3384 0.2863 0.2564 0.0287  0.0064  -0.0131 1010 PHE A CA  
7376  C C   . PHE A 1012 ? 0.3411 0.2893 0.2616 0.0297  0.0036  -0.0193 1010 PHE A C   
7377  O O   . PHE A 1012 ? 0.3536 0.3077 0.2711 0.0322  0.0028  -0.0236 1010 PHE A O   
7378  C CB  . PHE A 1012 ? 0.3284 0.2785 0.2476 0.0300  0.0082  -0.0144 1010 PHE A CB  
7379  C CG  . PHE A 1012 ? 0.3674 0.3123 0.2940 0.0294  0.0072  -0.0175 1010 PHE A CG  
7380  C CD1 . PHE A 1012 ? 0.3560 0.2948 0.2867 0.0267  0.0076  -0.0135 1010 PHE A CD1 
7381  C CD2 . PHE A 1012 ? 0.4145 0.3608 0.3444 0.0317  0.0056  -0.0244 1010 PHE A CD2 
7382  C CE1 . PHE A 1012 ? 0.3769 0.3112 0.3147 0.0259  0.0065  -0.0153 1010 PHE A CE1 
7383  C CE2 . PHE A 1012 ? 0.3846 0.3256 0.3226 0.0310  0.0042  -0.0267 1010 PHE A CE2 
7384  C CZ  . PHE A 1012 ? 0.3595 0.2946 0.3013 0.0280  0.0047  -0.0217 1010 PHE A CZ  
7385  N N   . GLY A 1013 ? 0.3524 0.2948 0.2788 0.0277  0.0020  -0.0200 1011 GLY A N   
7386  C CA  . GLY A 1013 ? 0.3669 0.3088 0.2970 0.0282  -0.0009 -0.0257 1011 GLY A CA  
7387  C C   . GLY A 1013 ? 0.3436 0.2805 0.2785 0.0252  -0.0023 -0.0238 1011 GLY A C   
7388  O O   . GLY A 1013 ? 0.3481 0.2840 0.2808 0.0236  -0.0013 -0.0190 1011 GLY A O   
7389  N N   . GLY A 1014 ? 0.3907 0.3249 0.3324 0.0245  -0.0047 -0.0276 1012 GLY A N   
7390  C CA  . GLY A 1014 ? 0.4124 0.3427 0.3596 0.0213  -0.0059 -0.0254 1012 GLY A CA  
7391  C C   . GLY A 1014 ? 0.4180 0.3493 0.3672 0.0211  -0.0088 -0.0291 1012 GLY A C   
7392  O O   . GLY A 1014 ? 0.4347 0.3702 0.3797 0.0234  -0.0098 -0.0326 1012 GLY A O   
7393  N N   . ARG A 1015 ? 0.3765 0.3049 0.3328 0.0182  -0.0104 -0.0281 1013 ARG A N   
7394  C CA  A ARG A 1015 ? 0.4214 0.3506 0.3810 0.0172  -0.0132 -0.0309 1013 ARG A CA  
7395  C CA  B ARG A 1015 ? 0.4214 0.3506 0.3809 0.0173  -0.0132 -0.0309 1013 ARG A CA  
7396  C C   . ARG A 1015 ? 0.3962 0.3217 0.3660 0.0152  -0.0158 -0.0328 1013 ARG A C   
7397  O O   . ARG A 1015 ? 0.3774 0.2995 0.3514 0.0146  -0.0155 -0.0315 1013 ARG A O   
7398  C CB  A ARG A 1015 ? 0.4290 0.3595 0.3871 0.0151  -0.0125 -0.0266 1013 ARG A CB  
7399  C CB  B ARG A 1015 ? 0.4290 0.3596 0.3869 0.0152  -0.0125 -0.0267 1013 ARG A CB  
7400  C CG  A ARG A 1015 ? 0.4143 0.3426 0.3760 0.0118  -0.0109 -0.0210 1013 ARG A CG  
7401  C CG  B ARG A 1015 ? 0.4162 0.3448 0.3760 0.0124  -0.0104 -0.0208 1013 ARG A CG  
7402  C CD  A ARG A 1015 ? 0.4288 0.3589 0.3941 0.0089  -0.0118 -0.0190 1013 ARG A CD  
7403  C CD  B ARG A 1015 ? 0.4290 0.3593 0.3920 0.0095  -0.0109 -0.0181 1013 ARG A CD  
7404  N NE  A ARG A 1015 ? 0.4278 0.3567 0.4017 0.0067  -0.0147 -0.0207 1013 ARG A NE  
7405  N NE  B ARG A 1015 ? 0.4403 0.3730 0.4041 0.0098  -0.0133 -0.0216 1013 ARG A NE  
7406  C CZ  A ARG A 1015 ? 0.4313 0.3576 0.4124 0.0040  -0.0152 -0.0181 1013 ARG A CZ  
7407  C CZ  B ARG A 1015 ? 0.4460 0.3785 0.4171 0.0079  -0.0160 -0.0235 1013 ARG A CZ  
7408  N NH1 A ARG A 1015 ? 0.3536 0.2786 0.3340 0.0032  -0.0129 -0.0139 1013 ARG A NH1 
7409  N NH1 B ARG A 1015 ? 0.4397 0.3693 0.4183 0.0053  -0.0167 -0.0220 1013 ARG A NH1 
7410  N NH2 A ARG A 1015 ? 0.4377 0.3630 0.4273 0.0018  -0.0182 -0.0195 1013 ARG A NH2 
7411  N NH2 B ARG A 1015 ? 0.4187 0.3538 0.3899 0.0084  -0.0181 -0.0269 1013 ARG A NH2 
7412  N N   . GLY A 1016 ? 0.4220 0.3481 0.3964 0.0140  -0.0188 -0.0354 1014 GLY A N   
7413  C CA  . GLY A 1016 ? 0.3818 0.3042 0.3671 0.0116  -0.0217 -0.0365 1014 GLY A CA  
7414  C C   . GLY A 1016 ? 0.4151 0.3350 0.4043 0.0141  -0.0235 -0.0421 1014 GLY A C   
7415  O O   . GLY A 1016 ? 0.4262 0.3490 0.4112 0.0177  -0.0241 -0.0482 1014 GLY A O   
7416  N N   . LEU A 1017 ? 0.3779 0.2931 0.3756 0.0122  -0.0245 -0.0401 1015 LEU A N   
7417  C CA  . LEU A 1017 ? 0.4170 0.3292 0.4203 0.0145  -0.0265 -0.0455 1015 LEU A CA  
7418  C C   . LEU A 1017 ? 0.4111 0.3253 0.4068 0.0182  -0.0234 -0.0467 1015 LEU A C   
7419  O O   . LEU A 1017 ? 0.3922 0.3052 0.3917 0.0209  -0.0247 -0.0518 1015 LEU A O   
7420  C CB  . LEU A 1017 ? 0.3837 0.2901 0.3986 0.0113  -0.0284 -0.0417 1015 LEU A CB  
7421  C CG  . LEU A 1017 ? 0.4625 0.3668 0.4877 0.0072  -0.0321 -0.0402 1015 LEU A CG  
7422  C CD1 . LEU A 1017 ? 0.4466 0.3458 0.4824 0.0039  -0.0335 -0.0346 1015 LEU A CD1 
7423  C CD2 . LEU A 1017 ? 0.4510 0.3549 0.4817 0.0092  -0.0364 -0.0491 1015 LEU A CD2 
7424  N N   . SER A 1018 ? 0.3862 0.3037 0.3719 0.0185  -0.0196 -0.0423 1016 SER A N   
7425  C CA  . SER A 1018 ? 0.3702 0.2898 0.3492 0.0214  -0.0165 -0.0421 1016 SER A CA  
7426  C C   . SER A 1018 ? 0.4007 0.3265 0.3713 0.0252  -0.0159 -0.0471 1016 SER A C   
7427  O O   . SER A 1018 ? 0.4003 0.3291 0.3664 0.0279  -0.0138 -0.0483 1016 SER A O   
7428  C CB  . SER A 1018 ? 0.3642 0.2838 0.3380 0.0194  -0.0129 -0.0341 1016 SER A CB  
7429  O OG  . SER A 1018 ? 0.4171 0.3322 0.3981 0.0163  -0.0131 -0.0295 1016 SER A OG  
7430  N N   . GLY A 1019 ? 0.4120 0.3408 0.3804 0.0254  -0.0175 -0.0497 1017 GLY A N   
7431  C CA  . GLY A 1019 ? 0.4358 0.3715 0.3959 0.0290  -0.0170 -0.0539 1017 GLY A CA  
7432  C C   . GLY A 1019 ? 0.4107 0.3496 0.3674 0.0286  -0.0185 -0.0546 1017 GLY A C   
7433  O O   . GLY A 1019 ? 0.3983 0.3345 0.3576 0.0256  -0.0192 -0.0510 1017 GLY A O   
7434  N N   . THR A 1020 ? 0.3748 0.3204 0.3254 0.0319  -0.0190 -0.0593 1018 THR A N   
7435  C CA  . THR A 1020 ? 0.3992 0.3494 0.3451 0.0324  -0.0202 -0.0601 1018 THR A CA  
7436  C C   . THR A 1020 ? 0.3994 0.3528 0.3361 0.0325  -0.0173 -0.0535 1018 THR A C   
7437  O O   . THR A 1020 ? 0.4211 0.3763 0.3550 0.0319  -0.0182 -0.0518 1018 THR A O   
7438  C CB  . THR A 1020 ? 0.4020 0.3591 0.3459 0.0361  -0.0225 -0.0686 1018 THR A CB  
7439  O OG1 . THR A 1020 ? 0.3545 0.3172 0.2919 0.0390  -0.0199 -0.0690 1018 THR A OG1 
7440  C CG2 . THR A 1020 ? 0.4210 0.3747 0.3754 0.0362  -0.0261 -0.0762 1018 THR A CG2 
7441  N N   . GLY A 1021 ? 0.3738 0.3279 0.3061 0.0332  -0.0142 -0.0499 1019 GLY A N   
7442  C CA  . GLY A 1021 ? 0.3365 0.2952 0.2602 0.0341  -0.0120 -0.0448 1019 GLY A CA  
7443  C C   . GLY A 1021 ? 0.4006 0.3683 0.3182 0.0373  -0.0131 -0.0491 1019 GLY A C   
7444  O O   . GLY A 1021 ? 0.3736 0.3441 0.2937 0.0390  -0.0156 -0.0567 1019 GLY A O   
7445  N N   . PRO A 1022 ? 0.3625 0.3354 0.2721 0.0381  -0.0115 -0.0442 1020 PRO A N   
7446  C CA  . PRO A 1022 ? 0.3524 0.3223 0.2594 0.0363  -0.0090 -0.0356 1020 PRO A CA  
7447  C C   . PRO A 1022 ? 0.3783 0.3469 0.2856 0.0362  -0.0059 -0.0333 1020 PRO A C   
7448  O O   . PRO A 1022 ? 0.3714 0.3427 0.2798 0.0380  -0.0056 -0.0382 1020 PRO A O   
7449  C CB  . PRO A 1022 ? 0.3551 0.3325 0.2544 0.0378  -0.0092 -0.0324 1020 PRO A CB  
7450  C CG  . PRO A 1022 ? 0.3877 0.3743 0.2836 0.0409  -0.0102 -0.0390 1020 PRO A CG  
7451  C CD  . PRO A 1022 ? 0.3814 0.3644 0.2844 0.0410  -0.0126 -0.0470 1020 PRO A CD  
7452  N N   . LYS A 1023 ? 0.3463 0.3108 0.2531 0.0342  -0.0039 -0.0263 1021 LYS A N   
7453  C CA  . LYS A 1023 ? 0.3610 0.3234 0.2687 0.0336  -0.0011 -0.0235 1021 LYS A CA  
7454  C C   . LYS A 1023 ? 0.3588 0.3295 0.2609 0.0359  0.0007  -0.0232 1021 LYS A C   
7455  O O   . LYS A 1023 ? 0.3371 0.3137 0.2332 0.0366  0.0009  -0.0199 1021 LYS A O   
7456  C CB  . LYS A 1023 ? 0.3712 0.3285 0.2792 0.0311  0.0003  -0.0162 1021 LYS A CB  
7457  C CG  . LYS A 1023 ? 0.3414 0.2913 0.2557 0.0286  -0.0005 -0.0160 1021 LYS A CG  
7458  C CD  . LYS A 1023 ? 0.3501 0.2968 0.2639 0.0267  0.0009  -0.0095 1021 LYS A CD  
7459  C CE  . LYS A 1023 ? 0.3504 0.2912 0.2700 0.0241  0.0007  -0.0088 1021 LYS A CE  
7460  N NZ  . LYS A 1023 ? 0.3569 0.2950 0.2802 0.0233  0.0021  -0.0093 1021 LYS A NZ  
7461  N N   . ALA A 1024 ? 0.3235 0.2949 0.2278 0.0368  0.0021  -0.0262 1022 ALA A N   
7462  C CA  . ALA A 1024 ? 0.3097 0.2894 0.2093 0.0387  0.0044  -0.0254 1022 ALA A CA  
7463  C C   . ALA A 1024 ? 0.3209 0.2995 0.2179 0.0367  0.0068  -0.0165 1022 ALA A C   
7464  O O   . ALA A 1024 ? 0.3905 0.3609 0.2910 0.0342  0.0073  -0.0126 1022 ALA A O   
7465  C CB  . ALA A 1024 ? 0.3459 0.3260 0.2498 0.0403  0.0051  -0.0311 1022 ALA A CB  
7466  N N   . GLY A 1025 ? 0.3273 0.3147 0.2182 0.0377  0.0082  -0.0131 1023 GLY A N   
7467  C CA  . GLY A 1025 ? 0.3077 0.2942 0.1969 0.0357  0.0101  -0.0045 1023 GLY A CA  
7468  C C   . GLY A 1025 ? 0.3412 0.3215 0.2309 0.0336  0.0085  0.0007  1023 GLY A C   
7469  O O   . GLY A 1025 ? 0.3502 0.3257 0.2416 0.0315  0.0095  0.0066  1023 GLY A O   
7470  N N   . GLY A 1026 ? 0.3217 0.3024 0.2104 0.0343  0.0059  -0.0018 1024 GLY A N   
7471  C CA  . GLY A 1026 ? 0.3372 0.3132 0.2265 0.0328  0.0040  0.0022  1024 GLY A CA  
7472  C C   . GLY A 1026 ? 0.3283 0.3115 0.2126 0.0343  0.0021  0.0030  1024 GLY A C   
7473  O O   . GLY A 1026 ? 0.3288 0.3209 0.2090 0.0364  0.0021  -0.0003 1024 GLY A O   
7474  N N   . PRO A 1027 ? 0.3249 0.3048 0.2096 0.0334  0.0001  0.0072  1025 PRO A N   
7475  C CA  . PRO A 1027 ? 0.3436 0.3306 0.2235 0.0345  -0.0017 0.0104  1025 PRO A CA  
7476  C C   . PRO A 1027 ? 0.3348 0.3256 0.2133 0.0363  -0.0043 0.0042  1025 PRO A C   
7477  O O   . PRO A 1027 ? 0.3451 0.3430 0.2191 0.0374  -0.0060 0.0065  1025 PRO A O   
7478  C CB  . PRO A 1027 ? 0.3532 0.3340 0.2359 0.0328  -0.0031 0.0171  1025 PRO A CB  
7479  C CG  . PRO A 1027 ? 0.3631 0.3341 0.2518 0.0314  -0.0031 0.0137  1025 PRO A CG  
7480  C CD  . PRO A 1027 ? 0.3367 0.3070 0.2266 0.0313  -0.0004 0.0098  1025 PRO A CD  
7481  N N   . LEU A 1028 ? 0.3296 0.3157 0.2120 0.0364  -0.0050 -0.0029 1026 LEU A N   
7482  C CA  . LEU A 1028 ? 0.3495 0.3391 0.2315 0.0380  -0.0076 -0.0094 1026 LEU A CA  
7483  C C   . LEU A 1028 ? 0.3435 0.3405 0.2232 0.0402  -0.0071 -0.0163 1026 LEU A C   
7484  O O   . LEU A 1028 ? 0.3536 0.3552 0.2325 0.0418  -0.0094 -0.0222 1026 LEU A O   
7485  C CB  . LEU A 1028 ? 0.3618 0.3427 0.2503 0.0366  -0.0089 -0.0131 1026 LEU A CB  
7486  C CG  . LEU A 1028 ? 0.3702 0.3459 0.2610 0.0352  -0.0104 -0.0085 1026 LEU A CG  
7487  C CD1 . LEU A 1028 ? 0.4343 0.4028 0.3318 0.0336  -0.0110 -0.0122 1026 LEU A CD1 
7488  C CD2 . LEU A 1028 ? 0.4325 0.4141 0.3197 0.0367  -0.0132 -0.0075 1026 LEU A CD2 
7489  N N   . TYR A 1029 ? 0.3593 0.3582 0.2384 0.0404  -0.0043 -0.0160 1027 TYR A N   
7490  C CA  . TYR A 1029 ? 0.3362 0.3410 0.2151 0.0427  -0.0038 -0.0238 1027 TYR A CA  
7491  C C   . TYR A 1029 ? 0.3388 0.3569 0.2110 0.0454  -0.0048 -0.0265 1027 TYR A C   
7492  O O   . TYR A 1029 ? 0.3165 0.3385 0.1894 0.0475  -0.0068 -0.0351 1027 TYR A O   
7493  C CB  . TYR A 1029 ? 0.3238 0.3282 0.2035 0.0423  -0.0004 -0.0220 1027 TYR A CB  
7494  C CG  . TYR A 1029 ? 0.3670 0.3729 0.2500 0.0442  0.0001  -0.0304 1027 TYR A CG  
7495  C CD1 . TYR A 1029 ? 0.3573 0.3539 0.2478 0.0435  -0.0012 -0.0354 1027 TYR A CD1 
7496  C CD2 . TYR A 1029 ? 0.3339 0.3507 0.2131 0.0466  0.0018  -0.0329 1027 TYR A CD2 
7497  C CE1 . TYR A 1029 ? 0.3507 0.3477 0.2456 0.0452  -0.0012 -0.0427 1027 TYR A CE1 
7498  C CE2 . TYR A 1029 ? 0.3479 0.3658 0.2311 0.0487  0.0020  -0.0410 1027 TYR A CE2 
7499  C CZ  . TYR A 1029 ? 0.3805 0.3878 0.2718 0.0479  0.0004  -0.0459 1027 TYR A CZ  
7500  O OH  . TYR A 1029 ? 0.3919 0.3994 0.2885 0.0500  0.0001  -0.0537 1027 TYR A OH  
7501  N N   . LEU A 1030 ? 0.3471 0.3729 0.2131 0.0454  -0.0038 -0.0193 1028 LEU A N   
7502  C CA  . LEU A 1030 ? 0.3323 0.3727 0.1915 0.0480  -0.0046 -0.0213 1028 LEU A CA  
7503  C C   . LEU A 1030 ? 0.3510 0.3930 0.2096 0.0490  -0.0084 -0.0250 1028 LEU A C   
7504  O O   . LEU A 1030 ? 0.3942 0.4465 0.2495 0.0516  -0.0098 -0.0317 1028 LEU A O   
7505  C CB  . LEU A 1030 ? 0.3102 0.3589 0.1634 0.0473  -0.0030 -0.0113 1028 LEU A CB  
7506  C CG  . LEU A 1030 ? 0.3389 0.3884 0.1923 0.0464  0.0007  -0.0074 1028 LEU A CG  
7507  C CD1 . LEU A 1030 ? 0.3413 0.4009 0.1888 0.0456  0.0018  0.0026  1028 LEU A CD1 
7508  C CD2 . LEU A 1030 ? 0.3702 0.4262 0.2239 0.0490  0.0023  -0.0167 1028 LEU A CD2 
7509  N N   . GLY A 1031 ? 0.3671 0.3995 0.2289 0.0470  -0.0102 -0.0212 1029 GLY A N   
7510  C CA  . GLY A 1031 ? 0.3776 0.4116 0.2389 0.0478  -0.0138 -0.0239 1029 GLY A CA  
7511  C C   . GLY A 1031 ? 0.3873 0.4210 0.2522 0.0493  -0.0158 -0.0351 1029 GLY A C   
7512  O O   . GLY A 1031 ? 0.4125 0.4512 0.2760 0.0506  -0.0189 -0.0389 1029 GLY A O   
7513  N N   . ARG A 1032 ? 0.3411 0.3687 0.2114 0.0490  -0.0145 -0.0404 1030 ARG A N   
7514  C CA  . ARG A 1032 ? 0.3240 0.3511 0.1992 0.0504  -0.0167 -0.0512 1030 ARG A CA  
7515  C C   . ARG A 1032 ? 0.3899 0.4303 0.2609 0.0539  -0.0170 -0.0585 1030 ARG A C   
7516  O O   . ARG A 1032 ? 0.3624 0.4045 0.2367 0.0556  -0.0196 -0.0682 1030 ARG A O   
7517  C CB  . ARG A 1032 ? 0.3438 0.3597 0.2271 0.0488  -0.0154 -0.0534 1030 ARG A CB  
7518  C CG  . ARG A 1032 ? 0.3637 0.3758 0.2546 0.0492  -0.0183 -0.0632 1030 ARG A CG  
7519  C CD  . ARG A 1032 ? 0.3907 0.3971 0.2854 0.0474  -0.0213 -0.0629 1030 ARG A CD  
7520  N NE  . ARG A 1032 ? 0.3620 0.3624 0.2657 0.0468  -0.0238 -0.0704 1030 ARG A NE  
7521  C CZ  . ARG A 1032 ? 0.3976 0.4004 0.3041 0.0475  -0.0275 -0.0771 1030 ARG A CZ  
7522  N NH1 . ARG A 1032 ? 0.3759 0.3868 0.2765 0.0490  -0.0292 -0.0773 1030 ARG A NH1 
7523  N NH2 . ARG A 1032 ? 0.4229 0.4198 0.3388 0.0468  -0.0298 -0.0835 1030 ARG A NH2 
7524  N N   . LEU A 1033 ? 0.3612 0.4115 0.2250 0.0550  -0.0144 -0.0541 1031 LEU A N   
7525  C CA  . LEU A 1033 ? 0.3745 0.4390 0.2340 0.0584  -0.0140 -0.0608 1031 LEU A CA  
7526  C C   . LEU A 1033 ? 0.4069 0.4861 0.2577 0.0601  -0.0153 -0.0589 1031 LEU A C   
7527  O O   . LEU A 1033 ? 0.3608 0.4547 0.2060 0.0627  -0.0143 -0.0619 1031 LEU A O   
7528  C CB  . LEU A 1033 ? 0.3357 0.4027 0.1940 0.0585  -0.0099 -0.0577 1031 LEU A CB  
7529  C CG  . LEU A 1033 ? 0.3645 0.4175 0.2313 0.0568  -0.0086 -0.0587 1031 LEU A CG  
7530  C CD1 . LEU A 1033 ? 0.3257 0.3818 0.1907 0.0567  -0.0045 -0.0544 1031 LEU A CD1 
7531  C CD2 . LEU A 1033 ? 0.4136 0.4635 0.2876 0.0586  -0.0110 -0.0709 1031 LEU A CD2 
7532  N N   . VAL A 1034 ? 0.3702 0.4464 0.2199 0.0587  -0.0177 -0.0540 1032 VAL A N   
7533  C CA  . VAL A 1034 ? 0.3860 0.4754 0.2282 0.0602  -0.0198 -0.0523 1032 VAL A CA  
7534  C C   . VAL A 1034 ? 0.4351 0.5197 0.2809 0.0602  -0.0240 -0.0568 1032 VAL A C   
7535  O O   . VAL A 1034 ? 0.4190 0.4895 0.2721 0.0581  -0.0248 -0.0573 1032 VAL A O   
7536  C CB  . VAL A 1034 ? 0.4143 0.5070 0.2509 0.0585  -0.0184 -0.0386 1032 VAL A CB  
7537  C CG1 . VAL A 1034 ? 0.3904 0.4911 0.2229 0.0586  -0.0144 -0.0344 1032 VAL A CG1 
7538  C CG2 . VAL A 1034 ? 0.4035 0.4798 0.2455 0.0551  -0.0185 -0.0310 1032 VAL A CG2 
7539  N N   . THR A 1035 ? 0.4168 0.5143 0.2571 0.0624  -0.0266 -0.0599 1033 THR A N   
7540  C CA  . THR A 1035 ? 0.4462 0.5409 0.2900 0.0626  -0.0309 -0.0651 1033 THR A CA  
7541  C C   . THR A 1035 ? 0.4510 0.5359 0.2966 0.0599  -0.0320 -0.0558 1033 THR A C   
7542  O O   . THR A 1035 ? 0.4643 0.5400 0.3163 0.0588  -0.0343 -0.0592 1033 THR A O   
7543  C CB  . THR A 1035 ? 0.4238 0.5358 0.2610 0.0658  -0.0336 -0.0707 1033 THR A CB  
7544  O OG1 . THR A 1035 ? 0.5421 0.6637 0.3709 0.0657  -0.0332 -0.0601 1033 THR A OG1 
7545  C CG2 . THR A 1035 ? 0.4171 0.5402 0.2523 0.0689  -0.0323 -0.0801 1033 THR A CG2 
7546  N N   . THR A 1036 ? 0.4493 0.5361 0.2901 0.0588  -0.0304 -0.0443 1034 THR A N   
7547  C CA  . THR A 1036 ? 0.4752 0.5531 0.3183 0.0566  -0.0315 -0.0353 1034 THR A CA  
7548  C C   . THR A 1036 ? 0.4596 0.5286 0.3045 0.0542  -0.0279 -0.0267 1034 THR A C   
7549  O O   . THR A 1036 ? 0.4665 0.5426 0.3063 0.0542  -0.0256 -0.0207 1034 THR A O   
7550  C CB  . THR A 1036 ? 0.5363 0.6250 0.3729 0.0575  -0.0340 -0.0289 1034 THR A CB  
7551  O OG1 . THR A 1036 ? 0.4954 0.5926 0.3305 0.0598  -0.0375 -0.0375 1034 THR A OG1 
7552  C CG2 . THR A 1036 ? 0.5525 0.6315 0.3926 0.0555  -0.0355 -0.0200 1034 THR A CG2 
7553  N N   . ALA A 1037 ? 0.4572 0.5117 0.3095 0.0520  -0.0276 -0.0262 1035 ALA A N   
7554  C CA  . ALA A 1037 ? 0.4111 0.4569 0.2658 0.0498  -0.0243 -0.0198 1035 ALA A CA  
7555  C C   . ALA A 1037 ? 0.4293 0.4754 0.2816 0.0487  -0.0244 -0.0081 1035 ALA A C   
7556  O O   . ALA A 1037 ? 0.4317 0.4768 0.2848 0.0487  -0.0275 -0.0050 1035 ALA A O   
7557  C CB  . ALA A 1037 ? 0.4164 0.4478 0.2796 0.0478  -0.0240 -0.0227 1035 ALA A CB  
7558  N N   . PRO A 1038 ? 0.4279 0.4751 0.2781 0.0477  -0.0215 -0.0013 1036 PRO A N   
7559  C CA  . PRO A 1038 ? 0.4205 0.4656 0.2705 0.0462  -0.0220 0.0101  1036 PRO A CA  
7560  C C   . PRO A 1038 ? 0.4047 0.4347 0.2624 0.0441  -0.0219 0.0125  1036 PRO A C   
7561  O O   . PRO A 1038 ? 0.3614 0.3831 0.2239 0.0435  -0.0209 0.0062  1036 PRO A O   
7562  C CB  . PRO A 1038 ? 0.4332 0.4851 0.2791 0.0457  -0.0187 0.0153  1036 PRO A CB  
7563  C CG  . PRO A 1038 ? 0.4315 0.4803 0.2795 0.0460  -0.0158 0.0071  1036 PRO A CG  
7564  C CD  . PRO A 1038 ? 0.3686 0.4182 0.2176 0.0479  -0.0179 -0.0040 1036 PRO A CD  
7565  N N   . VAL A 1039 ? 0.4020 0.4291 0.2610 0.0429  -0.0231 0.0219  1037 VAL A N   
7566  C CA  . VAL A 1039 ? 0.4200 0.4341 0.2861 0.0411  -0.0231 0.0248  1037 VAL A CA  
7567  C C   . VAL A 1039 ? 0.3648 0.3756 0.2318 0.0393  -0.0195 0.0286  1037 VAL A C   
7568  O O   . VAL A 1039 ? 0.3761 0.3917 0.2404 0.0387  -0.0190 0.0367  1037 VAL A O   
7569  C CB  . VAL A 1039 ? 0.4241 0.4364 0.2925 0.0410  -0.0266 0.0324  1037 VAL A CB  
7570  C CG1 . VAL A 1039 ? 0.3960 0.3957 0.2722 0.0394  -0.0267 0.0344  1037 VAL A CG1 
7571  C CG2 . VAL A 1039 ? 0.4185 0.4349 0.2860 0.0428  -0.0302 0.0285  1037 VAL A CG2 
7572  N N   . PRO A 1040 ? 0.3596 0.3629 0.2303 0.0384  -0.0171 0.0235  1038 PRO A N   
7573  C CA  . PRO A 1040 ? 0.3940 0.3946 0.2656 0.0369  -0.0137 0.0267  1038 PRO A CA  
7574  C C   . PRO A 1040 ? 0.3839 0.3787 0.2592 0.0351  -0.0144 0.0356  1038 PRO A C   
7575  O O   . PRO A 1040 ? 0.3678 0.3574 0.2471 0.0351  -0.0173 0.0373  1038 PRO A O   
7576  C CB  . PRO A 1040 ? 0.3834 0.3760 0.2595 0.0363  -0.0120 0.0193  1038 PRO A CB  
7577  C CG  . PRO A 1040 ? 0.3733 0.3672 0.2496 0.0377  -0.0140 0.0115  1038 PRO A CG  
7578  C CD  . PRO A 1040 ? 0.4089 0.4065 0.2836 0.0386  -0.0175 0.0148  1038 PRO A CD  
7579  N N   . PRO A 1041 ? 0.3684 0.3638 0.2434 0.0337  -0.0120 0.0409  1039 PRO A N   
7580  C CA  . PRO A 1041 ? 0.3818 0.3702 0.2619 0.0318  -0.0128 0.0484  1039 PRO A CA  
7581  C C   . PRO A 1041 ? 0.3681 0.3449 0.2552 0.0311  -0.0133 0.0445  1039 PRO A C   
7582  O O   . PRO A 1041 ? 0.3871 0.3606 0.2751 0.0311  -0.0113 0.0376  1039 PRO A O   
7583  C CB  . PRO A 1041 ? 0.3625 0.3539 0.2412 0.0304  -0.0094 0.0524  1039 PRO A CB  
7584  C CG  . PRO A 1041 ? 0.4006 0.4036 0.2721 0.0319  -0.0076 0.0490  1039 PRO A CG  
7585  C CD  . PRO A 1041 ? 0.3760 0.3782 0.2469 0.0338  -0.0085 0.0394  1039 PRO A CD  
7586  N N   . GLN A 1042 ? 0.3872 0.3582 0.2794 0.0307  -0.0161 0.0489  1040 GLN A N   
7587  C CA  . GLN A 1042 ? 0.3579 0.3192 0.2572 0.0301  -0.0169 0.0460  1040 GLN A CA  
7588  C C   . GLN A 1042 ? 0.3866 0.3464 0.2866 0.0313  -0.0175 0.0376  1040 GLN A C   
7589  O O   . GLN A 1042 ? 0.3858 0.3392 0.2910 0.0307  -0.0174 0.0341  1040 GLN A O   
7590  C CB  . GLN A 1042 ? 0.4348 0.3910 0.3369 0.0283  -0.0139 0.0458  1040 GLN A CB  
7591  C CG  . GLN A 1042 ? 0.4389 0.3958 0.3418 0.0268  -0.0136 0.0542  1040 GLN A CG  
7592  C CD  . GLN A 1042 ? 0.4776 0.4285 0.3847 0.0250  -0.0113 0.0537  1040 GLN A CD  
7593  O OE1 . GLN A 1042 ? 0.4416 0.3950 0.3458 0.0244  -0.0080 0.0526  1040 GLN A OE1 
7594  N NE2 . GLN A 1042 ? 0.5307 0.4740 0.4447 0.0245  -0.0132 0.0542  1040 GLN A NE2 
7595  N N   . HIS A 1043 ? 0.3292 0.2955 0.2245 0.0328  -0.0182 0.0343  1041 HIS A N   
7596  C CA  . HIS A 1043 ? 0.3676 0.3332 0.2637 0.0335  -0.0186 0.0263  1041 HIS A CA  
7597  C C   . HIS A 1043 ? 0.3534 0.3178 0.2528 0.0347  -0.0224 0.0262  1041 HIS A C   
7598  O O   . HIS A 1043 ? 0.3573 0.3274 0.2536 0.0361  -0.0248 0.0268  1041 HIS A O   
7599  C CB  . HIS A 1043 ? 0.3540 0.3273 0.2442 0.0346  -0.0176 0.0220  1041 HIS A CB  
7600  C CG  . HIS A 1043 ? 0.3468 0.3194 0.2385 0.0351  -0.0181 0.0138  1041 HIS A CG  
7601  N ND1 . HIS A 1043 ? 0.3503 0.3190 0.2446 0.0340  -0.0159 0.0087  1041 HIS A ND1 
7602  C CD2 . HIS A 1043 ? 0.3498 0.3253 0.2414 0.0364  -0.0209 0.0101  1041 HIS A CD2 
7603  C CE1 . HIS A 1043 ? 0.3612 0.3303 0.2572 0.0344  -0.0172 0.0025  1041 HIS A CE1 
7604  N NE2 . HIS A 1043 ? 0.3764 0.3497 0.2708 0.0359  -0.0202 0.0030  1041 HIS A NE2 
7605  N N   . SER A 1044 ? 0.3483 0.3058 0.2542 0.0341  -0.0231 0.0254  1042 SER A N   
7606  C CA  . SER A 1044 ? 0.3414 0.2977 0.2516 0.0353  -0.0266 0.0242  1042 SER A CA  
7607  C C   . SER A 1044 ? 0.3771 0.3272 0.2939 0.0345  -0.0260 0.0206  1042 SER A C   
7608  O O   . SER A 1044 ? 0.3372 0.2839 0.2552 0.0330  -0.0233 0.0204  1042 SER A O   
7609  C CB  . SER A 1044 ? 0.3834 0.3399 0.2949 0.0362  -0.0299 0.0315  1042 SER A CB  
7610  O OG  . SER A 1044 ? 0.3732 0.3239 0.2893 0.0351  -0.0295 0.0356  1042 SER A OG  
7611  N N   . SER A 1045 ? 0.3443 0.2940 0.2654 0.0356  -0.0286 0.0177  1043 SER A N   
7612  C CA  . SER A 1045 ? 0.3307 0.2767 0.2582 0.0351  -0.0283 0.0138  1043 SER A CA  
7613  C C   . SER A 1045 ? 0.3050 0.2510 0.2378 0.0371  -0.0322 0.0133  1043 SER A C   
7614  O O   . SER A 1045 ? 0.3496 0.2995 0.2810 0.0384  -0.0345 0.0125  1043 SER A O   
7615  C CB  . SER A 1045 ? 0.3099 0.2575 0.2370 0.0339  -0.0260 0.0075  1043 SER A CB  
7616  O OG  . SER A 1045 ? 0.3610 0.3065 0.2939 0.0332  -0.0254 0.0043  1043 SER A OG  
7617  N N   . VAL A 1046 ? 0.3495 0.2915 0.2889 0.0373  -0.0332 0.0134  1044 VAL A N   
7618  C CA  . VAL A 1046 ? 0.3476 0.2897 0.2932 0.0395  -0.0370 0.0119  1044 VAL A CA  
7619  C C   . VAL A 1046 ? 0.3280 0.2727 0.2768 0.0395  -0.0363 0.0048  1044 VAL A C   
7620  O O   . VAL A 1046 ? 0.3431 0.2889 0.2975 0.0414  -0.0392 0.0025  1044 VAL A O   
7621  C CB  . VAL A 1046 ? 0.3538 0.2907 0.3063 0.0403  -0.0391 0.0145  1044 VAL A CB  
7622  C CG1 . VAL A 1046 ? 0.4315 0.3662 0.3820 0.0401  -0.0404 0.0226  1044 VAL A CG1 
7623  C CG2 . VAL A 1046 ? 0.3434 0.2777 0.2985 0.0388  -0.0362 0.0113  1044 VAL A CG2 
7624  N N   . HIS A 1047 ? 0.3377 0.2840 0.2838 0.0374  -0.0327 0.0015  1045 HIS A N   
7625  C CA  A HIS A 1047 ? 0.3514 0.3011 0.3008 0.0369  -0.0320 -0.0044 1045 HIS A CA  
7626  C CA  B HIS A 1047 ? 0.3513 0.3010 0.3005 0.0367  -0.0317 -0.0044 1045 HIS A CA  
7627  C C   . HIS A 1047 ? 0.3566 0.3109 0.3036 0.0371  -0.0330 -0.0067 1045 HIS A C   
7628  O O   . HIS A 1047 ? 0.3609 0.3161 0.3022 0.0369  -0.0328 -0.0050 1045 HIS A O   
7629  C CB  A HIS A 1047 ? 0.3412 0.2901 0.2902 0.0343  -0.0280 -0.0061 1045 HIS A CB  
7630  C CB  B HIS A 1047 ? 0.3387 0.2878 0.2864 0.0340  -0.0276 -0.0060 1045 HIS A CB  
7631  C CG  A HIS A 1047 ? 0.3314 0.2760 0.2824 0.0340  -0.0271 -0.0039 1045 HIS A CG  
7632  C CG  B HIS A 1047 ? 0.3614 0.3150 0.3109 0.0325  -0.0264 -0.0108 1045 HIS A CG  
7633  N ND1 A HIS A 1047 ? 0.3410 0.2852 0.2985 0.0352  -0.0285 -0.0059 1045 HIS A ND1 
7634  N ND1 B HIS A 1047 ? 0.3301 0.2870 0.2855 0.0327  -0.0268 -0.0144 1045 HIS A ND1 
7635  C CD2 A HIS A 1047 ? 0.3617 0.3026 0.3095 0.0329  -0.0252 -0.0001 1045 HIS A CD2 
7636  C CD2 B HIS A 1047 ? 0.3554 0.3109 0.3022 0.0307  -0.0249 -0.0123 1045 HIS A CD2 
7637  C CE1 A HIS A 1047 ? 0.3381 0.2782 0.2965 0.0347  -0.0277 -0.0036 1045 HIS A CE1 
7638  C CE1 B HIS A 1047 ? 0.3425 0.3036 0.2985 0.0308  -0.0255 -0.0173 1045 HIS A CE1 
7639  N NE2 A HIS A 1047 ? 0.3189 0.2569 0.2714 0.0331  -0.0256 0.0002  1045 HIS A NE2 
7640  N NE2 B HIS A 1047 ? 0.2688 0.2285 0.2200 0.0295  -0.0246 -0.0161 1045 HIS A NE2 
7641  N N   . THR A 1048 ? 0.3444 0.3025 0.2962 0.0377  -0.0343 -0.0109 1046 THR A N   
7642  C CA  . THR A 1048 ? 0.3196 0.2824 0.2705 0.0378  -0.0356 -0.0137 1046 THR A CA  
7643  C C   . THR A 1048 ? 0.3687 0.3349 0.3227 0.0355  -0.0334 -0.0182 1046 THR A C   
7644  O O   . THR A 1048 ? 0.3651 0.3328 0.3243 0.0354  -0.0328 -0.0203 1046 THR A O   
7645  C CB  . THR A 1048 ? 0.3532 0.3185 0.3075 0.0407  -0.0397 -0.0141 1046 THR A CB  
7646  O OG1 . THR A 1048 ? 0.3460 0.3078 0.2987 0.0425  -0.0419 -0.0089 1046 THR A OG1 
7647  C CG2 . THR A 1048 ? 0.3382 0.3084 0.2905 0.0408  -0.0413 -0.0164 1046 THR A CG2 
7648  N N   . ASP A 1049 ? 0.3701 0.3380 0.3214 0.0337  -0.0324 -0.0197 1047 ASP A N   
7649  C CA  . ASP A 1049 ? 0.3437 0.3149 0.2986 0.0312  -0.0306 -0.0231 1047 ASP A CA  
7650  C C   . ASP A 1049 ? 0.2980 0.2749 0.2587 0.0321  -0.0327 -0.0263 1047 ASP A C   
7651  O O   . ASP A 1049 ? 0.3067 0.2857 0.2672 0.0340  -0.0357 -0.0271 1047 ASP A O   
7652  C CB  . ASP A 1049 ? 0.2996 0.2710 0.2515 0.0293  -0.0300 -0.0241 1047 ASP A CB  
7653  C CG  . ASP A 1049 ? 0.3126 0.2868 0.2689 0.0261  -0.0284 -0.0266 1047 ASP A CG  
7654  O OD1 . ASP A 1049 ? 0.3559 0.3352 0.3164 0.0258  -0.0300 -0.0293 1047 ASP A OD1 
7655  O OD2 . ASP A 1049 ? 0.3631 0.3348 0.3191 0.0239  -0.0257 -0.0254 1047 ASP A OD2 
7656  N N   . PRO A 1050 ? 0.3206 0.3010 0.2865 0.0310  -0.0313 -0.0282 1048 PRO A N   
7657  C CA  . PRO A 1050 ? 0.3146 0.3015 0.2863 0.0322  -0.0333 -0.0316 1048 PRO A CA  
7658  C C   . PRO A 1050 ? 0.3138 0.3061 0.2875 0.0304  -0.0339 -0.0340 1048 PRO A C   
7659  O O   . PRO A 1050 ? 0.3326 0.3301 0.3102 0.0319  -0.0363 -0.0365 1048 PRO A O   
7660  C CB  . PRO A 1050 ? 0.3470 0.3370 0.3230 0.0314  -0.0311 -0.0329 1048 PRO A CB  
7661  C CG  . PRO A 1050 ? 0.3651 0.3521 0.3381 0.0282  -0.0277 -0.0308 1048 PRO A CG  
7662  C CD  . PRO A 1050 ? 0.3463 0.3259 0.3129 0.0286  -0.0279 -0.0276 1048 PRO A CD  
7663  N N   . VAL A 1051 ? 0.3139 0.3051 0.2858 0.0272  -0.0321 -0.0335 1049 VAL A N   
7664  C CA  . VAL A 1051 ? 0.3170 0.3124 0.2914 0.0253  -0.0333 -0.0357 1049 VAL A CA  
7665  C C   . VAL A 1051 ? 0.2956 0.2896 0.2665 0.0275  -0.0364 -0.0363 1049 VAL A C   
7666  O O   . VAL A 1051 ? 0.3145 0.3132 0.2882 0.0277  -0.0388 -0.0389 1049 VAL A O   
7667  C CB  . VAL A 1051 ? 0.3193 0.3132 0.2939 0.0213  -0.0309 -0.0349 1049 VAL A CB  
7668  C CG1 . VAL A 1051 ? 0.3562 0.3537 0.3344 0.0191  -0.0326 -0.0372 1049 VAL A CG1 
7669  C CG2 . VAL A 1051 ? 0.3584 0.3552 0.3364 0.0190  -0.0279 -0.0338 1049 VAL A CG2 
7670  N N   . LEU A 1052 ? 0.2841 0.2724 0.2487 0.0291  -0.0365 -0.0339 1050 LEU A N   
7671  C CA  . LEU A 1052 ? 0.2824 0.2707 0.2431 0.0317  -0.0395 -0.0339 1050 LEU A CA  
7672  C C   . LEU A 1052 ? 0.3064 0.2984 0.2703 0.0346  -0.0425 -0.0345 1050 LEU A C   
7673  O O   . LEU A 1052 ? 0.3192 0.3151 0.2838 0.0357  -0.0455 -0.0364 1050 LEU A O   
7674  C CB  . LEU A 1052 ? 0.2815 0.2643 0.2352 0.0330  -0.0388 -0.0304 1050 LEU A CB  
7675  C CG  . LEU A 1052 ? 0.2978 0.2813 0.2463 0.0358  -0.0417 -0.0290 1050 LEU A CG  
7676  C CD1 . LEU A 1052 ? 0.2962 0.2804 0.2462 0.0389  -0.0444 -0.0267 1050 LEU A CD1 
7677  C CD2 . LEU A 1052 ? 0.2815 0.2695 0.2300 0.0354  -0.0438 -0.0329 1050 LEU A CD2 
7678  N N   . LEU A 1053 ? 0.3177 0.3084 0.2839 0.0360  -0.0420 -0.0331 1051 LEU A N   
7679  C CA  . LEU A 1053 ? 0.3437 0.3375 0.3141 0.0392  -0.0452 -0.0340 1051 LEU A CA  
7680  C C   . LEU A 1053 ? 0.3254 0.3268 0.3020 0.0384  -0.0461 -0.0383 1051 LEU A C   
7681  O O   . LEU A 1053 ? 0.3080 0.3131 0.2867 0.0407  -0.0495 -0.0396 1051 LEU A O   
7682  C CB  . LEU A 1053 ? 0.3200 0.3112 0.2933 0.0407  -0.0446 -0.0327 1051 LEU A CB  
7683  C CG  . LEU A 1053 ? 0.3151 0.2991 0.2838 0.0420  -0.0445 -0.0279 1051 LEU A CG  
7684  C CD1 . LEU A 1053 ? 0.3250 0.3065 0.2981 0.0432  -0.0440 -0.0277 1051 LEU A CD1 
7685  C CD2 . LEU A 1053 ? 0.2844 0.2675 0.2502 0.0447  -0.0483 -0.0251 1051 LEU A CD2 
7686  N N   . ASP A 1054 ? 0.3190 0.3235 0.2988 0.0351  -0.0433 -0.0401 1052 ASP A N   
7687  C CA  . ASP A 1054 ? 0.3508 0.3635 0.3368 0.0338  -0.0440 -0.0437 1052 ASP A CA  
7688  C C   . ASP A 1054 ? 0.3176 0.3319 0.3025 0.0330  -0.0463 -0.0450 1052 ASP A C   
7689  O O   . ASP A 1054 ? 0.3033 0.3238 0.2925 0.0338  -0.0488 -0.0477 1052 ASP A O   
7690  C CB  . ASP A 1054 ? 0.3112 0.3273 0.3007 0.0299  -0.0405 -0.0442 1052 ASP A CB  
7691  C CG  . ASP A 1054 ? 0.3773 0.3947 0.3692 0.0309  -0.0385 -0.0442 1052 ASP A CG  
7692  O OD1 . ASP A 1054 ? 0.3509 0.3679 0.3442 0.0347  -0.0405 -0.0450 1052 ASP A OD1 
7693  O OD2 . ASP A 1054 ? 0.4044 0.4232 0.3972 0.0278  -0.0353 -0.0435 1052 ASP A OD2 
7694  N N   . PHE A 1055 ? 0.2982 0.3076 0.2778 0.0315  -0.0456 -0.0437 1053 PHE A N   
7695  C CA  . PHE A 1055 ? 0.3090 0.3199 0.2873 0.0310  -0.0480 -0.0457 1053 PHE A CA  
7696  C C   . PHE A 1055 ? 0.3148 0.3270 0.2905 0.0349  -0.0518 -0.0458 1053 PHE A C   
7697  O O   . PHE A 1055 ? 0.3012 0.3184 0.2792 0.0352  -0.0547 -0.0486 1053 PHE A O   
7698  C CB  . PHE A 1055 ? 0.3168 0.3222 0.2901 0.0292  -0.0464 -0.0448 1053 PHE A CB  
7699  C CG  . PHE A 1055 ? 0.2851 0.2920 0.2573 0.0288  -0.0489 -0.0478 1053 PHE A CG  
7700  C CD1 . PHE A 1055 ? 0.3561 0.3676 0.3346 0.0263  -0.0502 -0.0511 1053 PHE A CD1 
7701  C CD2 . PHE A 1055 ? 0.3167 0.3209 0.2817 0.0309  -0.0501 -0.0473 1053 PHE A CD2 
7702  C CE1 . PHE A 1055 ? 0.3479 0.3608 0.3260 0.0261  -0.0530 -0.0545 1053 PHE A CE1 
7703  C CE2 . PHE A 1055 ? 0.3449 0.3514 0.3089 0.0308  -0.0526 -0.0509 1053 PHE A CE2 
7704  C CZ  . PHE A 1055 ? 0.3015 0.3120 0.2721 0.0285  -0.0542 -0.0548 1053 PHE A CZ  
7705  N N   . ALA A 1056 ? 0.3277 0.3357 0.2990 0.0378  -0.0521 -0.0424 1054 ALA A N   
7706  C CA  . ALA A 1056 ? 0.2777 0.2871 0.2466 0.0414  -0.0560 -0.0413 1054 ALA A CA  
7707  C C   . ALA A 1056 ? 0.3443 0.3593 0.3201 0.0433  -0.0587 -0.0433 1054 ALA A C   
7708  O O   . ALA A 1056 ? 0.3402 0.3592 0.3162 0.0452  -0.0623 -0.0443 1054 ALA A O   
7709  C CB  . ALA A 1056 ? 0.3029 0.3066 0.2667 0.0436  -0.0558 -0.0362 1054 ALA A CB  
7710  N N   . LYS A 1057 ? 0.3661 0.3822 0.3477 0.0430  -0.0570 -0.0442 1055 LYS A N   
7711  C CA  . LYS A 1057 ? 0.4056 0.4284 0.3947 0.0448  -0.0593 -0.0471 1055 LYS A CA  
7712  C C   . LYS A 1057 ? 0.3657 0.3956 0.3586 0.0425  -0.0600 -0.0510 1055 LYS A C   
7713  O O   . LYS A 1057 ? 0.4239 0.4593 0.4202 0.0444  -0.0634 -0.0530 1055 LYS A O   
7714  C CB  . LYS A 1057 ? 0.3931 0.4170 0.3877 0.0449  -0.0570 -0.0481 1055 LYS A CB  
7715  C CG  . LYS A 1057 ? 0.4200 0.4380 0.4136 0.0482  -0.0578 -0.0452 1055 LYS A CG  
7716  C CD  . LYS A 1057 ? 0.4043 0.4245 0.4043 0.0489  -0.0562 -0.0474 1055 LYS A CD  
7717  C CE  . LYS A 1057 ? 0.4105 0.4318 0.4100 0.0448  -0.0515 -0.0482 1055 LYS A CE  
7718  N NZ  . LYS A 1057 ? 0.4416 0.4646 0.4458 0.0458  -0.0499 -0.0500 1055 LYS A NZ  
7719  N N   . TRP A 1058 ? 0.3537 0.3836 0.3466 0.0383  -0.0571 -0.0519 1056 TRP A N   
7720  C CA  . TRP A 1058 ? 0.3482 0.3841 0.3452 0.0356  -0.0580 -0.0551 1056 TRP A CA  
7721  C C   . TRP A 1058 ? 0.4130 0.4492 0.4065 0.0370  -0.0618 -0.0562 1056 TRP A C   
7722  O O   . TRP A 1058 ? 0.4034 0.4461 0.4013 0.0372  -0.0646 -0.0591 1056 TRP A O   
7723  C CB  . TRP A 1058 ? 0.3769 0.4111 0.3745 0.0308  -0.0546 -0.0549 1056 TRP A CB  
7724  C CG  . TRP A 1058 ? 0.4122 0.4515 0.4148 0.0274  -0.0558 -0.0577 1056 TRP A CG  
7725  C CD1 . TRP A 1058 ? 0.4051 0.4526 0.4160 0.0249  -0.0555 -0.0594 1056 TRP A CD1 
7726  C CD2 . TRP A 1058 ? 0.4000 0.4372 0.4006 0.0260  -0.0576 -0.0593 1056 TRP A CD2 
7727  N NE1 . TRP A 1058 ? 0.4405 0.4903 0.4549 0.0218  -0.0571 -0.0614 1056 TRP A NE1 
7728  C CE2 . TRP A 1058 ? 0.4276 0.4710 0.4360 0.0226  -0.0586 -0.0618 1056 TRP A CE2 
7729  C CE3 . TRP A 1058 ? 0.3487 0.3801 0.3419 0.0274  -0.0586 -0.0591 1056 TRP A CE3 
7730  C CZ2 . TRP A 1058 ? 0.4189 0.4618 0.4285 0.0205  -0.0609 -0.0644 1056 TRP A CZ2 
7731  C CZ3 . TRP A 1058 ? 0.3955 0.4273 0.3895 0.0256  -0.0607 -0.0622 1056 TRP A CZ3 
7732  C CH2 . TRP A 1058 ? 0.3892 0.4262 0.3915 0.0223  -0.0620 -0.0650 1056 TRP A CH2 
7733  N N   . LEU A 1059 ? 0.3785 0.4087 0.3641 0.0379  -0.0619 -0.0540 1057 LEU A N   
7734  C CA  . LEU A 1059 ? 0.3748 0.4065 0.3562 0.0395  -0.0654 -0.0551 1057 LEU A CA  
7735  C C   . LEU A 1059 ? 0.3969 0.4330 0.3797 0.0434  -0.0694 -0.0549 1057 LEU A C   
7736  O O   . LEU A 1059 ? 0.4313 0.4729 0.4154 0.0440  -0.0727 -0.0577 1057 LEU A O   
7737  C CB  . LEU A 1059 ? 0.3233 0.3491 0.2957 0.0404  -0.0645 -0.0523 1057 LEU A CB  
7738  C CG  . LEU A 1059 ? 0.3753 0.3970 0.3452 0.0372  -0.0617 -0.0532 1057 LEU A CG  
7739  C CD1 . LEU A 1059 ? 0.3529 0.3697 0.3142 0.0388  -0.0606 -0.0499 1057 LEU A CD1 
7740  C CD2 . LEU A 1059 ? 0.3467 0.3724 0.3189 0.0355  -0.0639 -0.0582 1057 LEU A CD2 
7741  N N   . ASP A 1060 ? 0.3739 0.4078 0.3572 0.0461  -0.0693 -0.0518 1058 ASP A N   
7742  C CA  . ASP A 1060 ? 0.4500 0.4877 0.4361 0.0499  -0.0734 -0.0513 1058 ASP A CA  
7743  C C   . ASP A 1060 ? 0.4447 0.4902 0.4396 0.0496  -0.0748 -0.0557 1058 ASP A C   
7744  O O   . ASP A 1060 ? 0.4336 0.4844 0.4306 0.0518  -0.0788 -0.0571 1058 ASP A O   
7745  C CB  . ASP A 1060 ? 0.4926 0.5254 0.4790 0.0526  -0.0731 -0.0474 1058 ASP A CB  
7746  C CG  . ASP A 1060 ? 0.4599 0.4882 0.4389 0.0548  -0.0748 -0.0422 1058 ASP A CG  
7747  O OD1 . ASP A 1060 ? 0.5114 0.5429 0.4863 0.0559  -0.0779 -0.0418 1058 ASP A OD1 
7748  O OD2 . ASP A 1060 ? 0.5002 0.5225 0.4775 0.0554  -0.0732 -0.0384 1058 ASP A OD2 
7749  N N   . GLY A 1061 ? 0.4562 0.5035 0.4567 0.0468  -0.0714 -0.0577 1059 GLY A N   
7750  C CA  . GLY A 1061 ? 0.4138 0.4699 0.4227 0.0459  -0.0723 -0.0618 1059 GLY A CA  
7751  C C   . GLY A 1061 ? 0.5217 0.5823 0.5313 0.0437  -0.0744 -0.0647 1059 GLY A C   
7752  O O   . GLY A 1061 ? 0.4434 0.5116 0.4588 0.0445  -0.0772 -0.0675 1059 GLY A O   
7753  N N   . LYS A 1062 ? 0.4542 0.5105 0.4586 0.0412  -0.0733 -0.0644 1060 LYS A N   
7754  C CA  . LYS A 1062 ? 0.4617 0.5216 0.4668 0.0393  -0.0757 -0.0677 1060 LYS A CA  
7755  C C   . LYS A 1062 ? 0.4737 0.5349 0.4738 0.0429  -0.0802 -0.0679 1060 LYS A C   
7756  O O   . LYS A 1062 ? 0.5063 0.5714 0.5070 0.0419  -0.0828 -0.0713 1060 LYS A O   
7757  C CB  . LYS A 1062 ? 0.4898 0.5447 0.4921 0.0355  -0.0733 -0.0680 1060 LYS A CB  
7758  C CG  . LYS A 1062 ? 0.4783 0.5331 0.4864 0.0311  -0.0694 -0.0678 1060 LYS A CG  
7759  C CD  . LYS A 1062 ? 0.5504 0.6131 0.5678 0.0279  -0.0707 -0.0710 1060 LYS A CD  
7760  C CE  . LYS A 1062 ? 0.5655 0.6294 0.5887 0.0233  -0.0669 -0.0697 1060 LYS A CE  
7761  N NZ  . LYS A 1062 ? 0.6475 0.7201 0.6805 0.0198  -0.0679 -0.0719 1060 LYS A NZ  
7762  N N   . GLY A 1063 ? 0.4766 0.5351 0.4719 0.0468  -0.0813 -0.0642 1061 GLY A N   
7763  C CA  . GLY A 1063 ? 0.4560 0.5165 0.4462 0.0501  -0.0856 -0.0633 1061 GLY A CA  
7764  C C   . GLY A 1063 ? 0.4634 0.5196 0.4438 0.0501  -0.0850 -0.0615 1061 GLY A C   
7765  O O   . GLY A 1063 ? 0.4466 0.5055 0.4217 0.0527  -0.0884 -0.0602 1061 GLY A O   
7766  N N   . ALA A 1064 ? 0.4348 0.4852 0.4127 0.0473  -0.0810 -0.0611 1062 ALA A N   
7767  C CA  . ALA A 1064 ? 0.3829 0.4300 0.3521 0.0473  -0.0801 -0.0600 1062 ALA A CA  
7768  C C   . ALA A 1064 ? 0.3932 0.4358 0.3565 0.0499  -0.0793 -0.0537 1062 ALA A C   
7769  O O   . ALA A 1064 ? 0.3827 0.4190 0.3434 0.0488  -0.0757 -0.0510 1062 ALA A O   
7770  C CB  . ALA A 1064 ? 0.4188 0.4616 0.3889 0.0433  -0.0765 -0.0623 1062 ALA A CB  
7771  N N   . ARG A 1065 ? 0.3877 0.4338 0.3495 0.0534  -0.0831 -0.0510 1063 ARG A N   
7772  C CA  . ARG A 1065 ? 0.4566 0.4987 0.4151 0.0559  -0.0832 -0.0443 1063 ARG A CA  
7773  C C   . ARG A 1065 ? 0.4154 0.4546 0.3646 0.0557  -0.0814 -0.0408 1063 ARG A C   
7774  O O   . ARG A 1065 ? 0.4165 0.4496 0.3638 0.0558  -0.0789 -0.0361 1063 ARG A O   
7775  C CB  . ARG A 1065 ? 0.4548 0.5019 0.4145 0.0596  -0.0883 -0.0418 1063 ARG A CB  
7776  N N   . ALA A 1066 ? 0.3785 0.4225 0.3219 0.0557  -0.0826 -0.0432 1064 ALA A N   
7777  C CA  . ALA A 1066 ? 0.3597 0.4025 0.2941 0.0557  -0.0809 -0.0404 1064 ALA A CA  
7778  C C   . ALA A 1066 ? 0.4298 0.4657 0.3643 0.0528  -0.0759 -0.0416 1064 ALA A C   
7779  O O   . ALA A 1066 ? 0.3691 0.4006 0.2991 0.0528  -0.0733 -0.0369 1064 ALA A O   
7780  C CB  . ALA A 1066 ? 0.4034 0.4542 0.3323 0.0564  -0.0834 -0.0444 1064 ALA A CB  
7781  N N   . GLU A 1067 ? 0.3856 0.4205 0.3258 0.0502  -0.0745 -0.0474 1065 GLU A N   
7782  C CA  . GLU A 1067 ? 0.3839 0.4124 0.3250 0.0472  -0.0701 -0.0483 1065 GLU A CA  
7783  C C   . GLU A 1067 ? 0.3467 0.3691 0.2905 0.0470  -0.0674 -0.0436 1065 GLU A C   
7784  O O   . GLU A 1067 ? 0.3362 0.3532 0.2772 0.0459  -0.0640 -0.0411 1065 GLU A O   
7785  C CB  . GLU A 1067 ? 0.3752 0.4047 0.3231 0.0443  -0.0699 -0.0547 1065 GLU A CB  
7786  C CG  . GLU A 1067 ? 0.3870 0.4209 0.3329 0.0440  -0.0720 -0.0604 1065 GLU A CG  
7787  C CD  . GLU A 1067 ? 0.4802 0.5222 0.4262 0.0461  -0.0768 -0.0629 1065 GLU A CD  
7788  O OE1 . GLU A 1067 ? 0.3987 0.4427 0.3471 0.0478  -0.0787 -0.0601 1065 GLU A OE1 
7789  O OE2 . GLU A 1067 ? 0.4402 0.4866 0.3841 0.0463  -0.0789 -0.0679 1065 GLU A OE2 
7790  N N   . ALA A 1068 ? 0.3633 0.3869 0.3131 0.0480  -0.0691 -0.0429 1066 ALA A N   
7791  C CA  . ALA A 1068 ? 0.3775 0.3961 0.3308 0.0482  -0.0670 -0.0395 1066 ALA A CA  
7792  C C   . ALA A 1068 ? 0.3919 0.4065 0.3395 0.0500  -0.0667 -0.0331 1066 ALA A C   
7793  O O   . ALA A 1068 ? 0.3584 0.3671 0.3060 0.0491  -0.0637 -0.0305 1066 ALA A O   
7794  C CB  . ALA A 1068 ? 0.3799 0.4019 0.3409 0.0497  -0.0695 -0.0407 1066 ALA A CB  
7795  N N   . GLU A 1069 ? 0.3717 0.3899 0.3146 0.0525  -0.0701 -0.0302 1067 GLU A N   
7796  C CA  . GLU A 1069 ? 0.4175 0.4330 0.3550 0.0539  -0.0700 -0.0232 1067 GLU A CA  
7797  C C   . GLU A 1069 ? 0.4201 0.4330 0.3509 0.0520  -0.0663 -0.0226 1067 GLU A C   
7798  O O   . GLU A 1069 ? 0.3744 0.3822 0.3034 0.0517  -0.0641 -0.0179 1067 GLU A O   
7799  C CB  . GLU A 1069 ? 0.4722 0.4937 0.4060 0.0567  -0.0746 -0.0199 1067 GLU A CB  
7800  C CG  . GLU A 1069 ? 0.4917 0.5125 0.4185 0.0575  -0.0745 -0.0125 1067 GLU A CG  
7801  C CD  . GLU A 1069 ? 0.5792 0.5947 0.5101 0.0589  -0.0758 -0.0056 1067 GLU A CD  
7802  O OE1 . GLU A 1069 ? 0.6575 0.6680 0.5960 0.0587  -0.0750 -0.0074 1067 GLU A OE1 
7803  O OE2 . GLU A 1069 ? 0.7162 0.7333 0.6432 0.0601  -0.0778 0.0016  1067 GLU A OE2 
7804  N N   . ALA A 1070 ? 0.3956 0.4122 0.3233 0.0509  -0.0657 -0.0277 1068 ALA A N   
7805  C CA  . ALA A 1070 ? 0.4156 0.4302 0.3382 0.0492  -0.0623 -0.0283 1068 ALA A CA  
7806  C C   . ALA A 1070 ? 0.3801 0.3872 0.3068 0.0467  -0.0582 -0.0288 1068 ALA A C   
7807  O O   . ALA A 1070 ? 0.3599 0.3631 0.2831 0.0459  -0.0552 -0.0261 1068 ALA A O   
7808  C CB  . ALA A 1070 ? 0.3715 0.3914 0.2919 0.0487  -0.0631 -0.0348 1068 ALA A CB  
7809  N N   . ALA A 1071 ? 0.3603 0.3663 0.2944 0.0455  -0.0581 -0.0321 1069 ALA A N   
7810  C CA  . ALA A 1071 ? 0.3567 0.3571 0.2949 0.0431  -0.0544 -0.0323 1069 ALA A CA  
7811  C C   . ALA A 1071 ? 0.3688 0.3644 0.3068 0.0440  -0.0532 -0.0266 1069 ALA A C   
7812  O O   . ALA A 1071 ? 0.3199 0.3106 0.2567 0.0426  -0.0499 -0.0249 1069 ALA A O   
7813  C CB  . ALA A 1071 ? 0.2855 0.2877 0.2318 0.0416  -0.0548 -0.0365 1069 ALA A CB  
7814  N N   . ARG A 1072 ? 0.3635 0.3601 0.3035 0.0465  -0.0562 -0.0237 1070 ARG A N   
7815  C CA  . ARG A 1072 ? 0.3725 0.3642 0.3136 0.0475  -0.0557 -0.0185 1070 ARG A CA  
7816  C C   . ARG A 1072 ? 0.3697 0.3593 0.3035 0.0476  -0.0546 -0.0133 1070 ARG A C   
7817  O O   . ARG A 1072 ? 0.3731 0.3575 0.3069 0.0468  -0.0523 -0.0101 1070 ARG A O   
7818  C CB  . ARG A 1072 ? 0.3432 0.3364 0.2890 0.0504  -0.0599 -0.0167 1070 ARG A CB  
7819  C CG  . ARG A 1072 ? 0.4212 0.4166 0.3751 0.0505  -0.0606 -0.0217 1070 ARG A CG  
7820  C CD  . ARG A 1072 ? 0.4428 0.4395 0.4023 0.0538  -0.0649 -0.0202 1070 ARG A CD  
7821  N NE  . ARG A 1072 ? 0.4739 0.4757 0.4310 0.0557  -0.0690 -0.0192 1070 ARG A NE  
7822  C CZ  . ARG A 1072 ? 0.4678 0.4756 0.4278 0.0561  -0.0710 -0.0237 1070 ARG A CZ  
7823  N NH1 . ARG A 1072 ? 0.4580 0.4678 0.4235 0.0545  -0.0693 -0.0293 1070 ARG A NH1 
7824  N NH2 . ARG A 1072 ? 0.4413 0.4540 0.3989 0.0581  -0.0750 -0.0223 1070 ARG A NH2 
7825  N N   . ASN A 1073 ? 0.3362 0.3308 0.2638 0.0485  -0.0563 -0.0125 1071 ASN A N   
7826  C CA  . ASN A 1073 ? 0.3854 0.3798 0.3058 0.0485  -0.0549 -0.0077 1071 ASN A CA  
7827  C C   . ASN A 1073 ? 0.3666 0.3578 0.2848 0.0461  -0.0504 -0.0100 1071 ASN A C   
7828  O O   . ASN A 1073 ? 0.3532 0.3412 0.2686 0.0455  -0.0481 -0.0057 1071 ASN A O   
7829  C CB  . ASN A 1073 ? 0.4174 0.4198 0.3315 0.0500  -0.0574 -0.0073 1071 ASN A CB  
7830  C CG  . ASN A 1073 ? 0.4586 0.4641 0.3740 0.0524  -0.0620 -0.0029 1071 ASN A CG  
7831  O OD1 . ASN A 1073 ? 0.4451 0.4460 0.3652 0.0531  -0.0632 0.0016  1071 ASN A OD1 
7832  N ND2 . ASN A 1073 ? 0.4851 0.4985 0.3968 0.0538  -0.0649 -0.0044 1071 ASN A ND2 
7833  N N   . ALA A 1074 ? 0.3673 0.3593 0.2876 0.0446  -0.0492 -0.0166 1072 ALA A N   
7834  C CA  . ALA A 1074 ? 0.3375 0.3258 0.2571 0.0423  -0.0453 -0.0187 1072 ALA A CA  
7835  C C   . ALA A 1074 ? 0.3309 0.3126 0.2548 0.0409  -0.0428 -0.0163 1072 ALA A C   
7836  O O   . ALA A 1074 ? 0.3441 0.3222 0.2658 0.0398  -0.0398 -0.0143 1072 ALA A O   
7837  C CB  . ALA A 1074 ? 0.3231 0.3131 0.2455 0.0407  -0.0452 -0.0257 1072 ALA A CB  
7838  N N   . GLY A 1075 ? 0.3492 0.3300 0.2794 0.0413  -0.0441 -0.0168 1073 GLY A N   
7839  C CA  . GLY A 1075 ? 0.3035 0.2793 0.2379 0.0403  -0.0420 -0.0153 1073 GLY A CA  
7840  C C   . GLY A 1075 ? 0.3734 0.3453 0.3052 0.0412  -0.0416 -0.0091 1073 GLY A C   
7841  O O   . GLY A 1075 ? 0.3641 0.3316 0.2964 0.0398  -0.0388 -0.0077 1073 GLY A O   
7842  N N   . SER A 1076 ? 0.3565 0.3305 0.2858 0.0433  -0.0446 -0.0050 1074 SER A N   
7843  C CA  . SER A 1076 ? 0.3736 0.3444 0.3009 0.0438  -0.0446 0.0018  1074 SER A CA  
7844  C C   . SER A 1076 ? 0.3593 0.3309 0.2795 0.0427  -0.0419 0.0040  1074 SER A C   
7845  O O   . SER A 1076 ? 0.4462 0.4138 0.3657 0.0418  -0.0399 0.0080  1074 SER A O   
7846  C CB  . SER A 1076 ? 0.3663 0.3396 0.2939 0.0463  -0.0491 0.0064  1074 SER A CB  
7847  O OG  . SER A 1076 ? 0.4781 0.4502 0.4133 0.0477  -0.0518 0.0046  1074 SER A OG  
7848  N N   . SER A 1077 ? 0.3473 0.3243 0.2622 0.0428  -0.0418 0.0012  1075 SER A N   
7849  C CA  A SER A 1077 ? 0.3831 0.3624 0.2913 0.0422  -0.0394 0.0024  1075 SER A CA  
7850  C CA  B SER A 1077 ? 0.3815 0.3606 0.2898 0.0422  -0.0394 0.0027  1075 SER A CA  
7851  C CA  C SER A 1077 ? 0.3838 0.3629 0.2920 0.0422  -0.0394 0.0026  1075 SER A CA  
7852  C C   . SER A 1077 ? 0.3642 0.3392 0.2732 0.0400  -0.0354 -0.0006 1075 SER A C   
7853  O O   . SER A 1077 ? 0.3720 0.3471 0.2769 0.0394  -0.0330 0.0016  1075 SER A O   
7854  C CB  A SER A 1077 ? 0.3546 0.3418 0.2578 0.0433  -0.0410 -0.0010 1075 SER A CB  
7855  C CB  B SER A 1077 ? 0.3551 0.3422 0.2579 0.0434  -0.0410 -0.0001 1075 SER A CB  
7856  C CB  C SER A 1077 ? 0.3549 0.3421 0.2577 0.0434  -0.0410 -0.0003 1075 SER A CB  
7857  O OG  A SER A 1077 ? 0.3490 0.3391 0.2464 0.0429  -0.0385 -0.0017 1075 SER A OG  
7858  O OG  B SER A 1077 ? 0.3389 0.3305 0.2395 0.0452  -0.0443 0.0050  1075 SER A OG  
7859  O OG  C SER A 1077 ? 0.3486 0.3368 0.2545 0.0431  -0.0417 -0.0076 1075 SER A OG  
7860  N N   . SER A 1078 ? 0.3414 0.3136 0.2557 0.0388  -0.0347 -0.0054 1076 SER A N   
7861  C CA  . SER A 1078 ? 0.3224 0.2908 0.2382 0.0367  -0.0312 -0.0077 1076 SER A CA  
7862  C C   . SER A 1078 ? 0.3821 0.3457 0.2980 0.0359  -0.0290 -0.0028 1076 SER A C   
7863  O O   . SER A 1078 ? 0.3411 0.3024 0.2597 0.0366  -0.0303 0.0008  1076 SER A O   
7864  C CB  . SER A 1078 ? 0.3475 0.3143 0.2697 0.0353  -0.0311 -0.0122 1076 SER A CB  
7865  O OG  . SER A 1078 ? 0.3238 0.2868 0.2478 0.0330  -0.0279 -0.0130 1076 SER A OG  
7866  N N   . ALA A 1079 ? 0.3527 0.3147 0.2663 0.0346  -0.0259 -0.0029 1077 ALA A N   
7867  C CA  . ALA A 1079 ? 0.3837 0.3413 0.2979 0.0337  -0.0237 0.0012  1077 ALA A CA  
7868  C C   . ALA A 1079 ? 0.3580 0.3116 0.2768 0.0316  -0.0214 -0.0015 1077 ALA A C   
7869  O O   . ALA A 1079 ? 0.3261 0.2761 0.2454 0.0306  -0.0192 0.0010  1077 ALA A O   
7870  C CB  . ALA A 1079 ? 0.3652 0.3247 0.2736 0.0337  -0.0218 0.0040  1077 ALA A CB  
7871  N N   . LEU A 1080 ? 0.3319 0.2864 0.2542 0.0309  -0.0220 -0.0062 1078 LEU A N   
7872  C CA  . LEU A 1080 ? 0.3176 0.2696 0.2449 0.0289  -0.0203 -0.0080 1078 LEU A CA  
7873  C C   . LEU A 1080 ? 0.3040 0.2532 0.2342 0.0290  -0.0201 -0.0052 1078 LEU A C   
7874  O O   . LEU A 1080 ? 0.3209 0.2707 0.2530 0.0307  -0.0225 -0.0041 1078 LEU A O   
7875  C CB  . LEU A 1080 ? 0.3224 0.2773 0.2537 0.0284  -0.0218 -0.0124 1078 LEU A CB  
7876  C CG  . LEU A 1080 ? 0.3504 0.3047 0.2873 0.0263  -0.0204 -0.0138 1078 LEU A CG  
7877  C CD1 . LEU A 1080 ? 0.3265 0.2790 0.2635 0.0239  -0.0177 -0.0142 1078 LEU A CD1 
7878  C CD2 . LEU A 1080 ? 0.3003 0.2587 0.2415 0.0261  -0.0223 -0.0172 1078 LEU A CD2 
7879  N N   . GLY A 1081 ? 0.2967 0.2430 0.2280 0.0274  -0.0175 -0.0042 1079 GLY A N   
7880  C CA  . GLY A 1081 ? 0.3571 0.3010 0.2916 0.0275  -0.0173 -0.0022 1079 GLY A CA  
7881  C C   . GLY A 1081 ? 0.3337 0.2745 0.2656 0.0280  -0.0168 0.0026  1079 GLY A C   
7882  O O   . GLY A 1081 ? 0.3209 0.2590 0.2558 0.0279  -0.0168 0.0043  1079 GLY A O   
7883  N N   . LEU A 1082 ? 0.3249 0.2667 0.2515 0.0284  -0.0166 0.0048  1080 LEU A N   
7884  C CA  . LEU A 1082 ? 0.3291 0.2690 0.2532 0.0284  -0.0156 0.0097  1080 LEU A CA  
7885  C C   . LEU A 1082 ? 0.3094 0.2462 0.2353 0.0265  -0.0128 0.0097  1080 LEU A C   
7886  O O   . LEU A 1082 ? 0.2963 0.2335 0.2226 0.0252  -0.0109 0.0065  1080 LEU A O   
7887  C CB  . LEU A 1082 ? 0.3320 0.2754 0.2498 0.0289  -0.0150 0.0110  1080 LEU A CB  
7888  C CG  . LEU A 1082 ? 0.3393 0.2828 0.2536 0.0287  -0.0136 0.0162  1080 LEU A CG  
7889  C CD1 . LEU A 1082 ? 0.3672 0.3166 0.2755 0.0299  -0.0139 0.0169  1080 LEU A CD1 
7890  C CD2 . LEU A 1082 ? 0.3834 0.3248 0.2979 0.0270  -0.0102 0.0155  1080 LEU A CD2 
7891  N N   . ASP A 1083 ? 0.3416 0.2755 0.2692 0.0263  -0.0127 0.0135  1081 ASP A N   
7892  C CA  . ASP A 1083 ? 0.3421 0.2734 0.2719 0.0247  -0.0104 0.0135  1081 ASP A CA  
7893  C C   . ASP A 1083 ? 0.3751 0.3041 0.3044 0.0244  -0.0102 0.0189  1081 ASP A C   
7894  O O   . ASP A 1083 ? 0.3761 0.3027 0.3092 0.0249  -0.0123 0.0211  1081 ASP A O   
7895  C CB  . ASP A 1083 ? 0.3806 0.3110 0.3160 0.0245  -0.0112 0.0104  1081 ASP A CB  
7896  C CG  . ASP A 1083 ? 0.4642 0.3934 0.4015 0.0227  -0.0088 0.0096  1081 ASP A CG  
7897  O OD1 . ASP A 1083 ? 0.4954 0.4238 0.4301 0.0216  -0.0066 0.0115  1081 ASP A OD1 
7898  O OD2 . ASP A 1083 ? 0.5625 0.4924 0.5043 0.0226  -0.0093 0.0068  1081 ASP A OD2 
7899  N N   . LEU A 1084 ? 0.3642 0.2941 0.2896 0.0236  -0.0077 0.0208  1082 LEU A N   
7900  C CA  . LEU A 1084 ? 0.3488 0.2781 0.2732 0.0232  -0.0074 0.0264  1082 LEU A CA  
7901  C C   . LEU A 1084 ? 0.3573 0.2849 0.2826 0.0215  -0.0046 0.0269  1082 LEU A C   
7902  O O   . LEU A 1084 ? 0.3148 0.2428 0.2393 0.0208  -0.0025 0.0234  1082 LEU A O   
7903  C CB  . LEU A 1084 ? 0.3774 0.3113 0.2959 0.0239  -0.0071 0.0291  1082 LEU A CB  
7904  C CG  . LEU A 1084 ? 0.4108 0.3474 0.3277 0.0256  -0.0100 0.0300  1082 LEU A CG  
7905  C CD1 . LEU A 1084 ? 0.3935 0.3364 0.3039 0.0262  -0.0092 0.0323  1082 LEU A CD1 
7906  C CD2 . LEU A 1084 ? 0.4315 0.3651 0.3530 0.0259  -0.0131 0.0343  1082 LEU A CD2 
7907  N N   . GLU A 1085 ? 0.3929 0.3184 0.3201 0.0207  -0.0048 0.0315  1083 GLU A N   
7908  C CA  . GLU A 1085 ? 0.3623 0.2872 0.2897 0.0192  -0.0021 0.0328  1083 GLU A CA  
7909  C C   . GLU A 1085 ? 0.4179 0.3463 0.3411 0.0190  -0.0009 0.0376  1083 GLU A C   
7910  O O   . GLU A 1085 ? 0.4170 0.3462 0.3403 0.0192  -0.0028 0.0426  1083 GLU A O   
7911  C CB  . GLU A 1085 ? 0.4267 0.3475 0.3600 0.0181  -0.0031 0.0339  1083 GLU A CB  
7912  C CG  . GLU A 1085 ? 0.4170 0.3375 0.3503 0.0165  -0.0003 0.0349  1083 GLU A CG  
7913  C CD  . GLU A 1085 ? 0.4935 0.4105 0.4328 0.0154  -0.0011 0.0350  1083 GLU A CD  
7914  O OE1 . GLU A 1085 ? 0.5043 0.4193 0.4478 0.0160  -0.0032 0.0318  1083 GLU A OE1 
7915  O OE2 . GLU A 1085 ? 0.5028 0.4196 0.4427 0.0141  0.0004  0.0379  1083 GLU A OE2 
7916  N N   . LEU A 1086 ? 0.3523 0.2834 0.2721 0.0188  0.0020  0.0362  1084 LEU A N   
7917  C CA  . LEU A 1086 ? 0.3863 0.3227 0.3017 0.0189  0.0035  0.0397  1084 LEU A CA  
7918  C C   . LEU A 1086 ? 0.3706 0.3064 0.2881 0.0172  0.0051  0.0442  1084 LEU A C   
7919  O O   . LEU A 1086 ? 0.3719 0.3043 0.2926 0.0162  0.0062  0.0424  1084 LEU A O   
7920  C CB  . LEU A 1086 ? 0.3476 0.2878 0.2589 0.0200  0.0056  0.0351  1084 LEU A CB  
7921  C CG  . LEU A 1086 ? 0.3774 0.3183 0.2873 0.0214  0.0040  0.0301  1084 LEU A CG  
7922  C CD1 . LEU A 1086 ? 0.3837 0.3281 0.2907 0.0224  0.0057  0.0253  1084 LEU A CD1 
7923  C CD2 . LEU A 1086 ? 0.3505 0.2944 0.2581 0.0225  0.0016  0.0331  1084 LEU A CD2 
7924  N N   . PRO A 1087 ? 0.3935 0.3332 0.3093 0.0168  0.0051  0.0502  1085 PRO A N   
7925  C CA  . PRO A 1087 ? 0.3993 0.3393 0.3173 0.0150  0.0066  0.0549  1085 PRO A CA  
7926  C C   . PRO A 1087 ? 0.4094 0.3519 0.3255 0.0150  0.0100  0.0517  1085 PRO A C   
7927  O O   . PRO A 1087 ? 0.4049 0.3519 0.3166 0.0165  0.0115  0.0481  1085 PRO A O   
7928  C CB  . PRO A 1087 ? 0.4052 0.3513 0.3208 0.0147  0.0060  0.0620  1085 PRO A CB  
7929  C CG  . PRO A 1087 ? 0.4483 0.3955 0.3616 0.0162  0.0035  0.0617  1085 PRO A CG  
7930  C CD  . PRO A 1087 ? 0.3896 0.3343 0.3017 0.0178  0.0035  0.0535  1085 PRO A CD  
7931  N N   . GLY A 1088 ? 0.3951 0.3348 0.3152 0.0133  0.0111  0.0529  1086 GLY A N   
7932  C CA  . GLY A 1088 ? 0.4013 0.3428 0.3207 0.0132  0.0140  0.0503  1086 GLY A CA  
7933  C C   . GLY A 1088 ? 0.3239 0.2628 0.2480 0.0112  0.0147  0.0532  1086 GLY A C   
7934  O O   . GLY A 1088 ? 0.3424 0.2795 0.2700 0.0097  0.0130  0.0581  1086 GLY A O   
7935  N N   . PRO A 1089 ? 0.3437 0.2824 0.2686 0.0110  0.0167  0.0502  1087 PRO A N   
7936  C CA  . PRO A 1089 ? 0.3301 0.2671 0.2594 0.0091  0.0174  0.0527  1087 PRO A CA  
7937  C C   . PRO A 1089 ? 0.3825 0.3130 0.3169 0.0080  0.0150  0.0516  1087 PRO A C   
7938  O O   . PRO A 1089 ? 0.3624 0.2899 0.2967 0.0089  0.0134  0.0480  1087 PRO A O   
7939  C CB  . PRO A 1089 ? 0.3605 0.2992 0.2891 0.0096  0.0199  0.0489  1087 PRO A CB  
7940  C CG  . PRO A 1089 ? 0.4137 0.3509 0.3400 0.0113  0.0193  0.0435  1087 PRO A CG  
7941  C CD  . PRO A 1089 ? 0.3731 0.3126 0.2958 0.0125  0.0181  0.0445  1087 PRO A CD  
7942  N N   . VAL A 1090 ? 0.3677 0.2966 0.3067 0.0061  0.0146  0.0546  1088 VAL A N   
7943  C CA  . VAL A 1090 ? 0.3297 0.2534 0.2739 0.0053  0.0126  0.0524  1088 VAL A CA  
7944  C C   . VAL A 1090 ? 0.3275 0.2507 0.2712 0.0057  0.0138  0.0470  1088 VAL A C   
7945  O O   . VAL A 1090 ? 0.3407 0.2667 0.2816 0.0062  0.0162  0.0459  1088 VAL A O   
7946  C CB  . VAL A 1090 ? 0.3434 0.2658 0.2933 0.0032  0.0117  0.0564  1088 VAL A CB  
7947  C CG1 . VAL A 1090 ? 0.3415 0.2644 0.2929 0.0024  0.0101  0.0628  1088 VAL A CG1 
7948  C CG2 . VAL A 1090 ? 0.3333 0.2591 0.2827 0.0023  0.0147  0.0572  1088 VAL A CG2 
7949  N N   . GLY A 1091 ? 0.3540 0.2740 0.3009 0.0056  0.0120  0.0438  1089 GLY A N   
7950  C CA  . GLY A 1091 ? 0.3487 0.2692 0.2956 0.0056  0.0129  0.0395  1089 GLY A CA  
7951  C C   . GLY A 1091 ? 0.3681 0.2896 0.3111 0.0069  0.0136  0.0363  1089 GLY A C   
7952  O O   . GLY A 1091 ? 0.3290 0.2516 0.2717 0.0068  0.0147  0.0340  1089 GLY A O   
7953  N N   . GLU A 1092 ? 0.3374 0.2588 0.2779 0.0081  0.0127  0.0366  1090 GLU A N   
7954  C CA  . GLU A 1092 ? 0.3536 0.2760 0.2909 0.0094  0.0130  0.0335  1090 GLU A CA  
7955  C C   . GLU A 1092 ? 0.3636 0.2850 0.3003 0.0104  0.0108  0.0332  1090 GLU A C   
7956  O O   . GLU A 1092 ? 0.3309 0.2517 0.2680 0.0105  0.0096  0.0366  1090 GLU A O   
7957  C CB  . GLU A 1092 ? 0.3750 0.3002 0.3085 0.0101  0.0151  0.0342  1090 GLU A CB  
7958  C CG  . GLU A 1092 ? 0.4059 0.3319 0.3375 0.0112  0.0155  0.0304  1090 GLU A CG  
7959  C CD  . GLU A 1092 ? 0.4544 0.3834 0.3836 0.0122  0.0174  0.0303  1090 GLU A CD  
7960  O OE1 . GLU A 1092 ? 0.4004 0.3321 0.3262 0.0134  0.0175  0.0311  1090 GLU A OE1 
7961  O OE2 . GLU A 1092 ? 0.4695 0.3986 0.4002 0.0118  0.0186  0.0293  1090 GLU A OE2 
7962  N N   . ARG A 1093 ? 0.3036 0.2250 0.2398 0.0111  0.0100  0.0295  1091 ARG A N   
7963  C CA  . ARG A 1093 ? 0.3406 0.2615 0.2760 0.0123  0.0079  0.0288  1091 ARG A CA  
7964  C C   . ARG A 1093 ? 0.3387 0.2616 0.2703 0.0134  0.0086  0.0266  1091 ARG A C   
7965  O O   . ARG A 1093 ? 0.3121 0.2356 0.2441 0.0130  0.0093  0.0236  1091 ARG A O   
7966  C CB  . ARG A 1093 ? 0.3855 0.3052 0.3248 0.0124  0.0058  0.0258  1091 ARG A CB  
7967  C CG  . ARG A 1093 ? 0.4882 0.4056 0.4322 0.0120  0.0040  0.0272  1091 ARG A CG  
7968  C CD  . ARG A 1093 ? 0.5863 0.5029 0.5339 0.0131  0.0012  0.0241  1091 ARG A CD  
7969  N NE  . ARG A 1093 ? 0.6425 0.5617 0.5906 0.0130  0.0018  0.0194  1091 ARG A NE  
7970  C CZ  . ARG A 1093 ? 0.6489 0.5695 0.6001 0.0121  0.0021  0.0171  1091 ARG A CZ  
7971  N NH1 . ARG A 1093 ? 0.6971 0.6160 0.6515 0.0114  0.0016  0.0185  1091 ARG A NH1 
7972  N NH2 . ARG A 1093 ? 0.6211 0.5456 0.5723 0.0117  0.0028  0.0136  1091 ARG A NH2 
7973  N N   . ASN A 1094 ? 0.3379 0.2623 0.2663 0.0145  0.0081  0.0282  1092 ASN A N   
7974  C CA  . ASN A 1094 ? 0.3197 0.2466 0.2445 0.0157  0.0085  0.0258  1092 ASN A CA  
7975  C C   . ASN A 1094 ? 0.3248 0.2519 0.2488 0.0169  0.0061  0.0247  1092 ASN A C   
7976  O O   . ASN A 1094 ? 0.3572 0.2848 0.2805 0.0175  0.0047  0.0278  1092 ASN A O   
7977  C CB  . ASN A 1094 ? 0.3083 0.2385 0.2295 0.0163  0.0102  0.0279  1092 ASN A CB  
7978  C CG  . ASN A 1094 ? 0.3245 0.2548 0.2469 0.0155  0.0124  0.0278  1092 ASN A CG  
7979  O OD1 . ASN A 1094 ? 0.3400 0.2700 0.2631 0.0155  0.0131  0.0245  1092 ASN A OD1 
7980  N ND2 . ASN A 1094 ? 0.3251 0.2557 0.2482 0.0146  0.0134  0.0318  1092 ASN A ND2 
7981  N N   . LEU A 1095 ? 0.3298 0.2570 0.2545 0.0171  0.0056  0.0206  1093 LEU A N   
7982  C CA  . LEU A 1095 ? 0.3336 0.2610 0.2587 0.0180  0.0032  0.0189  1093 LEU A CA  
7983  C C   . LEU A 1095 ? 0.3114 0.2414 0.2335 0.0191  0.0030  0.0161  1093 LEU A C   
7984  O O   . LEU A 1095 ? 0.3326 0.2632 0.2544 0.0187  0.0043  0.0139  1093 LEU A O   
7985  C CB  . LEU A 1095 ? 0.3098 0.2360 0.2390 0.0172  0.0024  0.0163  1093 LEU A CB  
7986  C CG  . LEU A 1095 ? 0.3594 0.2837 0.2921 0.0162  0.0027  0.0179  1093 LEU A CG  
7987  C CD1 . LEU A 1095 ? 0.4259 0.3510 0.3623 0.0155  0.0023  0.0145  1093 LEU A CD1 
7988  C CD2 . LEU A 1095 ? 0.3642 0.2868 0.2981 0.0170  0.0008  0.0210  1093 LEU A CD2 
7989  N N   . TYR A 1096 ? 0.3230 0.2545 0.2437 0.0204  0.0009  0.0160  1094 TYR A N   
7990  C CA  . TYR A 1096 ? 0.3272 0.2618 0.2449 0.0217  0.0001  0.0132  1094 TYR A CA  
7991  C C   . TYR A 1096 ? 0.2995 0.2342 0.2190 0.0222  -0.0024 0.0113  1094 TYR A C   
7992  O O   . TYR A 1096 ? 0.3403 0.2745 0.2604 0.0229  -0.0042 0.0138  1094 TYR A O   
7993  C CB  . TYR A 1096 ? 0.3149 0.2532 0.2278 0.0230  0.0002  0.0159  1094 TYR A CB  
7994  C CG  . TYR A 1096 ? 0.3462 0.2889 0.2557 0.0246  -0.0009 0.0129  1094 TYR A CG  
7995  C CD1 . TYR A 1096 ? 0.3205 0.2654 0.2288 0.0251  0.0002  0.0088  1094 TYR A CD1 
7996  C CD2 . TYR A 1096 ? 0.3689 0.3140 0.2766 0.0259  -0.0034 0.0140  1094 TYR A CD2 
7997  C CE1 . TYR A 1096 ? 0.3679 0.3172 0.2733 0.0268  -0.0011 0.0053  1094 TYR A CE1 
7998  C CE2 . TYR A 1096 ? 0.3898 0.3396 0.2942 0.0274  -0.0045 0.0109  1094 TYR A CE2 
7999  C CZ  . TYR A 1096 ? 0.3604 0.3125 0.2636 0.0279  -0.0033 0.0063  1094 TYR A CZ  
8000  O OH  . TYR A 1096 ? 0.3875 0.3446 0.2879 0.0296  -0.0048 0.0024  1094 TYR A OH  
8001  N N   . THR A 1097 ? 0.3409 0.2762 0.2618 0.0220  -0.0028 0.0070  1095 THR A N   
8002  C CA  . THR A 1097 ? 0.3450 0.2810 0.2684 0.0222  -0.0050 0.0049  1095 THR A CA  
8003  C C   . THR A 1097 ? 0.3124 0.2511 0.2349 0.0228  -0.0062 0.0010  1095 THR A C   
8004  O O   . THR A 1097 ? 0.3093 0.2484 0.2313 0.0224  -0.0051 -0.0011 1095 THR A O   
8005  C CB  . THR A 1097 ? 0.3397 0.2745 0.2680 0.0206  -0.0045 0.0036  1095 THR A CB  
8006  O OG1 . THR A 1097 ? 0.3902 0.3246 0.3196 0.0189  -0.0027 0.0021  1095 THR A OG1 
8007  C CG2 . THR A 1097 ? 0.3489 0.2814 0.2788 0.0202  -0.0039 0.0065  1095 THR A CG2 
8008  N N   . LEU A 1098 ? 0.3111 0.2517 0.2340 0.0239  -0.0086 -0.0002 1096 LEU A N   
8009  C CA  . LEU A 1098 ? 0.3086 0.2520 0.2311 0.0245  -0.0102 -0.0041 1096 LEU A CA  
8010  C C   . LEU A 1098 ? 0.3116 0.2553 0.2393 0.0232  -0.0111 -0.0067 1096 LEU A C   
8011  O O   . LEU A 1098 ? 0.3387 0.2827 0.2685 0.0236  -0.0123 -0.0060 1096 LEU A O   
8012  C CB  . LEU A 1098 ? 0.3186 0.2652 0.2373 0.0267  -0.0124 -0.0033 1096 LEU A CB  
8013  C CG  . LEU A 1098 ? 0.3511 0.2998 0.2643 0.0279  -0.0116 -0.0006 1096 LEU A CG  
8014  C CD1 . LEU A 1098 ? 0.2944 0.2476 0.2040 0.0299  -0.0142 0.0002  1096 LEU A CD1 
8015  C CD2 . LEU A 1098 ? 0.3157 0.2655 0.2274 0.0277  -0.0099 -0.0038 1096 LEU A CD2 
8016  N N   . HIS A 1099 ? 0.3270 0.2710 0.2573 0.0217  -0.0108 -0.0097 1097 HIS A N   
8017  C CA  . HIS A 1099 ? 0.3093 0.2546 0.2449 0.0200  -0.0115 -0.0118 1097 HIS A CA  
8018  C C   . HIS A 1099 ? 0.3236 0.2712 0.2602 0.0201  -0.0136 -0.0156 1097 HIS A C   
8019  O O   . HIS A 1099 ? 0.3495 0.2977 0.2827 0.0216  -0.0144 -0.0171 1097 HIS A O   
8020  C CB  . HIS A 1099 ? 0.3283 0.2719 0.2673 0.0173  -0.0094 -0.0111 1097 HIS A CB  
8021  C CG  . HIS A 1099 ? 0.3890 0.3307 0.3273 0.0170  -0.0074 -0.0078 1097 HIS A CG  
8022  N ND1 . HIS A 1099 ? 0.3826 0.3258 0.3240 0.0159  -0.0068 -0.0070 1097 HIS A ND1 
8023  C CD2 . HIS A 1099 ? 0.3655 0.3046 0.3005 0.0177  -0.0058 -0.0054 1097 HIS A CD2 
8024  C CE1 . HIS A 1099 ? 0.4154 0.3565 0.3557 0.0159  -0.0052 -0.0045 1097 HIS A CE1 
8025  N NE2 . HIS A 1099 ? 0.3500 0.2884 0.2864 0.0169  -0.0046 -0.0033 1097 HIS A NE2 
8026  N N   . ALA A 1100 ? 0.2720 0.2218 0.2137 0.0185  -0.0146 -0.0173 1098 ALA A N   
8027  C CA  . ALA A 1100 ? 0.3309 0.2825 0.2749 0.0181  -0.0167 -0.0210 1098 ALA A CA  
8028  C C   . ALA A 1100 ? 0.3634 0.3124 0.3092 0.0167  -0.0161 -0.0223 1098 ALA A C   
8029  O O   . ALA A 1100 ? 0.3833 0.3298 0.3303 0.0152  -0.0140 -0.0200 1098 ALA A O   
8030  C CB  . ALA A 1100 ? 0.3164 0.2714 0.2662 0.0162  -0.0178 -0.0221 1098 ALA A CB  
8031  N N   . ARG A 1101 ? 0.3130 0.2630 0.2594 0.0174  -0.0182 -0.0263 1099 ARG A N   
8032  C CA  . ARG A 1101 ? 0.3544 0.3018 0.3037 0.0165  -0.0184 -0.0284 1099 ARG A CA  
8033  C C   . ARG A 1101 ? 0.3656 0.3122 0.3232 0.0129  -0.0191 -0.0283 1099 ARG A C   
8034  O O   . ARG A 1101 ? 0.3754 0.3189 0.3365 0.0112  -0.0181 -0.0271 1099 ARG A O   
8035  C CB  . ARG A 1101 ? 0.3768 0.3260 0.3242 0.0188  -0.0208 -0.0335 1099 ARG A CB  
8036  C CG  . ARG A 1101 ? 0.3900 0.3403 0.3298 0.0219  -0.0197 -0.0335 1099 ARG A CG  
8037  C CD  . ARG A 1101 ? 0.4148 0.3684 0.3530 0.0242  -0.0221 -0.0391 1099 ARG A CD  
8038  N NE  . ARG A 1101 ? 0.4571 0.4088 0.3979 0.0245  -0.0221 -0.0427 1099 ARG A NE  
8039  C CZ  . ARG A 1101 ? 0.5046 0.4569 0.4409 0.0264  -0.0203 -0.0427 1099 ARG A CZ  
8040  N NH1 . ARG A 1101 ? 0.4247 0.3789 0.3539 0.0277  -0.0181 -0.0384 1099 ARG A NH1 
8041  N NH2 . ARG A 1101 ? 0.4246 0.3759 0.3641 0.0271  -0.0209 -0.0473 1099 ARG A NH2 
8042  N N   . GLY A 1102 ? 0.3196 0.2696 0.2810 0.0117  -0.0208 -0.0292 1100 GLY A N   
8043  C CA  . GLY A 1102 ? 0.3667 0.3173 0.3364 0.0079  -0.0217 -0.0287 1100 GLY A CA  
8044  C C   . GLY A 1102 ? 0.3760 0.3303 0.3496 0.0074  -0.0247 -0.0320 1100 GLY A C   
8045  O O   . GLY A 1102 ? 0.3434 0.3014 0.3141 0.0090  -0.0251 -0.0325 1100 GLY A O   
8046  N N   . ARG A 1103 ? 0.3247 0.2779 0.3055 0.0053  -0.0271 -0.0343 1101 ARG A N   
8047  C CA  . ARG A 1103 ? 0.3310 0.2874 0.3162 0.0047  -0.0303 -0.0379 1101 ARG A CA  
8048  C C   . ARG A 1103 ? 0.3339 0.2891 0.3168 0.0077  -0.0328 -0.0439 1101 ARG A C   
8049  O O   . ARG A 1103 ? 0.3577 0.3089 0.3432 0.0078  -0.0336 -0.0461 1101 ARG A O   
8050  C CB  . ARG A 1103 ? 0.4083 0.3651 0.4043 0.0001  -0.0318 -0.0366 1101 ARG A CB  
8051  C CG  . ARG A 1103 ? 0.3464 0.3077 0.3475 -0.0010 -0.0350 -0.0397 1101 ARG A CG  
8052  C CD  . ARG A 1103 ? 0.4148 0.3780 0.4268 -0.0062 -0.0362 -0.0368 1101 ARG A CD  
8053  N NE  . ARG A 1103 ? 0.4845 0.4515 0.4966 -0.0086 -0.0330 -0.0307 1101 ARG A NE  
8054  C CZ  . ARG A 1103 ? 0.4618 0.4359 0.4737 -0.0092 -0.0321 -0.0294 1101 ARG A CZ  
8055  N NH1 . ARG A 1103 ? 0.4013 0.3794 0.4133 -0.0078 -0.0342 -0.0331 1101 ARG A NH1 
8056  N NH2 . ARG A 1103 ? 0.4588 0.4368 0.4706 -0.0110 -0.0291 -0.0245 1101 ARG A NH2 
8057  N N   . ILE A 1104 ? 0.3172 0.2762 0.2954 0.0104  -0.0342 -0.0467 1102 ILE A N   
8058  C CA  . ILE A 1104 ? 0.3276 0.2874 0.3028 0.0135  -0.0366 -0.0526 1102 ILE A CA  
8059  C C   . ILE A 1104 ? 0.3384 0.3001 0.3214 0.0120  -0.0406 -0.0574 1102 ILE A C   
8060  O O   . ILE A 1104 ? 0.3307 0.2959 0.3171 0.0103  -0.0416 -0.0564 1102 ILE A O   
8061  C CB  . ILE A 1104 ? 0.3202 0.2838 0.2858 0.0172  -0.0361 -0.0525 1102 ILE A CB  
8062  C CG1 . ILE A 1104 ? 0.3302 0.2919 0.2895 0.0182  -0.0324 -0.0471 1102 ILE A CG1 
8063  C CG2 . ILE A 1104 ? 0.3270 0.2929 0.2886 0.0205  -0.0383 -0.0582 1102 ILE A CG2 
8064  C CD1 . ILE A 1104 ? 0.3490 0.3070 0.3059 0.0190  -0.0306 -0.0471 1102 ILE A CD1 
8065  N N   . LEU A 1105 ? 0.3217 0.2813 0.3081 0.0126  -0.0431 -0.0628 1103 LEU A N   
8066  C CA  . LEU A 1105 ? 0.3434 0.3047 0.3375 0.0116  -0.0475 -0.0684 1103 LEU A CA  
8067  C C   . LEU A 1105 ? 0.3552 0.3224 0.3429 0.0150  -0.0494 -0.0728 1103 LEU A C   
8068  O O   . LEU A 1105 ? 0.3301 0.2990 0.3097 0.0188  -0.0489 -0.0753 1103 LEU A O   
8069  C CB  . LEU A 1105 ? 0.3254 0.2822 0.3257 0.0116  -0.0497 -0.0735 1103 LEU A CB  
8070  C CG  . LEU A 1105 ? 0.3563 0.3145 0.3649 0.0111  -0.0549 -0.0807 1103 LEU A CG  
8071  C CD1 . LEU A 1105 ? 0.3696 0.3277 0.3885 0.0061  -0.0564 -0.0773 1103 LEU A CD1 
8072  C CD2 . LEU A 1105 ? 0.3608 0.3146 0.3749 0.0121  -0.0573 -0.0867 1103 LEU A CD2 
8073  N N   . LEU A 1106 ? 0.3427 0.3140 0.3340 0.0137  -0.0516 -0.0735 1104 LEU A N   
8074  C CA  . LEU A 1106 ? 0.3019 0.2794 0.2878 0.0169  -0.0538 -0.0773 1104 LEU A CA  
8075  C C   . LEU A 1106 ? 0.3319 0.3111 0.3252 0.0164  -0.0586 -0.0848 1104 LEU A C   
8076  O O   . LEU A 1106 ? 0.3475 0.3255 0.3511 0.0125  -0.0605 -0.0848 1104 LEU A O   
8077  C CB  . LEU A 1106 ? 0.3251 0.3068 0.3092 0.0164  -0.0531 -0.0731 1104 LEU A CB  
8078  C CG  . LEU A 1106 ? 0.3851 0.3659 0.3621 0.0175  -0.0490 -0.0665 1104 LEU A CG  
8079  C CD1 . LEU A 1106 ? 0.3692 0.3554 0.3438 0.0186  -0.0495 -0.0647 1104 LEU A CD1 
8080  C CD2 . LEU A 1106 ? 0.3450 0.3242 0.3129 0.0208  -0.0471 -0.0662 1104 LEU A CD2 
8081  N N   . VAL A 1107 ? 0.3124 0.2949 0.3008 0.0201  -0.0607 -0.0912 1105 VAL A N   
8082  C CA  . VAL A 1107 ? 0.3212 0.3059 0.3164 0.0201  -0.0657 -0.0994 1105 VAL A CA  
8083  C C   . VAL A 1107 ? 0.3094 0.3024 0.2977 0.0233  -0.0678 -0.1026 1105 VAL A C   
8084  O O   . VAL A 1107 ? 0.3811 0.3784 0.3624 0.0272  -0.0687 -0.1074 1105 VAL A O   
8085  C CB  . VAL A 1107 ? 0.3072 0.2888 0.3051 0.0215  -0.0671 -0.1058 1105 VAL A CB  
8086  C CG1 . VAL A 1107 ? 0.3723 0.3552 0.3803 0.0207  -0.0728 -0.1144 1105 VAL A CG1 
8087  C CG2 . VAL A 1107 ? 0.3773 0.3506 0.3804 0.0187  -0.0645 -0.1011 1105 VAL A CG2 
8088  N N   . PRO A 1108 ? 0.3263 0.3226 0.3162 0.0219  -0.0685 -0.0998 1106 PRO A N   
8089  C CA  . PRO A 1108 ? 0.3553 0.3597 0.3388 0.0250  -0.0706 -0.1019 1106 PRO A CA  
8090  C C   . PRO A 1108 ? 0.3818 0.3905 0.3713 0.0252  -0.0760 -0.1107 1106 PRO A C   
8091  O O   . PRO A 1108 ? 0.3709 0.3760 0.3712 0.0223  -0.0784 -0.1145 1106 PRO A O   
8092  C CB  . PRO A 1108 ? 0.3961 0.4015 0.3808 0.0232  -0.0692 -0.0954 1106 PRO A CB  
8093  C CG  . PRO A 1108 ? 0.3534 0.3539 0.3500 0.0181  -0.0690 -0.0939 1106 PRO A CG  
8094  C CD  . PRO A 1108 ? 0.3468 0.3405 0.3443 0.0175  -0.0672 -0.0941 1106 PRO A CD  
8095  N N   . ALA A 1109 ? 0.3440 0.3606 0.3265 0.0287  -0.0781 -0.1136 1107 ALA A N   
8096  C CA  . ALA A 1109 ? 0.3819 0.4043 0.3691 0.0292  -0.0834 -0.1217 1107 ALA A CA  
8097  C C   . ALA A 1109 ? 0.4382 0.4665 0.4253 0.0291  -0.0852 -0.1196 1107 ALA A C   
8098  O O   . ALA A 1109 ? 0.4077 0.4385 0.4034 0.0273  -0.0891 -0.1242 1107 ALA A O   
8099  C CB  . ALA A 1109 ? 0.3922 0.4210 0.3716 0.0338  -0.0853 -0.1288 1107 ALA A CB  
8100  N N   . THR A 1110 ? 0.3950 0.4259 0.3734 0.0311  -0.0827 -0.1130 1108 THR A N   
8101  C CA  . THR A 1110 ? 0.3925 0.4293 0.3704 0.0317  -0.0845 -0.1110 1108 THR A CA  
8102  C C   . THR A 1110 ? 0.3761 0.4092 0.3543 0.0301  -0.0807 -0.1023 1108 THR A C   
8103  O O   . THR A 1110 ? 0.3861 0.4134 0.3611 0.0297  -0.0766 -0.0974 1108 THR A O   
8104  C CB  . THR A 1110 ? 0.4025 0.4474 0.3694 0.0364  -0.0861 -0.1118 1108 THR A CB  
8105  O OG1 . THR A 1110 ? 0.3657 0.4086 0.3230 0.0384  -0.0821 -0.1054 1108 THR A OG1 
8106  C CG2 . THR A 1110 ? 0.4274 0.4777 0.3931 0.0384  -0.0897 -0.1211 1108 THR A CG2 
8107  N N   . GLU A 1111 ? 0.3941 0.4311 0.3762 0.0294  -0.0822 -0.1007 1109 GLU A N   
8108  C CA  . GLU A 1111 ? 0.4306 0.4657 0.4134 0.0284  -0.0790 -0.0935 1109 GLU A CA  
8109  C C   . GLU A 1111 ? 0.3995 0.4334 0.3716 0.0318  -0.0763 -0.0878 1109 GLU A C   
8110  O O   . GLU A 1111 ? 0.3953 0.4240 0.3668 0.0308  -0.0724 -0.0824 1109 GLU A O   
8111  C CB  . GLU A 1111 ? 0.4434 0.4848 0.4315 0.0281  -0.0817 -0.0938 1109 GLU A CB  
8112  C CG  . GLU A 1111 ? 0.4504 0.4920 0.4377 0.0287  -0.0792 -0.0874 1109 GLU A CG  
8113  C CD  . GLU A 1111 ? 0.4723 0.5202 0.4668 0.0279  -0.0817 -0.0884 1109 GLU A CD  
8114  O OE1 . GLU A 1111 ? 0.4681 0.5163 0.4722 0.0239  -0.0815 -0.0894 1109 GLU A OE1 
8115  O OE2 . GLU A 1111 ? 0.4286 0.4817 0.4195 0.0312  -0.0840 -0.0879 1109 GLU A OE2 
8116  N N   . SER A 1112 ? 0.3648 0.4039 0.3288 0.0356  -0.0784 -0.0888 1110 SER A N   
8117  C CA  . SER A 1112 ? 0.3608 0.3991 0.3153 0.0385  -0.0761 -0.0828 1110 SER A CA  
8118  C C   . SER A 1112 ? 0.3759 0.4082 0.3265 0.0380  -0.0725 -0.0815 1110 SER A C   
8119  O O   . SER A 1112 ? 0.3306 0.3585 0.2777 0.0383  -0.0691 -0.0753 1110 SER A O   
8120  C CB  . SER A 1112 ? 0.4258 0.4720 0.3726 0.0424  -0.0794 -0.0837 1110 SER A CB  
8121  O OG  . SER A 1112 ? 0.4048 0.4506 0.3433 0.0448  -0.0775 -0.0770 1110 SER A OG  
8122  N N   . GLY A 1113 ? 0.3514 0.3836 0.3028 0.0375  -0.0733 -0.0875 1111 GLY A N   
8123  C CA  . GLY A 1113 ? 0.3458 0.3723 0.2946 0.0370  -0.0700 -0.0868 1111 GLY A CA  
8124  C C   . GLY A 1113 ? 0.3589 0.3773 0.3135 0.0336  -0.0664 -0.0825 1111 GLY A C   
8125  O O   . GLY A 1113 ? 0.3287 0.3426 0.2793 0.0338  -0.0628 -0.0777 1111 GLY A O   
8126  N N   . LEU A 1114 ? 0.3461 0.3635 0.3106 0.0304  -0.0675 -0.0841 1112 LEU A N   
8127  C CA  . LEU A 1114 ? 0.3270 0.3386 0.2973 0.0269  -0.0643 -0.0797 1112 LEU A CA  
8128  C C   . LEU A 1114 ? 0.2867 0.2975 0.2524 0.0281  -0.0615 -0.0728 1112 LEU A C   
8129  O O   . LEU A 1114 ? 0.3551 0.3607 0.3197 0.0271  -0.0578 -0.0686 1112 LEU A O   
8130  C CB  . LEU A 1114 ? 0.3543 0.3672 0.3356 0.0233  -0.0662 -0.0818 1112 LEU A CB  
8131  C CG  . LEU A 1114 ? 0.3506 0.3604 0.3377 0.0197  -0.0631 -0.0765 1112 LEU A CG  
8132  C CD1 . LEU A 1114 ? 0.3557 0.3583 0.3427 0.0180  -0.0597 -0.0740 1112 LEU A CD1 
8133  C CD2 . LEU A 1114 ? 0.3955 0.4084 0.3937 0.0160  -0.0652 -0.0783 1112 LEU A CD2 
8134  N N   . TYR A 1115 ? 0.3259 0.3419 0.2895 0.0303  -0.0634 -0.0717 1113 TYR A N   
8135  C CA  . TYR A 1115 ? 0.3422 0.3573 0.3028 0.0317  -0.0614 -0.0657 1113 TYR A CA  
8136  C C   . TYR A 1115 ? 0.3129 0.3246 0.2647 0.0339  -0.0590 -0.0618 1113 TYR A C   
8137  O O   . TYR A 1115 ? 0.2854 0.2927 0.2365 0.0335  -0.0559 -0.0570 1113 TYR A O   
8138  C CB  . TYR A 1115 ? 0.3031 0.3245 0.2635 0.0342  -0.0646 -0.0656 1113 TYR A CB  
8139  C CG  . TYR A 1115 ? 0.3700 0.3954 0.3395 0.0321  -0.0667 -0.0686 1113 TYR A CG  
8140  C CD1 . TYR A 1115 ? 0.3399 0.3633 0.3174 0.0280  -0.0650 -0.0694 1113 TYR A CD1 
8141  C CD2 . TYR A 1115 ? 0.3829 0.4149 0.3532 0.0342  -0.0704 -0.0701 1113 TYR A CD2 
8142  C CE1 . TYR A 1115 ? 0.3892 0.4175 0.3754 0.0259  -0.0669 -0.0716 1113 TYR A CE1 
8143  C CE2 . TYR A 1115 ? 0.4243 0.4607 0.4030 0.0324  -0.0723 -0.0727 1113 TYR A CE2 
8144  C CZ  . TYR A 1115 ? 0.4111 0.4460 0.3979 0.0282  -0.0704 -0.0734 1113 TYR A CZ  
8145  O OH  . TYR A 1115 ? 0.4558 0.4963 0.4514 0.0261  -0.0723 -0.0757 1113 TYR A OH  
8146  N N   . HIS A 1116 ? 0.3314 0.3458 0.2767 0.0362  -0.0604 -0.0638 1114 HIS A N   
8147  C CA  . HIS A 1116 ? 0.3569 0.3693 0.2940 0.0380  -0.0581 -0.0600 1114 HIS A CA  
8148  C C   . HIS A 1116 ? 0.3410 0.3467 0.2793 0.0357  -0.0545 -0.0597 1114 HIS A C   
8149  O O   . HIS A 1116 ? 0.3281 0.3300 0.2628 0.0360  -0.0515 -0.0547 1114 HIS A O   
8150  C CB  . HIS A 1116 ? 0.3788 0.3976 0.3088 0.0408  -0.0605 -0.0629 1114 HIS A CB  
8151  C CG  . HIS A 1116 ? 0.3807 0.4056 0.3065 0.0436  -0.0633 -0.0601 1114 HIS A CG  
8152  N ND1 . HIS A 1116 ? 0.4261 0.4569 0.3549 0.0443  -0.0673 -0.0638 1114 HIS A ND1 
8153  C CD2 . HIS A 1116 ? 0.3978 0.4240 0.3174 0.0458  -0.0630 -0.0536 1114 HIS A CD2 
8154  C CE1 . HIS A 1116 ? 0.4120 0.4475 0.3362 0.0470  -0.0693 -0.0598 1114 HIS A CE1 
8155  N NE2 . HIS A 1116 ? 0.4614 0.4941 0.3803 0.0478  -0.0669 -0.0533 1114 HIS A NE2 
8156  N N   . GLN A 1117 ? 0.3265 0.3308 0.2704 0.0335  -0.0550 -0.0649 1115 GLN A N   
8157  C CA  . GLN A 1117 ? 0.2993 0.2972 0.2453 0.0313  -0.0519 -0.0643 1115 GLN A CA  
8158  C C   . GLN A 1117 ? 0.2983 0.2917 0.2484 0.0289  -0.0490 -0.0592 1115 GLN A C   
8159  O O   . GLN A 1117 ? 0.3240 0.3128 0.2722 0.0283  -0.0457 -0.0555 1115 GLN A O   
8160  C CB  . GLN A 1117 ? 0.3208 0.3178 0.2738 0.0293  -0.0536 -0.0706 1115 GLN A CB  
8161  C CG  . GLN A 1117 ? 0.3189 0.3204 0.2685 0.0318  -0.0564 -0.0772 1115 GLN A CG  
8162  C CD  . GLN A 1117 ? 0.3561 0.3559 0.3145 0.0297  -0.0588 -0.0839 1115 GLN A CD  
8163  O OE1 . GLN A 1117 ? 0.3556 0.3519 0.3229 0.0261  -0.0590 -0.0833 1115 GLN A OE1 
8164  N NE2 . GLN A 1117 ? 0.3324 0.3349 0.2886 0.0319  -0.0607 -0.0904 1115 GLN A NE2 
8165  N N   . LEU A 1118 ? 0.2880 0.2836 0.2442 0.0274  -0.0502 -0.0591 1116 LEU A N   
8166  C CA  . LEU A 1118 ? 0.2994 0.2926 0.2596 0.0253  -0.0477 -0.0549 1116 LEU A CA  
8167  C C   . LEU A 1118 ? 0.2979 0.2897 0.2523 0.0276  -0.0458 -0.0498 1116 LEU A C   
8168  O O   . LEU A 1118 ? 0.2967 0.2847 0.2513 0.0264  -0.0426 -0.0463 1116 LEU A O   
8169  C CB  . LEU A 1118 ? 0.3119 0.3097 0.2796 0.0236  -0.0496 -0.0565 1116 LEU A CB  
8170  C CG  . LEU A 1118 ? 0.3585 0.3564 0.3326 0.0207  -0.0475 -0.0537 1116 LEU A CG  
8171  C CD1 . LEU A 1118 ? 0.3643 0.3571 0.3405 0.0177  -0.0444 -0.0518 1116 LEU A CD1 
8172  C CD2 . LEU A 1118 ? 0.4385 0.4420 0.4208 0.0186  -0.0500 -0.0566 1116 LEU A CD2 
8173  N N   . ALA A 1119 ? 0.2889 0.2841 0.2383 0.0308  -0.0478 -0.0492 1117 ALA A N   
8174  C CA  . ALA A 1119 ? 0.3180 0.3115 0.2629 0.0330  -0.0466 -0.0440 1117 ALA A CA  
8175  C C   . ALA A 1119 ? 0.3046 0.2934 0.2441 0.0330  -0.0436 -0.0412 1117 ALA A C   
8176  O O   . ALA A 1119 ? 0.3103 0.2952 0.2497 0.0325  -0.0411 -0.0373 1117 ALA A O   
8177  C CB  . ALA A 1119 ? 0.3009 0.2990 0.2418 0.0363  -0.0498 -0.0431 1117 ALA A CB  
8178  N N   . ALA A 1120 ? 0.2869 0.2768 0.2222 0.0337  -0.0440 -0.0437 1118 ALA A N   
8179  C CA  . ALA A 1120 ? 0.3115 0.2979 0.2420 0.0338  -0.0412 -0.0415 1118 ALA A CA  
8180  C C   . ALA A 1120 ? 0.2978 0.2785 0.2329 0.0309  -0.0381 -0.0406 1118 ALA A C   
8181  O O   . ALA A 1120 ? 0.3036 0.2806 0.2365 0.0307  -0.0353 -0.0364 1118 ALA A O   
8182  C CB  . ALA A 1120 ? 0.3514 0.3409 0.2783 0.0349  -0.0422 -0.0460 1118 ALA A CB  
8183  N N   . ALA A 1121 ? 0.3142 0.2945 0.2560 0.0284  -0.0386 -0.0441 1119 ALA A N   
8184  C CA  . ALA A 1121 ? 0.3126 0.2882 0.2589 0.0253  -0.0359 -0.0428 1119 ALA A CA  
8185  C C   . ALA A 1121 ? 0.3135 0.2882 0.2620 0.0244  -0.0341 -0.0387 1119 ALA A C   
8186  O O   . ALA A 1121 ? 0.2905 0.2614 0.2386 0.0234  -0.0312 -0.0356 1119 ALA A O   
8187  C CB  . ALA A 1121 ? 0.3261 0.3022 0.2800 0.0226  -0.0375 -0.0470 1119 ALA A CB  
8188  N N   . LEU A 1122 ? 0.3058 0.2844 0.2570 0.0249  -0.0359 -0.0390 1120 LEU A N   
8189  C CA  . LEU A 1122 ? 0.2770 0.2557 0.2310 0.0244  -0.0344 -0.0361 1120 LEU A CA  
8190  C C   . LEU A 1122 ? 0.2850 0.2610 0.2338 0.0268  -0.0333 -0.0322 1120 LEU A C   
8191  O O   . LEU A 1122 ? 0.3137 0.2873 0.2635 0.0261  -0.0310 -0.0296 1120 LEU A O   
8192  C CB  . LEU A 1122 ? 0.3131 0.2972 0.2716 0.0248  -0.0368 -0.0380 1120 LEU A CB  
8193  C CG  . LEU A 1122 ? 0.2936 0.2812 0.2589 0.0219  -0.0379 -0.0413 1120 LEU A CG  
8194  C CD1 . LEU A 1122 ? 0.3407 0.3345 0.3101 0.0227  -0.0403 -0.0430 1120 LEU A CD1 
8195  C CD2 . LEU A 1122 ? 0.2965 0.2828 0.2664 0.0182  -0.0350 -0.0396 1120 LEU A CD2 
8196  N N   . ALA A 1123 ? 0.3186 0.2952 0.2619 0.0296  -0.0350 -0.0314 1121 ALA A N   
8197  C CA  . ALA A 1123 ? 0.3057 0.2799 0.2447 0.0317  -0.0344 -0.0269 1121 ALA A CA  
8198  C C   . ALA A 1123 ? 0.3386 0.3081 0.2750 0.0305  -0.0311 -0.0245 1121 ALA A C   
8199  O O   . ALA A 1123 ? 0.3341 0.3008 0.2691 0.0312  -0.0301 -0.0206 1121 ALA A O   
8200  C CB  . ALA A 1123 ? 0.3005 0.2774 0.2339 0.0344  -0.0370 -0.0260 1121 ALA A CB  
8201  N N   . THR A 1124 ? 0.3052 0.2736 0.2414 0.0288  -0.0298 -0.0267 1122 THR A N   
8202  C CA  . THR A 1124 ? 0.2924 0.2567 0.2267 0.0277  -0.0268 -0.0248 1122 THR A CA  
8203  C C   . THR A 1124 ? 0.3105 0.2727 0.2503 0.0247  -0.0247 -0.0250 1122 THR A C   
8204  O O   . THR A 1124 ? 0.3106 0.2697 0.2500 0.0234  -0.0224 -0.0239 1122 THR A O   
8205  C CB  . THR A 1124 ? 0.3222 0.2872 0.2529 0.0282  -0.0269 -0.0272 1122 THR A CB  
8206  O OG1 . THR A 1124 ? 0.3203 0.2879 0.2542 0.0275  -0.0291 -0.0322 1122 THR A OG1 
8207  C CG2 . THR A 1124 ? 0.3350 0.3025 0.2587 0.0310  -0.0278 -0.0252 1122 THR A CG2 
8208  N N   . GLY A 1125 ? 0.2985 0.2632 0.2436 0.0236  -0.0255 -0.0260 1123 GLY A N   
8209  C CA  . GLY A 1125 ? 0.3032 0.2677 0.2532 0.0208  -0.0234 -0.0252 1123 GLY A CA  
8210  C C   . GLY A 1125 ? 0.3348 0.3000 0.2896 0.0177  -0.0233 -0.0272 1123 GLY A C   
8211  O O   . GLY A 1125 ? 0.2993 0.2649 0.2581 0.0151  -0.0216 -0.0258 1123 GLY A O   
8212  N N   . ASN A 1126 ? 0.2907 0.2564 0.2456 0.0180  -0.0254 -0.0303 1124 ASN A N   
8213  C CA  . ASN A 1126 ? 0.3022 0.2674 0.2623 0.0151  -0.0259 -0.0322 1124 ASN A CA  
8214  C C   . ASN A 1126 ? 0.3262 0.2960 0.2931 0.0130  -0.0276 -0.0338 1124 ASN A C   
8215  O O   . ASN A 1126 ? 0.3253 0.2993 0.2923 0.0143  -0.0291 -0.0348 1124 ASN A O   
8216  C CB  . ASN A 1126 ? 0.2905 0.2541 0.2482 0.0166  -0.0276 -0.0357 1124 ASN A CB  
8217  C CG  . ASN A 1126 ? 0.3404 0.3007 0.2917 0.0186  -0.0258 -0.0342 1124 ASN A CG  
8218  O OD1 . ASN A 1126 ? 0.3117 0.2684 0.2638 0.0172  -0.0237 -0.0325 1124 ASN A OD1 
8219  N ND2 . ASN A 1126 ? 0.2854 0.2474 0.2303 0.0217  -0.0267 -0.0347 1124 ASN A ND2 
8220  N N   . SER A 1127 ? 0.3557 0.3251 0.3289 0.0094  -0.0275 -0.0336 1125 SER A N   
8221  C CA  . SER A 1127 ? 0.3506 0.3241 0.3312 0.0069  -0.0297 -0.0355 1125 SER A CA  
8222  C C   . SER A 1127 ? 0.3454 0.3169 0.3270 0.0076  -0.0327 -0.0400 1125 SER A C   
8223  O O   . SER A 1127 ? 0.3380 0.3055 0.3149 0.0097  -0.0327 -0.0415 1125 SER A O   
8224  C CB  . SER A 1127 ? 0.3686 0.3430 0.3561 0.0024  -0.0284 -0.0323 1125 SER A CB  
8225  O OG  . SER A 1127 ? 0.3707 0.3394 0.3594 0.0012  -0.0280 -0.0315 1125 SER A OG  
8226  N N   . VAL A 1128 ? 0.3110 0.2861 0.2990 0.0058  -0.0355 -0.0425 1126 VAL A N   
8227  C CA  . VAL A 1128 ? 0.3120 0.2859 0.3016 0.0066  -0.0388 -0.0477 1126 VAL A CA  
8228  C C   . VAL A 1128 ? 0.3784 0.3527 0.3789 0.0023  -0.0410 -0.0485 1126 VAL A C   
8229  O O   . VAL A 1128 ? 0.3531 0.3311 0.3594 -0.0011 -0.0404 -0.0453 1126 VAL A O   
8230  C CB  . VAL A 1128 ? 0.3480 0.3263 0.3337 0.0098  -0.0413 -0.0513 1126 VAL A CB  
8231  C CG1 . VAL A 1128 ? 0.3195 0.2974 0.2954 0.0138  -0.0395 -0.0497 1126 VAL A CG1 
8232  C CG2 . VAL A 1128 ? 0.3323 0.3167 0.3232 0.0082  -0.0423 -0.0509 1126 VAL A CG2 
8233  N N   . ALA A 1129 ? 0.3197 0.2905 0.3232 0.0024  -0.0436 -0.0527 1127 ALA A N   
8234  C CA  . ALA A 1129 ? 0.3820 0.3529 0.3964 -0.0011 -0.0470 -0.0550 1127 ALA A CA  
8235  C C   . ALA A 1129 ? 0.3554 0.3281 0.3691 0.0016  -0.0509 -0.0622 1127 ALA A C   
8236  O O   . ALA A 1129 ? 0.3569 0.3270 0.3657 0.0049  -0.0516 -0.0664 1127 ALA A O   
8237  C CB  . ALA A 1129 ? 0.3614 0.3260 0.3822 -0.0035 -0.0473 -0.0539 1127 ALA A CB  
8238  N N   . ILE A 1130 ? 0.3674 0.3455 0.3854 0.0004  -0.0533 -0.0638 1128 ILE A N   
8239  C CA  . ILE A 1130 ? 0.3886 0.3699 0.4056 0.0030  -0.0571 -0.0705 1128 ILE A CA  
8240  C C   . ILE A 1130 ? 0.3863 0.3658 0.4146 0.0002  -0.0613 -0.0750 1128 ILE A C   
8241  O O   . ILE A 1130 ? 0.3693 0.3489 0.4077 -0.0046 -0.0620 -0.0719 1128 ILE A O   
8242  C CB  . ILE A 1130 ? 0.3680 0.3565 0.3832 0.0037  -0.0575 -0.0700 1128 ILE A CB  
8243  C CG1 . ILE A 1130 ? 0.3774 0.3672 0.3839 0.0059  -0.0536 -0.0650 1128 ILE A CG1 
8244  C CG2 . ILE A 1130 ? 0.3358 0.3279 0.3484 0.0069  -0.0614 -0.0767 1128 ILE A CG2 
8245  C CD1 . ILE A 1130 ? 0.3649 0.3616 0.3717 0.0063  -0.0540 -0.0641 1128 ILE A CD1 
8246  N N   . ASP A 1131 ? 0.3594 0.3378 0.3865 0.0031  -0.0644 -0.0822 1129 ASP A N   
8247  C CA  . ASP A 1131 ? 0.4196 0.3959 0.4580 0.0009  -0.0690 -0.0876 1129 ASP A CA  
8248  C C   . ASP A 1131 ? 0.4086 0.3902 0.4552 -0.0021 -0.0721 -0.0883 1129 ASP A C   
8249  O O   . ASP A 1131 ? 0.3846 0.3722 0.4265 0.0003  -0.0734 -0.0913 1129 ASP A O   
8250  C CB  . ASP A 1131 ? 0.3739 0.3501 0.4082 0.0054  -0.0717 -0.0964 1129 ASP A CB  
8251  C CG  . ASP A 1131 ? 0.4296 0.4037 0.4761 0.0037  -0.0772 -0.1034 1129 ASP A CG  
8252  O OD1 . ASP A 1131 ? 0.4275 0.3976 0.4862 -0.0011 -0.0786 -0.1006 1129 ASP A OD1 
8253  O OD2 . ASP A 1131 ? 0.4514 0.4284 0.4955 0.0073  -0.0803 -0.1118 1129 ASP A OD2 
8254  N N   . ALA A 1132 ? 0.4573 0.4371 0.5163 -0.0075 -0.0732 -0.0849 1130 ALA A N   
8255  C CA  . ALA A 1132 ? 0.4293 0.4146 0.4971 -0.0108 -0.0762 -0.0853 1130 ALA A CA  
8256  C C   . ALA A 1132 ? 0.4575 0.4436 0.5304 -0.0096 -0.0819 -0.0946 1130 ALA A C   
8257  O O   . ALA A 1132 ? 0.5027 0.4950 0.5794 -0.0105 -0.0845 -0.0967 1130 ALA A O   
8258  C CB  . ALA A 1132 ? 0.4446 0.4286 0.5249 -0.0174 -0.0760 -0.0787 1130 ALA A CB  
8259  N N   . ALA A 1133 ? 0.4365 0.4173 0.5097 -0.0072 -0.0841 -0.1007 1131 ALA A N   
8260  C CA  . ALA A 1133 ? 0.5164 0.4986 0.5942 -0.0055 -0.0897 -0.1107 1131 ALA A CA  
8261  C C   . ALA A 1133 ? 0.4715 0.4612 0.5377 -0.0004 -0.0900 -0.1156 1131 ALA A C   
8262  O O   . ALA A 1133 ? 0.5027 0.4953 0.5716 0.0013  -0.0947 -0.1240 1131 ALA A O   
8263  C CB  . ALA A 1133 ? 0.4641 0.4394 0.5456 -0.0039 -0.0919 -0.1166 1131 ALA A CB  
8264  N N   . SER A 1134 ? 0.4791 0.4719 0.5328 0.0021  -0.0855 -0.1104 1132 SER A N   
8265  C CA  . SER A 1134 ? 0.4505 0.4505 0.4935 0.0067  -0.0859 -0.1136 1132 SER A CA  
8266  C C   . SER A 1134 ? 0.4668 0.4737 0.5145 0.0051  -0.0886 -0.1142 1132 SER A C   
8267  O O   . SER A 1134 ? 0.4242 0.4376 0.4660 0.0086  -0.0907 -0.1186 1132 SER A O   
8268  C CB  . SER A 1134 ? 0.4609 0.4615 0.4907 0.0095  -0.0806 -0.1072 1132 SER A CB  
8269  O OG  . SER A 1134 ? 0.4390 0.4401 0.4713 0.0063  -0.0776 -0.0993 1132 SER A OG  
8270  N N   . GLY A 1135 ? 0.4720 0.4787 0.5303 -0.0001 -0.0885 -0.1095 1133 GLY A N   
8271  C CA  . GLY A 1135 ? 0.4916 0.5056 0.5546 -0.0018 -0.0905 -0.1093 1133 GLY A CA  
8272  C C   . GLY A 1135 ? 0.4960 0.5159 0.5490 0.0009  -0.0874 -0.1050 1133 GLY A C   
8273  O O   . GLY A 1135 ? 0.4278 0.4548 0.4826 0.0011  -0.0896 -0.1065 1133 GLY A O   
8274  N N   . LEU A 1136 ? 0.4092 0.4264 0.4524 0.0031  -0.0827 -0.0999 1134 LEU A N   
8275  C CA  . LEU A 1136 ? 0.4740 0.4959 0.5081 0.0062  -0.0802 -0.0962 1134 LEU A CA  
8276  C C   . LEU A 1136 ? 0.4583 0.4815 0.4955 0.0032  -0.0765 -0.0888 1134 LEU A C   
8277  O O   . LEU A 1136 ? 0.4640 0.4892 0.4936 0.0058  -0.0737 -0.0852 1134 LEU A O   
8278  C CB  . LEU A 1136 ? 0.4350 0.4540 0.4559 0.0110  -0.0777 -0.0956 1134 LEU A CB  
8279  C CG  . LEU A 1136 ? 0.4327 0.4535 0.4474 0.0151  -0.0809 -0.1025 1134 LEU A CG  
8280  C CD1 . LEU A 1136 ? 0.3993 0.4174 0.4019 0.0189  -0.0778 -0.1005 1134 LEU A CD1 
8281  C CD2 . LEU A 1136 ? 0.4631 0.4923 0.4761 0.0174  -0.0843 -0.1055 1134 LEU A CD2 
8282  N N   . GLN A 1137 ? 0.4561 0.4790 0.5047 -0.0022 -0.0766 -0.0866 1135 GLN A N   
8283  C CA  . GLN A 1137 ? 0.4478 0.4734 0.4993 -0.0052 -0.0729 -0.0797 1135 GLN A CA  
8284  C C   . GLN A 1137 ? 0.4663 0.5006 0.5163 -0.0035 -0.0727 -0.0790 1135 GLN A C   
8285  O O   . GLN A 1137 ? 0.4543 0.4907 0.5005 -0.0027 -0.0691 -0.0745 1135 GLN A O   
8286  C CB  . GLN A 1137 ? 0.4693 0.4948 0.5343 -0.0116 -0.0738 -0.0774 1135 GLN A CB  
8287  C CG  . GLN A 1137 ? 0.4508 0.4673 0.5180 -0.0137 -0.0730 -0.0759 1135 GLN A CG  
8288  C CD  . GLN A 1137 ? 0.4383 0.4500 0.5102 -0.0135 -0.0778 -0.0827 1135 GLN A CD  
8289  O OE1 . GLN A 1137 ? 0.4760 0.4903 0.5456 -0.0104 -0.0811 -0.0892 1135 GLN A OE1 
8290  N NE2 . GLN A 1137 ? 0.5419 0.5471 0.6213 -0.0168 -0.0784 -0.0815 1135 GLN A NE2 
8291  N N   . ALA A 1138 ? 0.4716 0.5112 0.5248 -0.0027 -0.0769 -0.0839 1136 ALA A N   
8292  C CA  . ALA A 1138 ? 0.4061 0.4542 0.4586 -0.0009 -0.0771 -0.0834 1136 ALA A CA  
8293  C C   . ALA A 1138 ? 0.4991 0.5467 0.5394 0.0051  -0.0758 -0.0830 1136 ALA A C   
8294  O O   . ALA A 1138 ? 0.4698 0.5236 0.5092 0.0072  -0.0758 -0.0822 1136 ALA A O   
8295  C CB  . ALA A 1138 ? 0.4554 0.5096 0.5148 -0.0015 -0.0822 -0.0888 1136 ALA A CB  
8296  N N   . SER A 1139 ? 0.4895 0.5302 0.5210 0.0078  -0.0747 -0.0832 1137 SER A N   
8297  C CA  . SER A 1139 ? 0.4858 0.5260 0.5064 0.0130  -0.0736 -0.0818 1137 SER A CA  
8298  C C   . SER A 1139 ? 0.3967 0.4350 0.4142 0.0133  -0.0689 -0.0760 1137 SER A C   
8299  O O   . SER A 1139 ? 0.4247 0.4627 0.4347 0.0173  -0.0681 -0.0742 1137 SER A O   
8300  C CB  . SER A 1139 ? 0.4471 0.4820 0.4594 0.0158  -0.0743 -0.0843 1137 SER A CB  
8301  O OG  . SER A 1139 ? 0.4735 0.5123 0.4863 0.0172  -0.0789 -0.0904 1137 SER A OG  
8302  N N   . LEU A 1140 ? 0.4063 0.4438 0.4300 0.0091  -0.0662 -0.0729 1138 LEU A N   
8303  C CA  . LEU A 1140 ? 0.4425 0.4784 0.4635 0.0091  -0.0618 -0.0678 1138 LEU A CA  
8304  C C   . LEU A 1140 ? 0.4761 0.5195 0.5052 0.0061  -0.0604 -0.0657 1138 LEU A C   
8305  O O   . LEU A 1140 ? 0.4813 0.5242 0.5127 0.0032  -0.0570 -0.0619 1138 LEU A O   
8306  C CB  . LEU A 1140 ? 0.4441 0.4721 0.4631 0.0072  -0.0591 -0.0654 1138 LEU A CB  
8307  C CG  . LEU A 1140 ? 0.3827 0.4037 0.3923 0.0106  -0.0590 -0.0664 1138 LEU A CG  
8308  C CD1 . LEU A 1140 ? 0.4477 0.4619 0.4572 0.0082  -0.0560 -0.0636 1138 LEU A CD1 
8309  C CD2 . LEU A 1140 ? 0.3569 0.3782 0.3579 0.0153  -0.0580 -0.0646 1138 LEU A CD2 
8310  N N   . LYS A 1141 ? 0.4831 0.5343 0.5167 0.0066  -0.0630 -0.0681 1139 LYS A N   
8311  C CA  . LYS A 1141 ? 0.5068 0.5670 0.5484 0.0039  -0.0617 -0.0665 1139 LYS A CA  
8312  C C   . LYS A 1141 ? 0.4901 0.5529 0.5279 0.0071  -0.0589 -0.0644 1139 LYS A C   
8313  O O   . LYS A 1141 ? 0.4782 0.5387 0.5094 0.0121  -0.0598 -0.0653 1139 LYS A O   
8314  C CB  . LYS A 1141 ? 0.5269 0.5952 0.5752 0.0036  -0.0656 -0.0702 1139 LYS A CB  
8315  N N   . ASN A 1142 ? 0.4430 0.5113 0.4857 0.0042  -0.0557 -0.0616 1140 ASN A N   
8316  C CA  . ASN A 1142 ? 0.4742 0.5467 0.5151 0.0071  -0.0533 -0.0606 1140 ASN A CA  
8317  C C   . ASN A 1142 ? 0.4490 0.5123 0.4806 0.0106  -0.0515 -0.0590 1140 ASN A C   
8318  O O   . ASN A 1142 ? 0.4471 0.5108 0.4755 0.0150  -0.0516 -0.0596 1140 ASN A O   
8319  C CB  . ASN A 1142 ? 0.5453 0.6253 0.5885 0.0107  -0.0559 -0.0639 1140 ASN A CB  
8320  C CG  . ASN A 1142 ? 0.5897 0.6798 0.6424 0.0074  -0.0577 -0.0656 1140 ASN A CG  
8321  O OD1 . ASN A 1142 ? 0.6103 0.7021 0.6645 0.0088  -0.0615 -0.0687 1140 ASN A OD1 
8322  N ND2 . ASN A 1142 ? 0.5737 0.6711 0.6331 0.0028  -0.0551 -0.0633 1140 ASN A ND2 
8323  N N   . LEU A 1143 ? 0.4626 0.5176 0.4907 0.0085  -0.0500 -0.0568 1141 LEU A N   
8324  C CA  . LEU A 1143 ? 0.4719 0.5190 0.4920 0.0111  -0.0478 -0.0547 1141 LEU A CA  
8325  C C   . LEU A 1143 ? 0.4748 0.5263 0.4961 0.0112  -0.0444 -0.0528 1141 LEU A C   
8326  O O   . LEU A 1143 ? 0.4916 0.5503 0.5190 0.0074  -0.0425 -0.0515 1141 LEU A O   
8327  C CB  . LEU A 1143 ? 0.4491 0.4877 0.4664 0.0086  -0.0466 -0.0528 1141 LEU A CB  
8328  C CG  . LEU A 1143 ? 0.4704 0.5018 0.4823 0.0105  -0.0491 -0.0548 1141 LEU A CG  
8329  C CD1 . LEU A 1143 ? 0.4799 0.5042 0.4909 0.0077  -0.0476 -0.0531 1141 LEU A CD1 
8330  C CD2 . LEU A 1143 ? 0.3915 0.4192 0.3949 0.0158  -0.0496 -0.0548 1141 LEU A CD2 
8331  N N   . PRO A 1144 ? 0.4633 0.5113 0.4792 0.0154  -0.0437 -0.0525 1142 PRO A N   
8332  C CA  . PRO A 1144 ? 0.4294 0.4807 0.4462 0.0155  -0.0405 -0.0511 1142 PRO A CA  
8333  C C   . PRO A 1144 ? 0.4311 0.4801 0.4477 0.0112  -0.0372 -0.0477 1142 PRO A C   
8334  O O   . PRO A 1144 ? 0.4107 0.4519 0.4242 0.0095  -0.0373 -0.0461 1142 PRO A O   
8335  C CB  . PRO A 1144 ? 0.4403 0.4845 0.4507 0.0205  -0.0410 -0.0510 1142 PRO A CB  
8336  C CG  . PRO A 1144 ? 0.4279 0.4691 0.4358 0.0234  -0.0448 -0.0525 1142 PRO A CG  
8337  C CD  . PRO A 1144 ? 0.4525 0.4935 0.4616 0.0199  -0.0459 -0.0530 1142 PRO A CD  
8338  N N   . GLN A 1145 ? 0.3860 0.4428 0.4063 0.0094  -0.0345 -0.0467 1143 GLN A N   
8339  C CA  . GLN A 1145 ? 0.3951 0.4514 0.4160 0.0049  -0.0315 -0.0429 1143 GLN A CA  
8340  C C   . GLN A 1145 ? 0.4111 0.4559 0.4246 0.0061  -0.0302 -0.0408 1143 GLN A C   
8341  O O   . GLN A 1145 ? 0.4078 0.4477 0.4207 0.0029  -0.0292 -0.0380 1143 GLN A O   
8342  C CB  . GLN A 1145 ? 0.4603 0.5284 0.4854 0.0035  -0.0287 -0.0424 1143 GLN A CB  
8343  N N   . THR A 1146 ? 0.3918 0.4323 0.4003 0.0107  -0.0303 -0.0420 1144 THR A N   
8344  C CA  . THR A 1146 ? 0.4353 0.4655 0.4371 0.0118  -0.0291 -0.0398 1144 THR A CA  
8345  C C   . THR A 1146 ? 0.3993 0.4212 0.3978 0.0112  -0.0306 -0.0392 1144 THR A C   
8346  O O   . THR A 1146 ? 0.3814 0.3967 0.3768 0.0097  -0.0291 -0.0368 1144 THR A O   
8347  C CB  . THR A 1146 ? 0.3996 0.4265 0.3976 0.0168  -0.0298 -0.0411 1144 THR A CB  
8348  O OG1 . THR A 1146 ? 0.4261 0.4549 0.4253 0.0199  -0.0331 -0.0438 1144 THR A OG1 
8349  C CG2 . THR A 1146 ? 0.4075 0.4407 0.4082 0.0175  -0.0277 -0.0418 1144 THR A CG2 
8350  N N   . VAL A 1147 ? 0.3833 0.4058 0.3825 0.0125  -0.0338 -0.0417 1145 VAL A N   
8351  C CA  . VAL A 1147 ? 0.3376 0.3536 0.3339 0.0122  -0.0356 -0.0422 1145 VAL A CA  
8352  C C   . VAL A 1147 ? 0.3812 0.3987 0.3832 0.0074  -0.0356 -0.0417 1145 VAL A C   
8353  O O   . VAL A 1147 ? 0.3996 0.4107 0.4000 0.0059  -0.0354 -0.0408 1145 VAL A O   
8354  C CB  . VAL A 1147 ? 0.3649 0.3819 0.3597 0.0156  -0.0392 -0.0452 1145 VAL A CB  
8355  C CG1 . VAL A 1147 ? 0.3377 0.3491 0.3290 0.0158  -0.0411 -0.0464 1145 VAL A CG1 
8356  C CG2 . VAL A 1147 ? 0.3209 0.3364 0.3114 0.0202  -0.0396 -0.0448 1145 VAL A CG2 
8357  N N   . GLY A 1148 ? 0.3988 0.4250 0.4082 0.0047  -0.0360 -0.0421 1146 GLY A N   
8358  C CA  . GLY A 1148 ? 0.3686 0.3966 0.3846 -0.0005 -0.0361 -0.0407 1146 GLY A CA  
8359  C C   . GLY A 1148 ? 0.4075 0.4313 0.4231 -0.0034 -0.0333 -0.0366 1146 GLY A C   
8360  O O   . GLY A 1148 ? 0.4031 0.4229 0.4219 -0.0065 -0.0341 -0.0354 1146 GLY A O   
8361  N N   . LEU A 1149 ? 0.3658 0.3904 0.3778 -0.0022 -0.0302 -0.0345 1147 LEU A N   
8362  C CA  . LEU A 1149 ? 0.3978 0.4189 0.4090 -0.0047 -0.0276 -0.0305 1147 LEU A CA  
8363  C C   . LEU A 1149 ? 0.4211 0.4309 0.4277 -0.0037 -0.0282 -0.0306 1147 LEU A C   
8364  O O   . LEU A 1149 ? 0.4078 0.4141 0.4161 -0.0066 -0.0272 -0.0276 1147 LEU A O   
8365  C CB  . LEU A 1149 ? 0.4571 0.4806 0.4645 -0.0028 -0.0246 -0.0293 1147 LEU A CB  
8366  C CG  . LEU A 1149 ? 0.4595 0.4954 0.4715 -0.0041 -0.0231 -0.0290 1147 LEU A CG  
8367  C CD1 . LEU A 1149 ? 0.4928 0.5297 0.5009 -0.0024 -0.0203 -0.0281 1147 LEU A CD1 
8368  C CD2 . LEU A 1149 ? 0.4845 0.5274 0.5041 -0.0099 -0.0227 -0.0257 1147 LEU A CD2 
8369  N N   . ARG A 1150 ? 0.3829 0.3879 0.3840 0.0004  -0.0300 -0.0337 1148 ARG A N   
8370  C CA  . ARG A 1150 ? 0.3474 0.3434 0.3436 0.0018  -0.0304 -0.0342 1148 ARG A CA  
8371  C C   . ARG A 1150 ? 0.3707 0.3644 0.3701 0.0009  -0.0336 -0.0373 1148 ARG A C   
8372  O O   . ARG A 1150 ? 0.3634 0.3505 0.3595 0.0020  -0.0342 -0.0384 1148 ARG A O   
8373  C CB  . ARG A 1150 ? 0.3687 0.3613 0.3566 0.0067  -0.0303 -0.0353 1148 ARG A CB  
8374  C CG  . ARG A 1150 ? 0.3914 0.3832 0.3758 0.0078  -0.0273 -0.0325 1148 ARG A CG  
8375  C CD  . ARG A 1150 ? 0.3821 0.3669 0.3588 0.0111  -0.0270 -0.0321 1148 ARG A CD  
8376  N NE  . ARG A 1150 ? 0.3670 0.3511 0.3405 0.0130  -0.0251 -0.0301 1148 ARG A NE  
8377  C CZ  . ARG A 1150 ? 0.4008 0.3811 0.3685 0.0164  -0.0254 -0.0297 1148 ARG A CZ  
8378  N NH1 . ARG A 1150 ? 0.3148 0.2927 0.2786 0.0184  -0.0274 -0.0309 1148 ARG A NH1 
8379  N NH2 . ARG A 1150 ? 0.3536 0.3331 0.3198 0.0177  -0.0239 -0.0279 1148 ARG A NH2 
8380  N N   . VAL A 1151 ? 0.3439 0.3433 0.3498 -0.0010 -0.0359 -0.0390 1149 VAL A N   
8381  C CA  . VAL A 1151 ? 0.3397 0.3378 0.3491 -0.0015 -0.0395 -0.0429 1149 VAL A CA  
8382  C C   . VAL A 1151 ? 0.4204 0.4192 0.4397 -0.0068 -0.0404 -0.0412 1149 VAL A C   
8383  O O   . VAL A 1151 ? 0.4419 0.4472 0.4670 -0.0102 -0.0394 -0.0381 1149 VAL A O   
8384  C CB  . VAL A 1151 ? 0.3952 0.3991 0.4048 0.0007  -0.0421 -0.0464 1149 VAL A CB  
8385  C CG1 . VAL A 1151 ? 0.4324 0.4363 0.4474 -0.0006 -0.0461 -0.0506 1149 VAL A CG1 
8386  C CG2 . VAL A 1151 ? 0.3594 0.3614 0.3597 0.0059  -0.0421 -0.0477 1149 VAL A CG2 
8387  N N   . SER A 1152 ? 0.3752 0.3678 0.3969 -0.0076 -0.0424 -0.0431 1150 SER A N   
8388  C CA  . SER A 1152 ? 0.3905 0.3831 0.4231 -0.0125 -0.0446 -0.0423 1150 SER A CA  
8389  C C   . SER A 1152 ? 0.3953 0.3849 0.4305 -0.0114 -0.0490 -0.0485 1150 SER A C   
8390  O O   . SER A 1152 ? 0.3780 0.3646 0.4057 -0.0069 -0.0497 -0.0528 1150 SER A O   
8391  C CB  . SER A 1152 ? 0.4018 0.3891 0.4373 -0.0154 -0.0430 -0.0378 1150 SER A CB  
8392  O OG  . SER A 1152 ? 0.4809 0.4602 0.5107 -0.0122 -0.0429 -0.0402 1150 SER A OG  
8393  N N   . TRP A 1153 ? 0.3982 0.3894 0.4445 -0.0155 -0.0520 -0.0490 1151 TRP A N   
8394  C CA  . TRP A 1153 ? 0.4048 0.3928 0.4558 -0.0150 -0.0567 -0.0552 1151 TRP A CA  
8395  C C   . TRP A 1153 ? 0.4375 0.4186 0.4970 -0.0182 -0.0583 -0.0543 1151 TRP A C   
8396  O O   . TRP A 1153 ? 0.4886 0.4697 0.5543 -0.0226 -0.0569 -0.0479 1151 TRP A O   
8397  C CB  . TRP A 1153 ? 0.3865 0.3815 0.4448 -0.0171 -0.0598 -0.0574 1151 TRP A CB  
8398  C CG  . TRP A 1153 ? 0.3932 0.3942 0.4436 -0.0132 -0.0592 -0.0596 1151 TRP A CG  
8399  C CD1 . TRP A 1153 ? 0.3799 0.3875 0.4271 -0.0129 -0.0562 -0.0558 1151 TRP A CD1 
8400  C CD2 . TRP A 1153 ? 0.3944 0.3962 0.4396 -0.0088 -0.0620 -0.0662 1151 TRP A CD2 
8401  N NE1 . TRP A 1153 ? 0.4126 0.4239 0.4535 -0.0086 -0.0571 -0.0595 1151 TRP A NE1 
8402  C CE2 . TRP A 1153 ? 0.3874 0.3955 0.4267 -0.0062 -0.0606 -0.0655 1151 TRP A CE2 
8403  C CE3 . TRP A 1153 ? 0.3979 0.3961 0.4431 -0.0067 -0.0657 -0.0729 1151 TRP A CE3 
8404  C CZ2 . TRP A 1153 ? 0.4214 0.4321 0.4547 -0.0018 -0.0628 -0.0703 1151 TRP A CZ2 
8405  C CZ3 . TRP A 1153 ? 0.4331 0.4349 0.4717 -0.0024 -0.0677 -0.0781 1151 TRP A CZ3 
8406  C CH2 . TRP A 1153 ? 0.3925 0.4003 0.4252 -0.0001 -0.0663 -0.0763 1151 TRP A CH2 
8407  N N   . SER A 1154 ? 0.4088 0.3843 0.4685 -0.0158 -0.0614 -0.0607 1152 SER A N   
8408  C CA  . SER A 1154 ? 0.4370 0.4049 0.5042 -0.0176 -0.0632 -0.0610 1152 SER A CA  
8409  C C   . SER A 1154 ? 0.4858 0.4516 0.5616 -0.0177 -0.0690 -0.0686 1152 SER A C   
8410  O O   . SER A 1154 ? 0.4461 0.4130 0.5160 -0.0132 -0.0707 -0.0760 1152 SER A O   
8411  C CB  . SER A 1154 ? 0.4444 0.4066 0.5022 -0.0136 -0.0605 -0.0616 1152 SER A CB  
8412  O OG  . SER A 1154 ? 0.4555 0.4104 0.5212 -0.0153 -0.0622 -0.0616 1152 SER A OG  
8413  N N   . LYS A 1155 ? 0.4964 0.4599 0.5866 -0.0228 -0.0722 -0.0667 1153 LYS A N   
8414  C CA  . LYS A 1155 ? 0.5097 0.4694 0.6100 -0.0230 -0.0781 -0.0742 1153 LYS A CA  
8415  C C   . LYS A 1155 ? 0.5299 0.4806 0.6333 -0.0217 -0.0794 -0.0766 1153 LYS A C   
8416  O O   . LYS A 1155 ? 0.6096 0.5575 0.7135 -0.0181 -0.0827 -0.0857 1153 LYS A O   
8417  C CB  . LYS A 1155 ? 0.5090 0.4708 0.6250 -0.0294 -0.0817 -0.0711 1153 LYS A CB  
8418  N N   . ASP A 1156 ? 0.5105 0.4574 0.6160 -0.0243 -0.0767 -0.0689 1154 ASP A N   
8419  C CA  . ASP A 1156 ? 0.5237 0.4620 0.6334 -0.0234 -0.0778 -0.0700 1154 ASP A CA  
8420  C C   . ASP A 1156 ? 0.5045 0.4422 0.5998 -0.0196 -0.0722 -0.0675 1154 ASP A C   
8421  O O   . ASP A 1156 ? 0.4751 0.4131 0.5683 -0.0220 -0.0684 -0.0588 1154 ASP A O   
8422  C CB  . ASP A 1156 ? 0.5153 0.4497 0.6402 -0.0300 -0.0799 -0.0623 1154 ASP A CB  
8423  C CG  . ASP A 1156 ? 0.6290 0.5541 0.7599 -0.0293 -0.0815 -0.0630 1154 ASP A CG  
8424  O OD1 . ASP A 1156 ? 0.6406 0.5627 0.7639 -0.0236 -0.0810 -0.0699 1154 ASP A OD1 
8425  O OD2 . ASP A 1156 ? 0.6433 0.5646 0.7870 -0.0344 -0.0835 -0.0563 1154 ASP A OD2 
8426  N N   . TRP A 1157 ? 0.4716 0.4091 0.5570 -0.0136 -0.0718 -0.0752 1155 TRP A N   
8427  C CA  . TRP A 1157 ? 0.4413 0.3793 0.5125 -0.0098 -0.0665 -0.0729 1155 TRP A CA  
8428  C C   . TRP A 1157 ? 0.4703 0.4021 0.5443 -0.0112 -0.0647 -0.0674 1155 TRP A C   
8429  O O   . TRP A 1157 ? 0.4635 0.3964 0.5299 -0.0114 -0.0599 -0.0608 1155 TRP A O   
8430  C CB  . TRP A 1157 ? 0.4177 0.3568 0.4794 -0.0036 -0.0670 -0.0819 1155 TRP A CB  
8431  C CG  . TRP A 1157 ? 0.4387 0.3844 0.4965 -0.0016 -0.0689 -0.0875 1155 TRP A CG  
8432  C CD1 . TRP A 1157 ? 0.4123 0.3631 0.4723 -0.0043 -0.0695 -0.0849 1155 TRP A CD1 
8433  C CD2 . TRP A 1157 ? 0.3685 0.3173 0.4195 0.0037  -0.0706 -0.0966 1155 TRP A CD2 
8434  N NE1 . TRP A 1157 ? 0.4250 0.3812 0.4802 -0.0010 -0.0717 -0.0919 1155 TRP A NE1 
8435  C CE2 . TRP A 1157 ? 0.4312 0.3866 0.4807 0.0038  -0.0724 -0.0989 1155 TRP A CE2 
8436  C CE3 . TRP A 1157 ? 0.4071 0.3549 0.4534 0.0083  -0.0708 -0.1030 1155 TRP A CE3 
8437  C CZ2 . TRP A 1157 ? 0.4281 0.3888 0.4711 0.0083  -0.0744 -0.1071 1155 TRP A CZ2 
8438  C CZ3 . TRP A 1157 ? 0.3744 0.3281 0.4142 0.0128  -0.0726 -0.1113 1155 TRP A CZ3 
8439  C CH2 . TRP A 1157 ? 0.4377 0.3977 0.4757 0.0127  -0.0745 -0.1132 1155 TRP A CH2 
8440  N N   . ALA A 1158 ? 0.4560 0.3813 0.5416 -0.0122 -0.0686 -0.0704 1156 ALA A N   
8441  C CA  . ALA A 1158 ? 0.4849 0.4042 0.5736 -0.0132 -0.0672 -0.0654 1156 ALA A CA  
8442  C C   . ALA A 1158 ? 0.5013 0.4216 0.5938 -0.0188 -0.0649 -0.0539 1156 ALA A C   
8443  O O   . ALA A 1158 ? 0.5274 0.4454 0.6174 -0.0192 -0.0619 -0.0482 1156 ALA A O   
8444  C CB  . ALA A 1158 ? 0.5497 0.4617 0.6522 -0.0132 -0.0727 -0.0708 1156 ALA A CB  
8445  N N   . ALA A 1159 ? 0.4825 0.4074 0.5807 -0.0232 -0.0661 -0.0503 1157 ALA A N   
8446  C CA  . ALA A 1159 ? 0.5477 0.4755 0.6499 -0.0287 -0.0639 -0.0394 1157 ALA A CA  
8447  C C   . ALA A 1159 ? 0.5313 0.4660 0.6199 -0.0276 -0.0580 -0.0350 1157 ALA A C   
8448  O O   . ALA A 1159 ? 0.5587 0.4956 0.6470 -0.0306 -0.0550 -0.0265 1157 ALA A O   
8449  C CB  . ALA A 1159 ? 0.5282 0.4593 0.6431 -0.0342 -0.0677 -0.0371 1157 ALA A CB  
8450  N N   . ASP A 1160 ? 0.5450 0.4835 0.6228 -0.0233 -0.0565 -0.0405 1158 ASP A N   
8451  C CA  . ASP A 1160 ? 0.4979 0.4430 0.5642 -0.0221 -0.0518 -0.0371 1158 ASP A CA  
8452  C C   . ASP A 1160 ? 0.4845 0.4272 0.5384 -0.0174 -0.0480 -0.0379 1158 ASP A C   
8453  O O   . ASP A 1160 ? 0.5205 0.4678 0.5644 -0.0155 -0.0445 -0.0364 1158 ASP A O   
8454  C CB  . ASP A 1160 ? 0.5008 0.4519 0.5641 -0.0207 -0.0529 -0.0417 1158 ASP A CB  
8455  C CG  . ASP A 1160 ? 0.5484 0.5030 0.6240 -0.0257 -0.0562 -0.0402 1158 ASP A CG  
8456  O OD1 . ASP A 1160 ? 0.5620 0.5173 0.6460 -0.0308 -0.0561 -0.0330 1158 ASP A OD1 
8457  O OD2 . ASP A 1160 ? 0.5308 0.4880 0.6080 -0.0247 -0.0592 -0.0459 1158 ASP A OD2 
8458  N N   . GLY A 1161 ? 0.4678 0.4037 0.5229 -0.0157 -0.0487 -0.0400 1159 GLY A N   
8459  C CA  . GLY A 1161 ? 0.4488 0.3826 0.4932 -0.0116 -0.0453 -0.0404 1159 GLY A CA  
8460  C C   . GLY A 1161 ? 0.5049 0.4383 0.5483 -0.0139 -0.0417 -0.0323 1159 GLY A C   
8461  O O   . GLY A 1161 ? 0.5194 0.4553 0.5691 -0.0186 -0.0416 -0.0258 1159 GLY A O   
8462  N N   . PRO A 1162 ? 0.4525 0.3833 0.4877 -0.0106 -0.0389 -0.0323 1160 PRO A N   
8463  C CA  . PRO A 1162 ? 0.4481 0.3771 0.4754 -0.0052 -0.0386 -0.0389 1160 PRO A CA  
8464  C C   . PRO A 1162 ? 0.4541 0.3885 0.4706 -0.0023 -0.0368 -0.0409 1160 PRO A C   
8465  O O   . PRO A 1162 ? 0.4595 0.3981 0.4720 -0.0035 -0.0343 -0.0364 1160 PRO A O   
8466  C CB  . PRO A 1162 ? 0.4594 0.3848 0.4830 -0.0041 -0.0357 -0.0358 1160 PRO A CB  
8467  C CG  . PRO A 1162 ? 0.4902 0.4183 0.5135 -0.0076 -0.0328 -0.0274 1160 PRO A CG  
8468  C CD  . PRO A 1162 ? 0.4777 0.4084 0.5109 -0.0123 -0.0354 -0.0249 1160 PRO A CD  
8469  N N   . PHE A 1163 ? 0.3859 0.3208 0.3980 0.0017  -0.0382 -0.0479 1161 PHE A N   
8470  C CA  . PHE A 1163 ? 0.3352 0.2749 0.3368 0.0049  -0.0367 -0.0493 1161 PHE A CA  
8471  C C   . PHE A 1163 ? 0.3833 0.3221 0.3752 0.0084  -0.0335 -0.0487 1161 PHE A C   
8472  O O   . PHE A 1163 ? 0.4272 0.3620 0.4205 0.0088  -0.0327 -0.0486 1161 PHE A O   
8473  C CB  . PHE A 1163 ? 0.3547 0.2971 0.3570 0.0069  -0.0404 -0.0567 1161 PHE A CB  
8474  C CG  . PHE A 1163 ? 0.3723 0.3158 0.3849 0.0032  -0.0437 -0.0572 1161 PHE A CG  
8475  C CD1 . PHE A 1163 ? 0.3614 0.3086 0.3749 0.0003  -0.0425 -0.0522 1161 PHE A CD1 
8476  C CD2 . PHE A 1163 ? 0.3869 0.3279 0.4088 0.0025  -0.0480 -0.0628 1161 PHE A CD2 
8477  C CE1 . PHE A 1163 ? 0.4061 0.3553 0.4294 -0.0034 -0.0454 -0.0521 1161 PHE A CE1 
8478  C CE2 . PHE A 1163 ? 0.3755 0.3175 0.4076 -0.0012 -0.0513 -0.0628 1161 PHE A CE2 
8479  C CZ  . PHE A 1163 ? 0.4109 0.3573 0.4435 -0.0044 -0.0498 -0.0571 1161 PHE A CZ  
8480  N N   . ALA A 1164 ? 0.3707 0.3134 0.3532 0.0107  -0.0316 -0.0479 1162 ALA A N   
8481  C CA  . ALA A 1164 ? 0.3915 0.3341 0.3649 0.0138  -0.0287 -0.0466 1162 ALA A CA  
8482  C C   . ALA A 1164 ? 0.3643 0.3109 0.3304 0.0179  -0.0297 -0.0515 1162 ALA A C   
8483  O O   . ALA A 1164 ? 0.3780 0.3261 0.3361 0.0203  -0.0273 -0.0498 1162 ALA A O   
8484  C CB  . ALA A 1164 ? 0.3723 0.3158 0.3410 0.0129  -0.0254 -0.0401 1162 ALA A CB  
8485  N N   . GLY A 1165 ? 0.3424 0.2916 0.3116 0.0185  -0.0332 -0.0572 1163 GLY A N   
8486  C CA  . GLY A 1165 ? 0.3542 0.3087 0.3167 0.0222  -0.0345 -0.0619 1163 GLY A CA  
8487  C C   . GLY A 1165 ? 0.3919 0.3493 0.3590 0.0216  -0.0384 -0.0663 1163 GLY A C   
8488  O O   . GLY A 1165 ? 0.3391 0.2946 0.3142 0.0182  -0.0397 -0.0650 1163 GLY A O   
8489  N N   . ALA A 1166 ? 0.3339 0.2969 0.2960 0.0249  -0.0403 -0.0715 1164 ALA A N   
8490  C CA  . ALA A 1166 ? 0.3078 0.2742 0.2741 0.0246  -0.0443 -0.0764 1164 ALA A CA  
8491  C C   . ALA A 1166 ? 0.3645 0.3385 0.3218 0.0281  -0.0452 -0.0782 1164 ALA A C   
8492  O O   . ALA A 1166 ? 0.3878 0.3650 0.3367 0.0312  -0.0436 -0.0782 1164 ALA A O   
8493  C CB  . ALA A 1166 ? 0.3651 0.3298 0.3398 0.0245  -0.0479 -0.0842 1164 ALA A CB  
8494  N N   . LEU A 1167 ? 0.2902 0.2676 0.2494 0.0275  -0.0478 -0.0793 1165 LEU A N   
8495  C CA  . LEU A 1167 ? 0.3426 0.3277 0.2948 0.0306  -0.0496 -0.0816 1165 LEU A CA  
8496  C C   . LEU A 1167 ? 0.3335 0.3217 0.2920 0.0305  -0.0543 -0.0894 1165 LEU A C   
8497  O O   . LEU A 1167 ? 0.3679 0.3535 0.3355 0.0273  -0.0560 -0.0897 1165 LEU A O   
8498  C CB  . LEU A 1167 ? 0.3666 0.3534 0.3152 0.0303  -0.0485 -0.0751 1165 LEU A CB  
8499  C CG  . LEU A 1167 ? 0.3861 0.3693 0.3297 0.0301  -0.0442 -0.0673 1165 LEU A CG  
8500  C CD1 . LEU A 1167 ? 0.2968 0.2811 0.2394 0.0297  -0.0438 -0.0619 1165 LEU A CD1 
8501  C CD2 . LEU A 1167 ? 0.3188 0.3050 0.2532 0.0333  -0.0427 -0.0667 1165 LEU A CD2 
8502  N N   . VAL A 1168 ? 0.3003 0.2948 0.2545 0.0339  -0.0565 -0.0959 1166 VAL A N   
8503  C CA  . VAL A 1168 ? 0.3326 0.3304 0.2928 0.0342  -0.0613 -0.1047 1166 VAL A CA  
8504  C C   . VAL A 1168 ? 0.3502 0.3578 0.3028 0.0373  -0.0635 -0.1068 1166 VAL A C   
8505  O O   . VAL A 1168 ? 0.3481 0.3610 0.2903 0.0403  -0.0617 -0.1047 1166 VAL A O   
8506  C CB  . VAL A 1168 ? 0.3305 0.3274 0.2944 0.0356  -0.0628 -0.1127 1166 VAL A CB  
8507  C CG1 . VAL A 1168 ? 0.3585 0.3580 0.3307 0.0356  -0.0683 -0.1223 1166 VAL A CG1 
8508  C CG2 . VAL A 1168 ? 0.3124 0.2996 0.2828 0.0330  -0.0604 -0.1095 1166 VAL A CG2 
8509  N N   . GLU A 1169 ? 0.3274 0.3377 0.2856 0.0363  -0.0674 -0.1107 1167 GLU A N   
8510  C CA  . GLU A 1169 ? 0.3312 0.3513 0.2838 0.0392  -0.0705 -0.1143 1167 GLU A CA  
8511  C C   . GLU A 1169 ? 0.3653 0.3889 0.3244 0.0399  -0.0754 -0.1253 1167 GLU A C   
8512  O O   . GLU A 1169 ? 0.3444 0.3629 0.3151 0.0367  -0.0777 -0.1283 1167 GLU A O   
8513  C CB  . GLU A 1169 ? 0.3517 0.3730 0.3052 0.0377  -0.0711 -0.1091 1167 GLU A CB  
8514  C CG  . GLU A 1169 ? 0.3306 0.3620 0.2789 0.0405  -0.0746 -0.1120 1167 GLU A CG  
8515  C CD  . GLU A 1169 ? 0.4074 0.4396 0.3599 0.0388  -0.0762 -0.1087 1167 GLU A CD  
8516  O OE1 . GLU A 1169 ? 0.3980 0.4236 0.3584 0.0352  -0.0748 -0.1053 1167 GLU A OE1 
8517  O OE2 . GLU A 1169 ? 0.4064 0.4465 0.3545 0.0410  -0.0788 -0.1094 1167 GLU A OE2 
8518  N N   . GLY A 1170 ? 0.3415 0.3743 0.2936 0.0439  -0.0771 -0.1314 1168 GLY A N   
8519  C CA  . GLY A 1170 ? 0.3776 0.4149 0.3357 0.0449  -0.0823 -0.1426 1168 GLY A CA  
8520  C C   . GLY A 1170 ? 0.3827 0.4313 0.3313 0.0497  -0.0833 -0.1489 1168 GLY A C   
8521  O O   . GLY A 1170 ? 0.3794 0.4321 0.3172 0.0520  -0.0798 -0.1441 1168 GLY A O   
8522  N N   . ASP A 1171 ? 0.4000 0.4543 0.3532 0.0512  -0.0883 -0.1599 1169 ASP A N   
8523  C CA  . ASP A 1171 ? 0.3857 0.4513 0.3316 0.0559  -0.0896 -0.1680 1169 ASP A CA  
8524  C C   . ASP A 1171 ? 0.4127 0.4738 0.3617 0.0568  -0.0878 -0.1723 1169 ASP A C   
8525  O O   . ASP A 1171 ? 0.3681 0.4170 0.3252 0.0536  -0.0859 -0.1688 1169 ASP A O   
8526  C CB  . ASP A 1171 ? 0.4522 0.5263 0.4021 0.0574  -0.0957 -0.1791 1169 ASP A CB  
8527  C CG  . ASP A 1171 ? 0.5081 0.5741 0.4744 0.0549  -0.0999 -0.1877 1169 ASP A CG  
8528  O OD1 . ASP A 1171 ? 0.4638 0.5194 0.4378 0.0530  -0.0985 -0.1876 1169 ASP A OD1 
8529  O OD2 . ASP A 1171 ? 0.5592 0.6294 0.5311 0.0548  -0.1051 -0.1946 1169 ASP A OD2 
8530  N N   . ALA A 1172 ? 0.3834 0.4552 0.3261 0.0612  -0.0884 -0.1800 1170 ALA A N   
8531  C CA  . ALA A 1172 ? 0.4169 0.4863 0.3605 0.0628  -0.0861 -0.1835 1170 ALA A CA  
8532  C C   . ALA A 1172 ? 0.3893 0.4469 0.3490 0.0606  -0.0888 -0.1900 1170 ALA A C   
8533  O O   . ALA A 1172 ? 0.4187 0.4665 0.3827 0.0589  -0.0859 -0.1862 1170 ALA A O   
8534  C CB  . ALA A 1172 ? 0.3968 0.4819 0.3320 0.0682  -0.0870 -0.1926 1170 ALA A CB  
8535  N N   . GLU A 1173 ? 0.4250 0.4835 0.3943 0.0603  -0.0947 -0.1996 1171 GLU A N   
8536  C CA  . GLU A 1173 ? 0.4451 0.4927 0.4310 0.0580  -0.0981 -0.2060 1171 GLU A CA  
8537  C C   . GLU A 1173 ? 0.4106 0.4438 0.4046 0.0522  -0.0962 -0.1952 1171 GLU A C   
8538  O O   . GLU A 1173 ? 0.4117 0.4343 0.4159 0.0501  -0.0961 -0.1950 1171 GLU A O   
8539  C CB  . GLU A 1173 ? 0.4627 0.5150 0.4574 0.0588  -0.1052 -0.2184 1171 GLU A CB  
8540  N N   . ARG A 1174 ? 0.3560 0.3894 0.3456 0.0497  -0.0948 -0.1862 1172 ARG A N   
8541  C CA  . ARG A 1174 ? 0.3842 0.4061 0.3803 0.0444  -0.0925 -0.1757 1172 ARG A CA  
8542  C C   . ARG A 1174 ? 0.3962 0.4121 0.3871 0.0440  -0.0867 -0.1671 1172 ARG A C   
8543  O O   . ARG A 1174 ? 0.3935 0.3987 0.3932 0.0403  -0.0855 -0.1625 1172 ARG A O   
8544  C CB  . ARG A 1174 ? 0.3912 0.4164 0.3828 0.0425  -0.0922 -0.1687 1172 ARG A CB  
8545  C CG  . ARG A 1174 ? 0.3826 0.3984 0.3785 0.0376  -0.0891 -0.1574 1172 ARG A CG  
8546  C CD  . ARG A 1174 ? 0.4433 0.4508 0.4560 0.0331  -0.0926 -0.1596 1172 ARG A CD  
8547  N NE  . ARG A 1174 ? 0.3962 0.3964 0.4132 0.0282  -0.0896 -0.1489 1172 ARG A NE  
8548  C CZ  . ARG A 1174 ? 0.4397 0.4312 0.4698 0.0238  -0.0906 -0.1471 1172 ARG A CZ  
8549  N NH1 . ARG A 1174 ? 0.3896 0.3770 0.4306 0.0235  -0.0946 -0.1549 1172 ARG A NH1 
8550  N NH2 . ARG A 1174 ? 0.3518 0.3390 0.3845 0.0196  -0.0877 -0.1372 1172 ARG A NH2 
8551  N N   . ILE A 1175 ? 0.3945 0.4178 0.3715 0.0475  -0.0830 -0.1646 1173 ILE A N   
8552  C CA  . ILE A 1175 ? 0.3597 0.3782 0.3314 0.0473  -0.0775 -0.1567 1173 ILE A CA  
8553  C C   . ILE A 1175 ? 0.3843 0.3971 0.3639 0.0480  -0.0779 -0.1625 1173 ILE A C   
8554  O O   . ILE A 1175 ? 0.3623 0.3653 0.3467 0.0453  -0.0754 -0.1565 1173 ILE A O   
8555  C CB  . ILE A 1175 ? 0.3625 0.3912 0.3183 0.0510  -0.0741 -0.1530 1173 ILE A CB  
8556  C CG1 . ILE A 1175 ? 0.4080 0.4395 0.3570 0.0498  -0.0731 -0.1446 1173 ILE A CG1 
8557  C CG2 . ILE A 1175 ? 0.3885 0.4132 0.3400 0.0513  -0.0690 -0.1473 1173 ILE A CG2 
8558  C CD1 . ILE A 1175 ? 0.4075 0.4510 0.3420 0.0534  -0.0714 -0.1418 1173 ILE A CD1 
8559  N N   . ARG A 1176 ? 0.3828 0.4022 0.3640 0.0518  -0.0813 -0.1746 1174 ARG A N   
8560  C CA  . ARG A 1176 ? 0.3654 0.3796 0.3556 0.0528  -0.0825 -0.1814 1174 ARG A CA  
8561  C C   . ARG A 1176 ? 0.3670 0.3679 0.3738 0.0481  -0.0853 -0.1804 1174 ARG A C   
8562  O O   . ARG A 1176 ? 0.3707 0.3625 0.3834 0.0465  -0.0836 -0.1770 1174 ARG A O   
8563  C CB  . ARG A 1176 ? 0.3942 0.4186 0.3850 0.0578  -0.0867 -0.1960 1174 ARG A CB  
8564  C CG  . ARG A 1176 ? 0.4304 0.4522 0.4270 0.0604  -0.0868 -0.2032 1174 ARG A CG  
8565  C CD  . ARG A 1176 ? 0.4776 0.5069 0.4804 0.0646  -0.0925 -0.2196 1174 ARG A CD  
8566  N NE  . ARG A 1176 ? 0.5267 0.5723 0.5171 0.0685  -0.0930 -0.2245 1174 ARG A NE  
8567  C CZ  . ARG A 1176 ? 0.5374 0.5960 0.5163 0.0728  -0.0895 -0.2255 1174 ARG A CZ  
8568  N NH1 . ARG A 1176 ? 0.5049 0.5621 0.4820 0.0745  -0.0860 -0.2245 1174 ARG A NH1 
8569  N NH2 . ARG A 1176 ? 0.4617 0.5354 0.4311 0.0754  -0.0897 -0.2270 1174 ARG A NH2 
8570  N N   . ALA A 1177 ? 0.3814 0.3813 0.3957 0.0455  -0.0895 -0.1824 1175 ALA A N   
8571  C CA  . ALA A 1177 ? 0.4085 0.3969 0.4390 0.0405  -0.0925 -0.1806 1175 ALA A CA  
8572  C C   . ALA A 1177 ? 0.3659 0.3458 0.3959 0.0360  -0.0877 -0.1667 1175 ALA A C   
8573  O O   . ALA A 1177 ? 0.3698 0.3400 0.4102 0.0331  -0.0879 -0.1638 1175 ALA A O   
8574  C CB  . ALA A 1177 ? 0.3662 0.3569 0.4034 0.0384  -0.0974 -0.1843 1175 ALA A CB  
8575  N N   . VAL A 1178 ? 0.3349 0.3188 0.3535 0.0354  -0.0838 -0.1582 1176 VAL A N   
8576  C CA  . VAL A 1178 ? 0.3520 0.3292 0.3694 0.0315  -0.0793 -0.1457 1176 VAL A CA  
8577  C C   . VAL A 1178 ? 0.3857 0.3590 0.3994 0.0328  -0.0751 -0.1424 1176 VAL A C   
8578  O O   . VAL A 1178 ? 0.3827 0.3475 0.4026 0.0294  -0.0734 -0.1358 1176 VAL A O   
8579  C CB  . VAL A 1178 ? 0.3611 0.3441 0.3674 0.0314  -0.0764 -0.1385 1176 VAL A CB  
8580  C CG1 . VAL A 1178 ? 0.3179 0.2955 0.3210 0.0285  -0.0711 -0.1265 1176 VAL A CG1 
8581  C CG2 . VAL A 1178 ? 0.3702 0.3559 0.3821 0.0292  -0.0803 -0.1403 1176 VAL A CG2 
8582  N N   . ASN A 1179 ? 0.3614 0.3416 0.3649 0.0378  -0.0735 -0.1467 1177 ASN A N   
8583  C CA  . ASN A 1179 ? 0.3620 0.3399 0.3613 0.0393  -0.0695 -0.1438 1177 ASN A CA  
8584  C C   . ASN A 1179 ? 0.3886 0.3578 0.4014 0.0383  -0.0719 -0.1479 1177 ASN A C   
8585  O O   . ASN A 1179 ? 0.3887 0.3511 0.4033 0.0367  -0.0689 -0.1414 1177 ASN A O   
8586  C CB  . ASN A 1179 ? 0.3840 0.3729 0.3711 0.0449  -0.0681 -0.1491 1177 ASN A CB  
8587  C CG  . ASN A 1179 ? 0.4633 0.4523 0.4414 0.0461  -0.0625 -0.1425 1177 ASN A CG  
8588  O OD1 . ASN A 1179 ? 0.4595 0.4421 0.4365 0.0430  -0.0590 -0.1323 1177 ASN A OD1 
8589  N ND2 . ASN A 1179 ? 0.4878 0.4851 0.4595 0.0507  -0.0617 -0.1485 1177 ASN A ND2 
8590  N N   . LYS A 1180 ? 0.3658 0.3349 0.3892 0.0392  -0.0776 -0.1584 1178 LYS A N   
8591  C CA  . LYS A 1180 ? 0.4012 0.3614 0.4396 0.0380  -0.0808 -0.1623 1178 LYS A CA  
8592  C C   . LYS A 1180 ? 0.4195 0.3693 0.4684 0.0317  -0.0811 -0.1529 1178 LYS A C   
8593  O O   . LYS A 1180 ? 0.4389 0.3807 0.4950 0.0300  -0.0804 -0.1491 1178 LYS A O   
8594  C CB  . LYS A 1180 ? 0.4319 0.3948 0.4798 0.0404  -0.0875 -0.1762 1178 LYS A CB  
8595  C CG  . LYS A 1180 ? 0.4187 0.3925 0.4580 0.0470  -0.0875 -0.1869 1178 LYS A CG  
8596  C CD  . LYS A 1180 ? 0.3963 0.3753 0.4431 0.0494  -0.0942 -0.2007 1178 LYS A CD  
8597  C CE  . LYS A 1180 ? 0.5902 0.5609 0.6549 0.0495  -0.0995 -0.2094 1178 LYS A CE  
8598  N NZ  . LYS A 1180 ? 0.6470 0.6212 0.7216 0.0509  -0.1067 -0.2223 1178 LYS A NZ  
8599  N N   . ALA A 1181 ? 0.3882 0.3390 0.4382 0.0282  -0.0820 -0.1488 1179 ALA A N   
8600  C CA  . ALA A 1181 ? 0.4137 0.3567 0.4726 0.0220  -0.0818 -0.1392 1179 ALA A CA  
8601  C C   . ALA A 1181 ? 0.4024 0.3429 0.4534 0.0206  -0.0755 -0.1277 1179 ALA A C   
8602  O O   . ALA A 1181 ? 0.3592 0.2923 0.4183 0.0166  -0.0750 -0.1209 1179 ALA A O   
8603  C CB  . ALA A 1181 ? 0.3395 0.2860 0.3998 0.0190  -0.0836 -0.1373 1179 ALA A CB  
8604  N N   . ILE A 1182 ? 0.3710 0.3178 0.4065 0.0236  -0.0710 -0.1252 1180 ILE A N   
8605  C CA  . ILE A 1182 ? 0.4019 0.3464 0.4300 0.0224  -0.0653 -0.1150 1180 ILE A CA  
8606  C C   . ILE A 1182 ? 0.4058 0.3452 0.4367 0.0238  -0.0641 -0.1156 1180 ILE A C   
8607  O O   . ILE A 1182 ? 0.3795 0.3131 0.4133 0.0208  -0.0617 -0.1077 1180 ILE A O   
8608  C CB  . ILE A 1182 ? 0.4193 0.3716 0.4313 0.0252  -0.0613 -0.1123 1180 ILE A CB  
8609  C CG1 . ILE A 1182 ? 0.4156 0.3716 0.4258 0.0232  -0.0620 -0.1095 1180 ILE A CG1 
8610  C CG2 . ILE A 1182 ? 0.4245 0.3745 0.4290 0.0249  -0.0557 -0.1036 1180 ILE A CG2 
8611  C CD1 . ILE A 1182 ? 0.3967 0.3602 0.3924 0.0261  -0.0590 -0.1069 1180 ILE A CD1 
8612  N N   . ALA A 1183 ? 0.4000 0.3423 0.4302 0.0284  -0.0659 -0.1253 1181 ALA A N   
8613  C CA  . ALA A 1183 ? 0.4494 0.3875 0.4830 0.0301  -0.0651 -0.1268 1181 ALA A CA  
8614  C C   . ALA A 1183 ? 0.4294 0.3574 0.4795 0.0262  -0.0685 -0.1250 1181 ALA A C   
8615  O O   . ALA A 1183 ? 0.4603 0.3830 0.5135 0.0259  -0.0669 -0.1214 1181 ALA A O   
8616  C CB  . ALA A 1183 ? 0.3834 0.3277 0.4149 0.0359  -0.0671 -0.1389 1181 ALA A CB  
8617  N N   . ALA A 1184 ? 0.4464 0.3719 0.5076 0.0231  -0.0732 -0.1269 1182 ALA A N   
8618  C CA  . ALA A 1184 ? 0.4445 0.3607 0.5225 0.0189  -0.0769 -0.1244 1182 ALA A CA  
8619  C C   . ALA A 1184 ? 0.4631 0.3754 0.5421 0.0131  -0.0739 -0.1110 1182 ALA A C   
8620  O O   . ALA A 1184 ? 0.4713 0.3766 0.5637 0.0091  -0.0765 -0.1069 1182 ALA A O   
8621  C CB  . ALA A 1184 ? 0.4523 0.3675 0.5430 0.0175  -0.0836 -0.1318 1182 ALA A CB  
8622  N N   . LEU A 1185 ? 0.4312 0.3486 0.4972 0.0126  -0.0688 -0.1043 1183 LEU A N   
8623  C CA  . LEU A 1185 ? 0.4412 0.3564 0.5075 0.0077  -0.0657 -0.0923 1183 LEU A CA  
8624  C C   . LEU A 1185 ? 0.4722 0.3822 0.5391 0.0075  -0.0631 -0.0871 1183 LEU A C   
8625  O O   . LEU A 1185 ? 0.4251 0.3365 0.4833 0.0118  -0.0604 -0.0897 1183 LEU A O   
8626  C CB  . LEU A 1185 ? 0.4386 0.3604 0.4910 0.0079  -0.0612 -0.0875 1183 LEU A CB  
8627  C CG  . LEU A 1185 ? 0.4298 0.3575 0.4803 0.0080  -0.0632 -0.0912 1183 LEU A CG  
8628  C CD1 . LEU A 1185 ? 0.3942 0.3278 0.4307 0.0089  -0.0586 -0.0862 1183 LEU A CD1 
8629  C CD2 . LEU A 1185 ? 0.4549 0.3804 0.5189 0.0026  -0.0670 -0.0890 1183 LEU A CD2 
8630  N N   . PRO A 1186 ? 0.4913 0.3959 0.5683 0.0027  -0.0639 -0.0795 1184 PRO A N   
8631  C CA  . PRO A 1186 ? 0.4489 0.3492 0.5265 0.0024  -0.0615 -0.0740 1184 PRO A CA  
8632  C C   . PRO A 1186 ? 0.3968 0.3012 0.4598 0.0029  -0.0551 -0.0671 1184 PRO A C   
8633  O O   . PRO A 1186 ? 0.4205 0.3300 0.4760 0.0018  -0.0527 -0.0640 1184 PRO A O   
8634  C CB  . PRO A 1186 ? 0.5777 0.4729 0.6698 -0.0036 -0.0643 -0.0665 1184 PRO A CB  
8635  C CG  . PRO A 1186 ? 0.6183 0.5180 0.7110 -0.0073 -0.0649 -0.0640 1184 PRO A CG  
8636  C CD  . PRO A 1186 ? 0.5337 0.4373 0.6216 -0.0031 -0.0667 -0.0746 1184 PRO A CD  
8637  N N   . GLY A 1187 ? 0.4410 0.3431 0.5009 0.0047  -0.0525 -0.0651 1185 GLY A N   
8638  C CA  . GLY A 1187 ? 0.4384 0.3435 0.4861 0.0050  -0.0467 -0.0585 1185 GLY A CA  
8639  C C   . GLY A 1187 ? 0.4334 0.3431 0.4679 0.0103  -0.0438 -0.0635 1185 GLY A C   
8640  O O   . GLY A 1187 ? 0.4302 0.3398 0.4648 0.0143  -0.0451 -0.0710 1185 GLY A O   
8641  N N   . PRO A 1188 ? 0.4133 0.3278 0.4364 0.0103  -0.0399 -0.0593 1186 PRO A N   
8642  C CA  . PRO A 1188 ? 0.3689 0.2878 0.3794 0.0147  -0.0367 -0.0617 1186 PRO A CA  
8643  C C   . PRO A 1188 ? 0.4137 0.3370 0.4213 0.0185  -0.0390 -0.0708 1186 PRO A C   
8644  O O   . PRO A 1188 ? 0.3562 0.2807 0.3683 0.0175  -0.0424 -0.0743 1186 PRO A O   
8645  C CB  . PRO A 1188 ? 0.4465 0.3688 0.4483 0.0131  -0.0330 -0.0546 1186 PRO A CB  
8646  C CG  . PRO A 1188 ? 0.4631 0.3853 0.4719 0.0090  -0.0353 -0.0523 1186 PRO A CG  
8647  C CD  . PRO A 1188 ? 0.4076 0.3242 0.4298 0.0063  -0.0386 -0.0523 1186 PRO A CD  
8648  N N   . LEU A 1189 ? 0.3755 0.3023 0.3754 0.0228  -0.0373 -0.0746 1187 LEU A N   
8649  C CA  . LEU A 1189 ? 0.3848 0.3182 0.3793 0.0268  -0.0387 -0.0827 1187 LEU A CA  
8650  C C   . LEU A 1189 ? 0.4156 0.3544 0.3999 0.0267  -0.0367 -0.0790 1187 LEU A C   
8651  O O   . LEU A 1189 ? 0.5187 0.4592 0.4944 0.0270  -0.0327 -0.0731 1187 LEU A O   
8652  C CB  . LEU A 1189 ? 0.4401 0.3769 0.4297 0.0312  -0.0372 -0.0873 1187 LEU A CB  
8653  C CG  . LEU A 1189 ? 0.5143 0.4482 0.5138 0.0332  -0.0403 -0.0949 1187 LEU A CG  
8654  C CD1 . LEU A 1189 ? 0.4650 0.3899 0.4746 0.0300  -0.0406 -0.0898 1187 LEU A CD1 
8655  C CD2 . LEU A 1189 ? 0.4879 0.4283 0.4803 0.0381  -0.0383 -0.0999 1187 LEU A CD2 
8656  N N   . LEU A 1190 ? 0.3908 0.3323 0.3766 0.0263  -0.0396 -0.0823 1188 LEU A N   
8657  C CA  . LEU A 1190 ? 0.3931 0.3392 0.3707 0.0260  -0.0382 -0.0784 1188 LEU A CA  
8658  C C   . LEU A 1190 ? 0.3834 0.3374 0.3499 0.0303  -0.0371 -0.0816 1188 LEU A C   
8659  O O   . LEU A 1190 ? 0.3871 0.3453 0.3537 0.0334  -0.0394 -0.0896 1188 LEU A O   
8660  C CB  . LEU A 1190 ? 0.4159 0.3625 0.3996 0.0237  -0.0417 -0.0803 1188 LEU A CB  
8661  C CG  . LEU A 1190 ? 0.4430 0.3836 0.4375 0.0188  -0.0428 -0.0759 1188 LEU A CG  
8662  C CD1 . LEU A 1190 ? 0.4391 0.3823 0.4373 0.0168  -0.0456 -0.0770 1188 LEU A CD1 
8663  C CD2 . LEU A 1190 ? 0.4249 0.3631 0.4161 0.0166  -0.0385 -0.0667 1188 LEU A CD2 
8664  N N   . LEU A 1191 ? 0.3918 0.3484 0.3491 0.0305  -0.0339 -0.0751 1189 LEU A N   
8665  C CA  . LEU A 1191 ? 0.3936 0.3584 0.3405 0.0339  -0.0333 -0.0764 1189 LEU A CA  
8666  C C   . LEU A 1191 ? 0.3818 0.3504 0.3290 0.0338  -0.0365 -0.0788 1189 LEU A C   
8667  O O   . LEU A 1191 ? 0.3643 0.3310 0.3123 0.0314  -0.0362 -0.0738 1189 LEU A O   
8668  C CB  . LEU A 1191 ? 0.3787 0.3442 0.3173 0.0340  -0.0292 -0.0682 1189 LEU A CB  
8669  C CG  . LEU A 1191 ? 0.4038 0.3775 0.3318 0.0373  -0.0278 -0.0677 1189 LEU A CG  
8670  C CD1 . LEU A 1191 ? 0.3984 0.3703 0.3210 0.0365  -0.0239 -0.0590 1189 LEU A CD1 
8671  C CD2 . LEU A 1191 ? 0.3522 0.3326 0.2757 0.0387  -0.0302 -0.0692 1189 LEU A CD2 
8672  N N   . VAL A 1192 ? 0.3899 0.3643 0.3370 0.0364  -0.0395 -0.0871 1190 VAL A N   
8673  C CA  . VAL A 1192 ? 0.3662 0.3447 0.3146 0.0366  -0.0432 -0.0911 1190 VAL A CA  
8674  C C   . VAL A 1192 ? 0.3756 0.3637 0.3128 0.0398  -0.0429 -0.0908 1190 VAL A C   
8675  O O   . VAL A 1192 ? 0.4027 0.3968 0.3335 0.0429  -0.0419 -0.0933 1190 VAL A O   
8676  C CB  . VAL A 1192 ? 0.3801 0.3586 0.3371 0.0373  -0.0475 -0.1012 1190 VAL A CB  
8677  C CG1 . VAL A 1192 ? 0.3646 0.3482 0.3228 0.0376  -0.0515 -0.1058 1190 VAL A CG1 
8678  C CG2 . VAL A 1192 ? 0.3598 0.3287 0.3292 0.0338  -0.0484 -0.1008 1190 VAL A CG2 
8679  N N   . GLN A 1193 ? 0.3640 0.3545 0.2992 0.0391  -0.0441 -0.0879 1191 GLN A N   
8680  C CA  . GLN A 1193 ? 0.3013 0.3012 0.2273 0.0419  -0.0449 -0.0878 1191 GLN A CA  
8681  C C   . GLN A 1193 ? 0.3324 0.3365 0.2618 0.0422  -0.0494 -0.0938 1191 GLN A C   
8682  O O   . GLN A 1193 ? 0.3424 0.3418 0.2791 0.0394  -0.0510 -0.0931 1191 GLN A O   
8683  C CB  . GLN A 1193 ? 0.3666 0.3663 0.2865 0.0413  -0.0424 -0.0781 1191 GLN A CB  
8684  C CG  . GLN A 1193 ? 0.3709 0.3666 0.2874 0.0409  -0.0380 -0.0717 1191 GLN A CG  
8685  C CD  . GLN A 1193 ? 0.4080 0.4046 0.3184 0.0408  -0.0364 -0.0630 1191 GLN A CD  
8686  O OE1 . GLN A 1193 ? 0.4278 0.4320 0.3307 0.0431  -0.0368 -0.0614 1191 GLN A OE1 
8687  N NE2 . GLN A 1193 ? 0.3947 0.3840 0.3089 0.0382  -0.0348 -0.0575 1191 GLN A NE2 
8688  N N   . ALA A 1194 ? 0.3258 0.3397 0.2498 0.0456  -0.0515 -0.0995 1192 ALA A N   
8689  C CA  . ALA A 1194 ? 0.3559 0.3748 0.2830 0.0462  -0.0561 -0.1065 1192 ALA A CA  
8690  C C   . ALA A 1194 ? 0.3962 0.4258 0.3134 0.0489  -0.0571 -0.1047 1192 ALA A C   
8691  O O   . ALA A 1194 ? 0.3589 0.3943 0.2668 0.0511  -0.0547 -0.1010 1192 ALA A O   
8692  C CB  . ALA A 1194 ? 0.3631 0.3843 0.2953 0.0479  -0.0590 -0.1178 1192 ALA A CB  
8693  N N   . ALA A 1195 ? 0.3422 0.3747 0.2618 0.0486  -0.0606 -0.1068 1193 ALA A N   
8694  C CA  . ALA A 1195 ? 0.3684 0.4114 0.2798 0.0510  -0.0624 -0.1055 1193 ALA A CA  
8695  C C   . ALA A 1195 ? 0.4013 0.4481 0.3181 0.0510  -0.0674 -0.1129 1193 ALA A C   
8696  O O   . ALA A 1195 ? 0.4041 0.4437 0.3312 0.0482  -0.0689 -0.1153 1193 ALA A O   
8697  C CB  . ALA A 1195 ? 0.3541 0.3950 0.2612 0.0501  -0.0603 -0.0944 1193 ALA A CB  
8698  N N   . SER A 1196 ? 0.3605 0.4192 0.2706 0.0541  -0.0701 -0.1162 1194 SER A N   
8699  C CA  . SER A 1196 ? 0.3939 0.4572 0.3083 0.0543  -0.0750 -0.1225 1194 SER A CA  
8700  C C   . SER A 1196 ? 0.3814 0.4430 0.2962 0.0528  -0.0755 -0.1149 1194 SER A C   
8701  O O   . SER A 1196 ? 0.3769 0.4361 0.2869 0.0525  -0.0725 -0.1053 1194 SER A O   
8702  C CB  . SER A 1196 ? 0.4332 0.5111 0.3400 0.0583  -0.0778 -0.1290 1194 SER A CB  
8703  O OG  . SER A 1196 ? 0.4727 0.5582 0.3683 0.0601  -0.0763 -0.1207 1194 SER A OG  
8704  N N   . SER A 1197 ? 0.3610 0.4242 0.2821 0.0519  -0.0797 -0.1196 1195 SER A N   
8705  C CA  . SER A 1197 ? 0.4076 0.4715 0.3289 0.0512  -0.0808 -0.1135 1195 SER A CA  
8706  C C   . SER A 1197 ? 0.3937 0.4669 0.3036 0.0543  -0.0808 -0.1078 1195 SER A C   
8707  O O   . SER A 1197 ? 0.3690 0.4398 0.2768 0.0539  -0.0794 -0.0989 1195 SER A O   
8708  C CB  . SER A 1197 ? 0.4425 0.5090 0.3719 0.0502  -0.0857 -0.1205 1195 SER A CB  
8709  O OG  . SER A 1197 ? 0.4278 0.4849 0.3690 0.0465  -0.0855 -0.1232 1195 SER A OG  
8710  N N   . GLY A 1198 ? 0.4241 0.5084 0.3271 0.0575  -0.0826 -0.1129 1196 GLY A N   
8711  C CA  . GLY A 1198 ? 0.4260 0.5205 0.3180 0.0603  -0.0830 -0.1070 1196 GLY A CA  
8712  C C   . GLY A 1198 ? 0.4465 0.5376 0.3322 0.0603  -0.0783 -0.0972 1196 GLY A C   
8713  O O   . GLY A 1198 ? 0.4136 0.5066 0.2944 0.0609  -0.0780 -0.0880 1196 GLY A O   
8714  N N   . GLU A 1199 ? 0.3878 0.4733 0.2743 0.0595  -0.0748 -0.0989 1197 GLU A N   
8715  C CA  . GLU A 1199 ? 0.4377 0.5197 0.3191 0.0592  -0.0703 -0.0899 1197 GLU A CA  
8716  C C   . GLU A 1199 ? 0.4484 0.5195 0.3340 0.0567  -0.0686 -0.0810 1197 GLU A C   
8717  O O   . GLU A 1199 ? 0.4306 0.5015 0.3113 0.0570  -0.0668 -0.0716 1197 GLU A O   
8718  C CB  . GLU A 1199 ? 0.4311 0.5089 0.3139 0.0588  -0.0672 -0.0943 1197 GLU A CB  
8719  C CG  . GLU A 1199 ? 0.5170 0.5926 0.3940 0.0587  -0.0626 -0.0859 1197 GLU A CG  
8720  C CD  . GLU A 1199 ? 0.6472 0.7366 0.5130 0.0616  -0.0624 -0.0827 1197 GLU A CD  
8721  O OE1 . GLU A 1199 ? 0.6681 0.7694 0.5300 0.0639  -0.0658 -0.0875 1197 GLU A OE1 
8722  O OE2 . GLU A 1199 ? 0.7097 0.7986 0.5707 0.0614  -0.0588 -0.0753 1197 GLU A OE2 
8723  N N   . ILE A 1200 ? 0.4185 0.4810 0.3139 0.0542  -0.0693 -0.0838 1198 ILE A N   
8724  C CA  . ILE A 1200 ? 0.3850 0.4388 0.2848 0.0521  -0.0678 -0.0765 1198 ILE A CA  
8725  C C   . ILE A 1200 ? 0.4221 0.4812 0.3187 0.0536  -0.0704 -0.0710 1198 ILE A C   
8726  O O   . ILE A 1200 ? 0.4257 0.4808 0.3215 0.0534  -0.0690 -0.0626 1198 ILE A O   
8727  C CB  . ILE A 1200 ? 0.3848 0.4307 0.2956 0.0490  -0.0683 -0.0809 1198 ILE A CB  
8728  C CG1 . ILE A 1200 ? 0.4047 0.4439 0.3192 0.0473  -0.0656 -0.0845 1198 ILE A CG1 
8729  C CG2 . ILE A 1200 ? 0.3834 0.4229 0.2988 0.0472  -0.0672 -0.0741 1198 ILE A CG2 
8730  C CD1 . ILE A 1200 ? 0.4049 0.4378 0.3307 0.0441  -0.0666 -0.0892 1198 ILE A CD1 
8731  N N   . ALA A 1201 ? 0.4018 0.4705 0.2968 0.0555  -0.0746 -0.0757 1199 ALA A N   
8732  C CA  . ALA A 1201 ? 0.3908 0.4654 0.2832 0.0571  -0.0776 -0.0705 1199 ALA A CA  
8733  C C   . ALA A 1201 ? 0.4463 0.5267 0.3288 0.0592  -0.0767 -0.0624 1199 ALA A C   
8734  O O   . ALA A 1201 ? 0.4465 0.5266 0.3281 0.0598  -0.0777 -0.0543 1199 ALA A O   
8735  C CB  . ALA A 1201 ? 0.4417 0.5255 0.3350 0.0585  -0.0825 -0.0779 1199 ALA A CB  
8736  N N   . ARG A 1202 ? 0.4354 0.5217 0.3111 0.0603  -0.0751 -0.0644 1200 ARG A N   
8737  C CA  . ARG A 1202 ? 0.4170 0.5117 0.2830 0.0622  -0.0746 -0.0570 1200 ARG A CA  
8738  C C   . ARG A 1202 ? 0.4947 0.5821 0.3590 0.0609  -0.0701 -0.0489 1200 ARG A C   
8739  O O   . ARG A 1202 ? 0.4797 0.5703 0.3390 0.0616  -0.0700 -0.0394 1200 ARG A O   
8740  C CB  . ARG A 1202 ? 0.4483 0.5561 0.3072 0.0644  -0.0753 -0.0637 1200 ARG A CB  
8741  C CG  . ARG A 1202 ? 0.4695 0.5882 0.3275 0.0663  -0.0803 -0.0703 1200 ARG A CG  
8742  C CD  . ARG A 1202 ? 0.4799 0.6133 0.3297 0.0688  -0.0809 -0.0762 1200 ARG A CD  
8743  N NE  . ARG A 1202 ? 0.4361 0.5656 0.2881 0.0683  -0.0779 -0.0838 1200 ARG A NE  
8744  C CZ  . ARG A 1202 ? 0.5113 0.6402 0.3689 0.0684  -0.0796 -0.0959 1200 ARG A CZ  
8745  N NH1 . ARG A 1202 ? 0.4532 0.5869 0.3139 0.0692  -0.0843 -0.1025 1200 ARG A NH1 
8746  N NH2 . ARG A 1202 ? 0.4687 0.5917 0.3297 0.0677  -0.0769 -0.1015 1200 ARG A NH2 
8747  N N   . ASN A 1203 ? 0.4286 0.5067 0.2972 0.0590  -0.0666 -0.0520 1201 ASN A N   
8748  C CA  . ASN A 1203 ? 0.4660 0.5385 0.3324 0.0580  -0.0623 -0.0452 1201 ASN A CA  
8749  C C   . ASN A 1203 ? 0.4806 0.5392 0.3549 0.0555  -0.0603 -0.0420 1201 ASN A C   
8750  O O   . ASN A 1203 ? 0.5044 0.5559 0.3851 0.0538  -0.0592 -0.0480 1201 ASN A O   
8751  C CB  . ASN A 1203 ? 0.4912 0.5662 0.3549 0.0582  -0.0595 -0.0512 1201 ASN A CB  
8752  C CG  . ASN A 1203 ? 0.4987 0.5687 0.3603 0.0572  -0.0551 -0.0446 1201 ASN A CG  
8753  O OD1 . ASN A 1203 ? 0.4732 0.5381 0.3351 0.0562  -0.0542 -0.0354 1201 ASN A OD1 
8754  N ND2 . ASN A 1203 ? 0.4773 0.5489 0.3372 0.0574  -0.0525 -0.0496 1201 ASN A ND2 
8755  N N   . PRO A 1204 ? 0.4805 0.5351 0.3549 0.0552  -0.0600 -0.0326 1202 PRO A N   
8756  C CA  . PRO A 1204 ? 0.4705 0.5128 0.3522 0.0530  -0.0580 -0.0300 1202 PRO A CA  
8757  C C   . PRO A 1204 ? 0.4734 0.5090 0.3562 0.0512  -0.0536 -0.0317 1202 PRO A C   
8758  O O   . PRO A 1204 ? 0.4382 0.4647 0.3277 0.0492  -0.0520 -0.0328 1202 PRO A O   
8759  C CB  . PRO A 1204 ? 0.5170 0.5580 0.3975 0.0535  -0.0587 -0.0197 1202 PRO A CB  
8760  C CG  . PRO A 1204 ? 0.5678 0.6192 0.4393 0.0552  -0.0592 -0.0154 1202 PRO A CG  
8761  C CD  . PRO A 1204 ? 0.4812 0.5426 0.3493 0.0566  -0.0612 -0.0237 1202 PRO A CD  
8762  N N   . ASP A 1205 ? 0.4791 0.5197 0.3557 0.0519  -0.0516 -0.0319 1203 ASP A N   
8763  C CA  . ASP A 1205 ? 0.4989 0.5340 0.3763 0.0505  -0.0476 -0.0337 1203 ASP A CA  
8764  C C   . ASP A 1205 ? 0.4558 0.4930 0.3349 0.0507  -0.0478 -0.0439 1203 ASP A C   
8765  O O   . ASP A 1205 ? 0.4577 0.4942 0.3354 0.0505  -0.0450 -0.0461 1203 ASP A O   
8766  C CB  . ASP A 1205 ? 0.5119 0.5510 0.3824 0.0511  -0.0452 -0.0272 1203 ASP A CB  
8767  C CG  . ASP A 1205 ? 0.6148 0.6510 0.4850 0.0507  -0.0454 -0.0167 1203 ASP A CG  
8768  O OD1 . ASP A 1205 ? 0.6313 0.6585 0.5079 0.0494  -0.0457 -0.0150 1203 ASP A OD1 
8769  O OD2 . ASP A 1205 ? 0.6486 0.6919 0.5127 0.0516  -0.0454 -0.0103 1203 ASP A OD2 
8770  N N   . ALA A 1206 ? 0.4541 0.4937 0.3365 0.0511  -0.0511 -0.0504 1204 ALA A N   
8771  C CA  . ALA A 1206 ? 0.4199 0.4613 0.3051 0.0513  -0.0520 -0.0605 1204 ALA A CA  
8772  C C   . ALA A 1206 ? 0.4106 0.4422 0.3017 0.0490  -0.0490 -0.0624 1204 ALA A C   
8773  O O   . ALA A 1206 ? 0.4024 0.4353 0.2933 0.0496  -0.0480 -0.0679 1204 ALA A O   
8774  C CB  . ALA A 1206 ? 0.4527 0.4957 0.3431 0.0511  -0.0561 -0.0662 1204 ALA A CB  
8775  N N   . TYR A 1207 ? 0.3952 0.4174 0.2917 0.0465  -0.0476 -0.0579 1205 TYR A N   
8776  C CA  . TYR A 1207 ? 0.3870 0.4001 0.2882 0.0442  -0.0444 -0.0574 1205 TYR A CA  
8777  C C   . TYR A 1207 ? 0.4185 0.4285 0.3158 0.0439  -0.0411 -0.0487 1205 TYR A C   
8778  O O   . TYR A 1207 ? 0.4694 0.4790 0.3655 0.0441  -0.0417 -0.0426 1205 TYR A O   
8779  C CB  . TYR A 1207 ? 0.4137 0.4198 0.3242 0.0414  -0.0451 -0.0587 1205 TYR A CB  
8780  C CG  . TYR A 1207 ? 0.3828 0.3914 0.2988 0.0412  -0.0486 -0.0669 1205 TYR A CG  
8781  C CD1 . TYR A 1207 ? 0.3855 0.3946 0.3035 0.0415  -0.0491 -0.0741 1205 TYR A CD1 
8782  C CD2 . TYR A 1207 ? 0.3641 0.3743 0.2838 0.0407  -0.0516 -0.0678 1205 TYR A CD2 
8783  C CE1 . TYR A 1207 ? 0.3587 0.3695 0.2828 0.0411  -0.0527 -0.0819 1205 TYR A CE1 
8784  C CE2 . TYR A 1207 ? 0.3885 0.4011 0.3139 0.0402  -0.0549 -0.0754 1205 TYR A CE2 
8785  C CZ  . TYR A 1207 ? 0.3713 0.3839 0.2989 0.0403  -0.0556 -0.0823 1205 TYR A CZ  
8786  O OH  . TYR A 1207 ? 0.3607 0.3751 0.2950 0.0397  -0.0593 -0.0900 1205 TYR A OH  
8787  N N   . CYS A 1208 ? 0.3595 0.3671 0.2555 0.0436  -0.0380 -0.0482 1206 CYS A N   
8788  C CA  . CYS A 1208 ? 0.4043 0.4097 0.2966 0.0434  -0.0350 -0.0403 1206 CYS A CA  
8789  C C   . CYS A 1208 ? 0.3756 0.3707 0.2740 0.0406  -0.0328 -0.0374 1206 CYS A C   
8790  O O   . CYS A 1208 ? 0.3940 0.3845 0.2975 0.0391  -0.0319 -0.0415 1206 CYS A O   
8791  C CB  . CYS A 1208 ? 0.4058 0.4160 0.2927 0.0447  -0.0328 -0.0411 1206 CYS A CB  
8792  S SG  . CYS A 1208 ? 0.4532 0.4613 0.3359 0.0441  -0.0292 -0.0312 1206 CYS A SG  
8793  N N   . LEU A 1209 ? 0.3902 0.3823 0.2888 0.0400  -0.0323 -0.0306 1207 LEU A N   
8794  C CA  . LEU A 1209 ? 0.3386 0.3223 0.2430 0.0376  -0.0305 -0.0285 1207 LEU A CA  
8795  C C   . LEU A 1209 ? 0.3398 0.3193 0.2436 0.0366  -0.0269 -0.0262 1207 LEU A C   
8796  O O   . LEU A 1209 ? 0.3386 0.3119 0.2474 0.0345  -0.0253 -0.0256 1207 LEU A O   
8797  C CB  . LEU A 1209 ? 0.3167 0.2988 0.2223 0.0377  -0.0315 -0.0230 1207 LEU A CB  
8798  C CG  . LEU A 1209 ? 0.3412 0.3272 0.2482 0.0388  -0.0352 -0.0249 1207 LEU A CG  
8799  C CD1 . LEU A 1209 ? 0.3701 0.3535 0.2798 0.0389  -0.0361 -0.0200 1207 LEU A CD1 
8800  C CD2 . LEU A 1209 ? 0.3664 0.3523 0.2790 0.0376  -0.0365 -0.0316 1207 LEU A CD2 
8801  N N   . ASN A 1210 ? 0.3544 0.3380 0.2523 0.0380  -0.0256 -0.0250 1208 ASN A N   
8802  C CA  . ASN A 1210 ? 0.4147 0.3950 0.3122 0.0371  -0.0222 -0.0232 1208 ASN A CA  
8803  C C   . ASN A 1210 ? 0.3708 0.3467 0.2739 0.0357  -0.0214 -0.0287 1208 ASN A C   
8804  O O   . ASN A 1210 ? 0.3413 0.3116 0.2471 0.0340  -0.0189 -0.0267 1208 ASN A O   
8805  C CB  . ASN A 1210 ? 0.4132 0.4007 0.3038 0.0390  -0.0211 -0.0225 1208 ASN A CB  
8806  C CG  . ASN A 1210 ? 0.4425 0.4348 0.3277 0.0400  -0.0217 -0.0155 1208 ASN A CG  
8807  O OD1 . ASN A 1210 ? 0.4935 0.4834 0.3803 0.0396  -0.0233 -0.0116 1208 ASN A OD1 
8808  N ND2 . ASN A 1210 ? 0.5100 0.5097 0.3892 0.0413  -0.0205 -0.0139 1208 ASN A ND2 
8809  N N   . TRP A 1211 ? 0.3665 0.3450 0.2718 0.0363  -0.0236 -0.0355 1209 TRP A N   
8810  C CA  . TRP A 1211 ? 0.3748 0.3496 0.2859 0.0351  -0.0235 -0.0408 1209 TRP A CA  
8811  C C   . TRP A 1211 ? 0.3808 0.3501 0.2996 0.0324  -0.0245 -0.0413 1209 TRP A C   
8812  O O   . TRP A 1211 ? 0.4187 0.3848 0.3436 0.0310  -0.0250 -0.0452 1209 TRP A O   
8813  C CB  . TRP A 1211 ? 0.3339 0.3145 0.2441 0.0373  -0.0257 -0.0486 1209 TRP A CB  
8814  C CG  . TRP A 1211 ? 0.3557 0.3451 0.2573 0.0402  -0.0252 -0.0480 1209 TRP A CG  
8815  C CD1 . TRP A 1211 ? 0.3819 0.3800 0.2791 0.0425  -0.0277 -0.0511 1209 TRP A CD1 
8816  C CD2 . TRP A 1211 ? 0.3674 0.3586 0.2639 0.0409  -0.0221 -0.0436 1209 TRP A CD2 
8817  N NE1 . TRP A 1211 ? 0.3820 0.3878 0.2714 0.0446  -0.0262 -0.0487 1209 TRP A NE1 
8818  C CE2 . TRP A 1211 ? 0.3829 0.3845 0.2719 0.0436  -0.0228 -0.0439 1209 TRP A CE2 
8819  C CE3 . TRP A 1211 ? 0.3820 0.3677 0.2797 0.0395  -0.0189 -0.0393 1209 TRP A CE3 
8820  C CZ2 . TRP A 1211 ? 0.4288 0.4357 0.3117 0.0446  -0.0202 -0.0398 1209 TRP A CZ2 
8821  C CZ3 . TRP A 1211 ? 0.3759 0.3663 0.2678 0.0406  -0.0164 -0.0356 1209 TRP A CZ3 
8822  C CH2 . TRP A 1211 ? 0.3398 0.3406 0.2245 0.0430  -0.0170 -0.0355 1209 TRP A CH2 
8823  N N   . LEU A 1212 ? 0.3234 0.2920 0.2425 0.0316  -0.0250 -0.0375 1210 LEU A N   
8824  C CA  . LEU A 1212 ? 0.3301 0.2953 0.2562 0.0291  -0.0257 -0.0374 1210 LEU A CA  
8825  C C   . LEU A 1212 ? 0.3429 0.3035 0.2705 0.0273  -0.0230 -0.0319 1210 LEU A C   
8826  O O   . LEU A 1212 ? 0.3168 0.2757 0.2497 0.0252  -0.0232 -0.0313 1210 LEU A O   
8827  C CB  . LEU A 1212 ? 0.3155 0.2845 0.2419 0.0298  -0.0286 -0.0384 1210 LEU A CB  
8828  C CG  . LEU A 1212 ? 0.3188 0.2923 0.2459 0.0309  -0.0317 -0.0449 1210 LEU A CG  
8829  C CD1 . LEU A 1212 ? 0.3232 0.3020 0.2479 0.0326  -0.0345 -0.0451 1210 LEU A CD1 
8830  C CD2 . LEU A 1212 ? 0.3227 0.2932 0.2584 0.0283  -0.0328 -0.0490 1210 LEU A CD2 
8831  N N   . VAL A 1213 ? 0.3149 0.2740 0.2381 0.0280  -0.0206 -0.0281 1211 VAL A N   
8832  C CA  . VAL A 1213 ? 0.3387 0.2936 0.2637 0.0263  -0.0181 -0.0236 1211 VAL A CA  
8833  C C   . VAL A 1213 ? 0.3537 0.3057 0.2791 0.0255  -0.0158 -0.0237 1211 VAL A C   
8834  O O   . VAL A 1213 ? 0.3774 0.3312 0.3006 0.0269  -0.0159 -0.0266 1211 VAL A O   
8835  C CB  . VAL A 1213 ? 0.3475 0.3025 0.2682 0.0276  -0.0174 -0.0184 1211 VAL A CB  
8836  C CG1 . VAL A 1213 ? 0.3716 0.3289 0.2932 0.0284  -0.0199 -0.0180 1211 VAL A CG1 
8837  C CG2 . VAL A 1213 ? 0.3523 0.3101 0.2666 0.0296  -0.0168 -0.0169 1211 VAL A CG2 
8838  N N   . GLU A 1214 ? 0.3157 0.2638 0.2441 0.0235  -0.0138 -0.0208 1212 GLU A N   
8839  C CA  . GLU A 1214 ? 0.3725 0.3177 0.3019 0.0226  -0.0116 -0.0201 1212 GLU A CA  
8840  C C   . GLU A 1214 ? 0.3488 0.2927 0.2746 0.0229  -0.0093 -0.0152 1212 GLU A C   
8841  O O   . GLU A 1214 ? 0.3334 0.2763 0.2600 0.0222  -0.0089 -0.0121 1212 GLU A O   
8842  C CB  . GLU A 1214 ? 0.3711 0.3133 0.3074 0.0196  -0.0113 -0.0203 1212 GLU A CB  
8843  C CG  . GLU A 1214 ? 0.4375 0.3766 0.3753 0.0188  -0.0094 -0.0194 1212 GLU A CG  
8844  C CD  . GLU A 1214 ? 0.5383 0.4749 0.4828 0.0157  -0.0091 -0.0181 1212 GLU A CD  
8845  O OE1 . GLU A 1214 ? 0.5524 0.4900 0.5016 0.0140  -0.0109 -0.0195 1212 GLU A OE1 
8846  O OE2 . GLU A 1214 ? 0.5614 0.4956 0.5068 0.0147  -0.0072 -0.0154 1212 GLU A OE2 
8847  N N   . GLU A 1215 ? 0.3238 0.2681 0.2462 0.0241  -0.0078 -0.0149 1213 GLU A N   
8848  C CA  . GLU A 1215 ? 0.3390 0.2821 0.2587 0.0241  -0.0055 -0.0102 1213 GLU A CA  
8849  C C   . GLU A 1215 ? 0.3750 0.3142 0.2990 0.0219  -0.0037 -0.0089 1213 GLU A C   
8850  O O   . GLU A 1215 ? 0.3344 0.2723 0.2616 0.0212  -0.0036 -0.0115 1213 GLU A O   
8851  C CB  . GLU A 1215 ? 0.3304 0.2770 0.2453 0.0261  -0.0046 -0.0104 1213 GLU A CB  
8852  C CG  . GLU A 1215 ? 0.3722 0.3243 0.2820 0.0283  -0.0062 -0.0107 1213 GLU A CG  
8853  C CD  . GLU A 1215 ? 0.3712 0.3284 0.2767 0.0302  -0.0051 -0.0122 1213 GLU A CD  
8854  O OE1 . GLU A 1215 ? 0.3486 0.3075 0.2554 0.0311  -0.0058 -0.0180 1213 GLU A OE1 
8855  O OE2 . GLU A 1215 ? 0.3870 0.3468 0.2884 0.0307  -0.0037 -0.0077 1213 GLU A OE2 
8856  N N   . VAL A 1216 ? 0.3226 0.2599 0.2467 0.0209  -0.0024 -0.0048 1214 VAL A N   
8857  C CA  . VAL A 1216 ? 0.3282 0.2627 0.2555 0.0190  -0.0006 -0.0030 1214 VAL A CA  
8858  C C   . VAL A 1216 ? 0.2994 0.2332 0.2239 0.0194  0.0012  0.0010  1214 VAL A C   
8859  O O   . VAL A 1216 ? 0.3192 0.2534 0.2419 0.0200  0.0007  0.0034  1214 VAL A O   
8860  C CB  . VAL A 1216 ? 0.3537 0.2875 0.2853 0.0170  -0.0011 -0.0027 1214 VAL A CB  
8861  C CG1 . VAL A 1216 ? 0.3271 0.2591 0.2614 0.0150  0.0008  -0.0004 1214 VAL A CG1 
8862  C CG2 . VAL A 1216 ? 0.3918 0.3266 0.3270 0.0161  -0.0028 -0.0061 1214 VAL A CG2 
8863  N N   . SER A 1217 ? 0.3106 0.2434 0.2355 0.0190  0.0030  0.0017  1215 SER A N   
8864  C CA  . SER A 1217 ? 0.2809 0.2131 0.2042 0.0188  0.0049  0.0054  1215 SER A CA  
8865  C C   . SER A 1217 ? 0.3143 0.2439 0.2415 0.0167  0.0059  0.0069  1215 SER A C   
8866  O O   . SER A 1217 ? 0.3358 0.2646 0.2664 0.0156  0.0059  0.0052  1215 SER A O   
8867  C CB  . SER A 1217 ? 0.3403 0.2743 0.2611 0.0201  0.0062  0.0050  1215 SER A CB  
8868  O OG  . SER A 1217 ? 0.3806 0.3140 0.3012 0.0195  0.0082  0.0085  1215 SER A OG  
8869  N N   . ALA A 1218 ? 0.3231 0.2519 0.2503 0.0162  0.0065  0.0100  1216 ALA A N   
8870  C CA  . ALA A 1218 ? 0.3336 0.2610 0.2640 0.0143  0.0075  0.0112  1216 ALA A CA  
8871  C C   . ALA A 1218 ? 0.3204 0.2471 0.2498 0.0143  0.0089  0.0145  1216 ALA A C   
8872  O O   . ALA A 1218 ? 0.3475 0.2741 0.2753 0.0150  0.0083  0.0165  1216 ALA A O   
8873  C CB  . ALA A 1218 ? 0.3012 0.2290 0.2342 0.0134  0.0064  0.0105  1216 ALA A CB  
8874  N N   . SER A 1219 ? 0.3150 0.2412 0.2458 0.0133  0.0105  0.0153  1217 SER A N   
8875  C CA  . SER A 1219 ? 0.3330 0.2588 0.2635 0.0130  0.0119  0.0183  1217 SER A CA  
8876  C C   . SER A 1219 ? 0.2903 0.2154 0.2242 0.0112  0.0122  0.0190  1217 SER A C   
8877  O O   . SER A 1219 ? 0.3251 0.2505 0.2611 0.0102  0.0127  0.0182  1217 SER A O   
8878  C CB  . SER A 1219 ? 0.3373 0.2641 0.2664 0.0138  0.0134  0.0186  1217 SER A CB  
8879  O OG  . SER A 1219 ? 0.3438 0.2711 0.2725 0.0135  0.0147  0.0218  1217 SER A OG  
8880  N N   . ILE A 1220 ? 0.2990 0.2236 0.2339 0.0108  0.0118  0.0205  1218 ILE A N   
8881  C CA  . ILE A 1220 ? 0.3057 0.2308 0.2437 0.0093  0.0119  0.0205  1218 ILE A CA  
8882  C C   . ILE A 1220 ? 0.2814 0.2058 0.2200 0.0088  0.0129  0.0231  1218 ILE A C   
8883  O O   . ILE A 1220 ? 0.3022 0.2254 0.2404 0.0093  0.0125  0.0250  1218 ILE A O   
8884  C CB  . ILE A 1220 ? 0.3297 0.2553 0.2695 0.0094  0.0101  0.0188  1218 ILE A CB  
8885  C CG1 . ILE A 1220 ? 0.3588 0.2855 0.2980 0.0100  0.0091  0.0163  1218 ILE A CG1 
8886  C CG2 . ILE A 1220 ? 0.3600 0.2877 0.3029 0.0081  0.0102  0.0180  1218 ILE A CG2 
8887  C CD1 . ILE A 1220 ? 0.4095 0.3357 0.3489 0.0113  0.0071  0.0153  1218 ILE A CD1 
8888  N N   . ASN A 1221 ? 0.3320 0.2574 0.2721 0.0076  0.0141  0.0236  1219 ASN A N   
8889  C CA  . ASN A 1221 ? 0.3398 0.2650 0.2811 0.0070  0.0150  0.0259  1219 ASN A CA  
8890  C C   . ASN A 1221 ? 0.3544 0.2798 0.2984 0.0062  0.0137  0.0252  1219 ASN A C   
8891  O O   . ASN A 1221 ? 0.3749 0.3026 0.3207 0.0053  0.0135  0.0235  1219 ASN A O   
8892  C CB  . ASN A 1221 ? 0.3224 0.2487 0.2647 0.0061  0.0164  0.0266  1219 ASN A CB  
8893  C CG  . ASN A 1221 ? 0.3809 0.3076 0.3248 0.0053  0.0172  0.0288  1219 ASN A CG  
8894  O OD1 . ASN A 1221 ? 0.3267 0.2525 0.2711 0.0053  0.0169  0.0301  1219 ASN A OD1 
8895  N ND2 . ASN A 1221 ? 0.3876 0.3157 0.3330 0.0045  0.0181  0.0294  1219 ASN A ND2 
8896  N N   . THR A 1222 ? 0.3221 0.2457 0.2670 0.0066  0.0127  0.0264  1220 THR A N   
8897  C CA  . THR A 1222 ? 0.3712 0.2947 0.3198 0.0062  0.0109  0.0250  1220 THR A CA  
8898  C C   . THR A 1222 ? 0.4188 0.3427 0.3702 0.0050  0.0114  0.0263  1220 THR A C   
8899  O O   . THR A 1222 ? 0.4434 0.3673 0.3985 0.0047  0.0097  0.0246  1220 THR A O   
8900  C CB  . THR A 1222 ? 0.4328 0.3537 0.3826 0.0073  0.0088  0.0253  1220 THR A CB  
8901  O OG1 . THR A 1222 ? 0.3835 0.3025 0.3324 0.0072  0.0092  0.0296  1220 THR A OG1 
8902  C CG2 . THR A 1222 ? 0.3912 0.3123 0.3388 0.0086  0.0080  0.0234  1220 THR A CG2 
8903  N N   . ALA A 1223 ? 0.3495 0.2738 0.2995 0.0044  0.0133  0.0289  1221 ALA A N   
8904  C CA  . ALA A 1223 ? 0.4284 0.3536 0.3809 0.0032  0.0139  0.0301  1221 ALA A CA  
8905  C C   . ALA A 1223 ? 0.5003 0.4289 0.4531 0.0024  0.0146  0.0285  1221 ALA A C   
8906  O O   . ALA A 1223 ? 0.6086 0.5387 0.5632 0.0014  0.0151  0.0294  1221 ALA A O   
8907  C CB  . ALA A 1223 ? 0.4022 0.3271 0.3536 0.0030  0.0156  0.0339  1221 ALA A CB  
8908  N N   . ALA A 1224 ? 0.5106 0.4409 0.4619 0.0026  0.0146  0.0265  1222 ALA A N   
8909  C CA  . ALA A 1224 ? 0.5626 0.4963 0.5140 0.0017  0.0154  0.0264  1222 ALA A CA  
8910  C C   . ALA A 1224 ? 0.6019 0.5398 0.5558 0.0005  0.0147  0.0251  1222 ALA A C   
8911  O O   . ALA A 1224 ? 0.6130 0.5539 0.5674 -0.0005 0.0154  0.0263  1222 ALA A O   
8912  C CB  . ALA A 1224 ? 0.5221 0.4568 0.4720 0.0019  0.0152  0.0250  1222 ALA A CB  
8913  N N   . ALA A 1225 ? 0.6372 0.5756 0.5931 0.0009  0.0131  0.0224  1223 ALA A N   
8914  C CA  . ALA A 1225 ? 0.6331 0.5764 0.5916 0.0001  0.0122  0.0201  1223 ALA A CA  
8915  C C   . ALA A 1225 ? 0.7030 0.6457 0.6637 -0.0007 0.0123  0.0216  1223 ALA A C   
8916  O O   . ALA A 1225 ? 0.6801 0.6276 0.6428 -0.0015 0.0116  0.0199  1223 ALA A O   
8917  C CB  . ALA A 1225 ? 0.5969 0.5413 0.5578 0.0011  0.0100  0.0156  1223 ALA A CB  
8918  N N   . GLY A 1226 ? 0.6613 0.5993 0.6217 -0.0006 0.0131  0.0248  1224 GLY A N   
8919  C CA  . GLY A 1226 ? 0.6652 0.6031 0.6281 -0.0015 0.0133  0.0267  1224 GLY A CA  
8920  C C   . GLY A 1226 ? 0.6617 0.5953 0.6274 -0.0014 0.0121  0.0276  1224 GLY A C   
8921  O O   . GLY A 1226 ? 0.6509 0.5844 0.6196 -0.0024 0.0119  0.0291  1224 GLY A O   
8922  N N   . GLY A 1227 ? 0.6214 0.5516 0.5866 -0.0004 0.0111  0.0272  1225 GLY A N   
8923  C CA  . GLY A 1227 ? 0.6304 0.5565 0.5988 -0.0005 0.0096  0.0290  1225 GLY A CA  
8924  C C   . GLY A 1227 ? 0.6617 0.5847 0.6286 0.0008  0.0087  0.0294  1225 GLY A C   
8925  O O   . GLY A 1227 ? 0.6536 0.5775 0.6173 0.0018  0.0091  0.0274  1225 GLY A O   
8926  N N   . ASN A 1228 ? 0.5671 0.4865 0.5368 0.0005  0.0074  0.0323  1226 ASN A N   
8927  C CA  . ASN A 1228 ? 0.6532 0.5697 0.6218 0.0015  0.0063  0.0339  1226 ASN A CA  
8928  C C   . ASN A 1228 ? 0.6933 0.6065 0.6685 0.0018  0.0025  0.0323  1226 ASN A C   
8929  O O   . ASN A 1228 ? 0.6705 0.5812 0.6507 0.0006  0.0009  0.0352  1226 ASN A O   
8930  C CB  . ASN A 1228 ? 0.6391 0.5551 0.6052 0.0010  0.0080  0.0397  1226 ASN A CB  
8931  C CG  . ASN A 1228 ? 0.6563 0.5708 0.6199 0.0022  0.0072  0.0416  1226 ASN A CG  
8932  O OD1 . ASN A 1228 ? 0.6860 0.5984 0.6516 0.0032  0.0047  0.0394  1226 ASN A OD1 
8933  N ND2 . ASN A 1228 ? 0.5417 0.4581 0.5012 0.0022  0.0093  0.0456  1226 ASN A ND2 
8934  N N   . ALA A 1229 ? 0.6457 0.5589 0.6214 0.0033  0.0008  0.0277  1227 ALA A N   
8935  C CA  . ALA A 1229 ? 0.6673 0.5773 0.6497 0.0041  -0.0032 0.0255  1227 ALA A CA  
8936  C C   . ALA A 1229 ? 0.6779 0.5838 0.6607 0.0045  -0.0046 0.0303  1227 ALA A C   
8937  O O   . ALA A 1229 ? 0.6919 0.5939 0.6813 0.0040  -0.0077 0.0325  1227 ALA A O   
8938  C CB  . ALA A 1229 ? 0.6408 0.5535 0.6238 0.0059  -0.0044 0.0186  1227 ALA A CB  
8939  N N   . PRO B 17   ? 0.7518 0.5767 0.7719 0.1350  -0.0962 -0.1278 15   PRO B N   
8940  C CA  . PRO B 17   ? 0.7634 0.5728 0.7718 0.1256  -0.1004 -0.1255 15   PRO B CA  
8941  C C   . PRO B 17   ? 0.7559 0.5689 0.7576 0.1224  -0.0949 -0.1292 15   PRO B C   
8942  O O   . PRO B 17   ? 0.7496 0.5797 0.7567 0.1218  -0.0877 -0.1297 15   PRO B O   
8943  C CB  . PRO B 17   ? 0.7578 0.5717 0.7699 0.1176  -0.1019 -0.1180 15   PRO B CB  
8944  C CG  . PRO B 17   ? 0.7344 0.5555 0.7577 0.1240  -0.1032 -0.1165 15   PRO B CG  
8945  C CD  . PRO B 17   ? 0.7330 0.5664 0.7636 0.1346  -0.0975 -0.1231 15   PRO B CD  
8946  N N   . ALA B 18   ? 0.7561 0.5541 0.7462 0.1196  -0.0983 -0.1309 16   ALA B N   
8947  C CA  . ALA B 18   ? 0.7322 0.5319 0.7148 0.1163  -0.0941 -0.1343 16   ALA B CA  
8948  C C   . ALA B 18   ? 0.7426 0.5488 0.7251 0.1068  -0.0920 -0.1303 16   ALA B C   
8949  O O   . ALA B 18   ? 0.7300 0.5333 0.7134 0.0995  -0.0956 -0.1231 16   ALA B O   
8950  C CB  . ALA B 18   ? 0.7541 0.5350 0.7245 0.1137  -0.0996 -0.1357 16   ALA B CB  
8951  N N   . PRO B 19   ? 0.6907 0.5097 0.6724 0.1051  -0.0848 -0.1322 17   PRO B N   
8952  C CA  . PRO B 19   ? 0.7073 0.5379 0.6901 0.0949  -0.0810 -0.1259 17   PRO B CA  
8953  C C   . PRO B 19   ? 0.6703 0.4870 0.6440 0.0848  -0.0867 -0.1219 17   PRO B C   
8954  O O   . PRO B 19   ? 0.6644 0.4671 0.6285 0.0842  -0.0904 -0.1257 17   PRO B O   
8955  C CB  . PRO B 19   ? 0.6664 0.5109 0.6489 0.0967  -0.0729 -0.1300 17   PRO B CB  
8956  C CG  . PRO B 19   ? 0.6857 0.5314 0.6706 0.1089  -0.0709 -0.1375 17   PRO B CG  
8957  C CD  . PRO B 19   ? 0.7387 0.5637 0.7187 0.1127  -0.0793 -0.1398 17   PRO B CD  
8958  N N   . PHE B 20   ? 0.6770 0.4976 0.6537 0.0768  -0.0876 -0.1141 18   PHE B N   
8959  C CA  . PHE B 20   ? 0.6547 0.4680 0.6249 0.0659  -0.0912 -0.1087 18   PHE B CA  
8960  C C   . PHE B 20   ? 0.6601 0.4512 0.6228 0.0642  -0.1003 -0.1083 18   PHE B C   
8961  O O   . PHE B 20   ? 0.6860 0.4695 0.6424 0.0552  -0.1037 -0.1044 18   PHE B O   
8962  C CB  . PHE B 20   ? 0.5924 0.4114 0.5576 0.0612  -0.0871 -0.1102 18   PHE B CB  
8963  C CG  . PHE B 20   ? 0.5531 0.3930 0.5249 0.0621  -0.0783 -0.1100 18   PHE B CG  
8964  C CD1 . PHE B 20   ? 0.5591 0.4110 0.5365 0.0562  -0.0754 -0.1034 18   PHE B CD1 
8965  C CD2 . PHE B 20   ? 0.5397 0.3870 0.5119 0.0689  -0.0731 -0.1164 18   PHE B CD2 
8966  C CE1 . PHE B 20   ? 0.5226 0.3926 0.5059 0.0568  -0.0678 -0.1030 18   PHE B CE1 
8967  C CE2 . PHE B 20   ? 0.5044 0.3708 0.4827 0.0692  -0.0652 -0.1156 18   PHE B CE2 
8968  C CZ  . PHE B 20   ? 0.5145 0.3917 0.4984 0.0631  -0.0628 -0.1089 18   PHE B CZ  
8969  N N   . ALA B 21   ? 0.7503 0.5307 0.7138 0.0724  -0.1047 -0.1118 19   ALA B N   
8970  C CA  . ALA B 21   ? 0.7410 0.4990 0.6973 0.0709  -0.1140 -0.1111 19   ALA B CA  
8971  C C   . ALA B 21   ? 0.7618 0.5162 0.7181 0.0617  -0.1180 -0.1019 19   ALA B C   
8972  O O   . ALA B 21   ? 0.8385 0.5781 0.7874 0.0548  -0.1242 -0.0989 19   ALA B O   
8973  C CB  . ALA B 21   ? 0.7488 0.4986 0.7072 0.0821  -0.1171 -0.1159 19   ALA B CB  
8974  N N   . ASP B 22   ? 0.7030 0.4711 0.6673 0.0613  -0.1147 -0.0971 20   ASP B N   
8975  C CA  . ASP B 22   ? 0.6302 0.3964 0.5941 0.0530  -0.1179 -0.0884 20   ASP B CA  
8976  C C   . ASP B 22   ? 0.5594 0.3437 0.5266 0.0460  -0.1111 -0.0836 20   ASP B C   
8977  O O   . ASP B 22   ? 0.5401 0.3324 0.5120 0.0442  -0.1101 -0.0784 20   ASP B O   
8978  C CB  . ASP B 22   ? 0.6689 0.4322 0.6378 0.0582  -0.1215 -0.0861 20   ASP B CB  
8979  N N   . PHE B 23   ? 0.5617 0.3522 0.5263 0.0422  -0.1069 -0.0854 21   PHE B N   
8980  C CA  . PHE B 23   ? 0.5049 0.3133 0.4733 0.0370  -0.1001 -0.0818 21   PHE B CA  
8981  C C   . PHE B 23   ? 0.4961 0.3040 0.4628 0.0277  -0.1021 -0.0733 21   PHE B C   
8982  O O   . PHE B 23   ? 0.4475 0.2660 0.4191 0.0268  -0.0994 -0.0692 21   PHE B O   
8983  C CB  . PHE B 23   ? 0.5158 0.3295 0.4810 0.0347  -0.0960 -0.0852 21   PHE B CB  
8984  C CG  . PHE B 23   ? 0.4869 0.3179 0.4555 0.0293  -0.0895 -0.0815 21   PHE B CG  
8985  C CD1 . PHE B 23   ? 0.4375 0.2842 0.4139 0.0334  -0.0834 -0.0819 21   PHE B CD1 
8986  C CD2 . PHE B 23   ? 0.4767 0.3081 0.4411 0.0202  -0.0896 -0.0774 21   PHE B CD2 
8987  C CE1 . PHE B 23   ? 0.4813 0.3426 0.4605 0.0287  -0.0778 -0.0784 21   PHE B CE1 
8988  C CE2 . PHE B 23   ? 0.4914 0.3383 0.4590 0.0159  -0.0838 -0.0740 21   PHE B CE2 
8989  C CZ  . PHE B 23   ? 0.4929 0.3541 0.4676 0.0203  -0.0779 -0.0747 21   PHE B CZ  
8990  N N   . ALA B 24   ? 0.4709 0.2671 0.4305 0.0205  -0.1069 -0.0704 22   ALA B N   
8991  C CA  . ALA B 24   ? 0.5122 0.3080 0.4697 0.0113  -0.1087 -0.0620 22   ALA B CA  
8992  C C   . ALA B 24   ? 0.5316 0.3086 0.4816 0.0060  -0.1166 -0.0596 22   ALA B C   
8993  O O   . ALA B 24   ? 0.5164 0.2925 0.4627 -0.0023 -0.1172 -0.0565 22   ALA B O   
8994  C CB  . ALA B 24   ? 0.4696 0.2808 0.4284 0.0050  -0.1024 -0.0592 22   ALA B CB  
8995  N N   . PRO B 25   ? 0.5325 0.2942 0.4806 0.0104  -0.1231 -0.0606 23   PRO B N   
8996  C CA  . PRO B 25   ? 0.5642 0.3065 0.5050 0.0050  -0.1313 -0.0579 23   PRO B CA  
8997  C C   . PRO B 25   ? 0.5835 0.3268 0.5224 -0.0050 -0.1327 -0.0481 23   PRO B C   
8998  O O   . PRO B 25   ? 0.5589 0.3104 0.5011 -0.0048 -0.1305 -0.0437 23   PRO B O   
8999  C CB  . PRO B 25   ? 0.5412 0.2691 0.4816 0.0134  -0.1371 -0.0610 23   PRO B CB  
9000  C CG  . PRO B 25   ? 0.5452 0.2868 0.4933 0.0195  -0.1326 -0.0607 23   PRO B CG  
9001  C CD  . PRO B 25   ? 0.4812 0.2430 0.4341 0.0198  -0.1235 -0.0632 23   PRO B CD  
9002  N N   . PRO B 26   ? 0.5658 0.3019 0.4996 -0.0141 -0.1360 -0.0444 24   PRO B N   
9003  C CA  . PRO B 26   ? 0.5861 0.3242 0.5183 -0.0239 -0.1370 -0.0347 24   PRO B CA  
9004  C C   . PRO B 26   ? 0.5941 0.3197 0.5238 -0.0235 -0.1431 -0.0298 24   PRO B C   
9005  O O   . PRO B 26   ? 0.6076 0.3188 0.5358 -0.0169 -0.1485 -0.0336 24   PRO B O   
9006  C CB  . PRO B 26   ? 0.5828 0.3130 0.5102 -0.0328 -0.1406 -0.0329 24   PRO B CB  
9007  C CG  . PRO B 26   ? 0.6516 0.3678 0.5758 -0.0269 -0.1448 -0.0415 24   PRO B CG  
9008  C CD  . PRO B 26   ? 0.5907 0.3177 0.5200 -0.0159 -0.1388 -0.0490 24   PRO B CD  
9009  N N   . VAL B 27   ? 0.5788 0.3104 0.5080 -0.0304 -0.1421 -0.0212 25   VAL B N   
9010  C CA  . VAL B 27   ? 0.6536 0.3732 0.5792 -0.0315 -0.1481 -0.0153 25   VAL B CA  
9011  C C   . VAL B 27   ? 0.6391 0.3363 0.5585 -0.0351 -0.1573 -0.0141 25   VAL B C   
9012  O O   . VAL B 27   ? 0.6741 0.3558 0.5910 -0.0309 -0.1639 -0.0141 25   VAL B O   
9013  C CB  . VAL B 27   ? 0.6104 0.3409 0.5353 -0.0392 -0.1449 -0.0060 25   VAL B CB  
9014  C CG1 . VAL B 27   ? 0.6208 0.3379 0.5408 -0.0415 -0.1517 0.0009  25   VAL B CG1 
9015  C CG2 . VAL B 27   ? 0.5558 0.3059 0.4863 -0.0345 -0.1369 -0.0077 25   VAL B CG2 
9016  N N   . ARG B 28   ? 0.6001 0.2948 0.5170 -0.0428 -0.1583 -0.0132 26   ARG B N   
9017  C CA  . ARG B 28   ? 0.6454 0.3185 0.5561 -0.0473 -0.1674 -0.0120 26   ARG B CA  
9018  C C   . ARG B 28   ? 0.6528 0.3259 0.5628 -0.0506 -0.1669 -0.0166 26   ARG B C   
9019  O O   . ARG B 28   ? 0.5792 0.2703 0.4932 -0.0518 -0.1595 -0.0181 26   ARG B O   
9020  C CB  . ARG B 28   ? 0.6976 0.3650 0.6043 -0.0582 -0.1715 -0.0006 26   ARG B CB  
9021  C CG  . ARG B 28   ? 0.6773 0.3607 0.5855 -0.0687 -0.1661 0.0057  26   ARG B CG  
9022  C CD  . ARG B 28   ? 0.7249 0.4071 0.6300 -0.0778 -0.1682 0.0173  26   ARG B CD  
9023  N NE  . ARG B 28   ? 0.7007 0.3920 0.6069 -0.0734 -0.1644 0.0201  26   ARG B NE  
9024  C CZ  . ARG B 28   ? 0.7526 0.4318 0.6553 -0.0707 -0.1697 0.0232  26   ARG B CZ  
9025  N NH1 . ARG B 28   ? 0.7426 0.3993 0.6405 -0.0716 -0.1791 0.0240  26   ARG B NH1 
9026  N NH2 . ARG B 28   ? 0.6950 0.3842 0.5988 -0.0670 -0.1659 0.0255  26   ARG B NH2 
9027  N N   . PRO B 29   ? 0.6860 0.3399 0.5908 -0.0518 -0.1746 -0.0189 27   PRO B N   
9028  C CA  . PRO B 29   ? 0.6703 0.3267 0.5741 -0.0562 -0.1740 -0.0216 27   PRO B CA  
9029  C C   . PRO B 29   ? 0.6756 0.3410 0.5802 -0.0695 -0.1726 -0.0132 27   PRO B C   
9030  O O   . PRO B 29   ? 0.7121 0.3748 0.6153 -0.0772 -0.1752 -0.0039 27   PRO B O   
9031  C CB  . PRO B 29   ? 0.7084 0.3478 0.6070 -0.0548 -0.1811 -0.0226 27   PRO B CB  
9032  C CG  . PRO B 29   ? 0.7134 0.3441 0.6117 -0.0446 -0.1835 -0.0251 27   PRO B CG  
9033  C CD  . PRO B 29   ? 0.6262 0.2641 0.5275 -0.0464 -0.1811 -0.0192 27   PRO B CD  
9034  N N   . GLN B 30   ? 0.6804 0.3588 0.5877 -0.0717 -0.1677 -0.0163 28   GLN B N   
9035  C CA  . GLN B 30   ? 0.6501 0.3429 0.5601 -0.0826 -0.1642 -0.0087 28   GLN B CA  
9036  C C   . GLN B 30   ? 0.6562 0.3376 0.5624 -0.0924 -0.1712 -0.0042 28   GLN B C   
9037  O O   . GLN B 30   ? 0.6535 0.3296 0.5576 -0.0903 -0.1734 -0.0098 28   GLN B O   
9038  C CB  . GLN B 30   ? 0.6615 0.3743 0.5764 -0.0801 -0.1560 -0.0134 28   GLN B CB  
9039  C CG  . GLN B 30   ? 0.5555 0.2805 0.4744 -0.0692 -0.1486 -0.0185 28   GLN B CG  
9040  C CD  . GLN B 30   ? 0.5865 0.3241 0.5087 -0.0704 -0.1438 -0.0113 28   GLN B CD  
9041  O OE1 . GLN B 30   ? 0.5286 0.2837 0.4545 -0.0752 -0.1378 -0.0070 28   GLN B OE1 
9042  N NE2 . GLN B 30   ? 0.5954 0.3243 0.5162 -0.0658 -0.1464 -0.0102 28   GLN B NE2 
9043  N N   . SER B 31   ? 0.6227 0.3040 0.5285 -0.1020 -0.1733 0.0063  29   SER B N   
9044  C CA  . SER B 31   ? 0.6056 0.2822 0.5096 -0.1114 -0.1780 0.0122  29   SER B CA  
9045  C C   . SER B 31   ? 0.6413 0.3324 0.5493 -0.1182 -0.1746 0.0125  29   SER B C   
9046  O O   . SER B 31   ? 0.6266 0.3323 0.5388 -0.1168 -0.1684 0.0096  29   SER B O   
9047  C CB  . SER B 31   ? 0.6935 0.3687 0.5965 -0.1200 -0.1802 0.0240  29   SER B CB  
9048  O OG  . SER B 31   ? 0.6439 0.3367 0.5515 -0.1267 -0.1741 0.0300  29   SER B OG  
9049  N N   . THR B 32   ? 0.6385 0.3256 0.5452 -0.1257 -0.1790 0.0163  30   THR B N   
9050  C CA  . THR B 32   ? 0.6325 0.3335 0.5434 -0.1328 -0.1764 0.0176  30   THR B CA  
9051  C C   . THR B 32   ? 0.5759 0.2964 0.4928 -0.1397 -0.1702 0.0250  30   THR B C   
9052  O O   . THR B 32   ? 0.5948 0.3307 0.5164 -0.1402 -0.1650 0.0225  30   THR B O   
9053  C CB  . THR B 32   ? 0.6903 0.3837 0.5992 -0.1407 -0.1828 0.0222  30   THR B CB  
9054  O OG1 . THR B 32   ? 0.7374 0.4135 0.6405 -0.1337 -0.1881 0.0143  30   THR B OG1 
9055  C CG2 . THR B 32   ? 0.6868 0.3956 0.6008 -0.1485 -0.1804 0.0244  30   THR B CG2 
9056  N N   . LEU B 33   ? 0.5668 0.2871 0.4834 -0.1447 -0.1705 0.0340  31   LEU B N   
9057  C CA  . LEU B 33   ? 0.5702 0.3092 0.4920 -0.1510 -0.1642 0.0414  31   LEU B CA  
9058  C C   . LEU B 33   ? 0.5737 0.3278 0.4984 -0.1396 -0.1549 0.0356  31   LEU B C   
9059  O O   . LEU B 33   ? 0.5295 0.3053 0.4598 -0.1402 -0.1469 0.0373  31   LEU B O   
9060  C CB  . LEU B 33   ? 0.5638 0.2993 0.4835 -0.1574 -0.1660 0.0522  31   LEU B CB  
9061  C CG  . LEU B 33   ? 0.6145 0.3468 0.5337 -0.1668 -0.1709 0.0596  31   LEU B CG  
9062  C CD1 . LEU B 33   ? 0.6185 0.3428 0.5337 -0.1709 -0.1740 0.0687  31   LEU B CD1 
9063  C CD2 . LEU B 33   ? 0.5814 0.3346 0.5078 -0.1756 -0.1662 0.0648  31   LEU B CD2 
9064  N N   . ARG B 34   ? 0.5402 0.2832 0.4613 -0.1292 -0.1559 0.0288  32   ARG B N   
9065  C CA  . ARG B 34   ? 0.5640 0.3211 0.4883 -0.1187 -0.1475 0.0233  32   ARG B CA  
9066  C C   . ARG B 34   ? 0.5526 0.3193 0.4802 -0.1146 -0.1436 0.0152  32   ARG B C   
9067  O O   . ARG B 34   ? 0.4906 0.2763 0.4229 -0.1109 -0.1353 0.0139  32   ARG B O   
9068  C CB  . ARG B 34   ? 0.5714 0.3147 0.4919 -0.1088 -0.1499 0.0184  32   ARG B CB  
9069  C CG  . ARG B 34   ? 0.5605 0.2981 0.4781 -0.1112 -0.1520 0.0263  32   ARG B CG  
9070  C CD  . ARG B 34   ? 0.5667 0.3244 0.4877 -0.1092 -0.1432 0.0300  32   ARG B CD  
9071  N NE  . ARG B 34   ? 0.5721 0.3373 0.4958 -0.0977 -0.1378 0.0218  32   ARG B NE  
9072  C CZ  . ARG B 34   ? 0.5880 0.3486 0.5103 -0.0901 -0.1380 0.0200  32   ARG B CZ  
9073  N NH1 . ARG B 34   ? 0.5646 0.3123 0.4822 -0.0920 -0.1434 0.0255  32   ARG B NH1 
9074  N NH2 . ARG B 34   ? 0.5623 0.3316 0.4880 -0.0805 -0.1327 0.0129  32   ARG B NH2 
9075  N N   . ARG B 35   ? 0.5286 0.2820 0.4532 -0.1154 -0.1498 0.0099  33   ARG B N   
9076  C CA  . ARG B 35   ? 0.5415 0.3034 0.4683 -0.1121 -0.1467 0.0026  33   ARG B CA  
9077  C C   . ARG B 35   ? 0.5316 0.3132 0.4642 -0.1199 -0.1421 0.0079  33   ARG B C   
9078  O O   . ARG B 35   ? 0.4938 0.2906 0.4301 -0.1159 -0.1358 0.0039  33   ARG B O   
9079  C CB  . ARG B 35   ? 0.6060 0.3484 0.5272 -0.1121 -0.1550 -0.0038 33   ARG B CB  
9080  C CG  . ARG B 35   ? 0.6568 0.3804 0.5726 -0.1026 -0.1591 -0.0109 33   ARG B CG  
9081  C CD  . ARG B 35   ? 0.7025 0.4129 0.6133 -0.1000 -0.1643 -0.0174 33   ARG B CD  
9082  N NE  . ARG B 35   ? 0.7931 0.4871 0.6993 -0.0908 -0.1677 -0.0224 33   ARG B NE  
9083  C CZ  . ARG B 35   ? 0.8342 0.5278 0.7404 -0.0797 -0.1646 -0.0301 33   ARG B CZ  
9084  N NH1 . ARG B 35   ? 0.7787 0.4863 0.6884 -0.0763 -0.1582 -0.0342 33   ARG B NH1 
9085  N NH2 . ARG B 35   ? 0.8737 0.5531 0.7763 -0.0718 -0.1681 -0.0335 33   ARG B NH2 
9086  N N   . ALA B 36   ? 0.5216 0.3033 0.4551 -0.1312 -0.1455 0.0170  34   ALA B N   
9087  C CA  . ALA B 36   ? 0.4966 0.2981 0.4365 -0.1386 -0.1411 0.0224  34   ALA B CA  
9088  C C   . ALA B 36   ? 0.4778 0.3009 0.4227 -0.1345 -0.1309 0.0249  34   ALA B C   
9089  O O   . ALA B 36   ? 0.4641 0.3052 0.4144 -0.1343 -0.1251 0.0244  34   ALA B O   
9090  C CB  . ALA B 36   ? 0.5304 0.3281 0.4707 -0.1517 -0.1467 0.0323  34   ALA B CB  
9091  N N   . ILE B 37   ? 0.4769 0.2978 0.4199 -0.1307 -0.1289 0.0273  35   ILE B N   
9092  C CA  . ILE B 37   ? 0.4715 0.3105 0.4181 -0.1257 -0.1197 0.0285  35   ILE B CA  
9093  C C   . ILE B 37   ? 0.4564 0.3025 0.4050 -0.1158 -0.1146 0.0193  35   ILE B C   
9094  O O   . ILE B 37   ? 0.4214 0.2859 0.3750 -0.1146 -0.1078 0.0193  35   ILE B O   
9095  C CB  . ILE B 37   ? 0.4739 0.3059 0.4167 -0.1227 -0.1199 0.0317  35   ILE B CB  
9096  C CG1 . ILE B 37   ? 0.4557 0.2852 0.3970 -0.1331 -0.1230 0.0424  35   ILE B CG1 
9097  C CG2 . ILE B 37   ? 0.4027 0.2497 0.3479 -0.1147 -0.1112 0.0297  35   ILE B CG2 
9098  C CD1 . ILE B 37   ? 0.4784 0.2970 0.4145 -0.1307 -0.1252 0.0455  35   ILE B CD1 
9099  N N   . THR B 38   ? 0.4275 0.2592 0.3722 -0.1082 -0.1179 0.0114  36   THR B N   
9100  C CA  . THR B 38   ? 0.4272 0.2649 0.3735 -0.0986 -0.1132 0.0028  36   THR B CA  
9101  C C   . THR B 38   ? 0.4370 0.2840 0.3861 -0.1007 -0.1116 0.0000  36   THR B C   
9102  O O   . THR B 38   ? 0.4377 0.2992 0.3905 -0.0959 -0.1050 -0.0031 36   THR B O   
9103  C CB  . THR B 38   ? 0.5036 0.3233 0.4451 -0.0910 -0.1178 -0.0046 36   THR B CB  
9104  O OG1 . THR B 38   ? 0.4856 0.2971 0.4248 -0.0891 -0.1196 -0.0015 36   THR B OG1 
9105  C CG2 . THR B 38   ? 0.4555 0.2825 0.3989 -0.0810 -0.1124 -0.0132 36   THR B CG2 
9106  N N   . ALA B 39   ? 0.4274 0.2662 0.3747 -0.1082 -0.1180 0.0014  37   ALA B N   
9107  C CA  . ALA B 39   ? 0.4606 0.3074 0.4102 -0.1110 -0.1176 -0.0009 37   ALA B CA  
9108  C C   . ALA B 39   ? 0.4586 0.3282 0.4153 -0.1146 -0.1108 0.0047  37   ALA B C   
9109  O O   . ALA B 39   ? 0.4377 0.3178 0.3972 -0.1137 -0.1081 0.0018  37   ALA B O   
9110  C CB  . ALA B 39   ? 0.4611 0.2940 0.4074 -0.1195 -0.1267 0.0005  37   ALA B CB  
9111  N N   . ALA B 40   ? 0.4149 0.2924 0.3742 -0.1184 -0.1079 0.0126  38   ALA B N   
9112  C CA  . ALA B 40   ? 0.4255 0.3245 0.3914 -0.1215 -0.1014 0.0179  38   ALA B CA  
9113  C C   . ALA B 40   ? 0.3864 0.2981 0.3545 -0.1130 -0.0929 0.0158  38   ALA B C   
9114  O O   . ALA B 40   ? 0.3821 0.3117 0.3555 -0.1142 -0.0870 0.0194  38   ALA B O   
9115  C CB  . ALA B 40   ? 0.4109 0.3133 0.3785 -0.1312 -0.1027 0.0282  38   ALA B CB  
9116  N N   . TYR B 41   ? 0.3730 0.2759 0.3376 -0.1045 -0.0924 0.0099  39   TYR B N   
9117  C CA  . TYR B 41   ? 0.3808 0.2936 0.3470 -0.0970 -0.0852 0.0084  39   TYR B CA  
9118  C C   . TYR B 41   ? 0.4006 0.3323 0.3724 -0.0954 -0.0785 0.0078  39   TYR B C   
9119  O O   . TYR B 41   ? 0.3684 0.3135 0.3431 -0.0951 -0.0728 0.0118  39   TYR B O   
9120  C CB  . TYR B 41   ? 0.3947 0.2960 0.3575 -0.0880 -0.0863 0.0005  39   TYR B CB  
9121  C CG  . TYR B 41   ? 0.3887 0.2934 0.3517 -0.0812 -0.0818 -0.0002 39   TYR B CG  
9122  C CD1 . TYR B 41   ? 0.3554 0.2761 0.3218 -0.0805 -0.0751 0.0031  39   TYR B CD1 
9123  C CD2 . TYR B 41   ? 0.4100 0.3020 0.3698 -0.0751 -0.0845 -0.0046 39   TYR B CD2 
9124  C CE1 . TYR B 41   ? 0.3918 0.3148 0.3580 -0.0744 -0.0715 0.0020  39   TYR B CE1 
9125  C CE2 . TYR B 41   ? 0.3860 0.2812 0.3463 -0.0691 -0.0810 -0.0053 39   TYR B CE2 
9126  C CZ  . TYR B 41   ? 0.3872 0.2976 0.3505 -0.0690 -0.0746 -0.0020 39   TYR B CZ  
9127  O OH  . TYR B 41   ? 0.3860 0.2990 0.3493 -0.0631 -0.0716 -0.0030 39   TYR B OH  
9128  N N   . ARG B 42   ? 0.3329 0.2658 0.3057 -0.0945 -0.0794 0.0030  40   ARG B N   
9129  C CA  . ARG B 42   ? 0.3332 0.2831 0.3109 -0.0921 -0.0733 0.0021  40   ARG B CA  
9130  C C   . ARG B 42   ? 0.3453 0.3002 0.3255 -0.0985 -0.0759 0.0036  40   ARG B C   
9131  O O   . ARG B 42   ? 0.3682 0.3308 0.3506 -0.0957 -0.0736 0.0000  40   ARG B O   
9132  C CB  . ARG B 42   ? 0.3847 0.3342 0.3615 -0.0827 -0.0700 -0.0056 40   ARG B CB  
9133  C CG  . ARG B 42   ? 0.3603 0.3080 0.3360 -0.0769 -0.0670 -0.0061 40   ARG B CG  
9134  C CD  . ARG B 42   ? 0.3812 0.3293 0.3569 -0.0680 -0.0637 -0.0129 40   ARG B CD  
9135  N NE  . ARG B 42   ? 0.3755 0.3175 0.3494 -0.0636 -0.0633 -0.0134 40   ARG B NE  
9136  C CZ  . ARG B 42   ? 0.3586 0.3087 0.3342 -0.0613 -0.0587 -0.0110 40   ARG B CZ  
9137  N NH1 . ARG B 42   ? 0.3013 0.2659 0.2804 -0.0623 -0.0537 -0.0082 40   ARG B NH1 
9138  N NH2 . ARG B 42   ? 0.3630 0.3062 0.3366 -0.0576 -0.0595 -0.0117 40   ARG B NH2 
9139  N N   . ARG B 43   ? 0.3409 0.2919 0.3212 -0.1073 -0.0808 0.0093  41   ARG B N   
9140  C CA  . ARG B 43   ? 0.3857 0.3405 0.3687 -0.1144 -0.0845 0.0112  41   ARG B CA  
9141  C C   . ARG B 43   ? 0.3735 0.3495 0.3636 -0.1145 -0.0784 0.0139  41   ARG B C   
9142  O O   . ARG B 43   ? 0.3703 0.3581 0.3638 -0.1133 -0.0726 0.0181  41   ARG B O   
9143  C CB  . ARG B 43   ? 0.3912 0.3397 0.3740 -0.1245 -0.0903 0.0182  41   ARG B CB  
9144  C CG  . ARG B 43   ? 0.3886 0.3406 0.3747 -0.1334 -0.0951 0.0213  41   ARG B CG  
9145  C CD  . ARG B 43   ? 0.4281 0.3674 0.4120 -0.1426 -0.1025 0.0266  41   ARG B CD  
9146  N NE  . ARG B 43   ? 0.4640 0.3806 0.4397 -0.1396 -0.1086 0.0206  41   ARG B NE  
9147  C CZ  . ARG B 43   ? 0.4872 0.3882 0.4586 -0.1436 -0.1142 0.0235  41   ARG B CZ  
9148  N NH1 . ARG B 43   ? 0.4493 0.3546 0.4233 -0.1511 -0.1142 0.0327  41   ARG B NH1 
9149  N NH2 . ARG B 43   ? 0.4857 0.3663 0.4498 -0.1399 -0.1198 0.0171  41   ARG B NH2 
9150  N N   . PRO B 44   ? 0.4146 0.3956 0.4067 -0.1155 -0.0798 0.0115  42   PRO B N   
9151  C CA  . PRO B 44   ? 0.4042 0.4055 0.4036 -0.1157 -0.0746 0.0145  42   PRO B CA  
9152  C C   . PRO B 44   ? 0.3486 0.3617 0.3539 -0.1228 -0.0730 0.0237  42   PRO B C   
9153  O O   . PRO B 44   ? 0.3539 0.3609 0.3589 -0.1310 -0.0782 0.0284  42   PRO B O   
9154  C CB  . PRO B 44   ? 0.4119 0.4128 0.4116 -0.1183 -0.0791 0.0115  42   PRO B CB  
9155  C CG  . PRO B 44   ? 0.4530 0.4350 0.4443 -0.1140 -0.0833 0.0036  42   PRO B CG  
9156  C CD  . PRO B 44   ? 0.4244 0.3928 0.4118 -0.1157 -0.0860 0.0054  42   PRO B CD  
9157  N N   . GLU B 45   ? 0.3314 0.3616 0.3419 -0.1195 -0.0657 0.0263  43   GLU B N   
9158  C CA  . GLU B 45   ? 0.3790 0.4225 0.3950 -0.1249 -0.0628 0.0349  43   GLU B CA  
9159  C C   . GLU B 45   ? 0.3768 0.4277 0.3988 -0.1344 -0.0671 0.0401  43   GLU B C   
9160  O O   . GLU B 45   ? 0.3973 0.4528 0.4225 -0.1419 -0.0679 0.0477  43   GLU B O   
9161  C CB  . GLU B 45   ? 0.3807 0.4408 0.4007 -0.1182 -0.0541 0.0353  43   GLU B CB  
9162  C CG  . GLU B 45   ? 0.3430 0.4130 0.3652 -0.1202 -0.0494 0.0423  43   GLU B CG  
9163  C CD  . GLU B 45   ? 0.3095 0.3875 0.3313 -0.1112 -0.0416 0.0403  43   GLU B CD  
9164  O OE1 . GLU B 45   ? 0.2951 0.3696 0.3147 -0.1036 -0.0400 0.0336  43   GLU B OE1 
9165  O OE2 . GLU B 45   ? 0.3259 0.4136 0.3492 -0.1120 -0.0371 0.0456  43   GLU B OE2 
9166  N N   . THR B 46   ? 0.3351 0.3872 0.3588 -0.1346 -0.0702 0.0365  44   THR B N   
9167  C CA  . THR B 46   ? 0.3885 0.4467 0.4178 -0.1440 -0.0753 0.0412  44   THR B CA  
9168  C C   . THR B 46   ? 0.3889 0.4299 0.4138 -0.1523 -0.0840 0.0425  44   THR B C   
9169  O O   . THR B 46   ? 0.3573 0.4032 0.3873 -0.1618 -0.0884 0.0484  44   THR B O   
9170  C CB  . THR B 46   ? 0.4095 0.4727 0.4408 -0.1418 -0.0768 0.0367  44   THR B CB  
9171  O OG1 . THR B 46   ? 0.4010 0.4476 0.4236 -0.1360 -0.0793 0.0280  44   THR B OG1 
9172  C CG2 . THR B 46   ? 0.3339 0.4167 0.3716 -0.1357 -0.0690 0.0374  44   THR B CG2 
9173  N N   . GLU B 47   ? 0.3747 0.3958 0.3907 -0.1489 -0.0870 0.0372  45   GLU B N   
9174  C CA  . GLU B 47   ? 0.3624 0.3661 0.3738 -0.1564 -0.0953 0.0389  45   GLU B CA  
9175  C C   . GLU B 47   ? 0.3934 0.3953 0.4045 -0.1602 -0.0940 0.0458  45   GLU B C   
9176  O O   . GLU B 47   ? 0.3947 0.3888 0.4055 -0.1694 -0.1002 0.0508  45   GLU B O   
9177  C CB  . GLU B 47   ? 0.4426 0.4247 0.4444 -0.1511 -0.0999 0.0298  45   GLU B CB  
9178  C CG  . GLU B 47   ? 0.4773 0.4583 0.4774 -0.1479 -0.1022 0.0228  45   GLU B CG  
9179  C CD  . GLU B 47   ? 0.5796 0.5415 0.5701 -0.1407 -0.1046 0.0136  45   GLU B CD  
9180  O OE1 . GLU B 47   ? 0.5964 0.5423 0.5816 -0.1413 -0.1081 0.0132  45   GLU B OE1 
9181  O OE2 . GLU B 47   ? 0.5411 0.5044 0.5295 -0.1343 -0.1029 0.0070  45   GLU B OE2 
9182  N N   . CYS B 48   ? 0.3784 0.3868 0.3892 -0.1536 -0.0865 0.0462  46   CYS B N   
9183  C CA  . CYS B 48   ? 0.4094 0.4161 0.4188 -0.1568 -0.0852 0.0528  46   CYS B CA  
9184  C C   . CYS B 48   ? 0.3925 0.4165 0.4100 -0.1657 -0.0834 0.0628  46   CYS B C   
9185  O O   . CYS B 48   ? 0.3736 0.3927 0.3903 -0.1735 -0.0865 0.0697  46   CYS B O   
9186  C CB  . CYS B 48   ? 0.3423 0.3523 0.3490 -0.1473 -0.0776 0.0504  46   CYS B CB  
9187  S SG  . CYS B 48   ? 0.4159 0.4070 0.4140 -0.1370 -0.0790 0.0398  46   CYS B SG  
9188  N N   . LEU B 49   ? 0.3563 0.4006 0.3817 -0.1645 -0.0783 0.0642  47   LEU B N   
9189  C CA  . LEU B 49   ? 0.4100 0.4735 0.4433 -0.1707 -0.0743 0.0737  47   LEU B CA  
9190  C C   . LEU B 49   ? 0.3982 0.4635 0.4369 -0.1835 -0.0809 0.0810  47   LEU B C   
9191  O O   . LEU B 49   ? 0.4062 0.4793 0.4481 -0.1902 -0.0793 0.0898  47   LEU B O   
9192  C CB  . LEU B 49   ? 0.3938 0.4794 0.4345 -0.1649 -0.0666 0.0731  47   LEU B CB  
9193  C CG  . LEU B 49   ? 0.3633 0.4577 0.4025 -0.1571 -0.0575 0.0737  47   LEU B CG  
9194  C CD1 . LEU B 49   ? 0.3408 0.4421 0.3813 -0.1634 -0.0551 0.0830  47   LEU B CD1 
9195  C CD2 . LEU B 49   ? 0.3538 0.4309 0.3834 -0.1487 -0.0573 0.0661  47   LEU B CD2 
9196  N N   . PRO B 50   ? 0.4190 0.4777 0.4587 -0.1877 -0.0883 0.0781  48   PRO B N   
9197  C CA  . PRO B 50   ? 0.4253 0.4880 0.4714 -0.2006 -0.0945 0.0856  48   PRO B CA  
9198  C C   . PRO B 50   ? 0.4451 0.4941 0.4870 -0.2091 -0.0995 0.0918  48   PRO B C   
9199  O O   . PRO B 50   ? 0.4102 0.4699 0.4573 -0.2153 -0.0982 0.1006  48   PRO B O   
9200  C CB  . PRO B 50   ? 0.4397 0.4930 0.4846 -0.2017 -0.1022 0.0792  48   PRO B CB  
9201  C CG  . PRO B 50   ? 0.4187 0.4767 0.4620 -0.1897 -0.0966 0.0709  48   PRO B CG  
9202  C CD  . PRO B 50   ? 0.4231 0.4758 0.4601 -0.1810 -0.0902 0.0685  48   PRO B CD  
9203  N N   . PRO B 51   ? 0.4421 0.4669 0.4734 -0.2065 -0.1041 0.0868  49   PRO B N   
9204  C CA  . PRO B 51   ? 0.4614 0.4735 0.4884 -0.2134 -0.1081 0.0932  49   PRO B CA  
9205  C C   . PRO B 51   ? 0.4621 0.4863 0.4904 -0.2133 -0.1004 0.1005  49   PRO B C   
9206  O O   . PRO B 51   ? 0.4968 0.5203 0.5251 -0.2206 -0.1018 0.1089  49   PRO B O   
9207  C CB  . PRO B 51   ? 0.4797 0.4648 0.4954 -0.2084 -0.1138 0.0850  49   PRO B CB  
9208  C CG  . PRO B 51   ? 0.4725 0.4603 0.4863 -0.1959 -0.1087 0.0752  49   PRO B CG  
9209  C CD  . PRO B 51   ? 0.4585 0.4659 0.4813 -0.1973 -0.1064 0.0756  49   PRO B CD  
9210  N N   . LEU B 52   ? 0.4105 0.4448 0.4382 -0.2027 -0.0915 0.0967  50   LEU B N   
9211  C CA  . LEU B 52   ? 0.4451 0.4915 0.4732 -0.2014 -0.0837 0.1030  50   LEU B CA  
9212  C C   . LEU B 52   ? 0.4546 0.5258 0.4936 -0.2087 -0.0795 0.1124  50   LEU B C   
9213  O O   . LEU B 52   ? 0.4665 0.5432 0.5064 -0.2154 -0.0779 0.1216  50   LEU B O   
9214  C CB  . LEU B 52   ? 0.4176 0.4684 0.4423 -0.1881 -0.0757 0.0961  50   LEU B CB  
9215  C CG  . LEU B 52   ? 0.4009 0.4300 0.4154 -0.1799 -0.0782 0.0874  50   LEU B CG  
9216  C CD1 . LEU B 52   ? 0.3334 0.3706 0.3466 -0.1676 -0.0699 0.0813  50   LEU B CD1 
9217  C CD2 . LEU B 52   ? 0.4223 0.4357 0.4293 -0.1838 -0.0819 0.0918  50   LEU B CD2 
9218  N N   . VAL B 53   ? 0.3753 0.4618 0.4227 -0.2075 -0.0777 0.1104  51   VAL B N   
9219  C CA  . VAL B 53   ? 0.4301 0.5407 0.4890 -0.2139 -0.0743 0.1189  51   VAL B CA  
9220  C C   . VAL B 53   ? 0.4750 0.5789 0.5334 -0.2225 -0.0803 0.1256  51   VAL B C   
9221  O O   . VAL B 53   ? 0.4471 0.5645 0.5094 -0.2261 -0.0763 0.1340  51   VAL B O   
9222  C CB  . VAL B 53   ? 0.4117 0.5351 0.4785 -0.2106 -0.0738 0.1145  51   VAL B CB  
9223  C CG1 . VAL B 53   ? 0.4378 0.5829 0.5147 -0.2138 -0.0707 0.1218  51   VAL B CG1 
9224  C CG2 . VAL B 53   ? 0.4083 0.5384 0.4736 -0.1980 -0.0662 0.1073  51   VAL B CG2 
9225  N N   . GLU B 54   ? 0.4606 0.5437 0.5142 -0.2257 -0.0899 0.1219  52   GLU B N   
9226  C CA  . GLU B 54   ? 0.4755 0.5515 0.5287 -0.2340 -0.0962 0.1280  52   GLU B CA  
9227  C C   . GLU B 54   ? 0.5094 0.5790 0.5571 -0.2374 -0.0953 0.1347  52   GLU B C   
9228  O O   . GLU B 54   ? 0.4621 0.5408 0.5133 -0.2435 -0.0946 0.1434  52   GLU B O   
9229  C CB  . GLU B 54   ? 0.4989 0.5519 0.5464 -0.2356 -0.1066 0.1218  52   GLU B CB  
9230  N N   . ALA B 55   ? 0.4640 0.5184 0.5029 -0.2336 -0.0953 0.1310  53   ALA B N   
9231  C CA  . ALA B 55   ? 0.5236 0.5712 0.5563 -0.2362 -0.0945 0.1372  53   ALA B CA  
9232  C C   . ALA B 55   ? 0.4909 0.5622 0.5281 -0.2356 -0.0842 0.1444  53   ALA B C   
9233  O O   . ALA B 55   ? 0.4940 0.5666 0.5290 -0.2400 -0.0834 0.1523  53   ALA B O   
9234  C CB  . ALA B 55   ? 0.4991 0.5251 0.5214 -0.2314 -0.0969 0.1311  53   ALA B CB  
9235  N N   . ALA B 56   ? 0.4716 0.5615 0.5145 -0.2296 -0.0764 0.1416  54   ALA B N   
9236  C CA  . ALA B 56   ? 0.4816 0.5937 0.5278 -0.2272 -0.0660 0.1472  54   ALA B CA  
9237  C C   . ALA B 56   ? 0.4849 0.6195 0.5415 -0.2304 -0.0628 0.1535  54   ALA B C   
9238  O O   . ALA B 56   ? 0.4667 0.6217 0.5270 -0.2273 -0.0538 0.1574  54   ALA B O   
9239  C CB  . ALA B 56   ? 0.4440 0.5654 0.4910 -0.2183 -0.0587 0.1412  54   ALA B CB  
9240  N N   . THR B 57   ? 0.4930 0.6240 0.5540 -0.2363 -0.0700 0.1545  55   THR B N   
9241  C CA  . THR B 57   ? 0.5383 0.6904 0.6099 -0.2396 -0.0677 0.1601  55   THR B CA  
9242  C C   . THR B 57   ? 0.5273 0.6848 0.5985 -0.2458 -0.0663 0.1701  55   THR B C   
9243  O O   . THR B 57   ? 0.5210 0.6605 0.5854 -0.2516 -0.0728 0.1728  55   THR B O   
9244  C CB  . THR B 57   ? 0.5073 0.6527 0.5830 -0.2439 -0.0763 0.1577  55   THR B CB  
9245  O OG1 . THR B 57   ? 0.4986 0.6463 0.5769 -0.2374 -0.0755 0.1493  55   THR B OG1 
9246  C CG2 . THR B 57   ? 0.5517 0.7151 0.6372 -0.2495 -0.0758 0.1651  55   THR B CG2 
9247  N N   . GLN B 58   ? 0.5486 0.7310 0.6271 -0.2442 -0.0578 0.1752  56   GLN B N   
9248  C CA  . GLN B 58   ? 0.5982 0.7894 0.6777 -0.2498 -0.0556 0.1848  56   GLN B CA  
9249  C C   . GLN B 58   ? 0.5718 0.7859 0.6638 -0.2522 -0.0532 0.1895  56   GLN B C   
9250  O O   . GLN B 58   ? 0.5460 0.7757 0.6456 -0.2464 -0.0487 0.1859  56   GLN B O   
9251  C CB  . GLN B 58   ? 0.5681 0.7670 0.6422 -0.2447 -0.0464 0.1870  56   GLN B CB  
9252  N N   . SER B 59   ? 0.6297 0.8458 0.7240 -0.2608 -0.0563 0.1977  57   SER B N   
9253  C CA  . SER B 59   ? 0.5537 0.7900 0.6599 -0.2645 -0.0552 0.2032  57   SER B CA  
9254  C C   . SER B 59   ? 0.6004 0.8639 0.7134 -0.2572 -0.0435 0.2045  57   SER B C   
9255  O O   . SER B 59   ? 0.6026 0.8693 0.7101 -0.2505 -0.0360 0.2029  57   SER B O   
9256  C CB  . SER B 59   ? 0.6129 0.8465 0.7192 -0.2750 -0.0597 0.2125  57   SER B CB  
9257  N N   . LYS B 60   ? 0.5778 0.8606 0.7027 -0.2584 -0.0421 0.2074  58   LYS B N   
9258  C CA  . LYS B 60   ? 0.5778 0.8865 0.7099 -0.2509 -0.0314 0.2082  58   LYS B CA  
9259  C C   . LYS B 60   ? 0.5873 0.9064 0.7168 -0.2512 -0.0241 0.2151  58   LYS B C   
9260  O O   . LYS B 60   ? 0.6052 0.9392 0.7350 -0.2427 -0.0144 0.2138  58   LYS B O   
9261  C CB  . LYS B 60   ? 0.5484 0.8749 0.6941 -0.2529 -0.0324 0.2106  58   LYS B CB  
9262  N N   . GLU B 61   ? 0.5817 0.8930 0.7082 -0.2607 -0.0287 0.2223  59   GLU B N   
9263  C CA  . GLU B 61   ? 0.5732 0.8930 0.6960 -0.2612 -0.0220 0.2289  59   GLU B CA  
9264  C C   . GLU B 61   ? 0.5882 0.8966 0.6984 -0.2547 -0.0179 0.2247  59   GLU B C   
9265  O O   . GLU B 61   ? 0.5925 0.9144 0.7008 -0.2475 -0.0081 0.2247  59   GLU B O   
9266  C CB  . GLU B 61   ? 0.6413 0.9540 0.7635 -0.2733 -0.0286 0.2377  59   GLU B CB  
9267  N N   . ILE B 62   ? 0.6106 0.8936 0.7115 -0.2569 -0.0254 0.2208  60   ILE B N   
9268  C CA  . ILE B 62   ? 0.5527 0.8233 0.6415 -0.2509 -0.0223 0.2165  60   ILE B CA  
9269  C C   . ILE B 62   ? 0.5919 0.8735 0.6820 -0.2391 -0.0144 0.2090  60   ILE B C   
9270  O O   . ILE B 62   ? 0.5885 0.8740 0.6719 -0.2323 -0.0068 0.2078  60   ILE B O   
9271  C CB  . ILE B 62   ? 0.5809 0.8222 0.6610 -0.2549 -0.0326 0.2128  60   ILE B CB  
9272  C CG1 . ILE B 62   ? 0.5825 0.8114 0.6586 -0.2653 -0.0394 0.2205  60   ILE B CG1 
9273  C CG2 . ILE B 62   ? 0.6021 0.8310 0.6712 -0.2473 -0.0298 0.2065  60   ILE B CG2 
9274  C CD1 . ILE B 62   ? 0.5674 0.7672 0.6360 -0.2697 -0.0506 0.2171  60   ILE B CD1 
9275  N N   . ARG B 63   ? 0.5661 0.8529 0.6645 -0.2364 -0.0161 0.2039  61   ARG B N   
9276  C CA  . ARG B 63   ? 0.5942 0.8906 0.6941 -0.2252 -0.0092 0.1967  61   ARG B CA  
9277  C C   . ARG B 63   ? 0.5638 0.8849 0.6681 -0.2189 0.0018  0.1994  61   ARG B C   
9278  O O   . ARG B 63   ? 0.5730 0.8983 0.6721 -0.2097 0.0093  0.1954  61   ARG B O   
9279  C CB  . ARG B 63   ? 0.5521 0.8495 0.6604 -0.2242 -0.0137 0.1913  61   ARG B CB  
9280  C CG  . ARG B 63   ? 0.5472 0.8215 0.6494 -0.2247 -0.0213 0.1844  61   ARG B CG  
9281  C CD  . ARG B 63   ? 0.5706 0.8492 0.6812 -0.2225 -0.0243 0.1792  61   ARG B CD  
9282  N NE  . ARG B 63   ? 0.5494 0.8250 0.6659 -0.2316 -0.0327 0.1828  61   ARG B NE  
9283  C CZ  . ARG B 63   ? 0.5818 0.8692 0.7086 -0.2315 -0.0341 0.1821  61   ARG B CZ  
9284  N NH1 . ARG B 63   ? 0.5358 0.8403 0.6688 -0.2229 -0.0274 0.1787  61   ARG B NH1 
9285  N NH2 . ARG B 63   ? 0.5294 0.8108 0.6599 -0.2402 -0.0426 0.1850  61   ARG B NH2 
9286  N N   . ASP B 64   ? 0.5467 0.8843 0.6606 -0.2235 0.0027  0.2060  62   ASP B N   
9287  C CA  . ASP B 64   ? 0.5682 0.9295 0.6867 -0.2176 0.0129  0.2089  62   ASP B CA  
9288  C C   . ASP B 64   ? 0.5258 0.8854 0.6335 -0.2158 0.0188  0.2118  62   ASP B C   
9289  O O   . ASP B 64   ? 0.5119 0.8812 0.6163 -0.2061 0.0277  0.2087  62   ASP B O   
9290  C CB  . ASP B 64   ? 0.5326 0.9104 0.6632 -0.2243 0.0119  0.2163  62   ASP B CB  
9291  N N   . ALA B 65   ? 0.5083 0.8549 0.6099 -0.2250 0.0137  0.2176  63   ALA B N   
9292  C CA  . ALA B 65   ? 0.5348 0.8776 0.6251 -0.2240 0.0183  0.2206  63   ALA B CA  
9293  C C   . ALA B 65   ? 0.5772 0.9081 0.6562 -0.2152 0.0212  0.2129  63   ALA B C   
9294  O O   . ALA B 65   ? 0.5210 0.8563 0.5920 -0.2094 0.0286  0.2131  63   ALA B O   
9295  C CB  . ALA B 65   ? 0.5524 0.8794 0.6377 -0.2356 0.0105  0.2275  63   ALA B CB  
9296  N N   . ALA B 66   ? 0.5732 0.8893 0.6511 -0.2140 0.0154  0.2062  64   ALA B N   
9297  C CA  . ALA B 66   ? 0.5619 0.8661 0.6294 -0.2063 0.0174  0.1991  64   ALA B CA  
9298  C C   . ALA B 66   ? 0.5369 0.8577 0.6063 -0.1942 0.0271  0.1937  64   ALA B C   
9299  O O   . ALA B 66   ? 0.5352 0.8562 0.5951 -0.1874 0.0335  0.1918  64   ALA B O   
9300  C CB  . ALA B 66   ? 0.5528 0.8372 0.6192 -0.2086 0.0085  0.1934  64   ALA B CB  
9301  N N   . ALA B 67   ? 0.5578 0.8922 0.6390 -0.1911 0.0280  0.1910  65   ALA B N   
9302  C CA  . ALA B 67   ? 0.5676 0.9169 0.6511 -0.1792 0.0366  0.1854  65   ALA B CA  
9303  C C   . ALA B 67   ? 0.5781 0.9444 0.6603 -0.1747 0.0460  0.1892  65   ALA B C   
9304  O O   . ALA B 67   ? 0.5637 0.9379 0.6428 -0.1639 0.0536  0.1843  65   ALA B O   
9305  C CB  . ALA B 67   ? 0.5559 0.9165 0.6529 -0.1775 0.0351  0.1828  65   ALA B CB  
9306  N N   . SER B 68   ? 0.5803 0.9521 0.6644 -0.1826 0.0455  0.1978  66   SER B N   
9307  C CA  . SER B 68   ? 0.5911 0.9779 0.6726 -0.1789 0.0543  0.2017  66   SER B CA  
9308  C C   . SER B 68   ? 0.5602 0.9346 0.6257 -0.1765 0.0570  0.2011  66   SER B C   
9309  O O   . SER B 68   ? 0.5682 0.9494 0.6275 -0.1668 0.0652  0.1978  66   SER B O   
9310  C CB  . SER B 68   ? 0.5365 0.9342 0.6257 -0.1885 0.0530  0.2114  66   SER B CB  
9311  O OG  . SER B 68   ? 0.6623 1.0782 0.7660 -0.1875 0.0542  0.2119  66   SER B OG  
9312  N N   . THR B 69   ? 0.5904 0.9455 0.6486 -0.1848 0.0498  0.2040  67   THR B N   
9313  C CA  . THR B 69   ? 0.5442 0.8845 0.5866 -0.1824 0.0509  0.2027  67   THR B CA  
9314  C C   . THR B 69   ? 0.5477 0.8835 0.5842 -0.1712 0.0543  0.1931  67   THR B C   
9315  O O   . THR B 69   ? 0.5690 0.9044 0.5945 -0.1640 0.0603  0.1908  67   THR B O   
9316  C CB  . THR B 69   ? 0.5708 0.8888 0.6076 -0.1926 0.0411  0.2060  67   THR B CB  
9317  O OG1 . THR B 69   ? 0.5949 0.9168 0.6361 -0.2028 0.0381  0.2152  67   THR B OG1 
9318  C CG2 . THR B 69   ? 0.5983 0.9000 0.6184 -0.1898 0.0417  0.2045  67   THR B CG2 
9319  N N   . ALA B 70   ? 0.5831 0.9157 0.6264 -0.1694 0.0505  0.1873  68   ALA B N   
9320  C CA  . ALA B 70   ? 0.5435 0.8713 0.5816 -0.1593 0.0532  0.1783  68   ALA B CA  
9321  C C   . ALA B 70   ? 0.5701 0.9164 0.6101 -0.1478 0.0630  0.1745  68   ALA B C   
9322  O O   . ALA B 70   ? 0.5620 0.9049 0.5923 -0.1387 0.0677  0.1690  68   ALA B O   
9323  C CB  . ALA B 70   ? 0.5727 0.8929 0.6180 -0.1607 0.0465  0.1734  68   ALA B CB  
9324  N N   . ARG B 71   ? 0.5898 0.9551 0.6421 -0.1478 0.0659  0.1774  69   ARG B N   
9325  C CA  . ARG B 71   ? 0.5481 0.9307 0.6024 -0.1367 0.0751  0.1741  69   ARG B CA  
9326  C C   . ARG B 71   ? 0.5289 0.9143 0.5717 -0.1332 0.0820  0.1763  69   ARG B C   
9327  O O   . ARG B 71   ? 0.5104 0.8993 0.5468 -0.1222 0.0886  0.1706  69   ARG B O   
9328  C CB  . ARG B 71   ? 0.5745 0.9765 0.6444 -0.1384 0.0761  0.1775  69   ARG B CB  
9329  C CG  . ARG B 71   ? 0.5643 0.9858 0.6362 -0.1294 0.0858  0.1772  69   ARG B CG  
9330  C CD  . ARG B 71   ? 0.5788 1.0171 0.6661 -0.1263 0.0867  0.1762  69   ARG B CD  
9331  N NE  . ARG B 71   ? 0.5874 1.0282 0.6739 -0.1135 0.0910  0.1673  69   ARG B NE  
9332  C CZ  . ARG B 71   ? 0.6188 1.0656 0.7159 -0.1098 0.0893  0.1636  69   ARG B CZ  
9333  N NH1 . ARG B 71   ? 0.6142 1.0653 0.7233 -0.1177 0.0835  0.1675  69   ARG B NH1 
9334  N NH2 . ARG B 71   ? 0.5826 1.0303 0.6776 -0.0978 0.0933  0.1556  69   ARG B NH2 
9335  N N   . LYS B 72   ? 0.5309 0.9144 0.5707 -0.1422 0.0804  0.1845  70   LYS B N   
9336  C CA  . LYS B 72   ? 0.5038 0.8884 0.5314 -0.1396 0.0864  0.1869  70   LYS B CA  
9337  C C   . LYS B 72   ? 0.5974 0.9654 0.6093 -0.1333 0.0868  0.1807  70   LYS B C   
9338  O O   . LYS B 72   ? 0.5791 0.9506 0.5816 -0.1245 0.0938  0.1776  70   LYS B O   
9339  C CB  . LYS B 72   ? 0.5467 0.9289 0.5733 -0.1515 0.0831  0.1969  70   LYS B CB  
9340  N N   . LEU B 73   ? 0.5909 0.9405 0.5996 -0.1375 0.0791  0.1787  71   LEU B N   
9341  C CA  . LEU B 73   ? 0.5976 0.9307 0.5914 -0.1324 0.0787  0.1733  71   LEU B CA  
9342  C C   . LEU B 73   ? 0.5620 0.8994 0.5546 -0.1195 0.0838  0.1637  71   LEU B C   
9343  O O   . LEU B 73   ? 0.5794 0.9132 0.5595 -0.1115 0.0883  0.1596  71   LEU B O   
9344  C CB  . LEU B 73   ? 0.5879 0.9008 0.5797 -0.1402 0.0690  0.1736  71   LEU B CB  
9345  C CG  . LEU B 73   ? 0.5778 0.8831 0.5691 -0.1527 0.0631  0.1827  71   LEU B CG  
9346  C CD1 . LEU B 73   ? 0.5243 0.8115 0.5177 -0.1606 0.0528  0.1825  71   LEU B CD1 
9347  C CD2 . LEU B 73   ? 0.5476 0.8457 0.5235 -0.1526 0.0653  0.1861  71   LEU B CD2 
9348  N N   . ILE B 74   ? 0.5555 0.9002 0.5609 -0.1173 0.0828  0.1600  72   ILE B N   
9349  C CA  . ILE B 74   ? 0.5579 0.9057 0.5627 -0.1052 0.0870  0.1509  72   ILE B CA  
9350  C C   . ILE B 74   ? 0.5590 0.9221 0.5621 -0.0960 0.0961  0.1496  72   ILE B C   
9351  O O   . ILE B 74   ? 0.5635 0.9242 0.5576 -0.0855 0.1005  0.1428  72   ILE B O   
9352  C CB  . ILE B 74   ? 0.5281 0.8801 0.5471 -0.1054 0.0834  0.1478  72   ILE B CB  
9353  N N   . GLU B 75   ? 0.5671 0.9458 0.5785 -0.0997 0.0989  0.1561  73   GLU B N   
9354  C CA  . GLU B 75   ? 0.5900 0.9834 0.5995 -0.0915 0.1077  0.1554  73   GLU B CA  
9355  C C   . GLU B 75   ? 0.5952 0.9801 0.5868 -0.0884 0.1113  0.1551  73   GLU B C   
9356  O O   . GLU B 75   ? 0.5774 0.9636 0.5609 -0.0775 0.1170  0.1488  73   GLU B O   
9357  C CB  . GLU B 75   ? 0.4832 0.8945 0.5046 -0.0975 0.1096  0.1634  73   GLU B CB  
9358  N N   . ALA B 76   ? 0.5820 0.9570 0.5669 -0.0979 0.1074  0.1615  74   ALA B N   
9359  C CA  . ALA B 76   ? 0.5950 0.9610 0.5623 -0.0957 0.1100  0.1617  74   ALA B CA  
9360  C C   . ALA B 76   ? 0.5988 0.9499 0.5539 -0.0872 0.1093  0.1527  74   ALA B C   
9361  O O   . ALA B 76   ? 0.6189 0.9677 0.5608 -0.0794 0.1141  0.1490  74   ALA B O   
9362  C CB  . ALA B 76   ? 0.4750 0.8309 0.4378 -0.1079 0.1046  0.1703  74   ALA B CB  
9363  N N   . LEU B 77   ? 0.5860 0.9268 0.5451 -0.0886 0.1031  0.1489  75   LEU B N   
9364  C CA  . LEU B 77   ? 0.6111 0.9374 0.5589 -0.0812 0.1018  0.1406  75   LEU B CA  
9365  C C   . LEU B 77   ? 0.6182 0.9525 0.5665 -0.0681 0.1079  0.1320  75   LEU B C   
9366  O O   . LEU B 77   ? 0.6412 0.9686 0.5760 -0.0597 0.1106  0.1263  75   LEU B O   
9367  C CB  . LEU B 77   ? 0.5156 0.8293 0.4679 -0.0867 0.0937  0.1392  75   LEU B CB  
9368  N N   . ARG B 78   ? 0.5809 0.9290 0.5444 -0.0659 0.1095  0.1309  76   ARG B N   
9369  C CA  . ARG B 78   ? 0.6157 0.9707 0.5805 -0.0534 0.1147  0.1229  76   ARG B CA  
9370  C C   . ARG B 78   ? 0.6257 0.9907 0.5840 -0.0467 0.1226  0.1229  76   ARG B C   
9371  O O   . ARG B 78   ? 0.5823 0.9499 0.5379 -0.0354 0.1269  0.1156  76   ARG B O   
9372  C CB  . ARG B 78   ? 0.6560 1.0229 0.6389 -0.0533 0.1138  0.1224  76   ARG B CB  
9373  N N   . GLY B 79   ? 0.5720 0.9422 0.5276 -0.0532 0.1245  0.1308  77   GLY B N   
9374  C CA  . GLY B 79   ? 0.6259 1.0053 0.5744 -0.0474 0.1321  0.1312  77   GLY B CA  
9375  C C   . GLY B 79   ? 0.6458 1.0122 0.5741 -0.0434 0.1336  0.1284  77   GLY B C   
9376  O O   . GLY B 79   ? 0.5816 0.9544 0.5023 -0.0374 0.1401  0.1275  77   GLY B O   
9377  N N   . LYS B 80   ? 0.6546 1.0029 0.5739 -0.0465 0.1276  0.1269  78   LYS B N   
9378  C CA  . LYS B 80   ? 0.6380 0.9724 0.5375 -0.0436 0.1277  0.1247  78   LYS B CA  
9379  C C   . LYS B 80   ? 0.7324 1.0498 0.6241 -0.0386 0.1230  0.1164  78   LYS B C   
9380  O O   . LYS B 80   ? 0.7277 1.0437 0.6154 -0.0279 0.1256  0.1077  78   LYS B O   
9381  C CB  . LYS B 80   ? 0.6505 0.9791 0.5444 -0.0549 0.1244  0.1340  78   LYS B CB  
9382  C CG  . LYS B 80   ? 0.6633 0.9821 0.5637 -0.0652 0.1159  0.1379  78   LYS B CG  
9383  C CD  . LYS B 80   ? 0.6616 0.9760 0.5584 -0.0767 0.1127  0.1479  78   LYS B CD  
9384  C CE  . LYS B 80   ? 0.6122 0.9125 0.5123 -0.0860 0.1034  0.1506  78   LYS B CE  
9385  N NZ  . LYS B 80   ? 0.5729 0.8660 0.4684 -0.0970 0.0992  0.1600  78   LYS B NZ  
9386  N N   . GLY B 85   ? 0.6806 0.8702 0.4744 0.0122  0.0935  0.0512  83   GLY B N   
9387  C CA  . GLY B 85   ? 0.6774 0.8668 0.4570 0.0226  0.0978  0.0446  83   GLY B CA  
9388  C C   . GLY B 85   ? 0.6557 0.8342 0.4369 0.0310  0.0945  0.0336  83   GLY B C   
9389  O O   . GLY B 85   ? 0.6586 0.8337 0.4294 0.0400  0.0967  0.0267  83   GLY B O   
9390  N N   . VAL B 86   ? 0.6683 0.8394 0.4634 0.0276  0.0884  0.0318  84   VAL B N   
9391  C CA  . VAL B 86   ? 0.6809 0.8419 0.4787 0.0348  0.0851  0.0220  84   VAL B CA  
9392  C C   . VAL B 86   ? 0.6876 0.8632 0.4926 0.0424  0.0924  0.0191  84   VAL B C   
9393  O O   . VAL B 86   ? 0.6844 0.8539 0.4854 0.0512  0.0923  0.0108  84   VAL B O   
9394  C CB  . VAL B 86   ? 0.6646 0.8136 0.4744 0.0291  0.0767  0.0211  84   VAL B CB  
9395  C CG1 . VAL B 86   ? 0.6796 0.8413 0.5072 0.0229  0.0784  0.0271  84   VAL B CG1 
9396  C CG2 . VAL B 86   ? 0.6410 0.7782 0.4520 0.0361  0.0728  0.0114  84   VAL B CG2 
9397  N N   . GLU B 87   ? 0.7171 0.9120 0.5326 0.0391  0.0985  0.0260  85   GLU B N   
9398  C CA  . GLU B 87   ? 0.6929 0.9010 0.5173 0.0459  0.1048  0.0237  85   GLU B CA  
9399  C C   . GLU B 87   ? 0.6618 0.8693 0.4753 0.0537  0.1092  0.0197  85   GLU B C   
9400  O O   . GLU B 87   ? 0.6039 0.8108 0.4191 0.0624  0.1110  0.0129  85   GLU B O   
9401  C CB  . GLU B 87   ? 0.6549 0.8811 0.4954 0.0392  0.1086  0.0322  85   GLU B CB  
9402  N N   . GLY B 88   ? 0.6544 0.8618 0.4564 0.0506  0.1109  0.0239  86   GLY B N   
9403  C CA  . GLY B 88   ? 0.6631 0.8696 0.4534 0.0577  0.1150  0.0201  86   GLY B CA  
9404  C C   . GLY B 88   ? 0.6555 0.8439 0.4322 0.0653  0.1108  0.0102  86   GLY B C   
9405  O O   . GLY B 88   ? 0.6467 0.8339 0.4182 0.0736  0.1136  0.0042  86   GLY B O   
9406  N N   . LEU B 89   ? 0.6285 0.8027 0.3994 0.0626  0.1035  0.0083  87   LEU B N   
9407  C CA  . LEU B 89   ? 0.6479 0.8042 0.4072 0.0692  0.0983  -0.0012 87   LEU B CA  
9408  C C   . LEU B 89   ? 0.5941 0.7488 0.3632 0.0761  0.0979  -0.0083 87   LEU B C   
9409  O O   . LEU B 89   ? 0.5794 0.7259 0.3419 0.0841  0.0976  -0.0160 87   LEU B O   
9410  C CB  . LEU B 89   ? 0.6159 0.7584 0.3679 0.0640  0.0903  -0.0008 87   LEU B CB  
9411  C CG  . LEU B 89   ? 0.6274 0.7507 0.3624 0.0682  0.0842  -0.0080 87   LEU B CG  
9412  C CD1 . LEU B 89   ? 0.7110 0.8228 0.4428 0.0604  0.0762  -0.0048 87   LEU B CD1 
9413  C CD2 . LEU B 89   ? 0.6241 0.7370 0.3613 0.0757  0.0810  -0.0178 87   LEU B CD2 
9414  N N   . VAL B 90   ? 0.5978 0.7598 0.3827 0.0728  0.0975  -0.0056 88   VAL B N   
9415  C CA  . VAL B 90   ? 0.6067 0.7680 0.4020 0.0788  0.0971  -0.0114 88   VAL B CA  
9416  C C   . VAL B 90   ? 0.6189 0.7896 0.4173 0.0859  0.1034  -0.0134 88   VAL B C   
9417  O O   . VAL B 90   ? 0.5711 0.7343 0.3680 0.0939  0.1025  -0.0209 88   VAL B O   
9418  C CB  . VAL B 90   ? 0.5542 0.7238 0.3659 0.0730  0.0961  -0.0069 88   VAL B CB  
9419  C CG1 . VAL B 90   ? 0.5581 0.7325 0.3828 0.0787  0.0977  -0.0107 88   VAL B CG1 
9420  C CG2 . VAL B 90   ? 0.5840 0.7362 0.3965 0.0666  0.0867  -0.0080 88   VAL B CG2 
9421  N N   . GLN B 91   ? 0.6054 0.7919 0.4074 0.0832  0.1097  -0.0066 89   GLN B N   
9422  C CA  . GLN B 91   ? 0.6243 0.8213 0.4300 0.0899  0.1159  -0.0080 89   GLN B CA  
9423  C C   . GLN B 91   ? 0.6135 0.8015 0.4023 0.0968  0.1169  -0.0138 89   GLN B C   
9424  O O   . GLN B 91   ? 0.6217 0.8092 0.4104 0.1054  0.1190  -0.0195 89   GLN B O   
9425  C CB  . GLN B 91   ? 0.6543 0.8715 0.4697 0.0844  0.1220  0.0013  89   GLN B CB  
9426  N N   . GLU B 92   ? 0.6178 0.7981 0.3919 0.0932  0.1152  -0.0125 90   GLU B N   
9427  C CA  . GLU B 92   ? 0.6026 0.7742 0.3599 0.0993  0.1159  -0.0179 90   GLU B CA  
9428  C C   . GLU B 92   ? 0.6025 0.7568 0.3540 0.1068  0.1106  -0.0281 90   GLU B C   
9429  O O   . GLU B 92   ? 0.5569 0.7082 0.3021 0.1148  0.1125  -0.0339 90   GLU B O   
9430  C CB  . GLU B 92   ? 0.6218 0.7872 0.3642 0.0934  0.1140  -0.0143 90   GLU B CB  
9431  C CG  . GLU B 92   ? 0.6932 0.8481 0.4170 0.0991  0.1139  -0.0201 90   GLU B CG  
9432  C CD  . GLU B 92   ? 0.6496 0.7996 0.3584 0.0932  0.1123  -0.0158 90   GLU B CD  
9433  O OE1 . GLU B 92   ? 0.6728 0.8260 0.3853 0.0845  0.1107  -0.0084 90   GLU B OE1 
9434  O OE2 . GLU B 92   ? 0.6855 0.8282 0.3788 0.0972  0.1125  -0.0198 90   GLU B OE2 
9435  N N   . TYR B 93   ? 0.5799 0.7226 0.3338 0.1043  0.1037  -0.0303 91   TYR B N   
9436  C CA  . TYR B 93   ? 0.5915 0.7168 0.3401 0.1104  0.0979  -0.0396 91   TYR B CA  
9437  C C   . TYR B 93   ? 0.5622 0.6890 0.3257 0.1137  0.0971  -0.0423 91   TYR B C   
9438  O O   . TYR B 93   ? 0.5404 0.6524 0.3015 0.1178  0.0916  -0.0493 91   TYR B O   
9439  C CB  . TYR B 93   ? 0.5529 0.6616 0.2916 0.1060  0.0898  -0.0413 91   TYR B CB  
9440  C CG  . TYR B 93   ? 0.5823 0.6853 0.3033 0.1051  0.0894  -0.0411 91   TYR B CG  
9441  C CD1 . TYR B 93   ? 0.5944 0.6843 0.3021 0.1114  0.0870  -0.0486 91   TYR B CD1 
9442  C CD2 . TYR B 93   ? 0.6237 0.7343 0.3413 0.0979  0.0914  -0.0331 91   TYR B CD2 
9443  C CE1 . TYR B 93   ? 0.6146 0.6995 0.3059 0.1105  0.0865  -0.0485 91   TYR B CE1 
9444  C CE2 . TYR B 93   ? 0.6190 0.7243 0.3199 0.0970  0.0911  -0.0326 91   TYR B CE2 
9445  C CZ  . TYR B 93   ? 0.6178 0.7105 0.3057 0.1034  0.0886  -0.0404 91   TYR B CZ  
9446  O OH  . TYR B 93   ? 0.6516 0.7389 0.3226 0.1025  0.0880  -0.0401 91   TYR B OH  
9447  N N   . SER B 94   ? 0.5524 0.6966 0.3312 0.1120  0.1021  -0.0367 92   SER B N   
9448  C CA  . SER B 94   ? 0.4956 0.6430 0.2892 0.1150  0.1017  -0.0385 92   SER B CA  
9449  C C   . SER B 94   ? 0.5162 0.6498 0.3117 0.1126  0.0943  -0.0417 92   SER B C   
9450  O O   . SER B 94   ? 0.5026 0.6254 0.2991 0.1179  0.0906  -0.0481 92   SER B O   
9451  C CB  . SER B 94   ? 0.5171 0.6625 0.3094 0.1250  0.1038  -0.0447 92   SER B CB  
9452  O OG  . SER B 94   ? 0.5767 0.7370 0.3691 0.1274  0.1112  -0.0415 92   SER B OG  
9453  N N   . LEU B 95   ? 0.4876 0.6213 0.2832 0.1045  0.0918  -0.0370 93   LEU B N   
9454  C CA  . LEU B 95   ? 0.4627 0.5844 0.2597 0.1015  0.0848  -0.0394 93   LEU B CA  
9455  C C   . LEU B 95   ? 0.4577 0.5887 0.2722 0.0994  0.0855  -0.0367 93   LEU B C   
9456  O O   . LEU B 95   ? 0.4607 0.6087 0.2858 0.0959  0.0904  -0.0300 93   LEU B O   
9457  C CB  . LEU B 95   ? 0.4695 0.5869 0.2584 0.0940  0.0815  -0.0355 93   LEU B CB  
9458  C CG  . LEU B 95   ? 0.5220 0.6297 0.2930 0.0946  0.0798  -0.0372 93   LEU B CG  
9459  C CD1 . LEU B 95   ? 0.5103 0.6121 0.2773 0.0859  0.0747  -0.0328 93   LEU B CD1 
9460  C CD2 . LEU B 95   ? 0.4726 0.5627 0.2341 0.1014  0.0751  -0.0465 93   LEU B CD2 
9461  N N   . SER B 96   ? 0.4107 0.5299 0.2290 0.1010  0.0800  -0.0417 94   SER B N   
9462  C CA  . SER B 96   ? 0.4096 0.5326 0.2456 0.0958  0.0778  -0.0385 94   SER B CA  
9463  C C   . SER B 96   ? 0.4562 0.5766 0.2967 0.0846  0.0734  -0.0329 94   SER B C   
9464  O O   . SER B 96   ? 0.4477 0.5605 0.2775 0.0813  0.0708  -0.0323 94   SER B O   
9465  C CB  . SER B 96   ? 0.4472 0.5564 0.2867 0.0996  0.0724  -0.0451 94   SER B CB  
9466  O OG  . SER B 96   ? 0.4039 0.4946 0.2362 0.0965  0.0649  -0.0484 94   SER B OG  
9467  N N   . SER B 97   ? 0.3676 0.4940 0.2237 0.0788  0.0722  -0.0288 95   SER B N   
9468  C CA  . SER B 97   ? 0.4151 0.5377 0.2760 0.0686  0.0675  -0.0240 95   SER B CA  
9469  C C   . SER B 97   ? 0.4561 0.5590 0.3109 0.0670  0.0596  -0.0286 95   SER B C   
9470  O O   . SER B 97   ? 0.3891 0.4859 0.2376 0.0619  0.0564  -0.0264 95   SER B O   
9471  C CB  . SER B 97   ? 0.4147 0.5452 0.2928 0.0637  0.0670  -0.0202 95   SER B CB  
9472  O OG  . SER B 97   ? 0.4982 0.6477 0.3825 0.0649  0.0740  -0.0157 95   SER B OG  
9473  N N   . GLN B 98   ? 0.3917 0.4846 0.2485 0.0713  0.0561  -0.0346 96   GLN B N   
9474  C CA  . GLN B 98   ? 0.4011 0.4761 0.2531 0.0698  0.0486  -0.0388 96   GLN B CA  
9475  C C   . GLN B 98   ? 0.3894 0.4563 0.2243 0.0727  0.0476  -0.0417 96   GLN B C   
9476  O O   . GLN B 98   ? 0.3910 0.4469 0.2209 0.0686  0.0419  -0.0421 96   GLN B O   
9477  C CB  . GLN B 98   ? 0.3630 0.4295 0.2196 0.0743  0.0456  -0.0445 96   GLN B CB  
9478  C CG  . GLN B 98   ? 0.3975 0.4668 0.2700 0.0698  0.0438  -0.0421 96   GLN B CG  
9479  C CD  . GLN B 98   ? 0.4229 0.4869 0.2998 0.0612  0.0386  -0.0391 96   GLN B CD  
9480  O OE1 . GLN B 98   ? 0.4534 0.5250 0.3325 0.0558  0.0401  -0.0337 96   GLN B OE1 
9481  N NE2 . GLN B 98   ? 0.3909 0.4420 0.2694 0.0600  0.0324  -0.0426 96   GLN B NE2 
9482  N N   . GLU B 99   ? 0.4027 0.4750 0.2281 0.0800  0.0532  -0.0438 97   GLU B N   
9483  C CA  . GLU B 99   ? 0.4413 0.5063 0.2491 0.0827  0.0525  -0.0464 97   GLU B CA  
9484  C C   . GLU B 99   ? 0.4397 0.5100 0.2434 0.0760  0.0534  -0.0398 97   GLU B C   
9485  O O   . GLU B 99   ? 0.4451 0.5052 0.2379 0.0741  0.0491  -0.0407 97   GLU B O   
9486  C CB  . GLU B 99   ? 0.4303 0.5002 0.2283 0.0927  0.0586  -0.0504 97   GLU B CB  
9487  C CG  . GLU B 99   ? 0.4025 0.4595 0.1968 0.1000  0.0553  -0.0588 97   GLU B CG  
9488  C CD  . GLU B 99   ? 0.4588 0.5230 0.2479 0.1104  0.0622  -0.0624 97   GLU B CD  
9489  O OE1 . GLU B 99   ? 0.4698 0.5488 0.2588 0.1109  0.0691  -0.0580 97   GLU B OE1 
9490  O OE2 . GLU B 99   ? 0.4798 0.5340 0.2682 0.1163  0.0596  -0.0686 97   GLU B OE2 
9491  N N   . GLY B 100  ? 0.4098 0.4960 0.2225 0.0722  0.0586  -0.0330 98   GLY B N   
9492  C CA  . GLY B 100  ? 0.4431 0.5341 0.2525 0.0652  0.0593  -0.0261 98   GLY B CA  
9493  C C   . GLY B 100  ? 0.4269 0.5069 0.2407 0.0572  0.0514  -0.0242 98   GLY B C   
9494  O O   . GLY B 100  ? 0.4108 0.4847 0.2154 0.0536  0.0484  -0.0221 98   GLY B O   
9495  N N   . VAL B 101  ? 0.3736 0.4506 0.2011 0.0548  0.0478  -0.0252 99   VAL B N   
9496  C CA  . VAL B 101  ? 0.4135 0.4798 0.2456 0.0481  0.0404  -0.0242 99   VAL B CA  
9497  C C   . VAL B 101  ? 0.4179 0.4680 0.2391 0.0503  0.0342  -0.0297 99   VAL B C   
9498  O O   . VAL B 101  ? 0.4263 0.4689 0.2434 0.0457  0.0292  -0.0278 99   VAL B O   
9499  C CB  . VAL B 101  ? 0.3862 0.4532 0.2345 0.0460  0.0385  -0.0247 99   VAL B CB  
9500  C CG1 . VAL B 101  ? 0.3982 0.4535 0.2509 0.0405  0.0308  -0.0249 99   VAL B CG1 
9501  C CG2 . VAL B 101  ? 0.4062 0.4887 0.2651 0.0427  0.0436  -0.0187 99   VAL B CG2 
9502  N N   . ALA B 102  ? 0.3927 0.4370 0.2093 0.0573  0.0339  -0.0364 100  ALA B N   
9503  C CA  . ALA B 102  ? 0.4068 0.4354 0.2136 0.0594  0.0275  -0.0420 100  ALA B CA  
9504  C C   . ALA B 102  ? 0.4677 0.4935 0.2580 0.0597  0.0273  -0.0411 100  ALA B C   
9505  O O   . ALA B 102  ? 0.4497 0.4641 0.2341 0.0571  0.0207  -0.0420 100  ALA B O   
9506  C CB  . ALA B 102  ? 0.4030 0.4261 0.2070 0.0671  0.0277  -0.0492 100  ALA B CB  
9507  N N   . LEU B 103  ? 0.4232 0.4597 0.2059 0.0629  0.0346  -0.0390 101  LEU B N   
9508  C CA  . LEU B 103  ? 0.4508 0.4855 0.2167 0.0636  0.0351  -0.0379 101  LEU B CA  
9509  C C   . LEU B 103  ? 0.4475 0.4818 0.2144 0.0551  0.0319  -0.0310 101  LEU B C   
9510  O O   . LEU B 103  ? 0.4489 0.4736 0.2042 0.0538  0.0271  -0.0313 101  LEU B O   
9511  C CB  . LEU B 103  ? 0.4171 0.4656 0.1762 0.0688  0.0445  -0.0365 101  LEU B CB  
9512  C CG  . LEU B 103  ? 0.4603 0.5097 0.2011 0.0701  0.0469  -0.0348 101  LEU B CG  
9513  C CD1 . LEU B 103  ? 0.4839 0.5181 0.2080 0.0758  0.0423  -0.0425 101  LEU B CD1 
9514  C CD2 . LEU B 103  ? 0.4855 0.5523 0.2243 0.0742  0.0572  -0.0321 101  LEU B CD2 
9515  N N   . MET B 104  ? 0.4052 0.4492 0.1856 0.0493  0.0341  -0.0248 102  MET B N   
9516  C CA  . MET B 104  ? 0.4474 0.4901 0.2293 0.0413  0.0307  -0.0183 102  MET B CA  
9517  C C   . MET B 104  ? 0.4839 0.5118 0.2691 0.0382  0.0213  -0.0208 102  MET B C   
9518  O O   . MET B 104  ? 0.4507 0.4719 0.2297 0.0342  0.0166  -0.0180 102  MET B O   
9519  C CB  . MET B 104  ? 0.4315 0.4871 0.2274 0.0359  0.0347  -0.0116 102  MET B CB  
9520  C CG  . MET B 104  ? 0.4087 0.4807 0.2024 0.0385  0.0441  -0.0083 102  MET B CG  
9521  S SD  . MET B 104  ? 0.5607 0.6351 0.3347 0.0389  0.0473  -0.0046 102  MET B SD  
9522  C CE  . MET B 104  ? 0.5929 0.6641 0.3703 0.0281  0.0423  0.0040  102  MET B CE  
9523  N N   . CYS B 105  ? 0.4130 0.4359 0.2078 0.0401  0.0185  -0.0258 103  CYS B N   
9524  C CA  . CYS B 105  ? 0.4576 0.4673 0.2552 0.0378  0.0098  -0.0287 103  CYS B CA  
9525  C C   . CYS B 105  ? 0.4542 0.4527 0.2360 0.0409  0.0053  -0.0326 103  CYS B C   
9526  O O   . CYS B 105  ? 0.4713 0.4613 0.2503 0.0374  -0.0012 -0.0316 103  CYS B O   
9527  C CB  . CYS B 105  ? 0.3933 0.4005 0.2031 0.0397  0.0083  -0.0333 103  CYS B CB  
9528  S SG  . CYS B 105  ? 0.4345 0.4524 0.2632 0.0353  0.0115  -0.0290 103  CYS B SG  
9529  N N   . LEU B 106  ? 0.4504 0.4485 0.2220 0.0476  0.0084  -0.0375 104  LEU B N   
9530  C CA  . LEU B 106  ? 0.4646 0.4521 0.2195 0.0508  0.0043  -0.0415 104  LEU B CA  
9531  C C   . LEU B 106  ? 0.5144 0.5031 0.2578 0.0476  0.0043  -0.0360 104  LEU B C   
9532  O O   . LEU B 106  ? 0.4875 0.4657 0.2223 0.0461  -0.0025 -0.0368 104  LEU B O   
9533  C CB  . LEU B 106  ? 0.4769 0.4649 0.2217 0.0590  0.0087  -0.0473 104  LEU B CB  
9534  C CG  . LEU B 106  ? 0.5200 0.4980 0.2450 0.0623  0.0053  -0.0510 104  LEU B CG  
9535  C CD1 . LEU B 106  ? 0.4786 0.4409 0.2036 0.0612  -0.0049 -0.0558 104  LEU B CD1 
9536  C CD2 . LEU B 106  ? 0.4855 0.4658 0.1985 0.0707  0.0111  -0.0559 104  LEU B CD2 
9537  N N   . ALA B 107  ? 0.4873 0.4889 0.2304 0.0462  0.0117  -0.0301 105  ALA B N   
9538  C CA  . ALA B 107  ? 0.4957 0.4991 0.2273 0.0430  0.0123  -0.0242 105  ALA B CA  
9539  C C   . ALA B 107  ? 0.5115 0.5091 0.2493 0.0355  0.0055  -0.0194 105  ALA B C   
9540  O O   . ALA B 107  ? 0.5247 0.5153 0.2513 0.0336  0.0010  -0.0174 105  ALA B O   
9541  C CB  . ALA B 107  ? 0.4815 0.5012 0.2135 0.0426  0.0219  -0.0185 105  ALA B CB  
9542  N N   . GLU B 108  ? 0.4985 0.4989 0.2538 0.0315  0.0047  -0.0175 106  GLU B N   
9543  C CA  . GLU B 108  ? 0.5136 0.5077 0.2763 0.0253  -0.0021 -0.0139 106  GLU B CA  
9544  C C   . GLU B 108  ? 0.5732 0.5530 0.3311 0.0263  -0.0111 -0.0185 106  GLU B C   
9545  O O   . GLU B 108  ? 0.5581 0.5313 0.3116 0.0227  -0.0167 -0.0153 106  GLU B O   
9546  C CB  . GLU B 108  ? 0.5119 0.5105 0.2939 0.0224  -0.0015 -0.0132 106  GLU B CB  
9547  C CG  . GLU B 108  ? 0.5440 0.5356 0.3352 0.0170  -0.0085 -0.0109 106  GLU B CG  
9548  C CD  . GLU B 108  ? 0.5612 0.5541 0.3696 0.0163  -0.0091 -0.0132 106  GLU B CD  
9549  O OE1 . GLU B 108  ? 0.5060 0.5074 0.3205 0.0184  -0.0033 -0.0144 106  GLU B OE1 
9550  O OE2 . GLU B 108  ? 0.5779 0.5636 0.3937 0.0138  -0.0154 -0.0138 106  GLU B OE2 
9551  N N   . ALA B 109  ? 0.5314 0.5060 0.2902 0.0310  -0.0128 -0.0259 107  ALA B N   
9552  C CA  . ALA B 109  ? 0.5921 0.5538 0.3470 0.0317  -0.0216 -0.0303 107  ALA B CA  
9553  C C   . ALA B 109  ? 0.6004 0.5563 0.3355 0.0335  -0.0238 -0.0305 107  ALA B C   
9554  O O   . ALA B 109  ? 0.6187 0.5655 0.3493 0.0314  -0.0315 -0.0301 107  ALA B O   
9555  C CB  . ALA B 109  ? 0.5529 0.5104 0.3129 0.0359  -0.0229 -0.0378 107  ALA B CB  
9556  N N   . LEU B 110  ? 0.5090 0.4704 0.2318 0.0377  -0.0171 -0.0312 108  LEU B N   
9557  C CA  . LEU B 110  ? 0.5833 0.5397 0.2858 0.0398  -0.0185 -0.0315 108  LEU B CA  
9558  C C   . LEU B 110  ? 0.6102 0.5673 0.3079 0.0343  -0.0202 -0.0236 108  LEU B C   
9559  O O   . LEU B 110  ? 0.6605 0.6095 0.3443 0.0341  -0.0254 -0.0234 108  LEU B O   
9560  C CB  . LEU B 110  ? 0.5463 0.5099 0.2371 0.0458  -0.0100 -0.0337 108  LEU B CB  
9561  C CG  . LEU B 110  ? 0.5802 0.5380 0.2688 0.0525  -0.0106 -0.0429 108  LEU B CG  
9562  C CD1 . LEU B 110  ? 0.5301 0.4961 0.2089 0.0591  -0.0015 -0.0450 108  LEU B CD1 
9563  C CD2 . LEU B 110  ? 0.6235 0.5659 0.3008 0.0538  -0.0200 -0.0480 108  LEU B CD2 
9564  N N   . LEU B 111  ? 0.5697 0.5359 0.2785 0.0295  -0.0162 -0.0169 109  LEU B N   
9565  C CA  . LEU B 111  ? 0.6285 0.5950 0.3340 0.0238  -0.0180 -0.0088 109  LEU B CA  
9566  C C   . LEU B 111  ? 0.6617 0.6177 0.3741 0.0198  -0.0278 -0.0079 109  LEU B C   
9567  O O   . LEU B 111  ? 0.6595 0.6126 0.3669 0.0156  -0.0311 -0.0019 109  LEU B O   
9568  C CB  . LEU B 111  ? 0.6004 0.5798 0.3154 0.0198  -0.0106 -0.0020 109  LEU B CB  
9569  C CG  . LEU B 111  ? 0.5727 0.5639 0.2787 0.0232  -0.0008 -0.0010 109  LEU B CG  
9570  C CD1 . LEU B 111  ? 0.5827 0.5875 0.3004 0.0194  0.0062  0.0052  109  LEU B CD1 
9571  C CD2 . LEU B 111  ? 0.6824 0.6718 0.3682 0.0235  -0.0005 0.0022  109  LEU B CD2 
9572  N N   . ARG B 112  ? 0.6545 0.6049 0.3782 0.0210  -0.0326 -0.0135 110  ARG B N   
9573  C CA  . ARG B 112  ? 0.6601 0.6006 0.3890 0.0183  -0.0422 -0.0135 110  ARG B CA  
9574  C C   . ARG B 112  ? 0.7030 0.6332 0.4164 0.0203  -0.0492 -0.0162 110  ARG B C   
9575  O O   . ARG B 112  ? 0.6889 0.6110 0.4047 0.0181  -0.0576 -0.0155 110  ARG B O   
9576  C CB  . ARG B 112  ? 0.6345 0.5736 0.3809 0.0188  -0.0448 -0.0184 110  ARG B CB  
9577  C CG  . ARG B 112  ? 0.6485 0.5969 0.4108 0.0164  -0.0390 -0.0158 110  ARG B CG  
9578  C CD  . ARG B 112  ? 0.7273 0.6734 0.5069 0.0158  -0.0429 -0.0192 110  ARG B CD  
9579  N NE  . ARG B 112  ? 0.7301 0.6730 0.5105 0.0201  -0.0439 -0.0265 110  ARG B NE  
9580  C CZ  . ARG B 112  ? 0.7649 0.7133 0.5523 0.0226  -0.0387 -0.0297 110  ARG B CZ  
9581  N NH1 . ARG B 112  ? 0.7335 0.6916 0.5286 0.0212  -0.0319 -0.0265 110  ARG B NH1 
9582  N NH2 . ARG B 112  ? 0.7869 0.7306 0.5737 0.0263  -0.0407 -0.0362 110  ARG B NH2 
9583  N N   . ILE B 113  ? 0.6652 0.5952 0.3625 0.0247  -0.0461 -0.0193 111  ILE B N   
9584  C CA  . ILE B 113  ? 0.7002 0.6207 0.3798 0.0264  -0.0522 -0.0211 111  ILE B CA  
9585  C C   . ILE B 113  ? 0.7593 0.6823 0.4260 0.0236  -0.0502 -0.0134 111  ILE B C   
9586  O O   . ILE B 113  ? 0.7457 0.6776 0.4049 0.0247  -0.0415 -0.0109 111  ILE B O   
9587  C CB  . ILE B 113  ? 0.7353 0.6535 0.4026 0.0328  -0.0500 -0.0287 111  ILE B CB  
9588  C CG1 . ILE B 113  ? 0.7473 0.6604 0.4265 0.0348  -0.0541 -0.0360 111  ILE B CG1 
9589  C CG2 . ILE B 113  ? 0.7270 0.6366 0.3727 0.0345  -0.0551 -0.0297 111  ILE B CG2 
9590  C CD1 . ILE B 113  ? 0.7637 0.6802 0.4413 0.0404  -0.0477 -0.0421 111  ILE B CD1 
9591  N N   . PRO B 114  ? 0.7474 0.6633 0.4116 0.0199  -0.0579 -0.0091 112  PRO B N   
9592  C CA  . PRO B 114  ? 0.7633 0.6818 0.4180 0.0161  -0.0561 -0.0004 112  PRO B CA  
9593  C C   . PRO B 114  ? 0.7690 0.6866 0.4000 0.0188  -0.0539 0.0000  112  PRO B C   
9594  O O   . PRO B 114  ? 0.7857 0.7106 0.4087 0.0170  -0.0475 0.0064  112  PRO B O   
9595  C CB  . PRO B 114  ? 0.7230 0.6325 0.3831 0.0121  -0.0662 0.0031  112  PRO B CB  
9596  C CG  . PRO B 114  ? 0.7579 0.6640 0.4354 0.0131  -0.0711 -0.0030 112  PRO B CG  
9597  C CD  . PRO B 114  ? 0.7651 0.6716 0.4384 0.0185  -0.0683 -0.0112 112  PRO B CD  
9598  N N   . ASP B 115  ? 0.8060 0.7150 0.4256 0.0231  -0.0591 -0.0067 113  ASP B N   
9599  C CA  . ASP B 115  ? 0.8683 0.7748 0.4638 0.0259  -0.0583 -0.0070 113  ASP B CA  
9600  C C   . ASP B 115  ? 0.8573 0.7724 0.4459 0.0312  -0.0479 -0.0109 113  ASP B C   
9601  O O   . ASP B 115  ? 0.8557 0.7695 0.4492 0.0356  -0.0472 -0.0189 113  ASP B O   
9602  C CB  . ASP B 115  ? 0.8331 0.7260 0.4192 0.0282  -0.0690 -0.0128 113  ASP B CB  
9603  C CG  . ASP B 115  ? 0.9199 0.8100 0.4821 0.0323  -0.0678 -0.0155 113  ASP B CG  
9604  O OD1 . ASP B 115  ? 0.9533 0.8488 0.5042 0.0307  -0.0631 -0.0091 113  ASP B OD1 
9605  O OD2 . ASP B 115  ? 0.9568 0.8420 0.5182 0.0361  -0.0707 -0.0237 113  ASP B OD2 
9606  N N   . THR B 116  ? 0.8635 0.7875 0.4408 0.0308  -0.0398 -0.0052 114  THR B N   
9607  C CA  . THR B 116  ? 0.8823 0.8164 0.4536 0.0361  -0.0291 -0.0083 114  THR B CA  
9608  C C   . THR B 116  ? 0.9022 0.8293 0.4613 0.0428  -0.0310 -0.0180 114  THR B C   
9609  O O   . THR B 116  ? 0.8589 0.7902 0.4228 0.0478  -0.0256 -0.0243 114  THR B O   
9610  C CB  . THR B 116  ? 0.8867 0.8312 0.4461 0.0341  -0.0211 0.0001  114  THR B CB  
9611  O OG1 . THR B 116  ? 0.8987 0.8530 0.4750 0.0281  -0.0168 0.0080  114  THR B OG1 
9612  C CG2 . THR B 116  ? 0.8896 0.8440 0.4407 0.0399  -0.0109 -0.0037 114  THR B CG2 
9613  N N   . ALA B 117  ? 0.9105 0.8282 0.4596 0.0421  -0.0387 -0.0191 115  ALA B N   
9614  C CA  . ALA B 117  ? 0.8580 0.7699 0.4005 0.0469  -0.0407 -0.0279 115  ALA B CA  
9615  C C   . ALA B 117  ? 0.8574 0.7614 0.4118 0.0494  -0.0461 -0.0361 115  ALA B C   
9616  O O   . ALA B 117  ? 0.9170 0.8200 0.4708 0.0544  -0.0436 -0.0436 115  ALA B O   
9617  C CB  . ALA B 117  ? 0.9032 0.8068 0.4330 0.0450  -0.0485 -0.0268 115  ALA B CB  
9618  N N   . THR B 118  ? 0.8557 0.7534 0.4212 0.0458  -0.0539 -0.0347 116  THR B N   
9619  C CA  . THR B 118  ? 0.8462 0.7373 0.4242 0.0475  -0.0590 -0.0419 116  THR B CA  
9620  C C   . THR B 118  ? 0.8376 0.7369 0.4251 0.0506  -0.0504 -0.0443 116  THR B C   
9621  O O   . THR B 118  ? 0.8131 0.7094 0.4057 0.0545  -0.0506 -0.0518 116  THR B O   
9622  C CB  . THR B 118  ? 0.8329 0.7170 0.4214 0.0427  -0.0688 -0.0393 116  THR B CB  
9623  N N   . ARG B 119  ? 0.8305 0.7417 0.4251 0.0481  -0.0427 -0.0375 117  ARG B N   
9624  C CA  . ARG B 119  ? 0.8158 0.7375 0.4241 0.0501  -0.0340 -0.0387 117  ARG B CA  
9625  C C   . ARG B 119  ? 0.8312 0.7564 0.4255 0.0576  -0.0265 -0.0440 117  ARG B C   
9626  O O   . ARG B 119  ? 0.8100 0.7343 0.4111 0.0619  -0.0251 -0.0507 117  ARG B O   
9627  C CB  . ARG B 119  ? 0.7965 0.7309 0.4161 0.0449  -0.0277 -0.0295 117  ARG B CB  
9628  C CG  . ARG B 119  ? 0.7197 0.6657 0.3541 0.0464  -0.0191 -0.0301 117  ARG B CG  
9629  C CD  . ARG B 119  ? 0.7303 0.6897 0.3710 0.0418  -0.0118 -0.0210 117  ARG B CD  
9630  N NE  . ARG B 119  ? 0.7359 0.6920 0.3838 0.0345  -0.0178 -0.0143 117  ARG B NE  
9631  C CZ  . ARG B 119  ? 0.8086 0.7675 0.4488 0.0302  -0.0168 -0.0063 117  ARG B CZ  
9632  N NH1 . ARG B 119  ? 0.7233 0.6900 0.3490 0.0320  -0.0095 -0.0033 117  ARG B NH1 
9633  N NH2 . ARG B 119  ? 0.8137 0.7677 0.4611 0.0240  -0.0232 -0.0009 117  ARG B NH2 
9634  N N   . ASP B 120  ? 0.8264 0.7576 0.4081 0.0577  -0.0213 -0.0402 118  ASP B N   
9635  C CA  . ASP B 120  ? 0.8649 0.8026 0.4404 0.0631  -0.0131 -0.0441 118  ASP B CA  
9636  C C   . ASP B 120  ? 0.8648 0.7909 0.4366 0.0677  -0.0182 -0.0536 118  ASP B C   
9637  O O   . ASP B 120  ? 0.8441 0.7733 0.4157 0.0732  -0.0125 -0.0588 118  ASP B O   
9638  C CB  . ASP B 120  ? 0.8680 0.8128 0.4296 0.0616  -0.0079 -0.0382 118  ASP B CB  
9639  C CG  . ASP B 120  ? 0.9034 0.8623 0.4696 0.0577  -0.0003 -0.0286 118  ASP B CG  
9640  O OD1 . ASP B 120  ? 0.9051 0.8678 0.4848 0.0563  0.0005  -0.0266 118  ASP B OD1 
9641  O OD2 . ASP B 120  ? 0.9202 0.8865 0.4766 0.0559  0.0048  -0.0229 118  ASP B OD2 
9642  N N   . ALA B 121  ? 0.9017 0.8146 0.4713 0.0654  -0.0293 -0.0559 119  ALA B N   
9643  C CA  . ALA B 121  ? 0.8875 0.7887 0.4545 0.0689  -0.0351 -0.0646 119  ALA B CA  
9644  C C   . ALA B 121  ? 0.8334 0.7307 0.4155 0.0704  -0.0375 -0.0698 119  ALA B C   
9645  O O   . ALA B 121  ? 0.8806 0.7736 0.4628 0.0751  -0.0368 -0.0767 119  ALA B O   
9646  C CB  . ALA B 121  ? 0.9015 0.7911 0.4613 0.0655  -0.0461 -0.0645 119  ALA B CB  
9647  N N   . LEU B 122  ? 0.8590 0.7570 0.4535 0.0665  -0.0405 -0.0666 120  LEU B N   
9648  C CA  . LEU B 122  ? 0.8369 0.7329 0.4461 0.0677  -0.0416 -0.0709 120  LEU B CA  
9649  C C   . LEU B 122  ? 0.8347 0.7402 0.4471 0.0730  -0.0311 -0.0729 120  LEU B C   
9650  O O   . LEU B 122  ? 0.8206 0.7220 0.4388 0.0766  -0.0314 -0.0791 120  LEU B O   
9651  C CB  . LEU B 122  ? 0.7849 0.6823 0.4062 0.0628  -0.0450 -0.0663 120  LEU B CB  
9652  C CG  . LEU B 122  ? 0.8149 0.7108 0.4551 0.0626  -0.0468 -0.0701 120  LEU B CG  
9653  C CD1 . LEU B 122  ? 0.8275 0.7088 0.4658 0.0632  -0.0570 -0.0769 120  LEU B CD1 
9654  C CD2 . LEU B 122  ? 0.6877 0.5908 0.3492 0.0560  -0.0468 -0.0637 120  LEU B CD2 
9655  N N   . ILE B 123  ? 0.7964 0.7151 0.4055 0.0733  -0.0218 -0.0674 121  ILE B N   
9656  C CA  . ILE B 123  ? 0.8167 0.7466 0.4305 0.0780  -0.0115 -0.0683 121  ILE B CA  
9657  C C   . ILE B 123  ? 0.8736 0.7992 0.4794 0.0842  -0.0097 -0.0752 121  ILE B C   
9658  O O   . ILE B 123  ? 0.8701 0.7946 0.4830 0.0886  -0.0078 -0.0804 121  ILE B O   
9659  C CB  . ILE B 123  ? 0.7715 0.7168 0.3831 0.0762  -0.0024 -0.0602 121  ILE B CB  
9660  C CG1 . ILE B 123  ? 0.6782 0.6278 0.2993 0.0707  -0.0038 -0.0537 121  ILE B CG1 
9661  C CG2 . ILE B 123  ? 0.7423 0.7000 0.3575 0.0815  0.0084  -0.0613 121  ILE B CG2 
9662  C CD1 . ILE B 123  ? 0.7004 0.6644 0.3212 0.0672  0.0039  -0.0445 121  ILE B CD1 
9663  N N   . ARG B 124  ? 0.8233 0.7457 0.4139 0.0846  -0.0106 -0.0753 122  ARG B N   
9664  C CA  . ARG B 124  ? 0.8687 0.7883 0.4499 0.0907  -0.0078 -0.0813 122  ARG B CA  
9665  C C   . ARG B 124  ? 0.9255 0.8299 0.5083 0.0933  -0.0158 -0.0894 122  ARG B C   
9666  O O   . ARG B 124  ? 0.9398 0.8421 0.5209 0.0992  -0.0130 -0.0951 122  ARG B O   
9667  C CB  . ARG B 124  ? 0.8595 0.7791 0.4235 0.0900  -0.0074 -0.0791 122  ARG B CB  
9668  N N   . ASP B 125  ? 0.8989 0.7928 0.4858 0.0887  -0.0260 -0.0900 123  ASP B N   
9669  C CA  . ASP B 125  ? 0.9170 0.7959 0.5035 0.0900  -0.0346 -0.0969 123  ASP B CA  
9670  C C   . ASP B 125  ? 0.8913 0.7650 0.4938 0.0882  -0.0397 -0.0990 123  ASP B C   
9671  O O   . ASP B 125  ? 0.9451 0.8069 0.5488 0.0892  -0.0464 -0.1046 123  ASP B O   
9672  C CB  . ASP B 125  ? 0.9141 0.7834 0.4901 0.0864  -0.0436 -0.0967 123  ASP B CB  
9673  C CG  . ASP B 125  ? 0.9431 0.8158 0.5017 0.0885  -0.0393 -0.0955 123  ASP B CG  
9674  O OD1 . ASP B 125  ? 1.0229 0.9052 0.5778 0.0857  -0.0349 -0.0888 123  ASP B OD1 
9675  O OD2 . ASP B 125  ? 0.9911 0.8568 0.5396 0.0928  -0.0403 -0.1012 123  ASP B OD2 
9676  N N   . LYS B 126  ? 0.8462 0.7283 0.4608 0.0855  -0.0368 -0.0946 124  LYS B N   
9677  C CA  . LYS B 126  ? 0.8676 0.7450 0.4973 0.0837  -0.0415 -0.0967 124  LYS B CA  
9678  C C   . LYS B 126  ? 0.8760 0.7640 0.5174 0.0858  -0.0335 -0.0954 124  LYS B C   
9679  O O   . LYS B 126  ? 0.8815 0.7654 0.5328 0.0872  -0.0351 -0.0991 124  LYS B O   
9680  C CB  . LYS B 126  ? 0.9191 0.7926 0.5543 0.0769  -0.0499 -0.0932 124  LYS B CB  
9681  N N   . ILE B 127  ? 0.8132 0.7148 0.4538 0.0859  -0.0251 -0.0899 125  ILE B N   
9682  C CA  . ILE B 127  ? 0.8081 0.7211 0.4611 0.0868  -0.0181 -0.0877 125  ILE B CA  
9683  C C   . ILE B 127  ? 0.7966 0.7181 0.4482 0.0933  -0.0085 -0.0893 125  ILE B C   
9684  O O   . ILE B 127  ? 0.8241 0.7491 0.4863 0.0961  -0.0053 -0.0911 125  ILE B O   
9685  C CB  . ILE B 127  ? 0.7710 0.6941 0.4267 0.0819  -0.0156 -0.0799 125  ILE B CB  
9686  C CG1 . ILE B 127  ? 0.7627 0.6775 0.4244 0.0749  -0.0255 -0.0778 125  ILE B CG1 
9687  C CG2 . ILE B 127  ? 0.7090 0.6451 0.3825 0.0813  -0.0085 -0.0764 125  ILE B CG2 
9688  C CD1 . ILE B 127  ? 0.7281 0.6525 0.3998 0.0680  -0.0238 -0.0689 125  ILE B CD1 
9689  N N   . ALA B 128  ? 0.7478 0.6731 0.3868 0.0957  -0.0041 -0.0885 126  ALA B N   
9690  C CA  . ALA B 128  ? 0.7858 0.7182 0.4229 0.1024  0.0043  -0.0908 126  ALA B CA  
9691  C C   . ALA B 128  ? 0.8612 0.7822 0.4997 0.1075  0.0008  -0.0986 126  ALA B C   
9692  O O   . ALA B 128  ? 0.7992 0.7255 0.4395 0.1134  0.0072  -0.1008 126  ALA B O   
9693  C CB  . ALA B 128  ? 0.8037 0.7401 0.4256 0.1038  0.0084  -0.0892 126  ALA B CB  
9694  N N   . ASP B 129  ? 0.8811 0.7869 0.5192 0.1051  -0.0092 -0.1024 127  ASP B N   
9695  C CA  . ASP B 129  ? 0.9241 0.8179 0.5647 0.1087  -0.0138 -0.1091 127  ASP B CA  
9696  C C   . ASP B 129  ? 0.9297 0.8221 0.5864 0.1067  -0.0163 -0.1093 127  ASP B C   
9697  O O   . ASP B 129  ? 0.9726 0.8536 0.6328 0.1079  -0.0219 -0.1141 127  ASP B O   
9698  C CB  . ASP B 129  ? 0.9364 0.8145 0.5670 0.1071  -0.0235 -0.1131 127  ASP B CB  
9699  C CG  . ASP B 129  ? 0.9741 0.8526 0.5877 0.1096  -0.0212 -0.1136 127  ASP B CG  
9700  O OD1 . ASP B 129  ? 1.0234 0.9075 0.6318 0.1157  -0.0138 -0.1152 127  ASP B OD1 
9701  O OD2 . ASP B 129  ? 0.9982 0.8717 0.6037 0.1054  -0.0268 -0.1121 127  ASP B OD2 
9702  N N   . GLY B 130  ? 0.8792 0.7831 0.5457 0.1035  -0.0124 -0.1040 128  GLY B N   
9703  C CA  . GLY B 130  ? 0.8490 0.7538 0.5308 0.1021  -0.0133 -0.1039 128  GLY B CA  
9704  C C   . GLY B 130  ? 0.8897 0.7839 0.5776 0.0963  -0.0232 -0.1046 128  GLY B C   
9705  O O   . GLY B 130  ? 0.9079 0.8032 0.6086 0.0946  -0.0240 -0.1042 128  GLY B O   
9706  N N   . ASN B 131  ? 0.9142 0.7986 0.5939 0.0930  -0.0308 -0.1055 129  ASN B N   
9707  C CA  . ASN B 131  ? 0.9050 0.7803 0.5916 0.0871  -0.0405 -0.1058 129  ASN B CA  
9708  C C   . ASN B 131  ? 0.9003 0.7828 0.5908 0.0816  -0.0410 -0.1000 129  ASN B C   
9709  O O   . ASN B 131  ? 0.9676 0.8450 0.6547 0.0772  -0.0478 -0.0985 129  ASN B O   
9710  C CB  . ASN B 131  ? 0.8930 0.7548 0.5704 0.0862  -0.0489 -0.1093 129  ASN B CB  
9711  N N   . TRP B 132  ? 0.8441 0.7403 0.5468 0.0807  -0.0333 -0.0951 130  TRP B N   
9712  C CA  . TRP B 132  ? 0.7916 0.6980 0.5033 0.0743  -0.0316 -0.0873 130  TRP B CA  
9713  C C   . TRP B 132  ? 0.8174 0.7225 0.5475 0.0677  -0.0372 -0.0848 130  TRP B C   
9714  O O   . TRP B 132  ? 0.8013 0.7094 0.5361 0.0621  -0.0396 -0.0797 130  TRP B O   
9715  C CB  . TRP B 132  ? 0.7540 0.6763 0.4706 0.0758  -0.0209 -0.0826 130  TRP B CB  
9716  C CG  . TRP B 132  ? 0.6671 0.5952 0.3988 0.0772  -0.0167 -0.0831 130  TRP B CG  
9717  C CD1 . TRP B 132  ? 0.6957 0.6252 0.4245 0.0843  -0.0117 -0.0872 130  TRP B CD1 
9718  C CD2 . TRP B 132  ? 0.6591 0.5921 0.4105 0.0718  -0.0174 -0.0793 130  TRP B CD2 
9719  N NE1 . TRP B 132  ? 0.6534 0.5884 0.3992 0.0833  -0.0094 -0.0859 130  TRP B NE1 
9720  C CE2 . TRP B 132  ? 0.6330 0.5702 0.3924 0.0756  -0.0127 -0.0812 130  TRP B CE2 
9721  C CE3 . TRP B 132  ? 0.6564 0.5905 0.4191 0.0645  -0.0215 -0.0747 130  TRP B CE3 
9722  C CZ2 . TRP B 132  ? 0.5695 0.5120 0.3471 0.0720  -0.0121 -0.0784 130  TRP B CZ2 
9723  C CZ3 . TRP B 132  ? 0.6198 0.5591 0.4004 0.0613  -0.0206 -0.0724 130  TRP B CZ3 
9724  C CH2 . TRP B 132  ? 0.5710 0.5145 0.3587 0.0648  -0.0159 -0.0741 130  TRP B CH2 
9725  N N   . LYS B 133  ? 0.8587 0.7594 0.5990 0.0682  -0.0394 -0.0882 131  LYS B N   
9726  C CA  . LYS B 133  ? 0.8570 0.7571 0.6146 0.0621  -0.0444 -0.0859 131  LYS B CA  
9727  C C   . LYS B 133  ? 0.9048 0.7953 0.6593 0.0582  -0.0541 -0.0866 131  LYS B C   
9728  O O   . LYS B 133  ? 0.9010 0.7941 0.6675 0.0526  -0.0574 -0.0827 131  LYS B O   
9729  C CB  . LYS B 133  ? 0.8290 0.7257 0.5965 0.0637  -0.0448 -0.0894 131  LYS B CB  
9730  N N   . SER B 134  ? 0.9300 0.8094 0.6682 0.0612  -0.0589 -0.0916 132  SER B N   
9731  C CA  . SER B 134  ? 0.9229 0.7930 0.6570 0.0578  -0.0687 -0.0925 132  SER B CA  
9732  C C   . SER B 134  ? 0.9474 0.8223 0.6764 0.0549  -0.0688 -0.0871 132  SER B C   
9733  O O   . SER B 134  ? 0.9844 0.8616 0.7246 0.0495  -0.0727 -0.0830 132  SER B O   
9734  C CB  . SER B 134  ? 0.8445 0.7010 0.5613 0.0621  -0.0739 -0.0996 132  SER B CB  
9735  N N   . HIS B 135  ? 0.9356 0.8121 0.6478 0.0586  -0.0644 -0.0870 133  HIS B N   
9736  C CA  . HIS B 135  ? 0.9227 0.8021 0.6271 0.0560  -0.0651 -0.0820 133  HIS B CA  
9737  C C   . HIS B 135  ? 0.9036 0.7947 0.6223 0.0513  -0.0608 -0.0744 133  HIS B C   
9738  O O   . HIS B 135  ? 0.9513 0.8431 0.6681 0.0477  -0.0637 -0.0698 133  HIS B O   
9739  C CB  . HIS B 135  ? 0.8840 0.7641 0.5675 0.0612  -0.0598 -0.0832 133  HIS B CB  
9740  N N   . LEU B 136  ? 0.8805 0.7803 0.6132 0.0513  -0.0544 -0.0731 134  LEU B N   
9741  C CA  . LEU B 136  ? 0.8305 0.7406 0.5770 0.0468  -0.0509 -0.0663 134  LEU B CA  
9742  C C   . LEU B 136  ? 0.8697 0.7825 0.6359 0.0447  -0.0509 -0.0667 134  LEU B C   
9743  O O   . LEU B 136  ? 0.8658 0.7846 0.6453 0.0405  -0.0504 -0.0620 134  LEU B O   
9744  C CB  . LEU B 136  ? 0.7537 0.6749 0.4956 0.0484  -0.0411 -0.0624 134  LEU B CB  
9745  C CG  . LEU B 136  ? 0.7651 0.6864 0.4877 0.0503  -0.0391 -0.0609 134  LEU B CG  
9746  C CD1 . LEU B 136  ? 0.6942 0.6287 0.4160 0.0516  -0.0287 -0.0567 134  LEU B CD1 
9747  C CD2 . LEU B 136  ? 0.7897 0.7071 0.5085 0.0456  -0.0454 -0.0566 134  LEU B CD2 
9748  N N   . ARG B 140  ? 0.5915 0.5207 0.4401 0.0250  -0.0595 -0.0541 138  ARG B N   
9749  C CA  . ARG B 140  ? 0.6017 0.5399 0.4541 0.0244  -0.0521 -0.0503 138  ARG B CA  
9750  C C   . ARG B 140  ? 0.6128 0.5542 0.4570 0.0281  -0.0453 -0.0518 138  ARG B C   
9751  O O   . ARG B 140  ? 0.5632 0.5008 0.3931 0.0309  -0.0453 -0.0536 138  ARG B O   
9752  C CB  . ARG B 140  ? 0.6154 0.5551 0.4636 0.0219  -0.0525 -0.0453 138  ARG B CB  
9753  N N   . SER B 141  ? 0.5652 0.5137 0.4185 0.0284  -0.0397 -0.0512 139  SER B N   
9754  C CA  . SER B 141  ? 0.5457 0.4985 0.3932 0.0322  -0.0331 -0.0524 139  SER B CA  
9755  C C   . SER B 141  ? 0.5338 0.4907 0.3697 0.0328  -0.0292 -0.0492 139  SER B C   
9756  O O   . SER B 141  ? 0.4799 0.4403 0.3174 0.0292  -0.0290 -0.0444 139  SER B O   
9757  C CB  . SER B 141  ? 0.5151 0.4761 0.3754 0.0318  -0.0279 -0.0512 139  SER B CB  
9758  O OG  . SER B 141  ? 0.5059 0.4728 0.3613 0.0356  -0.0212 -0.0516 139  SER B OG  
9759  N N   . LEU B 142  ? 0.5119 0.4682 0.3357 0.0374  -0.0261 -0.0519 140  LEU B N   
9760  C CA  . LEU B 142  ? 0.4616 0.4242 0.2754 0.0383  -0.0208 -0.0485 140  LEU B CA  
9761  C C   . LEU B 142  ? 0.4522 0.4269 0.2758 0.0359  -0.0144 -0.0435 140  LEU B C   
9762  O O   . LEU B 142  ? 0.4330 0.4135 0.2518 0.0341  -0.0111 -0.0388 140  LEU B O   
9763  C CB  . LEU B 142  ? 0.4647 0.4260 0.2655 0.0446  -0.0174 -0.0528 140  LEU B CB  
9764  C CG  . LEU B 142  ? 0.5286 0.4909 0.3128 0.0463  -0.0152 -0.0513 140  LEU B CG  
9765  C CD1 . LEU B 142  ? 0.6113 0.5619 0.3849 0.0456  -0.0230 -0.0533 140  LEU B CD1 
9766  C CD2 . LEU B 142  ? 0.5450 0.5103 0.3202 0.0531  -0.0093 -0.0549 140  LEU B CD2 
9767  N N   . PHE B 143  ? 0.4320 0.4102 0.2689 0.0356  -0.0129 -0.0443 141  PHE B N   
9768  C CA  . PHE B 143  ? 0.4256 0.4155 0.2711 0.0343  -0.0065 -0.0404 141  PHE B CA  
9769  C C   . PHE B 143  ? 0.4180 0.4102 0.2758 0.0285  -0.0084 -0.0365 141  PHE B C   
9770  O O   . PHE B 143  ? 0.3884 0.3889 0.2556 0.0272  -0.0043 -0.0342 141  PHE B O   
9771  C CB  . PHE B 143  ? 0.4027 0.3957 0.2531 0.0386  -0.0029 -0.0439 141  PHE B CB  
9772  C CG  . PHE B 143  ? 0.3879 0.3770 0.2260 0.0449  -0.0016 -0.0486 141  PHE B CG  
9773  C CD1 . PHE B 143  ? 0.3780 0.3720 0.2044 0.0475  0.0029  -0.0473 141  PHE B CD1 
9774  C CD2 . PHE B 143  ? 0.3400 0.3201 0.1777 0.0481  -0.0053 -0.0543 141  PHE B CD2 
9775  C CE1 . PHE B 143  ? 0.4126 0.4024 0.2266 0.0538  0.0040  -0.0521 141  PHE B CE1 
9776  C CE2 . PHE B 143  ? 0.3628 0.3378 0.1884 0.0541  -0.0047 -0.0590 141  PHE B CE2 
9777  C CZ  . PHE B 143  ? 0.4228 0.4026 0.2363 0.0572  0.0000  -0.0582 141  PHE B CZ  
9778  N N   . VAL B 144  ? 0.4338 0.4190 0.2915 0.0253  -0.0145 -0.0356 142  VAL B N   
9779  C CA  . VAL B 144  ? 0.4405 0.4265 0.3092 0.0205  -0.0168 -0.0324 142  VAL B CA  
9780  C C   . VAL B 144  ? 0.4575 0.4526 0.3287 0.0174  -0.0120 -0.0268 142  VAL B C   
9781  O O   . VAL B 144  ? 0.4477 0.4467 0.3300 0.0145  -0.0113 -0.0250 142  VAL B O   
9782  C CB  . VAL B 144  ? 0.4485 0.4258 0.3144 0.0183  -0.0239 -0.0320 142  VAL B CB  
9783  C CG1 . VAL B 144  ? 0.5038 0.4820 0.3790 0.0137  -0.0259 -0.0282 142  VAL B CG1 
9784  C CG2 . VAL B 144  ? 0.4990 0.4685 0.3667 0.0202  -0.0292 -0.0372 142  VAL B CG2 
9785  N N   . ASN B 145  ? 0.4647 0.4635 0.3257 0.0176  -0.0087 -0.0239 143  ASN B N   
9786  C CA  . ASN B 145  ? 0.4508 0.4586 0.3139 0.0141  -0.0043 -0.0181 143  ASN B CA  
9787  C C   . ASN B 145  ? 0.4479 0.4666 0.3113 0.0169  0.0031  -0.0178 143  ASN B C   
9788  O O   . ASN B 145  ? 0.4538 0.4809 0.3156 0.0147  0.0074  -0.0128 143  ASN B O   
9789  C CB  . ASN B 145  ? 0.4789 0.4846 0.3312 0.0115  -0.0055 -0.0136 143  ASN B CB  
9790  C CG  . ASN B 145  ? 0.5284 0.5260 0.3835 0.0075  -0.0122 -0.0117 143  ASN B CG  
9791  O OD1 . ASN B 145  ? 0.5568 0.5549 0.4228 0.0043  -0.0136 -0.0103 143  ASN B OD1 
9792  N ND2 . ASN B 145  ? 0.5318 0.5216 0.3766 0.0078  -0.0166 -0.0117 143  ASN B ND2 
9793  N N   . ALA B 146  ? 0.4418 0.4609 0.3080 0.0215  0.0047  -0.0227 144  ALA B N   
9794  C CA  . ALA B 146  ? 0.4295 0.4587 0.2952 0.0252  0.0115  -0.0229 144  ALA B CA  
9795  C C   . ALA B 146  ? 0.4171 0.4575 0.2936 0.0217  0.0155  -0.0183 144  ALA B C   
9796  O O   . ALA B 146  ? 0.4483 0.4994 0.3239 0.0232  0.0215  -0.0161 144  ALA B O   
9797  C CB  . ALA B 146  ? 0.4287 0.4545 0.2957 0.0309  0.0115  -0.0291 144  ALA B CB  
9798  N N   . ALA B 147  ? 0.4412 0.4796 0.3279 0.0172  0.0122  -0.0169 145  ALA B N   
9799  C CA  . ALA B 147  ? 0.4444 0.4926 0.3409 0.0136  0.0153  -0.0128 145  ALA B CA  
9800  C C   . ALA B 147  ? 0.4682 0.5230 0.3608 0.0094  0.0178  -0.0064 145  ALA B C   
9801  O O   . ALA B 147  ? 0.4190 0.4856 0.3155 0.0084  0.0227  -0.0029 145  ALA B O   
9802  C CB  . ALA B 147  ? 0.4339 0.4773 0.3406 0.0098  0.0109  -0.0131 145  ALA B CB  
9803  N N   . THR B 148  ? 0.4759 0.5234 0.3610 0.0067  0.0141  -0.0044 146  THR B N   
9804  C CA  . THR B 148  ? 0.4506 0.5033 0.3307 0.0024  0.0161  0.0022  146  THR B CA  
9805  C C   . THR B 148  ? 0.4686 0.5310 0.3409 0.0061  0.0227  0.0032  146  THR B C   
9806  O O   . THR B 148  ? 0.4715 0.5458 0.3466 0.0037  0.0276  0.0081  146  THR B O   
9807  C CB  . THR B 148  ? 0.5243 0.5660 0.3970 -0.0004 0.0104  0.0037  146  THR B CB  
9808  O OG1 . THR B 148  ? 0.4922 0.5259 0.3731 -0.0034 0.0047  0.0027  146  THR B OG1 
9809  C CG2 . THR B 148  ? 0.5212 0.5674 0.3881 -0.0053 0.0122  0.0111  146  THR B CG2 
9810  N N   . TRP B 149  ? 0.4103 0.4680 0.2728 0.0120  0.0229  -0.0016 147  TRP B N   
9811  C CA  . TRP B 149  ? 0.4431 0.5096 0.2974 0.0167  0.0294  -0.0016 147  TRP B CA  
9812  C C   . TRP B 149  ? 0.4161 0.4946 0.2796 0.0198  0.0350  -0.0024 147  TRP B C   
9813  O O   . TRP B 149  ? 0.4252 0.5158 0.2861 0.0216  0.0415  0.0002  147  TRP B O   
9814  C CB  . TRP B 149  ? 0.4256 0.4829 0.2676 0.0229  0.0276  -0.0076 147  TRP B CB  
9815  C CG  . TRP B 149  ? 0.4529 0.5003 0.2841 0.0205  0.0228  -0.0063 147  TRP B CG  
9816  C CD1 . TRP B 149  ? 0.4473 0.4809 0.2756 0.0208  0.0156  -0.0101 147  TRP B CD1 
9817  C CD2 . TRP B 149  ? 0.4288 0.4797 0.2507 0.0172  0.0245  -0.0002 147  TRP B CD2 
9818  N NE1 . TRP B 149  ? 0.4320 0.4600 0.2496 0.0182  0.0125  -0.0071 147  TRP B NE1 
9819  C CE2 . TRP B 149  ? 0.4600 0.4980 0.2732 0.0159  0.0179  -0.0009 147  TRP B CE2 
9820  C CE3 . TRP B 149  ? 0.4915 0.5554 0.3119 0.0150  0.0309  0.0060  147  TRP B CE3 
9821  C CZ2 . TRP B 149  ? 0.4938 0.5309 0.2961 0.0127  0.0174  0.0044  147  TRP B CZ2 
9822  C CZ3 . TRP B 149  ? 0.5120 0.5753 0.3217 0.0115  0.0308  0.0115  147  TRP B CZ3 
9823  C CH2 . TRP B 149  ? 0.4922 0.5418 0.2926 0.0104  0.0240  0.0106  147  TRP B CH2 
9824  N N   . GLY B 150  ? 0.4216 0.4974 0.2955 0.0206  0.0328  -0.0059 148  GLY B N   
9825  C CA  . GLY B 150  ? 0.4178 0.5049 0.3011 0.0228  0.0375  -0.0060 148  GLY B CA  
9826  C C   . GLY B 150  ? 0.4802 0.5800 0.3711 0.0171  0.0407  0.0011  148  GLY B C   
9827  O O   . GLY B 150  ? 0.4494 0.5626 0.3439 0.0191  0.0466  0.0029  148  GLY B O   
9828  N N   . LEU B 151  ? 0.4645 0.5601 0.3580 0.0098  0.0367  0.0052  149  LEU B N   
9829  C CA  . LEU B 151  ? 0.4956 0.6016 0.3945 0.0034  0.0389  0.0125  149  LEU B CA  
9830  C C   . LEU B 151  ? 0.5249 0.6401 0.4151 0.0035  0.0442  0.0170  149  LEU B C   
9831  O O   . LEU B 151  ? 0.5108 0.6406 0.4060 0.0018  0.0494  0.0217  149  LEU B O   
9832  C CB  . LEU B 151  ? 0.5282 0.6251 0.4299 -0.0039 0.0328  0.0153  149  LEU B CB  
9833  C CG  . LEU B 151  ? 0.5764 0.6752 0.4911 -0.0086 0.0306  0.0167  149  LEU B CG  
9834  C CD1 . LEU B 151  ? 0.5821 0.6701 0.4970 -0.0148 0.0244  0.0190  149  LEU B CD1 
9835  C CD2 . LEU B 151  ? 0.5397 0.6546 0.4609 -0.0114 0.0357  0.0221  149  LEU B CD2 
9836  N N   . VAL B 152  ? 0.4861 0.5934 0.3632 0.0053  0.0430  0.0159  150  VAL B N   
9837  C CA  . VAL B 152  ? 0.5273 0.6431 0.3945 0.0057  0.0482  0.0202  150  VAL B CA  
9838  C C   . VAL B 152  ? 0.5059 0.6345 0.3728 0.0129  0.0557  0.0180  150  VAL B C   
9839  O O   . VAL B 152  ? 0.5225 0.6660 0.3900 0.0119  0.0619  0.0232  150  VAL B O   
9840  C CB  . VAL B 152  ? 0.4755 0.5790 0.3277 0.0069  0.0449  0.0186  150  VAL B CB  
9841  C CG1 . VAL B 152  ? 0.5156 0.6281 0.3563 0.0077  0.0507  0.0229  150  VAL B CG1 
9842  C CG2 . VAL B 152  ? 0.5194 0.6110 0.3726 0.0000  0.0375  0.0213  150  VAL B CG2 
9843  N N   . VAL B 153  ? 0.4910 0.6143 0.3574 0.0202  0.0552  0.0104  151  VAL B N   
9844  C CA  . VAL B 153  ? 0.5050 0.6375 0.3684 0.0285  0.0616  0.0072  151  VAL B CA  
9845  C C   . VAL B 153  ? 0.4769 0.6233 0.3546 0.0292  0.0656  0.0085  151  VAL B C   
9846  O O   . VAL B 153  ? 0.4320 0.5936 0.3104 0.0320  0.0725  0.0111  151  VAL B O   
9847  C CB  . VAL B 153  ? 0.4731 0.5921 0.3285 0.0360  0.0587  -0.0016 151  VAL B CB  
9848  C CG1 . VAL B 153  ? 0.4354 0.5623 0.2896 0.0452  0.0646  -0.0058 151  VAL B CG1 
9849  C CG2 . VAL B 153  ? 0.4651 0.5730 0.3050 0.0361  0.0557  -0.0026 151  VAL B CG2 
9850  N N   . THR B 154  ? 0.4958 0.6377 0.3849 0.0267  0.0613  0.0071  152  THR B N   
9851  C CA  . THR B 154  ? 0.5127 0.6660 0.4150 0.0279  0.0641  0.0076  152  THR B CA  
9852  C C   . THR B 154  ? 0.4994 0.6601 0.4134 0.0192  0.0630  0.0141  152  THR B C   
9853  O O   . THR B 154  ? 0.4898 0.6633 0.4142 0.0194  0.0661  0.0161  152  THR B O   
9854  C CB  . THR B 154  ? 0.4704 0.6140 0.3773 0.0322  0.0603  0.0008  152  THR B CB  
9855  O OG1 . THR B 154  ? 0.4823 0.6158 0.3949 0.0259  0.0538  0.0011  152  THR B OG1 
9856  C CG2 . THR B 154  ? 0.5038 0.6358 0.3990 0.0397  0.0593  -0.0062 152  THR B CG2 
9857  N N   . GLY B 155  ? 0.4826 0.6351 0.3953 0.0117  0.0582  0.0173  153  GLY B N   
9858  C CA  . GLY B 155  ? 0.4481 0.6049 0.3713 0.0034  0.0560  0.0227  153  GLY B CA  
9859  C C   . GLY B 155  ? 0.4727 0.6212 0.4049 0.0018  0.0506  0.0195  153  GLY B C   
9860  O O   . GLY B 155  ? 0.5270 0.6777 0.4675 -0.0051 0.0482  0.0234  153  GLY B O   
9861  N N   . LYS B 156  ? 0.4692 0.6085 0.4001 0.0077  0.0486  0.0126  154  LYS B N   
9862  C CA  . LYS B 156  ? 0.5373 0.6688 0.4760 0.0065  0.0438  0.0094  154  LYS B CA  
9863  C C   . LYS B 156  ? 0.5109 0.6253 0.4437 0.0061  0.0379  0.0056  154  LYS B C   
9864  O O   . LYS B 156  ? 0.4740 0.5820 0.3964 0.0093  0.0377  0.0034  154  LYS B O   
9865  C CB  . LYS B 156  ? 0.5096 0.6450 0.4534 0.0132  0.0459  0.0050  154  LYS B CB  
9866  N N   . LEU B 157  ? 0.5025 0.6100 0.4419 0.0024  0.0331  0.0048  155  LEU B N   
9867  C CA  . LEU B 157  ? 0.5829 0.6754 0.5192 0.0020  0.0274  0.0012  155  LEU B CA  
9868  C C   . LEU B 157  ? 0.6088 0.6969 0.5509 0.0055  0.0257  -0.0041 155  LEU B C   
9869  O O   . LEU B 157  ? 0.6064 0.7017 0.5566 0.0057  0.0274  -0.0038 155  LEU B O   
9870  C CB  . LEU B 157  ? 0.5709 0.6582 0.5097 -0.0053 0.0230  0.0047  155  LEU B CB  
9871  N N   . THR B 158  ? 0.6509 0.7272 0.5890 0.0080  0.0220  -0.0086 156  THR B N   
9872  C CA  . THR B 158  ? 0.6191 0.6912 0.5616 0.0117  0.0207  -0.0135 156  THR B CA  
9873  C C   . THR B 158  ? 0.6014 0.6625 0.5465 0.0097  0.0152  -0.0160 156  THR B C   
9874  O O   . THR B 158  ? 0.6658 0.7251 0.6165 0.0114  0.0143  -0.0189 156  THR B O   
9875  C CB  . THR B 158  ? 0.6126 0.6823 0.5483 0.0184  0.0224  -0.0176 156  THR B CB  
9876  O OG1 . THR B 158  ? 0.5873 0.6481 0.5135 0.0188  0.0197  -0.0189 156  THR B OG1 
9877  C CG2 . THR B 158  ? 0.5796 0.6610 0.5136 0.0218  0.0284  -0.0159 156  THR B CG2 
9878  N N   . SER B 159  ? 0.5702 0.6242 0.5114 0.0066  0.0116  -0.0150 157  SER B N   
9879  C CA  . SER B 159  ? 0.5711 0.6152 0.5147 0.0052  0.0064  -0.0173 157  SER B CA  
9880  C C   . SER B 159  ? 0.5560 0.5922 0.4956 0.0093  0.0042  -0.0219 157  SER B C   
9881  O O   . SER B 159  ? 0.6016 0.6297 0.5386 0.0084  -0.0001 -0.0229 157  SER B O   
9882  C CB  . SER B 159  ? 0.5853 0.6309 0.5388 0.0033  0.0056  -0.0178 157  SER B CB  
9883  N N   . THR B 160  ? 0.4652 0.5032 0.4046 0.0138  0.0065  -0.0249 158  THR B N   
9884  C CA  . THR B 160  ? 0.4879 0.5178 0.4221 0.0176  0.0041  -0.0291 158  THR B CA  
9885  C C   . THR B 160  ? 0.4447 0.4774 0.3714 0.0224  0.0077  -0.0304 158  THR B C   
9886  O O   . THR B 160  ? 0.4301 0.4721 0.3574 0.0235  0.0125  -0.0283 158  THR B O   
9887  C CB  . THR B 160  ? 0.4402 0.4660 0.3814 0.0186  0.0019  -0.0325 158  THR B CB  
9888  O OG1 . THR B 160  ? 0.4471 0.4793 0.3935 0.0206  0.0054  -0.0327 158  THR B OG1 
9889  C CG2 . THR B 160  ? 0.4648 0.4878 0.4128 0.0146  -0.0016 -0.0317 158  THR B CG2 
9890  N N   . VAL B 161  ? 0.3670 0.3916 0.2867 0.0255  0.0052  -0.0341 159  VAL B N   
9891  C CA  . VAL B 161  ? 0.4277 0.4523 0.3368 0.0300  0.0076  -0.0357 159  VAL B CA  
9892  C C   . VAL B 161  ? 0.3741 0.3939 0.2828 0.0350  0.0071  -0.0406 159  VAL B C   
9893  O O   . VAL B 161  ? 0.3599 0.3715 0.2714 0.0344  0.0026  -0.0432 159  VAL B O   
9894  C CB  . VAL B 161  ? 0.4322 0.4499 0.3313 0.0290  0.0043  -0.0356 159  VAL B CB  
9895  C CG1 . VAL B 161  ? 0.4257 0.4395 0.3133 0.0343  0.0050  -0.0391 159  VAL B CG1 
9896  C CG2 . VAL B 161  ? 0.4802 0.5039 0.3780 0.0249  0.0061  -0.0302 159  VAL B CG2 
9897  N N   . ASN B 162  ? 0.3337 0.3586 0.2392 0.0399  0.0116  -0.0416 160  ASN B N   
9898  C CA  . ASN B 162  ? 0.3571 0.3758 0.2601 0.0452  0.0108  -0.0464 160  ASN B CA  
9899  C C   . ASN B 162  ? 0.3253 0.3355 0.2151 0.0481  0.0086  -0.0497 160  ASN B C   
9900  O O   . ASN B 162  ? 0.3464 0.3595 0.2272 0.0524  0.0122  -0.0504 160  ASN B O   
9901  C CB  . ASN B 162  ? 0.3450 0.3720 0.2504 0.0498  0.0162  -0.0465 160  ASN B CB  
9902  C CG  . ASN B 162  ? 0.3913 0.4107 0.2955 0.0551  0.0147  -0.0513 160  ASN B CG  
9903  O OD1 . ASN B 162  ? 0.3728 0.3809 0.2709 0.0562  0.0104  -0.0551 160  ASN B OD1 
9904  N ND2 . ASN B 162  ? 0.3651 0.3907 0.2752 0.0582  0.0180  -0.0511 160  ASN B ND2 
9905  N N   . ASP B 163  ? 0.3431 0.3428 0.2317 0.0458  0.0025  -0.0517 161  ASP B N   
9906  C CA  . ASP B 163  ? 0.3254 0.3163 0.2014 0.0478  -0.0007 -0.0547 161  ASP B CA  
9907  C C   . ASP B 163  ? 0.3793 0.3633 0.2483 0.0540  -0.0011 -0.0601 161  ASP B C   
9908  O O   . ASP B 163  ? 0.3839 0.3626 0.2401 0.0572  -0.0019 -0.0628 161  ASP B O   
9909  C CB  . ASP B 163  ? 0.3857 0.3684 0.2635 0.0433  -0.0076 -0.0549 161  ASP B CB  
9910  C CG  . ASP B 163  ? 0.3389 0.3176 0.2278 0.0414  -0.0111 -0.0563 161  ASP B CG  
9911  O OD1 . ASP B 163  ? 0.3277 0.3129 0.2267 0.0404  -0.0082 -0.0544 161  ASP B OD1 
9912  O OD2 . ASP B 163  ? 0.4336 0.4029 0.3210 0.0407  -0.0169 -0.0590 161  ASP B OD2 
9913  N N   . ARG B 164  ? 0.3260 0.3094 0.2023 0.0560  -0.0007 -0.0618 162  ARG B N   
9914  C CA  . ARG B 164  ? 0.3494 0.3260 0.2184 0.0625  -0.0007 -0.0669 162  ARG B CA  
9915  C C   . ARG B 164  ? 0.3494 0.3344 0.2120 0.0682  0.0061  -0.0669 162  ARG B C   
9916  O O   . ARG B 164  ? 0.3508 0.3303 0.2013 0.0738  0.0063  -0.0709 162  ARG B O   
9917  C CB  . ARG B 164  ? 0.3608 0.3338 0.2392 0.0629  -0.0024 -0.0683 162  ARG B CB  
9918  C CG  . ARG B 164  ? 0.3923 0.3563 0.2763 0.0580  -0.0093 -0.0691 162  ARG B CG  
9919  C CD  . ARG B 164  ? 0.4159 0.3696 0.2897 0.0574  -0.0148 -0.0719 162  ARG B CD  
9920  N NE  . ARG B 164  ? 0.5122 0.4580 0.3731 0.0635  -0.0154 -0.0769 162  ARG B NE  
9921  C CZ  . ARG B 164  ? 0.5278 0.4664 0.3762 0.0646  -0.0185 -0.0795 162  ARG B CZ  
9922  N NH1 . ARG B 164  ? 0.5299 0.4686 0.3772 0.0600  -0.0214 -0.0773 162  ARG B NH1 
9923  N NH2 . ARG B 164  ? 0.5113 0.4420 0.3476 0.0707  -0.0189 -0.0846 162  ARG B NH2 
9924  N N   . SER B 165  ? 0.3387 0.3370 0.2090 0.0670  0.0115  -0.0623 163  SER B N   
9925  C CA  . SER B 165  ? 0.3305 0.3391 0.1961 0.0719  0.0184  -0.0614 163  SER B CA  
9926  C C   . SER B 165  ? 0.3138 0.3232 0.1669 0.0720  0.0196  -0.0608 163  SER B C   
9927  O O   . SER B 165  ? 0.3264 0.3369 0.1690 0.0782  0.0230  -0.0633 163  SER B O   
9928  C CB  . SER B 165  ? 0.3082 0.3314 0.1857 0.0692  0.0231  -0.0561 163  SER B CB  
9929  O OG  . SER B 165  ? 0.3644 0.3994 0.2382 0.0729  0.0298  -0.0542 163  SER B OG  
9930  N N   . LEU B 166  ? 0.3392 0.3475 0.1929 0.0656  0.0166  -0.0576 164  LEU B N   
9931  C CA  . LEU B 166  ? 0.3451 0.3536 0.1868 0.0651  0.0172  -0.0564 164  LEU B CA  
9932  C C   . LEU B 166  ? 0.3782 0.3736 0.2058 0.0693  0.0132  -0.0622 164  LEU B C   
9933  O O   . LEU B 166  ? 0.3967 0.3932 0.2113 0.0732  0.0160  -0.0633 164  LEU B O   
9934  C CB  . LEU B 166  ? 0.3316 0.3408 0.1779 0.0572  0.0141  -0.0516 164  LEU B CB  
9935  C CG  . LEU B 166  ? 0.3813 0.4040 0.2384 0.0534  0.0188  -0.0456 164  LEU B CG  
9936  C CD1 . LEU B 166  ? 0.3604 0.3816 0.2233 0.0460  0.0149  -0.0417 164  LEU B CD1 
9937  C CD2 . LEU B 166  ? 0.3632 0.3975 0.2142 0.0555  0.0256  -0.0425 164  LEU B CD2 
9938  N N   . ALA B 167  ? 0.3784 0.3615 0.2082 0.0684  0.0065  -0.0660 165  ALA B N   
9939  C CA  . ALA B 167  ? 0.4214 0.3912 0.2382 0.0720  0.0018  -0.0717 165  ALA B CA  
9940  C C   . ALA B 167  ? 0.3737 0.3426 0.1819 0.0806  0.0057  -0.0764 165  ALA B C   
9941  O O   . ALA B 167  ? 0.3797 0.3440 0.1726 0.0849  0.0058  -0.0797 165  ALA B O   
9942  C CB  . ALA B 167  ? 0.3703 0.3283 0.1934 0.0689  -0.0060 -0.0743 165  ALA B CB  
9943  N N   . ALA B 168  ? 0.3731 0.3465 0.1903 0.0835  0.0089  -0.0768 166  ALA B N   
9944  C CA  . ALA B 168  ? 0.3673 0.3417 0.1777 0.0922  0.0133  -0.0808 166  ALA B CA  
9945  C C   . ALA B 168  ? 0.3744 0.3606 0.1763 0.0957  0.0207  -0.0787 166  ALA B C   
9946  O O   . ALA B 168  ? 0.3906 0.3737 0.1791 0.1028  0.0227  -0.0832 166  ALA B O   
9947  C CB  . ALA B 168  ? 0.3565 0.3361 0.1801 0.0939  0.0158  -0.0801 166  ALA B CB  
9948  N N   . ALA B 169  ? 0.3885 0.3886 0.1981 0.0907  0.0248  -0.0720 167  ALA B N   
9949  C CA  . ALA B 169  ? 0.3691 0.3821 0.1722 0.0934  0.0323  -0.0692 167  ALA B CA  
9950  C C   . ALA B 169  ? 0.3839 0.3912 0.1706 0.0934  0.0308  -0.0701 167  ALA B C   
9951  O O   . ALA B 169  ? 0.3998 0.4118 0.1748 0.0991  0.0359  -0.0714 167  ALA B O   
9952  C CB  . ALA B 169  ? 0.3783 0.4066 0.1940 0.0871  0.0363  -0.0614 167  ALA B CB  
9953  N N   . LEU B 170  ? 0.3907 0.3885 0.1762 0.0872  0.0238  -0.0695 168  LEU B N   
9954  C CA  . LEU B 170  ? 0.3970 0.3889 0.1666 0.0871  0.0217  -0.0703 168  LEU B CA  
9955  C C   . LEU B 170  ? 0.4155 0.3952 0.1701 0.0947  0.0195  -0.0782 168  LEU B C   
9956  O O   . LEU B 170  ? 0.4398 0.4200 0.1789 0.0990  0.0223  -0.0797 168  LEU B O   
9957  C CB  . LEU B 170  ? 0.3912 0.3754 0.1639 0.0791  0.0142  -0.0678 168  LEU B CB  
9958  C CG  . LEU B 170  ? 0.4715 0.4496 0.2284 0.0781  0.0112  -0.0678 168  LEU B CG  
9959  C CD1 . LEU B 170  ? 0.4122 0.4032 0.1621 0.0785  0.0187  -0.0628 168  LEU B CD1 
9960  C CD2 . LEU B 170  ? 0.5067 0.4784 0.2693 0.0704  0.0038  -0.0651 168  LEU B CD2 
9961  N N   . THR B 171  ? 0.4389 0.4070 0.1973 0.0963  0.0142  -0.0833 169  THR B N   
9962  C CA  . THR B 171  ? 0.4435 0.3992 0.1881 0.1039  0.0119  -0.0912 169  THR B CA  
9963  C C   . THR B 171  ? 0.4746 0.4391 0.2138 0.1123  0.0203  -0.0928 169  THR B C   
9964  O O   . THR B 171  ? 0.4826 0.4435 0.2107 0.1158  0.0211  -0.0952 169  THR B O   
9965  C CB  . THR B 171  ? 0.4603 0.4035 0.2125 0.1038  0.0054  -0.0955 169  THR B CB  
9966  O OG1 . THR B 171  ? 0.5442 0.4798 0.3017 0.0959  -0.0024 -0.0939 169  THR B OG1 
9967  C CG2 . THR B 171  ? 0.4829 0.4127 0.2224 0.1111  0.0027  -0.1033 169  THR B CG2 
9968  N N   . ARG B 172  ? 0.4454 0.4229 0.1968 0.1138  0.0264  -0.0899 170  ARG B N   
9969  C CA  . ARG B 172  ? 0.4596 0.4469 0.2116 0.1202  0.0339  -0.0899 170  ARG B CA  
9970  C C   . ARG B 172  ? 0.4554 0.4530 0.1987 0.1202  0.0397  -0.0863 170  ARG B C   
9971  O O   . ARG B 172  ? 0.5024 0.4997 0.2379 0.1255  0.0425  -0.0887 170  ARG B O   
9972  C CB  . ARG B 172  ? 0.4333 0.4337 0.2007 0.1211  0.0390  -0.0868 170  ARG B CB  
9973  C CG  . ARG B 172  ? 0.4270 0.4343 0.1970 0.1285  0.0448  -0.0880 170  ARG B CG  
9974  C CD  . ARG B 172  ? 0.4235 0.4454 0.2095 0.1288  0.0498  -0.0840 170  ARG B CD  
9975  N NE  . ARG B 172  ? 0.4004 0.4163 0.1956 0.1258  0.0449  -0.0847 170  ARG B NE  
9976  C CZ  . ARG B 172  ? 0.3820 0.4040 0.1885 0.1172  0.0438  -0.0789 170  ARG B CZ  
9977  N NH1 . ARG B 172  ? 0.3909 0.4243 0.1979 0.1120  0.0472  -0.0730 170  ARG B NH1 
9978  N NH2 . ARG B 172  ? 0.3689 0.3849 0.1872 0.1131  0.0389  -0.0785 170  ARG B NH2 
9979  N N   . LEU B 173  ? 0.4604 0.4670 0.2045 0.1141  0.0413  -0.0804 171  LEU B N   
9980  C CA  . LEU B 173  ? 0.4843 0.5026 0.2216 0.1135  0.0475  -0.0757 171  LEU B CA  
9981  C C   . LEU B 173  ? 0.4658 0.4726 0.1862 0.1140  0.0438  -0.0787 171  LEU B C   
9982  O O   . LEU B 173  ? 0.5051 0.5175 0.2177 0.1171  0.0488  -0.0782 171  LEU B O   
9983  C CB  . LEU B 173  ? 0.4607 0.4916 0.2038 0.1066  0.0500  -0.0679 171  LEU B CB  
9984  C CG  . LEU B 173  ? 0.4389 0.4625 0.1816 0.0976  0.0433  -0.0645 171  LEU B CG  
9985  C CD1 . LEU B 173  ? 0.4619 0.4836 0.1870 0.0968  0.0433  -0.0631 171  LEU B CD1 
9986  C CD2 . LEU B 173  ? 0.4190 0.4545 0.1788 0.0899  0.0451  -0.0566 171  LEU B CD2 
9987  N N   . ILE B 174  ? 0.4645 0.4556 0.1795 0.1111  0.0349  -0.0819 172  ILE B N   
9988  C CA  . ILE B 174  ? 0.4895 0.4690 0.1888 0.1114  0.0305  -0.0849 172  ILE B CA  
9989  C C   . ILE B 174  ? 0.4984 0.4701 0.1920 0.1187  0.0305  -0.0915 172  ILE B C   
9990  O O   . ILE B 174  ? 0.5154 0.4868 0.1969 0.1215  0.0327  -0.0926 172  ILE B O   
9991  C CB  . ILE B 174  ? 0.5159 0.4808 0.2125 0.1061  0.0204  -0.0864 172  ILE B CB  
9992  C CG1 . ILE B 174  ? 0.4976 0.4699 0.1978 0.0992  0.0202  -0.0797 172  ILE B CG1 
9993  C CG2 . ILE B 174  ? 0.5667 0.5188 0.2480 0.1068  0.0150  -0.0902 172  ILE B CG2 
9994  C CD1 . ILE B 174  ? 0.5708 0.5305 0.2745 0.0927  0.0102  -0.0798 172  ILE B CD1 
9995  N N   . SER B 175  ? 0.4941 0.4590 0.1956 0.1219  0.0280  -0.0959 173  SER B N   
9996  C CA  . SER B 175  ? 0.5169 0.4733 0.2127 0.1289  0.0274  -0.1021 173  SER B CA  
9997  C C   . SER B 175  ? 0.5162 0.4865 0.2122 0.1349  0.0369  -0.1009 173  SER B C   
9998  O O   . SER B 175  ? 0.5742 0.5390 0.2615 0.1410  0.0375  -0.1056 173  SER B O   
9999  C CB  . SER B 175  ? 0.5664 0.5122 0.2710 0.1306  0.0222  -0.1064 173  SER B CB  
10000 O OG  . SER B 175  ? 0.6039 0.5360 0.3086 0.1252  0.0130  -0.1080 173  SER B OG  
10001 N N   . ARG B 176  ? 0.5029 0.4909 0.2086 0.1334  0.0442  -0.0949 174  ARG B N   
10002 C CA  . ARG B 176  ? 0.5332 0.5362 0.2406 0.1385  0.0533  -0.0930 174  ARG B CA  
10003 C C   . ARG B 176  ? 0.5195 0.5303 0.2157 0.1371  0.0579  -0.0895 174  ARG B C   
10004 O O   . ARG B 176  ? 0.5429 0.5576 0.2323 0.1428  0.0626  -0.0913 174  ARG B O   
10005 C CB  . ARG B 176  ? 0.4886 0.5078 0.2130 0.1372  0.0588  -0.0877 174  ARG B CB  
10006 C CG  . ARG B 176  ? 0.5162 0.5508 0.2458 0.1430  0.0675  -0.0861 174  ARG B CG  
10007 C CD  . ARG B 176  ? 0.4837 0.5324 0.2317 0.1416  0.0712  -0.0814 174  ARG B CD  
10008 N NE  . ARG B 176  ? 0.4785 0.5409 0.2318 0.1342  0.0745  -0.0736 174  ARG B NE  
10009 C CZ  . ARG B 176  ? 0.5168 0.5796 0.2781 0.1279  0.0714  -0.0705 174  ARG B CZ  
10010 N NH1 . ARG B 176  ? 0.4656 0.5172 0.2322 0.1279  0.0655  -0.0741 174  ARG B NH1 
10011 N NH2 . ARG B 176  ? 0.5252 0.5999 0.2893 0.1212  0.0744  -0.0633 174  ARG B NH2 
10012 N N   . CYS B 177  ? 0.5574 0.5699 0.2509 0.1298  0.0562  -0.0847 175  CYS B N   
10013 C CA  . CYS B 177  ? 0.5229 0.5457 0.2082 0.1273  0.0613  -0.0796 175  CYS B CA  
10014 C C   . CYS B 177  ? 0.5752 0.5862 0.2454 0.1235  0.0553  -0.0803 175  CYS B C   
10015 O O   . CYS B 177  ? 0.5973 0.6138 0.2573 0.1229  0.0591  -0.0775 175  CYS B O   
10016 C CB  . CYS B 177  ? 0.5850 0.6249 0.2818 0.1213  0.0664  -0.0709 175  CYS B CB  
10017 S SG  . CYS B 177  ? 0.6498 0.7058 0.3667 0.1245  0.0731  -0.0687 175  CYS B SG  
10018 N N   . GLY B 178  ? 0.5685 0.5640 0.2372 0.1206  0.0461  -0.0835 176  GLY B N   
10019 C CA  . GLY B 178  ? 0.6507 0.6337 0.3047 0.1180  0.0396  -0.0851 176  GLY B CA  
10020 C C   . GLY B 178  ? 0.6254 0.6146 0.2750 0.1109  0.0400  -0.0778 176  GLY B C   
10021 O O   . GLY B 178  ? 0.6455 0.6457 0.3049 0.1065  0.0430  -0.0715 176  GLY B O   
10022 N N   . GLU B 179  ? 0.6730 0.6543 0.3072 0.1099  0.0366  -0.0788 177  GLU B N   
10023 C CA  . GLU B 179  ? 0.6798 0.6645 0.3075 0.1033  0.0358  -0.0720 177  GLU B CA  
10024 C C   . GLU B 179  ? 0.6337 0.6376 0.2653 0.1010  0.0454  -0.0638 177  GLU B C   
10025 O O   . GLU B 179  ? 0.6265 0.6350 0.2610 0.0944  0.0445  -0.0570 177  GLU B O   
10026 C CB  . GLU B 179  ? 0.7155 0.6900 0.3250 0.1036  0.0316  -0.0745 177  GLU B CB  
10027 C CG  . GLU B 179  ? 0.8108 0.7955 0.4107 0.1004  0.0369  -0.0675 177  GLU B CG  
10028 C CD  . GLU B 179  ? 0.9598 0.9347 0.5481 0.0949  0.0291  -0.0653 177  GLU B CD  
10029 O OE1 . GLU B 179  ? 0.9655 0.9254 0.5455 0.0964  0.0213  -0.0713 177  GLU B OE1 
10030 O OE2 . GLU B 179  ? 0.9455 0.9276 0.5331 0.0890  0.0306  -0.0573 177  GLU B OE2 
10031 N N   . PRO B 180  ? 0.6338 0.6492 0.2657 0.1058  0.0542  -0.0637 178  PRO B N   
10032 C CA  . PRO B 180  ? 0.6095 0.6434 0.2456 0.1024  0.0628  -0.0551 178  PRO B CA  
10033 C C   . PRO B 180  ? 0.6280 0.6715 0.2806 0.0977  0.0642  -0.0494 178  PRO B C   
10034 O O   . PRO B 180  ? 0.6046 0.6581 0.2588 0.0916  0.0672  -0.0410 178  PRO B O   
10035 C CB  . PRO B 180  ? 0.6240 0.6673 0.2602 0.1096  0.0712  -0.0576 178  PRO B CB  
10036 C CG  . PRO B 180  ? 0.6407 0.6688 0.2638 0.1154  0.0666  -0.0663 178  PRO B CG  
10037 C CD  . PRO B 180  ? 0.6137 0.6258 0.2404 0.1140  0.0566  -0.0708 178  PRO B CD  
10038 N N   . VAL B 181  ? 0.5397 0.5802 0.2045 0.1000  0.0619  -0.0533 179  VAL B N   
10039 C CA  . VAL B 181  ? 0.5679 0.6181 0.2481 0.0954  0.0633  -0.0478 179  VAL B CA  
10040 C C   . VAL B 181  ? 0.5821 0.6233 0.2605 0.0888  0.0554  -0.0453 179  VAL B C   
10041 O O   . VAL B 181  ? 0.5406 0.5908 0.2261 0.0829  0.0568  -0.0380 179  VAL B O   
10042 C CB  . VAL B 181  ? 0.5649 0.6163 0.2593 0.1000  0.0640  -0.0522 179  VAL B CB  
10043 C CG1 . VAL B 181  ? 0.5521 0.5848 0.2452 0.1016  0.0548  -0.0596 179  VAL B CG1 
10044 C CG2 . VAL B 181  ? 0.5663 0.6320 0.2769 0.0956  0.0676  -0.0457 179  VAL B CG2 
10045 N N   . ILE B 182  ? 0.5691 0.5926 0.2380 0.0895  0.0468  -0.0509 180  ILE B N   
10046 C CA  . ILE B 182  ? 0.5916 0.6058 0.2578 0.0836  0.0387  -0.0487 180  ILE B CA  
10047 C C   . ILE B 182  ? 0.5980 0.6181 0.2557 0.0781  0.0404  -0.0406 180  ILE B C   
10048 O O   . ILE B 182  ? 0.5879 0.6117 0.2547 0.0706  0.0388  -0.0336 180  ILE B O   
10049 C CB  . ILE B 182  ? 0.5912 0.5856 0.2492 0.0855  0.0290  -0.0563 180  ILE B CB  
10050 C CG1 . ILE B 182  ? 0.5773 0.5657 0.2453 0.0897  0.0268  -0.0633 180  ILE B CG1 
10051 C CG2 . ILE B 182  ? 0.6037 0.5886 0.2611 0.0786  0.0201  -0.0535 180  ILE B CG2 
10052 C CD1 . ILE B 182  ? 0.6293 0.5999 0.2899 0.0925  0.0188  -0.0713 180  ILE B CD1 
10053 N N   . ARG B 183  ? 0.5984 0.6191 0.2432 0.0799  0.0434  -0.0406 181  ARG B N   
10054 C CA  . ARG B 183  ? 0.6575 0.6835 0.2935 0.0745  0.0451  -0.0326 181  ARG B CA  
10055 C C   . ARG B 183  ? 0.6486 0.6929 0.2959 0.0701  0.0527  -0.0236 181  ARG B C   
10056 O O   . ARG B 183  ? 0.6433 0.6899 0.2903 0.0633  0.0510  -0.0159 181  ARG B O   
10057 C CB  . ARG B 183  ? 0.7208 0.7462 0.3418 0.0777  0.0483  -0.0345 181  ARG B CB  
10058 C CG  . ARG B 183  ? 0.8012 0.8356 0.4139 0.0727  0.0528  -0.0257 181  ARG B CG  
10059 C CD  . ARG B 183  ? 0.8198 0.8479 0.4284 0.0652  0.0458  -0.0194 181  ARG B CD  
10060 N NE  . ARG B 183  ? 0.8392 0.8489 0.4410 0.0659  0.0349  -0.0252 181  ARG B NE  
10061 C CZ  . ARG B 183  ? 0.8629 0.8641 0.4635 0.0607  0.0268  -0.0218 181  ARG B CZ  
10062 N NH1 . ARG B 183  ? 0.8770 0.8855 0.4820 0.0546  0.0280  -0.0125 181  ARG B NH1 
10063 N NH2 . ARG B 183  ? 0.9116 0.8964 0.5071 0.0616  0.0168  -0.0276 181  ARG B NH2 
10064 N N   . ARG B 184  ? 0.6428 0.6998 0.3007 0.0737  0.0607  -0.0242 182  ARG B N   
10065 C CA  . ARG B 184  ? 0.6239 0.6986 0.2945 0.0692  0.0674  -0.0158 182  ARG B CA  
10066 C C   . ARG B 184  ? 0.6323 0.7063 0.3152 0.0637  0.0627  -0.0125 182  ARG B C   
10067 O O   . ARG B 184  ? 0.6603 0.7420 0.3509 0.0556  0.0637  -0.0038 182  ARG B O   
10068 C CB  . ARG B 184  ? 0.6359 0.7233 0.3169 0.0746  0.0756  -0.0180 182  ARG B CB  
10069 C CG  . ARG B 184  ? 0.6916 0.7857 0.3636 0.0780  0.0825  -0.0177 182  ARG B CG  
10070 C CD  . ARG B 184  ? 0.7239 0.8342 0.3990 0.0716  0.0891  -0.0072 182  ARG B CD  
10071 N NE  . ARG B 184  ? 0.6925 0.8201 0.3840 0.0727  0.0966  -0.0045 182  ARG B NE  
10072 C CZ  . ARG B 184  ? 0.7059 0.8444 0.4124 0.0668  0.0980  0.0023  182  ARG B CZ  
10073 N NH1 . ARG B 184  ? 0.6962 0.8311 0.4034 0.0589  0.0930  0.0078  182  ARG B NH1 
10074 N NH2 . ARG B 184  ? 0.6880 0.8415 0.4094 0.0687  0.1042  0.0036  182  ARG B NH2 
10075 N N   . GLY B 185  ? 0.5911 0.6535 0.2821 0.0654  0.0564  -0.0193 183  GLY B N   
10076 C CA  . GLY B 185  ? 0.5751 0.6341 0.2840 0.0582  0.0508  -0.0165 183  GLY B CA  
10077 C C   . GLY B 185  ? 0.5916 0.6410 0.2973 0.0504  0.0434  -0.0119 183  GLY B C   
10078 O O   . GLY B 185  ? 0.5657 0.6192 0.2831 0.0428  0.0424  -0.0051 183  GLY B O   
10079 N N   . VAL B 186  ? 0.5664 0.6027 0.2563 0.0524  0.0379  -0.0155 184  VAL B N   
10080 C CA  . VAL B 186  ? 0.6457 0.6726 0.3311 0.0458  0.0306  -0.0111 184  VAL B CA  
10081 C C   . VAL B 186  ? 0.6239 0.6616 0.3063 0.0400  0.0353  -0.0010 184  VAL B C   
10082 O O   . VAL B 186  ? 0.6095 0.6464 0.3005 0.0322  0.0318  0.0054  184  VAL B O   
10083 C CB  . VAL B 186  ? 0.6158 0.6281 0.2830 0.0497  0.0245  -0.0169 184  VAL B CB  
10084 C CG1 . VAL B 186  ? 0.6603 0.6651 0.3194 0.0435  0.0182  -0.0112 184  VAL B CG1 
10085 C CG2 . VAL B 186  ? 0.6064 0.6064 0.2796 0.0530  0.0177  -0.0255 184  VAL B CG2 
10086 N N   . ASP B 187  ? 0.6394 0.6877 0.3097 0.0438  0.0435  0.0006  185  ASP B N   
10087 C CA  . ASP B 187  ? 0.6507 0.7102 0.3175 0.0381  0.0485  0.0107  185  ASP B CA  
10088 C C   . ASP B 187  ? 0.6445 0.7161 0.3311 0.0319  0.0518  0.0172  185  ASP B C   
10089 O O   . ASP B 187  ? 0.6109 0.6854 0.3001 0.0239  0.0511  0.0260  185  ASP B O   
10090 C CB  . ASP B 187  ? 0.6691 0.7398 0.3206 0.0442  0.0577  0.0107  185  ASP B CB  
10091 C CG  . ASP B 187  ? 0.7663 0.8238 0.3979 0.0489  0.0540  0.0048  185  ASP B CG  
10092 O OD1 . ASP B 187  ? 0.7741 0.8161 0.3997 0.0475  0.0444  0.0026  185  ASP B OD1 
10093 O OD2 . ASP B 187  ? 0.6684 0.7302 0.2936 0.0530  0.0599  0.0022  185  ASP B OD2 
10094 N N   . MET B 188  ? 0.6504 0.7286 0.3508 0.0354  0.0552  0.0131  186  MET B N   
10095 C CA  . MET B 188  ? 0.5798 0.6691 0.2994 0.0298  0.0578  0.0186  186  MET B CA  
10096 C C   . MET B 188  ? 0.6226 0.7007 0.3535 0.0226  0.0489  0.0203  186  MET B C   
10097 O O   . MET B 188  ? 0.6285 0.7115 0.3680 0.0148  0.0487  0.0281  186  MET B O   
10098 C CB  . MET B 188  ? 0.6281 0.7258 0.3584 0.0362  0.0628  0.0130  186  MET B CB  
10099 C CG  . MET B 188  ? 0.6772 0.7873 0.4271 0.0313  0.0658  0.0180  186  MET B CG  
10100 S SD  . MET B 188  ? 0.7616 0.8928 0.5109 0.0268  0.0752  0.0287  186  MET B SD  
10101 C CE  . MET B 188  ? 0.7285 0.8670 0.4598 0.0375  0.0835  0.0242  186  MET B CE  
10102 N N   . ALA B 189  ? 0.6097 0.6730 0.3413 0.0252  0.0415  0.0131  187  ALA B N   
10103 C CA  . ALA B 189  ? 0.6099 0.6631 0.3526 0.0193  0.0333  0.0142  187  ALA B CA  
10104 C C   . ALA B 189  ? 0.6240 0.6703 0.3587 0.0129  0.0284  0.0207  187  ALA B C   
10105 O O   . ALA B 189  ? 0.6332 0.6777 0.3778 0.0060  0.0248  0.0258  187  ALA B O   
10106 C CB  . ALA B 189  ? 0.5623 0.6022 0.3071 0.0237  0.0268  0.0052  187  ALA B CB  
10107 N N   . MET B 190  ? 0.6237 0.6654 0.3401 0.0153  0.0278  0.0205  188  MET B N   
10108 C CA  . MET B 190  ? 0.6660 0.7018 0.3734 0.0095  0.0236  0.0274  188  MET B CA  
10109 C C   . MET B 190  ? 0.6495 0.6970 0.3626 0.0022  0.0283  0.0376  188  MET B C   
10110 O O   . MET B 190  ? 0.6232 0.6654 0.3419 -0.0049 0.0232  0.0432  188  MET B O   
10111 C CB  . MET B 190  ? 0.6306 0.6624 0.3160 0.0137  0.0240  0.0259  188  MET B CB  
10112 C CG  . MET B 190  ? 0.7034 0.7200 0.3790 0.0108  0.0145  0.0273  188  MET B CG  
10113 S SD  . MET B 190  ? 0.8978 0.9122 0.5462 0.0144  0.0160  0.0279  188  MET B SD  
10114 C CE  . MET B 190  ? 0.6715 0.6809 0.3130 0.0249  0.0162  0.0151  188  MET B CE  
10115 N N   . ARG B 191  ? 0.6417 0.7052 0.3538 0.0039  0.0380  0.0400  189  ARG B N   
10116 C CA  . ARG B 191  ? 0.6452 0.7213 0.3633 -0.0033 0.0427  0.0501  189  ARG B CA  
10117 C C   . ARG B 191  ? 0.6239 0.7006 0.3622 -0.0089 0.0399  0.0520  189  ARG B C   
10118 O O   . ARG B 191  ? 0.6193 0.6939 0.3619 -0.0170 0.0367  0.0594  189  ARG B O   
10119 C CB  . ARG B 191  ? 0.6192 0.7140 0.3343 0.0004  0.0540  0.0516  189  ARG B CB  
10120 N N   . MET B 192  ? 0.5932 0.6717 0.3435 -0.0046 0.0407  0.0451  190  MET B N   
10121 C CA  . MET B 192  ? 0.5859 0.6655 0.3548 -0.0095 0.0384  0.0465  190  MET B CA  
10122 C C   . MET B 192  ? 0.6190 0.6822 0.3906 -0.0141 0.0284  0.0468  190  MET B C   
10123 O O   . MET B 192  ? 0.5963 0.6590 0.3754 -0.0216 0.0259  0.0532  190  MET B O   
10124 C CB  . MET B 192  ? 0.5973 0.6806 0.3769 -0.0034 0.0406  0.0387  190  MET B CB  
10125 C CG  . MET B 192  ? 0.6562 0.7557 0.4342 0.0020  0.0503  0.0379  190  MET B CG  
10126 S SD  . MET B 192  ? 0.7171 0.8213 0.5097 0.0081  0.0525  0.0301  190  MET B SD  
10127 C CE  . MET B 192  ? 0.5730 0.6837 0.3850 -0.0009 0.0513  0.0365  190  MET B CE  
10128 N N   . MET B 193  ? 0.5707 0.6205 0.3365 -0.0096 0.0225  0.0400  191  MET B N   
10129 C CA  . MET B 193  ? 0.5862 0.6215 0.3561 -0.0131 0.0131  0.0396  191  MET B CA  
10130 C C   . MET B 193  ? 0.6427 0.6711 0.4021 -0.0183 0.0090  0.0467  191  MET B C   
10131 O O   . MET B 193  ? 0.5820 0.6002 0.3463 -0.0225 0.0017  0.0486  191  MET B O   
10132 C CB  . MET B 193  ? 0.6489 0.6729 0.4169 -0.0069 0.0078  0.0305  191  MET B CB  
10133 C CG  . MET B 193  ? 0.6378 0.6646 0.4191 -0.0032 0.0093  0.0238  191  MET B CG  
10134 S SD  . MET B 193  ? 0.6942 0.7064 0.4752 0.0019  0.0015  0.0145  191  MET B SD  
10135 C CE  . MET B 193  ? 0.5759 0.5854 0.3364 0.0078  0.0029  0.0113  191  MET B CE  
10136 N N   . GLY B 194  ? 0.6319 0.6658 0.3769 -0.0179 0.0134  0.0508  192  GLY B N   
10137 C CA  . GLY B 194  ? 0.6136 0.6403 0.3467 -0.0224 0.0093  0.0575  192  GLY B CA  
10138 C C   . GLY B 194  ? 0.6392 0.6743 0.3738 -0.0303 0.0128  0.0682  192  GLY B C   
10139 O O   . GLY B 194  ? 0.6490 0.6760 0.3792 -0.0360 0.0075  0.0746  192  GLY B O   
10140 N N   . GLU B 195  ? 0.6216 0.6730 0.3630 -0.0309 0.0213  0.0704  193  GLU B N   
10141 C CA  . GLU B 195  ? 0.6336 0.6955 0.3751 -0.0383 0.0258  0.0810  193  GLU B CA  
10142 C C   . GLU B 195  ? 0.6224 0.6963 0.3815 -0.0422 0.0299  0.0834  193  GLU B C   
10143 O O   . GLU B 195  ? 0.5244 0.6035 0.2870 -0.0502 0.0308  0.0925  193  GLU B O   
10144 C CB  . GLU B 195  ? 0.6489 0.7224 0.3755 -0.0356 0.0340  0.0839  193  GLU B CB  
10145 N N   . GLN B 196  ? 0.6456 0.7239 0.4157 -0.0371 0.0320  0.0760  194  GLN B N   
10146 C CA  . GLN B 196  ? 0.6097 0.6993 0.3964 -0.0404 0.0354  0.0779  194  GLN B CA  
10147 C C   . GLN B 196  ? 0.6171 0.6957 0.4171 -0.0432 0.0278  0.0751  194  GLN B C   
10148 O O   . GLN B 196  ? 0.6366 0.7166 0.4459 -0.0507 0.0261  0.0809  194  GLN B O   
10149 C CB  . GLN B 196  ? 0.6078 0.7110 0.3984 -0.0330 0.0432  0.0721  194  GLN B CB  
10150 N N   . PHE B 197  ? 0.5765 0.6441 0.3774 -0.0375 0.0232  0.0663  195  PHE B N   
10151 C CA  . PHE B 197  ? 0.6121 0.6696 0.4250 -0.0396 0.0164  0.0634  195  PHE B CA  
10152 C C   . PHE B 197  ? 0.5858 0.6296 0.3953 -0.0455 0.0085  0.0683  195  PHE B C   
10153 O O   . PHE B 197  ? 0.5828 0.6217 0.4023 -0.0505 0.0042  0.0702  195  PHE B O   
10154 C CB  . PHE B 197  ? 0.5777 0.6283 0.3926 -0.0319 0.0140  0.0532  195  PHE B CB  
10155 C CG  . PHE B 197  ? 0.5690 0.6317 0.3892 -0.0263 0.0208  0.0483  195  PHE B CG  
10156 C CD1 . PHE B 197  ? 0.6227 0.6996 0.4528 -0.0291 0.0265  0.0519  195  PHE B CD1 
10157 C CD2 . PHE B 197  ? 0.6276 0.6871 0.4429 -0.0183 0.0213  0.0402  195  PHE B CD2 
10158 C CE1 . PHE B 197  ? 0.6377 0.7258 0.4728 -0.0235 0.0325  0.0476  195  PHE B CE1 
10159 C CE2 . PHE B 197  ? 0.6107 0.6804 0.4305 -0.0128 0.0273  0.0358  195  PHE B CE2 
10160 C CZ  . PHE B 197  ? 0.6308 0.7149 0.4606 -0.0152 0.0330  0.0395  195  PHE B CZ  
10161 N N   . VAL B 198  ? 0.5368 0.5740 0.3318 -0.0449 0.0064  0.0703  196  VAL B N   
10162 C CA  . VAL B 198  ? 0.5600 0.5847 0.3505 -0.0506 -0.0008 0.0761  196  VAL B CA  
10163 C C   . VAL B 198  ? 0.5926 0.6232 0.3708 -0.0548 0.0028  0.0850  196  VAL B C   
10164 O O   . VAL B 198  ? 0.6031 0.6436 0.3723 -0.0511 0.0096  0.0847  196  VAL B O   
10165 C CB  . VAL B 198  ? 0.5207 0.5293 0.3055 -0.0465 -0.0089 0.0706  196  VAL B CB  
10166 C CG1 . VAL B 198  ? 0.5633 0.5667 0.3612 -0.0430 -0.0124 0.0625  196  VAL B CG1 
10167 C CG2 . VAL B 198  ? 0.5454 0.5547 0.3157 -0.0404 -0.0066 0.0672  196  VAL B CG2 
10168 N N   . THR B 199  ? 0.5670 0.5914 0.3447 -0.0625 -0.0016 0.0931  197  THR B N   
10169 C CA  . THR B 199  ? 0.5561 0.5837 0.3209 -0.0670 0.0007  0.1023  197  THR B CA  
10170 C C   . THR B 199  ? 0.5967 0.6137 0.3451 -0.0630 -0.0033 0.1007  197  THR B C   
10171 O O   . THR B 199  ? 0.5931 0.6153 0.3276 -0.0634 0.0007  0.1055  197  THR B O   
10172 C CB  . THR B 199  ? 0.5561 0.5791 0.3257 -0.0768 -0.0034 0.1116  197  THR B CB  
10173 O OG1 . THR B 199  ? 0.5383 0.5687 0.3244 -0.0797 -0.0014 0.1110  197  THR B OG1 
10174 C CG2 . THR B 199  ? 0.5880 0.6191 0.3472 -0.0827 0.0010  0.1222  197  THR B CG2 
10175 N N   . GLY B 200  ? 0.5655 0.5683 0.3150 -0.0590 -0.0110 0.0940  198  GLY B N   
10176 C CA  . GLY B 200  ? 0.6017 0.5949 0.3369 -0.0543 -0.0152 0.0911  198  GLY B CA  
10177 C C   . GLY B 200  ? 0.5985 0.5788 0.3403 -0.0500 -0.0231 0.0829  198  GLY B C   
10178 O O   . GLY B 200  ? 0.5795 0.5560 0.3355 -0.0517 -0.0264 0.0812  198  GLY B O   
10179 N N   . GLU B 201  ? 0.6668 0.6406 0.3979 -0.0442 -0.0261 0.0778  199  GLU B N   
10180 C CA  . GLU B 201  ? 0.6863 0.6486 0.4231 -0.0399 -0.0337 0.0701  199  GLU B CA  
10181 C C   . GLU B 201  ? 0.6245 0.5727 0.3625 -0.0437 -0.0433 0.0742  199  GLU B C   
10182 O O   . GLU B 201  ? 0.6550 0.5957 0.4040 -0.0422 -0.0490 0.0695  199  GLU B O   
10183 C CB  . GLU B 201  ? 0.6446 0.6043 0.3695 -0.0331 -0.0345 0.0637  199  GLU B CB  
10184 N N   . THR B 202  ? 0.6237 0.5685 0.3507 -0.0485 -0.0450 0.0829  200  THR B N   
10185 C CA  . THR B 202  ? 0.6598 0.5909 0.3869 -0.0524 -0.0541 0.0878  200  THR B CA  
10186 C C   . THR B 202  ? 0.6766 0.6103 0.4040 -0.0607 -0.0520 0.0981  200  THR B C   
10187 O O   . THR B 202  ? 0.6353 0.5815 0.3589 -0.0634 -0.0438 0.1024  200  THR B O   
10188 C CB  . THR B 202  ? 0.6814 0.6027 0.3927 -0.0504 -0.0602 0.0890  200  THR B CB  
10189 O OG1 . THR B 202  ? 0.7109 0.6386 0.4065 -0.0529 -0.0549 0.0957  200  THR B OG1 
10190 C CG2 . THR B 202  ? 0.7453 0.6648 0.4551 -0.0426 -0.0621 0.0791  200  THR B CG2 
10191 N N   . ILE B 203  ? 0.6498 0.5716 0.3821 -0.0648 -0.0596 0.1021  201  ILE B N   
10192 C CA  . ILE B 203  ? 0.6515 0.5736 0.3840 -0.0733 -0.0590 0.1123  201  ILE B CA  
10193 C C   . ILE B 203  ? 0.6417 0.5664 0.3566 -0.0767 -0.0566 0.1210  201  ILE B C   
10194 O O   . ILE B 203  ? 0.6027 0.5358 0.3160 -0.0831 -0.0513 0.1290  201  ILE B O   
10195 C CB  . ILE B 203  ? 0.6240 0.5304 0.3636 -0.0763 -0.0688 0.1145  201  ILE B CB  
10196 C CG1 . ILE B 203  ? 0.5993 0.5060 0.3419 -0.0855 -0.0680 0.1241  201  ILE B CG1 
10197 C CG2 . ILE B 203  ? 0.6042 0.4963 0.3326 -0.0744 -0.0776 0.1162  201  ILE B CG2 
10198 C CD1 . ILE B 203  ? 0.5483 0.4687 0.3032 -0.0878 -0.0603 0.1227  201  ILE B CD1 
10199 N N   . ARG B 204  ? 0.6763 0.5947 0.3777 -0.0725 -0.0603 0.1194  202  ARG B N   
10200 C CA  . ARG B 204  ? 0.6868 0.6076 0.3699 -0.0749 -0.0580 0.1271  202  ARG B CA  
10201 C C   . ARG B 204  ? 0.6659 0.6050 0.3448 -0.0744 -0.0461 0.1273  202  ARG B C   
10202 O O   . ARG B 204  ? 0.6683 0.6150 0.3401 -0.0801 -0.0410 0.1365  202  ARG B O   
10203 C CB  . ARG B 204  ? 0.7223 0.6330 0.3923 -0.0694 -0.0644 0.1235  202  ARG B CB  
10204 C CG  . ARG B 204  ? 0.7574 0.6623 0.4092 -0.0732 -0.0673 0.1330  202  ARG B CG  
10205 C CD  . ARG B 204  ? 0.7915 0.6859 0.4319 -0.0673 -0.0747 0.1285  202  ARG B CD  
10206 N NE  . ARG B 204  ? 0.7934 0.6960 0.4290 -0.0602 -0.0695 0.1196  202  ARG B NE  
10207 C CZ  . ARG B 204  ? 0.7968 0.7078 0.4164 -0.0589 -0.0630 0.1211  202  ARG B CZ  
10208 N NH1 . ARG B 204  ? 0.8397 0.7530 0.4462 -0.0644 -0.0604 0.1315  202  ARG B NH1 
10209 N NH2 . ARG B 204  ? 0.8237 0.7406 0.4399 -0.0519 -0.0589 0.1120  202  ARG B NH2 
10210 N N   . GLU B 205  ? 0.6668 0.6135 0.3504 -0.0674 -0.0415 0.1175  203  GLU B N   
10211 C CA  . GLU B 205  ? 0.6780 0.6421 0.3582 -0.0657 -0.0303 0.1169  203  GLU B CA  
10212 C C   . GLU B 205  ? 0.6406 0.6165 0.3338 -0.0718 -0.0242 0.1219  203  GLU B C   
10213 O O   . GLU B 205  ? 0.6401 0.6296 0.3282 -0.0747 -0.0159 0.1278  203  GLU B O   
10214 C CB  . GLU B 205  ? 0.6847 0.6523 0.3675 -0.0567 -0.0279 0.1050  203  GLU B CB  
10215 C CG  . GLU B 205  ? 0.7496 0.7315 0.4225 -0.0527 -0.0179 0.1033  203  GLU B CG  
10216 C CD  . GLU B 205  ? 0.8189 0.8026 0.4950 -0.0439 -0.0162 0.0914  203  GLU B CD  
10217 O OE1 . GLU B 205  ? 0.7619 0.7464 0.4545 -0.0427 -0.0166 0.0860  203  GLU B OE1 
10218 O OE2 . GLU B 205  ? 0.9144 0.8980 0.5760 -0.0383 -0.0148 0.0874  203  GLU B OE2 
10219 N N   . ALA B 206  ? 0.6154 0.5864 0.3251 -0.0738 -0.0282 0.1198  204  ALA B N   
10220 C CA  . ALA B 206  ? 0.6137 0.5953 0.3365 -0.0795 -0.0231 0.1238  204  ALA B CA  
10221 C C   . ALA B 206  ? 0.6323 0.6136 0.3506 -0.0892 -0.0237 0.1365  204  ALA B C   
10222 O O   . ALA B 206  ? 0.6305 0.6258 0.3529 -0.0942 -0.0166 0.1423  204  ALA B O   
10223 C CB  . ALA B 206  ? 0.5321 0.5072 0.2725 -0.0790 -0.0279 0.1179  204  ALA B CB  
10224 N N   . LEU B 207  ? 0.6216 0.5873 0.3319 -0.0921 -0.0322 0.1413  205  LEU B N   
10225 C CA  . LEU B 207  ? 0.6207 0.5845 0.3259 -0.1016 -0.0334 0.1539  205  LEU B CA  
10226 C C   . LEU B 207  ? 0.6698 0.6468 0.3605 -0.1032 -0.0252 0.1608  205  LEU B C   
10227 O O   . LEU B 207  ? 0.6875 0.6741 0.3792 -0.1110 -0.0205 0.1702  205  LEU B O   
10228 C CB  . LEU B 207  ? 0.6381 0.5814 0.3374 -0.1034 -0.0448 0.1571  205  LEU B CB  
10229 C CG  . LEU B 207  ? 0.6187 0.5481 0.3322 -0.1041 -0.0534 0.1535  205  LEU B CG  
10230 C CD1 . LEU B 207  ? 0.6452 0.5550 0.3511 -0.1031 -0.0644 0.1547  205  LEU B CD1 
10231 C CD2 . LEU B 207  ? 0.5594 0.4912 0.2837 -0.1132 -0.0527 0.1606  205  LEU B CD2 
10232 N N   . LYS B 208  ? 0.6746 0.6524 0.3514 -0.0961 -0.0235 0.1562  206  LYS B N   
10233 C CA  . LYS B 208  ? 0.7440 0.7348 0.4060 -0.0967 -0.0150 0.1618  206  LYS B CA  
10234 C C   . LYS B 208  ? 0.6850 0.6973 0.3550 -0.0957 -0.0033 0.1604  206  LYS B C   
10235 O O   . LYS B 208  ? 0.6920 0.7178 0.3583 -0.0985 0.0046  0.1669  206  LYS B O   
10236 C CB  . LYS B 208  ? 0.7416 0.7271 0.3864 -0.0887 -0.0165 0.1562  206  LYS B CB  
10237 N N   . ARG B 209  ? 0.6731 0.6890 0.3572 -0.0905 -0.0019 0.1506  207  ARG B N   
10238 C CA  . ARG B 209  ? 0.6694 0.7055 0.3622 -0.0892 0.0086  0.1491  207  ARG B CA  
10239 C C   . ARG B 209  ? 0.6917 0.7354 0.3992 -0.0983 0.0103  0.1567  207  ARG B C   
10240 O O   . ARG B 209  ? 0.6769 0.7390 0.3915 -0.0988 0.0192  0.1578  207  ARG B O   
10241 C CB  . ARG B 209  ? 0.6802 0.7170 0.3819 -0.0800 0.0094  0.1359  207  ARG B CB  
10242 C CG  . ARG B 209  ? 0.6653 0.6988 0.3524 -0.0707 0.0099  0.1282  207  ARG B CG  
10243 C CD  . ARG B 209  ? 0.6597 0.6947 0.3562 -0.0624 0.0110  0.1160  207  ARG B CD  
10244 N NE  . ARG B 209  ? 0.7345 0.7649 0.4175 -0.0538 0.0106  0.1082  207  ARG B NE  
10245 C CZ  . ARG B 209  ? 0.7325 0.7605 0.4204 -0.0461 0.0099  0.0973  207  ARG B CZ  
10246 N NH1 . ARG B 209  ? 0.6492 0.6791 0.3549 -0.0456 0.0097  0.0927  207  ARG B NH1 
10247 N NH2 . ARG B 209  ? 0.7846 0.8079 0.4587 -0.0389 0.0092  0.0909  207  ARG B NH2 
10248 N N   . SER B 210  ? 0.7000 0.7299 0.4120 -0.1056 0.0018  0.1621  208  SER B N   
10249 C CA  . SER B 210  ? 0.6424 0.6773 0.3680 -0.1148 0.0020  0.1692  208  SER B CA  
10250 C C   . SER B 210  ? 0.6643 0.7075 0.3846 -0.1231 0.0061  0.1817  208  SER B C   
10251 O O   . SER B 210  ? 0.6454 0.6983 0.3787 -0.1295 0.0091  0.1866  208  SER B O   
10252 C CB  . SER B 210  ? 0.6133 0.6286 0.3472 -0.1182 -0.0093 0.1683  208  SER B CB  
10253 O OG  . SER B 210  ? 0.6015 0.6110 0.3443 -0.1103 -0.0122 0.1560  208  SER B OG  
10254 N N   . LYS B 211  ? 0.6494 0.6884 0.3549 -0.1211 0.0062  0.1843  209  LYS B N   
10255 C CA  . LYS B 211  ? 0.6598 0.7037 0.3637 -0.1273 0.0092  0.1939  209  LYS B CA  
10256 C C   . LYS B 211  ? 0.6420 0.7094 0.3543 -0.1277 0.0208  0.1956  209  LYS B C   
10257 O O   . LYS B 211  ? 0.6522 0.7260 0.3722 -0.1355 0.0226  0.2036  209  LYS B O   
10258 C CB  . LYS B 211  ? 0.6649 0.7013 0.3502 -0.1239 0.0081  0.1955  209  LYS B CB  
10259 C CG  . LYS B 211  ? 0.8126 0.8272 0.4885 -0.1213 -0.0030 0.1922  209  LYS B CG  
10260 C CD  . LYS B 211  ? 0.8359 0.8339 0.5180 -0.1294 -0.0134 0.1981  209  LYS B CD  
10261 C CE  . LYS B 211  ? 0.8741 0.8507 0.5470 -0.1259 -0.0244 0.1948  209  LYS B CE  
10262 N NZ  . LYS B 211  ? 0.8407 0.8001 0.5191 -0.1329 -0.0347 0.2003  209  LYS B NZ  
10263 N N   . GLU B 212  ? 0.6513 0.7314 0.3625 -0.1192 0.0286  0.1879  210  GLU B N   
10264 C CA  . GLU B 212  ? 0.6450 0.7474 0.3630 -0.1181 0.0399  0.1890  210  GLU B CA  
10265 C C   . GLU B 212  ? 0.6494 0.7614 0.3874 -0.1253 0.0408  0.1924  210  GLU B C   
10266 O O   . GLU B 212  ? 0.6713 0.7955 0.4159 -0.1306 0.0456  0.1993  210  GLU B O   
10267 C CB  . GLU B 212  ? 0.6280 0.7400 0.3416 -0.1068 0.0470  0.1791  210  GLU B CB  
10268 N N   . LEU B 213  ? 0.6129 0.7196 0.3605 -0.1255 0.0359  0.1878  211  LEU B N   
10269 C CA  . LEU B 213  ? 0.6524 0.7676 0.4187 -0.1322 0.0362  0.1906  211  LEU B CA  
10270 C C   . LEU B 213  ? 0.6397 0.7422 0.4106 -0.1433 0.0277  0.1989  211  LEU B C   
10271 O O   . LEU B 213  ? 0.6302 0.7416 0.4143 -0.1504 0.0289  0.2041  211  LEU B O   
10272 C CB  . LEU B 213  ? 0.5861 0.7015 0.3611 -0.1281 0.0349  0.1823  211  LEU B CB  
10273 C CG  . LEU B 213  ? 0.5620 0.6953 0.3392 -0.1186 0.0448  0.1748  211  LEU B CG  
10274 C CD1 . LEU B 213  ? 0.5797 0.7129 0.3656 -0.1149 0.0432  0.1669  211  LEU B CD1 
10275 C CD2 . LEU B 213  ? 0.6337 0.7880 0.4210 -0.1207 0.0536  0.1793  211  LEU B CD2 
10276 N N   . GLU B 214  ? 0.5991 0.6808 0.3592 -0.1446 0.0188  0.2003  212  GLU B N   
10277 C CA  . GLU B 214  ? 0.5958 0.6646 0.3588 -0.1546 0.0108  0.2084  212  GLU B CA  
10278 C C   . GLU B 214  ? 0.6249 0.7043 0.3876 -0.1602 0.0157  0.2175  212  GLU B C   
10279 O O   . GLU B 214  ? 0.6001 0.6795 0.3727 -0.1694 0.0128  0.2241  212  GLU B O   
10280 C CB  . GLU B 214  ? 0.6451 0.6902 0.3956 -0.1536 0.0008  0.2080  212  GLU B CB  
10281 C CG  . GLU B 214  ? 0.6211 0.6515 0.3742 -0.1508 -0.0069 0.2010  212  GLU B CG  
10282 C CD  . GLU B 214  ? 0.6221 0.6289 0.3639 -0.1501 -0.0175 0.2012  212  GLU B CD  
10283 O OE1 . GLU B 214  ? 0.6636 0.6666 0.3941 -0.1504 -0.0178 0.2058  212  GLU B OE1 
10284 O OE2 . GLU B 214  ? 0.6657 0.6576 0.4101 -0.1490 -0.0254 0.1968  212  GLU B OE2 
10285 N N   . GLU B 215  ? 0.6009 0.6889 0.3518 -0.1550 0.0228  0.2177  213  GLU B N   
10286 C CA  . GLU B 215  ? 0.6079 0.7069 0.3578 -0.1599 0.0282  0.2263  213  GLU B CA  
10287 C C   . GLU B 215  ? 0.6255 0.7462 0.3915 -0.1629 0.0357  0.2280  213  GLU B C   
10288 O O   . GLU B 215  ? 0.6808 0.8094 0.4511 -0.1700 0.0379  0.2363  213  GLU B O   
10289 C CB  . GLU B 215  ? 0.6728 0.7758 0.4056 -0.1526 0.0345  0.2253  213  GLU B CB  
10290 N N   . LYS B 216  ? 0.6787 0.8091 0.4540 -0.1578 0.0394  0.2206  214  LYS B N   
10291 C CA  . LYS B 216  ? 0.6320 0.7821 0.4241 -0.1603 0.0453  0.2216  214  LYS B CA  
10292 C C   . LYS B 216  ? 0.6729 0.8170 0.4801 -0.1692 0.0377  0.2241  214  LYS B C   
10293 O O   . LYS B 216  ? 0.6696 0.8291 0.4917 -0.1727 0.0412  0.2258  214  LYS B O   
10294 C CB  . LYS B 216  ? 0.6281 0.7916 0.4231 -0.1500 0.0529  0.2122  214  LYS B CB  
10295 N N   . GLY B 217  ? 0.5638 0.6859 0.3675 -0.1726 0.0272  0.2241  215  GLY B N   
10296 C CA  . GLY B 217  ? 0.5741 0.6874 0.3902 -0.1810 0.0190  0.2264  215  GLY B CA  
10297 C C   . GLY B 217  ? 0.5816 0.6834 0.4013 -0.1778 0.0134  0.2186  215  GLY B C   
10298 O O   . GLY B 217  ? 0.6003 0.6925 0.4292 -0.1843 0.0059  0.2197  215  GLY B O   
10299 N N   . PHE B 218  ? 0.5626 0.6650 0.3754 -0.1680 0.0166  0.2105  216  PHE B N   
10300 C CA  . PHE B 218  ? 0.5529 0.6437 0.3684 -0.1651 0.0109  0.2034  216  PHE B CA  
10301 C C   . PHE B 218  ? 0.5481 0.6128 0.3539 -0.1670 0.0000  0.2042  216  PHE B C   
10302 O O   . PHE B 218  ? 0.5959 0.6523 0.3906 -0.1681 -0.0023 0.2087  216  PHE B O   
10303 C CB  . PHE B 218  ? 0.5689 0.6681 0.3797 -0.1541 0.0173  0.1944  216  PHE B CB  
10304 C CG  . PHE B 218  ? 0.5816 0.7043 0.4039 -0.1510 0.0268  0.1917  216  PHE B CG  
10305 C CD1 . PHE B 218  ? 0.6127 0.7533 0.4336 -0.1484 0.0361  0.1941  216  PHE B CD1 
10306 C CD2 . PHE B 218  ? 0.5864 0.7130 0.4210 -0.1502 0.0263  0.1867  216  PHE B CD2 
10307 C CE1 . PHE B 218  ? 0.6002 0.7619 0.4321 -0.1448 0.0445  0.1914  216  PHE B CE1 
10308 C CE2 . PHE B 218  ? 0.5865 0.7346 0.4322 -0.1469 0.0346  0.1842  216  PHE B CE2 
10309 C CZ  . PHE B 218  ? 0.6114 0.7769 0.4559 -0.1440 0.0436  0.1864  216  PHE B CZ  
10310 N N   . SER B 219  ? 0.5774 0.6290 0.3877 -0.1670 -0.0070 0.1996  217  SER B N   
10311 C CA  . SER B 219  ? 0.5537 0.5805 0.3565 -0.1651 -0.0172 0.1966  217  SER B CA  
10312 C C   . SER B 219  ? 0.5318 0.5544 0.3382 -0.1533 -0.0178 0.1823  217  SER B C   
10313 O O   . SER B 219  ? 0.5381 0.5761 0.3518 -0.1481 -0.0107 0.1762  217  SER B O   
10314 C CB  . SER B 219  ? 0.5345 0.5449 0.3435 -0.1743 -0.0270 0.2016  217  SER B CB  
10315 O OG  . SER B 219  ? 0.5844 0.5957 0.4087 -0.1741 -0.0286 0.1951  217  SER B OG  
10316 N N   . TYR B 220  ? 0.5351 0.5371 0.3368 -0.1491 -0.0263 0.1772  218  TYR B N   
10317 C CA  . TYR B 220  ? 0.5079 0.5059 0.3111 -0.1379 -0.0269 0.1644  218  TYR B CA  
10318 C C   . TYR B 220  ? 0.4877 0.4659 0.2973 -0.1368 -0.0369 0.1587  218  TYR B C   
10319 O O   . TYR B 220  ? 0.5395 0.5024 0.3470 -0.1427 -0.0447 0.1643  218  TYR B O   
10320 C CB  . TYR B 220  ? 0.5235 0.5194 0.3116 -0.1308 -0.0255 0.1622  218  TYR B CB  
10321 C CG  . TYR B 220  ? 0.4998 0.5163 0.2834 -0.1269 -0.0144 0.1618  218  TYR B CG  
10322 C CD1 . TYR B 220  ? 0.5480 0.5768 0.3244 -0.1329 -0.0085 0.1722  218  TYR B CD1 
10323 C CD2 . TYR B 220  ? 0.4825 0.5059 0.2689 -0.1172 -0.0100 0.1511  218  TYR B CD2 
10324 C CE1 . TYR B 220  ? 0.5470 0.5949 0.3191 -0.1287 0.0019  0.1716  218  TYR B CE1 
10325 C CE2 . TYR B 220  ? 0.5162 0.5574 0.2981 -0.1130 -0.0002 0.1503  218  TYR B CE2 
10326 C CZ  . TYR B 220  ? 0.5287 0.5823 0.3034 -0.1185 0.0059  0.1604  218  TYR B CZ  
10327 O OH  . TYR B 220  ? 0.5732 0.6450 0.3434 -0.1136 0.0160  0.1592  218  TYR B OH  
10328 N N   . SER B 221  ? 0.5008 0.4795 0.3180 -0.1287 -0.0364 0.1476  219  SER B N   
10329 C CA  . SER B 221  ? 0.4656 0.4268 0.2875 -0.1248 -0.0448 0.1401  219  SER B CA  
10330 C C   . SER B 221  ? 0.4545 0.4173 0.2747 -0.1138 -0.0427 0.1297  219  SER B C   
10331 O O   . SER B 221  ? 0.4598 0.4367 0.2854 -0.1096 -0.0357 0.1244  219  SER B O   
10332 C CB  . SER B 221  ? 0.5002 0.4613 0.3366 -0.1280 -0.0466 0.1375  219  SER B CB  
10333 O OG  . SER B 221  ? 0.4910 0.4366 0.3318 -0.1231 -0.0538 0.1295  219  SER B OG  
10334 N N   . TYR B 222  ? 0.4835 0.4322 0.2961 -0.1092 -0.0488 0.1269  220  TYR B N   
10335 C CA  . TYR B 222  ? 0.4804 0.4304 0.2894 -0.0995 -0.0471 0.1182  220  TYR B CA  
10336 C C   . TYR B 222  ? 0.4950 0.4379 0.3146 -0.0937 -0.0511 0.1082  220  TYR B C   
10337 O O   . TYR B 222  ? 0.4871 0.4160 0.3109 -0.0951 -0.0587 0.1077  220  TYR B O   
10338 C CB  . TYR B 222  ? 0.4678 0.4076 0.2625 -0.0976 -0.0515 0.1208  220  TYR B CB  
10339 C CG  . TYR B 222  ? 0.4819 0.4302 0.2650 -0.1025 -0.0466 0.1302  220  TYR B CG  
10340 C CD1 . TYR B 222  ? 0.4812 0.4453 0.2591 -0.0989 -0.0377 0.1287  220  TYR B CD1 
10341 C CD2 . TYR B 222  ? 0.4983 0.4393 0.2758 -0.1108 -0.0505 0.1407  220  TYR B CD2 
10342 C CE1 . TYR B 222  ? 0.4927 0.4657 0.2597 -0.1031 -0.0325 0.1373  220  TYR B CE1 
10343 C CE2 . TYR B 222  ? 0.5169 0.4669 0.2838 -0.1157 -0.0455 0.1499  220  TYR B CE2 
10344 C CZ  . TYR B 222  ? 0.5087 0.4751 0.2702 -0.1116 -0.0363 0.1481  220  TYR B CZ  
10345 O OH  . TYR B 222  ? 0.5226 0.4988 0.2732 -0.1160 -0.0307 0.1572  220  TYR B OH  
10346 N N   . ASP B 223  ? 0.4483 0.4008 0.2717 -0.0870 -0.0459 0.1003  221  ASP B N   
10347 C CA  . ASP B 223  ? 0.4982 0.4473 0.3318 -0.0812 -0.0479 0.0906  221  ASP B CA  
10348 C C   . ASP B 223  ? 0.5335 0.4784 0.3610 -0.0732 -0.0495 0.0842  221  ASP B C   
10349 O O   . ASP B 223  ? 0.5107 0.4655 0.3340 -0.0690 -0.0437 0.0814  221  ASP B O   
10350 C CB  . ASP B 223  ? 0.5243 0.4883 0.3677 -0.0805 -0.0406 0.0872  221  ASP B CB  
10351 C CG  . ASP B 223  ? 0.6143 0.5772 0.4667 -0.0737 -0.0413 0.0770  221  ASP B CG  
10352 O OD1 . ASP B 223  ? 0.5961 0.5461 0.4503 -0.0709 -0.0480 0.0730  221  ASP B OD1 
10353 O OD2 . ASP B 223  ? 0.5812 0.5566 0.4392 -0.0711 -0.0349 0.0732  221  ASP B OD2 
10354 N N   . MET B 224  ? 0.5101 0.4403 0.3373 -0.0710 -0.0576 0.0821  222  MET B N   
10355 C CA  . MET B 224  ? 0.5629 0.4881 0.3837 -0.0644 -0.0604 0.0773  222  MET B CA  
10356 C C   . MET B 224  ? 0.5988 0.5288 0.4273 -0.0573 -0.0581 0.0673  222  MET B C   
10357 O O   . MET B 224  ? 0.6966 0.6212 0.5225 -0.0519 -0.0617 0.0626  222  MET B O   
10358 C CB  . MET B 224  ? 0.5398 0.4483 0.3583 -0.0645 -0.0701 0.0788  222  MET B CB  
10359 C CG  . MET B 224  ? 0.5847 0.4870 0.3937 -0.0713 -0.0730 0.0891  222  MET B CG  
10360 S SD  . MET B 224  ? 0.6685 0.5805 0.4613 -0.0724 -0.0670 0.0947  222  MET B SD  
10361 C CE  . MET B 224  ? 0.5450 0.4517 0.3316 -0.0636 -0.0708 0.0872  222  MET B CE  
10362 N N   . LEU B 225  ? 0.5929 0.5333 0.4307 -0.0575 -0.0524 0.0646  223  LEU B N   
10363 C CA  . LEU B 225  ? 0.6554 0.6016 0.5006 -0.0514 -0.0493 0.0559  223  LEU B CA  
10364 C C   . LEU B 225  ? 0.7542 0.6900 0.6044 -0.0467 -0.0559 0.0497  223  LEU B C   
10365 O O   . LEU B 225  ? 0.7602 0.6931 0.6056 -0.0420 -0.0580 0.0461  223  LEU B O   
10366 C CB  . LEU B 225  ? 0.6342 0.5898 0.4716 -0.0476 -0.0435 0.0539  223  LEU B CB  
10367 C CG  . LEU B 225  ? 0.6468 0.6161 0.4832 -0.0512 -0.0355 0.0586  223  LEU B CG  
10368 C CD1 . LEU B 225  ? 0.6592 0.6381 0.4876 -0.0468 -0.0292 0.0564  223  LEU B CD1 
10369 C CD2 . LEU B 225  ? 0.5973 0.5732 0.4471 -0.0531 -0.0326 0.0570  223  LEU B CD2 
10370 N N   . GLY B 226  ? 0.7257 0.6559 0.5855 -0.0481 -0.0594 0.0485  224  GLY B N   
10371 C CA  . GLY B 226  ? 0.6459 0.5685 0.5132 -0.0436 -0.0645 0.0423  224  GLY B CA  
10372 C C   . GLY B 226  ? 0.6350 0.5581 0.5137 -0.0451 -0.0641 0.0403  224  GLY B C   
10373 O O   . GLY B 226  ? 0.6393 0.5617 0.5184 -0.0508 -0.0639 0.0454  224  GLY B O   
10374 N N   . GLU B 227  ? 0.6558 0.5804 0.5434 -0.0404 -0.0638 0.0331  225  GLU B N   
10375 C CA  . GLU B 227  ? 0.6094 0.5336 0.5071 -0.0413 -0.0638 0.0305  225  GLU B CA  
10376 C C   . GLU B 227  ? 0.5762 0.5004 0.4819 -0.0351 -0.0646 0.0227  225  GLU B C   
10377 O O   . GLU B 227  ? 0.6290 0.5561 0.5332 -0.0309 -0.0638 0.0193  225  GLU B O   
10378 C CB  . GLU B 227  ? 0.6045 0.5398 0.5051 -0.0449 -0.0573 0.0321  225  GLU B CB  
10379 C CG  . GLU B 227  ? 0.6289 0.5763 0.5293 -0.0417 -0.0507 0.0290  225  GLU B CG  
10380 C CD  . GLU B 227  ? 0.6893 0.6482 0.5922 -0.0454 -0.0444 0.0315  225  GLU B CD  
10381 O OE1 . GLU B 227  ? 0.6786 0.6386 0.5894 -0.0471 -0.0442 0.0302  225  GLU B OE1 
10382 O OE2 . GLU B 227  ? 0.7297 0.6966 0.6266 -0.0464 -0.0398 0.0348  225  GLU B OE2 
10383 N N   . ALA B 228  ? 0.5398 0.4607 0.4537 -0.0349 -0.0662 0.0198  226  ALA B N   
10384 C CA  . ALA B 228  ? 0.4890 0.4109 0.4115 -0.0295 -0.0665 0.0127  226  ALA B CA  
10385 C C   . ALA B 228  ? 0.5349 0.4522 0.4562 -0.0247 -0.0706 0.0103  226  ALA B C   
10386 O O   . ALA B 228  ? 0.5296 0.4526 0.4519 -0.0212 -0.0684 0.0067  226  ALA B O   
10387 C CB  . ALA B 228  ? 0.4653 0.3992 0.3922 -0.0282 -0.0597 0.0093  226  ALA B CB  
10388 N N   . ALA B 229  ? 0.4772 0.3835 0.3961 -0.0248 -0.0771 0.0125  227  ALA B N   
10389 C CA  . ALA B 229  ? 0.4766 0.3779 0.3965 -0.0200 -0.0822 0.0100  227  ALA B CA  
10390 C C   . ALA B 229  ? 0.4423 0.3475 0.3731 -0.0150 -0.0812 0.0030  227  ALA B C   
10391 O O   . ALA B 229  ? 0.4684 0.3728 0.4058 -0.0147 -0.0807 0.0007  227  ALA B O   
10392 C CB  . ALA B 229  ? 0.3884 0.2770 0.3057 -0.0207 -0.0894 0.0133  227  ALA B CB  
10393 N N   . THR B 230  ? 0.4340 0.3437 0.3662 -0.0114 -0.0809 -0.0002 228  THR B N   
10394 C CA  . THR B 230  ? 0.4589 0.3727 0.4014 -0.0068 -0.0803 -0.0062 228  THR B CA  
10395 C C   . THR B 230  ? 0.4577 0.3649 0.4049 -0.0028 -0.0869 -0.0078 228  THR B C   
10396 O O   . THR B 230  ? 0.4298 0.3380 0.3864 0.0004  -0.0871 -0.0118 228  THR B O   
10397 C CB  . THR B 230  ? 0.4787 0.4009 0.4211 -0.0052 -0.0768 -0.0088 228  THR B CB  
10398 O OG1 . THR B 230  ? 0.5017 0.4301 0.4398 -0.0084 -0.0707 -0.0072 228  THR B OG1 
10399 C CG2 . THR B 230  ? 0.4161 0.3436 0.3696 -0.0014 -0.0755 -0.0144 228  THR B CG2 
10400 N N   . THR B 231  ? 0.3778 0.2786 0.3186 -0.0027 -0.0922 -0.0047 229  THR B N   
10401 C CA  . THR B 231  ? 0.4202 0.3152 0.3654 0.0014  -0.0989 -0.0059 229  THR B CA  
10402 C C   . THR B 231  ? 0.4390 0.3224 0.3778 -0.0003 -0.1046 -0.0009 229  THR B C   
10403 O O   . THR B 231  ? 0.3912 0.2715 0.3208 -0.0051 -0.1037 0.0040  229  THR B O   
10404 C CB  . THR B 231  ? 0.4372 0.3350 0.3814 0.0037  -0.1014 -0.0069 229  THR B CB  
10405 O OG1 . THR B 231  ? 0.4541 0.3478 0.3857 0.0008  -0.1032 -0.0021 229  THR B OG1 
10406 C CG2 . THR B 231  ? 0.4300 0.3384 0.3789 0.0046  -0.0958 -0.0112 229  THR B CG2 
10407 N N   . ALA B 232  ? 0.3901 0.2673 0.3341 0.0038  -0.1108 -0.0021 230  ALA B N   
10408 C CA  . ALA B 232  ? 0.4545 0.3195 0.3923 0.0028  -0.1173 0.0027  230  ALA B CA  
10409 C C   . ALA B 232  ? 0.4320 0.2944 0.3578 -0.0002 -0.1195 0.0079  230  ALA B C   
10410 O O   . ALA B 232  ? 0.4586 0.3134 0.3755 -0.0042 -0.1216 0.0136  230  ALA B O   
10411 C CB  . ALA B 232  ? 0.4582 0.3179 0.4040 0.0087  -0.1237 0.0002  230  ALA B CB  
10412 N N   . ALA B 233  ? 0.4423 0.3110 0.3675 0.0015  -0.1193 0.0062  231  ALA B N   
10413 C CA  . ALA B 233  ? 0.4720 0.3381 0.3850 -0.0007 -0.1217 0.0107  231  ALA B CA  
10414 C C   . ALA B 233  ? 0.4806 0.3496 0.3836 -0.0063 -0.1158 0.0144  231  ALA B C   
10415 O O   . ALA B 233  ? 0.4904 0.3541 0.3819 -0.0096 -0.1178 0.0202  231  ALA B O   
10416 C CB  . ALA B 233  ? 0.4601 0.3319 0.3746 0.0025  -0.1230 0.0073  231  ALA B CB  
10417 N N   . ASP B 234  ? 0.4137 0.2917 0.3210 -0.0073 -0.1083 0.0114  232  ASP B N   
10418 C CA  . ASP B 234  ? 0.4559 0.3378 0.3557 -0.0123 -0.1023 0.0149  232  ASP B CA  
10419 C C   . ASP B 234  ? 0.4805 0.3544 0.3761 -0.0166 -0.1042 0.0206  232  ASP B C   
10420 O O   . ASP B 234  ? 0.4787 0.3510 0.3636 -0.0210 -0.1036 0.0265  232  ASP B O   
10421 C CB  . ASP B 234  ? 0.4275 0.3194 0.3347 -0.0122 -0.0949 0.0106  232  ASP B CB  
10422 C CG  . ASP B 234  ? 0.5125 0.4125 0.4226 -0.0089 -0.0922 0.0056  232  ASP B CG  
10423 O OD1 . ASP B 234  ? 0.5183 0.4174 0.4221 -0.0077 -0.0948 0.0059  232  ASP B OD1 
10424 O OD2 . ASP B 234  ? 0.5402 0.4473 0.4584 -0.0078 -0.0875 0.0014  232  ASP B OD2 
10425 N N   . ALA B 235  ? 0.4407 0.3095 0.3444 -0.0156 -0.1065 0.0190  233  ALA B N   
10426 C CA  . ALA B 235  ? 0.4444 0.3049 0.3449 -0.0200 -0.1086 0.0240  233  ALA B CA  
10427 C C   . ALA B 235  ? 0.4657 0.3151 0.3572 -0.0212 -0.1156 0.0299  233  ALA B C   
10428 O O   . ALA B 235  ? 0.4168 0.2617 0.3001 -0.0268 -0.1159 0.0365  233  ALA B O   
10429 C CB  . ALA B 235  ? 0.4609 0.3172 0.3716 -0.0177 -0.1102 0.0200  233  ALA B CB  
10430 N N   . GLU B 236  ? 0.4379 0.2832 0.3307 -0.0163 -0.1214 0.0281  234  GLU B N   
10431 C CA  . GLU B 236  ? 0.4898 0.3246 0.3737 -0.0172 -0.1286 0.0339  234  GLU B CA  
10432 C C   . GLU B 236  ? 0.4531 0.2912 0.3237 -0.0213 -0.1262 0.0390  234  GLU B C   
10433 O O   . GLU B 236  ? 0.4943 0.3249 0.3551 -0.0254 -0.1291 0.0462  234  GLU B O   
10434 C CB  . GLU B 236  ? 0.4943 0.3254 0.3833 -0.0108 -0.1353 0.0305  234  GLU B CB  
10435 C CG  . GLU B 236  ? 0.5000 0.3179 0.3824 -0.0108 -0.1441 0.0361  234  GLU B CG  
10436 C CD  . GLU B 236  ? 0.6579 0.4730 0.5469 -0.0040 -0.1509 0.0326  234  GLU B CD  
10437 O OE1 . GLU B 236  ? 0.6032 0.4268 0.5028 0.0004  -0.1487 0.0260  234  GLU B OE1 
10438 O OE2 . GLU B 236  ? 0.6241 0.4287 0.5080 -0.0033 -0.1587 0.0369  234  GLU B OE2 
10439 N N   . ARG B 237  ? 0.4544 0.3035 0.3244 -0.0201 -0.1208 0.0357  235  ARG B N   
10440 C CA  . ARG B 237  ? 0.5001 0.3530 0.3571 -0.0233 -0.1178 0.0399  235  ARG B CA  
10441 C C   . ARG B 237  ? 0.4770 0.3327 0.3290 -0.0297 -0.1122 0.0452  235  ARG B C   
10442 O O   . ARG B 237  ? 0.4625 0.3152 0.3029 -0.0338 -0.1128 0.0521  235  ARG B O   
10443 C CB  . ARG B 237  ? 0.5355 0.3988 0.3933 -0.0201 -0.1133 0.0343  235  ARG B CB  
10444 C CG  . ARG B 237  ? 0.5560 0.4258 0.4021 -0.0233 -0.1075 0.0374  235  ARG B CG  
10445 C CD  . ARG B 237  ? 0.6002 0.4781 0.4456 -0.0198 -0.1042 0.0320  235  ARG B CD  
10446 N NE  . ARG B 237  ? 0.6655 0.5455 0.4960 -0.0217 -0.1019 0.0356  235  ARG B NE  
10447 C CZ  . ARG B 237  ? 0.6634 0.5492 0.4891 -0.0191 -0.0991 0.0318  235  ARG B CZ  
10448 N NH1 . ARG B 237  ? 0.6337 0.5236 0.4685 -0.0151 -0.0984 0.0247  235  ARG B NH1 
10449 N NH2 . ARG B 237  ? 0.6195 0.5066 0.4305 -0.0206 -0.0970 0.0354  235  ARG B NH2 
10450 N N   . TYR B 238  ? 0.4603 0.3221 0.3212 -0.0308 -0.1068 0.0423  236  TYR B N   
10451 C CA  . TYR B 238  ? 0.4811 0.3462 0.3389 -0.0371 -0.1020 0.0474  236  TYR B CA  
10452 C C   . TYR B 238  ? 0.4578 0.3108 0.3108 -0.0417 -0.1076 0.0546  236  TYR B C   
10453 O O   . TYR B 238  ? 0.4245 0.2780 0.2686 -0.0475 -0.1058 0.0617  236  TYR B O   
10454 C CB  . TYR B 238  ? 0.4459 0.3180 0.3148 -0.0373 -0.0967 0.0428  236  TYR B CB  
10455 C CG  . TYR B 238  ? 0.4921 0.3771 0.3644 -0.0343 -0.0898 0.0373  236  TYR B CG  
10456 C CD1 . TYR B 238  ? 0.5523 0.4445 0.4156 -0.0347 -0.0856 0.0389  236  TYR B CD1 
10457 C CD2 . TYR B 238  ? 0.4607 0.3501 0.3445 -0.0307 -0.0878 0.0304  236  TYR B CD2 
10458 C CE1 . TYR B 238  ? 0.6407 0.5434 0.5067 -0.0316 -0.0798 0.0336  236  TYR B CE1 
10459 C CE2 . TYR B 238  ? 0.5586 0.4588 0.4454 -0.0280 -0.0820 0.0256  236  TYR B CE2 
10460 C CZ  . TYR B 238  ? 0.6421 0.5485 0.5200 -0.0284 -0.0782 0.0271  236  TYR B CZ  
10461 O OH  . TYR B 238  ? 0.6295 0.5455 0.5100 -0.0255 -0.0729 0.0222  236  TYR B OH  
10462 N N   . TYR B 239  ? 0.4523 0.2942 0.3107 -0.0390 -0.1147 0.0530  237  TYR B N   
10463 C CA  . TYR B 239  ? 0.4530 0.2818 0.3066 -0.0430 -0.1209 0.0597  237  TYR B CA  
10464 C C   . TYR B 239  ? 0.5150 0.3393 0.3552 -0.0449 -0.1243 0.0665  237  TYR B C   
10465 O O   . TYR B 239  ? 0.4626 0.2826 0.2945 -0.0513 -0.1249 0.0746  237  TYR B O   
10466 C CB  . TYR B 239  ? 0.4598 0.2772 0.3215 -0.0384 -0.1282 0.0560  237  TYR B CB  
10467 C CG  . TYR B 239  ? 0.5288 0.3307 0.3847 -0.0414 -0.1359 0.0627  237  TYR B CG  
10468 C CD1 . TYR B 239  ? 0.5088 0.3043 0.3652 -0.0470 -0.1365 0.0665  237  TYR B CD1 
10469 C CD2 . TYR B 239  ? 0.5631 0.3563 0.4127 -0.0390 -0.1431 0.0657  237  TYR B CD2 
10470 C CE1 . TYR B 239  ? 0.5221 0.3024 0.3729 -0.0501 -0.1440 0.0729  237  TYR B CE1 
10471 C CE2 . TYR B 239  ? 0.5682 0.3465 0.4121 -0.0418 -0.1504 0.0722  237  TYR B CE2 
10472 C CZ  . TYR B 239  ? 0.5516 0.3232 0.3961 -0.0473 -0.1508 0.0758  237  TYR B CZ  
10473 O OH  . TYR B 239  ? 0.6617 0.4174 0.5005 -0.0503 -0.1586 0.0825  237  TYR B OH  
10474 N N   . ARG B 240  ? 0.4898 0.3150 0.3275 -0.0397 -0.1267 0.0636  238  ARG B N   
10475 C CA  . ARG B 240  ? 0.4993 0.3200 0.3234 -0.0411 -0.1303 0.0696  238  ARG B CA  
10476 C C   . ARG B 240  ? 0.4890 0.3193 0.3026 -0.0460 -0.1230 0.0742  238  ARG B C   
10477 O O   . ARG B 240  ? 0.5015 0.3274 0.3030 -0.0502 -0.1248 0.0820  238  ARG B O   
10478 C CB  . ARG B 240  ? 0.5331 0.3534 0.3575 -0.0344 -0.1346 0.0648  238  ARG B CB  
10479 C CG  . ARG B 240  ? 0.5662 0.3768 0.4000 -0.0295 -0.1426 0.0615  238  ARG B CG  
10480 C CD  . ARG B 240  ? 0.5408 0.3365 0.3685 -0.0321 -0.1504 0.0689  238  ARG B CD  
10481 N NE  . ARG B 240  ? 0.6089 0.3953 0.4464 -0.0269 -0.1577 0.0655  238  ARG B NE  
10482 C CZ  . ARG B 240  ? 0.6866 0.4587 0.5218 -0.0277 -0.1653 0.0703  238  ARG B CZ  
10483 N NH1 . ARG B 240  ? 0.6722 0.4371 0.4956 -0.0341 -0.1670 0.0792  238  ARG B NH1 
10484 N NH2 . ARG B 240  ? 0.6917 0.4566 0.5367 -0.0219 -0.1714 0.0662  238  ARG B NH2 
10485 N N   . ASP B 241  ? 0.4878 0.3313 0.3058 -0.0453 -0.1147 0.0696  239  ASP B N   
10486 C CA  . ASP B 241  ? 0.5221 0.3759 0.3315 -0.0495 -0.1070 0.0736  239  ASP B CA  
10487 C C   . ASP B 241  ? 0.4976 0.3505 0.3056 -0.0573 -0.1051 0.0812  239  ASP B C   
10488 O O   . ASP B 241  ? 0.4812 0.3367 0.2781 -0.0621 -0.1026 0.0885  239  ASP B O   
10489 C CB  . ASP B 241  ? 0.5070 0.3745 0.3228 -0.0465 -0.0991 0.0665  239  ASP B CB  
10490 C CG  . ASP B 241  ? 0.5733 0.4431 0.3871 -0.0401 -0.1001 0.0603  239  ASP B CG  
10491 O OD1 . ASP B 241  ? 0.6352 0.4973 0.4412 -0.0384 -0.1065 0.0620  239  ASP B OD1 
10492 O OD2 . ASP B 241  ? 0.6029 0.4819 0.4230 -0.0369 -0.0950 0.0538  239  ASP B OD2 
10493 N N   . TYR B 242  ? 0.4996 0.3491 0.3184 -0.0588 -0.1061 0.0798  240  TYR B N   
10494 C CA  . TYR B 242  ? 0.4801 0.3272 0.2980 -0.0667 -0.1055 0.0873  240  TYR B CA  
10495 C C   . TYR B 242  ? 0.4955 0.3291 0.3036 -0.0705 -0.1129 0.0957  240  TYR B C   
10496 O O   . TYR B 242  ? 0.4945 0.3293 0.2945 -0.0774 -0.1110 0.1044  240  TYR B O   
10497 C CB  . TYR B 242  ? 0.4540 0.2980 0.2849 -0.0669 -0.1066 0.0833  240  TYR B CB  
10498 C CG  . TYR B 242  ? 0.4599 0.3176 0.3001 -0.0658 -0.0988 0.0773  240  TYR B CG  
10499 C CD1 . TYR B 242  ? 0.4959 0.3680 0.3330 -0.0686 -0.0904 0.0794  240  TYR B CD1 
10500 C CD2 . TYR B 242  ? 0.4298 0.2857 0.2819 -0.0619 -0.0999 0.0699  240  TYR B CD2 
10501 C CE1 . TYR B 242  ? 0.5008 0.3850 0.3469 -0.0674 -0.0836 0.0741  240  TYR B CE1 
10502 C CE2 . TYR B 242  ? 0.4748 0.3425 0.3351 -0.0609 -0.0932 0.0648  240  TYR B CE2 
10503 C CZ  . TYR B 242  ? 0.4648 0.3464 0.3223 -0.0637 -0.0853 0.0669  240  TYR B CZ  
10504 O OH  . TYR B 242  ? 0.4674 0.3602 0.3334 -0.0625 -0.0792 0.0619  240  TYR B OH  
10505 N N   . GLU B 243  ? 0.4887 0.3095 0.2977 -0.0659 -0.1213 0.0936  241  GLU B N   
10506 C CA  . GLU B 243  ? 0.5087 0.3152 0.3085 -0.0687 -0.1293 0.1013  241  GLU B CA  
10507 C C   . GLU B 243  ? 0.5277 0.3381 0.3124 -0.0710 -0.1275 0.1076  241  GLU B C   
10508 O O   . GLU B 243  ? 0.5362 0.3415 0.3116 -0.0776 -0.1291 0.1172  241  GLU B O   
10509 C CB  . GLU B 243  ? 0.5180 0.3126 0.3223 -0.0617 -0.1381 0.0966  241  GLU B CB  
10510 C CG  . GLU B 243  ? 0.5952 0.3733 0.3915 -0.0637 -0.1474 0.1039  241  GLU B CG  
10511 C CD  . GLU B 243  ? 0.6151 0.3847 0.4140 -0.0558 -0.1555 0.0994  241  GLU B CD  
10512 O OE1 . GLU B 243  ? 0.6002 0.3781 0.4035 -0.0496 -0.1534 0.0919  241  GLU B OE1 
10513 O OE2 . GLU B 243  ? 0.6901 0.4446 0.4871 -0.0559 -0.1642 0.1033  241  GLU B OE2 
10514 N N   . SER B 244  ? 0.5133 0.3324 0.2950 -0.0657 -0.1243 0.1025  242  SER B N   
10515 C CA  . SER B 244  ? 0.5243 0.3478 0.2908 -0.0672 -0.1220 0.1076  242  SER B CA  
10516 C C   . SER B 244  ? 0.5265 0.3608 0.2879 -0.0742 -0.1135 0.1139  242  SER B C   
10517 O O   . SER B 244  ? 0.5426 0.3754 0.2913 -0.0792 -0.1136 0.1228  242  SER B O   
10518 C CB  . SER B 244  ? 0.5153 0.3463 0.2807 -0.0601 -0.1198 0.0996  242  SER B CB  
10519 O OG  . SER B 244  ? 0.6109 0.4446 0.3603 -0.0609 -0.1185 0.1040  242  SER B OG  
10520 N N   . ALA B 245  ? 0.5108 0.3567 0.2821 -0.0748 -0.1061 0.1098  243  ALA B N   
10521 C CA  . ALA B 245  ? 0.5190 0.3771 0.2870 -0.0810 -0.0977 0.1154  243  ALA B CA  
10522 C C   . ALA B 245  ? 0.5246 0.3756 0.2912 -0.0898 -0.1005 0.1254  243  ALA B C   
10523 O O   . ALA B 245  ? 0.5352 0.3920 0.2929 -0.0959 -0.0965 0.1339  243  ALA B O   
10524 C CB  . ALA B 245  ? 0.5076 0.3791 0.2877 -0.0792 -0.0900 0.1085  243  ALA B CB  
10525 N N   . ILE B 246  ? 0.5249 0.3631 0.3001 -0.0906 -0.1075 0.1246  244  ILE B N   
10526 C CA  . ILE B 246  ? 0.5482 0.3775 0.3219 -0.0991 -0.1113 0.1339  244  ILE B CA  
10527 C C   . ILE B 246  ? 0.5602 0.3811 0.3188 -0.1024 -0.1158 0.1433  244  ILE B C   
10528 O O   . ILE B 246  ? 0.5776 0.3992 0.3299 -0.1108 -0.1144 0.1534  244  ILE B O   
10529 C CB  . ILE B 246  ? 0.5365 0.3518 0.3212 -0.0981 -0.1188 0.1302  244  ILE B CB  
10530 C CG1 . ILE B 246  ? 0.5381 0.3626 0.3366 -0.0968 -0.1136 0.1228  244  ILE B CG1 
10531 C CG2 . ILE B 246  ? 0.5591 0.3609 0.3403 -0.1064 -0.1249 0.1401  244  ILE B CG2 
10532 C CD1 . ILE B 246  ? 0.5150 0.3264 0.3239 -0.0950 -0.1203 0.1181  244  ILE B CD1 
10533 N N   . HIS B 247  ? 0.5652 0.3786 0.3175 -0.0962 -0.1212 0.1406  245  HIS B N   
10534 C CA  . HIS B 247  ? 0.5862 0.3919 0.3229 -0.0989 -0.1256 0.1494  245  HIS B CA  
10535 C C   . HIS B 247  ? 0.5911 0.4113 0.3162 -0.1026 -0.1168 0.1550  245  HIS B C   
10536 O O   . HIS B 247  ? 0.6085 0.4262 0.3230 -0.1096 -0.1173 0.1657  245  HIS B O   
10537 C CB  . HIS B 247  ? 0.5894 0.3861 0.3219 -0.0910 -0.1328 0.1446  245  HIS B CB  
10538 C CG  . HIS B 247  ? 0.5927 0.3722 0.3326 -0.0883 -0.1431 0.1427  245  HIS B CG  
10539 N ND1 . HIS B 247  ? 0.6218 0.3860 0.3575 -0.0935 -0.1507 0.1513  245  HIS B ND1 
10540 C CD2 . HIS B 247  ? 0.5920 0.3675 0.3435 -0.0808 -0.1470 0.1332  245  HIS B CD2 
10541 C CE1 . HIS B 247  ? 0.6701 0.4211 0.4141 -0.0888 -0.1589 0.1468  245  HIS B CE1 
10542 N NE2 . HIS B 247  ? 0.6451 0.4032 0.3989 -0.0810 -0.1567 0.1358  245  HIS B NE2 
10543 N N   . ALA B 248  ? 0.5768 0.4122 0.3036 -0.0979 -0.1088 0.1479  246  ALA B N   
10544 C CA  . ALA B 248  ? 0.5812 0.4313 0.2972 -0.1003 -0.0999 0.1522  246  ALA B CA  
10545 C C   . ALA B 248  ? 0.5819 0.4413 0.3015 -0.1091 -0.0935 0.1596  246  ALA B C   
10546 O O   . ALA B 248  ? 0.5967 0.4600 0.3052 -0.1153 -0.0906 0.1695  246  ALA B O   
10547 C CB  . ALA B 248  ? 0.5655 0.4286 0.2836 -0.0926 -0.0931 0.1421  246  ALA B CB  
10548 N N   . ILE B 249  ? 0.5664 0.4300 0.3013 -0.1098 -0.0912 0.1552  247  ILE B N   
10549 C CA  . ILE B 249  ? 0.5809 0.4545 0.3210 -0.1181 -0.0853 0.1616  247  ILE B CA  
10550 C C   . ILE B 249  ? 0.5844 0.4460 0.3201 -0.1273 -0.0914 0.1731  247  ILE B C   
10551 O O   . ILE B 249  ? 0.6354 0.5048 0.3653 -0.1351 -0.0869 0.1829  247  ILE B O   
10552 C CB  . ILE B 249  ? 0.5459 0.4240 0.3033 -0.1167 -0.0833 0.1539  247  ILE B CB  
10553 C CG1 . ILE B 249  ? 0.5281 0.4199 0.2894 -0.1085 -0.0762 0.1437  247  ILE B CG1 
10554 C CG2 . ILE B 249  ? 0.5540 0.4397 0.3177 -0.1263 -0.0794 0.1612  247  ILE B CG2 
10555 C CD1 . ILE B 249  ? 0.5093 0.4009 0.2863 -0.1045 -0.0768 0.1341  247  ILE B CD1 
10556 N N   . GLY B 250  ? 0.6013 0.4437 0.3396 -0.1265 -0.1018 0.1722  248  GLY B N   
10557 C CA  . GLY B 250  ? 0.6090 0.4375 0.3430 -0.1348 -0.1088 0.1828  248  GLY B CA  
10558 C C   . GLY B 250  ? 0.6369 0.4646 0.3536 -0.1387 -0.1089 0.1932  248  GLY B C   
10559 O O   . GLY B 250  ? 0.6764 0.5054 0.3916 -0.1470 -0.1077 0.2023  248  GLY B O   
10560 N N   . LYS B 251  ? 0.6317 0.4592 0.3383 -0.1316 -0.1094 0.1897  249  LYS B N   
10561 C CA  . LYS B 251  ? 0.6498 0.4791 0.3420 -0.1336 -0.1081 0.1970  249  LYS B CA  
10562 C C   . LYS B 251  ? 0.6489 0.4997 0.3382 -0.1374 -0.0958 0.2008  249  LYS B C   
10563 O O   . LYS B 251  ? 0.6639 0.5186 0.3480 -0.1425 -0.0930 0.2086  249  LYS B O   
10564 C CB  . LYS B 251  ? 0.6656 0.4894 0.3474 -0.1249 -0.1120 0.1918  249  LYS B CB  
10565 N N   . ALA B 252  ? 0.6377 0.5028 0.3302 -0.1344 -0.0883 0.1954  250  ALA B N   
10566 C CA  . ALA B 252  ? 0.6476 0.5342 0.3397 -0.1374 -0.0762 0.1984  250  ALA B CA  
10567 C C   . ALA B 252  ? 0.6639 0.5552 0.3663 -0.1470 -0.0740 0.2057  250  ALA B C   
10568 O O   . ALA B 252  ? 0.6489 0.5522 0.3487 -0.1515 -0.0672 0.2123  250  ALA B O   
10569 C CB  . ALA B 252  ? 0.6603 0.5610 0.3585 -0.1309 -0.0689 0.1886  250  ALA B CB  
10570 N N   . SER B 253  ? 0.6601 0.5418 0.3743 -0.1502 -0.0798 0.2046  251  SER B N   
10571 C CA  . SER B 253  ? 0.6506 0.5352 0.3752 -0.1595 -0.0789 0.2109  251  SER B CA  
10572 C C   . SER B 253  ? 0.6717 0.5514 0.3908 -0.1656 -0.0812 0.2200  251  SER B C   
10573 O O   . SER B 253  ? 0.6900 0.5811 0.4133 -0.1728 -0.0760 0.2266  251  SER B O   
10574 C CB  . SER B 253  ? 0.6247 0.4945 0.3605 -0.1610 -0.0872 0.2077  251  SER B CB  
10575 O OG  . SER B 253  ? 0.6484 0.5193 0.3938 -0.1702 -0.0875 0.2134  251  SER B OG  
10576 N N   . ALA B 254  ? 0.6877 0.5506 0.3978 -0.1627 -0.0894 0.2206  252  ALA B N   
10577 C CA  . ALA B 254  ? 0.7447 0.6016 0.4478 -0.1676 -0.0921 0.2291  252  ALA B CA  
10578 C C   . ALA B 254  ? 0.7360 0.5896 0.4488 -0.1776 -0.0947 0.2358  252  ALA B C   
10579 O O   . ALA B 254  ? 0.7278 0.5886 0.4384 -0.1840 -0.0912 0.2439  252  ALA B O   
10580 C CB  . ALA B 254  ? 0.7541 0.6275 0.4463 -0.1669 -0.0826 0.2330  252  ALA B CB  
10581 N N   . GLY B 255  ? 0.7548 0.5973 0.4783 -0.1786 -0.1012 0.2320  253  GLY B N   
10582 C CA  . GLY B 255  ? 0.7415 0.5775 0.4741 -0.1874 -0.1056 0.2370  253  GLY B CA  
10583 C C   . GLY B 255  ? 0.7288 0.5838 0.4708 -0.1945 -0.0973 0.2405  253  GLY B C   
10584 O O   . GLY B 255  ? 0.7565 0.6088 0.5046 -0.2028 -0.1000 0.2461  253  GLY B O   
10585 N N   . ARG B 256  ? 0.7056 0.5801 0.4492 -0.1911 -0.0873 0.2370  254  ARG B N   
10586 C CA  . ARG B 256  ? 0.7013 0.5956 0.4551 -0.1969 -0.0791 0.2396  254  ARG B CA  
10587 C C   . ARG B 256  ? 0.7023 0.5913 0.4701 -0.2006 -0.0835 0.2365  254  ARG B C   
10588 O O   . ARG B 256  ? 0.6892 0.5923 0.4668 -0.2067 -0.0786 0.2393  254  ARG B O   
10589 C CB  . ARG B 256  ? 0.6469 0.5627 0.3987 -0.1910 -0.0676 0.2356  254  ARG B CB  
10590 C CG  . ARG B 256  ? 0.6608 0.5882 0.4006 -0.1894 -0.0604 0.2401  254  ARG B CG  
10591 C CD  . ARG B 256  ? 0.6920 0.6398 0.4305 -0.1827 -0.0494 0.2350  254  ARG B CD  
10592 N NE  . ARG B 256  ? 0.6715 0.6114 0.4032 -0.1734 -0.0518 0.2264  254  ARG B NE  
10593 C CZ  . ARG B 256  ? 0.6825 0.6357 0.4131 -0.1664 -0.0445 0.2198  254  ARG B CZ  
10594 N NH1 . ARG B 256  ? 0.6555 0.6306 0.3925 -0.1672 -0.0341 0.2201  254  ARG B NH1 
10595 N NH2 . ARG B 256  ? 0.6713 0.6156 0.3946 -0.1583 -0.0479 0.2124  254  ARG B NH2 
10596 N N   . GLY B 257  ? 0.7044 0.5739 0.4734 -0.1968 -0.0925 0.2306  255  GLY B N   
10597 C CA  . GLY B 257  ? 0.6604 0.5221 0.4414 -0.1999 -0.0977 0.2273  255  GLY B CA  
10598 C C   . GLY B 257  ? 0.6630 0.5368 0.4516 -0.1961 -0.0918 0.2203  255  GLY B C   
10599 O O   . GLY B 257  ? 0.6511 0.5417 0.4366 -0.1916 -0.0830 0.2184  255  GLY B O   
10600 N N   . ILE B 258  ? 0.6479 0.5129 0.4465 -0.1979 -0.0970 0.2163  256  ILE B N   
10601 C CA  . ILE B 258  ? 0.6526 0.5242 0.4577 -0.1933 -0.0935 0.2087  256  ILE B CA  
10602 C C   . ILE B 258  ? 0.6281 0.5251 0.4416 -0.1967 -0.0832 0.2100  256  ILE B C   
10603 O O   . ILE B 258  ? 0.6053 0.5122 0.4251 -0.1907 -0.0783 0.2018  256  ILE B O   
10604 C CB  . ILE B 258  ? 0.6399 0.4935 0.4531 -0.1933 -0.1024 0.2031  256  ILE B CB  
10605 C CG1 . ILE B 258  ? 0.6604 0.5125 0.4822 -0.2030 -0.1057 0.2077  256  ILE B CG1 
10606 C CG2 . ILE B 258  ? 0.6401 0.4698 0.4468 -0.1872 -0.1123 0.1993  256  ILE B CG2 
10607 C CD1 . ILE B 258  ? 0.6278 0.4622 0.4568 -0.2027 -0.1144 0.2016  256  ILE B CD1 
10608 N N   . TYR B 259  ? 0.6337 0.5432 0.4499 -0.2041 -0.0792 0.2175  257  TYR B N   
10609 C CA  . TYR B 259  ? 0.5935 0.5284 0.4186 -0.2066 -0.0692 0.2187  257  TYR B CA  
10610 C C   . TYR B 259  ? 0.6262 0.5804 0.4440 -0.2029 -0.0588 0.2210  257  TYR B C   
10611 O O   . TYR B 259  ? 0.6191 0.5909 0.4400 -0.1985 -0.0503 0.2170  257  TYR B O   
10612 C CB  . TYR B 259  ? 0.6283 0.5672 0.4632 -0.2168 -0.0711 0.2249  257  TYR B CB  
10613 C CG  . TYR B 259  ? 0.6199 0.5386 0.4609 -0.2203 -0.0819 0.2222  257  TYR B CG  
10614 C CD1 . TYR B 259  ? 0.6303 0.5475 0.4795 -0.2178 -0.0830 0.2148  257  TYR B CD1 
10615 C CD2 . TYR B 259  ? 0.6246 0.5255 0.4629 -0.2256 -0.0910 0.2267  257  TYR B CD2 
10616 C CE1 . TYR B 259  ? 0.5946 0.4928 0.4488 -0.2201 -0.0927 0.2115  257  TYR B CE1 
10617 C CE2 . TYR B 259  ? 0.6594 0.5412 0.5027 -0.2278 -0.1009 0.2234  257  TYR B CE2 
10618 C CZ  . TYR B 259  ? 0.6483 0.5288 0.4993 -0.2248 -0.1017 0.2156  257  TYR B CZ  
10619 O OH  . TYR B 259  ? 0.6760 0.5373 0.5314 -0.2263 -0.1114 0.2115  257  TYR B OH  
10620 N N   . GLU B 260  ? 0.6042 0.5553 0.4120 -0.2042 -0.0592 0.2270  258  GLU B N   
10621 C CA  . GLU B 260  ? 0.6620 0.6300 0.4616 -0.1999 -0.0495 0.2285  258  GLU B CA  
10622 C C   . GLU B 260  ? 0.6696 0.6308 0.4576 -0.1899 -0.0496 0.2220  258  GLU B C   
10623 O O   . GLU B 260  ? 0.6701 0.6469 0.4546 -0.1838 -0.0409 0.2186  258  GLU B O   
10624 C CB  . GLU B 260  ? 0.6143 0.5826 0.4073 -0.2053 -0.0494 0.2377  258  GLU B CB  
10625 N N   . GLY B 261  ? 0.6918 0.6298 0.4743 -0.1878 -0.0597 0.2197  259  GLY B N   
10626 C CA  . GLY B 261  ? 0.6636 0.5936 0.4347 -0.1787 -0.0612 0.2141  259  GLY B CA  
10627 C C   . GLY B 261  ? 0.6359 0.5676 0.4127 -0.1714 -0.0601 0.2038  259  GLY B C   
10628 O O   . GLY B 261  ? 0.6098 0.5464 0.4004 -0.1728 -0.0592 0.1998  259  GLY B O   
10629 N N   . PRO B 262  ? 0.6029 0.5319 0.3728 -0.1612 -0.0599 0.1959  260  PRO B N   
10630 C CA  . PRO B 262  ? 0.5559 0.4879 0.3345 -0.1514 -0.0582 0.1824  260  PRO B CA  
10631 C C   . PRO B 262  ? 0.5420 0.4545 0.3279 -0.1488 -0.0681 0.1759  260  PRO B C   
10632 O O   . PRO B 262  ? 0.6197 0.5140 0.4012 -0.1521 -0.0770 0.1803  260  PRO B O   
10633 C CB  . PRO B 262  ? 0.5660 0.5013 0.3329 -0.1424 -0.0549 0.1778  260  PRO B CB  
10634 C CG  . PRO B 262  ? 0.5671 0.4904 0.3194 -0.1461 -0.0602 0.1866  260  PRO B CG  
10635 C CD  . PRO B 262  ? 0.6108 0.5349 0.3640 -0.1584 -0.0608 0.1992  260  PRO B CD  
10636 N N   . GLY B 263  ? 0.5233 0.4400 0.3200 -0.1423 -0.0663 0.1652  261  GLY B N   
10637 C CA  . GLY B 263  ? 0.5159 0.4169 0.3204 -0.1385 -0.0742 0.1575  261  GLY B CA  
10638 C C   . GLY B 263  ? 0.5001 0.4045 0.3076 -0.1273 -0.0719 0.1454  261  GLY B C   
10639 O O   . GLY B 263  ? 0.5028 0.4198 0.3054 -0.1226 -0.0651 0.1431  261  GLY B O   
10640 N N   . ILE B 264  ? 0.4920 0.3848 0.3075 -0.1231 -0.0778 0.1377  262  ILE B N   
10641 C CA  . ILE B 264  ? 0.4840 0.3787 0.3039 -0.1129 -0.0767 0.1262  262  ILE B CA  
10642 C C   . ILE B 264  ? 0.4715 0.3677 0.3053 -0.1121 -0.0764 0.1195  262  ILE B C   
10643 O O   . ILE B 264  ? 0.4669 0.3549 0.3058 -0.1177 -0.0810 0.1223  262  ILE B O   
10644 C CB  . ILE B 264  ? 0.4889 0.3674 0.3036 -0.1068 -0.0846 0.1226  262  ILE B CB  
10645 C CG1 . ILE B 264  ? 0.4840 0.3678 0.3008 -0.0968 -0.0820 0.1122  262  ILE B CG1 
10646 C CG2 . ILE B 264  ? 0.4865 0.3475 0.3071 -0.1077 -0.0937 0.1213  262  ILE B CG2 
10647 C CD1 . ILE B 264  ? 0.4833 0.3537 0.2942 -0.0911 -0.0893 0.1096  262  ILE B CD1 
10648 N N   . SER B 265  ? 0.4489 0.3558 0.2884 -0.1052 -0.0711 0.1109  263  SER B N   
10649 C CA  . SER B 265  ? 0.4689 0.3776 0.3207 -0.1026 -0.0706 0.1032  263  SER B CA  
10650 C C   . SER B 265  ? 0.4673 0.3693 0.3213 -0.0932 -0.0736 0.0935  263  SER B C   
10651 O O   . SER B 265  ? 0.4840 0.3898 0.3326 -0.0876 -0.0714 0.0908  263  SER B O   
10652 C CB  . SER B 265  ? 0.4505 0.3788 0.3080 -0.1027 -0.0613 0.1016  263  SER B CB  
10653 O OG  . SER B 265  ? 0.4893 0.4253 0.3475 -0.1116 -0.0585 0.1102  263  SER B OG  
10654 N N   . ILE B 266  ? 0.4318 0.3243 0.2939 -0.0913 -0.0785 0.0883  264  ILE B N   
10655 C CA  . ILE B 266  ? 0.4094 0.2961 0.2750 -0.0827 -0.0814 0.0793  264  ILE B CA  
10656 C C   . ILE B 266  ? 0.4484 0.3405 0.3255 -0.0801 -0.0788 0.0719  264  ILE B C   
10657 O O   . ILE B 266  ? 0.4004 0.2959 0.2826 -0.0852 -0.0773 0.0737  264  ILE B O   
10658 C CB  . ILE B 266  ? 0.4359 0.3037 0.2991 -0.0814 -0.0910 0.0798  264  ILE B CB  
10659 C CG1 . ILE B 266  ? 0.4935 0.3512 0.3618 -0.0862 -0.0958 0.0813  264  ILE B CG1 
10660 C CG2 . ILE B 266  ? 0.4379 0.2996 0.2889 -0.0842 -0.0941 0.0877  264  ILE B CG2 
10661 C CD1 . ILE B 266  ? 0.5186 0.3584 0.3877 -0.0825 -0.1047 0.0785  264  ILE B CD1 
10662 N N   . LYS B 267  ? 0.4154 0.3084 0.2964 -0.0722 -0.0784 0.0636  265  LYS B N   
10663 C CA  . LYS B 267  ? 0.4028 0.2991 0.2943 -0.0689 -0.0768 0.0562  265  LYS B CA  
10664 C C   . LYS B 267  ? 0.3893 0.2723 0.2842 -0.0639 -0.0836 0.0509  265  LYS B C   
10665 O O   . LYS B 267  ? 0.4135 0.2918 0.3053 -0.0590 -0.0865 0.0491  265  LYS B O   
10666 C CB  . LYS B 267  ? 0.4408 0.3514 0.3352 -0.0641 -0.0696 0.0509  265  LYS B CB  
10667 C CG  . LYS B 267  ? 0.4723 0.3975 0.3667 -0.0685 -0.0624 0.0546  265  LYS B CG  
10668 C CD  . LYS B 267  ? 0.5458 0.4840 0.4440 -0.0631 -0.0557 0.0487  265  LYS B CD  
10669 C CE  . LYS B 267  ? 0.5840 0.5370 0.4811 -0.0666 -0.0485 0.0529  265  LYS B CE  
10670 N NZ  . LYS B 267  ? 0.6156 0.5692 0.5030 -0.0712 -0.0479 0.0610  265  LYS B NZ  
10671 N N   . LEU B 268  ? 0.3959 0.2731 0.2972 -0.0649 -0.0862 0.0484  266  LEU B N   
10672 C CA  . LEU B 268  ? 0.4029 0.2675 0.3075 -0.0598 -0.0924 0.0433  266  LEU B CA  
10673 C C   . LEU B 268  ? 0.4015 0.2720 0.3115 -0.0515 -0.0901 0.0353  266  LEU B C   
10674 O O   . LEU B 268  ? 0.3990 0.2615 0.3098 -0.0462 -0.0948 0.0322  266  LEU B O   
10675 C CB  . LEU B 268  ? 0.3758 0.2334 0.2854 -0.0624 -0.0953 0.0418  266  LEU B CB  
10676 C CG  . LEU B 268  ? 0.4178 0.2661 0.3226 -0.0708 -0.0996 0.0496  266  LEU B CG  
10677 C CD1 . LEU B 268  ? 0.4404 0.2799 0.3499 -0.0723 -0.1033 0.0468  266  LEU B CD1 
10678 C CD2 . LEU B 268  ? 0.4056 0.2409 0.3031 -0.0710 -0.1060 0.0544  266  LEU B CD2 
10679 N N   . SER B 269  ? 0.3724 0.2568 0.2863 -0.0503 -0.0831 0.0320  267  SER B N   
10680 C CA  . SER B 269  ? 0.3911 0.2809 0.3100 -0.0431 -0.0810 0.0249  267  SER B CA  
10681 C C   . SER B 269  ? 0.3702 0.2596 0.2837 -0.0398 -0.0823 0.0256  267  SER B C   
10682 O O   . SER B 269  ? 0.4056 0.2956 0.3230 -0.0337 -0.0832 0.0203  267  SER B O   
10683 C CB  . SER B 269  ? 0.3745 0.2785 0.2979 -0.0429 -0.0735 0.0220  267  SER B CB  
10684 O OG  . SER B 269  ? 0.4163 0.3296 0.3343 -0.0456 -0.0688 0.0261  267  SER B OG  
10685 N N   . ALA B 270  ? 0.3818 0.2700 0.2862 -0.0437 -0.0829 0.0323  268  ALA B N   
10686 C CA  . ALA B 270  ? 0.3890 0.2754 0.2871 -0.0407 -0.0850 0.0331  268  ALA B CA  
10687 C C   . ALA B 270  ? 0.4275 0.3005 0.3254 -0.0378 -0.0932 0.0328  268  ALA B C   
10688 O O   . ALA B 270  ? 0.4233 0.2948 0.3187 -0.0337 -0.0958 0.0315  268  ALA B O   
10689 C CB  . ALA B 270  ? 0.4562 0.3454 0.3436 -0.0456 -0.0830 0.0405  268  ALA B CB  
10690 N N   . LEU B 271  ? 0.4009 0.2638 0.3013 -0.0396 -0.0976 0.0339  269  LEU B N   
10691 C CA  . LEU B 271  ? 0.3918 0.2407 0.2905 -0.0375 -0.1059 0.0351  269  LEU B CA  
10692 C C   . LEU B 271  ? 0.4325 0.2775 0.3407 -0.0307 -0.1088 0.0277  269  LEU B C   
10693 O O   . LEU B 271  ? 0.4445 0.2782 0.3526 -0.0280 -0.1157 0.0280  269  LEU B O   
10694 C CB  . LEU B 271  ? 0.3993 0.2374 0.2935 -0.0438 -0.1098 0.0415  269  LEU B CB  
10695 C CG  . LEU B 271  ? 0.4706 0.3104 0.3544 -0.0505 -0.1084 0.0502  269  LEU B CG  
10696 C CD1 . LEU B 271  ? 0.4910 0.3208 0.3719 -0.0576 -0.1121 0.0566  269  LEU B CD1 
10697 C CD2 . LEU B 271  ? 0.4579 0.2937 0.3341 -0.0480 -0.1122 0.0527  269  LEU B CD2 
10698 N N   . HIS B 272  ? 0.3825 0.2370 0.2988 -0.0279 -0.1037 0.0214  270  HIS B N   
10699 C CA  . HIS B 272  ? 0.4304 0.2826 0.3558 -0.0214 -0.1059 0.0146  270  HIS B CA  
10700 C C   . HIS B 272  ? 0.4529 0.3187 0.3853 -0.0187 -0.0992 0.0089  270  HIS B C   
10701 O O   . HIS B 272  ? 0.4036 0.2770 0.3356 -0.0224 -0.0935 0.0095  270  HIS B O   
10702 C CB  . HIS B 272  ? 0.4614 0.3038 0.3896 -0.0222 -0.1091 0.0137  270  HIS B CB  
10703 C CG  . HIS B 272  ? 0.4729 0.3108 0.4089 -0.0149 -0.1124 0.0075  270  HIS B CG  
10704 N ND1 . HIS B 272  ? 0.4273 0.2740 0.3718 -0.0105 -0.1081 0.0006  270  HIS B ND1 
10705 C CD2 . HIS B 272  ? 0.4997 0.3259 0.4362 -0.0109 -0.1195 0.0071  270  HIS B CD2 
10706 C CE1 . HIS B 272  ? 0.4985 0.3399 0.4488 -0.0042 -0.1121 -0.0036 270  HIS B CE1 
10707 N NE2 . HIS B 272  ? 0.5652 0.3941 0.5110 -0.0040 -0.1191 0.0000  270  HIS B NE2 
10708 N N   . PRO B 273  ? 0.4119 0.2810 0.3507 -0.0124 -0.0996 0.0036  271  PRO B N   
10709 C CA  . PRO B 273  ? 0.4024 0.2841 0.3476 -0.0102 -0.0934 -0.0014 271  PRO B CA  
10710 C C   . PRO B 273  ? 0.4249 0.3090 0.3769 -0.0096 -0.0903 -0.0056 271  PRO B C   
10711 O O   . PRO B 273  ? 0.4066 0.3011 0.3627 -0.0090 -0.0846 -0.0087 271  PRO B O   
10712 C CB  . PRO B 273  ? 0.3956 0.2789 0.3458 -0.0041 -0.0960 -0.0050 271  PRO B CB  
10713 C CG  . PRO B 273  ? 0.4426 0.3139 0.3924 -0.0018 -0.1036 -0.0037 271  PRO B CG  
10714 C CD  . PRO B 273  ? 0.4622 0.3246 0.4024 -0.0075 -0.1060 0.0028  271  PRO B CD  
10715 N N   . ARG B 274  ? 0.3945 0.2690 0.3474 -0.0096 -0.0940 -0.0059 272  ARG B N   
10716 C CA  . ARG B 274  ? 0.3671 0.2430 0.3255 -0.0087 -0.0915 -0.0103 272  ARG B CA  
10717 C C   . ARG B 274  ? 0.3765 0.2449 0.3300 -0.0146 -0.0930 -0.0067 272  ARG B C   
10718 O O   . ARG B 274  ? 0.3778 0.2369 0.3325 -0.0136 -0.0965 -0.0085 272  ARG B O   
10719 C CB  . ARG B 274  ? 0.3929 0.2644 0.3582 -0.0019 -0.0946 -0.0157 272  ARG B CB  
10720 C CG  . ARG B 274  ? 0.3828 0.2629 0.3550 0.0038  -0.0932 -0.0195 272  ARG B CG  
10721 C CD  . ARG B 274  ? 0.3719 0.2656 0.3475 0.0032  -0.0860 -0.0219 272  ARG B CD  
10722 N NE  . ARG B 274  ? 0.4047 0.3007 0.3834 0.0028  -0.0825 -0.0251 272  ARG B NE  
10723 C CZ  . ARG B 274  ? 0.4244 0.3219 0.4100 0.0078  -0.0817 -0.0305 272  ARG B CZ  
10724 N NH1 . ARG B 274  ? 0.4021 0.2996 0.3934 0.0136  -0.0842 -0.0331 272  ARG B NH1 
10725 N NH2 . ARG B 274  ? 0.4301 0.3294 0.4168 0.0069  -0.0786 -0.0331 272  ARG B NH2 
10726 N N   . TYR B 275  ? 0.3607 0.2331 0.3087 -0.0208 -0.0903 -0.0015 273  TYR B N   
10727 C CA  . TYR B 275  ? 0.3960 0.2626 0.3398 -0.0273 -0.0916 0.0027  273  TYR B CA  
10728 C C   . TYR B 275  ? 0.3900 0.2633 0.3384 -0.0285 -0.0872 -0.0008 273  TYR B C   
10729 O O   . TYR B 275  ? 0.3866 0.2714 0.3355 -0.0311 -0.0815 0.0002  273  TYR B O   
10730 C CB  . TYR B 275  ? 0.3791 0.2488 0.3157 -0.0334 -0.0903 0.0101  273  TYR B CB  
10731 C CG  . TYR B 275  ? 0.3801 0.2463 0.3134 -0.0410 -0.0909 0.0150  273  TYR B CG  
10732 C CD1 . TYR B 275  ? 0.4106 0.2627 0.3426 -0.0428 -0.0971 0.0160  273  TYR B CD1 
10733 C CD2 . TYR B 275  ? 0.3762 0.2533 0.3079 -0.0463 -0.0855 0.0188  273  TYR B CD2 
10734 C CE1 . TYR B 275  ? 0.4051 0.2539 0.3345 -0.0504 -0.0981 0.0207  273  TYR B CE1 
10735 C CE2 . TYR B 275  ? 0.4101 0.2852 0.3397 -0.0536 -0.0861 0.0236  273  TYR B CE2 
10736 C CZ  . TYR B 275  ? 0.4162 0.2771 0.3447 -0.0559 -0.0926 0.0247  273  TYR B CZ  
10737 O OH  . TYR B 275  ? 0.4256 0.2845 0.3523 -0.0638 -0.0936 0.0298  273  TYR B OH  
10738 N N   . SER B 276  ? 0.4027 0.2686 0.3542 -0.0262 -0.0900 -0.0050 274  SER B N   
10739 C CA  . SER B 276  ? 0.3985 0.2698 0.3537 -0.0269 -0.0864 -0.0088 274  SER B CA  
10740 C C   . SER B 276  ? 0.3908 0.2496 0.3463 -0.0255 -0.0912 -0.0121 274  SER B C   
10741 O O   . SER B 276  ? 0.4268 0.2749 0.3819 -0.0215 -0.0964 -0.0135 274  SER B O   
10742 C CB  . SER B 276  ? 0.4018 0.2854 0.3632 -0.0216 -0.0807 -0.0142 274  SER B CB  
10743 O OG  . SER B 276  ? 0.4103 0.2898 0.3760 -0.0145 -0.0829 -0.0195 274  SER B OG  
10744 N N   . ARG B 277  ? 0.3878 0.2480 0.3439 -0.0286 -0.0897 -0.0136 275  ARG B N   
10745 C CA  . ARG B 277  ? 0.4142 0.2624 0.3698 -0.0273 -0.0943 -0.0174 275  ARG B CA  
10746 C C   . ARG B 277  ? 0.4068 0.2530 0.3667 -0.0182 -0.0947 -0.0246 275  ARG B C   
10747 O O   . ARG B 277  ? 0.4279 0.2609 0.3865 -0.0151 -0.1001 -0.0270 275  ARG B O   
10748 C CB  . ARG B 277  ? 0.3753 0.2276 0.3312 -0.0317 -0.0920 -0.0185 275  ARG B CB  
10749 C CG  . ARG B 277  ? 0.4240 0.2643 0.3787 -0.0302 -0.0963 -0.0234 275  ARG B CG  
10750 C CD  . ARG B 277  ? 0.4550 0.2776 0.4046 -0.0327 -0.1043 -0.0203 275  ARG B CD  
10751 N NE  . ARG B 277  ? 0.4624 0.2721 0.4101 -0.0307 -0.1088 -0.0256 275  ARG B NE  
10752 C CZ  . ARG B 277  ? 0.4783 0.2816 0.4274 -0.0222 -0.1105 -0.0321 275  ARG B CZ  
10753 N NH1 . ARG B 277  ? 0.4759 0.2849 0.4291 -0.0152 -0.1082 -0.0341 275  ARG B NH1 
10754 N NH2 . ARG B 277  ? 0.4707 0.2620 0.4171 -0.0205 -0.1146 -0.0370 275  ARG B NH2 
10755 N N   . ALA B 278  ? 0.4043 0.2634 0.3696 -0.0137 -0.0891 -0.0279 276  ALA B N   
10756 C CA  . ALA B 278  ? 0.4141 0.2731 0.3843 -0.0052 -0.0890 -0.0344 276  ALA B CA  
10757 C C   . ALA B 278  ? 0.4255 0.2756 0.3958 -0.0009 -0.0943 -0.0338 276  ALA B C   
10758 O O   . ALA B 278  ? 0.4501 0.2955 0.4235 0.0059  -0.0963 -0.0389 276  ALA B O   
10759 C CB  . ALA B 278  ? 0.4059 0.2808 0.3820 -0.0021 -0.0822 -0.0370 276  ALA B CB  
10760 N N   . GLN B 279  ? 0.4115 0.2592 0.3782 -0.0044 -0.0966 -0.0277 277  GLN B N   
10761 C CA  . GLN B 279  ? 0.4002 0.2394 0.3663 -0.0008 -0.1021 -0.0263 277  GLN B CA  
10762 C C   . GLN B 279  ? 0.4510 0.2750 0.4099 -0.0057 -0.1087 -0.0211 277  GLN B C   
10763 O O   . GLN B 279  ? 0.4363 0.2549 0.3923 -0.0060 -0.1127 -0.0168 277  GLN B O   
10764 C CB  . GLN B 279  ? 0.4330 0.2817 0.4004 -0.0003 -0.0999 -0.0236 277  GLN B CB  
10765 C CG  . GLN B 279  ? 0.4147 0.2778 0.3896 0.0042  -0.0940 -0.0283 277  GLN B CG  
10766 C CD  . GLN B 279  ? 0.4575 0.3192 0.4390 0.0124  -0.0955 -0.0343 277  GLN B CD  
10767 O OE1 . GLN B 279  ? 0.5056 0.3569 0.4868 0.0159  -0.1013 -0.0344 277  GLN B OE1 
10768 N NE2 . GLN B 279  ? 0.4053 0.2775 0.3930 0.0157  -0.0902 -0.0392 277  GLN B NE2 
10769 N N   . ALA B 280  ? 0.4411 0.2578 0.3969 -0.0096 -0.1103 -0.0214 278  ALA B N   
10770 C CA  . ALA B 280  ? 0.4498 0.2519 0.3987 -0.0154 -0.1165 -0.0160 278  ALA B CA  
10771 C C   . ALA B 280  ? 0.4828 0.2703 0.4302 -0.0108 -0.1239 -0.0157 278  ALA B C   
10772 O O   . ALA B 280  ? 0.4644 0.2424 0.4060 -0.0154 -0.1289 -0.0092 278  ALA B O   
10773 C CB  . ALA B 280  ? 0.4181 0.2137 0.3650 -0.0191 -0.1177 -0.0179 278  ALA B CB  
10774 N N   . ALA B 281  ? 0.4646 0.2503 0.4170 -0.0018 -0.1249 -0.0224 279  ALA B N   
10775 C CA  . ALA B 281  ? 0.5138 0.2866 0.4656 0.0035  -0.1320 -0.0224 279  ALA B CA  
10776 C C   . ALA B 281  ? 0.5023 0.2787 0.4532 0.0028  -0.1331 -0.0167 279  ALA B C   
10777 O O   . ALA B 281  ? 0.5091 0.2731 0.4545 0.0007  -0.1394 -0.0115 279  ALA B O   
10778 C CB  . ALA B 281  ? 0.5273 0.3012 0.4861 0.0139  -0.1316 -0.0307 279  ALA B CB  
10779 N N   . ARG B 282  ? 0.4725 0.2651 0.4279 0.0043  -0.1271 -0.0176 280  ARG B N   
10780 C CA  . ARG B 282  ? 0.5127 0.3090 0.4663 0.0035  -0.1281 -0.0126 280  ARG B CA  
10781 C C   . ARG B 282  ? 0.4904 0.2843 0.4354 -0.0058 -0.1285 -0.0044 280  ARG B C   
10782 O O   . ARG B 282  ? 0.5386 0.3273 0.4787 -0.0074 -0.1326 0.0011  280  ARG B O   
10783 C CB  . ARG B 282  ? 0.4930 0.3068 0.4531 0.0066  -0.1216 -0.0157 280  ARG B CB  
10784 C CG  . ARG B 282  ? 0.4876 0.3053 0.4568 0.0157  -0.1212 -0.0227 280  ARG B CG  
10785 C CD  . ARG B 282  ? 0.4975 0.3306 0.4723 0.0180  -0.1166 -0.0240 280  ARG B CD  
10786 N NE  . ARG B 282  ? 0.4883 0.3205 0.4593 0.0165  -0.1199 -0.0188 280  ARG B NE  
10787 C CZ  . ARG B 282  ? 0.5194 0.3629 0.4917 0.0159  -0.1166 -0.0179 280  ARG B CZ  
10788 N NH1 . ARG B 282  ? 0.4602 0.3169 0.4380 0.0166  -0.1100 -0.0217 280  ARG B NH1 
10789 N NH2 . ARG B 282  ? 0.4524 0.2933 0.4195 0.0143  -0.1203 -0.0131 280  ARG B NH2 
10790 N N   . VAL B 283  ? 0.4643 0.2627 0.4074 -0.0121 -0.1243 -0.0033 281  VAL B N   
10791 C CA  . VAL B 283  ? 0.4542 0.2525 0.3901 -0.0211 -0.1239 0.0046  281  VAL B CA  
10792 C C   . VAL B 283  ? 0.4921 0.2724 0.4215 -0.0245 -0.1319 0.0097  281  VAL B C   
10793 O O   . VAL B 283  ? 0.5040 0.2807 0.4272 -0.0284 -0.1345 0.0168  281  VAL B O   
10794 C CB  . VAL B 283  ? 0.4273 0.2349 0.3640 -0.0267 -0.1179 0.0044  281  VAL B CB  
10795 C CG1 . VAL B 283  ? 0.4517 0.2570 0.3813 -0.0363 -0.1185 0.0128  281  VAL B CG1 
10796 C CG2 . VAL B 283  ? 0.4204 0.2458 0.3618 -0.0243 -0.1101 0.0013  281  VAL B CG2 
10797 N N   . MET B 284  ? 0.4598 0.2278 0.3901 -0.0229 -0.1362 0.0063  282  MET B N   
10798 C CA  . MET B 284  ? 0.4967 0.2461 0.4206 -0.0263 -0.1444 0.0112  282  MET B CA  
10799 C C   . MET B 284  ? 0.5436 0.2839 0.4663 -0.0208 -0.1506 0.0126  282  MET B C   
10800 O O   . MET B 284  ? 0.5396 0.2678 0.4554 -0.0250 -0.1565 0.0194  282  MET B O   
10801 C CB  . MET B 284  ? 0.5290 0.2664 0.4537 -0.0254 -0.1479 0.0065  282  MET B CB  
10802 C CG  . MET B 284  ? 0.5125 0.2568 0.4376 -0.0317 -0.1432 0.0058  282  MET B CG  
10803 S SD  . MET B 284  ? 0.5897 0.3378 0.5086 -0.0446 -0.1419 0.0166  282  MET B SD  
10804 C CE  . MET B 284  ? 0.5807 0.3044 0.4927 -0.0499 -0.1524 0.0217  282  MET B CE  
10805 N N   . GLY B 285  ? 0.5437 0.2898 0.4729 -0.0117 -0.1495 0.0066  283  GLY B N   
10806 C CA  . GLY B 285  ? 0.5358 0.2735 0.4649 -0.0058 -0.1558 0.0073  283  GLY B CA  
10807 C C   . GLY B 285  ? 0.5497 0.2951 0.4762 -0.0069 -0.1550 0.0124  283  GLY B C   
10808 O O   . GLY B 285  ? 0.5609 0.2969 0.4841 -0.0052 -0.1615 0.0162  283  GLY B O   
10809 N N   . GLU B 286  ? 0.5171 0.2790 0.4446 -0.0098 -0.1474 0.0127  284  GLU B N   
10810 C CA  . GLU B 286  ? 0.5337 0.3043 0.4589 -0.0101 -0.1460 0.0161  284  GLU B CA  
10811 C C   . GLU B 286  ? 0.5350 0.3112 0.4523 -0.0191 -0.1421 0.0231  284  GLU B C   
10812 O O   . GLU B 286  ? 0.5508 0.3247 0.4610 -0.0217 -0.1447 0.0293  284  GLU B O   
10813 C CB  . GLU B 286  ? 0.5168 0.3027 0.4506 -0.0039 -0.1406 0.0094  284  GLU B CB  
10814 C CG  . GLU B 286  ? 0.5626 0.3456 0.5052 0.0054  -0.1436 0.0026  284  GLU B CG  
10815 C CD  . GLU B 286  ? 0.5907 0.3896 0.5427 0.0103  -0.1371 -0.0041 284  GLU B CD  
10816 O OE1 . GLU B 286  ? 0.5411 0.3523 0.4925 0.0076  -0.1319 -0.0031 284  GLU B OE1 
10817 O OE2 . GLU B 286  ? 0.6546 0.4537 0.6145 0.0168  -0.1371 -0.0105 284  GLU B OE2 
10818 N N   . LEU B 287  ? 0.4790 0.2636 0.3976 -0.0235 -0.1359 0.0221  285  LEU B N   
10819 C CA  . LEU B 287  ? 0.5031 0.2947 0.4153 -0.0318 -0.1316 0.0286  285  LEU B CA  
10820 C C   . LEU B 287  ? 0.5125 0.2910 0.4168 -0.0391 -0.1367 0.0365  285  LEU B C   
10821 O O   . LEU B 287  ? 0.4571 0.2359 0.3536 -0.0439 -0.1371 0.0438  285  LEU B O   
10822 C CB  . LEU B 287  ? 0.4252 0.2293 0.3421 -0.0340 -0.1239 0.0251  285  LEU B CB  
10823 C CG  . LEU B 287  ? 0.4452 0.2638 0.3591 -0.0391 -0.1167 0.0287  285  LEU B CG  
10824 C CD1 . LEU B 287  ? 0.4118 0.2426 0.3321 -0.0390 -0.1098 0.0237  285  LEU B CD1 
10825 C CD2 . LEU B 287  ? 0.4934 0.3079 0.3992 -0.0480 -0.1178 0.0376  285  LEU B CD2 
10826 N N   . LEU B 288  ? 0.4869 0.2535 0.3926 -0.0400 -0.1409 0.0352  286  LEU B N   
10827 C CA  . LEU B 288  ? 0.5231 0.2768 0.4217 -0.0479 -0.1459 0.0429  286  LEU B CA  
10828 C C   . LEU B 288  ? 0.5467 0.2895 0.4377 -0.0485 -0.1524 0.0496  286  LEU B C   
10829 O O   . LEU B 288  ? 0.5479 0.2894 0.4313 -0.0565 -0.1528 0.0583  286  LEU B O   
10830 C CB  . LEU B 288  ? 0.5242 0.2646 0.4255 -0.0475 -0.1505 0.0392  286  LEU B CB  
10831 C CG  . LEU B 288  ? 0.5955 0.3199 0.4899 -0.0555 -0.1571 0.0468  286  LEU B CG  
10832 C CD1 . LEU B 288  ? 0.5607 0.2941 0.4525 -0.0659 -0.1523 0.0530  286  LEU B CD1 
10833 C CD2 . LEU B 288  ? 0.5999 0.3073 0.4961 -0.0529 -0.1637 0.0423  286  LEU B CD2 
10834 N N   . PRO B 289  ? 0.5646 0.2996 0.4571 -0.0406 -0.1579 0.0466  287  PRO B N   
10835 C CA  . PRO B 289  ? 0.5134 0.2383 0.3980 -0.0415 -0.1644 0.0536  287  PRO B CA  
10836 C C   . PRO B 289  ? 0.5359 0.2725 0.4142 -0.0453 -0.1600 0.0593  287  PRO B C   
10837 O O   . PRO B 289  ? 0.5669 0.2964 0.4360 -0.0501 -0.1638 0.0677  287  PRO B O   
10838 C CB  . PRO B 289  ? 0.5966 0.3157 0.4866 -0.0310 -0.1694 0.0477  287  PRO B CB  
10839 C CG  . PRO B 289  ? 0.5905 0.3082 0.4891 -0.0265 -0.1685 0.0392  287  PRO B CG  
10840 C CD  . PRO B 289  ? 0.5806 0.3133 0.4817 -0.0310 -0.1595 0.0373  287  PRO B CD  
10841 N N   . ARG B 290  ? 0.5420 0.2959 0.4244 -0.0430 -0.1521 0.0548  288  ARG B N   
10842 C CA  A ARG B 290  ? 0.5127 0.2779 0.3884 -0.0464 -0.1475 0.0596  288  ARG B CA  
10843 C CA  B ARG B 290  ? 0.5129 0.2782 0.3887 -0.0464 -0.1474 0.0595  288  ARG B CA  
10844 C C   . ARG B 290  ? 0.5119 0.2802 0.3815 -0.0564 -0.1438 0.0671  288  ARG B C   
10845 O O   . ARG B 290  ? 0.5166 0.2844 0.3767 -0.0612 -0.1444 0.0750  288  ARG B O   
10846 C CB  A ARG B 290  ? 0.5162 0.2982 0.3981 -0.0414 -0.1403 0.0526  288  ARG B CB  
10847 C CB  B ARG B 290  ? 0.5161 0.2981 0.3982 -0.0414 -0.1402 0.0524  288  ARG B CB  
10848 C CG  A ARG B 290  ? 0.5208 0.3027 0.4064 -0.0328 -0.1436 0.0477  288  ARG B CG  
10849 C CG  B ARG B 290  ? 0.5206 0.3017 0.4082 -0.0321 -0.1436 0.0464  288  ARG B CG  
10850 C CD  A ARG B 290  ? 0.5307 0.3284 0.4236 -0.0284 -0.1365 0.0404  288  ARG B CD  
10851 C CD  B ARG B 290  ? 0.5298 0.3272 0.4239 -0.0279 -0.1367 0.0397  288  ARG B CD  
10852 N NE  A ARG B 290  ? 0.5478 0.3476 0.4435 -0.0215 -0.1392 0.0369  288  ARG B NE  
10853 N NE  B ARG B 290  ? 0.5477 0.3466 0.4430 -0.0217 -0.1396 0.0372  288  ARG B NE  
10854 C CZ  A ARG B 290  ? 0.5106 0.3222 0.4136 -0.0169 -0.1348 0.0304  288  ARG B CZ  
10855 C CZ  B ARG B 290  ? 0.5404 0.3403 0.4452 -0.0142 -0.1414 0.0304  288  ARG B CZ  
10856 N NH1 A ARG B 290  ? 0.4992 0.3212 0.4072 -0.0179 -0.1275 0.0265  288  ARG B NH1 
10857 N NH1 B ARG B 290  ? 0.5308 0.3304 0.4444 -0.0115 -0.1401 0.0249  288  ARG B NH1 
10858 N NH2 A ARG B 290  ? 0.5135 0.3262 0.4188 -0.0113 -0.1381 0.0279  288  ARG B NH2 
10859 N NH2 B ARG B 290  ? 0.5375 0.3391 0.4431 -0.0094 -0.1445 0.0292  288  ARG B NH2 
10860 N N   . VAL B 291  ? 0.4778 0.2495 0.3526 -0.0599 -0.1403 0.0651  289  VAL B N   
10861 C CA  . VAL B 291  ? 0.5230 0.2979 0.3932 -0.0698 -0.1373 0.0726  289  VAL B CA  
10862 C C   . VAL B 291  ? 0.4973 0.2558 0.3599 -0.0756 -0.1450 0.0812  289  VAL B C   
10863 O O   . VAL B 291  ? 0.5202 0.2810 0.3751 -0.0830 -0.1436 0.0900  289  VAL B O   
10864 C CB  . VAL B 291  ? 0.5301 0.3102 0.4079 -0.0724 -0.1334 0.0687  289  VAL B CB  
10865 C CG1 . VAL B 291  ? 0.5058 0.2947 0.3804 -0.0821 -0.1286 0.0760  289  VAL B CG1 
10866 C CG2 . VAL B 291  ? 0.4972 0.2900 0.3833 -0.0654 -0.1275 0.0593  289  VAL B CG2 
10867 N N   . LYS B 292  ? 0.5288 0.2702 0.3931 -0.0722 -0.1531 0.0789  290  LYS B N   
10868 C CA  . LYS B 292  ? 0.5621 0.2861 0.4193 -0.0778 -0.1611 0.0870  290  LYS B CA  
10869 C C   . LYS B 292  ? 0.5466 0.2688 0.3940 -0.0787 -0.1634 0.0944  290  LYS B C   
10870 O O   . LYS B 292  ? 0.5839 0.3012 0.4231 -0.0869 -0.1653 0.1042  290  LYS B O   
10871 C CB  . LYS B 292  ? 0.5774 0.2830 0.4383 -0.0723 -0.1696 0.0822  290  LYS B CB  
10872 N N   . ALA B 293  ? 0.5728 0.2992 0.4209 -0.0705 -0.1633 0.0899  291  ALA B N   
10873 C CA  . ALA B 293  ? 0.5613 0.2860 0.3996 -0.0707 -0.1658 0.0962  291  ALA B CA  
10874 C C   . ALA B 293  ? 0.5727 0.3111 0.4036 -0.0779 -0.1585 0.1029  291  ALA B C   
10875 O O   . ALA B 293  ? 0.6057 0.3392 0.4262 -0.0836 -0.1610 0.1123  291  ALA B O   
10876 C CB  . ALA B 293  ? 0.5556 0.2843 0.3973 -0.0606 -0.1667 0.0892  291  ALA B CB  
10877 N N   . LEU B 294  ? 0.5402 0.2961 0.3763 -0.0777 -0.1494 0.0983  292  LEU B N   
10878 C CA  . LEU B 294  ? 0.5219 0.2921 0.3519 -0.0838 -0.1418 0.1040  292  LEU B CA  
10879 C C   . LEU B 294  ? 0.5460 0.3123 0.3723 -0.0944 -0.1421 0.1131  292  LEU B C   
10880 O O   . LEU B 294  ? 0.5535 0.3228 0.3703 -0.1005 -0.1405 0.1221  292  LEU B O   
10881 C CB  . LEU B 294  ? 0.4965 0.2850 0.3339 -0.0811 -0.1324 0.0968  292  LEU B CB  
10882 C CG  . LEU B 294  ? 0.5072 0.3023 0.3474 -0.0718 -0.1307 0.0886  292  LEU B CG  
10883 C CD1 . LEU B 294  ? 0.4688 0.2792 0.3180 -0.0694 -0.1226 0.0813  292  LEU B CD1 
10884 C CD2 . LEU B 294  ? 0.5103 0.3096 0.3395 -0.0715 -0.1298 0.0930  292  LEU B CD2 
10885 N N   . ALA B 295  ? 0.5294 0.2896 0.3632 -0.0968 -0.1441 0.1111  293  ALA B N   
10886 C CA  . ALA B 295  ? 0.5571 0.3127 0.3884 -0.1074 -0.1454 0.1196  293  ALA B CA  
10887 C C   . ALA B 295  ? 0.5902 0.3283 0.4119 -0.1115 -0.1539 0.1288  293  ALA B C   
10888 O O   . ALA B 295  ? 0.5906 0.3290 0.4058 -0.1209 -0.1535 0.1390  293  ALA B O   
10889 C CB  . ALA B 295  ? 0.5372 0.2876 0.3781 -0.1083 -0.1471 0.1145  293  ALA B CB  
10890 N N   . LEU B 296  ? 0.6260 0.3492 0.4468 -0.1045 -0.1619 0.1255  294  LEU B N   
10891 C CA  . LEU B 296  ? 0.6339 0.3402 0.4452 -0.1073 -0.1705 0.1339  294  LEU B CA  
10892 C C   . LEU B 296  ? 0.6464 0.3610 0.4463 -0.1107 -0.1671 0.1421  294  LEU B C   
10893 O O   . LEU B 296  ? 0.6649 0.3723 0.4558 -0.1186 -0.1702 0.1529  294  LEU B O   
10894 C CB  . LEU B 296  ? 0.6654 0.3572 0.4789 -0.0975 -0.1787 0.1278  294  LEU B CB  
10895 C CG  . LEU B 296  ? 0.8048 0.4726 0.6140 -0.0987 -0.1902 0.1327  294  LEU B CG  
10896 C CD1 . LEU B 296  ? 0.7808 0.4418 0.5821 -0.1109 -0.1922 0.1449  294  LEU B CD1 
10897 C CD2 . LEU B 296  ? 0.8039 0.4604 0.6229 -0.0931 -0.1949 0.1240  294  LEU B CD2 
10898 N N   . LEU B 297  ? 0.5864 0.3160 0.3860 -0.1048 -0.1608 0.1371  295  LEU B N   
10899 C CA  . LEU B 297  ? 0.6390 0.3774 0.4271 -0.1074 -0.1570 0.1439  295  LEU B CA  
10900 C C   . LEU B 297  ? 0.6091 0.3607 0.3944 -0.1171 -0.1492 0.1513  295  LEU B C   
10901 O O   . LEU B 297  ? 0.6068 0.3581 0.3812 -0.1236 -0.1491 0.1616  295  LEU B O   
10902 C CB  . LEU B 297  ? 0.5770 0.3276 0.3657 -0.0985 -0.1525 0.1360  295  LEU B CB  
10903 N N   . ALA B 298  ? 0.6086 0.3724 0.4038 -0.1182 -0.1424 0.1464  296  ALA B N   
10904 C CA  . ALA B 298  ? 0.5805 0.3578 0.3747 -0.1273 -0.1350 0.1533  296  ALA B CA  
10905 C C   . ALA B 298  ? 0.6569 0.4218 0.4474 -0.1378 -0.1406 0.1641  296  ALA B C   
10906 O O   . ALA B 298  ? 0.6430 0.4154 0.4269 -0.1461 -0.1368 0.1741  296  ALA B O   
10907 C CB  . ALA B 298  ? 0.6043 0.3950 0.4109 -0.1263 -0.1282 0.1458  296  ALA B CB  
10908 N N   . LYS B 299  ? 0.6117 0.3576 0.4062 -0.1374 -0.1498 0.1625  297  LYS B N   
10909 C CA  . LYS B 299  ? 0.6242 0.3556 0.4149 -0.1472 -0.1564 0.1726  297  LYS B CA  
10910 C C   . LYS B 299  ? 0.6813 0.4043 0.4581 -0.1500 -0.1606 0.1827  297  LYS B C   
10911 O O   . LYS B 299  ? 0.6600 0.3867 0.4340 -0.1586 -0.1592 0.1909  297  LYS B O   
10912 C CB  . LYS B 299  ? 0.6286 0.3400 0.4259 -0.1447 -0.1657 0.1674  297  LYS B CB  
10913 N N   . ASN B 300  ? 0.6784 0.3957 0.4503 -0.1413 -0.1642 0.1789  298  ASN B N   
10914 C CA  . ASN B 300  ? 0.7084 0.4205 0.4695 -0.1424 -0.1675 0.1857  298  ASN B CA  
10915 C C   . ASN B 300  ? 0.6725 0.4031 0.4256 -0.1477 -0.1584 0.1927  298  ASN B C   
10916 O O   . ASN B 300  ? 0.6873 0.4170 0.4337 -0.1524 -0.1590 0.2001  298  ASN B O   
10917 C CB  . ASN B 300  ? 0.7821 0.4851 0.5396 -0.1319 -0.1733 0.1802  298  ASN B CB  
10918 C CG  . ASN B 300  ? 0.7939 0.4778 0.5589 -0.1264 -0.1830 0.1741  298  ASN B CG  
10919 O OD1 . ASN B 300  ? 0.7968 0.4712 0.5667 -0.1311 -0.1870 0.1755  298  ASN B OD1 
10920 N ND2 . ASN B 300  ? 0.7905 0.4695 0.5567 -0.1161 -0.1869 0.1670  298  ASN B ND2 
10921 N N   . TYR B 301  ? 0.6471 0.3947 0.4011 -0.1469 -0.1495 0.1905  299  TYR B N   
10922 C CA  . TYR B 301  ? 0.6613 0.4282 0.4088 -0.1514 -0.1398 0.1963  299  TYR B CA  
10923 C C   . TYR B 301  ? 0.6824 0.4613 0.4368 -0.1610 -0.1335 0.2012  299  TYR B C   
10924 O O   . TYR B 301  ? 0.6830 0.4788 0.4333 -0.1652 -0.1252 0.2065  299  TYR B O   
10925 C CB  . TYR B 301  ? 0.6576 0.4403 0.4043 -0.1433 -0.1322 0.1884  299  TYR B CB  
10926 C CG  . TYR B 301  ? 0.6336 0.4094 0.3717 -0.1347 -0.1365 0.1849  299  TYR B CG  
10927 C CD1 . TYR B 301  ? 0.6648 0.4387 0.3884 -0.1369 -0.1377 0.1929  299  TYR B CD1 
10928 C CD2 . TYR B 301  ? 0.6630 0.4362 0.4086 -0.1244 -0.1389 0.1729  299  TYR B CD2 
10929 C CE1 . TYR B 301  ? 0.6550 0.4228 0.3707 -0.1293 -0.1421 0.1897  299  TYR B CE1 
10930 C CE2 . TYR B 301  ? 0.6348 0.4027 0.3735 -0.1169 -0.1432 0.1698  299  TYR B CE2 
10931 C CZ  . TYR B 301  ? 0.6622 0.4268 0.3854 -0.1196 -0.1452 0.1785  299  TYR B CZ  
10932 O OH  . TYR B 301  ? 0.6452 0.4044 0.3614 -0.1123 -0.1499 0.1754  299  TYR B OH  
10933 N N   . ASP B 302  ? 0.6761 0.4470 0.4409 -0.1642 -0.1375 0.1992  300  ASP B N   
10934 C CA  . ASP B 302  ? 0.6520 0.4339 0.4252 -0.1728 -0.1326 0.2025  300  ASP B CA  
10935 C C   . ASP B 302  ? 0.6216 0.4265 0.3966 -0.1725 -0.1212 0.2012  300  ASP B C   
10936 O O   . ASP B 302  ? 0.6577 0.4798 0.4331 -0.1785 -0.1135 0.2070  300  ASP B O   
10937 C CB  . ASP B 302  ? 0.6655 0.4486 0.4366 -0.1819 -0.1330 0.2120  300  ASP B CB  
10938 C CG  . ASP B 302  ? 0.7773 0.5667 0.5590 -0.1907 -0.1312 0.2147  300  ASP B CG  
10939 O OD1 . ASP B 302  ? 0.7304 0.5107 0.5206 -0.1901 -0.1357 0.2091  300  ASP B OD1 
10940 O OD2 . ASP B 302  ? 0.7667 0.5708 0.5485 -0.1980 -0.1252 0.2220  300  ASP B OD2 
10941 N N   . ILE B 303  ? 0.6020 0.4117 0.3837 -0.1624 -0.1188 0.1889  301  ILE B N   
10942 C CA  . ILE B 303  ? 0.5825 0.4146 0.3704 -0.1595 -0.1080 0.1834  301  ILE B CA  
10943 C C   . ILE B 303  ? 0.5666 0.3985 0.3690 -0.1570 -0.1087 0.1741  301  ILE B C   
10944 O O   . ILE B 303  ? 0.5688 0.3834 0.3752 -0.1546 -0.1169 0.1696  301  ILE B O   
10945 C CB  . ILE B 303  ? 0.5735 0.4143 0.3556 -0.1495 -0.1032 0.1768  301  ILE B CB  
10946 C CG1 . ILE B 303  ? 0.5728 0.4010 0.3590 -0.1395 -0.1094 0.1658  301  ILE B CG1 
10947 C CG2 . ILE B 303  ? 0.5907 0.4304 0.3571 -0.1516 -0.1033 0.1856  301  ILE B CG2 
10948 C CD1 . ILE B 303  ? 0.5669 0.4048 0.3506 -0.1295 -0.1046 0.1575  301  ILE B CD1 
10949 N N   . GLY B 304  ? 0.5510 0.4024 0.3607 -0.1570 -0.0997 0.1710  302  GLY B N   
10950 C CA  . GLY B 304  ? 0.5349 0.3884 0.3576 -0.1540 -0.0993 0.1620  302  GLY B CA  
10951 C C   . GLY B 304  ? 0.5617 0.4143 0.3869 -0.1419 -0.0989 0.1497  302  GLY B C   
10952 O O   . GLY B 304  ? 0.5164 0.3758 0.3356 -0.1358 -0.0951 0.1473  302  GLY B O   
10953 N N   . LEU B 305  ? 0.5129 0.3564 0.3471 -0.1385 -0.1034 0.1419  303  LEU B N   
10954 C CA  . LEU B 305  ? 0.4972 0.3416 0.3364 -0.1276 -0.1026 0.1299  303  LEU B CA  
10955 C C   . LEU B 305  ? 0.4825 0.3343 0.3337 -0.1276 -0.0996 0.1238  303  LEU B C   
10956 O O   . LEU B 305  ? 0.5062 0.3472 0.3622 -0.1315 -0.1051 0.1239  303  LEU B O   
10957 C CB  . LEU B 305  ? 0.5043 0.3286 0.3417 -0.1220 -0.1119 0.1259  303  LEU B CB  
10958 C CG  . LEU B 305  ? 0.5137 0.3398 0.3560 -0.1108 -0.1110 0.1143  303  LEU B CG  
10959 C CD1 . LEU B 305  ? 0.5139 0.3254 0.3504 -0.1050 -0.1184 0.1131  303  LEU B CD1 
10960 C CD2 . LEU B 305  ? 0.5350 0.3590 0.3887 -0.1081 -0.1120 0.1061  303  LEU B CD2 
10961 N N   . ASN B 306  ? 0.4674 0.3367 0.3229 -0.1233 -0.0912 0.1185  304  ASN B N   
10962 C CA  . ASN B 306  ? 0.4892 0.3683 0.3556 -0.1235 -0.0873 0.1134  304  ASN B CA  
10963 C C   . ASN B 306  ? 0.4614 0.3401 0.3337 -0.1135 -0.0868 0.1016  304  ASN B C   
10964 O O   . ASN B 306  ? 0.4650 0.3477 0.3341 -0.1063 -0.0842 0.0975  304  ASN B O   
10965 C CB  . ASN B 306  ? 0.4766 0.3774 0.3443 -0.1267 -0.0776 0.1170  304  ASN B CB  
10966 C CG  . ASN B 306  ? 0.4675 0.3793 0.3464 -0.1257 -0.0734 0.1112  304  ASN B CG  
10967 O OD1 . ASN B 306  ? 0.5278 0.4506 0.4100 -0.1187 -0.0678 0.1042  304  ASN B OD1 
10968 N ND2 . ASN B 306  ? 0.4497 0.3576 0.3343 -0.1327 -0.0768 0.1138  304  ASN B ND2 
10969 N N   . ILE B 307  ? 0.4355 0.3099 0.3162 -0.1132 -0.0893 0.0964  305  ILE B N   
10970 C CA  . ILE B 307  ? 0.4730 0.3484 0.3604 -0.1045 -0.0883 0.0856  305  ILE B CA  
10971 C C   . ILE B 307  ? 0.4570 0.3508 0.3514 -0.1045 -0.0803 0.0828  305  ILE B C   
10972 O O   . ILE B 307  ? 0.4305 0.3275 0.3303 -0.1102 -0.0800 0.0844  305  ILE B O   
10973 C CB  . ILE B 307  ? 0.4200 0.2791 0.3116 -0.1033 -0.0959 0.0810  305  ILE B CB  
10974 C CG1 . ILE B 307  ? 0.5189 0.3598 0.4038 -0.1018 -0.1040 0.0831  305  ILE B CG1 
10975 C CG2 . ILE B 307  ? 0.4162 0.2788 0.3151 -0.0949 -0.0938 0.0702  305  ILE B CG2 
10976 C CD1 . ILE B 307  ? 0.5369 0.3599 0.4233 -0.1044 -0.1123 0.0829  305  ILE B CD1 
10977 N N   . ASP B 308  ? 0.4016 0.3070 0.2956 -0.0982 -0.0742 0.0787  306  ASP B N   
10978 C CA  . ASP B 308  ? 0.4273 0.3495 0.3280 -0.0966 -0.0667 0.0751  306  ASP B CA  
10979 C C   . ASP B 308  ? 0.4142 0.3331 0.3236 -0.0938 -0.0685 0.0675  306  ASP B C   
10980 O O   . ASP B 308  ? 0.4124 0.3183 0.3226 -0.0897 -0.0740 0.0626  306  ASP B O   
10981 C CB  . ASP B 308  ? 0.4171 0.3490 0.3151 -0.0894 -0.0610 0.0711  306  ASP B CB  
10982 C CG  . ASP B 308  ? 0.5148 0.4536 0.4039 -0.0918 -0.0574 0.0781  306  ASP B CG  
10983 O OD1 . ASP B 308  ? 0.4703 0.4102 0.3564 -0.0997 -0.0577 0.0867  306  ASP B OD1 
10984 O OD2 . ASP B 308  ? 0.4662 0.4095 0.3509 -0.0859 -0.0543 0.0750  306  ASP B OD2 
10985 N N   . ALA B 309  ? 0.3929 0.3242 0.3089 -0.0958 -0.0638 0.0666  307  ALA B N   
10986 C CA  . ALA B 309  ? 0.3995 0.3298 0.3233 -0.0931 -0.0647 0.0595  307  ALA B CA  
10987 C C   . ALA B 309  ? 0.3884 0.3295 0.3158 -0.0853 -0.0589 0.0525  307  ALA B C   
10988 O O   . ALA B 309  ? 0.3696 0.3241 0.2959 -0.0845 -0.0526 0.0541  307  ALA B O   
10989 C CB  . ALA B 309  ? 0.3810 0.3174 0.3102 -0.1006 -0.0641 0.0629  307  ALA B CB  
10990 N N   . GLU B 310  ? 0.3425 0.2775 0.2738 -0.0795 -0.0610 0.0446  308  GLU B N   
10991 C CA  . GLU B 310  ? 0.3938 0.3366 0.3281 -0.0719 -0.0565 0.0379  308  GLU B CA  
10992 C C   . GLU B 310  ? 0.3448 0.2927 0.2868 -0.0706 -0.0547 0.0327  308  GLU B C   
10993 O O   . GLU B 310  ? 0.3403 0.2954 0.2854 -0.0758 -0.0529 0.0356  308  GLU B O   
10994 C CB  . GLU B 310  ? 0.3409 0.2734 0.2726 -0.0654 -0.0601 0.0336  308  GLU B CB  
10995 C CG  . GLU B 310  ? 0.3708 0.2979 0.2941 -0.0670 -0.0624 0.0392  308  GLU B CG  
10996 C CD  . GLU B 310  ? 0.3702 0.2890 0.2909 -0.0605 -0.0658 0.0353  308  GLU B CD  
10997 O OE1 . GLU B 310  ? 0.4125 0.3381 0.3346 -0.0549 -0.0623 0.0308  308  GLU B OE1 
10998 O OE2 . GLU B 310  ? 0.3711 0.2768 0.2886 -0.0612 -0.0721 0.0372  308  GLU B OE2 
10999 N N   . GLU B 311  ? 0.3237 0.2691 0.2690 -0.0639 -0.0550 0.0252  309  GLU B N   
11000 C CA  . GLU B 311  ? 0.3503 0.3009 0.3021 -0.0623 -0.0530 0.0202  309  GLU B CA  
11001 C C   . GLU B 311  ? 0.3350 0.2774 0.2885 -0.0668 -0.0578 0.0205  309  GLU B C   
11002 O O   . GLU B 311  ? 0.3744 0.3039 0.3245 -0.0693 -0.0635 0.0225  309  GLU B O   
11003 C CB  . GLU B 311  ? 0.3463 0.2952 0.3008 -0.0543 -0.0525 0.0127  309  GLU B CB  
11004 C CG  . GLU B 311  ? 0.3637 0.3211 0.3173 -0.0496 -0.0478 0.0114  309  GLU B CG  
11005 C CD  . GLU B 311  ? 0.3983 0.3490 0.3460 -0.0479 -0.0504 0.0133  309  GLU B CD  
11006 O OE1 . GLU B 311  ? 0.3747 0.3147 0.3188 -0.0505 -0.0556 0.0163  309  GLU B OE1 
11007 O OE2 . GLU B 311  ? 0.4486 0.4046 0.3950 -0.0439 -0.0474 0.0117  309  GLU B OE2 
11008 N N   . ALA B 312  ? 0.2888 0.2380 0.2474 -0.0677 -0.0557 0.0181  310  ALA B N   
11009 C CA  . ALA B 312  ? 0.3413 0.2831 0.3010 -0.0723 -0.0603 0.0181  310  ALA B CA  
11010 C C   . ALA B 312  ? 0.3610 0.2872 0.3193 -0.0685 -0.0660 0.0129  310  ALA B C   
11011 O O   . ALA B 312  ? 0.3179 0.2325 0.2742 -0.0725 -0.0718 0.0142  310  ALA B O   
11012 C CB  . ALA B 312  ? 0.3329 0.2851 0.2981 -0.0730 -0.0572 0.0158  310  ALA B CB  
11013 N N   . ASP B 313  ? 0.3202 0.2459 0.2796 -0.0607 -0.0645 0.0071  311  ASP B N   
11014 C CA  . ASP B 313  ? 0.3627 0.2750 0.3216 -0.0566 -0.0695 0.0020  311  ASP B CA  
11015 C C   . ASP B 313  ? 0.3627 0.2625 0.3170 -0.0562 -0.0745 0.0045  311  ASP B C   
11016 O O   . ASP B 313  ? 0.3949 0.2836 0.3489 -0.0519 -0.0787 0.0003  311  ASP B O   
11017 C CB  . ASP B 313  ? 0.3502 0.2671 0.3130 -0.0487 -0.0662 -0.0053 311  ASP B CB  
11018 C CG  . ASP B 313  ? 0.3958 0.3191 0.3590 -0.0442 -0.0627 -0.0054 311  ASP B CG  
11019 O OD1 . ASP B 313  ? 0.3813 0.3048 0.3410 -0.0465 -0.0629 -0.0003 311  ASP B OD1 
11020 O OD2 . ASP B 313  ? 0.3744 0.3023 0.3413 -0.0383 -0.0599 -0.0106 311  ASP B OD2 
11021 N N   . ARG B 314  ? 0.3531 0.2545 0.3037 -0.0606 -0.0744 0.0113  312  ARG B N   
11022 C CA  . ARG B 314  ? 0.3610 0.2499 0.3065 -0.0615 -0.0798 0.0149  312  ARG B CA  
11023 C C   . ARG B 314  ? 0.3652 0.2467 0.3071 -0.0700 -0.0842 0.0216  312  ARG B C   
11024 O O   . ARG B 314  ? 0.3842 0.2534 0.3213 -0.0715 -0.0895 0.0250  312  ARG B O   
11025 C CB  . ARG B 314  ? 0.3556 0.2505 0.2983 -0.0593 -0.0769 0.0176  312  ARG B CB  
11026 C CG  . ARG B 314  ? 0.3625 0.2597 0.3081 -0.0507 -0.0752 0.0111  312  ARG B CG  
11027 C CD  . ARG B 314  ? 0.3743 0.2823 0.3185 -0.0487 -0.0703 0.0125  312  ARG B CD  
11028 N NE  . ARG B 314  ? 0.3330 0.2382 0.2781 -0.0417 -0.0716 0.0082  312  ARG B NE  
11029 C CZ  . ARG B 314  ? 0.4155 0.3274 0.3594 -0.0387 -0.0687 0.0080  312  ARG B CZ  
11030 N NH1 . ARG B 314  ? 0.3488 0.2710 0.2903 -0.0412 -0.0637 0.0112  312  ARG B NH1 
11031 N NH2 . ARG B 314  ? 0.3577 0.2657 0.3029 -0.0329 -0.0710 0.0044  312  ARG B NH2 
11032 N N   . LEU B 315  ? 0.3642 0.2524 0.3083 -0.0760 -0.0824 0.0238  313  LEU B N   
11033 C CA  . LEU B 315  ? 0.4191 0.3022 0.3605 -0.0852 -0.0861 0.0311  313  LEU B CA  
11034 C C   . LEU B 315  ? 0.4376 0.3008 0.3761 -0.0861 -0.0947 0.0300  313  LEU B C   
11035 O O   . LEU B 315  ? 0.4190 0.2716 0.3526 -0.0897 -0.0995 0.0355  313  LEU B O   
11036 C CB  . LEU B 315  ? 0.3690 0.2636 0.3148 -0.0908 -0.0830 0.0327  313  LEU B CB  
11037 C CG  . LEU B 315  ? 0.4207 0.3180 0.3654 -0.1011 -0.0841 0.0418  313  LEU B CG  
11038 C CD1 . LEU B 315  ? 0.3845 0.2973 0.3353 -0.1050 -0.0797 0.0426  313  LEU B CD1 
11039 C CD2 . LEU B 315  ? 0.4150 0.2943 0.3563 -0.1069 -0.0927 0.0446  313  LEU B CD2 
11040 N N   . GLU B 316  ? 0.3882 0.2456 0.3291 -0.0827 -0.0968 0.0229  314  GLU B N   
11041 C CA  . GLU B 316  ? 0.4499 0.2879 0.3877 -0.0836 -0.1050 0.0214  314  GLU B CA  
11042 C C   . GLU B 316  ? 0.4790 0.3048 0.4135 -0.0774 -0.1089 0.0199  314  GLU B C   
11043 O O   . GLU B 316  ? 0.4985 0.3083 0.4286 -0.0802 -0.1159 0.0229  314  GLU B O   
11044 C CB  . GLU B 316  ? 0.4578 0.2932 0.3983 -0.0809 -0.1060 0.0138  314  GLU B CB  
11045 C CG  . GLU B 316  ? 0.4392 0.2841 0.3823 -0.0886 -0.1041 0.0166  314  GLU B CG  
11046 C CD  . GLU B 316  ? 0.4812 0.3224 0.4256 -0.0873 -0.1060 0.0099  314  GLU B CD  
11047 O OE1 . GLU B 316  ? 0.5271 0.3515 0.4683 -0.0852 -0.1123 0.0057  314  GLU B OE1 
11048 O OE2 . GLU B 316  ? 0.4730 0.3281 0.4215 -0.0884 -0.1013 0.0088  314  GLU B OE2 
11049 N N   . LEU B 317  ? 0.4730 0.3059 0.4096 -0.0695 -0.1047 0.0158  315  LEU B N   
11050 C CA  . LEU B 317  ? 0.4810 0.3041 0.4151 -0.0638 -0.1083 0.0149  315  LEU B CA  
11051 C C   . LEU B 317  ? 0.4626 0.2808 0.3911 -0.0694 -0.1112 0.0238  315  LEU B C   
11052 O O   . LEU B 317  ? 0.4533 0.2560 0.3779 -0.0688 -0.1180 0.0254  315  LEU B O   
11053 C CB  . LEU B 317  ? 0.4382 0.2724 0.3762 -0.0556 -0.1030 0.0100  315  LEU B CB  
11054 C CG  . LEU B 317  ? 0.4729 0.2996 0.4093 -0.0495 -0.1063 0.0092  315  LEU B CG  
11055 C CD1 . LEU B 317  ? 0.4958 0.3053 0.4316 -0.0454 -0.1134 0.0052  315  LEU B CD1 
11056 C CD2 . LEU B 317  ? 0.4364 0.2754 0.3774 -0.0424 -0.1008 0.0045  315  LEU B CD2 
11057 N N   . SER B 318  ? 0.4237 0.2550 0.3515 -0.0748 -0.1062 0.0299  316  SER B N   
11058 C CA  . SER B 318  ? 0.4485 0.2765 0.3702 -0.0803 -0.1082 0.0387  316  SER B CA  
11059 C C   . SER B 318  ? 0.4809 0.2944 0.3990 -0.0882 -0.1153 0.0442  316  SER B C   
11060 O O   . SER B 318  ? 0.5118 0.3156 0.4242 -0.0911 -0.1198 0.0504  316  SER B O   
11061 C CB  . SER B 318  ? 0.4241 0.2701 0.3457 -0.0843 -0.1008 0.0438  316  SER B CB  
11062 O OG  . SER B 318  ? 0.4400 0.2937 0.3646 -0.0913 -0.0984 0.0464  316  SER B OG  
11063 N N   . LEU B 319  ? 0.4423 0.2537 0.3634 -0.0918 -0.1167 0.0421  317  LEU B N   
11064 C CA  . LEU B 319  ? 0.4470 0.2435 0.3646 -0.0996 -0.1240 0.0470  317  LEU B CA  
11065 C C   . LEU B 319  ? 0.4754 0.2505 0.3893 -0.0953 -0.1324 0.0445  317  LEU B C   
11066 O O   . LEU B 319  ? 0.5447 0.3057 0.4537 -0.1011 -0.1391 0.0506  317  LEU B O   
11067 C CB  . LEU B 319  ? 0.4786 0.2770 0.4001 -0.1040 -0.1243 0.0445  317  LEU B CB  
11068 C CG  . LEU B 319  ? 0.4887 0.3073 0.4146 -0.1097 -0.1172 0.0481  317  LEU B CG  
11069 C CD1 . LEU B 319  ? 0.4986 0.3166 0.4281 -0.1131 -0.1189 0.0446  317  LEU B CD1 
11070 C CD2 . LEU B 319  ? 0.4648 0.2877 0.3879 -0.1191 -0.1168 0.0593  317  LEU B CD2 
11071 N N   . ASP B 320  ? 0.5215 0.2937 0.4377 -0.0850 -0.1324 0.0356  318  ASP B N   
11072 C CA  . ASP B 320  ? 0.5565 0.3095 0.4697 -0.0798 -0.1400 0.0330  318  ASP B CA  
11073 C C   . ASP B 320  ? 0.5544 0.3028 0.4627 -0.0798 -0.1424 0.0394  318  ASP B C   
11074 O O   . ASP B 320  ? 0.5776 0.3080 0.4815 -0.0799 -0.1503 0.0416  318  ASP B O   
11075 C CB  . ASP B 320  ? 0.5264 0.2802 0.4441 -0.0686 -0.1385 0.0223  318  ASP B CB  
11076 C CG  . ASP B 320  ? 0.5304 0.2818 0.4506 -0.0682 -0.1389 0.0157  318  ASP B CG  
11077 O OD1 . ASP B 320  ? 0.6063 0.3418 0.5231 -0.0722 -0.1458 0.0165  318  ASP B OD1 
11078 O OD2 . ASP B 320  ? 0.5392 0.3041 0.4643 -0.0641 -0.1326 0.0099  318  ASP B OD2 
11079 N N   . LEU B 321  ? 0.5121 0.2761 0.4207 -0.0794 -0.1361 0.0424  319  LEU B N   
11080 C CA  . LEU B 321  ? 0.5290 0.2892 0.4318 -0.0803 -0.1383 0.0491  319  LEU B CA  
11081 C C   . LEU B 321  ? 0.5296 0.2849 0.4267 -0.0914 -0.1411 0.0596  319  LEU B C   
11082 O O   . LEU B 321  ? 0.5603 0.3015 0.4514 -0.0934 -0.1476 0.0651  319  LEU B O   
11083 C CB  . LEU B 321  ? 0.4657 0.2435 0.3696 -0.0766 -0.1308 0.0488  319  LEU B CB  
11084 C CG  . LEU B 321  ? 0.5259 0.3054 0.4339 -0.0655 -0.1300 0.0404  319  LEU B CG  
11085 C CD1 . LEU B 321  ? 0.5163 0.3084 0.4317 -0.0617 -0.1237 0.0325  319  LEU B CD1 
11086 C CD2 . LEU B 321  ? 0.5363 0.3226 0.4411 -0.0628 -0.1279 0.0431  319  LEU B CD2 
11087 N N   . LEU B 322  ? 0.5106 0.2776 0.4098 -0.0989 -0.1364 0.0628  320  LEU B N   
11088 C CA  . LEU B 322  ? 0.5286 0.2926 0.4236 -0.1103 -0.1388 0.0731  320  LEU B CA  
11089 C C   . LEU B 322  ? 0.5483 0.2895 0.4402 -0.1137 -0.1488 0.0746  320  LEU B C   
11090 O O   . LEU B 322  ? 0.5293 0.2602 0.4152 -0.1201 -0.1538 0.0832  320  LEU B O   
11091 C CB  . LEU B 322  ? 0.5239 0.3045 0.4236 -0.1170 -0.1325 0.0750  320  LEU B CB  
11092 C CG  . LEU B 322  ? 0.5643 0.3452 0.4609 -0.1293 -0.1339 0.0863  320  LEU B CG  
11093 C CD1 . LEU B 322  ? 0.5691 0.3544 0.4593 -0.1309 -0.1317 0.0943  320  LEU B CD1 
11094 C CD2 . LEU B 322  ? 0.5225 0.3204 0.4251 -0.1354 -0.1280 0.0877  320  LEU B CD2 
11095 N N   . GLU B 323  ? 0.5556 0.2881 0.4511 -0.1093 -0.1520 0.0661  321  GLU B N   
11096 C CA  . GLU B 323  ? 0.5901 0.2997 0.4825 -0.1117 -0.1619 0.0663  321  GLU B CA  
11097 C C   . GLU B 323  ? 0.6234 0.3162 0.5099 -0.1078 -0.1687 0.0687  321  GLU B C   
11098 O O   . GLU B 323  ? 0.6574 0.3348 0.5385 -0.1145 -0.1759 0.0759  321  GLU B O   
11099 C CB  . GLU B 323  ? 0.6173 0.3218 0.5139 -0.1053 -0.1632 0.0552  321  GLU B CB  
11100 C CG  . GLU B 323  ? 0.6805 0.3603 0.5736 -0.1061 -0.1735 0.0535  321  GLU B CG  
11101 C CD  . GLU B 323  ? 0.7054 0.3808 0.5982 -0.1170 -0.1767 0.0571  321  GLU B CD  
11102 O OE1 . GLU B 323  ? 0.6975 0.3894 0.5948 -0.1213 -0.1707 0.0569  321  GLU B OE1 
11103 O OE2 . GLU B 323  ? 0.7750 0.4296 0.6630 -0.1215 -0.1859 0.0601  321  GLU B OE2 
11104 N N   . VAL B 324  ? 0.6072 0.3031 0.4950 -0.0973 -0.1668 0.0632  322  VAL B N   
11105 C CA  . VAL B 324  ? 0.6306 0.3106 0.5135 -0.0927 -0.1738 0.0648  322  VAL B CA  
11106 C C   . VAL B 324  ? 0.6232 0.3040 0.4993 -0.0998 -0.1744 0.0764  322  VAL B C   
11107 O O   . VAL B 324  ? 0.6650 0.3282 0.5351 -0.1025 -0.1824 0.0821  322  VAL B O   
11108 C CB  . VAL B 324  ? 0.6366 0.3214 0.5235 -0.0799 -0.1715 0.0562  322  VAL B CB  
11109 C CG1 . VAL B 324  ? 0.5857 0.2564 0.4679 -0.0755 -0.1784 0.0589  322  VAL B CG1 
11110 C CG2 . VAL B 324  ? 0.6462 0.3275 0.5388 -0.0729 -0.1718 0.0452  322  VAL B CG2 
11111 N N   . LEU B 325  ? 0.5937 0.2948 0.4704 -0.1025 -0.1660 0.0799  323  LEU B N   
11112 C CA  . LEU B 325  ? 0.5932 0.2968 0.4628 -0.1088 -0.1656 0.0907  323  LEU B CA  
11113 C C   . LEU B 325  ? 0.6035 0.2976 0.4688 -0.1210 -0.1703 0.1004  323  LEU B C   
11114 O O   . LEU B 325  ? 0.6360 0.3198 0.4939 -0.1254 -0.1752 0.1090  323  LEU B O   
11115 C CB  . LEU B 325  ? 0.5749 0.3025 0.4458 -0.1092 -0.1552 0.0917  323  LEU B CB  
11116 C CG  . LEU B 325  ? 0.5651 0.3020 0.4395 -0.0979 -0.1510 0.0832  323  LEU B CG  
11117 C CD1 . LEU B 325  ? 0.5300 0.2900 0.4067 -0.0982 -0.1406 0.0828  323  LEU B CD1 
11118 C CD2 . LEU B 325  ? 0.5626 0.2898 0.4311 -0.0930 -0.1560 0.0854  323  LEU B CD2 
11119 N N   . CYS B 326  ? 0.5755 0.2725 0.4454 -0.1269 -0.1691 0.0993  324  CYS B N   
11120 C CA  . CYS B 326  ? 0.6081 0.2978 0.4748 -0.1394 -0.1733 0.1091  324  CYS B CA  
11121 C C   . CYS B 326  ? 0.6700 0.3322 0.5324 -0.1404 -0.1851 0.1100  324  CYS B C   
11122 O O   . CYS B 326  ? 0.6233 0.2780 0.4812 -0.1492 -0.1896 0.1192  324  CYS B O   
11123 C CB  . CYS B 326  ? 0.5981 0.3004 0.4714 -0.1457 -0.1687 0.1080  324  CYS B CB  
11124 S SG  . CYS B 326  ? 0.6604 0.3942 0.5370 -0.1483 -0.1556 0.1114  324  CYS B SG  
11125 N N   . LEU B 327  ? 0.6154 0.2653 0.4799 -0.1304 -0.1894 0.1000  325  LEU B N   
11126 C CA  . LEU B 327  ? 0.6600 0.2883 0.5214 -0.1280 -0.1992 0.0984  325  LEU B CA  
11127 C C   . LEU B 327  ? 0.6717 0.2903 0.5281 -0.1211 -0.2036 0.0998  325  LEU B C   
11128 O O   . LEU B 327  ? 0.6806 0.2845 0.5346 -0.1183 -0.2111 0.0988  325  LEU B O   
11129 C CB  . LEU B 327  ? 0.6599 0.2817 0.5264 -0.1204 -0.2012 0.0863  325  LEU B CB  
11130 C CG  . LEU B 327  ? 0.7076 0.3382 0.5787 -0.1268 -0.1978 0.0844  325  LEU B CG  
11131 C CD1 . LEU B 327  ? 0.7317 0.3576 0.6071 -0.1182 -0.1987 0.0719  325  LEU B CD1 
11132 C CD2 . LEU B 327  ? 0.7432 0.3708 0.6121 -0.1376 -0.2015 0.0923  325  LEU B CD2 
11133 N N   . ASP B 328  ? 0.6543 0.2815 0.5091 -0.1182 -0.1991 0.1020  326  ASP B N   
11134 C CA  . ASP B 328  ? 0.6753 0.2941 0.5255 -0.1114 -0.2034 0.1033  326  ASP B CA  
11135 C C   . ASP B 328  ? 0.6848 0.2998 0.5276 -0.1192 -0.2069 0.1143  326  ASP B C   
11136 O O   . ASP B 328  ? 0.6949 0.3212 0.5337 -0.1269 -0.2020 0.1231  326  ASP B O   
11137 C CB  . ASP B 328  ? 0.6268 0.2657 0.4795 -0.1043 -0.1950 0.0997  326  ASP B CB  
11138 C CG  . ASP B 328  ? 0.7348 0.3657 0.5840 -0.0958 -0.1996 0.0992  326  ASP B CG  
11139 O OD1 . ASP B 328  ? 0.7069 0.3183 0.5500 -0.0973 -0.2087 0.1046  326  ASP B OD1 
11140 O OD2 . ASP B 328  ? 0.7708 0.4150 0.6236 -0.0877 -0.1944 0.0935  326  ASP B OD2 
11141 N N   . GLY B 329  ? 0.6810 0.2805 0.5216 -0.1170 -0.2150 0.1138  327  GLY B N   
11142 C CA  . GLY B 329  ? 0.6862 0.2803 0.5200 -0.1242 -0.2192 0.1237  327  GLY B CA  
11143 C C   . GLY B 329  ? 0.6964 0.2954 0.5237 -0.1237 -0.2176 0.1305  327  GLY B C   
11144 O O   . GLY B 329  ? 0.7379 0.3365 0.5591 -0.1314 -0.2190 0.1400  327  GLY B O   
11145 N N   . ASP B 330  ? 0.6775 0.2814 0.5058 -0.1150 -0.2149 0.1260  328  ASP B N   
11146 C CA  . ASP B 330  ? 0.7110 0.3214 0.5325 -0.1148 -0.2128 0.1324  328  ASP B CA  
11147 C C   . ASP B 330  ? 0.7286 0.3553 0.5464 -0.1250 -0.2049 0.1411  328  ASP B C   
11148 O O   . ASP B 330  ? 0.7323 0.3638 0.5426 -0.1284 -0.2036 0.1490  328  ASP B O   
11149 C CB  . ASP B 330  ? 0.7284 0.3416 0.5523 -0.1033 -0.2116 0.1253  328  ASP B CB  
11150 C CG  . ASP B 330  ? 0.8128 0.4117 0.6395 -0.0928 -0.2195 0.1183  328  ASP B CG  
11151 O OD1 . ASP B 330  ? 0.8434 0.4298 0.6682 -0.0947 -0.2261 0.1202  328  ASP B OD1 
11152 O OD2 . ASP B 330  ? 0.7615 0.3621 0.5926 -0.0826 -0.2192 0.1110  328  ASP B OD2 
11153 N N   . LEU B 331  ? 0.6964 0.3324 0.5195 -0.1299 -0.1993 0.1396  329  LEU B N   
11154 C CA  . LEU B 331  ? 0.6796 0.3329 0.5007 -0.1394 -0.1912 0.1474  329  LEU B CA  
11155 C C   . LEU B 331  ? 0.6911 0.3445 0.5125 -0.1507 -0.1923 0.1542  329  LEU B C   
11156 O O   . LEU B 331  ? 0.6634 0.3320 0.4862 -0.1588 -0.1855 0.1592  329  LEU B O   
11157 C CB  . LEU B 331  ? 0.6505 0.3230 0.4803 -0.1361 -0.1820 0.1391  329  LEU B CB  
11158 C CG  . LEU B 331  ? 0.6461 0.3254 0.4798 -0.1231 -0.1790 0.1285  329  LEU B CG  
11159 C CD1 . LEU B 331  ? 0.5940 0.2897 0.4374 -0.1198 -0.1711 0.1193  329  LEU B CD1 
11160 C CD2 . LEU B 331  ? 0.6752 0.3645 0.5018 -0.1211 -0.1753 0.1327  329  LEU B CD2 
11161 N N   . SER B 332  ? 0.7278 0.3650 0.5481 -0.1512 -0.2008 0.1545  330  SER B N   
11162 C CA  . SER B 332  ? 0.6908 0.3255 0.5116 -0.1612 -0.2034 0.1602  330  SER B CA  
11163 C C   . SER B 332  ? 0.7463 0.3963 0.5633 -0.1716 -0.1973 0.1715  330  SER B C   
11164 O O   . SER B 332  ? 0.7798 0.4319 0.5894 -0.1717 -0.1965 0.1774  330  SER B O   
11165 C CB  . SER B 332  ? 0.7238 0.3383 0.5413 -0.1592 -0.2137 0.1602  330  SER B CB  
11166 O OG  . SER B 332  ? 0.7756 0.3868 0.5930 -0.1691 -0.2168 0.1664  330  SER B OG  
11167 N N   . GLY B 333  ? 0.7036 0.3650 0.5257 -0.1801 -0.1930 0.1742  331  GLY B N   
11168 C CA  . GLY B 333  ? 0.7495 0.4264 0.5694 -0.1902 -0.1872 0.1846  331  GLY B CA  
11169 C C   . GLY B 333  ? 0.7633 0.4618 0.5826 -0.1903 -0.1764 0.1869  331  GLY B C   
11170 O O   . GLY B 333  ? 0.7380 0.4526 0.5572 -0.1984 -0.1702 0.1947  331  GLY B O   
11171 N N   . TRP B 334  ? 0.7167 0.4164 0.5354 -0.1812 -0.1739 0.1802  332  TRP B N   
11172 C CA  . TRP B 334  ? 0.7006 0.4200 0.5181 -0.1801 -0.1638 0.1813  332  TRP B CA  
11173 C C   . TRP B 334  ? 0.6900 0.4232 0.5167 -0.1838 -0.1578 0.1787  332  TRP B C   
11174 O O   . TRP B 334  ? 0.7327 0.4596 0.5655 -0.1794 -0.1598 0.1703  332  TRP B O   
11175 C CB  . TRP B 334  ? 0.6572 0.3711 0.4708 -0.1688 -0.1646 0.1749  332  TRP B CB  
11176 C CG  . TRP B 334  ? 0.6659 0.4028 0.4807 -0.1642 -0.1537 0.1713  332  TRP B CG  
11177 C CD1 . TRP B 334  ? 0.6594 0.4129 0.4682 -0.1680 -0.1462 0.1785  332  TRP B CD1 
11178 C CD2 . TRP B 334  ? 0.5986 0.3453 0.4214 -0.1541 -0.1490 0.1587  332  TRP B CD2 
11179 N NE1 . TRP B 334  ? 0.6424 0.4147 0.4549 -0.1606 -0.1373 0.1707  332  TRP B NE1 
11180 C CE2 . TRP B 334  ? 0.5783 0.3467 0.3994 -0.1523 -0.1389 0.1588  332  TRP B CE2 
11181 C CE3 . TRP B 334  ? 0.6578 0.3970 0.4886 -0.1464 -0.1521 0.1474  332  TRP B CE3 
11182 C CZ2 . TRP B 334  ? 0.5569 0.3387 0.3843 -0.1434 -0.1324 0.1483  332  TRP B CZ2 
11183 C CZ3 . TRP B 334  ? 0.5959 0.3495 0.4331 -0.1378 -0.1453 0.1373  332  TRP B CZ3 
11184 C CH2 . TRP B 334  ? 0.5821 0.3563 0.4176 -0.1366 -0.1358 0.1380  332  TRP B CH2 
11185 N N   . ASN B 335  ? 0.6450 0.3978 0.4729 -0.1916 -0.1501 0.1857  333  ASN B N   
11186 C CA  . ASN B 335  ? 0.6461 0.4151 0.4830 -0.1953 -0.1435 0.1840  333  ASN B CA  
11187 C C   . ASN B 335  ? 0.6189 0.4083 0.4570 -0.1884 -0.1332 0.1791  333  ASN B C   
11188 O O   . ASN B 335  ? 0.6135 0.4224 0.4584 -0.1912 -0.1254 0.1790  333  ASN B O   
11189 C CB  . ASN B 335  ? 0.6706 0.4526 0.5110 -0.2061 -0.1405 0.1924  333  ASN B CB  
11190 C CG  . ASN B 335  ? 0.6867 0.4524 0.5285 -0.2113 -0.1500 0.1943  333  ASN B CG  
11191 O OD1 . ASN B 335  ? 0.6918 0.4418 0.5371 -0.2084 -0.1570 0.1873  333  ASN B OD1 
11192 N ND2 . ASN B 335  ? 0.6832 0.4519 0.5216 -0.2186 -0.1504 0.2035  333  ASN B ND2 
11193 N N   . GLY B 336  ? 0.6377 0.4245 0.4703 -0.1783 -0.1328 0.1739  334  GLY B N   
11194 C CA  . GLY B 336  ? 0.5646 0.3718 0.3981 -0.1712 -0.1229 0.1687  334  GLY B CA  
11195 C C   . GLY B 336  ? 0.5739 0.3854 0.4162 -0.1615 -0.1205 0.1553  334  GLY B C   
11196 O O   . GLY B 336  ? 0.5459 0.3736 0.3893 -0.1553 -0.1126 0.1504  334  GLY B O   
11197 N N   . MET B 337  ? 0.6063 0.4037 0.4546 -0.1597 -0.1271 0.1491  335  MET B N   
11198 C CA  . MET B 337  ? 0.5599 0.3623 0.4166 -0.1507 -0.1244 0.1367  335  MET B CA  
11199 C C   . MET B 337  ? 0.6188 0.4424 0.4833 -0.1538 -0.1158 0.1357  335  MET B C   
11200 O O   . MET B 337  ? 0.5689 0.3950 0.4369 -0.1632 -0.1162 0.1414  335  MET B O   
11201 C CB  . MET B 337  ? 0.6421 0.4253 0.5030 -0.1487 -0.1331 0.1307  335  MET B CB  
11202 C CG  . MET B 337  ? 0.6071 0.3950 0.4762 -0.1391 -0.1304 0.1178  335  MET B CG  
11203 S SD  . MET B 337  ? 0.7716 0.5507 0.6379 -0.1260 -0.1332 0.1097  335  MET B SD  
11204 C CE  . MET B 337  ? 0.6696 0.4716 0.5342 -0.1219 -0.1226 0.1092  335  MET B CE  
11205 N N   . GLY B 338  ? 0.5612 0.3999 0.4287 -0.1459 -0.1083 0.1286  336  GLY B N   
11206 C CA  . GLY B 338  ? 0.5089 0.3681 0.3839 -0.1472 -0.0999 0.1269  336  GLY B CA  
11207 C C   . GLY B 338  ? 0.5085 0.3697 0.3917 -0.1391 -0.0986 0.1151  336  GLY B C   
11208 O O   . GLY B 338  ? 0.4897 0.3425 0.3721 -0.1304 -0.1012 0.1076  336  GLY B O   
11209 N N   . PHE B 339  ? 0.4800 0.3534 0.3714 -0.1422 -0.0946 0.1136  337  PHE B N   
11210 C CA  . PHE B 339  ? 0.4582 0.3335 0.3574 -0.1356 -0.0936 0.1031  337  PHE B CA  
11211 C C   . PHE B 339  ? 0.4528 0.3494 0.3591 -0.1376 -0.0855 0.1030  337  PHE B C   
11212 O O   . PHE B 339  ? 0.4272 0.3301 0.3360 -0.1467 -0.0849 0.1100  337  PHE B O   
11213 C CB  . PHE B 339  ? 0.4439 0.3016 0.3459 -0.1377 -0.1021 0.1002  337  PHE B CB  
11214 C CG  . PHE B 339  ? 0.4545 0.3106 0.3624 -0.1296 -0.1021 0.0888  337  PHE B CG  
11215 C CD1 . PHE B 339  ? 0.4601 0.3053 0.3660 -0.1204 -0.1052 0.0817  337  PHE B CD1 
11216 C CD2 . PHE B 339  ? 0.4455 0.3113 0.3610 -0.1311 -0.0992 0.0854  337  PHE B CD2 
11217 C CE1 . PHE B 339  ? 0.4649 0.3094 0.3765 -0.1130 -0.1048 0.0715  337  PHE B CE1 
11218 C CE2 . PHE B 339  ? 0.4797 0.3439 0.4000 -0.1238 -0.0992 0.0752  337  PHE B CE2 
11219 C CZ  . PHE B 339  ? 0.4494 0.3033 0.3677 -0.1148 -0.1017 0.0684  337  PHE B CZ  
11220 N N   . VAL B 340  ? 0.4095 0.3168 0.3192 -0.1293 -0.0797 0.0953  338  VAL B N   
11221 C CA  . VAL B 340  ? 0.4359 0.3633 0.3524 -0.1295 -0.0720 0.0942  338  VAL B CA  
11222 C C   . VAL B 340  ? 0.4162 0.3417 0.3409 -0.1293 -0.0742 0.0881  338  VAL B C   
11223 O O   . VAL B 340  ? 0.4264 0.3398 0.3516 -0.1235 -0.0784 0.0805  338  VAL B O   
11224 C CB  . VAL B 340  ? 0.3895 0.3285 0.3048 -0.1206 -0.0648 0.0892  338  VAL B CB  
11225 C CG1 . VAL B 340  ? 0.4158 0.3746 0.3384 -0.1202 -0.0573 0.0877  338  VAL B CG1 
11226 C CG2 . VAL B 340  ? 0.4088 0.3497 0.3148 -0.1209 -0.0627 0.0953  338  VAL B CG2 
11227 N N   . VAL B 341  ? 0.3840 0.3220 0.3150 -0.1354 -0.0713 0.0913  339  VAL B N   
11228 C CA  . VAL B 341  ? 0.3747 0.3150 0.3135 -0.1347 -0.0720 0.0853  339  VAL B CA  
11229 C C   . VAL B 341  ? 0.3587 0.3214 0.3036 -0.1330 -0.0633 0.0848  339  VAL B C   
11230 O O   . VAL B 341  ? 0.4033 0.3798 0.3483 -0.1372 -0.0583 0.0919  339  VAL B O   
11231 C CB  . VAL B 341  ? 0.4073 0.3388 0.3485 -0.1443 -0.0788 0.0895  339  VAL B CB  
11232 C CG1 . VAL B 341  ? 0.4532 0.3826 0.4005 -0.1421 -0.0809 0.0817  339  VAL B CG1 
11233 C CG2 . VAL B 341  ? 0.4308 0.3409 0.3651 -0.1467 -0.0870 0.0920  339  VAL B CG2 
11234 N N   . GLN B 342  ? 0.4018 0.3680 0.3516 -0.1267 -0.0614 0.0764  340  GLN B N   
11235 C CA  . GLN B 342  ? 0.3614 0.3471 0.3165 -0.1230 -0.0535 0.0744  340  GLN B CA  
11236 C C   . GLN B 342  ? 0.3891 0.3832 0.3525 -0.1284 -0.0538 0.0753  340  GLN B C   
11237 O O   . GLN B 342  ? 0.3323 0.3185 0.2984 -0.1274 -0.0579 0.0696  340  GLN B O   
11238 C CB  . GLN B 342  ? 0.3593 0.3436 0.3142 -0.1123 -0.0512 0.0649  340  GLN B CB  
11239 C CG  . GLN B 342  ? 0.3518 0.3297 0.2992 -0.1067 -0.0507 0.0639  340  GLN B CG  
11240 C CD  . GLN B 342  ? 0.3473 0.3152 0.2941 -0.0981 -0.0528 0.0548  340  GLN B CD  
11241 O OE1 . GLN B 342  ? 0.3588 0.3156 0.3075 -0.0979 -0.0580 0.0507  340  GLN B OE1 
11242 N NE2 . GLN B 342  ? 0.3195 0.2919 0.2640 -0.0910 -0.0487 0.0515  340  GLN B NE2 
11243 N N   . ALA B 343  ? 0.3555 0.3661 0.3227 -0.1340 -0.0493 0.0824  341  ALA B N   
11244 C CA  . ALA B 343  ? 0.3510 0.3714 0.3268 -0.1398 -0.0497 0.0842  341  ALA B CA  
11245 C C   . ALA B 343  ? 0.3186 0.3471 0.3000 -0.1329 -0.0465 0.0764  341  ALA B C   
11246 O O   . ALA B 343  ? 0.3473 0.3779 0.3347 -0.1365 -0.0492 0.0754  341  ALA B O   
11247 C CB  . ALA B 343  ? 0.3266 0.3652 0.3060 -0.1464 -0.0448 0.0936  341  ALA B CB  
11248 N N   . TYR B 344  ? 0.3171 0.3495 0.2965 -0.1234 -0.0413 0.0709  342  TYR B N   
11249 C CA  . TYR B 344  ? 0.3204 0.3591 0.3050 -0.1174 -0.0390 0.0638  342  TYR B CA  
11250 C C   . TYR B 344  ? 0.3355 0.3582 0.3191 -0.1150 -0.0451 0.0565  342  TYR B C   
11251 O O   . TYR B 344  ? 0.3271 0.3537 0.3147 -0.1109 -0.0440 0.0508  342  TYR B O   
11252 C CB  . TYR B 344  ? 0.2948 0.3425 0.2781 -0.1083 -0.0318 0.0600  342  TYR B CB  
11253 C CG  . TYR B 344  ? 0.2901 0.3258 0.2666 -0.1007 -0.0324 0.0543  342  TYR B CG  
11254 C CD1 . TYR B 344  ? 0.3067 0.3242 0.2780 -0.1013 -0.0387 0.0529  342  TYR B CD1 
11255 C CD2 . TYR B 344  ? 0.2660 0.3092 0.2418 -0.0927 -0.0266 0.0503  342  TYR B CD2 
11256 C CE1 . TYR B 344  ? 0.3158 0.3240 0.2819 -0.0941 -0.0390 0.0478  342  TYR B CE1 
11257 C CE2 . TYR B 344  ? 0.3196 0.3534 0.2900 -0.0861 -0.0271 0.0455  342  TYR B CE2 
11258 C CZ  . TYR B 344  ? 0.3112 0.3281 0.2771 -0.0869 -0.0332 0.0443  342  TYR B CZ  
11259 O OH  . TYR B 344  ? 0.3194 0.3285 0.2808 -0.0802 -0.0336 0.0397  342  TYR B OH  
11260 N N   . GLY B 345  ? 0.3717 0.3768 0.3500 -0.1175 -0.0515 0.0568  343  GLY B N   
11261 C CA  . GLY B 345  ? 0.3673 0.3567 0.3441 -0.1148 -0.0572 0.0498  343  GLY B CA  
11262 C C   . GLY B 345  ? 0.3430 0.3276 0.3227 -0.1225 -0.0632 0.0513  343  GLY B C   
11263 O O   . GLY B 345  ? 0.3243 0.3098 0.3047 -0.1313 -0.0657 0.0588  343  GLY B O   
11264 N N   . LYS B 346  ? 0.3329 0.3122 0.3138 -0.1192 -0.0657 0.0442  344  LYS B N   
11265 C CA  . LYS B 346  ? 0.3206 0.2953 0.3039 -0.1259 -0.0716 0.0445  344  LYS B CA  
11266 C C   . LYS B 346  ? 0.3664 0.3213 0.3443 -0.1310 -0.0798 0.0462  344  LYS B C   
11267 O O   . LYS B 346  ? 0.3606 0.3110 0.3398 -0.1389 -0.0853 0.0490  344  LYS B O   
11268 C CB  . LYS B 346  ? 0.3305 0.3043 0.3153 -0.1204 -0.0718 0.0360  344  LYS B CB  
11269 C CG  . LYS B 346  ? 0.3243 0.3164 0.3142 -0.1151 -0.0642 0.0342  344  LYS B CG  
11270 C CD  . LYS B 346  ? 0.3689 0.3599 0.3598 -0.1101 -0.0647 0.0264  344  LYS B CD  
11271 C CE  . LYS B 346  ? 0.3532 0.3633 0.3505 -0.1082 -0.0588 0.0267  344  LYS B CE  
11272 N NZ  . LYS B 346  ? 0.3430 0.3524 0.3402 -0.1015 -0.0579 0.0190  344  LYS B NZ  
11273 N N   . ARG B 347  ? 0.3705 0.3132 0.3425 -0.1267 -0.0811 0.0448  345  ARG B N   
11274 C CA  . ARG B 347  ? 0.4101 0.3327 0.3767 -0.1306 -0.0892 0.0459  345  ARG B CA  
11275 C C   . ARG B 347  ? 0.3955 0.3177 0.3605 -0.1389 -0.0907 0.0560  345  ARG B C   
11276 O O   . ARG B 347  ? 0.4409 0.3465 0.4017 -0.1437 -0.0980 0.0584  345  ARG B O   
11277 C CB  . ARG B 347  ? 0.3817 0.2905 0.3431 -0.1215 -0.0906 0.0392  345  ARG B CB  
11278 C CG  . ARG B 347  ? 0.3550 0.2611 0.3174 -0.1144 -0.0906 0.0294  345  ARG B CG  
11279 C CD  . ARG B 347  ? 0.3425 0.2409 0.3016 -0.1044 -0.0897 0.0233  345  ARG B CD  
11280 N NE  . ARG B 347  ? 0.3590 0.2713 0.3200 -0.0994 -0.0821 0.0239  345  ARG B NE  
11281 C CZ  . ARG B 347  ? 0.3586 0.2671 0.3173 -0.0919 -0.0807 0.0204  345  ARG B CZ  
11282 N NH1 . ARG B 347  ? 0.3378 0.2301 0.2929 -0.0882 -0.0859 0.0164  345  ARG B NH1 
11283 N NH2 . ARG B 347  ? 0.3482 0.2695 0.3085 -0.0880 -0.0741 0.0210  345  ARG B NH2 
11284 N N   . CYS B 348  ? 0.3737 0.3137 0.3417 -0.1407 -0.0839 0.0619  346  CYS B N   
11285 C CA  . CYS B 348  ? 0.4319 0.3733 0.3974 -0.1472 -0.0837 0.0715  346  CYS B CA  
11286 C C   . CYS B 348  ? 0.4190 0.3509 0.3843 -0.1585 -0.0912 0.0783  346  CYS B C   
11287 O O   . CYS B 348  ? 0.4057 0.3245 0.3651 -0.1617 -0.0955 0.0827  346  CYS B O   
11288 C CB  . CYS B 348  ? 0.3619 0.3266 0.3318 -0.1475 -0.0748 0.0763  346  CYS B CB  
11289 S SG  . CYS B 348  ? 0.4939 0.4639 0.4600 -0.1542 -0.0725 0.0882  346  CYS B SG  
11290 N N   . PRO B 349  ? 0.3878 0.3249 0.3588 -0.1652 -0.0935 0.0796  347  PRO B N   
11291 C CA  . PRO B 349  ? 0.4759 0.4027 0.4464 -0.1766 -0.1012 0.0864  347  PRO B CA  
11292 C C   . PRO B 349  ? 0.4612 0.3616 0.4249 -0.1757 -0.1105 0.0819  347  PRO B C   
11293 O O   . PRO B 349  ? 0.4740 0.3613 0.4338 -0.1830 -0.1167 0.0881  347  PRO B O   
11294 C CB  . PRO B 349  ? 0.4128 0.3518 0.3916 -0.1825 -0.1016 0.0871  347  PRO B CB  
11295 C CG  . PRO B 349  ? 0.4022 0.3495 0.3836 -0.1728 -0.0968 0.0780  347  PRO B CG  
11296 C CD  . PRO B 349  ? 0.4146 0.3671 0.3930 -0.1633 -0.0895 0.0757  347  PRO B CD  
11297 N N   . PHE B 350  ? 0.4344 0.3262 0.3962 -0.1668 -0.1116 0.0714  348  PHE B N   
11298 C CA  . PHE B 350  ? 0.4633 0.3303 0.4185 -0.1647 -0.1201 0.0665  348  PHE B CA  
11299 C C   . PHE B 350  ? 0.4911 0.3475 0.4399 -0.1598 -0.1204 0.0674  348  PHE B C   
11300 O O   . PHE B 350  ? 0.4763 0.3124 0.4195 -0.1620 -0.1281 0.0683  348  PHE B O   
11301 C CB  . PHE B 350  ? 0.4536 0.3167 0.4090 -0.1564 -0.1205 0.0551  348  PHE B CB  
11302 C CG  . PHE B 350  ? 0.4523 0.3277 0.4138 -0.1602 -0.1194 0.0541  348  PHE B CG  
11303 C CD1 . PHE B 350  ? 0.5466 0.4128 0.5082 -0.1687 -0.1273 0.0554  348  PHE B CD1 
11304 C CD2 . PHE B 350  ? 0.4541 0.3503 0.4213 -0.1556 -0.1110 0.0522  348  PHE B CD2 
11305 C CE1 . PHE B 350  ? 0.5276 0.4055 0.4950 -0.1725 -0.1268 0.0548  348  PHE B CE1 
11306 C CE2 . PHE B 350  ? 0.4592 0.3670 0.4322 -0.1591 -0.1104 0.0516  348  PHE B CE2 
11307 C CZ  . PHE B 350  ? 0.5267 0.4257 0.4999 -0.1676 -0.1183 0.0530  348  PHE B CZ  
11308 N N   . VAL B 351  ? 0.4604 0.3299 0.4097 -0.1534 -0.1124 0.0672  349  VAL B N   
11309 C CA  . VAL B 351  ? 0.4466 0.3078 0.3899 -0.1496 -0.1127 0.0691  349  VAL B CA  
11310 C C   . VAL B 351  ? 0.4926 0.3503 0.4330 -0.1597 -0.1157 0.0804  349  VAL B C   
11311 O O   . VAL B 351  ? 0.4817 0.3225 0.4158 -0.1601 -0.1213 0.0827  349  VAL B O   
11312 C CB  . VAL B 351  ? 0.4417 0.3184 0.3860 -0.1412 -0.1036 0.0668  349  VAL B CB  
11313 C CG1 . VAL B 351  ? 0.4075 0.2758 0.3451 -0.1376 -0.1043 0.0692  349  VAL B CG1 
11314 C CG2 . VAL B 351  ? 0.4378 0.3168 0.3848 -0.1316 -0.1011 0.0561  349  VAL B CG2 
11315 N N   . LEU B 352  ? 0.4635 0.3375 0.4087 -0.1681 -0.1122 0.0880  350  LEU B N   
11316 C CA  . LEU B 352  ? 0.4530 0.3254 0.3962 -0.1787 -0.1147 0.0995  350  LEU B CA  
11317 C C   . LEU B 352  ? 0.5240 0.3751 0.4646 -0.1863 -0.1256 0.1015  350  LEU B C   
11318 O O   . LEU B 352  ? 0.5423 0.3808 0.4775 -0.1915 -0.1305 0.1083  350  LEU B O   
11319 C CB  . LEU B 352  ? 0.4982 0.3944 0.4484 -0.1856 -0.1081 0.1067  350  LEU B CB  
11320 C CG  . LEU B 352  ? 0.4582 0.3745 0.4094 -0.1794 -0.0976 0.1070  350  LEU B CG  
11321 C CD1 . LEU B 352  ? 0.4480 0.3879 0.4068 -0.1856 -0.0914 0.1135  350  LEU B CD1 
11322 C CD2 . LEU B 352  ? 0.4782 0.3883 0.4212 -0.1786 -0.0973 0.1123  350  LEU B CD2 
11323 N N   . ASP B 353  ? 0.5195 0.3656 0.4635 -0.1872 -0.1298 0.0956  351  ASP B N   
11324 C CA  . ASP B 353  ? 0.5428 0.3658 0.4833 -0.1928 -0.1408 0.0954  351  ASP B CA  
11325 C C   . ASP B 353  ? 0.5579 0.3582 0.4899 -0.1862 -0.1462 0.0918  351  ASP B C   
11326 O O   . ASP B 353  ? 0.5434 0.3260 0.4704 -0.1923 -0.1540 0.0972  351  ASP B O   
11327 C CB  . ASP B 353  ? 0.4996 0.3201 0.4434 -0.1915 -0.1437 0.0871  351  ASP B CB  
11328 C CG  . ASP B 353  ? 0.5861 0.4243 0.5381 -0.2007 -0.1418 0.0920  351  ASP B CG  
11329 O OD1 . ASP B 353  ? 0.5789 0.4264 0.5334 -0.2096 -0.1406 0.1025  351  ASP B OD1 
11330 O OD2 . ASP B 353  ? 0.5944 0.4382 0.5503 -0.1980 -0.1411 0.0851  351  ASP B OD2 
11331 N N   . PHE B 354  ? 0.4998 0.3009 0.4306 -0.1738 -0.1422 0.0829  352  PHE B N   
11332 C CA  . PHE B 354  ? 0.5439 0.3255 0.4678 -0.1662 -0.1468 0.0788  352  PHE B CA  
11333 C C   . PHE B 354  ? 0.5689 0.3487 0.4881 -0.1687 -0.1465 0.0876  352  PHE B C   
11334 O O   . PHE B 354  ? 0.5921 0.3514 0.5051 -0.1697 -0.1542 0.0898  352  PHE B O   
11335 C CB  . PHE B 354  ? 0.5477 0.3340 0.4727 -0.1528 -0.1417 0.0679  352  PHE B CB  
11336 C CG  . PHE B 354  ? 0.5440 0.3152 0.4633 -0.1443 -0.1447 0.0644  352  PHE B CG  
11337 C CD1 . PHE B 354  ? 0.5582 0.3080 0.4740 -0.1401 -0.1526 0.0579  352  PHE B CD1 
11338 C CD2 . PHE B 354  ? 0.5359 0.3146 0.4535 -0.1405 -0.1400 0.0675  352  PHE B CD2 
11339 C CE1 . PHE B 354  ? 0.5834 0.3201 0.4948 -0.1321 -0.1555 0.0549  352  PHE B CE1 
11340 C CE2 . PHE B 354  ? 0.5791 0.3444 0.4920 -0.1330 -0.1432 0.0647  352  PHE B CE2 
11341 C CZ  . PHE B 354  ? 0.6130 0.3577 0.5233 -0.1286 -0.1509 0.0585  352  PHE B CZ  
11342 N N   . ILE B 355  ? 0.5103 0.3106 0.4316 -0.1693 -0.1379 0.0928  353  ILE B N   
11343 C CA  . ILE B 355  ? 0.5294 0.3291 0.4453 -0.1715 -0.1371 0.1012  353  ILE B CA  
11344 C C   . ILE B 355  ? 0.5974 0.3885 0.5109 -0.1845 -0.1433 0.1123  353  ILE B C   
11345 O O   . ILE B 355  ? 0.6064 0.3826 0.5131 -0.1863 -0.1485 0.1174  353  ILE B O   
11346 C CB  . ILE B 355  ? 0.5366 0.3608 0.4549 -0.1691 -0.1262 0.1037  353  ILE B CB  
11347 C CG1 . ILE B 355  ? 0.5139 0.3434 0.4333 -0.1561 -0.1212 0.0932  353  ILE B CG1 
11348 C CG2 . ILE B 355  ? 0.5673 0.3919 0.4793 -0.1732 -0.1254 0.1138  353  ILE B CG2 
11349 C CD1 . ILE B 355  ? 0.4806 0.3336 0.4026 -0.1529 -0.1107 0.0941  353  ILE B CD1 
11350 N N   . ILE B 356  ? 0.5208 0.3212 0.4401 -0.1940 -0.1430 0.1165  354  ILE B N   
11351 C CA  . ILE B 356  ? 0.6165 0.4105 0.5345 -0.2068 -0.1486 0.1274  354  ILE B CA  
11352 C C   . ILE B 356  ? 0.6012 0.3706 0.5142 -0.2046 -0.1590 0.1235  354  ILE B C   
11353 O O   . ILE B 356  ? 0.6440 0.4040 0.5521 -0.2082 -0.1636 0.1300  354  ILE B O   
11354 C CB  . ILE B 356  ? 0.5707 0.3840 0.4974 -0.2143 -0.1452 0.1306  354  ILE B CB  
11355 C CG1 . ILE B 356  ? 0.5699 0.4090 0.5008 -0.2167 -0.1345 0.1368  354  ILE B CG1 
11356 C CG2 . ILE B 356  ? 0.5942 0.4028 0.5207 -0.2225 -0.1511 0.1375  354  ILE B CG2 
11357 C CD1 . ILE B 356  ? 0.5629 0.4231 0.5039 -0.2215 -0.1299 0.1376  354  ILE B CD1 
11358 N N   . ASP B 357  ? 0.5822 0.3409 0.4959 -0.1980 -0.1626 0.1127  355  ASP B N   
11359 C CA  . ASP B 357  ? 0.6434 0.3789 0.5519 -0.1944 -0.1719 0.1083  355  ASP B CA  
11360 C C   . ASP B 357  ? 0.6477 0.3679 0.5490 -0.1877 -0.1748 0.1076  355  ASP B C   
11361 O O   . ASP B 357  ? 0.6480 0.3523 0.5439 -0.1883 -0.1819 0.1101  355  ASP B O   
11362 C CB  . ASP B 357  ? 0.6637 0.3929 0.5743 -0.1883 -0.1742 0.0967  355  ASP B CB  
11363 C CG  . ASP B 357  ? 0.6775 0.3829 0.5822 -0.1823 -0.1829 0.0907  355  ASP B CG  
11364 O OD1 . ASP B 357  ? 0.6829 0.3794 0.5855 -0.1877 -0.1891 0.0946  355  ASP B OD1 
11365 O OD2 . ASP B 357  ? 0.6655 0.3613 0.5677 -0.1720 -0.1835 0.0823  355  ASP B OD2 
11366 N N   . LEU B 358  ? 0.6155 0.3400 0.5164 -0.1811 -0.1697 0.1042  356  LEU B N   
11367 C CA  . LEU B 358  ? 0.6333 0.3449 0.5277 -0.1746 -0.1723 0.1041  356  LEU B CA  
11368 C C   . LEU B 358  ? 0.6456 0.3572 0.5352 -0.1814 -0.1734 0.1160  356  LEU B C   
11369 O O   . LEU B 358  ? 0.6382 0.3336 0.5217 -0.1786 -0.1796 0.1171  356  LEU B O   
11370 C CB  . LEU B 358  ? 0.5913 0.3173 0.4877 -0.1639 -0.1638 0.0979  356  LEU B CB  
11371 C CG  . LEU B 358  ? 0.6091 0.3271 0.5001 -0.1547 -0.1647 0.0962  356  LEU B CG  
11372 C CD1 . LEU B 358  ? 0.5910 0.2829 0.4780 -0.1497 -0.1746 0.0911  356  LEU B CD1 
11373 C CD2 . LEU B 358  ? 0.5776 0.3126 0.4723 -0.1439 -0.1558 0.0885  356  LEU B CD2 
11374 N N   . ALA B 359  ? 0.6204 0.3508 0.5126 -0.1901 -0.1672 0.1248  357  ALA B N   
11375 C CA  . ALA B 359  ? 0.6615 0.3944 0.5490 -0.1964 -0.1671 0.1361  357  ALA B CA  
11376 C C   . ALA B 359  ? 0.7127 0.4338 0.5985 -0.2022 -0.1751 0.1400  357  ALA B C   
11377 O O   . ALA B 359  ? 0.6848 0.3967 0.5645 -0.2039 -0.1791 0.1460  357  ALA B O   
11378 C CB  . ALA B 359  ? 0.6278 0.3859 0.5192 -0.2033 -0.1576 0.1439  357  ALA B CB  
11379 N N   . ARG B 360  ? 0.7062 0.4270 0.5972 -0.2054 -0.1778 0.1366  358  ARG B N   
11380 C CA  . ARG B 360  ? 0.7353 0.4441 0.6245 -0.2110 -0.1859 0.1400  358  ARG B CA  
11381 C C   . ARG B 360  ? 0.7340 0.4178 0.6165 -0.2038 -0.1947 0.1349  358  ARG B C   
11382 O O   . ARG B 360  ? 0.7528 0.4260 0.6302 -0.2072 -0.2002 0.1410  358  ARG B O   
11383 C CB  . ARG B 360  ? 0.7717 0.4849 0.6673 -0.2148 -0.1871 0.1365  358  ARG B CB  
11384 C CG  . ARG B 360  ? 0.7802 0.5162 0.6824 -0.2247 -0.1811 0.1445  358  ARG B CG  
11385 C CD  . ARG B 360  ? 0.8431 0.5773 0.7494 -0.2304 -0.1860 0.1438  358  ARG B CD  
11386 N NE  . ARG B 360  ? 0.7883 0.5465 0.7030 -0.2375 -0.1794 0.1485  358  ARG B NE  
11387 C CZ  . ARG B 360  ? 0.8148 0.5853 0.7357 -0.2349 -0.1745 0.1426  358  ARG B CZ  
11388 N NH1 . ARG B 360  ? 0.8511 0.6129 0.7708 -0.2258 -0.1751 0.1318  358  ARG B NH1 
11389 N NH2 . ARG B 360  ? 0.7915 0.5844 0.7205 -0.2415 -0.1689 0.1477  358  ARG B NH2 
11390 N N   . ARG B 361  ? 0.7085 0.3831 0.5911 -0.1937 -0.1959 0.1237  359  ARG B N   
11391 C CA  . ARG B 361  ? 0.7458 0.3977 0.6230 -0.1860 -0.2041 0.1178  359  ARG B CA  
11392 C C   . ARG B 361  ? 0.7319 0.3768 0.6036 -0.1802 -0.2048 0.1196  359  ARG B C   
11393 O O   . ARG B 361  ? 0.7195 0.3461 0.5864 -0.1751 -0.2120 0.1172  359  ARG B O   
11394 C CB  . ARG B 361  ? 0.7349 0.3806 0.6144 -0.1766 -0.2049 0.1049  359  ARG B CB  
11395 C CG  . ARG B 361  ? 0.7190 0.3757 0.6019 -0.1697 -0.1975 0.0987  359  ARG B CG  
11396 C CD  . ARG B 361  ? 0.7441 0.3966 0.6298 -0.1617 -0.1980 0.0863  359  ARG B CD  
11397 N NE  . ARG B 361  ? 0.7073 0.3742 0.5977 -0.1577 -0.1901 0.0811  359  ARG B NE  
11398 C CZ  . ARG B 361  ? 0.6731 0.3378 0.5631 -0.1477 -0.1880 0.0746  359  ARG B CZ  
11399 N NH1 . ARG B 361  ? 0.6906 0.3400 0.5761 -0.1400 -0.1929 0.0720  359  ARG B NH1 
11400 N NH2 . ARG B 361  ? 0.6115 0.2903 0.5061 -0.1454 -0.1809 0.0706  359  ARG B NH2 
11401 N N   . SER B 362  ? 0.7171 0.3759 0.5891 -0.1805 -0.1974 0.1235  360  SER B N   
11402 C CA  . SER B 362  ? 0.6808 0.3336 0.5470 -0.1750 -0.1980 0.1255  360  SER B CA  
11403 C C   . SER B 362  ? 0.6876 0.3447 0.5493 -0.1832 -0.1977 0.1378  360  SER B C   
11404 O O   . SER B 362  ? 0.7171 0.3668 0.5729 -0.1793 -0.1998 0.1403  360  SER B O   
11405 C CB  . SER B 362  ? 0.6934 0.3569 0.5615 -0.1684 -0.1906 0.1212  360  SER B CB  
11406 O OG  . SER B 362  ? 0.6480 0.3323 0.5189 -0.1758 -0.1823 0.1278  360  SER B OG  
11407 N N   . GLY B 363  ? 0.6588 0.3281 0.5230 -0.1940 -0.1951 0.1456  361  GLY B N   
11408 C CA  . GLY B 363  ? 0.6699 0.3441 0.5298 -0.2016 -0.1944 0.1573  361  GLY B CA  
11409 C C   . GLY B 363  ? 0.6941 0.3842 0.5519 -0.2011 -0.1858 0.1620  361  GLY B C   
11410 O O   . GLY B 363  ? 0.7246 0.4145 0.5762 -0.2034 -0.1860 0.1696  361  GLY B O   
11411 N N   . ARG B 364  ? 0.6734 0.3772 0.5356 -0.1980 -0.1784 0.1576  362  ARG B N   
11412 C CA  . ARG B 364  ? 0.7221 0.4421 0.5823 -0.1970 -0.1696 0.1614  362  ARG B CA  
11413 C C   . ARG B 364  ? 0.6768 0.4202 0.5437 -0.2039 -0.1610 0.1648  362  ARG B C   
11414 O O   . ARG B 364  ? 0.7102 0.4578 0.5843 -0.2035 -0.1597 0.1587  362  ARG B O   
11415 C CB  . ARG B 364  ? 0.6606 0.3765 0.5198 -0.1860 -0.1680 0.1528  362  ARG B CB  
11416 C CG  . ARG B 364  ? 0.6532 0.3473 0.5078 -0.1775 -0.1763 0.1474  362  ARG B CG  
11417 C CD  . ARG B 364  ? 0.6980 0.3887 0.5439 -0.1763 -0.1774 0.1541  362  ARG B CD  
11418 N NE  . ARG B 364  ? 0.6846 0.3550 0.5271 -0.1677 -0.1856 0.1486  362  ARG B NE  
11419 C CZ  . ARG B 364  ? 0.6669 0.3325 0.5094 -0.1571 -0.1858 0.1411  362  ARG B CZ  
11420 N NH1 . ARG B 364  ? 0.6360 0.3192 0.4822 -0.1524 -0.1772 0.1364  362  ARG B NH1 
11421 N NH2 . ARG B 364  ? 0.6773 0.3252 0.5179 -0.1493 -0.1935 0.1361  362  ARG B NH2 
11422 N N   . ARG B 365  ? 0.6256 0.3849 0.4904 -0.2096 -0.1549 0.1742  363  ARG B N   
11423 C CA  . ARG B 365  ? 0.6642 0.4483 0.5350 -0.2135 -0.1450 0.1767  363  ARG B CA  
11424 C C   . ARG B 365  ? 0.5957 0.3867 0.4652 -0.2054 -0.1386 0.1714  363  ARG B C   
11425 O O   . ARG B 365  ? 0.6453 0.4391 0.5078 -0.2002 -0.1355 0.1727  363  ARG B O   
11426 C CB  . ARG B 365  ? 0.6774 0.4776 0.5464 -0.2211 -0.1398 0.1877  363  ARG B CB  
11427 C CG  . ARG B 365  ? 0.6500 0.4767 0.5269 -0.2255 -0.1301 0.1902  363  ARG B CG  
11428 C CD  . ARG B 365  ? 0.6912 0.5311 0.5690 -0.2344 -0.1275 0.2006  363  ARG B CD  
11429 N NE  . ARG B 365  ? 0.6684 0.5327 0.5558 -0.2388 -0.1196 0.2025  363  ARG B NE  
11430 C CZ  . ARG B 365  ? 0.6569 0.5442 0.5448 -0.2399 -0.1097 0.2079  363  ARG B CZ  
11431 N NH1 . ARG B 365  ? 0.6173 0.5064 0.4959 -0.2375 -0.1062 0.2121  363  ARG B NH1 
11432 N NH2 . ARG B 365  ? 0.6419 0.5509 0.5397 -0.2431 -0.1032 0.2088  363  ARG B NH2 
11433 N N   . ILE B 366  ? 0.6009 0.3990 0.4788 -0.2001 -0.1359 0.1614  364  ILE B N   
11434 C CA  . ILE B 366  ? 0.5719 0.3829 0.4521 -0.1883 -0.1284 0.1516  364  ILE B CA  
11435 C C   . ILE B 366  ? 0.6025 0.4410 0.4865 -0.1907 -0.1174 0.1553  364  ILE B C   
11436 O O   . ILE B 366  ? 0.5773 0.4267 0.4676 -0.1992 -0.1153 0.1600  364  ILE B O   
11437 C CB  . ILE B 366  ? 0.5632 0.3686 0.4503 -0.1815 -0.1307 0.1393  364  ILE B CB  
11438 C CG1 . ILE B 366  ? 0.6089 0.3871 0.4919 -0.1781 -0.1414 0.1353  364  ILE B CG1 
11439 C CG2 . ILE B 366  ? 0.5057 0.3260 0.3960 -0.1702 -0.1227 0.1299  364  ILE B CG2 
11440 C CD1 . ILE B 366  ? 0.6327 0.4046 0.5214 -0.1710 -0.1438 0.1231  364  ILE B CD1 
11441 N N   . MET B 367  ? 0.5773 0.4269 0.4574 -0.1831 -0.1105 0.1532  365  MET B N   
11442 C CA  . MET B 367  ? 0.5248 0.4002 0.4080 -0.1831 -0.0996 0.1552  365  MET B CA  
11443 C C   . MET B 367  ? 0.5401 0.4260 0.4321 -0.1755 -0.0950 0.1441  365  MET B C   
11444 O O   . MET B 367  ? 0.5055 0.3849 0.3968 -0.1654 -0.0959 0.1345  365  MET B O   
11445 C CB  . MET B 367  ? 0.5469 0.4279 0.4207 -0.1784 -0.0949 0.1577  365  MET B CB  
11446 C CG  . MET B 367  ? 0.5499 0.4176 0.4136 -0.1848 -0.1005 0.1680  365  MET B CG  
11447 S SD  . MET B 367  ? 0.6004 0.4722 0.4515 -0.1787 -0.0962 0.1704  365  MET B SD  
11448 C CE  . MET B 367  ? 0.6280 0.5292 0.4803 -0.1832 -0.0838 0.1772  365  MET B CE  
11449 N N   . VAL B 368  ? 0.4840 0.3861 0.3844 -0.1804 -0.0904 0.1456  366  VAL B N   
11450 C CA  . VAL B 368  ? 0.4553 0.3664 0.3644 -0.1743 -0.0869 0.1358  366  VAL B CA  
11451 C C   . VAL B 368  ? 0.4412 0.3776 0.3534 -0.1716 -0.0760 0.1363  366  VAL B C   
11452 O O   . VAL B 368  ? 0.4553 0.4071 0.3717 -0.1791 -0.0718 0.1436  366  VAL B O   
11453 C CB  . VAL B 368  ? 0.4570 0.3647 0.3741 -0.1810 -0.0917 0.1353  366  VAL B CB  
11454 C CG1 . VAL B 368  ? 0.4458 0.3598 0.3700 -0.1730 -0.0888 0.1242  366  VAL B CG1 
11455 C CG2 . VAL B 368  ? 0.5255 0.4076 0.4386 -0.1844 -0.1027 0.1358  366  VAL B CG2 
11456 N N   . ARG B 369  ? 0.4286 0.3694 0.3392 -0.1608 -0.0714 0.1283  367  ARG B N   
11457 C CA  . ARG B 369  ? 0.4151 0.3783 0.3285 -0.1569 -0.0613 0.1272  367  ARG B CA  
11458 C C   . ARG B 369  ? 0.4406 0.4122 0.3646 -0.1544 -0.0594 0.1201  367  ARG B C   
11459 O O   . ARG B 369  ? 0.4188 0.3824 0.3445 -0.1470 -0.0616 0.1106  367  ARG B O   
11460 C CB  . ARG B 369  ? 0.4547 0.4189 0.3611 -0.1468 -0.0575 0.1223  367  ARG B CB  
11461 C CG  . ARG B 369  ? 0.4438 0.4305 0.3523 -0.1430 -0.0472 0.1216  367  ARG B CG  
11462 C CD  . ARG B 369  ? 0.4732 0.4600 0.3765 -0.1321 -0.0440 0.1141  367  ARG B CD  
11463 N NE  . ARG B 369  ? 0.4472 0.4248 0.3390 -0.1315 -0.0462 0.1179  367  ARG B NE  
11464 C CZ  . ARG B 369  ? 0.5029 0.4720 0.3889 -0.1234 -0.0478 0.1119  367  ARG B CZ  
11465 N NH1 . ARG B 369  ? 0.5053 0.4737 0.3961 -0.1153 -0.0473 0.1019  367  ARG B NH1 
11466 N NH2 . ARG B 369  ? 0.4672 0.4284 0.3424 -0.1237 -0.0501 0.1163  367  ARG B NH2 
11467 N N   . LEU B 370  ? 0.3974 0.3853 0.3286 -0.1607 -0.0554 0.1251  368  LEU B N   
11468 C CA  . LEU B 370  ? 0.3949 0.3936 0.3360 -0.1585 -0.0528 0.1194  368  LEU B CA  
11469 C C   . LEU B 370  ? 0.3895 0.4064 0.3318 -0.1504 -0.0433 0.1157  368  LEU B C   
11470 O O   . LEU B 370  ? 0.4374 0.4695 0.3784 -0.1523 -0.0369 0.1219  368  LEU B O   
11471 C CB  . LEU B 370  ? 0.3878 0.3953 0.3367 -0.1693 -0.0537 0.1266  368  LEU B CB  
11472 C CG  . LEU B 370  ? 0.4444 0.4626 0.4038 -0.1678 -0.0520 0.1212  368  LEU B CG  
11473 C CD1 . LEU B 370  ? 0.3811 0.3819 0.3407 -0.1631 -0.0585 0.1115  368  LEU B CD1 
11474 C CD2 . LEU B 370  ? 0.4053 0.4330 0.3723 -0.1794 -0.0533 0.1295  368  LEU B CD2 
11475 N N   . VAL B 371  ? 0.3740 0.3889 0.3182 -0.1412 -0.0424 0.1056  369  VAL B N   
11476 C CA  . VAL B 371  ? 0.3435 0.3738 0.2890 -0.1332 -0.0342 0.1012  369  VAL B CA  
11477 C C   . VAL B 371  ? 0.3553 0.3925 0.3106 -0.1310 -0.0333 0.0952  369  VAL B C   
11478 O O   . VAL B 371  ? 0.3503 0.3784 0.3097 -0.1345 -0.0393 0.0934  369  VAL B O   
11479 C CB  . VAL B 371  ? 0.3810 0.4027 0.3189 -0.1237 -0.0338 0.0947  369  VAL B CB  
11480 C CG1 . VAL B 371  ? 0.3882 0.3994 0.3160 -0.1263 -0.0367 0.1004  369  VAL B CG1 
11481 C CG2 . VAL B 371  ? 0.3720 0.3795 0.3121 -0.1187 -0.0392 0.0858  369  VAL B CG2 
11482 N N   . LYS B 372  ? 0.3394 0.3923 0.2979 -0.1249 -0.0260 0.0920  370  LYS B N   
11483 C CA  . LYS B 372  ? 0.3364 0.3939 0.3031 -0.1214 -0.0255 0.0855  370  LYS B CA  
11484 C C   . LYS B 372  ? 0.3113 0.3558 0.2752 -0.1129 -0.0280 0.0758  370  LYS B C   
11485 O O   . LYS B 372  ? 0.3421 0.3759 0.3086 -0.1133 -0.0335 0.0715  370  LYS B O   
11486 C CB  . LYS B 372  ? 0.2973 0.3769 0.2697 -0.1189 -0.0173 0.0865  370  LYS B CB  
11487 C CG  . LYS B 372  ? 0.3157 0.4086 0.2932 -0.1286 -0.0158 0.0964  370  LYS B CG  
11488 C CD  . LYS B 372  ? 0.3738 0.4897 0.3579 -0.1266 -0.0078 0.0983  370  LYS B CD  
11489 C CE  . LYS B 372  ? 0.3977 0.5265 0.3866 -0.1367 -0.0065 0.1089  370  LYS B CE  
11490 N NZ  . LYS B 372  ? 0.3398 0.4926 0.3347 -0.1341 0.0021  0.1113  370  LYS B NZ  
11491 N N   . GLY B 373  ? 0.3110 0.3557 0.2694 -0.1054 -0.0244 0.0724  371  GLY B N   
11492 C CA  . GLY B 373  ? 0.3067 0.3380 0.2620 -0.0982 -0.0274 0.0644  371  GLY B CA  
11493 C C   . GLY B 373  ? 0.3421 0.3807 0.2963 -0.0892 -0.0218 0.0588  371  GLY B C   
11494 O O   . GLY B 373  ? 0.3271 0.3805 0.2859 -0.0872 -0.0161 0.0584  371  GLY B O   
11495 N N   . ALA B 374  ? 0.3166 0.3444 0.2650 -0.0836 -0.0237 0.0545  372  ALA B N   
11496 C CA  . ALA B 374  ? 0.3354 0.3684 0.2805 -0.0760 -0.0189 0.0506  372  ALA B CA  
11497 C C   . ALA B 374  ? 0.3039 0.3346 0.2529 -0.0688 -0.0188 0.0419  372  ALA B C   
11498 O O   . ALA B 374  ? 0.3198 0.3549 0.2667 -0.0626 -0.0151 0.0384  372  ALA B O   
11499 C CB  . ALA B 374  ? 0.3653 0.3892 0.3006 -0.0748 -0.0209 0.0522  372  ALA B CB  
11500 N N   . TYR B 375  ? 0.2870 0.3115 0.2415 -0.0697 -0.0227 0.0385  373  TYR B N   
11501 C CA  . TYR B 375  ? 0.3364 0.3565 0.2937 -0.0632 -0.0234 0.0306  373  TYR B CA  
11502 C C   . TYR B 375  ? 0.2998 0.3280 0.2649 -0.0628 -0.0214 0.0278  373  TYR B C   
11503 O O   . TYR B 375  ? 0.2749 0.2978 0.2429 -0.0596 -0.0234 0.0222  373  TYR B O   
11504 C CB  . TYR B 375  ? 0.2937 0.2977 0.2495 -0.0629 -0.0300 0.0277  373  TYR B CB  
11505 C CG  . TYR B 375  ? 0.3545 0.3491 0.3027 -0.0630 -0.0330 0.0303  373  TYR B CG  
11506 C CD1 . TYR B 375  ? 0.3549 0.3462 0.2993 -0.0696 -0.0354 0.0373  373  TYR B CD1 
11507 C CD2 . TYR B 375  ? 0.3848 0.3741 0.3300 -0.0568 -0.0337 0.0259  373  TYR B CD2 
11508 C CE1 . TYR B 375  ? 0.3838 0.3663 0.3207 -0.0697 -0.0384 0.0399  373  TYR B CE1 
11509 C CE2 . TYR B 375  ? 0.3978 0.3786 0.3360 -0.0569 -0.0369 0.0284  373  TYR B CE2 
11510 C CZ  . TYR B 375  ? 0.4150 0.3922 0.3488 -0.0632 -0.0392 0.0354  373  TYR B CZ  
11511 O OH  . TYR B 375  ? 0.4126 0.3810 0.3389 -0.0635 -0.0427 0.0382  373  TYR B OH  
11512 N N   . TRP B 376  ? 0.2886 0.3304 0.2571 -0.0655 -0.0173 0.0317  374  TRP B N   
11513 C CA  . TRP B 376  ? 0.2558 0.3046 0.2317 -0.0668 -0.0167 0.0303  374  TRP B CA  
11514 C C   . TRP B 376  ? 0.2988 0.3490 0.2776 -0.0597 -0.0147 0.0234  374  TRP B C   
11515 O O   . TRP B 376  ? 0.2695 0.3152 0.2518 -0.0595 -0.0174 0.0197  374  TRP B O   
11516 C CB  . TRP B 376  ? 0.2660 0.3306 0.2456 -0.0705 -0.0123 0.0361  374  TRP B CB  
11517 C CG  . TRP B 376  ? 0.2902 0.3617 0.2775 -0.0723 -0.0125 0.0352  374  TRP B CG  
11518 C CD1 . TRP B 376  ? 0.2745 0.3422 0.2651 -0.0786 -0.0172 0.0369  374  TRP B CD1 
11519 C CD2 . TRP B 376  ? 0.2981 0.3807 0.2905 -0.0676 -0.0083 0.0323  374  TRP B CD2 
11520 N NE1 . TRP B 376  ? 0.2857 0.3620 0.2830 -0.0783 -0.0162 0.0353  374  TRP B NE1 
11521 C CE2 . TRP B 376  ? 0.3274 0.4131 0.3261 -0.0715 -0.0107 0.0326  374  TRP B CE2 
11522 C CE3 . TRP B 376  ? 0.3283 0.4180 0.3203 -0.0605 -0.0030 0.0294  374  TRP B CE3 
11523 C CZ2 . TRP B 376  ? 0.2476 0.3435 0.2522 -0.0685 -0.0080 0.0304  374  TRP B CZ2 
11524 C CZ3 . TRP B 376  ? 0.2746 0.3739 0.2726 -0.0574 -0.0004 0.0272  374  TRP B CZ3 
11525 C CH2 . TRP B 376  ? 0.2811 0.3838 0.2854 -0.0614 -0.0028 0.0279  374  TRP B CH2 
11526 N N   . ASP B 377  ? 0.2833 0.3398 0.2606 -0.0541 -0.0100 0.0216  375  ASP B N   
11527 C CA  . ASP B 377  ? 0.3025 0.3603 0.2825 -0.0477 -0.0082 0.0155  375  ASP B CA  
11528 C C   . ASP B 377  ? 0.3167 0.3614 0.2957 -0.0453 -0.0125 0.0104  375  ASP B C   
11529 O O   . ASP B 377  ? 0.3049 0.3489 0.2878 -0.0430 -0.0129 0.0062  375  ASP B O   
11530 C CB  . ASP B 377  ? 0.3733 0.4367 0.3502 -0.0420 -0.0035 0.0144  375  ASP B CB  
11531 C CG  . ASP B 377  ? 0.4718 0.5499 0.4508 -0.0425 0.0017  0.0182  375  ASP B CG  
11532 O OD1 . ASP B 377  ? 0.5230 0.6094 0.5084 -0.0423 0.0033  0.0177  375  ASP B OD1 
11533 O OD2 . ASP B 377  ? 0.5487 0.6306 0.5229 -0.0429 0.0042  0.0217  375  ASP B OD2 
11534 N N   . ALA B 378  ? 0.2954 0.3301 0.2692 -0.0457 -0.0156 0.0109  376  ALA B N   
11535 C CA  . ALA B 378  ? 0.2928 0.3157 0.2661 -0.0430 -0.0196 0.0062  376  ALA B CA  
11536 C C   . ALA B 378  ? 0.3076 0.3250 0.2841 -0.0462 -0.0235 0.0052  376  ALA B C   
11537 O O   . ALA B 378  ? 0.3176 0.3303 0.2964 -0.0430 -0.0250 0.0002  376  ALA B O   
11538 C CB  . ALA B 378  ? 0.2769 0.2906 0.2440 -0.0431 -0.0226 0.0077  376  ALA B CB  
11539 N N   . GLU B 379  ? 0.2646 0.2826 0.2413 -0.0525 -0.0253 0.0099  377  GLU B N   
11540 C CA  . GLU B 379  ? 0.3006 0.3119 0.2795 -0.0557 -0.0297 0.0086  377  GLU B CA  
11541 C C   . GLU B 379  ? 0.2768 0.2953 0.2610 -0.0544 -0.0277 0.0055  377  GLU B C   
11542 O O   . GLU B 379  ? 0.3071 0.3193 0.2924 -0.0534 -0.0305 0.0014  377  GLU B O   
11543 C CB  . GLU B 379  ? 0.3203 0.3298 0.2980 -0.0635 -0.0326 0.0147  377  GLU B CB  
11544 C CG  . GLU B 379  ? 0.3272 0.3283 0.2992 -0.0658 -0.0354 0.0186  377  GLU B CG  
11545 C CD  . GLU B 379  ? 0.3663 0.3516 0.3353 -0.0634 -0.0408 0.0149  377  GLU B CD  
11546 O OE1 . GLU B 379  ? 0.3625 0.3431 0.3339 -0.0603 -0.0425 0.0093  377  GLU B OE1 
11547 O OE2 . GLU B 379  ? 0.3109 0.2888 0.2751 -0.0645 -0.0433 0.0178  377  GLU B OE2 
11548 N N   . ILE B 380  ? 0.2883 0.3200 0.2754 -0.0542 -0.0230 0.0075  378  ILE B N   
11549 C CA  . ILE B 380  ? 0.2836 0.3225 0.2755 -0.0525 -0.0211 0.0048  378  ILE B CA  
11550 C C   . ILE B 380  ? 0.2530 0.2879 0.2450 -0.0459 -0.0204 -0.0014 378  ILE B C   
11551 O O   . ILE B 380  ? 0.2634 0.2958 0.2573 -0.0449 -0.0218 -0.0050 378  ILE B O   
11552 C CB  . ILE B 380  ? 0.2525 0.3063 0.2476 -0.0524 -0.0161 0.0081  378  ILE B CB  
11553 C CG1 . ILE B 380  ? 0.2501 0.3094 0.2458 -0.0592 -0.0164 0.0148  378  ILE B CG1 
11554 C CG2 . ILE B 380  ? 0.2656 0.3264 0.2657 -0.0507 -0.0147 0.0056  378  ILE B CG2 
11555 C CD1 . ILE B 380  ? 0.2354 0.2924 0.2338 -0.0656 -0.0209 0.0164  378  ILE B CD1 
11556 N N   . LYS B 381  ? 0.2409 0.2757 0.2307 -0.0415 -0.0180 -0.0025 379  LYS B N   
11557 C CA  . LYS B 381  ? 0.2682 0.2999 0.2587 -0.0357 -0.0172 -0.0078 379  LYS B CA  
11558 C C   . LYS B 381  ? 0.2545 0.2748 0.2441 -0.0352 -0.0215 -0.0113 379  LYS B C   
11559 O O   . LYS B 381  ? 0.2450 0.2645 0.2370 -0.0326 -0.0215 -0.0154 379  LYS B O   
11560 C CB  . LYS B 381  ? 0.2389 0.2711 0.2265 -0.0319 -0.0149 -0.0080 379  LYS B CB  
11561 C CG  . LYS B 381  ? 0.2440 0.2729 0.2328 -0.0264 -0.0146 -0.0131 379  LYS B CG  
11562 C CD  . LYS B 381  ? 0.2960 0.3260 0.2822 -0.0228 -0.0125 -0.0135 379  LYS B CD  
11563 C CE  . LYS B 381  ? 0.3164 0.3449 0.3050 -0.0180 -0.0119 -0.0181 379  LYS B CE  
11564 N NZ  . LYS B 381  ? 0.2964 0.3233 0.2817 -0.0149 -0.0113 -0.0188 379  LYS B NZ  
11565 N N   . ARG B 382  ? 0.2249 0.2365 0.2112 -0.0376 -0.0252 -0.0096 380  ARG B N   
11566 C CA  . ARG B 382  ? 0.3062 0.3066 0.2916 -0.0363 -0.0294 -0.0131 380  ARG B CA  
11567 C C   . ARG B 382  ? 0.3004 0.2988 0.2876 -0.0381 -0.0314 -0.0152 380  ARG B C   
11568 O O   . ARG B 382  ? 0.2971 0.2913 0.2852 -0.0346 -0.0323 -0.0200 380  ARG B O   
11569 C CB  . ARG B 382  ? 0.3491 0.3402 0.3304 -0.0389 -0.0335 -0.0102 380  ARG B CB  
11570 C CG  . ARG B 382  ? 0.3916 0.3706 0.3720 -0.0366 -0.0380 -0.0139 380  ARG B CG  
11571 C CD  . ARG B 382  ? 0.4970 0.4747 0.4780 -0.0307 -0.0371 -0.0172 380  ARG B CD  
11572 N NE  . ARG B 382  ? 0.5046 0.4832 0.4893 -0.0263 -0.0360 -0.0226 380  ARG B NE  
11573 C CZ  . ARG B 382  ? 0.5424 0.5244 0.5296 -0.0216 -0.0337 -0.0253 380  ARG B CZ  
11574 N NH1 . ARG B 382  ? 0.5248 0.5093 0.5107 -0.0205 -0.0324 -0.0236 380  ARG B NH1 
11575 N NH2 . ARG B 382  ? 0.4983 0.4809 0.4889 -0.0180 -0.0328 -0.0298 380  ARG B NH2 
11576 N N   . ALA B 383  ? 0.2881 0.2895 0.2755 -0.0436 -0.0324 -0.0116 381  ALA B N   
11577 C CA  . ALA B 383  ? 0.2761 0.2753 0.2645 -0.0458 -0.0348 -0.0136 381  ALA B CA  
11578 C C   . ALA B 383  ? 0.2846 0.2910 0.2760 -0.0420 -0.0315 -0.0172 381  ALA B C   
11579 O O   . ALA B 383  ? 0.2617 0.2637 0.2528 -0.0407 -0.0332 -0.0213 381  ALA B O   
11580 C CB  . ALA B 383  ? 0.2577 0.2605 0.2466 -0.0529 -0.0363 -0.0085 381  ALA B CB  
11581 N N   . GLN B 384  ? 0.2553 0.2725 0.2492 -0.0402 -0.0268 -0.0158 382  GLN B N   
11582 C CA  . GLN B 384  ? 0.2755 0.2990 0.2721 -0.0368 -0.0239 -0.0188 382  GLN B CA  
11583 C C   . GLN B 384  ? 0.2677 0.2863 0.2641 -0.0312 -0.0233 -0.0237 382  GLN B C   
11584 O O   . GLN B 384  ? 0.2907 0.3091 0.2878 -0.0292 -0.0231 -0.0272 382  GLN B O   
11585 C CB  . GLN B 384  ? 0.2099 0.2453 0.2091 -0.0359 -0.0193 -0.0161 382  GLN B CB  
11586 C CG  . GLN B 384  ? 0.2422 0.2857 0.2433 -0.0410 -0.0192 -0.0113 382  GLN B CG  
11587 C CD  . GLN B 384  ? 0.2496 0.3049 0.2535 -0.0388 -0.0144 -0.0093 382  GLN B CD  
11588 O OE1 . GLN B 384  ? 0.2628 0.3185 0.2659 -0.0343 -0.0117 -0.0107 382  GLN B OE1 
11589 N NE2 . GLN B 384  ? 0.2146 0.2793 0.2218 -0.0418 -0.0137 -0.0061 382  GLN B NE2 
11590 N N   . LEU B 385  ? 0.2478 0.2628 0.2431 -0.0288 -0.0231 -0.0238 383  LEU B N   
11591 C CA  . LEU B 385  ? 0.2937 0.3047 0.2897 -0.0238 -0.0228 -0.0280 383  LEU B CA  
11592 C C   . LEU B 385  ? 0.3010 0.3037 0.2960 -0.0233 -0.0261 -0.0315 383  LEU B C   
11593 O O   . LEU B 385  ? 0.2635 0.2661 0.2599 -0.0196 -0.0250 -0.0354 383  LEU B O   
11594 C CB  . LEU B 385  ? 0.2950 0.3029 0.2898 -0.0221 -0.0231 -0.0271 383  LEU B CB  
11595 C CG  . LEU B 385  ? 0.3133 0.3285 0.3089 -0.0203 -0.0193 -0.0257 383  LEU B CG  
11596 C CD1 . LEU B 385  ? 0.3330 0.3438 0.3263 -0.0188 -0.0204 -0.0251 383  LEU B CD1 
11597 C CD2 . LEU B 385  ? 0.3311 0.3510 0.3301 -0.0165 -0.0164 -0.0289 383  LEU B CD2 
11598 N N   . ASP B 386  ? 0.2880 0.2834 0.2802 -0.0268 -0.0301 -0.0301 384  ASP B N   
11599 C CA  . ASP B 386  ? 0.2890 0.2744 0.2794 -0.0258 -0.0339 -0.0336 384  ASP B CA  
11600 C C   . ASP B 386  ? 0.3044 0.2896 0.2938 -0.0276 -0.0350 -0.0355 384  ASP B C   
11601 O O   . ASP B 386  ? 0.3305 0.3071 0.3176 -0.0265 -0.0381 -0.0391 384  ASP B O   
11602 C CB  . ASP B 386  ? 0.3251 0.3008 0.3124 -0.0286 -0.0384 -0.0312 384  ASP B CB  
11603 C CG  . ASP B 386  ? 0.4064 0.3797 0.3938 -0.0255 -0.0384 -0.0307 384  ASP B CG  
11604 O OD1 . ASP B 386  ? 0.4361 0.4147 0.4263 -0.0213 -0.0351 -0.0327 384  ASP B OD1 
11605 O OD2 . ASP B 386  ? 0.4207 0.3865 0.4053 -0.0276 -0.0419 -0.0282 384  ASP B OD2 
11606 N N   . GLY B 387  ? 0.3089 0.3031 0.2997 -0.0301 -0.0327 -0.0335 385  GLY B N   
11607 C CA  . GLY B 387  ? 0.2746 0.2693 0.2643 -0.0319 -0.0339 -0.0352 385  GLY B CA  
11608 C C   . GLY B 387  ? 0.3648 0.3504 0.3511 -0.0366 -0.0394 -0.0346 385  GLY B C   
11609 O O   . GLY B 387  ? 0.3435 0.3239 0.3272 -0.0364 -0.0419 -0.0382 385  GLY B O   
11610 N N   . LEU B 388  ? 0.3030 0.2863 0.2889 -0.0409 -0.0415 -0.0301 386  LEU B N   
11611 C CA  . LEU B 388  ? 0.3004 0.2732 0.2829 -0.0454 -0.0474 -0.0296 386  LEU B CA  
11612 C C   . LEU B 388  ? 0.3247 0.3023 0.3078 -0.0516 -0.0490 -0.0267 386  LEU B C   
11613 O O   . LEU B 388  ? 0.3401 0.3299 0.3267 -0.0523 -0.0455 -0.0247 386  LEU B O   
11614 C CB  . LEU B 388  ? 0.3209 0.2872 0.3022 -0.0475 -0.0497 -0.0259 386  LEU B CB  
11615 C CG  . LEU B 388  ? 0.3390 0.3005 0.3199 -0.0411 -0.0487 -0.0291 386  LEU B CG  
11616 C CD1 . LEU B 388  ? 0.3362 0.2920 0.3156 -0.0427 -0.0508 -0.0253 386  LEU B CD1 
11617 C CD2 . LEU B 388  ? 0.3620 0.3138 0.3407 -0.0368 -0.0513 -0.0354 386  LEU B CD2 
11618 N N   . ALA B 389  ? 0.3078 0.2753 0.2876 -0.0561 -0.0548 -0.0267 387  ALA B N   
11619 C CA  . ALA B 389  ? 0.3213 0.2919 0.3014 -0.0618 -0.0574 -0.0251 387  ALA B CA  
11620 C C   . ALA B 389  ? 0.3537 0.3369 0.3386 -0.0671 -0.0553 -0.0182 387  ALA B C   
11621 O O   . ALA B 389  ? 0.3583 0.3515 0.3461 -0.0692 -0.0542 -0.0169 387  ALA B O   
11622 C CB  . ALA B 389  ? 0.4068 0.3627 0.3822 -0.0660 -0.0648 -0.0262 387  ALA B CB  
11623 N N   . ASP B 390  ? 0.3611 0.3446 0.3468 -0.0692 -0.0547 -0.0135 388  ASP B N   
11624 C CA  . ASP B 390  ? 0.3264 0.3223 0.3165 -0.0740 -0.0523 -0.0068 388  ASP B CA  
11625 C C   . ASP B 390  ? 0.2843 0.2800 0.2738 -0.0727 -0.0499 -0.0036 388  ASP B C   
11626 O O   . ASP B 390  ? 0.2832 0.2696 0.2696 -0.0684 -0.0505 -0.0067 388  ASP B O   
11627 C CB  . ASP B 390  ? 0.3243 0.3184 0.3149 -0.0827 -0.0576 -0.0027 388  ASP B CB  
11628 C CG  . ASP B 390  ? 0.3913 0.4017 0.3879 -0.0871 -0.0548 0.0031  388  ASP B CG  
11629 O OD1 . ASP B 390  ? 0.3498 0.3704 0.3492 -0.0854 -0.0496 0.0065  388  ASP B OD1 
11630 O OD2 . ASP B 390  ? 0.4277 0.4407 0.4263 -0.0921 -0.0581 0.0042  388  ASP B OD2 
11631 N N   . PHE B 391  ? 0.2790 0.2853 0.2716 -0.0766 -0.0474 0.0027  389  PHE B N   
11632 C CA  . PHE B 391  ? 0.2915 0.2974 0.2825 -0.0758 -0.0453 0.0059  389  PHE B CA  
11633 C C   . PHE B 391  ? 0.2678 0.2625 0.2554 -0.0818 -0.0508 0.0097  389  PHE B C   
11634 O O   . PHE B 391  ? 0.2935 0.2848 0.2814 -0.0882 -0.0553 0.0117  389  PHE B O   
11635 C CB  . PHE B 391  ? 0.2674 0.2895 0.2624 -0.0767 -0.0398 0.0109  389  PHE B CB  
11636 C CG  . PHE B 391  ? 0.2367 0.2690 0.2349 -0.0708 -0.0348 0.0075  389  PHE B CG  
11637 C CD1 . PHE B 391  ? 0.2556 0.2867 0.2521 -0.0637 -0.0315 0.0038  389  PHE B CD1 
11638 C CD2 . PHE B 391  ? 0.2583 0.3006 0.2610 -0.0724 -0.0339 0.0081  389  PHE B CD2 
11639 C CE1 . PHE B 391  ? 0.2751 0.3144 0.2743 -0.0585 -0.0273 0.0009  389  PHE B CE1 
11640 C CE2 . PHE B 391  ? 0.2634 0.3143 0.2688 -0.0668 -0.0296 0.0052  389  PHE B CE2 
11641 C CZ  . PHE B 391  ? 0.2626 0.3115 0.2661 -0.0600 -0.0263 0.0017  389  PHE B CZ  
11642 N N   . PRO B 392  ? 0.2900 0.2781 0.2739 -0.0800 -0.0509 0.0108  390  PRO B N   
11643 C CA  . PRO B 392  ? 0.2941 0.2723 0.2746 -0.0860 -0.0557 0.0155  390  PRO B CA  
11644 C C   . PRO B 392  ? 0.3577 0.3466 0.3398 -0.0919 -0.0532 0.0237  390  PRO B C   
11645 O O   . PRO B 392  ? 0.3111 0.2932 0.2904 -0.0974 -0.0567 0.0288  390  PRO B O   
11646 C CB  . PRO B 392  ? 0.3055 0.2729 0.2815 -0.0805 -0.0567 0.0127  390  PRO B CB  
11647 C CG  . PRO B 392  ? 0.2944 0.2730 0.2722 -0.0739 -0.0500 0.0107  390  PRO B CG  
11648 C CD  . PRO B 392  ? 0.2858 0.2743 0.2683 -0.0725 -0.0471 0.0076  390  PRO B CD  
11649 N N   . VAL B 393  ? 0.3080 0.3135 0.2945 -0.0906 -0.0472 0.0252  391  VAL B N   
11650 C CA  . VAL B 393  ? 0.3155 0.3335 0.3040 -0.0952 -0.0437 0.0327  391  VAL B CA  
11651 C C   . VAL B 393  ? 0.2931 0.3259 0.2886 -0.0974 -0.0412 0.0339  391  VAL B C   
11652 O O   . VAL B 393  ? 0.3102 0.3444 0.3081 -0.0939 -0.0411 0.0287  391  VAL B O   
11653 C CB  . VAL B 393  ? 0.2801 0.3041 0.2661 -0.0898 -0.0379 0.0333  391  VAL B CB  
11654 C CG1 . VAL B 393  ? 0.2964 0.3058 0.2755 -0.0878 -0.0410 0.0324  391  VAL B CG1 
11655 C CG2 . VAL B 393  ? 0.2754 0.3070 0.2640 -0.0819 -0.0331 0.0275  391  VAL B CG2 
11656 N N   . PHE B 394  ? 0.2736 0.3178 0.2724 -0.1035 -0.0394 0.0412  392  PHE B N   
11657 C CA  . PHE B 394  ? 0.2605 0.3211 0.2668 -0.1054 -0.0366 0.0432  392  PHE B CA  
11658 C C   . PHE B 394  ? 0.2675 0.3397 0.2757 -0.0971 -0.0296 0.0400  392  PHE B C   
11659 O O   . PHE B 394  ? 0.3027 0.3728 0.3066 -0.0914 -0.0264 0.0382  392  PHE B O   
11660 C CB  . PHE B 394  ? 0.2727 0.3436 0.2827 -0.1139 -0.0362 0.0523  392  PHE B CB  
11661 C CG  . PHE B 394  ? 0.3204 0.3792 0.3287 -0.1226 -0.0437 0.0557  392  PHE B CG  
11662 C CD1 . PHE B 394  ? 0.2784 0.3316 0.2891 -0.1264 -0.0495 0.0534  392  PHE B CD1 
11663 C CD2 . PHE B 394  ? 0.2852 0.3364 0.2885 -0.1267 -0.0453 0.0607  392  PHE B CD2 
11664 C CE1 . PHE B 394  ? 0.3007 0.3409 0.3091 -0.1343 -0.0570 0.0560  392  PHE B CE1 
11665 C CE2 . PHE B 394  ? 0.3195 0.3576 0.3208 -0.1346 -0.0528 0.0636  392  PHE B CE2 
11666 C CZ  . PHE B 394  ? 0.2990 0.3314 0.3030 -0.1384 -0.0587 0.0611  392  PHE B CZ  
11667 N N   . THR B 395  ? 0.2641 0.3477 0.2786 -0.0963 -0.0279 0.0391  393  THR B N   
11668 C CA  . THR B 395  ? 0.2867 0.3814 0.3036 -0.0887 -0.0218 0.0362  393  THR B CA  
11669 C C   . THR B 395  ? 0.2922 0.4062 0.3151 -0.0899 -0.0166 0.0418  393  THR B C   
11670 O O   . THR B 395  ? 0.3084 0.4313 0.3326 -0.0832 -0.0111 0.0399  393  THR B O   
11671 C CB  . THR B 395  ? 0.2729 0.3660 0.2919 -0.0850 -0.0232 0.0302  393  THR B CB  
11672 O OG1 . THR B 395  ? 0.2664 0.3657 0.2910 -0.0910 -0.0263 0.0328  393  THR B OG1 
11673 C CG2 . THR B 395  ? 0.3142 0.3895 0.3273 -0.0828 -0.0275 0.0244  393  THR B CG2 
11674 N N   . ARG B 396  ? 0.2906 0.4114 0.3175 -0.0980 -0.0181 0.0486  394  ARG B N   
11675 C CA  . ARG B 396  ? 0.2972 0.4372 0.3300 -0.0996 -0.0128 0.0548  394  ARG B CA  
11676 C C   . ARG B 396  ? 0.3144 0.4545 0.3435 -0.1037 -0.0115 0.0609  394  ARG B C   
11677 O O   . ARG B 396  ? 0.3188 0.4486 0.3452 -0.1108 -0.0167 0.0639  394  ARG B O   
11678 C CB  . ARG B 396  ? 0.2647 0.4160 0.3066 -0.1062 -0.0152 0.0589  394  ARG B CB  
11679 C CG  . ARG B 396  ? 0.3042 0.4568 0.3498 -0.1024 -0.0167 0.0535  394  ARG B CG  
11680 C CD  . ARG B 396  ? 0.2962 0.4637 0.3517 -0.1080 -0.0181 0.0580  394  ARG B CD  
11681 N NE  . ARG B 396  ? 0.3499 0.5163 0.4073 -0.1043 -0.0202 0.0526  394  ARG B NE  
11682 C CZ  . ARG B 396  ? 0.3859 0.5673 0.4514 -0.1035 -0.0189 0.0538  394  ARG B CZ  
11683 N NH1 . ARG B 396  ? 0.3866 0.5865 0.4602 -0.1061 -0.0155 0.0603  394  ARG B NH1 
11684 N NH2 . ARG B 396  ? 0.3467 0.5249 0.4122 -0.0997 -0.0210 0.0485  394  ARG B NH2 
11685 N N   . LYS B 397  ? 0.3075 0.4591 0.3360 -0.0994 -0.0045 0.0630  395  LYS B N   
11686 C CA  . LYS B 397  ? 0.3027 0.4550 0.3266 -0.1029 -0.0026 0.0688  395  LYS B CA  
11687 C C   . LYS B 397  ? 0.2986 0.4575 0.3276 -0.1138 -0.0051 0.0774  395  LYS B C   
11688 O O   . LYS B 397  ? 0.3344 0.4860 0.3587 -0.1194 -0.0074 0.0820  395  LYS B O   
11689 C CB  . LYS B 397  ? 0.3510 0.5167 0.3738 -0.0961 0.0057  0.0694  395  LYS B CB  
11690 C CG  . LYS B 397  ? 0.3475 0.5098 0.3618 -0.0966 0.0080  0.0729  395  LYS B CG  
11691 C CD  . LYS B 397  ? 0.3893 0.5649 0.4070 -0.1043 0.0102  0.0824  395  LYS B CD  
11692 C CE  . LYS B 397  ? 0.4056 0.5799 0.4142 -0.1038 0.0136  0.0860  395  LYS B CE  
11693 N NZ  . LYS B 397  ? 0.3865 0.5764 0.3988 -0.1110 0.0169  0.0957  395  LYS B NZ  
11694 N N   . ILE B 398  ? 0.3237 0.4959 0.3625 -0.1171 -0.0053 0.0797  396  ILE B N   
11695 C CA  . ILE B 398  ? 0.3045 0.4839 0.3492 -0.1280 -0.0079 0.0882  396  ILE B CA  
11696 C C   . ILE B 398  ? 0.3110 0.4715 0.3525 -0.1356 -0.0171 0.0881  396  ILE B C   
11697 O O   . ILE B 398  ? 0.3071 0.4664 0.3491 -0.1448 -0.0201 0.0952  396  ILE B O   
11698 C CB  . ILE B 398  ? 0.3467 0.5459 0.4034 -0.1291 -0.0060 0.0904  396  ILE B CB  
11699 C CG1 . ILE B 398  ? 0.3919 0.6048 0.4558 -0.1393 -0.0061 0.1005  396  ILE B CG1 
11700 C CG2 . ILE B 398  ? 0.3207 0.5125 0.3805 -0.1291 -0.0121 0.0848  396  ILE B CG2 
11701 C CD1 . ILE B 398  ? 0.4276 0.6631 0.5038 -0.1392 -0.0027 0.1032  396  ILE B CD1 
11702 N N   . HIS B 399  ? 0.3107 0.4559 0.3487 -0.1317 -0.0216 0.0802  397  HIS B N   
11703 C CA  . HIS B 399  ? 0.3270 0.4524 0.3606 -0.1374 -0.0302 0.0791  397  HIS B CA  
11704 C C   . HIS B 399  ? 0.3137 0.4258 0.3384 -0.1390 -0.0314 0.0814  397  HIS B C   
11705 O O   . HIS B 399  ? 0.3285 0.4308 0.3515 -0.1473 -0.0373 0.0857  397  HIS B O   
11706 C CB  . HIS B 399  ? 0.3325 0.4453 0.3634 -0.1313 -0.0335 0.0696  397  HIS B CB  
11707 C CG  . HIS B 399  ? 0.3205 0.4433 0.3591 -0.1312 -0.0342 0.0676  397  HIS B CG  
11708 N ND1 . HIS B 399  ? 0.2841 0.4007 0.3214 -0.1249 -0.0354 0.0595  397  HIS B ND1 
11709 C CD2 . HIS B 399  ? 0.3299 0.4688 0.3778 -0.1369 -0.0340 0.0729  397  HIS B CD2 
11710 C CE1 . HIS B 399  ? 0.3103 0.4381 0.3550 -0.1265 -0.0361 0.0600  397  HIS B CE1 
11711 N NE2 . HIS B 399  ? 0.2913 0.4328 0.3428 -0.1337 -0.0354 0.0679  397  HIS B NE2 
11712 N N   . THR B 400  ? 0.2985 0.4094 0.3172 -0.1310 -0.0264 0.0785  398  THR B N   
11713 C CA  . THR B 400  ? 0.3283 0.4280 0.3385 -0.1321 -0.0273 0.0811  398  THR B CA  
11714 C C   . THR B 400  ? 0.3267 0.4365 0.3385 -0.1405 -0.0256 0.0915  398  THR B C   
11715 O O   . THR B 400  ? 0.3473 0.4457 0.3542 -0.1467 -0.0300 0.0960  398  THR B O   
11716 C CB  . THR B 400  ? 0.3119 0.4106 0.3158 -0.1219 -0.0220 0.0762  398  THR B CB  
11717 O OG1 . THR B 400  ? 0.2991 0.3853 0.3007 -0.1153 -0.0247 0.0671  398  THR B OG1 
11718 C CG2 . THR B 400  ? 0.3186 0.4089 0.3138 -0.1233 -0.0222 0.0800  398  THR B CG2 
11719 N N   . ASP B 401  ? 0.3063 0.4378 0.3255 -0.1411 -0.0194 0.0957  399  ASP B N   
11720 C CA  . ASP B 401  ? 0.3312 0.4745 0.3526 -0.1491 -0.0171 0.1060  399  ASP B CA  
11721 C C   . ASP B 401  ? 0.3358 0.4743 0.3616 -0.1610 -0.0245 0.1118  399  ASP B C   
11722 O O   . ASP B 401  ? 0.3401 0.4754 0.3632 -0.1689 -0.0264 0.1194  399  ASP B O   
11723 C CB  . ASP B 401  ? 0.3502 0.5190 0.3793 -0.1463 -0.0086 0.1089  399  ASP B CB  
11724 C CG  . ASP B 401  ? 0.4068 0.5806 0.4300 -0.1356 -0.0009 0.1050  399  ASP B CG  
11725 O OD1 . ASP B 401  ? 0.3785 0.5390 0.3913 -0.1327 -0.0014 0.1033  399  ASP B OD1 
11726 O OD2 . ASP B 401  ? 0.3606 0.5514 0.3895 -0.1300 0.0053  0.1037  399  ASP B OD2 
11727 N N   . VAL B 402  ? 0.3494 0.4863 0.3815 -0.1627 -0.0292 0.1082  400  VAL B N   
11728 C CA  . VAL B 402  ? 0.3409 0.4712 0.3766 -0.1740 -0.0373 0.1127  400  VAL B CA  
11729 C C   . VAL B 402  ? 0.3860 0.4902 0.4120 -0.1763 -0.0449 0.1108  400  VAL B C   
11730 O O   . VAL B 402  ? 0.3923 0.4895 0.4173 -0.1861 -0.0500 0.1177  400  VAL B O   
11731 C CB  . VAL B 402  ? 0.3554 0.4900 0.3991 -0.1744 -0.0405 0.1085  400  VAL B CB  
11732 C CG1 . VAL B 402  ? 0.3830 0.5088 0.4296 -0.1860 -0.0497 0.1125  400  VAL B CG1 
11733 C CG2 . VAL B 402  ? 0.3781 0.5390 0.4320 -0.1720 -0.0332 0.1111  400  VAL B CG2 
11734 N N   . SER B 403  ? 0.3270 0.4167 0.3460 -0.1672 -0.0458 0.1016  401  SER B N   
11735 C CA  . SER B 403  ? 0.3778 0.4433 0.3877 -0.1677 -0.0525 0.0991  401  SER B CA  
11736 C C   . SER B 403  ? 0.3851 0.4475 0.3891 -0.1717 -0.0516 0.1067  401  SER B C   
11737 O O   . SER B 403  ? 0.3894 0.4376 0.3898 -0.1792 -0.0584 0.1109  401  SER B O   
11738 C CB  . SER B 403  ? 0.3305 0.3856 0.3349 -0.1561 -0.0516 0.0886  401  SER B CB  
11739 O OG  . SER B 403  ? 0.3521 0.3848 0.3481 -0.1555 -0.0577 0.0859  401  SER B OG  
11740 N N   . TYR B 404  ? 0.3581 0.4333 0.3603 -0.1666 -0.0434 0.1085  402  TYR B N   
11741 C CA  . TYR B 404  ? 0.3717 0.4457 0.3675 -0.1700 -0.0418 0.1159  402  TYR B CA  
11742 C C   . TYR B 404  ? 0.3948 0.4742 0.3949 -0.1829 -0.0445 0.1268  402  TYR B C   
11743 O O   . TYR B 404  ? 0.4387 0.5047 0.4330 -0.1893 -0.0495 0.1321  402  TYR B O   
11744 C CB  . TYR B 404  ? 0.3932 0.4839 0.3877 -0.1627 -0.0319 0.1161  402  TYR B CB  
11745 C CG  . TYR B 404  ? 0.3915 0.4781 0.3764 -0.1630 -0.0299 0.1212  402  TYR B CG  
11746 C CD1 . TYR B 404  ? 0.4058 0.5015 0.3912 -0.1718 -0.0282 0.1321  402  TYR B CD1 
11747 C CD2 . TYR B 404  ? 0.3674 0.4418 0.3431 -0.1545 -0.0297 0.1152  402  TYR B CD2 
11748 C CE1 . TYR B 404  ? 0.4108 0.5029 0.3867 -0.1722 -0.0264 0.1369  402  TYR B CE1 
11749 C CE2 . TYR B 404  ? 0.3669 0.4376 0.3333 -0.1548 -0.0283 0.1199  402  TYR B CE2 
11750 C CZ  . TYR B 404  ? 0.3948 0.4741 0.3609 -0.1635 -0.0266 0.1307  402  TYR B CZ  
11751 O OH  . TYR B 404  ? 0.4247 0.5004 0.3808 -0.1639 -0.0251 0.1357  402  TYR B OH  
11752 N N   . ILE B 405  ? 0.3753 0.4743 0.3858 -0.1871 -0.0414 0.1306  403  ILE B N   
11753 C CA  . ILE B 405  ? 0.4037 0.5106 0.4195 -0.1998 -0.0432 0.1417  403  ILE B CA  
11754 C C   . ILE B 405  ? 0.3997 0.4867 0.4150 -0.2085 -0.0545 0.1425  403  ILE B C   
11755 O O   . ILE B 405  ? 0.4280 0.5081 0.4409 -0.2181 -0.0587 0.1508  403  ILE B O   
11756 C CB  . ILE B 405  ? 0.4092 0.5430 0.4376 -0.2015 -0.0374 0.1452  403  ILE B CB  
11757 C CG1 . ILE B 405  ? 0.4776 0.6297 0.5049 -0.1930 -0.0263 0.1452  403  ILE B CG1 
11758 C CG2 . ILE B 405  ? 0.4224 0.5650 0.4577 -0.2146 -0.0399 0.1562  403  ILE B CG2 
11759 C CD1 . ILE B 405  ? 0.5072 0.6869 0.5465 -0.1934 -0.0195 0.1488  403  ILE B CD1 
11760 N N   . ALA B 406  ? 0.4050 0.4815 0.4216 -0.2050 -0.0596 0.1336  404  ALA B N   
11761 C CA  . ALA B 406  ? 0.4301 0.4859 0.4450 -0.2120 -0.0705 0.1329  404  ALA B CA  
11762 C C   . ALA B 406  ? 0.4673 0.4992 0.4707 -0.2115 -0.0756 0.1325  404  ALA B C   
11763 O O   . ALA B 406  ? 0.4636 0.4816 0.4649 -0.2208 -0.0834 0.1376  404  ALA B O   
11764 C CB  . ALA B 406  ? 0.4430 0.4928 0.4602 -0.2066 -0.0740 0.1225  404  ALA B CB  
11765 N N   . CYS B 407  ? 0.4410 0.4675 0.4372 -0.2008 -0.0718 0.1263  405  CYS B N   
11766 C CA  . CYS B 407  ? 0.4761 0.4811 0.4618 -0.1997 -0.0765 0.1261  405  CYS B CA  
11767 C C   . CYS B 407  ? 0.4615 0.4704 0.4438 -0.2069 -0.0747 0.1375  405  CYS B C   
11768 O O   . CYS B 407  ? 0.4718 0.4626 0.4476 -0.2119 -0.0814 0.1413  405  CYS B O   
11769 C CB  . CYS B 407  ? 0.4460 0.4457 0.4258 -0.1865 -0.0729 0.1167  405  CYS B CB  
11770 S SG  . CYS B 407  ? 0.4934 0.4845 0.4758 -0.1789 -0.0764 0.1037  405  CYS B SG  
11771 N N   . ALA B 408  ? 0.4520 0.4844 0.4386 -0.2076 -0.0659 0.1432  406  ALA B N   
11772 C CA  . ALA B 408  ? 0.4792 0.5178 0.4633 -0.2155 -0.0638 0.1549  406  ALA B CA  
11773 C C   . ALA B 408  ? 0.5018 0.5354 0.4901 -0.2297 -0.0712 0.1636  406  ALA B C   
11774 O O   . ALA B 408  ? 0.5378 0.5619 0.5201 -0.2341 -0.0746 0.1698  406  ALA B O   
11775 C CB  . ALA B 408  ? 0.4547 0.5212 0.4436 -0.2132 -0.0526 0.1589  406  ALA B CB  
11776 N N   . ALA B 409  ? 0.5145 0.5537 0.5121 -0.2321 -0.0740 0.1610  407  ALA B N   
11777 C CA  . ALA B 409  ? 0.5181 0.5514 0.5183 -0.2400 -0.0814 0.1652  407  ALA B CA  
11778 C C   . ALA B 409  ? 0.4948 0.4980 0.4864 -0.2417 -0.0920 0.1626  407  ALA B C   
11779 O O   . ALA B 409  ? 0.5383 0.5329 0.5269 -0.2478 -0.0971 0.1686  407  ALA B O   
11780 C CB  . ALA B 409  ? 0.5085 0.5532 0.5196 -0.2414 -0.0824 0.1623  407  ALA B CB  
11781 N N   . LYS B 410  ? 0.5223 0.5095 0.5098 -0.2361 -0.0954 0.1536  408  LYS B N   
11782 C CA  . LYS B 410  ? 0.5100 0.4684 0.4893 -0.2360 -0.1053 0.1500  408  LYS B CA  
11783 C C   . LYS B 410  ? 0.5438 0.4912 0.5135 -0.2365 -0.1060 0.1555  408  LYS B C   
11784 O O   . LYS B 410  ? 0.5978 0.5278 0.5624 -0.2402 -0.1138 0.1580  408  LYS B O   
11785 C CB  . LYS B 410  ? 0.4777 0.4238 0.4550 -0.2285 -0.1075 0.1386  408  LYS B CB  
11786 C CG  . LYS B 410  ? 0.5236 0.4401 0.4924 -0.2265 -0.1172 0.1335  408  LYS B CG  
11787 C CD  . LYS B 410  ? 0.5442 0.4529 0.5103 -0.2137 -0.1166 0.1204  408  LYS B CD  
11788 C CE  . LYS B 410  ? 0.5682 0.4838 0.5412 -0.2124 -0.1169 0.1135  408  LYS B CE  
11789 N NZ  . LYS B 410  ? 0.5536 0.4517 0.5259 -0.2191 -0.1274 0.1125  408  LYS B NZ  
11790 N N   . LEU B 411  ? 0.5528 0.5103 0.5196 -0.2326 -0.0980 0.1575  409  LEU B N   
11791 C CA  . LEU B 411  ? 0.5492 0.4967 0.5060 -0.2323 -0.0983 0.1625  409  LEU B CA  
11792 C C   . LEU B 411  ? 0.5734 0.5288 0.5304 -0.2398 -0.0980 0.1729  409  LEU B C   
11793 O O   . LEU B 411  ? 0.5917 0.5311 0.5414 -0.2424 -0.1038 0.1768  409  LEU B O   
11794 C CB  . LEU B 411  ? 0.5645 0.5237 0.5174 -0.2215 -0.0889 0.1590  409  LEU B CB  
11795 C CG  . LEU B 411  ? 0.5650 0.5129 0.5140 -0.2082 -0.0894 0.1461  409  LEU B CG  
11796 C CD1 . LEU B 411  ? 0.5546 0.5200 0.5031 -0.1984 -0.0791 0.1424  409  LEU B CD1 
11797 C CD2 . LEU B 411  ? 0.5172 0.4396 0.4562 -0.2063 -0.0971 0.1451  409  LEU B CD2 
11798 N N   . LEU B 412  ? 0.5739 0.5542 0.5396 -0.2430 -0.0913 0.1775  410  LEU B N   
11799 C CA  . LEU B 412  ? 0.5741 0.5640 0.5410 -0.2501 -0.0904 0.1874  410  LEU B CA  
11800 C C   . LEU B 412  ? 0.5908 0.5646 0.5580 -0.2573 -0.1010 0.1895  410  LEU B C   
11801 O O   . LEU B 412  ? 0.6233 0.5964 0.5881 -0.2632 -0.1028 0.1976  410  LEU B O   
11802 C CB  . LEU B 412  ? 0.5270 0.5470 0.5045 -0.2511 -0.0815 0.1906  410  LEU B CB  
11803 C CG  . LEU B 412  ? 0.5516 0.5889 0.5270 -0.2443 -0.0702 0.1906  410  LEU B CG  
11804 C CD1 . LEU B 412  ? 0.5515 0.6178 0.5380 -0.2434 -0.0615 0.1919  410  LEU B CD1 
11805 C CD2 . LEU B 412  ? 0.6263 0.6617 0.5923 -0.2453 -0.0680 0.1977  410  LEU B CD2 
11806 N N   . ALA B 413  ? 0.5868 0.5472 0.5563 -0.2567 -0.1081 0.1824  411  ALA B N   
11807 C CA  . ALA B 413  ? 0.6282 0.5716 0.5967 -0.2628 -0.1185 0.1838  411  ALA B CA  
11808 C C   . ALA B 413  ? 0.6807 0.5957 0.6380 -0.2606 -0.1265 0.1815  411  ALA B C   
11809 O O   . ALA B 413  ? 0.6847 0.5829 0.6399 -0.2647 -0.1357 0.1819  411  ALA B O   
11810 C CB  . ALA B 413  ? 0.5963 0.5381 0.5714 -0.2629 -0.1228 0.1771  411  ALA B CB  
11811 N N   . ALA B 414  ? 0.5695 0.4789 0.5197 -0.2542 -0.1234 0.1793  412  ALA B N   
11812 C CA  . ALA B 414  ? 0.6499 0.5326 0.5899 -0.2507 -0.1308 0.1764  412  ALA B CA  
11813 C C   . ALA B 414  ? 0.6585 0.5413 0.5905 -0.2497 -0.1274 0.1826  412  ALA B C   
11814 O O   . ALA B 414  ? 0.6573 0.5214 0.5808 -0.2443 -0.1312 0.1793  412  ALA B O   
11815 C CB  . ALA B 414  ? 0.6039 0.4739 0.5422 -0.2420 -0.1327 0.1649  412  ALA B CB  
11816 N N   . THR B 415  ? 0.6522 0.5555 0.5865 -0.2543 -0.1203 0.1913  413  THR B N   
11817 C CA  . THR B 415  ? 0.6679 0.5736 0.5942 -0.2531 -0.1160 0.1972  413  THR B CA  
11818 C C   . THR B 415  ? 0.7044 0.5874 0.6217 -0.2552 -0.1248 0.2006  413  THR B C   
11819 O O   . THR B 415  ? 0.6869 0.5675 0.5959 -0.2530 -0.1227 0.2043  413  THR B O   
11820 C CB  . THR B 415  ? 0.6249 0.5573 0.5560 -0.2579 -0.1072 0.2058  413  THR B CB  
11821 O OG1 . THR B 415  ? 0.7189 0.6525 0.6550 -0.2669 -0.1119 0.2118  413  THR B OG1 
11822 C CG2 . THR B 415  ? 0.5745 0.5299 0.5143 -0.2546 -0.0982 0.2023  413  THR B CG2 
11823 N N   . ASP B 416  ? 0.6928 0.5590 0.6110 -0.2590 -0.1346 0.1993  414  ASP B N   
11824 C CA  . ASP B 416  ? 0.6472 0.4898 0.5567 -0.2597 -0.1435 0.2012  414  ASP B CA  
11825 C C   . ASP B 416  ? 0.7410 0.5638 0.6433 -0.2501 -0.1472 0.1929  414  ASP B C   
11826 O O   . ASP B 416  ? 0.8052 0.6143 0.6987 -0.2480 -0.1506 0.1950  414  ASP B O   
11827 C CB  . ASP B 416  ? 0.8063 0.6367 0.7187 -0.2660 -0.1530 0.2017  414  ASP B CB  
11828 N N   . VAL B 417  ? 0.6343 0.4558 0.5403 -0.2442 -0.1464 0.1834  415  VAL B N   
11829 C CA  . VAL B 417  ? 0.6962 0.4992 0.5966 -0.2347 -0.1501 0.1747  415  VAL B CA  
11830 C C   . VAL B 417  ? 0.6713 0.4851 0.5702 -0.2280 -0.1416 0.1722  415  VAL B C   
11831 O O   . VAL B 417  ? 0.7329 0.5323 0.6256 -0.2203 -0.1441 0.1673  415  VAL B O   
11832 C CB  . VAL B 417  ? 0.6704 0.4616 0.5750 -0.2316 -0.1559 0.1648  415  VAL B CB  
11833 N N   . VAL B 418  ? 0.6451 0.4836 0.5494 -0.2302 -0.1319 0.1753  416  VAL B N   
11834 C CA  . VAL B 418  ? 0.6230 0.4725 0.5257 -0.2238 -0.1237 0.1728  416  VAL B CA  
11835 C C   . VAL B 418  ? 0.6096 0.4833 0.5125 -0.2273 -0.1140 0.1814  416  VAL B C   
11836 O O   . VAL B 418  ? 0.6186 0.5055 0.5268 -0.2346 -0.1121 0.1877  416  VAL B O   
11837 C CB  . VAL B 418  ? 0.5896 0.4471 0.5002 -0.2182 -0.1203 0.1628  416  VAL B CB  
11838 C CG1 . VAL B 418  ? 0.5649 0.3999 0.4749 -0.2126 -0.1289 0.1527  416  VAL B CG1 
11839 C CG2 . VAL B 418  ? 0.5786 0.4558 0.4995 -0.2260 -0.1162 0.1664  416  VAL B CG2 
11840 N N   . PHE B 419  ? 0.5697 0.4499 0.4669 -0.2209 -0.1076 0.1808  417  PHE B N   
11841 C CA  . PHE B 419  ? 0.5816 0.4850 0.4776 -0.2223 -0.0974 0.1876  417  PHE B CA  
11842 C C   . PHE B 419  ? 0.5655 0.4897 0.4686 -0.2139 -0.0882 0.1792  417  PHE B C   
11843 O O   . PHE B 419  ? 0.5249 0.4482 0.4248 -0.2024 -0.0855 0.1702  417  PHE B O   
11844 C CB  . PHE B 419  ? 0.5500 0.4473 0.4335 -0.2184 -0.0967 0.1910  417  PHE B CB  
11845 C CG  . PHE B 419  ? 0.5621 0.4824 0.4429 -0.2185 -0.0861 0.1970  417  PHE B CG  
11846 C CD1 . PHE B 419  ? 0.5587 0.4948 0.4438 -0.2256 -0.0825 0.2047  417  PHE B CD1 
11847 C CD2 . PHE B 419  ? 0.5368 0.4651 0.4125 -0.2077 -0.0796 0.1910  417  PHE B CD2 
11848 C CE1 . PHE B 419  ? 0.5574 0.5151 0.4402 -0.2245 -0.0724 0.2091  417  PHE B CE1 
11849 C CE2 . PHE B 419  ? 0.5284 0.4769 0.4005 -0.2075 -0.0700 0.1962  417  PHE B CE2 
11850 C CZ  . PHE B 419  ? 0.5291 0.4925 0.4044 -0.2162 -0.0661 0.2057  417  PHE B CZ  
11851 N N   . PRO B 420  ? 0.5262 0.4693 0.4393 -0.2192 -0.0834 0.1816  418  PRO B N   
11852 C CA  . PRO B 420  ? 0.5025 0.4641 0.4228 -0.2111 -0.0754 0.1733  418  PRO B CA  
11853 C C   . PRO B 420  ? 0.5287 0.5089 0.4448 -0.2054 -0.0650 0.1748  418  PRO B C   
11854 O O   . PRO B 420  ? 0.4982 0.4898 0.4117 -0.2118 -0.0608 0.1851  418  PRO B O   
11855 C CB  . PRO B 420  ? 0.4860 0.4610 0.4181 -0.2200 -0.0748 0.1772  418  PRO B CB  
11856 C CG  . PRO B 420  ? 0.5085 0.4661 0.4400 -0.2302 -0.0848 0.1830  418  PRO B CG  
11857 C CD  . PRO B 420  ? 0.5504 0.4971 0.4705 -0.2304 -0.0867 0.1888  418  PRO B CD  
11858 N N   . GLN B 421  ? 0.4804 0.4638 0.3959 -0.1934 -0.0609 0.1644  419  GLN B N   
11859 C CA  . GLN B 421  ? 0.5025 0.5015 0.4135 -0.1861 -0.0515 0.1634  419  GLN B CA  
11860 C C   . GLN B 421  ? 0.4790 0.4950 0.3994 -0.1797 -0.0449 0.1557  419  GLN B C   
11861 O O   . GLN B 421  ? 0.4412 0.4496 0.3641 -0.1721 -0.0471 0.1454  419  GLN B O   
11862 C CB  . GLN B 421  ? 0.4513 0.4352 0.3514 -0.1774 -0.0539 0.1581  419  GLN B CB  
11863 C CG  . GLN B 421  ? 0.4792 0.4427 0.3705 -0.1829 -0.0622 0.1646  419  GLN B CG  
11864 C CD  . GLN B 421  ? 0.5126 0.4584 0.3956 -0.1740 -0.0669 0.1578  419  GLN B CD  
11865 O OE1 . GLN B 421  ? 0.4665 0.4007 0.3530 -0.1682 -0.0715 0.1485  419  GLN B OE1 
11866 N NE2 . GLN B 421  ? 0.4786 0.4222 0.3504 -0.1730 -0.0658 0.1626  419  GLN B NE2 
11867 N N   . PHE B 422  ? 0.4939 0.5328 0.4196 -0.1826 -0.0369 0.1608  420  PHE B N   
11868 C CA  . PHE B 422  ? 0.4458 0.5015 0.3817 -0.1777 -0.0312 0.1546  420  PHE B CA  
11869 C C   . PHE B 422  ? 0.4743 0.5418 0.4056 -0.1670 -0.0226 0.1497  420  PHE B C   
11870 O O   . PHE B 422  ? 0.4562 0.5402 0.3853 -0.1678 -0.0151 0.1555  420  PHE B O   
11871 C CB  . PHE B 422  ? 0.4537 0.5277 0.4000 -0.1870 -0.0283 0.1625  420  PHE B CB  
11872 C CG  . PHE B 422  ? 0.4741 0.5363 0.4246 -0.1982 -0.0372 0.1677  420  PHE B CG  
11873 C CD1 . PHE B 422  ? 0.4692 0.5182 0.4245 -0.1975 -0.0443 0.1604  420  PHE B CD1 
11874 C CD2 . PHE B 422  ? 0.4379 0.5020 0.3870 -0.2096 -0.0386 0.1799  420  PHE B CD2 
11875 C CE1 . PHE B 422  ? 0.4836 0.5207 0.4422 -0.2076 -0.0529 0.1647  420  PHE B CE1 
11876 C CE2 . PHE B 422  ? 0.4878 0.5399 0.4406 -0.2203 -0.0473 0.1848  420  PHE B CE2 
11877 C CZ  . PHE B 422  ? 0.5235 0.5617 0.4809 -0.2191 -0.0547 0.1768  420  PHE B CZ  
11878 N N   . ALA B 423  ? 0.4039 0.4627 0.3337 -0.1570 -0.0237 0.1389  421  ALA B N   
11879 C CA  . ALA B 423  ? 0.4426 0.5099 0.3680 -0.1465 -0.0166 0.1330  421  ALA B CA  
11880 C C   . ALA B 423  ? 0.4395 0.5249 0.3752 -0.1426 -0.0104 0.1287  421  ALA B C   
11881 O O   . ALA B 423  ? 0.4427 0.5238 0.3854 -0.1399 -0.0134 0.1217  421  ALA B O   
11882 C CB  . ALA B 423  ? 0.3904 0.4394 0.3094 -0.1382 -0.0212 0.1241  421  ALA B CB  
11883 N N   . THR B 424  ? 0.4422 0.5477 0.3784 -0.1417 -0.0018 0.1326  422  THR B N   
11884 C CA  . THR B 424  ? 0.4093 0.5325 0.3546 -0.1367 0.0045  0.1284  422  THR B CA  
11885 C C   . THR B 424  ? 0.4158 0.5579 0.3575 -0.1330 0.0143  0.1316  422  THR B C   
11886 O O   . THR B 424  ? 0.4241 0.5711 0.3601 -0.1381 0.0166  0.1402  422  THR B O   
11887 C CB  . THR B 424  ? 0.4467 0.5786 0.4051 -0.1445 0.0027  0.1321  422  THR B CB  
11888 O OG1 . THR B 424  ? 0.3991 0.5477 0.3662 -0.1387 0.0086  0.1276  422  THR B OG1 
11889 C CG2 . THR B 424  ? 0.4209 0.5635 0.3808 -0.1554 0.0043  0.1445  422  THR B CG2 
11890 N N   . HIS B 425  ? 0.4159 0.5684 0.3607 -0.1238 0.0199  0.1246  423  HIS B N   
11891 C CA  . HIS B 425  ? 0.4218 0.5937 0.3648 -0.1189 0.0296  0.1262  423  HIS B CA  
11892 C C   . HIS B 425  ? 0.4535 0.6471 0.4098 -0.1207 0.0347  0.1288  423  HIS B C   
11893 O O   . HIS B 425  ? 0.4329 0.6442 0.3896 -0.1155 0.0431  0.1292  423  HIS B O   
11894 C CB  . HIS B 425  ? 0.3807 0.5483 0.3168 -0.1067 0.0323  0.1164  423  HIS B CB  
11895 C CG  . HIS B 425  ? 0.4633 0.6121 0.3861 -0.1043 0.0281  0.1141  423  HIS B CG  
11896 N ND1 . HIS B 425  ? 0.4873 0.6227 0.4063 -0.0963 0.0250  0.1045  423  HIS B ND1 
11897 C CD2 . HIS B 425  ? 0.4617 0.6033 0.3743 -0.1091 0.0262  0.1205  423  HIS B CD2 
11898 C CE1 . HIS B 425  ? 0.4673 0.5883 0.3747 -0.0961 0.0213  0.1049  423  HIS B CE1 
11899 N NE2 . HIS B 425  ? 0.4314 0.5557 0.3345 -0.1036 0.0219  0.1145  423  HIS B NE2 
11900 N N   . ASN B 426  ? 0.3913 0.5838 0.3584 -0.1275 0.0295  0.1304  424  ASN B N   
11901 C CA  . ASN B 426  ? 0.4355 0.6471 0.4165 -0.1291 0.0328  0.1319  424  ASN B CA  
11902 C C   . ASN B 426  ? 0.4168 0.6421 0.4028 -0.1402 0.0345  0.1440  424  ASN B C   
11903 O O   . ASN B 426  ? 0.3944 0.6096 0.3813 -0.1502 0.0276  0.1494  424  ASN B O   
11904 C CB  . ASN B 426  ? 0.4277 0.6294 0.4168 -0.1297 0.0259  0.1260  424  ASN B CB  
11905 C CG  . ASN B 426  ? 0.4516 0.6721 0.4545 -0.1294 0.0290  0.1260  424  ASN B CG  
11906 O OD1 . ASN B 426  ? 0.4721 0.7112 0.4822 -0.1350 0.0329  0.1339  424  ASN B OD1 
11907 N ND2 . ASN B 426  ? 0.3975 0.6136 0.4044 -0.1230 0.0271  0.1173  424  ASN B ND2 
11908 N N   . ALA B 427  ? 0.4761 0.7247 0.4655 -0.1382 0.0435  0.1483  425  ALA B N   
11909 C CA  . ALA B 427  ? 0.4835 0.7449 0.4779 -0.1465 0.0453  0.1582  425  ALA B CA  
11910 C C   . ALA B 427  ? 0.4214 0.6855 0.4300 -0.1549 0.0394  0.1611  425  ALA B C   
11911 O O   . ALA B 427  ? 0.4247 0.6872 0.4356 -0.1639 0.0356  0.1682  425  ALA B O   
11912 C CB  . ALA B 427  ? 0.4845 0.7665 0.4808 -0.1384 0.0549  0.1579  425  ALA B CB  
11913 N N   . GLN B 428  ? 0.4571 0.7247 0.4747 -0.1521 0.0382  0.1556  426  GLN B N   
11914 C CA  . GLN B 428  ? 0.4809 0.7495 0.5109 -0.1599 0.0318  0.1577  426  GLN B CA  
11915 C C   . GLN B 428  ? 0.4583 0.7048 0.4841 -0.1696 0.0219  0.1599  426  GLN B C   
11916 O O   . GLN B 428  ? 0.4543 0.6987 0.4850 -0.1787 0.0165  0.1656  426  GLN B O   
11917 C CB  . GLN B 428  ? 0.4864 0.7623 0.5259 -0.1543 0.0324  0.1510  426  GLN B CB  
11918 C CG  . GLN B 428  ? 0.4845 0.7664 0.5375 -0.1608 0.0272  0.1532  426  GLN B CG  
11919 C CD  . GLN B 428  ? 0.4934 0.7559 0.5461 -0.1704 0.0167  0.1538  426  GLN B CD  
11920 O OE1 . GLN B 428  ? 0.5094 0.7537 0.5546 -0.1688 0.0128  0.1485  426  GLN B OE1 
11921 N NE2 . GLN B 428  ? 0.4362 0.7003 0.4962 -0.1789 0.0114  0.1590  426  GLN B NE2 
11922 N N   . THR B 429  ? 0.4664 0.6927 0.4826 -0.1650 0.0183  0.1529  427  THR B N   
11923 C CA  . THR B 429  ? 0.4536 0.6554 0.4642 -0.1713 0.0085  0.1530  427  THR B CA  
11924 C C   . THR B 429  ? 0.4410 0.6400 0.4451 -0.1803 0.0077  0.1634  427  THR B C   
11925 O O   . THR B 429  ? 0.4248 0.6141 0.4308 -0.1910 0.0004  0.1690  427  THR B O   
11926 C CB  . THR B 429  ? 0.4301 0.6111 0.4306 -0.1618 0.0055  0.1425  427  THR B CB  
11927 O OG1 . THR B 429  ? 0.4343 0.6196 0.4400 -0.1528 0.0075  0.1333  427  THR B OG1 
11928 C CG2 . THR B 429  ? 0.4174 0.5739 0.4142 -0.1676 -0.0050 0.1416  427  THR B CG2 
11929 N N   . LEU B 430  ? 0.4558 0.6622 0.4517 -0.1761 0.0149  0.1659  428  LEU B N   
11930 C CA  . LEU B 430  ? 0.4374 0.6396 0.4256 -0.1822 0.0142  0.1742  428  LEU B CA  
11931 C C   . LEU B 430  ? 0.5022 0.7157 0.5005 -0.1897 0.0131  0.1812  428  LEU B C   
11932 O O   . LEU B 430  ? 0.4921 0.6942 0.4888 -0.1985 0.0065  0.1869  428  LEU B O   
11933 C CB  . LEU B 430  ? 0.4566 0.6671 0.4347 -0.1740 0.0230  0.1739  428  LEU B CB  
11934 C CG  . LEU B 430  ? 0.4694 0.6746 0.4360 -0.1765 0.0237  0.1802  428  LEU B CG  
11935 C CD1 . LEU B 430  ? 0.4995 0.7092 0.4550 -0.1662 0.0314  0.1763  428  LEU B CD1 
11936 C CD2 . LEU B 430  ? 0.5348 0.7544 0.5081 -0.1821 0.0261  0.1880  428  LEU B CD2 
11937 N N   . ALA B 431  ? 0.4821 0.7179 0.4909 -0.1862 0.0194  0.1809  429  ALA B N   
11938 C CA  . ALA B 431  ? 0.4916 0.7398 0.5102 -0.1931 0.0188  0.1877  429  ALA B CA  
11939 C C   . ALA B 431  ? 0.4790 0.7155 0.5044 -0.2025 0.0085  0.1891  429  ALA B C   
11940 O O   . ALA B 431  ? 0.5275 0.7612 0.5546 -0.2113 0.0040  0.1960  429  ALA B O   
11941 C CB  . ALA B 431  ? 0.4809 0.7542 0.5100 -0.1866 0.0269  0.1862  429  ALA B CB  
11942 N N   . ALA B 432  ? 0.4769 0.7058 0.5059 -0.2007 0.0044  0.1823  430  ALA B N   
11943 C CA  . ALA B 432  ? 0.4547 0.6712 0.4892 -0.2088 -0.0057 0.1824  430  ALA B CA  
11944 C C   . ALA B 432  ? 0.4853 0.6786 0.5107 -0.2164 -0.0139 0.1861  430  ALA B C   
11945 O O   . ALA B 432  ? 0.4809 0.6687 0.5100 -0.2250 -0.0208 0.1906  430  ALA B O   
11946 C CB  . ALA B 432  ? 0.4632 0.6735 0.5007 -0.2045 -0.0083 0.1737  430  ALA B CB  
11947 N N   . ILE B 433  ? 0.5087 0.6875 0.5219 -0.2131 -0.0138 0.1841  431  ILE B N   
11948 C CA  . ILE B 433  ? 0.5579 0.7136 0.5619 -0.2195 -0.0218 0.1874  431  ILE B CA  
11949 C C   . ILE B 433  ? 0.4881 0.6500 0.4898 -0.2246 -0.0201 0.1965  431  ILE B C   
11950 O O   . ILE B 433  ? 0.5128 0.6624 0.5135 -0.2329 -0.0276 0.2013  431  ILE B O   
11951 C CB  . ILE B 433  ? 0.5336 0.6724 0.5252 -0.2141 -0.0222 0.1828  431  ILE B CB  
11952 C CG1 . ILE B 433  ? 0.5594 0.6915 0.5539 -0.2094 -0.0245 0.1736  431  ILE B CG1 
11953 C CG2 . ILE B 433  ? 0.5365 0.6512 0.5183 -0.2199 -0.0307 0.1863  431  ILE B CG2 
11954 C CD1 . ILE B 433  ? 0.5534 0.6657 0.5362 -0.1997 -0.0266 0.1649  431  ILE B CD1 
11955 N N   . TYR B 434  ? 0.5403 0.7212 0.5410 -0.2195 -0.0101 0.1987  432  TYR B N   
11956 C CA  . TYR B 434  ? 0.5333 0.7217 0.5314 -0.2237 -0.0074 0.2072  432  TYR B CA  
11957 C C   . TYR B 434  ? 0.5682 0.7632 0.5769 -0.2330 -0.0116 0.2134  432  TYR B C   
11958 O O   . TYR B 434  ? 0.5774 0.7663 0.5830 -0.2404 -0.0153 0.2206  432  TYR B O   
11959 C CB  . TYR B 434  ? 0.5222 0.7322 0.5192 -0.2155 0.0046  0.2071  432  TYR B CB  
11960 C CG  . TYR B 434  ? 0.5425 0.7661 0.5397 -0.2190 0.0092  0.2156  432  TYR B CG  
11961 C CD1 . TYR B 434  ? 0.5479 0.7607 0.5334 -0.2222 0.0080  0.2209  432  TYR B CD1 
11962 C CD2 . TYR B 434  ? 0.5832 0.8306 0.5920 -0.2189 0.0150  0.2182  432  TYR B CD2 
11963 C CE1 . TYR B 434  ? 0.5880 0.8137 0.5735 -0.2256 0.0125  0.2288  432  TYR B CE1 
11964 C CE2 . TYR B 434  ? 0.5706 0.8311 0.5798 -0.2221 0.0196  0.2260  432  TYR B CE2 
11965 C CZ  . TYR B 434  ? 0.5930 0.8427 0.5905 -0.2255 0.0184  0.2313  432  TYR B CZ  
11966 O OH  . TYR B 434  ? 0.5483 0.8112 0.5460 -0.2289 0.0232  0.2392  432  TYR B OH  
11967 N N   . HIS B 435  ? 0.5641 0.7709 0.5851 -0.2328 -0.0116 0.2107  433  HIS B N   
11968 C CA  . HIS B 435  ? 0.5623 0.7758 0.5937 -0.2413 -0.0159 0.2163  433  HIS B CA  
11969 C C   . HIS B 435  ? 0.5798 0.7716 0.6117 -0.2485 -0.0280 0.2149  433  HIS B C   
11970 O O   . HIS B 435  ? 0.5875 0.7777 0.6236 -0.2573 -0.0336 0.2208  433  HIS B O   
11971 C CB  . HIS B 435  ? 0.5776 0.8153 0.6220 -0.2375 -0.0100 0.2146  433  HIS B CB  
11972 C CG  . HIS B 435  ? 0.5899 0.8507 0.6359 -0.2328 0.0009  0.2183  433  HIS B CG  
11973 N ND1 . HIS B 435  ? 0.5569 0.8272 0.6045 -0.2389 0.0026  0.2272  433  HIS B ND1 
11974 C CD2 . HIS B 435  ? 0.5713 0.8470 0.6169 -0.2225 0.0106  0.2140  433  HIS B CD2 
11975 C CE1 . HIS B 435  ? 0.5596 0.8498 0.6078 -0.2324 0.0130  0.2282  433  HIS B CE1 
11976 N NE2 . HIS B 435  ? 0.5504 0.8440 0.5974 -0.2221 0.0180  0.2201  433  HIS B NE2 
11977 N N   . MET B 436  ? 0.5917 0.7664 0.6189 -0.2448 -0.0321 0.2073  434  MET B N   
11978 C CA  . MET B 436  ? 0.5454 0.6977 0.5717 -0.2504 -0.0437 0.2049  434  MET B CA  
11979 C C   . MET B 436  ? 0.5943 0.7259 0.6107 -0.2564 -0.0504 0.2097  434  MET B C   
11980 O O   . MET B 436  ? 0.5838 0.7000 0.6006 -0.2633 -0.0600 0.2108  434  MET B O   
11981 C CB  . MET B 436  ? 0.5709 0.7117 0.5946 -0.2438 -0.0452 0.1950  434  MET B CB  
11982 C CG  . MET B 436  ? 0.5884 0.7021 0.6077 -0.2472 -0.0566 0.1908  434  MET B CG  
11983 S SD  . MET B 436  ? 0.6567 0.7609 0.6732 -0.2384 -0.0562 0.1794  434  MET B SD  
11984 C CE  . MET B 436  ? 0.4993 0.6292 0.5297 -0.2348 -0.0503 0.1762  434  MET B CE  
11985 N N   . ALA B 437  ? 0.5983 0.7292 0.6053 -0.2537 -0.0455 0.2125  435  ALA B N   
11986 C CA  . ALA B 437  ? 0.6071 0.7181 0.6039 -0.2585 -0.0517 0.2170  435  ALA B CA  
11987 C C   . ALA B 437  ? 0.6710 0.7879 0.6708 -0.2675 -0.0536 0.2267  435  ALA B C   
11988 O O   . ALA B 437  ? 0.7089 0.8072 0.7022 -0.2732 -0.0612 0.2304  435  ALA B O   
11989 C CB  . ALA B 437  ? 0.5492 0.6577 0.5344 -0.2521 -0.0459 0.2167  435  ALA B CB  
11990 N N   . GLY B 438  ? 0.6516 0.7936 0.6613 -0.2689 -0.0470 0.2309  436  GLY B N   
11991 C CA  . GLY B 438  ? 0.6876 0.8369 0.7014 -0.2778 -0.0486 0.2404  436  GLY B CA  
11992 C C   . GLY B 438  ? 0.7623 0.9226 0.7705 -0.2774 -0.0410 0.2473  436  GLY B C   
11993 O O   . GLY B 438  ? 0.6857 0.8563 0.6900 -0.2692 -0.0320 0.2447  436  GLY B O   
11994 N N   . LYS B 439  ? 0.7320 0.8895 0.7392 -0.2862 -0.0447 0.2561  437  LYS B N   
11995 C CA  . LYS B 439  ? 0.6824 0.8504 0.6844 -0.2868 -0.0379 0.2634  437  LYS B CA  
11996 C C   . LYS B 439  ? 0.7443 0.8903 0.7330 -0.2900 -0.0434 0.2669  437  LYS B C   
11997 O O   . LYS B 439  ? 0.7927 0.9449 0.7744 -0.2887 -0.0373 0.2717  437  LYS B O   
11998 C CB  . LYS B 439  ? 0.7454 0.9330 0.7577 -0.2944 -0.0358 0.2722  437  LYS B CB  
11999 C CG  . LYS B 439  ? 0.6959 0.9043 0.7223 -0.2925 -0.0320 0.2696  437  LYS B CG  
12000 C CD  . LYS B 439  ? 0.7012 0.9379 0.7344 -0.2925 -0.0221 0.2760  437  LYS B CD  
12001 C CE  . LYS B 439  ? 0.7774 1.0350 0.8179 -0.2827 -0.0129 0.2698  437  LYS B CE  
12002 N NZ  . LYS B 439  ? 0.7735 1.0356 0.8044 -0.2728 -0.0035 0.2664  437  LYS B NZ  
12003 N N   . ASP B 440  ? 0.7366 0.8569 0.7213 -0.2937 -0.0546 0.2647  438  ASP B N   
12004 C CA  . ASP B 440  ? 0.7908 0.8893 0.7635 -0.2969 -0.0609 0.2683  438  ASP B CA  
12005 C C   . ASP B 440  ? 0.8616 0.9484 0.8223 -0.2879 -0.0586 0.2624  438  ASP B C   
12006 O O   . ASP B 440  ? 0.9146 0.9768 0.8679 -0.2868 -0.0667 0.2584  438  ASP B O   
12007 C CB  . ASP B 440  ? 0.7588 0.8342 0.7321 -0.3039 -0.0741 0.2680  438  ASP B CB  
12008 N N   . PHE B 441  ? 0.8477 0.9527 0.8064 -0.2809 -0.0474 0.2619  439  PHE B N   
12009 C CA  . PHE B 441  ? 0.7562 0.8541 0.7045 -0.2714 -0.0439 0.2556  439  PHE B CA  
12010 C C   . PHE B 441  ? 0.7548 0.8421 0.6894 -0.2715 -0.0441 0.2605  439  PHE B C   
12011 O O   . PHE B 441  ? 0.7394 0.8376 0.6727 -0.2756 -0.0402 0.2686  439  PHE B O   
12012 C CB  . PHE B 441  ? 0.6901 0.8122 0.6425 -0.2630 -0.0320 0.2517  439  PHE B CB  
12013 N N   . HIS B 442  ? 0.7843 0.8503 0.7084 -0.2669 -0.0488 0.2556  440  HIS B N   
12014 C CA  . HIS B 442  ? 0.7347 0.7895 0.6448 -0.2657 -0.0494 0.2593  440  HIS B CA  
12015 C C   . HIS B 442  ? 0.6799 0.7206 0.5807 -0.2565 -0.0503 0.2513  440  HIS B C   
12016 O O   . HIS B 442  ? 0.6927 0.7305 0.5980 -0.2523 -0.0515 0.2435  440  HIS B O   
12017 C CB  . HIS B 442  ? 0.7647 0.8001 0.6715 -0.2744 -0.0598 0.2655  440  HIS B CB  
12018 C CG  . HIS B 442  ? 0.7910 0.8008 0.6976 -0.2752 -0.0714 0.2602  440  HIS B CG  
12019 N ND1 . HIS B 442  ? 0.7918 0.7791 0.6875 -0.2702 -0.0770 0.2559  440  HIS B ND1 
12020 C CD2 . HIS B 442  ? 0.7770 0.7801 0.6926 -0.2801 -0.0787 0.2581  440  HIS B CD2 
12021 C CE1 . HIS B 442  ? 0.7732 0.7410 0.6714 -0.2716 -0.0869 0.2514  440  HIS B CE1 
12022 N NE2 . HIS B 442  ? 0.8141 0.7907 0.7239 -0.2776 -0.0882 0.2524  440  HIS B NE2 
12023 N N   . VAL B 443  ? 0.6623 0.6946 0.5497 -0.2535 -0.0497 0.2533  441  VAL B N   
12024 C CA  . VAL B 443  ? 0.6714 0.6894 0.5488 -0.2449 -0.0512 0.2464  441  VAL B CA  
12025 C C   . VAL B 443  ? 0.6724 0.6619 0.5473 -0.2471 -0.0639 0.2440  441  VAL B C   
12026 O O   . VAL B 443  ? 0.7162 0.6931 0.5888 -0.2537 -0.0710 0.2498  441  VAL B O   
12027 C CB  . VAL B 443  ? 0.6973 0.7176 0.5611 -0.2403 -0.0459 0.2493  441  VAL B CB  
12028 C CG1 . VAL B 443  ? 0.7226 0.7283 0.5763 -0.2314 -0.0480 0.2420  441  VAL B CG1 
12029 C CG2 . VAL B 443  ? 0.7041 0.7526 0.5704 -0.2374 -0.0331 0.2509  441  VAL B CG2 
12030 N N   . GLY B 444  ? 0.6826 0.6618 0.5579 -0.2412 -0.0668 0.2354  442  GLY B N   
12031 C CA  . GLY B 444  ? 0.6277 0.5816 0.5030 -0.2424 -0.0783 0.2316  442  GLY B CA  
12032 C C   . GLY B 444  ? 0.6684 0.6235 0.5564 -0.2457 -0.0815 0.2277  442  GLY B C   
12033 O O   . GLY B 444  ? 0.6441 0.5789 0.5323 -0.2447 -0.0902 0.2222  442  GLY B O   
12034 N N   . LYS B 445  ? 0.6761 0.6541 0.5745 -0.2492 -0.0749 0.2300  443  LYS B N   
12035 C CA  . LYS B 445  ? 0.6330 0.6138 0.5435 -0.2521 -0.0777 0.2263  443  LYS B CA  
12036 C C   . LYS B 445  ? 0.6136 0.5981 0.5272 -0.2444 -0.0741 0.2171  443  LYS B C   
12037 O O   . LYS B 445  ? 0.6098 0.5786 0.5252 -0.2430 -0.0809 0.2105  443  LYS B O   
12038 C CB  . LYS B 445  ? 0.6767 0.6812 0.5976 -0.2585 -0.0723 0.2324  443  LYS B CB  
12039 N N   . TYR B 446  ? 0.5982 0.6035 0.5121 -0.2391 -0.0633 0.2164  444  TYR B N   
12040 C CA  . TYR B 446  ? 0.5799 0.5897 0.4948 -0.2311 -0.0589 0.2082  444  TYR B CA  
12041 C C   . TYR B 446  ? 0.5708 0.5976 0.4796 -0.2247 -0.0483 0.2092  444  TYR B C   
12042 O O   . TYR B 446  ? 0.5984 0.6340 0.5031 -0.2268 -0.0443 0.2159  444  TYR B O   
12043 C CB  . TYR B 446  ? 0.5218 0.5443 0.4507 -0.2325 -0.0575 0.2044  444  TYR B CB  
12044 C CG  . TYR B 446  ? 0.5767 0.6268 0.5147 -0.2351 -0.0493 0.2092  444  TYR B CG  
12045 C CD1 . TYR B 446  ? 0.5705 0.6425 0.5105 -0.2285 -0.0384 0.2071  444  TYR B CD1 
12046 C CD2 . TYR B 446  ? 0.5675 0.6217 0.5124 -0.2438 -0.0526 0.2156  444  TYR B CD2 
12047 C CE1 . TYR B 446  ? 0.6116 0.7086 0.5603 -0.2300 -0.0310 0.2112  444  TYR B CE1 
12048 C CE2 . TYR B 446  ? 0.6012 0.6805 0.5547 -0.2460 -0.0453 0.2201  444  TYR B CE2 
12049 C CZ  . TYR B 446  ? 0.6147 0.7155 0.5704 -0.2388 -0.0344 0.2177  444  TYR B CZ  
12050 O OH  . TYR B 446  ? 0.7016 0.8273 0.6663 -0.2402 -0.0273 0.2219  444  TYR B OH  
12051 N N   . GLU B 447  ? 0.5687 0.5995 0.4762 -0.2167 -0.0437 0.2023  445  GLU B N   
12052 C CA  . GLU B 447  ? 0.5514 0.5986 0.4529 -0.2096 -0.0336 0.2019  445  GLU B CA  
12053 C C   . GLU B 447  ? 0.4970 0.5566 0.4055 -0.2016 -0.0279 0.1929  445  GLU B C   
12054 O O   . GLU B 447  ? 0.4708 0.5224 0.3867 -0.1994 -0.0326 0.1852  445  GLU B O   
12055 C CB  . GLU B 447  ? 0.5141 0.5461 0.3998 -0.2049 -0.0356 0.2017  445  GLU B CB  
12056 C CG  . GLU B 447  ? 0.5038 0.5199 0.3877 -0.1940 -0.0399 0.1888  445  GLU B CG  
12057 C CD  . GLU B 447  ? 0.4991 0.4995 0.3688 -0.1888 -0.0432 0.1878  445  GLU B CD  
12058 O OE1 . GLU B 447  ? 0.5029 0.5037 0.3633 -0.1939 -0.0423 0.1975  445  GLU B OE1 
12059 O OE2 . GLU B 447  ? 0.4929 0.4807 0.3609 -0.1797 -0.0468 0.1777  445  GLU B OE2 
12060 N N   . PHE B 448  ? 0.4779 0.5571 0.3845 -0.1956 -0.0177 0.1923  446  PHE B N   
12061 C CA  . PHE B 448  ? 0.5137 0.6023 0.4248 -0.1843 -0.0123 0.1812  446  PHE B CA  
12062 C C   . PHE B 448  ? 0.5086 0.5862 0.4079 -0.1735 -0.0122 0.1737  446  PHE B C   
12063 O O   . PHE B 448  ? 0.4961 0.5636 0.3835 -0.1746 -0.0143 0.1780  446  PHE B O   
12064 C CB  . PHE B 448  ? 0.5118 0.6289 0.4291 -0.1836 -0.0014 0.1844  446  PHE B CB  
12065 N N   . GLN B 449  ? 0.4569 0.5359 0.3594 -0.1632 -0.0101 0.1624  447  GLN B N   
12066 C CA  . GLN B 449  ? 0.4828 0.5529 0.3753 -0.1527 -0.0097 0.1547  447  GLN B CA  
12067 C C   . GLN B 449  ? 0.4896 0.5751 0.3856 -0.1429 -0.0017 0.1468  447  GLN B C   
12068 O O   . GLN B 449  ? 0.4615 0.5585 0.3691 -0.1427 0.0009  0.1442  447  GLN B O   
12069 C CB  . GLN B 449  ? 0.4141 0.4605 0.3055 -0.1497 -0.0193 0.1475  447  GLN B CB  
12070 C CG  . GLN B 449  ? 0.4499 0.4783 0.3379 -0.1583 -0.0283 0.1541  447  GLN B CG  
12071 C CD  . GLN B 449  ? 0.4770 0.4824 0.3599 -0.1529 -0.0365 0.1472  447  GLN B CD  
12072 O OE1 . GLN B 449  ? 0.4664 0.4696 0.3510 -0.1436 -0.0360 0.1370  447  GLN B OE1 
12073 N NE2 . GLN B 449  ? 0.4479 0.4364 0.3250 -0.1587 -0.0441 0.1529  447  GLN B NE2 
12074 N N   . CYS B 450  ? 0.4219 0.5072 0.3075 -0.1349 0.0018  0.1431  448  CYS B N   
12075 C CA  . CYS B 450  ? 0.4562 0.5533 0.3436 -0.1249 0.0087  0.1350  448  CYS B CA  
12076 C C   . CYS B 450  ? 0.4400 0.5241 0.3167 -0.1159 0.0066  0.1275  448  CYS B C   
12077 O O   . CYS B 450  ? 0.4773 0.5455 0.3451 -0.1174 0.0007  0.1293  448  CYS B O   
12078 C CB  . CYS B 450  ? 0.4891 0.6091 0.3755 -0.1247 0.0189  0.1402  448  CYS B CB  
12079 S SG  . CYS B 450  ? 0.4965 0.6162 0.3647 -0.1239 0.0223  0.1461  448  CYS B SG  
12080 N N   . LEU B 451  ? 0.4250 0.5161 0.3030 -0.1066 0.0114  0.1192  449  LEU B N   
12081 C CA  . LEU B 451  ? 0.4882 0.5692 0.3573 -0.0976 0.0100  0.1114  449  LEU B CA  
12082 C C   . LEU B 451  ? 0.5130 0.6031 0.3700 -0.0939 0.0167  0.1136  449  LEU B C   
12083 O O   . LEU B 451  ? 0.4837 0.5922 0.3427 -0.0935 0.0248  0.1163  449  LEU B O   
12084 C CB  . LEU B 451  ? 0.5039 0.5861 0.3812 -0.0899 0.0109  0.1010  449  LEU B CB  
12085 C CG  . LEU B 451  ? 0.5703 0.6432 0.4407 -0.0805 0.0095  0.0921  449  LEU B CG  
12086 C CD1 . LEU B 451  ? 0.5903 0.6425 0.4567 -0.0815 0.0003  0.0907  449  LEU B CD1 
12087 C CD2 . LEU B 451  ? 0.5877 0.6657 0.4671 -0.0738 0.0119  0.0834  449  LEU B CD2 
12088 N N   . HIS B 452  ? 0.4404 0.5177 0.2847 -0.0913 0.0131  0.1126  450  HIS B N   
12089 C CA  . HIS B 452  ? 0.5467 0.6304 0.3776 -0.0871 0.0187  0.1138  450  HIS B CA  
12090 C C   . HIS B 452  ? 0.5174 0.6138 0.3503 -0.0782 0.0260  0.1064  450  HIS B C   
12091 O O   . HIS B 452  ? 0.5334 0.6259 0.3733 -0.0727 0.0242  0.0977  450  HIS B O   
12092 C CB  . HIS B 452  ? 0.4862 0.5522 0.3043 -0.0840 0.0124  0.1114  450  HIS B CB  
12093 C CG  . HIS B 452  ? 0.5194 0.5897 0.3233 -0.0776 0.0172  0.1095  450  HIS B CG  
12094 N ND1 . HIS B 452  ? 0.5263 0.6011 0.3176 -0.0808 0.0203  0.1175  450  HIS B ND1 
12095 C CD2 . HIS B 452  ? 0.5343 0.6048 0.3340 -0.0681 0.0194  0.1005  450  HIS B CD2 
12096 C CE1 . HIS B 452  ? 0.5527 0.6302 0.3323 -0.0733 0.0242  0.1131  450  HIS B CE1 
12097 N NE2 . HIS B 452  ? 0.5421 0.6167 0.3266 -0.0655 0.0236  0.1027  450  HIS B NE2 
12098 N N   . GLY B 453  ? 0.5486 0.6606 0.3755 -0.0768 0.0344  0.1100  451  GLY B N   
12099 C CA  . GLY B 453  ? 0.5885 0.7122 0.4156 -0.0677 0.0415  0.1031  451  GLY B CA  
12100 C C   . GLY B 453  ? 0.6063 0.7401 0.4498 -0.0667 0.0440  0.0997  451  GLY B C   
12101 O O   . GLY B 453  ? 0.6052 0.7408 0.4511 -0.0584 0.0461  0.0912  451  GLY B O   
12102 N N   . MET B 454  ? 0.5718 0.7114 0.4264 -0.0751 0.0432  0.1062  452  MET B N   
12103 C CA  . MET B 454  ? 0.5170 0.6669 0.3872 -0.0749 0.0452  0.1039  452  MET B CA  
12104 C C   . MET B 454  ? 0.5402 0.7034 0.4186 -0.0845 0.0475  0.1140  452  MET B C   
12105 O O   . MET B 454  ? 0.5340 0.7164 0.4200 -0.0838 0.0545  0.1159  452  MET B O   
12106 C CB  . MET B 454  ? 0.5569 0.6917 0.4349 -0.0745 0.0373  0.0973  452  MET B CB  
12107 C CG  . MET B 454  ? 0.5781 0.7226 0.4719 -0.0756 0.0385  0.0958  452  MET B CG  
12108 S SD  . MET B 454  ? 0.6853 0.8488 0.5820 -0.0661 0.0481  0.0910  452  MET B SD  
12109 C CE  . MET B 454  ? 0.5644 0.7121 0.4528 -0.0555 0.0452  0.0793  452  MET B CE  
12110 N N   . GLY B 455  ? 0.4954 0.6485 0.3729 -0.0937 0.0413  0.1206  453  GLY B N   
12111 C CA  . GLY B 455  ? 0.5020 0.6656 0.3873 -0.1040 0.0423  0.1307  453  GLY B CA  
12112 C C   . GLY B 455  ? 0.5497 0.7258 0.4270 -0.1079 0.0484  0.1402  453  GLY B C   
12113 O O   . GLY B 455  ? 0.5288 0.7169 0.4133 -0.1166 0.0503  0.1492  453  GLY B O   
12114 N N   . GLU B 456  ? 0.6035 0.7773 0.4659 -0.1019 0.0515  0.1385  454  GLU B N   
12115 C CA  . GLU B 456  ? 0.6283 0.8129 0.4812 -0.1056 0.0572  0.1479  454  GLU B CA  
12116 C C   . GLU B 456  ? 0.5520 0.7620 0.4137 -0.1053 0.0668  0.1514  454  GLU B C   
12117 O O   . GLU B 456  ? 0.5939 0.8105 0.4601 -0.1122 0.0679  0.1593  454  GLU B O   
12118 C CB  . GLU B 456  ? 0.6412 0.8178 0.4758 -0.0980 0.0584  0.1440  454  GLU B CB  
12119 N N   . PRO B 457  ? 0.5704 0.7924 0.4374 -0.0962 0.0728  0.1441  455  PRO B N   
12120 C CA  . PRO B 457  ? 0.6064 0.8493 0.4857 -0.0948 0.0801  0.1457  455  PRO B CA  
12121 C C   . PRO B 457  ? 0.5732 0.8224 0.4684 -0.1053 0.0772  0.1528  455  PRO B C   
12122 O O   . PRO B 457  ? 0.5873 0.8486 0.4875 -0.1090 0.0808  0.1590  455  PRO B O   
12123 C CB  . PRO B 457  ? 0.5780 0.8275 0.4618 -0.0842 0.0839  0.1360  455  PRO B CB  
12124 C CG  . PRO B 457  ? 0.5888 0.8241 0.4563 -0.0773 0.0822  0.1295  455  PRO B CG  
12125 C CD  . PRO B 457  ? 0.6156 0.8301 0.4784 -0.0851 0.0725  0.1324  455  PRO B CD  
12126 N N   . LEU B 458  ? 0.5497 0.7905 0.4524 -0.1105 0.0704  0.1522  456  LEU B N   
12127 C CA  . LEU B 458  ? 0.5392 0.7847 0.4568 -0.1205 0.0667  0.1583  456  LEU B CA  
12128 C C   . LEU B 458  ? 0.5174 0.7556 0.4309 -0.1306 0.0627  0.1676  456  LEU B C   
12129 O O   . LEU B 458  ? 0.5274 0.7772 0.4493 -0.1362 0.0644  0.1740  456  LEU B O   
12130 C CB  . LEU B 458  ? 0.4909 0.7266 0.4157 -0.1236 0.0599  0.1550  456  LEU B CB  
12131 N N   . TYR B 459  ? 0.5557 0.7745 0.4562 -0.1330 0.0569  0.1686  457  TYR B N   
12132 C CA  . TYR B 459  ? 0.5371 0.7467 0.4344 -0.1431 0.0517  0.1774  457  TYR B CA  
12133 C C   . TYR B 459  ? 0.5086 0.7252 0.3968 -0.1419 0.0573  0.1821  457  TYR B C   
12134 O O   . TYR B 459  ? 0.5156 0.7287 0.4033 -0.1504 0.0543  0.1903  457  TYR B O   
12135 C CB  . TYR B 459  ? 0.5363 0.7212 0.4244 -0.1466 0.0422  0.1770  457  TYR B CB  
12136 C CG  . TYR B 459  ? 0.5169 0.6942 0.4162 -0.1511 0.0354  0.1748  457  TYR B CG  
12137 C CD1 . TYR B 459  ? 0.5314 0.7053 0.4400 -0.1619 0.0295  0.1812  457  TYR B CD1 
12138 C CD2 . TYR B 459  ? 0.4927 0.6638 0.3956 -0.1417 0.0339  0.1628  457  TYR B CD2 
12139 C CE1 . TYR B 459  ? 0.5252 0.6912 0.4439 -0.1651 0.0231  0.1780  457  TYR B CE1 
12140 C CE2 . TYR B 459  ? 0.5111 0.6738 0.4251 -0.1438 0.0273  0.1585  457  TYR B CE2 
12141 C CZ  . TYR B 459  ? 0.5371 0.6971 0.4586 -0.1554 0.0219  0.1659  457  TYR B CZ  
12142 O OH  . TYR B 459  ? 0.5137 0.6651 0.4453 -0.1576 0.0153  0.1616  457  TYR B OH  
12143 N N   . GLU B 460  ? 0.4971 0.7235 0.3786 -0.1316 0.0654  0.1772  458  GLU B N   
12144 C CA  . GLU B 460  ? 0.5632 0.8002 0.4385 -0.1300 0.0723  0.1813  458  GLU B CA  
12145 C C   . GLU B 460  ? 0.5911 0.8473 0.4814 -0.1348 0.0763  0.1869  458  GLU B C   
12146 O O   . GLU B 460  ? 0.6344 0.8977 0.5218 -0.1380 0.0798  0.1935  458  GLU B O   
12147 C CB  . GLU B 460  ? 0.5510 0.7932 0.4159 -0.1174 0.0797  0.1737  458  GLU B CB  
12148 N N   . GLU B 461  ? 0.5901 0.8547 0.4961 -0.1357 0.0756  0.1847  459  GLU B N   
12149 C CA  . GLU B 461  ? 0.6249 0.9058 0.5463 -0.1416 0.0774  0.1903  459  GLU B CA  
12150 C C   . GLU B 461  ? 0.6075 0.8790 0.5367 -0.1543 0.0682  0.1968  459  GLU B C   
12151 O O   . GLU B 461  ? 0.5742 0.8576 0.5179 -0.1597 0.0678  0.2005  459  GLU B O   
12152 C CB  . GLU B 461  ? 0.7405 1.0364 0.6742 -0.1344 0.0818  0.1838  459  GLU B CB  
12153 N N   . VAL B 462  ? 0.5895 0.8396 0.5093 -0.1590 0.0604  0.1982  460  VAL B N   
12154 C CA  . VAL B 462  ? 0.5657 0.8030 0.4910 -0.1704 0.0508  0.2034  460  VAL B CA  
12155 C C   . VAL B 462  ? 0.6068 0.8306 0.5208 -0.1770 0.0466  0.2107  460  VAL B C   
12156 O O   . VAL B 462  ? 0.6280 0.8504 0.5477 -0.1868 0.0421  0.2180  460  VAL B O   
12157 C CB  . VAL B 462  ? 0.5820 0.8033 0.5085 -0.1699 0.0436  0.1971  460  VAL B CB  
12158 C CG1 . VAL B 462  ? 0.5657 0.7693 0.4950 -0.1810 0.0326  0.2018  460  VAL B CG1 
12159 C CG2 . VAL B 462  ? 0.5474 0.7806 0.4853 -0.1644 0.0467  0.1905  460  VAL B CG2 
12160 N N   . VAL B 463  ? 0.6001 0.8119 0.4976 -0.1718 0.0469  0.2084  461  VAL B N   
12161 C CA  . VAL B 463  ? 0.5780 0.7761 0.4639 -0.1773 0.0427  0.2151  461  VAL B CA  
12162 C C   . VAL B 463  ? 0.6444 0.8583 0.5275 -0.1775 0.0505  0.2210  461  VAL B C   
12163 O O   . VAL B 463  ? 0.6109 0.8403 0.4923 -0.1691 0.0598  0.2175  461  VAL B O   
12164 C CB  . VAL B 463  ? 0.6279 0.8073 0.4971 -0.1717 0.0395  0.2106  461  VAL B CB  
12165 N N   . GLY B 464  ? 0.6066 0.8156 0.4885 -0.1867 0.0467  0.2299  462  GLY B N   
12166 C CA  . GLY B 464  ? 0.6593 0.8819 0.5377 -0.1878 0.0537  0.2364  462  GLY B CA  
12167 C C   . GLY B 464  ? 0.6692 0.9064 0.5627 -0.1967 0.0541  0.2437  462  GLY B C   
12168 O O   . GLY B 464  ? 0.6571 0.9016 0.5654 -0.1986 0.0527  0.2418  462  GLY B O   
12169 N N   . ARG B 465  ? 0.6818 0.9229 0.5712 -0.2023 0.0559  0.2525  463  ARG B N   
12170 C CA  . ARG B 465  ? 0.6716 0.9262 0.5744 -0.2114 0.0560  0.2604  463  ARG B CA  
12171 C C   . ARG B 465  ? 0.7194 0.9998 0.6345 -0.2064 0.0650  0.2579  463  ARG B C   
12172 O O   . ARG B 465  ? 0.7061 0.9970 0.6367 -0.2123 0.0633  0.2609  463  ARG B O   
12173 C CB  . ARG B 465  ? 0.7561 1.0105 0.6509 -0.2178 0.0569  0.2702  463  ARG B CB  
12174 N N   . GLY B 466  ? 0.6860 0.9763 0.5943 -0.1954 0.0741  0.2523  464  GLY B N   
12175 C CA  . GLY B 466  ? 0.6726 0.9863 0.5909 -0.1889 0.0830  0.2492  464  GLY B CA  
12176 C C   . GLY B 466  ? 0.6858 1.0014 0.6145 -0.1837 0.0816  0.2406  464  GLY B C   
12177 O O   . GLY B 466  ? 0.7065 1.0401 0.6425 -0.1765 0.0889  0.2365  464  GLY B O   
12178 N N   . LYS B 467  ? 0.6762 0.9735 0.6056 -0.1870 0.0724  0.2378  465  LYS B N   
12179 C CA  . LYS B 467  ? 0.6648 0.9619 0.6034 -0.1826 0.0704  0.2299  465  LYS B CA  
12180 C C   . LYS B 467  ? 0.7022 0.9914 0.6524 -0.1931 0.0607  0.2330  465  LYS B C   
12181 O O   . LYS B 467  ? 0.7061 1.0084 0.6689 -0.1993 0.0606  0.2384  465  LYS B O   
12182 C CB  . LYS B 467  ? 0.6679 0.9496 0.5939 -0.1743 0.0693  0.2215  465  LYS B CB  
12183 C CG  . LYS B 467  ? 0.6213 0.9122 0.5373 -0.1625 0.0791  0.2165  465  LYS B CG  
12184 C CD  . LYS B 467  ? 0.6631 0.9745 0.5910 -0.1553 0.0862  0.2115  465  LYS B CD  
12185 C CE  . LYS B 467  ? 0.6136 0.9373 0.5332 -0.1451 0.0965  0.2086  465  LYS B CE  
12186 N NZ  . LYS B 467  ? 0.7319 1.0401 0.6320 -0.1399 0.0965  0.2053  465  LYS B NZ  
12187 N N   . LEU B 468  ? 0.6279 0.8957 0.5737 -0.1950 0.0522  0.2298  466  LEU B N   
12188 C CA  . LEU B 468  ? 0.5743 0.8315 0.5293 -0.2047 0.0422  0.2323  466  LEU B CA  
12189 C C   . LEU B 468  ? 0.5918 0.8270 0.5374 -0.2128 0.0336  0.2376  466  LEU B C   
12190 O O   . LEU B 468  ? 0.5620 0.7862 0.5138 -0.2213 0.0246  0.2400  466  LEU B O   
12191 C CB  . LEU B 468  ? 0.6148 0.8650 0.5750 -0.2008 0.0384  0.2237  466  LEU B CB  
12192 C CG  . LEU B 468  ? 0.5893 0.8596 0.5598 -0.1929 0.0456  0.2180  466  LEU B CG  
12193 C CD1 . LEU B 468  ? 0.5931 0.8544 0.5675 -0.1896 0.0412  0.2099  466  LEU B CD1 
12194 C CD2 . LEU B 468  ? 0.6336 0.9232 0.6188 -0.1982 0.0474  0.2236  466  LEU B CD2 
12195 N N   . ASP B 469  ? 0.6439 0.8719 0.5745 -0.2102 0.0358  0.2392  467  ASP B N   
12196 C CA  . ASP B 469  ? 0.6690 0.8748 0.5889 -0.2163 0.0278  0.2437  467  ASP B CA  
12197 C C   . ASP B 469  ? 0.6107 0.7944 0.5314 -0.2189 0.0172  0.2395  467  ASP B C   
12198 O O   . ASP B 469  ? 0.6147 0.7844 0.5373 -0.2279 0.0082  0.2440  467  ASP B O   
12199 C CB  . ASP B 469  ? 0.6990 0.9084 0.6220 -0.2267 0.0258  0.2542  467  ASP B CB  
12200 C CG  . ASP B 469  ? 0.7819 0.9782 0.6898 -0.2288 0.0241  0.2595  467  ASP B CG  
12201 O OD1 . ASP B 469  ? 0.7808 0.9791 0.6769 -0.2208 0.0304  0.2569  467  ASP B OD1 
12202 O OD2 . ASP B 469  ? 0.9129 1.0965 0.8203 -0.2382 0.0162  0.2660  467  ASP B OD2 
12203 N N   . ARG B 470  ? 0.6267 0.8069 0.5456 -0.2107 0.0183  0.2307  468  ARG B N   
12204 C CA  . ARG B 470  ? 0.6019 0.7603 0.5194 -0.2118 0.0089  0.2261  468  ARG B CA  
12205 C C   . ARG B 470  ? 0.6088 0.7535 0.5112 -0.2041 0.0089  0.2210  468  ARG B C   
12206 O O   . ARG B 470  ? 0.5704 0.7262 0.4677 -0.1952 0.0171  0.2170  468  ARG B O   
12207 C CB  . ARG B 470  ? 0.5897 0.7545 0.5203 -0.2101 0.0085  0.2198  468  ARG B CB  
12208 C CG  . ARG B 470  ? 0.5409 0.7146 0.4864 -0.2186 0.0056  0.2242  468  ARG B CG  
12209 C CD  . ARG B 470  ? 0.5959 0.7517 0.5396 -0.2291 -0.0044 0.2307  468  ARG B CD  
12210 N NE  . ARG B 470  ? 0.5959 0.7601 0.5527 -0.2375 -0.0074 0.2354  468  ARG B NE  
12211 C CZ  . ARG B 470  ? 0.6562 0.8341 0.6167 -0.2429 -0.0043 0.2435  468  ARG B CZ  
12212 N NH1 . ARG B 470  ? 0.5302 0.7158 0.4825 -0.2407 0.0025  0.2477  468  ARG B NH1 
12213 N NH2 . ARG B 470  ? 0.5652 0.7488 0.5376 -0.2508 -0.0083 0.2474  468  ARG B NH2 
12214 N N   . PRO B 471  ? 0.5375 0.6579 0.4324 -0.2069 -0.0005 0.2211  469  PRO B N   
12215 C CA  . PRO B 471  ? 0.6155 0.7219 0.4956 -0.1999 -0.0014 0.2169  469  PRO B CA  
12216 C C   . PRO B 471  ? 0.5860 0.6898 0.4676 -0.1927 -0.0012 0.2076  469  PRO B C   
12217 O O   . PRO B 471  ? 0.5227 0.6285 0.4160 -0.1945 -0.0033 0.2044  469  PRO B O   
12218 C CB  . PRO B 471  ? 0.5688 0.6500 0.4425 -0.2062 -0.0125 0.2207  469  PRO B CB  
12219 C CG  . PRO B 471  ? 0.5719 0.6502 0.4586 -0.2146 -0.0187 0.2227  469  PRO B CG  
12220 C CD  . PRO B 471  ? 0.5792 0.6833 0.4774 -0.2168 -0.0108 0.2259  469  PRO B CD  
12221 N N   . CYS B 472  ? 0.5537 0.6531 0.4229 -0.1844 0.0012  0.2032  470  CYS B N   
12222 C CA  . CYS B 472  ? 0.5575 0.6545 0.4261 -0.1768 0.0018  0.1943  470  CYS B CA  
12223 C C   . CYS B 472  ? 0.5656 0.6424 0.4210 -0.1698 -0.0033 0.1887  470  CYS B C   
12224 O O   . CYS B 472  ? 0.5603 0.6376 0.4025 -0.1684 -0.0005 0.1926  470  CYS B O   
12225 C CB  . CYS B 472  ? 0.5237 0.6440 0.3954 -0.1688 0.0130  0.1899  470  CYS B CB  
12226 S SG  . CYS B 472  ? 0.5818 0.6980 0.4581 -0.1555 0.0130  0.1738  470  CYS B SG  
12227 N N   . ARG B 473  ? 0.5315 0.5911 0.3904 -0.1655 -0.0107 0.1798  471  ARG B N   
12228 C CA  . ARG B 473  ? 0.5087 0.5501 0.3573 -0.1578 -0.0158 0.1731  471  ARG B CA  
12229 C C   . ARG B 473  ? 0.4931 0.5411 0.3433 -0.1458 -0.0109 0.1613  471  ARG B C   
12230 O O   . ARG B 473  ? 0.4797 0.5316 0.3414 -0.1430 -0.0104 0.1545  471  ARG B O   
12231 C CB  . ARG B 473  ? 0.5143 0.5323 0.3655 -0.1603 -0.0271 0.1707  471  ARG B CB  
12232 C CG  . ARG B 473  ? 0.4860 0.4857 0.3275 -0.1524 -0.0328 0.1643  471  ARG B CG  
12233 C CD  . ARG B 473  ? 0.4932 0.4699 0.3361 -0.1556 -0.0440 0.1639  471  ARG B CD  
12234 N NE  . ARG B 473  ? 0.4993 0.4718 0.3425 -0.1676 -0.0478 0.1752  471  ARG B NE  
12235 C CZ  . ARG B 473  ? 0.5172 0.4806 0.3498 -0.1729 -0.0515 0.1842  471  ARG B CZ  
12236 N NH1 . ARG B 473  ? 0.5197 0.4764 0.3399 -0.1673 -0.0522 0.1833  471  ARG B NH1 
12237 N NH2 . ARG B 473  ? 0.5717 0.5320 0.4060 -0.1844 -0.0548 0.1945  471  ARG B NH2 
12238 N N   . ILE B 474  ? 0.4996 0.5485 0.3379 -0.1390 -0.0076 0.1592  472  ILE B N   
12239 C CA  . ILE B 474  ? 0.4800 0.5341 0.3178 -0.1277 -0.0032 0.1485  472  ILE B CA  
12240 C C   . ILE B 474  ? 0.4705 0.5046 0.3070 -0.1217 -0.0113 0.1397  472  ILE B C   
12241 O O   . ILE B 474  ? 0.4571 0.4761 0.2839 -0.1221 -0.0172 0.1416  472  ILE B O   
12242 C CB  . ILE B 474  ? 0.4898 0.5542 0.3147 -0.1232 0.0042  0.1502  472  ILE B CB  
12243 C CG1 . ILE B 474  ? 0.4892 0.5752 0.3164 -0.1289 0.0128  0.1591  472  ILE B CG1 
12244 C CG2 . ILE B 474  ? 0.4950 0.5625 0.3188 -0.1115 0.0077  0.1388  472  ILE B CG2 
12245 C CD1 . ILE B 474  ? 0.5185 0.6142 0.3313 -0.1263 0.0198  0.1631  472  ILE B CD1 
12246 N N   . TYR B 475  ? 0.4698 0.5041 0.3166 -0.1165 -0.0116 0.1306  473  TYR B N   
12247 C CA  . TYR B 475  ? 0.4483 0.4671 0.2950 -0.1096 -0.0177 0.1213  473  TYR B CA  
12248 C C   . TYR B 475  ? 0.5032 0.5253 0.3410 -0.1004 -0.0137 0.1155  473  TYR B C   
12249 O O   . TYR B 475  ? 0.5163 0.5526 0.3569 -0.0956 -0.0064 0.1115  473  TYR B O   
12250 C CB  . TYR B 475  ? 0.4690 0.4887 0.3297 -0.1079 -0.0187 0.1144  473  TYR B CB  
12251 C CG  . TYR B 475  ? 0.4613 0.4661 0.3244 -0.1018 -0.0250 0.1053  473  TYR B CG  
12252 C CD1 . TYR B 475  ? 0.5108 0.4994 0.3769 -0.1053 -0.0335 0.1056  473  TYR B CD1 
12253 C CD2 . TYR B 475  ? 0.5835 0.5907 0.4464 -0.0925 -0.0224 0.0963  473  TYR B CD2 
12254 C CE1 . TYR B 475  ? 0.5161 0.4924 0.3851 -0.0993 -0.0388 0.0972  473  TYR B CE1 
12255 C CE2 . TYR B 475  ? 0.5912 0.5862 0.4573 -0.0871 -0.0278 0.0883  473  TYR B CE2 
12256 C CZ  . TYR B 475  ? 0.5532 0.5333 0.4225 -0.0905 -0.0358 0.0888  473  TYR B CZ  
12257 O OH  . TYR B 475  ? 0.5769 0.5460 0.4497 -0.0849 -0.0407 0.0810  473  TYR B OH  
12258 N N   . ALA B 476  ? 0.4813 0.4901 0.3082 -0.0980 -0.0187 0.1151  474  ALA B N   
12259 C CA  . ALA B 476  ? 0.4681 0.4793 0.2833 -0.0910 -0.0154 0.1119  474  ALA B CA  
12260 C C   . ALA B 476  ? 0.5266 0.5251 0.3413 -0.0833 -0.0209 0.1024  474  ALA B C   
12261 O O   . ALA B 476  ? 0.4721 0.4550 0.2823 -0.0839 -0.0288 0.1031  474  ALA B O   
12262 C CB  . ALA B 476  ? 0.4630 0.4713 0.2639 -0.0953 -0.0161 0.1208  474  ALA B CB  
12263 N N   . PRO B 477  ? 0.4991 0.5037 0.3186 -0.0760 -0.0173 0.0936  475  PRO B N   
12264 C CA  . PRO B 477  ? 0.5019 0.4957 0.3206 -0.0688 -0.0221 0.0849  475  PRO B CA  
12265 C C   . PRO B 477  ? 0.5144 0.5017 0.3178 -0.0660 -0.0243 0.0858  475  PRO B C   
12266 O O   . PRO B 477  ? 0.5016 0.4973 0.2947 -0.0658 -0.0189 0.0893  475  PRO B O   
12267 C CB  . PRO B 477  ? 0.5090 0.5136 0.3342 -0.0625 -0.0162 0.0771  475  PRO B CB  
12268 C CG  . PRO B 477  ? 0.4729 0.4908 0.3075 -0.0672 -0.0106 0.0809  475  PRO B CG  
12269 C CD  . PRO B 477  ? 0.4939 0.5154 0.3213 -0.0744 -0.0091 0.0914  475  PRO B CD  
12270 N N   . VAL B 478  ? 0.4960 0.4685 0.2980 -0.0635 -0.0322 0.0823  476  VAL B N   
12271 C CA  . VAL B 478  ? 0.5014 0.4661 0.2897 -0.0604 -0.0358 0.0823  476  VAL B CA  
12272 C C   . VAL B 478  ? 0.5751 0.5322 0.3672 -0.0533 -0.0404 0.0728  476  VAL B C   
12273 O O   . VAL B 478  ? 0.5591 0.5082 0.3614 -0.0532 -0.0458 0.0699  476  VAL B O   
12274 C CB  . VAL B 478  ? 0.5329 0.4858 0.3144 -0.0660 -0.0426 0.0904  476  VAL B CB  
12275 C CG1 . VAL B 478  ? 0.5387 0.4842 0.3055 -0.0626 -0.0463 0.0902  476  VAL B CG1 
12276 C CG2 . VAL B 478  ? 0.4631 0.4236 0.2422 -0.0741 -0.0383 0.1005  476  VAL B CG2 
12277 N N   . GLY B 479  ? 0.5893 0.5489 0.3734 -0.0475 -0.0383 0.0680  477  GLY B N   
12278 C CA  . GLY B 479  ? 0.5761 0.5289 0.3638 -0.0413 -0.0429 0.0594  477  GLY B CA  
12279 C C   . GLY B 479  ? 0.6382 0.5970 0.4193 -0.0351 -0.0385 0.0534  477  GLY B C   
12280 O O   . GLY B 479  ? 0.6016 0.5707 0.3761 -0.0348 -0.0313 0.0551  477  GLY B O   
12281 N N   . THR B 480  ? 0.6153 0.5672 0.3988 -0.0301 -0.0433 0.0462  478  THR B N   
12282 C CA  . THR B 480  ? 0.6977 0.6521 0.4756 -0.0239 -0.0412 0.0395  478  THR B CA  
12283 C C   . THR B 480  ? 0.7309 0.6965 0.5175 -0.0214 -0.0338 0.0350  478  THR B C   
12284 O O   . THR B 480  ? 0.7245 0.6964 0.5217 -0.0245 -0.0303 0.0371  478  THR B O   
12285 C CB  . THR B 480  ? 0.6806 0.6244 0.4609 -0.0202 -0.0493 0.0336  478  THR B CB  
12286 O OG1 . THR B 480  ? 0.7142 0.6567 0.5111 -0.0205 -0.0514 0.0306  478  THR B OG1 
12287 C CG2 . THR B 480  ? 0.6467 0.5797 0.4179 -0.0221 -0.0569 0.0381  478  THR B CG2 
12288 N N   . HIS B 481  ? 0.7661 0.7335 0.5480 -0.0157 -0.0317 0.0287  479  HIS B N   
12289 C CA  . HIS B 481  ? 0.7520 0.7288 0.5417 -0.0126 -0.0253 0.0239  479  HIS B CA  
12290 C C   . HIS B 481  ? 0.7495 0.7235 0.5551 -0.0119 -0.0284 0.0191  479  HIS B C   
12291 O O   . HIS B 481  ? 0.7858 0.7676 0.6018 -0.0121 -0.0237 0.0181  479  HIS B O   
12292 C CB  . HIS B 481  ? 0.6783 0.6561 0.4574 -0.0065 -0.0229 0.0183  479  HIS B CB  
12293 C CG  . HIS B 481  ? 0.6871 0.6692 0.4501 -0.0064 -0.0187 0.0225  479  HIS B CG  
12294 N ND1 . HIS B 481  ? 0.7170 0.6999 0.4677 -0.0008 -0.0162 0.0180  479  HIS B ND1 
12295 C CD2 . HIS B 481  ? 0.7037 0.6894 0.4605 -0.0112 -0.0165 0.0307  479  HIS B CD2 
12296 C CE1 . HIS B 481  ? 0.7246 0.7120 0.4620 -0.0019 -0.0123 0.0232  479  HIS B CE1 
12297 N NE2 . HIS B 481  ? 0.7490 0.7384 0.4900 -0.0084 -0.0124 0.0312  479  HIS B NE2 
12298 N N   . GLU B 482  ? 0.7760 0.7394 0.5837 -0.0110 -0.0361 0.0164  480  GLU B N   
12299 C CA  . GLU B 482  ? 0.7355 0.6966 0.5580 -0.0102 -0.0389 0.0120  480  GLU B CA  
12300 C C   . GLU B 482  ? 0.7601 0.7237 0.5933 -0.0148 -0.0381 0.0160  480  GLU B C   
12301 O O   . GLU B 482  ? 0.7979 0.7662 0.6428 -0.0144 -0.0355 0.0132  480  GLU B O   
12302 C CB  . GLU B 482  ? 0.7899 0.7402 0.6125 -0.0086 -0.0475 0.0092  480  GLU B CB  
12303 N N   . THR B 483  ? 0.7658 0.7257 0.5948 -0.0193 -0.0405 0.0226  481  THR B N   
12304 C CA  . THR B 483  ? 0.7717 0.7326 0.6098 -0.0242 -0.0404 0.0266  481  THR B CA  
12305 C C   . THR B 483  ? 0.7617 0.7349 0.6029 -0.0261 -0.0324 0.0288  481  THR B C   
12306 O O   . THR B 483  ? 0.7944 0.7711 0.6470 -0.0276 -0.0309 0.0279  481  THR B O   
12307 C CB  . THR B 483  ? 0.7501 0.7033 0.5818 -0.0287 -0.0452 0.0336  481  THR B CB  
12308 N N   . LEU B 484  ? 0.7790 0.7592 0.6101 -0.0260 -0.0271 0.0316  482  LEU B N   
12309 C CA  . LEU B 484  ? 0.7442 0.7375 0.5783 -0.0278 -0.0194 0.0342  482  LEU B CA  
12310 C C   . LEU B 484  ? 0.7414 0.7410 0.5858 -0.0239 -0.0158 0.0279  482  LEU B C   
12311 O O   . LEU B 484  ? 0.7176 0.7231 0.5725 -0.0264 -0.0135 0.0289  482  LEU B O   
12312 C CB  . LEU B 484  ? 0.6952 0.6954 0.5161 -0.0270 -0.0141 0.0374  482  LEU B CB  
12313 N N   . LEU B 485  ? 0.7290 0.7270 0.5704 -0.0179 -0.0158 0.0214  483  LEU B N   
12314 C CA  . LEU B 485  ? 0.7495 0.7529 0.5998 -0.0140 -0.0125 0.0156  483  LEU B CA  
12315 C C   . LEU B 485  ? 0.7381 0.7380 0.6019 -0.0155 -0.0159 0.0134  483  LEU B C   
12316 O O   . LEU B 485  ? 0.6992 0.7054 0.5719 -0.0141 -0.0126 0.0106  483  LEU B O   
12317 C CB  . LEU B 485  ? 0.7158 0.7155 0.5596 -0.0078 -0.0133 0.0092  483  LEU B CB  
12318 C CG  . LEU B 485  ? 0.6864 0.6913 0.5171 -0.0049 -0.0084 0.0098  483  LEU B CG  
12319 C CD1 . LEU B 485  ? 0.7054 0.7023 0.5272 0.0002  -0.0119 0.0041  483  LEU B CD1 
12320 C CD2 . LEU B 485  ? 0.6434 0.6608 0.4784 -0.0029 -0.0006 0.0091  483  LEU B CD2 
12321 N N   . ALA B 486  ? 0.7000 0.6903 0.5654 -0.0180 -0.0224 0.0148  484  ALA B N   
12322 C CA  . ALA B 486  ? 0.6934 0.6799 0.5709 -0.0186 -0.0258 0.0121  484  ALA B CA  
12323 C C   . ALA B 486  ? 0.7163 0.7089 0.6023 -0.0228 -0.0230 0.0152  484  ALA B C   
12324 O O   . ALA B 486  ? 0.7006 0.6935 0.5967 -0.0222 -0.0234 0.0119  484  ALA B O   
12325 C CB  . ALA B 486  ? 0.7192 0.6938 0.5956 -0.0197 -0.0334 0.0128  484  ALA B CB  
12326 N N   . TYR B 487  ? 0.6944 0.6918 0.5763 -0.0272 -0.0203 0.0216  485  TYR B N   
12327 C CA  . TYR B 487  ? 0.6814 0.6844 0.5712 -0.0320 -0.0183 0.0251  485  TYR B CA  
12328 C C   . TYR B 487  ? 0.7132 0.7296 0.6013 -0.0334 -0.0112 0.0288  485  TYR B C   
12329 O O   . TYR B 487  ? 0.6418 0.6637 0.5347 -0.0384 -0.0096 0.0333  485  TYR B O   
12330 C CB  . TYR B 487  ? 0.6808 0.6755 0.5699 -0.0377 -0.0235 0.0303  485  TYR B CB  
12331 N N   . LEU B 488  ? 0.7193 0.7412 0.6007 -0.0288 -0.0069 0.0268  486  LEU B N   
12332 C CA  . LEU B 488  ? 0.7114 0.7466 0.5906 -0.0294 0.0002  0.0304  486  LEU B CA  
12333 C C   . LEU B 488  ? 0.7009 0.7463 0.5911 -0.0285 0.0044  0.0283  486  LEU B C   
12334 O O   . LEU B 488  ? 0.5964 0.6533 0.4896 -0.0314 0.0090  0.0328  486  LEU B O   
12335 C CB  . LEU B 488  ? 0.6460 0.6833 0.5138 -0.0242 0.0033  0.0284  486  LEU B CB  
12336 C CG  . LEU B 488  ? 0.6473 0.6988 0.5117 -0.0248 0.0109  0.0328  486  LEU B CG  
12337 C CD1 . LEU B 488  ? 0.6891 0.7434 0.5538 -0.0327 0.0106  0.0415  486  LEU B CD1 
12338 C CD2 . LEU B 488  ? 0.5836 0.6361 0.4346 -0.0197 0.0138  0.0312  486  LEU B CD2 
12339 N N   . VAL B 489  ? 0.6889 0.7306 0.5855 -0.0246 0.0027  0.0218  487  VAL B N   
12340 C CA  . VAL B 489  ? 0.6502 0.7004 0.5572 -0.0237 0.0059  0.0198  487  VAL B CA  
12341 C C   . VAL B 489  ? 0.6406 0.6946 0.5550 -0.0305 0.0053  0.0250  487  VAL B C   
12342 O O   . VAL B 489  ? 0.7164 0.7825 0.6352 -0.0321 0.0099  0.0279  487  VAL B O   
12343 C CB  . VAL B 489  ? 0.6757 0.7194 0.5883 -0.0195 0.0031  0.0128  487  VAL B CB  
12344 N N   . ARG B 490  ? 0.6941 0.7376 0.6097 -0.0345 -0.0006 0.0262  488  ARG B N   
12345 C CA  . ARG B 490  ? 0.6855 0.7304 0.6075 -0.0411 -0.0021 0.0306  488  ARG B CA  
12346 C C   . ARG B 490  ? 0.7175 0.7705 0.6359 -0.0464 0.0008  0.0385  488  ARG B C   
12347 O O   . ARG B 490  ? 0.6940 0.7556 0.6189 -0.0508 0.0027  0.0422  488  ARG B O   
12348 C CB  . ARG B 490  ? 0.6224 0.6531 0.5452 -0.0436 -0.0094 0.0300  488  ARG B CB  
12349 C CG  . ARG B 490  ? 0.6018 0.6322 0.5315 -0.0499 -0.0117 0.0332  488  ARG B CG  
12350 C CD  . ARG B 490  ? 0.6319 0.6479 0.5631 -0.0512 -0.0187 0.0314  488  ARG B CD  
12351 N NE  . ARG B 490  ? 0.5847 0.5914 0.5084 -0.0542 -0.0229 0.0358  488  ARG B NE  
12352 C CZ  . ARG B 490  ? 0.6699 0.6648 0.5897 -0.0513 -0.0276 0.0332  488  ARG B CZ  
12353 N NH1 . ARG B 490  ? 0.6086 0.6000 0.5318 -0.0457 -0.0288 0.0263  488  ARG B NH1 
12354 N NH2 . ARG B 490  ? 0.6596 0.6465 0.5723 -0.0543 -0.0313 0.0378  488  ARG B NH2 
12355 N N   . ARG B 491  ? 0.6623 0.7130 0.5702 -0.0462 0.0012  0.0413  489  ARG B N   
12356 C CA  . ARG B 491  ? 0.6798 0.7381 0.5836 -0.0515 0.0041  0.0494  489  ARG B CA  
12357 C C   . ARG B 491  ? 0.7351 0.8110 0.6419 -0.0499 0.0120  0.0507  489  ARG B C   
12358 O O   . ARG B 491  ? 0.7008 0.7866 0.6114 -0.0555 0.0145  0.0570  489  ARG B O   
12359 C CB  . ARG B 491  ? 0.7097 0.7615 0.6007 -0.0510 0.0029  0.0517  489  ARG B CB  
12360 N N   . LEU B 492  ? 0.7367 0.8166 0.6421 -0.0423 0.0156  0.0448  490  LEU B N   
12361 C CA  . LEU B 492  ? 0.7408 0.8370 0.6484 -0.0394 0.0232  0.0454  490  LEU B CA  
12362 C C   . LEU B 492  ? 0.7315 0.8363 0.6523 -0.0412 0.0243  0.0453  490  LEU B C   
12363 O O   . LEU B 492  ? 0.6824 0.8012 0.6079 -0.0444 0.0287  0.0504  490  LEU B O   
12364 C CB  . LEU B 492  ? 0.6802 0.7758 0.5820 -0.0304 0.0259  0.0387  490  LEU B CB  
12365 C CG  . LEU B 492  ? 0.6933 0.7819 0.5810 -0.0282 0.0252  0.0387  490  LEU B CG  
12366 C CD1 . LEU B 492  ? 0.6667 0.7515 0.5493 -0.0196 0.0261  0.0309  490  LEU B CD1 
12367 C CD2 . LEU B 492  ? 0.6824 0.7825 0.5638 -0.0307 0.0308  0.0456  490  LEU B CD2 
12368 N N   . LEU B 493  ? 0.7658 0.8629 0.6927 -0.0393 0.0205  0.0396  491  LEU B N   
12369 C CA  . LEU B 493  ? 0.6953 0.7990 0.6339 -0.0408 0.0208  0.0390  491  LEU B CA  
12370 C C   . LEU B 493  ? 0.7206 0.8288 0.6645 -0.0497 0.0195  0.0461  491  LEU B C   
12371 O O   . LEU B 493  ? 0.7766 0.8954 0.7294 -0.0517 0.0214  0.0478  491  LEU B O   
12372 C CB  . LEU B 493  ? 0.6699 0.7622 0.6126 -0.0386 0.0159  0.0327  491  LEU B CB  
12373 C CG  . LEU B 493  ? 0.6910 0.7852 0.6358 -0.0309 0.0183  0.0260  491  LEU B CG  
12374 C CD1 . LEU B 493  ? 0.6862 0.7713 0.6369 -0.0306 0.0136  0.0212  491  LEU B CD1 
12375 C CD2 . LEU B 493  ? 0.6640 0.7745 0.6143 -0.0291 0.0243  0.0274  491  LEU B CD2 
12376 N N   . GLY B 496  ? 0.7107 0.8584 0.6543 -0.0471 0.0363  0.0553  494  GLY B N   
12377 C CA  . GLY B 496  ? 0.6936 0.8471 0.6365 -0.0379 0.0410  0.0496  494  GLY B CA  
12378 C C   . GLY B 496  ? 0.7526 0.9113 0.7066 -0.0353 0.0411  0.0458  494  GLY B C   
12379 O O   . GLY B 496  ? 0.7505 0.9188 0.7063 -0.0287 0.0461  0.0431  494  GLY B O   
12380 N N   . ALA B 497  ? 0.7429 0.8948 0.7038 -0.0401 0.0357  0.0455  495  ALA B N   
12381 C CA  . ALA B 497  ? 0.6974 0.8541 0.6685 -0.0384 0.0353  0.0425  495  ALA B CA  
12382 C C   . ALA B 497  ? 0.6310 0.8069 0.6106 -0.0408 0.0399  0.0478  495  ALA B C   
12383 O O   . ALA B 497  ? 0.6805 0.8647 0.6601 -0.0463 0.0418  0.0547  495  ALA B O   
12384 C CB  . ALA B 497  ? 0.6235 0.7685 0.5989 -0.0433 0.0284  0.0411  495  ALA B CB  
12385 N N   . ASN B 498  ? 0.6451 0.8283 0.6327 -0.0368 0.0414  0.0448  496  ASN B N   
12386 C CA  . ASN B 498  ? 0.6162 0.8191 0.6121 -0.0369 0.0463  0.0490  496  ASN B CA  
12387 C C   . ASN B 498  ? 0.5941 0.8043 0.5967 -0.0470 0.0445  0.0566  496  ASN B C   
12388 O O   . ASN B 498  ? 0.5801 0.8062 0.5860 -0.0493 0.0491  0.0627  496  ASN B O   
12389 C CB  . ASN B 498  ? 0.5777 0.7849 0.5813 -0.0314 0.0467  0.0444  496  ASN B CB  
12390 N N   . SER B 499  ? 0.5533 0.7522 0.5581 -0.0532 0.0377  0.0565  497  SER B N   
12391 C CA  . SER B 499  ? 0.5266 0.7305 0.5378 -0.0632 0.0349  0.0634  497  SER B CA  
12392 C C   . SER B 499  ? 0.5368 0.7376 0.5415 -0.0697 0.0345  0.0696  497  SER B C   
12393 O O   . SER B 499  ? 0.4602 0.6654 0.4699 -0.0786 0.0322  0.0762  497  SER B O   
12394 C CB  . SER B 499  ? 0.5093 0.7007 0.5240 -0.0672 0.0275  0.0606  497  SER B CB  
12395 O OG  . SER B 499  ? 0.5049 0.6771 0.5108 -0.0669 0.0232  0.0570  497  SER B OG  
12396 N N   . SER B 500  ? 0.5645 0.7576 0.5583 -0.0657 0.0361  0.0679  498  SER B N   
12397 C CA  . SER B 500  ? 0.5636 0.7523 0.5504 -0.0719 0.0351  0.0739  498  SER B CA  
12398 C C   . SER B 500  ? 0.5791 0.7866 0.5664 -0.0731 0.0423  0.0808  498  SER B C   
12399 O O   . SER B 500  ? 0.5685 0.7888 0.5569 -0.0659 0.0487  0.0789  498  SER B O   
12400 C CB  . SER B 500  ? 0.5791 0.7512 0.5536 -0.0675 0.0333  0.0694  498  SER B CB  
12401 O OG  . SER B 500  ? 0.6493 0.8272 0.6179 -0.0590 0.0393  0.0663  498  SER B OG  
12402 N N   . PHE B 501  ? 0.5132 0.7223 0.4997 -0.0821 0.0410  0.0890  499  PHE B N   
12403 C CA  . PHE B 501  ? 0.5672 0.7949 0.5543 -0.0843 0.0478  0.0965  499  PHE B CA  
12404 C C   . PHE B 501  ? 0.6061 0.8351 0.5815 -0.0763 0.0538  0.0943  499  PHE B C   
12405 O O   . PHE B 501  ? 0.6274 0.8742 0.6042 -0.0723 0.0615  0.0963  499  PHE B O   
12406 C CB  . PHE B 501  ? 0.5090 0.7355 0.4961 -0.0961 0.0446  0.1059  499  PHE B CB  
12407 N N   . VAL B 502  ? 0.6213 0.8318 0.5854 -0.0735 0.0502  0.0899  500  VAL B N   
12408 C CA  . VAL B 502  ? 0.6855 0.8950 0.6370 -0.0668 0.0548  0.0880  500  VAL B CA  
12409 C C   . VAL B 502  ? 0.6911 0.9067 0.6426 -0.0555 0.0598  0.0804  500  VAL B C   
12410 O O   . VAL B 502  ? 0.7279 0.9472 0.6702 -0.0493 0.0650  0.0790  500  VAL B O   
12411 C CB  . VAL B 502  ? 0.6999 0.8875 0.6399 -0.0671 0.0486  0.0853  500  VAL B CB  
12412 N N   . HIS B 503  ? 0.6463 0.8623 0.6074 -0.0526 0.0580  0.0753  501  HIS B N   
12413 C CA  . HIS B 503  ? 0.6300 0.8544 0.5932 -0.0427 0.0630  0.0695  501  HIS B CA  
12414 C C   . HIS B 503  ? 0.6388 0.8855 0.6138 -0.0431 0.0685  0.0737  501  HIS B C   
12415 O O   . HIS B 503  ? 0.6757 0.9335 0.6509 -0.0348 0.0746  0.0710  501  HIS B O   
12416 C CB  . HIS B 503  ? 0.6298 0.8410 0.5958 -0.0383 0.0581  0.0612  501  HIS B CB  
12417 N N   . ARG B 504  ? 0.5660 0.8197 0.5507 -0.0525 0.0663  0.0805  502  ARG B N   
12418 C CA  . ARG B 504  ? 0.5553 0.8307 0.5529 -0.0537 0.0705  0.0848  502  ARG B CA  
12419 C C   . ARG B 504  ? 0.5908 0.8848 0.5870 -0.0545 0.0783  0.0919  502  ARG B C   
12420 O O   . ARG B 504  ? 0.5873 0.9004 0.5904 -0.0498 0.0846  0.0928  502  ARG B O   
12421 C CB  . ARG B 504  ? 0.4769 0.7520 0.4854 -0.0639 0.0644  0.0892  502  ARG B CB  
12422 C CG  . ARG B 504  ? 0.5359 0.7988 0.5489 -0.0619 0.0583  0.0822  502  ARG B CG  
12423 C CD  . ARG B 504  ? 0.5062 0.7630 0.5258 -0.0725 0.0510  0.0859  502  ARG B CD  
12424 N NE  . ARG B 504  ? 0.4415 0.7171 0.4726 -0.0795 0.0526  0.0938  502  ARG B NE  
12425 C CZ  . ARG B 504  ? 0.4988 0.7883 0.5417 -0.0780 0.0537  0.0936  502  ARG B CZ  
12426 N NH1 . ARG B 504  ? 0.5649 0.8520 0.6093 -0.0694 0.0540  0.0861  502  ARG B NH1 
12427 N NH2 . ARG B 504  ? 0.5143 0.8204 0.5678 -0.0855 0.0544  0.1014  502  ARG B NH2 
12428 N N   . ILE B 505  ? 0.5885 0.8778 0.5759 -0.0603 0.0780  0.0973  503  ILE B N   
12429 C CA  . ILE B 505  ? 0.5575 0.8643 0.5421 -0.0611 0.0858  0.1043  503  ILE B CA  
12430 C C   . ILE B 505  ? 0.5939 0.9057 0.5708 -0.0485 0.0928  0.0984  503  ILE B C   
12431 O O   . ILE B 505  ? 0.5575 0.8809 0.5356 -0.0452 0.0981  0.1003  503  ILE B O   
12432 C CB  . ILE B 505  ? 0.5935 0.8911 0.5682 -0.0694 0.0833  0.1107  503  ILE B CB  
12433 N N   . ASN B 506  ? 0.6288 0.9259 0.5985 -0.0405 0.0907  0.0892  504  ASN B N   
12434 C CA  . ASN B 506  ? 0.6357 0.9356 0.5977 -0.0283 0.0965  0.0827  504  ASN B CA  
12435 C C   . ASN B 506  ? 0.6682 0.9757 0.6406 -0.0206 0.0981  0.0771  504  ASN B C   
12436 O O   . ASN B 506  ? 0.6855 0.9931 0.6526 -0.0099 0.1020  0.0707  504  ASN B O   
12437 C CB  . ASN B 506  ? 0.6338 0.9112 0.5809 -0.0240 0.0925  0.0757  504  ASN B CB  
12438 N N   . ASP B 507  ? 0.6310 0.9426 0.6175 -0.0257 0.0944  0.0790  505  ASP B N   
12439 C CA  . ASP B 507  ? 0.6503 0.9716 0.6475 -0.0192 0.0962  0.0751  505  ASP B CA  
12440 C C   . ASP B 507  ? 0.6673 1.0059 0.6746 -0.0193 0.0999  0.0798  505  ASP B C   
12441 O O   . ASP B 507  ? 0.6675 1.0133 0.6838 -0.0289 0.0978  0.0870  505  ASP B O   
12442 C CB  . ASP B 507  ? 0.6011 0.9132 0.6078 -0.0239 0.0884  0.0733  505  ASP B CB  
12443 N N   . PRO B 508  ? 0.7002 1.0454 0.7062 -0.0091 0.1053  0.0762  506  PRO B N   
12444 C CA  . PRO B 508  ? 0.6598 1.0223 0.6753 -0.0091 0.1091  0.0808  506  PRO B CA  
12445 C C   . PRO B 508  ? 0.6800 1.0525 0.7123 -0.0122 0.1062  0.0830  506  PRO B C   
12446 O O   . PRO B 508  ? 0.6847 1.0716 0.7263 -0.0156 0.1079  0.0887  506  PRO B O   
12447 C CB  . PRO B 508  ? 0.6947 1.0592 0.7039 0.0038  0.1148  0.0747  506  PRO B CB  
12448 C CG  . PRO B 508  ? 0.6689 1.0161 0.6629 0.0088  0.1140  0.0680  506  PRO B CG  
12449 C CD  . PRO B 508  ? 0.6699 1.0066 0.6656 0.0027  0.1077  0.0675  506  PRO B CD  
12450 N N   . LYS B 509  ? 0.6511 1.0164 0.6871 -0.0111 0.1019  0.0787  507  LYS B N   
12451 C CA  . LYS B 509  ? 0.6928 1.0665 0.7440 -0.0143 0.0985  0.0806  507  LYS B CA  
12452 C C   . LYS B 509  ? 0.7198 1.0955 0.7777 -0.0279 0.0938  0.0882  507  LYS B C   
12453 O O   . LYS B 509  ? 0.6838 1.0709 0.7542 -0.0320 0.0922  0.0925  507  LYS B O   
12454 C CB  . LYS B 509  ? 0.5867 0.9514 0.6390 -0.0092 0.0952  0.0738  507  LYS B CB  
12455 N N   . VAL B 510  ? 0.6710 1.0352 0.7206 -0.0350 0.0910  0.0901  508  VAL B N   
12456 C CA  . VAL B 510  ? 0.6296 0.9935 0.6848 -0.0481 0.0859  0.0971  508  VAL B CA  
12457 C C   . VAL B 510  ? 0.6342 1.0101 0.6922 -0.0527 0.0888  0.1046  508  VAL B C   
12458 O O   . VAL B 510  ? 0.6344 1.0093 0.6825 -0.0512 0.0929  0.1060  508  VAL B O   
12459 C CB  . VAL B 510  ? 0.5647 0.9119 0.6098 -0.0542 0.0820  0.0970  508  VAL B CB  
12460 N N   . SER B 511  ? 0.6080 0.9952 0.6791 -0.0582 0.0866  0.1094  509  SER B N   
12461 C CA  . SER B 511  ? 0.6107 1.0104 0.6861 -0.0634 0.0889  0.1170  509  SER B CA  
12462 C C   . SER B 511  ? 0.6024 0.9938 0.6733 -0.0754 0.0849  0.1234  509  SER B C   
12463 O O   . SER B 511  ? 0.6449 1.0223 0.7128 -0.0812 0.0791  0.1227  509  SER B O   
12464 C CB  . SER B 511  ? 0.5755 0.9895 0.6667 -0.0658 0.0870  0.1201  509  SER B CB  
12465 N N   . ILE B 512  ? 0.5832 0.9831 0.6534 -0.0791 0.0881  0.1299  510  ILE B N   
12466 C CA  . ILE B 512  ? 0.6252 1.0185 0.6929 -0.0913 0.0838  0.1370  510  ILE B CA  
12467 C C   . ILE B 512  ? 0.6304 1.0227 0.7095 -0.1012 0.0760  0.1404  510  ILE B C   
12468 O O   . ILE B 512  ? 0.6245 1.0034 0.7004 -0.1103 0.0697  0.1429  510  ILE B O   
12469 C CB  . ILE B 512  ? 0.5854 0.9899 0.6516 -0.0933 0.0889  0.1437  510  ILE B CB  
12470 C CG1 . ILE B 512  ? 0.5877 0.9887 0.6395 -0.0849 0.0955  0.1403  510  ILE B CG1 
12471 C CG2 . ILE B 512  ? 0.5620 0.9616 0.6286 -0.1069 0.0837  0.1521  510  ILE B CG2 
12472 C CD1 . ILE B 512  ? 0.5455 0.9521 0.5920 -0.0889 0.0993  0.1472  510  ILE B CD1 
12473 N N   . ASP B 513  ? 0.6097 1.0152 0.7016 -0.0992 0.0759  0.1402  511  ASP B N   
12474 C CA  . ASP B 513  ? 0.5882 0.9925 0.6905 -0.1079 0.0682  0.1427  511  ASP B CA  
12475 C C   . ASP B 513  ? 0.5750 0.9622 0.6737 -0.1090 0.0622  0.1373  511  ASP B C   
12476 O O   . ASP B 513  ? 0.5643 0.9417 0.6647 -0.1190 0.0547  0.1399  511  ASP B O   
12477 C CB  . ASP B 513  ? 0.5829 1.0042 0.6986 -0.1041 0.0694  0.1427  511  ASP B CB  
12478 C CG  . ASP B 513  ? 0.6093 1.0472 0.7322 -0.1083 0.0721  0.1505  511  ASP B CG  
12479 O OD1 . ASP B 513  ? 0.7058 1.1422 0.8233 -0.1142 0.0731  0.1560  511  ASP B OD1 
12480 O OD2 . ASP B 513  ? 0.6200 1.0726 0.7542 -0.1058 0.0731  0.1513  511  ASP B OD2 
12481 N N   . GLU B 514  ? 0.5349 0.9180 0.6286 -0.0989 0.0652  0.1296  512  GLU B N   
12482 C CA  . GLU B 514  ? 0.5863 0.9540 0.6765 -0.0995 0.0601  0.1243  512  GLU B CA  
12483 C C   . GLU B 514  ? 0.5997 0.9506 0.6788 -0.1065 0.0570  0.1261  512  GLU B C   
12484 O O   . GLU B 514  ? 0.5452 0.8837 0.6246 -0.1138 0.0498  0.1260  512  GLU B O   
12485 C CB  . GLU B 514  ? 0.5647 0.9319 0.6512 -0.0869 0.0645  0.1159  512  GLU B CB  
12486 N N   . LEU B 515  ? 0.6158 0.9659 0.6850 -0.1044 0.0619  0.1279  513  LEU B N   
12487 C CA  . LEU B 515  ? 0.5396 0.8736 0.5973 -0.1104 0.0590  0.1299  513  LEU B CA  
12488 C C   . LEU B 515  ? 0.5540 0.8833 0.6148 -0.1236 0.0526  0.1376  513  LEU B C   
12489 O O   . LEU B 515  ? 0.5501 0.8626 0.6048 -0.1303 0.0468  0.1384  513  LEU B O   
12490 C CB  . LEU B 515  ? 0.5212 0.8563 0.5670 -0.1045 0.0659  0.1301  513  LEU B CB  
12491 C CG  . LEU B 515  ? 0.5411 0.8783 0.5811 -0.0910 0.0721  0.1222  513  LEU B CG  
12492 C CD1 . LEU B 515  ? 0.5945 0.9355 0.6244 -0.0860 0.0788  0.1234  513  LEU B CD1 
12493 C CD2 . LEU B 515  ? 0.5004 0.8204 0.5327 -0.0883 0.0687  0.1155  513  LEU B CD2 
12494 N N   . ILE B 516  ? 0.5156 0.8587 0.5857 -0.1274 0.0532  0.1433  514  ILE B N   
12495 C CA  . ILE B 516  ? 0.5055 0.8445 0.5783 -0.1398 0.0472  0.1509  514  ILE B CA  
12496 C C   . ILE B 516  ? 0.4793 0.8155 0.5624 -0.1462 0.0393  0.1507  514  ILE B C   
12497 O O   . ILE B 516  ? 0.4887 0.8228 0.5760 -0.1562 0.0337  0.1566  514  ILE B O   
12498 C CB  . ILE B 516  ? 0.5343 0.8892 0.6107 -0.1416 0.0518  0.1580  514  ILE B CB  
12499 C CG1 . ILE B 516  ? 0.5241 0.8986 0.6138 -0.1374 0.0548  0.1576  514  ILE B CG1 
12500 C CG2 . ILE B 516  ? 0.5168 0.8732 0.5818 -0.1355 0.0594  0.1581  514  ILE B CG2 
12501 C CD1 . ILE B 516  ? 0.5424 0.9342 0.6368 -0.1389 0.0597  0.1645  514  ILE B CD1 
12502 N N   . ALA B 517  ? 0.5009 0.8366 0.5877 -0.1404 0.0386  0.1438  515  ALA B N   
12503 C CA  . ALA B 517  ? 0.4811 0.8120 0.5760 -0.1460 0.0306  0.1426  515  ALA B CA  
12504 C C   . ALA B 517  ? 0.4950 0.8050 0.5839 -0.1559 0.0222  0.1440  515  ALA B C   
12505 O O   . ALA B 517  ? 0.5081 0.8042 0.5865 -0.1549 0.0221  0.1416  515  ALA B O   
12506 C CB  . ALA B 517  ? 0.4554 0.7871 0.5529 -0.1375 0.0315  0.1345  515  ALA B CB  
12507 N N   . ASP B 518  ? 0.4739 0.7810 0.5691 -0.1652 0.0149  0.1478  516  ASP B N   
12508 C CA  . ASP B 518  ? 0.4294 0.7160 0.5196 -0.1748 0.0059  0.1492  516  ASP B CA  
12509 C C   . ASP B 518  ? 0.4579 0.7310 0.5473 -0.1736 0.0004  0.1417  516  ASP B C   
12510 O O   . ASP B 518  ? 0.4745 0.7518 0.5720 -0.1735 -0.0029 0.1391  516  ASP B O   
12511 C CB  . ASP B 518  ? 0.4813 0.7703 0.5784 -0.1846 0.0001  0.1558  516  ASP B CB  
12512 C CG  . ASP B 518  ? 0.5107 0.7773 0.6021 -0.1943 -0.0096 0.1574  516  ASP B CG  
12513 O OD1 . ASP B 518  ? 0.4526 0.7014 0.5355 -0.1935 -0.0125 0.1529  516  ASP B OD1 
12514 O OD2 . ASP B 518  ? 0.5175 0.7839 0.6129 -0.2027 -0.0147 0.1631  516  ASP B OD2 
12515 N N   . PRO B 519  ? 0.4206 0.6771 0.5001 -0.1724 -0.0008 0.1379  517  PRO B N   
12516 C CA  . PRO B 519  ? 0.4153 0.6544 0.4915 -0.1671 -0.0065 0.1278  517  PRO B CA  
12517 C C   . PRO B 519  ? 0.4242 0.6532 0.5046 -0.1766 -0.0164 0.1285  517  PRO B C   
12518 O O   . PRO B 519  ? 0.4179 0.6432 0.5010 -0.1734 -0.0199 0.1221  517  PRO B O   
12519 C CB  . PRO B 519  ? 0.4206 0.6386 0.4824 -0.1617 -0.0069 0.1227  517  PRO B CB  
12520 C CG  . PRO B 519  ? 0.4351 0.6543 0.4926 -0.1682 -0.0052 0.1314  517  PRO B CG  
12521 C CD  . PRO B 519  ? 0.4589 0.7056 0.5264 -0.1709 0.0019  0.1394  517  PRO B CD  
12522 N N   . VAL B 520  ? 0.3807 0.6050 0.4612 -0.1881 -0.0212 0.1363  518  VAL B N   
12523 C CA  . VAL B 520  ? 0.4494 0.6601 0.5315 -0.1958 -0.0315 0.1358  518  VAL B CA  
12524 C C   . VAL B 520  ? 0.4819 0.7069 0.5749 -0.1954 -0.0325 0.1353  518  VAL B C   
12525 O O   . VAL B 520  ? 0.4733 0.6899 0.5679 -0.1962 -0.0389 0.1302  518  VAL B O   
12526 C CB  . VAL B 520  ? 0.4887 0.6899 0.5669 -0.2048 -0.0361 0.1430  518  VAL B CB  
12527 C CG1 . VAL B 520  ? 0.5058 0.6913 0.5846 -0.2121 -0.0470 0.1420  518  VAL B CG1 
12528 C CG2 . VAL B 520  ? 0.4334 0.6203 0.5003 -0.2045 -0.0351 0.1437  518  VAL B CG2 
12529 N N   . GLU B 521  ? 0.4661 0.7128 0.5665 -0.1935 -0.0261 0.1403  519  GLU B N   
12530 C CA  . GLU B 521  ? 0.4578 0.7190 0.5690 -0.1929 -0.0268 0.1404  519  GLU B CA  
12531 C C   . GLU B 521  ? 0.4687 0.7375 0.5832 -0.1836 -0.0232 0.1333  519  GLU B C   
12532 O O   . GLU B 521  ? 0.4504 0.7222 0.5710 -0.1836 -0.0271 0.1307  519  GLU B O   
12533 C CB  . GLU B 521  ? 0.4584 0.7402 0.5767 -0.1937 -0.0212 0.1480  519  GLU B CB  
12534 C CG  . GLU B 521  ? 0.4659 0.7420 0.5816 -0.2032 -0.0245 0.1557  519  GLU B CG  
12535 C CD  . GLU B 521  ? 0.5313 0.7911 0.6467 -0.2124 -0.0357 0.1561  519  GLU B CD  
12536 O OE1 . GLU B 521  ? 0.5435 0.8041 0.6643 -0.2123 -0.0400 0.1526  519  GLU B OE1 
12537 O OE2 . GLU B 521  ? 0.5625 0.8081 0.6717 -0.2195 -0.0403 0.1599  519  GLU B OE2 
12538 N N   . VAL B 522  ? 0.4633 0.7348 0.5735 -0.1756 -0.0162 0.1299  520  VAL B N   
12539 C CA  . VAL B 522  ? 0.4272 0.7045 0.5401 -0.1667 -0.0133 0.1230  520  VAL B CA  
12540 C C   . VAL B 522  ? 0.4689 0.7270 0.5775 -0.1678 -0.0212 0.1159  520  VAL B C   
12541 O O   . VAL B 522  ? 0.4494 0.7109 0.5628 -0.1648 -0.0234 0.1117  520  VAL B O   
12542 C CB  . VAL B 522  ? 0.4280 0.7108 0.5358 -0.1571 -0.0040 0.1206  520  VAL B CB  
12543 C CG1 . VAL B 522  ? 0.3913 0.6766 0.5002 -0.1458 -0.0015 0.1123  520  VAL B CG1 
12544 C CG2 . VAL B 522  ? 0.4674 0.7678 0.5779 -0.1552 0.0038  0.1268  520  VAL B CG2 
12545 N N   . VAL B 523  ? 0.4391 0.6743 0.5368 -0.1701 -0.0259 0.1136  521  VAL B N   
12546 C CA  . VAL B 523  ? 0.4418 0.6556 0.5333 -0.1692 -0.0336 0.1058  521  VAL B CA  
12547 C C   . VAL B 523  ? 0.4710 0.6854 0.5696 -0.1788 -0.0419 0.1082  521  VAL B C   
12548 O O   . VAL B 523  ? 0.4816 0.6903 0.5802 -0.1762 -0.0461 0.1019  521  VAL B O   
12549 C CB  . VAL B 523  ? 0.4662 0.6561 0.5452 -0.1699 -0.0369 0.1034  521  VAL B CB  
12550 C CG1 . VAL B 523  ? 0.4265 0.5951 0.5001 -0.1709 -0.0457 0.0966  521  VAL B CG1 
12551 C CG2 . VAL B 523  ? 0.4271 0.6143 0.4983 -0.1591 -0.0297 0.0990  521  VAL B CG2 
12552 N N   . ARG B 524  ? 0.4574 0.6763 0.5602 -0.1883 -0.0443 0.1164  522  ARG B N   
12553 C CA  . ARG B 524  ? 0.5009 0.7145 0.6067 -0.1949 -0.0527 0.1174  522  ARG B CA  
12554 C C   . ARG B 524  ? 0.4961 0.7252 0.6109 -0.1913 -0.0519 0.1157  522  ARG B C   
12555 O O   . ARG B 524  ? 0.5371 0.7589 0.6526 -0.1943 -0.0593 0.1130  522  ARG B O   
12556 C CB  . ARG B 524  ? 0.4837 0.6993 0.5910 -0.2030 -0.0541 0.1261  522  ARG B CB  
12557 C CG  . ARG B 524  ? 0.4821 0.6888 0.5910 -0.2109 -0.0636 0.1276  522  ARG B CG  
12558 C CD  . ARG B 524  ? 0.5290 0.7463 0.6434 -0.2178 -0.0633 0.1370  522  ARG B CD  
12559 N NE  . ARG B 524  ? 0.5096 0.7216 0.6184 -0.2210 -0.0612 0.1421  522  ARG B NE  
12560 C CZ  . ARG B 524  ? 0.5643 0.7546 0.6646 -0.2267 -0.0678 0.1425  522  ARG B CZ  
12561 N NH1 . ARG B 524  ? 0.5541 0.7253 0.6501 -0.2297 -0.0771 0.1378  522  ARG B NH1 
12562 N NH2 . ARG B 524  ? 0.5674 0.7545 0.6627 -0.2289 -0.0652 0.1475  522  ARG B NH2 
12563 N N   . ALA B 525  ? 0.4675 0.7172 0.5887 -0.1844 -0.0433 0.1170  523  ALA B N   
12564 C CA  . ALA B 525  ? 0.4745 0.7401 0.6048 -0.1805 -0.0422 0.1163  523  ALA B CA  
12565 C C   . ALA B 525  ? 0.4868 0.7510 0.6160 -0.1726 -0.0415 0.1082  523  ALA B C   
12566 O O   . ALA B 525  ? 0.4696 0.7449 0.6054 -0.1690 -0.0413 0.1070  523  ALA B O   
12567 C CB  . ALA B 525  ? 0.4761 0.7649 0.6142 -0.1767 -0.0335 0.1220  523  ALA B CB  
12568 N N   . MET B 526  ? 0.4509 0.7019 0.5719 -0.1699 -0.0412 0.1029  524  MET B N   
12569 C CA  A MET B 526  ? 0.4740 0.7202 0.5913 -0.1602 -0.0402 0.0944  524  MET B CA  
12570 C CA  B MET B 526  ? 0.4741 0.7200 0.5912 -0.1602 -0.0403 0.0943  524  MET B CA  
12571 C C   . MET B 526  ? 0.4947 0.7328 0.6124 -0.1639 -0.0491 0.0906  524  MET B C   
12572 O O   . MET B 526  ? 0.4637 0.6914 0.5801 -0.1731 -0.0568 0.0925  524  MET B O   
12573 C CB  A MET B 526  ? 0.4717 0.6985 0.5759 -0.1532 -0.0380 0.0878  524  MET B CB  
12574 C CB  B MET B 526  ? 0.4720 0.6979 0.5758 -0.1534 -0.0384 0.0878  524  MET B CB  
12575 C CG  A MET B 526  ? 0.4844 0.7183 0.5869 -0.1491 -0.0296 0.0910  524  MET B CG  
12576 C CG  B MET B 526  ? 0.4847 0.7181 0.5867 -0.1473 -0.0292 0.0896  524  MET B CG  
12577 S SD  A MET B 526  ? 0.4720 0.6884 0.5611 -0.1379 -0.0256 0.0825  524  MET B SD  
12578 S SD  B MET B 526  ? 0.4797 0.7358 0.5895 -0.1368 -0.0205 0.0888  524  MET B SD  
12579 C CE  A MET B 526  ? 0.4426 0.6718 0.5317 -0.1358 -0.0165 0.0885  524  MET B CE  
12580 C CE  B MET B 526  ? 0.4714 0.7124 0.5737 -0.1270 -0.0222 0.0778  524  MET B CE  
12581 N N   . PRO B 527  ? 0.4958 0.7374 0.6144 -0.1562 -0.0482 0.0852  525  PRO B N   
12582 C CA  . PRO B 527  ? 0.5301 0.7644 0.6483 -0.1594 -0.0566 0.0816  525  PRO B CA  
12583 C C   . PRO B 527  ? 0.4702 0.6778 0.5756 -0.1605 -0.0627 0.0751  525  PRO B C   
12584 O O   . PRO B 527  ? 0.4409 0.6396 0.5451 -0.1674 -0.0713 0.0743  525  PRO B O   
12585 C CB  . PRO B 527  ? 0.4795 0.7233 0.6002 -0.1494 -0.0527 0.0773  525  PRO B CB  
12586 C CG  . PRO B 527  ? 0.5075 0.7521 0.6242 -0.1397 -0.0436 0.0751  525  PRO B CG  
12587 C CD  . PRO B 527  ? 0.5020 0.7538 0.6217 -0.1445 -0.0399 0.0822  525  PRO B CD  
12588 N N   . VAL B 528  ? 0.4473 0.6419 0.5431 -0.1535 -0.0587 0.0703  526  VAL B N   
12589 C CA  . VAL B 528  ? 0.4366 0.6066 0.5207 -0.1540 -0.0638 0.0646  526  VAL B CA  
12590 C C   . VAL B 528  ? 0.3820 0.5455 0.4618 -0.1550 -0.0607 0.0674  526  VAL B C   
12591 O O   . VAL B 528  ? 0.4149 0.5812 0.4924 -0.1473 -0.0533 0.0661  526  VAL B O   
12592 C CB  . VAL B 528  ? 0.4308 0.5904 0.5069 -0.1438 -0.0623 0.0554  526  VAL B CB  
12593 C CG1 . VAL B 528  ? 0.4316 0.5670 0.4959 -0.1430 -0.0659 0.0497  526  VAL B CG1 
12594 C CG2 . VAL B 528  ? 0.4284 0.5925 0.5073 -0.1436 -0.0664 0.0526  526  VAL B CG2 
12595 N N   . VAL B 529  ? 0.3572 0.5121 0.4360 -0.1647 -0.0665 0.0716  527  VAL B N   
12596 C CA  . VAL B 529  ? 0.3694 0.5174 0.4437 -0.1663 -0.0642 0.0748  527  VAL B CA  
12597 C C   . VAL B 529  ? 0.3713 0.5001 0.4339 -0.1581 -0.0633 0.0669  527  VAL B C   
12598 O O   . VAL B 529  ? 0.3861 0.4983 0.4422 -0.1570 -0.0690 0.0604  527  VAL B O   
12599 C CB  . VAL B 529  ? 0.4134 0.5539 0.4882 -0.1787 -0.0716 0.0808  527  VAL B CB  
12600 C CG1 . VAL B 529  ? 0.4181 0.5494 0.4869 -0.1799 -0.0697 0.0839  527  VAL B CG1 
12601 C CG2 . VAL B 529  ? 0.4039 0.5658 0.4917 -0.1872 -0.0719 0.0896  527  VAL B CG2 
12602 N N   . GLY B 530  ? 0.3493 0.4811 0.4095 -0.1519 -0.0561 0.0672  528  GLY B N   
12603 C CA  . GLY B 530  ? 0.3583 0.4733 0.4084 -0.1446 -0.0551 0.0606  528  GLY B CA  
12604 C C   . GLY B 530  ? 0.3247 0.4385 0.3723 -0.1344 -0.0522 0.0524  528  GLY B C   
12605 O O   . GLY B 530  ? 0.3354 0.4339 0.3749 -0.1290 -0.0528 0.0463  528  GLY B O   
12606 N N   . ALA B 531  ? 0.2706 0.4001 0.3250 -0.1316 -0.0493 0.0524  529  ALA B N   
12607 C CA  . ALA B 531  ? 0.2979 0.4267 0.3499 -0.1219 -0.0462 0.0453  529  ALA B CA  
12608 C C   . ALA B 531  ? 0.3247 0.4504 0.3718 -0.1139 -0.0399 0.0428  529  ALA B C   
12609 O O   . ALA B 531  ? 0.3395 0.4737 0.3885 -0.1139 -0.0351 0.0475  529  ALA B O   
12610 C CB  . ALA B 531  ? 0.3490 0.4968 0.4097 -0.1199 -0.0433 0.0469  529  ALA B CB  
12611 N N   . LYS B 532  ? 0.2496 0.3627 0.2900 -0.1073 -0.0402 0.0355  530  LYS B N   
12612 C CA  . LYS B 532  ? 0.3014 0.4115 0.3374 -0.0992 -0.0347 0.0323  530  LYS B CA  
12613 C C   . LYS B 532  ? 0.3130 0.4405 0.3545 -0.0940 -0.0277 0.0341  530  LYS B C   
12614 O O   . LYS B 532  ? 0.2927 0.4326 0.3407 -0.0943 -0.0271 0.0354  530  LYS B O   
12615 C CB  . LYS B 532  ? 0.3299 0.4268 0.3599 -0.0932 -0.0363 0.0242  530  LYS B CB  
12616 C CG  . LYS B 532  ? 0.3582 0.4532 0.3849 -0.0845 -0.0309 0.0204  530  LYS B CG  
12617 C CD  . LYS B 532  ? 0.3468 0.4311 0.3689 -0.0792 -0.0323 0.0131  530  LYS B CD  
12618 C CE  . LYS B 532  ? 0.3554 0.4478 0.3811 -0.0775 -0.0321 0.0113  530  LYS B CE  
12619 N NZ  . LYS B 532  ? 0.3428 0.4483 0.3726 -0.0719 -0.0259 0.0122  530  LYS B NZ  
12620 N N   . HIS B 533  ? 0.3049 0.4328 0.3435 -0.0891 -0.0225 0.0340  531  HIS B N   
12621 C CA  . HIS B 533  ? 0.2955 0.4375 0.3378 -0.0829 -0.0158 0.0346  531  HIS B CA  
12622 C C   . HIS B 533  ? 0.3351 0.4788 0.3788 -0.0769 -0.0152 0.0296  531  HIS B C   
12623 O O   . HIS B 533  ? 0.2766 0.4080 0.3153 -0.0738 -0.0172 0.0240  531  HIS B O   
12624 C CB  . HIS B 533  ? 0.3258 0.4631 0.3622 -0.0777 -0.0115 0.0334  531  HIS B CB  
12625 C CG  . HIS B 533  ? 0.3436 0.4952 0.3829 -0.0726 -0.0047 0.0353  531  HIS B CG  
12626 N ND1 . HIS B 533  ? 0.2972 0.4556 0.3392 -0.0658 -0.0015 0.0321  531  HIS B ND1 
12627 C CD2 . HIS B 533  ? 0.3696 0.5295 0.4088 -0.0730 -0.0004 0.0398  531  HIS B CD2 
12628 C CE1 . HIS B 533  ? 0.3468 0.5167 0.3905 -0.0619 0.0043  0.0344  531  HIS B CE1 
12629 N NE2 . HIS B 533  ? 0.4127 0.5841 0.4546 -0.0661 0.0053  0.0390  531  HIS B NE2 
12630 N N   . ASP B 534  ? 0.3095 0.4692 0.3603 -0.0752 -0.0122 0.0320  532  ASP B N   
12631 C CA  . ASP B 534  ? 0.3130 0.4753 0.3657 -0.0701 -0.0119 0.0282  532  ASP B CA  
12632 C C   . ASP B 534  ? 0.3146 0.4703 0.3622 -0.0615 -0.0084 0.0228  532  ASP B C   
12633 O O   . ASP B 534  ? 0.3034 0.4556 0.3501 -0.0579 -0.0093 0.0187  532  ASP B O   
12634 C CB  . ASP B 534  ? 0.2757 0.4571 0.3374 -0.0696 -0.0093 0.0324  532  ASP B CB  
12635 N N   . ARG B 535  ? 0.3037 0.4573 0.3478 -0.0585 -0.0046 0.0229  533  ARG B N   
12636 C CA  . ARG B 535  ? 0.2996 0.4487 0.3397 -0.0505 -0.0011 0.0185  533  ARG B CA  
12637 C C   . ARG B 535  ? 0.3236 0.4566 0.3562 -0.0498 -0.0028 0.0147  533  ARG B C   
12638 O O   . ARG B 535  ? 0.3295 0.4583 0.3585 -0.0440 0.0000  0.0116  533  ARG B O   
12639 C CB  . ARG B 535  ? 0.3650 0.5249 0.4067 -0.0463 0.0048  0.0209  533  ARG B CB  
12640 N N   . ILE B 536  ? 0.2922 0.4159 0.3224 -0.0555 -0.0075 0.0149  534  ILE B N   
12641 C CA  . ILE B 536  ? 0.2790 0.3874 0.3026 -0.0546 -0.0097 0.0112  534  ILE B CA  
12642 C C   . ILE B 536  ? 0.3108 0.4105 0.3332 -0.0559 -0.0143 0.0074  534  ILE B C   
12643 O O   . ILE B 536  ? 0.2793 0.3787 0.3032 -0.0617 -0.0184 0.0092  534  ILE B O   
12644 C CB  . ILE B 536  ? 0.2669 0.3703 0.2876 -0.0595 -0.0113 0.0147  534  ILE B CB  
12645 C CG1 . ILE B 536  ? 0.2871 0.4001 0.3082 -0.0580 -0.0063 0.0186  534  ILE B CG1 
12646 C CG2 . ILE B 536  ? 0.2838 0.3714 0.2981 -0.0579 -0.0139 0.0107  534  ILE B CG2 
12647 C CD1 . ILE B 536  ? 0.3416 0.4506 0.3593 -0.0629 -0.0075 0.0227  534  ILE B CD1 
12648 N N   . ALA B 537  ? 0.2793 0.3720 0.2988 -0.0505 -0.0138 0.0022  535  ALA B N   
12649 C CA  . ALA B 537  ? 0.3229 0.4081 0.3407 -0.0508 -0.0174 -0.0018 535  ALA B CA  
12650 C C   . ALA B 537  ? 0.2620 0.3336 0.2751 -0.0538 -0.0218 -0.0035 535  ALA B C   
12651 O O   . ALA B 537  ? 0.2661 0.3309 0.2762 -0.0521 -0.0212 -0.0042 535  ALA B O   
12652 C CB  . ALA B 537  ? 0.2789 0.3625 0.2956 -0.0442 -0.0148 -0.0063 535  ALA B CB  
12653 N N   . LEU B 538  ? 0.2850 0.3521 0.2973 -0.0579 -0.0264 -0.0043 536  LEU B N   
12654 C CA  . LEU B 538  ? 0.3059 0.3584 0.3131 -0.0589 -0.0307 -0.0076 536  LEU B CA  
12655 C C   . LEU B 538  ? 0.2784 0.3249 0.2828 -0.0520 -0.0287 -0.0131 536  LEU B C   
12656 O O   . LEU B 538  ? 0.2682 0.3208 0.2742 -0.0479 -0.0254 -0.0148 536  LEU B O   
12657 C CB  . LEU B 538  ? 0.2975 0.3457 0.3035 -0.0634 -0.0360 -0.0086 536  LEU B CB  
12658 C CG  . LEU B 538  ? 0.3582 0.4082 0.3662 -0.0715 -0.0399 -0.0036 536  LEU B CG  
12659 C CD1 . LEU B 538  ? 0.3616 0.4065 0.3677 -0.0749 -0.0454 -0.0060 536  LEU B CD1 
12660 C CD2 . LEU B 538  ? 0.3201 0.3612 0.3255 -0.0745 -0.0420 -0.0014 536  LEU B CD2 
12661 N N   . PRO B 539  ? 0.2848 0.3197 0.2853 -0.0507 -0.0306 -0.0156 537  PRO B N   
12662 C CA  . PRO B 539  ? 0.2878 0.3183 0.2867 -0.0443 -0.0286 -0.0206 537  PRO B CA  
12663 C C   . PRO B 539  ? 0.2719 0.3033 0.2703 -0.0421 -0.0285 -0.0245 537  PRO B C   
12664 O O   . PRO B 539  ? 0.2751 0.3100 0.2744 -0.0372 -0.0250 -0.0267 537  PRO B O   
12665 C CB  . PRO B 539  ? 0.2898 0.3073 0.2849 -0.0444 -0.0320 -0.0224 537  PRO B CB  
12666 C CG  . PRO B 539  ? 0.2538 0.2710 0.2489 -0.0498 -0.0339 -0.0171 537  PRO B CG  
12667 C CD  . PRO B 539  ? 0.2931 0.3191 0.2911 -0.0549 -0.0344 -0.0136 537  PRO B CD  
12668 N N   . ALA B 540  ? 0.2601 0.2885 0.2567 -0.0458 -0.0325 -0.0251 538  ALA B N   
12669 C CA  . ALA B 540  ? 0.3250 0.3538 0.3199 -0.0439 -0.0327 -0.0288 538  ALA B CA  
12670 C C   . ALA B 540  ? 0.3442 0.3855 0.3428 -0.0428 -0.0293 -0.0269 538  ALA B C   
12671 O O   . ALA B 540  ? 0.2967 0.3394 0.2940 -0.0398 -0.0281 -0.0297 538  ALA B O   
12672 C CB  . ALA B 540  ? 0.3399 0.3621 0.3314 -0.0485 -0.0384 -0.0299 538  ALA B CB  
12673 N N   . GLU B 541  ? 0.3136 0.3639 0.3166 -0.0450 -0.0276 -0.0220 539  GLU B N   
12674 C CA  . GLU B 541  ? 0.3206 0.3831 0.3277 -0.0442 -0.0249 -0.0195 539  GLU B CA  
12675 C C   . GLU B 541  ? 0.3195 0.3877 0.3292 -0.0394 -0.0197 -0.0186 539  GLU B C   
12676 O O   . GLU B 541  ? 0.2842 0.3626 0.2978 -0.0386 -0.0173 -0.0159 539  GLU B O   
12677 C CB  . GLU B 541  ? 0.2861 0.3557 0.2967 -0.0502 -0.0271 -0.0147 539  GLU B CB  
12678 C CG  . GLU B 541  ? 0.3202 0.3851 0.3282 -0.0549 -0.0328 -0.0158 539  GLU B CG  
12679 C CD  . GLU B 541  ? 0.4852 0.5554 0.4969 -0.0621 -0.0361 -0.0108 539  GLU B CD  
12680 O OE1 . GLU B 541  ? 0.4730 0.5535 0.4900 -0.0633 -0.0335 -0.0060 539  GLU B OE1 
12681 O OE2 . GLU B 541  ? 0.4994 0.5632 0.5084 -0.0667 -0.0416 -0.0117 539  GLU B OE2 
12682 N N   . LEU B 542  ? 0.2718 0.3332 0.2795 -0.0360 -0.0183 -0.0210 540  LEU B N   
12683 C CA  . LEU B 542  ? 0.2793 0.3447 0.2889 -0.0318 -0.0140 -0.0204 540  LEU B CA  
12684 C C   . LEU B 542  ? 0.3061 0.3780 0.3175 -0.0281 -0.0111 -0.0210 540  LEU B C   
12685 O O   . LEU B 542  ? 0.2922 0.3699 0.3060 -0.0255 -0.0079 -0.0194 540  LEU B O   
12686 C CB  . LEU B 542  ? 0.3069 0.3634 0.3139 -0.0288 -0.0137 -0.0235 540  LEU B CB  
12687 C CG  . LEU B 542  ? 0.3355 0.3863 0.3410 -0.0303 -0.0150 -0.0223 540  LEU B CG  
12688 C CD1 . LEU B 542  ? 0.3032 0.3480 0.3075 -0.0260 -0.0139 -0.0252 540  LEU B CD1 
12689 C CD2 . LEU B 542  ? 0.3025 0.3604 0.3098 -0.0323 -0.0133 -0.0176 540  LEU B CD2 
12690 N N   . PHE B 543  ? 0.2620 0.3326 0.2720 -0.0277 -0.0123 -0.0234 541  PHE B N   
12691 C CA  . PHE B 543  ? 0.2883 0.3642 0.2995 -0.0243 -0.0098 -0.0238 541  PHE B CA  
12692 C C   . PHE B 543  ? 0.2764 0.3597 0.2892 -0.0265 -0.0111 -0.0216 541  PHE B C   
12693 O O   . PHE B 543  ? 0.2827 0.3697 0.2958 -0.0241 -0.0098 -0.0218 541  PHE B O   
12694 C CB  . PHE B 543  ? 0.2449 0.3145 0.2530 -0.0214 -0.0094 -0.0279 541  PHE B CB  
12695 C CG  . PHE B 543  ? 0.2594 0.3222 0.2667 -0.0195 -0.0087 -0.0300 541  PHE B CG  
12696 C CD1 . PHE B 543  ? 0.2616 0.3259 0.2711 -0.0171 -0.0061 -0.0289 541  PHE B CD1 
12697 C CD2 . PHE B 543  ? 0.2572 0.3118 0.2614 -0.0200 -0.0109 -0.0331 541  PHE B CD2 
12698 C CE1 . PHE B 543  ? 0.2517 0.3099 0.2605 -0.0156 -0.0060 -0.0306 541  PHE B CE1 
12699 C CE2 . PHE B 543  ? 0.2827 0.3314 0.2867 -0.0180 -0.0106 -0.0348 541  PHE B CE2 
12700 C CZ  . PHE B 543  ? 0.2927 0.3434 0.2992 -0.0160 -0.0082 -0.0334 541  PHE B CZ  
12701 N N   . GLY B 544  ? 0.3145 0.4001 0.3285 -0.0312 -0.0138 -0.0192 542  GLY B N   
12702 C CA  . GLY B 544  ? 0.3019 0.3963 0.3188 -0.0335 -0.0152 -0.0164 542  GLY B CA  
12703 C C   . GLY B 544  ? 0.3856 0.4777 0.3990 -0.0339 -0.0178 -0.0188 542  GLY B C   
12704 O O   . GLY B 544  ? 0.3415 0.4247 0.3500 -0.0350 -0.0202 -0.0222 542  GLY B O   
12705 N N   . ASP B 545  ? 0.3190 0.4190 0.3345 -0.0327 -0.0173 -0.0171 543  ASP B N   
12706 C CA  . ASP B 545  ? 0.3882 0.4869 0.4000 -0.0331 -0.0197 -0.0189 543  ASP B CA  
12707 C C   . ASP B 545  ? 0.3355 0.4285 0.3428 -0.0288 -0.0174 -0.0225 543  ASP B C   
12708 O O   . ASP B 545  ? 0.3482 0.4387 0.3508 -0.0289 -0.0192 -0.0246 543  ASP B O   
12709 C CB  . ASP B 545  ? 0.4240 0.5334 0.4397 -0.0334 -0.0203 -0.0154 543  ASP B CB  
12710 C CG  . ASP B 545  ? 0.4943 0.6109 0.5153 -0.0381 -0.0228 -0.0115 543  ASP B CG  
12711 O OD1 . ASP B 545  ? 0.4874 0.5991 0.5069 -0.0427 -0.0260 -0.0120 543  ASP B OD1 
12712 O OD2 . ASP B 545  ? 0.6358 0.7631 0.6626 -0.0371 -0.0215 -0.0078 543  ASP B OD2 
12713 N N   . ALA B 546  ? 0.3147 0.4057 0.3231 -0.0251 -0.0136 -0.0232 544  ALA B N   
12714 C CA  . ALA B 546  ? 0.3030 0.3897 0.3082 -0.0213 -0.0112 -0.0260 544  ALA B CA  
12715 C C   . ALA B 546  ? 0.3403 0.4183 0.3400 -0.0220 -0.0129 -0.0303 544  ALA B C   
12716 O O   . ALA B 546  ? 0.2859 0.3622 0.2815 -0.0204 -0.0125 -0.0325 544  ALA B O   
12717 C CB  . ALA B 546  ? 0.2969 0.3830 0.3050 -0.0179 -0.0075 -0.0258 544  ALA B CB  
12718 N N   . ARG B 547  ? 0.2897 0.3621 0.2890 -0.0241 -0.0147 -0.0314 545  ARG B N   
12719 C CA  . ARG B 547  ? 0.2869 0.3502 0.2811 -0.0239 -0.0163 -0.0358 545  ARG B CA  
12720 C C   . ARG B 547  ? 0.2934 0.3511 0.2880 -0.0268 -0.0189 -0.0358 545  ARG B C   
12721 O O   . ARG B 547  ? 0.3019 0.3626 0.3007 -0.0280 -0.0182 -0.0326 545  ARG B O   
12722 C CB  . ARG B 547  ? 0.3119 0.3724 0.3055 -0.0193 -0.0127 -0.0384 545  ARG B CB  
12723 C CG  . ARG B 547  ? 0.2889 0.3487 0.2865 -0.0176 -0.0104 -0.0375 545  ARG B CG  
12724 C CD  . ARG B 547  ? 0.3083 0.3653 0.3058 -0.0136 -0.0076 -0.0402 545  ARG B CD  
12725 N NE  . ARG B 547  ? 0.2902 0.3491 0.2920 -0.0119 -0.0051 -0.0384 545  ARG B NE  
12726 C CZ  . ARG B 547  ? 0.2994 0.3539 0.3026 -0.0111 -0.0052 -0.0393 545  ARG B CZ  
12727 N NH1 . ARG B 547  ? 0.2573 0.3050 0.2583 -0.0113 -0.0072 -0.0421 545  ARG B NH1 
12728 N NH2 . ARG B 547  ? 0.3096 0.3661 0.3162 -0.0098 -0.0033 -0.0375 545  ARG B NH2 
12729 N N   . THR B 548  ? 0.2801 0.3292 0.2699 -0.0277 -0.0219 -0.0393 546  THR B N   
12730 C CA  . THR B 548  ? 0.2904 0.3323 0.2797 -0.0305 -0.0251 -0.0395 546  THR B CA  
12731 C C   . THR B 548  ? 0.3021 0.3386 0.2920 -0.0270 -0.0230 -0.0415 546  THR B C   
12732 O O   . THR B 548  ? 0.2771 0.3106 0.2648 -0.0230 -0.0213 -0.0451 546  THR B O   
12733 C CB  . THR B 548  ? 0.3019 0.3358 0.2853 -0.0330 -0.0300 -0.0427 546  THR B CB  
12734 O OG1 . THR B 548  ? 0.3667 0.4061 0.3497 -0.0364 -0.0323 -0.0408 546  THR B OG1 
12735 C CG2 . THR B 548  ? 0.3249 0.3504 0.3076 -0.0363 -0.0338 -0.0426 546  THR B CG2 
12736 N N   . ASN B 549  ? 0.2510 0.2872 0.2439 -0.0284 -0.0230 -0.0388 547  ASN B N   
12737 C CA  . ASN B 549  ? 0.2685 0.2994 0.2620 -0.0255 -0.0218 -0.0402 547  ASN B CA  
12738 C C   . ASN B 549  ? 0.2643 0.2842 0.2534 -0.0251 -0.0252 -0.0443 547  ASN B C   
12739 O O   . ASN B 549  ? 0.3316 0.3464 0.3176 -0.0287 -0.0294 -0.0447 547  ASN B O   
12740 C CB  . ASN B 549  ? 0.2640 0.2965 0.2605 -0.0277 -0.0217 -0.0362 547  ASN B CB  
12741 C CG  . ASN B 549  ? 0.2877 0.3161 0.2850 -0.0245 -0.0204 -0.0371 547  ASN B CG  
12742 O OD1 . ASN B 549  ? 0.2800 0.3070 0.2774 -0.0203 -0.0185 -0.0402 547  ASN B OD1 
12743 N ND2 . ASN B 549  ? 0.2770 0.3039 0.2750 -0.0267 -0.0213 -0.0342 547  ASN B ND2 
12744 N N   . SER B 550  ? 0.2601 0.2763 0.2491 -0.0205 -0.0235 -0.0476 548  SER B N   
12745 C CA  . SER B 550  ? 0.3053 0.3108 0.2906 -0.0192 -0.0266 -0.0515 548  SER B CA  
12746 C C   . SER B 550  ? 0.2977 0.2964 0.2827 -0.0227 -0.0305 -0.0493 548  SER B C   
12747 O O   . SER B 550  ? 0.3055 0.3079 0.2937 -0.0247 -0.0296 -0.0452 548  SER B O   
12748 C CB  . SER B 550  ? 0.2823 0.2868 0.2692 -0.0135 -0.0238 -0.0546 548  SER B CB  
12749 O OG  . SER B 550  ? 0.3112 0.3177 0.3024 -0.0129 -0.0223 -0.0520 548  SER B OG  
12750 N N   . ALA B 551  ? 0.3352 0.3233 0.3159 -0.0233 -0.0348 -0.0522 549  ALA B N   
12751 C CA  . ALA B 551  ? 0.3260 0.3057 0.3057 -0.0267 -0.0392 -0.0503 549  ALA B CA  
12752 C C   . ALA B 551  ? 0.3477 0.3188 0.3268 -0.0223 -0.0401 -0.0533 549  ALA B C   
12753 O O   . ALA B 551  ? 0.3480 0.3161 0.3255 -0.0174 -0.0394 -0.0582 549  ALA B O   
12754 C CB  . ALA B 551  ? 0.3714 0.3440 0.3465 -0.0314 -0.0445 -0.0508 549  ALA B CB  
12755 N N   . GLY B 552  ? 0.3505 0.3184 0.3311 -0.0238 -0.0415 -0.0501 550  GLY B N   
12756 C CA  . GLY B 552  ? 0.3512 0.3103 0.3313 -0.0202 -0.0434 -0.0522 550  GLY B CA  
12757 C C   . GLY B 552  ? 0.3401 0.2860 0.3158 -0.0232 -0.0497 -0.0524 550  GLY B C   
12758 O O   . GLY B 552  ? 0.3866 0.3289 0.3590 -0.0273 -0.0528 -0.0524 550  GLY B O   
12759 N N   . LEU B 553  ? 0.3578 0.2959 0.3336 -0.0212 -0.0519 -0.0523 551  LEU B N   
12760 C CA  . LEU B 553  ? 0.4273 0.3512 0.3988 -0.0233 -0.0583 -0.0524 551  LEU B CA  
12761 C C   . LEU B 553  ? 0.3711 0.2926 0.3438 -0.0253 -0.0597 -0.0474 551  LEU B C   
12762 O O   . LEU B 553  ? 0.3947 0.3215 0.3709 -0.0217 -0.0566 -0.0469 551  LEU B O   
12763 C CB  . LEU B 553  ? 0.3973 0.3113 0.3664 -0.0171 -0.0605 -0.0589 551  LEU B CB  
12764 C CG  . LEU B 553  ? 0.3907 0.3045 0.3565 -0.0149 -0.0599 -0.0644 551  LEU B CG  
12765 C CD1 . LEU B 553  ? 0.4344 0.3405 0.3985 -0.0075 -0.0607 -0.0709 551  LEU B CD1 
12766 C CD2 . LEU B 553  ? 0.4348 0.3423 0.3957 -0.0214 -0.0646 -0.0634 551  LEU B CD2 
12767 N N   . ASP B 554  ? 0.3709 0.2845 0.3406 -0.0312 -0.0645 -0.0436 552  ASP B N   
12768 C CA  . ASP B 554  ? 0.3794 0.2915 0.3493 -0.0343 -0.0659 -0.0379 552  ASP B CA  
12769 C C   . ASP B 554  ? 0.3958 0.2938 0.3633 -0.0310 -0.0707 -0.0397 552  ASP B C   
12770 O O   . ASP B 554  ? 0.3778 0.2631 0.3412 -0.0333 -0.0764 -0.0403 552  ASP B O   
12771 C CB  . ASP B 554  ? 0.4348 0.3470 0.4031 -0.0431 -0.0682 -0.0321 552  ASP B CB  
12772 C CG  . ASP B 554  ? 0.3949 0.3066 0.3629 -0.0468 -0.0691 -0.0255 552  ASP B CG  
12773 O OD1 . ASP B 554  ? 0.3839 0.2946 0.3523 -0.0428 -0.0682 -0.0254 552  ASP B OD1 
12774 O OD2 . ASP B 554  ? 0.4239 0.3365 0.3909 -0.0542 -0.0708 -0.0202 552  ASP B OD2 
12775 N N   . LEU B 555  ? 0.3503 0.2503 0.3204 -0.0257 -0.0688 -0.0405 553  LEU B N   
12776 C CA  . LEU B 555  ? 0.3828 0.2701 0.3513 -0.0216 -0.0734 -0.0425 553  LEU B CA  
12777 C C   . LEU B 555  ? 0.4082 0.2873 0.3737 -0.0263 -0.0779 -0.0365 553  LEU B C   
12778 O O   . LEU B 555  ? 0.3646 0.2337 0.3289 -0.0231 -0.0819 -0.0372 553  LEU B O   
12779 C CB  . LEU B 555  ? 0.4013 0.2940 0.3744 -0.0139 -0.0702 -0.0459 553  LEU B CB  
12780 C CG  . LEU B 555  ? 0.4345 0.3331 0.4100 -0.0087 -0.0664 -0.0522 553  LEU B CG  
12781 C CD1 . LEU B 555  ? 0.4161 0.3204 0.3969 -0.0015 -0.0634 -0.0551 553  LEU B CD1 
12782 C CD2 . LEU B 555  ? 0.4355 0.3227 0.4068 -0.0072 -0.0703 -0.0571 553  LEU B CD2 
12783 N N   . SER B 556  ? 0.4317 0.3154 0.3960 -0.0338 -0.0774 -0.0305 554  SER B N   
12784 C CA  . SER B 556  ? 0.4354 0.3109 0.3960 -0.0395 -0.0819 -0.0242 554  SER B CA  
12785 C C   . SER B 556  ? 0.4374 0.3036 0.3945 -0.0460 -0.0869 -0.0228 554  SER B C   
12786 O O   . SER B 556  ? 0.4353 0.2936 0.3892 -0.0516 -0.0913 -0.0173 554  SER B O   
12787 C CB  . SER B 556  ? 0.4390 0.3265 0.4006 -0.0437 -0.0778 -0.0178 554  SER B CB  
12788 O OG  . SER B 556  ? 0.4094 0.3061 0.3722 -0.0494 -0.0751 -0.0154 554  SER B OG  
12789 N N   . ASN B 557  ? 0.4273 0.2940 0.3846 -0.0455 -0.0867 -0.0274 555  ASN B N   
12790 C CA  . ASN B 557  ? 0.4261 0.2844 0.3801 -0.0518 -0.0917 -0.0265 555  ASN B CA  
12791 C C   . ASN B 557  ? 0.4671 0.3071 0.4168 -0.0480 -0.0981 -0.0317 555  ASN B C   
12792 O O   . ASN B 557  ? 0.4357 0.2747 0.3858 -0.0407 -0.0968 -0.0389 555  ASN B O   
12793 C CB  . ASN B 557  ? 0.4142 0.2831 0.3701 -0.0534 -0.0882 -0.0287 555  ASN B CB  
12794 C CG  . ASN B 557  ? 0.4509 0.3124 0.4038 -0.0607 -0.0935 -0.0275 555  ASN B CG  
12795 O OD1 . ASN B 557  ? 0.4648 0.3102 0.4131 -0.0605 -0.0999 -0.0303 555  ASN B OD1 
12796 N ND2 . ASN B 557  ? 0.4598 0.3330 0.4153 -0.0671 -0.0913 -0.0232 555  ASN B ND2 
12797 N N   . GLU B 558  ? 0.4753 0.3011 0.4210 -0.0530 -0.1049 -0.0279 556  GLU B N   
12798 C CA  . GLU B 558  ? 0.4922 0.2992 0.4335 -0.0491 -0.1115 -0.0326 556  GLU B CA  
12799 C C   . GLU B 558  ? 0.4827 0.2842 0.4213 -0.0477 -0.1135 -0.0394 556  GLU B C   
12800 O O   . GLU B 558  ? 0.4787 0.2696 0.4148 -0.0405 -0.1159 -0.0462 556  GLU B O   
12801 C CB  . GLU B 558  ? 0.5038 0.2958 0.4408 -0.0556 -0.1190 -0.0266 556  GLU B CB  
12802 C CG  . GLU B 558  ? 0.5117 0.3042 0.4493 -0.0557 -0.1187 -0.0206 556  GLU B CG  
12803 C CD  . GLU B 558  ? 0.5071 0.2958 0.4458 -0.0455 -0.1185 -0.0252 556  GLU B CD  
12804 O OE1 . GLU B 558  ? 0.5096 0.2914 0.4479 -0.0382 -0.1199 -0.0329 556  GLU B OE1 
12805 O OE2 . GLU B 558  ? 0.5437 0.3366 0.4835 -0.0449 -0.1170 -0.0209 556  GLU B OE2 
12806 N N   . GLU B 559  ? 0.5035 0.3115 0.4421 -0.0544 -0.1127 -0.0378 557  GLU B N   
12807 C CA  . GLU B 559  ? 0.5028 0.3067 0.4384 -0.0530 -0.1144 -0.0444 557  GLU B CA  
12808 C C   . GLU B 559  ? 0.4802 0.2936 0.4181 -0.0435 -0.1080 -0.0515 557  GLU B C   
12809 O O   . GLU B 559  ? 0.4971 0.3021 0.4313 -0.0374 -0.1097 -0.0591 557  GLU B O   
12810 C CB  . GLU B 559  ? 0.5480 0.3596 0.4842 -0.0620 -0.1144 -0.0408 557  GLU B CB  
12811 C CG  . GLU B 559  ? 0.5633 0.3671 0.4977 -0.0727 -0.1208 -0.0337 557  GLU B CG  
12812 C CD  . GLU B 559  ? 0.6257 0.4413 0.5627 -0.0810 -0.1197 -0.0300 557  GLU B CD  
12813 O OE1 . GLU B 559  ? 0.7006 0.5291 0.6400 -0.0780 -0.1144 -0.0334 557  GLU B OE1 
12814 O OE2 . GLU B 559  ? 0.6181 0.4303 0.5549 -0.0905 -0.1242 -0.0235 557  GLU B OE2 
12815 N N   . THR B 560  ? 0.4257 0.2567 0.3693 -0.0424 -0.1007 -0.0491 558  THR B N   
12816 C CA  . THR B 560  ? 0.4542 0.2957 0.4009 -0.0342 -0.0943 -0.0546 558  THR B CA  
12817 C C   . THR B 560  ? 0.4638 0.2974 0.4103 -0.0252 -0.0950 -0.0594 558  THR B C   
12818 O O   . THR B 560  ? 0.4528 0.2861 0.3986 -0.0181 -0.0933 -0.0664 558  THR B O   
12819 C CB  . THR B 560  ? 0.4130 0.2732 0.3658 -0.0354 -0.0871 -0.0501 558  THR B CB  
12820 O OG1 . THR B 560  ? 0.4121 0.2802 0.3655 -0.0432 -0.0864 -0.0458 558  THR B OG1 
12821 C CG2 . THR B 560  ? 0.4258 0.2969 0.3819 -0.0277 -0.0807 -0.0553 558  THR B CG2 
12822 N N   . LEU B 561  ? 0.4448 0.2727 0.3922 -0.0252 -0.0974 -0.0556 559  LEU B N   
12823 C CA  . LEU B 561  ? 0.4782 0.2990 0.4263 -0.0165 -0.0986 -0.0598 559  LEU B CA  
12824 C C   . LEU B 561  ? 0.4734 0.2769 0.4157 -0.0130 -0.1045 -0.0660 559  LEU B C   
12825 O O   . LEU B 561  ? 0.4649 0.2666 0.4078 -0.0040 -0.1034 -0.0725 559  LEU B O   
12826 C CB  . LEU B 561  ? 0.4536 0.2705 0.4028 -0.0178 -0.1011 -0.0540 559  LEU B CB  
12827 C CG  . LEU B 561  ? 0.4078 0.2409 0.3623 -0.0193 -0.0951 -0.0490 559  LEU B CG  
12828 C CD1 . LEU B 561  ? 0.4118 0.2389 0.3656 -0.0214 -0.0986 -0.0430 559  LEU B CD1 
12829 C CD2 . LEU B 561  ? 0.3854 0.2299 0.3453 -0.0111 -0.0891 -0.0537 559  LEU B CD2 
12830 N N   . ALA B 562  ? 0.4705 0.2614 0.4073 -0.0197 -0.1110 -0.0640 560  ALA B N   
12831 C CA  . ALA B 562  ? 0.5051 0.2777 0.4354 -0.0165 -0.1173 -0.0700 560  ALA B CA  
12832 C C   . ALA B 562  ? 0.5155 0.2920 0.4436 -0.0119 -0.1143 -0.0779 560  ALA B C   
12833 O O   . ALA B 562  ? 0.5355 0.3035 0.4607 -0.0037 -0.1156 -0.0852 560  ALA B O   
12834 C CB  . ALA B 562  ? 0.4938 0.2519 0.4187 -0.0259 -0.1253 -0.0656 560  ALA B CB  
12835 N N   . SER B 563  ? 0.5076 0.2972 0.4370 -0.0167 -0.1101 -0.0764 561  SER B N   
12836 C CA  . SER B 563  ? 0.5233 0.3164 0.4497 -0.0127 -0.1074 -0.0835 561  SER B CA  
12837 C C   . SER B 563  ? 0.5069 0.3133 0.4383 -0.0036 -0.0997 -0.0875 561  SER B C   
12838 O O   . SER B 563  ? 0.4917 0.2966 0.4200 0.0033  -0.0982 -0.0949 561  SER B O   
12839 C CB  . SER B 563  ? 0.5047 0.3069 0.4306 -0.0209 -0.1062 -0.0804 561  SER B CB  
12840 O OG  . SER B 563  ? 0.5710 0.3925 0.5040 -0.0222 -0.0989 -0.0760 561  SER B OG  
12841 N N   . LEU B 564  ? 0.4611 0.2804 0.3999 -0.0035 -0.0948 -0.0827 562  LEU B N   
12842 C CA  . LEU B 564  ? 0.4966 0.3279 0.4409 0.0047  -0.0880 -0.0859 562  LEU B CA  
12843 C C   . LEU B 564  ? 0.5286 0.3500 0.4727 0.0137  -0.0903 -0.0911 562  LEU B C   
12844 O O   . LEU B 564  ? 0.5112 0.3377 0.4566 0.0217  -0.0862 -0.0970 562  LEU B O   
12845 C CB  . LEU B 564  ? 0.5034 0.3486 0.4550 0.0022  -0.0835 -0.0794 562  LEU B CB  
12846 C CG  . LEU B 564  ? 0.5640 0.4239 0.5223 0.0085  -0.0763 -0.0811 562  LEU B CG  
12847 C CD1 . LEU B 564  ? 0.5021 0.3705 0.4592 0.0104  -0.0717 -0.0854 562  LEU B CD1 
12848 C CD2 . LEU B 564  ? 0.5043 0.3759 0.4683 0.0046  -0.0730 -0.0743 562  LEU B CD2 
12849 N N   . THR B 565  ? 0.4723 0.2798 0.4148 0.0128  -0.0966 -0.0888 563  THR B N   
12850 C CA  . THR B 565  ? 0.5104 0.3068 0.4524 0.0214  -0.0997 -0.0937 563  THR B CA  
12851 C C   . THR B 565  ? 0.5684 0.3570 0.5043 0.0273  -0.1007 -0.1024 563  THR B C   
12852 O O   . THR B 565  ? 0.5710 0.3624 0.5090 0.0368  -0.0977 -0.1083 563  THR B O   
12853 C CB  . THR B 565  ? 0.5219 0.3016 0.4611 0.0180  -0.1078 -0.0896 563  THR B CB  
12854 O OG1 . THR B 565  ? 0.5019 0.2895 0.4465 0.0139  -0.1065 -0.0820 563  THR B OG1 
12855 C CG2 . THR B 565  ? 0.5692 0.3354 0.5071 0.0274  -0.1120 -0.0952 563  THR B CG2 
12856 N N   . GLU B 566  ? 0.5413 0.3204 0.4695 0.0216  -0.1049 -0.1033 564  GLU B N   
12857 C CA  . GLU B 566  ? 0.6078 0.3775 0.5285 0.0270  -0.1066 -0.1119 564  GLU B CA  
12858 C C   . GLU B 566  ? 0.5445 0.3302 0.4666 0.0314  -0.0985 -0.1162 564  GLU B C   
12859 O O   . GLU B 566  ? 0.5511 0.3347 0.4704 0.0402  -0.0969 -0.1238 564  GLU B O   
12860 C CB  . GLU B 566  ? 0.6461 0.4012 0.5581 0.0191  -0.1139 -0.1115 564  GLU B CB  
12861 C CG  . GLU B 566  ? 0.7077 0.4436 0.6168 0.0156  -0.1228 -0.1083 564  GLU B CG  
12862 C CD  . GLU B 566  ? 0.8027 0.5316 0.7136 0.0253  -0.1238 -0.1110 564  GLU B CD  
12863 O OE1 . GLU B 566  ? 0.8874 0.6156 0.7962 0.0343  -0.1216 -0.1179 564  GLU B OE1 
12864 O OE2 . GLU B 566  ? 0.8395 0.5638 0.7540 0.0240  -0.1269 -0.1061 564  GLU B OE2 
12865 N N   . ALA B 567  ? 0.5031 0.3047 0.4290 0.0255  -0.0934 -0.1115 565  ALA B N   
12866 C CA  . ALA B 567  ? 0.5455 0.3623 0.4727 0.0294  -0.0858 -0.1149 565  ALA B CA  
12867 C C   . ALA B 567  ? 0.5597 0.3871 0.4945 0.0383  -0.0798 -0.1169 565  ALA B C   
12868 O O   . ALA B 567  ? 0.4884 0.3228 0.4226 0.0449  -0.0748 -0.1223 565  ALA B O   
12869 C CB  . ALA B 567  ? 0.5221 0.3531 0.4522 0.0211  -0.0821 -0.1089 565  ALA B CB  
12870 N N   . LEU B 568  ? 0.4555 0.2848 0.3975 0.0385  -0.0802 -0.1123 566  LEU B N   
12871 C CA  . LEU B 568  ? 0.5037 0.3431 0.4536 0.0466  -0.0752 -0.1138 566  LEU B CA  
12872 C C   . LEU B 568  ? 0.5386 0.3679 0.4861 0.0565  -0.0774 -0.1212 566  LEU B C   
12873 O O   . LEU B 568  ? 0.4992 0.3380 0.4505 0.0644  -0.0719 -0.1256 566  LEU B O   
12874 C CB  . LEU B 568  ? 0.4673 0.3102 0.4247 0.0439  -0.0760 -0.1071 566  LEU B CB  
12875 C CG  . LEU B 568  ? 0.4956 0.3509 0.4570 0.0358  -0.0728 -0.0998 566  LEU B CG  
12876 C CD1 . LEU B 568  ? 0.4958 0.3515 0.4628 0.0342  -0.0746 -0.0941 566  LEU B CD1 
12877 C CD2 . LEU B 568  ? 0.4685 0.3419 0.4344 0.0375  -0.0646 -0.1006 566  LEU B CD2 
12878 N N   . ARG B 569  ? 0.5410 0.3509 0.4824 0.0563  -0.0853 -0.1227 567  ARG B N   
12879 C CA  . ARG B 569  ? 0.6019 0.4003 0.5399 0.0661  -0.0879 -0.1303 567  ARG B CA  
12880 C C   . ARG B 569  ? 0.5966 0.3969 0.5280 0.0708  -0.0844 -0.1379 567  ARG B C   
12881 O O   . ARG B 569  ? 0.6074 0.4113 0.5403 0.0809  -0.0808 -0.1440 567  ARG B O   
12882 C CB  . ARG B 569  ? 0.6327 0.4081 0.5638 0.0639  -0.0977 -0.1303 567  ARG B CB  
12883 C CG  . ARG B 569  ? 0.6719 0.4432 0.6081 0.0602  -0.1019 -0.1232 567  ARG B CG  
12884 C CD  . ARG B 569  ? 0.7420 0.4914 0.6716 0.0594  -0.1110 -0.1232 567  ARG B CD  
12885 N NE  . ARG B 569  ? 0.7958 0.5386 0.7282 0.0542  -0.1161 -0.1162 567  ARG B NE  
12886 C CZ  . ARG B 569  ? 0.8577 0.5850 0.7867 0.0529  -0.1232 -0.1134 567  ARG B CZ  
12887 N NH1 . ARG B 569  ? 0.8824 0.5988 0.8056 0.0566  -0.1262 -0.1172 567  ARG B NH1 
12888 N NH2 . ARG B 569  ? 0.8763 0.5989 0.8076 0.0478  -0.1274 -0.1065 567  ARG B NH2 
12889 N N   . GLU B 570  ? 0.5603 0.3584 0.4843 0.0637  -0.0854 -0.1376 568  GLU B N   
12890 C CA  . GLU B 570  ? 0.6023 0.4019 0.5188 0.0675  -0.0825 -0.1445 568  GLU B CA  
12891 C C   . GLU B 570  ? 0.5673 0.3881 0.4903 0.0724  -0.0725 -0.1454 568  GLU B C   
12892 O O   . GLU B 570  ? 0.5771 0.4004 0.4969 0.0807  -0.0689 -0.1522 568  GLU B O   
12893 C CB  . GLU B 570  ? 0.5862 0.3817 0.4949 0.0577  -0.0855 -0.1426 568  GLU B CB  
12894 C CG  . GLU B 570  ? 0.6868 0.4634 0.5891 0.0521  -0.0943 -0.1408 568  GLU B CG  
12895 C CD  . GLU B 570  ? 0.7597 0.5340 0.6567 0.0412  -0.0978 -0.1376 568  GLU B CD  
12896 O OE1 . GLU B 570  ? 0.8290 0.6177 0.7280 0.0378  -0.0928 -0.1359 568  GLU B OE1 
12897 O OE2 . GLU B 570  ? 0.8517 0.6120 0.7438 0.0356  -0.1047 -0.1354 568  GLU B OE2 
12898 N N   . SER B 571  ? 0.5554 0.3918 0.4873 0.0674  -0.0681 -0.1384 569  SER B N   
12899 C CA  . SER B 571  ? 0.5506 0.4070 0.4890 0.0709  -0.0590 -0.1383 569  SER B CA  
12900 C C   . SER B 571  ? 0.5856 0.4466 0.5307 0.0815  -0.0559 -0.1421 569  SER B C   
12901 O O   . SER B 571  ? 0.5603 0.4338 0.5074 0.0874  -0.0490 -0.1454 569  SER B O   
12902 C CB  . SER B 571  ? 0.5363 0.4063 0.4831 0.0634  -0.0560 -0.1299 569  SER B CB  
12903 O OG  . SER B 571  ? 0.5626 0.4350 0.5186 0.0653  -0.0564 -0.1265 569  SER B OG  
12904 N N   . ALA B 572  ? 0.5253 0.3770 0.4742 0.0840  -0.0608 -0.1413 570  ALA B N   
12905 C CA  . ALA B 572  ? 0.5413 0.3971 0.4973 0.0943  -0.0586 -0.1446 570  ALA B CA  
12906 C C   . ALA B 572  ? 0.6171 0.4655 0.5660 0.1037  -0.0584 -0.1535 570  ALA B C   
12907 O O   . ALA B 572  ? 0.5940 0.4522 0.5491 0.1121  -0.0535 -0.1558 570  ALA B O   
12908 C CB  . ALA B 572  ? 0.5489 0.3954 0.5099 0.0942  -0.0647 -0.1411 570  ALA B CB  
12909 N N   . ALA B 573  ? 0.5654 0.4003 0.5027 0.1004  -0.0625 -0.1554 571  ALA B N   
12910 C CA  . ALA B 573  ? 0.6285 0.4584 0.5587 0.1068  -0.0616 -0.1609 571  ALA B CA  
12911 C C   . ALA B 573  ? 0.6091 0.4501 0.5343 0.1081  -0.0547 -0.1643 571  ALA B C   
12912 O O   . ALA B 573  ? 0.5877 0.4262 0.5068 0.1138  -0.0529 -0.1691 571  ALA B O   
12913 C CB  . ALA B 573  ? 0.5991 0.4077 0.5193 0.1029  -0.0703 -0.1613 571  ALA B CB  
12914 N N   . MET B 574  ? 0.5784 0.4314 0.5055 0.1031  -0.0507 -0.1620 572  MET B N   
12915 C CA  . MET B 574  ? 0.5737 0.4374 0.4956 0.1040  -0.0442 -0.1647 572  MET B CA  
12916 C C   . MET B 574  ? 0.5695 0.4511 0.4995 0.1123  -0.0353 -0.1661 572  MET B C   
12917 O O   . MET B 574  ? 0.5198 0.4091 0.4614 0.1155  -0.0337 -0.1640 572  MET B O   
12918 C CB  . MET B 574  ? 0.5406 0.4103 0.4612 0.0953  -0.0436 -0.1614 572  MET B CB  
12919 C CG  . MET B 574  ? 0.5714 0.4251 0.4843 0.0864  -0.0521 -0.1595 572  MET B CG  
12920 S SD  . MET B 574  ? 0.6983 0.5637 0.6147 0.0738  -0.0504 -0.1504 572  MET B SD  
12921 C CE  . MET B 574  ? 0.6547 0.5000 0.5630 0.0647  -0.0610 -0.1486 572  MET B CE  
12922 N N   . LYS B 575  ? 0.4846 0.3730 0.4084 0.1155  -0.0297 -0.1695 573  LYS B N   
12923 C CA  . LYS B 575  ? 0.4953 0.4023 0.4266 0.1223  -0.0207 -0.1701 573  LYS B CA  
12924 C C   . LYS B 575  ? 0.4682 0.3918 0.4043 0.1177  -0.0151 -0.1665 573  LYS B C   
12925 O O   . LYS B 575  ? 0.4758 0.4029 0.4039 0.1146  -0.0125 -0.1671 573  LYS B O   
12926 C CB  . LYS B 575  ? 0.4822 0.3891 0.4045 0.1282  -0.0169 -0.1752 573  LYS B CB  
12927 C CG  . LYS B 575  ? 0.5433 0.4693 0.4737 0.1353  -0.0075 -0.1754 573  LYS B CG  
12928 C CD  . LYS B 575  ? 0.5520 0.4778 0.4727 0.1407  -0.0036 -0.1804 573  LYS B CD  
12929 C CE  . LYS B 575  ? 0.6205 0.5643 0.5497 0.1482  0.0053  -0.1805 573  LYS B CE  
12930 N NZ  . LYS B 575  ? 0.6284 0.5711 0.5471 0.1535  0.0090  -0.1855 573  LYS B NZ  
12931 N N   . TRP B 576  ? 0.4647 0.3984 0.4138 0.1174  -0.0135 -0.1626 574  TRP B N   
12932 C CA  . TRP B 576  ? 0.4179 0.3685 0.3738 0.1115  -0.0080 -0.1566 574  TRP B CA  
12933 C C   . TRP B 576  ? 0.4306 0.4002 0.3929 0.1180  0.0012  -0.1576 574  TRP B C   
12934 O O   . TRP B 576  ? 0.4122 0.3873 0.3835 0.1249  0.0032  -0.1587 574  TRP B O   
12935 C CB  . TRP B 576  ? 0.4019 0.3545 0.3689 0.1054  -0.0108 -0.1491 574  TRP B CB  
12936 C CG  . TRP B 576  ? 0.4489 0.3849 0.4101 0.0982  -0.0192 -0.1470 574  TRP B CG  
12937 C CD1 . TRP B 576  ? 0.4937 0.4153 0.4555 0.0992  -0.0263 -0.1476 574  TRP B CD1 
12938 C CD2 . TRP B 576  ? 0.4525 0.3849 0.4069 0.0890  -0.0215 -0.1437 574  TRP B CD2 
12939 N NE1 . TRP B 576  ? 0.5081 0.4176 0.4637 0.0907  -0.0326 -0.1446 574  TRP B NE1 
12940 C CE2 . TRP B 576  ? 0.4969 0.4132 0.4482 0.0844  -0.0297 -0.1422 574  TRP B CE2 
12941 C CE3 . TRP B 576  ? 0.4626 0.4040 0.4132 0.0841  -0.0174 -0.1416 574  TRP B CE3 
12942 C CZ2 . TRP B 576  ? 0.5387 0.4489 0.4842 0.0752  -0.0337 -0.1388 574  TRP B CZ2 
12943 C CZ3 . TRP B 576  ? 0.4791 0.4140 0.4238 0.0753  -0.0217 -0.1383 574  TRP B CZ3 
12944 C CH2 . TRP B 576  ? 0.5218 0.4417 0.4643 0.0709  -0.0296 -0.1369 574  TRP B CH2 
12945 N N   . THR B 577  ? 0.4084 0.3883 0.3665 0.1150  0.0067  -0.1563 575  THR B N   
12946 C CA  . THR B 577  ? 0.3809 0.3793 0.3439 0.1200  0.0158  -0.1566 575  THR B CA  
12947 C C   . THR B 577  ? 0.3973 0.4094 0.3646 0.1120  0.0202  -0.1492 575  THR B C   
12948 O O   . THR B 577  ? 0.3797 0.3864 0.3425 0.1036  0.0167  -0.1455 575  THR B O   
12949 C CB  . THR B 577  ? 0.3923 0.3889 0.3437 0.1243  0.0191  -0.1609 575  THR B CB  
12950 O OG1 . THR B 577  ? 0.4536 0.4427 0.3918 0.1186  0.0167  -0.1617 575  THR B OG1 
12951 C CG2 . THR B 577  ? 0.4617 0.4446 0.4094 0.1306  0.0151  -0.1656 575  THR B CG2 
12952 N N   . ALA B 578  ? 0.3421 0.3724 0.3182 0.1147  0.0278  -0.1470 576  ALA B N   
12953 C CA  . ALA B 578  ? 0.3318 0.3756 0.3114 0.1080  0.0326  -0.1404 576  ALA B CA  
12954 C C   . ALA B 578  ? 0.3518 0.4113 0.3321 0.1138  0.0415  -0.1421 576  ALA B C   
12955 O O   . ALA B 578  ? 0.4121 0.4801 0.4012 0.1207  0.0450  -0.1438 576  ALA B O   
12956 C CB  . ALA B 578  ? 0.2970 0.3475 0.2908 0.1025  0.0317  -0.1330 576  ALA B CB  
12957 N N   . LEU B 579  ? 0.3507 0.4138 0.3213 0.1111  0.0449  -0.1416 577  LEU B N   
12958 C CA  . LEU B 579  ? 0.3467 0.4225 0.3146 0.1154  0.0530  -0.1425 577  LEU B CA  
12959 C C   . LEU B 579  ? 0.3148 0.4048 0.2858 0.1091  0.0581  -0.1359 577  LEU B C   
12960 O O   . LEU B 579  ? 0.3127 0.3980 0.2826 0.1007  0.0543  -0.1310 577  LEU B O   
12961 C CB  . LEU B 579  ? 0.3459 0.4102 0.2965 0.1176  0.0519  -0.1476 577  LEU B CB  
12962 C CG  . LEU B 579  ? 0.4081 0.4541 0.3528 0.1219  0.0452  -0.1538 577  LEU B CG  
12963 C CD1 . LEU B 579  ? 0.4334 0.4690 0.3611 0.1233  0.0442  -0.1585 577  LEU B CD1 
12964 C CD2 . LEU B 579  ? 0.3891 0.4392 0.3445 0.1290  0.0470  -0.1548 577  LEU B CD2 
12965 N N   . PRO B 580  ? 0.3224 0.4280 0.2972 0.1113  0.0660  -0.1334 578  PRO B N   
12966 C CA  . PRO B 580  ? 0.3080 0.4252 0.2815 0.1056  0.0708  -0.1280 578  PRO B CA  
12967 C C   . PRO B 580  ? 0.3185 0.4269 0.2742 0.1036  0.0694  -0.1304 578  PRO B C   
12968 O O   . PRO B 580  ? 0.3676 0.4759 0.3138 0.1072  0.0728  -0.1326 578  PRO B O   
12969 C CB  . PRO B 580  ? 0.3177 0.4513 0.2986 0.1087  0.0791  -0.1246 578  PRO B CB  
12970 C CG  . PRO B 580  ? 0.3354 0.4674 0.3244 0.1157  0.0784  -0.1281 578  PRO B CG  
12971 C CD  . PRO B 580  ? 0.3407 0.4530 0.3200 0.1183  0.0708  -0.1348 578  PRO B CD  
12972 N N   . GLN B 581  ? 0.3452 0.4438 0.2967 0.0964  0.0634  -0.1279 579  GLN B N   
12973 C CA  . GLN B 581  ? 0.3871 0.4769 0.3226 0.0935  0.0608  -0.1297 579  GLN B CA  
12974 C C   . GLN B 581  ? 0.3279 0.4292 0.2616 0.0884  0.0656  -0.1233 579  GLN B C   
12975 O O   . GLN B 581  ? 0.3502 0.4519 0.2882 0.0808  0.0633  -0.1168 579  GLN B O   
12976 C CB  . GLN B 581  ? 0.3657 0.4397 0.2988 0.0878  0.0517  -0.1293 579  GLN B CB  
12977 C CG  . GLN B 581  ? 0.4163 0.4774 0.3497 0.0924  0.0463  -0.1353 579  GLN B CG  
12978 C CD  . GLN B 581  ? 0.4828 0.5339 0.4013 0.0987  0.0451  -0.1442 579  GLN B CD  
12979 O OE1 . GLN B 581  ? 0.4603 0.5139 0.3672 0.0995  0.0481  -0.1460 579  GLN B OE1 
12980 N NE2 . GLN B 581  ? 0.5075 0.5462 0.4256 0.1032  0.0402  -0.1497 579  GLN B NE2 
12981 N N   . LEU B 582  ? 0.3349 0.4456 0.2621 0.0928  0.0724  -0.1251 580  LEU B N   
12982 C CA  . LEU B 582  ? 0.3301 0.4504 0.2531 0.0882  0.0768  -0.1194 580  LEU B CA  
12983 C C   . LEU B 582  ? 0.4153 0.5247 0.3208 0.0858  0.0726  -0.1220 580  LEU B C   
12984 O O   . LEU B 582  ? 0.4135 0.5089 0.3100 0.0883  0.0671  -0.1286 580  LEU B O   
12985 C CB  . LEU B 582  ? 0.3811 0.5151 0.3064 0.0919  0.0855  -0.1173 580  LEU B CB  
12986 C CG  . LEU B 582  ? 0.4125 0.5617 0.3561 0.0915  0.0905  -0.1116 580  LEU B CG  
12987 C CD1 . LEU B 582  ? 0.3767 0.5225 0.3318 0.0956  0.0876  -0.1150 580  LEU B CD1 
12988 C CD2 . LEU B 582  ? 0.4565 0.6189 0.4011 0.0935  0.0988  -0.1083 580  LEU B CD2 
12989 N N   . ALA B 583  ? 0.3839 0.4994 0.2849 0.0806  0.0748  -0.1162 581  ALA B N   
12990 C CA  . ALA B 583  ? 0.4651 0.5718 0.3499 0.0782  0.0708  -0.1181 581  ALA B CA  
12991 C C   . ALA B 583  ? 0.4849 0.5849 0.3556 0.0846  0.0715  -0.1256 581  ALA B C   
12992 O O   . ALA B 583  ? 0.5558 0.6420 0.4147 0.0843  0.0652  -0.1306 581  ALA B O   
12993 C CB  . ALA B 583  ? 0.4434 0.5596 0.3258 0.0727  0.0742  -0.1104 581  ALA B CB  
12994 N N   . THR B 584  ? 0.4540 0.5622 0.3272 0.0894  0.0784  -0.1254 582  THR B N   
12995 C CA  . THR B 584  ? 0.4446 0.5462 0.3057 0.0948  0.0795  -0.1312 582  THR B CA  
12996 C C   . THR B 584  ? 0.4621 0.5517 0.3244 0.1004  0.0754  -0.1385 582  THR B C   
12997 O O   . THR B 584  ? 0.4537 0.5374 0.3070 0.1055  0.0763  -0.1438 582  THR B O   
12998 C CB  . THR B 584  ? 0.4650 0.5808 0.3287 0.0978  0.0888  -0.1280 582  THR B CB  
12999 O OG1 . THR B 584  ? 0.5168 0.6437 0.3984 0.0990  0.0927  -0.1246 582  THR B OG1 
13000 C CG2 . THR B 584  ? 0.5219 0.6466 0.3798 0.0927  0.0923  -0.1216 582  THR B CG2 
13001 N N   . GLY B 585  ? 0.4434 0.5291 0.3165 0.0995  0.0710  -0.1388 583  GLY B N   
13002 C CA  . GLY B 585  ? 0.4350 0.5086 0.3093 0.1044  0.0666  -0.1451 583  GLY B CA  
13003 C C   . GLY B 585  ? 0.4552 0.5373 0.3467 0.1077  0.0697  -0.1434 583  GLY B C   
13004 O O   . GLY B 585  ? 0.4177 0.5154 0.3201 0.1059  0.0754  -0.1374 583  GLY B O   
13005 N N   . PRO B 586  ? 0.4511 0.5229 0.3454 0.1122  0.0657  -0.1484 584  PRO B N   
13006 C CA  . PRO B 586  ? 0.4331 0.5124 0.3441 0.1153  0.0677  -0.1468 584  PRO B CA  
13007 C C   . PRO B 586  ? 0.4270 0.5204 0.3435 0.1206  0.0763  -0.1455 584  PRO B C   
13008 O O   . PRO B 586  ? 0.4238 0.5150 0.3307 0.1251  0.0790  -0.1494 584  PRO B O   
13009 C CB  . PRO B 586  ? 0.4337 0.4961 0.3433 0.1189  0.0604  -0.1529 584  PRO B CB  
13010 C CG  . PRO B 586  ? 0.4852 0.5337 0.3768 0.1200  0.0572  -0.1584 584  PRO B CG  
13011 C CD  . PRO B 586  ? 0.4124 0.4646 0.2956 0.1136  0.0580  -0.1551 584  PRO B CD  
13012 N N   . ALA B 587  ? 0.3969 0.5051 0.3292 0.1196  0.0805  -0.1401 585  ALA B N   
13013 C CA  . ALA B 587  ? 0.4091 0.5327 0.3497 0.1236  0.0887  -0.1377 585  ALA B CA  
13014 C C   . ALA B 587  ? 0.3845 0.5070 0.3354 0.1302  0.0878  -0.1408 585  ALA B C   
13015 O O   . ALA B 587  ? 0.4086 0.5233 0.3659 0.1300  0.0818  -0.1420 585  ALA B O   
13016 C CB  . ALA B 587  ? 0.3618 0.5026 0.3144 0.1181  0.0935  -0.1292 585  ALA B CB  
13017 N N   . ALA B 588  ? 0.3835 0.5141 0.3361 0.1361  0.0939  -0.1419 586  ALA B N   
13018 C CA  . ALA B 588  ? 0.4109 0.5435 0.3747 0.1427  0.0941  -0.1441 586  ALA B CA  
13019 C C   . ALA B 588  ? 0.4162 0.5635 0.3994 0.1400  0.0962  -0.1375 586  ALA B C   
13020 O O   . ALA B 588  ? 0.4143 0.5730 0.4022 0.1338  0.0995  -0.1311 586  ALA B O   
13021 C CB  . ALA B 588  ? 0.4447 0.5829 0.4049 0.1498  0.1006  -0.1471 586  ALA B CB  
13022 N N   . GLY B 589  ? 0.3937 0.5404 0.3883 0.1445  0.0939  -0.1390 587  GLY B N   
13023 C CA  . GLY B 589  ? 0.4370 0.5971 0.4503 0.1423  0.0951  -0.1332 587  GLY B CA  
13024 C C   . GLY B 589  ? 0.4478 0.6039 0.4710 0.1481  0.0912  -0.1360 587  GLY B C   
13025 O O   . GLY B 589  ? 0.4361 0.5803 0.4520 0.1544  0.0885  -0.1423 587  GLY B O   
13026 N N   . GLU B 590  ? 0.4294 0.5954 0.4694 0.1458  0.0906  -0.1312 588  GLU B N   
13027 C CA  . GLU B 590  ? 0.3988 0.5626 0.4499 0.1509  0.0868  -0.1328 588  GLU B CA  
13028 C C   . GLU B 590  ? 0.4049 0.5502 0.4515 0.1496  0.0773  -0.1360 588  GLU B C   
13029 O O   . GLU B 590  ? 0.3648 0.5072 0.4105 0.1427  0.0741  -0.1335 588  GLU B O   
13030 C CB  . GLU B 590  ? 0.3814 0.5629 0.4521 0.1485  0.0894  -0.1262 588  GLU B CB  
13031 N N   . THR B 591  ? 0.4447 0.5775 0.4886 0.1560  0.0727  -0.1414 589  THR B N   
13032 C CA  . THR B 591  ? 0.4610 0.5743 0.4986 0.1550  0.0635  -0.1449 589  THR B CA  
13033 C C   . THR B 591  ? 0.4703 0.5820 0.5209 0.1578  0.0585  -0.1442 589  THR B C   
13034 O O   . THR B 591  ? 0.4409 0.5599 0.5003 0.1640  0.0608  -0.1446 589  THR B O   
13035 C CB  . THR B 591  ? 0.4967 0.5931 0.5177 0.1595  0.0611  -0.1518 589  THR B CB  
13036 O OG1 . THR B 591  ? 0.4772 0.5744 0.4854 0.1564  0.0651  -0.1522 589  THR B OG1 
13037 C CG2 . THR B 591  ? 0.4721 0.5475 0.4866 0.1580  0.0512  -0.1549 589  THR B CG2 
13038 N N   . ARG B 592  ? 0.4311 0.5335 0.4831 0.1531  0.0515  -0.1431 590  ARG B N   
13039 C CA  . ARG B 592  ? 0.4194 0.5178 0.4820 0.1554  0.0456  -0.1427 590  ARG B CA  
13040 C C   . ARG B 592  ? 0.4384 0.5166 0.4930 0.1523  0.0365  -0.1449 590  ARG B C   
13041 O O   . ARG B 592  ? 0.4427 0.5130 0.4863 0.1471  0.0352  -0.1456 590  ARG B O   
13042 C CB  . ARG B 592  ? 0.4860 0.6016 0.5660 0.1519  0.0475  -0.1364 590  ARG B CB  
13043 C CG  . ARG B 592  ? 0.4559 0.5738 0.5361 0.1432  0.0468  -0.1326 590  ARG B CG  
13044 C CD  . ARG B 592  ? 0.5475 0.6759 0.6445 0.1400  0.0451  -0.1274 590  ARG B CD  
13045 N NE  . ARG B 592  ? 0.4977 0.6276 0.5945 0.1310  0.0444  -0.1232 590  ARG B NE  
13046 C CZ  . ARG B 592  ? 0.5511 0.6655 0.6418 0.1246  0.0374  -0.1214 590  ARG B CZ  
13047 N NH1 . ARG B 592  ? 0.4907 0.5886 0.5767 0.1275  0.0305  -0.1250 590  ARG B NH1 
13048 N NH2 . ARG B 592  ? 0.4833 0.5987 0.5726 0.1151  0.0374  -0.1157 590  ARG B NH2 
13049 N N   . THR B 593  ? 0.4487 0.5187 0.5092 0.1553  0.0302  -0.1455 591  THR B N   
13050 C CA  . THR B 593  ? 0.4480 0.4986 0.5016 0.1522  0.0214  -0.1470 591  THR B CA  
13051 C C   . THR B 593  ? 0.4263 0.4803 0.4872 0.1449  0.0188  -0.1424 591  THR B C   
13052 O O   . THR B 593  ? 0.4276 0.4971 0.5023 0.1439  0.0215  -0.1382 591  THR B O   
13053 C CB  . THR B 593  ? 0.4662 0.5048 0.5217 0.1582  0.0151  -0.1494 591  THR B CB  
13054 O OG1 . THR B 593  ? 0.4872 0.5381 0.5593 0.1603  0.0153  -0.1458 591  THR B OG1 
13055 C CG2 . THR B 593  ? 0.4857 0.5199 0.5335 0.1655  0.0175  -0.1544 591  THR B CG2 
13056 N N   . VAL B 594  ? 0.4188 0.4579 0.4697 0.1390  0.0135  -0.1425 592  VAL B N   
13057 C CA  . VAL B 594  ? 0.3898 0.4270 0.4442 0.1291  0.0096  -0.1354 592  VAL B CA  
13058 C C   . VAL B 594  ? 0.4320 0.4539 0.4870 0.1299  0.0009  -0.1356 592  VAL B C   
13059 O O   . VAL B 594  ? 0.3860 0.3913 0.4311 0.1329  -0.0037 -0.1403 592  VAL B O   
13060 C CB  . VAL B 594  ? 0.4129 0.4443 0.4557 0.1203  0.0096  -0.1334 592  VAL B CB  
13061 C CG1 . VAL B 594  ? 0.3233 0.3541 0.3699 0.1106  0.0063  -0.1261 592  VAL B CG1 
13062 C CG2 . VAL B 594  ? 0.3866 0.4319 0.4273 0.1205  0.0179  -0.1338 592  VAL B CG2 
13063 N N   . LEU B 595  ? 0.4328 0.4598 0.4992 0.1275  -0.0015 -0.1305 593  LEU B N   
13064 C CA  . LEU B 595  ? 0.4174 0.4317 0.4857 0.1290  -0.0094 -0.1303 593  LEU B CA  
13065 C C   . LEU B 595  ? 0.3776 0.3843 0.4437 0.1190  -0.0145 -0.1242 593  LEU B C   
13066 O O   . LEU B 595  ? 0.4116 0.4271 0.4797 0.1118  -0.0115 -0.1194 593  LEU B O   
13067 C CB  . LEU B 595  ? 0.4286 0.4540 0.5119 0.1357  -0.0091 -0.1298 593  LEU B CB  
13068 C CG  . LEU B 595  ? 0.4162 0.4510 0.5044 0.1469  -0.0041 -0.1355 593  LEU B CG  
13069 C CD1 . LEU B 595  ? 0.4762 0.5206 0.5802 0.1524  -0.0055 -0.1341 593  LEU B CD1 
13070 C CD2 . LEU B 595  ? 0.4490 0.4671 0.5244 0.1524  -0.0068 -0.1418 593  LEU B CD2 
13071 N N   . ASN B 596  ? 0.3957 0.3855 0.4569 0.1187  -0.0222 -0.1244 594  ASN B N   
13072 C CA  . ASN B 596  ? 0.3769 0.3586 0.4360 0.1100  -0.0275 -0.1187 594  ASN B CA  
13073 C C   . ASN B 596  ? 0.3572 0.3491 0.4290 0.1091  -0.0283 -0.1139 594  ASN B C   
13074 O O   . ASN B 596  ? 0.3531 0.3453 0.4322 0.1157  -0.0309 -0.1152 594  ASN B O   
13075 C CB  . ASN B 596  ? 0.3966 0.3575 0.4470 0.1109  -0.0355 -0.1206 594  ASN B CB  
13076 C CG  . ASN B 596  ? 0.4149 0.3660 0.4601 0.1016  -0.0405 -0.1151 594  ASN B CG  
13077 O OD1 . ASN B 596  ? 0.3665 0.3251 0.4173 0.0963  -0.0402 -0.1096 594  ASN B OD1 
13078 N ND2 . ASN B 596  ? 0.4346 0.3686 0.4684 0.0994  -0.0454 -0.1167 594  ASN B ND2 
13079 N N   . PRO B 597  ? 0.3531 0.3533 0.4279 0.1015  -0.0264 -0.1084 595  PRO B N   
13080 C CA  . PRO B 597  ? 0.3528 0.3619 0.4392 0.1005  -0.0277 -0.1041 595  PRO B CA  
13081 C C   . PRO B 597  ? 0.3685 0.3654 0.4546 0.1005  -0.0358 -0.1022 595  PRO B C   
13082 O O   . PRO B 597  ? 0.3356 0.3387 0.4318 0.1026  -0.0378 -0.1002 595  PRO B O   
13083 C CB  . PRO B 597  ? 0.3267 0.3432 0.4128 0.0917  -0.0246 -0.0991 595  PRO B CB  
13084 C CG  . PRO B 597  ? 0.3474 0.3556 0.4209 0.0873  -0.0236 -0.1001 595  PRO B CG  
13085 C CD  . PRO B 597  ? 0.3089 0.3111 0.3768 0.0940  -0.0228 -0.1063 595  PRO B CD  
13086 N N   . GLY B 598  ? 0.3705 0.3503 0.4454 0.0980  -0.0407 -0.1026 596  GLY B N   
13087 C CA  . GLY B 598  ? 0.3683 0.3355 0.4420 0.0981  -0.0486 -0.1007 596  GLY B CA  
13088 C C   . GLY B 598  ? 0.4257 0.3855 0.5012 0.1074  -0.0522 -0.1051 596  GLY B C   
13089 O O   . GLY B 598  ? 0.4600 0.4104 0.5361 0.1085  -0.0589 -0.1034 596  GLY B O   
13090 N N   . ASP B 599  ? 0.3883 0.3523 0.4645 0.1143  -0.0479 -0.1108 597  ASP B N   
13091 C CA  . ASP B 599  ? 0.4358 0.3923 0.5129 0.1241  -0.0509 -0.1160 597  ASP B CA  
13092 C C   . ASP B 599  ? 0.4375 0.4041 0.5164 0.1311  -0.0438 -0.1218 597  ASP B C   
13093 O O   . ASP B 599  ? 0.4230 0.3830 0.4916 0.1308  -0.0419 -0.1255 597  ASP B O   
13094 C CB  . ASP B 599  ? 0.4751 0.4091 0.5395 0.1230  -0.0577 -0.1174 597  ASP B CB  
13095 C CG  . ASP B 599  ? 0.5371 0.4610 0.6025 0.1330  -0.0625 -0.1221 597  ASP B CG  
13096 O OD1 . ASP B 599  ? 0.5065 0.4414 0.5812 0.1419  -0.0591 -0.1257 597  ASP B OD1 
13097 O OD2 . ASP B 599  ? 0.5467 0.4514 0.6036 0.1320  -0.0696 -0.1220 597  ASP B OD2 
13098 N N   . HIS B 600  ? 0.4252 0.4081 0.5172 0.1373  -0.0400 -0.1225 598  HIS B N   
13099 C CA  . HIS B 600  ? 0.4305 0.4261 0.5252 0.1435  -0.0322 -0.1273 598  HIS B CA  
13100 C C   . HIS B 600  ? 0.4395 0.4240 0.5272 0.1527  -0.0332 -0.1348 598  HIS B C   
13101 O O   . HIS B 600  ? 0.4425 0.4350 0.5281 0.1564  -0.0265 -0.1384 598  HIS B O   
13102 C CB  . HIS B 600  ? 0.4294 0.4460 0.5410 0.1475  -0.0282 -0.1255 598  HIS B CB  
13103 C CG  . HIS B 600  ? 0.4162 0.4463 0.5338 0.1387  -0.0249 -0.1193 598  HIS B CG  
13104 N ND1 . HIS B 600  ? 0.3763 0.4262 0.5086 0.1400  -0.0209 -0.1168 598  HIS B ND1 
13105 C CD2 . HIS B 600  ? 0.3567 0.3829 0.4674 0.1284  -0.0253 -0.1150 598  HIS B CD2 
13106 C CE1 . HIS B 600  ? 0.3776 0.4342 0.5113 0.1308  -0.0192 -0.1115 598  HIS B CE1 
13107 N NE2 . HIS B 600  ? 0.4181 0.4607 0.5389 0.1240  -0.0217 -0.1104 598  HIS B NE2 
13108 N N   . ARG B 601  ? 0.4695 0.4356 0.5520 0.1551  -0.0411 -0.1360 599  ARG B N   
13109 C CA  . ARG B 601  ? 0.4741 0.4276 0.5463 0.1598  -0.0423 -0.1405 599  ARG B CA  
13110 C C   . ARG B 601  ? 0.4291 0.3713 0.4863 0.1551  -0.0417 -0.1432 599  ARG B C   
13111 O O   . ARG B 601  ? 0.4789 0.4143 0.5274 0.1588  -0.0406 -0.1475 599  ARG B O   
13112 C CB  . ARG B 601  ? 0.5146 0.4512 0.5851 0.1622  -0.0513 -0.1398 599  ARG B CB  
13113 C CG  . ARG B 601  ? 0.5156 0.4616 0.6003 0.1668  -0.0531 -0.1369 599  ARG B CG  
13114 C CD  . ARG B 601  ? 0.5706 0.4984 0.6524 0.1669  -0.0631 -0.1349 599  ARG B CD  
13115 N NE  . ARG B 601  ? 0.5597 0.4762 0.6360 0.1584  -0.0685 -0.1312 599  ARG B NE  
13116 C CZ  . ARG B 601  ? 0.5811 0.4807 0.6530 0.1562  -0.0773 -0.1284 599  ARG B CZ  
13117 N NH1 . ARG B 601  ? 0.5783 0.4694 0.6505 0.1619  -0.0822 -0.1289 599  ARG B NH1 
13118 N NH2 . ARG B 601  ? 0.5789 0.4701 0.6456 0.1477  -0.0811 -0.1244 599  ARG B NH2 
13119 N N   . ASP B 602  ? 0.4784 0.4186 0.5323 0.1467  -0.0426 -0.1404 600  ASP B N   
13120 C CA  . ASP B 602  ? 0.4701 0.4003 0.5100 0.1404  -0.0426 -0.1415 600  ASP B CA  
13121 C C   . ASP B 602  ? 0.4592 0.4059 0.4995 0.1403  -0.0333 -0.1431 600  ASP B C   
13122 O O   . ASP B 602  ? 0.4704 0.4310 0.5162 0.1339  -0.0290 -0.1380 600  ASP B O   
13123 C CB  . ASP B 602  ? 0.4901 0.4132 0.5262 0.1288  -0.0470 -0.1347 600  ASP B CB  
13124 C CG  . ASP B 602  ? 0.5053 0.4185 0.5280 0.1218  -0.0476 -0.1353 600  ASP B CG  
13125 O OD1 . ASP B 602  ? 0.5209 0.4260 0.5349 0.1262  -0.0474 -0.1416 600  ASP B OD1 
13126 O OD2 . ASP B 602  ? 0.5274 0.4412 0.5483 0.1121  -0.0482 -0.1296 600  ASP B OD2 
13127 N N   . VAL B 603  ? 0.4610 0.4063 0.4947 0.1460  -0.0301 -0.1488 601  VAL B N   
13128 C CA  . VAL B 603  ? 0.4205 0.3794 0.4520 0.1460  -0.0216 -0.1504 601  VAL B CA  
13129 C C   . VAL B 603  ? 0.4697 0.4197 0.4888 0.1385  -0.0228 -0.1510 601  VAL B C   
13130 O O   . VAL B 603  ? 0.5125 0.4453 0.5194 0.1374  -0.0275 -0.1537 601  VAL B O   
13131 C CB  . VAL B 603  ? 0.4520 0.4130 0.4803 0.1539  -0.0176 -0.1548 601  VAL B CB  
13132 C CG1 . VAL B 603  ? 0.4622 0.4355 0.4862 0.1532  -0.0092 -0.1563 601  VAL B CG1 
13133 C CG2 . VAL B 603  ? 0.4548 0.4266 0.4968 0.1612  -0.0161 -0.1539 601  VAL B CG2 
13134 N N   . VAL B 604  ? 0.4085 0.3711 0.4303 0.1307  -0.0183 -0.1457 602  VAL B N   
13135 C CA  . VAL B 604  ? 0.4165 0.3726 0.4279 0.1215  -0.0194 -0.1435 602  VAL B CA  
13136 C C   . VAL B 604  ? 0.4340 0.3934 0.4364 0.1235  -0.0142 -0.1483 602  VAL B C   
13137 O O   . VAL B 604  ? 0.4767 0.4243 0.4669 0.1197  -0.0171 -0.1501 602  VAL B O   
13138 C CB  . VAL B 604  ? 0.4297 0.3966 0.4479 0.1122  -0.0177 -0.1354 602  VAL B CB  
13139 C CG1 . VAL B 604  ? 0.3882 0.3481 0.3964 0.1030  -0.0195 -0.1330 602  VAL B CG1 
13140 C CG2 . VAL B 604  ? 0.4180 0.3828 0.4452 0.1108  -0.0226 -0.1309 602  VAL B CG2 
13141 N N   . GLY B 605  ? 0.4023 0.3781 0.4104 0.1294  -0.0065 -0.1501 603  GLY B N   
13142 C CA  . GLY B 605  ? 0.4333 0.4130 0.4324 0.1320  -0.0011 -0.1547 603  GLY B CA  
13143 C C   . GLY B 605  ? 0.4432 0.4428 0.4508 0.1372  0.0076  -0.1540 603  GLY B C   
13144 O O   . GLY B 605  ? 0.4008 0.4087 0.4206 0.1414  0.0086  -0.1525 603  GLY B O   
13145 N N   . SER B 606  ? 0.4339 0.4411 0.4347 0.1364  0.0137  -0.1549 604  SER B N   
13146 C CA  . SER B 606  ? 0.4114 0.4372 0.4182 0.1405  0.0225  -0.1540 604  SER B CA  
13147 C C   . SER B 606  ? 0.3867 0.4256 0.3931 0.1347  0.0281  -0.1506 604  SER B C   
13148 O O   . SER B 606  ? 0.4109 0.4423 0.4061 0.1297  0.0265  -0.1514 604  SER B O   
13149 C CB  . SER B 606  ? 0.3727 0.3939 0.3697 0.1469  0.0249  -0.1590 604  SER B CB  
13150 O OG  . SER B 606  ? 0.5091 0.5187 0.5069 0.1528  0.0199  -0.1621 604  SER B OG  
13151 N N   . VAL B 607  ? 0.3730 0.4313 0.3918 0.1349  0.0346  -0.1465 605  VAL B N   
13152 C CA  . VAL B 607  ? 0.3514 0.4233 0.3704 0.1296  0.0405  -0.1426 605  VAL B CA  
13153 C C   . VAL B 607  ? 0.3978 0.4847 0.4189 0.1337  0.0490  -0.1419 605  VAL B C   
13154 O O   . VAL B 607  ? 0.3836 0.4783 0.4146 0.1391  0.0513  -0.1415 605  VAL B O   
13155 C CB  . VAL B 607  ? 0.3520 0.4322 0.3834 0.1220  0.0398  -0.1348 605  VAL B CB  
13156 C CG1 . VAL B 607  ? 0.3754 0.4666 0.4235 0.1263  0.0408  -0.1331 605  VAL B CG1 
13157 C CG2 . VAL B 607  ? 0.3117 0.4044 0.3426 0.1156  0.0456  -0.1296 605  VAL B CG2 
13158 N N   . THR B 608  ? 0.3632 0.4536 0.3744 0.1312  0.0534  -0.1416 606  THR B N   
13159 C CA  . THR B 608  ? 0.3318 0.4371 0.3440 0.1337  0.0620  -0.1400 606  THR B CA  
13160 C C   . THR B 608  ? 0.3187 0.4397 0.3380 0.1270  0.0667  -0.1333 606  THR B C   
13161 O O   . THR B 608  ? 0.3256 0.4431 0.3381 0.1209  0.0651  -0.1319 606  THR B O   
13162 C CB  . THR B 608  ? 0.3861 0.4831 0.3810 0.1357  0.0633  -0.1445 606  THR B CB  
13163 O OG1 . THR B 608  ? 0.3981 0.4803 0.3873 0.1419  0.0587  -0.1507 606  THR B OG1 
13164 C CG2 . THR B 608  ? 0.3468 0.4592 0.3416 0.1377  0.0725  -0.1426 606  THR B CG2 
13165 N N   . GLU B 609  ? 0.3311 0.4691 0.3640 0.1279  0.0721  -0.1288 607  GLU B N   
13166 C CA  . GLU B 609  ? 0.3408 0.4923 0.3824 0.1209  0.0751  -0.1220 607  GLU B CA  
13167 C C   . GLU B 609  ? 0.2904 0.4541 0.3278 0.1191  0.0830  -0.1186 607  GLU B C   
13168 O O   . GLU B 609  ? 0.3039 0.4700 0.3360 0.1241  0.0875  -0.1209 607  GLU B O   
13169 C CB  . GLU B 609  ? 0.3436 0.5056 0.4042 0.1210  0.0746  -0.1182 607  GLU B CB  
13170 C CG  . GLU B 609  ? 0.3755 0.5245 0.4391 0.1210  0.0661  -0.1207 607  GLU B CG  
13171 C CD  . GLU B 609  ? 0.4692 0.6269 0.5507 0.1196  0.0643  -0.1163 607  GLU B CD  
13172 O OE1 . GLU B 609  ? 0.4774 0.6495 0.5702 0.1224  0.0688  -0.1138 607  GLU B OE1 
13173 O OE2 . GLU B 609  ? 0.4315 0.5789 0.5143 0.1137  0.0575  -0.1134 607  GLU B OE2 
13174 N N   . THR B 610  ? 0.3404 0.5110 0.3795 0.1117  0.0845  -0.1132 608  THR B N   
13175 C CA  . THR B 610  ? 0.3334 0.5126 0.3658 0.1085  0.0907  -0.1096 608  THR B CA  
13176 C C   . THR B 610  ? 0.3321 0.5299 0.3772 0.1086  0.0977  -0.1040 608  THR B C   
13177 O O   . THR B 610  ? 0.3665 0.5731 0.4270 0.1061  0.0973  -0.0997 608  THR B O   
13178 C CB  . THR B 610  ? 0.3617 0.5398 0.3908 0.1004  0.0889  -0.1058 608  THR B CB  
13179 O OG1 . THR B 610  ? 0.3427 0.5024 0.3623 0.0990  0.0812  -0.1097 608  THR B OG1 
13180 C CG2 . THR B 610  ? 0.3745 0.5583 0.3936 0.0974  0.0943  -0.1028 608  THR B CG2 
13181 N N   . SER B 611  ? 0.3015 0.5053 0.3402 0.1111  0.1041  -0.1039 609  SER B N   
13182 C CA  . SER B 611  ? 0.3669 0.5890 0.4167 0.1095  0.1111  -0.0975 609  SER B CA  
13183 C C   . SER B 611  ? 0.3854 0.6147 0.4370 0.1006  0.1127  -0.0901 609  SER B C   
13184 O O   . SER B 611  ? 0.3722 0.5933 0.4128 0.0966  0.1100  -0.0903 609  SER B O   
13185 C CB  . SER B 611  ? 0.3782 0.6048 0.4203 0.1146  0.1177  -0.0995 609  SER B CB  
13186 O OG  . SER B 611  ? 0.3814 0.6024 0.4067 0.1124  0.1190  -0.1003 609  SER B OG  
13187 N N   . GLU B 612  ? 0.3875 0.6324 0.4535 0.0973  0.1168  -0.0832 610  GLU B N   
13188 C CA  . GLU B 612  ? 0.4348 0.6869 0.5029 0.0887  0.1184  -0.0756 610  GLU B CA  
13189 C C   . GLU B 612  ? 0.4081 0.6599 0.4610 0.0872  0.1228  -0.0744 610  GLU B C   
13190 O O   . GLU B 612  ? 0.3971 0.6462 0.4436 0.0811  0.1215  -0.0711 610  GLU B O   
13191 C CB  . GLU B 612  ? 0.4845 0.7532 0.5708 0.0855  0.1220  -0.0684 610  GLU B CB  
13192 C CG  . GLU B 612  ? 0.4883 0.7581 0.5900 0.0834  0.1167  -0.0669 610  GLU B CG  
13193 C CD  . GLU B 612  ? 0.5604 0.8467 0.6798 0.0792  0.1199  -0.0593 610  GLU B CD  
13194 O OE1 . GLU B 612  ? 0.6197 0.9147 0.7387 0.0741  0.1248  -0.0531 610  GLU B OE1 
13195 O OE2 . GLU B 612  ? 0.5039 0.7940 0.6374 0.0809  0.1173  -0.0594 610  GLU B OE2 
13196 N N   . GLU B 613  ? 0.4150 0.6697 0.4617 0.0926  0.1279  -0.0771 611  GLU B N   
13197 C CA  . GLU B 613  ? 0.3572 0.6111 0.3885 0.0915  0.1318  -0.0765 611  GLU B CA  
13198 C C   . GLU B 613  ? 0.4267 0.6644 0.4415 0.0913  0.1264  -0.0814 611  GLU B C   
13199 O O   . GLU B 613  ? 0.4183 0.6546 0.4232 0.0865  0.1268  -0.0784 611  GLU B O   
13200 C CB  . GLU B 613  ? 0.4249 0.6839 0.4522 0.0982  0.1378  -0.0796 611  GLU B CB  
13201 N N   . ASP B 614  ? 0.4026 0.6278 0.4144 0.0962  0.1209  -0.0888 612  ASP B N   
13202 C CA  . ASP B 614  ? 0.3919 0.6012 0.3887 0.0957  0.1151  -0.0936 612  ASP B CA  
13203 C C   . ASP B 614  ? 0.4183 0.6251 0.4184 0.0885  0.1105  -0.0899 612  ASP B C   
13204 O O   . ASP B 614  ? 0.3830 0.5809 0.3708 0.0856  0.1074  -0.0910 612  ASP B O   
13205 C CB  . ASP B 614  ? 0.3981 0.5942 0.3914 0.1025  0.1102  -0.1023 612  ASP B CB  
13206 C CG  . ASP B 614  ? 0.4734 0.6668 0.4563 0.1094  0.1135  -0.1077 612  ASP B CG  
13207 O OD1 . ASP B 614  ? 0.4682 0.6661 0.4417 0.1085  0.1184  -0.1059 612  ASP B OD1 
13208 O OD2 . ASP B 614  ? 0.4859 0.6720 0.4695 0.1158  0.1111  -0.1137 612  ASP B OD2 
13209 N N   . ALA B 615  ? 0.3443 0.5587 0.3609 0.0856  0.1099  -0.0855 613  ALA B N   
13210 C CA  . ALA B 615  ? 0.3761 0.5889 0.3959 0.0786  0.1060  -0.0817 613  ALA B CA  
13211 C C   . ALA B 615  ? 0.3982 0.6171 0.4128 0.0723  0.1095  -0.0748 613  ALA B C   
13212 O O   . ALA B 615  ? 0.3381 0.5466 0.3444 0.0670  0.1051  -0.0728 613  ALA B O   
13213 C CB  . ALA B 615  ? 0.3265 0.5438 0.3646 0.0760  0.1037  -0.0777 613  ALA B CB  
13214 N N   . ARG B 616  ? 0.3424 0.5743 0.3614 0.0718  0.1162  -0.0698 614  ARG B N   
13215 C CA  . ARG B 616  ? 0.3890 0.6264 0.4019 0.0662  0.1197  -0.0632 614  ARG B CA  
13216 C C   . ARG B 616  ? 0.3944 0.6226 0.3875 0.0678  0.1193  -0.0670 614  ARG B C   
13217 O O   . ARG B 616  ? 0.4110 0.6370 0.3961 0.0628  0.1182  -0.0635 614  ARG B O   
13218 C CB  . ARG B 616  ? 0.4283 0.6807 0.4498 0.0656  0.1268  -0.0574 614  ARG B CB  
13219 C CG  . ARG B 616  ? 0.4177 0.6799 0.4587 0.0615  0.1267  -0.0516 614  ARG B CG  
13220 C CD  . ARG B 616  ? 0.4685 0.7457 0.5182 0.0594  0.1334  -0.0449 614  ARG B CD  
13221 N NE  . ARG B 616  ? 0.5370 0.8195 0.5909 0.0664  0.1370  -0.0489 614  ARG B NE  
13222 C CZ  . ARG B 616  ? 0.5226 0.8096 0.5914 0.0691  0.1359  -0.0501 614  ARG B CZ  
13223 N NH1 . ARG B 616  ? 0.5189 0.8061 0.5999 0.0651  0.1313  -0.0476 614  ARG B NH1 
13224 N NH2 . ARG B 616  ? 0.4865 0.7777 0.5577 0.0760  0.1393  -0.0541 614  ARG B NH2 
13225 N N   . ARG B 617  ? 0.4036 0.6259 0.3883 0.0748  0.1197  -0.0742 615  ARG B N   
13226 C CA  . ARG B 617  ? 0.4303 0.6431 0.3959 0.0764  0.1187  -0.0783 615  ARG B CA  
13227 C C   . ARG B 617  ? 0.3653 0.5652 0.3235 0.0737  0.1113  -0.0811 615  ARG B C   
13228 O O   . ARG B 617  ? 0.3685 0.5643 0.3143 0.0705  0.1101  -0.0799 615  ARG B O   
13229 C CB  . ARG B 617  ? 0.4201 0.6281 0.3789 0.0845  0.1201  -0.0859 615  ARG B CB  
13230 C CG  . ARG B 617  ? 0.4363 0.6334 0.3750 0.0865  0.1185  -0.0909 615  ARG B CG  
13231 C CD  . ARG B 617  ? 0.5294 0.7266 0.4616 0.0938  0.1227  -0.0961 615  ARG B CD  
13232 N NE  . ARG B 617  ? 0.5174 0.7061 0.4524 0.1002  0.1192  -0.1037 615  ARG B NE  
13233 C CZ  . ARG B 617  ? 0.5871 0.7596 0.5116 0.1024  0.1127  -0.1107 615  ARG B CZ  
13234 N NH1 . ARG B 617  ? 0.5612 0.7247 0.4721 0.0987  0.1086  -0.1114 615  ARG B NH1 
13235 N NH2 . ARG B 617  ? 0.5358 0.7010 0.4637 0.1082  0.1098  -0.1169 615  ARG B NH2 
13236 N N   . ALA B 618  ? 0.3930 0.5870 0.3592 0.0748  0.1063  -0.0846 616  ALA B N   
13237 C CA  . ALA B 618  ? 0.3489 0.5279 0.3105 0.0705  0.0980  -0.0854 616  ALA B CA  
13238 C C   . ALA B 618  ? 0.3491 0.5290 0.3115 0.0619  0.0966  -0.0769 616  ALA B C   
13239 O O   . ALA B 618  ? 0.3320 0.5022 0.2840 0.0586  0.0922  -0.0768 616  ALA B O   
13240 C CB  . ALA B 618  ? 0.3208 0.4929 0.2940 0.0711  0.0926  -0.0873 616  ALA B CB  
13241 N N   . VAL B 619  ? 0.3774 0.5685 0.3527 0.0583  0.1000  -0.0698 617  VAL B N   
13242 C CA  . VAL B 619  ? 0.3884 0.5795 0.3652 0.0504  0.0984  -0.0617 617  VAL B CA  
13243 C C   . VAL B 619  ? 0.3857 0.5801 0.3490 0.0490  0.1018  -0.0593 617  VAL B C   
13244 O O   . VAL B 619  ? 0.4369 0.6248 0.3939 0.0441  0.0981  -0.0558 617  VAL B O   
13245 C CB  . VAL B 619  ? 0.3733 0.5751 0.3668 0.0468  0.1009  -0.0549 617  VAL B CB  
13246 C CG1 . VAL B 619  ? 0.3735 0.5739 0.3679 0.0390  0.0989  -0.0469 617  VAL B CG1 
13247 C CG2 . VAL B 619  ? 0.3303 0.5280 0.3363 0.0480  0.0967  -0.0574 617  VAL B CG2 
13248 N N   . ARG B 620  ? 0.4200 0.6246 0.3782 0.0537  0.1089  -0.0611 618  ARG B N   
13249 C CA  . ARG B 620  ? 0.3939 0.6012 0.3376 0.0529  0.1121  -0.0591 618  ARG B CA  
13250 C C   . ARG B 620  ? 0.4216 0.6149 0.3490 0.0543  0.1067  -0.0651 618  ARG B C   
13251 O O   . ARG B 620  ? 0.4149 0.6048 0.3321 0.0505  0.1049  -0.0619 618  ARG B O   
13252 C CB  . ARG B 620  ? 0.4627 0.6805 0.4050 0.0570  0.1199  -0.0591 618  ARG B CB  
13253 C CG  . ARG B 620  ? 0.5096 0.7414 0.4647 0.0529  0.1253  -0.0503 618  ARG B CG  
13254 C CD  . ARG B 620  ? 0.5305 0.7705 0.4816 0.0552  0.1323  -0.0486 618  ARG B CD  
13255 N NE  . ARG B 620  ? 0.6310 0.8694 0.5814 0.0630  0.1340  -0.0563 618  ARG B NE  
13256 C CZ  . ARG B 620  ? 0.5997 0.8441 0.5645 0.0660  0.1357  -0.0575 618  ARG B CZ  
13257 N NH1 . ARG B 620  ? 0.5843 0.8369 0.5657 0.0617  0.1360  -0.0516 618  ARG B NH1 
13258 N NH2 . ARG B 620  ? 0.5668 0.8086 0.5294 0.0735  0.1369  -0.0648 618  ARG B NH2 
13259 N N   . LEU B 621  ? 0.3978 0.5825 0.3226 0.0597  0.1036  -0.0737 619  LEU B N   
13260 C CA  . LEU B 621  ? 0.3834 0.5538 0.2938 0.0604  0.0974  -0.0793 619  LEU B CA  
13261 C C   . LEU B 621  ? 0.3928 0.5533 0.3056 0.0535  0.0897  -0.0754 619  LEU B C   
13262 O O   . LEU B 621  ? 0.3818 0.5346 0.2829 0.0512  0.0855  -0.0757 619  LEU B O   
13263 C CB  . LEU B 621  ? 0.4115 0.5741 0.3200 0.0673  0.0952  -0.0889 619  LEU B CB  
13264 C CG  . LEU B 621  ? 0.4245 0.5897 0.3273 0.0744  0.1003  -0.0937 619  LEU B CG  
13265 C CD1 . LEU B 621  ? 0.4396 0.5970 0.3465 0.0803  0.0975  -0.1012 619  LEU B CD1 
13266 C CD2 . LEU B 621  ? 0.4421 0.6008 0.3258 0.0751  0.0997  -0.0962 619  LEU B CD2 
13267 N N   . ALA B 622  ? 0.3781 0.5389 0.3062 0.0505  0.0876  -0.0718 620  ALA B N   
13268 C CA  . ALA B 622  ? 0.3904 0.5431 0.3214 0.0442  0.0811  -0.0677 620  ALA B CA  
13269 C C   . ALA B 622  ? 0.3713 0.5289 0.2993 0.0389  0.0825  -0.0598 620  ALA B C   
13270 O O   . ALA B 622  ? 0.4036 0.5539 0.3256 0.0352  0.0775  -0.0580 620  ALA B O   
13271 C CB  . ALA B 622  ? 0.3610 0.5131 0.3081 0.0426  0.0789  -0.0658 620  ALA B CB  
13272 N N   . ALA B 623  ? 0.3703 0.5404 0.3026 0.0384  0.0893  -0.0548 621  ALA B N   
13273 C CA  . ALA B 623  ? 0.3940 0.5683 0.3235 0.0332  0.0905  -0.0468 621  ALA B CA  
13274 C C   . ALA B 623  ? 0.4187 0.5900 0.3304 0.0339  0.0901  -0.0482 621  ALA B C   
13275 O O   . ALA B 623  ? 0.4085 0.5757 0.3152 0.0295  0.0865  -0.0438 621  ALA B O   
13276 C CB  . ALA B 623  ? 0.3632 0.5517 0.3010 0.0324  0.0979  -0.0410 621  ALA B CB  
13277 N N   . ASP B 624  ? 0.3933 0.5663 0.2950 0.0396  0.0935  -0.0546 622  ASP B N   
13278 C CA  . ASP B 624  ? 0.4139 0.5842 0.2976 0.0404  0.0931  -0.0564 622  ASP B CA  
13279 C C   . ASP B 624  ? 0.4520 0.6083 0.3285 0.0388  0.0844  -0.0597 622  ASP B C   
13280 O O   . ASP B 624  ? 0.4573 0.6107 0.3221 0.0365  0.0820  -0.0579 622  ASP B O   
13281 C CB  . ASP B 624  ? 0.5188 0.6934 0.3932 0.0475  0.0986  -0.0633 622  ASP B CB  
13282 C CG  . ASP B 624  ? 0.5794 0.7698 0.4600 0.0492  0.1079  -0.0595 622  ASP B CG  
13283 O OD1 . ASP B 624  ? 0.6470 0.8449 0.5352 0.0439  0.1102  -0.0506 622  ASP B OD1 
13284 O OD2 . ASP B 624  ? 0.6803 0.8715 0.5603 0.0546  0.1114  -0.0642 622  ASP B OD2 
13285 N N   . ALA B 625  ? 0.4213 0.5694 0.3050 0.0395  0.0794  -0.0641 623  ALA B N   
13286 C CA  . ALA B 625  ? 0.4614 0.5969 0.3398 0.0375  0.0711  -0.0669 623  ALA B CA  
13287 C C   . ALA B 625  ? 0.4246 0.5571 0.3128 0.0315  0.0663  -0.0607 623  ALA B C   
13288 O O   . ALA B 625  ? 0.4209 0.5443 0.3061 0.0294  0.0595  -0.0621 623  ALA B O   
13289 C CB  . ALA B 625  ? 0.4866 0.6137 0.3656 0.0417  0.0680  -0.0755 623  ALA B CB  
13290 N N   . ALA B 626  ? 0.3787 0.5186 0.2786 0.0289  0.0696  -0.0541 624  ALA B N   
13291 C CA  . ALA B 626  ? 0.4015 0.5380 0.3104 0.0239  0.0651  -0.0486 624  ALA B CA  
13292 C C   . ALA B 626  ? 0.3856 0.5177 0.2861 0.0204  0.0605  -0.0454 624  ALA B C   
13293 O O   . ALA B 626  ? 0.4186 0.5438 0.3227 0.0180  0.0545  -0.0451 624  ALA B O   
13294 C CB  . ALA B 626  ? 0.3271 0.4723 0.2481 0.0216  0.0695  -0.0417 624  ALA B CB  
13295 N N   . PRO B 627  ? 0.3921 0.5281 0.2817 0.0199  0.0626  -0.0427 625  PRO B N   
13296 C CA  . PRO B 627  ? 0.4008 0.5324 0.2833 0.0166  0.0574  -0.0395 625  PRO B CA  
13297 C C   . PRO B 627  ? 0.4244 0.5468 0.2989 0.0174  0.0510  -0.0457 625  PRO B C   
13298 O O   . PRO B 627  ? 0.4000 0.5177 0.2751 0.0143  0.0451  -0.0436 625  PRO B O   
13299 C CB  . PRO B 627  ? 0.4655 0.6037 0.3372 0.0165  0.0617  -0.0356 625  PRO B CB  
13300 C CG  . PRO B 627  ? 0.4317 0.5792 0.3094 0.0182  0.0695  -0.0342 625  PRO B CG  
13301 C CD  . PRO B 627  ? 0.4289 0.5744 0.3133 0.0219  0.0700  -0.0412 625  PRO B CD  
13302 N N   . ASP B 628  ? 0.4066 0.5264 0.2738 0.0215  0.0518  -0.0534 626  ASP B N   
13303 C CA  . ASP B 628  ? 0.4018 0.5119 0.2613 0.0218  0.0452  -0.0594 626  ASP B CA  
13304 C C   . ASP B 628  ? 0.4232 0.5271 0.2939 0.0198  0.0400  -0.0602 626  ASP B C   
13305 O O   . ASP B 628  ? 0.3833 0.4808 0.2515 0.0172  0.0334  -0.0607 626  ASP B O   
13306 C CB  . ASP B 628  ? 0.4088 0.5164 0.2586 0.0270  0.0471  -0.0677 626  ASP B CB  
13307 C CG  . ASP B 628  ? 0.5230 0.6349 0.3579 0.0289  0.0508  -0.0680 626  ASP B CG  
13308 O OD1 . ASP B 628  ? 0.5370 0.6524 0.3678 0.0257  0.0505  -0.0618 626  ASP B OD1 
13309 O OD2 . ASP B 628  ? 0.5829 0.6944 0.4099 0.0339  0.0539  -0.0744 626  ASP B OD2 
13310 N N   . TRP B 629  ? 0.3677 0.4736 0.2507 0.0209  0.0428  -0.0601 627  TRP B N   
13311 C CA  . TRP B 629  ? 0.3634 0.4636 0.2566 0.0191  0.0383  -0.0606 627  TRP B CA  
13312 C C   . TRP B 629  ? 0.3597 0.4614 0.2599 0.0145  0.0357  -0.0534 627  TRP B C   
13313 O O   . TRP B 629  ? 0.3508 0.4472 0.2536 0.0121  0.0301  -0.0534 627  TRP B O   
13314 C CB  . TRP B 629  ? 0.3619 0.4638 0.2657 0.0218  0.0417  -0.0626 627  TRP B CB  
13315 C CG  . TRP B 629  ? 0.3103 0.4064 0.2237 0.0199  0.0373  -0.0629 627  TRP B CG  
13316 C CD1 . TRP B 629  ? 0.3033 0.4020 0.2296 0.0184  0.0381  -0.0590 627  TRP B CD1 
13317 C CD2 . TRP B 629  ? 0.3331 0.4200 0.2438 0.0191  0.0310  -0.0669 627  TRP B CD2 
13318 N NE1 . TRP B 629  ? 0.2644 0.3563 0.1955 0.0169  0.0331  -0.0604 627  TRP B NE1 
13319 C CE2 . TRP B 629  ? 0.2611 0.3458 0.1832 0.0172  0.0287  -0.0650 627  TRP B CE2 
13320 C CE3 . TRP B 629  ? 0.3256 0.4055 0.2250 0.0196  0.0268  -0.0720 627  TRP B CE3 
13321 C CZ2 . TRP B 629  ? 0.3152 0.3919 0.2381 0.0156  0.0229  -0.0675 627  TRP B CZ2 
13322 C CZ3 . TRP B 629  ? 0.3244 0.3958 0.2251 0.0176  0.0205  -0.0744 627  TRP B CZ3 
13323 C CH2 . TRP B 629  ? 0.3515 0.4218 0.2640 0.0156  0.0188  -0.0720 627  TRP B CH2 
13324 N N   . ALA B 630  ? 0.3734 0.4822 0.2763 0.0134  0.0397  -0.0472 628  ALA B N   
13325 C CA  . ALA B 630  ? 0.3782 0.4877 0.2872 0.0097  0.0373  -0.0406 628  ALA B CA  
13326 C C   . ALA B 630  ? 0.3974 0.5034 0.2984 0.0075  0.0317  -0.0396 628  ALA B C   
13327 O O   . ALA B 630  ? 0.3842 0.4884 0.2908 0.0050  0.0276  -0.0364 628  ALA B O   
13328 C CB  . ALA B 630  ? 0.3830 0.4998 0.2948 0.0087  0.0423  -0.0341 628  ALA B CB  
13329 N N   . ALA B 631  ? 0.3657 0.4711 0.2536 0.0087  0.0313  -0.0425 629  ALA B N   
13330 C CA  . ALA B 631  ? 0.4083 0.5110 0.2877 0.0066  0.0257  -0.0417 629  ALA B CA  
13331 C C   . ALA B 631  ? 0.4130 0.5085 0.2921 0.0058  0.0194  -0.0466 629  ALA B C   
13332 O O   . ALA B 631  ? 0.3511 0.4444 0.2248 0.0036  0.0139  -0.0459 629  ALA B O   
13333 C CB  . ALA B 631  ? 0.4376 0.5421 0.3020 0.0081  0.0276  -0.0430 629  ALA B CB  
13334 N N   . VAL B 632  ? 0.3492 0.4409 0.2336 0.0073  0.0196  -0.0514 630  VAL B N   
13335 C CA  . VAL B 632  ? 0.3553 0.4401 0.2413 0.0056  0.0134  -0.0547 630  VAL B CA  
13336 C C   . VAL B 632  ? 0.3756 0.4619 0.2726 0.0024  0.0108  -0.0492 630  VAL B C   
13337 O O   . VAL B 632  ? 0.3701 0.4596 0.2772 0.0028  0.0143  -0.0462 630  VAL B O   
13338 C CB  . VAL B 632  ? 0.3641 0.4439 0.2528 0.0081  0.0142  -0.0608 630  VAL B CB  
13339 C CG1 . VAL B 632  ? 0.3355 0.4081 0.2264 0.0056  0.0076  -0.0633 630  VAL B CG1 
13340 C CG2 . VAL B 632  ? 0.3507 0.4289 0.2282 0.0120  0.0169  -0.0666 630  VAL B CG2 
13341 N N   . PRO B 633  ? 0.3416 0.4264 0.2372 -0.0005 0.0049  -0.0479 631  PRO B N   
13342 C CA  . PRO B 633  ? 0.3365 0.4237 0.2423 -0.0030 0.0027  -0.0426 631  PRO B CA  
13343 C C   . PRO B 633  ? 0.3719 0.4573 0.2887 -0.0028 0.0036  -0.0435 631  PRO B C   
13344 O O   . PRO B 633  ? 0.3510 0.4313 0.2672 -0.0021 0.0027  -0.0486 631  PRO B O   
13345 C CB  . PRO B 633  ? 0.3273 0.4124 0.2290 -0.0058 -0.0043 -0.0431 631  PRO B CB  
13346 C CG  . PRO B 633  ? 0.3850 0.4689 0.2727 -0.0050 -0.0049 -0.0457 631  PRO B CG  
13347 C CD  . PRO B 633  ? 0.3828 0.4644 0.2667 -0.0015 0.0002  -0.0507 631  PRO B CD  
13348 N N   . PRO B 634  ? 0.3802 0.4690 0.3067 -0.0032 0.0052  -0.0387 632  PRO B N   
13349 C CA  . PRO B 634  ? 0.3435 0.4305 0.2799 -0.0030 0.0061  -0.0394 632  PRO B CA  
13350 C C   . PRO B 634  ? 0.3013 0.3836 0.2390 -0.0047 0.0015  -0.0425 632  PRO B C   
13351 O O   . PRO B 634  ? 0.2859 0.3644 0.2268 -0.0038 0.0022  -0.0458 632  PRO B O   
13352 C CB  . PRO B 634  ? 0.3369 0.4280 0.2814 -0.0036 0.0068  -0.0334 632  PRO B CB  
13353 C CG  . PRO B 634  ? 0.3643 0.4592 0.3036 -0.0033 0.0085  -0.0298 632  PRO B CG  
13354 C CD  . PRO B 634  ? 0.3305 0.4244 0.2585 -0.0036 0.0064  -0.0325 632  PRO B CD  
13355 N N   . SER B 635  ? 0.2981 0.3808 0.2337 -0.0073 -0.0034 -0.0413 633  SER B N   
13356 C CA  . SER B 635  ? 0.3058 0.3845 0.2428 -0.0097 -0.0081 -0.0436 633  SER B CA  
13357 C C   . SER B 635  ? 0.3068 0.3785 0.2360 -0.0091 -0.0095 -0.0499 633  SER B C   
13358 O O   . SER B 635  ? 0.3157 0.3822 0.2471 -0.0103 -0.0119 -0.0525 633  SER B O   
13359 C CB  . SER B 635  ? 0.3854 0.4671 0.3219 -0.0128 -0.0132 -0.0406 633  SER B CB  
13360 O OG  . SER B 635  ? 0.4496 0.5309 0.3756 -0.0130 -0.0151 -0.0419 633  SER B OG  
13361 N N   . GLU B 636  ? 0.2944 0.3654 0.2138 -0.0073 -0.0083 -0.0524 634  GLU B N   
13362 C CA  . GLU B 636  ? 0.3143 0.3781 0.2257 -0.0058 -0.0093 -0.0589 634  GLU B CA  
13363 C C   . GLU B 636  ? 0.3367 0.3987 0.2518 -0.0022 -0.0044 -0.0618 634  GLU B C   
13364 O O   . GLU B 636  ? 0.3117 0.3666 0.2248 -0.0013 -0.0060 -0.0668 634  GLU B O   
13365 C CB  . GLU B 636  ? 0.3506 0.4142 0.2493 -0.0047 -0.0094 -0.0611 634  GLU B CB  
13366 C CG  . GLU B 636  ? 0.4552 0.5109 0.3442 -0.0023 -0.0103 -0.0685 634  GLU B CG  
13367 C CD  . GLU B 636  ? 0.5376 0.5846 0.4270 -0.0048 -0.0164 -0.0721 634  GLU B CD  
13368 O OE1 . GLU B 636  ? 0.4707 0.5173 0.3610 -0.0093 -0.0221 -0.0699 634  GLU B OE1 
13369 O OE2 . GLU B 636  ? 0.4918 0.5325 0.3810 -0.0024 -0.0156 -0.0769 634  GLU B OE2 
13370 N N   . ARG B 637  ? 0.2757 0.3437 0.1963 -0.0003 0.0011  -0.0586 635  ARG B N   
13371 C CA  . ARG B 637  ? 0.2670 0.3342 0.1932 0.0026  0.0051  -0.0606 635  ARG B CA  
13372 C C   . ARG B 637  ? 0.3040 0.3676 0.2389 0.0010  0.0026  -0.0603 635  ARG B C   
13373 O O   . ARG B 637  ? 0.2507 0.3094 0.1870 0.0027  0.0027  -0.0641 635  ARG B O   
13374 C CB  . ARG B 637  ? 0.2849 0.3595 0.2159 0.0042  0.0109  -0.0565 635  ARG B CB  
13375 C CG  . ARG B 637  ? 0.2824 0.3613 0.2049 0.0054  0.0138  -0.0558 635  ARG B CG  
13376 C CD  . ARG B 637  ? 0.2873 0.3730 0.2149 0.0069  0.0198  -0.0521 635  ARG B CD  
13377 N NE  . ARG B 637  ? 0.3004 0.3890 0.2373 0.0047  0.0197  -0.0463 635  ARG B NE  
13378 C CZ  . ARG B 637  ? 0.3296 0.4227 0.2663 0.0035  0.0208  -0.0410 635  ARG B CZ  
13379 N NH1 . ARG B 637  ? 0.3833 0.4790 0.3110 0.0038  0.0220  -0.0401 635  ARG B NH1 
13380 N NH2 . ARG B 637  ? 0.2905 0.3852 0.2357 0.0021  0.0207  -0.0364 635  ARG B NH2 
13381 N N   . ALA B 638  ? 0.2690 0.3353 0.2095 -0.0021 0.0004  -0.0557 636  ALA B N   
13382 C CA  . ALA B 638  ? 0.2473 0.3107 0.1951 -0.0039 -0.0020 -0.0551 636  ALA B CA  
13383 C C   . ALA B 638  ? 0.2522 0.3079 0.1955 -0.0056 -0.0070 -0.0592 636  ALA B C   
13384 O O   . ALA B 638  ? 0.2842 0.3352 0.2314 -0.0059 -0.0083 -0.0606 636  ALA B O   
13385 C CB  . ALA B 638  ? 0.2397 0.3082 0.1934 -0.0066 -0.0033 -0.0495 636  ALA B CB  
13386 N N   . ALA B 639  ? 0.2716 0.3254 0.2063 -0.0069 -0.0103 -0.0610 637  ALA B N   
13387 C CA  . ALA B 639  ? 0.3017 0.3470 0.2312 -0.0088 -0.0157 -0.0650 637  ALA B CA  
13388 C C   . ALA B 639  ? 0.3235 0.3616 0.2496 -0.0051 -0.0144 -0.0709 637  ALA B C   
13389 O O   . ALA B 639  ? 0.2993 0.3295 0.2254 -0.0062 -0.0181 -0.0736 637  ALA B O   
13390 C CB  . ALA B 639  ? 0.3047 0.3494 0.2249 -0.0108 -0.0196 -0.0660 637  ALA B CB  
13391 N N   . CYS B 640  ? 0.2750 0.3158 0.1984 -0.0006 -0.0092 -0.0728 638  CYS B N   
13392 C CA  . CYS B 640  ? 0.2838 0.3194 0.2053 0.0037  -0.0073 -0.0781 638  CYS B CA  
13393 C C   . CYS B 640  ? 0.2662 0.3002 0.1975 0.0041  -0.0067 -0.0771 638  CYS B C   
13394 O O   . CYS B 640  ? 0.2625 0.2885 0.1930 0.0053  -0.0089 -0.0810 638  CYS B O   
13395 C CB  . CYS B 640  ? 0.2971 0.3388 0.2159 0.0083  -0.0010 -0.0790 638  CYS B CB  
13396 S SG  . CYS B 640  ? 0.3577 0.3996 0.2623 0.0092  -0.0012 -0.0817 638  CYS B SG  
13397 N N   . LEU B 641  ? 0.2582 0.2993 0.1983 0.0031  -0.0038 -0.0719 639  LEU B N   
13398 C CA  . LEU B 641  ? 0.2604 0.3004 0.2094 0.0033  -0.0034 -0.0708 639  LEU B CA  
13399 C C   . LEU B 641  ? 0.2873 0.3203 0.2370 -0.0004 -0.0090 -0.0707 639  LEU B C   
13400 O O   . LEU B 641  ? 0.2977 0.3245 0.2496 0.0005  -0.0105 -0.0729 639  LEU B O   
13401 C CB  . LEU B 641  ? 0.2544 0.3026 0.2115 0.0026  0.0001  -0.0652 639  LEU B CB  
13402 C CG  . LEU B 641  ? 0.2329 0.2869 0.1934 0.0061  0.0058  -0.0647 639  LEU B CG  
13403 C CD1 . LEU B 641  ? 0.2882 0.3455 0.2415 0.0084  0.0087  -0.0665 639  LEU B CD1 
13404 C CD2 . LEU B 641  ? 0.2529 0.3131 0.2212 0.0045  0.0078  -0.0591 639  LEU B CD2 
13405 N N   . ASP B 642  ? 0.2723 0.3066 0.2205 -0.0047 -0.0124 -0.0680 640  ASP B N   
13406 C CA  . ASP B 642  ? 0.2678 0.2967 0.2171 -0.0089 -0.0178 -0.0673 640  ASP B CA  
13407 C C   . ASP B 642  ? 0.2768 0.2947 0.2190 -0.0085 -0.0219 -0.0729 640  ASP B C   
13408 O O   . ASP B 642  ? 0.3106 0.3217 0.2548 -0.0101 -0.0251 -0.0734 640  ASP B O   
13409 C CB  . ASP B 642  ? 0.2791 0.3128 0.2285 -0.0135 -0.0206 -0.0633 640  ASP B CB  
13410 C CG  . ASP B 642  ? 0.3314 0.3736 0.2896 -0.0145 -0.0180 -0.0575 640  ASP B CG  
13411 O OD1 . ASP B 642  ? 0.3100 0.3525 0.2741 -0.0129 -0.0155 -0.0567 640  ASP B OD1 
13412 O OD2 . ASP B 642  ? 0.3313 0.3799 0.2904 -0.0167 -0.0187 -0.0540 640  ASP B OD2 
13413 N N   . ARG B 643  ? 0.2726 0.2880 0.2059 -0.0062 -0.0219 -0.0771 641  ARG B N   
13414 C CA  . ARG B 643  ? 0.2807 0.2846 0.2066 -0.0051 -0.0259 -0.0831 641  ARG B CA  
13415 C C   . ARG B 643  ? 0.3200 0.3193 0.2486 -0.0003 -0.0236 -0.0862 641  ARG B C   
13416 O O   . ARG B 643  ? 0.3188 0.3080 0.2462 -0.0007 -0.0277 -0.0888 641  ARG B O   
13417 C CB  . ARG B 643  ? 0.2981 0.3005 0.2129 -0.0030 -0.0261 -0.0873 641  ARG B CB  
13418 C CG  . ARG B 643  ? 0.3365 0.3399 0.2467 -0.0082 -0.0308 -0.0854 641  ARG B CG  
13419 C CD  . ARG B 643  ? 0.4157 0.4148 0.3131 -0.0060 -0.0322 -0.0907 641  ARG B CD  
13420 N NE  . ARG B 643  ? 0.3518 0.3593 0.2469 -0.0017 -0.0258 -0.0906 641  ARG B NE  
13421 C CZ  . ARG B 643  ? 0.3844 0.4005 0.2788 -0.0034 -0.0245 -0.0866 641  ARG B CZ  
13422 N NH1 . ARG B 643  ? 0.3687 0.3871 0.2650 -0.0089 -0.0290 -0.0826 641  ARG B NH1 
13423 N NH2 . ARG B 643  ? 0.3933 0.4163 0.2852 0.0005  -0.0186 -0.0863 641  ARG B NH2 
13424 N N   . ALA B 644  ? 0.2728 0.2795 0.2056 0.0039  -0.0174 -0.0857 642  ALA B N   
13425 C CA  . ALA B 644  ? 0.3035 0.3075 0.2406 0.0083  -0.0152 -0.0880 642  ALA B CA  
13426 C C   . ALA B 644  ? 0.3551 0.3553 0.2993 0.0054  -0.0181 -0.0851 642  ALA B C   
13427 O O   . ALA B 644  ? 0.2931 0.2847 0.2372 0.0072  -0.0205 -0.0881 642  ALA B O   
13428 C CB  . ALA B 644  ? 0.2990 0.3133 0.2413 0.0121  -0.0083 -0.0865 642  ALA B CB  
13429 N N   . ALA B 645  ? 0.2713 0.2776 0.2212 0.0010  -0.0181 -0.0793 643  ALA B N   
13430 C CA  . ALA B 645  ? 0.2500 0.2538 0.2062 -0.0018 -0.0204 -0.0762 643  ALA B CA  
13431 C C   . ALA B 645  ? 0.2931 0.2857 0.2449 -0.0051 -0.0268 -0.0778 643  ALA B C   
13432 O O   . ALA B 645  ? 0.2927 0.2785 0.2467 -0.0049 -0.0290 -0.0782 643  ALA B O   
13433 C CB  . ALA B 645  ? 0.2532 0.2660 0.2152 -0.0055 -0.0190 -0.0700 643  ALA B CB  
13434 N N   . GLU B 646  ? 0.3173 0.3076 0.2627 -0.0082 -0.0304 -0.0788 644  GLU B N   
13435 C CA  . GLU B 646  ? 0.3649 0.3439 0.3057 -0.0118 -0.0371 -0.0805 644  GLU B CA  
13436 C C   . GLU B 646  ? 0.3820 0.3497 0.3180 -0.0071 -0.0387 -0.0866 644  GLU B C   
13437 O O   . GLU B 646  ? 0.3620 0.3197 0.2978 -0.0087 -0.0431 -0.0871 644  GLU B O   
13438 C CB  . GLU B 646  ? 0.3461 0.3247 0.2803 -0.0156 -0.0409 -0.0810 644  GLU B CB  
13439 C CG  . GLU B 646  ? 0.3873 0.3764 0.3261 -0.0204 -0.0405 -0.0749 644  GLU B CG  
13440 C CD  . GLU B 646  ? 0.4598 0.4498 0.4060 -0.0253 -0.0426 -0.0697 644  GLU B CD  
13441 O OE1 . GLU B 646  ? 0.5423 0.5225 0.4868 -0.0282 -0.0476 -0.0705 644  GLU B OE1 
13442 O OE2 . GLU B 646  ? 0.5004 0.5005 0.4536 -0.0261 -0.0391 -0.0648 644  GLU B OE2 
13443 N N   . LEU B 647  ? 0.3199 0.2887 0.2515 -0.0012 -0.0351 -0.0913 645  LEU B N   
13444 C CA  . LEU B 647  ? 0.3733 0.3322 0.3006 0.0043  -0.0360 -0.0975 645  LEU B CA  
13445 C C   . LEU B 647  ? 0.3401 0.2977 0.2751 0.0069  -0.0347 -0.0965 645  LEU B C   
13446 O O   . LEU B 647  ? 0.3512 0.2973 0.2843 0.0081  -0.0388 -0.0993 645  LEU B O   
13447 C CB  . LEU B 647  ? 0.3645 0.3274 0.2864 0.0104  -0.0314 -0.1022 645  LEU B CB  
13448 C CG  . LEU B 647  ? 0.4495 0.4105 0.3610 0.0091  -0.0336 -0.1050 645  LEU B CG  
13449 C CD1 . LEU B 647  ? 0.3820 0.3485 0.2885 0.0154  -0.0279 -0.1090 645  LEU B CD1 
13450 C CD2 . LEU B 647  ? 0.4104 0.3559 0.3136 0.0074  -0.0412 -0.1094 645  LEU B CD2 
13451 N N   . MET B 648  ? 0.3367 0.3054 0.2801 0.0076  -0.0296 -0.0923 646  MET B N   
13452 C CA  . MET B 648  ? 0.3038 0.2715 0.2544 0.0099  -0.0287 -0.0912 646  MET B CA  
13453 C C   . MET B 648  ? 0.3525 0.3134 0.3053 0.0047  -0.0338 -0.0877 646  MET B C   
13454 O O   . MET B 648  ? 0.3307 0.2844 0.2854 0.0065  -0.0360 -0.0885 646  MET B O   
13455 C CB  . MET B 648  ? 0.2945 0.2752 0.2532 0.0113  -0.0226 -0.0876 646  MET B CB  
13456 C CG  . MET B 648  ? 0.3816 0.3689 0.3403 0.0173  -0.0171 -0.0907 646  MET B CG  
13457 S SD  . MET B 648  ? 0.3455 0.3457 0.3149 0.0183  -0.0112 -0.0861 646  MET B SD  
13458 C CE  . MET B 648  ? 0.3416 0.3502 0.3087 0.0234  -0.0052 -0.0891 646  MET B CE  
13459 N N   . GLN B 649  ? 0.3288 0.2925 0.2816 -0.0017 -0.0358 -0.0833 647  GLN B N   
13460 C CA  . GLN B 649  ? 0.3580 0.3159 0.3124 -0.0072 -0.0405 -0.0796 647  GLN B CA  
13461 C C   . GLN B 649  ? 0.3357 0.2785 0.2836 -0.0079 -0.0469 -0.0834 647  GLN B C   
13462 O O   . GLN B 649  ? 0.3970 0.3316 0.3463 -0.0085 -0.0501 -0.0825 647  GLN B O   
13463 C CB  . GLN B 649  ? 0.3456 0.3108 0.3014 -0.0137 -0.0410 -0.0745 647  GLN B CB  
13464 C CG  . GLN B 649  ? 0.3406 0.3027 0.2992 -0.0197 -0.0449 -0.0696 647  GLN B CG  
13465 C CD  . GLN B 649  ? 0.3506 0.3179 0.3162 -0.0189 -0.0418 -0.0657 647  GLN B CD  
13466 O OE1 . GLN B 649  ? 0.3294 0.3079 0.2997 -0.0193 -0.0376 -0.0623 647  GLN B OE1 
13467 N NE2 . GLN B 649  ? 0.3344 0.2933 0.3005 -0.0174 -0.0439 -0.0664 647  GLN B NE2 
13468 N N   . ALA B 650  ? 0.3650 0.3032 0.3051 -0.0077 -0.0492 -0.0876 648  ALA B N   
13469 C CA  . ALA B 650  ? 0.3756 0.2982 0.3085 -0.0084 -0.0558 -0.0917 648  ALA B CA  
13470 C C   . ALA B 650  ? 0.3841 0.2978 0.3161 -0.0014 -0.0559 -0.0965 648  ALA B C   
13471 O O   . ALA B 650  ? 0.4387 0.3389 0.3680 -0.0022 -0.0616 -0.0978 648  ALA B O   
13472 C CB  . ALA B 650  ? 0.3865 0.3063 0.3105 -0.0088 -0.0579 -0.0958 648  ALA B CB  
13473 N N   . ARG B 651  ? 0.3595 0.2806 0.2939 0.0055  -0.0499 -0.0991 649  ARG B N   
13474 C CA  . ARG B 651  ? 0.3936 0.3085 0.3278 0.0131  -0.0493 -0.1041 649  ARG B CA  
13475 C C   . ARG B 651  ? 0.4104 0.3297 0.3539 0.0150  -0.0469 -0.1007 649  ARG B C   
13476 O O   . ARG B 651  ? 0.4177 0.3350 0.3629 0.0218  -0.0454 -0.1042 649  ARG B O   
13477 C CB  . ARG B 651  ? 0.3993 0.3199 0.3300 0.0198  -0.0442 -0.1095 649  ARG B CB  
13478 C CG  . ARG B 651  ? 0.4217 0.3374 0.3422 0.0179  -0.0470 -0.1129 649  ARG B CG  
13479 C CD  . ARG B 651  ? 0.4718 0.3935 0.3875 0.0241  -0.0419 -0.1179 649  ARG B CD  
13480 N NE  . ARG B 651  ? 0.4811 0.3980 0.3864 0.0213  -0.0452 -0.1206 649  ARG B NE  
13481 C CZ  . ARG B 651  ? 0.5091 0.4305 0.4076 0.0249  -0.0417 -0.1245 649  ARG B CZ  
13482 N NH1 . ARG B 651  ? 0.4054 0.3365 0.3066 0.0315  -0.0346 -0.1261 649  ARG B NH1 
13483 N NH2 . ARG B 651  ? 0.4877 0.4040 0.3765 0.0216  -0.0457 -0.1265 649  ARG B NH2 
13484 N N   . MET B 652  ? 0.3746 0.2997 0.3238 0.0093  -0.0467 -0.0941 650  MET B N   
13485 C CA  . MET B 652  ? 0.3751 0.3043 0.3324 0.0107  -0.0447 -0.0907 650  MET B CA  
13486 C C   . MET B 652  ? 0.4043 0.3217 0.3615 0.0145  -0.0486 -0.0931 650  MET B C   
13487 O O   . MET B 652  ? 0.4320 0.3535 0.3947 0.0199  -0.0457 -0.0940 650  MET B O   
13488 C CB  . MET B 652  ? 0.3451 0.2792 0.3063 0.0035  -0.0453 -0.0835 650  MET B CB  
13489 C CG  . MET B 652  ? 0.3905 0.3278 0.3588 0.0045  -0.0439 -0.0800 650  MET B CG  
13490 S SD  . MET B 652  ? 0.4096 0.3524 0.3813 -0.0033 -0.0443 -0.0720 650  MET B SD  
13491 C CE  . MET B 652  ? 0.3542 0.3134 0.3297 -0.0034 -0.0376 -0.0701 650  MET B CE  
13492 N N   . PRO B 653  ? 0.3945 0.2973 0.3460 0.0121  -0.0553 -0.0942 651  PRO B N   
13493 C CA  . PRO B 653  ? 0.4594 0.3506 0.4110 0.0165  -0.0591 -0.0965 651  PRO B CA  
13494 C C   . PRO B 653  ? 0.4296 0.3209 0.3812 0.0260  -0.0563 -0.1032 651  PRO B C   
13495 O O   . PRO B 653  ? 0.4557 0.3462 0.4122 0.0310  -0.0560 -0.1037 651  PRO B O   
13496 C CB  . PRO B 653  ? 0.4327 0.3077 0.3768 0.0119  -0.0669 -0.0972 651  PRO B CB  
13497 C CG  . PRO B 653  ? 0.4716 0.3520 0.4148 0.0034  -0.0672 -0.0924 651  PRO B CG  
13498 C CD  . PRO B 653  ? 0.4307 0.3267 0.3763 0.0050  -0.0603 -0.0928 651  PRO B CD  
13499 N N   . THR B 654  ? 0.4613 0.3539 0.4073 0.0289  -0.0542 -0.1083 652  THR B N   
13500 C CA  . THR B 654  ? 0.4465 0.3405 0.3923 0.0382  -0.0509 -0.1147 652  THR B CA  
13501 C C   . THR B 654  ? 0.4720 0.3826 0.4270 0.0417  -0.0436 -0.1127 652  THR B C   
13502 O O   . THR B 654  ? 0.4415 0.3539 0.4014 0.0487  -0.0418 -0.1152 652  THR B O   
13503 C CB  . THR B 654  ? 0.4287 0.3204 0.3652 0.0400  -0.0503 -0.1204 652  THR B CB  
13504 O OG1 . THR B 654  ? 0.5111 0.3856 0.4388 0.0372  -0.0580 -0.1227 652  THR B OG1 
13505 C CG2 . THR B 654  ? 0.5007 0.3959 0.4369 0.0500  -0.0458 -0.1268 652  THR B CG2 
13506 N N   . LEU B 655  ? 0.4006 0.3235 0.3586 0.0368  -0.0396 -0.1082 653  LEU B N   
13507 C CA  . LEU B 655  ? 0.3798 0.3180 0.3466 0.0390  -0.0331 -0.1057 653  LEU B CA  
13508 C C   . LEU B 655  ? 0.4226 0.3608 0.3975 0.0396  -0.0344 -0.1024 653  LEU B C   
13509 O O   . LEU B 655  ? 0.4005 0.3466 0.3824 0.0446  -0.0307 -0.1029 653  LEU B O   
13510 C CB  . LEU B 655  ? 0.3434 0.2925 0.3113 0.0331  -0.0298 -0.1010 653  LEU B CB  
13511 C CG  . LEU B 655  ? 0.4020 0.3525 0.3621 0.0320  -0.0285 -0.1034 653  LEU B CG  
13512 C CD1 . LEU B 655  ? 0.3526 0.3142 0.3147 0.0264  -0.0254 -0.0983 653  LEU B CD1 
13513 C CD2 . LEU B 655  ? 0.4113 0.3654 0.3695 0.0396  -0.0242 -0.1092 653  LEU B CD2 
13514 N N   . LEU B 656  ? 0.3996 0.3296 0.3736 0.0342  -0.0396 -0.0986 654  LEU B N   
13515 C CA  . LEU B 656  ? 0.4122 0.3402 0.3922 0.0346  -0.0417 -0.0955 654  LEU B CA  
13516 C C   . LEU B 656  ? 0.4178 0.3409 0.4000 0.0427  -0.0428 -0.1001 654  LEU B C   
13517 O O   . LEU B 656  ? 0.4337 0.3633 0.4237 0.0461  -0.0409 -0.0989 654  LEU B O   
13518 C CB  . LEU B 656  ? 0.4426 0.3597 0.4190 0.0282  -0.0479 -0.0917 654  LEU B CB  
13519 C CG  . LEU B 656  ? 0.4038 0.3267 0.3794 0.0204  -0.0469 -0.0865 654  LEU B CG  
13520 C CD1 . LEU B 656  ? 0.4458 0.3586 0.4184 0.0141  -0.0527 -0.0824 654  LEU B CD1 
13521 C CD2 . LEU B 656  ? 0.3889 0.3258 0.3720 0.0203  -0.0416 -0.0829 654  LEU B CD2 
13522 N N   . GLY B 657  ? 0.4241 0.3348 0.3994 0.0457  -0.0466 -0.1052 655  GLY B N   
13523 C CA  . GLY B 657  ? 0.4779 0.3825 0.4547 0.0539  -0.0482 -0.1098 655  GLY B CA  
13524 C C   . GLY B 657  ? 0.4606 0.3789 0.4440 0.0610  -0.0416 -0.1126 655  GLY B C   
13525 O O   . GLY B 657  ? 0.4555 0.3759 0.4458 0.0666  -0.0414 -0.1134 655  GLY B O   
13526 N N   . LEU B 658  ? 0.4235 0.3518 0.4052 0.0606  -0.0360 -0.1138 656  LEU B N   
13527 C CA  . LEU B 658  ? 0.3703 0.3128 0.3583 0.0665  -0.0292 -0.1157 656  LEU B CA  
13528 C C   . LEU B 658  ? 0.4212 0.3764 0.4200 0.0643  -0.0263 -0.1101 656  LEU B C   
13529 O O   . LEU B 658  ? 0.4222 0.3851 0.4293 0.0698  -0.0236 -0.1108 656  LEU B O   
13530 C CB  . LEU B 658  ? 0.4390 0.3881 0.4213 0.0661  -0.0245 -0.1180 656  LEU B CB  
13531 C CG  . LEU B 658  ? 0.4363 0.3984 0.4227 0.0730  -0.0174 -0.1212 656  LEU B CG  
13532 C CD1 . LEU B 658  ? 0.3755 0.3319 0.3624 0.0822  -0.0186 -0.1272 656  LEU B CD1 
13533 C CD2 . LEU B 658  ? 0.4114 0.3782 0.3902 0.0719  -0.0135 -0.1231 656  LEU B CD2 
13534 N N   . ILE B 659  ? 0.3715 0.3287 0.3704 0.0565  -0.0268 -0.1045 657  ILE B N   
13535 C CA  . ILE B 659  ? 0.3608 0.3288 0.3688 0.0543  -0.0243 -0.0994 657  ILE B CA  
13536 C C   . ILE B 659  ? 0.3965 0.3596 0.4100 0.0566  -0.0284 -0.0983 657  ILE B C   
13537 O O   . ILE B 659  ? 0.3611 0.3333 0.3836 0.0591  -0.0263 -0.0969 657  ILE B O   
13538 C CB  . ILE B 659  ? 0.3205 0.2906 0.3263 0.0460  -0.0243 -0.0941 657  ILE B CB  
13539 C CG1 . ILE B 659  ? 0.3694 0.3466 0.3713 0.0443  -0.0198 -0.0948 657  ILE B CG1 
13540 C CG2 . ILE B 659  ? 0.3338 0.3117 0.3477 0.0435  -0.0233 -0.0890 657  ILE B CG2 
13541 C CD1 . ILE B 659  ? 0.3672 0.3442 0.3655 0.0367  -0.0207 -0.0905 657  ILE B CD1 
13542 N N   . ILE B 660  ? 0.3480 0.2967 0.3562 0.0556  -0.0347 -0.0987 658  ILE B N   
13543 C CA  . ILE B 660  ? 0.3612 0.3039 0.3736 0.0575  -0.0393 -0.0972 658  ILE B CA  
13544 C C   . ILE B 660  ? 0.3570 0.3031 0.3757 0.0665  -0.0381 -0.1015 658  ILE B C   
13545 O O   . ILE B 660  ? 0.4054 0.3570 0.4325 0.0687  -0.0383 -0.0995 658  ILE B O   
13546 C CB  . ILE B 660  ? 0.3559 0.2813 0.3603 0.0547  -0.0464 -0.0969 658  ILE B CB  
13547 C CG1 . ILE B 660  ? 0.3762 0.3004 0.3771 0.0455  -0.0477 -0.0912 658  ILE B CG1 
13548 C CG2 . ILE B 660  ? 0.3546 0.2717 0.3622 0.0592  -0.0515 -0.0973 658  ILE B CG2 
13549 C CD1 . ILE B 660  ? 0.3965 0.3048 0.3891 0.0416  -0.0541 -0.0907 658  ILE B CD1 
13550 N N   . ARG B 661  ? 0.3707 0.3144 0.3855 0.0719  -0.0366 -0.1074 659  ARG B N   
13551 C CA  . ARG B 661  ? 0.3923 0.3378 0.4123 0.0813  -0.0359 -0.1120 659  ARG B CA  
13552 C C   . ARG B 661  ? 0.4041 0.3679 0.4326 0.0849  -0.0284 -0.1126 659  ARG B C   
13553 O O   . ARG B 661  ? 0.3817 0.3521 0.4193 0.0908  -0.0275 -0.1134 659  ARG B O   
13554 C CB  . ARG B 661  ? 0.4038 0.3369 0.4150 0.0864  -0.0382 -0.1185 659  ARG B CB  
13555 C CG  . ARG B 661  ? 0.4535 0.3678 0.4591 0.0854  -0.0465 -0.1185 659  ARG B CG  
13556 C CD  . ARG B 661  ? 0.4708 0.3715 0.4663 0.0894  -0.0491 -0.1251 659  ARG B CD  
13557 N NE  . ARG B 661  ? 0.5086 0.4108 0.5067 0.1003  -0.0472 -0.1315 659  ARG B NE  
13558 C CZ  . ARG B 661  ? 0.5316 0.4365 0.5250 0.1053  -0.0431 -0.1375 659  ARG B CZ  
13559 N NH1 . ARG B 661  ? 0.5292 0.4358 0.5150 0.1004  -0.0405 -0.1379 659  ARG B NH1 
13560 N NH2 . ARG B 661  ? 0.4582 0.3640 0.4541 0.1158  -0.0417 -0.1434 659  ARG B NH2 
13561 N N   . GLU B 662  ? 0.3733 0.3457 0.3992 0.0815  -0.0231 -0.1120 660  GLU B N   
13562 C CA  . GLU B 662  ? 0.3531 0.3428 0.3869 0.0845  -0.0160 -0.1120 660  GLU B CA  
13563 C C   . GLU B 662  ? 0.3512 0.3513 0.3947 0.0800  -0.0149 -0.1059 660  GLU B C   
13564 O O   . GLU B 662  ? 0.3180 0.3302 0.3716 0.0836  -0.0116 -0.1055 660  GLU B O   
13565 C CB  . GLU B 662  ? 0.3819 0.3768 0.4090 0.0828  -0.0108 -0.1136 660  GLU B CB  
13566 C CG  . GLU B 662  ? 0.3748 0.3880 0.4097 0.0845  -0.0032 -0.1125 660  GLU B CG  
13567 C CD  . GLU B 662  ? 0.3806 0.3987 0.4080 0.0836  0.0019  -0.1141 660  GLU B CD  
13568 O OE1 . GLU B 662  ? 0.3531 0.3663 0.3729 0.0772  0.0006  -0.1122 660  GLU B OE1 
13569 O OE2 . GLU B 662  ? 0.3690 0.3965 0.3984 0.0894  0.0073  -0.1173 660  GLU B OE2 
13570 N N   . ALA B 663  ? 0.3430 0.3388 0.3835 0.0724  -0.0176 -0.1013 661  ALA B N   
13571 C CA  . ALA B 663  ? 0.3293 0.3346 0.3771 0.0678  -0.0161 -0.0959 661  ALA B CA  
13572 C C   . ALA B 663  ? 0.3386 0.3383 0.3901 0.0664  -0.0217 -0.0928 661  ALA B C   
13573 O O   . ALA B 663  ? 0.3663 0.3730 0.4239 0.0631  -0.0211 -0.0887 661  ALA B O   
13574 C CB  . ALA B 663  ? 0.3379 0.3451 0.3803 0.0605  -0.0140 -0.0927 661  ALA B CB  
13575 N N   . GLY B 664  ? 0.3966 0.3834 0.4443 0.0688  -0.0272 -0.0946 662  GLY B N   
13576 C CA  . GLY B 664  ? 0.3640 0.3450 0.4146 0.0677  -0.0328 -0.0916 662  GLY B CA  
13577 C C   . GLY B 664  ? 0.3943 0.3689 0.4390 0.0598  -0.0357 -0.0869 662  GLY B C   
13578 O O   . GLY B 664  ? 0.3945 0.3672 0.4420 0.0580  -0.0393 -0.0834 662  GLY B O   
13579 N N   . LYS B 665  ? 0.3475 0.3191 0.3843 0.0552  -0.0344 -0.0866 663  LYS B N   
13580 C CA  . LYS B 665  ? 0.3748 0.3433 0.4071 0.0477  -0.0360 -0.0818 663  LYS B CA  
13581 C C   . LYS B 665  ? 0.3511 0.3047 0.3764 0.0456  -0.0422 -0.0810 663  LYS B C   
13582 O O   . LYS B 665  ? 0.3598 0.3039 0.3811 0.0488  -0.0449 -0.0846 663  LYS B O   
13583 C CB  . LYS B 665  ? 0.3462 0.3197 0.3742 0.0434  -0.0317 -0.0813 663  LYS B CB  
13584 C CG  . LYS B 665  ? 0.4081 0.3961 0.4425 0.0441  -0.0258 -0.0808 663  LYS B CG  
13585 C CD  . LYS B 665  ? 0.3663 0.3588 0.3972 0.0383  -0.0228 -0.0780 663  LYS B CD  
13586 C CE  . LYS B 665  ? 0.3670 0.3727 0.4048 0.0385  -0.0177 -0.0766 663  LYS B CE  
13587 N NZ  . LYS B 665  ? 0.3907 0.4007 0.4263 0.0330  -0.0155 -0.0731 663  LYS B NZ  
13588 N N   . SER B 666  ? 0.3764 0.3276 0.3998 0.0400  -0.0445 -0.0761 664  SER B N   
13589 C CA  . SER B 666  ? 0.4343 0.3724 0.4503 0.0363  -0.0498 -0.0742 664  SER B CA  
13590 C C   . SER B 666  ? 0.3962 0.3318 0.4052 0.0320  -0.0487 -0.0746 664  SER B C   
13591 O O   . SER B 666  ? 0.3695 0.3142 0.3790 0.0306  -0.0438 -0.0750 664  SER B O   
13592 C CB  . SER B 666  ? 0.4386 0.3762 0.4543 0.0316  -0.0520 -0.0686 664  SER B CB  
13593 O OG  . SER B 666  ? 0.4198 0.3655 0.4346 0.0266  -0.0480 -0.0658 664  SER B OG  
13594 N N   . ALA B 667  ? 0.3820 0.3047 0.3844 0.0296  -0.0537 -0.0743 665  ALA B N   
13595 C CA  . ALA B 667  ? 0.4062 0.3259 0.4020 0.0249  -0.0536 -0.0744 665  ALA B CA  
13596 C C   . ALA B 667  ? 0.4020 0.3304 0.3977 0.0185  -0.0505 -0.0696 665  ALA B C   
13597 O O   . ALA B 667  ? 0.3672 0.3011 0.3612 0.0163  -0.0473 -0.0702 665  ALA B O   
13598 C CB  . ALA B 667  ? 0.4246 0.3285 0.4138 0.0224  -0.0602 -0.0739 665  ALA B CB  
13599 N N   . LEU B 668  ? 0.3806 0.3105 0.3781 0.0159  -0.0513 -0.0649 666  LEU B N   
13600 C CA  . LEU B 668  ? 0.3761 0.3142 0.3735 0.0105  -0.0484 -0.0605 666  LEU B CA  
13601 C C   . LEU B 668  ? 0.3987 0.3497 0.4007 0.0123  -0.0424 -0.0619 666  LEU B C   
13602 O O   . LEU B 668  ? 0.3607 0.3175 0.3613 0.0090  -0.0394 -0.0607 666  LEU B O   
13603 C CB  . LEU B 668  ? 0.4685 0.4055 0.4666 0.0086  -0.0504 -0.0560 666  LEU B CB  
13604 C CG  . LEU B 668  ? 0.5204 0.4622 0.5164 0.0026  -0.0489 -0.0508 666  LEU B CG  
13605 C CD1 . LEU B 668  ? 0.5104 0.4464 0.5007 -0.0030 -0.0512 -0.0486 666  LEU B CD1 
13606 C CD2 . LEU B 668  ? 0.5253 0.4654 0.5216 0.0025  -0.0510 -0.0475 666  LEU B CD2 
13607 N N   . ASN B 669  ? 0.3385 0.2943 0.3464 0.0175  -0.0406 -0.0641 667  ASN B N   
13608 C CA  . ASN B 669  ? 0.3196 0.2873 0.3321 0.0191  -0.0351 -0.0651 667  ASN B CA  
13609 C C   . ASN B 669  ? 0.3309 0.3006 0.3417 0.0209  -0.0325 -0.0690 667  ASN B C   
13610 O O   . ASN B 669  ? 0.3184 0.2968 0.3301 0.0199  -0.0282 -0.0687 667  ASN B O   
13611 C CB  . ASN B 669  ? 0.3711 0.3438 0.3910 0.0237  -0.0343 -0.0661 667  ASN B CB  
13612 C CG  . ASN B 669  ? 0.3612 0.3338 0.3827 0.0218  -0.0364 -0.0621 667  ASN B CG  
13613 O OD1 . ASN B 669  ? 0.4669 0.4373 0.4919 0.0249  -0.0390 -0.0625 667  ASN B OD1 
13614 N ND2 . ASN B 669  ? 0.3778 0.3528 0.3964 0.0169  -0.0352 -0.0585 667  ASN B ND2 
13615 N N   . ALA B 670  ? 0.2930 0.2544 0.3007 0.0238  -0.0352 -0.0728 668  ALA B N   
13616 C CA  . ALA B 670  ? 0.3489 0.3113 0.3534 0.0255  -0.0329 -0.0767 668  ALA B CA  
13617 C C   . ALA B 670  ? 0.3170 0.2788 0.3158 0.0196  -0.0330 -0.0748 668  ALA B C   
13618 O O   . ALA B 670  ? 0.2886 0.2566 0.2861 0.0195  -0.0295 -0.0762 668  ALA B O   
13619 C CB  . ALA B 670  ? 0.3384 0.2907 0.3401 0.0303  -0.0363 -0.0816 668  ALA B CB  
13620 N N   . ILE B 671  ? 0.3348 0.2897 0.3302 0.0146  -0.0370 -0.0714 669  ILE B N   
13621 C CA  . ILE B 671  ? 0.3206 0.2764 0.3118 0.0086  -0.0371 -0.0689 669  ILE B CA  
13622 C C   . ILE B 671  ? 0.2893 0.2578 0.2840 0.0070  -0.0321 -0.0662 669  ILE B C   
13623 O O   . ILE B 671  ? 0.3281 0.3014 0.3208 0.0054  -0.0298 -0.0665 669  ILE B O   
13624 C CB  . ILE B 671  ? 0.3641 0.3119 0.3523 0.0034  -0.0419 -0.0649 669  ILE B CB  
13625 C CG1 . ILE B 671  ? 0.3615 0.2953 0.3450 0.0043  -0.0474 -0.0678 669  ILE B CG1 
13626 C CG2 . ILE B 671  ? 0.3540 0.3061 0.3399 -0.0030 -0.0412 -0.0613 669  ILE B CG2 
13627 C CD1 . ILE B 671  ? 0.4381 0.3626 0.4192 -0.0001 -0.0526 -0.0637 669  ILE B CD1 
13628 N N   . ALA B 672  ? 0.2896 0.2630 0.2891 0.0075  -0.0305 -0.0635 670  ALA B N   
13629 C CA  . ALA B 672  ? 0.3110 0.2952 0.3136 0.0061  -0.0262 -0.0610 670  ALA B CA  
13630 C C   . ALA B 672  ? 0.3056 0.2971 0.3102 0.0094  -0.0219 -0.0638 670  ALA B C   
13631 O O   . ALA B 672  ? 0.3136 0.3122 0.3183 0.0076  -0.0188 -0.0624 670  ALA B O   
13632 C CB  . ALA B 672  ? 0.3432 0.3300 0.3502 0.0067  -0.0259 -0.0584 670  ALA B CB  
13633 N N   . GLU B 673  ? 0.2693 0.2595 0.2758 0.0144  -0.0216 -0.0677 671  GLU B N   
13634 C CA  . GLU B 673  ? 0.3196 0.3174 0.3280 0.0175  -0.0172 -0.0702 671  GLU B CA  
13635 C C   . GLU B 673  ? 0.2768 0.2738 0.2790 0.0161  -0.0167 -0.0719 671  GLU B C   
13636 O O   . GLU B 673  ? 0.2909 0.2956 0.2931 0.0153  -0.0130 -0.0711 671  GLU B O   
13637 C CB  . GLU B 673  ? 0.3162 0.3133 0.3280 0.0235  -0.0169 -0.0740 671  GLU B CB  
13638 C CG  . GLU B 673  ? 0.3266 0.3308 0.3388 0.0268  -0.0123 -0.0770 671  GLU B CG  
13639 C CD  . GLU B 673  ? 0.4039 0.4156 0.4241 0.0312  -0.0094 -0.0777 671  GLU B CD  
13640 O OE1 . GLU B 673  ? 0.4163 0.4249 0.4407 0.0334  -0.0119 -0.0779 671  GLU B OE1 
13641 O OE2 . GLU B 673  ? 0.3333 0.3541 0.3556 0.0322  -0.0047 -0.0778 671  GLU B OE2 
13642 N N   . VAL B 674  ? 0.2600 0.2473 0.2565 0.0155  -0.0207 -0.0741 672  VAL B N   
13643 C CA  . VAL B 674  ? 0.3088 0.2943 0.2987 0.0138  -0.0211 -0.0758 672  VAL B CA  
13644 C C   . VAL B 674  ? 0.2900 0.2804 0.2792 0.0080  -0.0206 -0.0714 672  VAL B C   
13645 O O   . VAL B 674  ? 0.2667 0.2626 0.2538 0.0072  -0.0183 -0.0715 672  VAL B O   
13646 C CB  . VAL B 674  ? 0.2967 0.2694 0.2807 0.0138  -0.0265 -0.0790 672  VAL B CB  
13647 C CG1 . VAL B 674  ? 0.3141 0.2844 0.2909 0.0116  -0.0276 -0.0809 672  VAL B CG1 
13648 C CG2 . VAL B 674  ? 0.3344 0.3027 0.3192 0.0205  -0.0266 -0.0838 672  VAL B CG2 
13649 N N   . ARG B 675  ? 0.2767 0.2658 0.2677 0.0043  -0.0227 -0.0672 673  ARG B N   
13650 C CA  . ARG B 675  ? 0.2898 0.2850 0.2810 -0.0004 -0.0217 -0.0630 673  ARG B CA  
13651 C C   . ARG B 675  ? 0.2638 0.2697 0.2588 0.0011  -0.0166 -0.0617 673  ARG B C   
13652 O O   . ARG B 675  ? 0.2675 0.2788 0.2613 -0.0011 -0.0151 -0.0600 673  ARG B O   
13653 C CB  . ARG B 675  ? 0.2610 0.2543 0.2538 -0.0039 -0.0238 -0.0587 673  ARG B CB  
13654 C CG  . ARG B 675  ? 0.2680 0.2510 0.2570 -0.0069 -0.0291 -0.0584 673  ARG B CG  
13655 C CD  . ARG B 675  ? 0.3318 0.3162 0.3225 -0.0110 -0.0300 -0.0531 673  ARG B CD  
13656 N NE  . ARG B 675  ? 0.3059 0.2993 0.2976 -0.0142 -0.0276 -0.0498 673  ARG B NE  
13657 C CZ  . ARG B 675  ? 0.3178 0.3163 0.3117 -0.0164 -0.0262 -0.0455 673  ARG B CZ  
13658 N NH1 . ARG B 675  ? 0.2708 0.2663 0.2656 -0.0162 -0.0271 -0.0438 673  ARG B NH1 
13659 N NH2 . ARG B 675  ? 0.3003 0.3071 0.2952 -0.0187 -0.0241 -0.0429 673  ARG B NH2 
13660 N N   . GLU B 676  ? 0.2677 0.2766 0.2676 0.0045  -0.0142 -0.0622 674  GLU B N   
13661 C CA  . GLU B 676  ? 0.2738 0.2920 0.2774 0.0056  -0.0098 -0.0607 674  GLU B CA  
13662 C C   . GLU B 676  ? 0.2578 0.2798 0.2588 0.0073  -0.0072 -0.0631 674  GLU B C   
13663 O O   . GLU B 676  ? 0.2491 0.2776 0.2502 0.0060  -0.0047 -0.0611 674  GLU B O   
13664 C CB  . GLU B 676  ? 0.2973 0.3177 0.3069 0.0086  -0.0084 -0.0608 674  GLU B CB  
13665 C CG  . GLU B 676  ? 0.3076 0.3367 0.3214 0.0091  -0.0043 -0.0589 674  GLU B CG  
13666 C CD  . GLU B 676  ? 0.4705 0.5013 0.4907 0.0113  -0.0038 -0.0586 674  GLU B CD  
13667 O OE1 . GLU B 676  ? 0.4887 0.5141 0.5098 0.0123  -0.0068 -0.0594 674  GLU B OE1 
13668 O OE2 . GLU B 676  ? 0.4644 0.5017 0.4887 0.0119  -0.0009 -0.0573 674  GLU B OE2 
13669 N N   . ALA B 677  ? 0.2421 0.2599 0.2404 0.0103  -0.0078 -0.0674 675  ALA B N   
13670 C CA  . ALA B 677  ? 0.2679 0.2888 0.2622 0.0120  -0.0055 -0.0700 675  ALA B CA  
13671 C C   . ALA B 677  ? 0.2655 0.2861 0.2542 0.0080  -0.0070 -0.0687 675  ALA B C   
13672 O O   . ALA B 677  ? 0.2506 0.2775 0.2379 0.0077  -0.0043 -0.0677 675  ALA B O   
13673 C CB  . ALA B 677  ? 0.2639 0.2788 0.2549 0.0162  -0.0065 -0.0753 675  ALA B CB  
13674 N N   . ILE B 678  ? 0.2757 0.2890 0.2612 0.0049  -0.0116 -0.0685 676  ILE B N   
13675 C CA  . ILE B 678  ? 0.2089 0.2223 0.1901 0.0005  -0.0137 -0.0669 676  ILE B CA  
13676 C C   . ILE B 678  ? 0.2427 0.2650 0.2279 -0.0019 -0.0113 -0.0620 676  ILE B C   
13677 O O   . ILE B 678  ? 0.2423 0.2694 0.2253 -0.0032 -0.0104 -0.0609 676  ILE B O   
13678 C CB  . ILE B 678  ? 0.2457 0.2503 0.2246 -0.0030 -0.0192 -0.0666 676  ILE B CB  
13679 C CG1 . ILE B 678  ? 0.3109 0.3053 0.2848 -0.0003 -0.0221 -0.0719 676  ILE B CG1 
13680 C CG2 . ILE B 678  ? 0.2343 0.2405 0.2106 -0.0083 -0.0216 -0.0638 676  ILE B CG2 
13681 C CD1 . ILE B 678  ? 0.2693 0.2537 0.2422 -0.0030 -0.0273 -0.0714 676  ILE B CD1 
13682 N N   . ASP B 679  ? 0.2321 0.2563 0.2228 -0.0022 -0.0105 -0.0591 677  ASP B N   
13683 C CA  . ASP B 679  ? 0.2693 0.3010 0.2635 -0.0039 -0.0083 -0.0548 677  ASP B CA  
13684 C C   . ASP B 679  ? 0.2363 0.2750 0.2317 -0.0016 -0.0042 -0.0546 677  ASP B C   
13685 O O   . ASP B 679  ? 0.2180 0.2621 0.2132 -0.0031 -0.0031 -0.0520 677  ASP B O   
13686 C CB  . ASP B 679  ? 0.2352 0.2666 0.2341 -0.0039 -0.0082 -0.0525 677  ASP B CB  
13687 C CG  . ASP B 679  ? 0.2957 0.3219 0.2935 -0.0072 -0.0119 -0.0510 677  ASP B CG  
13688 O OD1 . ASP B 679  ? 0.3085 0.3339 0.3033 -0.0104 -0.0142 -0.0503 677  ASP B OD1 
13689 O OD2 . ASP B 679  ? 0.3352 0.3583 0.3351 -0.0068 -0.0128 -0.0504 677  ASP B OD2 
13690 N N   . PHE B 680  ? 0.2281 0.2673 0.2251 0.0020  -0.0018 -0.0569 678  PHE B N   
13691 C CA  . PHE B 680  ? 0.2375 0.2834 0.2355 0.0038  0.0022  -0.0564 678  PHE B CA  
13692 C C   . PHE B 680  ? 0.2361 0.2836 0.2280 0.0030  0.0023  -0.0571 678  PHE B C   
13693 O O   . PHE B 680  ? 0.2273 0.2804 0.2191 0.0022  0.0042  -0.0545 678  PHE B O   
13694 C CB  . PHE B 680  ? 0.1977 0.2443 0.1983 0.0076  0.0046  -0.0591 678  PHE B CB  
13695 C CG  . PHE B 680  ? 0.2280 0.2766 0.2357 0.0085  0.0058  -0.0573 678  PHE B CG  
13696 C CD1 . PHE B 680  ? 0.2155 0.2686 0.2266 0.0071  0.0073  -0.0535 678  PHE B CD1 
13697 C CD2 . PHE B 680  ? 0.2413 0.2869 0.2521 0.0110  0.0051  -0.0596 678  PHE B CD2 
13698 C CE1 . PHE B 680  ? 0.2480 0.3023 0.2652 0.0078  0.0079  -0.0522 678  PHE B CE1 
13699 C CE2 . PHE B 680  ? 0.2519 0.2993 0.2691 0.0117  0.0056  -0.0581 678  PHE B CE2 
13700 C CZ  . PHE B 680  ? 0.2557 0.3072 0.2759 0.0099  0.0070  -0.0545 678  PHE B CZ  
13701 N N   . LEU B 681  ? 0.2254 0.2674 0.2119 0.0034  0.0000  -0.0609 679  LEU B N   
13702 C CA  . LEU B 681  ? 0.2141 0.2567 0.1937 0.0028  -0.0005 -0.0621 679  LEU B CA  
13703 C C   . LEU B 681  ? 0.2666 0.3118 0.2455 -0.0013 -0.0026 -0.0584 679  LEU B C   
13704 O O   . LEU B 681  ? 0.2264 0.2766 0.2030 -0.0018 -0.0013 -0.0568 679  LEU B O   
13705 C CB  . LEU B 681  ? 0.2558 0.2901 0.2291 0.0036  -0.0037 -0.0670 679  LEU B CB  
13706 C CG  . LEU B 681  ? 0.2968 0.3288 0.2695 0.0085  -0.0017 -0.0715 679  LEU B CG  
13707 C CD1 . LEU B 681  ? 0.2677 0.2891 0.2361 0.0091  -0.0061 -0.0758 679  LEU B CD1 
13708 C CD2 . LEU B 681  ? 0.2552 0.2922 0.2234 0.0112  0.0020  -0.0733 679  LEU B CD2 
13709 N N   . ARG B 682  ? 0.2182 0.2603 0.1991 -0.0043 -0.0058 -0.0567 680  ARG B N   
13710 C CA  . ARG B 682  ? 0.2606 0.3062 0.2417 -0.0080 -0.0078 -0.0531 680  ARG B CA  
13711 C C   . ARG B 682  ? 0.2384 0.2915 0.2248 -0.0078 -0.0048 -0.0489 680  ARG B C   
13712 O O   . ARG B 682  ? 0.2595 0.3175 0.2454 -0.0093 -0.0050 -0.0462 680  ARG B O   
13713 C CB  . ARG B 682  ? 0.2258 0.2667 0.2079 -0.0114 -0.0118 -0.0523 680  ARG B CB  
13714 C CG  . ARG B 682  ? 0.2573 0.2900 0.2332 -0.0129 -0.0161 -0.0560 680  ARG B CG  
13715 C CD  . ARG B 682  ? 0.2723 0.3002 0.2497 -0.0166 -0.0200 -0.0545 680  ARG B CD  
13716 N NE  . ARG B 682  ? 0.2576 0.2767 0.2291 -0.0184 -0.0247 -0.0577 680  ARG B NE  
13717 C CZ  . ARG B 682  ? 0.2814 0.2930 0.2527 -0.0208 -0.0285 -0.0578 680  ARG B CZ  
13718 N NH1 . ARG B 682  ? 0.2858 0.2983 0.2623 -0.0221 -0.0281 -0.0544 680  ARG B NH1 
13719 N NH2 . ARG B 682  ? 0.2823 0.2845 0.2475 -0.0219 -0.0330 -0.0614 680  ARG B NH2 
13720 N N   . TYR B 683  ? 0.2536 0.3072 0.2448 -0.0057 -0.0023 -0.0483 681  TYR B N   
13721 C CA  . TYR B 683  ? 0.2459 0.3053 0.2415 -0.0053 0.0003  -0.0447 681  TYR B CA  
13722 C C   . TYR B 683  ? 0.2335 0.2975 0.2275 -0.0038 0.0029  -0.0440 681  TYR B C   
13723 O O   . TYR B 683  ? 0.2291 0.2977 0.2235 -0.0046 0.0032  -0.0409 681  TYR B O   
13724 C CB  . TYR B 683  ? 0.2520 0.3101 0.2525 -0.0036 0.0018  -0.0445 681  TYR B CB  
13725 C CG  . TYR B 683  ? 0.2318 0.2946 0.2363 -0.0029 0.0041  -0.0413 681  TYR B CG  
13726 C CD1 . TYR B 683  ? 0.2389 0.3038 0.2453 -0.0041 0.0033  -0.0383 681  TYR B CD1 
13727 C CD2 . TYR B 683  ? 0.2145 0.2794 0.2208 -0.0008 0.0070  -0.0411 681  TYR B CD2 
13728 C CE1 . TYR B 683  ? 0.2443 0.3124 0.2537 -0.0030 0.0052  -0.0357 681  TYR B CE1 
13729 C CE2 . TYR B 683  ? 0.2250 0.2929 0.2346 -0.0003 0.0086  -0.0382 681  TYR B CE2 
13730 C CZ  . TYR B 683  ? 0.2590 0.3279 0.2698 -0.0012 0.0075  -0.0357 681  TYR B CZ  
13731 O OH  . TYR B 683  ? 0.2392 0.3100 0.2526 -0.0002 0.0088  -0.0332 681  TYR B OH  
13732 N N   . TYR B 684  ? 0.2280 0.2912 0.2201 -0.0016 0.0049  -0.0467 682  TYR B N   
13733 C CA  . TYR B 684  ? 0.2403 0.3082 0.2307 -0.0004 0.0078  -0.0456 682  TYR B CA  
13734 C C   . TYR B 684  ? 0.2582 0.3272 0.2421 -0.0018 0.0061  -0.0455 682  TYR B C   
13735 O O   . TYR B 684  ? 0.2424 0.3159 0.2251 -0.0019 0.0075  -0.0428 682  TYR B O   
13736 C CB  . TYR B 684  ? 0.2604 0.3285 0.2509 0.0024  0.0109  -0.0482 682  TYR B CB  
13737 C CG  . TYR B 684  ? 0.2396 0.3077 0.2371 0.0037  0.0125  -0.0477 682  TYR B CG  
13738 C CD1 . TYR B 684  ? 0.2461 0.3164 0.2486 0.0029  0.0131  -0.0441 682  TYR B CD1 
13739 C CD2 . TYR B 684  ? 0.2285 0.2942 0.2274 0.0059  0.0131  -0.0511 682  TYR B CD2 
13740 C CE1 . TYR B 684  ? 0.2419 0.3118 0.2504 0.0039  0.0141  -0.0439 682  TYR B CE1 
13741 C CE2 . TYR B 684  ? 0.2213 0.2874 0.2268 0.0070  0.0140  -0.0506 682  TYR B CE2 
13742 C CZ  . TYR B 684  ? 0.2247 0.2927 0.2348 0.0057  0.0144  -0.0470 682  TYR B CZ  
13743 O OH  . TYR B 684  ? 0.2394 0.3072 0.2556 0.0066  0.0148  -0.0468 682  TYR B OH  
13744 N N   . ALA B 685  ? 0.2298 0.2945 0.2095 -0.0032 0.0027  -0.0482 683  ALA B N   
13745 C CA  . ALA B 685  ? 0.2619 0.3274 0.2360 -0.0052 0.0000  -0.0479 683  ALA B CA  
13746 C C   . ALA B 685  ? 0.2695 0.3399 0.2470 -0.0074 -0.0012 -0.0431 683  ALA B C   
13747 O O   . ALA B 685  ? 0.2205 0.2952 0.1959 -0.0077 -0.0010 -0.0408 683  ALA B O   
13748 C CB  . ALA B 685  ? 0.2250 0.2839 0.1948 -0.0068 -0.0042 -0.0514 683  ALA B CB  
13749 N N   . GLU B 686  ? 0.2246 0.2947 0.2077 -0.0087 -0.0023 -0.0414 684  GLU B N   
13750 C CA  . GLU B 686  ? 0.2658 0.3412 0.2526 -0.0101 -0.0031 -0.0371 684  GLU B CA  
13751 C C   . GLU B 686  ? 0.2648 0.3446 0.2545 -0.0079 0.0001  -0.0342 684  GLU B C   
13752 O O   . GLU B 686  ? 0.2551 0.3395 0.2447 -0.0082 -0.0004 -0.0312 684  GLU B O   
13753 C CB  . GLU B 686  ? 0.3016 0.3761 0.2933 -0.0116 -0.0044 -0.0361 684  GLU B CB  
13754 C CG  . GLU B 686  ? 0.3160 0.3967 0.3124 -0.0121 -0.0043 -0.0318 684  GLU B CG  
13755 C CD  . GLU B 686  ? 0.4032 0.4887 0.3983 -0.0144 -0.0072 -0.0297 684  GLU B CD  
13756 O OE1 . GLU B 686  ? 0.4234 0.5066 0.4133 -0.0163 -0.0100 -0.0318 684  GLU B OE1 
13757 O OE2 . GLU B 686  ? 0.3779 0.4693 0.3771 -0.0142 -0.0070 -0.0262 684  GLU B OE2 
13758 N N   . GLN B 687  ? 0.2304 0.3087 0.2226 -0.0057 0.0032  -0.0349 685  GLN B N   
13759 C CA  . GLN B 687  ? 0.2326 0.3140 0.2273 -0.0040 0.0060  -0.0320 685  GLN B CA  
13760 C C   . GLN B 687  ? 0.2418 0.3258 0.2317 -0.0038 0.0067  -0.0311 685  GLN B C   
13761 O O   . GLN B 687  ? 0.2402 0.3275 0.2308 -0.0034 0.0072  -0.0275 685  GLN B O   
13762 C CB  . GLN B 687  ? 0.2607 0.3399 0.2588 -0.0023 0.0086  -0.0331 685  GLN B CB  
13763 C CG  . GLN B 687  ? 0.2249 0.3017 0.2276 -0.0024 0.0078  -0.0333 685  GLN B CG  
13764 C CD  . GLN B 687  ? 0.2676 0.3470 0.2732 -0.0025 0.0073  -0.0299 685  GLN B CD  
13765 O OE1 . GLN B 687  ? 0.2694 0.3508 0.2764 -0.0013 0.0087  -0.0275 685  GLN B OE1 
13766 N NE2 . GLN B 687  ? 0.2811 0.3607 0.2875 -0.0038 0.0053  -0.0297 685  GLN B NE2 
13767 N N   . THR B 688  ? 0.2115 0.2939 0.1958 -0.0037 0.0068  -0.0342 686  THR B N   
13768 C CA  . THR B 688  ? 0.2460 0.3308 0.2242 -0.0036 0.0072  -0.0335 686  THR B CA  
13769 C C   . THR B 688  ? 0.2332 0.3205 0.2092 -0.0054 0.0038  -0.0311 686  THR B C   
13770 O O   . THR B 688  ? 0.2542 0.3451 0.2292 -0.0052 0.0041  -0.0277 686  THR B O   
13771 C CB  . THR B 688  ? 0.2470 0.3290 0.2188 -0.0030 0.0076  -0.0380 686  THR B CB  
13772 O OG1 . THR B 688  ? 0.2615 0.3425 0.2360 -0.0009 0.0111  -0.0398 686  THR B OG1 
13773 C CG2 . THR B 688  ? 0.2639 0.3484 0.2281 -0.0029 0.0080  -0.0373 686  THR B CG2 
13774 N N   . ARG B 689  ? 0.2484 0.3342 0.2242 -0.0074 0.0002  -0.0326 687  ARG B N   
13775 C CA  . ARG B 689  ? 0.2705 0.3598 0.2454 -0.0094 -0.0034 -0.0301 687  ARG B CA  
13776 C C   . ARG B 689  ? 0.2890 0.3831 0.2700 -0.0087 -0.0028 -0.0254 687  ARG B C   
13777 O O   . ARG B 689  ? 0.2747 0.3730 0.2549 -0.0092 -0.0048 -0.0224 687  ARG B O   
13778 C CB  . ARG B 689  ? 0.2655 0.3526 0.2406 -0.0122 -0.0073 -0.0320 687  ARG B CB  
13779 C CG  . ARG B 689  ? 0.2815 0.3638 0.2487 -0.0134 -0.0097 -0.0363 687  ARG B CG  
13780 C CD  . ARG B 689  ? 0.3303 0.4101 0.2980 -0.0169 -0.0144 -0.0374 687  ARG B CD  
13781 N NE  . ARG B 689  ? 0.2867 0.3641 0.2604 -0.0172 -0.0136 -0.0376 687  ARG B NE  
13782 C CZ  . ARG B 689  ? 0.3166 0.3872 0.2887 -0.0168 -0.0136 -0.0414 687  ARG B CZ  
13783 N NH1 . ARG B 689  ? 0.3152 0.3806 0.2802 -0.0156 -0.0138 -0.0457 687  ARG B NH1 
13784 N NH2 . ARG B 689  ? 0.3102 0.3789 0.2875 -0.0175 -0.0136 -0.0409 687  ARG B NH2 
13785 N N   . ARG B 690  ? 0.2409 0.3344 0.2279 -0.0072 -0.0004 -0.0246 688  ARG B N   
13786 C CA  . ARG B 690  ? 0.2703 0.3674 0.2626 -0.0058 0.0003  -0.0207 688  ARG B CA  
13787 C C   . ARG B 690  ? 0.2833 0.3810 0.2747 -0.0038 0.0026  -0.0182 688  ARG B C   
13788 O O   . ARG B 690  ? 0.2892 0.3895 0.2835 -0.0026 0.0023  -0.0146 688  ARG B O   
13789 C CB  . ARG B 690  ? 0.2368 0.3322 0.2349 -0.0050 0.0016  -0.0211 688  ARG B CB  
13790 C CG  . ARG B 690  ? 0.3080 0.4035 0.3080 -0.0071 -0.0007 -0.0222 688  ARG B CG  
13791 C CD  . ARG B 690  ? 0.3225 0.4241 0.3257 -0.0078 -0.0028 -0.0190 688  ARG B CD  
13792 N NE  . ARG B 690  ? 0.3274 0.4314 0.3353 -0.0050 -0.0009 -0.0164 688  ARG B NE  
13793 C CZ  . ARG B 690  ? 0.3668 0.4746 0.3757 -0.0031 -0.0010 -0.0134 688  ARG B CZ  
13794 N NH1 . ARG B 690  ? 0.3561 0.4667 0.3618 -0.0041 -0.0031 -0.0121 688  ARG B NH1 
13795 N NH2 . ARG B 690  ? 0.3175 0.4258 0.3302 -0.0001 0.0007  -0.0116 688  ARG B NH2 
13796 N N   . THR B 691  ? 0.2626 0.3580 0.2502 -0.0034 0.0049  -0.0196 689  THR B N   
13797 C CA  . THR B 691  ? 0.2973 0.3930 0.2856 -0.0020 0.0074  -0.0167 689  THR B CA  
13798 C C   . THR B 691  ? 0.3217 0.4185 0.3034 -0.0022 0.0085  -0.0158 689  THR B C   
13799 O O   . THR B 691  ? 0.3499 0.4482 0.3309 -0.0017 0.0087  -0.0119 689  THR B O   
13800 C CB  . THR B 691  ? 0.2811 0.3737 0.2736 -0.0010 0.0103  -0.0179 689  THR B CB  
13801 O OG1 . THR B 691  ? 0.2532 0.3440 0.2433 -0.0014 0.0115  -0.0219 689  THR B OG1 
13802 C CG2 . THR B 691  ? 0.2837 0.3750 0.2822 -0.0004 0.0095  -0.0182 689  THR B CG2 
13803 N N   . LEU B 692  ? 0.3241 0.4199 0.3007 -0.0027 0.0093  -0.0193 690  LEU B N   
13804 C CA  . LEU B 692  ? 0.2709 0.3679 0.2415 -0.0024 0.0117  -0.0186 690  LEU B CA  
13805 C C   . LEU B 692  ? 0.2992 0.3985 0.2630 -0.0032 0.0093  -0.0166 690  LEU B C   
13806 O O   . LEU B 692  ? 0.2926 0.3919 0.2529 -0.0042 0.0059  -0.0186 690  LEU B O   
13807 C CB  . LEU B 692  ? 0.2768 0.3722 0.2439 -0.0020 0.0138  -0.0234 690  LEU B CB  
13808 C CG  . LEU B 692  ? 0.2987 0.3924 0.2726 -0.0010 0.0164  -0.0251 690  LEU B CG  
13809 C CD1 . LEU B 692  ? 0.2818 0.3751 0.2527 0.0002  0.0191  -0.0292 690  LEU B CD1 
13810 C CD2 . LEU B 692  ? 0.2628 0.3575 0.2424 -0.0008 0.0185  -0.0209 690  LEU B CD2 
13811 N N   . GLY B 693  ? 0.3345 0.4356 0.2962 -0.0029 0.0107  -0.0124 691  GLY B N   
13812 C CA  . GLY B 693  ? 0.3495 0.4528 0.3040 -0.0034 0.0087  -0.0099 691  GLY B CA  
13813 C C   . GLY B 693  ? 0.3837 0.4882 0.3319 -0.0033 0.0122  -0.0086 691  GLY B C   
13814 O O   . GLY B 693  ? 0.3578 0.4620 0.3075 -0.0027 0.0163  -0.0101 691  GLY B O   
13815 N N   . PRO B 694  ? 0.3869 0.4933 0.3280 -0.0037 0.0108  -0.0054 692  PRO B N   
13816 C CA  . PRO B 694  ? 0.3944 0.5025 0.3278 -0.0037 0.0144  -0.0043 692  PRO B CA  
13817 C C   . PRO B 694  ? 0.4108 0.5195 0.3488 -0.0037 0.0186  -0.0002 692  PRO B C   
13818 O O   . PRO B 694  ? 0.4121 0.5228 0.3468 -0.0037 0.0229  -0.0006 692  PRO B O   
13819 C CB  . PRO B 694  ? 0.4276 0.5371 0.3525 -0.0043 0.0110  -0.0012 692  PRO B CB  
13820 C CG  . PRO B 694  ? 0.4380 0.5473 0.3686 -0.0045 0.0060  0.0007  692  PRO B CG  
13821 C CD  . PRO B 694  ? 0.3997 0.5072 0.3391 -0.0042 0.0058  -0.0030 692  PRO B CD  
13822 N N   . GLY B 695  ? 0.3993 0.5065 0.3449 -0.0037 0.0174  0.0037  693  GLY B N   
13823 C CA  . GLY B 695  ? 0.3558 0.4626 0.3062 -0.0042 0.0207  0.0075  693  GLY B CA  
13824 C C   . GLY B 695  ? 0.4087 0.5148 0.3663 -0.0040 0.0239  0.0045  693  GLY B C   
13825 O O   . GLY B 695  ? 0.3735 0.4796 0.3355 -0.0048 0.0264  0.0076  693  GLY B O   
13826 N N   . HIS B 696  ? 0.3660 0.4715 0.3254 -0.0031 0.0234  -0.0013 694  HIS B N   
13827 C CA  . HIS B 696  ? 0.3669 0.4717 0.3329 -0.0028 0.0261  -0.0044 694  HIS B CA  
13828 C C   . HIS B 696  ? 0.3986 0.5065 0.3597 -0.0022 0.0297  -0.0078 694  HIS B C   
13829 O O   . HIS B 696  ? 0.3831 0.4901 0.3420 -0.0011 0.0292  -0.0132 694  HIS B O   
13830 C CB  . HIS B 696  ? 0.3441 0.4457 0.3152 -0.0020 0.0233  -0.0082 694  HIS B CB  
13831 C CG  . HIS B 696  ? 0.3470 0.4467 0.3216 -0.0020 0.0198  -0.0052 694  HIS B CG  
13832 N ND1 . HIS B 696  ? 0.3478 0.4477 0.3203 -0.0018 0.0160  -0.0061 694  HIS B ND1 
13833 C CD2 . HIS B 696  ? 0.3118 0.4096 0.2917 -0.0018 0.0194  -0.0014 694  HIS B CD2 
13834 C CE1 . HIS B 696  ? 0.3345 0.4334 0.3113 -0.0012 0.0139  -0.0029 694  HIS B CE1 
13835 N NE2 . HIS B 696  ? 0.3237 0.4207 0.3045 -0.0010 0.0159  -0.0002 694  HIS B NE2 
13836 N N   . GLY B 697  ? 0.3947 0.5061 0.3540 -0.0029 0.0335  -0.0045 695  GLY B N   
13837 C CA  . GLY B 697  ? 0.3769 0.4925 0.3308 -0.0020 0.0375  -0.0070 695  GLY B CA  
13838 C C   . GLY B 697  ? 0.3334 0.4500 0.2939 -0.0008 0.0403  -0.0110 695  GLY B C   
13839 O O   . GLY B 697  ? 0.3321 0.4477 0.3020 -0.0015 0.0404  -0.0098 695  GLY B O   
13840 N N   . PRO B 698  ? 0.3610 0.4794 0.3165 0.0013  0.0423  -0.0161 696  PRO B N   
13841 C CA  . PRO B 698  ? 0.3355 0.4552 0.2973 0.0030  0.0449  -0.0202 696  PRO B CA  
13842 C C   . PRO B 698  ? 0.3045 0.4306 0.2719 0.0023  0.0499  -0.0165 696  PRO B C   
13843 O O   . PRO B 698  ? 0.2869 0.4170 0.2511 0.0008  0.0523  -0.0115 696  PRO B O   
13844 C CB  . PRO B 698  ? 0.3633 0.4833 0.3164 0.0058  0.0457  -0.0261 696  PRO B CB  
13845 C CG  . PRO B 698  ? 0.3629 0.4852 0.3054 0.0051  0.0465  -0.0235 696  PRO B CG  
13846 C CD  . PRO B 698  ? 0.3813 0.5003 0.3249 0.0024  0.0421  -0.0187 696  PRO B CD  
13847 N N   . LEU B 699  ? 0.2810 0.4083 0.2570 0.0034  0.0513  -0.0189 697  LEU B N   
13848 C CA  . LEU B 699  ? 0.2839 0.4184 0.2663 0.0028  0.0561  -0.0160 697  LEU B CA  
13849 C C   . LEU B 699  ? 0.2946 0.4362 0.2711 0.0053  0.0613  -0.0183 697  LEU B C   
13850 O O   . LEU B 699  ? 0.3079 0.4568 0.2844 0.0041  0.0657  -0.0139 697  LEU B O   
13851 C CB  . LEU B 699  ? 0.2832 0.4170 0.2771 0.0032  0.0555  -0.0179 697  LEU B CB  
13852 C CG  . LEU B 699  ? 0.3378 0.4646 0.3379 0.0013  0.0508  -0.0164 697  LEU B CG  
13853 C CD1 . LEU B 699  ? 0.3058 0.4326 0.3158 0.0023  0.0505  -0.0192 697  LEU B CD1 
13854 C CD2 . LEU B 699  ? 0.3476 0.4745 0.3502 -0.0022 0.0505  -0.0094 697  LEU B CD2 
13855 N N   . GLY B 700  ? 0.3062 0.4456 0.2773 0.0089  0.0607  -0.0251 698  GLY B N   
13856 C CA  . GLY B 700  ? 0.2721 0.4176 0.2382 0.0123  0.0656  -0.0286 698  GLY B CA  
13857 C C   . GLY B 700  ? 0.3008 0.4453 0.2728 0.0159  0.0657  -0.0347 698  GLY B C   
13858 O O   . GLY B 700  ? 0.3098 0.4475 0.2867 0.0156  0.0612  -0.0368 698  GLY B O   
13859 N N   . PRO B 701  ? 0.3142 0.4659 0.2861 0.0195  0.0708  -0.0374 699  PRO B N   
13860 C CA  . PRO B 701  ? 0.3038 0.4545 0.2811 0.0236  0.0707  -0.0435 699  PRO B CA  
13861 C C   . PRO B 701  ? 0.2864 0.4359 0.2774 0.0217  0.0684  -0.0416 699  PRO B C   
13862 O O   . PRO B 701  ? 0.2970 0.4524 0.2965 0.0188  0.0703  -0.0361 699  PRO B O   
13863 C CB  . PRO B 701  ? 0.3394 0.5011 0.3165 0.0273  0.0778  -0.0446 699  PRO B CB  
13864 C CG  . PRO B 701  ? 0.3249 0.4900 0.2903 0.0262  0.0806  -0.0418 699  PRO B CG  
13865 C CD  . PRO B 701  ? 0.3298 0.4910 0.2960 0.0204  0.0770  -0.0352 699  PRO B CD  
13866 N N   . ILE B 702  ? 0.2825 0.4238 0.2752 0.0232  0.0638  -0.0462 700  ILE B N   
13867 C CA  . ILE B 702  ? 0.2577 0.3967 0.2620 0.0219  0.0610  -0.0452 700  ILE B CA  
13868 C C   . ILE B 702  ? 0.2795 0.4194 0.2885 0.0266  0.0617  -0.0506 700  ILE B C   
13869 O O   . ILE B 702  ? 0.2738 0.4083 0.2757 0.0301  0.0602  -0.0564 700  ILE B O   
13870 C CB  . ILE B 702  ? 0.2787 0.4072 0.2817 0.0193  0.0547  -0.0452 700  ILE B CB  
13871 C CG1 . ILE B 702  ? 0.3378 0.4654 0.3365 0.0152  0.0537  -0.0399 700  ILE B CG1 
13872 C CG2 . ILE B 702  ? 0.2464 0.3725 0.2603 0.0185  0.0520  -0.0448 700  ILE B CG2 
13873 C CD1 . ILE B 702  ? 0.3064 0.4398 0.3123 0.0121  0.0560  -0.0335 700  ILE B CD1 
13874 N N   . VAL B 703  ? 0.2690 0.4152 0.2897 0.0265  0.0634  -0.0486 701  VAL B N   
13875 C CA  . VAL B 703  ? 0.2702 0.4176 0.2974 0.0309  0.0635  -0.0531 701  VAL B CA  
13876 C C   . VAL B 703  ? 0.2607 0.3986 0.2924 0.0294  0.0573  -0.0539 701  VAL B C   
13877 O O   . VAL B 703  ? 0.2381 0.3752 0.2758 0.0252  0.0552  -0.0495 701  VAL B O   
13878 C CB  . VAL B 703  ? 0.2417 0.4020 0.2801 0.0314  0.0684  -0.0502 701  VAL B CB  
13879 C CG1 . VAL B 703  ? 0.2766 0.4381 0.3237 0.0356  0.0676  -0.0542 701  VAL B CG1 
13880 C CG2 . VAL B 703  ? 0.2284 0.3987 0.2614 0.0332  0.0751  -0.0495 701  VAL B CG2 
13881 N N   . CYS B 704  ? 0.2029 0.3331 0.2311 0.0329  0.0542  -0.0596 702  CYS B N   
13882 C CA  . CYS B 704  ? 0.2161 0.3371 0.2474 0.0317  0.0484  -0.0606 702  CYS B CA  
13883 C C   . CYS B 704  ? 0.2362 0.3583 0.2751 0.0359  0.0480  -0.0640 702  CYS B C   
13884 O O   . CYS B 704  ? 0.2621 0.3825 0.2970 0.0408  0.0486  -0.0692 702  CYS B O   
13885 C CB  . CYS B 704  ? 0.2526 0.3626 0.2732 0.0315  0.0443  -0.0638 702  CYS B CB  
13886 S SG  . CYS B 704  ? 0.2921 0.4001 0.3045 0.0266  0.0435  -0.0597 702  CYS B SG  
13887 N N   . ILE B 705  ? 0.2521 0.3769 0.3018 0.0342  0.0467  -0.0611 703  ILE B N   
13888 C CA  . ILE B 705  ? 0.2184 0.3455 0.2768 0.0380  0.0461  -0.0635 703  ILE B CA  
13889 C C   . ILE B 705  ? 0.2158 0.3325 0.2756 0.0368  0.0398  -0.0642 703  ILE B C   
13890 O O   . ILE B 705  ? 0.2387 0.3531 0.3011 0.0323  0.0373  -0.0604 703  ILE B O   
13891 C CB  . ILE B 705  ? 0.2489 0.3884 0.3194 0.0370  0.0495  -0.0595 703  ILE B CB  
13892 C CG1 . ILE B 705  ? 0.2460 0.3967 0.3150 0.0385  0.0563  -0.0586 703  ILE B CG1 
13893 C CG2 . ILE B 705  ? 0.2374 0.3791 0.3180 0.0406  0.0478  -0.0616 703  ILE B CG2 
13894 C CD1 . ILE B 705  ? 0.2798 0.4440 0.3608 0.0367  0.0601  -0.0538 703  ILE B CD1 
13895 N N   . SER B 706  ? 0.2303 0.3403 0.2876 0.0408  0.0371  -0.0691 704  SER B N   
13896 C CA  . SER B 706  ? 0.2703 0.3694 0.3266 0.0395  0.0311  -0.0698 704  SER B CA  
13897 C C   . SER B 706  ? 0.2436 0.3427 0.3084 0.0428  0.0287  -0.0714 704  SER B C   
13898 O O   . SER B 706  ? 0.2276 0.3337 0.2976 0.0474  0.0315  -0.0735 704  SER B O   
13899 C CB  . SER B 706  ? 0.2531 0.3418 0.2980 0.0403  0.0285  -0.0735 704  SER B CB  
13900 O OG  . SER B 706  ? 0.2459 0.3354 0.2875 0.0459  0.0306  -0.0784 704  SER B OG  
13901 N N   . PRO B 707  ? 0.2776 0.3690 0.3438 0.0407  0.0236  -0.0705 705  PRO B N   
13902 C CA  . PRO B 707  ? 0.2400 0.3309 0.3140 0.0436  0.0206  -0.0716 705  PRO B CA  
13903 C C   . PRO B 707  ? 0.2942 0.3751 0.3631 0.0476  0.0171  -0.0762 705  PRO B C   
13904 O O   . PRO B 707  ? 0.3134 0.3870 0.3725 0.0477  0.0164  -0.0786 705  PRO B O   
13905 C CB  . PRO B 707  ? 0.2866 0.3739 0.3633 0.0387  0.0168  -0.0677 705  PRO B CB  
13906 C CG  . PRO B 707  ? 0.2930 0.3736 0.3603 0.0348  0.0160  -0.0666 705  PRO B CG  
13907 C CD  . PRO B 707  ? 0.2836 0.3688 0.3457 0.0353  0.0207  -0.0673 705  PRO B CD  
13908 N N   . TRP B 708  ? 0.2856 0.3660 0.3614 0.0509  0.0144  -0.0774 706  TRP B N   
13909 C CA  . TRP B 708  ? 0.3159 0.3862 0.3878 0.0550  0.0104  -0.0815 706  TRP B CA  
13910 C C   . TRP B 708  ? 0.2626 0.3209 0.3301 0.0514  0.0044  -0.0800 706  TRP B C   
13911 O O   . TRP B 708  ? 0.2905 0.3386 0.3529 0.0536  0.0007  -0.0829 706  TRP B O   
13912 C CB  . TRP B 708  ? 0.2919 0.3673 0.3733 0.0609  0.0102  -0.0835 706  TRP B CB  
13913 C CG  . TRP B 708  ? 0.3220 0.4041 0.4142 0.0587  0.0090  -0.0795 706  TRP B CG  
13914 C CD1 . TRP B 708  ? 0.3092 0.4050 0.4110 0.0582  0.0130  -0.0770 706  TRP B CD1 
13915 C CD2 . TRP B 708  ? 0.2287 0.3040 0.3227 0.0562  0.0031  -0.0773 706  TRP B CD2 
13916 N NE1 . TRP B 708  ? 0.2962 0.3936 0.4058 0.0556  0.0096  -0.0737 706  TRP B NE1 
13917 C CE2 . TRP B 708  ? 0.3103 0.3953 0.4149 0.0545  0.0036  -0.0739 706  TRP B CE2 
13918 C CE3 . TRP B 708  ? 0.3020 0.3640 0.3895 0.0552  -0.0025 -0.0778 706  TRP B CE3 
13919 C CZ2 . TRP B 708  ? 0.3162 0.3974 0.4243 0.0519  -0.0015 -0.0714 706  TRP B CZ2 
13920 C CZ3 . TRP B 708  ? 0.2722 0.3310 0.3631 0.0527  -0.0072 -0.0749 706  TRP B CZ3 
13921 C CH2 . TRP B 708  ? 0.3248 0.3931 0.4257 0.0514  -0.0067 -0.0720 706  TRP B CH2 
13922 N N   . ASN B 709  ? 0.2409 0.3000 0.3100 0.0461  0.0033  -0.0757 707  ASN B N   
13923 C CA  . ASN B 709  ? 0.3223 0.3713 0.3880 0.0432  -0.0022 -0.0741 707  ASN B CA  
13924 C C   . ASN B 709  ? 0.3229 0.3641 0.3783 0.0392  -0.0032 -0.0736 707  ASN B C   
13925 O O   . ASN B 709  ? 0.3466 0.3782 0.3976 0.0377  -0.0076 -0.0733 707  ASN B O   
13926 C CB  . ASN B 709  ? 0.2808 0.3338 0.3531 0.0399  -0.0034 -0.0701 707  ASN B CB  
13927 C CG  . ASN B 709  ? 0.3412 0.3997 0.4127 0.0354  0.0000  -0.0669 707  ASN B CG  
13928 O OD1 . ASN B 709  ? 0.3976 0.4615 0.4676 0.0355  0.0043  -0.0674 707  ASN B OD1 
13929 N ND2 . ASN B 709  ? 0.3312 0.3881 0.4035 0.0316  -0.0022 -0.0637 707  ASN B ND2 
13930 N N   . PHE B 710  ? 0.3355 0.3808 0.3871 0.0375  0.0007  -0.0733 708  PHE B N   
13931 C CA  . PHE B 710  ? 0.3412 0.3800 0.3832 0.0346  -0.0002 -0.0736 708  PHE B CA  
13932 C C   . PHE B 710  ? 0.2958 0.3373 0.3338 0.0373  0.0033  -0.0769 708  PHE B C   
13933 O O   . PHE B 710  ? 0.2783 0.3249 0.3137 0.0352  0.0067  -0.0756 708  PHE B O   
13934 C CB  . PHE B 710  ? 0.3317 0.3724 0.3722 0.0292  0.0005  -0.0694 708  PHE B CB  
13935 C CG  . PHE B 710  ? 0.3767 0.4135 0.4191 0.0268  -0.0031 -0.0666 708  PHE B CG  
13936 C CD1 . PHE B 710  ? 0.4030 0.4303 0.4404 0.0254  -0.0074 -0.0667 708  PHE B CD1 
13937 C CD2 . PHE B 710  ? 0.3813 0.4236 0.4303 0.0259  -0.0024 -0.0640 708  PHE B CD2 
13938 C CE1 . PHE B 710  ? 0.4413 0.4651 0.4796 0.0232  -0.0105 -0.0640 708  PHE B CE1 
13939 C CE2 . PHE B 710  ? 0.4502 0.4886 0.5001 0.0239  -0.0058 -0.0618 708  PHE B CE2 
13940 C CZ  . PHE B 710  ? 0.4502 0.4795 0.4945 0.0227  -0.0097 -0.0618 708  PHE B CZ  
13941 N N   . PRO B 711  ? 0.3143 0.3523 0.3514 0.0424  0.0025  -0.0813 709  PRO B N   
13942 C CA  . PRO B 711  ? 0.2963 0.3385 0.3306 0.0462  0.0065  -0.0849 709  PRO B CA  
13943 C C   . PRO B 711  ? 0.2882 0.3252 0.3117 0.0441  0.0063  -0.0863 709  PRO B C   
13944 O O   . PRO B 711  ? 0.3076 0.3489 0.3275 0.0466  0.0101  -0.0888 709  PRO B O   
13945 C CB  . PRO B 711  ? 0.2946 0.3329 0.3310 0.0526  0.0048  -0.0893 709  PRO B CB  
13946 C CG  . PRO B 711  ? 0.3023 0.3286 0.3365 0.0507  -0.0016 -0.0886 709  PRO B CG  
13947 C CD  . PRO B 711  ? 0.2900 0.3192 0.3279 0.0450  -0.0023 -0.0832 709  PRO B CD  
13948 N N   . LEU B 712  ? 0.3042 0.3327 0.3225 0.0396  0.0022  -0.0847 710  LEU B N   
13949 C CA  . LEU B 712  ? 0.2983 0.3238 0.3077 0.0365  0.0019  -0.0850 710  LEU B CA  
13950 C C   . LEU B 712  ? 0.3028 0.3331 0.3127 0.0309  0.0030  -0.0800 710  LEU B C   
13951 O O   . LEU B 712  ? 0.3013 0.3358 0.3071 0.0295  0.0056  -0.0794 710  LEU B O   
13952 C CB  . LEU B 712  ? 0.2783 0.2907 0.2806 0.0354  -0.0037 -0.0872 710  LEU B CB  
13953 C CG  . LEU B 712  ? 0.2859 0.2947 0.2790 0.0321  -0.0048 -0.0878 710  LEU B CG  
13954 C CD1 . LEU B 712  ? 0.2965 0.3071 0.2839 0.0362  -0.0019 -0.0925 710  LEU B CD1 
13955 C CD2 . LEU B 712  ? 0.3279 0.3241 0.3156 0.0290  -0.0111 -0.0883 710  LEU B CD2 
13956 N N   . ALA B 713  ? 0.2761 0.3057 0.2905 0.0279  0.0010  -0.0762 711  ALA B N   
13957 C CA  . ALA B 713  ? 0.2892 0.3216 0.3030 0.0229  0.0014  -0.0719 711  ALA B CA  
13958 C C   . ALA B 713  ? 0.2678 0.3106 0.2856 0.0229  0.0062  -0.0696 711  ALA B C   
13959 O O   . ALA B 713  ? 0.2709 0.3169 0.2852 0.0205  0.0079  -0.0678 711  ALA B O   
13960 C CB  . ALA B 713  ? 0.3142 0.3430 0.3310 0.0203  -0.0018 -0.0688 711  ALA B CB  
13961 N N   . ILE B 714  ? 0.2455 0.2938 0.2709 0.0251  0.0082  -0.0691 712  ILE B N   
13962 C CA  . ILE B 714  ? 0.2437 0.3016 0.2733 0.0244  0.0125  -0.0664 712  ILE B CA  
13963 C C   . ILE B 714  ? 0.2724 0.3353 0.2986 0.0268  0.0164  -0.0686 712  ILE B C   
13964 O O   . ILE B 714  ? 0.2594 0.3276 0.2839 0.0249  0.0193  -0.0663 712  ILE B O   
13965 C CB  . ILE B 714  ? 0.3070 0.3695 0.3461 0.0256  0.0131  -0.0651 712  ILE B CB  
13966 C CG1 . ILE B 714  ? 0.3021 0.3606 0.3432 0.0225  0.0097  -0.0622 712  ILE B CG1 
13967 C CG2 . ILE B 714  ? 0.2984 0.3710 0.3421 0.0254  0.0177  -0.0628 712  ILE B CG2 
13968 C CD1 . ILE B 714  ? 0.4281 0.4905 0.4782 0.0232  0.0095  -0.0608 712  ILE B CD1 
13969 N N   . PHE B 715  ? 0.2770 0.3379 0.3017 0.0311  0.0165  -0.0730 713  PHE B N   
13970 C CA  . PHE B 715  ? 0.2617 0.3256 0.2809 0.0338  0.0198  -0.0759 713  PHE B CA  
13971 C C   . PHE B 715  ? 0.2936 0.3549 0.3038 0.0305  0.0192  -0.0752 713  PHE B C   
13972 O O   . PHE B 715  ? 0.2862 0.3539 0.2942 0.0299  0.0229  -0.0737 713  PHE B O   
13973 C CB  . PHE B 715  ? 0.2641 0.3223 0.2810 0.0389  0.0182  -0.0815 713  PHE B CB  
13974 C CG  . PHE B 715  ? 0.2751 0.3351 0.2852 0.0425  0.0213  -0.0854 713  PHE B CG  
13975 C CD1 . PHE B 715  ? 0.2498 0.3197 0.2639 0.0465  0.0266  -0.0863 713  PHE B CD1 
13976 C CD2 . PHE B 715  ? 0.2848 0.3367 0.2842 0.0417  0.0188  -0.0882 713  PHE B CD2 
13977 C CE1 . PHE B 715  ? 0.2670 0.3390 0.2738 0.0502  0.0299  -0.0901 713  PHE B CE1 
13978 C CE2 . PHE B 715  ? 0.2887 0.3417 0.2805 0.0452  0.0215  -0.0922 713  PHE B CE2 
13979 C CZ  . PHE B 715  ? 0.3101 0.3731 0.3053 0.0497  0.0272  -0.0933 713  PHE B CZ  
13980 N N   . THR B 716  ? 0.2717 0.3238 0.2770 0.0282  0.0145  -0.0758 714  THR B N   
13981 C CA  . THR B 716  ? 0.2610 0.3104 0.2581 0.0251  0.0132  -0.0753 714  THR B CA  
13982 C C   . THR B 716  ? 0.2558 0.3110 0.2550 0.0210  0.0146  -0.0700 714  THR B C   
13983 O O   . THR B 716  ? 0.2784 0.3365 0.2725 0.0197  0.0161  -0.0690 714  THR B O   
13984 C CB  . THR B 716  ? 0.2341 0.2729 0.2269 0.0232  0.0075  -0.0768 714  THR B CB  
13985 O OG1 . THR B 716  ? 0.3021 0.3343 0.2919 0.0273  0.0059  -0.0820 714  THR B OG1 
13986 C CG2 . THR B 716  ? 0.2482 0.2849 0.2333 0.0195  0.0057  -0.0759 714  THR B CG2 
13987 N N   . GLY B 717  ? 0.2478 0.3041 0.2539 0.0192  0.0140  -0.0666 715  GLY B N   
13988 C CA  . GLY B 717  ? 0.2353 0.2956 0.2429 0.0157  0.0148  -0.0619 715  GLY B CA  
13989 C C   . GLY B 717  ? 0.2613 0.3301 0.2704 0.0162  0.0193  -0.0598 715  GLY B C   
13990 O O   . GLY B 717  ? 0.2532 0.3244 0.2590 0.0140  0.0201  -0.0573 715  GLY B O   
13991 N N   . GLN B 718  ? 0.2370 0.3106 0.2515 0.0189  0.0223  -0.0606 716  GLN B N   
13992 C CA  . GLN B 718  ? 0.2211 0.3032 0.2373 0.0189  0.0268  -0.0581 716  GLN B CA  
13993 C C   . GLN B 718  ? 0.2360 0.3196 0.2436 0.0199  0.0288  -0.0598 716  GLN B C   
13994 O O   . GLN B 718  ? 0.2264 0.3141 0.2314 0.0180  0.0308  -0.0567 716  GLN B O   
13995 C CB  . GLN B 718  ? 0.2081 0.2961 0.2324 0.0215  0.0297  -0.0585 716  GLN B CB  
13996 C CG  . GLN B 718  ? 0.2377 0.3245 0.2707 0.0205  0.0274  -0.0569 716  GLN B CG  
13997 C CD  . GLN B 718  ? 0.1972 0.2913 0.2391 0.0225  0.0301  -0.0565 716  GLN B CD  
13998 O OE1 . GLN B 718  ? 0.2656 0.3627 0.3145 0.0204  0.0300  -0.0532 716  GLN B OE1 
13999 N NE2 . GLN B 718  ? 0.2198 0.3170 0.2615 0.0267  0.0324  -0.0601 716  GLN B NE2 
14000 N N   . ILE B 719  ? 0.2310 0.3106 0.2337 0.0229  0.0280  -0.0648 717  ILE B N   
14001 C CA  . ILE B 719  ? 0.2394 0.3198 0.2329 0.0244  0.0297  -0.0672 717  ILE B CA  
14002 C C   . ILE B 719  ? 0.2353 0.3120 0.2216 0.0208  0.0268  -0.0657 717  ILE B C   
14003 O O   . ILE B 719  ? 0.2393 0.3199 0.2203 0.0200  0.0288  -0.0641 717  ILE B O   
14004 C CB  . ILE B 719  ? 0.2365 0.3121 0.2262 0.0289  0.0289  -0.0735 717  ILE B CB  
14005 C CG1 . ILE B 719  ? 0.2624 0.3446 0.2593 0.0331  0.0329  -0.0748 717  ILE B CG1 
14006 C CG2 . ILE B 719  ? 0.3025 0.3762 0.2808 0.0301  0.0292  -0.0767 717  ILE B CG2 
14007 C CD1 . ILE B 719  ? 0.2966 0.3733 0.2919 0.0379  0.0314  -0.0807 717  ILE B CD1 
14008 N N   . ALA B 720  ? 0.2443 0.3139 0.2305 0.0186  0.0220  -0.0657 718  ALA B N   
14009 C CA  . ALA B 720  ? 0.2977 0.3645 0.2782 0.0151  0.0189  -0.0642 718  ALA B CA  
14010 C C   . ALA B 720  ? 0.2765 0.3492 0.2591 0.0125  0.0206  -0.0587 718  ALA B C   
14011 O O   . ALA B 720  ? 0.2506 0.3248 0.2273 0.0110  0.0203  -0.0573 718  ALA B O   
14012 C CB  . ALA B 720  ? 0.2538 0.3133 0.2356 0.0129  0.0139  -0.0645 718  ALA B CB  
14013 N N   . ALA B 721  ? 0.2272 0.3031 0.2181 0.0119  0.0221  -0.0555 719  ALA B N   
14014 C CA  . ALA B 721  ? 0.2128 0.2932 0.2060 0.0097  0.0234  -0.0503 719  ALA B CA  
14015 C C   . ALA B 721  ? 0.2835 0.3702 0.2736 0.0104  0.0275  -0.0489 719  ALA B C   
14016 O O   . ALA B 721  ? 0.2832 0.3719 0.2697 0.0086  0.0275  -0.0458 719  ALA B O   
14017 C CB  . ALA B 721  ? 0.2487 0.3301 0.2510 0.0092  0.0238  -0.0478 719  ALA B CB  
14018 N N   . ALA B 722  ? 0.2539 0.3442 0.2455 0.0131  0.0310  -0.0509 720  ALA B N   
14019 C CA  . ALA B 722  ? 0.2362 0.3333 0.2247 0.0138  0.0354  -0.0493 720  ALA B CA  
14020 C C   . ALA B 722  ? 0.2354 0.3310 0.2127 0.0142  0.0347  -0.0514 720  ALA B C   
14021 O O   . ALA B 722  ? 0.2509 0.3499 0.2236 0.0128  0.0360  -0.0482 720  ALA B O   
14022 C CB  . ALA B 722  ? 0.2178 0.3201 0.2108 0.0169  0.0395  -0.0513 720  ALA B CB  
14023 N N   . LEU B 723  ? 0.2021 0.2917 0.1744 0.0159  0.0321  -0.0567 721  LEU B N   
14024 C CA  . LEU B 723  ? 0.2552 0.3423 0.2162 0.0162  0.0306  -0.0593 721  LEU B CA  
14025 C C   . LEU B 723  ? 0.2789 0.3645 0.2368 0.0124  0.0271  -0.0557 721  LEU B C   
14026 O O   . LEU B 723  ? 0.2963 0.3841 0.2468 0.0117  0.0275  -0.0545 721  LEU B O   
14027 C CB  . LEU B 723  ? 0.2548 0.3342 0.2116 0.0183  0.0275  -0.0656 721  LEU B CB  
14028 C CG  . LEU B 723  ? 0.2911 0.3714 0.2480 0.0232  0.0307  -0.0704 721  LEU B CG  
14029 C CD1 . LEU B 723  ? 0.3232 0.3936 0.2769 0.0248  0.0263  -0.0760 721  LEU B CD1 
14030 C CD2 . LEU B 723  ? 0.2540 0.3395 0.2028 0.0258  0.0350  -0.0717 721  LEU B CD2 
14031 N N   . VAL B 724  ? 0.2353 0.3172 0.1985 0.0100  0.0234  -0.0542 722  VAL B N   
14032 C CA  . VAL B 724  ? 0.2498 0.3306 0.2103 0.0069  0.0197  -0.0515 722  VAL B CA  
14033 C C   . VAL B 724  ? 0.2640 0.3506 0.2262 0.0056  0.0219  -0.0457 722  VAL B C   
14034 O O   . VAL B 724  ? 0.3068 0.3943 0.2642 0.0039  0.0199  -0.0434 722  VAL B O   
14035 C CB  . VAL B 724  ? 0.2533 0.3294 0.2190 0.0050  0.0157  -0.0513 722  VAL B CB  
14036 C CG1 . VAL B 724  ? 0.2631 0.3418 0.2382 0.0043  0.0170  -0.0472 722  VAL B CG1 
14037 C CG2 . VAL B 724  ? 0.2393 0.3133 0.2003 0.0022  0.0110  -0.0507 722  VAL B CG2 
14038 N N   . ALA B 725  ? 0.2735 0.3640 0.2421 0.0063  0.0256  -0.0433 723  ALA B N   
14039 C CA  . ALA B 725  ? 0.2739 0.3692 0.2436 0.0050  0.0278  -0.0378 723  ALA B CA  
14040 C C   . ALA B 725  ? 0.3138 0.4132 0.2756 0.0058  0.0308  -0.0374 723  ALA B C   
14041 O O   . ALA B 725  ? 0.3142 0.4175 0.2760 0.0047  0.0326  -0.0325 723  ALA B O   
14042 C CB  . ALA B 725  ? 0.2825 0.3799 0.2617 0.0050  0.0303  -0.0353 723  ALA B CB  
14043 N N   . GLY B 726  ? 0.2952 0.3935 0.2497 0.0079  0.0313  -0.0423 724  GLY B N   
14044 C CA  . GLY B 726  ? 0.2543 0.3564 0.1997 0.0089  0.0340  -0.0423 724  GLY B CA  
14045 C C   . GLY B 726  ? 0.3031 0.4109 0.2496 0.0114  0.0400  -0.0431 724  GLY B C   
14046 O O   . GLY B 726  ? 0.3054 0.4178 0.2451 0.0119  0.0432  -0.0417 724  GLY B O   
14047 N N   . ASN B 727  ? 0.2605 0.3687 0.2156 0.0130  0.0416  -0.0451 725  ASN B N   
14048 C CA  . ASN B 727  ? 0.2686 0.3834 0.2269 0.0155  0.0473  -0.0457 725  ASN B CA  
14049 C C   . ASN B 727  ? 0.2611 0.3738 0.2156 0.0198  0.0479  -0.0529 725  ASN B C   
14050 O O   . ASN B 727  ? 0.3125 0.4182 0.2686 0.0205  0.0440  -0.0567 725  ASN B O   
14051 C CB  . ASN B 727  ? 0.2942 0.4115 0.2655 0.0145  0.0483  -0.0427 725  ASN B CB  
14052 C CG  . ASN B 727  ? 0.2989 0.4163 0.2742 0.0105  0.0469  -0.0362 725  ASN B CG  
14053 O OD1 . ASN B 727  ? 0.3004 0.4229 0.2745 0.0090  0.0497  -0.0315 725  ASN B OD1 
14054 N ND2 . ASN B 727  ? 0.2556 0.3672 0.2354 0.0090  0.0425  -0.0359 725  ASN B ND2 
14055 N N   . PRO B 728  ? 0.2919 0.4100 0.2411 0.0229  0.0527  -0.0548 726  PRO B N   
14056 C CA  . PRO B 728  ? 0.2714 0.3880 0.2190 0.0279  0.0539  -0.0617 726  PRO B CA  
14057 C C   . PRO B 728  ? 0.3038 0.4239 0.2646 0.0292  0.0557  -0.0615 726  PRO B C   
14058 O O   . PRO B 728  ? 0.2845 0.4111 0.2541 0.0270  0.0582  -0.0561 726  PRO B O   
14059 C CB  . PRO B 728  ? 0.3152 0.4383 0.2536 0.0308  0.0592  -0.0630 726  PRO B CB  
14060 C CG  . PRO B 728  ? 0.2986 0.4301 0.2397 0.0273  0.0627  -0.0552 726  PRO B CG  
14061 C CD  . PRO B 728  ? 0.3074 0.4345 0.2538 0.0223  0.0579  -0.0503 726  PRO B CD  
14062 N N   . VAL B 729  ? 0.3069 0.4218 0.2689 0.0329  0.0540  -0.0674 727  VAL B N   
14063 C CA  . VAL B 729  ? 0.2837 0.3995 0.2579 0.0340  0.0538  -0.0677 727  VAL B CA  
14064 C C   . VAL B 729  ? 0.2943 0.4146 0.2699 0.0400  0.0578  -0.0725 727  VAL B C   
14065 O O   . VAL B 729  ? 0.2953 0.4112 0.2618 0.0441  0.0575  -0.0785 727  VAL B O   
14066 C CB  . VAL B 729  ? 0.2966 0.4017 0.2728 0.0325  0.0473  -0.0695 727  VAL B CB  
14067 C CG1 . VAL B 729  ? 0.2232 0.3283 0.2097 0.0351  0.0470  -0.0714 727  VAL B CG1 
14068 C CG2 . VAL B 729  ? 0.2525 0.3558 0.2311 0.0270  0.0443  -0.0640 727  VAL B CG2 
14069 N N   . LEU B 730  ? 0.2382 0.3672 0.2253 0.0407  0.0613  -0.0699 728  LEU B N   
14070 C CA  . LEU B 730  ? 0.2871 0.4210 0.2796 0.0464  0.0644  -0.0740 728  LEU B CA  
14071 C C   . LEU B 730  ? 0.2607 0.3890 0.2630 0.0463  0.0599  -0.0748 728  LEU B C   
14072 O O   . LEU B 730  ? 0.2905 0.4219 0.3027 0.0426  0.0592  -0.0698 728  LEU B O   
14073 C CB  . LEU B 730  ? 0.2488 0.3975 0.2486 0.0468  0.0714  -0.0699 728  LEU B CB  
14074 C CG  . LEU B 730  ? 0.2689 0.4253 0.2598 0.0470  0.0769  -0.0682 728  LEU B CG  
14075 C CD1 . LEU B 730  ? 0.2659 0.4165 0.2425 0.0519  0.0768  -0.0752 728  LEU B CD1 
14076 C CD2 . LEU B 730  ? 0.2994 0.4550 0.2874 0.0403  0.0756  -0.0616 728  LEU B CD2 
14077 N N   . ALA B 731  ? 0.2767 0.3960 0.2756 0.0501  0.0564  -0.0808 729  ALA B N   
14078 C CA  . ALA B 731  ? 0.2460 0.3583 0.2523 0.0498  0.0513  -0.0816 729  ALA B CA  
14079 C C   . ALA B 731  ? 0.2621 0.3800 0.2774 0.0554  0.0536  -0.0842 729  ALA B C   
14080 O O   . ALA B 731  ? 0.2703 0.3873 0.2810 0.0614  0.0550  -0.0899 729  ALA B O   
14081 C CB  . ALA B 731  ? 0.2550 0.3531 0.2524 0.0498  0.0452  -0.0858 729  ALA B CB  
14082 N N   . LYS B 732  ? 0.2389 0.3627 0.2669 0.0536  0.0537  -0.0803 730  LYS B N   
14083 C CA  . LYS B 732  ? 0.2147 0.3446 0.2529 0.0585  0.0553  -0.0821 730  LYS B CA  
14084 C C   . LYS B 732  ? 0.2670 0.3879 0.3107 0.0579  0.0489  -0.0827 730  LYS B C   
14085 O O   . LYS B 732  ? 0.2447 0.3673 0.2964 0.0535  0.0471  -0.0780 730  LYS B O   
14086 C CB  . LYS B 732  ? 0.2262 0.3713 0.2755 0.0569  0.0604  -0.0769 730  LYS B CB  
14087 C CG  . LYS B 732  ? 0.2652 0.4219 0.3220 0.0633  0.0653  -0.0793 730  LYS B CG  
14088 C CD  . LYS B 732  ? 0.2791 0.4327 0.3446 0.0673  0.0616  -0.0823 730  LYS B CD  
14089 C CE  . LYS B 732  ? 0.2513 0.4066 0.3287 0.0624  0.0583  -0.0771 730  LYS B CE  
14090 N NZ  . LYS B 732  ? 0.2983 0.4507 0.3833 0.0667  0.0545  -0.0801 730  LYS B NZ  
14091 N N   . PRO B 733  ? 0.2760 0.3872 0.3155 0.0622  0.0453  -0.0882 731  PRO B N   
14092 C CA  . PRO B 733  ? 0.2639 0.3659 0.3076 0.0614  0.0391  -0.0884 731  PRO B CA  
14093 C C   . PRO B 733  ? 0.2569 0.3661 0.3136 0.0648  0.0396  -0.0881 731  PRO B C   
14094 O O   . PRO B 733  ? 0.2669 0.3876 0.3291 0.0690  0.0447  -0.0890 731  PRO B O   
14095 C CB  . PRO B 733  ? 0.2548 0.3438 0.2884 0.0649  0.0354  -0.0945 731  PRO B CB  
14096 C CG  . PRO B 733  ? 0.2802 0.3755 0.3103 0.0713  0.0406  -0.0989 731  PRO B CG  
14097 C CD  . PRO B 733  ? 0.2689 0.3767 0.2993 0.0683  0.0468  -0.0947 731  PRO B CD  
14098 N N   . ALA B 734  ? 0.2786 0.3815 0.3404 0.0629  0.0342  -0.0868 732  ALA B N   
14099 C CA  . ALA B 734  ? 0.2573 0.3661 0.3315 0.0657  0.0336  -0.0862 732  ALA B CA  
14100 C C   . ALA B 734  ? 0.2859 0.3955 0.3610 0.0742  0.0347  -0.0919 732  ALA B C   
14101 O O   . ALA B 734  ? 0.2487 0.3477 0.3142 0.0774  0.0326  -0.0968 732  ALA B O   
14102 C CB  . ALA B 734  ? 0.2756 0.3751 0.3524 0.0625  0.0269  -0.0843 732  ALA B CB  
14103 N N   . GLU B 735  ? 0.2499 0.3721 0.3369 0.0778  0.0378  -0.0913 733  GLU B N   
14104 C CA  . GLU B 735  ? 0.2465 0.3712 0.3361 0.0866  0.0392  -0.0966 733  GLU B CA  
14105 C C   . GLU B 735  ? 0.3062 0.4156 0.3920 0.0898  0.0323  -0.1006 733  GLU B C   
14106 O O   . GLU B 735  ? 0.2773 0.3815 0.3580 0.0967  0.0322  -0.1064 733  GLU B O   
14107 C CB  . GLU B 735  ? 0.3490 0.4898 0.4545 0.0889  0.0422  -0.0942 733  GLU B CB  
14108 C CG  . GLU B 735  ? 0.4092 0.5576 0.5186 0.0983  0.0460  -0.0990 733  GLU B CG  
14109 C CD  . GLU B 735  ? 0.4401 0.6068 0.5665 0.0999  0.0494  -0.0957 733  GLU B CD  
14110 O OE1 . GLU B 735  ? 0.4481 0.6223 0.5816 0.0929  0.0500  -0.0896 733  GLU B OE1 
14111 O OE2 . GLU B 735  ? 0.4776 0.6506 0.6101 0.1080  0.0512  -0.0994 733  GLU B OE2 
14112 N N   . GLU B 736  ? 0.2489 0.3503 0.3366 0.0850  0.0263  -0.0975 734  GLU B N   
14113 C CA  . GLU B 736  ? 0.2879 0.3755 0.3734 0.0876  0.0195  -0.1002 734  GLU B CA  
14114 C C   . GLU B 736  ? 0.2841 0.3557 0.3550 0.0867  0.0162  -0.1034 734  GLU B C   
14115 O O   . GLU B 736  ? 0.3159 0.3764 0.3832 0.0910  0.0119  -0.1074 734  GLU B O   
14116 C CB  . GLU B 736  ? 0.2788 0.3638 0.3706 0.0825  0.0144  -0.0954 734  GLU B CB  
14117 C CG  . GLU B 736  ? 0.3310 0.4297 0.4379 0.0838  0.0157  -0.0927 734  GLU B CG  
14118 C CD  . GLU B 736  ? 0.3816 0.4926 0.4939 0.0779  0.0199  -0.0875 734  GLU B CD  
14119 O OE1 . GLU B 736  ? 0.2909 0.4027 0.3960 0.0744  0.0235  -0.0866 734  GLU B OE1 
14120 O OE2 . GLU B 736  ? 0.4170 0.5366 0.5411 0.0767  0.0192  -0.0842 734  GLU B OE2 
14121 N N   . THR B 737  ? 0.2959 0.3660 0.3586 0.0810  0.0178  -0.1017 735  THR B N   
14122 C CA  . THR B 737  ? 0.3128 0.3680 0.3626 0.0782  0.0138  -0.1035 735  THR B CA  
14123 C C   . THR B 737  ? 0.3321 0.3886 0.3720 0.0782  0.0179  -0.1058 735  THR B C   
14124 O O   . THR B 737  ? 0.3593 0.4128 0.3926 0.0721  0.0174  -0.1033 735  THR B O   
14125 C CB  . THR B 737  ? 0.3032 0.3531 0.3524 0.0702  0.0098  -0.0983 735  THR B CB  
14126 O OG1 . THR B 737  ? 0.2664 0.3271 0.3191 0.0654  0.0139  -0.0936 735  THR B OG1 
14127 C CG2 . THR B 737  ? 0.2710 0.3174 0.3278 0.0706  0.0049  -0.0965 735  THR B CG2 
14128 N N   . PRO B 738  ? 0.3328 0.3938 0.3710 0.0851  0.0219  -0.1106 736  PRO B N   
14129 C CA  . PRO B 738  ? 0.2959 0.3581 0.3237 0.0852  0.0258  -0.1129 736  PRO B CA  
14130 C C   . PRO B 738  ? 0.3190 0.3650 0.3331 0.0849  0.0210  -0.1172 736  PRO B C   
14131 O O   . PRO B 738  ? 0.3152 0.3604 0.3198 0.0824  0.0226  -0.1177 736  PRO B O   
14132 C CB  . PRO B 738  ? 0.2860 0.3589 0.3172 0.0934  0.0318  -0.1168 736  PRO B CB  
14133 C CG  . PRO B 738  ? 0.2956 0.3631 0.3327 0.0993  0.0279  -0.1198 736  PRO B CG  
14134 C CD  . PRO B 738  ? 0.3180 0.3837 0.3636 0.0935  0.0233  -0.1143 736  PRO B CD  
14135 N N   . LEU B 739  ? 0.2842 0.3171 0.2968 0.0873  0.0150  -0.1201 737  LEU B N   
14136 C CA  . LEU B 739  ? 0.3414 0.3587 0.3412 0.0875  0.0103  -0.1246 737  LEU B CA  
14137 C C   . LEU B 739  ? 0.3362 0.3469 0.3299 0.0784  0.0067  -0.1206 737  LEU B C   
14138 O O   . LEU B 739  ? 0.3095 0.3146 0.2923 0.0767  0.0060  -0.1228 737  LEU B O   
14139 C CB  . LEU B 739  ? 0.3498 0.3543 0.3501 0.0921  0.0044  -0.1282 737  LEU B CB  
14140 C CG  . LEU B 739  ? 0.3209 0.3309 0.3277 0.1019  0.0071  -0.1325 737  LEU B CG  
14141 C CD1 . LEU B 739  ? 0.3566 0.3525 0.3643 0.1051  0.0001  -0.1347 737  LEU B CD1 
14142 C CD2 . LEU B 739  ? 0.3381 0.3500 0.3367 0.1086  0.0117  -0.1390 737  LEU B CD2 
14143 N N   . ILE B 740  ? 0.3307 0.3422 0.3311 0.0728  0.0043  -0.1149 738  ILE B N   
14144 C CA  . ILE B 740  ? 0.3083 0.3147 0.3036 0.0646  0.0013  -0.1111 738  ILE B CA  
14145 C C   . ILE B 740  ? 0.2900 0.3068 0.2830 0.0614  0.0065  -0.1086 738  ILE B C   
14146 O O   . ILE B 740  ? 0.2894 0.3018 0.2745 0.0567  0.0047  -0.1078 738  ILE B O   
14147 C CB  . ILE B 740  ? 0.3434 0.3481 0.3456 0.0598  -0.0022 -0.1057 738  ILE B CB  
14148 C CG1 . ILE B 740  ? 0.3225 0.3221 0.3191 0.0519  -0.0053 -0.1021 738  ILE B CG1 
14149 C CG2 . ILE B 740  ? 0.3240 0.3427 0.3373 0.0595  0.0022  -0.1016 738  ILE B CG2 
14150 C CD1 . ILE B 740  ? 0.3860 0.3704 0.3731 0.0507  -0.0112 -0.1051 738  ILE B CD1 
14151 N N   . ALA B 741  ? 0.3087 0.3394 0.3087 0.0637  0.0126  -0.1072 739  ALA B N   
14152 C CA  . ALA B 741  ? 0.2964 0.3369 0.2941 0.0610  0.0176  -0.1047 739  ALA B CA  
14153 C C   . ALA B 741  ? 0.2841 0.3215 0.2699 0.0637  0.0189  -0.1097 739  ALA B C   
14154 O O   . ALA B 741  ? 0.2948 0.3322 0.2734 0.0594  0.0192  -0.1081 739  ALA B O   
14155 C CB  . ALA B 741  ? 0.2763 0.3320 0.2841 0.0631  0.0237  -0.1022 739  ALA B CB  
14156 N N   . ALA B 742  ? 0.2819 0.3164 0.2650 0.0710  0.0196  -0.1158 740  ALA B N   
14157 C CA  . ALA B 742  ? 0.3066 0.3366 0.2772 0.0742  0.0203  -0.1213 740  ALA B CA  
14158 C C   . ALA B 742  ? 0.3693 0.3848 0.3295 0.0694  0.0136  -0.1224 740  ALA B C   
14159 O O   . ALA B 742  ? 0.3364 0.3505 0.2865 0.0678  0.0139  -0.1238 740  ALA B O   
14160 C CB  . ALA B 742  ? 0.3355 0.3632 0.3053 0.0835  0.0215  -0.1282 740  ALA B CB  
14161 N N   . GLU B 743  ? 0.3252 0.3302 0.2879 0.0672  0.0074  -0.1217 741  GLU B N   
14162 C CA  . GLU B 743  ? 0.3290 0.3209 0.2834 0.0618  0.0008  -0.1218 741  GLU B CA  
14163 C C   . GLU B 743  ? 0.3295 0.3269 0.2837 0.0540  0.0012  -0.1158 741  GLU B C   
14164 O O   . GLU B 743  ? 0.3320 0.3243 0.2771 0.0505  -0.0014 -0.1165 741  GLU B O   
14165 C CB  . GLU B 743  ? 0.4142 0.3950 0.3724 0.0608  -0.0054 -0.1213 741  GLU B CB  
14166 C CG  . GLU B 743  ? 0.3873 0.3548 0.3382 0.0549  -0.0125 -0.1208 741  GLU B CG  
14167 C CD  . GLU B 743  ? 0.4319 0.3880 0.3703 0.0575  -0.0156 -0.1275 741  GLU B CD  
14168 O OE1 . GLU B 743  ? 0.4178 0.3745 0.3529 0.0652  -0.0126 -0.1334 741  GLU B OE1 
14169 O OE2 . GLU B 743  ? 0.4383 0.3850 0.3701 0.0519  -0.0211 -0.1269 741  GLU B OE2 
14170 N N   . GLY B 744  ? 0.2872 0.2951 0.2515 0.0514  0.0043  -0.1100 742  GLY B N   
14171 C CA  . GLY B 744  ? 0.2957 0.3100 0.2604 0.0450  0.0055  -0.1045 742  GLY B CA  
14172 C C   . GLY B 744  ? 0.2917 0.3119 0.2489 0.0454  0.0093  -0.1054 742  GLY B C   
14173 O O   . GLY B 744  ? 0.3159 0.3349 0.2676 0.0405  0.0074  -0.1033 742  GLY B O   
14174 N N   . VAL B 745  ? 0.2877 0.3150 0.2447 0.0512  0.0147  -0.1084 743  VAL B N   
14175 C CA  . VAL B 745  ? 0.3152 0.3479 0.2638 0.0521  0.0185  -0.1096 743  VAL B CA  
14176 C C   . VAL B 745  ? 0.3516 0.3727 0.2866 0.0527  0.0142  -0.1150 743  VAL B C   
14177 O O   . VAL B 745  ? 0.3125 0.3342 0.2396 0.0495  0.0138  -0.1142 743  VAL B O   
14178 C CB  . VAL B 745  ? 0.3533 0.3971 0.3053 0.0583  0.0257  -0.1112 743  VAL B CB  
14179 C CG1 . VAL B 745  ? 0.3137 0.3619 0.2549 0.0603  0.0297  -0.1136 743  VAL B CG1 
14180 C CG2 . VAL B 745  ? 0.2943 0.3504 0.2591 0.0561  0.0297  -0.1048 743  VAL B CG2 
14181 N N   . ARG B 746  ? 0.3049 0.3149 0.2370 0.0567  0.0104  -0.1207 744  ARG B N   
14182 C CA  . ARG B 746  ? 0.3739 0.3711 0.2929 0.0565  0.0053  -0.1259 744  ARG B CA  
14183 C C   . ARG B 746  ? 0.3499 0.3424 0.2661 0.0482  -0.0001 -0.1219 744  ARG B C   
14184 O O   . ARG B 746  ? 0.3292 0.3183 0.2351 0.0462  -0.0022 -0.1235 744  ARG B O   
14185 C CB  . ARG B 746  ? 0.3379 0.3218 0.2554 0.0608  0.0005  -0.1315 744  ARG B CB  
14186 C CG  . ARG B 746  ? 0.3757 0.3627 0.2949 0.0701  0.0051  -0.1366 744  ARG B CG  
14187 C CD  . ARG B 746  ? 0.3809 0.3530 0.2980 0.0741  -0.0006 -0.1420 744  ARG B CD  
14188 N NE  . ARG B 746  ? 0.4309 0.4076 0.3516 0.0834  0.0040  -0.1464 744  ARG B NE  
14189 C CZ  . ARG B 746  ? 0.3958 0.3755 0.3281 0.0864  0.0047  -0.1450 744  ARG B CZ  
14190 N NH1 . ARG B 746  ? 0.3616 0.3373 0.3015 0.0812  0.0003  -0.1402 744  ARG B NH1 
14191 N NH2 . ARG B 746  ? 0.3838 0.3711 0.3201 0.0948  0.0100  -0.1485 744  ARG B NH2 
14192 N N   . ILE B 747  ? 0.2979 0.2901 0.2232 0.0435  -0.0026 -0.1167 745  ILE B N   
14193 C CA  . ILE B 747  ? 0.3271 0.3156 0.2511 0.0357  -0.0076 -0.1126 745  ILE B CA  
14194 C C   . ILE B 747  ? 0.3322 0.3313 0.2555 0.0321  -0.0044 -0.1081 745  ILE B C   
14195 O O   . ILE B 747  ? 0.3009 0.2971 0.2174 0.0278  -0.0079 -0.1075 745  ILE B O   
14196 C CB  . ILE B 747  ? 0.3088 0.2956 0.2429 0.0324  -0.0101 -0.1082 745  ILE B CB  
14197 C CG1 . ILE B 747  ? 0.3302 0.3038 0.2630 0.0353  -0.0149 -0.1126 745  ILE B CG1 
14198 C CG2 . ILE B 747  ? 0.3269 0.3141 0.2619 0.0245  -0.0136 -0.1027 745  ILE B CG2 
14199 C CD1 . ILE B 747  ? 0.3264 0.2962 0.2669 0.0316  -0.0184 -0.1085 745  ILE B CD1 
14200 N N   . LEU B 748  ? 0.3100 0.3213 0.2403 0.0336  0.0018  -0.1048 746  LEU B N   
14201 C CA  . LEU B 748  ? 0.2903 0.3113 0.2200 0.0305  0.0049  -0.1002 746  LEU B CA  
14202 C C   . LEU B 748  ? 0.2930 0.3141 0.2106 0.0324  0.0060  -0.1038 746  LEU B C   
14203 O O   . LEU B 748  ? 0.2828 0.3057 0.1954 0.0284  0.0046  -0.1014 746  LEU B O   
14204 C CB  . LEU B 748  ? 0.2714 0.3044 0.2111 0.0318  0.0111  -0.0961 746  LEU B CB  
14205 C CG  . LEU B 748  ? 0.3195 0.3540 0.2695 0.0276  0.0096  -0.0905 746  LEU B CG  
14206 C CD1 . LEU B 748  ? 0.2770 0.3213 0.2372 0.0295  0.0149  -0.0874 746  LEU B CD1 
14207 C CD2 . LEU B 748  ? 0.3236 0.3600 0.2717 0.0220  0.0077  -0.0860 746  LEU B CD2 
14208 N N   . ARG B 749  ? 0.2961 0.3149 0.2084 0.0387  0.0082  -0.1099 747  ARG B N   
14209 C CA  . ARG B 749  ? 0.3100 0.3279 0.2093 0.0408  0.0090  -0.1140 747  ARG B CA  
14210 C C   . ARG B 749  ? 0.3253 0.3305 0.2146 0.0377  0.0013  -0.1172 747  ARG B C   
14211 O O   . ARG B 749  ? 0.3480 0.3535 0.2281 0.0354  -0.0001 -0.1171 747  ARG B O   
14212 C CB  . ARG B 749  ? 0.3450 0.3640 0.2411 0.0490  0.0136  -0.1199 747  ARG B CB  
14213 C CG  . ARG B 749  ? 0.3572 0.3910 0.2611 0.0519  0.0219  -0.1167 747  ARG B CG  
14214 C CD  . ARG B 749  ? 0.4250 0.4608 0.3234 0.0601  0.0267  -0.1230 747  ARG B CD  
14215 N NE  . ARG B 749  ? 0.3885 0.4395 0.2940 0.0627  0.0349  -0.1199 747  ARG B NE  
14216 C CZ  . ARG B 749  ? 0.4635 0.5200 0.3658 0.0697  0.0406  -0.1242 747  ARG B CZ  
14217 N NH1 . ARG B 749  ? 0.4734 0.5211 0.3651 0.0754  0.0390  -0.1322 747  ARG B NH1 
14218 N NH2 . ARG B 749  ? 0.4672 0.5385 0.3773 0.0712  0.0479  -0.1203 747  ARG B NH2 
14219 N N   . GLU B 750  ? 0.3220 0.3159 0.2127 0.0375  -0.0041 -0.1198 748  GLU B N   
14220 C CA  . GLU B 750  ? 0.3514 0.3326 0.2335 0.0337  -0.0120 -0.1225 748  GLU B CA  
14221 C C   . GLU B 750  ? 0.3247 0.3094 0.2088 0.0257  -0.0152 -0.1162 748  GLU B C   
14222 O O   . GLU B 750  ? 0.3452 0.3246 0.2204 0.0224  -0.0200 -0.1174 748  GLU B O   
14223 C CB  . GLU B 750  ? 0.3755 0.3443 0.2603 0.0342  -0.0171 -0.1252 748  GLU B CB  
14224 C CG  . GLU B 750  ? 0.4271 0.3814 0.3034 0.0300  -0.0260 -0.1279 748  GLU B CG  
14225 C CD  . GLU B 750  ? 0.4955 0.4370 0.3746 0.0307  -0.0309 -0.1303 748  GLU B CD  
14226 O OE1 . GLU B 750  ? 0.4406 0.3838 0.3266 0.0358  -0.0274 -0.1311 748  GLU B OE1 
14227 O OE2 . GLU B 750  ? 0.4831 0.4130 0.3579 0.0259  -0.0385 -0.1309 748  GLU B OE2 
14228 N N   . ALA B 751  ? 0.3079 0.3015 0.2035 0.0228  -0.0126 -0.1094 749  ALA B N   
14229 C CA  . ALA B 751  ? 0.3085 0.3070 0.2075 0.0161  -0.0147 -0.1031 749  ALA B CA  
14230 C C   . ALA B 751  ? 0.3262 0.3337 0.2203 0.0155  -0.0117 -0.1009 749  ALA B C   
14231 O O   . ALA B 751  ? 0.3302 0.3411 0.2256 0.0103  -0.0142 -0.0963 749  ALA B O   
14232 C CB  . ALA B 751  ? 0.2833 0.2882 0.1957 0.0140  -0.0126 -0.0972 749  ALA B CB  
14233 N N   . GLY B 752  ? 0.3381 0.3499 0.2271 0.0207  -0.0064 -0.1037 750  GLY B N   
14234 C CA  . GLY B 752  ? 0.3329 0.3525 0.2160 0.0199  -0.0039 -0.1014 750  GLY B CA  
14235 C C   . GLY B 752  ? 0.3576 0.3888 0.2446 0.0233  0.0042  -0.0988 750  GLY B C   
14236 O O   . GLY B 752  ? 0.3097 0.3468 0.1903 0.0234  0.0068  -0.0973 750  GLY B O   
14237 N N   . ILE B 753  ? 0.3440 0.3787 0.2412 0.0258  0.0081  -0.0979 751  ILE B N   
14238 C CA  . ILE B 753  ? 0.3541 0.4002 0.2557 0.0285  0.0156  -0.0950 751  ILE B CA  
14239 C C   . ILE B 753  ? 0.3330 0.3803 0.2252 0.0344  0.0197  -0.1005 751  ILE B C   
14240 O O   . ILE B 753  ? 0.3552 0.3964 0.2453 0.0390  0.0194  -0.1066 751  ILE B O   
14241 C CB  . ILE B 753  ? 0.3346 0.3845 0.2499 0.0295  0.0183  -0.0927 751  ILE B CB  
14242 C CG1 . ILE B 753  ? 0.3593 0.4078 0.2831 0.0241  0.0145  -0.0876 751  ILE B CG1 
14243 C CG2 . ILE B 753  ? 0.3401 0.4019 0.2598 0.0317  0.0257  -0.0895 751  ILE B CG2 
14244 C CD1 . ILE B 753  ? 0.3180 0.3726 0.2424 0.0196  0.0146  -0.0814 751  ILE B CD1 
14245 N N   . PRO B 754  ? 0.3231 0.3780 0.2091 0.0347  0.0237  -0.0985 752  PRO B N   
14246 C CA  . PRO B 754  ? 0.3375 0.3939 0.2131 0.0404  0.0278  -0.1037 752  PRO B CA  
14247 C C   . PRO B 754  ? 0.3708 0.4337 0.2541 0.0459  0.0343  -0.1052 752  PRO B C   
14248 O O   . PRO B 754  ? 0.3398 0.4095 0.2359 0.0446  0.0371  -0.1004 752  PRO B O   
14249 C CB  . PRO B 754  ? 0.3915 0.4560 0.2607 0.0383  0.0307  -0.0993 752  PRO B CB  
14250 C CG  . PRO B 754  ? 0.4162 0.4800 0.2897 0.0315  0.0259  -0.0933 752  PRO B CG  
14251 C CD  . PRO B 754  ? 0.3289 0.3904 0.2160 0.0298  0.0240  -0.0915 752  PRO B CD  
14252 N N   . ALA B 755  ? 0.3989 0.4595 0.2739 0.0522  0.0365  -0.1121 753  ALA B N   
14253 C CA  . ALA B 755  ? 0.3963 0.4633 0.2782 0.0583  0.0425  -0.1143 753  ALA B CA  
14254 C C   . ALA B 755  ? 0.4113 0.4939 0.3015 0.0575  0.0500  -0.1076 753  ALA B C   
14255 O O   . ALA B 755  ? 0.3640 0.4529 0.2671 0.0587  0.0531  -0.1055 753  ALA B O   
14256 C CB  . ALA B 755  ? 0.4822 0.5456 0.3517 0.0656  0.0444  -0.1227 753  ALA B CB  
14257 N N   . SER B 756  ? 0.3814 0.4701 0.2647 0.0549  0.0524  -0.1038 754  SER B N   
14258 C CA  . SER B 756  ? 0.3511 0.4540 0.2417 0.0537  0.0592  -0.0971 754  SER B CA  
14259 C C   . SER B 756  ? 0.3603 0.4654 0.2643 0.0477  0.0574  -0.0896 754  SER B C   
14260 O O   . SER B 756  ? 0.3731 0.4888 0.2867 0.0469  0.0624  -0.0844 754  SER B O   
14261 C CB  . SER B 756  ? 0.3900 0.4979 0.2684 0.0527  0.0621  -0.0949 754  SER B CB  
14262 O OG  . SER B 756  ? 0.4428 0.5442 0.3161 0.0470  0.0560  -0.0920 754  SER B OG  
14263 N N   . ALA B 757  ? 0.3216 0.4174 0.2265 0.0435  0.0503  -0.0890 755  ALA B N   
14264 C CA  . ALA B 757  ? 0.3007 0.3982 0.2177 0.0385  0.0486  -0.0825 755  ALA B CA  
14265 C C   . ALA B 757  ? 0.2966 0.3924 0.2260 0.0398  0.0478  -0.0836 755  ALA B C   
14266 O O   . ALA B 757  ? 0.2761 0.3746 0.2161 0.0363  0.0473  -0.0783 755  ALA B O   
14267 C CB  . ALA B 757  ? 0.3347 0.4246 0.2479 0.0333  0.0418  -0.0806 755  ALA B CB  
14268 N N   . LEU B 758  ? 0.2896 0.3803 0.2174 0.0448  0.0471  -0.0902 756  LEU B N   
14269 C CA  . LEU B 758  ? 0.3154 0.4032 0.2542 0.0461  0.0454  -0.0914 756  LEU B CA  
14270 C C   . LEU B 758  ? 0.3253 0.4147 0.2637 0.0535  0.0489  -0.0975 756  LEU B C   
14271 O O   . LEU B 758  ? 0.3362 0.4169 0.2656 0.0571  0.0463  -0.1041 756  LEU B O   
14272 C CB  . LEU B 758  ? 0.2772 0.3525 0.2150 0.0433  0.0378  -0.0930 756  LEU B CB  
14273 C CG  . LEU B 758  ? 0.3443 0.4152 0.2920 0.0446  0.0353  -0.0943 756  LEU B CG  
14274 C CD1 . LEU B 758  ? 0.3057 0.3850 0.2667 0.0426  0.0379  -0.0885 756  LEU B CD1 
14275 C CD2 . LEU B 758  ? 0.2966 0.3554 0.2419 0.0412  0.0279  -0.0952 756  LEU B CD2 
14276 N N   . GLN B 759  ? 0.3252 0.4258 0.2735 0.0556  0.0545  -0.0951 757  GLN B N   
14277 C CA  . GLN B 759  ? 0.2760 0.3806 0.2262 0.0629  0.0585  -0.1001 757  GLN B CA  
14278 C C   . GLN B 759  ? 0.2927 0.3977 0.2570 0.0637  0.0571  -0.0994 757  GLN B C   
14279 O O   . GLN B 759  ? 0.3221 0.4313 0.2966 0.0591  0.0567  -0.0934 757  GLN B O   
14280 C CB  . GLN B 759  ? 0.3181 0.4372 0.2682 0.0649  0.0667  -0.0979 757  GLN B CB  
14281 C CG  . GLN B 759  ? 0.2942 0.4127 0.2289 0.0647  0.0681  -0.0990 757  GLN B CG  
14282 C CD  . GLN B 759  ? 0.2958 0.4291 0.2304 0.0658  0.0763  -0.0956 757  GLN B CD  
14283 O OE1 . GLN B 759  ? 0.3573 0.4957 0.2868 0.0721  0.0812  -0.1001 757  GLN B OE1 
14284 N NE2 . GLN B 759  ? 0.3020 0.4422 0.2417 0.0598  0.0778  -0.0876 757  GLN B NE2 
14285 N N   . LEU B 760  ? 0.3076 0.4076 0.2722 0.0699  0.0560  -0.1056 758  LEU B N   
14286 C CA  . LEU B 760  ? 0.3094 0.4090 0.2866 0.0715  0.0541  -0.1056 758  LEU B CA  
14287 C C   . LEU B 760  ? 0.2842 0.3966 0.2693 0.0777  0.0607  -0.1067 758  LEU B C   
14288 O O   . LEU B 760  ? 0.2859 0.3996 0.2642 0.0843  0.0639  -0.1123 758  LEU B O   
14289 C CB  . LEU B 760  ? 0.2881 0.3723 0.2610 0.0740  0.0474  -0.1113 758  LEU B CB  
14290 C CG  . LEU B 760  ? 0.2961 0.3785 0.2808 0.0760  0.0449  -0.1115 758  LEU B CG  
14291 C CD1 . LEU B 760  ? 0.2743 0.3544 0.2660 0.0686  0.0408  -0.1053 758  LEU B CD1 
14292 C CD2 . LEU B 760  ? 0.3187 0.3877 0.2979 0.0813  0.0402  -0.1186 758  LEU B CD2 
14293 N N   . LEU B 761  ? 0.2900 0.4120 0.2894 0.0759  0.0625  -0.1016 759  LEU B N   
14294 C CA  . LEU B 761  ? 0.3067 0.4430 0.3161 0.0809  0.0687  -0.1016 759  LEU B CA  
14295 C C   . LEU B 761  ? 0.2607 0.3964 0.2834 0.0825  0.0655  -0.1015 759  LEU B C   
14296 O O   . LEU B 761  ? 0.2827 0.4250 0.3170 0.0782  0.0655  -0.0957 759  LEU B O   
14297 C CB  . LEU B 761  ? 0.3376 0.4889 0.3525 0.0766  0.0746  -0.0945 759  LEU B CB  
14298 C CG  . LEU B 761  ? 0.2950 0.4502 0.2984 0.0747  0.0788  -0.0930 759  LEU B CG  
14299 C CD1 . LEU B 761  ? 0.3439 0.4979 0.3354 0.0822  0.0818  -0.1004 759  LEU B CD1 
14300 C CD2 . LEU B 761  ? 0.3135 0.4584 0.3091 0.0677  0.0738  -0.0902 759  LEU B CD2 
14301 N N   . PRO B 762  ? 0.3052 0.4327 0.3263 0.0888  0.0626  -0.1079 760  PRO B N   
14302 C CA  . PRO B 762  ? 0.3040 0.4312 0.3376 0.0910  0.0595  -0.1078 760  PRO B CA  
14303 C C   . PRO B 762  ? 0.2986 0.4437 0.3460 0.0942  0.0655  -0.1055 760  PRO B C   
14304 O O   . PRO B 762  ? 0.2593 0.4158 0.3054 0.0981  0.0724  -0.1066 760  PRO B O   
14305 C CB  . PRO B 762  ? 0.3453 0.4598 0.3719 0.0980  0.0557  -0.1157 760  PRO B CB  
14306 C CG  . PRO B 762  ? 0.3086 0.4127 0.3180 0.0969  0.0545  -0.1191 760  PRO B CG  
14307 C CD  . PRO B 762  ? 0.2761 0.3935 0.2834 0.0943  0.0615  -0.1154 760  PRO B CD  
14308 N N   . GLY B 763  ? 0.3099 0.4579 0.3707 0.0923  0.0628  -0.1020 761  GLY B N   
14309 C CA  . GLY B 763  ? 0.2976 0.4619 0.3730 0.0955  0.0672  -0.1001 761  GLY B CA  
14310 C C   . GLY B 763  ? 0.3008 0.4691 0.3893 0.0893  0.0643  -0.0936 761  GLY B C   
14311 O O   . GLY B 763  ? 0.3083 0.4653 0.3945 0.0838  0.0583  -0.0916 761  GLY B O   
14312 N N   . ASP B 764  ? 0.3653 0.5503 0.4674 0.0902  0.0687  -0.0904 762  ASP B N   
14313 C CA  . ASP B 764  ? 0.3830 0.5728 0.4987 0.0851  0.0658  -0.0847 762  ASP B CA  
14314 C C   . ASP B 764  ? 0.3705 0.5678 0.4878 0.0768  0.0687  -0.0777 762  ASP B C   
14315 O O   . ASP B 764  ? 0.3033 0.4989 0.4098 0.0744  0.0716  -0.0770 762  ASP B O   
14316 C CB  . ASP B 764  ? 0.3647 0.5677 0.4957 0.0907  0.0676  -0.0852 762  ASP B CB  
14317 C CG  . ASP B 764  ? 0.4123 0.6343 0.5484 0.0940  0.0766  -0.0843 762  ASP B CG  
14318 O OD1 . ASP B 764  ? 0.4098 0.6364 0.5392 0.0905  0.0815  -0.0818 762  ASP B OD1 
14319 O OD2 . ASP B 764  ? 0.4899 0.7231 0.6371 0.1004  0.0789  -0.0859 762  ASP B OD2 
14320 N N   . GLY B 765  ? 0.3360 0.5410 0.4667 0.0725  0.0675  -0.0723 763  GLY B N   
14321 C CA  . GLY B 765  ? 0.2992 0.5095 0.4322 0.0643  0.0691  -0.0654 763  GLY B CA  
14322 C C   . GLY B 765  ? 0.2988 0.5241 0.4325 0.0643  0.0774  -0.0628 763  GLY B C   
14323 O O   . GLY B 765  ? 0.3342 0.5609 0.4649 0.0578  0.0790  -0.0577 763  GLY B O   
14324 N N   . ARG B 766  ? 0.2570 0.4936 0.3943 0.0715  0.0827  -0.0659 764  ARG B N   
14325 C CA  . ARG B 766  ? 0.3134 0.5639 0.4489 0.0722  0.0912  -0.0640 764  ARG B CA  
14326 C C   . ARG B 766  ? 0.3029 0.5441 0.4200 0.0719  0.0928  -0.0663 764  ARG B C   
14327 O O   . ARG B 766  ? 0.2980 0.5465 0.4110 0.0684  0.0979  -0.0623 764  ARG B O   
14328 C CB  . ARG B 766  ? 0.2950 0.5590 0.4373 0.0811  0.0967  -0.0678 764  ARG B CB  
14329 N N   . VAL B 767  ? 0.3431 0.5684 0.4489 0.0754  0.0883  -0.0726 765  VAL B N   
14330 C CA  . VAL B 767  ? 0.3189 0.5343 0.4074 0.0744  0.0885  -0.0747 765  VAL B CA  
14331 C C   . VAL B 767  ? 0.2909 0.4997 0.3762 0.0653  0.0852  -0.0688 765  VAL B C   
14332 O O   . VAL B 767  ? 0.3153 0.5263 0.3928 0.0619  0.0885  -0.0659 765  VAL B O   
14333 C CB  . VAL B 767  ? 0.2952 0.4950 0.3735 0.0800  0.0839  -0.0826 765  VAL B CB  
14334 C CG1 . VAL B 767  ? 0.2825 0.4712 0.3430 0.0781  0.0830  -0.0845 765  VAL B CG1 
14335 C CG2 . VAL B 767  ? 0.2840 0.4901 0.3642 0.0899  0.0876  -0.0887 765  VAL B CG2 
14336 N N   . GLY B 768  ? 0.2752 0.4758 0.3662 0.0614  0.0787  -0.0671 766  GLY B N   
14337 C CA  . GLY B 768  ? 0.2862 0.4813 0.3754 0.0532  0.0757  -0.0616 766  GLY B CA  
14338 C C   . GLY B 768  ? 0.2690 0.4772 0.3644 0.0483  0.0805  -0.0545 766  GLY B C   
14339 O O   . GLY B 768  ? 0.2875 0.4935 0.3756 0.0436  0.0813  -0.0509 766  GLY B O   
14340 N N   . ALA B 769  ? 0.2867 0.5088 0.3958 0.0493  0.0837  -0.0522 767  ALA B N   
14341 C CA  . ALA B 769  ? 0.2817 0.5165 0.3981 0.0439  0.0879  -0.0448 767  ALA B CA  
14342 C C   . ALA B 769  ? 0.2914 0.5333 0.3984 0.0447  0.0949  -0.0439 767  ALA B C   
14343 O O   . ALA B 769  ? 0.2875 0.5311 0.3917 0.0387  0.0964  -0.0380 767  ALA B O   
14344 C CB  . ALA B 769  ? 0.2784 0.5278 0.4121 0.0451  0.0899  -0.0428 767  ALA B CB  
14345 N N   . ALA B 770  ? 0.2381 0.4837 0.3395 0.0523  0.0991  -0.0496 768  ALA B N   
14346 C CA  . ALA B 770  ? 0.2876 0.5386 0.3777 0.0538  0.1055  -0.0497 768  ALA B CA  
14347 C C   . ALA B 770  ? 0.2987 0.5363 0.3737 0.0499  0.1024  -0.0492 768  ALA B C   
14348 O O   . ALA B 770  ? 0.2811 0.5232 0.3496 0.0466  0.1063  -0.0450 768  ALA B O   
14349 C CB  . ALA B 770  ? 0.2865 0.5406 0.3716 0.0634  0.1093  -0.0574 768  ALA B CB  
14350 N N   . LEU B 771  ? 0.2755 0.4970 0.3447 0.0501  0.0954  -0.0533 769  LEU B N   
14351 C CA  . LEU B 771  ? 0.2752 0.4848 0.3312 0.0463  0.0922  -0.0527 769  LEU B CA  
14352 C C   . LEU B 771  ? 0.2737 0.4839 0.3339 0.0381  0.0908  -0.0446 769  LEU B C   
14353 O O   . LEU B 771  ? 0.3157 0.5260 0.3676 0.0348  0.0926  -0.0411 769  LEU B O   
14354 C CB  . LEU B 771  ? 0.2546 0.4478 0.3049 0.0480  0.0851  -0.0583 769  LEU B CB  
14355 C CG  . LEU B 771  ? 0.2594 0.4481 0.3022 0.0557  0.0852  -0.0667 769  LEU B CG  
14356 C CD1 . LEU B 771  ? 0.2914 0.4643 0.3312 0.0563  0.0776  -0.0709 769  LEU B CD1 
14357 C CD2 . LEU B 771  ? 0.2621 0.4508 0.2899 0.0577  0.0889  -0.0689 769  LEU B CD2 
14358 N N   . VAL B 772  ? 0.2528 0.4627 0.3254 0.0350  0.0873  -0.0418 770  VAL B N   
14359 C CA  . VAL B 772  ? 0.2972 0.5058 0.3740 0.0274  0.0851  -0.0346 770  VAL B CA  
14360 C C   . VAL B 772  ? 0.3005 0.5219 0.3793 0.0241  0.0912  -0.0282 770  VAL B C   
14361 O O   . VAL B 772  ? 0.3103 0.5288 0.3850 0.0187  0.0905  -0.0229 770  VAL B O   
14362 C CB  . VAL B 772  ? 0.2681 0.4752 0.3582 0.0253  0.0804  -0.0334 770  VAL B CB  
14363 C CG1 . VAL B 772  ? 0.2961 0.5045 0.3922 0.0178  0.0791  -0.0257 770  VAL B CG1 
14364 C CG2 . VAL B 772  ? 0.2698 0.4619 0.3554 0.0268  0.0736  -0.0383 770  VAL B CG2 
14365 N N   . ALA B 773  ? 0.3149 0.5506 0.4000 0.0274  0.0973  -0.0283 771  ALA B N   
14366 C CA  . ALA B 773  ? 0.3128 0.5625 0.4017 0.0240  0.1035  -0.0215 771  ALA B CA  
14367 C C   . ALA B 773  ? 0.3811 0.6332 0.4557 0.0254  0.1086  -0.0214 771  ALA B C   
14368 O O   . ALA B 773  ? 0.4043 0.6659 0.4795 0.0215  0.1132  -0.0149 771  ALA B O   
14369 C CB  . ALA B 773  ? 0.3414 0.6074 0.4445 0.0267  0.1082  -0.0211 771  ALA B CB  
14370 N N   . ALA B 774  ? 0.3504 0.5939 0.4119 0.0305  0.1076  -0.0283 772  ALA B N   
14371 C CA  . ALA B 774  ? 0.3871 0.6322 0.4339 0.0321  0.1119  -0.0289 772  ALA B CA  
14372 C C   . ALA B 774  ? 0.3910 0.6324 0.4317 0.0251  0.1108  -0.0218 772  ALA B C   
14373 O O   . ALA B 774  ? 0.3752 0.6061 0.4173 0.0206  0.1046  -0.0196 772  ALA B O   
14374 C CB  . ALA B 774  ? 0.3946 0.6279 0.4284 0.0379  0.1090  -0.0376 772  ALA B CB  
14375 N N   . ALA B 775  ? 0.4132 0.6633 0.4466 0.0246  0.1168  -0.0185 773  ALA B N   
14376 C CA  . ALA B 775  ? 0.4397 0.6882 0.4682 0.0179  0.1164  -0.0106 773  ALA B CA  
14377 C C   . ALA B 775  ? 0.4105 0.6428 0.4274 0.0166  0.1098  -0.0124 773  ALA B C   
14378 O O   . ALA B 775  ? 0.4148 0.6409 0.4330 0.0108  0.1058  -0.0069 773  ALA B O   
14379 C CB  . ALA B 775  ? 0.3792 0.6402 0.4004 0.0185  0.1244  -0.0073 773  ALA B CB  
14380 N N   . GLU B 776  ? 0.3857 0.6108 0.3917 0.0219  0.1082  -0.0201 774  GLU B N   
14381 C CA  . GLU B 776  ? 0.3696 0.5809 0.3638 0.0207  0.1024  -0.0217 774  GLU B CA  
14382 C C   . GLU B 776  ? 0.3485 0.5476 0.3482 0.0198  0.0948  -0.0245 774  GLU B C   
14383 O O   . GLU B 776  ? 0.3497 0.5378 0.3412 0.0188  0.0897  -0.0258 774  GLU B O   
14384 C CB  . GLU B 776  ? 0.3741 0.5832 0.3532 0.0262  0.1039  -0.0284 774  GLU B CB  
14385 C CG  . GLU B 776  ? 0.4482 0.6694 0.4201 0.0277  0.1118  -0.0263 774  GLU B CG  
14386 C CD  . GLU B 776  ? 0.4859 0.7187 0.4631 0.0336  0.1182  -0.0304 774  GLU B CD  
14387 O OE1 . GLU B 776  ? 0.4676 0.7005 0.4566 0.0358  0.1168  -0.0335 774  GLU B OE1 
14388 O OE2 . GLU B 776  ? 0.5190 0.7614 0.4886 0.0363  0.1249  -0.0303 774  GLU B OE2 
14389 N N   . THR B 777  ? 0.3229 0.5241 0.3362 0.0200  0.0939  -0.0250 775  THR B N   
14390 C CA  . THR B 777  ? 0.3055 0.4956 0.3238 0.0191  0.0870  -0.0272 775  THR B CA  
14391 C C   . THR B 777  ? 0.3336 0.5180 0.3537 0.0128  0.0831  -0.0209 775  THR B C   
14392 O O   . THR B 777  ? 0.3460 0.5366 0.3732 0.0087  0.0850  -0.0143 775  THR B O   
14393 C CB  . THR B 777  ? 0.2939 0.4885 0.3261 0.0209  0.0872  -0.0290 775  THR B CB  
14394 O OG1 . THR B 777  ? 0.3275 0.5248 0.3571 0.0276  0.0897  -0.0359 775  THR B OG1 
14395 C CG2 . THR B 777  ? 0.2593 0.4432 0.2971 0.0191  0.0802  -0.0300 775  THR B CG2 
14396 N N   . ALA B 778  ? 0.3067 0.4795 0.3203 0.0122  0.0775  -0.0227 776  ALA B N   
14397 C CA  . ALA B 778  ? 0.2925 0.4591 0.3053 0.0073  0.0738  -0.0173 776  ALA B CA  
14398 C C   . ALA B 778  ? 0.2755 0.4338 0.2958 0.0059  0.0681  -0.0181 776  ALA B C   
14399 O O   . ALA B 778  ? 0.2985 0.4515 0.3194 0.0023  0.0648  -0.0140 776  ALA B O   
14400 C CB  . ALA B 778  ? 0.3142 0.4750 0.3134 0.0074  0.0719  -0.0180 776  ALA B CB  
14401 N N   . GLY B 779  ? 0.2771 0.4342 0.3028 0.0088  0.0669  -0.0232 777  GLY B N   
14402 C CA  . GLY B 779  ? 0.2658 0.4152 0.2977 0.0078  0.0616  -0.0242 777  GLY B CA  
14403 C C   . GLY B 779  ? 0.2492 0.3988 0.2858 0.0118  0.0613  -0.0299 777  GLY B C   
14404 O O   . GLY B 779  ? 0.2548 0.4075 0.2872 0.0159  0.0639  -0.0343 777  GLY B O   
14405 N N   . VAL B 780  ? 0.2376 0.3834 0.2824 0.0108  0.0576  -0.0300 778  VAL B N   
14406 C CA  . VAL B 780  ? 0.2447 0.3903 0.2949 0.0144  0.0567  -0.0348 778  VAL B CA  
14407 C C   . VAL B 780  ? 0.2119 0.3471 0.2630 0.0135  0.0507  -0.0364 778  VAL B C   
14408 O O   . VAL B 780  ? 0.2369 0.3688 0.2910 0.0099  0.0481  -0.0327 778  VAL B O   
14409 C CB  . VAL B 780  ? 0.2294 0.3848 0.2918 0.0144  0.0594  -0.0329 778  VAL B CB  
14410 C CG1 . VAL B 780  ? 0.2257 0.3799 0.2938 0.0182  0.0574  -0.0377 778  VAL B CG1 
14411 C CG2 . VAL B 780  ? 0.2341 0.4015 0.2960 0.0156  0.0660  -0.0314 778  VAL B CG2 
14412 N N   . MET B 781  ? 0.2181 0.3479 0.2661 0.0169  0.0485  -0.0418 779  MET B N   
14413 C CA  . MET B 781  ? 0.2419 0.3625 0.2908 0.0165  0.0431  -0.0435 779  MET B CA  
14414 C C   . MET B 781  ? 0.2630 0.3846 0.3189 0.0197  0.0423  -0.0468 779  MET B C   
14415 O O   . MET B 781  ? 0.2602 0.3836 0.3140 0.0238  0.0441  -0.0509 779  MET B O   
14416 C CB  . MET B 781  ? 0.2357 0.3481 0.2742 0.0170  0.0405  -0.0463 779  MET B CB  
14417 C CG  . MET B 781  ? 0.2523 0.3646 0.2841 0.0143  0.0413  -0.0430 779  MET B CG  
14418 S SD  . MET B 781  ? 0.2979 0.4023 0.3183 0.0149  0.0382  -0.0463 779  MET B SD  
14419 C CE  . MET B 781  ? 0.2799 0.3758 0.3035 0.0132  0.0328  -0.0464 779  MET B CE  
14420 N N   . PHE B 782  ? 0.2518 0.3723 0.3158 0.0180  0.0396  -0.0451 780  PHE B N   
14421 C CA  . PHE B 782  ? 0.2059 0.3292 0.2782 0.0207  0.0389  -0.0472 780  PHE B CA  
14422 C C   . PHE B 782  ? 0.2551 0.3697 0.3292 0.0198  0.0333  -0.0480 780  PHE B C   
14423 O O   . PHE B 782  ? 0.2726 0.3836 0.3471 0.0162  0.0309  -0.0449 780  PHE B O   
14424 C CB  . PHE B 782  ? 0.2389 0.3727 0.3218 0.0192  0.0417  -0.0435 780  PHE B CB  
14425 C CG  . PHE B 782  ? 0.2376 0.3745 0.3304 0.0215  0.0400  -0.0451 780  PHE B CG  
14426 C CD1 . PHE B 782  ? 0.2302 0.3722 0.3252 0.0267  0.0424  -0.0489 780  PHE B CD1 
14427 C CD2 . PHE B 782  ? 0.2481 0.3820 0.3475 0.0188  0.0358  -0.0431 780  PHE B CD2 
14428 C CE1 . PHE B 782  ? 0.2586 0.4034 0.3630 0.0292  0.0405  -0.0503 780  PHE B CE1 
14429 C CE2 . PHE B 782  ? 0.2237 0.3603 0.3321 0.0209  0.0338  -0.0445 780  PHE B CE2 
14430 C CZ  . PHE B 782  ? 0.2661 0.4086 0.3775 0.0261  0.0361  -0.0479 780  PHE B CZ  
14431 N N   . THR B 783  ? 0.2311 0.3425 0.3061 0.0234  0.0311  -0.0519 781  THR B N   
14432 C CA  . THR B 783  ? 0.2575 0.3614 0.3345 0.0229  0.0259  -0.0525 781  THR B CA  
14433 C C   . THR B 783  ? 0.2588 0.3666 0.3441 0.0264  0.0253  -0.0546 781  THR B C   
14434 O O   . THR B 783  ? 0.2833 0.3924 0.3676 0.0308  0.0267  -0.0582 781  THR B O   
14435 C CB  . THR B 783  ? 0.2562 0.3496 0.3238 0.0232  0.0227  -0.0551 781  THR B CB  
14436 O OG1 . THR B 783  ? 0.2578 0.3490 0.3188 0.0200  0.0233  -0.0529 781  THR B OG1 
14437 C CG2 . THR B 783  ? 0.2960 0.3822 0.3653 0.0225  0.0176  -0.0553 781  THR B CG2 
14438 N N   . GLY B 784  ? 0.2523 0.3622 0.3461 0.0246  0.0231  -0.0522 782  GLY B N   
14439 C CA  . GLY B 784  ? 0.2399 0.3553 0.3433 0.0278  0.0224  -0.0535 782  GLY B CA  
14440 C C   . GLY B 784  ? 0.2586 0.3779 0.3714 0.0245  0.0204  -0.0499 782  GLY B C   
14441 O O   . GLY B 784  ? 0.2492 0.3629 0.3597 0.0204  0.0177  -0.0475 782  GLY B O   
14442 N N   . SER B 785  ? 0.2772 0.4066 0.4007 0.0263  0.0218  -0.0495 783  SER B N   
14443 C CA  . SER B 785  ? 0.2964 0.4295 0.4300 0.0234  0.0189  -0.0465 783  SER B CA  
14444 C C   . SER B 785  ? 0.3289 0.4668 0.4650 0.0180  0.0210  -0.0417 783  SER B C   
14445 O O   . SER B 785  ? 0.2618 0.4051 0.3957 0.0174  0.0261  -0.0404 783  SER B O   
14446 C CB  . SER B 785  ? 0.2904 0.4338 0.4357 0.0270  0.0196  -0.0473 783  SER B CB  
14447 O OG  . SER B 785  ? 0.3131 0.4691 0.4631 0.0277  0.0259  -0.0460 783  SER B OG  
14448 N N   . THR B 786  ? 0.3272 0.4622 0.4675 0.0140  0.0167  -0.0391 784  THR B N   
14449 C CA  . THR B 786  ? 0.3281 0.4666 0.4718 0.0087  0.0177  -0.0345 784  THR B CA  
14450 C C   . THR B 786  ? 0.2993 0.4526 0.4528 0.0084  0.0227  -0.0319 784  THR B C   
14451 O O   . THR B 786  ? 0.3147 0.4720 0.4674 0.0053  0.0263  -0.0284 784  THR B O   
14452 C CB  . THR B 786  ? 0.3372 0.4707 0.4853 0.0052  0.0116  -0.0328 784  THR B CB  
14453 O OG1 . THR B 786  ? 0.3731 0.4934 0.5107 0.0045  0.0080  -0.0342 784  THR B OG1 
14454 C CG2 . THR B 786  ? 0.3427 0.4814 0.4973 -0.0002 0.0122  -0.0279 784  THR B CG2 
14455 N N   . GLU B 787  ? 0.2977 0.4596 0.4605 0.0119  0.0231  -0.0333 785  GLU B N   
14456 C CA  . GLU B 787  ? 0.3007 0.4783 0.4746 0.0115  0.0277  -0.0305 785  GLU B CA  
14457 C C   . GLU B 787  ? 0.2940 0.4777 0.4624 0.0138  0.0350  -0.0309 785  GLU B C   
14458 O O   . GLU B 787  ? 0.2794 0.4722 0.4515 0.0107  0.0393  -0.0268 785  GLU B O   
14459 C CB  . GLU B 787  ? 0.3400 0.5255 0.5252 0.0156  0.0263  -0.0324 785  GLU B CB  
14460 N N   . VAL B 788  ? 0.2452 0.4235 0.4043 0.0190  0.0362  -0.0358 786  VAL B N   
14461 C CA  . VAL B 788  ? 0.2514 0.4342 0.4037 0.0213  0.0426  -0.0367 786  VAL B CA  
14462 C C   . VAL B 788  ? 0.2131 0.3904 0.3564 0.0164  0.0436  -0.0335 786  VAL B C   
14463 O O   . VAL B 788  ? 0.2885 0.4731 0.4302 0.0153  0.0490  -0.0310 786  VAL B O   
14464 C CB  . VAL B 788  ? 0.2755 0.4522 0.4196 0.0278  0.0427  -0.0429 786  VAL B CB  
14465 C CG1 . VAL B 788  ? 0.2616 0.4401 0.3958 0.0297  0.0484  -0.0442 786  VAL B CG1 
14466 C CG2 . VAL B 788  ? 0.3121 0.4957 0.4656 0.0333  0.0426  -0.0458 786  VAL B CG2 
14467 N N   . ALA B 789  ? 0.2573 0.4218 0.3946 0.0137  0.0385  -0.0334 787  ALA B N   
14468 C CA  . ALA B 789  ? 0.2673 0.4263 0.3965 0.0095  0.0390  -0.0304 787  ALA B CA  
14469 C C   . ALA B 789  ? 0.2616 0.4285 0.3979 0.0043  0.0410  -0.0243 787  ALA B C   
14470 O O   . ALA B 789  ? 0.2372 0.4058 0.3685 0.0021  0.0445  -0.0214 787  ALA B O   
14471 C CB  . ALA B 789  ? 0.2808 0.4260 0.4040 0.0077  0.0332  -0.0312 787  ALA B CB  
14472 N N   . ARG B 790  ? 0.2524 0.4237 0.4002 0.0020  0.0385  -0.0221 788  ARG B N   
14473 C CA  . ARG B 790  ? 0.2366 0.4158 0.3923 -0.0035 0.0400  -0.0161 788  ARG B CA  
14474 C C   . ARG B 790  ? 0.2283 0.4224 0.3881 -0.0022 0.0473  -0.0142 788  ARG B C   
14475 O O   . ARG B 790  ? 0.2742 0.4734 0.4343 -0.0063 0.0505  -0.0092 788  ARG B O   
14476 C CB  . ARG B 790  ? 0.3103 0.4908 0.4778 -0.0063 0.0350  -0.0144 788  ARG B CB  
14477 N N   . LEU B 791  ? 0.2206 0.4220 0.3834 0.0036  0.0500  -0.0182 789  LEU B N   
14478 C CA  . LEU B 791  ? 0.2525 0.4685 0.4181 0.0057  0.0574  -0.0170 789  LEU B CA  
14479 C C   . LEU B 791  ? 0.2848 0.4978 0.4370 0.0061  0.0616  -0.0169 789  LEU B C   
14480 O O   . LEU B 791  ? 0.2539 0.4762 0.4067 0.0038  0.0669  -0.0127 789  LEU B O   
14481 C CB  . LEU B 791  ? 0.2490 0.4717 0.4190 0.0129  0.0592  -0.0222 789  LEU B CB  
14482 C CG  . LEU B 791  ? 0.2962 0.5257 0.4812 0.0131  0.0561  -0.0217 789  LEU B CG  
14483 C CD1 . LEU B 791  ? 0.3049 0.5391 0.4924 0.0212  0.0575  -0.0274 789  LEU B CD1 
14484 C CD2 . LEU B 791  ? 0.3282 0.5728 0.5264 0.0082  0.0590  -0.0152 789  LEU B CD2 
14485 N N   . ILE B 792  ? 0.2437 0.4441 0.3839 0.0088  0.0592  -0.0215 790  ILE B N   
14486 C CA  . ILE B 792  ? 0.2410 0.4375 0.3680 0.0092  0.0622  -0.0217 790  ILE B CA  
14487 C C   . ILE B 792  ? 0.2779 0.4721 0.4030 0.0026  0.0618  -0.0154 790  ILE B C   
14488 O O   . ILE B 792  ? 0.3009 0.5004 0.4215 0.0012  0.0665  -0.0123 790  ILE B O   
14489 C CB  . ILE B 792  ? 0.2401 0.4230 0.3560 0.0125  0.0585  -0.0274 790  ILE B CB  
14490 C CG1 . ILE B 792  ? 0.2534 0.4385 0.3698 0.0194  0.0595  -0.0335 790  ILE B CG1 
14491 C CG2 . ILE B 792  ? 0.2576 0.4352 0.3603 0.0117  0.0601  -0.0269 790  ILE B CG2 
14492 C CD1 . ILE B 792  ? 0.2678 0.4393 0.3757 0.0221  0.0548  -0.0388 790  ILE B CD1 
14493 N N   . GLN B 793  ? 0.2396 0.4252 0.3675 -0.0013 0.0560  -0.0136 791  GLN B N   
14494 C CA  . GLN B 793  ? 0.2664 0.4480 0.3927 -0.0073 0.0547  -0.0079 791  GLN B CA  
14495 C C   . GLN B 793  ? 0.2646 0.4589 0.3987 -0.0112 0.0591  -0.0017 791  GLN B C   
14496 O O   . GLN B 793  ? 0.2873 0.4816 0.4167 -0.0146 0.0612  0.0029  791  GLN B O   
14497 C CB  . GLN B 793  ? 0.2945 0.4657 0.4240 -0.0101 0.0477  -0.0077 791  GLN B CB  
14498 C CG  . GLN B 793  ? 0.3095 0.4741 0.4371 -0.0158 0.0453  -0.0024 791  GLN B CG  
14499 C CD  . GLN B 793  ? 0.3649 0.5243 0.5003 -0.0193 0.0393  -0.0011 791  GLN B CD  
14500 O OE1 . GLN B 793  ? 0.3432 0.5091 0.4890 -0.0192 0.0384  -0.0017 791  GLN B OE1 
14501 N NE2 . GLN B 793  ? 0.3491 0.4968 0.4795 -0.0220 0.0351  0.0003  791  GLN B NE2 
14502 N N   . ALA B 794  ? 0.2712 0.4771 0.4176 -0.0107 0.0608  -0.0012 792  ALA B N   
14503 C CA  . ALA B 794  ? 0.2847 0.5043 0.4399 -0.0147 0.0652  0.0051  792  ALA B CA  
14504 C C   . ALA B 794  ? 0.3222 0.5517 0.4715 -0.0121 0.0730  0.0056  792  ALA B C   
14505 O O   . ALA B 794  ? 0.3425 0.5775 0.4911 -0.0164 0.0764  0.0117  792  ALA B O   
14506 C CB  . ALA B 794  ? 0.2794 0.5095 0.4503 -0.0149 0.0645  0.0056  792  ALA B CB  
14507 N N   . GLN B 795  ? 0.3099 0.5418 0.4545 -0.0050 0.0758  -0.0007 793  GLN B N   
14508 C CA  . GLN B 795  ? 0.2509 0.4902 0.3873 -0.0020 0.0828  -0.0011 793  GLN B CA  
14509 C C   . GLN B 795  ? 0.2912 0.5216 0.4144 -0.0049 0.0825  0.0015  793  GLN B C   
14510 O O   . GLN B 795  ? 0.2919 0.5296 0.4112 -0.0066 0.0877  0.0057  793  GLN B O   
14511 C CB  . GLN B 795  ? 0.2935 0.5323 0.4244 0.0063  0.0844  -0.0092 793  GLN B CB  
14512 C CG  . GLN B 795  ? 0.3958 0.6449 0.5384 0.0110  0.0859  -0.0124 793  GLN B CG  
14513 C CD  . GLN B 795  ? 0.4061 0.6513 0.5413 0.0193  0.0864  -0.0208 793  GLN B CD  
14514 O OE1 . GLN B 795  ? 0.3979 0.6501 0.5273 0.0238  0.0923  -0.0231 793  GLN B OE1 
14515 N NE2 . GLN B 795  ? 0.3751 0.6085 0.5098 0.0212  0.0801  -0.0253 793  GLN B NE2 
14516 N N   . LEU B 796  ? 0.2853 0.5002 0.4015 -0.0053 0.0765  -0.0008 794  LEU B N   
14517 C CA  . LEU B 796  ? 0.3044 0.5108 0.4078 -0.0071 0.0760  0.0009  794  LEU B CA  
14518 C C   . LEU B 796  ? 0.3332 0.5399 0.4393 -0.0141 0.0755  0.0091  794  LEU B C   
14519 O O   . LEU B 796  ? 0.3398 0.5459 0.4372 -0.0158 0.0777  0.0125  794  LEU B O   
14520 C CB  . LEU B 796  ? 0.3066 0.4976 0.4027 -0.0055 0.0699  -0.0037 794  LEU B CB  
14521 C CG  . LEU B 796  ? 0.2770 0.4653 0.3672 0.0010  0.0700  -0.0114 794  LEU B CG  
14522 C CD1 . LEU B 796  ? 0.2670 0.4406 0.3512 0.0016  0.0637  -0.0149 794  LEU B CD1 
14523 C CD2 . LEU B 796  ? 0.3007 0.4941 0.3809 0.0040  0.0754  -0.0127 794  LEU B CD2 
14524 N N   . ALA B 797  ? 0.2843 0.4914 0.4019 -0.0183 0.0723  0.0124  795  ALA B N   
14525 C CA  . ALA B 797  ? 0.3791 0.5839 0.4993 -0.0253 0.0706  0.0199  795  ALA B CA  
14526 C C   . ALA B 797  ? 0.3611 0.5794 0.4840 -0.0285 0.0770  0.0265  795  ALA B C   
14527 O O   . ALA B 797  ? 0.3932 0.6089 0.5151 -0.0342 0.0762  0.0332  795  ALA B O   
14528 C CB  . ALA B 797  ? 0.3634 0.5648 0.4952 -0.0290 0.0651  0.0212  795  ALA B CB  
14529 N N   . ASP B 798  ? 0.3511 0.5836 0.4773 -0.0251 0.0832  0.0250  796  ASP B N   
14530 C CA  . ASP B 798  ? 0.4006 0.6466 0.5279 -0.0279 0.0900  0.0313  796  ASP B CA  
14531 C C   . ASP B 798  ? 0.4372 0.6811 0.5490 -0.0262 0.0935  0.0317  796  ASP B C   
14532 O O   . ASP B 798  ? 0.4280 0.6808 0.5384 -0.0294 0.0985  0.0379  796  ASP B O   
14533 C CB  . ASP B 798  ? 0.4649 0.7283 0.6018 -0.0244 0.0959  0.0297  796  ASP B CB  
14534 C CG  . ASP B 798  ? 0.5889 0.8682 0.7299 -0.0283 0.1029  0.0373  796  ASP B CG  
14535 O OD1 . ASP B 798  ? 0.6346 0.9130 0.7797 -0.0359 0.1012  0.0452  796  ASP B OD1 
14536 O OD2 . ASP B 798  ? 0.6454 0.9379 0.7854 -0.0237 0.1100  0.0355  796  ASP B OD2 
14537 N N   . ARG B 799  ? 0.4229 0.6554 0.5231 -0.0217 0.0908  0.0255  797  ARG B N   
14538 C CA  . ARG B 799  ? 0.4465 0.6767 0.5317 -0.0197 0.0934  0.0250  797  ARG B CA  
14539 C C   . ARG B 799  ? 0.4011 0.6159 0.4782 -0.0224 0.0875  0.0267  797  ARG B C   
14540 O O   . ARG B 799  ? 0.3944 0.5990 0.4758 -0.0239 0.0813  0.0258  797  ARG B O   
14541 C CB  . ARG B 799  ? 0.4368 0.6670 0.5144 -0.0119 0.0953  0.0162  797  ARG B CB  
14542 C CG  . ARG B 799  ? 0.4606 0.7028 0.5473 -0.0075 0.0993  0.0122  797  ARG B CG  
14543 C CD  . ARG B 799  ? 0.5045 0.7487 0.5810 0.0001  0.1030  0.0049  797  ARG B CD  
14544 N NE  . ARG B 799  ? 0.4190 0.6508 0.4911 0.0045  0.0977  -0.0029 797  ARG B NE  
14545 C CZ  . ARG B 799  ? 0.4443 0.6642 0.5036 0.0054  0.0944  -0.0057 797  ARG B CZ  
14546 N NH1 . ARG B 799  ? 0.4671 0.6855 0.5161 0.0029  0.0956  -0.0019 797  ARG B NH1 
14547 N NH2 . ARG B 799  ? 0.4506 0.6600 0.5075 0.0087  0.0895  -0.0122 797  ARG B NH2 
14548 N N   . LEU B 800  ? 0.3653 0.5787 0.4305 -0.0229 0.0894  0.0293  798  LEU B N   
14549 C CA  . LEU B 800  ? 0.4244 0.6239 0.4802 -0.0238 0.0842  0.0298  798  LEU B CA  
14550 C C   . LEU B 800  ? 0.4258 0.6232 0.4675 -0.0189 0.0856  0.0249  798  LEU B C   
14551 O O   . LEU B 800  ? 0.4578 0.6648 0.4954 -0.0158 0.0912  0.0229  798  LEU B O   
14552 C CB  . LEU B 800  ? 0.4543 0.6520 0.5089 -0.0300 0.0836  0.0389  798  LEU B CB  
14553 C CG  . LEU B 800  ? 0.4168 0.6113 0.4831 -0.0357 0.0799  0.0441  798  LEU B CG  
14554 C CD1 . LEU B 800  ? 0.4383 0.6303 0.5012 -0.0414 0.0794  0.0531  798  LEU B CD1 
14555 C CD2 . LEU B 800  ? 0.4029 0.5842 0.4714 -0.0344 0.0728  0.0395  798  LEU B CD2 
14556 N N   . SER B 801  ? 0.4546 0.6396 0.4890 -0.0181 0.0802  0.0227  799  SER B N   
14557 C CA  . SER B 801  ? 0.5073 0.6895 0.5282 -0.0145 0.0805  0.0190  799  SER B CA  
14558 C C   . SER B 801  ? 0.5752 0.7625 0.5876 -0.0168 0.0843  0.0251  799  SER B C   
14559 O O   . SER B 801  ? 0.5373 0.7279 0.5543 -0.0216 0.0855  0.0327  799  SER B O   
14560 C CB  . SER B 801  ? 0.4993 0.6681 0.5157 -0.0139 0.0738  0.0166  799  SER B CB  
14561 O OG  . SER B 801  ? 0.4913 0.6544 0.5069 -0.0181 0.0708  0.0231  799  SER B OG  
14562 N N   . PRO B 802  ? 0.6369 0.8250 0.6366 -0.0135 0.0861  0.0221  800  PRO B N   
14563 C CA  . PRO B 802  ? 0.5870 0.7790 0.5771 -0.0157 0.0892  0.0281  800  PRO B CA  
14564 C C   . PRO B 802  ? 0.6127 0.7971 0.6023 -0.0205 0.0849  0.0355  800  PRO B C   
14565 O O   . PRO B 802  ? 0.6713 0.8602 0.6593 -0.0244 0.0876  0.0431  800  PRO B O   
14566 C CB  . PRO B 802  ? 0.6518 0.8415 0.6277 -0.0110 0.0892  0.0222  800  PRO B CB  
14567 C CG  . PRO B 802  ? 0.6715 0.8616 0.6512 -0.0062 0.0894  0.0135  800  PRO B CG  
14568 C CD  . PRO B 802  ? 0.5679 0.7533 0.5611 -0.0079 0.0854  0.0133  800  PRO B CD  
14569 N N   . ALA B 803  ? 0.5710 0.7438 0.5620 -0.0204 0.0783  0.0335  801  ALA B N   
14570 C CA  . ALA B 803  ? 0.5597 0.7242 0.5511 -0.0241 0.0736  0.0396  801  ALA B CA  
14571 C C   . ALA B 803  ? 0.5761 0.7398 0.5803 -0.0284 0.0725  0.0443  801  ALA B C   
14572 O O   . ALA B 803  ? 0.5583 0.7134 0.5638 -0.0311 0.0679  0.0486  801  ALA B O   
14573 C CB  . ALA B 803  ? 0.5320 0.6853 0.5199 -0.0217 0.0672  0.0353  801  ALA B CB  
14574 N N   . GLY B 804  ? 0.5039 0.6760 0.5176 -0.0289 0.0762  0.0433  802  GLY B N   
14575 C CA  . GLY B 804  ? 0.4894 0.6618 0.5152 -0.0335 0.0752  0.0481  802  GLY B CA  
14576 C C   . GLY B 804  ? 0.4498 0.6121 0.4831 -0.0333 0.0691  0.0449  802  GLY B C   
14577 O O   . GLY B 804  ? 0.4006 0.5575 0.4399 -0.0375 0.0658  0.0496  802  GLY B O   
14578 N N   . ARG B 805  ? 0.4574 0.6167 0.4899 -0.0286 0.0674  0.0369  803  ARG B N   
14579 C CA  . ARG B 805  ? 0.4145 0.5645 0.4528 -0.0279 0.0619  0.0333  803  ARG B CA  
14580 C C   . ARG B 805  ? 0.3931 0.5481 0.4390 -0.0253 0.0632  0.0273  803  ARG B C   
14581 O O   . ARG B 805  ? 0.4122 0.5760 0.4564 -0.0225 0.0678  0.0243  803  ARG B O   
14582 C CB  . ARG B 805  ? 0.4925 0.6325 0.5223 -0.0248 0.0575  0.0297  803  ARG B CB  
14583 C CG  . ARG B 805  ? 0.4915 0.6257 0.5144 -0.0268 0.0553  0.0355  803  ARG B CG  
14584 C CD  . ARG B 805  ? 0.4965 0.6248 0.5260 -0.0313 0.0522  0.0414  803  ARG B CD  
14585 N NE  . ARG B 805  ? 0.5881 0.7091 0.6111 -0.0325 0.0492  0.0465  803  ARG B NE  
14586 C CZ  . ARG B 805  ? 0.5530 0.6754 0.5740 -0.0364 0.0506  0.0541  803  ARG B CZ  
14587 N NH1 . ARG B 805  ? 0.5423 0.6742 0.5676 -0.0399 0.0552  0.0581  803  ARG B NH1 
14588 N NH2 . ARG B 805  ? 0.5629 0.6775 0.5778 -0.0369 0.0471  0.0582  803  ARG B NH2 
14589 N N   . PRO B 806  ? 0.3760 0.5257 0.4303 -0.0259 0.0591  0.0256  804  PRO B N   
14590 C CA  . PRO B 806  ? 0.3738 0.5282 0.4357 -0.0235 0.0600  0.0204  804  PRO B CA  
14591 C C   . PRO B 806  ? 0.3353 0.4889 0.3906 -0.0180 0.0604  0.0130  804  PRO B C   
14592 O O   . PRO B 806  ? 0.3155 0.4611 0.3626 -0.0162 0.0576  0.0108  804  PRO B O   
14593 C CB  . PRO B 806  ? 0.3579 0.5036 0.4270 -0.0254 0.0543  0.0201  804  PRO B CB  
14594 C CG  . PRO B 806  ? 0.3887 0.5291 0.4574 -0.0301 0.0521  0.0270  804  PRO B CG  
14595 C CD  . PRO B 806  ? 0.3897 0.5292 0.4472 -0.0291 0.0538  0.0289  804  PRO B CD  
14596 N N   . ILE B 807  ? 0.3279 0.4898 0.3870 -0.0152 0.0639  0.0094  805  ILE B N   
14597 C CA  . ILE B 807  ? 0.3028 0.4635 0.3558 -0.0099 0.0642  0.0022  805  ILE B CA  
14598 C C   . ILE B 807  ? 0.3295 0.4814 0.3858 -0.0084 0.0589  -0.0024 805  ILE B C   
14599 O O   . ILE B 807  ? 0.2897 0.4425 0.3559 -0.0094 0.0574  -0.0023 805  ILE B O   
14600 C CB  . ILE B 807  ? 0.3556 0.5278 0.4114 -0.0069 0.0697  -0.0003 805  ILE B CB  
14601 C CG1 . ILE B 807  ? 0.3473 0.5284 0.3981 -0.0081 0.0753  0.0041  805  ILE B CG1 
14602 C CG2 . ILE B 807  ? 0.2889 0.4580 0.3390 -0.0013 0.0691  -0.0082 805  ILE B CG2 
14603 C CD1 . ILE B 807  ? 0.4373 0.6310 0.4920 -0.0055 0.0813  0.0027  805  ILE B CD1 
14604 N N   . PRO B 808  ? 0.3125 0.4561 0.3609 -0.0062 0.0558  -0.0060 806  PRO B N   
14605 C CA  . PRO B 808  ? 0.3048 0.4399 0.3558 -0.0053 0.0508  -0.0094 806  PRO B CA  
14606 C C   . PRO B 808  ? 0.3245 0.4619 0.3807 -0.0022 0.0510  -0.0146 806  PRO B C   
14607 O O   . PRO B 808  ? 0.3005 0.4431 0.3541 0.0010  0.0542  -0.0179 806  PRO B O   
14608 C CB  . PRO B 808  ? 0.3057 0.4336 0.3465 -0.0038 0.0484  -0.0116 806  PRO B CB  
14609 C CG  . PRO B 808  ? 0.3657 0.4965 0.3998 -0.0053 0.0509  -0.0075 806  PRO B CG  
14610 C CD  . PRO B 808  ? 0.2931 0.4345 0.3299 -0.0053 0.0563  -0.0061 806  PRO B CD  
14611 N N   . LEU B 809  ? 0.2957 0.4286 0.3585 -0.0028 0.0472  -0.0155 807  LEU B N   
14612 C CA  . LEU B 809  ? 0.2732 0.4070 0.3412 0.0001  0.0463  -0.0201 807  LEU B CA  
14613 C C   . LEU B 809  ? 0.2722 0.3957 0.3386 0.0005  0.0410  -0.0227 807  LEU B C   
14614 O O   . LEU B 809  ? 0.2982 0.4166 0.3669 -0.0022 0.0380  -0.0201 807  LEU B O   
14615 C CB  . LEU B 809  ? 0.2730 0.4140 0.3527 -0.0015 0.0473  -0.0179 807  LEU B CB  
14616 C CG  . LEU B 809  ? 0.2452 0.3856 0.3315 0.0010  0.0449  -0.0219 807  LEU B CG  
14617 C CD1 . LEU B 809  ? 0.2937 0.4359 0.3761 0.0062  0.0468  -0.0275 807  LEU B CD1 
14618 C CD2 . LEU B 809  ? 0.2841 0.4327 0.3830 -0.0010 0.0456  -0.0191 807  LEU B CD2 
14619 N N   . ILE B 810  ? 0.2352 0.3552 0.2972 0.0038  0.0399  -0.0277 808  ILE B N   
14620 C CA  . ILE B 810  ? 0.2719 0.3833 0.3332 0.0044  0.0352  -0.0302 808  ILE B CA  
14621 C C   . ILE B 810  ? 0.2825 0.3953 0.3500 0.0067  0.0344  -0.0335 808  ILE B C   
14622 O O   . ILE B 810  ? 0.2993 0.4149 0.3654 0.0100  0.0362  -0.0370 808  ILE B O   
14623 C CB  . ILE B 810  ? 0.2810 0.3864 0.3327 0.0057  0.0338  -0.0328 808  ILE B CB  
14624 C CG1 . ILE B 810  ? 0.2347 0.3395 0.2807 0.0036  0.0345  -0.0293 808  ILE B CG1 
14625 C CG2 . ILE B 810  ? 0.2813 0.3789 0.3330 0.0059  0.0293  -0.0348 808  ILE B CG2 
14626 C CD1 . ILE B 810  ? 0.3164 0.4162 0.3537 0.0046  0.0327  -0.0316 808  ILE B CD1 
14627 N N   . ALA B 811  ? 0.2742 0.3847 0.3483 0.0053  0.0313  -0.0325 809  ALA B N   
14628 C CA  . ALA B 811  ? 0.2492 0.3619 0.3307 0.0071  0.0301  -0.0347 809  ALA B CA  
14629 C C   . ALA B 811  ? 0.3191 0.4229 0.4000 0.0070  0.0249  -0.0363 809  ALA B C   
14630 O O   . ALA B 811  ? 0.3628 0.4626 0.4447 0.0043  0.0224  -0.0339 809  ALA B O   
14631 C CB  . ALA B 811  ? 0.2701 0.3910 0.3618 0.0050  0.0316  -0.0314 809  ALA B CB  
14632 N N   . GLU B 812  ? 0.2764 0.3768 0.3550 0.0100  0.0233  -0.0402 810  GLU B N   
14633 C CA  . GLU B 812  ? 0.3005 0.3931 0.3786 0.0101  0.0186  -0.0417 810  GLU B CA  
14634 C C   . GLU B 812  ? 0.3100 0.4056 0.3962 0.0120  0.0171  -0.0432 810  GLU B C   
14635 O O   . GLU B 812  ? 0.2655 0.3653 0.3535 0.0153  0.0190  -0.0456 810  GLU B O   
14636 C CB  . GLU B 812  ? 0.3093 0.3950 0.3787 0.0116  0.0172  -0.0444 810  GLU B CB  
14637 N N   . THR B 813  ? 0.2716 0.3652 0.3628 0.0103  0.0136  -0.0419 811  THR B N   
14638 C CA  . THR B 813  ? 0.2709 0.3693 0.3715 0.0114  0.0123  -0.0423 811  THR B CA  
14639 C C   . THR B 813  ? 0.3645 0.4559 0.4657 0.0114  0.0067  -0.0432 811  THR B C   
14640 O O   . THR B 813  ? 0.3451 0.4393 0.4542 0.0105  0.0043  -0.0421 811  THR B O   
14641 C CB  . THR B 813  ? 0.3346 0.4415 0.4439 0.0087  0.0141  -0.0387 811  THR B CB  
14642 O OG1 . THR B 813  ? 0.2877 0.3896 0.3945 0.0047  0.0124  -0.0358 811  THR B OG1 
14643 C CG2 . THR B 813  ? 0.3161 0.4321 0.4262 0.0095  0.0200  -0.0379 811  THR B CG2 
14644 N N   . GLY B 814  ? 0.3373 0.4201 0.4304 0.0122  0.0044  -0.0450 812  GLY B N   
14645 C CA  . GLY B 814  ? 0.3925 0.4698 0.4865 0.0130  -0.0005 -0.0462 812  GLY B CA  
14646 C C   . GLY B 814  ? 0.3878 0.4611 0.4823 0.0100  -0.0041 -0.0443 812  GLY B C   
14647 O O   . GLY B 814  ? 0.3967 0.4701 0.4903 0.0073  -0.0030 -0.0421 812  GLY B O   
14648 N N   . GLY B 815  ? 0.3825 0.4516 0.4780 0.0107  -0.0087 -0.0452 813  GLY B N   
14649 C CA  . GLY B 815  ? 0.3725 0.4359 0.4662 0.0083  -0.0126 -0.0440 813  GLY B CA  
14650 C C   . GLY B 815  ? 0.3625 0.4228 0.4584 0.0093  -0.0178 -0.0450 813  GLY B C   
14651 O O   . GLY B 815  ? 0.4332 0.4944 0.5309 0.0121  -0.0186 -0.0466 813  GLY B O   
14652 N N   . GLN B 816  ? 0.3441 0.3999 0.4390 0.0071  -0.0216 -0.0441 814  GLN B N   
14653 C CA  . GLN B 816  ? 0.3273 0.3788 0.4225 0.0076  -0.0273 -0.0448 814  GLN B CA  
14654 C C   . GLN B 816  ? 0.2915 0.3333 0.3751 0.0072  -0.0292 -0.0453 814  GLN B C   
14655 O O   . GLN B 816  ? 0.3118 0.3490 0.3923 0.0054  -0.0317 -0.0448 814  GLN B O   
14656 C CB  . GLN B 816  ? 0.3539 0.4085 0.4573 0.0051  -0.0305 -0.0434 814  GLN B CB  
14657 C CG  . GLN B 816  ? 0.4240 0.4777 0.5316 0.0060  -0.0363 -0.0440 814  GLN B CG  
14658 C CD  . GLN B 816  ? 0.4252 0.4860 0.5408 0.0091  -0.0355 -0.0448 814  GLN B CD  
14659 O OE1 . GLN B 816  ? 0.4094 0.4674 0.5203 0.0121  -0.0346 -0.0463 814  GLN B OE1 
14660 N NE2 . GLN B 816  ? 0.4003 0.4703 0.5282 0.0086  -0.0360 -0.0437 814  GLN B NE2 
14661 N N   . ASN B 817  ? 0.2638 0.3023 0.3410 0.0090  -0.0280 -0.0463 815  ASN B N   
14662 C CA  . ASN B 817  ? 0.2563 0.2880 0.3226 0.0085  -0.0277 -0.0462 815  ASN B CA  
14663 C C   . ASN B 817  ? 0.2755 0.3003 0.3366 0.0086  -0.0327 -0.0465 815  ASN B C   
14664 O O   . ASN B 817  ? 0.2804 0.3041 0.3432 0.0100  -0.0357 -0.0470 815  ASN B O   
14665 C CB  . ASN B 817  ? 0.2389 0.2706 0.3011 0.0097  -0.0244 -0.0467 815  ASN B CB  
14666 C CG  . ASN B 817  ? 0.2722 0.3108 0.3392 0.0100  -0.0199 -0.0467 815  ASN B CG  
14667 O OD1 . ASN B 817  ? 0.2534 0.2948 0.3216 0.0085  -0.0175 -0.0457 815  ASN B OD1 
14668 N ND2 . ASN B 817  ? 0.2593 0.3004 0.3290 0.0121  -0.0189 -0.0480 815  ASN B ND2 
14669 N N   . ALA B 818  ? 0.2592 0.2791 0.3136 0.0074  -0.0336 -0.0462 816  ALA B N   
14670 C CA  . ALA B 818  ? 0.2571 0.2703 0.3050 0.0074  -0.0380 -0.0464 816  ALA B CA  
14671 C C   . ALA B 818  ? 0.2516 0.2604 0.2890 0.0078  -0.0364 -0.0462 816  ALA B C   
14672 O O   . ALA B 818  ? 0.2563 0.2667 0.2911 0.0077  -0.0321 -0.0458 816  ALA B O   
14673 C CB  . ALA B 818  ? 0.2492 0.2597 0.2968 0.0060  -0.0407 -0.0466 816  ALA B CB  
14674 N N   . MET B 819  ? 0.2394 0.2428 0.2706 0.0082  -0.0400 -0.0461 817  MET B N   
14675 C CA  . MET B 819  ? 0.2345 0.2337 0.2551 0.0083  -0.0388 -0.0455 817  MET B CA  
14676 C C   . MET B 819  ? 0.2919 0.2855 0.3060 0.0083  -0.0429 -0.0460 817  MET B C   
14677 O O   . MET B 819  ? 0.2938 0.2853 0.3101 0.0084  -0.0477 -0.0463 817  MET B O   
14678 C CB  . MET B 819  ? 0.2896 0.2877 0.3074 0.0086  -0.0387 -0.0445 817  MET B CB  
14679 C CG  . MET B 819  ? 0.3137 0.3082 0.3209 0.0082  -0.0378 -0.0432 817  MET B CG  
14680 S SD  . MET B 819  ? 0.3574 0.3487 0.3609 0.0078  -0.0395 -0.0415 817  MET B SD  
14681 C CE  . MET B 819  ? 0.3108 0.3069 0.3199 0.0075  -0.0352 -0.0416 817  MET B CE  
14682 N N   . ILE B 820  ? 0.2785 0.2696 0.2848 0.0085  -0.0411 -0.0461 818  ILE B N   
14683 C CA  . ILE B 820  ? 0.2561 0.2412 0.2543 0.0089  -0.0446 -0.0470 818  ILE B CA  
14684 C C   . ILE B 820  ? 0.2879 0.2704 0.2756 0.0095  -0.0435 -0.0459 818  ILE B C   
14685 O O   . ILE B 820  ? 0.2875 0.2727 0.2726 0.0096  -0.0389 -0.0449 818  ILE B O   
14686 C CB  . ILE B 820  ? 0.2505 0.2342 0.2473 0.0091  -0.0436 -0.0485 818  ILE B CB  
14687 C CG1 . ILE B 820  ? 0.3113 0.2972 0.3186 0.0079  -0.0455 -0.0490 818  ILE B CG1 
14688 C CG2 . ILE B 820  ? 0.2824 0.2590 0.2685 0.0101  -0.0467 -0.0498 818  ILE B CG2 
14689 C CD1 . ILE B 820  ? 0.3489 0.3324 0.3554 0.0077  -0.0451 -0.0502 818  ILE B CD1 
14690 N N   . VAL B 821  ? 0.3048 0.2823 0.2864 0.0096  -0.0479 -0.0458 819  VAL B N   
14691 C CA  . VAL B 821  ? 0.3077 0.2825 0.2791 0.0098  -0.0475 -0.0441 819  VAL B CA  
14692 C C   . VAL B 821  ? 0.3078 0.2769 0.2691 0.0108  -0.0504 -0.0455 819  VAL B C   
14693 O O   . VAL B 821  ? 0.3294 0.2948 0.2917 0.0108  -0.0558 -0.0467 819  VAL B O   
14694 C CB  . VAL B 821  ? 0.3065 0.2802 0.2796 0.0091  -0.0506 -0.0423 819  VAL B CB  
14695 C CG1 . VAL B 821  ? 0.3059 0.2764 0.2681 0.0087  -0.0505 -0.0399 819  VAL B CG1 
14696 C CG2 . VAL B 821  ? 0.2700 0.2486 0.2529 0.0085  -0.0481 -0.0416 819  VAL B CG2 
14697 N N   . ASP B 822  ? 0.3402 0.3088 0.2918 0.0119  -0.0470 -0.0453 820  ASP B N   
14698 C CA  . ASP B 822  ? 0.3493 0.3120 0.2897 0.0133  -0.0496 -0.0468 820  ASP B CA  
14699 C C   . ASP B 822  ? 0.3805 0.3413 0.3109 0.0131  -0.0501 -0.0443 820  ASP B C   
14700 O O   . ASP B 822  ? 0.3480 0.3116 0.2805 0.0116  -0.0487 -0.0413 820  ASP B O   
14701 C CB  . ASP B 822  ? 0.3515 0.3143 0.2875 0.0154  -0.0459 -0.0489 820  ASP B CB  
14702 C CG  . ASP B 822  ? 0.3909 0.3585 0.3217 0.0164  -0.0395 -0.0472 820  ASP B CG  
14703 O OD1 . ASP B 822  ? 0.3466 0.3170 0.2753 0.0152  -0.0378 -0.0441 820  ASP B OD1 
14704 O OD2 . ASP B 822  ? 0.4111 0.3797 0.3400 0.0186  -0.0361 -0.0488 820  ASP B OD2 
14705 N N   . SER B 823  ? 0.3704 0.3260 0.2892 0.0145  -0.0524 -0.0455 821  SER B N   
14706 C CA  . SER B 823  ? 0.4037 0.3569 0.3121 0.0141  -0.0535 -0.0429 821  SER B CA  
14707 C C   . SER B 823  ? 0.4264 0.3847 0.3297 0.0140  -0.0470 -0.0401 821  SER B C   
14708 O O   . SER B 823  ? 0.4290 0.3864 0.3246 0.0130  -0.0474 -0.0370 821  SER B O   
14709 C CB  . SER B 823  ? 0.4247 0.3709 0.3212 0.0158  -0.0577 -0.0452 821  SER B CB  
14710 O OG  . SER B 823  ? 0.4523 0.3979 0.3430 0.0184  -0.0546 -0.0483 821  SER B OG  
14711 N N   . SER B 824  ? 0.3627 0.3266 0.2700 0.0148  -0.0414 -0.0407 822  SER B N   
14712 C CA  . SER B 824  ? 0.3763 0.3463 0.2801 0.0145  -0.0354 -0.0377 822  SER B CA  
14713 C C   . SER B 824  ? 0.4157 0.3901 0.3281 0.0114  -0.0340 -0.0343 822  SER B C   
14714 O O   . SER B 824  ? 0.4060 0.3849 0.3156 0.0101  -0.0302 -0.0309 822  SER B O   
14715 C CB  . SER B 824  ? 0.3846 0.3589 0.2882 0.0173  -0.0301 -0.0398 822  SER B CB  
14716 O OG  . SER B 824  ? 0.3711 0.3496 0.2866 0.0166  -0.0281 -0.0403 822  SER B OG  
14717 N N   . ALA B 825  ? 0.3517 0.3251 0.2746 0.0103  -0.0369 -0.0351 823  ALA B N   
14718 C CA  . ALA B 825  ? 0.4170 0.3939 0.3480 0.0078  -0.0357 -0.0326 823  ALA B CA  
14719 C C   . ALA B 825  ? 0.4202 0.3942 0.3464 0.0056  -0.0381 -0.0289 823  ALA B C   
14720 O O   . ALA B 825  ? 0.4102 0.3787 0.3297 0.0059  -0.0424 -0.0286 823  ALA B O   
14721 C CB  . ALA B 825  ? 0.3687 0.3451 0.3112 0.0077  -0.0383 -0.0348 823  ALA B CB  
14722 N N   . LEU B 826  ? 0.4088 0.3861 0.3384 0.0031  -0.0358 -0.0259 824  LEU B N   
14723 C CA  . LEU B 826  ? 0.4300 0.4038 0.3560 0.0006  -0.0384 -0.0220 824  LEU B CA  
14724 C C   . LEU B 826  ? 0.4064 0.3754 0.3396 0.0004  -0.0436 -0.0228 824  LEU B C   
14725 O O   . LEU B 826  ? 0.3993 0.3705 0.3420 0.0002  -0.0428 -0.0241 824  LEU B O   
14726 C CB  . LEU B 826  ? 0.4444 0.4232 0.3707 -0.0023 -0.0342 -0.0183 824  LEU B CB  
14727 C CG  . LEU B 826  ? 0.5132 0.4878 0.4356 -0.0057 -0.0369 -0.0136 824  LEU B CG  
14728 C CD1 . LEU B 826  ? 0.5067 0.4784 0.4170 -0.0058 -0.0381 -0.0111 824  LEU B CD1 
14729 C CD2 . LEU B 826  ? 0.5476 0.5272 0.4725 -0.0091 -0.0333 -0.0103 824  LEU B CD2 
14730 N N   . ALA B 827  ? 0.3949 0.3574 0.3234 0.0006  -0.0490 -0.0221 825  ALA B N   
14731 C CA  . ALA B 827  ? 0.4054 0.3637 0.3411 0.0014  -0.0544 -0.0234 825  ALA B CA  
14732 C C   . ALA B 827  ? 0.4001 0.3582 0.3425 -0.0002 -0.0544 -0.0218 825  ALA B C   
14733 O O   . ALA B 827  ? 0.3953 0.3539 0.3473 0.0011  -0.0556 -0.0242 825  ALA B O   
14734 C CB  . ALA B 827  ? 0.4156 0.3671 0.3442 0.0017  -0.0603 -0.0220 825  ALA B CB  
14735 N N   . GLU B 828  ? 0.3774 0.3343 0.3145 -0.0030 -0.0534 -0.0177 826  GLU B N   
14736 C CA  . GLU B 828  ? 0.4019 0.3570 0.3442 -0.0047 -0.0540 -0.0163 826  GLU B CA  
14737 C C   . GLU B 828  ? 0.4237 0.3849 0.3747 -0.0044 -0.0498 -0.0189 826  GLU B C   
14738 O O   . GLU B 828  ? 0.4164 0.3762 0.3747 -0.0039 -0.0511 -0.0204 826  GLU B O   
14739 C CB  . GLU B 828  ? 0.4165 0.3698 0.3514 -0.0085 -0.0533 -0.0111 826  GLU B CB  
14740 C CG  . GLU B 828  ? 0.5036 0.4492 0.4303 -0.0094 -0.0585 -0.0076 826  GLU B CG  
14741 C CD  . GLU B 828  ? 0.5580 0.5042 0.4750 -0.0084 -0.0582 -0.0071 826  GLU B CD  
14742 O OE1 . GLU B 828  ? 0.4943 0.4467 0.4104 -0.0071 -0.0538 -0.0093 826  GLU B OE1 
14743 O OE2 . GLU B 828  ? 0.5804 0.5203 0.4904 -0.0088 -0.0628 -0.0045 826  GLU B OE2 
14744 N N   . GLN B 829  ? 0.3744 0.3423 0.3243 -0.0045 -0.0446 -0.0196 827  GLN B N   
14745 C CA  . GLN B 829  ? 0.3894 0.3631 0.3469 -0.0043 -0.0407 -0.0217 827  GLN B CA  
14746 C C   . GLN B 829  ? 0.3808 0.3552 0.3462 -0.0013 -0.0418 -0.0260 827  GLN B C   
14747 O O   . GLN B 829  ? 0.3340 0.3100 0.3069 -0.0009 -0.0412 -0.0277 827  GLN B O   
14748 C CB  . GLN B 829  ? 0.4128 0.3934 0.3671 -0.0048 -0.0352 -0.0211 827  GLN B CB  
14749 C CG  . GLN B 829  ? 0.4598 0.4467 0.4214 -0.0045 -0.0312 -0.0230 827  GLN B CG  
14750 C CD  . GLN B 829  ? 0.5056 0.4994 0.4641 -0.0044 -0.0261 -0.0223 827  GLN B CD  
14751 O OE1 . GLN B 829  ? 0.5290 0.5228 0.4805 -0.0035 -0.0254 -0.0216 827  GLN B OE1 
14752 N NE2 . GLN B 829  ? 0.5194 0.5189 0.4829 -0.0051 -0.0227 -0.0225 827  GLN B NE2 
14753 N N   . VAL B 830  ? 0.3542 0.3274 0.3177 0.0007  -0.0437 -0.0276 828  VAL B N   
14754 C CA  . VAL B 830  ? 0.3595 0.3334 0.3307 0.0031  -0.0455 -0.0311 828  VAL B CA  
14755 C C   . VAL B 830  ? 0.3543 0.3250 0.3318 0.0038  -0.0494 -0.0315 828  VAL B C   
14756 O O   . VAL B 830  ? 0.3092 0.2829 0.2955 0.0051  -0.0486 -0.0339 828  VAL B O   
14757 C CB  . VAL B 830  ? 0.3192 0.2909 0.2862 0.0045  -0.0482 -0.0322 828  VAL B CB  
14758 C CG1 . VAL B 830  ? 0.3373 0.3086 0.3126 0.0063  -0.0519 -0.0349 828  VAL B CG1 
14759 C CG2 . VAL B 830  ? 0.3711 0.3465 0.3345 0.0050  -0.0440 -0.0333 828  VAL B CG2 
14760 N N   . VAL B 831  ? 0.3293 0.2938 0.3023 0.0033  -0.0537 -0.0292 829  VAL B N   
14761 C CA  . VAL B 831  ? 0.3099 0.2708 0.2889 0.0048  -0.0579 -0.0299 829  VAL B CA  
14762 C C   . VAL B 831  ? 0.3056 0.2678 0.2898 0.0044  -0.0555 -0.0305 829  VAL B C   
14763 O O   . VAL B 831  ? 0.3401 0.3036 0.3326 0.0067  -0.0562 -0.0331 829  VAL B O   
14764 C CB  . VAL B 831  ? 0.3332 0.2864 0.3056 0.0043  -0.0633 -0.0270 829  VAL B CB  
14765 C CG1 . VAL B 831  ? 0.3539 0.3026 0.3319 0.0057  -0.0671 -0.0272 829  VAL B CG1 
14766 C CG2 . VAL B 831  ? 0.3261 0.2780 0.2961 0.0057  -0.0670 -0.0276 829  VAL B CG2 
14767 N N   . GLY B 832  ? 0.3335 0.2955 0.3127 0.0015  -0.0528 -0.0281 830  GLY B N   
14768 C CA  . GLY B 832  ? 0.3830 0.3458 0.3664 0.0008  -0.0508 -0.0289 830  GLY B CA  
14769 C C   . GLY B 832  ? 0.3763 0.3462 0.3670 0.0025  -0.0469 -0.0323 830  GLY B C   
14770 O O   . GLY B 832  ? 0.3551 0.3254 0.3518 0.0040  -0.0468 -0.0345 830  GLY B O   
14771 N N   . ASP B 833  ? 0.3079 0.2834 0.2980 0.0024  -0.0437 -0.0328 831  ASP B N   
14772 C CA  . ASP B 833  ? 0.3112 0.2931 0.3077 0.0035  -0.0399 -0.0354 831  ASP B CA  
14773 C C   . ASP B 833  ? 0.3358 0.3189 0.3399 0.0064  -0.0418 -0.0382 831  ASP B C   
14774 O O   . ASP B 833  ? 0.3406 0.3281 0.3514 0.0076  -0.0396 -0.0403 831  ASP B O   
14775 C CB  . ASP B 833  ? 0.2814 0.2679 0.2745 0.0027  -0.0362 -0.0349 831  ASP B CB  
14776 C CG  . ASP B 833  ? 0.3478 0.3359 0.3357 0.0000  -0.0332 -0.0323 831  ASP B CG  
14777 O OD1 . ASP B 833  ? 0.3639 0.3500 0.3518 -0.0017 -0.0338 -0.0312 831  ASP B OD1 
14778 O OD2 . ASP B 833  ? 0.3507 0.3422 0.3348 -0.0004 -0.0304 -0.0314 831  ASP B OD2 
14779 N N   . VAL B 834  ? 0.2390 0.2189 0.2425 0.0075  -0.0460 -0.0380 832  VAL B N   
14780 C CA  . VAL B 834  ? 0.3123 0.2941 0.3240 0.0101  -0.0482 -0.0402 832  VAL B CA  
14781 C C   . VAL B 834  ? 0.3286 0.3089 0.3457 0.0120  -0.0500 -0.0413 832  VAL B C   
14782 O O   . VAL B 834  ? 0.3371 0.3221 0.3625 0.0141  -0.0487 -0.0436 832  VAL B O   
14783 C CB  . VAL B 834  ? 0.3308 0.3095 0.3400 0.0105  -0.0528 -0.0396 832  VAL B CB  
14784 C CG1 . VAL B 834  ? 0.2985 0.2788 0.3168 0.0130  -0.0563 -0.0413 832  VAL B CG1 
14785 C CG2 . VAL B 834  ? 0.3078 0.2887 0.3134 0.0095  -0.0509 -0.0398 832  VAL B CG2 
14786 N N   . ILE B 835  ? 0.3267 0.3000 0.3389 0.0116  -0.0531 -0.0396 833  ILE B N   
14787 C CA  . ILE B 835  ? 0.3645 0.3346 0.3808 0.0139  -0.0554 -0.0408 833  ILE B CA  
14788 C C   . ILE B 835  ? 0.3836 0.3575 0.4037 0.0144  -0.0511 -0.0429 833  ILE B C   
14789 O O   . ILE B 835  ? 0.3561 0.3322 0.3832 0.0175  -0.0510 -0.0455 833  ILE B O   
14790 C CB  . ILE B 835  ? 0.4012 0.3620 0.4103 0.0126  -0.0593 -0.0381 833  ILE B CB  
14791 C CG1 . ILE B 835  ? 0.3965 0.3532 0.4023 0.0129  -0.0643 -0.0361 833  ILE B CG1 
14792 C CG2 . ILE B 835  ? 0.4120 0.3683 0.4244 0.0150  -0.0612 -0.0396 833  ILE B CG2 
14793 C CD1 . ILE B 835  ? 0.4519 0.4046 0.4626 0.0165  -0.0696 -0.0369 833  ILE B CD1 
14794 N N   . THR B 836  ? 0.3155 0.2907 0.3308 0.0114  -0.0474 -0.0418 834  THR B N   
14795 C CA  . THR B 836  ? 0.3311 0.3100 0.3490 0.0114  -0.0434 -0.0437 834  THR B CA  
14796 C C   . THR B 836  ? 0.3262 0.3136 0.3514 0.0132  -0.0401 -0.0460 834  THR B C   
14797 O O   . THR B 836  ? 0.3426 0.3327 0.3733 0.0157  -0.0388 -0.0485 834  THR B O   
14798 C CB  . THR B 836  ? 0.3785 0.3577 0.3900 0.0076  -0.0407 -0.0416 834  THR B CB  
14799 O OG1 . THR B 836  ? 0.4317 0.4034 0.4370 0.0054  -0.0438 -0.0390 834  THR B OG1 
14800 C CG2 . THR B 836  ? 0.3950 0.3778 0.4087 0.0075  -0.0371 -0.0434 834  THR B CG2 
14801 N N   . SER B 837  ? 0.2833 0.2744 0.3082 0.0121  -0.0388 -0.0451 835  SER B N   
14802 C CA  . SER B 837  ? 0.2831 0.2819 0.3144 0.0130  -0.0356 -0.0466 835  SER B CA  
14803 C C   . SER B 837  ? 0.2574 0.2590 0.2974 0.0161  -0.0373 -0.0484 835  SER B C   
14804 O O   . SER B 837  ? 0.2341 0.2418 0.2803 0.0174  -0.0343 -0.0501 835  SER B O   
14805 C CB  . SER B 837  ? 0.2539 0.2544 0.2824 0.0112  -0.0347 -0.0453 835  SER B CB  
14806 O OG  . SER B 837  ? 0.2967 0.2965 0.3185 0.0089  -0.0323 -0.0437 835  SER B OG  
14807 N N   . ALA B 838  ? 0.2578 0.2556 0.2985 0.0173  -0.0421 -0.0480 836  ALA B N   
14808 C CA  . ALA B 838  ? 0.2688 0.2704 0.3187 0.0202  -0.0440 -0.0494 836  ALA B CA  
14809 C C   . ALA B 838  ? 0.3004 0.3013 0.3545 0.0237  -0.0447 -0.0514 836  ALA B C   
14810 O O   . ALA B 838  ? 0.3121 0.3195 0.3751 0.0265  -0.0437 -0.0531 836  ALA B O   
14811 C CB  . ALA B 838  ? 0.2743 0.2725 0.3237 0.0203  -0.0494 -0.0482 836  ALA B CB  
14812 N N   . PHE B 839  ? 0.3178 0.3110 0.3658 0.0239  -0.0465 -0.0511 837  PHE B N   
14813 C CA  . PHE B 839  ? 0.3268 0.3169 0.3781 0.0278  -0.0488 -0.0531 837  PHE B CA  
14814 C C   . PHE B 839  ? 0.3337 0.3207 0.3814 0.0282  -0.0465 -0.0547 837  PHE B C   
14815 O O   . PHE B 839  ? 0.3304 0.3157 0.3813 0.0321  -0.0475 -0.0572 837  PHE B O   
14816 C CB  . PHE B 839  ? 0.3175 0.2991 0.3656 0.0285  -0.0551 -0.0514 837  PHE B CB  
14817 C CG  . PHE B 839  ? 0.3162 0.2997 0.3666 0.0281  -0.0583 -0.0498 837  PHE B CG  
14818 C CD1 . PHE B 839  ? 0.3686 0.3601 0.4295 0.0306  -0.0585 -0.0512 837  PHE B CD1 
14819 C CD2 . PHE B 839  ? 0.3831 0.3609 0.4255 0.0250  -0.0612 -0.0470 837  PHE B CD2 
14820 C CE1 . PHE B 839  ? 0.3537 0.3467 0.4169 0.0299  -0.0620 -0.0498 837  PHE B CE1 
14821 C CE2 . PHE B 839  ? 0.3556 0.3345 0.3992 0.0247  -0.0645 -0.0458 837  PHE B CE2 
14822 C CZ  . PHE B 839  ? 0.3699 0.3562 0.4240 0.0270  -0.0652 -0.0473 837  PHE B CZ  
14823 N N   . ASP B 840  ? 0.3004 0.2865 0.3416 0.0244  -0.0437 -0.0536 838  ASP B N   
14824 C CA  . ASP B 840  ? 0.3379 0.3222 0.3761 0.0244  -0.0414 -0.0553 838  ASP B CA  
14825 C C   . ASP B 840  ? 0.3424 0.3344 0.3878 0.0280  -0.0377 -0.0587 838  ASP B C   
14826 O O   . ASP B 840  ? 0.3335 0.3342 0.3845 0.0281  -0.0349 -0.0586 838  ASP B O   
14827 C CB  . ASP B 840  ? 0.3336 0.3187 0.3656 0.0197  -0.0384 -0.0534 838  ASP B CB  
14828 C CG  . ASP B 840  ? 0.4058 0.3892 0.4345 0.0191  -0.0364 -0.0550 838  ASP B CG  
14829 O OD1 . ASP B 840  ? 0.4145 0.4039 0.4468 0.0210  -0.0329 -0.0575 838  ASP B OD1 
14830 O OD2 . ASP B 840  ? 0.4387 0.4150 0.4611 0.0165  -0.0386 -0.0536 838  ASP B OD2 
14831 N N   . SER B 841  ? 0.3325 0.3208 0.3772 0.0309  -0.0380 -0.0615 839  SER B N   
14832 C CA  . SER B 841  ? 0.3465 0.3418 0.3970 0.0350  -0.0344 -0.0650 839  SER B CA  
14833 C C   . SER B 841  ? 0.3087 0.3109 0.3690 0.0387  -0.0349 -0.0655 839  SER B C   
14834 O O   . SER B 841  ? 0.2811 0.2931 0.3479 0.0405  -0.0309 -0.0668 839  SER B O   
14835 C CB  . SER B 841  ? 0.3576 0.3604 0.4073 0.0326  -0.0289 -0.0650 839  SER B CB  
14836 O OG  . SER B 841  ? 0.3422 0.3393 0.3836 0.0292  -0.0288 -0.0644 839  SER B OG  
14837 N N   . ALA B 842  ? 0.3220 0.3193 0.3834 0.0394  -0.0400 -0.0640 840  ALA B N   
14838 C CA  . ALA B 842  ? 0.3083 0.3116 0.3792 0.0425  -0.0417 -0.0640 840  ALA B CA  
14839 C C   . ALA B 842  ? 0.3049 0.3189 0.3813 0.0400  -0.0383 -0.0625 840  ALA B C   
14840 O O   . ALA B 842  ? 0.2800 0.3030 0.3659 0.0426  -0.0369 -0.0633 840  ALA B O   
14841 C CB  . ALA B 842  ? 0.3447 0.3506 0.4221 0.0490  -0.0413 -0.0677 840  ALA B CB  
14842 N N   . GLY B 843  ? 0.2916 0.3044 0.3620 0.0350  -0.0369 -0.0602 841  GLY B N   
14843 C CA  . GLY B 843  ? 0.2871 0.3080 0.3614 0.0324  -0.0342 -0.0587 841  GLY B CA  
14844 C C   . GLY B 843  ? 0.3129 0.3435 0.3925 0.0333  -0.0286 -0.0600 841  GLY B C   
14845 O O   . GLY B 843  ? 0.3184 0.3568 0.4040 0.0320  -0.0269 -0.0588 841  GLY B O   
14846 N N   . GLN B 844  ? 0.2896 0.3197 0.3669 0.0356  -0.0259 -0.0625 842  GLN B N   
14847 C CA  . GLN B 844  ? 0.2950 0.3343 0.3763 0.0368  -0.0204 -0.0638 842  GLN B CA  
14848 C C   . GLN B 844  ? 0.2744 0.3136 0.3488 0.0330  -0.0168 -0.0628 842  GLN B C   
14849 O O   . GLN B 844  ? 0.3488 0.3908 0.4214 0.0340  -0.0130 -0.0645 842  GLN B O   
14850 C CB  . GLN B 844  ? 0.2346 0.2740 0.3173 0.0421  -0.0194 -0.0675 842  GLN B CB  
14851 C CG  . GLN B 844  ? 0.3044 0.3445 0.3948 0.0467  -0.0230 -0.0686 842  GLN B CG  
14852 C CD  . GLN B 844  ? 0.2726 0.3122 0.3640 0.0528  -0.0221 -0.0727 842  GLN B CD  
14853 O OE1 . GLN B 844  ? 0.2767 0.3247 0.3773 0.0572  -0.0208 -0.0740 842  GLN B OE1 
14854 N NE2 . GLN B 844  ? 0.3192 0.3490 0.4013 0.0533  -0.0229 -0.0747 842  GLN B NE2 
14855 N N   . ARG B 845  ? 0.2881 0.3241 0.3583 0.0287  -0.0181 -0.0601 843  ARG B N   
14856 C CA  . ARG B 845  ? 0.2823 0.3197 0.3477 0.0252  -0.0148 -0.0587 843  ARG B CA  
14857 C C   . ARG B 845  ? 0.2967 0.3412 0.3677 0.0233  -0.0132 -0.0565 843  ARG B C   
14858 O O   . ARG B 845  ? 0.2979 0.3422 0.3727 0.0228  -0.0161 -0.0553 843  ARG B O   
14859 C CB  . ARG B 845  ? 0.3025 0.3319 0.3594 0.0221  -0.0171 -0.0571 843  ARG B CB  
14860 C CG  . ARG B 845  ? 0.3095 0.3311 0.3606 0.0230  -0.0193 -0.0585 843  ARG B CG  
14861 C CD  . ARG B 845  ? 0.3212 0.3365 0.3649 0.0193  -0.0214 -0.0562 843  ARG B CD  
14862 N NE  . ARG B 845  ? 0.3753 0.3827 0.4133 0.0192  -0.0238 -0.0569 843  ARG B NE  
14863 C CZ  . ARG B 845  ? 0.3920 0.3978 0.4247 0.0172  -0.0224 -0.0570 843  ARG B CZ  
14864 N NH1 . ARG B 845  ? 0.3737 0.3854 0.4059 0.0156  -0.0185 -0.0565 843  ARG B NH1 
14865 N NH2 . ARG B 845  ? 0.4039 0.4017 0.4316 0.0167  -0.0253 -0.0576 843  ARG B NH2 
14866 N N   . CYS B 846  ? 0.3017 0.3519 0.3730 0.0221  -0.0088 -0.0560 844  CYS B N   
14867 C CA  . CYS B 846  ? 0.2820 0.3373 0.3573 0.0196  -0.0075 -0.0535 844  CYS B CA  
14868 C C   . CYS B 846  ? 0.2755 0.3248 0.3460 0.0167  -0.0103 -0.0516 844  CYS B C   
14869 O O   . CYS B 846  ? 0.2727 0.3236 0.3468 0.0151  -0.0115 -0.0500 844  CYS B O   
14870 C CB  . CYS B 846  ? 0.3909 0.4518 0.4654 0.0185  -0.0026 -0.0528 844  CYS B CB  
14871 S SG  . CYS B 846  ? 0.6323 0.7015 0.7118 0.0222  0.0015  -0.0550 844  CYS B SG  
14872 N N   . SER B 847  ? 0.2776 0.3202 0.3401 0.0160  -0.0115 -0.0518 845  SER B N   
14873 C CA  . SER B 847  ? 0.2858 0.3230 0.3428 0.0137  -0.0137 -0.0501 845  SER B CA  
14874 C C   . SER B 847  ? 0.2814 0.3135 0.3382 0.0143  -0.0185 -0.0501 845  SER B C   
14875 O O   . SER B 847  ? 0.2505 0.2783 0.3023 0.0127  -0.0204 -0.0488 845  SER B O   
14876 C CB  . SER B 847  ? 0.2711 0.3047 0.3201 0.0125  -0.0127 -0.0498 845  SER B CB  
14877 O OG  . SER B 847  ? 0.3102 0.3404 0.3574 0.0140  -0.0139 -0.0515 845  SER B OG  
14878 N N   . ALA B 848  ? 0.2612 0.2937 0.3230 0.0168  -0.0205 -0.0515 846  ALA B N   
14879 C CA  . ALA B 848  ? 0.2449 0.2716 0.3053 0.0176  -0.0254 -0.0515 846  ALA B CA  
14880 C C   . ALA B 848  ? 0.2656 0.2915 0.3267 0.0160  -0.0281 -0.0500 846  ALA B C   
14881 O O   . ALA B 848  ? 0.2390 0.2701 0.3055 0.0152  -0.0270 -0.0495 846  ALA B O   
14882 C CB  . ALA B 848  ? 0.2555 0.2836 0.3224 0.0212  -0.0271 -0.0533 846  ALA B CB  
14883 N N   . LEU B 849  ? 0.2484 0.2675 0.3036 0.0154  -0.0318 -0.0492 847  LEU B N   
14884 C CA  . LEU B 849  ? 0.2381 0.2551 0.2925 0.0143  -0.0352 -0.0482 847  LEU B CA  
14885 C C   . LEU B 849  ? 0.2568 0.2770 0.3203 0.0159  -0.0386 -0.0488 847  LEU B C   
14886 O O   . LEU B 849  ? 0.2890 0.3080 0.3550 0.0182  -0.0410 -0.0495 847  LEU B O   
14887 C CB  . LEU B 849  ? 0.2816 0.2907 0.3268 0.0135  -0.0383 -0.0471 847  LEU B CB  
14888 C CG  . LEU B 849  ? 0.2815 0.2871 0.3239 0.0127  -0.0425 -0.0464 847  LEU B CG  
14889 C CD1 . LEU B 849  ? 0.2638 0.2715 0.3056 0.0111  -0.0406 -0.0463 847  LEU B CD1 
14890 C CD2 . LEU B 849  ? 0.2865 0.2848 0.3185 0.0120  -0.0445 -0.0450 847  LEU B CD2 
14891 N N   . ARG B 850  ? 0.2528 0.2770 0.3214 0.0146  -0.0389 -0.0484 848  ARG B N   
14892 C CA  . ARG B 850  ? 0.2498 0.2783 0.3280 0.0155  -0.0421 -0.0485 848  ARG B CA  
14893 C C   . ARG B 850  ? 0.2219 0.2459 0.2979 0.0142  -0.0477 -0.0478 848  ARG B C   
14894 O O   . ARG B 850  ? 0.3074 0.3323 0.3889 0.0154  -0.0521 -0.0479 848  ARG B O   
14895 C CB  . ARG B 850  ? 0.2565 0.2940 0.3439 0.0146  -0.0387 -0.0483 848  ARG B CB  
14896 C CG  . ARG B 850  ? 0.2874 0.3300 0.3766 0.0160  -0.0330 -0.0490 848  ARG B CG  
14897 C CD  . ARG B 850  ? 0.2579 0.3003 0.3487 0.0197  -0.0335 -0.0506 848  ARG B CD  
14898 N NE  . ARG B 850  ? 0.3019 0.3496 0.3948 0.0213  -0.0283 -0.0517 848  ARG B NE  
14899 C CZ  . ARG B 850  ? 0.3042 0.3513 0.3972 0.0247  -0.0277 -0.0536 848  ARG B CZ  
14900 N NH1 . ARG B 850  ? 0.2778 0.3192 0.3695 0.0268  -0.0321 -0.0543 848  ARG B NH1 
14901 N NH2 . ARG B 850  ? 0.2612 0.3130 0.3550 0.0260  -0.0228 -0.0549 848  ARG B NH2 
14902 N N   . VAL B 851  ? 0.2706 0.2897 0.3384 0.0120  -0.0476 -0.0473 849  VAL B N   
14903 C CA  . VAL B 851  ? 0.2948 0.3090 0.3590 0.0107  -0.0528 -0.0471 849  VAL B CA  
14904 C C   . VAL B 851  ? 0.3043 0.3106 0.3553 0.0102  -0.0528 -0.0468 849  VAL B C   
14905 O O   . VAL B 851  ? 0.3147 0.3204 0.3605 0.0093  -0.0488 -0.0467 849  VAL B O   
14906 C CB  . VAL B 851  ? 0.3123 0.3291 0.3809 0.0084  -0.0531 -0.0469 849  VAL B CB  
14907 C CG1 . VAL B 851  ? 0.3246 0.3356 0.3894 0.0073  -0.0594 -0.0471 849  VAL B CG1 
14908 C CG2 . VAL B 851  ? 0.3202 0.3463 0.4023 0.0084  -0.0519 -0.0466 849  VAL B CG2 
14909 N N   . LEU B 852  ? 0.3102 0.3109 0.3558 0.0109  -0.0573 -0.0465 850  LEU B N   
14910 C CA  . LEU B 852  ? 0.3227 0.3164 0.3555 0.0104  -0.0575 -0.0459 850  LEU B CA  
14911 C C   . LEU B 852  ? 0.3212 0.3107 0.3494 0.0095  -0.0617 -0.0463 850  LEU B C   
14912 O O   . LEU B 852  ? 0.3079 0.2968 0.3401 0.0096  -0.0671 -0.0465 850  LEU B O   
14913 C CB  . LEU B 852  ? 0.2789 0.2686 0.3075 0.0116  -0.0598 -0.0448 850  LEU B CB  
14914 C CG  . LEU B 852  ? 0.2954 0.2783 0.3108 0.0109  -0.0605 -0.0435 850  LEU B CG  
14915 C CD1 . LEU B 852  ? 0.3055 0.2893 0.3150 0.0099  -0.0545 -0.0432 850  LEU B CD1 
14916 C CD2 . LEU B 852  ? 0.3103 0.2889 0.3229 0.0117  -0.0636 -0.0420 850  LEU B CD2 
14917 N N   . CYS B 853  ? 0.2923 0.2789 0.3122 0.0087  -0.0595 -0.0467 851  CYS B N   
14918 C CA  . CYS B 853  ? 0.3048 0.2865 0.3190 0.0080  -0.0630 -0.0477 851  CYS B CA  
14919 C C   . CYS B 853  ? 0.3077 0.2831 0.3081 0.0086  -0.0635 -0.0473 851  CYS B C   
14920 O O   . CYS B 853  ? 0.3103 0.2856 0.3044 0.0089  -0.0587 -0.0469 851  CYS B O   
14921 C CB  . CYS B 853  ? 0.2755 0.2585 0.2912 0.0071  -0.0602 -0.0487 851  CYS B CB  
14922 S SG  . CYS B 853  ? 0.3579 0.3493 0.3894 0.0060  -0.0585 -0.0485 851  CYS B SG  
14923 N N   . LEU B 854  ? 0.3047 0.2751 0.3003 0.0088  -0.0693 -0.0472 852  LEU B N   
14924 C CA  . LEU B 854  ? 0.3138 0.2786 0.2962 0.0093  -0.0702 -0.0463 852  LEU B CA  
14925 C C   . LEU B 854  ? 0.3073 0.2661 0.2807 0.0094  -0.0737 -0.0481 852  LEU B C   
14926 O O   . LEU B 854  ? 0.3418 0.2988 0.3188 0.0089  -0.0794 -0.0492 852  LEU B O   
14927 C CB  . LEU B 854  ? 0.3227 0.2856 0.3053 0.0097  -0.0744 -0.0445 852  LEU B CB  
14928 C CG  . LEU B 854  ? 0.3402 0.3071 0.3302 0.0100  -0.0717 -0.0430 852  LEU B CG  
14929 C CD1 . LEU B 854  ? 0.3243 0.2881 0.3145 0.0107  -0.0771 -0.0414 852  LEU B CD1 
14930 C CD2 . LEU B 854  ? 0.3321 0.2997 0.3157 0.0095  -0.0657 -0.0417 852  LEU B CD2 
14931 N N   . GLN B 855  ? 0.3735 0.3295 0.3353 0.0102  -0.0705 -0.0484 853  GLN B N   
14932 C CA  . GLN B 855  ? 0.3820 0.3314 0.3330 0.0109  -0.0738 -0.0503 853  GLN B CA  
14933 C C   . GLN B 855  ? 0.3923 0.3369 0.3385 0.0107  -0.0807 -0.0496 853  GLN B C   
14934 O O   . GLN B 855  ? 0.3736 0.3183 0.3175 0.0106  -0.0810 -0.0470 853  GLN B O   
14935 C CB  . GLN B 855  ? 0.3306 0.2786 0.2692 0.0124  -0.0687 -0.0505 853  GLN B CB  
14936 C CG  . GLN B 855  ? 0.3825 0.3238 0.3106 0.0138  -0.0714 -0.0536 853  GLN B CG  
14937 C CD  . GLN B 855  ? 0.4492 0.3895 0.3646 0.0160  -0.0663 -0.0539 853  GLN B CD  
14938 O OE1 . GLN B 855  ? 0.4174 0.3631 0.3352 0.0166  -0.0599 -0.0529 853  GLN B OE1 
14939 N NE2 . GLN B 855  ? 0.4343 0.3682 0.3363 0.0175  -0.0692 -0.0554 853  GLN B NE2 
14940 N N   . GLU B 856  ? 0.3888 0.3288 0.3336 0.0104  -0.0867 -0.0518 854  GLU B N   
14941 C CA  . GLU B 856  ? 0.4107 0.3466 0.3530 0.0100  -0.0944 -0.0513 854  GLU B CA  
14942 C C   . GLU B 856  ? 0.4259 0.3579 0.3547 0.0109  -0.0946 -0.0492 854  GLU B C   
14943 O O   . GLU B 856  ? 0.4135 0.3446 0.3434 0.0106  -0.0987 -0.0470 854  GLU B O   
14944 C CB  . GLU B 856  ? 0.4612 0.3913 0.4001 0.0095  -0.1004 -0.0544 854  GLU B CB  
14945 C CG  . GLU B 856  ? 0.5110 0.4358 0.4446 0.0092  -0.1089 -0.0541 854  GLU B CG  
14946 C CD  . GLU B 856  ? 0.6041 0.5336 0.5518 0.0082  -0.1136 -0.0521 854  GLU B CD  
14947 O OE1 . GLU B 856  ? 0.5831 0.5194 0.5457 0.0073  -0.1116 -0.0520 854  GLU B OE1 
14948 O OE2 . GLU B 856  ? 0.6085 0.5350 0.5522 0.0084  -0.1192 -0.0506 854  GLU B OE2 
14949 N N   . ASP B 857  ? 0.4234 0.3532 0.3396 0.0121  -0.0900 -0.0497 855  ASP B N   
14950 C CA  . ASP B 857  ? 0.4162 0.3422 0.3181 0.0127  -0.0903 -0.0476 855  ASP B CA  
14951 C C   . ASP B 857  ? 0.4869 0.4166 0.3916 0.0119  -0.0875 -0.0434 855  ASP B C   
14952 O O   . ASP B 857  ? 0.5056 0.4318 0.4010 0.0117  -0.0897 -0.0408 855  ASP B O   
14953 C CB  . ASP B 857  ? 0.4764 0.4007 0.3650 0.0145  -0.0854 -0.0492 855  ASP B CB  
14954 N N   . VAL B 858  ? 0.3935 0.3295 0.3098 0.0113  -0.0827 -0.0426 856  VAL B N   
14955 C CA  . VAL B 858  ? 0.4042 0.3427 0.3232 0.0103  -0.0805 -0.0389 856  VAL B CA  
14956 C C   . VAL B 858  ? 0.3581 0.2990 0.2915 0.0099  -0.0835 -0.0384 856  VAL B C   
14957 O O   . VAL B 858  ? 0.3764 0.3186 0.3130 0.0094  -0.0822 -0.0357 856  VAL B O   
14958 C CB  . VAL B 858  ? 0.3933 0.3369 0.3119 0.0101  -0.0722 -0.0378 856  VAL B CB  
14959 C CG1 . VAL B 858  ? 0.3992 0.3412 0.3031 0.0109  -0.0691 -0.0377 856  VAL B CG1 
14960 C CG2 . VAL B 858  ? 0.3867 0.3354 0.3161 0.0104  -0.0687 -0.0404 856  VAL B CG2 
14961 N N   . ALA B 859  ? 0.3727 0.3143 0.3148 0.0102  -0.0876 -0.0408 857  ALA B N   
14962 C CA  . ALA B 859  ? 0.3641 0.3100 0.3212 0.0102  -0.0891 -0.0407 857  ALA B CA  
14963 C C   . ALA B 859  ? 0.3469 0.2901 0.3044 0.0106  -0.0938 -0.0380 857  ALA B C   
14964 O O   . ALA B 859  ? 0.3276 0.2735 0.2928 0.0110  -0.0921 -0.0367 857  ALA B O   
14965 C CB  . ALA B 859  ? 0.3622 0.3098 0.3282 0.0101  -0.0930 -0.0433 857  ALA B CB  
14966 N N   . ASP B 860  ? 0.4032 0.3404 0.3520 0.0107  -0.0999 -0.0371 858  ASP B N   
14967 C CA  . ASP B 860  ? 0.4111 0.3453 0.3609 0.0113  -0.1052 -0.0344 858  ASP B CA  
14968 C C   . ASP B 860  ? 0.3629 0.2955 0.3076 0.0108  -0.1015 -0.0311 858  ASP B C   
14969 O O   . ASP B 860  ? 0.3934 0.3258 0.3447 0.0114  -0.1032 -0.0294 858  ASP B O   
14970 C CB  . ASP B 860  ? 0.4113 0.3390 0.3512 0.0114  -0.1127 -0.0337 858  ASP B CB  
14971 C CG  . ASP B 860  ? 0.4784 0.4072 0.4248 0.0116  -0.1180 -0.0366 858  ASP B CG  
14972 O OD1 . ASP B 860  ? 0.4815 0.4164 0.4432 0.0120  -0.1181 -0.0379 858  ASP B OD1 
14973 O OD2 . ASP B 860  ? 0.5330 0.4568 0.4691 0.0112  -0.1221 -0.0375 858  ASP B OD2 
14974 N N   . ARG B 861  ? 0.3872 0.3184 0.3201 0.0096  -0.0968 -0.0300 859  ARG B N   
14975 C CA  . ARG B 861  ? 0.4003 0.3301 0.3282 0.0084  -0.0938 -0.0263 859  ARG B CA  
14976 C C   . ARG B 861  ? 0.4086 0.3434 0.3474 0.0082  -0.0888 -0.0266 859  ARG B C   
14977 O O   . ARG B 861  ? 0.3802 0.3132 0.3217 0.0079  -0.0895 -0.0243 859  ARG B O   
14978 C CB  . ARG B 861  ? 0.4953 0.4241 0.4089 0.0071  -0.0895 -0.0249 859  ARG B CB  
14979 C CG  . ARG B 861  ? 0.5426 0.4717 0.4527 0.0052  -0.0852 -0.0209 859  ARG B CG  
14980 C CD  . ARG B 861  ? 0.6304 0.5579 0.5252 0.0038  -0.0829 -0.0181 859  ARG B CD  
14981 N NE  . ARG B 861  ? 0.6595 0.5882 0.5526 0.0013  -0.0788 -0.0139 859  ARG B NE  
14982 C CZ  . ARG B 861  ? 0.5942 0.5291 0.4897 0.0003  -0.0718 -0.0140 859  ARG B CZ  
14983 N NH1 . ARG B 861  ? 0.5672 0.5073 0.4662 0.0019  -0.0678 -0.0179 859  ARG B NH1 
14984 N NH2 . ARG B 861  ? 0.6418 0.5774 0.5363 -0.0024 -0.0692 -0.0099 859  ARG B NH2 
14985 N N   . ILE B 862  ? 0.3717 0.3124 0.3166 0.0084  -0.0839 -0.0296 860  ILE B N   
14986 C CA  . ILE B 862  ? 0.3159 0.2616 0.2709 0.0084  -0.0794 -0.0302 860  ILE B CA  
14987 C C   . ILE B 862  ? 0.3069 0.2532 0.2739 0.0100  -0.0833 -0.0311 860  ILE B C   
14988 O O   . ILE B 862  ? 0.3334 0.2800 0.3053 0.0102  -0.0820 -0.0302 860  ILE B O   
14989 C CB  . ILE B 862  ? 0.3308 0.2825 0.2894 0.0084  -0.0739 -0.0331 860  ILE B CB  
14990 C CG1 . ILE B 862  ? 0.3726 0.3242 0.3197 0.0073  -0.0693 -0.0320 860  ILE B CG1 
14991 C CG2 . ILE B 862  ? 0.3656 0.3228 0.3357 0.0087  -0.0700 -0.0342 860  ILE B CG2 
14992 C CD1 . ILE B 862  ? 0.3724 0.3287 0.3212 0.0078  -0.0644 -0.0347 860  ILE B CD1 
14993 N N   . LEU B 863  ? 0.3308 0.2773 0.3026 0.0114  -0.0883 -0.0328 861  LEU B N   
14994 C CA  . LEU B 863  ? 0.3485 0.2966 0.3322 0.0134  -0.0921 -0.0334 861  LEU B CA  
14995 C C   . LEU B 863  ? 0.3767 0.3186 0.3572 0.0141  -0.0961 -0.0305 861  LEU B C   
14996 O O   . LEU B 863  ? 0.3564 0.2990 0.3449 0.0157  -0.0962 -0.0306 861  LEU B O   
14997 C CB  . LEU B 863  ? 0.3729 0.3225 0.3620 0.0143  -0.0974 -0.0351 861  LEU B CB  
14998 C CG  . LEU B 863  ? 0.4426 0.3995 0.4411 0.0141  -0.0942 -0.0381 861  LEU B CG  
14999 C CD1 . LEU B 863  ? 0.4807 0.4382 0.4825 0.0140  -0.1000 -0.0394 861  LEU B CD1 
15000 C CD2 . LEU B 863  ? 0.4236 0.3869 0.4352 0.0156  -0.0912 -0.0390 861  LEU B CD2 
15001 N N   . THR B 864  ? 0.3706 0.3059 0.3391 0.0130  -0.0997 -0.0278 862  THR B N   
15002 C CA  . THR B 864  ? 0.3857 0.3142 0.3502 0.0133  -0.1036 -0.0244 862  THR B CA  
15003 C C   . THR B 864  ? 0.3983 0.3261 0.3625 0.0121  -0.0988 -0.0230 862  THR B C   
15004 O O   . THR B 864  ? 0.3946 0.3194 0.3637 0.0134  -0.1010 -0.0222 862  THR B O   
15005 C CB  . THR B 864  ? 0.4740 0.3959 0.4241 0.0118  -0.1074 -0.0214 862  THR B CB  
15006 O OG1 . THR B 864  ? 0.4257 0.3474 0.3768 0.0131  -0.1132 -0.0229 862  THR B OG1 
15007 C CG2 . THR B 864  ? 0.5167 0.4309 0.4618 0.0115  -0.1113 -0.0172 862  THR B CG2 
15008 N N   . MET B 865  ? 0.3494 0.2798 0.3080 0.0097  -0.0925 -0.0228 863  MET B N   
15009 C CA  . MET B 865  ? 0.4135 0.3437 0.3715 0.0079  -0.0880 -0.0212 863  MET B CA  
15010 C C   . MET B 865  ? 0.3661 0.3007 0.3369 0.0098  -0.0858 -0.0243 863  MET B C   
15011 O O   . MET B 865  ? 0.3311 0.2625 0.3040 0.0099  -0.0861 -0.0234 863  MET B O   
15012 C CB  . MET B 865  ? 0.3482 0.2820 0.2988 0.0052  -0.0817 -0.0205 863  MET B CB  
15013 C CG  . MET B 865  ? 0.3937 0.3269 0.3414 0.0025  -0.0778 -0.0178 863  MET B CG  
15014 S SD  . MET B 865  ? 0.4701 0.4089 0.4092 -0.0001 -0.0708 -0.0166 863  MET B SD  
15015 C CE  . MET B 865  ? 0.4228 0.3585 0.3515 0.0008  -0.0745 -0.0162 863  MET B CE  
15016 N N   . LEU B 866  ? 0.3589 0.3003 0.3376 0.0113  -0.0839 -0.0279 864  LEU B N   
15017 C CA  . LEU B 866  ? 0.3535 0.3001 0.3441 0.0133  -0.0814 -0.0308 864  LEU B CA  
15018 C C   . LEU B 866  ? 0.3652 0.3085 0.3625 0.0164  -0.0865 -0.0310 864  LEU B C   
15019 O O   . LEU B 866  ? 0.3733 0.3161 0.3751 0.0176  -0.0852 -0.0319 864  LEU B O   
15020 C CB  . LEU B 866  ? 0.3566 0.3108 0.3541 0.0141  -0.0793 -0.0339 864  LEU B CB  
15021 C CG  . LEU B 866  ? 0.3564 0.3173 0.3661 0.0160  -0.0763 -0.0367 864  LEU B CG  
15022 C CD1 . LEU B 866  ? 0.3779 0.3395 0.3859 0.0147  -0.0709 -0.0366 864  LEU B CD1 
15023 C CD2 . LEU B 866  ? 0.3981 0.3661 0.4134 0.0158  -0.0743 -0.0389 864  LEU B CD2 
15024 N N   . LYS B 867  ? 0.3485 0.2892 0.3459 0.0178  -0.0927 -0.0304 865  LYS B N   
15025 C CA  . LYS B 867  ? 0.3637 0.3017 0.3680 0.0213  -0.0980 -0.0305 865  LYS B CA  
15026 C C   . LYS B 867  ? 0.4431 0.3718 0.4408 0.0209  -0.1002 -0.0277 865  LYS B C   
15027 O O   . LYS B 867  ? 0.3962 0.3227 0.3999 0.0237  -0.1016 -0.0286 865  LYS B O   
15028 C CB  . LYS B 867  ? 0.3853 0.3230 0.3911 0.0227  -0.1045 -0.0302 865  LYS B CB  
15029 C CG  . LYS B 867  ? 0.4026 0.3498 0.4186 0.0237  -0.1033 -0.0333 865  LYS B CG  
15030 C CD  . LYS B 867  ? 0.4620 0.4085 0.4761 0.0233  -0.1092 -0.0327 865  LYS B CD  
15031 C CE  . LYS B 867  ? 0.4984 0.4543 0.5239 0.0238  -0.1086 -0.0355 865  LYS B CE  
15032 N NZ  . LYS B 867  ? 0.5553 0.5103 0.5792 0.0231  -0.1149 -0.0351 865  LYS B NZ  
15033 N N   . GLY B 868  ? 0.4002 0.3231 0.3854 0.0174  -0.1005 -0.0240 866  GLY B N   
15034 C CA  . GLY B 868  ? 0.3834 0.2973 0.3621 0.0161  -0.1024 -0.0207 866  GLY B CA  
15035 C C   . GLY B 868  ? 0.3964 0.3110 0.3780 0.0153  -0.0975 -0.0219 866  GLY B C   
15036 O O   . GLY B 868  ? 0.4217 0.3299 0.4047 0.0165  -0.1000 -0.0215 866  GLY B O   
15037 N N   . ALA B 869  ? 0.4052 0.3271 0.3873 0.0133  -0.0909 -0.0236 867  ALA B N   
15038 C CA  . ALA B 869  ? 0.4316 0.3550 0.4166 0.0125  -0.0863 -0.0250 867  ALA B CA  
15039 C C   . ALA B 869  ? 0.3837 0.3095 0.3801 0.0170  -0.0866 -0.0291 867  ALA B C   
15040 O O   . ALA B 869  ? 0.4009 0.3232 0.3987 0.0176  -0.0860 -0.0300 867  ALA B O   
15041 C CB  . ALA B 869  ? 0.3844 0.3158 0.3682 0.0099  -0.0795 -0.0258 867  ALA B CB  
15042 N N   . LEU B 870  ? 0.3686 0.3007 0.3730 0.0202  -0.0873 -0.0317 868  LEU B N   
15043 C CA  . LEU B 870  ? 0.4142 0.3503 0.4299 0.0247  -0.0869 -0.0355 868  LEU B CA  
15044 C C   . LEU B 870  ? 0.4220 0.3497 0.4388 0.0280  -0.0923 -0.0353 868  LEU B C   
15045 O O   . LEU B 870  ? 0.4131 0.3404 0.4350 0.0309  -0.0910 -0.0380 868  LEU B O   
15046 C CB  . LEU B 870  ? 0.4174 0.3620 0.4418 0.0271  -0.0876 -0.0375 868  LEU B CB  
15047 C CG  . LEU B 870  ? 0.5002 0.4533 0.5362 0.0304  -0.0839 -0.0414 868  LEU B CG  
15048 C CD1 . LEU B 870  ? 0.4609 0.4190 0.4952 0.0275  -0.0768 -0.0424 868  LEU B CD1 
15049 C CD2 . LEU B 870  ? 0.5524 0.5135 0.5984 0.0328  -0.0857 -0.0427 868  LEU B CD2 
15050 N N   . HIS B 871  ? 0.3833 0.3036 0.3950 0.0279  -0.0984 -0.0321 869  HIS B N   
15051 C CA  . HIS B 871  ? 0.4122 0.3240 0.4255 0.0315  -0.1041 -0.0318 869  HIS B CA  
15052 C C   . HIS B 871  ? 0.4310 0.3331 0.4376 0.0296  -0.1040 -0.0305 869  HIS B C   
15053 O O   . HIS B 871  ? 0.4146 0.3084 0.4223 0.0328  -0.1086 -0.0307 869  HIS B O   
15054 C CB  . HIS B 871  ? 0.5050 0.4115 0.5146 0.0319  -0.1112 -0.0285 869  HIS B CB  
15055 C CG  . HIS B 871  ? 0.5379 0.4530 0.5563 0.0349  -0.1130 -0.0303 869  HIS B CG  
15056 N ND1 . HIS B 871  ? 0.6200 0.5397 0.6508 0.0406  -0.1146 -0.0335 869  HIS B ND1 
15057 C CD2 . HIS B 871  ? 0.5330 0.4528 0.5497 0.0329  -0.1135 -0.0294 869  HIS B CD2 
15058 C CE1 . HIS B 871  ? 0.5872 0.5147 0.6241 0.0415  -0.1162 -0.0340 869  HIS B CE1 
15059 N NE2 . HIS B 871  ? 0.5886 0.5158 0.6170 0.0368  -0.1158 -0.0317 869  HIS B NE2 
15060 N N   . GLU B 872  ? 0.3738 0.2769 0.3741 0.0245  -0.0992 -0.0293 870  GLU B N   
15061 C CA  . GLU B 872  ? 0.3998 0.2947 0.3945 0.0220  -0.0989 -0.0281 870  GLU B CA  
15062 C C   . GLU B 872  ? 0.4032 0.3018 0.4039 0.0239  -0.0945 -0.0327 870  GLU B C   
15063 O O   . GLU B 872  ? 0.4288 0.3207 0.4254 0.0219  -0.0945 -0.0323 870  GLU B O   
15064 C CB  . GLU B 872  ? 0.4148 0.3092 0.3996 0.0152  -0.0964 -0.0237 870  GLU B CB  
15065 C CG  . GLU B 872  ? 0.3641 0.2538 0.3408 0.0128  -0.1005 -0.0187 870  GLU B CG  
15066 C CD  . GLU B 872  ? 0.4467 0.3236 0.4199 0.0139  -0.1079 -0.0158 870  GLU B CD  
15067 O OE1 . GLU B 872  ? 0.4962 0.3659 0.4702 0.0144  -0.1092 -0.0166 870  GLU B OE1 
15068 O OE2 . GLU B 872  ? 0.4772 0.3505 0.4465 0.0142  -0.1126 -0.0129 870  GLU B OE2 
15069 N N   . LEU B 873  ? 0.3704 0.2795 0.3802 0.0275  -0.0910 -0.0368 871  LEU B N   
15070 C CA  . LEU B 873  ? 0.3830 0.2965 0.3980 0.0295  -0.0864 -0.0412 871  LEU B CA  
15071 C C   . LEU B 873  ? 0.4068 0.3141 0.4261 0.0353  -0.0899 -0.0443 871  LEU B C   
15072 O O   . LEU B 873  ? 0.4034 0.3083 0.4266 0.0395  -0.0947 -0.0443 871  LEU B O   
15073 C CB  . LEU B 873  ? 0.3663 0.2935 0.3892 0.0311  -0.0813 -0.0440 871  LEU B CB  
15074 C CG  . LEU B 873  ? 0.4597 0.3943 0.4798 0.0264  -0.0769 -0.0422 871  LEU B CG  
15075 C CD1 . LEU B 873  ? 0.3803 0.3272 0.4094 0.0285  -0.0724 -0.0453 871  LEU B CD1 
15076 C CD2 . LEU B 873  ? 0.4315 0.3639 0.4440 0.0214  -0.0736 -0.0406 871  LEU B CD2 
15077 N N   . HIS B 874  ? 0.3891 0.2940 0.4078 0.0359  -0.0875 -0.0472 872  HIS B N   
15078 C CA  . HIS B 874  ? 0.4356 0.3344 0.4578 0.0419  -0.0901 -0.0510 872  HIS B CA  
15079 C C   . HIS B 874  ? 0.4276 0.3377 0.4582 0.0463  -0.0845 -0.0562 872  HIS B C   
15080 O O   . HIS B 874  ? 0.3854 0.3008 0.4145 0.0435  -0.0791 -0.0575 872  HIS B O   
15081 C CB  . HIS B 874  ? 0.3999 0.2856 0.4137 0.0393  -0.0924 -0.0505 872  HIS B CB  
15082 C CG  . HIS B 874  ? 0.4187 0.2962 0.4345 0.0456  -0.0953 -0.0549 872  HIS B CG  
15083 N ND1 . HIS B 874  ? 0.5067 0.3880 0.5313 0.0535  -0.0963 -0.0585 872  HIS B ND1 
15084 C CD2 . HIS B 874  ? 0.4552 0.3209 0.4654 0.0453  -0.0976 -0.0564 872  HIS B CD2 
15085 C CE1 . HIS B 874  ? 0.4620 0.3342 0.4859 0.0583  -0.0987 -0.0623 872  HIS B CE1 
15086 N NE2 . HIS B 874  ? 0.5172 0.3793 0.5322 0.0534  -0.0997 -0.0612 872  HIS B NE2 
15087 N N   . ILE B 875  ? 0.3994 0.3140 0.4390 0.0529  -0.0857 -0.0589 873  ILE B N   
15088 C CA  . ILE B 875  ? 0.4117 0.3381 0.4601 0.0575  -0.0804 -0.0635 873  ILE B CA  
15089 C C   . ILE B 875  ? 0.4346 0.3549 0.4849 0.0644  -0.0820 -0.0681 873  ILE B C   
15090 O O   . ILE B 875  ? 0.3580 0.2703 0.4093 0.0686  -0.0879 -0.0680 873  ILE B O   
15091 C CB  . ILE B 875  ? 0.4249 0.3635 0.4835 0.0598  -0.0799 -0.0630 873  ILE B CB  
15092 C CG1 . ILE B 875  ? 0.4358 0.3789 0.4915 0.0533  -0.0788 -0.0589 873  ILE B CG1 
15093 C CG2 . ILE B 875  ? 0.4088 0.3602 0.4770 0.0643  -0.0742 -0.0672 873  ILE B CG2 
15094 C CD1 . ILE B 875  ? 0.5168 0.4594 0.5749 0.0536  -0.0843 -0.0559 873  ILE B CD1 
15095 N N   . GLY B 876  ? 0.4088 0.3324 0.4590 0.0660  -0.0771 -0.0722 874  GLY B N   
15096 C CA  . GLY B 876  ? 0.3896 0.3075 0.4408 0.0731  -0.0782 -0.0772 874  GLY B CA  
15097 C C   . GLY B 876  ? 0.4138 0.3342 0.4618 0.0730  -0.0726 -0.0812 874  GLY B C   
15098 O O   . GLY B 876  ? 0.3537 0.2819 0.4002 0.0678  -0.0676 -0.0799 874  GLY B O   
15099 N N   . ARG B 877  ? 0.4159 0.3291 0.4625 0.0792  -0.0738 -0.0861 875  ARG B N   
15100 C CA  . ARG B 877  ? 0.4524 0.3666 0.4950 0.0800  -0.0692 -0.0906 875  ARG B CA  
15101 C C   . ARG B 877  ? 0.4471 0.3532 0.4791 0.0716  -0.0698 -0.0881 875  ARG B C   
15102 O O   . ARG B 877  ? 0.4551 0.3478 0.4806 0.0681  -0.0756 -0.0853 875  ARG B O   
15103 C CB  . ARG B 877  ? 0.4689 0.3743 0.5105 0.0884  -0.0715 -0.0965 875  ARG B CB  
15104 C CG  . ARG B 877  ? 0.5071 0.4158 0.5456 0.0910  -0.0661 -0.1020 875  ARG B CG  
15105 C CD  . ARG B 877  ? 0.5619 0.4632 0.6003 0.1007  -0.0680 -0.1084 875  ARG B CD  
15106 N NE  . ARG B 877  ? 0.5947 0.4771 0.6216 0.0995  -0.0730 -0.1105 875  ARG B NE  
15107 C CZ  . ARG B 877  ? 0.7037 0.5759 0.7273 0.1072  -0.0753 -0.1166 875  ARG B CZ  
15108 N NH1 . ARG B 877  ? 0.6087 0.4885 0.6400 0.1172  -0.0728 -0.1211 875  ARG B NH1 
15109 N NH2 . ARG B 877  ? 0.7005 0.5547 0.7130 0.1049  -0.0804 -0.1181 875  ARG B NH2 
15110 N N   . THR B 878  ? 0.4046 0.3192 0.4350 0.0682  -0.0639 -0.0888 876  THR B N   
15111 C CA  . THR B 878  ? 0.4087 0.3206 0.4316 0.0596  -0.0635 -0.0853 876  THR B CA  
15112 C C   . THR B 878  ? 0.4370 0.3362 0.4502 0.0579  -0.0658 -0.0877 876  THR B C   
15113 O O   . THR B 878  ? 0.5073 0.4073 0.5153 0.0514  -0.0641 -0.0859 876  THR B O   
15114 C CB  . THR B 878  ? 0.4013 0.3283 0.4271 0.0565  -0.0564 -0.0843 876  THR B CB  
15115 O OG1 . THR B 878  ? 0.4300 0.3642 0.4585 0.0619  -0.0516 -0.0895 876  THR B OG1 
15116 C CG2 . THR B 878  ? 0.3494 0.2868 0.3830 0.0557  -0.0552 -0.0807 876  THR B CG2 
15117 N N   . ASP B 879  ? 0.4868 0.3740 0.4974 0.0633  -0.0701 -0.0916 877  ASP B N   
15118 C CA  . ASP B 879  ? 0.5099 0.3827 0.5107 0.0608  -0.0737 -0.0934 877  ASP B CA  
15119 C C   . ASP B 879  ? 0.4748 0.3328 0.4703 0.0559  -0.0811 -0.0888 877  ASP B C   
15120 O O   . ASP B 879  ? 0.4576 0.3003 0.4460 0.0556  -0.0863 -0.0906 877  ASP B O   
15121 C CB  . ASP B 879  ? 0.5227 0.3896 0.5219 0.0693  -0.0741 -0.1010 877  ASP B CB  
15122 C CG  . ASP B 879  ? 0.5629 0.4224 0.5659 0.0769  -0.0787 -0.1028 877  ASP B CG  
15123 O OD1 . ASP B 879  ? 0.5801 0.4444 0.5899 0.0774  -0.0798 -0.0991 877  ASP B OD1 
15124 O OD2 . ASP B 879  ? 0.6479 0.4962 0.6467 0.0828  -0.0815 -0.1084 877  ASP B OD2 
15125 N N   . ARG B 880  ? 0.4661 0.3284 0.4645 0.0516  -0.0818 -0.0828 878  ARG B N   
15126 C CA  . ARG B 880  ? 0.4724 0.3234 0.4656 0.0455  -0.0877 -0.0771 878  ARG B CA  
15127 C C   . ARG B 880  ? 0.4382 0.2986 0.4308 0.0372  -0.0843 -0.0713 878  ARG B C   
15128 O O   . ARG B 880  ? 0.4203 0.2945 0.4189 0.0378  -0.0797 -0.0703 878  ARG B O   
15129 C CB  . ARG B 880  ? 0.4215 0.2673 0.4182 0.0497  -0.0926 -0.0753 878  ARG B CB  
15130 N N   . LEU B 881  ? 0.4375 0.2903 0.4229 0.0296  -0.0869 -0.0676 879  LEU B N   
15131 C CA  . LEU B 881  ? 0.4023 0.2635 0.3868 0.0218  -0.0839 -0.0619 879  LEU B CA  
15132 C C   . LEU B 881  ? 0.4392 0.3051 0.4267 0.0213  -0.0843 -0.0573 879  LEU B C   
15133 O O   . LEU B 881  ? 0.4125 0.2902 0.4021 0.0183  -0.0798 -0.0546 879  LEU B O   
15134 C CB  . LEU B 881  ? 0.4185 0.2696 0.3953 0.0140  -0.0876 -0.0583 879  LEU B CB  
15135 C CG  . LEU B 881  ? 0.4426 0.3029 0.4182 0.0061  -0.0843 -0.0525 879  LEU B CG  
15136 C CD1 . LEU B 881  ? 0.4511 0.3240 0.4291 0.0058  -0.0779 -0.0552 879  LEU B CD1 
15137 C CD2 . LEU B 881  ? 0.4281 0.2781 0.3970 -0.0017 -0.0889 -0.0478 879  LEU B CD2 
15138 N N   . SER B 882  ? 0.4300 0.2864 0.4175 0.0243  -0.0898 -0.0563 880  SER B N   
15139 C CA  . SER B 882  ? 0.4479 0.3071 0.4374 0.0241  -0.0912 -0.0519 880  SER B CA  
15140 C C   . SER B 882  ? 0.4521 0.3250 0.4501 0.0292  -0.0870 -0.0542 880  SER B C   
15141 O O   . SER B 882  ? 0.4678 0.3444 0.4674 0.0286  -0.0878 -0.0508 880  SER B O   
15142 C CB  . SER B 882  ? 0.4359 0.2807 0.4232 0.0267  -0.0988 -0.0507 880  SER B CB  
15143 O OG  . SER B 882  ? 0.4847 0.3271 0.4769 0.0353  -0.1000 -0.0566 880  SER B OG  
15144 N N   . VAL B 883  ? 0.4102 0.2907 0.4133 0.0339  -0.0827 -0.0596 881  VAL B N   
15145 C CA  . VAL B 883  ? 0.3889 0.2824 0.4009 0.0386  -0.0791 -0.0615 881  VAL B CA  
15146 C C   . VAL B 883  ? 0.4041 0.3102 0.4170 0.0338  -0.0734 -0.0593 881  VAL B C   
15147 O O   . VAL B 883  ? 0.4025 0.3117 0.4125 0.0304  -0.0696 -0.0599 881  VAL B O   
15148 C CB  . VAL B 883  ? 0.4220 0.3187 0.4394 0.0460  -0.0769 -0.0680 881  VAL B CB  
15149 C CG1 . VAL B 883  ? 0.3601 0.2724 0.3870 0.0494  -0.0721 -0.0693 881  VAL B CG1 
15150 C CG2 . VAL B 883  ? 0.4769 0.3615 0.4943 0.0519  -0.0829 -0.0702 881  VAL B CG2 
15151 N N   . ASP B 884  ? 0.3807 0.2938 0.3975 0.0337  -0.0730 -0.0568 882  ASP B N   
15152 C CA  . ASP B 884  ? 0.4005 0.3245 0.4180 0.0297  -0.0681 -0.0547 882  ASP B CA  
15153 C C   . ASP B 884  ? 0.3914 0.3282 0.4173 0.0333  -0.0630 -0.0581 882  ASP B C   
15154 O O   . ASP B 884  ? 0.4180 0.3627 0.4439 0.0307  -0.0580 -0.0582 882  ASP B O   
15155 C CB  . ASP B 884  ? 0.3748 0.2984 0.3907 0.0271  -0.0708 -0.0501 882  ASP B CB  
15156 C CG  . ASP B 884  ? 0.4132 0.3252 0.4202 0.0226  -0.0753 -0.0458 882  ASP B CG  
15157 O OD1 . ASP B 884  ? 0.4286 0.3387 0.4302 0.0179  -0.0736 -0.0445 882  ASP B OD1 
15158 O OD2 . ASP B 884  ? 0.4039 0.3089 0.4095 0.0237  -0.0806 -0.0436 882  ASP B OD2 
15159 N N   . VAL B 885  ? 0.3749 0.3142 0.4082 0.0393  -0.0644 -0.0606 883  VAL B N   
15160 C CA  . VAL B 885  ? 0.3962 0.3483 0.4385 0.0426  -0.0600 -0.0630 883  VAL B CA  
15161 C C   . VAL B 885  ? 0.3628 0.3149 0.4104 0.0497  -0.0600 -0.0677 883  VAL B C   
15162 O O   . VAL B 885  ? 0.3643 0.3094 0.4132 0.0537  -0.0650 -0.0683 883  VAL B O   
15163 C CB  . VAL B 885  ? 0.4416 0.3997 0.4895 0.0426  -0.0616 -0.0606 883  VAL B CB  
15164 C CG1 . VAL B 885  ? 0.4309 0.4019 0.4895 0.0464  -0.0578 -0.0630 883  VAL B CG1 
15165 C CG2 . VAL B 885  ? 0.4324 0.3914 0.4747 0.0363  -0.0608 -0.0565 883  VAL B CG2 
15166 N N   . GLY B 886  ? 0.3230 0.2829 0.3733 0.0514  -0.0546 -0.0710 884  GLY B N   
15167 C CA  . GLY B 886  ? 0.3398 0.3012 0.3949 0.0585  -0.0537 -0.0757 884  GLY B CA  
15168 C C   . GLY B 886  ? 0.3369 0.3117 0.4037 0.0626  -0.0511 -0.0766 884  GLY B C   
15169 O O   . GLY B 886  ? 0.3168 0.2973 0.3883 0.0605  -0.0519 -0.0734 884  GLY B O   
15170 N N   . PRO B 887  ? 0.3524 0.3327 0.4239 0.0686  -0.0479 -0.0809 885  PRO B N   
15171 C CA  . PRO B 887  ? 0.3112 0.3051 0.3950 0.0731  -0.0453 -0.0818 885  PRO B CA  
15172 C C   . PRO B 887  ? 0.2835 0.2909 0.3712 0.0694  -0.0392 -0.0803 885  PRO B C   
15173 O O   . PRO B 887  ? 0.2667 0.2733 0.3475 0.0647  -0.0361 -0.0796 885  PRO B O   
15174 C CB  . PRO B 887  ? 0.2938 0.2874 0.3791 0.0808  -0.0437 -0.0872 885  PRO B CB  
15175 C CG  . PRO B 887  ? 0.3413 0.3262 0.4149 0.0782  -0.0421 -0.0892 885  PRO B CG  
15176 C CD  . PRO B 887  ? 0.3422 0.3153 0.4075 0.0717  -0.0470 -0.0853 885  PRO B CD  
15177 N N   . VAL B 888  ? 0.2748 0.2949 0.3741 0.0716  -0.0375 -0.0797 886  VAL B N   
15178 C CA  . VAL B 888  ? 0.3234 0.3570 0.4275 0.0693  -0.0311 -0.0788 886  VAL B CA  
15179 C C   . VAL B 888  ? 0.2423 0.2823 0.3484 0.0748  -0.0258 -0.0831 886  VAL B C   
15180 O O   . VAL B 888  ? 0.2587 0.2937 0.3643 0.0810  -0.0274 -0.0868 886  VAL B O   
15181 C CB  . VAL B 888  ? 0.2965 0.3413 0.4119 0.0680  -0.0315 -0.0758 886  VAL B CB  
15182 C CG1 . VAL B 888  ? 0.2942 0.3323 0.4056 0.0622  -0.0364 -0.0718 886  VAL B CG1 
15183 C CG2 . VAL B 888  ? 0.2554 0.3067 0.3822 0.0748  -0.0332 -0.0773 886  VAL B CG2 
15184 N N   . ILE B 889  ? 0.2573 0.3079 0.3650 0.0726  -0.0195 -0.0826 887  ILE B N   
15185 C CA  . ILE B 889  ? 0.2619 0.3150 0.3661 0.0762  -0.0143 -0.0865 887  ILE B CA  
15186 C C   . ILE B 889  ? 0.3072 0.3695 0.4207 0.0844  -0.0120 -0.0898 887  ILE B C   
15187 O O   . ILE B 889  ? 0.2729 0.3321 0.3820 0.0898  -0.0102 -0.0945 887  ILE B O   
15188 C CB  . ILE B 889  ? 0.2418 0.3026 0.3437 0.0711  -0.0086 -0.0845 887  ILE B CB  
15189 C CG1 . ILE B 889  ? 0.2999 0.3619 0.3957 0.0743  -0.0036 -0.0885 887  ILE B CG1 
15190 C CG2 . ILE B 889  ? 0.2755 0.3513 0.3892 0.0695  -0.0056 -0.0812 887  ILE B CG2 
15191 C CD1 . ILE B 889  ? 0.2609 0.3075 0.3445 0.0752  -0.0068 -0.0918 887  ILE B CD1 
15192 N N   . THR B 890  ? 0.2794 0.3530 0.4058 0.0856  -0.0121 -0.0877 888  THR B N   
15193 C CA  . THR B 890  ? 0.2650 0.3499 0.4018 0.0933  -0.0093 -0.0903 888  THR B CA  
15194 C C   . THR B 890  ? 0.2621 0.3520 0.4112 0.0950  -0.0139 -0.0881 888  THR B C   
15195 O O   . THR B 890  ? 0.2520 0.3392 0.4022 0.0894  -0.0181 -0.0841 888  THR B O   
15196 C CB  . THR B 890  ? 0.3265 0.4281 0.4691 0.0928  -0.0012 -0.0896 888  THR B CB  
15197 O OG1 . THR B 890  ? 0.2665 0.3757 0.4152 0.0858  -0.0011 -0.0842 888  THR B OG1 
15198 C CG2 . THR B 890  ? 0.2962 0.3943 0.4267 0.0919  0.0036  -0.0920 888  THR B CG2 
15199 N N   . SER B 891  ? 0.2896 0.3882 0.4485 0.1029  -0.0126 -0.0907 889  SER B N   
15200 C CA  . SER B 891  ? 0.2831 0.3899 0.4560 0.1050  -0.0162 -0.0885 889  SER B CA  
15201 C C   . SER B 891  ? 0.3016 0.4222 0.4838 0.0986  -0.0141 -0.0835 889  SER B C   
15202 O O   . SER B 891  ? 0.3054 0.4271 0.4943 0.0958  -0.0192 -0.0801 889  SER B O   
15203 C CB  . SER B 891  ? 0.2946 0.4110 0.4773 0.1151  -0.0140 -0.0923 889  SER B CB  
15204 O OG  . SER B 891  ? 0.4515 0.5541 0.6259 0.1217  -0.0167 -0.0972 889  SER B OG  
15205 N N   . GLU B 892  ? 0.2683 0.3994 0.4510 0.0963  -0.0067 -0.0829 890  GLU B N   
15206 C CA  . GLU B 892  ? 0.3288 0.4727 0.5204 0.0899  -0.0046 -0.0780 890  GLU B CA  
15207 C C   . GLU B 892  ? 0.3062 0.4399 0.4908 0.0814  -0.0091 -0.0743 890  GLU B C   
15208 O O   . GLU B 892  ? 0.3158 0.4538 0.5082 0.0773  -0.0125 -0.0706 890  GLU B O   
15209 C CB  . GLU B 892  ? 0.4019 0.5575 0.5937 0.0891  0.0042  -0.0779 890  GLU B CB  
15210 C CG  . GLU B 892  ? 0.4459 0.6126 0.6449 0.0815  0.0064  -0.0724 890  GLU B CG  
15211 C CD  . GLU B 892  ? 0.5668 0.7448 0.7654 0.0805  0.0150  -0.0719 890  GLU B CD  
15212 O OE1 . GLU B 892  ? 0.6643 0.8430 0.8580 0.0865  0.0196  -0.0760 890  GLU B OE1 
15213 O OE2 . GLU B 892  ? 0.6266 0.8121 0.8292 0.0739  0.0171  -0.0673 890  GLU B OE2 
15214 N N   . ALA B 893  ? 0.2768 0.3968 0.4466 0.0787  -0.0093 -0.0755 891  ALA B N   
15215 C CA  . ALA B 893  ? 0.2861 0.3959 0.4485 0.0714  -0.0135 -0.0724 891  ALA B CA  
15216 C C   . ALA B 893  ? 0.2985 0.4011 0.4632 0.0719  -0.0215 -0.0714 891  ALA B C   
15217 O O   . ALA B 893  ? 0.2810 0.3838 0.4482 0.0668  -0.0249 -0.0680 891  ALA B O   
15218 C CB  . ALA B 893  ? 0.2540 0.3507 0.4008 0.0695  -0.0126 -0.0741 891  ALA B CB  
15219 N N   . LYS B 894  ? 0.2680 0.3640 0.4316 0.0782  -0.0247 -0.0745 892  LYS B N   
15220 C CA  . LYS B 894  ? 0.2863 0.3751 0.4517 0.0792  -0.0325 -0.0735 892  LYS B CA  
15221 C C   . LYS B 894  ? 0.3288 0.4306 0.5093 0.0791  -0.0345 -0.0708 892  LYS B C   
15222 O O   . LYS B 894  ? 0.3087 0.4067 0.4898 0.0753  -0.0403 -0.0679 892  LYS B O   
15223 C CB  . LYS B 894  ? 0.3121 0.3925 0.4750 0.0867  -0.0353 -0.0773 892  LYS B CB  
15224 C CG  . LYS B 894  ? 0.3453 0.4196 0.5115 0.0886  -0.0436 -0.0760 892  LYS B CG  
15225 C CD  . LYS B 894  ? 0.3533 0.4182 0.5169 0.0962  -0.0467 -0.0797 892  LYS B CD  
15226 C CE  . LYS B 894  ? 0.3930 0.4517 0.5597 0.0979  -0.0553 -0.0778 892  LYS B CE  
15227 N NZ  . LYS B 894  ? 0.4029 0.4535 0.5691 0.1062  -0.0586 -0.0813 892  LYS B NZ  
15228 N N   . ASP B 895  ? 0.2618 0.3791 0.4546 0.0832  -0.0300 -0.0717 893  ASP B N   
15229 C CA  . ASP B 895  ? 0.3091 0.4398 0.5173 0.0827  -0.0320 -0.0688 893  ASP B CA  
15230 C C   . ASP B 895  ? 0.3148 0.4494 0.5241 0.0739  -0.0318 -0.0645 893  ASP B C   
15231 O O   . ASP B 895  ? 0.2833 0.4207 0.4999 0.0712  -0.0371 -0.0616 893  ASP B O   
15232 C CB  . ASP B 895  ? 0.3090 0.4570 0.5304 0.0888  -0.0263 -0.0703 893  ASP B CB  
15233 C CG  . ASP B 895  ? 0.3714 0.5164 0.5940 0.0985  -0.0277 -0.0746 893  ASP B CG  
15234 O OD1 . ASP B 895  ? 0.4532 0.5854 0.6713 0.1002  -0.0348 -0.0752 893  ASP B OD1 
15235 O OD2 . ASP B 895  ? 0.4268 0.5820 0.6547 0.1046  -0.0217 -0.0774 893  ASP B OD2 
15236 N N   . ASN B 896  ? 0.2432 0.3771 0.4449 0.0696  -0.0263 -0.0641 894  ASN B N   
15237 C CA  . ASN B 896  ? 0.2876 0.4240 0.4895 0.0615  -0.0260 -0.0602 894  ASN B CA  
15238 C C   . ASN B 896  ? 0.3324 0.4548 0.5255 0.0570  -0.0330 -0.0587 894  ASN B C   
15239 O O   . ASN B 896  ? 0.2998 0.4245 0.4978 0.0524  -0.0368 -0.0557 894  ASN B O   
15240 C CB  . ASN B 896  ? 0.3506 0.4883 0.5453 0.0588  -0.0187 -0.0604 894  ASN B CB  
15241 C CG  . ASN B 896  ? 0.4472 0.5859 0.6407 0.0507  -0.0181 -0.0566 894  ASN B CG  
15242 O OD1 . ASN B 896  ? 0.4588 0.5876 0.6461 0.0464  -0.0230 -0.0551 894  ASN B OD1 
15243 N ND2 . ASN B 896  ? 0.5479 0.6983 0.7467 0.0488  -0.0120 -0.0549 894  ASN B ND2 
15244 N N   . ILE B 897  ? 0.2877 0.3956 0.4679 0.0583  -0.0349 -0.0608 895  ILE B N   
15245 C CA  . ILE B 897  ? 0.3246 0.4192 0.4954 0.0546  -0.0410 -0.0594 895  ILE B CA  
15246 C C   . ILE B 897  ? 0.3590 0.4537 0.5370 0.0562  -0.0485 -0.0583 895  ILE B C   
15247 O O   . ILE B 897  ? 0.3309 0.4231 0.5084 0.0517  -0.0531 -0.0558 895  ILE B O   
15248 C CB  . ILE B 897  ? 0.2623 0.3427 0.4189 0.0560  -0.0412 -0.0616 895  ILE B CB  
15249 C CG1 . ILE B 897  ? 0.3133 0.3935 0.4623 0.0534  -0.0346 -0.0623 895  ILE B CG1 
15250 C CG2 . ILE B 897  ? 0.2821 0.3495 0.4294 0.0527  -0.0476 -0.0600 895  ILE B CG2 
15251 C CD1 . ILE B 897  ? 0.2578 0.3288 0.3970 0.0567  -0.0332 -0.0654 895  ILE B CD1 
15252 N N   . GLU B 898  ? 0.3491 0.4463 0.5335 0.0630  -0.0500 -0.0603 896  GLU B N   
15253 C CA  . GLU B 898  ? 0.3507 0.4478 0.5421 0.0651  -0.0575 -0.0592 896  GLU B CA  
15254 C C   . GLU B 898  ? 0.3652 0.4762 0.5708 0.0624  -0.0587 -0.0565 896  GLU B C   
15255 O O   . GLU B 898  ? 0.3415 0.4504 0.5495 0.0605  -0.0657 -0.0545 896  GLU B O   
15256 C CB  . GLU B 898  ? 0.4122 0.5093 0.6079 0.0736  -0.0586 -0.0620 896  GLU B CB  
15257 C CG  . GLU B 898  ? 0.4087 0.4893 0.5899 0.0755  -0.0597 -0.0642 896  GLU B CG  
15258 C CD  . GLU B 898  ? 0.4725 0.5517 0.6571 0.0842  -0.0607 -0.0674 896  GLU B CD  
15259 O OE1 . GLU B 898  ? 0.5121 0.6048 0.7092 0.0892  -0.0574 -0.0689 896  GLU B OE1 
15260 O OE2 . GLU B 898  ? 0.5264 0.5910 0.7012 0.0860  -0.0649 -0.0684 896  GLU B OE2 
15261 N N   . LYS B 899  ? 0.3305 0.4556 0.5453 0.0620  -0.0522 -0.0562 897  LYS B N   
15262 C CA  . LYS B 899  ? 0.3351 0.4734 0.5632 0.0581  -0.0531 -0.0530 897  LYS B CA  
15263 C C   . LYS B 899  ? 0.3503 0.4809 0.5713 0.0502  -0.0571 -0.0504 897  LYS B C   
15264 O O   . LYS B 899  ? 0.3393 0.4730 0.5675 0.0474  -0.0629 -0.0482 897  LYS B O   
15265 C CB  . LYS B 899  ? 0.3696 0.5228 0.6058 0.0579  -0.0446 -0.0527 897  LYS B CB  
15266 C CG  . LYS B 899  ? 0.3796 0.5466 0.6292 0.0527  -0.0446 -0.0489 897  LYS B CG  
15267 C CD  . LYS B 899  ? 0.4291 0.6091 0.6839 0.0522  -0.0355 -0.0483 897  LYS B CD  
15268 C CE  . LYS B 899  ? 0.4695 0.6611 0.7349 0.0453  -0.0350 -0.0439 897  LYS B CE  
15269 N NZ  . LYS B 899  ? 0.4426 0.6423 0.7078 0.0432  -0.0261 -0.0429 897  LYS B NZ  
15270 N N   . HIS B 900  ? 0.3157 0.4359 0.5225 0.0467  -0.0543 -0.0509 898  HIS B N   
15271 C CA  . HIS B 900  ? 0.3381 0.4496 0.5366 0.0401  -0.0579 -0.0490 898  HIS B CA  
15272 C C   . HIS B 900  ? 0.3466 0.4465 0.5387 0.0406  -0.0661 -0.0489 898  HIS B C   
15273 O O   . HIS B 900  ? 0.3702 0.4680 0.5625 0.0365  -0.0716 -0.0471 898  HIS B O   
15274 C CB  . HIS B 900  ? 0.3384 0.4418 0.5234 0.0372  -0.0528 -0.0496 898  HIS B CB  
15275 C CG  . HIS B 900  ? 0.3377 0.4296 0.5115 0.0321  -0.0567 -0.0484 898  HIS B CG  
15276 N ND1 . HIS B 900  ? 0.3422 0.4365 0.5188 0.0266  -0.0583 -0.0462 898  HIS B ND1 
15277 C CD2 . HIS B 900  ? 0.3193 0.3975 0.4792 0.0317  -0.0591 -0.0492 898  HIS B CD2 
15278 C CE1 . HIS B 900  ? 0.3719 0.4541 0.5361 0.0236  -0.0614 -0.0461 898  HIS B CE1 
15279 N NE2 . HIS B 900  ? 0.3229 0.3958 0.4769 0.0265  -0.0617 -0.0477 898  HIS B NE2 
15280 N N   . ILE B 901  ? 0.3169 0.4086 0.5023 0.0453  -0.0673 -0.0509 899  ILE B N   
15281 C CA  . ILE B 901  ? 0.3432 0.4230 0.5209 0.0457  -0.0748 -0.0505 899  ILE B CA  
15282 C C   . ILE B 901  ? 0.4310 0.5173 0.6208 0.0472  -0.0816 -0.0492 899  ILE B C   
15283 O O   . ILE B 901  ? 0.4309 0.5118 0.6174 0.0440  -0.0882 -0.0476 899  ILE B O   
15284 C CB  . ILE B 901  ? 0.3580 0.4279 0.5270 0.0504  -0.0746 -0.0526 899  ILE B CB  
15285 C CG1 . ILE B 901  ? 0.3656 0.4278 0.5213 0.0479  -0.0691 -0.0534 899  ILE B CG1 
15286 C CG2 . ILE B 901  ? 0.4034 0.4625 0.5664 0.0514  -0.0828 -0.0516 899  ILE B CG2 
15287 C CD1 . ILE B 901  ? 0.3058 0.3591 0.4538 0.0520  -0.0683 -0.0555 899  ILE B CD1 
15288 N N   . GLU B 902  ? 0.3688 0.4675 0.5728 0.0520  -0.0800 -0.0499 900  GLU B N   
15289 C CA  . GLU B 902  ? 0.3990 0.5058 0.6164 0.0538  -0.0863 -0.0485 900  GLU B CA  
15290 C C   . GLU B 902  ? 0.3984 0.5129 0.6233 0.0474  -0.0883 -0.0458 900  GLU B C   
15291 O O   . GLU B 902  ? 0.4186 0.5337 0.6483 0.0462  -0.0960 -0.0442 900  GLU B O   
15292 C CB  . GLU B 902  ? 0.4134 0.5331 0.6451 0.0608  -0.0832 -0.0499 900  GLU B CB  
15293 C CG  . GLU B 902  ? 0.4430 0.5536 0.6689 0.0679  -0.0845 -0.0524 900  GLU B CG  
15294 C CD  . GLU B 902  ? 0.5433 0.6420 0.7630 0.0681  -0.0940 -0.0512 900  GLU B CD  
15295 O OE1 . GLU B 902  ? 0.4940 0.5988 0.7234 0.0674  -0.1003 -0.0492 900  GLU B OE1 
15296 O OE2 . GLU B 902  ? 0.5718 0.6552 0.7768 0.0685  -0.0953 -0.0520 900  GLU B OE2 
15297 N N   . ARG B 903  ? 0.3493 0.4692 0.5748 0.0431  -0.0820 -0.0453 901  ARG B N   
15298 C CA  . ARG B 903  ? 0.3897 0.5145 0.6205 0.0364  -0.0843 -0.0427 901  ARG B CA  
15299 C C   . ARG B 903  ? 0.4572 0.5672 0.6742 0.0318  -0.0904 -0.0422 901  ARG B C   
15300 O O   . ARG B 903  ? 0.4728 0.5838 0.6941 0.0280  -0.0969 -0.0404 901  ARG B O   
15301 C CB  . ARG B 903  ? 0.3950 0.5273 0.6281 0.0330  -0.0761 -0.0420 901  ARG B CB  
15302 C CG  . ARG B 903  ? 0.4540 0.5920 0.6939 0.0260  -0.0782 -0.0391 901  ARG B CG  
15303 C CD  . ARG B 903  ? 0.5007 0.6481 0.7453 0.0232  -0.0701 -0.0379 901  ARG B CD  
15304 N NE  . ARG B 903  ? 0.5698 0.7216 0.8210 0.0160  -0.0728 -0.0348 901  ARG B NE  
15305 C CZ  . ARG B 903  ? 0.5922 0.7331 0.8326 0.0104  -0.0745 -0.0343 901  ARG B CZ  
15306 N NH1 . ARG B 903  ? 0.6088 0.7354 0.8322 0.0110  -0.0730 -0.0364 901  ARG B NH1 
15307 N NH2 . ARG B 903  ? 0.5907 0.7351 0.8379 0.0041  -0.0778 -0.0316 901  ARG B NH2 
15308 N N   . MET B 904  ? 0.4003 0.4966 0.6006 0.0320  -0.0887 -0.0437 902  MET B N   
15309 C CA  . MET B 904  ? 0.4408 0.5231 0.6270 0.0285  -0.0940 -0.0434 902  MET B CA  
15310 C C   . MET B 904  ? 0.4968 0.5738 0.6821 0.0310  -0.1026 -0.0430 902  MET B C   
15311 O O   . MET B 904  ? 0.5203 0.5924 0.7022 0.0277  -0.1094 -0.0420 902  MET B O   
15312 C CB  . MET B 904  ? 0.4198 0.4906 0.5895 0.0284  -0.0893 -0.0448 902  MET B CB  
15313 C CG  . MET B 904  ? 0.3267 0.4009 0.4951 0.0255  -0.0815 -0.0449 902  MET B CG  
15314 S SD  . MET B 904  ? 0.5179 0.5919 0.6859 0.0183  -0.0834 -0.0433 902  MET B SD  
15315 C CE  . MET B 904  ? 0.5016 0.5939 0.6893 0.0174  -0.0796 -0.0417 902  MET B CE  
15316 N N   . ARG B 905  ? 0.4951 0.5720 0.6825 0.0371  -0.1027 -0.0440 903  ARG B N   
15317 C CA  . ARG B 905  ? 0.5445 0.6178 0.7332 0.0401  -0.1111 -0.0433 903  ARG B CA  
15318 C C   . ARG B 905  ? 0.5296 0.6141 0.7335 0.0388  -0.1168 -0.0416 903  ARG B C   
15319 O O   . ARG B 905  ? 0.5531 0.6324 0.7544 0.0372  -0.1252 -0.0404 903  ARG B O   
15320 C CB  . ARG B 905  ? 0.5256 0.5994 0.7173 0.0474  -0.1097 -0.0447 903  ARG B CB  
15321 C CG  . ARG B 905  ? 0.5482 0.6075 0.7275 0.0498  -0.1150 -0.0446 903  ARG B CG  
15322 C CD  . ARG B 905  ? 0.5103 0.5706 0.6951 0.0573  -0.1148 -0.0460 903  ARG B CD  
15323 N NE  . ARG B 905  ? 0.5063 0.5591 0.6814 0.0592  -0.1088 -0.0479 903  ARG B NE  
15324 C CZ  . ARG B 905  ? 0.5126 0.5506 0.6730 0.0593  -0.1108 -0.0477 903  ARG B CZ  
15325 N NH1 . ARG B 905  ? 0.5809 0.6095 0.7331 0.0573  -0.1181 -0.0455 903  ARG B NH1 
15326 N NH2 . ARG B 905  ? 0.5145 0.5470 0.6682 0.0612  -0.1056 -0.0495 903  ARG B NH2 
15327 N N   . GLY B 906  ? 0.4900 0.5899 0.7096 0.0391  -0.1124 -0.0413 904  GLY B N   
15328 C CA  . GLY B 906  ? 0.5062 0.6182 0.7416 0.0371  -0.1175 -0.0393 904  GLY B CA  
15329 C C   . GLY B 906  ? 0.5669 0.6736 0.7970 0.0297  -0.1225 -0.0379 904  GLY B C   
15330 O O   . GLY B 906  ? 0.5810 0.6900 0.8174 0.0280  -0.1308 -0.0364 904  GLY B O   
15331 N N   . LEU B 907  ? 0.5555 0.6548 0.7738 0.0254  -0.1179 -0.0385 905  LEU B N   
15332 C CA  . LEU B 907  ? 0.5330 0.6259 0.7448 0.0188  -0.1223 -0.0377 905  LEU B CA  
15333 C C   . LEU B 907  ? 0.5449 0.6220 0.7404 0.0184  -0.1293 -0.0384 905  LEU B C   
15334 O O   . LEU B 907  ? 0.5882 0.6581 0.7759 0.0135  -0.1332 -0.0383 905  LEU B O   
15335 C CB  . LEU B 907  ? 0.4821 0.5731 0.6878 0.0147  -0.1149 -0.0381 905  LEU B CB  
15336 N N   . GLY B 908  ? 0.5444 0.6155 0.7341 0.0235  -0.1309 -0.0390 906  GLY B N   
15337 C CA  . GLY B 908  ? 0.5435 0.6008 0.7186 0.0234  -0.1379 -0.0390 906  GLY B CA  
15338 C C   . GLY B 908  ? 0.5943 0.6377 0.7496 0.0225  -0.1340 -0.0401 906  GLY B C   
15339 O O   . GLY B 908  ? 0.5992 0.6311 0.7411 0.0221  -0.1393 -0.0399 906  GLY B O   
15340 N N   . ARG B 909  ? 0.5578 0.6025 0.7108 0.0223  -0.1250 -0.0411 907  ARG B N   
15341 C CA  . ARG B 909  ? 0.5053 0.5382 0.6407 0.0214  -0.1211 -0.0420 907  ARG B CA  
15342 C C   . ARG B 909  ? 0.5451 0.5704 0.6723 0.0256  -0.1217 -0.0420 907  ARG B C   
15343 O O   . ARG B 909  ? 0.6227 0.6531 0.7589 0.0301  -0.1213 -0.0420 907  ARG B O   
15344 C CB  . ARG B 909  ? 0.5337 0.5708 0.6700 0.0201  -0.1117 -0.0429 907  ARG B CB  
15345 N N   . LYS B 910  ? 0.5271 0.5401 0.6374 0.0243  -0.1228 -0.0418 908  LYS B N   
15346 C CA  . LYS B 910  ? 0.5555 0.5604 0.6570 0.0275  -0.1233 -0.0412 908  LYS B CA  
15347 C C   . LYS B 910  ? 0.5779 0.5850 0.6808 0.0296  -0.1151 -0.0422 908  LYS B C   
15348 O O   . LYS B 910  ? 0.5763 0.5853 0.6771 0.0274  -0.1085 -0.0432 908  LYS B O   
15349 C CB  . LYS B 910  ? 0.5828 0.5751 0.6656 0.0250  -0.1253 -0.0404 908  LYS B CB  
15350 N N   . VAL B 911  ? 0.5764 0.5828 0.6827 0.0342  -0.1160 -0.0421 909  VAL B N   
15351 C CA  . VAL B 911  ? 0.5552 0.5638 0.6640 0.0369  -0.1093 -0.0435 909  VAL B CA  
15352 C C   . VAL B 911  ? 0.5318 0.5298 0.6317 0.0396  -0.1113 -0.0428 909  VAL B C   
15353 O O   . VAL B 911  ? 0.6214 0.6177 0.7250 0.0431  -0.1173 -0.0420 909  VAL B O   
15354 C CB  . VAL B 911  ? 0.5552 0.5766 0.6817 0.0407  -0.1075 -0.0448 909  VAL B CB  
15355 C CG1 . VAL B 911  ? 0.4912 0.5134 0.6184 0.0440  -0.1009 -0.0466 909  VAL B CG1 
15356 C CG2 . VAL B 911  ? 0.4909 0.5231 0.6268 0.0374  -0.1053 -0.0449 909  VAL B CG2 
15357 N N   . GLU B 912  ? 0.5263 0.5175 0.6148 0.0379  -0.1067 -0.0428 910  GLU B N   
15358 C CA  . GLU B 912  ? 0.5290 0.5100 0.6089 0.0397  -0.1079 -0.0419 910  GLU B CA  
15359 C C   . GLU B 912  ? 0.5545 0.5381 0.6390 0.0425  -0.1021 -0.0441 910  GLU B C   
15360 O O   . GLU B 912  ? 0.4715 0.4613 0.5584 0.0410  -0.0955 -0.0457 910  GLU B O   
15361 C CB  . GLU B 912  ? 0.5789 0.5504 0.6425 0.0353  -0.1072 -0.0400 910  GLU B CB  
15362 C CG  . GLU B 912  ? 0.5886 0.5492 0.6423 0.0359  -0.1083 -0.0383 910  GLU B CG  
15363 C CD  . GLU B 912  ? 0.6084 0.5604 0.6552 0.0361  -0.1163 -0.0354 910  GLU B CD  
15364 O OE1 . GLU B 912  ? 0.5893 0.5434 0.6374 0.0355  -0.1209 -0.0348 910  GLU B OE1 
15365 O OE2 . GLU B 912  ? 0.6156 0.5583 0.6553 0.0368  -0.1183 -0.0335 910  GLU B OE2 
15366 N N   . GLN B 913  ? 0.4957 0.4741 0.5811 0.0468  -0.1049 -0.0443 911  GLN B N   
15367 C CA  . GLN B 913  ? 0.5145 0.4935 0.6028 0.0500  -0.1001 -0.0467 911  GLN B CA  
15368 C C   . GLN B 913  ? 0.5743 0.5402 0.6537 0.0514  -0.1032 -0.0457 911  GLN B C   
15369 O O   . GLN B 913  ? 0.5917 0.5509 0.6689 0.0530  -0.1101 -0.0437 911  GLN B O   
15370 C CB  . GLN B 913  ? 0.4877 0.4774 0.5916 0.0555  -0.0995 -0.0492 911  GLN B CB  
15371 C CG  . GLN B 913  ? 0.4446 0.4482 0.5583 0.0539  -0.0949 -0.0503 911  GLN B CG  
15372 C CD  . GLN B 913  ? 0.5009 0.5159 0.6296 0.0594  -0.0928 -0.0527 911  GLN B CD  
15373 O OE1 . GLN B 913  ? 0.5197 0.5362 0.6561 0.0642  -0.0977 -0.0528 911  GLN B OE1 
15374 N NE2 . GLN B 913  ? 0.3979 0.4215 0.5308 0.0590  -0.0854 -0.0545 911  GLN B NE2 
15375 N N   . ILE B 914  ? 0.5377 0.5000 0.6120 0.0508  -0.0984 -0.0470 912  ILE B N   
15376 C CA  . ILE B 914  ? 0.5537 0.5039 0.6213 0.0525  -0.1011 -0.0466 912  ILE B CA  
15377 C C   . ILE B 914  ? 0.6457 0.5968 0.7231 0.0599  -0.1038 -0.0492 912  ILE B C   
15378 O O   . ILE B 914  ? 0.5870 0.5494 0.6761 0.0636  -0.1007 -0.0521 912  ILE B O   
15379 C CB  . ILE B 914  ? 0.5591 0.5059 0.6193 0.0496  -0.0954 -0.0475 912  ILE B CB  
15380 N N   . GLY B 915  ? 0.6430 0.5820 0.7156 0.0623  -0.1095 -0.0480 913  GLY B N   
15381 C CA  . GLY B 915  ? 0.6076 0.5457 0.6883 0.0699  -0.1122 -0.0506 913  GLY B CA  
15382 C C   . GLY B 915  ? 0.6305 0.5664 0.7104 0.0723  -0.1073 -0.0545 913  GLY B C   
15383 O O   . GLY B 915  ? 0.7049 0.6333 0.7746 0.0680  -0.1050 -0.0539 913  GLY B O   
15384 N N   . LEU B 916  ? 0.5780 0.5211 0.6688 0.0793  -0.1057 -0.0585 914  LEU B N   
15385 C CA  . LEU B 916  ? 0.6009 0.5426 0.6913 0.0826  -0.1011 -0.0628 914  LEU B CA  
15386 C C   . LEU B 916  ? 0.6203 0.5498 0.7095 0.0890  -0.1065 -0.0645 914  LEU B C   
15387 O O   . LEU B 916  ? 0.5875 0.5184 0.6846 0.0948  -0.1113 -0.0646 914  LEU B O   
15388 C CB  . LEU B 916  ? 0.5759 0.5341 0.6784 0.0863  -0.0946 -0.0665 914  LEU B CB  
15389 C CG  . LEU B 916  ? 0.5581 0.5284 0.6623 0.0804  -0.0887 -0.0654 914  LEU B CG  
15390 C CD1 . LEU B 916  ? 0.5099 0.4962 0.6266 0.0846  -0.0828 -0.0687 914  LEU B CD1 
15391 C CD2 . LEU B 916  ? 0.5034 0.4674 0.5954 0.0739  -0.0850 -0.0646 914  LEU B CD2 
15392 N N   . ALA B 917  ? 0.5825 0.4999 0.6621 0.0880  -0.1061 -0.0658 915  ALA B N   
15393 C CA  . ALA B 917  ? 0.6374 0.5413 0.7147 0.0940  -0.1113 -0.0678 915  ALA B CA  
15394 C C   . ALA B 917  ? 0.5954 0.5075 0.6840 0.1037  -0.1089 -0.0734 915  ALA B C   
15395 O O   . ALA B 917  ? 0.5769 0.5036 0.6725 0.1048  -0.1019 -0.0762 915  ALA B O   
15396 C CB  . ALA B 917  ? 0.6561 0.5458 0.7208 0.0901  -0.1111 -0.0682 915  ALA B CB  
15397 N N   . SER B 918  ? 0.6598 0.5621 0.7497 0.1109  -0.1148 -0.0750 916  SER B N   
15398 C CA  . SER B 918  ? 0.6714 0.5811 0.7720 0.1211  -0.1129 -0.0805 916  SER B CA  
15399 C C   . SER B 918  ? 0.6307 0.5426 0.7286 0.1226  -0.1056 -0.0859 916  SER B C   
15400 O O   . SER B 918  ? 0.5836 0.5099 0.6910 0.1280  -0.0999 -0.0898 916  SER B O   
15401 C CB  . SER B 918  ? 0.6090 0.5049 0.7095 0.1287  -0.1209 -0.0814 916  SER B CB  
15402 N N   . GLU B 919  ? 0.6438 0.5421 0.7284 0.1174  -0.1057 -0.0859 917  GLU B N   
15403 C CA  . GLU B 919  ? 0.6484 0.5463 0.7286 0.1185  -0.0999 -0.0910 917  GLU B CA  
15404 C C   . GLU B 919  ? 0.6232 0.5397 0.7086 0.1157  -0.0909 -0.0920 917  GLU B C   
15405 O O   . GLU B 919  ? 0.6280 0.5473 0.7117 0.1181  -0.0855 -0.0967 917  GLU B O   
15406 C CB  . GLU B 919  ? 0.6367 0.5174 0.7021 0.1116  -0.1024 -0.0896 917  GLU B CB  
15407 N N   . THR B 920  ? 0.5995 0.5279 0.6904 0.1107  -0.0894 -0.0876 918  THR B N   
15408 C CA  . THR B 920  ? 0.5066 0.4521 0.6026 0.1080  -0.0813 -0.0881 918  THR B CA  
15409 C C   . THR B 920  ? 0.5243 0.4860 0.6342 0.1159  -0.0772 -0.0915 918  THR B C   
15410 O O   . THR B 920  ? 0.4633 0.4391 0.5776 0.1144  -0.0701 -0.0924 918  THR B O   
15411 C CB  . THR B 920  ? 0.5390 0.4903 0.6353 0.0996  -0.0814 -0.0824 918  THR B CB  
15412 O OG1 . THR B 920  ? 0.4867 0.4427 0.5920 0.1021  -0.0861 -0.0799 918  THR B OG1 
15413 C CG2 . THR B 920  ? 0.5071 0.4440 0.5901 0.0919  -0.0848 -0.0788 918  THR B CG2 
15414 N N   . GLY B 921  ? 0.4767 0.4373 0.5940 0.1241  -0.0816 -0.0930 919  GLY B N   
15415 C CA  . GLY B 921  ? 0.5056 0.4830 0.6373 0.1318  -0.0779 -0.0958 919  GLY B CA  
15416 C C   . GLY B 921  ? 0.4858 0.4690 0.6174 0.1369  -0.0705 -0.1017 919  GLY B C   
15417 O O   . GLY B 921  ? 0.4905 0.4914 0.6336 0.1410  -0.0649 -0.1032 919  GLY B O   
15418 N N   . VAL B 922  ? 0.4525 0.4214 0.5713 0.1366  -0.0704 -0.1048 920  VAL B N   
15419 C CA  . VAL B 922  ? 0.4588 0.4322 0.5756 0.1412  -0.0635 -0.1106 920  VAL B CA  
15420 C C   . VAL B 922  ? 0.4433 0.4274 0.5578 0.1340  -0.0560 -0.1093 920  VAL B C   
15421 O O   . VAL B 922  ? 0.4359 0.4269 0.5497 0.1374  -0.0495 -0.1136 920  VAL B O   
15422 C CB  . VAL B 922  ? 0.4633 0.4162 0.5671 0.1441  -0.0672 -0.1149 920  VAL B CB  
15423 C CG1 . VAL B 922  ? 0.4758 0.4187 0.5828 0.1526  -0.0744 -0.1165 920  VAL B CG1 
15424 C CG2 . VAL B 922  ? 0.4852 0.4235 0.5758 0.1339  -0.0706 -0.1112 920  VAL B CG2 
15425 N N   . GLY B 923  ? 0.4143 0.4001 0.5272 0.1245  -0.0566 -0.1037 921  GLY B N   
15426 C CA  . GLY B 923  ? 0.4098 0.4053 0.5208 0.1175  -0.0500 -0.1021 921  GLY B CA  
15427 C C   . GLY B 923  ? 0.3402 0.3505 0.4615 0.1131  -0.0485 -0.0972 921  GLY B C   
15428 O O   . GLY B 923  ? 0.4220 0.4363 0.5528 0.1160  -0.0524 -0.0955 921  GLY B O   
15429 N N   . THR B 924  ? 0.3280 0.3460 0.4477 0.1062  -0.0435 -0.0949 922  THR B N   
15430 C CA  . THR B 924  ? 0.3139 0.3449 0.4427 0.1014  -0.0423 -0.0903 922  THR B CA  
15431 C C   . THR B 924  ? 0.3269 0.3491 0.4475 0.0926  -0.0459 -0.0858 922  THR B C   
15432 O O   . THR B 924  ? 0.3054 0.3266 0.4187 0.0867  -0.0426 -0.0847 922  THR B O   
15433 C CB  . THR B 924  ? 0.3111 0.3581 0.4450 0.1004  -0.0340 -0.0907 922  THR B CB  
15434 O OG1 . THR B 924  ? 0.3669 0.4084 0.4891 0.0966  -0.0303 -0.0919 922  THR B OG1 
15435 C CG2 . THR B 924  ? 0.2940 0.3521 0.4373 0.1094  -0.0301 -0.0947 922  THR B CG2 
15436 N N   . PHE B 925  ? 0.3231 0.3396 0.4453 0.0919  -0.0527 -0.0830 923  PHE B N   
15437 C CA  . PHE B 925  ? 0.3267 0.3348 0.4410 0.0843  -0.0564 -0.0787 923  PHE B CA  
15438 C C   . PHE B 925  ? 0.3019 0.3189 0.4244 0.0812  -0.0582 -0.0749 923  PHE B C   
15439 O O   . PHE B 925  ? 0.3428 0.3673 0.4764 0.0856  -0.0603 -0.0749 923  PHE B O   
15440 C CB  . PHE B 925  ? 0.3809 0.3718 0.4869 0.0852  -0.0635 -0.0783 923  PHE B CB  
15441 C CG  . PHE B 925  ? 0.3669 0.3463 0.4627 0.0862  -0.0628 -0.0814 923  PHE B CG  
15442 C CD1 . PHE B 925  ? 0.3510 0.3289 0.4489 0.0940  -0.0620 -0.0863 923  PHE B CD1 
15443 C CD2 . PHE B 925  ? 0.3431 0.3131 0.4271 0.0793  -0.0630 -0.0794 923  PHE B CD2 
15444 C CE1 . PHE B 925  ? 0.3795 0.3456 0.4673 0.0947  -0.0620 -0.0895 923  PHE B CE1 
15445 C CE2 . PHE B 925  ? 0.3825 0.3419 0.4573 0.0796  -0.0628 -0.0821 923  PHE B CE2 
15446 C CZ  . PHE B 925  ? 0.4018 0.3586 0.4781 0.0872  -0.0626 -0.0872 923  PHE B CZ  
15447 N N   . VAL B 926  ? 0.3055 0.3212 0.4221 0.0737  -0.0577 -0.0716 924  VAL B N   
15448 C CA  . VAL B 926  ? 0.2905 0.3106 0.4113 0.0698  -0.0607 -0.0679 924  VAL B CA  
15449 C C   . VAL B 926  ? 0.3103 0.3171 0.4191 0.0648  -0.0652 -0.0650 924  VAL B C   
15450 O O   . VAL B 926  ? 0.3216 0.3232 0.4207 0.0605  -0.0625 -0.0646 924  VAL B O   
15451 C CB  . VAL B 926  ? 0.2837 0.3163 0.4094 0.0656  -0.0553 -0.0667 924  VAL B CB  
15452 C CG1 . VAL B 926  ? 0.2884 0.3232 0.4169 0.0613  -0.0593 -0.0631 924  VAL B CG1 
15453 C CG2 . VAL B 926  ? 0.3058 0.3525 0.4434 0.0703  -0.0504 -0.0690 924  VAL B CG2 
15454 N N   . PRO B 927  ? 0.3444 0.3462 0.4534 0.0649  -0.0720 -0.0627 925  PRO B N   
15455 C CA  . PRO B 927  ? 0.3645 0.3541 0.4615 0.0601  -0.0759 -0.0597 925  PRO B CA  
15456 C C   . PRO B 927  ? 0.3538 0.3469 0.4468 0.0535  -0.0733 -0.0574 925  PRO B C   
15457 O O   . PRO B 927  ? 0.3341 0.3380 0.4350 0.0525  -0.0714 -0.0571 925  PRO B O   
15458 C CB  . PRO B 927  ? 0.4320 0.4174 0.5317 0.0626  -0.0837 -0.0579 925  PRO B CB  
15459 C CG  . PRO B 927  ? 0.3808 0.3798 0.4952 0.0661  -0.0834 -0.0589 925  PRO B CG  
15460 C CD  . PRO B 927  ? 0.3504 0.3581 0.4708 0.0694  -0.0764 -0.0625 925  PRO B CD  
15461 N N   . PRO B 928  ? 0.3832 0.3677 0.4642 0.0488  -0.0730 -0.0556 926  PRO B N   
15462 C CA  . PRO B 928  ? 0.3785 0.3650 0.4549 0.0431  -0.0715 -0.0533 926  PRO B CA  
15463 C C   . PRO B 928  ? 0.3718 0.3609 0.4523 0.0427  -0.0763 -0.0514 926  PRO B C   
15464 O O   . PRO B 928  ? 0.4503 0.4336 0.5301 0.0446  -0.0824 -0.0502 926  PRO B O   
15465 C CB  . PRO B 928  ? 0.3794 0.3547 0.4426 0.0395  -0.0725 -0.0512 926  PRO B CB  
15466 C CG  . PRO B 928  ? 0.4503 0.4209 0.5120 0.0421  -0.0711 -0.0534 926  PRO B CG  
15467 C CD  . PRO B 928  ? 0.3745 0.3479 0.4462 0.0486  -0.0734 -0.0559 926  PRO B CD  
15468 N N   . THR B 929  ? 0.3579 0.3557 0.4430 0.0403  -0.0738 -0.0512 927  THR B N   
15469 C CA  . THR B 929  ? 0.3535 0.3554 0.4443 0.0398  -0.0782 -0.0500 927  THR B CA  
15470 C C   . THR B 929  ? 0.3705 0.3719 0.4549 0.0345  -0.0773 -0.0484 927  THR B C   
15471 O O   . THR B 929  ? 0.3769 0.3815 0.4594 0.0321  -0.0718 -0.0489 927  THR B O   
15472 C CB  . THR B 929  ? 0.3808 0.3954 0.4867 0.0427  -0.0766 -0.0515 927  THR B CB  
15473 O OG1 . THR B 929  ? 0.3566 0.3718 0.4682 0.0484  -0.0771 -0.0534 927  THR B OG1 
15474 C CG2 . THR B 929  ? 0.3869 0.4059 0.4995 0.0418  -0.0819 -0.0500 927  THR B CG2 
15475 N N   . ILE B 930  ? 0.4504 0.4476 0.5311 0.0331  -0.0831 -0.0466 928  ILE B N   
15476 C CA  . ILE B 930  ? 0.3820 0.3785 0.4570 0.0288  -0.0833 -0.0456 928  ILE B CA  
15477 C C   . ILE B 930  ? 0.4283 0.4309 0.5126 0.0288  -0.0877 -0.0455 928  ILE B C   
15478 O O   . ILE B 930  ? 0.4759 0.4778 0.5645 0.0312  -0.0936 -0.0449 928  ILE B O   
15479 C CB  . ILE B 930  ? 0.4219 0.4075 0.4825 0.0267  -0.0864 -0.0436 928  ILE B CB  
15480 C CG1 . ILE B 930  ? 0.4488 0.4289 0.5011 0.0263  -0.0825 -0.0432 928  ILE B CG1 
15481 C CG2 . ILE B 930  ? 0.3997 0.3847 0.4543 0.0230  -0.0867 -0.0431 928  ILE B CG2 
15482 C CD1 . ILE B 930  ? 0.4360 0.4065 0.4746 0.0240  -0.0849 -0.0407 928  ILE B CD1 
15483 N N   . ILE B 931  ? 0.4027 0.4112 0.4905 0.0260  -0.0851 -0.0459 929  ILE B N   
15484 C CA  . ILE B 931  ? 0.4131 0.4274 0.5099 0.0250  -0.0891 -0.0456 929  ILE B CA  
15485 C C   . ILE B 931  ? 0.4524 0.4624 0.5408 0.0207  -0.0901 -0.0452 929  ILE B C   
15486 O O   . ILE B 931  ? 0.3938 0.4040 0.4780 0.0185  -0.0848 -0.0457 929  ILE B O   
15487 C CB  . ILE B 931  ? 0.3838 0.4107 0.4955 0.0257  -0.0852 -0.0464 929  ILE B CB  
15488 C CG1 . ILE B 931  ? 0.4035 0.4349 0.5232 0.0308  -0.0839 -0.0473 929  ILE B CG1 
15489 C CG2 . ILE B 931  ? 0.3720 0.4054 0.4935 0.0238  -0.0897 -0.0456 929  ILE B CG2 
15490 C CD1 . ILE B 931  ? 0.3743 0.4187 0.5078 0.0319  -0.0792 -0.0481 929  ILE B CD1 
15491 N N   . GLU B 932  ? 0.4735 0.4794 0.5591 0.0197  -0.0972 -0.0445 930  GLU B N   
15492 C CA  . GLU B 932  ? 0.4732 0.4739 0.5497 0.0162  -0.0988 -0.0446 930  GLU B CA  
15493 C C   . GLU B 932  ? 0.4225 0.4302 0.5096 0.0138  -0.1005 -0.0449 930  GLU B C   
15494 O O   . GLU B 932  ? 0.4686 0.4817 0.5665 0.0145  -0.1053 -0.0444 930  GLU B O   
15495 C CB  . GLU B 932  ? 0.5118 0.5030 0.5770 0.0162  -0.1054 -0.0437 930  GLU B CB  
15496 C CG  . GLU B 932  ? 0.5535 0.5379 0.6084 0.0179  -0.1035 -0.0428 930  GLU B CG  
15497 C CD  . GLU B 932  ? 0.6672 0.6421 0.7096 0.0177  -0.1095 -0.0414 930  GLU B CD  
15498 O OE1 . GLU B 932  ? 0.7104 0.6816 0.7458 0.0156  -0.1127 -0.0417 930  GLU B OE1 
15499 O OE2 . GLU B 932  ? 0.6656 0.6364 0.7048 0.0197  -0.1111 -0.0399 930  GLU B OE2 
15500 N N   . LEU B 933  ? 0.4004 0.4081 0.4848 0.0110  -0.0965 -0.0455 931  LEU B N   
15501 C CA  . LEU B 933  ? 0.4383 0.4518 0.5320 0.0081  -0.0976 -0.0455 931  LEU B CA  
15502 C C   . LEU B 933  ? 0.4951 0.5001 0.5789 0.0051  -0.1022 -0.0462 931  LEU B C   
15503 O O   . LEU B 933  ? 0.5054 0.5011 0.5745 0.0054  -0.1021 -0.0469 931  LEU B O   
15504 C CB  . LEU B 933  ? 0.4462 0.4660 0.5450 0.0071  -0.0898 -0.0456 931  LEU B CB  
15505 C CG  . LEU B 933  ? 0.4070 0.4346 0.5135 0.0100  -0.0838 -0.0455 931  LEU B CG  
15506 C CD1 . LEU B 933  ? 0.3950 0.4279 0.5049 0.0083  -0.0769 -0.0454 931  LEU B CD1 
15507 C CD2 . LEU B 933  ? 0.4590 0.4956 0.5799 0.0120  -0.0869 -0.0448 931  LEU B CD2 
15508 N N   . GLU B 934  ? 0.5361 0.5445 0.6281 0.0022  -0.1062 -0.0461 932  GLU B N   
15509 C CA  . GLU B 934  ? 0.5205 0.5204 0.6035 -0.0007 -0.1107 -0.0471 932  GLU B CA  
15510 C C   . GLU B 934  ? 0.5830 0.5806 0.6615 -0.0026 -0.1051 -0.0479 932  GLU B C   
15511 O O   . GLU B 934  ? 0.6642 0.6523 0.7286 -0.0027 -0.1051 -0.0494 932  GLU B O   
15512 C CB  . GLU B 934  ? 0.5706 0.5741 0.6641 -0.0035 -0.1184 -0.0465 932  GLU B CB  
15513 N N   . LYS B 935  ? 0.5275 0.5340 0.6177 -0.0038 -0.1004 -0.0469 933  LYS B N   
15514 C CA  . LYS B 935  ? 0.5484 0.5536 0.6357 -0.0055 -0.0949 -0.0472 933  LYS B CA  
15515 C C   . LYS B 935  ? 0.5331 0.5469 0.6270 -0.0039 -0.0868 -0.0461 933  LYS B C   
15516 O O   . LYS B 935  ? 0.4664 0.4889 0.5706 -0.0023 -0.0859 -0.0451 933  LYS B O   
15517 C CB  . LYS B 935  ? 0.5057 0.5120 0.6003 -0.0099 -0.0984 -0.0466 933  LYS B CB  
15518 N N   . LEU B 936  ? 0.4847 0.4959 0.5722 -0.0041 -0.0811 -0.0465 934  LEU B N   
15519 C CA  . LEU B 936  ? 0.5177 0.5363 0.6100 -0.0028 -0.0735 -0.0456 934  LEU B CA  
15520 C C   . LEU B 936  ? 0.5534 0.5833 0.6616 -0.0046 -0.0723 -0.0438 934  LEU B C   
15521 O O   . LEU B 936  ? 0.5095 0.5479 0.6252 -0.0026 -0.0683 -0.0431 934  LEU B O   
15522 C CB  . LEU B 936  ? 0.5451 0.5588 0.6281 -0.0031 -0.0685 -0.0461 934  LEU B CB  
15523 C CG  . LEU B 936  ? 0.5036 0.5211 0.5852 -0.0011 -0.0611 -0.0458 934  LEU B CG  
15524 C CD1 . LEU B 936  ? 0.5535 0.5770 0.6409 0.0015  -0.0602 -0.0456 934  LEU B CD1 
15525 C CD2 . LEU B 936  ? 0.5080 0.5174 0.5753 0.0004  -0.0590 -0.0469 934  LEU B CD2 
15526 N N   . SER B 937  ? 0.5170 0.5470 0.6304 -0.0085 -0.0760 -0.0429 935  SER B N   
15527 C CA  . SER B 937  ? 0.5275 0.5690 0.6563 -0.0109 -0.0747 -0.0405 935  SER B CA  
15528 C C   . SER B 937  ? 0.5138 0.5648 0.6548 -0.0094 -0.0774 -0.0398 935  SER B C   
15529 O O   . SER B 937  ? 0.5195 0.5820 0.6743 -0.0109 -0.0757 -0.0377 935  SER B O   
15530 C CB  . SER B 937  ? 0.4855 0.5238 0.6167 -0.0160 -0.0789 -0.0394 935  SER B CB  
15531 O OG  . SER B 937  ? 0.5508 0.5820 0.6785 -0.0171 -0.0872 -0.0407 935  SER B OG  
15532 N N   . ASP B 938  ? 0.4817 0.5286 0.6181 -0.0064 -0.0813 -0.0412 936  ASP B N   
15533 C CA  . ASP B 938  ? 0.4999 0.5557 0.6473 -0.0038 -0.0831 -0.0407 936  ASP B CA  
15534 C C   . ASP B 938  ? 0.5432 0.6071 0.6952 -0.0001 -0.0757 -0.0407 936  ASP B C   
15535 O O   . ASP B 938  ? 0.4782 0.5523 0.6423 0.0020  -0.0756 -0.0401 936  ASP B O   
15536 C CB  . ASP B 938  ? 0.4946 0.5425 0.6345 -0.0014 -0.0893 -0.0421 936  ASP B CB  
15537 C CG  . ASP B 938  ? 0.5792 0.6198 0.7152 -0.0047 -0.0976 -0.0423 936  ASP B CG  
15538 O OD1 . ASP B 938  ? 0.5071 0.5516 0.6513 -0.0088 -0.0999 -0.0410 936  ASP B OD1 
15539 O OD2 . ASP B 938  ? 0.5710 0.6019 0.6954 -0.0033 -0.1018 -0.0436 936  ASP B OD2 
15540 N N   . LEU B 939  ? 0.4749 0.5344 0.6173 0.0009  -0.0697 -0.0416 937  LEU B N   
15541 C CA  . LEU B 939  ? 0.4919 0.5580 0.6371 0.0040  -0.0627 -0.0419 937  LEU B CA  
15542 C C   . LEU B 939  ? 0.4994 0.5741 0.6523 0.0013  -0.0576 -0.0401 937  LEU B C   
15543 O O   . LEU B 939  ? 0.5523 0.6224 0.6990 -0.0016 -0.0555 -0.0396 937  LEU B O   
15544 C CB  . LEU B 939  ? 0.4554 0.5124 0.5862 0.0060  -0.0594 -0.0435 937  LEU B CB  
15545 C CG  . LEU B 939  ? 0.4619 0.5228 0.5927 0.0096  -0.0533 -0.0444 937  LEU B CG  
15546 C CD1 . LEU B 939  ? 0.4252 0.4907 0.5634 0.0137  -0.0553 -0.0451 937  LEU B CD1 
15547 C CD2 . LEU B 939  ? 0.4404 0.4918 0.5569 0.0104  -0.0509 -0.0456 937  LEU B CD2 
15548 N N   . GLN B 940  ? 0.4661 0.5537 0.6329 0.0022  -0.0556 -0.0389 938  GLN B N   
15549 C CA  . GLN B 940  ? 0.4858 0.5832 0.6619 -0.0010 -0.0516 -0.0364 938  GLN B CA  
15550 C C   . GLN B 940  ? 0.5577 0.6638 0.7368 0.0018  -0.0435 -0.0365 938  GLN B C   
15551 O O   . GLN B 940  ? 0.5403 0.6571 0.7289 -0.0002 -0.0398 -0.0341 938  GLN B O   
15552 C CB  . GLN B 940  ? 0.5498 0.6567 0.7409 -0.0034 -0.0561 -0.0342 938  GLN B CB  
15553 N N   . ARG B 941  ? 0.4782 0.5801 0.6493 0.0064  -0.0408 -0.0390 939  ARG B N   
15554 C CA  . ARG B 941  ? 0.4900 0.5982 0.6614 0.0092  -0.0334 -0.0397 939  ARG B CA  
15555 C C   . ARG B 941  ? 0.4373 0.5359 0.5962 0.0129  -0.0324 -0.0426 939  ARG B C   
15556 O O   . ARG B 941  ? 0.3926 0.4824 0.5456 0.0140  -0.0373 -0.0439 939  ARG B O   
15557 C CB  . ARG B 941  ? 0.4883 0.6106 0.6736 0.0123  -0.0312 -0.0394 939  ARG B CB  
15558 C CG  . ARG B 941  ? 0.4653 0.5873 0.6539 0.0172  -0.0354 -0.0415 939  ARG B CG  
15559 C CD  . ARG B 941  ? 0.4656 0.6022 0.6675 0.0212  -0.0320 -0.0416 939  ARG B CD  
15560 N NE  . ARG B 941  ? 0.4506 0.5867 0.6554 0.0269  -0.0355 -0.0439 939  ARG B NE  
15561 C CZ  . ARG B 941  ? 0.4267 0.5605 0.6268 0.0326  -0.0327 -0.0469 939  ARG B CZ  
15562 N NH1 . ARG B 941  ? 0.4821 0.6137 0.6740 0.0333  -0.0266 -0.0482 939  ARG B NH1 
15563 N NH2 . ARG B 941  ? 0.3591 0.4923 0.5629 0.0378  -0.0365 -0.0487 939  ARG B NH2 
15564 N N   . GLU B 942  ? 0.4138 0.5142 0.5687 0.0144  -0.0261 -0.0434 940  GLU B N   
15565 C CA  . GLU B 942  ? 0.4408 0.5330 0.5849 0.0176  -0.0251 -0.0460 940  GLU B CA  
15566 C C   . GLU B 942  ? 0.3815 0.4757 0.5297 0.0229  -0.0264 -0.0482 940  GLU B C   
15567 O O   . GLU B 942  ? 0.4240 0.5289 0.5822 0.0255  -0.0239 -0.0484 940  GLU B O   
15568 C CB  . GLU B 942  ? 0.4992 0.5928 0.6378 0.0175  -0.0185 -0.0462 940  GLU B CB  
15569 C CG  . GLU B 942  ? 0.4813 0.5639 0.6063 0.0179  -0.0183 -0.0477 940  GLU B CG  
15570 C CD  . GLU B 942  ? 0.5256 0.6103 0.6459 0.0185  -0.0122 -0.0483 940  GLU B CD  
15571 O OE1 . GLU B 942  ? 0.5669 0.6610 0.6936 0.0202  -0.0081 -0.0484 940  GLU B OE1 
15572 O OE2 . GLU B 942  ? 0.4929 0.5702 0.6030 0.0175  -0.0116 -0.0486 940  GLU B OE2 
15573 N N   . VAL B 943  ? 0.3555 0.4396 0.4961 0.0246  -0.0305 -0.0497 941  VAL B N   
15574 C CA  . VAL B 943  ? 0.3331 0.4163 0.4756 0.0297  -0.0324 -0.0518 941  VAL B CA  
15575 C C   . VAL B 943  ? 0.3296 0.4046 0.4608 0.0316  -0.0301 -0.0539 941  VAL B C   
15576 O O   . VAL B 943  ? 0.3079 0.3724 0.4287 0.0299  -0.0326 -0.0537 941  VAL B O   
15577 C CB  . VAL B 943  ? 0.3520 0.4300 0.4954 0.0300  -0.0399 -0.0514 941  VAL B CB  
15578 C CG1 . VAL B 943  ? 0.3245 0.4013 0.4703 0.0358  -0.0421 -0.0534 941  VAL B CG1 
15579 C CG2 . VAL B 943  ? 0.3686 0.4547 0.5232 0.0275  -0.0425 -0.0492 941  VAL B CG2 
15580 N N   . PHE B 944  ? 0.2632 0.3433 0.3963 0.0350  -0.0254 -0.0558 942  PHE B N   
15581 C CA  . PHE B 944  ? 0.3009 0.3745 0.4236 0.0358  -0.0224 -0.0576 942  PHE B CA  
15582 C C   . PHE B 944  ? 0.3230 0.3887 0.4419 0.0401  -0.0257 -0.0601 942  PHE B C   
15583 O O   . PHE B 944  ? 0.2916 0.3590 0.4117 0.0446  -0.0235 -0.0627 942  PHE B O   
15584 C CB  . PHE B 944  ? 0.2966 0.3790 0.4218 0.0369  -0.0157 -0.0584 942  PHE B CB  
15585 C CG  . PHE B 944  ? 0.3629 0.4397 0.4771 0.0351  -0.0125 -0.0590 942  PHE B CG  
15586 C CD1 . PHE B 944  ? 0.3327 0.4077 0.4421 0.0301  -0.0116 -0.0566 942  PHE B CD1 
15587 C CD2 . PHE B 944  ? 0.3433 0.4163 0.4518 0.0385  -0.0109 -0.0620 942  PHE B CD2 
15588 C CE1 . PHE B 944  ? 0.3631 0.4337 0.4630 0.0286  -0.0090 -0.0569 942  PHE B CE1 
15589 C CE2 . PHE B 944  ? 0.3166 0.3847 0.4151 0.0365  -0.0085 -0.0624 942  PHE B CE2 
15590 C CZ  . PHE B 944  ? 0.3043 0.3718 0.3990 0.0315  -0.0075 -0.0597 942  PHE B CZ  
15591 N N   . GLY B 945  ? 0.2768 0.3332 0.3906 0.0387  -0.0312 -0.0591 943  GLY B N   
15592 C CA  . GLY B 945  ? 0.2538 0.3019 0.3643 0.0422  -0.0353 -0.0606 943  GLY B CA  
15593 C C   . GLY B 945  ? 0.3294 0.3669 0.4315 0.0392  -0.0404 -0.0587 943  GLY B C   
15594 O O   . GLY B 945  ? 0.2987 0.3351 0.3967 0.0347  -0.0401 -0.0567 943  GLY B O   
15595 N N   . PRO B 946  ? 0.3247 0.3541 0.4239 0.0417  -0.0450 -0.0593 944  PRO B N   
15596 C CA  . PRO B 946  ? 0.2972 0.3157 0.3867 0.0388  -0.0494 -0.0573 944  PRO B CA  
15597 C C   . PRO B 946  ? 0.2862 0.3053 0.3790 0.0375  -0.0544 -0.0552 944  PRO B C   
15598 O O   . PRO B 946  ? 0.3305 0.3441 0.4227 0.0393  -0.0600 -0.0546 944  PRO B O   
15599 C CB  . PRO B 946  ? 0.2984 0.3081 0.3839 0.0422  -0.0523 -0.0587 944  PRO B CB  
15600 C CG  . PRO B 946  ? 0.3355 0.3520 0.4320 0.0481  -0.0522 -0.0611 944  PRO B CG  
15601 C CD  . PRO B 946  ? 0.3060 0.3351 0.4098 0.0477  -0.0461 -0.0619 944  PRO B CD  
15602 N N   . VAL B 947  ? 0.2719 0.2975 0.3680 0.0345  -0.0527 -0.0541 945  VAL B N   
15603 C CA  . VAL B 947  ? 0.2809 0.3086 0.3816 0.0332  -0.0572 -0.0525 945  VAL B CA  
15604 C C   . VAL B 947  ? 0.3519 0.3764 0.4449 0.0283  -0.0569 -0.0509 945  VAL B C   
15605 O O   . VAL B 947  ? 0.3087 0.3384 0.4033 0.0260  -0.0526 -0.0508 945  VAL B O   
15606 C CB  . VAL B 947  ? 0.3353 0.3752 0.4502 0.0347  -0.0562 -0.0529 945  VAL B CB  
15607 C CG1 . VAL B 947  ? 0.3380 0.3794 0.4574 0.0328  -0.0618 -0.0512 945  VAL B CG1 
15608 C CG2 . VAL B 947  ? 0.3225 0.3662 0.4452 0.0405  -0.0564 -0.0548 945  VAL B CG2 
15609 N N   . LEU B 948  ? 0.3473 0.3630 0.4317 0.0269  -0.0613 -0.0496 946  LEU B N   
15610 C CA  . LEU B 948  ? 0.3054 0.3172 0.3811 0.0229  -0.0611 -0.0484 946  LEU B CA  
15611 C C   . LEU B 948  ? 0.3207 0.3335 0.3996 0.0216  -0.0660 -0.0476 946  LEU B C   
15612 O O   . LEU B 948  ? 0.3558 0.3656 0.4355 0.0230  -0.0718 -0.0471 946  LEU B O   
15613 C CB  . LEU B 948  ? 0.3072 0.3091 0.3703 0.0220  -0.0624 -0.0473 946  LEU B CB  
15614 C CG  . LEU B 948  ? 0.3293 0.3273 0.3828 0.0186  -0.0620 -0.0461 946  LEU B CG  
15615 C CD1 . LEU B 948  ? 0.3006 0.3030 0.3539 0.0169  -0.0557 -0.0467 946  LEU B CD1 
15616 C CD2 . LEU B 948  ? 0.3294 0.3186 0.3713 0.0179  -0.0638 -0.0446 946  LEU B CD2 
15617 N N   . HIS B 949  ? 0.3239 0.3401 0.4041 0.0189  -0.0642 -0.0475 947  HIS B N   
15618 C CA  . HIS B 949  ? 0.3503 0.3662 0.4321 0.0169  -0.0690 -0.0469 947  HIS B CA  
15619 C C   . HIS B 949  ? 0.3434 0.3505 0.4116 0.0147  -0.0702 -0.0465 947  HIS B C   
15620 O O   . HIS B 949  ? 0.3267 0.3316 0.3876 0.0137  -0.0656 -0.0465 947  HIS B O   
15621 C CB  . HIS B 949  ? 0.3154 0.3398 0.4071 0.0151  -0.0666 -0.0470 947  HIS B CB  
15622 C CG  . HIS B 949  ? 0.3541 0.3886 0.4589 0.0174  -0.0644 -0.0473 947  HIS B CG  
15623 N ND1 . HIS B 949  ? 0.3239 0.3624 0.4301 0.0190  -0.0582 -0.0480 947  HIS B ND1 
15624 C CD2 . HIS B 949  ? 0.3655 0.4072 0.4826 0.0187  -0.0676 -0.0470 947  HIS B CD2 
15625 C CE1 . HIS B 949  ? 0.3130 0.3606 0.4312 0.0214  -0.0573 -0.0484 947  HIS B CE1 
15626 N NE2 . HIS B 949  ? 0.3754 0.4256 0.5009 0.0214  -0.0628 -0.0476 947  HIS B NE2 
15627 N N   . VAL B 950  ? 0.3756 0.3779 0.4402 0.0141  -0.0764 -0.0461 948  VAL B N   
15628 C CA  . VAL B 950  ? 0.3552 0.3490 0.4059 0.0126  -0.0778 -0.0458 948  VAL B CA  
15629 C C   . VAL B 950  ? 0.3414 0.3338 0.3920 0.0105  -0.0822 -0.0463 948  VAL B C   
15630 O O   . VAL B 950  ? 0.3652 0.3597 0.4232 0.0106  -0.0877 -0.0462 948  VAL B O   
15631 C CB  . VAL B 950  ? 0.3801 0.3668 0.4223 0.0139  -0.0815 -0.0447 948  VAL B CB  
15632 C CG1 . VAL B 950  ? 0.3763 0.3551 0.4040 0.0124  -0.0828 -0.0443 948  VAL B CG1 
15633 C CG2 . VAL B 950  ? 0.3856 0.3721 0.4268 0.0154  -0.0776 -0.0441 948  VAL B CG2 
15634 N N   . ILE B 951  ? 0.3132 0.3022 0.3559 0.0088  -0.0800 -0.0470 949  ILE B N   
15635 C CA  . ILE B 951  ? 0.3408 0.3259 0.3805 0.0070  -0.0845 -0.0479 949  ILE B CA  
15636 C C   . ILE B 951  ? 0.3579 0.3343 0.3815 0.0070  -0.0846 -0.0484 949  ILE B C   
15637 O O   . ILE B 951  ? 0.3347 0.3097 0.3510 0.0078  -0.0795 -0.0480 949  ILE B O   
15638 C CB  . ILE B 951  ? 0.4274 0.4169 0.4745 0.0049  -0.0822 -0.0485 949  ILE B CB  
15639 C CG1 . ILE B 951  ? 0.3701 0.3597 0.4124 0.0049  -0.0750 -0.0487 949  ILE B CG1 
15640 C CG2 . ILE B 951  ? 0.4566 0.4560 0.5202 0.0046  -0.0822 -0.0477 949  ILE B CG2 
15641 C CD1 . ILE B 951  ? 0.5002 0.4936 0.5495 0.0029  -0.0727 -0.0489 949  ILE B CD1 
15642 N N   . ARG B 952  ? 0.3188 0.2894 0.3366 0.0062  -0.0906 -0.0493 950  ARG B N   
15643 C CA  . ARG B 952  ? 0.3669 0.3290 0.3687 0.0065  -0.0914 -0.0502 950  ARG B CA  
15644 C C   . ARG B 952  ? 0.3649 0.3239 0.3638 0.0053  -0.0915 -0.0523 950  ARG B C   
15645 O O   . ARG B 952  ? 0.3878 0.3488 0.3957 0.0034  -0.0947 -0.0529 950  ARG B O   
15646 C CB  . ARG B 952  ? 0.3471 0.3037 0.3426 0.0069  -0.0988 -0.0498 950  ARG B CB  
15647 C CG  . ARG B 952  ? 0.4355 0.3950 0.4367 0.0082  -0.1003 -0.0476 950  ARG B CG  
15648 C CD  . ARG B 952  ? 0.5012 0.4576 0.5022 0.0083  -0.1090 -0.0471 950  ARG B CD  
15649 N NE  . ARG B 952  ? 0.5668 0.5146 0.5514 0.0087  -0.1119 -0.0468 950  ARG B NE  
15650 C CZ  . ARG B 952  ? 0.5040 0.4488 0.4823 0.0098  -0.1132 -0.0445 950  ARG B CZ  
15651 N NH1 . ARG B 952  ? 0.4704 0.4190 0.4570 0.0110  -0.1120 -0.0426 950  ARG B NH1 
15652 N NH2 . ARG B 952  ? 0.5151 0.4523 0.4777 0.0099  -0.1156 -0.0441 950  ARG B NH2 
15653 N N   . TYR B 953  ? 0.3557 0.3100 0.3424 0.0063  -0.0879 -0.0533 951  TYR B N   
15654 C CA  . TYR B 953  ? 0.3377 0.2878 0.3206 0.0057  -0.0880 -0.0557 951  TYR B CA  
15655 C C   . TYR B 953  ? 0.3606 0.3023 0.3263 0.0074  -0.0888 -0.0574 951  TYR B C   
15656 O O   . TYR B 953  ? 0.3400 0.2810 0.2970 0.0090  -0.0863 -0.0562 951  TYR B O   
15657 C CB  . TYR B 953  ? 0.3581 0.3130 0.3464 0.0057  -0.0809 -0.0554 951  TYR B CB  
15658 C CG  . TYR B 953  ? 0.3417 0.2971 0.3215 0.0077  -0.0742 -0.0549 951  TYR B CG  
15659 C CD1 . TYR B 953  ? 0.3239 0.2849 0.3071 0.0082  -0.0703 -0.0526 951  TYR B CD1 
15660 C CD2 . TYR B 953  ? 0.3341 0.2846 0.3030 0.0093  -0.0720 -0.0566 951  TYR B CD2 
15661 C CE1 . TYR B 953  ? 0.3391 0.3009 0.3152 0.0095  -0.0646 -0.0518 951  TYR B CE1 
15662 C CE2 . TYR B 953  ? 0.3397 0.2919 0.3019 0.0111  -0.0659 -0.0558 951  TYR B CE2 
15663 C CZ  . TYR B 953  ? 0.3321 0.2902 0.2982 0.0109  -0.0623 -0.0533 951  TYR B CZ  
15664 O OH  . TYR B 953  ? 0.3362 0.2964 0.2961 0.0122  -0.0566 -0.0522 951  TYR B OH  
15665 N N   . ARG B 954  ? 0.3973 0.3323 0.3578 0.0071  -0.0925 -0.0601 952  ARG B N   
15666 C CA  . ARG B 954  ? 0.4186 0.3454 0.3622 0.0093  -0.0928 -0.0624 952  ARG B CA  
15667 C C   . ARG B 954  ? 0.4395 0.3672 0.3798 0.0112  -0.0853 -0.0632 952  ARG B C   
15668 O O   . ARG B 954  ? 0.3896 0.3206 0.3394 0.0101  -0.0828 -0.0631 952  ARG B O   
15669 C CB  . ARG B 954  ? 0.4849 0.4030 0.4238 0.0083  -0.1006 -0.0654 952  ARG B CB  
15670 N N   . ARG B 955  ? 0.4410 0.3666 0.3680 0.0140  -0.0816 -0.0636 953  ARG B N   
15671 C CA  . ARG B 955  ? 0.4688 0.3969 0.3937 0.0161  -0.0742 -0.0639 953  ARG B CA  
15672 C C   . ARG B 955  ? 0.4873 0.4105 0.4127 0.0166  -0.0751 -0.0669 953  ARG B C   
15673 O O   . ARG B 955  ? 0.4507 0.3777 0.3818 0.0170  -0.0701 -0.0665 953  ARG B O   
15674 C CB  . ARG B 955  ? 0.4642 0.3909 0.3744 0.0191  -0.0705 -0.0640 953  ARG B CB  
15675 C CG  . ARG B 955  ? 0.5631 0.4930 0.4708 0.0218  -0.0630 -0.0644 953  ARG B CG  
15676 C CD  . ARG B 955  ? 0.5467 0.4854 0.4678 0.0203  -0.0580 -0.0617 953  ARG B CD  
15677 N NE  . ARG B 955  ? 0.6281 0.5705 0.5471 0.0228  -0.0512 -0.0617 953  ARG B NE  
15678 C CZ  . ARG B 955  ? 0.6568 0.5967 0.5764 0.0245  -0.0500 -0.0640 953  ARG B CZ  
15679 N NH1 . ARG B 955  ? 0.5934 0.5267 0.5155 0.0236  -0.0551 -0.0663 953  ARG B NH1 
15680 N NH2 . ARG B 955  ? 0.6005 0.5447 0.5187 0.0271  -0.0438 -0.0636 953  ARG B NH2 
15681 N N   . ASP B 956  ? 0.4691 0.3834 0.3888 0.0163  -0.0819 -0.0698 954  ASP B N   
15682 C CA  . ASP B 956  ? 0.5601 0.4679 0.4799 0.0164  -0.0838 -0.0728 954  ASP B CA  
15683 C C   . ASP B 956  ? 0.5354 0.4483 0.4718 0.0130  -0.0837 -0.0709 954  ASP B C   
15684 O O   . ASP B 956  ? 0.5335 0.4431 0.4716 0.0131  -0.0830 -0.0722 954  ASP B O   
15685 C CB  . ASP B 956  ? 0.5969 0.4940 0.5083 0.0159  -0.0923 -0.0761 954  ASP B CB  
15686 C CG  . ASP B 956  ? 0.6893 0.5797 0.5820 0.0201  -0.0920 -0.0789 954  ASP B CG  
15687 O OD1 . ASP B 956  ? 0.6876 0.5818 0.5747 0.0234  -0.0848 -0.0783 954  ASP B OD1 
15688 O OD2 . ASP B 956  ? 0.7431 0.6247 0.6268 0.0200  -0.0990 -0.0816 954  ASP B OD2 
15689 N N   . ASP B 957  ? 0.4770 0.3975 0.4252 0.0101  -0.0846 -0.0679 955  ASP B N   
15690 C CA  . ASP B 957  ? 0.4713 0.3974 0.4352 0.0067  -0.0847 -0.0660 955  ASP B CA  
15691 C C   . ASP B 957  ? 0.3907 0.3264 0.3623 0.0071  -0.0768 -0.0633 955  ASP B C   
15692 O O   . ASP B 957  ? 0.3990 0.3413 0.3839 0.0046  -0.0761 -0.0611 955  ASP B O   
15693 C CB  . ASP B 957  ? 0.4409 0.3701 0.4140 0.0036  -0.0907 -0.0645 955  ASP B CB  
15694 C CG  . ASP B 957  ? 0.5510 0.4711 0.5189 0.0022  -0.0994 -0.0670 955  ASP B CG  
15695 O OD1 . ASP B 957  ? 0.5617 0.4739 0.5249 0.0021  -0.1014 -0.0695 955  ASP B OD1 
15696 O OD2 . ASP B 957  ? 0.5742 0.4947 0.5428 0.0012  -0.1046 -0.0665 955  ASP B OD2 
15697 N N   . LEU B 958  ? 0.3812 0.3180 0.3447 0.0103  -0.0711 -0.0632 956  LEU B N   
15698 C CA  . LEU B 958  ? 0.3623 0.3079 0.3323 0.0106  -0.0641 -0.0607 956  LEU B CA  
15699 C C   . LEU B 958  ? 0.3548 0.3025 0.3337 0.0092  -0.0620 -0.0601 956  LEU B C   
15700 O O   . LEU B 958  ? 0.3410 0.2966 0.3310 0.0074  -0.0594 -0.0578 956  LEU B O   
15701 C CB  . LEU B 958  ? 0.3872 0.3330 0.3465 0.0141  -0.0587 -0.0610 956  LEU B CB  
15702 C CG  . LEU B 958  ? 0.3878 0.3423 0.3525 0.0144  -0.0518 -0.0585 956  LEU B CG  
15703 C CD1 . LEU B 958  ? 0.3548 0.3158 0.3279 0.0122  -0.0519 -0.0560 956  LEU B CD1 
15704 C CD2 . LEU B 958  ? 0.4517 0.4065 0.4057 0.0176  -0.0473 -0.0586 956  LEU B CD2 
15705 N N   . ASP B 959  ? 0.3865 0.3269 0.3605 0.0101  -0.0634 -0.0623 957  ASP B N   
15706 C CA  . ASP B 959  ? 0.3708 0.3126 0.3526 0.0087  -0.0615 -0.0613 957  ASP B CA  
15707 C C   . ASP B 959  ? 0.3668 0.3119 0.3616 0.0042  -0.0652 -0.0595 957  ASP B C   
15708 O O   . ASP B 959  ? 0.3816 0.3332 0.3862 0.0025  -0.0620 -0.0571 957  ASP B O   
15709 C CB  . ASP B 959  ? 0.4010 0.3329 0.3747 0.0108  -0.0630 -0.0640 957  ASP B CB  
15710 C CG  . ASP B 959  ? 0.3842 0.3177 0.3640 0.0103  -0.0596 -0.0625 957  ASP B CG  
15711 O OD1 . ASP B 959  ? 0.3802 0.3220 0.3641 0.0110  -0.0537 -0.0602 957  ASP B OD1 
15712 O OD2 . ASP B 959  ? 0.4151 0.3413 0.3954 0.0090  -0.0633 -0.0634 957  ASP B OD2 
15713 N N   . ARG B 960  ? 0.3953 0.3368 0.3905 0.0023  -0.0718 -0.0605 958  ARG B N   
15714 C CA  . ARG B 960  ? 0.3527 0.2991 0.3614 -0.0019 -0.0752 -0.0584 958  ARG B CA  
15715 C C   . ARG B 960  ? 0.3823 0.3400 0.4000 -0.0022 -0.0718 -0.0559 958  ARG B C   
15716 O O   . ARG B 960  ? 0.3776 0.3428 0.4080 -0.0049 -0.0710 -0.0535 958  ARG B O   
15717 C CB  . ARG B 960  ? 0.3756 0.3154 0.3826 -0.0039 -0.0837 -0.0601 958  ARG B CB  
15718 N N   . LEU B 961  ? 0.3143 0.2733 0.3256 0.0005  -0.0697 -0.0562 959  LEU B N   
15719 C CA  . LEU B 961  ? 0.3290 0.2974 0.3481 0.0005  -0.0666 -0.0540 959  LEU B CA  
15720 C C   . LEU B 961  ? 0.3535 0.3287 0.3779 0.0007  -0.0597 -0.0523 959  LEU B C   
15721 O O   . LEU B 961  ? 0.3418 0.3253 0.3769 -0.0005 -0.0577 -0.0504 959  LEU B O   
15722 C CB  . LEU B 961  ? 0.2981 0.2652 0.3084 0.0030  -0.0662 -0.0545 959  LEU B CB  
15723 C CG  . LEU B 961  ? 0.3380 0.3129 0.3541 0.0036  -0.0629 -0.0525 959  LEU B CG  
15724 C CD1 . LEU B 961  ? 0.4108 0.3905 0.4382 0.0019  -0.0669 -0.0516 959  LEU B CD1 
15725 C CD2 . LEU B 961  ? 0.3392 0.3117 0.3449 0.0058  -0.0618 -0.0525 959  LEU B CD2 
15726 N N   . VAL B 962  ? 0.3087 0.2807 0.3259 0.0024  -0.0559 -0.0529 960  VAL B N   
15727 C CA  . VAL B 962  ? 0.3182 0.2961 0.3400 0.0025  -0.0500 -0.0512 960  VAL B CA  
15728 C C   . VAL B 962  ? 0.3637 0.3445 0.3962 -0.0007 -0.0508 -0.0497 960  VAL B C   
15729 O O   . VAL B 962  ? 0.3170 0.3059 0.3579 -0.0017 -0.0472 -0.0476 960  VAL B O   
15730 C CB  . VAL B 962  ? 0.3636 0.3373 0.3757 0.0052  -0.0465 -0.0522 960  VAL B CB  
15731 C CG1 . VAL B 962  ? 0.3221 0.3008 0.3392 0.0049  -0.0415 -0.0504 960  VAL B CG1 
15732 C CG2 . VAL B 962  ? 0.2942 0.2683 0.2978 0.0078  -0.0443 -0.0527 960  VAL B CG2 
15733 N N   . ASP B 963  ? 0.3614 0.3355 0.3935 -0.0025 -0.0558 -0.0506 961  ASP B N   
15734 C CA  . ASP B 963  ? 0.4136 0.3906 0.4566 -0.0063 -0.0575 -0.0486 961  ASP B CA  
15735 C C   . ASP B 963  ? 0.3652 0.3520 0.4200 -0.0082 -0.0579 -0.0468 961  ASP B C   
15736 O O   . ASP B 963  ? 0.3948 0.3895 0.4593 -0.0101 -0.0548 -0.0443 961  ASP B O   
15737 C CB  . ASP B 963  ? 0.4144 0.3820 0.4552 -0.0085 -0.0644 -0.0500 961  ASP B CB  
15738 C CG  . ASP B 963  ? 0.4548 0.4131 0.4867 -0.0070 -0.0641 -0.0514 961  ASP B CG  
15739 O OD1 . ASP B 963  ? 0.4876 0.4485 0.5187 -0.0054 -0.0585 -0.0503 961  ASP B OD1 
15740 O OD2 . ASP B 963  ? 0.5089 0.4570 0.5345 -0.0073 -0.0698 -0.0538 961  ASP B OD2 
15741 N N   . ASP B 964  ? 0.3464 0.3327 0.4001 -0.0075 -0.0616 -0.0480 962  ASP B N   
15742 C CA  . ASP B 964  ? 0.3633 0.3585 0.4282 -0.0086 -0.0626 -0.0466 962  ASP B CA  
15743 C C   . ASP B 964  ? 0.3774 0.3814 0.4463 -0.0068 -0.0560 -0.0453 962  ASP B C   
15744 O O   . ASP B 964  ? 0.3235 0.3367 0.4037 -0.0080 -0.0544 -0.0435 962  ASP B O   
15745 C CB  . ASP B 964  ? 0.3836 0.3754 0.4447 -0.0074 -0.0680 -0.0481 962  ASP B CB  
15746 C CG  . ASP B 964  ? 0.4435 0.4279 0.5029 -0.0098 -0.0755 -0.0493 962  ASP B CG  
15747 O OD1 . ASP B 964  ? 0.4535 0.4351 0.5151 -0.0125 -0.0767 -0.0488 962  ASP B OD1 
15748 O OD2 . ASP B 964  ? 0.4875 0.4685 0.5431 -0.0091 -0.0806 -0.0505 962  ASP B OD2 
15749 N N   . VAL B 965  ? 0.3263 0.3281 0.3861 -0.0039 -0.0522 -0.0462 963  VAL B N   
15750 C CA  . VAL B 965  ? 0.3052 0.3144 0.3680 -0.0024 -0.0463 -0.0453 963  VAL B CA  
15751 C C   . VAL B 965  ? 0.3149 0.3290 0.3832 -0.0039 -0.0420 -0.0434 963  VAL B C   
15752 O O   . VAL B 965  ? 0.3529 0.3755 0.4293 -0.0042 -0.0389 -0.0421 963  VAL B O   
15753 C CB  . VAL B 965  ? 0.3470 0.3525 0.3989 0.0004  -0.0437 -0.0463 963  VAL B CB  
15754 C CG1 . VAL B 965  ? 0.2853 0.2975 0.3396 0.0015  -0.0379 -0.0454 963  VAL B CG1 
15755 C CG2 . VAL B 965  ? 0.3161 0.3179 0.3633 0.0017  -0.0477 -0.0475 963  VAL B CG2 
15756 N N   . ASN B 966  ? 0.3177 0.3263 0.3813 -0.0048 -0.0418 -0.0433 964  ASN B N   
15757 C CA  . ASN B 966  ? 0.3503 0.3628 0.4187 -0.0064 -0.0382 -0.0411 964  ASN B CA  
15758 C C   . ASN B 966  ? 0.3929 0.4114 0.4733 -0.0099 -0.0398 -0.0390 964  ASN B C   
15759 O O   . ASN B 966  ? 0.3767 0.4022 0.4634 -0.0112 -0.0359 -0.0367 964  ASN B O   
15760 C CB  . ASN B 966  ? 0.3710 0.3750 0.4320 -0.0065 -0.0388 -0.0414 964  ASN B CB  
15761 C CG  . ASN B 966  ? 0.3687 0.3695 0.4194 -0.0030 -0.0355 -0.0428 964  ASN B CG  
15762 O OD1 . ASN B 966  ? 0.3379 0.3440 0.3881 -0.0014 -0.0316 -0.0426 964  ASN B OD1 
15763 N ND2 . ASN B 966  ? 0.3241 0.3163 0.3667 -0.0019 -0.0372 -0.0441 964  ASN B ND2 
15764 N N   . ALA B 967  ? 0.3380 0.3543 0.4217 -0.0116 -0.0457 -0.0395 965  ALA B N   
15765 C CA  . ALA B 967  ? 0.3535 0.3752 0.4490 -0.0155 -0.0480 -0.0372 965  ALA B CA  
15766 C C   . ALA B 967  ? 0.3594 0.3940 0.4660 -0.0154 -0.0445 -0.0355 965  ALA B C   
15767 O O   . ALA B 967  ? 0.3846 0.4260 0.5017 -0.0187 -0.0445 -0.0328 965  ALA B O   
15768 C CB  . ALA B 967  ? 0.3674 0.3838 0.4637 -0.0172 -0.0556 -0.0384 965  ALA B CB  
15769 N N   . THR B 968  ? 0.3504 0.3883 0.4549 -0.0117 -0.0417 -0.0370 966  THR B N   
15770 C CA  . THR B 968  ? 0.3703 0.4200 0.4846 -0.0109 -0.0382 -0.0359 966  THR B CA  
15771 C C   . THR B 968  ? 0.3811 0.4373 0.4985 -0.0118 -0.0320 -0.0336 966  THR B C   
15772 O O   . THR B 968  ? 0.3817 0.4485 0.5082 -0.0118 -0.0290 -0.0323 966  THR B O   
15773 C CB  . THR B 968  ? 0.3795 0.4296 0.4897 -0.0066 -0.0368 -0.0382 966  THR B CB  
15774 O OG1 . THR B 968  ? 0.3664 0.4141 0.4681 -0.0049 -0.0319 -0.0387 966  THR B OG1 
15775 C CG2 . THR B 968  ? 0.4097 0.4516 0.5138 -0.0055 -0.0425 -0.0402 966  THR B CG2 
15776 N N   . GLY B 969  ? 0.3772 0.4275 0.4868 -0.0123 -0.0300 -0.0332 967  GLY B N   
15777 C CA  . GLY B 969  ? 0.3559 0.4116 0.4668 -0.0130 -0.0243 -0.0310 967  GLY B CA  
15778 C C   . GLY B 969  ? 0.3787 0.4370 0.4844 -0.0094 -0.0193 -0.0323 967  GLY B C   
15779 O O   . GLY B 969  ? 0.3721 0.4329 0.4761 -0.0097 -0.0149 -0.0308 967  GLY B O   
15780 N N   . TYR B 970  ? 0.3274 0.3847 0.4303 -0.0063 -0.0201 -0.0350 968  TYR B N   
15781 C CA  . TYR B 970  ? 0.3250 0.3830 0.4220 -0.0033 -0.0162 -0.0364 968  TYR B CA  
15782 C C   . TYR B 970  ? 0.3462 0.3953 0.4321 -0.0025 -0.0166 -0.0374 968  TYR B C   
15783 O O   . TYR B 970  ? 0.3621 0.4040 0.4441 -0.0033 -0.0202 -0.0378 968  TYR B O   
15784 C CB  . TYR B 970  ? 0.3162 0.3762 0.4150 -0.0005 -0.0172 -0.0386 968  TYR B CB  
15785 C CG  . TYR B 970  ? 0.4360 0.5058 0.5460 -0.0001 -0.0163 -0.0380 968  TYR B CG  
15786 C CD1 . TYR B 970  ? 0.4264 0.5042 0.5394 0.0012  -0.0110 -0.0377 968  TYR B CD1 
15787 C CD2 . TYR B 970  ? 0.3945 0.4660 0.5119 -0.0008 -0.0207 -0.0379 968  TYR B CD2 
15788 C CE1 . TYR B 970  ? 0.4076 0.4954 0.5310 0.0020  -0.0097 -0.0373 968  TYR B CE1 
15789 C CE2 . TYR B 970  ? 0.4775 0.5593 0.6061 -0.0002 -0.0198 -0.0373 968  TYR B CE2 
15790 C CZ  . TYR B 970  ? 0.4917 0.5818 0.6232 0.0014  -0.0140 -0.0370 968  TYR B CZ  
15791 O OH  . TYR B 970  ? 0.5598 0.6608 0.7025 0.0025  -0.0126 -0.0365 968  TYR B OH  
15792 N N   . GLY B 971  ? 0.3214 0.3712 0.4020 -0.0007 -0.0129 -0.0379 969  GLY B N   
15793 C CA  . GLY B 971  ? 0.3049 0.3479 0.3758 0.0002  -0.0129 -0.0387 969  GLY B CA  
15794 C C   . GLY B 971  ? 0.2875 0.3324 0.3542 0.0021  -0.0097 -0.0395 969  GLY B C   
15795 O O   . GLY B 971  ? 0.3188 0.3640 0.3815 0.0021  -0.0068 -0.0386 969  GLY B O   
15796 N N   . LEU B 972  ? 0.2936 0.3393 0.3609 0.0037  -0.0104 -0.0412 970  LEU B N   
15797 C CA  . LEU B 972  ? 0.2822 0.3292 0.3457 0.0052  -0.0078 -0.0421 970  LEU B CA  
15798 C C   . LEU B 972  ? 0.2723 0.3132 0.3277 0.0058  -0.0093 -0.0429 970  LEU B C   
15799 O O   . LEU B 972  ? 0.2832 0.3224 0.3333 0.0055  -0.0079 -0.0421 970  LEU B O   
15800 C CB  . LEU B 972  ? 0.2875 0.3388 0.3561 0.0068  -0.0074 -0.0434 970  LEU B CB  
15801 C CG  . LEU B 972  ? 0.2754 0.3278 0.3402 0.0082  -0.0047 -0.0446 970  LEU B CG  
15802 C CD1 . LEU B 972  ? 0.3276 0.3828 0.3897 0.0072  -0.0009 -0.0432 970  LEU B CD1 
15803 C CD2 . LEU B 972  ? 0.2840 0.3408 0.3542 0.0103  -0.0040 -0.0462 970  LEU B CD2 
15804 N N   . THR B 973  ? 0.2235 0.2613 0.2779 0.0068  -0.0122 -0.0441 971  THR B N   
15805 C CA  . THR B 973  ? 0.2261 0.2584 0.2728 0.0070  -0.0136 -0.0443 971  THR B CA  
15806 C C   . THR B 973  ? 0.2395 0.2668 0.2843 0.0068  -0.0175 -0.0444 971  THR B C   
15807 O O   . THR B 973  ? 0.2238 0.2516 0.2739 0.0066  -0.0200 -0.0447 971  THR B O   
15808 C CB  . THR B 973  ? 0.2602 0.2913 0.3051 0.0080  -0.0142 -0.0452 971  THR B CB  
15809 O OG1 . THR B 973  ? 0.2486 0.2798 0.2987 0.0091  -0.0169 -0.0462 971  THR B OG1 
15810 C CG2 . THR B 973  ? 0.2668 0.3016 0.3117 0.0082  -0.0107 -0.0455 971  THR B CG2 
15811 N N   . PHE B 974  ? 0.2435 0.2665 0.2806 0.0068  -0.0179 -0.0441 972  PHE B N   
15812 C CA  . PHE B 974  ? 0.2573 0.2751 0.2904 0.0069  -0.0214 -0.0444 972  PHE B CA  
15813 C C   . PHE B 974  ? 0.2392 0.2537 0.2639 0.0073  -0.0213 -0.0440 972  PHE B C   
15814 O O   . PHE B 974  ? 0.2265 0.2426 0.2479 0.0073  -0.0182 -0.0433 972  PHE B O   
15815 C CB  . PHE B 974  ? 0.2122 0.2284 0.2446 0.0066  -0.0213 -0.0443 972  PHE B CB  
15816 C CG  . PHE B 974  ? 0.2502 0.2602 0.2764 0.0070  -0.0246 -0.0451 972  PHE B CG  
15817 C CD1 . PHE B 974  ? 0.2819 0.2892 0.3105 0.0066  -0.0292 -0.0458 972  PHE B CD1 
15818 C CD2 . PHE B 974  ? 0.2639 0.2711 0.2817 0.0080  -0.0233 -0.0450 972  PHE B CD2 
15819 C CE1 . PHE B 974  ? 0.3148 0.3158 0.3366 0.0070  -0.0326 -0.0468 972  PHE B CE1 
15820 C CE2 . PHE B 974  ? 0.2688 0.2702 0.2799 0.0088  -0.0262 -0.0460 972  PHE B CE2 
15821 C CZ  . PHE B 974  ? 0.2811 0.2789 0.2936 0.0083  -0.0309 -0.0470 972  PHE B CZ  
15822 N N   . GLY B 975  ? 0.2375 0.2476 0.2588 0.0076  -0.0249 -0.0443 973  GLY B N   
15823 C CA  . GLY B 975  ? 0.2793 0.2864 0.2924 0.0076  -0.0249 -0.0434 973  GLY B CA  
15824 C C   . GLY B 975  ? 0.2695 0.2718 0.2759 0.0082  -0.0272 -0.0438 973  GLY B C   
15825 O O   . GLY B 975  ? 0.2658 0.2656 0.2739 0.0083  -0.0305 -0.0449 973  GLY B O   
15826 N N   . LEU B 976  ? 0.2485 0.2500 0.2471 0.0085  -0.0253 -0.0429 974  LEU B N   
15827 C CA  . LEU B 976  ? 0.2773 0.2743 0.2678 0.0095  -0.0270 -0.0434 974  LEU B CA  
15828 C C   . LEU B 976  ? 0.2841 0.2804 0.2671 0.0091  -0.0263 -0.0416 974  LEU B C   
15829 O O   . LEU B 976  ? 0.2798 0.2800 0.2621 0.0085  -0.0227 -0.0400 974  LEU B O   
15830 C CB  . LEU B 976  ? 0.2911 0.2885 0.2791 0.0109  -0.0245 -0.0443 974  LEU B CB  
15831 C CG  . LEU B 976  ? 0.2969 0.2896 0.2752 0.0126  -0.0256 -0.0453 974  LEU B CG  
15832 C CD1 . LEU B 976  ? 0.2714 0.2579 0.2485 0.0126  -0.0311 -0.0470 974  LEU B CD1 
15833 C CD2 . LEU B 976  ? 0.2997 0.2931 0.2761 0.0146  -0.0226 -0.0462 974  LEU B CD2 
15834 N N   . HIS B 977  ? 0.2964 0.2878 0.2739 0.0092  -0.0300 -0.0415 975  HIS B N   
15835 C CA  . HIS B 977  ? 0.2807 0.2711 0.2503 0.0086  -0.0296 -0.0393 975  HIS B CA  
15836 C C   . HIS B 977  ? 0.2818 0.2689 0.2418 0.0103  -0.0301 -0.0401 975  HIS B C   
15837 O O   . HIS B 977  ? 0.2994 0.2813 0.2567 0.0109  -0.0344 -0.0416 975  HIS B O   
15838 C CB  . HIS B 977  ? 0.2932 0.2803 0.2634 0.0073  -0.0336 -0.0380 975  HIS B CB  
15839 C CG  . HIS B 977  ? 0.3260 0.3158 0.3014 0.0057  -0.0322 -0.0365 975  HIS B CG  
15840 N ND1 . HIS B 977  ? 0.3745 0.3640 0.3454 0.0040  -0.0314 -0.0336 975  HIS B ND1 
15841 C CD2 . HIS B 977  ? 0.3502 0.3429 0.3344 0.0056  -0.0312 -0.0374 975  HIS B CD2 
15842 C CE1 . HIS B 977  ? 0.3601 0.3514 0.3368 0.0028  -0.0306 -0.0332 975  HIS B CE1 
15843 N NE2 . HIS B 977  ? 0.3449 0.3382 0.3294 0.0040  -0.0304 -0.0356 975  HIS B NE2 
15844 N N   . THR B 978  ? 0.2710 0.2614 0.2259 0.0111  -0.0257 -0.0393 976  THR B N   
15845 C CA  . THR B 978  ? 0.3222 0.3101 0.2670 0.0134  -0.0252 -0.0403 976  THR B CA  
15846 C C   . THR B 978  ? 0.3432 0.3372 0.2840 0.0138  -0.0198 -0.0381 976  THR B C   
15847 O O   . THR B 978  ? 0.3277 0.3276 0.2745 0.0129  -0.0164 -0.0368 976  THR B O   
15848 C CB  . THR B 978  ? 0.3354 0.3205 0.2807 0.0158  -0.0260 -0.0438 976  THR B CB  
15849 O OG1 . THR B 978  ? 0.3428 0.3250 0.2773 0.0185  -0.0254 -0.0451 976  THR B OG1 
15850 C CG2 . THR B 978  ? 0.3401 0.3304 0.2924 0.0163  -0.0221 -0.0440 976  THR B CG2 
15851 N N   . ARG B 979  ? 0.3457 0.3386 0.2762 0.0151  -0.0191 -0.0375 977  ARG B N   
15852 C CA  . ARG B 979  ? 0.3586 0.3582 0.2851 0.0160  -0.0136 -0.0356 977  ARG B CA  
15853 C C   . ARG B 979  ? 0.3580 0.3584 0.2814 0.0203  -0.0109 -0.0385 977  ARG B C   
15854 O O   . ARG B 979  ? 0.3494 0.3562 0.2703 0.0218  -0.0061 -0.0373 977  ARG B O   
15855 C CB  . ARG B 979  ? 0.3788 0.3782 0.2956 0.0151  -0.0134 -0.0328 977  ARG B CB  
15856 C CG  . ARG B 979  ? 0.4643 0.4648 0.3840 0.0107  -0.0145 -0.0286 977  ARG B CG  
15857 C CD  . ARG B 979  ? 0.5137 0.5109 0.4232 0.0097  -0.0163 -0.0261 977  ARG B CD  
15858 N NE  . ARG B 979  ? 0.5631 0.5606 0.4750 0.0054  -0.0175 -0.0218 977  ARG B NE  
15859 C CZ  . ARG B 979  ? 0.5910 0.5875 0.4951 0.0033  -0.0181 -0.0180 977  ARG B CZ  
15860 N NH1 . ARG B 979  ? 0.5356 0.5317 0.4286 0.0052  -0.0169 -0.0178 977  ARG B NH1 
15861 N NH2 . ARG B 979  ? 0.6393 0.6346 0.5464 -0.0008 -0.0200 -0.0143 977  ARG B NH2 
15862 N N   . LEU B 980  ? 0.3363 0.3304 0.2601 0.0222  -0.0140 -0.0423 978  LEU B N   
15863 C CA  . LEU B 980  ? 0.3321 0.3240 0.2504 0.0267  -0.0126 -0.0456 978  LEU B CA  
15864 C C   . LEU B 980  ? 0.3261 0.3203 0.2526 0.0279  -0.0108 -0.0469 978  LEU B C   
15865 O O   . LEU B 980  ? 0.3265 0.3176 0.2603 0.0263  -0.0138 -0.0479 978  LEU B O   
15866 C CB  . LEU B 980  ? 0.3280 0.3099 0.2399 0.0279  -0.0180 -0.0490 978  LEU B CB  
15867 C CG  . LEU B 980  ? 0.4024 0.3810 0.3056 0.0266  -0.0207 -0.0477 978  LEU B CG  
15868 C CD1 . LEU B 980  ? 0.3737 0.3422 0.2707 0.0278  -0.0268 -0.0513 978  LEU B CD1 
15869 C CD2 . LEU B 980  ? 0.3753 0.3588 0.2691 0.0285  -0.0159 -0.0459 978  LEU B CD2 
15870 N N   . ASP B 981  ? 0.3250 0.3249 0.2501 0.0309  -0.0059 -0.0467 979  ASP B N   
15871 C CA  . ASP B 981  ? 0.3408 0.3432 0.2733 0.0323  -0.0040 -0.0474 979  ASP B CA  
15872 C C   . ASP B 981  ? 0.3310 0.3246 0.2637 0.0340  -0.0078 -0.0512 979  ASP B C   
15873 O O   . ASP B 981  ? 0.3172 0.3109 0.2580 0.0331  -0.0082 -0.0512 979  ASP B O   
15874 C CB  . ASP B 981  ? 0.3268 0.3363 0.2568 0.0361  0.0014  -0.0468 979  ASP B CB  
15875 C CG  . ASP B 981  ? 0.3653 0.3854 0.2992 0.0336  0.0053  -0.0425 979  ASP B CG  
15876 O OD1 . ASP B 981  ? 0.3866 0.4081 0.3269 0.0290  0.0038  -0.0402 979  ASP B OD1 
15877 O OD2 . ASP B 981  ? 0.3898 0.4168 0.3206 0.0363  0.0097  -0.0414 979  ASP B OD2 
15878 N N   . GLU B 982  ? 0.3151 0.3008 0.2385 0.0365  -0.0105 -0.0542 980  GLU B N   
15879 C CA  . GLU B 982  ? 0.3622 0.3386 0.2856 0.0377  -0.0146 -0.0578 980  GLU B CA  
15880 C C   . GLU B 982  ? 0.3511 0.3245 0.2825 0.0331  -0.0193 -0.0572 980  GLU B C   
15881 O O   . GLU B 982  ? 0.3322 0.3026 0.2699 0.0323  -0.0213 -0.0581 980  GLU B O   
15882 C CB  . GLU B 982  ? 0.3622 0.3301 0.2730 0.0411  -0.0171 -0.0614 980  GLU B CB  
15883 C CG  . GLU B 982  ? 0.3969 0.3539 0.3076 0.0413  -0.0227 -0.0650 980  GLU B CG  
15884 C CD  . GLU B 982  ? 0.5128 0.4601 0.4108 0.0438  -0.0267 -0.0688 980  GLU B CD  
15885 O OE1 . GLU B 982  ? 0.5302 0.4776 0.4222 0.0426  -0.0279 -0.0681 980  GLU B OE1 
15886 O OE2 . GLU B 982  ? 0.4776 0.4166 0.3711 0.0469  -0.0288 -0.0725 980  GLU B OE2 
15887 N N   . THR B 983  ? 0.3478 0.3225 0.2794 0.0300  -0.0210 -0.0554 981  THR B N   
15888 C CA  . THR B 983  ? 0.3242 0.2974 0.2641 0.0261  -0.0250 -0.0548 981  THR B CA  
15889 C C   . THR B 983  ? 0.3272 0.3074 0.2783 0.0239  -0.0223 -0.0524 981  THR B C   
15890 O O   . THR B 983  ? 0.3176 0.2968 0.2767 0.0219  -0.0245 -0.0526 981  THR B O   
15891 C CB  . THR B 983  ? 0.3536 0.3259 0.2903 0.0240  -0.0278 -0.0535 981  THR B CB  
15892 O OG1 . THR B 983  ? 0.4121 0.3772 0.3378 0.0260  -0.0309 -0.0559 981  THR B OG1 
15893 C CG2 . THR B 983  ? 0.3341 0.3061 0.2805 0.0205  -0.0316 -0.0528 981  THR B CG2 
15894 N N   . ILE B 984  ? 0.2611 0.2488 0.2128 0.0242  -0.0174 -0.0501 982  ILE B N   
15895 C CA  . ILE B 984  ? 0.3004 0.2945 0.2618 0.0224  -0.0149 -0.0481 982  ILE B CA  
15896 C C   . ILE B 984  ? 0.3148 0.3075 0.2797 0.0240  -0.0143 -0.0494 982  ILE B C   
15897 O O   . ILE B 984  ? 0.3255 0.3190 0.2985 0.0220  -0.0151 -0.0489 982  ILE B O   
15898 C CB  . ILE B 984  ? 0.3032 0.3053 0.2641 0.0223  -0.0102 -0.0454 982  ILE B CB  
15899 C CG1 . ILE B 984  ? 0.3576 0.3605 0.3162 0.0198  -0.0113 -0.0435 982  ILE B CG1 
15900 C CG2 . ILE B 984  ? 0.3080 0.3163 0.2776 0.0210  -0.0077 -0.0437 982  ILE B CG2 
15901 C CD1 . ILE B 984  ? 0.3465 0.3572 0.3053 0.0187  -0.0073 -0.0404 982  ILE B CD1 
15902 N N   . ALA B 985  ? 0.3033 0.2940 0.2621 0.0279  -0.0128 -0.0510 983  ALA B N   
15903 C CA  . ALA B 985  ? 0.3191 0.3076 0.2808 0.0297  -0.0125 -0.0520 983  ALA B CA  
15904 C C   . ALA B 985  ? 0.3267 0.3073 0.2911 0.0280  -0.0175 -0.0537 983  ALA B C   
15905 O O   . ALA B 985  ? 0.3166 0.2973 0.2880 0.0266  -0.0178 -0.0530 983  ALA B O   
15906 C CB  . ALA B 985  ? 0.3131 0.2997 0.2668 0.0348  -0.0104 -0.0539 983  ALA B CB  
15907 N N   . HIS B 986  ? 0.3082 0.2822 0.2671 0.0278  -0.0215 -0.0558 984  HIS B N   
15908 C CA  . HIS B 986  ? 0.3420 0.3087 0.3037 0.0258  -0.0268 -0.0572 984  HIS B CA  
15909 C C   . HIS B 986  ? 0.3169 0.2884 0.2898 0.0214  -0.0276 -0.0549 984  HIS B C   
15910 O O   . HIS B 986  ? 0.3349 0.3060 0.3147 0.0198  -0.0283 -0.0543 984  HIS B O   
15911 C CB  . HIS B 986  ? 0.3180 0.2777 0.2714 0.0263  -0.0312 -0.0597 984  HIS B CB  
15912 C CG  . HIS B 986  ? 0.4047 0.3576 0.3612 0.0236  -0.0374 -0.0610 984  HIS B CG  
15913 N ND1 . HIS B 986  ? 0.4079 0.3530 0.3568 0.0240  -0.0423 -0.0635 984  HIS B ND1 
15914 C CD2 . HIS B 986  ? 0.3974 0.3505 0.3639 0.0203  -0.0396 -0.0599 984  HIS B CD2 
15915 C CE1 . HIS B 986  ? 0.4464 0.3873 0.4009 0.0209  -0.0476 -0.0640 984  HIS B CE1 
15916 N NE2 . HIS B 986  ? 0.4094 0.3554 0.3749 0.0186  -0.0458 -0.0617 984  HIS B NE2 
15917 N N   . VAL B 987  ? 0.2803 0.2566 0.2549 0.0196  -0.0272 -0.0534 985  VAL B N   
15918 C CA  . VAL B 987  ? 0.3085 0.2887 0.2928 0.0161  -0.0284 -0.0518 985  VAL B CA  
15919 C C   . VAL B 987  ? 0.3280 0.3147 0.3199 0.0152  -0.0245 -0.0498 985  VAL B C   
15920 O O   . VAL B 987  ? 0.3456 0.3338 0.3456 0.0130  -0.0255 -0.0490 985  VAL B O   
15921 C CB  . VAL B 987  ? 0.2988 0.2812 0.2818 0.0152  -0.0291 -0.0510 985  VAL B CB  
15922 C CG1 . VAL B 987  ? 0.3023 0.2896 0.2952 0.0125  -0.0295 -0.0494 985  VAL B CG1 
15923 C CG2 . VAL B 987  ? 0.2905 0.2659 0.2669 0.0155  -0.0341 -0.0528 985  VAL B CG2 
15924 N N   . THR B 988  ? 0.3094 0.3007 0.2990 0.0169  -0.0200 -0.0487 986  THR B N   
15925 C CA  . THR B 988  ? 0.3173 0.3149 0.3135 0.0160  -0.0166 -0.0467 986  THR B CA  
15926 C C   . THR B 988  ? 0.3360 0.3311 0.3344 0.0166  -0.0165 -0.0468 986  THR B C   
15927 O O   . THR B 988  ? 0.3386 0.3377 0.3435 0.0150  -0.0151 -0.0451 986  THR B O   
15928 C CB  . THR B 988  ? 0.3236 0.3271 0.3172 0.0172  -0.0124 -0.0453 986  THR B CB  
15929 O OG1 . THR B 988  ? 0.3479 0.3498 0.3351 0.0205  -0.0108 -0.0461 986  THR B OG1 
15930 C CG2 . THR B 988  ? 0.3389 0.3444 0.3304 0.0160  -0.0126 -0.0447 986  THR B CG2 
15931 N N   . SER B 989  ? 0.3527 0.3409 0.3453 0.0189  -0.0183 -0.0487 987  SER B N   
15932 C CA  . SER B 989  ? 0.3838 0.3680 0.3784 0.0193  -0.0191 -0.0487 987  SER B CA  
15933 C C   . SER B 989  ? 0.3707 0.3511 0.3710 0.0159  -0.0232 -0.0487 987  SER B C   
15934 O O   . SER B 989  ? 0.3980 0.3771 0.4025 0.0148  -0.0235 -0.0475 987  SER B O   
15935 C CB  . SER B 989  ? 0.3596 0.3367 0.3456 0.0234  -0.0198 -0.0511 987  SER B CB  
15936 O OG  . SER B 989  ? 0.4536 0.4226 0.4346 0.0235  -0.0244 -0.0538 987  SER B OG  
15937 N N   . ARG B 990  ? 0.3132 0.2924 0.3143 0.0141  -0.0264 -0.0496 988  ARG B N   
15938 C CA  . ARG B 990  ? 0.3219 0.2981 0.3289 0.0108  -0.0307 -0.0494 988  ARG B CA  
15939 C C   . ARG B 990  ? 0.3441 0.3283 0.3608 0.0076  -0.0299 -0.0473 988  ARG B C   
15940 O O   . ARG B 990  ? 0.3473 0.3321 0.3714 0.0047  -0.0317 -0.0461 988  ARG B O   
15941 C CB  . ARG B 990  ? 0.3369 0.3056 0.3384 0.0110  -0.0359 -0.0521 988  ARG B CB  
15942 C CG  . ARG B 990  ? 0.3999 0.3601 0.3905 0.0148  -0.0368 -0.0548 988  ARG B CG  
15943 C CD  . ARG B 990  ? 0.4234 0.3760 0.4145 0.0144  -0.0395 -0.0554 988  ARG B CD  
15944 N NE  . ARG B 990  ? 0.3801 0.3250 0.3709 0.0121  -0.0460 -0.0571 988  ARG B NE  
15945 C CZ  . ARG B 990  ? 0.3948 0.3316 0.3860 0.0109  -0.0499 -0.0577 988  ARG B CZ  
15946 N NH1 . ARG B 990  ? 0.4197 0.3550 0.4121 0.0117  -0.0478 -0.0565 988  ARG B NH1 
15947 N NH2 . ARG B 990  ? 0.4159 0.3454 0.4059 0.0087  -0.0563 -0.0594 988  ARG B NH2 
15948 N N   . ILE B 991  ? 0.3173 0.3075 0.3341 0.0082  -0.0273 -0.0469 989  ILE B N   
15949 C CA  . ILE B 991  ? 0.3063 0.3034 0.3315 0.0060  -0.0266 -0.0454 989  ILE B CA  
15950 C C   . ILE B 991  ? 0.3155 0.3182 0.3465 0.0049  -0.0229 -0.0432 989  ILE B C   
15951 O O   . ILE B 991  ? 0.3148 0.3178 0.3426 0.0064  -0.0200 -0.0426 989  ILE B O   
15952 C CB  . ILE B 991  ? 0.2950 0.2954 0.3177 0.0070  -0.0252 -0.0457 989  ILE B CB  
15953 C CG1 . ILE B 991  ? 0.2980 0.3033 0.3286 0.0053  -0.0263 -0.0451 989  ILE B CG1 
15954 C CG2 . ILE B 991  ? 0.3193 0.3239 0.3393 0.0084  -0.0204 -0.0447 989  ILE B CG2 
15955 C CD1 . ILE B 991  ? 0.3214 0.3230 0.3538 0.0043  -0.0317 -0.0462 989  ILE B CD1 
15956 N N   . LYS B 992  ? 0.3211 0.3288 0.3607 0.0025  -0.0230 -0.0419 990  LYS B N   
15957 C CA  . LYS B 992  ? 0.3616 0.3753 0.4066 0.0014  -0.0194 -0.0397 990  LYS B CA  
15958 C C   . LYS B 992  ? 0.3386 0.3598 0.3878 0.0014  -0.0170 -0.0395 990  LYS B C   
15959 O O   . LYS B 992  ? 0.3933 0.4186 0.4498 -0.0001 -0.0179 -0.0391 990  LYS B O   
15960 C CB  . LYS B 992  ? 0.3424 0.3558 0.3941 -0.0016 -0.0212 -0.0380 990  LYS B CB  
15961 C CG  . LYS B 992  ? 0.4001 0.4045 0.4471 -0.0015 -0.0240 -0.0384 990  LYS B CG  
15962 C CD  . LYS B 992  ? 0.4366 0.4392 0.4902 -0.0050 -0.0274 -0.0370 990  LYS B CD  
15963 C CE  . LYS B 992  ? 0.5030 0.4944 0.5507 -0.0048 -0.0316 -0.0383 990  LYS B CE  
15964 N NZ  . LYS B 992  ? 0.5725 0.5605 0.6251 -0.0082 -0.0371 -0.0382 990  LYS B NZ  
15965 N N   . ALA B 993  ? 0.3222 0.3451 0.3668 0.0031  -0.0143 -0.0399 991  ALA B N   
15966 C CA  . ALA B 993  ? 0.2979 0.3266 0.3452 0.0033  -0.0122 -0.0400 991  ALA B CA  
15967 C C   . ALA B 993  ? 0.3090 0.3405 0.3529 0.0041  -0.0083 -0.0392 991  ALA B C   
15968 O O   . ALA B 993  ? 0.2807 0.3095 0.3191 0.0051  -0.0076 -0.0390 991  ALA B O   
15969 C CB  . ALA B 993  ? 0.2576 0.2842 0.3027 0.0043  -0.0145 -0.0416 991  ALA B CB  
15970 N N   . GLY B 994  ? 0.2600 0.2973 0.3074 0.0038  -0.0058 -0.0388 992  GLY B N   
15971 C CA  . GLY B 994  ? 0.2597 0.2999 0.3040 0.0043  -0.0026 -0.0381 992  GLY B CA  
15972 C C   . GLY B 994  ? 0.2631 0.3020 0.3019 0.0053  -0.0025 -0.0390 992  GLY B C   
15973 O O   . GLY B 994  ? 0.2542 0.2944 0.2895 0.0056  -0.0006 -0.0382 992  GLY B O   
15974 N N   . ASN B 995  ? 0.2411 0.2777 0.2793 0.0056  -0.0046 -0.0404 993  ASN B N   
15975 C CA  . ASN B 995  ? 0.2192 0.2547 0.2526 0.0060  -0.0048 -0.0408 993  ASN B CA  
15976 C C   . ASN B 995  ? 0.2458 0.2762 0.2758 0.0064  -0.0077 -0.0414 993  ASN B C   
15977 O O   . ASN B 995  ? 0.2491 0.2777 0.2815 0.0064  -0.0103 -0.0423 993  ASN B O   
15978 C CB  . ASN B 995  ? 0.2200 0.2575 0.2554 0.0059  -0.0045 -0.0418 993  ASN B CB  
15979 C CG  . ASN B 995  ? 0.2052 0.2471 0.2408 0.0056  -0.0014 -0.0413 993  ASN B CG  
15980 O OD1 . ASN B 995  ? 0.2607 0.3061 0.3000 0.0056  0.0002  -0.0410 993  ASN B OD1 
15981 N ND2 . ASN B 995  ? 0.2295 0.2713 0.2608 0.0052  -0.0009 -0.0410 993  ASN B ND2 
15982 N N   . LEU B 996  ? 0.2589 0.2875 0.2834 0.0068  -0.0074 -0.0408 994  LEU B N   
15983 C CA  . LEU B 996  ? 0.2101 0.2341 0.2298 0.0074  -0.0097 -0.0412 994  LEU B CA  
15984 C C   . LEU B 996  ? 0.2258 0.2497 0.2410 0.0070  -0.0095 -0.0406 994  LEU B C   
15985 O O   . LEU B 996  ? 0.2540 0.2814 0.2685 0.0064  -0.0072 -0.0395 994  LEU B O   
15986 C CB  . LEU B 996  ? 0.1994 0.2216 0.2155 0.0087  -0.0091 -0.0411 994  LEU B CB  
15987 C CG  . LEU B 996  ? 0.2760 0.2977 0.2957 0.0088  -0.0091 -0.0411 994  LEU B CG  
15988 C CD1 . LEU B 996  ? 0.3353 0.3535 0.3500 0.0106  -0.0091 -0.0414 994  LEU B CD1 
15989 C CD2 . LEU B 996  ? 0.2751 0.2949 0.2998 0.0077  -0.0121 -0.0420 994  LEU B CD2 
15990 N N   . TYR B 997  ? 0.2384 0.2583 0.2507 0.0070  -0.0123 -0.0409 995  TYR B N   
15991 C CA  . TYR B 997  ? 0.2261 0.2452 0.2342 0.0061  -0.0126 -0.0398 995  TYR B CA  
15992 C C   . TYR B 997  ? 0.2520 0.2671 0.2536 0.0067  -0.0143 -0.0395 995  TYR B C   
15993 O O   . TYR B 997  ? 0.2808 0.2920 0.2824 0.0073  -0.0174 -0.0407 995  TYR B O   
15994 C CB  . TYR B 997  ? 0.2431 0.2607 0.2543 0.0054  -0.0147 -0.0403 995  TYR B CB  
15995 C CG  . TYR B 997  ? 0.2721 0.2935 0.2883 0.0051  -0.0128 -0.0408 995  TYR B CG  
15996 C CD1 . TYR B 997  ? 0.3024 0.3260 0.3171 0.0039  -0.0111 -0.0399 995  TYR B CD1 
15997 C CD2 . TYR B 997  ? 0.2782 0.3014 0.3006 0.0059  -0.0128 -0.0421 995  TYR B CD2 
15998 C CE1 . TYR B 997  ? 0.2955 0.3221 0.3137 0.0037  -0.0096 -0.0407 995  TYR B CE1 
15999 C CE2 . TYR B 997  ? 0.2849 0.3119 0.3110 0.0058  -0.0107 -0.0427 995  TYR B CE2 
16000 C CZ  . TYR B 997  ? 0.3096 0.3379 0.3331 0.0049  -0.0092 -0.0421 995  TYR B CZ  
16001 O OH  . TYR B 997  ? 0.3804 0.4119 0.4065 0.0050  -0.0073 -0.0429 995  TYR B OH  
16002 N N   . ILE B 998  ? 0.2527 0.2692 0.2489 0.0065  -0.0125 -0.0380 996  ILE B N   
16003 C CA  . ILE B 998  ? 0.2700 0.2836 0.2590 0.0073  -0.0134 -0.0376 996  ILE B CA  
16004 C C   . ILE B 998  ? 0.2434 0.2563 0.2284 0.0055  -0.0140 -0.0354 996  ILE B C   
16005 O O   . ILE B 998  ? 0.2876 0.3046 0.2725 0.0040  -0.0117 -0.0335 996  ILE B O   
16006 C CB  . ILE B 998  ? 0.2750 0.2914 0.2606 0.0092  -0.0102 -0.0375 996  ILE B CB  
16007 C CG1 . ILE B 998  ? 0.2665 0.2827 0.2561 0.0108  -0.0098 -0.0393 996  ILE B CG1 
16008 C CG2 . ILE B 998  ? 0.2762 0.2894 0.2532 0.0105  -0.0109 -0.0375 996  ILE B CG2 
16009 C CD1 . ILE B 998  ? 0.3537 0.3644 0.3438 0.0114  -0.0133 -0.0413 996  ILE B CD1 
16010 N N   . ASN B 999  ? 0.2334 0.2411 0.2152 0.0054  -0.0176 -0.0355 997  ASN B N   
16011 C CA  . ASN B 999  ? 0.2653 0.2710 0.2421 0.0035  -0.0188 -0.0330 997  ASN B CA  
16012 C C   . ASN B 999  ? 0.2633 0.2695 0.2442 0.0012  -0.0193 -0.0318 997  ASN B C   
16013 O O   . ASN B 999  ? 0.2926 0.2995 0.2705 -0.0010 -0.0187 -0.0291 997  ASN B O   
16014 C CB  . ASN B 999  ? 0.3038 0.3127 0.2737 0.0035  -0.0157 -0.0309 997  ASN B CB  
16015 C CG  . ASN B 999  ? 0.2910 0.2975 0.2548 0.0061  -0.0161 -0.0324 997  ASN B CG  
16016 O OD1 . ASN B 999  ? 0.3002 0.3011 0.2629 0.0069  -0.0199 -0.0340 997  ASN B OD1 
16017 N ND2 . ASN B 999  ? 0.2907 0.3012 0.2507 0.0078  -0.0124 -0.0322 997  ASN B ND2 
16018 N N   . ARG B 1000 ? 0.2795 0.2851 0.2672 0.0018  -0.0205 -0.0338 998  ARG B N   
16019 C CA  . ARG B 1000 ? 0.2631 0.2680 0.2545 0.0003  -0.0214 -0.0336 998  ARG B CA  
16020 C C   . ARG B 1000 ? 0.2781 0.2813 0.2758 0.0020  -0.0237 -0.0362 998  ARG B C   
16021 O O   . ARG B 1000 ? 0.2807 0.2835 0.2801 0.0037  -0.0246 -0.0377 998  ARG B O   
16022 C CB  . ARG B 1000 ? 0.2630 0.2733 0.2564 -0.0010 -0.0179 -0.0330 998  ARG B CB  
16023 C CG  . ARG B 1000 ? 0.2440 0.2591 0.2411 0.0008  -0.0150 -0.0346 998  ARG B CG  
16024 C CD  . ARG B 1000 ? 0.2638 0.2830 0.2648 -0.0002 -0.0129 -0.0348 998  ARG B CD  
16025 N NE  . ARG B 1000 ? 0.2708 0.2875 0.2758 0.0000  -0.0147 -0.0365 998  ARG B NE  
16026 C CZ  . ARG B 1000 ? 0.3116 0.3306 0.3193 -0.0005 -0.0136 -0.0373 998  ARG B CZ  
16027 N NH1 . ARG B 1000 ? 0.2774 0.3011 0.2846 -0.0016 -0.0110 -0.0362 998  ARG B NH1 
16028 N NH2 . ARG B 1000 ? 0.2835 0.3001 0.2943 0.0004  -0.0151 -0.0393 998  ARG B NH2 
16029 N N   . ASN B 1001 ? 0.2655 0.2675 0.2665 0.0016  -0.0246 -0.0368 999  ASN B N   
16030 C CA  . ASN B 1001 ? 0.2591 0.2607 0.2666 0.0037  -0.0261 -0.0393 999  ASN B CA  
16031 C C   . ASN B 1001 ? 0.2717 0.2793 0.2842 0.0045  -0.0227 -0.0408 999  ASN B C   
16032 O O   . ASN B 1001 ? 0.2728 0.2840 0.2837 0.0037  -0.0196 -0.0400 999  ASN B O   
16033 C CB  . ASN B 1001 ? 0.2638 0.2618 0.2728 0.0037  -0.0283 -0.0398 999  ASN B CB  
16034 C CG  . ASN B 1001 ? 0.3341 0.3343 0.3437 0.0026  -0.0258 -0.0401 999  ASN B CG  
16035 O OD1 . ASN B 1001 ? 0.3030 0.3086 0.3155 0.0029  -0.0226 -0.0411 999  ASN B OD1 
16036 N ND2 . ASN B 1001 ? 0.3585 0.3542 0.3650 0.0010  -0.0277 -0.0390 999  ASN B ND2 
16037 N N   . ILE B 1002 ? 0.2306 0.2396 0.2496 0.0063  -0.0234 -0.0427 1000 ILE B N   
16038 C CA  . ILE B 1002 ? 0.2614 0.2759 0.2851 0.0068  -0.0203 -0.0437 1000 ILE B CA  
16039 C C   . ILE B 1002 ? 0.2766 0.2941 0.3048 0.0076  -0.0186 -0.0451 1000 ILE B C   
16040 O O   . ILE B 1002 ? 0.2863 0.3086 0.3194 0.0083  -0.0165 -0.0459 1000 ILE B O   
16041 C CB  . ILE B 1002 ? 0.2792 0.2943 0.3068 0.0078  -0.0218 -0.0443 1000 ILE B CB  
16042 C CG1 . ILE B 1002 ? 0.2224 0.2368 0.2557 0.0093  -0.0249 -0.0456 1000 ILE B CG1 
16043 C CG2 . ILE B 1002 ? 0.2558 0.2674 0.2775 0.0072  -0.0234 -0.0433 1000 ILE B CG2 
16044 C CD1 . ILE B 1002 ? 0.2473 0.2634 0.2857 0.0097  -0.0265 -0.0460 1000 ILE B CD1 
16045 N N   . ILE B 1003 ? 0.2810 0.2956 0.3073 0.0075  -0.0196 -0.0455 1001 ILE B N   
16046 C CA  . ILE B 1003 ? 0.2631 0.2794 0.2927 0.0087  -0.0184 -0.0474 1001 ILE B CA  
16047 C C   . ILE B 1003 ? 0.3270 0.3434 0.3523 0.0070  -0.0167 -0.0470 1001 ILE B C   
16048 O O   . ILE B 1003 ? 0.3419 0.3567 0.3623 0.0047  -0.0168 -0.0449 1001 ILE B O   
16049 C CB  . ILE B 1003 ? 0.3030 0.3150 0.3345 0.0108  -0.0217 -0.0490 1001 ILE B CB  
16050 C CG1 . ILE B 1003 ? 0.3173 0.3220 0.3427 0.0093  -0.0249 -0.0476 1001 ILE B CG1 
16051 C CG2 . ILE B 1003 ? 0.2915 0.3045 0.3281 0.0125  -0.0237 -0.0493 1001 ILE B CG2 
16052 C CD1 . ILE B 1003 ? 0.3472 0.3465 0.3739 0.0116  -0.0283 -0.0493 1001 ILE B CD1 
16053 N N   . GLY B 1004 ? 0.3084 0.3270 0.3356 0.0080  -0.0150 -0.0489 1002 GLY B N   
16054 C CA  . GLY B 1004 ? 0.3650 0.3824 0.3880 0.0064  -0.0144 -0.0490 1002 GLY B CA  
16055 C C   . GLY B 1004 ? 0.3411 0.3633 0.3623 0.0044  -0.0115 -0.0473 1002 GLY B C   
16056 O O   . GLY B 1004 ? 0.3466 0.3677 0.3638 0.0019  -0.0119 -0.0457 1002 GLY B O   
16057 N N   . ALA B 1005 ? 0.2948 0.3225 0.3195 0.0054  -0.0088 -0.0472 1003 ALA B N   
16058 C CA  . ALA B 1005 ? 0.2614 0.2936 0.2847 0.0039  -0.0062 -0.0455 1003 ALA B CA  
16059 C C   . ALA B 1005 ? 0.3259 0.3588 0.3462 0.0028  -0.0056 -0.0460 1003 ALA B C   
16060 O O   . ALA B 1005 ? 0.3293 0.3614 0.3499 0.0040  -0.0056 -0.0483 1003 ALA B O   
16061 C CB  . ALA B 1005 ? 0.3123 0.3494 0.3398 0.0052  -0.0037 -0.0456 1003 ALA B CB  
16062 N N   . VAL B 1006 ? 0.2469 0.2813 0.2643 0.0006  -0.0052 -0.0439 1004 VAL B N   
16063 C CA  . VAL B 1006 ? 0.2833 0.3180 0.2977 -0.0013 -0.0055 -0.0439 1004 VAL B CA  
16064 C C   . VAL B 1006 ? 0.2482 0.2889 0.2632 -0.0011 -0.0027 -0.0433 1004 VAL B C   
16065 O O   . VAL B 1006 ? 0.2430 0.2874 0.2591 -0.0010 -0.0010 -0.0413 1004 VAL B O   
16066 C CB  . VAL B 1006 ? 0.2787 0.3121 0.2902 -0.0042 -0.0072 -0.0414 1004 VAL B CB  
16067 C CG1 . VAL B 1006 ? 0.2769 0.3117 0.2859 -0.0067 -0.0077 -0.0409 1004 VAL B CG1 
16068 C CG2 . VAL B 1006 ? 0.3122 0.3387 0.3224 -0.0046 -0.0102 -0.0418 1004 VAL B CG2 
16069 N N   . VAL B 1007 ? 0.2431 0.2841 0.2567 -0.0008 -0.0024 -0.0452 1005 VAL B N   
16070 C CA  . VAL B 1007 ? 0.2751 0.3214 0.2883 -0.0007 0.0000  -0.0447 1005 VAL B CA  
16071 C C   . VAL B 1007 ? 0.2678 0.3177 0.2802 -0.0027 0.0002  -0.0415 1005 VAL B C   
16072 O O   . VAL B 1007 ? 0.2521 0.3011 0.2624 -0.0050 -0.0017 -0.0405 1005 VAL B O   
16073 C CB  . VAL B 1007 ? 0.2765 0.3215 0.2864 -0.0006 -0.0006 -0.0472 1005 VAL B CB  
16074 C CG1 . VAL B 1007 ? 0.2653 0.3156 0.2737 -0.0010 0.0014  -0.0462 1005 VAL B CG1 
16075 C CG2 . VAL B 1007 ? 0.2745 0.3174 0.2859 0.0023  0.0000  -0.0504 1005 VAL B CG2 
16076 N N   . GLY B 1008 ? 0.2718 0.3261 0.2861 -0.0017 0.0024  -0.0399 1006 GLY B N   
16077 C CA  . GLY B 1008 ? 0.2915 0.3499 0.3054 -0.0027 0.0029  -0.0371 1006 GLY B CA  
16078 C C   . GLY B 1008 ? 0.2796 0.3377 0.2943 -0.0031 0.0024  -0.0353 1006 GLY B C   
16079 O O   . GLY B 1008 ? 0.2622 0.3243 0.2771 -0.0033 0.0031  -0.0330 1006 GLY B O   
16080 N N   . VAL B 1009 ? 0.2277 0.2814 0.2425 -0.0030 0.0012  -0.0363 1007 VAL B N   
16081 C CA  . VAL B 1009 ? 0.2559 0.3090 0.2704 -0.0032 0.0008  -0.0347 1007 VAL B CA  
16082 C C   . VAL B 1009 ? 0.2453 0.2960 0.2614 -0.0009 0.0013  -0.0354 1007 VAL B C   
16083 O O   . VAL B 1009 ? 0.2519 0.3038 0.2679 0.0001  0.0022  -0.0341 1007 VAL B O   
16084 C CB  . VAL B 1009 ? 0.2695 0.3189 0.2819 -0.0054 -0.0016 -0.0346 1007 VAL B CB  
16085 C CG1 . VAL B 1009 ? 0.2561 0.3057 0.2675 -0.0058 -0.0016 -0.0325 1007 VAL B CG1 
16086 C CG2 . VAL B 1009 ? 0.2536 0.3047 0.2646 -0.0081 -0.0027 -0.0340 1007 VAL B CG2 
16087 N N   . GLN B 1010 ? 0.2563 0.3036 0.2738 -0.0001 0.0006  -0.0375 1008 GLN B N   
16088 C CA  . GLN B 1010 ? 0.2530 0.2991 0.2732 0.0018  0.0010  -0.0383 1008 GLN B CA  
16089 C C   . GLN B 1010 ? 0.2627 0.3108 0.2856 0.0025  0.0023  -0.0394 1008 GLN B C   
16090 O O   . GLN B 1010 ? 0.2846 0.3311 0.3092 0.0032  0.0016  -0.0414 1008 GLN B O   
16091 C CB  . GLN B 1010 ? 0.2489 0.2901 0.2691 0.0021  -0.0013 -0.0394 1008 GLN B CB  
16092 C CG  . GLN B 1010 ? 0.2628 0.3019 0.2795 0.0012  -0.0025 -0.0380 1008 GLN B CG  
16093 C CD  . GLN B 1010 ? 0.2690 0.3058 0.2835 -0.0006 -0.0043 -0.0379 1008 GLN B CD  
16094 O OE1 . GLN B 1010 ? 0.2977 0.3319 0.3131 -0.0006 -0.0056 -0.0397 1008 GLN B OE1 
16095 N NE2 . GLN B 1010 ? 0.2576 0.2952 0.2691 -0.0023 -0.0045 -0.0357 1008 GLN B NE2 
16096 N N   . PRO B 1011 ? 0.2498 0.3017 0.2730 0.0027  0.0043  -0.0382 1009 PRO B N   
16097 C CA  . PRO B 1011 ? 0.2498 0.3041 0.2756 0.0033  0.0059  -0.0387 1009 PRO B CA  
16098 C C   . PRO B 1011 ? 0.2644 0.3172 0.2942 0.0042  0.0055  -0.0396 1009 PRO B C   
16099 O O   . PRO B 1011 ? 0.2392 0.2899 0.2700 0.0045  0.0046  -0.0389 1009 PRO B O   
16100 C CB  . PRO B 1011 ? 0.2465 0.3038 0.2720 0.0033  0.0075  -0.0363 1009 PRO B CB  
16101 C CG  . PRO B 1011 ? 0.2666 0.3245 0.2891 0.0027  0.0069  -0.0351 1009 PRO B CG  
16102 C CD  . PRO B 1011 ? 0.2523 0.3066 0.2739 0.0025  0.0051  -0.0360 1009 PRO B CD  
16103 N N   . PHE B 1012 ? 0.2147 0.2687 0.2469 0.0048  0.0061  -0.0412 1010 PHE B N   
16104 C CA  . PHE B 1012 ? 0.2695 0.3223 0.3060 0.0058  0.0050  -0.0424 1010 PHE B CA  
16105 C C   . PHE B 1012 ? 0.2410 0.2978 0.2825 0.0060  0.0069  -0.0417 1010 PHE B C   
16106 O O   . PHE B 1012 ? 0.2519 0.3128 0.2937 0.0061  0.0093  -0.0416 1010 PHE B O   
16107 C CB  . PHE B 1012 ? 0.2630 0.3141 0.2992 0.0068  0.0039  -0.0450 1010 PHE B CB  
16108 C CG  . PHE B 1012 ? 0.2616 0.3115 0.3025 0.0081  0.0023  -0.0462 1010 PHE B CG  
16109 C CD1 . PHE B 1012 ? 0.2824 0.3280 0.3230 0.0078  -0.0006 -0.0458 1010 PHE B CD1 
16110 C CD2 . PHE B 1012 ? 0.3187 0.3724 0.3644 0.0096  0.0037  -0.0475 1010 PHE B CD2 
16111 C CE1 . PHE B 1012 ? 0.2452 0.2897 0.2902 0.0089  -0.0026 -0.0468 1010 PHE B CE1 
16112 C CE2 . PHE B 1012 ? 0.3078 0.3613 0.3588 0.0109  0.0019  -0.0484 1010 PHE B CE2 
16113 C CZ  . PHE B 1012 ? 0.2871 0.3359 0.3378 0.0105  -0.0015 -0.0480 1010 PHE B CZ  
16114 N N   . GLY B 1013 ? 0.2358 0.2915 0.2810 0.0057  0.0056  -0.0410 1011 GLY B N   
16115 C CA  . GLY B 1013 ? 0.2468 0.3064 0.2980 0.0054  0.0067  -0.0401 1011 GLY B CA  
16116 C C   . GLY B 1013 ? 0.2939 0.3508 0.3469 0.0043  0.0050  -0.0385 1011 GLY B C   
16117 O O   . GLY B 1013 ? 0.2781 0.3310 0.3268 0.0041  0.0039  -0.0378 1011 GLY B O   
16118 N N   . GLY B 1014 ? 0.3163 0.3757 0.3757 0.0036  0.0047  -0.0378 1012 GLY B N   
16119 C CA  . GLY B 1014 ? 0.3078 0.3637 0.3690 0.0024  0.0022  -0.0366 1012 GLY B CA  
16120 C C   . GLY B 1014 ? 0.3539 0.4130 0.4196 0.0004  0.0034  -0.0340 1012 GLY B C   
16121 O O   . GLY B 1014 ? 0.4190 0.4830 0.4852 0.0000  0.0067  -0.0326 1012 GLY B O   
16122 N N   . ARG B 1015 ? 0.3665 0.4224 0.4352 -0.0010 0.0005  -0.0332 1013 ARG B N   
16123 C CA  A ARG B 1015 ? 0.4079 0.4646 0.4808 -0.0036 0.0005  -0.0304 1013 ARG B CA  
16124 C CA  B ARG B 1015 ? 0.4071 0.4643 0.4802 -0.0036 0.0007  -0.0303 1013 ARG B CA  
16125 C C   . ARG B 1015 ? 0.3616 0.4220 0.4433 -0.0051 -0.0012 -0.0300 1013 ARG B C   
16126 O O   . ARG B 1015 ? 0.3474 0.4093 0.4316 -0.0038 -0.0025 -0.0321 1013 ARG B O   
16127 C CB  A ARG B 1015 ? 0.4170 0.4654 0.4853 -0.0040 -0.0022 -0.0299 1013 ARG B CB  
16128 C CB  B ARG B 1015 ? 0.4167 0.4660 0.4851 -0.0041 -0.0016 -0.0295 1013 ARG B CB  
16129 C CG  A ARG B 1015 ? 0.4212 0.4634 0.4864 -0.0027 -0.0060 -0.0326 1013 ARG B CG  
16130 C CG  B ARG B 1015 ? 0.4281 0.4703 0.4920 -0.0026 -0.0051 -0.0321 1013 ARG B CG  
16131 C CD  A ARG B 1015 ? 0.4503 0.4846 0.5135 -0.0036 -0.0096 -0.0323 1013 ARG B CD  
16132 C CD  B ARG B 1015 ? 0.4483 0.4836 0.5122 -0.0039 -0.0090 -0.0317 1013 ARG B CD  
16133 N NE  A ARG B 1015 ? 0.4671 0.5022 0.5376 -0.0066 -0.0119 -0.0307 1013 ARG B NE  
16134 N NE  B ARG B 1015 ? 0.4511 0.4876 0.5221 -0.0060 -0.0119 -0.0316 1013 ARG B NE  
16135 C CZ  A ARG B 1015 ? 0.4292 0.4644 0.5043 -0.0076 -0.0152 -0.0317 1013 ARG B CZ  
16136 C CZ  B ARG B 1015 ? 0.4374 0.4759 0.5151 -0.0091 -0.0126 -0.0291 1013 ARG B CZ  
16137 N NH1 A ARG B 1015 ? 0.4055 0.4398 0.4784 -0.0055 -0.0167 -0.0343 1013 ARG B NH1 
16138 N NH1 B ARG B 1015 ? 0.4434 0.4825 0.5212 -0.0106 -0.0106 -0.0263 1013 ARG B NH1 
16139 N NH2 A ARG B 1015 ? 0.4420 0.4784 0.5243 -0.0108 -0.0174 -0.0298 1013 ARG B NH2 
16140 N NH2 B ARG B 1015 ? 0.4376 0.4778 0.5221 -0.0110 -0.0157 -0.0292 1013 ARG B NH2 
16141 N N   . GLY B 1016 ? 0.3534 0.4151 0.4400 -0.0081 -0.0016 -0.0271 1014 GLY B N   
16142 C CA  . GLY B 1016 ? 0.3313 0.3966 0.4270 -0.0102 -0.0038 -0.0263 1014 GLY B CA  
16143 C C   . GLY B 1016 ? 0.3331 0.4087 0.4354 -0.0091 -0.0007 -0.0266 1014 GLY B C   
16144 O O   . GLY B 1016 ? 0.3700 0.4518 0.4721 -0.0086 0.0039  -0.0256 1014 GLY B O   
16145 N N   . LEU B 1017 ? 0.2986 0.3762 0.4066 -0.0085 -0.0034 -0.0282 1015 LEU B N   
16146 C CA  . LEU B 1017 ? 0.3088 0.3961 0.4237 -0.0067 -0.0010 -0.0289 1015 LEU B CA  
16147 C C   . LEU B 1017 ? 0.3147 0.4014 0.4233 -0.0026 0.0013  -0.0321 1015 LEU B C   
16148 O O   . LEU B 1017 ? 0.3284 0.4221 0.4414 -0.0002 0.0035  -0.0334 1015 LEU B O   
16149 C CB  . LEU B 1017 ? 0.3482 0.4371 0.4711 -0.0070 -0.0053 -0.0296 1015 LEU B CB  
16150 C CG  . LEU B 1017 ? 0.3873 0.4781 0.5184 -0.0115 -0.0081 -0.0264 1015 LEU B CG  
16151 C CD1 . LEU B 1017 ? 0.3796 0.4693 0.5163 -0.0117 -0.0138 -0.0276 1015 LEU B CD1 
16152 C CD2 . LEU B 1017 ? 0.3509 0.4540 0.4910 -0.0132 -0.0035 -0.0231 1015 LEU B CD2 
16153 N N   . SER B 1018 ? 0.2918 0.3704 0.3906 -0.0016 0.0007  -0.0334 1016 SER B N   
16154 C CA  . SER B 1018 ? 0.3155 0.3925 0.4081 0.0016  0.0021  -0.0362 1016 SER B CA  
16155 C C   . SER B 1018 ? 0.3283 0.4091 0.4171 0.0020  0.0069  -0.0356 1016 SER B C   
16156 O O   . SER B 1018 ? 0.3348 0.4158 0.4198 0.0046  0.0085  -0.0379 1016 SER B O   
16157 C CB  . SER B 1018 ? 0.3396 0.4069 0.4239 0.0021  -0.0010 -0.0376 1016 SER B CB  
16158 O OG  . SER B 1018 ? 0.3519 0.4159 0.4386 0.0023  -0.0055 -0.0388 1016 SER B OG  
16159 N N   . GLY B 1019 ? 0.3441 0.4269 0.4333 -0.0004 0.0089  -0.0325 1017 GLY B N   
16160 C CA  . GLY B 1019 ? 0.3336 0.4217 0.4204 0.0000  0.0136  -0.0316 1017 GLY B CA  
16161 C C   . GLY B 1019 ? 0.3066 0.3933 0.3906 -0.0026 0.0147  -0.0282 1017 GLY B C   
16162 O O   . GLY B 1019 ? 0.3222 0.4039 0.4065 -0.0046 0.0120  -0.0265 1017 GLY B O   
16163 N N   . THR B 1020 ? 0.3069 0.3980 0.3877 -0.0022 0.0187  -0.0272 1018 THR B N   
16164 C CA  . THR B 1020 ? 0.2579 0.3483 0.3353 -0.0043 0.0200  -0.0237 1018 THR B CA  
16165 C C   . THR B 1020 ? 0.2910 0.3746 0.3598 -0.0033 0.0188  -0.0245 1018 THR B C   
16166 O O   . THR B 1020 ? 0.3150 0.3953 0.3813 -0.0048 0.0183  -0.0218 1018 THR B O   
16167 C CB  . THR B 1020 ? 0.3066 0.4054 0.3839 -0.0042 0.0249  -0.0222 1018 THR B CB  
16168 O OG1 . THR B 1020 ? 0.2229 0.3223 0.2947 -0.0011 0.0264  -0.0258 1018 THR B OG1 
16169 C CG2 . THR B 1020 ? 0.2537 0.3613 0.3405 -0.0051 0.0268  -0.0210 1018 THR B CG2 
16170 N N   . GLY B 1021 ? 0.2764 0.3580 0.3408 -0.0009 0.0184  -0.0279 1019 GLY B N   
16171 C CA  . GLY B 1021 ? 0.2728 0.3509 0.3296 -0.0001 0.0183  -0.0283 1019 GLY B CA  
16172 C C   . GLY B 1021 ? 0.2445 0.3275 0.2980 -0.0002 0.0217  -0.0267 1019 GLY B C   
16173 O O   . GLY B 1021 ? 0.2898 0.3790 0.3466 -0.0008 0.0245  -0.0256 1019 GLY B O   
16174 N N   . PRO B 1022 ? 0.2441 0.3249 0.2909 0.0003  0.0216  -0.0266 1020 PRO B N   
16175 C CA  . PRO B 1022 ? 0.2310 0.3062 0.2740 0.0010  0.0189  -0.0278 1020 PRO B CA  
16176 C C   . PRO B 1022 ? 0.2621 0.3358 0.3042 0.0025  0.0177  -0.0316 1020 PRO B C   
16177 O O   . PRO B 1022 ? 0.2550 0.3317 0.2984 0.0034  0.0190  -0.0336 1020 PRO B O   
16178 C CB  . PRO B 1022 ? 0.2727 0.3489 0.3100 0.0010  0.0198  -0.0262 1020 PRO B CB  
16179 C CG  . PRO B 1022 ? 0.2644 0.3461 0.3004 0.0010  0.0228  -0.0265 1020 PRO B CG  
16180 C CD  . PRO B 1022 ? 0.2494 0.3344 0.2918 0.0003  0.0243  -0.0255 1020 PRO B CD  
16181 N N   . LYS B 1023 ? 0.2327 0.3018 0.2723 0.0029  0.0152  -0.0325 1021 LYS B N   
16182 C CA  . LYS B 1023 ? 0.2543 0.3211 0.2928 0.0039  0.0137  -0.0356 1021 LYS B CA  
16183 C C   . LYS B 1023 ? 0.2454 0.3139 0.2798 0.0044  0.0146  -0.0373 1021 LYS B C   
16184 O O   . LYS B 1023 ? 0.2196 0.2893 0.2499 0.0039  0.0153  -0.0362 1021 LYS B O   
16185 C CB  . LYS B 1023 ? 0.2544 0.3167 0.2904 0.0039  0.0113  -0.0356 1021 LYS B CB  
16186 C CG  . LYS B 1023 ? 0.2401 0.2991 0.2789 0.0038  0.0096  -0.0350 1021 LYS B CG  
16187 C CD  . LYS B 1023 ? 0.2349 0.2903 0.2699 0.0042  0.0080  -0.0349 1021 LYS B CD  
16188 C CE  . LYS B 1023 ? 0.2748 0.3257 0.3110 0.0046  0.0058  -0.0353 1021 LYS B CE  
16189 N NZ  . LYS B 1023 ? 0.2650 0.3142 0.3022 0.0048  0.0040  -0.0374 1021 LYS B NZ  
16190 N N   . ALA B 1024 ? 0.2543 0.3222 0.2895 0.0056  0.0142  -0.0402 1022 ALA B N   
16191 C CA  . ALA B 1024 ? 0.2695 0.3370 0.3002 0.0062  0.0142  -0.0426 1022 ALA B CA  
16192 C C   . ALA B 1024 ? 0.2791 0.3424 0.3056 0.0052  0.0116  -0.0427 1022 ALA B C   
16193 O O   . ALA B 1024 ? 0.2907 0.3509 0.3183 0.0048  0.0097  -0.0421 1022 ALA B O   
16194 C CB  . ALA B 1024 ? 0.2801 0.3470 0.3129 0.0082  0.0140  -0.0458 1022 ALA B CB  
16195 N N   . GLY B 1025 ? 0.2497 0.3134 0.2713 0.0046  0.0116  -0.0432 1023 GLY B N   
16196 C CA  . GLY B 1025 ? 0.2194 0.2804 0.2377 0.0031  0.0092  -0.0427 1023 GLY B CA  
16197 C C   . GLY B 1025 ? 0.2311 0.2935 0.2503 0.0022  0.0092  -0.0396 1023 GLY B C   
16198 O O   . GLY B 1025 ? 0.2348 0.2954 0.2532 0.0013  0.0074  -0.0389 1023 GLY B O   
16199 N N   . GLY B 1026 ? 0.2413 0.3068 0.2620 0.0026  0.0111  -0.0376 1024 GLY B N   
16200 C CA  . GLY B 1026 ? 0.2538 0.3202 0.2749 0.0023  0.0111  -0.0347 1024 GLY B CA  
16201 C C   . GLY B 1026 ? 0.2428 0.3129 0.2621 0.0021  0.0124  -0.0327 1024 GLY B C   
16202 O O   . GLY B 1026 ? 0.2478 0.3199 0.2655 0.0020  0.0137  -0.0334 1024 GLY B O   
16203 N N   . PRO B 1027 ? 0.2548 0.3258 0.2740 0.0022  0.0122  -0.0301 1025 PRO B N   
16204 C CA  . PRO B 1027 ? 0.2371 0.3115 0.2540 0.0020  0.0127  -0.0279 1025 PRO B CA  
16205 C C   . PRO B 1027 ? 0.2460 0.3216 0.2636 0.0022  0.0146  -0.0260 1025 PRO B C   
16206 O O   . PRO B 1027 ? 0.2246 0.3028 0.2396 0.0019  0.0150  -0.0241 1025 PRO B O   
16207 C CB  . PRO B 1027 ? 0.2392 0.3142 0.2565 0.0026  0.0116  -0.0258 1025 PRO B CB  
16208 C CG  . PRO B 1027 ? 0.2524 0.3238 0.2726 0.0036  0.0114  -0.0264 1025 PRO B CG  
16209 C CD  . PRO B 1027 ? 0.2597 0.3288 0.2804 0.0029  0.0111  -0.0293 1025 PRO B CD  
16210 N N   . LEU B 1028 ? 0.2438 0.3177 0.2650 0.0024  0.0155  -0.0261 1026 LEU B N   
16211 C CA  . LEU B 1028 ? 0.2340 0.3095 0.2563 0.0020  0.0173  -0.0239 1026 LEU B CA  
16212 C C   . LEU B 1028 ? 0.2571 0.3357 0.2788 0.0016  0.0194  -0.0254 1026 LEU B C   
16213 O O   . LEU B 1028 ? 0.2518 0.3330 0.2741 0.0010  0.0214  -0.0233 1026 LEU B O   
16214 C CB  . LEU B 1028 ? 0.2657 0.3383 0.2925 0.0019  0.0170  -0.0228 1026 LEU B CB  
16215 C CG  . LEU B 1028 ? 0.2902 0.3591 0.3172 0.0029  0.0151  -0.0217 1026 LEU B CG  
16216 C CD1 . LEU B 1028 ? 0.2707 0.3357 0.3014 0.0027  0.0145  -0.0207 1026 LEU B CD1 
16217 C CD2 . LEU B 1028 ? 0.3367 0.4071 0.3607 0.0034  0.0150  -0.0190 1026 LEU B CD2 
16218 N N   . TYR B 1029 ? 0.2654 0.3436 0.2859 0.0021  0.0190  -0.0289 1027 TYR B N   
16219 C CA  . TYR B 1029 ? 0.2301 0.3107 0.2510 0.0026  0.0210  -0.0310 1027 TYR B CA  
16220 C C   . TYR B 1029 ? 0.2472 0.3318 0.2635 0.0025  0.0231  -0.0301 1027 TYR B C   
16221 O O   . TYR B 1029 ? 0.2416 0.3299 0.2593 0.0025  0.0259  -0.0292 1027 TYR B O   
16222 C CB  . TYR B 1029 ? 0.2380 0.3160 0.2578 0.0035  0.0195  -0.0351 1027 TYR B CB  
16223 C CG  . TYR B 1029 ? 0.2523 0.3315 0.2746 0.0049  0.0209  -0.0379 1027 TYR B CG  
16224 C CD1 . TYR B 1029 ? 0.2482 0.3276 0.2771 0.0052  0.0212  -0.0377 1027 TYR B CD1 
16225 C CD2 . TYR B 1029 ? 0.2425 0.3222 0.2606 0.0062  0.0216  -0.0410 1027 TYR B CD2 
16226 C CE1 . TYR B 1029 ? 0.2245 0.3056 0.2563 0.0069  0.0224  -0.0401 1027 TYR B CE1 
16227 C CE2 . TYR B 1029 ? 0.2256 0.3064 0.2462 0.0082  0.0230  -0.0438 1027 TYR B CE2 
16228 C CZ  . TYR B 1029 ? 0.2796 0.3616 0.3074 0.0086  0.0234  -0.0433 1027 TYR B CZ  
16229 O OH  . TYR B 1029 ? 0.2855 0.3694 0.3166 0.0109  0.0246  -0.0460 1027 TYR B OH  
16230 N N   . LEU B 1030 ? 0.2624 0.3467 0.2731 0.0022  0.0218  -0.0302 1028 LEU B N   
16231 C CA  . LEU B 1030 ? 0.2660 0.3536 0.2709 0.0022  0.0233  -0.0299 1028 LEU B CA  
16232 C C   . LEU B 1030 ? 0.2790 0.3696 0.2843 0.0013  0.0253  -0.0253 1028 LEU B C   
16233 O O   . LEU B 1030 ? 0.2700 0.3643 0.2723 0.0014  0.0279  -0.0247 1028 LEU B O   
16234 C CB  . LEU B 1030 ? 0.2623 0.3487 0.2614 0.0016  0.0207  -0.0306 1028 LEU B CB  
16235 C CG  . LEU B 1030 ? 0.3047 0.3879 0.3019 0.0019  0.0185  -0.0349 1028 LEU B CG  
16236 C CD1 . LEU B 1030 ? 0.2711 0.3540 0.2624 0.0007  0.0159  -0.0350 1028 LEU B CD1 
16237 C CD2 . LEU B 1030 ? 0.2729 0.3559 0.2690 0.0036  0.0205  -0.0388 1028 LEU B CD2 
16238 N N   . GLY B 1031 ? 0.2748 0.3636 0.2834 0.0006  0.0240  -0.0221 1029 GLY B N   
16239 C CA  . GLY B 1031 ? 0.2854 0.3757 0.2944 -0.0003 0.0252  -0.0175 1029 GLY B CA  
16240 C C   . GLY B 1031 ? 0.2717 0.3650 0.2843 -0.0010 0.0284  -0.0163 1029 GLY B C   
16241 O O   . GLY B 1031 ? 0.2759 0.3715 0.2874 -0.0022 0.0300  -0.0124 1029 GLY B O   
16242 N N   . ARG B 1032 ? 0.2497 0.3433 0.2666 -0.0004 0.0292  -0.0193 1030 ARG B N   
16243 C CA  . ARG B 1032 ? 0.2648 0.3626 0.2861 -0.0010 0.0323  -0.0182 1030 ARG B CA  
16244 C C   . ARG B 1032 ? 0.2685 0.3719 0.2855 -0.0001 0.0357  -0.0194 1030 ARG B C   
16245 O O   . ARG B 1032 ? 0.2864 0.3952 0.3066 -0.0007 0.0390  -0.0177 1030 ARG B O   
16246 C CB  . ARG B 1032 ? 0.3169 0.4133 0.3451 -0.0004 0.0315  -0.0208 1030 ARG B CB  
16247 C CG  . ARG B 1032 ? 0.3073 0.4082 0.3421 -0.0015 0.0339  -0.0190 1030 ARG B CG  
16248 C CD  . ARG B 1032 ? 0.2876 0.3864 0.3261 -0.0041 0.0328  -0.0142 1030 ARG B CD  
16249 N NE  . ARG B 1032 ? 0.3235 0.4265 0.3699 -0.0056 0.0344  -0.0127 1030 ARG B NE  
16250 C CZ  . ARG B 1032 ? 0.3464 0.4538 0.3951 -0.0081 0.0367  -0.0081 1030 ARG B CZ  
16251 N NH1 . ARG B 1032 ? 0.3620 0.4695 0.4052 -0.0092 0.0377  -0.0045 1030 ARG B NH1 
16252 N NH2 . ARG B 1032 ? 0.3469 0.4588 0.4036 -0.0096 0.0380  -0.0069 1030 ARG B NH2 
16253 N N   . LEU B 1033 ? 0.2684 0.3710 0.2785 0.0013  0.0350  -0.0225 1031 LEU B N   
16254 C CA  . LEU B 1033 ? 0.2717 0.3785 0.2765 0.0028  0.0379  -0.0249 1031 LEU B CA  
16255 C C   . LEU B 1033 ? 0.2913 0.4002 0.2880 0.0020  0.0387  -0.0222 1031 LEU B C   
16256 O O   . LEU B 1033 ? 0.2776 0.3887 0.2674 0.0034  0.0404  -0.0248 1031 LEU B O   
16257 C CB  . LEU B 1033 ? 0.2581 0.3617 0.2603 0.0049  0.0362  -0.0307 1031 LEU B CB  
16258 C CG  . LEU B 1033 ? 0.2820 0.3831 0.2920 0.0057  0.0349  -0.0329 1031 LEU B CG  
16259 C CD1 . LEU B 1033 ? 0.3010 0.3976 0.3083 0.0074  0.0325  -0.0381 1031 LEU B CD1 
16260 C CD2 . LEU B 1033 ? 0.2678 0.3744 0.2844 0.0064  0.0384  -0.0325 1031 LEU B CD2 
16261 N N   . VAL B 1034 ? 0.2584 0.3660 0.2552 0.0000  0.0374  -0.0174 1032 VAL B N   
16262 C CA  . VAL B 1034 ? 0.2932 0.4024 0.2828 -0.0009 0.0377  -0.0138 1032 VAL B CA  
16263 C C   . VAL B 1034 ? 0.3128 0.4234 0.3063 -0.0031 0.0390  -0.0077 1032 VAL B C   
16264 O O   . VAL B 1034 ? 0.3146 0.4234 0.3160 -0.0040 0.0385  -0.0065 1032 VAL B O   
16265 C CB  . VAL B 1034 ? 0.3126 0.4178 0.2976 -0.0010 0.0333  -0.0140 1032 VAL B CB  
16266 C CG1 . VAL B 1034 ? 0.2981 0.4021 0.2773 0.0005  0.0320  -0.0194 1032 VAL B CG1 
16267 C CG2 . VAL B 1034 ? 0.2524 0.3530 0.2440 -0.0013 0.0302  -0.0131 1032 VAL B CG2 
16268 N N   . THR B 1035 ? 0.3080 0.4214 0.2957 -0.0042 0.0404  -0.0037 1033 THR B N   
16269 C CA  . THR B 1035 ? 0.3598 0.4743 0.3509 -0.0067 0.0418  0.0026  1033 THR B CA  
16270 C C   . THR B 1035 ? 0.3779 0.4865 0.3704 -0.0076 0.0377  0.0063  1033 THR B C   
16271 O O   . THR B 1035 ? 0.4021 0.5092 0.3992 -0.0096 0.0377  0.0108  1033 THR B O   
16272 C CB  . THR B 1035 ? 0.3966 0.5169 0.3810 -0.0077 0.0454  0.0060  1033 THR B CB  
16273 O OG1 . THR B 1035 ? 0.4108 0.5305 0.3852 -0.0064 0.0439  0.0046  1033 THR B OG1 
16274 C CG2 . THR B 1035 ? 0.4236 0.5510 0.4096 -0.0069 0.0505  0.0037  1033 THR B CG2 
16275 N N   . THR B 1036 ? 0.3664 0.4716 0.3551 -0.0062 0.0342  0.0045  1034 THR B N   
16276 C CA  . THR B 1036 ? 0.3513 0.4511 0.3423 -0.0060 0.0303  0.0068  1034 THR B CA  
16277 C C   . THR B 1036 ? 0.3463 0.4433 0.3396 -0.0042 0.0277  0.0018  1034 THR B C   
16278 O O   . THR B 1036 ? 0.3137 0.4119 0.3022 -0.0032 0.0266  -0.0013 1034 THR B O   
16279 C CB  . THR B 1036 ? 0.3967 0.4962 0.3808 -0.0061 0.0284  0.0106  1034 THR B CB  
16280 O OG1 . THR B 1036 ? 0.4621 0.5645 0.4429 -0.0080 0.0310  0.0154  1034 THR B OG1 
16281 C CG2 . THR B 1036 ? 0.3982 0.4924 0.3856 -0.0053 0.0245  0.0131  1034 THR B CG2 
16282 N N   . ALA B 1037 ? 0.3289 0.4221 0.3290 -0.0040 0.0264  0.0011  1035 ALA B N   
16283 C CA  . ALA B 1037 ? 0.3090 0.4000 0.3113 -0.0024 0.0244  -0.0033 1035 ALA B CA  
16284 C C   . ALA B 1037 ? 0.3492 0.4386 0.3491 -0.0012 0.0211  -0.0025 1035 ALA B C   
16285 O O   . ALA B 1037 ? 0.3652 0.4527 0.3653 -0.0010 0.0197  0.0014  1035 ALA B O   
16286 C CB  . ALA B 1037 ? 0.3124 0.3998 0.3219 -0.0024 0.0240  -0.0042 1035 ALA B CB  
16287 N N   . PRO B 1038 ? 0.2674 0.3577 0.2654 -0.0005 0.0196  -0.0060 1036 PRO B N   
16288 C CA  . PRO B 1038 ? 0.3065 0.3964 0.3040 0.0006  0.0165  -0.0052 1036 PRO B CA  
16289 C C   . PRO B 1038 ? 0.3083 0.3947 0.3115 0.0019  0.0153  -0.0055 1036 PRO B C   
16290 O O   . PRO B 1038 ? 0.2614 0.3453 0.2686 0.0018  0.0164  -0.0068 1036 PRO B O   
16291 C CB  . PRO B 1038 ? 0.2832 0.3752 0.2775 0.0003  0.0155  -0.0091 1036 PRO B CB  
16292 C CG  . PRO B 1038 ? 0.3130 0.4040 0.3092 0.0000  0.0176  -0.0130 1036 PRO B CG  
16293 C CD  . PRO B 1038 ? 0.2928 0.3842 0.2900 -0.0005 0.0206  -0.0109 1036 PRO B CD  
16294 N N   . VAL B 1039 ? 0.3113 0.3982 0.3148 0.0033  0.0129  -0.0044 1037 VAL B N   
16295 C CA  . VAL B 1039 ? 0.2440 0.3286 0.2520 0.0050  0.0118  -0.0053 1037 VAL B CA  
16296 C C   . VAL B 1039 ? 0.2542 0.3404 0.2629 0.0046  0.0114  -0.0092 1037 VAL B C   
16297 O O   . VAL B 1039 ? 0.2523 0.3420 0.2588 0.0040  0.0100  -0.0096 1037 VAL B O   
16298 C CB  . VAL B 1039 ? 0.3295 0.4148 0.3380 0.0072  0.0097  -0.0022 1037 VAL B CB  
16299 C CG1 . VAL B 1039 ? 0.2912 0.3748 0.3038 0.0096  0.0089  -0.0035 1037 VAL B CG1 
16300 C CG2 . VAL B 1039 ? 0.3160 0.3988 0.3233 0.0075  0.0096  0.0019  1037 VAL B CG2 
16301 N N   . PRO B 1040 ? 0.2563 0.3397 0.2677 0.0045  0.0122  -0.0119 1038 PRO B N   
16302 C CA  . PRO B 1040 ? 0.2692 0.3534 0.2808 0.0038  0.0117  -0.0152 1038 PRO B CA  
16303 C C   . PRO B 1040 ? 0.2584 0.3447 0.2713 0.0048  0.0099  -0.0147 1038 PRO B C   
16304 O O   . PRO B 1040 ? 0.2768 0.3631 0.2915 0.0068  0.0095  -0.0125 1038 PRO B O   
16305 C CB  . PRO B 1040 ? 0.2784 0.3586 0.2929 0.0039  0.0127  -0.0174 1038 PRO B CB  
16306 C CG  . PRO B 1040 ? 0.2642 0.3426 0.2797 0.0038  0.0141  -0.0155 1038 PRO B CG  
16307 C CD  . PRO B 1040 ? 0.2816 0.3608 0.2959 0.0047  0.0134  -0.0118 1038 PRO B CD  
16308 N N   . PRO B 1041 ? 0.2536 0.3420 0.2660 0.0035  0.0089  -0.0166 1039 PRO B N   
16309 C CA  . PRO B 1041 ? 0.2800 0.3714 0.2946 0.0041  0.0076  -0.0158 1039 PRO B CA  
16310 C C   . PRO B 1041 ? 0.2864 0.3752 0.3041 0.0063  0.0085  -0.0160 1039 PRO B C   
16311 O O   . PRO B 1041 ? 0.2793 0.3637 0.2974 0.0063  0.0094  -0.0179 1039 PRO B O   
16312 C CB  . PRO B 1041 ? 0.2909 0.3830 0.3044 0.0015  0.0065  -0.0182 1039 PRO B CB  
16313 C CG  . PRO B 1041 ? 0.2768 0.3672 0.2864 0.0000  0.0066  -0.0198 1039 PRO B CG  
16314 C CD  . PRO B 1041 ? 0.3022 0.3898 0.3120 0.0013  0.0088  -0.0195 1039 PRO B CD  
16315 N N   . GLN B 1042 ? 0.2565 0.3483 0.2761 0.0086  0.0081  -0.0140 1040 GLN B N   
16316 C CA  . GLN B 1042 ? 0.3169 0.4068 0.3386 0.0112  0.0088  -0.0144 1040 GLN B CA  
16317 C C   . GLN B 1042 ? 0.2773 0.3606 0.2989 0.0129  0.0096  -0.0147 1040 GLN B C   
16318 O O   . GLN B 1042 ? 0.2299 0.3098 0.2522 0.0148  0.0099  -0.0158 1040 GLN B O   
16319 C CB  . GLN B 1042 ? 0.3234 0.4130 0.3454 0.0099  0.0091  -0.0166 1040 GLN B CB  
16320 C CG  . GLN B 1042 ? 0.3282 0.4236 0.3506 0.0075  0.0081  -0.0161 1040 GLN B CG  
16321 C CD  . GLN B 1042 ? 0.4302 0.5250 0.4529 0.0065  0.0083  -0.0175 1040 GLN B CD  
16322 O OE1 . GLN B 1042 ? 0.4789 0.5693 0.5002 0.0046  0.0081  -0.0197 1040 GLN B OE1 
16323 N NE2 . GLN B 1042 ? 0.4942 0.5937 0.5190 0.0080  0.0089  -0.0162 1040 GLN B NE2 
16324 N N   . HIS B 1043 ? 0.2252 0.3066 0.2456 0.0120  0.0096  -0.0136 1041 HIS B N   
16325 C CA  . HIS B 1043 ? 0.2592 0.3344 0.2800 0.0126  0.0101  -0.0135 1041 HIS B CA  
16326 C C   . HIS B 1043 ? 0.2776 0.3507 0.2987 0.0155  0.0094  -0.0110 1041 HIS B C   
16327 O O   . HIS B 1043 ? 0.3031 0.3767 0.3232 0.0153  0.0090  -0.0083 1041 HIS B O   
16328 C CB  . HIS B 1043 ? 0.2394 0.3141 0.2591 0.0098  0.0108  -0.0135 1041 HIS B CB  
16329 C CG  . HIS B 1043 ? 0.3081 0.3776 0.3289 0.0095  0.0113  -0.0129 1041 HIS B CG  
16330 N ND1 . HIS B 1043 ? 0.2520 0.3182 0.2745 0.0086  0.0116  -0.0152 1041 HIS B ND1 
16331 C CD2 . HIS B 1043 ? 0.2940 0.3610 0.3147 0.0097  0.0111  -0.0100 1041 HIS B CD2 
16332 C CE1 . HIS B 1043 ? 0.2865 0.3490 0.3104 0.0080  0.0117  -0.0137 1041 HIS B CE1 
16333 N NE2 . HIS B 1043 ? 0.2877 0.3503 0.3104 0.0086  0.0114  -0.0105 1041 HIS B NE2 
16334 N N   . SER B 1044 ? 0.2421 0.3124 0.2641 0.0185  0.0091  -0.0118 1042 SER B N   
16335 C CA  . SER B 1044 ? 0.2629 0.3298 0.2850 0.0220  0.0082  -0.0100 1042 SER B CA  
16336 C C   . SER B 1044 ? 0.2779 0.3402 0.3000 0.0250  0.0081  -0.0123 1042 SER B C   
16337 O O   . SER B 1044 ? 0.2991 0.3627 0.3212 0.0244  0.0088  -0.0148 1042 SER B O   
16338 C CB  . SER B 1044 ? 0.2423 0.3155 0.2649 0.0241  0.0076  -0.0076 1042 SER B CB  
16339 O OG  . SER B 1044 ? 0.2811 0.3591 0.3050 0.0261  0.0082  -0.0090 1042 SER B OG  
16340 N N   . SER B 1045 ? 0.2411 0.2978 0.2628 0.0283  0.0070  -0.0115 1043 SER B N   
16341 C CA  . SER B 1045 ? 0.2213 0.2724 0.2419 0.0317  0.0067  -0.0140 1043 SER B CA  
16342 C C   . SER B 1045 ? 0.2405 0.2888 0.2606 0.0368  0.0056  -0.0127 1043 SER B C   
16343 O O   . SER B 1045 ? 0.2691 0.3148 0.2895 0.0368  0.0043  -0.0099 1043 SER B O   
16344 C CB  . SER B 1045 ? 0.2464 0.2889 0.2662 0.0295  0.0057  -0.0155 1043 SER B CB  
16345 O OG  . SER B 1045 ? 0.2673 0.3035 0.2851 0.0327  0.0049  -0.0182 1043 SER B OG  
16346 N N   . VAL B 1046 ? 0.2329 0.2815 0.2522 0.0414  0.0062  -0.0147 1044 VAL B N   
16347 C CA  . VAL B 1046 ? 0.2980 0.3433 0.3167 0.0473  0.0052  -0.0141 1044 VAL B CA  
16348 C C   . VAL B 1046 ? 0.2577 0.2902 0.2735 0.0492  0.0032  -0.0160 1044 VAL B C   
16349 O O   . VAL B 1046 ? 0.3173 0.3445 0.3320 0.0541  0.0018  -0.0157 1044 VAL B O   
16350 C CB  . VAL B 1046 ? 0.2536 0.3062 0.2729 0.0524  0.0070  -0.0153 1044 VAL B CB  
16351 C CG1 . VAL B 1046 ? 0.3240 0.3895 0.3470 0.0508  0.0082  -0.0128 1044 VAL B CG1 
16352 C CG2 . VAL B 1046 ? 0.2984 0.3500 0.3154 0.0526  0.0084  -0.0190 1044 VAL B CG2 
16353 N N   . HIS B 1047 ? 0.2859 0.3128 0.3005 0.0454  0.0026  -0.0178 1045 HIS B N   
16354 C CA  A HIS B 1047 ? 0.2914 0.3059 0.3032 0.0466  0.0002  -0.0196 1045 HIS B CA  
16355 C CA  B HIS B 1047 ? 0.2917 0.3060 0.3035 0.0462  0.0002  -0.0197 1045 HIS B CA  
16356 C C   . HIS B 1047 ? 0.2875 0.2955 0.3004 0.0431  -0.0021 -0.0165 1045 HIS B C   
16357 O O   . HIS B 1047 ? 0.3159 0.3288 0.3313 0.0383  -0.0013 -0.0139 1045 HIS B O   
16358 C CB  A HIS B 1047 ? 0.2979 0.3099 0.3079 0.0445  0.0003  -0.0231 1045 HIS B CB  
16359 C CB  B HIS B 1047 ? 0.2939 0.3062 0.3046 0.0429  0.0003  -0.0227 1045 HIS B CB  
16360 C CG  A HIS B 1047 ? 0.2913 0.3104 0.3000 0.0473  0.0028  -0.0254 1045 HIS B CG  
16361 C CG  B HIS B 1047 ? 0.2997 0.3000 0.3089 0.0412  -0.0028 -0.0238 1045 HIS B CG  
16362 N ND1 A HIS B 1047 ? 0.3058 0.3234 0.3114 0.0536  0.0033  -0.0276 1045 HIS B ND1 
16363 N ND1 B HIS B 1047 ? 0.2949 0.2850 0.3000 0.0454  -0.0051 -0.0265 1045 HIS B ND1 
16364 C CD2 A HIS B 1047 ? 0.2783 0.3064 0.2884 0.0445  0.0050  -0.0256 1045 HIS B CD2 
16365 C CD2 B HIS B 1047 ? 0.2997 0.2970 0.3111 0.0356  -0.0042 -0.0227 1045 HIS B CD2 
16366 C CE1 A HIS B 1047 ? 0.2703 0.2964 0.2756 0.0543  0.0060  -0.0287 1045 HIS B CE1 
16367 C CE1 B HIS B 1047 ? 0.3414 0.3222 0.3463 0.0420  -0.0081 -0.0268 1045 HIS B CE1 
16368 N NE2 A HIS B 1047 ? 0.2849 0.3170 0.2929 0.0487  0.0068  -0.0275 1045 HIS B NE2 
16369 N NE2 B HIS B 1047 ? 0.2610 0.2466 0.2702 0.0360  -0.0074 -0.0244 1045 HIS B NE2 
16370 N N   . THR B 1048 ? 0.2790 0.2760 0.2898 0.0459  -0.0049 -0.0166 1046 THR B N   
16371 C CA  . THR B 1048 ? 0.2830 0.2723 0.2945 0.0425  -0.0075 -0.0134 1046 THR B CA  
16372 C C   . THR B 1048 ? 0.2712 0.2490 0.2809 0.0409  -0.0103 -0.0159 1046 THR B C   
16373 O O   . THR B 1048 ? 0.3126 0.2831 0.3187 0.0455  -0.0117 -0.0195 1046 THR B O   
16374 C CB  . THR B 1048 ? 0.3544 0.3391 0.3650 0.0467  -0.0093 -0.0107 1046 THR B CB  
16375 O OG1 . THR B 1048 ? 0.3438 0.3395 0.3560 0.0495  -0.0071 -0.0092 1046 THR B OG1 
16376 C CG2 . THR B 1048 ? 0.3619 0.3415 0.3738 0.0420  -0.0114 -0.0059 1046 THR B CG2 
16377 N N   . ASP B 1049 ? 0.2736 0.2501 0.2858 0.0346  -0.0110 -0.0140 1047 ASP B N   
16378 C CA  . ASP B 1049 ? 0.2883 0.2546 0.2998 0.0323  -0.0141 -0.0160 1047 ASP B CA  
16379 C C   . ASP B 1049 ? 0.3036 0.2563 0.3118 0.0356  -0.0181 -0.0159 1047 ASP B C   
16380 O O   . ASP B 1049 ? 0.3318 0.2821 0.3406 0.0358  -0.0191 -0.0119 1047 ASP B O   
16381 C CB  . ASP B 1049 ? 0.3031 0.2718 0.3191 0.0249  -0.0142 -0.0130 1047 ASP B CB  
16382 C CG  . ASP B 1049 ? 0.3186 0.2783 0.3349 0.0217  -0.0176 -0.0147 1047 ASP B CG  
16383 O OD1 . ASP B 1049 ? 0.3614 0.3104 0.3770 0.0209  -0.0212 -0.0130 1047 ASP B OD1 
16384 O OD2 . ASP B 1049 ? 0.3368 0.2999 0.3540 0.0201  -0.0169 -0.0176 1047 ASP B OD2 
16385 N N   . PRO B 1050 ? 0.2834 0.2264 0.2875 0.0387  -0.0207 -0.0202 1048 PRO B N   
16386 C CA  . PRO B 1050 ? 0.3539 0.2828 0.3542 0.0426  -0.0248 -0.0206 1048 PRO B CA  
16387 C C   . PRO B 1050 ? 0.3608 0.2796 0.3629 0.0369  -0.0289 -0.0171 1048 PRO B C   
16388 O O   . PRO B 1050 ? 0.3688 0.2777 0.3690 0.0390  -0.0319 -0.0151 1048 PRO B O   
16389 C CB  . PRO B 1050 ? 0.3520 0.2741 0.3467 0.0470  -0.0261 -0.0269 1048 PRO B CB  
16390 C CG  . PRO B 1050 ? 0.3720 0.3008 0.3685 0.0425  -0.0246 -0.0286 1048 PRO B CG  
16391 C CD  . PRO B 1050 ? 0.3351 0.2792 0.3369 0.0394  -0.0201 -0.0251 1048 PRO B CD  
16392 N N   . VAL B 1051 ? 0.3457 0.2669 0.3517 0.0298  -0.0292 -0.0160 1049 VAL B N   
16393 C CA  . VAL B 1051 ? 0.3811 0.2946 0.3900 0.0236  -0.0328 -0.0120 1049 VAL B CA  
16394 C C   . VAL B 1051 ? 0.3552 0.2744 0.3673 0.0211  -0.0309 -0.0056 1049 VAL B C   
16395 O O   . VAL B 1051 ? 0.3759 0.2860 0.3879 0.0193  -0.0342 -0.0016 1049 VAL B O   
16396 C CB  . VAL B 1051 ? 0.3539 0.2702 0.3669 0.0170  -0.0333 -0.0125 1049 VAL B CB  
16397 C CG1 . VAL B 1051 ? 0.3622 0.2720 0.3792 0.0101  -0.0368 -0.0077 1049 VAL B CG1 
16398 C CG2 . VAL B 1051 ? 0.3728 0.2822 0.3816 0.0196  -0.0358 -0.0188 1049 VAL B CG2 
16399 N N   . LEU B 1052 ? 0.3587 0.2924 0.3731 0.0210  -0.0260 -0.0043 1050 LEU B N   
16400 C CA  . LEU B 1052 ? 0.3329 0.2723 0.3489 0.0197  -0.0242 0.0013  1050 LEU B CA  
16401 C C   . LEU B 1052 ? 0.3814 0.3122 0.3936 0.0253  -0.0267 0.0026  1050 LEU B C   
16402 O O   . LEU B 1052 ? 0.3314 0.2580 0.3440 0.0232  -0.0284 0.0078  1050 LEU B O   
16403 C CB  . LEU B 1052 ? 0.2961 0.2513 0.3137 0.0202  -0.0191 0.0011  1050 LEU B CB  
16404 C CG  . LEU B 1052 ? 0.2949 0.2584 0.3133 0.0193  -0.0167 0.0061  1050 LEU B CG  
16405 C CD1 . LEU B 1052 ? 0.3305 0.2924 0.3458 0.0258  -0.0173 0.0066  1050 LEU B CD1 
16406 C CD2 . LEU B 1052 ? 0.2887 0.2496 0.3094 0.0130  -0.0178 0.0120  1050 LEU B CD2 
16407 N N   . LEU B 1053 ? 0.3379 0.2666 0.3464 0.0327  -0.0267 -0.0020 1051 LEU B N   
16408 C CA  . LEU B 1053 ? 0.3784 0.2989 0.3834 0.0391  -0.0291 -0.0014 1051 LEU B CA  
16409 C C   . LEU B 1053 ? 0.3993 0.3024 0.4023 0.0377  -0.0348 0.0000  1051 LEU B C   
16410 O O   . LEU B 1053 ? 0.4066 0.3034 0.4088 0.0388  -0.0371 0.0042  1051 LEU B O   
16411 C CB  . LEU B 1053 ? 0.4024 0.3240 0.4041 0.0473  -0.0279 -0.0072 1051 LEU B CB  
16412 C CG  . LEU B 1053 ? 0.3924 0.3307 0.3961 0.0496  -0.0228 -0.0077 1051 LEU B CG  
16413 C CD1 . LEU B 1053 ? 0.4103 0.3509 0.4111 0.0564  -0.0212 -0.0134 1051 LEU B CD1 
16414 C CD2 . LEU B 1053 ? 0.3700 0.3132 0.3750 0.0515  -0.0223 -0.0030 1051 LEU B CD2 
16415 N N   . ASP B 1054 ? 0.4034 0.2982 0.4055 0.0353  -0.0374 -0.0033 1052 ASP B N   
16416 C CA  . ASP B 1054 ? 0.4063 0.2837 0.4065 0.0333  -0.0434 -0.0021 1052 ASP B CA  
16417 C C   . ASP B 1054 ? 0.3951 0.2726 0.3995 0.0254  -0.0444 0.0055  1052 ASP B C   
16418 O O   . ASP B 1054 ? 0.3886 0.2539 0.3916 0.0249  -0.0487 0.0091  1052 ASP B O   
16419 C CB  . ASP B 1054 ? 0.4513 0.3212 0.4501 0.0313  -0.0462 -0.0070 1052 ASP B CB  
16420 C CG  . ASP B 1054 ? 0.4890 0.3550 0.4819 0.0395  -0.0463 -0.0144 1052 ASP B CG  
16421 O OD1 . ASP B 1054 ? 0.4625 0.3270 0.4519 0.0473  -0.0456 -0.0155 1052 ASP B OD1 
16422 O OD2 . ASP B 1054 ? 0.5184 0.3831 0.5099 0.0384  -0.0469 -0.0189 1052 ASP B OD2 
16423 N N   . PHE B 1055 ? 0.4152 0.3064 0.4248 0.0192  -0.0405 0.0080  1053 PHE B N   
16424 C CA  . PHE B 1055 ? 0.3634 0.2573 0.3770 0.0118  -0.0403 0.0153  1053 PHE B CA  
16425 C C   . PHE B 1055 ? 0.4328 0.3281 0.4447 0.0144  -0.0396 0.0202  1053 PHE B C   
16426 O O   . PHE B 1055 ? 0.4002 0.2881 0.4122 0.0108  -0.0425 0.0261  1053 PHE B O   
16427 C CB  . PHE B 1055 ? 0.3642 0.2739 0.3831 0.0062  -0.0355 0.0160  1053 PHE B CB  
16428 C CG  . PHE B 1055 ? 0.3527 0.2666 0.3758 -0.0016 -0.0347 0.0231  1053 PHE B CG  
16429 C CD1 . PHE B 1055 ? 0.3687 0.2723 0.3938 -0.0074 -0.0390 0.0268  1053 PHE B CD1 
16430 C CD2 . PHE B 1055 ? 0.3622 0.2909 0.3872 -0.0033 -0.0295 0.0261  1053 PHE B CD2 
16431 C CE1 . PHE B 1055 ? 0.3896 0.2984 0.4188 -0.0148 -0.0377 0.0339  1053 PHE B CE1 
16432 C CE2 . PHE B 1055 ? 0.3440 0.2775 0.3723 -0.0102 -0.0282 0.0327  1053 PHE B CE2 
16433 C CZ  . PHE B 1055 ? 0.3646 0.2888 0.3953 -0.0159 -0.0320 0.0368  1053 PHE B CZ  
16434 N N   . ALA B 1056 ? 0.4022 0.3070 0.4127 0.0204  -0.0361 0.0182  1054 ALA B N   
16435 C CA  . ALA B 1056 ? 0.4118 0.3185 0.4207 0.0233  -0.0358 0.0227  1054 ALA B CA  
16436 C C   . ALA B 1056 ? 0.4063 0.2962 0.4114 0.0276  -0.0413 0.0239  1054 ALA B C   
16437 O O   . ALA B 1056 ? 0.4343 0.3205 0.4387 0.0264  -0.0431 0.0301  1054 ALA B O   
16438 C CB  . ALA B 1056 ? 0.4242 0.3435 0.4326 0.0293  -0.0318 0.0197  1054 ALA B CB  
16439 N N   . LYS B 1057 ? 0.4184 0.2978 0.4205 0.0330  -0.0441 0.0181  1055 LYS B N   
16440 C CA  . LYS B 1057 ? 0.4703 0.3326 0.4683 0.0378  -0.0496 0.0186  1055 LYS B CA  
16441 C C   . LYS B 1057 ? 0.4611 0.3099 0.4595 0.0305  -0.0545 0.0235  1055 LYS B C   
16442 O O   . LYS B 1057 ? 0.5026 0.3407 0.4990 0.0313  -0.0584 0.0281  1055 LYS B O   
16443 C CB  . LYS B 1057 ? 0.4889 0.3428 0.4829 0.0454  -0.0513 0.0107  1055 LYS B CB  
16444 C CG  . LYS B 1057 ? 0.4885 0.3534 0.4816 0.0539  -0.0472 0.0066  1055 LYS B CG  
16445 C CD  . LYS B 1057 ? 0.5005 0.3568 0.4889 0.0615  -0.0487 -0.0011 1055 LYS B CD  
16446 C CE  . LYS B 1057 ? 0.4739 0.3301 0.4621 0.0571  -0.0483 -0.0056 1055 LYS B CE  
16447 N NZ  . LYS B 1057 ? 0.5005 0.3512 0.4833 0.0651  -0.0487 -0.0134 1055 LYS B NZ  
16448 N N   . TRP B 1058 ? 0.4425 0.2916 0.4437 0.0234  -0.0547 0.0227  1056 TRP B N   
16449 C CA  . TRP B 1058 ? 0.4510 0.2901 0.4541 0.0150  -0.0589 0.0280  1056 TRP B CA  
16450 C C   . TRP B 1058 ? 0.4495 0.2950 0.4549 0.0099  -0.0572 0.0369  1056 TRP B C   
16451 O O   . TRP B 1058 ? 0.4873 0.3209 0.4916 0.0070  -0.0616 0.0426  1056 TRP B O   
16452 C CB  . TRP B 1058 ? 0.4484 0.2915 0.4555 0.0082  -0.0582 0.0258  1056 TRP B CB  
16453 C CG  . TRP B 1058 ? 0.5093 0.3439 0.5197 -0.0011 -0.0624 0.0312  1056 TRP B CG  
16454 C CD1 . TRP B 1058 ? 0.5210 0.3365 0.5290 -0.0024 -0.0695 0.0309  1056 TRP B CD1 
16455 C CD2 . TRP B 1058 ? 0.4897 0.3350 0.5063 -0.0104 -0.0597 0.0376  1056 TRP B CD2 
16456 N NE1 . TRP B 1058 ? 0.5527 0.3665 0.5657 -0.0126 -0.0716 0.0371  1056 TRP B NE1 
16457 C CE2 . TRP B 1058 ? 0.5370 0.3696 0.5556 -0.0175 -0.0654 0.0414  1056 TRP B CE2 
16458 C CE3 . TRP B 1058 ? 0.4912 0.3557 0.5120 -0.0134 -0.0530 0.0404  1056 TRP B CE3 
16459 C CZ2 . TRP B 1058 ? 0.5088 0.3484 0.5338 -0.0275 -0.0642 0.0483  1056 TRP B CZ2 
16460 C CZ3 . TRP B 1058 ? 0.5180 0.3890 0.5445 -0.0228 -0.0518 0.0468  1056 TRP B CZ3 
16461 C CH2 . TRP B 1058 ? 0.4992 0.3585 0.5281 -0.0297 -0.0571 0.0508  1056 TRP B CH2 
16462 N N   . LEU B 1059 ? 0.4479 0.3118 0.4559 0.0087  -0.0510 0.0382  1057 LEU B N   
16463 C CA  . LEU B 1059 ? 0.4675 0.3382 0.4766 0.0044  -0.0491 0.0463  1057 LEU B CA  
16464 C C   . LEU B 1059 ? 0.5279 0.3907 0.5326 0.0102  -0.0520 0.0496  1057 LEU B C   
16465 O O   . LEU B 1059 ? 0.5575 0.4152 0.5615 0.0061  -0.0542 0.0571  1057 LEU B O   
16466 C CB  . LEU B 1059 ? 0.4008 0.2920 0.4125 0.0032  -0.0422 0.0459  1057 LEU B CB  
16467 C CG  . LEU B 1059 ? 0.4240 0.3243 0.4407 -0.0029 -0.0391 0.0438  1057 LEU B CG  
16468 C CD1 . LEU B 1059 ? 0.3995 0.3182 0.4174 -0.0022 -0.0328 0.0423  1057 LEU B CD1 
16469 C CD2 . LEU B 1059 ? 0.4261 0.3241 0.4463 -0.0124 -0.0404 0.0506  1057 LEU B CD2 
16470 N N   . ASP B 1060 ? 0.4979 0.3602 0.4998 0.0196  -0.0520 0.0442  1058 ASP B N   
16471 C CA  . ASP B 1060 ? 0.5372 0.3913 0.5353 0.0262  -0.0553 0.0467  1058 ASP B CA  
16472 C C   . ASP B 1060 ? 0.5523 0.3848 0.5477 0.0253  -0.0624 0.0492  1058 ASP B C   
16473 O O   . ASP B 1060 ? 0.5703 0.3954 0.5636 0.0256  -0.0655 0.0554  1058 ASP B O   
16474 C CB  . ASP B 1060 ? 0.5680 0.4250 0.5643 0.0368  -0.0541 0.0397  1058 ASP B CB  
16475 C CG  . ASP B 1060 ? 0.5552 0.4322 0.5536 0.0386  -0.0482 0.0392  1058 ASP B CG  
16476 O OD1 . ASP B 1060 ? 0.6360 0.5210 0.6351 0.0348  -0.0465 0.0452  1058 ASP B OD1 
16477 O OD2 . ASP B 1060 ? 0.5824 0.4666 0.5813 0.0437  -0.0454 0.0327  1058 ASP B OD2 
16478 N N   . GLY B 1061 ? 0.5339 0.3557 0.5290 0.0244  -0.0653 0.0444  1059 GLY B N   
16479 C CA  . GLY B 1061 ? 0.6282 0.4283 0.6205 0.0233  -0.0726 0.0462  1059 GLY B CA  
16480 C C   . GLY B 1061 ? 0.6221 0.4186 0.6164 0.0133  -0.0747 0.0557  1059 GLY B C   
16481 O O   . GLY B 1061 ? 0.6398 0.4206 0.6313 0.0131  -0.0803 0.0604  1059 GLY B O   
16482 N N   . LYS B 1062 ? 0.6021 0.4132 0.6013 0.0049  -0.0701 0.0587  1060 LYS B N   
16483 C CA  . LYS B 1062 ? 0.6353 0.4459 0.6371 -0.0053 -0.0709 0.0679  1060 LYS B CA  
16484 C C   . LYS B 1062 ? 0.6527 0.4699 0.6528 -0.0055 -0.0689 0.0755  1060 LYS B C   
16485 O O   . LYS B 1062 ? 0.6678 0.4833 0.6689 -0.0133 -0.0699 0.0840  1060 LYS B O   
16486 C CB  . LYS B 1062 ? 0.6081 0.4331 0.6160 -0.0135 -0.0662 0.0679  1060 LYS B CB  
16487 C CG  . LYS B 1062 ? 0.6096 0.4279 0.6199 -0.0158 -0.0689 0.0623  1060 LYS B CG  
16488 C CD  . LYS B 1062 ? 0.5762 0.4128 0.5924 -0.0207 -0.0630 0.0605  1060 LYS B CD  
16489 C CE  . LYS B 1062 ? 0.6070 0.4559 0.6272 -0.0289 -0.0590 0.0691  1060 LYS B CE  
16490 N NZ  . LYS B 1062 ? 0.5742 0.4137 0.5975 -0.0382 -0.0634 0.0759  1060 LYS B NZ  
16491 N N   . GLY B 1063 ? 0.6093 0.4345 0.6070 0.0027  -0.0662 0.0729  1061 GLY B N   
16492 C CA  . GLY B 1063 ? 0.5889 0.4224 0.5849 0.0026  -0.0641 0.0796  1061 GLY B CA  
16493 C C   . GLY B 1063 ? 0.6056 0.4600 0.6045 -0.0026 -0.0570 0.0814  1061 GLY B C   
16494 O O   . GLY B 1063 ? 0.6010 0.4630 0.5980 -0.0037 -0.0551 0.0873  1061 GLY B O   
16495 N N   . ALA B 1064 ? 0.5586 0.4223 0.5617 -0.0055 -0.0532 0.0764  1062 ALA B N   
16496 C CA  . ALA B 1064 ? 0.5079 0.3911 0.5137 -0.0098 -0.0464 0.0771  1062 ALA B CA  
16497 C C   . ALA B 1064 ? 0.5127 0.4078 0.5168 -0.0024 -0.0427 0.0724  1062 ALA B C   
16498 O O   . ALA B 1064 ? 0.4668 0.3707 0.4730 0.0000  -0.0394 0.0656  1062 ALA B O   
16499 C CB  . ALA B 1064 ? 0.4886 0.3764 0.4997 -0.0151 -0.0443 0.0734  1062 ALA B CB  
16500 N N   . ARG B 1065 ? 0.5423 0.4378 0.5426 0.0010  -0.0436 0.0767  1063 ARG B N   
16501 C CA  . ARG B 1065 ? 0.5245 0.4285 0.5233 0.0090  -0.0418 0.0725  1063 ARG B CA  
16502 C C   . ARG B 1065 ? 0.4967 0.4197 0.4969 0.0070  -0.0354 0.0705  1063 ARG B C   
16503 O O   . ARG B 1065 ? 0.4929 0.4235 0.4944 0.0118  -0.0331 0.0639  1063 ARG B O   
16504 C CB  . ARG B 1065 ? 0.5137 0.4130 0.5082 0.0129  -0.0450 0.0781  1063 ARG B CB  
16505 N N   . ALA B 1066 ? 0.4954 0.4262 0.4953 0.0000  -0.0325 0.0761  1064 ALA B N   
16506 C CA  . ALA B 1066 ? 0.4669 0.4147 0.4676 -0.0018 -0.0266 0.0739  1064 ALA B CA  
16507 C C   . ALA B 1066 ? 0.4497 0.4022 0.4550 -0.0026 -0.0239 0.0668  1064 ALA B C   
16508 O O   . ALA B 1066 ? 0.4317 0.3954 0.4377 -0.0002 -0.0204 0.0618  1064 ALA B O   
16509 C CB  . ALA B 1066 ? 0.4509 0.4053 0.4502 -0.0092 -0.0239 0.0810  1064 ALA B CB  
16510 N N   . GLU B 1067 ? 0.4183 0.3620 0.4267 -0.0062 -0.0259 0.0664  1065 GLU B N   
16511 C CA  . GLU B 1067 ? 0.4348 0.3819 0.4475 -0.0071 -0.0239 0.0600  1065 GLU B CA  
16512 C C   . GLU B 1067 ? 0.4066 0.3498 0.4188 0.0005  -0.0255 0.0525  1065 GLU B C   
16513 O O   . GLU B 1067 ? 0.4252 0.3768 0.4392 0.0020  -0.0224 0.0467  1065 GLU B O   
16514 C CB  . GLU B 1067 ? 0.4093 0.3480 0.4255 -0.0135 -0.0262 0.0623  1065 GLU B CB  
16515 C CG  . GLU B 1067 ? 0.4230 0.3688 0.4412 -0.0218 -0.0235 0.0692  1065 GLU B CG  
16516 C CD  . GLU B 1067 ? 0.4936 0.4342 0.5078 -0.0238 -0.0255 0.0778  1065 GLU B CD  
16517 O OE1 . GLU B 1067 ? 0.4982 0.4276 0.5087 -0.0190 -0.0299 0.0785  1065 GLU B OE1 
16518 O OE2 . GLU B 1067 ? 0.4854 0.4332 0.5001 -0.0301 -0.0226 0.0839  1065 GLU B OE2 
16519 N N   . ALA B 1068 ? 0.4496 0.3799 0.4592 0.0054  -0.0302 0.0526  1066 ALA B N   
16520 C CA  . ALA B 1068 ? 0.4603 0.3879 0.4691 0.0134  -0.0312 0.0458  1066 ALA B CA  
16521 C C   . ALA B 1068 ? 0.4093 0.3510 0.4176 0.0176  -0.0274 0.0433  1066 ALA B C   
16522 O O   . ALA B 1068 ? 0.4392 0.3863 0.4487 0.0209  -0.0254 0.0370  1066 ALA B O   
16523 C CB  . ALA B 1068 ? 0.4562 0.3684 0.4618 0.0186  -0.0367 0.0469  1066 ALA B CB  
16524 N N   . GLU B 1069 ? 0.4241 0.3720 0.4306 0.0172  -0.0265 0.0483  1067 GLU B N   
16525 C CA  . GLU B 1069 ? 0.4360 0.3975 0.4421 0.0202  -0.0232 0.0464  1067 GLU B CA  
16526 C C   . GLU B 1069 ? 0.4321 0.4056 0.4405 0.0161  -0.0185 0.0430  1067 GLU B C   
16527 O O   . GLU B 1069 ? 0.4144 0.3960 0.4238 0.0193  -0.0163 0.0381  1067 GLU B O   
16528 C CB  . GLU B 1069 ? 0.4877 0.4527 0.4907 0.0196  -0.0238 0.0529  1067 GLU B CB  
16529 C CG  . GLU B 1069 ? 0.5182 0.4975 0.5206 0.0215  -0.0209 0.0517  1067 GLU B CG  
16530 C CD  . GLU B 1069 ? 0.5915 0.5719 0.5944 0.0296  -0.0225 0.0485  1067 GLU B CD  
16531 O OE1 . GLU B 1069 ? 0.5859 0.5556 0.5890 0.0343  -0.0258 0.0476  1067 GLU B OE1 
16532 O OE2 . GLU B 1069 ? 0.6095 0.6017 0.6127 0.0312  -0.0205 0.0469  1067 GLU B OE2 
16533 N N   . ALA B 1070 ? 0.4203 0.3951 0.4299 0.0092  -0.0169 0.0458  1068 ALA B N   
16534 C CA  . ALA B 1070 ? 0.4066 0.3925 0.4187 0.0058  -0.0125 0.0426  1068 ALA B CA  
16535 C C   . ALA B 1070 ? 0.3397 0.3235 0.3546 0.0077  -0.0124 0.0358  1068 ALA B C   
16536 O O   . ALA B 1070 ? 0.3707 0.3635 0.3868 0.0084  -0.0094 0.0314  1068 ALA B O   
16537 C CB  . ALA B 1070 ? 0.4125 0.4005 0.4258 -0.0016 -0.0107 0.0472  1068 ALA B CB  
16538 N N   . ALA B 1071 ? 0.3471 0.3185 0.3626 0.0086  -0.0161 0.0349  1069 ALA B N   
16539 C CA  . ALA B 1071 ? 0.3264 0.2949 0.3435 0.0107  -0.0165 0.0285  1069 ALA B CA  
16540 C C   . ALA B 1071 ? 0.3571 0.3293 0.3727 0.0178  -0.0158 0.0237  1069 ALA B C   
16541 O O   . ALA B 1071 ? 0.3301 0.3080 0.3470 0.0188  -0.0136 0.0187  1069 ALA B O   
16542 C CB  . ALA B 1071 ? 0.3423 0.2955 0.3593 0.0105  -0.0211 0.0285  1069 ALA B CB  
16543 N N   . ARG B 1072 ? 0.3221 0.2914 0.3352 0.0228  -0.0176 0.0255  1070 ARG B N   
16544 C CA  . ARG B 1072 ? 0.3045 0.2788 0.3171 0.0294  -0.0167 0.0214  1070 ARG B CA  
16545 C C   . ARG B 1072 ? 0.3475 0.3368 0.3612 0.0281  -0.0127 0.0207  1070 ARG B C   
16546 O O   . ARG B 1072 ? 0.3180 0.3134 0.3326 0.0306  -0.0108 0.0161  1070 ARG B O   
16547 C CB  . ARG B 1072 ? 0.4281 0.3968 0.4386 0.0353  -0.0197 0.0238  1070 ARG B CB  
16548 C CG  . ARG B 1072 ? 0.4764 0.4312 0.4855 0.0399  -0.0232 0.0210  1070 ARG B CG  
16549 C CD  . ARG B 1072 ? 0.4651 0.4155 0.4725 0.0471  -0.0259 0.0224  1070 ARG B CD  
16550 N NE  . ARG B 1072 ? 0.5134 0.4494 0.5187 0.0462  -0.0304 0.0267  1070 ARG B NE  
16551 C CZ  . ARG B 1072 ? 0.5435 0.4790 0.5481 0.0433  -0.0317 0.0333  1070 ARG B CZ  
16552 N NH1 . ARG B 1072 ? 0.5181 0.4665 0.5234 0.0416  -0.0290 0.0363  1070 ARG B NH1 
16553 N NH2 . ARG B 1072 ? 0.5386 0.4598 0.5413 0.0420  -0.0360 0.0372  1070 ARG B NH2 
16554 N N   . ASN B 1073 ? 0.3399 0.3349 0.3531 0.0239  -0.0115 0.0252  1071 ASN B N   
16555 C CA  . ASN B 1073 ? 0.3265 0.3346 0.3399 0.0224  -0.0081 0.0243  1071 ASN B CA  
16556 C C   . ASN B 1073 ? 0.3306 0.3429 0.3462 0.0192  -0.0054 0.0201  1071 ASN B C   
16557 O O   . ASN B 1073 ? 0.3162 0.3370 0.3323 0.0200  -0.0032 0.0168  1071 ASN B O   
16558 C CB  . ASN B 1073 ? 0.3651 0.3773 0.3764 0.0187  -0.0075 0.0299  1071 ASN B CB  
16559 C CG  . ASN B 1073 ? 0.4185 0.4295 0.4274 0.0225  -0.0101 0.0337  1071 ASN B CG  
16560 O OD1 . ASN B 1073 ? 0.4780 0.4899 0.4876 0.0281  -0.0112 0.0315  1071 ASN B OD1 
16561 N ND2 . ASN B 1073 ? 0.4964 0.5059 0.5027 0.0196  -0.0109 0.0396  1071 ASN B ND2 
16562 N N   . ALA B 1074 ? 0.3452 0.3517 0.3623 0.0154  -0.0058 0.0203  1072 ALA B N   
16563 C CA  . ALA B 1074 ? 0.3147 0.3247 0.3343 0.0128  -0.0037 0.0163  1072 ALA B CA  
16564 C C   . ALA B 1074 ? 0.3091 0.3169 0.3290 0.0170  -0.0043 0.0108  1072 ALA B C   
16565 O O   . ALA B 1074 ? 0.2648 0.2790 0.2857 0.0167  -0.0021 0.0071  1072 ALA B O   
16566 C CB  . ALA B 1074 ? 0.3160 0.3204 0.3379 0.0077  -0.0045 0.0182  1072 ALA B CB  
16567 N N   . GLY B 1075 ? 0.3153 0.3136 0.3339 0.0210  -0.0073 0.0101  1073 GLY B N   
16568 C CA  . GLY B 1075 ? 0.3297 0.3258 0.3477 0.0255  -0.0076 0.0049  1073 GLY B CA  
16569 C C   . GLY B 1075 ? 0.3685 0.3747 0.3863 0.0290  -0.0053 0.0030  1073 GLY B C   
16570 O O   . GLY B 1075 ? 0.3565 0.3660 0.3745 0.0303  -0.0040 -0.0011 1073 GLY B O   
16571 N N   . SER B 1076 ? 0.3028 0.3144 0.3202 0.0301  -0.0050 0.0064  1074 SER B N   
16572 C CA  . SER B 1076 ? 0.3233 0.3452 0.3411 0.0328  -0.0032 0.0050  1074 SER B CA  
16573 C C   . SER B 1076 ? 0.3514 0.3827 0.3702 0.0284  -0.0005 0.0041  1074 SER B C   
16574 O O   . SER B 1076 ? 0.3842 0.4216 0.4037 0.0294  0.0010  0.0010  1074 SER B O   
16575 C CB  . SER B 1076 ? 0.3713 0.3957 0.3885 0.0358  -0.0045 0.0088  1074 SER B CB  
16576 O OG  . SER B 1076 ? 0.3883 0.4051 0.4049 0.0415  -0.0068 0.0086  1074 SER B OG  
16577 N N   . SER B 1077 ? 0.3172 0.3496 0.3357 0.0236  0.0002  0.0068  1075 SER B N   
16578 C CA  . SER B 1077 ? 0.3391 0.3803 0.3578 0.0202  0.0026  0.0057  1075 SER B CA  
16579 C C   . SER B 1077 ? 0.3173 0.3580 0.3377 0.0178  0.0040  0.0020  1075 SER B C   
16580 O O   . SER B 1077 ? 0.3437 0.3910 0.3644 0.0160  0.0058  0.0001  1075 SER B O   
16581 C CB  . SER B 1077 ? 0.4050 0.4490 0.4222 0.0165  0.0033  0.0098  1075 SER B CB  
16582 O OG  . SER B 1077 ? 0.3834 0.4223 0.4014 0.0131  0.0034  0.0114  1075 SER B OG  
16583 N N   . SER B 1078 ? 0.2811 0.3136 0.3024 0.0179  0.0026  0.0009  1076 SER B N   
16584 C CA  . SER B 1078 ? 0.2970 0.3287 0.3199 0.0163  0.0033  -0.0028 1076 SER B CA  
16585 C C   . SER B 1078 ? 0.2935 0.3301 0.3160 0.0187  0.0043  -0.0064 1076 SER B C   
16586 O O   . SER B 1078 ? 0.3123 0.3494 0.3337 0.0227  0.0038  -0.0069 1076 SER B O   
16587 C CB  . SER B 1078 ? 0.2530 0.2743 0.2763 0.0168  0.0008  -0.0037 1076 SER B CB  
16588 O OG  . SER B 1078 ? 0.2500 0.2705 0.2745 0.0158  0.0010  -0.0074 1076 SER B OG  
16589 N N   . ALA B 1079 ? 0.2655 0.3061 0.2891 0.0162  0.0058  -0.0088 1077 ALA B N   
16590 C CA  . ALA B 1079 ? 0.2596 0.3040 0.2828 0.0177  0.0066  -0.0120 1077 ALA B CA  
16591 C C   . ALA B 1079 ? 0.2781 0.3170 0.3013 0.0183  0.0057  -0.0152 1077 ALA B C   
16592 O O   . ALA B 1079 ? 0.2510 0.2927 0.2738 0.0188  0.0064  -0.0178 1077 ALA B O   
16593 C CB  . ALA B 1079 ? 0.2891 0.3409 0.3126 0.0150  0.0083  -0.0126 1077 ALA B CB  
16594 N N   . LEU B 1080 ? 0.2609 0.2920 0.2845 0.0179  0.0039  -0.0149 1078 LEU B N   
16595 C CA  . LEU B 1080 ? 0.2502 0.2749 0.2732 0.0188  0.0023  -0.0180 1078 LEU B CA  
16596 C C   . LEU B 1080 ? 0.2824 0.3069 0.3023 0.0234  0.0025  -0.0203 1078 LEU B C   
16597 O O   . LEU B 1080 ? 0.2678 0.2919 0.2863 0.0270  0.0023  -0.0193 1078 LEU B O   
16598 C CB  . LEU B 1080 ? 0.2694 0.2848 0.2926 0.0183  -0.0003 -0.0168 1078 LEU B CB  
16599 C CG  . LEU B 1080 ? 0.2766 0.2837 0.2981 0.0195  -0.0028 -0.0200 1078 LEU B CG  
16600 C CD1 . LEU B 1080 ? 0.2398 0.2485 0.2636 0.0161  -0.0029 -0.0219 1078 LEU B CD1 
16601 C CD2 . LEU B 1080 ? 0.2469 0.2434 0.2677 0.0198  -0.0060 -0.0188 1078 LEU B CD2 
16602 N N   . GLY B 1081 ? 0.2442 0.2695 0.2632 0.0233  0.0028  -0.0233 1079 GLY B N   
16603 C CA  . GLY B 1081 ? 0.2690 0.2952 0.2849 0.0272  0.0034  -0.0254 1079 GLY B CA  
16604 C C   . GLY B 1081 ? 0.3122 0.3482 0.3287 0.0273  0.0058  -0.0249 1079 GLY B C   
16605 O O   . GLY B 1081 ? 0.2357 0.2741 0.2501 0.0303  0.0067  -0.0261 1079 GLY B O   
16606 N N   . LEU B 1082 ? 0.2830 0.3248 0.3019 0.0240  0.0067  -0.0230 1080 LEU B N   
16607 C CA  . LEU B 1082 ? 0.2927 0.3428 0.3121 0.0230  0.0083  -0.0228 1080 LEU B CA  
16608 C C   . LEU B 1082 ? 0.2987 0.3485 0.3167 0.0225  0.0085  -0.0254 1080 LEU B C   
16609 O O   . LEU B 1082 ? 0.2819 0.3269 0.2998 0.0208  0.0074  -0.0270 1080 LEU B O   
16610 C CB  . LEU B 1082 ? 0.2496 0.3035 0.2709 0.0192  0.0088  -0.0214 1080 LEU B CB  
16611 C CG  . LEU B 1082 ? 0.2465 0.3077 0.2681 0.0173  0.0097  -0.0214 1080 LEU B CG  
16612 C CD1 . LEU B 1082 ? 0.3334 0.4000 0.3548 0.0199  0.0102  -0.0202 1080 LEU B CD1 
16613 C CD2 . LEU B 1082 ? 0.2377 0.3019 0.2601 0.0145  0.0100  -0.0200 1080 LEU B CD2 
16614 N N   . ASP B 1083 ? 0.2658 0.3212 0.2830 0.0236  0.0097  -0.0254 1081 ASP B N   
16615 C CA  . ASP B 1083 ? 0.2722 0.3272 0.2873 0.0232  0.0099  -0.0273 1081 ASP B CA  
16616 C C   . ASP B 1083 ? 0.3173 0.3806 0.3332 0.0220  0.0112  -0.0260 1081 ASP B C   
16617 O O   . ASP B 1083 ? 0.3186 0.3867 0.3342 0.0246  0.0124  -0.0251 1081 ASP B O   
16618 C CB  . ASP B 1083 ? 0.3422 0.3927 0.3540 0.0273  0.0097  -0.0289 1081 ASP B CB  
16619 C CG  . ASP B 1083 ? 0.4542 0.5041 0.4629 0.0271  0.0099  -0.0306 1081 ASP B CG  
16620 O OD1 . ASP B 1083 ? 0.4784 0.5291 0.4878 0.0235  0.0094  -0.0308 1081 ASP B OD1 
16621 O OD2 . ASP B 1083 ? 0.5031 0.5518 0.5083 0.0307  0.0106  -0.0317 1081 ASP B OD2 
16622 N N   . LEU B 1084 ? 0.3037 0.3686 0.3205 0.0181  0.0108  -0.0261 1082 LEU B N   
16623 C CA  . LEU B 1084 ? 0.2856 0.3575 0.3034 0.0160  0.0113  -0.0247 1082 LEU B CA  
16624 C C   . LEU B 1084 ? 0.3309 0.4021 0.3471 0.0138  0.0110  -0.0256 1082 LEU B C   
16625 O O   . LEU B 1084 ? 0.2866 0.3520 0.3017 0.0129  0.0099  -0.0274 1082 LEU B O   
16626 C CB  . LEU B 1084 ? 0.2737 0.3474 0.2933 0.0132  0.0107  -0.0239 1082 LEU B CB  
16627 C CG  . LEU B 1084 ? 0.3087 0.3843 0.3295 0.0148  0.0109  -0.0222 1082 LEU B CG  
16628 C CD1 . LEU B 1084 ? 0.3326 0.4099 0.3540 0.0119  0.0104  -0.0216 1082 LEU B CD1 
16629 C CD2 . LEU B 1084 ? 0.4021 0.4841 0.4239 0.0172  0.0117  -0.0203 1082 LEU B CD2 
16630 N N   . GLU B 1085 ? 0.2726 0.3498 0.2889 0.0128  0.0117  -0.0241 1083 GLU B N   
16631 C CA  . GLU B 1085 ? 0.3091 0.3859 0.3242 0.0096  0.0109  -0.0242 1083 GLU B CA  
16632 C C   . GLU B 1085 ? 0.3032 0.3825 0.3201 0.0059  0.0097  -0.0235 1083 GLU B C   
16633 O O   . GLU B 1085 ? 0.3477 0.4331 0.3665 0.0055  0.0101  -0.0217 1083 GLU B O   
16634 C CB  . GLU B 1085 ? 0.2914 0.3727 0.3051 0.0100  0.0122  -0.0228 1083 GLU B CB  
16635 C CG  . GLU B 1085 ? 0.3555 0.4361 0.3680 0.0060  0.0110  -0.0223 1083 GLU B CG  
16636 C CD  . GLU B 1085 ? 0.3891 0.4718 0.3988 0.0064  0.0123  -0.0211 1083 GLU B CD  
16637 O OE1 . GLU B 1085 ? 0.4072 0.4924 0.4157 0.0102  0.0143  -0.0210 1083 GLU B OE1 
16638 O OE2 . GLU B 1085 ? 0.4095 0.4909 0.4178 0.0030  0.0111  -0.0202 1083 GLU B OE2 
16639 N N   . LEU B 1086 ? 0.2931 0.3675 0.3091 0.0035  0.0082  -0.0250 1084 LEU B N   
16640 C CA  . LEU B 1086 ? 0.3077 0.3826 0.3243 0.0004  0.0068  -0.0252 1084 LEU B CA  
16641 C C   . LEU B 1086 ? 0.3259 0.4023 0.3417 -0.0029 0.0056  -0.0239 1084 LEU B C   
16642 O O   . LEU B 1086 ? 0.3157 0.3897 0.3298 -0.0033 0.0054  -0.0238 1084 LEU B O   
16643 C CB  . LEU B 1086 ? 0.2958 0.3644 0.3120 0.0001  0.0058  -0.0277 1084 LEU B CB  
16644 C CG  . LEU B 1086 ? 0.2908 0.3579 0.3082 0.0025  0.0068  -0.0285 1084 LEU B CG  
16645 C CD1 . LEU B 1086 ? 0.3153 0.3784 0.3332 0.0019  0.0061  -0.0307 1084 LEU B CD1 
16646 C CD2 . LEU B 1086 ? 0.3324 0.4044 0.3508 0.0032  0.0077  -0.0268 1084 LEU B CD2 
16647 N N   . PRO B 1087 ? 0.3147 0.3950 0.3314 -0.0056 0.0046  -0.0228 1085 PRO B N   
16648 C CA  . PRO B 1087 ? 0.3073 0.3882 0.3235 -0.0095 0.0028  -0.0215 1085 PRO B CA  
16649 C C   . PRO B 1087 ? 0.2874 0.3599 0.3011 -0.0109 0.0009  -0.0236 1085 PRO B C   
16650 O O   . PRO B 1087 ? 0.3577 0.4255 0.3708 -0.0099 0.0003  -0.0263 1085 PRO B O   
16651 C CB  . PRO B 1087 ? 0.3438 0.4285 0.3610 -0.0119 0.0013  -0.0208 1085 PRO B CB  
16652 C CG  . PRO B 1087 ? 0.3122 0.4011 0.3311 -0.0089 0.0029  -0.0205 1085 PRO B CG  
16653 C CD  . PRO B 1087 ? 0.3260 0.4102 0.3442 -0.0052 0.0046  -0.0223 1085 PRO B CD  
16654 N N   . GLY B 1088 ? 0.2690 0.3402 0.2815 -0.0132 -0.0001 -0.0222 1086 GLY B N   
16655 C CA  . GLY B 1088 ? 0.3075 0.3706 0.3176 -0.0145 -0.0023 -0.0238 1086 GLY B CA  
16656 C C   . GLY B 1088 ? 0.2991 0.3621 0.3078 -0.0178 -0.0036 -0.0210 1086 GLY B C   
16657 O O   . GLY B 1088 ? 0.2726 0.3424 0.2827 -0.0201 -0.0030 -0.0179 1086 GLY B O   
16658 N N   . PRO B 1089 ? 0.2937 0.3493 0.2999 -0.0183 -0.0053 -0.0219 1087 PRO B N   
16659 C CA  . PRO B 1089 ? 0.2864 0.3409 0.2907 -0.0218 -0.0068 -0.0188 1087 PRO B CA  
16660 C C   . PRO B 1089 ? 0.2978 0.3580 0.3014 -0.0208 -0.0039 -0.0161 1087 PRO B C   
16661 O O   . PRO B 1089 ? 0.2607 0.3226 0.2642 -0.0167 -0.0015 -0.0174 1087 PRO B O   
16662 C CB  . PRO B 1089 ? 0.3163 0.3606 0.3180 -0.0215 -0.0095 -0.0209 1087 PRO B CB  
16663 C CG  . PRO B 1089 ? 0.3416 0.3843 0.3442 -0.0167 -0.0080 -0.0243 1087 PRO B CG  
16664 C CD  . PRO B 1089 ? 0.3175 0.3659 0.3229 -0.0154 -0.0061 -0.0253 1087 PRO B CD  
16665 N N   . VAL B 1090 ? 0.2807 0.3436 0.2834 -0.0247 -0.0044 -0.0123 1088 VAL B N   
16666 C CA  . VAL B 1090 ? 0.2566 0.3243 0.2575 -0.0238 -0.0017 -0.0096 1088 VAL B CA  
16667 C C   . VAL B 1090 ? 0.3033 0.3631 0.2997 -0.0214 -0.0024 -0.0113 1088 VAL B C   
16668 O O   . VAL B 1090 ? 0.2568 0.3077 0.2521 -0.0215 -0.0054 -0.0136 1088 VAL B O   
16669 C CB  . VAL B 1090 ? 0.2834 0.3559 0.2842 -0.0290 -0.0020 -0.0046 1088 VAL B CB  
16670 C CG1 . VAL B 1090 ? 0.2383 0.3190 0.2442 -0.0318 -0.0019 -0.0028 1088 VAL B CG1 
16671 C CG2 . VAL B 1090 ? 0.2839 0.3470 0.2815 -0.0330 -0.0060 -0.0035 1088 VAL B CG2 
16672 N N   . GLY B 1091 ? 0.2589 0.3221 0.2528 -0.0189 0.0004  -0.0103 1089 GLY B N   
16673 C CA  . GLY B 1091 ? 0.2889 0.3449 0.2779 -0.0168 -0.0006 -0.0117 1089 GLY B CA  
16674 C C   . GLY B 1091 ? 0.3148 0.3657 0.3045 -0.0126 -0.0012 -0.0162 1089 GLY B C   
16675 O O   . GLY B 1091 ? 0.2791 0.3232 0.2657 -0.0112 -0.0029 -0.0177 1089 GLY B O   
16676 N N   . GLU B 1092 ? 0.2875 0.3417 0.2815 -0.0108 0.0001  -0.0181 1090 GLU B N   
16677 C CA  . GLU B 1092 ? 0.3054 0.3557 0.3008 -0.0073 -0.0002 -0.0218 1090 GLU B CA  
16678 C C   . GLU B 1092 ? 0.3014 0.3583 0.2994 -0.0047 0.0028  -0.0222 1090 GLU B C   
16679 O O   . GLU B 1092 ? 0.2815 0.3453 0.2820 -0.0061 0.0042  -0.0202 1090 GLU B O   
16680 C CB  . GLU B 1092 ? 0.2948 0.3403 0.2929 -0.0086 -0.0028 -0.0239 1090 GLU B CB  
16681 C CG  . GLU B 1092 ? 0.3581 0.3969 0.3565 -0.0063 -0.0046 -0.0270 1090 GLU B CG  
16682 C CD  . GLU B 1092 ? 0.3901 0.4247 0.3909 -0.0073 -0.0070 -0.0288 1090 GLU B CD  
16683 O OE1 . GLU B 1092 ? 0.3360 0.3735 0.3394 -0.0077 -0.0061 -0.0295 1090 GLU B OE1 
16684 O OE2 . GLU B 1092 ? 0.4456 0.4739 0.4452 -0.0075 -0.0097 -0.0296 1090 GLU B OE2 
16685 N N   . ARG B 1093 ? 0.3109 0.3656 0.3086 -0.0010 0.0034  -0.0246 1091 ARG B N   
16686 C CA  . ARG B 1093 ? 0.2638 0.3228 0.2640 0.0018  0.0056  -0.0252 1091 ARG B CA  
16687 C C   . ARG B 1093 ? 0.3027 0.3571 0.3055 0.0028  0.0043  -0.0279 1091 ARG B C   
16688 O O   . ARG B 1093 ? 0.2667 0.3152 0.2684 0.0040  0.0028  -0.0298 1091 ARG B O   
16689 C CB  . ARG B 1093 ? 0.3047 0.3650 0.3017 0.0055  0.0077  -0.0253 1091 ARG B CB  
16690 C CG  . ARG B 1093 ? 0.4573 0.5231 0.4569 0.0084  0.0101  -0.0252 1091 ARG B CG  
16691 C CD  . ARG B 1093 ? 0.5029 0.5684 0.4987 0.0129  0.0118  -0.0262 1091 ARG B CD  
16692 N NE  . ARG B 1093 ? 0.4953 0.5617 0.4861 0.0128  0.0127  -0.0251 1091 ARG B NE  
16693 C CZ  . ARG B 1093 ? 0.6051 0.6655 0.5903 0.0148  0.0119  -0.0269 1091 ARG B CZ  
16694 N NH1 . ARG B 1093 ? 0.5897 0.6425 0.5741 0.0167  0.0100  -0.0300 1091 ARG B NH1 
16695 N NH2 . ARG B 1093 ? 0.6108 0.6728 0.5909 0.0145  0.0130  -0.0255 1091 ARG B NH2 
16696 N N   . ASN B 1094 ? 0.2945 0.3520 0.3009 0.0022  0.0048  -0.0278 1092 ASN B N   
16697 C CA  . ASN B 1094 ? 0.2704 0.3248 0.2795 0.0026  0.0039  -0.0298 1092 ASN B CA  
16698 C C   . ASN B 1094 ? 0.2546 0.3119 0.2655 0.0050  0.0057  -0.0297 1092 ASN B C   
16699 O O   . ASN B 1094 ? 0.2665 0.3294 0.2785 0.0049  0.0069  -0.0281 1092 ASN B O   
16700 C CB  . ASN B 1094 ? 0.2553 0.3098 0.2659 -0.0002 0.0027  -0.0300 1092 ASN B CB  
16701 C CG  . ASN B 1094 ? 0.2504 0.2998 0.2593 -0.0020 0.0003  -0.0306 1092 ASN B CG  
16702 O OD1 . ASN B 1094 ? 0.2544 0.2989 0.2637 -0.0010 -0.0010 -0.0324 1092 ASN B OD1 
16703 N ND2 . ASN B 1094 ? 0.2790 0.3294 0.2863 -0.0047 -0.0004 -0.0287 1092 ASN B ND2 
16704 N N   . LEU B 1095 ? 0.2400 0.2932 0.2511 0.0071  0.0054  -0.0313 1093 LEU B N   
16705 C CA  . LEU B 1095 ? 0.2683 0.3223 0.2803 0.0097  0.0066  -0.0312 1093 LEU B CA  
16706 C C   . LEU B 1095 ? 0.2233 0.2755 0.2384 0.0093  0.0061  -0.0319 1093 LEU B C   
16707 O O   . LEU B 1095 ? 0.2434 0.2923 0.2597 0.0081  0.0048  -0.0332 1093 LEU B O   
16708 C CB  . LEU B 1095 ? 0.2820 0.3320 0.2909 0.0124  0.0063  -0.0322 1093 LEU B CB  
16709 C CG  . LEU B 1095 ? 0.3017 0.3538 0.3067 0.0130  0.0072  -0.0314 1093 LEU B CG  
16710 C CD1 . LEU B 1095 ? 0.3981 0.4457 0.3988 0.0162  0.0070  -0.0329 1093 LEU B CD1 
16711 C CD2 . LEU B 1095 ? 0.3312 0.3912 0.3372 0.0134  0.0094  -0.0291 1093 LEU B CD2 
16712 N N   . TYR B 1096 ? 0.2110 0.2655 0.2275 0.0104  0.0072  -0.0308 1094 TYR B N   
16713 C CA  . TYR B 1096 ? 0.2230 0.2766 0.2422 0.0099  0.0072  -0.0308 1094 TYR B CA  
16714 C C   . TYR B 1096 ? 0.2242 0.2762 0.2434 0.0123  0.0075  -0.0300 1094 TYR B C   
16715 O O   . TYR B 1096 ? 0.2104 0.2655 0.2288 0.0140  0.0085  -0.0286 1094 TYR B O   
16716 C CB  . TYR B 1096 ? 0.2033 0.2616 0.2235 0.0081  0.0079  -0.0299 1094 TYR B CB  
16717 C CG  . TYR B 1096 ? 0.2272 0.2859 0.2494 0.0076  0.0085  -0.0294 1094 TYR B CG  
16718 C CD1 . TYR B 1096 ? 0.2303 0.2876 0.2542 0.0063  0.0082  -0.0307 1094 TYR B CD1 
16719 C CD2 . TYR B 1096 ? 0.2780 0.3390 0.3003 0.0086  0.0093  -0.0274 1094 TYR B CD2 
16720 C CE1 . TYR B 1096 ? 0.2323 0.2909 0.2579 0.0058  0.0092  -0.0299 1094 TYR B CE1 
16721 C CE2 . TYR B 1096 ? 0.2487 0.3103 0.2723 0.0078  0.0099  -0.0265 1094 TYR B CE2 
16722 C CZ  . TYR B 1096 ? 0.2368 0.2974 0.2619 0.0063  0.0100  -0.0277 1094 TYR B CZ  
16723 O OH  . TYR B 1096 ? 0.2428 0.3049 0.2691 0.0055  0.0111  -0.0265 1094 TYR B OH  
16724 N N   . THR B 1097 ? 0.2512 0.2983 0.2715 0.0124  0.0065  -0.0307 1095 THR B N   
16725 C CA  . THR B 1097 ? 0.2604 0.3040 0.2803 0.0146  0.0061  -0.0302 1095 THR B CA  
16726 C C   . THR B 1097 ? 0.2330 0.2745 0.2560 0.0130  0.0056  -0.0293 1095 THR B C   
16727 O O   . THR B 1097 ? 0.2416 0.2833 0.2671 0.0108  0.0052  -0.0299 1095 THR B O   
16728 C CB  . THR B 1097 ? 0.2755 0.3132 0.2924 0.0165  0.0046  -0.0321 1095 THR B CB  
16729 O OG1 . THR B 1097 ? 0.3221 0.3566 0.3402 0.0145  0.0029  -0.0336 1095 THR B OG1 
16730 C CG2 . THR B 1097 ? 0.2806 0.3209 0.2941 0.0182  0.0056  -0.0326 1095 THR B CG2 
16731 N N   . LEU B 1098 ? 0.2480 0.2879 0.2710 0.0143  0.0056  -0.0276 1096 LEU B N   
16732 C CA  . LEU B 1098 ? 0.2376 0.2756 0.2634 0.0125  0.0051  -0.0261 1096 LEU B CA  
16733 C C   . LEU B 1098 ? 0.2339 0.2639 0.2591 0.0136  0.0029  -0.0264 1096 LEU B C   
16734 O O   . LEU B 1098 ? 0.2538 0.2808 0.2763 0.0167  0.0024  -0.0264 1096 LEU B O   
16735 C CB  . LEU B 1098 ? 0.2393 0.2813 0.2655 0.0123  0.0065  -0.0232 1096 LEU B CB  
16736 C CG  . LEU B 1098 ? 0.2448 0.2940 0.2711 0.0109  0.0083  -0.0229 1096 LEU B CG  
16737 C CD1 . LEU B 1098 ? 0.2486 0.3008 0.2745 0.0109  0.0092  -0.0199 1096 LEU B CD1 
16738 C CD2 . LEU B 1098 ? 0.2053 0.2558 0.2340 0.0082  0.0087  -0.0240 1096 LEU B CD2 
16739 N N   . HIS B 1099 ? 0.2335 0.2604 0.2615 0.0112  0.0013  -0.0268 1097 HIS B N   
16740 C CA  . HIS B 1099 ? 0.2300 0.2486 0.2576 0.0114  -0.0016 -0.0274 1097 HIS B CA  
16741 C C   . HIS B 1099 ? 0.2506 0.2678 0.2823 0.0084  -0.0023 -0.0246 1097 HIS B C   
16742 O O   . HIS B 1099 ? 0.2740 0.2973 0.3089 0.0061  -0.0002 -0.0225 1097 HIS B O   
16743 C CB  . HIS B 1099 ? 0.2906 0.3062 0.3183 0.0107  -0.0037 -0.0302 1097 HIS B CB  
16744 C CG  . HIS B 1099 ? 0.2881 0.3048 0.3116 0.0131  -0.0031 -0.0326 1097 HIS B CG  
16745 N ND1 . HIS B 1099 ? 0.3107 0.3215 0.3292 0.0159  -0.0048 -0.0348 1097 HIS B ND1 
16746 C CD2 . HIS B 1099 ? 0.2862 0.3090 0.3094 0.0129  -0.0012 -0.0330 1097 HIS B CD2 
16747 C CE1 . HIS B 1099 ? 0.3396 0.3535 0.3550 0.0172  -0.0035 -0.0361 1097 HIS B CE1 
16748 N NE2 . HIS B 1099 ? 0.3127 0.3337 0.3311 0.0152  -0.0016 -0.0349 1097 HIS B NE2 
16749 N N   . ALA B 1100 ? 0.2621 0.2711 0.2935 0.0083  -0.0053 -0.0245 1098 ALA B N   
16750 C CA  . ALA B 1100 ? 0.2955 0.3028 0.3314 0.0046  -0.0065 -0.0216 1098 ALA B CA  
16751 C C   . ALA B 1100 ? 0.3103 0.3229 0.3517 0.0010  -0.0061 -0.0218 1098 ALA B C   
16752 O O   . ALA B 1100 ? 0.2864 0.3000 0.3277 0.0016  -0.0067 -0.0248 1098 ALA B O   
16753 C CB  . ALA B 1100 ? 0.3537 0.3499 0.3880 0.0048  -0.0106 -0.0220 1098 ALA B CB  
16754 N N   . ARG B 1101 ? 0.3104 0.3271 0.3569 -0.0024 -0.0050 -0.0185 1099 ARG B N   
16755 C CA  . ARG B 1101 ? 0.3412 0.3640 0.3937 -0.0054 -0.0043 -0.0185 1099 ARG B CA  
16756 C C   . ARG B 1101 ? 0.3356 0.3533 0.3922 -0.0081 -0.0083 -0.0187 1099 ARG B C   
16757 O O   . ARG B 1101 ? 0.3567 0.3764 0.4163 -0.0087 -0.0094 -0.0208 1099 ARG B O   
16758 C CB  . ARG B 1101 ? 0.3615 0.3923 0.4177 -0.0078 -0.0009 -0.0150 1099 ARG B CB  
16759 C CG  . ARG B 1101 ? 0.3596 0.3983 0.4141 -0.0061 0.0029  -0.0160 1099 ARG B CG  
16760 C CD  . ARG B 1101 ? 0.3804 0.4271 0.4381 -0.0084 0.0063  -0.0129 1099 ARG B CD  
16761 N NE  . ARG B 1101 ? 0.4520 0.5058 0.5149 -0.0094 0.0079  -0.0141 1099 ARG B NE  
16762 C CZ  . ARG B 1101 ? 0.4991 0.5587 0.5607 -0.0077 0.0104  -0.0163 1099 ARG B CZ  
16763 N NH1 . ARG B 1101 ? 0.4304 0.4897 0.4860 -0.0054 0.0115  -0.0174 1099 ARG B NH1 
16764 N NH2 . ARG B 1101 ? 0.4348 0.5006 0.5016 -0.0083 0.0118  -0.0172 1099 ARG B NH2 
16765 N N   . GLY B 1102 ? 0.3099 0.3206 0.3665 -0.0097 -0.0108 -0.0164 1100 GLY B N   
16766 C CA  . GLY B 1102 ? 0.3609 0.3668 0.4219 -0.0131 -0.0151 -0.0161 1100 GLY B CA  
16767 C C   . GLY B 1102 ? 0.3172 0.3191 0.3808 -0.0167 -0.0166 -0.0117 1100 GLY B C   
16768 O O   . GLY B 1102 ? 0.3098 0.3052 0.3685 -0.0151 -0.0171 -0.0105 1100 GLY B O   
16769 N N   . ARG B 1103 ? 0.2997 0.3052 0.3712 -0.0216 -0.0176 -0.0089 1101 ARG B N   
16770 C CA  . ARG B 1103 ? 0.2741 0.2773 0.3489 -0.0260 -0.0186 -0.0038 1101 ARG B CA  
16771 C C   . ARG B 1103 ? 0.2799 0.2952 0.3590 -0.0280 -0.0132 0.0003  1101 ARG B C   
16772 O O   . ARG B 1103 ? 0.3002 0.3260 0.3851 -0.0291 -0.0106 0.0000  1101 ARG B O   
16773 C CB  . ARG B 1103 ? 0.3022 0.3014 0.3833 -0.0309 -0.0236 -0.0028 1101 ARG B CB  
16774 C CG  . ARG B 1103 ? 0.3347 0.3282 0.4182 -0.0357 -0.0259 0.0026  1101 ARG B CG  
16775 C CD  . ARG B 1103 ? 0.3230 0.3098 0.4115 -0.0404 -0.0323 0.0029  1101 ARG B CD  
16776 N NE  . ARG B 1103 ? 0.4442 0.4189 0.5262 -0.0372 -0.0373 -0.0025 1101 ARG B NE  
16777 C CZ  . ARG B 1103 ? 0.4827 0.4426 0.5578 -0.0358 -0.0417 -0.0035 1101 ARG B CZ  
16778 N NH1 . ARG B 1103 ? 0.4258 0.3802 0.4996 -0.0374 -0.0420 0.0007  1101 ARG B NH1 
16779 N NH2 . ARG B 1103 ? 0.4674 0.4175 0.5365 -0.0327 -0.0460 -0.0089 1101 ARG B NH2 
16780 N N   . ILE B 1104 ? 0.2596 0.2734 0.3356 -0.0282 -0.0116 0.0039  1102 ILE B N   
16781 C CA  . ILE B 1104 ? 0.2979 0.3224 0.3759 -0.0297 -0.0064 0.0078  1102 ILE B CA  
16782 C C   . ILE B 1104 ? 0.2508 0.2766 0.3353 -0.0359 -0.0071 0.0138  1102 ILE B C   
16783 O O   . ILE B 1104 ? 0.2519 0.2673 0.3354 -0.0381 -0.0112 0.0163  1102 ILE B O   
16784 C CB  . ILE B 1104 ? 0.2622 0.2847 0.3324 -0.0261 -0.0043 0.0086  1102 ILE B CB  
16785 C CG1 . ILE B 1104 ? 0.2464 0.2669 0.3107 -0.0204 -0.0042 0.0029  1102 ILE B CG1 
16786 C CG2 . ILE B 1104 ? 0.2858 0.3195 0.3569 -0.0274 0.0011  0.0121  1102 ILE B CG2 
16787 C CD1 . ILE B 1104 ? 0.2592 0.2893 0.3254 -0.0190 -0.0011 -0.0004 1102 ILE B CD1 
16788 N N   . LEU B 1105 ? 0.2535 0.2918 0.3448 -0.0388 -0.0033 0.0162  1103 LEU B N   
16789 C CA  . LEU B 1105 ? 0.2754 0.3169 0.3732 -0.0450 -0.0032 0.0227  1103 LEU B CA  
16790 C C   . LEU B 1105 ? 0.2435 0.2849 0.3363 -0.0455 -0.0005 0.0276  1103 LEU B C   
16791 O O   . LEU B 1105 ? 0.2681 0.3175 0.3574 -0.0429 0.0045  0.0274  1103 LEU B O   
16792 C CB  . LEU B 1105 ? 0.2443 0.3005 0.3514 -0.0475 0.0004  0.0237  1103 LEU B CB  
16793 C CG  . LEU B 1105 ? 0.3025 0.3657 0.4170 -0.0540 0.0020  0.0310  1103 LEU B CG  
16794 C CD1 . LEU B 1105 ? 0.2787 0.3330 0.3985 -0.0594 -0.0044 0.0334  1103 LEU B CD1 
16795 C CD2 . LEU B 1105 ? 0.2830 0.3632 0.4058 -0.0547 0.0072  0.0313  1103 LEU B CD2 
16796 N N   . LEU B 1106 ? 0.2629 0.2948 0.3550 -0.0489 -0.0041 0.0320  1104 LEU B N   
16797 C CA  . LEU B 1106 ? 0.3110 0.3419 0.3985 -0.0500 -0.0022 0.0375  1104 LEU B CA  
16798 C C   . LEU B 1106 ? 0.2684 0.3066 0.3632 -0.0571 -0.0005 0.0448  1104 LEU B C   
16799 O O   . LEU B 1106 ? 0.2754 0.3096 0.3766 -0.0621 -0.0045 0.0472  1104 LEU B O   
16800 C CB  . LEU B 1106 ? 0.2612 0.2758 0.3422 -0.0485 -0.0075 0.0379  1104 LEU B CB  
16801 C CG  . LEU B 1106 ? 0.3351 0.3447 0.4069 -0.0415 -0.0072 0.0339  1104 LEU B CG  
16802 C CD1 . LEU B 1106 ? 0.3133 0.3286 0.3842 -0.0367 -0.0052 0.0269  1104 LEU B CD1 
16803 C CD2 . LEU B 1106 ? 0.2985 0.2912 0.3656 -0.0398 -0.0133 0.0334  1104 LEU B CD2 
16804 N N   . VAL B 1107 ? 0.2822 0.3312 0.3757 -0.0575 0.0052  0.0484  1105 VAL B N   
16805 C CA  . VAL B 1107 ? 0.3111 0.3680 0.4107 -0.0642 0.0076  0.0561  1105 VAL B CA  
16806 C C   . VAL B 1107 ? 0.3074 0.3608 0.3995 -0.0648 0.0088  0.0617  1105 VAL B C   
16807 O O   . VAL B 1107 ? 0.3117 0.3753 0.4004 -0.0637 0.0145  0.0634  1105 VAL B O   
16808 C CB  . VAL B 1107 ? 0.2954 0.3702 0.4011 -0.0645 0.0140  0.0555  1105 VAL B CB  
16809 C CG1 . VAL B 1107 ? 0.2719 0.3560 0.3861 -0.0720 0.0161  0.0635  1105 VAL B CG1 
16810 C CG2 . VAL B 1107 ? 0.2803 0.3572 0.3913 -0.0620 0.0125  0.0488  1105 VAL B CG2 
16811 N N   . PRO B 1108 ? 0.2767 0.3154 0.3655 -0.0663 0.0033  0.0646  1106 PRO B N   
16812 C CA  . PRO B 1108 ? 0.3475 0.3820 0.4292 -0.0670 0.0038  0.0705  1106 PRO B CA  
16813 C C   . PRO B 1108 ? 0.3258 0.3670 0.4122 -0.0746 0.0060  0.0796  1106 PRO B C   
16814 O O   . PRO B 1108 ? 0.3489 0.3946 0.4448 -0.0803 0.0055  0.0822  1106 PRO B O   
16815 C CB  . PRO B 1108 ? 0.3041 0.3196 0.3818 -0.0656 -0.0035 0.0697  1106 PRO B CB  
16816 C CG  . PRO B 1108 ? 0.3473 0.3586 0.4332 -0.0694 -0.0079 0.0680  1106 PRO B CG  
16817 C CD  . PRO B 1108 ? 0.3143 0.3386 0.4050 -0.0671 -0.0039 0.0623  1106 PRO B CD  
16818 N N   . ALA B 1109 ? 0.3173 0.3594 0.3969 -0.0747 0.0084  0.0848  1107 ALA B N   
16819 C CA  . ALA B 1109 ? 0.3645 0.4102 0.4460 -0.0818 0.0099  0.0946  1107 ALA B CA  
16820 C C   . ALA B 1109 ? 0.3623 0.3916 0.4385 -0.0837 0.0042  0.1000  1107 ALA B C   
16821 O O   . ALA B 1109 ? 0.3818 0.4075 0.4624 -0.0910 0.0019  0.1074  1107 ALA B O   
16822 C CB  . ALA B 1109 ? 0.3706 0.4314 0.4480 -0.0809 0.0176  0.0970  1107 ALA B CB  
16823 N N   . THR B 1110 ? 0.3541 0.3731 0.4214 -0.0773 0.0016  0.0966  1108 THR B N   
16824 C CA  . THR B 1110 ? 0.3812 0.3843 0.4425 -0.0775 -0.0039 0.1011  1108 THR B CA  
16825 C C   . THR B 1110 ? 0.3943 0.3819 0.4530 -0.0718 -0.0102 0.0942  1108 THR B C   
16826 O O   . THR B 1110 ? 0.3585 0.3488 0.4177 -0.0665 -0.0094 0.0859  1108 THR B O   
16827 C CB  . THR B 1110 ? 0.3836 0.3895 0.4353 -0.0744 -0.0010 0.1044  1108 THR B CB  
16828 O OG1 . THR B 1110 ? 0.3928 0.4015 0.4394 -0.0662 0.0006  0.0964  1108 THR B OG1 
16829 C CG2 . THR B 1110 ? 0.4163 0.4380 0.4688 -0.0793 0.0057  0.1107  1108 THR B CG2 
16830 N N   . GLU B 1111 ? 0.3981 0.3691 0.4536 -0.0727 -0.0164 0.0979  1109 GLU B N   
16831 C CA  . GLU B 1111 ? 0.4248 0.3802 0.4769 -0.0668 -0.0223 0.0917  1109 GLU B CA  
16832 C C   . GLU B 1111 ? 0.3907 0.3490 0.4360 -0.0577 -0.0201 0.0856  1109 GLU B C   
16833 O O   . GLU B 1111 ? 0.3828 0.3390 0.4279 -0.0523 -0.0211 0.0775  1109 GLU B O   
16834 C CB  . GLU B 1111 ? 0.4261 0.3630 0.4749 -0.0687 -0.0292 0.0971  1109 GLU B CB  
16835 C CG  . GLU B 1111 ? 0.4276 0.3483 0.4714 -0.0612 -0.0349 0.0906  1109 GLU B CG  
16836 C CD  . GLU B 1111 ? 0.4988 0.3996 0.5394 -0.0627 -0.0423 0.0954  1109 GLU B CD  
16837 O OE1 . GLU B 1111 ? 0.4929 0.3835 0.5376 -0.0676 -0.0473 0.0961  1109 GLU B OE1 
16838 O OE2 . GLU B 1111 ? 0.5637 0.4587 0.5977 -0.0590 -0.0435 0.0984  1109 GLU B OE2 
16839 N N   . SER B 1112 ? 0.3830 0.3463 0.4225 -0.0561 -0.0172 0.0896  1110 SER B N   
16840 C CA  . SER B 1112 ? 0.3789 0.3455 0.4124 -0.0481 -0.0155 0.0843  1110 SER B CA  
16841 C C   . SER B 1112 ? 0.3973 0.3782 0.4337 -0.0459 -0.0103 0.0775  1110 SER B C   
16842 O O   . SER B 1112 ? 0.3659 0.3466 0.4001 -0.0395 -0.0104 0.0705  1110 SER B O   
16843 C CB  . SER B 1112 ? 0.4121 0.3821 0.4391 -0.0475 -0.0136 0.0902  1110 SER B CB  
16844 O OG  . SER B 1112 ? 0.4502 0.4235 0.4721 -0.0400 -0.0125 0.0853  1110 SER B OG  
16845 N N   . GLY B 1113 ? 0.3868 0.3801 0.4280 -0.0512 -0.0056 0.0797  1111 GLY B N   
16846 C CA  . GLY B 1113 ? 0.3805 0.3862 0.4250 -0.0493 -0.0012 0.0733  1111 GLY B CA  
16847 C C   . GLY B 1113 ? 0.3306 0.3303 0.3793 -0.0473 -0.0044 0.0664  1111 GLY B C   
16848 O O   . GLY B 1113 ? 0.3376 0.3412 0.3854 -0.0422 -0.0030 0.0594  1111 GLY B O   
16849 N N   . LEU B 1114 ? 0.3183 0.3081 0.3713 -0.0514 -0.0090 0.0684  1112 LEU B N   
16850 C CA  . LEU B 1114 ? 0.3574 0.3402 0.4136 -0.0496 -0.0128 0.0620  1112 LEU B CA  
16851 C C   . LEU B 1114 ? 0.3567 0.3300 0.4063 -0.0418 -0.0156 0.0562  1112 LEU B C   
16852 O O   . LEU B 1114 ? 0.3357 0.3103 0.3856 -0.0377 -0.0154 0.0491  1112 LEU B O   
16853 C CB  . LEU B 1114 ? 0.3584 0.3303 0.4192 -0.0557 -0.0182 0.0657  1112 LEU B CB  
16854 C CG  . LEU B 1114 ? 0.3394 0.3001 0.4017 -0.0540 -0.0237 0.0597  1112 LEU B CG  
16855 C CD1 . LEU B 1114 ? 0.3441 0.3154 0.4109 -0.0526 -0.0208 0.0533  1112 LEU B CD1 
16856 C CD2 . LEU B 1114 ? 0.3696 0.3205 0.4366 -0.0612 -0.0290 0.0645  1112 LEU B CD2 
16857 N N   . TYR B 1115 ? 0.3500 0.3142 0.3938 -0.0395 -0.0181 0.0595  1113 TYR B N   
16858 C CA  . TYR B 1115 ? 0.3907 0.3468 0.4288 -0.0316 -0.0206 0.0544  1113 TYR B CA  
16859 C C   . TYR B 1115 ? 0.3125 0.2806 0.3484 -0.0265 -0.0159 0.0495  1113 TYR B C   
16860 O O   . TYR B 1115 ? 0.3449 0.3114 0.3795 -0.0212 -0.0165 0.0429  1113 TYR B O   
16861 C CB  . TYR B 1115 ? 0.3767 0.3223 0.4094 -0.0300 -0.0239 0.0594  1113 TYR B CB  
16862 C CG  . TYR B 1115 ? 0.3787 0.3087 0.4124 -0.0339 -0.0299 0.0632  1113 TYR B CG  
16863 C CD1 . TYR B 1115 ? 0.4076 0.3314 0.4457 -0.0368 -0.0331 0.0604  1113 TYR B CD1 
16864 C CD2 . TYR B 1115 ? 0.4288 0.3497 0.4587 -0.0346 -0.0329 0.0698  1113 TYR B CD2 
16865 C CE1 . TYR B 1115 ? 0.4758 0.3845 0.5146 -0.0409 -0.0392 0.0639  1113 TYR B CE1 
16866 C CE2 . TYR B 1115 ? 0.4738 0.3793 0.5043 -0.0384 -0.0389 0.0735  1113 TYR B CE2 
16867 C CZ  . TYR B 1115 ? 0.4722 0.3715 0.5071 -0.0416 -0.0421 0.0705  1113 TYR B CZ  
16868 O OH  . TYR B 1115 ? 0.4956 0.3786 0.5308 -0.0458 -0.0486 0.0742  1113 TYR B OH  
16869 N N   . HIS B 1116 ? 0.3104 0.2904 0.3453 -0.0281 -0.0112 0.0528  1114 HIS B N   
16870 C CA  . HIS B 1116 ? 0.3364 0.3276 0.3693 -0.0239 -0.0070 0.0484  1114 HIS B CA  
16871 C C   . HIS B 1116 ? 0.3161 0.3137 0.3536 -0.0240 -0.0050 0.0423  1114 HIS B C   
16872 O O   . HIS B 1116 ? 0.3020 0.3018 0.3378 -0.0191 -0.0043 0.0364  1114 HIS B O   
16873 C CB  . HIS B 1116 ? 0.3233 0.3256 0.3539 -0.0260 -0.0026 0.0529  1114 HIS B CB  
16874 C CG  . HIS B 1116 ? 0.3357 0.3338 0.3602 -0.0240 -0.0042 0.0575  1114 HIS B CG  
16875 N ND1 . HIS B 1116 ? 0.3857 0.3750 0.4090 -0.0271 -0.0072 0.0643  1114 HIS B ND1 
16876 C CD2 . HIS B 1116 ? 0.3960 0.3978 0.4153 -0.0192 -0.0034 0.0564  1114 HIS B CD2 
16877 C CE1 . HIS B 1116 ? 0.3916 0.3792 0.4092 -0.0240 -0.0083 0.0672  1114 HIS B CE1 
16878 N NE2 . HIS B 1116 ? 0.4266 0.4219 0.4418 -0.0192 -0.0060 0.0624  1114 HIS B NE2 
16879 N N   . GLN B 1117 ? 0.3286 0.3295 0.3721 -0.0295 -0.0042 0.0439  1115 GLN B N   
16880 C CA  . GLN B 1117 ? 0.2920 0.2988 0.3401 -0.0295 -0.0027 0.0384  1115 GLN B CA  
16881 C C   . GLN B 1117 ? 0.2926 0.2893 0.3403 -0.0260 -0.0070 0.0328  1115 GLN B C   
16882 O O   . GLN B 1117 ? 0.2856 0.2860 0.3332 -0.0226 -0.0058 0.0269  1115 GLN B O   
16883 C CB  . GLN B 1117 ? 0.2649 0.2772 0.3205 -0.0362 -0.0015 0.0416  1115 GLN B CB  
16884 C CG  . GLN B 1117 ? 0.3031 0.3283 0.3597 -0.0393 0.0039  0.0462  1115 GLN B CG  
16885 C CD  . GLN B 1117 ? 0.3146 0.3456 0.3796 -0.0459 0.0050  0.0499  1115 GLN B CD  
16886 O OE1 . GLN B 1117 ? 0.2934 0.3175 0.3634 -0.0488 0.0009  0.0499  1115 GLN B OE1 
16887 N NE2 . GLN B 1117 ? 0.2784 0.3226 0.3450 -0.0482 0.0105  0.0528  1115 GLN B NE2 
16888 N N   . LEU B 1118 ? 0.3037 0.2872 0.3509 -0.0269 -0.0120 0.0345  1116 LEU B N   
16889 C CA  . LEU B 1118 ? 0.3287 0.3016 0.3741 -0.0231 -0.0162 0.0290  1116 LEU B CA  
16890 C C   . LEU B 1118 ? 0.2975 0.2705 0.3372 -0.0157 -0.0152 0.0247  1116 LEU B C   
16891 O O   . LEU B 1118 ? 0.3042 0.2769 0.3431 -0.0121 -0.0155 0.0187  1116 LEU B O   
16892 C CB  . LEU B 1118 ? 0.3517 0.3091 0.3960 -0.0247 -0.0220 0.0318  1116 LEU B CB  
16893 C CG  . LEU B 1118 ? 0.3735 0.3270 0.4238 -0.0308 -0.0251 0.0328  1116 LEU B CG  
16894 C CD1 . LEU B 1118 ? 0.3832 0.3218 0.4324 -0.0336 -0.0307 0.0373  1116 LEU B CD1 
16895 C CD2 . LEU B 1118 ? 0.4104 0.3611 0.4609 -0.0279 -0.0270 0.0254  1116 LEU B CD2 
16896 N N   . ALA B 1119 ? 0.3080 0.2818 0.3436 -0.0134 -0.0143 0.0279  1117 ALA B N   
16897 C CA  . ALA B 1119 ? 0.3170 0.2919 0.3480 -0.0066 -0.0135 0.0244  1117 ALA B CA  
16898 C C   . ALA B 1119 ? 0.3370 0.3239 0.3689 -0.0052 -0.0094 0.0200  1117 ALA B C   
16899 O O   . ALA B 1119 ? 0.2883 0.2748 0.3185 -0.0006 -0.0096 0.0149  1117 ALA B O   
16900 C CB  . ALA B 1119 ? 0.3037 0.2791 0.3311 -0.0052 -0.0132 0.0293  1117 ALA B CB  
16901 N N   . ALA B 1120 ? 0.3073 0.3049 0.3417 -0.0091 -0.0056 0.0221  1118 ALA B N   
16902 C CA  . ALA B 1120 ? 0.2976 0.3058 0.3328 -0.0081 -0.0020 0.0180  1118 ALA B CA  
16903 C C   . ALA B 1120 ? 0.3128 0.3190 0.3508 -0.0076 -0.0031 0.0128  1118 ALA B C   
16904 O O   . ALA B 1120 ? 0.2759 0.2851 0.3125 -0.0041 -0.0022 0.0082  1118 ALA B O   
16905 C CB  . ALA B 1120 ? 0.3129 0.3317 0.3505 -0.0124 0.0020  0.0210  1118 ALA B CB  
16906 N N   . ALA B 1121 ? 0.2706 0.2719 0.3126 -0.0115 -0.0054 0.0138  1119 ALA B N   
16907 C CA  . ALA B 1121 ? 0.2505 0.2504 0.2951 -0.0115 -0.0068 0.0090  1119 ALA B CA  
16908 C C   . ALA B 1121 ? 0.2742 0.2638 0.3147 -0.0068 -0.0103 0.0050  1119 ALA B C   
16909 O O   . ALA B 1121 ? 0.2714 0.2619 0.3111 -0.0044 -0.0102 0.0000  1119 ALA B O   
16910 C CB  . ALA B 1121 ? 0.2927 0.2911 0.3434 -0.0172 -0.0085 0.0115  1119 ALA B CB  
16911 N N   . LEU B 1122 ? 0.2720 0.2514 0.3094 -0.0054 -0.0134 0.0069  1120 LEU B N   
16912 C CA  . LEU B 1122 ? 0.3176 0.2872 0.3505 -0.0002 -0.0165 0.0028  1120 LEU B CA  
16913 C C   . LEU B 1122 ? 0.3151 0.2903 0.3442 0.0056  -0.0138 -0.0001 1120 LEU B C   
16914 O O   . LEU B 1122 ? 0.3088 0.2819 0.3353 0.0094  -0.0143 -0.0049 1120 LEU B O   
16915 C CB  . LEU B 1122 ? 0.2910 0.2479 0.3214 0.0003  -0.0206 0.0056  1120 LEU B CB  
16916 C CG  . LEU B 1122 ? 0.3366 0.2851 0.3703 -0.0054 -0.0245 0.0082  1120 LEU B CG  
16917 C CD1 . LEU B 1122 ? 0.3551 0.2907 0.3858 -0.0047 -0.0286 0.0117  1120 LEU B CD1 
16918 C CD2 . LEU B 1122 ? 0.3044 0.2474 0.3386 -0.0057 -0.0275 0.0032  1120 LEU B CD2 
16919 N N   . ALA B 1123 ? 0.2789 0.2614 0.3074 0.0062  -0.0110 0.0029  1121 ALA B N   
16920 C CA  . ALA B 1123 ? 0.2892 0.2777 0.3149 0.0112  -0.0087 0.0006  1121 ALA B CA  
16921 C C   . ALA B 1123 ? 0.3156 0.3122 0.3423 0.0111  -0.0062 -0.0034 1121 ALA B C   
16922 O O   . ALA B 1123 ? 0.2746 0.2745 0.2991 0.0153  -0.0051 -0.0063 1121 ALA B O   
16923 C CB  . ALA B 1123 ? 0.3055 0.3007 0.3305 0.0110  -0.0067 0.0049  1121 ALA B CB  
16924 N N   . THR B 1124 ? 0.2681 0.2685 0.2986 0.0066  -0.0053 -0.0035 1122 THR B N   
16925 C CA  . THR B 1124 ? 0.2688 0.2758 0.3004 0.0065  -0.0033 -0.0072 1122 THR B CA  
16926 C C   . THR B 1124 ? 0.2642 0.2649 0.2962 0.0065  -0.0059 -0.0108 1122 THR B C   
16927 O O   . THR B 1124 ? 0.3009 0.3060 0.3347 0.0055  -0.0050 -0.0133 1122 THR B O   
16928 C CB  . THR B 1124 ? 0.2833 0.2996 0.3185 0.0024  -0.0004 -0.0053 1122 THR B CB  
16929 O OG1 . THR B 1124 ? 0.2864 0.3006 0.3251 -0.0019 -0.0013 -0.0018 1122 THR B OG1 
16930 C CG2 . THR B 1124 ? 0.2688 0.2922 0.3018 0.0035  0.0023  -0.0033 1122 THR B CG2 
16931 N N   . GLY B 1125 ? 0.2681 0.2580 0.2979 0.0080  -0.0095 -0.0112 1123 GLY B N   
16932 C CA  . GLY B 1125 ? 0.2505 0.2333 0.2792 0.0086  -0.0124 -0.0150 1123 GLY B CA  
16933 C C   . GLY B 1125 ? 0.2757 0.2564 0.3091 0.0034  -0.0146 -0.0143 1123 GLY B C   
16934 O O   . GLY B 1125 ? 0.2903 0.2663 0.3231 0.0034  -0.0172 -0.0176 1123 GLY B O   
16935 N N   . ASN B 1126 ? 0.2666 0.2512 0.3049 -0.0013 -0.0137 -0.0099 1124 ASN B N   
16936 C CA  . ASN B 1126 ? 0.2902 0.2755 0.3345 -0.0064 -0.0153 -0.0090 1124 ASN B CA  
16937 C C   . ASN B 1126 ? 0.3017 0.2760 0.3469 -0.0093 -0.0200 -0.0069 1124 ASN B C   
16938 O O   . ASN B 1126 ? 0.3270 0.2937 0.3688 -0.0078 -0.0216 -0.0050 1124 ASN B O   
16939 C CB  . ASN B 1126 ? 0.2728 0.2697 0.3226 -0.0102 -0.0114 -0.0055 1124 ASN B CB  
16940 C CG  . ASN B 1126 ? 0.2417 0.2485 0.2904 -0.0078 -0.0073 -0.0077 1124 ASN B CG  
16941 O OD1 . ASN B 1126 ? 0.2844 0.2940 0.3340 -0.0070 -0.0071 -0.0113 1124 ASN B OD1 
16942 N ND2 . ASN B 1126 ? 0.2581 0.2698 0.3047 -0.0067 -0.0042 -0.0055 1124 ASN B ND2 
16943 N N   . SER B 1127 ? 0.3132 0.2864 0.3632 -0.0133 -0.0227 -0.0073 1125 SER B N   
16944 C CA  . SER B 1127 ? 0.2816 0.2471 0.3349 -0.0181 -0.0269 -0.0040 1125 SER B CA  
16945 C C   . SER B 1127 ? 0.3096 0.2853 0.3703 -0.0236 -0.0238 0.0016  1125 SER B C   
16946 O O   . SER B 1127 ? 0.2722 0.2600 0.3349 -0.0232 -0.0188 0.0021  1125 SER B O   
16947 C CB  . SER B 1127 ? 0.3272 0.2864 0.3822 -0.0200 -0.0319 -0.0071 1125 SER B CB  
16948 O OG  . SER B 1127 ? 0.3347 0.3045 0.3957 -0.0222 -0.0301 -0.0080 1125 SER B OG  
16949 N N   . VAL B 1128 ? 0.2995 0.2702 0.3640 -0.0288 -0.0269 0.0061  1126 VAL B N   
16950 C CA  . VAL B 1128 ? 0.3259 0.3065 0.3974 -0.0342 -0.0238 0.0120  1126 VAL B CA  
16951 C C   . VAL B 1128 ? 0.3316 0.3105 0.4109 -0.0409 -0.0277 0.0146  1126 VAL B C   
16952 O O   . VAL B 1128 ? 0.3561 0.3227 0.4341 -0.0418 -0.0337 0.0129  1126 VAL B O   
16953 C CB  . VAL B 1128 ? 0.3236 0.3023 0.3920 -0.0346 -0.0222 0.0172  1126 VAL B CB  
16954 C CG1 . VAL B 1128 ? 0.2852 0.2661 0.3464 -0.0281 -0.0188 0.0148  1126 VAL B CG1 
16955 C CG2 . VAL B 1128 ? 0.3237 0.2867 0.3897 -0.0363 -0.0282 0.0195  1126 VAL B CG2 
16956 N N   . ALA B 1129 ? 0.2833 0.2750 0.3707 -0.0454 -0.0242 0.0186  1127 ALA B N   
16957 C CA  . ALA B 1129 ? 0.2784 0.2713 0.3746 -0.0529 -0.0267 0.0233  1127 ALA B CA  
16958 C C   . ALA B 1129 ? 0.3034 0.3031 0.4017 -0.0565 -0.0227 0.0306  1127 ALA B C   
16959 O O   . ALA B 1129 ? 0.2644 0.2772 0.3638 -0.0553 -0.0165 0.0314  1127 ALA B O   
16960 C CB  . ALA B 1129 ? 0.2946 0.2988 0.3996 -0.0549 -0.0259 0.0216  1127 ALA B CB  
16961 N N   . ILE B 1130 ? 0.2713 0.2613 0.3694 -0.0608 -0.0265 0.0356  1128 ILE B N   
16962 C CA  . ILE B 1130 ? 0.2992 0.2941 0.3985 -0.0646 -0.0232 0.0431  1128 ILE B CA  
16963 C C   . ILE B 1130 ? 0.2669 0.2712 0.3775 -0.0727 -0.0228 0.0487  1128 ILE B C   
16964 O O   . ILE B 1130 ? 0.3175 0.3154 0.4335 -0.0774 -0.0285 0.0495  1128 ILE B O   
16965 C CB  . ILE B 1130 ? 0.3195 0.2984 0.4118 -0.0647 -0.0275 0.0461  1128 ILE B CB  
16966 C CG1 . ILE B 1130 ? 0.3001 0.2697 0.3822 -0.0562 -0.0285 0.0400  1128 ILE B CG1 
16967 C CG2 . ILE B 1130 ? 0.3151 0.2997 0.4070 -0.0677 -0.0235 0.0538  1128 ILE B CG2 
16968 C CD1 . ILE B 1130 ? 0.3088 0.2612 0.3843 -0.0552 -0.0336 0.0418  1128 ILE B CD1 
16969 N N   . ASP B 1131 ? 0.2897 0.3095 0.4039 -0.0744 -0.0161 0.0528  1129 ASP B N   
16970 C CA  . ASP B 1131 ? 0.3097 0.3409 0.4351 -0.0819 -0.0145 0.0589  1129 ASP B CA  
16971 C C   . ASP B 1131 ? 0.3059 0.3270 0.4336 -0.0892 -0.0196 0.0659  1129 ASP B C   
16972 O O   . ASP B 1131 ? 0.3339 0.3497 0.4559 -0.0901 -0.0190 0.0708  1129 ASP B O   
16973 C CB  . ASP B 1131 ? 0.3249 0.3732 0.4513 -0.0815 -0.0060 0.0621  1129 ASP B CB  
16974 C CG  . ASP B 1131 ? 0.3155 0.3769 0.4531 -0.0891 -0.0034 0.0693  1129 ASP B CG  
16975 O OD1 . ASP B 1131 ? 0.3104 0.3748 0.4580 -0.0930 -0.0064 0.0691  1129 ASP B OD1 
16976 O OD2 . ASP B 1131 ? 0.3291 0.3982 0.4654 -0.0910 0.0017  0.0751  1129 ASP B OD2 
16977 N N   . ALA B 1132 ? 0.3438 0.3615 0.4797 -0.0946 -0.0252 0.0666  1130 ALA B N   
16978 C CA  . ALA B 1132 ? 0.3452 0.3515 0.4832 -0.1021 -0.0311 0.0730  1130 ALA B CA  
16979 C C   . ALA B 1132 ? 0.3402 0.3572 0.4833 -0.1087 -0.0266 0.0828  1130 ALA B C   
16980 O O   . ALA B 1132 ? 0.3639 0.3706 0.5057 -0.1140 -0.0303 0.0892  1130 ALA B O   
16981 C CB  . ALA B 1132 ? 0.3445 0.3467 0.4911 -0.1071 -0.0379 0.0718  1130 ALA B CB  
16982 N N   . ALA B 1133 ? 0.3475 0.3847 0.4959 -0.1084 -0.0186 0.0842  1131 ALA B N   
16983 C CA  . ALA B 1133 ? 0.3667 0.4158 0.5199 -0.1147 -0.0136 0.0936  1131 ALA B CA  
16984 C C   . ALA B 1133 ? 0.3641 0.4086 0.5063 -0.1124 -0.0107 0.0972  1131 ALA B C   
16985 O O   . ALA B 1133 ? 0.3900 0.4410 0.5342 -0.1181 -0.0076 0.1058  1131 ALA B O   
16986 C CB  . ALA B 1133 ? 0.3913 0.4638 0.5530 -0.1142 -0.0057 0.0934  1131 ALA B CB  
16987 N N   . SER B 1134 ? 0.3408 0.3747 0.4714 -0.1045 -0.0116 0.0911  1132 SER B N   
16988 C CA  . SER B 1134 ? 0.3363 0.3646 0.4565 -0.1022 -0.0099 0.0944  1132 SER B CA  
16989 C C   . SER B 1134 ? 0.3505 0.3632 0.4690 -0.1080 -0.0161 0.1015  1132 SER B C   
16990 O O   . SER B 1134 ? 0.3771 0.3876 0.4894 -0.1086 -0.0145 0.1072  1132 SER B O   
16991 C CB  . SER B 1134 ? 0.3193 0.3397 0.4289 -0.0924 -0.0103 0.0862  1132 SER B CB  
16992 O OG  . SER B 1134 ? 0.3463 0.3497 0.4538 -0.0904 -0.0179 0.0812  1132 SER B OG  
16993 N N   . GLY B 1135 ? 0.3196 0.3208 0.4431 -0.1122 -0.0236 0.1011  1133 GLY B N   
16994 C CA  . GLY B 1135 ? 0.3795 0.3646 0.5015 -0.1180 -0.0301 0.1077  1133 GLY B CA  
16995 C C   . GLY B 1135 ? 0.3815 0.3470 0.4912 -0.1120 -0.0347 0.1050  1133 GLY B C   
16996 O O   . GLY B 1135 ? 0.4289 0.3812 0.5355 -0.1158 -0.0392 0.1112  1133 GLY B O   
16997 N N   . LEU B 1136 ? 0.4001 0.3634 0.5031 -0.1026 -0.0338 0.0961  1134 LEU B N   
16998 C CA  . LEU B 1136 ? 0.4207 0.3692 0.5122 -0.0955 -0.0365 0.0932  1134 LEU B CA  
16999 C C   . LEU B 1136 ? 0.4219 0.3516 0.5102 -0.0921 -0.0445 0.0866  1134 LEU B C   
17000 O O   . LEU B 1136 ? 0.4634 0.3833 0.5428 -0.0842 -0.0460 0.0816  1134 LEU B O   
17001 C CB  . LEU B 1136 ? 0.3884 0.3478 0.4741 -0.0872 -0.0298 0.0882  1134 LEU B CB  
17002 C CG  . LEU B 1136 ? 0.4044 0.3796 0.4900 -0.0892 -0.0223 0.0944  1134 LEU B CG  
17003 C CD1 . LEU B 1136 ? 0.3960 0.3823 0.4768 -0.0814 -0.0163 0.0883  1134 LEU B CD1 
17004 C CD2 . LEU B 1136 ? 0.4379 0.4038 0.5176 -0.0916 -0.0243 0.1025  1134 LEU B CD2 
17005 N N   . GLN B 1137 ? 0.4363 0.3609 0.5315 -0.0979 -0.0497 0.0865  1135 GLN B N   
17006 C CA  . GLN B 1137 ? 0.4607 0.3688 0.5525 -0.0943 -0.0570 0.0791  1135 GLN B CA  
17007 C C   . GLN B 1137 ? 0.5209 0.4071 0.6035 -0.0914 -0.0632 0.0797  1135 GLN B C   
17008 O O   . GLN B 1137 ? 0.5694 0.4429 0.6452 -0.0845 -0.0671 0.0722  1135 GLN B O   
17009 C CB  . GLN B 1137 ? 0.4875 0.3944 0.5887 -0.1020 -0.0620 0.0796  1135 GLN B CB  
17010 C CG  . GLN B 1137 ? 0.5006 0.4267 0.6105 -0.1028 -0.0572 0.0764  1135 GLN B CG  
17011 C CD  . GLN B 1137 ? 0.4288 0.3746 0.5483 -0.1096 -0.0509 0.0844  1135 GLN B CD  
17012 O OE1 . GLN B 1137 ? 0.4209 0.3683 0.5389 -0.1125 -0.0483 0.0919  1135 GLN B OE1 
17013 N NE2 . GLN B 1137 ? 0.4446 0.4056 0.5739 -0.1120 -0.0483 0.0829  1135 GLN B NE2 
17014 N N   . ALA B 1138 ? 0.4906 0.3722 0.5724 -0.0963 -0.0642 0.0885  1136 ALA B N   
17015 C CA  . ALA B 1138 ? 0.5028 0.3631 0.5758 -0.0932 -0.0703 0.0894  1136 ALA B CA  
17016 C C   . ALA B 1138 ? 0.5170 0.3774 0.5806 -0.0831 -0.0667 0.0861  1136 ALA B C   
17017 O O   . ALA B 1138 ? 0.5268 0.3703 0.5829 -0.0789 -0.0714 0.0861  1136 ALA B O   
17018 C CB  . ALA B 1138 ? 0.4698 0.3242 0.5451 -0.1021 -0.0731 0.1005  1136 ALA B CB  
17019 N N   . SER B 1139 ? 0.4821 0.3609 0.5463 -0.0791 -0.0587 0.0835  1137 SER B N   
17020 C CA  . SER B 1139 ? 0.5072 0.3880 0.5634 -0.0701 -0.0552 0.0806  1137 SER B CA  
17021 C C   . SER B 1139 ? 0.5090 0.3817 0.5596 -0.0608 -0.0574 0.0706  1137 SER B C   
17022 O O   . SER B 1139 ? 0.4930 0.3648 0.5369 -0.0529 -0.0557 0.0681  1137 SER B O   
17023 C CB  . SER B 1139 ? 0.4516 0.3547 0.5101 -0.0697 -0.0462 0.0816  1137 SER B CB  
17024 O OG  . SER B 1139 ? 0.4582 0.3683 0.5190 -0.0765 -0.0435 0.0912  1137 SER B OG  
17025 N N   . LEU B 1140 ? 0.4981 0.3657 0.5513 -0.0614 -0.0610 0.0649  1138 LEU B N   
17026 C CA  . LEU B 1140 ? 0.5298 0.3906 0.5775 -0.0528 -0.0627 0.0554  1138 LEU B CA  
17027 C C   . LEU B 1140 ? 0.5465 0.3850 0.5904 -0.0525 -0.0716 0.0530  1138 LEU B C   
17028 O O   . LEU B 1140 ? 0.5907 0.4239 0.6338 -0.0504 -0.0745 0.0460  1138 LEU B O   
17029 C CB  . LEU B 1140 ? 0.5205 0.3952 0.5729 -0.0525 -0.0589 0.0496  1138 LEU B CB  
17030 C CG  . LEU B 1140 ? 0.5102 0.4062 0.5657 -0.0522 -0.0503 0.0512  1138 LEU B CG  
17031 C CD1 . LEU B 1140 ? 0.4513 0.3596 0.5107 -0.0510 -0.0470 0.0450  1138 LEU B CD1 
17032 C CD2 . LEU B 1140 ? 0.5279 0.4253 0.5761 -0.0448 -0.0471 0.0507  1138 LEU B CD2 
17033 N N   . LYS B 1141 ? 0.5492 0.3738 0.5902 -0.0542 -0.0760 0.0586  1139 LYS B N   
17034 C CA  . LYS B 1141 ? 0.5644 0.3659 0.6008 -0.0536 -0.0849 0.0566  1139 LYS B CA  
17035 C C   . LYS B 1141 ? 0.6355 0.4266 0.6624 -0.0418 -0.0862 0.0491  1139 LYS B C   
17036 O O   . LYS B 1141 ? 0.6412 0.4371 0.6643 -0.0357 -0.0824 0.0499  1139 LYS B O   
17037 C CB  . LYS B 1141 ? 0.5924 0.3824 0.6294 -0.0603 -0.0895 0.0659  1139 LYS B CB  
17038 N N   . ASN B 1142 ? 0.6437 0.4212 0.6667 -0.0386 -0.0917 0.0418  1140 ASN B N   
17039 C CA  . ASN B 1142 ? 0.6540 0.4202 0.6677 -0.0273 -0.0934 0.0342  1140 ASN B CA  
17040 C C   . ASN B 1142 ? 0.6101 0.3932 0.6226 -0.0197 -0.0858 0.0288  1140 ASN B C   
17041 O O   . ASN B 1142 ? 0.6268 0.4079 0.6334 -0.0104 -0.0843 0.0257  1140 ASN B O   
17042 C CB  . ASN B 1142 ? 0.6755 0.4273 0.6835 -0.0234 -0.0969 0.0380  1140 ASN B CB  
17043 N N   . LEU B 1143 ? 0.5850 0.3849 0.6036 -0.0236 -0.0811 0.0277  1141 LEU B N   
17044 C CA  . LEU B 1143 ? 0.5792 0.3950 0.5971 -0.0174 -0.0741 0.0228  1141 LEU B CA  
17045 C C   . LEU B 1143 ? 0.5401 0.3476 0.5512 -0.0094 -0.0763 0.0134  1141 LEU B C   
17046 O O   . LEU B 1143 ? 0.5770 0.3727 0.5867 -0.0113 -0.0819 0.0099  1141 LEU B O   
17047 C CB  . LEU B 1143 ? 0.5150 0.3490 0.5412 -0.0241 -0.0694 0.0241  1141 LEU B CB  
17048 C CG  . LEU B 1143 ? 0.4997 0.3536 0.5276 -0.0208 -0.0614 0.0225  1141 LEU B CG  
17049 C CD1 . LEU B 1143 ? 0.5043 0.3661 0.5322 -0.0202 -0.0571 0.0284  1141 LEU B CD1 
17050 C CD2 . LEU B 1143 ? 0.5217 0.3894 0.5575 -0.0272 -0.0586 0.0226  1141 LEU B CD2 
17051 N N   . PRO B 1144 ? 0.5612 0.3749 0.5680 -0.0005 -0.0720 0.0091  1142 PRO B N   
17052 C CA  . PRO B 1144 ? 0.5640 0.3720 0.5643 0.0071  -0.0730 0.0003  1142 PRO B CA  
17053 C C   . PRO B 1144 ? 0.5329 0.3473 0.5361 0.0031  -0.0726 -0.0035 1142 PRO B C   
17054 O O   . PRO B 1144 ? 0.5207 0.3511 0.5308 -0.0019 -0.0681 -0.0010 1142 PRO B O   
17055 C CB  . PRO B 1144 ? 0.5471 0.3666 0.5450 0.0155  -0.0668 -0.0017 1142 PRO B CB  
17056 C CG  . PRO B 1144 ? 0.5681 0.3906 0.5683 0.0141  -0.0654 0.0057  1142 PRO B CG  
17057 C CD  . PRO B 1144 ? 0.5436 0.3690 0.5507 0.0032  -0.0663 0.0124  1142 PRO B CD  
17058 N N   . GLN B 1145 ? 0.5743 0.3757 0.5720 0.0057  -0.0776 -0.0098 1143 GLN B N   
17059 C CA  . GLN B 1145 ? 0.5379 0.3435 0.5374 0.0023  -0.0782 -0.0137 1143 GLN B CA  
17060 C C   . GLN B 1145 ? 0.5175 0.3424 0.5191 0.0049  -0.0707 -0.0159 1143 GLN B C   
17061 O O   . GLN B 1145 ? 0.5174 0.3519 0.5244 -0.0003 -0.0695 -0.0158 1143 GLN B O   
17062 C CB  . GLN B 1145 ? 0.5405 0.3290 0.5313 0.0067  -0.0843 -0.0210 1143 GLN B CB  
17063 N N   . THR B 1146 ? 0.5050 0.3355 0.5027 0.0128  -0.0661 -0.0177 1144 THR B N   
17064 C CA  . THR B 1146 ? 0.5238 0.3722 0.5234 0.0149  -0.0592 -0.0193 1144 THR B CA  
17065 C C   . THR B 1146 ? 0.4776 0.3412 0.4863 0.0078  -0.0551 -0.0133 1144 THR B C   
17066 O O   . THR B 1146 ? 0.4996 0.3756 0.5120 0.0056  -0.0517 -0.0144 1144 THR B O   
17067 C CB  . THR B 1146 ? 0.5048 0.3568 0.4996 0.0239  -0.0552 -0.0212 1144 THR B CB  
17068 O OG1 . THR B 1146 ? 0.5336 0.3806 0.5288 0.0247  -0.0562 -0.0163 1144 THR B OG1 
17069 C CG2 . THR B 1146 ? 0.5720 0.4139 0.5580 0.0318  -0.0573 -0.0284 1144 THR B CG2 
17070 N N   . VAL B 1147 ? 0.4551 0.3177 0.4669 0.0045  -0.0553 -0.0069 1145 VAL B N   
17071 C CA  . VAL B 1147 ? 0.4357 0.3125 0.4554 -0.0022 -0.0514 -0.0011 1145 VAL B CA  
17072 C C   . VAL B 1147 ? 0.4610 0.3370 0.4870 -0.0107 -0.0545 0.0008  1145 VAL B C   
17073 O O   . VAL B 1147 ? 0.4612 0.3507 0.4934 -0.0147 -0.0510 0.0017  1145 VAL B O   
17074 C CB  . VAL B 1147 ? 0.4385 0.3154 0.4589 -0.0028 -0.0504 0.0054  1145 VAL B CB  
17075 C CG1 . VAL B 1147 ? 0.4804 0.3733 0.5077 -0.0087 -0.0454 0.0108  1145 VAL B CG1 
17076 C CG2 . VAL B 1147 ? 0.4017 0.2785 0.4162 0.0061  -0.0482 0.0033  1145 VAL B CG2 
17077 N N   . GLY B 1148 ? 0.4494 0.3094 0.4740 -0.0134 -0.0613 0.0013  1146 GLY B N   
17078 C CA  . GLY B 1148 ? 0.4700 0.3292 0.5014 -0.0220 -0.0648 0.0037  1146 GLY B CA  
17079 C C   . GLY B 1148 ? 0.4725 0.3389 0.5062 -0.0228 -0.0643 -0.0011 1146 GLY B C   
17080 O O   . GLY B 1148 ? 0.4307 0.3061 0.4728 -0.0297 -0.0638 0.0017  1146 GLY B O   
17081 N N   . LEU B 1149 ? 0.4627 0.3260 0.4892 -0.0157 -0.0642 -0.0082 1147 LEU B N   
17082 C CA  . LEU B 1149 ? 0.4693 0.3390 0.4970 -0.0159 -0.0638 -0.0128 1147 LEU B CA  
17083 C C   . LEU B 1149 ? 0.4372 0.3266 0.4715 -0.0174 -0.0569 -0.0109 1147 LEU B C   
17084 O O   . LEU B 1149 ? 0.4657 0.3622 0.5037 -0.0196 -0.0567 -0.0129 1147 LEU B O   
17085 C CB  . LEU B 1149 ? 0.4838 0.3465 0.5015 -0.0076 -0.0645 -0.0203 1147 LEU B CB  
17086 N N   . ARG B 1150 ? 0.3909 0.2889 0.4264 -0.0163 -0.0516 -0.0071 1148 ARG B N   
17087 C CA  . ARG B 1150 ? 0.4147 0.3305 0.4560 -0.0178 -0.0454 -0.0053 1148 ARG B CA  
17088 C C   . ARG B 1150 ? 0.3937 0.3171 0.4439 -0.0255 -0.0443 0.0013  1148 ARG B C   
17089 O O   . ARG B 1150 ? 0.4055 0.3437 0.4607 -0.0269 -0.0391 0.0029  1148 ARG B O   
17090 C CB  . ARG B 1150 ? 0.3912 0.3135 0.4284 -0.0120 -0.0401 -0.0054 1148 ARG B CB  
17091 C CG  . ARG B 1150 ? 0.4059 0.3273 0.4363 -0.0048 -0.0390 -0.0117 1148 ARG B CG  
17092 C CD  . ARG B 1150 ? 0.3939 0.3293 0.4249 -0.0022 -0.0326 -0.0113 1148 ARG B CD  
17093 N NE  . ARG B 1150 ? 0.4088 0.3436 0.4332 0.0048  -0.0312 -0.0161 1148 ARG B NE  
17094 C CZ  . ARG B 1150 ? 0.3788 0.3218 0.4016 0.0086  -0.0268 -0.0158 1148 ARG B CZ  
17095 N NH1 . ARG B 1150 ? 0.3183 0.2704 0.3449 0.0062  -0.0234 -0.0114 1148 ARG B NH1 
17096 N NH2 . ARG B 1150 ? 0.3660 0.3084 0.3833 0.0148  -0.0258 -0.0199 1148 ARG B NH2 
17097 N N   . VAL B 1151 ? 0.4162 0.3300 0.4685 -0.0303 -0.0490 0.0052  1149 VAL B N   
17098 C CA  . VAL B 1151 ? 0.3723 0.2927 0.4324 -0.0376 -0.0477 0.0126  1149 VAL B CA  
17099 C C   . VAL B 1151 ? 0.4329 0.3526 0.5006 -0.0447 -0.0519 0.0138  1149 VAL B C   
17100 O O   . VAL B 1151 ? 0.4105 0.3162 0.4761 -0.0459 -0.0587 0.0118  1149 VAL B O   
17101 C CB  . VAL B 1151 ? 0.4232 0.3338 0.4801 -0.0383 -0.0495 0.0176  1149 VAL B CB  
17102 C CG1 . VAL B 1151 ? 0.4194 0.3348 0.4845 -0.0471 -0.0494 0.0257  1149 VAL B CG1 
17103 C CG2 . VAL B 1151 ? 0.4058 0.3209 0.4572 -0.0321 -0.0446 0.0176  1149 VAL B CG2 
17104 N N   . SER B 1152 ? 0.3885 0.3236 0.4652 -0.0492 -0.0481 0.0168  1150 SER B N   
17105 C CA  . SER B 1152 ? 0.3612 0.2983 0.4473 -0.0570 -0.0516 0.0198  1150 SER B CA  
17106 C C   . SER B 1152 ? 0.3764 0.3256 0.4705 -0.0630 -0.0473 0.0277  1150 SER B C   
17107 O O   . SER B 1152 ? 0.3669 0.3249 0.4592 -0.0606 -0.0412 0.0298  1150 SER B O   
17108 C CB  . SER B 1152 ? 0.3833 0.3282 0.4736 -0.0565 -0.0517 0.0150  1150 SER B CB  
17109 O OG  . SER B 1152 ? 0.4083 0.3699 0.5017 -0.0543 -0.0445 0.0148  1150 SER B OG  
17110 N N   . TRP B 1153 ? 0.3421 0.2915 0.4447 -0.0709 -0.0508 0.0323  1151 TRP B N   
17111 C CA  . TRP B 1153 ? 0.3480 0.3101 0.4592 -0.0773 -0.0468 0.0401  1151 TRP B CA  
17112 C C   . TRP B 1153 ? 0.3823 0.3589 0.5050 -0.0813 -0.0457 0.0401  1151 TRP B C   
17113 O O   . TRP B 1153 ? 0.3910 0.3624 0.5169 -0.0832 -0.0515 0.0371  1151 TRP B O   
17114 C CB  . TRP B 1153 ? 0.3950 0.3463 0.5077 -0.0841 -0.0517 0.0468  1151 TRP B CB  
17115 C CG  . TRP B 1153 ? 0.4166 0.3549 0.5189 -0.0803 -0.0524 0.0478  1151 TRP B CG  
17116 C CD1 . TRP B 1153 ? 0.3893 0.3093 0.4821 -0.0754 -0.0578 0.0431  1151 TRP B CD1 
17117 C CD2 . TRP B 1153 ? 0.4058 0.3489 0.5060 -0.0806 -0.0476 0.0538  1151 TRP B CD2 
17118 N NE1 . TRP B 1153 ? 0.4247 0.3379 0.5103 -0.0725 -0.0568 0.0459  1151 TRP B NE1 
17119 C CE2 . TRP B 1153 ? 0.4450 0.3719 0.5348 -0.0759 -0.0507 0.0526  1151 TRP B CE2 
17120 C CE3 . TRP B 1153 ? 0.3785 0.3378 0.4841 -0.0844 -0.0410 0.0602  1151 TRP B CE3 
17121 C CZ2 . TRP B 1153 ? 0.4590 0.3856 0.5443 -0.0749 -0.0479 0.0578  1151 TRP B CZ2 
17122 C CZ3 . TRP B 1153 ? 0.3846 0.3433 0.4848 -0.0836 -0.0381 0.0652  1151 TRP B CZ3 
17123 C CH2 . TRP B 1153 ? 0.4283 0.3707 0.5186 -0.0790 -0.0417 0.0640  1151 TRP B CH2 
17124 N N   . SER B 1154 ? 0.3419 0.3365 0.4706 -0.0822 -0.0384 0.0433  1152 SER B N   
17125 C CA  . SER B 1154 ? 0.3306 0.3406 0.4706 -0.0850 -0.0365 0.0433  1152 SER B CA  
17126 C C   . SER B 1154 ? 0.2769 0.2995 0.4273 -0.0926 -0.0334 0.0519  1152 SER B C   
17127 O O   . SER B 1154 ? 0.3138 0.3433 0.4621 -0.0924 -0.0274 0.0561  1152 SER B O   
17128 C CB  . SER B 1154 ? 0.3154 0.3373 0.4536 -0.0781 -0.0302 0.0382  1152 SER B CB  
17129 O OG  . SER B 1154 ? 0.3123 0.3492 0.4620 -0.0806 -0.0285 0.0385  1152 SER B OG  
17130 N N   . LYS B 1155 ? 0.3353 0.3616 0.4970 -0.0993 -0.0373 0.0545  1153 LYS B N   
17131 C CA  . LYS B 1155 ? 0.3275 0.3694 0.5016 -0.1066 -0.0339 0.0622  1153 LYS B CA  
17132 C C   . LYS B 1155 ? 0.3117 0.3729 0.4958 -0.1051 -0.0295 0.0601  1153 LYS B C   
17133 O O   . LYS B 1155 ? 0.3904 0.4666 0.5865 -0.1108 -0.0268 0.0659  1153 LYS B O   
17134 C CB  . LYS B 1155 ? 0.3663 0.4002 0.5476 -0.1159 -0.0416 0.0675  1153 LYS B CB  
17135 N N   . ASP B 1156 ? 0.3019 0.3627 0.4812 -0.0977 -0.0289 0.0521  1154 ASP B N   
17136 C CA  . ASP B 1156 ? 0.2601 0.3366 0.4485 -0.0957 -0.0262 0.0492  1154 ASP B CA  
17137 C C   . ASP B 1156 ? 0.2744 0.3496 0.4527 -0.0862 -0.0228 0.0416  1154 ASP B C   
17138 O O   . ASP B 1156 ? 0.2805 0.3459 0.4538 -0.0825 -0.0275 0.0354  1154 ASP B O   
17139 C CB  . ASP B 1156 ? 0.2583 0.3317 0.4549 -0.0995 -0.0340 0.0478  1154 ASP B CB  
17140 C CG  . ASP B 1156 ? 0.2250 0.3162 0.4332 -0.0984 -0.0314 0.0462  1154 ASP B CG  
17141 O OD1 . ASP B 1156 ? 0.2557 0.3568 0.4618 -0.0921 -0.0248 0.0431  1154 ASP B OD1 
17142 O OD2 . ASP B 1156 ? 0.3011 0.3963 0.5208 -0.1039 -0.0363 0.0483  1154 ASP B OD2 
17143 N N   . TRP B 1157 ? 0.2213 0.3063 0.3964 -0.0827 -0.0149 0.0424  1155 TRP B N   
17144 C CA  . TRP B 1157 ? 0.2462 0.3286 0.4109 -0.0743 -0.0120 0.0359  1155 TRP B CA  
17145 C C   . TRP B 1157 ? 0.2849 0.3726 0.4532 -0.0703 -0.0126 0.0299  1155 TRP B C   
17146 O O   . TRP B 1157 ? 0.2663 0.3460 0.4263 -0.0646 -0.0142 0.0237  1155 TRP B O   
17147 C CB  . TRP B 1157 ? 0.2300 0.3225 0.3910 -0.0717 -0.0036 0.0379  1155 TRP B CB  
17148 C CG  . TRP B 1157 ? 0.2741 0.3621 0.4302 -0.0749 -0.0023 0.0439  1155 TRP B CG  
17149 C CD1 . TRP B 1157 ? 0.2682 0.3423 0.4216 -0.0791 -0.0077 0.0473  1155 TRP B CD1 
17150 C CD2 . TRP B 1157 ? 0.2662 0.3634 0.4189 -0.0739 0.0049  0.0472  1155 TRP B CD2 
17151 N NE1 . TRP B 1157 ? 0.2618 0.3362 0.4109 -0.0810 -0.0044 0.0529  1155 TRP B NE1 
17152 C CE2 . TRP B 1157 ? 0.2663 0.3550 0.4147 -0.0778 0.0035  0.0530  1155 TRP B CE2 
17153 C CE3 . TRP B 1157 ? 0.2841 0.3954 0.4367 -0.0699 0.0123  0.0457  1155 TRP B CE3 
17154 C CZ2 . TRP B 1157 ? 0.2997 0.3939 0.4433 -0.0780 0.0091  0.0576  1155 TRP B CZ2 
17155 C CZ3 . TRP B 1157 ? 0.2753 0.3918 0.4227 -0.0700 0.0179  0.0498  1155 TRP B CZ3 
17156 C CH2 . TRP B 1157 ? 0.3034 0.4118 0.4466 -0.0742 0.0163  0.0559  1155 TRP B CH2 
17157 N N   . ALA B 1158 ? 0.2459 0.3479 0.4271 -0.0730 -0.0114 0.0318  1156 ALA B N   
17158 C CA  . ALA B 1158 ? 0.2926 0.4001 0.4773 -0.0686 -0.0119 0.0263  1156 ALA B CA  
17159 C C   . ALA B 1158 ? 0.2770 0.3721 0.4609 -0.0692 -0.0206 0.0226  1156 ALA B C   
17160 O O   . ALA B 1158 ? 0.3061 0.3988 0.4863 -0.0641 -0.0219 0.0167  1156 ALA B O   
17161 C CB  . ALA B 1158 ? 0.2136 0.3405 0.4128 -0.0706 -0.0083 0.0292  1156 ALA B CB  
17162 N N   . ALA B 1159 ? 0.2753 0.3623 0.4622 -0.0756 -0.0266 0.0261  1157 ALA B N   
17163 C CA  . ALA B 1159 ? 0.2720 0.3464 0.4574 -0.0766 -0.0353 0.0225  1157 ALA B CA  
17164 C C   . ALA B 1159 ? 0.3038 0.3597 0.4738 -0.0724 -0.0382 0.0180  1157 ALA B C   
17165 O O   . ALA B 1159 ? 0.3102 0.3564 0.4757 -0.0702 -0.0438 0.0131  1157 ALA B O   
17166 C CB  . ALA B 1159 ? 0.2723 0.3446 0.4669 -0.0853 -0.0412 0.0278  1157 ALA B CB  
17167 N N   . ASP B 1160 ? 0.2946 0.3457 0.4565 -0.0710 -0.0346 0.0197  1158 ASP B N   
17168 C CA  . ASP B 1160 ? 0.3193 0.3536 0.4673 -0.0670 -0.0371 0.0159  1158 ASP B CA  
17169 C C   . ASP B 1160 ? 0.3269 0.3625 0.4660 -0.0591 -0.0325 0.0108  1158 ASP B C   
17170 O O   . ASP B 1160 ? 0.3317 0.3552 0.4597 -0.0551 -0.0341 0.0073  1158 ASP B O   
17171 C CB  . ASP B 1160 ? 0.3038 0.3309 0.4480 -0.0701 -0.0369 0.0209  1158 ASP B CB  
17172 C CG  . ASP B 1160 ? 0.3448 0.3663 0.4960 -0.0781 -0.0431 0.0255  1158 ASP B CG  
17173 O OD1 . ASP B 1160 ? 0.3878 0.4064 0.5435 -0.0802 -0.0491 0.0234  1158 ASP B OD1 
17174 O OD2 . ASP B 1160 ? 0.3762 0.3960 0.5282 -0.0824 -0.0423 0.0315  1158 ASP B OD2 
17175 N N   . GLY B 1161 ? 0.2882 0.3382 0.4320 -0.0568 -0.0269 0.0101  1159 GLY B N   
17176 C CA  . GLY B 1161 ? 0.2953 0.3466 0.4313 -0.0499 -0.0231 0.0054  1159 GLY B CA  
17177 C C   . GLY B 1161 ? 0.3667 0.4123 0.4999 -0.0466 -0.0275 -0.0004 1159 GLY B C   
17178 O O   . GLY B 1161 ? 0.3880 0.4273 0.5238 -0.0494 -0.0338 -0.0010 1159 GLY B O   
17179 N N   . PRO B 1162 ? 0.3722 0.4199 0.4997 -0.0409 -0.0244 -0.0046 1160 PRO B N   
17180 C CA  . PRO B 1162 ? 0.3372 0.3928 0.4618 -0.0374 -0.0174 -0.0046 1160 PRO B CA  
17181 C C   . PRO B 1162 ? 0.3304 0.3778 0.4451 -0.0359 -0.0159 -0.0039 1160 PRO B C   
17182 O O   . PRO B 1162 ? 0.3594 0.3945 0.4671 -0.0349 -0.0199 -0.0057 1160 PRO B O   
17183 C CB  . PRO B 1162 ? 0.3887 0.4453 0.5099 -0.0324 -0.0171 -0.0099 1160 PRO B CB  
17184 C CG  . PRO B 1162 ? 0.3452 0.3887 0.4606 -0.0317 -0.0235 -0.0131 1160 PRO B CG  
17185 C CD  . PRO B 1162 ? 0.4344 0.4749 0.5566 -0.0374 -0.0284 -0.0100 1160 PRO B CD  
17186 N N   . PHE B 1163 ? 0.2741 0.3286 0.3883 -0.0357 -0.0103 -0.0012 1161 PHE B N   
17187 C CA  . PHE B 1163 ? 0.3005 0.3492 0.4055 -0.0335 -0.0085 -0.0006 1161 PHE B CA  
17188 C C   . PHE B 1163 ? 0.2816 0.3338 0.3805 -0.0282 -0.0046 -0.0043 1161 PHE B C   
17189 O O   . PHE B 1163 ? 0.3021 0.3614 0.4041 -0.0264 -0.0030 -0.0069 1161 PHE B O   
17190 C CB  . PHE B 1163 ? 0.2832 0.3364 0.3908 -0.0373 -0.0054 0.0055  1161 PHE B CB  
17191 C CG  . PHE B 1163 ? 0.3018 0.3519 0.4160 -0.0433 -0.0093 0.0098  1161 PHE B CG  
17192 C CD1 . PHE B 1163 ? 0.2969 0.3327 0.4070 -0.0443 -0.0151 0.0096  1161 PHE B CD1 
17193 C CD2 . PHE B 1163 ? 0.2905 0.3519 0.4152 -0.0479 -0.0074 0.0139  1161 PHE B CD2 
17194 C CE1 . PHE B 1163 ? 0.3324 0.3641 0.4483 -0.0503 -0.0193 0.0135  1161 PHE B CE1 
17195 C CE2 . PHE B 1163 ? 0.2810 0.3397 0.4123 -0.0541 -0.0113 0.0183  1161 PHE B CE2 
17196 C CZ  . PHE B 1163 ? 0.3337 0.3770 0.4606 -0.0555 -0.0176 0.0181  1161 PHE B CZ  
17197 N N   . ALA B 1164 ? 0.3087 0.3554 0.3991 -0.0256 -0.0036 -0.0046 1162 ALA B N   
17198 C CA  . ALA B 1164 ? 0.3004 0.3493 0.3846 -0.0209 -0.0006 -0.0079 1162 ALA B CA  
17199 C C   . ALA B 1164 ? 0.3220 0.3770 0.4036 -0.0205 0.0042  -0.0053 1162 ALA B C   
17200 O O   . ALA B 1164 ? 0.3284 0.3851 0.4046 -0.0171 0.0065  -0.0076 1162 ALA B O   
17201 C CB  . ALA B 1164 ? 0.3069 0.3451 0.3829 -0.0176 -0.0035 -0.0110 1162 ALA B CB  
17202 N N   . GLY B 1165 ? 0.2844 0.3426 0.3695 -0.0242 0.0056  -0.0004 1163 GLY B N   
17203 C CA  . GLY B 1165 ? 0.2693 0.3327 0.3512 -0.0241 0.0099  0.0026  1163 GLY B CA  
17204 C C   . GLY B 1165 ? 0.2747 0.3387 0.3605 -0.0290 0.0099  0.0087  1163 GLY B C   
17205 O O   . GLY B 1165 ? 0.2672 0.3266 0.3579 -0.0323 0.0062  0.0103  1163 GLY B O   
17206 N N   . ALA B 1166 ? 0.2792 0.3487 0.3626 -0.0296 0.0138  0.0122  1164 ALA B N   
17207 C CA  . ALA B 1166 ? 0.2784 0.3487 0.3648 -0.0345 0.0141  0.0187  1164 ALA B CA  
17208 C C   . ALA B 1166 ? 0.2356 0.3058 0.3147 -0.0337 0.0166  0.0219  1164 ALA B C   
17209 O O   . ALA B 1166 ? 0.2916 0.3679 0.3662 -0.0307 0.0203  0.0200  1164 ALA B O   
17210 C CB  . ALA B 1166 ? 0.2611 0.3435 0.3565 -0.0380 0.0173  0.0212  1164 ALA B CB  
17211 N N   . LEU B 1167 ? 0.2309 0.2937 0.3086 -0.0365 0.0141  0.0267  1165 LEU B N   
17212 C CA  . LEU B 1167 ? 0.3039 0.3663 0.3753 -0.0366 0.0158  0.0310  1165 LEU B CA  
17213 C C   . LEU B 1167 ? 0.2907 0.3574 0.3667 -0.0426 0.0173  0.0383  1165 LEU B C   
17214 O O   . LEU B 1167 ? 0.2978 0.3594 0.3794 -0.0467 0.0138  0.0409  1165 LEU B O   
17215 C CB  . LEU B 1167 ? 0.2655 0.3147 0.3306 -0.0342 0.0114  0.0308  1165 LEU B CB  
17216 C CG  . LEU B 1167 ? 0.2798 0.3244 0.3404 -0.0285 0.0098  0.0243  1165 LEU B CG  
17217 C CD1 . LEU B 1167 ? 0.2787 0.3123 0.3333 -0.0259 0.0063  0.0251  1165 LEU B CD1 
17218 C CD2 . LEU B 1167 ? 0.2569 0.3108 0.3141 -0.0253 0.0140  0.0214  1165 LEU B CD2 
17219 N N   . VAL B 1168 ? 0.2945 0.3707 0.3681 -0.0433 0.0223  0.0416  1166 VAL B N   
17220 C CA  . VAL B 1168 ? 0.3069 0.3896 0.3850 -0.0491 0.0247  0.0487  1166 VAL B CA  
17221 C C   . VAL B 1168 ? 0.3057 0.3869 0.3759 -0.0498 0.0261  0.0542  1166 VAL B C   
17222 O O   . VAL B 1168 ? 0.3118 0.3953 0.3743 -0.0457 0.0283  0.0520  1166 VAL B O   
17223 C CB  . VAL B 1168 ? 0.2812 0.3795 0.3650 -0.0497 0.0305  0.0480  1166 VAL B CB  
17224 C CG1 . VAL B 1168 ? 0.3224 0.4288 0.4117 -0.0560 0.0333  0.0558  1166 VAL B CG1 
17225 C CG2 . VAL B 1168 ? 0.2692 0.3692 0.3605 -0.0483 0.0289  0.0421  1166 VAL B CG2 
17226 N N   . GLU B 1169 ? 0.3046 0.3819 0.3767 -0.0552 0.0244  0.0615  1167 GLU B N   
17227 C CA  . GLU B 1169 ? 0.3348 0.4113 0.4002 -0.0568 0.0257  0.0681  1167 GLU B CA  
17228 C C   . GLU B 1169 ? 0.3477 0.4354 0.4181 -0.0629 0.0300  0.0751  1167 GLU B C   
17229 O O   . GLU B 1169 ? 0.3434 0.4314 0.4228 -0.0681 0.0284  0.0780  1167 GLU B O   
17230 C CB  . GLU B 1169 ? 0.3509 0.4115 0.4133 -0.0579 0.0193  0.0713  1167 GLU B CB  
17231 C CG  . GLU B 1169 ? 0.3595 0.4178 0.4153 -0.0599 0.0197  0.0789  1167 GLU B CG  
17232 C CD  . GLU B 1169 ? 0.3759 0.4180 0.4306 -0.0620 0.0131  0.0831  1167 GLU B CD  
17233 O OE1 . GLU B 1169 ? 0.3470 0.3804 0.4069 -0.0629 0.0085  0.0806  1167 GLU B OE1 
17234 O OE2 . GLU B 1169 ? 0.4300 0.4677 0.4784 -0.0628 0.0123  0.0889  1167 GLU B OE2 
17235 N N   . GLY B 1170 ? 0.3695 0.4668 0.4343 -0.0625 0.0354  0.0778  1168 GLY B N   
17236 C CA  . GLY B 1170 ? 0.3638 0.4718 0.4324 -0.0683 0.0399  0.0852  1168 GLY B CA  
17237 C C   . GLY B 1170 ? 0.3781 0.4978 0.4392 -0.0661 0.0466  0.0859  1168 GLY B C   
17238 O O   . GLY B 1170 ? 0.3872 0.5066 0.4404 -0.0603 0.0474  0.0803  1168 GLY B O   
17239 N N   . ASP B 1171 ? 0.4180 0.5483 0.4814 -0.0712 0.0513  0.0930  1169 ASP B N   
17240 C CA  . ASP B 1171 ? 0.4198 0.5627 0.4762 -0.0691 0.0582  0.0933  1169 ASP B CA  
17241 C C   . ASP B 1171 ? 0.4151 0.5703 0.4766 -0.0653 0.0630  0.0863  1169 ASP B C   
17242 O O   . ASP B 1171 ? 0.3949 0.5490 0.4654 -0.0646 0.0607  0.0816  1169 ASP B O   
17243 C CB  . ASP B 1171 ? 0.4536 0.6040 0.5097 -0.0754 0.0621  0.1036  1169 ASP B CB  
17244 C CG  . ASP B 1171 ? 0.5005 0.6594 0.5703 -0.0817 0.0638  0.1081  1169 ASP B CG  
17245 O OD1 . ASP B 1171 ? 0.4351 0.5964 0.5148 -0.0807 0.0629  0.1029  1169 ASP B OD1 
17246 O OD2 . ASP B 1171 ? 0.4959 0.6594 0.5666 -0.0879 0.0661  0.1174  1169 ASP B OD2 
17247 N N   . ALA B 1172 ? 0.4105 0.5773 0.4658 -0.0627 0.0694  0.0854  1170 ALA B N   
17248 C CA  . ALA B 1172 ? 0.3943 0.5718 0.4528 -0.0581 0.0738  0.0781  1170 ALA B CA  
17249 C C   . ALA B 1172 ? 0.4007 0.5876 0.4740 -0.0614 0.0756  0.0793  1170 ALA B C   
17250 O O   . ALA B 1172 ? 0.4232 0.6116 0.5030 -0.0581 0.0748  0.0725  1170 ALA B O   
17251 C CB  . ALA B 1172 ? 0.4439 0.6323 0.4926 -0.0552 0.0807  0.0778  1170 ALA B CB  
17252 N N   . GLU B 1173 ? 0.3809 0.5743 0.4599 -0.0681 0.0778  0.0882  1171 GLU B N   
17253 C CA  . GLU B 1173 ? 0.3819 0.5856 0.4759 -0.0718 0.0794  0.0901  1171 GLU B CA  
17254 C C   . GLU B 1173 ? 0.3655 0.5579 0.4684 -0.0732 0.0718  0.0874  1171 GLU B C   
17255 O O   . GLU B 1173 ? 0.3659 0.5638 0.4786 -0.0717 0.0717  0.0827  1171 GLU B O   
17256 C CB  . GLU B 1173 ? 0.4485 0.6608 0.5469 -0.0796 0.0828  0.1011  1171 GLU B CB  
17257 N N   . ARG B 1174 ? 0.3572 0.5337 0.4565 -0.0759 0.0652  0.0902  1172 ARG B N   
17258 C CA  . ARG B 1174 ? 0.3490 0.5132 0.4547 -0.0768 0.0577  0.0872  1172 ARG B CA  
17259 C C   . ARG B 1174 ? 0.3270 0.4880 0.4312 -0.0695 0.0561  0.0767  1172 ARG B C   
17260 O O   . ARG B 1174 ? 0.3488 0.5093 0.4620 -0.0694 0.0533  0.0729  1172 ARG B O   
17261 C CB  . ARG B 1174 ? 0.3917 0.5385 0.4913 -0.0794 0.0512  0.0911  1172 ARG B CB  
17262 C CG  . ARG B 1174 ? 0.3739 0.5062 0.4778 -0.0796 0.0432  0.0876  1172 ARG B CG  
17263 C CD  . ARG B 1174 ? 0.4117 0.5479 0.5293 -0.0861 0.0414  0.0911  1172 ARG B CD  
17264 N NE  . ARG B 1174 ? 0.4143 0.5362 0.5351 -0.0861 0.0335  0.0873  1172 ARG B NE  
17265 C CZ  . ARG B 1174 ? 0.4175 0.5409 0.5498 -0.0898 0.0304  0.0871  1172 ARG B CZ  
17266 N NH1 . ARG B 1174 ? 0.3562 0.4955 0.4993 -0.0939 0.0345  0.0907  1172 ARG B NH1 
17267 N NH2 . ARG B 1174 ? 0.4023 0.5114 0.5352 -0.0890 0.0231  0.0829  1172 ARG B NH2 
17268 N N   . ILE B 1175 ? 0.2857 0.4446 0.3785 -0.0635 0.0579  0.0721  1173 ILE B N   
17269 C CA  . ILE B 1175 ? 0.3762 0.5310 0.4668 -0.0570 0.0560  0.0626  1173 ILE B CA  
17270 C C   . ILE B 1175 ? 0.3541 0.5217 0.4527 -0.0546 0.0600  0.0582  1173 ILE B C   
17271 O O   . ILE B 1175 ? 0.3237 0.4883 0.4279 -0.0525 0.0568  0.0526  1173 ILE B O   
17272 C CB  . ILE B 1175 ? 0.3883 0.5392 0.4652 -0.0518 0.0571  0.0594  1173 ILE B CB  
17273 C CG1 . ILE B 1175 ? 0.3952 0.5314 0.4653 -0.0529 0.0516  0.0623  1173 ILE B CG1 
17274 C CG2 . ILE B 1175 ? 0.3695 0.5198 0.4444 -0.0453 0.0567  0.0500  1173 ILE B CG2 
17275 C CD1 . ILE B 1175 ? 0.4128 0.5470 0.4700 -0.0491 0.0528  0.0613  1173 ILE B CD1 
17276 N N   . ARG B 1176 ? 0.3161 0.4986 0.4157 -0.0549 0.0670  0.0607  1174 ARG B N   
17277 C CA  . ARG B 1176 ? 0.3388 0.5346 0.4466 -0.0522 0.0712  0.0567  1174 ARG B CA  
17278 C C   . ARG B 1176 ? 0.2962 0.4943 0.4188 -0.0563 0.0681  0.0584  1174 ARG B C   
17279 O O   . ARG B 1176 ? 0.3158 0.5154 0.4446 -0.0531 0.0667  0.0525  1174 ARG B O   
17280 C CB  . ARG B 1176 ? 0.3401 0.5518 0.4462 -0.0521 0.0795  0.0600  1174 ARG B CB  
17281 C CG  . ARG B 1176 ? 0.3801 0.6068 0.4946 -0.0485 0.0845  0.0560  1174 ARG B CG  
17282 C CD  . ARG B 1176 ? 0.4277 0.6716 0.5421 -0.0492 0.0932  0.0605  1174 ARG B CD  
17283 N NE  . ARG B 1176 ? 0.5369 0.7784 0.6363 -0.0482 0.0960  0.0623  1174 ARG B NE  
17284 C CZ  . ARG B 1176 ? 0.5656 0.8074 0.6536 -0.0417 0.0989  0.0562  1174 ARG B CZ  
17285 N NH1 . ARG B 1176 ? 0.5631 0.8080 0.6529 -0.0353 0.0999  0.0480  1174 ARG B NH1 
17286 N NH2 . ARG B 1176 ? 0.5432 0.7815 0.6175 -0.0416 0.1002  0.0585  1174 ARG B NH2 
17287 N N   . ALA B 1177 ? 0.2958 0.4934 0.4241 -0.0637 0.0665  0.0665  1175 ALA B N   
17288 C CA  . ALA B 1177 ? 0.3244 0.5242 0.4671 -0.0685 0.0631  0.0687  1175 ALA B CA  
17289 C C   . ALA B 1177 ? 0.2707 0.4553 0.4141 -0.0671 0.0550  0.0633  1175 ALA B C   
17290 O O   . ALA B 1177 ? 0.2885 0.4760 0.4420 -0.0671 0.0527  0.0605  1175 ALA B O   
17291 C CB  . ALA B 1177 ? 0.2887 0.4895 0.4360 -0.0772 0.0626  0.0789  1175 ALA B CB  
17292 N N   . VAL B 1178 ? 0.2827 0.4516 0.4156 -0.0659 0.0507  0.0621  1176 VAL B N   
17293 C CA  . VAL B 1178 ? 0.2756 0.4301 0.4080 -0.0642 0.0435  0.0570  1176 VAL B CA  
17294 C C   . VAL B 1178 ? 0.3041 0.4604 0.4349 -0.0570 0.0443  0.0481  1176 VAL B C   
17295 O O   . VAL B 1178 ? 0.2994 0.4522 0.4358 -0.0561 0.0402  0.0439  1176 VAL B O   
17296 C CB  . VAL B 1178 ? 0.2764 0.4147 0.3982 -0.0643 0.0392  0.0582  1176 VAL B CB  
17297 C CG1 . VAL B 1178 ? 0.3139 0.4378 0.4337 -0.0615 0.0324  0.0524  1176 VAL B CG1 
17298 C CG2 . VAL B 1178 ? 0.3194 0.4547 0.4436 -0.0718 0.0376  0.0673  1176 VAL B CG2 
17299 N N   . ASN B 1179 ? 0.2967 0.4580 0.4193 -0.0521 0.0493  0.0453  1177 ASN B N   
17300 C CA  . ASN B 1179 ? 0.3005 0.4636 0.4210 -0.0455 0.0503  0.0372  1177 ASN B CA  
17301 C C   . ASN B 1179 ? 0.3043 0.4793 0.4368 -0.0450 0.0521  0.0354  1177 ASN B C   
17302 O O   . ASN B 1179 ? 0.2645 0.4371 0.3995 -0.0414 0.0495  0.0294  1177 ASN B O   
17303 C CB  . ASN B 1179 ? 0.3076 0.4747 0.4173 -0.0412 0.0555  0.0354  1177 ASN B CB  
17304 C CG  . ASN B 1179 ? 0.3564 0.5200 0.4605 -0.0346 0.0549  0.0272  1177 ASN B CG  
17305 O OD1 . ASN B 1179 ? 0.3478 0.5010 0.4512 -0.0332 0.0497  0.0233  1177 ASN B OD1 
17306 N ND2 . ASN B 1179 ? 0.3489 0.5208 0.4484 -0.0306 0.0602  0.0245  1177 ASN B ND2 
17307 N N   . LYS B 1180 ? 0.2911 0.4796 0.4317 -0.0488 0.0565  0.0410  1178 LYS B N   
17308 C CA  . LYS B 1180 ? 0.2848 0.4861 0.4384 -0.0486 0.0583  0.0401  1178 LYS B CA  
17309 C C   . LYS B 1180 ? 0.2529 0.4483 0.4163 -0.0523 0.0514  0.0404  1178 LYS B C   
17310 O O   . LYS B 1180 ? 0.2613 0.4601 0.4319 -0.0497 0.0498  0.0360  1178 LYS B O   
17311 C CB  . LYS B 1180 ? 0.2806 0.4987 0.4406 -0.0520 0.0650  0.0466  1178 LYS B CB  
17312 C CG  . LYS B 1180 ? 0.3639 0.5913 0.5158 -0.0471 0.0727  0.0449  1178 LYS B CG  
17313 C CD  . LYS B 1180 ? 0.4264 0.6706 0.5839 -0.0509 0.0797  0.0522  1178 LYS B CD  
17314 C CE  . LYS B 1180 ? 0.5179 0.7778 0.6911 -0.0511 0.0821  0.0525  1178 LYS B CE  
17315 N NZ  . LYS B 1180 ? 0.5438 0.8089 0.7161 -0.0425 0.0848  0.0440  1178 LYS B NZ  
17316 N N   . ALA B 1181 ? 0.2738 0.4598 0.4373 -0.0583 0.0468  0.0455  1179 ALA B N   
17317 C CA  . ALA B 1181 ? 0.2600 0.4384 0.4313 -0.0618 0.0395  0.0453  1179 ALA B CA  
17318 C C   . ALA B 1181 ? 0.2535 0.4188 0.4184 -0.0567 0.0344  0.0376  1179 ALA B C   
17319 O O   . ALA B 1181 ? 0.2438 0.4079 0.4157 -0.0564 0.0301  0.0345  1179 ALA B O   
17320 C CB  . ALA B 1181 ? 0.2977 0.4673 0.4690 -0.0692 0.0355  0.0522  1179 ALA B CB  
17321 N N   . ILE B 1182 ? 0.2378 0.3938 0.3897 -0.0526 0.0347  0.0345  1180 ILE B N   
17322 C CA  . ILE B 1182 ? 0.2869 0.4313 0.4326 -0.0479 0.0304  0.0276  1180 ILE B CA  
17323 C C   . ILE B 1182 ? 0.2877 0.4398 0.4363 -0.0425 0.0325  0.0217  1180 ILE B C   
17324 O O   . ILE B 1182 ? 0.2844 0.4314 0.4353 -0.0407 0.0280  0.0173  1180 ILE B O   
17325 C CB  . ILE B 1182 ? 0.3026 0.4367 0.4344 -0.0450 0.0305  0.0263  1180 ILE B CB  
17326 C CG1 . ILE B 1182 ? 0.2813 0.4044 0.4104 -0.0497 0.0266  0.0312  1180 ILE B CG1 
17327 C CG2 . ILE B 1182 ? 0.3235 0.4493 0.4489 -0.0393 0.0279  0.0189  1180 ILE B CG2 
17328 C CD1 . ILE B 1182 ? 0.2930 0.4086 0.4100 -0.0475 0.0273  0.0316  1180 ILE B CD1 
17329 N N   . ALA B 1183 ? 0.3096 0.4738 0.4580 -0.0398 0.0391  0.0215  1181 ALA B N   
17330 C CA  . ALA B 1183 ? 0.3137 0.4851 0.4651 -0.0344 0.0411  0.0159  1181 ALA B CA  
17331 C C   . ALA B 1183 ? 0.2865 0.4648 0.4518 -0.0360 0.0387  0.0161  1181 ALA B C   
17332 O O   . ALA B 1183 ? 0.2932 0.4730 0.4609 -0.0316 0.0377  0.0109  1181 ALA B O   
17333 C CB  . ALA B 1183 ? 0.3034 0.4870 0.4523 -0.0313 0.0488  0.0159  1181 ALA B CB  
17334 N N   . ALA B 1184 ? 0.2574 0.4396 0.4319 -0.0425 0.0373  0.0221  1182 ALA B N   
17335 C CA  . ALA B 1184 ? 0.2963 0.4856 0.4849 -0.0448 0.0345  0.0229  1182 ALA B CA  
17336 C C   . ALA B 1184 ? 0.2859 0.4616 0.4752 -0.0469 0.0258  0.0212  1182 ALA B C   
17337 O O   . ALA B 1184 ? 0.2645 0.4446 0.4649 -0.0490 0.0223  0.0216  1182 ALA B O   
17338 C CB  . ALA B 1184 ? 0.2321 0.4340 0.4316 -0.0513 0.0373  0.0307  1182 ALA B CB  
17339 N N   . LEU B 1185 ? 0.2676 0.4274 0.4453 -0.0464 0.0223  0.0193  1183 LEU B N   
17340 C CA  . LEU B 1185 ? 0.3043 0.4510 0.4815 -0.0479 0.0143  0.0174  1183 LEU B CA  
17341 C C   . LEU B 1185 ? 0.3093 0.4551 0.4871 -0.0427 0.0119  0.0109  1183 LEU B C   
17342 O O   . LEU B 1185 ? 0.2949 0.4439 0.4680 -0.0370 0.0157  0.0069  1183 LEU B O   
17343 C CB  . LEU B 1185 ? 0.3060 0.4366 0.4705 -0.0478 0.0117  0.0168  1183 LEU B CB  
17344 C CG  . LEU B 1185 ? 0.3069 0.4349 0.4691 -0.0527 0.0127  0.0230  1183 LEU B CG  
17345 C CD1 . LEU B 1185 ? 0.2375 0.3499 0.3864 -0.0506 0.0104  0.0211  1183 LEU B CD1 
17346 C CD2 . LEU B 1185 ? 0.2938 0.4215 0.4659 -0.0599 0.0083  0.0280  1183 LEU B CD2 
17347 N N   . PRO B 1186 ? 0.3226 0.4634 0.5056 -0.0447 0.0054  0.0099  1184 PRO B N   
17348 C CA  . PRO B 1186 ? 0.3645 0.5030 0.5470 -0.0400 0.0024  0.0041  1184 PRO B CA  
17349 C C   . PRO B 1186 ? 0.2862 0.4100 0.4546 -0.0361 0.0003  -0.0005 1184 PRO B C   
17350 O O   . PRO B 1186 ? 0.3238 0.4374 0.4841 -0.0376 -0.0007 0.0006  1184 PRO B O   
17351 C CB  . PRO B 1186 ? 0.3284 0.4657 0.5205 -0.0443 -0.0045 0.0053  1184 PRO B CB  
17352 C CG  . PRO B 1186 ? 0.3606 0.4907 0.5517 -0.0506 -0.0071 0.0100  1184 PRO B CG  
17353 C CD  . PRO B 1186 ? 0.3306 0.4680 0.5204 -0.0516 0.0000  0.0142  1184 PRO B CD  
17354 N N   . GLY B 1187 ? 0.3077 0.4307 0.4737 -0.0310 -0.0003 -0.0056 1185 GLY B N   
17355 C CA  . GLY B 1187 ? 0.3204 0.4307 0.4741 -0.0275 -0.0024 -0.0098 1185 GLY B CA  
17356 C C   . GLY B 1187 ? 0.3154 0.4261 0.4601 -0.0236 0.0031  -0.0114 1185 GLY B C   
17357 O O   . GLY B 1187 ? 0.3366 0.4576 0.4842 -0.0212 0.0081  -0.0117 1185 GLY B O   
17358 N N   . PRO B 1188 ? 0.3625 0.4624 0.4964 -0.0227 0.0022  -0.0125 1186 PRO B N   
17359 C CA  . PRO B 1188 ? 0.3250 0.4245 0.4500 -0.0189 0.0064  -0.0145 1186 PRO B CA  
17360 C C   . PRO B 1188 ? 0.3304 0.4376 0.4558 -0.0202 0.0120  -0.0109 1186 PRO B C   
17361 O O   . PRO B 1188 ? 0.3033 0.4122 0.4325 -0.0245 0.0122  -0.0063 1186 PRO B O   
17362 C CB  . PRO B 1188 ? 0.3616 0.4481 0.4765 -0.0184 0.0034  -0.0158 1186 PRO B CB  
17363 C CG  . PRO B 1188 ? 0.4093 0.4908 0.5271 -0.0228 -0.0003 -0.0126 1186 PRO B CG  
17364 C CD  . PRO B 1188 ? 0.3661 0.4541 0.4955 -0.0254 -0.0025 -0.0115 1186 PRO B CD  
17365 N N   . LEU B 1189 ? 0.3158 0.4268 0.4362 -0.0165 0.0163  -0.0130 1187 LEU B N   
17366 C CA  . LEU B 1189 ? 0.3389 0.4564 0.4571 -0.0171 0.0217  -0.0102 1187 LEU B CA  
17367 C C   . LEU B 1189 ? 0.3364 0.4452 0.4456 -0.0182 0.0210  -0.0085 1187 LEU B C   
17368 O O   . LEU B 1189 ? 0.3445 0.4459 0.4456 -0.0154 0.0197  -0.0116 1187 LEU B O   
17369 C CB  . LEU B 1189 ? 0.3317 0.4552 0.4468 -0.0125 0.0260  -0.0136 1187 LEU B CB  
17370 C CG  . LEU B 1189 ? 0.3241 0.4585 0.4479 -0.0104 0.0282  -0.0151 1187 LEU B CG  
17371 C CD1 . LEU B 1189 ? 0.4111 0.5420 0.5395 -0.0089 0.0235  -0.0184 1187 LEU B CD1 
17372 C CD2 . LEU B 1189 ? 0.3197 0.4587 0.4382 -0.0060 0.0329  -0.0181 1187 LEU B CD2 
17373 N N   . LEU B 1190 ? 0.2855 0.3952 0.3963 -0.0222 0.0218  -0.0033 1188 LEU B N   
17374 C CA  . LEU B 1190 ? 0.3251 0.4259 0.4280 -0.0231 0.0205  -0.0014 1188 LEU B CA  
17375 C C   . LEU B 1190 ? 0.3075 0.4111 0.4025 -0.0210 0.0248  -0.0012 1188 LEU B C   
17376 O O   . LEU B 1190 ? 0.3083 0.4216 0.4048 -0.0210 0.0295  0.0002  1188 LEU B O   
17377 C CB  . LEU B 1190 ? 0.2958 0.3951 0.4029 -0.0284 0.0190  0.0044  1188 LEU B CB  
17378 C CG  . LEU B 1190 ? 0.3310 0.4262 0.4455 -0.0316 0.0139  0.0049  1188 LEU B CG  
17379 C CD1 . LEU B 1190 ? 0.3006 0.3902 0.4162 -0.0366 0.0115  0.0103  1188 LEU B CD1 
17380 C CD2 . LEU B 1190 ? 0.2929 0.3787 0.4038 -0.0286 0.0093  -0.0003 1188 LEU B CD2 
17381 N N   . LEU B 1191 ? 0.3333 0.4285 0.4197 -0.0190 0.0232  -0.0027 1189 LEU B N   
17382 C CA  . LEU B 1191 ? 0.3213 0.4177 0.3999 -0.0176 0.0262  -0.0019 1189 LEU B CA  
17383 C C   . LEU B 1191 ? 0.3552 0.4506 0.4333 -0.0212 0.0266  0.0041  1189 LEU B C   
17384 O O   . LEU B 1191 ? 0.3353 0.4219 0.4119 -0.0224 0.0229  0.0058  1189 LEU B O   
17385 C CB  . LEU B 1191 ? 0.3898 0.4785 0.4607 -0.0144 0.0239  -0.0054 1189 LEU B CB  
17386 C CG  . LEU B 1191 ? 0.4338 0.5244 0.4968 -0.0120 0.0264  -0.0065 1189 LEU B CG  
17387 C CD1 . LEU B 1191 ? 0.3953 0.4797 0.4533 -0.0090 0.0239  -0.0105 1189 LEU B CD1 
17388 C CD2 . LEU B 1191 ? 0.3642 0.4541 0.4231 -0.0136 0.0274  -0.0017 1189 LEU B CD2 
17389 N N   . VAL B 1192 ? 0.3167 0.4210 0.3960 -0.0228 0.0309  0.0075  1190 VAL B N   
17390 C CA  . VAL B 1192 ? 0.3331 0.4375 0.4126 -0.0269 0.0316  0.0140  1190 VAL B CA  
17391 C C   . VAL B 1192 ? 0.3316 0.4346 0.4014 -0.0254 0.0332  0.0154  1190 VAL B C   
17392 O O   . VAL B 1192 ? 0.3440 0.4527 0.4092 -0.0227 0.0366  0.0130  1190 VAL B O   
17393 C CB  . VAL B 1192 ? 0.3375 0.4536 0.4246 -0.0300 0.0356  0.0176  1190 VAL B CB  
17394 C CG1 . VAL B 1192 ? 0.2948 0.4115 0.3813 -0.0345 0.0367  0.0249  1190 VAL B CG1 
17395 C CG2 . VAL B 1192 ? 0.3046 0.4222 0.4023 -0.0318 0.0332  0.0166  1190 VAL B CG2 
17396 N N   . GLN B 1193 ? 0.2892 0.3840 0.3556 -0.0270 0.0304  0.0190  1191 GLN B N   
17397 C CA  . GLN B 1193 ? 0.3067 0.4004 0.3648 -0.0262 0.0315  0.0216  1191 GLN B CA  
17398 C C   . GLN B 1193 ? 0.3094 0.4036 0.3686 -0.0308 0.0321  0.0290  1191 GLN B C   
17399 O O   . GLN B 1193 ? 0.3101 0.3985 0.3742 -0.0340 0.0289  0.0319  1191 GLN B O   
17400 C CB  . GLN B 1193 ? 0.2742 0.3577 0.3266 -0.0235 0.0274  0.0198  1191 GLN B CB  
17401 C CG  . GLN B 1193 ? 0.2715 0.3536 0.3224 -0.0194 0.0264  0.0132  1191 GLN B CG  
17402 C CD  . GLN B 1193 ? 0.3426 0.4169 0.3875 -0.0167 0.0233  0.0123  1191 GLN B CD  
17403 O OE1 . GLN B 1193 ? 0.3465 0.4218 0.3854 -0.0157 0.0242  0.0140  1191 GLN B OE1 
17404 N NE2 . GLN B 1193 ? 0.2823 0.3491 0.3289 -0.0154 0.0197  0.0098  1191 GLN B NE2 
17405 N N   . ALA B 1194 ? 0.2824 0.3830 0.3367 -0.0313 0.0359  0.0322  1192 ALA B N   
17406 C CA  . ALA B 1194 ? 0.3259 0.4283 0.3811 -0.0360 0.0372  0.0399  1192 ALA B CA  
17407 C C   . ALA B 1194 ? 0.3351 0.4351 0.3805 -0.0353 0.0374  0.0432  1192 ALA B C   
17408 O O   . ALA B 1194 ? 0.3329 0.4348 0.3712 -0.0315 0.0387  0.0397  1192 ALA B O   
17409 C CB  . ALA B 1194 ? 0.3157 0.4312 0.3760 -0.0386 0.0426  0.0420  1192 ALA B CB  
17410 N N   . ALA B 1195 ? 0.3299 0.4254 0.3750 -0.0391 0.0358  0.0501  1193 ALA B N   
17411 C CA  . ALA B 1195 ? 0.3751 0.4686 0.4115 -0.0391 0.0359  0.0547  1193 ALA B CA  
17412 C C   . ALA B 1195 ? 0.4073 0.5010 0.4458 -0.0451 0.0364  0.0634  1193 ALA B C   
17413 O O   . ALA B 1195 ? 0.3573 0.4490 0.4040 -0.0490 0.0349  0.0657  1193 ALA B O   
17414 C CB  . ALA B 1195 ? 0.3914 0.4730 0.4230 -0.0358 0.0306  0.0532  1193 ALA B CB  
17415 N N   . SER B 1196 ? 0.4255 0.5217 0.4565 -0.0460 0.0384  0.0685  1194 SER B N   
17416 C CA  . SER B 1196 ? 0.4157 0.5102 0.4470 -0.0516 0.0381  0.0776  1194 SER B CA  
17417 C C   . SER B 1196 ? 0.4272 0.5067 0.4558 -0.0513 0.0316  0.0804  1194 SER B C   
17418 O O   . SER B 1196 ? 0.4556 0.5282 0.4800 -0.0463 0.0283  0.0758  1194 SER B O   
17419 C CB  . SER B 1196 ? 0.4437 0.5472 0.4672 -0.0526 0.0430  0.0823  1194 SER B CB  
17420 O OG  . SER B 1196 ? 0.4730 0.5716 0.4863 -0.0485 0.0410  0.0810  1194 SER B OG  
17421 N N   . SER B 1197 ? 0.4246 0.4991 0.4556 -0.0568 0.0297  0.0882  1195 SER B N   
17422 C CA  . SER B 1197 ? 0.4640 0.5236 0.4918 -0.0566 0.0234  0.0915  1195 SER B CA  
17423 C C   . SER B 1197 ? 0.4508 0.5084 0.4679 -0.0524 0.0229  0.0921  1195 SER B C   
17424 O O   . SER B 1197 ? 0.4445 0.4913 0.4587 -0.0487 0.0179  0.0905  1195 SER B O   
17425 C CB  . SER B 1197 ? 0.4349 0.4901 0.4657 -0.0637 0.0219  0.1007  1195 SER B CB  
17426 O OG  . SER B 1197 ? 0.4015 0.4595 0.4427 -0.0681 0.0222  0.1006  1195 SER B OG  
17427 N N   . GLY B 1198 ? 0.4698 0.5383 0.4811 -0.0529 0.0279  0.0944  1196 GLY B N   
17428 C CA  . GLY B 1198 ? 0.4961 0.5634 0.4970 -0.0493 0.0271  0.0952  1196 GLY B CA  
17429 C C   . GLY B 1198 ? 0.5014 0.5690 0.4999 -0.0427 0.0261  0.0865  1196 GLY B C   
17430 O O   . GLY B 1198 ? 0.5388 0.6006 0.5316 -0.0390 0.0226  0.0863  1196 GLY B O   
17431 N N   . GLU B 1199 ? 0.4823 0.5569 0.4854 -0.0411 0.0290  0.0795  1197 GLU B N   
17432 C CA  . GLU B 1199 ? 0.5057 0.5799 0.5071 -0.0353 0.0278  0.0715  1197 GLU B CA  
17433 C C   . GLU B 1199 ? 0.4953 0.5578 0.5005 -0.0327 0.0222  0.0689  1197 GLU B C   
17434 O O   . GLU B 1199 ? 0.4725 0.5313 0.4740 -0.0282 0.0194  0.0659  1197 GLU B O   
17435 C CB  . GLU B 1199 ? 0.5200 0.6037 0.5250 -0.0343 0.0321  0.0650  1197 GLU B CB  
17436 C CG  . GLU B 1199 ? 0.5932 0.6760 0.5966 -0.0290 0.0306  0.0571  1197 GLU B CG  
17437 C CD  . GLU B 1199 ? 0.6752 0.7677 0.6793 -0.0275 0.0348  0.0511  1197 GLU B CD  
17438 O OE1 . GLU B 1199 ? 0.6493 0.7483 0.6582 -0.0302 0.0386  0.0517  1197 GLU B OE1 
17439 O OE2 . GLU B 1199 ? 0.7107 0.8040 0.7106 -0.0237 0.0342  0.0458  1197 GLU B OE2 
17440 N N   . ILE B 1200 ? 0.4327 0.4895 0.4452 -0.0355 0.0204  0.0699  1198 ILE B N   
17441 C CA  . ILE B 1200 ? 0.4410 0.4858 0.4563 -0.0331 0.0149  0.0676  1198 ILE B CA  
17442 C C   . ILE B 1200 ? 0.4830 0.5190 0.4924 -0.0309 0.0108  0.0716  1198 ILE B C   
17443 O O   . ILE B 1200 ? 0.4204 0.4499 0.4288 -0.0259 0.0073  0.0679  1198 ILE B O   
17444 C CB  . ILE B 1200 ? 0.4360 0.4753 0.4591 -0.0374 0.0132  0.0694  1198 ILE B CB  
17445 C CG1 . ILE B 1200 ? 0.3970 0.4445 0.4268 -0.0385 0.0164  0.0644  1198 ILE B CG1 
17446 C CG2 . ILE B 1200 ? 0.4334 0.4585 0.4576 -0.0350 0.0072  0.0679  1198 ILE B CG2 
17447 C CD1 . ILE B 1200 ? 0.3510 0.3947 0.3889 -0.0433 0.0147  0.0665  1198 ILE B CD1 
17448 N N   . ALA B 1201 ? 0.4516 0.4876 0.4570 -0.0343 0.0112  0.0793  1199 ALA B N   
17449 C CA  . ALA B 1201 ? 0.4980 0.5256 0.4977 -0.0323 0.0070  0.0838  1199 ALA B CA  
17450 C C   . ALA B 1201 ? 0.5329 0.5657 0.5257 -0.0275 0.0075  0.0814  1199 ALA B C   
17451 O O   . ALA B 1201 ? 0.4985 0.5247 0.4890 -0.0231 0.0033  0.0810  1199 ALA B O   
17452 C CB  . ALA B 1201 ? 0.4776 0.5032 0.4749 -0.0379 0.0071  0.0934  1199 ALA B CB  
17453 N N   . ARG B 1202 ? 0.5403 0.5851 0.5301 -0.0282 0.0123  0.0798  1200 ARG B N   
17454 C CA  . ARG B 1202 ? 0.5197 0.5698 0.5022 -0.0246 0.0125  0.0783  1200 ARG B CA  
17455 C C   . ARG B 1202 ? 0.5275 0.5807 0.5117 -0.0199 0.0125  0.0697  1200 ARG B C   
17456 O O   . ARG B 1202 ? 0.5002 0.5540 0.4801 -0.0161 0.0103  0.0684  1200 ARG B O   
17457 C CB  . ARG B 1202 ? 0.5418 0.6024 0.5186 -0.0277 0.0175  0.0810  1200 ARG B CB  
17458 N N   . ASN B 1203 ? 0.4883 0.5439 0.4787 -0.0202 0.0145  0.0643  1201 ASN B N   
17459 C CA  . ASN B 1203 ? 0.5199 0.5797 0.5113 -0.0165 0.0151  0.0565  1201 ASN B CA  
17460 C C   . ASN B 1203 ? 0.5152 0.5681 0.5132 -0.0141 0.0124  0.0522  1201 ASN B C   
17461 O O   . ASN B 1203 ? 0.5039 0.5551 0.5076 -0.0164 0.0133  0.0511  1201 ASN B O   
17462 C CB  . ASN B 1203 ? 0.5170 0.5866 0.5088 -0.0183 0.0203  0.0531  1201 ASN B CB  
17463 C CG  . ASN B 1203 ? 0.5681 0.6414 0.5609 -0.0150 0.0207  0.0453  1201 ASN B CG  
17464 O OD1 . ASN B 1203 ? 0.5467 0.6168 0.5392 -0.0114 0.0175  0.0427  1201 ASN B OD1 
17465 N ND2 . ASN B 1203 ? 0.5595 0.6397 0.5536 -0.0160 0.0247  0.0417  1201 ASN B ND2 
17466 N N   . PRO B 1204 ? 0.5392 0.5884 0.5365 -0.0095 0.0091  0.0498  1202 PRO B N   
17467 C CA  . PRO B 1204 ? 0.4652 0.5080 0.4678 -0.0069 0.0069  0.0454  1202 PRO B CA  
17468 C C   . PRO B 1204 ? 0.4960 0.5439 0.5024 -0.0068 0.0094  0.0389  1202 PRO B C   
17469 O O   . PRO B 1204 ? 0.4990 0.5419 0.5099 -0.0058 0.0081  0.0357  1202 PRO B O   
17470 C CB  . PRO B 1204 ? 0.5267 0.5672 0.5272 -0.0017 0.0036  0.0446  1202 PRO B CB  
17471 C CG  . PRO B 1204 ? 0.5017 0.5502 0.4967 -0.0017 0.0047  0.0460  1202 PRO B CG  
17472 C CD  . PRO B 1204 ? 0.5364 0.5877 0.5282 -0.0065 0.0073  0.0508  1202 PRO B CD  
17473 N N   . ASP B 1205 ? 0.4516 0.5086 0.4559 -0.0079 0.0128  0.0369  1203 ASP B N   
17474 C CA  . ASP B 1205 ? 0.4952 0.5567 0.5029 -0.0080 0.0152  0.0312  1203 ASP B CA  
17475 C C   . ASP B 1205 ? 0.4480 0.5136 0.4582 -0.0121 0.0187  0.0323  1203 ASP B C   
17476 O O   . ASP B 1205 ? 0.4307 0.5024 0.4422 -0.0122 0.0214  0.0282  1203 ASP B O   
17477 C CB  . ASP B 1205 ? 0.5084 0.5765 0.5123 -0.0058 0.0162  0.0272  1203 ASP B CB  
17478 C CG  . ASP B 1205 ? 0.5566 0.6221 0.5609 -0.0018 0.0131  0.0245  1203 ASP B CG  
17479 O OD1 . ASP B 1205 ? 0.5314 0.5900 0.5384 -0.0001 0.0106  0.0252  1203 ASP B OD1 
17480 O OD2 . ASP B 1205 ? 0.6101 0.6805 0.6118 -0.0003 0.0132  0.0217  1203 ASP B OD2 
17481 N N   . ALA B 1206 ? 0.4284 0.4911 0.4397 -0.0154 0.0186  0.0380  1204 ALA B N   
17482 C CA  . ALA B 1206 ? 0.4310 0.4985 0.4462 -0.0196 0.0219  0.0397  1204 ALA B CA  
17483 C C   . ALA B 1206 ? 0.4211 0.4895 0.4430 -0.0194 0.0225  0.0344  1204 ALA B C   
17484 O O   . ALA B 1206 ? 0.4034 0.4796 0.4275 -0.0207 0.0261  0.0327  1204 ALA B O   
17485 C CB  . ALA B 1206 ? 0.4372 0.4991 0.4542 -0.0234 0.0205  0.0466  1204 ALA B CB  
17486 N N   . TYR B 1207 ? 0.3805 0.4411 0.4054 -0.0175 0.0189  0.0317  1205 TYR B N   
17487 C CA  . TYR B 1207 ? 0.3871 0.4478 0.4174 -0.0169 0.0188  0.0264  1205 TYR B CA  
17488 C C   . TYR B 1207 ? 0.3362 0.3957 0.3641 -0.0124 0.0175  0.0209  1205 TYR B C   
17489 O O   . TYR B 1207 ? 0.4153 0.4694 0.4404 -0.0097 0.0148  0.0212  1205 TYR B O   
17490 C CB  . TYR B 1207 ? 0.3404 0.3930 0.3761 -0.0189 0.0157  0.0275  1205 TYR B CB  
17491 C CG  . TYR B 1207 ? 0.3265 0.3803 0.3659 -0.0242 0.0166  0.0332  1205 TYR B CG  
17492 C CD1 . TYR B 1207 ? 0.3357 0.3990 0.3794 -0.0270 0.0205  0.0334  1205 TYR B CD1 
17493 C CD2 . TYR B 1207 ? 0.3309 0.3764 0.3698 -0.0263 0.0136  0.0386  1205 TYR B CD2 
17494 C CE1 . TYR B 1207 ? 0.3198 0.3856 0.3677 -0.0322 0.0216  0.0391  1205 TYR B CE1 
17495 C CE2 . TYR B 1207 ? 0.3318 0.3785 0.3744 -0.0319 0.0143  0.0444  1205 TYR B CE2 
17496 C CZ  . TYR B 1207 ? 0.3170 0.3745 0.3644 -0.0349 0.0185  0.0448  1205 TYR B CZ  
17497 O OH  . TYR B 1207 ? 0.3272 0.3871 0.3789 -0.0406 0.0195  0.0510  1205 TYR B OH  
17498 N N   . CYS B 1208 ? 0.2926 0.3574 0.3221 -0.0115 0.0194  0.0160  1206 CYS B N   
17499 C CA  . CYS B 1208 ? 0.3050 0.3699 0.3321 -0.0079 0.0185  0.0112  1206 CYS B CA  
17500 C C   . CYS B 1208 ? 0.3215 0.3805 0.3522 -0.0065 0.0160  0.0077  1206 CYS B C   
17501 O O   . CYS B 1208 ? 0.3041 0.3633 0.3395 -0.0080 0.0163  0.0060  1206 CYS B O   
17502 C CB  . CYS B 1208 ? 0.2998 0.3725 0.3258 -0.0077 0.0216  0.0078  1206 CYS B CB  
17503 S SG  . CYS B 1208 ? 0.3644 0.4374 0.3871 -0.0042 0.0203  0.0029  1206 CYS B SG  
17504 N N   . LEU B 1209 ? 0.2985 0.3528 0.3269 -0.0033 0.0135  0.0066  1207 LEU B N   
17505 C CA  . LEU B 1209 ? 0.2856 0.3341 0.3163 -0.0016 0.0113  0.0032  1207 LEU B CA  
17506 C C   . LEU B 1209 ? 0.2774 0.3297 0.3089 -0.0006 0.0123  -0.0017 1207 LEU B C   
17507 O O   . LEU B 1209 ? 0.2913 0.3396 0.3248 0.0001  0.0107  -0.0045 1207 LEU B O   
17508 C CB  . LEU B 1209 ? 0.2621 0.3049 0.2901 0.0019  0.0087  0.0035  1207 LEU B CB  
17509 C CG  . LEU B 1209 ? 0.2981 0.3353 0.3249 0.0016  0.0069  0.0083  1207 LEU B CG  
17510 C CD1 . LEU B 1209 ? 0.3162 0.3476 0.3408 0.0062  0.0043  0.0078  1207 LEU B CD1 
17511 C CD2 . LEU B 1209 ? 0.2823 0.3142 0.3124 -0.0019 0.0058  0.0106  1207 LEU B CD2 
17512 N N   . ASN B 1210 ? 0.2752 0.3345 0.3048 -0.0007 0.0145  -0.0028 1208 ASN B N   
17513 C CA  . ASN B 1210 ? 0.3112 0.3733 0.3414 0.0000  0.0152  -0.0072 1208 ASN B CA  
17514 C C   . ASN B 1210 ? 0.3277 0.3891 0.3627 -0.0016 0.0153  -0.0089 1208 ASN B C   
17515 O O   . ASN B 1210 ? 0.2962 0.3562 0.3324 -0.0006 0.0144  -0.0123 1208 ASN B O   
17516 C CB  . ASN B 1210 ? 0.3404 0.4091 0.3675 -0.0002 0.0173  -0.0080 1208 ASN B CB  
17517 C CG  . ASN B 1210 ? 0.3527 0.4228 0.3753 0.0013  0.0166  -0.0069 1208 ASN B CG  
17518 O OD1 . ASN B 1210 ? 0.3968 0.4635 0.4188 0.0027  0.0149  -0.0049 1208 ASN B OD1 
17519 N ND2 . ASN B 1210 ? 0.3907 0.4655 0.4100 0.0011  0.0177  -0.0081 1208 ASN B ND2 
17520 N N   . TRP B 1211 ? 0.2715 0.3344 0.3095 -0.0042 0.0165  -0.0061 1209 TRP B N   
17521 C CA  . TRP B 1211 ? 0.2782 0.3425 0.3218 -0.0060 0.0169  -0.0072 1209 TRP B CA  
17522 C C   . TRP B 1211 ? 0.2718 0.3293 0.3190 -0.0070 0.0138  -0.0066 1209 TRP B C   
17523 O O   . TRP B 1211 ? 0.2997 0.3580 0.3520 -0.0087 0.0134  -0.0074 1209 TRP B O   
17524 C CB  . TRP B 1211 ? 0.2916 0.3629 0.3373 -0.0085 0.0201  -0.0045 1209 TRP B CB  
17525 C CG  . TRP B 1211 ? 0.3303 0.4070 0.3707 -0.0075 0.0228  -0.0045 1209 TRP B CG  
17526 C CD1 . TRP B 1211 ? 0.3251 0.4049 0.3624 -0.0087 0.0247  -0.0006 1209 TRP B CD1 
17527 C CD2 . TRP B 1211 ? 0.2750 0.3539 0.3119 -0.0052 0.0233  -0.0085 1209 TRP B CD2 
17528 N NE1 . TRP B 1211 ? 0.3290 0.4129 0.3610 -0.0072 0.0263  -0.0023 1209 TRP B NE1 
17529 C CE2 . TRP B 1211 ? 0.3496 0.4329 0.3814 -0.0052 0.0254  -0.0071 1209 TRP B CE2 
17530 C CE3 . TRP B 1211 ? 0.3154 0.3927 0.3528 -0.0034 0.0220  -0.0129 1209 TRP B CE3 
17531 C CZ2 . TRP B 1211 ? 0.3100 0.3955 0.3371 -0.0035 0.0259  -0.0103 1209 TRP B CZ2 
17532 C CZ3 . TRP B 1211 ? 0.3224 0.4020 0.3555 -0.0019 0.0226  -0.0158 1209 TRP B CZ3 
17533 C CH2 . TRP B 1211 ? 0.3469 0.4304 0.3749 -0.0020 0.0244  -0.0146 1209 TRP B CH2 
17534 N N   . LEU B 1212 ? 0.2776 0.3280 0.3220 -0.0059 0.0114  -0.0054 1210 LEU B N   
17535 C CA  . LEU B 1212 ? 0.2368 0.2791 0.2833 -0.0066 0.0080  -0.0051 1210 LEU B CA  
17536 C C   . LEU B 1212 ? 0.2546 0.2916 0.2989 -0.0034 0.0057  -0.0093 1210 LEU B C   
17537 O O   . LEU B 1212 ? 0.2610 0.2903 0.3055 -0.0032 0.0026  -0.0098 1210 LEU B O   
17538 C CB  . LEU B 1212 ? 0.2617 0.2987 0.3064 -0.0072 0.0066  -0.0008 1210 LEU B CB  
17539 C CG  . LEU B 1212 ? 0.2521 0.2931 0.2997 -0.0113 0.0084  0.0041  1210 LEU B CG  
17540 C CD1 . LEU B 1212 ? 0.2507 0.2865 0.2954 -0.0116 0.0071  0.0087  1210 LEU B CD1 
17541 C CD2 . LEU B 1212 ? 0.2383 0.2791 0.2926 -0.0150 0.0073  0.0046  1210 LEU B CD2 
17542 N N   . VAL B 1213 ? 0.2899 0.3308 0.3318 -0.0012 0.0070  -0.0122 1211 VAL B N   
17543 C CA  . VAL B 1213 ? 0.2818 0.3190 0.3216 0.0014  0.0053  -0.0159 1211 VAL B CA  
17544 C C   . VAL B 1213 ? 0.3071 0.3484 0.3492 0.0007  0.0060  -0.0187 1211 VAL B C   
17545 O O   . VAL B 1213 ? 0.2743 0.3219 0.3188 -0.0008 0.0083  -0.0183 1211 VAL B O   
17546 C CB  . VAL B 1213 ? 0.2816 0.3195 0.3166 0.0047  0.0059  -0.0166 1211 VAL B CB  
17547 C CG1 . VAL B 1213 ? 0.2642 0.2967 0.2971 0.0064  0.0045  -0.0143 1211 VAL B CG1 
17548 C CG2 . VAL B 1213 ? 0.2784 0.3241 0.3124 0.0043  0.0086  -0.0159 1211 VAL B CG2 
17549 N N   . GLU B 1214 ? 0.2727 0.3102 0.3138 0.0021  0.0041  -0.0217 1212 GLU B N   
17550 C CA  . GLU B 1214 ? 0.3284 0.3685 0.3712 0.0018  0.0041  -0.0244 1212 GLU B CA  
17551 C C   . GLU B 1214 ? 0.2324 0.2733 0.2707 0.0042  0.0046  -0.0266 1212 GLU B C   
17552 O O   . GLU B 1214 ? 0.2684 0.3054 0.3031 0.0063  0.0035  -0.0273 1212 GLU B O   
17553 C CB  . GLU B 1214 ? 0.2693 0.3042 0.3144 0.0010  0.0009  -0.0259 1212 GLU B CB  
17554 C CG  . GLU B 1214 ? 0.4078 0.4450 0.4549 0.0009  0.0004  -0.0284 1212 GLU B CG  
17555 C CD  . GLU B 1214 ? 0.4789 0.5104 0.5273 0.0004  -0.0034 -0.0299 1212 GLU B CD  
17556 O OE1 . GLU B 1214 ? 0.5310 0.5592 0.5821 -0.0014 -0.0053 -0.0284 1212 GLU B OE1 
17557 O OE2 . GLU B 1214 ? 0.5669 0.5967 0.6131 0.0017  -0.0048 -0.0324 1212 GLU B OE2 
17558 N N   . GLU B 1215 ? 0.1986 0.2447 0.2372 0.0038  0.0062  -0.0275 1213 GLU B N   
17559 C CA  . GLU B 1215 ? 0.2183 0.2654 0.2534 0.0052  0.0064  -0.0293 1213 GLU B CA  
17560 C C   . GLU B 1215 ? 0.2214 0.2653 0.2564 0.0056  0.0044  -0.0317 1213 GLU B C   
17561 O O   . GLU B 1215 ? 0.2452 0.2890 0.2837 0.0045  0.0035  -0.0326 1213 GLU B O   
17562 C CB  . GLU B 1215 ? 0.2776 0.3302 0.3126 0.0045  0.0084  -0.0295 1213 GLU B CB  
17563 C CG  . GLU B 1215 ? 0.2820 0.3384 0.3164 0.0040  0.0104  -0.0273 1213 GLU B CG  
17564 C CD  . GLU B 1215 ? 0.2671 0.3282 0.3011 0.0034  0.0120  -0.0282 1213 GLU B CD  
17565 O OE1 . GLU B 1215 ? 0.2476 0.3108 0.2847 0.0026  0.0130  -0.0286 1213 GLU B OE1 
17566 O OE2 . GLU B 1215 ? 0.2797 0.3424 0.3103 0.0037  0.0121  -0.0287 1213 GLU B OE2 
17567 N N   . VAL B 1216 ? 0.2429 0.2847 0.2738 0.0072  0.0037  -0.0326 1214 VAL B N   
17568 C CA  . VAL B 1216 ? 0.1991 0.2380 0.2286 0.0075  0.0019  -0.0346 1214 VAL B CA  
17569 C C   . VAL B 1216 ? 0.2393 0.2804 0.2653 0.0080  0.0027  -0.0349 1214 VAL B C   
17570 O O   . VAL B 1216 ? 0.2638 0.3065 0.2871 0.0091  0.0039  -0.0339 1214 VAL B O   
17571 C CB  . VAL B 1216 ? 0.2542 0.2870 0.2815 0.0087  -0.0002 -0.0353 1214 VAL B CB  
17572 C CG1 . VAL B 1216 ? 0.2818 0.3119 0.3064 0.0092  -0.0020 -0.0371 1214 VAL B CG1 
17573 C CG2 . VAL B 1216 ? 0.2907 0.3207 0.3221 0.0075  -0.0018 -0.0349 1214 VAL B CG2 
17574 N N   . SER B 1217 ? 0.2186 0.2598 0.2450 0.0071  0.0019  -0.0361 1215 SER B N   
17575 C CA  . SER B 1217 ? 0.1989 0.2412 0.2221 0.0069  0.0020  -0.0363 1215 SER B CA  
17576 C C   . SER B 1217 ? 0.2226 0.2607 0.2430 0.0073  0.0000  -0.0372 1215 SER B C   
17577 O O   . SER B 1217 ? 0.2448 0.2797 0.2669 0.0073  -0.0020 -0.0384 1215 SER B O   
17578 C CB  . SER B 1217 ? 0.2385 0.2829 0.2633 0.0055  0.0022  -0.0370 1215 SER B CB  
17579 O OG  . SER B 1217 ? 0.3082 0.3518 0.3301 0.0049  0.0013  -0.0372 1215 SER B OG  
17580 N N   . ALA B 1218 ? 0.2410 0.2796 0.2572 0.0078  0.0004  -0.0366 1216 ALA B N   
17581 C CA  . ALA B 1218 ? 0.2647 0.2998 0.2772 0.0081  -0.0012 -0.0371 1216 ALA B CA  
17582 C C   . ALA B 1218 ? 0.2386 0.2760 0.2484 0.0069  -0.0007 -0.0359 1216 ALA B C   
17583 O O   . ALA B 1218 ? 0.2792 0.3211 0.2884 0.0068  0.0013  -0.0344 1216 ALA B O   
17584 C CB  . ALA B 1218 ? 0.2587 0.2913 0.2677 0.0104  -0.0012 -0.0374 1216 ALA B CB  
17585 N N   . SER B 1219 ? 0.2304 0.2647 0.2388 0.0058  -0.0027 -0.0363 1217 SER B N   
17586 C CA  . SER B 1219 ? 0.2334 0.2689 0.2395 0.0039  -0.0028 -0.0348 1217 SER B CA  
17587 C C   . SER B 1219 ? 0.2338 0.2661 0.2349 0.0042  -0.0041 -0.0343 1217 SER B C   
17588 O O   . SER B 1219 ? 0.2443 0.2717 0.2448 0.0045  -0.0066 -0.0355 1217 SER B O   
17589 C CB  . SER B 1219 ? 0.2508 0.2847 0.2593 0.0022  -0.0044 -0.0355 1217 SER B CB  
17590 O OG  . SER B 1219 ? 0.3019 0.3355 0.3077 0.0000  -0.0052 -0.0340 1217 SER B OG  
17591 N N   . ILE B 1220 ? 0.2689 0.3044 0.2664 0.0042  -0.0022 -0.0325 1218 ILE B N   
17592 C CA  . ILE B 1220 ? 0.2861 0.3195 0.2778 0.0048  -0.0027 -0.0318 1218 ILE B CA  
17593 C C   . ILE B 1220 ? 0.2869 0.3218 0.2764 0.0018  -0.0029 -0.0292 1218 ILE B C   
17594 O O   . ILE B 1220 ? 0.3113 0.3520 0.3021 0.0004  -0.0008 -0.0271 1218 ILE B O   
17595 C CB  . ILE B 1220 ? 0.3565 0.3929 0.3453 0.0076  -0.0001 -0.0318 1218 ILE B CB  
17596 C CG1 . ILE B 1220 ? 0.3426 0.3762 0.3334 0.0102  -0.0004 -0.0342 1218 ILE B CG1 
17597 C CG2 . ILE B 1220 ? 0.3177 0.3522 0.2994 0.0084  -0.0002 -0.0311 1218 ILE B CG2 
17598 C CD1 . ILE B 1220 ? 0.3840 0.4221 0.3796 0.0106  0.0015  -0.0340 1218 ILE B CD1 
17599 N N   . ASN B 1221 ? 0.2740 0.3037 0.2605 0.0007  -0.0056 -0.0289 1219 ASN B N   
17600 C CA  . ASN B 1221 ? 0.2884 0.3182 0.2720 -0.0024 -0.0062 -0.0259 1219 ASN B CA  
17601 C C   . ASN B 1221 ? 0.3333 0.3673 0.3116 -0.0019 -0.0036 -0.0237 1219 ASN B C   
17602 O O   . ASN B 1221 ? 0.3208 0.3515 0.2938 -0.0001 -0.0043 -0.0242 1219 ASN B O   
17603 C CB  . ASN B 1221 ? 0.2802 0.3024 0.2620 -0.0034 -0.0103 -0.0262 1219 ASN B CB  
17604 C CG  . ASN B 1221 ? 0.3432 0.3642 0.3212 -0.0068 -0.0114 -0.0227 1219 ASN B CG  
17605 O OD1 . ASN B 1221 ? 0.3139 0.3403 0.2913 -0.0089 -0.0092 -0.0199 1219 ASN B OD1 
17606 N ND2 . ASN B 1221 ? 0.3707 0.3846 0.3462 -0.0073 -0.0152 -0.0226 1219 ASN B ND2 
17607 N N   . THR B 1222 ? 0.2976 0.3390 0.2771 -0.0033 -0.0008 -0.0211 1220 THR B N   
17608 C CA  . THR B 1222 ? 0.3300 0.3770 0.3051 -0.0025 0.0023  -0.0188 1220 THR B CA  
17609 C C   . THR B 1222 ? 0.3551 0.4029 0.3267 -0.0064 0.0018  -0.0148 1220 THR B C   
17610 O O   . THR B 1222 ? 0.3801 0.4340 0.3483 -0.0063 0.0049  -0.0122 1220 THR B O   
17611 C CB  . THR B 1222 ? 0.3346 0.3909 0.3137 -0.0013 0.0060  -0.0181 1220 THR B CB  
17612 O OG1 . THR B 1222 ? 0.3345 0.3943 0.3187 -0.0051 0.0055  -0.0162 1220 THR B OG1 
17613 C CG2 . THR B 1222 ? 0.3456 0.4004 0.3271 0.0028  0.0065  -0.0218 1220 THR B CG2 
17614 N N   . ALA B 1223 ? 0.3816 0.4234 0.3537 -0.0097 -0.0018 -0.0140 1221 ALA B N   
17615 C CA  . ALA B 1223 ? 0.4050 0.4453 0.3728 -0.0135 -0.0031 -0.0101 1221 ALA B CA  
17616 C C   . ALA B 1223 ? 0.5136 0.5461 0.4748 -0.0122 -0.0056 -0.0107 1221 ALA B C   
17617 O O   . ALA B 1223 ? 0.5973 0.6284 0.5535 -0.0148 -0.0064 -0.0072 1221 ALA B O   
17618 C CB  . ALA B 1223 ? 0.3965 0.4334 0.3679 -0.0179 -0.0062 -0.0087 1221 ALA B CB  
17619 N N   . ALA B 1224 ? 0.4787 0.5066 0.4399 -0.0083 -0.0069 -0.0149 1222 ALA B N   
17620 C CA  . ALA B 1224 ? 0.5396 0.5590 0.4964 -0.0073 -0.0107 -0.0161 1222 ALA B CA  
17621 C C   . ALA B 1224 ? 0.5731 0.5923 0.5208 -0.0072 -0.0100 -0.0137 1222 ALA B C   
17622 O O   . ALA B 1224 ? 0.5442 0.5565 0.4872 -0.0078 -0.0136 -0.0130 1222 ALA B O   
17623 C CB  . ALA B 1224 ? 0.4743 0.4905 0.4335 -0.0034 -0.0118 -0.0208 1222 ALA B CB  
# 
