data_9DL5
# 
_entry.id   9DL5 
# 
_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   9DL5         pdb_00009dl5 10.2210/pdb9dl5/pdb 
WWPDB D_1000287801 ?            ?                   
# 
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                        9DL5 
_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           N 
# 
_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 'FLAVIN-ADENINE DINUCLEOTIDE'       785.550    2    ?                ? ? ? 
3 non-polymer syn 'TRIETHYLENE GLYCOL'                150.173    3    ?                ? ? ? 
4 non-polymer syn 'FORMIC ACID'                       46.025     6    ?                ? ? ? 
5 non-polymer syn 'DI(HYDROXYETHYL)ETHER'             106.120    8    ?                ? ? ? 
6 non-polymer syn 'TETRAETHYLENE GLYCOL'              194.226    2    ?                ? ? ? 
7 non-polymer syn 5-chloro-2,3-dihydro-1H-inden-1-one 166.604    1    ?                ? ? ? 
8 non-polymer syn 'SULFATE ION'                       96.063     19   ?                ? ? ? 
9 water       nat water                               18.015     1772 ?                ? ? ? 
# 
_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 'FLAVIN-ADENINE DINUCLEOTIDE'       FAD   
3 'TRIETHYLENE GLYCOL'                PGE   
4 'FORMIC ACID'                       FMT   
5 'DI(HYDROXYETHYL)ETHER'             PEG   
6 'TETRAETHYLENE GLYCOL'              PG4   
7 5-chloro-2,3-dihydro-1H-inden-1-one A1BDA 
8 'SULFATE ION'                       SO4   
9 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 
A1BDA non-polymer         . 5-chloro-2,3-dihydro-1H-inden-1-one 5-chloro-1-indanone 'C9 H7 Cl O'        166.604 
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 
PG4   non-polymer         . 'TETRAETHYLENE GLYCOL'              ?                   'C8 H18 O5'         194.226 
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 
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   14   ALA ALA 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  ?    ?   ?   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  ?    ?   ?   A . n 
A 1 482  GLU 482  480  ?    ?   ?   A . n 
A 1 483  THR 483  481  ?    ?   ?   A . n 
A 1 484  LEU 484  482  ?    ?   ?   A . n 
A 1 485  LEU 485  483  ?    ?   ?   A . n 
A 1 486  ALA 486  484  ?    ?   ?   A . n 
A 1 487  TYR 487  485  ?    ?   ?   A . n 
A 1 488  LEU 488  486  ?    ?   ?   A . n 
A 1 489  VAL 489  487  ?    ?   ?   A . n 
A 1 490  ARG 490  488  ?    ?   ?   A . n 
A 1 491  ARG 491  489  ?    ?   ?   A . n 
A 1 492  LEU 492  490  ?    ?   ?   A . n 
A 1 493  LEU 493  491  ?    ?   ?   A . n 
A 1 494  GLU 494  492  ?    ?   ?   A . n 
A 1 495  ASN 495  493  ?    ?   ?   A . n 
A 1 496  GLY 496  494  ?    ?   ?   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 1228 SER SER A . n 
A 1 1231 LEU 1231 1229 1229 LEU LEU 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   14   ALA ALA 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  492  GLU GLU B . n 
B 1 495  ASN 495  493  493  ASN ASN 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 ?    ?   ?   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 A1BDA ? ? A1BDA ? ? 'SUBJECT OF INVESTIGATION' ? 
2 FAD   ? ? FAD   ? ? '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 FAD   1   2001 2001 FAD   FAD A . 
D  3 PGE   1   2002 2002 PGE   PGE A . 
E  4 FMT   1   2003 2003 FMT   FMT A . 
F  5 PEG   1   2004 2004 PEG   PEG A . 
G  3 PGE   1   2005 2006 PGE   PGE A . 
H  6 PG4   1   2006 2007 PG4   PG4 A . 
I  5 PEG   1   2007 2008 PEG   PEG A . 
J  7 A1BDA 1   2008 2009 A1BDA 195 A . 
K  4 FMT   1   2009 2011 FMT   FMT A . 
L  5 PEG   1   2010 2012 PEG   PEG A . 
M  8 SO4   1   2011 1    SO4   SO4 A . 
N  8 SO4   1   2012 4    SO4   SO4 A . 
O  8 SO4   1   2013 5    SO4   SO4 A . 
P  8 SO4   1   2014 6    SO4   SO4 A . 
Q  8 SO4   1   2015 7    SO4   SO4 A . 
R  8 SO4   1   2016 10   SO4   SO4 A . 
S  8 SO4   1   2017 11   SO4   SO4 A . 
T  8 SO4   1   2018 17   SO4   SO4 A . 
U  8 SO4   1   2019 19   SO4   SO4 A . 
V  2 FAD   1   2001 2001 FAD   FAD B . 
W  5 PEG   1   2002 2002 PEG   PEG B . 
X  3 PGE   1   2003 2003 PGE   PGE B . 
Y  5 PEG   1   2004 2004 PEG   PEG B . 
Z  5 PEG   1   2005 2006 PEG   PEG B . 
AA 6 PG4   1   2006 2007 PG4   PG4 B . 
BA 4 FMT   1   2007 2009 FMT   FMT B . 
CA 5 PEG   1   2008 2010 PEG   PEG B . 
DA 4 FMT   1   2009 2011 FMT   FMT B . 
EA 4 FMT   1   2010 2013 FMT   FMT B . 
FA 5 PEG   1   2011 2015 PEG   PEG B . 
GA 4 FMT   1   2012 2018 FMT   FMT B . 
HA 8 SO4   1   2013 2    SO4   SO4 B . 
IA 8 SO4   1   2014 3    SO4   SO4 B . 
JA 8 SO4   1   2015 8    SO4   SO4 B . 
KA 8 SO4   1   2016 9    SO4   SO4 B . 
LA 8 SO4   1   2017 12   SO4   SO4 B . 
MA 8 SO4   1   2018 13   SO4   SO4 B . 
NA 8 SO4   1   2019 14   SO4   SO4 B . 
OA 8 SO4   1   2020 18   SO4   SO4 B . 
PA 8 SO4   1   2021 20   SO4   SO4 B . 
QA 8 SO4   1   2022 21   SO4   SO4 B . 
RA 9 HOH   1   2101 1397 HOH   HOH A . 
RA 9 HOH   2   2102 1373 HOH   HOH A . 
RA 9 HOH   3   2103 1779 HOH   HOH A . 
RA 9 HOH   4   2104 103  HOH   HOH A . 
RA 9 HOH   5   2105 449  HOH   HOH A . 
RA 9 HOH   6   2106 893  HOH   HOH A . 
RA 9 HOH   7   2107 1828 HOH   HOH A . 
RA 9 HOH   8   2108 1892 HOH   HOH A . 
RA 9 HOH   9   2109 1405 HOH   HOH A . 
RA 9 HOH   10  2110 803  HOH   HOH A . 
RA 9 HOH   11  2111 1377 HOH   HOH A . 
RA 9 HOH   12  2112 1513 HOH   HOH A . 
RA 9 HOH   13  2113 1893 HOH   HOH A . 
RA 9 HOH   14  2114 647  HOH   HOH A . 
RA 9 HOH   15  2115 925  HOH   HOH A . 
RA 9 HOH   16  2116 1344 HOH   HOH A . 
RA 9 HOH   17  2117 1746 HOH   HOH A . 
RA 9 HOH   18  2118 1884 HOH   HOH A . 
RA 9 HOH   19  2119 1750 HOH   HOH A . 
RA 9 HOH   20  2120 749  HOH   HOH A . 
RA 9 HOH   21  2121 811  HOH   HOH A . 
RA 9 HOH   22  2122 1748 HOH   HOH A . 
RA 9 HOH   23  2123 947  HOH   HOH A . 
RA 9 HOH   24  2124 505  HOH   HOH A . 
RA 9 HOH   25  2125 903  HOH   HOH A . 
RA 9 HOH   26  2126 959  HOH   HOH A . 
RA 9 HOH   27  2127 279  HOH   HOH A . 
RA 9 HOH   28  2128 1854 HOH   HOH A . 
RA 9 HOH   29  2129 1699 HOH   HOH A . 
RA 9 HOH   30  2130 206  HOH   HOH A . 
RA 9 HOH   31  2131 140  HOH   HOH A . 
RA 9 HOH   32  2132 172  HOH   HOH A . 
RA 9 HOH   33  2133 981  HOH   HOH A . 
RA 9 HOH   34  2134 1491 HOH   HOH A . 
RA 9 HOH   35  2135 195  HOH   HOH A . 
RA 9 HOH   36  2136 1944 HOH   HOH A . 
RA 9 HOH   37  2137 1772 HOH   HOH A . 
RA 9 HOH   38  2138 1388 HOH   HOH A . 
RA 9 HOH   39  2139 874  HOH   HOH A . 
RA 9 HOH   40  2140 1112 HOH   HOH A . 
RA 9 HOH   41  2141 1196 HOH   HOH A . 
RA 9 HOH   42  2142 363  HOH   HOH A . 
RA 9 HOH   43  2143 945  HOH   HOH A . 
RA 9 HOH   44  2144 225  HOH   HOH A . 
RA 9 HOH   45  2145 539  HOH   HOH A . 
RA 9 HOH   46  2146 844  HOH   HOH A . 
RA 9 HOH   47  2147 1940 HOH   HOH A . 
RA 9 HOH   48  2148 371  HOH   HOH A . 
RA 9 HOH   49  2149 969  HOH   HOH A . 
RA 9 HOH   50  2150 826  HOH   HOH A . 
RA 9 HOH   51  2151 364  HOH   HOH A . 
RA 9 HOH   52  2152 405  HOH   HOH A . 
RA 9 HOH   53  2153 728  HOH   HOH A . 
RA 9 HOH   54  2154 1666 HOH   HOH A . 
RA 9 HOH   55  2155 64   HOH   HOH A . 
RA 9 HOH   56  2156 988  HOH   HOH A . 
RA 9 HOH   57  2157 1042 HOH   HOH A . 
RA 9 HOH   58  2158 906  HOH   HOH A . 
RA 9 HOH   59  2159 829  HOH   HOH A . 
RA 9 HOH   60  2160 560  HOH   HOH A . 
RA 9 HOH   61  2161 366  HOH   HOH A . 
RA 9 HOH   62  2162 503  HOH   HOH A . 
RA 9 HOH   63  2163 1826 HOH   HOH A . 
RA 9 HOH   64  2164 685  HOH   HOH A . 
RA 9 HOH   65  2165 472  HOH   HOH A . 
RA 9 HOH   66  2166 155  HOH   HOH A . 
RA 9 HOH   67  2167 670  HOH   HOH A . 
RA 9 HOH   68  2168 222  HOH   HOH A . 
RA 9 HOH   69  2169 993  HOH   HOH A . 
RA 9 HOH   70  2170 521  HOH   HOH A . 
RA 9 HOH   71  2171 191  HOH   HOH A . 
RA 9 HOH   72  2172 171  HOH   HOH A . 
RA 9 HOH   73  2173 1445 HOH   HOH A . 
RA 9 HOH   74  2174 281  HOH   HOH A . 
RA 9 HOH   75  2175 378  HOH   HOH A . 
RA 9 HOH   76  2176 1918 HOH   HOH A . 
RA 9 HOH   77  2177 344  HOH   HOH A . 
RA 9 HOH   78  2178 846  HOH   HOH A . 
RA 9 HOH   79  2179 1866 HOH   HOH A . 
RA 9 HOH   80  2180 87   HOH   HOH A . 
RA 9 HOH   81  2181 882  HOH   HOH A . 
RA 9 HOH   82  2182 273  HOH   HOH A . 
RA 9 HOH   83  2183 721  HOH   HOH A . 
RA 9 HOH   84  2184 1467 HOH   HOH A . 
RA 9 HOH   85  2185 895  HOH   HOH A . 
RA 9 HOH   86  2186 1296 HOH   HOH A . 
RA 9 HOH   87  2187 525  HOH   HOH A . 
RA 9 HOH   88  2188 1501 HOH   HOH A . 
RA 9 HOH   89  2189 209  HOH   HOH A . 
RA 9 HOH   90  2190 639  HOH   HOH A . 
RA 9 HOH   91  2191 624  HOH   HOH A . 
RA 9 HOH   92  2192 1671 HOH   HOH A . 
RA 9 HOH   93  2193 1376 HOH   HOH A . 
RA 9 HOH   94  2194 537  HOH   HOH A . 
RA 9 HOH   95  2195 571  HOH   HOH A . 
RA 9 HOH   96  2196 970  HOH   HOH A . 
RA 9 HOH   97  2197 522  HOH   HOH A . 
RA 9 HOH   98  2198 407  HOH   HOH A . 
RA 9 HOH   99  2199 95   HOH   HOH A . 
RA 9 HOH   100 2200 1582 HOH   HOH A . 
RA 9 HOH   101 2201 570  HOH   HOH A . 
RA 9 HOH   102 2202 376  HOH   HOH A . 
RA 9 HOH   103 2203 1482 HOH   HOH A . 
RA 9 HOH   104 2204 425  HOH   HOH A . 
RA 9 HOH   105 2205 102  HOH   HOH A . 
RA 9 HOH   106 2206 331  HOH   HOH A . 
RA 9 HOH   107 2207 355  HOH   HOH A . 
RA 9 HOH   108 2208 28   HOH   HOH A . 
RA 9 HOH   109 2209 1303 HOH   HOH A . 
RA 9 HOH   110 2210 413  HOH   HOH A . 
RA 9 HOH   111 2211 860  HOH   HOH A . 
RA 9 HOH   112 2212 113  HOH   HOH A . 
RA 9 HOH   113 2213 143  HOH   HOH A . 
RA 9 HOH   114 2214 504  HOH   HOH A . 
RA 9 HOH   115 2215 1021 HOH   HOH A . 
RA 9 HOH   116 2216 15   HOH   HOH A . 
RA 9 HOH   117 2217 851  HOH   HOH A . 
RA 9 HOH   118 2218 317  HOH   HOH A . 
RA 9 HOH   119 2219 1141 HOH   HOH A . 
RA 9 HOH   120 2220 974  HOH   HOH A . 
RA 9 HOH   121 2221 557  HOH   HOH A . 
RA 9 HOH   122 2222 381  HOH   HOH A . 
RA 9 HOH   123 2223 305  HOH   HOH A . 
RA 9 HOH   124 2224 372  HOH   HOH A . 
RA 9 HOH   125 2225 1742 HOH   HOH A . 
RA 9 HOH   126 2226 316  HOH   HOH A . 
RA 9 HOH   127 2227 328  HOH   HOH A . 
RA 9 HOH   128 2228 1560 HOH   HOH A . 
RA 9 HOH   129 2229 312  HOH   HOH A . 
RA 9 HOH   130 2230 722  HOH   HOH A . 
RA 9 HOH   131 2231 719  HOH   HOH A . 
RA 9 HOH   132 2232 181  HOH   HOH A . 
RA 9 HOH   133 2233 1238 HOH   HOH A . 
RA 9 HOH   134 2234 684  HOH   HOH A . 
RA 9 HOH   135 2235 108  HOH   HOH A . 
RA 9 HOH   136 2236 822  HOH   HOH A . 
RA 9 HOH   137 2237 847  HOH   HOH A . 
RA 9 HOH   138 2238 83   HOH   HOH A . 
RA 9 HOH   139 2239 1818 HOH   HOH A . 
RA 9 HOH   140 2240 510  HOH   HOH A . 
RA 9 HOH   141 2241 11   HOH   HOH A . 
RA 9 HOH   142 2242 910  HOH   HOH A . 
RA 9 HOH   143 2243 1692 HOH   HOH A . 
RA 9 HOH   144 2244 1252 HOH   HOH A . 
RA 9 HOH   145 2245 805  HOH   HOH A . 
RA 9 HOH   146 2246 1916 HOH   HOH A . 
RA 9 HOH   147 2247 506  HOH   HOH A . 
RA 9 HOH   148 2248 645  HOH   HOH A . 
RA 9 HOH   149 2249 214  HOH   HOH A . 
RA 9 HOH   150 2250 1327 HOH   HOH A . 
RA 9 HOH   151 2251 1255 HOH   HOH A . 
RA 9 HOH   152 2252 1662 HOH   HOH A . 
RA 9 HOH   153 2253 575  HOH   HOH A . 
RA 9 HOH   154 2254 526  HOH   HOH A . 
RA 9 HOH   155 2255 137  HOH   HOH A . 
RA 9 HOH   156 2256 80   HOH   HOH A . 
RA 9 HOH   157 2257 1068 HOH   HOH A . 
RA 9 HOH   158 2258 474  HOH   HOH A . 
RA 9 HOH   159 2259 679  HOH   HOH A . 
RA 9 HOH   160 2260 496  HOH   HOH A . 
RA 9 HOH   161 2261 88   HOH   HOH A . 
RA 9 HOH   162 2262 1678 HOH   HOH A . 
RA 9 HOH   163 2263 523  HOH   HOH A . 
RA 9 HOH   164 2264 1256 HOH   HOH A . 
RA 9 HOH   165 2265 194  HOH   HOH A . 
RA 9 HOH   166 2266 12   HOH   HOH A . 
RA 9 HOH   167 2267 758  HOH   HOH A . 
RA 9 HOH   168 2268 631  HOH   HOH A . 
RA 9 HOH   169 2269 293  HOH   HOH A . 
RA 9 HOH   170 2270 971  HOH   HOH A . 
RA 9 HOH   171 2271 842  HOH   HOH A . 
RA 9 HOH   172 2272 46   HOH   HOH A . 
RA 9 HOH   173 2273 1808 HOH   HOH A . 
RA 9 HOH   174 2274 125  HOH   HOH A . 
RA 9 HOH   175 2275 1360 HOH   HOH A . 
RA 9 HOH   176 2276 387  HOH   HOH A . 
RA 9 HOH   177 2277 598  HOH   HOH A . 
RA 9 HOH   178 2278 158  HOH   HOH A . 
RA 9 HOH   179 2279 322  HOH   HOH A . 
RA 9 HOH   180 2280 985  HOH   HOH A . 
RA 9 HOH   181 2281 419  HOH   HOH A . 
RA 9 HOH   182 2282 761  HOH   HOH A . 
RA 9 HOH   183 2283 1167 HOH   HOH A . 
RA 9 HOH   184 2284 547  HOH   HOH A . 
RA 9 HOH   185 2285 310  HOH   HOH A . 
RA 9 HOH   186 2286 1609 HOH   HOH A . 
RA 9 HOH   187 2287 394  HOH   HOH A . 
RA 9 HOH   188 2288 176  HOH   HOH A . 
RA 9 HOH   189 2289 31   HOH   HOH A . 
RA 9 HOH   190 2290 59   HOH   HOH A . 
RA 9 HOH   191 2291 377  HOH   HOH A . 
RA 9 HOH   192 2292 276  HOH   HOH A . 
RA 9 HOH   193 2293 1839 HOH   HOH A . 
RA 9 HOH   194 2294 587  HOH   HOH A . 
RA 9 HOH   195 2295 1617 HOH   HOH A . 
RA 9 HOH   196 2296 254  HOH   HOH A . 
RA 9 HOH   197 2297 130  HOH   HOH A . 
RA 9 HOH   198 2298 889  HOH   HOH A . 
RA 9 HOH   199 2299 85   HOH   HOH A . 
RA 9 HOH   200 2300 1099 HOH   HOH A . 
RA 9 HOH   201 2301 1271 HOH   HOH A . 
RA 9 HOH   202 2302 257  HOH   HOH A . 
RA 9 HOH   203 2303 686  HOH   HOH A . 
RA 9 HOH   204 2304 581  HOH   HOH A . 
RA 9 HOH   205 2305 933  HOH   HOH A . 
RA 9 HOH   206 2306 964  HOH   HOH A . 
RA 9 HOH   207 2307 77   HOH   HOH A . 
RA 9 HOH   208 2308 1299 HOH   HOH A . 
RA 9 HOH   209 2309 529  HOH   HOH A . 
RA 9 HOH   210 2310 368  HOH   HOH A . 
RA 9 HOH   211 2311 914  HOH   HOH A . 
RA 9 HOH   212 2312 399  HOH   HOH A . 
RA 9 HOH   213 2313 351  HOH   HOH A . 
RA 9 HOH   214 2314 887  HOH   HOH A . 
RA 9 HOH   215 2315 197  HOH   HOH A . 
RA 9 HOH   216 2316 1216 HOH   HOH A . 
RA 9 HOH   217 2317 323  HOH   HOH A . 
RA 9 HOH   218 2318 245  HOH   HOH A . 
RA 9 HOH   219 2319 656  HOH   HOH A . 
RA 9 HOH   220 2320 247  HOH   HOH A . 
RA 9 HOH   221 2321 690  HOH   HOH A . 
RA 9 HOH   222 2322 421  HOH   HOH A . 
RA 9 HOH   223 2323 816  HOH   HOH A . 
RA 9 HOH   224 2324 414  HOH   HOH A . 
RA 9 HOH   225 2325 615  HOH   HOH A . 
RA 9 HOH   226 2326 1209 HOH   HOH A . 
RA 9 HOH   227 2327 491  HOH   HOH A . 
RA 9 HOH   228 2328 1551 HOH   HOH A . 
RA 9 HOH   229 2329 269  HOH   HOH A . 
RA 9 HOH   230 2330 1161 HOH   HOH A . 
RA 9 HOH   231 2331 94   HOH   HOH A . 
RA 9 HOH   232 2332 234  HOH   HOH A . 
RA 9 HOH   233 2333 284  HOH   HOH A . 
RA 9 HOH   234 2334 267  HOH   HOH A . 
RA 9 HOH   235 2335 1463 HOH   HOH A . 
RA 9 HOH   236 2336 650  HOH   HOH A . 
RA 9 HOH   237 2337 1118 HOH   HOH A . 
RA 9 HOH   238 2338 365  HOH   HOH A . 
RA 9 HOH   239 2339 335  HOH   HOH A . 
RA 9 HOH   240 2340 601  HOH   HOH A . 
RA 9 HOH   241 2341 563  HOH   HOH A . 
RA 9 HOH   242 2342 687  HOH   HOH A . 
RA 9 HOH   243 2343 1084 HOH   HOH A . 
RA 9 HOH   244 2344 1451 HOH   HOH A . 
RA 9 HOH   245 2345 1321 HOH   HOH A . 
RA 9 HOH   246 2346 332  HOH   HOH A . 
RA 9 HOH   247 2347 395  HOH   HOH A . 
RA 9 HOH   248 2348 50   HOH   HOH A . 
RA 9 HOH   249 2349 236  HOH   HOH A . 
RA 9 HOH   250 2350 84   HOH   HOH A . 
RA 9 HOH   251 2351 1649 HOH   HOH A . 
RA 9 HOH   252 2352 628  HOH   HOH A . 
RA 9 HOH   253 2353 579  HOH   HOH A . 
RA 9 HOH   254 2354 1061 HOH   HOH A . 
RA 9 HOH   255 2355 205  HOH   HOH A . 
RA 9 HOH   256 2356 753  HOH   HOH A . 
RA 9 HOH   257 2357 58   HOH   HOH A . 
RA 9 HOH   258 2358 66   HOH   HOH A . 
RA 9 HOH   259 2359 184  HOH   HOH A . 
RA 9 HOH   260 2360 1246 HOH   HOH A . 
RA 9 HOH   261 2361 1301 HOH   HOH A . 
RA 9 HOH   262 2362 991  HOH   HOH A . 
RA 9 HOH   263 2363 705  HOH   HOH A . 
RA 9 HOH   264 2364 1380 HOH   HOH A . 
RA 9 HOH   265 2365 76   HOH   HOH A . 
RA 9 HOH   266 2366 1532 HOH   HOH A . 
RA 9 HOH   267 2367 1607 HOH   HOH A . 
RA 9 HOH   268 2368 336  HOH   HOH A . 
RA 9 HOH   269 2369 203  HOH   HOH A . 
RA 9 HOH   270 2370 1151 HOH   HOH A . 
RA 9 HOH   271 2371 277  HOH   HOH A . 
RA 9 HOH   272 2372 987  HOH   HOH A . 
RA 9 HOH   273 2373 109  HOH   HOH A . 
RA 9 HOH   274 2374 139  HOH   HOH A . 
RA 9 HOH   275 2375 446  HOH   HOH A . 
RA 9 HOH   276 2376 201  HOH   HOH A . 
RA 9 HOH   277 2377 703  HOH   HOH A . 
RA 9 HOH   278 2378 996  HOH   HOH A . 
RA 9 HOH   279 2379 1093 HOH   HOH A . 
RA 9 HOH   280 2380 1740 HOH   HOH A . 
RA 9 HOH   281 2381 111  HOH   HOH A . 
RA 9 HOH   282 2382 1307 HOH   HOH A . 
RA 9 HOH   283 2383 1164 HOH   HOH A . 
RA 9 HOH   284 2384 1391 HOH   HOH A . 
RA 9 HOH   285 2385 966  HOH   HOH A . 
RA 9 HOH   286 2386 1374 HOH   HOH A . 
RA 9 HOH   287 2387 1180 HOH   HOH A . 
RA 9 HOH   288 2388 1943 HOH   HOH A . 
RA 9 HOH   289 2389 514  HOH   HOH A . 
RA 9 HOH   290 2390 30   HOH   HOH A . 
RA 9 HOH   291 2391 255  HOH   HOH A . 
RA 9 HOH   292 2392 666  HOH   HOH A . 
RA 9 HOH   293 2393 187  HOH   HOH A . 
RA 9 HOH   294 2394 509  HOH   HOH A . 
RA 9 HOH   295 2395 1367 HOH   HOH A . 
RA 9 HOH   296 2396 1387 HOH   HOH A . 
RA 9 HOH   297 2397 1496 HOH   HOH A . 
RA 9 HOH   298 2398 776  HOH   HOH A . 
RA 9 HOH   299 2399 833  HOH   HOH A . 
RA 9 HOH   300 2400 149  HOH   HOH A . 
RA 9 HOH   301 2401 1686 HOH   HOH A . 
RA 9 HOH   302 2402 1177 HOH   HOH A . 
RA 9 HOH   303 2403 32   HOH   HOH A . 
RA 9 HOH   304 2404 741  HOH   HOH A . 
RA 9 HOH   305 2405 55   HOH   HOH A . 
RA 9 HOH   306 2406 409  HOH   HOH A . 
RA 9 HOH   307 2407 1095 HOH   HOH A . 
RA 9 HOH   308 2408 594  HOH   HOH A . 
RA 9 HOH   309 2409 460  HOH   HOH A . 
RA 9 HOH   310 2410 452  HOH   HOH A . 
RA 9 HOH   311 2411 782  HOH   HOH A . 
RA 9 HOH   312 2412 353  HOH   HOH A . 
RA 9 HOH   313 2413 927  HOH   HOH A . 
RA 9 HOH   314 2414 1324 HOH   HOH A . 
RA 9 HOH   315 2415 170  HOH   HOH A . 
RA 9 HOH   316 2416 1137 HOH   HOH A . 
RA 9 HOH   317 2417 1250 HOH   HOH A . 
RA 9 HOH   318 2418 338  HOH   HOH A . 
RA 9 HOH   319 2419 119  HOH   HOH A . 
RA 9 HOH   320 2420 1861 HOH   HOH A . 
RA 9 HOH   321 2421 520  HOH   HOH A . 
RA 9 HOH   322 2422 62   HOH   HOH A . 
RA 9 HOH   323 2423 734  HOH   HOH A . 
RA 9 HOH   324 2424 213  HOH   HOH A . 
RA 9 HOH   325 2425 831  HOH   HOH A . 
RA 9 HOH   326 2426 813  HOH   HOH A . 
RA 9 HOH   327 2427 278  HOH   HOH A . 
RA 9 HOH   328 2428 1158 HOH   HOH A . 
RA 9 HOH   329 2429 430  HOH   HOH A . 
RA 9 HOH   330 2430 1283 HOH   HOH A . 
RA 9 HOH   331 2431 128  HOH   HOH A . 
RA 9 HOH   332 2432 152  HOH   HOH A . 
RA 9 HOH   333 2433 574  HOH   HOH A . 
RA 9 HOH   334 2434 1335 HOH   HOH A . 
RA 9 HOH   335 2435 683  HOH   HOH A . 
RA 9 HOH   336 2436 1720 HOH   HOH A . 
RA 9 HOH   337 2437 99   HOH   HOH A . 
RA 9 HOH   338 2438 990  HOH   HOH A . 
RA 9 HOH   339 2439 540  HOH   HOH A . 
RA 9 HOH   340 2440 16   HOH   HOH A . 
RA 9 HOH   341 2441 949  HOH   HOH A . 
RA 9 HOH   342 2442 383  HOH   HOH A . 
RA 9 HOH   343 2443 49   HOH   HOH A . 
RA 9 HOH   344 2444 285  HOH   HOH A . 
RA 9 HOH   345 2445 720  HOH   HOH A . 
RA 9 HOH   346 2446 588  HOH   HOH A . 
RA 9 HOH   347 2447 919  HOH   HOH A . 
RA 9 HOH   348 2448 1150 HOH   HOH A . 
RA 9 HOH   349 2449 1941 HOH   HOH A . 
RA 9 HOH   350 2450 230  HOH   HOH A . 
RA 9 HOH   351 2451 711  HOH   HOH A . 
RA 9 HOH   352 2452 659  HOH   HOH A . 
RA 9 HOH   353 2453 43   HOH   HOH A . 
RA 9 HOH   354 2454 290  HOH   HOH A . 
RA 9 HOH   355 2455 1144 HOH   HOH A . 
RA 9 HOH   356 2456 832  HOH   HOH A . 
RA 9 HOH   357 2457 1951 HOH   HOH A . 
RA 9 HOH   358 2458 359  HOH   HOH A . 
RA 9 HOH   359 2459 415  HOH   HOH A . 
RA 9 HOH   360 2460 283  HOH   HOH A . 
RA 9 HOH   361 2461 482  HOH   HOH A . 
RA 9 HOH   362 2462 1149 HOH   HOH A . 
RA 9 HOH   363 2463 226  HOH   HOH A . 
RA 9 HOH   364 2464 41   HOH   HOH A . 
RA 9 HOH   365 2465 834  HOH   HOH A . 
RA 9 HOH   366 2466 745  HOH   HOH A . 
RA 9 HOH   367 2467 432  HOH   HOH A . 
RA 9 HOH   368 2468 1697 HOH   HOH A . 
RA 9 HOH   369 2469 340  HOH   HOH A . 
RA 9 HOH   370 2470 718  HOH   HOH A . 
RA 9 HOH   371 2471 616  HOH   HOH A . 
RA 9 HOH   372 2472 314  HOH   HOH A . 
RA 9 HOH   373 2473 51   HOH   HOH A . 
RA 9 HOH   374 2474 1237 HOH   HOH A . 
RA 9 HOH   375 2475 1533 HOH   HOH A . 
RA 9 HOH   376 2476 35   HOH   HOH A . 
RA 9 HOH   377 2477 785  HOH   HOH A . 
RA 9 HOH   378 2478 1434 HOH   HOH A . 
RA 9 HOH   379 2479 192  HOH   HOH A . 
RA 9 HOH   380 2480 1245 HOH   HOH A . 
RA 9 HOH   381 2481 330  HOH   HOH A . 
RA 9 HOH   382 2482 362  HOH   HOH A . 
RA 9 HOH   383 2483 774  HOH   HOH A . 
RA 9 HOH   384 2484 325  HOH   HOH A . 
RA 9 HOH   385 2485 654  HOH   HOH A . 
RA 9 HOH   386 2486 1935 HOH   HOH A . 
RA 9 HOH   387 2487 572  HOH   HOH A . 
RA 9 HOH   388 2488 163  HOH   HOH A . 
RA 9 HOH   389 2489 632  HOH   HOH A . 
RA 9 HOH   390 2490 564  HOH   HOH A . 
RA 9 HOH   391 2491 867  HOH   HOH A . 
RA 9 HOH   392 2492 760  HOH   HOH A . 
RA 9 HOH   393 2493 1276 HOH   HOH A . 
RA 9 HOH   394 2494 858  HOH   HOH A . 
RA 9 HOH   395 2495 856  HOH   HOH A . 
RA 9 HOH   396 2496 578  HOH   HOH A . 
RA 9 HOH   397 2497 241  HOH   HOH A . 
RA 9 HOH   398 2498 357  HOH   HOH A . 
RA 9 HOH   399 2499 940  HOH   HOH A . 
RA 9 HOH   400 2500 894  HOH   HOH A . 
RA 9 HOH   401 2501 1497 HOH   HOH A . 
RA 9 HOH   402 2502 350  HOH   HOH A . 
RA 9 HOH   403 2503 1105 HOH   HOH A . 
RA 9 HOH   404 2504 296  HOH   HOH A . 
RA 9 HOH   405 2505 1074 HOH   HOH A . 
RA 9 HOH   406 2506 1486 HOH   HOH A . 
RA 9 HOH   407 2507 17   HOH   HOH A . 
RA 9 HOH   408 2508 337  HOH   HOH A . 
RA 9 HOH   409 2509 558  HOH   HOH A . 
RA 9 HOH   410 2510 116  HOH   HOH A . 
RA 9 HOH   411 2511 1732 HOH   HOH A . 
RA 9 HOH   412 2512 493  HOH   HOH A . 
RA 9 HOH   413 2513 447  HOH   HOH A . 
RA 9 HOH   414 2514 1561 HOH   HOH A . 
RA 9 HOH   415 2515 1460 HOH   HOH A . 
RA 9 HOH   416 2516 1958 HOH   HOH A . 
RA 9 HOH   417 2517 260  HOH   HOH A . 
RA 9 HOH   418 2518 295  HOH   HOH A . 
RA 9 HOH   419 2519 1378 HOH   HOH A . 
RA 9 HOH   420 2520 60   HOH   HOH A . 
RA 9 HOH   421 2521 360  HOH   HOH A . 
RA 9 HOH   422 2522 938  HOH   HOH A . 
RA 9 HOH   423 2523 1194 HOH   HOH A . 
RA 9 HOH   424 2524 1111 HOH   HOH A . 
RA 9 HOH   425 2525 1762 HOH   HOH A . 
RA 9 HOH   426 2526 132  HOH   HOH A . 
RA 9 HOH   427 2527 767  HOH   HOH A . 
RA 9 HOH   428 2528 885  HOH   HOH A . 
RA 9 HOH   429 2529 733  HOH   HOH A . 
RA 9 HOH   430 2530 1306 HOH   HOH A . 
RA 9 HOH   431 2531 263  HOH   HOH A . 
RA 9 HOH   432 2532 809  HOH   HOH A . 
RA 9 HOH   433 2533 939  HOH   HOH A . 
RA 9 HOH   434 2534 24   HOH   HOH A . 
RA 9 HOH   435 2535 216  HOH   HOH A . 
RA 9 HOH   436 2536 1076 HOH   HOH A . 
RA 9 HOH   437 2537 1220 HOH   HOH A . 
RA 9 HOH   438 2538 1945 HOH   HOH A . 
RA 9 HOH   439 2539 614  HOH   HOH A . 
RA 9 HOH   440 2540 26   HOH   HOH A . 
RA 9 HOH   441 2541 1384 HOH   HOH A . 
RA 9 HOH   442 2542 89   HOH   HOH A . 
RA 9 HOH   443 2543 238  HOH   HOH A . 
RA 9 HOH   444 2544 288  HOH   HOH A . 
RA 9 HOH   445 2545 9    HOH   HOH A . 
RA 9 HOH   446 2546 36   HOH   HOH A . 
RA 9 HOH   447 2547 1616 HOH   HOH A . 
RA 9 HOH   448 2548 796  HOH   HOH A . 
RA 9 HOH   449 2549 737  HOH   HOH A . 
RA 9 HOH   450 2550 1052 HOH   HOH A . 
RA 9 HOH   451 2551 773  HOH   HOH A . 
RA 9 HOH   452 2552 607  HOH   HOH A . 
RA 9 HOH   453 2553 1593 HOH   HOH A . 
RA 9 HOH   454 2554 274  HOH   HOH A . 
RA 9 HOH   455 2555 518  HOH   HOH A . 
RA 9 HOH   456 2556 352  HOH   HOH A . 
RA 9 HOH   457 2557 1555 HOH   HOH A . 
RA 9 HOH   458 2558 122  HOH   HOH A . 
RA 9 HOH   459 2559 327  HOH   HOH A . 
RA 9 HOH   460 2560 998  HOH   HOH A . 
RA 9 HOH   461 2561 1035 HOH   HOH A . 
RA 9 HOH   462 2562 859  HOH   HOH A . 
RA 9 HOH   463 2563 1623 HOH   HOH A . 
RA 9 HOH   464 2564 81   HOH   HOH A . 
RA 9 HOH   465 2565 1270 HOH   HOH A . 
RA 9 HOH   466 2566 61   HOH   HOH A . 
RA 9 HOH   467 2567 735  HOH   HOH A . 
RA 9 HOH   468 2568 727  HOH   HOH A . 
RA 9 HOH   469 2569 38   HOH   HOH A . 
RA 9 HOH   470 2570 440  HOH   HOH A . 
RA 9 HOH   471 2571 1278 HOH   HOH A . 
RA 9 HOH   472 2572 1912 HOH   HOH A . 
RA 9 HOH   473 2573 1315 HOH   HOH A . 
RA 9 HOH   474 2574 127  HOH   HOH A . 
RA 9 HOH   475 2575 553  HOH   HOH A . 
RA 9 HOH   476 2576 177  HOH   HOH A . 
RA 9 HOH   477 2577 698  HOH   HOH A . 
RA 9 HOH   478 2578 98   HOH   HOH A . 
RA 9 HOH   479 2579 866  HOH   HOH A . 
RA 9 HOH   480 2580 883  HOH   HOH A . 
RA 9 HOH   481 2581 1590 HOH   HOH A . 
RA 9 HOH   482 2582 208  HOH   HOH A . 
RA 9 HOH   483 2583 1266 HOH   HOH A . 
RA 9 HOH   484 2584 90   HOH   HOH A . 
RA 9 HOH   485 2585 13   HOH   HOH A . 
RA 9 HOH   486 2586 233  HOH   HOH A . 
RA 9 HOH   487 2587 435  HOH   HOH A . 
RA 9 HOH   488 2588 892  HOH   HOH A . 
RA 9 HOH   489 2589 239  HOH   HOH A . 
RA 9 HOH   490 2590 699  HOH   HOH A . 
RA 9 HOH   491 2591 1289 HOH   HOH A . 
RA 9 HOH   492 2592 45   HOH   HOH A . 
RA 9 HOH   493 2593 380  HOH   HOH A . 
RA 9 HOH   494 2594 793  HOH   HOH A . 
RA 9 HOH   495 2595 448  HOH   HOH A . 
RA 9 HOH   496 2596 347  HOH   HOH A . 
RA 9 HOH   497 2597 494  HOH   HOH A . 
RA 9 HOH   498 2598 78   HOH   HOH A . 
RA 9 HOH   499 2599 148  HOH   HOH A . 
RA 9 HOH   500 2600 611  HOH   HOH A . 
RA 9 HOH   501 2601 1396 HOH   HOH A . 
RA 9 HOH   502 2602 1970 HOH   HOH A . 
RA 9 HOH   503 2603 1765 HOH   HOH A . 
RA 9 HOH   504 2604 1228 HOH   HOH A . 
RA 9 HOH   505 2605 1688 HOH   HOH A . 
RA 9 HOH   506 2606 593  HOH   HOH A . 
RA 9 HOH   507 2607 1012 HOH   HOH A . 
RA 9 HOH   508 2608 1521 HOH   HOH A . 
RA 9 HOH   509 2609 795  HOH   HOH A . 
RA 9 HOH   510 2610 289  HOH   HOH A . 
RA 9 HOH   511 2611 913  HOH   HOH A . 
RA 9 HOH   512 2612 303  HOH   HOH A . 
RA 9 HOH   513 2613 602  HOH   HOH A . 
RA 9 HOH   514 2614 907  HOH   HOH A . 
RA 9 HOH   515 2615 673  HOH   HOH A . 
RA 9 HOH   516 2616 1134 HOH   HOH A . 
RA 9 HOH   517 2617 511  HOH   HOH A . 
RA 9 HOH   518 2618 1483 HOH   HOH A . 
RA 9 HOH   519 2619 1082 HOH   HOH A . 
RA 9 HOH   520 2620 42   HOH   HOH A . 
RA 9 HOH   521 2621 691  HOH   HOH A . 
RA 9 HOH   522 2622 714  HOH   HOH A . 
RA 9 HOH   523 2623 1968 HOH   HOH A . 
RA 9 HOH   524 2624 1341 HOH   HOH A . 
RA 9 HOH   525 2625 533  HOH   HOH A . 
RA 9 HOH   526 2626 561  HOH   HOH A . 
RA 9 HOH   527 2627 1656 HOH   HOH A . 
RA 9 HOH   528 2628 348  HOH   HOH A . 
RA 9 HOH   529 2629 1766 HOH   HOH A . 
RA 9 HOH   530 2630 173  HOH   HOH A . 
RA 9 HOH   531 2631 922  HOH   HOH A . 
RA 9 HOH   532 2632 67   HOH   HOH A . 
RA 9 HOH   533 2633 1181 HOH   HOH A . 
RA 9 HOH   534 2634 75   HOH   HOH A . 
RA 9 HOH   535 2635 709  HOH   HOH A . 
RA 9 HOH   536 2636 56   HOH   HOH A . 
RA 9 HOH   537 2637 573  HOH   HOH A . 
RA 9 HOH   538 2638 1523 HOH   HOH A . 
RA 9 HOH   539 2639 402  HOH   HOH A . 
RA 9 HOH   540 2640 636  HOH   HOH A . 
RA 9 HOH   541 2641 1154 HOH   HOH A . 
RA 9 HOH   542 2642 1549 HOH   HOH A . 
RA 9 HOH   543 2643 641  HOH   HOH A . 
RA 9 HOH   544 2644 516  HOH   HOH A . 
RA 9 HOH   545 2645 339  HOH   HOH A . 
RA 9 HOH   546 2646 693  HOH   HOH A . 
RA 9 HOH   547 2647 562  HOH   HOH A . 
RA 9 HOH   548 2648 308  HOH   HOH A . 
RA 9 HOH   549 2649 1908 HOH   HOH A . 
RA 9 HOH   550 2650 994  HOH   HOH A . 
RA 9 HOH   551 2651 115  HOH   HOH A . 
RA 9 HOH   552 2652 648  HOH   HOH A . 
RA 9 HOH   553 2653 1385 HOH   HOH A . 
RA 9 HOH   554 2654 1050 HOH   HOH A . 
RA 9 HOH   555 2655 1089 HOH   HOH A . 
RA 9 HOH   556 2656 1345 HOH   HOH A . 
RA 9 HOH   557 2657 837  HOH   HOH A . 
RA 9 HOH   558 2658 190  HOH   HOH A . 
RA 9 HOH   559 2659 1079 HOH   HOH A . 
RA 9 HOH   560 2660 923  HOH   HOH A . 
RA 9 HOH   561 2661 528  HOH   HOH A . 
RA 9 HOH   562 2662 1937 HOH   HOH A . 
RA 9 HOH   563 2663 454  HOH   HOH A . 
RA 9 HOH   564 2664 839  HOH   HOH A . 
RA 9 HOH   565 2665 400  HOH   HOH A . 
RA 9 HOH   566 2666 936  HOH   HOH A . 
RA 9 HOH   567 2667 899  HOH   HOH A . 
RA 9 HOH   568 2668 182  HOH   HOH A . 
RA 9 HOH   569 2669 980  HOH   HOH A . 
RA 9 HOH   570 2670 694  HOH   HOH A . 
RA 9 HOH   571 2671 204  HOH   HOH A . 
RA 9 HOH   572 2672 1797 HOH   HOH A . 
RA 9 HOH   573 2673 973  HOH   HOH A . 
RA 9 HOH   574 2674 1969 HOH   HOH A . 
RA 9 HOH   575 2675 879  HOH   HOH A . 
RA 9 HOH   576 2676 1049 HOH   HOH A . 
RA 9 HOH   577 2677 1034 HOH   HOH A . 
RA 9 HOH   578 2678 147  HOH   HOH A . 
RA 9 HOH   579 2679 1163 HOH   HOH A . 
RA 9 HOH   580 2680 418  HOH   HOH A . 
RA 9 HOH   581 2681 1781 HOH   HOH A . 
RA 9 HOH   582 2682 1025 HOH   HOH A . 
RA 9 HOH   583 2683 732  HOH   HOH A . 
RA 9 HOH   584 2684 1331 HOH   HOH A . 
RA 9 HOH   585 2685 1190 HOH   HOH A . 
RA 9 HOH   586 2686 876  HOH   HOH A . 
RA 9 HOH   587 2687 1058 HOH   HOH A . 
RA 9 HOH   588 2688 497  HOH   HOH A . 
RA 9 HOH   589 2689 242  HOH   HOH A . 
RA 9 HOH   590 2690 692  HOH   HOH A . 
RA 9 HOH   591 2691 1424 HOH   HOH A . 
RA 9 HOH   592 2692 1645 HOH   HOH A . 
RA 9 HOH   593 2693 1534 HOH   HOH A . 
RA 9 HOH   594 2694 1495 HOH   HOH A . 
RA 9 HOH   595 2695 1106 HOH   HOH A . 
RA 9 HOH   596 2696 568  HOH   HOH A . 
RA 9 HOH   597 2697 235  HOH   HOH A . 
RA 9 HOH   598 2698 657  HOH   HOH A . 
RA 9 HOH   599 2699 862  HOH   HOH A . 
RA 9 HOH   600 2700 131  HOH   HOH A . 
RA 9 HOH   601 2701 1638 HOH   HOH A . 
RA 9 HOH   602 2702 389  HOH   HOH A . 
RA 9 HOH   603 2703 1308 HOH   HOH A . 
RA 9 HOH   604 2704 1514 HOH   HOH A . 
RA 9 HOH   605 2705 1922 HOH   HOH A . 
RA 9 HOH   606 2706 396  HOH   HOH A . 
RA 9 HOH   607 2707 1187 HOH   HOH A . 
RA 9 HOH   608 2708 1564 HOH   HOH A . 
RA 9 HOH   609 2709 1103 HOH   HOH A . 
RA 9 HOH   610 2710 901  HOH   HOH A . 
RA 9 HOH   611 2711 1080 HOH   HOH A . 
RA 9 HOH   612 2712 1165 HOH   HOH A . 
RA 9 HOH   613 2713 870  HOH   HOH A . 
RA 9 HOH   614 2714 1653 HOH   HOH A . 
RA 9 HOH   615 2715 612  HOH   HOH A . 
RA 9 HOH   616 2716 1814 HOH   HOH A . 
RA 9 HOH   617 2717 1346 HOH   HOH A . 
RA 9 HOH   618 2718 471  HOH   HOH A . 
RA 9 HOH   619 2719 183  HOH   HOH A . 
RA 9 HOH   620 2720 1408 HOH   HOH A . 
RA 9 HOH   621 2721 794  HOH   HOH A . 
RA 9 HOH   622 2722 1222 HOH   HOH A . 
RA 9 HOH   623 2723 921  HOH   HOH A . 
RA 9 HOH   624 2724 1801 HOH   HOH A . 
RA 9 HOH   625 2725 672  HOH   HOH A . 
RA 9 HOH   626 2726 1008 HOH   HOH A . 
RA 9 HOH   627 2727 220  HOH   HOH A . 
RA 9 HOH   628 2728 361  HOH   HOH A . 
RA 9 HOH   629 2729 1011 HOH   HOH A . 
RA 9 HOH   630 2730 1140 HOH   HOH A . 
RA 9 HOH   631 2731 1421 HOH   HOH A . 
RA 9 HOH   632 2732 477  HOH   HOH A . 
RA 9 HOH   633 2733 441  HOH   HOH A . 
RA 9 HOH   634 2734 1291 HOH   HOH A . 
RA 9 HOH   635 2735 483  HOH   HOH A . 
RA 9 HOH   636 2736 606  HOH   HOH A . 
RA 9 HOH   637 2737 1876 HOH   HOH A . 
RA 9 HOH   638 2738 311  HOH   HOH A . 
RA 9 HOH   639 2739 897  HOH   HOH A . 
RA 9 HOH   640 2740 1698 HOH   HOH A . 
RA 9 HOH   641 2741 1606 HOH   HOH A . 
RA 9 HOH   642 2742 551  HOH   HOH A . 
RA 9 HOH   643 2743 306  HOH   HOH A . 
RA 9 HOH   644 2744 1436 HOH   HOH A . 
RA 9 HOH   645 2745 1562 HOH   HOH A . 
RA 9 HOH   646 2746 1261 HOH   HOH A . 
RA 9 HOH   647 2747 1773 HOH   HOH A . 
RA 9 HOH   648 2748 1004 HOH   HOH A . 
RA 9 HOH   649 2749 1041 HOH   HOH A . 
RA 9 HOH   650 2750 1867 HOH   HOH A . 
RA 9 HOH   651 2751 1749 HOH   HOH A . 
RA 9 HOH   652 2752 1028 HOH   HOH A . 
RA 9 HOH   653 2753 14   HOH   HOH A . 
RA 9 HOH   654 2754 169  HOH   HOH A . 
RA 9 HOH   655 2755 1247 HOH   HOH A . 
RA 9 HOH   656 2756 1807 HOH   HOH A . 
RA 9 HOH   657 2757 1934 HOH   HOH A . 
RA 9 HOH   658 2758 1248 HOH   HOH A . 
RA 9 HOH   659 2759 821  HOH   HOH A . 
RA 9 HOH   660 2760 1531 HOH   HOH A . 
RA 9 HOH   661 2761 1286 HOH   HOH A . 
RA 9 HOH   662 2762 397  HOH   HOH A . 
RA 9 HOH   663 2763 1878 HOH   HOH A . 
RA 9 HOH   664 2764 416  HOH   HOH A . 
RA 9 HOH   665 2765 249  HOH   HOH A . 
RA 9 HOH   666 2766 221  HOH   HOH A . 
RA 9 HOH   667 2767 819  HOH   HOH A . 
RA 9 HOH   668 2768 324  HOH   HOH A . 
RA 9 HOH   669 2769 27   HOH   HOH A . 
RA 9 HOH   670 2770 1724 HOH   HOH A . 
RA 9 HOH   671 2771 1469 HOH   HOH A . 
RA 9 HOH   672 2772 619  HOH   HOH A . 
RA 9 HOH   673 2773 623  HOH   HOH A . 
RA 9 HOH   674 2774 729  HOH   HOH A . 
RA 9 HOH   675 2775 1368 HOH   HOH A . 
RA 9 HOH   676 2776 1898 HOH   HOH A . 
RA 9 HOH   677 2777 1544 HOH   HOH A . 
RA 9 HOH   678 2778 1356 HOH   HOH A . 
RA 9 HOH   679 2779 617  HOH   HOH A . 
RA 9 HOH   680 2780 1718 HOH   HOH A . 
RA 9 HOH   681 2781 1764 HOH   HOH A . 
RA 9 HOH   682 2782 1024 HOH   HOH A . 
RA 9 HOH   683 2783 1601 HOH   HOH A . 
RA 9 HOH   684 2784 1877 HOH   HOH A . 
RA 9 HOH   685 2785 1725 HOH   HOH A . 
RA 9 HOH   686 2786 1485 HOH   HOH A . 
RA 9 HOH   687 2787 918  HOH   HOH A . 
RA 9 HOH   688 2788 515  HOH   HOH A . 
RA 9 HOH   689 2789 1036 HOH   HOH A . 
RA 9 HOH   690 2790 800  HOH   HOH A . 
RA 9 HOH   691 2791 1712 HOH   HOH A . 
RA 9 HOH   692 2792 1864 HOH   HOH A . 
RA 9 HOH   693 2793 1428 HOH   HOH A . 
RA 9 HOH   694 2794 992  HOH   HOH A . 
RA 9 HOH   695 2795 1461 HOH   HOH A . 
RA 9 HOH   696 2796 1018 HOH   HOH A . 
RA 9 HOH   697 2797 1452 HOH   HOH A . 
RA 9 HOH   698 2798 1087 HOH   HOH A . 
RA 9 HOH   699 2799 1070 HOH   HOH A . 
RA 9 HOH   700 2800 1528 HOH   HOH A . 
RA 9 HOH   701 2801 1925 HOH   HOH A . 
RA 9 HOH   702 2802 643  HOH   HOH A . 
RA 9 HOH   703 2803 1837 HOH   HOH A . 
RA 9 HOH   704 2804 1754 HOH   HOH A . 
RA 9 HOH   705 2805 1655 HOH   HOH A . 
RA 9 HOH   706 2806 388  HOH   HOH A . 
RA 9 HOH   707 2807 1668 HOH   HOH A . 
RA 9 HOH   708 2808 1919 HOH   HOH A . 
RA 9 HOH   709 2809 1037 HOH   HOH A . 
RA 9 HOH   710 2810 662  HOH   HOH A . 
RA 9 HOH   711 2811 1853 HOH   HOH A . 
RA 9 HOH   712 2812 1006 HOH   HOH A . 
RA 9 HOH   713 2813 1856 HOH   HOH A . 
RA 9 HOH   714 2814 1722 HOH   HOH A . 
RA 9 HOH   715 2815 1642 HOH   HOH A . 
RA 9 HOH   716 2816 697  HOH   HOH A . 
RA 9 HOH   717 2817 1785 HOH   HOH A . 
RA 9 HOH   718 2818 1715 HOH   HOH A . 
RA 9 HOH   719 2819 1844 HOH   HOH A . 
RA 9 HOH   720 2820 1859 HOH   HOH A . 
RA 9 HOH   721 2821 1295 HOH   HOH A . 
RA 9 HOH   722 2822 1031 HOH   HOH A . 
RA 9 HOH   723 2823 1625 HOH   HOH A . 
RA 9 HOH   724 2824 1208 HOH   HOH A . 
RA 9 HOH   725 2825 678  HOH   HOH A . 
RA 9 HOH   726 2826 1364 HOH   HOH A . 
RA 9 HOH   727 2827 1905 HOH   HOH A . 
RA 9 HOH   728 2828 1799 HOH   HOH A . 
RA 9 HOH   729 2829 1714 HOH   HOH A . 
RA 9 HOH   730 2830 1540 HOH   HOH A . 
RA 9 HOH   731 2831 1798 HOH   HOH A . 
RA 9 HOH   732 2832 1185 HOH   HOH A . 
RA 9 HOH   733 2833 1738 HOH   HOH A . 
RA 9 HOH   734 2834 1500 HOH   HOH A . 
RA 9 HOH   735 2835 1512 HOH   HOH A . 
RA 9 HOH   736 2836 1297 HOH   HOH A . 
RA 9 HOH   737 2837 1536 HOH   HOH A . 
RA 9 HOH   738 2838 1527 HOH   HOH A . 
RA 9 HOH   739 2839 1375 HOH   HOH A . 
RA 9 HOH   740 2840 1552 HOH   HOH A . 
RA 9 HOH   741 2841 1622 HOH   HOH A . 
RA 9 HOH   742 2842 864  HOH   HOH A . 
RA 9 HOH   743 2843 1524 HOH   HOH A . 
RA 9 HOH   744 2844 1730 HOH   HOH A . 
RA 9 HOH   745 2845 1700 HOH   HOH A . 
RA 9 HOH   746 2846 1843 HOH   HOH A . 
RA 9 HOH   747 2847 768  HOH   HOH A . 
RA 9 HOH   748 2848 1776 HOH   HOH A . 
RA 9 HOH   749 2849 1862 HOH   HOH A . 
RA 9 HOH   750 2850 1522 HOH   HOH A . 
RA 9 HOH   751 2851 467  HOH   HOH A . 
RA 9 HOH   752 2852 1651 HOH   HOH A . 
RA 9 HOH   753 2853 1735 HOH   HOH A . 
RA 9 HOH   754 2854 1707 HOH   HOH A . 
RA 9 HOH   755 2855 1572 HOH   HOH A . 
RA 9 HOH   756 2856 1318 HOH   HOH A . 
RA 9 HOH   757 2857 1886 HOH   HOH A . 
RA 9 HOH   758 2858 1390 HOH   HOH A . 
RA 9 HOH   759 2859 1936 HOH   HOH A . 
RA 9 HOH   760 2860 1694 HOH   HOH A . 
RA 9 HOH   761 2861 1872 HOH   HOH A . 
RA 9 HOH   762 2862 1369 HOH   HOH A . 
RA 9 HOH   763 2863 1193 HOH   HOH A . 
RA 9 HOH   764 2864 1737 HOH   HOH A . 
RA 9 HOH   765 2865 1234 HOH   HOH A . 
RA 9 HOH   766 2866 1689 HOH   HOH A . 
RA 9 HOH   767 2867 580  HOH   HOH A . 
RA 9 HOH   768 2868 1480 HOH   HOH A . 
RA 9 HOH   769 2869 1152 HOH   HOH A . 
RA 9 HOH   770 2870 1337 HOH   HOH A . 
RA 9 HOH   771 2871 997  HOH   HOH A . 
RA 9 HOH   772 2872 469  HOH   HOH A . 
RA 9 HOH   773 2873 1260 HOH   HOH A . 
RA 9 HOH   774 2874 1326 HOH   HOH A . 
RA 9 HOH   775 2875 1708 HOH   HOH A . 
RA 9 HOH   776 2876 1298 HOH   HOH A . 
RA 9 HOH   777 2877 1929 HOH   HOH A . 
RA 9 HOH   778 2878 1640 HOH   HOH A . 
RA 9 HOH   779 2879 1183 HOH   HOH A . 
RA 9 HOH   780 2880 917  HOH   HOH A . 
RA 9 HOH   781 2881 1736 HOH   HOH A . 
RA 9 HOH   782 2882 1733 HOH   HOH A . 
RA 9 HOH   783 2883 1389 HOH   HOH A . 
RA 9 HOH   784 2884 948  HOH   HOH A . 
RA 9 HOH   785 2885 1952 HOH   HOH A . 
RA 9 HOH   786 2886 1895 HOH   HOH A . 
RA 9 HOH   787 2887 1758 HOH   HOH A . 
RA 9 HOH   788 2888 1530 HOH   HOH A . 
RA 9 HOH   789 2889 1847 HOH   HOH A . 
RA 9 HOH   790 2890 424  HOH   HOH A . 
RA 9 HOH   791 2891 1231 HOH   HOH A . 
RA 9 HOH   792 2892 1459 HOH   HOH A . 
RA 9 HOH   793 2893 410  HOH   HOH A . 
RA 9 HOH   794 2894 1840 HOH   HOH A . 
RA 9 HOH   795 2895 1423 HOH   HOH A . 
RA 9 HOH   796 2896 253  HOH   HOH A . 
RA 9 HOH   797 2897 1568 HOH   HOH A . 
RA 9 HOH   798 2898 765  HOH   HOH A . 
RA 9 HOH   799 2899 1669 HOH   HOH A . 
RA 9 HOH   800 2900 1687 HOH   HOH A . 
RA 9 HOH   801 2901 1425 HOH   HOH A . 
RA 9 HOH   802 2902 1927 HOH   HOH A . 
RA 9 HOH   803 2903 1097 HOH   HOH A . 
RA 9 HOH   804 2904 1946 HOH   HOH A . 
RA 9 HOH   805 2905 1930 HOH   HOH A . 
RA 9 HOH   806 2906 1804 HOH   HOH A . 
RA 9 HOH   807 2907 1280 HOH   HOH A . 
RA 9 HOH   808 2908 1865 HOH   HOH A . 
RA 9 HOH   809 2909 1960 HOH   HOH A . 
RA 9 HOH   810 2910 1768 HOH   HOH A . 
RA 9 HOH   811 2911 585  HOH   HOH A . 
RA 9 HOH   812 2912 596  HOH   HOH A . 
RA 9 HOH   813 2913 524  HOH   HOH A . 
RA 9 HOH   814 2914 1849 HOH   HOH A . 
RA 9 HOH   815 2915 1873 HOH   HOH A . 
RA 9 HOH   816 2916 1124 HOH   HOH A . 
RA 9 HOH   817 2917 1584 HOH   HOH A . 
RA 9 HOH   818 2918 963  HOH   HOH A . 
RA 9 HOH   819 2919 898  HOH   HOH A . 
RA 9 HOH   820 2920 853  HOH   HOH A . 
RA 9 HOH   821 2921 475  HOH   HOH A . 
RA 9 HOH   822 2922 848  HOH   HOH A . 
RA 9 HOH   823 2923 1683 HOH   HOH A . 
RA 9 HOH   824 2924 1201 HOH   HOH A . 
RA 9 HOH   825 2925 1630 HOH   HOH A . 
RA 9 HOH   826 2926 1747 HOH   HOH A . 
RA 9 HOH   827 2927 1879 HOH   HOH A . 
RA 9 HOH   828 2928 1964 HOH   HOH A . 
RA 9 HOH   829 2929 1169 HOH   HOH A . 
RA 9 HOH   830 2930 1330 HOH   HOH A . 
RA 9 HOH   831 2931 787  HOH   HOH A . 
RA 9 HOH   832 2932 1529 HOH   HOH A . 
RA 9 HOH   833 2933 1673 HOH   HOH A . 
RA 9 HOH   834 2934 1319 HOH   HOH A . 
RA 9 HOH   835 2935 1323 HOH   HOH A . 
RA 9 HOH   836 2936 1899 HOH   HOH A . 
RA 9 HOH   837 2937 1770 HOH   HOH A . 
RA 9 HOH   838 2938 1703 HOH   HOH A . 
RA 9 HOH   839 2939 1774 HOH   HOH A . 
RA 9 HOH   840 2940 1473 HOH   HOH A . 
RA 9 HOH   841 2941 1835 HOH   HOH A . 
RA 9 HOH   842 2942 838  HOH   HOH A . 
RA 9 HOH   843 2943 962  HOH   HOH A . 
RA 9 HOH   844 2944 1147 HOH   HOH A . 
RA 9 HOH   845 2945 1588 HOH   HOH A . 
RA 9 HOH   846 2946 1249 HOH   HOH A . 
RA 9 HOH   847 2947 1148 HOH   HOH A . 
RA 9 HOH   848 2948 1931 HOH   HOH A . 
RA 9 HOH   849 2949 717  HOH   HOH A . 
RA 9 HOH   850 2950 1894 HOH   HOH A . 
RA 9 HOH   851 2951 736  HOH   HOH A . 
RA 9 HOH   852 2952 437  HOH   HOH A . 
RA 9 HOH   853 2953 1591 HOH   HOH A . 
RA 9 HOH   854 2954 1961 HOH   HOH A . 
RA 9 HOH   855 2955 1336 HOH   HOH A . 
RA 9 HOH   856 2956 1182 HOH   HOH A . 
RA 9 HOH   857 2957 1348 HOH   HOH A . 
RA 9 HOH   858 2958 1168 HOH   HOH A . 
RA 9 HOH   859 2959 967  HOH   HOH A . 
RA 9 HOH   860 2960 1502 HOH   HOH A . 
RA 9 HOH   861 2961 1592 HOH   HOH A . 
RA 9 HOH   862 2962 1175 HOH   HOH A . 
RA 9 HOH   863 2963 982  HOH   HOH A . 
RA 9 HOH   864 2964 1537 HOH   HOH A . 
RA 9 HOH   865 2965 1258 HOH   HOH A . 
RA 9 HOH   866 2966 1959 HOH   HOH A . 
RA 9 HOH   867 2967 227  HOH   HOH A . 
RA 9 HOH   868 2968 1129 HOH   HOH A . 
RA 9 HOH   869 2969 1096 HOH   HOH A . 
RA 9 HOH   870 2970 622  HOH   HOH A . 
RA 9 HOH   871 2971 886  HOH   HOH A . 
RA 9 HOH   872 2972 1887 HOH   HOH A . 
RA 9 HOH   873 2973 1775 HOH   HOH A . 
RA 9 HOH   874 2974 1019 HOH   HOH A . 
RA 9 HOH   875 2975 955  HOH   HOH A . 
RA 9 HOH   876 2976 630  HOH   HOH A . 
RA 9 HOH   877 2977 1002 HOH   HOH A . 
RA 9 HOH   878 2978 1745 HOH   HOH A . 
RA 9 HOH   879 2979 1563 HOH   HOH A . 
RA 9 HOH   880 2980 1282 HOH   HOH A . 
RA 9 HOH   881 2981 1757 HOH   HOH A . 
RA 9 HOH   882 2982 1743 HOH   HOH A . 
RA 9 HOH   883 2983 1639 HOH   HOH A . 
RA 9 HOH   884 2984 1422 HOH   HOH A . 
RA 9 HOH   885 2985 1771 HOH   HOH A . 
RA 9 HOH   886 2986 841  HOH   HOH A . 
RA 9 HOH   887 2987 1786 HOH   HOH A . 
RA 9 HOH   888 2988 1171 HOH   HOH A . 
RA 9 HOH   889 2989 1312 HOH   HOH A . 
RA 9 HOH   890 2990 1535 HOH   HOH A . 
RA 9 HOH   891 2991 854  HOH   HOH A . 
RA 9 HOH   892 2992 243  HOH   HOH A . 
RA 9 HOH   893 2993 1709 HOH   HOH A . 
RA 9 HOH   894 2994 1949 HOH   HOH A . 
RA 9 HOH   895 2995 1329 HOH   HOH A . 
RA 9 HOH   896 2996 1493 HOH   HOH A . 
RA 9 HOH   897 2997 766  HOH   HOH A . 
RA 9 HOH   898 2998 1262 HOH   HOH A . 
RA 9 HOH   899 2999 1647 HOH   HOH A . 
RA 9 HOH   900 3000 1767 HOH   HOH A . 
RA 9 HOH   901 3001 1292 HOH   HOH A . 
RA 9 HOH   902 3002 1755 HOH   HOH A . 
RA 9 HOH   903 3003 1573 HOH   HOH A . 
RA 9 HOH   904 3004 1069 HOH   HOH A . 
RA 9 HOH   905 3005 651  HOH   HOH A . 
RA 9 HOH   906 3006 1759 HOH   HOH A . 
RA 9 HOH   907 3007 1365 HOH   HOH A . 
RA 9 HOH   908 3008 1217 HOH   HOH A . 
RA 9 HOH   909 3009 708  HOH   HOH A . 
RA 9 HOH   910 3010 1581 HOH   HOH A . 
RA 9 HOH   911 3011 1784 HOH   HOH A . 
RA 9 HOH   912 3012 783  HOH   HOH A . 
RA 9 HOH   913 3013 1928 HOH   HOH A . 
RA 9 HOH   914 3014 1803 HOH   HOH A . 
RA 9 HOH   915 3015 1796 HOH   HOH A . 
RA 9 HOH   916 3016 1363 HOH   HOH A . 
RA 9 HOH   917 3017 701  HOH   HOH A . 
RA 9 HOH   918 3018 1178 HOH   HOH A . 
RA 9 HOH   919 3019 1787 HOH   HOH A . 
RA 9 HOH   920 3020 1780 HOH   HOH A . 
RA 9 HOH   921 3021 1104 HOH   HOH A . 
RA 9 HOH   922 3022 1212 HOH   HOH A . 
RA 9 HOH   923 3023 1225 HOH   HOH A . 
RA 9 HOH   924 3024 908  HOH   HOH A . 
RA 9 HOH   925 3025 763  HOH   HOH A . 
SA 9 HOH   1   2101 488  HOH   HOH B . 
SA 9 HOH   2   2102 1400 HOH   HOH B . 
SA 9 HOH   3   2103 1416 HOH   HOH B . 
SA 9 HOH   4   2104 1632 HOH   HOH B . 
SA 9 HOH   5   2105 637  HOH   HOH B . 
SA 9 HOH   6   2106 1155 HOH   HOH B . 
SA 9 HOH   7   2107 436  HOH   HOH B . 
SA 9 HOH   8   2108 1215 HOH   HOH B . 
SA 9 HOH   9   2109 1902 HOH   HOH B . 
SA 9 HOH   10  2110 739  HOH   HOH B . 
SA 9 HOH   11  2111 828  HOH   HOH B . 
SA 9 HOH   12  2112 912  HOH   HOH B . 
SA 9 HOH   13  2113 904  HOH   HOH B . 
SA 9 HOH   14  2114 532  HOH   HOH B . 
SA 9 HOH   15  2115 1267 HOH   HOH B . 
SA 9 HOH   16  2116 466  HOH   HOH B . 
SA 9 HOH   17  2117 534  HOH   HOH B . 
SA 9 HOH   18  2118 983  HOH   HOH B . 
SA 9 HOH   19  2119 1830 HOH   HOH B . 
SA 9 HOH   20  2120 499  HOH   HOH B . 
SA 9 HOH   21  2121 695  HOH   HOH B . 
SA 9 HOH   22  2122 696  HOH   HOH B . 
SA 9 HOH   23  2123 1088 HOH   HOH B . 
SA 9 HOH   24  2124 398  HOH   HOH B . 
SA 9 HOH   25  2125 1032 HOH   HOH B . 
SA 9 HOH   26  2126 1481 HOH   HOH B . 
SA 9 HOH   27  2127 725  HOH   HOH B . 
SA 9 HOH   28  2128 1906 HOH   HOH B . 
SA 9 HOH   29  2129 1681 HOH   HOH B . 
SA 9 HOH   30  2130 1059 HOH   HOH B . 
SA 9 HOH   31  2131 248  HOH   HOH B . 
SA 9 HOH   32  2132 603  HOH   HOH B . 
SA 9 HOH   33  2133 550  HOH   HOH B . 
SA 9 HOH   34  2134 1051 HOH   HOH B . 
SA 9 HOH   35  2135 778  HOH   HOH B . 
SA 9 HOH   36  2136 877  HOH   HOH B . 
SA 9 HOH   37  2137 1637 HOH   HOH B . 
SA 9 HOH   38  2138 1868 HOH   HOH B . 
SA 9 HOH   39  2139 541  HOH   HOH B . 
SA 9 HOH   40  2140 259  HOH   HOH B . 
SA 9 HOH   41  2141 1848 HOH   HOH B . 
SA 9 HOH   42  2142 309  HOH   HOH B . 
SA 9 HOH   43  2143 1825 HOH   HOH B . 
SA 9 HOH   44  2144 1195 HOH   HOH B . 
SA 9 HOH   45  2145 508  HOH   HOH B . 
SA 9 HOH   46  2146 391  HOH   HOH B . 
SA 9 HOH   47  2147 104  HOH   HOH B . 
SA 9 HOH   48  2148 237  HOH   HOH B . 
SA 9 HOH   49  2149 937  HOH   HOH B . 
SA 9 HOH   50  2150 1829 HOH   HOH B . 
SA 9 HOH   51  2151 863  HOH   HOH B . 
SA 9 HOH   52  2152 455  HOH   HOH B . 
SA 9 HOH   53  2153 731  HOH   HOH B . 
SA 9 HOH   54  2154 334  HOH   HOH B . 
SA 9 HOH   55  2155 1629 HOH   HOH B . 
SA 9 HOH   56  2156 82   HOH   HOH B . 
SA 9 HOH   57  2157 609  HOH   HOH B . 
SA 9 HOH   58  2158 37   HOH   HOH B . 
SA 9 HOH   59  2159 341  HOH   HOH B . 
SA 9 HOH   60  2160 1332 HOH   HOH B . 
SA 9 HOH   61  2161 507  HOH   HOH B . 
SA 9 HOH   62  2162 1506 HOH   HOH B . 
SA 9 HOH   63  2163 1914 HOH   HOH B . 
SA 9 HOH   64  2164 464  HOH   HOH B . 
SA 9 HOH   65  2165 1325 HOH   HOH B . 
SA 9 HOH   66  2166 649  HOH   HOH B . 
SA 9 HOH   67  2167 549  HOH   HOH B . 
SA 9 HOH   68  2168 72   HOH   HOH B . 
SA 9 HOH   69  2169 880  HOH   HOH B . 
SA 9 HOH   70  2170 411  HOH   HOH B . 
SA 9 HOH   71  2171 999  HOH   HOH B . 
SA 9 HOH   72  2172 953  HOH   HOH B . 
SA 9 HOH   73  2173 231  HOH   HOH B . 
SA 9 HOH   74  2174 8    HOH   HOH B . 
SA 9 HOH   75  2175 1094 HOH   HOH B . 
SA 9 HOH   76  2176 756  HOH   HOH B . 
SA 9 HOH   77  2177 1913 HOH   HOH B . 
SA 9 HOH   78  2178 915  HOH   HOH B . 
SA 9 HOH   79  2179 1159 HOH   HOH B . 
SA 9 HOH   80  2180 1213 HOH   HOH B . 
SA 9 HOH   81  2181 1294 HOH   HOH B . 
SA 9 HOH   82  2182 591  HOH   HOH B . 
SA 9 HOH   83  2183 1437 HOH   HOH B . 
SA 9 HOH   84  2184 320  HOH   HOH B . 
SA 9 HOH   85  2185 599  HOH   HOH B . 
SA 9 HOH   86  2186 244  HOH   HOH B . 
SA 9 HOH   87  2187 1120 HOH   HOH B . 
SA 9 HOH   88  2188 590  HOH   HOH B . 
SA 9 HOH   89  2189 633  HOH   HOH B . 
SA 9 HOH   90  2190 476  HOH   HOH B . 
SA 9 HOH   91  2191 1207 HOH   HOH B . 
SA 9 HOH   92  2192 1102 HOH   HOH B . 
SA 9 HOH   93  2193 1858 HOH   HOH B . 
SA 9 HOH   94  2194 193  HOH   HOH B . 
SA 9 HOH   95  2195 1509 HOH   HOH B . 
SA 9 HOH   96  2196 70   HOH   HOH B . 
SA 9 HOH   97  2197 1189 HOH   HOH B . 
SA 9 HOH   98  2198 584  HOH   HOH B . 
SA 9 HOH   99  2199 136  HOH   HOH B . 
SA 9 HOH   100 2200 1672 HOH   HOH B . 
SA 9 HOH   101 2201 1091 HOH   HOH B . 
SA 9 HOH   102 2202 976  HOH   HOH B . 
SA 9 HOH   103 2203 486  HOH   HOH B . 
SA 9 HOH   104 2204 433  HOH   HOH B . 
SA 9 HOH   105 2205 713  HOH   HOH B . 
SA 9 HOH   106 2206 1085 HOH   HOH B . 
SA 9 HOH   107 2207 157  HOH   HOH B . 
SA 9 HOH   108 2208 1139 HOH   HOH B . 
SA 9 HOH   109 2209 723  HOH   HOH B . 
SA 9 HOH   110 2210 438  HOH   HOH B . 
SA 9 HOH   111 2211 635  HOH   HOH B . 
SA 9 HOH   112 2212 1138 HOH   HOH B . 
SA 9 HOH   113 2213 1338 HOH   HOH B . 
SA 9 HOH   114 2214 1023 HOH   HOH B . 
SA 9 HOH   115 2215 751  HOH   HOH B . 
SA 9 HOH   116 2216 1383 HOH   HOH B . 
SA 9 HOH   117 2217 950  HOH   HOH B . 
SA 9 HOH   118 2218 1763 HOH   HOH B . 
SA 9 HOH   119 2219 668  HOH   HOH B . 
SA 9 HOH   120 2220 1241 HOH   HOH B . 
SA 9 HOH   121 2221 251  HOH   HOH B . 
SA 9 HOH   122 2222 406  HOH   HOH B . 
SA 9 HOH   123 2223 188  HOH   HOH B . 
SA 9 HOH   124 2224 44   HOH   HOH B . 
SA 9 HOH   125 2225 930  HOH   HOH B . 
SA 9 HOH   126 2226 110  HOH   HOH B . 
SA 9 HOH   127 2227 1253 HOH   HOH B . 
SA 9 HOH   128 2228 490  HOH   HOH B . 
SA 9 HOH   129 2229 156  HOH   HOH B . 
SA 9 HOH   130 2230 315  HOH   HOH B . 
SA 9 HOH   131 2231 538  HOH   HOH B . 
SA 9 HOH   132 2232 92   HOH   HOH B . 
SA 9 HOH   133 2233 1125 HOH   HOH B . 
SA 9 HOH   134 2234 1172 HOH   HOH B . 
SA 9 HOH   135 2235 1519 HOH   HOH B . 
SA 9 HOH   136 2236 1685 HOH   HOH B . 
SA 9 HOH   137 2237 1426 HOH   HOH B . 
SA 9 HOH   138 2238 465  HOH   HOH B . 
SA 9 HOH   139 2239 810  HOH   HOH B . 
SA 9 HOH   140 2240 307  HOH   HOH B . 
SA 9 HOH   141 2241 178  HOH   HOH B . 
SA 9 HOH   142 2242 370  HOH   HOH B . 
SA 9 HOH   143 2243 74   HOH   HOH B . 
SA 9 HOH   144 2244 1909 HOH   HOH B . 
SA 9 HOH   145 2245 417  HOH   HOH B . 
SA 9 HOH   146 2246 1939 HOH   HOH B . 
SA 9 HOH   147 2247 566  HOH   HOH B . 
SA 9 HOH   148 2248 642  HOH   HOH B . 
SA 9 HOH   149 2249 68   HOH   HOH B . 
SA 9 HOH   150 2250 212  HOH   HOH B . 
SA 9 HOH   151 2251 675  HOH   HOH B . 
SA 9 HOH   152 2252 1413 HOH   HOH B . 
SA 9 HOH   153 2253 189  HOH   HOH B . 
SA 9 HOH   154 2254 1756 HOH   HOH B . 
SA 9 HOH   155 2255 1229 HOH   HOH B . 
SA 9 HOH   156 2256 164  HOH   HOH B . 
SA 9 HOH   157 2257 101  HOH   HOH B . 
SA 9 HOH   158 2258 196  HOH   HOH B . 
SA 9 HOH   159 2259 1179 HOH   HOH B . 
SA 9 HOH   160 2260 1334 HOH   HOH B . 
SA 9 HOH   161 2261 498  HOH   HOH B . 
SA 9 HOH   162 2262 463  HOH   HOH B . 
SA 9 HOH   163 2263 1110 HOH   HOH B . 
SA 9 HOH   164 2264 431  HOH   HOH B . 
SA 9 HOH   165 2265 1834 HOH   HOH B . 
SA 9 HOH   166 2266 676  HOH   HOH B . 
SA 9 HOH   167 2267 250  HOH   HOH B . 
SA 9 HOH   168 2268 1659 HOH   HOH B . 
SA 9 HOH   169 2269 1064 HOH   HOH B . 
SA 9 HOH   170 2270 772  HOH   HOH B . 
SA 9 HOH   171 2271 313  HOH   HOH B . 
SA 9 HOH   172 2272 151  HOH   HOH B . 
SA 9 HOH   173 2273 660  HOH   HOH B . 
SA 9 HOH   174 2274 69   HOH   HOH B . 
SA 9 HOH   175 2275 1063 HOH   HOH B . 
SA 9 HOH   176 2276 640  HOH   HOH B . 
SA 9 HOH   177 2277 2    HOH   HOH B . 
SA 9 HOH   178 2278 597  HOH   HOH B . 
SA 9 HOH   179 2279 393  HOH   HOH B . 
SA 9 HOH   180 2280 202  HOH   HOH B . 
SA 9 HOH   181 2281 480  HOH   HOH B . 
SA 9 HOH   182 2282 10   HOH   HOH B . 
SA 9 HOH   183 2283 861  HOH   HOH B . 
SA 9 HOH   184 2284 865  HOH   HOH B . 
SA 9 HOH   185 2285 266  HOH   HOH B . 
SA 9 HOH   186 2286 1340 HOH   HOH B . 
SA 9 HOH   187 2287 489  HOH   HOH B . 
SA 9 HOH   188 2288 869  HOH   HOH B . 
SA 9 HOH   189 2289 270  HOH   HOH B . 
SA 9 HOH   190 2290 63   HOH   HOH B . 
SA 9 HOH   191 2291 634  HOH   HOH B . 
SA 9 HOH   192 2292 343  HOH   HOH B . 
SA 9 HOH   193 2293 1432 HOH   HOH B . 
SA 9 HOH   194 2294 827  HOH   HOH B . 
SA 9 HOH   195 2295 1060 HOH   HOH B . 
SA 9 HOH   196 2296 777  HOH   HOH B . 
SA 9 HOH   197 2297 420  HOH   HOH B . 
SA 9 HOH   198 2298 1515 HOH   HOH B . 
SA 9 HOH   199 2299 286  HOH   HOH B . 
SA 9 HOH   200 2300 33   HOH   HOH B . 
SA 9 HOH   201 2301 712  HOH   HOH B . 
SA 9 HOH   202 2302 824  HOH   HOH B . 
SA 9 HOH   203 2303 369  HOH   HOH B . 
SA 9 HOH   204 2304 1938 HOH   HOH B . 
SA 9 HOH   205 2305 605  HOH   HOH B . 
SA 9 HOH   206 2306 1100 HOH   HOH B . 
SA 9 HOH   207 2307 744  HOH   HOH B . 
SA 9 HOH   208 2308 1477 HOH   HOH B . 
SA 9 HOH   209 2309 978  HOH   HOH B . 
SA 9 HOH   210 2310 555  HOH   HOH B . 
SA 9 HOH   211 2311 715  HOH   HOH B . 
SA 9 HOH   212 2312 818  HOH   HOH B . 
SA 9 HOH   213 2313 199  HOH   HOH B . 
SA 9 HOH   214 2314 1243 HOH   HOH B . 
SA 9 HOH   215 2315 610  HOH   HOH B . 
SA 9 HOH   216 2316 1816 HOH   HOH B . 
SA 9 HOH   217 2317 1411 HOH   HOH B . 
SA 9 HOH   218 2318 135  HOH   HOH B . 
SA 9 HOH   219 2319 39   HOH   HOH B . 
SA 9 HOH   220 2320 105  HOH   HOH B . 
SA 9 HOH   221 2321 356  HOH   HOH B . 
SA 9 HOH   222 2322 456  HOH   HOH B . 
SA 9 HOH   223 2323 1128 HOH   HOH B . 
SA 9 HOH   224 2324 1403 HOH   HOH B . 
SA 9 HOH   225 2325 804  HOH   HOH B . 
SA 9 HOH   226 2326 618  HOH   HOH B . 
SA 9 HOH   227 2327 661  HOH   HOH B . 
SA 9 HOH   228 2328 852  HOH   HOH B . 
SA 9 HOH   229 2329 349  HOH   HOH B . 
SA 9 HOH   230 2330 1636 HOH   HOH B . 
SA 9 HOH   231 2331 487  HOH   HOH B . 
SA 9 HOH   232 2332 626  HOH   HOH B . 
SA 9 HOH   233 2333 775  HOH   HOH B . 
SA 9 HOH   234 2334 96   HOH   HOH B . 
SA 9 HOH   235 2335 700  HOH   HOH B . 
SA 9 HOH   236 2336 1203 HOH   HOH B . 
SA 9 HOH   237 2337 1429 HOH   HOH B . 
SA 9 HOH   238 2338 1631 HOH   HOH B . 
SA 9 HOH   239 2339 1142 HOH   HOH B . 
SA 9 HOH   240 2340 755  HOH   HOH B . 
SA 9 HOH   241 2341 299  HOH   HOH B . 
SA 9 HOH   242 2342 153  HOH   HOH B . 
SA 9 HOH   243 2343 582  HOH   HOH B . 
SA 9 HOH   244 2344 1197 HOH   HOH B . 
SA 9 HOH   245 2345 1805 HOH   HOH B . 
SA 9 HOH   246 2346 47   HOH   HOH B . 
SA 9 HOH   247 2347 1000 HOH   HOH B . 
SA 9 HOH   248 2348 1634 HOH   HOH B . 
SA 9 HOH   249 2349 786  HOH   HOH B . 
SA 9 HOH   250 2350 264  HOH   HOH B . 
SA 9 HOH   251 2351 1693 HOH   HOH B . 
SA 9 HOH   252 2352 1701 HOH   HOH B . 
SA 9 HOH   253 2353 73   HOH   HOH B . 
SA 9 HOH   254 2354 138  HOH   HOH B . 
SA 9 HOH   255 2355 548  HOH   HOH B . 
SA 9 HOH   256 2356 1311 HOH   HOH B . 
SA 9 HOH   257 2357 1254 HOH   HOH B . 
SA 9 HOH   258 2358 40   HOH   HOH B . 
SA 9 HOH   259 2359 1545 HOH   HOH B . 
SA 9 HOH   260 2360 246  HOH   HOH B . 
SA 9 HOH   261 2361 224  HOH   HOH B . 
SA 9 HOH   262 2362 404  HOH   HOH B . 
SA 9 HOH   263 2363 346  HOH   HOH B . 
SA 9 HOH   264 2364 301  HOH   HOH B . 
SA 9 HOH   265 2365 931  HOH   HOH B . 
SA 9 HOH   266 2366 7    HOH   HOH B . 
SA 9 HOH   267 2367 792  HOH   HOH B . 
SA 9 HOH   268 2368 946  HOH   HOH B . 
SA 9 HOH   269 2369 1541 HOH   HOH B . 
SA 9 HOH   270 2370 1372 HOH   HOH B . 
SA 9 HOH   271 2371 261  HOH   HOH B . 
SA 9 HOH   272 2372 608  HOH   HOH B . 
SA 9 HOH   273 2373 319  HOH   HOH B . 
SA 9 HOH   274 2374 280  HOH   HOH B . 
SA 9 HOH   275 2375 25   HOH   HOH B . 
SA 9 HOH   276 2376 118  HOH   HOH B . 
SA 9 HOH   277 2377 932  HOH   HOH B . 
SA 9 HOH   278 2378 1457 HOH   HOH B . 
SA 9 HOH   279 2379 282  HOH   HOH B . 
SA 9 HOH   280 2380 144  HOH   HOH B . 
SA 9 HOH   281 2381 1857 HOH   HOH B . 
SA 9 HOH   282 2382 513  HOH   HOH B . 
SA 9 HOH   283 2383 333  HOH   HOH B . 
SA 9 HOH   284 2384 845  HOH   HOH B . 
SA 9 HOH   285 2385 217  HOH   HOH B . 
SA 9 HOH   286 2386 544  HOH   HOH B . 
SA 9 HOH   287 2387 583  HOH   HOH B . 
SA 9 HOH   288 2388 275  HOH   HOH B . 
SA 9 HOH   289 2389 228  HOH   HOH B . 
SA 9 HOH   290 2390 403  HOH   HOH B . 
SA 9 HOH   291 2391 878  HOH   HOH B . 
SA 9 HOH   292 2392 1456 HOH   HOH B . 
SA 9 HOH   293 2393 168  HOH   HOH B . 
SA 9 HOH   294 2394 412  HOH   HOH B . 
SA 9 HOH   295 2395 706  HOH   HOH B . 
SA 9 HOH   296 2396 120  HOH   HOH B . 
SA 9 HOH   297 2397 625  HOH   HOH B . 
SA 9 HOH   298 2398 1440 HOH   HOH B . 
SA 9 HOH   299 2399 252  HOH   HOH B . 
SA 9 HOH   300 2400 1081 HOH   HOH B . 
SA 9 HOH   301 2401 439  HOH   HOH B . 
SA 9 HOH   302 2402 1494 HOH   HOH B . 
SA 9 HOH   303 2403 849  HOH   HOH B . 
SA 9 HOH   304 2404 1915 HOH   HOH B . 
SA 9 HOH   305 2405 704  HOH   HOH B . 
SA 9 HOH   306 2406 468  HOH   HOH B . 
SA 9 HOH   307 2407 479  HOH   HOH B . 
SA 9 HOH   308 2408 167  HOH   HOH B . 
SA 9 HOH   309 2409 1322 HOH   HOH B . 
SA 9 HOH   310 2410 791  HOH   HOH B . 
SA 9 HOH   311 2411 23   HOH   HOH B . 
SA 9 HOH   312 2412 57   HOH   HOH B . 
SA 9 HOH   313 2413 941  HOH   HOH B . 
SA 9 HOH   314 2414 1869 HOH   HOH B . 
SA 9 HOH   315 2415 592  HOH   HOH B . 
SA 9 HOH   316 2416 764  HOH   HOH B . 
SA 9 HOH   317 2417 1831 HOH   HOH B . 
SA 9 HOH   318 2418 141  HOH   HOH B . 
SA 9 HOH   319 2419 1160 HOH   HOH B . 
SA 9 HOH   320 2420 757  HOH   HOH B . 
SA 9 HOH   321 2421 1153 HOH   HOH B . 
SA 9 HOH   322 2422 600  HOH   HOH B . 
SA 9 HOH   323 2423 944  HOH   HOH B . 
SA 9 HOH   324 2424 682  HOH   HOH B . 
SA 9 HOH   325 2425 934  HOH   HOH B . 
SA 9 HOH   326 2426 1570 HOH   HOH B . 
SA 9 HOH   327 2427 291  HOH   HOH B . 
SA 9 HOH   328 2428 154  HOH   HOH B . 
SA 9 HOH   329 2429 229  HOH   HOH B . 
SA 9 HOH   330 2430 5    HOH   HOH B . 
SA 9 HOH   331 2431 133  HOH   HOH B . 
SA 9 HOH   332 2432 868  HOH   HOH B . 
SA 9 HOH   333 2433 159  HOH   HOH B . 
SA 9 HOH   334 2434 1191 HOH   HOH B . 
SA 9 HOH   335 2435 850  HOH   HOH B . 
SA 9 HOH   336 2436 298  HOH   HOH B . 
SA 9 HOH   337 2437 1101 HOH   HOH B . 
SA 9 HOH   338 2438 814  HOH   HOH B . 
SA 9 HOH   339 2439 4    HOH   HOH B . 
SA 9 HOH   340 2440 740  HOH   HOH B . 
SA 9 HOH   341 2441 93   HOH   HOH B . 
SA 9 HOH   342 2442 646  HOH   HOH B . 
SA 9 HOH   343 2443 210  HOH   HOH B . 
SA 9 HOH   344 2444 769  HOH   HOH B . 
SA 9 HOH   345 2445 1490 HOH   HOH B . 
SA 9 HOH   346 2446 19   HOH   HOH B . 
SA 9 HOH   347 2447 1351 HOH   HOH B . 
SA 9 HOH   348 2448 527  HOH   HOH B . 
SA 9 HOH   349 2449 385  HOH   HOH B . 
SA 9 HOH   350 2450 1586 HOH   HOH B . 
SA 9 HOH   351 2451 329  HOH   HOH B . 
SA 9 HOH   352 2452 166  HOH   HOH B . 
SA 9 HOH   353 2453 3    HOH   HOH B . 
SA 9 HOH   354 2454 1170 HOH   HOH B . 
SA 9 HOH   355 2455 1430 HOH   HOH B . 
SA 9 HOH   356 2456 123  HOH   HOH B . 
SA 9 HOH   357 2457 1263 HOH   HOH B . 
SA 9 HOH   358 2458 738  HOH   HOH B . 
SA 9 HOH   359 2459 754  HOH   HOH B . 
SA 9 HOH   360 2460 1290 HOH   HOH B . 
SA 9 HOH   361 2461 1566 HOH   HOH B . 
SA 9 HOH   362 2462 386  HOH   HOH B . 
SA 9 HOH   363 2463 543  HOH   HOH B . 
SA 9 HOH   364 2464 200  HOH   HOH B . 
SA 9 HOH   365 2465 442  HOH   HOH B . 
SA 9 HOH   366 2466 256  HOH   HOH B . 
SA 9 HOH   367 2467 124  HOH   HOH B . 
SA 9 HOH   368 2468 262  HOH   HOH B . 
SA 9 HOH   369 2469 434  HOH   HOH B . 
SA 9 HOH   370 2470 1056 HOH   HOH B . 
SA 9 HOH   371 2471 300  HOH   HOH B . 
SA 9 HOH   372 2472 1395 HOH   HOH B . 
SA 9 HOH   373 2473 1810 HOH   HOH B . 
SA 9 HOH   374 2474 71   HOH   HOH B . 
SA 9 HOH   375 2475 22   HOH   HOH B . 
SA 9 HOH   376 2476 1135 HOH   HOH B . 
SA 9 HOH   377 2477 462  HOH   HOH B . 
SA 9 HOH   378 2478 268  HOH   HOH B . 
SA 9 HOH   379 2479 812  HOH   HOH B . 
SA 9 HOH   380 2480 1040 HOH   HOH B . 
SA 9 HOH   381 2481 1498 HOH   HOH B . 
SA 9 HOH   382 2482 961  HOH   HOH B . 
SA 9 HOH   383 2483 1300 HOH   HOH B . 
SA 9 HOH   384 2484 1789 HOH   HOH B . 
SA 9 HOH   385 2485 655  HOH   HOH B . 
SA 9 HOH   386 2486 554  HOH   HOH B . 
SA 9 HOH   387 2487 112  HOH   HOH B . 
SA 9 HOH   388 2488 146  HOH   HOH B . 
SA 9 HOH   389 2489 1122 HOH   HOH B . 
SA 9 HOH   390 2490 677  HOH   HOH B . 
SA 9 HOH   391 2491 530  HOH   HOH B . 
SA 9 HOH   392 2492 34   HOH   HOH B . 
SA 9 HOH   393 2493 542  HOH   HOH B . 
SA 9 HOH   394 2494 1850 HOH   HOH B . 
SA 9 HOH   395 2495 107  HOH   HOH B . 
SA 9 HOH   396 2496 408  HOH   HOH B . 
SA 9 HOH   397 2497 577  HOH   HOH B . 
SA 9 HOH   398 2498 161  HOH   HOH B . 
SA 9 HOH   399 2499 1033 HOH   HOH B . 
SA 9 HOH   400 2500 1030 HOH   HOH B . 
SA 9 HOH   401 2501 258  HOH   HOH B . 
SA 9 HOH   402 2502 546  HOH   HOH B . 
SA 9 HOH   403 2503 1599 HOH   HOH B . 
SA 9 HOH   404 2504 1620 HOH   HOH B . 
SA 9 HOH   405 2505 536  HOH   HOH B . 
SA 9 HOH   406 2506 134  HOH   HOH B . 
SA 9 HOH   407 2507 473  HOH   HOH B . 
SA 9 HOH   408 2508 688  HOH   HOH B . 
SA 9 HOH   409 2509 1553 HOH   HOH B . 
SA 9 HOH   410 2510 145  HOH   HOH B . 
SA 9 HOH   411 2511 1230 HOH   HOH B . 
SA 9 HOH   412 2512 495  HOH   HOH B . 
SA 9 HOH   413 2513 79   HOH   HOH B . 
SA 9 HOH   414 2514 443  HOH   HOH B . 
SA 9 HOH   415 2515 54   HOH   HOH B . 
SA 9 HOH   416 2516 836  HOH   HOH B . 
SA 9 HOH   417 2517 502  HOH   HOH B . 
SA 9 HOH   418 2518 186  HOH   HOH B . 
SA 9 HOH   419 2519 53   HOH   HOH B . 
SA 9 HOH   420 2520 586  HOH   HOH B . 
SA 9 HOH   421 2521 707  HOH   HOH B . 
SA 9 HOH   422 2522 106  HOH   HOH B . 
SA 9 HOH   423 2523 265  HOH   HOH B . 
SA 9 HOH   424 2524 174  HOH   HOH B . 
SA 9 HOH   425 2525 979  HOH   HOH B . 
SA 9 HOH   426 2526 65   HOH   HOH B . 
SA 9 HOH   427 2527 126  HOH   HOH B . 
SA 9 HOH   428 2528 1438 HOH   HOH B . 
SA 9 HOH   429 2529 457  HOH   HOH B . 
SA 9 HOH   430 2530 972  HOH   HOH B . 
SA 9 HOH   431 2531 710  HOH   HOH B . 
SA 9 HOH   432 2532 297  HOH   HOH B . 
SA 9 HOH   433 2533 770  HOH   HOH B . 
SA 9 HOH   434 2534 272  HOH   HOH B . 
SA 9 HOH   435 2535 223  HOH   HOH B . 
SA 9 HOH   436 2536 771  HOH   HOH B . 
SA 9 HOH   437 2537 97   HOH   HOH B . 
SA 9 HOH   438 2538 1518 HOH   HOH B . 
SA 9 HOH   439 2539 680  HOH   HOH B . 
SA 9 HOH   440 2540 1705 HOH   HOH B . 
SA 9 HOH   441 2541 52   HOH   HOH B . 
SA 9 HOH   442 2542 1077 HOH   HOH B . 
SA 9 HOH   443 2543 788  HOH   HOH B . 
SA 9 HOH   444 2544 459  HOH   HOH B . 
SA 9 HOH   445 2545 1431 HOH   HOH B . 
SA 9 HOH   446 2546 1071 HOH   HOH B . 
SA 9 HOH   447 2547 321  HOH   HOH B . 
SA 9 HOH   448 2548 1066 HOH   HOH B . 
SA 9 HOH   449 2549 843  HOH   HOH B . 
SA 9 HOH   450 2550 1116 HOH   HOH B . 
SA 9 HOH   451 2551 1078 HOH   HOH B . 
SA 9 HOH   452 2552 1053 HOH   HOH B . 
SA 9 HOH   453 2553 871  HOH   HOH B . 
SA 9 HOH   454 2554 392  HOH   HOH B . 
SA 9 HOH   455 2555 689  HOH   HOH B . 
SA 9 HOH   456 2556 576  HOH   HOH B . 
SA 9 HOH   457 2557 613  HOH   HOH B . 
SA 9 HOH   458 2558 1133 HOH   HOH B . 
SA 9 HOH   459 2559 595  HOH   HOH B . 
SA 9 HOH   460 2560 302  HOH   HOH B . 
SA 9 HOH   461 2561 160  HOH   HOH B . 
SA 9 HOH   462 2562 681  HOH   HOH B . 
SA 9 HOH   463 2563 1092 HOH   HOH B . 
SA 9 HOH   464 2564 884  HOH   HOH B . 
SA 9 HOH   465 2565 287  HOH   HOH B . 
SA 9 HOH   466 2566 367  HOH   HOH B . 
SA 9 HOH   467 2567 342  HOH   HOH B . 
SA 9 HOH   468 2568 653  HOH   HOH B . 
SA 9 HOH   469 2569 746  HOH   HOH B . 
SA 9 HOH   470 2570 1347 HOH   HOH B . 
SA 9 HOH   471 2571 185  HOH   HOH B . 
SA 9 HOH   472 2572 240  HOH   HOH B . 
SA 9 HOH   473 2573 1407 HOH   HOH B . 
SA 9 HOH   474 2574 373  HOH   HOH B . 
SA 9 HOH   475 2575 855  HOH   HOH B . 
SA 9 HOH   476 2576 86   HOH   HOH B . 
SA 9 HOH   477 2577 484  HOH   HOH B . 
SA 9 HOH   478 2578 807  HOH   HOH B . 
SA 9 HOH   479 2579 716  HOH   HOH B . 
SA 9 HOH   480 2580 358  HOH   HOH B . 
SA 9 HOH   481 2581 943  HOH   HOH B . 
SA 9 HOH   482 2582 211  HOH   HOH B . 
SA 9 HOH   483 2583 799  HOH   HOH B . 
SA 9 HOH   484 2584 1603 HOH   HOH B . 
SA 9 HOH   485 2585 559  HOH   HOH B . 
SA 9 HOH   486 2586 150  HOH   HOH B . 
SA 9 HOH   487 2587 426  HOH   HOH B . 
SA 9 HOH   488 2588 1075 HOH   HOH B . 
SA 9 HOH   489 2589 1016 HOH   HOH B . 
SA 9 HOH   490 2590 129  HOH   HOH B . 
SA 9 HOH   491 2591 1539 HOH   HOH B . 
SA 9 HOH   492 2592 384  HOH   HOH B . 
SA 9 HOH   493 2593 1143 HOH   HOH B . 
SA 9 HOH   494 2594 965  HOH   HOH B . 
SA 9 HOH   495 2595 797  HOH   HOH B . 
SA 9 HOH   496 2596 179  HOH   HOH B . 
SA 9 HOH   497 2597 500  HOH   HOH B . 
SA 9 HOH   498 2598 1721 HOH   HOH B . 
SA 9 HOH   499 2599 1577 HOH   HOH B . 
SA 9 HOH   500 2600 1702 HOH   HOH B . 
SA 9 HOH   501 2601 165  HOH   HOH B . 
SA 9 HOH   502 2602 470  HOH   HOH B . 
SA 9 HOH   503 2603 1157 HOH   HOH B . 
SA 9 HOH   504 2604 1903 HOH   HOH B . 
SA 9 HOH   505 2605 121  HOH   HOH B . 
SA 9 HOH   506 2606 1788 HOH   HOH B . 
SA 9 HOH   507 2607 1942 HOH   HOH B . 
SA 9 HOH   508 2608 730  HOH   HOH B . 
SA 9 HOH   509 2609 501  HOH   HOH B . 
SA 9 HOH   510 2610 1475 HOH   HOH B . 
SA 9 HOH   511 2611 1824 HOH   HOH B . 
SA 9 HOH   512 2612 957  HOH   HOH B . 
SA 9 HOH   513 2613 326  HOH   HOH B . 
SA 9 HOH   514 2614 780  HOH   HOH B . 
SA 9 HOH   515 2615 1657 HOH   HOH B . 
SA 9 HOH   516 2616 1409 HOH   HOH B . 
SA 9 HOH   517 2617 784  HOH   HOH B . 
SA 9 HOH   518 2618 142  HOH   HOH B . 
SA 9 HOH   519 2619 920  HOH   HOH B . 
SA 9 HOH   520 2620 1547 HOH   HOH B . 
SA 9 HOH   521 2621 29   HOH   HOH B . 
SA 9 HOH   522 2622 958  HOH   HOH B . 
SA 9 HOH   523 2623 1370 HOH   HOH B . 
SA 9 HOH   524 2624 1410 HOH   HOH B . 
SA 9 HOH   525 2625 1404 HOH   HOH B . 
SA 9 HOH   526 2626 1933 HOH   HOH B . 
SA 9 HOH   527 2627 1956 HOH   HOH B . 
SA 9 HOH   528 2628 742  HOH   HOH B . 
SA 9 HOH   529 2629 891  HOH   HOH B . 
SA 9 HOH   530 2630 162  HOH   HOH B . 
SA 9 HOH   531 2631 890  HOH   HOH B . 
SA 9 HOH   532 2632 198  HOH   HOH B . 
SA 9 HOH   533 2633 747  HOH   HOH B . 
SA 9 HOH   534 2634 1455 HOH   HOH B . 
SA 9 HOH   535 2635 1468 HOH   HOH B . 
SA 9 HOH   536 2636 215  HOH   HOH B . 
SA 9 HOH   537 2637 100  HOH   HOH B . 
SA 9 HOH   538 2638 802  HOH   HOH B . 
SA 9 HOH   539 2639 1399 HOH   HOH B . 
SA 9 HOH   540 2640 292  HOH   HOH B . 
SA 9 HOH   541 2641 702  HOH   HOH B . 
SA 9 HOH   542 2642 535  HOH   HOH B . 
SA 9 HOH   543 2643 1871 HOH   HOH B . 
SA 9 HOH   544 2644 1576 HOH   HOH B . 
SA 9 HOH   545 2645 117  HOH   HOH B . 
SA 9 HOH   546 2646 444  HOH   HOH B . 
SA 9 HOH   547 2647 1057 HOH   HOH B . 
SA 9 HOH   548 2648 926  HOH   HOH B . 
SA 9 HOH   549 2649 20   HOH   HOH B . 
SA 9 HOH   550 2650 1439 HOH   HOH B . 
SA 9 HOH   551 2651 665  HOH   HOH B . 
SA 9 HOH   552 2652 1443 HOH   HOH B . 
SA 9 HOH   553 2653 6    HOH   HOH B . 
SA 9 HOH   554 2654 942  HOH   HOH B . 
SA 9 HOH   555 2655 567  HOH   HOH B . 
SA 9 HOH   556 2656 294  HOH   HOH B . 
SA 9 HOH   557 2657 1401 HOH   HOH B . 
SA 9 HOH   558 2658 726  HOH   HOH B . 
SA 9 HOH   559 2659 1382 HOH   HOH B . 
SA 9 HOH   560 2660 888  HOH   HOH B . 
SA 9 HOH   561 2661 1126 HOH   HOH B . 
SA 9 HOH   562 2662 1836 HOH   HOH B . 
SA 9 HOH   563 2663 1414 HOH   HOH B . 
SA 9 HOH   564 2664 1131 HOH   HOH B . 
SA 9 HOH   565 2665 806  HOH   HOH B . 
SA 9 HOH   566 2666 1503 HOH   HOH B . 
SA 9 HOH   567 2667 374  HOH   HOH B . 
SA 9 HOH   568 2668 1065 HOH   HOH B . 
SA 9 HOH   569 2669 114  HOH   HOH B . 
SA 9 HOH   570 2670 556  HOH   HOH B . 
SA 9 HOH   571 2671 669  HOH   HOH B . 
SA 9 HOH   572 2672 428  HOH   HOH B . 
SA 9 HOH   573 2673 1827 HOH   HOH B . 
SA 9 HOH   574 2674 589  HOH   HOH B . 
SA 9 HOH   575 2675 1062 HOH   HOH B . 
SA 9 HOH   576 2676 1674 HOH   HOH B . 
SA 9 HOH   577 2677 935  HOH   HOH B . 
SA 9 HOH   578 2678 423  HOH   HOH B . 
SA 9 HOH   579 2679 1595 HOH   HOH B . 
SA 9 HOH   580 2680 1815 HOH   HOH B . 
SA 9 HOH   581 2681 1186 HOH   HOH B . 
SA 9 HOH   582 2682 1910 HOH   HOH B . 
SA 9 HOH   583 2683 1583 HOH   HOH B . 
SA 9 HOH   584 2684 1265 HOH   HOH B . 
SA 9 HOH   585 2685 458  HOH   HOH B . 
SA 9 HOH   586 2686 1381 HOH   HOH B . 
SA 9 HOH   587 2687 219  HOH   HOH B . 
SA 9 HOH   588 2688 1817 HOH   HOH B . 
SA 9 HOH   589 2689 1048 HOH   HOH B . 
SA 9 HOH   590 2690 671  HOH   HOH B . 
SA 9 HOH   591 2691 1554 HOH   HOH B . 
SA 9 HOH   592 2692 1932 HOH   HOH B . 
SA 9 HOH   593 2693 1427 HOH   HOH B . 
SA 9 HOH   594 2694 91   HOH   HOH B . 
SA 9 HOH   595 2695 481  HOH   HOH B . 
SA 9 HOH   596 2696 1402 HOH   HOH B . 
SA 9 HOH   597 2697 604  HOH   HOH B . 
SA 9 HOH   598 2698 1478 HOH   HOH B . 
SA 9 HOH   599 2699 531  HOH   HOH B . 
SA 9 HOH   600 2700 1907 HOH   HOH B . 
SA 9 HOH   601 2701 1244 HOH   HOH B . 
SA 9 HOH   602 2702 1578 HOH   HOH B . 
SA 9 HOH   603 2703 1279 HOH   HOH B . 
SA 9 HOH   604 2704 1462 HOH   HOH B . 
SA 9 HOH   605 2705 175  HOH   HOH B . 
SA 9 HOH   606 2706 1875 HOH   HOH B . 
SA 9 HOH   607 2707 1117 HOH   HOH B . 
SA 9 HOH   608 2708 1739 HOH   HOH B . 
SA 9 HOH   609 2709 875  HOH   HOH B . 
SA 9 HOH   610 2710 762  HOH   HOH B . 
SA 9 HOH   611 2711 960  HOH   HOH B . 
SA 9 HOH   612 2712 512  HOH   HOH B . 
SA 9 HOH   613 2713 652  HOH   HOH B . 
SA 9 HOH   614 2714 1130 HOH   HOH B . 
SA 9 HOH   615 2715 1476 HOH   HOH B . 
SA 9 HOH   616 2716 1648 HOH   HOH B . 
SA 9 HOH   617 2717 1860 HOH   HOH B . 
SA 9 HOH   618 2718 461  HOH   HOH B . 
SA 9 HOH   619 2719 1107 HOH   HOH B . 
SA 9 HOH   620 2720 1719 HOH   HOH B . 
SA 9 HOH   621 2721 451  HOH   HOH B . 
SA 9 HOH   622 2722 1444 HOH   HOH B . 
SA 9 HOH   623 2723 1679 HOH   HOH B . 
SA 9 HOH   624 2724 427  HOH   HOH B . 
SA 9 HOH   625 2725 1711 HOH   HOH B . 
SA 9 HOH   626 2726 1838 HOH   HOH B . 
SA 9 HOH   627 2727 1398 HOH   HOH B . 
SA 9 HOH   628 2728 1038 HOH   HOH B . 
SA 9 HOH   629 2729 1559 HOH   HOH B . 
SA 9 HOH   630 2730 1954 HOH   HOH B . 
SA 9 HOH   631 2731 1458 HOH   HOH B . 
SA 9 HOH   632 2732 1923 HOH   HOH B . 
SA 9 HOH   633 2733 1419 HOH   HOH B . 
SA 9 HOH   634 2734 1287 HOH   HOH B . 
SA 9 HOH   635 2735 552  HOH   HOH B . 
SA 9 HOH   636 2736 1660 HOH   HOH B . 
SA 9 HOH   637 2737 1713 HOH   HOH B . 
SA 9 HOH   638 2738 1633 HOH   HOH B . 
SA 9 HOH   639 2739 1418 HOH   HOH B . 
SA 9 HOH   640 2740 1474 HOH   HOH B . 
SA 9 HOH   641 2741 986  HOH   HOH B . 
SA 9 HOH   642 2742 1812 HOH   HOH B . 
SA 9 HOH   643 2743 1802 HOH   HOH B . 
SA 9 HOH   644 2744 881  HOH   HOH B . 
SA 9 HOH   645 2745 1039 HOH   HOH B . 
SA 9 HOH   646 2746 1508 HOH   HOH B . 
SA 9 HOH   647 2747 1446 HOH   HOH B . 
SA 9 HOH   648 2748 781  HOH   HOH B . 
SA 9 HOH   649 2749 1604 HOH   HOH B . 
SA 9 HOH   650 2750 1621 HOH   HOH B . 
SA 9 HOH   651 2751 1863 HOH   HOH B . 
SA 9 HOH   652 2752 1741 HOH   HOH B . 
SA 9 HOH   653 2753 951  HOH   HOH B . 
SA 9 HOH   654 2754 1108 HOH   HOH B . 
SA 9 HOH   655 2755 1676 HOH   HOH B . 
SA 9 HOH   656 2756 1371 HOH   HOH B . 
SA 9 HOH   657 2757 1293 HOH   HOH B . 
SA 9 HOH   658 2758 1917 HOH   HOH B . 
SA 9 HOH   659 2759 902  HOH   HOH B . 
SA 9 HOH   660 2760 1731 HOH   HOH B . 
SA 9 HOH   661 2761 1811 HOH   HOH B . 
SA 9 HOH   662 2762 1471 HOH   HOH B . 
SA 9 HOH   663 2763 752  HOH   HOH B . 
SA 9 HOH   664 2764 1605 HOH   HOH B . 
SA 9 HOH   665 2765 1305 HOH   HOH B . 
SA 9 HOH   666 2766 1046 HOH   HOH B . 
SA 9 HOH   667 2767 1123 HOH   HOH B . 
SA 9 HOH   668 2768 1240 HOH   HOH B . 
SA 9 HOH   669 2769 1484 HOH   HOH B . 
SA 9 HOH   670 2770 1920 HOH   HOH B . 
SA 9 HOH   671 2771 1658 HOH   HOH B . 
SA 9 HOH   672 2772 492  HOH   HOH B . 
SA 9 HOH   673 2773 1587 HOH   HOH B . 
SA 9 HOH   674 2774 1842 HOH   HOH B . 
SA 9 HOH   675 2775 1029 HOH   HOH B . 
SA 9 HOH   676 2776 1136 HOH   HOH B . 
SA 9 HOH   677 2777 1888 HOH   HOH B . 
SA 9 HOH   678 2778 1963 HOH   HOH B . 
SA 9 HOH   679 2779 820  HOH   HOH B . 
SA 9 HOH   680 2780 1379 HOH   HOH B . 
SA 9 HOH   681 2781 1891 HOH   HOH B . 
SA 9 HOH   682 2782 1206 HOH   HOH B . 
SA 9 HOH   683 2783 840  HOH   HOH B . 
SA 9 HOH   684 2784 1813 HOH   HOH B . 
SA 9 HOH   685 2785 1874 HOH   HOH B . 
SA 9 HOH   686 2786 1680 HOH   HOH B . 
SA 9 HOH   687 2787 1643 HOH   HOH B . 
SA 9 HOH   688 2788 1880 HOH   HOH B . 
SA 9 HOH   689 2789 621  HOH   HOH B . 
SA 9 HOH   690 2790 1415 HOH   HOH B . 
SA 9 HOH   691 2791 1953 HOH   HOH B . 
SA 9 HOH   692 2792 1188 HOH   HOH B . 
SA 9 HOH   693 2793 629  HOH   HOH B . 
SA 9 HOH   694 2794 401  HOH   HOH B . 
SA 9 HOH   695 2795 1119 HOH   HOH B . 
SA 9 HOH   696 2796 1921 HOH   HOH B . 
SA 9 HOH   697 2797 743  HOH   HOH B . 
SA 9 HOH   698 2798 928  HOH   HOH B . 
SA 9 HOH   699 2799 1664 HOH   HOH B . 
SA 9 HOH   700 2800 1145 HOH   HOH B . 
SA 9 HOH   701 2801 1242 HOH   HOH B . 
SA 9 HOH   702 2802 1127 HOH   HOH B . 
SA 9 HOH   703 2803 1855 HOH   HOH B . 
SA 9 HOH   704 2804 956  HOH   HOH B . 
SA 9 HOH   705 2805 924  HOH   HOH B . 
SA 9 HOH   706 2806 1795 HOH   HOH B . 
SA 9 HOH   707 2807 1001 HOH   HOH B . 
SA 9 HOH   708 2808 1793 HOH   HOH B . 
SA 9 HOH   709 2809 1517 HOH   HOH B . 
SA 9 HOH   710 2810 1753 HOH   HOH B . 
SA 9 HOH   711 2811 1176 HOH   HOH B . 
SA 9 HOH   712 2812 1966 HOH   HOH B . 
SA 9 HOH   713 2813 1890 HOH   HOH B . 
SA 9 HOH   714 2814 354  HOH   HOH B . 
SA 9 HOH   715 2815 1115 HOH   HOH B . 
SA 9 HOH   716 2816 1314 HOH   HOH B . 
SA 9 HOH   717 2817 1955 HOH   HOH B . 
SA 9 HOH   718 2818 638  HOH   HOH B . 
SA 9 HOH   719 2819 1846 HOH   HOH B . 
SA 9 HOH   720 2820 977  HOH   HOH B . 
SA 9 HOH   721 2821 1316 HOH   HOH B . 
SA 9 HOH   722 2822 1366 HOH   HOH B . 
SA 9 HOH   723 2823 798  HOH   HOH B . 
SA 9 HOH   724 2824 823  HOH   HOH B . 
SA 9 HOH   725 2825 1706 HOH   HOH B . 
SA 9 HOH   726 2826 1449 HOH   HOH B . 
SA 9 HOH   727 2827 1792 HOH   HOH B . 
SA 9 HOH   728 2828 1911 HOH   HOH B . 
SA 9 HOH   729 2829 545  HOH   HOH B . 
SA 9 HOH   730 2830 1210 HOH   HOH B . 
SA 9 HOH   731 2831 995  HOH   HOH B . 
SA 9 HOH   732 2832 1600 HOH   HOH B . 
SA 9 HOH   733 2833 1614 HOH   HOH B . 
SA 9 HOH   734 2834 569  HOH   HOH B . 
SA 9 HOH   735 2835 1132 HOH   HOH B . 
SA 9 HOH   736 2836 1239 HOH   HOH B . 
SA 9 HOH   737 2837 1072 HOH   HOH B . 
SA 9 HOH   738 2838 1285 HOH   HOH B . 
SA 9 HOH   739 2839 1652 HOH   HOH B . 
SA 9 HOH   740 2840 1565 HOH   HOH B . 
SA 9 HOH   741 2841 954  HOH   HOH B . 
SA 9 HOH   742 2842 1646 HOH   HOH B . 
SA 9 HOH   743 2843 1596 HOH   HOH B . 
SA 9 HOH   744 2844 478  HOH   HOH B . 
SA 9 HOH   745 2845 1809 HOH   HOH B . 
SA 9 HOH   746 2846 1487 HOH   HOH B . 
SA 9 HOH   747 2847 1227 HOH   HOH B . 
SA 9 HOH   748 2848 1589 HOH   HOH B . 
SA 9 HOH   749 2849 748  HOH   HOH B . 
SA 9 HOH   750 2850 1965 HOH   HOH B . 
SA 9 HOH   751 2851 453  HOH   HOH B . 
SA 9 HOH   752 2852 759  HOH   HOH B . 
SA 9 HOH   753 2853 1833 HOH   HOH B . 
SA 9 HOH   754 2854 1221 HOH   HOH B . 
SA 9 HOH   755 2855 1967 HOH   HOH B . 
SA 9 HOH   756 2856 1957 HOH   HOH B . 
SA 9 HOH   757 2857 968  HOH   HOH B . 
SA 9 HOH   758 2858 1447 HOH   HOH B . 
SA 9 HOH   759 2859 1264 HOH   HOH B . 
SA 9 HOH   760 2860 1343 HOH   HOH B . 
SA 9 HOH   761 2861 1597 HOH   HOH B . 
SA 9 HOH   762 2862 1333 HOH   HOH B . 
SA 9 HOH   763 2863 517  HOH   HOH B . 
SA 9 HOH   764 2864 1259 HOH   HOH B . 
SA 9 HOH   765 2865 1354 HOH   HOH B . 
SA 9 HOH   766 2866 1353 HOH   HOH B . 
SA 9 HOH   767 2867 1794 HOH   HOH B . 
SA 9 HOH   768 2868 1761 HOH   HOH B . 
SA 9 HOH   769 2869 1054 HOH   HOH B . 
SA 9 HOH   770 2870 1010 HOH   HOH B . 
SA 9 HOH   771 2871 1045 HOH   HOH B . 
SA 9 HOH   772 2872 1146 HOH   HOH B . 
SA 9 HOH   773 2873 1226 HOH   HOH B . 
SA 9 HOH   774 2874 1199 HOH   HOH B . 
SA 9 HOH   775 2875 835  HOH   HOH B . 
SA 9 HOH   776 2876 1275 HOH   HOH B . 
SA 9 HOH   777 2877 1162 HOH   HOH B . 
SA 9 HOH   778 2878 627  HOH   HOH B . 
SA 9 HOH   779 2879 1273 HOH   HOH B . 
SA 9 HOH   780 2880 1950 HOH   HOH B . 
SA 9 HOH   781 2881 1769 HOH   HOH B . 
SA 9 HOH   782 2882 620  HOH   HOH B . 
SA 9 HOH   783 2883 1420 HOH   HOH B . 
SA 9 HOH   784 2884 830  HOH   HOH B . 
SA 9 HOH   785 2885 1744 HOH   HOH B . 
SA 9 HOH   786 2886 1268 HOH   HOH B . 
SA 9 HOH   787 2887 1218 HOH   HOH B . 
SA 9 HOH   788 2888 1585 HOH   HOH B . 
SA 9 HOH   789 2889 429  HOH   HOH B . 
SA 9 HOH   790 2890 808  HOH   HOH B . 
SA 9 HOH   791 2891 1406 HOH   HOH B . 
SA 9 HOH   792 2892 1962 HOH   HOH B . 
SA 9 HOH   793 2893 1499 HOH   HOH B . 
SA 9 HOH   794 2894 984  HOH   HOH B . 
SA 9 HOH   795 2895 1778 HOH   HOH B . 
SA 9 HOH   796 2896 1695 HOH   HOH B . 
SA 9 HOH   797 2897 1224 HOH   HOH B . 
SA 9 HOH   798 2898 1650 HOH   HOH B . 
SA 9 HOH   799 2899 929  HOH   HOH B . 
SA 9 HOH   800 2900 1109 HOH   HOH B . 
SA 9 HOH   801 2901 1236 HOH   HOH B . 
SA 9 HOH   802 2902 664  HOH   HOH B . 
SA 9 HOH   803 2903 644  HOH   HOH B . 
SA 9 HOH   804 2904 1546 HOH   HOH B . 
SA 9 HOH   805 2905 1726 HOH   HOH B . 
SA 9 HOH   806 2906 1349 HOH   HOH B . 
SA 9 HOH   807 2907 801  HOH   HOH B . 
SA 9 HOH   808 2908 1516 HOH   HOH B . 
SA 9 HOH   809 2909 1947 HOH   HOH B . 
SA 9 HOH   810 2910 1274 HOH   HOH B . 
SA 9 HOH   811 2911 1489 HOH   HOH B . 
SA 9 HOH   812 2912 658  HOH   HOH B . 
SA 9 HOH   813 2913 1610 HOH   HOH B . 
SA 9 HOH   814 2914 1852 HOH   HOH B . 
SA 9 HOH   815 2915 1641 HOH   HOH B . 
SA 9 HOH   816 2916 1232 HOH   HOH B . 
SA 9 HOH   817 2917 909  HOH   HOH B . 
SA 9 HOH   818 2918 1948 HOH   HOH B . 
SA 9 HOH   819 2919 989  HOH   HOH B . 
SA 9 HOH   820 2920 1567 HOH   HOH B . 
SA 9 HOH   821 2921 1870 HOH   HOH B . 
SA 9 HOH   822 2922 1272 HOH   HOH B . 
SA 9 HOH   823 2923 1520 HOH   HOH B . 
SA 9 HOH   824 2924 318  HOH   HOH B . 
SA 9 HOH   825 2925 1412 HOH   HOH B . 
SA 9 HOH   826 2926 1900 HOH   HOH B . 
SA 9 HOH   827 2927 1734 HOH   HOH B . 
SA 9 HOH   828 2928 905  HOH   HOH B . 
SA 9 HOH   829 2929 1889 HOH   HOH B . 
SA 9 HOH   830 2930 1841 HOH   HOH B . 
SA 9 HOH   831 2931 1717 HOH   HOH B . 
SA 9 HOH   832 2932 1619 HOH   HOH B . 
SA 9 HOH   833 2933 724  HOH   HOH B . 
SA 9 HOH   834 2934 1760 HOH   HOH B . 
SA 9 HOH   835 2935 1901 HOH   HOH B . 
SA 9 HOH   836 2936 1612 HOH   HOH B . 
SA 9 HOH   837 2937 663  HOH   HOH B . 
SA 9 HOH   838 2938 1851 HOH   HOH B . 
SA 9 HOH   839 2939 1783 HOH   HOH B . 
SA 9 HOH   840 2940 1453 HOH   HOH B . 
SA 9 HOH   841 2941 1665 HOH   HOH B . 
SA 9 HOH   842 2942 1192 HOH   HOH B . 
SA 9 HOH   843 2943 1017 HOH   HOH B . 
SA 9 HOH   844 2944 975  HOH   HOH B . 
SA 9 HOH   845 2945 1611 HOH   HOH B . 
SA 9 HOH   846 2946 817  HOH   HOH B . 
SA 9 HOH   847 2947 1618 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 GLU 52   ? CG  ? A GLU 54   CG  
2   1 Y 1 A GLU 52   ? CD  ? A GLU 54   CD  
3   1 Y 1 A GLU 52   ? OE1 ? A GLU 54   OE1 
4   1 Y 1 A GLU 52   ? OE2 ? A GLU 54   OE2 
5   1 Y 1 A LYS 58   ? CG  ? A LYS 60   CG  
6   1 Y 1 A LYS 58   ? CD  ? A LYS 60   CD  
7   1 Y 1 A LYS 58   ? CE  ? A LYS 60   CE  
8   1 Y 1 A LYS 58   ? NZ  ? A LYS 60   NZ  
9   1 Y 1 A GLU 59   ? CG  ? A GLU 61   CG  
10  1 Y 1 A GLU 59   ? CD  ? A GLU 61   CD  
11  1 Y 1 A GLU 59   ? OE1 ? A GLU 61   OE1 
12  1 Y 1 A GLU 59   ? OE2 ? A GLU 61   OE2 
13  1 Y 1 A LYS 70   ? CG  ? A LYS 72   CG  
14  1 Y 1 A LYS 70   ? CD  ? A LYS 72   CD  
15  1 Y 1 A LYS 70   ? CE  ? A LYS 72   CE  
16  1 Y 1 A LYS 70   ? NZ  ? A LYS 72   NZ  
17  1 Y 1 A VAL 84   ? CG1 ? A VAL 86   CG1 
18  1 Y 1 A VAL 84   ? CG2 ? A VAL 86   CG2 
19  1 Y 1 A GLU 85   ? CG  ? A GLU 87   CG  
20  1 Y 1 A GLU 85   ? CD  ? A GLU 87   CD  
21  1 Y 1 A GLU 85   ? OE1 ? A GLU 87   OE1 
22  1 Y 1 A GLU 85   ? OE2 ? A GLU 87   OE2 
23  1 Y 1 A GLN 89   ? CG  ? A GLN 91   CG  
24  1 Y 1 A GLN 89   ? CD  ? A GLN 91   CD  
25  1 Y 1 A GLN 89   ? OE1 ? A GLN 91   OE1 
26  1 Y 1 A GLN 89   ? NE2 ? A GLN 91   NE2 
27  1 Y 1 A ASP 113  ? CG  ? A ASP 115  CG  
28  1 Y 1 A ASP 113  ? OD1 ? A ASP 115  OD1 
29  1 Y 1 A ASP 113  ? OD2 ? A ASP 115  OD2 
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 HIS 133  ? CG  ? A HIS 135  CG  
52  1 Y 1 A HIS 133  ? ND1 ? A HIS 135  ND1 
53  1 Y 1 A HIS 133  ? CD2 ? A HIS 135  CD2 
54  1 Y 1 A HIS 133  ? CE1 ? A HIS 135  CE1 
55  1 Y 1 A HIS 133  ? NE2 ? A HIS 135  NE2 
56  1 Y 1 A ARG 138  ? CG  ? A ARG 140  CG  
57  1 Y 1 A ARG 138  ? CD  ? A ARG 140  CD  
58  1 Y 1 A ARG 138  ? NE  ? A ARG 140  NE  
59  1 Y 1 A ARG 138  ? CZ  ? A ARG 140  CZ  
60  1 Y 1 A ARG 138  ? NH1 ? A ARG 140  NH1 
61  1 Y 1 A ARG 138  ? NH2 ? A ARG 140  NH2 
62  1 Y 1 A LYS 154  ? CG  ? A LYS 156  CG  
63  1 Y 1 A LYS 154  ? CD  ? A LYS 156  CD  
64  1 Y 1 A LYS 154  ? CE  ? A LYS 156  CE  
65  1 Y 1 A LYS 154  ? NZ  ? A LYS 156  NZ  
66  1 Y 1 A ARG 181  ? CG  ? A ARG 183  CG  
67  1 Y 1 A ARG 181  ? CD  ? A ARG 183  CD  
68  1 Y 1 A ARG 181  ? NE  ? A ARG 183  NE  
69  1 Y 1 A ARG 181  ? CZ  ? A ARG 183  CZ  
70  1 Y 1 A ARG 181  ? NH1 ? A ARG 183  NH1 
71  1 Y 1 A ARG 181  ? NH2 ? A ARG 183  NH2 
72  1 Y 1 A ARG 189  ? CG  ? A ARG 191  CG  
73  1 Y 1 A ARG 189  ? CD  ? A ARG 191  CD  
74  1 Y 1 A ARG 189  ? NE  ? A ARG 191  NE  
75  1 Y 1 A ARG 189  ? CZ  ? A ARG 191  CZ  
76  1 Y 1 A ARG 189  ? NH1 ? A ARG 191  NH1 
77  1 Y 1 A ARG 189  ? NH2 ? A ARG 191  NH2 
78  1 Y 1 A GLN 194  ? CG  ? A GLN 196  CG  
79  1 Y 1 A GLN 194  ? CD  ? A GLN 196  CD  
80  1 Y 1 A GLN 194  ? OE1 ? A GLN 196  OE1 
81  1 Y 1 A GLN 194  ? NE2 ? A GLN 196  NE2 
82  1 Y 1 A ARG 202  ? CG  ? A ARG 204  CG  
83  1 Y 1 A ARG 202  ? CD  ? A ARG 204  CD  
84  1 Y 1 A ARG 202  ? NE  ? A ARG 204  NE  
85  1 Y 1 A ARG 202  ? CZ  ? A ARG 204  CZ  
86  1 Y 1 A ARG 202  ? NH1 ? A ARG 204  NH1 
87  1 Y 1 A ARG 202  ? NH2 ? A ARG 204  NH2 
88  1 Y 1 A LYS 206  ? CG  ? A LYS 208  CG  
89  1 Y 1 A LYS 206  ? CD  ? A LYS 208  CD  
90  1 Y 1 A LYS 206  ? CE  ? A LYS 208  CE  
91  1 Y 1 A LYS 206  ? NZ  ? A LYS 208  NZ  
92  1 Y 1 A LYS 209  ? CG  ? A LYS 211  CG  
93  1 Y 1 A LYS 209  ? CD  ? A LYS 211  CD  
94  1 Y 1 A LYS 209  ? CE  ? A LYS 211  CE  
95  1 Y 1 A LYS 209  ? NZ  ? A LYS 211  NZ  
96  1 Y 1 A GLU 213  ? CG  ? A GLU 215  CG  
97  1 Y 1 A GLU 213  ? CD  ? A GLU 215  CD  
98  1 Y 1 A GLU 213  ? OE1 ? A GLU 215  OE1 
99  1 Y 1 A GLU 213  ? OE2 ? A GLU 215  OE2 
100 1 Y 1 A LYS 214  ? CG  ? A LYS 216  CG  
101 1 Y 1 A LYS 214  ? CD  ? A LYS 216  CD  
102 1 Y 1 A LYS 214  ? CE  ? A LYS 216  CE  
103 1 Y 1 A LYS 214  ? NZ  ? A LYS 216  NZ  
104 1 Y 1 A GLU 258  ? CG  ? A GLU 260  CG  
105 1 Y 1 A GLU 258  ? CD  ? A GLU 260  CD  
106 1 Y 1 A GLU 258  ? OE1 ? A GLU 260  OE1 
107 1 Y 1 A GLU 258  ? OE2 ? A GLU 260  OE2 
108 1 Y 1 A LEU 295  ? CG  ? A LEU 297  CG  
109 1 Y 1 A LEU 295  ? CD1 ? A LEU 297  CD1 
110 1 Y 1 A LEU 295  ? CD2 ? A LEU 297  CD2 
111 1 Y 1 A LYS 437  ? CG  ? A LYS 439  CG  
112 1 Y 1 A LYS 437  ? CD  ? A LYS 439  CD  
113 1 Y 1 A LYS 437  ? CE  ? A LYS 439  CE  
114 1 Y 1 A LYS 437  ? NZ  ? A LYS 439  NZ  
115 1 Y 1 A GLU 458  ? CG  ? A GLU 460  CG  
116 1 Y 1 A GLU 458  ? CD  ? A GLU 460  CD  
117 1 Y 1 A GLU 458  ? OE1 ? A GLU 460  OE1 
118 1 Y 1 A GLU 458  ? OE2 ? A GLU 460  OE2 
119 1 Y 1 A ARG 463  ? CG  ? A ARG 465  CG  
120 1 Y 1 A ARG 463  ? CD  ? A ARG 465  CD  
121 1 Y 1 A ARG 463  ? NE  ? A ARG 465  NE  
122 1 Y 1 A ARG 463  ? CZ  ? A ARG 465  CZ  
123 1 Y 1 A ARG 463  ? NH1 ? A ARG 465  NH1 
124 1 Y 1 A ARG 463  ? NH2 ? A ARG 465  NH2 
125 1 Y 1 A ASN 496  ? CG  ? A ASN 498  CG  
126 1 Y 1 A ASN 496  ? OD1 ? A ASN 498  OD1 
127 1 Y 1 A ASN 496  ? ND2 ? A ASN 498  ND2 
128 1 Y 1 A VAL 500  ? CG1 ? A VAL 502  CG1 
129 1 Y 1 A VAL 500  ? CG2 ? A VAL 502  CG2 
130 1 Y 1 A LYS 507  ? CG  ? A LYS 509  CG  
131 1 Y 1 A LYS 507  ? CD  ? A LYS 509  CD  
132 1 Y 1 A LYS 507  ? CE  ? A LYS 509  CE  
133 1 Y 1 A LYS 507  ? NZ  ? A LYS 509  NZ  
134 1 Y 1 A ARG 533  ? CG  ? A ARG 535  CG  
135 1 Y 1 A ARG 533  ? CD  ? A ARG 535  CD  
136 1 Y 1 A ARG 533  ? NE  ? A ARG 535  NE  
137 1 Y 1 A ARG 533  ? CZ  ? A ARG 535  CZ  
138 1 Y 1 A ARG 533  ? NH1 ? A ARG 535  NH1 
139 1 Y 1 A ARG 533  ? NH2 ? A ARG 535  NH2 
140 1 Y 1 A GLU 564  ? CG  ? A GLU 566  CG  
141 1 Y 1 A GLU 564  ? CD  ? A GLU 566  CD  
142 1 Y 1 A GLU 564  ? OE1 ? A GLU 566  OE1 
143 1 Y 1 A GLU 564  ? OE2 ? A GLU 566  OE2 
144 1 Y 1 A LYS 573  ? CG  ? A LYS 575  CG  
145 1 Y 1 A LYS 573  ? CD  ? A LYS 575  CD  
146 1 Y 1 A LYS 573  ? CE  ? A LYS 575  CE  
147 1 Y 1 A LYS 573  ? NZ  ? A LYS 575  NZ  
148 1 Y 1 A GLU 588  ? CG  ? A GLU 590  CG  
149 1 Y 1 A GLU 588  ? CD  ? A GLU 590  CD  
150 1 Y 1 A GLU 588  ? OE1 ? A GLU 590  OE1 
151 1 Y 1 A GLU 588  ? OE2 ? A GLU 590  OE2 
152 1 Y 1 A GLU 610  ? CG  ? A GLU 612  CG  
153 1 Y 1 A GLU 610  ? CD  ? A GLU 612  CD  
154 1 Y 1 A GLU 610  ? OE1 ? A GLU 612  OE1 
155 1 Y 1 A GLU 610  ? OE2 ? A GLU 612  OE2 
156 1 Y 1 A GLU 611  ? CG  ? A GLU 613  CG  
157 1 Y 1 A GLU 611  ? CD  ? A GLU 613  CD  
158 1 Y 1 A GLU 611  ? OE1 ? A GLU 613  OE1 
159 1 Y 1 A GLU 611  ? OE2 ? A GLU 613  OE2 
160 1 Y 1 A GLU 634  ? CG  ? A GLU 636  CG  
161 1 Y 1 A GLU 634  ? CD  ? A GLU 636  CD  
162 1 Y 1 A GLU 634  ? OE1 ? A GLU 636  OE1 
163 1 Y 1 A GLU 634  ? OE2 ? A GLU 636  OE2 
164 1 Y 1 A ARG 764  ? CG  ? A ARG 766  CG  
165 1 Y 1 A ARG 764  ? CD  ? A ARG 766  CD  
166 1 Y 1 A ARG 764  ? NE  ? A ARG 766  NE  
167 1 Y 1 A ARG 764  ? CZ  ? A ARG 766  CZ  
168 1 Y 1 A ARG 764  ? NH1 ? A ARG 766  NH1 
169 1 Y 1 A ARG 764  ? NH2 ? A ARG 766  NH2 
170 1 Y 1 A ASP 796  ? CG  ? A ASP 798  CG  
171 1 Y 1 A ASP 796  ? OD1 ? A ASP 798  OD1 
172 1 Y 1 A ASP 796  ? OD2 ? A ASP 798  OD2 
173 1 Y 1 A GLN 827  ? CG  ? A GLN 829  CG  
174 1 Y 1 A GLN 827  ? CD  ? A GLN 829  CD  
175 1 Y 1 A GLN 827  ? OE1 ? A GLN 829  OE1 
176 1 Y 1 A GLN 827  ? NE2 ? A GLN 829  NE2 
177 1 Y 1 A ASP 855  ? CG  ? A ASP 857  CG  
178 1 Y 1 A ASP 855  ? OD1 ? A ASP 857  OD1 
179 1 Y 1 A ASP 855  ? OD2 ? A ASP 857  OD2 
180 1 Y 1 A LYS 897  ? CG  ? A LYS 899  CG  
181 1 Y 1 A LYS 897  ? CD  ? A LYS 899  CD  
182 1 Y 1 A LYS 897  ? CE  ? A LYS 899  CE  
183 1 Y 1 A LYS 897  ? NZ  ? A LYS 899  NZ  
184 1 Y 1 A ARG 901  ? CG  ? A ARG 903  CG  
185 1 Y 1 A ARG 901  ? CD  ? A ARG 903  CD  
186 1 Y 1 A ARG 901  ? NE  ? A ARG 903  NE  
187 1 Y 1 A ARG 901  ? CZ  ? A ARG 903  CZ  
188 1 Y 1 A ARG 901  ? NH1 ? A ARG 903  NH1 
189 1 Y 1 A ARG 901  ? NH2 ? A ARG 903  NH2 
190 1 Y 1 A ILE 912  ? CG1 ? A ILE 914  CG1 
191 1 Y 1 A ILE 912  ? CG2 ? A ILE 914  CG2 
192 1 Y 1 A ILE 912  ? CD1 ? A ILE 914  CD1 
193 1 Y 1 A LYS 933  ? CG  ? A LYS 935  CG  
194 1 Y 1 A LYS 933  ? CD  ? A LYS 935  CD  
195 1 Y 1 A LYS 933  ? CE  ? A LYS 935  CE  
196 1 Y 1 A LYS 933  ? NZ  ? A LYS 935  NZ  
197 1 Y 1 A LEU 934  ? CG  ? A LEU 936  CG  
198 1 Y 1 A LEU 934  ? CD1 ? A LEU 936  CD1 
199 1 Y 1 A LEU 934  ? CD2 ? A LEU 936  CD2 
200 1 Y 1 A GLN 938  ? CG  ? A GLN 940  CG  
201 1 Y 1 A GLN 938  ? CD  ? A GLN 940  CD  
202 1 Y 1 A GLN 938  ? OE1 ? A GLN 940  OE1 
203 1 Y 1 A GLN 938  ? NE2 ? A GLN 940  NE2 
204 1 Y 1 A ARG 939  ? CG  ? A ARG 941  CG  
205 1 Y 1 A ARG 939  ? CD  ? A ARG 941  CD  
206 1 Y 1 A ARG 939  ? NE  ? A ARG 941  NE  
207 1 Y 1 A ARG 939  ? CZ  ? A ARG 941  CZ  
208 1 Y 1 A ARG 939  ? NH1 ? A ARG 941  NH1 
209 1 Y 1 A ARG 939  ? NH2 ? A ARG 941  NH2 
210 1 Y 1 A ARG 958  ? CG  ? A ARG 960  CG  
211 1 Y 1 A ARG 958  ? CD  ? A ARG 960  CD  
212 1 Y 1 A ARG 958  ? NE  ? A ARG 960  NE  
213 1 Y 1 A ARG 958  ? CZ  ? A ARG 960  CZ  
214 1 Y 1 A ARG 958  ? NH1 ? A ARG 960  NH1 
215 1 Y 1 A ARG 958  ? NH2 ? A ARG 960  NH2 
216 1 Y 1 A LYS 990  ? CG  ? A LYS 992  CG  
217 1 Y 1 A LYS 990  ? CD  ? A LYS 992  CD  
218 1 Y 1 A LYS 990  ? CE  ? A LYS 992  CE  
219 1 Y 1 A LYS 990  ? NZ  ? A LYS 992  NZ  
220 1 Y 1 A ARG 1091 ? CG  ? A ARG 1093 CG  
221 1 Y 1 A ARG 1091 ? CD  ? A ARG 1093 CD  
222 1 Y 1 A ARG 1091 ? NE  ? A ARG 1093 NE  
223 1 Y 1 A ARG 1091 ? CZ  ? A ARG 1093 CZ  
224 1 Y 1 A ARG 1091 ? NH1 ? A ARG 1093 NH1 
225 1 Y 1 A ARG 1091 ? NH2 ? A ARG 1093 NH2 
226 1 Y 1 A LYS 1139 ? CG  ? A LYS 1141 CG  
227 1 Y 1 A LYS 1139 ? CD  ? A LYS 1141 CD  
228 1 Y 1 A LYS 1139 ? CE  ? A LYS 1141 CE  
229 1 Y 1 A LYS 1139 ? NZ  ? A LYS 1141 NZ  
230 1 Y 1 A GLN 1143 ? CG  ? A GLN 1145 CG  
231 1 Y 1 A GLN 1143 ? CD  ? A GLN 1145 CD  
232 1 Y 1 A GLN 1143 ? OE1 ? A GLN 1145 OE1 
233 1 Y 1 A GLN 1143 ? NE2 ? A GLN 1145 NE2 
234 1 Y 1 A SER 1150 ? OG  ? A SER 1152 OG  
235 1 Y 1 A LYS 1153 ? CG  ? A LYS 1155 CG  
236 1 Y 1 A LYS 1153 ? CD  ? A LYS 1155 CD  
237 1 Y 1 A LYS 1153 ? CE  ? A LYS 1155 CE  
238 1 Y 1 A LYS 1153 ? NZ  ? A LYS 1155 NZ  
239 1 Y 1 A GLU 1171 ? CG  ? A GLU 1173 CG  
240 1 Y 1 A GLU 1171 ? CD  ? A GLU 1173 CD  
241 1 Y 1 A GLU 1171 ? OE1 ? A GLU 1173 OE1 
242 1 Y 1 A GLU 1171 ? OE2 ? A GLU 1173 OE2 
243 1 Y 1 A SER 1228 ? OG  ? A SER 1230 OG  
244 1 Y 1 B ASP 20   ? CG  ? B ASP 22   CG  
245 1 Y 1 B ASP 20   ? OD1 ? B ASP 22   OD1 
246 1 Y 1 B ASP 20   ? OD2 ? B ASP 22   OD2 
247 1 Y 1 B GLU 52   ? CG  ? B GLU 54   CG  
248 1 Y 1 B GLU 52   ? CD  ? B GLU 54   CD  
249 1 Y 1 B GLU 52   ? OE1 ? B GLU 54   OE1 
250 1 Y 1 B GLU 52   ? OE2 ? B GLU 54   OE2 
251 1 Y 1 B LYS 58   ? CG  ? B LYS 60   CG  
252 1 Y 1 B LYS 58   ? CD  ? B LYS 60   CD  
253 1 Y 1 B LYS 58   ? CE  ? B LYS 60   CE  
254 1 Y 1 B LYS 58   ? NZ  ? B LYS 60   NZ  
255 1 Y 1 B GLU 59   ? CG  ? B GLU 61   CG  
256 1 Y 1 B GLU 59   ? CD  ? B GLU 61   CD  
257 1 Y 1 B GLU 59   ? OE1 ? B GLU 61   OE1 
258 1 Y 1 B GLU 59   ? OE2 ? B GLU 61   OE2 
259 1 Y 1 B SER 66   ? OG  ? B SER 68   OG  
260 1 Y 1 B LYS 70   ? CG  ? B LYS 72   CG  
261 1 Y 1 B LYS 70   ? CD  ? B LYS 72   CD  
262 1 Y 1 B LYS 70   ? CE  ? B LYS 72   CE  
263 1 Y 1 B LYS 70   ? NZ  ? B LYS 72   NZ  
264 1 Y 1 B GLU 73   ? CG  ? B GLU 75   CG  
265 1 Y 1 B GLU 73   ? CD  ? B GLU 75   CD  
266 1 Y 1 B GLU 73   ? OE1 ? B GLU 75   OE1 
267 1 Y 1 B GLU 73   ? OE2 ? B GLU 75   OE2 
268 1 Y 1 B GLU 85   ? CG  ? B GLU 87   CG  
269 1 Y 1 B GLU 85   ? CD  ? B GLU 87   CD  
270 1 Y 1 B GLU 85   ? OE1 ? B GLU 87   OE1 
271 1 Y 1 B GLU 85   ? OE2 ? B GLU 87   OE2 
272 1 Y 1 B GLN 89   ? CG  ? B GLN 91   CG  
273 1 Y 1 B GLN 89   ? CD  ? B GLN 91   CD  
274 1 Y 1 B GLN 89   ? OE1 ? B GLN 91   OE1 
275 1 Y 1 B GLN 89   ? NE2 ? B GLN 91   NE2 
276 1 Y 1 B ARG 122  ? CG  ? B ARG 124  CG  
277 1 Y 1 B ARG 122  ? CD  ? B ARG 124  CD  
278 1 Y 1 B ARG 122  ? NE  ? B ARG 124  NE  
279 1 Y 1 B ARG 122  ? CZ  ? B ARG 124  CZ  
280 1 Y 1 B ARG 122  ? NH1 ? B ARG 124  NH1 
281 1 Y 1 B ARG 122  ? NH2 ? B ARG 124  NH2 
282 1 Y 1 B LYS 124  ? CG  ? B LYS 126  CG  
283 1 Y 1 B LYS 124  ? CD  ? B LYS 126  CD  
284 1 Y 1 B LYS 124  ? CE  ? B LYS 126  CE  
285 1 Y 1 B LYS 124  ? NZ  ? B LYS 126  NZ  
286 1 Y 1 B ASP 127  ? CG  ? B ASP 129  CG  
287 1 Y 1 B ASP 127  ? OD1 ? B ASP 129  OD1 
288 1 Y 1 B ASP 127  ? OD2 ? B ASP 129  OD2 
289 1 Y 1 B ASN 129  ? CG  ? B ASN 131  CG  
290 1 Y 1 B ASN 129  ? OD1 ? B ASN 131  OD1 
291 1 Y 1 B ASN 129  ? ND2 ? B ASN 131  ND2 
292 1 Y 1 B LYS 131  ? CG  ? B LYS 133  CG  
293 1 Y 1 B LYS 131  ? CD  ? B LYS 133  CD  
294 1 Y 1 B LYS 131  ? CE  ? B LYS 133  CE  
295 1 Y 1 B LYS 131  ? NZ  ? B LYS 133  NZ  
296 1 Y 1 B SER 132  ? OG  ? B SER 134  OG  
297 1 Y 1 B HIS 133  ? CG  ? B HIS 135  CG  
298 1 Y 1 B HIS 133  ? ND1 ? B HIS 135  ND1 
299 1 Y 1 B HIS 133  ? CD2 ? B HIS 135  CD2 
300 1 Y 1 B HIS 133  ? CE1 ? B HIS 135  CE1 
301 1 Y 1 B HIS 133  ? NE2 ? B HIS 135  NE2 
302 1 Y 1 B LYS 154  ? CG  ? B LYS 156  CG  
303 1 Y 1 B LYS 154  ? CD  ? B LYS 156  CD  
304 1 Y 1 B LYS 154  ? CE  ? B LYS 156  CE  
305 1 Y 1 B LYS 154  ? NZ  ? B LYS 156  NZ  
306 1 Y 1 B ARG 181  ? CG  ? B ARG 183  CG  
307 1 Y 1 B ARG 181  ? CD  ? B ARG 183  CD  
308 1 Y 1 B ARG 181  ? NE  ? B ARG 183  NE  
309 1 Y 1 B ARG 181  ? CZ  ? B ARG 183  CZ  
310 1 Y 1 B ARG 181  ? NH1 ? B ARG 183  NH1 
311 1 Y 1 B ARG 181  ? NH2 ? B ARG 183  NH2 
312 1 Y 1 B ARG 189  ? CG  ? B ARG 191  CG  
313 1 Y 1 B ARG 189  ? CD  ? B ARG 191  CD  
314 1 Y 1 B ARG 189  ? NE  ? B ARG 191  NE  
315 1 Y 1 B ARG 189  ? CZ  ? B ARG 191  CZ  
316 1 Y 1 B ARG 189  ? NH1 ? B ARG 191  NH1 
317 1 Y 1 B ARG 189  ? NH2 ? B ARG 191  NH2 
318 1 Y 1 B GLN 194  ? CG  ? B GLN 196  CG  
319 1 Y 1 B GLN 194  ? CD  ? B GLN 196  CD  
320 1 Y 1 B GLN 194  ? OE1 ? B GLN 196  OE1 
321 1 Y 1 B GLN 194  ? NE2 ? B GLN 196  NE2 
322 1 Y 1 B LYS 206  ? CG  ? B LYS 208  CG  
323 1 Y 1 B LYS 206  ? CD  ? B LYS 208  CD  
324 1 Y 1 B LYS 206  ? CE  ? B LYS 208  CE  
325 1 Y 1 B LYS 206  ? NZ  ? B LYS 208  NZ  
326 1 Y 1 B LYS 209  ? CG  ? B LYS 211  CG  
327 1 Y 1 B LYS 209  ? CD  ? B LYS 211  CD  
328 1 Y 1 B LYS 209  ? CE  ? B LYS 211  CE  
329 1 Y 1 B LYS 209  ? NZ  ? B LYS 211  NZ  
330 1 Y 1 B LYS 214  ? CG  ? B LYS 216  CG  
331 1 Y 1 B LYS 214  ? CD  ? B LYS 216  CD  
332 1 Y 1 B LYS 214  ? CE  ? B LYS 216  CE  
333 1 Y 1 B LYS 214  ? NZ  ? B LYS 216  NZ  
334 1 Y 1 B LYS 249  ? CG  ? B LYS 251  CG  
335 1 Y 1 B LYS 249  ? CD  ? B LYS 251  CD  
336 1 Y 1 B LYS 249  ? CE  ? B LYS 251  CE  
337 1 Y 1 B LYS 249  ? NZ  ? B LYS 251  NZ  
338 1 Y 1 B GLU 258  ? CG  ? B GLU 260  CG  
339 1 Y 1 B GLU 258  ? CD  ? B GLU 260  CD  
340 1 Y 1 B GLU 258  ? OE1 ? B GLU 260  OE1 
341 1 Y 1 B GLU 258  ? OE2 ? B GLU 260  OE2 
342 1 Y 1 B LYS 437  ? CG  ? B LYS 439  CG  
343 1 Y 1 B LYS 437  ? CD  ? B LYS 439  CD  
344 1 Y 1 B LYS 437  ? CE  ? B LYS 439  CE  
345 1 Y 1 B LYS 437  ? NZ  ? B LYS 439  NZ  
346 1 Y 1 B ASP 438  ? CG  ? B ASP 440  CG  
347 1 Y 1 B ASP 438  ? OD1 ? B ASP 440  OD1 
348 1 Y 1 B ASP 438  ? OD2 ? B ASP 440  OD2 
349 1 Y 1 B LYS 443  ? CG  ? B LYS 445  CG  
350 1 Y 1 B LYS 443  ? CD  ? B LYS 445  CD  
351 1 Y 1 B LYS 443  ? CE  ? B LYS 445  CE  
352 1 Y 1 B LYS 443  ? NZ  ? B LYS 445  NZ  
353 1 Y 1 B LEU 449  ? CG  ? B LEU 451  CG  
354 1 Y 1 B LEU 449  ? CD1 ? B LEU 451  CD1 
355 1 Y 1 B LEU 449  ? CD2 ? B LEU 451  CD2 
356 1 Y 1 B GLU 458  ? CG  ? B GLU 460  CG  
357 1 Y 1 B GLU 458  ? CD  ? B GLU 460  CD  
358 1 Y 1 B GLU 458  ? OE1 ? B GLU 460  OE1 
359 1 Y 1 B GLU 458  ? OE2 ? B GLU 460  OE2 
360 1 Y 1 B ARG 463  ? CG  ? B ARG 465  CG  
361 1 Y 1 B ARG 463  ? CD  ? B ARG 465  CD  
362 1 Y 1 B ARG 463  ? NE  ? B ARG 465  NE  
363 1 Y 1 B ARG 463  ? CZ  ? B ARG 465  CZ  
364 1 Y 1 B ARG 463  ? NH1 ? B ARG 465  NH1 
365 1 Y 1 B ARG 463  ? NH2 ? B ARG 465  NH2 
366 1 Y 1 B ASP 467  ? CG  ? B ASP 469  CG  
367 1 Y 1 B ASP 467  ? OD1 ? B ASP 469  OD1 
368 1 Y 1 B ASP 467  ? OD2 ? B ASP 469  OD2 
369 1 Y 1 B HIS 479  ? CG  ? B HIS 481  CG  
370 1 Y 1 B HIS 479  ? ND1 ? B HIS 481  ND1 
371 1 Y 1 B HIS 479  ? CD2 ? B HIS 481  CD2 
372 1 Y 1 B HIS 479  ? CE1 ? B HIS 481  CE1 
373 1 Y 1 B HIS 479  ? NE2 ? B HIS 481  NE2 
374 1 Y 1 B GLU 480  ? CG  ? B GLU 482  CG  
375 1 Y 1 B GLU 480  ? CD  ? B GLU 482  CD  
376 1 Y 1 B GLU 480  ? OE1 ? B GLU 482  OE1 
377 1 Y 1 B GLU 480  ? OE2 ? B GLU 482  OE2 
378 1 Y 1 B LEU 482  ? CG  ? B LEU 484  CG  
379 1 Y 1 B LEU 482  ? CD1 ? B LEU 484  CD1 
380 1 Y 1 B LEU 482  ? CD2 ? B LEU 484  CD2 
381 1 Y 1 B TYR 485  ? CG  ? B TYR 487  CG  
382 1 Y 1 B TYR 485  ? CD1 ? B TYR 487  CD1 
383 1 Y 1 B TYR 485  ? CD2 ? B TYR 487  CD2 
384 1 Y 1 B TYR 485  ? CE1 ? B TYR 487  CE1 
385 1 Y 1 B TYR 485  ? CE2 ? B TYR 487  CE2 
386 1 Y 1 B TYR 485  ? CZ  ? B TYR 487  CZ  
387 1 Y 1 B TYR 485  ? OH  ? B TYR 487  OH  
388 1 Y 1 B ARG 488  ? CG  ? B ARG 490  CG  
389 1 Y 1 B ARG 488  ? CD  ? B ARG 490  CD  
390 1 Y 1 B ARG 488  ? NE  ? B ARG 490  NE  
391 1 Y 1 B ARG 488  ? CZ  ? B ARG 490  CZ  
392 1 Y 1 B ARG 488  ? NH1 ? B ARG 490  NH1 
393 1 Y 1 B ARG 488  ? NH2 ? B ARG 490  NH2 
394 1 Y 1 B ASN 496  ? CG  ? B ASN 498  CG  
395 1 Y 1 B ASN 496  ? OD1 ? B ASN 498  OD1 
396 1 Y 1 B ASN 496  ? ND2 ? B ASN 498  ND2 
397 1 Y 1 B SER 498  ? OG  ? B SER 500  OG  
398 1 Y 1 B VAL 500  ? CG1 ? B VAL 502  CG1 
399 1 Y 1 B VAL 500  ? CG2 ? B VAL 502  CG2 
400 1 Y 1 B ILE 503  ? CG1 ? B ILE 505  CG1 
401 1 Y 1 B ILE 503  ? CG2 ? B ILE 505  CG2 
402 1 Y 1 B ILE 503  ? CD1 ? B ILE 505  CD1 
403 1 Y 1 B ASN 504  ? CG  ? B ASN 506  CG  
404 1 Y 1 B ASN 504  ? OD1 ? B ASN 506  OD1 
405 1 Y 1 B ASN 504  ? ND2 ? B ASN 506  ND2 
406 1 Y 1 B LYS 507  ? CG  ? B LYS 509  CG  
407 1 Y 1 B LYS 507  ? CD  ? B LYS 509  CD  
408 1 Y 1 B LYS 507  ? CE  ? B LYS 509  CE  
409 1 Y 1 B LYS 507  ? NZ  ? B LYS 509  NZ  
410 1 Y 1 B ILE 510  ? CG1 ? B ILE 512  CG1 
411 1 Y 1 B ILE 510  ? CG2 ? B ILE 512  CG2 
412 1 Y 1 B ILE 510  ? CD1 ? B ILE 512  CD1 
413 1 Y 1 B ASP 532  ? CG  ? B ASP 534  CG  
414 1 Y 1 B ASP 532  ? OD1 ? B ASP 534  OD1 
415 1 Y 1 B ASP 532  ? OD2 ? B ASP 534  OD2 
416 1 Y 1 B ARG 533  ? CG  ? B ARG 535  CG  
417 1 Y 1 B ARG 533  ? CD  ? B ARG 535  CD  
418 1 Y 1 B ARG 533  ? NE  ? B ARG 535  NE  
419 1 Y 1 B ARG 533  ? CZ  ? B ARG 535  CZ  
420 1 Y 1 B ARG 533  ? NH1 ? B ARG 535  NH1 
421 1 Y 1 B ARG 533  ? NH2 ? B ARG 535  NH2 
422 1 Y 1 B GLU 564  ? CG  ? B GLU 566  CG  
423 1 Y 1 B GLU 564  ? CD  ? B GLU 566  CD  
424 1 Y 1 B GLU 564  ? OE1 ? B GLU 566  OE1 
425 1 Y 1 B GLU 564  ? OE2 ? B GLU 566  OE2 
426 1 Y 1 B GLU 588  ? CG  ? B GLU 590  CG  
427 1 Y 1 B GLU 588  ? CD  ? B GLU 590  CD  
428 1 Y 1 B GLU 588  ? OE1 ? B GLU 590  OE1 
429 1 Y 1 B GLU 588  ? OE2 ? B GLU 590  OE2 
430 1 Y 1 B ARG 590  ? CG  ? B ARG 592  CG  
431 1 Y 1 B ARG 590  ? CD  ? B ARG 592  CD  
432 1 Y 1 B ARG 590  ? NE  ? B ARG 592  NE  
433 1 Y 1 B ARG 590  ? CZ  ? B ARG 592  CZ  
434 1 Y 1 B ARG 590  ? NH1 ? B ARG 592  NH1 
435 1 Y 1 B ARG 590  ? NH2 ? B ARG 592  NH2 
436 1 Y 1 B GLU 611  ? CG  ? B GLU 613  CG  
437 1 Y 1 B GLU 611  ? CD  ? B GLU 613  CD  
438 1 Y 1 B GLU 611  ? OE1 ? B GLU 613  OE1 
439 1 Y 1 B GLU 611  ? OE2 ? B GLU 613  OE2 
440 1 Y 1 B GLU 634  ? CG  ? B GLU 636  CG  
441 1 Y 1 B GLU 634  ? CD  ? B GLU 636  CD  
442 1 Y 1 B GLU 634  ? OE1 ? B GLU 636  OE1 
443 1 Y 1 B GLU 634  ? OE2 ? B GLU 636  OE2 
444 1 Y 1 B ARG 764  ? CG  ? B ARG 766  CG  
445 1 Y 1 B ARG 764  ? CD  ? B ARG 766  CD  
446 1 Y 1 B ARG 764  ? NE  ? B ARG 766  NE  
447 1 Y 1 B ARG 764  ? CZ  ? B ARG 766  CZ  
448 1 Y 1 B ARG 764  ? NH1 ? B ARG 766  NH1 
449 1 Y 1 B ARG 764  ? NH2 ? B ARG 766  NH2 
450 1 Y 1 B GLU 785  ? CG  ? B GLU 787  CG  
451 1 Y 1 B GLU 785  ? CD  ? B GLU 787  CD  
452 1 Y 1 B GLU 785  ? OE1 ? B GLU 787  OE1 
453 1 Y 1 B GLU 785  ? OE2 ? B GLU 787  OE2 
454 1 Y 1 B GLN 827  ? CG  ? B GLN 829  CG  
455 1 Y 1 B GLN 827  ? CD  ? B GLN 829  CD  
456 1 Y 1 B GLN 827  ? OE1 ? B GLN 829  OE1 
457 1 Y 1 B GLN 827  ? NE2 ? B GLN 829  NE2 
458 1 Y 1 B GLU 854  ? CG  ? B GLU 856  CG  
459 1 Y 1 B GLU 854  ? CD  ? B GLU 856  CD  
460 1 Y 1 B GLU 854  ? OE1 ? B GLU 856  OE1 
461 1 Y 1 B GLU 854  ? OE2 ? B GLU 856  OE2 
462 1 Y 1 B ASP 855  ? CG  ? B ASP 857  CG  
463 1 Y 1 B ASP 855  ? OD1 ? B ASP 857  OD1 
464 1 Y 1 B ASP 855  ? OD2 ? B ASP 857  OD2 
465 1 Y 1 B ARG 859  ? CG  ? B ARG 861  CG  
466 1 Y 1 B ARG 859  ? CD  ? B ARG 861  CD  
467 1 Y 1 B ARG 859  ? NE  ? B ARG 861  NE  
468 1 Y 1 B ARG 859  ? CZ  ? B ARG 861  CZ  
469 1 Y 1 B ARG 859  ? NH1 ? B ARG 861  NH1 
470 1 Y 1 B ARG 859  ? NH2 ? B ARG 861  NH2 
471 1 Y 1 B LEU 868  ? CG  ? B LEU 870  CG  
472 1 Y 1 B LEU 868  ? CD1 ? B LEU 870  CD1 
473 1 Y 1 B LEU 868  ? CD2 ? B LEU 870  CD2 
474 1 Y 1 B GLU 890  ? CG  ? B GLU 892  CG  
475 1 Y 1 B GLU 890  ? CD  ? B GLU 892  CD  
476 1 Y 1 B GLU 890  ? OE1 ? B GLU 892  OE1 
477 1 Y 1 B GLU 890  ? OE2 ? B GLU 892  OE2 
478 1 Y 1 B LEU 905  ? CG  ? B LEU 907  CG  
479 1 Y 1 B LEU 905  ? CD1 ? B LEU 907  CD1 
480 1 Y 1 B LEU 905  ? CD2 ? B LEU 907  CD2 
481 1 Y 1 B ARG 907  ? CG  ? B ARG 909  CG  
482 1 Y 1 B ARG 907  ? CD  ? B ARG 909  CD  
483 1 Y 1 B ARG 907  ? NE  ? B ARG 909  NE  
484 1 Y 1 B ARG 907  ? CZ  ? B ARG 909  CZ  
485 1 Y 1 B ARG 907  ? NH1 ? B ARG 909  NH1 
486 1 Y 1 B ARG 907  ? NH2 ? B ARG 909  NH2 
487 1 Y 1 B LYS 908  ? CG  ? B LYS 910  CG  
488 1 Y 1 B LYS 908  ? CD  ? B LYS 910  CD  
489 1 Y 1 B LYS 908  ? CE  ? B LYS 910  CE  
490 1 Y 1 B LYS 908  ? NZ  ? B LYS 910  NZ  
491 1 Y 1 B ILE 912  ? CG1 ? B ILE 914  CG1 
492 1 Y 1 B ILE 912  ? CG2 ? B ILE 914  CG2 
493 1 Y 1 B ILE 912  ? CD1 ? B ILE 914  CD1 
494 1 Y 1 B GLU 917  ? CG  ? B GLU 919  CG  
495 1 Y 1 B GLU 917  ? CD  ? B GLU 919  CD  
496 1 Y 1 B GLU 917  ? OE1 ? B GLU 919  OE1 
497 1 Y 1 B GLU 917  ? OE2 ? B GLU 919  OE2 
498 1 Y 1 B GLU 932  ? CG  ? B GLU 934  CG  
499 1 Y 1 B GLU 932  ? CD  ? B GLU 934  CD  
500 1 Y 1 B GLU 932  ? OE1 ? B GLU 934  OE1 
501 1 Y 1 B GLU 932  ? OE2 ? B GLU 934  OE2 
502 1 Y 1 B LYS 933  ? CG  ? B LYS 935  CG  
503 1 Y 1 B LYS 933  ? CD  ? B LYS 935  CD  
504 1 Y 1 B LYS 933  ? CE  ? B LYS 935  CE  
505 1 Y 1 B LYS 933  ? NZ  ? B LYS 935  NZ  
506 1 Y 1 B SER 935  ? OG  ? B SER 937  OG  
507 1 Y 1 B LEU 937  ? CG  ? B LEU 939  CG  
508 1 Y 1 B LEU 937  ? CD1 ? B LEU 939  CD1 
509 1 Y 1 B LEU 937  ? CD2 ? B LEU 939  CD2 
510 1 Y 1 B GLN 938  ? CG  ? B GLN 940  CG  
511 1 Y 1 B GLN 938  ? CD  ? B GLN 940  CD  
512 1 Y 1 B GLN 938  ? OE1 ? B GLN 940  OE1 
513 1 Y 1 B GLN 938  ? NE2 ? B GLN 940  NE2 
514 1 Y 1 B ARG 952  ? CG  ? B ARG 954  CG  
515 1 Y 1 B ARG 952  ? CD  ? B ARG 954  CD  
516 1 Y 1 B ARG 952  ? NE  ? B ARG 954  NE  
517 1 Y 1 B ARG 952  ? CZ  ? B ARG 954  CZ  
518 1 Y 1 B ARG 952  ? NH1 ? B ARG 954  NH1 
519 1 Y 1 B ARG 952  ? NH2 ? B ARG 954  NH2 
520 1 Y 1 B ARG 953  ? CG  ? B ARG 955  CG  
521 1 Y 1 B ARG 953  ? CD  ? B ARG 955  CD  
522 1 Y 1 B ARG 953  ? NE  ? B ARG 955  NE  
523 1 Y 1 B ARG 953  ? CZ  ? B ARG 955  CZ  
524 1 Y 1 B ARG 953  ? NH1 ? B ARG 955  NH1 
525 1 Y 1 B ARG 953  ? NH2 ? B ARG 955  NH2 
526 1 Y 1 B ARG 958  ? CG  ? B ARG 960  CG  
527 1 Y 1 B ARG 958  ? CD  ? B ARG 960  CD  
528 1 Y 1 B ARG 958  ? NE  ? B ARG 960  NE  
529 1 Y 1 B ARG 958  ? CZ  ? B ARG 960  CZ  
530 1 Y 1 B ARG 958  ? NH1 ? B ARG 960  NH1 
531 1 Y 1 B ARG 958  ? NH2 ? B ARG 960  NH2 
532 1 Y 1 B ARG 977  ? CG  ? B ARG 979  CG  
533 1 Y 1 B ARG 977  ? CD  ? B ARG 979  CD  
534 1 Y 1 B ARG 977  ? NE  ? B ARG 979  NE  
535 1 Y 1 B ARG 977  ? CZ  ? B ARG 979  CZ  
536 1 Y 1 B ARG 977  ? NH1 ? B ARG 979  NH1 
537 1 Y 1 B ARG 977  ? NH2 ? B ARG 979  NH2 
538 1 Y 1 B LYS 990  ? CG  ? B LYS 992  CG  
539 1 Y 1 B LYS 990  ? CD  ? B LYS 992  CD  
540 1 Y 1 B LYS 990  ? CE  ? B LYS 992  CE  
541 1 Y 1 B LYS 990  ? NZ  ? B LYS 992  NZ  
542 1 Y 1 B ARG 1063 ? CG  ? B ARG 1065 CG  
543 1 Y 1 B ARG 1063 ? CD  ? B ARG 1065 CD  
544 1 Y 1 B ARG 1063 ? NE  ? B ARG 1065 NE  
545 1 Y 1 B ARG 1063 ? CZ  ? B ARG 1065 CZ  
546 1 Y 1 B ARG 1063 ? NH1 ? B ARG 1065 NH1 
547 1 Y 1 B ARG 1063 ? NH2 ? B ARG 1065 NH2 
548 1 Y 1 B ARG 1091 ? CG  ? B ARG 1093 CG  
549 1 Y 1 B ARG 1091 ? CD  ? B ARG 1093 CD  
550 1 Y 1 B ARG 1091 ? NE  ? B ARG 1093 NE  
551 1 Y 1 B ARG 1091 ? CZ  ? B ARG 1093 CZ  
552 1 Y 1 B ARG 1091 ? NH1 ? B ARG 1093 NH1 
553 1 Y 1 B ARG 1091 ? NH2 ? B ARG 1093 NH2 
554 1 Y 1 B LYS 1139 ? CG  ? B LYS 1141 CG  
555 1 Y 1 B LYS 1139 ? CD  ? B LYS 1141 CD  
556 1 Y 1 B LYS 1139 ? CE  ? B LYS 1141 CE  
557 1 Y 1 B LYS 1139 ? NZ  ? B LYS 1141 NZ  
558 1 Y 1 B ASN 1140 ? CG  ? B ASN 1142 CG  
559 1 Y 1 B ASN 1140 ? OD1 ? B ASN 1142 OD1 
560 1 Y 1 B ASN 1140 ? ND2 ? B ASN 1142 ND2 
561 1 Y 1 B GLN 1143 ? CG  ? B GLN 1145 CG  
562 1 Y 1 B GLN 1143 ? CD  ? B GLN 1145 CD  
563 1 Y 1 B GLN 1143 ? OE1 ? B GLN 1145 OE1 
564 1 Y 1 B GLN 1143 ? NE2 ? B GLN 1145 NE2 
565 1 Y 1 B LEU 1147 ? CG  ? B LEU 1149 CG  
566 1 Y 1 B LEU 1147 ? CD1 ? B LEU 1149 CD1 
567 1 Y 1 B LEU 1147 ? CD2 ? B LEU 1149 CD2 
568 1 Y 1 B LYS 1153 ? CG  ? B LYS 1155 CG  
569 1 Y 1 B LYS 1153 ? CD  ? B LYS 1155 CD  
570 1 Y 1 B LYS 1153 ? CE  ? B LYS 1155 CE  
571 1 Y 1 B LYS 1153 ? NZ  ? B LYS 1155 NZ  
572 1 Y 1 B GLU 1171 ? CG  ? B GLU 1173 CG  
573 1 Y 1 B GLU 1171 ? CD  ? B GLU 1173 CD  
574 1 Y 1 B GLU 1171 ? OE1 ? B GLU 1173 OE1 
575 1 Y 1 B GLU 1171 ? OE2 ? B GLU 1173 OE2 
576 1 Y 1 B LYS 1178 ? CG  ? B LYS 1180 CG  
577 1 Y 1 B LYS 1178 ? CD  ? B LYS 1180 CD  
578 1 Y 1 B LYS 1178 ? CE  ? B LYS 1180 CE  
579 1 Y 1 B LYS 1178 ? NZ  ? B LYS 1180 NZ  
580 1 Y 1 B GLU 1197 ? CG  ? B GLU 1199 CG  
581 1 Y 1 B GLU 1197 ? CD  ? B GLU 1199 CD  
582 1 Y 1 B GLU 1197 ? OE1 ? B GLU 1199 OE1 
583 1 Y 1 B GLU 1197 ? OE2 ? B GLU 1199 OE2 
# 
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  ? ? ? 1.21rc1_5156 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .            2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .            3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .            4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   106.31 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9DL5 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     100.538 
_cell.length_a_esd                 ? 
_cell.length_b                     101.077 
_cell.length_b_esd                 ? 
_cell.length_c                     125.757 
_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                         9DL5 
_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                   9DL5 
_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             2.32 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          47.07 
_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, 0.1 M ammonium sulfate, and 16% (w/v) PEG 3350. Crystal was soaked in cryobuffer containing 10 mM 5-Chloro-1-indanone (10% DMSO) 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                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 S 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-10-20 
_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   1.000024 
_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 8.2.1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.000024 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   8.2.1 
_diffrn_source.pdbx_synchrotron_site       ALS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9DL5 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.77 
_reflns.d_resolution_low                               48.25 
_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                                     436068 
_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                           99.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15.2 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.04 
_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                                0.069 
_reflns.pdbx_Rpim_I_all                                0.037 
_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                              0.058 
_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                                    1.77 
_reflns_shell.d_res_low                                     1.80 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           41392 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             11546 
_reflns_shell.percent_possible_obs                          99.5 
_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                               3.6 
_reflns_shell.pdbx_chi_squared                              0.96 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.6 
_reflns_shell.pdbx_Rrim_I_all                               0.980 
_reflns_shell.pdbx_Rpim_I_all                               0.511 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.577 
_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                                  0.834 
_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                                 9DL5 
_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                            1.77 
_refine.ls_d_res_low                             46.62 
_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                     436068 
_refine.ls_number_reflns_R_free                  21720 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    94.13 
_refine.ls_percent_reflns_R_free                 4.98 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1747 
_refine.ls_R_factor_R_free                       0.2061 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1731 
_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                          0.03 
_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                 21.17 
_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                            0.21 
_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.pdbx_number_atoms_protein        17427 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         342 
_refine_hist.number_atoms_solvent             1772 
_refine_hist.number_atoms_total               19541 
_refine_hist.d_res_high                       1.77 
_refine_hist.d_res_low                        46.62 
# 
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  ? 18156 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.821  ? 24763 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 13.527 ? 6526  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.047  ? 2909  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008  ? 3216  ? 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' 1.77 1.79  . . 692 13821 94.00 . . . . 0.3046 . . . . . . . . . . . 0.3536 
'X-RAY DIFFRACTION' 1.79 1.81  . . 704 13811 94.00 . . . . 0.2845 . . . . . . . . . . . 0.3148 
'X-RAY DIFFRACTION' 1.81 1.83  . . 765 13881 94.00 . . . . 0.2676 . . . . . . . . . . . 0.2801 
'X-RAY DIFFRACTION' 1.83 1.86  . . 812 13719 94.00 . . . . 0.2612 . . . . . . . . . . . 0.2713 
'X-RAY DIFFRACTION' 1.86 1.88  . . 721 13751 94.00 . . . . 0.2495 . . . . . . . . . . . 0.2899 
'X-RAY DIFFRACTION' 1.88 1.91  . . 727 13957 94.00 . . . . 0.2418 . . . . . . . . . . . 0.2931 
'X-RAY DIFFRACTION' 1.91 1.93  . . 763 13804 95.00 . . . . 0.2317 . . . . . . . . . . . 0.2691 
'X-RAY DIFFRACTION' 1.93 1.96  . . 710 13866 94.00 . . . . 0.2254 . . . . . . . . . . . 0.2674 
'X-RAY DIFFRACTION' 1.96 1.99  . . 800 13666 94.00 . . . . 0.2162 . . . . . . . . . . . 0.2548 
'X-RAY DIFFRACTION' 1.99 2.03  . . 730 13865 94.00 . . . . 0.2139 . . . . . . . . . . . 0.2617 
'X-RAY DIFFRACTION' 2.03 2.06  . . 700 13896 94.00 . . . . 0.2009 . . . . . . . . . . . 0.2197 
'X-RAY DIFFRACTION' 2.06 2.10  . . 716 13914 95.00 . . . . 0.1863 . . . . . . . . . . . 0.2328 
'X-RAY DIFFRACTION' 2.10 2.14  . . 710 13867 95.00 . . . . 0.1859 . . . . . . . . . . . 0.2372 
'X-RAY DIFFRACTION' 2.14 2.18  . . 683 13974 95.00 . . . . 0.1766 . . . . . . . . . . . 0.2205 
'X-RAY DIFFRACTION' 2.18 2.23  . . 682 13747 94.00 . . . . 0.1766 . . . . . . . . . . . 0.2048 
'X-RAY DIFFRACTION' 2.23 2.28  . . 655 13483 91.00 . . . . 0.1694 . . . . . . . . . . . 0.2128 
'X-RAY DIFFRACTION' 2.28 2.34  . . 668 13224 90.00 . . . . 0.1700 . . . . . . . . . . . 0.2075 
'X-RAY DIFFRACTION' 2.34 2.40  . . 755 13886 95.00 . . . . 0.1699 . . . . . . . . . . . 0.2229 
'X-RAY DIFFRACTION' 2.40 2.47  . . 733 13912 95.00 . . . . 0.1683 . . . . . . . . . . . 0.2198 
'X-RAY DIFFRACTION' 2.47 2.55  . . 756 13934 95.00 . . . . 0.1686 . . . . . . . . . . . 0.2100 
'X-RAY DIFFRACTION' 2.55 2.64  . . 693 14117 95.00 . . . . 0.1649 . . . . . . . . . . . 0.1988 
'X-RAY DIFFRACTION' 2.64 2.75  . . 734 13895 95.00 . . . . 0.1699 . . . . . . . . . . . 0.2092 
'X-RAY DIFFRACTION' 2.75 2.87  . . 760 13904 95.00 . . . . 0.1754 . . . . . . . . . . . 0.2259 
'X-RAY DIFFRACTION' 2.87 3.03  . . 756 13801 95.00 . . . . 0.1678 . . . . . . . . . . . 0.2080 
'X-RAY DIFFRACTION' 3.03 3.22  . . 727 13968 95.00 . . . . 0.1665 . . . . . . . . . . . 0.1943 
'X-RAY DIFFRACTION' 3.22 3.46  . . 728 13812 94.00 . . . . 0.1609 . . . . . . . . . . . 0.1813 
'X-RAY DIFFRACTION' 3.46 3.81  . . 696 13757 94.00 . . . . 0.1465 . . . . . . . . . . . 0.1841 
'X-RAY DIFFRACTION' 3.81 4.36  . . 694 13293 90.00 . . . . 0.1379 . . . . . . . . . . . 0.1536 
'X-RAY DIFFRACTION' 4.36 5.50  . . 772 13796 95.00 . . . . 0.1470 . . . . . . . . . . . 0.1744 
'X-RAY DIFFRACTION' 5.50 46.62 . . 678 14027 95.00 . . . . 0.1602 . . . . . . . . . . . 0.1733 
# 
_struct.entry_id                     9DL5 
_struct.title                        'Structure of proline utilization A complexed with 5-chloro-1-indanone' 
_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        9DL5 
_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 5 ? 
G  N N 3 ? 
H  N N 6 ? 
I  N N 5 ? 
J  N N 7 ? 
K  N N 4 ? 
L  N N 5 ? 
M  N N 8 ? 
N  N N 8 ? 
O  N N 8 ? 
P  N N 8 ? 
Q  N N 8 ? 
R  N N 8 ? 
S  N N 8 ? 
T  N N 8 ? 
U  N N 8 ? 
V  N N 2 ? 
W  N N 5 ? 
X  N N 3 ? 
Y  N N 5 ? 
Z  N N 5 ? 
AA N N 6 ? 
BA N N 4 ? 
CA N N 5 ? 
DA N N 4 ? 
EA N N 4 ? 
FA N N 5 ? 
GA N N 4 ? 
HA N N 8 ? 
IA N N 8 ? 
JA N N 8 ? 
KA N N 8 ? 
LA N N 8 ? 
MA N N 8 ? 
NA N N 8 ? 
OA N N 8 ? 
PA N N 8 ? 
QA N N 8 ? 
RA N N 9 ? 
SA N N 9 ? 
# 
_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 9DL5 A 3 ? 1235 ? F7X6I3 1 ? 1233 ? 1 1233 
2 1 9DL5 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 9DL5 SER A 1 ? UNP F7X6I3 ? ? 'expression tag' -1 1 
1 9DL5 MET A 2 ? UNP F7X6I3 ? ? 'expression tag' 0  2 
2 9DL5 SER B 1 ? UNP F7X6I3 ? ? 'expression tag' -1 3 
2 9DL5 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)' 14910 ? 
1 MORE         -283  ? 
1 'SSA (A^2)'  77880 ? 
# 
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,BA,CA,DA,EA,FA,GA,HA,IA,JA,KA,LA,MA,NA,OA,PA,QA,RA,SA 
2 1 A,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,RA                                                                   
3 1 B,V,W,X,Y,Z,AA,BA,CA,DA,EA,FA,GA,HA,IA,JA,KA,LA,MA,NA,OA,PA,QA,SA                                            
# 
_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   ? TYR A 41   ? SER A 29   TYR A 39   1 ? 11 
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 145  ? GLY A 155  ? ASN A 143  GLY A 153  1 ? 11 
HELX_P HELX_P8   AA8 ASN A 162  ? GLY A 178  ? ASN A 160  GLY A 176  1 ? 17 
HELX_P HELX_P9   AA9 GLY A 178  ? GLN A 196  ? GLY A 176  GLN A 194  1 ? 19 
HELX_P HELX_P10  AB1 THR A 202  ? LYS A 216  ? THR A 200  LYS A 214  1 ? 15 
HELX_P HELX_P11  AB2 THR A 231  ? ALA A 254  ? THR A 229  ALA A 252  1 ? 24 
HELX_P HELX_P12  AB3 ARG A 256  ? GLY A 261  ? ARG A 254  GLY A 259  1 ? 6  
HELX_P HELX_P13  AB4 LYS A 267  ? LEU A 271  ? LYS A 265  LEU A 269  5 ? 5  
HELX_P HELX_P14  AB5 SER A 276  ? ALA A 278  ? SER A 274  ALA A 276  5 ? 3  
HELX_P HELX_P15  AB6 GLN A 279  ? ASP A 302  ? GLN A 277  ASP A 300  1 ? 24 
HELX_P HELX_P16  AB7 GLU A 311  ? ASP A 313  ? GLU A 309  ASP A 311  5 ? 3  
HELX_P HELX_P17  AB8 ARG A 314  ? ASP A 328  ? ARG A 312  ASP A 326  1 ? 15 
HELX_P HELX_P18  AB9 GLY A 329  ? SER A 332  ? GLY A 327  SER A 330  5 ? 4  
HELX_P HELX_P19  AC1 ARG A 347  ? GLY A 363  ? ARG A 345  GLY A 361  1 ? 17 
HELX_P HELX_P20  AC2 TYR A 375  ? ASP A 386  ? TYR A 373  ASP A 384  1 ? 12 
HELX_P HELX_P21  AC3 ARG A 396  ? ALA A 413  ? ARG A 394  ALA A 411  1 ? 18 
HELX_P HELX_P22  AC4 ASN A 426  ? GLY A 438  ? ASN A 424  GLY A 436  1 ? 13 
HELX_P HELX_P23  AC5 GLY A 455  ? GLU A 460  ? GLY A 453  GLU A 458  1 ? 6  
HELX_P HELX_P24  AC6 SER A 500  ? ASN A 506  ? SER A 498  ASN A 504  1 ? 7  
HELX_P HELX_P25  AC7 SER A 511  ? ILE A 516  ? SER A 509  ILE A 514  1 ? 6  
HELX_P HELX_P26  AC8 ASP A 518  ? ALA A 525  ? ASP A 516  ALA A 523  1 ? 8  
HELX_P HELX_P27  AC9 LEU A 538  ? LEU A 542  ? LEU A 536  LEU A 540  5 ? 5  
HELX_P HELX_P28  AD1 ASN A 557  ? ALA A 573  ? ASN A 555  ALA A 571  1 ? 17 
HELX_P HELX_P29  AD2 SER A 611  ? VAL A 632  ? SER A 609  VAL A 630  1 ? 22 
HELX_P HELX_P30  AD3 PRO A 633  ? ARG A 651  ? PRO A 631  ARG A 649  1 ? 19 
HELX_P HELX_P31  AD4 ARG A 651  ? GLY A 664  ? ARG A 649  GLY A 662  1 ? 14 
HELX_P HELX_P32  AD5 SER A 666  ? LEU A 692  ? SER A 664  LEU A 690  1 ? 27 
HELX_P HELX_P33  AD6 LEU A 712  ? ALA A 725  ? LEU A 710  ALA A 723  1 ? 14 
HELX_P HELX_P34  AD7 THR A 737  ? ALA A 751  ? THR A 735  ALA A 749  1 ? 15 
HELX_P HELX_P35  AD8 ASP A 764  ? ALA A 774  ? ASP A 762  ALA A 772  1 ? 11 
HELX_P HELX_P36  AD9 SER A 785  ? ALA A 797  ? SER A 783  ALA A 795  1 ? 13 
HELX_P HELX_P37  AE1 LEU A 826  ? ASP A 840  ? LEU A 824  ASP A 838  1 ? 15 
HELX_P HELX_P38  AE2 SER A 841  ? GLN A 844  ? SER A 839  GLN A 842  5 ? 4  
HELX_P HELX_P39  AE3 GLU A 856  ? HIS A 871  ? GLU A 854  HIS A 869  1 ? 16 
HELX_P HELX_P40  AE4 THR A 890  ? LEU A 907  ? THR A 888  LEU A 905  1 ? 18 
HELX_P HELX_P41  AE5 ALA A 917  ? GLY A 923  ? ALA A 915  GLY A 921  5 ? 7  
HELX_P HELX_P42  AE6 LYS A 935  ? LEU A 939  ? LYS A 933  LEU A 937  5 ? 5  
HELX_P HELX_P43  AE7 ARG A 954  ? ASP A 956  ? ARG A 952  ASP A 954  5 ? 3  
HELX_P HELX_P44  AE8 ASP A 957  ? THR A 968  ? ASP A 955  THR A 966  1 ? 12 
HELX_P HELX_P45  AE9 LEU A 980  ? ILE A 991  ? LEU A 978  ILE A 989  1 ? 12 
HELX_P HELX_P46  AF1 ARG A 1015 ? GLY A 1019 ? ARG A 1013 GLY A 1017 5 ? 5  
HELX_P HELX_P47  AF2 TYR A 1029 ? VAL A 1034 ? TYR A 1027 VAL A 1032 5 ? 6  
HELX_P HELX_P48  AF3 ASP A 1049 ? GLY A 1063 ? ASP A 1047 GLY A 1061 1 ? 15 
HELX_P HELX_P49  AF4 ALA A 1064 ? SER A 1078 ? ALA A 1062 SER A 1076 1 ? 15 
HELX_P HELX_P50  AF5 THR A 1110 ? THR A 1124 ? THR A 1108 THR A 1122 1 ? 15 
HELX_P HELX_P51  AF6 ALA A 1133 ? GLY A 1135 ? ALA A 1131 GLY A 1133 5 ? 3  
HELX_P HELX_P52  AF7 LEU A 1136 ? LYS A 1141 ? LEU A 1134 LYS A 1139 5 ? 6  
HELX_P HELX_P53  AF8 PRO A 1144 ? LEU A 1149 ? PRO A 1142 LEU A 1147 1 ? 6  
HELX_P HELX_P54  AF9 ASP A 1156 ? ASP A 1160 ? ASP A 1154 ASP A 1158 5 ? 5  
HELX_P HELX_P55  AG1 ASP A 1171 ? ALA A 1184 ? ASP A 1169 ALA A 1182 1 ? 14 
HELX_P HELX_P56  AG2 SER A 1196 ? ASN A 1203 ? SER A 1194 ASN A 1201 1 ? 8  
HELX_P HELX_P57  AG3 CYS A 1208 ? TRP A 1211 ? CYS A 1206 TRP A 1209 5 ? 4  
HELX_P HELX_P58  AG4 SER B 31   ? ALA B 40   ? SER B 29   ALA B 38   1 ? 10 
HELX_P HELX_P59  AG5 PRO B 44   ? THR B 57   ? PRO B 42   THR B 55   1 ? 14 
HELX_P HELX_P60  AG6 SER B 59   ? LYS B 80   ? SER B 57   LYS B 78   1 ? 22 
HELX_P HELX_P61  AG7 VAL B 86   ? TYR B 93   ? VAL B 84   TYR B 91   1 ? 8  
HELX_P HELX_P62  AG8 SER B 96   ? ARG B 112  ? SER B 94   ARG B 110  1 ? 17 
HELX_P HELX_P63  AG9 ASP B 115  ? LYS B 126  ? ASP B 113  LYS B 124  1 ? 12 
HELX_P HELX_P64  AH1 ASN B 131  ? LEU B 136  ? ASN B 129  LEU B 134  1 ? 6  
HELX_P HELX_P65  AH2 ASN B 145  ? GLY B 155  ? ASN B 143  GLY B 153  1 ? 11 
HELX_P HELX_P66  AH3 ASN B 162  ? GLY B 178  ? ASN B 160  GLY B 176  1 ? 17 
HELX_P HELX_P67  AH4 GLY B 178  ? GLN B 196  ? GLY B 176  GLN B 194  1 ? 19 
HELX_P HELX_P68  AH5 THR B 202  ? LYS B 216  ? THR B 200  LYS B 214  1 ? 15 
HELX_P HELX_P69  AH6 THR B 231  ? ALA B 254  ? THR B 229  ALA B 252  1 ? 24 
HELX_P HELX_P70  AH7 ARG B 256  ? GLY B 261  ? ARG B 254  GLY B 259  1 ? 6  
HELX_P HELX_P71  AH8 LYS B 267  ? LEU B 271  ? LYS B 265  LEU B 269  5 ? 5  
HELX_P HELX_P72  AH9 SER B 276  ? ALA B 278  ? SER B 274  ALA B 276  5 ? 3  
HELX_P HELX_P73  AI1 GLN B 279  ? ASP B 302  ? GLN B 277  ASP B 300  1 ? 24 
HELX_P HELX_P74  AI2 GLU B 311  ? ASP B 313  ? GLU B 309  ASP B 311  5 ? 3  
HELX_P HELX_P75  AI3 ARG B 314  ? LEU B 327  ? ARG B 312  LEU B 325  1 ? 14 
HELX_P HELX_P76  AI4 ASP B 328  ? SER B 332  ? ASP B 326  SER B 330  5 ? 5  
HELX_P HELX_P77  AI5 ARG B 347  ? GLY B 363  ? ARG B 345  GLY B 361  1 ? 17 
HELX_P HELX_P78  AI6 TYR B 375  ? ASP B 386  ? TYR B 373  ASP B 384  1 ? 12 
HELX_P HELX_P79  AI7 ARG B 396  ? ALA B 413  ? ARG B 394  ALA B 411  1 ? 18 
HELX_P HELX_P80  AI8 ASN B 426  ? GLY B 438  ? ASN B 424  GLY B 436  1 ? 13 
HELX_P HELX_P81  AI9 GLY B 455  ? GLU B 460  ? GLY B 453  GLU B 458  1 ? 6  
HELX_P HELX_P82  AJ1 HIS B 481  ? LEU B 493  ? HIS B 479  LEU B 491  1 ? 13 
HELX_P HELX_P83  AJ2 GLU B 494  ? ALA B 497  ? GLU B 492  ALA B 495  5 ? 4  
HELX_P HELX_P84  AJ3 SER B 500  ? ILE B 505  ? SER B 498  ILE B 503  1 ? 6  
HELX_P HELX_P85  AJ4 SER B 511  ? ILE B 516  ? SER B 509  ILE B 514  1 ? 6  
HELX_P HELX_P86  AJ5 ASP B 518  ? ALA B 525  ? ASP B 516  ALA B 523  1 ? 8  
HELX_P HELX_P87  AJ6 LEU B 538  ? LEU B 542  ? LEU B 536  LEU B 540  5 ? 5  
HELX_P HELX_P88  AJ7 PHE B 543  ? ARG B 547  ? PHE B 541  ARG B 545  5 ? 5  
HELX_P HELX_P89  AJ8 ASN B 557  ? ALA B 573  ? ASN B 555  ALA B 571  1 ? 17 
HELX_P HELX_P90  AJ9 SER B 611  ? ALA B 631  ? SER B 609  ALA B 629  1 ? 21 
HELX_P HELX_P91  AK1 PRO B 633  ? ARG B 651  ? PRO B 631  ARG B 649  1 ? 19 
HELX_P HELX_P92  AK2 ARG B 651  ? GLY B 664  ? ARG B 649  GLY B 662  1 ? 14 
HELX_P HELX_P93  AK3 SER B 666  ? LEU B 692  ? SER B 664  LEU B 690  1 ? 27 
HELX_P HELX_P94  AK4 LEU B 712  ? ALA B 725  ? LEU B 710  ALA B 723  1 ? 14 
HELX_P HELX_P95  AK5 THR B 737  ? ALA B 751  ? THR B 735  ALA B 749  1 ? 15 
HELX_P HELX_P96  AK6 PRO B 754  ? SER B 756  ? PRO B 752  SER B 754  5 ? 3  
HELX_P HELX_P97  AK7 ASP B 764  ? ALA B 774  ? ASP B 762  ALA B 772  1 ? 11 
HELX_P HELX_P98  AK8 SER B 785  ? ALA B 797  ? SER B 783  ALA B 795  1 ? 13 
HELX_P HELX_P99  AK9 LEU B 826  ? ASP B 840  ? LEU B 824  ASP B 838  1 ? 15 
HELX_P HELX_P100 AL1 SER B 841  ? GLN B 844  ? SER B 839  GLN B 842  5 ? 4  
HELX_P HELX_P101 AL2 GLU B 856  ? HIS B 871  ? GLU B 854  HIS B 869  1 ? 16 
HELX_P HELX_P102 AL3 THR B 890  ? LEU B 907  ? THR B 888  LEU B 905  1 ? 18 
HELX_P HELX_P103 AL4 ALA B 917  ? GLY B 923  ? ALA B 915  GLY B 921  5 ? 7  
HELX_P HELX_P104 AL5 LYS B 935  ? LEU B 939  ? LYS B 933  LEU B 937  5 ? 5  
HELX_P HELX_P105 AL6 ARG B 954  ? ASP B 956  ? ARG B 952  ASP B 954  5 ? 3  
HELX_P HELX_P106 AL7 ASP B 957  ? ALA B 967  ? ASP B 955  ALA B 965  1 ? 11 
HELX_P HELX_P107 AL8 LEU B 980  ? ILE B 991  ? LEU B 978  ILE B 989  1 ? 12 
HELX_P HELX_P108 AL9 ARG B 1015 ? GLY B 1019 ? ARG B 1013 GLY B 1017 5 ? 5  
HELX_P HELX_P109 AM1 TYR B 1029 ? VAL B 1034 ? TYR B 1027 VAL B 1032 5 ? 6  
HELX_P HELX_P110 AM2 ASP B 1049 ? LYS B 1062 ? ASP B 1047 LYS B 1060 1 ? 14 
HELX_P HELX_P111 AM3 ALA B 1064 ? SER B 1078 ? ALA B 1062 SER B 1076 1 ? 15 
HELX_P HELX_P112 AM4 THR B 1110 ? THR B 1124 ? THR B 1108 THR B 1122 1 ? 15 
HELX_P HELX_P113 AM5 ALA B 1133 ? GLY B 1135 ? ALA B 1131 GLY B 1133 5 ? 3  
HELX_P HELX_P114 AM6 LEU B 1136 ? LYS B 1141 ? LEU B 1134 LYS B 1139 5 ? 6  
HELX_P HELX_P115 AM7 PRO B 1144 ? LEU B 1149 ? PRO B 1142 LEU B 1147 1 ? 6  
HELX_P HELX_P116 AM8 ASP B 1156 ? GLY B 1161 ? ASP B 1154 GLY B 1159 1 ? 6  
HELX_P HELX_P117 AM9 ASP B 1171 ? ALA B 1184 ? ASP B 1169 ALA B 1182 1 ? 14 
HELX_P HELX_P118 AN1 SER B 1196 ? ASN B 1203 ? SER B 1194 ASN B 1201 1 ? 8  
HELX_P HELX_P119 AN2 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 -2.13 
2 GLY 1161 A . ? GLY 1159 A PRO 1162 A ? PRO 1160 A 1 3.31  
3 GLY 1021 B . ? GLY 1019 B PRO 1022 B ? PRO 1020 B 1 -3.41 
4 GLY 1161 B . ? GLY 1159 B PRO 1162 B ? PRO 1160 B 1 2.45  
# 
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  ? MET A 224  ? PHE A 216  MET A 222  
AA1 2  GLY A 263  ? ILE A 266  ? GLY A 261  ILE A 264  
AA1 3  GLY A 304  ? ILE A 307  ? GLY A 302  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  ? VAL A 478  ? CYS A 470  VAL A 476  
AA1 9  PHE A 218  ? MET A 224  ? PHE A 216  MET A 222  
AA2 1  TRP A 576  ? ALA A 578  ? TRP A 574  ALA A 576  
AA2 2  ASP A 599  ? GLU A 609  ? ASP A 597  GLU A 607  
AA2 3  GLU A 590  ? ASN A 596  ? GLU A 588  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  GLY A 1165 ? GLU A 1169 ? GLY A 1163 GLU A 1167 
AA6 5  VAL A 1192 ? ALA A 1195 ? VAL A 1190 ALA A 1193 
AA7 1  PHE B 218  ? MET B 224  ? PHE B 216  MET B 222  
AA7 2  GLY B 263  ? ILE B 266  ? GLY B 261  ILE B 264  
AA7 3  GLY B 304  ? ILE B 307  ? GLY B 302  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  ? VAL B 478  ? CYS B 470  VAL B 476  
AA7 9  PHE B 218  ? MET B 224  ? PHE B 216  MET B 222  
AA8 1  TRP B 576  ? ALA B 578  ? TRP B 574  ALA B 576  
AA8 2  ASP B 599  ? THR B 608  ? ASP B 597  THR B 606  
AA8 3  THR B 591  ? ASN B 596  ? THR B 589  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  LYS B 910  ? GLN B 913  ? LYS B 908  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 MET A 337  ? N MET A 335  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 VAL A 703  ? N VAL A 701  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 GLY B 263  ? O GLY B 261  
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 PHE B 339  ? N PHE B 337  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 VAL B 607  ? O VAL B 605  N ARG B 592  ? N ARG B 590  
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 LYS B 732  ? O LYS B 730  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 ILE B 931  ? N ILE B 929  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 PHE B 974  ? N PHE B 972  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 ALA B 1218 ? O ALA B 1216 N LEU B 1095 ? N LEU B 1093 
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 1154 ? O SER B 1152 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                   9DL5 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   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 OD1 A ASN 298  ? A O A HOH 2101 ? ? 2.11 
2 1 OE1 A GLU 539  ? ? O A HOH 2102 ? ? 2.12 
3 1 O   A HOH 2233 ? ? O A HOH 2813 ? ? 2.13 
4 1 OE1 B GLU 539  ? ? O B HOH 2101 ? ? 2.13 
5 1 O   A HOH 2683 ? ? O A HOH 2711 ? ? 2.14 
6 1 OE1 B GLU 1212 ? ? O B HOH 2102 ? ? 2.16 
7 1 O   A HOH 2660 ? ? O A HOH 2856 ? ? 2.18 
8 1 O   A HOH 2683 ? ? O A HOH 2718 ? ? 2.19 
9 1 O   A HOH 2436 ? ? O A HOH 2814 ? ? 2.19 
# 
_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     2111 
_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     2769 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_556 
_pdbx_validate_symm_contact.dist              2.17 
# 
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   ? ? -157.37 58.76   
2  1 GLU A 308  ? ? -121.78 -132.91 
3  1 MET A 452  ? ? -146.41 -47.95  
4  1 VAL A 460  ? ? -120.09 -50.88  
5  1 LYS A 465  ? ? -119.17 -122.96 
6  1 ASP A 597  ? ? -172.94 97.20   
7  1 THR A 689  ? ? -131.22 -43.92  
8  1 HIS A 694  ? ? -102.02 77.82   
9  1 THR A 811  ? ? -125.84 -161.52 
10 1 GLN A 814  ? ? -105.73 73.21   
11 1 GLN A 842  ? ? -90.72  31.15   
12 1 ASP A 877  ? ? -85.18  31.65   
13 1 LEU A 970  ? ? -97.82  -85.01  
14 1 VAL A 1007 ? ? -122.07 -54.19  
15 1 GLN A 1008 ? ? -116.60 77.56   
16 1 ALA B 22   ? ? -154.65 60.31   
17 1 LYS B 124  ? ? -137.98 -52.05  
18 1 GLU B 308  ? ? -119.78 -134.97 
19 1 LYS B 465  ? ? -105.90 -119.42 
20 1 ASP B 597  ? ? -171.10 99.54   
21 1 THR B 689  ? ? -131.87 -40.75  
22 1 HIS B 694  ? ? -100.56 74.02   
23 1 GLN B 814  ? ? -118.95 75.48   
24 1 GLN B 842  ? ? -95.06  31.78   
25 1 LEU B 970  ? ? -96.24  -86.52  
26 1 LYS B 990  ? ? -115.90 77.46   
27 1 GLN B 1040 ? ? 59.19   15.28   
# 
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 -25.4501 66.6250 92.9808 0.1995 ? 0.0032  ? 0.0165  ? 0.1528 ? 0.0137  ? 0.1856 ? 0.4278 ? -0.0251 
? 0.1499 ? 0.1202 ? 0.0402  ? 0.2574 ? -0.0161 ? -0.0123 ? 0.0018 ? 0.0238 ? 0.0238 ? 0.0043  ? 0.0078 ? 0.0164  ? -0.0086 ? 
2 'X-RAY DIFFRACTION' ? refined 5.9940   31.7623 90.9365 0.1228 ? -0.0005 ? -0.0008 ? 0.1552 ? -0.0126 ? 0.1443 ? 0.2209 ? -0.0099 
? 0.1297 ? 0.2512 ? -0.0814 ? 0.4621 ? 0.0219  ? -0.0438 ? 0.0007 ? 0.0477 ? 0.0197 ? -0.0152 ? 0.0438 ? -0.0904 ? -0.0411 ? 
# 
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 HIS 79   ? A HIS 81   
17 1 Y 1 A SER 80   ? A SER 82   
18 1 Y 1 A GLY 81   ? A GLY 83   
19 1 Y 1 A SER 82   ? A SER 84   
20 1 Y 1 A GLY 135  ? A GLY 137  
21 1 Y 1 A GLY 136  ? A GLY 138  
22 1 Y 1 A SER 137  ? A SER 139  
23 1 Y 1 A HIS 479  ? A HIS 481  
24 1 Y 1 A GLU 480  ? A GLU 482  
25 1 Y 1 A THR 481  ? A THR 483  
26 1 Y 1 A LEU 482  ? A LEU 484  
27 1 Y 1 A LEU 483  ? A LEU 485  
28 1 Y 1 A ALA 484  ? A ALA 486  
29 1 Y 1 A TYR 485  ? A TYR 487  
30 1 Y 1 A LEU 486  ? A LEU 488  
31 1 Y 1 A VAL 487  ? A VAL 489  
32 1 Y 1 A ARG 488  ? A ARG 490  
33 1 Y 1 A ARG 489  ? A ARG 491  
34 1 Y 1 A LEU 490  ? A LEU 492  
35 1 Y 1 A LEU 491  ? A LEU 493  
36 1 Y 1 A GLU 492  ? A GLU 494  
37 1 Y 1 A ASN 493  ? A ASN 495  
38 1 Y 1 A GLY 494  ? A GLY 496  
39 1 Y 1 A MET 1230 ? A MET 1232 
40 1 Y 1 A ALA 1231 ? A ALA 1233 
41 1 Y 1 A ILE 1232 ? A ILE 1234 
42 1 Y 1 A GLY 1233 ? A GLY 1235 
43 1 Y 1 B SER -1   ? B SER 1    
44 1 Y 1 B MET 0    ? B MET 2    
45 1 Y 1 B MET 1    ? B MET 3    
46 1 Y 1 B SER 2    ? B SER 4    
47 1 Y 1 B PRO 3    ? B PRO 5    
48 1 Y 1 B ASN 4    ? B ASN 6    
49 1 Y 1 B PRO 5    ? B PRO 7    
50 1 Y 1 B LEU 6    ? B LEU 8    
51 1 Y 1 B GLN 7    ? B GLN 9    
52 1 Y 1 B LYS 8    ? B LYS 10   
53 1 Y 1 B PRO 9    ? B PRO 11   
54 1 Y 1 B ALA 10   ? B ALA 12   
55 1 Y 1 B ILE 11   ? B ILE 13   
56 1 Y 1 B ASP 12   ? B ASP 14   
57 1 Y 1 B ALA 13   ? B ALA 15   
58 1 Y 1 B HIS 79   ? B HIS 81   
59 1 Y 1 B SER 80   ? B SER 82   
60 1 Y 1 B GLY 81   ? B GLY 83   
61 1 Y 1 B SER 82   ? B SER 84   
62 1 Y 1 B GLY 135  ? B GLY 137  
63 1 Y 1 B GLY 136  ? B GLY 138  
64 1 Y 1 B SER 137  ? B SER 139  
65 1 Y 1 B ALA 1222 ? B ALA 1224 
66 1 Y 1 B ALA 1223 ? B ALA 1225 
67 1 Y 1 B GLY 1224 ? B GLY 1226 
68 1 Y 1 B GLY 1225 ? B GLY 1227 
69 1 Y 1 B ASN 1226 ? B ASN 1228 
70 1 Y 1 B ALA 1227 ? B ALA 1229 
71 1 Y 1 B SER 1228 ? B SER 1230 
72 1 Y 1 B LEU 1229 ? B LEU 1231 
73 1 Y 1 B MET 1230 ? B MET 1232 
74 1 Y 1 B ALA 1231 ? B ALA 1233 
75 1 Y 1 B ILE 1232 ? B ILE 1234 
76 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 
A1BDA C10    C  Y N 1   
A1BDA C11    C  Y N 2   
A1BDA C02    C  Y N 3   
A1BDA C03    C  Y N 4   
A1BDA C04    C  Y N 5   
A1BDA C05    C  Y N 6   
A1BDA C06    C  N N 7   
A1BDA C08    C  N N 8   
A1BDA C09    C  N N 9   
A1BDA O07    O  N N 10  
A1BDA CL01   CL N N 11  
A1BDA H1     H  N N 12  
A1BDA H2     H  N N 13  
A1BDA H3     H  N N 14  
A1BDA H4     H  N N 15  
A1BDA H5     H  N N 16  
A1BDA H6     H  N N 17  
A1BDA H7     H  N N 18  
ALA   N      N  N N 19  
ALA   CA     C  N S 20  
ALA   C      C  N N 21  
ALA   O      O  N N 22  
ALA   CB     C  N N 23  
ALA   OXT    O  N N 24  
ALA   H      H  N N 25  
ALA   H2     H  N N 26  
ALA   HA     H  N N 27  
ALA   HB1    H  N N 28  
ALA   HB2    H  N N 29  
ALA   HB3    H  N N 30  
ALA   HXT    H  N N 31  
ARG   N      N  N N 32  
ARG   CA     C  N S 33  
ARG   C      C  N N 34  
ARG   O      O  N N 35  
ARG   CB     C  N N 36  
ARG   CG     C  N N 37  
ARG   CD     C  N N 38  
ARG   NE     N  N N 39  
ARG   CZ     C  N N 40  
ARG   NH1    N  N N 41  
ARG   NH2    N  N N 42  
ARG   OXT    O  N N 43  
ARG   H      H  N N 44  
ARG   H2     H  N N 45  
ARG   HA     H  N N 46  
ARG   HB2    H  N N 47  
ARG   HB3    H  N N 48  
ARG   HG2    H  N N 49  
ARG   HG3    H  N N 50  
ARG   HD2    H  N N 51  
ARG   HD3    H  N N 52  
ARG   HE     H  N N 53  
ARG   HH11   H  N N 54  
ARG   HH12   H  N N 55  
ARG   HH21   H  N N 56  
ARG   HH22   H  N N 57  
ARG   HXT    H  N N 58  
ASN   N      N  N N 59  
ASN   CA     C  N S 60  
ASN   C      C  N N 61  
ASN   O      O  N N 62  
ASN   CB     C  N N 63  
ASN   CG     C  N N 64  
ASN   OD1    O  N N 65  
ASN   ND2    N  N N 66  
ASN   OXT    O  N N 67  
ASN   H      H  N N 68  
ASN   H2     H  N N 69  
ASN   HA     H  N N 70  
ASN   HB2    H  N N 71  
ASN   HB3    H  N N 72  
ASN   HD21   H  N N 73  
ASN   HD22   H  N N 74  
ASN   HXT    H  N N 75  
ASP   N      N  N N 76  
ASP   CA     C  N S 77  
ASP   C      C  N N 78  
ASP   O      O  N N 79  
ASP   CB     C  N N 80  
ASP   CG     C  N N 81  
ASP   OD1    O  N N 82  
ASP   OD2    O  N N 83  
ASP   OXT    O  N N 84  
ASP   H      H  N N 85  
ASP   H2     H  N N 86  
ASP   HA     H  N N 87  
ASP   HB2    H  N N 88  
ASP   HB3    H  N N 89  
ASP   HD2    H  N N 90  
ASP   HXT    H  N N 91  
CYS   N      N  N N 92  
CYS   CA     C  N R 93  
CYS   C      C  N N 94  
CYS   O      O  N N 95  
CYS   CB     C  N N 96  
CYS   SG     S  N N 97  
CYS   OXT    O  N N 98  
CYS   H      H  N N 99  
CYS   H2     H  N N 100 
CYS   HA     H  N N 101 
CYS   HB2    H  N N 102 
CYS   HB3    H  N N 103 
CYS   HG     H  N N 104 
CYS   HXT    H  N N 105 
FAD   PA     P  N R 106 
FAD   O1A    O  N N 107 
FAD   O2A    O  N N 108 
FAD   O5B    O  N N 109 
FAD   C5B    C  N N 110 
FAD   C4B    C  N R 111 
FAD   O4B    O  N N 112 
FAD   C3B    C  N S 113 
FAD   O3B    O  N N 114 
FAD   C2B    C  N R 115 
FAD   O2B    O  N N 116 
FAD   C1B    C  N R 117 
FAD   N9A    N  Y N 118 
FAD   C8A    C  Y N 119 
FAD   N7A    N  Y N 120 
FAD   C5A    C  Y N 121 
FAD   C6A    C  Y N 122 
FAD   N6A    N  N N 123 
FAD   N1A    N  Y N 124 
FAD   C2A    C  Y N 125 
FAD   N3A    N  Y N 126 
FAD   C4A    C  Y N 127 
FAD   N1     N  N N 128 
FAD   C2     C  N N 129 
FAD   O2     O  N N 130 
FAD   N3     N  N N 131 
FAD   C4     C  N N 132 
FAD   O4     O  N N 133 
FAD   C4X    C  N N 134 
FAD   N5     N  N N 135 
FAD   C5X    C  Y N 136 
FAD   C6     C  Y N 137 
FAD   C7     C  Y N 138 
FAD   C7M    C  N N 139 
FAD   C8     C  Y N 140 
FAD   C8M    C  N N 141 
FAD   C9     C  Y N 142 
FAD   C9A    C  Y N 143 
FAD   N10    N  N N 144 
FAD   C10    C  N N 145 
FAD   "C1'"  C  N N 146 
FAD   "C2'"  C  N S 147 
FAD   "O2'"  O  N N 148 
FAD   "C3'"  C  N S 149 
FAD   "O3'"  O  N N 150 
FAD   "C4'"  C  N R 151 
FAD   "O4'"  O  N N 152 
FAD   "C5'"  C  N N 153 
FAD   "O5'"  O  N N 154 
FAD   P      P  N R 155 
FAD   O1P    O  N N 156 
FAD   O2P    O  N N 157 
FAD   O3P    O  N N 158 
FAD   HOA2   H  N N 159 
FAD   H51A   H  N N 160 
FAD   H52A   H  N N 161 
FAD   H4B    H  N N 162 
FAD   H3B    H  N N 163 
FAD   HO3A   H  N N 164 
FAD   H2B    H  N N 165 
FAD   HO2A   H  N N 166 
FAD   H1B    H  N N 167 
FAD   H8A    H  N N 168 
FAD   H61A   H  N N 169 
FAD   H62A   H  N N 170 
FAD   H2A    H  N N 171 
FAD   HN3    H  N N 172 
FAD   H6     H  N N 173 
FAD   HM71   H  N N 174 
FAD   HM72   H  N N 175 
FAD   HM73   H  N N 176 
FAD   HM81   H  N N 177 
FAD   HM82   H  N N 178 
FAD   HM83   H  N N 179 
FAD   H9     H  N N 180 
FAD   "H1'1" H  N N 181 
FAD   "H1'2" H  N N 182 
FAD   "H2'"  H  N N 183 
FAD   "HO2'" H  N N 184 
FAD   "H3'"  H  N N 185 
FAD   "HO3'" H  N N 186 
FAD   "H4'"  H  N N 187 
FAD   "HO4'" H  N N 188 
FAD   "H5'1" H  N N 189 
FAD   "H5'2" H  N N 190 
FAD   HOP2   H  N N 191 
FMT   C      C  N N 192 
FMT   O1     O  N N 193 
FMT   O2     O  N N 194 
FMT   H      H  N N 195 
FMT   HO2    H  N N 196 
GLN   N      N  N N 197 
GLN   CA     C  N S 198 
GLN   C      C  N N 199 
GLN   O      O  N N 200 
GLN   CB     C  N N 201 
GLN   CG     C  N N 202 
GLN   CD     C  N N 203 
GLN   OE1    O  N N 204 
GLN   NE2    N  N N 205 
GLN   OXT    O  N N 206 
GLN   H      H  N N 207 
GLN   H2     H  N N 208 
GLN   HA     H  N N 209 
GLN   HB2    H  N N 210 
GLN   HB3    H  N N 211 
GLN   HG2    H  N N 212 
GLN   HG3    H  N N 213 
GLN   HE21   H  N N 214 
GLN   HE22   H  N N 215 
GLN   HXT    H  N N 216 
GLU   N      N  N N 217 
GLU   CA     C  N S 218 
GLU   C      C  N N 219 
GLU   O      O  N N 220 
GLU   CB     C  N N 221 
GLU   CG     C  N N 222 
GLU   CD     C  N N 223 
GLU   OE1    O  N N 224 
GLU   OE2    O  N N 225 
GLU   OXT    O  N N 226 
GLU   H      H  N N 227 
GLU   H2     H  N N 228 
GLU   HA     H  N N 229 
GLU   HB2    H  N N 230 
GLU   HB3    H  N N 231 
GLU   HG2    H  N N 232 
GLU   HG3    H  N N 233 
GLU   HE2    H  N N 234 
GLU   HXT    H  N N 235 
GLY   N      N  N N 236 
GLY   CA     C  N N 237 
GLY   C      C  N N 238 
GLY   O      O  N N 239 
GLY   OXT    O  N N 240 
GLY   H      H  N N 241 
GLY   H2     H  N N 242 
GLY   HA2    H  N N 243 
GLY   HA3    H  N N 244 
GLY   HXT    H  N N 245 
HIS   N      N  N N 246 
HIS   CA     C  N S 247 
HIS   C      C  N N 248 
HIS   O      O  N N 249 
HIS   CB     C  N N 250 
HIS   CG     C  Y N 251 
HIS   ND1    N  Y N 252 
HIS   CD2    C  Y N 253 
HIS   CE1    C  Y N 254 
HIS   NE2    N  Y N 255 
HIS   OXT    O  N N 256 
HIS   H      H  N N 257 
HIS   H2     H  N N 258 
HIS   HA     H  N N 259 
HIS   HB2    H  N N 260 
HIS   HB3    H  N N 261 
HIS   HD1    H  N N 262 
HIS   HD2    H  N N 263 
HIS   HE1    H  N N 264 
HIS   HE2    H  N N 265 
HIS   HXT    H  N N 266 
HOH   O      O  N N 267 
HOH   H1     H  N N 268 
HOH   H2     H  N N 269 
ILE   N      N  N N 270 
ILE   CA     C  N S 271 
ILE   C      C  N N 272 
ILE   O      O  N N 273 
ILE   CB     C  N S 274 
ILE   CG1    C  N N 275 
ILE   CG2    C  N N 276 
ILE   CD1    C  N N 277 
ILE   OXT    O  N N 278 
ILE   H      H  N N 279 
ILE   H2     H  N N 280 
ILE   HA     H  N N 281 
ILE   HB     H  N N 282 
ILE   HG12   H  N N 283 
ILE   HG13   H  N N 284 
ILE   HG21   H  N N 285 
ILE   HG22   H  N N 286 
ILE   HG23   H  N N 287 
ILE   HD11   H  N N 288 
ILE   HD12   H  N N 289 
ILE   HD13   H  N N 290 
ILE   HXT    H  N N 291 
LEU   N      N  N N 292 
LEU   CA     C  N S 293 
LEU   C      C  N N 294 
LEU   O      O  N N 295 
LEU   CB     C  N N 296 
LEU   CG     C  N N 297 
LEU   CD1    C  N N 298 
LEU   CD2    C  N N 299 
LEU   OXT    O  N N 300 
LEU   H      H  N N 301 
LEU   H2     H  N N 302 
LEU   HA     H  N N 303 
LEU   HB2    H  N N 304 
LEU   HB3    H  N N 305 
LEU   HG     H  N N 306 
LEU   HD11   H  N N 307 
LEU   HD12   H  N N 308 
LEU   HD13   H  N N 309 
LEU   HD21   H  N N 310 
LEU   HD22   H  N N 311 
LEU   HD23   H  N N 312 
LEU   HXT    H  N N 313 
LYS   N      N  N N 314 
LYS   CA     C  N S 315 
LYS   C      C  N N 316 
LYS   O      O  N N 317 
LYS   CB     C  N N 318 
LYS   CG     C  N N 319 
LYS   CD     C  N N 320 
LYS   CE     C  N N 321 
LYS   NZ     N  N N 322 
LYS   OXT    O  N N 323 
LYS   H      H  N N 324 
LYS   H2     H  N N 325 
LYS   HA     H  N N 326 
LYS   HB2    H  N N 327 
LYS   HB3    H  N N 328 
LYS   HG2    H  N N 329 
LYS   HG3    H  N N 330 
LYS   HD2    H  N N 331 
LYS   HD3    H  N N 332 
LYS   HE2    H  N N 333 
LYS   HE3    H  N N 334 
LYS   HZ1    H  N N 335 
LYS   HZ2    H  N N 336 
LYS   HZ3    H  N N 337 
LYS   HXT    H  N N 338 
MET   N      N  N N 339 
MET   CA     C  N S 340 
MET   C      C  N N 341 
MET   O      O  N N 342 
MET   CB     C  N N 343 
MET   CG     C  N N 344 
MET   SD     S  N N 345 
MET   CE     C  N N 346 
MET   OXT    O  N N 347 
MET   H      H  N N 348 
MET   H2     H  N N 349 
MET   HA     H  N N 350 
MET   HB2    H  N N 351 
MET   HB3    H  N N 352 
MET   HG2    H  N N 353 
MET   HG3    H  N N 354 
MET   HE1    H  N N 355 
MET   HE2    H  N N 356 
MET   HE3    H  N N 357 
MET   HXT    H  N N 358 
PEG   C1     C  N N 359 
PEG   O1     O  N N 360 
PEG   C2     C  N N 361 
PEG   O2     O  N N 362 
PEG   C3     C  N N 363 
PEG   C4     C  N N 364 
PEG   O4     O  N N 365 
PEG   H11    H  N N 366 
PEG   H12    H  N N 367 
PEG   HO1    H  N N 368 
PEG   H21    H  N N 369 
PEG   H22    H  N N 370 
PEG   H31    H  N N 371 
PEG   H32    H  N N 372 
PEG   H41    H  N N 373 
PEG   H42    H  N N 374 
PEG   HO4    H  N N 375 
PG4   O1     O  N N 376 
PG4   C1     C  N N 377 
PG4   C2     C  N N 378 
PG4   O2     O  N N 379 
PG4   C3     C  N N 380 
PG4   C4     C  N N 381 
PG4   O3     O  N N 382 
PG4   C5     C  N N 383 
PG4   C6     C  N N 384 
PG4   O4     O  N N 385 
PG4   C7     C  N N 386 
PG4   C8     C  N N 387 
PG4   O5     O  N N 388 
PG4   HO1    H  N N 389 
PG4   H11    H  N N 390 
PG4   H12    H  N N 391 
PG4   H21    H  N N 392 
PG4   H22    H  N N 393 
PG4   H31    H  N N 394 
PG4   H32    H  N N 395 
PG4   H41    H  N N 396 
PG4   H42    H  N N 397 
PG4   H51    H  N N 398 
PG4   H52    H  N N 399 
PG4   H61    H  N N 400 
PG4   H62    H  N N 401 
PG4   H71    H  N N 402 
PG4   H72    H  N N 403 
PG4   H81    H  N N 404 
PG4   H82    H  N N 405 
PG4   HO5    H  N N 406 
PGE   C1     C  N N 407 
PGE   O1     O  N N 408 
PGE   C2     C  N N 409 
PGE   O2     O  N N 410 
PGE   C3     C  N N 411 
PGE   C4     C  N N 412 
PGE   O4     O  N N 413 
PGE   C6     C  N N 414 
PGE   C5     C  N N 415 
PGE   O3     O  N N 416 
PGE   H1     H  N N 417 
PGE   H12    H  N N 418 
PGE   HO1    H  N N 419 
PGE   H2     H  N N 420 
PGE   H22    H  N N 421 
PGE   H3     H  N N 422 
PGE   H32    H  N N 423 
PGE   H4     H  N N 424 
PGE   H42    H  N N 425 
PGE   HO4    H  N N 426 
PGE   H6     H  N N 427 
PGE   H62    H  N N 428 
PGE   H5     H  N N 429 
PGE   H52    H  N N 430 
PHE   N      N  N N 431 
PHE   CA     C  N S 432 
PHE   C      C  N N 433 
PHE   O      O  N N 434 
PHE   CB     C  N N 435 
PHE   CG     C  Y N 436 
PHE   CD1    C  Y N 437 
PHE   CD2    C  Y N 438 
PHE   CE1    C  Y N 439 
PHE   CE2    C  Y N 440 
PHE   CZ     C  Y N 441 
PHE   OXT    O  N N 442 
PHE   H      H  N N 443 
PHE   H2     H  N N 444 
PHE   HA     H  N N 445 
PHE   HB2    H  N N 446 
PHE   HB3    H  N N 447 
PHE   HD1    H  N N 448 
PHE   HD2    H  N N 449 
PHE   HE1    H  N N 450 
PHE   HE2    H  N N 451 
PHE   HZ     H  N N 452 
PHE   HXT    H  N N 453 
PRO   N      N  N N 454 
PRO   CA     C  N S 455 
PRO   C      C  N N 456 
PRO   O      O  N N 457 
PRO   CB     C  N N 458 
PRO   CG     C  N N 459 
PRO   CD     C  N N 460 
PRO   OXT    O  N N 461 
PRO   H      H  N N 462 
PRO   HA     H  N N 463 
PRO   HB2    H  N N 464 
PRO   HB3    H  N N 465 
PRO   HG2    H  N N 466 
PRO   HG3    H  N N 467 
PRO   HD2    H  N N 468 
PRO   HD3    H  N N 469 
PRO   HXT    H  N N 470 
SER   N      N  N N 471 
SER   CA     C  N S 472 
SER   C      C  N N 473 
SER   O      O  N N 474 
SER   CB     C  N N 475 
SER   OG     O  N N 476 
SER   OXT    O  N N 477 
SER   H      H  N N 478 
SER   H2     H  N N 479 
SER   HA     H  N N 480 
SER   HB2    H  N N 481 
SER   HB3    H  N N 482 
SER   HG     H  N N 483 
SER   HXT    H  N N 484 
SO4   S      S  N N 485 
SO4   O1     O  N N 486 
SO4   O2     O  N N 487 
SO4   O3     O  N N 488 
SO4   O4     O  N N 489 
THR   N      N  N N 490 
THR   CA     C  N S 491 
THR   C      C  N N 492 
THR   O      O  N N 493 
THR   CB     C  N R 494 
THR   OG1    O  N N 495 
THR   CG2    C  N N 496 
THR   OXT    O  N N 497 
THR   H      H  N N 498 
THR   H2     H  N N 499 
THR   HA     H  N N 500 
THR   HB     H  N N 501 
THR   HG1    H  N N 502 
THR   HG21   H  N N 503 
THR   HG22   H  N N 504 
THR   HG23   H  N N 505 
THR   HXT    H  N N 506 
TRP   N      N  N N 507 
TRP   CA     C  N S 508 
TRP   C      C  N N 509 
TRP   O      O  N N 510 
TRP   CB     C  N N 511 
TRP   CG     C  Y N 512 
TRP   CD1    C  Y N 513 
TRP   CD2    C  Y N 514 
TRP   NE1    N  Y N 515 
TRP   CE2    C  Y N 516 
TRP   CE3    C  Y N 517 
TRP   CZ2    C  Y N 518 
TRP   CZ3    C  Y N 519 
TRP   CH2    C  Y N 520 
TRP   OXT    O  N N 521 
TRP   H      H  N N 522 
TRP   H2     H  N N 523 
TRP   HA     H  N N 524 
TRP   HB2    H  N N 525 
TRP   HB3    H  N N 526 
TRP   HD1    H  N N 527 
TRP   HE1    H  N N 528 
TRP   HE3    H  N N 529 
TRP   HZ2    H  N N 530 
TRP   HZ3    H  N N 531 
TRP   HH2    H  N N 532 
TRP   HXT    H  N N 533 
TYR   N      N  N N 534 
TYR   CA     C  N S 535 
TYR   C      C  N N 536 
TYR   O      O  N N 537 
TYR   CB     C  N N 538 
TYR   CG     C  Y N 539 
TYR   CD1    C  Y N 540 
TYR   CD2    C  Y N 541 
TYR   CE1    C  Y N 542 
TYR   CE2    C  Y N 543 
TYR   CZ     C  Y N 544 
TYR   OH     O  N N 545 
TYR   OXT    O  N N 546 
TYR   H      H  N N 547 
TYR   H2     H  N N 548 
TYR   HA     H  N N 549 
TYR   HB2    H  N N 550 
TYR   HB3    H  N N 551 
TYR   HD1    H  N N 552 
TYR   HD2    H  N N 553 
TYR   HE1    H  N N 554 
TYR   HE2    H  N N 555 
TYR   HH     H  N N 556 
TYR   HXT    H  N N 557 
VAL   N      N  N N 558 
VAL   CA     C  N S 559 
VAL   C      C  N N 560 
VAL   O      O  N N 561 
VAL   CB     C  N N 562 
VAL   CG1    C  N N 563 
VAL   CG2    C  N N 564 
VAL   OXT    O  N N 565 
VAL   H      H  N N 566 
VAL   H2     H  N N 567 
VAL   HA     H  N N 568 
VAL   HB     H  N N 569 
VAL   HG11   H  N N 570 
VAL   HG12   H  N N 571 
VAL   HG13   H  N N 572 
VAL   HG21   H  N N 573 
VAL   HG22   H  N N 574 
VAL   HG23   H  N N 575 
VAL   HXT    H  N N 576 
# 
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 
A1BDA C08   C09    sing N N 1   
A1BDA C08   C06    sing N N 2   
A1BDA C09   C10    sing N N 3   
A1BDA C06   O07    doub N N 4   
A1BDA C06   C05    sing N N 5   
A1BDA C10   C11    doub Y N 6   
A1BDA C10   C05    sing Y N 7   
A1BDA C11   C02    sing Y N 8   
A1BDA C05   C04    doub Y N 9   
A1BDA C02   C03    doub Y N 10  
A1BDA C02   CL01   sing N N 11  
A1BDA C04   C03    sing Y N 12  
A1BDA C11   H1     sing N N 13  
A1BDA C03   H2     sing N N 14  
A1BDA C04   H3     sing N N 15  
A1BDA C08   H4     sing N N 16  
A1BDA C09   H5     sing N N 17  
A1BDA C08   H6     sing N N 18  
A1BDA C09   H7     sing N N 19  
ALA   N     CA     sing N N 20  
ALA   N     H      sing N N 21  
ALA   N     H2     sing N N 22  
ALA   CA    C      sing N N 23  
ALA   CA    CB     sing N N 24  
ALA   CA    HA     sing N N 25  
ALA   C     O      doub N N 26  
ALA   C     OXT    sing N N 27  
ALA   CB    HB1    sing N N 28  
ALA   CB    HB2    sing N N 29  
ALA   CB    HB3    sing N N 30  
ALA   OXT   HXT    sing N N 31  
ARG   N     CA     sing N N 32  
ARG   N     H      sing N N 33  
ARG   N     H2     sing N N 34  
ARG   CA    C      sing N N 35  
ARG   CA    CB     sing N N 36  
ARG   CA    HA     sing N N 37  
ARG   C     O      doub N N 38  
ARG   C     OXT    sing N N 39  
ARG   CB    CG     sing N N 40  
ARG   CB    HB2    sing N N 41  
ARG   CB    HB3    sing N N 42  
ARG   CG    CD     sing N N 43  
ARG   CG    HG2    sing N N 44  
ARG   CG    HG3    sing N N 45  
ARG   CD    NE     sing N N 46  
ARG   CD    HD2    sing N N 47  
ARG   CD    HD3    sing N N 48  
ARG   NE    CZ     sing N N 49  
ARG   NE    HE     sing N N 50  
ARG   CZ    NH1    sing N N 51  
ARG   CZ    NH2    doub N N 52  
ARG   NH1   HH11   sing N N 53  
ARG   NH1   HH12   sing N N 54  
ARG   NH2   HH21   sing N N 55  
ARG   NH2   HH22   sing N N 56  
ARG   OXT   HXT    sing N N 57  
ASN   N     CA     sing N N 58  
ASN   N     H      sing N N 59  
ASN   N     H2     sing N N 60  
ASN   CA    C      sing N N 61  
ASN   CA    CB     sing N N 62  
ASN   CA    HA     sing N N 63  
ASN   C     O      doub N N 64  
ASN   C     OXT    sing N N 65  
ASN   CB    CG     sing N N 66  
ASN   CB    HB2    sing N N 67  
ASN   CB    HB3    sing N N 68  
ASN   CG    OD1    doub N N 69  
ASN   CG    ND2    sing N N 70  
ASN   ND2   HD21   sing N N 71  
ASN   ND2   HD22   sing N N 72  
ASN   OXT   HXT    sing N N 73  
ASP   N     CA     sing N N 74  
ASP   N     H      sing N N 75  
ASP   N     H2     sing N N 76  
ASP   CA    C      sing N N 77  
ASP   CA    CB     sing N N 78  
ASP   CA    HA     sing N N 79  
ASP   C     O      doub N N 80  
ASP   C     OXT    sing N N 81  
ASP   CB    CG     sing N N 82  
ASP   CB    HB2    sing N N 83  
ASP   CB    HB3    sing N N 84  
ASP   CG    OD1    doub N N 85  
ASP   CG    OD2    sing N N 86  
ASP   OD2   HD2    sing N N 87  
ASP   OXT   HXT    sing N N 88  
CYS   N     CA     sing N N 89  
CYS   N     H      sing N N 90  
CYS   N     H2     sing N N 91  
CYS   CA    C      sing N N 92  
CYS   CA    CB     sing N N 93  
CYS   CA    HA     sing N N 94  
CYS   C     O      doub N N 95  
CYS   C     OXT    sing N N 96  
CYS   CB    SG     sing N N 97  
CYS   CB    HB2    sing N N 98  
CYS   CB    HB3    sing N N 99  
CYS   SG    HG     sing N N 100 
CYS   OXT   HXT    sing N N 101 
FAD   PA    O1A    doub N N 102 
FAD   PA    O2A    sing N N 103 
FAD   PA    O5B    sing N N 104 
FAD   PA    O3P    sing N N 105 
FAD   O2A   HOA2   sing N N 106 
FAD   O5B   C5B    sing N N 107 
FAD   C5B   C4B    sing N N 108 
FAD   C5B   H51A   sing N N 109 
FAD   C5B   H52A   sing N N 110 
FAD   C4B   O4B    sing N N 111 
FAD   C4B   C3B    sing N N 112 
FAD   C4B   H4B    sing N N 113 
FAD   O4B   C1B    sing N N 114 
FAD   C3B   O3B    sing N N 115 
FAD   C3B   C2B    sing N N 116 
FAD   C3B   H3B    sing N N 117 
FAD   O3B   HO3A   sing N N 118 
FAD   C2B   O2B    sing N N 119 
FAD   C2B   C1B    sing N N 120 
FAD   C2B   H2B    sing N N 121 
FAD   O2B   HO2A   sing N N 122 
FAD   C1B   N9A    sing N N 123 
FAD   C1B   H1B    sing N N 124 
FAD   N9A   C8A    sing Y N 125 
FAD   N9A   C4A    sing Y N 126 
FAD   C8A   N7A    doub Y N 127 
FAD   C8A   H8A    sing N N 128 
FAD   N7A   C5A    sing Y N 129 
FAD   C5A   C6A    sing Y N 130 
FAD   C5A   C4A    doub Y N 131 
FAD   C6A   N6A    sing N N 132 
FAD   C6A   N1A    doub Y N 133 
FAD   N6A   H61A   sing N N 134 
FAD   N6A   H62A   sing N N 135 
FAD   N1A   C2A    sing Y N 136 
FAD   C2A   N3A    doub Y N 137 
FAD   C2A   H2A    sing N N 138 
FAD   N3A   C4A    sing Y N 139 
FAD   N1    C2     sing N N 140 
FAD   N1    C10    doub N N 141 
FAD   C2    O2     doub N N 142 
FAD   C2    N3     sing N N 143 
FAD   N3    C4     sing N N 144 
FAD   N3    HN3    sing N N 145 
FAD   C4    O4     doub N N 146 
FAD   C4    C4X    sing N N 147 
FAD   C4X   N5     doub N N 148 
FAD   C4X   C10    sing N N 149 
FAD   N5    C5X    sing N N 150 
FAD   C5X   C6     doub Y N 151 
FAD   C5X   C9A    sing Y N 152 
FAD   C6    C7     sing Y N 153 
FAD   C6    H6     sing N N 154 
FAD   C7    C7M    sing N N 155 
FAD   C7    C8     doub Y N 156 
FAD   C7M   HM71   sing N N 157 
FAD   C7M   HM72   sing N N 158 
FAD   C7M   HM73   sing N N 159 
FAD   C8    C8M    sing N N 160 
FAD   C8    C9     sing Y N 161 
FAD   C8M   HM81   sing N N 162 
FAD   C8M   HM82   sing N N 163 
FAD   C8M   HM83   sing N N 164 
FAD   C9    C9A    doub Y N 165 
FAD   C9    H9     sing N N 166 
FAD   C9A   N10    sing N N 167 
FAD   N10   C10    sing N N 168 
FAD   N10   "C1'"  sing N N 169 
FAD   "C1'" "C2'"  sing N N 170 
FAD   "C1'" "H1'1" sing N N 171 
FAD   "C1'" "H1'2" sing N N 172 
FAD   "C2'" "O2'"  sing N N 173 
FAD   "C2'" "C3'"  sing N N 174 
FAD   "C2'" "H2'"  sing N N 175 
FAD   "O2'" "HO2'" sing N N 176 
FAD   "C3'" "O3'"  sing N N 177 
FAD   "C3'" "C4'"  sing N N 178 
FAD   "C3'" "H3'"  sing N N 179 
FAD   "O3'" "HO3'" sing N N 180 
FAD   "C4'" "O4'"  sing N N 181 
FAD   "C4'" "C5'"  sing N N 182 
FAD   "C4'" "H4'"  sing N N 183 
FAD   "O4'" "HO4'" sing N N 184 
FAD   "C5'" "O5'"  sing N N 185 
FAD   "C5'" "H5'1" sing N N 186 
FAD   "C5'" "H5'2" sing N N 187 
FAD   "O5'" P      sing N N 188 
FAD   P     O1P    doub N N 189 
FAD   P     O2P    sing N N 190 
FAD   P     O3P    sing N N 191 
FAD   O2P   HOP2   sing N N 192 
FMT   C     O1     doub N N 193 
FMT   C     O2     sing N N 194 
FMT   C     H      sing N N 195 
FMT   O2    HO2    sing N N 196 
GLN   N     CA     sing N N 197 
GLN   N     H      sing N N 198 
GLN   N     H2     sing N N 199 
GLN   CA    C      sing N N 200 
GLN   CA    CB     sing N N 201 
GLN   CA    HA     sing N N 202 
GLN   C     O      doub N N 203 
GLN   C     OXT    sing N N 204 
GLN   CB    CG     sing N N 205 
GLN   CB    HB2    sing N N 206 
GLN   CB    HB3    sing N N 207 
GLN   CG    CD     sing N N 208 
GLN   CG    HG2    sing N N 209 
GLN   CG    HG3    sing N N 210 
GLN   CD    OE1    doub N N 211 
GLN   CD    NE2    sing N N 212 
GLN   NE2   HE21   sing N N 213 
GLN   NE2   HE22   sing N N 214 
GLN   OXT   HXT    sing N N 215 
GLU   N     CA     sing N N 216 
GLU   N     H      sing N N 217 
GLU   N     H2     sing N N 218 
GLU   CA    C      sing N N 219 
GLU   CA    CB     sing N N 220 
GLU   CA    HA     sing N N 221 
GLU   C     O      doub N N 222 
GLU   C     OXT    sing N N 223 
GLU   CB    CG     sing N N 224 
GLU   CB    HB2    sing N N 225 
GLU   CB    HB3    sing N N 226 
GLU   CG    CD     sing N N 227 
GLU   CG    HG2    sing N N 228 
GLU   CG    HG3    sing N N 229 
GLU   CD    OE1    doub N N 230 
GLU   CD    OE2    sing N N 231 
GLU   OE2   HE2    sing N N 232 
GLU   OXT   HXT    sing N N 233 
GLY   N     CA     sing N N 234 
GLY   N     H      sing N N 235 
GLY   N     H2     sing N N 236 
GLY   CA    C      sing N N 237 
GLY   CA    HA2    sing N N 238 
GLY   CA    HA3    sing N N 239 
GLY   C     O      doub N N 240 
GLY   C     OXT    sing N N 241 
GLY   OXT   HXT    sing N N 242 
HIS   N     CA     sing N N 243 
HIS   N     H      sing N N 244 
HIS   N     H2     sing N N 245 
HIS   CA    C      sing N N 246 
HIS   CA    CB     sing N N 247 
HIS   CA    HA     sing N N 248 
HIS   C     O      doub N N 249 
HIS   C     OXT    sing N N 250 
HIS   CB    CG     sing N N 251 
HIS   CB    HB2    sing N N 252 
HIS   CB    HB3    sing N N 253 
HIS   CG    ND1    sing Y N 254 
HIS   CG    CD2    doub Y N 255 
HIS   ND1   CE1    doub Y N 256 
HIS   ND1   HD1    sing N N 257 
HIS   CD2   NE2    sing Y N 258 
HIS   CD2   HD2    sing N N 259 
HIS   CE1   NE2    sing Y N 260 
HIS   CE1   HE1    sing N N 261 
HIS   NE2   HE2    sing N N 262 
HIS   OXT   HXT    sing N N 263 
HOH   O     H1     sing N N 264 
HOH   O     H2     sing N N 265 
ILE   N     CA     sing N N 266 
ILE   N     H      sing N N 267 
ILE   N     H2     sing N N 268 
ILE   CA    C      sing N N 269 
ILE   CA    CB     sing N N 270 
ILE   CA    HA     sing N N 271 
ILE   C     O      doub N N 272 
ILE   C     OXT    sing N N 273 
ILE   CB    CG1    sing N N 274 
ILE   CB    CG2    sing N N 275 
ILE   CB    HB     sing N N 276 
ILE   CG1   CD1    sing N N 277 
ILE   CG1   HG12   sing N N 278 
ILE   CG1   HG13   sing N N 279 
ILE   CG2   HG21   sing N N 280 
ILE   CG2   HG22   sing N N 281 
ILE   CG2   HG23   sing N N 282 
ILE   CD1   HD11   sing N N 283 
ILE   CD1   HD12   sing N N 284 
ILE   CD1   HD13   sing N N 285 
ILE   OXT   HXT    sing N N 286 
LEU   N     CA     sing N N 287 
LEU   N     H      sing N N 288 
LEU   N     H2     sing N N 289 
LEU   CA    C      sing N N 290 
LEU   CA    CB     sing N N 291 
LEU   CA    HA     sing N N 292 
LEU   C     O      doub N N 293 
LEU   C     OXT    sing N N 294 
LEU   CB    CG     sing N N 295 
LEU   CB    HB2    sing N N 296 
LEU   CB    HB3    sing N N 297 
LEU   CG    CD1    sing N N 298 
LEU   CG    CD2    sing N N 299 
LEU   CG    HG     sing N N 300 
LEU   CD1   HD11   sing N N 301 
LEU   CD1   HD12   sing N N 302 
LEU   CD1   HD13   sing N N 303 
LEU   CD2   HD21   sing N N 304 
LEU   CD2   HD22   sing N N 305 
LEU   CD2   HD23   sing N N 306 
LEU   OXT   HXT    sing N N 307 
LYS   N     CA     sing N N 308 
LYS   N     H      sing N N 309 
LYS   N     H2     sing N N 310 
LYS   CA    C      sing N N 311 
LYS   CA    CB     sing N N 312 
LYS   CA    HA     sing N N 313 
LYS   C     O      doub N N 314 
LYS   C     OXT    sing N N 315 
LYS   CB    CG     sing N N 316 
LYS   CB    HB2    sing N N 317 
LYS   CB    HB3    sing N N 318 
LYS   CG    CD     sing N N 319 
LYS   CG    HG2    sing N N 320 
LYS   CG    HG3    sing N N 321 
LYS   CD    CE     sing N N 322 
LYS   CD    HD2    sing N N 323 
LYS   CD    HD3    sing N N 324 
LYS   CE    NZ     sing N N 325 
LYS   CE    HE2    sing N N 326 
LYS   CE    HE3    sing N N 327 
LYS   NZ    HZ1    sing N N 328 
LYS   NZ    HZ2    sing N N 329 
LYS   NZ    HZ3    sing N N 330 
LYS   OXT   HXT    sing N N 331 
MET   N     CA     sing N N 332 
MET   N     H      sing N N 333 
MET   N     H2     sing N N 334 
MET   CA    C      sing N N 335 
MET   CA    CB     sing N N 336 
MET   CA    HA     sing N N 337 
MET   C     O      doub N N 338 
MET   C     OXT    sing N N 339 
MET   CB    CG     sing N N 340 
MET   CB    HB2    sing N N 341 
MET   CB    HB3    sing N N 342 
MET   CG    SD     sing N N 343 
MET   CG    HG2    sing N N 344 
MET   CG    HG3    sing N N 345 
MET   SD    CE     sing N N 346 
MET   CE    HE1    sing N N 347 
MET   CE    HE2    sing N N 348 
MET   CE    HE3    sing N N 349 
MET   OXT   HXT    sing N N 350 
PEG   C1    O1     sing N N 351 
PEG   C1    C2     sing N N 352 
PEG   C1    H11    sing N N 353 
PEG   C1    H12    sing N N 354 
PEG   O1    HO1    sing N N 355 
PEG   C2    O2     sing N N 356 
PEG   C2    H21    sing N N 357 
PEG   C2    H22    sing N N 358 
PEG   O2    C3     sing N N 359 
PEG   C3    C4     sing N N 360 
PEG   C3    H31    sing N N 361 
PEG   C3    H32    sing N N 362 
PEG   C4    O4     sing N N 363 
PEG   C4    H41    sing N N 364 
PEG   C4    H42    sing N N 365 
PEG   O4    HO4    sing N N 366 
PG4   O1    C1     sing N N 367 
PG4   O1    HO1    sing N N 368 
PG4   C1    C2     sing N N 369 
PG4   C1    H11    sing N N 370 
PG4   C1    H12    sing N N 371 
PG4   C2    O2     sing N N 372 
PG4   C2    H21    sing N N 373 
PG4   C2    H22    sing N N 374 
PG4   O2    C3     sing N N 375 
PG4   C3    C4     sing N N 376 
PG4   C3    H31    sing N N 377 
PG4   C3    H32    sing N N 378 
PG4   C4    O3     sing N N 379 
PG4   C4    H41    sing N N 380 
PG4   C4    H42    sing N N 381 
PG4   O3    C5     sing N N 382 
PG4   C5    C6     sing N N 383 
PG4   C5    H51    sing N N 384 
PG4   C5    H52    sing N N 385 
PG4   C6    O4     sing N N 386 
PG4   C6    H61    sing N N 387 
PG4   C6    H62    sing N N 388 
PG4   O4    C7     sing N N 389 
PG4   C7    C8     sing N N 390 
PG4   C7    H71    sing N N 391 
PG4   C7    H72    sing N N 392 
PG4   C8    O5     sing N N 393 
PG4   C8    H81    sing N N 394 
PG4   C8    H82    sing N N 395 
PG4   O5    HO5    sing N N 396 
PGE   C1    O1     sing N N 397 
PGE   C1    C2     sing N N 398 
PGE   C1    H1     sing N N 399 
PGE   C1    H12    sing N N 400 
PGE   O1    HO1    sing N N 401 
PGE   C2    O2     sing N N 402 
PGE   C2    H2     sing N N 403 
PGE   C2    H22    sing N N 404 
PGE   O2    C3     sing N N 405 
PGE   C3    C4     sing N N 406 
PGE   C3    H3     sing N N 407 
PGE   C3    H32    sing N N 408 
PGE   C4    O3     sing N N 409 
PGE   C4    H4     sing N N 410 
PGE   C4    H42    sing N N 411 
PGE   O4    C6     sing N N 412 
PGE   O4    HO4    sing N N 413 
PGE   C6    C5     sing N N 414 
PGE   C6    H6     sing N N 415 
PGE   C6    H62    sing N N 416 
PGE   C5    O3     sing N N 417 
PGE   C5    H5     sing N N 418 
PGE   C5    H52    sing N N 419 
PHE   N     CA     sing N N 420 
PHE   N     H      sing N N 421 
PHE   N     H2     sing N N 422 
PHE   CA    C      sing N N 423 
PHE   CA    CB     sing N N 424 
PHE   CA    HA     sing N N 425 
PHE   C     O      doub N N 426 
PHE   C     OXT    sing N N 427 
PHE   CB    CG     sing N N 428 
PHE   CB    HB2    sing N N 429 
PHE   CB    HB3    sing N N 430 
PHE   CG    CD1    doub Y N 431 
PHE   CG    CD2    sing Y N 432 
PHE   CD1   CE1    sing Y N 433 
PHE   CD1   HD1    sing N N 434 
PHE   CD2   CE2    doub Y N 435 
PHE   CD2   HD2    sing N N 436 
PHE   CE1   CZ     doub Y N 437 
PHE   CE1   HE1    sing N N 438 
PHE   CE2   CZ     sing Y N 439 
PHE   CE2   HE2    sing N N 440 
PHE   CZ    HZ     sing N N 441 
PHE   OXT   HXT    sing N N 442 
PRO   N     CA     sing N N 443 
PRO   N     CD     sing N N 444 
PRO   N     H      sing N N 445 
PRO   CA    C      sing N N 446 
PRO   CA    CB     sing N N 447 
PRO   CA    HA     sing N N 448 
PRO   C     O      doub N N 449 
PRO   C     OXT    sing N N 450 
PRO   CB    CG     sing N N 451 
PRO   CB    HB2    sing N N 452 
PRO   CB    HB3    sing N N 453 
PRO   CG    CD     sing N N 454 
PRO   CG    HG2    sing N N 455 
PRO   CG    HG3    sing N N 456 
PRO   CD    HD2    sing N N 457 
PRO   CD    HD3    sing N N 458 
PRO   OXT   HXT    sing N N 459 
SER   N     CA     sing N N 460 
SER   N     H      sing N N 461 
SER   N     H2     sing N N 462 
SER   CA    C      sing N N 463 
SER   CA    CB     sing N N 464 
SER   CA    HA     sing N N 465 
SER   C     O      doub N N 466 
SER   C     OXT    sing N N 467 
SER   CB    OG     sing N N 468 
SER   CB    HB2    sing N N 469 
SER   CB    HB3    sing N N 470 
SER   OG    HG     sing N N 471 
SER   OXT   HXT    sing N N 472 
SO4   S     O1     doub N N 473 
SO4   S     O2     doub N N 474 
SO4   S     O3     sing N N 475 
SO4   S     O4     sing N N 476 
THR   N     CA     sing N N 477 
THR   N     H      sing N N 478 
THR   N     H2     sing N N 479 
THR   CA    C      sing N N 480 
THR   CA    CB     sing N N 481 
THR   CA    HA     sing N N 482 
THR   C     O      doub N N 483 
THR   C     OXT    sing N N 484 
THR   CB    OG1    sing N N 485 
THR   CB    CG2    sing N N 486 
THR   CB    HB     sing N N 487 
THR   OG1   HG1    sing N N 488 
THR   CG2   HG21   sing N N 489 
THR   CG2   HG22   sing N N 490 
THR   CG2   HG23   sing N N 491 
THR   OXT   HXT    sing N N 492 
TRP   N     CA     sing N N 493 
TRP   N     H      sing N N 494 
TRP   N     H2     sing N N 495 
TRP   CA    C      sing N N 496 
TRP   CA    CB     sing N N 497 
TRP   CA    HA     sing N N 498 
TRP   C     O      doub N N 499 
TRP   C     OXT    sing N N 500 
TRP   CB    CG     sing N N 501 
TRP   CB    HB2    sing N N 502 
TRP   CB    HB3    sing N N 503 
TRP   CG    CD1    doub Y N 504 
TRP   CG    CD2    sing Y N 505 
TRP   CD1   NE1    sing Y N 506 
TRP   CD1   HD1    sing N N 507 
TRP   CD2   CE2    doub Y N 508 
TRP   CD2   CE3    sing Y N 509 
TRP   NE1   CE2    sing Y N 510 
TRP   NE1   HE1    sing N N 511 
TRP   CE2   CZ2    sing Y N 512 
TRP   CE3   CZ3    doub Y N 513 
TRP   CE3   HE3    sing N N 514 
TRP   CZ2   CH2    doub Y N 515 
TRP   CZ2   HZ2    sing N N 516 
TRP   CZ3   CH2    sing Y N 517 
TRP   CZ3   HZ3    sing N N 518 
TRP   CH2   HH2    sing N N 519 
TRP   OXT   HXT    sing N N 520 
TYR   N     CA     sing N N 521 
TYR   N     H      sing N N 522 
TYR   N     H2     sing N N 523 
TYR   CA    C      sing N N 524 
TYR   CA    CB     sing N N 525 
TYR   CA    HA     sing N N 526 
TYR   C     O      doub N N 527 
TYR   C     OXT    sing N N 528 
TYR   CB    CG     sing N N 529 
TYR   CB    HB2    sing N N 530 
TYR   CB    HB3    sing N N 531 
TYR   CG    CD1    doub Y N 532 
TYR   CG    CD2    sing Y N 533 
TYR   CD1   CE1    sing Y N 534 
TYR   CD1   HD1    sing N N 535 
TYR   CD2   CE2    doub Y N 536 
TYR   CD2   HD2    sing N N 537 
TYR   CE1   CZ     doub Y N 538 
TYR   CE1   HE1    sing N N 539 
TYR   CE2   CZ     sing Y N 540 
TYR   CE2   HE2    sing N N 541 
TYR   CZ    OH     sing N N 542 
TYR   OH    HH     sing N N 543 
TYR   OXT   HXT    sing N N 544 
VAL   N     CA     sing N N 545 
VAL   N     H      sing N N 546 
VAL   N     H2     sing N N 547 
VAL   CA    C      sing N N 548 
VAL   CA    CB     sing N N 549 
VAL   CA    HA     sing N N 550 
VAL   C     O      doub N N 551 
VAL   C     OXT    sing N N 552 
VAL   CB    CG1    sing N N 553 
VAL   CB    CG2    sing N N 554 
VAL   CB    HB     sing N N 555 
VAL   CG1   HG11   sing N N 556 
VAL   CG1   HG12   sing N N 557 
VAL   CG1   HG13   sing N N 558 
VAL   CG2   HG21   sing N N 559 
VAL   CG2   HG22   sing N N 560 
VAL   CG2   HG23   sing N N 561 
VAL   OXT   HXT    sing N N 562 
# 
_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                    9DL5 
_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]   0.009946 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002910 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009893 
_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]   0.008285 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
O  
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     . ALA   A  1 16   ? -49.039 93.745  103.605 1.00 50.65 ? 14   ALA   A N     1 
ATOM   2     C  CA    . ALA   A  1 16   ? -48.029 92.726  103.886 1.00 46.72 ? 14   ALA   A CA    1 
ATOM   3     C  C     . ALA   A  1 16   ? -48.670 91.347  103.956 1.00 46.77 ? 14   ALA   A C     1 
ATOM   4     O  O     . ALA   A  1 16   ? -49.432 91.060  104.876 1.00 48.26 ? 14   ALA   A O     1 
ATOM   5     C  CB    . ALA   A  1 16   ? -47.290 93.040  105.190 1.00 45.01 ? 14   ALA   A CB    1 
ATOM   6     N  N     . PRO   A  1 17   ? -48.366 90.492  102.982 1.00 44.68 ? 15   PRO   A N     1 
ATOM   7     C  CA    . PRO   A  1 17   ? -48.946 89.146  102.987 1.00 37.75 ? 15   PRO   A CA    1 
ATOM   8     C  C     . PRO   A  1 17   ? -48.483 88.373  104.210 1.00 38.30 ? 15   PRO   A C     1 
ATOM   9     O  O     . PRO   A  1 17   ? -47.320 88.451  104.613 1.00 39.33 ? 15   PRO   A O     1 
ATOM   10    C  CB    . PRO   A  1 17   ? -48.420 88.525  101.688 1.00 37.37 ? 15   PRO   A CB    1 
ATOM   11    C  CG    . PRO   A  1 17   ? -47.961 89.693  100.853 1.00 38.73 ? 15   PRO   A CG    1 
ATOM   12    C  CD    . PRO   A  1 17   ? -47.472 90.705  101.833 1.00 40.25 ? 15   PRO   A CD    1 
ATOM   13    N  N     . ALA   A  1 18   ? -49.414 87.645  104.815 1.00 35.12 ? 16   ALA   A N     1 
ATOM   14    C  CA    . ALA   A  1 18   ? -49.087 86.872  106.002 1.00 33.95 ? 16   ALA   A CA    1 
ATOM   15    C  C     . ALA   A  1 18   ? -48.044 85.813  105.650 1.00 29.33 ? 16   ALA   A C     1 
ATOM   16    O  O     . ALA   A  1 18   ? -48.160 85.153  104.609 1.00 27.29 ? 16   ALA   A O     1 
ATOM   17    C  CB    . ALA   A  1 18   ? -50.345 86.216  106.566 1.00 29.33 ? 16   ALA   A CB    1 
ATOM   18    N  N     . PRO   A  1 19   ? -47.005 85.642  106.468 1.00 27.75 ? 17   PRO   A N     1 
ATOM   19    C  CA    . PRO   A  1 19   ? -45.932 84.709  106.102 1.00 24.26 ? 17   PRO   A CA    1 
ATOM   20    C  C     . PRO   A  1 19   ? -46.471 83.301  105.928 1.00 26.24 ? 17   PRO   A C     1 
ATOM   21    O  O     . PRO   A  1 19   ? -47.220 82.800  106.769 1.00 25.63 ? 17   PRO   A O     1 
ATOM   22    C  CB    . PRO   A  1 19   ? -44.961 84.798  107.285 1.00 27.56 ? 17   PRO   A CB    1 
ATOM   23    C  CG    . PRO   A  1 19   ? -45.228 86.127  107.886 1.00 28.57 ? 17   PRO   A CG    1 
ATOM   24    C  CD    . PRO   A  1 19   ? -46.715 86.331  107.735 1.00 29.41 ? 17   PRO   A CD    1 
ATOM   25    N  N     . PHE   A  1 20   ? -46.103 82.677  104.806 1.00 21.09 ? 18   PHE   A N     1 
ATOM   26    C  CA    . PHE   A  1 20   ? -46.399 81.284  104.499 1.00 21.76 ? 18   PHE   A CA    1 
ATOM   27    C  C     . PHE   A  1 20   ? -47.874 81.031  104.252 1.00 25.85 ? 18   PHE   A C     1 
ATOM   28    O  O     . PHE   A  1 20   ? -48.279 79.870  104.164 1.00 23.07 ? 18   PHE   A O     1 
ATOM   29    C  CB    . PHE   A  1 20   ? -45.913 80.340  105.607 1.00 20.35 ? 18   PHE   A CB    1 
ATOM   30    C  CG    . PHE   A  1 20   ? -44.439 80.392  105.828 1.00 20.27 ? 18   PHE   A CG    1 
ATOM   31    C  CD1   . PHE   A  1 20   ? -43.571 79.829  104.894 1.00 19.28 ? 18   PHE   A CD1   1 
ATOM   32    C  CD2   . PHE   A  1 20   ? -43.914 80.993  106.965 1.00 21.20 ? 18   PHE   A CD2   1 
ATOM   33    C  CE1   . PHE   A  1 20   ? -42.192 79.873  105.087 1.00 21.40 ? 18   PHE   A CE1   1 
ATOM   34    C  CE2   . PHE   A  1 20   ? -42.530 81.043  107.165 1.00 20.38 ? 18   PHE   A CE2   1 
ATOM   35    C  CZ    . PHE   A  1 20   ? -41.678 80.479  106.231 1.00 21.65 ? 18   PHE   A CZ    1 
ATOM   36    N  N     . ALA   A  1 21   ? -48.691 82.079  104.138 1.00 26.51 ? 19   ALA   A N     1 
ATOM   37    C  CA    . ALA   A  1 21   ? -50.110 81.866  103.886 1.00 28.39 ? 19   ALA   A CA    1 
ATOM   38    C  C     . ALA   A  1 21   ? -50.355 81.274  102.504 1.00 28.51 ? 19   ALA   A C     1 
ATOM   39    O  O     . ALA   A  1 21   ? -51.404 80.669  102.275 1.00 31.11 ? 19   ALA   A O     1 
ATOM   40    C  CB    . ALA   A  1 21   ? -50.878 83.176  104.061 1.00 29.54 ? 19   ALA   A CB    1 
ATOM   41    N  N     . ASP   A  1 22   ? -49.397 81.401  101.592 1.00 22.78 ? 20   ASP   A N     1 
ATOM   42    C  CA    . ASP   A  1 22   ? -49.516 80.857  100.245 1.00 28.07 ? 20   ASP   A CA    1 
ATOM   43    C  C     . ASP   A  1 22   ? -48.308 79.995  99.909  1.00 25.05 ? 20   ASP   A C     1 
ATOM   44    O  O     . ASP   A  1 22   ? -47.807 80.001  98.777  1.00 23.12 ? 20   ASP   A O     1 
ATOM   45    C  CB    . ASP   A  1 22   ? -49.684 81.983  99.232  1.00 26.72 ? 20   ASP   A CB    1 
ATOM   46    C  CG    . ASP   A  1 22   ? -50.916 82.826  99.514  1.00 39.65 ? 20   ASP   A CG    1 
ATOM   47    O  OD1   . ASP   A  1 22   ? -52.028 82.253  99.535  1.00 43.86 ? 20   ASP   A OD1   1 
ATOM   48    O  OD2   . ASP   A  1 22   ? -50.772 84.048  99.749  1.00 47.09 ? 20   ASP   A OD2   1 
ATOM   49    N  N     . PHE   A  1 23   ? -47.832 79.229  100.894 1.00 18.95 ? 21   PHE   A N     1 
ATOM   50    C  CA    . PHE   A  1 23   ? -46.564 78.528  100.736 1.00 18.45 ? 21   PHE   A CA    1 
ATOM   51    C  C     . PHE   A  1 23   ? -46.610 77.529  99.588  1.00 18.89 ? 21   PHE   A C     1 
ATOM   52    O  O     . PHE   A  1 23   ? -45.775 77.573  98.678  1.00 19.17 ? 21   PHE   A O     1 
ATOM   53    C  CB    . PHE   A  1 23   ? -46.170 77.816  102.026 1.00 18.05 ? 21   PHE   A CB    1 
ATOM   54    C  CG    . PHE   A  1 23   ? -44.911 77.016  101.869 1.00 17.73 ? 21   PHE   A CG    1 
ATOM   55    C  CD1   . PHE   A  1 23   ? -43.721 77.658  101.567 1.00 19.56 ? 21   PHE   A CD1   1 
ATOM   56    C  CD2   . PHE   A  1 23   ? -44.921 75.634  101.980 1.00 20.28 ? 21   PHE   A CD2   1 
ATOM   57    C  CE1   . PHE   A  1 23   ? -42.550 76.942  101.387 1.00 20.85 ? 21   PHE   A CE1   1 
ATOM   58    C  CE2   . PHE   A  1 23   ? -43.752 74.906  101.803 1.00 20.25 ? 21   PHE   A CE2   1 
ATOM   59    C  CZ    . PHE   A  1 23   ? -42.565 75.565  101.508 1.00 23.65 ? 21   PHE   A CZ    1 
ATOM   60    N  N     . ALA   A  1 24   ? -47.565 76.597  99.630  1.00 20.14 ? 22   ALA   A N     1 
ATOM   61    C  CA    . ALA   A  1 24   ? -47.644 75.564  98.600  1.00 21.47 ? 22   ALA   A CA    1 
ATOM   62    C  C     . ALA   A  1 24   ? -49.050 74.987  98.516  1.00 21.63 ? 22   ALA   A C     1 
ATOM   63    O  O     . ALA   A  1 24   ? -49.243 73.773  98.681  1.00 19.42 ? 22   ALA   A O     1 
ATOM   64    C  CB    . ALA   A  1 24   ? -46.640 74.447  98.881  1.00 20.38 ? 22   ALA   A CB    1 
ATOM   65    N  N     . PRO   A  1 25   ? -50.055 75.813  98.249  1.00 23.51 ? 23   PRO   A N     1 
ATOM   66    C  CA    . PRO   A  1 25   ? -51.418 75.296  98.129  1.00 22.89 ? 23   PRO   A CA    1 
ATOM   67    C  C     . PRO   A  1 25   ? -51.496 74.279  97.006  1.00 20.55 ? 23   PRO   A C     1 
ATOM   68    O  O     . PRO   A  1 25   ? -50.908 74.481  95.933  1.00 22.05 ? 23   PRO   A O     1 
ATOM   69    C  CB    . PRO   A  1 25   ? -52.243 76.551  97.814  1.00 22.90 ? 23   PRO   A CB    1 
ATOM   70    C  CG    . PRO   A  1 25   ? -51.294 77.456  97.152  1.00 27.41 ? 23   PRO   A CG    1 
ATOM   71    C  CD    . PRO   A  1 25   ? -49.972 77.231  97.861  1.00 22.67 ? 23   PRO   A CD    1 
ATOM   72    N  N     . PRO   A  1 26   ? -52.177 73.160  97.225  1.00 20.72 ? 24   PRO   A N     1 
ATOM   73    C  CA    . PRO   A  1 26   ? -52.278 72.141  96.176  1.00 21.25 ? 24   PRO   A CA    1 
ATOM   74    C  C     . PRO   A  1 26   ? -53.133 72.628  95.020  1.00 20.28 ? 24   PRO   A C     1 
ATOM   75    O  O     . PRO   A  1 26   ? -53.921 73.566  95.147  1.00 20.58 ? 24   PRO   A O     1 
ATOM   76    C  CB    . PRO   A  1 26   ? -52.933 70.959  96.896  1.00 23.96 ? 24   PRO   A CB    1 
ATOM   77    C  CG    . PRO   A  1 26   ? -53.747 71.617  97.971  1.00 23.56 ? 24   PRO   A CG    1 
ATOM   78    C  CD    . PRO   A  1 26   ? -52.913 72.778  98.439  1.00 22.65 ? 24   PRO   A CD    1 
ATOM   79    N  N     . VAL   A  1 27   ? -52.953 71.976  93.867  1.00 19.57 ? 25   VAL   A N     1 
ATOM   80    C  CA    . VAL   A  1 27   ? -53.719 72.348  92.676  1.00 21.67 ? 25   VAL   A CA    1 
ATOM   81    C  C     . VAL   A  1 27   ? -55.207 72.169  92.932  1.00 22.37 ? 25   VAL   A C     1 
ATOM   82    O  O     . VAL   A  1 27   ? -56.033 72.969  92.473  1.00 23.33 ? 25   VAL   A O     1 
ATOM   83    C  CB    . VAL   A  1 27   ? -53.244 71.537  91.457  1.00 26.41 ? 25   VAL   A CB    1 
ATOM   84    C  CG1   . VAL   A  1 27   ? -54.135 71.808  90.243  1.00 21.36 ? 25   VAL   A CG1   1 
ATOM   85    C  CG2   . VAL   A  1 27   ? -51.801 71.900  91.131  1.00 22.73 ? 25   VAL   A CG2   1 
ATOM   86    N  N     . ARG   A  1 28   ? -55.569 71.154  93.705  1.00 21.07 ? 26   ARG   A N     1 
ATOM   87    C  CA    . ARG   A  1 28   ? -56.959 70.936  94.070  1.00 23.96 ? 26   ARG   A CA    1 
ATOM   88    C  C     . ARG   A  1 28   ? -56.998 70.225  95.413  1.00 26.42 ? 26   ARG   A C     1 
ATOM   89    O  O     . ARG   A  1 28   ? -56.001 69.620  95.828  1.00 22.12 ? 26   ARG   A O     1 
ATOM   90    C  CB    . ARG   A  1 28   ? -57.679 70.104  93.002  1.00 26.07 ? 26   ARG   A CB    1 
ATOM   91    C  CG    . ARG   A  1 28   ? -57.159 68.675  92.937  1.00 28.21 ? 26   ARG   A CG    1 
ATOM   92    C  CD    . ARG   A  1 28   ? -57.772 67.890  91.798  1.00 32.15 ? 26   ARG   A CD    1 
ATOM   93    N  NE    . ARG   A  1 28   ? -57.031 68.109  90.563  1.00 37.00 ? 26   ARG   A NE    1 
ATOM   94    C  CZ    . ARG   A  1 28   ? -57.490 68.795  89.529  1.00 36.24 ? 26   ARG   A CZ    1 
ATOM   95    N  NH1   . ARG   A  1 28   ? -58.720 69.292  89.518  1.00 39.52 ? 26   ARG   A NH1   1 
ATOM   96    N  NH2   . ARG   A  1 28   ? -56.700 68.982  88.478  1.00 33.59 ? 26   ARG   A NH2   1 
ATOM   97    N  N     . PRO   A  1 29   ? -58.134 70.273  96.118  1.00 27.43 ? 27   PRO   A N     1 
ATOM   98    C  CA    . PRO   A  1 29   ? -58.272 69.454  97.326  1.00 27.27 ? 27   PRO   A CA    1 
ATOM   99    C  C     . PRO   A  1 29   ? -58.042 67.990  96.990  1.00 21.17 ? 27   PRO   A C     1 
ATOM   100   O  O     . PRO   A  1 29   ? -58.495 67.493  95.957  1.00 25.09 ? 27   PRO   A O     1 
ATOM   101   C  CB    . PRO   A  1 29   ? -59.716 69.714  97.778  1.00 26.12 ? 27   PRO   A CB    1 
ATOM   102   C  CG    . PRO   A  1 29   ? -60.059 71.045  97.190  1.00 27.65 ? 27   PRO   A CG    1 
ATOM   103   C  CD    . PRO   A  1 29   ? -59.333 71.099  95.874  1.00 27.28 ? 27   PRO   A CD    1 
ATOM   104   N  N     . GLN   A  1 30   ? -57.318 67.308  97.872  1.00 23.29 ? 28   GLN   A N     1 
ATOM   105   C  CA    . GLN   A  1 30   ? -56.891 65.936  97.634  1.00 23.79 ? 28   GLN   A CA    1 
ATOM   106   C  C     . GLN   A  1 30   ? -58.037 64.995  97.975  1.00 24.53 ? 28   GLN   A C     1 
ATOM   107   O  O     . GLN   A  1 30   ? -58.441 64.890  99.135  1.00 24.57 ? 28   GLN   A O     1 
ATOM   108   C  CB    . GLN   A  1 30   ? -55.650 65.623  98.463  1.00 22.16 ? 28   GLN   A CB    1 
ATOM   109   C  CG    . GLN   A  1 30   ? -54.470 66.553  98.160  1.00 21.38 ? 28   GLN   A CG    1 
ATOM   110   C  CD    . GLN   A  1 30   ? -53.985 66.394  96.725  1.00 23.78 ? 28   GLN   A CD    1 
ATOM   111   O  OE1   . GLN   A  1 30   ? -53.244 65.455  96.405  1.00 22.59 ? 28   GLN   A OE1   1 
ATOM   112   N  NE2   . GLN   A  1 30   ? -54.401 67.309  95.853  1.00 22.21 ? 28   GLN   A NE2   1 
ATOM   113   N  N     . SER   A  1 31   ? -58.567 64.322  96.960  1.00 22.92 ? 29   SER   A N     1 
ATOM   114   C  CA    . SER   A  1 31   ? -59.611 63.334  97.156  1.00 24.89 ? 29   SER   A CA    1 
ATOM   115   C  C     . SER   A  1 31   ? -59.077 62.141  97.952  1.00 22.61 ? 29   SER   A C     1 
ATOM   116   O  O     . SER   A  1 31   ? -57.873 61.978  98.158  1.00 23.10 ? 29   SER   A O     1 
ATOM   117   C  CB    . SER   A  1 31   ? -60.155 62.876  95.806  1.00 21.78 ? 29   SER   A CB    1 
ATOM   118   O  OG    . SER   A  1 31   ? -59.224 62.021  95.159  1.00 22.87 ? 29   SER   A OG    1 
ATOM   119   N  N     . THR   A  1 32   ? -60.006 61.306  98.420  1.00 20.39 ? 30   THR   A N     1 
ATOM   120   C  CA    . THR   A  1 32   ? -59.622 60.062  99.073  1.00 20.31 ? 30   THR   A CA    1 
ATOM   121   C  C     . THR   A  1 32   ? -58.670 59.259  98.199  1.00 21.70 ? 30   THR   A C     1 
ATOM   122   O  O     . THR   A  1 32   ? -57.658 58.737  98.681  1.00 20.01 ? 30   THR   A O     1 
ATOM   123   C  CB    . THR   A  1 32   ? -60.874 59.246  99.388  1.00 26.22 ? 30   THR   A CB    1 
ATOM   124   O  OG1   . THR   A  1 32   ? -61.708 60.013  100.259 1.00 28.89 ? 30   THR   A OG1   1 
ATOM   125   C  CG2   . THR   A  1 32   ? -60.502 57.940  100.070 1.00 27.88 ? 30   THR   A CG2   1 
ATOM   126   N  N     . LEU   A  1 33   ? -58.983 59.153  96.907  1.00 19.04 ? 31   LEU   A N     1 
ATOM   127   C  CA    . LEU   A  1 33   ? -58.139 58.382  96.008  1.00 21.86 ? 31   LEU   A CA    1 
ATOM   128   C  C     . LEU   A  1 33   ? -56.776 59.034  95.838  1.00 21.88 ? 31   LEU   A C     1 
ATOM   129   O  O     . LEU   A  1 33   ? -55.760 58.337  95.761  1.00 19.00 ? 31   LEU   A O     1 
ATOM   130   C  CB    . LEU   A  1 33   ? -58.825 58.221  94.664  1.00 22.59 ? 31   LEU   A CB    1 
ATOM   131   C  CG    . LEU   A  1 33   ? -59.995 57.242  94.678  1.00 25.07 ? 31   LEU   A CG    1 
ATOM   132   C  CD1   . LEU   A  1 33   ? -60.765 57.407  93.400  1.00 24.55 ? 31   LEU   A CD1   1 
ATOM   133   C  CD2   . LEU   A  1 33   ? -59.491 55.816  94.834  1.00 24.86 ? 31   LEU   A CD2   1 
ATOM   134   N  N     . ARG   A  1 34   ? -56.735 60.369  95.774  1.00 19.21 ? 32   ARG   A N     1 
ATOM   135   C  CA    . ARG   A  1 34   ? -55.446 61.050  95.673  1.00 18.54 ? 32   ARG   A CA    1 
ATOM   136   C  C     . ARG   A  1 34   ? -54.630 60.877  96.946  1.00 20.96 ? 32   ARG   A C     1 
ATOM   137   O  O     . ARG   A  1 34   ? -53.410 60.698  96.883  1.00 19.71 ? 32   ARG   A O     1 
ATOM   138   C  CB    . ARG   A  1 34   ? -55.652 62.537  95.367  1.00 20.14 ? 32   ARG   A CB    1 
ATOM   139   C  CG    . ARG   A  1 34   ? -56.119 62.817  93.941  1.00 21.25 ? 32   ARG   A CG    1 
ATOM   140   C  CD    . ARG   A  1 34   ? -55.010 62.559  92.901  1.00 21.59 ? 32   ARG   A CD    1 
ATOM   141   N  NE    . ARG   A  1 34   ? -53.879 63.473  93.038  1.00 21.97 ? 32   ARG   A NE    1 
ATOM   142   C  CZ    . ARG   A  1 34   ? -53.759 64.635  92.404  1.00 23.51 ? 32   ARG   A CZ    1 
ATOM   143   N  NH1   . ARG   A  1 34   ? -54.685 65.064  91.558  1.00 24.34 ? 32   ARG   A NH1   1 
ATOM   144   N  NH2   . ARG   A  1 34   ? -52.684 65.390  92.627  1.00 21.56 ? 32   ARG   A NH2   1 
ATOM   145   N  N     . ARG   A  1 35   ? -55.280 60.938  98.118  1.00 17.71 ? 33   ARG   A N     1 
ATOM   146   C  CA    . ARG   A  1 35   ? -54.532 60.779  99.358  1.00 19.19 ? 33   ARG   A CA    1 
ATOM   147   C  C     . ARG   A  1 35   ? -53.970 59.372  99.489  1.00 22.27 ? 33   ARG   A C     1 
ATOM   148   O  O     . ARG   A  1 35   ? -52.913 59.187  100.104 1.00 20.80 ? 33   ARG   A O     1 
ATOM   149   C  CB    . ARG   A  1 35   ? -55.409 61.117  100.563 1.00 21.62 ? 33   ARG   A CB    1 
ATOM   150   C  CG    . ARG   A  1 35   ? -55.824 62.583  100.633 1.00 24.57 ? 33   ARG   A CG    1 
ATOM   151   C  CD    . ARG   A  1 35   ? -56.396 62.930  102.011 1.00 33.89 ? 33   ARG   A CD    1 
ATOM   152   N  NE    . ARG   A  1 35   ? -55.312 63.134  102.971 1.00 43.86 ? 33   ARG   A NE    1 
ATOM   153   C  CZ    . ARG   A  1 35   ? -55.474 63.388  104.264 1.00 44.99 ? 33   ARG   A CZ    1 
ATOM   154   N  NH1   . ARG   A  1 35   ? -56.678 63.465  104.811 1.00 42.51 ? 33   ARG   A NH1   1 
ATOM   155   N  NH2   . ARG   A  1 35   ? -54.398 63.560  105.030 1.00 42.28 ? 33   ARG   A NH2   1 
ATOM   156   N  N     . ALA   A  1 36   ? -54.660 58.373  98.928  1.00 18.36 ? 34   ALA   A N     1 
ATOM   157   C  CA    . ALA   A  1 36   ? -54.157 57.006  98.997  1.00 20.69 ? 34   ALA   A CA    1 
ATOM   158   C  C     . ALA   A  1 36   ? -52.901 56.854  98.158  1.00 20.47 ? 34   ALA   A C     1 
ATOM   159   O  O     . ALA   A  1 36   ? -51.995 56.086  98.513  1.00 19.01 ? 34   ALA   A O     1 
ATOM   160   C  CB    . ALA   A  1 36   ? -55.234 56.022  98.535  1.00 20.54 ? 34   ALA   A CB    1 
ATOM   161   N  N     . ILE   A  1 37   ? -52.834 57.582  97.043  1.00 18.31 ? 35   ILE   A N     1 
ATOM   162   C  CA    . ILE   A  1 37   ? -51.608 57.627  96.261  1.00 18.18 ? 35   ILE   A CA    1 
ATOM   163   C  C     . ILE   A  1 37   ? -50.470 58.203  97.096  1.00 17.74 ? 35   ILE   A C     1 
ATOM   164   O  O     . ILE   A  1 37   ? -49.410 57.582  97.252  1.00 17.72 ? 35   ILE   A O     1 
ATOM   165   C  CB    . ILE   A  1 37   ? -51.845 58.437  94.973  1.00 18.02 ? 35   ILE   A CB    1 
ATOM   166   C  CG1   . ILE   A  1 37   ? -52.804 57.675  94.058  1.00 18.38 ? 35   ILE   A CG1   1 
ATOM   167   C  CG2   . ILE   A  1 37   ? -50.532 58.732  94.267  1.00 16.62 ? 35   ILE   A CG2   1 
ATOM   168   C  CD1   . ILE   A  1 37   ? -53.293 58.491  92.889  1.00 18.40 ? 35   ILE   A CD1   1 
ATOM   169   N  N     . THR   A  1 38   ? -50.685 59.389  97.671  1.00 17.00 ? 36   THR   A N     1 
ATOM   170   C  CA    . THR   A  1 38   ? -49.619 60.062  98.405  1.00 19.80 ? 36   THR   A CA    1 
ATOM   171   C  C     . THR   A  1 38   ? -49.157 59.225  99.590  1.00 19.06 ? 36   THR   A C     1 
ATOM   172   O  O     . THR   A  1 38   ? -47.958 59.163  99.886  1.00 18.97 ? 36   THR   A O     1 
ATOM   173   C  CB    . THR   A  1 38   ? -50.098 61.440  98.869  1.00 18.92 ? 36   THR   A CB    1 
ATOM   174   O  OG1   . THR   A  1 38   ? -50.700 62.129  97.765  1.00 19.44 ? 36   THR   A OG1   1 
ATOM   175   C  CG2   . THR   A  1 38   ? -48.933 62.260  99.380  1.00 19.36 ? 36   THR   A CG2   1 
ATOM   176   N  N     . ALA   A  1 39   ? -50.092 58.547  100.263 1.00 17.39 ? 37   ALA   A N     1 
ATOM   177   C  CA    . ALA   A  1 39   ? -49.725 57.733  101.416 1.00 19.72 ? 37   ALA   A CA    1 
ATOM   178   C  C     . ALA   A  1 39   ? -48.754 56.619  101.045 1.00 20.18 ? 37   ALA   A C     1 
ATOM   179   O  O     . ALA   A  1 39   ? -47.950 56.203  101.884 1.00 19.79 ? 37   ALA   A O     1 
ATOM   180   C  CB    . ALA   A  1 39   ? -50.977 57.143  102.071 1.00 21.08 ? 37   ALA   A CB    1 
ATOM   181   N  N     . ALA   A  1 40   ? -48.811 56.126  99.804  1.00 18.65 ? 38   ALA   A N     1 
ATOM   182   C  CA    . ALA   A  1 40   ? -47.970 55.030  99.332  1.00 18.97 ? 38   ALA   A CA    1 
ATOM   183   C  C     . ALA   A  1 40   ? -46.599 55.481  98.836  1.00 18.33 ? 38   ALA   A C     1 
ATOM   184   O  O     . ALA   A  1 40   ? -45.751 54.623  98.572  1.00 20.08 ? 38   ALA   A O     1 
ATOM   185   C  CB    . ALA   A  1 40   ? -48.689 54.282  98.199  1.00 18.44 ? 38   ALA   A CB    1 
ATOM   186   N  N     . TYR   A  1 41   ? -46.376 56.793  98.704  1.00 17.89 ? 39   TYR   A N     1 
ATOM   187   C  CA    . TYR   A  1 41   ? -45.186 57.346  98.050  1.00 17.47 ? 39   TYR   A CA    1 
ATOM   188   C  C     . TYR   A  1 41   ? -43.905 56.621  98.450  1.00 18.23 ? 39   TYR   A C     1 
ATOM   189   O  O     . TYR   A  1 41   ? -43.153 56.152  97.595  1.00 19.79 ? 39   TYR   A O     1 
ATOM   190   C  CB    . TYR   A  1 41   ? -45.098 58.837  98.395  1.00 17.53 ? 39   TYR   A CB    1 
ATOM   191   C  CG    . TYR   A  1 41   ? -44.356 59.735  97.416  1.00 17.25 ? 39   TYR   A CG    1 
ATOM   192   C  CD1   . TYR   A  1 41   ? -43.294 59.265  96.654  1.00 17.12 ? 39   TYR   A CD1   1 
ATOM   193   C  CD2   . TYR   A  1 41   ? -44.731 61.062  97.269  1.00 18.25 ? 39   TYR   A CD2   1 
ATOM   194   C  CE1   . TYR   A  1 41   ? -42.623 60.101  95.789  1.00 17.74 ? 39   TYR   A CE1   1 
ATOM   195   C  CE2   . TYR   A  1 41   ? -44.073 61.908  96.403  1.00 17.77 ? 39   TYR   A CE2   1 
ATOM   196   C  CZ    . TYR   A  1 41   ? -43.027 61.419  95.656  1.00 18.49 ? 39   TYR   A CZ    1 
ATOM   197   O  OH    . TYR   A  1 41   ? -42.363 62.257  94.779  1.00 17.27 ? 39   TYR   A OH    1 
ATOM   198   N  N     . ARG   A  1 42   ? -43.646 56.512  99.749  1.00 18.94 ? 40   ARG   A N     1 
ATOM   199   C  CA    . ARG   A  1 42   ? -42.418 55.901  100.244 1.00 16.73 ? 40   ARG   A CA    1 
ATOM   200   C  C     . ARG   A  1 42   ? -42.715 54.786  101.232 1.00 21.14 ? 40   ARG   A C     1 
ATOM   201   O  O     . ARG   A  1 42   ? -41.943 54.542  102.167 1.00 20.91 ? 40   ARG   A O     1 
ATOM   202   C  CB    . ARG   A  1 42   ? -41.508 56.966  100.852 1.00 18.91 ? 40   ARG   A CB    1 
ATOM   203   C  CG    . ARG   A  1 42   ? -41.051 57.921  99.765  1.00 18.54 ? 40   ARG   A CG    1 
ATOM   204   C  CD    . ARG   A  1 42   ? -40.220 59.079  100.231 1.00 22.44 ? 40   ARG   A CD    1 
ATOM   205   N  NE    . ARG   A  1 42   ? -40.239 60.113  99.201  1.00 18.84 ? 40   ARG   A NE    1 
ATOM   206   C  CZ    . ARG   A  1 42   ? -39.445 60.142  98.137  1.00 20.77 ? 40   ARG   A CZ    1 
ATOM   207   N  NH1   . ARG   A  1 42   ? -38.477 59.248  97.964  1.00 19.56 ? 40   ARG   A NH1   1 
ATOM   208   N  NH2   . ARG   A  1 42   ? -39.626 61.093  97.221  1.00 18.08 ? 40   ARG   A NH2   1 
ATOM   209   N  N     . ARG   A  1 43   ? -43.820 54.089  101.014 1.00 20.65 ? 41   ARG   A N     1 
ATOM   210   C  CA    . ARG   A  1 43   ? -44.211 53.004  101.897 1.00 21.44 ? 41   ARG   A CA    1 
ATOM   211   C  C     . ARG   A  1 43   ? -43.116 51.941  101.926 1.00 21.84 ? 41   ARG   A C     1 
ATOM   212   O  O     . ARG   A  1 43   ? -42.560 51.600  100.878 1.00 20.23 ? 41   ARG   A O     1 
ATOM   213   C  CB    . ARG   A  1 43   ? -45.528 52.396  101.419 1.00 20.15 ? 41   ARG   A CB    1 
ATOM   214   C  CG    . ARG   A  1 43   ? -46.036 51.211  102.239 1.00 20.62 ? 41   ARG   A CG    1 
ATOM   215   C  CD    . ARG   A  1 43   ? -47.475 50.943  101.876 1.00 23.60 ? 41   ARG   A CD    1 
ATOM   216   N  NE    . ARG   A  1 43   ? -48.325 52.064  102.258 1.00 23.35 ? 41   ARG   A NE    1 
ATOM   217   C  CZ    . ARG   A  1 43   ? -49.419 52.430  101.607 1.00 21.50 ? 41   ARG   A CZ    1 
ATOM   218   N  NH1   . ARG   A  1 43   ? -49.838 51.773  100.541 1.00 22.79 ? 41   ARG   A NH1   1 
ATOM   219   N  NH2   . ARG   A  1 43   ? -50.104 53.490  102.032 1.00 24.84 ? 41   ARG   A NH2   1 
ATOM   220   N  N     . PRO   A  1 44   ? -42.778 51.410  103.100 1.00 22.73 ? 42   PRO   A N     1 
ATOM   221   C  CA    . PRO   A  1 44   ? -41.743 50.373  103.175 1.00 24.69 ? 42   PRO   A CA    1 
ATOM   222   C  C     . PRO   A  1 44   ? -42.031 49.225  102.222 1.00 22.28 ? 42   PRO   A C     1 
ATOM   223   O  O     . PRO   A  1 44   ? -43.182 48.846  101.994 1.00 22.45 ? 42   PRO   A O     1 
ATOM   224   C  CB    . PRO   A  1 44   ? -41.804 49.918  104.639 1.00 25.37 ? 42   PRO   A CB    1 
ATOM   225   C  CG    . PRO   A  1 44   ? -42.322 51.112  105.370 1.00 25.03 ? 42   PRO   A CG    1 
ATOM   226   C  CD    . PRO   A  1 44   ? -43.290 51.783  104.432 1.00 25.26 ? 42   PRO   A CD    1 
ATOM   227   N  N     . GLU   A  1 45   ? -40.957 48.676  101.657 1.00 27.57 ? 43   GLU   A N     1 
ATOM   228   C  CA    . GLU   A  1 45   ? -41.100 47.654  100.628 1.00 22.98 ? 43   GLU   A CA    1 
ATOM   229   C  C     . GLU   A  1 45   ? -41.786 46.406  101.174 1.00 22.90 ? 43   GLU   A C     1 
ATOM   230   O  O     . GLU   A  1 45   ? -42.583 45.771  100.475 1.00 23.72 ? 43   GLU   A O     1 
ATOM   231   C  CB    . GLU   A  1 45   ? -39.714 47.341  100.053 1.00 26.26 ? 43   GLU   A CB    1 
ATOM   232   C  CG    . GLU   A  1 45   ? -39.729 46.849  98.619  1.00 27.00 ? 43   GLU   A CG    1 
ATOM   233   C  CD    . GLU   A  1 45   ? -38.439 47.150  97.852  1.00 21.56 ? 43   GLU   A CD    1 
ATOM   234   O  OE1   . GLU   A  1 45   ? -37.572 47.901  98.352  1.00 23.81 ? 43   GLU   A OE1   1 
ATOM   235   O  OE2   . GLU   A  1 45   ? -38.306 46.616  96.729  1.00 23.83 ? 43   GLU   A OE2   1 
ATOM   236   N  N     . THR   A  1 46   ? -41.511 46.055  102.437 1.00 22.78 ? 44   THR   A N     1 
ATOM   237   C  CA    . THR   A  1 46   ? -42.146 44.896  103.059 1.00 24.98 ? 44   THR   A CA    1 
ATOM   238   C  C     . THR   A  1 46   ? -43.646 45.072  103.217 1.00 26.33 ? 44   THR   A C     1 
ATOM   239   O  O     . THR   A  1 46   ? -44.367 44.079  103.328 1.00 29.84 ? 44   THR   A O     1 
ATOM   240   C  CB    . THR   A  1 46   ? -41.537 44.620  104.434 1.00 25.24 ? 44   THR   A CB    1 
ATOM   241   O  OG1   . THR   A  1 46   ? -41.571 45.823  105.217 1.00 24.28 ? 44   THR   A OG1   1 
ATOM   242   C  CG2   . THR   A  1 46   ? -40.102 44.146  104.287 1.00 25.54 ? 44   THR   A CG2   1 
ATOM   243   N  N     . GLU   A  1 47   ? -44.128 46.304  103.244 1.00 24.41 ? 45   GLU   A N     1 
ATOM   244   C  CA    . GLU   A  1 47   ? -45.559 46.554  103.311 1.00 23.84 ? 45   GLU   A CA    1 
ATOM   245   C  C     . GLU   A  1 47   ? -46.199 46.627  101.935 1.00 24.47 ? 45   GLU   A C     1 
ATOM   246   O  O     . GLU   A  1 47   ? -47.374 46.286  101.794 1.00 24.47 ? 45   GLU   A O     1 
ATOM   247   C  CB    . GLU   A  1 47   ? -45.817 47.847  104.083 1.00 25.76 ? 45   GLU   A CB    1 
ATOM   248   C  CG    . GLU   A  1 47   ? -45.262 47.786  105.498 1.00 31.01 ? 45   GLU   A CG    1 
ATOM   249   C  CD    . GLU   A  1 47   ? -45.398 49.096  106.240 1.00 36.10 ? 45   GLU   A CD    1 
ATOM   250   O  OE1   . GLU   A  1 47   ? -46.170 49.961  105.777 1.00 35.27 ? 45   GLU   A OE1   1 
ATOM   251   O  OE2   . GLU   A  1 47   ? -44.732 49.255  107.286 1.00 43.10 ? 45   GLU   A OE2   1 
ATOM   252   N  N     . CYS   A  1 48   ? -45.446 47.038  100.910 1.00 21.60 ? 46   CYS   A N     1 
ATOM   253   C  CA    . CYS   A  1 48   ? -46.013 47.111  99.563  1.00 22.38 ? 46   CYS   A CA    1 
ATOM   254   C  C     . CYS   A  1 48   ? -46.227 45.724  98.969  1.00 22.57 ? 46   CYS   A C     1 
ATOM   255   O  O     . CYS   A  1 48   ? -47.217 45.485  98.265  1.00 20.82 ? 46   CYS   A O     1 
ATOM   256   C  CB    . CYS   A  1 48   ? -45.095 47.910  98.635  1.00 23.01 ? 46   CYS   A CB    1 
ATOM   257   S  SG    . CYS   A  1 48   ? -44.869 49.632  99.056  1.00 24.73 ? 46   CYS   A SG    1 
ATOM   258   N  N     . LEU   A  1 49   ? -45.302 44.804  99.220  1.00 23.52 ? 47   LEU   A N     1 
ATOM   259   C  CA    . LEU   A  1 49   ? -45.277 43.587  98.415  1.00 24.67 ? 47   LEU   A CA    1 
ATOM   260   C  C     . LEU   A  1 49   ? -46.388 42.581  98.720  1.00 23.60 ? 47   LEU   A C     1 
ATOM   261   O  O     . LEU   A  1 49   ? -46.921 41.994  97.773  1.00 26.03 ? 47   LEU   A O     1 
ATOM   262   C  CB    . LEU   A  1 49   ? -43.907 42.908  98.524  1.00 24.82 ? 47   LEU   A CB    1 
ATOM   263   C  CG    . LEU   A  1 49   ? -42.949 43.238  97.369  1.00 26.57 ? 47   LEU   A CG    1 
ATOM   264   C  CD1   . LEU   A  1 49   ? -43.449 42.660  96.051  1.00 25.96 ? 47   LEU   A CD1   1 
ATOM   265   C  CD2   . LEU   A  1 49   ? -42.743 44.738  97.220  1.00 22.95 ? 47   LEU   A CD2   1 
ATOM   266   N  N     . PRO   A  1 50   ? -46.784 42.338  99.975  1.00 26.23 ? 48   PRO   A N     1 
ATOM   267   C  CA    . PRO   A  1 50   ? -47.804 41.296  100.229 1.00 25.36 ? 48   PRO   A CA    1 
ATOM   268   C  C     . PRO   A  1 50   ? -49.090 41.516  99.445  1.00 23.98 ? 48   PRO   A C     1 
ATOM   269   O  O     . PRO   A  1 50   ? -49.583 40.566  98.813  1.00 26.37 ? 48   PRO   A O     1 
ATOM   270   C  CB    . PRO   A  1 50   ? -48.025 41.378  101.746 1.00 27.53 ? 48   PRO   A CB    1 
ATOM   271   C  CG    . PRO   A  1 50   ? -46.659 41.731  102.261 1.00 25.13 ? 48   PRO   A CG    1 
ATOM   272   C  CD    . PRO   A  1 50   ? -46.171 42.780  101.245 1.00 26.54 ? 48   PRO   A CD    1 
ATOM   273   N  N     . PRO   A  1 51   ? -49.678 42.727  99.436  1.00 25.71 ? 49   PRO   A N     1 
ATOM   274   C  CA    . PRO   A  1 51   ? -50.895 42.901  98.625  1.00 25.58 ? 49   PRO   A CA    1 
ATOM   275   C  C     . PRO   A  1 51   ? -50.651 42.725  97.138  1.00 27.09 ? 49   PRO   A C     1 
ATOM   276   O  O     . PRO   A  1 51   ? -51.571 42.325  96.416  1.00 26.67 ? 49   PRO   A O     1 
ATOM   277   C  CB    . PRO   A  1 51   ? -51.348 44.331  98.953  1.00 25.85 ? 49   PRO   A CB    1 
ATOM   278   C  CG    . PRO   A  1 51   ? -50.121 45.021  99.393  1.00 28.18 ? 49   PRO   A CG    1 
ATOM   279   C  CD    . PRO   A  1 51   ? -49.326 43.984  100.131 1.00 25.49 ? 49   PRO   A CD    1 
ATOM   280   N  N     . LEU   A  1 52   ? -49.445 43.031  96.654  1.00 26.36 ? 50   LEU   A N     1 
ATOM   281   C  CA    . LEU   A  1 52   ? -49.151 42.803  95.244  1.00 22.86 ? 50   LEU   A CA    1 
ATOM   282   C  C     . LEU   A  1 52   ? -49.034 41.313  94.949  1.00 26.54 ? 50   LEU   A C     1 
ATOM   283   O  O     . LEU   A  1 52   ? -49.587 40.824  93.955  1.00 23.07 ? 50   LEU   A O     1 
ATOM   284   C  CB    . LEU   A  1 52   ? -47.871 43.538  94.853  1.00 21.70 ? 50   LEU   A CB    1 
ATOM   285   C  CG    . LEU   A  1 52   ? -47.928 45.059  95.041  1.00 21.97 ? 50   LEU   A CG    1 
ATOM   286   C  CD1   . LEU   A  1 52   ? -46.529 45.661  94.848  1.00 20.38 ? 50   LEU   A CD1   1 
ATOM   287   C  CD2   . LEU   A  1 52   ? -48.928 45.686  94.063  1.00 22.15 ? 50   LEU   A CD2   1 
ATOM   288   N  N     . VAL   A  1 53   ? -48.324 40.577  95.809  1.00 25.68 ? 51   VAL   A N     1 
ATOM   289   C  CA    . VAL   A  1 53   ? -48.305 39.119  95.705  1.00 26.18 ? 51   VAL   A CA    1 
ATOM   290   C  C     . VAL   A  1 53   ? -49.728 38.576  95.632  1.00 29.81 ? 51   VAL   A C     1 
ATOM   291   O  O     . VAL   A  1 53   ? -50.063 37.773  94.752  1.00 27.09 ? 51   VAL   A O     1 
ATOM   292   C  CB    . VAL   A  1 53   ? -47.526 38.506  96.884  1.00 28.25 ? 51   VAL   A CB    1 
ATOM   293   C  CG1   . VAL   A  1 53   ? -47.647 36.983  96.867  1.00 31.30 ? 51   VAL   A CG1   1 
ATOM   294   C  CG2   . VAL   A  1 53   ? -46.066 38.927  96.842  1.00 25.34 ? 51   VAL   A CG2   1 
ATOM   295   N  N     . GLU   A  1 54   ? -50.599 39.026  96.544  1.00 25.50 ? 52   GLU   A N     1 
ATOM   296   C  CA    . GLU   A  1 54   ? -51.959 38.491  96.556  1.00 30.52 ? 52   GLU   A CA    1 
ATOM   297   C  C     . GLU   A  1 54   ? -52.695 38.838  95.269  1.00 29.09 ? 52   GLU   A C     1 
ATOM   298   O  O     . GLU   A  1 54   ? -53.396 37.995  94.702  1.00 28.18 ? 52   GLU   A O     1 
ATOM   299   C  CB    . GLU   A  1 54   ? -52.730 39.004  97.775  1.00 29.48 ? 52   GLU   A CB    1 
ATOM   300   N  N     . ALA   A  1 55   ? -52.518 40.067  94.773  1.00 25.57 ? 53   ALA   A N     1 
ATOM   301   C  CA    . ALA   A  1 55   ? -53.233 40.488  93.576  1.00 25.91 ? 53   ALA   A CA    1 
ATOM   302   C  C     . ALA   A  1 55   ? -52.709 39.793  92.327  1.00 26.31 ? 53   ALA   A C     1 
ATOM   303   O  O     . ALA   A  1 55   ? -53.463 39.590  91.370  1.00 28.37 ? 53   ALA   A O     1 
ATOM   304   C  CB    . ALA   A  1 55   ? -53.133 42.008  93.409  1.00 26.23 ? 53   ALA   A CB    1 
ATOM   305   N  N     . ALA   A  1 56   ? -51.430 39.433  92.312  1.00 27.37 ? 54   ALA   A N     1 
ATOM   306   C  CA    . ALA   A  1 56   ? -50.795 38.817  91.156  1.00 25.34 ? 54   ALA   A CA    1 
ATOM   307   C  C     . ALA   A  1 56   ? -50.919 37.298  91.156  1.00 33.35 ? 54   ALA   A C     1 
ATOM   308   O  O     . ALA   A  1 56   ? -50.482 36.654  90.197  1.00 27.99 ? 54   ALA   A O     1 
ATOM   309   C  CB    . ALA   A  1 56   ? -49.314 39.217  91.105  1.00 25.75 ? 54   ALA   A CB    1 
ATOM   310   N  N     . THR   A  1 57   ? -51.515 36.720  92.197  1.00 35.07 ? 55   THR   A N     1 
ATOM   311   C  CA    . THR   A  1 57   ? -51.613 35.270  92.307  1.00 33.84 ? 55   THR   A CA    1 
ATOM   312   C  C     . THR   A  1 57   ? -52.575 34.719  91.264  1.00 31.91 ? 55   THR   A C     1 
ATOM   313   O  O     . THR   A  1 57   ? -53.672 35.251  91.068  1.00 30.24 ? 55   THR   A O     1 
ATOM   314   C  CB    . THR   A  1 57   ? -52.067 34.882  93.713  1.00 30.46 ? 55   THR   A CB    1 
ATOM   315   O  OG1   . THR   A  1 57   ? -51.071 35.294  94.656  1.00 33.42 ? 55   THR   A OG1   1 
ATOM   316   C  CG2   . THR   A  1 57   ? -52.278 33.372  93.827  1.00 31.84 ? 55   THR   A CG2   1 
ATOM   317   N  N     . GLN   A  1 58   ? -52.153 33.660  90.576  1.00 30.13 ? 56   GLN   A N     1 
ATOM   318   C  CA    . GLN   A  1 58   ? -52.991 32.980  89.606  1.00 31.88 ? 56   GLN   A CA    1 
ATOM   319   C  C     . GLN   A  1 58   ? -52.996 31.489  89.916  1.00 31.94 ? 56   GLN   A C     1 
ATOM   320   O  O     . GLN   A  1 58   ? -52.150 30.988  90.658  1.00 29.44 ? 56   GLN   A O     1 
ATOM   321   C  CB    . GLN   A  1 58   ? -52.516 33.228  88.166  1.00 34.60 ? 56   GLN   A CB    1 
ATOM   322   C  CG    . GLN   A  1 58   ? -52.391 34.703  87.793  1.00 31.34 ? 56   GLN   A CG    1 
ATOM   323   C  CD    . GLN   A  1 58   ? -52.422 34.927  86.293  1.00 28.63 ? 56   GLN   A CD    1 
ATOM   324   O  OE1   . GLN   A  1 58   ? -53.465 34.782  85.655  1.00 32.45 ? 56   GLN   A OE1   1 
ATOM   325   N  NE2   . GLN   A  1 58   ? -51.276 35.273  85.719  1.00 31.46 ? 56   GLN   A NE2   1 
ATOM   326   N  N     . SER   A  1 59   ? -53.962 30.789  89.327  1.00 33.17 ? 57   SER   A N     1 
ATOM   327   C  CA    . SER   A  1 59   ? -54.146 29.369  89.599  1.00 37.99 ? 57   SER   A CA    1 
ATOM   328   C  C     . SER   A  1 59   ? -52.926 28.564  89.154  1.00 38.96 ? 57   SER   A C     1 
ATOM   329   O  O     . SER   A  1 59   ? -52.109 29.017  88.346  1.00 34.57 ? 57   SER   A O     1 
ATOM   330   C  CB    . SER   A  1 59   ? -55.395 28.852  88.889  1.00 37.09 ? 57   SER   A CB    1 
ATOM   331   O  OG    . SER   A  1 59   ? -55.201 28.827  87.484  1.00 37.39 ? 57   SER   A OG    1 
ATOM   332   N  N     . LYS   A  1 60   ? -52.806 27.347  89.704  1.00 32.74 ? 58   LYS   A N     1 
ATOM   333   C  CA    . LYS   A  1 60   ? -51.751 26.441  89.255  1.00 38.29 ? 58   LYS   A CA    1 
ATOM   334   C  C     . LYS   A  1 60   ? -51.856 26.186  87.756  1.00 36.61 ? 58   LYS   A C     1 
ATOM   335   O  O     . LYS   A  1 60   ? -50.845 26.201  87.042  1.00 36.42 ? 58   LYS   A O     1 
ATOM   336   C  CB    . LYS   A  1 60   ? -51.817 25.117  90.027  1.00 31.31 ? 58   LYS   A CB    1 
ATOM   337   N  N     . GLU   A  1 61   ? -53.076 25.965  87.261  1.00 34.30 ? 59   GLU   A N     1 
ATOM   338   C  CA    . GLU   A  1 61   ? -53.270 25.697  85.840  1.00 34.80 ? 59   GLU   A CA    1 
ATOM   339   C  C     . GLU   A  1 61   ? -52.795 26.866  84.986  1.00 35.29 ? 59   GLU   A C     1 
ATOM   340   O  O     . GLU   A  1 61   ? -52.111 26.674  83.977  1.00 35.38 ? 59   GLU   A O     1 
ATOM   341   C  CB    . GLU   A  1 61   ? -54.743 25.398  85.562  1.00 35.69 ? 59   GLU   A CB    1 
ATOM   342   N  N     . ILE   A  1 62   ? -53.168 28.090  85.367  1.00 30.81 ? 60   ILE   A N     1 
ATOM   343   C  CA    . ILE   A  1 62   ? -52.732 29.261  84.615  1.00 33.89 ? 60   ILE   A CA    1 
ATOM   344   C  C     . ILE   A  1 62   ? -51.218 29.425  84.707  1.00 34.42 ? 60   ILE   A C     1 
ATOM   345   O  O     . ILE   A  1 62   ? -50.552 29.756  83.718  1.00 32.85 ? 60   ILE   A O     1 
ATOM   346   C  CB    . ILE   A  1 62   ? -53.477 30.512  85.116  1.00 34.37 ? 60   ILE   A CB    1 
ATOM   347   C  CG1   . ILE   A  1 62   ? -54.921 30.499  84.607  1.00 38.94 ? 60   ILE   A CG1   1 
ATOM   348   C  CG2   . ILE   A  1 62   ? -52.748 31.778  84.690  1.00 30.77 ? 60   ILE   A CG2   1 
ATOM   349   C  CD1   . ILE   A  1 62   ? -55.749 31.670  85.088  1.00 36.26 ? 60   ILE   A CD1   1 
ATOM   350   N  N     . ARG   A  1 63   ? -50.648 29.191  85.891  1.00 32.04 ? 61   ARG   A N     1 
ATOM   351   C  CA    . ARG   A  1 63   ? -49.206 29.331  86.048  1.00 31.48 ? 61   ARG   A CA    1 
ATOM   352   C  C     . ARG   A  1 63   ? -48.454 28.335  85.175  1.00 33.78 ? 61   ARG   A C     1 
ATOM   353   O  O     . ARG   A  1 63   ? -47.415 28.669  84.593  1.00 30.64 ? 61   ARG   A O     1 
ATOM   354   C  CB    . ARG   A  1 63   ? -48.824 29.170  87.515  1.00 31.46 ? 61   ARG   A CB    1 
ATOM   355   C  CG    . ARG   A  1 63   ? -49.266 30.344  88.354  1.00 37.45 ? 61   ARG   A CG    1 
ATOM   356   C  CD    . ARG   A  1 63   ? -48.616 30.352  89.726  1.00 39.57 ? 61   ARG   A CD    1 
ATOM   357   N  NE    . ARG   A  1 63   ? -49.261 29.437  90.655  1.00 39.10 ? 61   ARG   A NE    1 
ATOM   358   C  CZ    . ARG   A  1 63   ? -48.692 28.340  91.128  1.00 43.10 ? 61   ARG   A CZ    1 
ATOM   359   N  NH1   . ARG   A  1 63   ? -47.471 27.985  90.764  1.00 47.18 ? 61   ARG   A NH1   1 
ATOM   360   N  NH2   . ARG   A  1 63   ? -49.359 27.588  92.001  1.00 37.22 ? 61   ARG   A NH2   1 
ATOM   361   N  N     . ASP   A  1 64   ? -48.972 27.108  85.061  1.00 35.17 ? 62   ASP   A N     1 
ATOM   362   C  CA    . ASP   A  1 64   ? -48.379 26.132  84.151  1.00 35.49 ? 62   ASP   A CA    1 
ATOM   363   C  C     . ASP   A  1 64   ? -48.549 26.556  82.701  1.00 33.17 ? 62   ASP   A C     1 
ATOM   364   O  O     . ASP   A  1 64   ? -47.616 26.436  81.899  1.00 33.84 ? 62   ASP   A O     1 
ATOM   365   C  CB    . ASP   A  1 64   ? -49.008 24.756  84.364  1.00 37.11 ? 62   ASP   A CB    1 
ATOM   366   C  CG    . ASP   A  1 64   ? -48.642 24.137  85.700  1.00 37.76 ? 62   ASP   A CG    1 
ATOM   367   O  OD1   . ASP   A  1 64   ? -47.874 24.750  86.469  1.00 38.83 ? 62   ASP   A OD1   1 
ATOM   368   O  OD2   . ASP   A  1 64   ? -49.126 23.025  85.979  1.00 42.29 ? 62   ASP   A OD2   1 
ATOM   369   N  N     . ALA   A  1 65   ? -49.747 27.022  82.336  1.00 31.03 ? 63   ALA   A N     1 
ATOM   370   C  CA    . ALA   A  1 65   ? -49.974 27.480  80.970  1.00 34.58 ? 63   ALA   A CA    1 
ATOM   371   C  C     . ALA   A  1 65   ? -49.069 28.658  80.632  1.00 32.70 ? 63   ALA   A C     1 
ATOM   372   O  O     . ALA   A  1 65   ? -48.520 28.734  79.525  1.00 31.40 ? 63   ALA   A O     1 
ATOM   373   C  CB    . ALA   A  1 65   ? -51.445 27.850  80.782  1.00 34.44 ? 63   ALA   A CB    1 
ATOM   374   N  N     . ALA   A  1 66   ? -48.881 29.575  81.584  1.00 32.48 ? 64   ALA   A N     1 
ATOM   375   C  CA    . ALA   A  1 66   ? -48.033 30.738  81.338  1.00 34.09 ? 64   ALA   A CA    1 
ATOM   376   C  C     . ALA   A  1 66   ? -46.568 30.341  81.191  1.00 32.30 ? 64   ALA   A C     1 
ATOM   377   O  O     . ALA   A  1 66   ? -45.873 30.837  80.296  1.00 29.23 ? 64   ALA   A O     1 
ATOM   378   C  CB    . ALA   A  1 66   ? -48.201 31.761  82.461  1.00 30.68 ? 64   ALA   A CB    1 
ATOM   379   N  N     . ALA   A  1 67   ? -46.076 29.454  82.062  1.00 31.55 ? 65   ALA   A N     1 
ATOM   380   C  CA    . ALA   A  1 67   ? -44.699 28.988  81.935  1.00 33.24 ? 65   ALA   A CA    1 
ATOM   381   C  C     . ALA   A  1 67   ? -44.465 28.305  80.592  1.00 33.60 ? 65   ALA   A C     1 
ATOM   382   O  O     . ALA   A  1 67   ? -43.385 28.439  80.000  1.00 34.46 ? 65   ALA   A O     1 
ATOM   383   C  CB    . ALA   A  1 67   ? -44.353 28.040  83.082  1.00 30.40 ? 65   ALA   A CB    1 
ATOM   384   N  N     . SER   A  1 68   ? -45.469 27.588  80.091  1.00 34.71 ? 66   SER   A N     1 
ATOM   385   C  CA    . SER   A  1 68   ? -45.342 26.921  78.803  1.00 35.42 ? 66   SER   A CA    1 
ATOM   386   C  C     . SER   A  1 68   ? -45.319 27.925  77.658  1.00 35.48 ? 66   SER   A C     1 
ATOM   387   O  O     . SER   A  1 68   ? -44.503 27.805  76.735  1.00 33.86 ? 66   SER   A O     1 
ATOM   388   C  CB    . SER   A  1 68   ? -46.485 25.925  78.626  1.00 38.28 ? 66   SER   A CB    1 
ATOM   389   O  OG    . SER   A  1 68   ? -46.646 25.593  77.262  1.00 46.68 ? 66   SER   A OG    1 
ATOM   390   N  N     . THR   A  1 69   ? -46.204 28.925  77.700  1.00 32.86 ? 67   THR   A N     1 
ATOM   391   C  CA    . THR   A  1 69   ? -46.192 29.967  76.680  1.00 32.68 ? 67   THR   A CA    1 
ATOM   392   C  C     . THR   A  1 69   ? -44.890 30.757  76.717  1.00 30.90 ? 67   THR   A C     1 
ATOM   393   O  O     . THR   A  1 69   ? -44.320 31.073  75.666  1.00 30.51 ? 67   THR   A O     1 
ATOM   394   C  CB    . THR   A  1 69   ? -47.385 30.905  76.866  1.00 29.25 ? 67   THR   A CB    1 
ATOM   395   O  OG1   . THR   A  1 69   ? -48.597 30.162  76.730  1.00 33.56 ? 67   THR   A OG1   1 
ATOM   396   C  CG2   . THR   A  1 69   ? -47.359 32.031  75.827  1.00 28.05 ? 67   THR   A CG2   1 
ATOM   397   N  N     . ALA   A  1 70   ? -44.407 31.093  77.921  1.00 29.34 ? 68   ALA   A N     1 
ATOM   398   C  CA    . ALA   A  1 70   ? -43.154 31.838  78.029  1.00 30.72 ? 68   ALA   A CA    1 
ATOM   399   C  C     . ALA   A  1 70   ? -41.985 31.016  77.505  1.00 32.84 ? 68   ALA   A C     1 
ATOM   400   O  O     . ALA   A  1 70   ? -41.091 31.547  76.836  1.00 27.78 ? 68   ALA   A O     1 
ATOM   401   C  CB    . ALA   A  1 70   ? -42.896 32.257  79.476  1.00 25.11 ? 68   ALA   A CB    1 
ATOM   402   N  N     . ARG   A  1 71   ? -41.975 29.716  77.803  1.00 32.69 ? 69   ARG   A N     1 
ATOM   403   C  CA    . ARG   A  1 71   ? -40.952 28.842  77.236  1.00 36.44 ? 69   ARG   A CA    1 
ATOM   404   C  C     . ARG   A  1 71   ? -41.001 28.866  75.715  1.00 30.38 ? 69   ARG   A C     1 
ATOM   405   O  O     . ARG   A  1 71   ? -39.969 29.023  75.054  1.00 34.81 ? 69   ARG   A O     1 
ATOM   406   C  CB    . ARG   A  1 71   ? -41.120 27.413  77.753  1.00 31.33 ? 69   ARG   A CB    1 
ATOM   407   C  CG    . ARG   A  1 71   ? -40.204 26.417  77.050  1.00 34.57 ? 69   ARG   A CG    1 
ATOM   408   C  CD    . ARG   A  1 71   ? -40.107 25.085  77.792  1.00 33.91 ? 69   ARG   A CD    1 
ATOM   409   N  NE    . ARG   A  1 71   ? -39.178 25.155  78.913  1.00 38.52 ? 69   ARG   A NE    1 
ATOM   410   C  CZ    . ARG   A  1 71   ? -37.858 25.205  78.789  1.00 42.33 ? 69   ARG   A CZ    1 
ATOM   411   N  NH1   . ARG   A  1 71   ? -37.274 25.185  77.601  1.00 44.00 ? 69   ARG   A NH1   1 
ATOM   412   N  NH2   . ARG   A  1 71   ? -37.106 25.290  79.882  1.00 40.53 ? 69   ARG   A NH2   1 
ATOM   413   N  N     . LYS   A  1 72   ? -42.203 28.732  75.145  1.00 28.72 ? 70   LYS   A N     1 
ATOM   414   C  CA    . LYS   A  1 72   ? -42.343 28.726  73.692  1.00 31.63 ? 70   LYS   A CA    1 
ATOM   415   C  C     . LYS   A  1 72   ? -41.848 30.030  73.083  1.00 36.63 ? 70   LYS   A C     1 
ATOM   416   O  O     . LYS   A  1 72   ? -41.166 30.019  72.053  1.00 34.69 ? 70   LYS   A O     1 
ATOM   417   C  CB    . LYS   A  1 72   ? -43.799 28.472  73.301  1.00 37.77 ? 70   LYS   A CB    1 
ATOM   418   N  N     . LEU   A  1 73   ? -42.178 31.166  73.709  1.00 31.32 ? 71   LEU   A N     1 
ATOM   419   C  CA    . LEU   A  1 73   ? -41.707 32.454  73.209  1.00 32.63 ? 71   LEU   A CA    1 
ATOM   420   C  C     . LEU   A  1 73   ? -40.192 32.557  73.283  1.00 32.10 ? 71   LEU   A C     1 
ATOM   421   O  O     . LEU   A  1 73   ? -39.549 33.041  72.346  1.00 32.39 ? 71   LEU   A O     1 
ATOM   422   C  CB    . LEU   A  1 73   ? -42.337 33.595  74.007  1.00 29.52 ? 71   LEU   A CB    1 
ATOM   423   C  CG    . LEU   A  1 73   ? -43.853 33.702  73.918  1.00 30.40 ? 71   LEU   A CG    1 
ATOM   424   C  CD1   . LEU   A  1 73   ? -44.347 34.692  74.965  1.00 30.53 ? 71   LEU   A CD1   1 
ATOM   425   C  CD2   . LEU   A  1 73   ? -44.249 34.147  72.528  1.00 31.31 ? 71   LEU   A CD2   1 
ATOM   426   N  N     . ILE   A  1 74   ? -39.606 32.125  74.402  1.00 30.92 ? 72   ILE   A N     1 
ATOM   427   C  CA    . ILE   A  1 74   ? -38.167 32.267  74.588  1.00 32.74 ? 72   ILE   A CA    1 
ATOM   428   C  C     . ILE   A  1 74   ? -37.414 31.317  73.667  1.00 33.53 ? 72   ILE   A C     1 
ATOM   429   O  O     . ILE   A  1 74   ? -36.357 31.664  73.128  1.00 34.79 ? 72   ILE   A O     1 
ATOM   430   C  CB    . ILE   A  1 74   ? -37.807 32.052  76.067  1.00 33.87 ? 72   ILE   A CB    1 
ATOM   431   C  CG1   . ILE   A  1 74   ? -38.346 33.214  76.902  1.00 33.60 ? 72   ILE   A CG1   1 
ATOM   432   C  CG2   . ILE   A  1 74   ? -36.297 31.938  76.264  1.00 32.01 ? 72   ILE   A CG2   1 
ATOM   433   C  CD1   . ILE   A  1 74   ? -38.317 32.944  78.391  1.00 36.77 ? 72   ILE   A CD1   1 
ATOM   434   N  N     . GLU   A  1 75   ? -37.948 30.110  73.464  1.00 37.16 ? 73   GLU   A N     1 
ATOM   435   C  CA    . GLU   A  1 75   ? -37.347 29.194  72.501  1.00 37.72 ? 73   GLU   A CA    1 
ATOM   436   C  C     . GLU   A  1 75   ? -37.348 29.797  71.101  1.00 35.04 ? 73   GLU   A C     1 
ATOM   437   O  O     . GLU   A  1 75   ? -36.341 29.728  70.390  1.00 39.27 ? 73   GLU   A O     1 
ATOM   438   C  CB    . GLU   A  1 75   ? -38.074 27.847  72.530  1.00 36.01 ? 73   GLU   A CB    1 
ATOM   439   C  CG    . GLU   A  1 75   ? -37.611 26.967  73.686  1.00 38.90 ? 73   GLU   A CG    1 
ATOM   440   C  CD    . GLU   A  1 75   ? -38.481 25.748  73.942  1.00 42.52 ? 73   GLU   A CD    1 
ATOM   441   O  OE1   . GLU   A  1 75   ? -39.581 25.633  73.354  1.00 39.10 ? 73   GLU   A OE1   1 
ATOM   442   O  OE2   . GLU   A  1 75   ? -38.055 24.902  74.755  1.00 43.31 ? 73   GLU   A OE2   1 
ATOM   443   N  N     . ALA   A  1 76   ? -38.459 30.417  70.700  1.00 36.52 ? 74   ALA   A N     1 
ATOM   444   C  CA    . ALA   A  1 76   ? -38.487 31.151  69.436  1.00 39.43 ? 74   ALA   A CA    1 
ATOM   445   C  C     . ALA   A  1 76   ? -37.430 32.249  69.411  1.00 37.23 ? 74   ALA   A C     1 
ATOM   446   O  O     . ALA   A  1 76   ? -36.691 32.392  68.432  1.00 40.94 ? 74   ALA   A O     1 
ATOM   447   C  CB    . ALA   A  1 76   ? -39.877 31.747  69.201  1.00 34.83 ? 74   ALA   A CB    1 
ATOM   448   N  N     . LEU   A  1 77   ? -37.347 33.040  70.484  1.00 37.26 ? 75   LEU   A N     1 
ATOM   449   C  CA    . LEU   A  1 77   ? -36.408 34.158  70.520  1.00 39.24 ? 75   LEU   A CA    1 
ATOM   450   C  C     . LEU   A  1 77   ? -34.972 33.683  70.355  1.00 42.90 ? 75   LEU   A C     1 
ATOM   451   O  O     . LEU   A  1 77   ? -34.209 34.235  69.554  1.00 40.47 ? 75   LEU   A O     1 
ATOM   452   C  CB    . LEU   A  1 77   ? -36.550 34.924  71.832  1.00 35.82 ? 75   LEU   A CB    1 
ATOM   453   C  CG    . LEU   A  1 77   ? -37.599 36.028  71.869  1.00 35.72 ? 75   LEU   A CG    1 
ATOM   454   C  CD1   . LEU   A  1 77   ? -37.551 36.705  73.222  1.00 37.84 ? 75   LEU   A CD1   1 
ATOM   455   C  CD2   . LEU   A  1 77   ? -37.357 37.024  70.751  1.00 35.55 ? 75   LEU   A CD2   1 
ATOM   456   N  N     . ARG   A  1 78   ? -34.582 32.668  71.124  1.00 38.43 ? 76   ARG   A N     1 
ATOM   457   C  CA    . ARG   A  1 78   ? -33.209 32.193  71.090  1.00 41.30 ? 76   ARG   A CA    1 
ATOM   458   C  C     . ARG   A  1 78   ? -32.897 31.402  69.832  1.00 43.24 ? 76   ARG   A C     1 
ATOM   459   O  O     . ARG   A  1 78   ? -31.721 31.149  69.559  1.00 45.72 ? 76   ARG   A O     1 
ATOM   460   C  CB    . ARG   A  1 78   ? -32.923 31.355  72.338  1.00 37.26 ? 76   ARG   A CB    1 
ATOM   461   C  CG    . ARG   A  1 78   ? -32.815 32.194  73.595  1.00 37.50 ? 76   ARG   A CG    1 
ATOM   462   C  CD    . ARG   A  1 78   ? -32.403 31.374  74.796  1.00 35.96 ? 76   ARG   A CD    1 
ATOM   463   N  NE    . ARG   A  1 78   ? -31.838 32.220  75.839  1.00 36.23 ? 76   ARG   A NE    1 
ATOM   464   C  CZ    . ARG   A  1 78   ? -31.434 31.785  77.024  1.00 36.56 ? 76   ARG   A CZ    1 
ATOM   465   N  NH1   . ARG   A  1 78   ? -31.550 30.513  77.369  1.00 39.35 ? 76   ARG   A NH1   1 
ATOM   466   N  NH2   . ARG   A  1 78   ? -30.902 32.650  77.886  1.00 37.80 ? 76   ARG   A NH2   1 
ATOM   467   N  N     . GLY   A  1 79   ? -33.909 31.017  69.064  1.00 42.59 ? 77   GLY   A N     1 
ATOM   468   C  CA    . GLY   A  1 79   ? -33.693 30.307  67.820  1.00 46.62 ? 77   GLY   A CA    1 
ATOM   469   C  C     . GLY   A  1 79   ? -33.734 31.221  66.612  1.00 46.71 ? 77   GLY   A C     1 
ATOM   470   O  O     . GLY   A  1 79   ? -33.900 30.763  65.478  1.00 50.68 ? 77   GLY   A O     1 
ATOM   471   N  N     . LYS   A  1 80   ? -33.597 32.519  66.846  1.00 47.88 ? 78   LYS   A N     1 
ATOM   472   C  CA    . LYS   A  1 80   ? -33.505 33.480  65.759  1.00 51.30 ? 78   LYS   A CA    1 
ATOM   473   C  C     . LYS   A  1 80   ? -32.542 34.593  66.152  1.00 46.03 ? 78   LYS   A C     1 
ATOM   474   O  O     . LYS   A  1 80   ? -31.935 35.232  65.295  1.00 53.86 ? 78   LYS   A O     1 
ATOM   475   C  CB    . LYS   A  1 80   ? -34.886 34.050  65.410  1.00 49.48 ? 78   LYS   A CB    1 
ATOM   476   C  CG    . LYS   A  1 80   ? -35.527 34.840  66.534  1.00 47.47 ? 78   LYS   A CG    1 
ATOM   477   C  CD    . LYS   A  1 80   ? -36.735 35.652  66.064  1.00 42.31 ? 78   LYS   A CD    1 
ATOM   478   C  CE    . LYS   A  1 80   ? -38.040 34.926  66.309  1.00 39.53 ? 78   LYS   A CE    1 
ATOM   479   N  NZ    . LYS   A  1 80   ? -39.195 35.878  66.395  1.00 33.36 ? 78   LYS   A NZ    1 
ATOM   480   N  N     . GLY   A  1 85   ? -24.854 41.901  64.526  1.00 54.14 ? 83   GLY   A N     1 
ATOM   481   C  CA    . GLY   A  1 85   ? -24.608 43.143  63.815  1.00 44.02 ? 83   GLY   A CA    1 
ATOM   482   C  C     . GLY   A  1 85   ? -23.225 43.698  64.113  1.00 46.35 ? 83   GLY   A C     1 
ATOM   483   O  O     . GLY   A  1 85   ? -22.248 43.371  63.430  1.00 43.01 ? 83   GLY   A O     1 
ATOM   484   N  N     . VAL   A  1 86   ? -23.142 44.544  65.143  1.00 46.07 ? 84   VAL   A N     1 
ATOM   485   C  CA    . VAL   A  1 86   ? -21.845 45.059  65.575  1.00 42.10 ? 84   VAL   A CA    1 
ATOM   486   C  C     . VAL   A  1 86   ? -20.913 43.912  65.939  1.00 37.29 ? 84   VAL   A C     1 
ATOM   487   O  O     . VAL   A  1 86   ? -19.701 43.983  65.698  1.00 35.52 ? 84   VAL   A O     1 
ATOM   488   C  CB    . VAL   A  1 86   ? -22.025 46.045  66.746  1.00 42.10 ? 84   VAL   A CB    1 
ATOM   489   N  N     . GLU   A  1 87   ? -21.460 42.821  66.485  1.00 40.70 ? 85   GLU   A N     1 
ATOM   490   C  CA    . GLU   A  1 87   ? -20.618 41.699  66.893  1.00 39.27 ? 85   GLU   A CA    1 
ATOM   491   C  C     . GLU   A  1 87   ? -19.996 41.000  65.691  1.00 39.66 ? 85   GLU   A C     1 
ATOM   492   O  O     . GLU   A  1 87   ? -18.860 40.514  65.769  1.00 40.73 ? 85   GLU   A O     1 
ATOM   493   C  CB    . GLU   A  1 87   ? -21.424 40.706  67.731  1.00 49.11 ? 85   GLU   A CB    1 
ATOM   494   N  N     . GLY   A  1 88   ? -20.722 40.926  64.574  1.00 39.29 ? 86   GLY   A N     1 
ATOM   495   C  CA    . GLY   A  1 88   ? -20.134 40.353  63.377  1.00 35.68 ? 86   GLY   A CA    1 
ATOM   496   C  C     . GLY   A  1 88   ? -19.027 41.213  62.805  1.00 37.18 ? 86   GLY   A C     1 
ATOM   497   O  O     . GLY   A  1 88   ? -18.064 40.697  62.228  1.00 31.76 ? 86   GLY   A O     1 
ATOM   498   N  N     . LEU   A  1 89   ? -19.158 42.533  62.935  1.00 33.66 ? 87   LEU   A N     1 
ATOM   499   C  CA    . LEU   A  1 89   ? -18.111 43.442  62.488  1.00 33.80 ? 87   LEU   A CA    1 
ATOM   500   C  C     . LEU   A  1 89   ? -16.847 43.262  63.325  1.00 29.88 ? 87   LEU   A C     1 
ATOM   501   O  O     . LEU   A  1 89   ? -15.742 43.110  62.787  1.00 30.53 ? 87   LEU   A O     1 
ATOM   502   C  CB    . LEU   A  1 89   ? -18.639 44.877  62.570  1.00 33.29 ? 87   LEU   A CB    1 
ATOM   503   C  CG    . LEU   A  1 89   ? -17.770 46.021  62.066  1.00 37.12 ? 87   LEU   A CG    1 
ATOM   504   C  CD1   . LEU   A  1 89   ? -17.197 45.656  60.720  1.00 41.60 ? 87   LEU   A CD1   1 
ATOM   505   C  CD2   . LEU   A  1 89   ? -18.607 47.287  61.968  1.00 39.02 ? 87   LEU   A CD2   1 
ATOM   506   N  N     . VAL   A  1 90   ? -17.008 43.249  64.651  1.00 31.39 ? 88   VAL   A N     1 
ATOM   507   C  CA    . VAL   A  1 90   ? -15.896 43.006  65.564  1.00 30.24 ? 88   VAL   A CA    1 
ATOM   508   C  C     . VAL   A  1 90   ? -15.202 41.693  65.234  1.00 33.47 ? 88   VAL   A C     1 
ATOM   509   O  O     . VAL   A  1 90   ? -13.966 41.605  65.239  1.00 32.58 ? 88   VAL   A O     1 
ATOM   510   C  CB    . VAL   A  1 90   ? -16.405 43.023  67.017  1.00 26.75 ? 88   VAL   A CB    1 
ATOM   511   C  CG1   . VAL   A  1 90   ? -15.350 42.486  67.948  1.00 29.73 ? 88   VAL   A CG1   1 
ATOM   512   C  CG2   . VAL   A  1 90   ? -16.816 44.428  67.408  1.00 29.23 ? 88   VAL   A CG2   1 
ATOM   513   N  N     . GLN   A  1 91   ? -15.986 40.651  64.947  1.00 34.04 ? 89   GLN   A N     1 
ATOM   514   C  CA    . GLN   A  1 91   ? -15.412 39.357  64.599  1.00 34.06 ? 89   GLN   A CA    1 
ATOM   515   C  C     . GLN   A  1 91   ? -14.691 39.414  63.260  1.00 33.79 ? 89   GLN   A C     1 
ATOM   516   O  O     . GLN   A  1 91   ? -13.562 38.924  63.131  1.00 33.41 ? 89   GLN   A O     1 
ATOM   517   C  CB    . GLN   A  1 91   ? -16.506 38.286  64.570  1.00 35.81 ? 89   GLN   A CB    1 
ATOM   518   N  N     . GLU   A  1 92   ? -15.326 40.010  62.249  1.00 32.63 ? 90   GLU   A N     1 
ATOM   519   C  CA    . GLU   A  1 92   ? -14.753 39.970  60.906  1.00 35.79 ? 90   GLU   A CA    1 
ATOM   520   C  C     . GLU   A  1 92   ? -13.404 40.676  60.855  1.00 32.01 ? 90   GLU   A C     1 
ATOM   521   O  O     . GLU   A  1 92   ? -12.492 40.235  60.150  1.00 31.37 ? 90   GLU   A O     1 
ATOM   522   C  CB    . GLU   A  1 92   ? -15.720 40.590  59.898  1.00 36.32 ? 90   GLU   A CB    1 
ATOM   523   C  CG    . GLU   A  1 92   ? -15.204 40.588  58.468  1.00 40.05 ? 90   GLU   A CG    1 
ATOM   524   C  CD    . GLU   A  1 92   ? -16.133 41.320  57.520  1.00 45.00 ? 90   GLU   A CD    1 
ATOM   525   O  OE1   . GLU   A  1 92   ? -17.235 41.722  57.960  1.00 44.69 ? 90   GLU   A OE1   1 
ATOM   526   O  OE2   . GLU   A  1 92   ? -15.756 41.498  56.343  1.00 42.86 ? 90   GLU   A OE2   1 
ATOM   527   N  N     . TYR   A  1 93   ? -13.245 41.758  61.616  1.00 30.39 ? 91   TYR   A N     1 
ATOM   528   C  CA    . TYR   A  1 93   ? -12.003 42.518  61.603  1.00 28.07 ? 91   TYR   A CA    1 
ATOM   529   C  C     . TYR   A  1 93   ? -11.169 42.329  62.863  1.00 27.46 ? 91   TYR   A C     1 
ATOM   530   O  O     . TYR   A  1 93   ? -10.199 43.071  63.065  1.00 30.21 ? 91   TYR   A O     1 
ATOM   531   C  CB    . TYR   A  1 93   ? -12.308 43.998  61.374  1.00 28.27 ? 91   TYR   A CB    1 
ATOM   532   C  CG    . TYR   A  1 93   ? -12.741 44.249  59.951  1.00 31.30 ? 91   TYR   A CG    1 
ATOM   533   C  CD1   . TYR   A  1 93   ? -11.802 44.460  58.950  1.00 27.48 ? 91   TYR   A CD1   1 
ATOM   534   C  CD2   . TYR   A  1 93   ? -14.082 44.239  59.603  1.00 30.28 ? 91   TYR   A CD2   1 
ATOM   535   C  CE1   . TYR   A  1 93   ? -12.183 44.671  57.645  1.00 31.58 ? 91   TYR   A CE1   1 
ATOM   536   C  CE2   . TYR   A  1 93   ? -14.478 44.450  58.298  1.00 35.77 ? 91   TYR   A CE2   1 
ATOM   537   C  CZ    . TYR   A  1 93   ? -13.524 44.662  57.325  1.00 34.22 ? 91   TYR   A CZ    1 
ATOM   538   O  OH    . TYR   A  1 93   ? -13.915 44.872  56.033  1.00 37.78 ? 91   TYR   A OH    1 
ATOM   539   N  N     . SER   A  1 94   ? -11.516 41.357  63.703  1.00 26.20 ? 92   SER   A N     1 
ATOM   540   C  CA    . SER   A  1 94   ? -10.742 41.041  64.907  1.00 27.72 ? 92   SER   A CA    1 
ATOM   541   C  C     . SER   A  1 94   ? -10.543 42.277  65.777  1.00 25.56 ? 92   SER   A C     1 
ATOM   542   O  O     . SER   A  1 94   ? -9.455  42.523  66.305  1.00 27.10 ? 92   SER   A O     1 
ATOM   543   C  CB    . SER   A  1 94   ? -9.395  40.414  64.546  1.00 33.41 ? 92   SER   A CB    1 
ATOM   544   O  OG    . SER   A  1 94   ? -9.583  39.278  63.717  1.00 37.08 ? 92   SER   A OG    1 
ATOM   545   N  N     . LEU   A  1 95   ? -11.605 43.063  65.921  1.00 24.62 ? 93   LEU   A N     1 
ATOM   546   C  CA    . LEU   A  1 95   ? -11.528 44.297  66.679  1.00 25.86 ? 93   LEU   A CA    1 
ATOM   547   C  C     . LEU   A  1 95   ? -11.560 44.004  68.165  1.00 25.05 ? 93   LEU   A C     1 
ATOM   548   O  O     . LEU   A  1 95   ? -12.319 43.153  68.631  1.00 23.24 ? 93   LEU   A O     1 
ATOM   549   C  CB    . LEU   A  1 95   ? -12.686 45.228  66.326  1.00 22.55 ? 93   LEU   A CB    1 
ATOM   550   C  CG    . LEU   A  1 95   ? -12.819 45.564  64.837  1.00 25.10 ? 93   LEU   A CG    1 
ATOM   551   C  CD1   . LEU   A  1 95   ? -13.939 46.576  64.635  1.00 28.29 ? 93   LEU   A CD1   1 
ATOM   552   C  CD2   . LEU   A  1 95   ? -11.484 46.086  64.298  1.00 22.69 ? 93   LEU   A CD2   1 
ATOM   553   N  N     . SER   A  1 96   ? -10.730 44.717  68.907  1.00 21.91 ? 94   SER   A N     1 
ATOM   554   C  CA    . SER   A  1 96   ? -10.914 44.790  70.341  1.00 24.69 ? 94   SER   A CA    1 
ATOM   555   C  C     . SER   A  1 96   ? -12.169 45.600  70.639  1.00 21.83 ? 94   SER   A C     1 
ATOM   556   O  O     . SER   A  1 96   ? -12.707 46.289  69.770  1.00 22.46 ? 94   SER   A O     1 
ATOM   557   C  CB    . SER   A  1 96   ? -9.703  45.446  70.998  1.00 20.71 ? 94   SER   A CB    1 
ATOM   558   O  OG    . SER   A  1 96   ? -9.681  46.820  70.656  1.00 20.68 ? 94   SER   A OG    1 
ATOM   559   N  N     . SER   A  1 97   ? -12.623 45.534  71.892  1.00 21.44 ? 95   SER   A N     1 
ATOM   560   C  CA    . SER   A  1 97   ? -13.766 46.339  72.311  1.00 25.17 ? 95   SER   A CA    1 
ATOM   561   C  C     . SER   A  1 97   ? -13.508 47.821  72.086  1.00 22.04 ? 95   SER   A C     1 
ATOM   562   O  O     . SER   A  1 97   ? -14.364 48.535  71.555  1.00 21.21 ? 95   SER   A O     1 
ATOM   563   C  CB    . SER   A  1 97   ? -14.095 46.077  73.782  1.00 28.25 ? 95   SER   A CB    1 
ATOM   564   O  OG    . SER   A  1 97   ? -14.730 44.829  73.928  1.00 35.04 ? 95   SER   A OG    1 
ATOM   565   N  N     . GLN   A  1 98   ? -12.325 48.306  72.475  1.00 19.01 ? 96   GLN   A N     1 
ATOM   566   C  CA    . GLN   A  1 98   ? -12.052 49.729  72.296  1.00 19.07 ? 96   GLN   A CA    1 
ATOM   567   C  C     . GLN   A  1 98   ? -12.028 50.100  70.820  1.00 19.38 ? 96   GLN   A C     1 
ATOM   568   O  O     . GLN   A  1 98   ? -12.483 51.184  70.437  1.00 18.33 ? 96   GLN   A O     1 
ATOM   569   C  CB    . GLN   A  1 98   ? -10.740 50.113  72.980  1.00 18.86 ? 96   GLN   A CB    1 
ATOM   570   C  CG    . GLN   A  1 98   ? -10.853 50.194  74.498  1.00 20.66 ? 96   GLN   A CG    1 
ATOM   571   C  CD    . GLN   A  1 98   ? -11.819 51.275  74.941  1.00 20.72 ? 96   GLN   A CD    1 
ATOM   572   O  OE1   . GLN   A  1 98   ? -13.033 51.074  74.954  1.00 23.63 ? 96   GLN   A OE1   1 
ATOM   573   N  NE2   . GLN   A  1 98   ? -11.285 52.442  75.279  1.00 20.46 ? 96   GLN   A NE2   1 
ATOM   574   N  N     . GLU   A  1 99   ? -11.491 49.216  69.979  1.00 19.17 ? 97   GLU   A N     1 
ATOM   575   C  CA    . GLU   A  1 99   ? -11.497 49.460  68.540  1.00 19.12 ? 97   GLU   A CA    1 
ATOM   576   C  C     . GLU   A  1 99   ? -12.921 49.512  67.995  1.00 20.13 ? 97   GLU   A C     1 
ATOM   577   O  O     . GLU   A  1 99   ? -13.246 50.366  67.160  1.00 19.35 ? 97   GLU   A O     1 
ATOM   578   C  CB    . GLU   A  1 99   ? -10.678 48.383  67.827  1.00 19.59 ? 97   GLU   A CB    1 
ATOM   579   C  CG    . GLU   A  1 99   ? -9.178  48.557  68.040  1.00 19.75 ? 97   GLU   A CG    1 
ATOM   580   C  CD    . GLU   A  1 99   ? -8.359  47.378  67.552  1.00 20.21 ? 97   GLU   A CD    1 
ATOM   581   O  OE1   . GLU   A  1 99   ? -8.947  46.387  67.063  1.00 21.50 ? 97   GLU   A OE1   1 
ATOM   582   O  OE2   . GLU   A  1 99   ? -7.118  47.440  67.678  1.00 22.12 ? 97   GLU   A OE2   1 
ATOM   583   N  N     . GLY   A  1 100  ? -13.786 48.612  68.453  1.00 19.62 ? 98   GLY   A N     1 
ATOM   584   C  CA    . GLY   A  1 100  ? -15.174 48.663  68.006  1.00 18.87 ? 98   GLY   A CA    1 
ATOM   585   C  C     . GLY   A  1 100  ? -15.856 49.964  68.392  1.00 19.76 ? 98   GLY   A C     1 
ATOM   586   O  O     . GLY   A  1 100  ? -16.553 50.580  67.583  1.00 19.84 ? 98   GLY   A O     1 
ATOM   587   N  N     . VAL   A  1 101  ? -15.658 50.401  69.637  1.00 18.20 ? 99   VAL   A N     1 
ATOM   588   C  CA    . VAL   A  1 101  ? -16.218 51.679  70.078  1.00 19.01 ? 99   VAL   A CA    1 
ATOM   589   C  C     . VAL   A  1 101  ? -15.636 52.824  69.258  1.00 20.60 ? 99   VAL   A C     1 
ATOM   590   O  O     . VAL   A  1 101  ? -16.367 53.695  68.765  1.00 18.23 ? 99   VAL   A O     1 
ATOM   591   C  CB    . VAL   A  1 101  ? -15.961 51.887  71.579  1.00 18.59 ? 99   VAL   A CB    1 
ATOM   592   C  CG1   . VAL   A  1 101  ? -16.413 53.276  72.012  1.00 18.20 ? 99   VAL   A CG1   1 
ATOM   593   C  CG2   . VAL   A  1 101  ? -16.637 50.789  72.396  1.00 21.00 ? 99   VAL   A CG2   1 
ATOM   594   N  N     . ALA   A  1 102  ? -14.306 52.830  69.087  1.00 18.10 ? 100  ALA   A N     1 
ATOM   595   C  CA    . ALA   A  1 102  ? -13.668 53.918  68.352  1.00 18.19 ? 100  ALA   A CA    1 
ATOM   596   C  C     . ALA   A  1 102  ? -14.142 53.961  66.910  1.00 19.29 ? 100  ALA   A C     1 
ATOM   597   O  O     . ALA   A  1 102  ? -14.341 55.045  66.345  1.00 18.39 ? 100  ALA   A O     1 
ATOM   598   C  CB    . ALA   A  1 102  ? -12.148 53.775  68.396  1.00 18.58 ? 100  ALA   A CB    1 
ATOM   599   N  N     . LEU   A  1 103  ? -14.285 52.788  66.288  1.00 18.69 ? 101  LEU   A N     1 
ATOM   600   C  CA    . LEU   A  1 103  ? -14.806 52.714  64.928  1.00 18.93 ? 101  LEU   A CA    1 
ATOM   601   C  C     . LEU   A  1 103  ? -16.213 53.293  64.840  1.00 20.23 ? 101  LEU   A C     1 
ATOM   602   O  O     . LEU   A  1 103  ? -16.530 54.031  63.902  1.00 20.97 ? 101  LEU   A O     1 
ATOM   603   C  CB    . LEU   A  1 103  ? -14.815 51.268  64.452  1.00 19.70 ? 101  LEU   A CB    1 
ATOM   604   C  CG    . LEU   A  1 103  ? -15.449 51.052  63.078  1.00 19.53 ? 101  LEU   A CG    1 
ATOM   605   C  CD1   . LEU   A  1 103  ? -14.641 51.803  62.034  1.00 19.79 ? 101  LEU   A CD1   1 
ATOM   606   C  CD2   . LEU   A  1 103  ? -15.528 49.576  62.758  1.00 20.16 ? 101  LEU   A CD2   1 
ATOM   607   N  N     . MET   A  1 104  ? -17.076 52.957  65.799  1.00 20.26 ? 102  MET   A N     1 
ATOM   608   C  CA    . MET   A  1 104  ? -18.436 53.490  65.751  1.00 23.32 ? 102  MET   A CA    1 
ATOM   609   C  C     . MET   A  1 104  ? -18.444 54.999  65.955  1.00 22.12 ? 102  MET   A C     1 
ATOM   610   O  O     . MET   A  1 104  ? -19.263 55.698  65.343  1.00 23.79 ? 102  MET   A O     1 
ATOM   611   C  CB    . MET   A  1 104  ? -19.322 52.792  66.786  1.00 20.96 ? 102  MET   A CB    1 
ATOM   612   C  CG    . MET   A  1 104  ? -19.533 51.303  66.510  1.00 21.34 ? 102  MET   A CG    1 
ATOM   613   S  SD    . MET   A  1 104  ? -19.985 50.886  64.804  1.00 32.66 ? 102  MET   A SD    1 
ATOM   614   C  CE    . MET   A  1 104  ? -21.639 51.543  64.727  1.00 31.21 ? 102  MET   A CE    1 
ATOM   615   N  N     . CYS   A  1 105  ? -17.540 55.521  66.797  1.00 19.05 ? 103  CYS   A N     1 
ATOM   616   C  CA    . CYS   A  1 105  ? -17.434 56.970  66.955  1.00 23.61 ? 103  CYS   A CA    1 
ATOM   617   C  C     . CYS   A  1 105  ? -16.969 57.624  65.668  1.00 26.79 ? 103  CYS   A C     1 
ATOM   618   O  O     . CYS   A  1 105  ? -17.464 58.692  65.294  1.00 24.80 ? 103  CYS   A O     1 
ATOM   619   C  CB    . CYS   A  1 105  ? -16.475 57.331  68.084  1.00 22.66 ? 103  CYS   A CB    1 
ATOM   620   S  SG    . CYS   A  1 105  ? -17.006 56.825  69.690  1.00 21.74 ? 103  CYS   A SG    1 
ATOM   621   N  N     . LEU   A  1 106  ? -15.991 57.012  64.992  1.00 22.49 ? 104  LEU   A N     1 
ATOM   622   C  CA    . LEU   A  1 106  ? -15.570 57.509  63.689  1.00 23.04 ? 104  LEU   A CA    1 
ATOM   623   C  C     . LEU   A  1 106  ? -16.729 57.497  62.707  1.00 25.90 ? 104  LEU   A C     1 
ATOM   624   O  O     . LEU   A  1 106  ? -16.942 58.463  61.963  1.00 27.48 ? 104  LEU   A O     1 
ATOM   625   C  CB    . LEU   A  1 106  ? -14.418 56.660  63.150  1.00 22.05 ? 104  LEU   A CB    1 
ATOM   626   C  CG    . LEU   A  1 106  ? -14.028 56.998  61.708  1.00 23.48 ? 104  LEU   A CG    1 
ATOM   627   C  CD1   . LEU   A  1 106  ? -13.526 58.439  61.610  1.00 25.97 ? 104  LEU   A CD1   1 
ATOM   628   C  CD2   . LEU   A  1 106  ? -12.982 56.013  61.173  1.00 25.26 ? 104  LEU   A CD2   1 
ATOM   629   N  N     . ALA   A  1 107  ? -17.475 56.392  62.673  1.00 20.27 ? 105  ALA   A N     1 
ATOM   630   C  CA    . ALA   A  1 107  ? -18.572 56.275  61.722  1.00 27.36 ? 105  ALA   A CA    1 
ATOM   631   C  C     . ALA   A  1 107  ? -19.640 57.331  61.985  1.00 31.23 ? 105  ALA   A C     1 
ATOM   632   O  O     . ALA   A  1 107  ? -20.151 57.952  61.046  1.00 28.73 ? 105  ALA   A O     1 
ATOM   633   C  CB    . ALA   A  1 107  ? -19.164 54.871  61.789  1.00 23.50 ? 105  ALA   A CB    1 
ATOM   634   N  N     . GLU   A  1 108  ? -19.976 57.554  63.260  1.00 28.60 ? 106  GLU   A N     1 
ATOM   635   C  CA    . GLU   A  1 108  ? -20.905 58.623  63.624  1.00 29.12 ? 106  GLU   A CA    1 
ATOM   636   C  C     . GLU   A  1 108  ? -20.420 59.975  63.108  1.00 33.60 ? 106  GLU   A C     1 
ATOM   637   O  O     . GLU   A  1 108  ? -21.193 60.748  62.527  1.00 31.74 ? 106  GLU   A O     1 
ATOM   638   C  CB    . GLU   A  1 108  ? -21.080 58.658  65.146  1.00 27.83 ? 106  GLU   A CB    1 
ATOM   639   C  CG    . GLU   A  1 108  ? -21.826 59.868  65.671  1.00 33.60 ? 106  GLU   A CG    1 
ATOM   640   C  CD    . GLU   A  1 108  ? -21.601 60.105  67.157  1.00 37.96 ? 106  GLU   A CD    1 
ATOM   641   O  OE1   . GLU   A  1 108  ? -21.138 59.173  67.865  1.00 34.29 ? 106  GLU   A OE1   1 
ATOM   642   O  OE2   . GLU   A  1 108  ? -21.882 61.236  67.619  1.00 39.38 ? 106  GLU   A OE2   1 
ATOM   643   N  N     . ALA   A  1 109  ? -19.136 60.274  63.306  1.00 29.22 ? 107  ALA   A N     1 
ATOM   644   C  CA    . ALA   A  1 109  ? -18.586 61.543  62.841  1.00 35.73 ? 107  ALA   A CA    1 
ATOM   645   C  C     . ALA   A  1 109  ? -18.664 61.648  61.323  1.00 36.76 ? 107  ALA   A C     1 
ATOM   646   O  O     . ALA   A  1 109  ? -19.076 62.680  60.786  1.00 34.04 ? 107  ALA   A O     1 
ATOM   647   C  CB    . ALA   A  1 109  ? -17.143 61.698  63.320  1.00 35.56 ? 107  ALA   A CB    1 
ATOM   648   N  N     . LEU   A  1 110  ? -18.274 60.579  60.617  1.00 30.58 ? 108  LEU   A N     1 
ATOM   649   C  CA    . LEU   A  1 110  ? -18.362 60.561  59.158  1.00 32.68 ? 108  LEU   A CA    1 
ATOM   650   C  C     . LEU   A  1 110  ? -19.794 60.741  58.672  1.00 35.74 ? 108  LEU   A C     1 
ATOM   651   O  O     . LEU   A  1 110  ? -20.018 61.300  57.593  1.00 37.53 ? 108  LEU   A O     1 
ATOM   652   C  CB    . LEU   A  1 110  ? -17.794 59.253  58.610  1.00 27.84 ? 108  LEU   A CB    1 
ATOM   653   C  CG    . LEU   A  1 110  ? -16.270 59.192  58.691  1.00 31.73 ? 108  LEU   A CG    1 
ATOM   654   C  CD1   . LEU   A  1 110  ? -15.774 57.777  58.466  1.00 28.07 ? 108  LEU   A CD1   1 
ATOM   655   C  CD2   . LEU   A  1 110  ? -15.651 60.155  57.679  1.00 34.65 ? 108  LEU   A CD2   1 
ATOM   656   N  N     . LEU   A  1 111  ? -20.771 60.264  59.436  1.00 38.73 ? 109  LEU   A N     1 
ATOM   657   C  CA    . LEU   A  1 111  ? -22.164 60.450  59.056  1.00 38.98 ? 109  LEU   A CA    1 
ATOM   658   C  C     . LEU   A  1 111  ? -22.658 61.867  59.315  1.00 40.22 ? 109  LEU   A C     1 
ATOM   659   O  O     . LEU   A  1 111  ? -23.706 62.245  58.785  1.00 43.70 ? 109  LEU   A O     1 
ATOM   660   C  CB    . LEU   A  1 111  ? -23.042 59.431  59.783  1.00 34.39 ? 109  LEU   A CB    1 
ATOM   661   C  CG    . LEU   A  1 111  ? -22.785 58.020  59.257  1.00 33.59 ? 109  LEU   A CG    1 
ATOM   662   C  CD1   . LEU   A  1 111  ? -23.480 56.991  60.097  1.00 34.02 ? 109  LEU   A CD1   1 
ATOM   663   C  CD2   . LEU   A  1 111  ? -23.226 57.915  57.816  1.00 35.65 ? 109  LEU   A CD2   1 
ATOM   664   N  N     . ARG   A  1 112  ? -21.928 62.664  60.099  1.00 41.17 ? 110  ARG   A N     1 
ATOM   665   C  CA    . ARG   A  1 112  ? -22.245 64.085  60.172  1.00 42.02 ? 110  ARG   A CA    1 
ATOM   666   C  C     . ARG   A  1 112  ? -21.909 64.816  58.878  1.00 48.59 ? 110  ARG   A C     1 
ATOM   667   O  O     . ARG   A  1 112  ? -22.250 65.997  58.745  1.00 50.76 ? 110  ARG   A O     1 
ATOM   668   C  CB    . ARG   A  1 112  ? -21.522 64.734  61.351  1.00 43.41 ? 110  ARG   A CB    1 
ATOM   669   C  CG    . ARG   A  1 112  ? -22.012 64.229  62.701  1.00 41.25 ? 110  ARG   A CG    1 
ATOM   670   C  CD    . ARG   A  1 112  ? -21.609 65.157  63.840  1.00 48.47 ? 110  ARG   A CD    1 
ATOM   671   N  NE    . ARG   A  1 112  ? -20.229 64.974  64.275  1.00 52.13 ? 110  ARG   A NE    1 
ATOM   672   C  CZ    . ARG   A  1 112  ? -19.850 64.169  65.261  1.00 54.88 ? 110  ARG   A CZ    1 
ATOM   673   N  NH1   . ARG   A  1 112  ? -20.721 63.407  65.906  1.00 53.16 ? 110  ARG   A NH1   1 
ATOM   674   N  NH2   . ARG   A  1 112  ? -18.568 64.133  65.615  1.00 50.77 ? 110  ARG   A NH2   1 
ATOM   675   N  N     . ILE   A  1 113  ? -21.263 64.146  57.930  1.00 48.09 ? 111  ILE   A N     1 
ATOM   676   C  CA    . ILE   A  1 113  ? -21.024 64.693  56.599  1.00 47.12 ? 111  ILE   A CA    1 
ATOM   677   C  C     . ILE   A  1 113  ? -22.228 64.343  55.732  1.00 53.19 ? 111  ILE   A C     1 
ATOM   678   O  O     . ILE   A  1 113  ? -22.468 63.148  55.478  1.00 53.49 ? 111  ILE   A O     1 
ATOM   679   C  CB    . ILE   A  1 113  ? -19.731 64.137  55.990  1.00 48.25 ? 111  ILE   A CB    1 
ATOM   680   C  CG1   . ILE   A  1 113  ? -18.523 64.618  56.795  1.00 44.07 ? 111  ILE   A CG1   1 
ATOM   681   C  CG2   . ILE   A  1 113  ? -19.610 64.525  54.519  1.00 50.23 ? 111  ILE   A CG2   1 
ATOM   682   C  CD1   . ILE   A  1 113  ? -17.244 63.980  56.372  1.00 35.88 ? 111  ILE   A CD1   1 
ATOM   683   N  N     . PRO   A  1 114  ? -23.001 65.326  55.260  1.00 56.43 ? 112  PRO   A N     1 
ATOM   684   C  CA    . PRO   A  1 114  ? -24.257 64.990  54.571  1.00 55.32 ? 112  PRO   A CA    1 
ATOM   685   C  C     . PRO   A  1 114  ? -24.065 64.385  53.191  1.00 53.39 ? 112  PRO   A C     1 
ATOM   686   O  O     . PRO   A  1 114  ? -24.796 63.452  52.834  1.00 55.26 ? 112  PRO   A O     1 
ATOM   687   C  CB    . PRO   A  1 114  ? -24.988 66.339  54.511  1.00 60.88 ? 112  PRO   A CB    1 
ATOM   688   C  CG    . PRO   A  1 114  ? -24.344 67.178  55.577  1.00 57.64 ? 112  PRO   A CG    1 
ATOM   689   C  CD    . PRO   A  1 114  ? -22.909 66.759  55.575  1.00 58.03 ? 112  PRO   A CD    1 
ATOM   690   N  N     . ASP   A  1 115  ? -23.113 64.884  52.403  1.00 53.86 ? 113  ASP   A N     1 
ATOM   691   C  CA    . ASP   A  1 115  ? -22.967 64.460  51.012  1.00 53.28 ? 113  ASP   A CA    1 
ATOM   692   C  C     . ASP   A  1 115  ? -22.171 63.161  50.934  1.00 53.43 ? 113  ASP   A C     1 
ATOM   693   O  O     . ASP   A  1 115  ? -20.981 63.134  51.271  1.00 54.70 ? 113  ASP   A O     1 
ATOM   694   C  CB    . ASP   A  1 115  ? -22.292 65.557  50.192  1.00 50.98 ? 113  ASP   A CB    1 
ATOM   695   N  N     . THR   A  1 116  ? -22.822 62.096  50.458  1.00 48.25 ? 114  THR   A N     1 
ATOM   696   C  CA    . THR   A  1 116  ? -22.205 60.771  50.448  1.00 50.15 ? 114  THR   A CA    1 
ATOM   697   C  C     . THR   A  1 116  ? -20.892 60.763  49.672  1.00 53.95 ? 114  THR   A C     1 
ATOM   698   O  O     . THR   A  1 116  ? -19.879 60.241  50.153  1.00 53.33 ? 114  THR   A O     1 
ATOM   699   C  CB    . THR   A  1 116  ? -23.179 59.748  49.864  1.00 50.16 ? 114  THR   A CB    1 
ATOM   700   O  OG1   . THR   A  1 116  ? -24.241 59.507  50.798  1.00 49.45 ? 114  THR   A OG1   1 
ATOM   701   C  CG2   . THR   A  1 116  ? -22.459 58.437  49.556  1.00 48.53 ? 114  THR   A CG2   1 
ATOM   702   N  N     . ALA   A  1 117  ? -20.887 61.327  48.463  1.00 51.43 ? 115  ALA   A N     1 
ATOM   703   C  CA    . ALA   A  1 117  ? -19.649 61.379  47.692  1.00 50.15 ? 115  ALA   A CA    1 
ATOM   704   C  C     . ALA   A  1 117  ? -18.564 62.143  48.442  1.00 49.49 ? 115  ALA   A C     1 
ATOM   705   O  O     . ALA   A  1 117  ? -17.385 61.777  48.384  1.00 54.00 ? 115  ALA   A O     1 
ATOM   706   C  CB    . ALA   A  1 117  ? -19.906 62.007  46.322  1.00 48.47 ? 115  ALA   A CB    1 
ATOM   707   N  N     . THR   A  1 118  ? -18.945 63.204  49.159  1.00 50.53 ? 116  THR   A N     1 
ATOM   708   C  CA    . THR   A  1 118  ? -17.975 63.950  49.956  1.00 50.65 ? 116  THR   A CA    1 
ATOM   709   C  C     . THR   A  1 118  ? -17.410 63.085  51.075  1.00 50.93 ? 116  THR   A C     1 
ATOM   710   O  O     . THR   A  1 118  ? -16.204 63.108  51.346  1.00 46.58 ? 116  THR   A O     1 
ATOM   711   C  CB    . THR   A  1 118  ? -18.631 65.202  50.538  1.00 52.03 ? 116  THR   A CB    1 
ATOM   712   O  OG1   . THR   A  1 118  ? -19.296 65.925  49.494  1.00 56.60 ? 116  THR   A OG1   1 
ATOM   713   C  CG2   . THR   A  1 118  ? -17.594 66.098  51.193  1.00 46.27 ? 116  THR   A CG2   1 
ATOM   714   N  N     . ARG   A  1 119  ? -18.276 62.319  51.734  1.00 48.77 ? 117  ARG   A N     1 
ATOM   715   C  CA    . ARG   A  1 119  ? -17.844 61.433  52.807  1.00 50.16 ? 117  ARG   A CA    1 
ATOM   716   C  C     . ARG   A  1 119  ? -16.984 60.295  52.267  1.00 46.69 ? 117  ARG   A C     1 
ATOM   717   O  O     . ARG   A  1 119  ? -15.944 59.961  52.845  1.00 44.79 ? 117  ARG   A O     1 
ATOM   718   C  CB    . ARG   A  1 119  ? -19.076 60.894  53.534  1.00 46.44 ? 117  ARG   A CB    1 
ATOM   719   C  CG    . ARG   A  1 119  ? -18.809 59.987  54.717  1.00 41.63 ? 117  ARG   A CG    1 
ATOM   720   C  CD    . ARG   A  1 119  ? -20.073 59.212  55.022  1.00 38.08 ? 117  ARG   A CD    1 
ATOM   721   N  NE    . ARG   A  1 119  ? -21.232 60.097  55.041  1.00 44.11 ? 117  ARG   A NE    1 
ATOM   722   C  CZ    . ARG   A  1 119  ? -22.421 59.787  54.542  1.00 45.18 ? 117  ARG   A CZ    1 
ATOM   723   N  NH1   . ARG   A  1 119  ? -22.644 58.622  53.956  1.00 43.16 ? 117  ARG   A NH1   1 
ATOM   724   N  NH2   . ARG   A  1 119  ? -23.411 60.672  54.629  1.00 56.33 ? 117  ARG   A NH2   1 
ATOM   725   N  N     . ASP   A  1 120  ? -17.404 59.688  51.153  1.00 48.35 ? 118  ASP   A N     1 
ATOM   726   C  CA    . ASP   A  1 120  ? -16.642 58.583  50.580  1.00 46.84 ? 118  ASP   A CA    1 
ATOM   727   C  C     . ASP   A  1 120  ? -15.272 59.045  50.110  1.00 47.17 ? 118  ASP   A C     1 
ATOM   728   O  O     . ASP   A  1 120  ? -14.290 58.297  50.203  1.00 44.72 ? 118  ASP   A O     1 
ATOM   729   C  CB    . ASP   A  1 120  ? -17.426 57.943  49.436  1.00 46.93 ? 118  ASP   A CB    1 
ATOM   730   C  CG    . ASP   A  1 120  ? -18.727 57.338  49.904  1.00 53.01 ? 118  ASP   A CG    1 
ATOM   731   O  OD1   . ASP   A  1 120  ? -18.866 57.142  51.129  1.00 47.35 ? 118  ASP   A OD1   1 
ATOM   732   O  OD2   . ASP   A  1 120  ? -19.607 57.056  49.063  1.00 57.17 ? 118  ASP   A OD2   1 
ATOM   733   N  N     . ALA   A  1 121  ? -15.182 60.281  49.613  1.00 47.11 ? 119  ALA   A N     1 
ATOM   734   C  CA    . ALA   A  1 121  ? -13.887 60.829  49.228  1.00 48.28 ? 119  ALA   A CA    1 
ATOM   735   C  C     . ALA   A  1 121  ? -13.001 61.045  50.445  1.00 44.50 ? 119  ALA   A C     1 
ATOM   736   O  O     . ALA   A  1 121  ? -11.790 60.803  50.391  1.00 43.54 ? 119  ALA   A O     1 
ATOM   737   C  CB    . ALA   A  1 121  ? -14.076 62.139  48.463  1.00 49.28 ? 119  ALA   A CB    1 
ATOM   738   N  N     . LEU   A  1 122  ? -13.586 61.508  51.552  1.00 44.94 ? 120  LEU   A N     1 
ATOM   739   C  CA    . LEU   A  1 122  ? -12.806 61.709  52.767  1.00 43.15 ? 120  LEU   A CA    1 
ATOM   740   C  C     . LEU   A  1 122  ? -12.251 60.387  53.284  1.00 40.67 ? 120  LEU   A C     1 
ATOM   741   O  O     . LEU   A  1 122  ? -11.092 60.312  53.709  1.00 39.16 ? 120  LEU   A O     1 
ATOM   742   C  CB    . LEU   A  1 122  ? -13.668 62.378  53.837  1.00 42.19 ? 120  LEU   A CB    1 
ATOM   743   C  CG    . LEU   A  1 122  ? -12.845 62.997  54.965  1.00 46.10 ? 120  LEU   A CG    1 
ATOM   744   C  CD1   . LEU   A  1 122  ? -11.945 64.069  54.394  1.00 43.38 ? 120  LEU   A CD1   1 
ATOM   745   C  CD2   . LEU   A  1 122  ? -13.738 63.565  56.057  1.00 44.74 ? 120  LEU   A CD2   1 
ATOM   746   N  N     . ILE   A  1 123  ? -13.073 59.337  53.260  1.00 41.59 ? 121  ILE   A N     1 
ATOM   747   C  CA    . ILE   A  1 123  ? -12.638 58.027  53.736  1.00 39.17 ? 121  ILE   A CA    1 
ATOM   748   C  C     . ILE   A  1 123  ? -11.477 57.515  52.891  1.00 43.42 ? 121  ILE   A C     1 
ATOM   749   O  O     . ILE   A  1 123  ? -10.406 57.175  53.411  1.00 35.76 ? 121  ILE   A O     1 
ATOM   750   C  CB    . ILE   A  1 123  ? -13.823 57.046  53.727  1.00 37.47 ? 121  ILE   A CB    1 
ATOM   751   C  CG1   . ILE   A  1 123  ? -14.884 57.487  54.741  1.00 37.18 ? 121  ILE   A CG1   1 
ATOM   752   C  CG2   . ILE   A  1 123  ? -13.352 55.630  53.987  1.00 37.09 ? 121  ILE   A CG2   1 
ATOM   753   C  CD1   . ILE   A  1 123  ? -16.164 56.697  54.656  1.00 34.92 ? 121  ILE   A CD1   1 
ATOM   754   N  N     . ARG   A  1 124  ? -11.664 57.490  51.568  1.00 43.19 ? 122  ARG   A N     1 
ATOM   755   C  CA    . ARG   A  1 124  ? -10.652 56.925  50.677  1.00 45.54 ? 122  ARG   A CA    1 
ATOM   756   C  C     . ARG   A  1 124  ? -9.360  57.733  50.700  1.00 44.81 ? 122  ARG   A C     1 
ATOM   757   O  O     . ARG   A  1 124  ? -8.263  57.163  50.666  1.00 45.31 ? 122  ARG   A O     1 
ATOM   758   C  CB    . ARG   A  1 124  ? -11.198 56.846  49.250  1.00 39.35 ? 122  ARG   A CB    1 
ATOM   759   N  N     . ASP   A  1 125  ? -9.464  59.059  50.766  1.00 43.40 ? 123  ASP   A N     1 
ATOM   760   C  CA    . ASP   A  1 125  ? -8.306  59.917  50.565  1.00 45.82 ? 123  ASP   A CA    1 
ATOM   761   C  C     . ASP   A  1 125  ? -7.666  60.412  51.853  1.00 43.66 ? 123  ASP   A C     1 
ATOM   762   O  O     . ASP   A  1 125  ? -6.475  60.743  51.838  1.00 51.79 ? 123  ASP   A O     1 
ATOM   763   C  CB    . ASP   A  1 125  ? -8.686  61.132  49.705  1.00 52.98 ? 123  ASP   A CB    1 
ATOM   764   C  CG    . ASP   A  1 125  ? -9.286  60.738  48.363  1.00 52.53 ? 123  ASP   A CG    1 
ATOM   765   O  OD1   . ASP   A  1 125  ? -8.868  59.709  47.791  1.00 50.82 ? 123  ASP   A OD1   1 
ATOM   766   O  OD2   . ASP   A  1 125  ? -10.186 61.458  47.883  1.00 57.55 ? 123  ASP   A OD2   1 
ATOM   767   N  N     . LYS   A  1 126  ? -8.400  60.469  52.960  1.00 39.52 ? 124  LYS   A N     1 
ATOM   768   C  CA    . LYS   A  1 126  ? -7.823  61.029  54.177  1.00 45.13 ? 124  LYS   A CA    1 
ATOM   769   C  C     . LYS   A  1 126  ? -7.948  60.090  55.374  1.00 42.95 ? 124  LYS   A C     1 
ATOM   770   O  O     . LYS   A  1 126  ? -6.974  59.873  56.100  1.00 42.98 ? 124  LYS   A O     1 
ATOM   771   C  CB    . LYS   A  1 126  ? -8.475  62.379  54.496  1.00 46.40 ? 124  LYS   A CB    1 
ATOM   772   N  N     . ILE   A  1 127  ? -9.139  59.531  55.597  1.00 39.96 ? 125  ILE   A N     1 
ATOM   773   C  CA    . ILE   A  1 127  ? -9.360  58.731  56.800  1.00 38.48 ? 125  ILE   A CA    1 
ATOM   774   C  C     . ILE   A  1 127  ? -8.595  57.416  56.712  1.00 40.36 ? 125  ILE   A C     1 
ATOM   775   O  O     . ILE   A  1 127  ? -7.861  57.045  57.634  1.00 42.78 ? 125  ILE   A O     1 
ATOM   776   C  CB    . ILE   A  1 127  ? -10.861 58.485  57.024  1.00 38.47 ? 125  ILE   A CB    1 
ATOM   777   C  CG1   . ILE   A  1 127  ? -11.661 59.792  56.920  1.00 40.30 ? 125  ILE   A CG1   1 
ATOM   778   C  CG2   . ILE   A  1 127  ? -11.074 57.798  58.365  1.00 36.57 ? 125  ILE   A CG2   1 
ATOM   779   C  CD1   . ILE   A  1 127  ? -11.251 60.865  57.910  1.00 40.47 ? 125  ILE   A CD1   1 
ATOM   780   N  N     . ALA   A  1 128  ? -8.759  56.690  55.603  1.00 37.00 ? 126  ALA   A N     1 
ATOM   781   C  CA    . ALA   A  1 128  ? -8.108  55.397  55.435  1.00 37.11 ? 126  ALA   A CA    1 
ATOM   782   C  C     . ALA   A  1 128  ? -6.592  55.491  55.455  1.00 42.60 ? 126  ALA   A C     1 
ATOM   783   O  O     . ALA   A  1 128  ? -5.930  54.458  55.604  1.00 41.44 ? 126  ALA   A O     1 
ATOM   784   C  CB    . ALA   A  1 128  ? -8.558  54.739  54.130  1.00 34.78 ? 126  ALA   A CB    1 
ATOM   785   N  N     . ASP   A  1 129  ? -6.029  56.690  55.316  1.00 42.26 ? 127  ASP   A N     1 
ATOM   786   C  CA    . ASP   A  1 129  ? -4.590  56.898  55.360  1.00 45.53 ? 127  ASP   A CA    1 
ATOM   787   C  C     . ASP   A  1 129  ? -4.108  57.345  56.735  1.00 47.36 ? 127  ASP   A C     1 
ATOM   788   O  O     . ASP   A  1 129  ? -2.955  57.763  56.869  1.00 49.78 ? 127  ASP   A O     1 
ATOM   789   C  CB    . ASP   A  1 129  ? -4.172  57.918  54.298  1.00 50.44 ? 127  ASP   A CB    1 
ATOM   790   N  N     . GLY   A  1 130  ? -4.964  57.272  57.757  1.00 48.62 ? 128  GLY   A N     1 
ATOM   791   C  CA    . GLY   A  1 130  ? -4.592  57.590  59.116  1.00 46.82 ? 128  GLY   A CA    1 
ATOM   792   C  C     . GLY   A  1 130  ? -4.903  59.008  59.548  1.00 51.23 ? 128  GLY   A C     1 
ATOM   793   O  O     . GLY   A  1 130  ? -4.980  59.270  60.755  1.00 47.84 ? 128  GLY   A O     1 
ATOM   794   N  N     . ASN   A  1 131  ? -5.086  59.928  58.599  1.00 53.44 ? 129  ASN   A N     1 
ATOM   795   C  CA    . ASN   A  1 131  ? -5.381  61.324  58.917  1.00 53.94 ? 129  ASN   A CA    1 
ATOM   796   C  C     . ASN   A  1 131  ? -6.881  61.447  59.170  1.00 54.98 ? 129  ASN   A C     1 
ATOM   797   O  O     . ASN   A  1 131  ? -7.676  61.787  58.288  1.00 57.21 ? 129  ASN   A O     1 
ATOM   798   C  CB    . ASN   A  1 131  ? -4.917  62.247  57.796  1.00 53.49 ? 129  ASN   A CB    1 
ATOM   799   N  N     . TRP   A  1 132  ? -7.274  61.143  60.408  1.00 52.92 ? 130  TRP   A N     1 
ATOM   800   C  CA    . TRP   A  1 132  ? -8.670  61.218  60.804  1.00 51.59 ? 130  TRP   A CA    1 
ATOM   801   C  C     . TRP   A  1 132  ? -8.964  62.333  61.797  1.00 54.27 ? 130  TRP   A C     1 
ATOM   802   O  O     . TRP   A  1 132  ? -10.116 62.770  61.884  1.00 57.32 ? 130  TRP   A O     1 
ATOM   803   C  CB    . TRP   A  1 132  ? -9.136  59.875  61.394  1.00 49.32 ? 130  TRP   A CB    1 
ATOM   804   C  CG    . TRP   A  1 132  ? -8.318  59.352  62.570  1.00 42.36 ? 130  TRP   A CG    1 
ATOM   805   C  CD1   . TRP   A  1 132  ? -7.303  58.429  62.525  1.00 36.63 ? 130  TRP   A CD1   1 
ATOM   806   C  CD2   . TRP   A  1 132  ? -8.471  59.708  63.951  1.00 33.97 ? 130  TRP   A CD2   1 
ATOM   807   N  NE1   . TRP   A  1 132  ? -6.819  58.196  63.792  1.00 36.95 ? 130  TRP   A NE1   1 
ATOM   808   C  CE2   . TRP   A  1 132  ? -7.514  58.973  64.683  1.00 33.55 ? 130  TRP   A CE2   1 
ATOM   809   C  CE3   . TRP   A  1 132  ? -9.313  60.586  64.636  1.00 37.58 ? 130  TRP   A CE3   1 
ATOM   810   C  CZ2   . TRP   A  1 132  ? -7.383  59.089  66.063  1.00 30.69 ? 130  TRP   A CZ2   1 
ATOM   811   C  CZ3   . TRP   A  1 132  ? -9.181  60.703  66.002  1.00 33.35 ? 130  TRP   A CZ3   1 
ATOM   812   C  CH2   . TRP   A  1 132  ? -8.225  59.960  66.705  1.00 29.78 ? 130  TRP   A CH2   1 
ATOM   813   N  N     . LYS   A  1 133  ? -7.961  62.804  62.537  1.00 59.80 ? 131  LYS   A N     1 
ATOM   814   C  CA    . LYS   A  1 133  ? -8.190  63.873  63.503  1.00 63.04 ? 131  LYS   A CA    1 
ATOM   815   C  C     . LYS   A  1 133  ? -8.256  65.235  62.825  1.00 67.38 ? 131  LYS   A C     1 
ATOM   816   O  O     . LYS   A  1 133  ? -9.025  66.105  63.248  1.00 72.09 ? 131  LYS   A O     1 
ATOM   817   C  CB    . LYS   A  1 133  ? -7.093  63.861  64.571  1.00 61.10 ? 131  LYS   A CB    1 
ATOM   818   N  N     . SER   A  1 134  ? -7.463  65.433  61.768  1.00 72.60 ? 132  SER   A N     1 
ATOM   819   C  CA    . SER   A  1 134  ? -7.410  66.725  61.095  1.00 72.00 ? 132  SER   A CA    1 
ATOM   820   C  C     . SER   A  1 134  ? -8.683  67.037  60.320  1.00 73.08 ? 132  SER   A C     1 
ATOM   821   O  O     . SER   A  1 134  ? -8.935  68.209  60.017  1.00 72.92 ? 132  SER   A O     1 
ATOM   822   C  CB    . SER   A  1 134  ? -6.207  66.775  60.150  1.00 72.07 ? 132  SER   A CB    1 
ATOM   823   N  N     . HIS   A  1 135  ? -9.490  66.024  59.999  1.00 72.52 ? 133  HIS   A N     1 
ATOM   824   C  CA    . HIS   A  1 135  ? -10.661 66.207  59.151  1.00 68.81 ? 133  HIS   A CA    1 
ATOM   825   C  C     . HIS   A  1 135  ? -11.981 66.186  59.913  1.00 70.08 ? 133  HIS   A C     1 
ATOM   826   O  O     . HIS   A  1 135  ? -13.018 66.509  59.322  1.00 71.74 ? 133  HIS   A O     1 
ATOM   827   C  CB    . HIS   A  1 135  ? -10.692 65.129  58.059  1.00 63.91 ? 133  HIS   A CB    1 
ATOM   828   N  N     . LEU   A  1 136  ? -11.980 65.822  61.194  1.00 67.88 ? 134  LEU   A N     1 
ATOM   829   C  CA    . LEU   A  1 136  ? -13.236 65.674  61.931  1.00 66.76 ? 134  LEU   A CA    1 
ATOM   830   C  C     . LEU   A  1 136  ? -13.165 66.221  63.361  1.00 67.00 ? 134  LEU   A C     1 
ATOM   831   O  O     . LEU   A  1 136  ? -12.095 66.283  63.972  1.00 69.15 ? 134  LEU   A O     1 
ATOM   832   C  CB    . LEU   A  1 136  ? -13.653 64.200  61.961  1.00 60.60 ? 134  LEU   A CB    1 
ATOM   833   C  CG    . LEU   A  1 136  ? -13.987 63.540  60.620  1.00 50.75 ? 134  LEU   A CG    1 
ATOM   834   C  CD1   . LEU   A  1 136  ? -13.883 62.033  60.718  1.00 44.26 ? 134  LEU   A CD1   1 
ATOM   835   C  CD2   . LEU   A  1 136  ? -15.372 63.947  60.159  1.00 51.96 ? 134  LEU   A CD2   1 
ATOM   836   N  N     . ARG   A  1 140  ? -14.365 69.415  68.515  1.00 30.36 ? 138  ARG   A N     1 
ATOM   837   C  CA    . ARG   A  1 140  ? -15.009 68.402  69.347  1.00 33.18 ? 138  ARG   A CA    1 
ATOM   838   C  C     . ARG   A  1 140  ? -14.374 67.019  69.147  1.00 35.61 ? 138  ARG   A C     1 
ATOM   839   O  O     . ARG   A  1 140  ? -14.109 66.600  68.017  1.00 35.31 ? 138  ARG   A O     1 
ATOM   840   C  CB    . ARG   A  1 140  ? -16.507 68.339  69.050  1.00 36.86 ? 138  ARG   A CB    1 
ATOM   841   N  N     . SER   A  1 141  ? -14.125 66.330  70.258  1.00 32.04 ? 139  SER   A N     1 
ATOM   842   C  CA    . SER   A  1 141  ? -13.561 64.988  70.209  1.00 31.25 ? 139  SER   A CA    1 
ATOM   843   C  C     . SER   A  1 141  ? -14.433 64.061  69.369  1.00 30.09 ? 139  SER   A C     1 
ATOM   844   O  O     . SER   A  1 141  ? -15.660 64.126  69.407  1.00 25.51 ? 139  SER   A O     1 
ATOM   845   C  CB    . SER   A  1 141  ? -13.418 64.437  71.630  1.00 28.61 ? 139  SER   A CB    1 
ATOM   846   O  OG    . SER   A  1 141  ? -13.063 63.064  71.625  1.00 26.73 ? 139  SER   A OG    1 
ATOM   847   N  N     . LEU   A  1 142  ? -13.786 63.194  68.588  1.00 26.93 ? 140  LEU   A N     1 
ATOM   848   C  CA    . LEU   A  1 142  ? -14.507 62.127  67.905  1.00 24.98 ? 140  LEU   A CA    1 
ATOM   849   C  C     . LEU   A  1 142  ? -15.312 61.260  68.869  1.00 23.70 ? 140  LEU   A C     1 
ATOM   850   O  O     . LEU   A  1 142  ? -16.304 60.639  68.464  1.00 23.11 ? 140  LEU   A O     1 
ATOM   851   C  CB    . LEU   A  1 142  ? -13.502 61.254  67.145  1.00 25.46 ? 140  LEU   A CB    1 
ATOM   852   C  CG    . LEU   A  1 142  ? -13.902 60.869  65.733  1.00 30.07 ? 140  LEU   A CG    1 
ATOM   853   C  CD1   . LEU   A  1 142  ? -13.817 62.103  64.861  1.00 36.36 ? 140  LEU   A CD1   1 
ATOM   854   C  CD2   . LEU   A  1 142  ? -12.989 59.780  65.228  1.00 31.32 ? 140  LEU   A CD2   1 
ATOM   855   N  N     . PHE   A  1 143  ? -14.929 61.228  70.144  1.00 21.21 ? 141  PHE   A N     1 
ATOM   856   C  CA    . PHE   A  1 143  ? -15.411 60.218  71.073  1.00 21.15 ? 141  PHE   A CA    1 
ATOM   857   C  C     . PHE   A  1 143  ? -16.383 60.781  72.102  1.00 21.95 ? 141  PHE   A C     1 
ATOM   858   O  O     . PHE   A  1 143  ? -16.585 60.168  73.158  1.00 21.69 ? 141  PHE   A O     1 
ATOM   859   C  CB    . PHE   A  1 143  ? -14.205 59.555  71.739  1.00 21.93 ? 141  PHE   A CB    1 
ATOM   860   C  CG    . PHE   A  1 143  ? -13.153 59.143  70.749  1.00 20.41 ? 141  PHE   A CG    1 
ATOM   861   C  CD1   . PHE   A  1 143  ? -13.418 58.141  69.841  1.00 17.50 ? 141  PHE   A CD1   1 
ATOM   862   C  CD2   . PHE   A  1 143  ? -11.925 59.784  70.697  1.00 20.60 ? 141  PHE   A CD2   1 
ATOM   863   C  CE1   . PHE   A  1 143  ? -12.476 57.769  68.895  1.00 19.99 ? 141  PHE   A CE1   1 
ATOM   864   C  CE2   . PHE   A  1 143  ? -10.977 59.411  69.771  1.00 20.45 ? 141  PHE   A CE2   1 
ATOM   865   C  CZ    . PHE   A  1 143  ? -11.250 58.403  68.863  1.00 21.18 ? 141  PHE   A CZ    1 
ATOM   866   N  N     . VAL   A  1 144  ? -17.017 61.920  71.804  1.00 22.85 ? 142  VAL   A N     1 
ATOM   867   C  CA    . VAL   A  1 144  ? -17.940 62.516  72.773  1.00 23.35 ? 142  VAL   A CA    1 
ATOM   868   C  C     . VAL   A  1 144  ? -19.064 61.559  73.140  1.00 22.27 ? 142  VAL   A C     1 
ATOM   869   O  O     . VAL   A  1 144  ? -19.549 61.574  74.277  1.00 26.43 ? 142  VAL   A O     1 
ATOM   870   C  CB    . VAL   A  1 144  ? -18.496 63.858  72.252  1.00 23.35 ? 142  VAL   A CB    1 
ATOM   871   C  CG1   . VAL   A  1 144  ? -17.371 64.877  72.147  1.00 27.37 ? 142  VAL   A CG1   1 
ATOM   872   C  CG2   . VAL   A  1 144  ? -19.177 63.682  70.917  1.00 26.56 ? 142  VAL   A CG2   1 
ATOM   873   N  N     . ASN   A  1 145  ? -19.501 60.715  72.209  1.00 21.78 ? 143  ASN   A N     1 
ATOM   874   C  CA    . ASN   A  1 145  ? -20.593 59.788  72.485  1.00 23.15 ? 143  ASN   A CA    1 
ATOM   875   C  C     . ASN   A  1 145  ? -20.107 58.359  72.678  1.00 25.32 ? 143  ASN   A C     1 
ATOM   876   O  O     . ASN   A  1 145  ? -20.896 57.412  72.566  1.00 22.83 ? 143  ASN   A O     1 
ATOM   877   C  CB    . ASN   A  1 145  ? -21.639 59.864  71.376  1.00 30.50 ? 143  ASN   A CB    1 
ATOM   878   C  CG    . ASN   A  1 145  ? -22.403 61.157  71.420  1.00 30.52 ? 143  ASN   A CG    1 
ATOM   879   O  OD1   . ASN   A  1 145  ? -22.862 61.577  72.486  1.00 34.15 ? 143  ASN   A OD1   1 
ATOM   880   N  ND2   . ASN   A  1 145  ? -22.508 61.821  70.284  1.00 29.00 ? 143  ASN   A ND2   1 
ATOM   881   N  N     . ALA   A  1 146  ? -18.824 58.192  72.994  1.00 21.18 ? 144  ALA   A N     1 
ATOM   882   C  CA    . ALA   A  1 146  ? -18.260 56.852  73.115  1.00 23.58 ? 144  ALA   A CA    1 
ATOM   883   C  C     . ALA   A  1 146  ? -18.922 56.043  74.225  1.00 21.53 ? 144  ALA   A C     1 
ATOM   884   O  O     . ALA   A  1 146  ? -18.946 54.812  74.151  1.00 23.74 ? 144  ALA   A O     1 
ATOM   885   C  CB    . ALA   A  1 146  ? -16.753 56.949  73.362  1.00 19.29 ? 144  ALA   A CB    1 
ATOM   886   N  N     . ALA   A  1 147  ? -19.448 56.708  75.265  1.00 22.86 ? 145  ALA   A N     1 
ATOM   887   C  CA    . ALA   A  1 147  ? -20.127 55.976  76.332  1.00 25.06 ? 145  ALA   A CA    1 
ATOM   888   C  C     . ALA   A  1 147  ? -21.324 55.217  75.784  1.00 25.02 ? 145  ALA   A C     1 
ATOM   889   O  O     . ALA   A  1 147  ? -21.588 54.077  76.185  1.00 27.09 ? 145  ALA   A O     1 
ATOM   890   C  CB    . ALA   A  1 147  ? -20.560 56.933  77.448  1.00 25.51 ? 145  ALA   A CB    1 
ATOM   891   N  N     . THR   A  1 148  ? -22.046 55.833  74.846  1.00 22.74 ? 146  THR   A N     1 
ATOM   892   C  CA    . THR   A  1 148  ? -23.169 55.174  74.198  1.00 22.22 ? 146  THR   A CA    1 
ATOM   893   C  C     . THR   A  1 148  ? -22.695 54.011  73.344  1.00 22.94 ? 146  THR   A C     1 
ATOM   894   O  O     . THR   A  1 148  ? -23.210 52.896  73.453  1.00 22.79 ? 146  THR   A O     1 
ATOM   895   C  CB    . THR   A  1 148  ? -23.935 56.194  73.352  1.00 30.50 ? 146  THR   A CB    1 
ATOM   896   O  OG1   . THR   A  1 148  ? -24.348 57.277  74.195  1.00 33.05 ? 146  THR   A OG1   1 
ATOM   897   C  CG2   . THR   A  1 148  ? -25.150 55.563  72.681  1.00 27.80 ? 146  THR   A CG2   1 
ATOM   898   N  N     . TRP   A  1 149  ? -21.703 54.254  72.490  1.00 21.18 ? 147  TRP   A N     1 
ATOM   899   C  CA    . TRP   A  1 149  ? -21.173 53.181  71.660  1.00 21.84 ? 147  TRP   A CA    1 
ATOM   900   C  C     . TRP   A  1 149  ? -20.545 52.085  72.502  1.00 20.95 ? 147  TRP   A C     1 
ATOM   901   O  O     . TRP   A  1 149  ? -20.618 50.907  72.135  1.00 24.63 ? 147  TRP   A O     1 
ATOM   902   C  CB    . TRP   A  1 149  ? -20.166 53.743  70.657  1.00 22.57 ? 147  TRP   A CB    1 
ATOM   903   C  CG    . TRP   A  1 149  ? -20.835 54.604  69.636  1.00 23.67 ? 147  TRP   A CG    1 
ATOM   904   C  CD1   . TRP   A  1 149  ? -20.642 55.940  69.429  1.00 24.07 ? 147  TRP   A CD1   1 
ATOM   905   C  CD2   . TRP   A  1 149  ? -21.834 54.190  68.694  1.00 24.73 ? 147  TRP   A CD2   1 
ATOM   906   N  NE1   . TRP   A  1 149  ? -21.451 56.380  68.403  1.00 26.67 ? 147  TRP   A NE1   1 
ATOM   907   C  CE2   . TRP   A  1 149  ? -22.195 55.326  67.940  1.00 28.17 ? 147  TRP   A CE2   1 
ATOM   908   C  CE3   . TRP   A  1 149  ? -22.455 52.970  68.415  1.00 26.29 ? 147  TRP   A CE3   1 
ATOM   909   C  CZ2   . TRP   A  1 149  ? -23.147 55.275  66.923  1.00 29.71 ? 147  TRP   A CZ2   1 
ATOM   910   C  CZ3   . TRP   A  1 149  ? -23.406 52.922  67.397  1.00 32.41 ? 147  TRP   A CZ3   1 
ATOM   911   C  CH2   . TRP   A  1 149  ? -23.741 54.068  66.670  1.00 31.14 ? 147  TRP   A CH2   1 
ATOM   912   N  N     . GLY   A  1 150  ? -19.919 52.448  73.625  1.00 20.42 ? 148  GLY   A N     1 
ATOM   913   C  CA    . GLY   A  1 150  ? -19.420 51.427  74.531  1.00 20.90 ? 148  GLY   A CA    1 
ATOM   914   C  C     . GLY   A  1 150  ? -20.527 50.513  75.014  1.00 25.94 ? 148  GLY   A C     1 
ATOM   915   O  O     . GLY   A  1 150  ? -20.368 49.291  75.058  1.00 25.82 ? 148  GLY   A O     1 
ATOM   916   N  N     . LEU   A  1 151  ? -21.675 51.096  75.369  1.00 24.59 ? 149  LEU   A N     1 
ATOM   917   C  CA    . LEU   A  1 151  ? -22.819 50.285  75.764  1.00 26.13 ? 149  LEU   A CA    1 
ATOM   918   C  C     . LEU   A  1 151  ? -23.252 49.385  74.617  1.00 24.52 ? 149  LEU   A C     1 
ATOM   919   O  O     . LEU   A  1 151  ? -23.487 48.186  74.810  1.00 29.03 ? 149  LEU   A O     1 
ATOM   920   C  CB    . LEU   A  1 151  ? -23.958 51.199  76.226  1.00 27.86 ? 149  LEU   A CB    1 
ATOM   921   C  CG    . LEU   A  1 151  ? -25.117 50.570  76.990  1.00 32.64 ? 149  LEU   A CG    1 
ATOM   922   C  CD1   . LEU   A  1 151  ? -24.607 49.717  78.132  1.00 31.79 ? 149  LEU   A CD1   1 
ATOM   923   C  CD2   . LEU   A  1 151  ? -26.015 51.672  77.527  1.00 32.44 ? 149  LEU   A CD2   1 
ATOM   924   N  N     . VAL   A  1 152  ? -23.301 49.933  73.404  1.00 25.30 ? 150  VAL   A N     1 
ATOM   925   C  CA    . VAL   A  1 152  ? -23.662 49.141  72.228  1.00 25.47 ? 150  VAL   A CA    1 
ATOM   926   C  C     . VAL   A  1 152  ? -22.680 47.990  72.031  1.00 28.72 ? 150  VAL   A C     1 
ATOM   927   O  O     . VAL   A  1 152  ? -23.077 46.842  71.804  1.00 27.48 ? 150  VAL   A O     1 
ATOM   928   C  CB    . VAL   A  1 152  ? -23.726 50.040  70.978  1.00 27.68 ? 150  VAL   A CB    1 
ATOM   929   C  CG1   . VAL   A  1 152  ? -23.814 49.196  69.711  1.00 31.12 ? 150  VAL   A CG1   1 
ATOM   930   C  CG2   . VAL   A  1 152  ? -24.883 51.022  71.074  1.00 24.63 ? 150  VAL   A CG2   1 
ATOM   931   N  N     . VAL   A  1 153  ? -21.380 48.279  72.110  1.00 24.96 ? 151  VAL   A N     1 
ATOM   932   C  CA    . VAL   A  1 153  ? -20.382 47.279  71.743  1.00 26.47 ? 151  VAL   A CA    1 
ATOM   933   C  C     . VAL   A  1 153  ? -20.164 46.276  72.868  1.00 27.45 ? 151  VAL   A C     1 
ATOM   934   O  O     . VAL   A  1 153  ? -20.029 45.070  72.624  1.00 29.97 ? 151  VAL   A O     1 
ATOM   935   C  CB    . VAL   A  1 153  ? -19.066 47.975  71.345  1.00 23.52 ? 151  VAL   A CB    1 
ATOM   936   C  CG1   . VAL   A  1 153  ? -17.962 46.959  71.147  1.00 25.59 ? 151  VAL   A CG1   1 
ATOM   937   C  CG2   . VAL   A  1 153  ? -19.263 48.798  70.089  1.00 23.46 ? 151  VAL   A CG2   1 
ATOM   938   N  N     . THR   A  1 154  ? -20.102 46.749  74.112  1.00 26.39 ? 152  THR   A N     1 
ATOM   939   C  CA    . THR   A  1 154  ? -19.701 45.909  75.230  1.00 28.50 ? 152  THR   A CA    1 
ATOM   940   C  C     . THR   A  1 154  ? -20.827 45.595  76.202  1.00 29.94 ? 152  THR   A C     1 
ATOM   941   O  O     . THR   A  1 154  ? -20.648 44.726  77.062  1.00 32.59 ? 152  THR   A O     1 
ATOM   942   C  CB    . THR   A  1 154  ? -18.556 46.567  76.016  1.00 27.02 ? 152  THR   A CB    1 
ATOM   943   O  OG1   . THR   A  1 154  ? -19.057 47.699  76.745  1.00 28.40 ? 152  THR   A OG1   1 
ATOM   944   C  CG2   . THR   A  1 154  ? -17.458 47.019  75.070  1.00 29.50 ? 152  THR   A CG2   1 
ATOM   945   N  N     . GLY   A  1 155  ? -21.964 46.279  76.112  1.00 27.41 ? 153  GLY   A N     1 
ATOM   946   C  CA    . GLY   A  1 155  ? -22.987 46.123  77.126  1.00 28.30 ? 153  GLY   A CA    1 
ATOM   947   C  C     . GLY   A  1 155  ? -22.665 46.763  78.457  1.00 34.08 ? 153  GLY   A C     1 
ATOM   948   O  O     . GLY   A  1 155  ? -23.430 46.592  79.413  1.00 34.76 ? 153  GLY   A O     1 
ATOM   949   N  N     . LYS   A  1 156  ? -21.562 47.492  78.556  1.00 26.80 ? 154  LYS   A N     1 
ATOM   950   C  CA    . LYS   A  1 156  ? -21.168 48.145  79.790  1.00 30.82 ? 154  LYS   A CA    1 
ATOM   951   C  C     . LYS   A  1 156  ? -21.216 49.654  79.603  1.00 29.81 ? 154  LYS   A C     1 
ATOM   952   O  O     . LYS   A  1 156  ? -20.956 50.175  78.514  1.00 25.74 ? 154  LYS   A O     1 
ATOM   953   C  CB    . LYS   A  1 156  ? -19.769 47.710  80.222  1.00 29.63 ? 154  LYS   A CB    1 
ATOM   954   N  N     . LEU   A  1 157  ? -21.572 50.351  80.673  1.00 33.03 ? 155  LEU   A N     1 
ATOM   955   C  CA    . LEU   A  1 157  ? -21.687 51.799  80.662  1.00 34.32 ? 155  LEU   A CA    1 
ATOM   956   C  C     . LEU   A  1 157  ? -20.576 52.397  81.513  1.00 36.80 ? 155  LEU   A C     1 
ATOM   957   O  O     . LEU   A  1 157  ? -20.295 51.906  82.610  1.00 35.70 ? 155  LEU   A O     1 
ATOM   958   C  CB    . LEU   A  1 157  ? -23.055 52.240  81.181  1.00 34.78 ? 155  LEU   A CB    1 
ATOM   959   C  CG    . LEU   A  1 157  ? -23.355 53.740  81.166  1.00 39.79 ? 155  LEU   A CG    1 
ATOM   960   C  CD1   . LEU   A  1 157  ? -23.273 54.297  79.757  1.00 32.74 ? 155  LEU   A CD1   1 
ATOM   961   C  CD2   . LEU   A  1 157  ? -24.732 53.998  81.766  1.00 45.28 ? 155  LEU   A CD2   1 
ATOM   962   N  N     . THR   A  1 158  ? -19.926 53.430  80.989  1.00 33.42 ? 156  THR   A N     1 
ATOM   963   C  CA    . THR   A  1 158  ? -19.043 54.282  81.769  1.00 34.48 ? 156  THR   A CA    1 
ATOM   964   C  C     . THR   A  1 158  ? -19.605 55.694  81.718  1.00 30.93 ? 156  THR   A C     1 
ATOM   965   O  O     . THR   A  1 158  ? -20.265 56.069  80.746  1.00 32.64 ? 156  THR   A O     1 
ATOM   966   C  CB    . THR   A  1 158  ? -17.612 54.269  81.224  1.00 37.02 ? 156  THR   A CB    1 
ATOM   967   O  OG1   . THR   A  1 158  ? -17.627 54.690  79.852  1.00 40.36 ? 156  THR   A OG1   1 
ATOM   968   C  CG2   . THR   A  1 158  ? -17.016 52.871  81.316  1.00 37.58 ? 156  THR   A CG2   1 
ATOM   969   N  N     . SER   A  1 159  ? -19.367 56.479  82.771  1.00 26.59 ? 157  SER   A N     1 
ATOM   970   C  CA    . SER   A  1 159  ? -19.826 57.863  82.722  1.00 29.21 ? 157  SER   A CA    1 
ATOM   971   C  C     . SER   A  1 159  ? -18.927 58.697  81.821  1.00 29.71 ? 157  SER   A C     1 
ATOM   972   O  O     . SER   A  1 159  ? -19.396 59.607  81.126  1.00 33.47 ? 157  SER   A O     1 
ATOM   973   C  CB    . SER   A  1 159  ? -19.886 58.468  84.128  1.00 33.65 ? 157  SER   A CB    1 
ATOM   974   O  OG    . SER   A  1 159  ? -18.596 58.562  84.719  1.00 39.52 ? 157  SER   A OG    1 
ATOM   975   N  N     . THR   A  1 160  ? -17.637 58.399  81.814  1.00 25.88 ? 158  THR   A N     1 
ATOM   976   C  CA    . THR   A  1 160  ? -16.675 59.141  81.019  1.00 23.76 ? 158  THR   A CA    1 
ATOM   977   C  C     . THR   A  1 160  ? -15.900 58.180  80.130  1.00 25.43 ? 158  THR   A C     1 
ATOM   978   O  O     . THR   A  1 160  ? -15.920 56.960  80.306  1.00 28.67 ? 158  THR   A O     1 
ATOM   979   C  CB    . THR   A  1 160  ? -15.712 59.948  81.903  1.00 25.20 ? 158  THR   A CB    1 
ATOM   980   O  OG1   . THR   A  1 160  ? -14.996 59.064  82.766  1.00 26.81 ? 158  THR   A OG1   1 
ATOM   981   C  CG2   . THR   A  1 160  ? -16.469 60.968  82.734  1.00 30.49 ? 158  THR   A CG2   1 
ATOM   982   N  N     . VAL   A  1 161  ? -15.167 58.779  79.206  1.00 20.60 ? 159  VAL   A N     1 
ATOM   983   C  CA    . VAL   A  1 161  ? -14.646 58.137  78.016  1.00 21.13 ? 159  VAL   A CA    1 
ATOM   984   C  C     . VAL   A  1 161  ? -13.131 58.220  78.086  1.00 20.86 ? 159  VAL   A C     1 
ATOM   985   O  O     . VAL   A  1 161  ? -12.588 59.301  78.317  1.00 18.87 ? 159  VAL   A O     1 
ATOM   986   C  CB    . VAL   A  1 161  ? -15.196 58.859  76.770  1.00 21.04 ? 159  VAL   A CB    1 
ATOM   987   C  CG1   . VAL   A  1 161  ? -14.378 58.598  75.574  1.00 22.49 ? 159  VAL   A CG1   1 
ATOM   988   C  CG2   . VAL   A  1 161  ? -16.668 58.486  76.554  1.00 29.85 ? 159  VAL   A CG2   1 
ATOM   989   N  N     . ASN   A  1 162  ? -12.448 57.089  77.917  1.00 19.45 ? 160  ASN   A N     1 
ATOM   990   C  CA    . ASN   A  1 162  ? -10.987 57.144  77.830  1.00 20.40 ? 160  ASN   A CA    1 
ATOM   991   C  C     . ASN   A  1 162  ? -10.646 57.479  76.386  1.00 18.46 ? 160  ASN   A C     1 
ATOM   992   O  O     . ASN   A  1 162  ? -10.463 56.601  75.534  1.00 17.21 ? 160  ASN   A O     1 
ATOM   993   C  CB    . ASN   A  1 162  ? -10.338 55.842  78.290  1.00 20.30 ? 160  ASN   A CB    1 
ATOM   994   C  CG    . ASN   A  1 162  ? -8.805  55.926  78.297  1.00 19.82 ? 160  ASN   A CG    1 
ATOM   995   O  OD1   . ASN   A  1 162  ? -8.205  56.747  77.592  1.00 17.22 ? 160  ASN   A OD1   1 
ATOM   996   N  ND2   . ASN   A  1 162  ? -8.174  55.073  79.094  1.00 22.98 ? 160  ASN   A ND2   1 
ATOM   997   N  N     . ASP   A  1 163  ? -10.578 58.782  76.100  1.00 18.36 ? 161  ASP   A N     1 
ATOM   998   C  CA    . ASP   A  1 163  ? -10.365 59.208  74.727  1.00 16.99 ? 161  ASP   A CA    1 
ATOM   999   C  C     . ASP   A  1 163  ? -8.956  58.898  74.231  1.00 17.30 ? 161  ASP   A C     1 
ATOM   1000  O  O     . ASP   A  1 163  ? -8.762  58.769  73.024  1.00 18.47 ? 161  ASP   A O     1 
ATOM   1001  C  CB    . ASP   A  1 163  ? -10.700 60.702  74.565  1.00 19.65 ? 161  ASP   A CB    1 
ATOM   1002  C  CG    . ASP   A  1 163  ? -10.089 61.597  75.649  1.00 23.77 ? 161  ASP   A CG    1 
ATOM   1003  O  OD1   . ASP   A  1 163  ? -10.004 61.195  76.833  1.00 20.17 ? 161  ASP   A OD1   1 
ATOM   1004  O  OD2   . ASP   A  1 163  ? -9.719  62.743  75.306  1.00 23.60 ? 161  ASP   A OD2   1 
ATOM   1005  N  N     . ARG   A  1 164  ? -7.974  58.747  75.123  1.00 17.50 ? 162  ARG   A N     1 
ATOM   1006  C  CA    . ARG   A  1 164  ? -6.639  58.391  74.656  1.00 17.63 ? 162  ARG   A CA    1 
ATOM   1007  C  C     . ARG   A  1 164  ? -6.592  56.932  74.232  1.00 17.84 ? 162  ARG   A C     1 
ATOM   1008  O  O     . ARG   A  1 164  ? -5.984  56.594  73.211  1.00 18.15 ? 162  ARG   A O     1 
ATOM   1009  C  CB    . ARG   A  1 164  ? -5.593  58.665  75.739  1.00 18.35 ? 162  ARG   A CB    1 
ATOM   1010  C  CG    . ARG   A  1 164  ? -5.371  60.135  76.066  1.00 19.24 ? 162  ARG   A CG    1 
ATOM   1011  C  CD    . ARG   A  1 164  ? -5.424  61.033  74.830  1.00 28.91 ? 162  ARG   A CD    1 
ATOM   1012  N  NE    . ARG   A  1 164  ? -4.521  60.640  73.755  1.00 29.83 ? 162  ARG   A NE    1 
ATOM   1013  C  CZ    . ARG   A  1 164  ? -4.720  60.947  72.477  1.00 31.82 ? 162  ARG   A CZ    1 
ATOM   1014  N  NH1   . ARG   A  1 164  ? -5.775  61.651  72.090  1.00 33.63 ? 162  ARG   A NH1   1 
ATOM   1015  N  NH2   . ARG   A  1 164  ? -3.843  60.538  71.565  1.00 28.07 ? 162  ARG   A NH2   1 
ATOM   1016  N  N     . SER   A  1 165  ? -7.249  56.061  75.001  1.00 17.71 ? 163  SER   A N     1 
ATOM   1017  C  CA    . SER   A  1 165  ? -7.386  54.664  74.598  1.00 19.53 ? 163  SER   A CA    1 
ATOM   1018  C  C     . SER   A  1 165  ? -8.128  54.533  73.274  1.00 18.47 ? 163  SER   A C     1 
ATOM   1019  O  O     . SER   A  1 165  ? -7.748  53.731  72.415  1.00 18.32 ? 163  SER   A O     1 
ATOM   1020  C  CB    . SER   A  1 165  ? -8.120  53.881  75.689  1.00 18.16 ? 163  SER   A CB    1 
ATOM   1021  O  OG    . SER   A  1 165  ? -8.437  52.578  75.251  1.00 22.23 ? 163  SER   A OG    1 
ATOM   1022  N  N     . LEU   A  1 166  ? -9.232  55.275  73.119  1.00 17.78 ? 164  LEU   A N     1 
ATOM   1023  C  CA    . LEU   A  1 166  ? -10.003 55.214  71.881  1.00 17.89 ? 164  LEU   A CA    1 
ATOM   1024  C  C     . LEU   A  1 166  ? -9.214  55.759  70.704  1.00 18.17 ? 164  LEU   A C     1 
ATOM   1025  O  O     . LEU   A  1 166  ? -9.299  55.227  69.595  1.00 18.44 ? 164  LEU   A O     1 
ATOM   1026  C  CB    . LEU   A  1 166  ? -11.299 55.991  72.050  1.00 17.58 ? 164  LEU   A CB    1 
ATOM   1027  C  CG    . LEU   A  1 166  ? -12.259 55.280  72.994  1.00 17.87 ? 164  LEU   A CG    1 
ATOM   1028  C  CD1   . LEU   A  1 166  ? -13.427 56.183  73.224  1.00 19.16 ? 164  LEU   A CD1   1 
ATOM   1029  C  CD2   . LEU   A  1 166  ? -12.713 53.956  72.400  1.00 18.50 ? 164  LEU   A CD2   1 
ATOM   1030  N  N     . ALA   A  1 167  ? -8.452  56.831  70.923  1.00 18.15 ? 165  ALA   A N     1 
ATOM   1031  C  CA    . ALA   A  1 167  ? -7.632  57.375  69.841  1.00 18.45 ? 165  ALA   A CA    1 
ATOM   1032  C  C     . ALA   A  1 167  ? -6.551  56.388  69.431  1.00 18.82 ? 165  ALA   A C     1 
ATOM   1033  O  O     . ALA   A  1 167  ? -6.285  56.209  68.238  1.00 19.14 ? 165  ALA   A O     1 
ATOM   1034  C  CB    . ALA   A  1 167  ? -6.996  58.698  70.269  1.00 18.37 ? 165  ALA   A CB    1 
ATOM   1035  N  N     . ALA   A  1 168  ? -5.905  55.754  70.406  1.00 18.79 ? 166  ALA   A N     1 
ATOM   1036  C  CA    . ALA   A  1 168  ? -4.929  54.722  70.072  1.00 19.80 ? 166  ALA   A CA    1 
ATOM   1037  C  C     . ALA   A  1 168  ? -5.591  53.600  69.290  1.00 19.33 ? 166  ALA   A C     1 
ATOM   1038  O  O     . ALA   A  1 168  ? -5.058  53.130  68.275  1.00 19.71 ? 166  ALA   A O     1 
ATOM   1039  C  CB    . ALA   A  1 168  ? -4.286  54.185  71.349  1.00 19.07 ? 166  ALA   A CB    1 
ATOM   1040  N  N     . ALA   A  1 169  ? -6.780  53.184  69.735  1.00 19.07 ? 167  ALA   A N     1 
ATOM   1041  C  CA    . ALA   A  1 169  ? -7.450  52.060  69.099  1.00 19.24 ? 167  ALA   A CA    1 
ATOM   1042  C  C     . ALA   A  1 169  ? -7.870  52.406  67.676  1.00 19.43 ? 167  ALA   A C     1 
ATOM   1043  O  O     . ALA   A  1 169  ? -7.784  51.570  66.774  1.00 19.77 ? 167  ALA   A O     1 
ATOM   1044  C  CB    . ALA   A  1 169  ? -8.653  51.636  69.941  1.00 18.93 ? 167  ALA   A CB    1 
ATOM   1045  N  N     . LEU   A  1 170  ? -8.317  53.637  67.454  1.00 19.24 ? 168  LEU   A N     1 
ATOM   1046  C  CA    . LEU   A  1 170  ? -8.748  54.024  66.114  1.00 19.43 ? 168  LEU   A CA    1 
ATOM   1047  C  C     . LEU   A  1 170  ? -7.563  54.070  65.162  1.00 19.86 ? 168  LEU   A C     1 
ATOM   1048  O  O     . LEU   A  1 170  ? -7.636  53.556  64.040  1.00 20.19 ? 168  LEU   A O     1 
ATOM   1049  C  CB    . LEU   A  1 170  ? -9.459  55.373  66.174  1.00 19.14 ? 168  LEU   A CB    1 
ATOM   1050  C  CG    . LEU   A  1 170  ? -10.026 55.870  64.851  1.00 20.65 ? 168  LEU   A CG    1 
ATOM   1051  C  CD1   . LEU   A  1 170  ? -11.026 54.858  64.307  1.00 20.15 ? 168  LEU   A CD1   1 
ATOM   1052  C  CD2   . LEU   A  1 170  ? -10.685 57.222  65.045  1.00 24.01 ? 168  LEU   A CD2   1 
ATOM   1053  N  N     . THR   A  1 171  ? -6.455  54.681  65.602  1.00 19.89 ? 169  THR   A N     1 
ATOM   1054  C  CA    . THR   A  1 171  ? -5.231  54.653  64.811  1.00 20.32 ? 169  THR   A CA    1 
ATOM   1055  C  C     . THR   A  1 171  ? -4.832  53.219  64.513  1.00 20.65 ? 169  THR   A C     1 
ATOM   1056  O  O     . THR   A  1 171  ? -4.516  52.870  63.370  1.00 21.06 ? 169  THR   A O     1 
ATOM   1057  C  CB    . THR   A  1 171  ? -4.101  55.368  65.558  1.00 20.97 ? 169  THR   A CB    1 
ATOM   1058  O  OG1   . THR   A  1 171  ? -4.453  56.739  65.767  1.00 24.28 ? 169  THR   A OG1   1 
ATOM   1059  C  CG2   . THR   A  1 171  ? -2.778  55.271  64.791  1.00 21.45 ? 169  THR   A CG2   1 
ATOM   1060  N  N     . ARG   A  1 172  ? -4.881  52.361  65.534  1.00 20.49 ? 170  ARG   A N     1 
ATOM   1061  C  CA    . ARG   A  1 172  ? -4.447  50.982  65.349  1.00 21.06 ? 170  ARG   A CA    1 
ATOM   1062  C  C     . ARG   A  1 172  ? -5.321  50.274  64.324  1.00 21.02 ? 170  ARG   A C     1 
ATOM   1063  O  O     . ARG   A  1 172  ? -4.815  49.611  63.413  1.00 21.46 ? 170  ARG   A O     1 
ATOM   1064  C  CB    . ARG   A  1 172  ? -4.459  50.237  66.690  1.00 20.61 ? 170  ARG   A CB    1 
ATOM   1065  C  CG    . ARG   A  1 172  ? -3.784  48.866  66.615  1.00 20.99 ? 170  ARG   A CG    1 
ATOM   1066  C  CD    . ARG   A  1 172  ? -3.883  48.082  67.939  1.00 20.80 ? 170  ARG   A CD    1 
ATOM   1067  N  NE    . ARG   A  1 172  ? -3.678  48.912  69.123  1.00 20.43 ? 170  ARG   A NE    1 
ATOM   1068  C  CZ    . ARG   A  1 172  ? -4.650  49.333  69.927  1.00 20.00 ? 170  ARG   A CZ    1 
ATOM   1069  N  NH1   . ARG   A  1 172  ? -5.921  49.039  69.693  1.00 19.87 ? 170  ARG   A NH1   1 
ATOM   1070  N  NH2   . ARG   A  1 172  ? -4.338  50.059  70.997  1.00 19.72 ? 170  ARG   A NH2   1 
ATOM   1071  N  N     . LEU   A  1 173  ? -6.645  50.431  64.434  1.00 20.71 ? 171  LEU   A N     1 
ATOM   1072  C  CA    . LEU   A  1 173  ? -7.518  49.664  63.555  1.00 20.90 ? 171  LEU   A CA    1 
ATOM   1073  C  C     . LEU   A  1 173  ? -7.462  50.194  62.127  1.00 21.20 ? 171  LEU   A C     1 
ATOM   1074  O  O     . LEU   A  1 173  ? -7.546  49.419  61.172  1.00 21.57 ? 171  LEU   A O     1 
ATOM   1075  C  CB    . LEU   A  1 173  ? -8.948  49.661  64.091  1.00 21.10 ? 171  LEU   A CB    1 
ATOM   1076  C  CG    . LEU   A  1 173  ? -9.839  50.899  63.996  1.00 23.11 ? 171  LEU   A CG    1 
ATOM   1077  C  CD1   . LEU   A  1 173  ? -10.617 50.932  62.671  1.00 22.76 ? 171  LEU   A CD1   1 
ATOM   1078  C  CD2   . LEU   A  1 173  ? -10.798 50.922  65.158  1.00 22.21 ? 171  LEU   A CD2   1 
ATOM   1079  N  N     . ILE   A  1 174  ? -7.318  51.507  61.955  1.00 21.08 ? 172  ILE   A N     1 
ATOM   1080  C  CA    . ILE   A  1 174  ? -7.216  52.041  60.599  1.00 21.40 ? 172  ILE   A CA    1 
ATOM   1081  C  C     . ILE   A  1 174  ? -5.908  51.608  59.955  1.00 22.93 ? 172  ILE   A C     1 
ATOM   1082  O  O     . ILE   A  1 174  ? -5.876  51.217  58.783  1.00 25.20 ? 172  ILE   A O     1 
ATOM   1083  C  CB    . ILE   A  1 174  ? -7.370  53.571  60.601  1.00 23.70 ? 172  ILE   A CB    1 
ATOM   1084  C  CG1   . ILE   A  1 174  ? -8.826  53.944  60.888  1.00 21.00 ? 172  ILE   A CG1   1 
ATOM   1085  C  CG2   . ILE   A  1 174  ? -6.965  54.149  59.232  1.00 24.14 ? 172  ILE   A CG2   1 
ATOM   1086  C  CD1   . ILE   A  1 174  ? -8.989  55.371  61.312  1.00 23.58 ? 172  ILE   A CD1   1 
ATOM   1087  N  N     . SER   A  1 175  ? -4.806  51.661  60.705  1.00 21.91 ? 173  SER   A N     1 
ATOM   1088  C  CA    . SER   A  1 175  ? -3.526  51.265  60.123  1.00 22.40 ? 173  SER   A CA    1 
ATOM   1089  C  C     . SER   A  1 175  ? -3.488  49.778  59.808  1.00 24.01 ? 173  SER   A C     1 
ATOM   1090  O  O     . SER   A  1 175  ? -2.786  49.361  58.881  1.00 25.80 ? 173  SER   A O     1 
ATOM   1091  C  CB    . SER   A  1 175  ? -2.371  51.618  61.051  1.00 22.35 ? 173  SER   A CB    1 
ATOM   1092  O  OG    . SER   A  1 175  ? -2.267  53.010  61.250  1.00 29.33 ? 173  SER   A OG    1 
ATOM   1093  N  N     . ARG   A  1 176  ? -4.241  48.970  60.553  1.00 22.49 ? 174  ARG   A N     1 
ATOM   1094  C  CA    . ARG   A  1 176  ? -4.247  47.525  60.347  1.00 23.76 ? 174  ARG   A CA    1 
ATOM   1095  C  C     . ARG   A  1 176  ? -5.234  47.105  59.261  1.00 25.64 ? 174  ARG   A C     1 
ATOM   1096  O  O     . ARG   A  1 176  ? -4.932  46.223  58.454  1.00 26.47 ? 174  ARG   A O     1 
ATOM   1097  C  CB    . ARG   A  1 176  ? -4.585  46.830  61.669  1.00 26.08 ? 174  ARG   A CB    1 
ATOM   1098  C  CG    . ARG   A  1 176  ? -4.502  45.310  61.646  1.00 26.31 ? 174  ARG   A CG    1 
ATOM   1099  C  CD    . ARG   A  1 176  ? -4.795  44.726  63.044  1.00 22.53 ? 174  ARG   A CD    1 
ATOM   1100  N  NE    . ARG   A  1 176  ? -6.215  44.749  63.385  1.00 22.13 ? 174  ARG   A NE    1 
ATOM   1101  C  CZ    . ARG   A  1 176  ? -6.766  45.469  64.357  1.00 23.26 ? 174  ARG   A CZ    1 
ATOM   1102  N  NH1   . ARG   A  1 176  ? -6.043  46.256  65.144  1.00 21.40 ? 174  ARG   A NH1   1 
ATOM   1103  N  NH2   . ARG   A  1 176  ? -8.081  45.394  64.549  1.00 26.77 ? 174  ARG   A NH2   1 
ATOM   1104  N  N     . CYS   A  1 177  ? -6.417  47.723  59.219  1.00 24.26 ? 175  CYS   A N     1 
ATOM   1105  C  CA    . CYS   A  1 177  ? -7.479  47.272  58.335  1.00 25.15 ? 175  CYS   A CA    1 
ATOM   1106  C  C     . CYS   A  1 177  ? -7.849  48.258  57.234  1.00 31.24 ? 175  CYS   A C     1 
ATOM   1107  O  O     . CYS   A  1 177  ? -8.418  47.833  56.227  1.00 29.80 ? 175  CYS   A O     1 
ATOM   1108  C  CB    . CYS   A  1 177  ? -8.745  46.941  59.145  1.00 24.62 ? 175  CYS   A CB    1 
ATOM   1109  S  SG    . CYS   A  1 177  ? -8.457  45.754  60.505  1.00 30.07 ? 175  CYS   A SG    1 
ATOM   1110  N  N     . GLY   A  1 178  ? -7.576  49.550  57.406  1.00 28.93 ? 176  GLY   A N     1 
ATOM   1111  C  CA    . GLY   A  1 178  ? -7.774  50.475  56.300  1.00 30.86 ? 176  GLY   A CA    1 
ATOM   1112  C  C     . GLY   A  1 178  ? -9.228  50.761  55.950  1.00 25.16 ? 176  GLY   A C     1 
ATOM   1113  O  O     . GLY   A  1 178  ? -10.149 50.599  56.749  1.00 25.72 ? 176  GLY   A O     1 
ATOM   1114  N  N     . GLU   A  1 179  ? -9.417  51.202  54.707  1.00 30.96 ? 177  GLU   A N     1 
ATOM   1115  C  CA    . GLU   A  1 179  ? -10.740 51.630  54.251  1.00 26.04 ? 177  GLU   A CA    1 
ATOM   1116  C  C     . GLU   A  1 179  ? -11.850 50.598  54.450  1.00 24.98 ? 177  GLU   A C     1 
ATOM   1117  O  O     . GLU   A  1 179  ? -12.964 51.002  54.831  1.00 26.70 ? 177  GLU   A O     1 
ATOM   1118  C  CB    . GLU   A  1 179  ? -10.648 52.039  52.772  1.00 25.44 ? 177  GLU   A CB    1 
ATOM   1119  C  CG    . GLU   A  1 179  ? -11.928 52.646  52.215  1.00 35.26 ? 177  GLU   A CG    1 
ATOM   1120  C  CD    . GLU   A  1 179  ? -11.777 53.092  50.773  1.00 45.54 ? 177  GLU   A CD    1 
ATOM   1121  O  OE1   . GLU   A  1 179  ? -10.640 53.050  50.262  1.00 51.64 ? 177  GLU   A OE1   1 
ATOM   1122  O  OE2   . GLU   A  1 179  ? -12.788 53.480  50.149  1.00 52.40 ? 177  GLU   A OE2   1 
ATOM   1123  N  N     . PRO   A  1 180  ? -11.647 49.298  54.213  1.00 23.98 ? 178  PRO   A N     1 
ATOM   1124  C  CA    . PRO   A  1 180  ? -12.775 48.365  54.344  1.00 25.39 ? 178  PRO   A CA    1 
ATOM   1125  C  C     . PRO   A  1 180  ? -13.442 48.377  55.710  1.00 28.07 ? 178  PRO   A C     1 
ATOM   1126  O  O     . PRO   A  1 180  ? -14.679 48.310  55.786  1.00 26.79 ? 178  PRO   A O     1 
ATOM   1127  C  CB    . PRO   A  1 180  ? -12.125 47.012  54.029  1.00 28.03 ? 178  PRO   A CB    1 
ATOM   1128  C  CG    . PRO   A  1 180  ? -11.060 47.350  53.054  1.00 26.79 ? 178  PRO   A CG    1 
ATOM   1129  C  CD    . PRO   A  1 180  ? -10.491 48.645  53.566  1.00 27.92 ? 178  PRO   A CD    1 
ATOM   1130  N  N     . VAL   A  1 181  ? -12.667 48.467  56.795  1.00 24.15 ? 179  VAL   A N     1 
ATOM   1131  C  CA    . VAL   A  1 181  ? -13.287 48.476  58.115  1.00 25.77 ? 179  VAL   A CA    1 
ATOM   1132  C  C     . VAL   A  1 181  ? -14.034 49.785  58.343  1.00 23.40 ? 179  VAL   A C     1 
ATOM   1133  O  O     . VAL   A  1 181  ? -15.067 49.808  59.023  1.00 26.63 ? 179  VAL   A O     1 
ATOM   1134  C  CB    . VAL   A  1 181  ? -12.231 48.207  59.210  1.00 25.86 ? 179  VAL   A CB    1 
ATOM   1135  C  CG1   . VAL   A  1 181  ? -11.316 49.420  59.431  1.00 24.82 ? 179  VAL   A CG1   1 
ATOM   1136  C  CG2   . VAL   A  1 181  ? -12.901 47.804  60.510  1.00 27.55 ? 179  VAL   A CG2   1 
ATOM   1137  N  N     . ILE   A  1 182  ? -13.537 50.892  57.782  1.00 23.68 ? 180  ILE   A N     1 
ATOM   1138  C  CA    . ILE   A  1 182  ? -14.228 52.170  57.924  1.00 26.10 ? 180  ILE   A CA    1 
ATOM   1139  C  C     . ILE   A  1 182  ? -15.566 52.118  57.200  1.00 27.39 ? 180  ILE   A C     1 
ATOM   1140  O  O     . ILE   A  1 182  ? -16.610 52.509  57.740  1.00 25.24 ? 180  ILE   A O     1 
ATOM   1141  C  CB    . ILE   A  1 182  ? -13.347 53.318  57.396  1.00 23.95 ? 180  ILE   A CB    1 
ATOM   1142  C  CG1   . ILE   A  1 182  ? -12.017 53.375  58.151  1.00 22.42 ? 180  ILE   A CG1   1 
ATOM   1143  C  CG2   . ILE   A  1 182  ? -14.085 54.653  57.517  1.00 25.41 ? 180  ILE   A CG2   1 
ATOM   1144  C  CD1   . ILE   A  1 182  ? -10.951 54.226  57.471  1.00 28.20 ? 180  ILE   A CD1   1 
ATOM   1145  N  N     . ARG   A  1 183  ? -15.553 51.616  55.966  1.00 25.53 ? 181  ARG   A N     1 
ATOM   1146  C  CA    . ARG   A  1 183  ? -16.796 51.508  55.206  1.00 27.99 ? 181  ARG   A CA    1 
ATOM   1147  C  C     . ARG   A  1 183  ? -17.803 50.620  55.927  1.00 29.77 ? 181  ARG   A C     1 
ATOM   1148  O  O     . ARG   A  1 183  ? -18.988 50.966  56.031  1.00 30.60 ? 181  ARG   A O     1 
ATOM   1149  C  CB    . ARG   A  1 183  ? -16.501 50.982  53.798  1.00 26.43 ? 181  ARG   A CB    1 
ATOM   1150  N  N     . ARG   A  1 184  ? -17.348 49.482  56.453  1.00 28.81 ? 182  ARG   A N     1 
ATOM   1151  C  CA    . ARG   A  1 184  ? -18.239 48.613  57.212  1.00 29.31 ? 182  ARG   A CA    1 
ATOM   1152  C  C     . ARG   A  1 184  ? -18.760 49.306  58.466  1.00 28.24 ? 182  ARG   A C     1 
ATOM   1153  O  O     . ARG   A  1 184  ? -19.937 49.168  58.817  1.00 29.53 ? 182  ARG   A O     1 
ATOM   1154  C  CB    . ARG   A  1 184  ? -17.513 47.321  57.568  1.00 31.82 ? 182  ARG   A CB    1 
ATOM   1155  C  CG    . ARG   A  1 184  ? -17.538 46.302  56.451  1.00 35.67 ? 182  ARG   A CG    1 
ATOM   1156  C  CD    . ARG   A  1 184  ? -18.832 45.499  56.492  1.00 36.54 ? 182  ARG   A CD    1 
ATOM   1157  N  NE    . ARG   A  1 184  ? -18.691 44.300  57.312  1.00 42.67 ? 182  ARG   A NE    1 
ATOM   1158  C  CZ    . ARG   A  1 184  ? -19.425 44.017  58.379  1.00 42.12 ? 182  ARG   A CZ    1 
ATOM   1159  N  NH1   . ARG   A  1 184  ? -20.400 44.816  58.781  1.00 41.54 ? 182  ARG   A NH1   1 
ATOM   1160  N  NH2   . ARG   A  1 184  ? -19.181 42.895  59.054  1.00 40.72 ? 182  ARG   A NH2   1 
ATOM   1161  N  N     . GLY   A  1 185  ? -17.902 50.050  59.156  1.00 24.33 ? 183  GLY   A N     1 
ATOM   1162  C  CA    . GLY   A  1 185  ? -18.363 50.787  60.319  1.00 25.95 ? 183  GLY   A CA    1 
ATOM   1163  C  C     . GLY   A  1 185  ? -19.390 51.844  59.962  1.00 27.51 ? 183  GLY   A C     1 
ATOM   1164  O  O     . GLY   A  1 185  ? -20.394 52.005  60.658  1.00 26.00 ? 183  GLY   A O     1 
ATOM   1165  N  N     . VAL   A  1 186  ? -19.143 52.587  58.879  1.00 25.90 ? 184  VAL   A N     1 
ATOM   1166  C  CA    . VAL   A  1 186  ? -20.077 53.624  58.449  1.00 27.76 ? 184  VAL   A CA    1 
ATOM   1167  C  C     . VAL   A  1 186  ? -21.432 53.012  58.124  1.00 30.01 ? 184  VAL   A C     1 
ATOM   1168  O  O     . VAL   A  1 186  ? -22.479 53.529  58.534  1.00 31.59 ? 184  VAL   A O     1 
ATOM   1169  C  CB    . VAL   A  1 186  ? -19.503 54.399  57.248  1.00 32.85 ? 184  VAL   A CB    1 
ATOM   1170  C  CG1   . VAL   A  1 186  ? -20.603 55.187  56.535  1.00 27.74 ? 184  VAL   A CG1   1 
ATOM   1171  C  CG2   . VAL   A  1 186  ? -18.388 55.331  57.705  1.00 29.26 ? 184  VAL   A CG2   1 
ATOM   1172  N  N     . ASP   A  1 187  ? -21.434 51.896  57.393  1.00 29.28 ? 185  ASP   A N     1 
ATOM   1173  C  CA    . ASP   A  1 187  ? -22.703 51.268  57.035  1.00 30.58 ? 185  ASP   A CA    1 
ATOM   1174  C  C     . ASP   A  1 187  ? -23.420 50.745  58.271  1.00 32.62 ? 185  ASP   A C     1 
ATOM   1175  O  O     . ASP   A  1 187  ? -24.650 50.848  58.374  1.00 32.79 ? 185  ASP   A O     1 
ATOM   1176  C  CB    . ASP   A  1 187  ? -22.473 50.151  56.017  1.00 32.54 ? 185  ASP   A CB    1 
ATOM   1177  C  CG    . ASP   A  1 187  ? -21.933 50.676  54.699  1.00 40.88 ? 185  ASP   A CG    1 
ATOM   1178  O  OD1   . ASP   A  1 187  ? -22.196 51.858  54.383  1.00 48.57 ? 185  ASP   A OD1   1 
ATOM   1179  O  OD2   . ASP   A  1 187  ? -21.243 49.918  53.984  1.00 43.55 ? 185  ASP   A OD2   1 
ATOM   1180  N  N     . MET   A  1 188  ? -22.667 50.201  59.229  1.00 30.79 ? 186  MET   A N     1 
ATOM   1181  C  CA    . MET   A  1 188  ? -23.271 49.710  60.462  1.00 30.87 ? 186  MET   A CA    1 
ATOM   1182  C  C     . MET   A  1 188  ? -23.890 50.850  61.262  1.00 32.71 ? 186  MET   A C     1 
ATOM   1183  O  O     . MET   A  1 188  ? -25.038 50.755  61.719  1.00 33.71 ? 186  MET   A O     1 
ATOM   1184  C  CB    . MET   A  1 188  ? -22.221 48.977  61.297  1.00 32.94 ? 186  MET   A CB    1 
ATOM   1185  C  CG    . MET   A  1 188  ? -22.771 48.352  62.563  1.00 38.07 ? 186  MET   A CG    1 
ATOM   1186  S  SD    . MET   A  1 188  ? -23.692 46.850  62.203  1.00 56.34 ? 186  MET   A SD    1 
ATOM   1187  C  CE    . MET   A  1 188  ? -22.369 45.860  61.507  1.00 46.31 ? 186  MET   A CE    1 
ATOM   1188  N  N     . ALA   A  1 189  ? -23.144 51.943  61.443  1.00 31.65 ? 187  ALA   A N     1 
ATOM   1189  C  CA    . ALA   A  1 189  ? -23.667 53.056  62.231  1.00 34.28 ? 187  ALA   A CA    1 
ATOM   1190  C  C     . ALA   A  1 189  ? -24.877 53.683  61.557  1.00 34.93 ? 187  ALA   A C     1 
ATOM   1191  O  O     . ALA   A  1 189  ? -25.841 54.064  62.231  1.00 32.52 ? 187  ALA   A O     1 
ATOM   1192  C  CB    . ALA   A  1 189  ? -22.584 54.108  62.461  1.00 31.19 ? 187  ALA   A CB    1 
ATOM   1193  N  N     . MET   A  1 190  ? -24.845 53.793  60.226  1.00 31.53 ? 188  MET   A N     1 
ATOM   1194  C  CA    . MET   A  1 190  ? -25.965 54.383  59.500  1.00 36.04 ? 188  MET   A CA    1 
ATOM   1195  C  C     . MET   A  1 190  ? -27.236 53.567  59.691  1.00 35.89 ? 188  MET   A C     1 
ATOM   1196  O  O     . MET   A  1 190  ? -28.315 54.130  59.910  1.00 37.90 ? 188  MET   A O     1 
ATOM   1197  C  CB    . MET   A  1 190  ? -25.618 54.498  58.017  1.00 34.84 ? 188  MET   A CB    1 
ATOM   1198  C  CG    . MET   A  1 190  ? -26.555 55.371  57.213  1.00 40.94 ? 188  MET   A CG    1 
ATOM   1199  S  SD    . MET   A  1 190  ? -26.282 55.151  55.436  1.00 54.47 ? 188  MET   A SD    1 
ATOM   1200  C  CE    . MET   A  1 190  ? -24.651 55.850  55.211  1.00 47.96 ? 188  MET   A CE    1 
ATOM   1201  N  N     . ARG   A  1 191  ? -27.125 52.237  59.619  1.00 34.27 ? 189  ARG   A N     1 
ATOM   1202  C  CA    . ARG   A  1 191  ? -28.279 51.378  59.860  1.00 38.11 ? 189  ARG   A CA    1 
ATOM   1203  C  C     . ARG   A  1 191  ? -28.755 51.474  61.305  1.00 39.95 ? 189  ARG   A C     1 
ATOM   1204  O  O     . ARG   A  1 191  ? -29.966 51.494  61.567  1.00 36.71 ? 189  ARG   A O     1 
ATOM   1205  C  CB    . ARG   A  1 191  ? -27.937 49.931  59.514  1.00 35.04 ? 189  ARG   A CB    1 
ATOM   1206  N  N     . MET   A  1 192  ? -27.824 51.519  62.259  1.00 34.97 ? 190  MET   A N     1 
ATOM   1207  C  CA    . MET   A  1 192  ? -28.224 51.543  63.663  1.00 34.86 ? 190  MET   A CA    1 
ATOM   1208  C  C     . MET   A  1 192  ? -28.879 52.866  64.034  1.00 37.88 ? 190  MET   A C     1 
ATOM   1209  O  O     . MET   A  1 192  ? -29.924 52.890  64.698  1.00 34.86 ? 190  MET   A O     1 
ATOM   1210  C  CB    . MET   A  1 192  ? -27.017 51.286  64.559  1.00 34.98 ? 190  MET   A CB    1 
ATOM   1211  C  CG    . MET   A  1 192  ? -26.478 49.883  64.452  1.00 34.43 ? 190  MET   A CG    1 
ATOM   1212  S  SD    . MET   A  1 192  ? -25.252 49.619  65.734  1.00 45.90 ? 190  MET   A SD    1 
ATOM   1213  C  CE    . MET   A  1 192  ? -26.331 49.359  67.128  1.00 33.17 ? 190  MET   A CE    1 
ATOM   1214  N  N     . MET   A  1 193  ? -28.262 53.981  63.637  1.00 34.40 ? 191  MET   A N     1 
ATOM   1215  C  CA    . MET   A  1 193  ? -28.773 55.284  64.041  1.00 39.07 ? 191  MET   A CA    1 
ATOM   1216  C  C     . MET   A  1 193  ? -29.976 55.715  63.217  1.00 35.92 ? 191  MET   A C     1 
ATOM   1217  O  O     . MET   A  1 193  ? -30.803 56.490  63.707  1.00 37.32 ? 191  MET   A O     1 
ATOM   1218  C  CB    . MET   A  1 193  ? -27.676 56.340  63.939  1.00 34.35 ? 191  MET   A CB    1 
ATOM   1219  C  CG    . MET   A  1 193  ? -26.546 56.134  64.922  1.00 35.71 ? 191  MET   A CG    1 
ATOM   1220  S  SD    . MET   A  1 193  ? -25.427 57.541  64.985  1.00 49.52 ? 191  MET   A SD    1 
ATOM   1221  C  CE    . MET   A  1 193  ? -24.805 57.601  63.317  1.00 37.67 ? 191  MET   A CE    1 
ATOM   1222  N  N     . GLY   A  1 194  ? -30.091 55.233  61.982  1.00 35.00 ? 192  GLY   A N     1 
ATOM   1223  C  CA    . GLY   A  1 194  ? -31.174 55.650  61.116  1.00 37.83 ? 192  GLY   A CA    1 
ATOM   1224  C  C     . GLY   A  1 194  ? -32.373 54.722  61.121  1.00 40.74 ? 192  GLY   A C     1 
ATOM   1225  O  O     . GLY   A  1 194  ? -33.485 55.153  60.793  1.00 36.34 ? 192  GLY   A O     1 
ATOM   1226  N  N     . GLU   A  1 195  ? -32.173 53.454  61.498  1.00 34.46 ? 193  GLU   A N     1 
ATOM   1227  C  CA    . GLU   A  1 195  ? -33.214 52.440  61.359  1.00 35.98 ? 193  GLU   A CA    1 
ATOM   1228  C  C     . GLU   A  1 195  ? -33.467 51.593  62.597  1.00 31.99 ? 193  GLU   A C     1 
ATOM   1229  O  O     . GLU   A  1 195  ? -34.555 51.012  62.693  1.00 26.81 ? 193  GLU   A O     1 
ATOM   1230  C  CB    . GLU   A  1 195  ? -32.886 51.482  60.209  1.00 39.15 ? 193  GLU   A CB    1 
ATOM   1231  C  CG    . GLU   A  1 195  ? -32.630 52.142  58.884  1.00 44.01 ? 193  GLU   A CG    1 
ATOM   1232  C  CD    . GLU   A  1 195  ? -32.043 51.169  57.897  1.00 48.11 ? 193  GLU   A CD    1 
ATOM   1233  O  OE1   . GLU   A  1 195  ? -32.478 49.998  57.902  1.00 48.45 ? 193  GLU   A OE1   1 
ATOM   1234  O  OE2   . GLU   A  1 195  ? -31.137 51.564  57.136  1.00 54.44 ? 193  GLU   A OE2   1 
ATOM   1235  N  N     . GLN   A  1 196  ? -32.509 51.473  63.520  1.00 37.75 ? 194  GLN   A N     1 
ATOM   1236  C  CA    . GLN   A  1 196  ? -32.628 50.625  64.706  1.00 33.97 ? 194  GLN   A CA    1 
ATOM   1237  C  C     . GLN   A  1 196  ? -32.836 51.409  65.992  1.00 33.87 ? 194  GLN   A C     1 
ATOM   1238  O  O     . GLN   A  1 196  ? -33.665 51.022  66.819  1.00 37.75 ? 194  GLN   A O     1 
ATOM   1239  C  CB    . GLN   A  1 196  ? -31.380 49.745  64.853  1.00 36.41 ? 194  GLN   A CB    1 
ATOM   1240  N  N     . PHE   A  1 197  ? -32.093 52.497  66.195  1.00 29.05 ? 195  PHE   A N     1 
ATOM   1241  C  CA    . PHE   A  1 197  ? -32.341 53.344  67.355  1.00 28.57 ? 195  PHE   A CA    1 
ATOM   1242  C  C     . PHE   A  1 197  ? -33.606 54.154  67.171  1.00 30.15 ? 195  PHE   A C     1 
ATOM   1243  O  O     . PHE   A  1 197  ? -34.298 54.457  68.145  1.00 34.42 ? 195  PHE   A O     1 
ATOM   1244  C  CB    . PHE   A  1 197  ? -31.169 54.287  67.598  1.00 30.46 ? 195  PHE   A CB    1 
ATOM   1245  C  CG    . PHE   A  1 197  ? -29.882 53.584  67.896  1.00 31.76 ? 195  PHE   A CG    1 
ATOM   1246  C  CD1   . PHE   A  1 197  ? -29.884 52.313  68.442  1.00 35.70 ? 195  PHE   A CD1   1 
ATOM   1247  C  CD2   . PHE   A  1 197  ? -28.671 54.194  67.628  1.00 34.99 ? 195  PHE   A CD2   1 
ATOM   1248  C  CE1   . PHE   A  1 197  ? -28.702 51.663  68.719  1.00 35.33 ? 195  PHE   A CE1   1 
ATOM   1249  C  CE2   . PHE   A  1 197  ? -27.483 53.551  67.905  1.00 38.57 ? 195  PHE   A CE2   1 
ATOM   1250  C  CZ    . PHE   A  1 197  ? -27.505 52.284  68.455  1.00 34.75 ? 195  PHE   A CZ    1 
ATOM   1251  N  N     . VAL   A  1 198  ? -33.905 54.531  65.939  1.00 26.44 ? 196  VAL   A N     1 
ATOM   1252  C  CA    . VAL   A  1 198  ? -35.095 55.304  65.633  1.00 27.00 ? 196  VAL   A CA    1 
ATOM   1253  C  C     . VAL   A  1 198  ? -35.841 54.588  64.523  1.00 24.72 ? 196  VAL   A C     1 
ATOM   1254  O  O     . VAL   A  1 198  ? -35.254 53.880  63.698  1.00 29.58 ? 196  VAL   A O     1 
ATOM   1255  C  CB    . VAL   A  1 198  ? -34.775 56.761  65.220  1.00 25.55 ? 196  VAL   A CB    1 
ATOM   1256  C  CG1   . VAL   A  1 198  ? -34.000 57.484  66.323  1.00 28.37 ? 196  VAL   A CG1   1 
ATOM   1257  C  CG2   . VAL   A  1 198  ? -34.028 56.797  63.902  1.00 28.15 ? 196  VAL   A CG2   1 
ATOM   1258  N  N     . THR   A  1 199  ? -37.153 54.754  64.522  1.00 22.55 ? 197  THR   A N     1 
ATOM   1259  C  CA    . THR   A  1 199  ? -37.920 54.281  63.386  1.00 23.41 ? 197  THR   A CA    1 
ATOM   1260  C  C     . THR   A  1 199  ? -37.653 55.143  62.163  1.00 25.99 ? 197  THR   A C     1 
ATOM   1261  O  O     . THR   A  1 199  ? -37.632 54.635  61.037  1.00 30.91 ? 197  THR   A O     1 
ATOM   1262  C  CB    . THR   A  1 199  ? -39.399 54.277  63.752  1.00 27.11 ? 197  THR   A CB    1 
ATOM   1263  O  OG1   . THR   A  1 199  ? -39.578 53.456  64.920  1.00 27.34 ? 197  THR   A OG1   1 
ATOM   1264  C  CG2   . THR   A  1 199  ? -40.226 53.744  62.612  1.00 24.51 ? 197  THR   A CG2   1 
ATOM   1265  N  N     . GLY   A  1 200  ? -37.428 56.433  62.367  1.00 25.27 ? 198  GLY   A N     1 
ATOM   1266  C  CA    . GLY   A  1 200  ? -37.099 57.324  61.270  1.00 27.63 ? 198  GLY   A CA    1 
ATOM   1267  C  C     . GLY   A  1 200  ? -36.473 58.589  61.803  1.00 27.40 ? 198  GLY   A C     1 
ATOM   1268  O  O     . GLY   A  1 200  ? -36.572 58.897  62.994  1.00 24.79 ? 198  GLY   A O     1 
ATOM   1269  N  N     . GLU   A  1 201  ? -35.789 59.311  60.911  1.00 27.04 ? 199  GLU   A N     1 
ATOM   1270  C  CA    . GLU   A  1 201  ? -35.194 60.577  61.324  1.00 31.45 ? 199  GLU   A CA    1 
ATOM   1271  C  C     . GLU   A  1 201  ? -36.230 61.680  61.395  1.00 24.86 ? 199  GLU   A C     1 
ATOM   1272  O  O     . GLU   A  1 201  ? -36.054 62.645  62.143  1.00 25.66 ? 199  GLU   A O     1 
ATOM   1273  C  CB    . GLU   A  1 201  ? -34.060 60.974  60.375  1.00 31.90 ? 199  GLU   A CB    1 
ATOM   1274  C  CG    . GLU   A  1 201  ? -32.819 60.127  60.575  1.00 41.08 ? 199  GLU   A CG    1 
ATOM   1275  C  CD    . GLU   A  1 201  ? -31.674 60.533  59.676  1.00 48.77 ? 199  GLU   A CD    1 
ATOM   1276  O  OE1   . GLU   A  1 201  ? -31.871 61.409  58.803  1.00 51.08 ? 199  GLU   A OE1   1 
ATOM   1277  O  OE2   . GLU   A  1 201  ? -30.576 59.967  59.851  1.00 52.02 ? 199  GLU   A OE2   1 
ATOM   1278  N  N     . THR   A  1 202  ? -37.303 61.554  60.620  1.00 23.46 ? 200  THR   A N     1 
ATOM   1279  C  CA    . THR   A  1 202  ? -38.410 62.491  60.625  1.00 23.36 ? 200  THR   A CA    1 
ATOM   1280  C  C     . THR   A  1 202  ? -39.691 61.685  60.753  1.00 25.00 ? 200  THR   A C     1 
ATOM   1281  O  O     . THR   A  1 202  ? -39.718 60.485  60.466  1.00 22.73 ? 200  THR   A O     1 
ATOM   1282  C  CB    . THR   A  1 202  ? -38.475 63.309  59.337  1.00 23.22 ? 200  THR   A CB    1 
ATOM   1283  O  OG1   . THR   A  1 202  ? -38.706 62.404  58.250  1.00 23.99 ? 200  THR   A OG1   1 
ATOM   1284  C  CG2   . THR   A  1 202  ? -37.176 64.076  59.103  1.00 27.50 ? 200  THR   A CG2   1 
ATOM   1285  N  N     . ILE   A  1 203  ? -40.770 62.353  61.152  1.00 22.07 ? 201  ILE   A N     1 
ATOM   1286  C  CA    . ILE   A  1 203  ? -42.038 61.634  61.275  1.00 21.83 ? 201  ILE   A CA    1 
ATOM   1287  C  C     . ILE   A  1 203  ? -42.483 61.100  59.920  1.00 21.86 ? 201  ILE   A C     1 
ATOM   1288  O  O     . ILE   A  1 203  ? -43.020 59.991  59.826  1.00 24.23 ? 201  ILE   A O     1 
ATOM   1289  C  CB    . ILE   A  1 203  ? -43.114 62.519  61.929  1.00 22.26 ? 201  ILE   A CB    1 
ATOM   1290  C  CG1   . ILE   A  1 203  ? -44.371 61.685  62.239  1.00 20.26 ? 201  ILE   A CG1   1 
ATOM   1291  C  CG2   . ILE   A  1 203  ? -43.470 63.702  61.039  1.00 27.83 ? 201  ILE   A CG2   1 
ATOM   1292  C  CD1   . ILE   A  1 203  ? -44.094 60.464  63.114  1.00 19.75 ? 201  ILE   A CD1   1 
ATOM   1293  N  N     . ARG   A  1 204  ? -42.235 61.855  58.840  1.00 24.15 ? 202  ARG   A N     1 
ATOM   1294  C  CA    . ARG   A  1 204  ? -42.603 61.361  57.516  1.00 24.49 ? 202  ARG   A CA    1 
ATOM   1295  C  C     . ARG   A  1 204  ? -41.879 60.062  57.204  1.00 25.36 ? 202  ARG   A C     1 
ATOM   1296  O  O     . ARG   A  1 204  ? -42.489 59.103  56.719  1.00 25.12 ? 202  ARG   A O     1 
ATOM   1297  C  CB    . ARG   A  1 204  ? -42.302 62.417  56.447  1.00 27.81 ? 202  ARG   A CB    1 
ATOM   1298  N  N     . GLU   A  1 205  ? -40.579 60.002  57.503  1.00 24.93 ? 203  GLU   A N     1 
ATOM   1299  C  CA    . GLU   A  1 205  ? -39.819 58.782  57.271  1.00 27.78 ? 203  GLU   A CA    1 
ATOM   1300  C  C     . GLU   A  1 205  ? -40.284 57.658  58.186  1.00 26.19 ? 203  GLU   A C     1 
ATOM   1301  O  O     . GLU   A  1 205  ? -40.422 56.510  57.748  1.00 27.03 ? 203  GLU   A O     1 
ATOM   1302  C  CB    . GLU   A  1 205  ? -38.329 59.049  57.478  1.00 29.18 ? 203  GLU   A CB    1 
ATOM   1303  C  CG    . GLU   A  1 205  ? -37.447 57.843  57.224  1.00 33.00 ? 203  GLU   A CG    1 
ATOM   1304  C  CD    . GLU   A  1 205  ? -35.970 58.162  57.408  1.00 37.32 ? 203  GLU   A CD    1 
ATOM   1305  O  OE1   . GLU   A  1 205  ? -35.540 58.392  58.562  1.00 37.87 ? 203  GLU   A OE1   1 
ATOM   1306  O  OE2   . GLU   A  1 205  ? -35.240 58.196  56.393  1.00 43.76 ? 203  GLU   A OE2   1 
ATOM   1307  N  N     . ALA   A  1 206  ? -40.522 57.967  59.461  1.00 24.28 ? 204  ALA   A N     1 
ATOM   1308  C  CA    . ALA   A  1 206  ? -40.989 56.942  60.390  1.00 25.41 ? 204  ALA   A CA    1 
ATOM   1309  C  C     . ALA   A  1 206  ? -42.314 56.351  59.928  1.00 24.88 ? 204  ALA   A C     1 
ATOM   1310  O  O     . ALA   A  1 206  ? -42.504 55.128  59.955  1.00 21.75 ? 204  ALA   A O     1 
ATOM   1311  C  CB    . ALA   A  1 206  ? -41.108 57.535  61.795  1.00 22.55 ? 204  ALA   A CB    1 
ATOM   1312  N  N     . LEU   A  1 207  ? -43.233 57.206  59.475  1.00 22.53 ? 205  LEU   A N     1 
ATOM   1313  C  CA    . LEU   A  1 207  ? -44.522 56.728  58.985  1.00 21.63 ? 205  LEU   A CA    1 
ATOM   1314  C  C     . LEU   A  1 207  ? -44.357 55.827  57.769  1.00 25.53 ? 205  LEU   A C     1 
ATOM   1315  O  O     . LEU   A  1 207  ? -45.017 54.786  57.667  1.00 25.83 ? 205  LEU   A O     1 
ATOM   1316  C  CB    . LEU   A  1 207  ? -45.425 57.914  58.656  1.00 26.95 ? 205  LEU   A CB    1 
ATOM   1317  C  CG    . LEU   A  1 207  ? -45.929 58.675  59.876  1.00 23.20 ? 205  LEU   A CG    1 
ATOM   1318  C  CD1   . LEU   A  1 207  ? -46.493 60.023  59.474  1.00 24.66 ? 205  LEU   A CD1   1 
ATOM   1319  C  CD2   . LEU   A  1 207  ? -46.978 57.835  60.615  1.00 19.68 ? 205  LEU   A CD2   1 
ATOM   1320  N  N     . LYS   A  1 208  ? -43.487 56.215  56.831  1.00 24.43 ? 206  LYS   A N     1 
ATOM   1321  C  CA    . LYS   A  1 208  ? -43.225 55.370  55.670  1.00 27.82 ? 206  LYS   A CA    1 
ATOM   1322  C  C     . LYS   A  1 208  ? -42.736 53.990  56.091  1.00 25.67 ? 206  LYS   A C     1 
ATOM   1323  O  O     . LYS   A  1 208  ? -43.166 52.974  55.538  1.00 29.36 ? 206  LYS   A O     1 
ATOM   1324  C  CB    . LYS   A  1 208  ? -42.201 56.039  54.749  1.00 30.57 ? 206  LYS   A CB    1 
ATOM   1325  N  N     . ARG   A  1 209  ? -41.852 53.929  57.079  1.00 28.26 ? 207  ARG   A N     1 
ATOM   1326  C  CA    . ARG   A  1 209  ? -41.295 52.648  57.483  1.00 29.41 ? 207  ARG   A CA    1 
ATOM   1327  C  C     . ARG   A  1 209  ? -42.220 51.842  58.381  1.00 30.95 ? 207  ARG   A C     1 
ATOM   1328  O  O     . ARG   A  1 209  ? -41.911 50.684  58.672  1.00 31.54 ? 207  ARG   A O     1 
ATOM   1329  C  CB    . ARG   A  1 209  ? -39.963 52.866  58.185  1.00 28.52 ? 207  ARG   A CB    1 
ATOM   1330  C  CG    . ARG   A  1 209  ? -38.917 53.405  57.248  1.00 33.96 ? 207  ARG   A CG    1 
ATOM   1331  C  CD    . ARG   A  1 209  ? -37.649 53.695  57.997  1.00 31.54 ? 207  ARG   A CD    1 
ATOM   1332  N  NE    . ARG   A  1 209  ? -36.604 54.176  57.105  1.00 41.67 ? 207  ARG   A NE    1 
ATOM   1333  C  CZ    . ARG   A  1 209  ? -35.471 54.716  57.524  1.00 43.78 ? 207  ARG   A CZ    1 
ATOM   1334  N  NH1   . ARG   A  1 209  ? -35.215 54.864  58.815  1.00 38.89 ? 207  ARG   A NH1   1 
ATOM   1335  N  NH2   . ARG   A  1 209  ? -34.576 55.125  56.629  1.00 46.48 ? 207  ARG   A NH2   1 
ATOM   1336  N  N     . SER   A  1 210  ? -43.338 52.415  58.821  1.00 27.45 ? 208  SER   A N     1 
ATOM   1337  C  CA    . SER   A  1 210  ? -44.251 51.686  59.689  1.00 26.07 ? 208  SER   A CA    1 
ATOM   1338  C  C     . SER   A  1 210  ? -45.232 50.813  58.917  1.00 30.01 ? 208  SER   A C     1 
ATOM   1339  O  O     . SER   A  1 210  ? -45.849 49.923  59.516  1.00 26.55 ? 208  SER   A O     1 
ATOM   1340  C  CB    . SER   A  1 210  ? -45.016 52.675  60.566  1.00 23.79 ? 208  SER   A CB    1 
ATOM   1341  O  OG    . SER   A  1 210  ? -44.111 53.423  61.365  1.00 24.97 ? 208  SER   A OG    1 
ATOM   1342  N  N     . LYS   A  1 211  ? -45.382 51.047  57.610  1.00 29.52 ? 209  LYS   A N     1 
ATOM   1343  C  CA    . LYS   A  1 211  ? -46.360 50.307  56.819  1.00 31.13 ? 209  LYS   A CA    1 
ATOM   1344  C  C     . LYS   A  1 211  ? -46.129 48.803  56.905  1.00 28.81 ? 209  LYS   A C     1 
ATOM   1345  O  O     . LYS   A  1 211  ? -47.086 48.025  56.993  1.00 30.30 ? 209  LYS   A O     1 
ATOM   1346  C  CB    . LYS   A  1 211  ? -46.308 50.775  55.364  1.00 29.30 ? 209  LYS   A CB    1 
ATOM   1347  N  N     . GLU   A  1 212  ? -44.866 48.379  56.917  1.00 30.96 ? 210  GLU   A N     1 
ATOM   1348  C  CA    . GLU   A  1 212  ? -44.557 46.955  56.860  1.00 36.29 ? 210  GLU   A CA    1 
ATOM   1349  C  C     . GLU   A  1 212  ? -45.147 46.205  58.050  1.00 33.36 ? 210  GLU   A C     1 
ATOM   1350  O  O     . GLU   A  1 212  ? -45.861 45.212  57.879  1.00 35.18 ? 210  GLU   A O     1 
ATOM   1351  C  CB    . GLU   A  1 212  ? -43.044 46.755  56.789  1.00 35.55 ? 210  GLU   A CB    1 
ATOM   1352  C  CG    . GLU   A  1 212  ? -42.632 45.297  56.740  1.00 42.08 ? 210  GLU   A CG    1 
ATOM   1353  C  CD    . GLU   A  1 212  ? -41.133 45.126  56.716  1.00 47.55 ? 210  GLU   A CD    1 
ATOM   1354  O  OE1   . GLU   A  1 212  ? -40.428 46.140  56.542  1.00 51.42 ? 210  GLU   A OE1   1 
ATOM   1355  O  OE2   . GLU   A  1 212  ? -40.658 43.983  56.878  1.00 51.84 ? 210  GLU   A OE2   1 
ATOM   1356  N  N     . LEU   A  1 213  ? -44.864 46.665  59.267  1.00 30.72 ? 211  LEU   A N     1 
ATOM   1357  C  CA    . LEU   A  1 213  ? -45.364 45.963  60.443  1.00 30.18 ? 211  LEU   A CA    1 
ATOM   1358  C  C     . LEU   A  1 213  ? -46.824 46.268  60.731  1.00 26.51 ? 211  LEU   A C     1 
ATOM   1359  O  O     . LEU   A  1 213  ? -47.500 45.451  61.362  1.00 31.25 ? 211  LEU   A O     1 
ATOM   1360  C  CB    . LEU   A  1 213  ? -44.499 46.292  61.658  1.00 28.60 ? 211  LEU   A CB    1 
ATOM   1361  C  CG    . LEU   A  1 213  ? -43.095 45.700  61.509  1.00 31.84 ? 211  LEU   A CG    1 
ATOM   1362  C  CD1   . LEU   A  1 213  ? -42.286 45.847  62.790  1.00 29.25 ? 211  LEU   A CD1   1 
ATOM   1363  C  CD2   . LEU   A  1 213  ? -43.183 44.242  61.080  1.00 31.55 ? 211  LEU   A CD2   1 
ATOM   1364  N  N     . GLU   A  1 214  ? -47.343 47.397  60.253  1.00 27.20 ? 212  GLU   A N     1 
ATOM   1365  C  CA    . GLU   A  1 214  ? -48.780 47.613  60.370  1.00 29.47 ? 212  GLU   A CA    1 
ATOM   1366  C  C     . GLU   A  1 214  ? -49.552 46.603  59.527  1.00 32.00 ? 212  GLU   A C     1 
ATOM   1367  O  O     . GLU   A  1 214  ? -50.637 46.165  59.919  1.00 31.79 ? 212  GLU   A O     1 
ATOM   1368  C  CB    . GLU   A  1 214  ? -49.137 49.045  59.978  1.00 27.61 ? 212  GLU   A CB    1 
ATOM   1369  C  CG    . GLU   A  1 214  ? -48.697 50.084  61.001  1.00 26.83 ? 212  GLU   A CG    1 
ATOM   1370  C  CD    . GLU   A  1 214  ? -49.150 51.477  60.643  1.00 29.78 ? 212  GLU   A CD    1 
ATOM   1371  O  OE1   . GLU   A  1 214  ? -49.524 51.696  59.469  1.00 33.21 ? 212  GLU   A OE1   1 
ATOM   1372  O  OE2   . GLU   A  1 214  ? -49.141 52.358  61.533  1.00 31.98 ? 212  GLU   A OE2   1 
ATOM   1373  N  N     . GLU   A  1 215  ? -49.003 46.208  58.376  1.00 30.39 ? 213  GLU   A N     1 
ATOM   1374  C  CA    . GLU   A  1 215  ? -49.676 45.195  57.566  1.00 34.08 ? 213  GLU   A CA    1 
ATOM   1375  C  C     . GLU   A  1 215  ? -49.656 43.829  58.246  1.00 36.78 ? 213  GLU   A C     1 
ATOM   1376  O  O     . GLU   A  1 215  ? -50.532 42.996  57.982  1.00 40.66 ? 213  GLU   A O     1 
ATOM   1377  C  CB    . GLU   A  1 215  ? -49.040 45.117  56.174  1.00 34.59 ? 213  GLU   A CB    1 
ATOM   1378  N  N     . LYS   A  1 216  ? -48.686 43.585  59.129  1.00 35.90 ? 214  LYS   A N     1 
ATOM   1379  C  CA    . LYS   A  1 216  ? -48.614 42.338  59.880  1.00 35.66 ? 214  LYS   A CA    1 
ATOM   1380  C  C     . LYS   A  1 216  ? -49.364 42.391  61.208  1.00 38.20 ? 214  LYS   A C     1 
ATOM   1381  O  O     . LYS   A  1 216  ? -49.336 41.407  61.955  1.00 39.79 ? 214  LYS   A O     1 
ATOM   1382  C  CB    . LYS   A  1 216  ? -47.157 41.951  60.133  1.00 30.55 ? 214  LYS   A CB    1 
ATOM   1383  N  N     . GLY   A  1 217  ? -50.028 43.504  61.524  1.00 32.52 ? 215  GLY   A N     1 
ATOM   1384  C  CA    . GLY   A  1 217  ? -50.887 43.591  62.691  1.00 30.76 ? 215  GLY   A CA    1 
ATOM   1385  C  C     . GLY   A  1 217  ? -50.346 44.421  63.836  1.00 32.94 ? 215  GLY   A C     1 
ATOM   1386  O  O     . GLY   A  1 217  ? -50.982 44.469  64.896  1.00 27.77 ? 215  GLY   A O     1 
ATOM   1387  N  N     . PHE   A  1 218  ? -49.191 45.056  63.676  1.00 27.00 ? 216  PHE   A N     1 
ATOM   1388  C  CA    . PHE   A  1 218  ? -48.705 45.963  64.699  1.00 28.09 ? 216  PHE   A CA    1 
ATOM   1389  C  C     . PHE   A  1 218  ? -49.359 47.328  64.543  1.00 23.72 ? 216  PHE   A C     1 
ATOM   1390  O  O     . PHE   A  1 218  ? -49.867 47.685  63.480  1.00 25.53 ? 216  PHE   A O     1 
ATOM   1391  C  CB    . PHE   A  1 218  ? -47.190 46.137  64.607  1.00 23.67 ? 216  PHE   A CB    1 
ATOM   1392  C  CG    . PHE   A  1 218  ? -46.406 44.935  65.026  1.00 24.74 ? 216  PHE   A CG    1 
ATOM   1393  C  CD1   . PHE   A  1 218  ? -46.185 43.895  64.142  1.00 30.08 ? 216  PHE   A CD1   1 
ATOM   1394  C  CD2   . PHE   A  1 218  ? -45.864 44.859  66.297  1.00 23.43 ? 216  PHE   A CD2   1 
ATOM   1395  C  CE1   . PHE   A  1 218  ? -45.447 42.788  64.525  1.00 31.27 ? 216  PHE   A CE1   1 
ATOM   1396  C  CE2   . PHE   A  1 218  ? -45.114 43.753  66.685  1.00 27.67 ? 216  PHE   A CE2   1 
ATOM   1397  C  CZ    . PHE   A  1 218  ? -44.904 42.724  65.803  1.00 25.91 ? 216  PHE   A CZ    1 
ATOM   1398  N  N     . SER   A  1 219  ? -49.308 48.105  65.610  1.00 20.63 ? 217  SER   A N     1 
ATOM   1399  C  CA    . SER   A  1 219  ? -49.614 49.520  65.544  1.00 20.50 ? 217  SER   A CA    1 
ATOM   1400  C  C     . SER   A  1 219  ? -48.408 50.285  66.067  1.00 19.95 ? 217  SER   A C     1 
ATOM   1401  O  O     . SER   A  1 219  ? -47.407 49.693  66.472  1.00 20.33 ? 217  SER   A O     1 
ATOM   1402  C  CB    . SER   A  1 219  ? -50.873 49.852  66.346  1.00 22.61 ? 217  SER   A CB    1 
ATOM   1403  O  OG    . SER   A  1 219  ? -50.681 49.524  67.704  1.00 22.81 ? 217  SER   A OG    1 
ATOM   1404  N  N     . TYR   A  1 220  ? -48.511 51.612  66.060  1.00 20.35 ? 218  TYR   A N     1 
ATOM   1405  C  CA    . TYR   A  1 220  ? -47.374 52.456  66.400  1.00 18.07 ? 218  TYR   A CA    1 
ATOM   1406  C  C     . TYR   A  1 220  ? -47.792 53.578  67.335  1.00 18.73 ? 218  TYR   A C     1 
ATOM   1407  O  O     . TYR   A  1 220  ? -48.920 54.068  67.274  1.00 19.36 ? 218  TYR   A O     1 
ATOM   1408  C  CB    . TYR   A  1 220  ? -46.740 53.062  65.145  1.00 21.05 ? 218  TYR   A CB    1 
ATOM   1409  C  CG    . TYR   A  1 220  ? -45.803 52.115  64.468  1.00 20.43 ? 218  TYR   A CG    1 
ATOM   1410  C  CD1   . TYR   A  1 220  ? -46.270 51.167  63.561  1.00 21.19 ? 218  TYR   A CD1   1 
ATOM   1411  C  CD2   . TYR   A  1 220  ? -44.448 52.139  64.760  1.00 22.18 ? 218  TYR   A CD2   1 
ATOM   1412  C  CE1   . TYR   A  1 220  ? -45.396 50.285  62.953  1.00 22.95 ? 218  TYR   A CE1   1 
ATOM   1413  C  CE2   . TYR   A  1 220  ? -43.572 51.267  64.156  1.00 22.87 ? 218  TYR   A CE2   1 
ATOM   1414  C  CZ    . TYR   A  1 220  ? -44.046 50.350  63.253  1.00 23.80 ? 218  TYR   A CZ    1 
ATOM   1415  O  OH    . TYR   A  1 220  ? -43.160 49.483  62.671  1.00 24.28 ? 218  TYR   A OH    1 
ATOM   1416  N  N     . SER   A  1 221  ? -46.851 53.977  68.198  1.00 18.26 ? 219  SER   A N     1 
ATOM   1417  C  CA    . SER   A  1 221  ? -46.920 55.222  68.955  1.00 18.90 ? 219  SER   A CA    1 
ATOM   1418  C  C     . SER   A  1 221  ? -45.596 55.946  68.758  1.00 18.44 ? 219  SER   A C     1 
ATOM   1419  O  O     . SER   A  1 221  ? -44.547 55.427  69.149  1.00 20.93 ? 219  SER   A O     1 
ATOM   1420  C  CB    . SER   A  1 221  ? -47.163 54.962  70.441  1.00 20.52 ? 219  SER   A CB    1 
ATOM   1421  O  OG    . SER   A  1 221  ? -47.298 56.184  71.142  1.00 22.58 ? 219  SER   A OG    1 
ATOM   1422  N  N     . TYR   A  1 222  ? -45.634 57.133  68.154  1.00 19.49 ? 220  TYR   A N     1 
ATOM   1423  C  CA    . TYR   A  1 222  ? -44.405 57.823  67.787  1.00 17.81 ? 220  TYR   A CA    1 
ATOM   1424  C  C     . TYR   A  1 222  ? -43.943 58.733  68.908  1.00 19.99 ? 220  TYR   A C     1 
ATOM   1425  O  O     . TYR   A  1 222  ? -44.736 59.474  69.495  1.00 19.78 ? 220  TYR   A O     1 
ATOM   1426  C  CB    . TYR   A  1 222  ? -44.590 58.618  66.492  1.00 19.01 ? 220  TYR   A CB    1 
ATOM   1427  C  CG    . TYR   A  1 222  ? -44.926 57.688  65.374  1.00 19.51 ? 220  TYR   A CG    1 
ATOM   1428  C  CD1   . TYR   A  1 222  ? -43.925 56.997  64.696  1.00 18.25 ? 220  TYR   A CD1   1 
ATOM   1429  C  CD2   . TYR   A  1 222  ? -46.254 57.441  65.026  1.00 17.49 ? 220  TYR   A CD2   1 
ATOM   1430  C  CE1   . TYR   A  1 222  ? -44.242 56.099  63.688  1.00 19.45 ? 220  TYR   A CE1   1 
ATOM   1431  C  CE2   . TYR   A  1 222  ? -46.573 56.544  64.020  1.00 17.28 ? 220  TYR   A CE2   1 
ATOM   1432  C  CZ    . TYR   A  1 222  ? -45.561 55.890  63.354  1.00 18.30 ? 220  TYR   A CZ    1 
ATOM   1433  O  OH    . TYR   A  1 222  ? -45.871 54.995  62.363  1.00 20.64 ? 220  TYR   A OH    1 
ATOM   1434  N  N     . ASP   A  1 223  ? -42.656 58.670  69.187  1.00 20.32 ? 221  ASP   A N     1 
ATOM   1435  C  CA    . ASP   A  1 223  ? -42.011 59.452  70.228  1.00 22.70 ? 221  ASP   A CA    1 
ATOM   1436  C  C     . ASP   A  1 223  ? -41.077 60.415  69.517  1.00 24.87 ? 221  ASP   A C     1 
ATOM   1437  O  O     . ASP   A  1 223  ? -40.021 60.007  69.015  1.00 24.45 ? 221  ASP   A O     1 
ATOM   1438  C  CB    . ASP   A  1 223  ? -41.258 58.533  71.181  1.00 22.92 ? 221  ASP   A CB    1 
ATOM   1439  C  CG    . ASP   A  1 223  ? -40.370 59.286  72.169  1.00 28.67 ? 221  ASP   A CG    1 
ATOM   1440  O  OD1   . ASP   A  1 223  ? -40.492 60.516  72.317  1.00 30.14 ? 221  ASP   A OD1   1 
ATOM   1441  O  OD2   . ASP   A  1 223  ? -39.541 58.622  72.813  1.00 36.39 ? 221  ASP   A OD2   1 
ATOM   1442  N  N     . MET   A  1 224  ? -41.492 61.674  69.433  1.00 23.13 ? 222  MET   A N     1 
ATOM   1443  C  CA    . MET   A  1 224  ? -40.608 62.733  68.966  1.00 23.79 ? 222  MET   A CA    1 
ATOM   1444  C  C     . MET   A  1 224  ? -39.605 62.998  70.074  1.00 27.66 ? 222  MET   A C     1 
ATOM   1445  O  O     . MET   A  1 224  ? -39.967 63.517  71.132  1.00 37.77 ? 222  MET   A O     1 
ATOM   1446  C  CB    . MET   A  1 224  ? -41.404 63.986  68.622  1.00 24.65 ? 222  MET   A CB    1 
ATOM   1447  C  CG    . MET   A  1 224  ? -42.571 63.697  67.674  1.00 26.58 ? 222  MET   A CG    1 
ATOM   1448  S  SD    . MET   A  1 224  ? -42.026 63.047  66.076  1.00 31.86 ? 222  MET   A SD    1 
ATOM   1449  C  CE    . MET   A  1 224  ? -41.165 64.462  65.420  1.00 28.65 ? 222  MET   A CE    1 
ATOM   1450  N  N     . LEU   A  1 225  ? -38.369 62.577  69.859  1.00 29.42 ? 223  LEU   A N     1 
ATOM   1451  C  CA    . LEU   A  1 225  ? -37.368 62.602  70.915  1.00 33.60 ? 223  LEU   A CA    1 
ATOM   1452  C  C     . LEU   A  1 225  ? -37.263 64.006  71.480  1.00 36.63 ? 223  LEU   A C     1 
ATOM   1453  O  O     . LEU   A  1 225  ? -36.830 64.940  70.794  1.00 42.57 ? 223  LEU   A O     1 
ATOM   1454  C  CB    . LEU   A  1 225  ? -36.034 62.096  70.381  1.00 30.19 ? 223  LEU   A CB    1 
ATOM   1455  C  CG    . LEU   A  1 225  ? -36.135 60.606  70.045  1.00 28.54 ? 223  LEU   A CG    1 
ATOM   1456  C  CD1   . LEU   A  1 225  ? -34.858 60.107  69.370  1.00 29.00 ? 223  LEU   A CD1   1 
ATOM   1457  C  CD2   . LEU   A  1 225  ? -36.448 59.796  71.302  1.00 29.81 ? 223  LEU   A CD2   1 
ATOM   1458  N  N     . GLY   A  1 226  ? -37.713 64.156  72.717  1.00 33.52 ? 224  GLY   A N     1 
ATOM   1459  C  CA    . GLY   A  1 226  ? -37.913 65.448  73.332  1.00 34.56 ? 224  GLY   A CA    1 
ATOM   1460  C  C     . GLY   A  1 226  ? -38.257 65.283  74.796  1.00 29.46 ? 224  GLY   A C     1 
ATOM   1461  O  O     . GLY   A  1 226  ? -39.183 64.545  75.150  1.00 28.76 ? 224  GLY   A O     1 
ATOM   1462  N  N     . GLU   A  1 227  ? -37.487 65.936  75.660  1.00 27.86 ? 225  GLU   A N     1 
ATOM   1463  C  CA    . GLU   A  1 227  ? -37.769 65.918  77.085  1.00 24.03 ? 225  GLU   A CA    1 
ATOM   1464  C  C     . GLU   A  1 227  ? -36.907 66.969  77.752  1.00 24.86 ? 225  GLU   A C     1 
ATOM   1465  O  O     . GLU   A  1 227  ? -35.946 67.477  77.163  1.00 25.17 ? 225  GLU   A O     1 
ATOM   1466  C  CB    . GLU   A  1 227  ? -37.498 64.553  77.718  1.00 26.19 ? 225  GLU   A CB    1 
ATOM   1467  C  CG    . GLU   A  1 227  ? -36.090 64.047  77.543  1.00 33.67 ? 225  GLU   A CG    1 
ATOM   1468  C  CD    . GLU   A  1 227  ? -35.942 62.628  78.048  1.00 33.96 ? 225  GLU   A CD    1 
ATOM   1469  O  OE1   . GLU   A  1 227  ? -35.720 62.447  79.264  1.00 37.51 ? 225  GLU   A OE1   1 
ATOM   1470  O  OE2   . GLU   A  1 227  ? -36.078 61.696  77.234  1.00 35.07 ? 225  GLU   A OE2   1 
ATOM   1471  N  N     . ALA   A  1 228  ? -37.277 67.285  78.987  1.00 22.05 ? 226  ALA   A N     1 
ATOM   1472  C  CA    . ALA   A  1 228  ? -36.472 68.132  79.853  1.00 23.89 ? 226  ALA   A CA    1 
ATOM   1473  C  C     . ALA   A  1 228  ? -36.129 69.452  79.168  1.00 23.29 ? 226  ALA   A C     1 
ATOM   1474  O  O     . ALA   A  1 228  ? -34.962 69.828  79.038  1.00 23.85 ? 226  ALA   A O     1 
ATOM   1475  C  CB    . ALA   A  1 228  ? -35.204 67.392  80.284  1.00 21.46 ? 226  ALA   A CB    1 
ATOM   1476  N  N     . ALA   A  1 229  ? -37.159 70.158  78.716  1.00 21.18 ? 227  ALA   A N     1 
ATOM   1477  C  CA    . ALA   A  1 229  ? -36.933 71.486  78.163  1.00 20.56 ? 227  ALA   A CA    1 
ATOM   1478  C  C     . ALA   A  1 229  ? -36.233 72.348  79.201  1.00 20.09 ? 227  ALA   A C     1 
ATOM   1479  O  O     . ALA   A  1 229  ? -36.585 72.328  80.385  1.00 17.41 ? 227  ALA   A O     1 
ATOM   1480  C  CB    . ALA   A  1 229  ? -38.250 72.142  77.744  1.00 19.67 ? 227  ALA   A CB    1 
ATOM   1481  N  N     . THR   A  1 230  ? -35.217 73.077  78.752  1.00 18.03 ? 228  THR   A N     1 
ATOM   1482  C  CA    . THR   A  1 230  ? -34.449 73.970  79.606  1.00 21.46 ? 228  THR   A CA    1 
ATOM   1483  C  C     . THR   A  1 230  ? -34.917 75.412  79.507  1.00 20.12 ? 228  THR   A C     1 
ATOM   1484  O  O     . THR   A  1 230  ? -34.761 76.180  80.459  1.00 20.99 ? 228  THR   A O     1 
ATOM   1485  C  CB    . THR   A  1 230  ? -32.959 73.893  79.223  1.00 22.91 ? 228  THR   A CB    1 
ATOM   1486  O  OG1   . THR   A  1 230  ? -32.521 72.531  79.294  1.00 30.33 ? 228  THR   A OG1   1 
ATOM   1487  C  CG2   . THR   A  1 230  ? -32.117 74.721  80.150  1.00 28.74 ? 228  THR   A CG2   1 
ATOM   1488  N  N     . THR   A  1 231  ? -35.463 75.801  78.363  1.00 19.40 ? 229  THR   A N     1 
ATOM   1489  C  CA    . THR   A  1 231  ? -35.839 77.183  78.111  1.00 19.41 ? 229  THR   A CA    1 
ATOM   1490  C  C     . THR   A  1 231  ? -37.227 77.214  77.489  1.00 15.56 ? 229  THR   A C     1 
ATOM   1491  O  O     . THR   A  1 231  ? -37.729 76.202  76.993  1.00 18.06 ? 229  THR   A O     1 
ATOM   1492  C  CB    . THR   A  1 231  ? -34.865 77.863  77.158  1.00 22.59 ? 229  THR   A CB    1 
ATOM   1493  O  OG1   . THR   A  1 231  ? -35.022 77.269  75.864  1.00 20.72 ? 229  THR   A OG1   1 
ATOM   1494  C  CG2   . THR   A  1 231  ? -33.404 77.683  77.630  1.00 20.61 ? 229  THR   A CG2   1 
ATOM   1495  N  N     . ALA   A  1 232  ? -37.843 78.394  77.517  1.00 18.61 ? 230  ALA   A N     1 
ATOM   1496  C  CA    . ALA   A  1 232  ? -39.104 78.573  76.804  1.00 18.57 ? 230  ALA   A CA    1 
ATOM   1497  C  C     . ALA   A  1 232  ? -38.952 78.209  75.332  1.00 21.56 ? 230  ALA   A C     1 
ATOM   1498  O  O     . ALA   A  1 232  ? -39.830 77.560  74.745  1.00 19.96 ? 230  ALA   A O     1 
ATOM   1499  C  CB    . ALA   A  1 232  ? -39.596 80.011  76.961  1.00 19.61 ? 230  ALA   A CB    1 
ATOM   1500  N  N     . ALA   A  1 233  ? -37.832 78.597  74.722  1.00 21.91 ? 231  ALA   A N     1 
ATOM   1501  C  CA    . ALA   A  1 233  ? -37.650 78.321  73.300  1.00 23.58 ? 231  ALA   A CA    1 
ATOM   1502  C  C     . ALA   A  1 233  ? -37.582 76.824  73.043  1.00 23.22 ? 231  ALA   A C     1 
ATOM   1503  O  O     . ALA   A  1 233  ? -38.121 76.335  72.043  1.00 23.60 ? 231  ALA   A O     1 
ATOM   1504  C  CB    . ALA   A  1 233  ? -36.387 79.014  72.781  1.00 25.22 ? 231  ALA   A CB    1 
ATOM   1505  N  N     . ASP   A  1 234  ? -36.935 76.075  73.943  1.00 21.14 ? 232  ASP   A N     1 
ATOM   1506  C  CA    . ASP   A  1 234  ? -36.871 74.631  73.762  1.00 22.10 ? 232  ASP   A CA    1 
ATOM   1507  C  C     . ASP   A  1 234  ? -38.242 74.006  73.947  1.00 18.08 ? 232  ASP   A C     1 
ATOM   1508  O  O     . ASP   A  1 234  ? -38.611 73.081  73.217  1.00 19.58 ? 232  ASP   A O     1 
ATOM   1509  C  CB    . ASP   A  1 234  ? -35.872 74.004  74.733  1.00 21.63 ? 232  ASP   A CB    1 
ATOM   1510  C  CG    . ASP   A  1 234  ? -34.429 74.248  74.322  1.00 27.63 ? 232  ASP   A CG    1 
ATOM   1511  O  OD1   . ASP   A  1 234  ? -34.194 74.559  73.140  1.00 33.63 ? 232  ASP   A OD1   1 
ATOM   1512  O  OD2   . ASP   A  1 234  ? -33.534 74.141  75.187  1.00 41.20 ? 232  ASP   A OD2   1 
ATOM   1513  N  N     . ALA   A  1 235  ? -39.012 74.505  74.912  1.00 18.21 ? 233  ALA   A N     1 
ATOM   1514  C  CA    . ALA   A  1 235  ? -40.363 73.988  75.102  1.00 19.28 ? 233  ALA   A CA    1 
ATOM   1515  C  C     . ALA   A  1 235  ? -41.226 74.263  73.881  1.00 20.67 ? 233  ALA   A C     1 
ATOM   1516  O  O     . ALA   A  1 235  ? -42.014 73.408  73.459  1.00 17.75 ? 233  ALA   A O     1 
ATOM   1517  C  CB    . ALA   A  1 235  ? -40.986 74.607  76.342  1.00 18.66 ? 233  ALA   A CB    1 
ATOM   1518  N  N     . GLU   A  1 236  ? -41.088 75.458  73.305  1.00 19.41 ? 234  GLU   A N     1 
ATOM   1519  C  CA    . GLU   A  1 236  ? -41.835 75.801  72.101  1.00 23.62 ? 234  GLU   A CA    1 
ATOM   1520  C  C     . GLU   A  1 236  ? -41.407 74.935  70.915  1.00 20.47 ? 234  GLU   A C     1 
ATOM   1521  O  O     . GLU   A  1 236  ? -42.244 74.531  70.094  1.00 19.99 ? 234  GLU   A O     1 
ATOM   1522  C  CB    . GLU   A  1 236  ? -41.653 77.295  71.807  1.00 22.72 ? 234  GLU   A CB    1 
ATOM   1523  C  CG    . GLU   A  1 236  ? -42.494 77.823  70.663  1.00 32.07 ? 234  GLU   A CG    1 
ATOM   1524  C  CD    . GLU   A  1 236  ? -43.995 77.612  70.863  1.00 36.58 ? 234  GLU   A CD    1 
ATOM   1525  O  OE1   . GLU   A  1 236  ? -44.489 77.821  71.993  1.00 39.88 ? 234  GLU   A OE1   1 
ATOM   1526  O  OE2   . GLU   A  1 236  ? -44.684 77.228  69.887  1.00 35.54 ? 234  GLU   A OE2   1 
ATOM   1527  N  N     . ARG   A  1 237  ? -40.110 74.624  70.817  1.00 20.31 ? 235  ARG   A N     1 
ATOM   1528  C  CA    . ARG   A  1 237  ? -39.628 73.756  69.747  1.00 23.25 ? 235  ARG   A CA    1 
ATOM   1529  C  C     . ARG   A  1 237  ? -40.199 72.348  69.880  1.00 22.25 ? 235  ARG   A C     1 
ATOM   1530  O  O     . ARG   A  1 237  ? -40.655 71.758  68.892  1.00 22.62 ? 235  ARG   A O     1 
ATOM   1531  C  CB    . ARG   A  1 237  ? -38.092 73.720  69.745  1.00 22.52 ? 235  ARG   A CB    1 
ATOM   1532  C  CG    . ARG   A  1 237  ? -37.493 72.725  68.754  1.00 28.21 ? 235  ARG   A CG    1 
ATOM   1533  C  CD    . ARG   A  1 237  ? -36.006 73.015  68.480  1.00 32.82 ? 235  ARG   A CD    1 
ATOM   1534  N  NE    . ARG   A  1 237  ? -35.217 72.954  69.703  1.00 39.03 ? 235  ARG   A NE    1 
ATOM   1535  C  CZ    . ARG   A  1 237  ? -34.777 71.833  70.256  1.00 43.94 ? 235  ARG   A CZ    1 
ATOM   1536  N  NH1   . ARG   A  1 237  ? -34.984 70.653  69.688  1.00 46.55 ? 235  ARG   A NH1   1 
ATOM   1537  N  NH2   . ARG   A  1 237  ? -34.118 71.894  71.411  1.00 40.37 ? 235  ARG   A NH2   1 
ATOM   1538  N  N     . TYR   A  1 238  ? -40.200 71.797  71.094  1.00 19.25 ? 236  TYR   A N     1 
ATOM   1539  C  CA    . TYR   A  1 238  ? -40.815 70.489  71.292  1.00 17.16 ? 236  TYR   A CA    1 
ATOM   1540  C  C     . TYR   A  1 238  ? -42.310 70.540  71.024  1.00 19.23 ? 236  TYR   A C     1 
ATOM   1541  O  O     . TYR   A  1 238  ? -42.884 69.582  70.491  1.00 21.69 ? 236  TYR   A O     1 
ATOM   1542  C  CB    . TYR   A  1 238  ? -40.552 69.992  72.711  1.00 17.23 ? 236  TYR   A CB    1 
ATOM   1543  C  CG    . TYR   A  1 238  ? -39.098 69.671  72.974  1.00 19.50 ? 236  TYR   A CG    1 
ATOM   1544  C  CD1   . TYR   A  1 238  ? -38.309 69.088  71.993  1.00 27.14 ? 236  TYR   A CD1   1 
ATOM   1545  C  CD2   . TYR   A  1 238  ? -38.518 69.956  74.202  1.00 19.93 ? 236  TYR   A CD2   1 
ATOM   1546  C  CE1   . TYR   A  1 238  ? -36.977 68.795  72.231  1.00 29.62 ? 236  TYR   A CE1   1 
ATOM   1547  C  CE2   . TYR   A  1 238  ? -37.192 69.665  74.447  1.00 22.73 ? 236  TYR   A CE2   1 
ATOM   1548  C  CZ    . TYR   A  1 238  ? -36.430 69.088  73.460  1.00 28.08 ? 236  TYR   A CZ    1 
ATOM   1549  O  OH    . TYR   A  1 238  ? -35.116 68.797  73.708  1.00 33.08 ? 236  TYR   A OH    1 
ATOM   1550  N  N     . TYR   A  1 239  ? -42.961 71.644  71.397  1.00 18.24 ? 237  TYR   A N     1 
ATOM   1551  C  CA    . TYR   A  1 239  ? -44.381 71.778  71.103  1.00 20.93 ? 237  TYR   A CA    1 
ATOM   1552  C  C     . TYR   A  1 239  ? -44.626 71.701  69.605  1.00 19.78 ? 237  TYR   A C     1 
ATOM   1553  O  O     . TYR   A  1 239  ? -45.475 70.937  69.141  1.00 17.32 ? 237  TYR   A O     1 
ATOM   1554  C  CB    . TYR   A  1 239  ? -44.945 73.084  71.652  1.00 20.46 ? 237  TYR   A CB    1 
ATOM   1555  C  CG    . TYR   A  1 239  ? -46.413 73.182  71.352  1.00 19.36 ? 237  TYR   A CG    1 
ATOM   1556  C  CD1   . TYR   A  1 239  ? -46.870 73.701  70.143  1.00 20.41 ? 237  TYR   A CD1   1 
ATOM   1557  C  CD2   . TYR   A  1 239  ? -47.344 72.691  72.243  1.00 19.97 ? 237  TYR   A CD2   1 
ATOM   1558  C  CE1   . TYR   A  1 239  ? -48.209 73.752  69.852  1.00 23.94 ? 237  TYR   A CE1   1 
ATOM   1559  C  CE2   . TYR   A  1 239  ? -48.682 72.756  71.971  1.00 19.76 ? 237  TYR   A CE2   1 
ATOM   1560  C  CZ    . TYR   A  1 239  ? -49.115 73.278  70.776  1.00 26.35 ? 237  TYR   A CZ    1 
ATOM   1561  O  OH    . TYR   A  1 239  ? -50.456 73.330  70.502  1.00 24.36 ? 237  TYR   A OH    1 
ATOM   1562  N  N     . ARG   A  1 240  ? -43.898 72.491  68.823  1.00 19.73 ? 238  ARG   A N     1 
ATOM   1563  C  CA    . ARG   A  1 240  ? -44.214 72.465  67.405  1.00 21.73 ? 238  ARG   A CA    1 
ATOM   1564  C  C     . ARG   A  1 240  ? -43.785 71.153  66.755  1.00 19.01 ? 238  ARG   A C     1 
ATOM   1565  O  O     . ARG   A  1 240  ? -44.400 70.745  65.762  1.00 19.71 ? 238  ARG   A O     1 
ATOM   1566  C  CB    . ARG   A  1 240  ? -43.615 73.687  66.703  1.00 24.66 ? 238  ARG   A CB    1 
ATOM   1567  C  CG    . ARG   A  1 240  ? -42.137 73.776  66.707  1.00 24.17 ? 238  ARG   A CG    1 
ATOM   1568  C  CD    . ARG   A  1 240  ? -41.698 74.979  65.881  1.00 23.78 ? 238  ARG   A CD    1 
ATOM   1569  N  NE    . ARG   A  1 240  ? -40.263 75.154  66.006  1.00 27.62 ? 238  ARG   A NE    1 
ATOM   1570  C  CZ    . ARG   A  1 240  ? -39.677 75.958  66.886  1.00 27.03 ? 238  ARG   A CZ    1 
ATOM   1571  N  NH1   . ARG   A  1 240  ? -40.378 76.749  67.686  1.00 25.09 ? 238  ARG   A NH1   1 
ATOM   1572  N  NH2   . ARG   A  1 240  ? -38.352 75.966  66.966  1.00 30.35 ? 238  ARG   A NH2   1 
ATOM   1573  N  N     . ASP   A  1 241  ? -42.789 70.456  67.316  1.00 20.29 ? 239  ASP   A N     1 
ATOM   1574  C  CA    . ASP   A  1 241  ? -42.480 69.100  66.859  1.00 19.21 ? 239  ASP   A CA    1 
ATOM   1575  C  C     . ASP   A  1 241  ? -43.651 68.151  67.110  1.00 19.95 ? 239  ASP   A C     1 
ATOM   1576  O  O     . ASP   A  1 241  ? -44.010 67.348  66.244  1.00 19.35 ? 239  ASP   A O     1 
ATOM   1577  C  CB    . ASP   A  1 241  ? -41.224 68.569  67.556  1.00 25.28 ? 239  ASP   A CB    1 
ATOM   1578  C  CG    . ASP   A  1 241  ? -39.959 69.329  67.161  1.00 32.95 ? 239  ASP   A CG    1 
ATOM   1579  O  OD1   . ASP   A  1 241  ? -40.030 70.165  66.233  1.00 35.45 ? 239  ASP   A OD1   1 
ATOM   1580  O  OD2   . ASP   A  1 241  ? -38.904 69.101  67.804  1.00 36.11 ? 239  ASP   A OD2   1 
ATOM   1581  N  N     . TYR   A  1 242  ? -44.238 68.210  68.310  1.00 16.02 ? 240  TYR   A N     1 
ATOM   1582  C  CA    . TYR   A  1 242  ? -45.404 67.378  68.604  1.00 16.97 ? 240  TYR   A CA    1 
ATOM   1583  C  C     . TYR   A  1 242  ? -46.574 67.743  67.702  1.00 16.21 ? 240  TYR   A C     1 
ATOM   1584  O  O     . TYR   A  1 242  ? -47.277 66.866  67.180  1.00 17.32 ? 240  TYR   A O     1 
ATOM   1585  C  CB    . TYR   A  1 242  ? -45.825 67.541  70.064  1.00 17.17 ? 240  TYR   A CB    1 
ATOM   1586  C  CG    . TYR   A  1 242  ? -44.938 66.891  71.092  1.00 16.97 ? 240  TYR   A CG    1 
ATOM   1587  C  CD1   . TYR   A  1 242  ? -44.264 65.710  70.826  1.00 19.52 ? 240  TYR   A CD1   1 
ATOM   1588  C  CD2   . TYR   A  1 242  ? -44.794 67.459  72.350  1.00 17.42 ? 240  TYR   A CD2   1 
ATOM   1589  C  CE1   . TYR   A  1 242  ? -43.450 65.122  71.790  1.00 21.74 ? 240  TYR   A CE1   1 
ATOM   1590  C  CE2   . TYR   A  1 242  ? -43.996 66.888  73.306  1.00 18.50 ? 240  TYR   A CE2   1 
ATOM   1591  C  CZ    . TYR   A  1 242  ? -43.324 65.722  73.023  1.00 18.28 ? 240  TYR   A CZ    1 
ATOM   1592  O  OH    . TYR   A  1 242  ? -42.543 65.152  73.994  1.00 17.40 ? 240  TYR   A OH    1 
ATOM   1593  N  N     . GLU   A  1 243  ? -46.836 69.040  67.557  1.00 16.27 ? 241  GLU   A N     1 
ATOM   1594  C  CA    . GLU   A  1 243  ? -47.992 69.467  66.782  1.00 16.46 ? 241  GLU   A CA    1 
ATOM   1595  C  C     . GLU   A  1 243  ? -47.857 69.023  65.334  1.00 18.60 ? 241  GLU   A C     1 
ATOM   1596  O  O     . GLU   A  1 243  ? -48.800 68.475  64.751  1.00 16.79 ? 241  GLU   A O     1 
ATOM   1597  C  CB    . GLU   A  1 243  ? -48.151 70.985  66.877  1.00 17.28 ? 241  GLU   A CB    1 
ATOM   1598  C  CG    . GLU   A  1 243  ? -49.210 71.560  65.954  1.00 18.07 ? 241  GLU   A CG    1 
ATOM   1599  C  CD    . GLU   A  1 243  ? -49.160 73.083  65.895  1.00 22.89 ? 241  GLU   A CD    1 
ATOM   1600  O  OE1   . GLU   A  1 243  ? -48.050 73.655  65.952  1.00 28.85 ? 241  GLU   A OE1   1 
ATOM   1601  O  OE2   . GLU   A  1 243  ? -50.228 73.710  65.804  1.00 26.05 ? 241  GLU   A OE2   1 
ATOM   1602  N  N     . SER   A  1 244  ? -46.668 69.228  64.747  1.00 19.04 ? 242  SER   A N     1 
ATOM   1603  C  CA    . SER   A  1 244  ? -46.446 68.816  63.363  1.00 19.49 ? 242  SER   A CA    1 
ATOM   1604  C  C     . SER   A  1 244  ? -46.539 67.300  63.231  1.00 19.40 ? 242  SER   A C     1 
ATOM   1605  O  O     . SER   A  1 244  ? -47.090 66.789  62.249  1.00 19.02 ? 242  SER   A O     1 
ATOM   1606  C  CB    . SER   A  1 244  ? -45.093 69.335  62.859  1.00 20.71 ? 242  SER   A CB    1 
ATOM   1607  O  OG    . SER   A  1 244  ? -44.005 68.769  63.572  1.00 23.15 ? 242  SER   A OG    1 
ATOM   1608  N  N     . ALA   A  1 245  ? -46.039 66.563  64.231  1.00 18.55 ? 243  ALA   A N     1 
ATOM   1609  C  CA    . ALA   A  1 245  ? -46.148 65.110  64.198  1.00 17.80 ? 243  ALA   A CA    1 
ATOM   1610  C  C     . ALA   A  1 245  ? -47.605 64.653  64.306  1.00 16.79 ? 243  ALA   A C     1 
ATOM   1611  O  O     . ALA   A  1 245  ? -48.001 63.680  63.659  1.00 17.37 ? 243  ALA   A O     1 
ATOM   1612  C  CB    . ALA   A  1 245  ? -45.315 64.495  65.323  1.00 19.71 ? 243  ALA   A CB    1 
ATOM   1613  N  N     . ILE   A  1 246  ? -48.406 65.303  65.154  1.00 16.69 ? 244  ILE   A N     1 
ATOM   1614  C  CA    . ILE   A  1 246  ? -49.809 64.891  65.255  1.00 16.77 ? 244  ILE   A CA    1 
ATOM   1615  C  C     . ILE   A  1 246  ? -50.490 65.020  63.902  1.00 18.21 ? 244  ILE   A C     1 
ATOM   1616  O  O     . ILE   A  1 246  ? -51.251 64.134  63.485  1.00 17.31 ? 244  ILE   A O     1 
ATOM   1617  C  CB    . ILE   A  1 246  ? -50.541 65.691  66.344  1.00 16.66 ? 244  ILE   A CB    1 
ATOM   1618  C  CG1   . ILE   A  1 246  ? -49.994 65.312  67.723  1.00 16.43 ? 244  ILE   A CG1   1 
ATOM   1619  C  CG2   . ILE   A  1 246  ? -52.051 65.409  66.290  1.00 19.41 ? 244  ILE   A CG2   1 
ATOM   1620  C  CD1   . ILE   A  1 246  ? -50.568 66.162  68.879  1.00 17.83 ? 244  ILE   A CD1   1 
ATOM   1621  N  N     . HIS   A  1 247  ? -50.210 66.108  63.178  1.00 18.65 ? 245  HIS   A N     1 
ATOM   1622  C  CA    . HIS   A  1 247  ? -50.799 66.247  61.852  1.00 17.74 ? 245  HIS   A CA    1 
ATOM   1623  C  C     . HIS   A  1 247  ? -50.345 65.123  60.931  1.00 18.80 ? 245  HIS   A C     1 
ATOM   1624  O  O     . HIS   A  1 247  ? -51.160 64.545  60.205  1.00 20.62 ? 245  HIS   A O     1 
ATOM   1625  C  CB    . HIS   A  1 247  ? -50.450 67.606  61.244  1.00 19.89 ? 245  HIS   A CB    1 
ATOM   1626  C  CG    . HIS   A  1 247  ? -51.203 68.748  61.847  1.00 17.45 ? 245  HIS   A CG    1 
ATOM   1627  N  ND1   . HIS   A  1 247  ? -52.550 68.935  61.647  1.00 18.84 ? 245  HIS   A ND1   1 
ATOM   1628  C  CD2   . HIS   A  1 247  ? -50.790 69.782  62.618  1.00 19.21 ? 245  HIS   A CD2   1 
ATOM   1629  C  CE1   . HIS   A  1 247  ? -52.944 70.021  62.288  1.00 22.09 ? 245  HIS   A CE1   1 
ATOM   1630  N  NE2   . HIS   A  1 247  ? -51.895 70.554  62.883  1.00 19.37 ? 245  HIS   A NE2   1 
ATOM   1631  N  N     . ALA   A  1 248  ? -49.048 64.795  60.950  1.00 18.27 ? 246  ALA   A N     1 
ATOM   1632  C  CA    . ALA   A  1 248  ? -48.537 63.765  60.054  1.00 20.05 ? 246  ALA   A CA    1 
ATOM   1633  C  C     . ALA   A  1 248  ? -49.111 62.396  60.400  1.00 22.11 ? 246  ALA   A C     1 
ATOM   1634  O  O     . ALA   A  1 248  ? -49.532 61.647  59.512  1.00 19.24 ? 246  ALA   A O     1 
ATOM   1635  C  CB    . ALA   A  1 248  ? -47.008 63.742  60.103  1.00 20.20 ? 246  ALA   A CB    1 
ATOM   1636  N  N     . ILE   A  1 249  ? -49.131 62.058  61.694  1.00 19.71 ? 247  ILE   A N     1 
ATOM   1637  C  CA    . ILE   A  1 249  ? -49.694 60.786  62.142  1.00 19.13 ? 247  ILE   A CA    1 
ATOM   1638  C  C     . ILE   A  1 249  ? -51.192 60.733  61.870  1.00 17.84 ? 247  ILE   A C     1 
ATOM   1639  O  O     . ILE   A  1 249  ? -51.726 59.698  61.461  1.00 19.81 ? 247  ILE   A O     1 
ATOM   1640  C  CB    . ILE   A  1 249  ? -49.397 60.582  63.638  1.00 18.10 ? 247  ILE   A CB    1 
ATOM   1641  C  CG1   . ILE   A  1 249  ? -47.887 60.564  63.909  1.00 19.52 ? 247  ILE   A CG1   1 
ATOM   1642  C  CG2   . ILE   A  1 249  ? -50.107 59.326  64.161  1.00 18.01 ? 247  ILE   A CG2   1 
ATOM   1643  C  CD1   . ILE   A  1 249  ? -47.539 60.912  65.373  1.00 16.76 ? 247  ILE   A CD1   1 
ATOM   1644  N  N     . GLY   A  1 250  ? -51.900 61.836  62.114  1.00 17.53 ? 248  GLY   A N     1 
ATOM   1645  C  CA    . GLY   A  1 250  ? -53.331 61.837  61.880  1.00 19.70 ? 248  GLY   A CA    1 
ATOM   1646  C  C     . GLY   A  1 250  ? -53.667 61.728  60.406  1.00 18.57 ? 248  GLY   A C     1 
ATOM   1647  O  O     . GLY   A  1 250  ? -54.607 61.025  60.023  1.00 18.46 ? 248  GLY   A O     1 
ATOM   1648  N  N     . LYS   A  1 251  ? -52.899 62.416  59.560  1.00 18.91 ? 249  LYS   A N     1 
ATOM   1649  C  CA    . LYS   A  1 251  ? -53.054 62.266  58.118  1.00 19.52 ? 249  LYS   A CA    1 
ATOM   1650  C  C     . LYS   A  1 251  ? -52.832 60.824  57.683  1.00 20.59 ? 249  LYS   A C     1 
ATOM   1651  O  O     . LYS   A  1 251  ? -53.587 60.284  56.862  1.00 20.72 ? 249  LYS   A O     1 
ATOM   1652  C  CB    . LYS   A  1 251  ? -52.066 63.164  57.385  1.00 22.10 ? 249  LYS   A CB    1 
ATOM   1653  C  CG    . LYS   A  1 251  ? -52.366 64.636  57.386  1.00 22.28 ? 249  LYS   A CG    1 
ATOM   1654  C  CD    . LYS   A  1 251  ? -51.281 65.276  56.543  1.00 25.72 ? 249  LYS   A CD    1 
ATOM   1655  C  CE    . LYS   A  1 251  ? -51.141 66.746  56.769  1.00 29.10 ? 249  LYS   A CE    1 
ATOM   1656  N  NZ    . LYS   A  1 251  ? -49.870 67.156  56.080  1.00 23.94 ? 249  LYS   A NZ    1 
ATOM   1657  N  N     . ALA   A  1 252  ? -51.777 60.196  58.207  1.00 18.51 ? 250  ALA   A N     1 
ATOM   1658  C  CA    . ALA   A  1 252  ? -51.494 58.804  57.877  1.00 19.02 ? 250  ALA   A CA    1 
ATOM   1659  C  C     . ALA   A  1 252  ? -52.524 57.870  58.498  1.00 23.56 ? 250  ALA   A C     1 
ATOM   1660  O  O     . ALA   A  1 252  ? -52.906 56.862  57.887  1.00 25.69 ? 250  ALA   A O     1 
ATOM   1661  C  CB    . ALA   A  1 252  ? -50.085 58.432  58.343  1.00 21.47 ? 250  ALA   A CB    1 
ATOM   1662  N  N     . SER   A  1 253  ? -52.985 58.180  59.713  1.00 19.46 ? 251  SER   A N     1 
ATOM   1663  C  CA    . SER   A  1 253  ? -53.970 57.311  60.350  1.00 21.70 ? 251  SER   A CA    1 
ATOM   1664  C  C     . SER   A  1 253  ? -55.189 57.133  59.463  1.00 24.39 ? 251  SER   A C     1 
ATOM   1665  O  O     . SER   A  1 253  ? -55.718 56.021  59.330  1.00 23.21 ? 251  SER   A O     1 
ATOM   1666  C  CB    . SER   A  1 253  ? -54.389 57.876  61.701  1.00 20.27 ? 251  SER   A CB    1 
ATOM   1667  O  OG    . SER   A  1 253  ? -55.435 57.088  62.224  1.00 21.52 ? 251  SER   A OG    1 
ATOM   1668  N  N     . ALA   A  1 254  ? -55.644 58.223  58.846  1.00 21.92 ? 252  ALA   A N     1 
ATOM   1669  C  CA    . ALA   A  1 254  ? -56.694 58.175  57.835  1.00 23.84 ? 252  ALA   A CA    1 
ATOM   1670  C  C     . ALA   A  1 254  ? -57.960 57.516  58.377  1.00 25.60 ? 252  ALA   A C     1 
ATOM   1671  O  O     . ALA   A  1 254  ? -58.591 56.691  57.713  1.00 25.35 ? 252  ALA   A O     1 
ATOM   1672  C  CB    . ALA   A  1 254  ? -56.200 57.467  56.575  1.00 26.11 ? 252  ALA   A CB    1 
ATOM   1673  N  N     . GLY   A  1 255  ? -58.342 57.886  59.594  1.00 23.69 ? 253  GLY   A N     1 
ATOM   1674  C  CA    . GLY   A  1 255  ? -59.576 57.379  60.155  1.00 23.34 ? 253  GLY   A CA    1 
ATOM   1675  C  C     . GLY   A  1 255  ? -59.505 55.987  60.734  1.00 25.07 ? 253  GLY   A C     1 
ATOM   1676  O  O     . GLY   A  1 255  ? -60.555 55.409  61.021  1.00 26.58 ? 253  GLY   A O     1 
ATOM   1677  N  N     . ARG   A  1 256  ? -58.307 55.422  60.918  1.00 22.55 ? 254  ARG   A N     1 
ATOM   1678  C  CA    . ARG   A  1 256  ? -58.210 54.094  61.514  1.00 21.72 ? 254  ARG   A CA    1 
ATOM   1679  C  C     . ARG   A  1 256  ? -58.573 54.075  62.993  1.00 25.11 ? 254  ARG   A C     1 
ATOM   1680  O  O     . ARG   A  1 256  ? -58.771 52.986  63.550  1.00 24.37 ? 254  ARG   A O     1 
ATOM   1681  C  CB    . ARG   A  1 256  ? -56.803 53.531  61.329  1.00 20.38 ? 254  ARG   A CB    1 
ATOM   1682  C  CG    . ARG   A  1 256  ? -56.613 52.785  60.014  1.00 23.25 ? 254  ARG   A CG    1 
ATOM   1683  C  CD    . ARG   A  1 256  ? -55.194 52.297  59.843  1.00 24.39 ? 254  ARG   A CD    1 
ATOM   1684  N  NE    . ARG   A  1 256  ? -54.301 53.407  59.545  1.00 26.73 ? 254  ARG   A NE    1 
ATOM   1685  C  CZ    . ARG   A  1 256  ? -52.979 53.313  59.501  1.00 29.79 ? 254  ARG   A CZ    1 
ATOM   1686  N  NH1   . ARG   A  1 256  ? -52.354 52.187  59.812  1.00 29.83 ? 254  ARG   A NH1   1 
ATOM   1687  N  NH2   . ARG   A  1 256  ? -52.268 54.371  59.121  1.00 26.66 ? 254  ARG   A NH2   1 
ATOM   1688  N  N     . GLY   A  1 257  ? -58.646 55.230  63.642  1.00 22.96 ? 255  GLY   A N     1 
ATOM   1689  C  CA    . GLY   A  1 257  ? -59.061 55.287  65.029  1.00 23.17 ? 255  GLY   A CA    1 
ATOM   1690  C  C     . GLY   A  1 257  ? -57.924 54.997  65.988  1.00 21.15 ? 255  GLY   A C     1 
ATOM   1691  O  O     . GLY   A  1 257  ? -56.773 54.784  65.604  1.00 24.78 ? 255  GLY   A O     1 
ATOM   1692  N  N     . ILE   A  1 258  ? -58.261 54.988  67.280  1.00 22.35 ? 256  ILE   A N     1 
ATOM   1693  C  CA    . ILE   A  1 258  ? -57.207 55.028  68.289  1.00 20.88 ? 256  ILE   A CA    1 
ATOM   1694  C  C     . ILE   A  1 258  ? -56.585 53.668  68.564  1.00 20.43 ? 256  ILE   A C     1 
ATOM   1695  O  O     . ILE   A  1 258  ? -55.475 53.606  69.101  1.00 21.26 ? 256  ILE   A O     1 
ATOM   1696  C  CB    . ILE   A  1 258  ? -57.726 55.632  69.600  1.00 21.12 ? 256  ILE   A CB    1 
ATOM   1697  C  CG1   . ILE   A  1 258  ? -58.865 54.777  70.169  1.00 21.69 ? 256  ILE   A CG1   1 
ATOM   1698  C  CG2   . ILE   A  1 258  ? -58.148 57.096  69.379  1.00 17.61 ? 256  ILE   A CG2   1 
ATOM   1699  C  CD1   . ILE   A  1 258  ? -59.457 55.329  71.457  1.00 24.46 ? 256  ILE   A CD1   1 
ATOM   1700  N  N     . TYR   A  1 259  ? -57.246 52.571  68.207  1.00 20.10 ? 257  TYR   A N     1 
ATOM   1701  C  CA    . TYR   A  1 259  ? -56.700 51.257  68.513  1.00 20.22 ? 257  TYR   A CA    1 
ATOM   1702  C  C     . TYR   A  1 259  ? -55.956 50.665  67.331  1.00 21.65 ? 257  TYR   A C     1 
ATOM   1703  O  O     . TYR   A  1 259  ? -54.809 50.234  67.476  1.00 26.54 ? 257  TYR   A O     1 
ATOM   1704  C  CB    . TYR   A  1 259  ? -57.814 50.311  68.976  1.00 24.00 ? 257  TYR   A CB    1 
ATOM   1705  C  CG    . TYR   A  1 259  ? -58.645 50.886  70.104  1.00 21.21 ? 257  TYR   A CG    1 
ATOM   1706  C  CD1   . TYR   A  1 259  ? -58.069 51.182  71.339  1.00 21.03 ? 257  TYR   A CD1   1 
ATOM   1707  C  CD2   . TYR   A  1 259  ? -59.999 51.159  69.928  1.00 25.89 ? 257  TYR   A CD2   1 
ATOM   1708  C  CE1   . TYR   A  1 259  ? -58.820 51.712  72.364  1.00 22.43 ? 257  TYR   A CE1   1 
ATOM   1709  C  CE2   . TYR   A  1 259  ? -60.764 51.692  70.957  1.00 23.46 ? 257  TYR   A CE2   1 
ATOM   1710  C  CZ    . TYR   A  1 259  ? -60.169 51.967  72.166  1.00 20.09 ? 257  TYR   A CZ    1 
ATOM   1711  O  OH    . TYR   A  1 259  ? -60.906 52.506  73.191  1.00 22.55 ? 257  TYR   A OH    1 
ATOM   1712  N  N     . GLU   A  1 260  ? -56.574 50.675  66.145  1.00 23.30 ? 258  GLU   A N     1 
ATOM   1713  C  CA    . GLU   A  1 260  ? -55.911 50.143  64.962  1.00 25.12 ? 258  GLU   A CA    1 
ATOM   1714  C  C     . GLU   A  1 260  ? -54.907 51.125  64.372  1.00 26.36 ? 258  GLU   A C     1 
ATOM   1715  O  O     . GLU   A  1 260  ? -53.916 50.702  63.767  1.00 29.65 ? 258  GLU   A O     1 
ATOM   1716  C  CB    . GLU   A  1 260  ? -56.948 49.767  63.898  1.00 28.18 ? 258  GLU   A CB    1 
ATOM   1717  N  N     . GLY   A  1 261  ? -55.133 52.425  64.541  1.00 22.84 ? 259  GLY   A N     1 
ATOM   1718  C  CA    . GLY   A  1 261  ? -54.285 53.425  63.937  1.00 18.26 ? 259  GLY   A CA    1 
ATOM   1719  C  C     . GLY   A  1 261  ? -53.198 53.911  64.875  1.00 22.77 ? 259  GLY   A C     1 
ATOM   1720  O  O     . GLY   A  1 261  ? -53.213 53.650  66.083  1.00 22.06 ? 259  GLY   A O     1 
ATOM   1721  N  N     . PRO   A  1 262  ? -52.240 54.647  64.323  1.00 19.84 ? 260  PRO   A N     1 
ATOM   1722  C  CA    . PRO   A  1 262  ? -51.082 55.077  65.105  1.00 17.58 ? 260  PRO   A CA    1 
ATOM   1723  C  C     . PRO   A  1 262  ? -51.437 56.221  66.041  1.00 19.74 ? 260  PRO   A C     1 
ATOM   1724  O  O     . PRO   A  1 262  ? -52.443 56.917  65.874  1.00 19.53 ? 260  PRO   A O     1 
ATOM   1725  C  CB    . PRO   A  1 262  ? -50.086 55.533  64.032  1.00 18.45 ? 260  PRO   A CB    1 
ATOM   1726  C  CG    . PRO   A  1 262  ? -50.983 56.013  62.914  1.00 21.13 ? 260  PRO   A CG    1 
ATOM   1727  C  CD    . PRO   A  1 262  ? -52.151 55.071  62.916  1.00 22.75 ? 260  PRO   A CD    1 
ATOM   1728  N  N     . GLY   A  1 263  ? -50.597 56.377  67.063  1.00 18.16 ? 261  GLY   A N     1 
ATOM   1729  C  CA    . GLY   A  1 263  ? -50.747 57.462  68.009  1.00 17.66 ? 261  GLY   A CA    1 
ATOM   1730  C  C     . GLY   A  1 263  ? -49.423 58.154  68.271  1.00 18.31 ? 261  GLY   A C     1 
ATOM   1731  O  O     . GLY   A  1 263  ? -48.423 57.860  67.606  1.00 16.74 ? 261  GLY   A O     1 
ATOM   1732  N  N     . ILE   A  1 264  ? -49.412 59.067  69.242  1.00 17.49 ? 262  ILE   A N     1 
ATOM   1733  C  CA    . ILE   A  1 264  ? -48.228 59.837  69.596  1.00 16.87 ? 262  ILE   A CA    1 
ATOM   1734  C  C     . ILE   A  1 264  ? -48.038 59.726  71.101  1.00 18.53 ? 262  ILE   A C     1 
ATOM   1735  O  O     . ILE   A  1 264  ? -48.994 59.505  71.851  1.00 16.17 ? 262  ILE   A O     1 
ATOM   1736  C  CB    . ILE   A  1 264  ? -48.334 61.318  69.135  1.00 16.74 ? 262  ILE   A CB    1 
ATOM   1737  C  CG1   . ILE   A  1 264  ? -46.959 61.995  69.188  1.00 17.32 ? 262  ILE   A CG1   1 
ATOM   1738  C  CG2   . ILE   A  1 264  ? -49.380 62.099  69.938  1.00 16.24 ? 262  ILE   A CG2   1 
ATOM   1739  C  CD1   . ILE   A  1 264  ? -46.946 63.440  68.651  1.00 20.33 ? 262  ILE   A CD1   1 
ATOM   1740  N  N     . SER   A  1 265  ? -46.784 59.807  71.534  1.00 16.01 ? 263  SER   A N     1 
ATOM   1741  C  CA    . SER   A  1 265  ? -46.439 59.856  72.946  1.00 15.85 ? 263  SER   A CA    1 
ATOM   1742  C  C     . SER   A  1 265  ? -45.693 61.151  73.210  1.00 17.66 ? 263  SER   A C     1 
ATOM   1743  O  O     . SER   A  1 265  ? -44.818 61.531  72.431  1.00 20.99 ? 263  SER   A O     1 
ATOM   1744  C  CB    . SER   A  1 265  ? -45.576 58.665  73.355  1.00 17.83 ? 263  SER   A CB    1 
ATOM   1745  O  OG    . SER   A  1 265  ? -46.328 57.461  73.329  1.00 20.94 ? 263  SER   A OG    1 
ATOM   1746  N  N     . ILE   A  1 266  ? -46.039 61.825  74.308  1.00 17.60 ? 264  ILE   A N     1 
ATOM   1747  C  CA    . ILE   A  1 266  ? -45.415 63.093  74.659  1.00 16.09 ? 264  ILE   A CA    1 
ATOM   1748  C  C     . ILE   A  1 266  ? -44.881 63.005  76.080  1.00 18.35 ? 264  ILE   A C     1 
ATOM   1749  O  O     . ILE   A  1 266  ? -45.313 62.183  76.890  1.00 15.88 ? 264  ILE   A O     1 
ATOM   1750  C  CB    . ILE   A  1 266  ? -46.383 64.289  74.533  1.00 17.50 ? 264  ILE   A CB    1 
ATOM   1751  C  CG1   . ILE   A  1 266  ? -47.532 64.155  75.537  1.00 16.56 ? 264  ILE   A CG1   1 
ATOM   1752  C  CG2   . ILE   A  1 266  ? -46.934 64.397  73.115  1.00 17.70 ? 264  ILE   A CG2   1 
ATOM   1753  C  CD1   . ILE   A  1 266  ? -48.377 65.420  75.671  1.00 20.03 ? 264  ILE   A CD1   1 
ATOM   1754  N  N     . LYS   A  1 267  ? -43.912 63.864  76.368  1.00 16.02 ? 265  LYS   A N     1 
ATOM   1755  C  CA    . LYS   A  1 267  ? -43.378 64.020  77.705  1.00 17.34 ? 265  LYS   A CA    1 
ATOM   1756  C  C     . LYS   A  1 267  ? -43.698 65.428  78.182  1.00 17.71 ? 265  LYS   A C     1 
ATOM   1757  O  O     . LYS   A  1 267  ? -43.411 66.411  77.488  1.00 16.63 ? 265  LYS   A O     1 
ATOM   1758  C  CB    . LYS   A  1 267  ? -41.873 63.751  77.732  1.00 19.07 ? 265  LYS   A CB    1 
ATOM   1759  C  CG    . LYS   A  1 267  ? -41.540 62.267  77.638  1.00 21.96 ? 265  LYS   A CG    1 
ATOM   1760  C  CD    . LYS   A  1 267  ? -40.041 62.042  77.648  1.00 25.09 ? 265  LYS   A CD    1 
ATOM   1761  C  CE    . LYS   A  1 267  ? -39.712 60.553  77.694  1.00 31.07 ? 265  LYS   A CE    1 
ATOM   1762  N  NZ    . LYS   A  1 267  ? -40.216 59.841  76.487  1.00 28.83 ? 265  LYS   A NZ    1 
ATOM   1763  N  N     . LEU   A  1 268  ? -44.338 65.518  79.341  1.00 15.54 ? 266  LEU   A N     1 
ATOM   1764  C  CA    . LEU   A  1 268  ? -44.714 66.831  79.845  1.00 15.61 ? 266  LEU   A CA    1 
ATOM   1765  C  C     . LEU   A  1 268  ? -43.490 67.699  80.097  1.00 17.70 ? 266  LEU   A C     1 
ATOM   1766  O  O     . LEU   A  1 268  ? -43.555 68.923  79.934  1.00 16.70 ? 266  LEU   A O     1 
ATOM   1767  C  CB    . LEU   A  1 268  ? -45.535 66.691  81.122  1.00 16.44 ? 266  LEU   A CB    1 
ATOM   1768  C  CG    . LEU   A  1 268  ? -46.866 65.961  80.933  1.00 19.09 ? 266  LEU   A CG    1 
ATOM   1769  C  CD1   . LEU   A  1 268  ? -47.617 65.859  82.242  1.00 22.07 ? 266  LEU   A CD1   1 
ATOM   1770  C  CD2   . LEU   A  1 268  ? -47.712 66.691  79.875  1.00 18.29 ? 266  LEU   A CD2   1 
ATOM   1771  N  N     . SER   A  1 269  ? -42.372 67.089  80.493  1.00 16.97 ? 267  SER   A N     1 
ATOM   1772  C  CA    . SER   A  1 269  ? -41.159 67.863  80.728  1.00 16.45 ? 267  SER   A CA    1 
ATOM   1773  C  C     . SER   A  1 269  ? -40.640 68.522  79.456  1.00 17.80 ? 267  SER   A C     1 
ATOM   1774  O  O     . SER   A  1 269  ? -39.843 69.459  79.544  1.00 17.36 ? 267  SER   A O     1 
ATOM   1775  C  CB    . SER   A  1 269  ? -40.067 66.976  81.314  1.00 19.45 ? 267  SER   A CB    1 
ATOM   1776  O  OG    . SER   A  1 269  ? -39.515 66.163  80.300  1.00 18.25 ? 267  SER   A OG    1 
ATOM   1777  N  N     . ALA   A  1 270  ? -41.051 68.040  78.277  1.00 15.47 ? 268  ALA   A N     1 
ATOM   1778  C  CA    . ALA   A  1 270  ? -40.650 68.678  77.026  1.00 17.14 ? 268  ALA   A CA    1 
ATOM   1779  C  C     . ALA   A  1 270  ? -41.404 69.975  76.769  1.00 16.66 ? 268  ALA   A C     1 
ATOM   1780  O  O     . ALA   A  1 270  ? -40.951 70.803  75.973  1.00 17.27 ? 268  ALA   A O     1 
ATOM   1781  C  CB    . ALA   A  1 270  ? -40.886 67.724  75.843  1.00 17.32 ? 268  ALA   A CB    1 
ATOM   1782  N  N     . LEU   A  1 271  ? -42.539 70.171  77.425  1.00 17.18 ? 269  LEU   A N     1 
ATOM   1783  C  CA    . LEU   A  1 271  ? -43.466 71.221  77.052  1.00 16.36 ? 269  LEU   A CA    1 
ATOM   1784  C  C     . LEU   A  1 271  ? -43.425 72.412  77.990  1.00 16.16 ? 269  LEU   A C     1 
ATOM   1785  O  O     . LEU   A  1 271  ? -44.131 73.394  77.753  1.00 17.05 ? 269  LEU   A O     1 
ATOM   1786  C  CB    . LEU   A  1 271  ? -44.878 70.653  76.998  1.00 17.43 ? 269  LEU   A CB    1 
ATOM   1787  C  CG    . LEU   A  1 271  ? -45.071 69.653  75.856  1.00 18.36 ? 269  LEU   A CG    1 
ATOM   1788  C  CD1   . LEU   A  1 271  ? -46.457 69.033  75.930  1.00 21.60 ? 269  LEU   A CD1   1 
ATOM   1789  C  CD2   . LEU   A  1 271  ? -44.858 70.378  74.533  1.00 19.01 ? 269  LEU   A CD2   1 
ATOM   1790  N  N     . HIS   A  1 272  ? -42.621 72.349  79.041  1.00 16.14 ? 270  HIS   A N     1 
ATOM   1791  C  CA    . HIS   A  1 272  ? -42.481 73.487  79.896  1.00 16.08 ? 270  HIS   A CA    1 
ATOM   1792  C  C     . HIS   A  1 272  ? -41.122 73.362  80.570  1.00 17.61 ? 270  HIS   A C     1 
ATOM   1793  O  O     . HIS   A  1 272  ? -40.775 72.265  81.026  1.00 17.08 ? 270  HIS   A O     1 
ATOM   1794  C  CB    . HIS   A  1 272  ? -43.597 73.549  80.939  1.00 16.93 ? 270  HIS   A CB    1 
ATOM   1795  C  CG    . HIS   A  1 272  ? -43.731 74.899  81.556  1.00 21.46 ? 270  HIS   A CG    1 
ATOM   1796  N  ND1   . HIS   A  1 272  ? -42.848 75.371  82.502  1.00 24.08 ? 270  HIS   A ND1   1 
ATOM   1797  C  CD2   . HIS   A  1 272  ? -44.603 75.908  81.315  1.00 23.05 ? 270  HIS   A CD2   1 
ATOM   1798  C  CE1   . HIS   A  1 272  ? -43.190 76.603  82.842  1.00 24.55 ? 270  HIS   A CE1   1 
ATOM   1799  N  NE2   . HIS   A  1 272  ? -44.244 76.956  82.128  1.00 23.36 ? 270  HIS   A NE2   1 
ATOM   1800  N  N     . PRO   A  1 273  ? -40.331 74.437  80.647  1.00 18.91 ? 271  PRO   A N     1 
ATOM   1801  C  CA    . PRO   A  1 273  ? -39.008 74.323  81.279  1.00 16.40 ? 271  PRO   A CA    1 
ATOM   1802  C  C     . PRO   A  1 273  ? -39.044 74.245  82.789  1.00 19.43 ? 271  PRO   A C     1 
ATOM   1803  O  O     . PRO   A  1 273  ? -37.999 73.975  83.391  1.00 19.81 ? 271  PRO   A O     1 
ATOM   1804  C  CB    . PRO   A  1 273  ? -38.295 75.605  80.834  1.00 18.31 ? 271  PRO   A CB    1 
ATOM   1805  C  CG    . PRO   A  1 273  ? -39.404 76.588  80.670  1.00 18.82 ? 271  PRO   A CG    1 
ATOM   1806  C  CD    . PRO   A  1 273  ? -40.578 75.787  80.117  1.00 17.95 ? 271  PRO   A CD    1 
ATOM   1807  N  N     . ARG   A  1 274  ? -40.187 74.505  83.419  1.00 17.31 ? 272  ARG   A N     1 
ATOM   1808  C  CA    . ARG   A  1 274  ? -40.286 74.413  84.872  1.00 17.40 ? 272  ARG   A CA    1 
ATOM   1809  C  C     . ARG   A  1 274  ? -41.410 73.467  85.259  1.00 20.33 ? 272  ARG   A C     1 
ATOM   1810  O  O     . ARG   A  1 274  ? -42.341 73.851  85.975  1.00 19.31 ? 272  ARG   A O     1 
ATOM   1811  C  CB    . ARG   A  1 274  ? -40.523 75.791  85.491  1.00 17.53 ? 272  ARG   A CB    1 
ATOM   1812  C  CG    . ARG   A  1 274  ? -39.392 76.795  85.219  1.00 17.45 ? 272  ARG   A CG    1 
ATOM   1813  C  CD    . ARG   A  1 274  ? -38.037 76.264  85.710  1.00 20.55 ? 272  ARG   A CD    1 
ATOM   1814  N  NE    . ARG   A  1 274  ? -38.102 75.828  87.106  1.00 21.51 ? 272  ARG   A NE    1 
ATOM   1815  C  CZ    . ARG   A  1 274  ? -38.025 76.652  88.142  1.00 19.68 ? 272  ARG   A CZ    1 
ATOM   1816  N  NH1   . ARG   A  1 274  ? -37.932 77.962  87.975  1.00 21.48 ? 272  ARG   A NH1   1 
ATOM   1817  N  NH2   . ARG   A  1 274  ? -38.060 76.150  89.377  1.00 21.13 ? 272  ARG   A NH2   1 
ATOM   1818  N  N     . TYR   A  1 275  ? -41.332 72.233  84.783  1.00 17.21 ? 273  TYR   A N     1 
ATOM   1819  C  CA    . TYR   A  1 275  ? -42.360 71.232  85.064  1.00 15.14 ? 273  TYR   A CA    1 
ATOM   1820  C  C     . TYR   A  1 275  ? -42.019 70.576  86.398  1.00 16.32 ? 273  TYR   A C     1 
ATOM   1821  O  O     . TYR   A  1 275  ? -41.260 69.614  86.459  1.00 18.05 ? 273  TYR   A O     1 
ATOM   1822  C  CB    . TYR   A  1 275  ? -42.425 70.220  83.922  1.00 18.09 ? 273  TYR   A CB    1 
ATOM   1823  C  CG    . TYR   A  1 275  ? -43.350 69.063  84.217  1.00 15.55 ? 273  TYR   A CG    1 
ATOM   1824  C  CD1   . TYR   A  1 275  ? -44.626 69.288  84.700  1.00 16.30 ? 273  TYR   A CD1   1 
ATOM   1825  C  CD2   . TYR   A  1 275  ? -42.939 67.753  84.010  1.00 15.22 ? 273  TYR   A CD2   1 
ATOM   1826  C  CE1   . TYR   A  1 275  ? -45.482 68.234  84.975  1.00 18.86 ? 273  TYR   A CE1   1 
ATOM   1827  C  CE2   . TYR   A  1 275  ? -43.784 66.689  84.293  1.00 15.85 ? 273  TYR   A CE2   1 
ATOM   1828  C  CZ    . TYR   A  1 275  ? -45.047 66.939  84.770  1.00 17.98 ? 273  TYR   A CZ    1 
ATOM   1829  O  OH    . TYR   A  1 275  ? -45.884 65.885  85.054  1.00 18.91 ? 273  TYR   A OH    1 
ATOM   1830  N  N     . SER   A  1 276  ? -42.588 71.103  87.485  1.00 16.78 ? 274  SER   A N     1 
ATOM   1831  C  CA    . SER   A  1 276  ? -42.333 70.551  88.812  1.00 16.87 ? 274  SER   A CA    1 
ATOM   1832  C  C     . SER   A  1 276  ? -43.463 70.958  89.742  1.00 19.28 ? 274  SER   A C     1 
ATOM   1833  O  O     . SER   A  1 276  ? -44.209 71.908  89.469  1.00 15.43 ? 274  SER   A O     1 
ATOM   1834  C  CB    . SER   A  1 276  ? -40.996 71.032  89.382  1.00 20.64 ? 274  SER   A CB    1 
ATOM   1835  O  OG    . SER   A  1 276  ? -41.092 72.411  89.656  1.00 21.13 ? 274  SER   A OG    1 
ATOM   1836  N  N     . ARG   A  1 277  ? -43.583 70.209  90.846  1.00 17.40 ? 275  ARG   A N     1 
ATOM   1837  C  CA    . ARG   A  1 277  ? -44.564 70.549  91.873  1.00 18.37 ? 275  ARG   A CA    1 
ATOM   1838  C  C     . ARG   A  1 277  ? -44.341 71.956  92.408  1.00 17.77 ? 275  ARG   A C     1 
ATOM   1839  O  O     . ARG   A  1 277  ? -45.302 72.681  92.687  1.00 17.06 ? 275  ARG   A O     1 
ATOM   1840  C  CB    . ARG   A  1 277  ? -44.501 69.537  93.017  1.00 15.30 ? 275  ARG   A CB    1 
ATOM   1841  C  CG    . ARG   A  1 277  ? -45.395 69.871  94.218  1.00 16.46 ? 275  ARG   A CG    1 
ATOM   1842  C  CD    . ARG   A  1 277  ? -46.875 70.066  93.813  1.00 17.17 ? 275  ARG   A CD    1 
ATOM   1843  N  NE    . ARG   A  1 277  ? -47.731 70.375  94.958  1.00 17.64 ? 275  ARG   A NE    1 
ATOM   1844  C  CZ    . ARG   A  1 277  ? -47.930 71.599  95.438  1.00 19.04 ? 275  ARG   A CZ    1 
ATOM   1845  N  NH1   . ARG   A  1 277  ? -47.321 72.655  94.917  1.00 16.96 ? 275  ARG   A NH1   1 
ATOM   1846  N  NH2   . ARG   A  1 277  ? -48.764 71.771  96.467  1.00 17.38 ? 275  ARG   A NH2   1 
ATOM   1847  N  N     . ALA   A  1 278  ? -43.080 72.348  92.599  1.00 18.20 ? 276  ALA   A N     1 
ATOM   1848  C  CA    . ALA   A  1 278  ? -42.821 73.678  93.145  1.00 19.33 ? 276  ALA   A CA    1 
ATOM   1849  C  C     . ALA   A  1 278  ? -43.380 74.760  92.239  1.00 17.09 ? 276  ALA   A C     1 
ATOM   1850  O  O     . ALA   A  1 278  ? -43.736 75.843  92.709  1.00 20.30 ? 276  ALA   A O     1 
ATOM   1851  C  CB    . ALA   A  1 278  ? -41.318 73.895  93.348  1.00 19.64 ? 276  ALA   A CB    1 
ATOM   1852  N  N     . GLN   A  1 279  ? -43.470 74.484  90.939  1.00 17.62 ? 277  GLN   A N     1 
ATOM   1853  C  CA    . GLN   A  1 279  ? -43.976 75.433  89.955  1.00 15.88 ? 277  GLN   A CA    1 
ATOM   1854  C  C     . GLN   A  1 279  ? -45.375 75.050  89.483  1.00 21.01 ? 277  GLN   A C     1 
ATOM   1855  O  O     . GLN   A  1 279  ? -45.726 75.265  88.319  1.00 16.94 ? 277  GLN   A O     1 
ATOM   1856  C  CB    . GLN   A  1 279  ? -43.008 75.512  88.776  1.00 18.76 ? 277  GLN   A CB    1 
ATOM   1857  C  CG    . GLN   A  1 279  ? -41.606 75.906  89.217  1.00 16.10 ? 277  GLN   A CG    1 
ATOM   1858  C  CD    . GLN   A  1 279  ? -41.570 77.347  89.685  1.00 21.83 ? 277  GLN   A CD    1 
ATOM   1859  O  OE1   . GLN   A  1 279  ? -42.121 78.221  89.026  1.00 26.22 ? 277  GLN   A OE1   1 
ATOM   1860  N  NE2   . GLN   A  1 279  ? -40.951 77.598  90.832  1.00 17.97 ? 277  GLN   A NE2   1 
ATOM   1861  N  N     . ALA   A  1 280  ? -46.185 74.487  90.387  1.00 17.52 ? 278  ALA   A N     1 
ATOM   1862  C  CA    . ALA   A  1 280  ? -47.444 73.882  89.965  1.00 18.77 ? 278  ALA   A CA    1 
ATOM   1863  C  C     . ALA   A  1 280  ? -48.371 74.912  89.339  1.00 17.95 ? 278  ALA   A C     1 
ATOM   1864  O  O     . ALA   A  1 280  ? -49.094 74.600  88.386  1.00 17.05 ? 278  ALA   A O     1 
ATOM   1865  C  CB    . ALA   A  1 280  ? -48.121 73.194  91.147  1.00 17.68 ? 278  ALA   A CB    1 
ATOM   1866  N  N     . ALA   A  1 281  ? -48.355 76.147  89.852  1.00 16.73 ? 279  ALA   A N     1 
ATOM   1867  C  CA    . ALA   A  1 281  ? -49.217 77.185  89.288  1.00 19.94 ? 279  ALA   A CA    1 
ATOM   1868  C  C     . ALA   A  1 281  ? -48.847 77.475  87.842  1.00 21.92 ? 279  ALA   A C     1 
ATOM   1869  O  O     . ALA   A  1 281  ? -49.729 77.628  86.986  1.00 18.00 ? 279  ALA   A O     1 
ATOM   1870  C  CB    . ALA   A  1 281  ? -49.137 78.466  90.121  1.00 22.20 ? 279  ALA   A CB    1 
ATOM   1871  N  N     . ARG   A  1 282  ? -47.545 77.572  87.548  1.00 16.75 ? 280  ARG   A N     1 
ATOM   1872  C  CA    . ARG   A  1 282  ? -47.149 77.781  86.158  1.00 18.83 ? 280  ARG   A CA    1 
ATOM   1873  C  C     . ARG   A  1 282  ? -47.461 76.561  85.310  1.00 21.13 ? 280  ARG   A C     1 
ATOM   1874  O  O     . ARG   A  1 282  ? -47.784 76.692  84.124  1.00 19.65 ? 280  ARG   A O     1 
ATOM   1875  C  CB    . ARG   A  1 282  ? -45.655 78.110  86.061  1.00 20.55 ? 280  ARG   A CB    1 
ATOM   1876  C  CG    . ARG   A  1 282  ? -45.256 79.437  86.694  1.00 22.32 ? 280  ARG   A CG    1 
ATOM   1877  C  CD    . ARG   A  1 282  ? -43.822 79.751  86.303  1.00 20.83 ? 280  ARG   A CD    1 
ATOM   1878  N  NE    . ARG   A  1 282  ? -43.726 79.823  84.851  1.00 19.91 ? 280  ARG   A NE    1 
ATOM   1879  C  CZ    . ARG   A  1 282  ? -42.597 79.868  84.158  1.00 23.28 ? 280  ARG   A CZ    1 
ATOM   1880  N  NH1   . ARG   A  1 282  ? -41.412 79.857  84.758  1.00 17.31 ? 280  ARG   A NH1   1 
ATOM   1881  N  NH2   . ARG   A  1 282  ? -42.658 79.914  82.827  1.00 19.49 ? 280  ARG   A NH2   1 
ATOM   1882  N  N     . VAL   A  1 283  ? -47.345 75.369  85.891  1.00 17.60 ? 281  VAL   A N     1 
ATOM   1883  C  CA    . VAL   A  1 283  ? -47.641 74.150  85.145  1.00 15.47 ? 281  VAL   A CA    1 
ATOM   1884  C  C     . VAL   A  1 283  ? -49.109 74.125  84.737  1.00 16.48 ? 281  VAL   A C     1 
ATOM   1885  O  O     . VAL   A  1 283  ? -49.441 73.902  83.570  1.00 16.41 ? 281  VAL   A O     1 
ATOM   1886  C  CB    . VAL   A  1 283  ? -47.261 72.911  85.972  1.00 15.41 ? 281  VAL   A CB    1 
ATOM   1887  C  CG1   . VAL   A  1 283  ? -47.906 71.646  85.376  1.00 16.16 ? 281  VAL   A CG1   1 
ATOM   1888  C  CG2   . VAL   A  1 283  ? -45.747 72.771  86.039  1.00 16.32 ? 281  VAL   A CG2   1 
ATOM   1889  N  N     . MET   A  1 284  ? -50.007 74.401  85.685  1.00 16.23 ? 282  MET   A N     1 
ATOM   1890  C  CA    . MET   A  1 284  ? -51.432 74.400  85.359  1.00 19.58 ? 282  MET   A CA    1 
ATOM   1891  C  C     . MET   A  1 284  ? -51.807 75.558  84.442  1.00 20.62 ? 282  MET   A C     1 
ATOM   1892  O  O     . MET   A  1 284  ? -52.695 75.414  83.593  1.00 19.19 ? 282  MET   A O     1 
ATOM   1893  C  CB    . MET   A  1 284  ? -52.257 74.449  86.645  1.00 18.23 ? 282  MET   A CB    1 
ATOM   1894  C  CG    . MET   A  1 284  ? -51.983 73.291  87.589  1.00 18.27 ? 282  MET   A CG    1 
ATOM   1895  S  SD    . MET   A  1 284  ? -52.180 71.678  86.794  1.00 22.50 ? 282  MET   A SD    1 
ATOM   1896  C  CE    . MET   A  1 284  ? -53.958 71.582  86.586  1.00 19.51 ? 282  MET   A CE    1 
ATOM   1897  N  N     . GLY   A  1 285  ? -51.148 76.708  84.602  1.00 17.71 ? 283  GLY   A N     1 
ATOM   1898  C  CA    . GLY   A  1 285  ? -51.485 77.874  83.809  1.00 19.50 ? 283  GLY   A CA    1 
ATOM   1899  C  C     . GLY   A  1 285  ? -50.868 77.885  82.430  1.00 19.68 ? 283  GLY   A C     1 
ATOM   1900  O  O     . GLY   A  1 285  ? -51.439 78.461  81.503  1.00 18.56 ? 283  GLY   A O     1 
ATOM   1901  N  N     . GLU   A  1 286  ? -49.712 77.248  82.257  1.00 16.69 ? 284  GLU   A N     1 
ATOM   1902  C  CA    . GLU   A  1 286  ? -48.981 77.394  81.005  1.00 17.69 ? 284  GLU   A CA    1 
ATOM   1903  C  C     . GLU   A  1 286  ? -48.749 76.082  80.282  1.00 22.10 ? 284  GLU   A C     1 
ATOM   1904  O  O     . GLU   A  1 286  ? -48.810 76.043  79.048  1.00 21.44 ? 284  GLU   A O     1 
ATOM   1905  C  CB    . GLU   A  1 286  ? -47.625 78.069  81.266  1.00 20.38 ? 284  GLU   A CB    1 
ATOM   1906  C  CG    . GLU   A  1 286  ? -47.738 79.363  82.061  1.00 21.84 ? 284  GLU   A CG    1 
ATOM   1907  C  CD    . GLU   A  1 286  ? -46.394 79.853  82.553  1.00 25.32 ? 284  GLU   A CD    1 
ATOM   1908  O  OE1   . GLU   A  1 286  ? -45.359 79.370  82.048  1.00 24.99 ? 284  GLU   A OE1   1 
ATOM   1909  O  OE2   . GLU   A  1 286  ? -46.378 80.704  83.459  1.00 23.56 ? 284  GLU   A OE2   1 
ATOM   1910  N  N     . LEU   A  1 287  ? -48.439 75.017  81.018  1.00 17.76 ? 285  LEU   A N     1 
ATOM   1911  C  CA    . LEU   A  1 287  ? -48.232 73.707  80.417  1.00 18.79 ? 285  LEU   A CA    1 
ATOM   1912  C  C     . LEU   A  1 287  ? -49.562 73.063  80.027  1.00 19.55 ? 285  LEU   A C     1 
ATOM   1913  O  O     . LEU   A  1 287  ? -49.720 72.580  78.903  1.00 18.72 ? 285  LEU   A O     1 
ATOM   1914  C  CB    . LEU   A  1 287  ? -47.444 72.825  81.392  1.00 17.49 ? 285  LEU   A CB    1 
ATOM   1915  C  CG    . LEU   A  1 287  ? -47.176 71.343  81.106  1.00 25.25 ? 285  LEU   A CG    1 
ATOM   1916  C  CD1   . LEU   A  1 287  ? -46.945 71.094  79.666  1.00 26.78 ? 285  LEU   A CD1   1 
ATOM   1917  C  CD2   . LEU   A  1 287  ? -45.969 70.848  81.908  1.00 21.56 ? 285  LEU   A CD2   1 
ATOM   1918  N  N     . LEU   A  1 288  ? -50.526 73.048  80.944  1.00 17.68 ? 286  LEU   A N     1 
ATOM   1919  C  CA    . LEU   A  1 288  ? -51.814 72.413  80.667  1.00 20.02 ? 286  LEU   A CA    1 
ATOM   1920  C  C     . LEU   A  1 288  ? -52.480 72.919  79.391  1.00 17.49 ? 286  LEU   A C     1 
ATOM   1921  O  O     . LEU   A  1 288  ? -52.924 72.083  78.587  1.00 18.24 ? 286  LEU   A O     1 
ATOM   1922  C  CB    . LEU   A  1 288  ? -52.727 72.584  81.889  1.00 18.00 ? 286  LEU   A CB    1 
ATOM   1923  C  CG    . LEU   A  1 288  ? -54.187 72.127  81.772  1.00 22.87 ? 286  LEU   A CG    1 
ATOM   1924  C  CD1   . LEU   A  1 288  ? -54.266 70.645  81.455  1.00 20.72 ? 286  LEU   A CD1   1 
ATOM   1925  C  CD2   . LEU   A  1 288  ? -54.916 72.448  83.068  1.00 26.66 ? 286  LEU   A CD2   1 
ATOM   1926  N  N     . PRO   A  1 289  ? -52.561 74.226  79.120  1.00 18.56 ? 287  PRO   A N     1 
ATOM   1927  C  CA    . PRO   A  1 289  ? -53.166 74.650  77.847  1.00 21.75 ? 287  PRO   A CA    1 
ATOM   1928  C  C     . PRO   A  1 289  ? -52.444 74.097  76.642  1.00 16.14 ? 287  PRO   A C     1 
ATOM   1929  O  O     . PRO   A  1 289  ? -53.073 73.852  75.604  1.00 17.31 ? 287  PRO   A O     1 
ATOM   1930  C  CB    . PRO   A  1 289  ? -53.072 76.181  77.902  1.00 22.31 ? 287  PRO   A CB    1 
ATOM   1931  C  CG    . PRO   A  1 289  ? -52.984 76.510  79.342  1.00 24.76 ? 287  PRO   A CG    1 
ATOM   1932  C  CD    . PRO   A  1 289  ? -52.203 75.387  79.956  1.00 17.78 ? 287  PRO   A CD    1 
ATOM   1933  N  N     . ARG   A  1 290  ? -51.127 73.912  76.740  1.00 20.04 ? 288  ARG   A N     1 
ATOM   1934  C  CA    . ARG   A  1 290  ? -50.394 73.355  75.615  1.00 17.30 ? 288  ARG   A CA    1 
ATOM   1935  C  C     . ARG   A  1 290  ? -50.747 71.898  75.408  1.00 16.43 ? 288  ARG   A C     1 
ATOM   1936  O  O     . ARG   A  1 290  ? -50.921 71.462  74.267  1.00 16.53 ? 288  ARG   A O     1 
ATOM   1937  C  CB    . ARG   A  1 290  ? -48.891 73.514  75.829  1.00 20.88 ? 288  ARG   A CB    1 
ATOM   1938  C  CG    . ARG   A  1 290  ? -48.472 74.947  75.954  1.00 20.94 ? 288  ARG   A CG    1 
ATOM   1939  C  CD    . ARG   A  1 290  ? -46.975 75.076  76.213  1.00 21.39 ? 288  ARG   A CD    1 
ATOM   1940  N  NE    . ARG   A  1 290  ? -46.631 76.479  76.414  1.00 29.43 ? 288  ARG   A NE    1 
ATOM   1941  C  CZ    . ARG   A  1 290  ? -45.673 76.912  77.226  1.00 32.98 ? 288  ARG   A CZ    1 
ATOM   1942  N  NH1   . ARG   A  1 290  ? -44.908 76.072  77.908  1.00 26.23 ? 288  ARG   A NH1   1 
ATOM   1943  N  NH2   . ARG   A  1 290  ? -45.474 78.224  77.355  1.00 33.85 ? 288  ARG   A NH2   1 
ATOM   1944  N  N     . VAL   A  1 291  ? -50.845 71.121  76.493  1.00 16.76 ? 289  VAL   A N     1 
ATOM   1945  C  CA    . VAL   A  1 291  ? -51.260 69.731  76.335  1.00 17.35 ? 289  VAL   A CA    1 
ATOM   1946  C  C     . VAL   A  1 291  ? -52.672 69.667  75.775  1.00 17.91 ? 289  VAL   A C     1 
ATOM   1947  O  O     . VAL   A  1 291  ? -52.969 68.852  74.890  1.00 17.11 ? 289  VAL   A O     1 
ATOM   1948  C  CB    . VAL   A  1 291  ? -51.161 68.955  77.662  1.00 19.46 ? 289  VAL   A CB    1 
ATOM   1949  C  CG1   . VAL   A  1 291  ? -51.503 67.474  77.408  1.00 18.89 ? 289  VAL   A CG1   1 
ATOM   1950  C  CG2   . VAL   A  1 291  ? -49.781 69.098  78.263  1.00 19.78 ? 289  VAL   A CG2   1 
ATOM   1951  N  N     . LYS   A  1 292  ? -53.561 70.531  76.276  1.00 16.41 ? 290  LYS   A N     1 
ATOM   1952  C  CA    . LYS   A  1 292  ? -54.919 70.573  75.743  1.00 16.27 ? 290  LYS   A CA    1 
ATOM   1953  C  C     . LYS   A  1 292  ? -54.919 70.836  74.245  1.00 16.37 ? 290  LYS   A C     1 
ATOM   1954  O  O     . LYS   A  1 292  ? -55.657 70.187  73.500  1.00 16.48 ? 290  LYS   A O     1 
ATOM   1955  C  CB    . LYS   A  1 292  ? -55.744 71.633  76.464  1.00 16.39 ? 290  LYS   A CB    1 
ATOM   1956  C  CG    . LYS   A  1 292  ? -57.135 71.795  75.851  1.00 18.50 ? 290  LYS   A CG    1 
ATOM   1957  C  CD    . LYS   A  1 292  ? -57.983 72.790  76.614  1.00 19.24 ? 290  LYS   A CD    1 
ATOM   1958  C  CE    . LYS   A  1 292  ? -59.393 72.823  76.030  1.00 20.03 ? 290  LYS   A CE    1 
ATOM   1959  N  NZ    . LYS   A  1 292  ? -60.308 73.619  76.890  1.00 20.24 ? 290  LYS   A NZ    1 
ATOM   1960  N  N     . ALA   A  1 293  ? -54.095 71.781  73.779  1.00 16.35 ? 291  ALA   A N     1 
ATOM   1961  C  CA    . ALA   A  1 293  ? -54.079 72.093  72.353  1.00 16.47 ? 291  ALA   A CA    1 
ATOM   1962  C  C     . ALA   A  1 293  ? -53.639 70.887  71.536  1.00 16.44 ? 291  ALA   A C     1 
ATOM   1963  O  O     . ALA   A  1 293  ? -54.216 70.594  70.482  1.00 16.58 ? 291  ALA   A O     1 
ATOM   1964  C  CB    . ALA   A  1 293  ? -53.168 73.301  72.087  1.00 16.47 ? 291  ALA   A CB    1 
ATOM   1965  N  N     . LEU   A  1 294  ? -52.619 70.167  72.009  1.00 16.52 ? 292  LEU   A N     1 
ATOM   1966  C  CA    . LEU   A  1 294  ? -52.184 68.977  71.288  1.00 16.24 ? 292  LEU   A CA    1 
ATOM   1967  C  C     . LEU   A  1 294  ? -53.252 67.892  71.339  1.00 16.33 ? 292  LEU   A C     1 
ATOM   1968  O  O     . LEU   A  1 294  ? -53.496 67.207  70.341  1.00 16.73 ? 292  LEU   A O     1 
ATOM   1969  C  CB    . LEU   A  1 294  ? -50.870 68.459  71.874  1.00 16.32 ? 292  LEU   A CB    1 
ATOM   1970  C  CG    . LEU   A  1 294  ? -49.679 69.408  71.767  1.00 15.98 ? 292  LEU   A CG    1 
ATOM   1971  C  CD1   . LEU   A  1 294  ? -48.495 68.833  72.553  1.00 15.80 ? 292  LEU   A CD1   1 
ATOM   1972  C  CD2   . LEU   A  1 294  ? -49.301 69.615  70.321  1.00 17.48 ? 292  LEU   A CD2   1 
ATOM   1973  N  N     . ALA   A  1 295  ? -53.890 67.718  72.499  1.00 16.30 ? 293  ALA   A N     1 
ATOM   1974  C  CA    . ALA   A  1 295  ? -54.961 66.734  72.614  1.00 16.41 ? 293  ALA   A CA    1 
ATOM   1975  C  C     . ALA   A  1 295  ? -56.132 67.078  71.699  1.00 17.54 ? 293  ALA   A C     1 
ATOM   1976  O  O     . ALA   A  1 295  ? -56.760 66.182  71.117  1.00 16.82 ? 293  ALA   A O     1 
ATOM   1977  C  CB    . ALA   A  1 295  ? -55.426 66.635  74.070  1.00 16.37 ? 293  ALA   A CB    1 
ATOM   1978  N  N     . LEU   A  1 296  ? -56.460 68.367  71.575  1.00 16.68 ? 294  LEU   A N     1 
ATOM   1979  C  CA    . LEU   A  1 296  ? -57.538 68.757  70.670  1.00 17.67 ? 294  LEU   A CA    1 
ATOM   1980  C  C     . LEU   A  1 296  ? -57.215 68.369  69.236  1.00 19.06 ? 294  LEU   A C     1 
ATOM   1981  O  O     . LEU   A  1 296  ? -58.109 67.981  68.473  1.00 17.65 ? 294  LEU   A O     1 
ATOM   1982  C  CB    . LEU   A  1 296  ? -57.803 70.258  70.767  1.00 17.06 ? 294  LEU   A CB    1 
ATOM   1983  C  CG    . LEU   A  1 296  ? -58.457 70.752  72.055  1.00 19.60 ? 294  LEU   A CG    1 
ATOM   1984  C  CD1   . LEU   A  1 296  ? -58.466 72.275  72.093  1.00 20.12 ? 294  LEU   A CD1   1 
ATOM   1985  C  CD2   . LEU   A  1 296  ? -59.885 70.201  72.207  1.00 19.67 ? 294  LEU   A CD2   1 
ATOM   1986  N  N     . LEU   A  1 297  ? -55.944 68.494  68.841  1.00 16.88 ? 295  LEU   A N     1 
ATOM   1987  C  CA    . LEU   A  1 297  ? -55.545 68.071  67.506  1.00 16.98 ? 295  LEU   A CA    1 
ATOM   1988  C  C     . LEU   A  1 297  ? -55.610 66.554  67.371  1.00 18.66 ? 295  LEU   A C     1 
ATOM   1989  O  O     . LEU   A  1 297  ? -56.074 66.038  66.346  1.00 17.34 ? 295  LEU   A O     1 
ATOM   1990  C  CB    . LEU   A  1 297  ? -54.133 68.598  67.193  1.00 16.88 ? 295  LEU   A CB    1 
ATOM   1991  N  N     . ALA   A  1 298  ? -55.168 65.817  68.402  1.00 16.83 ? 296  ALA   A N     1 
ATOM   1992  C  CA    . ALA   A  1 298  ? -55.260 64.363  68.334  1.00 16.87 ? 296  ALA   A CA    1 
ATOM   1993  C  C     . ALA   A  1 298  ? -56.714 63.926  68.276  1.00 19.00 ? 296  ALA   A C     1 
ATOM   1994  O  O     . ALA   A  1 298  ? -57.058 62.973  67.567  1.00 17.58 ? 296  ALA   A O     1 
ATOM   1995  C  CB    . ALA   A  1 298  ? -54.560 63.717  69.531  1.00 16.69 ? 296  ALA   A CB    1 
ATOM   1996  N  N     . LYS   A  1 299  ? -57.576 64.620  69.019  1.00 17.07 ? 297  LYS   A N     1 
ATOM   1997  C  CA    . LYS   A  1 299  ? -59.006 64.349  68.954  1.00 17.48 ? 297  LYS   A CA    1 
ATOM   1998  C  C     . LYS   A  1 299  ? -59.528 64.516  67.533  1.00 20.91 ? 297  LYS   A C     1 
ATOM   1999  O  O     . LYS   A  1 299  ? -60.271 63.664  67.034  1.00 19.33 ? 297  LYS   A O     1 
ATOM   2000  C  CB    . LYS   A  1 299  ? -59.753 65.267  69.919  1.00 18.93 ? 297  LYS   A CB    1 
ATOM   2001  C  CG    . LYS   A  1 299  ? -61.239 65.421  69.612  1.00 17.85 ? 297  LYS   A CG    1 
ATOM   2002  C  CD    . LYS   A  1 299  ? -61.986 66.130  70.725  1.00 19.67 ? 297  LYS   A CD    1 
ATOM   2003  C  CE    . LYS   A  1 299  ? -63.345 66.628  70.217  1.00 22.42 ? 297  LYS   A CE    1 
ATOM   2004  N  NZ    . LYS   A  1 299  ? -64.103 67.325  71.282  1.00 29.18 ? 297  LYS   A NZ    1 
ATOM   2005  N  N     . ASN   A  1 300  ? -59.139 65.601  66.851  1.00 17.64 ? 298  ASN   A N     1 
ATOM   2006  C  CA    A ASN   A  1 300  ? -59.666 65.862  65.513  0.49 19.34 ? 298  ASN   A CA    1 
ATOM   2007  C  CA    B ASN   A  1 300  ? -59.727 65.812  65.537  0.51 19.32 ? 298  ASN   A CA    1 
ATOM   2008  C  C     . ASN   A  1 300  ? -59.290 64.751  64.539  1.00 20.24 ? 298  ASN   A C     1 
ATOM   2009  O  O     . ASN   A  1 300  ? -60.057 64.420  63.629  1.00 23.50 ? 298  ASN   A O     1 
ATOM   2010  C  CB    A ASN   A  1 300  ? -59.161 67.216  65.006  0.49 22.73 ? 298  ASN   A CB    1 
ATOM   2011  C  CB    B ASN   A  1 300  ? -59.407 67.191  64.983  0.51 23.08 ? 298  ASN   A CB    1 
ATOM   2012  C  CG    A ASN   A  1 300  ? -59.778 68.390  65.757  0.49 23.62 ? 298  ASN   A CG    1 
ATOM   2013  C  CG    B ASN   A  1 300  ? -60.334 67.555  63.847  0.51 25.78 ? 298  ASN   A CG    1 
ATOM   2014  O  OD1   A ASN   A  1 300  ? -60.780 68.243  66.450  0.49 26.32 ? 298  ASN   A OD1   1 
ATOM   2015  O  OD1   B ASN   A  1 300  ? -61.478 67.956  64.072  0.51 30.03 ? 298  ASN   A OD1   1 
ATOM   2016  N  ND2   A ASN   A  1 300  ? -59.180 69.559  65.614  0.49 25.32 ? 298  ASN   A ND2   1 
ATOM   2017  N  ND2   B ASN   A  1 300  ? -59.877 67.354  62.625  0.51 24.58 ? 298  ASN   A ND2   1 
ATOM   2018  N  N     . TYR   A  1 301  ? -58.097 64.184  64.694  1.00 17.99 ? 299  TYR   A N     1 
ATOM   2019  C  CA    . TYR   A  1 301  ? -57.688 63.073  63.845  1.00 17.76 ? 299  TYR   A CA    1 
ATOM   2020  C  C     . TYR   A  1 301  ? -58.066 61.713  64.413  1.00 19.53 ? 299  TYR   A C     1 
ATOM   2021  O  O     . TYR   A  1 301  ? -57.832 60.694  63.744  1.00 20.52 ? 299  TYR   A O     1 
ATOM   2022  C  CB    . TYR   A  1 301  ? -56.183 63.082  63.634  1.00 17.62 ? 299  TYR   A CB    1 
ATOM   2023  C  CG    . TYR   A  1 301  ? -55.683 64.180  62.746  1.00 17.67 ? 299  TYR   A CG    1 
ATOM   2024  C  CD1   . TYR   A  1 301  ? -55.838 64.106  61.372  1.00 17.92 ? 299  TYR   A CD1   1 
ATOM   2025  C  CD2   . TYR   A  1 301  ? -55.019 65.270  63.280  1.00 19.96 ? 299  TYR   A CD2   1 
ATOM   2026  C  CE1   . TYR   A  1 301  ? -55.354 65.106  60.539  1.00 19.19 ? 299  TYR   A CE1   1 
ATOM   2027  C  CE2   . TYR   A  1 301  ? -54.523 66.266  62.466  1.00 19.72 ? 299  TYR   A CE2   1 
ATOM   2028  C  CZ    . TYR   A  1 301  ? -54.705 66.182  61.095  1.00 22.38 ? 299  TYR   A CZ    1 
ATOM   2029  O  OH    . TYR   A  1 301  ? -54.217 67.176  60.278  1.00 21.61 ? 299  TYR   A OH    1 
ATOM   2030  N  N     . ASP   A  1 302  ? -58.579 61.680  65.640  1.00 19.02 ? 300  ASP   A N     1 
ATOM   2031  C  CA    . ASP   A  1 302  ? -58.904 60.452  66.363  1.00 18.92 ? 300  ASP   A CA    1 
ATOM   2032  C  C     . ASP   A  1 302  ? -57.699 59.508  66.416  1.00 21.09 ? 300  ASP   A C     1 
ATOM   2033  O  O     . ASP   A  1 302  ? -57.750 58.351  66.000  1.00 18.80 ? 300  ASP   A O     1 
ATOM   2034  C  CB    . ASP   A  1 302  ? -60.127 59.768  65.741  1.00 19.71 ? 300  ASP   A CB    1 
ATOM   2035  C  CG    . ASP   A  1 302  ? -60.837 58.848  66.717  1.00 24.69 ? 300  ASP   A CG    1 
ATOM   2036  O  OD1   . ASP   A  1 302  ? -60.890 59.185  67.924  1.00 23.88 ? 300  ASP   A OD1   1 
ATOM   2037  O  OD2   . ASP   A  1 302  ? -61.340 57.788  66.274  1.00 23.58 ? 300  ASP   A OD2   1 
ATOM   2038  N  N     . ILE   A  1 303  ? -56.589 60.030  66.933  1.00 19.56 ? 301  ILE   A N     1 
ATOM   2039  C  CA    . ILE   A  1 303  ? -55.412 59.214  67.200  1.00 17.30 ? 301  ILE   A CA    1 
ATOM   2040  C  C     . ILE   A  1 303  ? -55.164 59.213  68.700  1.00 17.49 ? 301  ILE   A C     1 
ATOM   2041  O  O     . ILE   A  1 303  ? -55.697 60.037  69.447  1.00 17.09 ? 301  ILE   A O     1 
ATOM   2042  C  CB    . ILE   A  1 303  ? -54.154 59.711  66.446  1.00 18.32 ? 301  ILE   A CB    1 
ATOM   2043  C  CG1   . ILE   A  1 303  ? -53.653 61.042  67.032  1.00 17.70 ? 301  ILE   A CG1   1 
ATOM   2044  C  CG2   . ILE   A  1 303  ? -54.454 59.848  64.940  1.00 19.08 ? 301  ILE   A CG2   1 
ATOM   2045  C  CD1   . ILE   A  1 303  ? -52.304 61.494  66.441  1.00 17.49 ? 301  ILE   A CD1   1 
ATOM   2046  N  N     . GLY   A  1 304  ? -54.344 58.263  69.140  1.00 18.01 ? 302  GLY   A N     1 
ATOM   2047  C  CA    . GLY   A  1 304  ? -53.960 58.218  70.538  1.00 19.85 ? 302  GLY   A CA    1 
ATOM   2048  C  C     . GLY   A  1 304  ? -52.939 59.296  70.861  1.00 16.94 ? 302  GLY   A C     1 
ATOM   2049  O  O     . GLY   A  1 304  ? -52.069 59.626  70.056  1.00 18.50 ? 302  GLY   A O     1 
ATOM   2050  N  N     . LEU   A  1 305  ? -53.061 59.852  72.062  1.00 18.04 ? 303  LEU   A N     1 
ATOM   2051  C  CA    . LEU   A  1 305  ? -52.075 60.784  72.588  1.00 16.30 ? 303  LEU   A CA    1 
ATOM   2052  C  C     . LEU   A  1 305  ? -51.756 60.329  74.002  1.00 16.20 ? 303  LEU   A C     1 
ATOM   2053  O  O     . LEU   A  1 305  ? -52.584 60.467  74.902  1.00 18.31 ? 303  LEU   A O     1 
ATOM   2054  C  CB    . LEU   A  1 305  ? -52.581 62.225  72.567  1.00 16.27 ? 303  LEU   A CB    1 
ATOM   2055  C  CG    . LEU   A  1 305  ? -51.528 63.240  73.029  1.00 17.98 ? 303  LEU   A CG    1 
ATOM   2056  C  CD1   . LEU   A  1 305  ? -51.605 64.508  72.191  1.00 22.98 ? 303  LEU   A CD1   1 
ATOM   2057  C  CD2   . LEU   A  1 305  ? -51.691 63.577  74.509  1.00 22.09 ? 303  LEU   A CD2   1 
ATOM   2058  N  N     . ASN   A  1 306  ? -50.555 59.800  74.193  1.00 16.45 ? 304  ASN   A N     1 
ATOM   2059  C  CA    . ASN   A  1 306  ? -50.152 59.205  75.456  1.00 16.03 ? 304  ASN   A CA    1 
ATOM   2060  C  C     . ASN   A  1 306  ? -49.204 60.139  76.192  1.00 15.82 ? 304  ASN   A C     1 
ATOM   2061  O  O     . ASN   A  1 306  ? -48.244 60.637  75.600  1.00 16.51 ? 304  ASN   A O     1 
ATOM   2062  C  CB    . ASN   A  1 306  ? -49.450 57.878  75.217  1.00 17.10 ? 304  ASN   A CB    1 
ATOM   2063  C  CG    . ASN   A  1 306  ? -48.774 57.368  76.460  1.00 19.10 ? 304  ASN   A CG    1 
ATOM   2064  O  OD1   . ASN   A  1 306  ? -47.575 57.614  76.692  1.00 21.14 ? 304  ASN   A OD1   1 
ATOM   2065  N  ND2   . ASN   A  1 306  ? -49.535 56.670  77.284  1.00 16.99 ? 304  ASN   A ND2   1 
ATOM   2066  N  N     . ILE   A  1 307  ? -49.445 60.333  77.484  1.00 15.77 ? 305  ILE   A N     1 
ATOM   2067  C  CA    . ILE   A  1 307  ? -48.520 61.071  78.336  1.00 15.60 ? 305  ILE   A CA    1 
ATOM   2068  C  C     . ILE   A  1 307  ? -47.543 60.094  78.975  1.00 17.77 ? 305  ILE   A C     1 
ATOM   2069  O  O     . ILE   A  1 307  ? -47.918 59.309  79.854  1.00 16.34 ? 305  ILE   A O     1 
ATOM   2070  C  CB    . ILE   A  1 307  ? -49.256 61.879  79.405  1.00 16.72 ? 305  ILE   A CB    1 
ATOM   2071  C  CG1   . ILE   A  1 307  ? -50.242 62.836  78.724  1.00 17.21 ? 305  ILE   A CG1   1 
ATOM   2072  C  CG2   . ILE   A  1 307  ? -48.216 62.596  80.319  1.00 17.52 ? 305  ILE   A CG2   1 
ATOM   2073  C  CD1   . ILE   A  1 307  ? -51.149 63.557  79.685  1.00 20.43 ? 305  ILE   A CD1   1 
ATOM   2074  N  N     . ASP   A  1 308  ? -46.276 60.183  78.565  1.00 16.62 ? 306  ASP   A N     1 
ATOM   2075  C  CA    . ASP   A  1 308  ? -45.217 59.345  79.114  1.00 15.57 ? 306  ASP   A CA    1 
ATOM   2076  C  C     . ASP   A  1 308  ? -44.997 59.667  80.586  1.00 17.28 ? 306  ASP   A C     1 
ATOM   2077  O  O     . ASP   A  1 308  ? -45.200 60.803  81.027  1.00 17.61 ? 306  ASP   A O     1 
ATOM   2078  C  CB    . ASP   A  1 308  ? -43.902 59.576  78.360  1.00 17.62 ? 306  ASP   A CB    1 
ATOM   2079  C  CG    . ASP   A  1 308  ? -43.856 58.890  77.007  1.00 21.14 ? 306  ASP   A CG    1 
ATOM   2080  O  OD1   . ASP   A  1 308  ? -44.754 58.084  76.698  1.00 22.48 ? 306  ASP   A OD1   1 
ATOM   2081  O  OD2   . ASP   A  1 308  ? -42.890 59.162  76.252  1.00 25.01 ? 306  ASP   A OD2   1 
ATOM   2082  N  N     . ALA   A  1 309  ? -44.565 58.661  81.353  1.00 15.36 ? 307  ALA   A N     1 
ATOM   2083  C  CA    . ALA   A  1 309  ? -44.304 58.855  82.775  1.00 16.19 ? 307  ALA   A CA    1 
ATOM   2084  C  C     . ALA   A  1 309  ? -42.818 59.109  82.995  1.00 18.40 ? 307  ALA   A C     1 
ATOM   2085  O  O     . ALA   A  1 309  ? -41.969 58.464  82.372  1.00 17.14 ? 307  ALA   A O     1 
ATOM   2086  C  CB    . ALA   A  1 309  ? -44.756 57.655  83.613  1.00 15.91 ? 307  ALA   A CB    1 
ATOM   2087  N  N     . GLU   A  1 310  ? -42.509 60.058  83.878  1.00 16.53 ? 308  GLU   A N     1 
ATOM   2088  C  CA    . GLU   A  1 310  ? -41.118 60.461  84.052  1.00 17.48 ? 308  GLU   A CA    1 
ATOM   2089  C  C     . GLU   A  1 310  ? -40.708 60.252  85.503  1.00 16.85 ? 308  GLU   A C     1 
ATOM   2090  O  O     . GLU   A  1 310  ? -40.986 59.184  86.064  1.00 16.10 ? 308  GLU   A O     1 
ATOM   2091  C  CB    . GLU   A  1 310  ? -40.929 61.904  83.574  1.00 16.15 ? 308  GLU   A CB    1 
ATOM   2092  C  CG    . GLU   A  1 310  ? -41.372 62.064  82.107  1.00 19.51 ? 308  GLU   A CG    1 
ATOM   2093  C  CD    . GLU   A  1 310  ? -41.084 63.441  81.542  1.00 20.67 ? 308  GLU   A CD    1 
ATOM   2094  O  OE1   . GLU   A  1 310  ? -39.895 63.737  81.303  1.00 19.85 ? 308  GLU   A OE1   1 
ATOM   2095  O  OE2   . GLU   A  1 310  ? -42.051 64.217  81.352  1.00 19.28 ? 308  GLU   A OE2   1 
ATOM   2096  N  N     . GLU   A  1 311  ? -40.060 61.239  86.125  1.00 15.64 ? 309  GLU   A N     1 
ATOM   2097  C  CA    . GLU   A  1 311  ? -39.527 61.009  87.460  1.00 15.94 ? 309  GLU   A CA    1 
ATOM   2098  C  C     . GLU   A  1 311  ? -40.652 60.885  88.480  1.00 17.86 ? 309  GLU   A C     1 
ATOM   2099  O  O     . GLU   A  1 311  ? -41.754 61.409  88.300  1.00 15.40 ? 309  GLU   A O     1 
ATOM   2100  C  CB    . GLU   A  1 311  ? -38.576 62.138  87.882  1.00 17.67 ? 309  GLU   A CB    1 
ATOM   2101  C  CG    . GLU   A  1 311  ? -37.300 62.223  87.034  1.00 20.84 ? 309  GLU   A CG    1 
ATOM   2102  C  CD    . GLU   A  1 311  ? -37.485 63.053  85.774  1.00 21.43 ? 309  GLU   A CD    1 
ATOM   2103  O  OE1   . GLU   A  1 311  ? -38.630 63.433  85.456  1.00 19.60 ? 309  GLU   A OE1   1 
ATOM   2104  O  OE2   . GLU   A  1 311  ? -36.479 63.334  85.095  1.00 26.58 ? 309  GLU   A OE2   1 
ATOM   2105  N  N     . ALA   A  1 312  ? -40.342 60.205  89.588  1.00 17.73 ? 310  ALA   A N     1 
ATOM   2106  C  CA    . ALA   A  1 312  ? -41.351 59.961  90.613  1.00 17.19 ? 310  ALA   A CA    1 
ATOM   2107  C  C     . ALA   A  1 312  ? -41.916 61.257  91.182  1.00 15.14 ? 310  ALA   A C     1 
ATOM   2108  O  O     . ALA   A  1 312  ? -43.082 61.288  91.586  1.00 17.09 ? 310  ALA   A O     1 
ATOM   2109  C  CB    . ALA   A  1 312  ? -40.767 59.103  91.740  1.00 16.54 ? 310  ALA   A CB    1 
ATOM   2110  N  N     . ASP   A  1 313  ? -41.123 62.332  91.228  1.00 15.00 ? 311  ASP   A N     1 
ATOM   2111  C  CA    . ASP   A  1 313  ? -41.632 63.566  91.823  1.00 17.94 ? 311  ASP   A CA    1 
ATOM   2112  C  C     . ASP   A  1 313  ? -42.520 64.354  90.866  1.00 17.68 ? 311  ASP   A C     1 
ATOM   2113  O  O     . ASP   A  1 313  ? -42.998 65.438  91.227  1.00 16.41 ? 311  ASP   A O     1 
ATOM   2114  C  CB    . ASP   A  1 313  ? -40.479 64.442  92.353  1.00 17.23 ? 311  ASP   A CB    1 
ATOM   2115  C  CG    . ASP   A  1 313  ? -39.569 64.977  91.260  1.00 19.18 ? 311  ASP   A CG    1 
ATOM   2116  O  OD1   . ASP   A  1 313  ? -39.804 64.698  90.074  1.00 19.44 ? 311  ASP   A OD1   1 
ATOM   2117  O  OD2   . ASP   A  1 313  ? -38.594 65.679  91.611  1.00 23.90 ? 311  ASP   A OD2   1 
ATOM   2118  N  N     . ARG   A  1 314  ? -42.766 63.821  89.673  1.00 15.00 ? 312  ARG   A N     1 
ATOM   2119  C  CA    . ARG   A  1 314  ? -43.717 64.399  88.738  1.00 15.01 ? 312  ARG   A CA    1 
ATOM   2120  C  C     . ARG   A  1 314  ? -44.994 63.583  88.597  1.00 15.34 ? 312  ARG   A C     1 
ATOM   2121  O  O     . ARG   A  1 314  ? -45.950 64.075  87.988  1.00 17.48 ? 312  ARG   A O     1 
ATOM   2122  C  CB    . ARG   A  1 314  ? -43.061 64.568  87.365  1.00 17.08 ? 312  ARG   A CB    1 
ATOM   2123  C  CG    . ARG   A  1 314  ? -41.989 65.647  87.408  1.00 18.09 ? 312  ARG   A CG    1 
ATOM   2124  C  CD    . ARG   A  1 314  ? -41.046 65.563  86.232  1.00 16.05 ? 312  ARG   A CD    1 
ATOM   2125  N  NE    . ARG   A  1 314  ? -40.474 66.876  85.961  1.00 19.14 ? 312  ARG   A NE    1 
ATOM   2126  C  CZ    . ARG   A  1 314  ? -39.508 67.104  85.084  1.00 19.66 ? 312  ARG   A CZ    1 
ATOM   2127  N  NH1   . ARG   A  1 314  ? -38.875 66.109  84.479  1.00 17.26 ? 312  ARG   A NH1   1 
ATOM   2128  N  NH2   . ARG   A  1 314  ? -39.157 68.363  84.821  1.00 19.58 ? 312  ARG   A NH2   1 
ATOM   2129  N  N     . LEU   A  1 315  ? -45.042 62.374  89.159  1.00 15.25 ? 313  LEU   A N     1 
ATOM   2130  C  CA    . LEU   A  1 315  ? -46.227 61.523  89.026  1.00 15.41 ? 313  LEU   A CA    1 
ATOM   2131  C  C     . LEU   A  1 315  ? -47.502 62.258  89.429  1.00 16.70 ? 313  LEU   A C     1 
ATOM   2132  O  O     . LEU   A  1 315  ? -48.428 62.420  88.625  1.00 15.59 ? 313  LEU   A O     1 
ATOM   2133  C  CB    . LEU   A  1 315  ? -46.067 60.260  89.871  1.00 16.49 ? 313  LEU   A CB    1 
ATOM   2134  C  CG    . LEU   A  1 315  ? -46.852 59.021  89.407  1.00 16.58 ? 313  LEU   A CG    1 
ATOM   2135  C  CD1   . LEU   A  1 315  ? -46.445 57.819  90.291  1.00 18.55 ? 313  LEU   A CD1   1 
ATOM   2136  C  CD2   . LEU   A  1 315  ? -48.369 59.190  89.412  1.00 18.66 ? 313  LEU   A CD2   1 
ATOM   2137  N  N     . GLU   A  1 316  ? -47.588 62.679  90.685  1.00 17.14 ? 314  GLU   A N     1 
ATOM   2138  C  CA    . GLU   A  1 316  ? -48.881 63.183  91.144  1.00 17.21 ? 314  GLU   A CA    1 
ATOM   2139  C  C     . GLU   A  1 316  ? -49.232 64.514  90.484  1.00 17.00 ? 314  GLU   A C     1 
ATOM   2140  O  O     . GLU   A  1 316  ? -50.407 64.773  90.205  1.00 16.90 ? 314  GLU   A O     1 
ATOM   2141  C  CB    . GLU   A  1 316  ? -48.887 63.278  92.668  1.00 17.68 ? 314  GLU   A CB    1 
ATOM   2142  C  CG    . GLU   A  1 316  ? -48.821 61.871  93.297  1.00 18.42 ? 314  GLU   A CG    1 
ATOM   2143  C  CD    . GLU   A  1 316  ? -48.835 61.883  94.802  1.00 21.63 ? 314  GLU   A CD    1 
ATOM   2144  O  OE1   . GLU   A  1 316  ? -49.611 62.675  95.393  1.00 20.56 ? 314  GLU   A OE1   1 
ATOM   2145  O  OE2   . GLU   A  1 316  ? -48.061 61.093  95.390  1.00 19.92 ? 314  GLU   A OE2   1 
ATOM   2146  N  N     . LEU   A  1 317  ? -48.235 65.357  90.205  1.00 15.56 ? 315  LEU   A N     1 
ATOM   2147  C  CA    . LEU   A  1 317  ? -48.494 66.561  89.415  1.00 17.23 ? 315  LEU   A CA    1 
ATOM   2148  C  C     . LEU   A  1 317  ? -49.123 66.221  88.061  1.00 17.44 ? 315  LEU   A C     1 
ATOM   2149  O  O     . LEU   A  1 317  ? -50.050 66.903  87.612  1.00 17.25 ? 315  LEU   A O     1 
ATOM   2150  C  CB    . LEU   A  1 317  ? -47.193 67.337  89.218  1.00 19.29 ? 315  LEU   A CB    1 
ATOM   2151  C  CG    . LEU   A  1 317  ? -47.254 68.583  88.331  1.00 18.16 ? 315  LEU   A CG    1 
ATOM   2152  C  CD1   . LEU   A  1 317  ? -48.242 69.603  88.876  1.00 20.56 ? 315  LEU   A CD1   1 
ATOM   2153  C  CD2   . LEU   A  1 317  ? -45.868 69.206  88.189  1.00 22.40 ? 315  LEU   A CD2   1 
ATOM   2154  N  N     . SER   A  1 318  ? -48.615 65.184  87.386  1.00 17.40 ? 316  SER   A N     1 
ATOM   2155  C  CA    . SER   A  1 318  ? -49.165 64.816  86.083  1.00 18.42 ? 316  SER   A CA    1 
ATOM   2156  C  C     . SER   A  1 318  ? -50.613 64.362  86.209  1.00 19.73 ? 316  SER   A C     1 
ATOM   2157  O  O     . SER   A  1 318  ? -51.395 64.521  85.263  1.00 16.38 ? 316  SER   A O     1 
ATOM   2158  C  CB    . SER   A  1 318  ? -48.308 63.726  85.417  1.00 18.03 ? 316  SER   A CB    1 
ATOM   2159  O  OG    . SER   A  1 318  ? -48.501 62.451  86.029  1.00 15.49 ? 316  SER   A OG    1 
ATOM   2160  N  N     . LEU   A  1 319  ? -50.991 63.806  87.368  1.00 15.77 ? 317  LEU   A N     1 
ATOM   2161  C  CA    . LEU   A  1 319  ? -52.386 63.415  87.571  1.00 16.05 ? 317  LEU   A CA    1 
ATOM   2162  C  C     . LEU   A  1 319  ? -53.306 64.626  87.556  1.00 18.05 ? 317  LEU   A C     1 
ATOM   2163  O  O     . LEU   A  1 319  ? -54.452 64.534  87.101  1.00 17.29 ? 317  LEU   A O     1 
ATOM   2164  C  CB    . LEU   A  1 319  ? -52.543 62.659  88.890  1.00 16.13 ? 317  LEU   A CB    1 
ATOM   2165  C  CG    . LEU   A  1 319  ? -51.809 61.322  88.992  1.00 18.68 ? 317  LEU   A CG    1 
ATOM   2166  C  CD1   . LEU   A  1 319  ? -51.994 60.735  90.387  1.00 17.74 ? 317  LEU   A CD1   1 
ATOM   2167  C  CD2   . LEU   A  1 319  ? -52.314 60.359  87.916  1.00 17.13 ? 317  LEU   A CD2   1 
ATOM   2168  N  N     . ASP   A  1 320  ? -52.833 65.767  88.058  1.00 18.53 ? 318  ASP   A N     1 
ATOM   2169  C  CA    . ASP   A  1 320  ? -53.670 66.959  88.018  1.00 18.72 ? 318  ASP   A CA    1 
ATOM   2170  C  C     . ASP   A  1 320  ? -53.926 67.384  86.584  1.00 19.36 ? 318  ASP   A C     1 
ATOM   2171  O  O     . ASP   A  1 320  ? -55.027 67.840  86.255  1.00 19.50 ? 318  ASP   A O     1 
ATOM   2172  C  CB    . ASP   A  1 320  ? -53.033 68.089  88.820  1.00 19.20 ? 318  ASP   A CB    1 
ATOM   2173  C  CG    . ASP   A  1 320  ? -53.194 67.880  90.312  1.00 23.61 ? 318  ASP   A CG    1 
ATOM   2174  O  OD1   . ASP   A  1 320  ? -54.351 67.688  90.749  1.00 26.10 ? 318  ASP   A OD1   1 
ATOM   2175  O  OD2   . ASP   A  1 320  ? -52.170 67.856  91.029  1.00 26.58 ? 318  ASP   A OD2   1 
ATOM   2176  N  N     . LEU   A  1 321  ? -52.921 67.249  85.719  1.00 16.27 ? 319  LEU   A N     1 
ATOM   2177  C  CA    . LEU   A  1 321  ? -53.132 67.561  84.311  1.00 16.20 ? 319  LEU   A CA    1 
ATOM   2178  C  C     . LEU   A  1 321  ? -54.076 66.553  83.683  1.00 17.63 ? 319  LEU   A C     1 
ATOM   2179  O  O     . LEU   A  1 321  ? -55.017 66.928  82.970  1.00 19.40 ? 319  LEU   A O     1 
ATOM   2180  C  CB    . LEU   A  1 321  ? -51.809 67.590  83.550  1.00 18.77 ? 319  LEU   A CB    1 
ATOM   2181  C  CG    . LEU   A  1 321  ? -50.992 68.860  83.783  1.00 23.63 ? 319  LEU   A CG    1 
ATOM   2182  C  CD1   . LEU   A  1 321  ? -50.039 68.641  84.933  1.00 26.46 ? 319  LEU   A CD1   1 
ATOM   2183  C  CD2   . LEU   A  1 321  ? -50.234 69.231  82.520  1.00 24.19 ? 319  LEU   A CD2   1 
ATOM   2184  N  N     . LEU   A  1 322  ? -53.847 65.267  83.954  1.00 17.62 ? 320  LEU   A N     1 
ATOM   2185  C  CA    . LEU   A  1 322  ? -54.743 64.235  83.436  1.00 17.81 ? 320  LEU   A CA    1 
ATOM   2186  C  C     . LEU   A  1 322  ? -56.184 64.496  83.846  1.00 16.93 ? 320  LEU   A C     1 
ATOM   2187  O  O     . LEU   A  1 322  ? -57.106 64.348  83.033  1.00 18.50 ? 320  LEU   A O     1 
ATOM   2188  C  CB    . LEU   A  1 322  ? -54.313 62.859  83.931  1.00 17.77 ? 320  LEU   A CB    1 
ATOM   2189  C  CG    . LEU   A  1 322  ? -55.128 61.689  83.375  1.00 16.33 ? 320  LEU   A CG    1 
ATOM   2190  C  CD1   . LEU   A  1 322  ? -54.925 61.570  81.848  1.00 17.00 ? 320  LEU   A CD1   1 
ATOM   2191  C  CD2   . LEU   A  1 322  ? -54.731 60.408  84.084  1.00 16.50 ? 320  LEU   A CD2   1 
ATOM   2192  N  N     . GLU   A  1 323  ? -56.403 64.872  85.104  1.00 20.76 ? 321  GLU   A N     1 
ATOM   2193  C  CA    A GLU   A  1 323  ? -57.767 65.073  85.589  0.56 20.24 ? 321  GLU   A CA    1 
ATOM   2194  C  CA    B GLU   A  1 323  ? -57.773 65.052  85.562  0.44 20.28 ? 321  GLU   A CA    1 
ATOM   2195  C  C     . GLU   A  1 323  ? -58.436 66.229  84.858  1.00 21.46 ? 321  GLU   A C     1 
ATOM   2196  O  O     . GLU   A  1 323  ? -59.564 66.105  84.375  1.00 18.95 ? 321  GLU   A O     1 
ATOM   2197  C  CB    A GLU   A  1 323  ? -57.765 65.315  87.102  0.56 22.47 ? 321  GLU   A CB    1 
ATOM   2198  C  CB    B GLU   A  1 323  ? -57.819 65.220  87.075  0.44 22.48 ? 321  GLU   A CB    1 
ATOM   2199  C  CG    A GLU   A  1 323  ? -59.115 65.802  87.648  0.56 19.84 ? 321  GLU   A CG    1 
ATOM   2200  C  CG    B GLU   A  1 323  ? -59.036 64.522  87.647  0.44 23.88 ? 321  GLU   A CG    1 
ATOM   2201  C  CD    A GLU   A  1 323  ? -59.609 64.995  88.835  0.56 25.64 ? 321  GLU   A CD    1 
ATOM   2202  C  CD    B GLU   A  1 323  ? -59.588 65.200  88.859  0.44 25.71 ? 321  GLU   A CD    1 
ATOM   2203  O  OE1   A GLU   A  1 323  ? -59.222 63.822  88.972  0.56 24.61 ? 321  GLU   A OE1   1 
ATOM   2204  O  OE1   B GLU   A  1 323  ? -58.800 65.829  89.595  0.44 24.91 ? 321  GLU   A OE1   1 
ATOM   2205  O  OE2   A GLU   A  1 323  ? -60.398 65.532  89.638  0.56 31.80 ? 321  GLU   A OE2   1 
ATOM   2206  O  OE2   B GLU   A  1 323  ? -60.820 65.105  89.063  0.44 27.05 ? 321  GLU   A OE2   1 
ATOM   2207  N  N     . VAL   A  1 324  ? -57.743 67.370  84.761  1.00 18.60 ? 322  VAL   A N     1 
ATOM   2208  C  CA    . VAL   A  1 324  ? -58.326 68.515  84.058  1.00 17.01 ? 322  VAL   A CA    1 
ATOM   2209  C  C     . VAL   A  1 324  ? -58.657 68.140  82.621  1.00 18.63 ? 322  VAL   A C     1 
ATOM   2210  O  O     . VAL   A  1 324  ? -59.751 68.424  82.122  1.00 19.29 ? 322  VAL   A O     1 
ATOM   2211  C  CB    . VAL   A  1 324  ? -57.389 69.732  84.108  1.00 18.68 ? 322  VAL   A CB    1 
ATOM   2212  C  CG1   . VAL   A  1 324  ? -58.019 70.885  83.315  1.00 22.75 ? 322  VAL   A CG1   1 
ATOM   2213  C  CG2   . VAL   A  1 324  ? -57.155 70.135  85.534  1.00 22.10 ? 322  VAL   A CG2   1 
ATOM   2214  N  N     . LEU   A  1 325  ? -57.712 67.493  81.933  1.00 16.50 ? 323  LEU   A N     1 
ATOM   2215  C  CA    . LEU   A  1 325  ? -57.925 67.136  80.534  1.00 17.88 ? 323  LEU   A CA    1 
ATOM   2216  C  C     . LEU   A  1 325  ? -59.128 66.214  80.374  1.00 18.67 ? 323  LEU   A C     1 
ATOM   2217  O  O     . LEU   A  1 325  ? -59.977 66.432  79.506  1.00 16.86 ? 323  LEU   A O     1 
ATOM   2218  C  CB    . LEU   A  1 325  ? -56.669 66.478  79.964  1.00 17.21 ? 323  LEU   A CB    1 
ATOM   2219  C  CG    . LEU   A  1 325  ? -55.468 67.415  79.883  1.00 16.29 ? 323  LEU   A CG    1 
ATOM   2220  C  CD1   . LEU   A  1 325  ? -54.208 66.588  79.664  1.00 16.37 ? 323  LEU   A CD1   1 
ATOM   2221  C  CD2   . LEU   A  1 325  ? -55.654 68.417  78.770  1.00 18.22 ? 323  LEU   A CD2   1 
ATOM   2222  N  N     . CYS   A  1 326  ? -59.222 65.179  81.208  1.00 18.15 ? 324  CYS   A N     1 
ATOM   2223  C  CA    . CYS   A  1 326  ? -60.310 64.217  81.045  1.00 17.97 ? 324  CYS   A CA    1 
ATOM   2224  C  C     . CYS   A  1 326  ? -61.666 64.804  81.397  1.00 21.41 ? 324  CYS   A C     1 
ATOM   2225  O  O     . CYS   A  1 326  ? -62.688 64.288  80.925  1.00 20.45 ? 324  CYS   A O     1 
ATOM   2226  C  CB    . CYS   A  1 326  ? -60.062 62.972  81.893  1.00 18.82 ? 324  CYS   A CB    1 
ATOM   2227  S  SG    . CYS   A  1 326  ? -58.694 62.011  81.243  1.00 22.16 ? 324  CYS   A SG    1 
ATOM   2228  N  N     . LEU   A  1 327  ? -61.700 65.866  82.201  1.00 17.78 ? 325  LEU   A N     1 
ATOM   2229  C  CA    . LEU   A  1 327  ? -62.952 66.530  82.548  1.00 18.79 ? 325  LEU   A CA    1 
ATOM   2230  C  C     . LEU   A  1 327  ? -63.262 67.717  81.648  1.00 19.77 ? 325  LEU   A C     1 
ATOM   2231  O  O     . LEU   A  1 327  ? -64.334 68.315  81.779  1.00 19.54 ? 325  LEU   A O     1 
ATOM   2232  C  CB    . LEU   A  1 327  ? -62.905 66.988  84.006  1.00 22.08 ? 325  LEU   A CB    1 
ATOM   2233  C  CG    . LEU   A  1 327  ? -62.760 65.867  85.044  1.00 26.08 ? 325  LEU   A CG    1 
ATOM   2234  C  CD1   . LEU   A  1 327  ? -62.557 66.449  86.439  1.00 28.82 ? 325  LEU   A CD1   1 
ATOM   2235  C  CD2   . LEU   A  1 327  ? -63.965 64.953  85.029  1.00 26.60 ? 325  LEU   A CD2   1 
ATOM   2236  N  N     . ASP   A  1 328  ? -62.352 68.071  80.746  1.00 18.70 ? 326  ASP   A N     1 
ATOM   2237  C  CA    . ASP   A  1 328  ? -62.535 69.216  79.863  1.00 19.22 ? 326  ASP   A CA    1 
ATOM   2238  C  C     . ASP   A  1 328  ? -63.473 68.834  78.725  1.00 19.63 ? 326  ASP   A C     1 
ATOM   2239  O  O     . ASP   A  1 328  ? -63.137 67.979  77.896  1.00 18.32 ? 326  ASP   A O     1 
ATOM   2240  C  CB    . ASP   A  1 328  ? -61.186 69.680  79.319  1.00 19.85 ? 326  ASP   A CB    1 
ATOM   2241  C  CG    . ASP   A  1 328  ? -61.270 71.027  78.625  1.00 22.64 ? 326  ASP   A CG    1 
ATOM   2242  O  OD1   . ASP   A  1 328  ? -62.211 71.244  77.832  1.00 23.30 ? 326  ASP   A OD1   1 
ATOM   2243  O  OD2   . ASP   A  1 328  ? -60.409 71.892  78.902  1.00 23.88 ? 326  ASP   A OD2   1 
ATOM   2244  N  N     . GLY   A  1 329  ? -64.643 69.475  78.679  1.00 19.23 ? 327  GLY   A N     1 
ATOM   2245  C  CA    . GLY   A  1 329  ? -65.638 69.126  77.675  1.00 21.37 ? 327  GLY   A CA    1 
ATOM   2246  C  C     . GLY   A  1 329  ? -65.195 69.348  76.244  1.00 19.54 ? 327  GLY   A C     1 
ATOM   2247  O  O     . GLY   A  1 329  ? -65.737 68.715  75.335  1.00 19.25 ? 327  GLY   A O     1 
ATOM   2248  N  N     . ASP   A  1 330  ? -64.224 70.237  76.018  1.00 19.99 ? 328  ASP   A N     1 
ATOM   2249  C  CA    . ASP   A  1 330  ? -63.714 70.445  74.669  1.00 19.11 ? 328  ASP   A CA    1 
ATOM   2250  C  C     . ASP   A  1 330  ? -63.083 69.189  74.092  1.00 18.08 ? 328  ASP   A C     1 
ATOM   2251  O  O     . ASP   A  1 330  ? -62.968 69.077  72.868  1.00 18.80 ? 328  ASP   A O     1 
ATOM   2252  C  CB    . ASP   A  1 330  ? -62.669 71.566  74.638  1.00 18.12 ? 328  ASP   A CB    1 
ATOM   2253  C  CG    . ASP   A  1 330  ? -63.263 72.926  74.898  1.00 24.34 ? 328  ASP   A CG    1 
ATOM   2254  O  OD1   . ASP   A  1 330  ? -64.469 73.106  74.627  1.00 27.83 ? 328  ASP   A OD1   1 
ATOM   2255  O  OD2   . ASP   A  1 330  ? -62.518 73.816  75.364  1.00 22.96 ? 328  ASP   A OD2   1 
ATOM   2256  N  N     . LEU   A  1 331  ? -62.647 68.268  74.947  1.00 17.39 ? 329  LEU   A N     1 
ATOM   2257  C  CA    . LEU   A  1 331  ? -62.012 67.028  74.533  1.00 17.30 ? 329  LEU   A CA    1 
ATOM   2258  C  C     . LEU   A  1 331  ? -62.994 65.863  74.487  1.00 20.48 ? 329  LEU   A C     1 
ATOM   2259  O  O     . LEU   A  1 331  ? -62.581 64.722  74.252  1.00 19.13 ? 329  LEU   A O     1 
ATOM   2260  C  CB    . LEU   A  1 331  ? -60.839 66.707  75.468  1.00 17.07 ? 329  LEU   A CB    1 
ATOM   2261  C  CG    . LEU   A  1 331  ? -59.587 67.562  75.202  1.00 18.32 ? 329  LEU   A CG    1 
ATOM   2262  C  CD1   . LEU   A  1 331  ? -58.569 67.380  76.301  1.00 16.69 ? 329  LEU   A CD1   1 
ATOM   2263  C  CD2   . LEU   A  1 331  ? -58.957 67.218  73.850  1.00 16.85 ? 329  LEU   A CD2   1 
ATOM   2264  N  N     . SER   A  1 332  ? -64.282 66.126  74.673  1.00 18.63 ? 330  SER   A N     1 
ATOM   2265  C  CA    . SER   A  1 332  ? -65.248 65.038  74.753  1.00 20.48 ? 330  SER   A CA    1 
ATOM   2266  C  C     . SER   A  1 332  ? -65.395 64.342  73.406  1.00 19.54 ? 330  SER   A C     1 
ATOM   2267  O  O     . SER   A  1 332  ? -65.181 64.938  72.351  1.00 20.37 ? 330  SER   A O     1 
ATOM   2268  C  CB    . SER   A  1 332  ? -66.609 65.564  75.202  1.00 20.92 ? 330  SER   A CB    1 
ATOM   2269  O  OG    . SER   A  1 332  ? -67.098 66.504  74.269  1.00 23.96 ? 330  SER   A OG    1 
ATOM   2270  N  N     . GLY   A  1 333  ? -65.780 63.068  73.452  1.00 19.33 ? 331  GLY   A N     1 
ATOM   2271  C  CA    . GLY   A  1 333  ? -66.009 62.303  72.241  1.00 21.32 ? 331  GLY   A CA    1 
ATOM   2272  C  C     . GLY   A  1 333  ? -64.774 61.624  71.705  1.00 20.58 ? 331  GLY   A C     1 
ATOM   2273  O  O     . GLY   A  1 333  ? -64.840 60.968  70.660  1.00 21.45 ? 331  GLY   A O     1 
ATOM   2274  N  N     . TRP   A  1 334  ? -63.655 61.757  72.391  1.00 17.85 ? 332  TRP   A N     1 
ATOM   2275  C  CA    . TRP   A  1 334  ? -62.393 61.165  71.988  1.00 17.95 ? 332  TRP   A CA    1 
ATOM   2276  C  C     . TRP   A  1 334  ? -61.873 60.331  73.143  1.00 17.61 ? 332  TRP   A C     1 
ATOM   2277  O  O     . TRP   A  1 334  ? -61.802 60.824  74.268  1.00 18.26 ? 332  TRP   A O     1 
ATOM   2278  C  CB    . TRP   A  1 334  ? -61.424 62.283  71.628  1.00 19.21 ? 332  TRP   A CB    1 
ATOM   2279  C  CG    . TRP   A  1 334  ? -59.980 61.917  71.444  1.00 17.31 ? 332  TRP   A CG    1 
ATOM   2280  C  CD1   . TRP   A  1 334  ? -59.440 61.171  70.443  1.00 17.88 ? 332  TRP   A CD1   1 
ATOM   2281  C  CD2   . TRP   A  1 334  ? -58.889 62.366  72.250  1.00 17.60 ? 332  TRP   A CD2   1 
ATOM   2282  N  NE1   . TRP   A  1 334  ? -58.078 61.100  70.587  1.00 17.98 ? 332  TRP   A NE1   1 
ATOM   2283  C  CE2   . TRP   A  1 334  ? -57.710 61.831  71.691  1.00 16.97 ? 332  TRP   A CE2   1 
ATOM   2284  C  CE3   . TRP   A  1 334  ? -58.795 63.159  73.400  1.00 16.95 ? 332  TRP   A CE3   1 
ATOM   2285  C  CZ2   . TRP   A  1 334  ? -56.444 62.058  72.245  1.00 16.75 ? 332  TRP   A CZ2   1 
ATOM   2286  C  CZ3   . TRP   A  1 334  ? -57.536 63.399  73.948  1.00 17.85 ? 332  TRP   A CZ3   1 
ATOM   2287  C  CH2   . TRP   A  1 334  ? -56.370 62.843  73.364  1.00 17.26 ? 332  TRP   A CH2   1 
ATOM   2288  N  N     . ASN   A  1 335  ? -61.502 59.078  72.869  1.00 18.11 ? 333  ASN   A N     1 
ATOM   2289  C  CA    . ASN   A  1 335  ? -60.965 58.187  73.889  1.00 17.91 ? 333  ASN   A CA    1 
ATOM   2290  C  C     . ASN   A  1 335  ? -59.477 57.952  73.709  1.00 19.76 ? 333  ASN   A C     1 
ATOM   2291  O  O     . ASN   A  1 335  ? -58.943 56.970  74.239  1.00 19.21 ? 333  ASN   A O     1 
ATOM   2292  C  CB    . ASN   A  1 335  ? -61.695 56.845  73.883  1.00 21.99 ? 333  ASN   A CB    1 
ATOM   2293  C  CG    . ASN   A  1 335  ? -63.059 56.936  74.531  1.00 21.53 ? 333  ASN   A CG    1 
ATOM   2294  O  OD1   . ASN   A  1 335  ? -63.252 57.689  75.481  1.00 21.21 ? 333  ASN   A OD1   1 
ATOM   2295  N  ND2   . ASN   A  1 335  ? -64.012 56.175  74.015  1.00 24.62 ? 333  ASN   A ND2   1 
ATOM   2296  N  N     . GLY   A  1 336  ? -58.800 58.828  72.961  1.00 17.27 ? 334  GLY   A N     1 
ATOM   2297  C  CA    . GLY   A  1 336  ? -57.399 58.625  72.653  1.00 17.11 ? 334  GLY   A CA    1 
ATOM   2298  C  C     . GLY   A  1 336  ? -56.411 59.101  73.699  1.00 17.79 ? 334  GLY   A C     1 
ATOM   2299  O  O     . GLY   A  1 336  ? -55.214 58.843  73.551  1.00 17.66 ? 334  GLY   A O     1 
ATOM   2300  N  N     . MET   A  1 337  ? -56.866 59.775  74.757  1.00 16.92 ? 335  MET   A N     1 
ATOM   2301  C  CA    A MET   A  1 337  ? -55.949 60.221  75.797  0.59 17.08 ? 335  MET   A CA    1 
ATOM   2302  C  CA    B MET   A  1 337  ? -55.944 60.218  75.794  0.41 17.10 ? 335  MET   A CA    1 
ATOM   2303  C  C     . MET   A  1 337  ? -55.374 59.022  76.541  1.00 17.33 ? 335  MET   A C     1 
ATOM   2304  O  O     . MET   A  1 337  ? -56.118 58.152  77.009  1.00 16.78 ? 335  MET   A O     1 
ATOM   2305  C  CB    A MET   A  1 337  ? -56.652 61.164  76.772  0.59 18.05 ? 335  MET   A CB    1 
ATOM   2306  C  CB    B MET   A  1 337  ? -56.634 61.167  76.770  0.41 18.05 ? 335  MET   A CB    1 
ATOM   2307  C  CG    A MET   A  1 337  ? -55.739 61.721  77.837  0.59 20.07 ? 335  MET   A CG    1 
ATOM   2308  C  CG    B MET   A  1 337  ? -55.778 61.506  77.969  0.41 20.08 ? 335  MET   A CG    1 
ATOM   2309  S  SD    A MET   A  1 337  ? -54.493 62.825  77.165  0.59 27.45 ? 335  MET   A SD    1 
ATOM   2310  S  SD    B MET   A  1 337  ? -55.687 63.275  78.253  0.41 21.92 ? 335  MET   A SD    1 
ATOM   2311  C  CE    A MET   A  1 337  ? -55.463 64.301  76.885  0.59 20.45 ? 335  MET   A CE    1 
ATOM   2312  C  CE    B MET   A  1 337  ? -55.008 63.808  76.682  0.41 19.69 ? 335  MET   A CE    1 
ATOM   2313  N  N     . GLY   A  1 338  ? -54.043 58.977  76.642  1.00 16.51 ? 336  GLY   A N     1 
ATOM   2314  C  CA    . GLY   A  1 338  ? -53.373 57.874  77.285  1.00 16.43 ? 336  GLY   A CA    1 
ATOM   2315  C  C     . GLY   A  1 338  ? -52.434 58.372  78.370  1.00 18.59 ? 336  GLY   A C     1 
ATOM   2316  O  O     . GLY   A  1 338  ? -52.066 59.549  78.420  1.00 16.93 ? 336  GLY   A O     1 
ATOM   2317  N  N     . PHE   A  1 339  ? -52.053 57.444  79.242  1.00 16.31 ? 337  PHE   A N     1 
ATOM   2318  C  CA    . PHE   A  1 339  ? -51.297 57.804  80.436  1.00 16.16 ? 337  PHE   A CA    1 
ATOM   2319  C  C     . PHE   A  1 339  ? -50.506 56.596  80.912  1.00 16.83 ? 337  PHE   A C     1 
ATOM   2320  O  O     . PHE   A  1 339  ? -51.060 55.499  81.053  1.00 16.36 ? 337  PHE   A O     1 
ATOM   2321  C  CB    . PHE   A  1 339  ? -52.245 58.291  81.547  1.00 16.55 ? 337  PHE   A CB    1 
ATOM   2322  C  CG    . PHE   A  1 339  ? -51.552 58.989  82.680  1.00 17.36 ? 337  PHE   A CG    1 
ATOM   2323  C  CD1   . PHE   A  1 339  ? -51.266 60.357  82.601  1.00 16.23 ? 337  PHE   A CD1   1 
ATOM   2324  C  CD2   . PHE   A  1 339  ? -51.206 58.288  83.827  1.00 16.26 ? 337  PHE   A CD2   1 
ATOM   2325  C  CE1   . PHE   A  1 339  ? -50.644 61.008  83.674  1.00 18.81 ? 337  PHE   A CE1   1 
ATOM   2326  C  CE2   . PHE   A  1 339  ? -50.574 58.932  84.887  1.00 18.72 ? 337  PHE   A CE2   1 
ATOM   2327  C  CZ    . PHE   A  1 339  ? -50.299 60.287  84.803  1.00 16.82 ? 337  PHE   A CZ    1 
ATOM   2328  N  N     . VAL   A  1 340  ? -49.212 56.799  81.138  1.00 16.46 ? 338  VAL   A N     1 
ATOM   2329  C  CA    . VAL   A  1 340  ? -48.315 55.747  81.592  1.00 16.04 ? 338  VAL   A CA    1 
ATOM   2330  C  C     . VAL   A  1 340  ? -48.334 55.688  83.108  1.00 16.04 ? 338  VAL   A C     1 
ATOM   2331  O  O     . VAL   A  1 340  ? -48.311 56.727  83.787  1.00 16.14 ? 338  VAL   A O     1 
ATOM   2332  C  CB    . VAL   A  1 340  ? -46.885 56.001  81.082  1.00 16.43 ? 338  VAL   A CB    1 
ATOM   2333  C  CG1   . VAL   A  1 340  ? -45.953 54.914  81.609  1.00 15.90 ? 338  VAL   A CG1   1 
ATOM   2334  C  CG2   . VAL   A  1 340  ? -46.877 56.056  79.571  1.00 15.88 ? 338  VAL   A CG2   1 
ATOM   2335  N  N     . VAL   A  1 341  ? -48.336 54.473  83.650  1.00 16.21 ? 339  VAL   A N     1 
ATOM   2336  C  CA    . VAL   A  1 341  ? -48.085 54.260  85.069  1.00 16.24 ? 339  VAL   A CA    1 
ATOM   2337  C  C     . VAL   A  1 341  ? -46.953 53.248  85.197  1.00 16.27 ? 339  VAL   A C     1 
ATOM   2338  O  O     . VAL   A  1 341  ? -46.878 52.281  84.434  1.00 16.40 ? 339  VAL   A O     1 
ATOM   2339  C  CB    . VAL   A  1 341  ? -49.353 53.794  85.818  1.00 17.15 ? 339  VAL   A CB    1 
ATOM   2340  C  CG1   . VAL   A  1 341  ? -50.493 54.787  85.565  1.00 18.03 ? 339  VAL   A CG1   1 
ATOM   2341  C  CG2   . VAL   A  1 341  ? -49.791 52.424  85.350  1.00 23.00 ? 339  VAL   A CG2   1 
ATOM   2342  N  N     . GLN   A  1 342  ? -46.062 53.492  86.144  1.00 16.94 ? 340  GLN   A N     1 
ATOM   2343  C  CA    . GLN   A  1 342  ? -44.816 52.745  86.256  1.00 16.58 ? 340  GLN   A CA    1 
ATOM   2344  C  C     . GLN   A  1 342  ? -44.944 51.755  87.401  1.00 16.38 ? 340  GLN   A C     1 
ATOM   2345  O  O     . GLN   A  1 342  ? -45.032 52.151  88.569  1.00 16.62 ? 340  GLN   A O     1 
ATOM   2346  C  CB    . GLN   A  1 342  ? -43.644 53.690  86.489  1.00 15.92 ? 340  GLN   A CB    1 
ATOM   2347  C  CG    . GLN   A  1 342  ? -43.477 54.747  85.400  1.00 15.72 ? 340  GLN   A CG    1 
ATOM   2348  C  CD    . GLN   A  1 342  ? -42.912 56.048  85.943  1.00 15.52 ? 340  GLN   A CD    1 
ATOM   2349  O  OE1   . GLN   A  1 342  ? -43.409 56.589  86.927  1.00 15.83 ? 340  GLN   A OE1   1 
ATOM   2350  N  NE2   . GLN   A  1 342  ? -41.863 56.547  85.307  1.00 16.75 ? 340  GLN   A NE2   1 
ATOM   2351  N  N     . ALA   A  1 343  ? -44.913 50.470  87.064  1.00 16.60 ? 341  ALA   A N     1 
ATOM   2352  C  CA    . ALA   A  1 343  ? -45.069 49.430  88.066  1.00 16.86 ? 341  ALA   A CA    1 
ATOM   2353  C  C     . ALA   A  1 343  ? -43.871 49.320  88.993  1.00 17.21 ? 341  ALA   A C     1 
ATOM   2354  O  O     . ALA   A  1 343  ? -43.986 48.690  90.051  1.00 17.01 ? 341  ALA   A O     1 
ATOM   2355  C  CB    . ALA   A  1 343  ? -45.338 48.092  87.375  1.00 17.85 ? 341  ALA   A CB    1 
ATOM   2356  N  N     . TYR   A  1 344  ? -42.731 49.930  88.657  1.00 17.01 ? 342  TYR   A N     1 
ATOM   2357  C  CA    . TYR   A  1 344  ? -41.681 49.912  89.659  1.00 17.41 ? 342  TYR   A CA    1 
ATOM   2358  C  C     . TYR   A  1 344  ? -41.944 50.903  90.781  1.00 16.82 ? 342  TYR   A C     1 
ATOM   2359  O  O     . TYR   A  1 344  ? -41.167 50.937  91.734  1.00 16.98 ? 342  TYR   A O     1 
ATOM   2360  C  CB    . TYR   A  1 344  ? -40.294 50.140  89.028  1.00 16.34 ? 342  TYR   A CB    1 
ATOM   2361  C  CG    . TYR   A  1 344  ? -39.886 51.523  88.513  1.00 17.86 ? 342  TYR   A CG    1 
ATOM   2362  C  CD1   . TYR   A  1 344  ? -40.760 52.611  88.484  1.00 15.91 ? 342  TYR   A CD1   1 
ATOM   2363  C  CD2   . TYR   A  1 344  ? -38.587 51.716  88.042  1.00 17.55 ? 342  TYR   A CD2   1 
ATOM   2364  C  CE1   . TYR   A  1 344  ? -40.341 53.859  87.996  1.00 15.67 ? 342  TYR   A CE1   1 
ATOM   2365  C  CE2   . TYR   A  1 344  ? -38.167 52.935  87.556  1.00 17.53 ? 342  TYR   A CE2   1 
ATOM   2366  C  CZ    . TYR   A  1 344  ? -39.040 54.003  87.539  1.00 16.49 ? 342  TYR   A CZ    1 
ATOM   2367  O  OH    . TYR   A  1 344  ? -38.595 55.202  87.059  1.00 18.07 ? 342  TYR   A OH    1 
ATOM   2368  N  N     . GLY   A  1 345  ? -43.023 51.681  90.703  1.00 17.27 ? 343  GLY   A N     1 
ATOM   2369  C  CA    . GLY   A  1 345  ? -43.326 52.685  91.705  1.00 16.31 ? 343  GLY   A CA    1 
ATOM   2370  C  C     . GLY   A  1 345  ? -44.333 52.150  92.707  1.00 17.12 ? 343  GLY   A C     1 
ATOM   2371  O  O     . GLY   A  1 345  ? -45.281 51.453  92.343  1.00 17.29 ? 343  GLY   A O     1 
ATOM   2372  N  N     . LYS   A  1 346  ? -44.101 52.482  93.976  1.00 16.62 ? 344  LYS   A N     1 
ATOM   2373  C  CA    . LYS   A  1 346  ? -44.929 51.994  95.068  1.00 16.91 ? 344  LYS   A CA    1 
ATOM   2374  C  C     . LYS   A  1 346  ? -46.361 52.507  94.995  1.00 17.85 ? 344  LYS   A C     1 
ATOM   2375  O  O     . LYS   A  1 346  ? -47.259 51.906  95.601  1.00 19.95 ? 344  LYS   A O     1 
ATOM   2376  C  CB    . LYS   A  1 346  ? -44.278 52.394  96.385  1.00 16.91 ? 344  LYS   A CB    1 
ATOM   2377  C  CG    . LYS   A  1 346  ? -42.937 51.719  96.600  1.00 18.32 ? 344  LYS   A CG    1 
ATOM   2378  C  CD    . LYS   A  1 346  ? -42.301 52.193  97.882  1.00 19.18 ? 344  LYS   A CD    1 
ATOM   2379  C  CE    . LYS   A  1 346  ? -40.962 51.521  98.106  1.00 20.17 ? 344  LYS   A CE    1 
ATOM   2380  N  NZ    . LYS   A  1 346  ? -40.258 52.166  99.256  1.00 20.52 ? 344  LYS   A NZ    1 
ATOM   2381  N  N     . ARG   A  1 347  ? -46.596 53.595  94.271  1.00 16.87 ? 345  ARG   A N     1 
ATOM   2382  C  CA    . ARG   A  1 347  ? -47.931 54.171  94.178  1.00 18.97 ? 345  ARG   A CA    1 
ATOM   2383  C  C     . ARG   A  1 347  ? -48.762 53.568  93.053  1.00 17.74 ? 345  ARG   A C     1 
ATOM   2384  O  O     . ARG   A  1 347  ? -49.972 53.830  92.984  1.00 17.63 ? 345  ARG   A O     1 
ATOM   2385  C  CB    . ARG   A  1 347  ? -47.815 55.691  94.004  1.00 18.29 ? 345  ARG   A CB    1 
ATOM   2386  C  CG    . ARG   A  1 347  ? -47.336 56.385  95.287  1.00 16.56 ? 345  ARG   A CG    1 
ATOM   2387  C  CD    . ARG   A  1 347  ? -46.955 57.829  95.027  1.00 16.31 ? 345  ARG   A CD    1 
ATOM   2388  N  NE    . ARG   A  1 347  ? -45.728 57.896  94.245  1.00 16.07 ? 345  ARG   A NE    1 
ATOM   2389  C  CZ    . ARG   A  1 347  ? -45.266 58.998  93.672  1.00 18.23 ? 345  ARG   A CZ    1 
ATOM   2390  N  NH1   . ARG   A  1 347  ? -45.895 60.155  93.804  1.00 16.38 ? 345  ARG   A NH1   1 
ATOM   2391  N  NH2   . ARG   A  1 347  ? -44.163 58.928  92.921  1.00 15.67 ? 345  ARG   A NH2   1 
ATOM   2392  N  N     . CYS   A  1 348  ? -48.154 52.736  92.206  1.00 17.17 ? 346  CYS   A N     1 
ATOM   2393  C  CA    . CYS   A  1 348  ? -48.790 52.305  90.961  1.00 17.12 ? 346  CYS   A CA    1 
ATOM   2394  C  C     . CYS   A  1 348  ? -50.217 51.792  91.131  1.00 18.63 ? 346  CYS   A C     1 
ATOM   2395  O  O     . CYS   A  1 348  ? -51.103 52.274  90.410  1.00 17.27 ? 346  CYS   A O     1 
ATOM   2396  C  CB    . CYS   A  1 348  ? -47.921 51.245  90.270  1.00 19.40 ? 346  CYS   A CB    1 
ATOM   2397  S  SG    . CYS   A  1 348  ? -48.444 50.979  88.559  1.00 22.59 ? 346  CYS   A SG    1 
ATOM   2398  N  N     . PRO   A  1 349  ? -50.521 50.862  92.039  1.00 17.54 ? 347  PRO   A N     1 
ATOM   2399  C  CA    . PRO   A  1 349  ? -51.915 50.391  92.120  1.00 19.19 ? 347  PRO   A CA    1 
ATOM   2400  C  C     . PRO   A  1 349  ? -52.883 51.473  92.555  1.00 17.84 ? 347  PRO   A C     1 
ATOM   2401  O  O     . PRO   A  1 349  ? -54.027 51.501  92.086  1.00 19.21 ? 347  PRO   A O     1 
ATOM   2402  C  CB    . PRO   A  1 349  ? -51.854 49.243  93.139  1.00 22.04 ? 347  PRO   A CB    1 
ATOM   2403  C  CG    . PRO   A  1 349  ? -50.599 49.439  93.900  1.00 23.10 ? 347  PRO   A CG    1 
ATOM   2404  C  CD    . PRO   A  1 349  ? -49.637 50.154  92.990  1.00 18.66 ? 347  PRO   A CD    1 
ATOM   2405  N  N     . PHE   A  1 350  ? -52.441 52.374  93.429  1.00 17.70 ? 348  PHE   A N     1 
ATOM   2406  C  CA    . PHE   A  1 350  ? -53.286 53.474  93.872  1.00 20.11 ? 348  PHE   A CA    1 
ATOM   2407  C  C     . PHE   A  1 350  ? -53.462 54.502  92.770  1.00 17.45 ? 348  PHE   A C     1 
ATOM   2408  O  O     . PHE   A  1 350  ? -54.534 55.097  92.637  1.00 18.27 ? 348  PHE   A O     1 
ATOM   2409  C  CB    . PHE   A  1 350  ? -52.672 54.086  95.124  1.00 19.15 ? 348  PHE   A CB    1 
ATOM   2410  C  CG    . PHE   A  1 350  ? -52.332 53.054  96.147  1.00 21.98 ? 348  PHE   A CG    1 
ATOM   2411  C  CD1   . PHE   A  1 350  ? -53.329 52.523  96.954  1.00 20.33 ? 348  PHE   A CD1   1 
ATOM   2412  C  CD2   . PHE   A  1 350  ? -51.046 52.542  96.236  1.00 20.40 ? 348  PHE   A CD2   1 
ATOM   2413  C  CE1   . PHE   A  1 350  ? -53.032 51.532  97.870  1.00 24.30 ? 348  PHE   A CE1   1 
ATOM   2414  C  CE2   . PHE   A  1 350  ? -50.740 51.552  97.150  1.00 22.49 ? 348  PHE   A CE2   1 
ATOM   2415  C  CZ    . PHE   A  1 350  ? -51.736 51.045  97.964  1.00 24.37 ? 348  PHE   A CZ    1 
ATOM   2416  N  N     . VAL   A  1 351  ? -52.420 54.726  91.974  1.00 17.17 ? 349  VAL   A N     1 
ATOM   2417  C  CA    . VAL   A  1 351  ? -52.575 55.551  90.780  1.00 16.97 ? 349  VAL   A CA    1 
ATOM   2418  C  C     . VAL   A  1 351  ? -53.601 54.926  89.849  1.00 17.72 ? 349  VAL   A C     1 
ATOM   2419  O  O     . VAL   A  1 351  ? -54.453 55.617  89.282  1.00 17.77 ? 349  VAL   A O     1 
ATOM   2420  C  CB    . VAL   A  1 351  ? -51.216 55.738  90.083  1.00 16.69 ? 349  VAL   A CB    1 
ATOM   2421  C  CG1   . VAL   A  1 351  ? -51.381 56.520  88.765  1.00 16.52 ? 349  VAL   A CG1   1 
ATOM   2422  C  CG2   . VAL   A  1 351  ? -50.259 56.446  91.019  1.00 17.17 ? 349  VAL   A CG2   1 
ATOM   2423  N  N     . LEU   A  1 352  ? -53.531 53.611  89.665  1.00 18.08 ? 350  LEU   A N     1 
ATOM   2424  C  CA    . LEU   A  1 352  ? -54.490 52.967  88.781  1.00 18.18 ? 350  LEU   A CA    1 
ATOM   2425  C  C     . LEU   A  1 352  ? -55.908 53.090  89.321  1.00 19.52 ? 350  LEU   A C     1 
ATOM   2426  O  O     . LEU   A  1 352  ? -56.841 53.344  88.554  1.00 18.99 ? 350  LEU   A O     1 
ATOM   2427  C  CB    . LEU   A  1 352  ? -54.118 51.506  88.578  1.00 19.44 ? 350  LEU   A CB    1 
ATOM   2428  C  CG    . LEU   A  1 352  ? -52.921 51.322  87.660  1.00 20.54 ? 350  LEU   A CG    1 
ATOM   2429  C  CD1   . LEU   A  1 352  ? -52.505 49.865  87.747  1.00 20.60 ? 350  LEU   A CD1   1 
ATOM   2430  C  CD2   . LEU   A  1 352  ? -53.325 51.699  86.245  1.00 18.85 ? 350  LEU   A CD2   1 
ATOM   2431  N  N     . ASP   A  1 353  ? -56.097 52.916  90.634  1.00 18.64 ? 351  ASP   A N     1 
ATOM   2432  C  CA    . ASP   A  1 353  ? -57.416 53.159  91.212  1.00 18.18 ? 351  ASP   A CA    1 
ATOM   2433  C  C     . ASP   A  1 353  ? -57.922 54.548  90.847  1.00 18.20 ? 351  ASP   A C     1 
ATOM   2434  O  O     . ASP   A  1 353  ? -59.087 54.724  90.480  1.00 19.45 ? 351  ASP   A O     1 
ATOM   2435  C  CB    . ASP   A  1 353  ? -57.376 53.026  92.732  1.00 20.11 ? 351  ASP   A CB    1 
ATOM   2436  C  CG    . ASP   A  1 353  ? -57.225 51.596  93.192  1.00 24.31 ? 351  ASP   A CG    1 
ATOM   2437  O  OD1   . ASP   A  1 353  ? -57.536 50.679  92.411  1.00 24.12 ? 351  ASP   A OD1   1 
ATOM   2438  O  OD2   . ASP   A  1 353  ? -56.797 51.402  94.348  1.00 26.80 ? 351  ASP   A OD2   1 
ATOM   2439  N  N     . PHE   A  1 354  ? -57.055 55.553  90.975  1.00 17.73 ? 352  PHE   A N     1 
ATOM   2440  C  CA    . PHE   A  1 354  ? -57.456 56.923  90.681  1.00 17.59 ? 352  PHE   A CA    1 
ATOM   2441  C  C     . PHE   A  1 354  ? -57.817 57.088  89.207  1.00 18.69 ? 352  PHE   A C     1 
ATOM   2442  O  O     . PHE   A  1 354  ? -58.832 57.703  88.875  1.00 18.45 ? 352  PHE   A O     1 
ATOM   2443  C  CB    . PHE   A  1 354  ? -56.331 57.896  91.071  1.00 17.67 ? 352  PHE   A CB    1 
ATOM   2444  C  CG    . PHE   A  1 354  ? -56.539 59.275  90.536  1.00 19.19 ? 352  PHE   A CG    1 
ATOM   2445  C  CD1   . PHE   A  1 354  ? -57.318 60.195  91.233  1.00 20.71 ? 352  PHE   A CD1   1 
ATOM   2446  C  CD2   . PHE   A  1 354  ? -55.995 59.642  89.310  1.00 18.62 ? 352  PHE   A CD2   1 
ATOM   2447  C  CE1   . PHE   A  1 354  ? -57.532 61.470  90.720  1.00 21.05 ? 352  PHE   A CE1   1 
ATOM   2448  C  CE2   . PHE   A  1 354  ? -56.208 60.910  88.790  1.00 21.37 ? 352  PHE   A CE2   1 
ATOM   2449  C  CZ    . PHE   A  1 354  ? -56.973 61.822  89.494  1.00 21.69 ? 352  PHE   A CZ    1 
ATOM   2450  N  N     . ILE   A  1 355  ? -56.986 56.552  88.308  1.00 17.36 ? 353  ILE   A N     1 
ATOM   2451  C  CA    . ILE   A  1 355  ? -57.238 56.684  86.872  1.00 17.28 ? 353  ILE   A CA    1 
ATOM   2452  C  C     . ILE   A  1 355  ? -58.521 55.969  86.465  1.00 17.76 ? 353  ILE   A C     1 
ATOM   2453  O  O     . ILE   A  1 355  ? -59.312 56.483  85.660  1.00 17.60 ? 353  ILE   A O     1 
ATOM   2454  C  CB    . ILE   A  1 355  ? -56.041 56.145  86.074  1.00 17.11 ? 353  ILE   A CB    1 
ATOM   2455  C  CG1   . ILE   A  1 355  ? -54.830 57.049  86.291  1.00 17.39 ? 353  ILE   A CG1   1 
ATOM   2456  C  CG2   . ILE   A  1 355  ? -56.380 56.072  84.575  1.00 18.38 ? 353  ILE   A CG2   1 
ATOM   2457  C  CD1   . ILE   A  1 355  ? -53.560 56.509  85.633  1.00 17.74 ? 353  ILE   A CD1   1 
ATOM   2458  N  N     . ILE   A  1 356  ? -58.724 54.753  86.973  1.00 17.81 ? 354  ILE   A N     1 
ATOM   2459  C  CA    . ILE   A  1 356  ? -59.941 54.012  86.644  1.00 18.12 ? 354  ILE   A CA    1 
ATOM   2460  C  C     . ILE   A  1 356  ? -61.168 54.781  87.105  1.00 18.54 ? 354  ILE   A C     1 
ATOM   2461  O  O     . ILE   A  1 356  ? -62.162 54.883  86.376  1.00 18.40 ? 354  ILE   A O     1 
ATOM   2462  C  CB    . ILE   A  1 356  ? -59.884 52.599  87.256  1.00 19.06 ? 354  ILE   A CB    1 
ATOM   2463  C  CG1   . ILE   A  1 356  ? -58.828 51.766  86.523  1.00 18.28 ? 354  ILE   A CG1   1 
ATOM   2464  C  CG2   . ILE   A  1 356  ? -61.260 51.923  87.218  1.00 18.77 ? 354  ILE   A CG2   1 
ATOM   2465  C  CD1   . ILE   A  1 356  ? -58.407 50.491  87.275  1.00 18.49 ? 354  ILE   A CD1   1 
ATOM   2466  N  N     . ASP   A  1 357  ? -61.119 55.340  88.314  1.00 18.57 ? 355  ASP   A N     1 
ATOM   2467  C  CA    . ASP   A  1 357  ? -62.228 56.168  88.778  1.00 19.19 ? 355  ASP   A CA    1 
ATOM   2468  C  C     . ASP   A  1 357  ? -62.395 57.404  87.907  1.00 20.62 ? 355  ASP   A C     1 
ATOM   2469  O  O     . ASP   A  1 357  ? -63.522 57.821  87.604  1.00 19.89 ? 355  ASP   A O     1 
ATOM   2470  C  CB    . ASP   A  1 357  ? -62.005 56.577  90.232  1.00 20.82 ? 355  ASP   A CB    1 
ATOM   2471  C  CG    . ASP   A  1 357  ? -63.073 57.521  90.731  1.00 21.76 ? 355  ASP   A CG    1 
ATOM   2472  O  OD1   . ASP   A  1 357  ? -64.183 57.039  91.023  1.00 21.60 ? 355  ASP   A OD1   1 
ATOM   2473  O  OD2   . ASP   A  1 357  ? -62.805 58.735  90.822  1.00 22.10 ? 355  ASP   A OD2   1 
ATOM   2474  N  N     . LEU   A  1 358  ? -61.282 58.016  87.501  1.00 18.34 ? 356  LEU   A N     1 
ATOM   2475  C  CA    . LEU   A  1 358  ? -61.382 59.178  86.629  1.00 19.58 ? 356  LEU   A CA    1 
ATOM   2476  C  C     . LEU   A  1 358  ? -62.004 58.802  85.294  1.00 17.92 ? 356  LEU   A C     1 
ATOM   2477  O  O     . LEU   A  1 358  ? -62.827 59.550  84.751  1.00 18.84 ? 356  LEU   A O     1 
ATOM   2478  C  CB    . LEU   A  1 358  ? -60.005 59.799  86.432  1.00 17.42 ? 356  LEU   A CB    1 
ATOM   2479  C  CG    . LEU   A  1 358  ? -59.908 60.923  85.415  1.00 19.14 ? 356  LEU   A CG    1 
ATOM   2480  C  CD1   . LEU   A  1 358  ? -60.814 62.092  85.792  1.00 20.59 ? 356  LEU   A CD1   1 
ATOM   2481  C  CD2   . LEU   A  1 358  ? -58.414 61.370  85.300  1.00 16.94 ? 356  LEU   A CD2   1 
ATOM   2482  N  N     . ALA   A  1 359  ? -61.631 57.643  84.750  1.00 19.27 ? 357  ALA   A N     1 
ATOM   2483  C  CA    . ALA   A  1 359  ? -62.276 57.168  83.532  1.00 18.53 ? 357  ALA   A CA    1 
ATOM   2484  C  C     . ALA   A  1 359  ? -63.784 57.014  83.730  1.00 19.73 ? 357  ALA   A C     1 
ATOM   2485  O  O     . ALA   A  1 359  ? -64.573 57.414  82.867  1.00 20.21 ? 357  ALA   A O     1 
ATOM   2486  C  CB    . ALA   A  1 359  ? -61.644 55.845  83.084  1.00 19.14 ? 357  ALA   A CB    1 
ATOM   2487  N  N     . ARG   A  1 360  ? -64.201 56.463  84.872  1.00 20.84 ? 358  ARG   A N     1 
ATOM   2488  C  CA    . ARG   A  1 360  ? -65.629 56.307  85.142  1.00 19.73 ? 358  ARG   A CA    1 
ATOM   2489  C  C     . ARG   A  1 360  ? -66.333 57.656  85.234  1.00 22.99 ? 358  ARG   A C     1 
ATOM   2490  O  O     . ARG   A  1 360  ? -67.407 57.845  84.649  1.00 25.26 ? 358  ARG   A O     1 
ATOM   2491  C  CB    . ARG   A  1 360  ? -65.845 55.512  86.428  1.00 20.37 ? 358  ARG   A CB    1 
ATOM   2492  C  CG    . ARG   A  1 360  ? -65.341 54.086  86.337  1.00 25.79 ? 358  ARG   A CG    1 
ATOM   2493  C  CD    . ARG   A  1 360  ? -65.789 53.253  87.534  1.00 30.58 ? 358  ARG   A CD    1 
ATOM   2494  N  NE    . ARG   A  1 360  ? -65.001 52.032  87.644  1.00 32.88 ? 358  ARG   A NE    1 
ATOM   2495  C  CZ    . ARG   A  1 360  ? -65.290 50.897  87.022  1.00 36.51 ? 358  ARG   A CZ    1 
ATOM   2496  N  NH1   . ARG   A  1 360  ? -66.369 50.784  86.256  1.00 32.90 ? 358  ARG   A NH1   1 
ATOM   2497  N  NH2   . ARG   A  1 360  ? -64.485 49.849  87.177  1.00 36.92 ? 358  ARG   A NH2   1 
ATOM   2498  N  N     . ARG   A  1 361  ? -65.752 58.597  85.982  1.00 21.06 ? 359  ARG   A N     1 
ATOM   2499  C  CA    . ARG   A  1 361  ? -66.365 59.915  86.166  1.00 23.16 ? 359  ARG   A CA    1 
ATOM   2500  C  C     . ARG   A  1 361  ? -66.454 60.673  84.850  1.00 21.53 ? 359  ARG   A C     1 
ATOM   2501  O  O     . ARG   A  1 361  ? -67.473 61.306  84.544  1.00 24.31 ? 359  ARG   A O     1 
ATOM   2502  C  CB    . ARG   A  1 361  ? -65.551 60.741  87.167  1.00 22.48 ? 359  ARG   A CB    1 
ATOM   2503  C  CG    . ARG   A  1 361  ? -65.560 60.197  88.580  1.00 26.27 ? 359  ARG   A CG    1 
ATOM   2504  C  CD    . ARG   A  1 361  ? -64.895 61.172  89.530  1.00 28.53 ? 359  ARG   A CD    1 
ATOM   2505  N  NE    . ARG   A  1 361  ? -63.433 61.131  89.485  1.00 24.45 ? 359  ARG   A NE    1 
ATOM   2506  C  CZ    . ARG   A  1 361  ? -62.659 62.180  89.239  1.00 24.87 ? 359  ARG   A CZ    1 
ATOM   2507  N  NH1   . ARG   A  1 361  ? -63.170 63.351  88.895  1.00 23.23 ? 359  ARG   A NH1   1 
ATOM   2508  N  NH2   . ARG   A  1 361  ? -61.335 62.051  89.343  1.00 24.09 ? 359  ARG   A NH2   1 
ATOM   2509  N  N     . SER   A  1 362  ? -65.371 60.664  84.083  1.00 20.97 ? 360  SER   A N     1 
ATOM   2510  C  CA    . SER   A  1 362  ? -65.316 61.434  82.852  1.00 19.98 ? 360  SER   A CA    1 
ATOM   2511  C  C     . SER   A  1 362  ? -66.029 60.741  81.708  1.00 21.32 ? 360  SER   A C     1 
ATOM   2512  O  O     . SER   A  1 362  ? -66.376 61.398  80.722  1.00 22.91 ? 360  SER   A O     1 
ATOM   2513  C  CB    . SER   A  1 362  ? -63.857 61.686  82.458  1.00 21.71 ? 360  SER   A CB    1 
ATOM   2514  O  OG    . SER   A  1 362  ? -63.192 60.469  82.135  1.00 20.50 ? 360  SER   A OG    1 
ATOM   2515  N  N     . GLY   A  1 363  ? -66.239 59.433  81.814  1.00 20.37 ? 361  GLY   A N     1 
ATOM   2516  C  CA    . GLY   A  1 363  ? -66.738 58.682  80.688  1.00 22.62 ? 361  GLY   A CA    1 
ATOM   2517  C  C     . GLY   A  1 363  ? -65.740 58.502  79.571  1.00 24.64 ? 361  GLY   A C     1 
ATOM   2518  O  O     . GLY   A  1 363  ? -66.134 58.108  78.471  1.00 26.26 ? 361  GLY   A O     1 
ATOM   2519  N  N     . ARG   A  1 364  ? -64.462 58.796  79.817  1.00 23.54 ? 362  ARG   A N     1 
ATOM   2520  C  CA    . ARG   A  1 364  ? -63.405 58.623  78.830  1.00 21.16 ? 362  ARG   A CA    1 
ATOM   2521  C  C     . ARG   A  1 364  ? -62.720 57.294  79.090  1.00 23.08 ? 362  ARG   A C     1 
ATOM   2522  O  O     . ARG   A  1 364  ? -62.355 56.993  80.231  1.00 23.78 ? 362  ARG   A O     1 
ATOM   2523  C  CB    . ARG   A  1 364  ? -62.376 59.747  78.909  1.00 21.67 ? 362  ARG   A CB    1 
ATOM   2524  C  CG    . ARG   A  1 364  ? -62.968 61.142  79.008  1.00 27.93 ? 362  ARG   A CG    1 
ATOM   2525  C  CD    . ARG   A  1 364  ? -62.766 61.934  77.739  1.00 23.99 ? 362  ARG   A CD    1 
ATOM   2526  N  NE    . ARG   A  1 364  ? -63.555 63.160  77.773  1.00 20.30 ? 362  ARG   A NE    1 
ATOM   2527  C  CZ    . ARG   A  1 364  ? -63.043 64.371  77.928  1.00 20.30 ? 362  ARG   A CZ    1 
ATOM   2528  N  NH1   . ARG   A  1 364  ? -61.732 64.568  77.963  1.00 17.21 ? 362  ARG   A NH1   1 
ATOM   2529  N  NH2   . ARG   A  1 364  ? -63.867 65.411  78.045  1.00 18.13 ? 362  ARG   A NH2   1 
ATOM   2530  N  N     . ARG   A  1 365  ? -62.550 56.505  78.040  1.00 20.40 ? 363  ARG   A N     1 
ATOM   2531  C  CA    . ARG   A  1 365  ? -61.871 55.225  78.180  1.00 21.07 ? 363  ARG   A CA    1 
ATOM   2532  C  C     . ARG   A  1 365  ? -60.379 55.501  78.104  1.00 20.71 ? 363  ARG   A C     1 
ATOM   2533  O  O     . ARG   A  1 365  ? -59.763 55.463  77.036  1.00 22.19 ? 363  ARG   A O     1 
ATOM   2534  C  CB    . ARG   A  1 365  ? -62.329 54.244  77.110  1.00 18.25 ? 363  ARG   A CB    1 
ATOM   2535  C  CG    . ARG   A  1 365  ? -61.730 52.871  77.302  1.00 18.98 ? 363  ARG   A CG    1 
ATOM   2536  C  CD    . ARG   A  1 365  ? -62.618 51.772  76.789  1.00 21.95 ? 363  ARG   A CD    1 
ATOM   2537  N  NE    . ARG   A  1 365  ? -62.010 50.471  77.052  1.00 24.25 ? 363  ARG   A NE    1 
ATOM   2538  C  CZ    . ARG   A  1 365  ? -61.311 49.791  76.157  1.00 20.84 ? 363  ARG   A CZ    1 
ATOM   2539  N  NH1   . ARG   A  1 365  ? -61.166 50.232  74.919  1.00 22.34 ? 363  ARG   A NH1   1 
ATOM   2540  N  NH2   . ARG   A  1 365  ? -60.740 48.644  76.513  1.00 23.97 ? 363  ARG   A NH2   1 
ATOM   2541  N  N     . ILE   A  1 366  ? -59.789 55.795  79.259  1.00 18.07 ? 364  ILE   A N     1 
ATOM   2542  C  CA    . ILE   A  1 366  ? -58.399 56.234  79.291  1.00 17.30 ? 364  ILE   A CA    1 
ATOM   2543  C  C     . ILE   A  1 366  ? -57.490 55.090  78.867  1.00 17.82 ? 364  ILE   A C     1 
ATOM   2544  O  O     . ILE   A  1 366  ? -57.638 53.954  79.330  1.00 17.49 ? 364  ILE   A O     1 
ATOM   2545  C  CB    . ILE   A  1 366  ? -58.044 56.757  80.690  1.00 17.46 ? 364  ILE   A CB    1 
ATOM   2546  C  CG1   . ILE   A  1 366  ? -58.943 57.952  81.034  1.00 18.61 ? 364  ILE   A CG1   1 
ATOM   2547  C  CG2   . ILE   A  1 366  ? -56.555 57.098  80.778  1.00 17.69 ? 364  ILE   A CG2   1 
ATOM   2548  C  CD1   . ILE   A  1 366  ? -58.810 58.437  82.488  1.00 18.01 ? 364  ILE   A CD1   1 
ATOM   2549  N  N     . MET   A  1 367  ? -56.545 55.386  77.976  1.00 17.14 ? 365  MET   A N     1 
ATOM   2550  C  CA    . MET   A  1 367  ? -55.556 54.399  77.564  1.00 17.14 ? 365  MET   A CA    1 
ATOM   2551  C  C     . MET   A  1 367  ? -54.457 54.380  78.615  1.00 18.09 ? 365  MET   A C     1 
ATOM   2552  O  O     . MET   A  1 367  ? -53.843 55.409  78.893  1.00 19.25 ? 365  MET   A O     1 
ATOM   2553  C  CB    . MET   A  1 367  ? -55.003 54.737  76.181  1.00 17.06 ? 365  MET   A CB    1 
ATOM   2554  C  CG    . MET   A  1 367  ? -56.113 54.893  75.123  1.00 19.06 ? 365  MET   A CG    1 
ATOM   2555  S  SD    . MET   A  1 367  ? -55.499 55.307  73.475  1.00 22.63 ? 365  MET   A SD    1 
ATOM   2556  C  CE    . MET   A  1 367  ? -55.235 53.698  72.725  1.00 22.33 ? 365  MET   A CE    1 
ATOM   2557  N  N     . VAL   A  1 368  ? -54.246 53.239  79.251  1.00 17.39 ? 366  VAL   A N     1 
ATOM   2558  C  CA    . VAL   A  1 368  ? -53.311 53.163  80.359  1.00 16.99 ? 366  VAL   A CA    1 
ATOM   2559  C  C     . VAL   A  1 368  ? -52.171 52.272  79.917  1.00 16.98 ? 366  VAL   A C     1 
ATOM   2560  O  O     . VAL   A  1 368  ? -52.365 51.070  79.710  1.00 18.90 ? 366  VAL   A O     1 
ATOM   2561  C  CB    . VAL   A  1 368  ? -53.969 52.631  81.638  1.00 17.17 ? 366  VAL   A CB    1 
ATOM   2562  C  CG1   . VAL   A  1 368  ? -52.929 52.585  82.746  1.00 18.17 ? 366  VAL   A CG1   1 
ATOM   2563  C  CG2   . VAL   A  1 368  ? -55.135 53.526  82.032  1.00 18.08 ? 366  VAL   A CG2   1 
ATOM   2564  N  N     . ARG   A  1 369  ? -50.990 52.863  79.729  1.00 16.75 ? 367  ARG   A N     1 
ATOM   2565  C  CA    . ARG   A  1 369  ? -49.805 52.083  79.402  1.00 17.22 ? 367  ARG   A CA    1 
ATOM   2566  C  C     . ARG   A  1 369  ? -49.142 51.682  80.710  1.00 16.72 ? 367  ARG   A C     1 
ATOM   2567  O  O     . ARG   A  1 369  ? -48.648 52.536  81.449  1.00 17.90 ? 367  ARG   A O     1 
ATOM   2568  C  CB    . ARG   A  1 369  ? -48.825 52.853  78.520  1.00 18.31 ? 367  ARG   A CB    1 
ATOM   2569  C  CG    . ARG   A  1 369  ? -47.613 51.989  78.145  1.00 19.72 ? 367  ARG   A CG    1 
ATOM   2570  C  CD    . ARG   A  1 369  ? -46.462 52.829  77.623  1.00 19.94 ? 367  ARG   A CD    1 
ATOM   2571  N  NE    . ARG   A  1 369  ? -46.819 53.537  76.403  1.00 20.23 ? 367  ARG   A NE    1 
ATOM   2572  C  CZ    . ARG   A  1 369  ? -46.247 54.661  75.992  1.00 21.59 ? 367  ARG   A CZ    1 
ATOM   2573  N  NH1   . ARG   A  1 369  ? -45.296 55.258  76.704  1.00 20.39 ? 367  ARG   A NH1   1 
ATOM   2574  N  NH2   . ARG   A  1 369  ? -46.641 55.204  74.841  1.00 17.98 ? 367  ARG   A NH2   1 
ATOM   2575  N  N     . LEU   A  1 370  ? -49.130 50.387  80.990  1.00 16.95 ? 368  LEU   A N     1 
ATOM   2576  C  CA    . LEU   A  1 370  ? -48.440 49.862  82.155  1.00 17.78 ? 368  LEU   A CA    1 
ATOM   2577  C  C     . LEU   A  1 370  ? -47.003 49.553  81.757  1.00 17.33 ? 368  LEU   A C     1 
ATOM   2578  O  O     . LEU   A  1 370  ? -46.770 48.764  80.841  1.00 17.12 ? 368  LEU   A O     1 
ATOM   2579  C  CB    . LEU   A  1 370  ? -49.122 48.606  82.677  1.00 18.56 ? 368  LEU   A CB    1 
ATOM   2580  C  CG    . LEU   A  1 370  ? -48.501 48.056  83.950  1.00 18.48 ? 368  LEU   A CG    1 
ATOM   2581  C  CD1   . LEU   A  1 370  ? -48.677 49.065  85.103  1.00 20.04 ? 368  LEU   A CD1   1 
ATOM   2582  C  CD2   . LEU   A  1 370  ? -49.124 46.692  84.295  1.00 17.75 ? 368  LEU   A CD2   1 
ATOM   2583  N  N     . VAL   A  1 371  ? -46.053 50.176  82.442  1.00 16.67 ? 369  VAL   A N     1 
ATOM   2584  C  CA    . VAL   A  1 371  ? -44.636 49.950  82.199  1.00 16.59 ? 369  VAL   A CA    1 
ATOM   2585  C  C     . VAL   A  1 371  ? -44.014 49.577  83.529  1.00 16.61 ? 369  VAL   A C     1 
ATOM   2586  O  O     . VAL   A  1 371  ? -44.631 49.717  84.586  1.00 18.37 ? 369  VAL   A O     1 
ATOM   2587  C  CB    . VAL   A  1 371  ? -43.925 51.182  81.604  1.00 16.31 ? 369  VAL   A CB    1 
ATOM   2588  C  CG1   . VAL   A  1 371  ? -44.638 51.670  80.357  1.00 16.99 ? 369  VAL   A CG1   1 
ATOM   2589  C  CG2   . VAL   A  1 371  ? -43.858 52.278  82.639  1.00 19.58 ? 369  VAL   A CG2   1 
ATOM   2590  N  N     . LYS   A  1 372  ? -42.779 49.075  83.473  1.00 16.86 ? 370  LYS   A N     1 
ATOM   2591  C  CA    . LYS   A  1 372  ? -42.059 48.912  84.727  1.00 16.59 ? 370  LYS   A CA    1 
ATOM   2592  C  C     . LYS   A  1 372  ? -41.457 50.243  85.173  1.00 17.29 ? 370  LYS   A C     1 
ATOM   2593  O  O     . LYS   A  1 372  ? -41.881 50.809  86.186  1.00 17.30 ? 370  LYS   A O     1 
ATOM   2594  C  CB    . LYS   A  1 372  ? -41.035 47.780  84.595  1.00 19.44 ? 370  LYS   A CB    1 
ATOM   2595  C  CG    . LYS   A  1 372  ? -41.805 46.459  84.408  1.00 17.74 ? 370  LYS   A CG    1 
ATOM   2596  C  CD    . LYS   A  1 372  ? -40.970 45.184  84.410  1.00 17.33 ? 370  LYS   A CD    1 
ATOM   2597  C  CE    . LYS   A  1 372  ? -41.885 43.984  84.066  1.00 22.44 ? 370  LYS   A CE    1 
ATOM   2598  N  NZ    . LYS   A  1 372  ? -41.114 42.735  83.785  1.00 21.89 ? 370  LYS   A NZ    1 
ATOM   2599  N  N     . GLY   A  1 373  ? -40.541 50.802  84.405  1.00 16.20 ? 371  GLY   A N     1 
ATOM   2600  C  CA    . GLY   A  1 373  ? -40.099 52.168  84.650  1.00 15.86 ? 371  GLY   A CA    1 
ATOM   2601  C  C     . GLY   A  1 373  ? -38.667 52.373  84.192  1.00 16.43 ? 371  GLY   A C     1 
ATOM   2602  O  O     . GLY   A  1 373  ? -37.834 51.486  84.275  1.00 17.63 ? 371  GLY   A O     1 
ATOM   2603  N  N     . ALA   A  1 374  ? -38.383 53.588  83.718  1.00 17.44 ? 372  ALA   A N     1 
ATOM   2604  C  CA    . ALA   A  1 374  ? -37.128 53.861  83.027  1.00 18.15 ? 372  ALA   A CA    1 
ATOM   2605  C  C     . ALA   A  1 374  ? -36.116 54.645  83.848  1.00 19.36 ? 372  ALA   A C     1 
ATOM   2606  O  O     . ALA   A  1 374  ? -34.995 54.859  83.369  1.00 20.53 ? 372  ALA   A O     1 
ATOM   2607  C  CB    . ALA   A  1 374  ? -37.394 54.627  81.716  1.00 16.90 ? 372  ALA   A CB    1 
ATOM   2608  N  N     . TYR   A  1 375  ? -36.456 55.084  85.052  1.00 15.55 ? 373  TYR   A N     1 
ATOM   2609  C  CA    . TYR   A  1 375  ? -35.608 56.019  85.783  1.00 16.32 ? 373  TYR   A CA    1 
ATOM   2610  C  C     . TYR   A  1 375  ? -35.049 55.419  87.068  1.00 15.33 ? 373  TYR   A C     1 
ATOM   2611  O  O     . TYR   A  1 375  ? -34.752 56.159  88.008  1.00 18.10 ? 373  TYR   A O     1 
ATOM   2612  C  CB    . TYR   A  1 375  ? -36.368 57.305  86.120  1.00 18.32 ? 373  TYR   A CB    1 
ATOM   2613  C  CG    . TYR   A  1 375  ? -36.942 57.999  84.909  1.00 16.84 ? 373  TYR   A CG    1 
ATOM   2614  C  CD1   . TYR   A  1 375  ? -38.137 57.569  84.348  1.00 18.70 ? 373  TYR   A CD1   1 
ATOM   2615  C  CD2   . TYR   A  1 375  ? -36.286 59.069  84.324  1.00 19.07 ? 373  TYR   A CD2   1 
ATOM   2616  C  CE1   . TYR   A  1 375  ? -38.663 58.189  83.233  1.00 17.18 ? 373  TYR   A CE1   1 
ATOM   2617  C  CE2   . TYR   A  1 375  ? -36.811 59.701  83.207  1.00 20.88 ? 373  TYR   A CE2   1 
ATOM   2618  C  CZ    . TYR   A  1 375  ? -37.993 59.256  82.670  1.00 22.32 ? 373  TYR   A CZ    1 
ATOM   2619  O  OH    . TYR   A  1 375  ? -38.520 59.884  81.561  1.00 23.69 ? 373  TYR   A OH    1 
ATOM   2620  N  N     . TRP   A  1 376  ? -34.866 54.096  87.119  1.00 15.63 ? 374  TRP   A N     1 
ATOM   2621  C  CA    . TRP   A  1 376  ? -34.632 53.449  88.411  1.00 18.45 ? 374  TRP   A CA    1 
ATOM   2622  C  C     . TRP   A  1 376  ? -33.376 53.981  89.095  1.00 20.44 ? 374  TRP   A C     1 
ATOM   2623  O  O     . TRP   A  1 376  ? -33.420 54.375  90.267  1.00 18.55 ? 374  TRP   A O     1 
ATOM   2624  C  CB    . TRP   A  1 376  ? -34.544 51.933  88.251  1.00 17.23 ? 374  TRP   A CB    1 
ATOM   2625  C  CG    . TRP   A  1 376  ? -34.406 51.252  89.569  1.00 19.54 ? 374  TRP   A CG    1 
ATOM   2626  C  CD1   . TRP   A  1 376  ? -35.411 50.973  90.452  1.00 19.11 ? 374  TRP   A CD1   1 
ATOM   2627  C  CD2   . TRP   A  1 376  ? -33.194 50.795  90.183  1.00 20.99 ? 374  TRP   A CD2   1 
ATOM   2628  N  NE1   . TRP   A  1 376  ? -34.901 50.361  91.574  1.00 16.81 ? 374  TRP   A NE1   1 
ATOM   2629  C  CE2   . TRP   A  1 376  ? -33.544 50.231  91.431  1.00 20.26 ? 374  TRP   A CE2   1 
ATOM   2630  C  CE3   . TRP   A  1 376  ? -31.850 50.787  89.792  1.00 23.55 ? 374  TRP   A CE3   1 
ATOM   2631  C  CZ2   . TRP   A  1 376  ? -32.595 49.671  92.297  1.00 18.57 ? 374  TRP   A CZ2   1 
ATOM   2632  C  CZ3   . TRP   A  1 376  ? -30.906 50.240  90.658  1.00 24.06 ? 374  TRP   A CZ3   1 
ATOM   2633  C  CH2   . TRP   A  1 376  ? -31.286 49.692  91.894  1.00 24.25 ? 374  TRP   A CH2   1 
ATOM   2634  N  N     . ASP   A  1 377  ? -32.241 53.976  88.380  1.00 18.94 ? 375  ASP   A N     1 
ATOM   2635  C  CA    . ASP   A  1 377  ? -30.977 54.452  88.948  1.00 22.83 ? 375  ASP   A CA    1 
ATOM   2636  C  C     . ASP   A  1 377  ? -31.108 55.864  89.480  1.00 20.18 ? 375  ASP   A C     1 
ATOM   2637  O  O     . ASP   A  1 377  ? -30.599 56.189  90.562  1.00 19.87 ? 375  ASP   A O     1 
ATOM   2638  C  CB    . ASP   A  1 377  ? -29.872 54.426  87.883  1.00 24.74 ? 375  ASP   A CB    1 
ATOM   2639  C  CG    . ASP   A  1 377  ? -29.382 53.041  87.593  1.00 36.05 ? 375  ASP   A CG    1 
ATOM   2640  O  OD1   . ASP   A  1 377  ? -29.208 52.281  88.558  1.00 40.07 ? 375  ASP   A OD1   1 
ATOM   2641  O  OD2   . ASP   A  1 377  ? -29.162 52.716  86.406  1.00 42.99 ? 375  ASP   A OD2   1 
ATOM   2642  N  N     . ALA   A  1 378  ? -31.770 56.727  88.716  1.00 19.87 ? 376  ALA   A N     1 
ATOM   2643  C  CA    . ALA   A  1 378  ? -31.886 58.118  89.121  1.00 19.56 ? 376  ALA   A CA    1 
ATOM   2644  C  C     . ALA   A  1 378  ? -32.744 58.251  90.369  1.00 18.00 ? 376  ALA   A C     1 
ATOM   2645  O  O     . ALA   A  1 378  ? -32.480 59.112  91.219  1.00 18.12 ? 376  ALA   A O     1 
ATOM   2646  C  CB    . ALA   A  1 378  ? -32.454 58.952  87.967  1.00 17.77 ? 376  ALA   A CB    1 
ATOM   2647  N  N     . GLU   A  1 379  ? -33.781 57.412  90.497  1.00 16.39 ? 377  GLU   A N     1 
ATOM   2648  C  CA    . GLU   A  1 379  ? -34.639 57.503  91.676  1.00 16.23 ? 377  GLU   A CA    1 
ATOM   2649  C  C     . GLU   A  1 379  ? -33.894 57.063  92.927  1.00 18.08 ? 377  GLU   A C     1 
ATOM   2650  O  O     . GLU   A  1 379  ? -34.055 57.669  93.995  1.00 18.32 ? 377  GLU   A O     1 
ATOM   2651  C  CB    . GLU   A  1 379  ? -35.907 56.668  91.488  1.00 19.81 ? 377  GLU   A CB    1 
ATOM   2652  C  CG    . GLU   A  1 379  ? -36.748 57.071  90.257  1.00 17.59 ? 377  GLU   A CG    1 
ATOM   2653  C  CD    . GLU   A  1 379  ? -37.420 58.435  90.384  1.00 16.71 ? 377  GLU   A CD    1 
ATOM   2654  O  OE1   . GLU   A  1 379  ? -37.283 59.120  91.432  1.00 19.47 ? 377  GLU   A OE1   1 
ATOM   2655  O  OE2   . GLU   A  1 379  ? -38.124 58.813  89.427  1.00 16.77 ? 377  GLU   A OE2   1 
ATOM   2656  N  N     . ILE   A  1 380  ? -33.083 56.009  92.821  1.00 15.54 ? 378  ILE   A N     1 
ATOM   2657  C  CA    . ILE   A  1 380  ? -32.305 55.571  93.980  1.00 16.66 ? 378  ILE   A CA    1 
ATOM   2658  C  C     . ILE   A  1 380  ? -31.382 56.693  94.436  1.00 17.22 ? 378  ILE   A C     1 
ATOM   2659  O  O     . ILE   A  1 380  ? -31.343 57.047  95.619  1.00 18.71 ? 378  ILE   A O     1 
ATOM   2660  C  CB    . ILE   A  1 380  ? -31.512 54.292  93.658  1.00 15.48 ? 378  ILE   A CB    1 
ATOM   2661  C  CG1   . ILE   A  1 380  ? -32.444 53.166  93.207  1.00 17.80 ? 378  ILE   A CG1   1 
ATOM   2662  C  CG2   . ILE   A  1 380  ? -30.674 53.870  94.883  1.00 18.36 ? 378  ILE   A CG2   1 
ATOM   2663  C  CD1   . ILE   A  1 380  ? -33.513 52.785  94.228  1.00 19.93 ? 378  ILE   A CD1   1 
ATOM   2664  N  N     . LYS   A  1 381  ? -30.636 57.278  93.490  1.00 15.85 ? 379  LYS   A N     1 
ATOM   2665  C  CA    . LYS   A  1 381  ? -29.686 58.331  93.831  1.00 18.52 ? 379  LYS   A CA    1 
ATOM   2666  C  C     . LYS   A  1 381  ? -30.396 59.531  94.427  1.00 18.22 ? 379  LYS   A C     1 
ATOM   2667  O  O     . LYS   A  1 381  ? -29.944 60.099  95.426  1.00 15.55 ? 379  LYS   A O     1 
ATOM   2668  C  CB    . LYS   A  1 381  ? -28.889 58.750  92.595  1.00 15.55 ? 379  LYS   A CB    1 
ATOM   2669  C  CG    . LYS   A  1 381  ? -27.981 59.969  92.832  1.00 17.62 ? 379  LYS   A CG    1 
ATOM   2670  C  CD    . LYS   A  1 381  ? -27.078 60.212  91.617  1.00 18.19 ? 379  LYS   A CD    1 
ATOM   2671  C  CE    . LYS   A  1 381  ? -26.057 61.334  91.858  1.00 19.51 ? 379  LYS   A CE    1 
ATOM   2672  N  NZ    . LYS   A  1 381  ? -25.163 61.522  90.657  1.00 17.63 ? 379  LYS   A NZ    1 
ATOM   2673  N  N     . ARG   A  1 382  ? -31.524 59.921  93.837  1.00 18.14 ? 380  ARG   A N     1 
ATOM   2674  C  CA    . ARG   A  1 382  ? -32.199 61.130  94.287  1.00 18.04 ? 380  ARG   A CA    1 
ATOM   2675  C  C     . ARG   A  1 382  ? -32.692 60.984  95.718  1.00 18.28 ? 380  ARG   A C     1 
ATOM   2676  O  O     . ARG   A  1 382  ? -32.546 61.903  96.535  1.00 17.90 ? 380  ARG   A O     1 
ATOM   2677  C  CB    . ARG   A  1 382  ? -33.364 61.451  93.345  1.00 18.77 ? 380  ARG   A CB    1 
ATOM   2678  C  CG    . ARG   A  1 382  ? -34.019 62.776  93.634  1.00 24.73 ? 380  ARG   A CG    1 
ATOM   2679  C  CD    . ARG   A  1 382  ? -33.175 63.915  93.094  1.00 37.37 ? 380  ARG   A CD    1 
ATOM   2680  N  NE    . ARG   A  1 382  ? -32.571 64.694  94.167  1.00 39.11 ? 380  ARG   A NE    1 
ATOM   2681  C  CZ    . ARG   A  1 382  ? -31.542 65.518  94.014  1.00 42.98 ? 380  ARG   A CZ    1 
ATOM   2682  N  NH1   . ARG   A  1 382  ? -30.965 65.692  92.833  1.00 45.33 ? 380  ARG   A NH1   1 
ATOM   2683  N  NH2   . ARG   A  1 382  ? -31.079 66.183  95.073  1.00 35.02 ? 380  ARG   A NH2   1 
ATOM   2684  N  N     . ALA   A  1 383  ? -33.302 59.839  96.035  1.00 17.18 ? 381  ALA   A N     1 
ATOM   2685  C  CA    . ALA   A  1 383  ? -33.818 59.630  97.385  1.00 16.31 ? 381  ALA   A CA    1 
ATOM   2686  C  C     . ALA   A  1 383  ? -32.689 59.613  98.402  1.00 15.33 ? 381  ALA   A C     1 
ATOM   2687  O  O     . ALA   A  1 383  ? -32.844 60.117  99.521  1.00 16.52 ? 381  ALA   A O     1 
ATOM   2688  C  CB    . ALA   A  1 383  ? -34.613 58.324  97.454  1.00 16.38 ? 381  ALA   A CB    1 
ATOM   2689  N  N     . GLN   A  1 384  ? -31.539 59.045  98.030  1.00 15.36 ? 382  GLN   A N     1 
ATOM   2690  C  CA    . GLN   A  1 384  ? -30.395 59.064  98.942  1.00 15.36 ? 382  GLN   A CA    1 
ATOM   2691  C  C     . GLN   A  1 384  ? -29.892 60.484  99.146  1.00 16.84 ? 382  GLN   A C     1 
ATOM   2692  O  O     . GLN   A  1 384  ? -29.689 60.922  100.286 1.00 19.51 ? 382  GLN   A O     1 
ATOM   2693  C  CB    . GLN   A  1 384  ? -29.278 58.162  98.407  1.00 16.05 ? 382  GLN   A CB    1 
ATOM   2694  C  CG    . GLN   A  1 384  ? -29.636 56.686  98.513  1.00 16.27 ? 382  GLN   A CG    1 
ATOM   2695  C  CD    . GLN   A  1 384  ? -28.535 55.783  98.011  1.00 18.08 ? 382  GLN   A CD    1 
ATOM   2696  O  OE1   . GLN   A  1 384  ? -27.701 56.195  97.207  1.00 20.35 ? 382  GLN   A OE1   1 
ATOM   2697  N  NE2   . GLN   A  1 384  ? -28.540 54.540  98.472  1.00 19.08 ? 382  GLN   A NE2   1 
ATOM   2698  N  N     . LEU   A  1 385  ? -29.718 61.235  98.052  1.00 16.41 ? 383  LEU   A N     1 
ATOM   2699  C  CA    . LEU   A  1 385  ? -29.264 62.619  98.178  1.00 18.23 ? 383  LEU   A CA    1 
ATOM   2700  C  C     . LEU   A  1 385  ? -30.203 63.432  99.056  1.00 20.26 ? 383  LEU   A C     1 
ATOM   2701  O  O     . LEU   A  1 385  ? -29.757 64.258  99.860  1.00 19.01 ? 383  LEU   A O     1 
ATOM   2702  C  CB    . LEU   A  1 385  ? -29.152 63.271  96.801  1.00 19.24 ? 383  LEU   A CB    1 
ATOM   2703  C  CG    . LEU   A  1 385  ? -27.965 62.851  95.935  1.00 19.42 ? 383  LEU   A CG    1 
ATOM   2704  C  CD1   . LEU   A  1 385  ? -28.114 63.491  94.569  1.00 21.61 ? 383  LEU   A CD1   1 
ATOM   2705  C  CD2   . LEU   A  1 385  ? -26.680 63.283  96.580  1.00 22.31 ? 383  LEU   A CD2   1 
ATOM   2706  N  N     . ASP   A  1 386  ? -31.505 63.215  98.917  1.00 17.97 ? 384  ASP   A N     1 
ATOM   2707  C  CA    . ASP   A  1 386  ? -32.479 64.037  99.619  1.00 16.51 ? 384  ASP   A CA    1 
ATOM   2708  C  C     . ASP   A  1 386  ? -32.775 63.545  101.029 1.00 18.76 ? 384  ASP   A C     1 
ATOM   2709  O  O     . ASP   A  1 386  ? -33.592 64.165  101.727 1.00 17.83 ? 384  ASP   A O     1 
ATOM   2710  C  CB    . ASP   A  1 386  ? -33.767 64.114  98.794  1.00 19.67 ? 384  ASP   A CB    1 
ATOM   2711  C  CG    . ASP   A  1 386  ? -33.595 64.947  97.532  1.00 25.56 ? 384  ASP   A CG    1 
ATOM   2712  O  OD1   . ASP   A  1 386  ? -32.576 65.659  97.429  1.00 28.35 ? 384  ASP   A OD1   1 
ATOM   2713  O  OD2   . ASP   A  1 386  ? -34.469 64.893  96.645  1.00 23.42 ? 384  ASP   A OD2   1 
ATOM   2714  N  N     . GLY   A  1 387  ? -32.131 62.466  101.467 1.00 17.27 ? 385  GLY   A N     1 
ATOM   2715  C  CA    . GLY   A  1 387  ? -32.332 61.975  102.827 1.00 16.71 ? 385  GLY   A CA    1 
ATOM   2716  C  C     . GLY   A  1 387  ? -33.771 61.629  103.140 1.00 18.11 ? 385  GLY   A C     1 
ATOM   2717  O  O     . GLY   A  1 387  ? -34.246 61.891  104.254 1.00 20.22 ? 385  GLY   A O     1 
ATOM   2718  N  N     . LEU   A  1 388  ? -34.477 61.033  102.187 1.00 17.67 ? 386  LEU   A N     1 
ATOM   2719  C  CA    . LEU   A  1 388  ? -35.897 60.784  102.381 1.00 18.60 ? 386  LEU   A CA    1 
ATOM   2720  C  C     . LEU   A  1 388  ? -36.116 59.422  103.026 1.00 20.73 ? 386  LEU   A C     1 
ATOM   2721  O  O     . LEU   A  1 388  ? -35.204 58.603  103.143 1.00 20.16 ? 386  LEU   A O     1 
ATOM   2722  C  CB    . LEU   A  1 388  ? -36.640 60.918  101.052 1.00 17.35 ? 386  LEU   A CB    1 
ATOM   2723  C  CG    . LEU   A  1 388  ? -36.466 62.345  100.497 1.00 20.09 ? 386  LEU   A CG    1 
ATOM   2724  C  CD1   . LEU   A  1 388  ? -37.210 62.553  99.173  1.00 17.84 ? 386  LEU   A CD1   1 
ATOM   2725  C  CD2   . LEU   A  1 388  ? -36.870 63.425  101.505 1.00 22.11 ? 386  LEU   A CD2   1 
ATOM   2726  N  N     . ALA   A  1 389  ? -37.349 59.205  103.493 1.00 19.95 ? 387  ALA   A N     1 
ATOM   2727  C  CA    . ALA   A  1 389  ? -37.619 58.066  104.357 1.00 22.54 ? 387  ALA   A CA    1 
ATOM   2728  C  C     . ALA   A  1 389  ? -37.349 56.744  103.652 1.00 22.22 ? 387  ALA   A C     1 
ATOM   2729  O  O     . ALA   A  1 389  ? -36.911 55.774  104.277 1.00 22.44 ? 387  ALA   A O     1 
ATOM   2730  C  CB    . ALA   A  1 389  ? -39.071 58.137  104.837 1.00 21.33 ? 387  ALA   A CB    1 
ATOM   2731  N  N     . ASP   A  1 390  ? -37.578 56.691  102.353 1.00 20.40 ? 388  ASP   A N     1 
ATOM   2732  C  CA    . ASP   A  1 390  ? -37.501 55.444  101.606 1.00 20.17 ? 388  ASP   A CA    1 
ATOM   2733  C  C     . ASP   A  1 390  ? -37.520 55.827  100.136 1.00 18.75 ? 388  ASP   A C     1 
ATOM   2734  O  O     . ASP   A  1 390  ? -37.583 57.009  99.785  1.00 19.33 ? 388  ASP   A O     1 
ATOM   2735  C  CB    . ASP   A  1 390  ? -38.657 54.508  101.979 1.00 19.63 ? 388  ASP   A CB    1 
ATOM   2736  C  CG    . ASP   A  1 390  ? -38.314 53.034  101.793 1.00 25.28 ? 388  ASP   A CG    1 
ATOM   2737  O  OD1   . ASP   A  1 390  ? -37.558 52.701  100.856 1.00 22.94 ? 388  ASP   A OD1   1 
ATOM   2738  O  OD2   . ASP   A  1 390  ? -38.802 52.195  102.593 1.00 26.85 ? 388  ASP   A OD2   1 
ATOM   2739  N  N     . PHE   A  1 391  ? -37.432 54.847  99.302  1.00 18.35 ? 389  PHE   A N     1 
ATOM   2740  C  CA    . PHE   A  1 391  ? -37.472 55.071  97.873  1.00 18.97 ? 389  PHE   A CA    1 
ATOM   2741  C  C     . PHE   A  1 391  ? -38.913 55.079  97.387  1.00 19.13 ? 389  PHE   A C     1 
ATOM   2742  O  O     . PHE   A  1 391  ? -39.789 54.475  98.014  1.00 19.44 ? 389  PHE   A O     1 
ATOM   2743  C  CB    . PHE   A  1 391  ? -36.684 53.984  97.149  1.00 18.53 ? 389  PHE   A CB    1 
ATOM   2744  C  CG    . PHE   A  1 391  ? -35.268 53.890  97.618  1.00 17.81 ? 389  PHE   A CG    1 
ATOM   2745  C  CD1   . PHE   A  1 391  ? -34.323 54.800  97.161  1.00 16.86 ? 389  PHE   A CD1   1 
ATOM   2746  C  CD2   . PHE   A  1 391  ? -34.888 52.928  98.551  1.00 18.62 ? 389  PHE   A CD2   1 
ATOM   2747  C  CE1   . PHE   A  1 391  ? -33.005 54.746  97.612  1.00 19.63 ? 389  PHE   A CE1   1 
ATOM   2748  C  CE2   . PHE   A  1 391  ? -33.575 52.869  99.012  1.00 17.47 ? 389  PHE   A CE2   1 
ATOM   2749  C  CZ    . PHE   A  1 391  ? -32.638 53.773  98.534  1.00 18.11 ? 389  PHE   A CZ    1 
ATOM   2750  N  N     . PRO   A  1 392  ? -39.168 55.809  96.302  1.00 18.58 ? 390  PRO   A N     1 
ATOM   2751  C  CA    . PRO   A  1 392  ? -40.488 55.781  95.661  1.00 18.45 ? 390  PRO   A CA    1 
ATOM   2752  C  C     . PRO   A  1 392  ? -40.613 54.672  94.633  1.00 16.98 ? 390  PRO   A C     1 
ATOM   2753  O  O     . PRO   A  1 392  ? -41.649 54.582  93.968  1.00 18.00 ? 390  PRO   A O     1 
ATOM   2754  C  CB    . PRO   A  1 392  ? -40.561 57.155  94.985  1.00 15.69 ? 390  PRO   A CB    1 
ATOM   2755  C  CG    . PRO   A  1 392  ? -39.099 57.393  94.552  1.00 16.59 ? 390  PRO   A CG    1 
ATOM   2756  C  CD    . PRO   A  1 392  ? -38.250 56.776  95.667  1.00 15.90 ? 390  PRO   A CD    1 
ATOM   2757  N  N     . VAL   A  1 393  ? -39.575 53.847  94.500  1.00 18.05 ? 391  VAL   A N     1 
ATOM   2758  C  CA    . VAL   A  1 393  ? -39.570 52.696  93.616  1.00 16.41 ? 391  VAL   A CA    1 
ATOM   2759  C  C     . VAL   A  1 393  ? -39.096 51.502  94.426  1.00 19.10 ? 391  VAL   A C     1 
ATOM   2760  O  O     . VAL   A  1 393  ? -38.466 51.645  95.474  1.00 17.85 ? 391  VAL   A O     1 
ATOM   2761  C  CB    . VAL   A  1 393  ? -38.658 52.883  92.380  1.00 17.97 ? 391  VAL   A CB    1 
ATOM   2762  C  CG1   . VAL   A  1 393  ? -39.228 53.936  91.423  1.00 17.95 ? 391  VAL   A CG1   1 
ATOM   2763  C  CG2   . VAL   A  1 393  ? -37.239 53.267  92.832  1.00 16.18 ? 391  VAL   A CG2   1 
ATOM   2764  N  N     . PHE   A  1 394  ? -39.391 50.316  93.914  1.00 17.46 ? 392  PHE   A N     1 
ATOM   2765  C  CA    . PHE   A  1 394  ? -38.867 49.110  94.525  1.00 18.10 ? 392  PHE   A CA    1 
ATOM   2766  C  C     . PHE   A  1 394  ? -37.363 49.043  94.306  1.00 18.73 ? 392  PHE   A C     1 
ATOM   2767  O  O     . PHE   A  1 394  ? -36.815 49.713  93.434  1.00 19.51 ? 392  PHE   A O     1 
ATOM   2768  C  CB    . PHE   A  1 394  ? -39.583 47.890  93.951  1.00 18.50 ? 392  PHE   A CB    1 
ATOM   2769  C  CG    . PHE   A  1 394  ? -41.065 47.948  94.162  1.00 17.20 ? 392  PHE   A CG    1 
ATOM   2770  C  CD1   . PHE   A  1 394  ? -41.587 47.895  95.449  1.00 19.65 ? 392  PHE   A CD1   1 
ATOM   2771  C  CD2   . PHE   A  1 394  ? -41.923 48.148  93.098  1.00 19.06 ? 392  PHE   A CD2   1 
ATOM   2772  C  CE1   . PHE   A  1 394  ? -42.937 47.997  95.668  1.00 18.02 ? 392  PHE   A CE1   1 
ATOM   2773  C  CE2   . PHE   A  1 394  ? -43.285 48.254  93.307  1.00 19.50 ? 392  PHE   A CE2   1 
ATOM   2774  C  CZ    . PHE   A  1 394  ? -43.791 48.169  94.595  1.00 18.54 ? 392  PHE   A CZ    1 
ATOM   2775  N  N     . THR   A  1 395  ? -36.683 48.245  95.133  1.00 20.09 ? 393  THR   A N     1 
ATOM   2776  C  CA    . THR   A  1 395  ? -35.239 48.093  95.000  1.00 19.26 ? 393  THR   A CA    1 
ATOM   2777  C  C     . THR   A  1 395  ? -34.812 46.703  94.555  1.00 19.36 ? 393  THR   A C     1 
ATOM   2778  O  O     . THR   A  1 395  ? -33.625 46.499  94.283  1.00 20.28 ? 393  THR   A O     1 
ATOM   2779  C  CB    . THR   A  1 395  ? -34.523 48.426  96.315  1.00 20.39 ? 393  THR   A CB    1 
ATOM   2780  O  OG1   . THR   A  1 395  ? -34.952 47.512  97.326  1.00 20.45 ? 393  THR   A OG1   1 
ATOM   2781  C  CG2   . THR   A  1 395  ? -34.836 49.852  96.746  1.00 21.57 ? 393  THR   A CG2   1 
ATOM   2782  N  N     . ARG   A  1 396  ? -35.729 45.748  94.486  1.00 20.23 ? 394  ARG   A N     1 
ATOM   2783  C  CA    . ARG   A  1 396  ? -35.468 44.448  93.884  1.00 23.76 ? 394  ARG   A CA    1 
ATOM   2784  C  C     . ARG   A  1 396  ? -36.269 44.338  92.599  1.00 23.18 ? 394  ARG   A C     1 
ATOM   2785  O  O     . ARG   A  1 396  ? -37.475 44.599  92.597  1.00 24.22 ? 394  ARG   A O     1 
ATOM   2786  C  CB    . ARG   A  1 396  ? -35.846 43.309  94.830  1.00 23.44 ? 394  ARG   A CB    1 
ATOM   2787  C  CG    . ARG   A  1 396  ? -34.976 43.215  96.053  1.00 26.40 ? 394  ARG   A CG    1 
ATOM   2788  C  CD    . ARG   A  1 396  ? -35.314 41.976  96.861  1.00 26.30 ? 394  ARG   A CD    1 
ATOM   2789  N  NE    . ARG   A  1 396  ? -34.651 42.019  98.158  1.00 32.42 ? 394  ARG   A NE    1 
ATOM   2790  C  CZ    . ARG   A  1 396  ? -33.858 41.066  98.632  1.00 41.97 ? 394  ARG   A CZ    1 
ATOM   2791  N  NH1   . ARG   A  1 396  ? -33.650 39.943  97.960  1.00 47.76 ? 394  ARG   A NH1   1 
ATOM   2792  N  NH2   . ARG   A  1 396  ? -33.267 41.240  99.813  1.00 35.34 ? 394  ARG   A NH2   1 
ATOM   2793  N  N     . LYS   A  1 397  ? -35.597 43.945  91.516  1.00 20.17 ? 395  LYS   A N     1 
ATOM   2794  C  CA    . LYS   A  1 397  ? -36.263 43.848  90.217  1.00 20.27 ? 395  LYS   A CA    1 
ATOM   2795  C  C     . LYS   A  1 397  ? -37.479 42.936  90.281  1.00 20.07 ? 395  LYS   A C     1 
ATOM   2796  O  O     . LYS   A  1 397  ? -38.517 43.219  89.662  1.00 20.33 ? 395  LYS   A O     1 
ATOM   2797  C  CB    . LYS   A  1 397  ? -35.264 43.352  89.171  1.00 25.10 ? 395  LYS   A CB    1 
ATOM   2798  C  CG    . LYS   A  1 397  ? -35.677 43.584  87.729  1.00 24.70 ? 395  LYS   A CG    1 
ATOM   2799  C  CD    . LYS   A  1 397  ? -36.421 42.394  87.173  1.00 24.33 ? 395  LYS   A CD    1 
ATOM   2800  C  CE    . LYS   A  1 397  ? -36.752 42.596  85.691  1.00 23.53 ? 395  LYS   A CE    1 
ATOM   2801  N  NZ    . LYS   A  1 397  ? -37.484 41.411  85.172  1.00 21.00 ? 395  LYS   A NZ    1 
ATOM   2802  N  N     . ILE   A  1 398  ? -37.375 41.835  91.031  1.00 19.04 ? 396  ILE   A N     1 
ATOM   2803  C  CA    . ILE   A  1 398  ? -38.478 40.890  91.104  1.00 21.78 ? 396  ILE   A CA    1 
ATOM   2804  C  C     . ILE   A  1 398  ? -39.710 41.549  91.720  1.00 18.49 ? 396  ILE   A C     1 
ATOM   2805  O  O     . ILE   A  1 398  ? -40.845 41.183  91.401  1.00 21.42 ? 396  ILE   A O     1 
ATOM   2806  C  CB    . ILE   A  1 398  ? -38.021 39.629  91.879  1.00 20.14 ? 396  ILE   A CB    1 
ATOM   2807  C  CG1   . ILE   A  1 398  ? -39.012 38.493  91.672  1.00 29.66 ? 396  ILE   A CG1   1 
ATOM   2808  C  CG2   . ILE   A  1 398  ? -37.865 39.936  93.349  1.00 23.43 ? 396  ILE   A CG2   1 
ATOM   2809  C  CD1   . ILE   A  1 398  ? -38.393 37.129  91.773  1.00 32.91 ? 396  ILE   A CD1   1 
ATOM   2810  N  N     . HIS   A  1 399  ? -39.510 42.548  92.585  1.00 21.78 ? 397  HIS   A N     1 
ATOM   2811  C  CA    . HIS   A  1 399  ? -40.641 43.269  93.158  1.00 21.26 ? 397  HIS   A CA    1 
ATOM   2812  C  C     . HIS   A  1 399  ? -41.385 44.053  92.086  1.00 20.69 ? 397  HIS   A C     1 
ATOM   2813  O  O     . HIS   A  1 399  ? -42.617 44.031  92.034  1.00 19.87 ? 397  HIS   A O     1 
ATOM   2814  C  CB    . HIS   A  1 399  ? -40.166 44.198  94.278  1.00 22.36 ? 397  HIS   A CB    1 
ATOM   2815  C  CG    . HIS   A  1 399  ? -39.654 43.476  95.483  1.00 22.34 ? 397  HIS   A CG    1 
ATOM   2816  N  ND1   . HIS   A  1 399  ? -39.007 44.122  96.514  1.00 21.20 ? 397  HIS   A ND1   1 
ATOM   2817  C  CD2   . HIS   A  1 399  ? -39.699 42.167  95.827  1.00 25.15 ? 397  HIS   A CD2   1 
ATOM   2818  C  CE1   . HIS   A  1 399  ? -38.663 43.238  97.436  1.00 22.32 ? 397  HIS   A CE1   1 
ATOM   2819  N  NE2   . HIS   A  1 399  ? -39.071 42.045  97.045  1.00 22.49 ? 397  HIS   A NE2   1 
ATOM   2820  N  N     . THR   A  1 400  ? -40.645 44.720  91.203  1.00 19.70 ? 398  THR   A N     1 
ATOM   2821  C  CA    . THR   A  1 400  ? -41.268 45.396  90.074  1.00 19.89 ? 398  THR   A CA    1 
ATOM   2822  C  C     . THR   A  1 400  ? -42.053 44.422  89.207  1.00 20.26 ? 398  THR   A C     1 
ATOM   2823  O  O     . THR   A  1 400  ? -43.155 44.744  88.752  1.00 18.76 ? 398  THR   A O     1 
ATOM   2824  C  CB    . THR   A  1 400  ? -40.199 46.110  89.258  1.00 17.68 ? 398  THR   A CB    1 
ATOM   2825  O  OG1   . THR   A  1 400  ? -39.649 47.153  90.066  1.00 17.10 ? 398  THR   A OG1   1 
ATOM   2826  C  CG2   . THR   A  1 400  ? -40.795 46.696  87.977  1.00 17.52 ? 398  THR   A CG2   1 
ATOM   2827  N  N     . ASP   A  1 401  ? -41.519 43.214  88.986  1.00 20.16 ? 399  ASP   A N     1 
ATOM   2828  C  CA    . ASP   A  1 401  ? -42.250 42.227  88.192  1.00 18.31 ? 399  ASP   A CA    1 
ATOM   2829  C  C     . ASP   A  1 401  ? -43.560 41.837  88.862  1.00 20.29 ? 399  ASP   A C     1 
ATOM   2830  O  O     . ASP   A  1 401  ? -44.592 41.716  88.195  1.00 21.16 ? 399  ASP   A O     1 
ATOM   2831  C  CB    . ASP   A  1 401  ? -41.393 40.983  87.960  1.00 18.58 ? 399  ASP   A CB    1 
ATOM   2832  C  CG    . ASP   A  1 401  ? -40.220 41.237  87.025  1.00 23.24 ? 399  ASP   A CG    1 
ATOM   2833  O  OD1   . ASP   A  1 401  ? -40.266 42.185  86.218  1.00 24.95 ? 399  ASP   A OD1   1 
ATOM   2834  O  OD2   . ASP   A  1 401  ? -39.242 40.477  87.109  1.00 25.21 ? 399  ASP   A OD2   1 
ATOM   2835  N  N     . VAL   A  1 402  ? -43.537 41.607  90.179  1.00 19.07 ? 400  VAL   A N     1 
ATOM   2836  C  CA    . VAL   A  1 402  ? -44.777 41.273  90.881  1.00 19.00 ? 400  VAL   A CA    1 
ATOM   2837  C  C     . VAL   A  1 402  ? -45.735 42.447  90.827  1.00 20.44 ? 400  VAL   A C     1 
ATOM   2838  O  O     . VAL   A  1 402  ? -46.938 42.286  90.574  1.00 20.87 ? 400  VAL   A O     1 
ATOM   2839  C  CB    . VAL   A  1 402  ? -44.482 40.869  92.335  1.00 22.32 ? 400  VAL   A CB    1 
ATOM   2840  C  CG1   . VAL   A  1 402  ? -45.790 40.687  93.096  1.00 20.53 ? 400  VAL   A CG1   1 
ATOM   2841  C  CG2   . VAL   A  1 402  ? -43.639 39.590  92.370  1.00 23.66 ? 400  VAL   A CG2   1 
ATOM   2842  N  N     . SER   A  1 403  ? -45.212 43.649  91.074  1.00 19.03 ? 401  SER   A N     1 
ATOM   2843  C  CA    . SER   A  1 403  ? -46.037 44.845  90.995  1.00 20.13 ? 401  SER   A CA    1 
ATOM   2844  C  C     . SER   A  1 403  ? -46.707 44.941  89.635  1.00 22.78 ? 401  SER   A C     1 
ATOM   2845  O  O     . SER   A  1 403  ? -47.917 45.188  89.539  1.00 18.47 ? 401  SER   A O     1 
ATOM   2846  C  CB    . SER   A  1 403  ? -45.184 46.085  91.263  1.00 17.80 ? 401  SER   A CB    1 
ATOM   2847  O  OG    . SER   A  1 403  ? -45.944 47.262  91.046  1.00 19.11 ? 401  SER   A OG    1 
ATOM   2848  N  N     . TYR   A  1 404  ? -45.929 44.720  88.570  1.00 18.49 ? 402  TYR   A N     1 
ATOM   2849  C  CA    . TYR   A  1 404  ? -46.470 44.799  87.217  1.00 20.12 ? 402  TYR   A CA    1 
ATOM   2850  C  C     . TYR   A  1 404  ? -47.630 43.825  87.034  1.00 18.96 ? 402  TYR   A C     1 
ATOM   2851  O  O     . TYR   A  1 404  ? -48.708 44.204  86.560  1.00 18.39 ? 402  TYR   A O     1 
ATOM   2852  C  CB    . TYR   A  1 404  ? -45.353 44.520  86.212  1.00 19.47 ? 402  TYR   A CB    1 
ATOM   2853  C  CG    . TYR   A  1 404  ? -45.698 44.845  84.779  1.00 18.11 ? 402  TYR   A CG    1 
ATOM   2854  C  CD1   . TYR   A  1 404  ? -46.451 43.962  84.007  1.00 20.09 ? 402  TYR   A CD1   1 
ATOM   2855  C  CD2   . TYR   A  1 404  ? -45.264 46.024  84.194  1.00 18.30 ? 402  TYR   A CD2   1 
ATOM   2856  C  CE1   . TYR   A  1 404  ? -46.767 44.252  82.691  1.00 21.83 ? 402  TYR   A CE1   1 
ATOM   2857  C  CE2   . TYR   A  1 404  ? -45.570 46.322  82.868  1.00 17.69 ? 402  TYR   A CE2   1 
ATOM   2858  C  CZ    . TYR   A  1 404  ? -46.328 45.423  82.127  1.00 18.43 ? 402  TYR   A CZ    1 
ATOM   2859  O  OH    . TYR   A  1 404  ? -46.650 45.712  80.814  1.00 21.74 ? 402  TYR   A OH    1 
ATOM   2860  N  N     . ILE   A  1 405  ? -47.432 42.567  87.431  1.00 19.07 ? 403  ILE   A N     1 
ATOM   2861  C  CA    . ILE   A  1 405  ? -48.469 41.567  87.237  1.00 19.11 ? 403  ILE   A CA    1 
ATOM   2862  C  C     . ILE   A  1 405  ? -49.685 41.894  88.092  1.00 19.82 ? 403  ILE   A C     1 
ATOM   2863  O  O     . ILE   A  1 405  ? -50.824 41.760  87.640  1.00 19.39 ? 403  ILE   A O     1 
ATOM   2864  C  CB    . ILE   A  1 405  ? -47.904 40.165  87.524  1.00 19.47 ? 403  ILE   A CB    1 
ATOM   2865  C  CG1   . ILE   A  1 405  ? -46.807 39.841  86.505  1.00 22.62 ? 403  ILE   A CG1   1 
ATOM   2866  C  CG2   . ILE   A  1 405  ? -48.991 39.117  87.462  1.00 24.22 ? 403  ILE   A CG2   1 
ATOM   2867  C  CD1   . ILE   A  1 405  ? -45.990 38.592  86.840  1.00 26.12 ? 403  ILE   A CD1   1 
ATOM   2868  N  N     . ALA   A  1 406  ? -49.458 42.375  89.320  1.00 19.69 ? 404  ALA   A N     1 
ATOM   2869  C  CA    . ALA   A  1 406  ? -50.564 42.779  90.183  1.00 21.91 ? 404  ALA   A CA    1 
ATOM   2870  C  C     . ALA   A  1 406  ? -51.361 43.917  89.560  1.00 21.02 ? 404  ALA   A C     1 
ATOM   2871  O  O     . ALA   A  1 406  ? -52.596 43.936  89.619  1.00 21.39 ? 404  ALA   A O     1 
ATOM   2872  C  CB    . ALA   A  1 406  ? -50.026 43.201  91.548  1.00 21.95 ? 404  ALA   A CB    1 
ATOM   2873  N  N     . CYS   A  1 407  ? -50.669 44.889  88.975  1.00 20.81 ? 405  CYS   A N     1 
ATOM   2874  C  CA    . CYS   A  1 407  ? -51.375 46.015  88.380  1.00 18.71 ? 405  CYS   A CA    1 
ATOM   2875  C  C     . CYS   A  1 407  ? -52.056 45.618  87.080  1.00 20.94 ? 405  CYS   A C     1 
ATOM   2876  O  O     . CYS   A  1 407  ? -53.082 46.203  86.718  1.00 21.20 ? 405  CYS   A O     1 
ATOM   2877  C  CB    . CYS   A  1 407  ? -50.402 47.163  88.149  1.00 18.17 ? 405  CYS   A CB    1 
ATOM   2878  S  SG    . CYS   A  1 407  ? -49.828 47.877  89.696  1.00 24.04 ? 405  CYS   A SG    1 
ATOM   2879  N  N     . ALA   A  1 408  ? -51.489 44.646  86.359  1.00 18.63 ? 406  ALA   A N     1 
ATOM   2880  C  CA    . ALA   A  1 408  ? -52.166 44.122  85.181  1.00 18.80 ? 406  ALA   A CA    1 
ATOM   2881  C  C     . ALA   A  1 408  ? -53.492 43.478  85.564  1.00 19.18 ? 406  ALA   A C     1 
ATOM   2882  O  O     . ALA   A  1 408  ? -54.487 43.621  84.845  1.00 21.66 ? 406  ALA   A O     1 
ATOM   2883  C  CB    . ALA   A  1 408  ? -51.270 43.119  84.453  1.00 21.49 ? 406  ALA   A CB    1 
ATOM   2884  N  N     . ALA   A  1 409  ? -53.525 42.774  86.698  1.00 21.12 ? 407  ALA   A N     1 
ATOM   2885  C  CA    . ALA   A  1 409  ? -54.777 42.182  87.161  1.00 24.78 ? 407  ALA   A CA    1 
ATOM   2886  C  C     . ALA   A  1 409  ? -55.822 43.253  87.428  1.00 25.41 ? 407  ALA   A C     1 
ATOM   2887  O  O     . ALA   A  1 409  ? -57.005 43.069  87.119  1.00 21.48 ? 407  ALA   A O     1 
ATOM   2888  C  CB    . ALA   A  1 409  ? -54.530 41.349  88.417  1.00 24.07 ? 407  ALA   A CB    1 
ATOM   2889  N  N     . LYS   A  1 410  ? -55.405 44.379  88.019  1.00 20.76 ? 408  LYS   A N     1 
ATOM   2890  C  CA    . LYS   A  1 410  ? -56.341 45.468  88.266  1.00 22.49 ? 408  LYS   A CA    1 
ATOM   2891  C  C     . LYS   A  1 410  ? -56.860 46.039  86.959  1.00 23.15 ? 408  LYS   A C     1 
ATOM   2892  O  O     . LYS   A  1 410  ? -58.063 46.312  86.815  1.00 20.92 ? 408  LYS   A O     1 
ATOM   2893  C  CB    . LYS   A  1 410  ? -55.664 46.564  89.087  1.00 21.21 ? 408  LYS   A CB    1 
ATOM   2894  C  CG    . LYS   A  1 410  ? -56.583 47.736  89.424  1.00 23.93 ? 408  LYS   A CG    1 
ATOM   2895  C  CD    . LYS   A  1 410  ? -55.811 48.785  90.209  1.00 25.71 ? 408  LYS   A CD    1 
ATOM   2896  C  CE    . LYS   A  1 410  ? -55.252 48.211  91.501  1.00 23.30 ? 408  LYS   A CE    1 
ATOM   2897  N  NZ    . LYS   A  1 410  ? -56.369 47.992  92.467  1.00 25.11 ? 408  LYS   A NZ    1 
ATOM   2898  N  N     . LEU   A  1 411  ? -55.956 46.238  85.999  1.00 20.05 ? 409  LEU   A N     1 
ATOM   2899  C  CA    . LEU   A  1 411  ? -56.346 46.782  84.708  1.00 18.77 ? 409  LEU   A CA    1 
ATOM   2900  C  C     . LEU   A  1 411  ? -57.279 45.840  83.963  1.00 20.33 ? 409  LEU   A C     1 
ATOM   2901  O  O     . LEU   A  1 411  ? -58.255 46.279  83.338  1.00 21.73 ? 409  LEU   A O     1 
ATOM   2902  C  CB    . LEU   A  1 411  ? -55.098 47.054  83.878  1.00 18.80 ? 409  LEU   A CB    1 
ATOM   2903  C  CG    . LEU   A  1 411  ? -54.360 48.342  84.223  1.00 20.92 ? 409  LEU   A CG    1 
ATOM   2904  C  CD1   . LEU   A  1 411  ? -52.953 48.321  83.593  1.00 20.71 ? 409  LEU   A CD1   1 
ATOM   2905  C  CD2   . LEU   A  1 411  ? -55.152 49.537  83.720  1.00 19.85 ? 409  LEU   A CD2   1 
ATOM   2906  N  N     . LEU   A  1 412  ? -56.964 44.544  83.973  1.00 19.96 ? 410  LEU   A N     1 
ATOM   2907  C  CA    . LEU   A  1 412  ? -57.761 43.585  83.225  1.00 23.80 ? 410  LEU   A CA    1 
ATOM   2908  C  C     . LEU   A  1 412  ? -59.157 43.448  83.793  1.00 23.75 ? 410  LEU   A C     1 
ATOM   2909  O  O     . LEU   A  1 412  ? -60.063 43.010  83.079  1.00 25.87 ? 410  LEU   A O     1 
ATOM   2910  C  CB    . LEU   A  1 412  ? -57.067 42.223  83.201  1.00 22.26 ? 410  LEU   A CB    1 
ATOM   2911  C  CG    . LEU   A  1 412  ? -55.863 42.181  82.253  1.00 22.57 ? 410  LEU   A CG    1 
ATOM   2912  C  CD1   . LEU   A  1 412  ? -55.123 40.853  82.367  1.00 26.24 ? 410  LEU   A CD1   1 
ATOM   2913  C  CD2   . LEU   A  1 412  ? -56.279 42.433  80.813  1.00 25.33 ? 410  LEU   A CD2   1 
ATOM   2914  N  N     . ALA   A  1 413  ? -59.349 43.826  85.047  1.00 20.27 ? 411  ALA   A N     1 
ATOM   2915  C  CA    . ALA   A  1 413  ? -60.681 43.860  85.629  1.00 23.57 ? 411  ALA   A CA    1 
ATOM   2916  C  C     . ALA   A  1 413  ? -61.445 45.122  85.271  1.00 26.92 ? 411  ALA   A C     1 
ATOM   2917  O  O     . ALA   A  1 413  ? -62.590 45.263  85.700  1.00 22.33 ? 411  ALA   A O     1 
ATOM   2918  C  CB    . ALA   A  1 413  ? -60.600 43.735  87.152  1.00 25.98 ? 411  ALA   A CB    1 
ATOM   2919  N  N     . ALA   A  1 414  ? -60.847 46.039  84.505  1.00 23.50 ? 412  ALA   A N     1 
ATOM   2920  C  CA    . ALA   A  1 414  ? -61.470 47.329  84.219  1.00 25.52 ? 412  ALA   A CA    1 
ATOM   2921  C  C     . ALA   A  1 414  ? -61.427 47.653  82.730  1.00 22.66 ? 412  ALA   A C     1 
ATOM   2922  O  O     . ALA   A  1 414  ? -61.446 48.827  82.348  1.00 22.06 ? 412  ALA   A O     1 
ATOM   2923  C  CB    . ALA   A  1 414  ? -60.799 48.447  85.027  1.00 22.81 ? 412  ALA   A CB    1 
ATOM   2924  N  N     . THR   A  1 415  ? -61.371 46.627  81.870  1.00 23.29 ? 413  THR   A N     1 
ATOM   2925  C  CA    . THR   A  1 415  ? -61.285 46.879  80.434  1.00 22.52 ? 413  THR   A CA    1 
ATOM   2926  C  C     . THR   A  1 415  ? -62.526 47.568  79.890  1.00 23.40 ? 413  THR   A C     1 
ATOM   2927  O  O     . THR   A  1 415  ? -62.477 48.116  78.789  1.00 21.96 ? 413  THR   A O     1 
ATOM   2928  C  CB    . THR   A  1 415  ? -61.043 45.577  79.653  1.00 27.25 ? 413  THR   A CB    1 
ATOM   2929  O  OG1   . THR   A  1 415  ? -62.112 44.655  79.892  1.00 25.53 ? 413  THR   A OG1   1 
ATOM   2930  C  CG2   . THR   A  1 415  ? -59.718 44.940  80.064  1.00 25.31 ? 413  THR   A CG2   1 
ATOM   2931  N  N     . ASP   A  1 416  ? -63.641 47.557  80.620  1.00 26.31 ? 414  ASP   A N     1 
ATOM   2932  C  CA    . ASP   A  1 416  ? -64.793 48.299  80.121  1.00 30.04 ? 414  ASP   A CA    1 
ATOM   2933  C  C     . ASP   A  1 416  ? -64.583 49.807  80.231  1.00 25.70 ? 414  ASP   A C     1 
ATOM   2934  O  O     . ASP   A  1 416  ? -65.139 50.557  79.426  1.00 26.60 ? 414  ASP   A O     1 
ATOM   2935  C  CB    . ASP   A  1 416  ? -66.077 47.868  80.843  1.00 29.79 ? 414  ASP   A CB    1 
ATOM   2936  C  CG    . ASP   A  1 416  ? -65.993 48.041  82.338  1.00 33.54 ? 414  ASP   A CG    1 
ATOM   2937  O  OD1   . ASP   A  1 416  ? -64.869 47.974  82.883  1.00 35.18 ? 414  ASP   A OD1   1 
ATOM   2938  O  OD2   . ASP   A  1 416  ? -67.052 48.239  82.972  1.00 44.02 ? 414  ASP   A OD2   1 
ATOM   2939  N  N     . VAL   A  1 417  ? -63.756 50.276  81.171  1.00 22.96 ? 415  VAL   A N     1 
ATOM   2940  C  CA    . VAL   A  1 417  ? -63.606 51.713  81.375  1.00 24.08 ? 415  VAL   A CA    1 
ATOM   2941  C  C     . VAL   A  1 417  ? -62.212 52.240  81.050  1.00 20.03 ? 415  VAL   A C     1 
ATOM   2942  O  O     . VAL   A  1 417  ? -62.053 53.461  80.914  1.00 22.31 ? 415  VAL   A O     1 
ATOM   2943  C  CB    . VAL   A  1 417  ? -64.010 52.135  82.802  1.00 28.75 ? 415  VAL   A CB    1 
ATOM   2944  C  CG1   . VAL   A  1 417  ? -65.469 51.790  83.051  1.00 30.70 ? 415  VAL   A CG1   1 
ATOM   2945  C  CG2   . VAL   A  1 417  ? -63.101 51.504  83.831  1.00 25.68 ? 415  VAL   A CG2   1 
ATOM   2946  N  N     . VAL   A  1 418  ? -61.202 51.382  80.936  1.00 19.41 ? 416  VAL   A N     1 
ATOM   2947  C  CA    . VAL   A  1 418  ? -59.874 51.805  80.509  1.00 18.21 ? 416  VAL   A CA    1 
ATOM   2948  C  C     . VAL   A  1 418  ? -59.380 50.828  79.454  1.00 18.29 ? 416  VAL   A C     1 
ATOM   2949  O  O     . VAL   A  1 418  ? -59.876 49.708  79.317  1.00 19.67 ? 416  VAL   A O     1 
ATOM   2950  C  CB    . VAL   A  1 418  ? -58.847 51.900  81.669  1.00 19.40 ? 416  VAL   A CB    1 
ATOM   2951  C  CG1   . VAL   A  1 418  ? -59.278 52.950  82.671  1.00 21.02 ? 416  VAL   A CG1   1 
ATOM   2952  C  CG2   . VAL   A  1 418  ? -58.651 50.551  82.354  1.00 19.46 ? 416  VAL   A CG2   1 
ATOM   2953  N  N     . PHE   A  1 419  ? -58.396 51.275  78.702  1.00 18.23 ? 417  PHE   A N     1 
ATOM   2954  C  CA    . PHE   A  1 419  ? -57.764 50.449  77.685  1.00 18.54 ? 417  PHE   A CA    1 
ATOM   2955  C  C     . PHE   A  1 419  ? -56.362 50.103  78.154  1.00 18.35 ? 417  PHE   A C     1 
ATOM   2956  O  O     . PHE   A  1 419  ? -55.451 50.941  78.037  1.00 18.80 ? 417  PHE   A O     1 
ATOM   2957  C  CB    . PHE   A  1 419  ? -57.714 51.199  76.352  1.00 17.99 ? 417  PHE   A CB    1 
ATOM   2958  C  CG    . PHE   A  1 419  ? -57.012 50.450  75.262  1.00 19.83 ? 417  PHE   A CG    1 
ATOM   2959  C  CD1   . PHE   A  1 419  ? -57.457 49.197  74.868  1.00 20.29 ? 417  PHE   A CD1   1 
ATOM   2960  C  CD2   . PHE   A  1 419  ? -55.921 51.001  74.616  1.00 17.83 ? 417  PHE   A CD2   1 
ATOM   2961  C  CE1   . PHE   A  1 419  ? -56.837 48.516  73.856  1.00 19.09 ? 417  PHE   A CE1   1 
ATOM   2962  C  CE2   . PHE   A  1 419  ? -55.285 50.316  73.602  1.00 18.96 ? 417  PHE   A CE2   1 
ATOM   2963  C  CZ    . PHE   A  1 419  ? -55.740 49.070  73.222  1.00 20.55 ? 417  PHE   A CZ    1 
ATOM   2964  N  N     . PRO   A  1 420  ? -56.136 48.908  78.710  1.00 18.15 ? 418  PRO   A N     1 
ATOM   2965  C  CA    . PRO   A  1 420  ? -54.790 48.567  79.194  1.00 18.03 ? 418  PRO   A CA    1 
ATOM   2966  C  C     . PRO   A  1 420  ? -53.840 48.313  78.038  1.00 19.89 ? 418  PRO   A C     1 
ATOM   2967  O  O     . PRO   A  1 420  ? -54.212 47.734  77.016  1.00 20.43 ? 418  PRO   A O     1 
ATOM   2968  C  CB    . PRO   A  1 420  ? -55.013 47.296  80.022  1.00 18.33 ? 418  PRO   A CB    1 
ATOM   2969  C  CG    . PRO   A  1 420  ? -56.505 47.282  80.311  1.00 18.56 ? 418  PRO   A CG    1 
ATOM   2970  C  CD    . PRO   A  1 420  ? -57.128 47.890  79.100  1.00 18.84 ? 418  PRO   A CD    1 
ATOM   2971  N  N     . GLN   A  1 421  ? -52.603 48.769  78.216  1.00 17.71 ? 419  GLN   A N     1 
ATOM   2972  C  CA    . GLN   A  1 421  ? -51.542 48.642  77.226  1.00 18.83 ? 419  GLN   A CA    1 
ATOM   2973  C  C     . GLN   A  1 421  ? -50.319 48.125  77.965  1.00 19.12 ? 419  GLN   A C     1 
ATOM   2974  O  O     . GLN   A  1 421  ? -49.696 48.863  78.738  1.00 19.16 ? 419  GLN   A O     1 
ATOM   2975  C  CB    . GLN   A  1 421  ? -51.253 49.984  76.559  1.00 17.71 ? 419  GLN   A CB    1 
ATOM   2976  C  CG    . GLN   A  1 421  ? -52.487 50.575  75.900  1.00 18.30 ? 419  GLN   A CG    1 
ATOM   2977  C  CD    . GLN   A  1 421  ? -52.312 52.043  75.598  1.00 19.83 ? 419  GLN   A CD    1 
ATOM   2978  O  OE1   . GLN   A  1 421  ? -52.109 52.847  76.506  1.00 17.71 ? 419  GLN   A OE1   1 
ATOM   2979  N  NE2   . GLN   A  1 421  ? -52.392 52.402  74.321  1.00 17.30 ? 419  GLN   A NE2   1 
ATOM   2980  N  N     . PHE   A  1 422  ? -50.000 46.857  77.752  1.00 17.82 ? 420  PHE   A N     1 
ATOM   2981  C  CA    . PHE   A  1 422  ? -48.983 46.184  78.552  1.00 17.94 ? 420  PHE   A CA    1 
ATOM   2982  C  C     . PHE   A  1 422  ? -47.657 46.285  77.814  1.00 19.23 ? 420  PHE   A C     1 
ATOM   2983  O  O     . PHE   A  1 422  ? -47.359 45.479  76.928  1.00 19.17 ? 420  PHE   A O     1 
ATOM   2984  C  CB    . PHE   A  1 422  ? -49.398 44.743  78.819  1.00 19.06 ? 420  PHE   A CB    1 
ATOM   2985  C  CG    . PHE   A  1 422  ? -50.696 44.640  79.578  1.00 20.07 ? 420  PHE   A CG    1 
ATOM   2986  C  CD1   . PHE   A  1 422  ? -50.774 45.082  80.890  1.00 20.28 ? 420  PHE   A CD1   1 
ATOM   2987  C  CD2   . PHE   A  1 422  ? -51.841 44.149  78.964  1.00 19.22 ? 420  PHE   A CD2   1 
ATOM   2988  C  CE1   . PHE   A  1 422  ? -51.966 45.003  81.592  1.00 19.93 ? 420  PHE   A CE1   1 
ATOM   2989  C  CE2   . PHE   A  1 422  ? -53.036 44.076  79.658  1.00 20.71 ? 420  PHE   A CE2   1 
ATOM   2990  C  CZ    . PHE   A  1 422  ? -53.093 44.502  80.979  1.00 21.15 ? 420  PHE   A CZ    1 
ATOM   2991  N  N     . ALA   A  1 423  ? -46.858 47.274  78.194  1.00 17.40 ? 421  ALA   A N     1 
ATOM   2992  C  CA    . ALA   A  1 423  ? -45.555 47.501  77.578  1.00 17.27 ? 421  ALA   A CA    1 
ATOM   2993  C  C     . ALA   A  1 423  ? -44.526 46.649  78.311  1.00 21.71 ? 421  ALA   A C     1 
ATOM   2994  O  O     . ALA   A  1 423  ? -44.238 46.891  79.492  1.00 20.29 ? 421  ALA   A O     1 
ATOM   2995  C  CB    . ALA   A  1 423  ? -45.195 48.983  77.630  1.00 20.17 ? 421  ALA   A CB    1 
ATOM   2996  N  N     . THR   A  1 424  ? -43.989 45.639  77.626  1.00 20.82 ? 422  THR   A N     1 
ATOM   2997  C  CA    . THR   A  1 424  ? -42.921 44.832  78.218  1.00 19.14 ? 422  THR   A CA    1 
ATOM   2998  C  C     . THR   A  1 424  ? -42.263 44.008  77.129  1.00 21.90 ? 422  THR   A C     1 
ATOM   2999  O  O     . THR   A  1 424  ? -42.913 43.600  76.157  1.00 21.36 ? 422  THR   A O     1 
ATOM   3000  C  CB    . THR   A  1 424  ? -43.427 43.898  79.333  1.00 20.64 ? 422  THR   A CB    1 
ATOM   3001  O  OG1   . THR   A  1 424  ? -42.314 43.198  79.913  1.00 23.82 ? 422  THR   A OG1   1 
ATOM   3002  C  CG2   . THR   A  1 424  ? -44.437 42.875  78.789  1.00 22.18 ? 422  THR   A CG2   1 
ATOM   3003  N  N     . HIS   A  1 425  ? -40.960 43.789  77.300  1.00 19.06 ? 423  HIS   A N     1 
ATOM   3004  C  CA    . HIS   A  1 425  ? -40.183 42.878  76.479  1.00 22.51 ? 423  HIS   A CA    1 
ATOM   3005  C  C     . HIS   A  1 425  ? -39.920 41.565  77.185  1.00 25.49 ? 423  HIS   A C     1 
ATOM   3006  O  O     . HIS   A  1 425  ? -39.214 40.713  76.640  1.00 25.38 ? 423  HIS   A O     1 
ATOM   3007  C  CB    . HIS   A  1 425  ? -38.846 43.518  76.095  1.00 18.97 ? 423  HIS   A CB    1 
ATOM   3008  C  CG    . HIS   A  1 425  ? -38.995 44.770  75.297  1.00 22.73 ? 423  HIS   A CG    1 
ATOM   3009  N  ND1   . HIS   A  1 425  ? -38.206 45.883  75.500  1.00 25.49 ? 423  HIS   A ND1   1 
ATOM   3010  C  CD2   . HIS   A  1 425  ? -39.864 45.098  74.311  1.00 24.50 ? 423  HIS   A CD2   1 
ATOM   3011  C  CE1   . HIS   A  1 425  ? -38.579 46.840  74.667  1.00 29.20 ? 423  HIS   A CE1   1 
ATOM   3012  N  NE2   . HIS   A  1 425  ? -39.585 46.389  73.937  1.00 23.30 ? 423  HIS   A NE2   1 
ATOM   3013  N  N     . ASN   A  1 426  ? -40.454 41.398  78.391  1.00 21.51 ? 424  ASN   A N     1 
ATOM   3014  C  CA    . ASN   A  1 426  ? -40.194 40.228  79.220  1.00 25.52 ? 424  ASN   A CA    1 
ATOM   3015  C  C     . ASN   A  1 426  ? -41.224 39.166  78.861  1.00 24.26 ? 424  ASN   A C     1 
ATOM   3016  O  O     . ASN   A  1 426  ? -42.422 39.350  79.100  1.00 24.49 ? 424  ASN   A O     1 
ATOM   3017  C  CB    . ASN   A  1 426  ? -40.262 40.617  80.693  1.00 24.03 ? 424  ASN   A CB    1 
ATOM   3018  C  CG    . ASN   A  1 426  ? -39.897 39.482  81.624  1.00 26.74 ? 424  ASN   A CG    1 
ATOM   3019  O  OD1   . ASN   A  1 426  ? -40.300 38.336  81.427  1.00 26.59 ? 424  ASN   A OD1   1 
ATOM   3020  N  ND2   . ASN   A  1 426  ? -39.143 39.807  82.667  1.00 25.49 ? 424  ASN   A ND2   1 
ATOM   3021  N  N     . ALA   A  1 427  ? -40.758 38.063  78.271  1.00 24.14 ? 425  ALA   A N     1 
ATOM   3022  C  CA    . ALA   A  1 427  ? -41.664 37.023  77.800  1.00 25.52 ? 425  ALA   A CA    1 
ATOM   3023  C  C     . ALA   A  1 427  ? -42.429 36.368  78.943  1.00 23.19 ? 425  ALA   A C     1 
ATOM   3024  O  O     . ALA   A  1 427  ? -43.537 35.867  78.734  1.00 24.08 ? 425  ALA   A O     1 
ATOM   3025  C  CB    . ALA   A  1 427  ? -40.883 35.960  77.016  1.00 28.24 ? 425  ALA   A CB    1 
ATOM   3026  N  N     . GLN   A  1 428  ? -41.847 36.330  80.145  1.00 26.04 ? 426  GLN   A N     1 
ATOM   3027  C  CA    . GLN   A  1 428  ? -42.559 35.761  81.287  1.00 25.67 ? 426  GLN   A CA    1 
ATOM   3028  C  C     . GLN   A  1 428  ? -43.695 36.679  81.714  1.00 22.89 ? 426  GLN   A C     1 
ATOM   3029  O  O     . GLN   A  1 428  ? -44.828 36.227  81.925  1.00 24.12 ? 426  GLN   A O     1 
ATOM   3030  C  CB    . GLN   A  1 428  ? -41.591 35.519  82.452  1.00 25.34 ? 426  GLN   A CB    1 
ATOM   3031  C  CG    . GLN   A  1 428  ? -42.143 34.600  83.545  1.00 26.06 ? 426  GLN   A CG    1 
ATOM   3032  C  CD    . GLN   A  1 428  ? -43.193 35.265  84.409  1.00 31.68 ? 426  GLN   A CD    1 
ATOM   3033  O  OE1   . GLN   A  1 428  ? -43.096 36.457  84.706  1.00 29.74 ? 426  GLN   A OE1   1 
ATOM   3034  N  NE2   . GLN   A  1 428  ? -44.220 34.507  84.797  1.00 26.70 ? 426  GLN   A NE2   1 
ATOM   3035  N  N     . THR   A  1 429  ? -43.397 37.973  81.852  1.00 25.54 ? 427  THR   A N     1 
ATOM   3036  C  CA    . THR   A  1 429  ? -44.423 38.974  82.126  1.00 22.38 ? 427  THR   A CA    1 
ATOM   3037  C  C     . THR   A  1 429  ? -45.549 38.900  81.102  1.00 25.58 ? 427  THR   A C     1 
ATOM   3038  O  O     . THR   A  1 429  ? -46.732 38.824  81.455  1.00 24.02 ? 427  THR   A O     1 
ATOM   3039  C  CB    . THR   A  1 429  ? -43.797 40.371  82.113  1.00 25.68 ? 427  THR   A CB    1 
ATOM   3040  O  OG1   . THR   A  1 429  ? -42.603 40.383  82.909  1.00 23.66 ? 427  THR   A OG1   1 
ATOM   3041  C  CG2   . THR   A  1 429  ? -44.770 41.368  82.681  1.00 22.60 ? 427  THR   A CG2   1 
ATOM   3042  N  N     . LEU   A  1 430  ? -45.184 38.939  79.818  1.00 21.59 ? 428  LEU   A N     1 
ATOM   3043  C  CA    . LEU   A  1 430  ? -46.149 38.818  78.731  1.00 22.89 ? 428  LEU   A CA    1 
ATOM   3044  C  C     . LEU   A  1 430  ? -47.027 37.585  78.896  1.00 25.21 ? 428  LEU   A C     1 
ATOM   3045  O  O     . LEU   A  1 430  ? -48.262 37.675  78.853  1.00 24.50 ? 428  LEU   A O     1 
ATOM   3046  C  CB    . LEU   A  1 430  ? -45.392 38.775  77.401  1.00 22.65 ? 428  LEU   A CB    1 
ATOM   3047  C  CG    . LEU   A  1 430  ? -46.086 38.991  76.045  1.00 27.66 ? 428  LEU   A CG    1 
ATOM   3048  C  CD1   . LEU   A  1 430  ? -45.012 39.029  74.973  1.00 28.54 ? 428  LEU   A CD1   1 
ATOM   3049  C  CD2   . LEU   A  1 430  ? -47.105 37.919  75.710  1.00 28.77 ? 428  LEU   A CD2   1 
ATOM   3050  N  N     . ALA   A  1 431  ? -46.402 36.417  79.073  1.00 23.77 ? 429  ALA   A N     1 
ATOM   3051  C  CA    . ALA   A  1 431  ? -47.162 35.173  79.155  1.00 24.31 ? 429  ALA   A CA    1 
ATOM   3052  C  C     . ALA   A  1 431  ? -48.120 35.180  80.339  1.00 22.71 ? 429  ALA   A C     1 
ATOM   3053  O  O     . ALA   A  1 431  ? -49.268 34.740  80.216  1.00 24.64 ? 429  ALA   A O     1 
ATOM   3054  C  CB    . ALA   A  1 431  ? -46.210 33.979  79.245  1.00 26.73 ? 429  ALA   A CB    1 
ATOM   3055  N  N     . ALA   A  1 432  ? -47.670 35.691  81.488  1.00 24.52 ? 430  ALA   A N     1 
ATOM   3056  C  CA    . ALA   A  1 432  ? -48.533 35.746  82.666  1.00 25.86 ? 430  ALA   A CA    1 
ATOM   3057  C  C     . ALA   A  1 432  ? -49.792 36.546  82.378  1.00 25.28 ? 430  ALA   A C     1 
ATOM   3058  O  O     . ALA   A  1 432  ? -50.897 36.157  82.778  1.00 26.87 ? 430  ALA   A O     1 
ATOM   3059  C  CB    . ALA   A  1 432  ? -47.781 36.361  83.848  1.00 23.63 ? 430  ALA   A CB    1 
ATOM   3060  N  N     . ILE   A  1 433  ? -49.642 37.659  81.667  1.00 23.19 ? 431  ILE   A N     1 
ATOM   3061  C  CA    . ILE   A  1 433  ? -50.765 38.547  81.403  1.00 25.97 ? 431  ILE   A CA    1 
ATOM   3062  C  C     . ILE   A  1 433  ? -51.640 37.997  80.292  1.00 24.60 ? 431  ILE   A C     1 
ATOM   3063  O  O     . ILE   A  1 433  ? -52.872 38.102  80.347  1.00 24.03 ? 431  ILE   A O     1 
ATOM   3064  C  CB    . ILE   A  1 433  ? -50.217 39.947  81.082  1.00 26.91 ? 431  ILE   A CB    1 
ATOM   3065  C  CG1   . ILE   A  1 433  ? -49.636 40.544  82.356  1.00 24.20 ? 431  ILE   A CG1   1 
ATOM   3066  C  CG2   . ILE   A  1 433  ? -51.275 40.833  80.483  1.00 24.74 ? 431  ILE   A CG2   1 
ATOM   3067  C  CD1   . ILE   A  1 433  ? -48.902 41.788  82.124  1.00 27.90 ? 431  ILE   A CD1   1 
ATOM   3068  N  N     . TYR   A  1 434  ? -51.021 37.402  79.270  1.00 23.25 ? 432  TYR   A N     1 
ATOM   3069  C  CA    . TYR   A  1 434  ? -51.779 36.760  78.204  1.00 25.41 ? 432  TYR   A CA    1 
ATOM   3070  C  C     . TYR   A  1 434  ? -52.748 35.730  78.776  1.00 24.64 ? 432  TYR   A C     1 
ATOM   3071  O  O     . TYR   A  1 434  ? -53.927 35.690  78.406  1.00 28.07 ? 432  TYR   A O     1 
ATOM   3072  C  CB    . TYR   A  1 434  ? -50.805 36.118  77.208  1.00 25.05 ? 432  TYR   A CB    1 
ATOM   3073  C  CG    . TYR   A  1 434  ? -51.442 35.230  76.169  1.00 25.86 ? 432  TYR   A CG    1 
ATOM   3074  C  CD1   . TYR   A  1 434  ? -52.237 35.763  75.162  1.00 27.20 ? 432  TYR   A CD1   1 
ATOM   3075  C  CD2   . TYR   A  1 434  ? -51.227 33.861  76.181  1.00 26.42 ? 432  TYR   A CD2   1 
ATOM   3076  C  CE1   . TYR   A  1 434  ? -52.814 34.950  74.202  1.00 29.03 ? 432  TYR   A CE1   1 
ATOM   3077  C  CE2   . TYR   A  1 434  ? -51.797 33.039  75.230  1.00 30.52 ? 432  TYR   A CE2   1 
ATOM   3078  C  CZ    . TYR   A  1 434  ? -52.590 33.585  74.246  1.00 31.92 ? 432  TYR   A CZ    1 
ATOM   3079  O  OH    . TYR   A  1 434  ? -53.158 32.756  73.305  1.00 33.58 ? 432  TYR   A OH    1 
ATOM   3080  N  N     . HIS   A  1 435  ? -52.273 34.900  79.704  1.00 26.61 ? 433  HIS   A N     1 
ATOM   3081  C  CA    . HIS   A  1 435  ? -53.159 33.893  80.283  1.00 26.82 ? 433  HIS   A CA    1 
ATOM   3082  C  C     . HIS   A  1 435  ? -54.086 34.495  81.331  1.00 28.24 ? 433  HIS   A C     1 
ATOM   3083  O  O     . HIS   A  1 435  ? -55.235 34.047  81.482  1.00 27.56 ? 433  HIS   A O     1 
ATOM   3084  C  CB    . HIS   A  1 435  ? -52.325 32.746  80.858  1.00 33.08 ? 433  HIS   A CB    1 
ATOM   3085  C  CG    . HIS   A  1 435  ? -51.725 31.869  79.802  1.00 30.30 ? 433  HIS   A CG    1 
ATOM   3086  N  ND1   . HIS   A  1 435  ? -52.424 30.843  79.205  1.00 32.57 ? 433  HIS   A ND1   1 
ATOM   3087  C  CD2   . HIS   A  1 435  ? -50.510 31.893  79.204  1.00 32.48 ? 433  HIS   A CD2   1 
ATOM   3088  C  CE1   . HIS   A  1 435  ? -51.660 30.259  78.298  1.00 31.90 ? 433  HIS   A CE1   1 
ATOM   3089  N  NE2   . HIS   A  1 435  ? -50.491 30.874  78.281  1.00 33.11 ? 433  HIS   A NE2   1 
ATOM   3090  N  N     . MET   A  1 436  ? -53.619 35.515  82.051  1.00 27.51 ? 434  MET   A N     1 
ATOM   3091  C  CA    . MET   A  1 436  ? -54.503 36.218  82.970  1.00 25.62 ? 434  MET   A CA    1 
ATOM   3092  C  C     . MET   A  1 436  ? -55.686 36.817  82.228  1.00 25.70 ? 434  MET   A C     1 
ATOM   3093  O  O     . MET   A  1 436  ? -56.812 36.812  82.736  1.00 29.23 ? 434  MET   A O     1 
ATOM   3094  C  CB    . MET   A  1 436  ? -53.728 37.300  83.715  1.00 25.45 ? 434  MET   A CB    1 
ATOM   3095  C  CG    . MET   A  1 436  ? -54.578 38.067  84.697  1.00 30.82 ? 434  MET   A CG    1 
ATOM   3096  S  SD    . MET   A  1 436  ? -53.651 39.404  85.456  1.00 28.96 ? 434  MET   A SD    1 
ATOM   3097  C  CE    . MET   A  1 436  ? -52.532 38.505  86.515  1.00 29.93 ? 434  MET   A CE    1 
ATOM   3098  N  N     . ALA   A  1 437  ? -55.459 37.302  81.003  1.00 23.55 ? 435  ALA   A N     1 
ATOM   3099  C  CA    . ALA   A  1 437  ? -56.526 37.937  80.241  1.00 25.92 ? 435  ALA   A CA    1 
ATOM   3100  C  C     . ALA   A  1 437  ? -57.591 36.946  79.782  1.00 30.34 ? 435  ALA   A C     1 
ATOM   3101  O  O     . ALA   A  1 437  ? -58.733 37.353  79.527  1.00 27.91 ? 435  ALA   A O     1 
ATOM   3102  C  CB    . ALA   A  1 437  ? -55.942 38.671  79.037  1.00 27.04 ? 435  ALA   A CB    1 
ATOM   3103  N  N     . GLY   A  1 438  ? -57.255 35.666  79.680  1.00 30.52 ? 436  GLY   A N     1 
ATOM   3104  C  CA    . GLY   A  1 438  ? -58.229 34.667  79.299  1.00 31.19 ? 436  GLY   A CA    1 
ATOM   3105  C  C     . GLY   A  1 438  ? -58.526 34.691  77.814  1.00 34.16 ? 436  GLY   A C     1 
ATOM   3106  O  O     . GLY   A  1 438  ? -57.870 35.374  77.019  1.00 31.43 ? 436  GLY   A O     1 
ATOM   3107  N  N     . LYS   A  1 439  ? -59.574 33.948  77.447  1.00 34.76 ? 437  LYS   A N     1 
ATOM   3108  C  CA    . LYS   A  1 439  ? -59.826 33.587  76.057  1.00 35.85 ? 437  LYS   A CA    1 
ATOM   3109  C  C     . LYS   A  1 439  ? -60.603 34.637  75.278  1.00 37.51 ? 437  LYS   A C     1 
ATOM   3110  O  O     . LYS   A  1 439  ? -60.467 34.708  74.051  1.00 41.68 ? 437  LYS   A O     1 
ATOM   3111  C  CB    . LYS   A  1 439  ? -60.587 32.256  75.993  1.00 39.71 ? 437  LYS   A CB    1 
ATOM   3112  N  N     . ASP   A  1 440  ? -61.427 35.440  75.944  1.00 38.33 ? 438  ASP   A N     1 
ATOM   3113  C  CA    . ASP   A  1 440  ? -62.230 36.441  75.254  1.00 34.62 ? 438  ASP   A CA    1 
ATOM   3114  C  C     . ASP   A  1 440  ? -61.362 37.633  74.881  1.00 34.17 ? 438  ASP   A C     1 
ATOM   3115  O  O     . ASP   A  1 440  ? -60.853 38.337  75.761  1.00 33.78 ? 438  ASP   A O     1 
ATOM   3116  C  CB    . ASP   A  1 440  ? -63.397 36.890  76.129  1.00 36.71 ? 438  ASP   A CB    1 
ATOM   3117  C  CG    . ASP   A  1 440  ? -64.545 35.907  76.109  1.00 42.05 ? 438  ASP   A CG    1 
ATOM   3118  O  OD1   . ASP   A  1 440  ? -64.497 34.960  75.297  1.00 42.10 ? 438  ASP   A OD1   1 
ATOM   3119  O  OD2   . ASP   A  1 440  ? -65.493 36.080  76.901  1.00 52.07 ? 438  ASP   A OD2   1 
ATOM   3120  N  N     . PHE   A  1 441  ? -61.204 37.872  73.582  1.00 33.20 ? 439  PHE   A N     1 
ATOM   3121  C  CA    . PHE   A  1 441  ? -60.432 39.017  73.129  1.00 29.66 ? 439  PHE   A CA    1 
ATOM   3122  C  C     . PHE   A  1 441  ? -61.111 39.666  71.936  1.00 30.71 ? 439  PHE   A C     1 
ATOM   3123  O  O     . PHE   A  1 441  ? -61.735 38.998  71.112  1.00 28.76 ? 439  PHE   A O     1 
ATOM   3124  C  CB    . PHE   A  1 441  ? -58.991 38.644  72.743  1.00 27.41 ? 439  PHE   A CB    1 
ATOM   3125  C  CG    . PHE   A  1 441  ? -58.161 39.842  72.397  1.00 28.11 ? 439  PHE   A CG    1 
ATOM   3126  C  CD1   . PHE   A  1 441  ? -57.722 40.691  73.394  1.00 29.92 ? 439  PHE   A CD1   1 
ATOM   3127  C  CD2   . PHE   A  1 441  ? -57.891 40.165  71.084  1.00 27.88 ? 439  PHE   A CD2   1 
ATOM   3128  C  CE1   . PHE   A  1 441  ? -56.990 41.831  73.087  1.00 22.50 ? 439  PHE   A CE1   1 
ATOM   3129  C  CE2   . PHE   A  1 441  ? -57.158 41.304  70.779  1.00 25.67 ? 439  PHE   A CE2   1 
ATOM   3130  C  CZ    . PHE   A  1 441  ? -56.721 42.134  71.790  1.00 22.19 ? 439  PHE   A CZ    1 
ATOM   3131  N  N     . HIS   A  1 442  ? -60.978 40.983  71.854  1.00 27.42 ? 440  HIS   A N     1 
ATOM   3132  C  CA    . HIS   A  1 442  ? -61.339 41.730  70.659  1.00 28.48 ? 440  HIS   A CA    1 
ATOM   3133  C  C     . HIS   A  1 442  ? -60.421 42.939  70.582  1.00 29.94 ? 440  HIS   A C     1 
ATOM   3134  O  O     . HIS   A  1 442  ? -59.971 43.451  71.610  1.00 25.64 ? 440  HIS   A O     1 
ATOM   3135  C  CB    . HIS   A  1 442  ? -62.811 42.165  70.674  1.00 30.32 ? 440  HIS   A CB    1 
ATOM   3136  C  CG    . HIS   A  1 442  ? -63.173 43.023  71.843  1.00 27.48 ? 440  HIS   A CG    1 
ATOM   3137  N  ND1   . HIS   A  1 442  ? -63.084 44.399  71.814  1.00 29.27 ? 440  HIS   A ND1   1 
ATOM   3138  C  CD2   . HIS   A  1 442  ? -63.614 42.700  73.082  1.00 27.54 ? 440  HIS   A CD2   1 
ATOM   3139  C  CE1   . HIS   A  1 442  ? -63.465 44.888  72.981  1.00 27.25 ? 440  HIS   A CE1   1 
ATOM   3140  N  NE2   . HIS   A  1 442  ? -63.790 43.878  73.769  1.00 30.55 ? 440  HIS   A NE2   1 
ATOM   3141  N  N     . VAL   A  1 443  ? -60.131 43.385  69.358  1.00 29.51 ? 441  VAL   A N     1 
ATOM   3142  C  CA    . VAL   A  1 443  ? -59.278 44.555  69.203  1.00 30.94 ? 441  VAL   A CA    1 
ATOM   3143  C  C     . VAL   A  1 443  ? -59.933 45.736  69.897  1.00 30.04 ? 441  VAL   A C     1 
ATOM   3144  O  O     . VAL   A  1 443  ? -61.107 46.045  69.659  1.00 28.79 ? 441  VAL   A O     1 
ATOM   3145  C  CB    . VAL   A  1 443  ? -59.010 44.836  67.718  1.00 34.55 ? 441  VAL   A CB    1 
ATOM   3146  C  CG1   . VAL   A  1 443  ? -58.353 46.187  67.558  1.00 30.55 ? 441  VAL   A CG1   1 
ATOM   3147  C  CG2   . VAL   A  1 443  ? -58.121 43.742  67.138  1.00 36.56 ? 441  VAL   A CG2   1 
ATOM   3148  N  N     . GLY   A  1 444  ? -59.179 46.388  70.784  1.00 24.30 ? 442  GLY   A N     1 
ATOM   3149  C  CA    . GLY   A  1 444  ? -59.693 47.435  71.646  1.00 24.36 ? 442  GLY   A CA    1 
ATOM   3150  C  C     . GLY   A  1 444  ? -59.877 47.018  73.090  1.00 20.37 ? 442  GLY   A C     1 
ATOM   3151  O  O     . GLY   A  1 444  ? -60.084 47.886  73.947  1.00 23.83 ? 442  GLY   A O     1 
ATOM   3152  N  N     . LYS   A  1 445  ? -59.810 45.725  73.395  1.00 22.38 ? 443  LYS   A N     1 
ATOM   3153  C  CA    . LYS   A  1 445  ? -59.964 45.311  74.783  1.00 20.64 ? 443  LYS   A CA    1 
ATOM   3154  C  C     . LYS   A  1 445  ? -58.707 45.623  75.580  1.00 21.12 ? 443  LYS   A C     1 
ATOM   3155  O  O     . LYS   A  1 445  ? -58.773 46.209  76.668  1.00 21.30 ? 443  LYS   A O     1 
ATOM   3156  C  CB    . LYS   A  1 445  ? -60.293 43.826  74.856  1.00 25.59 ? 443  LYS   A CB    1 
ATOM   3157  C  CG    . LYS   A  1 445  ? -60.723 43.395  76.235  1.00 25.80 ? 443  LYS   A CG    1 
ATOM   3158  C  CD    . LYS   A  1 445  ? -61.069 41.921  76.275  1.00 31.24 ? 443  LYS   A CD    1 
ATOM   3159  C  CE    . LYS   A  1 445  ? -61.715 41.558  77.608  1.00 37.82 ? 443  LYS   A CE    1 
ATOM   3160  N  NZ    . LYS   A  1 445  ? -62.209 40.144  77.619  1.00 36.20 ? 443  LYS   A NZ    1 
ATOM   3161  N  N     . TYR   A  1 446  ? -57.552 45.219  75.056  1.00 21.73 ? 444  TYR   A N     1 
ATOM   3162  C  CA    . TYR   A  1 446  ? -56.255 45.654  75.555  1.00 21.00 ? 444  TYR   A CA    1 
ATOM   3163  C  C     . TYR   A  1 446  ? -55.243 45.407  74.441  1.00 20.30 ? 444  TYR   A C     1 
ATOM   3164  O  O     . TYR   A  1 446  ? -55.564 44.848  73.391  1.00 19.53 ? 444  TYR   A O     1 
ATOM   3165  C  CB    . TYR   A  1 446  ? -55.863 44.929  76.848  1.00 21.40 ? 444  TYR   A CB    1 
ATOM   3166  C  CG    . TYR   A  1 446  ? -55.675 43.444  76.650  1.00 23.55 ? 444  TYR   A CG    1 
ATOM   3167  C  CD1   . TYR   A  1 446  ? -54.452 42.918  76.257  1.00 23.74 ? 444  TYR   A CD1   1 
ATOM   3168  C  CD2   . TYR   A  1 446  ? -56.743 42.569  76.830  1.00 25.78 ? 444  TYR   A CD2   1 
ATOM   3169  C  CE1   . TYR   A  1 446  ? -54.297 41.552  76.056  1.00 28.26 ? 444  TYR   A CE1   1 
ATOM   3170  C  CE2   . TYR   A  1 446  ? -56.597 41.219  76.639  1.00 28.39 ? 444  TYR   A CE2   1 
ATOM   3171  C  CZ    . TYR   A  1 446  ? -55.377 40.714  76.250  1.00 29.53 ? 444  TYR   A CZ    1 
ATOM   3172  O  OH    . TYR   A  1 446  ? -55.248 39.356  76.057  1.00 39.20 ? 444  TYR   A OH    1 
ATOM   3173  N  N     . GLU   A  1 447  ? -54.006 45.823  74.678  1.00 19.14 ? 445  GLU   A N     1 
ATOM   3174  C  CA    . GLU   A  1 447  ? -52.958 45.525  73.721  1.00 19.80 ? 445  GLU   A CA    1 
ATOM   3175  C  C     . GLU   A  1 447  ? -51.659 45.377  74.484  1.00 20.14 ? 445  GLU   A C     1 
ATOM   3176  O  O     . GLU   A  1 447  ? -51.557 45.760  75.651  1.00 20.03 ? 445  GLU   A O     1 
ATOM   3177  C  CB    . GLU   A  1 447  ? -52.841 46.618  72.653  1.00 18.78 ? 445  GLU   A CB    1 
ATOM   3178  C  CG    . GLU   A  1 447  ? -52.338 47.929  73.233  1.00 19.52 ? 445  GLU   A CG    1 
ATOM   3179  C  CD    . GLU   A  1 447  ? -52.265 49.060  72.227  1.00 21.05 ? 445  GLU   A CD    1 
ATOM   3180  O  OE1   . GLU   A  1 447  ? -52.869 48.947  71.139  1.00 20.01 ? 445  GLU   A OE1   1 
ATOM   3181  O  OE2   . GLU   A  1 447  ? -51.598 50.079  72.531  1.00 19.77 ? 445  GLU   A OE2   1 
ATOM   3182  N  N     . PHE   A  1 448  ? -50.670 44.799  73.824  1.00 19.35 ? 446  PHE   A N     1 
ATOM   3183  C  CA    . PHE   A  1 448  ? -49.309 44.868  74.324  1.00 20.02 ? 446  PHE   A CA    1 
ATOM   3184  C  C     . PHE   A  1 448  ? -48.590 46.020  73.639  1.00 18.34 ? 446  PHE   A C     1 
ATOM   3185  O  O     . PHE   A  1 448  ? -49.080 46.589  72.658  1.00 20.77 ? 446  PHE   A O     1 
ATOM   3186  C  CB    . PHE   A  1 448  ? -48.574 43.549  74.079  1.00 19.62 ? 446  PHE   A CB    1 
ATOM   3187  C  CG    . PHE   A  1 448  ? -49.141 42.401  74.849  1.00 18.95 ? 446  PHE   A CG    1 
ATOM   3188  C  CD1   . PHE   A  1 448  ? -48.755 42.177  76.168  1.00 22.16 ? 446  PHE   A CD1   1 
ATOM   3189  C  CD2   . PHE   A  1 448  ? -50.067 41.550  74.263  1.00 20.51 ? 446  PHE   A CD2   1 
ATOM   3190  C  CE1   . PHE   A  1 448  ? -49.285 41.116  76.885  1.00 26.53 ? 446  PHE   A CE1   1 
ATOM   3191  C  CE2   . PHE   A  1 448  ? -50.609 40.486  74.981  1.00 24.86 ? 446  PHE   A CE2   1 
ATOM   3192  C  CZ    . PHE   A  1 448  ? -50.207 40.268  76.292  1.00 25.07 ? 446  PHE   A CZ    1 
ATOM   3193  N  N     . GLN   A  1 449  ? -47.430 46.382  74.184  1.00 17.85 ? 447  GLN   A N     1 
ATOM   3194  C  CA    . GLN   A  1 449  ? -46.577 47.390  73.574  1.00 17.60 ? 447  GLN   A CA    1 
ATOM   3195  C  C     . GLN   A  1 449  ? -45.122 46.969  73.706  1.00 19.01 ? 447  GLN   A C     1 
ATOM   3196  O  O     . GLN   A  1 449  ? -44.749 46.209  74.601  1.00 18.63 ? 447  GLN   A O     1 
ATOM   3197  C  CB    . GLN   A  1 449  ? -46.772 48.778  74.203  1.00 17.29 ? 447  GLN   A CB    1 
ATOM   3198  C  CG    . GLN   A  1 449  ? -48.189 49.280  74.076  1.00 19.42 ? 447  GLN   A CG    1 
ATOM   3199  C  CD    . GLN   A  1 449  ? -48.292 50.771  74.268  1.00 19.48 ? 447  GLN   A CD    1 
ATOM   3200  O  OE1   . GLN   A  1 449  ? -47.360 51.413  74.748  1.00 19.26 ? 447  GLN   A OE1   1 
ATOM   3201  N  NE2   . GLN   A  1 449  ? -49.441 51.331  73.906  1.00 18.89 ? 447  GLN   A NE2   1 
ATOM   3202  N  N     . CYS   A  1 450  ? -44.300 47.476  72.793  1.00 19.29 ? 448  CYS   A N     1 
ATOM   3203  C  CA    . CYS   A  1 450  ? -42.877 47.179  72.802  1.00 20.45 ? 448  CYS   A CA    1 
ATOM   3204  C  C     . CYS   A  1 450  ? -42.147 48.346  72.165  1.00 22.25 ? 448  CYS   A C     1 
ATOM   3205  O  O     . CYS   A  1 450  ? -42.754 49.216  71.537  1.00 21.31 ? 448  CYS   A O     1 
ATOM   3206  C  CB    . CYS   A  1 450  ? -42.558 45.893  72.043  1.00 21.35 ? 448  CYS   A CB    1 
ATOM   3207  S  SG    . CYS   A  1 450  ? -42.732 46.054  70.218  1.00 24.39 ? 448  CYS   A SG    1 
ATOM   3208  N  N     . LEU   A  1 451  ? -40.824 48.336  72.303  1.00 19.85 ? 449  LEU   A N     1 
ATOM   3209  C  CA    . LEU   A  1 451  ? -39.985 49.367  71.722  1.00 22.26 ? 449  LEU   A CA    1 
ATOM   3210  C  C     . LEU   A  1 451  ? -39.513 48.958  70.335  1.00 20.97 ? 449  LEU   A C     1 
ATOM   3211  O  O     . LEU   A  1 451  ? -39.152 47.801  70.100  1.00 23.64 ? 449  LEU   A O     1 
ATOM   3212  C  CB    . LEU   A  1 451  ? -38.776 49.641  72.617  1.00 22.30 ? 449  LEU   A CB    1 
ATOM   3213  C  CG    . LEU   A  1 451  ? -37.724 50.634  72.118  1.00 28.47 ? 449  LEU   A CG    1 
ATOM   3214  C  CD1   . LEU   A  1 451  ? -38.312 52.025  71.841  1.00 28.66 ? 449  LEU   A CD1   1 
ATOM   3215  C  CD2   . LEU   A  1 451  ? -36.579 50.728  73.132  1.00 34.45 ? 449  LEU   A CD2   1 
ATOM   3216  N  N     . HIS   A  1 452  ? -39.528 49.923  69.420  1.00 21.53 ? 450  HIS   A N     1 
ATOM   3217  C  CA    . HIS   A  1 452  ? -38.988 49.723  68.083  1.00 22.69 ? 450  HIS   A CA    1 
ATOM   3218  C  C     . HIS   A  1 452  ? -37.561 49.195  68.148  1.00 24.37 ? 450  HIS   A C     1 
ATOM   3219  O  O     . HIS   A  1 452  ? -36.765 49.624  68.983  1.00 23.17 ? 450  HIS   A O     1 
ATOM   3220  C  CB    . HIS   A  1 452  ? -38.999 51.041  67.305  1.00 21.68 ? 450  HIS   A CB    1 
ATOM   3221  C  CG    . HIS   A  1 452  ? -38.175 50.994  66.061  1.00 21.75 ? 450  HIS   A CG    1 
ATOM   3222  N  ND1   . HIS   A  1 452  ? -38.671 50.538  64.858  1.00 24.67 ? 450  HIS   A ND1   1 
ATOM   3223  C  CD2   . HIS   A  1 452  ? -36.871 51.294  65.845  1.00 24.01 ? 450  HIS   A CD2   1 
ATOM   3224  C  CE1   . HIS   A  1 452  ? -37.713 50.582  63.948  1.00 28.83 ? 450  HIS   A CE1   1 
ATOM   3225  N  NE2   . HIS   A  1 452  ? -36.607 51.021  64.527  1.00 23.97 ? 450  HIS   A NE2   1 
ATOM   3226  N  N     . GLY   A  1 453  ? -37.243 48.264  67.250  1.00 28.92 ? 451  GLY   A N     1 
ATOM   3227  C  CA    . GLY   A  1 453  ? -35.885 47.756  67.174  1.00 28.39 ? 451  GLY   A CA    1 
ATOM   3228  C  C     . GLY   A  1 453  ? -35.431 47.005  68.400  1.00 33.74 ? 451  GLY   A C     1 
ATOM   3229  O  O     . GLY   A  1 453  ? -34.226 46.881  68.637  1.00 40.58 ? 451  GLY   A O     1 
ATOM   3230  N  N     . MET   A  1 454  ? -36.367 46.513  69.202  1.00 31.26 ? 452  MET   A N     1 
ATOM   3231  C  CA    . MET   A  1 454  ? -36.034 45.748  70.393  1.00 32.51 ? 452  MET   A CA    1 
ATOM   3232  C  C     . MET   A  1 454  ? -37.088 44.679  70.632  1.00 30.24 ? 452  MET   A C     1 
ATOM   3233  O  O     . MET   A  1 454  ? -36.758 43.511  70.847  1.00 29.93 ? 452  MET   A O     1 
ATOM   3234  C  CB    . MET   A  1 454  ? -35.917 46.663  71.609  1.00 28.76 ? 452  MET   A CB    1 
ATOM   3235  C  CG    . MET   A  1 454  ? -35.551 45.936  72.899  1.00 34.68 ? 452  MET   A CG    1 
ATOM   3236  S  SD    . MET   A  1 454  ? -34.029 44.974  72.745  1.00 50.14 ? 452  MET   A SD    1 
ATOM   3237  C  CE    . MET   A  1 454  ? -32.842 46.271  72.360  1.00 42.15 ? 452  MET   A CE    1 
ATOM   3238  N  N     . GLY   A  1 455  ? -38.362 45.061  70.573  1.00 26.43 ? 453  GLY   A N     1 
ATOM   3239  C  CA    . GLY   A  1 455  ? -39.418 44.120  70.894  1.00 23.72 ? 453  GLY   A CA    1 
ATOM   3240  C  C     . GLY   A  1 455  ? -40.021 43.338  69.741  1.00 24.82 ? 453  GLY   A C     1 
ATOM   3241  O  O     . GLY   A  1 455  ? -40.756 42.378  69.985  1.00 25.55 ? 453  GLY   A O     1 
ATOM   3242  N  N     . GLU   A  1 456  ? -39.748 43.714  68.493  1.00 27.55 ? 454  GLU   A N     1 
ATOM   3243  C  CA    . GLU   A  1 456  ? -40.363 43.005  67.374  1.00 29.60 ? 454  GLU   A CA    1 
ATOM   3244  C  C     . GLU   A  1 456  ? -40.041 41.518  67.338  1.00 28.03 ? 454  GLU   A C     1 
ATOM   3245  O  O     . GLU   A  1 456  ? -40.949 40.736  67.009  1.00 31.37 ? 454  GLU   A O     1 
ATOM   3246  C  CB    . GLU   A  1 456  ? -39.962 43.651  66.044  1.00 30.46 ? 454  GLU   A CB    1 
ATOM   3247  C  CG    . GLU   A  1 456  ? -40.513 45.036  65.845  1.00 31.56 ? 454  GLU   A CG    1 
ATOM   3248  C  CD    . GLU   A  1 456  ? -39.537 46.090  66.273  1.00 31.09 ? 454  GLU   A CD    1 
ATOM   3249  O  OE1   . GLU   A  1 456  ? -38.683 45.779  67.131  1.00 31.74 ? 454  GLU   A OE1   1 
ATOM   3250  O  OE2   . GLU   A  1 456  ? -39.609 47.219  65.742  1.00 31.69 ? 454  GLU   A OE2   1 
ATOM   3251  N  N     . PRO   A  1 457  ? -38.817 41.058  67.633  1.00 26.39 ? 455  PRO   A N     1 
ATOM   3252  C  CA    . PRO   A  1 457  ? -38.596 39.601  67.631  1.00 32.37 ? 455  PRO   A CA    1 
ATOM   3253  C  C     . PRO   A  1 457  ? -39.516 38.869  68.584  1.00 30.60 ? 455  PRO   A C     1 
ATOM   3254  O  O     . PRO   A  1 457  ? -40.038 37.801  68.240  1.00 28.67 ? 455  PRO   A O     1 
ATOM   3255  C  CB    . PRO   A  1 457  ? -37.126 39.462  68.050  1.00 28.71 ? 455  PRO   A CB    1 
ATOM   3256  C  CG    . PRO   A  1 457  ? -36.503 40.747  67.697  1.00 31.89 ? 455  PRO   A CG    1 
ATOM   3257  C  CD    . PRO   A  1 457  ? -37.565 41.791  67.906  1.00 26.25 ? 455  PRO   A CD    1 
ATOM   3258  N  N     . LEU   A  1 458  ? -39.750 39.430  69.773  1.00 28.91 ? 456  LEU   A N     1 
ATOM   3259  C  CA    . LEU   A  1 458  ? -40.685 38.799  70.696  1.00 28.95 ? 456  LEU   A CA    1 
ATOM   3260  C  C     . LEU   A  1 458  ? -42.108 38.887  70.166  1.00 26.23 ? 456  LEU   A C     1 
ATOM   3261  O  O     . LEU   A  1 458  ? -42.826 37.885  70.123  1.00 26.44 ? 456  LEU   A O     1 
ATOM   3262  C  CB    . LEU   A  1 458  ? -40.586 39.441  72.079  1.00 27.07 ? 456  LEU   A CB    1 
ATOM   3263  C  CG    . LEU   A  1 458  ? -41.690 39.069  73.077  1.00 29.35 ? 456  LEU   A CG    1 
ATOM   3264  C  CD1   . LEU   A  1 458  ? -41.819 37.553  73.242  1.00 28.83 ? 456  LEU   A CD1   1 
ATOM   3265  C  CD2   . LEU   A  1 458  ? -41.431 39.737  74.435  1.00 29.31 ? 456  LEU   A CD2   1 
ATOM   3266  N  N     . TYR   A  1 459  ? -42.537 40.079  69.762  1.00 26.64 ? 457  TYR   A N     1 
ATOM   3267  C  CA    . TYR   A  1 459  ? -43.937 40.246  69.408  1.00 26.36 ? 457  TYR   A CA    1 
ATOM   3268  C  C     . TYR   A  1 459  ? -44.264 39.753  68.009  1.00 27.41 ? 457  TYR   A C     1 
ATOM   3269  O  O     . TYR   A  1 459  ? -45.448 39.621  67.687  1.00 30.32 ? 457  TYR   A O     1 
ATOM   3270  C  CB    . TYR   A  1 459  ? -44.347 41.707  69.602  1.00 24.53 ? 457  TYR   A CB    1 
ATOM   3271  C  CG    . TYR   A  1 459  ? -44.538 41.987  71.068  1.00 22.26 ? 457  TYR   A CG    1 
ATOM   3272  C  CD1   . TYR   A  1 459  ? -45.695 41.575  71.714  1.00 22.74 ? 457  TYR   A CD1   1 
ATOM   3273  C  CD2   . TYR   A  1 459  ? -43.544 42.592  71.825  1.00 24.75 ? 457  TYR   A CD2   1 
ATOM   3274  C  CE1   . TYR   A  1 459  ? -45.876 41.788  73.060  1.00 21.71 ? 457  TYR   A CE1   1 
ATOM   3275  C  CE2   . TYR   A  1 459  ? -43.723 42.814  73.184  1.00 24.25 ? 457  TYR   A CE2   1 
ATOM   3276  C  CZ    . TYR   A  1 459  ? -44.895 42.410  73.795  1.00 24.70 ? 457  TYR   A CZ    1 
ATOM   3277  O  OH    . TYR   A  1 459  ? -45.094 42.616  75.152  1.00 23.04 ? 457  TYR   A OH    1 
ATOM   3278  N  N     . GLU   A  1 460  ? -43.257 39.448  67.186  1.00 27.91 ? 458  GLU   A N     1 
ATOM   3279  C  CA    . GLU   A  1 460  ? -43.519 38.662  65.984  1.00 30.95 ? 458  GLU   A CA    1 
ATOM   3280  C  C     . GLU   A  1 460  ? -44.065 37.282  66.328  1.00 33.23 ? 458  GLU   A C     1 
ATOM   3281  O  O     . GLU   A  1 460  ? -44.711 36.652  65.484  1.00 33.89 ? 458  GLU   A O     1 
ATOM   3282  C  CB    . GLU   A  1 460  ? -42.242 38.526  65.148  1.00 30.91 ? 458  GLU   A CB    1 
ATOM   3283  N  N     . GLU   A  1 461  ? -43.817 36.803  67.546  1.00 29.04 ? 459  GLU   A N     1 
ATOM   3284  C  CA    . GLU   A  1 461  ? -44.360 35.547  68.046  1.00 32.60 ? 459  GLU   A CA    1 
ATOM   3285  C  C     . GLU   A  1 461  ? -45.694 35.722  68.758  1.00 34.51 ? 459  GLU   A C     1 
ATOM   3286  O  O     . GLU   A  1 461  ? -46.220 34.747  69.307  1.00 30.19 ? 459  GLU   A O     1 
ATOM   3287  C  CB    . GLU   A  1 461  ? -43.359 34.890  69.004  1.00 32.92 ? 459  GLU   A CB    1 
ATOM   3288  C  CG    . GLU   A  1 461  ? -41.976 34.735  68.426  1.00 36.19 ? 459  GLU   A CG    1 
ATOM   3289  C  CD    . GLU   A  1 461  ? -41.959 33.792  67.243  1.00 38.27 ? 459  GLU   A CD    1 
ATOM   3290  O  OE1   . GLU   A  1 461  ? -42.871 32.939  67.146  1.00 36.09 ? 459  GLU   A OE1   1 
ATOM   3291  O  OE2   . GLU   A  1 461  ? -41.040 33.911  66.407  1.00 40.92 ? 459  GLU   A OE2   1 
ATOM   3292  N  N     . VAL   A  1 462  ? -46.242 36.939  68.768  1.00 30.86 ? 460  VAL   A N     1 
ATOM   3293  C  CA    . VAL   A  1 462  ? -47.466 37.264  69.489  1.00 29.20 ? 460  VAL   A CA    1 
ATOM   3294  C  C     . VAL   A  1 462  ? -48.546 37.770  68.543  1.00 30.55 ? 460  VAL   A C     1 
ATOM   3295  O  O     . VAL   A  1 462  ? -49.686 37.290  68.565  1.00 32.18 ? 460  VAL   A O     1 
ATOM   3296  C  CB    . VAL   A  1 462  ? -47.198 38.300  70.604  1.00 27.79 ? 460  VAL   A CB    1 
ATOM   3297  C  CG1   . VAL   A  1 462  ? -48.505 38.704  71.275  1.00 27.19 ? 460  VAL   A CG1   1 
ATOM   3298  C  CG2   . VAL   A  1 462  ? -46.210 37.754  71.616  1.00 27.91 ? 460  VAL   A CG2   1 
ATOM   3299  N  N     . VAL   A  1 463  ? -48.206 38.752  67.708  1.00 28.66 ? 461  VAL   A N     1 
ATOM   3300  C  CA    . VAL   A  1 463  ? -49.173 39.359  66.806  1.00 29.93 ? 461  VAL   A CA    1 
ATOM   3301  C  C     . VAL   A  1 463  ? -49.580 38.357  65.736  1.00 33.86 ? 461  VAL   A C     1 
ATOM   3302  O  O     . VAL   A  1 463  ? -48.756 37.574  65.244  1.00 35.19 ? 461  VAL   A O     1 
ATOM   3303  C  CB    . VAL   A  1 463  ? -48.578 40.633  66.178  1.00 29.09 ? 461  VAL   A CB    1 
ATOM   3304  C  CG1   . VAL   A  1 463  ? -49.536 41.229  65.179  1.00 32.90 ? 461  VAL   A CG1   1 
ATOM   3305  C  CG2   . VAL   A  1 463  ? -48.247 41.651  67.270  1.00 25.28 ? 461  VAL   A CG2   1 
ATOM   3306  N  N     . GLY   A  1 464  ? -50.852 38.367  65.382  1.00 32.59 ? 462  GLY   A N     1 
ATOM   3307  C  CA    . GLY   A  1 464  ? -51.275 37.607  64.228  1.00 36.84 ? 462  GLY   A CA    1 
ATOM   3308  C  C     . GLY   A  1 464  ? -52.017 36.341  64.619  1.00 39.14 ? 462  GLY   A C     1 
ATOM   3309  O  O     . GLY   A  1 464  ? -51.736 35.711  65.648  1.00 35.73 ? 462  GLY   A O     1 
ATOM   3310  N  N     . ARG   A  1 465  ? -52.974 35.953  63.770  1.00 39.10 ? 463  ARG   A N     1 
ATOM   3311  C  CA    . ARG   A  1 465  ? -53.801 34.783  64.036  1.00 37.73 ? 463  ARG   A CA    1 
ATOM   3312  C  C     . ARG   A  1 465  ? -52.981 33.506  64.156  1.00 38.87 ? 463  ARG   A C     1 
ATOM   3313  O  O     . ARG   A  1 465  ? -53.423 32.560  64.817  1.00 43.68 ? 463  ARG   A O     1 
ATOM   3314  C  CB    . ARG   A  1 465  ? -54.856 34.630  62.936  1.00 41.56 ? 463  ARG   A CB    1 
ATOM   3315  N  N     . GLY   A  1 466  ? -51.802 33.458  63.546  1.00 38.79 ? 464  GLY   A N     1 
ATOM   3316  C  CA    . GLY   A  1 466  ? -50.965 32.282  63.626  1.00 40.81 ? 464  GLY   A CA    1 
ATOM   3317  C  C     . GLY   A  1 466  ? -50.135 32.178  64.876  1.00 42.91 ? 464  GLY   A C     1 
ATOM   3318  O  O     . GLY   A  1 466  ? -49.444 31.177  65.073  1.00 41.37 ? 464  GLY   A O     1 
ATOM   3319  N  N     . LYS   A  1 467  ? -50.186 33.194  65.739  1.00 37.83 ? 465  LYS   A N     1 
ATOM   3320  C  CA    . LYS   A  1 467  ? -49.372 33.218  66.954  1.00 34.70 ? 465  LYS   A CA    1 
ATOM   3321  C  C     . LYS   A  1 467  ? -50.340 33.268  68.128  1.00 36.72 ? 465  LYS   A C     1 
ATOM   3322  O  O     . LYS   A  1 467  ? -51.187 32.390  68.246  1.00 39.21 ? 465  LYS   A O     1 
ATOM   3323  C  CB    . LYS   A  1 467  ? -48.363 34.345  66.900  1.00 36.01 ? 465  LYS   A CB    1 
ATOM   3324  C  CG    . LYS   A  1 467  ? -47.444 34.280  65.687  1.00 39.02 ? 465  LYS   A CG    1 
ATOM   3325  C  CD    . LYS   A  1 467  ? -46.462 33.118  65.815  1.00 38.23 ? 465  LYS   A CD    1 
ATOM   3326  C  CE    . LYS   A  1 467  ? -45.445 33.116  64.690  1.00 40.97 ? 465  LYS   A CE    1 
ATOM   3327  N  NZ    . LYS   A  1 467  ? -44.239 32.323  65.067  1.00 43.37 ? 465  LYS   A NZ    1 
ATOM   3328  N  N     . LEU   A  1 468  ? -50.239 34.274  68.994  1.00 34.02 ? 466  LEU   A N     1 
ATOM   3329  C  CA    . LEU   A  1 468  ? -51.166 34.435  70.106  1.00 33.53 ? 466  LEU   A CA    1 
ATOM   3330  C  C     . LEU   A  1 468  ? -52.334 35.346  69.763  1.00 33.47 ? 466  LEU   A C     1 
ATOM   3331  O  O     . LEU   A  1 468  ? -53.276 35.456  70.560  1.00 31.07 ? 466  LEU   A O     1 
ATOM   3332  C  CB    . LEU   A  1 468  ? -50.429 34.981  71.340  1.00 31.82 ? 466  LEU   A CB    1 
ATOM   3333  C  CG    . LEU   A  1 468  ? -49.167 34.234  71.791  1.00 30.00 ? 466  LEU   A CG    1 
ATOM   3334  C  CD1   . LEU   A  1 468  ? -48.620 34.818  73.093  1.00 32.47 ? 466  LEU   A CD1   1 
ATOM   3335  C  CD2   . LEU   A  1 468  ? -49.422 32.724  71.925  1.00 31.89 ? 466  LEU   A CD2   1 
ATOM   3336  N  N     . ASP   A  1 469  ? -52.292 35.992  68.595  1.00 32.02 ? 467  ASP   A N     1 
ATOM   3337  C  CA    . ASP   A  1 469  ? -53.394 36.810  68.093  1.00 32.85 ? 467  ASP   A CA    1 
ATOM   3338  C  C     . ASP   A  1 469  ? -53.724 37.940  69.061  1.00 26.83 ? 467  ASP   A C     1 
ATOM   3339  O  O     . ASP   A  1 469  ? -54.890 38.214  69.356  1.00 26.46 ? 467  ASP   A O     1 
ATOM   3340  C  CB    . ASP   A  1 469  ? -54.627 35.947  67.804  1.00 31.91 ? 467  ASP   A CB    1 
ATOM   3341  C  CG    . ASP   A  1 469  ? -55.612 36.624  66.873  1.00 37.67 ? 467  ASP   A CG    1 
ATOM   3342  O  OD1   . ASP   A  1 469  ? -55.216 37.586  66.182  1.00 38.74 ? 467  ASP   A OD1   1 
ATOM   3343  O  OD2   . ASP   A  1 469  ? -56.784 36.196  66.840  1.00 45.91 ? 467  ASP   A OD2   1 
ATOM   3344  N  N     . ARG   A  1 470  ? -52.683 38.595  69.572  1.00 26.86 ? 468  ARG   A N     1 
ATOM   3345  C  CA    . ARG   A  1 470  ? -52.857 39.798  70.365  1.00 26.60 ? 468  ARG   A CA    1 
ATOM   3346  C  C     . ARG   A  1 470  ? -52.049 40.927  69.742  1.00 25.94 ? 468  ARG   A C     1 
ATOM   3347  O  O     . ARG   A  1 470  ? -50.907 40.711  69.318  1.00 25.83 ? 468  ARG   A O     1 
ATOM   3348  C  CB    . ARG   A  1 470  ? -52.411 39.592  71.821  1.00 23.06 ? 468  ARG   A CB    1 
ATOM   3349  C  CG    . ARG   A  1 470  ? -53.141 38.470  72.553  1.00 26.20 ? 468  ARG   A CG    1 
ATOM   3350  C  CD    . ARG   A  1 470  ? -54.599 38.832  72.793  1.00 26.76 ? 468  ARG   A CD    1 
ATOM   3351  N  NE    . ARG   A  1 470  ? -55.318 37.763  73.473  1.00 27.67 ? 468  ARG   A NE    1 
ATOM   3352  C  CZ    . ARG   A  1 470  ? -56.045 36.845  72.851  1.00 28.66 ? 468  ARG   A CZ    1 
ATOM   3353  N  NH1   . ARG   A  1 470  ? -56.138 36.818  71.531  1.00 28.02 ? 468  ARG   A NH1   1 
ATOM   3354  N  NH2   . ARG   A  1 470  ? -56.705 35.942  73.571  1.00 31.08 ? 468  ARG   A NH2   1 
ATOM   3355  N  N     . PRO   A  1 471  ? -52.606 42.128  69.664  1.00 24.57 ? 469  PRO   A N     1 
ATOM   3356  C  CA    . PRO   A  1 471  ? -51.916 43.215  68.974  1.00 20.53 ? 469  PRO   A CA    1 
ATOM   3357  C  C     . PRO   A  1 471  ? -50.801 43.789  69.830  1.00 22.20 ? 469  PRO   A C     1 
ATOM   3358  O  O     . PRO   A  1 471  ? -50.756 43.627  71.051  1.00 19.95 ? 469  PRO   A O     1 
ATOM   3359  C  CB    . PRO   A  1 471  ? -53.022 44.246  68.739  1.00 22.02 ? 469  PRO   A CB    1 
ATOM   3360  C  CG    . PRO   A  1 471  ? -53.971 44.019  69.855  1.00 22.61 ? 469  PRO   A CG    1 
ATOM   3361  C  CD    . PRO   A  1 471  ? -53.941 42.533  70.135  1.00 24.76 ? 469  PRO   A CD    1 
ATOM   3362  N  N     . CYS   A  1 472  ? -49.888 44.469  69.153  1.00 22.91 ? 470  CYS   A N     1 
ATOM   3363  C  CA    . CYS   A  1 472  ? -48.774 45.111  69.827  1.00 20.87 ? 470  CYS   A CA    1 
ATOM   3364  C  C     . CYS   A  1 472  ? -48.560 46.470  69.199  1.00 20.75 ? 470  CYS   A C     1 
ATOM   3365  O  O     . CYS   A  1 472  ? -48.484 46.577  67.972  1.00 24.04 ? 470  CYS   A O     1 
ATOM   3366  C  CB    . CYS   A  1 472  ? -47.493 44.275  69.718  1.00 20.35 ? 470  CYS   A CB    1 
ATOM   3367  S  SG    . CYS   A  1 472  ? -46.103 45.039  70.585  1.00 23.49 ? 470  CYS   A SG    1 
ATOM   3368  N  N     . ARG   A  1 473  ? -48.474 47.500  70.030  1.00 19.15 ? 471  ARG   A N     1 
ATOM   3369  C  CA    . ARG   A  1 473  ? -48.155 48.840  69.564  1.00 19.03 ? 471  ARG   A CA    1 
ATOM   3370  C  C     . ARG   A  1 473  ? -46.667 49.092  69.762  1.00 19.79 ? 471  ARG   A C     1 
ATOM   3371  O  O     . ARG   A  1 473  ? -46.143 48.910  70.865  1.00 20.57 ? 471  ARG   A O     1 
ATOM   3372  C  CB    . ARG   A  1 473  ? -48.973 49.895  70.299  1.00 18.40 ? 471  ARG   A CB    1 
ATOM   3373  C  CG    . ARG   A  1 473  ? -48.770 51.300  69.748  1.00 19.19 ? 471  ARG   A CG    1 
ATOM   3374  C  CD    . ARG   A  1 473  ? -49.706 52.274  70.425  1.00 17.74 ? 471  ARG   A CD    1 
ATOM   3375  N  NE    . ARG   A  1 473  ? -51.074 51.771  70.396  1.00 18.21 ? 471  ARG   A NE    1 
ATOM   3376  C  CZ    . ARG   A  1 473  ? -51.913 51.935  69.380  1.00 20.60 ? 471  ARG   A CZ    1 
ATOM   3377  N  NH1   . ARG   A  1 473  ? -51.602 52.691  68.339  1.00 18.60 ? 471  ARG   A NH1   1 
ATOM   3378  N  NH2   . ARG   A  1 473  ? -53.091 51.320  69.407  1.00 20.88 ? 471  ARG   A NH2   1 
ATOM   3379  N  N     . ILE   A  1 474  ? -46.000 49.498  68.695  1.00 21.56 ? 472  ILE   A N     1 
ATOM   3380  C  CA    . ILE   A  1 474  ? -44.566 49.753  68.721  1.00 19.94 ? 472  ILE   A CA    1 
ATOM   3381  C  C     . ILE   A  1 474  ? -44.331 51.211  69.079  1.00 21.23 ? 472  ILE   A C     1 
ATOM   3382  O  O     . ILE   A  1 474  ? -44.825 52.116  68.396  1.00 21.55 ? 472  ILE   A O     1 
ATOM   3383  C  CB    . ILE   A  1 474  ? -43.916 49.415  67.376  1.00 19.72 ? 472  ILE   A CB    1 
ATOM   3384  C  CG1   . ILE   A  1 474  ? -44.022 47.915  67.093  1.00 24.70 ? 472  ILE   A CG1   1 
ATOM   3385  C  CG2   . ILE   A  1 474  ? -42.459 49.887  67.375  1.00 19.51 ? 472  ILE   A CG2   1 
ATOM   3386  C  CD1   . ILE   A  1 474  ? -43.748 47.570  65.651  1.00 25.53 ? 472  ILE   A CD1   1 
ATOM   3387  N  N     . TYR   A  1 475  ? -43.585 51.433  70.158  1.00 17.93 ? 473  TYR   A N     1 
ATOM   3388  C  CA    . TYR   A  1 475  ? -43.129 52.763  70.537  1.00 20.53 ? 473  TYR   A CA    1 
ATOM   3389  C  C     . TYR   A  1 475  ? -41.953 53.126  69.642  1.00 22.20 ? 473  TYR   A C     1 
ATOM   3390  O  O     . TYR   A  1 475  ? -40.910 52.463  69.678  1.00 21.37 ? 473  TYR   A O     1 
ATOM   3391  C  CB    . TYR   A  1 475  ? -42.735 52.771  72.009  1.00 22.16 ? 473  TYR   A CB    1 
ATOM   3392  C  CG    . TYR   A  1 475  ? -42.413 54.115  72.637  1.00 23.60 ? 473  TYR   A CG    1 
ATOM   3393  C  CD1   . TYR   A  1 475  ? -41.113 54.619  72.642  1.00 29.28 ? 473  TYR   A CD1   1 
ATOM   3394  C  CD2   . TYR   A  1 475  ? -43.402 54.857  73.271  1.00 22.23 ? 473  TYR   A CD2   1 
ATOM   3395  C  CE1   . TYR   A  1 475  ? -40.820 55.843  73.251  1.00 30.31 ? 473  TYR   A CE1   1 
ATOM   3396  C  CE2   . TYR   A  1 475  ? -43.126 56.071  73.868  1.00 23.63 ? 473  TYR   A CE2   1 
ATOM   3397  C  CZ    . TYR   A  1 475  ? -41.834 56.556  73.866  1.00 29.23 ? 473  TYR   A CZ    1 
ATOM   3398  O  OH    . TYR   A  1 475  ? -41.577 57.771  74.460  1.00 30.66 ? 473  TYR   A OH    1 
ATOM   3399  N  N     . ALA   A  1 476  ? -42.129 54.165  68.835  1.00 20.11 ? 474  ALA   A N     1 
ATOM   3400  C  CA    . ALA   A  1 476  ? -41.263 54.445  67.691  1.00 20.99 ? 474  ALA   A CA    1 
ATOM   3401  C  C     . ALA   A  1 476  ? -40.571 55.777  67.903  1.00 19.96 ? 474  ALA   A C     1 
ATOM   3402  O  O     . ALA   A  1 476  ? -41.183 56.840  67.688  1.00 20.02 ? 474  ALA   A O     1 
ATOM   3403  C  CB    . ALA   A  1 476  ? -42.069 54.464  66.393  1.00 19.62 ? 474  ALA   A CB    1 
ATOM   3404  N  N     . PRO   A  1 477  ? -39.313 55.776  68.339  1.00 21.24 ? 475  PRO   A N     1 
ATOM   3405  C  CA    . PRO   A  1 477  ? -38.579 57.033  68.452  1.00 19.54 ? 475  PRO   A CA    1 
ATOM   3406  C  C     . PRO   A  1 477  ? -38.374 57.638  67.076  1.00 21.57 ? 475  PRO   A C     1 
ATOM   3407  O  O     . PRO   A  1 477  ? -38.165 56.929  66.087  1.00 21.19 ? 475  PRO   A O     1 
ATOM   3408  C  CB    . PRO   A  1 477  ? -37.246 56.615  69.087  1.00 23.75 ? 475  PRO   A CB    1 
ATOM   3409  C  CG    . PRO   A  1 477  ? -37.485 55.237  69.649  1.00 24.82 ? 475  PRO   A CG    1 
ATOM   3410  C  CD    . PRO   A  1 477  ? -38.487 54.622  68.725  1.00 21.73 ? 475  PRO   A CD    1 
ATOM   3411  N  N     . VAL   A  1 478  ? -38.441 58.959  67.018  1.00 20.07 ? 476  VAL   A N     1 
ATOM   3412  C  CA    . VAL   A  1 478  ? -38.290 59.695  65.776  1.00 21.71 ? 476  VAL   A CA    1 
ATOM   3413  C  C     . VAL   A  1 478  ? -37.355 60.866  66.034  1.00 22.83 ? 476  VAL   A C     1 
ATOM   3414  O  O     . VAL   A  1 478  ? -37.593 61.670  66.940  1.00 21.88 ? 476  VAL   A O     1 
ATOM   3415  C  CB    . VAL   A  1 478  ? -39.648 60.190  65.244  1.00 25.01 ? 476  VAL   A CB    1 
ATOM   3416  C  CG1   . VAL   A  1 478  ? -39.451 60.996  63.959  1.00 23.33 ? 476  VAL   A CG1   1 
ATOM   3417  C  CG2   . VAL   A  1 478  ? -40.584 59.015  65.007  1.00 20.77 ? 476  VAL   A CG2   1 
ATOM   3418  N  N     . GLY   A  1 479  ? -36.298 60.964  65.252  1.00 24.17 ? 477  GLY   A N     1 
ATOM   3419  C  CA    . GLY   A  1 479  ? -35.456 62.135  65.345  1.00 26.73 ? 477  GLY   A CA    1 
ATOM   3420  C  C     . GLY   A  1 479  ? -34.060 61.853  64.840  1.00 32.58 ? 477  GLY   A C     1 
ATOM   3421  O  O     . GLY   A  1 479  ? -33.740 60.753  64.387  1.00 26.35 ? 477  GLY   A O     1 
ATOM   3422  N  N     . THR   A  1 480  ? -33.234 62.887  64.927  1.00 31.04 ? 478  THR   A N     1 
ATOM   3423  C  CA    . THR   A  1 480  ? -31.840 62.775  64.532  1.00 37.30 ? 478  THR   A CA    1 
ATOM   3424  C  C     . THR   A  1 480  ? -30.942 62.758  65.765  1.00 43.76 ? 478  THR   A C     1 
ATOM   3425  O  O     . THR   A  1 480  ? -29.720 62.864  65.655  1.00 58.68 ? 478  THR   A O     1 
ATOM   3426  C  CB    . THR   A  1 480  ? -31.427 63.933  63.620  1.00 38.23 ? 478  THR   A CB    1 
ATOM   3427  O  OG1   . THR   A  1 480  ? -31.385 65.138  64.389  1.00 45.46 ? 478  THR   A OG1   1 
ATOM   3428  C  CG2   . THR   A  1 480  ? -32.430 64.105  62.495  1.00 41.30 ? 478  THR   A CG2   1 
ATOM   3429  N  N     . ALA   A  1 497  ? -28.059 46.476  81.794  1.00 49.61 ? 495  ALA   A N     1 
ATOM   3430  C  CA    . ALA   A  1 497  ? -28.384 45.916  83.100  1.00 40.59 ? 495  ALA   A CA    1 
ATOM   3431  C  C     . ALA   A  1 497  ? -28.448 44.396  83.041  1.00 32.25 ? 495  ALA   A C     1 
ATOM   3432  O  O     . ALA   A  1 497  ? -29.235 43.829  82.281  1.00 38.02 ? 495  ALA   A O     1 
ATOM   3433  C  CB    . ALA   A  1 497  ? -29.704 46.481  83.607  1.00 37.35 ? 495  ALA   A CB    1 
ATOM   3434  N  N     . ASN   A  1 498  ? -27.625 43.737  83.860  1.00 35.09 ? 496  ASN   A N     1 
ATOM   3435  C  CA    . ASN   A  1 498  ? -27.616 42.277  83.890  1.00 37.45 ? 496  ASN   A CA    1 
ATOM   3436  C  C     . ASN   A  1 498  ? -28.939 41.702  84.378  1.00 36.40 ? 496  ASN   A C     1 
ATOM   3437  O  O     . ASN   A  1 498  ? -29.220 40.523  84.133  1.00 38.47 ? 496  ASN   A O     1 
ATOM   3438  C  CB    . ASN   A  1 498  ? -26.466 41.772  84.771  1.00 42.62 ? 496  ASN   A CB    1 
ATOM   3439  N  N     . SER   A  1 499  ? -29.754 42.501  85.066  1.00 36.29 ? 497  SER   A N     1 
ATOM   3440  C  CA    . SER   A  1 499  ? -31.066 42.061  85.521  1.00 34.60 ? 497  SER   A CA    1 
ATOM   3441  C  C     . SER   A  1 499  ? -32.128 42.113  84.427  1.00 35.77 ? 497  SER   A C     1 
ATOM   3442  O  O     . SER   A  1 499  ? -33.202 41.521  84.604  1.00 31.09 ? 497  SER   A O     1 
ATOM   3443  C  CB    . SER   A  1 499  ? -31.507 42.916  86.716  1.00 32.51 ? 497  SER   A CB    1 
ATOM   3444  O  OG    . SER   A  1 499  ? -31.444 44.307  86.416  1.00 36.02 ? 497  SER   A OG    1 
ATOM   3445  N  N     . SER   A  1 500  ? -31.852 42.791  83.313  1.00 34.19 ? 498  SER   A N     1 
ATOM   3446  C  CA    . SER   A  1 500  ? -32.848 43.001  82.267  1.00 30.92 ? 498  SER   A CA    1 
ATOM   3447  C  C     . SER   A  1 500  ? -33.115 41.723  81.486  1.00 33.91 ? 498  SER   A C     1 
ATOM   3448  O  O     . SER   A  1 500  ? -32.196 40.952  81.191  1.00 32.88 ? 498  SER   A O     1 
ATOM   3449  C  CB    . SER   A  1 500  ? -32.381 44.085  81.295  1.00 32.72 ? 498  SER   A CB    1 
ATOM   3450  O  OG    . SER   A  1 500  ? -32.334 45.348  81.921  1.00 41.11 ? 498  SER   A OG    1 
ATOM   3451  N  N     . PHE   A  1 501  ? -34.386 41.517  81.125  1.00 29.37 ? 499  PHE   A N     1 
ATOM   3452  C  CA    . PHE   A  1 501  ? -34.738 40.376  80.290  1.00 32.19 ? 499  PHE   A CA    1 
ATOM   3453  C  C     . PHE   A  1 501  ? -33.963 40.393  78.981  1.00 34.49 ? 499  PHE   A C     1 
ATOM   3454  O  O     . PHE   A  1 501  ? -33.512 39.346  78.507  1.00 35.76 ? 499  PHE   A O     1 
ATOM   3455  C  CB    . PHE   A  1 501  ? -36.243 40.361  80.008  1.00 27.97 ? 499  PHE   A CB    1 
ATOM   3456  C  CG    . PHE   A  1 501  ? -36.686 39.204  79.160  1.00 31.19 ? 499  PHE   A CG    1 
ATOM   3457  C  CD1   . PHE   A  1 501  ? -37.044 38.002  79.743  1.00 30.30 ? 499  PHE   A CD1   1 
ATOM   3458  C  CD2   . PHE   A  1 501  ? -36.734 39.313  77.777  1.00 31.48 ? 499  PHE   A CD2   1 
ATOM   3459  C  CE1   . PHE   A  1 501  ? -37.453 36.934  78.969  1.00 32.39 ? 499  PHE   A CE1   1 
ATOM   3460  C  CE2   . PHE   A  1 501  ? -37.135 38.249  76.996  1.00 31.69 ? 499  PHE   A CE2   1 
ATOM   3461  C  CZ    . PHE   A  1 501  ? -37.498 37.055  77.592  1.00 34.45 ? 499  PHE   A CZ    1 
ATOM   3462  N  N     . VAL   A  1 502  ? -33.807 41.575  78.379  1.00 33.54 ? 500  VAL   A N     1 
ATOM   3463  C  CA    . VAL   A  1 502  ? -33.153 41.675  77.078  1.00 38.20 ? 500  VAL   A CA    1 
ATOM   3464  C  C     . VAL   A  1 502  ? -31.701 41.235  77.175  1.00 38.02 ? 500  VAL   A C     1 
ATOM   3465  O  O     . VAL   A  1 502  ? -31.149 40.674  76.223  1.00 46.51 ? 500  VAL   A O     1 
ATOM   3466  C  CB    . VAL   A  1 502  ? -33.272 43.109  76.523  1.00 42.27 ? 500  VAL   A CB    1 
ATOM   3467  N  N     . HIS   A  1 503  ? -31.060 41.478  78.316  1.00 37.89 ? 501  HIS   A N     1 
ATOM   3468  C  CA    . HIS   A  1 503  ? -29.695 41.008  78.517  1.00 34.34 ? 501  HIS   A CA    1 
ATOM   3469  C  C     . HIS   A  1 503  ? -29.674 39.512  78.800  1.00 41.13 ? 501  HIS   A C     1 
ATOM   3470  O  O     . HIS   A  1 503  ? -28.875 38.769  78.216  1.00 38.58 ? 501  HIS   A O     1 
ATOM   3471  C  CB    . HIS   A  1 503  ? -29.042 41.787  79.659  1.00 37.69 ? 501  HIS   A CB    1 
ATOM   3472  C  CG    . HIS   A  1 503  ? -27.651 41.335  79.988  1.00 44.42 ? 501  HIS   A CG    1 
ATOM   3473  N  ND1   . HIS   A  1 503  ? -27.386 40.349  80.916  1.00 43.86 ? 501  HIS   A ND1   1 
ATOM   3474  C  CD2   . HIS   A  1 503  ? -26.448 41.743  79.520  1.00 40.67 ? 501  HIS   A CD2   1 
ATOM   3475  C  CE1   . HIS   A  1 503  ? -26.080 40.169  81.004  1.00 45.28 ? 501  HIS   A CE1   1 
ATOM   3476  N  NE2   . HIS   A  1 503  ? -25.489 40.999  80.164  1.00 43.92 ? 501  HIS   A NE2   1 
ATOM   3477  N  N     . ARG   A  1 504  ? -30.566 39.052  79.679  1.00 33.69 ? 502  ARG   A N     1 
ATOM   3478  C  CA    . ARG   A  1 504  ? -30.572 37.653  80.080  1.00 36.04 ? 502  ARG   A CA    1 
ATOM   3479  C  C     . ARG   A  1 504  ? -30.962 36.732  78.932  1.00 40.44 ? 502  ARG   A C     1 
ATOM   3480  O  O     . ARG   A  1 504  ? -30.434 35.619  78.835  1.00 39.71 ? 502  ARG   A O     1 
ATOM   3481  C  CB    . ARG   A  1 504  ? -31.506 37.472  81.276  1.00 35.21 ? 502  ARG   A CB    1 
ATOM   3482  C  CG    . ARG   A  1 504  ? -31.022 38.230  82.514  1.00 35.65 ? 502  ARG   A CG    1 
ATOM   3483  C  CD    . ARG   A  1 504  ? -32.126 38.413  83.535  1.00 40.05 ? 502  ARG   A CD    1 
ATOM   3484  N  NE    . ARG   A  1 504  ? -32.842 37.175  83.817  1.00 35.86 ? 502  ARG   A NE    1 
ATOM   3485  C  CZ    . ARG   A  1 504  ? -32.404 36.225  84.632  1.00 41.06 ? 502  ARG   A CZ    1 
ATOM   3486  N  NH1   . ARG   A  1 504  ? -31.212 36.300  85.206  1.00 39.70 ? 502  ARG   A NH1   1 
ATOM   3487  N  NH2   . ARG   A  1 504  ? -33.181 35.173  84.878  1.00 46.31 ? 502  ARG   A NH2   1 
ATOM   3488  N  N     . ILE   A  1 505  ? -31.859 37.174  78.044  1.00 38.37 ? 503  ILE   A N     1 
ATOM   3489  C  CA    . ILE   A  1 505  ? -32.239 36.327  76.913  1.00 38.83 ? 503  ILE   A CA    1 
ATOM   3490  C  C     . ILE   A  1 505  ? -31.022 36.019  76.044  1.00 41.08 ? 503  ILE   A C     1 
ATOM   3491  O  O     . ILE   A  1 505  ? -30.922 34.930  75.464  1.00 40.73 ? 503  ILE   A O     1 
ATOM   3492  C  CB    . ILE   A  1 505  ? -33.379 36.987  76.105  1.00 38.89 ? 503  ILE   A CB    1 
ATOM   3493  C  CG1   . ILE   A  1 505  ? -33.853 36.078  74.973  1.00 40.66 ? 503  ILE   A CG1   1 
ATOM   3494  C  CG2   . ILE   A  1 505  ? -32.939 38.308  75.523  1.00 40.16 ? 503  ILE   A CG2   1 
ATOM   3495  C  CD1   . ILE   A  1 505  ? -34.649 34.898  75.437  1.00 36.69 ? 503  ILE   A CD1   1 
ATOM   3496  N  N     . ASN   A  1 506  ? -30.068 36.946  75.962  1.00 38.85 ? 504  ASN   A N     1 
ATOM   3497  C  CA    . ASN   A  1 506  ? -28.856 36.744  75.177  1.00 40.24 ? 504  ASN   A CA    1 
ATOM   3498  C  C     . ASN   A  1 506  ? -27.716 36.132  75.980  1.00 45.31 ? 504  ASN   A C     1 
ATOM   3499  O  O     . ASN   A  1 506  ? -26.659 35.845  75.409  1.00 45.10 ? 504  ASN   A O     1 
ATOM   3500  C  CB    . ASN   A  1 506  ? -28.399 38.069  74.562  1.00 44.23 ? 504  ASN   A CB    1 
ATOM   3501  C  CG    . ASN   A  1 506  ? -29.319 38.538  73.449  1.00 44.36 ? 504  ASN   A CG    1 
ATOM   3502  O  OD1   . ASN   A  1 506  ? -29.913 37.726  72.739  1.00 47.49 ? 504  ASN   A OD1   1 
ATOM   3503  N  ND2   . ASN   A  1 506  ? -29.437 39.850  73.289  1.00 47.33 ? 504  ASN   A ND2   1 
ATOM   3504  N  N     . ASP   A  1 507  ? -27.903 35.915  77.282  1.00 43.22 ? 505  ASP   A N     1 
ATOM   3505  C  CA    . ASP   A  1 507  ? -26.856 35.349  78.122  1.00 44.54 ? 505  ASP   A CA    1 
ATOM   3506  C  C     . ASP   A  1 507  ? -26.954 33.832  78.074  1.00 45.36 ? 505  ASP   A C     1 
ATOM   3507  O  O     . ASP   A  1 507  ? -27.940 33.270  78.578  1.00 41.04 ? 505  ASP   A O     1 
ATOM   3508  C  CB    . ASP   A  1 507  ? -26.991 35.847  79.553  1.00 44.62 ? 505  ASP   A CB    1 
ATOM   3509  C  CG    . ASP   A  1 507  ? -25.769 35.536  80.398  1.00 47.68 ? 505  ASP   A CG    1 
ATOM   3510  O  OD1   . ASP   A  1 507  ? -25.142 34.475  80.184  1.00 46.45 ? 505  ASP   A OD1   1 
ATOM   3511  O  OD2   . ASP   A  1 507  ? -25.438 36.358  81.278  1.00 44.68 ? 505  ASP   A OD2   1 
ATOM   3512  N  N     . PRO   A  1 508  ? -25.966 33.129  77.511  1.00 49.08 ? 506  PRO   A N     1 
ATOM   3513  C  CA    . PRO   A  1 508  ? -26.086 31.667  77.400  1.00 45.65 ? 506  PRO   A CA    1 
ATOM   3514  C  C     . PRO   A  1 508  ? -26.120 30.964  78.745  1.00 44.06 ? 506  PRO   A C     1 
ATOM   3515  O  O     . PRO   A  1 508  ? -26.699 29.877  78.845  1.00 48.37 ? 506  PRO   A O     1 
ATOM   3516  C  CB    . PRO   A  1 508  ? -24.843 31.268  76.586  1.00 48.84 ? 506  PRO   A CB    1 
ATOM   3517  C  CG    . PRO   A  1 508  ? -24.311 32.555  76.001  1.00 51.93 ? 506  PRO   A CG    1 
ATOM   3518  C  CD    . PRO   A  1 508  ? -24.692 33.627  76.968  1.00 46.59 ? 506  PRO   A CD    1 
ATOM   3519  N  N     . LYS   A  1 509  ? -25.523 31.550  79.783  1.00 40.84 ? 507  LYS   A N     1 
ATOM   3520  C  CA    . LYS   A  1 509  ? -25.538 30.936  81.104  1.00 46.13 ? 507  LYS   A CA    1 
ATOM   3521  C  C     . LYS   A  1 509  ? -26.892 31.038  81.797  1.00 48.13 ? 507  LYS   A C     1 
ATOM   3522  O  O     . LYS   A  1 509  ? -27.046 30.478  82.889  1.00 47.84 ? 507  LYS   A O     1 
ATOM   3523  C  CB    . LYS   A  1 509  ? -24.460 31.568  81.986  1.00 50.10 ? 507  LYS   A CB    1 
ATOM   3524  N  N     . VAL   A  1 510  ? -27.865 31.734  81.212  1.00 46.71 ? 508  VAL   A N     1 
ATOM   3525  C  CA    . VAL   A  1 510  ? -29.201 31.847  81.784  1.00 42.07 ? 508  VAL   A CA    1 
ATOM   3526  C  C     . VAL   A  1 510  ? -30.105 30.855  81.069  1.00 40.06 ? 508  VAL   A C     1 
ATOM   3527  O  O     . VAL   A  1 510  ? -30.357 30.986  79.864  1.00 42.17 ? 508  VAL   A O     1 
ATOM   3528  C  CB    . VAL   A  1 510  ? -29.751 33.277  81.665  1.00 42.37 ? 508  VAL   A CB    1 
ATOM   3529  C  CG1   . VAL   A  1 510  ? -31.174 33.335  82.214  1.00 37.94 ? 508  VAL   A CG1   1 
ATOM   3530  C  CG2   . VAL   A  1 510  ? -28.848 34.261  82.393  1.00 38.58 ? 508  VAL   A CG2   1 
ATOM   3531  N  N     . SER   A  1 511  ? -30.597 29.865  81.803  1.00 36.49 ? 509  SER   A N     1 
ATOM   3532  C  CA    . SER   A  1 511  ? -31.475 28.882  81.199  1.00 38.03 ? 509  SER   A CA    1 
ATOM   3533  C  C     . SER   A  1 511  ? -32.861 29.474  80.966  1.00 39.71 ? 509  SER   A C     1 
ATOM   3534  O  O     . SER   A  1 511  ? -33.220 30.534  81.492  1.00 37.53 ? 509  SER   A O     1 
ATOM   3535  C  CB    . SER   A  1 511  ? -31.583 27.637  82.078  1.00 42.13 ? 509  SER   A CB    1 
ATOM   3536  O  OG    . SER   A  1 511  ? -32.204 27.944  83.312  1.00 36.85 ? 509  SER   A OG    1 
ATOM   3537  N  N     . ILE   A  1 512  ? -33.646 28.763  80.159  1.00 37.65 ? 510  ILE   A N     1 
ATOM   3538  C  CA    . ILE   A  1 512  ? -35.041 29.133  79.980  1.00 39.56 ? 510  ILE   A CA    1 
ATOM   3539  C  C     . ILE   A  1 512  ? -35.801 28.967  81.288  1.00 40.21 ? 510  ILE   A C     1 
ATOM   3540  O  O     . ILE   A  1 512  ? -36.645 29.802  81.640  1.00 36.06 ? 510  ILE   A O     1 
ATOM   3541  C  CB    . ILE   A  1 512  ? -35.659 28.308  78.838  1.00 37.55 ? 510  ILE   A CB    1 
ATOM   3542  C  CG1   . ILE   A  1 512  ? -34.894 28.584  77.541  1.00 33.87 ? 510  ILE   A CG1   1 
ATOM   3543  C  CG2   . ILE   A  1 512  ? -37.142 28.619  78.691  1.00 37.74 ? 510  ILE   A CG2   1 
ATOM   3544  C  CD1   . ILE   A  1 512  ? -35.552 28.033  76.316  1.00 38.21 ? 510  ILE   A CD1   1 
ATOM   3545  N  N     . ASP   A  1 513  ? -35.488 27.906  82.045  1.00 39.56 ? 511  ASP   A N     1 
ATOM   3546  C  CA    . ASP   A  1 513  ? -36.096 27.700  83.357  1.00 39.38 ? 511  ASP   A CA    1 
ATOM   3547  C  C     . ASP   A  1 513  ? -35.924 28.920  84.251  1.00 38.30 ? 511  ASP   A C     1 
ATOM   3548  O  O     . ASP   A  1 513  ? -36.858 29.318  84.956  1.00 38.94 ? 511  ASP   A O     1 
ATOM   3549  C  CB    . ASP   A  1 513  ? -35.491 26.470  84.034  1.00 41.08 ? 511  ASP   A CB    1 
ATOM   3550  C  CG    . ASP   A  1 513  ? -35.961 25.175  83.415  1.00 50.92 ? 511  ASP   A CG    1 
ATOM   3551  O  OD1   . ASP   A  1 513  ? -37.131 25.120  82.971  1.00 51.16 ? 511  ASP   A OD1   1 
ATOM   3552  O  OD2   . ASP   A  1 513  ? -35.161 24.213  83.376  1.00 54.47 ? 511  ASP   A OD2   1 
ATOM   3553  N  N     . GLU   A  1 514  ? -34.732 29.521  84.241  1.00 35.43 ? 512  GLU   A N     1 
ATOM   3554  C  CA    . GLU   A  1 514  ? -34.524 30.750  84.999  1.00 36.96 ? 512  GLU   A CA    1 
ATOM   3555  C  C     . GLU   A  1 514  ? -35.383 31.881  84.454  1.00 35.58 ? 512  GLU   A C     1 
ATOM   3556  O  O     . GLU   A  1 514  ? -35.914 32.689  85.221  1.00 38.73 ? 512  GLU   A O     1 
ATOM   3557  C  CB    . GLU   A  1 514  ? -33.051 31.161  84.970  1.00 37.07 ? 512  GLU   A CB    1 
ATOM   3558  C  CG    . GLU   A  1 514  ? -32.095 30.160  85.593  1.00 46.16 ? 512  GLU   A CG    1 
ATOM   3559  C  CD    . GLU   A  1 514  ? -30.642 30.593  85.472  1.00 48.09 ? 512  GLU   A CD    1 
ATOM   3560  O  OE1   . GLU   A  1 514  ? -30.286 31.663  86.014  1.00 56.95 ? 512  GLU   A OE1   1 
ATOM   3561  O  OE2   . GLU   A  1 514  ? -29.855 29.871  84.825  1.00 50.76 ? 512  GLU   A OE2   1 
ATOM   3562  N  N     . LEU   A  1 515  ? -35.523 31.958  83.128  1.00 38.59 ? 513  LEU   A N     1 
ATOM   3563  C  CA    . LEU   A  1 515  ? -36.237 33.075  82.517  1.00 35.17 ? 513  LEU   A CA    1 
ATOM   3564  C  C     . LEU   A  1 515  ? -37.746 32.960  82.689  1.00 33.71 ? 513  LEU   A C     1 
ATOM   3565  O  O     . LEU   A  1 515  ? -38.449 33.975  82.649  1.00 30.68 ? 513  LEU   A O     1 
ATOM   3566  C  CB    . LEU   A  1 515  ? -35.900 33.169  81.032  1.00 35.97 ? 513  LEU   A CB    1 
ATOM   3567  C  CG    . LEU   A  1 515  ? -34.499 33.621  80.639  1.00 37.59 ? 513  LEU   A CG    1 
ATOM   3568  C  CD1   . LEU   A  1 515  ? -34.324 33.434  79.141  1.00 37.00 ? 513  LEU   A CD1   1 
ATOM   3569  C  CD2   . LEU   A  1 515  ? -34.279 35.066  81.029  1.00 33.68 ? 513  LEU   A CD2   1 
ATOM   3570  N  N     . ILE   A  1 516  ? -38.269 31.749  82.859  1.00 33.08 ? 514  ILE   A N     1 
ATOM   3571  C  CA    . ILE   A  1 516  ? -39.701 31.555  83.013  1.00 33.66 ? 514  ILE   A CA    1 
ATOM   3572  C  C     . ILE   A  1 516  ? -40.093 31.368  84.474  1.00 33.98 ? 514  ILE   A C     1 
ATOM   3573  O  O     . ILE   A  1 516  ? -41.245 31.016  84.764  1.00 34.92 ? 514  ILE   A O     1 
ATOM   3574  C  CB    . ILE   A  1 516  ? -40.190 30.380  82.156  1.00 33.88 ? 514  ILE   A CB    1 
ATOM   3575  C  CG1   . ILE   A  1 516  ? -39.624 29.061  82.689  1.00 33.09 ? 514  ILE   A CG1   1 
ATOM   3576  C  CG2   . ILE   A  1 516  ? -39.797 30.608  80.696  1.00 30.63 ? 514  ILE   A CG2   1 
ATOM   3577  C  CD1   . ILE   A  1 516  ? -40.304 27.837  82.102  1.00 36.85 ? 514  ILE   A CD1   1 
ATOM   3578  N  N     . ALA   A  1 517  ? -39.159 31.590  85.399  1.00 33.04 ? 515  ALA   A N     1 
ATOM   3579  C  CA    . ALA   A  1 517  ? -39.473 31.556  86.820  1.00 36.40 ? 515  ALA   A CA    1 
ATOM   3580  C  C     . ALA   A  1 517  ? -40.538 32.593  87.146  1.00 34.79 ? 515  ALA   A C     1 
ATOM   3581  O  O     . ALA   A  1 517  ? -40.492 33.726  86.664  1.00 30.82 ? 515  ALA   A O     1 
ATOM   3582  C  CB    . ALA   A  1 517  ? -38.214 31.817  87.650  1.00 35.76 ? 515  ALA   A CB    1 
ATOM   3583  N  N     . ASP   A  1 518  ? -41.498 32.194  87.960  1.00 34.19 ? 516  ASP   A N     1 
ATOM   3584  C  CA    . ASP   A  1 518  ? -42.629 33.036  88.316  1.00 33.03 ? 516  ASP   A CA    1 
ATOM   3585  C  C     . ASP   A  1 518  ? -42.250 33.988  89.444  1.00 29.04 ? 516  ASP   A C     1 
ATOM   3586  O  O     . ASP   A  1 518  ? -42.139 33.564  90.602  1.00 26.58 ? 516  ASP   A O     1 
ATOM   3587  C  CB    . ASP   A  1 518  ? -43.807 32.155  88.724  1.00 33.38 ? 516  ASP   A CB    1 
ATOM   3588  C  CG    . ASP   A  1 518  ? -45.077 32.942  88.954  1.00 34.08 ? 516  ASP   A CG    1 
ATOM   3589  O  OD1   . ASP   A  1 518  ? -45.080 34.182  88.790  1.00 32.59 ? 516  ASP   A OD1   1 
ATOM   3590  O  OD2   . ASP   A  1 518  ? -46.083 32.305  89.300  1.00 36.57 ? 516  ASP   A OD2   1 
ATOM   3591  N  N     . PRO   A  1 519  ? -42.077 35.281  89.164  1.00 29.96 ? 517  PRO   A N     1 
ATOM   3592  C  CA    . PRO   A  1 519  ? -41.655 36.196  90.236  1.00 29.21 ? 517  PRO   A CA    1 
ATOM   3593  C  C     . PRO   A  1 519  ? -42.631 36.226  91.402  1.00 27.80 ? 517  PRO   A C     1 
ATOM   3594  O  O     . PRO   A  1 519  ? -42.210 36.403  92.553  1.00 26.62 ? 517  PRO   A O     1 
ATOM   3595  C  CB    . PRO   A  1 519  ? -41.569 37.555  89.521  1.00 29.13 ? 517  PRO   A CB    1 
ATOM   3596  C  CG    . PRO   A  1 519  ? -42.508 37.452  88.396  1.00 27.21 ? 517  PRO   A CG    1 
ATOM   3597  C  CD    . PRO   A  1 519  ? -42.499 36.005  87.949  1.00 31.05 ? 517  PRO   A CD    1 
ATOM   3598  N  N     . VAL   A  1 520  ? -43.923 36.028  91.131  1.00 28.97 ? 518  VAL   A N     1 
ATOM   3599  C  CA    . VAL   A  1 520  ? -44.932 36.023  92.188  1.00 30.55 ? 518  VAL   A CA    1 
ATOM   3600  C  C     . VAL   A  1 520  ? -44.630 34.930  93.206  1.00 32.13 ? 518  VAL   A C     1 
ATOM   3601  O  O     . VAL   A  1 520  ? -44.618 35.169  94.420  1.00 30.58 ? 518  VAL   A O     1 
ATOM   3602  C  CB    . VAL   A  1 520  ? -46.332 35.848  91.579  1.00 32.01 ? 518  VAL   A CB    1 
ATOM   3603  C  CG1   . VAL   A  1 520  ? -47.399 35.854  92.670  1.00 31.86 ? 518  VAL   A CG1   1 
ATOM   3604  C  CG2   . VAL   A  1 520  ? -46.592 36.921  90.518  1.00 27.99 ? 518  VAL   A CG2   1 
ATOM   3605  N  N     . GLU   A  1 521  ? -44.375 33.713  92.723  1.00 32.65 ? 519  GLU   A N     1 
ATOM   3606  C  CA    . GLU   A  1 521  ? -44.126 32.596  93.628  1.00 32.09 ? 519  GLU   A CA    1 
ATOM   3607  C  C     . GLU   A  1 521  ? -42.713 32.613  94.190  1.00 34.03 ? 519  GLU   A C     1 
ATOM   3608  O  O     . GLU   A  1 521  ? -42.491 32.109  95.297  1.00 32.59 ? 519  GLU   A O     1 
ATOM   3609  C  CB    . GLU   A  1 521  ? -44.401 31.273  92.917  1.00 30.61 ? 519  GLU   A CB    1 
ATOM   3610  C  CG    . GLU   A  1 521  ? -45.853 31.099  92.501  1.00 36.68 ? 519  GLU   A CG    1 
ATOM   3611  C  CD    . GLU   A  1 521  ? -46.827 31.220  93.666  1.00 40.31 ? 519  GLU   A CD    1 
ATOM   3612  O  OE1   . GLU   A  1 521  ? -46.447 30.896  94.816  1.00 40.41 ? 519  GLU   A OE1   1 
ATOM   3613  O  OE2   . GLU   A  1 521  ? -47.982 31.638  93.428  1.00 44.08 ? 519  GLU   A OE2   1 
ATOM   3614  N  N     . VAL   A  1 522  ? -41.748 33.172  93.450  1.00 30.32 ? 520  VAL   A N     1 
ATOM   3615  C  CA    . VAL   A  1 522  ? -40.423 33.386  94.022  1.00 29.56 ? 520  VAL   A CA    1 
ATOM   3616  C  C     . VAL   A  1 522  ? -40.504 34.361  95.190  1.00 33.91 ? 520  VAL   A C     1 
ATOM   3617  O  O     . VAL   A  1 522  ? -39.920 34.127  96.253  1.00 32.12 ? 520  VAL   A O     1 
ATOM   3618  C  CB    . VAL   A  1 522  ? -39.433 33.873  92.947  1.00 30.97 ? 520  VAL   A CB    1 
ATOM   3619  C  CG1   . VAL   A  1 522  ? -38.073 34.180  93.577  1.00 27.68 ? 520  VAL   A CG1   1 
ATOM   3620  C  CG2   . VAL   A  1 522  ? -39.291 32.843  91.842  1.00 32.43 ? 520  VAL   A CG2   1 
ATOM   3621  N  N     . VAL   A  1 523  ? -41.235 35.464  95.018  1.00 26.66 ? 521  VAL   A N     1 
ATOM   3622  C  CA    . VAL   A  1 523  ? -41.349 36.442  96.096  1.00 27.93 ? 521  VAL   A CA    1 
ATOM   3623  C  C     . VAL   A  1 523  ? -42.099 35.850  97.286  1.00 30.30 ? 521  VAL   A C     1 
ATOM   3624  O  O     . VAL   A  1 523  ? -41.698 36.038  98.441  1.00 30.89 ? 521  VAL   A O     1 
ATOM   3625  C  CB    . VAL   A  1 523  ? -42.020 37.727  95.585  1.00 26.80 ? 521  VAL   A CB    1 
ATOM   3626  C  CG1   . VAL   A  1 523  ? -42.454 38.589  96.757  1.00 26.99 ? 521  VAL   A CG1   1 
ATOM   3627  C  CG2   . VAL   A  1 523  ? -41.044 38.494  94.706  1.00 27.67 ? 521  VAL   A CG2   1 
ATOM   3628  N  N     . ARG   A  1 524  ? -43.192 35.129  97.025  1.00 30.99 ? 522  ARG   A N     1 
ATOM   3629  C  CA    . ARG   A  1 524  ? -43.976 34.548  98.112  1.00 34.56 ? 522  ARG   A CA    1 
ATOM   3630  C  C     . ARG   A  1 524  ? -43.129 33.640  98.997  1.00 39.53 ? 522  ARG   A C     1 
ATOM   3631  O  O     . ARG   A  1 524  ? -43.350 33.577  100.211 1.00 40.06 ? 522  ARG   A O     1 
ATOM   3632  C  CB    . ARG   A  1 524  ? -45.161 33.769  97.547  1.00 32.37 ? 522  ARG   A CB    1 
ATOM   3633  C  CG    . ARG   A  1 524  ? -46.220 33.396  98.585  1.00 35.72 ? 522  ARG   A CG    1 
ATOM   3634  C  CD    . ARG   A  1 524  ? -47.111 32.279  98.084  1.00 35.93 ? 522  ARG   A CD    1 
ATOM   3635  N  NE    . ARG   A  1 524  ? -47.716 32.596  96.796  1.00 39.67 ? 522  ARG   A NE    1 
ATOM   3636  C  CZ    . ARG   A  1 524  ? -48.820 33.315  96.641  1.00 36.07 ? 522  ARG   A CZ    1 
ATOM   3637  N  NH1   . ARG   A  1 524  ? -49.441 33.859  97.672  1.00 38.36 ? 522  ARG   A NH1   1 
ATOM   3638  N  NH2   . ARG   A  1 524  ? -49.320 33.484  95.422  1.00 36.13 ? 522  ARG   A NH2   1 
ATOM   3639  N  N     . ALA   A  1 525  ? -42.139 32.964  98.420  1.00 36.68 ? 523  ALA   A N     1 
ATOM   3640  C  CA    . ALA   A  1 525  ? -41.327 31.996  99.142  1.00 39.35 ? 523  ALA   A CA    1 
ATOM   3641  C  C     . ALA   A  1 525  ? -40.119 32.610  99.841  1.00 38.56 ? 523  ALA   A C     1 
ATOM   3642  O  O     . ALA   A  1 525  ? -39.397 31.890  100.537 1.00 36.34 ? 523  ALA   A O     1 
ATOM   3643  C  CB    . ALA   A  1 525  ? -40.856 30.896  98.186  1.00 36.01 ? 523  ALA   A CB    1 
ATOM   3644  N  N     . MET   A  1 526  ? -39.875 33.907  99.685  1.00 33.76 ? 524  MET   A N     1 
ATOM   3645  C  CA    . MET   A  1 526  ? -38.707 34.501  100.312 1.00 39.70 ? 524  MET   A CA    1 
ATOM   3646  C  C     . MET   A  1 526  ? -38.900 34.595  101.826 1.00 40.06 ? 524  MET   A C     1 
ATOM   3647  O  O     . MET   A  1 526  ? -40.033 34.666  102.310 1.00 37.19 ? 524  MET   A O     1 
ATOM   3648  C  CB    . MET   A  1 526  ? -38.435 35.881  99.729  1.00 38.90 ? 524  MET   A CB    1 
ATOM   3649  C  CG    . MET   A  1 526  ? -38.023 35.814  98.289  1.00 37.92 ? 524  MET   A CG    1 
ATOM   3650  S  SD    . MET   A  1 526  ? -37.602 37.420  97.632  1.00 47.47 ? 524  MET   A SD    1 
ATOM   3651  C  CE    . MET   A  1 526  ? -36.973 36.952  96.019  1.00 45.33 ? 524  MET   A CE    1 
ATOM   3652  N  N     . PRO   A  1 527  ? -37.805 34.578  102.597 1.00 37.56 ? 525  PRO   A N     1 
ATOM   3653  C  CA    . PRO   A  1 527  ? -37.951 34.628  104.063 1.00 39.65 ? 525  PRO   A CA    1 
ATOM   3654  C  C     . PRO   A  1 527  ? -38.677 35.868  104.552 1.00 41.85 ? 525  PRO   A C     1 
ATOM   3655  O  O     . PRO   A  1 527  ? -39.524 35.769  105.449 1.00 41.46 ? 525  PRO   A O     1 
ATOM   3656  C  CB    . PRO   A  1 527  ? -36.500 34.575  104.568 1.00 40.05 ? 525  PRO   A CB    1 
ATOM   3657  C  CG    . PRO   A  1 527  ? -35.647 34.929  103.386 1.00 41.17 ? 525  PRO   A CG    1 
ATOM   3658  C  CD    . PRO   A  1 527  ? -36.398 34.458  102.179 1.00 41.15 ? 525  PRO   A CD    1 
ATOM   3659  N  N     . VAL   A  1 528  ? -38.384 37.034  103.982 1.00 39.42 ? 526  VAL   A N     1 
ATOM   3660  C  CA    . VAL   A  1 528  ? -39.090 38.271  104.301 1.00 34.36 ? 526  VAL   A CA    1 
ATOM   3661  C  C     . VAL   A  1 528  ? -39.646 38.824  102.999 1.00 33.26 ? 526  VAL   A C     1 
ATOM   3662  O  O     . VAL   A  1 528  ? -38.889 39.334  102.160 1.00 29.22 ? 526  VAL   A O     1 
ATOM   3663  C  CB    . VAL   A  1 528  ? -38.185 39.299  104.986 1.00 35.59 ? 526  VAL   A CB    1 
ATOM   3664  C  CG1   . VAL   A  1 528  ? -38.956 40.606  105.192 1.00 34.84 ? 526  VAL   A CG1   1 
ATOM   3665  C  CG2   . VAL   A  1 528  ? -37.672 38.748  106.307 1.00 40.38 ? 526  VAL   A CG2   1 
ATOM   3666  N  N     . VAL   A  1 529  ? -40.963 38.723  102.826 1.00 30.07 ? 527  VAL   A N     1 
ATOM   3667  C  CA    . VAL   A  1 529  ? -41.586 39.179  101.591 1.00 30.70 ? 527  VAL   A CA    1 
ATOM   3668  C  C     . VAL   A  1 529  ? -41.420 40.687  101.479 1.00 29.69 ? 527  VAL   A C     1 
ATOM   3669  O  O     . VAL   A  1 529  ? -41.789 41.440  102.389 1.00 29.18 ? 527  VAL   A O     1 
ATOM   3670  C  CB    . VAL   A  1 529  ? -43.064 38.771  101.542 1.00 27.63 ? 527  VAL   A CB    1 
ATOM   3671  C  CG1   . VAL   A  1 529  ? -43.753 39.418  100.338 1.00 30.67 ? 527  VAL   A CG1   1 
ATOM   3672  C  CG2   . VAL   A  1 529  ? -43.190 37.251  101.480 1.00 34.91 ? 527  VAL   A CG2   1 
ATOM   3673  N  N     . GLY   A  1 530  ? -40.834 41.133  100.373 1.00 25.99 ? 528  GLY   A N     1 
ATOM   3674  C  CA    . GLY   A  1 530  ? -40.638 42.551  100.168 1.00 24.42 ? 528  GLY   A CA    1 
ATOM   3675  C  C     . GLY   A  1 530  ? -39.411 43.149  100.817 1.00 26.10 ? 528  GLY   A C     1 
ATOM   3676  O  O     . GLY   A  1 530  ? -39.288 44.377  100.841 1.00 21.44 ? 528  GLY   A O     1 
ATOM   3677  N  N     . ALA   A  1 531  ? -38.495 42.336  101.341 1.00 27.24 ? 529  ALA   A N     1 
ATOM   3678  C  CA    . ALA   A  1 531  ? -37.258 42.885  101.883 1.00 25.73 ? 529  ALA   A CA    1 
ATOM   3679  C  C     . ALA   A  1 531  ? -36.557 43.750  100.842 1.00 26.49 ? 529  ALA   A C     1 
ATOM   3680  O  O     . ALA   A  1 531  ? -36.469 43.385  99.667  1.00 23.87 ? 529  ALA   A O     1 
ATOM   3681  C  CB    . ALA   A  1 531  ? -36.330 41.759  102.343 1.00 26.30 ? 529  ALA   A CB    1 
ATOM   3682  N  N     . LYS   A  1 532  ? -36.078 44.913  101.286 1.00 23.54 ? 530  LYS   A N     1 
ATOM   3683  C  CA    . LYS   A  1 532  ? -35.262 45.788  100.455 1.00 26.76 ? 530  LYS   A CA    1 
ATOM   3684  C  C     . LYS   A  1 532  ? -34.023 45.049  99.958  1.00 25.73 ? 530  LYS   A C     1 
ATOM   3685  O  O     . LYS   A  1 532  ? -33.520 44.133  100.610 1.00 24.80 ? 530  LYS   A O     1 
ATOM   3686  C  CB    . LYS   A  1 532  ? -34.843 47.026  101.259 1.00 28.49 ? 530  LYS   A CB    1 
ATOM   3687  C  CG    . LYS   A  1 532  ? -33.791 47.907  100.581 1.00 34.58 ? 530  LYS   A CG    1 
ATOM   3688  C  CD    . LYS   A  1 532  ? -33.320 49.053  101.464 1.00 27.83 ? 530  LYS   A CD    1 
ATOM   3689  C  CE    . LYS   A  1 532  ? -32.538 48.551  102.665 1.00 31.70 ? 530  LYS   A CE    1 
ATOM   3690  N  NZ    . LYS   A  1 532  ? -31.235 47.913  102.303 1.00 28.92 ? 530  LYS   A NZ    1 
ATOM   3691  N  N     . HIS   A  1 533  ? -33.528 45.456  98.794  1.00 22.32 ? 531  HIS   A N     1 
ATOM   3692  C  CA    . HIS   A  1 533  ? -32.277 44.909  98.283  1.00 24.78 ? 531  HIS   A CA    1 
ATOM   3693  C  C     . HIS   A  1 533  ? -31.165 45.087  99.309  1.00 25.14 ? 531  HIS   A C     1 
ATOM   3694  O  O     . HIS   A  1 533  ? -31.005 46.167  99.885  1.00 26.53 ? 531  HIS   A O     1 
ATOM   3695  C  CB    . HIS   A  1 533  ? -31.892 45.591  96.969  1.00 25.59 ? 531  HIS   A CB    1 
ATOM   3696  C  CG    . HIS   A  1 533  ? -30.842 44.854  96.203  1.00 30.03 ? 531  HIS   A CG    1 
ATOM   3697  N  ND1   . HIS   A  1 533  ? -29.524 44.807  96.606  1.00 31.32 ? 531  HIS   A ND1   1 
ATOM   3698  C  CD2   . HIS   A  1 533  ? -30.917 44.112  95.072  1.00 34.74 ? 531  HIS   A CD2   1 
ATOM   3699  C  CE1   . HIS   A  1 533  ? -28.830 44.075  95.753  1.00 31.19 ? 531  HIS   A CE1   1 
ATOM   3700  N  NE2   . HIS   A  1 533  ? -29.651 43.641  94.813  1.00 35.80 ? 531  HIS   A NE2   1 
ATOM   3701  N  N     . ASP   A  1 534  ? -30.399 44.013  99.521  1.00 26.49 ? 532  ASP   A N     1 
ATOM   3702  C  CA    . ASP   A  1 534  ? -29.335 43.986  100.522 1.00 31.57 ? 532  ASP   A CA    1 
ATOM   3703  C  C     . ASP   A  1 534  ? -28.249 45.022  100.268 1.00 28.36 ? 532  ASP   A C     1 
ATOM   3704  O  O     . ASP   A  1 534  ? -27.601 45.477  101.218 1.00 28.86 ? 532  ASP   A O     1 
ATOM   3705  C  CB    . ASP   A  1 534  ? -28.686 42.599  100.560 1.00 34.00 ? 532  ASP   A CB    1 
ATOM   3706  C  CG    . ASP   A  1 534  ? -29.462 41.615  101.400 1.00 46.42 ? 532  ASP   A CG    1 
ATOM   3707  O  OD1   . ASP   A  1 534  ? -30.435 42.041  102.060 1.00 48.65 ? 532  ASP   A OD1   1 
ATOM   3708  O  OD2   . ASP   A  1 534  ? -29.096 40.416  101.405 1.00 57.12 ? 532  ASP   A OD2   1 
ATOM   3709  N  N     . ARG   A  1 535  ? -27.996 45.373  99.009  1.00 24.80 ? 533  ARG   A N     1 
ATOM   3710  C  CA    . ARG   A  1 535  ? -26.844 46.192  98.667  1.00 25.17 ? 533  ARG   A CA    1 
ATOM   3711  C  C     . ARG   A  1 535  ? -27.204 47.651  98.414  1.00 27.55 ? 533  ARG   A C     1 
ATOM   3712  O  O     . ARG   A  1 535  ? -26.344 48.429  97.991  1.00 29.63 ? 533  ARG   A O     1 
ATOM   3713  C  CB    . ARG   A  1 535  ? -26.126 45.606  97.448  1.00 30.96 ? 533  ARG   A CB    1 
ATOM   3714  N  N     . ILE   A  1 536  ? -28.438 48.053  98.678  1.00 24.08 ? 534  ILE   A N     1 
ATOM   3715  C  CA    . ILE   A  1 536  ? -28.841 49.442  98.500  1.00 26.30 ? 534  ILE   A CA    1 
ATOM   3716  C  C     . ILE   A  1 536  ? -29.189 50.012  99.866  1.00 24.09 ? 534  ILE   A C     1 
ATOM   3717  O  O     . ILE   A  1 536  ? -30.050 49.473  100.572 1.00 25.27 ? 534  ILE   A O     1 
ATOM   3718  C  CB    . ILE   A  1 536  ? -30.019 49.573  97.527  1.00 25.69 ? 534  ILE   A CB    1 
ATOM   3719  C  CG1   . ILE   A  1 536  ? -29.587 49.097  96.139  1.00 27.00 ? 534  ILE   A CG1   1 
ATOM   3720  C  CG2   . ILE   A  1 536  ? -30.517 51.017  97.480  1.00 26.95 ? 534  ILE   A CG2   1 
ATOM   3721  C  CD1   . ILE   A  1 536  ? -30.742 48.824  95.227  1.00 28.75 ? 534  ILE   A CD1   1 
ATOM   3722  N  N     . ALA   A  1 537  ? -28.514 51.091  100.243 1.00 20.47 ? 535  ALA   A N     1 
ATOM   3723  C  CA    . ALA   A  1 537  ? -28.755 51.698  101.541 1.00 21.61 ? 535  ALA   A CA    1 
ATOM   3724  C  C     . ALA   A  1 537  ? -29.993 52.580  101.483 1.00 21.48 ? 535  ALA   A C     1 
ATOM   3725  O  O     . ALA   A  1 537  ? -30.164 53.366  100.546 1.00 19.95 ? 535  ALA   A O     1 
ATOM   3726  C  CB    . ALA   A  1 537  ? -27.547 52.524  101.984 1.00 22.96 ? 535  ALA   A CB    1 
ATOM   3727  N  N     . LEU   A  1 538  ? -30.861 52.441  102.481 1.00 19.42 ? 536  LEU   A N     1 
ATOM   3728  C  CA    . LEU   A  1 538  ? -31.825 53.496  102.726 1.00 19.19 ? 536  LEU   A CA    1 
ATOM   3729  C  C     . LEU   A  1 538  ? -31.069 54.807  102.915 1.00 20.96 ? 536  LEU   A C     1 
ATOM   3730  O  O     . LEU   A  1 538  ? -29.921 54.805  103.369 1.00 21.86 ? 536  LEU   A O     1 
ATOM   3731  C  CB    . LEU   A  1 538  ? -32.659 53.197  103.971 1.00 19.92 ? 536  LEU   A CB    1 
ATOM   3732  C  CG    . LEU   A  1 538  ? -33.630 52.031  103.847 1.00 20.92 ? 536  LEU   A CG    1 
ATOM   3733  C  CD1   . LEU   A  1 538  ? -34.169 51.645  105.210 1.00 28.67 ? 536  LEU   A CD1   1 
ATOM   3734  C  CD2   . LEU   A  1 538  ? -34.771 52.390  102.895 1.00 24.88 ? 536  LEU   A CD2   1 
ATOM   3735  N  N     . PRO   A  1 539  ? -31.675 55.934  102.561 1.00 19.13 ? 537  PRO   A N     1 
ATOM   3736  C  CA    . PRO   A  1 539  ? -30.986 57.216  102.773 1.00 19.36 ? 537  PRO   A CA    1 
ATOM   3737  C  C     . PRO   A  1 539  ? -30.482 57.396  104.196 1.00 16.39 ? 537  PRO   A C     1 
ATOM   3738  O  O     . PRO   A  1 539  ? -29.354 57.871  104.377 1.00 20.92 ? 537  PRO   A O     1 
ATOM   3739  C  CB    . PRO   A  1 539  ? -32.058 58.240  102.393 1.00 18.45 ? 537  PRO   A CB    1 
ATOM   3740  C  CG    . PRO   A  1 539  ? -32.865 57.514  101.313 1.00 16.80 ? 537  PRO   A CG    1 
ATOM   3741  C  CD    . PRO   A  1 539  ? -32.944 56.094  101.827 1.00 18.53 ? 537  PRO   A CD    1 
ATOM   3742  N  N     . ALA   A  1 540  ? -31.266 57.002  105.207 1.00 16.95 ? 538  ALA   A N     1 
ATOM   3743  C  CA    . ALA   A  1 540  ? -30.834 57.162  106.596 1.00 19.61 ? 538  ALA   A CA    1 
ATOM   3744  C  C     . ALA   A  1 540  ? -29.577 56.364  106.918 1.00 23.16 ? 538  ALA   A C     1 
ATOM   3745  O  O     . ALA   A  1 540  ? -28.871 56.699  107.878 1.00 24.94 ? 538  ALA   A O     1 
ATOM   3746  C  CB    . ALA   A  1 540  ? -31.945 56.746  107.568 1.00 25.80 ? 538  ALA   A CB    1 
ATOM   3747  N  N     . GLU   A  1 541  ? -29.284 55.317  106.149 1.00 20.81 ? 539  GLU   A N     1 
ATOM   3748  C  CA    . GLU   A  1 541  ? -28.186 54.408  106.457 1.00 23.99 ? 539  GLU   A CA    1 
ATOM   3749  C  C     . GLU   A  1 541  ? -27.030 54.570  105.479 1.00 24.83 ? 539  GLU   A C     1 
ATOM   3750  O  O     . GLU   A  1 541  ? -26.173 53.685  105.370 1.00 21.67 ? 539  GLU   A O     1 
ATOM   3751  C  CB    . GLU   A  1 541  ? -28.707 52.971  106.486 1.00 24.11 ? 539  GLU   A CB    1 
ATOM   3752  C  CG    . GLU   A  1 541  ? -29.901 52.829  107.433 1.00 31.19 ? 539  GLU   A CG    1 
ATOM   3753  C  CD    . GLU   A  1 541  ? -30.539 51.453  107.397 1.00 41.24 ? 539  GLU   A CD    1 
ATOM   3754  O  OE1   . GLU   A  1 541  ? -30.044 50.584  106.654 1.00 43.29 ? 539  GLU   A OE1   1 
ATOM   3755  O  OE2   . GLU   A  1 541  ? -31.536 51.240  108.115 1.00 44.43 ? 539  GLU   A OE2   1 
ATOM   3756  N  N     . LEU   A  1 542  ? -26.977 55.716  104.795 1.00 21.08 ? 540  LEU   A N     1 
ATOM   3757  C  CA    . LEU   A  1 542  ? -25.934 55.969  103.810 1.00 24.53 ? 540  LEU   A CA    1 
ATOM   3758  C  C     . LEU   A  1 542  ? -24.539 55.781  104.389 1.00 24.10 ? 540  LEU   A C     1 
ATOM   3759  O  O     . LEU   A  1 542  ? -23.624 55.367  103.676 1.00 25.17 ? 540  LEU   A O     1 
ATOM   3760  C  CB    . LEU   A  1 542  ? -26.069 57.394  103.264 1.00 21.77 ? 540  LEU   A CB    1 
ATOM   3761  C  CG    . LEU   A  1 542  ? -26.596 57.624  101.852 1.00 27.96 ? 540  LEU   A CG    1 
ATOM   3762  C  CD1   . LEU   A  1 542  ? -26.101 58.970  101.333 1.00 21.14 ? 540  LEU   A CD1   1 
ATOM   3763  C  CD2   . LEU   A  1 542  ? -26.231 56.494  100.907 1.00 22.67 ? 540  LEU   A CD2   1 
ATOM   3764  N  N     . PHE   A  1 543  ? -24.354 56.081  105.672 1.00 20.99 ? 541  PHE   A N     1 
ATOM   3765  C  CA    . PHE   A  1 543  ? -23.041 56.027  106.299 1.00 21.65 ? 541  PHE   A CA    1 
ATOM   3766  C  C     . PHE   A  1 543  ? -22.870 54.818  107.206 1.00 24.79 ? 541  PHE   A C     1 
ATOM   3767  O  O     . PHE   A  1 543  ? -21.866 54.729  107.924 1.00 26.68 ? 541  PHE   A O     1 
ATOM   3768  C  CB    . PHE   A  1 543  ? -22.796 57.326  107.061 1.00 20.31 ? 541  PHE   A CB    1 
ATOM   3769  C  CG    . PHE   A  1 543  ? -23.058 58.537  106.223 1.00 23.09 ? 541  PHE   A CG    1 
ATOM   3770  C  CD1   . PHE   A  1 543  ? -22.453 58.662  104.986 1.00 24.87 ? 541  PHE   A CD1   1 
ATOM   3771  C  CD2   . PHE   A  1 543  ? -23.957 59.506  106.628 1.00 21.03 ? 541  PHE   A CD2   1 
ATOM   3772  C  CE1   . PHE   A  1 543  ? -22.699 59.755  104.179 1.00 21.96 ? 541  PHE   A CE1   1 
ATOM   3773  C  CE2   . PHE   A  1 543  ? -24.216 60.600  105.834 1.00 20.23 ? 541  PHE   A CE2   1 
ATOM   3774  C  CZ    . PHE   A  1 543  ? -23.593 60.731  104.604 1.00 21.30 ? 541  PHE   A CZ    1 
ATOM   3775  N  N     . GLY   A  1 544  ? -23.819 53.885  107.178 1.00 23.31 ? 542  GLY   A N     1 
ATOM   3776  C  CA    . GLY   A  1 544  ? -23.696 52.658  107.946 1.00 25.47 ? 542  GLY   A CA    1 
ATOM   3777  C  C     . GLY   A  1 544  ? -23.552 52.922  109.433 1.00 25.64 ? 542  GLY   A C     1 
ATOM   3778  O  O     . GLY   A  1 544  ? -24.266 53.740  110.025 1.00 23.35 ? 542  GLY   A O     1 
ATOM   3779  N  N     . ASP   A  1 545  ? -22.605 52.220  110.048 1.00 27.43 ? 543  ASP   A N     1 
ATOM   3780  C  CA    . ASP   A  1 545  ? -22.409 52.303  111.487 1.00 30.58 ? 543  ASP   A CA    1 
ATOM   3781  C  C     . ASP   A  1 545  ? -21.701 53.574  111.926 1.00 27.90 ? 543  ASP   A C     1 
ATOM   3782  O  O     . ASP   A  1 545  ? -21.648 53.842  113.129 1.00 33.03 ? 543  ASP   A O     1 
ATOM   3783  C  CB    . ASP   A  1 545  ? -21.617 51.088  111.978 1.00 30.49 ? 543  ASP   A CB    1 
ATOM   3784  C  CG    . ASP   A  1 545  ? -22.341 49.784  111.716 1.00 43.85 ? 543  ASP   A CG    1 
ATOM   3785  O  OD1   . ASP   A  1 545  ? -23.595 49.794  111.672 1.00 43.31 ? 543  ASP   A OD1   1 
ATOM   3786  O  OD2   . ASP   A  1 545  ? -21.661 48.750  111.548 1.00 54.83 ? 543  ASP   A OD2   1 
ATOM   3787  N  N     . ALA   A  1 546  ? -21.147 54.350  110.997 1.00 27.74 ? 544  ALA   A N     1 
ATOM   3788  C  CA    . ALA   A  1 546  ? -20.425 55.554  111.388 1.00 27.82 ? 544  ALA   A CA    1 
ATOM   3789  C  C     . ALA   A  1 546  ? -21.360 56.546  112.063 1.00 29.88 ? 544  ALA   A C     1 
ATOM   3790  O  O     . ALA   A  1 546  ? -21.084 57.024  113.169 1.00 26.82 ? 544  ALA   A O     1 
ATOM   3791  C  CB    . ALA   A  1 546  ? -19.756 56.186  110.171 1.00 23.19 ? 544  ALA   A CB    1 
ATOM   3792  N  N     . ARG   A  1 547  ? -22.483 56.853  111.417 1.00 27.55 ? 545  ARG   A N     1 
ATOM   3793  C  CA    . ARG   A  1 547  ? -23.396 57.874  111.908 1.00 22.48 ? 545  ARG   A CA    1 
ATOM   3794  C  C     . ARG   A  1 547  ? -24.684 57.788  111.111 1.00 21.95 ? 545  ARG   A C     1 
ATOM   3795  O  O     . ARG   A  1 547  ? -24.721 57.244  110.005 1.00 22.04 ? 545  ARG   A O     1 
ATOM   3796  C  CB    . ARG   A  1 547  ? -22.802 59.277  111.784 1.00 25.76 ? 545  ARG   A CB    1 
ATOM   3797  C  CG    . ARG   A  1 547  ? -22.457 59.616  110.377 1.00 26.94 ? 545  ARG   A CG    1 
ATOM   3798  C  CD    . ARG   A  1 547  ? -21.616 60.871  110.287 1.00 27.86 ? 545  ARG   A CD    1 
ATOM   3799  N  NE    . ARG   A  1 547  ? -21.036 60.968  108.959 1.00 31.93 ? 545  ARG   A NE    1 
ATOM   3800  C  CZ    . ARG   A  1 547  ? -21.506 61.756  108.005 1.00 24.45 ? 545  ARG   A CZ    1 
ATOM   3801  N  NH1   . ARG   A  1 547  ? -22.536 62.554  108.219 1.00 23.78 ? 545  ARG   A NH1   1 
ATOM   3802  N  NH2   . ARG   A  1 547  ? -20.933 61.733  106.809 1.00 25.19 ? 545  ARG   A NH2   1 
ATOM   3803  N  N     . THR   A  1 548  ? -25.731 58.359  111.685 1.00 21.86 ? 546  THR   A N     1 
ATOM   3804  C  CA    . THR   A  1 548  ? -27.044 58.381  111.067 1.00 20.05 ? 546  THR   A CA    1 
ATOM   3805  C  C     . THR   A  1 548  ? -27.139 59.582  110.142 1.00 19.78 ? 546  THR   A C     1 
ATOM   3806  O  O     . THR   A  1 548  ? -26.871 60.713  110.560 1.00 17.92 ? 546  THR   A O     1 
ATOM   3807  C  CB    . THR   A  1 548  ? -28.119 58.449  112.149 1.00 22.78 ? 546  THR   A CB    1 
ATOM   3808  O  OG1   . THR   A  1 548  ? -28.027 57.284  112.972 1.00 24.12 ? 546  THR   A OG1   1 
ATOM   3809  C  CG2   . THR   A  1 548  ? -29.492 58.535  111.537 1.00 20.14 ? 546  THR   A CG2   1 
ATOM   3810  N  N     . ASN   A  1 549  ? -27.512 59.335  108.885 1.00 18.61 ? 547  ASN   A N     1 
ATOM   3811  C  CA    . ASN   A  1 549  ? -27.672 60.434  107.939 1.00 17.53 ? 547  ASN   A CA    1 
ATOM   3812  C  C     . ASN   A  1 549  ? -28.814 61.326  108.399 1.00 19.24 ? 547  ASN   A C     1 
ATOM   3813  O  O     . ASN   A  1 549  ? -29.794 60.846  108.969 1.00 20.88 ? 547  ASN   A O     1 
ATOM   3814  C  CB    . ASN   A  1 549  ? -27.941 59.883  106.533 1.00 19.50 ? 547  ASN   A CB    1 
ATOM   3815  C  CG    . ASN   A  1 549  ? -27.840 60.947  105.439 1.00 18.43 ? 547  ASN   A CG    1 
ATOM   3816  O  OD1   . ASN   A  1 549  ? -27.352 62.052  105.663 1.00 19.57 ? 547  ASN   A OD1   1 
ATOM   3817  N  ND2   . ASN   A  1 549  ? -28.275 60.593  104.236 1.00 18.03 ? 547  ASN   A ND2   1 
ATOM   3818  N  N     . SER   A  1 550  ? -28.676 62.631  108.194 1.00 17.53 ? 548  SER   A N     1 
ATOM   3819  C  CA    . SER   A  1 550  ? -29.809 63.519  108.448 1.00 16.24 ? 548  SER   A CA    1 
ATOM   3820  C  C     . SER   A  1 550  ? -30.932 63.208  107.472 1.00 18.88 ? 548  SER   A C     1 
ATOM   3821  O  O     . SER   A  1 550  ? -30.702 62.718  106.367 1.00 17.87 ? 548  SER   A O     1 
ATOM   3822  C  CB    . SER   A  1 550  ? -29.399 64.985  108.300 1.00 19.48 ? 548  SER   A CB    1 
ATOM   3823  O  OG    . SER   A  1 550  ? -28.859 65.221  107.005 1.00 18.65 ? 548  SER   A OG    1 
ATOM   3824  N  N     . ALA   A  1 551  ? -32.164 63.495  107.892 1.00 19.12 ? 549  ALA   A N     1 
ATOM   3825  C  CA    . ALA   A  1 551  ? -33.339 63.277  107.059 1.00 19.81 ? 549  ALA   A CA    1 
ATOM   3826  C  C     . ALA   A  1 551  ? -33.836 64.603  106.507 1.00 18.62 ? 549  ALA   A C     1 
ATOM   3827  O  O     . ALA   A  1 551  ? -33.841 65.615  107.206 1.00 19.47 ? 549  ALA   A O     1 
ATOM   3828  C  CB    . ALA   A  1 551  ? -34.461 62.599  107.848 1.00 20.21 ? 549  ALA   A CB    1 
ATOM   3829  N  N     . GLY   A  1 552  ? -34.235 64.590  105.243 1.00 19.95 ? 550  GLY   A N     1 
ATOM   3830  C  CA    . GLY   A  1 552  ? -34.839 65.733  104.613 1.00 17.72 ? 550  GLY   A CA    1 
ATOM   3831  C  C     . GLY   A  1 552  ? -36.348 65.653  104.645 1.00 18.45 ? 550  GLY   A C     1 
ATOM   3832  O  O     . GLY   A  1 552  ? -36.947 64.898  105.419 1.00 21.44 ? 550  GLY   A O     1 
ATOM   3833  N  N     . LEU   A  1 553  ? -36.966 66.441  103.781 1.00 18.64 ? 551  LEU   A N     1 
ATOM   3834  C  CA    . LEU   A  1 553  ? -38.409 66.502  103.638 1.00 19.44 ? 551  LEU   A CA    1 
ATOM   3835  C  C     . LEU   A  1 553  ? -38.714 66.466  102.156 1.00 19.29 ? 551  LEU   A C     1 
ATOM   3836  O  O     . LEU   A  1 553  ? -37.975 67.046  101.358 1.00 20.05 ? 551  LEU   A O     1 
ATOM   3837  C  CB    . LEU   A  1 553  ? -38.978 67.770  104.249 1.00 20.95 ? 551  LEU   A CB    1 
ATOM   3838  C  CG    . LEU   A  1 553  ? -38.903 67.896  105.762 1.00 21.67 ? 551  LEU   A CG    1 
ATOM   3839  C  CD1   . LEU   A  1 553  ? -39.420 69.274  106.188 1.00 23.26 ? 551  LEU   A CD1   1 
ATOM   3840  C  CD2   . LEU   A  1 553  ? -39.690 66.758  106.437 1.00 22.50 ? 551  LEU   A CD2   1 
ATOM   3841  N  N     . ASP   A  1 554  ? -39.787 65.787  101.784 1.00 17.32 ? 552  ASP   A N     1 
ATOM   3842  C  CA    . ASP   A  1 554  ? -40.115 65.627  100.371 1.00 20.37 ? 552  ASP   A CA    1 
ATOM   3843  C  C     . ASP   A  1 554  ? -41.072 66.742  99.992  1.00 18.36 ? 552  ASP   A C     1 
ATOM   3844  O  O     . ASP   A  1 554  ? -42.261 66.679  100.301 1.00 17.91 ? 552  ASP   A O     1 
ATOM   3845  C  CB    . ASP   A  1 554  ? -40.724 64.255  100.114 1.00 18.80 ? 552  ASP   A CB    1 
ATOM   3846  C  CG    . ASP   A  1 554  ? -41.023 64.019  98.641  1.00 19.79 ? 552  ASP   A CG    1 
ATOM   3847  O  OD1   . ASP   A  1 554  ? -40.760 64.928  97.818  1.00 20.45 ? 552  ASP   A OD1   1 
ATOM   3848  O  OD2   . ASP   A  1 554  ? -41.512 62.916  98.320  1.00 20.92 ? 552  ASP   A OD2   1 
ATOM   3849  N  N     . LEU   A  1 555  ? -40.561 67.766  99.303  1.00 20.16 ? 553  LEU   A N     1 
ATOM   3850  C  CA    . LEU   A  1 555  ? -41.407 68.890  98.933  1.00 18.81 ? 553  LEU   A CA    1 
ATOM   3851  C  C     . LEU   A  1 555  ? -42.306 68.586  97.740  1.00 18.99 ? 553  LEU   A C     1 
ATOM   3852  O  O     . LEU   A  1 555  ? -42.958 69.501  97.235  1.00 20.43 ? 553  LEU   A O     1 
ATOM   3853  C  CB    . LEU   A  1 555  ? -40.556 70.127  98.640  1.00 18.28 ? 553  LEU   A CB    1 
ATOM   3854  C  CG    . LEU   A  1 555  ? -39.706 70.587  99.830  1.00 19.52 ? 553  LEU   A CG    1 
ATOM   3855  C  CD1   . LEU   A  1 555  ? -38.947 71.864  99.501  1.00 25.03 ? 553  LEU   A CD1   1 
ATOM   3856  C  CD2   . LEU   A  1 555  ? -40.566 70.770  101.080 1.00 22.96 ? 553  LEU   A CD2   1 
ATOM   3857  N  N     . SER   A  1 556  ? -42.329 67.347  97.258  1.00 21.74 ? 554  SER   A N     1 
ATOM   3858  C  CA    . SER   A  1 556  ? -43.312 66.924  96.268  1.00 21.66 ? 554  SER   A CA    1 
ATOM   3859  C  C     . SER   A  1 556  ? -44.433 66.119  96.897  1.00 19.84 ? 554  SER   A C     1 
ATOM   3860  O  O     . SER   A  1 556  ? -45.354 65.705  96.194  1.00 19.81 ? 554  SER   A O     1 
ATOM   3861  C  CB    . SER   A  1 556  ? -42.646 66.098  95.160  1.00 20.87 ? 554  SER   A CB    1 
ATOM   3862  O  OG    . SER   A  1 556  ? -42.325 64.790  95.625  1.00 25.00 ? 554  SER   A OG    1 
ATOM   3863  N  N     . ASN   A  1 557  ? -44.373 65.895  98.204  1.00 19.12 ? 555  ASN   A N     1 
ATOM   3864  C  CA    . ASN   A  1 557  ? -45.372 65.116  98.914  1.00 17.29 ? 555  ASN   A CA    1 
ATOM   3865  C  C     . ASN   A  1 557  ? -46.421 66.067  99.483  1.00 19.52 ? 555  ASN   A C     1 
ATOM   3866  O  O     . ASN   A  1 557  ? -46.091 66.930  100.300 1.00 17.57 ? 555  ASN   A O     1 
ATOM   3867  C  CB    . ASN   A  1 557  ? -44.691 64.316  100.026 1.00 19.25 ? 555  ASN   A CB    1 
ATOM   3868  C  CG    . ASN   A  1 557  ? -45.645 63.420  100.772 1.00 18.02 ? 555  ASN   A CG    1 
ATOM   3869  O  OD1   . ASN   A  1 557  ? -46.663 63.875  101.282 1.00 19.38 ? 555  ASN   A OD1   1 
ATOM   3870  N  ND2   . ASN   A  1 557  ? -45.327 62.126  100.827 1.00 18.14 ? 555  ASN   A ND2   1 
ATOM   3871  N  N     . GLU   A  1 558  ? -47.689 65.896  99.073  1.00 21.18 ? 556  GLU   A N     1 
ATOM   3872  C  CA    . GLU   A  1 558  ? -48.728 66.834  99.501  1.00 20.60 ? 556  GLU   A CA    1 
ATOM   3873  C  C     . GLU   A  1 558  ? -48.958 66.776  101.003 1.00 20.96 ? 556  GLU   A C     1 
ATOM   3874  O  O     . GLU   A  1 558  ? -49.275 67.800  101.625 1.00 21.21 ? 556  GLU   A O     1 
ATOM   3875  C  CB    . GLU   A  1 558  ? -50.052 66.584  98.769  1.00 23.33 ? 556  GLU   A CB    1 
ATOM   3876  C  CG    . GLU   A  1 558  ? -50.042 66.869  97.276  1.00 25.75 ? 556  GLU   A CG    1 
ATOM   3877  C  CD    . GLU   A  1 558  ? -49.842 68.350  96.896  1.00 23.09 ? 556  GLU   A CD    1 
ATOM   3878  O  OE1   . GLU   A  1 558  ? -49.899 69.247  97.768  1.00 22.90 ? 556  GLU   A OE1   1 
ATOM   3879  O  OE2   . GLU   A  1 558  ? -49.627 68.610  95.688  1.00 19.70 ? 556  GLU   A OE2   1 
ATOM   3880  N  N     . GLU   A  1 559  ? -48.836 65.595  101.611 1.00 19.73 ? 557  GLU   A N     1 
ATOM   3881  C  CA    . GLU   A  1 559  ? -48.989 65.541  103.063 1.00 21.73 ? 557  GLU   A CA    1 
ATOM   3882  C  C     . GLU   A  1 559  ? -47.896 66.358  103.735 1.00 19.82 ? 557  GLU   A C     1 
ATOM   3883  O  O     . GLU   A  1 559  ? -48.163 67.156  104.637 1.00 19.54 ? 557  GLU   A O     1 
ATOM   3884  C  CB    . GLU   A  1 559  ? -48.968 64.096  103.562 1.00 22.27 ? 557  GLU   A CB    1 
ATOM   3885  C  CG    . GLU   A  1 559  ? -50.061 63.223  102.996 1.00 27.52 ? 557  GLU   A CG    1 
ATOM   3886  C  CD    . GLU   A  1 559  ? -51.445 63.617  103.494 1.00 40.91 ? 557  GLU   A CD    1 
ATOM   3887  O  OE1   . GLU   A  1 559  ? -51.535 64.271  104.563 1.00 42.61 ? 557  GLU   A OE1   1 
ATOM   3888  O  OE2   . GLU   A  1 559  ? -52.446 63.271  102.814 1.00 40.34 ? 557  GLU   A OE2   1 
ATOM   3889  N  N     . THR   A  1 560  ? -46.652 66.165  103.298 1.00 20.35 ? 558  THR   A N     1 
ATOM   3890  C  CA    . THR   A  1 560  ? -45.546 66.965  103.814 1.00 23.47 ? 558  THR   A CA    1 
ATOM   3891  C  C     . THR   A  1 560  ? -45.786 68.454  103.596 1.00 19.74 ? 558  THR   A C     1 
ATOM   3892  O  O     . THR   A  1 560  ? -45.610 69.260  104.513 1.00 20.57 ? 558  THR   A O     1 
ATOM   3893  C  CB    . THR   A  1 560  ? -44.240 66.531  103.146 1.00 19.62 ? 558  THR   A CB    1 
ATOM   3894  O  OG1   . THR   A  1 560  ? -44.026 65.140  103.401 1.00 20.63 ? 558  THR   A OG1   1 
ATOM   3895  C  CG2   . THR   A  1 560  ? -43.056 67.340  103.685 1.00 19.85 ? 558  THR   A CG2   1 
ATOM   3896  N  N     . LEU   A  1 561  ? -46.191 68.842  102.380 1.00 18.11 ? 559  LEU   A N     1 
ATOM   3897  C  CA    . LEU   A  1 561  ? -46.399 70.260  102.109 1.00 18.01 ? 559  LEU   A CA    1 
ATOM   3898  C  C     . LEU   A  1 561  ? -47.472 70.844  103.014 1.00 19.58 ? 559  LEU   A C     1 
ATOM   3899  O  O     . LEU   A  1 561  ? -47.331 71.969  103.508 1.00 20.03 ? 559  LEU   A O     1 
ATOM   3900  C  CB    . LEU   A  1 561  ? -46.763 70.477  100.640 1.00 18.34 ? 559  LEU   A CB    1 
ATOM   3901  C  CG    . LEU   A  1 561  ? -45.598 70.215  99.680  1.00 17.11 ? 559  LEU   A CG    1 
ATOM   3902  C  CD1   . LEU   A  1 561  ? -46.045 70.371  98.223  1.00 19.33 ? 559  LEU   A CD1   1 
ATOM   3903  C  CD2   . LEU   A  1 561  ? -44.401 71.138  99.993  1.00 18.57 ? 559  LEU   A CD2   1 
ATOM   3904  N  N     . ALA   A  1 562  ? -48.561 70.097  103.232 1.00 20.47 ? 560  ALA   A N     1 
ATOM   3905  C  CA    . ALA   A  1 562  ? -49.640 70.603  104.074 1.00 21.80 ? 560  ALA   A CA    1 
ATOM   3906  C  C     . ALA   A  1 562  ? -49.190 70.711  105.523 1.00 22.93 ? 560  ALA   A C     1 
ATOM   3907  O  O     . ALA   A  1 562  ? -49.446 71.722  106.188 1.00 23.74 ? 560  ALA   A O     1 
ATOM   3908  C  CB    . ALA   A  1 562  ? -50.871 69.699  103.962 1.00 24.40 ? 560  ALA   A CB    1 
ATOM   3909  N  N     . SER   A  1 563  ? -48.513 69.674  106.021 1.00 21.52 ? 561  SER   A N     1 
ATOM   3910  C  CA    . SER   A  1 563  ? -47.950 69.711  107.366 1.00 24.21 ? 561  SER   A CA    1 
ATOM   3911  C  C     . SER   A  1 563  ? -46.916 70.823  107.507 1.00 24.13 ? 561  SER   A C     1 
ATOM   3912  O  O     . SER   A  1 563  ? -46.886 71.543  108.512 1.00 24.16 ? 561  SER   A O     1 
ATOM   3913  C  CB    . SER   A  1 563  ? -47.318 68.351  107.678 1.00 29.35 ? 561  SER   A CB    1 
ATOM   3914  O  OG    . SER   A  1 563  ? -46.722 68.350  108.956 1.00 39.90 ? 561  SER   A OG    1 
ATOM   3915  N  N     . LEU   A  1 564  ? -46.042 70.965  106.516 1.00 23.20 ? 562  LEU   A N     1 
ATOM   3916  C  CA    . LEU   A  1 564  ? -45.003 71.975  106.604 1.00 22.20 ? 562  LEU   A CA    1 
ATOM   3917  C  C     . LEU   A  1 564  ? -45.598 73.378  106.547 1.00 21.66 ? 562  LEU   A C     1 
ATOM   3918  O  O     . LEU   A  1 564  ? -45.159 74.271  107.272 1.00 22.28 ? 562  LEU   A O     1 
ATOM   3919  C  CB    . LEU   A  1 564  ? -43.990 71.740  105.489 1.00 21.60 ? 562  LEU   A CB    1 
ATOM   3920  C  CG    . LEU   A  1 564  ? -42.724 72.559  105.426 1.00 24.13 ? 562  LEU   A CG    1 
ATOM   3921  C  CD1   . LEU   A  1 564  ? -41.943 72.397  106.706 1.00 23.55 ? 562  LEU   A CD1   1 
ATOM   3922  C  CD2   . LEU   A  1 564  ? -41.923 72.078  104.224 1.00 24.29 ? 562  LEU   A CD2   1 
ATOM   3923  N  N     . THR   A  1 565  ? -46.614 73.585  105.710 1.00 20.86 ? 563  THR   A N     1 
ATOM   3924  C  CA    . THR   A  1 565  ? -47.287 74.877  105.676 1.00 24.34 ? 563  THR   A CA    1 
ATOM   3925  C  C     . THR   A  1 565  ? -47.728 75.305  107.067 1.00 22.40 ? 563  THR   A C     1 
ATOM   3926  O  O     . THR   A  1 565  ? -47.503 76.445  107.479 1.00 21.82 ? 563  THR   A O     1 
ATOM   3927  C  CB    . THR   A  1 565  ? -48.487 74.821  104.733 1.00 20.34 ? 563  THR   A CB    1 
ATOM   3928  O  OG1   . THR   A  1 565  ? -48.021 74.658  103.388 1.00 21.68 ? 563  THR   A OG1   1 
ATOM   3929  C  CG2   . THR   A  1 565  ? -49.289 76.102  104.827 1.00 21.85 ? 563  THR   A CG2   1 
ATOM   3930  N  N     . GLU   A  1 566  ? -48.349 74.390  107.814 1.00 22.11 ? 564  GLU   A N     1 
ATOM   3931  C  CA    . GLU   A  1 566  ? -48.811 74.727  109.155 1.00 23.33 ? 564  GLU   A CA    1 
ATOM   3932  C  C     . GLU   A  1 566  ? -47.639 75.020  110.086 1.00 23.92 ? 564  GLU   A C     1 
ATOM   3933  O  O     . GLU   A  1 566  ? -47.667 75.996  110.846 1.00 23.55 ? 564  GLU   A O     1 
ATOM   3934  C  CB    . GLU   A  1 566  ? -49.671 73.592  109.705 1.00 24.63 ? 564  GLU   A CB    1 
ATOM   3935  N  N     . ALA   A  1 567  ? -46.598 74.189  110.042 1.00 22.50 ? 565  ALA   A N     1 
ATOM   3936  C  CA    . ALA   A  1 567  ? -45.439 74.414  110.904 1.00 25.47 ? 565  ALA   A CA    1 
ATOM   3937  C  C     . ALA   A  1 567  ? -44.741 75.723  110.560 1.00 22.59 ? 565  ALA   A C     1 
ATOM   3938  O  O     . ALA   A  1 567  ? -44.271 76.442  111.456 1.00 22.27 ? 565  ALA   A O     1 
ATOM   3939  C  CB    . ALA   A  1 567  ? -44.466 73.243  110.782 1.00 23.32 ? 565  ALA   A CB    1 
ATOM   3940  N  N     . LEU   A  1 568  ? -44.653 76.045  109.266 1.00 18.40 ? 566  LEU   A N     1 
ATOM   3941  C  CA    . LEU   A  1 568  ? -44.000 77.284  108.856 1.00 20.93 ? 566  LEU   A CA    1 
ATOM   3942  C  C     . LEU   A  1 568  ? -44.797 78.490  109.331 1.00 21.34 ? 566  LEU   A C     1 
ATOM   3943  O  O     . LEU   A  1 568  ? -44.236 79.444  109.885 1.00 20.76 ? 566  LEU   A O     1 
ATOM   3944  C  CB    . LEU   A  1 568  ? -43.825 77.311  107.333 1.00 18.66 ? 566  LEU   A CB    1 
ATOM   3945  C  CG    . LEU   A  1 568  ? -42.864 76.269  106.747 1.00 21.36 ? 566  LEU   A CG    1 
ATOM   3946  C  CD1   . LEU   A  1 568  ? -42.856 76.302  105.210 1.00 20.60 ? 566  LEU   A CD1   1 
ATOM   3947  C  CD2   . LEU   A  1 568  ? -41.459 76.482  107.297 1.00 18.29 ? 566  LEU   A CD2   1 
ATOM   3948  N  N     . ARG   A  1 569  ? -46.114 78.460  109.123 1.00 22.66 ? 567  ARG   A N     1 
ATOM   3949  C  CA    . ARG   A  1 569  ? -46.971 79.529  109.629 1.00 19.77 ? 567  ARG   A CA    1 
ATOM   3950  C  C     . ARG   A  1 569  ? -46.824 79.690  111.134 1.00 23.94 ? 567  ARG   A C     1 
ATOM   3951  O  O     . ARG   A  1 569  ? -46.713 80.814  111.637 1.00 25.14 ? 567  ARG   A O     1 
ATOM   3952  C  CB    . ARG   A  1 569  ? -48.431 79.249  109.268 1.00 20.96 ? 567  ARG   A CB    1 
ATOM   3953  C  CG    . ARG   A  1 569  ? -48.745 79.447  107.795 1.00 23.05 ? 567  ARG   A CG    1 
ATOM   3954  C  CD    . ARG   A  1 569  ? -50.207 79.116  107.503 1.00 25.10 ? 567  ARG   A CD    1 
ATOM   3955  N  NE    . ARG   A  1 569  ? -50.519 79.116  106.077 1.00 31.23 ? 567  ARG   A NE    1 
ATOM   3956  C  CZ    . ARG   A  1 569  ? -51.666 78.678  105.569 1.00 41.22 ? 567  ARG   A CZ    1 
ATOM   3957  N  NH1   . ARG   A  1 569  ? -52.608 78.153  106.339 1.00 37.44 ? 567  ARG   A NH1   1 
ATOM   3958  N  NH2   . ARG   A  1 569  ? -51.872 78.761  104.256 1.00 41.65 ? 567  ARG   A NH2   1 
ATOM   3959  N  N     . GLU   A  1 570  ? -46.795 78.578  111.869 1.00 22.44 ? 568  GLU   A N     1 
ATOM   3960  C  CA    . GLU   A  1 570  ? -46.634 78.664  113.315 1.00 24.53 ? 568  GLU   A CA    1 
ATOM   3961  C  C     . GLU   A  1 570  ? -45.288 79.279  113.682 1.00 27.34 ? 568  GLU   A C     1 
ATOM   3962  O  O     . GLU   A  1 570  ? -45.200 80.091  114.616 1.00 24.80 ? 568  GLU   A O     1 
ATOM   3963  C  CB    . GLU   A  1 570  ? -46.807 77.274  113.938 1.00 30.13 ? 568  GLU   A CB    1 
ATOM   3964  C  CG    . GLU   A  1 570  ? -48.267 76.803  113.891 1.00 36.02 ? 568  GLU   A CG    1 
ATOM   3965  C  CD    . GLU   A  1 570  ? -48.458 75.316  114.187 1.00 43.61 ? 568  GLU   A CD    1 
ATOM   3966  O  OE1   . GLU   A  1 570  ? -47.451 74.585  114.306 1.00 45.92 ? 568  GLU   A OE1   1 
ATOM   3967  O  OE2   . GLU   A  1 570  ? -49.628 74.876  114.288 1.00 45.32 ? 568  GLU   A OE2   1 
ATOM   3968  N  N     . SER   A  1 571  ? -44.234 78.932  112.935 1.00 23.73 ? 569  SER   A N     1 
ATOM   3969  C  CA    . SER   A  1 571  ? -42.918 79.500  113.210 1.00 25.22 ? 569  SER   A CA    1 
ATOM   3970  C  C     . SER   A  1 571  ? -42.921 81.011  113.042 1.00 24.58 ? 569  SER   A C     1 
ATOM   3971  O  O     . SER   A  1 571  ? -42.175 81.709  113.735 1.00 22.58 ? 569  SER   A O     1 
ATOM   3972  C  CB    . SER   A  1 571  ? -41.860 78.885  112.292 1.00 23.66 ? 569  SER   A CB    1 
ATOM   3973  O  OG    . SER   A  1 571  ? -41.895 79.500  111.013 1.00 23.53 ? 569  SER   A OG    1 
ATOM   3974  N  N     . ALA   A  1 572  ? -43.749 81.533  112.134 1.00 23.69 ? 570  ALA   A N     1 
ATOM   3975  C  CA    . ALA   A  1 572  ? -43.801 82.971  111.899 1.00 24.89 ? 570  ALA   A CA    1 
ATOM   3976  C  C     . ALA   A  1 572  ? -44.597 83.711  112.963 1.00 30.49 ? 570  ALA   A C     1 
ATOM   3977  O  O     . ALA   A  1 572  ? -44.474 84.936  113.068 1.00 31.58 ? 570  ALA   A O     1 
ATOM   3978  C  CB    . ALA   A  1 572  ? -44.389 83.262  110.519 1.00 26.17 ? 570  ALA   A CB    1 
ATOM   3979  N  N     . ALA   A  1 573  ? -45.409 83.001  113.743 1.00 27.38 ? 571  ALA   A N     1 
ATOM   3980  C  CA    . ALA   A  1 573  ? -46.101 83.584  114.883 1.00 27.82 ? 571  ALA   A CA    1 
ATOM   3981  C  C     . ALA   A  1 573  ? -45.258 83.573  116.153 1.00 35.63 ? 571  ALA   A C     1 
ATOM   3982  O  O     . ALA   A  1 573  ? -45.715 84.072  117.185 1.00 37.16 ? 571  ALA   A O     1 
ATOM   3983  C  CB    . ALA   A  1 573  ? -47.418 82.845  115.143 1.00 28.74 ? 571  ALA   A CB    1 
ATOM   3984  N  N     . MET   A  1 574  ? -44.052 83.019  116.112 1.00 29.89 ? 572  MET   A N     1 
ATOM   3985  C  CA    . MET   A  1 574  ? -43.220 82.918  117.304 1.00 33.00 ? 572  MET   A CA    1 
ATOM   3986  C  C     . MET   A  1 574  ? -42.453 84.214  117.526 1.00 27.27 ? 572  MET   A C     1 
ATOM   3987  O  O     . MET   A  1 574  ? -42.049 84.883  116.572 1.00 30.76 ? 572  MET   A O     1 
ATOM   3988  C  CB    . MET   A  1 574  ? -42.255 81.739  117.191 1.00 30.75 ? 572  MET   A CB    1 
ATOM   3989  C  CG    . MET   A  1 574  ? -42.954 80.397  117.322 1.00 32.20 ? 572  MET   A CG    1 
ATOM   3990  S  SD    . MET   A  1 574  ? -41.888 79.023  116.938 1.00 34.24 ? 572  MET   A SD    1 
ATOM   3991  C  CE    . MET   A  1 574  ? -43.026 77.648  117.081 1.00 38.21 ? 572  MET   A CE    1 
ATOM   3992  N  N     . LYS   A  1 575  ? -42.271 84.568  118.799 1.00 31.95 ? 573  LYS   A N     1 
ATOM   3993  C  CA    . LYS   A  1 575  ? -41.539 85.779  119.174 1.00 26.70 ? 573  LYS   A CA    1 
ATOM   3994  C  C     . LYS   A  1 575  ? -40.065 85.421  119.374 1.00 28.42 ? 573  LYS   A C     1 
ATOM   3995  O  O     . LYS   A  1 575  ? -39.533 85.350  120.488 1.00 29.69 ? 573  LYS   A O     1 
ATOM   3996  C  CB    . LYS   A  1 575  ? -42.155 86.410  120.418 1.00 36.07 ? 573  LYS   A CB    1 
ATOM   3997  N  N     . TRP   A  1 576  ? -39.409 85.184  118.243 1.00 26.01 ? 574  TRP   A N     1 
ATOM   3998  C  CA    . TRP   A  1 576  ? -37.991 84.837  118.242 1.00 26.09 ? 574  TRP   A CA    1 
ATOM   3999  C  C     . TRP   A  1 576  ? -37.156 85.961  118.843 1.00 22.71 ? 574  TRP   A C     1 
ATOM   4000  O  O     . TRP   A  1 576  ? -37.375 87.143  118.556 1.00 24.56 ? 574  TRP   A O     1 
ATOM   4001  C  CB    . TRP   A  1 576  ? -37.530 84.565  116.812 1.00 23.69 ? 574  TRP   A CB    1 
ATOM   4002  C  CG    . TRP   A  1 576  ? -38.209 83.408  116.146 1.00 22.86 ? 574  TRP   A CG    1 
ATOM   4003  C  CD1   . TRP   A  1 576  ? -39.179 83.467  115.185 1.00 23.95 ? 574  TRP   A CD1   1 
ATOM   4004  C  CD2   . TRP   A  1 576  ? -37.951 82.020  116.373 1.00 20.37 ? 574  TRP   A CD2   1 
ATOM   4005  N  NE1   . TRP   A  1 576  ? -39.542 82.196  114.799 1.00 23.87 ? 574  TRP   A NE1   1 
ATOM   4006  C  CE2   . TRP   A  1 576  ? -38.808 81.288  115.515 1.00 22.42 ? 574  TRP   A CE2   1 
ATOM   4007  C  CE3   . TRP   A  1 576  ? -37.084 81.321  117.224 1.00 23.52 ? 574  TRP   A CE3   1 
ATOM   4008  C  CZ2   . TRP   A  1 576  ? -38.819 79.893  115.476 1.00 21.70 ? 574  TRP   A CZ2   1 
ATOM   4009  C  CZ3   . TRP   A  1 576  ? -37.091 79.932  117.186 1.00 23.81 ? 574  TRP   A CZ3   1 
ATOM   4010  C  CH2   . TRP   A  1 576  ? -37.963 79.233  116.323 1.00 22.35 ? 574  TRP   A CH2   1 
ATOM   4011  N  N     . THR   A  1 577  ? -36.209 85.594  119.699 1.00 23.10 ? 575  THR   A N     1 
ATOM   4012  C  CA    . THR   A  1 577  ? -35.282 86.560  120.268 1.00 24.22 ? 575  THR   A CA    1 
ATOM   4013  C  C     . THR   A  1 577  ? -33.881 85.974  120.266 1.00 24.41 ? 575  THR   A C     1 
ATOM   4014  O  O     . THR   A  1 577  ? -33.683 84.759  120.213 1.00 22.43 ? 575  THR   A O     1 
ATOM   4015  C  CB    . THR   A  1 577  ? -35.641 86.969  121.708 1.00 28.57 ? 575  THR   A CB    1 
ATOM   4016  O  OG1   . THR   A  1 577  ? -35.573 85.822  122.562 1.00 24.52 ? 575  THR   A OG1   1 
ATOM   4017  C  CG2   . THR   A  1 577  ? -37.036 87.583  121.785 1.00 31.24 ? 575  THR   A CG2   1 
ATOM   4018  N  N     . ALA   A  1 578  ? -32.902 86.867  120.326 1.00 23.16 ? 576  ALA   A N     1 
ATOM   4019  C  CA    . ALA   A  1 578  ? -31.516 86.496  120.553 1.00 20.76 ? 576  ALA   A CA    1 
ATOM   4020  C  C     . ALA   A  1 578  ? -30.975 87.457  121.592 1.00 22.84 ? 576  ALA   A C     1 
ATOM   4021  O  O     . ALA   A  1 578  ? -31.174 88.668  121.480 1.00 23.95 ? 576  ALA   A O     1 
ATOM   4022  C  CB    . ALA   A  1 578  ? -30.689 86.571  119.269 1.00 20.36 ? 576  ALA   A CB    1 
ATOM   4023  N  N     . LEU   A  1 579  ? -30.323 86.921  122.606 1.00 25.45 ? 577  LEU   A N     1 
ATOM   4024  C  CA    . LEU   A  1 579  ? -29.812 87.702  123.718 1.00 27.74 ? 577  LEU   A CA    1 
ATOM   4025  C  C     . LEU   A  1 579  ? -28.359 87.337  123.943 1.00 22.87 ? 577  LEU   A C     1 
ATOM   4026  O  O     . LEU   A  1 579  ? -27.924 86.236  123.580 1.00 22.99 ? 577  LEU   A O     1 
ATOM   4027  C  CB    . LEU   A  1 579  ? -30.603 87.431  125.007 1.00 26.80 ? 577  LEU   A CB    1 
ATOM   4028  C  CG    . LEU   A  1 579  ? -32.121 87.508  124.915 1.00 30.78 ? 577  LEU   A CG    1 
ATOM   4029  C  CD1   . LEU   A  1 579  ? -32.720 87.199  126.274 1.00 35.23 ? 577  LEU   A CD1   1 
ATOM   4030  C  CD2   . LEU   A  1 579  ? -32.534 88.881  124.439 1.00 31.74 ? 577  LEU   A CD2   1 
ATOM   4031  N  N     . PRO   A  1 580  ? -27.576 88.244  124.542 1.00 23.88 ? 578  PRO   A N     1 
ATOM   4032  C  CA    . PRO   A  1 580  ? -26.262 87.845  125.043 1.00 23.97 ? 578  PRO   A CA    1 
ATOM   4033  C  C     . PRO   A  1 580  ? -26.477 86.829  126.137 1.00 28.24 ? 578  PRO   A C     1 
ATOM   4034  O  O     . PRO   A  1 580  ? -27.009 87.161  127.199 1.00 28.53 ? 578  PRO   A O     1 
ATOM   4035  C  CB    . PRO   A  1 580  ? -25.664 89.149  125.577 1.00 25.40 ? 578  PRO   A CB    1 
ATOM   4036  C  CG    . PRO   A  1 580  ? -26.539 90.245  125.016 1.00 23.51 ? 578  PRO   A CG    1 
ATOM   4037  C  CD    . PRO   A  1 580  ? -27.890 89.638  124.886 1.00 25.41 ? 578  PRO   A CD    1 
ATOM   4038  N  N     . GLN   A  1 581  ? -26.138 85.582  125.866 1.00 23.40 ? 579  GLN   A N     1 
ATOM   4039  C  CA    . GLN   A  1 581  ? -26.351 84.497  126.816 1.00 24.15 ? 579  GLN   A CA    1 
ATOM   4040  C  C     . GLN   A  1 581  ? -24.993 84.183  127.421 1.00 26.57 ? 579  GLN   A C     1 
ATOM   4041  O  O     . GLN   A  1 581  ? -24.236 83.363  126.904 1.00 23.52 ? 579  GLN   A O     1 
ATOM   4042  C  CB    . GLN   A  1 581  ? -26.968 83.281  126.136 1.00 21.51 ? 579  GLN   A CB    1 
ATOM   4043  C  CG    . GLN   A  1 581  ? -28.361 83.532  125.578 1.00 24.83 ? 579  GLN   A CG    1 
ATOM   4044  C  CD    . GLN   A  1 581  ? -29.409 83.698  126.670 1.00 28.77 ? 579  GLN   A CD    1 
ATOM   4045  O  OE1   . GLN   A  1 581  ? -29.118 83.560  127.857 1.00 28.76 ? 579  GLN   A OE1   1 
ATOM   4046  N  NE2   . GLN   A  1 581  ? -30.638 83.992  126.267 1.00 28.73 ? 579  GLN   A NE2   1 
ATOM   4047  N  N     . LEU   A  1 582  ? -24.687 84.850  128.529 1.00 24.48 ? 580  LEU   A N     1 
ATOM   4048  C  CA    . LEU   A  1 582  ? -23.435 84.608  129.215 1.00 27.50 ? 580  LEU   A CA    1 
ATOM   4049  C  C     . LEU   A  1 582  ? -23.578 83.415  130.158 1.00 28.35 ? 580  LEU   A C     1 
ATOM   4050  O  O     . LEU   A  1 582  ? -24.681 82.923  130.417 1.00 28.38 ? 580  LEU   A O     1 
ATOM   4051  C  CB    . LEU   A  1 582  ? -22.999 85.863  129.969 1.00 27.74 ? 580  LEU   A CB    1 
ATOM   4052  C  CG    . LEU   A  1 582  ? -22.133 86.839  129.161 1.00 32.34 ? 580  LEU   A CG    1 
ATOM   4053  C  CD1   . LEU   A  1 582  ? -22.857 87.358  127.939 1.00 31.89 ? 580  LEU   A CD1   1 
ATOM   4054  C  CD2   . LEU   A  1 582  ? -21.676 88.001  130.044 1.00 35.89 ? 580  LEU   A CD2   1 
ATOM   4055  N  N     . ALA   A  1 583  ? -22.437 82.936  130.666 1.00 25.13 ? 581  ALA   A N     1 
ATOM   4056  C  CA    . ALA   A  1 583  ? -22.470 81.830  131.619 1.00 26.12 ? 581  ALA   A CA    1 
ATOM   4057  C  C     . ALA   A  1 583  ? -23.332 82.169  132.825 1.00 31.28 ? 581  ALA   A C     1 
ATOM   4058  O  O     . ALA   A  1 583  ? -23.969 81.283  133.407 1.00 33.85 ? 581  ALA   A O     1 
ATOM   4059  C  CB    . ALA   A  1 583  ? -21.057 81.481  132.078 1.00 27.91 ? 581  ALA   A CB    1 
ATOM   4060  N  N     . THR   A  1 584  ? -23.376 83.444  133.195 1.00 29.30 ? 582  THR   A N     1 
ATOM   4061  C  CA    . THR   A  1 584  ? -24.069 83.928  134.379 1.00 32.69 ? 582  THR   A CA    1 
ATOM   4062  C  C     . THR   A  1 584  ? -25.538 84.247  134.120 1.00 37.28 ? 582  THR   A C     1 
ATOM   4063  O  O     . THR   A  1 584  ? -26.238 84.673  135.047 1.00 37.65 ? 582  THR   A O     1 
ATOM   4064  C  CB    . THR   A  1 584  ? -23.345 85.169  134.906 1.00 33.61 ? 582  THR   A CB    1 
ATOM   4065  O  OG1   . THR   A  1 584  ? -23.214 86.123  133.848 1.00 36.23 ? 582  THR   A OG1   1 
ATOM   4066  C  CG2   . THR   A  1 584  ? -21.953 84.803  135.385 1.00 34.28 ? 582  THR   A CG2   1 
ATOM   4067  N  N     . GLY   A  1 585  ? -26.018 84.041  132.893 1.00 29.24 ? 583  GLY   A N     1 
ATOM   4068  C  CA    . GLY   A  1 585  ? -27.380 84.349  132.522 1.00 32.19 ? 583  GLY   A CA    1 
ATOM   4069  C  C     . GLY   A  1 585  ? -27.462 85.350  131.385 1.00 28.66 ? 583  GLY   A C     1 
ATOM   4070  O  O     . GLY   A  1 585  ? -26.446 85.867  130.911 1.00 30.23 ? 583  GLY   A O     1 
ATOM   4071  N  N     . PRO   A  1 586  ? -28.678 85.645  130.924 1.00 34.56 ? 584  PRO   A N     1 
ATOM   4072  C  CA    . PRO   A  1 586  ? -28.829 86.625  129.840 1.00 30.62 ? 584  PRO   A CA    1 
ATOM   4073  C  C     . PRO   A  1 586  ? -28.381 88.003  130.296 1.00 33.82 ? 584  PRO   A C     1 
ATOM   4074  O  O     . PRO   A  1 586  ? -28.571 88.388  131.450 1.00 33.55 ? 584  PRO   A O     1 
ATOM   4075  C  CB    . PRO   A  1 586  ? -30.331 86.594  129.531 1.00 34.56 ? 584  PRO   A CB    1 
ATOM   4076  C  CG    . PRO   A  1 586  ? -30.967 86.094  130.795 1.00 35.57 ? 584  PRO   A CG    1 
ATOM   4077  C  CD    . PRO   A  1 586  ? -29.976 85.123  131.386 1.00 32.52 ? 584  PRO   A CD    1 
ATOM   4078  N  N     . ALA   A  1 587  ? -27.775 88.747  129.382 1.00 31.00 ? 585  ALA   A N     1 
ATOM   4079  C  CA    . ALA   A  1 587  ? -27.276 90.076  129.690 1.00 31.10 ? 585  ALA   A CA    1 
ATOM   4080  C  C     . ALA   A  1 587  ? -28.182 91.129  129.072 1.00 34.38 ? 585  ALA   A C     1 
ATOM   4081  O  O     . ALA   A  1 587  ? -28.875 90.878  128.080 1.00 30.80 ? 585  ALA   A O     1 
ATOM   4082  C  CB    . ALA   A  1 587  ? -25.841 90.265  129.185 1.00 34.82 ? 585  ALA   A CB    1 
ATOM   4083  N  N     . ALA   A  1 588  ? -28.193 92.306  129.691 1.00 34.66 ? 586  ALA   A N     1 
ATOM   4084  C  CA    . ALA   A  1 588  ? -28.879 93.444  129.107 1.00 37.60 ? 586  ALA   A CA    1 
ATOM   4085  C  C     . ALA   A  1 588  ? -28.051 94.015  127.958 1.00 32.66 ? 586  ALA   A C     1 
ATOM   4086  O  O     . ALA   A  1 588  ? -26.825 93.866  127.905 1.00 36.57 ? 586  ALA   A O     1 
ATOM   4087  C  CB    . ALA   A  1 588  ? -29.130 94.519  130.168 1.00 38.46 ? 586  ALA   A CB    1 
ATOM   4088  N  N     . GLY   A  1 589  ? -28.730 94.674  127.031 1.00 33.30 ? 587  GLY   A N     1 
ATOM   4089  C  CA    . GLY   A  1 589  ? -28.019 95.285  125.923 1.00 34.37 ? 587  GLY   A CA    1 
ATOM   4090  C  C     . GLY   A  1 589  ? -28.970 96.077  125.060 1.00 35.06 ? 587  GLY   A C     1 
ATOM   4091  O  O     . GLY   A  1 589  ? -30.160 96.220  125.367 1.00 35.46 ? 587  GLY   A O     1 
ATOM   4092  N  N     . GLU   A  1 590  ? -28.422 96.598  123.965 1.00 31.42 ? 588  GLU   A N     1 
ATOM   4093  C  CA    . GLU   A  1 590  ? -29.219 97.365  123.018 1.00 34.35 ? 588  GLU   A CA    1 
ATOM   4094  C  C     . GLU   A  1 590  ? -29.995 96.407  122.124 1.00 34.17 ? 588  GLU   A C     1 
ATOM   4095  O  O     . GLU   A  1 590  ? -29.412 95.488  121.534 1.00 31.23 ? 588  GLU   A O     1 
ATOM   4096  C  CB    . GLU   A  1 590  ? -28.323 98.281  122.182 1.00 38.33 ? 588  GLU   A CB    1 
ATOM   4097  N  N     . THR   A  1 591  ? -31.305 96.619  122.028 1.00 32.46 ? 589  THR   A N     1 
ATOM   4098  C  CA    . THR   A  1 591  ? -32.211 95.705  121.343 1.00 31.32 ? 589  THR   A CA    1 
ATOM   4099  C  C     . THR   A  1 591  ? -32.694 96.335  120.042 1.00 30.42 ? 589  THR   A C     1 
ATOM   4100  O  O     . THR   A  1 591  ? -33.079 97.508  120.019 1.00 33.79 ? 589  THR   A O     1 
ATOM   4101  C  CB    . THR   A  1 591  ? -33.399 95.345  122.247 1.00 33.04 ? 589  THR   A CB    1 
ATOM   4102  O  OG1   . THR   A  1 591  ? -32.915 94.726  123.451 1.00 33.16 ? 589  THR   A OG1   1 
ATOM   4103  C  CG2   . THR   A  1 591  ? -34.342 94.384  121.549 1.00 32.79 ? 589  THR   A CG2   1 
ATOM   4104  N  N     . ARG   A  1 592  ? -32.652 95.561  118.960 1.00 30.60 ? 590  ARG   A N     1 
ATOM   4105  C  CA    . ARG   A  1 592  ? -33.170 96.006  117.676 1.00 32.96 ? 590  ARG   A CA    1 
ATOM   4106  C  C     . ARG   A  1 592  ? -33.946 94.864  117.044 1.00 29.88 ? 590  ARG   A C     1 
ATOM   4107  O  O     . ARG   A  1 592  ? -33.795 93.702  117.422 1.00 26.56 ? 590  ARG   A O     1 
ATOM   4108  C  CB    . ARG   A  1 592  ? -32.054 96.486  116.731 1.00 38.94 ? 590  ARG   A CB    1 
ATOM   4109  C  CG    . ARG   A  1 592  ? -30.845 95.586  116.659 1.00 41.93 ? 590  ARG   A CG    1 
ATOM   4110  C  CD    . ARG   A  1 592  ? -29.941 95.947  115.478 1.00 47.40 ? 590  ARG   A CD    1 
ATOM   4111  N  NE    . ARG   A  1 592  ? -30.484 95.453  114.217 1.00 50.83 ? 590  ARG   A NE    1 
ATOM   4112  C  CZ    . ARG   A  1 592  ? -30.055 94.370  113.579 1.00 50.66 ? 590  ARG   A CZ    1 
ATOM   4113  N  NH1   . ARG   A  1 592  ? -29.035 93.656  114.033 1.00 45.11 ? 590  ARG   A NH1   1 
ATOM   4114  N  NH2   . ARG   A  1 592  ? -30.658 94.000  112.450 1.00 45.55 ? 590  ARG   A NH2   1 
ATOM   4115  N  N     . THR   A  1 593  ? -34.772 95.204  116.064 1.00 28.39 ? 591  THR   A N     1 
ATOM   4116  C  CA    . THR   A  1 593  ? -35.588 94.202  115.404 1.00 27.21 ? 591  THR   A CA    1 
ATOM   4117  C  C     . THR   A  1 593  ? -34.811 93.545  114.265 1.00 30.19 ? 591  THR   A C     1 
ATOM   4118  O  O     . THR   A  1 593  ? -33.925 94.149  113.654 1.00 32.15 ? 591  THR   A O     1 
ATOM   4119  C  CB    . THR   A  1 593  ? -36.882 94.828  114.887 1.00 32.43 ? 591  THR   A CB    1 
ATOM   4120  O  OG1   . THR   A  1 593  ? -36.564 95.865  113.956 1.00 34.90 ? 591  THR   A OG1   1 
ATOM   4121  C  CG2   . THR   A  1 593  ? -37.651 95.437  116.047 1.00 32.99 ? 591  THR   A CG2   1 
ATOM   4122  N  N     . VAL   A  1 594  ? -35.128 92.281  114.016 1.00 23.30 ? 592  VAL   A N     1 
ATOM   4123  C  CA    . VAL   A  1 594  ? -34.556 91.513  112.914 1.00 24.08 ? 592  VAL   A CA    1 
ATOM   4124  C  C     . VAL   A  1 594  ? -35.618 91.422  111.824 1.00 24.59 ? 592  VAL   A C     1 
ATOM   4125  O  O     . VAL   A  1 594  ? -36.761 91.029  112.092 1.00 23.83 ? 592  VAL   A O     1 
ATOM   4126  C  CB    . VAL   A  1 594  ? -34.109 90.116  113.386 1.00 23.05 ? 592  VAL   A CB    1 
ATOM   4127  C  CG1   . VAL   A  1 594  ? -33.527 89.306  112.246 1.00 22.20 ? 592  VAL   A CG1   1 
ATOM   4128  C  CG2   . VAL   A  1 594  ? -33.088 90.241  114.514 1.00 24.96 ? 592  VAL   A CG2   1 
ATOM   4129  N  N     . LEU   A  1 595  ? -35.257 91.805  110.605 1.00 23.03 ? 593  LEU   A N     1 
ATOM   4130  C  CA    . LEU   A  1 595  ? -36.209 91.932  109.509 1.00 22.43 ? 593  LEU   A CA    1 
ATOM   4131  C  C     . LEU   A  1 595  ? -35.960 90.863  108.452 1.00 24.02 ? 593  LEU   A C     1 
ATOM   4132  O  O     . LEU   A  1 595  ? -34.827 90.423  108.246 1.00 21.76 ? 593  LEU   A O     1 
ATOM   4133  C  CB    . LEU   A  1 595  ? -36.113 93.316  108.856 1.00 24.98 ? 593  LEU   A CB    1 
ATOM   4134  C  CG    . LEU   A  1 595  ? -36.303 94.538  109.761 1.00 26.08 ? 593  LEU   A CG    1 
ATOM   4135  C  CD1   . LEU   A  1 595  ? -36.247 95.836  108.950 1.00 28.45 ? 593  LEU   A CD1   1 
ATOM   4136  C  CD2   . LEU   A  1 595  ? -37.608 94.429  110.506 1.00 25.19 ? 593  LEU   A CD2   1 
ATOM   4137  N  N     . ASN   A  1 596  ? -37.036 90.452  107.791 1.00 21.91 ? 594  ASN   A N     1 
ATOM   4138  C  CA    . ASN   A  1 596  ? -36.952 89.536  106.656 1.00 22.28 ? 594  ASN   A CA    1 
ATOM   4139  C  C     . ASN   A  1 596  ? -36.260 90.263  105.510 1.00 19.66 ? 594  ASN   A C     1 
ATOM   4140  O  O     . ASN   A  1 596  ? -36.751 91.314  105.077 1.00 20.84 ? 594  ASN   A O     1 
ATOM   4141  C  CB    . ASN   A  1 596  ? -38.369 89.098  106.273 1.00 19.97 ? 594  ASN   A CB    1 
ATOM   4142  C  CG    . ASN   A  1 596  ? -38.415 88.041  105.175 1.00 21.71 ? 594  ASN   A CG    1 
ATOM   4143  O  OD1   . ASN   A  1 596  ? -37.544 87.964  104.309 1.00 21.25 ? 594  ASN   A OD1   1 
ATOM   4144  N  ND2   . ASN   A  1 596  ? -39.460 87.223  105.210 1.00 21.72 ? 594  ASN   A ND2   1 
ATOM   4145  N  N     . PRO   A  1 597  ? -35.118 89.782  105.014 1.00 20.40 ? 595  PRO   A N     1 
ATOM   4146  C  CA    . PRO   A  1 597  ? -34.486 90.471  103.877 1.00 20.84 ? 595  PRO   A CA    1 
ATOM   4147  C  C     . PRO   A  1 597  ? -35.374 90.509  102.652 1.00 20.29 ? 595  PRO   A C     1 
ATOM   4148  O  O     . PRO   A  1 597  ? -35.182 91.377  101.791 1.00 20.55 ? 595  PRO   A O     1 
ATOM   4149  C  CB    . PRO   A  1 597  ? -33.201 89.665  103.622 1.00 19.63 ? 595  PRO   A CB    1 
ATOM   4150  C  CG    . PRO   A  1 597  ? -33.376 88.375  104.315 1.00 23.78 ? 595  PRO   A CG    1 
ATOM   4151  C  CD    . PRO   A  1 597  ? -34.411 88.547  105.399 1.00 20.47 ? 595  PRO   A CD    1 
ATOM   4152  N  N     . GLY   A  1 598  ? -36.356 89.611  102.551 1.00 18.89 ? 596  GLY   A N     1 
ATOM   4153  C  CA    . GLY   A  1 598  ? -37.234 89.646  101.399 1.00 18.07 ? 596  GLY   A CA    1 
ATOM   4154  C  C     . GLY   A  1 598  ? -38.385 90.613  101.514 1.00 19.38 ? 596  GLY   A C     1 
ATOM   4155  O  O     . GLY   A  1 598  ? -39.090 90.849  100.530 1.00 21.11 ? 596  GLY   A O     1 
ATOM   4156  N  N     . ASP   A  1 599  ? -38.565 91.194  102.688 1.00 20.76 ? 597  ASP   A N     1 
ATOM   4157  C  CA    . ASP   A  1 599  ? -39.688 92.074  102.959 1.00 19.17 ? 597  ASP   A CA    1 
ATOM   4158  C  C     . ASP   A  1 599  ? -39.478 92.687  104.326 1.00 19.41 ? 597  ASP   A C     1 
ATOM   4159  O  O     . ASP   A  1 599  ? -39.803 92.058  105.334 1.00 21.51 ? 597  ASP   A O     1 
ATOM   4160  C  CB    . ASP   A  1 599  ? -41.001 91.298  102.921 1.00 20.21 ? 597  ASP   A CB    1 
ATOM   4161  C  CG    . ASP   A  1 599  ? -42.221 92.197  103.015 1.00 25.05 ? 597  ASP   A CG    1 
ATOM   4162  O  OD1   . ASP   A  1 599  ? -42.068 93.388  103.372 1.00 22.27 ? 597  ASP   A OD1   1 
ATOM   4163  O  OD2   . ASP   A  1 599  ? -43.329 91.700  102.710 1.00 27.20 ? 597  ASP   A OD2   1 
ATOM   4164  N  N     . HIS   A  1 600  ? -38.938 93.904  104.374 1.00 22.52 ? 598  HIS   A N     1 
ATOM   4165  C  CA    . HIS   A  1 600  ? -38.577 94.505  105.652 1.00 24.54 ? 598  HIS   A CA    1 
ATOM   4166  C  C     . HIS   A  1 600  ? -39.786 94.827  106.514 1.00 26.14 ? 598  HIS   A C     1 
ATOM   4167  O  O     . HIS   A  1 600  ? -39.613 95.122  107.702 1.00 27.01 ? 598  HIS   A O     1 
ATOM   4168  C  CB    . HIS   A  1 600  ? -37.748 95.763  105.425 1.00 22.54 ? 598  HIS   A CB    1 
ATOM   4169  C  CG    . HIS   A  1 600  ? -36.369 95.480  104.921 1.00 24.39 ? 598  HIS   A CG    1 
ATOM   4170  N  ND1   . HIS   A  1 600  ? -35.417 96.463  104.764 1.00 28.77 ? 598  HIS   A ND1   1 
ATOM   4171  C  CD2   . HIS   A  1 600  ? -35.782 94.319  104.542 1.00 23.82 ? 598  HIS   A CD2   1 
ATOM   4172  C  CE1   . HIS   A  1 600  ? -34.300 95.921  104.312 1.00 29.19 ? 598  HIS   A CE1   1 
ATOM   4173  N  NE2   . HIS   A  1 600  ? -34.494 94.620  104.168 1.00 27.16 ? 598  HIS   A NE2   1 
ATOM   4174  N  N     . ARG   A  1 601  ? -40.996 94.758  105.955 1.00 23.89 ? 599  ARG   A N     1 
ATOM   4175  C  CA    . ARG   A  1 601  ? -42.199 94.888  106.767 1.00 25.90 ? 599  ARG   A CA    1 
ATOM   4176  C  C     . ARG   A  1 601  ? -42.408 93.674  107.656 1.00 24.39 ? 599  ARG   A C     1 
ATOM   4177  O  O     . ARG   A  1 601  ? -43.164 93.753  108.629 1.00 24.03 ? 599  ARG   A O     1 
ATOM   4178  C  CB    . ARG   A  1 601  ? -43.420 95.083  105.872 1.00 26.07 ? 599  ARG   A CB    1 
ATOM   4179  C  CG    . ARG   A  1 601  ? -43.310 96.255  104.923 1.00 28.44 ? 599  ARG   A CG    1 
ATOM   4180  C  CD    . ARG   A  1 601  ? -44.407 96.187  103.889 1.00 27.20 ? 599  ARG   A CD    1 
ATOM   4181  N  NE    . ARG   A  1 601  ? -44.427 94.889  103.224 1.00 28.27 ? 599  ARG   A NE    1 
ATOM   4182  C  CZ    . ARG   A  1 601  ? -45.309 94.537  102.299 1.00 35.20 ? 599  ARG   A CZ    1 
ATOM   4183  N  NH1   . ARG   A  1 601  ? -46.261 95.368  101.898 1.00 34.08 ? 599  ARG   A NH1   1 
ATOM   4184  N  NH2   . ARG   A  1 601  ? -45.230 93.325  101.754 1.00 29.61 ? 599  ARG   A NH2   1 
ATOM   4185  N  N     . ASP   A  1 602  ? -41.745 92.563  107.346 1.00 23.11 ? 600  ASP   A N     1 
ATOM   4186  C  CA    . ASP   A  1 602  ? -41.920 91.299  108.058 1.00 23.36 ? 600  ASP   A CA    1 
ATOM   4187  C  C     . ASP   A  1 602  ? -40.861 91.228  109.150 1.00 25.66 ? 600  ASP   A C     1 
ATOM   4188  O  O     . ASP   A  1 602  ? -39.690 90.932  108.892 1.00 23.75 ? 600  ASP   A O     1 
ATOM   4189  C  CB    . ASP   A  1 602  ? -41.834 90.129  107.083 1.00 22.97 ? 600  ASP   A CB    1 
ATOM   4190  C  CG    . ASP   A  1 602  ? -42.000 88.787  107.759 1.00 27.08 ? 600  ASP   A CG    1 
ATOM   4191  O  OD1   . ASP   A  1 602  ? -42.650 88.736  108.825 1.00 26.21 ? 600  ASP   A OD1   1 
ATOM   4192  O  OD2   . ASP   A  1 602  ? -41.463 87.783  107.228 1.00 25.44 ? 600  ASP   A OD2   1 
ATOM   4193  N  N     . VAL   A  1 603  ? -41.271 91.529  110.377 1.00 26.26 ? 601  VAL   A N     1 
ATOM   4194  C  CA    . VAL   A  1 603  ? -40.375 91.492  111.527 1.00 26.02 ? 601  VAL   A CA    1 
ATOM   4195  C  C     . VAL   A  1 603  ? -40.279 90.055  112.019 1.00 24.20 ? 601  VAL   A C     1 
ATOM   4196  O  O     . VAL   A  1 603  ? -41.288 89.434  112.365 1.00 23.46 ? 601  VAL   A O     1 
ATOM   4197  C  CB    . VAL   A  1 603  ? -40.877 92.423  112.638 1.00 26.22 ? 601  VAL   A CB    1 
ATOM   4198  C  CG1   . VAL   A  1 603  ? -39.893 92.431  113.815 1.00 26.73 ? 601  VAL   A CG1   1 
ATOM   4199  C  CG2   . VAL   A  1 603  ? -41.080 93.817  112.078 1.00 26.85 ? 601  VAL   A CG2   1 
ATOM   4200  N  N     . VAL   A  1 604  ? -39.066 89.522  112.053 1.00 20.96 ? 602  VAL   A N     1 
ATOM   4201  C  CA    . VAL   A  1 604  ? -38.889 88.126  112.424 1.00 20.84 ? 602  VAL   A CA    1 
ATOM   4202  C  C     . VAL   A  1 604  ? -38.686 87.974  113.924 1.00 22.56 ? 602  VAL   A C     1 
ATOM   4203  O  O     . VAL   A  1 604  ? -39.155 87.008  114.529 1.00 22.16 ? 602  VAL   A O     1 
ATOM   4204  C  CB    . VAL   A  1 604  ? -37.709 87.536  111.634 1.00 20.75 ? 602  VAL   A CB    1 
ATOM   4205  C  CG1   . VAL   A  1 604  ? -37.584 86.053  111.907 1.00 20.53 ? 602  VAL   A CG1   1 
ATOM   4206  C  CG2   . VAL   A  1 604  ? -37.892 87.800  110.130 1.00 20.80 ? 602  VAL   A CG2   1 
ATOM   4207  N  N     . GLY   A  1 605  ? -38.001 88.919  114.547 1.00 21.04 ? 603  GLY   A N     1 
ATOM   4208  C  CA    . GLY   A  1 605  ? -37.717 88.791  115.959 1.00 20.85 ? 603  GLY   A CA    1 
ATOM   4209  C  C     . GLY   A  1 605  ? -36.931 89.981  116.447 1.00 21.53 ? 603  GLY   A C     1 
ATOM   4210  O  O     . GLY   A  1 605  ? -36.851 91.016  115.781 1.00 23.27 ? 603  GLY   A O     1 
ATOM   4211  N  N     . SER   A  1 606  ? -36.355 89.822  117.631 1.00 23.06 ? 604  SER   A N     1 
ATOM   4212  C  CA    . SER   A  1 606  ? -35.599 90.890  118.262 1.00 23.79 ? 604  SER   A CA    1 
ATOM   4213  C  C     . SER   A  1 606  ? -34.255 90.353  118.710 1.00 22.53 ? 604  SER   A C     1 
ATOM   4214  O  O     . SER   A  1 606  ? -34.159 89.231  119.215 1.00 22.33 ? 604  SER   A O     1 
ATOM   4215  C  CB    . SER   A  1 606  ? -36.341 91.478  119.466 1.00 27.74 ? 604  SER   A CB    1 
ATOM   4216  O  OG    . SER   A  1 606  ? -37.466 92.206  119.028 1.00 38.29 ? 604  SER   A OG    1 
ATOM   4217  N  N     . VAL   A  1 607  ? -33.216 91.153  118.527 1.00 24.37 ? 605  VAL   A N     1 
ATOM   4218  C  CA    . VAL   A  1 607  ? -31.893 90.792  119.009 1.00 23.57 ? 605  VAL   A CA    1 
ATOM   4219  C  C     . VAL   A  1 607  ? -31.444 91.853  119.998 1.00 25.30 ? 605  VAL   A C     1 
ATOM   4220  O  O     . VAL   A  1 607  ? -31.583 93.055  119.738 1.00 25.38 ? 605  VAL   A O     1 
ATOM   4221  C  CB    . VAL   A  1 607  ? -30.877 90.635  117.865 1.00 21.00 ? 605  VAL   A CB    1 
ATOM   4222  C  CG1   . VAL   A  1 607  ? -30.858 91.877  116.985 1.00 23.34 ? 605  VAL   A CG1   1 
ATOM   4223  C  CG2   . VAL   A  1 607  ? -29.500 90.359  118.440 1.00 21.15 ? 605  VAL   A CG2   1 
ATOM   4224  N  N     . THR   A  1 608  ? -30.963 91.401  121.147 1.00 24.75 ? 606  THR   A N     1 
ATOM   4225  C  CA    . THR   A  1 608  ? -30.279 92.246  122.112 1.00 25.10 ? 606  THR   A CA    1 
ATOM   4226  C  C     . THR   A  1 608  ? -28.799 91.992  121.926 1.00 24.47 ? 606  THR   A C     1 
ATOM   4227  O  O     . THR   A  1 608  ? -28.354 90.842  121.982 1.00 24.83 ? 606  THR   A O     1 
ATOM   4228  C  CB    . THR   A  1 608  ? -30.719 91.914  123.534 1.00 24.66 ? 606  THR   A CB    1 
ATOM   4229  O  OG1   . THR   A  1 608  ? -32.124 92.154  123.642 1.00 27.47 ? 606  THR   A OG1   1 
ATOM   4230  C  CG2   . THR   A  1 608  ? -29.977 92.768  124.548 1.00 29.59 ? 606  THR   A CG2   1 
ATOM   4231  N  N     . GLU   A  1 609  ? -28.048 93.047  121.668 1.00 26.21 ? 607  GLU   A N     1 
ATOM   4232  C  CA    . GLU   A  1 609  ? -26.679 92.870  121.232 1.00 27.38 ? 607  GLU   A CA    1 
ATOM   4233  C  C     . GLU   A  1 609  ? -25.728 93.057  122.405 1.00 27.36 ? 607  GLU   A C     1 
ATOM   4234  O  O     . GLU   A  1 609  ? -26.050 93.720  123.397 1.00 28.67 ? 607  GLU   A O     1 
ATOM   4235  C  CB    . GLU   A  1 609  ? -26.377 93.807  120.056 1.00 30.19 ? 607  GLU   A CB    1 
ATOM   4236  C  CG    . GLU   A  1 609  ? -27.066 93.281  118.775 1.00 30.29 ? 607  GLU   A CG    1 
ATOM   4237  C  CD    . GLU   A  1 609  ? -26.840 94.134  117.538 1.00 39.87 ? 607  GLU   A CD    1 
ATOM   4238  O  OE1   . GLU   A  1 609  ? -26.702 95.371  117.677 1.00 42.79 ? 607  GLU   A OE1   1 
ATOM   4239  O  OE2   . GLU   A  1 609  ? -26.808 93.558  116.421 1.00 36.67 ? 607  GLU   A OE2   1 
ATOM   4240  N  N     . THR   A  1 610  ? -24.573 92.405  122.294 1.00 25.42 ? 608  THR   A N     1 
ATOM   4241  C  CA    . THR   A  1 610  ? -23.612 92.289  123.385 1.00 25.38 ? 608  THR   A CA    1 
ATOM   4242  C  C     . THR   A  1 610  ? -22.749 93.537  123.472 1.00 27.09 ? 608  THR   A C     1 
ATOM   4243  O  O     . THR   A  1 610  ? -22.245 94.021  122.455 1.00 28.39 ? 608  THR   A O     1 
ATOM   4244  C  CB    . THR   A  1 610  ? -22.726 91.062  123.156 1.00 26.42 ? 608  THR   A CB    1 
ATOM   4245  O  OG1   . THR   A  1 610  ? -23.555 89.933  122.878 1.00 22.85 ? 608  THR   A OG1   1 
ATOM   4246  C  CG2   . THR   A  1 610  ? -21.843 90.769  124.378 1.00 25.14 ? 608  THR   A CG2   1 
ATOM   4247  N  N     . SER   A  1 611  ? -22.585 94.061  124.684 1.00 28.71 ? 609  SER   A N     1 
ATOM   4248  C  CA    . SER   A  1 611  ? -21.635 95.139  124.898 1.00 30.70 ? 609  SER   A CA    1 
ATOM   4249  C  C     . SER   A  1 611  ? -20.213 94.606  124.784 1.00 29.65 ? 609  SER   A C     1 
ATOM   4250  O  O     . SER   A  1 611  ? -19.948 93.422  125.013 1.00 28.95 ? 609  SER   A O     1 
ATOM   4251  C  CB    . SER   A  1 611  ? -21.849 95.774  126.270 1.00 32.34 ? 609  SER   A CB    1 
ATOM   4252  O  OG    . SER   A  1 611  ? -21.351 94.920  127.284 1.00 29.48 ? 609  SER   A OG    1 
ATOM   4253  N  N     . GLU   A  1 612  ? -19.287 95.492  124.409 1.00 29.68 ? 610  GLU   A N     1 
ATOM   4254  C  CA    . GLU   A  1 612  ? -17.884 95.095  124.388 1.00 33.59 ? 610  GLU   A CA    1 
ATOM   4255  C  C     . GLU   A  1 612  ? -17.438 94.598  125.755 1.00 30.35 ? 610  GLU   A C     1 
ATOM   4256  O  O     . GLU   A  1 612  ? -16.635 93.665  125.844 1.00 29.93 ? 610  GLU   A O     1 
ATOM   4257  C  CB    . GLU   A  1 612  ? -17.008 96.264  123.934 1.00 35.30 ? 610  GLU   A CB    1 
ATOM   4258  N  N     . GLU   A  1 613  ? -17.965 95.190  126.829 1.00 26.27 ? 611  GLU   A N     1 
ATOM   4259  C  CA    . GLU   A  1 613  ? -17.573 94.746  128.166 1.00 30.10 ? 611  GLU   A CA    1 
ATOM   4260  C  C     . GLU   A  1 613  ? -18.059 93.328  128.436 1.00 29.06 ? 611  GLU   A C     1 
ATOM   4261  O  O     . GLU   A  1 613  ? -17.310 92.507  128.974 1.00 31.86 ? 611  GLU   A O     1 
ATOM   4262  C  CB    . GLU   A  1 613  ? -18.097 95.709  129.238 1.00 29.86 ? 611  GLU   A CB    1 
ATOM   4263  N  N     . ASP   A  1 614  ? -19.299 93.012  128.050 1.00 30.39 ? 612  ASP   A N     1 
ATOM   4264  C  CA    . ASP   A  1 614  ? -19.825 91.670  128.294 1.00 28.33 ? 612  ASP   A CA    1 
ATOM   4265  C  C     . ASP   A  1 614  ? -19.138 90.624  127.421 1.00 25.77 ? 612  ASP   A C     1 
ATOM   4266  O  O     . ASP   A  1 614  ? -18.934 89.486  127.859 1.00 26.34 ? 612  ASP   A O     1 
ATOM   4267  C  CB    . ASP   A  1 614  ? -21.338 91.655  128.081 1.00 30.71 ? 612  ASP   A CB    1 
ATOM   4268  C  CG    . ASP   A  1 614  ? -22.085 92.268  129.249 1.00 34.92 ? 612  ASP   A CG    1 
ATOM   4269  O  OD1   . ASP   A  1 614  ? -21.529 92.246  130.370 1.00 37.16 ? 612  ASP   A OD1   1 
ATOM   4270  O  OD2   . ASP   A  1 614  ? -23.209 92.778  129.058 1.00 34.31 ? 612  ASP   A OD2   1 
ATOM   4271  N  N     . ALA   A  1 615  ? -18.774 90.983  126.188 1.00 25.40 ? 613  ALA   A N     1 
ATOM   4272  C  CA    . ALA   A  1 615  ? -17.963 90.088  125.368 1.00 27.24 ? 613  ALA   A CA    1 
ATOM   4273  C  C     . ALA   A  1 615  ? -16.673 89.716  126.087 1.00 25.62 ? 613  ALA   A C     1 
ATOM   4274  O  O     . ALA   A  1 615  ? -16.298 88.538  126.149 1.00 25.60 ? 613  ALA   A O     1 
ATOM   4275  C  CB    . ALA   A  1 615  ? -17.652 90.739  124.022 1.00 29.03 ? 613  ALA   A CB    1 
ATOM   4276  N  N     . ARG   A  1 616  ? -15.977 90.714  126.641 1.00 26.75 ? 614  ARG   A N     1 
ATOM   4277  C  CA    . ARG   A  1 616  ? -14.744 90.430  127.365 1.00 28.70 ? 614  ARG   A CA    1 
ATOM   4278  C  C     . ARG   A  1 616  ? -15.027 89.621  128.621 1.00 28.19 ? 614  ARG   A C     1 
ATOM   4279  O  O     . ARG   A  1 616  ? -14.246 88.733  128.983 1.00 26.23 ? 614  ARG   A O     1 
ATOM   4280  C  CB    . ARG   A  1 616  ? -14.023 91.734  127.709 1.00 32.20 ? 614  ARG   A CB    1 
ATOM   4281  C  CG    . ARG   A  1 616  ? -13.527 92.490  126.488 1.00 36.35 ? 614  ARG   A CG    1 
ATOM   4282  C  CD    . ARG   A  1 616  ? -12.624 93.654  126.871 1.00 38.77 ? 614  ARG   A CD    1 
ATOM   4283  N  NE    . ARG   A  1 616  ? -13.311 94.607  127.734 1.00 46.81 ? 614  ARG   A NE    1 
ATOM   4284  C  CZ    . ARG   A  1 616  ? -13.925 95.704  127.311 1.00 45.20 ? 614  ARG   A CZ    1 
ATOM   4285  N  NH1   . ARG   A  1 616  ? -13.948 96.034  126.028 1.00 48.33 ? 614  ARG   A NH1   1 
ATOM   4286  N  NH2   . ARG   A  1 616  ? -14.527 96.492  128.197 1.00 42.33 ? 614  ARG   A NH2   1 
ATOM   4287  N  N     . ARG   A  1 617  ? -16.142 89.913  129.293 1.00 26.41 ? 615  ARG   A N     1 
ATOM   4288  C  CA    . ARG   A  1 617  ? -16.515 89.128  130.461 1.00 27.18 ? 615  ARG   A CA    1 
ATOM   4289  C  C     . ARG   A  1 617  ? -16.832 87.692  130.070 1.00 26.02 ? 615  ARG   A C     1 
ATOM   4290  O  O     . ARG   A  1 617  ? -16.475 86.752  130.789 1.00 25.16 ? 615  ARG   A O     1 
ATOM   4291  C  CB    . ARG   A  1 617  ? -17.704 89.772  131.169 1.00 28.33 ? 615  ARG   A CB    1 
ATOM   4292  C  CG    . ARG   A  1 617  ? -18.033 89.128  132.496 1.00 35.87 ? 615  ARG   A CG    1 
ATOM   4293  C  CD    . ARG   A  1 617  ? -18.797 90.078  133.406 1.00 42.61 ? 615  ARG   A CD    1 
ATOM   4294  N  NE    . ARG   A  1 617  ? -20.069 90.500  132.831 1.00 42.69 ? 615  ARG   A NE    1 
ATOM   4295  C  CZ    . ARG   A  1 617  ? -21.211 89.836  132.962 1.00 48.59 ? 615  ARG   A CZ    1 
ATOM   4296  N  NH1   . ARG   A  1 617  ? -21.275 88.688  133.625 1.00 42.79 ? 615  ARG   A NH1   1 
ATOM   4297  N  NH2   . ARG   A  1 617  ? -22.319 90.335  132.416 1.00 40.30 ? 615  ARG   A NH2   1 
ATOM   4298  N  N     . ALA   A  1 618  ? -17.494 87.504  128.924 1.00 25.44 ? 616  ALA   A N     1 
ATOM   4299  C  CA    . ALA   A  1 618  ? -17.792 86.154  128.451 1.00 22.91 ? 616  ALA   A CA    1 
ATOM   4300  C  C     . ALA   A  1 618  ? -16.522 85.330  128.278 1.00 24.13 ? 616  ALA   A C     1 
ATOM   4301  O  O     . ALA   A  1 618  ? -16.486 84.146  128.639 1.00 22.68 ? 616  ALA   A O     1 
ATOM   4302  C  CB    . ALA   A  1 618  ? -18.578 86.214  127.136 1.00 21.94 ? 616  ALA   A CB    1 
ATOM   4303  N  N     . VAL   A  1 619  ? -15.462 85.929  127.727 1.00 23.94 ? 617  VAL   A N     1 
ATOM   4304  C  CA    . VAL   A  1 619  ? -14.231 85.166  127.552 1.00 24.67 ? 617  VAL   A CA    1 
ATOM   4305  C  C     . VAL   A  1 619  ? -13.666 84.769  128.905 1.00 22.38 ? 617  VAL   A C     1 
ATOM   4306  O  O     . VAL   A  1 619  ? -13.189 83.641  129.084 1.00 23.55 ? 617  VAL   A O     1 
ATOM   4307  C  CB    . VAL   A  1 619  ? -13.197 85.950  126.722 1.00 23.56 ? 617  VAL   A CB    1 
ATOM   4308  C  CG1   . VAL   A  1 619  ? -11.898 85.137  126.584 1.00 24.34 ? 617  VAL   A CG1   1 
ATOM   4309  C  CG2   . VAL   A  1 619  ? -13.757 86.278  125.355 1.00 24.80 ? 617  VAL   A CG2   1 
ATOM   4310  N  N     . ARG   A  1 620  ? -13.709 85.683  129.882 1.00 22.64 ? 618  ARG   A N     1 
ATOM   4311  C  CA    . ARG   A  1 620  ? -13.174 85.345  131.197 1.00 26.64 ? 618  ARG   A CA    1 
ATOM   4312  C  C     . ARG   A  1 620  ? -13.991 84.243  131.846 1.00 26.44 ? 618  ARG   A C     1 
ATOM   4313  O  O     . ARG   A  1 620  ? -13.429 83.351  132.494 1.00 25.96 ? 618  ARG   A O     1 
ATOM   4314  C  CB    . ARG   A  1 620  ? -13.107 86.586  132.092 1.00 25.72 ? 618  ARG   A CB    1 
ATOM   4315  C  CG    . ARG   A  1 620  ? -11.983 87.528  131.675 1.00 35.25 ? 618  ARG   A CG    1 
ATOM   4316  C  CD    . ARG   A  1 620  ? -11.841 88.737  132.596 1.00 40.75 ? 618  ARG   A CD    1 
ATOM   4317  N  NE    . ARG   A  1 620  ? -12.430 89.934  132.005 1.00 44.85 ? 618  ARG   A NE    1 
ATOM   4318  C  CZ    . ARG   A  1 620  ? -13.578 90.472  132.391 1.00 40.43 ? 618  ARG   A CZ    1 
ATOM   4319  N  NH1   . ARG   A  1 620  ? -14.263 89.982  133.412 1.00 48.26 ? 618  ARG   A NH1   1 
ATOM   4320  N  NH2   . ARG   A  1 620  ? -14.048 91.534  131.741 1.00 40.73 ? 618  ARG   A NH2   1 
ATOM   4321  N  N     . LEU   A  1 621  ? -15.313 84.268  131.657 1.00 22.98 ? 619  LEU   A N     1 
ATOM   4322  C  CA    . LEU   A  1 621  ? -16.156 83.204  132.193 1.00 25.72 ? 619  LEU   A CA    1 
ATOM   4323  C  C     . LEU   A  1 621  ? -15.867 81.870  131.521 1.00 26.47 ? 619  LEU   A C     1 
ATOM   4324  O  O     . LEU   A  1 621  ? -15.856 80.827  132.185 1.00 26.03 ? 619  LEU   A O     1 
ATOM   4325  C  CB    . LEU   A  1 621  ? -17.625 83.563  132.023 1.00 23.85 ? 619  LEU   A CB    1 
ATOM   4326  C  CG    . LEU   A  1 621  ? -18.131 84.692  132.908 1.00 26.91 ? 619  LEU   A CG    1 
ATOM   4327  C  CD1   . LEU   A  1 621  ? -19.471 85.134  132.382 1.00 30.32 ? 619  LEU   A CD1   1 
ATOM   4328  C  CD2   . LEU   A  1 621  ? -18.242 84.204  134.336 1.00 29.77 ? 619  LEU   A CD2   1 
ATOM   4329  N  N     . ALA   A  1 622  ? -15.655 81.883  130.199 1.00 22.78 ? 620  ALA   A N     1 
ATOM   4330  C  CA    . ALA   A  1 622  ? -15.277 80.664  129.488 1.00 22.52 ? 620  ALA   A CA    1 
ATOM   4331  C  C     . ALA   A  1 622  ? -13.942 80.128  129.988 1.00 24.49 ? 620  ALA   A C     1 
ATOM   4332  O  O     . ALA   A  1 622  ? -13.780 78.918  130.168 1.00 24.18 ? 620  ALA   A O     1 
ATOM   4333  C  CB    . ALA   A  1 622  ? -15.203 80.932  127.984 1.00 21.30 ? 620  ALA   A CB    1 
ATOM   4334  N  N     . ALA   A  1 623  ? -12.969 81.015  130.207 1.00 22.74 ? 621  ALA   A N     1 
ATOM   4335  C  CA    . ALA   A  1 623  ? -11.690 80.567  130.742 1.00 24.17 ? 621  ALA   A CA    1 
ATOM   4336  C  C     . ALA   A  1 623  ? -11.875 79.901  132.096 1.00 24.95 ? 621  ALA   A C     1 
ATOM   4337  O  O     . ALA   A  1 623  ? -11.273 78.858  132.370 1.00 25.11 ? 621  ALA   A O     1 
ATOM   4338  C  CB    . ALA   A  1 623  ? -10.716 81.738  130.846 1.00 25.92 ? 621  ALA   A CB    1 
ATOM   4339  N  N     . ASP   A  1 624  ? -12.719 80.481  132.950 1.00 27.16 ? 622  ASP   A N     1 
ATOM   4340  C  CA    . ASP   A  1 624  ? -12.935 79.904  134.272 1.00 30.37 ? 622  ASP   A CA    1 
ATOM   4341  C  C     . ASP   A  1 624  ? -13.590 78.533  134.167 1.00 29.91 ? 622  ASP   A C     1 
ATOM   4342  O  O     . ASP   A  1 624  ? -13.249 77.613  134.917 1.00 36.76 ? 622  ASP   A O     1 
ATOM   4343  C  CB    . ASP   A  1 624  ? -13.788 80.843  135.124 1.00 32.22 ? 622  ASP   A CB    1 
ATOM   4344  C  CG    . ASP   A  1 624  ? -13.101 82.168  135.400 1.00 41.46 ? 622  ASP   A CG    1 
ATOM   4345  O  OD1   . ASP   A  1 624  ? -11.853 82.235  135.305 1.00 45.23 ? 622  ASP   A OD1   1 
ATOM   4346  O  OD2   . ASP   A  1 624  ? -13.813 83.145  135.716 1.00 49.75 ? 622  ASP   A OD2   1 
ATOM   4347  N  N     . ALA   A  1 625  ? -14.507 78.371  133.220 1.00 31.39 ? 623  ALA   A N     1 
ATOM   4348  C  CA    . ALA   A  1 625  ? -15.226 77.118  133.049 1.00 34.00 ? 623  ALA   A CA    1 
ATOM   4349  C  C     . ALA   A  1 625  ? -14.484 76.094  132.203 1.00 30.13 ? 623  ALA   A C     1 
ATOM   4350  O  O     . ALA   A  1 625  ? -14.963 74.963  132.079 1.00 28.95 ? 623  ALA   A O     1 
ATOM   4351  C  CB    . ALA   A  1 625  ? -16.585 77.387  132.411 1.00 36.15 ? 623  ALA   A CB    1 
ATOM   4352  N  N     . ALA   A  1 626  ? -13.349 76.461  131.607 1.00 29.03 ? 624  ALA   A N     1 
ATOM   4353  C  CA    . ALA   A  1 626  ? -12.680 75.558  130.675 1.00 25.21 ? 624  ALA   A CA    1 
ATOM   4354  C  C     . ALA   A  1 626  ? -12.282 74.230  131.307 1.00 26.92 ? 624  ALA   A C     1 
ATOM   4355  O  O     . ALA   A  1 626  ? -12.528 73.182  130.685 1.00 29.80 ? 624  ALA   A O     1 
ATOM   4356  C  CB    . ALA   A  1 626  ? -11.469 76.267  130.057 1.00 25.69 ? 624  ALA   A CB    1 
ATOM   4357  N  N     . PRO   A  1 627  ? -11.676 74.182  132.503 1.00 30.75 ? 625  PRO   A N     1 
ATOM   4358  C  CA    . PRO   A  1 627  ? -11.328 72.865  133.068 1.00 31.70 ? 625  PRO   A CA    1 
ATOM   4359  C  C     . PRO   A  1 627  ? -12.531 71.964  133.294 1.00 30.61 ? 625  PRO   A C     1 
ATOM   4360  O  O     . PRO   A  1 627  ? -12.426 70.746  133.115 1.00 32.67 ? 625  PRO   A O     1 
ATOM   4361  C  CB    . PRO   A  1 627  ? -10.638 73.227  134.390 1.00 34.86 ? 625  PRO   A CB    1 
ATOM   4362  C  CG    . PRO   A  1 627  ? -10.106 74.603  134.171 1.00 33.13 ? 625  PRO   A CG    1 
ATOM   4363  C  CD    . PRO   A  1 627  ? -11.137 75.283  133.328 1.00 31.06 ? 625  PRO   A CD    1 
ATOM   4364  N  N     . ASP   A  1 628  ? -13.671 72.525  133.695 1.00 31.03 ? 626  ASP   A N     1 
ATOM   4365  C  CA    . ASP   A  1 628  ? -14.842 71.694  133.944 1.00 31.23 ? 626  ASP   A CA    1 
ATOM   4366  C  C     . ASP   A  1 628  ? -15.355 71.070  132.655 1.00 32.31 ? 626  ASP   A C     1 
ATOM   4367  O  O     . ASP   A  1 628  ? -15.695 69.881  132.624 1.00 31.45 ? 626  ASP   A O     1 
ATOM   4368  C  CB    . ASP   A  1 628  ? -15.941 72.513  134.621 1.00 30.88 ? 626  ASP   A CB    1 
ATOM   4369  C  CG    . ASP   A  1 628  ? -15.598 72.864  136.059 1.00 39.46 ? 626  ASP   A CG    1 
ATOM   4370  O  OD1   . ASP   A  1 628  ? -14.506 72.466  136.518 1.00 43.73 ? 626  ASP   A OD1   1 
ATOM   4371  O  OD2   . ASP   A  1 628  ? -16.409 73.540  136.723 1.00 40.18 ? 626  ASP   A OD2   1 
ATOM   4372  N  N     . TRP   A  1 629  ? -15.408 71.847  131.575 1.00 27.86 ? 627  TRP   A N     1 
ATOM   4373  C  CA    . TRP   A  1 629  ? -15.873 71.282  130.321 1.00 23.59 ? 627  TRP   A CA    1 
ATOM   4374  C  C     . TRP   A  1 629  ? -14.845 70.315  129.743 1.00 28.72 ? 627  TRP   A C     1 
ATOM   4375  O  O     . TRP   A  1 629  ? -15.208 69.254  129.217 1.00 25.21 ? 627  TRP   A O     1 
ATOM   4376  C  CB    . TRP   A  1 629  ? -16.190 72.398  129.334 1.00 24.65 ? 627  TRP   A CB    1 
ATOM   4377  C  CG    . TRP   A  1 629  ? -16.662 71.866  128.038 1.00 23.40 ? 627  TRP   A CG    1 
ATOM   4378  C  CD1   . TRP   A  1 629  ? -16.063 72.031  126.814 1.00 20.91 ? 627  TRP   A CD1   1 
ATOM   4379  C  CD2   . TRP   A  1 629  ? -17.817 71.050  127.816 1.00 22.89 ? 627  TRP   A CD2   1 
ATOM   4380  N  NE1   . TRP   A  1 629  ? -16.788 71.388  125.851 1.00 20.74 ? 627  TRP   A NE1   1 
ATOM   4381  C  CE2   . TRP   A  1 629  ? -17.867 70.773  126.434 1.00 20.07 ? 627  TRP   A CE2   1 
ATOM   4382  C  CE3   . TRP   A  1 629  ? -18.811 70.526  128.648 1.00 23.10 ? 627  TRP   A CE3   1 
ATOM   4383  C  CZ2   . TRP   A  1 629  ? -18.871 69.995  125.862 1.00 21.11 ? 627  TRP   A CZ2   1 
ATOM   4384  C  CZ3   . TRP   A  1 629  ? -19.810 69.758  128.081 1.00 25.22 ? 627  TRP   A CZ3   1 
ATOM   4385  C  CH2   . TRP   A  1 629  ? -19.835 69.500  126.698 1.00 25.54 ? 627  TRP   A CH2   1 
ATOM   4386  N  N     . ALA   A  1 630  ? -13.554 70.652  129.854 1.00 25.59 ? 628  ALA   A N     1 
ATOM   4387  C  CA    . ALA   A  1 630  ? -12.519 69.744  129.376 1.00 28.39 ? 628  ALA   A CA    1 
ATOM   4388  C  C     . ALA   A  1 630  ? -12.573 68.407  130.105 1.00 28.48 ? 628  ALA   A C     1 
ATOM   4389  O  O     . ALA   A  1 630  ? -12.179 67.380  129.545 1.00 27.60 ? 628  ALA   A O     1 
ATOM   4390  C  CB    . ALA   A  1 630  ? -11.145 70.388  129.534 1.00 27.82 ? 628  ALA   A CB    1 
ATOM   4391  N  N     . ALA   A  1 631  ? -13.079 68.400  131.341 1.00 27.11 ? 629  ALA   A N     1 
ATOM   4392  C  CA    . ALA   A  1 631  ? -13.119 67.191  132.152 1.00 31.39 ? 629  ALA   A CA    1 
ATOM   4393  C  C     . ALA   A  1 631  ? -14.294 66.289  131.807 1.00 27.49 ? 629  ALA   A C     1 
ATOM   4394  O  O     . ALA   A  1 631  ? -14.299 65.124  132.208 1.00 28.89 ? 629  ALA   A O     1 
ATOM   4395  C  CB    . ALA   A  1 631  ? -13.168 67.552  133.640 1.00 33.00 ? 629  ALA   A CB    1 
ATOM   4396  N  N     . VAL   A  1 632  ? -15.282 66.787  131.070 1.00 28.92 ? 630  VAL   A N     1 
ATOM   4397  C  CA    . VAL   A  1 632  ? -16.375 65.940  130.597 1.00 25.77 ? 630  VAL   A CA    1 
ATOM   4398  C  C     . VAL   A  1 632  ? -15.782 64.976  129.575 1.00 27.76 ? 630  VAL   A C     1 
ATOM   4399  O  O     . VAL   A  1 632  ? -15.146 65.421  128.606 1.00 25.55 ? 630  VAL   A O     1 
ATOM   4400  C  CB    . VAL   A  1 632  ? -17.515 66.789  130.017 1.00 27.09 ? 630  VAL   A CB    1 
ATOM   4401  C  CG1   . VAL   A  1 632  ? -18.600 65.914  129.381 1.00 24.46 ? 630  VAL   A CG1   1 
ATOM   4402  C  CG2   . VAL   A  1 632  ? -18.102 67.678  131.132 1.00 24.87 ? 630  VAL   A CG2   1 
ATOM   4403  N  N     . PRO   A  1 633  ? -15.936 63.668  129.758 1.00 27.38 ? 631  PRO   A N     1 
ATOM   4404  C  CA    . PRO   A  1 633  ? -15.282 62.707  128.863 1.00 23.40 ? 631  PRO   A CA    1 
ATOM   4405  C  C     . PRO   A  1 633  ? -15.720 62.924  127.425 1.00 27.16 ? 631  PRO   A C     1 
ATOM   4406  O  O     . PRO   A  1 633  ? -16.875 63.298  127.166 1.00 22.39 ? 631  PRO   A O     1 
ATOM   4407  C  CB    . PRO   A  1 633  ? -15.759 61.346  129.392 1.00 27.83 ? 631  PRO   A CB    1 
ATOM   4408  C  CG    . PRO   A  1 633  ? -16.156 61.597  130.806 1.00 26.01 ? 631  PRO   A CG    1 
ATOM   4409  C  CD    . PRO   A  1 633  ? -16.697 63.003  130.832 1.00 26.45 ? 631  PRO   A CD    1 
ATOM   4410  N  N     . PRO   A  1 634  ? -14.814 62.724  126.461 1.00 22.82 ? 632  PRO   A N     1 
ATOM   4411  C  CA    . PRO   A  1 634  ? -15.156 63.014  125.056 1.00 21.76 ? 632  PRO   A CA    1 
ATOM   4412  C  C     . PRO   A  1 634  ? -16.436 62.351  124.576 1.00 21.77 ? 632  PRO   A C     1 
ATOM   4413  O  O     . PRO   A  1 634  ? -17.190 62.963  123.813 1.00 20.84 ? 632  PRO   A O     1 
ATOM   4414  C  CB    . PRO   A  1 634  ? -13.943 62.477  124.286 1.00 23.18 ? 632  PRO   A CB    1 
ATOM   4415  C  CG    . PRO   A  1 634  ? -12.805 62.525  125.277 1.00 27.40 ? 632  PRO   A CG    1 
ATOM   4416  C  CD    . PRO   A  1 634  ? -13.406 62.315  126.637 1.00 23.57 ? 632  PRO   A CD    1 
ATOM   4417  N  N     . SER   A  1 635  ? -16.686 61.104  124.976 1.00 22.03 ? 633  SER   A N     1 
ATOM   4418  C  CA    . SER   A  1 635  ? -17.885 60.409  124.511 1.00 24.32 ? 633  SER   A CA    1 
ATOM   4419  C  C     . SER   A  1 635  ? -19.157 61.063  125.036 1.00 23.90 ? 633  SER   A C     1 
ATOM   4420  O  O     . SER   A  1 635  ? -20.199 61.015  124.369 1.00 21.16 ? 633  SER   A O     1 
ATOM   4421  C  CB    . SER   A  1 635  ? -17.837 58.943  124.936 1.00 27.59 ? 633  SER   A CB    1 
ATOM   4422  O  OG    . SER   A  1 635  ? -17.929 58.848  126.346 1.00 34.79 ? 633  SER   A OG    1 
ATOM   4423  N  N     . GLU   A  1 636  ? -19.094 61.672  126.218 1.00 20.81 ? 634  GLU   A N     1 
ATOM   4424  C  CA    . GLU   A  1 636  ? -20.248 62.387  126.751 1.00 23.42 ? 634  GLU   A CA    1 
ATOM   4425  C  C     . GLU   A  1 636  ? -20.420 63.728  126.055 1.00 21.59 ? 634  GLU   A C     1 
ATOM   4426  O  O     . GLU   A  1 636  ? -21.550 64.131  125.755 1.00 22.75 ? 634  GLU   A O     1 
ATOM   4427  C  CB    . GLU   A  1 636  ? -20.111 62.584  128.261 1.00 25.11 ? 634  GLU   A CB    1 
ATOM   4428  N  N     . ARG   A  1 637  ? -19.311 64.419  125.766 1.00 21.92 ? 635  ARG   A N     1 
ATOM   4429  C  CA    . ARG   A  1 637  ? -19.402 65.611  124.933 1.00 21.33 ? 635  ARG   A CA    1 
ATOM   4430  C  C     . ARG   A  1 637  ? -20.006 65.275  123.576 1.00 20.02 ? 635  ARG   A C     1 
ATOM   4431  O  O     . ARG   A  1 637  ? -20.867 66.009  123.077 1.00 21.64 ? 635  ARG   A O     1 
ATOM   4432  C  CB    . ARG   A  1 637  ? -18.025 66.253  124.773 1.00 20.61 ? 635  ARG   A CB    1 
ATOM   4433  C  CG    . ARG   A  1 637  ? -17.350 66.579  126.112 1.00 22.58 ? 635  ARG   A CG    1 
ATOM   4434  C  CD    . ARG   A  1 637  ? -16.163 67.521  125.949 1.00 23.16 ? 635  ARG   A CD    1 
ATOM   4435  N  NE    . ARG   A  1 637  ? -15.153 67.027  125.027 1.00 23.33 ? 635  ARG   A NE    1 
ATOM   4436  C  CZ    . ARG   A  1 637  ? -13.923 66.652  125.367 1.00 24.31 ? 635  ARG   A CZ    1 
ATOM   4437  N  NH1   . ARG   A  1 637  ? -13.526 66.630  126.631 1.00 27.26 ? 635  ARG   A NH1   1 
ATOM   4438  N  NH2   . ARG   A  1 637  ? -13.065 66.308  124.413 1.00 24.99 ? 635  ARG   A NH2   1 
ATOM   4439  N  N     . ALA   A  1 638  ? -19.584 64.155  122.977 1.00 21.02 ? 636  ALA   A N     1 
ATOM   4440  C  CA    . ALA   A  1 638  ? -20.158 63.733  121.700 1.00 19.54 ? 636  ALA   A CA    1 
ATOM   4441  C  C     . ALA   A  1 638  ? -21.633 63.391  121.846 1.00 20.53 ? 636  ALA   A C     1 
ATOM   4442  O  O     . ALA   A  1 638  ? -22.430 63.662  120.940 1.00 18.73 ? 636  ALA   A O     1 
ATOM   4443  C  CB    . ALA   A  1 638  ? -19.398 62.530  121.141 1.00 19.96 ? 636  ALA   A CB    1 
ATOM   4444  N  N     . ALA   A  1 639  ? -22.013 62.789  122.976 1.00 21.82 ? 637  ALA   A N     1 
ATOM   4445  C  CA    . ALA   A  1 639  ? -23.426 62.503  123.215 1.00 21.54 ? 637  ALA   A CA    1 
ATOM   4446  C  C     . ALA   A  1 639  ? -24.245 63.789  123.238 1.00 21.98 ? 637  ALA   A C     1 
ATOM   4447  O  O     . ALA   A  1 639  ? -25.389 63.806  122.774 1.00 21.25 ? 637  ALA   A O     1 
ATOM   4448  C  CB    . ALA   A  1 639  ? -23.609 61.722  124.522 1.00 22.42 ? 637  ALA   A CB    1 
ATOM   4449  N  N     . CYS   A  1 640  ? -23.682 64.876  123.785 1.00 19.55 ? 638  CYS   A N     1 
ATOM   4450  C  CA    . CYS   A  1 640  ? -24.362 66.164  123.697 1.00 19.80 ? 638  CYS   A CA    1 
ATOM   4451  C  C     . CYS   A  1 640  ? -24.617 66.531  122.247 1.00 21.94 ? 638  CYS   A C     1 
ATOM   4452  O  O     . CYS   A  1 640  ? -25.723 66.938  121.879 1.00 20.46 ? 638  CYS   A O     1 
ATOM   4453  C  CB    . CYS   A  1 640  ? -23.548 67.259  124.367 1.00 22.61 ? 638  CYS   A CB    1 
ATOM   4454  S  SG    . CYS   A  1 640  ? -23.432 67.106  126.133 1.00 25.13 ? 638  CYS   A SG    1 
ATOM   4455  N  N     . LEU   A  1 641  ? -23.595 66.389  121.406 1.00 19.18 ? 639  LEU   A N     1 
ATOM   4456  C  CA    . LEU   A  1 641  ? -23.765 66.693  119.992 1.00 18.42 ? 639  LEU   A CA    1 
ATOM   4457  C  C     . LEU   A  1 641  ? -24.853 65.826  119.378 1.00 19.31 ? 639  LEU   A C     1 
ATOM   4458  O  O     . LEU   A  1 641  ? -25.713 66.322  118.645 1.00 18.17 ? 639  LEU   A O     1 
ATOM   4459  C  CB    . LEU   A  1 641  ? -22.445 66.504  119.254 1.00 18.18 ? 639  LEU   A CB    1 
ATOM   4460  C  CG    . LEU   A  1 641  ? -21.588 67.759  119.137 1.00 21.15 ? 639  LEU   A CG    1 
ATOM   4461  C  CD1   . LEU   A  1 641  ? -21.248 68.293  120.509 1.00 20.24 ? 639  LEU   A CD1   1 
ATOM   4462  C  CD2   . LEU   A  1 641  ? -20.331 67.479  118.323 1.00 18.63 ? 639  LEU   A CD2   1 
ATOM   4463  N  N     . ASP   A  1 642  ? -24.836 64.525  119.669 1.00 20.95 ? 640  ASP   A N     1 
ATOM   4464  C  CA    . ASP   A  1 642  ? -25.824 63.644  119.064 1.00 21.40 ? 640  ASP   A CA    1 
ATOM   4465  C  C     . ASP   A  1 642  ? -27.231 63.995  119.535 1.00 20.99 ? 640  ASP   A C     1 
ATOM   4466  O  O     . ASP   A  1 642  ? -28.187 63.907  118.758 1.00 19.34 ? 640  ASP   A O     1 
ATOM   4467  C  CB    . ASP   A  1 642  ? -25.504 62.183  119.377 1.00 21.33 ? 640  ASP   A CB    1 
ATOM   4468  C  CG    . ASP   A  1 642  ? -24.388 61.626  118.505 1.00 24.16 ? 640  ASP   A CG    1 
ATOM   4469  O  OD1   . ASP   A  1 642  ? -24.177 62.144  117.387 1.00 22.50 ? 640  ASP   A OD1   1 
ATOM   4470  O  OD2   . ASP   A  1 642  ? -23.726 60.662  118.945 1.00 23.93 ? 640  ASP   A OD2   1 
ATOM   4471  N  N     . ARG   A  1 643  ? -27.381 64.376  120.808 1.00 20.77 ? 641  ARG   A N     1 
ATOM   4472  C  CA    . ARG   A  1 643  ? -28.707 64.771  121.289 1.00 21.56 ? 641  ARG   A CA    1 
ATOM   4473  C  C     . ARG   A  1 643  ? -29.165 66.060  120.627 1.00 19.83 ? 641  ARG   A C     1 
ATOM   4474  O  O     . ARG   A  1 643  ? -30.348 66.212  120.305 1.00 22.89 ? 641  ARG   A O     1 
ATOM   4475  C  CB    . ARG   A  1 643  ? -28.711 64.928  122.812 1.00 20.52 ? 641  ARG   A CB    1 
ATOM   4476  C  CG    . ARG   A  1 643  ? -28.838 63.614  123.565 1.00 25.42 ? 641  ARG   A CG    1 
ATOM   4477  C  CD    . ARG   A  1 643  ? -28.986 63.810  125.079 1.00 24.90 ? 641  ARG   A CD    1 
ATOM   4478  N  NE    . ARG   A  1 643  ? -27.877 64.543  125.678 1.00 25.14 ? 641  ARG   A NE    1 
ATOM   4479  C  CZ    . ARG   A  1 643  ? -26.838 63.973  126.276 1.00 25.15 ? 641  ARG   A CZ    1 
ATOM   4480  N  NH1   . ARG   A  1 643  ? -26.736 62.657  126.390 1.00 24.68 ? 641  ARG   A NH1   1 
ATOM   4481  N  NH2   . ARG   A  1 643  ? -25.877 64.743  126.776 1.00 25.30 ? 641  ARG   A NH2   1 
ATOM   4482  N  N     . ALA   A  1 644  ? -28.243 67.005  120.420 1.00 18.87 ? 642  ALA   A N     1 
ATOM   4483  C  CA    . ALA   A  1 644  ? -28.607 68.224  119.709 1.00 18.60 ? 642  ALA   A CA    1 
ATOM   4484  C  C     . ALA   A  1 644  ? -29.021 67.911  118.278 1.00 19.43 ? 642  ALA   A C     1 
ATOM   4485  O  O     . ALA   A  1 644  ? -29.955 68.524  117.751 1.00 18.22 ? 642  ALA   A O     1 
ATOM   4486  C  CB    . ALA   A  1 644  ? -27.450 69.222  119.730 1.00 21.18 ? 642  ALA   A CB    1 
ATOM   4487  N  N     . ALA   A  1 645  ? -28.349 66.945  117.635 1.00 18.67 ? 643  ALA   A N     1 
ATOM   4488  C  CA    . ALA   A  1 645  ? -28.759 66.552  116.288 1.00 18.92 ? 643  ALA   A CA    1 
ATOM   4489  C  C     . ALA   A  1 645  ? -30.187 66.023  116.273 1.00 19.72 ? 643  ALA   A C     1 
ATOM   4490  O  O     . ALA   A  1 645  ? -30.974 66.356  115.375 1.00 20.53 ? 643  ALA   A O     1 
ATOM   4491  C  CB    . ALA   A  1 645  ? -27.809 65.498  115.719 1.00 19.97 ? 643  ALA   A CB    1 
ATOM   4492  N  N     . GLU   A  1 646  ? -30.532 65.178  117.243 1.00 20.15 ? 644  GLU   A N     1 
ATOM   4493  C  CA    . GLU   A  1 646  ? -31.902 64.679  117.325 1.00 21.97 ? 644  GLU   A CA    1 
ATOM   4494  C  C     . GLU   A  1 646  ? -32.892 65.822  117.515 1.00 21.96 ? 644  GLU   A C     1 
ATOM   4495  O  O     . GLU   A  1 646  ? -33.977 65.820  116.923 1.00 21.48 ? 644  GLU   A O     1 
ATOM   4496  C  CB    . GLU   A  1 646  ? -32.037 63.680  118.475 1.00 23.86 ? 644  GLU   A CB    1 
ATOM   4497  C  CG    . GLU   A  1 646  ? -31.181 62.449  118.328 1.00 29.54 ? 644  GLU   A CG    1 
ATOM   4498  C  CD    . GLU   A  1 646  ? -31.614 61.602  117.158 1.00 32.86 ? 644  GLU   A CD    1 
ATOM   4499  O  OE1   . GLU   A  1 646  ? -32.843 61.407  117.003 1.00 36.66 ? 644  GLU   A OE1   1 
ATOM   4500  O  OE2   . GLU   A  1 646  ? -30.731 61.155  116.389 1.00 31.08 ? 644  GLU   A OE2   1 
ATOM   4501  N  N     . LEU   A  1 647  ? -32.547 66.791  118.367 1.00 22.54 ? 645  LEU   A N     1 
ATOM   4502  C  CA    . LEU   A  1 647  ? -33.431 67.928  118.602 1.00 21.58 ? 645  LEU   A CA    1 
ATOM   4503  C  C     . LEU   A  1 647  ? -33.605 68.760  117.340 1.00 23.53 ? 645  LEU   A C     1 
ATOM   4504  O  O     . LEU   A  1 647  ? -34.718 69.198  117.023 1.00 21.47 ? 645  LEU   A O     1 
ATOM   4505  C  CB    . LEU   A  1 647  ? -32.880 68.792  119.733 1.00 20.97 ? 645  LEU   A CB    1 
ATOM   4506  C  CG    . LEU   A  1 647  ? -32.947 68.177  121.130 1.00 24.47 ? 645  LEU   A CG    1 
ATOM   4507  C  CD1   . LEU   A  1 647  ? -32.208 69.069  122.131 1.00 22.65 ? 645  LEU   A CD1   1 
ATOM   4508  C  CD2   . LEU   A  1 647  ? -34.400 67.955  121.542 1.00 25.02 ? 645  LEU   A CD2   1 
ATOM   4509  N  N     . MET   A  1 648  ? -32.510 69.019  116.625 1.00 18.87 ? 646  MET   A N     1 
ATOM   4510  C  CA    . MET   A  1 648  ? -32.614 69.783  115.388 1.00 23.03 ? 646  MET   A CA    1 
ATOM   4511  C  C     . MET   A  1 648  ? -33.431 69.037  114.352 1.00 20.71 ? 646  MET   A C     1 
ATOM   4512  O  O     . MET   A  1 648  ? -34.196 69.650  113.599 1.00 21.37 ? 646  MET   A O     1 
ATOM   4513  C  CB    . MET   A  1 648  ? -31.230 70.090  114.828 1.00 19.98 ? 646  MET   A CB    1 
ATOM   4514  C  CG    . MET   A  1 648  ? -30.486 71.106  115.632 1.00 21.96 ? 646  MET   A CG    1 
ATOM   4515  S  SD    . MET   A  1 648  ? -29.191 71.863  114.623 1.00 22.03 ? 646  MET   A SD    1 
ATOM   4516  C  CE    . MET   A  1 648  ? -28.423 72.819  115.928 1.00 23.22 ? 646  MET   A CE    1 
ATOM   4517  N  N     . GLN   A  1 649  ? -33.268 67.714  114.289 1.00 20.52 ? 647  GLN   A N     1 
ATOM   4518  C  CA    . GLN   A  1 649  ? -34.034 66.930  113.328 1.00 18.65 ? 647  GLN   A CA    1 
ATOM   4519  C  C     . GLN   A  1 649  ? -35.519 67.019  113.636 1.00 21.35 ? 647  GLN   A C     1 
ATOM   4520  O  O     . GLN   A  1 649  ? -36.339 67.244  112.741 1.00 21.08 ? 647  GLN   A O     1 
ATOM   4521  C  CB    . GLN   A  1 649  ? -33.580 65.475  113.337 1.00 20.92 ? 647  GLN   A CB    1 
ATOM   4522  C  CG    . GLN   A  1 649  ? -34.302 64.634  112.278 1.00 19.39 ? 647  GLN   A CG    1 
ATOM   4523  C  CD    . GLN   A  1 649  ? -33.757 64.873  110.875 1.00 20.58 ? 647  GLN   A CD    1 
ATOM   4524  O  OE1   . GLN   A  1 649  ? -32.716 64.337  110.513 1.00 21.51 ? 647  GLN   A OE1   1 
ATOM   4525  N  NE2   . GLN   A  1 649  ? -34.465 65.680  110.081 1.00 20.92 ? 647  GLN   A NE2   1 
ATOM   4526  N  N     . ALA   A  1 650  ? -35.873 66.869  114.913 1.00 21.00 ? 648  ALA   A N     1 
ATOM   4527  C  CA    . ALA   A  1 650  ? -37.273 66.957  115.322 1.00 26.81 ? 648  ALA   A CA    1 
ATOM   4528  C  C     . ALA   A  1 650  ? -37.841 68.346  115.065 1.00 24.04 ? 648  ALA   A C     1 
ATOM   4529  O  O     . ALA   A  1 650  ? -39.012 68.491  114.698 1.00 28.13 ? 648  ALA   A O     1 
ATOM   4530  C  CB    . ALA   A  1 650  ? -37.401 66.595  116.802 1.00 21.70 ? 648  ALA   A CB    1 
ATOM   4531  N  N     . ARG   A  1 651  ? -37.028 69.377  115.251 1.00 22.13 ? 649  ARG   A N     1 
ATOM   4532  C  CA    . ARG   A  1 651  ? -37.462 70.758  115.122 1.00 23.20 ? 649  ARG   A CA    1 
ATOM   4533  C  C     . ARG   A  1 651  ? -37.296 71.306  113.710 1.00 22.48 ? 649  ARG   A C     1 
ATOM   4534  O  O     . ARG   A  1 651  ? -37.552 72.497  113.488 1.00 21.61 ? 649  ARG   A O     1 
ATOM   4535  C  CB    . ARG   A  1 651  ? -36.687 71.630  116.112 1.00 25.25 ? 649  ARG   A CB    1 
ATOM   4536  C  CG    . ARG   A  1 651  ? -37.392 72.906  116.500 1.00 33.57 ? 649  ARG   A CG    1 
ATOM   4537  C  CD    . ARG   A  1 651  ? -37.076 73.297  117.933 1.00 32.73 ? 649  ARG   A CD    1 
ATOM   4538  N  NE    . ARG   A  1 651  ? -37.486 74.669  118.202 1.00 30.33 ? 649  ARG   A NE    1 
ATOM   4539  C  CZ    . ARG   A  1 651  ? -38.735 75.051  118.424 1.00 34.07 ? 649  ARG   A CZ    1 
ATOM   4540  N  NH1   . ARG   A  1 651  ? -39.741 74.194  118.368 1.00 35.78 ? 649  ARG   A NH1   1 
ATOM   4541  N  NH2   . ARG   A  1 651  ? -38.980 76.327  118.709 1.00 36.45 ? 649  ARG   A NH2   1 
ATOM   4542  N  N     . MET   A  1 652  ? -36.893 70.472  112.752 1.00 21.56 ? 650  MET   A N     1 
ATOM   4543  C  CA    . MET   A  1 652  ? -36.558 70.974  111.421 1.00 18.80 ? 650  MET   A CA    1 
ATOM   4544  C  C     . MET   A  1 652  ? -37.638 71.858  110.815 1.00 20.77 ? 650  MET   A C     1 
ATOM   4545  O  O     . MET   A  1 652  ? -37.300 72.950  110.331 1.00 22.44 ? 650  MET   A O     1 
ATOM   4546  C  CB    . MET   A  1 652  ? -36.233 69.812  110.474 1.00 19.75 ? 650  MET   A CB    1 
ATOM   4547  C  CG    . MET   A  1 652  ? -36.054 70.271  109.033 1.00 20.91 ? 650  MET   A CG    1 
ATOM   4548  S  SD    . MET   A  1 652  ? -35.569 68.920  107.938 1.00 25.42 ? 650  MET   A SD    1 
ATOM   4549  C  CE    . MET   A  1 652  ? -33.838 68.782  108.326 1.00 21.88 ? 650  MET   A CE    1 
ATOM   4550  N  N     . PRO   A  1 653  ? -38.923 71.488  110.828 1.00 21.27 ? 651  PRO   A N     1 
ATOM   4551  C  CA    . PRO   A  1 653  ? -39.925 72.372  110.202 1.00 22.46 ? 651  PRO   A CA    1 
ATOM   4552  C  C     . PRO   A  1 653  ? -39.945 73.770  110.791 1.00 21.21 ? 651  PRO   A C     1 
ATOM   4553  O  O     . PRO   A  1 653  ? -40.002 74.754  110.044 1.00 21.99 ? 651  PRO   A O     1 
ATOM   4554  C  CB    . PRO   A  1 653  ? -41.244 71.629  110.453 1.00 23.08 ? 651  PRO   A CB    1 
ATOM   4555  C  CG    . PRO   A  1 653  ? -40.832 70.192  110.606 1.00 25.06 ? 651  PRO   A CG    1 
ATOM   4556  C  CD    . PRO   A  1 653  ? -39.544 70.262  111.366 1.00 21.32 ? 651  PRO   A CD    1 
ATOM   4557  N  N     . THR   A  1 654  ? -39.880 73.888  112.118 1.00 19.83 ? 652  THR   A N     1 
ATOM   4558  C  CA    . THR   A  1 654  ? -39.820 75.209  112.731 1.00 21.34 ? 652  THR   A CA    1 
ATOM   4559  C  C     . THR   A  1 654  ? -38.524 75.930  112.371 1.00 21.88 ? 652  THR   A C     1 
ATOM   4560  O  O     . THR   A  1 654  ? -38.541 77.125  112.048 1.00 20.30 ? 652  THR   A O     1 
ATOM   4561  C  CB    . THR   A  1 654  ? -39.964 75.084  114.241 1.00 22.94 ? 652  THR   A CB    1 
ATOM   4562  O  OG1   . THR   A  1 654  ? -41.193 74.409  114.539 1.00 21.33 ? 652  THR   A OG1   1 
ATOM   4563  C  CG2   . THR   A  1 654  ? -39.976 76.468  114.886 1.00 23.05 ? 652  THR   A CG2   1 
ATOM   4564  N  N     . LEU   A  1 655  ? -37.391 75.224  112.443 1.00 19.39 ? 653  LEU   A N     1 
ATOM   4565  C  CA    . LEU   A  1 655  ? -36.115 75.824  112.062 1.00 20.17 ? 653  LEU   A CA    1 
ATOM   4566  C  C     . LEU   A  1 655  ? -36.145 76.303  110.619 1.00 21.81 ? 653  LEU   A C     1 
ATOM   4567  O  O     . LEU   A  1 655  ? -35.601 77.372  110.308 1.00 20.36 ? 653  LEU   A O     1 
ATOM   4568  C  CB    . LEU   A  1 655  ? -34.972 74.826  112.267 1.00 17.94 ? 653  LEU   A CB    1 
ATOM   4569  C  CG    . LEU   A  1 655  ? -34.760 74.369  113.703 1.00 21.40 ? 653  LEU   A CG    1 
ATOM   4570  C  CD1   . LEU   A  1 655  ? -33.572 73.403  113.816 1.00 20.41 ? 653  LEU   A CD1   1 
ATOM   4571  C  CD2   . LEU   A  1 655  ? -34.534 75.578  114.578 1.00 23.00 ? 653  LEU   A CD2   1 
ATOM   4572  N  N     . LEU   A  1 656  ? -36.779 75.531  109.721 1.00 21.37 ? 654  LEU   A N     1 
ATOM   4573  C  CA    . LEU   A  1 656  ? -36.899 75.959  108.327 1.00 22.46 ? 654  LEU   A CA    1 
ATOM   4574  C  C     . LEU   A  1 656  ? -37.557 77.319  108.231 1.00 23.44 ? 654  LEU   A C     1 
ATOM   4575  O  O     . LEU   A  1 656  ? -37.098 78.197  107.486 1.00 22.49 ? 654  LEU   A O     1 
ATOM   4576  C  CB    . LEU   A  1 656  ? -37.726 74.964  107.511 1.00 22.93 ? 654  LEU   A CB    1 
ATOM   4577  C  CG    . LEU   A  1 656  ? -37.224 73.541  107.374 1.00 22.27 ? 654  LEU   A CG    1 
ATOM   4578  C  CD1   . LEU   A  1 656  ? -38.105 72.767  106.410 1.00 21.15 ? 654  LEU   A CD1   1 
ATOM   4579  C  CD2   . LEU   A  1 656  ? -35.811 73.560  106.907 1.00 23.40 ? 654  LEU   A CD2   1 
ATOM   4580  N  N     . GLY   A  1 657  ? -38.668 77.495  108.952 1.00 20.48 ? 655  GLY   A N     1 
ATOM   4581  C  CA    . GLY   A  1 657  ? -39.407 78.738  108.845 1.00 21.20 ? 655  GLY   A CA    1 
ATOM   4582  C  C     . GLY   A  1 657  ? -38.587 79.921  109.302 1.00 19.01 ? 655  GLY   A C     1 
ATOM   4583  O  O     . GLY   A  1 657  ? -38.687 81.013  108.740 1.00 21.24 ? 655  GLY   A O     1 
ATOM   4584  N  N     . LEU   A  1 658  ? -37.752 79.715  110.320 1.00 19.33 ? 656  LEU   A N     1 
ATOM   4585  C  CA    . LEU   A  1 658  ? -36.930 80.807  110.813 1.00 19.20 ? 656  LEU   A CA    1 
ATOM   4586  C  C     . LEU   A  1 658  ? -35.844 81.160  109.805 1.00 17.81 ? 656  LEU   A C     1 
ATOM   4587  O  O     . LEU   A  1 658  ? -35.646 82.338  109.480 1.00 19.45 ? 656  LEU   A O     1 
ATOM   4588  C  CB    . LEU   A  1 658  ? -36.332 80.427  112.166 1.00 18.63 ? 656  LEU   A CB    1 
ATOM   4589  C  CG    . LEU   A  1 658  ? -35.474 81.485  112.852 1.00 21.28 ? 656  LEU   A CG    1 
ATOM   4590  C  CD1   . LEU   A  1 658  ? -36.227 82.803  112.943 1.00 19.45 ? 656  LEU   A CD1   1 
ATOM   4591  C  CD2   . LEU   A  1 658  ? -35.074 80.983  114.247 1.00 18.56 ? 656  LEU   A CD2   1 
ATOM   4592  N  N     . ILE   A  1 659  ? -35.151 80.142  109.282 1.00 19.95 ? 657  ILE   A N     1 
ATOM   4593  C  CA    . ILE   A  1 659  ? -34.107 80.360  108.283 1.00 19.27 ? 657  ILE   A CA    1 
ATOM   4594  C  C     . ILE   A  1 659  ? -34.678 81.026  107.042 1.00 17.47 ? 657  ILE   A C     1 
ATOM   4595  O  O     . ILE   A  1 659  ? -34.058 81.923  106.462 1.00 18.28 ? 657  ILE   A O     1 
ATOM   4596  C  CB    . ILE   A  1 659  ? -33.421 79.027  107.934 1.00 16.89 ? 657  ILE   A CB    1 
ATOM   4597  C  CG1   . ILE   A  1 659  ? -32.741 78.471  109.194 1.00 19.13 ? 657  ILE   A CG1   1 
ATOM   4598  C  CG2   . ILE   A  1 659  ? -32.437 79.228  106.788 1.00 18.99 ? 657  ILE   A CG2   1 
ATOM   4599  C  CD1   . ILE   A  1 659  ? -32.199 77.082  109.052 1.00 21.93 ? 657  ILE   A CD1   1 
ATOM   4600  N  N     . ILE   A  1 660  ? -35.857 80.584  106.601 1.00 17.50 ? 658  ILE   A N     1 
ATOM   4601  C  CA    . ILE   A  1 660  ? -36.488 81.181  105.427 1.00 16.97 ? 658  ILE   A CA    1 
ATOM   4602  C  C     . ILE   A  1 660  ? -36.704 82.674  105.641 1.00 18.84 ? 658  ILE   A C     1 
ATOM   4603  O  O     . ILE   A  1 660  ? -36.401 83.500  104.769 1.00 20.38 ? 658  ILE   A O     1 
ATOM   4604  C  CB    . ILE   A  1 660  ? -37.817 80.464  105.116 1.00 17.60 ? 658  ILE   A CB    1 
ATOM   4605  C  CG1   . ILE   A  1 660  ? -37.567 79.076  104.520 1.00 18.60 ? 658  ILE   A CG1   1 
ATOM   4606  C  CG2   . ILE   A  1 660  ? -38.671 81.330  104.188 1.00 19.18 ? 658  ILE   A CG2   1 
ATOM   4607  C  CD1   . ILE   A  1 660  ? -38.803 78.204  104.493 1.00 23.13 ? 658  ILE   A CD1   1 
ATOM   4608  N  N     . ARG   A  1 661  ? -37.241 83.044  106.806 1.00 17.55 ? 659  ARG   A N     1 
ATOM   4609  C  CA    . ARG   A  1 661  ? -37.612 84.440  107.007 1.00 20.51 ? 659  ARG   A CA    1 
ATOM   4610  C  C     . ARG   A  1 661  ? -36.443 85.291  107.481 1.00 22.29 ? 659  ARG   A C     1 
ATOM   4611  O  O     . ARG   A  1 661  ? -36.348 86.457  107.090 1.00 20.86 ? 659  ARG   A O     1 
ATOM   4612  C  CB    . ARG   A  1 661  ? -38.788 84.546  107.986 1.00 20.33 ? 659  ARG   A CB    1 
ATOM   4613  C  CG    . ARG   A  1 661  ? -40.109 84.147  107.341 1.00 22.01 ? 659  ARG   A CG    1 
ATOM   4614  C  CD    . ARG   A  1 661  ? -41.289 84.176  108.310 1.00 20.46 ? 659  ARG   A CD    1 
ATOM   4615  N  NE    . ARG   A  1 661  ? -41.498 85.466  108.967 1.00 23.12 ? 659  ARG   A NE    1 
ATOM   4616  C  CZ    . ARG   A  1 661  ? -41.404 85.663  110.275 1.00 22.69 ? 659  ARG   A CZ    1 
ATOM   4617  N  NH1   . ARG   A  1 661  ? -41.063 84.683  111.101 1.00 24.66 ? 659  ARG   A NH1   1 
ATOM   4618  N  NH2   . ARG   A  1 661  ? -41.667 86.872  110.774 1.00 21.51 ? 659  ARG   A NH2   1 
ATOM   4619  N  N     . GLU   A  1 662  ? -35.547 84.739  108.317 1.00 17.96 ? 660  GLU   A N     1 
ATOM   4620  C  CA    . GLU   A  1 662  ? -34.448 85.544  108.848 1.00 19.64 ? 660  GLU   A CA    1 
ATOM   4621  C  C     . GLU   A  1 662  ? -33.316 85.678  107.840 1.00 17.89 ? 660  GLU   A C     1 
ATOM   4622  O  O     . GLU   A  1 662  ? -32.719 86.749  107.708 1.00 18.38 ? 660  GLU   A O     1 
ATOM   4623  C  CB    . GLU   A  1 662  ? -33.899 84.945  110.152 1.00 21.31 ? 660  GLU   A CB    1 
ATOM   4624  C  CG    . GLU   A  1 662  ? -32.723 85.754  110.693 1.00 21.91 ? 660  GLU   A CG    1 
ATOM   4625  C  CD    . GLU   A  1 662  ? -32.171 85.235  112.010 1.00 22.21 ? 660  GLU   A CD    1 
ATOM   4626  O  OE1   . GLU   A  1 662  ? -32.134 84.006  112.216 1.00 22.47 ? 660  GLU   A OE1   1 
ATOM   4627  O  OE2   . GLU   A  1 662  ? -31.760 86.068  112.840 1.00 22.39 ? 660  GLU   A OE2   1 
ATOM   4628  N  N     . ALA   A  1 663  ? -33.020 84.613  107.107 1.00 18.94 ? 661  ALA   A N     1 
ATOM   4629  C  CA    . ALA   A  1 663  ? -31.873 84.607  106.218 1.00 19.53 ? 661  ALA   A CA    1 
ATOM   4630  C  C     . ALA   A  1 663  ? -32.262 84.740  104.753 1.00 20.77 ? 661  ALA   A C     1 
ATOM   4631  O  O     . ALA   A  1 663  ? -31.376 84.820  103.898 1.00 21.40 ? 661  ALA   A O     1 
ATOM   4632  C  CB    . ALA   A  1 663  ? -31.054 83.332  106.438 1.00 18.72 ? 661  ALA   A CB    1 
ATOM   4633  N  N     . GLY   A  1 664  ? -33.556 84.772  104.439 1.00 19.55 ? 662  GLY   A N     1 
ATOM   4634  C  CA    . GLY   A  1 664  ? -33.988 84.935  103.063 1.00 20.21 ? 662  GLY   A CA    1 
ATOM   4635  C  C     . GLY   A  1 664  ? -33.785 83.718  102.191 1.00 19.22 ? 662  GLY   A C     1 
ATOM   4636  O  O     . GLY   A  1 664  ? -33.652 83.853  100.975 1.00 21.67 ? 662  GLY   A O     1 
ATOM   4637  N  N     . LYS   A  1 665  ? -33.760 82.529  102.782 1.00 21.78 ? 663  LYS   A N     1 
ATOM   4638  C  CA    . LYS   A  1 665  ? -33.482 81.303  102.053 1.00 19.94 ? 663  LYS   A CA    1 
ATOM   4639  C  C     . LYS   A  1 665  ? -34.770 80.651  101.569 1.00 19.73 ? 663  LYS   A C     1 
ATOM   4640  O  O     . LYS   A  1 665  ? -35.830 80.823  102.165 1.00 16.99 ? 663  LYS   A O     1 
ATOM   4641  C  CB    . LYS   A  1 665  ? -32.730 80.327  102.948 1.00 20.11 ? 663  LYS   A CB    1 
ATOM   4642  C  CG    . LYS   A  1 665  ? -31.378 80.841  103.379 1.00 20.97 ? 663  LYS   A CG    1 
ATOM   4643  C  CD    . LYS   A  1 665  ? -30.491 79.664  103.732 1.00 29.84 ? 663  LYS   A CD    1 
ATOM   4644  C  CE    . LYS   A  1 665  ? -29.042 80.038  103.634 1.00 29.32 ? 663  LYS   A CE    1 
ATOM   4645  N  NZ    . LYS   A  1 665  ? -28.152 78.844  103.845 1.00 27.55 ? 663  LYS   A NZ    1 
ATOM   4646  N  N     . SER   A  1 666  ? -34.660 79.882  100.491 1.00 20.83 ? 664  SER   A N     1 
ATOM   4647  C  CA    . SER   A  1 666  ? -35.786 79.076  100.043 1.00 18.60 ? 664  SER   A CA    1 
ATOM   4648  C  C     . SER   A  1 666  ? -35.961 77.859  100.952 1.00 22.01 ? 664  SER   A C     1 
ATOM   4649  O  O     . SER   A  1 666  ? -35.068 77.491  101.727 1.00 19.53 ? 664  SER   A O     1 
ATOM   4650  C  CB    . SER   A  1 666  ? -35.577 78.621  98.597  1.00 21.92 ? 664  SER   A CB    1 
ATOM   4651  O  OG    . SER   A  1 666  ? -34.516 77.675  98.535  1.00 23.62 ? 664  SER   A OG    1 
ATOM   4652  N  N     . ALA   A  1 667  ? -37.131 77.226  100.849 1.00 17.91 ? 665  ALA   A N     1 
ATOM   4653  C  CA    . ALA   A  1 667  ? -37.405 76.055  101.678 1.00 20.57 ? 665  ALA   A CA    1 
ATOM   4654  C  C     . ALA   A  1 667  ? -36.371 74.962  101.443 1.00 21.23 ? 665  ALA   A C     1 
ATOM   4655  O  O     . ALA   A  1 667  ? -35.834 74.388  102.398 1.00 17.08 ? 665  ALA   A O     1 
ATOM   4656  C  CB    . ALA   A  1 667  ? -38.814 75.530  101.407 1.00 21.43 ? 665  ALA   A CB    1 
ATOM   4657  N  N     . LEU   A  1 668  ? -36.072 74.665  100.174 1.00 17.17 ? 666  LEU   A N     1 
ATOM   4658  C  CA    . LEU   A  1 668  ? -35.113 73.605  99.875  1.00 18.94 ? 666  LEU   A CA    1 
ATOM   4659  C  C     . LEU   A  1 668  ? -33.749 73.908  100.475 1.00 21.21 ? 666  LEU   A C     1 
ATOM   4660  O  O     . LEU   A  1 668  ? -33.096 73.018  101.032 1.00 19.74 ? 666  LEU   A O     1 
ATOM   4661  C  CB    . LEU   A  1 668  ? -34.985 73.412  98.364  1.00 24.50 ? 666  LEU   A CB    1 
ATOM   4662  C  CG    . LEU   A  1 668  ? -35.660 72.162  97.815  1.00 33.05 ? 666  LEU   A CG    1 
ATOM   4663  C  CD1   . LEU   A  1 668  ? -35.732 72.234  96.292  1.00 36.08 ? 666  LEU   A CD1   1 
ATOM   4664  C  CD2   . LEU   A  1 668  ? -34.886 70.935  98.272  1.00 31.96 ? 666  LEU   A CD2   1 
ATOM   4665  N  N     . ASN   A  1 669  ? -33.306 75.163  100.381 1.00 19.50 ? 667  ASN   A N     1 
ATOM   4666  C  CA    . ASN   A  1 669  ? -32.008 75.508  100.940 1.00 21.02 ? 667  ASN   A CA    1 
ATOM   4667  C  C     . ASN   A  1 669  ? -32.031 75.487  102.457 1.00 18.61 ? 667  ASN   A C     1 
ATOM   4668  O  O     . ASN   A  1 669  ? -31.012 75.169  103.080 1.00 19.09 ? 667  ASN   A O     1 
ATOM   4669  C  CB    . ASN   A  1 669  ? -31.556 76.870  100.435 1.00 20.21 ? 667  ASN   A CB    1 
ATOM   4670  C  CG    . ASN   A  1 669  ? -31.216 76.841  98.957  1.00 28.44 ? 667  ASN   A CG    1 
ATOM   4671  O  OD1   . ASN   A  1 669  ? -31.595 77.732  98.207  1.00 28.65 ? 667  ASN   A OD1   1 
ATOM   4672  N  ND2   . ASN   A  1 669  ? -30.517 75.794  98.531  1.00 28.67 ? 667  ASN   A ND2   1 
ATOM   4673  N  N     . ALA   A  1 670  ? -33.174 75.826  103.062 1.00 16.96 ? 668  ALA   A N     1 
ATOM   4674  C  CA    . ALA   A  1 670  ? -33.287 75.737  104.511 1.00 17.93 ? 668  ALA   A CA    1 
ATOM   4675  C  C     . ALA   A  1 670  ? -33.236 74.287  104.974 1.00 20.14 ? 668  ALA   A C     1 
ATOM   4676  O  O     . ALA   A  1 670  ? -32.606 73.979  105.994 1.00 19.04 ? 668  ALA   A O     1 
ATOM   4677  C  CB    . ALA   A  1 670  ? -34.566 76.427  104.984 1.00 22.92 ? 668  ALA   A CB    1 
ATOM   4678  N  N     . ILE   A  1 671  ? -33.899 73.379  104.245 1.00 18.59 ? 669  ILE   A N     1 
ATOM   4679  C  CA    . ILE   A  1 671  ? -33.781 71.958  104.565 1.00 18.12 ? 669  ILE   A CA    1 
ATOM   4680  C  C     . ILE   A  1 671  ? -32.322 71.534  104.530 1.00 19.00 ? 669  ILE   A C     1 
ATOM   4681  O  O     . ILE   A  1 671  ? -31.822 70.870  105.450 1.00 18.71 ? 669  ILE   A O     1 
ATOM   4682  C  CB    . ILE   A  1 671  ? -34.625 71.110  103.598 1.00 19.13 ? 669  ILE   A CB    1 
ATOM   4683  C  CG1   . ILE   A  1 671  ? -36.113 71.385  103.831 1.00 19.75 ? 669  ILE   A CG1   1 
ATOM   4684  C  CG2   . ILE   A  1 671  ? -34.312 69.625  103.798 1.00 16.76 ? 669  ILE   A CG2   1 
ATOM   4685  C  CD1   . ILE   A  1 671  ? -37.003 70.869  102.725 1.00 20.31 ? 669  ILE   A CD1   1 
ATOM   4686  N  N     . ALA   A  1 672  ? -31.624 71.903  103.456 1.00 18.35 ? 670  ALA   A N     1 
ATOM   4687  C  CA    . ALA   A  1 672  ? -30.229 71.520  103.314 1.00 18.69 ? 670  ALA   A CA    1 
ATOM   4688  C  C     . ALA   A  1 672  ? -29.407 72.072  104.463 1.00 17.45 ? 670  ALA   A C     1 
ATOM   4689  O  O     . ALA   A  1 672  ? -28.477 71.422  104.943 1.00 18.16 ? 670  ALA   A O     1 
ATOM   4690  C  CB    . ALA   A  1 672  ? -29.678 72.022  101.977 1.00 21.18 ? 670  ALA   A CB    1 
ATOM   4691  N  N     . GLU   A  1 673  ? -29.735 73.282  104.903 1.00 18.89 ? 671  GLU   A N     1 
ATOM   4692  C  CA    . GLU   A  1 673  ? -28.979 73.904  105.972 1.00 19.03 ? 671  GLU   A CA    1 
ATOM   4693  C  C     . GLU   A  1 673  ? -29.217 73.202  107.301 1.00 20.42 ? 671  GLU   A C     1 
ATOM   4694  O  O     . GLU   A  1 673  ? -28.269 72.962  108.060 1.00 18.08 ? 671  GLU   A O     1 
ATOM   4695  C  CB    . GLU   A  1 673  ? -29.350 75.375  106.073 1.00 18.26 ? 671  GLU   A CB    1 
ATOM   4696  C  CG    . GLU   A  1 673  ? -28.850 75.978  107.363 1.00 24.40 ? 671  GLU   A CG    1 
ATOM   4697  C  CD    . GLU   A  1 673  ? -28.198 77.310  107.136 1.00 26.88 ? 671  GLU   A CD    1 
ATOM   4698  O  OE1   . GLU   A  1 673  ? -28.683 78.035  106.241 1.00 29.97 ? 671  GLU   A OE1   1 
ATOM   4699  O  OE2   . GLU   A  1 673  ? -27.215 77.624  107.848 1.00 22.61 ? 671  GLU   A OE2   1 
ATOM   4700  N  N     . VAL   A  1 674  ? -30.473 72.881  107.623 1.00 17.09 ? 672  VAL   A N     1 
ATOM   4701  C  CA    . VAL   A  1 674  ? -30.705 72.136  108.857 1.00 17.53 ? 672  VAL   A CA    1 
ATOM   4702  C  C     . VAL   A  1 674  ? -30.056 70.762  108.767 1.00 17.56 ? 672  VAL   A C     1 
ATOM   4703  O  O     . VAL   A  1 674  ? -29.460 70.279  109.736 1.00 16.36 ? 672  VAL   A O     1 
ATOM   4704  C  CB    . VAL   A  1 674  ? -32.208 72.033  109.179 1.00 18.01 ? 672  VAL   A CB    1 
ATOM   4705  C  CG1   . VAL   A  1 674  ? -32.410 71.226  110.471 1.00 16.71 ? 672  VAL   A CG1   1 
ATOM   4706  C  CG2   . VAL   A  1 674  ? -32.815 73.432  109.329 1.00 18.06 ? 672  VAL   A CG2   1 
ATOM   4707  N  N     . ARG   A  1 675  ? -30.171 70.106  107.608 1.00 16.03 ? 673  ARG   A N     1 
ATOM   4708  C  CA    . ARG   A  1 675  ? -29.518 68.811  107.440 1.00 17.06 ? 673  ARG   A CA    1 
ATOM   4709  C  C     . ARG   A  1 675  ? -28.018 68.917  107.662 1.00 16.88 ? 673  ARG   A C     1 
ATOM   4710  O  O     . ARG   A  1 675  ? -27.417 68.039  108.287 1.00 16.99 ? 673  ARG   A O     1 
ATOM   4711  C  CB    . ARG   A  1 675  ? -29.794 68.254  106.048 1.00 16.38 ? 673  ARG   A CB    1 
ATOM   4712  C  CG    . ARG   A  1 675  ? -31.207 67.719  105.900 1.00 15.76 ? 673  ARG   A CG    1 
ATOM   4713  C  CD    . ARG   A  1 675  ? -31.338 66.932  104.620 1.00 18.59 ? 673  ARG   A CD    1 
ATOM   4714  N  NE    . ARG   A  1 675  ? -30.551 65.708  104.690 1.00 20.42 ? 673  ARG   A NE    1 
ATOM   4715  C  CZ    . ARG   A  1 675  ? -30.164 65.012  103.629 1.00 20.86 ? 673  ARG   A CZ    1 
ATOM   4716  N  NH1   . ARG   A  1 675  ? -30.464 65.408  102.398 1.00 18.33 ? 673  ARG   A NH1   1 
ATOM   4717  N  NH2   . ARG   A  1 675  ? -29.463 63.894  103.807 1.00 18.10 ? 673  ARG   A NH2   1 
ATOM   4718  N  N     . GLU   A  1 676  ? -27.399 69.976  107.139 1.00 18.32 ? 674  GLU   A N     1 
ATOM   4719  C  CA    . GLU   A  1 676  ? -25.957 70.138  107.285 1.00 15.96 ? 674  GLU   A CA    1 
ATOM   4720  C  C     . GLU   A  1 676  ? -25.572 70.328  108.745 1.00 16.03 ? 674  GLU   A C     1 
ATOM   4721  O  O     . GLU   A  1 676  ? -24.579 69.762  109.217 1.00 16.08 ? 674  GLU   A O     1 
ATOM   4722  C  CB    . GLU   A  1 676  ? -25.472 71.326  106.449 1.00 15.70 ? 674  GLU   A CB    1 
ATOM   4723  C  CG    . GLU   A  1 676  ? -23.937 71.434  106.430 1.00 22.48 ? 674  GLU   A CG    1 
ATOM   4724  C  CD    . GLU   A  1 676  ? -23.419 72.585  105.573 1.00 28.85 ? 674  GLU   A CD    1 
ATOM   4725  O  OE1   . GLU   A  1 676  ? -24.236 73.360  105.037 1.00 35.16 ? 674  GLU   A OE1   1 
ATOM   4726  O  OE2   . GLU   A  1 676  ? -22.188 72.721  105.438 1.00 39.50 ? 674  GLU   A OE2   1 
ATOM   4727  N  N     . ALA   A  1 677  ? -26.363 71.110  109.483 1.00 16.21 ? 675  ALA   A N     1 
ATOM   4728  C  CA    . ALA   A  1 677  ? -26.103 71.286  110.906 1.00 16.47 ? 675  ALA   A CA    1 
ATOM   4729  C  C     . ALA   A  1 677  ? -26.207 69.958  111.646 1.00 17.45 ? 675  ALA   A C     1 
ATOM   4730  O  O     . ALA   A  1 677  ? -25.359 69.637  112.486 1.00 16.71 ? 675  ALA   A O     1 
ATOM   4731  C  CB    . ALA   A  1 677  ? -27.077 72.316  111.490 1.00 16.67 ? 675  ALA   A CB    1 
ATOM   4732  N  N     . ILE   A  1 678  ? -27.238 69.168  111.336 1.00 17.97 ? 676  ILE   A N     1 
ATOM   4733  C  CA    . ILE   A  1 678  ? -27.378 67.836  111.920 1.00 16.72 ? 676  ILE   A CA    1 
ATOM   4734  C  C     . ILE   A  1 678  ? -26.170 66.975  111.579 1.00 17.40 ? 676  ILE   A C     1 
ATOM   4735  O  O     . ILE   A  1 678  ? -25.635 66.255  112.432 1.00 16.78 ? 676  ILE   A O     1 
ATOM   4736  C  CB    . ILE   A  1 678  ? -28.681 67.179  111.425 1.00 16.89 ? 676  ILE   A CB    1 
ATOM   4737  C  CG1   . ILE   A  1 678  ? -29.905 67.907  111.997 1.00 18.69 ? 676  ILE   A CG1   1 
ATOM   4738  C  CG2   . ILE   A  1 678  ? -28.708 65.677  111.761 1.00 17.00 ? 676  ILE   A CG2   1 
ATOM   4739  C  CD1   . ILE   A  1 678  ? -31.190 67.568  111.246 1.00 18.54 ? 676  ILE   A CD1   1 
ATOM   4740  N  N     . ASP   A  1 679  ? -25.766 66.997  110.306 1.00 16.30 ? 677  ASP   A N     1 
ATOM   4741  C  CA    . ASP   A  1 679  ? -24.623 66.204  109.857 1.00 17.29 ? 677  ASP   A CA    1 
ATOM   4742  C  C     . ASP   A  1 679  ? -23.339 66.621  110.567 1.00 16.82 ? 677  ASP   A C     1 
ATOM   4743  O  O     . ASP   A  1 679  ? -22.545 65.765  110.971 1.00 16.37 ? 677  ASP   A O     1 
ATOM   4744  C  CB    . ASP   A  1 679  ? -24.444 66.341  108.341 1.00 15.93 ? 677  ASP   A CB    1 
ATOM   4745  C  CG    . ASP   A  1 679  ? -25.618 65.766  107.541 1.00 20.69 ? 677  ASP   A CG    1 
ATOM   4746  O  OD1   . ASP   A  1 679  ? -26.308 64.851  108.035 1.00 19.42 ? 677  ASP   A OD1   1 
ATOM   4747  O  OD2   . ASP   A  1 679  ? -25.824 66.222  106.399 1.00 23.37 ? 677  ASP   A OD2   1 
ATOM   4748  N  N     . PHE   A  1 680  ? -23.095 67.929  110.698 1.00 16.31 ? 678  PHE   A N     1 
ATOM   4749  C  CA    . PHE   A  1 680  ? -21.925 68.389  111.451 1.00 16.90 ? 678  PHE   A CA    1 
ATOM   4750  C  C     . PHE   A  1 680  ? -21.921 67.814  112.859 1.00 16.69 ? 678  PHE   A C     1 
ATOM   4751  O  O     . PHE   A  1 680  ? -20.916 67.261  113.319 1.00 16.87 ? 678  PHE   A O     1 
ATOM   4752  C  CB    . PHE   A  1 680  ? -21.901 69.915  111.540 1.00 18.53 ? 678  PHE   A CB    1 
ATOM   4753  C  CG    . PHE   A  1 680  ? -21.264 70.596  110.374 1.00 16.26 ? 678  PHE   A CG    1 
ATOM   4754  C  CD1   . PHE   A  1 680  ? -20.030 70.189  109.891 1.00 16.16 ? 678  PHE   A CD1   1 
ATOM   4755  C  CD2   . PHE   A  1 680  ? -21.894 71.686  109.787 1.00 16.23 ? 678  PHE   A CD2   1 
ATOM   4756  C  CE1   . PHE   A  1 680  ? -19.437 70.846  108.826 1.00 19.07 ? 678  PHE   A CE1   1 
ATOM   4757  C  CE2   . PHE   A  1 680  ? -21.317 72.354  108.716 1.00 19.46 ? 678  PHE   A CE2   1 
ATOM   4758  C  CZ    . PHE   A  1 680  ? -20.079 71.934  108.228 1.00 17.95 ? 678  PHE   A CZ    1 
ATOM   4759  N  N     . LEU   A  1 681  ? -23.039 67.977  113.567 1.00 16.86 ? 679  LEU   A N     1 
ATOM   4760  C  CA    . LEU   A  1 681  ? -23.160 67.487  114.936 1.00 17.15 ? 679  LEU   A CA    1 
ATOM   4761  C  C     . LEU   A  1 681  ? -22.836 66.004  115.018 1.00 18.66 ? 679  LEU   A C     1 
ATOM   4762  O  O     . LEU   A  1 681  ? -22.017 65.574  115.841 1.00 17.49 ? 679  LEU   A O     1 
ATOM   4763  C  CB    . LEU   A  1 681  ? -24.577 67.754  115.447 1.00 17.31 ? 679  LEU   A CB    1 
ATOM   4764  C  CG    . LEU   A  1 681  ? -24.932 69.211  115.747 1.00 17.40 ? 679  LEU   A CG    1 
ATOM   4765  C  CD1   . LEU   A  1 681  ? -26.454 69.372  115.867 1.00 17.49 ? 679  LEU   A CD1   1 
ATOM   4766  C  CD2   . LEU   A  1 681  ? -24.255 69.645  117.036 1.00 18.86 ? 679  LEU   A CD2   1 
ATOM   4767  N  N     . ARG   A  1 682  ? -23.476 65.200  114.169 1.00 17.05 ? 680  ARG   A N     1 
ATOM   4768  C  CA    . ARG   A  1 682  ? -23.228 63.763  114.211 1.00 17.11 ? 680  ARG   A CA    1 
ATOM   4769  C  C     . ARG   A  1 682  ? -21.841 63.398  113.708 1.00 16.99 ? 680  ARG   A C     1 
ATOM   4770  O  O     . ARG   A  1 682  ? -21.242 62.436  114.205 1.00 17.47 ? 680  ARG   A O     1 
ATOM   4771  C  CB    . ARG   A  1 682  ? -24.287 63.028  113.397 1.00 17.00 ? 680  ARG   A CB    1 
ATOM   4772  C  CG    . ARG   A  1 682  ? -25.645 63.097  114.065 1.00 17.52 ? 680  ARG   A CG    1 
ATOM   4773  C  CD    . ARG   A  1 682  ? -26.716 62.563  113.156 1.00 19.35 ? 680  ARG   A CD    1 
ATOM   4774  N  NE    . ARG   A  1 682  ? -28.004 62.487  113.839 1.00 19.64 ? 680  ARG   A NE    1 
ATOM   4775  C  CZ    . ARG   A  1 682  ? -29.155 62.257  113.224 1.00 19.52 ? 680  ARG   A CZ    1 
ATOM   4776  N  NH1   . ARG   A  1 682  ? -29.210 62.042  111.919 1.00 16.98 ? 680  ARG   A NH1   1 
ATOM   4777  N  NH2   . ARG   A  1 682  ? -30.280 62.261  113.935 1.00 20.50 ? 680  ARG   A NH2   1 
ATOM   4778  N  N     . TYR   A  1 683  ? -21.320 64.132  112.726 1.00 16.74 ? 681  TYR   A N     1 
ATOM   4779  C  CA    . TYR   A  1 683  ? -20.000 63.798  112.197 1.00 16.70 ? 681  TYR   A CA    1 
ATOM   4780  C  C     . TYR   A  1 683  ? -18.912 64.079  113.222 1.00 18.22 ? 681  TYR   A C     1 
ATOM   4781  O  O     . TYR   A  1 683  ? -18.042 63.235  113.461 1.00 16.92 ? 681  TYR   A O     1 
ATOM   4782  C  CB    . TYR   A  1 683  ? -19.730 64.580  110.919 1.00 17.36 ? 681  TYR   A CB    1 
ATOM   4783  C  CG    . TYR   A  1 683  ? -18.359 64.342  110.341 1.00 19.05 ? 681  TYR   A CG    1 
ATOM   4784  C  CD1   . TYR   A  1 683  ? -18.089 63.208  109.587 1.00 19.01 ? 681  TYR   A CD1   1 
ATOM   4785  C  CD2   . TYR   A  1 683  ? -17.328 65.259  110.554 1.00 18.52 ? 681  TYR   A CD2   1 
ATOM   4786  C  CE1   . TYR   A  1 683  ? -16.815 62.986  109.050 1.00 18.83 ? 681  TYR   A CE1   1 
ATOM   4787  C  CE2   . TYR   A  1 683  ? -16.068 65.048  110.023 1.00 17.97 ? 681  TYR   A CE2   1 
ATOM   4788  C  CZ    . TYR   A  1 683  ? -15.818 63.914  109.278 1.00 18.04 ? 681  TYR   A CZ    1 
ATOM   4789  O  OH    . TYR   A  1 683  ? -14.553 63.708  108.763 1.00 18.19 ? 681  TYR   A OH    1 
ATOM   4790  N  N     . TYR   A  1 684  ? -18.931 65.275  113.821 1.00 17.96 ? 682  TYR   A N     1 
ATOM   4791  C  CA    . TYR   A  1 684  ? -17.917 65.594  114.821 1.00 18.05 ? 682  TYR   A CA    1 
ATOM   4792  C  C     . TYR   A  1 684  ? -18.085 64.738  116.072 1.00 20.06 ? 682  TYR   A C     1 
ATOM   4793  O  O     . TYR   A  1 684  ? -17.092 64.409  116.736 1.00 18.24 ? 682  TYR   A O     1 
ATOM   4794  C  CB    . TYR   A  1 684  ? -17.954 67.092  115.166 1.00 17.16 ? 682  TYR   A CB    1 
ATOM   4795  C  CG    . TYR   A  1 684  ? -17.584 68.000  114.001 1.00 17.75 ? 682  TYR   A CG    1 
ATOM   4796  C  CD1   . TYR   A  1 684  ? -16.518 67.695  113.151 1.00 17.68 ? 682  TYR   A CD1   1 
ATOM   4797  C  CD2   . TYR   A  1 684  ? -18.294 69.163  113.762 1.00 17.10 ? 682  TYR   A CD2   1 
ATOM   4798  C  CE1   . TYR   A  1 684  ? -16.184 68.535  112.076 1.00 16.94 ? 682  TYR   A CE1   1 
ATOM   4799  C  CE2   . TYR   A  1 684  ? -17.978 69.994  112.710 1.00 16.67 ? 682  TYR   A CE2   1 
ATOM   4800  C  CZ    . TYR   A  1 684  ? -16.918 69.677  111.865 1.00 17.68 ? 682  TYR   A CZ    1 
ATOM   4801  O  OH    . TYR   A  1 684  ? -16.610 70.521  110.822 1.00 18.04 ? 682  TYR   A OH    1 
ATOM   4802  N  N     . ALA   A  1 685  ? -19.317 64.328  116.391 1.00 17.49 ? 683  ALA   A N     1 
ATOM   4803  C  CA    . ALA   A  1 685  ? -19.492 63.380  117.488 1.00 17.79 ? 683  ALA   A CA    1 
ATOM   4804  C  C     . ALA   A  1 685  ? -18.787 62.071  117.177 1.00 21.07 ? 683  ALA   A C     1 
ATOM   4805  O  O     . ALA   A  1 685  ? -18.051 61.534  118.010 1.00 18.02 ? 683  ALA   A O     1 
ATOM   4806  C  CB    . ALA   A  1 685  ? -20.974 63.125  117.759 1.00 17.90 ? 683  ALA   A CB    1 
ATOM   4807  N  N     . GLU   A  1 686  ? -19.004 61.540  115.971 1.00 17.56 ? 684  GLU   A N     1 
ATOM   4808  C  CA    . GLU   A  1 686  ? -18.368 60.275  115.612 1.00 21.23 ? 684  GLU   A CA    1 
ATOM   4809  C  C     . GLU   A  1 686  ? -16.854 60.425  115.556 1.00 18.27 ? 684  GLU   A C     1 
ATOM   4810  O  O     . GLU   A  1 686  ? -16.122 59.563  116.055 1.00 18.06 ? 684  GLU   A O     1 
ATOM   4811  C  CB    . GLU   A  1 686  ? -18.908 59.759  114.275 1.00 21.10 ? 684  GLU   A CB    1 
ATOM   4812  C  CG    . GLU   A  1 686  ? -18.173 58.532  113.720 1.00 22.44 ? 684  GLU   A CG    1 
ATOM   4813  C  CD    . GLU   A  1 686  ? -18.279 57.277  114.608 1.00 25.05 ? 684  GLU   A CD    1 
ATOM   4814  O  OE1   . GLU   A  1 686  ? -19.068 57.254  115.580 1.00 25.07 ? 684  GLU   A OE1   1 
ATOM   4815  O  OE2   . GLU   A  1 686  ? -17.564 56.293  114.325 1.00 28.84 ? 684  GLU   A OE2   1 
ATOM   4816  N  N     . GLN   A  1 687  ? -16.370 61.516  114.959 1.00 18.69 ? 685  GLN   A N     1 
ATOM   4817  C  CA    . GLN   A  1 687  ? -14.926 61.729  114.877 1.00 19.02 ? 685  GLN   A CA    1 
ATOM   4818  C  C     . GLN   A  1 687  ? -14.311 61.811  116.266 1.00 17.63 ? 685  GLN   A C     1 
ATOM   4819  O  O     . GLN   A  1 687  ? -13.197 61.323  116.489 1.00 19.07 ? 685  GLN   A O     1 
ATOM   4820  C  CB    . GLN   A  1 687  ? -14.618 62.994  114.076 1.00 17.30 ? 685  GLN   A CB    1 
ATOM   4821  C  CG    . GLN   A  1 687  ? -14.961 62.847  112.586 1.00 16.83 ? 685  GLN   A CG    1 
ATOM   4822  C  CD    . GLN   A  1 687  ? -14.228 61.678  111.958 1.00 22.07 ? 685  GLN   A CD    1 
ATOM   4823  O  OE1   . GLN   A  1 687  ? -13.001 61.609  112.006 1.00 20.06 ? 685  GLN   A OE1   1 
ATOM   4824  N  NE2   . GLN   A  1 687  ? -14.979 60.737  111.393 1.00 23.25 ? 685  GLN   A NE2   1 
ATOM   4825  N  N     . THR   A  1 688  ? -15.028 62.419  117.212 1.00 18.01 ? 686  THR   A N     1 
ATOM   4826  C  CA    . THR   A  1 688  ? -14.572 62.430  118.597 1.00 19.11 ? 686  THR   A CA    1 
ATOM   4827  C  C     . THR   A  1 688  ? -14.488 61.017  119.156 1.00 18.89 ? 686  THR   A C     1 
ATOM   4828  O  O     . THR   A  1 688  ? -13.491 60.641  119.781 1.00 19.99 ? 686  THR   A O     1 
ATOM   4829  C  CB    . THR   A  1 688  ? -15.513 63.286  119.449 1.00 19.77 ? 686  THR   A CB    1 
ATOM   4830  O  OG1   . THR   A  1 688  ? -15.434 64.646  119.009 1.00 18.61 ? 686  THR   A OG1   1 
ATOM   4831  C  CG2   . THR   A  1 688  ? -15.120 63.204  120.926 1.00 18.63 ? 686  THR   A CG2   1 
ATOM   4832  N  N     . ARG   A  1 689  ? -15.541 60.223  118.960 1.00 19.35 ? 687  ARG   A N     1 
ATOM   4833  C  CA    . ARG   A  1 689  ? -15.527 58.858  119.476 1.00 19.99 ? 687  ARG   A CA    1 
ATOM   4834  C  C     . ARG   A  1 689  ? -14.407 58.046  118.851 1.00 22.61 ? 687  ARG   A C     1 
ATOM   4835  O  O     . ARG   A  1 689  ? -13.886 57.115  119.475 1.00 21.99 ? 687  ARG   A O     1 
ATOM   4836  C  CB    . ARG   A  1 689  ? -16.879 58.176  119.224 1.00 21.33 ? 687  ARG   A CB    1 
ATOM   4837  C  CG    . ARG   A  1 689  ? -18.017 58.666  120.132 1.00 24.32 ? 687  ARG   A CG    1 
ATOM   4838  C  CD    . ARG   A  1 689  ? -19.267 57.818  119.922 1.00 21.03 ? 687  ARG   A CD    1 
ATOM   4839  N  NE    . ARG   A  1 689  ? -19.793 57.950  118.566 1.00 22.68 ? 687  ARG   A NE    1 
ATOM   4840  C  CZ    . ARG   A  1 689  ? -20.758 58.792  118.216 1.00 25.65 ? 687  ARG   A CZ    1 
ATOM   4841  N  NH1   . ARG   A  1 689  ? -21.322 59.599  119.097 1.00 24.94 ? 687  ARG   A NH1   1 
ATOM   4842  N  NH2   . ARG   A  1 689  ? -21.174 58.816  116.953 1.00 22.67 ? 687  ARG   A NH2   1 
ATOM   4843  N  N     . ARG   A  1 690  ? -14.019 58.390  117.627 1.00 19.62 ? 688  ARG   A N     1 
ATOM   4844  C  CA    . ARG   A  1 690  ? -12.919 57.703  116.967 1.00 20.17 ? 688  ARG   A CA    1 
ATOM   4845  C  C     . ARG   A  1 690  ? -11.542 58.156  117.452 1.00 22.32 ? 688  ARG   A C     1 
ATOM   4846  O  O     . ARG   A  1 690  ? -10.581 57.412  117.263 1.00 21.28 ? 688  ARG   A O     1 
ATOM   4847  C  CB    . ARG   A  1 690  ? -12.995 57.910  115.451 1.00 19.18 ? 688  ARG   A CB    1 
ATOM   4848  C  CG    . ARG   A  1 690  ? -14.232 57.298  114.770 1.00 21.50 ? 688  ARG   A CG    1 
ATOM   4849  C  CD    . ARG   A  1 690  ? -14.181 55.772  114.732 1.00 26.67 ? 688  ARG   A CD    1 
ATOM   4850  N  NE    . ARG   A  1 690  ? -13.028 55.292  113.974 1.00 27.06 ? 688  ARG   A NE    1 
ATOM   4851  C  CZ    . ARG   A  1 690  ? -11.981 54.686  114.517 1.00 28.34 ? 688  ARG   A CZ    1 
ATOM   4852  N  NH1   . ARG   A  1 690  ? -11.918 54.447  115.822 1.00 26.41 ? 688  ARG   A NH1   1 
ATOM   4853  N  NH2   . ARG   A  1 690  ? -10.976 54.303  113.734 1.00 22.89 ? 688  ARG   A NH2   1 
ATOM   4854  N  N     . THR   A  1 691  ? -11.408 59.351  118.063 1.00 18.94 ? 689  THR   A N     1 
ATOM   4855  C  CA    . THR   A  1 691  ? -10.046 59.874  118.215 1.00 18.63 ? 689  THR   A CA    1 
ATOM   4856  C  C     . THR   A  1 691  ? -9.675  60.370  119.606 1.00 23.76 ? 689  THR   A C     1 
ATOM   4857  O  O     . THR   A  1 691  ? -8.550  60.116  120.048 1.00 22.71 ? 689  THR   A O     1 
ATOM   4858  C  CB    . THR   A  1 691  ? -9.786  61.026  117.236 1.00 22.83 ? 689  THR   A CB    1 
ATOM   4859  O  OG1   . THR   A  1 691  ? -10.794 62.033  117.401 1.00 21.11 ? 689  THR   A OG1   1 
ATOM   4860  C  CG2   . THR   A  1 691  ? -9.771  60.522  115.785 1.00 20.51 ? 689  THR   A CG2   1 
ATOM   4861  N  N     . LEU   A  1 692  ? -10.545 61.121  120.282 1.00 22.69 ? 690  LEU   A N     1 
ATOM   4862  C  CA    . LEU   A  1 692  ? -10.073 61.985  121.364 1.00 20.70 ? 690  LEU   A CA    1 
ATOM   4863  C  C     . LEU   A  1 692  ? -9.900  61.222  122.672 1.00 21.30 ? 690  LEU   A C     1 
ATOM   4864  O  O     . LEU   A  1 692  ? -10.781 60.463  123.092 1.00 23.03 ? 690  LEU   A O     1 
ATOM   4865  C  CB    . LEU   A  1 692  ? -11.015 63.170  121.561 1.00 24.08 ? 690  LEU   A CB    1 
ATOM   4866  C  CG    . LEU   A  1 692  ? -11.025 64.149  120.385 1.00 23.83 ? 690  LEU   A CG    1 
ATOM   4867  C  CD1   . LEU   A  1 692  ? -11.845 65.382  120.739 1.00 24.36 ? 690  LEU   A CD1   1 
ATOM   4868  C  CD2   . LEU   A  1 692  ? -9.612  64.548  119.994 1.00 21.88 ? 690  LEU   A CD2   1 
ATOM   4869  N  N     . GLY   A  1 693  ? -8.754  61.425  123.302 1.00 24.69 ? 691  GLY   A N     1 
ATOM   4870  C  CA    . GLY   A  1 693  ? -8.435  60.826  124.575 1.00 24.39 ? 691  GLY   A CA    1 
ATOM   4871  C  C     . GLY   A  1 693  ? -7.928  61.902  125.511 1.00 30.72 ? 691  GLY   A C     1 
ATOM   4872  O  O     . GLY   A  1 693  ? -8.003  63.094  125.205 1.00 29.30 ? 691  GLY   A O     1 
ATOM   4873  N  N     . PRO   A  1 694  ? -7.405  61.515  126.676 1.00 32.93 ? 692  PRO   A N     1 
ATOM   4874  C  CA    . PRO   A  1 694  ? -6.983  62.536  127.651 1.00 33.92 ? 692  PRO   A CA    1 
ATOM   4875  C  C     . PRO   A  1 694  ? -5.707  63.263  127.256 1.00 31.29 ? 692  PRO   A C     1 
ATOM   4876  O  O     . PRO   A  1 694  ? -5.487  64.387  127.717 1.00 35.43 ? 692  PRO   A O     1 
ATOM   4877  C  CB    . PRO   A  1 694  ? -6.804  61.737  128.950 1.00 39.30 ? 692  PRO   A CB    1 
ATOM   4878  C  CG    . PRO   A  1 694  ? -6.542  60.342  128.512 1.00 35.58 ? 692  PRO   A CG    1 
ATOM   4879  C  CD    . PRO   A  1 694  ? -7.280  60.145  127.204 1.00 33.02 ? 692  PRO   A CD    1 
ATOM   4880  N  N     . GLY   A  1 695  ? -4.871  62.677  126.402 1.00 29.60 ? 693  GLY   A N     1 
ATOM   4881  C  CA    . GLY   A  1 695  ? -3.690  63.381  125.942 1.00 33.46 ? 693  GLY   A CA    1 
ATOM   4882  C  C     . GLY   A  1 695  ? -3.957  64.460  124.913 1.00 32.02 ? 693  GLY   A C     1 
ATOM   4883  O  O     . GLY   A  1 695  ? -3.026  65.189  124.556 1.00 28.72 ? 693  GLY   A O     1 
ATOM   4884  N  N     . HIS   A  1 696  ? -5.195  64.578  124.426 1.00 26.13 ? 694  HIS   A N     1 
ATOM   4885  C  CA    . HIS   A  1 696  ? -5.539  65.568  123.404 1.00 26.16 ? 694  HIS   A CA    1 
ATOM   4886  C  C     . HIS   A  1 696  ? -6.241  66.712  124.123 1.00 27.98 ? 694  HIS   A C     1 
ATOM   4887  O  O     . HIS   A  1 696  ? -7.466  66.835  124.119 1.00 28.76 ? 694  HIS   A O     1 
ATOM   4888  C  CB    . HIS   A  1 696  ? -6.405  64.948  122.309 1.00 25.41 ? 694  HIS   A CB    1 
ATOM   4889  C  CG    . HIS   A  1 696  ? -5.828  63.687  121.743 1.00 25.68 ? 694  HIS   A CG    1 
ATOM   4890  N  ND1   . HIS   A  1 696  ? -6.442  62.460  121.873 1.00 23.50 ? 694  HIS   A ND1   1 
ATOM   4891  C  CD2   . HIS   A  1 696  ? -4.669  63.462  121.078 1.00 24.45 ? 694  HIS   A CD2   1 
ATOM   4892  C  CE1   . HIS   A  1 696  ? -5.696  61.534  121.297 1.00 23.87 ? 694  HIS   A CE1   1 
ATOM   4893  N  NE2   . HIS   A  1 696  ? -4.616  62.117  120.803 1.00 24.51 ? 694  HIS   A NE2   1 
ATOM   4894  N  N     . GLY   A  1 697  ? -5.435  67.543  124.775 1.00 25.16 ? 695  GLY   A N     1 
ATOM   4895  C  CA    . GLY   A  1 697  ? -5.953  68.572  125.641 1.00 25.28 ? 695  GLY   A CA    1 
ATOM   4896  C  C     . GLY   A  1 697  ? -6.564  69.710  124.857 1.00 23.72 ? 695  GLY   A C     1 
ATOM   4897  O  O     . GLY   A  1 697  ? -6.127  70.049  123.751 1.00 23.54 ? 695  GLY   A O     1 
ATOM   4898  N  N     . PRO   A  1 698  ? -7.596  70.324  125.412 1.00 26.32 ? 696  PRO   A N     1 
ATOM   4899  C  CA    . PRO   A  1 698  ? -8.245  71.431  124.712 1.00 24.49 ? 696  PRO   A CA    1 
ATOM   4900  C  C     . PRO   A  1 698  ? -7.335  72.649  124.630 1.00 24.10 ? 696  PRO   A C     1 
ATOM   4901  O  O     . PRO   A  1 698  ? -6.396  72.828  125.411 1.00 24.41 ? 696  PRO   A O     1 
ATOM   4902  C  CB    . PRO   A  1 698  ? -9.474  71.718  125.580 1.00 27.12 ? 696  PRO   A CB    1 
ATOM   4903  C  CG    . PRO   A  1 698  ? -9.014  71.377  126.944 1.00 34.36 ? 696  PRO   A CG    1 
ATOM   4904  C  CD    . PRO   A  1 698  ? -8.146  70.137  126.763 1.00 32.24 ? 696  PRO   A CD    1 
ATOM   4905  N  N     . LEU   A  1 699  ? -7.630  73.496  123.646 1.00 22.03 ? 697  LEU   A N     1 
ATOM   4906  C  CA    . LEU   A  1 699  ? -6.957  74.783  123.553 1.00 21.63 ? 697  LEU   A CA    1 
ATOM   4907  C  C     . LEU   A  1 699  ? -7.376  75.706  124.686 1.00 23.80 ? 697  LEU   A C     1 
ATOM   4908  O  O     . LEU   A  1 699  ? -6.541  76.411  125.262 1.00 22.34 ? 697  LEU   A O     1 
ATOM   4909  C  CB    . LEU   A  1 699  ? -7.269  75.435  122.208 1.00 21.54 ? 697  LEU   A CB    1 
ATOM   4910  C  CG    . LEU   A  1 699  ? -6.776  74.713  120.956 1.00 22.23 ? 697  LEU   A CG    1 
ATOM   4911  C  CD1   . LEU   A  1 699  ? -7.295  75.456  119.733 1.00 21.22 ? 697  LEU   A CD1   1 
ATOM   4912  C  CD2   . LEU   A  1 699  ? -5.256  74.621  120.939 1.00 24.53 ? 697  LEU   A CD2   1 
ATOM   4913  N  N     . GLY   A  1 700  ? -8.661  75.716  125.021 1.00 22.85 ? 698  GLY   A N     1 
ATOM   4914  C  CA    . GLY   A  1 700  ? -9.209  76.732  125.887 1.00 21.40 ? 698  GLY   A CA    1 
ATOM   4915  C  C     . GLY   A  1 700  ? -10.342 77.432  125.167 1.00 21.22 ? 698  GLY   A C     1 
ATOM   4916  O  O     . GLY   A  1 700  ? -10.860 76.930  124.165 1.00 22.22 ? 698  GLY   A O     1 
ATOM   4917  N  N     . PRO   A  1 701  ? -10.748 78.604  125.653 1.00 22.24 ? 699  PRO   A N     1 
ATOM   4918  C  CA    . PRO   A  1 701  ? -11.907 79.285  125.049 1.00 20.40 ? 699  PRO   A CA    1 
ATOM   4919  C  C     . PRO   A  1 701  ? -11.688 79.539  123.562 1.00 19.90 ? 699  PRO   A C     1 
ATOM   4920  O  O     . PRO   A  1 701  ? -10.653 80.058  123.146 1.00 20.65 ? 699  PRO   A O     1 
ATOM   4921  C  CB    . PRO   A  1 701  ? -12.003 80.595  125.841 1.00 23.24 ? 699  PRO   A CB    1 
ATOM   4922  C  CG    . PRO   A  1 701  ? -11.278 80.304  127.151 1.00 23.91 ? 699  PRO   A CG    1 
ATOM   4923  C  CD    . PRO   A  1 701  ? -10.170 79.360  126.776 1.00 22.36 ? 699  PRO   A CD    1 
ATOM   4924  N  N     . ILE   A  1 702  ? -12.672 79.157  122.755 1.00 20.73 ? 700  ILE   A N     1 
ATOM   4925  C  CA    . ILE   A  1 702  ? -12.592 79.312  121.311 1.00 20.10 ? 700  ILE   A CA    1 
ATOM   4926  C  C     . ILE   A  1 702  ? -13.663 80.302  120.879 1.00 21.65 ? 700  ILE   A C     1 
ATOM   4927  O  O     . ILE   A  1 702  ? -14.830 80.174  121.266 1.00 19.34 ? 700  ILE   A O     1 
ATOM   4928  C  CB    . ILE   A  1 702  ? -12.744 77.966  120.580 1.00 22.66 ? 700  ILE   A CB    1 
ATOM   4929  C  CG1   . ILE   A  1 702  ? -11.511 77.094  120.866 1.00 20.13 ? 700  ILE   A CG1   1 
ATOM   4930  C  CG2   . ILE   A  1 702  ? -12.911 78.194  119.100 1.00 19.00 ? 700  ILE   A CG2   1 
ATOM   4931  C  CD1   . ILE   A  1 702  ? -11.414 75.855  120.024 1.00 25.27 ? 700  ILE   A CD1   1 
ATOM   4932  N  N     . VAL   A  1 703  ? -13.261 81.292  120.092 1.00 20.48 ? 701  VAL   A N     1 
ATOM   4933  C  CA    . VAL   A  1 703  ? -14.193 82.265  119.546 1.00 19.23 ? 701  VAL   A CA    1 
ATOM   4934  C  C     . VAL   A  1 703  ? -14.649 81.736  118.197 1.00 20.58 ? 701  VAL   A C     1 
ATOM   4935  O  O     . VAL   A  1 703  ? -13.822 81.479  117.316 1.00 21.50 ? 701  VAL   A O     1 
ATOM   4936  C  CB    . VAL   A  1 703  ? -13.549 83.651  119.402 1.00 19.44 ? 701  VAL   A CB    1 
ATOM   4937  C  CG1   . VAL   A  1 703  ? -14.511 84.578  118.675 1.00 19.50 ? 701  VAL   A CG1   1 
ATOM   4938  C  CG2   . VAL   A  1 703  ? -13.192 84.218  120.779 1.00 19.98 ? 701  VAL   A CG2   1 
ATOM   4939  N  N     . CYS   A  1 704  ? -15.957 81.537  118.051 1.00 18.75 ? 702  CYS   A N     1 
ATOM   4940  C  CA    . CYS   A  1 704  ? -16.546 81.062  116.805 1.00 19.24 ? 702  CYS   A CA    1 
ATOM   4941  C  C     . CYS   A  1 704  ? -17.339 82.215  116.208 1.00 19.86 ? 702  CYS   A C     1 
ATOM   4942  O  O     . CYS   A  1 704  ? -18.350 82.648  116.776 1.00 18.62 ? 702  CYS   A O     1 
ATOM   4943  C  CB    . CYS   A  1 704  ? -17.426 79.833  117.036 1.00 18.28 ? 702  CYS   A CB    1 
ATOM   4944  S  SG    . CYS   A  1 704  ? -16.555 78.407  117.763 1.00 19.94 ? 702  CYS   A SG    1 
ATOM   4945  N  N     . ILE   A  1 705  ? -16.869 82.715  115.067 1.00 18.86 ? 703  ILE   A N     1 
ATOM   4946  C  CA    . ILE   A  1 705  ? -17.515 83.801  114.343 1.00 19.08 ? 703  ILE   A CA    1 
ATOM   4947  C  C     . ILE   A  1 705  ? -18.086 83.201  113.071 1.00 18.22 ? 703  ILE   A C     1 
ATOM   4948  O  O     . ILE   A  1 705  ? -17.344 82.645  112.251 1.00 20.61 ? 703  ILE   A O     1 
ATOM   4949  C  CB    . ILE   A  1 705  ? -16.531 84.941  114.041 1.00 21.95 ? 703  ILE   A CB    1 
ATOM   4950  C  CG1   . ILE   A  1 705  ? -16.072 85.579  115.356 1.00 20.39 ? 703  ILE   A CG1   1 
ATOM   4951  C  CG2   . ILE   A  1 705  ? -17.180 85.980  113.139 1.00 22.55 ? 703  ILE   A CG2   1 
ATOM   4952  C  CD1   . ILE   A  1 705  ? -14.862 86.466  115.217 1.00 21.89 ? 703  ILE   A CD1   1 
ATOM   4953  N  N     . SER   A  1 706  ? -19.398 83.282  112.923 1.00 20.21 ? 704  SER   A N     1 
ATOM   4954  C  CA    . SER   A  1 706  ? -20.097 82.585  111.858 1.00 19.07 ? 704  SER   A CA    1 
ATOM   4955  C  C     . SER   A  1 706  ? -20.732 83.585  110.904 1.00 19.87 ? 704  SER   A C     1 
ATOM   4956  O  O     . SER   A  1 706  ? -20.941 84.754  111.256 1.00 21.23 ? 704  SER   A O     1 
ATOM   4957  C  CB    . SER   A  1 706  ? -21.167 81.655  112.440 1.00 19.26 ? 704  SER   A CB    1 
ATOM   4958  O  OG    . SER   A  1 706  ? -21.974 82.367  113.369 1.00 20.56 ? 704  SER   A OG    1 
ATOM   4959  N  N     . PRO   A  1 707  ? -21.026 83.164  109.673 1.00 21.01 ? 705  PRO   A N     1 
ATOM   4960  C  CA    . PRO   A  1 707  ? -21.532 84.102  108.663 1.00 21.42 ? 705  PRO   A CA    1 
ATOM   4961  C  C     . PRO   A  1 707  ? -23.042 84.086  108.556 1.00 20.20 ? 705  PRO   A C     1 
ATOM   4962  O  O     . PRO   A  1 707  ? -23.709 83.216  109.125 1.00 19.60 ? 705  PRO   A O     1 
ATOM   4963  C  CB    . PRO   A  1 707  ? -20.886 83.589  107.373 1.00 21.57 ? 705  PRO   A CB    1 
ATOM   4964  C  CG    . PRO   A  1 707  ? -20.878 82.096  107.580 1.00 20.76 ? 705  PRO   A CG    1 
ATOM   4965  C  CD    . PRO   A  1 707  ? -20.638 81.876  109.074 1.00 20.47 ? 705  PRO   A CD    1 
ATOM   4966  N  N     . TRP   A  1 708  ? -23.592 85.049  107.821 1.00 20.60 ? 706  TRP   A N     1 
ATOM   4967  C  CA    . TRP   A  1 708  ? -25.038 85.133  107.687 1.00 20.46 ? 706  TRP   A CA    1 
ATOM   4968  C  C     . TRP   A  1 708  ? -25.573 84.203  106.610 1.00 21.09 ? 706  TRP   A C     1 
ATOM   4969  O  O     . TRP   A  1 708  ? -26.785 83.959  106.566 1.00 22.19 ? 706  TRP   A O     1 
ATOM   4970  C  CB    . TRP   A  1 708  ? -25.457 86.573  107.382 1.00 20.12 ? 706  TRP   A CB    1 
ATOM   4971  C  CG    . TRP   A  1 708  ? -24.658 87.169  106.285 1.00 21.72 ? 706  TRP   A CG    1 
ATOM   4972  C  CD1   . TRP   A  1 708  ? -23.582 87.988  106.419 1.00 28.54 ? 706  TRP   A CD1   1 
ATOM   4973  C  CD2   . TRP   A  1 708  ? -24.835 86.967  104.882 1.00 19.90 ? 706  TRP   A CD2   1 
ATOM   4974  N  NE1   . TRP   A  1 708  ? -23.081 88.317  105.188 1.00 27.46 ? 706  TRP   A NE1   1 
ATOM   4975  C  CE2   . TRP   A  1 708  ? -23.836 87.708  104.226 1.00 22.48 ? 706  TRP   A CE2   1 
ATOM   4976  C  CE3   . TRP   A  1 708  ? -25.760 86.260  104.116 1.00 20.41 ? 706  TRP   A CE3   1 
ATOM   4977  C  CZ2   . TRP   A  1 708  ? -23.719 87.743  102.839 1.00 23.20 ? 706  TRP   A CZ2   1 
ATOM   4978  C  CZ3   . TRP   A  1 708  ? -25.642 86.289  102.739 1.00 19.68 ? 706  TRP   A CZ3   1 
ATOM   4979  C  CH2   . TRP   A  1 708  ? -24.629 87.030  102.114 1.00 24.08 ? 706  TRP   A CH2   1 
ATOM   4980  N  N     . ASN   A  1 709  ? -24.707 83.677  105.741 1.00 20.28 ? 707  ASN   A N     1 
ATOM   4981  C  CA    . ASN   A  1 709  ? -25.206 82.915  104.600 1.00 22.02 ? 707  ASN   A CA    1 
ATOM   4982  C  C     . ASN   A  1 709  ? -25.472 81.457  104.933 1.00 22.19 ? 707  ASN   A C     1 
ATOM   4983  O  O     . ASN   A  1 709  ? -26.236 80.803  104.220 1.00 22.31 ? 707  ASN   A O     1 
ATOM   4984  C  CB    . ASN   A  1 709  ? -24.227 83.007  103.424 1.00 20.84 ? 707  ASN   A CB    1 
ATOM   4985  C  CG    . ASN   A  1 709  ? -22.903 82.331  103.708 1.00 22.17 ? 707  ASN   A CG    1 
ATOM   4986  O  OD1   . ASN   A  1 709  ? -22.469 82.238  104.855 1.00 26.49 ? 707  ASN   A OD1   1 
ATOM   4987  N  ND2   . ASN   A  1 709  ? -22.256 81.845  102.661 1.00 22.79 ? 707  ASN   A ND2   1 
ATOM   4988  N  N     . PHE   A  1 710  ? -24.865 80.928  105.985 1.00 21.02 ? 708  PHE   A N     1 
ATOM   4989  C  CA    . PHE   A  1 710  ? -25.243 79.626  106.532 1.00 19.14 ? 708  PHE   A CA    1 
ATOM   4990  C  C     . PHE   A  1 710  ? -25.402 79.808  108.027 1.00 21.09 ? 708  PHE   A C     1 
ATOM   4991  O  O     . PHE   A  1 710  ? -24.590 79.321  108.827 1.00 18.28 ? 708  PHE   A O     1 
ATOM   4992  C  CB    . PHE   A  1 710  ? -24.224 78.541  106.191 1.00 20.86 ? 708  PHE   A CB    1 
ATOM   4993  C  CG    . PHE   A  1 710  ? -24.167 78.233  104.727 1.00 22.84 ? 708  PHE   A CG    1 
ATOM   4994  C  CD1   . PHE   A  1 710  ? -25.188 77.523  104.118 1.00 27.90 ? 708  PHE   A CD1   1 
ATOM   4995  C  CD2   . PHE   A  1 710  ? -23.106 78.672  103.958 1.00 26.84 ? 708  PHE   A CD2   1 
ATOM   4996  C  CE1   . PHE   A  1 710  ? -25.144 77.246  102.757 1.00 29.01 ? 708  PHE   A CE1   1 
ATOM   4997  C  CE2   . PHE   A  1 710  ? -23.047 78.392  102.599 1.00 32.81 ? 708  PHE   A CE2   1 
ATOM   4998  C  CZ    . PHE   A  1 710  ? -24.072 77.687  101.999 1.00 30.01 ? 708  PHE   A CZ    1 
ATOM   4999  N  N     . PRO   A  1 711  ? -26.460 80.514  108.436 1.00 19.45 ? 709  PRO   A N     1 
ATOM   5000  C  CA    . PRO   A  1 711  ? -26.540 81.010  109.808 1.00 20.26 ? 709  PRO   A CA    1 
ATOM   5001  C  C     . PRO   A  1 711  ? -26.838 79.938  110.829 1.00 19.10 ? 709  PRO   A C     1 
ATOM   5002  O  O     . PRO   A  1 711  ? -26.707 80.209  112.025 1.00 19.15 ? 709  PRO   A O     1 
ATOM   5003  C  CB    . PRO   A  1 711  ? -27.674 82.036  109.731 1.00 20.01 ? 709  PRO   A CB    1 
ATOM   5004  C  CG    . PRO   A  1 711  ? -28.574 81.494  108.655 1.00 17.08 ? 709  PRO   A CG    1 
ATOM   5005  C  CD    . PRO   A  1 711  ? -27.640 80.889  107.635 1.00 18.72 ? 709  PRO   A CD    1 
ATOM   5006  N  N     . LEU   A  1 712  ? -27.247 78.746  110.411 1.00 22.02 ? 710  LEU   A N     1 
ATOM   5007  C  CA    . LEU   A  1 712  ? -27.333 77.608  111.317 1.00 18.27 ? 710  LEU   A CA    1 
ATOM   5008  C  C     . LEU   A  1 712  ? -26.250 76.574  111.071 1.00 18.55 ? 710  LEU   A C     1 
ATOM   5009  O  O     . LEU   A  1 712  ? -25.653 76.082  112.021 1.00 18.10 ? 710  LEU   A O     1 
ATOM   5010  C  CB    . LEU   A  1 712  ? -28.708 76.928  111.210 1.00 18.16 ? 710  LEU   A CB    1 
ATOM   5011  C  CG    . LEU   A  1 712  ? -28.887 75.737  112.158 1.00 20.45 ? 710  LEU   A CG    1 
ATOM   5012  C  CD1   . LEU   A  1 712  ? -28.853 76.184  113.638 1.00 17.43 ? 710  LEU   A CD1   1 
ATOM   5013  C  CD2   . LEU   A  1 712  ? -30.170 74.984  111.848 1.00 21.02 ? 710  LEU   A CD2   1 
ATOM   5014  N  N     . ALA   A  1 713  ? -25.950 76.242  109.817 1.00 17.13 ? 711  ALA   A N     1 
ATOM   5015  C  CA    . ALA   A  1 713  ? -25.079 75.098  109.576 1.00 17.59 ? 711  ALA   A CA    1 
ATOM   5016  C  C     . ALA   A  1 713  ? -23.630 75.421  109.915 1.00 18.34 ? 711  ALA   A C     1 
ATOM   5017  O  O     . ALA   A  1 713  ? -22.966 74.661  110.630 1.00 18.34 ? 711  ALA   A O     1 
ATOM   5018  C  CB    . ALA   A  1 713  ? -25.195 74.643  108.120 1.00 18.81 ? 711  ALA   A CB    1 
ATOM   5019  N  N     . ILE   A  1 714  ? -23.105 76.523  109.384 1.00 20.67 ? 712  ILE   A N     1 
ATOM   5020  C  CA    . ILE   A  1 714  ? -21.718 76.846  109.683 1.00 18.94 ? 712  ILE   A CA    1 
ATOM   5021  C  C     . ILE   A  1 714  ? -21.585 77.283  111.134 1.00 19.19 ? 712  ILE   A C     1 
ATOM   5022  O  O     . ILE   A  1 714  ? -20.601 76.957  111.811 1.00 20.67 ? 712  ILE   A O     1 
ATOM   5023  C  CB    . ILE   A  1 714  ? -21.187 77.902  108.704 1.00 20.56 ? 712  ILE   A CB    1 
ATOM   5024  C  CG1   . ILE   A  1 714  ? -21.102 77.273  107.307 1.00 22.47 ? 712  ILE   A CG1   1 
ATOM   5025  C  CG2   . ILE   A  1 714  ? -19.804 78.405  109.172 1.00 18.06 ? 712  ILE   A CG2   1 
ATOM   5026  C  CD1   . ILE   A  1 714  ? -20.299 78.075  106.294 1.00 26.59 ? 712  ILE   A CD1   1 
ATOM   5027  N  N     . PHE   A  1 715  ? -22.586 78.008  111.633 1.00 17.82 ? 713  PHE   A N     1 
ATOM   5028  C  CA    . PHE   A  1 715  ? -22.663 78.339  113.050 1.00 19.52 ? 713  PHE   A CA    1 
ATOM   5029  C  C     . PHE   A  1 715  ? -22.539 77.085  113.906 1.00 21.64 ? 713  PHE   A C     1 
ATOM   5030  O  O     . PHE   A  1 715  ? -21.678 77.000  114.791 1.00 19.40 ? 713  PHE   A O     1 
ATOM   5031  C  CB    . PHE   A  1 715  ? -23.985 79.056  113.324 1.00 19.27 ? 713  PHE   A CB    1 
ATOM   5032  C  CG    . PHE   A  1 715  ? -24.239 79.348  114.776 1.00 18.29 ? 713  PHE   A CG    1 
ATOM   5033  C  CD1   . PHE   A  1 715  ? -23.732 80.497  115.363 1.00 20.31 ? 713  PHE   A CD1   1 
ATOM   5034  C  CD2   . PHE   A  1 715  ? -25.015 78.495  115.543 1.00 21.19 ? 713  PHE   A CD2   1 
ATOM   5035  C  CE1   . PHE   A  1 715  ? -23.981 80.786  116.716 1.00 22.43 ? 713  PHE   A CE1   1 
ATOM   5036  C  CE2   . PHE   A  1 715  ? -25.264 78.767  116.887 1.00 20.05 ? 713  PHE   A CE2   1 
ATOM   5037  C  CZ    . PHE   A  1 715  ? -24.752 79.920  117.472 1.00 23.02 ? 713  PHE   A CZ    1 
ATOM   5038  N  N     . THR   A  1 716  ? -23.385 76.090  113.638 1.00 17.21 ? 714  THR   A N     1 
ATOM   5039  C  CA    . THR   A  1 716  ? -23.362 74.863  114.427 1.00 17.28 ? 714  THR   A CA    1 
ATOM   5040  C  C     . THR   A  1 716  ? -22.061 74.101  114.242 1.00 17.88 ? 714  THR   A C     1 
ATOM   5041  O  O     . THR   A  1 716  ? -21.492 73.593  115.214 1.00 19.12 ? 714  THR   A O     1 
ATOM   5042  C  CB    . THR   A  1 716  ? -24.548 73.978  114.049 1.00 19.80 ? 714  THR   A CB    1 
ATOM   5043  O  OG1   . THR   A  1 716  ? -25.758 74.689  114.320 1.00 19.17 ? 714  THR   A OG1   1 
ATOM   5044  C  CG2   . THR   A  1 716  ? -24.534 72.679  114.852 1.00 18.34 ? 714  THR   A CG2   1 
ATOM   5045  N  N     . GLY   A  1 717  ? -21.574 74.008  113.006 1.00 18.18 ? 715  GLY   A N     1 
ATOM   5046  C  CA    . GLY   A  1 717  ? -20.395 73.192  112.760 1.00 17.92 ? 715  GLY   A CA    1 
ATOM   5047  C  C     . GLY   A  1 717  ? -19.181 73.687  113.522 1.00 19.69 ? 715  GLY   A C     1 
ATOM   5048  O  O     . GLY   A  1 717  ? -18.483 72.905  114.169 1.00 18.52 ? 715  GLY   A O     1 
ATOM   5049  N  N     . GLN   A  1 718  ? -18.910 74.994  113.456 1.00 18.08 ? 716  GLN   A N     1 
ATOM   5050  C  CA    . GLN   A  1 718  ? -17.763 75.524  114.197 1.00 19.85 ? 716  GLN   A CA    1 
ATOM   5051  C  C     . GLN   A  1 718  ? -17.929 75.295  115.691 1.00 18.74 ? 716  GLN   A C     1 
ATOM   5052  O  O     . GLN   A  1 718  ? -17.010 74.826  116.371 1.00 18.09 ? 716  GLN   A O     1 
ATOM   5053  C  CB    . GLN   A  1 718  ? -17.578 77.013  113.908 1.00 18.64 ? 716  GLN   A CB    1 
ATOM   5054  C  CG    . GLN   A  1 718  ? -17.222 77.295  112.435 1.00 17.24 ? 716  GLN   A CG    1 
ATOM   5055  C  CD    . GLN   A  1 718  ? -16.913 78.755  112.173 1.00 21.88 ? 716  GLN   A CD    1 
ATOM   5056  O  OE1   . GLN   A  1 718  ? -16.029 79.071  111.383 1.00 22.53 ? 716  GLN   A OE1   1 
ATOM   5057  N  NE2   . GLN   A  1 718  ? -17.634 79.651  112.836 1.00 20.37 ? 716  GLN   A NE2   1 
ATOM   5058  N  N     . ILE   A  1 719  ? -19.100 75.629  116.224 1.00 17.67 ? 717  ILE   A N     1 
ATOM   5059  C  CA    . ILE   A  1 719  ? -19.304 75.511  117.663 1.00 17.99 ? 717  ILE   A CA    1 
ATOM   5060  C  C     . ILE   A  1 719  ? -19.240 74.056  118.097 1.00 18.64 ? 717  ILE   A C     1 
ATOM   5061  O  O     . ILE   A  1 719  ? -18.634 73.729  119.126 1.00 19.78 ? 717  ILE   A O     1 
ATOM   5062  C  CB    . ILE   A  1 719  ? -20.639 76.161  118.047 1.00 19.33 ? 717  ILE   A CB    1 
ATOM   5063  C  CG1   . ILE   A  1 719  ? -20.515 77.662  117.842 1.00 18.23 ? 717  ILE   A CG1   1 
ATOM   5064  C  CG2   . ILE   A  1 719  ? -21.019 75.800  119.475 1.00 23.33 ? 717  ILE   A CG2   1 
ATOM   5065  C  CD1   . ILE   A  1 719  ? -21.823 78.308  117.644 1.00 25.97 ? 717  ILE   A CD1   1 
ATOM   5066  N  N     . ALA   A  1 720  ? -19.870 73.163  117.328 1.00 18.10 ? 718  ALA   A N     1 
ATOM   5067  C  CA    . ALA   A  1 720  ? -19.911 71.756  117.722 1.00 19.63 ? 718  ALA   A CA    1 
ATOM   5068  C  C     . ALA   A  1 720  ? -18.513 71.167  117.770 1.00 18.42 ? 718  ALA   A C     1 
ATOM   5069  O  O     . ALA   A  1 720  ? -18.167 70.429  118.698 1.00 17.96 ? 718  ALA   A O     1 
ATOM   5070  C  CB    . ALA   A  1 720  ? -20.781 70.954  116.758 1.00 17.74 ? 718  ALA   A CB    1 
ATOM   5071  N  N     . ALA   A  1 721  ? -17.697 71.474  116.766 1.00 17.94 ? 719  ALA   A N     1 
ATOM   5072  C  CA    . ALA   A  1 721  ? -16.337 70.966  116.762 1.00 17.53 ? 719  ALA   A CA    1 
ATOM   5073  C  C     . ALA   A  1 721  ? -15.551 71.486  117.963 1.00 17.83 ? 719  ALA   A C     1 
ATOM   5074  O  O     . ALA   A  1 721  ? -14.887 70.717  118.659 1.00 17.97 ? 719  ALA   A O     1 
ATOM   5075  C  CB    . ALA   A  1 721  ? -15.650 71.343  115.452 1.00 17.28 ? 719  ALA   A CB    1 
ATOM   5076  N  N     . ALA   A  1 722  ? -15.597 72.795  118.210 1.00 17.94 ? 720  ALA   A N     1 
ATOM   5077  C  CA    . ALA   A  1 722  ? -14.831 73.346  119.325 1.00 18.24 ? 720  ALA   A CA    1 
ATOM   5078  C  C     . ALA   A  1 722  ? -15.294 72.741  120.644 1.00 18.74 ? 720  ALA   A C     1 
ATOM   5079  O  O     . ALA   A  1 722  ? -14.477 72.318  121.471 1.00 18.71 ? 720  ALA   A O     1 
ATOM   5080  C  CB    . ALA   A  1 722  ? -14.957 74.868  119.353 1.00 18.34 ? 720  ALA   A CB    1 
ATOM   5081  N  N     . LEU   A  1 723  ? -16.613 72.689  120.852 1.00 18.77 ? 721  LEU   A N     1 
ATOM   5082  C  CA    . LEU   A  1 723  ? -17.160 72.096  122.068 1.00 18.85 ? 721  LEU   A CA    1 
ATOM   5083  C  C     . LEU   A  1 723  ? -16.725 70.648  122.224 1.00 18.85 ? 721  LEU   A C     1 
ATOM   5084  O  O     . LEU   A  1 723  ? -16.306 70.225  123.308 1.00 19.71 ? 721  LEU   A O     1 
ATOM   5085  C  CB    . LEU   A  1 723  ? -18.684 72.170  122.047 1.00 19.24 ? 721  LEU   A CB    1 
ATOM   5086  C  CG    . LEU   A  1 723  ? -19.349 73.526  122.245 1.00 20.85 ? 721  LEU   A CG    1 
ATOM   5087  C  CD1   . LEU   A  1 723  ? -20.864 73.362  122.050 1.00 18.97 ? 721  LEU   A CD1   1 
ATOM   5088  C  CD2   . LEU   A  1 723  ? -19.040 74.073  123.627 1.00 19.40 ? 721  LEU   A CD2   1 
ATOM   5089  N  N     . VAL   A  1 724  ? -16.866 69.852  121.161 1.00 19.61 ? 722  VAL   A N     1 
ATOM   5090  C  CA    . VAL   A  1 724  ? -16.655 68.426  121.346 1.00 20.06 ? 722  VAL   A CA    1 
ATOM   5091  C  C     . VAL   A  1 724  ? -15.180 68.126  121.522 1.00 19.23 ? 722  VAL   A C     1 
ATOM   5092  O  O     . VAL   A  1 724  ? -14.822 67.116  122.142 1.00 22.03 ? 722  VAL   A O     1 
ATOM   5093  C  CB    . VAL   A  1 724  ? -17.292 67.636  120.188 1.00 18.30 ? 722  VAL   A CB    1 
ATOM   5094  C  CG1   . VAL   A  1 724  ? -16.392 67.638  118.953 1.00 19.28 ? 722  VAL   A CG1   1 
ATOM   5095  C  CG2   . VAL   A  1 724  ? -17.647 66.228  120.649 1.00 18.86 ? 722  VAL   A CG2   1 
ATOM   5096  N  N     . ALA   A  1 725  ? -14.313 69.003  121.017 1.00 18.52 ? 723  ALA   A N     1 
ATOM   5097  C  CA    . ALA   A  1 725  ? -12.885 68.940  121.285 1.00 19.29 ? 723  ALA   A CA    1 
ATOM   5098  C  C     . ALA   A  1 725  ? -12.536 69.335  122.716 1.00 20.62 ? 723  ALA   A C     1 
ATOM   5099  O  O     . ALA   A  1 725  ? -11.355 69.310  123.074 1.00 21.80 ? 723  ALA   A O     1 
ATOM   5100  C  CB    . ALA   A  1 725  ? -12.137 69.839  120.302 1.00 19.83 ? 723  ALA   A CB    1 
ATOM   5101  N  N     . GLY   A  1 726  ? -13.513 69.716  123.535 1.00 21.54 ? 724  GLY   A N     1 
ATOM   5102  C  CA    . GLY   A  1 726  ? -13.248 70.043  124.917 1.00 22.51 ? 724  GLY   A CA    1 
ATOM   5103  C  C     . GLY   A  1 726  ? -13.047 71.512  125.212 1.00 20.48 ? 724  GLY   A C     1 
ATOM   5104  O  O     . GLY   A  1 726  ? -12.572 71.843  126.302 1.00 24.51 ? 724  GLY   A O     1 
ATOM   5105  N  N     . ASN   A  1 727  ? -13.397 72.394  124.291 1.00 19.68 ? 725  ASN   A N     1 
ATOM   5106  C  CA    . ASN   A  1 727  ? -13.182 73.815  124.481 1.00 19.60 ? 725  ASN   A CA    1 
ATOM   5107  C  C     . ASN   A  1 727  ? -14.494 74.517  124.770 1.00 20.31 ? 725  ASN   A C     1 
ATOM   5108  O  O     . ASN   A  1 727  ? -15.499 74.232  124.114 1.00 21.36 ? 725  ASN   A O     1 
ATOM   5109  C  CB    . ASN   A  1 727  ? -12.566 74.455  123.239 1.00 21.24 ? 725  ASN   A CB    1 
ATOM   5110  C  CG    . ASN   A  1 727  ? -11.351 73.716  122.755 1.00 20.48 ? 725  ASN   A CG    1 
ATOM   5111  O  OD1   . ASN   A  1 727  ? -10.276 73.840  123.334 1.00 21.12 ? 725  ASN   A OD1   1 
ATOM   5112  N  ND2   . ASN   A  1 727  ? -11.509 72.943  121.683 1.00 19.64 ? 725  ASN   A ND2   1 
ATOM   5113  N  N     . PRO   A  1 728  ? -14.513 75.460  125.703 1.00 20.05 ? 726  PRO   A N     1 
ATOM   5114  C  CA    . PRO   A  1 728  ? -15.689 76.327  125.832 1.00 20.15 ? 726  PRO   A CA    1 
ATOM   5115  C  C     . PRO   A  1 728  ? -15.704 77.337  124.699 1.00 19.92 ? 726  PRO   A C     1 
ATOM   5116  O  O     . PRO   A  1 728  ? -14.658 77.745  124.189 1.00 21.32 ? 726  PRO   A O     1 
ATOM   5117  C  CB    . PRO   A  1 728  ? -15.489 76.999  127.196 1.00 20.62 ? 726  PRO   A CB    1 
ATOM   5118  C  CG    . PRO   A  1 728  ? -13.973 77.072  127.325 1.00 23.11 ? 726  PRO   A CG    1 
ATOM   5119  C  CD    . PRO   A  1 728  ? -13.429 75.839  126.631 1.00 20.48 ? 726  PRO   A CD    1 
ATOM   5120  N  N     . VAL   A  1 729  ? -16.908 77.723  124.291 1.00 20.60 ? 727  VAL   A N     1 
ATOM   5121  C  CA    . VAL   A  1 729  ? -17.114 78.467  123.055 1.00 19.59 ? 727  VAL   A CA    1 
ATOM   5122  C  C     . VAL   A  1 729  ? -17.785 79.803  123.340 1.00 20.07 ? 727  VAL   A C     1 
ATOM   5123  O  O     . VAL   A  1 729  ? -18.751 79.886  124.109 1.00 21.20 ? 727  VAL   A O     1 
ATOM   5124  C  CB    . VAL   A  1 729  ? -17.952 77.650  122.052 1.00 19.24 ? 727  VAL   A CB    1 
ATOM   5125  C  CG1   . VAL   A  1 729  ? -18.414 78.528  120.875 1.00 19.03 ? 727  VAL   A CG1   1 
ATOM   5126  C  CG2   . VAL   A  1 729  ? -17.134 76.482  121.553 1.00 19.00 ? 727  VAL   A CG2   1 
ATOM   5127  N  N     . LEU   A  1 730  ? -17.271 80.845  122.700 1.00 19.78 ? 728  LEU   A N     1 
ATOM   5128  C  CA    . LEU   A  1 730  ? -17.935 82.136  122.594 1.00 19.94 ? 728  LEU   A CA    1 
ATOM   5129  C  C     . LEU   A  1 730  ? -18.475 82.207  121.174 1.00 19.59 ? 728  LEU   A C     1 
ATOM   5130  O  O     . LEU   A  1 730  ? -17.699 82.273  120.217 1.00 20.43 ? 728  LEU   A O     1 
ATOM   5131  C  CB    . LEU   A  1 730  ? -16.976 83.290  122.873 1.00 20.19 ? 728  LEU   A CB    1 
ATOM   5132  C  CG    . LEU   A  1 730  ? -16.229 83.335  124.219 1.00 20.56 ? 728  LEU   A CG    1 
ATOM   5133  C  CD1   . LEU   A  1 730  ? -17.216 83.084  125.366 1.00 20.85 ? 728  LEU   A CD1   1 
ATOM   5134  C  CD2   . LEU   A  1 730  ? -15.039 82.369  124.279 1.00 21.91 ? 728  LEU   A CD2   1 
ATOM   5135  N  N     . ALA   A  1 731  ? -19.795 82.144  121.034 1.00 19.84 ? 729  ALA   A N     1 
ATOM   5136  C  CA    . ALA   A  1 731  ? -20.431 82.061  119.725 1.00 19.23 ? 729  ALA   A CA    1 
ATOM   5137  C  C     . ALA   A  1 731  ? -20.866 83.459  119.309 1.00 20.43 ? 729  ALA   A C     1 
ATOM   5138  O  O     . ALA   A  1 731  ? -21.784 84.036  119.909 1.00 21.60 ? 729  ALA   A O     1 
ATOM   5139  C  CB    . ALA   A  1 731  ? -21.619 81.100  119.763 1.00 20.24 ? 729  ALA   A CB    1 
ATOM   5140  N  N     . LYS   A  1 732  ? -20.215 83.998  118.279 1.00 19.76 ? 730  LYS   A N     1 
ATOM   5141  C  CA    . LYS   A  1 732  ? -20.545 85.320  117.753 1.00 19.31 ? 730  LYS   A CA    1 
ATOM   5142  C  C     . LYS   A  1 732  ? -21.213 85.144  116.399 1.00 21.32 ? 730  LYS   A C     1 
ATOM   5143  O  O     . LYS   A  1 732  ? -20.521 84.964  115.384 1.00 19.77 ? 730  LYS   A O     1 
ATOM   5144  C  CB    . LYS   A  1 732  ? -19.292 86.188  117.621 1.00 22.03 ? 730  LYS   A CB    1 
ATOM   5145  C  CG    . LYS   A  1 732  ? -19.494 87.650  118.016 1.00 26.94 ? 730  LYS   A CG    1 
ATOM   5146  C  CD    . LYS   A  1 732  ? -20.512 88.349  117.130 1.00 27.57 ? 730  LYS   A CD    1 
ATOM   5147  C  CE    . LYS   A  1 732  ? -20.030 88.437  115.695 1.00 31.83 ? 730  LYS   A CE    1 
ATOM   5148  N  NZ    . LYS   A  1 732  ? -20.936 89.310  114.894 1.00 25.62 ? 730  LYS   A NZ    1 
ATOM   5149  N  N     . PRO   A  1 733  ? -22.535 85.160  116.330 1.00 21.22 ? 731  PRO   A N     1 
ATOM   5150  C  CA    . PRO   A  1 733  ? -23.209 84.999  115.042 1.00 19.29 ? 731  PRO   A CA    1 
ATOM   5151  C  C     . PRO   A  1 733  ? -23.163 86.290  114.245 1.00 20.46 ? 731  PRO   A C     1 
ATOM   5152  O  O     . PRO   A  1 733  ? -22.940 87.377  114.779 1.00 20.37 ? 731  PRO   A O     1 
ATOM   5153  C  CB    . PRO   A  1 733  ? -24.644 84.654  115.445 1.00 20.40 ? 731  PRO   A CB    1 
ATOM   5154  C  CG    . PRO   A  1 733  ? -24.835 85.369  116.739 1.00 23.09 ? 731  PRO   A CG    1 
ATOM   5155  C  CD    . PRO   A  1 733  ? -23.493 85.374  117.432 1.00 20.11 ? 731  PRO   A CD    1 
ATOM   5156  N  N     . ALA   A  1 734  ? -23.374 86.151  112.939 1.00 18.50 ? 732  ALA   A N     1 
ATOM   5157  C  CA    . ALA   A  1 734  ? -23.473 87.324  112.085 1.00 20.00 ? 732  ALA   A CA    1 
ATOM   5158  C  C     . ALA   A  1 734  ? -24.549 88.272  112.597 1.00 19.97 ? 732  ALA   A C     1 
ATOM   5159  O  O     . ALA   A  1 734  ? -25.615 87.846  113.050 1.00 21.81 ? 732  ALA   A O     1 
ATOM   5160  C  CB    . ALA   A  1 734  ? -23.787 86.910  110.647 1.00 20.48 ? 732  ALA   A CB    1 
ATOM   5161  N  N     . GLU   A  1 735  ? -24.267 89.571  112.490 1.00 21.14 ? 733  GLU   A N     1 
ATOM   5162  C  CA    . GLU   A  1 735  ? -25.224 90.590  112.909 1.00 23.65 ? 733  GLU   A CA    1 
ATOM   5163  C  C     . GLU   A  1 735  ? -26.575 90.425  112.219 1.00 22.42 ? 733  GLU   A C     1 
ATOM   5164  O  O     . GLU   A  1 735  ? -27.618 90.772  112.791 1.00 21.52 ? 733  GLU   A O     1 
ATOM   5165  C  CB    . GLU   A  1 735  ? -24.648 91.965  112.605 1.00 27.73 ? 733  GLU   A CB    1 
ATOM   5166  C  CG    . GLU   A  1 735  ? -25.456 93.115  113.151 1.00 35.80 ? 733  GLU   A CG    1 
ATOM   5167  C  CD    . GLU   A  1 735  ? -24.820 94.449  112.833 1.00 40.03 ? 733  GLU   A CD    1 
ATOM   5168  O  OE1   . GLU   A  1 735  ? -23.760 94.452  112.162 1.00 42.98 ? 733  GLU   A OE1   1 
ATOM   5169  O  OE2   . GLU   A  1 735  ? -25.380 95.485  113.249 1.00 50.72 ? 733  GLU   A OE2   1 
ATOM   5170  N  N     . GLU   A  1 736  ? -26.580 89.881  111.005 1.00 22.76 ? 734  GLU   A N     1 
ATOM   5171  C  CA    . GLU   A  1 736  ? -27.812 89.786  110.239 1.00 23.92 ? 734  GLU   A CA    1 
ATOM   5172  C  C     . GLU   A  1 736  ? -28.700 88.629  110.675 1.00 23.50 ? 734  GLU   A C     1 
ATOM   5173  O  O     . GLU   A  1 736  ? -29.913 88.662  110.419 1.00 22.93 ? 734  GLU   A O     1 
ATOM   5174  C  CB    . GLU   A  1 736  ? -27.487 89.648  108.751 1.00 22.52 ? 734  GLU   A CB    1 
ATOM   5175  C  CG    . GLU   A  1 736  ? -26.766 90.860  108.141 1.00 25.87 ? 734  GLU   A CG    1 
ATOM   5176  C  CD    . GLU   A  1 736  ? -25.238 90.797  108.258 1.00 29.70 ? 734  GLU   A CD    1 
ATOM   5177  O  OE1   . GLU   A  1 736  ? -24.712 90.003  109.064 1.00 25.07 ? 734  GLU   A OE1   1 
ATOM   5178  O  OE2   . GLU   A  1 736  ? -24.562 91.554  107.532 1.00 36.30 ? 734  GLU   A OE2   1 
ATOM   5179  N  N     . THR   A  1 737  ? -28.143 87.600  111.317 1.00 19.48 ? 735  THR   A N     1 
ATOM   5180  C  CA    . THR   A  1 737  ? -28.869 86.345  111.535 1.00 20.82 ? 735  THR   A CA    1 
ATOM   5181  C  C     . THR   A  1 737  ? -28.676 85.819  112.954 1.00 20.83 ? 735  THR   A C     1 
ATOM   5182  O  O     . THR   A  1 737  ? -28.295 84.664  113.150 1.00 21.69 ? 735  THR   A O     1 
ATOM   5183  C  CB    . THR   A  1 737  ? -28.424 85.300  110.514 1.00 21.37 ? 735  THR   A CB    1 
ATOM   5184  O  OG1   . THR   A  1 737  ? -27.002 85.111  110.620 1.00 20.92 ? 735  THR   A OG1   1 
ATOM   5185  C  CG2   . THR   A  1 737  ? -28.763 85.763  109.116 1.00 20.82 ? 735  THR   A CG2   1 
ATOM   5186  N  N     . PRO   A  1 738  ? -28.994 86.628  113.975 1.00 20.03 ? 736  PRO   A N     1 
ATOM   5187  C  CA    . PRO   A  1 738  ? -28.811 86.161  115.361 1.00 20.26 ? 736  PRO   A CA    1 
ATOM   5188  C  C     . PRO   A  1 738  ? -29.884 85.203  115.850 1.00 22.47 ? 736  PRO   A C     1 
ATOM   5189  O  O     . PRO   A  1 738  ? -29.619 84.447  116.794 1.00 21.24 ? 736  PRO   A O     1 
ATOM   5190  C  CB    . PRO   A  1 738  ? -28.861 87.462  116.167 1.00 21.84 ? 736  PRO   A CB    1 
ATOM   5191  C  CG    . PRO   A  1 738  ? -29.838 88.277  115.407 1.00 19.70 ? 736  PRO   A CG    1 
ATOM   5192  C  CD    . PRO   A  1 738  ? -29.547 87.992  113.944 1.00 20.28 ? 736  PRO   A CD    1 
ATOM   5193  N  N     . LEU   A  1 739  ? -31.082 85.216  115.262 1.00 19.14 ? 737  LEU   A N     1 
ATOM   5194  C  CA    . LEU   A  1 739  ? -32.189 84.466  115.854 1.00 19.23 ? 737  LEU   A CA    1 
ATOM   5195  C  C     . LEU   A  1 739  ? -31.969 82.969  115.721 1.00 20.47 ? 737  LEU   A C     1 
ATOM   5196  O  O     . LEU   A  1 739  ? -32.105 82.224  116.697 1.00 21.02 ? 737  LEU   A O     1 
ATOM   5197  C  CB    . LEU   A  1 739  ? -33.511 84.875  115.203 1.00 19.72 ? 737  LEU   A CB    1 
ATOM   5198  C  CG    . LEU   A  1 739  ? -33.825 86.363  115.330 1.00 20.11 ? 737  LEU   A CG    1 
ATOM   5199  C  CD1   . LEU   A  1 739  ? -35.067 86.680  114.532 1.00 19.58 ? 737  LEU   A CD1   1 
ATOM   5200  C  CD2   . LEU   A  1 739  ? -33.981 86.788  116.792 1.00 20.45 ? 737  LEU   A CD2   1 
ATOM   5201  N  N     . ILE   A  1 740  ? -31.619 82.507  114.521 1.00 19.53 ? 738  ILE   A N     1 
ATOM   5202  C  CA    . ILE   A  1 740  ? -31.375 81.079  114.357 1.00 19.16 ? 738  ILE   A CA    1 
ATOM   5203  C  C     . ILE   A  1 740  ? -30.150 80.650  115.160 1.00 19.63 ? 738  ILE   A C     1 
ATOM   5204  O  O     . ILE   A  1 740  ? -30.093 79.521  115.657 1.00 18.82 ? 738  ILE   A O     1 
ATOM   5205  C  CB    . ILE   A  1 740  ? -31.252 80.734  112.858 1.00 22.13 ? 738  ILE   A CB    1 
ATOM   5206  C  CG1   . ILE   A  1 740  ? -31.146 79.222  112.651 1.00 21.19 ? 738  ILE   A CG1   1 
ATOM   5207  C  CG2   . ILE   A  1 740  ? -30.067 81.468  112.231 1.00 20.70 ? 738  ILE   A CG2   1 
ATOM   5208  C  CD1   . ILE   A  1 740  ? -32.422 78.450  113.013 1.00 20.64 ? 738  ILE   A CD1   1 
ATOM   5209  N  N     . ALA   A  1 741  ? -29.173 81.547  115.335 1.00 19.93 ? 739  ALA   A N     1 
ATOM   5210  C  CA    . ALA   A  1 741  ? -28.036 81.255  116.198 1.00 19.81 ? 739  ALA   A CA    1 
ATOM   5211  C  C     . ALA   A  1 741  ? -28.483 81.033  117.636 1.00 21.07 ? 739  ALA   A C     1 
ATOM   5212  O  O     . ALA   A  1 741  ? -28.059 80.071  118.288 1.00 20.28 ? 739  ALA   A O     1 
ATOM   5213  C  CB    . ALA   A  1 741  ? -27.020 82.391  116.126 1.00 20.15 ? 739  ALA   A CB    1 
ATOM   5214  N  N     . ALA   A  1 742  ? -29.341 81.923  118.149 1.00 20.25 ? 740  ALA   A N     1 
ATOM   5215  C  CA    . ALA   A  1 742  ? -29.850 81.770  119.507 1.00 19.55 ? 740  ALA   A CA    1 
ATOM   5216  C  C     . ALA   A  1 742  ? -30.616 80.466  119.658 1.00 19.94 ? 740  ALA   A C     1 
ATOM   5217  O  O     . ALA   A  1 742  ? -30.533 79.801  120.695 1.00 22.82 ? 740  ALA   A O     1 
ATOM   5218  C  CB    . ALA   A  1 742  ? -30.752 82.956  119.865 1.00 22.26 ? 740  ALA   A CB    1 
ATOM   5219  N  N     . GLU   A  1 743  ? -31.399 80.106  118.640 1.00 19.39 ? 741  GLU   A N     1 
ATOM   5220  C  CA    . GLU   A  1 743  ? -32.111 78.836  118.672 1.00 20.68 ? 741  GLU   A CA    1 
ATOM   5221  C  C     . GLU   A  1 743  ? -31.145 77.656  118.630 1.00 21.84 ? 741  GLU   A C     1 
ATOM   5222  O  O     . GLU   A  1 743  ? -31.359 76.650  119.312 1.00 19.86 ? 741  GLU   A O     1 
ATOM   5223  C  CB    . GLU   A  1 743  ? -33.104 78.783  117.510 1.00 20.49 ? 741  GLU   A CB    1 
ATOM   5224  C  CG    . GLU   A  1 743  ? -33.867 77.477  117.384 1.00 24.03 ? 741  GLU   A CG    1 
ATOM   5225  C  CD    . GLU   A  1 743  ? -34.805 77.177  118.544 1.00 26.02 ? 741  GLU   A CD    1 
ATOM   5226  O  OE1   . GLU   A  1 743  ? -35.016 78.043  119.425 1.00 27.12 ? 741  GLU   A OE1   1 
ATOM   5227  O  OE2   . GLU   A  1 743  ? -35.324 76.043  118.574 1.00 30.52 ? 741  GLU   A OE2   1 
ATOM   5228  N  N     . GLY   A  1 744  ? -30.074 77.759  117.841 1.00 21.17 ? 742  GLY   A N     1 
ATOM   5229  C  CA    . GLY   A  1 744  ? -29.059 76.715  117.864 1.00 19.10 ? 742  GLY   A CA    1 
ATOM   5230  C  C     . GLY   A  1 744  ? -28.415 76.569  119.233 1.00 18.79 ? 742  GLY   A C     1 
ATOM   5231  O  O     . GLY   A  1 744  ? -28.223 75.453  119.725 1.00 20.23 ? 742  GLY   A O     1 
ATOM   5232  N  N     . VAL   A  1 745  ? -28.081 77.694  119.870 1.00 20.20 ? 743  VAL   A N     1 
ATOM   5233  C  CA    . VAL   A  1 745  ? -27.518 77.639  121.219 1.00 20.41 ? 743  VAL   A CA    1 
ATOM   5234  C  C     . VAL   A  1 745  ? -28.534 77.071  122.199 1.00 20.57 ? 743  VAL   A C     1 
ATOM   5235  O  O     . VAL   A  1 745  ? -28.190 76.260  123.066 1.00 21.03 ? 743  VAL   A O     1 
ATOM   5236  C  CB    . VAL   A  1 745  ? -27.018 79.029  121.659 1.00 21.62 ? 743  VAL   A CB    1 
ATOM   5237  C  CG1   . VAL   A  1 745  ? -26.759 79.063  123.173 1.00 21.72 ? 743  VAL   A CG1   1 
ATOM   5238  C  CG2   . VAL   A  1 745  ? -25.751 79.397  120.892 1.00 20.49 ? 743  VAL   A CG2   1 
ATOM   5239  N  N     . ARG   A  1 746  ? -29.797 77.493  122.086 1.00 21.89 ? 744  ARG   A N     1 
ATOM   5240  C  CA    . ARG   A  1 746  ? -30.834 76.921  122.941 1.00 22.42 ? 744  ARG   A CA    1 
ATOM   5241  C  C     . ARG   A  1 746  ? -30.884 75.403  122.799 1.00 21.70 ? 744  ARG   A C     1 
ATOM   5242  O  O     . ARG   A  1 746  ? -30.968 74.683  123.799 1.00 24.37 ? 744  ARG   A O     1 
ATOM   5243  C  CB    . ARG   A  1 746  ? -32.195 77.538  122.606 1.00 24.23 ? 744  ARG   A CB    1 
ATOM   5244  C  CG    . ARG   A  1 746  ? -33.273 77.225  123.626 1.00 28.35 ? 744  ARG   A CG    1 
ATOM   5245  C  CD    . ARG   A  1 746  ? -34.691 77.465  123.059 1.00 28.39 ? 744  ARG   A CD    1 
ATOM   5246  N  NE    . ARG   A  1 746  ? -34.978 76.583  121.929 1.00 29.26 ? 744  ARG   A NE    1 
ATOM   5247  C  CZ    . ARG   A  1 746  ? -35.291 75.298  122.046 1.00 31.63 ? 744  ARG   A CZ    1 
ATOM   5248  N  NH1   . ARG   A  1 746  ? -35.363 74.709  123.233 1.00 34.35 ? 744  ARG   A NH1   1 
ATOM   5249  N  NH2   . ARG   A  1 746  ? -35.532 74.583  120.948 1.00 29.40 ? 744  ARG   A NH2   1 
ATOM   5250  N  N     . ILE   A  1 747  ? -30.788 74.901  121.565 1.00 22.29 ? 745  ILE   A N     1 
ATOM   5251  C  CA    . ILE   A  1 747  ? -30.846 73.459  121.321 1.00 19.99 ? 745  ILE   A CA    1 
ATOM   5252  C  C     . ILE   A  1 747  ? -29.620 72.758  121.896 1.00 20.60 ? 745  ILE   A C     1 
ATOM   5253  O  O     . ILE   A  1 747  ? -29.735 71.719  122.558 1.00 19.55 ? 745  ILE   A O     1 
ATOM   5254  C  CB    . ILE   A  1 747  ? -31.000 73.188  119.815 1.00 23.02 ? 745  ILE   A CB    1 
ATOM   5255  C  CG1   . ILE   A  1 747  ? -32.441 73.497  119.387 1.00 23.79 ? 745  ILE   A CG1   1 
ATOM   5256  C  CG2   . ILE   A  1 747  ? -30.574 71.752  119.473 1.00 21.45 ? 745  ILE   A CG2   1 
ATOM   5257  C  CD1   . ILE   A  1 747  ? -32.643 73.533  117.887 1.00 22.33 ? 745  ILE   A CD1   1 
ATOM   5258  N  N     . LEU   A  1 748  ? -28.426 73.316  121.654 1.00 19.50 ? 746  LEU   A N     1 
ATOM   5259  C  CA    . LEU   A  1 748  ? -27.210 72.719  122.209 1.00 19.68 ? 746  LEU   A CA    1 
ATOM   5260  C  C     . LEU   A  1 748  ? -27.224 72.718  123.730 1.00 23.85 ? 746  LEU   A C     1 
ATOM   5261  O  O     . LEU   A  1 748  ? -26.780 71.752  124.364 1.00 21.87 ? 746  LEU   A O     1 
ATOM   5262  C  CB    . LEU   A  1 748  ? -25.978 73.458  121.702 1.00 19.72 ? 746  LEU   A CB    1 
ATOM   5263  C  CG    . LEU   A  1 748  ? -25.538 73.066  120.294 1.00 24.26 ? 746  LEU   A CG    1 
ATOM   5264  C  CD1   . LEU   A  1 748  ? -24.619 74.138  119.713 1.00 26.44 ? 746  LEU   A CD1   1 
ATOM   5265  C  CD2   . LEU   A  1 748  ? -24.809 71.742  120.342 1.00 23.95 ? 746  LEU   A CD2   1 
ATOM   5266  N  N     . ARG   A  1 749  ? -27.701 73.799  124.339 1.00 21.93 ? 747  ARG   A N     1 
ATOM   5267  C  CA    . ARG   A  1 749  ? -27.826 73.792  125.790 1.00 22.94 ? 747  ARG   A CA    1 
ATOM   5268  C  C     . ARG   A  1 749  ? -28.856 72.763  126.245 1.00 25.90 ? 747  ARG   A C     1 
ATOM   5269  O  O     . ARG   A  1 749  ? -28.623 72.034  127.214 1.00 23.83 ? 747  ARG   A O     1 
ATOM   5270  C  CB    . ARG   A  1 749  ? -28.170 75.191  126.303 1.00 23.41 ? 747  ARG   A CB    1 
ATOM   5271  C  CG    . ARG   A  1 749  ? -26.952 76.104  126.390 1.00 26.74 ? 747  ARG   A CG    1 
ATOM   5272  C  CD    . ARG   A  1 749  ? -27.342 77.480  126.845 1.00 28.99 ? 747  ARG   A CD    1 
ATOM   5273  N  NE    . ARG   A  1 749  ? -26.201 78.380  126.969 1.00 25.76 ? 747  ARG   A NE    1 
ATOM   5274  C  CZ    . ARG   A  1 749  ? -26.271 79.564  127.563 1.00 27.72 ? 747  ARG   A CZ    1 
ATOM   5275  N  NH1   . ARG   A  1 749  ? -27.407 80.007  128.073 1.00 28.86 ? 747  ARG   A NH1   1 
ATOM   5276  N  NH2   . ARG   A  1 749  ? -25.174 80.319  127.651 1.00 25.59 ? 747  ARG   A NH2   1 
ATOM   5277  N  N     . GLU   A  1 750  ? -29.992 72.669  125.551 1.00 22.52 ? 748  GLU   A N     1 
ATOM   5278  C  CA    . GLU   A  1 750  ? -30.973 71.647  125.916 1.00 23.80 ? 748  GLU   A CA    1 
ATOM   5279  C  C     . GLU   A  1 750  ? -30.370 70.249  125.813 1.00 24.90 ? 748  GLU   A C     1 
ATOM   5280  O  O     . GLU   A  1 750  ? -30.649 69.371  126.641 1.00 23.79 ? 748  GLU   A O     1 
ATOM   5281  C  CB    . GLU   A  1 750  ? -32.214 71.759  125.034 1.00 21.93 ? 748  GLU   A CB    1 
ATOM   5282  C  CG    . GLU   A  1 750  ? -33.277 70.739  125.398 1.00 25.48 ? 748  GLU   A CG    1 
ATOM   5283  C  CD    . GLU   A  1 750  ? -34.472 70.757  124.464 1.00 26.79 ? 748  GLU   A CD    1 
ATOM   5284  O  OE1   . GLU   A  1 750  ? -34.652 71.749  123.731 1.00 36.12 ? 748  GLU   A OE1   1 
ATOM   5285  O  OE2   . GLU   A  1 750  ? -35.218 69.761  124.448 1.00 31.07 ? 748  GLU   A OE2   1 
ATOM   5286  N  N     . ALA   A  1 751  ? -29.501 70.042  124.831 1.00 22.68 ? 749  ALA   A N     1 
ATOM   5287  C  CA    . ALA   A  1 751  ? -28.832 68.763  124.640 1.00 22.95 ? 749  ALA   A CA    1 
ATOM   5288  C  C     . ALA   A  1 751  ? -27.796 68.459  125.713 1.00 23.01 ? 749  ALA   A C     1 
ATOM   5289  O  O     . ALA   A  1 751  ? -27.248 67.354  125.714 1.00 21.88 ? 749  ALA   A O     1 
ATOM   5290  C  CB    . ALA   A  1 751  ? -28.166 68.739  123.267 1.00 21.89 ? 749  ALA   A CB    1 
ATOM   5291  N  N     . GLY   A  1 752  ? -27.497 69.401  126.603 1.00 21.27 ? 750  GLY   A N     1 
ATOM   5292  C  CA    . GLY   A  1 752  ? -26.572 69.149  127.692 1.00 23.46 ? 750  GLY   A CA    1 
ATOM   5293  C  C     . GLY   A  1 752  ? -25.310 69.992  127.687 1.00 25.21 ? 750  GLY   A C     1 
ATOM   5294  O  O     . GLY   A  1 752  ? -24.525 69.883  128.637 1.00 24.69 ? 750  GLY   A O     1 
ATOM   5295  N  N     . ILE   A  1 753  ? -25.049 70.824  126.681 1.00 20.46 ? 751  ILE   A N     1 
ATOM   5296  C  CA    . ILE   A  1 753  ? -23.906 71.736  126.757 1.00 24.12 ? 751  ILE   A CA    1 
ATOM   5297  C  C     . ILE   A  1 753  ? -24.154 72.746  127.869 1.00 22.15 ? 751  ILE   A C     1 
ATOM   5298  O  O     . ILE   A  1 753  ? -25.128 73.504  127.802 1.00 24.26 ? 751  ILE   A O     1 
ATOM   5299  C  CB    . ILE   A  1 753  ? -23.652 72.483  125.439 1.00 23.71 ? 751  ILE   A CB    1 
ATOM   5300  C  CG1   . ILE   A  1 753  ? -23.486 71.516  124.264 1.00 22.31 ? 751  ILE   A CG1   1 
ATOM   5301  C  CG2   . ILE   A  1 753  ? -22.423 73.382  125.599 1.00 22.50 ? 751  ILE   A CG2   1 
ATOM   5302  C  CD1   . ILE   A  1 753  ? -22.244 70.630  124.354 1.00 19.58 ? 751  ILE   A CD1   1 
ATOM   5303  N  N     . PRO   A  1 754  ? -23.300 72.808  128.887 1.00 24.10 ? 752  PRO   A N     1 
ATOM   5304  C  CA    . PRO   A  1 754  ? -23.506 73.776  129.972 1.00 25.56 ? 752  PRO   A CA    1 
ATOM   5305  C  C     . PRO   A  1 754  ? -23.443 75.210  129.469 1.00 26.11 ? 752  PRO   A C     1 
ATOM   5306  O  O     . PRO   A  1 754  ? -22.756 75.523  128.492 1.00 21.42 ? 752  PRO   A O     1 
ATOM   5307  C  CB    . PRO   A  1 754  ? -22.351 73.479  130.936 1.00 28.32 ? 752  PRO   A CB    1 
ATOM   5308  C  CG    . PRO   A  1 754  ? -21.925 72.086  130.619 1.00 29.49 ? 752  PRO   A CG    1 
ATOM   5309  C  CD    . PRO   A  1 754  ? -22.163 71.912  129.146 1.00 25.09 ? 752  PRO   A CD    1 
ATOM   5310  N  N     . ALA   A  1 755  ? -24.156 76.093  130.178 1.00 26.29 ? 753  ALA   A N     1 
ATOM   5311  C  CA    . ALA   A  1 755  ? -24.169 77.508  129.819 1.00 25.45 ? 753  ALA   A CA    1 
ATOM   5312  C  C     . ALA   A  1 755  ? -22.762 78.093  129.805 1.00 25.56 ? 753  ALA   A C     1 
ATOM   5313  O  O     . ALA   A  1 755  ? -22.443 78.953  128.976 1.00 26.84 ? 753  ALA   A O     1 
ATOM   5314  C  CB    . ALA   A  1 755  ? -25.055 78.284  130.796 1.00 23.27 ? 753  ALA   A CB    1 
ATOM   5315  N  N     . SER   A  1 756  ? -21.908 77.645  130.720 1.00 24.68 ? 754  SER   A N     1 
ATOM   5316  C  CA    . SER   A  1 756  ? -20.554 78.169  130.776 1.00 24.84 ? 754  SER   A CA    1 
ATOM   5317  C  C     . SER   A  1 756  ? -19.702 77.680  129.611 1.00 24.68 ? 754  SER   A C     1 
ATOM   5318  O  O     . SER   A  1 756  ? -18.713 78.334  129.261 1.00 27.38 ? 754  SER   A O     1 
ATOM   5319  C  CB    . SER   A  1 756  ? -19.919 77.786  132.106 1.00 26.12 ? 754  SER   A CB    1 
ATOM   5320  O  OG    . SER   A  1 756  ? -19.826 76.376  132.207 1.00 30.25 ? 754  SER   A OG    1 
ATOM   5321  N  N     . ALA   A  1 757  ? -20.067 76.566  128.987 1.00 22.18 ? 755  ALA   A N     1 
ATOM   5322  C  CA    . ALA   A  1 757  ? -19.304 76.069  127.851 1.00 21.16 ? 755  ALA   A CA    1 
ATOM   5323  C  C     . ALA   A  1 757  ? -19.759 76.659  126.522 1.00 20.81 ? 755  ALA   A C     1 
ATOM   5324  O  O     . ALA   A  1 757  ? -19.024 76.565  125.536 1.00 20.13 ? 755  ALA   A O     1 
ATOM   5325  C  CB    . ALA   A  1 757  ? -19.383 74.539  127.784 1.00 23.45 ? 755  ALA   A CB    1 
ATOM   5326  N  N     . LEU   A  1 758  ? -20.943 77.265  126.466 1.00 21.11 ? 756  LEU   A N     1 
ATOM   5327  C  CA    . LEU   A  1 758  ? -21.470 77.804  125.213 1.00 22.55 ? 756  LEU   A CA    1 
ATOM   5328  C  C     . LEU   A  1 758  ? -22.190 79.109  125.514 1.00 22.62 ? 756  LEU   A C     1 
ATOM   5329  O  O     . LEU   A  1 758  ? -23.323 79.108  126.007 1.00 22.48 ? 756  LEU   A O     1 
ATOM   5330  C  CB    . LEU   A  1 758  ? -22.403 76.819  124.532 1.00 21.86 ? 756  LEU   A CB    1 
ATOM   5331  C  CG    . LEU   A  1 758  ? -23.027 77.352  123.248 1.00 21.15 ? 756  LEU   A CG    1 
ATOM   5332  C  CD1   . LEU   A  1 758  ? -21.937 77.896  122.294 1.00 20.45 ? 756  LEU   A CD1   1 
ATOM   5333  C  CD2   . LEU   A  1 758  ? -23.796 76.238  122.589 1.00 25.14 ? 756  LEU   A CD2   1 
ATOM   5334  N  N     . GLN   A  1 759  ? -21.534 80.215  125.206 1.00 20.50 ? 757  GLN   A N     1 
ATOM   5335  C  CA    . GLN   A  1 759  ? -22.100 81.529  125.432 1.00 22.35 ? 757  GLN   A CA    1 
ATOM   5336  C  C     . GLN   A  1 759  ? -22.387 82.171  124.090 1.00 21.47 ? 757  GLN   A C     1 
ATOM   5337  O  O     . GLN   A  1 759  ? -21.579 82.062  123.160 1.00 22.49 ? 757  GLN   A O     1 
ATOM   5338  C  CB    . GLN   A  1 759  ? -21.149 82.399  126.253 1.00 24.61 ? 757  GLN   A CB    1 
ATOM   5339  C  CG    . GLN   A  1 759  ? -20.953 81.890  127.656 1.00 22.13 ? 757  GLN   A CG    1 
ATOM   5340  C  CD    . GLN   A  1 759  ? -19.904 82.684  128.402 1.00 21.77 ? 757  GLN   A CD    1 
ATOM   5341  O  OE1   . GLN   A  1 759  ? -20.226 83.649  129.091 1.00 25.45 ? 757  GLN   A OE1   1 
ATOM   5342  N  NE2   . GLN   A  1 759  ? -18.639 82.292  128.252 1.00 21.68 ? 757  GLN   A NE2   1 
ATOM   5343  N  N     . LEU   A  1 760  ? -23.543 82.818  123.990 1.00 21.07 ? 758  LEU   A N     1 
ATOM   5344  C  CA    . LEU   A  1 760  ? -23.975 83.454  122.752 1.00 23.89 ? 758  LEU   A CA    1 
ATOM   5345  C  C     . LEU   A  1 760  ? -23.798 84.957  122.886 1.00 20.63 ? 758  LEU   A C     1 
ATOM   5346  O  O     . LEU   A  1 760  ? -24.288 85.556  123.846 1.00 22.40 ? 758  LEU   A O     1 
ATOM   5347  C  CB    . LEU   A  1 760  ? -25.431 83.126  122.430 1.00 20.37 ? 758  LEU   A CB    1 
ATOM   5348  C  CG    . LEU   A  1 760  ? -25.928 83.775  121.122 1.00 20.05 ? 758  LEU   A CG    1 
ATOM   5349  C  CD1   . LEU   A  1 760  ? -25.462 83.000  119.878 1.00 21.29 ? 758  LEU   A CD1   1 
ATOM   5350  C  CD2   . LEU   A  1 760  ? -27.436 83.925  121.149 1.00 21.95 ? 758  LEU   A CD2   1 
ATOM   5351  N  N     . LEU   A  1 761  ? -23.089 85.558  121.933 1.00 21.19 ? 759  LEU   A N     1 
ATOM   5352  C  CA    . LEU   A  1 761  ? -22.760 86.983  121.960 1.00 21.99 ? 759  LEU   A CA    1 
ATOM   5353  C  C     . LEU   A  1 761  ? -23.208 87.615  120.653 1.00 21.26 ? 759  LEU   A C     1 
ATOM   5354  O  O     . LEU   A  1 761  ? -22.399 87.802  119.735 1.00 21.36 ? 759  LEU   A O     1 
ATOM   5355  C  CB    . LEU   A  1 761  ? -21.260 87.213  122.164 1.00 20.78 ? 759  LEU   A CB    1 
ATOM   5356  C  CG    . LEU   A  1 761  ? -20.619 86.761  123.482 1.00 23.75 ? 759  LEU   A CG    1 
ATOM   5357  C  CD1   . LEU   A  1 761  ? -21.536 87.035  124.655 1.00 24.04 ? 759  LEU   A CD1   1 
ATOM   5358  C  CD2   . LEU   A  1 761  ? -20.202 85.305  123.445 1.00 26.46 ? 759  LEU   A CD2   1 
ATOM   5359  N  N     . PRO   A  1 762  ? -24.485 87.958  120.529 1.00 23.83 ? 760  PRO   A N     1 
ATOM   5360  C  CA    . PRO   A  1 762  ? -24.944 88.639  119.314 1.00 21.93 ? 760  PRO   A CA    1 
ATOM   5361  C  C     . PRO   A  1 762  ? -24.343 90.034  119.213 1.00 24.94 ? 760  PRO   A C     1 
ATOM   5362  O  O     . PRO   A  1 762  ? -23.997 90.662  120.214 1.00 25.43 ? 760  PRO   A O     1 
ATOM   5363  C  CB    . PRO   A  1 762  ? -26.467 88.708  119.494 1.00 23.16 ? 760  PRO   A CB    1 
ATOM   5364  C  CG    . PRO   A  1 762  ? -26.794 87.747  120.613 1.00 20.70 ? 760  PRO   A CG    1 
ATOM   5365  C  CD    . PRO   A  1 762  ? -25.578 87.735  121.492 1.00 21.79 ? 760  PRO   A CD    1 
ATOM   5366  N  N     . GLY   A  1 763  ? -24.208 90.517  117.992 1.00 23.72 ? 761  GLY   A N     1 
ATOM   5367  C  CA    . GLY   A  1 763  ? -23.736 91.867  117.780 1.00 26.59 ? 761  GLY   A CA    1 
ATOM   5368  C  C     . GLY   A  1 763  ? -22.970 91.987  116.479 1.00 29.17 ? 761  GLY   A C     1 
ATOM   5369  O  O     . GLY   A  1 763  ? -22.926 91.063  115.667 1.00 28.21 ? 761  GLY   A O     1 
ATOM   5370  N  N     . ASP   A  1 764  ? -22.351 93.149  116.310 1.00 31.38 ? 762  ASP   A N     1 
ATOM   5371  C  CA    . ASP   A  1 764  ? -21.659 93.476  115.074 1.00 33.18 ? 762  ASP   A CA    1 
ATOM   5372  C  C     . ASP   A  1 764  ? -20.180 93.111  115.199 1.00 38.35 ? 762  ASP   A C     1 
ATOM   5373  O  O     . ASP   A  1 764  ? -19.787 92.318  116.061 1.00 32.38 ? 762  ASP   A O     1 
ATOM   5374  C  CB    . ASP   A  1 764  ? -21.888 94.953  114.724 1.00 37.27 ? 762  ASP   A CB    1 
ATOM   5375  C  CG    . ASP   A  1 764  ? -21.463 95.902  115.828 1.00 38.70 ? 762  ASP   A CG    1 
ATOM   5376  O  OD1   . ASP   A  1 764  ? -20.587 95.551  116.649 1.00 39.30 ? 762  ASP   A OD1   1 
ATOM   5377  O  OD2   . ASP   A  1 764  ? -22.018 97.016  115.874 1.00 42.60 ? 762  ASP   A OD2   1 
ATOM   5378  N  N     . GLY   A  1 765  ? -19.348 93.681  114.326 1.00 36.13 ? 763  GLY   A N     1 
ATOM   5379  C  CA    . GLY   A  1 765  ? -17.943 93.332  114.319 1.00 34.50 ? 763  GLY   A CA    1 
ATOM   5380  C  C     . GLY   A  1 765  ? -17.204 93.803  115.551 1.00 30.59 ? 763  GLY   A C     1 
ATOM   5381  O  O     . GLY   A  1 765  ? -16.172 93.236  115.908 1.00 36.29 ? 763  GLY   A O     1 
ATOM   5382  N  N     . ARG   A  1 766  ? -17.704 94.849  116.210 1.00 29.41 ? 764  ARG   A N     1 
ATOM   5383  C  CA    . ARG   A  1 766  ? -17.100 95.269  117.470 1.00 34.78 ? 764  ARG   A CA    1 
ATOM   5384  C  C     . ARG   A  1 766  ? -17.126 94.132  118.482 1.00 30.74 ? 764  ARG   A C     1 
ATOM   5385  O  O     . ARG   A  1 766  ? -16.159 93.928  119.222 1.00 26.91 ? 764  ARG   A O     1 
ATOM   5386  C  CB    . ARG   A  1 766  ? -17.817 96.507  118.019 1.00 32.57 ? 764  ARG   A CB    1 
ATOM   5387  N  N     . VAL   A  1 767  ? -18.217 93.361  118.511 1.00 30.02 ? 765  VAL   A N     1 
ATOM   5388  C  CA    . VAL   A  1 767  ? -18.275 92.217  119.413 1.00 28.01 ? 765  VAL   A CA    1 
ATOM   5389  C  C     . VAL   A  1 767  ? -17.269 91.159  118.987 1.00 24.28 ? 765  VAL   A C     1 
ATOM   5390  O  O     . VAL   A  1 767  ? -16.537 90.612  119.820 1.00 28.83 ? 765  VAL   A O     1 
ATOM   5391  C  CB    . VAL   A  1 767  ? -19.705 91.654  119.486 1.00 28.32 ? 765  VAL   A CB    1 
ATOM   5392  C  CG1   . VAL   A  1 767  ? -19.749 90.423  120.386 1.00 24.42 ? 765  VAL   A CG1   1 
ATOM   5393  C  CG2   . VAL   A  1 767  ? -20.659 92.729  120.007 1.00 27.64 ? 765  VAL   A CG2   1 
ATOM   5394  N  N     . GLY   A  1 768  ? -17.207 90.860  117.689 1.00 24.40 ? 766  GLY   A N     1 
ATOM   5395  C  CA    . GLY   A  1 768  ? -16.231 89.897  117.208 1.00 25.00 ? 766  GLY   A CA    1 
ATOM   5396  C  C     . GLY   A  1 768  ? -14.809 90.319  117.521 1.00 25.57 ? 766  GLY   A C     1 
ATOM   5397  O  O     . GLY   A  1 768  ? -13.996 89.508  117.967 1.00 23.26 ? 766  GLY   A O     1 
ATOM   5398  N  N     . ALA   A  1 769  ? -14.504 91.603  117.319 1.00 24.29 ? 767  ALA   A N     1 
ATOM   5399  C  CA    . ALA   A  1 769  ? -13.156 92.107  117.566 1.00 25.16 ? 767  ALA   A CA    1 
ATOM   5400  C  C     . ALA   A  1 769  ? -12.800 92.014  119.044 1.00 28.16 ? 767  ALA   A C     1 
ATOM   5401  O  O     . ALA   A  1 769  ? -11.679 91.634  119.402 1.00 26.43 ? 767  ALA   A O     1 
ATOM   5402  C  CB    . ALA   A  1 769  ? -13.043 93.550  117.073 1.00 24.98 ? 767  ALA   A CB    1 
ATOM   5403  N  N     . ALA   A  1 770  ? -13.743 92.355  119.918 1.00 26.51 ? 768  ALA   A N     1 
ATOM   5404  C  CA    . ALA   A  1 770  ? -13.490 92.232  121.347 1.00 28.21 ? 768  ALA   A CA    1 
ATOM   5405  C  C     . ALA   A  1 770  ? -13.191 90.787  121.728 1.00 27.38 ? 768  ALA   A C     1 
ATOM   5406  O  O     . ALA   A  1 770  ? -12.300 90.522  122.540 1.00 24.74 ? 768  ALA   A O     1 
ATOM   5407  C  CB    . ALA   A  1 770  ? -14.688 92.765  122.136 1.00 27.16 ? 768  ALA   A CB    1 
ATOM   5408  N  N     . LEU   A  1 771  ? -13.922 89.835  121.147 1.00 24.30 ? 769  LEU   A N     1 
ATOM   5409  C  CA    . LEU   A  1 771  ? -13.700 88.431  121.473 1.00 27.40 ? 769  LEU   A CA    1 
ATOM   5410  C  C     . LEU   A  1 771  ? -12.326 87.976  121.014 1.00 22.77 ? 769  LEU   A C     1 
ATOM   5411  O  O     . LEU   A  1 771  ? -11.583 87.343  121.770 1.00 27.05 ? 769  LEU   A O     1 
ATOM   5412  C  CB    . LEU   A  1 771  ? -14.789 87.571  120.830 1.00 23.00 ? 769  LEU   A CB    1 
ATOM   5413  C  CG    . LEU   A  1 771  ? -16.182 87.782  121.424 1.00 25.51 ? 769  LEU   A CG    1 
ATOM   5414  C  CD1   . LEU   A  1 771  ? -17.211 87.061  120.579 1.00 23.74 ? 769  LEU   A CD1   1 
ATOM   5415  C  CD2   . LEU   A  1 771  ? -16.229 87.300  122.869 1.00 22.40 ? 769  LEU   A CD2   1 
ATOM   5416  N  N     . VAL   A  1 772  ? -11.978 88.289  119.769 1.00 22.21 ? 770  VAL   A N     1 
ATOM   5417  C  CA    . VAL   A  1 772  ? -10.698 87.869  119.214 1.00 21.35 ? 770  VAL   A CA    1 
ATOM   5418  C  C     . VAL   A  1 772  ? -9.548  88.421  120.046 1.00 23.81 ? 770  VAL   A C     1 
ATOM   5419  O  O     . VAL   A  1 772  ? -8.556  87.727  120.299 1.00 26.09 ? 770  VAL   A O     1 
ATOM   5420  C  CB    . VAL   A  1 772  ? -10.612 88.306  117.738 1.00 21.87 ? 770  VAL   A CB    1 
ATOM   5421  C  CG1   . VAL   A  1 772  ? -9.192  88.174  117.220 1.00 27.17 ? 770  VAL   A CG1   1 
ATOM   5422  C  CG2   . VAL   A  1 772  ? -11.584 87.462  116.900 1.00 22.29 ? 770  VAL   A CG2   1 
ATOM   5423  N  N     . ALA   A  1 773  ? -9.672  89.665  120.502 1.00 25.89 ? 771  ALA   A N     1 
ATOM   5424  C  CA    . ALA   A  1 773  ? -8.595  90.338  121.220 1.00 23.92 ? 771  ALA   A CA    1 
ATOM   5425  C  C     . ALA   A  1 773  ? -8.514  89.947  122.687 1.00 29.65 ? 771  ALA   A C     1 
ATOM   5426  O  O     . ALA   A  1 773  ? -7.557  90.343  123.363 1.00 31.43 ? 771  ALA   A O     1 
ATOM   5427  C  CB    . ALA   A  1 773  ? -8.756  91.857  121.125 1.00 29.58 ? 771  ALA   A CB    1 
ATOM   5428  N  N     . ALA   A  1 774  ? -9.479  89.196  123.203 1.00 29.34 ? 772  ALA   A N     1 
ATOM   5429  C  CA    . ALA   A  1 774  ? -9.466  88.887  124.626 1.00 27.87 ? 772  ALA   A CA    1 
ATOM   5430  C  C     . ALA   A  1 774  ? -8.274  87.998  124.955 1.00 26.96 ? 772  ALA   A C     1 
ATOM   5431  O  O     . ALA   A  1 774  ? -7.955  87.057  124.222 1.00 27.42 ? 772  ALA   A O     1 
ATOM   5432  C  CB    . ALA   A  1 774  ? -10.775 88.224  125.050 1.00 24.89 ? 772  ALA   A CB    1 
ATOM   5433  N  N     . ALA   A  1 775  ? -7.611  88.316  126.072 1.00 30.12 ? 773  ALA   A N     1 
ATOM   5434  C  CA    . ALA   A  1 775  ? -6.363  87.649  126.421 1.00 31.56 ? 773  ALA   A CA    1 
ATOM   5435  C  C     . ALA   A  1 775  ? -6.538  86.141  126.525 1.00 29.73 ? 773  ALA   A C     1 
ATOM   5436  O  O     . ALA   A  1 775  ? -5.640  85.383  126.147 1.00 32.47 ? 773  ALA   A O     1 
ATOM   5437  C  CB    . ALA   A  1 775  ? -5.813  88.215  127.732 1.00 33.43 ? 773  ALA   A CB    1 
ATOM   5438  N  N     . GLU   A  1 776  ? -7.687  85.678  127.012 1.00 24.78 ? 774  GLU   A N     1 
ATOM   5439  C  CA    . GLU   A  1 776  ? -7.850  84.249  127.228 1.00 24.67 ? 774  GLU   A CA    1 
ATOM   5440  C  C     . GLU   A  1 776  ? -8.428  83.523  126.023 1.00 25.09 ? 774  GLU   A C     1 
ATOM   5441  O  O     . GLU   A  1 776  ? -8.677  82.313  126.097 1.00 24.67 ? 774  GLU   A O     1 
ATOM   5442  C  CB    . GLU   A  1 776  ? -8.692  84.004  128.470 1.00 29.76 ? 774  GLU   A CB    1 
ATOM   5443  C  CG    . GLU   A  1 776  ? -7.835  84.130  129.723 1.00 34.16 ? 774  GLU   A CG    1 
ATOM   5444  C  CD    . GLU   A  1 776  ? -8.607  84.579  130.922 1.00 42.12 ? 774  GLU   A CD    1 
ATOM   5445  O  OE1   . GLU   A  1 776  ? -9.495  85.447  130.766 1.00 39.77 ? 774  GLU   A OE1   1 
ATOM   5446  O  OE2   . GLU   A  1 776  ? -8.318  84.060  132.021 1.00 50.72 ? 774  GLU   A OE2   1 
ATOM   5447  N  N     . THR   A  1 777  ? -8.604  84.217  124.907 1.00 21.91 ? 775  THR   A N     1 
ATOM   5448  C  CA    . THR   A  1 777  ? -9.044  83.552  123.691 1.00 24.94 ? 775  THR   A CA    1 
ATOM   5449  C  C     . THR   A  1 777  ? -7.938  82.634  123.191 1.00 22.46 ? 775  THR   A C     1 
ATOM   5450  O  O     . THR   A  1 777  ? -6.816  83.079  122.930 1.00 23.40 ? 775  THR   A O     1 
ATOM   5451  C  CB    . THR   A  1 777  ? -9.424  84.589  122.643 1.00 23.73 ? 775  THR   A CB    1 
ATOM   5452  O  OG1   . THR   A  1 777  ? -10.607 85.251  123.084 1.00 25.01 ? 775  THR   A OG1   1 
ATOM   5453  C  CG2   . THR   A  1 777  ? -9.672  83.936  121.292 1.00 22.62 ? 775  THR   A CG2   1 
ATOM   5454  N  N     . ALA   A  1 778  ? -8.238  81.348  123.097 1.00 20.15 ? 776  ALA   A N     1 
ATOM   5455  C  CA    . ALA   A  1 778  ? -7.210  80.361  122.796 1.00 20.00 ? 776  ALA   A CA    1 
ATOM   5456  C  C     . ALA   A  1 778  ? -7.272  79.867  121.363 1.00 20.35 ? 776  ALA   A C     1 
ATOM   5457  O  O     . ALA   A  1 778  ? -6.367  79.154  120.924 1.00 23.82 ? 776  ALA   A O     1 
ATOM   5458  C  CB    . ALA   A  1 778  ? -7.321  79.177  123.765 1.00 21.39 ? 776  ALA   A CB    1 
ATOM   5459  N  N     . GLY   A  1 779  ? -8.302  80.239  120.624 1.00 20.84 ? 777  GLY   A N     1 
ATOM   5460  C  CA    . GLY   A  1 779  ? -8.439  79.813  119.248 1.00 19.23 ? 777  GLY   A CA    1 
ATOM   5461  C  C     . GLY   A  1 779  ? -9.592  80.562  118.628 1.00 19.50 ? 777  GLY   A C     1 
ATOM   5462  O  O     . GLY   A  1 779  ? -10.512 80.990  119.334 1.00 20.08 ? 777  GLY   A O     1 
ATOM   5463  N  N     . VAL   A  1 780  ? -9.556  80.757  117.317 1.00 19.54 ? 778  VAL   A N     1 
ATOM   5464  C  CA    . VAL   A  1 780  ? -10.627 81.446  116.616 1.00 19.50 ? 778  VAL   A CA    1 
ATOM   5465  C  C     . VAL   A  1 780  ? -11.015 80.604  115.420 1.00 19.06 ? 778  VAL   A C     1 
ATOM   5466  O  O     . VAL   A  1 780  ? -10.148 80.156  114.661 1.00 20.69 ? 778  VAL   A O     1 
ATOM   5467  C  CB    . VAL   A  1 780  ? -10.220 82.859  116.164 1.00 22.22 ? 778  VAL   A CB    1 
ATOM   5468  C  CG1   . VAL   A  1 780  ? -11.348 83.501  115.373 1.00 20.05 ? 778  VAL   A CG1   1 
ATOM   5469  C  CG2   . VAL   A  1 780  ? -9.848  83.713  117.365 1.00 19.17 ? 778  VAL   A CG2   1 
ATOM   5470  N  N     . MET   A  1 781  ? -12.310 80.382  115.266 1.00 21.42 ? 779  MET   A N     1 
ATOM   5471  C  CA    . MET   A  1 781  ? -12.870 79.767  114.078 1.00 17.92 ? 779  MET   A CA    1 
ATOM   5472  C  C     . MET   A  1 781  ? -13.693 80.839  113.387 1.00 18.56 ? 779  MET   A C     1 
ATOM   5473  O  O     . MET   A  1 781  ? -14.624 81.395  113.980 1.00 18.81 ? 779  MET   A O     1 
ATOM   5474  C  CB    . MET   A  1 781  ? -13.702 78.543  114.454 1.00 21.20 ? 779  MET   A CB    1 
ATOM   5475  C  CG    . MET   A  1 781  ? -12.890 77.545  115.272 1.00 21.60 ? 779  MET   A CG    1 
ATOM   5476  S  SD    . MET   A  1 781  ? -13.909 76.212  115.941 1.00 21.08 ? 779  MET   A SD    1 
ATOM   5477  C  CE    . MET   A  1 781  ? -14.164 75.224  114.456 1.00 20.36 ? 779  MET   A CE    1 
ATOM   5478  N  N     . PHE   A  1 782  ? -13.308 81.177  112.165 1.00 19.25 ? 780  PHE   A N     1 
ATOM   5479  C  CA    . PHE   A  1 782  ? -13.935 82.276  111.452 1.00 19.42 ? 780  PHE   A CA    1 
ATOM   5480  C  C     . PHE   A  1 782  ? -14.335 81.796  110.075 1.00 21.81 ? 780  PHE   A C     1 
ATOM   5481  O  O     . PHE   A  1 782  ? -13.512 81.225  109.358 1.00 18.39 ? 780  PHE   A O     1 
ATOM   5482  C  CB    . PHE   A  1 782  ? -12.989 83.473  111.305 1.00 20.39 ? 780  PHE   A CB    1 
ATOM   5483  C  CG    . PHE   A  1 782  ? -13.525 84.549  110.403 1.00 19.70 ? 780  PHE   A CG    1 
ATOM   5484  C  CD1   . PHE   A  1 782  ? -14.452 85.461  110.876 1.00 20.00 ? 780  PHE   A CD1   1 
ATOM   5485  C  CD2   . PHE   A  1 782  ? -13.113 84.637  109.077 1.00 19.20 ? 780  PHE   A CD2   1 
ATOM   5486  C  CE1   . PHE   A  1 782  ? -14.961 86.450  110.056 1.00 22.92 ? 780  PHE   A CE1   1 
ATOM   5487  C  CE2   . PHE   A  1 782  ? -13.612 85.629  108.244 1.00 22.71 ? 780  PHE   A CE2   1 
ATOM   5488  C  CZ    . PHE   A  1 782  ? -14.531 86.542  108.735 1.00 21.81 ? 780  PHE   A CZ    1 
ATOM   5489  N  N     . THR   A  1 783  ? -15.582 82.046  109.706 1.00 20.17 ? 781  THR   A N     1 
ATOM   5490  C  CA    . THR   A  1 783  ? -16.028 81.897  108.328 1.00 22.76 ? 781  THR   A CA    1 
ATOM   5491  C  C     . THR   A  1 783  ? -16.632 83.221  107.897 1.00 20.74 ? 781  THR   A C     1 
ATOM   5492  O  O     . THR   A  1 783  ? -17.564 83.725  108.538 1.00 19.93 ? 781  THR   A O     1 
ATOM   5493  C  CB    . THR   A  1 783  ? -17.029 80.746  108.191 1.00 19.84 ? 781  THR   A CB    1 
ATOM   5494  O  OG1   . THR   A  1 783  ? -16.413 79.536  108.646 1.00 21.23 ? 781  THR   A OG1   1 
ATOM   5495  C  CG2   . THR   A  1 783  ? -17.441 80.567  106.743 1.00 20.57 ? 781  THR   A CG2   1 
ATOM   5496  N  N     . GLY   A  1 784  ? -16.091 83.794  106.828 1.00 20.27 ? 782  GLY   A N     1 
ATOM   5497  C  CA    . GLY   A  1 784  ? -16.525 85.109  106.397 1.00 22.43 ? 782  GLY   A CA    1 
ATOM   5498  C  C     . GLY   A  1 784  ? -15.604 85.631  105.313 1.00 21.98 ? 782  GLY   A C     1 
ATOM   5499  O  O     . GLY   A  1 784  ? -14.941 84.857  104.625 1.00 23.69 ? 782  GLY   A O     1 
ATOM   5500  N  N     . SER   A  1 785  ? -15.569 86.953  105.183 1.00 21.96 ? 783  SER   A N     1 
ATOM   5501  C  CA    . SER   A  1 785  ? -14.752 87.574  104.151 1.00 25.58 ? 783  SER   A CA    1 
ATOM   5502  C  C     . SER   A  1 785  ? -13.259 87.383  104.418 1.00 27.56 ? 783  SER   A C     1 
ATOM   5503  O  O     . SER   A  1 785  ? -12.804 87.331  105.566 1.00 22.36 ? 783  SER   A O     1 
ATOM   5504  C  CB    . SER   A  1 785  ? -15.065 89.065  104.056 1.00 25.00 ? 783  SER   A CB    1 
ATOM   5505  O  OG    . SER   A  1 785  ? -14.669 89.738  105.241 1.00 27.85 ? 783  SER   A OG    1 
ATOM   5506  N  N     . THR   A  1 786  ? -12.493 87.299  103.325 1.00 25.66 ? 784  THR   A N     1 
ATOM   5507  C  CA    . THR   A  1 786  ? -11.036 87.248  103.430 1.00 26.12 ? 784  THR   A CA    1 
ATOM   5508  C  C     . THR   A  1 786  ? -10.489 88.471  104.156 1.00 25.94 ? 784  THR   A C     1 
ATOM   5509  O  O     . THR   A  1 786  ? -9.511  88.372  104.910 1.00 25.63 ? 784  THR   A O     1 
ATOM   5510  C  CB    . THR   A  1 786  ? -10.411 87.148  102.036 1.00 31.29 ? 784  THR   A CB    1 
ATOM   5511  O  OG1   . THR   A  1 786  ? -10.873 85.961  101.381 1.00 31.86 ? 784  THR   A OG1   1 
ATOM   5512  C  CG2   . THR   A  1 786  ? -8.892  87.099  102.140 1.00 32.74 ? 784  THR   A CG2   1 
ATOM   5513  N  N     . GLU   A  1 787  ? -11.105 89.637  103.941 1.00 25.98 ? 785  GLU   A N     1 
ATOM   5514  C  CA    . GLU   A  1 787  ? -10.561 90.857  104.525 1.00 26.78 ? 785  GLU   A CA    1 
ATOM   5515  C  C     . GLU   A  1 787  ? -10.718 90.853  106.040 1.00 23.63 ? 785  GLU   A C     1 
ATOM   5516  O  O     . GLU   A  1 787  ? -9.806  91.272  106.761 1.00 22.92 ? 785  GLU   A O     1 
ATOM   5517  C  CB    . GLU   A  1 787  ? -11.215 92.094  103.896 1.00 27.90 ? 785  GLU   A CB    1 
ATOM   5518  C  CG    . GLU   A  1 787  ? -12.715 92.203  104.096 1.00 34.97 ? 785  GLU   A CG    1 
ATOM   5519  C  CD    . GLU   A  1 787  ? -13.380 93.176  103.130 1.00 40.72 ? 785  GLU   A CD    1 
ATOM   5520  O  OE1   . GLU   A  1 787  ? -12.779 93.469  102.079 1.00 47.15 ? 785  GLU   A OE1   1 
ATOM   5521  O  OE2   . GLU   A  1 787  ? -14.503 93.646  103.420 1.00 38.63 ? 785  GLU   A OE2   1 
ATOM   5522  N  N     . VAL   A  1 788  ? -11.849 90.362  106.547 1.00 23.82 ? 786  VAL   A N     1 
ATOM   5523  C  CA    . VAL   A  1 788  ? -12.016 90.304  107.993 1.00 22.66 ? 786  VAL   A CA    1 
ATOM   5524  C  C     . VAL   A  1 788  ? -11.142 89.208  108.587 1.00 19.87 ? 786  VAL   A C     1 
ATOM   5525  O  O     . VAL   A  1 788  ? -10.569 89.374  109.669 1.00 22.86 ? 786  VAL   A O     1 
ATOM   5526  C  CB    . VAL   A  1 788  ? -13.499 90.126  108.359 1.00 27.31 ? 786  VAL   A CB    1 
ATOM   5527  C  CG1   . VAL   A  1 788  ? -13.636 89.730  109.822 1.00 25.39 ? 786  VAL   A CG1   1 
ATOM   5528  C  CG2   . VAL   A  1 788  ? -14.242 91.432  108.112 1.00 26.99 ? 786  VAL   A CG2   1 
ATOM   5529  N  N     . ALA   A  1 789  ? -11.009 88.080  107.886 1.00 20.01 ? 787  ALA   A N     1 
ATOM   5530  C  CA    . ALA   A  1 789  ? -10.081 87.045  108.336 1.00 21.36 ? 787  ALA   A CA    1 
ATOM   5531  C  C     . ALA   A  1 789  ? -8.672  87.603  108.486 1.00 20.34 ? 787  ALA   A C     1 
ATOM   5532  O  O     . ALA   A  1 789  ? -7.962  87.280  109.446 1.00 20.04 ? 787  ALA   A O     1 
ATOM   5533  C  CB    . ALA   A  1 789  ? -10.096 85.872  107.359 1.00 20.97 ? 787  ALA   A CB    1 
ATOM   5534  N  N     . ARG   A  1 790  ? -8.260  88.459  107.550 1.00 20.55 ? 788  ARG   A N     1 
ATOM   5535  C  CA    . ARG   A  1 790  ? -6.928  89.060  107.602 1.00 20.40 ? 788  ARG   A CA    1 
ATOM   5536  C  C     . ARG   A  1 790  ? -6.788  89.984  108.809 1.00 22.73 ? 788  ARG   A C     1 
ATOM   5537  O  O     . ARG   A  1 790  ? -5.728  90.031  109.442 1.00 23.52 ? 788  ARG   A O     1 
ATOM   5538  C  CB    . ARG   A  1 790  ? -6.670  89.805  106.285 1.00 27.14 ? 788  ARG   A CB    1 
ATOM   5539  C  CG    . ARG   A  1 790  ? -5.219  90.069  105.914 1.00 35.81 ? 788  ARG   A CG    1 
ATOM   5540  C  CD    . ARG   A  1 790  ? -5.098  90.607  104.458 1.00 31.01 ? 788  ARG   A CD    1 
ATOM   5541  N  NE    . ARG   A  1 790  ? -5.005  89.535  103.465 1.00 35.01 ? 788  ARG   A NE    1 
ATOM   5542  C  CZ    . ARG   A  1 790  ? -5.790  89.398  102.401 1.00 32.31 ? 788  ARG   A CZ    1 
ATOM   5543  N  NH1   . ARG   A  1 790  ? -6.779  90.246  102.146 1.00 37.82 ? 788  ARG   A NH1   1 
ATOM   5544  N  NH2   . ARG   A  1 790  ? -5.578  88.385  101.567 1.00 35.99 ? 788  ARG   A NH2   1 
ATOM   5545  N  N     . LEU   A  1 791  ? -7.857  90.713  109.154 1.00 21.09 ? 789  LEU   A N     1 
ATOM   5546  C  CA    . LEU   A  1 791  ? -7.842  91.537  110.359 1.00 24.07 ? 789  LEU   A CA    1 
ATOM   5547  C  C     . LEU   A  1 791  ? -7.743  90.683  111.614 1.00 23.44 ? 789  LEU   A C     1 
ATOM   5548  O  O     . LEU   A  1 791  ? -7.047  91.047  112.568 1.00 23.21 ? 789  LEU   A O     1 
ATOM   5549  C  CB    . LEU   A  1 791  ? -9.100  92.396  110.426 1.00 20.89 ? 789  LEU   A CB    1 
ATOM   5550  C  CG    . LEU   A  1 791  ? -9.201  93.513  109.392 1.00 27.31 ? 789  LEU   A CG    1 
ATOM   5551  C  CD1   . LEU   A  1 791  ? -10.569 94.148  109.486 1.00 27.10 ? 789  LEU   A CD1   1 
ATOM   5552  C  CD2   . LEU   A  1 791  ? -8.103  94.541  109.644 1.00 27.32 ? 789  LEU   A CD2   1 
ATOM   5553  N  N     . ILE   A  1 792  ? -8.451  89.554  111.640 1.00 20.05 ? 790  ILE   A N     1 
ATOM   5554  C  CA    . ILE   A  1 792  ? -8.360  88.661  112.789 1.00 23.25 ? 790  ILE   A CA    1 
ATOM   5555  C  C     . ILE   A  1 792  ? -6.951  88.101  112.907 1.00 19.87 ? 790  ILE   A C     1 
ATOM   5556  O  O     . ILE   A  1 792  ? -6.356  88.089  113.993 1.00 23.20 ? 790  ILE   A O     1 
ATOM   5557  C  CB    . ILE   A  1 792  ? -9.409  87.542  112.681 1.00 20.53 ? 790  ILE   A CB    1 
ATOM   5558  C  CG1   . ILE   A  1 792  ? -10.804 88.151  112.823 1.00 19.91 ? 790  ILE   A CG1   1 
ATOM   5559  C  CG2   . ILE   A  1 792  ? -9.141  86.466  113.730 1.00 19.85 ? 790  ILE   A CG2   1 
ATOM   5560  C  CD1   . ILE   A  1 792  ? -11.923 87.229  112.405 1.00 21.26 ? 790  ILE   A CD1   1 
ATOM   5561  N  N     . GLN   A  1 793  ? -6.394  87.641  111.786 1.00 21.20 ? 791  GLN   A N     1 
ATOM   5562  C  CA    . GLN   A  1 793  ? -5.032  87.113  111.784 1.00 20.07 ? 791  GLN   A CA    1 
ATOM   5563  C  C     . GLN   A  1 793  ? -4.048  88.129  112.357 1.00 24.37 ? 791  GLN   A C     1 
ATOM   5564  O  O     . GLN   A  1 793  ? -3.161  87.777  113.146 1.00 23.99 ? 791  GLN   A O     1 
ATOM   5565  C  CB    . GLN   A  1 793  ? -4.640  86.725  110.358 1.00 21.32 ? 791  GLN   A CB    1 
ATOM   5566  C  CG    . GLN   A  1 793  ? -3.199  86.268  110.183 1.00 26.18 ? 791  GLN   A CG    1 
ATOM   5567  C  CD    . GLN   A  1 793  ? -2.703  86.389  108.729 1.00 35.76 ? 791  GLN   A CD    1 
ATOM   5568  O  OE1   . GLN   A  1 793  ? -3.044  87.341  108.012 1.00 36.67 ? 791  GLN   A OE1   1 
ATOM   5569  N  NE2   . GLN   A  1 793  ? -1.885  85.425  108.298 1.00 36.12 ? 791  GLN   A NE2   1 
ATOM   5570  N  N     . ALA   A  1 794  ? -4.204  89.403  111.985 1.00 25.12 ? 792  ALA   A N     1 
ATOM   5571  C  CA    . ALA   A  1 794  ? -3.290  90.432  112.478 1.00 25.88 ? 792  ALA   A CA    1 
ATOM   5572  C  C     . ALA   A  1 794  ? -3.445  90.642  113.982 1.00 26.09 ? 792  ALA   A C     1 
ATOM   5573  O  O     . ALA   A  1 794  ? -2.455  90.854  114.687 1.00 26.12 ? 792  ALA   A O     1 
ATOM   5574  C  CB    . ALA   A  1 794  ? -3.516  91.740  111.721 1.00 26.40 ? 792  ALA   A CB    1 
ATOM   5575  N  N     . GLN   A  1 795  ? -4.671  90.567  114.498 1.00 25.04 ? 793  GLN   A N     1 
ATOM   5576  C  CA    . GLN   A  1 795  ? -4.862  90.673  115.942 1.00 26.81 ? 793  GLN   A CA    1 
ATOM   5577  C  C     . GLN   A  1 795  ? -4.263  89.479  116.668 1.00 26.18 ? 793  GLN   A C     1 
ATOM   5578  O  O     . GLN   A  1 795  ? -3.610  89.634  117.706 1.00 26.07 ? 793  GLN   A O     1 
ATOM   5579  C  CB    . GLN   A  1 795  ? -6.348  90.793  116.275 1.00 28.15 ? 793  GLN   A CB    1 
ATOM   5580  C  CG    . GLN   A  1 795  ? -6.901  92.159  115.999 1.00 36.93 ? 793  GLN   A CG    1 
ATOM   5581  C  CD    . GLN   A  1 795  ? -6.174  93.220  116.795 1.00 45.60 ? 793  GLN   A CD    1 
ATOM   5582  O  OE1   . GLN   A  1 795  ? -5.951  93.063  117.999 1.00 43.36 ? 793  GLN   A OE1   1 
ATOM   5583  N  NE2   . GLN   A  1 795  ? -5.781  94.302  116.122 1.00 43.00 ? 793  GLN   A NE2   1 
ATOM   5584  N  N     . LEU   A  1 796  ? -4.486  88.275  116.144 1.00 26.84 ? 794  LEU   A N     1 
ATOM   5585  C  CA    . LEU   A  1 796  ? -3.942  87.086  116.784 1.00 28.81 ? 794  LEU   A CA    1 
ATOM   5586  C  C     . LEU   A  1 796  ? -2.425  87.037  116.728 1.00 29.34 ? 794  LEU   A C     1 
ATOM   5587  O  O     . LEU   A  1 796  ? -1.808  86.392  117.584 1.00 31.19 ? 794  LEU   A O     1 
ATOM   5588  C  CB    . LEU   A  1 796  ? -4.517  85.830  116.136 1.00 22.65 ? 794  LEU   A CB    1 
ATOM   5589  C  CG    . LEU   A  1 796  ? -6.009  85.612  116.343 1.00 25.98 ? 794  LEU   A CG    1 
ATOM   5590  C  CD1   . LEU   A  1 796  ? -6.427  84.289  115.713 1.00 22.94 ? 794  LEU   A CD1   1 
ATOM   5591  C  CD2   . LEU   A  1 796  ? -6.326  85.656  117.832 1.00 27.27 ? 794  LEU   A CD2   1 
ATOM   5592  N  N     . ALA   A  1 797  ? -1.808  87.707  115.753 1.00 25.44 ? 795  ALA   A N     1 
ATOM   5593  C  CA    . ALA   A  1 797  ? -0.361  87.614  115.608 1.00 32.09 ? 795  ALA   A CA    1 
ATOM   5594  C  C     . ALA   A  1 797  ? 0.372   88.242  116.783 1.00 32.45 ? 795  ALA   A C     1 
ATOM   5595  O  O     . ALA   A  1 797  ? 1.539   87.920  117.015 1.00 37.86 ? 795  ALA   A O     1 
ATOM   5596  C  CB    . ALA   A  1 797  ? 0.084   88.267  114.301 1.00 30.19 ? 795  ALA   A CB    1 
ATOM   5597  N  N     . ASP   A  1 798  ? -0.295  89.113  117.537 1.00 34.91 ? 796  ASP   A N     1 
ATOM   5598  C  CA    . ASP   A  1 798  ? 0.307   89.753  118.696 1.00 33.94 ? 796  ASP   A CA    1 
ATOM   5599  C  C     . ASP   A  1 798  ? 0.382   88.838  119.910 1.00 38.29 ? 796  ASP   A C     1 
ATOM   5600  O  O     . ASP   A  1 798  ? 1.083   89.180  120.867 1.00 37.22 ? 796  ASP   A O     1 
ATOM   5601  C  CB    . ASP   A  1 798  ? -0.481  91.011  119.064 1.00 32.58 ? 796  ASP   A CB    1 
ATOM   5602  N  N     . ARG   A  1 799  ? -0.299  87.690  119.893 1.00 34.25 ? 797  ARG   A N     1 
ATOM   5603  C  CA    . ARG   A  1 799  ? -0.471  86.883  121.091 1.00 30.81 ? 797  ARG   A CA    1 
ATOM   5604  C  C     . ARG   A  1 799  ? 0.119   85.494  120.910 1.00 32.39 ? 797  ARG   A C     1 
ATOM   5605  O  O     . ARG   A  1 799  ? 0.271   84.993  119.791 1.00 27.84 ? 797  ARG   A O     1 
ATOM   5606  C  CB    . ARG   A  1 799  ? -1.954  86.760  121.463 1.00 38.65 ? 797  ARG   A CB    1 
ATOM   5607  C  CG    . ARG   A  1 799  ? -2.693  88.093  121.530 1.00 38.92 ? 797  ARG   A CG    1 
ATOM   5608  C  CD    . ARG   A  1 799  ? -3.796  88.043  122.579 1.00 38.95 ? 797  ARG   A CD    1 
ATOM   5609  N  NE    . ARG   A  1 799  ? -4.649  86.876  122.397 1.00 42.05 ? 797  ARG   A NE    1 
ATOM   5610  C  CZ    . ARG   A  1 799  ? -5.751  86.874  121.665 1.00 39.18 ? 797  ARG   A CZ    1 
ATOM   5611  N  NH1   . ARG   A  1 799  ? -6.183  87.974  121.072 1.00 36.96 ? 797  ARG   A NH1   1 
ATOM   5612  N  NH2   . ARG   A  1 799  ? -6.430  85.738  121.515 1.00 34.61 ? 797  ARG   A NH2   1 
ATOM   5613  N  N     . LEU   A  1 800  ? 0.440   84.871  122.042 1.00 29.06 ? 798  LEU   A N     1 
ATOM   5614  C  CA    . LEU   A  1 800  ? 0.843   83.474  122.089 1.00 29.95 ? 798  LEU   A CA    1 
ATOM   5615  C  C     . LEU   A  1 800  ? -0.026  82.735  123.095 1.00 27.46 ? 798  LEU   A C     1 
ATOM   5616  O  O     . LEU   A  1 800  ? -0.584  83.328  124.016 1.00 28.84 ? 798  LEU   A O     1 
ATOM   5617  C  CB    . LEU   A  1 800  ? 2.316   83.323  122.462 1.00 33.14 ? 798  LEU   A CB    1 
ATOM   5618  C  CG    . LEU   A  1 800  ? 3.287   83.851  121.413 1.00 33.23 ? 798  LEU   A CG    1 
ATOM   5619  C  CD1   . LEU   A  1 800  ? 4.708   83.816  121.957 1.00 31.06 ? 798  LEU   A CD1   1 
ATOM   5620  C  CD2   . LEU   A  1 800  ? 3.161   83.036  120.127 1.00 28.52 ? 798  LEU   A CD2   1 
ATOM   5621  N  N     . SER   A  1 801  ? -0.134  81.427  122.906 1.00 30.11 ? 799  SER   A N     1 
ATOM   5622  C  CA    . SER   A  1 801  ? -0.876  80.590  123.833 1.00 31.68 ? 799  SER   A CA    1 
ATOM   5623  C  C     . SER   A  1 801  ? -0.110  80.506  125.150 1.00 36.50 ? 799  SER   A C     1 
ATOM   5624  O  O     . SER   A  1 801  ? 1.036   80.958  125.241 1.00 35.47 ? 799  SER   A O     1 
ATOM   5625  C  CB    . SER   A  1 801  ? -1.091  79.201  123.232 1.00 32.49 ? 799  SER   A CB    1 
ATOM   5626  O  OG    . SER   A  1 801  ? 0.115   78.454  123.221 1.00 33.18 ? 799  SER   A OG    1 
ATOM   5627  N  N     . PRO   A  1 802  ? -0.727  79.956  126.203 1.00 37.93 ? 800  PRO   A N     1 
ATOM   5628  C  CA    . PRO   A  1 802  ? 0.042   79.695  127.432 1.00 40.71 ? 800  PRO   A CA    1 
ATOM   5629  C  C     . PRO   A  1 802  ? 1.299   78.876  127.191 1.00 40.21 ? 800  PRO   A C     1 
ATOM   5630  O  O     . PRO   A  1 802  ? 2.314   79.103  127.861 1.00 41.41 ? 800  PRO   A O     1 
ATOM   5631  C  CB    . PRO   A  1 802  ? -0.961  78.943  128.316 1.00 41.21 ? 800  PRO   A CB    1 
ATOM   5632  C  CG    . PRO   A  1 802  ? -2.294  79.430  127.859 1.00 40.44 ? 800  PRO   A CG    1 
ATOM   5633  C  CD    . PRO   A  1 802  ? -2.166  79.681  126.382 1.00 38.00 ? 800  PRO   A CD    1 
ATOM   5634  N  N     . ALA   A  1 803  ? 1.269   77.938  126.245 1.00 35.99 ? 801  ALA   A N     1 
ATOM   5635  C  CA    . ALA   A  1 803  ? 2.440   77.142  125.907 1.00 37.11 ? 801  ALA   A CA    1 
ATOM   5636  C  C     . ALA   A  1 803  ? 3.374   77.842  124.919 1.00 39.14 ? 801  ALA   A C     1 
ATOM   5637  O  O     . ALA   A  1 803  ? 4.318   77.208  124.435 1.00 40.75 ? 801  ALA   A O     1 
ATOM   5638  C  CB    . ALA   A  1 803  ? 2.008   75.786  125.345 1.00 39.53 ? 801  ALA   A CB    1 
ATOM   5639  N  N     . GLY   A  1 804  ? 3.135   79.115  124.604 1.00 39.31 ? 802  GLY   A N     1 
ATOM   5640  C  CA    . GLY   A  1 804  ? 4.013   79.852  123.716 1.00 34.56 ? 802  GLY   A CA    1 
ATOM   5641  C  C     . GLY   A  1 804  ? 3.856   79.555  122.241 1.00 33.39 ? 802  GLY   A C     1 
ATOM   5642  O  O     . GLY   A  1 804  ? 4.795   79.786  121.470 1.00 29.52 ? 802  GLY   A O     1 
ATOM   5643  N  N     . ARG   A  1 805  ? 2.704   79.052  121.817 1.00 28.99 ? 803  ARG   A N     1 
ATOM   5644  C  CA    . ARG   A  1 805  ? 2.458   78.743  120.421 1.00 28.85 ? 803  ARG   A CA    1 
ATOM   5645  C  C     . ARG   A  1 805  ? 1.532   79.781  119.808 1.00 27.95 ? 803  ARG   A C     1 
ATOM   5646  O  O     . ARG   A  1 805  ? 0.810   80.482  120.525 1.00 25.69 ? 803  ARG   A O     1 
ATOM   5647  C  CB    . ARG   A  1 805  ? 1.832   77.352  120.259 1.00 28.92 ? 803  ARG   A CB    1 
ATOM   5648  C  CG    . ARG   A  1 805  ? 2.706   76.215  120.729 1.00 37.94 ? 803  ARG   A CG    1 
ATOM   5649  C  CD    . ARG   A  1 805  ? 2.307   74.896  120.066 1.00 37.43 ? 803  ARG   A CD    1 
ATOM   5650  N  NE    . ARG   A  1 805  ? 2.987   73.771  120.697 1.00 46.99 ? 803  ARG   A NE    1 
ATOM   5651  C  CZ    . ARG   A  1 805  ? 2.558   73.159  121.794 1.00 54.10 ? 803  ARG   A CZ    1 
ATOM   5652  N  NH1   . ARG   A  1 805  ? 1.415   73.500  122.378 1.00 50.26 ? 803  ARG   A NH1   1 
ATOM   5653  N  NH2   . ARG   A  1 805  ? 3.291   72.182  122.320 1.00 53.84 ? 803  ARG   A NH2   1 
ATOM   5654  N  N     . PRO   A  1 806  ? 1.547   79.928  118.481 1.00 24.31 ? 804  PRO   A N     1 
ATOM   5655  C  CA    . PRO   A  1 806  ? 0.547   80.782  117.829 1.00 26.90 ? 804  PRO   A CA    1 
ATOM   5656  C  C     . PRO   A  1 806  ? -0.863  80.328  118.177 1.00 26.13 ? 804  PRO   A C     1 
ATOM   5657  O  O     . PRO   A  1 806  ? -1.128  79.136  118.365 1.00 25.83 ? 804  PRO   A O     1 
ATOM   5658  C  CB    . PRO   A  1 806  ? 0.835   80.598  116.334 1.00 27.28 ? 804  PRO   A CB    1 
ATOM   5659  C  CG    . PRO   A  1 806  ? 2.283   80.178  116.275 1.00 26.44 ? 804  PRO   A CG    1 
ATOM   5660  C  CD    . PRO   A  1 806  ? 2.492   79.344  117.513 1.00 30.23 ? 804  PRO   A CD    1 
ATOM   5661  N  N     . ILE   A  1 807  ? -1.767  81.298  118.262 1.00 23.37 ? 805  ILE   A N     1 
ATOM   5662  C  CA    . ILE   A  1 807  ? -3.178  81.023  118.517 1.00 23.24 ? 805  ILE   A CA    1 
ATOM   5663  C  C     . ILE   A  1 807  ? -3.771  80.452  117.236 1.00 24.63 ? 805  ILE   A C     1 
ATOM   5664  O  O     . ILE   A  1 807  ? -3.735  81.121  116.196 1.00 24.53 ? 805  ILE   A O     1 
ATOM   5665  C  CB    . ILE   A  1 807  ? -3.936  82.290  118.951 1.00 23.93 ? 805  ILE   A CB    1 
ATOM   5666  C  CG1   . ILE   A  1 807  ? -3.282  82.945  120.174 1.00 27.22 ? 805  ILE   A CG1   1 
ATOM   5667  C  CG2   . ILE   A  1 807  ? -5.395  81.971  119.236 1.00 22.04 ? 805  ILE   A CG2   1 
ATOM   5668  C  CD1   . ILE   A  1 807  ? -3.301  82.091  121.407 1.00 25.11 ? 805  ILE   A CD1   1 
ATOM   5669  N  N     . PRO   A  1 808  ? -4.327  79.243  117.251 1.00 22.92 ? 806  PRO   A N     1 
ATOM   5670  C  CA    . PRO   A  1 808  ? -4.896  78.690  116.015 1.00 24.43 ? 806  PRO   A CA    1 
ATOM   5671  C  C     . PRO   A  1 808  ? -6.026  79.552  115.483 1.00 23.33 ? 806  PRO   A C     1 
ATOM   5672  O  O     . PRO   A  1 808  ? -6.908  79.986  116.226 1.00 21.80 ? 806  PRO   A O     1 
ATOM   5673  C  CB    . PRO   A  1 808  ? -5.408  77.307  116.440 1.00 21.92 ? 806  PRO   A CB    1 
ATOM   5674  C  CG    . PRO   A  1 808  ? -4.631  76.973  117.656 1.00 24.07 ? 806  PRO   A CG    1 
ATOM   5675  C  CD    . PRO   A  1 808  ? -4.394  78.285  118.363 1.00 23.49 ? 806  PRO   A CD    1 
ATOM   5676  N  N     . LEU   A  1 809  ? -5.993  79.785  114.172 1.00 23.98 ? 807  LEU   A N     1 
ATOM   5677  C  CA    . LEU   A  1 809  ? -7.080  80.416  113.443 1.00 23.12 ? 807  LEU   A CA    1 
ATOM   5678  C  C     . LEU   A  1 809  ? -7.501  79.467  112.335 1.00 22.35 ? 807  LEU   A C     1 
ATOM   5679  O  O     . LEU   A  1 809  ? -6.668  79.062  111.514 1.00 20.73 ? 807  LEU   A O     1 
ATOM   5680  C  CB    . LEU   A  1 809  ? -6.656  81.768  112.855 1.00 24.53 ? 807  LEU   A CB    1 
ATOM   5681  C  CG    . LEU   A  1 809  ? -7.660  82.381  111.864 1.00 21.14 ? 807  LEU   A CG    1 
ATOM   5682  C  CD1   . LEU   A  1 809  ? -8.997  82.756  112.526 1.00 21.81 ? 807  LEU   A CD1   1 
ATOM   5683  C  CD2   . LEU   A  1 809  ? -7.057  83.587  111.164 1.00 23.47 ? 807  LEU   A CD2   1 
ATOM   5684  N  N     . ILE   A  1 810  ? -8.775  79.083  112.334 1.00 19.10 ? 808  ILE   A N     1 
ATOM   5685  C  CA    . ILE   A  1 810  ? -9.379  78.370  111.217 1.00 19.95 ? 808  ILE   A CA    1 
ATOM   5686  C  C     . ILE   A  1 810  ? -10.248 79.381  110.506 1.00 23.10 ? 808  ILE   A C     1 
ATOM   5687  O  O     . ILE   A  1 810  ? -11.273 79.807  111.048 1.00 21.35 ? 808  ILE   A O     1 
ATOM   5688  C  CB    . ILE   A  1 810  ? -10.224 77.168  111.657 1.00 17.23 ? 808  ILE   A CB    1 
ATOM   5689  C  CG1   . ILE   A  1 810  ? -9.417  76.176  112.470 1.00 21.67 ? 808  ILE   A CG1   1 
ATOM   5690  C  CG2   . ILE   A  1 810  ? -10.795 76.442  110.425 1.00 21.17 ? 808  ILE   A CG2   1 
ATOM   5691  C  CD1   . ILE   A  1 810  ? -10.269 74.993  112.881 1.00 24.19 ? 808  ILE   A CD1   1 
ATOM   5692  N  N     . ALA   A  1 811  ? -9.855  79.765  109.302 1.00 20.68 ? 809  ALA   A N     1 
ATOM   5693  C  CA    . ALA   A  1 811  ? -10.546 80.811  108.558 1.00 21.34 ? 809  ALA   A CA    1 
ATOM   5694  C  C     . ALA   A  1 811  ? -10.972 80.229  107.220 1.00 24.36 ? 809  ALA   A C     1 
ATOM   5695  O  O     . ALA   A  1 811  ? -10.120 79.827  106.419 1.00 23.67 ? 809  ALA   A O     1 
ATOM   5696  C  CB    . ALA   A  1 811  ? -9.648  82.033  108.370 1.00 23.66 ? 809  ALA   A CB    1 
ATOM   5697  N  N     . GLU   A  1 812  ? -12.283 80.146  107.000 1.00 21.90 ? 810  GLU   A N     1 
ATOM   5698  C  CA    . GLU   A  1 812  ? -12.851 79.773  105.709 1.00 25.79 ? 810  GLU   A CA    1 
ATOM   5699  C  C     . GLU   A  1 812  ? -13.358 81.047  105.050 1.00 24.50 ? 810  GLU   A C     1 
ATOM   5700  O  O     . GLU   A  1 812  ? -14.213 81.745  105.613 1.00 21.52 ? 810  GLU   A O     1 
ATOM   5701  C  CB    . GLU   A  1 812  ? -13.992 78.761  105.856 1.00 28.23 ? 810  GLU   A CB    1 
ATOM   5702  C  CG    . GLU   A  1 812  ? -14.315 77.981  104.551 1.00 35.76 ? 810  GLU   A CG    1 
ATOM   5703  C  CD    . GLU   A  1 812  ? -15.478 78.538  103.707 1.00 36.39 ? 810  GLU   A CD    1 
ATOM   5704  O  OE1   . GLU   A  1 812  ? -16.666 78.366  104.084 1.00 34.77 ? 810  GLU   A OE1   1 
ATOM   5705  O  OE2   . GLU   A  1 812  ? -15.203 79.121  102.635 1.00 35.27 ? 810  GLU   A OE2   1 
ATOM   5706  N  N     . THR   A  1 813  ? -12.812 81.368  103.884 1.00 22.54 ? 811  THR   A N     1 
ATOM   5707  C  CA    . THR   A  1 813  ? -13.078 82.658  103.268 1.00 23.55 ? 811  THR   A CA    1 
ATOM   5708  C  C     . THR   A  1 813  ? -13.594 82.437  101.850 1.00 25.83 ? 811  THR   A C     1 
ATOM   5709  O  O     . THR   A  1 813  ? -14.067 81.356  101.483 1.00 24.33 ? 811  THR   A O     1 
ATOM   5710  C  CB    . THR   A  1 813  ? -11.824 83.545  103.364 1.00 24.98 ? 811  THR   A CB    1 
ATOM   5711  O  OG1   . THR   A  1 813  ? -10.676 82.838  102.870 1.00 24.28 ? 811  THR   A OG1   1 
ATOM   5712  C  CG2   . THR   A  1 813  ? -11.583 83.915  104.833 1.00 22.86 ? 811  THR   A CG2   1 
ATOM   5713  N  N     . GLY   A  1 814  ? -13.526 83.473  101.034 1.00 26.13 ? 812  GLY   A N     1 
ATOM   5714  C  CA    . GLY   A  1 814  ? -14.239 83.455  99.780  1.00 34.21 ? 812  GLY   A CA    1 
ATOM   5715  C  C     . GLY   A  1 814  ? -13.614 82.529  98.751  1.00 33.69 ? 812  GLY   A C     1 
ATOM   5716  O  O     . GLY   A  1 814  ? -12.596 81.868  98.964  1.00 29.13 ? 812  GLY   A O     1 
ATOM   5717  N  N     . GLY   A  1 815  ? -14.265 82.483  97.603  1.00 27.38 ? 813  GLY   A N     1 
ATOM   5718  C  CA    . GLY   A  1 815  ? -13.687 81.844  96.437  1.00 25.95 ? 813  GLY   A CA    1 
ATOM   5719  C  C     . GLY   A  1 815  ? -14.129 82.594  95.206  1.00 24.18 ? 813  GLY   A C     1 
ATOM   5720  O  O     . GLY   A  1 815  ? -15.199 83.202  95.185  1.00 29.63 ? 813  GLY   A O     1 
ATOM   5721  N  N     . GLN   A  1 816  ? -13.288 82.570  94.182  1.00 24.33 ? 814  GLN   A N     1 
ATOM   5722  C  CA    . GLN   A  1 816  ? -13.670 83.026  92.851  1.00 21.92 ? 814  GLN   A CA    1 
ATOM   5723  C  C     . GLN   A  1 816  ? -13.854 81.784  91.987  1.00 20.19 ? 814  GLN   A C     1 
ATOM   5724  O  O     . GLN   A  1 816  ? -13.017 81.445  91.143  1.00 19.38 ? 814  GLN   A O     1 
ATOM   5725  C  CB    . GLN   A  1 816  ? -12.610 83.963  92.286  1.00 22.43 ? 814  GLN   A CB    1 
ATOM   5726  C  CG    . GLN   A  1 816  ? -13.050 84.682  91.047  1.00 28.19 ? 814  GLN   A CG    1 
ATOM   5727  C  CD    . GLN   A  1 816  ? -14.023 85.788  91.372  1.00 37.13 ? 814  GLN   A CD    1 
ATOM   5728  O  OE1   . GLN   A  1 816  ? -15.199 85.532  91.635  1.00 28.85 ? 814  GLN   A OE1   1 
ATOM   5729  N  NE2   . GLN   A  1 816  ? -13.535 87.029  91.380  1.00 30.36 ? 814  GLN   A NE2   1 
ATOM   5730  N  N     . ASN   A  1 817  ? -14.951 81.077  92.242  1.00 18.94 ? 815  ASN   A N     1 
ATOM   5731  C  CA    . ASN   A  1 817  ? -15.067 79.692  91.812  1.00 19.32 ? 815  ASN   A CA    1 
ATOM   5732  C  C     . ASN   A  1 817  ? -15.415 79.611  90.336  1.00 18.22 ? 815  ASN   A C     1 
ATOM   5733  O  O     . ASN   A  1 817  ? -16.318 80.306  89.856  1.00 18.36 ? 815  ASN   A O     1 
ATOM   5734  C  CB    . ASN   A  1 817  ? -16.115 78.978  92.655  1.00 16.57 ? 815  ASN   A CB    1 
ATOM   5735  C  CG    . ASN   A  1 817  ? -15.883 79.208  94.131  1.00 18.23 ? 815  ASN   A CG    1 
ATOM   5736  O  OD1   . ASN   A  1 817  ? -14.781 78.972  94.627  1.00 18.31 ? 815  ASN   A OD1   1 
ATOM   5737  N  ND2   . ASN   A  1 817  ? -16.894 79.719  94.825  1.00 16.96 ? 815  ASN   A ND2   1 
ATOM   5738  N  N     . ALA   A  1 818  ? -14.702 78.748  89.625  1.00 18.17 ? 816  ALA   A N     1 
ATOM   5739  C  CA    . ALA   A  1 818  ? -14.859 78.607  88.192  1.00 16.40 ? 816  ALA   A CA    1 
ATOM   5740  C  C     . ALA   A  1 818  ? -15.414 77.238  87.851  1.00 15.52 ? 816  ALA   A C     1 
ATOM   5741  O  O     . ALA   A  1 818  ? -15.269 76.272  88.598  1.00 16.64 ? 816  ALA   A O     1 
ATOM   5742  C  CB    . ALA   A  1 818  ? -13.524 78.811  87.472  1.00 20.71 ? 816  ALA   A CB    1 
ATOM   5743  N  N     . MET   A  1 819  ? -16.032 77.163  86.686  1.00 17.76 ? 817  MET   A N     1 
ATOM   5744  C  CA    . MET   A  1 819  ? -16.389 75.898  86.073  1.00 16.62 ? 817  MET   A CA    1 
ATOM   5745  C  C     . MET   A  1 819  ? -15.915 75.941  84.633  1.00 18.41 ? 817  MET   A C     1 
ATOM   5746  O  O     . MET   A  1 819  ? -16.160 76.926  83.930  1.00 18.21 ? 817  MET   A O     1 
ATOM   5747  C  CB    . MET   A  1 819  ? -17.893 75.644  86.112  1.00 16.23 ? 817  MET   A CB    1 
ATOM   5748  C  CG    . MET   A  1 819  ? -18.315 74.394  85.365  1.00 16.72 ? 817  MET   A CG    1 
ATOM   5749  S  SD    . MET   A  1 819  ? -20.114 74.228  85.285  1.00 21.06 ? 817  MET   A SD    1 
ATOM   5750  C  CE    . MET   A  1 819  ? -20.528 73.913  87.000  1.00 19.82 ? 817  MET   A CE    1 
ATOM   5751  N  N     . ILE   A  1 820  ? -15.228 74.893  84.202  1.00 17.49 ? 818  ILE   A N     1 
ATOM   5752  C  CA    . ILE   A  1 820  ? -14.788 74.770  82.819  1.00 15.91 ? 818  ILE   A CA    1 
ATOM   5753  C  C     . ILE   A  1 820  ? -15.671 73.746  82.114  1.00 17.85 ? 818  ILE   A C     1 
ATOM   5754  O  O     . ILE   A  1 820  ? -15.927 72.652  82.638  1.00 15.73 ? 818  ILE   A O     1 
ATOM   5755  C  CB    . ILE   A  1 820  ? -13.302 74.379  82.740  1.00 18.21 ? 818  ILE   A CB    1 
ATOM   5756  C  CG1   . ILE   A  1 820  ? -12.429 75.478  83.348  1.00 19.06 ? 818  ILE   A CG1   1 
ATOM   5757  C  CG2   . ILE   A  1 820  ? -12.896 74.171  81.296  1.00 18.59 ? 818  ILE   A CG2   1 
ATOM   5758  C  CD1   . ILE   A  1 820  ? -10.944 75.155  83.336  1.00 19.04 ? 818  ILE   A CD1   1 
ATOM   5759  N  N     . VAL   A  1 821  ? -16.144 74.104  80.926  1.00 16.84 ? 819  VAL   A N     1 
ATOM   5760  C  CA    . VAL   A  1 821  ? -17.070 73.279  80.165  1.00 17.93 ? 819  VAL   A CA    1 
ATOM   5761  C  C     . VAL   A  1 821  ? -16.492 73.114  78.774  1.00 20.42 ? 819  VAL   A C     1 
ATOM   5762  O  O     . VAL   A  1 821  ? -16.294 74.115  78.073  1.00 19.61 ? 819  VAL   A O     1 
ATOM   5763  C  CB    . VAL   A  1 821  ? -18.461 73.927  80.077  1.00 16.47 ? 819  VAL   A CB    1 
ATOM   5764  C  CG1   . VAL   A  1 821  ? -19.362 73.123  79.165  1.00 17.04 ? 819  VAL   A CG1   1 
ATOM   5765  C  CG2   . VAL   A  1 821  ? -19.061 74.079  81.479  1.00 16.86 ? 819  VAL   A CG2   1 
ATOM   5766  N  N     . ASP   A  1 822  ? -16.242 71.867  78.356  1.00 18.53 ? 820  ASP   A N     1 
ATOM   5767  C  CA    . ASP   A  1 822  ? -15.706 71.671  77.013  1.00 18.25 ? 820  ASP   A CA    1 
ATOM   5768  C  C     . ASP   A  1 822  ? -16.819 71.219  76.066  1.00 21.04 ? 820  ASP   A C     1 
ATOM   5769  O  O     . ASP   A  1 822  ? -17.979 71.076  76.451  1.00 19.27 ? 820  ASP   A O     1 
ATOM   5770  C  CB    . ASP   A  1 822  ? -14.491 70.727  77.017  1.00 20.95 ? 820  ASP   A CB    1 
ATOM   5771  C  CG    . ASP   A  1 822  ? -14.835 69.261  77.268  1.00 20.43 ? 820  ASP   A CG    1 
ATOM   5772  O  OD1   . ASP   A  1 822  ? -16.010 68.859  77.180  1.00 21.19 ? 820  ASP   A OD1   1 
ATOM   5773  O  OD2   . ASP   A  1 822  ? -13.876 68.493  77.549  1.00 20.63 ? 820  ASP   A OD2   1 
ATOM   5774  N  N     . SER   A  1 823  ? -16.461 71.024  74.793  1.00 19.43 ? 821  SER   A N     1 
ATOM   5775  C  CA    . SER   A  1 823  ? -17.460 70.713  73.774  1.00 22.31 ? 821  SER   A CA    1 
ATOM   5776  C  C     . SER   A  1 823  ? -18.032 69.302  73.892  1.00 22.01 ? 821  SER   A C     1 
ATOM   5777  O  O     . SER   A  1 823  ? -18.926 68.954  73.118  1.00 22.78 ? 821  SER   A O     1 
ATOM   5778  C  CB    . SER   A  1 823  ? -16.864 70.910  72.372  1.00 21.67 ? 821  SER   A CB    1 
ATOM   5779  O  OG    . SER   A  1 823  ? -15.707 70.109  72.202  1.00 21.98 ? 821  SER   A OG    1 
ATOM   5780  N  N     . SER   A  1 824  ? -17.531 68.473  74.805  1.00 20.99 ? 822  SER   A N     1 
ATOM   5781  C  CA    . SER   A  1 824  ? -18.100 67.150  75.012  1.00 17.81 ? 822  SER   A CA    1 
ATOM   5782  C  C     . SER   A  1 824  ? -19.223 67.153  76.039  1.00 21.82 ? 822  SER   A C     1 
ATOM   5783  O  O     . SER   A  1 824  ? -19.963 66.166  76.138  1.00 22.67 ? 822  SER   A O     1 
ATOM   5784  C  CB    . SER   A  1 824  ? -17.013 66.163  75.453  1.00 21.47 ? 822  SER   A CB    1 
ATOM   5785  O  OG    . SER   A  1 824  ? -16.627 66.405  76.798  1.00 19.02 ? 822  SER   A OG    1 
ATOM   5786  N  N     . ALA   A  1 825  ? -19.366 68.230  76.805  1.00 19.00 ? 823  ALA   A N     1 
ATOM   5787  C  CA    . ALA   A  1 825  ? -20.380 68.268  77.844  1.00 21.33 ? 823  ALA   A CA    1 
ATOM   5788  C  C     . ALA   A  1 825  ? -21.773 68.306  77.231  1.00 19.53 ? 823  ALA   A C     1 
ATOM   5789  O  O     . ALA   A  1 825  ? -21.964 68.754  76.101  1.00 22.87 ? 823  ALA   A O     1 
ATOM   5790  C  CB    . ALA   A  1 825  ? -20.164 69.489  78.741  1.00 20.47 ? 823  ALA   A CB    1 
ATOM   5791  N  N     . LEU   A  1 826  ? -22.753 67.831  77.994  1.00 20.37 ? 824  LEU   A N     1 
ATOM   5792  C  CA    . LEU   A  1 826  ? -24.159 67.888  77.601  1.00 24.89 ? 824  LEU   A CA    1 
ATOM   5793  C  C     . LEU   A  1 826  ? -24.727 69.236  78.031  1.00 24.89 ? 824  LEU   A C     1 
ATOM   5794  O  O     . LEU   A  1 826  ? -24.815 69.523  79.229  1.00 21.95 ? 824  LEU   A O     1 
ATOM   5795  C  CB    . LEU   A  1 826  ? -24.939 66.738  78.234  1.00 26.38 ? 824  LEU   A CB    1 
ATOM   5796  C  CG    . LEU   A  1 826  ? -26.415 66.608  77.847  1.00 35.34 ? 824  LEU   A CG    1 
ATOM   5797  C  CD1   . LEU   A  1 826  ? -26.573 66.566  76.332  1.00 40.72 ? 824  LEU   A CD1   1 
ATOM   5798  C  CD2   . LEU   A  1 826  ? -27.023 65.361  78.475  1.00 40.34 ? 824  LEU   A CD2   1 
ATOM   5799  N  N     . ALA   A  1 827  ? -25.120 70.060  77.053  1.00 22.37 ? 825  ALA   A N     1 
ATOM   5800  C  CA    . ALA   A  1 827  ? -25.516 71.438  77.337  1.00 23.29 ? 825  ALA   A CA    1 
ATOM   5801  C  C     . ALA   A  1 827  ? -26.594 71.520  78.411  1.00 23.42 ? 825  ALA   A C     1 
ATOM   5802  O  O     . ALA   A  1 827  ? -26.513 72.362  79.316  1.00 22.37 ? 825  ALA   A O     1 
ATOM   5803  C  CB    . ALA   A  1 827  ? -26.001 72.119  76.053  1.00 26.70 ? 825  ALA   A CB    1 
ATOM   5804  N  N     . GLU   A  1 828  ? -27.608 70.652  78.333  1.00 22.56 ? 826  GLU   A N     1 
ATOM   5805  C  CA    . GLU   A  1 828  ? -28.723 70.725  79.277  1.00 24.10 ? 826  GLU   A CA    1 
ATOM   5806  C  C     . GLU   A  1 828  ? -28.263 70.452  80.699  1.00 23.00 ? 826  GLU   A C     1 
ATOM   5807  O  O     . GLU   A  1 828  ? -28.708 71.119  81.643  1.00 20.66 ? 826  GLU   A O     1 
ATOM   5808  C  CB    . GLU   A  1 828  ? -29.820 69.734  78.889  1.00 27.33 ? 826  GLU   A CB    1 
ATOM   5809  C  CG    . GLU   A  1 828  ? -30.639 70.125  77.678  1.00 32.65 ? 826  GLU   A CG    1 
ATOM   5810  C  CD    . GLU   A  1 828  ? -29.895 69.937  76.366  1.00 39.05 ? 826  GLU   A CD    1 
ATOM   5811  O  OE1   . GLU   A  1 828  ? -28.762 69.394  76.378  1.00 35.65 ? 826  GLU   A OE1   1 
ATOM   5812  O  OE2   . GLU   A  1 828  ? -30.446 70.344  75.315  1.00 47.19 ? 826  GLU   A OE2   1 
ATOM   5813  N  N     . GLN   A  1 829  ? -27.397 69.450  80.877  1.00 20.42 ? 827  GLN   A N     1 
ATOM   5814  C  CA    . GLN   A  1 829  ? -26.834 69.188  82.198  1.00 20.18 ? 827  GLN   A CA    1 
ATOM   5815  C  C     . GLN   A  1 829  ? -25.999 70.365  82.673  1.00 18.97 ? 827  GLN   A C     1 
ATOM   5816  O  O     . GLN   A  1 829  ? -26.078 70.767  83.841  1.00 20.81 ? 827  GLN   A O     1 
ATOM   5817  C  CB    . GLN   A  1 829  ? -25.997 67.906  82.170  1.00 24.67 ? 827  GLN   A CB    1 
ATOM   5818  N  N     . VAL   A  1 830  ? -25.192 70.931  81.775  1.00 19.74 ? 828  VAL   A N     1 
ATOM   5819  C  CA    . VAL   A  1 830  ? -24.375 72.090  82.121  1.00 17.98 ? 828  VAL   A CA    1 
ATOM   5820  C  C     . VAL   A  1 830  ? -25.251 73.245  82.594  1.00 17.55 ? 828  VAL   A C     1 
ATOM   5821  O  O     . VAL   A  1 830  ? -24.976 73.883  83.617  1.00 17.40 ? 828  VAL   A O     1 
ATOM   5822  C  CB    . VAL   A  1 830  ? -23.520 72.515  80.917  1.00 17.85 ? 828  VAL   A CB    1 
ATOM   5823  C  CG1   . VAL   A  1 830  ? -22.917 73.889  81.178  1.00 20.13 ? 828  VAL   A CG1   1 
ATOM   5824  C  CG2   . VAL   A  1 830  ? -22.419 71.482  80.653  1.00 20.63 ? 828  VAL   A CG2   1 
ATOM   5825  N  N     . VAL   A  1 831  ? -26.307 73.544  81.841  1.00 18.70 ? 829  VAL   A N     1 
ATOM   5826  C  CA    . VAL   A  1 831  ? -27.112 74.718  82.154  1.00 17.73 ? 829  VAL   A CA    1 
ATOM   5827  C  C     . VAL   A  1 831  ? -27.780 74.559  83.510  1.00 18.72 ? 829  VAL   A C     1 
ATOM   5828  O  O     . VAL   A  1 831  ? -27.775 75.486  84.329  1.00 17.76 ? 829  VAL   A O     1 
ATOM   5829  C  CB    . VAL   A  1 831  ? -28.130 74.966  81.031  1.00 18.66 ? 829  VAL   A CB    1 
ATOM   5830  C  CG1   . VAL   A  1 831  ? -29.130 76.015  81.464  1.00 19.11 ? 829  VAL   A CG1   1 
ATOM   5831  C  CG2   . VAL   A  1 831  ? -27.392 75.428  79.784  1.00 21.57 ? 829  VAL   A CG2   1 
ATOM   5832  N  N     . GLY   A  1 832  ? -28.347 73.378  83.778  1.00 16.87 ? 830  GLY   A N     1 
ATOM   5833  C  CA    . GLY   A  1 832  ? -28.926 73.133  85.088  1.00 18.69 ? 830  GLY   A CA    1 
ATOM   5834  C  C     . GLY   A  1 832  ? -27.909 73.290  86.204  1.00 21.30 ? 830  GLY   A C     1 
ATOM   5835  O  O     . GLY   A  1 832  ? -28.180 73.924  87.226  1.00 18.34 ? 830  GLY   A O     1 
ATOM   5836  N  N     . ASP   A  1 833  ? -26.713 72.732  86.016  1.00 15.44 ? 831  ASP   A N     1 
ATOM   5837  C  CA    . ASP   A  1 833  ? -25.708 72.844  87.070  1.00 18.76 ? 831  ASP   A CA    1 
ATOM   5838  C  C     . ASP   A  1 833  ? -25.180 74.269  87.200  1.00 15.43 ? 831  ASP   A C     1 
ATOM   5839  O  O     . ASP   A  1 833  ? -24.795 74.692  88.298  1.00 17.62 ? 831  ASP   A O     1 
ATOM   5840  C  CB    . ASP   A  1 833  ? -24.567 71.860  86.807  1.00 17.93 ? 831  ASP   A CB    1 
ATOM   5841  C  CG    . ASP   A  1 833  ? -25.003 70.421  86.971  1.00 19.31 ? 831  ASP   A CG    1 
ATOM   5842  O  OD1   . ASP   A  1 833  ? -26.059 70.202  87.590  1.00 19.71 ? 831  ASP   A OD1   1 
ATOM   5843  O  OD2   . ASP   A  1 833  ? -24.290 69.507  86.495  1.00 22.14 ? 831  ASP   A OD2   1 
ATOM   5844  N  N     . VAL   A  1 834  ? -25.145 75.022  86.103  1.00 16.50 ? 832  VAL   A N     1 
ATOM   5845  C  CA    . VAL   A  1 834  ? -24.679 76.404  86.166  1.00 16.26 ? 832  VAL   A CA    1 
ATOM   5846  C  C     . VAL   A  1 834  ? -25.716 77.280  86.860  1.00 17.36 ? 832  VAL   A C     1 
ATOM   5847  O  O     . VAL   A  1 834  ? -25.389 78.055  87.768  1.00 16.81 ? 832  VAL   A O     1 
ATOM   5848  C  CB    . VAL   A  1 834  ? -24.353 76.920  84.750  1.00 17.35 ? 832  VAL   A CB    1 
ATOM   5849  C  CG1   . VAL   A  1 834  ? -24.140 78.401  84.762  1.00 17.10 ? 832  VAL   A CG1   1 
ATOM   5850  C  CG2   . VAL   A  1 834  ? -23.092 76.231  84.211  1.00 18.71 ? 832  VAL   A CG2   1 
ATOM   5851  N  N     . ILE   A  1 835  ? -26.983 77.169  86.437  1.00 15.46 ? 833  ILE   A N     1 
ATOM   5852  C  CA    . ILE   A  1 835  ? -28.069 77.932  87.065  1.00 17.43 ? 833  ILE   A CA    1 
ATOM   5853  C  C     . ILE   A  1 835  ? -28.089 77.683  88.568  1.00 18.24 ? 833  ILE   A C     1 
ATOM   5854  O  O     . ILE   A  1 835  ? -28.154 78.616  89.382  1.00 17.40 ? 833  ILE   A O     1 
ATOM   5855  C  CB    . ILE   A  1 835  ? -29.420 77.574  86.419  1.00 20.59 ? 833  ILE   A CB    1 
ATOM   5856  C  CG1   . ILE   A  1 835  ? -29.491 78.098  84.975  1.00 22.02 ? 833  ILE   A CG1   1 
ATOM   5857  C  CG2   . ILE   A  1 835  ? -30.576 78.111  87.276  1.00 20.75 ? 833  ILE   A CG2   1 
ATOM   5858  C  CD1   . ILE   A  1 835  ? -29.501 79.626  84.859  1.00 22.15 ? 833  ILE   A CD1   1 
ATOM   5859  N  N     . THR   A  1 836  ? -28.018 76.418  88.959  1.00 17.26 ? 834  THR   A N     1 
ATOM   5860  C  CA    . THR   A  1 836  ? -28.008 76.092  90.377  1.00 18.14 ? 834  THR   A CA    1 
ATOM   5861  C  C     . THR   A  1 836  ? -26.756 76.643  91.053  1.00 18.40 ? 834  THR   A C     1 
ATOM   5862  O  O     . THR   A  1 836  ? -26.846 77.315  92.081  1.00 18.08 ? 834  THR   A O     1 
ATOM   5863  C  CB    . THR   A  1 836  ? -28.116 74.579  90.560  1.00 20.88 ? 834  THR   A CB    1 
ATOM   5864  O  OG1   . THR   A  1 836  ? -29.391 74.143  90.084  1.00 25.31 ? 834  THR   A OG1   1 
ATOM   5865  C  CG2   . THR   A  1 836  ? -27.981 74.196  92.010  1.00 20.18 ? 834  THR   A CG2   1 
ATOM   5866  N  N     . SER   A  1 837  ? -25.572 76.394  90.476  1.00 15.15 ? 835  SER   A N     1 
ATOM   5867  C  CA    . SER   A  1 837  ? -24.346 76.777  91.167  1.00 17.60 ? 835  SER   A CA    1 
ATOM   5868  C  C     . SER   A  1 837  ? -24.226 78.288  91.310  1.00 17.65 ? 835  SER   A C     1 
ATOM   5869  O  O     . SER   A  1 837  ? -23.699 78.777  92.312  1.00 16.28 ? 835  SER   A O     1 
ATOM   5870  C  CB    . SER   A  1 837  ? -23.122 76.224  90.435  1.00 14.88 ? 835  SER   A CB    1 
ATOM   5871  O  OG    . SER   A  1 837  ? -23.145 74.803  90.435  1.00 16.82 ? 835  SER   A OG    1 
ATOM   5872  N  N     . ALA   A  1 838  ? -24.678 79.044  90.315  1.00 15.16 ? 836  ALA   A N     1 
ATOM   5873  C  CA    . ALA   A  1 838  ? -24.475 80.488  90.338  1.00 15.84 ? 836  ALA   A CA    1 
ATOM   5874  C  C     . ALA   A  1 838  ? -25.559 81.236  91.101  1.00 17.78 ? 836  ALA   A C     1 
ATOM   5875  O  O     . ALA   A  1 838  ? -25.275 82.262  91.720  1.00 18.65 ? 836  ALA   A O     1 
ATOM   5876  C  CB    . ALA   A  1 838  ? -24.407 81.034  88.906  1.00 15.47 ? 836  ALA   A CB    1 
ATOM   5877  N  N     . PHE   A  1 839  ? -26.796 80.765  91.062  1.00 17.52 ? 837  PHE   A N     1 
ATOM   5878  C  CA    . PHE   A  1 839  ? -27.903 81.576  91.538  1.00 17.73 ? 837  PHE   A CA    1 
ATOM   5879  C  C     . PHE   A  1 839  ? -28.643 80.989  92.719  1.00 18.75 ? 837  PHE   A C     1 
ATOM   5880  O  O     . PHE   A  1 839  ? -29.404 81.723  93.368  1.00 16.69 ? 837  PHE   A O     1 
ATOM   5881  C  CB    . PHE   A  1 839  ? -28.886 81.844  90.390  1.00 16.50 ? 837  PHE   A CB    1 
ATOM   5882  C  CG    . PHE   A  1 839  ? -28.232 82.462  89.194  1.00 18.38 ? 837  PHE   A CG    1 
ATOM   5883  C  CD1   . PHE   A  1 839  ? -27.448 83.604  89.326  1.00 18.58 ? 837  PHE   A CD1   1 
ATOM   5884  C  CD2   . PHE   A  1 839  ? -28.344 81.876  87.946  1.00 18.64 ? 837  PHE   A CD2   1 
ATOM   5885  C  CE1   . PHE   A  1 839  ? -26.821 84.167  88.229  1.00 17.86 ? 837  PHE   A CE1   1 
ATOM   5886  C  CE2   . PHE   A  1 839  ? -27.709 82.431  86.846  1.00 16.97 ? 837  PHE   A CE2   1 
ATOM   5887  C  CZ    . PHE   A  1 839  ? -26.951 83.576  86.982  1.00 16.98 ? 837  PHE   A CZ    1 
ATOM   5888  N  N     . ASP   A  1 840  ? -28.442 79.707  93.032  1.00 18.71 ? 838  ASP   A N     1 
ATOM   5889  C  CA    . ASP   A  1 840  ? -28.981 79.164  94.268  1.00 20.21 ? 838  ASP   A CA    1 
ATOM   5890  C  C     . ASP   A  1 840  ? -28.580 80.057  95.430  1.00 17.87 ? 838  ASP   A C     1 
ATOM   5891  O  O     . ASP   A  1 840  ? -27.446 80.545  95.490  1.00 20.22 ? 838  ASP   A O     1 
ATOM   5892  C  CB    . ASP   A  1 840  ? -28.474 77.739  94.499  1.00 20.30 ? 838  ASP   A CB    1 
ATOM   5893  C  CG    . ASP   A  1 840  ? -29.022 77.131  95.760  1.00 24.10 ? 838  ASP   A CG    1 
ATOM   5894  O  OD1   . ASP   A  1 840  ? -28.476 77.420  96.846  1.00 22.79 ? 838  ASP   A OD1   1 
ATOM   5895  O  OD2   . ASP   A  1 840  ? -30.015 76.379  95.666  1.00 27.59 ? 838  ASP   A OD2   1 
ATOM   5896  N  N     . SER   A  1 841  ? -29.536 80.315  96.324  1.00 17.06 ? 839  SER   A N     1 
ATOM   5897  C  CA    . SER   A  1 841  ? -29.298 81.162  97.492  1.00 20.73 ? 839  SER   A CA    1 
ATOM   5898  C  C     . SER   A  1 841  ? -28.826 82.548  97.077  1.00 16.88 ? 839  SER   A C     1 
ATOM   5899  O  O     . SER   A  1 841  ? -28.053 83.195  97.790  1.00 18.03 ? 839  SER   A O     1 
ATOM   5900  C  CB    . SER   A  1 841  ? -28.291 80.518  98.447  1.00 21.35 ? 839  SER   A CB    1 
ATOM   5901  O  OG    . SER   A  1 841  ? -28.678 79.186  98.743  1.00 21.34 ? 839  SER   A OG    1 
ATOM   5902  N  N     . ALA   A  1 842  ? -29.276 83.003  95.907  1.00 17.14 ? 840  ALA   A N     1 
ATOM   5903  C  CA    . ALA   A  1 842  ? -28.891 84.305  95.370  1.00 16.71 ? 840  ALA   A CA    1 
ATOM   5904  C  C     . ALA   A  1 842  ? -27.378 84.421  95.248  1.00 17.37 ? 840  ALA   A C     1 
ATOM   5905  O  O     . ALA   A  1 842  ? -26.811 85.497  95.436  1.00 19.71 ? 840  ALA   A O     1 
ATOM   5906  C  CB    . ALA   A  1 842  ? -29.454 85.459  96.223  1.00 20.12 ? 840  ALA   A CB    1 
ATOM   5907  N  N     . GLY   A  1 843  ? -26.720 83.301  94.957  1.00 17.78 ? 841  GLY   A N     1 
ATOM   5908  C  CA    . GLY   A  1 843  ? -25.275 83.304  94.830  1.00 15.89 ? 841  GLY   A CA    1 
ATOM   5909  C  C     . GLY   A  1 843  ? -24.539 83.621  96.114  1.00 18.59 ? 841  GLY   A C     1 
ATOM   5910  O  O     . GLY   A  1 843  ? -23.348 83.958  96.075  1.00 21.35 ? 841  GLY   A O     1 
ATOM   5911  N  N     . GLN   A  1 844  ? -25.218 83.527  97.260  1.00 16.05 ? 842  GLN   A N     1 
ATOM   5912  C  CA    . GLN   A  1 844  ? -24.602 83.811  98.545  1.00 18.63 ? 842  GLN   A CA    1 
ATOM   5913  C  C     . GLN   A  1 844  ? -23.997 82.576  99.170  1.00 20.50 ? 842  GLN   A C     1 
ATOM   5914  O  O     . GLN   A  1 844  ? -23.983 82.442  100.399 1.00 28.08 ? 842  GLN   A O     1 
ATOM   5915  C  CB    . GLN   A  1 844  ? -25.617 84.471  99.479  1.00 16.38 ? 842  GLN   A CB    1 
ATOM   5916  C  CG    . GLN   A  1 844  ? -26.075 85.811  98.917  1.00 16.94 ? 842  GLN   A CG    1 
ATOM   5917  C  CD    . GLN   A  1 844  ? -27.098 86.520  99.812  1.00 18.84 ? 842  GLN   A CD    1 
ATOM   5918  O  OE1   . GLN   A  1 844  ? -26.989 87.715  100.051 1.00 19.70 ? 842  GLN   A OE1   1 
ATOM   5919  N  NE2   . GLN   A  1 844  ? -28.080 85.772  100.318 1.00 20.60 ? 842  GLN   A NE2   1 
ATOM   5920  N  N     . ARG   A  1 845  ? -23.521 81.647  98.350  1.00 20.45 ? 843  ARG   A N     1 
ATOM   5921  C  CA    . ARG   A  1 845  ? -22.741 80.521  98.827  1.00 20.01 ? 843  ARG   A CA    1 
ATOM   5922  C  C     . ARG   A  1 845  ? -21.279 80.839  98.586  1.00 20.61 ? 843  ARG   A C     1 
ATOM   5923  O  O     . ARG   A  1 845  ? -20.929 81.432  97.563  1.00 21.95 ? 843  ARG   A O     1 
ATOM   5924  C  CB    . ARG   A  1 845  ? -23.119 79.223  98.103  1.00 19.36 ? 843  ARG   A CB    1 
ATOM   5925  C  CG    . ARG   A  1 845  ? -24.536 78.741  98.373  1.00 21.13 ? 843  ARG   A CG    1 
ATOM   5926  C  CD    . ARG   A  1 845  ? -24.783 77.435  97.631  1.00 22.03 ? 843  ARG   A CD    1 
ATOM   5927  N  NE    . ARG   A  1 845  ? -26.106 76.893  97.904  1.00 27.27 ? 843  ARG   A NE    1 
ATOM   5928  C  CZ    . ARG   A  1 845  ? -26.363 75.937  98.786  1.00 24.26 ? 843  ARG   A CZ    1 
ATOM   5929  N  NH1   . ARG   A  1 845  ? -25.402 75.387  99.520  1.00 27.59 ? 843  ARG   A NH1   1 
ATOM   5930  N  NH2   . ARG   A  1 845  ? -27.610 75.507  98.921  1.00 27.37 ? 843  ARG   A NH2   1 
ATOM   5931  N  N     . CYS   A  1 846  ? -20.422 80.487  99.544  1.00 21.03 ? 844  CYS   A N     1 
ATOM   5932  C  CA    A CYS   A  1 846  ? -18.995 80.651  99.300  0.63 23.27 ? 844  CYS   A CA    1 
ATOM   5933  C  CA    B CYS   A  1 846  ? -18.993 80.644  99.306  0.37 23.26 ? 844  CYS   A CA    1 
ATOM   5934  C  C     . CYS   A  1 846  ? -18.550 79.809  98.115  1.00 18.35 ? 844  CYS   A C     1 
ATOM   5935  O  O     . CYS   A  1 846  ? -17.611 80.179  97.413  1.00 18.48 ? 844  CYS   A O     1 
ATOM   5936  C  CB    A CYS   A  1 846  ? -18.194 80.283  100.550 0.63 25.90 ? 844  CYS   A CB    1 
ATOM   5937  C  CB    B CYS   A  1 846  ? -18.206 80.250  100.553 0.37 25.87 ? 844  CYS   A CB    1 
ATOM   5938  S  SG    A CYS   A  1 846  ? -18.470 81.412  101.932 0.63 38.11 ? 844  CYS   A SG    1 
ATOM   5939  S  SG    B CYS   A  1 846  ? -18.651 78.625  101.165 0.37 23.79 ? 844  CYS   A SG    1 
ATOM   5940  N  N     . SER   A  1 847  ? -19.225 78.690  97.881  1.00 17.55 ? 845  SER   A N     1 
ATOM   5941  C  CA    . SER   A  1 847  ? -18.972 77.771  96.779  1.00 17.01 ? 845  SER   A CA    1 
ATOM   5942  C  C     . SER   A  1 847  ? -19.594 78.211  95.459  1.00 18.59 ? 845  SER   A C     1 
ATOM   5943  O  O     . SER   A  1 847  ? -19.422 77.510  94.451  1.00 16.48 ? 845  SER   A O     1 
ATOM   5944  C  CB    . SER   A  1 847  ? -19.548 76.408  97.145  1.00 21.30 ? 845  SER   A CB    1 
ATOM   5945  O  OG    . SER   A  1 847  ? -20.929 76.589  97.412  1.00 25.75 ? 845  SER   A OG    1 
ATOM   5946  N  N     . ALA   A  1 848  ? -20.336 79.316  95.443  1.00 16.88 ? 846  ALA   A N     1 
ATOM   5947  C  CA    . ALA   A  1 848  ? -21.154 79.633  94.280  1.00 17.84 ? 846  ALA   A CA    1 
ATOM   5948  C  C     . ALA   A  1 848  ? -20.287 79.806  93.041  1.00 15.62 ? 846  ALA   A C     1 
ATOM   5949  O  O     . ALA   A  1 848  ? -19.139 80.244  93.108  1.00 17.79 ? 846  ALA   A O     1 
ATOM   5950  C  CB    . ALA   A  1 848  ? -21.975 80.903  94.527  1.00 17.72 ? 846  ALA   A CB    1 
ATOM   5951  N  N     . LEU   A  1 849  ? -20.844 79.433  91.899  1.00 15.36 ? 847  LEU   A N     1 
ATOM   5952  C  CA    . LEU   A  1 849  ? -20.130 79.570  90.635  1.00 15.42 ? 847  LEU   A CA    1 
ATOM   5953  C  C     . LEU   A  1 849  ? -20.042 81.040  90.247  1.00 16.61 ? 847  LEU   A C     1 
ATOM   5954  O  O     . LEU   A  1 849  ? -21.067 81.694  90.033  1.00 17.99 ? 847  LEU   A O     1 
ATOM   5955  C  CB    . LEU   A  1 849  ? -20.847 78.775  89.548  1.00 15.28 ? 847  LEU   A CB    1 
ATOM   5956  C  CG    . LEU   A  1 849  ? -20.243 78.909  88.154  1.00 16.74 ? 847  LEU   A CG    1 
ATOM   5957  C  CD1   . LEU   A  1 849  ? -18.787 78.390  88.161  1.00 16.23 ? 847  LEU   A CD1   1 
ATOM   5958  C  CD2   . LEU   A  1 849  ? -21.108 78.175  87.147  1.00 16.63 ? 847  LEU   A CD2   1 
ATOM   5959  N  N     . ARG   A  1 850  ? -18.817 81.556  90.144  1.00 15.80 ? 848  ARG   A N     1 
ATOM   5960  C  CA    . ARG   A  1 850  ? -18.591 82.947  89.787  1.00 19.26 ? 848  ARG   A CA    1 
ATOM   5961  C  C     . ARG   A  1 850  ? -18.158 83.124  88.342  1.00 17.38 ? 848  ARG   A C     1 
ATOM   5962  O  O     . ARG   A  1 850  ? -18.499 84.135  87.730  1.00 16.46 ? 848  ARG   A O     1 
ATOM   5963  C  CB    . ARG   A  1 850  ? -17.524 83.578  90.688  1.00 17.15 ? 848  ARG   A CB    1 
ATOM   5964  C  CG    . ARG   A  1 850  ? -17.770 83.372  92.162  1.00 18.62 ? 848  ARG   A CG    1 
ATOM   5965  C  CD    . ARG   A  1 850  ? -19.143 83.871  92.543  1.00 19.07 ? 848  ARG   A CD    1 
ATOM   5966  N  NE    . ARG   A  1 850  ? -19.346 83.819  93.988  1.00 20.01 ? 848  ARG   A NE    1 
ATOM   5967  C  CZ    . ARG   A  1 850  ? -20.499 84.103  94.576  1.00 22.58 ? 848  ARG   A CZ    1 
ATOM   5968  N  NH1   . ARG   A  1 850  ? -21.568 84.417  93.867  1.00 18.08 ? 848  ARG   A NH1   1 
ATOM   5969  N  NH2   . ARG   A  1 850  ? -20.578 84.071  95.908  1.00 17.43 ? 848  ARG   A NH2   1 
ATOM   5970  N  N     . VAL   A  1 851  ? -17.412 82.174  87.785  1.00 16.85 ? 849  VAL   A N     1 
ATOM   5971  C  CA    . VAL   A  1 851  ? -16.877 82.307  86.436  1.00 19.64 ? 849  VAL   A CA    1 
ATOM   5972  C  C     . VAL   A  1 851  ? -17.111 81.009  85.685  1.00 17.85 ? 849  VAL   A C     1 
ATOM   5973  O  O     . VAL   A  1 851  ? -16.540 79.971  86.035  1.00 17.49 ? 849  VAL   A O     1 
ATOM   5974  C  CB    . VAL   A  1 851  ? -15.382 82.648  86.421  1.00 19.34 ? 849  VAL   A CB    1 
ATOM   5975  C  CG1   . VAL   A  1 851  ? -14.955 82.866  84.978  1.00 20.63 ? 849  VAL   A CG1   1 
ATOM   5976  C  CG2   . VAL   A  1 851  ? -15.086 83.882  87.243  1.00 23.77 ? 849  VAL   A CG2   1 
ATOM   5977  N  N     . LEU   A  1 852  ? -17.914 81.074  84.633  1.00 18.51 ? 850  LEU   A N     1 
ATOM   5978  C  CA    . LEU   A  1 852  ? -18.146 79.931  83.767  1.00 17.52 ? 850  LEU   A CA    1 
ATOM   5979  C  C     . LEU   A  1 852  ? -17.255 80.077  82.545  1.00 18.07 ? 850  LEU   A C     1 
ATOM   5980  O  O     . LEU   A  1 852  ? -17.282 81.118  81.879  1.00 18.38 ? 850  LEU   A O     1 
ATOM   5981  C  CB    . LEU   A  1 852  ? -19.613 79.853  83.352  1.00 15.79 ? 850  LEU   A CB    1 
ATOM   5982  C  CG    . LEU   A  1 852  ? -19.959 78.758  82.345  1.00 17.52 ? 850  LEU   A CG    1 
ATOM   5983  C  CD1   . LEU   A  1 852  ? -19.736 77.365  82.938  1.00 15.85 ? 850  LEU   A CD1   1 
ATOM   5984  C  CD2   . LEU   A  1 852  ? -21.419 78.926  81.906  1.00 17.32 ? 850  LEU   A CD2   1 
ATOM   5985  N  N     . CYS   A  1 853  ? -16.475 79.035  82.245  1.00 16.42 ? 851  CYS   A N     1 
ATOM   5986  C  CA    . CYS   A  1 853  ? -15.549 79.047  81.116  1.00 18.69 ? 851  CYS   A CA    1 
ATOM   5987  C  C     . CYS   A  1 853  ? -16.047 78.053  80.073  1.00 18.61 ? 851  CYS   A C     1 
ATOM   5988  O  O     . CYS   A  1 853  ? -16.075 76.843  80.323  1.00 19.61 ? 851  CYS   A O     1 
ATOM   5989  C  CB    . CYS   A  1 853  ? -14.129 78.706  81.571  1.00 17.81 ? 851  CYS   A CB    1 
ATOM   5990  S  SG    . CYS   A  1 853  ? -13.612 79.617  83.029  1.00 21.07 ? 851  CYS   A SG    1 
ATOM   5991  N  N     . LEU   A  1 854  ? -16.436 78.570  78.911  1.00 18.49 ? 852  LEU   A N     1 
ATOM   5992  C  CA    . LEU   A  1 854  ? -17.098 77.799  77.874  1.00 16.41 ? 852  LEU   A CA    1 
ATOM   5993  C  C     . LEU   A  1 854  ? -16.149 77.622  76.703  1.00 19.28 ? 852  LEU   A C     1 
ATOM   5994  O  O     . LEU   A  1 854  ? -15.645 78.606  76.161  1.00 18.59 ? 852  LEU   A O     1 
ATOM   5995  C  CB    . LEU   A  1 854  ? -18.373 78.508  77.398  1.00 19.18 ? 852  LEU   A CB    1 
ATOM   5996  C  CG    . LEU   A  1 854  ? -19.486 78.607  78.443  1.00 21.48 ? 852  LEU   A CG    1 
ATOM   5997  C  CD1   . LEU   A  1 854  ? -20.753 79.311  77.892  1.00 17.36 ? 852  LEU   A CD1   1 
ATOM   5998  C  CD2   . LEU   A  1 854  ? -19.822 77.204  78.930  1.00 18.41 ? 852  LEU   A CD2   1 
ATOM   5999  N  N     . GLN   A  1 855  ? -15.929 76.381  76.292  1.00 18.92 ? 853  GLN   A N     1 
ATOM   6000  C  CA    . GLN   A  1 855  ? -15.143 76.182  75.084  1.00 18.69 ? 853  GLN   A CA    1 
ATOM   6001  C  C     . GLN   A  1 855  ? -15.817 76.880  73.909  1.00 19.55 ? 853  GLN   A C     1 
ATOM   6002  O  O     . GLN   A  1 855  ? -17.028 76.753  73.712  1.00 20.89 ? 853  GLN   A O     1 
ATOM   6003  C  CB    . GLN   A  1 855  ? -14.971 74.702  74.779  1.00 18.98 ? 853  GLN   A CB    1 
ATOM   6004  C  CG    . GLN   A  1 855  ? -13.930 74.496  73.677  1.00 20.03 ? 853  GLN   A CG    1 
ATOM   6005  C  CD    . GLN   A  1 855  ? -13.792 73.054  73.285  1.00 20.68 ? 853  GLN   A CD    1 
ATOM   6006  O  OE1   . GLN   A  1 855  ? -13.769 72.181  74.140  1.00 23.81 ? 853  GLN   A OE1   1 
ATOM   6007  N  NE2   . GLN   A  1 855  ? -13.704 72.791  71.985  1.00 24.39 ? 853  GLN   A NE2   1 
ATOM   6008  N  N     . GLU   A  1 856  ? -15.011 77.596  73.120  1.00 20.53 ? 854  GLU   A N     1 
ATOM   6009  C  CA    . GLU   A  1 856  ? -15.542 78.518  72.120  1.00 24.49 ? 854  GLU   A CA    1 
ATOM   6010  C  C     . GLU   A  1 856  ? -16.569 77.857  71.204  1.00 23.01 ? 854  GLU   A C     1 
ATOM   6011  O  O     . GLU   A  1 856  ? -17.604 78.458  70.894  1.00 25.84 ? 854  GLU   A O     1 
ATOM   6012  C  CB    . GLU   A  1 856  ? -14.387 79.114  71.304  1.00 24.39 ? 854  GLU   A CB    1 
ATOM   6013  C  CG    . GLU   A  1 856  ? -14.839 79.984  70.126  1.00 29.28 ? 854  GLU   A CG    1 
ATOM   6014  C  CD    . GLU   A  1 856  ? -15.657 81.186  70.561  1.00 31.89 ? 854  GLU   A CD    1 
ATOM   6015  O  OE1   . GLU   A  1 856  ? -15.385 81.740  71.645  1.00 31.63 ? 854  GLU   A OE1   1 
ATOM   6016  O  OE2   . GLU   A  1 856  ? -16.585 81.575  69.827  1.00 35.81 ? 854  GLU   A OE2   1 
ATOM   6017  N  N     . ASP   A  1 857  ? -16.321 76.608  70.791  1.00 24.49 ? 855  ASP   A N     1 
ATOM   6018  C  CA    . ASP   A  1 857  ? -17.177 75.970  69.789  1.00 24.61 ? 855  ASP   A CA    1 
ATOM   6019  C  C     . ASP   A  1 857  ? -18.607 75.764  70.285  1.00 26.54 ? 855  ASP   A C     1 
ATOM   6020  O  O     . ASP   A  1 857  ? -19.535 75.704  69.469  1.00 26.79 ? 855  ASP   A O     1 
ATOM   6021  C  CB    . ASP   A  1 857  ? -16.578 74.627  69.355  1.00 28.34 ? 855  ASP   A CB    1 
ATOM   6022  N  N     . VAL   A  1 858  ? -18.813 75.658  71.600  1.00 20.61 ? 856  VAL   A N     1 
ATOM   6023  C  CA    . VAL   A  1 858  ? -20.139 75.455  72.172  1.00 21.77 ? 856  VAL   A CA    1 
ATOM   6024  C  C     . VAL   A  1 858  ? -20.621 76.651  72.972  1.00 22.06 ? 856  VAL   A C     1 
ATOM   6025  O  O     . VAL   A  1 858  ? -21.725 76.594  73.541  1.00 22.28 ? 856  VAL   A O     1 
ATOM   6026  C  CB    . VAL   A  1 858  ? -20.194 74.183  73.044  1.00 24.46 ? 856  VAL   A CB    1 
ATOM   6027  C  CG1   . VAL   A  1 858  ? -19.942 72.949  72.191  1.00 27.56 ? 856  VAL   A CG1   1 
ATOM   6028  C  CG2   . VAL   A  1 858  ? -19.178 74.263  74.198  1.00 23.83 ? 856  VAL   A CG2   1 
ATOM   6029  N  N     . ALA   A  1 859  ? -19.848 77.738  73.019  1.00 20.74 ? 857  ALA   A N     1 
ATOM   6030  C  CA    . ALA   A  1 859  ? -20.163 78.836  73.929  1.00 21.63 ? 857  ALA   A CA    1 
ATOM   6031  C  C     . ALA   A  1 859  ? -21.495 79.491  73.587  1.00 24.96 ? 857  ALA   A C     1 
ATOM   6032  O  O     . ALA   A  1 859  ? -22.285 79.797  74.487  1.00 23.82 ? 857  ALA   A O     1 
ATOM   6033  C  CB    . ALA   A  1 859  ? -19.046 79.875  73.910  1.00 21.27 ? 857  ALA   A CB    1 
ATOM   6034  N  N     . ASP   A  1 860  ? -21.756 79.732  72.295  1.00 22.43 ? 858  ASP   A N     1 
ATOM   6035  C  CA    . ASP   A  1 860  ? -22.968 80.457  71.921  1.00 26.89 ? 858  ASP   A CA    1 
ATOM   6036  C  C     . ASP   A  1 860  ? -24.216 79.651  72.238  1.00 20.39 ? 858  ASP   A C     1 
ATOM   6037  O  O     . ASP   A  1 860  ? -25.196 80.195  72.762  1.00 24.22 ? 858  ASP   A O     1 
ATOM   6038  C  CB    . ASP   A  1 860  ? -22.933 80.822  70.439  1.00 26.57 ? 858  ASP   A CB    1 
ATOM   6039  C  CG    . ASP   A  1 860  ? -21.972 81.949  70.148  1.00 34.62 ? 858  ASP   A CG    1 
ATOM   6040  O  OD1   . ASP   A  1 860  ? -21.840 82.863  70.992  1.00 34.97 ? 858  ASP   A OD1   1 
ATOM   6041  O  OD2   . ASP   A  1 860  ? -21.342 81.915  69.076  1.00 39.60 ? 858  ASP   A OD2   1 
ATOM   6042  N  N     . ARG   A  1 861  ? -24.196 78.351  71.942  1.00 21.87 ? 859  ARG   A N     1 
ATOM   6043  C  CA    . ARG   A  1 861  ? -25.351 77.506  72.218  1.00 23.59 ? 859  ARG   A CA    1 
ATOM   6044  C  C     . ARG   A  1 861  ? -25.623 77.414  73.714  1.00 21.95 ? 859  ARG   A C     1 
ATOM   6045  O  O     . ARG   A  1 861  ? -26.772 77.516  74.158  1.00 20.55 ? 859  ARG   A O     1 
ATOM   6046  C  CB    . ARG   A  1 861  ? -25.136 76.111  71.629  1.00 24.79 ? 859  ARG   A CB    1 
ATOM   6047  C  CG    . ARG   A  1 861  ? -26.221 75.136  72.026  1.00 31.27 ? 859  ARG   A CG    1 
ATOM   6048  C  CD    . ARG   A  1 861  ? -26.287 73.921  71.116  1.00 42.70 ? 859  ARG   A CD    1 
ATOM   6049  N  NE    . ARG   A  1 861  ? -27.421 73.076  71.478  1.00 49.80 ? 859  ARG   A NE    1 
ATOM   6050  C  CZ    . ARG   A  1 861  ? -27.344 72.022  72.279  1.00 43.83 ? 859  ARG   A CZ    1 
ATOM   6051  N  NH1   . ARG   A  1 861  ? -26.187 71.619  72.781  1.00 46.43 ? 859  ARG   A NH1   1 
ATOM   6052  N  NH2   . ARG   A  1 861  ? -28.455 71.356  72.584  1.00 44.23 ? 859  ARG   A NH2   1 
ATOM   6053  N  N     . ILE   A  1 862  ? -24.575 77.202  74.507  1.00 18.67 ? 860  ILE   A N     1 
ATOM   6054  C  CA    . ILE   A  1 862  ? -24.769 77.099  75.949  1.00 18.47 ? 860  ILE   A CA    1 
ATOM   6055  C  C     . ILE   A  1 862  ? -25.201 78.442  76.530  1.00 20.27 ? 860  ILE   A C     1 
ATOM   6056  O  O     . ILE   A  1 862  ? -26.078 78.506  77.404  1.00 19.94 ? 860  ILE   A O     1 
ATOM   6057  C  CB    . ILE   A  1 862  ? -23.487 76.559  76.609  1.00 20.54 ? 860  ILE   A CB    1 
ATOM   6058  C  CG1   . ILE   A  1 862  ? -23.273 75.103  76.189  1.00 23.01 ? 860  ILE   A CG1   1 
ATOM   6059  C  CG2   . ILE   A  1 862  ? -23.580 76.658  78.121  1.00 19.49 ? 860  ILE   A CG2   1 
ATOM   6060  C  CD1   . ILE   A  1 862  ? -21.871 74.568  76.491  1.00 25.48 ? 860  ILE   A CD1   1 
ATOM   6061  N  N     . LEU   A  1 863  ? -24.600 79.534  76.061  1.00 19.44 ? 861  LEU   A N     1 
ATOM   6062  C  CA    . LEU   A  1 863  ? -25.005 80.856  76.525  1.00 19.90 ? 861  LEU   A CA    1 
ATOM   6063  C  C     . LEU   A  1 863  ? -26.474 81.126  76.217  1.00 19.79 ? 861  LEU   A C     1 
ATOM   6064  O  O     . LEU   A  1 863  ? -27.203 81.655  77.062  1.00 18.47 ? 861  LEU   A O     1 
ATOM   6065  C  CB    . LEU   A  1 863  ? -24.111 81.913  75.883  1.00 18.96 ? 861  LEU   A CB    1 
ATOM   6066  C  CG    . LEU   A  1 863  ? -23.722 83.222  76.564  1.00 32.77 ? 861  LEU   A CG    1 
ATOM   6067  C  CD1   . LEU   A  1 863  ? -23.699 83.105  78.071  1.00 25.13 ? 861  LEU   A CD1   1 
ATOM   6068  C  CD2   . LEU   A  1 863  ? -22.353 83.615  76.036  1.00 31.57 ? 861  LEU   A CD2   1 
ATOM   6069  N  N     . THR   A  1 864  ? -26.926 80.783  75.007  1.00 19.13 ? 862  THR   A N     1 
ATOM   6070  C  CA    . THR   A  1 864  ? -28.331 81.002  74.659  1.00 18.61 ? 862  THR   A CA    1 
ATOM   6071  C  C     . THR   A  1 864  ? -29.250 80.222  75.590  1.00 18.74 ? 862  THR   A C     1 
ATOM   6072  O  O     . THR   A  1 864  ? -30.252 80.753  76.087  1.00 19.15 ? 862  THR   A O     1 
ATOM   6073  C  CB    . THR   A  1 864  ? -28.567 80.609  73.197  1.00 20.01 ? 862  THR   A CB    1 
ATOM   6074  O  OG1   . THR   A  1 864  ? -27.836 81.502  72.359  1.00 21.82 ? 862  THR   A OG1   1 
ATOM   6075  C  CG2   . THR   A  1 864  ? -30.045 80.660  72.841  1.00 22.16 ? 862  THR   A CG2   1 
ATOM   6076  N  N     . MET   A  1 865  ? -28.905 78.963  75.854  1.00 18.86 ? 863  MET   A N     1 
ATOM   6077  C  CA    A MET   A  1 865  ? -29.700 78.146  76.758  0.48 19.04 ? 863  MET   A CA    1 
ATOM   6078  C  CA    B MET   A  1 865  ? -29.699 78.147  76.763  0.52 19.04 ? 863  MET   A CA    1 
ATOM   6079  C  C     . MET   A  1 865  ? -29.620 78.672  78.187  1.00 18.06 ? 863  MET   A C     1 
ATOM   6080  O  O     . MET   A  1 865  ? -30.616 78.664  78.919  1.00 17.60 ? 863  MET   A O     1 
ATOM   6081  C  CB    A MET   A  1 865  ? -29.220 76.697  76.671  0.48 19.58 ? 863  MET   A CB    1 
ATOM   6082  C  CB    B MET   A  1 865  ? -29.219 76.701  76.711  0.52 19.53 ? 863  MET   A CB    1 
ATOM   6083  C  CG    A MET   A  1 865  ? -30.099 75.690  77.375  0.48 20.95 ? 863  MET   A CG    1 
ATOM   6084  C  CG    B MET   A  1 865  ? -29.644 75.954  75.483  0.52 22.51 ? 863  MET   A CG    1 
ATOM   6085  S  SD    A MET   A  1 865  ? -29.408 74.028  77.228  0.48 26.48 ? 863  MET   A SD    1 
ATOM   6086  S  SD    B MET   A  1 865  ? -28.821 74.361  75.471  0.52 26.82 ? 863  MET   A SD    1 
ATOM   6087  C  CE    A MET   A  1 865  ? -29.893 73.629  75.552  0.48 24.65 ? 863  MET   A CE    1 
ATOM   6088  C  CE    B MET   A  1 865  ? -29.239 73.761  77.103  0.52 26.00 ? 863  MET   A CE    1 
ATOM   6089  N  N     . LEU   A  1 866  ? -28.446 79.137  78.597  1.00 18.86 ? 864  LEU   A N     1 
ATOM   6090  C  CA    A LEU   A  1 866  ? -28.304 79.675  79.942  0.58 18.28 ? 864  LEU   A CA    1 
ATOM   6091  C  CA    B LEU   A  1 866  ? -28.296 79.685  79.941  0.42 18.38 ? 864  LEU   A CA    1 
ATOM   6092  C  C     . LEU   A  1 866  ? -29.164 80.920  80.133  1.00 16.14 ? 864  LEU   A C     1 
ATOM   6093  O  O     . LEU   A  1 866  ? -29.835 81.066  81.157  1.00 17.97 ? 864  LEU   A O     1 
ATOM   6094  C  CB    A LEU   A  1 866  ? -26.837 79.984  80.210  0.58 20.11 ? 864  LEU   A CB    1 
ATOM   6095  C  CB    B LEU   A  1 866  ? -26.839 80.037  80.207  0.42 20.07 ? 864  LEU   A CB    1 
ATOM   6096  C  CG    A LEU   A  1 866  ? -26.517 80.563  81.574  0.58 19.64 ? 864  LEU   A CG    1 
ATOM   6097  C  CG    B LEU   A  1 866  ? -25.946 78.996  80.850  0.42 18.79 ? 864  LEU   A CG    1 
ATOM   6098  C  CD1   A LEU   A  1 866  ? -26.835 79.527  82.626  0.58 19.04 ? 864  LEU   A CD1   1 
ATOM   6099  C  CD1   B LEU   A  1 866  ? -24.636 79.678  81.097  0.42 19.80 ? 864  LEU   A CD1   1 
ATOM   6100  C  CD2   A LEU   A  1 866  ? -25.053 80.951  81.609  0.58 19.54 ? 864  LEU   A CD2   1 
ATOM   6101  C  CD2   B LEU   A  1 866  ? -26.549 78.512  82.150  0.42 18.38 ? 864  LEU   A CD2   1 
ATOM   6102  N  N     . LYS   A  1 867  ? -29.141 81.836  79.165  1.00 17.36 ? 865  LYS   A N     1 
ATOM   6103  C  CA    . LYS   A  1 867  ? -29.981 83.022  79.282  1.00 17.11 ? 865  LYS   A CA    1 
ATOM   6104  C  C     . LYS   A  1 867  ? -31.449 82.633  79.310  1.00 19.79 ? 865  LYS   A C     1 
ATOM   6105  O  O     . LYS   A  1 867  ? -32.237 83.198  80.076  1.00 19.02 ? 865  LYS   A O     1 
ATOM   6106  C  CB    . LYS   A  1 867  ? -29.697 83.992  78.134  1.00 19.26 ? 865  LYS   A CB    1 
ATOM   6107  C  CG    . LYS   A  1 867  ? -28.267 84.513  78.142  1.00 20.01 ? 865  LYS   A CG    1 
ATOM   6108  C  CD    . LYS   A  1 867  ? -27.981 85.377  76.922  1.00 25.09 ? 865  LYS   A CD    1 
ATOM   6109  C  CE    . LYS   A  1 867  ? -26.531 85.850  76.941  1.00 28.78 ? 865  LYS   A CE    1 
ATOM   6110  N  NZ    . LYS   A  1 867  ? -26.130 86.591  75.702  1.00 30.41 ? 865  LYS   A NZ    1 
ATOM   6111  N  N     . GLY   A  1 868  ? -31.831 81.654  78.493  1.00 17.73 ? 866  GLY   A N     1 
ATOM   6112  C  CA    . GLY   A  1 868  ? -33.213 81.211  78.501  1.00 17.72 ? 866  GLY   A CA    1 
ATOM   6113  C  C     . GLY   A  1 868  ? -33.611 80.644  79.845  1.00 19.62 ? 866  GLY   A C     1 
ATOM   6114  O  O     . GLY   A  1 868  ? -34.710 80.910  80.343  1.00 19.23 ? 866  GLY   A O     1 
ATOM   6115  N  N     . ALA   A  1 869  ? -32.717 79.857  80.454  1.00 17.17 ? 867  ALA   A N     1 
ATOM   6116  C  CA    . ALA   A  1 869  ? -33.005 79.261  81.754  1.00 18.66 ? 867  ALA   A CA    1 
ATOM   6117  C  C     . ALA   A  1 869  ? -33.044 80.322  82.843  1.00 18.43 ? 867  ALA   A C     1 
ATOM   6118  O  O     . ALA   A  1 869  ? -33.833 80.225  83.787  1.00 17.31 ? 867  ALA   A O     1 
ATOM   6119  C  CB    . ALA   A  1 869  ? -31.956 78.200  82.091  1.00 17.30 ? 867  ALA   A CB    1 
ATOM   6120  N  N     . LEU   A  1 870  ? -32.186 81.332  82.729  1.00 17.29 ? 868  LEU   A N     1 
ATOM   6121  C  CA    . LEU   A  1 870  ? -32.189 82.440  83.681  1.00 18.22 ? 868  LEU   A CA    1 
ATOM   6122  C  C     . LEU   A  1 870  ? -33.572 83.056  83.814  1.00 17.87 ? 868  LEU   A C     1 
ATOM   6123  O  O     . LEU   A  1 870  ? -34.021 83.367  84.919  1.00 17.60 ? 868  LEU   A O     1 
ATOM   6124  C  CB    . LEU   A  1 870  ? -31.200 83.514  83.219  1.00 15.94 ? 868  LEU   A CB    1 
ATOM   6125  C  CG    . LEU   A  1 870  ? -30.973 84.691  84.170  1.00 19.67 ? 868  LEU   A CG    1 
ATOM   6126  C  CD1   . LEU   A  1 870  ? -29.977 84.256  85.203  1.00 23.10 ? 868  LEU   A CD1   1 
ATOM   6127  C  CD2   . LEU   A  1 870  ? -30.439 85.923  83.436  1.00 22.40 ? 868  LEU   A CD2   1 
ATOM   6128  N  N     . HIS   A  1 871  ? -34.248 83.268  82.687  1.00 16.48 ? 869  HIS   A N     1 
ATOM   6129  C  CA    . HIS   A  1 871  ? -35.534 83.951  82.703  1.00 16.85 ? 869  HIS   A CA    1 
ATOM   6130  C  C     . HIS   A  1 871  ? -36.679 83.074  83.176  1.00 18.15 ? 869  HIS   A C     1 
ATOM   6131  O  O     . HIS   A  1 871  ? -37.798 83.576  83.300  1.00 21.79 ? 869  HIS   A O     1 
ATOM   6132  C  CB    . HIS   A  1 871  ? -35.824 84.515  81.323  1.00 19.23 ? 869  HIS   A CB    1 
ATOM   6133  C  CG    . HIS   A  1 871  ? -34.924 85.653  80.972  1.00 19.39 ? 869  HIS   A CG    1 
ATOM   6134  N  ND1   . HIS   A  1 871  ? -35.051 86.899  81.549  1.00 22.95 ? 869  HIS   A ND1   1 
ATOM   6135  C  CD2   . HIS   A  1 871  ? -33.850 85.726  80.149  1.00 22.40 ? 869  HIS   A CD2   1 
ATOM   6136  C  CE1   . HIS   A  1 871  ? -34.107 87.697  81.081  1.00 25.55 ? 869  HIS   A CE1   1 
ATOM   6137  N  NE2   . HIS   A  1 871  ? -33.364 87.010  80.233  1.00 24.73 ? 869  HIS   A NE2   1 
ATOM   6138  N  N     . GLU   A  1 872  ? -36.426 81.804  83.474  1.00 17.02 ? 870  GLU   A N     1 
ATOM   6139  C  CA    . GLU   A  1 872  ? -37.446 80.956  84.066  1.00 19.01 ? 870  GLU   A CA    1 
ATOM   6140  C  C     . GLU   A  1 872  ? -37.395 80.951  85.582  1.00 19.15 ? 870  GLU   A C     1 
ATOM   6141  O  O     . GLU   A  1 872  ? -38.206 80.266  86.206  1.00 18.20 ? 870  GLU   A O     1 
ATOM   6142  C  CB    . GLU   A  1 872  ? -37.321 79.525  83.533  1.00 17.08 ? 870  GLU   A CB    1 
ATOM   6143  C  CG    . GLU   A  1 872  ? -37.525 79.456  82.024  1.00 18.96 ? 870  GLU   A CG    1 
ATOM   6144  C  CD    . GLU   A  1 872  ? -38.924 79.903  81.604  1.00 22.73 ? 870  GLU   A CD    1 
ATOM   6145  O  OE1   . GLU   A  1 872  ? -39.848 79.844  82.441  1.00 22.72 ? 870  GLU   A OE1   1 
ATOM   6146  O  OE2   . GLU   A  1 872  ? -39.108 80.301  80.433  1.00 22.15 ? 870  GLU   A OE2   1 
ATOM   6147  N  N     . LEU   A  1 873  ? -36.486 81.712  86.186  1.00 18.77 ? 871  LEU   A N     1 
ATOM   6148  C  CA    . LEU   A  1 873  ? -36.366 81.726  87.639  1.00 17.61 ? 871  LEU   A CA    1 
ATOM   6149  C  C     . LEU   A  1 873  ? -37.374 82.684  88.256  1.00 18.18 ? 871  LEU   A C     1 
ATOM   6150  O  O     . LEU   A  1 873  ? -37.632 83.771  87.734  1.00 18.04 ? 871  LEU   A O     1 
ATOM   6151  C  CB    . LEU   A  1 873  ? -34.953 82.126  88.060  1.00 15.62 ? 871  LEU   A CB    1 
ATOM   6152  C  CG    . LEU   A  1 873  ? -33.880 81.185  87.496  1.00 15.83 ? 871  LEU   A CG    1 
ATOM   6153  C  CD1   . LEU   A  1 873  ? -32.483 81.750  87.772  1.00 18.17 ? 871  LEU   A CD1   1 
ATOM   6154  C  CD2   . LEU   A  1 873  ? -34.044 79.784  88.061  1.00 21.81 ? 871  LEU   A CD2   1 
ATOM   6155  N  N     . HIS   A  1 874  ? -37.929 82.273  89.386  1.00 20.02 ? 872  HIS   A N     1 
ATOM   6156  C  CA    . HIS   A  1 874  ? -38.877 83.079  90.136  1.00 20.94 ? 872  HIS   A CA    1 
ATOM   6157  C  C     . HIS   A  1 874  ? -38.142 83.677  91.331  1.00 17.59 ? 872  HIS   A C     1 
ATOM   6158  O  O     . HIS   A  1 874  ? -37.654 82.942  92.194  1.00 16.93 ? 872  HIS   A O     1 
ATOM   6159  C  CB    . HIS   A  1 874  ? -40.054 82.210  90.576  1.00 19.99 ? 872  HIS   A CB    1 
ATOM   6160  C  CG    . HIS   A  1 874  ? -41.105 82.931  91.362  1.00 22.72 ? 872  HIS   A CG    1 
ATOM   6161  N  ND1   . HIS   A  1 874  ? -42.295 82.333  91.718  1.00 23.60 ? 872  HIS   A ND1   1 
ATOM   6162  C  CD2   . HIS   A  1 874  ? -41.154 84.190  91.859  1.00 29.85 ? 872  HIS   A CD2   1 
ATOM   6163  C  CE1   . HIS   A  1 874  ? -43.030 83.190  92.405  1.00 27.39 ? 872  HIS   A CE1   1 
ATOM   6164  N  NE2   . HIS   A  1 874  ? -42.361 84.325  92.505  1.00 26.17 ? 872  HIS   A NE2   1 
ATOM   6165  N  N     . ILE   A  1 875  ? -38.059 84.999  91.374  1.00 18.36 ? 873  ILE   A N     1 
ATOM   6166  C  CA    . ILE   A  1 875  ? -37.392 85.722  92.452  1.00 19.61 ? 873  ILE   A CA    1 
ATOM   6167  C  C     . ILE   A  1 875  ? -38.470 86.374  93.305  1.00 19.58 ? 873  ILE   A C     1 
ATOM   6168  O  O     . ILE   A  1 875  ? -39.376 87.020  92.772  1.00 23.11 ? 873  ILE   A O     1 
ATOM   6169  C  CB    . ILE   A  1 875  ? -36.405 86.774  91.911  1.00 22.67 ? 873  ILE   A CB    1 
ATOM   6170  C  CG1   . ILE   A  1 875  ? -35.101 86.138  91.418  1.00 25.23 ? 873  ILE   A CG1   1 
ATOM   6171  C  CG2   . ILE   A  1 875  ? -36.041 87.775  92.992  1.00 22.48 ? 873  ILE   A CG2   1 
ATOM   6172  C  CD1   . ILE   A  1 875  ? -35.213 85.199  90.243  1.00 22.70 ? 873  ILE   A CD1   1 
ATOM   6173  N  N     . GLY   A  1 876  ? -38.376 86.211  94.620  1.00 20.04 ? 874  GLY   A N     1 
ATOM   6174  C  CA    . GLY   A  1 876  ? -39.340 86.853  95.499  1.00 19.32 ? 874  GLY   A CA    1 
ATOM   6175  C  C     . GLY   A  1 876  ? -39.097 86.458  96.940  1.00 21.93 ? 874  GLY   A C     1 
ATOM   6176  O  O     . GLY   A  1 876  ? -38.133 85.756  97.270  1.00 19.31 ? 874  GLY   A O     1 
ATOM   6177  N  N     . ARG   A  1 877  ? -39.992 86.932  97.801  1.00 21.66 ? 875  ARG   A N     1 
ATOM   6178  C  CA    . ARG   A  1 877  ? -39.949 86.543  99.201  1.00 21.70 ? 875  ARG   A CA    1 
ATOM   6179  C  C     . ARG   A  1 877  ? -40.084 85.031  99.309  1.00 17.73 ? 875  ARG   A C     1 
ATOM   6180  O  O     . ARG   A  1 877  ? -40.907 84.419  98.626  1.00 18.54 ? 875  ARG   A O     1 
ATOM   6181  C  CB    . ARG   A  1 877  ? -41.068 87.235  99.972  1.00 21.27 ? 875  ARG   A CB    1 
ATOM   6182  C  CG    . ARG   A  1 877  ? -40.814 87.232  101.461 1.00 24.03 ? 875  ARG   A CG    1 
ATOM   6183  C  CD    . ARG   A  1 877  ? -41.885 88.025  102.189 1.00 25.54 ? 875  ARG   A CD    1 
ATOM   6184  N  NE    . ARG   A  1 877  ? -43.146 87.307  102.282 1.00 24.33 ? 875  ARG   A NE    1 
ATOM   6185  C  CZ    . ARG   A  1 877  ? -44.224 87.799  102.875 1.00 33.45 ? 875  ARG   A CZ    1 
ATOM   6186  N  NH1   . ARG   A  1 877  ? -44.250 89.041  103.334 1.00 30.23 ? 875  ARG   A NH1   1 
ATOM   6187  N  NH2   . ARG   A  1 877  ? -45.298 87.024  103.018 1.00 31.41 ? 875  ARG   A NH2   1 
ATOM   6188  N  N     . THR   A  1 878  ? -39.249 84.421  100.147 1.00 19.45 ? 876  THR   A N     1 
ATOM   6189  C  CA    . THR   A  1 878  ? -39.027 82.984  100.068 1.00 20.00 ? 876  THR   A CA    1 
ATOM   6190  C  C     . THR   A  1 878  ? -40.026 82.157  100.865 1.00 19.78 ? 876  THR   A C     1 
ATOM   6191  O  O     . THR   A  1 878  ? -39.842 80.941  100.985 1.00 20.57 ? 876  THR   A O     1 
ATOM   6192  C  CB    . THR   A  1 878  ? -37.604 82.638  100.513 1.00 18.60 ? 876  THR   A CB    1 
ATOM   6193  O  OG1   . THR   A  1 878  ? -37.316 83.275  101.761 1.00 19.94 ? 876  THR   A OG1   1 
ATOM   6194  C  CG2   . THR   A  1 878  ? -36.607 83.101  99.470  1.00 21.07 ? 876  THR   A CG2   1 
ATOM   6195  N  N     . ASP   A  1 879  ? -41.085 82.762  101.382 1.00 18.41 ? 877  ASP   A N     1 
ATOM   6196  C  CA    . ASP   A  1 879  ? -42.104 81.964  102.050 1.00 21.82 ? 877  ASP   A CA    1 
ATOM   6197  C  C     . ASP   A  1 879  ? -43.104 81.420  101.036 1.00 21.42 ? 877  ASP   A C     1 
ATOM   6198  O  O     . ASP   A  1 879  ? -44.286 81.252  101.349 1.00 21.65 ? 877  ASP   A O     1 
ATOM   6199  C  CB    . ASP   A  1 879  ? -42.796 82.787  103.136 1.00 22.52 ? 877  ASP   A CB    1 
ATOM   6200  C  CG    . ASP   A  1 879  ? -43.551 83.980  102.572 1.00 25.80 ? 877  ASP   A CG    1 
ATOM   6201  O  OD1   . ASP   A  1 879  ? -43.093 84.572  101.573 1.00 26.52 ? 877  ASP   A OD1   1 
ATOM   6202  O  OD2   . ASP   A  1 879  ? -44.607 84.319  103.130 1.00 24.80 ? 877  ASP   A OD2   1 
ATOM   6203  N  N     . ARG   A  1 880  ? -42.640 81.151  99.813  1.00 21.59 ? 878  ARG   A N     1 
ATOM   6204  C  CA    . ARG   A  1 880  ? -43.433 80.506  98.770  1.00 21.33 ? 878  ARG   A CA    1 
ATOM   6205  C  C     . ARG   A  1 880  ? -42.575 79.425  98.138  1.00 19.68 ? 878  ARG   A C     1 
ATOM   6206  O  O     . ARG   A  1 880  ? -41.428 79.686  97.765  1.00 19.09 ? 878  ARG   A O     1 
ATOM   6207  C  CB    . ARG   A  1 880  ? -43.881 81.485  97.679  1.00 25.59 ? 878  ARG   A CB    1 
ATOM   6208  C  CG    . ARG   A  1 880  ? -45.143 82.284  97.962  1.00 31.66 ? 878  ARG   A CG    1 
ATOM   6209  C  CD    . ARG   A  1 880  ? -45.444 83.184  96.756  1.00 31.67 ? 878  ARG   A CD    1 
ATOM   6210  N  NE    . ARG   A  1 880  ? -46.570 84.079  96.990  1.00 46.56 ? 878  ARG   A NE    1 
ATOM   6211  C  CZ    . ARG   A  1 880  ? -47.802 83.866  96.547  1.00 45.71 ? 878  ARG   A CZ    1 
ATOM   6212  N  NH1   . ARG   A  1 880  ? -48.112 82.772  95.869  1.00 48.63 ? 878  ARG   A NH1   1 
ATOM   6213  N  NH2   . ARG   A  1 880  ? -48.744 84.777  96.781  1.00 47.27 ? 878  ARG   A NH2   1 
ATOM   6214  N  N     . LEU   A  1 881  ? -43.136 78.220  98.008  1.00 20.05 ? 879  LEU   A N     1 
ATOM   6215  C  CA    . LEU   A  1 881  ? -42.394 77.119  97.403  1.00 17.50 ? 879  LEU   A CA    1 
ATOM   6216  C  C     . LEU   A  1 881  ? -41.991 77.438  95.971  1.00 17.40 ? 879  LEU   A C     1 
ATOM   6217  O  O     . LEU   A  1 881  ? -40.955 76.958  95.487  1.00 15.80 ? 879  LEU   A O     1 
ATOM   6218  C  CB    . LEU   A  1 881  ? -43.238 75.850  97.439  1.00 15.91 ? 879  LEU   A CB    1 
ATOM   6219  C  CG    . LEU   A  1 881  ? -42.622 74.579  96.868  1.00 18.02 ? 879  LEU   A CG    1 
ATOM   6220  C  CD1   . LEU   A  1 881  ? -41.382 74.185  97.675  1.00 22.08 ? 879  LEU   A CD1   1 
ATOM   6221  C  CD2   . LEU   A  1 881  ? -43.671 73.476  96.896  1.00 18.38 ? 879  LEU   A CD2   1 
ATOM   6222  N  N     . SER   A  1 882  ? -42.781 78.253  95.286  1.00 18.61 ? 880  SER   A N     1 
ATOM   6223  C  CA    . SER   A  1 882  ? -42.489 78.582  93.899  1.00 18.47 ? 880  SER   A CA    1 
ATOM   6224  C  C     . SER   A  1 882  ? -41.284 79.500  93.746  1.00 20.43 ? 880  SER   A C     1 
ATOM   6225  O  O     . SER   A  1 882  ? -40.828 79.701  92.619  1.00 20.56 ? 880  SER   A O     1 
ATOM   6226  C  CB    . SER   A  1 882  ? -43.712 79.235  93.253  1.00 22.00 ? 880  SER   A CB    1 
ATOM   6227  O  OG    . SER   A  1 882  ? -44.038 80.443  93.924  1.00 21.48 ? 880  SER   A OG    1 
ATOM   6228  N  N     . VAL   A  1 883  ? -40.756 80.063  94.826  1.00 17.53 ? 881  VAL   A N     1 
ATOM   6229  C  CA    . VAL   A  1 883  ? -39.641 80.993  94.679  1.00 18.55 ? 881  VAL   A CA    1 
ATOM   6230  C  C     . VAL   A  1 883  ? -38.350 80.205  94.512  1.00 18.86 ? 881  VAL   A C     1 
ATOM   6231  O  O     . VAL   A  1 883  ? -38.040 79.315  95.311  1.00 21.84 ? 881  VAL   A O     1 
ATOM   6232  C  CB    . VAL   A  1 883  ? -39.557 81.956  95.872  1.00 19.90 ? 881  VAL   A CB    1 
ATOM   6233  C  CG1   . VAL   A  1 883  ? -38.200 82.655  95.863  1.00 17.30 ? 881  VAL   A CG1   1 
ATOM   6234  C  CG2   . VAL   A  1 883  ? -40.680 82.981  95.774  1.00 22.14 ? 881  VAL   A CG2   1 
ATOM   6235  N  N     . ASP   A  1 884  ? -37.601 80.525  93.463  1.00 16.12 ? 882  ASP   A N     1 
ATOM   6236  C  CA    . ASP   A  1 884  ? -36.315 79.883  93.210  1.00 19.54 ? 882  ASP   A CA    1 
ATOM   6237  C  C     . ASP   A  1 884  ? -35.162 80.623  93.859  1.00 20.23 ? 882  ASP   A C     1 
ATOM   6238  O  O     . ASP   A  1 884  ? -34.226 80.002  94.374  1.00 21.73 ? 882  ASP   A O     1 
ATOM   6239  C  CB    . ASP   A  1 884  ? -36.068 79.812  91.710  1.00 19.59 ? 882  ASP   A CB    1 
ATOM   6240  C  CG    . ASP   A  1 884  ? -37.142 79.038  90.995  1.00 20.38 ? 882  ASP   A CG    1 
ATOM   6241  O  OD1   . ASP   A  1 884  ? -37.384 77.873  91.391  1.00 22.39 ? 882  ASP   A OD1   1 
ATOM   6242  O  OD2   . ASP   A  1 884  ? -37.750 79.607  90.063  1.00 20.25 ? 882  ASP   A OD2   1 
ATOM   6243  N  N     . VAL   A  1 885  ? -35.192 81.944  93.798  1.00 16.97 ? 883  VAL   A N     1 
ATOM   6244  C  CA    . VAL   A  1 885  ? -34.087 82.763  94.263  1.00 18.15 ? 883  VAL   A CA    1 
ATOM   6245  C  C     . VAL   A  1 885  ? -34.661 83.842  95.156  1.00 18.62 ? 883  VAL   A C     1 
ATOM   6246  O  O     . VAL   A  1 885  ? -35.556 84.583  94.739  1.00 18.26 ? 883  VAL   A O     1 
ATOM   6247  C  CB    . VAL   A  1 885  ? -33.306 83.390  93.094  1.00 23.02 ? 883  VAL   A CB    1 
ATOM   6248  C  CG1   . VAL   A  1 885  ? -32.224 84.321  93.638  1.00 18.88 ? 883  VAL   A CG1   1 
ATOM   6249  C  CG2   . VAL   A  1 885  ? -32.705 82.298  92.198  1.00 20.80 ? 883  VAL   A CG2   1 
ATOM   6250  N  N     . GLY   A  1 886  ? -34.140 83.935  96.374  1.00 18.20 ? 884  GLY   A N     1 
ATOM   6251  C  CA    . GLY   A  1 886  ? -34.610 84.913  97.320  1.00 18.59 ? 884  GLY   A CA    1 
ATOM   6252  C  C     . GLY   A  1 886  ? -33.798 86.184  97.289  1.00 17.66 ? 884  GLY   A C     1 
ATOM   6253  O  O     . GLY   A  1 886  ? -33.034 86.445  96.352  1.00 18.35 ? 884  GLY   A O     1 
ATOM   6254  N  N     . PRO   A  1 887  ? -33.938 86.995  98.329  1.00 17.84 ? 885  PRO   A N     1 
ATOM   6255  C  CA    . PRO   A  1 887  ? -33.212 88.261  98.396  1.00 17.21 ? 885  PRO   A CA    1 
ATOM   6256  C  C     . PRO   A  1 887  ? -31.755 88.060  98.773  1.00 17.73 ? 885  PRO   A C     1 
ATOM   6257  O  O     . PRO   A  1 887  ? -31.359 87.021  99.302  1.00 17.16 ? 885  PRO   A O     1 
ATOM   6258  C  CB    . PRO   A  1 887  ? -33.946 89.006  99.514  1.00 17.52 ? 885  PRO   A CB    1 
ATOM   6259  C  CG    . PRO   A  1 887  ? -34.308 87.892  100.457 1.00 19.53 ? 885  PRO   A CG    1 
ATOM   6260  C  CD    . PRO   A  1 887  ? -34.717 86.752  99.554  1.00 20.91 ? 885  PRO   A CD    1 
ATOM   6261  N  N     . VAL   A  1 888  ? -30.960 89.104  98.520  1.00 17.66 ? 886  VAL   A N     1 
ATOM   6262  C  CA    . VAL   A  1 888  ? -29.669 89.180  99.182  1.00 17.39 ? 886  VAL   A CA    1 
ATOM   6263  C  C     . VAL   A  1 888  ? -29.865 89.742  100.590 1.00 17.65 ? 886  VAL   A C     1 
ATOM   6264  O  O     . VAL   A  1 888  ? -30.916 90.298  100.933 1.00 20.04 ? 886  VAL   A O     1 
ATOM   6265  C  CB    . VAL   A  1 888  ? -28.642 89.987  98.366  1.00 20.29 ? 886  VAL   A CB    1 
ATOM   6266  C  CG1   . VAL   A  1 888  ? -28.413 89.305  97.021  1.00 21.05 ? 886  VAL   A CG1   1 
ATOM   6267  C  CG2   . VAL   A  1 888  ? -29.072 91.425  98.172  1.00 18.87 ? 886  VAL   A CG2   1 
ATOM   6268  N  N     . ILE   A  1 889  ? -28.840 89.572  101.423 1.00 18.65 ? 887  ILE   A N     1 
ATOM   6269  C  CA    . ILE   A  1 889  ? -29.059 89.639  102.865 1.00 20.31 ? 887  ILE   A CA    1 
ATOM   6270  C  C     . ILE   A  1 889  ? -29.380 91.057  103.342 1.00 20.50 ? 887  ILE   A C     1 
ATOM   6271  O  O     . ILE   A  1 889  ? -30.175 91.237  104.278 1.00 22.26 ? 887  ILE   A O     1 
ATOM   6272  C  CB    . ILE   A  1 889  ? -27.842 89.038  103.602 1.00 20.31 ? 887  ILE   A CB    1 
ATOM   6273  C  CG1   . ILE   A  1 889  ? -28.141 88.925  105.099 1.00 21.41 ? 887  ILE   A CG1   1 
ATOM   6274  C  CG2   . ILE   A  1 889  ? -26.547 89.828  103.301 1.00 17.89 ? 887  ILE   A CG2   1 
ATOM   6275  C  CD1   . ILE   A  1 889  ? -29.252 87.922  105.389 1.00 21.49 ? 887  ILE   A CD1   1 
ATOM   6276  N  N     . THR   A  1 890  ? -28.792 92.082  102.731 1.00 18.68 ? 888  THR   A N     1 
ATOM   6277  C  CA    . THR   A  1 890  ? -28.948 93.448  103.225 1.00 20.10 ? 888  THR   A CA    1 
ATOM   6278  C  C     . THR   A  1 890  ? -28.961 94.416  102.053 1.00 21.04 ? 888  THR   A C     1 
ATOM   6279  O  O     . THR   A  1 890  ? -28.571 94.075  100.937 1.00 19.36 ? 888  THR   A O     1 
ATOM   6280  C  CB    . THR   A  1 890  ? -27.811 93.874  104.165 1.00 20.80 ? 888  THR   A CB    1 
ATOM   6281  O  OG1   . THR   A  1 890  ? -26.567 93.763  103.459 1.00 21.17 ? 888  THR   A OG1   1 
ATOM   6282  C  CG2   . THR   A  1 890  ? -27.760 93.018  105.416 1.00 25.41 ? 888  THR   A CG2   1 
ATOM   6283  N  N     . SER   A  1 891  ? -29.371 95.654  102.340 1.00 23.19 ? 889  SER   A N     1 
ATOM   6284  C  CA    A SER   A  1 891  ? -29.298 96.708  101.330 0.55 23.98 ? 889  SER   A CA    1 
ATOM   6285  C  CA    B SER   A  1 891  ? -29.301 96.700  101.326 0.45 23.97 ? 889  SER   A CA    1 
ATOM   6286  C  C     . SER   A  1 891  ? -27.858 96.987  100.933 1.00 23.51 ? 889  SER   A C     1 
ATOM   6287  O  O     . SER   A  1 891  ? -27.576 97.294  99.771  1.00 23.79 ? 889  SER   A O     1 
ATOM   6288  C  CB    A SER   A  1 891  ? -29.952 97.994  101.840 0.55 24.06 ? 889  SER   A CB    1 
ATOM   6289  C  CB    B SER   A  1 891  ? -29.978 97.972  101.833 0.45 24.06 ? 889  SER   A CB    1 
ATOM   6290  O  OG    A SER   A  1 891  ? -31.325 97.807  102.100 0.55 25.82 ? 889  SER   A OG    1 
ATOM   6291  O  OG    B SER   A  1 891  ? -29.319 98.448  102.992 0.45 25.81 ? 889  SER   A OG    1 
ATOM   6292  N  N     . GLU   A  1 892  ? -26.930 96.907  101.894 1.00 23.53 ? 890  GLU   A N     1 
ATOM   6293  C  CA    . GLU   A  1 892  ? -25.529 97.146  101.564 1.00 24.05 ? 890  GLU   A CA    1 
ATOM   6294  C  C     . GLU   A  1 892  ? -25.006 96.068  100.624 1.00 22.96 ? 890  GLU   A C     1 
ATOM   6295  O  O     . GLU   A  1 892  ? -24.254 96.364  99.689  1.00 22.26 ? 890  GLU   A O     1 
ATOM   6296  C  CB    . GLU   A  1 892  ? -24.674 97.209  102.830 1.00 24.72 ? 890  GLU   A CB    1 
ATOM   6297  C  CG    . GLU   A  1 892  ? -25.283 98.042  103.954 1.00 32.94 ? 890  GLU   A CG    1 
ATOM   6298  C  CD    . GLU   A  1 892  ? -26.232 97.230  104.835 1.00 30.88 ? 890  GLU   A CD    1 
ATOM   6299  O  OE1   . GLU   A  1 892  ? -25.741 96.382  105.616 1.00 49.14 ? 890  GLU   A OE1   1 
ATOM   6300  O  OE2   . GLU   A  1 892  ? -27.462 97.429  104.733 1.00 25.76 ? 890  GLU   A OE2   1 
ATOM   6301  N  N     . ALA   A  1 893  ? -25.377 94.810  100.868 1.00 21.26 ? 891  ALA   A N     1 
ATOM   6302  C  CA    . ALA   A  1 893  ? -25.006 93.743  99.944  1.00 20.96 ? 891  ALA   A CA    1 
ATOM   6303  C  C     . ALA   A  1 893  ? -25.573 94.025  98.562  1.00 23.81 ? 891  ALA   A C     1 
ATOM   6304  O  O     . ALA   A  1 893  ? -24.857 93.966  97.556  1.00 23.68 ? 891  ALA   A O     1 
ATOM   6305  C  CB    . ALA   A  1 893  ? -25.495 92.390  100.472 1.00 19.64 ? 891  ALA   A CB    1 
ATOM   6306  N  N     . LYS   A  1 894  ? -26.861 94.365  98.503  1.00 19.33 ? 892  LYS   A N     1 
ATOM   6307  C  CA    . LYS   A  1 894  ? -27.490 94.725  97.240  1.00 23.32 ? 892  LYS   A CA    1 
ATOM   6308  C  C     . LYS   A  1 894  ? -26.726 95.840  96.536  1.00 25.62 ? 892  LYS   A C     1 
ATOM   6309  O  O     . LYS   A  1 894  ? -26.392 95.723  95.351  1.00 24.25 ? 892  LYS   A O     1 
ATOM   6310  C  CB    . LYS   A  1 894  ? -28.941 95.132  97.488  1.00 21.08 ? 892  LYS   A CB    1 
ATOM   6311  C  CG    . LYS   A  1 894  ? -29.660 95.633  96.259  1.00 22.06 ? 892  LYS   A CG    1 
ATOM   6312  C  CD    . LYS   A  1 894  ? -31.139 95.867  96.551  1.00 22.06 ? 892  LYS   A CD    1 
ATOM   6313  C  CE    . LYS   A  1 894  ? -31.832 96.467  95.338  1.00 25.79 ? 892  LYS   A CE    1 
ATOM   6314  N  NZ    . LYS   A  1 894  ? -32.888 97.393  95.778  1.00 34.04 ? 892  LYS   A NZ    1 
ATOM   6315  N  N     . ASP   A  1 895  ? -26.417 96.925  97.258  1.00 23.65 ? 893  ASP   A N     1 
ATOM   6316  C  CA    . ASP   A  1 895  ? -25.724 98.052  96.634  1.00 26.66 ? 893  ASP   A CA    1 
ATOM   6317  C  C     . ASP   A  1 895  ? -24.346 97.655  96.114  1.00 24.89 ? 893  ASP   A C     1 
ATOM   6318  O  O     . ASP   A  1 895  ? -23.945 98.078  95.021  1.00 24.17 ? 893  ASP   A O     1 
ATOM   6319  C  CB    . ASP   A  1 895  ? -25.582 99.210  97.621  1.00 29.50 ? 893  ASP   A CB    1 
ATOM   6320  C  CG    . ASP   A  1 895  ? -26.898 99.911  97.899  1.00 38.33 ? 893  ASP   A CG    1 
ATOM   6321  O  OD1   . ASP   A  1 895  ? -27.856 99.766  97.097  1.00 44.46 ? 893  ASP   A OD1   1 
ATOM   6322  O  OD2   . ASP   A  1 895  ? -26.971 100.619 98.930  1.00 42.94 ? 893  ASP   A OD2   1 
ATOM   6323  N  N     . ASN   A  1 896  ? -23.590 96.885  96.900  1.00 22.95 ? 894  ASN   A N     1 
ATOM   6324  C  CA    . ASN   A  1 896  ? -22.273 96.439  96.458  1.00 22.84 ? 894  ASN   A CA    1 
ATOM   6325  C  C     . ASN   A  1 896  ? -22.379 95.609  95.185  1.00 26.07 ? 894  ASN   A C     1 
ATOM   6326  O  O     . ASN   A  1 896  ? -21.615 95.803  94.231  1.00 23.50 ? 894  ASN   A O     1 
ATOM   6327  C  CB    . ASN   A  1 896  ? -21.596 95.637  97.573  1.00 25.46 ? 894  ASN   A CB    1 
ATOM   6328  C  CG    . ASN   A  1 896  ? -20.247 95.048  97.148  1.00 36.68 ? 894  ASN   A CG    1 
ATOM   6329  O  OD1   . ASN   A  1 896  ? -20.184 93.997  96.505  1.00 40.78 ? 894  ASN   A OD1   1 
ATOM   6330  N  ND2   . ASN   A  1 896  ? -19.166 95.721  97.521  1.00 37.34 ? 894  ASN   A ND2   1 
ATOM   6331  N  N     . ILE   A  1 897  ? -23.333 94.678  95.148  1.00 22.93 ? 895  ILE   A N     1 
ATOM   6332  C  CA    . ILE   A  1 897  ? -23.486 93.833  93.968  1.00 21.99 ? 895  ILE   A CA    1 
ATOM   6333  C  C     . ILE   A  1 897  ? -23.904 94.667  92.760  1.00 24.44 ? 895  ILE   A C     1 
ATOM   6334  O  O     . ILE   A  1 897  ? -23.370 94.508  91.653  1.00 22.20 ? 895  ILE   A O     1 
ATOM   6335  C  CB    . ILE   A  1 897  ? -24.496 92.711  94.263  1.00 21.17 ? 895  ILE   A CB    1 
ATOM   6336  C  CG1   . ILE   A  1 897  ? -23.980 91.817  95.395  1.00 21.41 ? 895  ILE   A CG1   1 
ATOM   6337  C  CG2   . ILE   A  1 897  ? -24.759 91.905  93.011  1.00 19.84 ? 895  ILE   A CG2   1 
ATOM   6338  C  CD1   . ILE   A  1 897  ? -25.082 91.040  96.099  1.00 20.82 ? 895  ILE   A CD1   1 
ATOM   6339  N  N     . GLU   A  1 898  ? -24.864 95.567  92.949  1.00 22.43 ? 896  GLU   A N     1 
ATOM   6340  C  CA    . GLU   A  1 898  ? -25.354 96.343  91.817  1.00 23.18 ? 896  GLU   A CA    1 
ATOM   6341  C  C     . GLU   A  1 898  ? -24.292 97.290  91.287  1.00 24.61 ? 896  GLU   A C     1 
ATOM   6342  O  O     . GLU   A  1 898  ? -24.254 97.559  90.080  1.00 25.70 ? 896  GLU   A O     1 
ATOM   6343  C  CB    . GLU   A  1 898  ? -26.630 97.090  92.212  1.00 27.32 ? 896  GLU   A CB    1 
ATOM   6344  C  CG    . GLU   A  1 898  ? -27.807 96.118  92.352  1.00 27.74 ? 896  GLU   A CG    1 
ATOM   6345  C  CD    . GLU   A  1 898  ? -29.113 96.776  92.743  1.00 30.00 ? 896  GLU   A CD    1 
ATOM   6346  O  OE1   . GLU   A  1 898  ? -29.087 97.868  93.351  1.00 34.31 ? 896  GLU   A OE1   1 
ATOM   6347  O  OE2   . GLU   A  1 898  ? -30.168 96.184  92.439  1.00 39.14 ? 896  GLU   A OE2   1 
ATOM   6348  N  N     . LYS   A  1 899  ? -23.423 97.807  92.158  1.00 22.83 ? 897  LYS   A N     1 
ATOM   6349  C  CA    . LYS   A  1 899  ? -22.342 98.653  91.675  1.00 24.62 ? 897  LYS   A CA    1 
ATOM   6350  C  C     . LYS   A  1 899  ? -21.426 97.862  90.752  1.00 25.09 ? 897  LYS   A C     1 
ATOM   6351  O  O     . LYS   A  1 899  ? -20.962 98.377  89.728  1.00 28.07 ? 897  LYS   A O     1 
ATOM   6352  C  CB    . LYS   A  1 899  ? -21.556 99.241  92.847  1.00 24.62 ? 897  LYS   A CB    1 
ATOM   6353  N  N     . HIS   A  1 900  ? -21.159 96.604  91.096  1.00 24.02 ? 898  HIS   A N     1 
ATOM   6354  C  CA    . HIS   A  1 900  ? -20.351 95.772  90.217  1.00 25.49 ? 898  HIS   A CA    1 
ATOM   6355  C  C     . HIS   A  1 900  ? -21.032 95.589  88.868  1.00 25.39 ? 898  HIS   A C     1 
ATOM   6356  O  O     . HIS   A  1 900  ? -20.410 95.760  87.815  1.00 23.34 ? 898  HIS   A O     1 
ATOM   6357  C  CB    . HIS   A  1 900  ? -20.090 94.419  90.868  1.00 25.17 ? 898  HIS   A CB    1 
ATOM   6358  C  CG    . HIS   A  1 900  ? -19.407 93.453  89.960  1.00 25.65 ? 898  HIS   A CG    1 
ATOM   6359  N  ND1   . HIS   A  1 900  ? -18.075 93.568  89.629  1.00 25.13 ? 898  HIS   A ND1   1 
ATOM   6360  C  CD2   . HIS   A  1 900  ? -19.875 92.375  89.284  1.00 24.56 ? 898  HIS   A CD2   1 
ATOM   6361  C  CE1   . HIS   A  1 900  ? -17.744 92.587  88.806  1.00 29.66 ? 898  HIS   A CE1   1 
ATOM   6362  N  NE2   . HIS   A  1 900  ? -18.816 91.848  88.583  1.00 25.84 ? 898  HIS   A NE2   1 
ATOM   6363  N  N     . ILE   A  1 901  ? -22.324 95.259  88.883  1.00 22.27 ? 899  ILE   A N     1 
ATOM   6364  C  CA    . ILE   A  1 901  ? -23.033 95.004  87.633  1.00 23.88 ? 899  ILE   A CA    1 
ATOM   6365  C  C     . ILE   A  1 901  ? -23.016 96.239  86.748  1.00 25.94 ? 899  ILE   A C     1 
ATOM   6366  O  O     . ILE   A  1 901  ? -22.784 96.150  85.533  1.00 25.23 ? 899  ILE   A O     1 
ATOM   6367  C  CB    . ILE   A  1 901  ? -24.468 94.537  87.926  1.00 21.39 ? 899  ILE   A CB    1 
ATOM   6368  C  CG1   . ILE   A  1 901  ? -24.435 93.231  88.729  1.00 22.18 ? 899  ILE   A CG1   1 
ATOM   6369  C  CG2   . ILE   A  1 901  ? -25.236 94.372  86.618  1.00 24.03 ? 899  ILE   A CG2   1 
ATOM   6370  C  CD1   . ILE   A  1 901  ? -25.780 92.865  89.351  1.00 19.72 ? 899  ILE   A CD1   1 
ATOM   6371  N  N     . GLU   A  1 902  ? -23.245 97.413  87.341  1.00 24.04 ? 900  GLU   A N     1 
ATOM   6372  C  CA    . GLU   A  1 902  ? -23.257 98.640  86.554  1.00 28.56 ? 900  GLU   A CA    1 
ATOM   6373  C  C     . GLU   A  1 902  ? -21.869 98.991  86.035  1.00 26.24 ? 900  GLU   A C     1 
ATOM   6374  O  O     . GLU   A  1 902  ? -21.735 99.519  84.926  1.00 27.89 ? 900  GLU   A O     1 
ATOM   6375  C  CB    . GLU   A  1 902  ? -23.842 99.789  87.376  1.00 28.39 ? 900  GLU   A CB    1 
ATOM   6376  C  CG    . GLU   A  1 902  ? -25.311 99.591  87.661  1.00 31.80 ? 900  GLU   A CG    1 
ATOM   6377  C  CD    . GLU   A  1 902  ? -26.085 99.158  86.421  1.00 35.64 ? 900  GLU   A CD    1 
ATOM   6378  O  OE1   . GLU   A  1 902  ? -26.039 99.886  85.408  1.00 36.38 ? 900  GLU   A OE1   1 
ATOM   6379  O  OE2   . GLU   A  1 902  ? -26.733 98.088  86.458  1.00 35.25 ? 900  GLU   A OE2   1 
ATOM   6380  N  N     . ARG   A  1 903  ? -20.823 98.718  86.814  1.00 26.92 ? 901  ARG   A N     1 
ATOM   6381  C  CA    . ARG   A  1 903  ? -19.474 98.931  86.306  1.00 27.52 ? 901  ARG   A CA    1 
ATOM   6382  C  C     . ARG   A  1 903  ? -19.217 98.068  85.074  1.00 32.01 ? 901  ARG   A C     1 
ATOM   6383  O  O     . ARG   A  1 903  ? -18.717 98.556  84.053  1.00 29.36 ? 901  ARG   A O     1 
ATOM   6384  C  CB    . ARG   A  1 903  ? -18.442 98.646  87.400  1.00 28.83 ? 901  ARG   A CB    1 
ATOM   6385  N  N     . MET   A  1 904  ? -19.569 96.780  85.146  1.00 29.51 ? 902  MET   A N     1 
ATOM   6386  C  CA    . MET   A  1 904  ? -19.408 95.904  83.988  1.00 29.38 ? 902  MET   A CA    1 
ATOM   6387  C  C     . MET   A  1 904  ? -20.230 96.406  82.813  1.00 29.44 ? 902  MET   A C     1 
ATOM   6388  O  O     . MET   A  1 904  ? -19.747 96.455  81.675  1.00 29.92 ? 902  MET   A O     1 
ATOM   6389  C  CB    . MET   A  1 904  ? -19.808 94.471  84.341  1.00 25.66 ? 902  MET   A CB    1 
ATOM   6390  C  CG    . MET   A  1 904  ? -18.938 93.795  85.362  1.00 27.74 ? 902  MET   A CG    1 
ATOM   6391  S  SD    . MET   A  1 904  ? -17.225 93.633  84.835  1.00 35.10 ? 902  MET   A SD    1 
ATOM   6392  C  CE    . MET   A  1 904  ? -16.456 95.014  85.683  1.00 35.74 ? 902  MET   A CE    1 
ATOM   6393  N  N     . ARG   A  1 905  ? -21.477 96.798  83.074  1.00 25.70 ? 903  ARG   A N     1 
ATOM   6394  C  CA    . ARG   A  1 905  ? -22.312 97.324  82.006  1.00 28.04 ? 903  ARG   A CA    1 
ATOM   6395  C  C     . ARG   A  1 905  ? -21.700 98.587  81.420  1.00 29.60 ? 903  ARG   A C     1 
ATOM   6396  O  O     . ARG   A  1 905  ? -21.750 98.801  80.204  1.00 29.66 ? 903  ARG   A O     1 
ATOM   6397  C  CB    . ARG   A  1 905  ? -23.727 97.598  82.523  1.00 27.55 ? 903  ARG   A CB    1 
ATOM   6398  C  CG    . ARG   A  1 905  ? -24.757 97.706  81.414  1.00 30.28 ? 903  ARG   A CG    1 
ATOM   6399  C  CD    . ARG   A  1 905  ? -26.082 98.273  81.912  1.00 31.67 ? 903  ARG   A CD    1 
ATOM   6400  N  NE    . ARG   A  1 905  ? -26.545 97.654  83.149  1.00 32.10 ? 903  ARG   A NE    1 
ATOM   6401  C  CZ    . ARG   A  1 905  ? -27.321 96.581  83.209  1.00 29.34 ? 903  ARG   A CZ    1 
ATOM   6402  N  NH1   . ARG   A  1 905  ? -27.638 95.895  82.125  1.00 32.48 ? 903  ARG   A NH1   1 
ATOM   6403  N  NH2   . ARG   A  1 905  ? -27.803 96.195  84.387  1.00 35.11 ? 903  ARG   A NH2   1 
ATOM   6404  N  N     . GLY   A  1 906  ? -21.101 99.426  82.272  1.00 27.93 ? 904  GLY   A N     1 
ATOM   6405  C  CA    . GLY   A  1 906  ? -20.486 100.649 81.789  1.00 28.15 ? 904  GLY   A CA    1 
ATOM   6406  C  C     . GLY   A  1 906  ? -19.254 100.396 80.948  1.00 33.42 ? 904  GLY   A C     1 
ATOM   6407  O  O     . GLY   A  1 906  ? -18.906 101.217 80.093  1.00 35.18 ? 904  GLY   A O     1 
ATOM   6408  N  N     . LEU   A  1 907  ? -18.582 99.268  81.172  1.00 32.45 ? 905  LEU   A N     1 
ATOM   6409  C  CA    . LEU   A  1 907  ? -17.427 98.869  80.375  1.00 33.54 ? 905  LEU   A CA    1 
ATOM   6410  C  C     . LEU   A  1 907  ? -17.814 98.241  79.045  1.00 32.59 ? 905  LEU   A C     1 
ATOM   6411  O  O     . LEU   A  1 907  ? -16.927 97.844  78.285  1.00 37.72 ? 905  LEU   A O     1 
ATOM   6412  C  CB    . LEU   A  1 907  ? -16.552 97.892  81.163  1.00 32.86 ? 905  LEU   A CB    1 
ATOM   6413  C  CG    . LEU   A  1 907  ? -15.877 98.535  82.376  1.00 35.93 ? 905  LEU   A CG    1 
ATOM   6414  C  CD1   . LEU   A  1 907  ? -15.045 97.525  83.147  1.00 37.89 ? 905  LEU   A CD1   1 
ATOM   6415  C  CD2   . LEU   A  1 907  ? -15.039 99.719  81.936  1.00 36.56 ? 905  LEU   A CD2   1 
ATOM   6416  N  N     . GLY   A  1 908  ? -19.103 98.130  78.754  1.00 30.90 ? 906  GLY   A N     1 
ATOM   6417  C  CA    . GLY   A  1 908  ? -19.556 97.552  77.512  1.00 32.71 ? 906  GLY   A CA    1 
ATOM   6418  C  C     . GLY   A  1 908  ? -19.749 96.054  77.527  1.00 31.02 ? 906  GLY   A C     1 
ATOM   6419  O  O     . GLY   A  1 908  ? -20.009 95.477  76.468  1.00 29.35 ? 906  GLY   A O     1 
ATOM   6420  N  N     . ARG   A  1 909  ? -19.622 95.403  78.684  1.00 31.03 ? 907  ARG   A N     1 
ATOM   6421  C  CA    . ARG   A  1 909  ? -19.871 93.970  78.764  1.00 26.38 ? 907  ARG   A CA    1 
ATOM   6422  C  C     . ARG   A  1 909  ? -21.356 93.685  78.594  1.00 29.83 ? 907  ARG   A C     1 
ATOM   6423  O  O     . ARG   A  1 909  ? -22.210 94.438  79.076  1.00 31.18 ? 907  ARG   A O     1 
ATOM   6424  C  CB    . ARG   A  1 909  ? -19.393 93.405  80.104  1.00 27.63 ? 907  ARG   A CB    1 
ATOM   6425  C  CG    . ARG   A  1 909  ? -17.922 93.626  80.408  1.00 29.64 ? 907  ARG   A CG    1 
ATOM   6426  C  CD    . ARG   A  1 909  ? -17.033 93.108  79.291  1.00 36.84 ? 907  ARG   A CD    1 
ATOM   6427  N  NE    . ARG   A  1 909  ? -15.622 93.185  79.659  1.00 42.73 ? 907  ARG   A NE    1 
ATOM   6428  C  CZ    . ARG   A  1 909  ? -14.830 94.207  79.366  1.00 50.19 ? 907  ARG   A CZ    1 
ATOM   6429  N  NH1   . ARG   A  1 909  ? -15.271 95.250  78.681  1.00 46.93 ? 907  ARG   A NH1   1 
ATOM   6430  N  NH2   . ARG   A  1 909  ? -13.562 94.182  79.770  1.00 52.02 ? 907  ARG   A NH2   1 
ATOM   6431  N  N     . LYS   A  1 910  ? -21.664 92.591  77.903  1.00 25.41 ? 908  LYS   A N     1 
ATOM   6432  C  CA    . LYS   A  1 910  ? -23.050 92.170  77.772  1.00 27.23 ? 908  LYS   A CA    1 
ATOM   6433  C  C     . LYS   A  1 910  ? -23.560 91.673  79.117  1.00 25.73 ? 908  LYS   A C     1 
ATOM   6434  O  O     . LYS   A  1 910  ? -22.957 90.790  79.739  1.00 25.84 ? 908  LYS   A O     1 
ATOM   6435  C  CB    . LYS   A  1 910  ? -23.190 91.073  76.720  1.00 27.22 ? 908  LYS   A CB    1 
ATOM   6436  C  CG    . LYS   A  1 910  ? -22.765 91.486  75.334  1.00 35.63 ? 908  LYS   A CG    1 
ATOM   6437  C  CD    . LYS   A  1 910  ? -23.083 90.389  74.334  1.00 33.84 ? 908  LYS   A CD    1 
ATOM   6438  C  CE    . LYS   A  1 910  ? -24.526 89.947  74.451  1.00 35.82 ? 908  LYS   A CE    1 
ATOM   6439  N  NZ    . LYS   A  1 910  ? -24.907 89.104  73.274  1.00 51.21 ? 908  LYS   A NZ    1 
ATOM   6440  N  N     . VAL   A  1 911  ? -24.671 92.248  79.562  1.00 25.61 ? 909  VAL   A N     1 
ATOM   6441  C  CA    . VAL   A  1 911  ? -25.282 91.933  80.846  1.00 22.62 ? 909  VAL   A CA    1 
ATOM   6442  C  C     . VAL   A  1 911  ? -26.692 91.434  80.583  1.00 24.94 ? 909  VAL   A C     1 
ATOM   6443  O  O     . VAL   A  1 911  ? -27.481 92.113  79.915  1.00 24.30 ? 909  VAL   A O     1 
ATOM   6444  C  CB    . VAL   A  1 911  ? -25.307 93.160  81.775  1.00 25.20 ? 909  VAL   A CB    1 
ATOM   6445  C  CG1   . VAL   A  1 911  ? -26.052 92.831  83.065  1.00 22.91 ? 909  VAL   A CG1   1 
ATOM   6446  C  CG2   . VAL   A  1 911  ? -23.878 93.664  82.048  1.00 23.85 ? 909  VAL   A CG2   1 
ATOM   6447  N  N     . GLU   A  1 912  ? -26.995 90.246  81.086  1.00 19.63 ? 910  GLU   A N     1 
ATOM   6448  C  CA    . GLU   A  1 912  ? -28.321 89.658  81.006  1.00 19.88 ? 910  GLU   A CA    1 
ATOM   6449  C  C     . GLU   A  1 912  ? -28.906 89.622  82.407  1.00 20.90 ? 910  GLU   A C     1 
ATOM   6450  O  O     . GLU   A  1 912  ? -28.267 89.120  83.335  1.00 19.68 ? 910  GLU   A O     1 
ATOM   6451  C  CB    . GLU   A  1 912  ? -28.264 88.246  80.424  1.00 24.36 ? 910  GLU   A CB    1 
ATOM   6452  C  CG    . GLU   A  1 912  ? -29.624 87.641  80.153  1.00 22.38 ? 910  GLU   A CG    1 
ATOM   6453  C  CD    . GLU   A  1 912  ? -30.260 88.218  78.903  1.00 25.67 ? 910  GLU   A CD    1 
ATOM   6454  O  OE1   . GLU   A  1 912  ? -29.528 88.841  78.108  1.00 27.87 ? 910  GLU   A OE1   1 
ATOM   6455  O  OE2   . GLU   A  1 912  ? -31.483 88.046  78.717  1.00 28.26 ? 910  GLU   A OE2   1 
ATOM   6456  N  N     . GLN   A  1 913  ? -30.117 90.144  82.564  1.00 21.59 ? 911  GLN   A N     1 
ATOM   6457  C  CA    . GLN   A  1 913  ? -30.741 90.158  83.876  1.00 19.83 ? 911  GLN   A CA    1 
ATOM   6458  C  C     . GLN   A  1 913  ? -32.206 89.792  83.762  1.00 22.80 ? 911  GLN   A C     1 
ATOM   6459  O  O     . GLN   A  1 913  ? -32.886 90.217  82.827  1.00 23.93 ? 911  GLN   A O     1 
ATOM   6460  C  CB    . GLN   A  1 913  ? -30.633 91.538  84.541  1.00 23.50 ? 911  GLN   A CB    1 
ATOM   6461  C  CG    . GLN   A  1 913  ? -29.232 91.960  84.889  1.00 24.70 ? 911  GLN   A CG    1 
ATOM   6462  C  CD    . GLN   A  1 913  ? -29.241 93.171  85.793  1.00 25.84 ? 911  GLN   A CD    1 
ATOM   6463  O  OE1   . GLN   A  1 913  ? -29.688 94.239  85.401  1.00 29.54 ? 911  GLN   A OE1   1 
ATOM   6464  N  NE2   . GLN   A  1 913  ? -28.768 93.001  87.013  1.00 21.60 ? 911  GLN   A NE2   1 
ATOM   6465  N  N     . ILE   A  1 914  ? -32.686 89.017  84.732  1.00 22.76 ? 912  ILE   A N     1 
ATOM   6466  C  CA    . ILE   A  1 914  ? -34.116 88.770  84.848  1.00 22.58 ? 912  ILE   A CA    1 
ATOM   6467  C  C     . ILE   A  1 914  ? -34.796 90.028  85.369  1.00 27.91 ? 912  ILE   A C     1 
ATOM   6468  O  O     . ILE   A  1 914  ? -34.257 90.743  86.226  1.00 23.50 ? 912  ILE   A O     1 
ATOM   6469  C  CB    . ILE   A  1 914  ? -34.374 87.565  85.772  1.00 27.22 ? 912  ILE   A CB    1 
ATOM   6470  N  N     . GLY   A  1 915  ? -35.978 90.324  84.838  1.00 27.34 ? 913  GLY   A N     1 
ATOM   6471  C  CA    . GLY   A  1 915  ? -36.758 91.431  85.368  1.00 27.04 ? 913  GLY   A CA    1 
ATOM   6472  C  C     . GLY   A  1 915  ? -37.444 91.010  86.655  1.00 24.05 ? 913  GLY   A C     1 
ATOM   6473  O  O     . GLY   A  1 915  ? -37.975 89.907  86.766  1.00 27.58 ? 913  GLY   A O     1 
ATOM   6474  N  N     . LEU   A  1 916  ? -37.401 91.895  87.649  1.00 25.50 ? 914  LEU   A N     1 
ATOM   6475  C  CA    . LEU   A  1 916  ? -37.952 91.599  88.967  1.00 27.19 ? 914  LEU   A CA    1 
ATOM   6476  C  C     . LEU   A  1 916  ? -39.362 92.156  89.106  1.00 30.71 ? 914  LEU   A C     1 
ATOM   6477  O  O     . LEU   A  1 916  ? -39.680 93.215  88.560  1.00 28.76 ? 914  LEU   A O     1 
ATOM   6478  C  CB    . LEU   A  1 916  ? -37.074 92.174  90.075  1.00 28.30 ? 914  LEU   A CB    1 
ATOM   6479  C  CG    . LEU   A  1 916  ? -35.697 91.541  90.218  1.00 26.77 ? 914  LEU   A CG    1 
ATOM   6480  C  CD1   . LEU   A  1 916  ? -35.105 91.964  91.539  1.00 29.06 ? 914  LEU   A CD1   1 
ATOM   6481  C  CD2   . LEU   A  1 916  ? -35.805 90.020  90.099  1.00 25.98 ? 914  LEU   A CD2   1 
ATOM   6482  N  N     . ALA   A  1 917  ? -40.200 91.442  89.854  1.00 27.96 ? 915  ALA   A N     1 
ATOM   6483  C  CA    . ALA   A  1 917  ? -41.554 91.910  90.098  1.00 31.64 ? 915  ALA   A CA    1 
ATOM   6484  C  C     . ALA   A  1 917  ? -41.539 93.083  91.068  1.00 30.87 ? 915  ALA   A C     1 
ATOM   6485  O  O     . ALA   A  1 917  ? -40.595 93.275  91.842  1.00 28.06 ? 915  ALA   A O     1 
ATOM   6486  C  CB    . ALA   A  1 917  ? -42.426 90.783  90.647  1.00 31.04 ? 915  ALA   A CB    1 
ATOM   6487  N  N     . SER   A  1 918  ? -42.613 93.874  91.022  1.00 31.83 ? 916  SER   A N     1 
ATOM   6488  C  CA    . SER   A  1 918  ? -42.682 95.067  91.857  1.00 30.53 ? 916  SER   A CA    1 
ATOM   6489  C  C     . SER   A  1 918  ? -42.671 94.712  93.337  1.00 25.34 ? 916  SER   A C     1 
ATOM   6490  O  O     . SER   A  1 918  ? -42.126 95.466  94.149  1.00 27.35 ? 916  SER   A O     1 
ATOM   6491  C  CB    . SER   A  1 918  ? -43.933 95.872  91.510  1.00 32.50 ? 916  SER   A CB    1 
ATOM   6492  O  OG    . SER   A  1 918  ? -45.095 95.132  91.848  1.00 40.16 ? 916  SER   A OG    1 
ATOM   6493  N  N     . GLU   A  1 919  ? -43.231 93.555  93.696  1.00 29.70 ? 917  GLU   A N     1 
ATOM   6494  C  CA    . GLU   A  1 919  ? -43.253 93.110  95.086  1.00 30.69 ? 917  GLU   A CA    1 
ATOM   6495  C  C     . GLU   A  1 919  ? -41.858 92.971  95.680  1.00 32.10 ? 917  GLU   A C     1 
ATOM   6496  O  O     . GLU   A  1 919  ? -41.719 92.990  96.906  1.00 32.13 ? 917  GLU   A O     1 
ATOM   6497  C  CB    . GLU   A  1 919  ? -43.982 91.768  95.211  1.00 34.38 ? 917  GLU   A CB    1 
ATOM   6498  C  CG    . GLU   A  1 919  ? -45.495 91.848  95.043  1.00 46.13 ? 917  GLU   A CG    1 
ATOM   6499  C  CD    . GLU   A  1 919  ? -45.951 91.629  93.608  1.00 46.36 ? 917  GLU   A CD    1 
ATOM   6500  O  OE1   . GLU   A  1 919  ? -45.161 91.889  92.671  1.00 40.61 ? 917  GLU   A OE1   1 
ATOM   6501  O  OE2   . GLU   A  1 919  ? -47.107 91.185  93.420  1.00 53.24 ? 917  GLU   A OE2   1 
ATOM   6502  N  N     . THR   A  1 920  ? -40.822 92.810  94.856  1.00 26.73 ? 918  THR   A N     1 
ATOM   6503  C  CA    . THR   A  1 920  ? -39.490 92.733  95.442  1.00 25.48 ? 918  THR   A CA    1 
ATOM   6504  C  C     . THR   A  1 920  ? -39.055 94.053  96.059  1.00 27.44 ? 918  THR   A C     1 
ATOM   6505  O  O     . THR   A  1 920  ? -38.082 94.067  96.818  1.00 23.31 ? 918  THR   A O     1 
ATOM   6506  C  CB    . THR   A  1 920  ? -38.456 92.276  94.399  1.00 25.72 ? 918  THR   A CB    1 
ATOM   6507  O  OG1   . THR   A  1 920  ? -38.392 93.216  93.320  1.00 25.14 ? 918  THR   A OG1   1 
ATOM   6508  C  CG2   . THR   A  1 920  ? -38.819 90.896  93.860  1.00 25.43 ? 918  THR   A CG2   1 
ATOM   6509  N  N     . GLY   A  1 921  ? -39.779 95.147  95.794  1.00 26.60 ? 919  GLY   A N     1 
ATOM   6510  C  CA    . GLY   A  1 921  ? -39.350 96.446  96.281  1.00 27.32 ? 919  GLY   A CA    1 
ATOM   6511  C  C     . GLY   A  1 921  ? -39.261 96.542  97.791  1.00 23.60 ? 919  GLY   A C     1 
ATOM   6512  O  O     . GLY   A  1 921  ? -38.475 97.335  98.316  1.00 28.49 ? 919  GLY   A O     1 
ATOM   6513  N  N     . VAL   A  1 922  ? -40.055 95.742  98.511  1.00 23.77 ? 920  VAL   A N     1 
ATOM   6514  C  CA    . VAL   A  1 922  ? -40.079 95.824  99.973  1.00 23.95 ? 920  VAL   A CA    1 
ATOM   6515  C  C     . VAL   A  1 922  ? -38.913 95.093  100.624 1.00 22.22 ? 920  VAL   A C     1 
ATOM   6516  O  O     . VAL   A  1 922  ? -38.722 95.202  101.839 1.00 23.10 ? 920  VAL   A O     1 
ATOM   6517  C  CB    . VAL   A  1 922  ? -41.408 95.274  100.521 1.00 25.80 ? 920  VAL   A CB    1 
ATOM   6518  C  CG1   . VAL   A  1 922  ? -42.559 96.204  100.167 1.00 27.91 ? 920  VAL   A CG1   1 
ATOM   6519  C  CG2   . VAL   A  1 922  ? -41.656 93.880  99.974  1.00 23.93 ? 920  VAL   A CG2   1 
ATOM   6520  N  N     . GLY   A  1 923  ? -38.125 94.357  99.853  1.00 21.48 ? 921  GLY   A N     1 
ATOM   6521  C  CA    . GLY   A  1 923  ? -36.931 93.719  100.363 1.00 21.18 ? 921  GLY   A CA    1 
ATOM   6522  C  C     . GLY   A  1 923  ? -35.704 94.105  99.562  1.00 22.42 ? 921  GLY   A C     1 
ATOM   6523  O  O     . GLY   A  1 923  ? -35.719 95.105  98.841  1.00 22.60 ? 921  GLY   A O     1 
ATOM   6524  N  N     . THR   A  1 924  ? -34.631 93.323  99.668  1.00 20.44 ? 922  THR   A N     1 
ATOM   6525  C  CA    . THR   A  1 924  ? -33.363 93.675  99.033  1.00 21.51 ? 922  THR   A CA    1 
ATOM   6526  C  C     . THR   A  1 924  ? -33.003 92.559  98.058  1.00 21.02 ? 922  THR   A C     1 
ATOM   6527  O  O     . THR   A  1 924  ? -32.389 91.558  98.428  1.00 20.55 ? 922  THR   A O     1 
ATOM   6528  C  CB    . THR   A  1 924  ? -32.275 93.909  100.081 1.00 20.46 ? 922  THR   A CB    1 
ATOM   6529  O  OG1   . THR   A  1 924  ? -32.183 92.775  100.952 1.00 20.58 ? 922  THR   A OG1   1 
ATOM   6530  C  CG2   . THR   A  1 924  ? -32.613 95.143  100.913 1.00 22.29 ? 922  THR   A CG2   1 
ATOM   6531  N  N     . PHE   A  1 925  ? -33.384 92.744  96.803  1.00 19.21 ? 923  PHE   A N     1 
ATOM   6532  C  CA    . PHE   A  1 925  ? -33.187 91.733  95.776  1.00 20.59 ? 923  PHE   A CA    1 
ATOM   6533  C  C     . PHE   A  1 925  ? -32.236 92.242  94.708  1.00 20.27 ? 923  PHE   A C     1 
ATOM   6534  O  O     . PHE   A  1 925  ? -32.293 93.411  94.305  1.00 19.53 ? 923  PHE   A O     1 
ATOM   6535  C  CB    . PHE   A  1 925  ? -34.503 91.349  95.111  1.00 19.12 ? 923  PHE   A CB    1 
ATOM   6536  C  CG    . PHE   A  1 925  ? -35.453 90.668  96.020  1.00 19.10 ? 923  PHE   A CG    1 
ATOM   6537  C  CD1   . PHE   A  1 925  ? -36.239 91.400  96.905  1.00 19.64 ? 923  PHE   A CD1   1 
ATOM   6538  C  CD2   . PHE   A  1 925  ? -35.566 89.288  96.001  1.00 19.98 ? 923  PHE   A CD2   1 
ATOM   6539  C  CE1   . PHE   A  1 925  ? -37.136 90.758  97.744  1.00 19.05 ? 923  PHE   A CE1   1 
ATOM   6540  C  CE2   . PHE   A  1 925  ? -36.462 88.637  96.831  1.00 18.63 ? 923  PHE   A CE2   1 
ATOM   6541  C  CZ    . PHE   A  1 925  ? -37.241 89.371  97.709  1.00 20.09 ? 923  PHE   A CZ    1 
ATOM   6542  N  N     . VAL   A  1 926  ? -31.381 91.343  94.253  1.00 20.41 ? 924  VAL   A N     1 
ATOM   6543  C  CA    . VAL   A  1 926  ? -30.582 91.526  93.049  1.00 21.52 ? 924  VAL   A CA    1 
ATOM   6544  C  C     . VAL   A  1 926  ? -31.048 90.492  92.037  1.00 19.24 ? 924  VAL   A C     1 
ATOM   6545  O  O     . VAL   A  1 926  ? -31.096 89.299  92.363  1.00 19.96 ? 924  VAL   A O     1 
ATOM   6546  C  CB    . VAL   A  1 926  ? -29.078 91.374  93.329  1.00 18.68 ? 924  VAL   A CB    1 
ATOM   6547  C  CG1   . VAL   A  1 926  ? -28.280 91.490  92.037  1.00 21.05 ? 924  VAL   A CG1   1 
ATOM   6548  C  CG2   . VAL   A  1 926  ? -28.636 92.439  94.315  1.00 20.92 ? 924  VAL   A CG2   1 
ATOM   6549  N  N     . PRO   A  1 927  ? -31.429 90.891  90.837  1.00 20.43 ? 925  PRO   A N     1 
ATOM   6550  C  CA    . PRO   A  1 927  ? -31.830 89.908  89.850  1.00 21.86 ? 925  PRO   A CA    1 
ATOM   6551  C  C     . PRO   A  1 927  ? -30.647 89.045  89.462  1.00 16.96 ? 925  PRO   A C     1 
ATOM   6552  O  O     . PRO   A  1 927  ? -29.525 89.556  89.313  1.00 17.47 ? 925  PRO   A O     1 
ATOM   6553  C  CB    . PRO   A  1 927  ? -32.316 90.758  88.666  1.00 21.48 ? 925  PRO   A CB    1 
ATOM   6554  C  CG    . PRO   A  1 927  ? -31.695 92.067  88.828  1.00 25.17 ? 925  PRO   A CG    1 
ATOM   6555  C  CD    . PRO   A  1 927  ? -31.387 92.261  90.294  1.00 22.61 ? 925  PRO   A CD    1 
ATOM   6556  N  N     . PRO   A  1 928  ? -30.848 87.737  89.343  1.00 20.48 ? 926  PRO   A N     1 
ATOM   6557  C  CA    . PRO   A  1 928  ? -29.822 86.887  88.739  1.00 19.67 ? 926  PRO   A CA    1 
ATOM   6558  C  C     . PRO   A  1 928  ? -29.347 87.485  87.427  1.00 18.38 ? 926  PRO   A C     1 
ATOM   6559  O  O     . PRO   A  1 928  ? -30.142 87.917  86.590  1.00 18.27 ? 926  PRO   A O     1 
ATOM   6560  C  CB    . PRO   A  1 928  ? -30.551 85.556  88.540  1.00 18.82 ? 926  PRO   A CB    1 
ATOM   6561  C  CG    . PRO   A  1 928  ? -31.527 85.528  89.690  1.00 22.88 ? 926  PRO   A CG    1 
ATOM   6562  C  CD    . PRO   A  1 928  ? -32.001 86.956  89.815  1.00 18.83 ? 926  PRO   A CD    1 
ATOM   6563  N  N     . THR   A  1 929  ? -28.030 87.502  87.254  1.00 18.17 ? 927  THR   A N     1 
ATOM   6564  C  CA    . THR   A  1 929  ? -27.365 88.320  86.256  1.00 19.05 ? 927  THR   A CA    1 
ATOM   6565  C  C     . THR   A  1 929  ? -26.285 87.476  85.598  1.00 19.58 ? 927  THR   A C     1 
ATOM   6566  O  O     . THR   A  1 929  ? -25.618 86.699  86.278  1.00 18.95 ? 927  THR   A O     1 
ATOM   6567  C  CB    . THR   A  1 929  ? -26.747 89.565  86.912  1.00 18.83 ? 927  THR   A CB    1 
ATOM   6568  O  OG1   . THR   A  1 929  ? -27.790 90.372  87.473  1.00 21.33 ? 927  THR   A OG1   1 
ATOM   6569  C  CG2   . THR   A  1 929  ? -25.957 90.397  85.899  1.00 19.11 ? 927  THR   A CG2   1 
ATOM   6570  N  N     . ILE   A  1 930  ? -26.145 87.595  84.276  1.00 18.89 ? 928  ILE   A N     1 
ATOM   6571  C  CA    . ILE   A  1 930  ? -25.055 86.965  83.534  1.00 19.28 ? 928  ILE   A CA    1 
ATOM   6572  C  C     . ILE   A  1 930  ? -24.268 88.076  82.866  1.00 20.05 ? 928  ILE   A C     1 
ATOM   6573  O  O     . ILE   A  1 930  ? -24.851 88.918  82.173  1.00 20.87 ? 928  ILE   A O     1 
ATOM   6574  C  CB    . ILE   A  1 930  ? -25.567 85.966  82.480  1.00 16.61 ? 928  ILE   A CB    1 
ATOM   6575  C  CG1   . ILE   A  1 930  ? -26.330 84.826  83.143  1.00 16.73 ? 928  ILE   A CG1   1 
ATOM   6576  C  CG2   . ILE   A  1 930  ? -24.399 85.408  81.651  1.00 21.70 ? 928  ILE   A CG2   1 
ATOM   6577  C  CD1   . ILE   A  1 930  ? -27.245 84.063  82.165  1.00 21.91 ? 928  ILE   A CD1   1 
ATOM   6578  N  N     . ILE   A  1 931  ? -22.951 88.078  83.077  1.00 19.03 ? 929  ILE   A N     1 
ATOM   6579  C  CA    . ILE   A  1 931  ? -22.055 89.077  82.505  1.00 21.27 ? 929  ILE   A CA    1 
ATOM   6580  C  C     . ILE   A  1 931  ? -21.008 88.350  81.672  1.00 22.24 ? 929  ILE   A C     1 
ATOM   6581  O  O     . ILE   A  1 931  ? -20.293 87.482  82.186  1.00 22.15 ? 929  ILE   A O     1 
ATOM   6582  C  CB    . ILE   A  1 931  ? -21.375 89.932  83.586  1.00 24.19 ? 929  ILE   A CB    1 
ATOM   6583  C  CG1   . ILE   A  1 931  ? -22.418 90.579  84.503  1.00 20.06 ? 929  ILE   A CG1   1 
ATOM   6584  C  CG2   . ILE   A  1 931  ? -20.481 90.998  82.934  1.00 22.67 ? 929  ILE   A CG2   1 
ATOM   6585  C  CD1   . ILE   A  1 931  ? -21.811 91.340  85.673  1.00 23.15 ? 929  ILE   A CD1   1 
ATOM   6586  N  N     . GLU   A  1 932  ? -20.906 88.711  80.399  1.00 20.54 ? 930  GLU   A N     1 
ATOM   6587  C  CA    . GLU   A  1 932  ? -19.924 88.102  79.512  1.00 23.43 ? 930  GLU   A CA    1 
ATOM   6588  C  C     . GLU   A  1 932  ? -18.635 88.911  79.574  1.00 22.93 ? 930  GLU   A C     1 
ATOM   6589  O  O     . GLU   A  1 932  ? -18.626 90.107  79.256  1.00 25.16 ? 930  GLU   A O     1 
ATOM   6590  C  CB    . GLU   A  1 932  ? -20.484 88.018  78.094  1.00 22.15 ? 930  GLU   A CB    1 
ATOM   6591  C  CG    . GLU   A  1 932  ? -21.655 87.052  78.034  1.00 23.53 ? 930  GLU   A CG    1 
ATOM   6592  C  CD    . GLU   A  1 932  ? -22.448 87.153  76.752  1.00 30.43 ? 930  GLU   A CD    1 
ATOM   6593  O  OE1   . GLU   A  1 932  ? -21.834 87.069  75.668  1.00 31.30 ? 930  GLU   A OE1   1 
ATOM   6594  O  OE2   . GLU   A  1 932  ? -23.685 87.306  76.837  1.00 26.75 ? 930  GLU   A OE2   1 
ATOM   6595  N  N     . LEU   A  1 933  ? -17.564 88.273  80.019  1.00 22.85 ? 931  LEU   A N     1 
ATOM   6596  C  CA    . LEU   A  1 933  ? -16.278 88.937  80.161  1.00 26.37 ? 931  LEU   A CA    1 
ATOM   6597  C  C     . LEU   A  1 933  ? -15.382 88.598  78.982  1.00 30.24 ? 931  LEU   A C     1 
ATOM   6598  O  O     . LEU   A  1 933  ? -15.539 87.562  78.337  1.00 25.59 ? 931  LEU   A O     1 
ATOM   6599  C  CB    . LEU   A  1 933  ? -15.587 88.533  81.462  1.00 26.27 ? 931  LEU   A CB    1 
ATOM   6600  C  CG    . LEU   A  1 933  ? -16.339 88.873  82.754  1.00 30.39 ? 931  LEU   A CG    1 
ATOM   6601  C  CD1   . LEU   A  1 933  ? -15.500 88.468  83.949  1.00 31.10 ? 931  LEU   A CD1   1 
ATOM   6602  C  CD2   . LEU   A  1 933  ? -16.636 90.347  82.795  1.00 31.29 ? 931  LEU   A CD2   1 
ATOM   6603  N  N     . GLU   A  1 934  ? -14.429 89.495  78.710  1.00 31.69 ? 932  GLU   A N     1 
ATOM   6604  C  CA    . GLU   A  1 934  ? -13.407 89.217  77.704  1.00 35.80 ? 932  GLU   A CA    1 
ATOM   6605  C  C     . GLU   A  1 934  ? -12.338 88.282  78.258  1.00 43.73 ? 932  GLU   A C     1 
ATOM   6606  O  O     . GLU   A  1 934  ? -12.046 87.237  77.667  1.00 41.48 ? 932  GLU   A O     1 
ATOM   6607  C  CB    . GLU   A  1 934  ? -12.776 90.524  77.221  1.00 43.86 ? 932  GLU   A CB    1 
ATOM   6608  C  CG    . GLU   A  1 934  ? -13.732 91.413  76.450  1.00 43.85 ? 932  GLU   A CG    1 
ATOM   6609  C  CD    . GLU   A  1 934  ? -14.201 90.766  75.154  1.00 52.70 ? 932  GLU   A CD    1 
ATOM   6610  O  OE1   . GLU   A  1 934  ? -13.342 90.464  74.294  1.00 62.24 ? 932  GLU   A OE1   1 
ATOM   6611  O  OE2   . GLU   A  1 934  ? -15.424 90.544  75.000  1.00 55.18 ? 932  GLU   A OE2   1 
ATOM   6612  N  N     . LYS   A  1 935  ? -11.764 88.633  79.405  1.00 41.16 ? 933  LYS   A N     1 
ATOM   6613  C  CA    . LYS   A  1 935  ? -10.730 87.835  80.047  1.00 45.75 ? 933  LYS   A CA    1 
ATOM   6614  C  C     . LYS   A  1 935  ? -11.097 87.616  81.507  1.00 39.93 ? 933  LYS   A C     1 
ATOM   6615  O  O     . LYS   A  1 935  ? -11.783 88.439  82.116  1.00 35.37 ? 933  LYS   A O     1 
ATOM   6616  C  CB    . LYS   A  1 935  ? -9.354  88.514  79.952  1.00 44.19 ? 933  LYS   A CB    1 
ATOM   6617  N  N     . LEU   A  1 936  ? -10.634 86.494  82.066  1.00 40.66 ? 934  LEU   A N     1 
ATOM   6618  C  CA    . LEU   A  1 936  ? -10.845 86.252  83.489  1.00 42.48 ? 934  LEU   A CA    1 
ATOM   6619  C  C     . LEU   A  1 936  ? -10.290 87.384  84.341  1.00 41.94 ? 934  LEU   A C     1 
ATOM   6620  O  O     . LEU   A  1 936  ? -10.765 87.593  85.464  1.00 39.52 ? 934  LEU   A O     1 
ATOM   6621  C  CB    . LEU   A  1 936  ? -10.214 84.923  83.907  1.00 43.03 ? 934  LEU   A CB    1 
ATOM   6622  N  N     . SER   A  1 937  ? -9.317  88.136  83.817  1.00 43.79 ? 935  SER   A N     1 
ATOM   6623  C  CA    . SER   A  1 937  ? -8.739  89.262  84.542  1.00 42.73 ? 935  SER   A CA    1 
ATOM   6624  C  C     . SER   A  1 937  ? -9.684  90.457  84.623  1.00 40.97 ? 935  SER   A C     1 
ATOM   6625  O  O     . SER   A  1 937  ? -9.449  91.358  85.435  1.00 41.65 ? 935  SER   A O     1 
ATOM   6626  C  CB    . SER   A  1 937  ? -7.411  89.673  83.893  1.00 45.53 ? 935  SER   A CB    1 
ATOM   6627  O  OG    . SER   A  1 937  ? -7.483  89.606  82.475  1.00 44.14 ? 935  SER   A OG    1 
ATOM   6628  N  N     . ASP   A  1 938  ? -10.743 90.490  83.808  1.00 39.35 ? 936  ASP   A N     1 
ATOM   6629  C  CA    . ASP   A  1 938  ? -11.749 91.538  83.950  1.00 39.75 ? 936  ASP   A CA    1 
ATOM   6630  C  C     . ASP   A  1 938  ? -12.427 91.490  85.309  1.00 40.43 ? 936  ASP   A C     1 
ATOM   6631  O  O     . ASP   A  1 938  ? -12.982 92.501  85.754  1.00 40.98 ? 936  ASP   A O     1 
ATOM   6632  C  CB    . ASP   A  1 938  ? -12.819 91.419  82.864  1.00 40.85 ? 936  ASP   A CB    1 
ATOM   6633  C  CG    . ASP   A  1 938  ? -12.234 91.370  81.477  1.00 48.59 ? 936  ASP   A CG    1 
ATOM   6634  O  OD1   . ASP   A  1 938  ? -11.067 91.787  81.311  1.00 49.24 ? 936  ASP   A OD1   1 
ATOM   6635  O  OD2   . ASP   A  1 938  ? -12.945 90.916  80.551  1.00 47.77 ? 936  ASP   A OD2   1 
ATOM   6636  N  N     . LEU   A  1 939  ? -12.404 90.337  85.966  1.00 36.84 ? 937  LEU   A N     1 
ATOM   6637  C  CA    . LEU   A  1 939  ? -13.054 90.142  87.253  1.00 37.96 ? 937  LEU   A CA    1 
ATOM   6638  C  C     . LEU   A  1 939  ? -11.990 90.245  88.342  1.00 39.27 ? 937  LEU   A C     1 
ATOM   6639  O  O     . LEU   A  1 939  ? -11.108 89.386  88.444  1.00 41.95 ? 937  LEU   A O     1 
ATOM   6640  C  CB    . LEU   A  1 939  ? -13.767 88.795  87.284  1.00 34.73 ? 937  LEU   A CB    1 
ATOM   6641  C  CG    . LEU   A  1 939  ? -14.680 88.600  88.484  1.00 38.13 ? 937  LEU   A CG    1 
ATOM   6642  C  CD1   . LEU   A  1 939  ? -15.790 89.641  88.439  1.00 35.32 ? 937  LEU   A CD1   1 
ATOM   6643  C  CD2   . LEU   A  1 939  ? -15.246 87.198  88.480  1.00 32.72 ? 937  LEU   A CD2   1 
ATOM   6644  N  N     . GLN   A  1 940  ? -12.076 91.292  89.157  1.00 40.27 ? 938  GLN   A N     1 
ATOM   6645  C  CA    . GLN   A  1 940  ? -11.001 91.638  90.074  1.00 41.90 ? 938  GLN   A CA    1 
ATOM   6646  C  C     . GLN   A  1 940  ? -11.363 91.509  91.549  1.00 46.32 ? 938  GLN   A C     1 
ATOM   6647  O  O     . GLN   A  1 940  ? -10.524 91.825  92.400  1.00 45.85 ? 938  GLN   A O     1 
ATOM   6648  C  CB    . GLN   A  1 940  ? -10.520 93.068  89.791  1.00 43.53 ? 938  GLN   A CB    1 
ATOM   6649  N  N     . ARG   A  1 941  ? -12.568 91.054  91.885  1.00 41.76 ? 939  ARG   A N     1 
ATOM   6650  C  CA    . ARG   A  1 941  ? -12.957 90.915  93.283  1.00 42.11 ? 939  ARG   A CA    1 
ATOM   6651  C  C     . ARG   A  1 941  ? -14.164 89.990  93.368  1.00 36.44 ? 939  ARG   A C     1 
ATOM   6652  O  O     . ARG   A  1 941  ? -14.992 89.956  92.457  1.00 36.44 ? 939  ARG   A O     1 
ATOM   6653  C  CB    . ARG   A  1 941  ? -13.279 92.276  93.913  1.00 41.16 ? 939  ARG   A CB    1 
ATOM   6654  N  N     . GLU   A  1 942  ? -14.243 89.231  94.460  1.00 35.87 ? 940  GLU   A N     1 
ATOM   6655  C  CA    . GLU   A  1 942  ? -15.371 88.331  94.678  1.00 33.58 ? 940  GLU   A CA    1 
ATOM   6656  C  C     . GLU   A  1 942  ? -16.648 89.148  94.842  1.00 33.79 ? 940  GLU   A C     1 
ATOM   6657  O  O     . GLU   A  1 942  ? -16.726 90.025  95.710  1.00 35.02 ? 940  GLU   A O     1 
ATOM   6658  C  CB    . GLU   A  1 942  ? -15.131 87.449  95.905  1.00 35.35 ? 940  GLU   A CB    1 
ATOM   6659  C  CG    . GLU   A  1 942  ? -16.254 86.425  96.158  1.00 37.02 ? 940  GLU   A CG    1 
ATOM   6660  C  CD    . GLU   A  1 942  ? -16.209 85.786  97.547  1.00 37.51 ? 940  GLU   A CD    1 
ATOM   6661  O  OE1   . GLU   A  1 942  ? -15.962 86.503  98.547  1.00 43.72 ? 940  GLU   A OE1   1 
ATOM   6662  O  OE2   . GLU   A  1 942  ? -16.426 84.559  97.643  1.00 35.65 ? 940  GLU   A OE2   1 
ATOM   6663  N  N     . VAL   A  1 943  ? -17.646 88.869  94.006  1.00 28.95 ? 941  VAL   A N     1 
ATOM   6664  C  CA    . VAL   A  1 943  ? -18.929 89.561  94.054  1.00 28.22 ? 941  VAL   A CA    1 
ATOM   6665  C  C     . VAL   A  1 943  ? -19.943 88.578  94.611  1.00 27.97 ? 941  VAL   A C     1 
ATOM   6666  O  O     . VAL   A  1 943  ? -20.337 87.618  93.936  1.00 22.16 ? 941  VAL   A O     1 
ATOM   6667  C  CB    . VAL   A  1 943  ? -19.352 90.093  92.681  1.00 26.85 ? 941  VAL   A CB    1 
ATOM   6668  C  CG1   . VAL   A  1 943  ? -20.750 90.696  92.751  1.00 30.70 ? 941  VAL   A CG1   1 
ATOM   6669  C  CG2   . VAL   A  1 943  ? -18.353 91.122  92.197  1.00 28.90 ? 941  VAL   A CG2   1 
ATOM   6670  N  N     . PHE   A  1 944  ? -20.372 88.826  95.842  1.00 22.62 ? 942  PHE   A N     1 
ATOM   6671  C  CA    . PHE   A  1 944  ? -21.063 87.810  96.630  1.00 24.48 ? 942  PHE   A CA    1 
ATOM   6672  C  C     . PHE   A  1 944  ? -22.570 87.933  96.418  1.00 23.06 ? 942  PHE   A C     1 
ATOM   6673  O  O     . PHE   A  1 944  ? -23.334 88.347  97.293  1.00 24.49 ? 942  PHE   A O     1 
ATOM   6674  C  CB    . PHE   A  1 944  ? -20.685 87.938  98.097  1.00 24.42 ? 942  PHE   A CB    1 
ATOM   6675  C  CG    . PHE   A  1 944  ? -20.795 86.656  98.843  1.00 24.04 ? 942  PHE   A CG    1 
ATOM   6676  C  CD1   . PHE   A  1 944  ? -19.858 85.650  98.647  1.00 23.47 ? 942  PHE   A CD1   1 
ATOM   6677  C  CD2   . PHE   A  1 944  ? -21.835 86.444  99.732  1.00 23.48 ? 942  PHE   A CD2   1 
ATOM   6678  C  CE1   . PHE   A  1 944  ? -19.960 84.458  99.330  1.00 24.89 ? 942  PHE   A CE1   1 
ATOM   6679  C  CE2   . PHE   A  1 944  ? -21.940 85.259  100.415 1.00 22.49 ? 942  PHE   A CE2   1 
ATOM   6680  C  CZ    . PHE   A  1 944  ? -21.001 84.260  100.211 1.00 20.62 ? 942  PHE   A CZ    1 
ATOM   6681  N  N     . GLY   A  1 945  ? -22.988 87.566  95.209  1.00 19.26 ? 943  GLY   A N     1 
ATOM   6682  C  CA    . GLY   A  1 945  ? -24.375 87.669  94.838  1.00 20.27 ? 943  GLY   A CA    1 
ATOM   6683  C  C     . GLY   A  1 945  ? -24.666 86.847  93.604  1.00 18.79 ? 943  GLY   A C     1 
ATOM   6684  O  O     . GLY   A  1 945  ? -23.822 86.081  93.131  1.00 19.53 ? 943  GLY   A O     1 
ATOM   6685  N  N     . PRO   A  1 946  ? -25.866 87.001  93.054  1.00 17.51 ? 944  PRO   A N     1 
ATOM   6686  C  CA    . PRO   A  1 946  ? -26.312 86.126  91.959  1.00 16.35 ? 944  PRO   A CA    1 
ATOM   6687  C  C     . PRO   A  1 946  ? -25.818 86.655  90.620  1.00 17.98 ? 944  PRO   A C     1 
ATOM   6688  O  O     . PRO   A  1 946  ? -26.575 87.111  89.767  1.00 17.94 ? 944  PRO   A O     1 
ATOM   6689  C  CB    . PRO   A  1 946  ? -27.837 86.177  92.101  1.00 18.84 ? 944  PRO   A CB    1 
ATOM   6690  C  CG    . PRO   A  1 946  ? -28.099 87.583  92.589  1.00 18.56 ? 944  PRO   A CG    1 
ATOM   6691  C  CD    . PRO   A  1 946  ? -26.892 87.994  93.428  1.00 17.31 ? 944  PRO   A CD    1 
ATOM   6692  N  N     . VAL   A  1 947  ? -24.499 86.614  90.435  1.00 17.46 ? 945  VAL   A N     1 
ATOM   6693  C  CA    . VAL   A  1 947  ? -23.859 87.244  89.286  1.00 16.66 ? 945  VAL   A CA    1 
ATOM   6694  C  C     . VAL   A  1 947  ? -22.879 86.247  88.690  1.00 18.85 ? 945  VAL   A C     1 
ATOM   6695  O  O     . VAL   A  1 947  ? -21.823 85.984  89.271  1.00 22.54 ? 945  VAL   A O     1 
ATOM   6696  C  CB    . VAL   A  1 947  ? -23.143 88.546  89.657  1.00 20.01 ? 945  VAL   A CB    1 
ATOM   6697  C  CG1   . VAL   A  1 947  ? -22.503 89.170  88.419  1.00 21.00 ? 945  VAL   A CG1   1 
ATOM   6698  C  CG2   . VAL   A  1 947  ? -24.107 89.519  90.320  1.00 20.14 ? 945  VAL   A CG2   1 
ATOM   6699  N  N     . LEU   A  1 948  ? -23.219 85.712  87.532  1.00 18.49 ? 946  LEU   A N     1 
ATOM   6700  C  CA    . LEU   A  1 948  ? -22.387 84.753  86.822  1.00 16.27 ? 946  LEU   A CA    1 
ATOM   6701  C  C     . LEU   A  1 948  ? -21.596 85.485  85.752  1.00 18.22 ? 946  LEU   A C     1 
ATOM   6702  O  O     . LEU   A  1 948  ? -22.170 86.209  84.935  1.00 20.40 ? 946  LEU   A O     1 
ATOM   6703  C  CB    . LEU   A  1 948  ? -23.243 83.671  86.171  1.00 16.30 ? 946  LEU   A CB    1 
ATOM   6704  C  CG    . LEU   A  1 948  ? -22.416 82.663  85.375  1.00 17.52 ? 946  LEU   A CG    1 
ATOM   6705  C  CD1   . LEU   A  1 948  ? -21.525 81.832  86.316  1.00 16.00 ? 946  LEU   A CD1   1 
ATOM   6706  C  CD2   . LEU   A  1 948  ? -23.340 81.767  84.569  1.00 19.61 ? 946  LEU   A CD2   1 
ATOM   6707  N  N     . HIS   A  1 949  ? -20.289 85.295  85.755  1.00 17.97 ? 947  HIS   A N     1 
ATOM   6708  C  CA    . HIS   A  1 949  ? -19.445 85.813  84.696  1.00 19.00 ? 947  HIS   A CA    1 
ATOM   6709  C  C     . HIS   A  1 949  ? -19.113 84.673  83.756  1.00 18.12 ? 947  HIS   A C     1 
ATOM   6710  O  O     . HIS   A  1 949  ? -18.896 83.541  84.193  1.00 20.27 ? 947  HIS   A O     1 
ATOM   6711  C  CB    . HIS   A  1 949  ? -18.177 86.428  85.263  1.00 19.24 ? 947  HIS   A CB    1 
ATOM   6712  C  CG    . HIS   A  1 949  ? -18.453 87.463  86.299  1.00 22.02 ? 947  HIS   A CG    1 
ATOM   6713  N  ND1   . HIS   A  1 949  ? -18.740 87.138  87.605  1.00 21.85 ? 947  HIS   A ND1   1 
ATOM   6714  C  CD2   . HIS   A  1 949  ? -18.564 88.808  86.208  1.00 24.38 ? 947  HIS   A CD2   1 
ATOM   6715  C  CE1   . HIS   A  1 949  ? -18.972 88.245  88.287  1.00 23.53 ? 947  HIS   A CE1   1 
ATOM   6716  N  NE2   . HIS   A  1 949  ? -18.870 89.271  87.463  1.00 23.09 ? 947  HIS   A NE2   1 
ATOM   6717  N  N     . VAL   A  1 950  ? -19.099 84.972  82.463  1.00 20.78 ? 948  VAL   A N     1 
ATOM   6718  C  CA    . VAL   A  1 950  ? -18.888 83.965  81.435  1.00 19.60 ? 948  VAL   A CA    1 
ATOM   6719  C  C     . VAL   A  1 950  ? -17.703 84.391  80.590  1.00 21.32 ? 948  VAL   A C     1 
ATOM   6720  O  O     . VAL   A  1 950  ? -17.653 85.524  80.104  1.00 19.98 ? 948  VAL   A O     1 
ATOM   6721  C  CB    . VAL   A  1 950  ? -20.136 83.779  80.558  1.00 20.19 ? 948  VAL   A CB    1 
ATOM   6722  C  CG1   . VAL   A  1 950  ? -19.885 82.700  79.501  1.00 20.35 ? 948  VAL   A CG1   1 
ATOM   6723  C  CG2   . VAL   A  1 950  ? -21.347 83.418  81.421  1.00 16.82 ? 948  VAL   A CG2   1 
ATOM   6724  N  N     . ILE   A  1 951  ? -16.758 83.480  80.401  1.00 21.15 ? 949  ILE   A N     1 
ATOM   6725  C  CA    . ILE   A  1 951  ? -15.686 83.709  79.447  1.00 22.46 ? 949  ILE   A CA    1 
ATOM   6726  C  C     . ILE   A  1 951  ? -15.618 82.516  78.509  1.00 23.05 ? 949  ILE   A C     1 
ATOM   6727  O  O     . ILE   A  1 951  ? -16.098 81.423  78.814  1.00 20.79 ? 949  ILE   A O     1 
ATOM   6728  C  CB    . ILE   A  1 951  ? -14.330 83.940  80.130  1.00 26.04 ? 949  ILE   A CB    1 
ATOM   6729  C  CG1   . ILE   A  1 951  ? -13.897 82.693  80.877  1.00 24.00 ? 949  ILE   A CG1   1 
ATOM   6730  C  CG2   . ILE   A  1 951  ? -14.412 85.113  81.100  1.00 28.85 ? 949  ILE   A CG2   1 
ATOM   6731  C  CD1   . ILE   A  1 951  ? -12.618 82.907  81.654  1.00 31.83 ? 949  ILE   A CD1   1 
ATOM   6732  N  N     . ARG   A  1 952  ? -15.029 82.749  77.343  1.00 19.47 ? 950  ARG   A N     1 
ATOM   6733  C  CA    . ARG   A  1 952  ? -14.885 81.727  76.321  1.00 21.61 ? 950  ARG   A CA    1 
ATOM   6734  C  C     . ARG   A  1 952  ? -13.409 81.417  76.146  1.00 20.58 ? 950  ARG   A C     1 
ATOM   6735  O  O     . ARG   A  1 952  ? -12.567 82.299  76.292  1.00 20.45 ? 950  ARG   A O     1 
ATOM   6736  C  CB    . ARG   A  1 952  ? -15.487 82.206  74.999  1.00 26.03 ? 950  ARG   A CB    1 
ATOM   6737  C  CG    . ARG   A  1 952  ? -16.851 82.848  75.165  1.00 29.28 ? 950  ARG   A CG    1 
ATOM   6738  C  CD    . ARG   A  1 952  ? -17.106 83.867  74.076  1.00 31.59 ? 950  ARG   A CD    1 
ATOM   6739  N  NE    . ARG   A  1 952  ? -17.448 83.219  72.819  1.00 30.40 ? 950  ARG   A NE    1 
ATOM   6740  C  CZ    . ARG   A  1 952  ? -18.690 83.041  72.386  1.00 32.59 ? 950  ARG   A CZ    1 
ATOM   6741  N  NH1   . ARG   A  1 952  ? -19.733 83.483  73.072  1.00 32.19 ? 950  ARG   A NH1   1 
ATOM   6742  N  NH2   . ARG   A  1 952  ? -18.893 82.399  71.240  1.00 26.05 ? 950  ARG   A NH2   1 
ATOM   6743  N  N     . TYR   A  1 953  ? -13.087 80.164  75.849  1.00 21.54 ? 951  TYR   A N     1 
ATOM   6744  C  CA    . TYR   A  1 953  ? -11.688 79.812  75.639  1.00 23.65 ? 951  TYR   A CA    1 
ATOM   6745  C  C     . TYR   A  1 953  ? -11.557 78.901  74.428  1.00 22.56 ? 951  TYR   A C     1 
ATOM   6746  O  O     . TYR   A  1 953  ? -12.468 78.131  74.107  1.00 22.42 ? 951  TYR   A O     1 
ATOM   6747  C  CB    . TYR   A  1 953  ? -11.090 79.141  76.891  1.00 21.79 ? 951  TYR   A CB    1 
ATOM   6748  C  CG    . TYR   A  1 953  ? -11.594 77.740  77.144  1.00 20.65 ? 951  TYR   A CG    1 
ATOM   6749  C  CD1   . TYR   A  1 953  ? -12.803 77.520  77.801  1.00 18.01 ? 951  TYR   A CD1   1 
ATOM   6750  C  CD2   . TYR   A  1 953  ? -10.861 76.631  76.728  1.00 23.34 ? 951  TYR   A CD2   1 
ATOM   6751  C  CE1   . TYR   A  1 953  ? -13.262 76.234  78.040  1.00 18.42 ? 951  TYR   A CE1   1 
ATOM   6752  C  CE2   . TYR   A  1 953  ? -11.323 75.347  76.947  1.00 21.20 ? 951  TYR   A CE2   1 
ATOM   6753  C  CZ    . TYR   A  1 953  ? -12.523 75.152  77.605  1.00 20.68 ? 951  TYR   A CZ    1 
ATOM   6754  O  OH    . TYR   A  1 953  ? -12.976 73.872  77.834  1.00 20.73 ? 951  TYR   A OH    1 
ATOM   6755  N  N     . ARG   A  1 954  ? -10.419 79.015  73.741  1.00 23.84 ? 952  ARG   A N     1 
ATOM   6756  C  CA    . ARG   A  1 954  ? -10.083 78.080  72.676  1.00 26.18 ? 952  ARG   A CA    1 
ATOM   6757  C  C     . ARG   A  1 954  ? -9.551  76.782  73.266  1.00 25.06 ? 952  ARG   A C     1 
ATOM   6758  O  O     . ARG   A  1 954  ? -8.822  76.798  74.261  1.00 28.18 ? 952  ARG   A O     1 
ATOM   6759  C  CB    . ARG   A  1 954  ? -9.040  78.690  71.733  1.00 27.08 ? 952  ARG   A CB    1 
ATOM   6760  C  CG    . ARG   A  1 954  ? -9.568  79.826  70.870  1.00 34.69 ? 952  ARG   A CG    1 
ATOM   6761  C  CD    . ARG   A  1 954  ? -10.977 79.517  70.358  1.00 37.88 ? 952  ARG   A CD    1 
ATOM   6762  N  NE    . ARG   A  1 954  ? -11.129 79.649  68.913  1.00 47.10 ? 952  ARG   A NE    1 
ATOM   6763  C  CZ    . ARG   A  1 954  ? -11.181 80.806  68.264  1.00 49.78 ? 952  ARG   A CZ    1 
ATOM   6764  N  NH1   . ARG   A  1 954  ? -11.000 81.960  68.885  1.00 51.39 ? 952  ARG   A NH1   1 
ATOM   6765  N  NH2   . ARG   A  1 954  ? -11.423 80.805  66.958  1.00 50.58 ? 952  ARG   A NH2   1 
ATOM   6766  N  N     . ARG   A  1 955  ? -9.901  75.654  72.633  1.00 24.88 ? 953  ARG   A N     1 
ATOM   6767  C  CA    . ARG   A  1 955  ? -9.514  74.351  73.168  1.00 25.43 ? 953  ARG   A CA    1 
ATOM   6768  C  C     . ARG   A  1 955  ? -8.026  74.300  73.506  1.00 28.68 ? 953  ARG   A C     1 
ATOM   6769  O  O     . ARG   A  1 955  ? -7.645  73.892  74.605  1.00 29.00 ? 953  ARG   A O     1 
ATOM   6770  C  CB    . ARG   A  1 955  ? -9.874  73.239  72.180  1.00 30.44 ? 953  ARG   A CB    1 
ATOM   6771  C  CG    . ARG   A  1 955  ? -9.364  71.842  72.610  1.00 38.16 ? 953  ARG   A CG    1 
ATOM   6772  C  CD    . ARG   A  1 955  ? -9.747  71.579  74.056  1.00 39.67 ? 953  ARG   A CD    1 
ATOM   6773  N  NE    . ARG   A  1 955  ? -9.404  70.266  74.597  1.00 46.47 ? 953  ARG   A NE    1 
ATOM   6774  C  CZ    . ARG   A  1 955  ? -8.377  70.024  75.405  1.00 47.37 ? 953  ARG   A CZ    1 
ATOM   6775  N  NH1   . ARG   A  1 955  ? -7.481  70.959  75.691  1.00 45.14 ? 953  ARG   A NH1   1 
ATOM   6776  N  NH2   . ARG   A  1 955  ? -8.247  68.813  75.946  1.00 43.88 ? 953  ARG   A NH2   1 
ATOM   6777  N  N     . ASP   A  1 956  ? -7.167  74.746  72.587  1.00 26.60 ? 954  ASP   A N     1 
ATOM   6778  C  CA    . ASP   A  1 956  ? -5.733  74.636  72.851  1.00 26.49 ? 954  ASP   A CA    1 
ATOM   6779  C  C     . ASP   A  1 956  ? -5.266  75.508  74.006  1.00 28.32 ? 954  ASP   A C     1 
ATOM   6780  O  O     . ASP   A  1 956  ? -4.141  75.317  74.484  1.00 32.04 ? 954  ASP   A O     1 
ATOM   6781  C  CB    . ASP   A  1 956  ? -4.935  74.978  71.599  1.00 28.96 ? 954  ASP   A CB    1 
ATOM   6782  C  CG    . ASP   A  1 956  ? -5.154  73.974  70.488  1.00 35.36 ? 954  ASP   A CG    1 
ATOM   6783  O  OD1   . ASP   A  1 956  ? -5.641  72.861  70.784  1.00 35.18 ? 954  ASP   A OD1   1 
ATOM   6784  O  OD2   . ASP   A  1 956  ? -4.837  74.300  69.328  1.00 39.90 ? 954  ASP   A OD2   1 
ATOM   6785  N  N     . ASP   A  1 957  ? -6.084  76.453  74.464  1.00 23.73 ? 955  ASP   A N     1 
ATOM   6786  C  CA    . ASP   A  1 957  ? -5.714  77.308  75.578  1.00 25.96 ? 955  ASP   A CA    1 
ATOM   6787  C  C     . ASP   A  1 957  ? -6.218  76.791  76.919  1.00 23.37 ? 955  ASP   A C     1 
ATOM   6788  O  O     . ASP   A  1 957  ? -6.151  77.525  77.908  1.00 22.80 ? 955  ASP   A O     1 
ATOM   6789  C  CB    . ASP   A  1 957  ? -6.238  78.727  75.356  1.00 27.15 ? 955  ASP   A CB    1 
ATOM   6790  C  CG    . ASP   A  1 957  ? -5.537  79.435  74.225  1.00 31.55 ? 955  ASP   A CG    1 
ATOM   6791  O  OD1   . ASP   A  1 957  ? -4.388  79.068  73.911  1.00 34.96 ? 955  ASP   A OD1   1 
ATOM   6792  O  OD2   . ASP   A  1 957  ? -6.135  80.370  73.661  1.00 35.85 ? 955  ASP   A OD2   1 
ATOM   6793  N  N     . LEU   A  1 958  ? -6.722  75.556  76.977  1.00 24.32 ? 956  LEU   A N     1 
ATOM   6794  C  CA    . LEU   A  1 958  ? -7.233  75.023  78.237  1.00 22.70 ? 956  LEU   A CA    1 
ATOM   6795  C  C     . LEU   A  1 958  ? -6.203  75.143  79.351  1.00 22.13 ? 956  LEU   A C     1 
ATOM   6796  O  O     . LEU   A  1 958  ? -6.519  75.588  80.459  1.00 22.31 ? 956  LEU   A O     1 
ATOM   6797  C  CB    . LEU   A  1 958  ? -7.660  73.563  78.066  1.00 21.19 ? 956  LEU   A CB    1 
ATOM   6798  C  CG    . LEU   A  1 958  ? -8.225  72.847  79.294  1.00 24.33 ? 956  LEU   A CG    1 
ATOM   6799  C  CD1   . LEU   A  1 958  ? -9.389  73.632  79.890  1.00 23.82 ? 956  LEU   A CD1   1 
ATOM   6800  C  CD2   . LEU   A  1 958  ? -8.653  71.428  78.932  1.00 25.75 ? 956  LEU   A CD2   1 
ATOM   6801  N  N     . ASP   A  1 959  ? -4.953  74.756  79.074  1.00 23.55 ? 957  ASP   A N     1 
ATOM   6802  C  CA    . ASP   A  1 959  ? -3.964  74.745  80.143  1.00 25.64 ? 957  ASP   A CA    1 
ATOM   6803  C  C     . ASP   A  1 959  ? -3.683  76.153  80.645  1.00 24.30 ? 957  ASP   A C     1 
ATOM   6804  O  O     . ASP   A  1 959  ? -3.567  76.370  81.855  1.00 25.04 ? 957  ASP   A O     1 
ATOM   6805  C  CB    . ASP   A  1 959  ? -2.668  74.077  79.685  1.00 25.48 ? 957  ASP   A CB    1 
ATOM   6806  C  CG    . ASP   A  1 959  ? -1.796  73.693  80.857  1.00 27.87 ? 957  ASP   A CG    1 
ATOM   6807  O  OD1   . ASP   A  1 959  ? -2.300  72.993  81.761  1.00 28.02 ? 957  ASP   A OD1   1 
ATOM   6808  O  OD2   . ASP   A  1 959  ? -0.623  74.111  80.907  1.00 30.94 ? 957  ASP   A OD2   1 
ATOM   6809  N  N     . ARG   A  1 960  ? -3.583  77.127  79.733  1.00 24.34 ? 958  ARG   A N     1 
ATOM   6810  C  CA    . ARG   A  1 960  ? -3.433  78.509  80.171  1.00 23.26 ? 958  ARG   A CA    1 
ATOM   6811  C  C     . ARG   A  1 960  ? -4.658  78.970  80.950  1.00 24.68 ? 958  ARG   A C     1 
ATOM   6812  O  O     . ARG   A  1 960  ? -4.538  79.760  81.893  1.00 26.90 ? 958  ARG   A O     1 
ATOM   6813  C  CB    . ARG   A  1 960  ? -3.186  79.432  78.974  1.00 25.50 ? 958  ARG   A CB    1 
ATOM   6814  N  N     . LEU   A  1 961  ? -5.842  78.494  80.571  1.00 22.68 ? 959  LEU   A N     1 
ATOM   6815  C  CA    . LEU   A  1 961  ? -7.047  78.878  81.296  1.00 22.90 ? 959  LEU   A CA    1 
ATOM   6816  C  C     . LEU   A  1 961  ? -6.987  78.395  82.738  1.00 21.79 ? 959  LEU   A C     1 
ATOM   6817  O  O     . LEU   A  1 961  ? -7.255  79.159  83.672  1.00 23.40 ? 959  LEU   A O     1 
ATOM   6818  C  CB    . LEU   A  1 961  ? -8.281  78.327  80.585  1.00 22.38 ? 959  LEU   A CB    1 
ATOM   6819  C  CG    . LEU   A  1 961  ? -9.577  78.518  81.373  1.00 18.80 ? 959  LEU   A CG    1 
ATOM   6820  C  CD1   . LEU   A  1 961  ? -9.868  80.007  81.543  1.00 23.45 ? 959  LEU   A CD1   1 
ATOM   6821  C  CD2   . LEU   A  1 961  ? -10.719 77.802  80.684  1.00 23.80 ? 959  LEU   A CD2   1 
ATOM   6822  N  N     . VAL   A  1 962  ? -6.609  77.130  82.941  1.00 20.93 ? 960  VAL   A N     1 
ATOM   6823  C  CA    . VAL   A  1 962  ? -6.430  76.625  84.300  1.00 21.46 ? 960  VAL   A CA    1 
ATOM   6824  C  C     . VAL   A  1 962  ? -5.418  77.482  85.054  1.00 25.22 ? 960  VAL   A C     1 
ATOM   6825  O  O     . VAL   A  1 962  ? -5.618  77.808  86.231  1.00 24.84 ? 960  VAL   A O     1 
ATOM   6826  C  CB    . VAL   A  1 962  ? -6.023  75.141  84.259  1.00 23.27 ? 960  VAL   A CB    1 
ATOM   6827  C  CG1   . VAL   A  1 962  ? -5.651  74.629  85.672  1.00 25.08 ? 960  VAL   A CG1   1 
ATOM   6828  C  CG2   . VAL   A  1 962  ? -7.161  74.306  83.655  1.00 20.06 ? 960  VAL   A CG2   1 
ATOM   6829  N  N     . ASP   A  1 963  ? -4.336  77.887  84.374  1.00 24.07 ? 961  ASP   A N     1 
ATOM   6830  C  CA    . ASP   A  1 963  ? -3.372  78.829  84.952  1.00 26.16 ? 961  ASP   A CA    1 
ATOM   6831  C  C     . ASP   A  1 963  ? -4.045  80.122  85.398  1.00 28.51 ? 961  ASP   A C     1 
ATOM   6832  O  O     . ASP   A  1 963  ? -3.785  80.624  86.499  1.00 30.17 ? 961  ASP   A O     1 
ATOM   6833  C  CB    . ASP   A  1 963  ? -2.280  79.160  83.936  1.00 29.29 ? 961  ASP   A CB    1 
ATOM   6834  C  CG    . ASP   A  1 963  ? -1.217  78.115  83.864  1.00 34.25 ? 961  ASP   A CG    1 
ATOM   6835  O  OD1   . ASP   A  1 963  ? -1.223  77.209  84.717  1.00 36.45 ? 961  ASP   A OD1   1 
ATOM   6836  O  OD2   . ASP   A  1 963  ? -0.368  78.202  82.946  1.00 38.56 ? 961  ASP   A OD2   1 
ATOM   6837  N  N     . ASP   A  1 964  ? -4.890  80.694  84.533  1.00 26.98 ? 962  ASP   A N     1 
ATOM   6838  C  CA    . ASP   A  1 964  ? -5.581  81.943  84.858  1.00 30.35 ? 962  ASP   A CA    1 
ATOM   6839  C  C     . ASP   A  1 964  ? -6.552  81.767  86.020  1.00 29.11 ? 962  ASP   A C     1 
ATOM   6840  O  O     . ASP   A  1 964  ? -6.687  82.662  86.865  1.00 28.87 ? 962  ASP   A O     1 
ATOM   6841  C  CB    . ASP   A  1 964  ? -6.332  82.459  83.632  1.00 29.10 ? 962  ASP   A CB    1 
ATOM   6842  C  CG    . ASP   A  1 964  ? -5.404  82.871  82.514  1.00 34.26 ? 962  ASP   A CG    1 
ATOM   6843  O  OD1   . ASP   A  1 964  ? -4.179  82.979  82.753  1.00 36.20 ? 962  ASP   A OD1   1 
ATOM   6844  O  OD2   . ASP   A  1 964  ? -5.912  83.085  81.396  1.00 41.15 ? 962  ASP   A OD2   1 
ATOM   6845  N  N     . VAL   A  1 965  ? -7.252  80.634  86.071  1.00 23.63 ? 963  VAL   A N     1 
ATOM   6846  C  CA    . VAL   A  1 965  ? -8.111  80.355  87.217  1.00 28.69 ? 963  VAL   A CA    1 
ATOM   6847  C  C     . VAL   A  1 965  ? -7.284  80.302  88.494  1.00 29.02 ? 963  VAL   A C     1 
ATOM   6848  O  O     . VAL   A  1 965  ? -7.644  80.903  89.513  1.00 28.24 ? 963  VAL   A O     1 
ATOM   6849  C  CB    . VAL   A  1 965  ? -8.896  79.050  87.001  1.00 26.63 ? 963  VAL   A CB    1 
ATOM   6850  C  CG1   . VAL   A  1 965  ? -9.642  78.665  88.270  1.00 22.65 ? 963  VAL   A CG1   1 
ATOM   6851  C  CG2   . VAL   A  1 965  ? -9.866  79.201  85.849  1.00 23.87 ? 963  VAL   A CG2   1 
ATOM   6852  N  N     . ASN   A  1 966  ? -6.163  79.571  88.461  1.00 25.00 ? 964  ASN   A N     1 
ATOM   6853  C  CA    . ASN   A  1 966  ? -5.325  79.466  89.650  1.00 24.18 ? 964  ASN   A CA    1 
ATOM   6854  C  C     . ASN   A  1 966  ? -4.774  80.828  90.047  1.00 26.12 ? 964  ASN   A C     1 
ATOM   6855  O  O     . ASN   A  1 966  ? -4.604  81.103  91.240  1.00 25.14 ? 964  ASN   A O     1 
ATOM   6856  C  CB    . ASN   A  1 966  ? -4.168  78.484  89.415  1.00 25.46 ? 964  ASN   A CB    1 
ATOM   6857  C  CG    . ASN   A  1 966  ? -4.617  77.024  89.383  1.00 23.23 ? 964  ASN   A CG    1 
ATOM   6858  O  OD1   . ASN   A  1 966  ? -5.640  76.650  89.967  1.00 23.44 ? 964  ASN   A OD1   1 
ATOM   6859  N  ND2   . ASN   A  1 966  ? -3.836  76.189  88.710  1.00 25.80 ? 964  ASN   A ND2   1 
ATOM   6860  N  N     . ALA   A  1 967  ? -4.532  81.702  89.065  1.00 23.26 ? 965  ALA   A N     1 
ATOM   6861  C  CA    . ALA   A  1 967  ? -3.865  82.979  89.298  1.00 30.42 ? 965  ALA   A CA    1 
ATOM   6862  C  C     . ALA   A  1 967  ? -4.687  83.951  90.134  1.00 28.65 ? 965  ALA   A C     1 
ATOM   6863  O  O     . ALA   A  1 967  ? -4.121  84.930  90.632  1.00 32.99 ? 965  ALA   A O     1 
ATOM   6864  C  CB    . ALA   A  1 967  ? -3.494  83.633  87.963  1.00 30.78 ? 965  ALA   A CB    1 
ATOM   6865  N  N     . THR   A  1 968  ? -5.987  83.712  90.318  1.00 30.51 ? 966  THR   A N     1 
ATOM   6866  C  CA    . THR   A  1 968  ? -6.749  84.557  91.232  1.00 27.08 ? 966  THR   A CA    1 
ATOM   6867  C  C     . THR   A  1 968  ? -6.239  84.454  92.658  1.00 29.56 ? 966  THR   A C     1 
ATOM   6868  O  O     . THR   A  1 968  ? -6.512  85.348  93.462  1.00 32.68 ? 966  THR   A O     1 
ATOM   6869  C  CB    . THR   A  1 968  ? -8.236  84.193  91.239  1.00 30.88 ? 966  THR   A CB    1 
ATOM   6870  O  OG1   . THR   A  1 968  ? -8.402  82.913  91.865  1.00 31.39 ? 966  THR   A OG1   1 
ATOM   6871  C  CG2   . THR   A  1 968  ? -8.819  84.179  89.821  1.00 30.62 ? 966  THR   A CG2   1 
ATOM   6872  N  N     . GLY   A  1 969  ? -5.518  83.382  92.993  1.00 29.82 ? 967  GLY   A N     1 
ATOM   6873  C  CA    . GLY   A  1 969  ? -5.120  83.126  94.362  1.00 28.77 ? 967  GLY   A CA    1 
ATOM   6874  C  C     . GLY   A  1 969  ? -6.171  82.433  95.201  1.00 26.35 ? 967  GLY   A C     1 
ATOM   6875  O  O     . GLY   A  1 969  ? -5.859  81.983  96.315  1.00 26.44 ? 967  GLY   A O     1 
ATOM   6876  N  N     . TYR   A  1 970  ? -7.405  82.351  94.717  1.00 23.84 ? 968  TYR   A N     1 
ATOM   6877  C  CA    . TYR   A  1 970  ? -8.451  81.607  95.398  1.00 27.09 ? 968  TYR   A CA    1 
ATOM   6878  C  C     . TYR   A  1 970  ? -8.320  80.118  95.082  1.00 23.73 ? 968  TYR   A C     1 
ATOM   6879  O  O     . TYR   A  1 970  ? -7.533  79.702  94.233  1.00 26.93 ? 968  TYR   A O     1 
ATOM   6880  C  CB    . TYR   A  1 970  ? -9.826  82.129  94.985  1.00 23.61 ? 968  TYR   A CB    1 
ATOM   6881  C  CG    . TYR   A  1 970  ? -10.128 83.513  95.506  1.00 29.54 ? 968  TYR   A CG    1 
ATOM   6882  C  CD1   . TYR   A  1 970  ? -10.644 83.692  96.781  1.00 30.33 ? 968  TYR   A CD1   1 
ATOM   6883  C  CD2   . TYR   A  1 970  ? -9.901  84.639  94.727  1.00 31.54 ? 968  TYR   A CD2   1 
ATOM   6884  C  CE1   . TYR   A  1 970  ? -10.926 84.950  97.269  1.00 34.62 ? 968  TYR   A CE1   1 
ATOM   6885  C  CE2   . TYR   A  1 970  ? -10.180 85.908  95.211  1.00 32.77 ? 968  TYR   A CE2   1 
ATOM   6886  C  CZ    . TYR   A  1 970  ? -10.691 86.056  96.481  1.00 39.13 ? 968  TYR   A CZ    1 
ATOM   6887  O  OH    . TYR   A  1 970  ? -10.975 87.316  96.971  1.00 43.70 ? 968  TYR   A OH    1 
ATOM   6888  N  N     . GLY   A  1 971  ? -9.086  79.300  95.794  1.00 21.93 ? 969  GLY   A N     1 
ATOM   6889  C  CA    . GLY   A  1 971  ? -9.018  77.874  95.552  1.00 22.37 ? 969  GLY   A CA    1 
ATOM   6890  C  C     . GLY   A  1 971  ? -10.057 77.112  96.340  1.00 21.69 ? 969  GLY   A C     1 
ATOM   6891  O  O     . GLY   A  1 971  ? -9.727  76.205  97.107  1.00 21.66 ? 969  GLY   A O     1 
ATOM   6892  N  N     . LEU   A  1 972  ? -11.322 77.476  96.165  1.00 22.02 ? 970  LEU   A N     1 
ATOM   6893  C  CA    . LEU   A  1 972  ? -12.359 76.858  96.976  1.00 19.37 ? 970  LEU   A CA    1 
ATOM   6894  C  C     . LEU   A  1 972  ? -13.015 75.731  96.192  1.00 21.15 ? 970  LEU   A C     1 
ATOM   6895  O  O     . LEU   A  1 972  ? -12.631 74.564  96.319  1.00 20.00 ? 970  LEU   A O     1 
ATOM   6896  C  CB    . LEU   A  1 972  ? -13.393 77.897  97.405  1.00 20.94 ? 970  LEU   A CB    1 
ATOM   6897  C  CG    . LEU   A  1 972  ? -14.388 77.420  98.451  1.00 21.09 ? 970  LEU   A CG    1 
ATOM   6898  C  CD1   . LEU   A  1 972  ? -13.676 76.721  99.621  1.00 21.62 ? 970  LEU   A CD1   1 
ATOM   6899  C  CD2   . LEU   A  1 972  ? -15.162 78.633  98.943  1.00 25.68 ? 970  LEU   A CD2   1 
ATOM   6900  N  N     . THR   A  1 973  ? -14.002 76.068  95.372  1.00 21.89 ? 971  THR   A N     1 
ATOM   6901  C  CA    . THR   A  1 973  ? -14.678 75.070  94.565  1.00 16.78 ? 971  THR   A CA    1 
ATOM   6902  C  C     . THR   A  1 973  ? -14.329 75.272  93.100  1.00 16.02 ? 971  THR   A C     1 
ATOM   6903  O  O     . THR   A  1 973  ? -14.050 76.384  92.641  1.00 16.81 ? 971  THR   A O     1 
ATOM   6904  C  CB    . THR   A  1 973  ? -16.196 75.122  94.732  1.00 17.04 ? 971  THR   A CB    1 
ATOM   6905  O  OG1   . THR   A  1 973  ? -16.665 76.425  94.372  1.00 20.00 ? 971  THR   A OG1   1 
ATOM   6906  C  CG2   . THR   A  1 973  ? -16.575 74.829  96.170  1.00 18.75 ? 971  THR   A CG2   1 
ATOM   6907  N  N     . PHE   A  1 974  ? -14.372 74.171  92.368  1.00 15.54 ? 972  PHE   A N     1 
ATOM   6908  C  CA    . PHE   A  1 974  ? -14.046 74.188  90.961  1.00 16.16 ? 972  PHE   A CA    1 
ATOM   6909  C  C     . PHE   A  1 974  ? -14.894 73.115  90.320  1.00 15.10 ? 972  PHE   A C     1 
ATOM   6910  O  O     . PHE   A  1 974  ? -15.024 72.026  90.875  1.00 15.99 ? 972  PHE   A O     1 
ATOM   6911  C  CB    . PHE   A  1 974  ? -12.564 73.905  90.713  1.00 15.36 ? 972  PHE   A CB    1 
ATOM   6912  C  CG    . PHE   A  1 974  ? -12.250 73.736  89.268  1.00 15.42 ? 972  PHE   A CG    1 
ATOM   6913  C  CD1   . PHE   A  1 974  ? -12.138 74.845  88.454  1.00 15.56 ? 972  PHE   A CD1   1 
ATOM   6914  C  CD2   . PHE   A  1 974  ? -12.124 72.473  88.713  1.00 17.83 ? 972  PHE   A CD2   1 
ATOM   6915  C  CE1   . PHE   A  1 974  ? -11.893 74.706  87.108  1.00 18.72 ? 972  PHE   A CE1   1 
ATOM   6916  C  CE2   . PHE   A  1 974  ? -11.870 72.316  87.358  1.00 16.65 ? 972  PHE   A CE2   1 
ATOM   6917  C  CZ    . PHE   A  1 974  ? -11.746 73.430  86.561  1.00 21.23 ? 972  PHE   A CZ    1 
ATOM   6918  N  N     . GLY   A  1 975  ? -15.463 73.413  89.156  1.00 16.67 ? 973  GLY   A N     1 
ATOM   6919  C  CA    . GLY   A  1 975  ? -16.270 72.453  88.435  1.00 16.13 ? 973  GLY   A CA    1 
ATOM   6920  C  C     . GLY   A  1 975  ? -15.713 72.178  87.054  1.00 15.71 ? 973  GLY   A C     1 
ATOM   6921  O  O     . GLY   A  1 975  ? -15.151 73.056  86.406  1.00 15.65 ? 973  GLY   A O     1 
ATOM   6922  N  N     . LEU   A  1 976  ? -15.879 70.940  86.607  1.00 15.01 ? 974  LEU   A N     1 
ATOM   6923  C  CA    . LEU   A  1 976  ? -15.466 70.563  85.266  1.00 15.10 ? 974  LEU   A CA    1 
ATOM   6924  C  C     . LEU   A  1 976  ? -16.561 69.710  84.661  1.00 17.03 ? 974  LEU   A C     1 
ATOM   6925  O  O     . LEU   A  1 976  ? -16.981 68.707  85.254  1.00 14.90 ? 974  LEU   A O     1 
ATOM   6926  C  CB    . LEU   A  1 976  ? -14.129 69.817  85.285  1.00 18.13 ? 974  LEU   A CB    1 
ATOM   6927  C  CG    . LEU   A  1 976  ? -13.668 69.241  83.944  1.00 19.43 ? 974  LEU   A CG    1 
ATOM   6928  C  CD1   . LEU   A  1 976  ? -13.303 70.338  82.949  1.00 18.96 ? 974  LEU   A CD1   1 
ATOM   6929  C  CD2   . LEU   A  1 976  ? -12.501 68.311  84.200  1.00 16.30 ? 974  LEU   A CD2   1 
ATOM   6930  N  N     . HIS   A  1 977  ? -17.048 70.135  83.502  1.00 17.52 ? 975  HIS   A N     1 
ATOM   6931  C  CA    . HIS   A  1 977  ? -17.993 69.353  82.725  1.00 16.02 ? 975  HIS   A CA    1 
ATOM   6932  C  C     . HIS   A  1 977  ? -17.285 68.869  81.476  1.00 16.72 ? 975  HIS   A C     1 
ATOM   6933  O  O     . HIS   A  1 977  ? -16.937 69.666  80.595  1.00 15.90 ? 975  HIS   A O     1 
ATOM   6934  C  CB    . HIS   A  1 977  ? -19.229 70.167  82.376  1.00 17.18 ? 975  HIS   A CB    1 
ATOM   6935  C  CG    . HIS   A  1 977  ? -20.323 70.016  83.375  1.00 18.43 ? 975  HIS   A CG    1 
ATOM   6936  N  ND1   . HIS   A  1 977  ? -21.434 69.237  83.145  1.00 23.35 ? 975  HIS   A ND1   1 
ATOM   6937  C  CD2   . HIS   A  1 977  ? -20.457 70.507  84.628  1.00 22.05 ? 975  HIS   A CD2   1 
ATOM   6938  C  CE1   . HIS   A  1 977  ? -22.227 69.293  84.199  1.00 21.16 ? 975  HIS   A CE1   1 
ATOM   6939  N  NE2   . HIS   A  1 977  ? -21.659 70.058  85.110  1.00 20.51 ? 975  HIS   A NE2   1 
ATOM   6940  N  N     . THR   A  1 978  ? -17.065 67.564  81.417  1.00 15.79 ? 976  THR   A N     1 
ATOM   6941  C  CA    . THR   A  1 978  ? -16.462 66.948  80.252  1.00 17.12 ? 976  THR   A CA    1 
ATOM   6942  C  C     . THR   A  1 978  ? -16.764 65.467  80.331  1.00 16.98 ? 976  THR   A C     1 
ATOM   6943  O  O     . THR   A  1 978  ? -16.976 64.922  81.415  1.00 18.09 ? 976  THR   A O     1 
ATOM   6944  C  CB    . THR   A  1 978  ? -14.943 67.176  80.182  1.00 18.26 ? 976  THR   A CB    1 
ATOM   6945  O  OG1   . THR   A  1 978  ? -14.420 66.508  79.023  1.00 17.80 ? 976  THR   A OG1   1 
ATOM   6946  C  CG2   . THR   A  1 978  ? -14.265 66.594  81.394  1.00 19.38 ? 976  THR   A CG2   1 
ATOM   6947  N  N     . ARG   A  1 979  ? -16.792 64.823  79.177  1.00 19.17 ? 977  ARG   A N     1 
ATOM   6948  C  CA    . ARG   A  1 979  ? -16.885 63.375  79.144  1.00 22.90 ? 977  ARG   A CA    1 
ATOM   6949  C  C     . ARG   A  1 979  ? -15.543 62.706  78.880  1.00 20.61 ? 977  ARG   A C     1 
ATOM   6950  O  O     . ARG   A  1 979  ? -15.489 61.474  78.816  1.00 21.87 ? 977  ARG   A O     1 
ATOM   6951  C  CB    . ARG   A  1 979  ? -17.914 62.949  78.092  1.00 24.93 ? 977  ARG   A CB    1 
ATOM   6952  C  CG    . ARG   A  1 979  ? -19.320 63.463  78.430  1.00 30.00 ? 977  ARG   A CG    1 
ATOM   6953  C  CD    . ARG   A  1 979  ? -20.395 62.808  77.592  1.00 35.51 ? 977  ARG   A CD    1 
ATOM   6954  N  NE    . ARG   A  1 979  ? -20.788 63.636  76.459  1.00 39.53 ? 977  ARG   A NE    1 
ATOM   6955  C  CZ    . ARG   A  1 979  ? -21.695 63.289  75.554  1.00 41.04 ? 977  ARG   A CZ    1 
ATOM   6956  N  NH1   . ARG   A  1 979  ? -22.302 62.112  75.596  1.00 37.59 ? 977  ARG   A NH1   1 
ATOM   6957  N  NH2   . ARG   A  1 979  ? -22.006 64.147  74.585  1.00 47.32 ? 977  ARG   A NH2   1 
ATOM   6958  N  N     . LEU   A  1 980  ? -14.461 63.480  78.765  1.00 16.91 ? 978  LEU   A N     1 
ATOM   6959  C  CA    . LEU   A  1 980  ? -13.178 62.987  78.267  1.00 18.58 ? 978  LEU   A CA    1 
ATOM   6960  C  C     . LEU   A  1 980  ? -12.194 62.797  79.420  1.00 19.09 ? 978  LEU   A C     1 
ATOM   6961  O  O     . LEU   A  1 980  ? -11.839 63.766  80.095  1.00 18.27 ? 978  LEU   A O     1 
ATOM   6962  C  CB    . LEU   A  1 980  ? -12.605 63.963  77.239  1.00 18.93 ? 978  LEU   A CB    1 
ATOM   6963  C  CG    . LEU   A  1 980  ? -13.558 64.310  76.094  1.00 20.94 ? 978  LEU   A CG    1 
ATOM   6964  C  CD1   . LEU   A  1 980  ? -12.923 65.335  75.145  1.00 21.83 ? 978  LEU   A CD1   1 
ATOM   6965  C  CD2   . LEU   A  1 980  ? -13.971 63.039  75.341  1.00 21.90 ? 978  LEU   A CD2   1 
ATOM   6966  N  N     . ASP   A  1 981  ? -11.741 61.553  79.630  1.00 19.22 ? 979  ASP   A N     1 
ATOM   6967  C  CA    . ASP   A  1 981  ? -10.836 61.269  80.750  1.00 18.52 ? 979  ASP   A CA    1 
ATOM   6968  C  C     . ASP   A  1 981  ? -9.542  62.059  80.648  1.00 16.45 ? 979  ASP   A C     1 
ATOM   6969  O  O     . ASP   A  1 981  ? -8.966  62.445  81.674  1.00 20.11 ? 979  ASP   A O     1 
ATOM   6970  C  CB    . ASP   A  1 981  ? -10.509 59.782  80.818  1.00 21.60 ? 979  ASP   A CB    1 
ATOM   6971  C  CG    . ASP   A  1 981  ? -11.664 58.957  81.297  1.00 21.86 ? 979  ASP   A CG    1 
ATOM   6972  O  OD1   . ASP   A  1 981  ? -12.596 59.539  81.881  1.00 24.05 ? 979  ASP   A OD1   1 
ATOM   6973  O  OD2   . ASP   A  1 981  ? -11.639 57.725  81.081  1.00 26.34 ? 979  ASP   A OD2   1 
ATOM   6974  N  N     . GLU   A  1 982  ? -9.038  62.272  79.424  1.00 17.65 ? 980  GLU   A N     1 
ATOM   6975  C  CA    . GLU   A  1 982  ? -7.801  63.031  79.278  1.00 19.82 ? 980  GLU   A CA    1 
ATOM   6976  C  C     . GLU   A  1 982  ? -7.980  64.455  79.787  1.00 20.41 ? 980  GLU   A C     1 
ATOM   6977  O  O     . GLU   A  1 982  ? -7.073  65.024  80.407  1.00 19.53 ? 980  GLU   A O     1 
ATOM   6978  C  CB    . GLU   A  1 982  ? -7.339  63.058  77.820  1.00 21.74 ? 980  GLU   A CB    1 
ATOM   6979  C  CG    . GLU   A  1 982  ? -6.059  63.890  77.628  1.00 24.69 ? 980  GLU   A CG    1 
ATOM   6980  C  CD    . GLU   A  1 982  ? -5.779  64.278  76.179  1.00 29.35 ? 980  GLU   A CD    1 
ATOM   6981  O  OE1   . GLU   A  1 982  ? -6.714  64.731  75.481  1.00 35.34 ? 980  GLU   A OE1   1 
ATOM   6982  O  OE2   . GLU   A  1 982  ? -4.614  64.139  75.743  1.00 23.21 ? 980  GLU   A OE2   1 
ATOM   6983  N  N     . THR   A  1 983  ? -9.143  65.046  79.530  1.00 19.20 ? 981  THR   A N     1 
ATOM   6984  C  CA    . THR   A  1 983  ? -9.396  66.395  80.027  1.00 20.16 ? 981  THR   A CA    1 
ATOM   6985  C  C     . THR   A  1 983  ? -9.583  66.397  81.542  1.00 16.48 ? 981  THR   A C     1 
ATOM   6986  O  O     . THR   A  1 983  ? -9.078  67.289  82.235  1.00 18.66 ? 981  THR   A O     1 
ATOM   6987  C  CB    . THR   A  1 983  ? -10.616 66.980  79.310  1.00 22.39 ? 981  THR   A CB    1 
ATOM   6988  O  OG1   . THR   A  1 983  ? -10.331 67.059  77.907  1.00 20.64 ? 981  THR   A OG1   1 
ATOM   6989  C  CG2   . THR   A  1 983  ? -10.947 68.368  79.863  1.00 20.98 ? 981  THR   A CG2   1 
ATOM   6990  N  N     . ILE   A  1 984  ? -10.288 65.395  82.075  1.00 16.38 ? 982  ILE   A N     1 
ATOM   6991  C  CA    . ILE   A  1 984  ? -10.419 65.270  83.527  1.00 19.72 ? 982  ILE   A CA    1 
ATOM   6992  C  C     . ILE   A  1 984  ? -9.050  65.169  84.183  1.00 18.54 ? 982  ILE   A C     1 
ATOM   6993  O  O     . ILE   A  1 984  ? -8.752  65.879  85.150  1.00 17.16 ? 982  ILE   A O     1 
ATOM   6994  C  CB    . ILE   A  1 984  ? -11.291 64.060  83.891  1.00 18.11 ? 982  ILE   A CB    1 
ATOM   6995  C  CG1   . ILE   A  1 984  ? -12.713 64.290  83.381  1.00 17.57 ? 982  ILE   A CG1   1 
ATOM   6996  C  CG2   . ILE   A  1 984  ? -11.283 63.852  85.397  1.00 17.87 ? 982  ILE   A CG2   1 
ATOM   6997  C  CD1   . ILE   A  1 984  ? -13.648 63.116  83.592  1.00 21.50 ? 982  ILE   A CD1   1 
ATOM   6998  N  N     . ALA   A  1 985  ? -8.210  64.258  83.685  1.00 17.32 ? 983  ALA   A N     1 
ATOM   6999  C  CA    . ALA   A  1 985  ? -6.894  64.067  84.279  1.00 19.91 ? 983  ALA   A CA    1 
ATOM   7000  C  C     . ALA   A  1 985  ? -6.075  65.348  84.189  1.00 21.17 ? 983  ALA   A C     1 
ATOM   7001  O  O     . ALA   A  1 985  ? -5.471  65.787  85.174  1.00 20.48 ? 983  ALA   A O     1 
ATOM   7002  C  CB    . ALA   A  1 985  ? -6.180  62.908  83.588  1.00 19.32 ? 983  ALA   A CB    1 
ATOM   7003  N  N     . HIS   A  1 986  ? -6.080  65.977  83.015  1.00 19.93 ? 984  HIS   A N     1 
ATOM   7004  C  CA    . HIS   A  1 986  ? -5.332  67.210  82.806  1.00 21.77 ? 984  HIS   A CA    1 
ATOM   7005  C  C     . HIS   A  1 986  ? -5.800  68.296  83.759  1.00 21.93 ? 984  HIS   A C     1 
ATOM   7006  O  O     . HIS   A  1 986  ? -5.007  68.860  84.522  1.00 23.37 ? 984  HIS   A O     1 
ATOM   7007  C  CB    . HIS   A  1 986  ? -5.495  67.661  81.351  1.00 23.57 ? 984  HIS   A CB    1 
ATOM   7008  C  CG    . HIS   A  1 986  ? -4.933  69.020  81.064  1.00 23.49 ? 984  HIS   A CG    1 
ATOM   7009  N  ND1   . HIS   A  1 986  ? -5.246  69.718  79.918  1.00 28.54 ? 984  HIS   A ND1   1 
ATOM   7010  C  CD2   . HIS   A  1 986  ? -4.069  69.800  81.757  1.00 23.64 ? 984  HIS   A CD2   1 
ATOM   7011  C  CE1   . HIS   A  1 986  ? -4.601  70.873  79.919  1.00 30.72 ? 984  HIS   A CE1   1 
ATOM   7012  N  NE2   . HIS   A  1 986  ? -3.884  70.950  81.026  1.00 28.12 ? 984  HIS   A NE2   1 
ATOM   7013  N  N     . VAL   A  1 987  ? -7.096  68.601  83.724  1.00 18.75 ? 985  VAL   A N     1 
ATOM   7014  C  CA    . VAL   A  1 987  ? -7.607  69.745  84.470  1.00 20.03 ? 985  VAL   A CA    1 
ATOM   7015  C  C     . VAL   A  1 987  ? -7.478  69.510  85.968  1.00 20.65 ? 985  VAL   A C     1 
ATOM   7016  O  O     . VAL   A  1 987  ? -6.991  70.378  86.702  1.00 20.80 ? 985  VAL   A O     1 
ATOM   7017  C  CB    . VAL   A  1 987  ? -9.057  70.049  84.059  1.00 18.41 ? 985  VAL   A CB    1 
ATOM   7018  C  CG1   . VAL   A  1 987  ? -9.646  71.121  84.953  1.00 17.51 ? 985  VAL   A CG1   1 
ATOM   7019  C  CG2   . VAL   A  1 987  ? -9.093  70.518  82.609  1.00 19.68 ? 985  VAL   A CG2   1 
ATOM   7020  N  N     . THR   A  1 988  ? -7.891  68.329  86.445  1.00 19.35 ? 986  THR   A N     1 
ATOM   7021  C  CA    . THR   A  1 988  ? -7.842  68.084  87.883  1.00 21.08 ? 986  THR   A CA    1 
ATOM   7022  C  C     . THR   A  1 988  ? -6.416  67.959  88.401  1.00 26.86 ? 986  THR   A C     1 
ATOM   7023  O  O     . THR   A  1 988  ? -6.188  68.163  89.598  1.00 27.69 ? 986  THR   A O     1 
ATOM   7024  C  CB    . THR   A  1 988  ? -8.634  66.832  88.273  1.00 23.82 ? 986  THR   A CB    1 
ATOM   7025  O  OG1   . THR   A  1 988  ? -8.073  65.687  87.630  1.00 22.73 ? 986  THR   A OG1   1 
ATOM   7026  C  CG2   . THR   A  1 988  ? -10.098 66.971  87.887  1.00 23.33 ? 986  THR   A CG2   1 
ATOM   7027  N  N     . SER   A  1 989  ? -5.445  67.653  87.542  1.00 22.57 ? 987  SER   A N     1 
ATOM   7028  C  CA    . SER   A  1 989  ? -4.080  67.616  88.038  1.00 25.74 ? 987  SER   A CA    1 
ATOM   7029  C  C     . SER   A  1 989  ? -3.458  69.006  88.118  1.00 28.01 ? 987  SER   A C     1 
ATOM   7030  O  O     . SER   A  1 989  ? -2.479  69.189  88.845  1.00 32.20 ? 987  SER   A O     1 
ATOM   7031  C  CB    . SER   A  1 989  ? -3.213  66.687  87.177  1.00 25.10 ? 987  SER   A CB    1 
ATOM   7032  O  OG    . SER   A  1 989  ? -3.050  67.196  85.869  1.00 33.55 ? 987  SER   A OG    1 
ATOM   7033  N  N     . ARG   A  1 990  ? -4.014  69.992  87.419  1.00 24.47 ? 988  ARG   A N     1 
ATOM   7034  C  CA    . ARG   A  1 990  ? -3.441  71.331  87.377  1.00 26.12 ? 988  ARG   A CA    1 
ATOM   7035  C  C     . ARG   A  1 990  ? -4.197  72.348  88.216  1.00 24.74 ? 988  ARG   A C     1 
ATOM   7036  O  O     . ARG   A  1 990  ? -3.581  73.282  88.735  1.00 24.65 ? 988  ARG   A O     1 
ATOM   7037  C  CB    . ARG   A  1 990  ? -3.389  71.835  85.935  1.00 23.62 ? 988  ARG   A CB    1 
ATOM   7038  C  CG    . ARG   A  1 990  ? -2.654  70.904  84.999  1.00 29.82 ? 988  ARG   A CG    1 
ATOM   7039  C  CD    . ARG   A  1 990  ? -1.161  71.091  85.120  1.00 35.28 ? 988  ARG   A CD    1 
ATOM   7040  N  NE    . ARG   A  1 990  ? -0.661  71.947  84.053  1.00 33.51 ? 988  ARG   A NE    1 
ATOM   7041  C  CZ    . ARG   A  1 990  ? 0.589   72.374  83.966  1.00 30.69 ? 988  ARG   A CZ    1 
ATOM   7042  N  NH1   . ARG   A  1 990  ? 1.474   72.116  84.917  1.00 32.11 ? 988  ARG   A NH1   1 
ATOM   7043  N  NH2   . ARG   A  1 990  ? 0.960   73.077  82.900  1.00 26.18 ? 988  ARG   A NH2   1 
ATOM   7044  N  N     . ILE   A  1 991  ? -5.514  72.190  88.355  1.00 22.56 ? 989  ILE   A N     1 
ATOM   7045  C  CA    . ILE   A  1 991  ? -6.305  73.128  89.140  1.00 19.69 ? 989  ILE   A CA    1 
ATOM   7046  C  C     . ILE   A  1 991  ? -5.892  73.054  90.607  1.00 21.41 ? 989  ILE   A C     1 
ATOM   7047  O  O     . ILE   A  1 991  ? -5.574  71.982  91.132  1.00 24.55 ? 989  ILE   A O     1 
ATOM   7048  C  CB    . ILE   A  1 991  ? -7.805  72.828  88.953  1.00 22.39 ? 989  ILE   A CB    1 
ATOM   7049  C  CG1   . ILE   A  1 991  ? -8.647  74.016  89.422  1.00 21.43 ? 989  ILE   A CG1   1 
ATOM   7050  C  CG2   . ILE   A  1 991  ? -8.194  71.529  89.673  1.00 22.27 ? 989  ILE   A CG2   1 
ATOM   7051  C  CD1   . ILE   A  1 991  ? -8.386  75.274  88.607  1.00 23.89 ? 989  ILE   A CD1   1 
ATOM   7052  N  N     . LYS   A  1 992  ? -5.864  74.199  91.276  1.00 19.06 ? 990  LYS   A N     1 
ATOM   7053  C  CA    . LYS   A  1 992  ? -5.511  74.251  92.695  1.00 21.24 ? 990  LYS   A CA    1 
ATOM   7054  C  C     . LYS   A  1 992  ? -6.751  74.717  93.457  1.00 23.44 ? 990  LYS   A C     1 
ATOM   7055  O  O     . LYS   A  1 992  ? -6.928  75.910  93.719  1.00 27.74 ? 990  LYS   A O     1 
ATOM   7056  C  CB    . LYS   A  1 992  ? -4.326  75.171  92.942  1.00 23.53 ? 990  LYS   A CB    1 
ATOM   7057  N  N     . ALA   A  1 993  ? -7.610  73.766  93.808  1.00 21.59 ? 991  ALA   A N     1 
ATOM   7058  C  CA    . ALA   A  1 993  ? -8.823  74.074  94.549  1.00 19.87 ? 991  ALA   A CA    1 
ATOM   7059  C  C     . ALA   A  1 993  ? -9.090  72.953  95.535  1.00 19.46 ? 991  ALA   A C     1 
ATOM   7060  O  O     . ALA   A  1 993  ? -8.694  71.805  95.308  1.00 21.06 ? 991  ALA   A O     1 
ATOM   7061  C  CB    . ALA   A  1 993  ? -10.035 74.256  93.629  1.00 20.32 ? 991  ALA   A CB    1 
ATOM   7062  N  N     . GLY   A  1 994  ? -9.772  73.306  96.629  1.00 16.86 ? 992  GLY   A N     1 
ATOM   7063  C  CA    . GLY   A  1 994  ? -10.026 72.346  97.686  1.00 17.09 ? 992  GLY   A CA    1 
ATOM   7064  C  C     . GLY   A  1 994  ? -11.158 71.393  97.388  1.00 17.74 ? 992  GLY   A C     1 
ATOM   7065  O  O     . GLY   A  1 994  ? -11.173 70.271  97.896  1.00 16.62 ? 992  GLY   A O     1 
ATOM   7066  N  N     . ASN   A  1 995  ? -12.114 71.813  96.570  1.00 15.36 ? 993  ASN   A N     1 
ATOM   7067  C  CA    . ASN   A  1 995  ? -13.325 71.035  96.331  1.00 16.87 ? 993  ASN   A CA    1 
ATOM   7068  C  C     . ASN   A  1 995  ? -13.551 70.993  94.829  1.00 15.96 ? 993  ASN   A C     1 
ATOM   7069  O  O     . ASN   A  1 995  ? -13.851 72.018  94.213  1.00 18.79 ? 993  ASN   A O     1 
ATOM   7070  C  CB    . ASN   A  1 995  ? -14.526 71.637  97.067  1.00 15.10 ? 993  ASN   A CB    1 
ATOM   7071  C  CG    . ASN   A  1 995  ? -14.582 71.196  98.522  1.00 17.81 ? 993  ASN   A CG    1 
ATOM   7072  O  OD1   . ASN   A  1 995  ? -13.931 71.779  99.381  1.00 18.60 ? 993  ASN   A OD1   1 
ATOM   7073  N  ND2   . ASN   A  1 995  ? -15.332 70.129  98.793  1.00 17.01 ? 993  ASN   A ND2   1 
ATOM   7074  N  N     . LEU   A  1 996  ? -13.365 69.818  94.238  1.00 15.17 ? 994  LEU   A N     1 
ATOM   7075  C  CA    . LEU   A  1 996  ? -13.549 69.629  92.811  1.00 16.01 ? 994  LEU   A CA    1 
ATOM   7076  C  C     . LEU   A  1 996  ? -14.854 68.906  92.566  1.00 14.88 ? 994  LEU   A C     1 
ATOM   7077  O  O     . LEU   A  1 996  ? -15.237 68.026  93.333  1.00 14.97 ? 994  LEU   A O     1 
ATOM   7078  C  CB    . LEU   A  1 996  ? -12.417 68.802  92.219  1.00 15.09 ? 994  LEU   A CB    1 
ATOM   7079  C  CG    . LEU   A  1 996  ? -11.030 69.281  92.634  1.00 20.77 ? 994  LEU   A CG    1 
ATOM   7080  C  CD1   . LEU   A  1 996  ? -9.976  68.449  91.912  1.00 20.46 ? 994  LEU   A CD1   1 
ATOM   7081  C  CD2   . LEU   A  1 996  ? -10.862 70.765  92.343  1.00 21.66 ? 994  LEU   A CD2   1 
ATOM   7082  N  N     . TYR   A  1 997  ? -15.511 69.252  91.462  1.00 15.50 ? 995  TYR   A N     1 
ATOM   7083  C  CA    . TYR   A  1 997  ? -16.786 68.643  91.113  1.00 15.44 ? 995  TYR   A CA    1 
ATOM   7084  C  C     . TYR   A  1 997  ? -16.761 68.327  89.629  1.00 16.05 ? 995  TYR   A C     1 
ATOM   7085  O  O     . TYR   A  1 997  ? -16.496 69.217  88.821  1.00 15.26 ? 995  TYR   A O     1 
ATOM   7086  C  CB    . TYR   A  1 997  ? -17.952 69.584  91.433  1.00 14.68 ? 995  TYR   A CB    1 
ATOM   7087  C  CG    . TYR   A  1 997  ? -18.049 69.916  92.906  1.00 15.79 ? 995  TYR   A CG    1 
ATOM   7088  C  CD1   . TYR   A  1 997  ? -18.732 69.079  93.773  1.00 17.78 ? 995  TYR   A CD1   1 
ATOM   7089  C  CD2   . TYR   A  1 997  ? -17.440 71.045  93.426  1.00 14.79 ? 995  TYR   A CD2   1 
ATOM   7090  C  CE1   . TYR   A  1 997  ? -18.818 69.367  95.119  1.00 18.42 ? 995  TYR   A CE1   1 
ATOM   7091  C  CE2   . TYR   A  1 997  ? -17.524 71.345  94.776  1.00 17.36 ? 995  TYR   A CE2   1 
ATOM   7092  C  CZ    . TYR   A  1 997  ? -18.217 70.504  95.612  1.00 19.45 ? 995  TYR   A CZ    1 
ATOM   7093  O  OH    . TYR   A  1 997  ? -18.312 70.787  96.965  1.00 23.46 ? 995  TYR   A OH    1 
ATOM   7094  N  N     . ILE   A  1 998  ? -17.033 67.076  89.272  1.00 14.72 ? 996  ILE   A N     1 
ATOM   7095  C  CA    . ILE   A  1 998  ? -16.965 66.640  87.882  1.00 15.04 ? 996  ILE   A CA    1 
ATOM   7096  C  C     . ILE   A  1 998  ? -18.373 66.281  87.430  1.00 14.68 ? 996  ILE   A C     1 
ATOM   7097  O  O     . ILE   A  1 998  ? -19.003 65.389  88.004  1.00 15.11 ? 996  ILE   A O     1 
ATOM   7098  C  CB    . ILE   A  1 998  ? -16.010 65.449  87.702  1.00 17.03 ? 996  ILE   A CB    1 
ATOM   7099  C  CG1   . ILE   A  1 998  ? -14.614 65.781  88.256  1.00 18.65 ? 996  ILE   A CG1   1 
ATOM   7100  C  CG2   . ILE   A  1 998  ? -15.951 65.041  86.201  1.00 15.31 ? 996  ILE   A CG2   1 
ATOM   7101  C  CD1   . ILE   A  1 998  ? -13.932 66.917  87.562  1.00 24.06 ? 996  ILE   A CD1   1 
ATOM   7102  N  N     . ASN   A  1 999  ? -18.859 66.984  86.402  1.00 14.68 ? 997  ASN   A N     1 
ATOM   7103  C  CA    . ASN   A  1 999  ? -20.139 66.685  85.755  1.00 17.75 ? 997  ASN   A CA    1 
ATOM   7104  C  C     . ASN   A  1 999  ? -21.325 66.824  86.708  1.00 16.46 ? 997  ASN   A C     1 
ATOM   7105  O  O     . ASN   A  1 999  ? -22.313 66.094  86.615  1.00 14.85 ? 997  ASN   A O     1 
ATOM   7106  C  CB    . ASN   A  1 999  ? -20.108 65.306  85.104  1.00 17.34 ? 997  ASN   A CB    1 
ATOM   7107  C  CG    . ASN   A  1 999  ? -19.178 65.277  83.917  1.00 17.76 ? 997  ASN   A CG    1 
ATOM   7108  O  OD1   . ASN   A  1 999  ? -18.995 66.300  83.256  1.00 18.36 ? 997  ASN   A OD1   1 
ATOM   7109  N  ND2   . ASN   A  1 999  ? -18.588 64.124  83.635  1.00 18.12 ? 997  ASN   A ND2   1 
ATOM   7110  N  N     . ARG   A  1 1000 ? -21.250 67.815  87.589  1.00 17.40 ? 998  ARG   A N     1 
ATOM   7111  C  CA    . ARG   A  1 1000 ? -22.334 68.120  88.513  1.00 15.95 ? 998  ARG   A CA    1 
ATOM   7112  C  C     . ARG   A  1 1000 ? -22.184 69.574  88.934  1.00 15.88 ? 998  ARG   A C     1 
ATOM   7113  O  O     . ARG   A  1 1000 ? -21.260 70.266  88.512  1.00 15.99 ? 998  ARG   A O     1 
ATOM   7114  C  CB    . ARG   A  1 1000 ? -22.316 67.193  89.727  1.00 14.58 ? 998  ARG   A CB    1 
ATOM   7115  C  CG    . ARG   A  1 1000 ? -20.910 67.069  90.379  1.00 15.49 ? 998  ARG   A CG    1 
ATOM   7116  C  CD    . ARG   A  1 1000 ? -21.019 66.764  91.860  1.00 16.16 ? 998  ARG   A CD    1 
ATOM   7117  N  NE    . ARG   A  1 1000 ? -21.625 67.860  92.613  1.00 16.97 ? 998  ARG   A NE    1 
ATOM   7118  C  CZ    . ARG   A  1 1000 ? -21.871 67.806  93.914  1.00 16.73 ? 998  ARG   A CZ    1 
ATOM   7119  N  NH1   . ARG   A  1 1000 ? -21.586 66.725  94.622  1.00 16.99 ? 998  ARG   A NH1   1 
ATOM   7120  N  NH2   . ARG   A  1 1000 ? -22.410 68.863  94.522  1.00 16.68 ? 998  ARG   A NH2   1 
ATOM   7121  N  N     . ASN   A  1 1001 ? -23.097 70.033  89.781  1.00 16.53 ? 999  ASN   A N     1 
ATOM   7122  C  CA    . ASN   A  1 1001 ? -22.949 71.383  90.302  1.00 16.61 ? 999  ASN   A CA    1 
ATOM   7123  C  C     . ASN   A  1 1001 ? -21.790 71.419  91.308  1.00 16.98 ? 999  ASN   A C     1 
ATOM   7124  O  O     . ASN   A  1 1001 ? -21.218 70.386  91.672  1.00 16.03 ? 999  ASN   A O     1 
ATOM   7125  C  CB    . ASN   A  1 1001 ? -24.278 71.874  90.910  1.00 16.45 ? 999  ASN   A CB    1 
ATOM   7126  C  CG    . ASN   A  1 1001 ? -24.643 71.185  92.229  1.00 18.58 ? 999  ASN   A CG    1 
ATOM   7127  O  OD1   . ASN   A  1 1001 ? -23.815 71.009  93.115  1.00 19.99 ? 999  ASN   A OD1   1 
ATOM   7128  N  ND2   . ASN   A  1 1001 ? -25.911 70.817  92.363  1.00 23.46 ? 999  ASN   A ND2   1 
ATOM   7129  N  N     . ILE   A  1 1002 ? -21.429 72.624  91.741  1.00 16.43 ? 1000 ILE   A N     1 
ATOM   7130  C  CA    . ILE   A  1 1002 ? -20.262 72.816  92.596  1.00 14.80 ? 1000 ILE   A CA    1 
ATOM   7131  C  C     . ILE   A  1 1002 ? -20.654 73.288  93.994  1.00 18.85 ? 1000 ILE   A C     1 
ATOM   7132  O  O     . ILE   A  1 1002 ? -19.814 73.800  94.737  1.00 16.09 ? 1000 ILE   A O     1 
ATOM   7133  C  CB    . ILE   A  1 1002 ? -19.245 73.772  91.949  1.00 16.55 ? 1000 ILE   A CB    1 
ATOM   7134  C  CG1   . ILE   A  1 1002 ? -19.780 75.218  91.875  1.00 14.93 ? 1000 ILE   A CG1   1 
ATOM   7135  C  CG2   . ILE   A  1 1002 ? -18.877 73.259  90.567  1.00 17.04 ? 1000 ILE   A CG2   1 
ATOM   7136  C  CD1   . ILE   A  1 1002 ? -18.692 76.226  91.416  1.00 15.09 ? 1000 ILE   A CD1   1 
ATOM   7137  N  N     . ILE   A  1 1003 ? -21.909 73.102  94.379  1.00 17.21 ? 1001 ILE   A N     1 
ATOM   7138  C  CA    . ILE   A  1 1003 ? -22.410 73.633  95.637  1.00 18.44 ? 1001 ILE   A CA    1 
ATOM   7139  C  C     . ILE   A  1 1003 ? -22.954 72.498  96.501  1.00 21.33 ? 1001 ILE   A C     1 
ATOM   7140  O  O     . ILE   A  1 1003 ? -23.173 71.374  96.042  1.00 22.47 ? 1001 ILE   A O     1 
ATOM   7141  C  CB    . ILE   A  1 1003 ? -23.505 74.696  95.426  1.00 16.79 ? 1001 ILE   A CB    1 
ATOM   7142  C  CG1   . ILE   A  1 1003 ? -24.716 74.058  94.747  1.00 21.25 ? 1001 ILE   A CG1   1 
ATOM   7143  C  CG2   . ILE   A  1 1003 ? -22.965 75.899  94.632  1.00 15.41 ? 1001 ILE   A CG2   1 
ATOM   7144  C  CD1   . ILE   A  1 1003 ? -26.004 74.919  94.852  1.00 22.31 ? 1001 ILE   A CD1   1 
ATOM   7145  N  N     . GLY   A  1 1004 ? -23.232 72.835  97.755  1.00 20.57 ? 1002 GLY   A N     1 
ATOM   7146  C  CA    . GLY   A  1 1004 ? -23.876 71.894  98.652  1.00 21.94 ? 1002 GLY   A CA    1 
ATOM   7147  C  C     . GLY   A  1 1004 ? -22.981 70.756  99.087  1.00 24.33 ? 1002 GLY   A C     1 
ATOM   7148  O  O     . GLY   A  1 1004 ? -23.436 69.608  99.144  1.00 23.36 ? 1002 GLY   A O     1 
ATOM   7149  N  N     . ALA   A  1 1005 ? -21.713 71.044  99.374  1.00 21.15 ? 1003 ALA   A N     1 
ATOM   7150  C  CA    . ALA   A  1 1005 ? -20.799 70.018  99.850  1.00 20.29 ? 1003 ALA   A CA    1 
ATOM   7151  C  C     . ALA   A  1 1005 ? -21.359 69.348  101.096 1.00 23.19 ? 1003 ALA   A C     1 
ATOM   7152  O  O     . ALA   A  1 1005 ? -21.894 70.010  101.991 1.00 24.39 ? 1003 ALA   A O     1 
ATOM   7153  C  CB    . ALA   A  1 1005 ? -19.434 70.626  100.159 1.00 24.25 ? 1003 ALA   A CB    1 
ATOM   7154  N  N     . VAL   A  1 1006 ? -21.249 68.027  101.143 1.00 17.86 ? 1004 VAL   A N     1 
ATOM   7155  C  CA    . VAL   A  1 1006 ? -21.899 67.214  102.160 1.00 18.82 ? 1004 VAL   A CA    1 
ATOM   7156  C  C     . VAL   A  1 1006 ? -20.877 66.824  103.212 1.00 16.83 ? 1004 VAL   A C     1 
ATOM   7157  O  O     . VAL   A  1 1006 ? -19.780 66.362  102.885 1.00 16.48 ? 1004 VAL   A O     1 
ATOM   7158  C  CB    . VAL   A  1 1006 ? -22.547 65.966  101.546 1.00 16.90 ? 1004 VAL   A CB    1 
ATOM   7159  C  CG1   . VAL   A  1 1006 ? -23.062 65.056  102.637 1.00 19.52 ? 1004 VAL   A CG1   1 
ATOM   7160  C  CG2   . VAL   A  1 1006 ? -23.687 66.379  100.624 1.00 17.14 ? 1004 VAL   A CG2   1 
ATOM   7161  N  N     . VAL   A  1 1007 ? -21.254 66.995  104.477 1.00 17.92 ? 1005 VAL   A N     1 
ATOM   7162  C  CA    . VAL   A  1 1007 ? -20.372 66.674  105.590 1.00 15.55 ? 1005 VAL   A CA    1 
ATOM   7163  C  C     . VAL   A  1 1007 ? -19.901 65.230  105.493 1.00 15.52 ? 1005 VAL   A C     1 
ATOM   7164  O  O     . VAL   A  1 1007 ? -20.702 64.308  105.306 1.00 18.89 ? 1005 VAL   A O     1 
ATOM   7165  C  CB    . VAL   A  1 1007 ? -21.106 66.945  106.910 1.00 17.11 ? 1005 VAL   A CB    1 
ATOM   7166  C  CG1   . VAL   A  1 1007 ? -20.265 66.486  108.091 1.00 16.30 ? 1005 VAL   A CG1   1 
ATOM   7167  C  CG2   . VAL   A  1 1007 ? -21.426 68.437  107.044 1.00 16.18 ? 1005 VAL   A CG2   1 
ATOM   7168  N  N     . GLY   A  1 1008 ? -18.583 65.025  105.622 1.00 17.65 ? 1006 GLY   A N     1 
ATOM   7169  C  CA    . GLY   A  1 1008 ? -18.008 63.696  105.604 1.00 15.91 ? 1006 GLY   A CA    1 
ATOM   7170  C  C     . GLY   A  1 1008 ? -18.050 63.017  104.257 1.00 18.20 ? 1006 GLY   A C     1 
ATOM   7171  O  O     . GLY   A  1 1008 ? -17.670 61.847  104.154 1.00 18.86 ? 1006 GLY   A O     1 
ATOM   7172  N  N     . VAL   A  1 1009 ? -18.517 63.716  103.225 1.00 16.55 ? 1007 VAL   A N     1 
ATOM   7173  C  CA    . VAL   A  1 1009 ? -18.620 63.183  101.874 1.00 15.22 ? 1007 VAL   A CA    1 
ATOM   7174  C  C     . VAL   A  1 1009 ? -17.827 64.037  100.906 1.00 16.30 ? 1007 VAL   A C     1 
ATOM   7175  O  O     . VAL   A  1 1009 ? -16.954 63.539  100.189 1.00 17.81 ? 1007 VAL   A O     1 
ATOM   7176  C  CB    . VAL   A  1 1009 ? -20.095 63.078  101.418 1.00 19.57 ? 1007 VAL   A CB    1 
ATOM   7177  C  CG1   . VAL   A  1 1009 ? -20.155 62.537  99.977  1.00 19.42 ? 1007 VAL   A CG1   1 
ATOM   7178  C  CG2   . VAL   A  1 1009 ? -20.907 62.195  102.377 1.00 17.87 ? 1007 VAL   A CG2   1 
ATOM   7179  N  N     . GLN   A  1 1010 ? -18.104 65.345  100.889 1.00 15.06 ? 1008 GLN   A N     1 
ATOM   7180  C  CA    . GLN   A  1 1010 ? -17.203 66.344  100.324 1.00 15.69 ? 1008 GLN   A CA    1 
ATOM   7181  C  C     . GLN   A  1 1010 ? -16.770 67.263  101.461 1.00 15.46 ? 1008 GLN   A C     1 
ATOM   7182  O  O     . GLN   A  1 1010 ? -17.299 68.377  101.592 1.00 19.40 ? 1008 GLN   A O     1 
ATOM   7183  C  CB    . GLN   A  1 1010 ? -17.850 67.150  99.201  1.00 18.13 ? 1008 GLN   A CB    1 
ATOM   7184  C  CG    . GLN   A  1 1010 ? -18.406 66.310  98.061  1.00 17.67 ? 1008 GLN   A CG    1 
ATOM   7185  C  CD    . GLN   A  1 1010 ? -19.904 66.063  98.209  1.00 20.14 ? 1008 GLN   A CD    1 
ATOM   7186  O  OE1   . GLN   A  1 1010 ? -20.630 66.878  98.799  1.00 19.23 ? 1008 GLN   A OE1   1 
ATOM   7187  N  NE2   . GLN   A  1 1010 ? -20.374 64.956  97.647  1.00 18.06 ? 1008 GLN   A NE2   1 
ATOM   7188  N  N     . PRO   A  1 1011 ? -15.835 66.822  102.309 1.00 18.73 ? 1009 PRO   A N     1 
ATOM   7189  C  CA    . PRO   A  1 1011 ? -15.246 67.731  103.304 1.00 15.42 ? 1009 PRO   A CA    1 
ATOM   7190  C  C     . PRO   A  1 1011 ? -14.868 69.030  102.618 1.00 20.01 ? 1009 PRO   A C     1 
ATOM   7191  O  O     . PRO   A  1 1011 ? -14.327 69.027  101.510 1.00 17.03 ? 1009 PRO   A O     1 
ATOM   7192  C  CB    . PRO   A  1 1011 ? -14.015 66.964  103.801 1.00 15.84 ? 1009 PRO   A CB    1 
ATOM   7193  C  CG    . PRO   A  1 1011 ? -14.392 65.516  103.616 1.00 18.49 ? 1009 PRO   A CG    1 
ATOM   7194  C  CD    . PRO   A  1 1011 ? -15.176 65.502  102.316 1.00 16.23 ? 1009 PRO   A CD    1 
ATOM   7195  N  N     . PHE   A  1 1012 ? -15.201 70.141  103.259 1.00 19.32 ? 1010 PHE   A N     1 
ATOM   7196  C  CA    . PHE   A  1 1012 ? -15.303 71.414  102.576 1.00 17.86 ? 1010 PHE   A CA    1 
ATOM   7197  C  C     . PHE   A  1 1012 ? -14.268 72.406  103.079 1.00 19.05 ? 1010 PHE   A C     1 
ATOM   7198  O  O     . PHE   A  1 1012 ? -14.099 72.592  104.292 1.00 19.67 ? 1010 PHE   A O     1 
ATOM   7199  C  CB    . PHE   A  1 1012 ? -16.697 72.018  102.736 1.00 19.76 ? 1010 PHE   A CB    1 
ATOM   7200  C  CG    . PHE   A  1 1012 ? -16.875 73.238  101.914 1.00 21.21 ? 1010 PHE   A CG    1 
ATOM   7201  C  CD1   . PHE   A  1 1012 ? -17.086 73.131  100.551 1.00 22.57 ? 1010 PHE   A CD1   1 
ATOM   7202  C  CD2   . PHE   A  1 1012 ? -16.765 74.499  102.482 1.00 22.84 ? 1010 PHE   A CD2   1 
ATOM   7203  C  CE1   . PHE   A  1 1012 ? -17.227 74.252  99.779  1.00 21.91 ? 1010 PHE   A CE1   1 
ATOM   7204  C  CE2   . PHE   A  1 1012 ? -16.900 75.621  101.704 1.00 24.47 ? 1010 PHE   A CE2   1 
ATOM   7205  C  CZ    . PHE   A  1 1012 ? -17.141 75.496  100.354 1.00 19.27 ? 1010 PHE   A CZ    1 
ATOM   7206  N  N     . GLY   A  1 1013 ? -13.617 73.071  102.140 1.00 20.51 ? 1011 GLY   A N     1 
ATOM   7207  C  CA    . GLY   A  1 1013 ? -12.585 74.018  102.491 1.00 23.60 ? 1011 GLY   A CA    1 
ATOM   7208  C  C     . GLY   A  1 1013 ? -11.525 74.064  101.421 1.00 22.84 ? 1011 GLY   A C     1 
ATOM   7209  O  O     . GLY   A  1 1013 ? -11.195 73.051  100.787 1.00 21.14 ? 1011 GLY   A O     1 
ATOM   7210  N  N     . GLY   A  1 1014 ? -10.979 75.249  101.214 1.00 21.33 ? 1012 GLY   A N     1 
ATOM   7211  C  CA    . GLY   A  1 1014 ? -10.053 75.441  100.126 1.00 25.78 ? 1012 GLY   A CA    1 
ATOM   7212  C  C     . GLY   A  1 1014 ? -8.710  75.934  100.606 1.00 26.28 ? 1012 GLY   A C     1 
ATOM   7213  O  O     . GLY   A  1 1014 ? -8.357  75.815  101.789 1.00 27.05 ? 1012 GLY   A O     1 
ATOM   7214  N  N     . ARG   A  1 1015 ? -7.969  76.519  99.679  1.00 22.19 ? 1013 ARG   A N     1 
ATOM   7215  C  CA    . ARG   A  1 1015 ? -6.584  76.885  99.879  1.00 24.62 ? 1013 ARG   A CA    1 
ATOM   7216  C  C     . ARG   A  1 1015 ? -6.394  78.311  99.397  1.00 24.83 ? 1013 ARG   A C     1 
ATOM   7217  O  O     . ARG   A  1 1015 ? -7.310  78.931  98.849  1.00 23.76 ? 1013 ARG   A O     1 
ATOM   7218  C  CB    . ARG   A  1 1015 ? -5.669  75.927  99.110  1.00 23.51 ? 1013 ARG   A CB    1 
ATOM   7219  C  CG    . ARG   A  1 1015 ? -6.056  75.876  97.638  1.00 25.64 ? 1013 ARG   A CG    1 
ATOM   7220  C  CD    . ARG   A  1 1015 ? -4.987  75.261  96.754  1.00 35.47 ? 1013 ARG   A CD    1 
ATOM   7221  N  NE    . ARG   A  1 1015 ? -3.657  75.457  97.309  1.00 35.68 ? 1013 ARG   A NE    1 
ATOM   7222  C  CZ    . ARG   A  1 1015 ? -2.946  76.569  97.191  1.00 40.72 ? 1013 ARG   A CZ    1 
ATOM   7223  N  NH1   . ARG   A  1 1015 ? -3.396  77.610  96.502  1.00 39.06 ? 1013 ARG   A NH1   1 
ATOM   7224  N  NH2   . ARG   A  1 1015 ? -1.761  76.644  97.791  1.00 37.33 ? 1013 ARG   A NH2   1 
ATOM   7225  N  N     . GLY   A  1 1016 ? -5.181  78.814  99.565  1.00 26.27 ? 1014 GLY   A N     1 
ATOM   7226  C  CA    . GLY   A  1 1016 ? -4.891  80.155  99.091  1.00 27.09 ? 1014 GLY   A CA    1 
ATOM   7227  C  C     . GLY   A  1 1016 ? -5.767  81.164  99.803  1.00 27.59 ? 1014 GLY   A C     1 
ATOM   7228  O  O     . GLY   A  1 1016 ? -5.956  81.111  101.022 1.00 26.38 ? 1014 GLY   A O     1 
ATOM   7229  N  N     . LEU   A  1 1017 ? -6.335  82.089  99.032  1.00 23.16 ? 1015 LEU   A N     1 
ATOM   7230  C  CA    . LEU   A  1 1017 ? -7.208  83.105  99.607  1.00 23.46 ? 1015 LEU   A CA    1 
ATOM   7231  C  C     . LEU   A  1 1017 ? -8.512  82.533  100.139 1.00 23.73 ? 1015 LEU   A C     1 
ATOM   7232  O  O     . LEU   A  1 1017 ? -9.287  83.275  100.747 1.00 24.28 ? 1015 LEU   A O     1 
ATOM   7233  C  CB    . LEU   A  1 1017 ? -7.525  84.171  98.564  1.00 23.26 ? 1015 LEU   A CB    1 
ATOM   7234  C  CG    . LEU   A  1 1017 ? -6.325  84.917  97.993  1.00 28.52 ? 1015 LEU   A CG    1 
ATOM   7235  C  CD1   . LEU   A  1 1017 ? -6.800  85.860  96.902  1.00 22.94 ? 1015 LEU   A CD1   1 
ATOM   7236  C  CD2   . LEU   A  1 1017 ? -5.585  85.675  99.092  1.00 28.14 ? 1015 LEU   A CD2   1 
ATOM   7237  N  N     . SER   A  1 1018 ? -8.778  81.250  99.919  1.00 20.11 ? 1016 SER   A N     1 
ATOM   7238  C  CA    . SER   A  1 1018 ? -10.054 80.675  100.312 1.00 20.85 ? 1016 SER   A CA    1 
ATOM   7239  C  C     . SER   A  1 1018 ? -10.038 80.073  101.701 1.00 22.54 ? 1016 SER   A C     1 
ATOM   7240  O  O     . SER   A  1 1018 ? -11.105 79.721  102.211 1.00 23.81 ? 1016 SER   A O     1 
ATOM   7241  C  CB    . SER   A  1 1018 ? -10.495 79.602  99.318  1.00 21.73 ? 1016 SER   A CB    1 
ATOM   7242  O  OG    . SER   A  1 1018 ? -10.711 80.174  98.042  1.00 23.47 ? 1016 SER   A OG    1 
ATOM   7243  N  N     . GLY   A  1 1019 ? -8.882  79.940  102.329 1.00 22.47 ? 1017 GLY   A N     1 
ATOM   7244  C  CA    . GLY   A  1 1019 ? -8.924  79.389  103.660 1.00 25.24 ? 1017 GLY   A CA    1 
ATOM   7245  C  C     . GLY   A  1 1019 ? -7.585  78.892  104.129 1.00 24.01 ? 1017 GLY   A C     1 
ATOM   7246  O  O     . GLY   A  1 1019 ? -6.630  78.731  103.366 1.00 23.29 ? 1017 GLY   A O     1 
ATOM   7247  N  N     . THR   A  1 1020 ? -7.526  78.667  105.431 1.00 21.00 ? 1018 THR   A N     1 
ATOM   7248  C  CA    . THR   A  1 1020 ? -6.400  78.029  106.082 1.00 20.03 ? 1018 THR   A CA    1 
ATOM   7249  C  C     . THR   A  1 1020 ? -6.522  76.518  106.097 1.00 21.56 ? 1018 THR   A C     1 
ATOM   7250  O  O     . THR   A  1 1020 ? -5.512  75.820  106.215 1.00 24.18 ? 1018 THR   A O     1 
ATOM   7251  C  CB    . THR   A  1 1020 ? -6.317  78.504  107.531 1.00 20.78 ? 1018 THR   A CB    1 
ATOM   7252  O  OG1   . THR   A  1 1020 ? -7.540  78.135  108.200 1.00 18.82 ? 1018 THR   A OG1   1 
ATOM   7253  C  CG2   . THR   A  1 1020 ? -6.150  80.017  107.590 1.00 23.75 ? 1018 THR   A CG2   1 
ATOM   7254  N  N     . GLY   A  1 1021 ? -7.744  76.003  106.047 1.00 23.75 ? 1019 GLY   A N     1 
ATOM   7255  C  CA    . GLY   A  1 1021 ? -7.994  74.647  106.461 1.00 20.49 ? 1019 GLY   A CA    1 
ATOM   7256  C  C     . GLY   A  1 1021 ? -7.776  74.519  107.961 1.00 22.27 ? 1019 GLY   A C     1 
ATOM   7257  O  O     . GLY   A  1 1021 ? -7.442  75.493  108.648 1.00 20.62 ? 1019 GLY   A O     1 
ATOM   7258  N  N     . PRO   A  1 1022 ? -7.970  73.311  108.507 1.00 18.57 ? 1020 PRO   A N     1 
ATOM   7259  C  CA    . PRO   A  1 1022 ? -8.415  72.090  107.827 1.00 21.42 ? 1020 PRO   A CA    1 
ATOM   7260  C  C     . PRO   A  1 1022 ? -9.868  72.183  107.376 1.00 23.16 ? 1020 PRO   A C     1 
ATOM   7261  O  O     . PRO   A  1 1022 ? -10.621 73.080  107.765 1.00 21.24 ? 1020 PRO   A O     1 
ATOM   7262  C  CB    . PRO   A  1 1022 ? -8.220  71.004  108.891 1.00 17.99 ? 1020 PRO   A CB    1 
ATOM   7263  C  CG    . PRO   A  1 1022 ? -8.359  71.730  110.207 1.00 20.70 ? 1020 PRO   A CG    1 
ATOM   7264  C  CD    . PRO   A  1 1022 ? -7.816  73.116  109.964 1.00 20.33 ? 1020 PRO   A CD    1 
ATOM   7265  N  N     . LYS   A  1 1023 ? -10.267 71.234  106.540 1.00 18.84 ? 1021 LYS   A N     1 
ATOM   7266  C  CA    . LYS   A  1 1023 ? -11.613 71.240  105.985 1.00 19.86 ? 1021 LYS   A CA    1 
ATOM   7267  C  C     . LYS   A  1 1023 ? -12.653 70.987  107.060 1.00 19.35 ? 1021 LYS   A C     1 
ATOM   7268  O  O     . LYS   A  1 1023 ? -12.527 70.059  107.861 1.00 16.19 ? 1021 LYS   A O     1 
ATOM   7269  C  CB    . LYS   A  1 1023 ? -11.753 70.166  104.916 1.00 19.52 ? 1021 LYS   A CB    1 
ATOM   7270  C  CG    . LYS   A  1 1023 ? -11.086 70.487  103.585 1.00 19.16 ? 1021 LYS   A CG    1 
ATOM   7271  C  CD    . LYS   A  1 1023 ? -11.314 69.313  102.658 1.00 19.10 ? 1021 LYS   A CD    1 
ATOM   7272  C  CE    . LYS   A  1 1023 ? -10.826 69.605  101.250 1.00 20.80 ? 1021 LYS   A CE    1 
ATOM   7273  N  NZ    . LYS   A  1 1023 ? -11.812 70.442  100.505 1.00 19.55 ? 1021 LYS   A NZ    1 
ATOM   7274  N  N     . ALA   A  1 1024 ? -13.713 71.788  107.034 1.00 17.05 ? 1022 ALA   A N     1 
ATOM   7275  C  CA    . ALA   A  1 1024 ? -14.888 71.485  107.831 1.00 18.80 ? 1022 ALA   A CA    1 
ATOM   7276  C  C     . ALA   A  1 1024 ? -15.538 70.206  107.319 1.00 17.29 ? 1022 ALA   A C     1 
ATOM   7277  O  O     . ALA   A  1 1024 ? -15.482 69.887  106.129 1.00 19.59 ? 1022 ALA   A O     1 
ATOM   7278  C  CB    . ALA   A  1 1024 ? -15.881 72.647  107.776 1.00 19.55 ? 1022 ALA   A CB    1 
ATOM   7279  N  N     . GLY   A  1 1025 ? -16.134 69.451  108.235 1.00 17.00 ? 1023 GLY   A N     1 
ATOM   7280  C  CA    . GLY   A  1 1025 ? -16.746 68.211  107.814 1.00 15.87 ? 1023 GLY   A CA    1 
ATOM   7281  C  C     . GLY   A  1 1025 ? -15.749 67.201  107.324 1.00 16.68 ? 1023 GLY   A C     1 
ATOM   7282  O  O     . GLY   A  1 1025 ? -16.108 66.303  106.555 1.00 17.11 ? 1023 GLY   A O     1 
ATOM   7283  N  N     . GLY   A  1 1026 ? -14.493 67.337  107.743 1.00 16.92 ? 1024 GLY   A N     1 
ATOM   7284  C  CA    . GLY   A  1 1026 ? -13.449 66.415  107.382 1.00 15.94 ? 1024 GLY   A CA    1 
ATOM   7285  C  C     . GLY   A  1 1026 ? -12.699 65.953  108.613 1.00 16.37 ? 1024 GLY   A C     1 
ATOM   7286  O  O     . GLY   A  1 1026 ? -12.884 66.471  109.718 1.00 16.48 ? 1024 GLY   A O     1 
ATOM   7287  N  N     . PRO   A  1 1027 ? -11.806 64.978  108.426 1.00 19.52 ? 1025 PRO   A N     1 
ATOM   7288  C  CA    . PRO   A  1 1027 ? -11.225 64.264  109.567 1.00 17.68 ? 1025 PRO   A CA    1 
ATOM   7289  C  C     . PRO   A  1 1027 ? -10.061 64.972  110.242 1.00 16.66 ? 1025 PRO   A C     1 
ATOM   7290  O  O     . PRO   A  1 1027 ? -9.630  64.513  111.308 1.00 17.51 ? 1025 PRO   A O     1 
ATOM   7291  C  CB    . PRO   A  1 1027 ? -10.759 62.944  108.938 1.00 16.41 ? 1025 PRO   A CB    1 
ATOM   7292  C  CG    . PRO   A  1 1027 ? -10.425 63.316  107.512 1.00 19.27 ? 1025 PRO   A CG    1 
ATOM   7293  C  CD    . PRO   A  1 1027 ? -11.458 64.360  107.134 1.00 17.95 ? 1025 PRO   A CD    1 
ATOM   7294  N  N     . LEU   A  1 1028 ? -9.524  66.037  109.654 1.00 16.50 ? 1026 LEU   A N     1 
ATOM   7295  C  CA    . LEU   A  1 1028 ? -8.461  66.813  110.277 1.00 16.64 ? 1026 LEU   A CA    1 
ATOM   7296  C  C     . LEU   A  1 1028 ? -8.983  67.932  111.156 1.00 16.73 ? 1026 LEU   A C     1 
ATOM   7297  O  O     . LEU   A  1 1028 ? -8.195  68.560  111.870 1.00 17.56 ? 1026 LEU   A O     1 
ATOM   7298  C  CB    . LEU   A  1 1028 ? -7.541  67.416  109.206 1.00 16.56 ? 1026 LEU   A CB    1 
ATOM   7299  C  CG    . LEU   A  1 1028 ? -6.706  66.339  108.519 1.00 19.36 ? 1026 LEU   A CG    1 
ATOM   7300  C  CD1   . LEU   A  1 1028 ? -5.933  66.927  107.344 1.00 24.10 ? 1026 LEU   A CD1   1 
ATOM   7301  C  CD2   . LEU   A  1 1028 ? -5.740  65.765  109.560 1.00 22.00 ? 1026 LEU   A CD2   1 
ATOM   7302  N  N     . TYR   A  1 1029 ? -10.291 68.182  111.133 1.00 16.65 ? 1027 TYR   A N     1 
ATOM   7303  C  CA    . TYR   A  1 1029 ? -10.841 69.389  111.736 1.00 17.31 ? 1027 TYR   A CA    1 
ATOM   7304  C  C     . TYR   A  1 1029 ? -10.645 69.420  113.248 1.00 16.99 ? 1027 TYR   A C     1 
ATOM   7305  O  O     . TYR   A  1 1029 ? -10.138 70.405  113.799 1.00 17.14 ? 1027 TYR   A O     1 
ATOM   7306  C  CB    . TYR   A  1 1029 ? -12.321 69.462  111.390 1.00 18.04 ? 1027 TYR   A CB    1 
ATOM   7307  C  CG    . TYR   A  1 1029 ? -12.951 70.816  111.427 1.00 16.61 ? 1027 TYR   A CG    1 
ATOM   7308  C  CD1   . TYR   A  1 1029 ? -12.592 71.804  110.525 1.00 20.05 ? 1027 TYR   A CD1   1 
ATOM   7309  C  CD2   . TYR   A  1 1029 ? -13.969 71.086  112.331 1.00 17.20 ? 1027 TYR   A CD2   1 
ATOM   7310  C  CE1   . TYR   A  1 1029 ? -13.213 73.043  110.542 1.00 19.08 ? 1027 TYR   A CE1   1 
ATOM   7311  C  CE2   . TYR   A  1 1029 ? -14.595 72.305  112.348 1.00 20.05 ? 1027 TYR   A CE2   1 
ATOM   7312  C  CZ    . TYR   A  1 1029 ? -14.221 73.274  111.456 1.00 23.57 ? 1027 TYR   A CZ    1 
ATOM   7313  O  OH    . TYR   A  1 1029 ? -14.873 74.479  111.497 1.00 20.03 ? 1027 TYR   A OH    1 
ATOM   7314  N  N     . LEU   A  1 1030 ? -11.082 68.369  113.946 1.00 17.08 ? 1028 LEU   A N     1 
ATOM   7315  C  CA    . LEU   A  1 1030 ? -11.006 68.385  115.407 1.00 18.89 ? 1028 LEU   A CA    1 
ATOM   7316  C  C     . LEU   A  1 1030 ? -9.572  68.502  115.902 1.00 18.35 ? 1028 LEU   A C     1 
ATOM   7317  O  O     . LEU   A  1 1030 ? -9.327  69.124  116.941 1.00 18.35 ? 1028 LEU   A O     1 
ATOM   7318  C  CB    . LEU   A  1 1030 ? -11.649 67.131  115.994 1.00 18.62 ? 1028 LEU   A CB    1 
ATOM   7319  C  CG    . LEU   A  1 1030 ? -13.146 66.960  115.718 1.00 18.91 ? 1028 LEU   A CG    1 
ATOM   7320  C  CD1   . LEU   A  1 1030 ? -13.657 65.743  116.435 1.00 18.00 ? 1028 LEU   A CD1   1 
ATOM   7321  C  CD2   . LEU   A  1 1030 ? -13.893 68.182  116.197 1.00 19.67 ? 1028 LEU   A CD2   1 
ATOM   7322  N  N     . GLY   A  1 1031 ? -8.617  67.909  115.184 1.00 18.49 ? 1029 GLY   A N     1 
ATOM   7323  C  CA    . GLY   A  1 1031 ? -7.230  67.939  115.625 1.00 19.82 ? 1029 GLY   A CA    1 
ATOM   7324  C  C     . GLY   A  1 1031 ? -6.641  69.331  115.702 1.00 21.90 ? 1029 GLY   A C     1 
ATOM   7325  O  O     . GLY   A  1 1031 ? -5.635  69.541  116.396 1.00 19.05 ? 1029 GLY   A O     1 
ATOM   7326  N  N     . ARG   A  1 1032 ? -7.228  70.283  114.985 1.00 17.53 ? 1030 ARG   A N     1 
ATOM   7327  C  CA    . ARG   A  1 1032 ? -6.806  71.668  115.070 1.00 19.05 ? 1030 ARG   A CA    1 
ATOM   7328  C  C     . ARG   A  1 1032 ? -7.284  72.331  116.352 1.00 21.57 ? 1030 ARG   A C     1 
ATOM   7329  O  O     . ARG   A  1 1032 ? -6.786  73.401  116.703 1.00 19.38 ? 1030 ARG   A O     1 
ATOM   7330  C  CB    . ARG   A  1 1032 ? -7.328  72.440  113.853 1.00 18.14 ? 1030 ARG   A CB    1 
ATOM   7331  C  CG    . ARG   A  1 1032 ? -6.735  73.833  113.670 1.00 21.94 ? 1030 ARG   A CG    1 
ATOM   7332  C  CD    . ARG   A  1 1032 ? -5.256  73.776  113.288 1.00 22.25 ? 1030 ARG   A CD    1 
ATOM   7333  N  NE    . ARG   A  1 1032 ? -4.785  75.085  112.832 1.00 23.19 ? 1030 ARG   A NE    1 
ATOM   7334  C  CZ    . ARG   A  1 1032 ? -3.766  75.755  113.355 1.00 30.87 ? 1030 ARG   A CZ    1 
ATOM   7335  N  NH1   . ARG   A  1 1032 ? -3.028  75.246  114.330 1.00 24.18 ? 1030 ARG   A NH1   1 
ATOM   7336  N  NH2   . ARG   A  1 1032 ? -3.480  76.970  112.886 1.00 25.09 ? 1030 ARG   A NH2   1 
ATOM   7337  N  N     . LEU   A  1 1033 ? -8.237  71.721  117.053 1.00 18.53 ? 1031 LEU   A N     1 
ATOM   7338  C  CA    . LEU   A  1 1033 ? -8.895  72.346  118.189 1.00 19.11 ? 1031 LEU   A CA    1 
ATOM   7339  C  C     . LEU   A  1 1033 ? -8.406  71.777  119.511 1.00 22.70 ? 1031 LEU   A C     1 
ATOM   7340  O  O     . LEU   A  1 1033 ? -9.044  71.979  120.544 1.00 19.46 ? 1031 LEU   A O     1 
ATOM   7341  C  CB    . LEU   A  1 1033 ? -10.411 72.196  118.052 1.00 18.02 ? 1031 LEU   A CB    1 
ATOM   7342  C  CG    . LEU   A  1 1033 ? -10.930 72.728  116.709 1.00 20.94 ? 1031 LEU   A CG    1 
ATOM   7343  C  CD1   . LEU   A  1 1033 ? -12.428 72.541  116.560 1.00 17.65 ? 1031 LEU   A CD1   1 
ATOM   7344  C  CD2   . LEU   A  1 1033 ? -10.575 74.201  116.524 1.00 20.91 ? 1031 LEU   A CD2   1 
ATOM   7345  N  N     . VAL   A  1 1034 ? -7.283  71.058  119.488 1.00 19.53 ? 1032 VAL   A N     1 
ATOM   7346  C  CA    . VAL   A  1 1034 ? -6.659  70.499  120.677 1.00 18.74 ? 1032 VAL   A CA    1 
ATOM   7347  C  C     . VAL   A  1 1034 ? -5.178  70.816  120.573 1.00 21.13 ? 1032 VAL   A C     1 
ATOM   7348  O  O     . VAL   A  1 1034 ? -4.657  71.097  119.493 1.00 21.48 ? 1032 VAL   A O     1 
ATOM   7349  C  CB    . VAL   A  1 1034 ? -6.896  68.978  120.814 1.00 19.15 ? 1032 VAL   A CB    1 
ATOM   7350  C  CG1   . VAL   A  1 1034 ? -8.377  68.679  121.137 1.00 19.02 ? 1032 VAL   A CG1   1 
ATOM   7351  C  CG2   . VAL   A  1 1034 ? -6.495  68.252  119.546 1.00 18.83 ? 1032 VAL   A CG2   1 
ATOM   7352  N  N     . THR   A  1 1035 ? -4.495  70.765  121.708 1.00 23.03 ? 1033 THR   A N     1 
ATOM   7353  C  CA    . THR   A  1 1035 ? -3.090  71.137  121.699 1.00 25.94 ? 1033 THR   A CA    1 
ATOM   7354  C  C     . THR   A  1 1035 ? -2.210  70.018  121.161 1.00 25.59 ? 1033 THR   A C     1 
ATOM   7355  O  O     . THR   A  1 1035 ? -1.109  70.285  120.669 1.00 31.04 ? 1033 THR   A O     1 
ATOM   7356  C  CB    . THR   A  1 1035 ? -2.649  71.532  123.106 1.00 31.82 ? 1033 THR   A CB    1 
ATOM   7357  O  OG1   . THR   A  1 1035 ? -3.028  70.497  124.016 1.00 32.53 ? 1033 THR   A OG1   1 
ATOM   7358  C  CG2   . THR   A  1 1035 ? -3.331  72.825  123.516 1.00 29.27 ? 1033 THR   A CG2   1 
ATOM   7359  N  N     . THR   A  1 1036 ? -2.668  68.772  121.242 1.00 23.62 ? 1034 THR   A N     1 
ATOM   7360  C  CA    . THR   A  1 1036 ? -1.953  67.641  120.660 1.00 22.28 ? 1034 THR   A CA    1 
ATOM   7361  C  C     . THR   A  1 1036 ? -2.928  66.913  119.749 1.00 22.86 ? 1034 THR   A C     1 
ATOM   7362  O  O     . THR   A  1 1036 ? -3.915  66.346  120.222 1.00 23.27 ? 1034 THR   A O     1 
ATOM   7363  C  CB    . THR   A  1 1036 ? -1.405  66.704  121.730 1.00 25.25 ? 1034 THR   A CB    1 
ATOM   7364  O  OG1   . THR   A  1 1036 ? -0.526  67.436  122.592 1.00 29.73 ? 1034 THR   A OG1   1 
ATOM   7365  C  CG2   . THR   A  1 1036 ? -0.618  65.571  121.062 1.00 34.48 ? 1034 THR   A CG2   1 
ATOM   7366  N  N     . ALA   A  1 1037 ? -2.652  66.927  118.460 1.00 22.58 ? 1035 ALA   A N     1 
ATOM   7367  C  CA    . ALA   A  1 1037 ? -3.617  66.408  117.501 1.00 21.18 ? 1035 ALA   A CA    1 
ATOM   7368  C  C     . ALA   A  1 1037 ? -3.645  64.881  117.554 1.00 21.16 ? 1035 ALA   A C     1 
ATOM   7369  O  O     . ALA   A  1 1037 ? -2.592  64.241  117.642 1.00 21.31 ? 1035 ALA   A O     1 
ATOM   7370  C  CB    . ALA   A  1 1037 ? -3.274  66.886  116.089 1.00 20.84 ? 1035 ALA   A CB    1 
ATOM   7371  N  N     . PRO   A  1 1038 ? -4.824  64.273  117.523 1.00 22.35 ? 1036 PRO   A N     1 
ATOM   7372  C  CA    . PRO   A  1 1038 ? -4.904  62.815  117.417 1.00 20.89 ? 1036 PRO   A CA    1 
ATOM   7373  C  C     . PRO   A  1 1038 ? -4.617  62.381  115.986 1.00 20.84 ? 1036 PRO   A C     1 
ATOM   7374  O  O     . PRO   A  1 1038 ? -4.563  63.187  115.057 1.00 21.54 ? 1036 PRO   A O     1 
ATOM   7375  C  CB    . PRO   A  1 1038 ? -6.352  62.512  117.805 1.00 20.49 ? 1036 PRO   A CB    1 
ATOM   7376  C  CG    . PRO   A  1 1038 ? -7.099  63.725  117.271 1.00 20.24 ? 1036 PRO   A CG    1 
ATOM   7377  C  CD    . PRO   A  1 1038 ? -6.160  64.903  117.519 1.00 19.51 ? 1036 PRO   A CD    1 
ATOM   7378  N  N     . VAL   A  1 1039 ? -4.439  61.077  115.827 1.00 19.47 ? 1037 VAL   A N     1 
ATOM   7379  C  CA    . VAL   A  1 1039 ? -4.343  60.472  114.501 1.00 21.45 ? 1037 VAL   A CA    1 
ATOM   7380  C  C     . VAL   A  1 1039 ? -5.757  60.278  113.967 1.00 19.15 ? 1037 VAL   A C     1 
ATOM   7381  O  O     . VAL   A  1 1039 ? -6.523  59.486  114.538 1.00 19.80 ? 1037 VAL   A O     1 
ATOM   7382  C  CB    . VAL   A  1 1039 ? -3.581  59.142  114.563 1.00 24.07 ? 1037 VAL   A CB    1 
ATOM   7383  C  CG1   . VAL   A  1 1039 ? -3.494  58.520  113.178 1.00 23.28 ? 1037 VAL   A CG1   1 
ATOM   7384  C  CG2   . VAL   A  1 1039 ? -2.201  59.360  115.150 1.00 23.73 ? 1037 VAL   A CG2   1 
ATOM   7385  N  N     . PRO   A  1 1040 ? -6.152  60.962  112.892 1.00 19.70 ? 1038 PRO   A N     1 
ATOM   7386  C  CA    . PRO   A  1 1040 ? -7.523  60.837  112.407 1.00 20.01 ? 1038 PRO   A CA    1 
ATOM   7387  C  C     . PRO   A  1 1040 ? -7.792  59.439  111.886 1.00 18.02 ? 1038 PRO   A C     1 
ATOM   7388  O  O     . PRO   A  1 1040 ? -6.857  58.709  111.515 1.00 19.91 ? 1038 PRO   A O     1 
ATOM   7389  C  CB    . PRO   A  1 1040 ? -7.606  61.881  111.278 1.00 19.85 ? 1038 PRO   A CB    1 
ATOM   7390  C  CG    . PRO   A  1 1040 ? -6.504  62.837  111.550 1.00 20.50 ? 1038 PRO   A CG    1 
ATOM   7391  C  CD    . PRO   A  1 1040 ? -5.405  62.002  112.168 1.00 18.51 ? 1038 PRO   A CD    1 
ATOM   7392  N  N     . PRO   A  1 1041 ? -9.054  59.023  111.869 1.00 19.37 ? 1039 PRO   A N     1 
ATOM   7393  C  CA    . PRO   A  1 1041 ? -9.401  57.748  111.241 1.00 17.25 ? 1039 PRO   A CA    1 
ATOM   7394  C  C     . PRO   A  1 1041 ? -8.900  57.723  109.809 1.00 17.46 ? 1039 PRO   A C     1 
ATOM   7395  O  O     . PRO   A  1 1041 ? -8.956  58.728  109.096 1.00 19.23 ? 1039 PRO   A O     1 
ATOM   7396  C  CB    . PRO   A  1 1041 ? -10.935 57.725  111.298 1.00 21.54 ? 1039 PRO   A CB    1 
ATOM   7397  C  CG    . PRO   A  1 1041 ? -11.292 58.713  112.350 1.00 22.31 ? 1039 PRO   A CG    1 
ATOM   7398  C  CD    . PRO   A  1 1041 ? -10.249 59.778  112.283 1.00 20.10 ? 1039 PRO   A CD    1 
ATOM   7399  N  N     . GLN   A  1 1042 ? -8.376  56.572  109.413 1.00 17.62 ? 1040 GLN   A N     1 
ATOM   7400  C  CA    . GLN   A  1 1042 ? -7.917  56.280  108.061 1.00 18.50 ? 1040 GLN   A CA    1 
ATOM   7401  C  C     . GLN   A  1 1042 ? -6.791  57.192  107.596 1.00 21.61 ? 1040 GLN   A C     1 
ATOM   7402  O  O     . GLN   A  1 1042 ? -6.499  57.228  106.398 1.00 21.02 ? 1040 GLN   A O     1 
ATOM   7403  C  CB    . GLN   A  1 1042 ? -9.075  56.350  107.057 1.00 21.51 ? 1040 GLN   A CB    1 
ATOM   7404  C  CG    . GLN   A  1 1042 ? -10.161 55.340  107.338 1.00 24.37 ? 1040 GLN   A CG    1 
ATOM   7405  C  CD    . GLN   A  1 1042 ? -11.116 55.241  106.184 1.00 30.68 ? 1040 GLN   A CD    1 
ATOM   7406  O  OE1   . GLN   A  1 1042 ? -12.195 55.809  106.216 1.00 30.87 ? 1040 GLN   A OE1   1 
ATOM   7407  N  NE2   . GLN   A  1 1042 ? -10.707 54.540  105.142 1.00 32.52 ? 1040 GLN   A NE2   1 
ATOM   7408  N  N     . HIS   A  1 1043 ? -6.145  57.921  108.509 1.00 19.22 ? 1041 HIS   A N     1 
ATOM   7409  C  CA    . HIS   A  1 1043 ? -5.161  58.941  108.151 1.00 18.50 ? 1041 HIS   A CA    1 
ATOM   7410  C  C     . HIS   A  1 1043 ? -3.773  58.315  108.200 1.00 19.38 ? 1041 HIS   A C     1 
ATOM   7411  O  O     . HIS   A  1 1043 ? -3.160  58.214  109.265 1.00 19.71 ? 1041 HIS   A O     1 
ATOM   7412  C  CB    . HIS   A  1 1043 ? -5.269  60.132  109.091 1.00 18.08 ? 1041 HIS   A CB    1 
ATOM   7413  C  CG    . HIS   A  1 1043 ? -4.300  61.235  108.807 1.00 20.22 ? 1041 HIS   A CG    1 
ATOM   7414  N  ND1   . HIS   A  1 1043 ? -4.600  62.292  107.977 1.00 18.28 ? 1041 HIS   A ND1   1 
ATOM   7415  C  CD2   . HIS   A  1 1043 ? -3.054  61.475  109.287 1.00 19.25 ? 1041 HIS   A CD2   1 
ATOM   7416  C  CE1   . HIS   A  1 1043 ? -3.578  63.127  107.942 1.00 20.59 ? 1041 HIS   A CE1   1 
ATOM   7417  N  NE2   . HIS   A  1 1043 ? -2.626  62.656  108.731 1.00 20.82 ? 1041 HIS   A NE2   1 
ATOM   7418  N  N     . SER   A  1 1044 ? -3.295  57.874  107.043 1.00 18.55 ? 1042 SER   A N     1 
ATOM   7419  C  CA    . SER   A  1 1044 ? -1.963  57.309  106.883 1.00 19.16 ? 1042 SER   A CA    1 
ATOM   7420  C  C     . SER   A  1 1044 ? -1.697  57.212  105.390 1.00 19.85 ? 1042 SER   A C     1 
ATOM   7421  O  O     . SER   A  1 1044 ? -2.618  57.320  104.576 1.00 19.00 ? 1042 SER   A O     1 
ATOM   7422  C  CB    . SER   A  1 1044 ? -1.837  55.931  107.536 1.00 18.64 ? 1042 SER   A CB    1 
ATOM   7423  O  OG    . SER   A  1 1044 ? -2.587  54.968  106.813 1.00 21.01 ? 1042 SER   A OG    1 
ATOM   7424  N  N     . SER   A  1 1045 ? -0.429  56.998  105.043 1.00 18.27 ? 1043 SER   A N     1 
ATOM   7425  C  CA    . SER   A  1 1045 ? -0.042  56.780  103.656 1.00 20.61 ? 1043 SER   A CA    1 
ATOM   7426  C  C     . SER   A  1 1045 ? 1.159   55.856  103.630 1.00 17.66 ? 1043 SER   A C     1 
ATOM   7427  O  O     . SER   A  1 1045 ? 2.058   55.987  104.460 1.00 19.63 ? 1043 SER   A O     1 
ATOM   7428  C  CB    . SER   A  1 1045 ? 0.327   58.082  102.947 1.00 18.11 ? 1043 SER   A CB    1 
ATOM   7429  O  OG    . SER   A  1 1045 ? 0.677   57.813  101.602 1.00 20.18 ? 1043 SER   A OG    1 
ATOM   7430  N  N     . VAL   A  1 1046 ? 1.172   54.921  102.675 1.00 17.72 ? 1044 VAL   A N     1 
ATOM   7431  C  CA    . VAL   A  1 1046 ? 2.340   54.070  102.517 1.00 20.13 ? 1044 VAL   A CA    1 
ATOM   7432  C  C     . VAL   A  1 1046 ? 3.370   54.704  101.609 1.00 19.22 ? 1044 VAL   A C     1 
ATOM   7433  O  O     . VAL   A  1 1046 ? 4.439   54.125  101.413 1.00 21.05 ? 1044 VAL   A O     1 
ATOM   7434  C  CB    . VAL   A  1 1046 ? 1.976   52.669  101.974 1.00 20.37 ? 1044 VAL   A CB    1 
ATOM   7435  C  CG1   . VAL   A  1 1046 ? 1.028   51.966  102.931 1.00 24.14 ? 1044 VAL   A CG1   1 
ATOM   7436  C  CG2   . VAL   A  1 1046 ? 1.373   52.774  100.609 1.00 17.94 ? 1044 VAL   A CG2   1 
ATOM   7437  N  N     . HIS   A  1 1047 ? 3.080   55.874  101.047 1.00 19.89 ? 1045 HIS   A N     1 
ATOM   7438  C  CA    A HIS   A  1 1047 ? 3.980   56.571  100.128 0.58 22.42 ? 1045 HIS   A CA    1 
ATOM   7439  C  CA    B HIS   A  1 1047 ? 4.018   56.510  100.144 0.42 22.41 ? 1045 HIS   A CA    1 
ATOM   7440  C  C     . HIS   A  1 1047 ? 4.946   57.439  100.914 1.00 21.25 ? 1045 HIS   A C     1 
ATOM   7441  O  O     . HIS   A  1 1047 ? 4.551   58.076  101.894 1.00 22.07 ? 1045 HIS   A O     1 
ATOM   7442  C  CB    A HIS   A  1 1047 ? 3.187   57.449  99.154  0.58 23.59 ? 1045 HIS   A CB    1 
ATOM   7443  C  CB    B HIS   A  1 1047 ? 3.252   57.240  99.045  0.42 23.58 ? 1045 HIS   A CB    1 
ATOM   7444  C  CG    A HIS   A  1 1047 ? 3.991   58.556  98.534  0.58 22.24 ? 1045 HIS   A CG    1 
ATOM   7445  C  CG    B HIS   A  1 1047 ? 2.328   56.336  98.289  0.42 22.08 ? 1045 HIS   A CG    1 
ATOM   7446  N  ND1   A HIS   A  1 1047 ? 4.850   58.352  97.474  0.58 23.02 ? 1045 HIS   A ND1   1 
ATOM   7447  N  ND1   B HIS   A  1 1047 ? 2.781   55.253  97.565  0.42 21.68 ? 1045 HIS   A ND1   1 
ATOM   7448  C  CD2   A HIS   A  1 1047 ? 4.058   59.879  98.820  0.58 23.27 ? 1045 HIS   A CD2   1 
ATOM   7449  C  CD2   B HIS   A  1 1047 ? 0.978   56.320  98.185  0.42 23.85 ? 1045 HIS   A CD2   1 
ATOM   7450  C  CE1   A HIS   A  1 1047 ? 5.411   59.500  97.136  0.58 23.63 ? 1045 HIS   A CE1   1 
ATOM   7451  C  CE1   B HIS   A  1 1047 ? 1.752   54.625  97.027  0.42 21.75 ? 1045 HIS   A CE1   1 
ATOM   7452  N  NE2   A HIS   A  1 1047 ? 4.951   60.443  97.941  0.58 17.78 ? 1045 HIS   A NE2   1 
ATOM   7453  N  NE2   B HIS   A  1 1047 ? 0.646   55.252  97.388  0.42 23.41 ? 1045 HIS   A NE2   1 
ATOM   7454  N  N     . THR   A  1 1048 ? 6.206   57.460  100.488 1.00 21.11 ? 1046 THR   A N     1 
ATOM   7455  C  CA    . THR   A  1 1048 ? 7.229   58.296  101.091 1.00 22.78 ? 1046 THR   A CA    1 
ATOM   7456  C  C     . THR   A  1 1048 ? 7.716   59.278  100.039 1.00 21.31 ? 1046 THR   A C     1 
ATOM   7457  O  O     . THR   A  1 1048 ? 8.082   58.876  98.928  1.00 21.77 ? 1046 THR   A O     1 
ATOM   7458  C  CB    . THR   A  1 1048 ? 8.400   57.463  101.625 1.00 21.76 ? 1046 THR   A CB    1 
ATOM   7459  O  OG1   . THR   A  1 1048 ? 7.885   56.427  102.461 1.00 21.60 ? 1046 THR   A OG1   1 
ATOM   7460  C  CG2   . THR   A  1 1048 ? 9.321   58.326  102.456 1.00 20.77 ? 1046 THR   A CG2   1 
ATOM   7461  N  N     . ASP   A  1 1049 ? 7.695   60.553  100.377 1.00 20.78 ? 1047 ASP   A N     1 
ATOM   7462  C  CA    . ASP   A  1 1049 ? 8.208   61.551  99.459  1.00 20.01 ? 1047 ASP   A CA    1 
ATOM   7463  C  C     . ASP   A  1 1049 ? 9.655   61.221  99.100  1.00 18.51 ? 1047 ASP   A C     1 
ATOM   7464  O  O     . ASP   A  1 1049 ? 10.480  61.005  100.001 1.00 19.10 ? 1047 ASP   A O     1 
ATOM   7465  C  CB    . ASP   A  1 1049 ? 8.120   62.950  100.066 1.00 18.13 ? 1047 ASP   A CB    1 
ATOM   7466  C  CG    . ASP   A  1 1049 ? 8.563   64.025  99.080  1.00 19.61 ? 1047 ASP   A CG    1 
ATOM   7467  O  OD1   . ASP   A  1 1049 ? 9.788   64.243  98.944  1.00 21.45 ? 1047 ASP   A OD1   1 
ATOM   7468  O  OD2   . ASP   A  1 1049 ? 7.689   64.598  98.391  1.00 21.75 ? 1047 ASP   A OD2   1 
ATOM   7469  N  N     . PRO   A  1 1050 ? 10.001  61.159  97.813  1.00 18.74 ? 1048 PRO   A N     1 
ATOM   7470  C  CA    . PRO   A  1 1050 ? 11.373  60.766  97.454  1.00 18.91 ? 1048 PRO   A CA    1 
ATOM   7471  C  C     . PRO   A  1 1050 ? 12.392  61.853  97.730  1.00 19.91 ? 1048 PRO   A C     1 
ATOM   7472  O  O     . PRO   A  1 1050 ? 13.582  61.556  97.903  1.00 20.44 ? 1048 PRO   A O     1 
ATOM   7473  C  CB    . PRO   A  1 1050 ? 11.268  60.456  95.954  1.00 24.59 ? 1048 PRO   A CB    1 
ATOM   7474  C  CG    . PRO   A  1 1050 ? 10.127  61.291  95.484  1.00 21.09 ? 1048 PRO   A CG    1 
ATOM   7475  C  CD    . PRO   A  1 1050 ? 9.142   61.342  96.625  1.00 20.59 ? 1048 PRO   A CD    1 
ATOM   7476  N  N     . VAL   A  1 1051 ? 11.976  63.115  97.743  1.00 19.16 ? 1049 VAL   A N     1 
ATOM   7477  C  CA    . VAL   A  1 1051 ? 12.934  64.166  98.058  1.00 19.99 ? 1049 VAL   A CA    1 
ATOM   7478  C  C     . VAL   A  1 1051 ? 13.235  64.164  99.552  1.00 19.18 ? 1049 VAL   A C     1 
ATOM   7479  O  O     . VAL   A  1 1051 ? 14.375  64.401  99.975  1.00 19.44 ? 1049 VAL   A O     1 
ATOM   7480  C  CB    . VAL   A  1 1051 ? 12.403  65.524  97.570  1.00 18.99 ? 1049 VAL   A CB    1 
ATOM   7481  C  CG1   . VAL   A  1 1051 ? 13.378  66.626  97.941  1.00 23.39 ? 1049 VAL   A CG1   1 
ATOM   7482  C  CG2   . VAL   A  1 1051 ? 12.183  65.485  96.053  1.00 19.68 ? 1049 VAL   A CG2   1 
ATOM   7483  N  N     . LEU   A  1 1052 ? 12.223  63.881  100.375 1.00 18.96 ? 1050 LEU   A N     1 
ATOM   7484  C  CA    . LEU   A  1 1052 ? 12.475  63.610  101.784 1.00 19.04 ? 1050 LEU   A CA    1 
ATOM   7485  C  C     . LEU   A  1 1052 ? 13.553  62.545  101.931 1.00 19.32 ? 1050 LEU   A C     1 
ATOM   7486  O  O     . LEU   A  1 1052 ? 14.498  62.699  102.714 1.00 19.55 ? 1050 LEU   A O     1 
ATOM   7487  C  CB    . LEU   A  1 1052 ? 11.181  63.178  102.481 1.00 18.80 ? 1050 LEU   A CB    1 
ATOM   7488  C  CG    . LEU   A  1 1052 ? 11.211  62.775  103.972 1.00 19.06 ? 1050 LEU   A CG    1 
ATOM   7489  C  CD1   . LEU   A  1 1052 ? 11.750  61.355  104.211 1.00 19.07 ? 1050 LEU   A CD1   1 
ATOM   7490  C  CD2   . LEU   A  1 1052 ? 12.017  63.777  104.792 1.00 19.05 ? 1050 LEU   A CD2   1 
ATOM   7491  N  N     . LEU   A  1 1053 ? 13.417  61.444  101.187 1.00 19.33 ? 1051 LEU   A N     1 
ATOM   7492  C  CA    . LEU   A  1 1053 ? 14.386  60.358  101.290 1.00 20.42 ? 1051 LEU   A CA    1 
ATOM   7493  C  C     . LEU   A  1 1053 ? 15.775  60.811  100.863 1.00 19.91 ? 1051 LEU   A C     1 
ATOM   7494  O  O     . LEU   A  1 1053 ? 16.768  60.477  101.514 1.00 20.17 ? 1051 LEU   A O     1 
ATOM   7495  C  CB    . LEU   A  1 1053 ? 13.926  59.164  100.453 1.00 21.02 ? 1051 LEU   A CB    1 
ATOM   7496  C  CG    . LEU   A  1 1053 ? 12.719  58.396  101.009 1.00 20.52 ? 1051 LEU   A CG    1 
ATOM   7497  C  CD1   . LEU   A  1 1053 ? 12.310  57.314  100.020 1.00 21.21 ? 1051 LEU   A CD1   1 
ATOM   7498  C  CD2   . LEU   A  1 1053 ? 13.020  57.805  102.380 1.00 20.88 ? 1051 LEU   A CD2   1 
ATOM   7499  N  N     . ASP   A  1 1054 ? 15.870  61.558  99.763  1.00 20.43 ? 1052 ASP   A N     1 
ATOM   7500  C  CA    . ASP   A  1 1054 ? 17.168  62.089  99.362  1.00 20.19 ? 1052 ASP   A CA    1 
ATOM   7501  C  C     . ASP   A  1 1054 ? 17.744  62.994  100.440 1.00 20.29 ? 1052 ASP   A C     1 
ATOM   7502  O  O     . ASP   A  1 1054 ? 18.948  62.945  100.725 1.00 21.87 ? 1052 ASP   A O     1 
ATOM   7503  C  CB    . ASP   A  1 1054 ? 17.056  62.857  98.048  1.00 20.15 ? 1052 ASP   A CB    1 
ATOM   7504  C  CG    . ASP   A  1 1054 ? 16.705  61.969  96.875  1.00 25.33 ? 1052 ASP   A CG    1 
ATOM   7505  O  OD1   . ASP   A  1 1054 ? 16.830  60.729  96.997  1.00 23.99 ? 1052 ASP   A OD1   1 
ATOM   7506  O  OD2   . ASP   A  1 1054 ? 16.306  62.530  95.832  1.00 27.53 ? 1052 ASP   A OD2   1 
ATOM   7507  N  N     . PHE   A  1 1055 ? 16.901  63.830  101.043 1.00 20.06 ? 1053 PHE   A N     1 
ATOM   7508  C  CA    . PHE   A  1 1055 ? 17.365  64.712  102.108 1.00 20.16 ? 1053 PHE   A CA    1 
ATOM   7509  C  C     . PHE   A  1 1055 ? 17.856  63.921  103.314 1.00 20.32 ? 1053 PHE   A C     1 
ATOM   7510  O  O     . PHE   A  1 1055 ? 18.880  64.265  103.917 1.00 20.93 ? 1053 PHE   A O     1 
ATOM   7511  C  CB    . PHE   A  1 1055 ? 16.241  65.671  102.509 1.00 19.89 ? 1053 PHE   A CB    1 
ATOM   7512  C  CG    . PHE   A  1 1055 ? 16.632  66.634  103.586 1.00 20.00 ? 1053 PHE   A CG    1 
ATOM   7513  C  CD1   . PHE   A  1 1055 ? 17.732  67.469  103.416 1.00 22.12 ? 1053 PHE   A CD1   1 
ATOM   7514  C  CD2   . PHE   A  1 1055 ? 15.899  66.717  104.756 1.00 19.87 ? 1053 PHE   A CD2   1 
ATOM   7515  C  CE1   . PHE   A  1 1055 ? 18.100  68.372  104.425 1.00 23.40 ? 1053 PHE   A CE1   1 
ATOM   7516  C  CE2   . PHE   A  1 1055 ? 16.253  67.616  105.757 1.00 20.00 ? 1053 PHE   A CE2   1 
ATOM   7517  C  CZ    . PHE   A  1 1055 ? 17.360  68.437  105.588 1.00 20.27 ? 1053 PHE   A CZ    1 
ATOM   7518  N  N     . ALA   A  1 1056 ? 17.136  62.863  103.695 1.00 20.19 ? 1054 ALA   A N     1 
ATOM   7519  C  CA    . ALA   A  1 1056 ? 17.586  62.068  104.834 1.00 20.37 ? 1054 ALA   A CA    1 
ATOM   7520  C  C     . ALA   A  1 1056 ? 18.943  61.427  104.556 1.00 22.24 ? 1054 ALA   A C     1 
ATOM   7521  O  O     . ALA   A  1 1056 ? 19.794  61.366  105.451 1.00 22.91 ? 1054 ALA   A O     1 
ATOM   7522  C  CB    . ALA   A  1 1056 ? 16.543  61.018  105.206 1.00 21.67 ? 1054 ALA   A CB    1 
ATOM   7523  N  N     . LYS   A  1 1057 ? 19.175  60.953  103.317 1.00 21.56 ? 1055 LYS   A N     1 
ATOM   7524  C  CA    . LYS   A  1 1057 ? 20.495  60.422  102.968 1.00 22.85 ? 1055 LYS   A CA    1 
ATOM   7525  C  C     . LYS   A  1 1057 ? 21.560  61.506  103.020 1.00 24.99 ? 1055 LYS   A C     1 
ATOM   7526  O  O     . LYS   A  1 1057 ? 22.679  61.271  103.500 1.00 27.58 ? 1055 LYS   A O     1 
ATOM   7527  C  CB    . LYS   A  1 1057 ? 20.465  59.789  101.573 1.00 23.43 ? 1055 LYS   A CB    1 
ATOM   7528  C  CG    . LYS   A  1 1057 ? 19.765  58.444  101.542 1.00 29.51 ? 1055 LYS   A CG    1 
ATOM   7529  C  CD    . LYS   A  1 1057 ? 19.969  57.745  100.205 1.00 28.67 ? 1055 LYS   A CD    1 
ATOM   7530  C  CE    . LYS   A  1 1057 ? 19.386  58.572  99.067  1.00 27.63 ? 1055 LYS   A CE    1 
ATOM   7531  N  NZ    . LYS   A  1 1057 ? 19.184  57.722  97.863  1.00 31.15 ? 1055 LYS   A NZ    1 
ATOM   7532  N  N     . TRP   A  1 1058 ? 21.243  62.689  102.496 1.00 22.67 ? 1056 TRP   A N     1 
ATOM   7533  C  CA    . TRP   A  1 1058 ? 22.168  63.810  102.589 1.00 24.95 ? 1056 TRP   A CA    1 
ATOM   7534  C  C     . TRP   A  1 1058 ? 22.499  64.134  104.039 1.00 26.98 ? 1056 TRP   A C     1 
ATOM   7535  O  O     . TRP   A  1 1058 ? 23.662  64.390  104.369 1.00 27.36 ? 1056 TRP   A O     1 
ATOM   7536  C  CB    . TRP   A  1 1058 ? 21.579  65.030  101.882 1.00 24.64 ? 1056 TRP   A CB    1 
ATOM   7537  C  CG    . TRP   A  1 1058 ? 22.419  66.259  101.993 1.00 26.11 ? 1056 TRP   A CG    1 
ATOM   7538  C  CD1   . TRP   A  1 1058 ? 23.432  66.646  101.154 1.00 31.18 ? 1056 TRP   A CD1   1 
ATOM   7539  C  CD2   . TRP   A  1 1058 ? 22.317  67.281  102.996 1.00 29.28 ? 1056 TRP   A CD2   1 
ATOM   7540  N  NE1   . TRP   A  1 1058 ? 23.964  67.841  101.581 1.00 33.21 ? 1056 TRP   A NE1   1 
ATOM   7541  C  CE2   . TRP   A  1 1058 ? 23.296  68.254  102.703 1.00 29.01 ? 1056 TRP   A CE2   1 
ATOM   7542  C  CE3   . TRP   A  1 1058 ? 21.494  67.467  104.114 1.00 24.41 ? 1056 TRP   A CE3   1 
ATOM   7543  C  CZ2   . TRP   A  1 1058 ? 23.474  69.396  103.487 1.00 29.27 ? 1056 TRP   A CZ2   1 
ATOM   7544  C  CZ3   . TRP   A  1 1058 ? 21.668  68.601  104.888 1.00 26.25 ? 1056 TRP   A CZ3   1 
ATOM   7545  C  CH2   . TRP   A  1 1058 ? 22.662  69.548  104.576 1.00 28.31 ? 1056 TRP   A CH2   1 
ATOM   7546  N  N     . LEU   A  1 1059 ? 21.492  64.121  104.921 1.00 23.42 ? 1057 LEU   A N     1 
ATOM   7547  C  CA    . LEU   A  1 1059 ? 21.742  64.392  106.336 1.00 23.04 ? 1057 LEU   A CA    1 
ATOM   7548  C  C     . LEU   A  1 1059 ? 22.735  63.399  106.912 1.00 27.61 ? 1057 LEU   A C     1 
ATOM   7549  O  O     . LEU   A  1 1059 ? 23.679  63.779  107.618 1.00 30.66 ? 1057 LEU   A O     1 
ATOM   7550  C  CB    . LEU   A  1 1059 ? 20.430  64.341  107.120 1.00 22.46 ? 1057 LEU   A CB    1 
ATOM   7551  C  CG    . LEU   A  1 1059 ? 19.517  65.552  106.950 1.00 22.43 ? 1057 LEU   A CG    1 
ATOM   7552  C  CD1   . LEU   A  1 1059 ? 18.154  65.277  107.556 1.00 22.05 ? 1057 LEU   A CD1   1 
ATOM   7553  C  CD2   . LEU   A  1 1059 ? 20.169  66.771  107.618 1.00 22.02 ? 1057 LEU   A CD2   1 
ATOM   7554  N  N     . ASP   A  1 1060 ? 22.536  62.113  106.620 1.00 24.09 ? 1058 ASP   A N     1 
ATOM   7555  C  CA    . ASP   A  1 1060 ? 23.474  61.101  107.090 1.00 31.31 ? 1058 ASP   A CA    1 
ATOM   7556  C  C     . ASP   A  1 1060 ? 24.868  61.335  106.524 1.00 32.44 ? 1058 ASP   A C     1 
ATOM   7557  O  O     . ASP   A  1 1060 ? 25.868  61.183  107.236 1.00 33.81 ? 1058 ASP   A O     1 
ATOM   7558  C  CB    . ASP   A  1 1060 ? 22.971  59.715  106.712 1.00 31.49 ? 1058 ASP   A CB    1 
ATOM   7559  C  CG    . ASP   A  1 1060 ? 22.149  59.091  107.803 1.00 32.51 ? 1058 ASP   A CG    1 
ATOM   7560  O  OD1   . ASP   A  1 1060 ? 22.447  59.353  108.995 1.00 34.80 ? 1058 ASP   A OD1   1 
ATOM   7561  O  OD2   . ASP   A  1 1060 ? 21.204  58.348  107.474 1.00 30.66 ? 1058 ASP   A OD2   1 
ATOM   7562  N  N     . GLY   A  1 1061 ? 24.954  61.710  105.247 1.00 30.59 ? 1059 GLY   A N     1 
ATOM   7563  C  CA    . GLY   A  1 1061 ? 26.249  62.027  104.668 1.00 30.98 ? 1059 GLY   A CA    1 
ATOM   7564  C  C     . GLY   A  1 1061 ? 26.951  63.164  105.383 1.00 33.22 ? 1059 GLY   A C     1 
ATOM   7565  O  O     . GLY   A  1 1061 ? 28.182  63.174  105.483 1.00 32.19 ? 1059 GLY   A O     1 
ATOM   7566  N  N     . LYS   A  1 1062 ? 26.190  64.127  105.897 1.00 30.81 ? 1060 LYS   A N     1 
ATOM   7567  C  CA    . LYS   A  1 1062 ? 26.771  65.270  106.593 1.00 32.29 ? 1060 LYS   A CA    1 
ATOM   7568  C  C     . LYS   A  1 1062 ? 27.079  64.986  108.055 1.00 33.62 ? 1060 LYS   A C     1 
ATOM   7569  O  O     . LYS   A  1 1062 ? 27.670  65.842  108.722 1.00 35.69 ? 1060 LYS   A O     1 
ATOM   7570  C  CB    . LYS   A  1 1062 ? 25.843  66.488  106.504 1.00 32.43 ? 1060 LYS   A CB    1 
ATOM   7571  C  CG    . LYS   A  1 1062 ? 25.730  67.121  105.118 1.00 33.35 ? 1060 LYS   A CG    1 
ATOM   7572  C  CD    . LYS   A  1 1062 ? 27.058  67.709  104.660 1.00 37.07 ? 1060 LYS   A CD    1 
ATOM   7573  C  CE    . LYS   A  1 1062 ? 26.899  68.478  103.359 1.00 40.62 ? 1060 LYS   A CE    1 
ATOM   7574  N  NZ    . LYS   A  1 1062 ? 28.187  69.020  102.837 1.00 41.04 ? 1060 LYS   A NZ    1 
ATOM   7575  N  N     . GLY   A  1 1063 ? 26.707  63.817  108.569 1.00 29.96 ? 1061 GLY   A N     1 
ATOM   7576  C  CA    . GLY   A  1 1063 ? 26.920  63.495  109.962 1.00 32.95 ? 1061 GLY   A CA    1 
ATOM   7577  C  C     . GLY   A  1 1063 ? 25.757  63.833  110.865 1.00 34.72 ? 1061 GLY   A C     1 
ATOM   7578  O  O     . GLY   A  1 1063 ? 25.825  63.556  112.076 1.00 33.37 ? 1061 GLY   A O     1 
ATOM   7579  N  N     . ALA   A  1 1064 ? 24.686  64.410  110.317 1.00 27.89 ? 1062 ALA   A N     1 
ATOM   7580  C  CA    . ALA   A  1 1064 ? 23.508  64.794  111.094 1.00 26.91 ? 1062 ALA   A CA    1 
ATOM   7581  C  C     . ALA   A  1 1064 ? 22.615  63.565  111.280 1.00 29.59 ? 1062 ALA   A C     1 
ATOM   7582  O  O     . ALA   A  1 1064 ? 21.531  63.427  110.703 1.00 24.66 ? 1062 ALA   A O     1 
ATOM   7583  C  CB    . ALA   A  1 1064 ? 22.777  65.939  110.410 1.00 25.33 ? 1062 ALA   A CB    1 
ATOM   7584  N  N     . ARG   A  1 1065 ? 23.101  62.653  112.115 1.00 27.04 ? 1063 ARG   A N     1 
ATOM   7585  C  CA    . ARG   A  1 1065 ? 22.480  61.339  112.213 1.00 27.19 ? 1063 ARG   A CA    1 
ATOM   7586  C  C     . ARG   A  1 1065 ? 21.106  61.413  112.867 1.00 25.81 ? 1063 ARG   A C     1 
ATOM   7587  O  O     . ARG   A  1 1065 ? 20.164  60.761  112.413 1.00 27.76 ? 1063 ARG   A O     1 
ATOM   7588  C  CB    . ARG   A  1 1065 ? 23.397  60.394  112.990 1.00 30.09 ? 1063 ARG   A CB    1 
ATOM   7589  C  CG    . ARG   A  1 1065 ? 24.825  60.397  112.486 1.00 35.83 ? 1063 ARG   A CG    1 
ATOM   7590  C  CD    . ARG   A  1 1065 ? 24.894  59.932  111.038 1.00 37.72 ? 1063 ARG   A CD    1 
ATOM   7591  N  NE    . ARG   A  1 1065 ? 26.274  59.848  110.570 1.00 42.97 ? 1063 ARG   A NE    1 
ATOM   7592  C  CZ    . ARG   A  1 1065 ? 26.651  59.193  109.481 1.00 42.25 ? 1063 ARG   A CZ    1 
ATOM   7593  N  NH1   . ARG   A  1 1065 ? 25.771  58.574  108.710 1.00 40.65 ? 1063 ARG   A NH1   1 
ATOM   7594  N  NH2   . ARG   A  1 1065 ? 27.943  59.151  109.163 1.00 38.92 ? 1063 ARG   A NH2   1 
ATOM   7595  N  N     . ALA   A  1 1066 ? 20.974  62.184  113.943 1.00 25.92 ? 1064 ALA   A N     1 
ATOM   7596  C  CA    . ALA   A  1 1066 ? 19.677  62.286  114.595 1.00 24.73 ? 1064 ALA   A CA    1 
ATOM   7597  C  C     . ALA   A  1 1066 ? 18.658  62.954  113.678 1.00 25.50 ? 1064 ALA   A C     1 
ATOM   7598  O  O     . ALA   A  1 1066 ? 17.486  62.562  113.648 1.00 23.94 ? 1064 ALA   A O     1 
ATOM   7599  C  CB    . ALA   A  1 1066 ? 19.801  63.061  115.903 1.00 24.66 ? 1064 ALA   A CB    1 
ATOM   7600  N  N     . GLU   A  1 1067 ? 19.092  63.971  112.934 1.00 23.77 ? 1065 GLU   A N     1 
ATOM   7601  C  CA    . GLU   A  1 1067 ? 18.189  64.661  112.022 1.00 23.87 ? 1065 GLU   A CA    1 
ATOM   7602  C  C     . GLU   A  1 1067 ? 17.760  63.744  110.882 1.00 22.62 ? 1065 GLU   A C     1 
ATOM   7603  O  O     . GLU   A  1 1067 ? 16.598  63.770  110.459 1.00 23.46 ? 1065 GLU   A O     1 
ATOM   7604  C  CB    . GLU   A  1 1067 ? 18.870  65.915  111.487 1.00 24.62 ? 1065 GLU   A CB    1 
ATOM   7605  C  CG    . GLU   A  1 1067 ? 19.044  67.018  112.523 1.00 23.10 ? 1065 GLU   A CG    1 
ATOM   7606  C  CD    . GLU   A  1 1067 ? 20.349  66.939  113.307 1.00 31.81 ? 1065 GLU   A CD    1 
ATOM   7607  O  OE1   . GLU   A  1 1067 ? 21.084  65.923  113.220 1.00 27.94 ? 1065 GLU   A OE1   1 
ATOM   7608  O  OE2   . GLU   A  1 1067 ? 20.644  67.924  114.022 1.00 36.70 ? 1065 GLU   A OE2   1 
ATOM   7609  N  N     . ALA   A  1 1068 ? 18.688  62.924  110.382 1.00 22.25 ? 1066 ALA   A N     1 
ATOM   7610  C  CA    . ALA   A  1 1068 ? 18.355  61.953  109.341 1.00 21.62 ? 1066 ALA   A CA    1 
ATOM   7611  C  C     . ALA   A  1 1068 ? 17.293  60.971  109.823 1.00 25.41 ? 1066 ALA   A C     1 
ATOM   7612  O  O     . ALA   A  1 1068 ? 16.344  60.655  109.094 1.00 24.10 ? 1066 ALA   A O     1 
ATOM   7613  C  CB    . ALA   A  1 1068 ? 19.621  61.202  108.902 1.00 24.32 ? 1066 ALA   A CB    1 
ATOM   7614  N  N     . GLU   A  1 1069 ? 17.448  60.464  111.049 1.00 23.23 ? 1067 GLU   A N     1 
ATOM   7615  C  CA    . GLU   A  1 1069 ? 16.431  59.590  111.626 1.00 24.50 ? 1067 GLU   A CA    1 
ATOM   7616  C  C     . GLU   A  1 1069 ? 15.089  60.302  111.733 1.00 25.11 ? 1067 GLU   A C     1 
ATOM   7617  O  O     . GLU   A  1 1069 ? 14.047  59.730  111.394 1.00 23.32 ? 1067 GLU   A O     1 
ATOM   7618  C  CB    . GLU   A  1 1069 ? 16.885  59.088  113.001 1.00 28.29 ? 1067 GLU   A CB    1 
ATOM   7619  C  CG    . GLU   A  1 1069 ? 15.823  58.284  113.748 1.00 32.58 ? 1067 GLU   A CG    1 
ATOM   7620  C  CD    . GLU   A  1 1069 ? 15.634  56.885  113.185 1.00 41.70 ? 1067 GLU   A CD    1 
ATOM   7621  O  OE1   . GLU   A  1 1069 ? 16.482  56.437  112.374 1.00 46.80 ? 1067 GLU   A OE1   1 
ATOM   7622  O  OE2   . GLU   A  1 1069 ? 14.636  56.228  113.558 1.00 45.80 ? 1067 GLU   A OE2   1 
ATOM   7623  N  N     . ALA   A  1 1070 ? 15.096  61.554  112.203 1.00 23.93 ? 1068 ALA   A N     1 
ATOM   7624  C  CA    . ALA   A  1 1070 ? 13.865  62.328  112.288 1.00 23.04 ? 1068 ALA   A CA    1 
ATOM   7625  C  C     . ALA   A  1 1070 ? 13.268  62.564  110.909 1.00 23.04 ? 1068 ALA   A C     1 
ATOM   7626  O  O     . ALA   A  1 1070 ? 12.042  62.583  110.750 1.00 23.53 ? 1068 ALA   A O     1 
ATOM   7627  C  CB    . ALA   A  1 1070 ? 14.131  63.666  112.975 1.00 26.69 ? 1068 ALA   A CB    1 
ATOM   7628  N  N     . ALA   A  1 1071 ? 14.121  62.778  109.908 1.00 21.43 ? 1069 ALA   A N     1 
ATOM   7629  C  CA    . ALA   A  1 1071 ? 13.638  62.934  108.542 1.00 20.37 ? 1069 ALA   A CA    1 
ATOM   7630  C  C     . ALA   A  1 1071 ? 12.940  61.662  108.069 1.00 23.46 ? 1069 ALA   A C     1 
ATOM   7631  O  O     . ALA   A  1 1071 ? 11.813  61.707  107.568 1.00 19.63 ? 1069 ALA   A O     1 
ATOM   7632  C  CB    . ALA   A  1 1071 ? 14.800  63.308  107.619 1.00 20.13 ? 1069 ALA   A CB    1 
ATOM   7633  N  N     . ARG   A  1 1072 ? 13.578  60.506  108.266 1.00 23.05 ? 1070 ARG   A N     1 
ATOM   7634  C  CA    . ARG   A  1 1072 ? 12.942  59.245  107.891 1.00 21.12 ? 1070 ARG   A CA    1 
ATOM   7635  C  C     . ARG   A  1 1072 ? 11.637  59.036  108.646 1.00 19.99 ? 1070 ARG   A C     1 
ATOM   7636  O  O     . ARG   A  1 1072 ? 10.641  58.595  108.065 1.00 23.20 ? 1070 ARG   A O     1 
ATOM   7637  C  CB    . ARG   A  1 1072 ? 13.911  58.081  108.134 1.00 20.00 ? 1070 ARG   A CB    1 
ATOM   7638  C  CG    . ARG   A  1 1072 ? 15.052  58.051  107.126 1.00 25.03 ? 1070 ARG   A CG    1 
ATOM   7639  C  CD    . ARG   A  1 1072 ? 15.878  56.784  107.251 1.00 29.56 ? 1070 ARG   A CD    1 
ATOM   7640  N  NE    . ARG   A  1 1072 ? 16.575  56.734  108.529 1.00 30.57 ? 1070 ARG   A NE    1 
ATOM   7641  C  CZ    . ARG   A  1 1072 ? 17.781  57.240  108.751 1.00 30.93 ? 1070 ARG   A CZ    1 
ATOM   7642  N  NH1   . ARG   A  1 1072 ? 18.479  57.825  107.785 1.00 32.31 ? 1070 ARG   A NH1   1 
ATOM   7643  N  NH2   . ARG   A  1 1072 ? 18.305  57.155  109.971 1.00 32.82 ? 1070 ARG   A NH2   1 
ATOM   7644  N  N     . ASN   A  1 1073 ? 11.619  59.361  109.938 1.00 20.42 ? 1071 ASN   A N     1 
ATOM   7645  C  CA    . ASN   A  1 1073 ? 10.384  59.255  110.703 1.00 21.97 ? 1071 ASN   A CA    1 
ATOM   7646  C  C     . ASN   A  1 1073 ? 9.304   60.167  110.140 1.00 24.54 ? 1071 ASN   A C     1 
ATOM   7647  O  O     . ASN   A  1 1073 ? 8.138   59.770  110.044 1.00 22.44 ? 1071 ASN   A O     1 
ATOM   7648  C  CB    . ASN   A  1 1073 ? 10.644  59.577  112.172 1.00 25.98 ? 1071 ASN   A CB    1 
ATOM   7649  C  CG    . ASN   A  1 1073 ? 11.389  58.471  112.877 1.00 31.98 ? 1071 ASN   A CG    1 
ATOM   7650  O  OD1   . ASN   A  1 1073 ? 11.340  57.317  112.458 1.00 36.23 ? 1071 ASN   A OD1   1 
ATOM   7651  N  ND2   . ASN   A  1 1073 ? 12.082  58.814  113.949 1.00 35.81 ? 1071 ASN   A ND2   1 
ATOM   7652  N  N     . ALA   A  1 1074 ? 9.669   61.396  109.766 1.00 19.43 ? 1072 ALA   A N     1 
ATOM   7653  C  CA    . ALA   A  1 1074 ? 8.686   62.293  109.164 1.00 18.78 ? 1072 ALA   A CA    1 
ATOM   7654  C  C     . ALA   A  1 1074 ? 8.159   61.722  107.860 1.00 18.75 ? 1072 ALA   A C     1 
ATOM   7655  O  O     . ALA   A  1 1074 ? 6.966   61.832  107.566 1.00 19.85 ? 1072 ALA   A O     1 
ATOM   7656  C  CB    . ALA   A  1 1074 ? 9.301   63.672  108.927 1.00 22.19 ? 1072 ALA   A CB    1 
ATOM   7657  N  N     . GLY   A  1 1075 ? 9.038   61.102  107.067 1.00 19.86 ? 1073 GLY   A N     1 
ATOM   7658  C  CA    . GLY   A  1 1075 ? 8.599   60.505  105.812 1.00 21.32 ? 1073 GLY   A CA    1 
ATOM   7659  C  C     . GLY   A  1 1075 ? 7.551   59.430  106.022 1.00 21.75 ? 1073 GLY   A C     1 
ATOM   7660  O  O     . GLY   A  1 1075 ? 6.582   59.331  105.262 1.00 20.11 ? 1073 GLY   A O     1 
ATOM   7661  N  N     . SER   A  1 1076 ? 7.717   58.632  107.078 1.00 20.30 ? 1074 SER   A N     1 
ATOM   7662  C  CA    . SER   A  1 1076 ? 6.755   57.580  107.389 1.00 24.13 ? 1074 SER   A CA    1 
ATOM   7663  C  C     . SER   A  1 1076 ? 5.474   58.137  107.987 1.00 22.33 ? 1074 SER   A C     1 
ATOM   7664  O  O     . SER   A  1 1076 ? 4.379   57.650  107.672 1.00 24.22 ? 1074 SER   A O     1 
ATOM   7665  C  CB    . SER   A  1 1076 ? 7.369   56.568  108.354 1.00 23.95 ? 1074 SER   A CB    1 
ATOM   7666  O  OG    . SER   A  1 1076 ? 8.272   55.730  107.666 1.00 29.95 ? 1074 SER   A OG    1 
ATOM   7667  N  N     . SER   A  1 1077 ? 5.595   59.122  108.882 1.00 20.53 ? 1075 SER   A N     1 
ATOM   7668  C  CA    . SER   A  1 1077 ? 4.417   59.668  109.550 1.00 23.44 ? 1075 SER   A CA    1 
ATOM   7669  C  C     . SER   A  1 1077 ? 3.570   60.516  108.609 1.00 24.16 ? 1075 SER   A C     1 
ATOM   7670  O  O     . SER   A  1 1077 ? 2.358   60.657  108.817 1.00 21.83 ? 1075 SER   A O     1 
ATOM   7671  C  CB    . SER   A  1 1077 ? 4.837   60.489  110.769 1.00 25.46 ? 1075 SER   A CB    1 
ATOM   7672  O  OG    . SER   A  1 1077 ? 5.485   59.656  111.718 1.00 34.09 ? 1075 SER   A OG    1 
ATOM   7673  N  N     . SER   A  1 1078 ? 4.179   61.086  107.578 1.00 17.95 ? 1076 SER   A N     1 
ATOM   7674  C  CA    . SER   A  1 1078 ? 3.410   61.881  106.627 1.00 18.27 ? 1076 SER   A CA    1 
ATOM   7675  C  C     . SER   A  1 1078 ? 2.263   61.067  106.056 1.00 19.39 ? 1076 SER   A C     1 
ATOM   7676  O  O     . SER   A  1 1078 ? 2.412   59.883  105.758 1.00 19.41 ? 1076 SER   A O     1 
ATOM   7677  C  CB    . SER   A  1 1078 ? 4.299   62.344  105.480 1.00 19.12 ? 1076 SER   A CB    1 
ATOM   7678  O  OG    . SER   A  1 1078 ? 3.530   63.045  104.513 1.00 18.02 ? 1076 SER   A OG    1 
ATOM   7679  N  N     . ALA   A  1 1079 ? 1.112   61.711  105.893 1.00 17.32 ? 1077 ALA   A N     1 
ATOM   7680  C  CA    . ALA   A  1 1079 ? -0.005  61.089  105.209 1.00 17.52 ? 1077 ALA   A CA    1 
ATOM   7681  C  C     . ALA   A  1 1079 ? -0.136  61.590  103.782 1.00 18.57 ? 1077 ALA   A C     1 
ATOM   7682  O  O     . ALA   A  1 1079 ? -1.154  61.327  103.130 1.00 16.82 ? 1077 ALA   A O     1 
ATOM   7683  C  CB    . ALA   A  1 1079 ? -1.305  61.316  105.986 1.00 19.62 ? 1077 ALA   A CB    1 
ATOM   7684  N  N     . LEU   A  1 1080 ? 0.874   62.300  103.286 1.00 18.77 ? 1078 LEU   A N     1 
ATOM   7685  C  CA    . LEU   A  1 1080 ? 0.899   62.696  101.886 1.00 16.96 ? 1078 LEU   A CA    1 
ATOM   7686  C  C     . LEU   A  1 1080 ? 0.666   61.481  101.005 1.00 18.11 ? 1078 LEU   A C     1 
ATOM   7687  O  O     . LEU   A  1 1080 ? 1.318   60.446  101.168 1.00 18.31 ? 1078 LEU   A O     1 
ATOM   7688  C  CB    . LEU   A  1 1080 ? 2.248   63.337  101.543 1.00 17.18 ? 1078 LEU   A CB    1 
ATOM   7689  C  CG    . LEU   A  1 1080 ? 2.483   63.576  100.048 1.00 17.10 ? 1078 LEU   A CG    1 
ATOM   7690  C  CD1   . LEU   A  1 1080 ? 1.663   64.793  99.564  1.00 16.92 ? 1078 LEU   A CD1   1 
ATOM   7691  C  CD2   . LEU   A  1 1080 ? 3.986   63.745  99.769  1.00 18.60 ? 1078 LEU   A CD2   1 
ATOM   7692  N  N     . GLY   A  1 1081 ? -0.271  61.603  100.070 1.00 16.76 ? 1079 GLY   A N     1 
ATOM   7693  C  CA    . GLY   A  1 1081 ? -0.586  60.507  99.184  1.00 20.20 ? 1079 GLY   A CA    1 
ATOM   7694  C  C     . GLY   A  1 1081 ? -1.795  59.706  99.610  1.00 21.29 ? 1079 GLY   A C     1 
ATOM   7695  O  O     . GLY   A  1 1081 ? -2.210  58.797  98.876  1.00 18.43 ? 1079 GLY   A O     1 
ATOM   7696  N  N     . LEU   A  1 1082 ? -2.346  59.996  100.783 1.00 16.62 ? 1080 LEU   A N     1 
ATOM   7697  C  CA    A LEU   A  1 1082 ? -3.609  59.395  101.180 0.48 17.28 ? 1080 LEU   A CA    1 
ATOM   7698  C  CA    B LEU   A  1 1082 ? -3.608  59.388  101.178 0.52 17.44 ? 1080 LEU   A CA    1 
ATOM   7699  C  C     . LEU   A  1 1082 ? -4.632  59.568  100.066 1.00 17.66 ? 1080 LEU   A C     1 
ATOM   7700  O  O     . LEU   A  1 1082 ? -4.757  60.644  99.483  1.00 16.85 ? 1080 LEU   A O     1 
ATOM   7701  C  CB    A LEU   A  1 1082 ? -4.110  60.046  102.470 0.48 16.50 ? 1080 LEU   A CB    1 
ATOM   7702  C  CB    B LEU   A  1 1082 ? -4.112  60.014  102.482 0.52 16.50 ? 1080 LEU   A CB    1 
ATOM   7703  C  CG    A LEU   A  1 1082 ? -5.452  59.566  103.012 0.48 17.36 ? 1080 LEU   A CG    1 
ATOM   7704  C  CG    B LEU   A  1 1082 ? -5.455  59.539  103.042 0.52 17.29 ? 1080 LEU   A CG    1 
ATOM   7705  C  CD1   A LEU   A  1 1082 ? -5.400  58.087  103.287 0.48 18.91 ? 1080 LEU   A CD1   1 
ATOM   7706  C  CD1   B LEU   A  1 1082 ? -5.464  59.668  104.563 0.52 17.31 ? 1080 LEU   A CD1   1 
ATOM   7707  C  CD2   A LEU   A  1 1082 ? -5.808  60.339  104.282 0.48 16.85 ? 1080 LEU   A CD2   1 
ATOM   7708  C  CD2   B LEU   A  1 1082 ? -6.608  60.344  102.455 0.52 16.43 ? 1080 LEU   A CD2   1 
ATOM   7709  N  N     . ASP   A  1 1083 ? -5.365  58.499  99.769  1.00 18.04 ? 1081 ASP   A N     1 
ATOM   7710  C  CA    . ASP   A  1 1083 ? -6.299  58.529  98.642  1.00 21.57 ? 1081 ASP   A CA    1 
ATOM   7711  C  C     . ASP   A  1 1083 ? -7.480  57.633  98.999  1.00 20.49 ? 1081 ASP   A C     1 
ATOM   7712  O  O     . ASP   A  1 1083 ? -7.399  56.409  98.869  1.00 23.53 ? 1081 ASP   A O     1 
ATOM   7713  C  CB    . ASP   A  1 1083 ? -5.606  58.069  97.367  1.00 21.93 ? 1081 ASP   A CB    1 
ATOM   7714  C  CG    . ASP   A  1 1083 ? -6.479  58.201  96.135  1.00 28.27 ? 1081 ASP   A CG    1 
ATOM   7715  O  OD1   . ASP   A  1 1083 ? -7.540  58.844  96.203  1.00 30.50 ? 1081 ASP   A OD1   1 
ATOM   7716  O  OD2   . ASP   A  1 1083 ? -6.089  57.655  95.083  1.00 35.77 ? 1081 ASP   A OD2   1 
ATOM   7717  N  N     . LEU   A  1 1084 ? -8.569  58.246  99.433  1.00 18.83 ? 1082 LEU   A N     1 
ATOM   7718  C  CA    . LEU   A  1 1084 ? -9.698  57.510  99.976  1.00 18.56 ? 1082 LEU   A CA    1 
ATOM   7719  C  C     . LEU   A  1 1084 ? -10.951 57.801  99.175  1.00 19.22 ? 1082 LEU   A C     1 
ATOM   7720  O  O     . LEU   A  1 1084 ? -11.121 58.893  98.628  1.00 20.45 ? 1082 LEU   A O     1 
ATOM   7721  C  CB    . LEU   A  1 1084 ? -9.956  57.885  101.443 1.00 20.01 ? 1082 LEU   A CB    1 
ATOM   7722  C  CG    . LEU   A  1 1084 ? -8.835  57.519  102.404 1.00 22.74 ? 1082 LEU   A CG    1 
ATOM   7723  C  CD1   . LEU   A  1 1084 ? -9.230  57.926  103.807 1.00 25.69 ? 1082 LEU   A CD1   1 
ATOM   7724  C  CD2   . LEU   A  1 1084 ? -8.519  56.033  102.309 1.00 25.96 ? 1082 LEU   A CD2   1 
ATOM   7725  N  N     . GLU   A  1 1085 ? -11.832 56.816  99.108  1.00 21.03 ? 1083 GLU   A N     1 
ATOM   7726  C  CA    . GLU   A  1 1085 ? -13.184 57.060  98.637  1.00 21.31 ? 1083 GLU   A CA    1 
ATOM   7727  C  C     . GLU   A  1 1085 ? -14.106 57.093  99.845  1.00 20.38 ? 1083 GLU   A C     1 
ATOM   7728  O  O     . GLU   A  1 1085 ? -14.044 56.208  100.703 1.00 24.00 ? 1083 GLU   A O     1 
ATOM   7729  C  CB    . GLU   A  1 1085 ? -13.643 56.007  97.630  1.00 23.23 ? 1083 GLU   A CB    1 
ATOM   7730  C  CG    . GLU   A  1 1085 ? -15.056 56.292  97.165  1.00 23.51 ? 1083 GLU   A CG    1 
ATOM   7731  C  CD    . GLU   A  1 1085 ? -15.490 55.460  95.990  1.00 26.62 ? 1083 GLU   A CD    1 
ATOM   7732  O  OE1   . GLU   A  1 1085 ? -14.647 54.742  95.412  1.00 32.12 ? 1083 GLU   A OE1   1 
ATOM   7733  O  OE2   . GLU   A  1 1085 ? -16.683 55.544  95.644  1.00 30.37 ? 1083 GLU   A OE2   1 
ATOM   7734  N  N     . LEU   A  1 1086 ? -14.923 58.131  99.930  1.00 18.70 ? 1084 LEU   A N     1 
ATOM   7735  C  CA    . LEU   A  1 1086 ? -15.815 58.306  101.062 1.00 19.43 ? 1084 LEU   A CA    1 
ATOM   7736  C  C     . LEU   A  1 1086 ? -17.206 57.792  100.711 1.00 22.95 ? 1084 LEU   A C     1 
ATOM   7737  O  O     . LEU   A  1 1086 ? -17.670 57.985  99.579  1.00 20.38 ? 1084 LEU   A O     1 
ATOM   7738  C  CB    . LEU   A  1 1086 ? -15.894 59.782  101.459 1.00 18.68 ? 1084 LEU   A CB    1 
ATOM   7739  C  CG    . LEU   A  1 1086 ? -14.538 60.417  101.785 1.00 19.00 ? 1084 LEU   A CG    1 
ATOM   7740  C  CD1   . LEU   A  1 1086 ? -14.681 61.897  102.172 1.00 19.10 ? 1084 LEU   A CD1   1 
ATOM   7741  C  CD2   . LEU   A  1 1086 ? -13.826 59.624  102.907 1.00 21.77 ? 1084 LEU   A CD2   1 
ATOM   7742  N  N     . PRO   A  1 1087 ? -17.859 57.113  101.651 1.00 22.45 ? 1085 PRO   A N     1 
ATOM   7743  C  CA    . PRO   A  1 1087 ? -19.211 56.600  101.390 1.00 21.82 ? 1085 PRO   A CA    1 
ATOM   7744  C  C     . PRO   A  1 1087 ? -20.180 57.738  101.129 1.00 23.72 ? 1085 PRO   A C     1 
ATOM   7745  O  O     . PRO   A  1 1087 ? -20.205 58.734  101.851 1.00 23.68 ? 1085 PRO   A O     1 
ATOM   7746  C  CB    . PRO   A  1 1087 ? -19.568 55.852  102.680 1.00 26.39 ? 1085 PRO   A CB    1 
ATOM   7747  C  CG    . PRO   A  1 1087 ? -18.272 55.583  103.353 1.00 28.90 ? 1085 PRO   A CG    1 
ATOM   7748  C  CD    . PRO   A  1 1087 ? -17.347 56.695  102.967 1.00 24.68 ? 1085 PRO   A CD    1 
ATOM   7749  N  N     . GLY   A  1 1088 ? -20.986 57.579  100.088 1.00 22.24 ? 1086 GLY   A N     1 
ATOM   7750  C  CA    . GLY   A  1 1088 ? -22.009 58.545  99.763  1.00 23.94 ? 1086 GLY   A CA    1 
ATOM   7751  C  C     . GLY   A  1 1088 ? -23.110 57.886  98.956  1.00 18.49 ? 1086 GLY   A C     1 
ATOM   7752  O  O     . GLY   A  1 1088 ? -23.300 56.671  99.011  1.00 19.10 ? 1086 GLY   A O     1 
ATOM   7753  N  N     . PRO   A  1 1089 ? -23.835 58.668  98.169  1.00 22.71 ? 1087 PRO   A N     1 
ATOM   7754  C  CA    . PRO   A  1 1089 ? -24.925 58.099  97.376  1.00 18.62 ? 1087 PRO   A CA    1 
ATOM   7755  C  C     . PRO   A  1 1089 ? -24.404 57.269  96.215  1.00 24.35 ? 1087 PRO   A C     1 
ATOM   7756  O  O     . PRO   A  1 1089 ? -23.265 57.412  95.756  1.00 21.50 ? 1087 PRO   A O     1 
ATOM   7757  C  CB    . PRO   A  1 1089 ? -25.667 59.334  96.858  1.00 20.15 ? 1087 PRO   A CB    1 
ATOM   7758  C  CG    . PRO   A  1 1089 ? -24.546 60.345  96.701  1.00 22.00 ? 1087 PRO   A CG    1 
ATOM   7759  C  CD    . PRO   A  1 1089 ? -23.593 60.085  97.842  1.00 23.95 ? 1087 PRO   A CD    1 
ATOM   7760  N  N     . VAL   A  1 1090 ? -25.282 56.395  95.721  1.00 19.17 ? 1088 VAL   A N     1 
ATOM   7761  C  CA    . VAL   A  1 1090 ? -25.002 55.752  94.450  1.00 18.36 ? 1088 VAL   A CA    1 
ATOM   7762  C  C     . VAL   A  1 1090 ? -24.897 56.827  93.371  1.00 17.92 ? 1088 VAL   A C     1 
ATOM   7763  O  O     . VAL   A  1 1090 ? -25.391 57.951  93.521  1.00 18.70 ? 1088 VAL   A O     1 
ATOM   7764  C  CB    . VAL   A  1 1090 ? -26.082 54.723  94.085  1.00 22.04 ? 1088 VAL   A CB    1 
ATOM   7765  C  CG1   . VAL   A  1 1090 ? -26.189 53.622  95.156  1.00 23.70 ? 1088 VAL   A CG1   1 
ATOM   7766  C  CG2   . VAL   A  1 1090 ? -27.437 55.429  93.866  1.00 20.65 ? 1088 VAL   A CG2   1 
ATOM   7767  N  N     . GLY   A  1 1091 ? -24.233 56.477  92.275  1.00 17.27 ? 1089 GLY   A N     1 
ATOM   7768  C  CA    . GLY   A  1 1091 ? -24.150 57.390  91.146  1.00 20.92 ? 1089 GLY   A CA    1 
ATOM   7769  C  C     . GLY   A  1 1091 ? -23.199 58.544  91.349  1.00 19.58 ? 1089 GLY   A C     1 
ATOM   7770  O  O     . GLY   A  1 1091 ? -23.243 59.526  90.603  1.00 18.20 ? 1089 GLY   A O     1 
ATOM   7771  N  N     . GLU   A  1 1092 ? -22.330 58.448  92.347  1.00 17.91 ? 1090 GLU   A N     1 
ATOM   7772  C  CA    . GLU   A  1 1092 ? -21.369 59.494  92.636  1.00 18.01 ? 1090 GLU   A CA    1 
ATOM   7773  C  C     . GLU   A  1 1092 ? -20.143 58.833  93.239  1.00 19.10 ? 1090 GLU   A C     1 
ATOM   7774  O  O     . GLU   A  1 1092 ? -20.262 57.851  93.972  1.00 18.89 ? 1090 GLU   A O     1 
ATOM   7775  C  CB    . GLU   A  1 1092 ? -21.976 60.512  93.601  1.00 20.43 ? 1090 GLU   A CB    1 
ATOM   7776  C  CG    . GLU   A  1 1092 ? -21.305 61.858  93.639  1.00 25.27 ? 1090 GLU   A CG    1 
ATOM   7777  C  CD    . GLU   A  1 1092 ? -22.095 62.802  94.520  1.00 25.05 ? 1090 GLU   A CD    1 
ATOM   7778  O  OE1   . GLU   A  1 1092 ? -22.012 62.640  95.757  1.00 21.16 ? 1090 GLU   A OE1   1 
ATOM   7779  O  OE2   . GLU   A  1 1092 ? -22.841 63.651  93.969  1.00 24.78 ? 1090 GLU   A OE2   1 
ATOM   7780  N  N     . ARG   A  1 1093 ? -18.968 59.359  92.923  1.00 16.20 ? 1091 ARG   A N     1 
ATOM   7781  C  CA    . ARG   A  1 1093 ? -17.730 58.883  93.526  1.00 16.04 ? 1091 ARG   A CA    1 
ATOM   7782  C  C     . ARG   A  1 1093 ? -17.115 60.062  94.258  1.00 17.33 ? 1091 ARG   A C     1 
ATOM   7783  O  O     . ARG   A  1 1093 ? -16.882 61.114  93.658  1.00 17.52 ? 1091 ARG   A O     1 
ATOM   7784  C  CB    . ARG   A  1 1093 ? -16.772 58.312  92.469  1.00 18.70 ? 1091 ARG   A CB    1 
ATOM   7785  N  N     . ASN   A  1 1094 ? -16.891 59.904  95.557  1.00 16.97 ? 1092 ASN   A N     1 
ATOM   7786  C  CA    . ASN   A  1 1094 ? -16.433 61.004  96.386  1.00 17.60 ? 1092 ASN   A CA    1 
ATOM   7787  C  C     . ASN   A  1 1094 ? -15.070 60.649  96.941  1.00 16.62 ? 1092 ASN   A C     1 
ATOM   7788  O  O     . ASN   A  1 1094 ? -14.937 59.685  97.696  1.00 18.71 ? 1092 ASN   A O     1 
ATOM   7789  C  CB    . ASN   A  1 1094 ? -17.448 61.297  97.482  1.00 15.16 ? 1092 ASN   A CB    1 
ATOM   7790  C  CG    . ASN   A  1 1094 ? -18.682 61.928  96.910  1.00 19.96 ? 1092 ASN   A CG    1 
ATOM   7791  O  OD1   . ASN   A  1 1094 ? -18.620 63.059  96.424  1.00 17.50 ? 1092 ASN   A OD1   1 
ATOM   7792  N  ND2   . ASN   A  1 1094 ? -19.796 61.196  96.906  1.00 19.23 ? 1092 ASN   A ND2   1 
ATOM   7793  N  N     . LEU   A  1 1095 ? -14.062 61.411  96.532  1.00 17.21 ? 1093 LEU   A N     1 
ATOM   7794  C  CA    . LEU   A  1 1095 ? -12.675 61.087  96.788  1.00 18.26 ? 1093 LEU   A CA    1 
ATOM   7795  C  C     . LEU   A  1 1095 ? -12.078 62.139  97.693  1.00 18.24 ? 1093 LEU   A C     1 
ATOM   7796  O  O     . LEU   A  1 1095 ? -12.424 63.320  97.622  1.00 17.88 ? 1093 LEU   A O     1 
ATOM   7797  C  CB    . LEU   A  1 1095 ? -11.860 61.026  95.500  1.00 16.17 ? 1093 LEU   A CB    1 
ATOM   7798  C  CG    . LEU   A  1 1095 ? -12.504 60.098  94.466  1.00 22.54 ? 1093 LEU   A CG    1 
ATOM   7799  C  CD1   . LEU   A  1 1095 ? -11.621 60.042  93.223  1.00 26.11 ? 1093 LEU   A CD1   1 
ATOM   7800  C  CD2   . LEU   A  1 1095 ? -12.732 58.716  95.078  1.00 23.31 ? 1093 LEU   A CD2   1 
ATOM   7801  N  N     . TYR   A  1 1096 ? -11.147 61.699  98.524  1.00 17.49 ? 1094 TYR   A N     1 
ATOM   7802  C  CA    . TYR   A  1 1096 ? -10.532 62.579  99.501  1.00 15.84 ? 1094 TYR   A CA    1 
ATOM   7803  C  C     . TYR   A  1 1096 ? -9.056  62.257  99.475  1.00 17.55 ? 1094 TYR   A C     1 
ATOM   7804  O  O     . TYR   A  1 1096 ? -8.684  61.101  99.677  1.00 17.12 ? 1094 TYR   A O     1 
ATOM   7805  C  CB    . TYR   A  1 1096 ? -11.124 62.336  100.890 1.00 18.96 ? 1094 TYR   A CB    1 
ATOM   7806  C  CG    . TYR   A  1 1096 ? -10.415 63.026  102.021 1.00 16.56 ? 1094 TYR   A CG    1 
ATOM   7807  C  CD1   . TYR   A  1 1096 ? -10.739 64.323  102.379 1.00 15.63 ? 1094 TYR   A CD1   1 
ATOM   7808  C  CD2   . TYR   A  1 1096 ? -9.447  62.358  102.775 1.00 16.75 ? 1094 TYR   A CD2   1 
ATOM   7809  C  CE1   . TYR   A  1 1096 ? -10.098 64.951  103.431 1.00 18.48 ? 1094 TYR   A CE1   1 
ATOM   7810  C  CE2   . TYR   A  1 1096 ? -8.807  62.984  103.827 1.00 19.43 ? 1094 TYR   A CE2   1 
ATOM   7811  C  CZ    . TYR   A  1 1096 ? -9.136  64.274  104.149 1.00 18.36 ? 1094 TYR   A CZ    1 
ATOM   7812  O  OH    . TYR   A  1 1096 ? -8.512  64.907  105.196 1.00 18.60 ? 1094 TYR   A OH    1 
ATOM   7813  N  N     . THR   A  1 1097 ? -8.226  63.255  99.199  1.00 17.27 ? 1095 THR   A N     1 
ATOM   7814  C  CA    . THR   A  1 1097 ? -6.811  62.993  98.989  1.00 17.41 ? 1095 THR   A CA    1 
ATOM   7815  C  C     . THR   A  1 1097 ? -5.990  64.044  99.716  1.00 16.54 ? 1095 THR   A C     1 
ATOM   7816  O  O     . THR   A  1 1097 ? -6.434  65.178  99.903  1.00 17.02 ? 1095 THR   A O     1 
ATOM   7817  C  CB    . THR   A  1 1097 ? -6.455  63.004  97.500  1.00 20.09 ? 1095 THR   A CB    1 
ATOM   7818  O  OG1   . THR   A  1 1097 ? -6.868  64.252  96.928  1.00 23.15 ? 1095 THR   A OG1   1 
ATOM   7819  C  CG2   . THR   A  1 1097 ? -7.182  61.881  96.767  1.00 21.36 ? 1095 THR   A CG2   1 
ATOM   7820  N  N     . LEU   A  1 1098 ? -4.782  63.661  100.112 1.00 16.38 ? 1096 LEU   A N     1 
ATOM   7821  C  CA    . LEU   A  1 1098 ? -3.865  64.585  100.770 1.00 16.61 ? 1096 LEU   A CA    1 
ATOM   7822  C  C     . LEU   A  1 1098 ? -2.704  64.859  99.835  1.00 16.30 ? 1096 LEU   A C     1 
ATOM   7823  O  O     . LEU   A  1 1098 ? -2.001  63.931  99.423  1.00 17.10 ? 1096 LEU   A O     1 
ATOM   7824  C  CB    . LEU   A  1 1098 ? -3.359  64.033  102.097 1.00 16.35 ? 1096 LEU   A CB    1 
ATOM   7825  C  CG    . LEU   A  1 1098 ? -4.438  63.862  103.164 1.00 16.30 ? 1096 LEU   A CG    1 
ATOM   7826  C  CD1   . LEU   A  1 1098 ? -3.796  63.318  104.456 1.00 16.50 ? 1096 LEU   A CD1   1 
ATOM   7827  C  CD2   . LEU   A  1 1098 ? -5.217  65.165  103.429 1.00 16.20 ? 1096 LEU   A CD2   1 
ATOM   7828  N  N     . HIS   A  1 1099 ? -2.509  66.128  99.517  1.00 18.31 ? 1097 HIS   A N     1 
ATOM   7829  C  CA    . HIS   A  1 1099 ? -1.472  66.585  98.615  1.00 17.86 ? 1097 HIS   A CA    1 
ATOM   7830  C  C     . HIS   A  1 1099 ? -0.519  67.503  99.357  1.00 16.96 ? 1097 HIS   A C     1 
ATOM   7831  O  O     . HIS   A  1 1099 ? -0.757  67.896  100.502 1.00 18.95 ? 1097 HIS   A O     1 
ATOM   7832  C  CB    . HIS   A  1 1099 ? -2.079  67.344  97.428  1.00 18.70 ? 1097 HIS   A CB    1 
ATOM   7833  C  CG    . HIS   A  1 1099 ? -3.078  66.550  96.650  1.00 22.52 ? 1097 HIS   A CG    1 
ATOM   7834  N  ND1   . HIS   A  1 1099 ? -2.788  65.988  95.426  1.00 24.21 ? 1097 HIS   A ND1   1 
ATOM   7835  C  CD2   . HIS   A  1 1099 ? -4.363  66.213  96.925  1.00 21.82 ? 1097 HIS   A CD2   1 
ATOM   7836  C  CE1   . HIS   A  1 1099 ? -3.854  65.352  94.970  1.00 24.40 ? 1097 HIS   A CE1   1 
ATOM   7837  N  NE2   . HIS   A  1 1099 ? -4.822  65.469  95.863  1.00 24.13 ? 1097 HIS   A NE2   1 
ATOM   7838  N  N     . ALA   A  1 1100 ? 0.561   67.862  98.674  1.00 16.72 ? 1098 ALA   A N     1 
ATOM   7839  C  CA    . ALA   A  1 1100 ? 1.426   68.915  99.186  1.00 19.45 ? 1098 ALA   A CA    1 
ATOM   7840  C  C     . ALA   A  1 1100 ? 0.666   70.237  99.231  1.00 21.60 ? 1098 ALA   A C     1 
ATOM   7841  O  O     . ALA   A  1 1100 ? -0.237  70.483  98.432  1.00 20.30 ? 1098 ALA   A O     1 
ATOM   7842  C  CB    . ALA   A  1 1100 ? 2.667   69.046  98.305  1.00 18.75 ? 1098 ALA   A CB    1 
ATOM   7843  N  N     . ARG   A  1 1101 ? 1.031   71.091  100.190 1.00 20.79 ? 1099 ARG   A N     1 
ATOM   7844  C  CA    . ARG   A  1 1101 ? 0.407   72.404  100.277 1.00 20.32 ? 1099 ARG   A CA    1 
ATOM   7845  C  C     . ARG   A  1 1101 ? 0.962   73.358  99.231  1.00 23.96 ? 1099 ARG   A C     1 
ATOM   7846  O  O     . ARG   A  1 1101 ? 0.213   74.148  98.650  1.00 21.78 ? 1099 ARG   A O     1 
ATOM   7847  C  CB    . ARG   A  1 1101 ? 0.606   72.989  101.675 1.00 23.36 ? 1099 ARG   A CB    1 
ATOM   7848  C  CG    . ARG   A  1 1101 ? -0.279  72.389  102.717 1.00 24.00 ? 1099 ARG   A CG    1 
ATOM   7849  C  CD    . ARG   A  1 1101 ? -0.117  73.108  104.036 1.00 27.97 ? 1099 ARG   A CD    1 
ATOM   7850  N  NE    . ARG   A  1 1101 ? -1.018  74.245  104.220 1.00 27.85 ? 1099 ARG   A NE    1 
ATOM   7851  C  CZ    . ARG   A  1 1101 ? -2.238  74.158  104.739 1.00 31.95 ? 1099 ARG   A CZ    1 
ATOM   7852  N  NH1   . ARG   A  1 1101 ? -2.797  72.987  105.002 1.00 27.95 ? 1099 ARG   A NH1   1 
ATOM   7853  N  NH2   . ARG   A  1 1101 ? -2.907  75.276  105.018 1.00 26.18 ? 1099 ARG   A NH2   1 
ATOM   7854  N  N     . GLY   A  1 1102 ? 2.265   73.307  98.991  1.00 19.25 ? 1100 GLY   A N     1 
ATOM   7855  C  CA    . GLY   A  1 1102 ? 2.915   74.240  98.098  1.00 19.11 ? 1100 GLY   A CA    1 
ATOM   7856  C  C     . GLY   A  1 1102 ? 4.306   74.562  98.599  1.00 24.04 ? 1100 GLY   A C     1 
ATOM   7857  O  O     . GLY   A  1 1102 ? 5.106   73.651  98.854  1.00 21.11 ? 1100 GLY   A O     1 
ATOM   7858  N  N     . ARG   A  1 1103 ? 4.611   75.848  98.756  1.00 18.82 ? 1101 ARG   A N     1 
ATOM   7859  C  CA    . ARG   A  1 1103 ? 5.909   76.272  99.257  1.00 19.16 ? 1101 ARG   A CA    1 
ATOM   7860  C  C     . ARG   A  1 1103 ? 5.734   76.706  100.704 1.00 20.35 ? 1101 ARG   A C     1 
ATOM   7861  O  O     . ARG   A  1 1103 ? 4.929   77.594  100.999 1.00 21.02 ? 1101 ARG   A O     1 
ATOM   7862  C  CB    . ARG   A  1 1103 ? 6.510   77.403  98.416  1.00 22.95 ? 1101 ARG   A CB    1 
ATOM   7863  C  CG    . ARG   A  1 1103 ? 7.965   77.713  98.808  1.00 21.23 ? 1101 ARG   A CG    1 
ATOM   7864  C  CD    . ARG   A  1 1103 ? 8.665   78.622  97.796  1.00 26.06 ? 1101 ARG   A CD    1 
ATOM   7865  N  NE    . ARG   A  1 1103 ? 8.699   78.037  96.458  1.00 29.79 ? 1101 ARG   A NE    1 
ATOM   7866  C  CZ    . ARG   A  1 1103 ? 9.695   77.313  95.955  1.00 35.31 ? 1101 ARG   A CZ    1 
ATOM   7867  N  NH1   . ARG   A  1 1103 ? 10.814  77.075  96.642  1.00 29.62 ? 1101 ARG   A NH1   1 
ATOM   7868  N  NH2   . ARG   A  1 1103 ? 9.574   76.824  94.724  1.00 37.31 ? 1101 ARG   A NH2   1 
ATOM   7869  N  N     . ILE   A  1 1104 ? 6.459   76.061  101.596 1.00 18.70 ? 1102 ILE   A N     1 
ATOM   7870  C  CA    . ILE   A  1 1104 ? 6.400   76.387  103.014 1.00 21.70 ? 1102 ILE   A CA    1 
ATOM   7871  C  C     . ILE   A  1 1104 ? 7.509   77.377  103.337 1.00 18.87 ? 1102 ILE   A C     1 
ATOM   7872  O  O     . ILE   A  1 1104 ? 8.672   77.169  102.976 1.00 18.88 ? 1102 ILE   A O     1 
ATOM   7873  C  CB    . ILE   A  1 1104 ? 6.524   75.124  103.880 1.00 18.86 ? 1102 ILE   A CB    1 
ATOM   7874  C  CG1   . ILE   A  1 1104 ? 5.489   74.068  103.449 1.00 18.62 ? 1102 ILE   A CG1   1 
ATOM   7875  C  CG2   . ILE   A  1 1104 ? 6.377   75.489  105.361 1.00 18.62 ? 1102 ILE   A CG2   1 
ATOM   7876  C  CD1   . ILE   A  1 1104 ? 4.029   74.524  103.524 1.00 18.82 ? 1102 ILE   A CD1   1 
ATOM   7877  N  N     . LEU   A  1 1105 ? 7.145   78.462  104.011 1.00 18.79 ? 1103 LEU   A N     1 
ATOM   7878  C  CA    . LEU   A  1 1105 ? 8.122   79.400  104.544 1.00 19.68 ? 1103 LEU   A CA    1 
ATOM   7879  C  C     . LEU   A  1 1105 ? 8.770   78.797  105.785 1.00 19.23 ? 1103 LEU   A C     1 
ATOM   7880  O  O     . LEU   A  1 1105 ? 8.077   78.452  106.749 1.00 19.71 ? 1103 LEU   A O     1 
ATOM   7881  C  CB    . LEU   A  1 1105 ? 7.444   80.725  104.888 1.00 19.21 ? 1103 LEU   A CB    1 
ATOM   7882  C  CG    . LEU   A  1 1105 ? 8.343   81.741  105.583 1.00 19.58 ? 1103 LEU   A CG    1 
ATOM   7883  C  CD1   . LEU   A  1 1105 ? 9.481   82.178  104.661 1.00 21.69 ? 1103 LEU   A CD1   1 
ATOM   7884  C  CD2   . LEU   A  1 1105 ? 7.493   82.925  106.019 1.00 22.25 ? 1103 LEU   A CD2   1 
ATOM   7885  N  N     . LEU   A  1 1106 ? 10.085  78.645  105.759 1.00 19.47 ? 1104 LEU   A N     1 
ATOM   7886  C  CA    . LEU   A  1 1106 ? 10.823  78.114  106.899 1.00 19.61 ? 1104 LEU   A CA    1 
ATOM   7887  C  C     . LEU   A  1 1106 ? 11.554  79.270  107.551 1.00 21.21 ? 1104 LEU   A C     1 
ATOM   7888  O  O     . LEU   A  1 1106 ? 12.324  79.968  106.886 1.00 22.57 ? 1104 LEU   A O     1 
ATOM   7889  C  CB    . LEU   A  1 1106 ? 11.827  77.037  106.486 1.00 19.66 ? 1104 LEU   A CB    1 
ATOM   7890  C  CG    . LEU   A  1 1106 ? 11.303  75.778  105.803 1.00 22.11 ? 1104 LEU   A CG    1 
ATOM   7891  C  CD1   . LEU   A  1 1106 ? 12.376  74.682  105.863 1.00 20.77 ? 1104 LEU   A CD1   1 
ATOM   7892  C  CD2   . LEU   A  1 1106 ? 10.021  75.318  106.448 1.00 20.67 ? 1104 LEU   A CD2   1 
ATOM   7893  N  N     . VAL   A  1 1107 ? 11.318  79.465  108.841 1.00 20.03 ? 1105 VAL   A N     1 
ATOM   7894  C  CA    . VAL   A  1 1107 ? 12.031  80.491  109.587 1.00 20.38 ? 1105 VAL   A CA    1 
ATOM   7895  C  C     . VAL   A  1 1107 ? 12.780  79.792  110.711 1.00 20.52 ? 1105 VAL   A C     1 
ATOM   7896  O  O     . VAL   A  1 1107 ? 12.322  79.773  111.860 1.00 22.55 ? 1105 VAL   A O     1 
ATOM   7897  C  CB    . VAL   A  1 1107 ? 11.076  81.573  110.109 1.00 21.23 ? 1105 VAL   A CB    1 
ATOM   7898  C  CG1   . VAL   A  1 1107 ? 11.879  82.760  110.627 1.00 21.10 ? 1105 VAL   A CG1   1 
ATOM   7899  C  CG2   . VAL   A  1 1107 ? 10.131  82.003  108.985 1.00 24.31 ? 1105 VAL   A CG2   1 
ATOM   7900  N  N     . PRO   A  1 1108 ? 13.932  79.209  110.427 1.00 20.66 ? 1106 PRO   A N     1 
ATOM   7901  C  CA    . PRO   A  1 1108 ? 14.669  78.483  111.458 1.00 21.30 ? 1106 PRO   A CA    1 
ATOM   7902  C  C     . PRO   A  1 1108 ? 15.505  79.429  112.309 1.00 23.78 ? 1106 PRO   A C     1 
ATOM   7903  O  O     . PRO   A  1 1108 ? 15.754  80.580  111.948 1.00 24.86 ? 1106 PRO   A O     1 
ATOM   7904  C  CB    . PRO   A  1 1108 ? 15.569  77.556  110.637 1.00 22.31 ? 1106 PRO   A CB    1 
ATOM   7905  C  CG    . PRO   A  1 1108 ? 15.897  78.399  109.427 1.00 20.90 ? 1106 PRO   A CG    1 
ATOM   7906  C  CD    . PRO   A  1 1108 ? 14.618  79.172  109.123 1.00 20.70 ? 1106 PRO   A CD    1 
ATOM   7907  N  N     . ALA   A  1 1109 ? 15.947  78.911  113.447 1.00 21.34 ? 1107 ALA   A N     1 
ATOM   7908  C  CA    . ALA   A  1 1109 ? 16.906  79.608  114.299 1.00 24.48 ? 1107 ALA   A CA    1 
ATOM   7909  C  C     . ALA   A  1 1109 ? 18.239  78.885  114.404 1.00 26.50 ? 1107 ALA   A C     1 
ATOM   7910  O  O     . ALA   A  1 1109 ? 19.286  79.533  114.469 1.00 29.42 ? 1107 ALA   A O     1 
ATOM   7911  C  CB    . ALA   A  1 1109 ? 16.313  79.816  115.704 1.00 24.95 ? 1107 ALA   A CB    1 
ATOM   7912  N  N     . THR   A  1 1110 ? 18.231  77.555  114.393 1.00 22.51 ? 1108 THR   A N     1 
ATOM   7913  C  CA    . THR   A  1 1110 ? 19.430  76.742  114.500 1.00 23.20 ? 1108 THR   A CA    1 
ATOM   7914  C  C     . THR   A  1 1110 ? 19.531  75.818  113.295 1.00 22.80 ? 1108 THR   A C     1 
ATOM   7915  O  O     . THR   A  1 1110 ? 18.551  75.576  112.583 1.00 22.93 ? 1108 THR   A O     1 
ATOM   7916  C  CB    . THR   A  1 1110 ? 19.422  75.904  115.787 1.00 23.75 ? 1108 THR   A CB    1 
ATOM   7917  O  OG1   . THR   A  1 1110 ? 18.346  74.960  115.734 1.00 22.95 ? 1108 THR   A OG1   1 
ATOM   7918  C  CG2   . THR   A  1 1110 ? 19.222  76.797  117.004 1.00 26.20 ? 1108 THR   A CG2   1 
ATOM   7919  N  N     . GLU   A  1 1111 ? 20.730  75.286  113.075 1.00 23.20 ? 1109 GLU   A N     1 
ATOM   7920  C  CA    . GLU   A  1 1111 ? 20.905  74.328  111.988 1.00 24.69 ? 1109 GLU   A CA    1 
ATOM   7921  C  C     . GLU   A  1 1111 ? 20.018  73.099  112.179 1.00 22.95 ? 1109 GLU   A C     1 
ATOM   7922  O  O     . GLU   A  1 1111 ? 19.366  72.635  111.236 1.00 23.48 ? 1109 GLU   A O     1 
ATOM   7923  C  CB    . GLU   A  1 1111 ? 22.369  73.921  111.894 1.00 28.81 ? 1109 GLU   A CB    1 
ATOM   7924  C  CG    . GLU   A  1 1111 ? 22.589  72.712  111.017 1.00 27.81 ? 1109 GLU   A CG    1 
ATOM   7925  C  CD    . GLU   A  1 1111 ? 24.054  72.395  110.867 1.00 31.47 ? 1109 GLU   A CD    1 
ATOM   7926  O  OE1   . GLU   A  1 1111 ? 24.725  73.103  110.092 1.00 32.43 ? 1109 GLU   A OE1   1 
ATOM   7927  O  OE2   . GLU   A  1 1111 ? 24.536  71.461  111.541 1.00 34.33 ? 1109 GLU   A OE2   1 
ATOM   7928  N  N     . SER   A  1 1112 ? 19.996  72.544  113.390 1.00 23.28 ? 1110 SER   A N     1 
ATOM   7929  C  CA    . SER   A  1 1112 ? 19.167  71.371  113.636 1.00 22.38 ? 1110 SER   A CA    1 
ATOM   7930  C  C     . SER   A  1 1112 ? 17.700  71.696  113.440 1.00 23.72 ? 1110 SER   A C     1 
ATOM   7931  O  O     . SER   A  1 1112 ? 16.948  70.887  112.889 1.00 21.57 ? 1110 SER   A O     1 
ATOM   7932  C  CB    . SER   A  1 1112 ? 19.399  70.834  115.043 1.00 24.66 ? 1110 SER   A CB    1 
ATOM   7933  O  OG    . SER   A  1 1112 ? 18.600  69.686  115.255 1.00 25.78 ? 1110 SER   A OG    1 
ATOM   7934  N  N     . GLY   A  1 1113 ? 17.276  72.877  113.893 1.00 21.90 ? 1111 GLY   A N     1 
ATOM   7935  C  CA    . GLY   A  1 1113 ? 15.909  73.299  113.649 1.00 20.78 ? 1111 GLY   A CA    1 
ATOM   7936  C  C     . GLY   A  1 1113 ? 15.588  73.359  112.172 1.00 20.63 ? 1111 GLY   A C     1 
ATOM   7937  O  O     . GLY   A  1 1113 ? 14.553  72.857  111.729 1.00 20.26 ? 1111 GLY   A O     1 
ATOM   7938  N  N     . LEU   A  1 1114 ? 16.488  73.955  111.387 1.00 20.73 ? 1112 LEU   A N     1 
ATOM   7939  C  CA    . LEU   A  1 1114 ? 16.301  73.990  109.940 1.00 23.24 ? 1112 LEU   A CA    1 
ATOM   7940  C  C     . LEU   A  1 1114 ? 16.152  72.585  109.367 1.00 20.39 ? 1112 LEU   A C     1 
ATOM   7941  O  O     . LEU   A  1 1114 ? 15.289  72.341  108.516 1.00 20.12 ? 1112 LEU   A O     1 
ATOM   7942  C  CB    . LEU   A  1 1114 ? 17.474  74.711  109.270 1.00 22.73 ? 1112 LEU   A CB    1 
ATOM   7943  C  CG    . LEU   A  1 1114 ? 17.461  74.607  107.739 1.00 23.37 ? 1112 LEU   A CG    1 
ATOM   7944  C  CD1   . LEU   A  1 1114 ? 16.167  75.195  107.162 1.00 20.46 ? 1112 LEU   A CD1   1 
ATOM   7945  C  CD2   . LEU   A  1 1114 ? 18.674  75.290  107.139 1.00 24.94 ? 1112 LEU   A CD2   1 
ATOM   7946  N  N     . TYR   A  1 1115 ? 16.988  71.644  109.813 1.00 20.85 ? 1113 TYR   A N     1 
ATOM   7947  C  CA    . TYR   A  1 1115 ? 16.907  70.295  109.257 1.00 20.43 ? 1113 TYR   A CA    1 
ATOM   7948  C  C     . TYR   A  1 1115 ? 15.575  69.642  109.603 1.00 20.13 ? 1113 TYR   A C     1 
ATOM   7949  O  O     . TYR   A  1 1115 ? 14.973  68.970  108.760 1.00 19.91 ? 1113 TYR   A O     1 
ATOM   7950  C  CB    . TYR   A  1 1115 ? 18.064  69.426  109.762 1.00 20.70 ? 1113 TYR   A CB    1 
ATOM   7951  C  CG    . TYR   A  1 1115 ? 19.444  69.843  109.284 1.00 21.01 ? 1113 TYR   A CG    1 
ATOM   7952  C  CD1   . TYR   A  1 1115 ? 19.609  70.665  108.170 1.00 21.43 ? 1113 TYR   A CD1   1 
ATOM   7953  C  CD2   . TYR   A  1 1115 ? 20.583  69.399  109.946 1.00 22.88 ? 1113 TYR   A CD2   1 
ATOM   7954  C  CE1   . TYR   A  1 1115 ? 20.888  71.041  107.732 1.00 22.34 ? 1113 TYR   A CE1   1 
ATOM   7955  C  CE2   . TYR   A  1 1115 ? 21.851  69.764  109.522 1.00 23.17 ? 1113 TYR   A CE2   1 
ATOM   7956  C  CZ    . TYR   A  1 1115 ? 21.996  70.582  108.420 1.00 24.45 ? 1113 TYR   A CZ    1 
ATOM   7957  O  OH    . TYR   A  1 1115 ? 23.263  70.942  108.008 1.00 27.25 ? 1113 TYR   A OH    1 
ATOM   7958  N  N     . HIS   A  1 1116 ? 15.118  69.802  110.850 1.00 20.33 ? 1114 HIS   A N     1 
ATOM   7959  C  CA    . HIS   A  1 1116 ? 13.815  69.270  111.239 1.00 19.89 ? 1114 HIS   A CA    1 
ATOM   7960  C  C     . HIS   A  1 1116 ? 12.684  69.932  110.457 1.00 21.03 ? 1114 HIS   A C     1 
ATOM   7961  O  O     . HIS   A  1 1116 ? 11.732  69.256  110.047 1.00 19.81 ? 1114 HIS   A O     1 
ATOM   7962  C  CB    . HIS   A  1 1116 ? 13.584  69.452  112.740 1.00 21.76 ? 1114 HIS   A CB    1 
ATOM   7963  C  CG    . HIS   A  1 1116 ? 14.309  68.456  113.587 1.00 22.56 ? 1114 HIS   A CG    1 
ATOM   7964  N  ND1   . HIS   A  1 1116 ? 15.611  68.639  114.004 1.00 25.49 ? 1114 HIS   A ND1   1 
ATOM   7965  C  CD2   . HIS   A  1 1116 ? 13.914  67.264  114.092 1.00 23.39 ? 1114 HIS   A CD2   1 
ATOM   7966  C  CE1   . HIS   A  1 1116 ? 15.986  67.603  114.732 1.00 24.06 ? 1114 HIS   A CE1   1 
ATOM   7967  N  NE2   . HIS   A  1 1116 ? 14.977  66.754  114.801 1.00 26.11 ? 1114 HIS   A NE2   1 
ATOM   7968  N  N     . GLN   A  1 1117 ? 12.748  71.259  110.270 1.00 19.65 ? 1115 GLN   A N     1 
ATOM   7969  C  CA    . GLN   A  1 1117 ? 11.713  71.944  109.502 1.00 19.42 ? 1115 GLN   A CA    1 
ATOM   7970  C  C     . GLN   A  1 1117 ? 11.715  71.464  108.062 1.00 19.27 ? 1115 GLN   A C     1 
ATOM   7971  O  O     . GLN   A  1 1117 ? 10.663  71.197  107.482 1.00 19.01 ? 1115 GLN   A O     1 
ATOM   7972  C  CB    . GLN   A  1 1117 ? 11.924  73.454  109.532 1.00 19.56 ? 1115 GLN   A CB    1 
ATOM   7973  C  CG    . GLN   A  1 1117 ? 11.719  74.109  110.889 1.00 19.69 ? 1115 GLN   A CG    1 
ATOM   7974  C  CD    . GLN   A  1 1117 ? 11.980  75.590  110.812 1.00 22.92 ? 1115 GLN   A CD    1 
ATOM   7975  O  OE1   . GLN   A  1 1117 ? 12.567  76.065  109.840 1.00 22.69 ? 1115 GLN   A OE1   1 
ATOM   7976  N  NE2   . GLN   A  1 1117 ? 11.550  76.333  111.827 1.00 20.25 ? 1115 GLN   A NE2   1 
ATOM   7977  N  N     . LEU   A  1 1118 ? 12.899  71.398  107.462 1.00 19.47 ? 1116 LEU   A N     1 
ATOM   7978  C  CA    A LEU   A  1 1118 ? 12.996  70.924  106.091 0.54 19.39 ? 1116 LEU   A CA    1 
ATOM   7979  C  CA    B LEU   A  1 1118 ? 13.028  70.908  106.095 0.46 19.40 ? 1116 LEU   A CA    1 
ATOM   7980  C  C     . LEU   A  1 1118 ? 12.467  69.500  105.968 1.00 19.21 ? 1116 LEU   A C     1 
ATOM   7981  O  O     . LEU   A  1 1118 ? 11.725  69.190  105.028 1.00 19.29 ? 1116 LEU   A O     1 
ATOM   7982  C  CB    A LEU   A  1 1118 ? 14.445  71.025  105.611 0.54 19.69 ? 1116 LEU   A CB    1 
ATOM   7983  C  CB    B LEU   A  1 1118 ? 14.499  70.940  105.674 0.46 19.70 ? 1116 LEU   A CB    1 
ATOM   7984  C  CG    A LEU   A  1 1118 ? 14.685  70.781  104.120 0.54 19.67 ? 1116 LEU   A CG    1 
ATOM   7985  C  CG    B LEU   A  1 1118 ? 15.044  72.236  105.083 0.46 19.87 ? 1116 LEU   A CG    1 
ATOM   7986  C  CD1   A LEU   A  1 1118 ? 13.660  71.522  103.254 0.54 19.45 ? 1116 LEU   A CD1   1 
ATOM   7987  C  CD1   B LEU   A  1 1118 ? 16.559  72.157  104.931 0.46 20.22 ? 1116 LEU   A CD1   1 
ATOM   7988  C  CD2   A LEU   A  1 1118 ? 16.085  71.220  103.768 0.54 21.68 ? 1116 LEU   A CD2   1 
ATOM   7989  C  CD2   B LEU   A  1 1118 ? 14.392  72.494  103.742 0.46 21.17 ? 1116 LEU   A CD2   1 
ATOM   7990  N  N     . ALA   A  1 1119 ? 12.813  68.630  106.917 1.00 20.91 ? 1117 ALA   A N     1 
ATOM   7991  C  CA    . ALA   A  1 1119 ? 12.285  67.268  106.885 1.00 20.63 ? 1117 ALA   A CA    1 
ATOM   7992  C  C     . ALA   A  1 1119 ? 10.762  67.272  106.921 1.00 18.97 ? 1117 ALA   A C     1 
ATOM   7993  O  O     . ALA   A  1 1119 ? 10.114  66.554  106.152 1.00 20.28 ? 1117 ALA   A O     1 
ATOM   7994  C  CB    . ALA   A  1 1119 ? 12.846  66.453  108.052 1.00 19.38 ? 1117 ALA   A CB    1 
ATOM   7995  N  N     . ALA   A  1 1120 ? 10.171  68.069  107.819 1.00 18.84 ? 1118 ALA   A N     1 
ATOM   7996  C  CA    . ALA   A  1 1120 ? 8.712   68.098  107.913 1.00 19.00 ? 1118 ALA   A CA    1 
ATOM   7997  C  C     . ALA   A  1 1120 ? 8.090   68.567  106.608 1.00 18.37 ? 1118 ALA   A C     1 
ATOM   7998  O  O     . ALA   A  1 1120 ? 7.100   67.994  106.134 1.00 18.15 ? 1118 ALA   A O     1 
ATOM   7999  C  CB    . ALA   A  1 1120 ? 8.273   68.999  109.070 1.00 18.61 ? 1118 ALA   A CB    1 
ATOM   8000  N  N     . ALA   A  1 1121 ? 8.678   69.594  105.996 1.00 18.46 ? 1119 ALA   A N     1 
ATOM   8001  C  CA    . ALA   A  1 1121 ? 8.105   70.150  104.776 1.00 18.30 ? 1119 ALA   A CA    1 
ATOM   8002  C  C     . ALA   A  1 1121 ? 8.288   69.205  103.599 1.00 19.08 ? 1119 ALA   A C     1 
ATOM   8003  O  O     . ALA   A  1 1121 ? 7.367   69.027  102.791 1.00 18.07 ? 1119 ALA   A O     1 
ATOM   8004  C  CB    . ALA   A  1 1121 ? 8.738   71.507  104.475 1.00 18.47 ? 1119 ALA   A CB    1 
ATOM   8005  N  N     . LEU   A  1 1122 ? 9.467   68.595  103.481 1.00 18.46 ? 1120 LEU   A N     1 
ATOM   8006  C  CA    . LEU   A  1 1122 ? 9.716   67.697  102.358 1.00 18.45 ? 1120 LEU   A CA    1 
ATOM   8007  C  C     . LEU   A  1 1122 ? 8.900   66.422  102.484 1.00 18.28 ? 1120 LEU   A C     1 
ATOM   8008  O  O     . LEU   A  1 1122 ? 8.388   65.910  101.483 1.00 21.55 ? 1120 LEU   A O     1 
ATOM   8009  C  CB    . LEU   A  1 1122 ? 11.196  67.352  102.262 1.00 21.33 ? 1120 LEU   A CB    1 
ATOM   8010  C  CG    . LEU   A  1 1122 ? 12.163  68.484  101.940 1.00 18.97 ? 1120 LEU   A CG    1 
ATOM   8011  C  CD1   . LEU   A  1 1122 ? 13.561  67.927  101.961 1.00 21.14 ? 1120 LEU   A CD1   1 
ATOM   8012  C  CD2   . LEU   A  1 1122 ? 11.830  69.086  100.584 1.00 20.54 ? 1120 LEU   A CD2   1 
ATOM   8013  N  N     . ALA   A  1 1123 ? 8.773   65.896  103.704 1.00 18.31 ? 1121 ALA   A N     1 
ATOM   8014  C  CA    . ALA   A  1 1123 ? 8.012   64.671  103.914 1.00 18.19 ? 1121 ALA   A CA    1 
ATOM   8015  C  C     . ALA   A  1 1123 ? 6.555   64.830  103.523 1.00 19.38 ? 1121 ALA   A C     1 
ATOM   8016  O  O     . ALA   A  1 1123 ? 5.882   63.824  103.272 1.00 19.13 ? 1121 ALA   A O     1 
ATOM   8017  C  CB    . ALA   A  1 1123 ? 8.074   64.235  105.375 1.00 19.81 ? 1121 ALA   A CB    1 
ATOM   8018  N  N     . THR   A  1 1124 ? 6.048   66.061  103.507 1.00 17.79 ? 1122 THR   A N     1 
ATOM   8019  C  CA    . THR   A  1 1124 ? 4.683   66.334  103.096 1.00 17.54 ? 1122 THR   A CA    1 
ATOM   8020  C  C     . THR   A  1 1124 ? 4.611   66.878  101.672 1.00 17.46 ? 1122 THR   A C     1 
ATOM   8021  O  O     . THR   A  1 1124 ? 3.582   67.437  101.275 1.00 17.91 ? 1122 THR   A O     1 
ATOM   8022  C  CB    . THR   A  1 1124 ? 4.023   67.281  104.102 1.00 17.48 ? 1122 THR   A CB    1 
ATOM   8023  O  OG1   . THR   A  1 1124 ? 4.914   68.352  104.417 1.00 18.23 ? 1122 THR   A OG1   1 
ATOM   8024  C  CG2   . THR   A  1 1124 ? 3.735   66.530  105.389 1.00 17.52 ? 1122 THR   A CG2   1 
ATOM   8025  N  N     . GLY   A  1 1125 ? 5.678   66.696  100.891 1.00 17.63 ? 1123 GLY   A N     1 
ATOM   8026  C  CA    . GLY   A  1 1125 ? 5.656   66.979  99.463  1.00 17.62 ? 1123 GLY   A CA    1 
ATOM   8027  C  C     . GLY   A  1 1125 ? 5.927   68.416  99.087  1.00 18.28 ? 1123 GLY   A C     1 
ATOM   8028  O  O     . GLY   A  1 1125 ? 5.858   68.756  97.900  1.00 18.63 ? 1123 GLY   A O     1 
ATOM   8029  N  N     . ASN   A  1 1126 ? 6.258   69.262  100.050 1.00 18.39 ? 1124 ASN   A N     1 
ATOM   8030  C  CA    . ASN   A  1 1126 ? 6.338   70.691  99.813  1.00 17.83 ? 1124 ASN   A CA    1 
ATOM   8031  C  C     . ASN   A  1 1126 ? 7.724   71.092  99.340  1.00 18.11 ? 1124 ASN   A C     1 
ATOM   8032  O  O     . ASN   A  1 1126 ? 8.715   70.389  99.556  1.00 18.60 ? 1124 ASN   A O     1 
ATOM   8033  C  CB    . ASN   A  1 1126 ? 5.989   71.461  101.089 1.00 17.82 ? 1124 ASN   A CB    1 
ATOM   8034  C  CG    . ASN   A  1 1126 ? 4.590   71.170  101.563 1.00 17.65 ? 1124 ASN   A CG    1 
ATOM   8035  O  OD1   . ASN   A  1 1126 ? 3.621   71.587  100.927 1.00 18.82 ? 1124 ASN   A OD1   1 
ATOM   8036  N  ND2   . ASN   A  1 1126 ? 4.467   70.443  102.678 1.00 17.56 ? 1124 ASN   A ND2   1 
ATOM   8037  N  N     . SER   A  1 1127 ? 7.769   72.235  98.668  1.00 18.68 ? 1125 SER   A N     1 
ATOM   8038  C  CA    . SER   A  1 1127 ? 8.989   73.004  98.524  1.00 19.51 ? 1125 SER   A CA    1 
ATOM   8039  C  C     . SER   A  1 1127 ? 9.065   73.982  99.684  1.00 18.58 ? 1125 SER   A C     1 
ATOM   8040  O  O     . SER   A  1 1127 ? 8.115   74.136  100.452 1.00 20.24 ? 1125 SER   A O     1 
ATOM   8041  C  CB    . SER   A  1 1127 ? 9.004   73.745  97.193  1.00 21.81 ? 1125 SER   A CB    1 
ATOM   8042  O  OG    . SER   A  1 1127 ? 7.905   74.619  97.126  1.00 23.18 ? 1125 SER   A OG    1 
ATOM   8043  N  N     . VAL   A  1 1128 ? 10.207  74.650  99.816  1.00 18.88 ? 1126 VAL   A N     1 
ATOM   8044  C  CA    . VAL   A  1 1128 ? 10.411  75.549  100.943 1.00 19.02 ? 1126 VAL   A CA    1 
ATOM   8045  C  C     . VAL   A  1 1128 ? 11.046  76.832  100.447 1.00 22.19 ? 1126 VAL   A C     1 
ATOM   8046  O  O     . VAL   A  1 1128 ? 11.763  76.849  99.444  1.00 19.45 ? 1126 VAL   A O     1 
ATOM   8047  C  CB    . VAL   A  1 1128 ? 11.299  74.931  102.044 1.00 20.84 ? 1126 VAL   A CB    1 
ATOM   8048  C  CG1   . VAL   A  1 1128 ? 10.653  73.684  102.613 1.00 18.93 ? 1126 VAL   A CG1   1 
ATOM   8049  C  CG2   . VAL   A  1 1128 ? 12.673  74.627  101.487 1.00 21.32 ? 1126 VAL   A CG2   1 
ATOM   8050  N  N     . ALA   A  1 1129 ? 10.769  77.912  101.163 1.00 20.76 ? 1127 ALA   A N     1 
ATOM   8051  C  CA    . ALA   A  1 1129 ? 11.551  79.135  101.079 1.00 24.50 ? 1127 ALA   A CA    1 
ATOM   8052  C  C     . ALA   A  1 1129 ? 12.119  79.361  102.468 1.00 24.18 ? 1127 ALA   A C     1 
ATOM   8053  O  O     . ALA   A  1 1129 ? 11.357  79.441  103.436 1.00 21.41 ? 1127 ALA   A O     1 
ATOM   8054  C  CB    . ALA   A  1 1129 ? 10.694  80.317  100.625 1.00 23.58 ? 1127 ALA   A CB    1 
ATOM   8055  N  N     . ILE   A  1 1130 ? 13.447  79.418  102.578 1.00 21.07 ? 1128 ILE   A N     1 
ATOM   8056  C  CA    . ILE   A  1 1130 ? 14.108  79.509  103.879 1.00 24.07 ? 1128 ILE   A CA    1 
ATOM   8057  C  C     . ILE   A  1 1130 ? 14.524  80.953  104.123 1.00 26.51 ? 1128 ILE   A C     1 
ATOM   8058  O  O     . ILE   A  1 1130 ? 15.133  81.590  103.253 1.00 25.56 ? 1128 ILE   A O     1 
ATOM   8059  C  CB    . ILE   A  1 1130 ? 15.329  78.581  103.976 1.00 22.24 ? 1128 ILE   A CB    1 
ATOM   8060  C  CG1   . ILE   A  1 1130 ? 14.982  77.145  103.594 1.00 23.09 ? 1128 ILE   A CG1   1 
ATOM   8061  C  CG2   . ILE   A  1 1130 ? 15.902  78.636  105.396 1.00 21.29 ? 1128 ILE   A CG2   1 
ATOM   8062  C  CD1   . ILE   A  1 1130 ? 16.233  76.276  103.422 1.00 24.50 ? 1128 ILE   A CD1   1 
ATOM   8063  N  N     . ASP   A  1 1131 ? 14.196  81.467  105.307 1.00 26.06 ? 1129 ASP   A N     1 
ATOM   8064  C  CA    . ASP   A  1 1131 ? 14.593  82.816  105.689 1.00 24.50 ? 1129 ASP   A CA    1 
ATOM   8065  C  C     . ASP   A  1 1131 ? 16.098  82.998  105.533 1.00 27.18 ? 1129 ASP   A C     1 
ATOM   8066  O  O     . ASP   A  1 1131 ? 16.887  82.361  106.241 1.00 25.72 ? 1129 ASP   A O     1 
ATOM   8067  C  CB    . ASP   A  1 1131 ? 14.167  83.105  107.126 1.00 25.47 ? 1129 ASP   A CB    1 
ATOM   8068  C  CG    . ASP   A  1 1131 ? 14.533  84.506  107.571 1.00 29.57 ? 1129 ASP   A CG    1 
ATOM   8069  O  OD1   . ASP   A  1 1131 ? 14.660  85.395  106.706 1.00 27.25 ? 1129 ASP   A OD1   1 
ATOM   8070  O  OD2   . ASP   A  1 1131 ? 14.702  84.711  108.790 1.00 28.88 ? 1129 ASP   A OD2   1 
ATOM   8071  N  N     . ALA   A  1 1132 ? 16.502  83.851  104.592 1.00 28.00 ? 1130 ALA   A N     1 
ATOM   8072  C  CA    . ALA   A  1 1132 ? 17.924  84.128  104.419 1.00 31.46 ? 1130 ALA   A CA    1 
ATOM   8073  C  C     . ALA   A  1 1132 ? 18.514  84.860  105.621 1.00 29.56 ? 1130 ALA   A C     1 
ATOM   8074  O  O     . ALA   A  1 1132 ? 19.723  84.772  105.858 1.00 34.11 ? 1130 ALA   A O     1 
ATOM   8075  C  CB    . ALA   A  1 1132 ? 18.142  84.933  103.138 1.00 31.68 ? 1130 ALA   A CB    1 
ATOM   8076  N  N     . ALA   A  1 1133 ? 17.689  85.567  106.395 1.00 31.18 ? 1131 ALA   A N     1 
ATOM   8077  C  CA    . ALA   A  1 1133 ? 18.194  86.265  107.569 1.00 33.26 ? 1131 ALA   A CA    1 
ATOM   8078  C  C     . ALA   A  1 1133 ? 18.607  85.312  108.682 1.00 32.24 ? 1131 ALA   A C     1 
ATOM   8079  O  O     . ALA   A  1 1133 ? 19.260  85.746  109.635 1.00 32.97 ? 1131 ALA   A O     1 
ATOM   8080  C  CB    . ALA   A  1 1133 ? 17.144  87.251  108.083 1.00 33.24 ? 1131 ALA   A CB    1 
ATOM   8081  N  N     . SER   A  1 1134 ? 18.255  84.032  108.581 1.00 31.72 ? 1132 SER   A N     1 
ATOM   8082  C  CA    . SER   A  1 1134 ? 18.680  83.052  109.570 1.00 27.45 ? 1132 SER   A CA    1 
ATOM   8083  C  C     . SER   A  1 1134 ? 20.185  82.865  109.583 1.00 31.47 ? 1132 SER   A C     1 
ATOM   8084  O  O     . SER   A  1 1134 ? 20.728  82.408  110.591 1.00 24.08 ? 1132 SER   A O     1 
ATOM   8085  C  CB    . SER   A  1 1134 ? 18.023  81.700  109.293 1.00 30.49 ? 1132 SER   A CB    1 
ATOM   8086  O  OG    . SER   A  1 1134 ? 18.537  81.131  108.094 1.00 28.26 ? 1132 SER   A OG    1 
ATOM   8087  N  N     . GLY   A  1 1135 ? 20.862  83.183  108.481 1.00 27.87 ? 1133 GLY   A N     1 
ATOM   8088  C  CA    . GLY   A  1 1135 ? 22.293  82.973  108.392 1.00 32.27 ? 1133 GLY   A CA    1 
ATOM   8089  C  C     . GLY   A  1 1135 ? 22.713  81.527  108.307 1.00 31.27 ? 1133 GLY   A C     1 
ATOM   8090  O  O     . GLY   A  1 1135 ? 23.886  81.220  108.521 1.00 30.76 ? 1133 GLY   A O     1 
ATOM   8091  N  N     . LEU   A  1 1136 ? 21.790  80.619  107.991 1.00 26.93 ? 1134 LEU   A N     1 
ATOM   8092  C  CA    . LEU   A  1 1136 ? 22.076  79.191  108.011 1.00 31.37 ? 1134 LEU   A CA    1 
ATOM   8093  C  C     . LEU   A  1 1136 ? 22.374  78.632  106.626 1.00 30.25 ? 1134 LEU   A C     1 
ATOM   8094  O  O     . LEU   A  1 1136 ? 22.273  77.418  106.426 1.00 29.12 ? 1134 LEU   A O     1 
ATOM   8095  C  CB    . LEU   A  1 1136 ? 20.911  78.426  108.647 1.00 27.94 ? 1134 LEU   A CB    1 
ATOM   8096  C  CG    . LEU   A  1 1136 ? 20.658  78.707  110.132 1.00 28.47 ? 1134 LEU   A CG    1 
ATOM   8097  C  CD1   . LEU   A  1 1136 ? 19.317  78.114  110.571 1.00 25.33 ? 1134 LEU   A CD1   1 
ATOM   8098  C  CD2   . LEU   A  1 1136 ? 21.802  78.175  111.002 1.00 30.29 ? 1134 LEU   A CD2   1 
ATOM   8099  N  N     . GLN   A  1 1137 ? 22.732  79.490  105.666 1.00 29.82 ? 1135 GLN   A N     1 
ATOM   8100  C  CA    . GLN   A  1 1137 ? 22.989  79.008  104.311 1.00 30.15 ? 1135 GLN   A CA    1 
ATOM   8101  C  C     . GLN   A  1 1137 ? 24.104  77.968  104.289 1.00 30.01 ? 1135 GLN   A C     1 
ATOM   8102  O  O     . GLN   A  1 1137 ? 24.018  76.974  103.559 1.00 31.72 ? 1135 GLN   A O     1 
ATOM   8103  C  CB    . GLN   A  1 1137 ? 23.330  80.174  103.386 1.00 30.09 ? 1135 GLN   A CB    1 
ATOM   8104  C  CG    . GLN   A  1 1137 ? 22.136  81.045  103.014 1.00 31.17 ? 1135 GLN   A CG    1 
ATOM   8105  C  CD    . GLN   A  1 1137 ? 21.961  82.229  103.949 1.00 27.99 ? 1135 GLN   A CD    1 
ATOM   8106  O  OE1   . GLN   A  1 1137 ? 22.354  82.180  105.116 1.00 34.01 ? 1135 GLN   A OE1   1 
ATOM   8107  N  NE2   . GLN   A  1 1137 ? 21.387  83.311  103.431 1.00 37.71 ? 1135 GLN   A NE2   1 
ATOM   8108  N  N     . ALA   A  1 1138 ? 25.150  78.162  105.095 1.00 31.40 ? 1136 ALA   A N     1 
ATOM   8109  C  CA    . ALA   A  1 1138 ? 26.242  77.193  105.100 1.00 28.80 ? 1136 ALA   A CA    1 
ATOM   8110  C  C     . ALA   A  1 1138 ? 25.815  75.813  105.586 1.00 31.05 ? 1136 ALA   A C     1 
ATOM   8111  O  O     . ALA   A  1 1138 ? 26.586  74.859  105.431 1.00 30.64 ? 1136 ALA   A O     1 
ATOM   8112  C  CB    . ALA   A  1 1138 ? 27.409  77.693  105.960 1.00 31.43 ? 1136 ALA   A CB    1 
ATOM   8113  N  N     . SER   A  1 1139 ? 24.619  75.678  106.166 1.00 29.01 ? 1137 SER   A N     1 
ATOM   8114  C  CA    . SER   A  1 1139 ? 24.172  74.384  106.658 1.00 31.20 ? 1137 SER   A CA    1 
ATOM   8115  C  C     . SER   A  1 1139 ? 23.580  73.507  105.563 1.00 24.87 ? 1137 SER   A C     1 
ATOM   8116  O  O     . SER   A  1 1139 ? 23.301  72.332  105.821 1.00 28.24 ? 1137 SER   A O     1 
ATOM   8117  C  CB    . SER   A  1 1139 ? 23.138  74.561  107.774 1.00 30.23 ? 1137 SER   A CB    1 
ATOM   8118  O  OG    . SER   A  1 1139 ? 23.708  75.197  108.911 1.00 32.91 ? 1137 SER   A OG    1 
ATOM   8119  N  N     . LEU   A  1 1140 ? 23.379  74.039  104.364 1.00 29.82 ? 1138 LEU   A N     1 
ATOM   8120  C  CA    . LEU   A  1 1140 ? 22.806  73.281  103.256 1.00 28.53 ? 1138 LEU   A CA    1 
ATOM   8121  C  C     . LEU   A  1 1140 ? 23.765  73.207  102.081 1.00 31.29 ? 1138 LEU   A C     1 
ATOM   8122  O  O     . LEU   A  1 1140 ? 23.355  73.260  100.923 1.00 36.62 ? 1138 LEU   A O     1 
ATOM   8123  C  CB    . LEU   A  1 1140 ? 21.478  73.878  102.803 1.00 29.65 ? 1138 LEU   A CB    1 
ATOM   8124  C  CG    . LEU   A  1 1140 ? 20.266  73.685  103.702 1.00 28.46 ? 1138 LEU   A CG    1 
ATOM   8125  C  CD1   . LEU   A  1 1140 ? 19.037  74.125  102.938 1.00 32.33 ? 1138 LEU   A CD1   1 
ATOM   8126  C  CD2   . LEU   A  1 1140 ? 20.120  72.241  104.188 1.00 22.71 ? 1138 LEU   A CD2   1 
ATOM   8127  N  N     . LYS   A  1 1141 ? 25.058  73.091  102.361 1.00 30.34 ? 1139 LYS   A N     1 
ATOM   8128  C  CA    . LYS   A  1 1141 ? 26.020  72.903  101.287 1.00 41.30 ? 1139 LYS   A CA    1 
ATOM   8129  C  C     . LYS   A  1 1141 ? 25.821  71.538  100.634 1.00 39.69 ? 1139 LYS   A C     1 
ATOM   8130  O  O     . LYS   A  1 1141 ? 25.536  70.544  101.309 1.00 36.62 ? 1139 LYS   A O     1 
ATOM   8131  C  CB    . LYS   A  1 1141 ? 27.447  73.031  101.823 1.00 37.74 ? 1139 LYS   A CB    1 
ATOM   8132  N  N     . ASN   A  1 1142 ? 25.948  71.502  99.306  1.00 38.22 ? 1140 ASN   A N     1 
ATOM   8133  C  CA    . ASN   A  1 1142 ? 26.056  70.251  98.553  1.00 38.12 ? 1140 ASN   A CA    1 
ATOM   8134  C  C     . ASN   A  1 1142 ? 24.785  69.410  98.642  1.00 35.82 ? 1140 ASN   A C     1 
ATOM   8135  O  O     . ASN   A  1 1142 ? 24.853  68.190  98.799  1.00 34.41 ? 1140 ASN   A O     1 
ATOM   8136  C  CB    . ASN   A  1 1142 ? 27.259  69.422  99.013  1.00 40.26 ? 1140 ASN   A CB    1 
ATOM   8137  C  CG    . ASN   A  1 1142 ? 28.533  70.233  99.094  1.00 49.58 ? 1140 ASN   A CG    1 
ATOM   8138  O  OD1   . ASN   A  1 1142 ? 29.222  70.229  100.119 1.00 48.73 ? 1140 ASN   A OD1   1 
ATOM   8139  N  ND2   . ASN   A  1 1142 ? 28.856  70.939  98.013  1.00 47.67 ? 1140 ASN   A ND2   1 
ATOM   8140  N  N     . LEU   A  1 1143 ? 23.625  70.053  98.536  1.00 35.37 ? 1141 LEU   A N     1 
ATOM   8141  C  CA    . LEU   A  1 1143 ? 22.381  69.301  98.512  1.00 32.39 ? 1141 LEU   A CA    1 
ATOM   8142  C  C     . LEU   A  1 1143 ? 22.276  68.485  97.226  1.00 34.27 ? 1141 LEU   A C     1 
ATOM   8143  O  O     . LEU   A  1 1143 ? 22.728  68.919  96.163  1.00 31.08 ? 1141 LEU   A O     1 
ATOM   8144  C  CB    . LEU   A  1 1143 ? 21.179  70.233  98.606  1.00 31.70 ? 1141 LEU   A CB    1 
ATOM   8145  C  CG    . LEU   A  1 1143 ? 20.775  70.833  99.948  1.00 30.26 ? 1141 LEU   A CG    1 
ATOM   8146  C  CD1   . LEU   A  1 1143 ? 19.605  71.753  99.691  1.00 28.98 ? 1141 LEU   A CD1   1 
ATOM   8147  C  CD2   . LEU   A  1 1143 ? 20.408  69.752  100.972 1.00 29.70 ? 1141 LEU   A CD2   1 
ATOM   8148  N  N     . PRO   A  1 1144 ? 21.673  67.302  97.290  1.00 33.27 ? 1142 PRO   A N     1 
ATOM   8149  C  CA    . PRO   A  1 1144 ? 21.296  66.619  96.048  1.00 34.41 ? 1142 PRO   A CA    1 
ATOM   8150  C  C     . PRO   A  1 1144 ? 20.417  67.542  95.216  1.00 32.06 ? 1142 PRO   A C     1 
ATOM   8151  O  O     . PRO   A  1 1144 ? 19.635  68.329  95.757  1.00 28.61 ? 1142 PRO   A O     1 
ATOM   8152  C  CB    . PRO   A  1 1144 ? 20.525  65.386  96.537  1.00 33.01 ? 1142 PRO   A CB    1 
ATOM   8153  C  CG    . PRO   A  1 1144 ? 20.943  65.206  97.968  1.00 32.90 ? 1142 PRO   A CG    1 
ATOM   8154  C  CD    . PRO   A  1 1144 ? 21.204  66.586  98.487  1.00 31.22 ? 1142 PRO   A CD    1 
ATOM   8155  N  N     . GLN   A  1 1145 ? 20.568  67.462  93.891  1.00 29.64 ? 1143 GLN   A N     1 
ATOM   8156  C  CA    . GLN   A  1 1145 ? 19.779  68.317  93.007  1.00 31.27 ? 1143 GLN   A CA    1 
ATOM   8157  C  C     . GLN   A  1 1145 ? 18.284  68.189  93.286  1.00 29.66 ? 1143 GLN   A C     1 
ATOM   8158  O  O     . GLN   A  1 1145 ? 17.551  69.183  93.236  1.00 27.40 ? 1143 GLN   A O     1 
ATOM   8159  C  CB    . GLN   A  1 1145 ? 20.079  67.987  91.542  1.00 36.16 ? 1143 GLN   A CB    1 
ATOM   8160  N  N     . THR   A  1 1146 ? 17.813  66.976  93.590  1.00 27.99 ? 1144 THR   A N     1 
ATOM   8161  C  CA    . THR   A  1 1146 ? 16.389  66.781  93.852  1.00 30.11 ? 1144 THR   A CA    1 
ATOM   8162  C  C     . THR   A  1 1146 ? 15.915  67.644  95.013  1.00 29.13 ? 1144 THR   A C     1 
ATOM   8163  O  O     . THR   A  1 1146 ? 14.798  68.180  94.987  1.00 26.74 ? 1144 THR   A O     1 
ATOM   8164  C  CB    . THR   A  1 1146 ? 16.091  65.315  94.164  1.00 29.13 ? 1144 THR   A CB    1 
ATOM   8165  O  OG1   . THR   A  1 1146 ? 16.991  64.863  95.177  1.00 30.30 ? 1144 THR   A OG1   1 
ATOM   8166  C  CG2   . THR   A  1 1146 ? 16.235  64.443  92.921  1.00 30.45 ? 1144 THR   A CG2   1 
ATOM   8167  N  N     . VAL   A  1 1147 ? 16.737  67.756  96.056  1.00 25.94 ? 1145 VAL   A N     1 
ATOM   8168  C  CA    . VAL   A  1 1147 ? 16.376  68.581  97.201  1.00 22.15 ? 1145 VAL   A CA    1 
ATOM   8169  C  C     . VAL   A  1 1147 ? 16.603  70.045  96.875  1.00 25.06 ? 1145 VAL   A C     1 
ATOM   8170  O  O     . VAL   A  1 1147 ? 15.780  70.902  97.214  1.00 23.61 ? 1145 VAL   A O     1 
ATOM   8171  C  CB    . VAL   A  1 1147 ? 17.172  68.146  98.449  1.00 26.56 ? 1145 VAL   A CB    1 
ATOM   8172  C  CG1   . VAL   A  1 1147 ? 16.717  68.934  99.667  1.00 21.69 ? 1145 VAL   A CG1   1 
ATOM   8173  C  CG2   . VAL   A  1 1147 ? 17.029  66.636  98.683  1.00 23.86 ? 1145 VAL   A CG2   1 
ATOM   8174  N  N     . GLY   A  1 1148 ? 17.716  70.348  96.204  1.00 27.80 ? 1146 GLY   A N     1 
ATOM   8175  C  CA    . GLY   A  1 1148 ? 17.985  71.718  95.811  1.00 26.88 ? 1146 GLY   A CA    1 
ATOM   8176  C  C     . GLY   A  1 1148 ? 16.856  72.330  95.010  1.00 23.79 ? 1146 GLY   A C     1 
ATOM   8177  O  O     . GLY   A  1 1148 ? 16.506  73.495  95.212  1.00 27.06 ? 1146 GLY   A O     1 
ATOM   8178  N  N     . LEU   A  1 1149 ? 16.250  71.547  94.106  1.00 23.41 ? 1147 LEU   A N     1 
ATOM   8179  C  CA    . LEU   A  1 1149 ? 15.130  72.057  93.319  1.00 28.37 ? 1147 LEU   A CA    1 
ATOM   8180  C  C     . LEU   A  1 1149 ? 13.989  72.510  94.210  1.00 25.26 ? 1147 LEU   A C     1 
ATOM   8181  O  O     . LEU   A  1 1149 ? 13.208  73.381  93.822  1.00 28.41 ? 1147 LEU   A O     1 
ATOM   8182  C  CB    . LEU   A  1 1149 ? 14.614  70.993  92.346  1.00 30.11 ? 1147 LEU   A CB    1 
ATOM   8183  C  CG    . LEU   A  1 1149 ? 15.566  70.546  91.235  1.00 35.10 ? 1147 LEU   A CG    1 
ATOM   8184  C  CD1   . LEU   A  1 1149 ? 14.979  69.351  90.504  1.00 34.84 ? 1147 LEU   A CD1   1 
ATOM   8185  C  CD2   . LEU   A  1 1149 ? 15.851  71.685  90.274  1.00 38.88 ? 1147 LEU   A CD2   1 
ATOM   8186  N  N     . ARG   A  1 1150 ? 13.870  71.930  95.399  1.00 25.53 ? 1148 ARG   A N     1 
ATOM   8187  C  CA    . ARG   A  1 1150 ? 12.770  72.270  96.284  1.00 24.04 ? 1148 ARG   A CA    1 
ATOM   8188  C  C     . ARG   A  1 1150 ? 13.104  73.400  97.239  1.00 23.18 ? 1148 ARG   A C     1 
ATOM   8189  O  O     . ARG   A  1 1150 ? 12.214  73.863  97.952  1.00 25.34 ? 1148 ARG   A O     1 
ATOM   8190  C  CB    . ARG   A  1 1150 ? 12.341  71.039  97.090  1.00 25.58 ? 1148 ARG   A CB    1 
ATOM   8191  C  CG    . ARG   A  1 1150 ? 11.593  69.993  96.277  1.00 25.02 ? 1148 ARG   A CG    1 
ATOM   8192  C  CD    . ARG   A  1 1150 ? 10.394  69.525  97.055  1.00 24.35 ? 1148 ARG   A CD    1 
ATOM   8193  N  NE    . ARG   A  1 1150 ? 9.799   68.323  96.493  1.00 23.50 ? 1148 ARG   A NE    1 
ATOM   8194  C  CZ    . ARG   A  1 1150 ? 9.256   67.369  97.231  1.00 23.92 ? 1148 ARG   A CZ    1 
ATOM   8195  N  NH1   . ARG   A  1 1150 ? 9.173   67.486  98.548  1.00 21.51 ? 1148 ARG   A NH1   1 
ATOM   8196  N  NH2   . ARG   A  1 1150 ? 8.785   66.275  96.635  1.00 20.93 ? 1148 ARG   A NH2   1 
ATOM   8197  N  N     . VAL   A  1 1151 ? 14.353  73.855  97.277  1.00 21.25 ? 1149 VAL   A N     1 
ATOM   8198  C  CA    . VAL   A  1 1151 ? 14.795  74.811  98.280  1.00 24.43 ? 1149 VAL   A CA    1 
ATOM   8199  C  C     . VAL   A  1 1151 ? 15.053  76.158  97.620  1.00 29.63 ? 1149 VAL   A C     1 
ATOM   8200  O  O     . VAL   A  1 1151 ? 15.783  76.248  96.626  1.00 26.10 ? 1149 VAL   A O     1 
ATOM   8201  C  CB    . VAL   A  1 1151 ? 16.038  74.301  99.024  1.00 24.76 ? 1149 VAL   A CB    1 
ATOM   8202  C  CG1   . VAL   A  1 1151 ? 16.615  75.398  99.928  1.00 29.89 ? 1149 VAL   A CG1   1 
ATOM   8203  C  CG2   . VAL   A  1 1151 ? 15.668  73.087  99.837  1.00 27.22 ? 1149 VAL   A CG2   1 
ATOM   8204  N  N     . SER   A  1 1152 ? 14.439  77.199  98.169  1.00 25.97 ? 1150 SER   A N     1 
ATOM   8205  C  CA    . SER   A  1 1152 ? 14.749  78.575  97.826  1.00 27.53 ? 1150 SER   A CA    1 
ATOM   8206  C  C     . SER   A  1 1152 ? 15.130  79.305  99.104  1.00 26.77 ? 1150 SER   A C     1 
ATOM   8207  O  O     . SER   A  1 1152 ? 14.692  78.938  100.199 1.00 24.55 ? 1150 SER   A O     1 
ATOM   8208  C  CB    . SER   A  1 1152 ? 13.554  79.268  97.151  1.00 27.34 ? 1150 SER   A CB    1 
ATOM   8209  N  N     . TRP   A  1 1153 ? 15.961  80.329  98.964  1.00 25.66 ? 1151 TRP   A N     1 
ATOM   8210  C  CA    . TRP   A  1 1153 ? 16.319  81.201  100.074 1.00 28.78 ? 1151 TRP   A CA    1 
ATOM   8211  C  C     . TRP   A  1 1153 ? 15.660  82.552  99.853  1.00 33.56 ? 1151 TRP   A C     1 
ATOM   8212  O  O     . TRP   A  1 1153 ? 15.710  83.097  98.745  1.00 31.52 ? 1151 TRP   A O     1 
ATOM   8213  C  CB    . TRP   A  1 1153 ? 17.830  81.350  100.190 1.00 29.39 ? 1151 TRP   A CB    1 
ATOM   8214  C  CG    . TRP   A  1 1153 ? 18.508  80.120  100.729 1.00 29.18 ? 1151 TRP   A CG    1 
ATOM   8215  C  CD1   . TRP   A  1 1153 ? 18.999  79.071  100.008 1.00 27.14 ? 1151 TRP   A CD1   1 
ATOM   8216  C  CD2   . TRP   A  1 1153 ? 18.757  79.812  102.110 1.00 26.10 ? 1151 TRP   A CD2   1 
ATOM   8217  N  NE1   . TRP   A  1 1153 ? 19.550  78.134  100.853 1.00 31.19 ? 1151 TRP   A NE1   1 
ATOM   8218  C  CE2   . TRP   A  1 1153 ? 19.414  78.566  102.149 1.00 28.24 ? 1151 TRP   A CE2   1 
ATOM   8219  C  CE3   . TRP   A  1 1153 ? 18.496  80.473  103.313 1.00 26.03 ? 1151 TRP   A CE3   1 
ATOM   8220  C  CZ2   . TRP   A  1 1153 ? 19.814  77.967  103.345 1.00 26.01 ? 1151 TRP   A CZ2   1 
ATOM   8221  C  CZ3   . TRP   A  1 1153 ? 18.906  79.882  104.502 1.00 28.11 ? 1151 TRP   A CZ3   1 
ATOM   8222  C  CH2   . TRP   A  1 1153 ? 19.554  78.641  104.509 1.00 27.79 ? 1151 TRP   A CH2   1 
ATOM   8223  N  N     . SER   A  1 1154 ? 15.037  83.084  100.898 1.00 29.16 ? 1152 SER   A N     1 
ATOM   8224  C  CA    . SER   A  1 1154 ? 14.208  84.273  100.780 1.00 27.29 ? 1152 SER   A CA    1 
ATOM   8225  C  C     . SER   A  1 1154 ? 14.701  85.325  101.758 1.00 29.14 ? 1152 SER   A C     1 
ATOM   8226  O  O     . SER   A  1 1154 ? 14.671  85.105  102.974 1.00 25.36 ? 1152 SER   A O     1 
ATOM   8227  C  CB    . SER   A  1 1154 ? 12.744  83.947  101.056 1.00 28.27 ? 1152 SER   A CB    1 
ATOM   8228  O  OG    . SER   A  1 1154 ? 11.939  85.085  100.807 1.00 29.03 ? 1152 SER   A OG    1 
ATOM   8229  N  N     . LYS   A  1 1155 ? 15.160  86.457  101.226 1.00 28.51 ? 1153 LYS   A N     1 
ATOM   8230  C  CA    . LYS   A  1 1155 ? 15.387  87.645  102.037 1.00 28.20 ? 1153 LYS   A CA    1 
ATOM   8231  C  C     . LYS   A  1 1155 ? 14.113  88.471  102.176 1.00 31.71 ? 1153 LYS   A C     1 
ATOM   8232  O  O     . LYS   A  1 1155 ? 13.796  88.951  103.273 1.00 36.02 ? 1153 LYS   A O     1 
ATOM   8233  C  CB    . LYS   A  1 1155 ? 16.506  88.495  101.427 1.00 30.17 ? 1153 LYS   A CB    1 
ATOM   8234  N  N     . ASP   A  1 1156 ? 13.376  88.627  101.083 1.00 29.21 ? 1154 ASP   A N     1 
ATOM   8235  C  CA    . ASP   A  1 1156 ? 12.147  89.414  101.005 1.00 30.17 ? 1154 ASP   A CA    1 
ATOM   8236  C  C     . ASP   A  1 1156 ? 10.991  88.421  100.898 1.00 28.86 ? 1154 ASP   A C     1 
ATOM   8237  O  O     . ASP   A  1 1156 ? 10.617  88.002  99.802  1.00 29.64 ? 1154 ASP   A O     1 
ATOM   8238  C  CB    . ASP   A  1 1156 ? 12.199  90.365  99.797  1.00 28.94 ? 1154 ASP   A CB    1 
ATOM   8239  C  CG    . ASP   A  1 1156 ? 11.000  91.301  99.714  1.00 38.70 ? 1154 ASP   A CG    1 
ATOM   8240  O  OD1   . ASP   A  1 1156 ? 10.007  91.104  100.448 1.00 38.84 ? 1154 ASP   A OD1   1 
ATOM   8241  O  OD2   . ASP   A  1 1156 ? 11.054  92.250  98.897  1.00 37.12 ? 1154 ASP   A OD2   1 
ATOM   8242  N  N     . TRP   A  1 1157 ? 10.419  88.057  102.049 1.00 29.02 ? 1155 TRP   A N     1 
ATOM   8243  C  CA    . TRP   A  1 1157 ? 9.394   87.014  102.074 1.00 27.25 ? 1155 TRP   A CA    1 
ATOM   8244  C  C     . TRP   A  1 1157 ? 8.197   87.384  101.213 1.00 29.70 ? 1155 TRP   A C     1 
ATOM   8245  O  O     . TRP   A  1 1157 ? 7.651   86.532  100.502 1.00 31.58 ? 1155 TRP   A O     1 
ATOM   8246  C  CB    . TRP   A  1 1157 ? 8.930   86.752  103.501 1.00 26.94 ? 1155 TRP   A CB    1 
ATOM   8247  C  CG    . TRP   A  1 1157 ? 9.991   86.323  104.465 1.00 27.70 ? 1155 TRP   A CG    1 
ATOM   8248  C  CD1   . TRP   A  1 1157 ? 11.282  85.981  104.188 1.00 25.44 ? 1155 TRP   A CD1   1 
ATOM   8249  C  CD2   . TRP   A  1 1157 ? 9.836   86.203  105.882 1.00 28.34 ? 1155 TRP   A CD2   1 
ATOM   8250  N  NE1   . TRP   A  1 1157 ? 11.937  85.646  105.351 1.00 28.45 ? 1155 TRP   A NE1   1 
ATOM   8251  C  CE2   . TRP   A  1 1157 ? 11.069  85.778  106.404 1.00 28.15 ? 1155 TRP   A CE2   1 
ATOM   8252  C  CE3   . TRP   A  1 1157 ? 8.766   86.416  106.760 1.00 28.39 ? 1155 TRP   A CE3   1 
ATOM   8253  C  CZ2   . TRP   A  1 1157 ? 11.267  85.563  107.767 1.00 28.98 ? 1155 TRP   A CZ2   1 
ATOM   8254  C  CZ3   . TRP   A  1 1157 ? 8.963   86.203  108.107 1.00 26.07 ? 1155 TRP   A CZ3   1 
ATOM   8255  C  CH2   . TRP   A  1 1157 ? 10.203  85.782  108.598 1.00 25.05 ? 1155 TRP   A CH2   1 
ATOM   8256  N  N     . ALA   A  1 1158 ? 7.763   88.648  101.271 1.00 31.46 ? 1156 ALA   A N     1 
ATOM   8257  C  CA    . ALA   A  1 1158 ? 6.603   89.069  100.490 1.00 34.08 ? 1156 ALA   A CA    1 
ATOM   8258  C  C     . ALA   A  1 1158 ? 6.853   88.988  98.990  1.00 33.51 ? 1156 ALA   A C     1 
ATOM   8259  O  O     . ALA   A  1 1158 ? 5.896   88.883  98.217  1.00 39.02 ? 1156 ALA   A O     1 
ATOM   8260  C  CB    . ALA   A  1 1158 ? 6.194   90.494  100.868 1.00 33.30 ? 1156 ALA   A CB    1 
ATOM   8261  N  N     . ALA   A  1 1159 ? 8.113   89.032  98.561  1.00 33.45 ? 1157 ALA   A N     1 
ATOM   8262  C  CA    . ALA   A  1 1159 ? 8.426   88.939  97.142  1.00 34.86 ? 1157 ALA   A CA    1 
ATOM   8263  C  C     . ALA   A  1 1159 ? 8.450   87.503  96.643  1.00 37.93 ? 1157 ALA   A C     1 
ATOM   8264  O  O     . ALA   A  1 1159 ? 8.254   87.270  95.445  1.00 39.76 ? 1157 ALA   A O     1 
ATOM   8265  C  CB    . ALA   A  1 1159 ? 9.775   89.603  96.856  1.00 31.45 ? 1157 ALA   A CB    1 
ATOM   8266  N  N     . ASP   A  1 1160 ? 8.657   86.538  97.531  1.00 35.51 ? 1158 ASP   A N     1 
ATOM   8267  C  CA    . ASP   A  1 1160 ? 8.889   85.156  97.145  1.00 32.94 ? 1158 ASP   A CA    1 
ATOM   8268  C  C     . ASP   A  1 1160 ? 7.678   84.269  97.385  1.00 33.54 ? 1158 ASP   A C     1 
ATOM   8269  O  O     . ASP   A  1 1160 ? 7.760   83.051  97.199  1.00 33.12 ? 1158 ASP   A O     1 
ATOM   8270  C  CB    . ASP   A  1 1160 ? 10.121  84.633  97.883  1.00 33.79 ? 1158 ASP   A CB    1 
ATOM   8271  C  CG    . ASP   A  1 1160 ? 11.358  85.449  97.561  1.00 38.74 ? 1158 ASP   A CG    1 
ATOM   8272  O  OD1   . ASP   A  1 1160 ? 11.387  86.023  96.450  1.00 43.27 ? 1158 ASP   A OD1   1 
ATOM   8273  O  OD2   . ASP   A  1 1160 ? 12.289  85.538  98.396  1.00 33.50 ? 1158 ASP   A OD2   1 
ATOM   8274  N  N     . GLY   A  1 1161 ? 6.555   84.855  97.781  1.00 32.64 ? 1159 GLY   A N     1 
ATOM   8275  C  CA    . GLY   A  1 1161 ? 5.343   84.112  97.969  1.00 31.00 ? 1159 GLY   A CA    1 
ATOM   8276  C  C     . GLY   A  1 1161 ? 4.550   84.007  96.683  1.00 37.34 ? 1159 GLY   A C     1 
ATOM   8277  O  O     . GLY   A  1 1161 ? 5.009   84.395  95.604  1.00 35.60 ? 1159 GLY   A O     1 
ATOM   8278  N  N     . PRO   A  1 1162 ? 3.326   83.492  96.780  1.00 33.75 ? 1160 PRO   A N     1 
ATOM   8279  C  CA    . PRO   A  1 1162 ? 2.644   83.080  98.009  1.00 30.69 ? 1160 PRO   A CA    1 
ATOM   8280  C  C     . PRO   A  1 1162 ? 3.176   81.785  98.601  1.00 29.25 ? 1160 PRO   A C     1 
ATOM   8281  O  O     . PRO   A  1 1162 ? 3.585   80.847  97.916  1.00 26.81 ? 1160 PRO   A O     1 
ATOM   8282  C  CB    . PRO   A  1 1162 ? 1.186   82.924  97.552  1.00 31.06 ? 1160 PRO   A CB    1 
ATOM   8283  C  CG    . PRO   A  1 1162 ? 1.299   82.519  96.110  1.00 36.39 ? 1160 PRO   A CG    1 
ATOM   8284  C  CD    . PRO   A  1 1162 ? 2.476   83.315  95.590  1.00 34.48 ? 1160 PRO   A CD    1 
ATOM   8285  N  N     . PHE   A  1 1163 ? 3.174   81.722  99.921  1.00 23.44 ? 1161 PHE   A N     1 
ATOM   8286  C  CA    . PHE   A  1 1163 ? 3.434   80.481  100.620 1.00 19.38 ? 1161 PHE   A CA    1 
ATOM   8287  C  C     . PHE   A  1 1163 ? 2.123   79.798  100.982 1.00 21.12 ? 1161 PHE   A C     1 
ATOM   8288  O  O     . PHE   A  1 1163 ? 1.028   80.356  100.849 1.00 26.55 ? 1161 PHE   A O     1 
ATOM   8289  C  CB    . PHE   A  1 1163 ? 4.287   80.756  101.854 1.00 20.56 ? 1161 PHE   A CB    1 
ATOM   8290  C  CG    . PHE   A  1 1163 ? 5.516   81.549  101.534 1.00 22.20 ? 1161 PHE   A CG    1 
ATOM   8291  C  CD1   . PHE   A  1 1163 ? 6.495   81.011  100.713 1.00 23.05 ? 1161 PHE   A CD1   1 
ATOM   8292  C  CD2   . PHE   A  1 1163 ? 5.676   82.836  102.017 1.00 22.82 ? 1161 PHE   A CD2   1 
ATOM   8293  C  CE1   . PHE   A  1 1163 ? 7.623   81.747  100.385 1.00 23.75 ? 1161 PHE   A CE1   1 
ATOM   8294  C  CE2   . PHE   A  1 1163 ? 6.803   83.569  101.707 1.00 24.85 ? 1161 PHE   A CE2   1 
ATOM   8295  C  CZ    . PHE   A  1 1163 ? 7.781   83.024  100.894 1.00 27.40 ? 1161 PHE   A CZ    1 
ATOM   8296  N  N     . ALA   A  1 1164 ? 2.249   78.552  101.411 1.00 20.89 ? 1162 ALA   A N     1 
ATOM   8297  C  CA    . ALA   A  1 1164 ? 1.104   77.733  101.777 1.00 22.51 ? 1162 ALA   A CA    1 
ATOM   8298  C  C     . ALA   A  1 1164 ? 1.153   77.335  103.239 1.00 22.09 ? 1162 ALA   A C     1 
ATOM   8299  O  O     . ALA   A  1 1164 ? 0.319   76.543  103.685 1.00 23.64 ? 1162 ALA   A O     1 
ATOM   8300  C  CB    . ALA   A  1 1164 ? 1.046   76.488  100.889 1.00 22.69 ? 1162 ALA   A CB    1 
ATOM   8301  N  N     . GLY   A  1 1165 ? 2.118   77.860  103.984 1.00 18.13 ? 1163 GLY   A N     1 
ATOM   8302  C  CA    . GLY   A  1 1165 ? 2.280   77.537  105.383 1.00 17.93 ? 1163 GLY   A CA    1 
ATOM   8303  C  C     . GLY   A  1 1165 ? 3.624   78.046  105.841 1.00 19.87 ? 1163 GLY   A C     1 
ATOM   8304  O  O     . GLY   A  1 1165 ? 4.430   78.544  105.050 1.00 19.41 ? 1163 GLY   A O     1 
ATOM   8305  N  N     . ALA   A  1 1166 ? 3.865   77.919  107.143 1.00 18.89 ? 1164 ALA   A N     1 
ATOM   8306  C  CA    . ALA   A  1 1166 ? 5.134   78.382  107.685 1.00 19.59 ? 1164 ALA   A CA    1 
ATOM   8307  C  C     . ALA   A  1 1166 ? 5.522   77.530  108.884 1.00 19.78 ? 1164 ALA   A C     1 
ATOM   8308  O  O     . ALA   A  1 1166 ? 4.657   77.099  109.651 1.00 21.86 ? 1164 ALA   A O     1 
ATOM   8309  C  CB    . ALA   A  1 1166 ? 5.067   79.860  108.085 1.00 20.99 ? 1164 ALA   A CB    1 
ATOM   8310  N  N     . LEU   A  1 1167 ? 6.828   77.286  109.025 1.00 19.34 ? 1165 LEU   A N     1 
ATOM   8311  C  CA    . LEU   A  1 1167 ? 7.401   76.653  110.207 1.00 19.07 ? 1165 LEU   A CA    1 
ATOM   8312  C  C     . LEU   A  1 1167 ? 8.388   77.629  110.821 1.00 20.90 ? 1165 LEU   A C     1 
ATOM   8313  O  O     . LEU   A  1 1167 ? 9.244   78.172  110.116 1.00 21.35 ? 1165 LEU   A O     1 
ATOM   8314  C  CB    . LEU   A  1 1167 ? 8.110   75.341  109.867 1.00 19.03 ? 1165 LEU   A CB    1 
ATOM   8315  C  CG    . LEU   A  1 1167 ? 7.242   74.304  109.152 1.00 20.39 ? 1165 LEU   A CG    1 
ATOM   8316  C  CD1   . LEU   A  1 1167 ? 8.084   73.112  108.762 1.00 18.77 ? 1165 LEU   A CD1   1 
ATOM   8317  C  CD2   . LEU   A  1 1167 ? 6.106   73.864  110.045 1.00 19.88 ? 1165 LEU   A CD2   1 
ATOM   8318  N  N     . VAL   A  1 1168 ? 8.259   77.861  112.123 1.00 19.55 ? 1166 VAL   A N     1 
ATOM   8319  C  CA    . VAL   A  1 1168 ? 9.044   78.873  112.815 1.00 19.90 ? 1166 VAL   A CA    1 
ATOM   8320  C  C     . VAL   A  1 1168 ? 9.732   78.219  113.996 1.00 21.02 ? 1166 VAL   A C     1 
ATOM   8321  O  O     . VAL   A  1 1168 ? 9.127   77.412  114.706 1.00 20.61 ? 1166 VAL   A O     1 
ATOM   8322  C  CB    . VAL   A  1 1168 ? 8.167   80.053  113.284 1.00 20.07 ? 1166 VAL   A CB    1 
ATOM   8323  C  CG1   . VAL   A  1 1168 ? 9.022   81.088  114.030 1.00 22.13 ? 1166 VAL   A CG1   1 
ATOM   8324  C  CG2   . VAL   A  1 1168 ? 7.434   80.674  112.081 1.00 23.20 ? 1166 VAL   A CG2   1 
ATOM   8325  N  N     . GLU   A  1 1169 ? 10.998  78.565  114.205 1.00 21.14 ? 1167 GLU   A N     1 
ATOM   8326  C  CA    . GLU   A  1 1169 ? 11.744  78.146  115.383 1.00 21.33 ? 1167 GLU   A CA    1 
ATOM   8327  C  C     . GLU   A  1 1169 ? 12.217  79.375  116.143 1.00 23.96 ? 1167 GLU   A C     1 
ATOM   8328  O  O     . GLU   A  1 1169 ? 12.711  80.336  115.543 1.00 22.02 ? 1167 GLU   A O     1 
ATOM   8329  C  CB    . GLU   A  1 1169 ? 12.941  77.288  114.994 1.00 20.76 ? 1167 GLU   A CB    1 
ATOM   8330  C  CG    . GLU   A  1 1169 ? 13.828  76.865  116.152 1.00 21.74 ? 1167 GLU   A CG    1 
ATOM   8331  C  CD    . GLU   A  1 1169 ? 15.172  76.355  115.670 1.00 21.67 ? 1167 GLU   A CD    1 
ATOM   8332  O  OE1   . GLU   A  1 1169 ? 15.457  76.510  114.466 1.00 23.84 ? 1167 GLU   A OE1   1 
ATOM   8333  O  OE2   . GLU   A  1 1169 ? 15.941  75.806  116.483 1.00 25.66 ? 1167 GLU   A OE2   1 
ATOM   8334  N  N     . GLY   A  1 1170 ? 12.062  79.349  117.456 1.00 22.92 ? 1168 GLY   A N     1 
ATOM   8335  C  CA    . GLY   A  1 1170 ? 12.596  80.420  118.273 1.00 24.90 ? 1168 GLY   A CA    1 
ATOM   8336  C  C     . GLY   A  1 1170 ? 11.960  80.428  119.643 1.00 26.25 ? 1168 GLY   A C     1 
ATOM   8337  O  O     . GLY   A  1 1170 ? 11.078  79.628  119.953 1.00 26.17 ? 1168 GLY   A O     1 
ATOM   8338  N  N     . ASP   A  1 1171 ? 12.431  81.364  120.467 1.00 26.91 ? 1169 ASP   A N     1 
ATOM   8339  C  CA    . ASP   A  1 1171 ? 11.782  81.594  121.745 1.00 25.68 ? 1169 ASP   A CA    1 
ATOM   8340  C  C     . ASP   A  1 1171 ? 10.515  82.419  121.526 1.00 29.22 ? 1169 ASP   A C     1 
ATOM   8341  O  O     . ASP   A  1 1171 ? 10.181  82.811  120.402 1.00 27.07 ? 1169 ASP   A O     1 
ATOM   8342  C  CB    . ASP   A  1 1171 ? 12.753  82.240  122.740 1.00 28.16 ? 1169 ASP   A CB    1 
ATOM   8343  C  CG    . ASP   A  1 1171 ? 13.232  83.623  122.320 1.00 30.68 ? 1169 ASP   A CG    1 
ATOM   8344  O  OD1   . ASP   A  1 1171 ? 12.666  84.242  121.394 1.00 29.08 ? 1169 ASP   A OD1   1 
ATOM   8345  O  OD2   . ASP   A  1 1171 ? 14.200  84.111  122.943 1.00 34.36 ? 1169 ASP   A OD2   1 
ATOM   8346  N  N     . ALA   A  1 1172 ? 9.797   82.686  122.617 1.00 28.13 ? 1170 ALA   A N     1 
ATOM   8347  C  CA    . ALA   A  1 1172 ? 8.479   83.306  122.501 1.00 29.41 ? 1170 ALA   A CA    1 
ATOM   8348  C  C     . ALA   A  1 1172 ? 8.548   84.662  121.806 1.00 27.33 ? 1170 ALA   A C     1 
ATOM   8349  O  O     . ALA   A  1 1172 ? 7.696   84.975  120.965 1.00 26.86 ? 1170 ALA   A O     1 
ATOM   8350  C  CB    . ALA   A  1 1172 ? 7.840   83.439  123.884 1.00 32.40 ? 1170 ALA   A CB    1 
ATOM   8351  N  N     . GLU   A  1 1173 ? 9.559   85.478  122.131 1.00 29.02 ? 1171 GLU   A N     1 
ATOM   8352  C  CA    . GLU   A  1 1173 ? 9.681   86.788  121.492 1.00 30.51 ? 1171 GLU   A CA    1 
ATOM   8353  C  C     . GLU   A  1 1173 ? 9.941   86.648  119.996 1.00 29.72 ? 1171 GLU   A C     1 
ATOM   8354  O  O     . GLU   A  1 1173 ? 9.360   87.379  119.180 1.00 29.15 ? 1171 GLU   A O     1 
ATOM   8355  C  CB    . GLU   A  1 1173 ? 10.795  87.607  122.160 1.00 28.72 ? 1171 GLU   A CB    1 
ATOM   8356  N  N     . ARG   A  1 1174 ? 10.801  85.699  119.617 1.00 26.76 ? 1172 ARG   A N     1 
ATOM   8357  C  CA    . ARG   A  1 1174 ? 11.093  85.481  118.203 1.00 25.92 ? 1172 ARG   A CA    1 
ATOM   8358  C  C     . ARG   A  1 1174 ? 9.867   84.964  117.461 1.00 26.11 ? 1172 ARG   A C     1 
ATOM   8359  O  O     . ARG   A  1 1174 ? 9.564   85.422  116.349 1.00 24.26 ? 1172 ARG   A O     1 
ATOM   8360  C  CB    . ARG   A  1 1174 ? 12.266  84.506  118.062 1.00 25.72 ? 1172 ARG   A CB    1 
ATOM   8361  C  CG    . ARG   A  1 1174 ? 12.595  84.104  116.621 1.00 25.54 ? 1172 ARG   A CG    1 
ATOM   8362  C  CD    . ARG   A  1 1174 ? 13.025  85.315  115.799 1.00 30.95 ? 1172 ARG   A CD    1 
ATOM   8363  N  NE    . ARG   A  1 1174 ? 13.407  84.945  114.440 1.00 30.32 ? 1172 ARG   A NE    1 
ATOM   8364  C  CZ    . ARG   A  1 1174 ? 13.504  85.800  113.430 1.00 31.05 ? 1172 ARG   A CZ    1 
ATOM   8365  N  NH1   . ARG   A  1 1174 ? 13.256  87.091  113.588 1.00 28.52 ? 1172 ARG   A NH1   1 
ATOM   8366  N  NH2   . ARG   A  1 1174 ? 13.850  85.349  112.232 1.00 25.03 ? 1172 ARG   A NH2   1 
ATOM   8367  N  N     . ILE   A  1 1175 ? 9.155   84.008  118.061 1.00 24.71 ? 1173 ILE   A N     1 
ATOM   8368  C  CA    . ILE   A  1 1175 ? 7.943   83.473  117.443 1.00 24.24 ? 1173 ILE   A CA    1 
ATOM   8369  C  C     . ILE   A  1 1175 ? 6.921   84.583  117.236 1.00 25.40 ? 1173 ILE   A C     1 
ATOM   8370  O  O     . ILE   A  1 1175 ? 6.305   84.689  116.169 1.00 23.30 ? 1173 ILE   A O     1 
ATOM   8371  C  CB    . ILE   A  1 1175 ? 7.368   82.329  118.301 1.00 24.12 ? 1173 ILE   A CB    1 
ATOM   8372  C  CG1   . ILE   A  1 1175 ? 8.292   81.105  118.286 1.00 24.60 ? 1173 ILE   A CG1   1 
ATOM   8373  C  CG2   . ILE   A  1 1175 ? 5.956   81.964  117.843 1.00 21.81 ? 1173 ILE   A CG2   1 
ATOM   8374  C  CD1   . ILE   A  1 1175 ? 7.890   80.041  119.289 1.00 23.53 ? 1173 ILE   A CD1   1 
ATOM   8375  N  N     . ARG   A  1 1176 ? 6.746   85.446  118.246 1.00 26.42 ? 1174 ARG   A N     1 
ATOM   8376  C  CA    . ARG   A  1 1176 ? 5.775   86.531  118.138 1.00 25.59 ? 1174 ARG   A CA    1 
ATOM   8377  C  C     . ARG   A  1 1176 ? 6.148   87.473  117.005 1.00 25.34 ? 1174 ARG   A C     1 
ATOM   8378  O  O     . ARG   A  1 1176 ? 5.304   87.838  116.178 1.00 28.23 ? 1174 ARG   A O     1 
ATOM   8379  C  CB    . ARG   A  1 1176 ? 5.680   87.291  119.469 1.00 24.93 ? 1174 ARG   A CB    1 
ATOM   8380  C  CG    . ARG   A  1 1176 ? 4.422   88.141  119.589 1.00 32.65 ? 1174 ARG   A CG    1 
ATOM   8381  C  CD    . ARG   A  1 1176 ? 4.449   89.055  120.819 1.00 34.34 ? 1174 ARG   A CD    1 
ATOM   8382  N  NE    . ARG   A  1 1176 ? 4.864   88.354  122.031 1.00 41.28 ? 1174 ARG   A NE    1 
ATOM   8383  C  CZ    . ARG   A  1 1176 ? 4.038   87.743  122.874 1.00 45.10 ? 1174 ARG   A CZ    1 
ATOM   8384  N  NH1   . ARG   A  1 1176 ? 2.730   87.706  122.660 1.00 42.81 ? 1174 ARG   A NH1   1 
ATOM   8385  N  NH2   . ARG   A  1 1176 ? 4.534   87.158  123.962 1.00 40.22 ? 1174 ARG   A NH2   1 
ATOM   8386  N  N     . ALA   A  1 1177 ? 7.428   87.847  116.934 1.00 23.54 ? 1175 ALA   A N     1 
ATOM   8387  C  CA    . ALA   A  1 1177 ? 7.889   88.762  115.896 1.00 27.61 ? 1175 ALA   A CA    1 
ATOM   8388  C  C     . ALA   A  1 1177 ? 7.756   88.141  114.514 1.00 25.44 ? 1175 ALA   A C     1 
ATOM   8389  O  O     . ALA   A  1 1177 ? 7.379   88.821  113.554 1.00 25.33 ? 1175 ALA   A O     1 
ATOM   8390  C  CB    . ALA   A  1 1177 ? 9.341   89.169  116.157 1.00 27.93 ? 1175 ALA   A CB    1 
ATOM   8391  N  N     . VAL   A  1 1178 ? 8.081   86.855  114.387 1.00 25.23 ? 1176 VAL   A N     1 
ATOM   8392  C  CA    . VAL   A  1 1178 ? 7.947   86.204  113.088 1.00 24.38 ? 1176 VAL   A CA    1 
ATOM   8393  C  C     . VAL   A  1 1178 ? 6.479   86.077  112.712 1.00 25.52 ? 1176 VAL   A C     1 
ATOM   8394  O  O     . VAL   A  1 1178 ? 6.095   86.311  111.560 1.00 25.40 ? 1176 VAL   A O     1 
ATOM   8395  C  CB    . VAL   A  1 1178 ? 8.642   84.834  113.085 1.00 22.58 ? 1176 VAL   A CB    1 
ATOM   8396  C  CG1   . VAL   A  1 1178 ? 8.326   84.101  111.773 1.00 20.49 ? 1176 VAL   A CG1   1 
ATOM   8397  C  CG2   . VAL   A  1 1178 ? 10.144  84.996  113.272 1.00 24.33 ? 1176 VAL   A CG2   1 
ATOM   8398  N  N     . ASN   A  1 1179 ? 5.641   85.699  113.676 1.00 25.43 ? 1177 ASN   A N     1 
ATOM   8399  C  CA    . ASN   A  1 1179 ? 4.211   85.549  113.419 1.00 26.17 ? 1177 ASN   A CA    1 
ATOM   8400  C  C     . ASN   A  1 1179 ? 3.600   86.869  112.956 1.00 27.64 ? 1177 ASN   A C     1 
ATOM   8401  O  O     . ASN   A  1 1179 ? 2.708   86.885  112.101 1.00 29.31 ? 1177 ASN   A O     1 
ATOM   8402  C  CB    . ASN   A  1 1179 ? 3.531   85.028  114.686 1.00 28.91 ? 1177 ASN   A CB    1 
ATOM   8403  C  CG    . ASN   A  1 1179 ? 2.226   84.299  114.418 1.00 34.02 ? 1177 ASN   A CG    1 
ATOM   8404  O  OD1   . ASN   A  1 1179 ? 1.990   83.771  113.328 1.00 36.31 ? 1177 ASN   A OD1   1 
ATOM   8405  N  ND2   . ASN   A  1 1179 ? 1.360   84.269  115.432 1.00 36.02 ? 1177 ASN   A ND2   1 
ATOM   8406  N  N     . LYS   A  1 1180 ? 4.089   87.989  113.493 1.00 24.97 ? 1178 LYS   A N     1 
ATOM   8407  C  CA    . LYS   A  1 1180 ? 3.617   89.295  113.046 1.00 30.43 ? 1178 LYS   A CA    1 
ATOM   8408  C  C     . LYS   A  1 1180 ? 4.101   89.600  111.634 1.00 27.08 ? 1178 LYS   A C     1 
ATOM   8409  O  O     . LYS   A  1 1180 ? 3.348   90.143  110.821 1.00 29.89 ? 1178 LYS   A O     1 
ATOM   8410  C  CB    . LYS   A  1 1180 ? 4.074   90.387  114.026 1.00 28.59 ? 1178 LYS   A CB    1 
ATOM   8411  C  CG    . LYS   A  1 1180 ? 3.333   90.372  115.359 1.00 31.21 ? 1178 LYS   A CG    1 
ATOM   8412  C  CD    . LYS   A  1 1180 ? 4.032   91.245  116.410 1.00 30.54 ? 1178 LYS   A CD    1 
ATOM   8413  C  CE    . LYS   A  1 1180 ? 4.209   92.690  115.942 1.00 41.49 ? 1178 LYS   A CE    1 
ATOM   8414  N  NZ    . LYS   A  1 1180 ? 5.285   93.425  116.700 1.00 44.08 ? 1178 LYS   A NZ    1 
ATOM   8415  N  N     . ALA   A  1 1181 ? 5.358   89.259  111.323 1.00 21.60 ? 1179 ALA   A N     1 
ATOM   8416  C  CA    . ALA   A  1 1181 ? 5.869   89.471  109.974 1.00 25.71 ? 1179 ALA   A CA    1 
ATOM   8417  C  C     . ALA   A  1 1181 ? 5.135   88.604  108.964 1.00 27.28 ? 1179 ALA   A C     1 
ATOM   8418  O  O     . ALA   A  1 1181 ? 4.888   89.034  107.831 1.00 26.16 ? 1179 ALA   A O     1 
ATOM   8419  C  CB    . ALA   A  1 1181 ? 7.371   89.189  109.920 1.00 23.69 ? 1179 ALA   A CB    1 
ATOM   8420  N  N     . ILE   A  1 1182 ? 4.782   87.377  109.351 1.00 24.74 ? 1180 ILE   A N     1 
ATOM   8421  C  CA    . ILE   A  1 1182 ? 4.088   86.491  108.417 1.00 22.32 ? 1180 ILE   A CA    1 
ATOM   8422  C  C     . ILE   A  1 1182 ? 2.675   86.994  108.161 1.00 24.14 ? 1180 ILE   A C     1 
ATOM   8423  O  O     . ILE   A  1 1182 ? 2.157   86.897  107.039 1.00 24.34 ? 1180 ILE   A O     1 
ATOM   8424  C  CB    . ILE   A  1 1182 ? 4.096   85.047  108.954 1.00 25.39 ? 1180 ILE   A CB    1 
ATOM   8425  C  CG1   . ILE   A  1 1182 ? 5.506   84.463  108.900 1.00 25.96 ? 1180 ILE   A CG1   1 
ATOM   8426  C  CG2   . ILE   A  1 1182 ? 3.093   84.171  108.203 1.00 26.81 ? 1180 ILE   A CG2   1 
ATOM   8427  C  CD1   . ILE   A  1 1182 ? 5.639   83.112  109.621 1.00 26.21 ? 1180 ILE   A CD1   1 
ATOM   8428  N  N     . ALA   A  1 1183 ? 2.023   87.536  109.198 1.00 22.55 ? 1181 ALA   A N     1 
ATOM   8429  C  CA    . ALA   A  1 1183 ? 0.673   88.052  109.013 1.00 28.88 ? 1181 ALA   A CA    1 
ATOM   8430  C  C     . ALA   A  1 1183 ? 0.663   89.226  108.048 1.00 31.58 ? 1181 ALA   A C     1 
ATOM   8431  O  O     . ALA   A  1 1183 ? -0.355  89.485  107.396 1.00 28.96 ? 1181 ALA   A O     1 
ATOM   8432  C  CB    . ALA   A  1 1183 ? 0.067   88.458  110.356 1.00 24.19 ? 1181 ALA   A CB    1 
ATOM   8433  N  N     . ALA   A  1 1184 ? 1.788   89.933  107.931 1.00 25.15 ? 1182 ALA   A N     1 
ATOM   8434  C  CA    . ALA   A  1 1184 ? 1.891   91.059  107.013 1.00 29.41 ? 1182 ALA   A CA    1 
ATOM   8435  C  C     . ALA   A  1 1184 ? 2.170   90.638  105.581 1.00 30.19 ? 1182 ALA   A C     1 
ATOM   8436  O  O     . ALA   A  1 1184 ? 2.199   91.504  104.700 1.00 29.65 ? 1182 ALA   A O     1 
ATOM   8437  C  CB    . ALA   A  1 1184 ? 2.985   92.030  107.473 1.00 27.79 ? 1182 ALA   A CB    1 
ATOM   8438  N  N     . LEU   A  1 1185 ? 2.385   89.354  105.325 1.00 28.35 ? 1183 LEU   A N     1 
ATOM   8439  C  CA    . LEU   A  1 1185 ? 2.645   88.922  103.964 1.00 29.21 ? 1183 LEU   A CA    1 
ATOM   8440  C  C     . LEU   A  1 1185 ? 1.365   89.042  103.147 1.00 31.99 ? 1183 LEU   A C     1 
ATOM   8441  O  O     . LEU   A  1 1185 ? 0.293   88.634  103.617 1.00 29.05 ? 1183 LEU   A O     1 
ATOM   8442  C  CB    . LEU   A  1 1185 ? 3.167   87.489  103.937 1.00 23.85 ? 1183 LEU   A CB    1 
ATOM   8443  C  CG    . LEU   A  1 1185 ? 4.510   87.259  104.629 1.00 28.26 ? 1183 LEU   A CG    1 
ATOM   8444  C  CD1   . LEU   A  1 1185 ? 4.878   85.787  104.593 1.00 24.79 ? 1183 LEU   A CD1   1 
ATOM   8445  C  CD2   . LEU   A  1 1185 ? 5.614   88.107  103.990 1.00 25.88 ? 1183 LEU   A CD2   1 
ATOM   8446  N  N     . PRO   A  1 1186 ? 1.424   89.606  101.943 1.00 30.16 ? 1184 PRO   A N     1 
ATOM   8447  C  CA    . PRO   A  1 1186 ? 0.222   89.678  101.107 1.00 31.85 ? 1184 PRO   A CA    1 
ATOM   8448  C  C     . PRO   A  1 1186 ? -0.254  88.297  100.695 1.00 27.57 ? 1184 PRO   A C     1 
ATOM   8449  O  O     . PRO   A  1 1186 ? 0.526   87.352  100.565 1.00 28.01 ? 1184 PRO   A O     1 
ATOM   8450  C  CB    . PRO   A  1 1186 ? 0.678   90.487  99.887  1.00 33.97 ? 1184 PRO   A CB    1 
ATOM   8451  C  CG    . PRO   A  1 1186 ? 2.172   90.333  99.860  1.00 40.93 ? 1184 PRO   A CG    1 
ATOM   8452  C  CD    . PRO   A  1 1186 ? 2.590   90.239  101.304 1.00 35.15 ? 1184 PRO   A CD    1 
ATOM   8453  N  N     . GLY   A  1 1187 ? -1.557  88.191  100.485 1.00 30.43 ? 1185 GLY   A N     1 
ATOM   8454  C  CA    . GLY   A  1 1187 ? -2.127  86.989  99.938  1.00 30.87 ? 1185 GLY   A CA    1 
ATOM   8455  C  C     . GLY   A  1 1187 ? -2.760  86.117  100.997 1.00 28.29 ? 1185 GLY   A C     1 
ATOM   8456  O  O     . GLY   A  1 1187 ? -3.472  86.595  101.887 1.00 27.60 ? 1185 GLY   A O     1 
ATOM   8457  N  N     . PRO   A  1 1188 ? -2.495  84.813  100.924 1.00 25.49 ? 1186 PRO   A N     1 
ATOM   8458  C  CA    . PRO   A  1 1188 ? -3.230  83.855  101.758 1.00 26.73 ? 1186 PRO   A CA    1 
ATOM   8459  C  C     . PRO   A  1 1188 ? -2.855  83.951  103.227 1.00 26.82 ? 1186 PRO   A C     1 
ATOM   8460  O  O     . PRO   A  1 1188 ? -1.733  84.310  103.588 1.00 22.94 ? 1186 PRO   A O     1 
ATOM   8461  C  CB    . PRO   A  1 1188 ? -2.816  82.498  101.182 1.00 28.40 ? 1186 PRO   A CB    1 
ATOM   8462  C  CG    . PRO   A  1 1188 ? -1.451  82.743  100.626 1.00 31.40 ? 1186 PRO   A CG    1 
ATOM   8463  C  CD    . PRO   A  1 1188 ? -1.462  84.163  100.103 1.00 27.05 ? 1186 PRO   A CD    1 
ATOM   8464  N  N     . LEU   A  1 1189 ? -3.816  83.606  104.080 1.00 21.80 ? 1187 LEU   A N     1 
ATOM   8465  C  CA    . LEU   A  1 1189 ? -3.538  83.468  105.509 1.00 24.07 ? 1187 LEU   A CA    1 
ATOM   8466  C  C     . LEU   A  1 1189 ? -2.735  82.197  105.726 1.00 26.69 ? 1187 LEU   A C     1 
ATOM   8467  O  O     . LEU   A  1 1189 ? -3.229  81.096  105.468 1.00 34.39 ? 1187 LEU   A O     1 
ATOM   8468  C  CB    . LEU   A  1 1189 ? -4.832  83.431  106.314 1.00 26.77 ? 1187 LEU   A CB    1 
ATOM   8469  C  CG    . LEU   A  1 1189 ? -5.482  84.762  106.678 1.00 28.45 ? 1187 LEU   A CG    1 
ATOM   8470  C  CD1   . LEU   A  1 1189 ? -5.941  85.515  105.438 1.00 33.13 ? 1187 LEU   A CD1   1 
ATOM   8471  C  CD2   . LEU   A  1 1189 ? -6.648  84.514  107.623 1.00 28.69 ? 1187 LEU   A CD2   1 
ATOM   8472  N  N     . LEU   A  1 1190 ? -1.500  82.334  106.196 1.00 23.92 ? 1188 LEU   A N     1 
ATOM   8473  C  CA    . LEU   A  1 1190 ? -0.632  81.177  106.340 1.00 25.56 ? 1188 LEU   A CA    1 
ATOM   8474  C  C     . LEU   A  1 1190 ? -0.912  80.466  107.654 1.00 26.82 ? 1188 LEU   A C     1 
ATOM   8475  O  O     . LEU   A  1 1190 ? -0.991  81.102  108.712 1.00 23.16 ? 1188 LEU   A O     1 
ATOM   8476  C  CB    . LEU   A  1 1190 ? 0.835   81.592  106.279 1.00 25.41 ? 1188 LEU   A CB    1 
ATOM   8477  C  CG    . LEU   A  1 1190 ? 1.284   82.254  104.979 1.00 26.34 ? 1188 LEU   A CG    1 
ATOM   8478  C  CD1   . LEU   A  1 1190 ? 2.809   82.298  104.932 1.00 26.79 ? 1188 LEU   A CD1   1 
ATOM   8479  C  CD2   . LEU   A  1 1190 ? 0.745   81.477  103.793 1.00 26.09 ? 1188 LEU   A CD2   1 
ATOM   8480  N  N     . LEU   A  1 1191 ? -1.060  79.147  107.582 1.00 22.67 ? 1189 LEU   A N     1 
ATOM   8481  C  CA    . LEU   A  1 1191 ? -1.094  78.317  108.778 1.00 24.27 ? 1189 LEU   A CA    1 
ATOM   8482  C  C     . LEU   A  1 1191 ? 0.335   78.193  109.289 1.00 25.29 ? 1189 LEU   A C     1 
ATOM   8483  O  O     . LEU   A  1 1191 ? 1.172   77.527  108.662 1.00 23.62 ? 1189 LEU   A O     1 
ATOM   8484  C  CB    . LEU   A  1 1191 ? -1.706  76.956  108.463 1.00 23.63 ? 1189 LEU   A CB    1 
ATOM   8485  C  CG    . LEU   A  1 1191 ? -2.320  76.181  109.632 1.00 26.61 ? 1189 LEU   A CG    1 
ATOM   8486  C  CD1   . LEU   A  1 1191 ? -3.189  75.042  109.106 1.00 24.35 ? 1189 LEU   A CD1   1 
ATOM   8487  C  CD2   . LEU   A  1 1191 ? -1.240  75.643  110.562 1.00 22.72 ? 1189 LEU   A CD2   1 
ATOM   8488  N  N     . VAL   A  1 1192 ? 0.619   78.849  110.419 1.00 24.44 ? 1190 VAL   A N     1 
ATOM   8489  C  CA    . VAL   A  1 1192 ? 1.958   78.910  110.990 1.00 23.57 ? 1190 VAL   A CA    1 
ATOM   8490  C  C     . VAL   A  1 1192 ? 2.059   77.919  112.142 1.00 24.03 ? 1190 VAL   A C     1 
ATOM   8491  O  O     . VAL   A  1 1192 ? 1.144   77.812  112.970 1.00 24.27 ? 1190 VAL   A O     1 
ATOM   8492  C  CB    . VAL   A  1 1192 ? 2.289   80.336  111.471 1.00 23.76 ? 1190 VAL   A CB    1 
ATOM   8493  C  CG1   . VAL   A  1 1192 ? 3.726   80.395  111.972 1.00 26.47 ? 1190 VAL   A CG1   1 
ATOM   8494  C  CG2   . VAL   A  1 1192 ? 2.091   81.338  110.349 1.00 24.58 ? 1190 VAL   A CG2   1 
ATOM   8495  N  N     . GLN   A  1 1193 ? 3.171   77.194  112.199 1.00 22.03 ? 1191 GLN   A N     1 
ATOM   8496  C  CA    . GLN   A  1 1193 ? 3.500   76.360  113.345 1.00 18.79 ? 1191 GLN   A CA    1 
ATOM   8497  C  C     . GLN   A  1 1193 ? 4.816   76.823  113.939 1.00 20.29 ? 1191 GLN   A C     1 
ATOM   8498  O  O     . GLN   A  1 1193 ? 5.772   77.101  113.212 1.00 20.10 ? 1191 GLN   A O     1 
ATOM   8499  C  CB    . GLN   A  1 1193 ? 3.631   74.903  112.975 1.00 19.29 ? 1191 GLN   A CB    1 
ATOM   8500  C  CG    . GLN   A  1 1193 ? 2.342   74.273  112.506 1.00 19.90 ? 1191 GLN   A CG    1 
ATOM   8501  C  CD    . GLN   A  1 1193 ? 2.508   72.787  112.345 1.00 22.20 ? 1191 GLN   A CD    1 
ATOM   8502  O  OE1   . GLN   A  1 1193 ? 2.542   72.052  113.328 1.00 24.26 ? 1191 GLN   A OE1   1 
ATOM   8503  N  NE2   . GLN   A  1 1193 ? 2.601   72.330  111.104 1.00 21.51 ? 1191 GLN   A NE2   1 
ATOM   8504  N  N     . ALA   A  1 1194 ? 4.880   76.867  115.261 1.00 19.77 ? 1192 ALA   A N     1 
ATOM   8505  C  CA    . ALA   A  1 1194 ? 6.069   77.360  115.926 1.00 22.20 ? 1192 ALA   A CA    1 
ATOM   8506  C  C     . ALA   A  1 1194 ? 6.505   76.383  117.004 1.00 20.12 ? 1192 ALA   A C     1 
ATOM   8507  O  O     . ALA   A  1 1194 ? 5.683   75.696  117.619 1.00 21.25 ? 1192 ALA   A O     1 
ATOM   8508  C  CB    . ALA   A  1 1194 ? 5.825   78.743  116.534 1.00 19.87 ? 1192 ALA   A CB    1 
ATOM   8509  N  N     . ALA   A  1 1195 ? 7.815   76.320  117.206 1.00 20.94 ? 1193 ALA   A N     1 
ATOM   8510  C  CA    . ALA   A  1 1195 ? 8.404   75.483  118.233 1.00 22.09 ? 1193 ALA   A CA    1 
ATOM   8511  C  C     . ALA   A  1 1195 ? 9.700   76.137  118.690 1.00 26.18 ? 1193 ALA   A C     1 
ATOM   8512  O  O     . ALA   A  1 1195 ? 10.380  76.811  117.910 1.00 25.54 ? 1193 ALA   A O     1 
ATOM   8513  C  CB    . ALA   A  1 1195 ? 8.671   74.064  117.716 1.00 23.17 ? 1193 ALA   A CB    1 
ATOM   8514  N  N     . SER   A  1 1196 ? 10.032  75.948  119.963 1.00 21.20 ? 1194 SER   A N     1 
ATOM   8515  C  CA    . SER   A  1 1196 ? 11.349  76.335  120.430 1.00 21.37 ? 1194 SER   A CA    1 
ATOM   8516  C  C     . SER   A  1 1196 ? 12.385  75.313  119.971 1.00 22.08 ? 1194 SER   A C     1 
ATOM   8517  O  O     . SER   A  1 1196 ? 12.056  74.189  119.599 1.00 21.34 ? 1194 SER   A O     1 
ATOM   8518  C  CB    . SER   A  1 1196 ? 11.378  76.430  121.952 1.00 30.48 ? 1194 SER   A CB    1 
ATOM   8519  O  OG    . SER   A  1 1196 ? 11.250  75.135  122.514 1.00 26.39 ? 1194 SER   A OG    1 
ATOM   8520  N  N     . SER   A  1 1197 ? 13.652  75.710  120.014 1.00 21.42 ? 1195 SER   A N     1 
ATOM   8521  C  CA    . SER   A  1 1197 ? 14.720  74.757  119.719 1.00 23.00 ? 1195 SER   A CA    1 
ATOM   8522  C  C     . SER   A  1 1197 ? 14.643  73.547  120.638 1.00 24.80 ? 1195 SER   A C     1 
ATOM   8523  O  O     . SER   A  1 1197 ? 14.853  72.409  120.201 1.00 23.32 ? 1195 SER   A O     1 
ATOM   8524  C  CB    . SER   A  1 1197 ? 16.081  75.437  119.845 1.00 25.06 ? 1195 SER   A CB    1 
ATOM   8525  O  OG    . SER   A  1 1197 ? 16.150  76.583  119.018 1.00 27.27 ? 1195 SER   A OG    1 
ATOM   8526  N  N     . GLY   A  1 1198 ? 14.353  73.773  121.920 1.00 26.25 ? 1196 GLY   A N     1 
ATOM   8527  C  CA    . GLY   A  1 1198 ? 14.260  72.661  122.851 1.00 24.19 ? 1196 GLY   A CA    1 
ATOM   8528  C  C     . GLY   A  1 1198 ? 13.074  71.766  122.567 1.00 25.54 ? 1196 GLY   A C     1 
ATOM   8529  O  O     . GLY   A  1 1198 ? 13.160  70.544  122.722 1.00 23.62 ? 1196 GLY   A O     1 
ATOM   8530  N  N     . GLU   A  1 1199 ? 11.957  72.353  122.132 1.00 24.19 ? 1197 GLU   A N     1 
ATOM   8531  C  CA    . GLU   A  1 1199 ? 10.813  71.535  121.751 1.00 25.84 ? 1197 GLU   A CA    1 
ATOM   8532  C  C     . GLU   A  1 1199 ? 11.130  70.690  120.524 1.00 27.08 ? 1197 GLU   A C     1 
ATOM   8533  O  O     . GLU   A  1 1199 ? 10.696  69.537  120.426 1.00 21.52 ? 1197 GLU   A O     1 
ATOM   8534  C  CB    . GLU   A  1 1199 ? 9.597   72.419  121.493 1.00 25.54 ? 1197 GLU   A CB    1 
ATOM   8535  C  CG    . GLU   A  1 1199 ? 8.311   71.640  121.269 1.00 31.50 ? 1197 GLU   A CG    1 
ATOM   8536  C  CD    . GLU   A  1 1199 ? 7.730   71.045  122.549 1.00 36.71 ? 1197 GLU   A CD    1 
ATOM   8537  O  OE1   . GLU   A  1 1199 ? 8.295   71.278  123.643 1.00 34.46 ? 1197 GLU   A OE1   1 
ATOM   8538  O  OE2   . GLU   A  1 1199 ? 6.694   70.345  122.455 1.00 40.33 ? 1197 GLU   A OE2   1 
ATOM   8539  N  N     . ILE   A  1 1200 ? 11.873  71.252  119.569 1.00 21.73 ? 1198 ILE   A N     1 
ATOM   8540  C  CA    . ILE   A  1 1200 ? 12.275  70.462  118.409 1.00 22.97 ? 1198 ILE   A CA    1 
ATOM   8541  C  C     . ILE   A  1 1200 ? 13.127  69.280  118.855 1.00 27.67 ? 1198 ILE   A C     1 
ATOM   8542  O  O     . ILE   A  1 1200 ? 12.993  68.169  118.335 1.00 23.86 ? 1198 ILE   A O     1 
ATOM   8543  C  CB    . ILE   A  1 1200 ? 13.016  71.346  117.388 1.00 21.80 ? 1198 ILE   A CB    1 
ATOM   8544  C  CG1   . ILE   A  1 1200 ? 12.063  72.390  116.798 1.00 22.24 ? 1198 ILE   A CG1   1 
ATOM   8545  C  CG2   . ILE   A  1 1200 ? 13.616  70.494  116.272 1.00 21.72 ? 1198 ILE   A CG2   1 
ATOM   8546  C  CD1   . ILE   A  1 1200 ? 12.728  73.337  115.825 1.00 21.56 ? 1198 ILE   A CD1   1 
ATOM   8547  N  N     . ALA   A  1 1201 ? 13.997  69.494  119.845 1.00 24.05 ? 1199 ALA   A N     1 
ATOM   8548  C  CA    . ALA   A  1 1201 ? 14.851  68.411  120.322 1.00 26.18 ? 1199 ALA   A CA    1 
ATOM   8549  C  C     . ALA   A  1 1201 ? 14.054  67.367  121.098 1.00 24.89 ? 1199 ALA   A C     1 
ATOM   8550  O  O     . ALA   A  1 1201 ? 14.353  66.169  121.019 1.00 26.11 ? 1199 ALA   A O     1 
ATOM   8551  C  CB    . ALA   A  1 1201 ? 15.976  68.972  121.197 1.00 25.85 ? 1199 ALA   A CB    1 
ATOM   8552  N  N     . ARG   A  1 1202 ? 13.048  67.802  121.866 1.00 21.46 ? 1200 ARG   A N     1 
ATOM   8553  C  CA    . ARG   A  1 1202 ? 12.311  66.913  122.758 1.00 23.82 ? 1200 ARG   A CA    1 
ATOM   8554  C  C     . ARG   A  1 1202 ? 11.131  66.222  122.087 1.00 27.65 ? 1200 ARG   A C     1 
ATOM   8555  O  O     . ARG   A  1 1202 ? 10.852  65.056  122.377 1.00 28.21 ? 1200 ARG   A O     1 
ATOM   8556  C  CB    . ARG   A  1 1202 ? 11.778  67.686  123.968 1.00 22.50 ? 1200 ARG   A CB    1 
ATOM   8557  C  CG    . ARG   A  1 1202 ? 12.824  68.147  124.962 1.00 24.73 ? 1200 ARG   A CG    1 
ATOM   8558  C  CD    . ARG   A  1 1202 ? 12.116  68.670  126.213 1.00 24.40 ? 1200 ARG   A CD    1 
ATOM   8559  N  NE    . ARG   A  1 1202 ? 11.242  69.784  125.869 1.00 25.22 ? 1200 ARG   A NE    1 
ATOM   8560  C  CZ    . ARG   A  1 1202 ? 11.634  71.050  125.821 1.00 28.32 ? 1200 ARG   A CZ    1 
ATOM   8561  N  NH1   . ARG   A  1 1202 ? 12.848  71.417  126.212 1.00 25.50 ? 1200 ARG   A NH1   1 
ATOM   8562  N  NH2   . ARG   A  1 1202 ? 10.792  71.970  125.358 1.00 29.58 ? 1200 ARG   A NH2   1 
ATOM   8563  N  N     . ASN   A  1 1203 ? 10.419  66.921  121.214 1.00 23.04 ? 1201 ASN   A N     1 
ATOM   8564  C  CA    . ASN   A  1 1203 ? 9.126   66.437  120.763 1.00 25.64 ? 1201 ASN   A CA    1 
ATOM   8565  C  C     . ASN   A  1 1203 ? 9.181   66.096  119.284 1.00 28.25 ? 1201 ASN   A C     1 
ATOM   8566  O  O     . ASN   A  1 1203 ? 9.303   67.003  118.443 1.00 25.89 ? 1201 ASN   A O     1 
ATOM   8567  C  CB    . ASN   A  1 1203 ? 8.049   67.486  121.039 1.00 28.46 ? 1201 ASN   A CB    1 
ATOM   8568  C  CG    . ASN   A  1 1203 ? 6.675   67.038  120.606 1.00 30.07 ? 1201 ASN   A CG    1 
ATOM   8569  O  OD1   . ASN   A  1 1203 ? 6.480   65.897  120.190 1.00 29.59 ? 1201 ASN   A OD1   1 
ATOM   8570  N  ND2   . ASN   A  1 1203 ? 5.707   67.939  120.707 1.00 28.32 ? 1201 ASN   A ND2   1 
ATOM   8571  N  N     . PRO   A  1 1204 ? 9.076   64.820  118.920 1.00 29.77 ? 1202 PRO   A N     1 
ATOM   8572  C  CA    . PRO   A  1 1204 ? 9.086   64.463  117.494 1.00 28.16 ? 1202 PRO   A CA    1 
ATOM   8573  C  C     . PRO   A  1 1204 ? 7.943   65.095  116.725 1.00 28.22 ? 1202 PRO   A C     1 
ATOM   8574  O  O     . PRO   A  1 1204 ? 8.039   65.242  115.502 1.00 27.24 ? 1202 PRO   A O     1 
ATOM   8575  C  CB    . PRO   A  1 1204 ? 8.976   62.932  117.514 1.00 31.97 ? 1202 PRO   A CB    1 
ATOM   8576  C  CG    . PRO   A  1 1204 ? 8.340   62.618  118.825 1.00 35.35 ? 1202 PRO   A CG    1 
ATOM   8577  C  CD    . PRO   A  1 1204 ? 8.842   63.655  119.791 1.00 31.16 ? 1202 PRO   A CD    1 
ATOM   8578  N  N     . ASP   A  1 1205 ? 6.877   65.491  117.413 1.00 30.02 ? 1203 ASP   A N     1 
ATOM   8579  C  CA    . ASP   A  1 1205 ? 5.726   66.139  116.804 1.00 29.20 ? 1203 ASP   A CA    1 
ATOM   8580  C  C     . ASP   A  1 1205 ? 5.709   67.643  117.056 1.00 27.40 ? 1203 ASP   A C     1 
ATOM   8581  O  O     . ASP   A  1 1205 ? 4.634   68.255  117.026 1.00 26.60 ? 1203 ASP   A O     1 
ATOM   8582  C  CB    . ASP   A  1 1205 ? 4.436   65.501  117.322 1.00 32.11 ? 1203 ASP   A CB    1 
ATOM   8583  C  CG    . ASP   A  1 1205 ? 4.388   64.002  117.073 1.00 34.08 ? 1203 ASP   A CG    1 
ATOM   8584  O  OD1   . ASP   A  1 1205 ? 4.854   63.547  116.005 1.00 37.19 ? 1203 ASP   A OD1   1 
ATOM   8585  O  OD2   . ASP   A  1 1205 ? 3.893   63.279  117.958 1.00 42.50 ? 1203 ASP   A OD2   1 
ATOM   8586  N  N     . ALA   A  1 1206 ? 6.877   68.240  117.328 1.00 24.82 ? 1204 ALA   A N     1 
ATOM   8587  C  CA    . ALA   A  1 1206 ? 6.959   69.687  117.500 1.00 22.89 ? 1204 ALA   A CA    1 
ATOM   8588  C  C     . ALA   A  1 1206 ? 6.263   70.409  116.361 1.00 26.77 ? 1204 ALA   A C     1 
ATOM   8589  O  O     . ALA   A  1 1206 ? 5.532   71.384  116.581 1.00 26.38 ? 1204 ALA   A O     1 
ATOM   8590  C  CB    . ALA   A  1 1206 ? 8.421   70.121  117.592 1.00 25.36 ? 1204 ALA   A CB    1 
ATOM   8591  N  N     . TYR   A  1 1207 ? 6.475   69.937  115.135 1.00 20.82 ? 1205 TYR   A N     1 
ATOM   8592  C  CA    . TYR   A  1 1207 ? 5.736   70.386  113.962 1.00 20.79 ? 1205 TYR   A CA    1 
ATOM   8593  C  C     . TYR   A  1 1207 ? 4.798   69.270  113.532 1.00 24.54 ? 1205 TYR   A C     1 
ATOM   8594  O  O     . TYR   A  1 1207 ? 5.247   68.156  113.240 1.00 28.91 ? 1205 TYR   A O     1 
ATOM   8595  C  CB    . TYR   A  1 1207 ? 6.690   70.755  112.828 1.00 21.32 ? 1205 TYR   A CB    1 
ATOM   8596  C  CG    . TYR   A  1 1207 ? 7.601   71.889  113.183 1.00 20.26 ? 1205 TYR   A CG    1 
ATOM   8597  C  CD1   . TYR   A  1 1207 ? 7.075   73.137  113.524 1.00 23.56 ? 1205 TYR   A CD1   1 
ATOM   8598  C  CD2   . TYR   A  1 1207 ? 8.983   71.728  113.193 1.00 22.16 ? 1205 TYR   A CD2   1 
ATOM   8599  C  CE1   . TYR   A  1 1207 ? 7.896   74.192  113.855 1.00 19.97 ? 1205 TYR   A CE1   1 
ATOM   8600  C  CE2   . TYR   A  1 1207 ? 9.823   72.789  113.533 1.00 22.71 ? 1205 TYR   A CE2   1 
ATOM   8601  C  CZ    . TYR   A  1 1207 ? 9.261   74.017  113.861 1.00 22.33 ? 1205 TYR   A CZ    1 
ATOM   8602  O  OH    . TYR   A  1 1207 ? 10.056  75.075  114.194 1.00 22.20 ? 1205 TYR   A OH    1 
ATOM   8603  N  N     . CYS   A  1 1208 ? 3.509   69.565  113.481 1.00 20.39 ? 1206 CYS   A N     1 
ATOM   8604  C  CA    . CYS   A  1 1208 ? 2.524   68.548  113.173 1.00 22.16 ? 1206 CYS   A CA    1 
ATOM   8605  C  C     . CYS   A  1 1208 ? 2.340   68.455  111.661 1.00 23.38 ? 1206 CYS   A C     1 
ATOM   8606  O  O     . CYS   A  1 1208 ? 2.099   69.465  110.990 1.00 20.73 ? 1206 CYS   A O     1 
ATOM   8607  C  CB    . CYS   A  1 1208 ? 1.208   68.867  113.878 1.00 23.18 ? 1206 CYS   A CB    1 
ATOM   8608  S  SG    . CYS   A  1 1208 ? -0.097  67.684  113.497 1.00 26.98 ? 1206 CYS   A SG    1 
ATOM   8609  N  N     . LEU   A  1 1209 ? 2.463   67.240  111.122 1.00 19.93 ? 1207 LEU   A N     1 
ATOM   8610  C  CA    . LEU   A  1 1209 ? 2.376   67.072  109.678 1.00 19.41 ? 1207 LEU   A CA    1 
ATOM   8611  C  C     . LEU   A  1 1209 ? 0.949   67.156  109.147 1.00 17.82 ? 1207 LEU   A C     1 
ATOM   8612  O  O     . LEU   A  1 1209 ? 0.775   67.276  107.929 1.00 18.46 ? 1207 LEU   A O     1 
ATOM   8613  C  CB    . LEU   A  1 1209 ? 3.001   65.736  109.256 1.00 18.42 ? 1207 LEU   A CB    1 
ATOM   8614  C  CG    . LEU   A  1 1209 ? 4.467   65.494  109.650 1.00 18.05 ? 1207 LEU   A CG    1 
ATOM   8615  C  CD1   . LEU   A  1 1209 ? 4.996   64.208  109.028 1.00 20.08 ? 1207 LEU   A CD1   1 
ATOM   8616  C  CD2   . LEU   A  1 1209 ? 5.323   66.672  109.235 1.00 19.77 ? 1207 LEU   A CD2   1 
ATOM   8617  N  N     . ASN   A  1 1210 ? -0.066  67.103  110.016 1.00 21.37 ? 1208 ASN   A N     1 
ATOM   8618  C  CA    . ASN   A  1 1210 ? -1.441  67.310  109.556 1.00 24.15 ? 1208 ASN   A CA    1 
ATOM   8619  C  C     . ASN   A  1 1210 ? -1.579  68.625  108.807 1.00 21.05 ? 1208 ASN   A C     1 
ATOM   8620  O  O     . ASN   A  1 1210 ? -2.336  68.719  107.834 1.00 21.14 ? 1208 ASN   A O     1 
ATOM   8621  C  CB    . ASN   A  1 1210 ? -2.433  67.316  110.730 1.00 22.39 ? 1208 ASN   A CB    1 
ATOM   8622  C  CG    . ASN   A  1 1210 ? -2.496  66.001  111.479 1.00 27.96 ? 1208 ASN   A CG    1 
ATOM   8623  O  OD1   . ASN   A  1 1210 ? -1.676  65.102  111.283 1.00 33.83 ? 1208 ASN   A OD1   1 
ATOM   8624  N  ND2   . ASN   A  1 1210 ? -3.478  65.897  112.377 1.00 33.89 ? 1208 ASN   A ND2   1 
ATOM   8625  N  N     . TRP   A  1 1211 ? -0.873  69.664  109.262 1.00 20.10 ? 1209 TRP   A N     1 
ATOM   8626  C  CA    . TRP   A  1 1211 ? -1.074  71.017  108.754 1.00 21.33 ? 1209 TRP   A CA    1 
ATOM   8627  C  C     . TRP   A  1 1211 ? -0.120  71.372  107.625 1.00 21.55 ? 1209 TRP   A C     1 
ATOM   8628  O  O     . TRP   A  1 1211 ? -0.118  72.525  107.174 1.00 22.95 ? 1209 TRP   A O     1 
ATOM   8629  C  CB    . TRP   A  1 1211 ? -0.964  72.036  109.908 1.00 19.36 ? 1209 TRP   A CB    1 
ATOM   8630  C  CG    . TRP   A  1 1211 ? -1.593  71.517  111.164 1.00 21.12 ? 1209 TRP   A CG    1 
ATOM   8631  C  CD1   . TRP   A  1 1211 ? -1.009  71.428  112.401 1.00 24.09 ? 1209 TRP   A CD1   1 
ATOM   8632  C  CD2   . TRP   A  1 1211 ? -2.907  70.958  111.304 1.00 21.02 ? 1209 TRP   A CD2   1 
ATOM   8633  N  NE1   . TRP   A  1 1211 ? -1.884  70.861  113.300 1.00 24.87 ? 1209 TRP   A NE1   1 
ATOM   8634  C  CE2   . TRP   A  1 1211 ? -3.052  70.561  112.652 1.00 21.75 ? 1209 TRP   A CE2   1 
ATOM   8635  C  CE3   . TRP   A  1 1211 ? -3.977  70.755  110.423 1.00 22.40 ? 1209 TRP   A CE3   1 
ATOM   8636  C  CZ2   . TRP   A  1 1211 ? -4.220  69.981  113.136 1.00 23.51 ? 1209 TRP   A CZ2   1 
ATOM   8637  C  CZ3   . TRP   A  1 1211 ? -5.141  70.177  110.914 1.00 20.39 ? 1209 TRP   A CZ3   1 
ATOM   8638  C  CH2   . TRP   A  1 1211 ? -5.248  69.790  112.245 1.00 21.72 ? 1209 TRP   A CH2   1 
ATOM   8639  N  N     . LEU   A  1 1212 ? 0.675   70.408  107.156 1.00 18.13 ? 1210 LEU   A N     1 
ATOM   8640  C  CA    . LEU   A  1 1212 ? 1.605   70.596  106.054 1.00 18.48 ? 1210 LEU   A CA    1 
ATOM   8641  C  C     . LEU   A  1 1212 ? 1.182   69.867  104.789 1.00 18.65 ? 1210 LEU   A C     1 
ATOM   8642  O  O     . LEU   A  1 1212 ? 1.922   69.887  103.795 1.00 18.31 ? 1210 LEU   A O     1 
ATOM   8643  C  CB    . LEU   A  1 1212 ? 3.010   70.139  106.468 1.00 17.55 ? 1210 LEU   A CB    1 
ATOM   8644  C  CG    . LEU   A  1 1212 ? 3.670   71.084  107.478 1.00 19.28 ? 1210 LEU   A CG    1 
ATOM   8645  C  CD1   . LEU   A  1 1212 ? 4.882   70.433  108.144 1.00 21.01 ? 1210 LEU   A CD1   1 
ATOM   8646  C  CD2   . LEU   A  1 1212 ? 4.067   72.399  106.778 1.00 20.18 ? 1210 LEU   A CD2   1 
ATOM   8647  N  N     . VAL   A  1 1213 ? 0.037   69.197  104.805 1.00 16.96 ? 1211 VAL   A N     1 
ATOM   8648  C  CA    . VAL   A  1 1213 ? -0.567  68.664  103.597 1.00 17.43 ? 1211 VAL   A CA    1 
ATOM   8649  C  C     . VAL   A  1 1213 ? -1.830  69.464  103.312 1.00 20.67 ? 1211 VAL   A C     1 
ATOM   8650  O  O     . VAL   A  1 1213 ? -2.352  70.186  104.166 1.00 19.57 ? 1211 VAL   A O     1 
ATOM   8651  C  CB    . VAL   A  1 1213 ? -0.886  67.152  103.705 1.00 20.43 ? 1211 VAL   A CB    1 
ATOM   8652  C  CG1   . VAL   A  1 1213 ? 0.398   66.342  103.842 1.00 18.33 ? 1211 VAL   A CG1   1 
ATOM   8653  C  CG2   . VAL   A  1 1213 ? -1.835  66.878  104.867 1.00 17.21 ? 1211 VAL   A CG2   1 
ATOM   8654  N  N     . GLU   A  1 1214 ? -2.343  69.295  102.107 1.00 19.09 ? 1212 GLU   A N     1 
ATOM   8655  C  CA    . GLU   A  1 1214 ? -3.547  69.973  101.664 1.00 25.12 ? 1212 GLU   A CA    1 
ATOM   8656  C  C     . GLU   A  1 1214 ? -4.601  68.926  101.352 1.00 18.24 ? 1212 GLU   A C     1 
ATOM   8657  O  O     . GLU   A  1 1214 ? -4.345  67.991  100.594 1.00 17.56 ? 1212 GLU   A O     1 
ATOM   8658  C  CB    . GLU   A  1 1214 ? -3.259  70.818  100.432 1.00 23.46 ? 1212 GLU   A CB    1 
ATOM   8659  C  CG    . GLU   A  1 1214 ? -4.411  71.672  99.970  1.00 30.83 ? 1212 GLU   A CG    1 
ATOM   8660  C  CD    . GLU   A  1 1214 ? -4.012  72.521  98.782  1.00 40.37 ? 1212 GLU   A CD    1 
ATOM   8661  O  OE1   . GLU   A  1 1214 ? -3.133  73.406  98.945  1.00 42.09 ? 1212 GLU   A OE1   1 
ATOM   8662  O  OE2   . GLU   A  1 1214 ? -4.555  72.279  97.681  1.00 45.70 ? 1212 GLU   A OE2   1 
ATOM   8663  N  N     . GLU   A  1 1215 ? -5.776  69.076  101.945 1.00 17.85 ? 1213 GLU   A N     1 
ATOM   8664  C  CA    . GLU   A  1 1215 ? -6.868  68.170  101.652 1.00 16.20 ? 1213 GLU   A CA    1 
ATOM   8665  C  C     . GLU   A  1 1215 ? -7.529  68.583  100.349 1.00 18.29 ? 1213 GLU   A C     1 
ATOM   8666  O  O     . GLU   A  1 1215 ? -7.757  69.772  100.108 1.00 16.43 ? 1213 GLU   A O     1 
ATOM   8667  C  CB    . GLU   A  1 1215 ? -7.906  68.226  102.760 1.00 17.40 ? 1213 GLU   A CB    1 
ATOM   8668  C  CG    . GLU   A  1 1215 ? -7.365  67.935  104.123 1.00 18.10 ? 1213 GLU   A CG    1 
ATOM   8669  C  CD    . GLU   A  1 1215 ? -8.373  68.287  105.183 1.00 17.54 ? 1213 GLU   A CD    1 
ATOM   8670  O  OE1   . GLU   A  1 1215 ? -8.405  69.465  105.600 1.00 20.31 ? 1213 GLU   A OE1   1 
ATOM   8671  O  OE2   . GLU   A  1 1215 ? -9.141  67.390  105.575 1.00 19.47 ? 1213 GLU   A OE2   1 
ATOM   8672  N  N     . VAL   A  1 1216 ? -7.861  67.599  99.520  1.00 15.82 ? 1214 VAL   A N     1 
ATOM   8673  C  CA    . VAL   A  1 1216 ? -8.626  67.847  98.309  1.00 15.54 ? 1214 VAL   A CA    1 
ATOM   8674  C  C     . VAL   A  1 1216 ? -9.791  66.874  98.285  1.00 16.22 ? 1214 VAL   A C     1 
ATOM   8675  O  O     . VAL   A  1 1216 ? -9.616  65.670  98.515  1.00 16.63 ? 1214 VAL   A O     1 
ATOM   8676  C  CB    . VAL   A  1 1216 ? -7.775  67.714  97.037  1.00 17.21 ? 1214 VAL   A CB    1 
ATOM   8677  C  CG1   . VAL   A  1 1216 ? -8.663  67.779  95.808  1.00 15.50 ? 1214 VAL   A CG1   1 
ATOM   8678  C  CG2   . VAL   A  1 1216 ? -6.743  68.836  96.987  1.00 20.46 ? 1214 VAL   A CG2   1 
ATOM   8679  N  N     . SER   A  1 1217 ? -10.971 67.404  98.035  1.00 15.79 ? 1215 SER   A N     1 
ATOM   8680  C  CA    . SER   A  1 1217 ? -12.183 66.624  97.860  1.00 15.19 ? 1215 SER   A CA    1 
ATOM   8681  C  C     . SER   A  1 1217 ? -12.587 66.711  96.398  1.00 15.99 ? 1215 SER   A C     1 
ATOM   8682  O  O     . SER   A  1 1217 ? -12.513 67.785  95.788  1.00 17.39 ? 1215 SER   A O     1 
ATOM   8683  C  CB    . SER   A  1 1217 ? -13.299 67.154  98.755  1.00 16.05 ? 1215 SER   A CB    1 
ATOM   8684  O  OG    . SER   A  1 1217 ? -14.556 66.662  98.321  1.00 20.87 ? 1215 SER   A OG    1 
ATOM   8685  N  N     . ALA   A  1 1218 ? -12.951 65.571  95.824  1.00 15.29 ? 1216 ALA   A N     1 
ATOM   8686  C  CA    . ALA   A  1 1218 ? -13.392 65.509  94.436  1.00 16.33 ? 1216 ALA   A CA    1 
ATOM   8687  C  C     . ALA   A  1 1218 ? -14.671 64.695  94.402  1.00 19.27 ? 1216 ALA   A C     1 
ATOM   8688  O  O     . ALA   A  1 1218 ? -14.706 63.570  94.917  1.00 18.94 ? 1216 ALA   A O     1 
ATOM   8689  C  CB    . ALA   A  1 1218 ? -12.340 64.883  93.528  1.00 16.60 ? 1216 ALA   A CB    1 
ATOM   8690  N  N     . SER   A  1 1219 ? -15.720 65.269  93.826  1.00 16.12 ? 1217 SER   A N     1 
ATOM   8691  C  CA    . SER   A  1 1219 ? -17.005 64.591  93.715  1.00 14.75 ? 1217 SER   A CA    1 
ATOM   8692  C  C     . SER   A  1 1219 ? -17.318 64.419  92.238  1.00 15.51 ? 1217 SER   A C     1 
ATOM   8693  O  O     . SER   A  1 1219 ? -17.466 65.411  91.518  1.00 18.73 ? 1217 SER   A O     1 
ATOM   8694  C  CB    . SER   A  1 1219 ? -18.112 65.387  94.410  1.00 16.69 ? 1217 SER   A CB    1 
ATOM   8695  O  OG    . SER   A  1 1219 ? -19.343 64.691  94.316  1.00 17.21 ? 1217 SER   A OG    1 
ATOM   8696  N  N     . ILE   A  1 1220 ? -17.399 63.172  91.788  1.00 14.75 ? 1218 ILE   A N     1 
ATOM   8697  C  CA    . ILE   A  1 1220 ? -17.606 62.851  90.379  1.00 16.16 ? 1218 ILE   A CA    1 
ATOM   8698  C  C     . ILE   A  1 1220 ? -18.999 62.264  90.224  1.00 14.74 ? 1218 ILE   A C     1 
ATOM   8699  O  O     . ILE   A  1 1220 ? -19.324 61.244  90.840  1.00 16.10 ? 1218 ILE   A O     1 
ATOM   8700  C  CB    . ILE   A  1 1220 ? -16.553 61.872  89.841  1.00 18.72 ? 1218 ILE   A CB    1 
ATOM   8701  C  CG1   . ILE   A  1 1220 ? -15.148 62.467  90.003  1.00 25.04 ? 1218 ILE   A CG1   1 
ATOM   8702  C  CG2   . ILE   A  1 1220 ? -16.845 61.597  88.364  1.00 22.22 ? 1218 ILE   A CG2   1 
ATOM   8703  C  CD1   . ILE   A  1 1220 ? -14.275 61.765  91.026  1.00 29.11 ? 1218 ILE   A CD1   1 
ATOM   8704  N  N     . ASN   A  1 1221 ? -19.813 62.913  89.400  1.00 16.81 ? 1219 ASN   A N     1 
ATOM   8705  C  CA    . ASN   A  1 1221 ? -21.124 62.390  89.049  1.00 18.20 ? 1219 ASN   A CA    1 
ATOM   8706  C  C     . ASN   A  1 1221 ? -20.932 61.252  88.057  1.00 18.98 ? 1219 ASN   A C     1 
ATOM   8707  O  O     . ASN   A  1 1221 ? -20.587 61.483  86.897  1.00 21.09 ? 1219 ASN   A O     1 
ATOM   8708  C  CB    . ASN   A  1 1221 ? -21.985 63.505  88.467  1.00 18.58 ? 1219 ASN   A CB    1 
ATOM   8709  C  CG    . ASN   A  1 1221 ? -23.365 63.021  88.063  1.00 21.02 ? 1219 ASN   A CG    1 
ATOM   8710  O  OD1   . ASN   A  1 1221 ? -23.729 61.877  88.321  1.00 17.69 ? 1219 ASN   A OD1   1 
ATOM   8711  N  ND2   . ASN   A  1 1221 ? -24.147 63.904  87.445  1.00 22.84 ? 1219 ASN   A ND2   1 
ATOM   8712  N  N     . THR   A  1 1222 ? -21.144 60.019  88.509  1.00 20.11 ? 1220 THR   A N     1 
ATOM   8713  C  CA    . THR   A  1 1222 ? -20.971 58.853  87.653  1.00 21.73 ? 1220 THR   A CA    1 
ATOM   8714  C  C     . THR   A  1 1222 ? -22.287 58.367  87.074  1.00 23.11 ? 1220 THR   A C     1 
ATOM   8715  O  O     . THR   A  1 1222 ? -22.331 57.297  86.463  1.00 26.57 ? 1220 THR   A O     1 
ATOM   8716  C  CB    . THR   A  1 1222 ? -20.286 57.726  88.417  1.00 22.43 ? 1220 THR   A CB    1 
ATOM   8717  O  OG1   . THR   A  1 1222 ? -21.100 57.347  89.528  1.00 20.49 ? 1220 THR   A OG1   1 
ATOM   8718  C  CG2   . THR   A  1 1222 ? -18.932 58.176  88.915  1.00 20.76 ? 1220 THR   A CG2   1 
ATOM   8719  N  N     . ALA   A  1 1223 ? -23.358 59.118  87.270  1.00 18.34 ? 1221 ALA   A N     1 
ATOM   8720  C  CA    . ALA   A  1 1223 ? -24.589 58.899  86.531  1.00 28.50 ? 1221 ALA   A CA    1 
ATOM   8721  C  C     . ALA   A  1 1223 ? -24.642 59.767  85.288  1.00 34.72 ? 1221 ALA   A C     1 
ATOM   8722  O  O     . ALA   A  1 1223 ? -25.621 59.699  84.538  1.00 43.02 ? 1221 ALA   A O     1 
ATOM   8723  C  CB    . ALA   A  1 1223 ? -25.806 59.187  87.417  1.00 25.42 ? 1221 ALA   A CB    1 
ATOM   8724  N  N     . ALA   A  1 1224 ? -23.579 60.545  85.051  1.00 38.00 ? 1222 ALA   A N     1 
ATOM   8725  C  CA    . ALA   A  1 1224 ? -23.614 61.672  84.126  1.00 37.84 ? 1222 ALA   A CA    1 
ATOM   8726  C  C     . ALA   A  1 1224 ? -23.814 61.237  82.681  1.00 44.41 ? 1222 ALA   A C     1 
ATOM   8727  O  O     . ALA   A  1 1224 ? -24.315 62.023  81.871  1.00 45.62 ? 1222 ALA   A O     1 
ATOM   8728  C  CB    . ALA   A  1 1224 ? -22.323 62.480  84.266  1.00 30.98 ? 1222 ALA   A CB    1 
ATOM   8729  N  N     . ALA   A  1 1225 ? -23.428 60.009  82.332  1.00 43.85 ? 1223 ALA   A N     1 
ATOM   8730  C  CA    . ALA   A  1 1225 ? -23.691 59.497  80.992  1.00 46.23 ? 1223 ALA   A CA    1 
ATOM   8731  C  C     . ALA   A  1 1225 ? -25.126 59.011  80.818  1.00 51.20 ? 1223 ALA   A C     1 
ATOM   8732  O  O     . ALA   A  1 1225 ? -25.462 58.491  79.747  1.00 54.48 ? 1223 ALA   A O     1 
ATOM   8733  C  CB    . ALA   A  1 1225 ? -22.712 58.369  80.646  1.00 40.94 ? 1223 ALA   A CB    1 
ATOM   8734  N  N     . GLY   A  1 1226 ? -25.978 59.173  81.833  1.00 47.85 ? 1224 GLY   A N     1 
ATOM   8735  C  CA    . GLY   A  1 1226 ? -27.385 58.842  81.750  1.00 49.83 ? 1224 GLY   A CA    1 
ATOM   8736  C  C     . GLY   A  1 1226 ? -27.810 57.704  82.650  1.00 50.11 ? 1224 GLY   A C     1 
ATOM   8737  O  O     . GLY   A  1 1226 ? -29.006 57.584  82.953  1.00 52.94 ? 1224 GLY   A O     1 
ATOM   8738  N  N     . GLY   A  1 1227 ? -26.872 56.865  83.088  1.00 48.12 ? 1225 GLY   A N     1 
ATOM   8739  C  CA    . GLY   A  1 1227 ? -27.198 55.739  83.936  1.00 48.81 ? 1225 GLY   A CA    1 
ATOM   8740  C  C     . GLY   A  1 1227 ? -26.088 55.460  84.931  1.00 48.91 ? 1225 GLY   A C     1 
ATOM   8741  O  O     . GLY   A  1 1227 ? -25.029 56.093  84.912  1.00 52.27 ? 1225 GLY   A O     1 
ATOM   8742  N  N     . ASN   A  1 1228 ? -26.352 54.494  85.799  1.00 48.00 ? 1226 ASN   A N     1 
ATOM   8743  C  CA    . ASN   A  1 1228 ? -25.422 54.087  86.845  1.00 52.75 ? 1226 ASN   A CA    1 
ATOM   8744  C  C     . ASN   A  1 1228 ? -24.893 52.696  86.501  1.00 56.26 ? 1226 ASN   A C     1 
ATOM   8745  O  O     . ASN   A  1 1228 ? -25.644 51.713  86.530  1.00 53.98 ? 1226 ASN   A O     1 
ATOM   8746  C  CB    . ASN   A  1 1228 ? -26.115 54.111  88.205  1.00 50.52 ? 1226 ASN   A CB    1 
ATOM   8747  C  CG    . ASN   A  1 1228 ? -25.161 53.863  89.351  1.00 53.50 ? 1226 ASN   A CG    1 
ATOM   8748  O  OD1   . ASN   A  1 1228 ? -24.077 53.300  89.173  1.00 54.37 ? 1226 ASN   A OD1   1 
ATOM   8749  N  ND2   . ASN   A  1 1228 ? -25.567 54.273  90.549  1.00 50.27 ? 1226 ASN   A ND2   1 
ATOM   8750  N  N     . ALA   A  1 1229 ? -23.598 52.618  86.186  1.00 55.15 ? 1227 ALA   A N     1 
ATOM   8751  C  CA    . ALA   A  1 1229 ? -22.989 51.345  85.814  1.00 54.61 ? 1227 ALA   A CA    1 
ATOM   8752  C  C     . ALA   A  1 1229 ? -23.100 50.325  86.943  1.00 60.81 ? 1227 ALA   A C     1 
ATOM   8753  O  O     . ALA   A  1 1229 ? -23.650 49.231  86.759  1.00 61.38 ? 1227 ALA   A O     1 
ATOM   8754  C  CB    . ALA   A  1 1229 ? -21.526 51.562  85.430  1.00 49.39 ? 1227 ALA   A CB    1 
ATOM   8755  N  N     . SER   A  1 1230 ? -22.579 50.668  88.127  1.00 57.65 ? 1228 SER   A N     1 
ATOM   8756  C  CA    . SER   A  1 1230 ? -22.562 49.720  89.238  1.00 53.82 ? 1228 SER   A CA    1 
ATOM   8757  C  C     . SER   A  1 1230 ? -23.971 49.327  89.673  1.00 60.12 ? 1228 SER   A C     1 
ATOM   8758  O  O     . SER   A  1 1230 ? -24.172 48.235  90.220  1.00 61.37 ? 1228 SER   A O     1 
ATOM   8759  C  CB    . SER   A  1 1230 ? -21.782 50.310  90.414  1.00 54.72 ? 1228 SER   A CB    1 
ATOM   8760  N  N     . LEU   A  1 1231 ? -24.954 50.190  89.438  1.00 58.31 ? 1229 LEU   A N     1 
ATOM   8761  C  CA    . LEU   A  1 1231 ? -26.337 49.866  89.755  1.00 56.35 ? 1229 LEU   A CA    1 
ATOM   8762  C  C     . LEU   A  1 1231 ? -27.069 49.364  88.516  1.00 59.35 ? 1229 LEU   A C     1 
ATOM   8763  O  O     . LEU   A  1 1231 ? -27.633 48.270  88.518  1.00 66.83 ? 1229 LEU   A O     1 
ATOM   8764  C  CB    . LEU   A  1 1231 ? -27.057 51.081  90.338  1.00 51.61 ? 1229 LEU   A CB    1 
ATOM   8765  C  CG    . LEU   A  1 1231 ? -27.013 51.330  91.844  1.00 46.46 ? 1229 LEU   A CG    1 
ATOM   8766  C  CD1   . LEU   A  1 1231 ? -28.060 52.370  92.195  1.00 43.35 ? 1229 LEU   A CD1   1 
ATOM   8767  C  CD2   . LEU   A  1 1231 ? -27.259 50.049  92.617  1.00 47.93 ? 1229 LEU   A CD2   1 
ATOM   8768  N  N     . ALA   B  1 16   ? 30.226  5.190   80.479  1.00 47.34 ? 14   ALA   B N     1 
ATOM   8769  C  CA    . ALA   B  1 16   ? 29.209  6.214   80.706  1.00 47.12 ? 14   ALA   B CA    1 
ATOM   8770  C  C     . ALA   B  1 16   ? 27.815  5.607   80.739  1.00 47.70 ? 14   ALA   B C     1 
ATOM   8771  O  O     . ALA   B  1 16   ? 27.457  4.833   79.852  1.00 49.35 ? 14   ALA   B O     1 
ATOM   8772  C  CB    . ALA   B  1 16   ? 29.283  7.288   79.630  1.00 43.42 ? 14   ALA   B CB    1 
ATOM   8773  N  N     . PRO   B  1 17   ? 27.027  5.959   81.756  1.00 49.73 ? 15   PRO   B N     1 
ATOM   8774  C  CA    . PRO   B  1 17   ? 25.634  5.496   81.793  1.00 45.22 ? 15   PRO   B CA    1 
ATOM   8775  C  C     . PRO   B  1 17   ? 24.885  5.941   80.544  1.00 44.94 ? 15   PRO   B C     1 
ATOM   8776  O  O     . PRO   B  1 17   ? 25.075  7.054   80.049  1.00 43.73 ? 15   PRO   B O     1 
ATOM   8777  C  CB    . PRO   B  1 17   ? 25.070  6.159   83.054  1.00 45.44 ? 15   PRO   B CB    1 
ATOM   8778  C  CG    . PRO   B  1 17   ? 26.272  6.519   83.878  1.00 48.71 ? 15   PRO   B CG    1 
ATOM   8779  C  CD    . PRO   B  1 17   ? 27.359  6.827   82.898  1.00 45.16 ? 15   PRO   B CD    1 
ATOM   8780  N  N     . ALA   B  1 18   ? 24.049  5.045   80.027  1.00 39.74 ? 16   ALA   B N     1 
ATOM   8781  C  CA    . ALA   B  1 18   ? 23.222  5.376   78.877  1.00 35.98 ? 16   ALA   B CA    1 
ATOM   8782  C  C     . ALA   B  1 18   ? 22.319  6.561   79.214  1.00 34.94 ? 16   ALA   B C     1 
ATOM   8783  O  O     . ALA   B  1 18   ? 21.749  6.612   80.309  1.00 30.59 ? 16   ALA   B O     1 
ATOM   8784  C  CB    . ALA   B  1 18   ? 22.375  4.171   78.458  1.00 36.55 ? 16   ALA   B CB    1 
ATOM   8785  N  N     . PRO   B  1 19   ? 22.183  7.536   78.316  1.00 28.00 ? 17   PRO   B N     1 
ATOM   8786  C  CA    . PRO   B  1 19   ? 21.331  8.695   78.614  1.00 29.15 ? 17   PRO   B CA    1 
ATOM   8787  C  C     . PRO   B  1 19   ? 19.921  8.259   78.985  1.00 26.40 ? 17   PRO   B C     1 
ATOM   8788  O  O     . PRO   B  1 19   ? 19.322  7.402   78.329  1.00 26.24 ? 17   PRO   B O     1 
ATOM   8789  C  CB    . PRO   B  1 19   ? 21.353  9.500   77.307  1.00 25.35 ? 17   PRO   B CB    1 
ATOM   8790  C  CG    . PRO   B  1 19   ? 22.597  9.060   76.603  1.00 31.48 ? 17   PRO   B CG    1 
ATOM   8791  C  CD    . PRO   B  1 19   ? 22.772  7.611   76.967  1.00 30.67 ? 17   PRO   B CD    1 
ATOM   8792  N  N     . PHE   B  1 20   ? 19.420  8.821   80.083  1.00 26.80 ? 18   PHE   B N     1 
ATOM   8793  C  CA    . PHE   B  1 20   ? 18.044  8.673   80.555  1.00 26.72 ? 18   PHE   B CA    1 
ATOM   8794  C  C     . PHE   B  1 20   ? 17.693  7.253   80.962  1.00 28.48 ? 18   PHE   B C     1 
ATOM   8795  O  O     . PHE   B  1 20   ? 16.511  6.963   81.196  1.00 25.39 ? 18   PHE   B O     1 
ATOM   8796  C  CB    . PHE   B  1 20   ? 17.041  9.154   79.508  1.00 23.81 ? 18   PHE   B CB    1 
ATOM   8797  C  CG    . PHE   B  1 20   ? 17.252  10.567  79.095  1.00 21.96 ? 18   PHE   B CG    1 
ATOM   8798  C  CD1   . PHE   B  1 20   ? 16.901  11.608  79.947  1.00 21.84 ? 18   PHE   B CD1   1 
ATOM   8799  C  CD2   . PHE   B  1 20   ? 17.802  10.860  77.856  1.00 21.19 ? 18   PHE   B CD2   1 
ATOM   8800  C  CE1   . PHE   B  1 20   ? 17.097  12.927  79.563  1.00 24.29 ? 18   PHE   B CE1   1 
ATOM   8801  C  CE2   . PHE   B  1 20   ? 17.999  12.163  77.464  1.00 23.05 ? 18   PHE   B CE2   1 
ATOM   8802  C  CZ    . PHE   B  1 20   ? 17.654  13.203  78.318  1.00 24.44 ? 18   PHE   B CZ    1 
ATOM   8803  N  N     . ALA   B  1 21   ? 18.683  6.360   81.050  1.00 27.90 ? 19   ALA   B N     1 
ATOM   8804  C  CA    . ALA   B  1 21   ? 18.407  4.981   81.437  1.00 31.46 ? 19   ALA   B CA    1 
ATOM   8805  C  C     . ALA   B  1 21   ? 17.779  4.895   82.829  1.00 34.77 ? 19   ALA   B C     1 
ATOM   8806  O  O     . ALA   B  1 21   ? 16.954  4.008   83.083  1.00 37.25 ? 19   ALA   B O     1 
ATOM   8807  C  CB    . ALA   B  1 21   ? 19.695  4.163   81.367  1.00 35.33 ? 19   ALA   B CB    1 
ATOM   8808  N  N     . ASP   B  1 22   ? 18.130  5.811   83.733  1.00 29.76 ? 20   ASP   B N     1 
ATOM   8809  C  CA    . ASP   B  1 22   ? 17.509  5.832   85.056  1.00 31.02 ? 20   ASP   B CA    1 
ATOM   8810  C  C     . ASP   B  1 22   ? 16.871  7.186   85.325  1.00 25.17 ? 20   ASP   B C     1 
ATOM   8811  O  O     . ASP   B  1 22   ? 17.135  7.811   86.357  1.00 24.50 ? 20   ASP   B O     1 
ATOM   8812  C  CB    . ASP   B  1 22   ? 18.534  5.516   86.143  1.00 33.25 ? 20   ASP   B CB    1 
ATOM   8813  N  N     . PHE   B  1 23   ? 16.032  7.656   84.404  1.00 22.76 ? 21   PHE   B N     1 
ATOM   8814  C  CA    . PHE   B  1 23   ? 15.539  9.025   84.508  1.00 21.59 ? 21   PHE   B CA    1 
ATOM   8815  C  C     . PHE   B  1 23   ? 14.589  9.187   85.687  1.00 21.08 ? 21   PHE   B C     1 
ATOM   8816  O  O     . PHE   B  1 23   ? 14.772  10.072  86.532  1.00 20.14 ? 21   PHE   B O     1 
ATOM   8817  C  CB    . PHE   B  1 23   ? 14.849  9.442   83.212  1.00 19.88 ? 21   PHE   B CB    1 
ATOM   8818  C  CG    . PHE   B  1 23   ? 14.169  10.771  83.309  1.00 23.71 ? 21   PHE   B CG    1 
ATOM   8819  C  CD1   . PHE   B  1 23   ? 14.915  11.926  83.464  1.00 18.99 ? 21   PHE   B CD1   1 
ATOM   8820  C  CD2   . PHE   B  1 23   ? 12.786  10.868  83.262  1.00 20.81 ? 21   PHE   B CD2   1 
ATOM   8821  C  CE1   . PHE   B  1 23   ? 14.289  13.161  83.579  1.00 22.29 ? 21   PHE   B CE1   1 
ATOM   8822  C  CE2   . PHE   B  1 23   ? 12.162  12.095  83.365  1.00 22.20 ? 21   PHE   B CE2   1 
ATOM   8823  C  CZ    . PHE   B  1 23   ? 12.912  13.241  83.528  1.00 22.06 ? 21   PHE   B CZ    1 
ATOM   8824  N  N     . ALA   B  1 24   ? 13.559  8.361   85.748  1.00 20.07 ? 22   ALA   B N     1 
ATOM   8825  C  CA    . ALA   B  1 24   ? 12.593  8.490   86.825  1.00 22.58 ? 22   ALA   B CA    1 
ATOM   8826  C  C     . ALA   B  1 24   ? 11.900  7.157   87.083  1.00 22.74 ? 22   ALA   B C     1 
ATOM   8827  O  O     . ALA   B  1 24   ? 10.672  7.075   86.967  1.00 20.69 ? 22   ALA   B O     1 
ATOM   8828  C  CB    . ALA   B  1 24   ? 11.566  9.579   86.486  1.00 19.16 ? 22   ALA   B CB    1 
ATOM   8829  N  N     . PRO   B  1 25   ? 12.628  6.103   87.444  1.00 23.66 ? 23   PRO   B N     1 
ATOM   8830  C  CA    . PRO   B  1 25   ? 11.978  4.814   87.682  1.00 24.60 ? 23   PRO   B CA    1 
ATOM   8831  C  C     . PRO   B  1 25   ? 11.005  4.908   88.842  1.00 21.88 ? 23   PRO   B C     1 
ATOM   8832  O  O     . PRO   B  1 25   ? 11.321  5.510   89.878  1.00 24.39 ? 23   PRO   B O     1 
ATOM   8833  C  CB    . PRO   B  1 25   ? 13.150  3.882   88.015  1.00 24.44 ? 23   PRO   B CB    1 
ATOM   8834  C  CG    . PRO   B  1 25   ? 14.192  4.781   88.544  1.00 25.66 ? 23   PRO   B CG    1 
ATOM   8835  C  CD    . PRO   B  1 25   ? 14.065  6.053   87.766  1.00 23.71 ? 23   PRO   B CD    1 
ATOM   8836  N  N     . PRO   B  1 26   ? 9.811   4.343   88.699  1.00 23.25 ? 24   PRO   B N     1 
ATOM   8837  C  CA    . PRO   B  1 26   ? 8.836   4.397   89.789  1.00 23.64 ? 24   PRO   B CA    1 
ATOM   8838  C  C     . PRO   B  1 26   ? 9.310   3.592   90.986  1.00 24.78 ? 24   PRO   B C     1 
ATOM   8839  O  O     . PRO   B  1 26   ? 10.135  2.682   90.877  1.00 23.79 ? 24   PRO   B O     1 
ATOM   8840  C  CB    . PRO   B  1 26   ? 7.582   3.770   89.175  1.00 23.51 ? 24   PRO   B CB    1 
ATOM   8841  C  CG    . PRO   B  1 26   ? 8.116   2.841   88.119  1.00 26.00 ? 24   PRO   B CG    1 
ATOM   8842  C  CD    . PRO   B  1 26   ? 9.313   3.560   87.551  1.00 24.51 ? 24   PRO   B CD    1 
ATOM   8843  N  N     . VAL   B  1 27   ? 8.762   3.942   92.148  1.00 23.42 ? 25   VAL   B N     1 
ATOM   8844  C  CA    . VAL   B  1 27   ? 9.088   3.203   93.364  1.00 26.04 ? 25   VAL   B CA    1 
ATOM   8845  C  C     . VAL   B  1 27   ? 8.760   1.725   93.187  1.00 26.52 ? 25   VAL   B C     1 
ATOM   8846  O  O     . VAL   B  1 27   ? 9.536   0.847   93.588  1.00 27.30 ? 25   VAL   B O     1 
ATOM   8847  C  CB    . VAL   B  1 27   ? 8.353   3.818   94.568  1.00 24.43 ? 25   VAL   B CB    1 
ATOM   8848  C  CG1   . VAL   B  1 27   ? 8.555   2.963   95.814  1.00 27.25 ? 25   VAL   B CG1   1 
ATOM   8849  C  CG2   . VAL   B  1 27   ? 8.856   5.223   94.803  1.00 25.03 ? 25   VAL   B CG2   1 
ATOM   8850  N  N     . ARG   B  1 28   ? 7.638   1.429   92.541  1.00 25.93 ? 26   ARG   B N     1 
ATOM   8851  C  CA    . ARG   B  1 28   ? 7.191   0.058   92.352  1.00 26.80 ? 26   ARG   B CA    1 
ATOM   8852  C  C     . ARG   B  1 28   ? 6.427   -0.022  91.041  1.00 28.72 ? 26   ARG   B C     1 
ATOM   8853  O  O     . ARG   B  1 28   ? 5.963   1.002   90.526  1.00 25.27 ? 26   ARG   B O     1 
ATOM   8854  C  CB    . ARG   B  1 28   ? 6.310   -0.397  93.524  1.00 30.13 ? 26   ARG   B CB    1 
ATOM   8855  C  CG    . ARG   B  1 28   ? 4.939   0.284   93.584  1.00 30.22 ? 26   ARG   B CG    1 
ATOM   8856  C  CD    . ARG   B  1 28   ? 4.200   -0.066  94.877  1.00 31.06 ? 26   ARG   B CD    1 
ATOM   8857  N  NE    . ARG   B  1 28   ? 4.855   0.522   96.044  1.00 32.95 ? 26   ARG   B NE    1 
ATOM   8858  C  CZ    . ARG   B  1 28   ? 5.599   -0.155  96.909  1.00 37.00 ? 26   ARG   B CZ    1 
ATOM   8859  N  NH1   . ARG   B  1 28   ? 5.769   -1.467  96.798  1.00 35.17 ? 26   ARG   B NH1   1 
ATOM   8860  N  NH2   . ARG   B  1 28   ? 6.179   0.497   97.914  1.00 33.81 ? 26   ARG   B NH2   1 
ATOM   8861  N  N     . PRO   B  1 29   ? 6.290   -1.217  90.465  1.00 28.49 ? 27   PRO   B N     1 
ATOM   8862  C  CA    . PRO   B  1 29   ? 5.414   -1.360  89.297  1.00 27.92 ? 27   PRO   B CA    1 
ATOM   8863  C  C     . PRO   B  1 29   ? 3.994   -0.933  89.641  1.00 27.73 ? 27   PRO   B C     1 
ATOM   8864  O  O     . PRO   B  1 29   ? 3.480   -1.223  90.723  1.00 28.94 ? 27   PRO   B O     1 
ATOM   8865  C  CB    . PRO   B  1 29   ? 5.493   -2.855  88.970  1.00 30.23 ? 27   PRO   B CB    1 
ATOM   8866  C  CG    . PRO   B  1 29   ? 6.789   -3.299  89.565  1.00 32.73 ? 27   PRO   B CG    1 
ATOM   8867  C  CD    . PRO   B  1 29   ? 6.945   -2.488  90.816  1.00 29.49 ? 27   PRO   B CD    1 
ATOM   8868  N  N     . GLN   B  1 30   ? 3.360   -0.224  88.715  1.00 25.68 ? 28   GLN   B N     1 
ATOM   8869  C  CA    . GLN   B  1 30   ? 2.056   0.365   88.996  1.00 28.39 ? 28   GLN   B CA    1 
ATOM   8870  C  C     . GLN   B  1 30   ? 0.969   -0.679  88.770  1.00 29.52 ? 28   GLN   B C     1 
ATOM   8871  O  O     . GLN   B  1 30   ? 0.740   -1.118  87.639  1.00 28.83 ? 28   GLN   B O     1 
ATOM   8872  C  CB    . GLN   B  1 30   ? 1.839   1.600   88.128  1.00 29.10 ? 28   GLN   B CB    1 
ATOM   8873  C  CG    . GLN   B  1 30   ? 2.939   2.647   88.315  1.00 25.33 ? 28   GLN   B CG    1 
ATOM   8874  C  CD    . GLN   B  1 30   ? 2.870   3.335   89.665  1.00 24.65 ? 28   GLN   B CD    1 
ATOM   8875  O  OE1   . GLN   B  1 30   ? 1.963   4.127   89.918  1.00 25.20 ? 28   GLN   B OE1   1 
ATOM   8876  N  NE2   . GLN   B  1 30   ? 3.834   3.045   90.537  1.00 26.43 ? 28   GLN   B NE2   1 
ATOM   8877  N  N     . SER   B  1 31   ? 0.289   -1.062  89.847  1.00 27.08 ? 29   SER   B N     1 
ATOM   8878  C  CA    . SER   B  1 31   ? -0.833  -1.987  89.771  1.00 28.40 ? 29   SER   B CA    1 
ATOM   8879  C  C     . SER   B  1 31   ? -1.990  -1.362  88.998  1.00 29.19 ? 29   SER   B C     1 
ATOM   8880  O  O     . SER   B  1 31   ? -1.987  -0.173  88.673  1.00 28.32 ? 29   SER   B O     1 
ATOM   8881  C  CB    . SER   B  1 31   ? -1.313  -2.344  91.170  1.00 31.24 ? 29   SER   B CB    1 
ATOM   8882  O  OG    . SER   B  1 31   ? -1.949  -1.216  91.747  1.00 28.82 ? 29   SER   B OG    1 
ATOM   8883  N  N     . THR   B  1 32   ? -3.012  -2.186  88.734  1.00 27.98 ? 30   THR   B N     1 
ATOM   8884  C  CA    . THR   B  1 32   ? -4.222  -1.696  88.086  1.00 29.69 ? 30   THR   B CA    1 
ATOM   8885  C  C     . THR   B  1 32   ? -4.875  -0.585  88.901  1.00 26.51 ? 30   THR   B C     1 
ATOM   8886  O  O     . THR   B  1 32   ? -5.284  0.443   88.348  1.00 28.35 ? 30   THR   B O     1 
ATOM   8887  C  CB    . THR   B  1 32   ? -5.193  -2.859  87.875  1.00 32.98 ? 30   THR   B CB    1 
ATOM   8888  O  OG1   . THR   B  1 32   ? -4.567  -3.849  87.051  1.00 35.31 ? 30   THR   B OG1   1 
ATOM   8889  C  CG2   . THR   B  1 32   ? -6.482  -2.390  87.208  1.00 34.86 ? 30   THR   B CG2   1 
ATOM   8890  N  N     . LEU   B  1 33   ? -4.965  -0.764  90.221  1.00 25.35 ? 31   LEU   B N     1 
ATOM   8891  C  CA    . LEU   B  1 33   ? -5.578  0.262   91.060  1.00 28.22 ? 31   LEU   B CA    1 
ATOM   8892  C  C     . LEU   B  1 33   ? -4.738  1.536   91.101  1.00 26.71 ? 31   LEU   B C     1 
ATOM   8893  O  O     . LEU   B  1 33   ? -5.288  2.643   91.110  1.00 25.88 ? 31   LEU   B O     1 
ATOM   8894  C  CB    . LEU   B  1 33   ? -5.808  -0.284  92.467  1.00 24.32 ? 31   LEU   B CB    1 
ATOM   8895  C  CG    . LEU   B  1 33   ? -6.909  -1.338  92.474  1.00 29.48 ? 31   LEU   B CG    1 
ATOM   8896  C  CD1   . LEU   B  1 33   ? -6.921  -2.076  93.783  1.00 25.95 ? 31   LEU   B CD1   1 
ATOM   8897  C  CD2   . LEU   B  1 33   ? -8.257  -0.684  92.206  1.00 29.37 ? 31   LEU   B CD2   1 
ATOM   8898  N  N     . ARG   B  1 34   ? -3.409  1.409   91.131  1.00 24.47 ? 32   ARG   B N     1 
ATOM   8899  C  CA    . ARG   B  1 34   ? -2.579  2.612   91.094  1.00 26.80 ? 32   ARG   B CA    1 
ATOM   8900  C  C     . ARG   B  1 34   ? -2.722  3.329   89.757  1.00 27.71 ? 32   ARG   B C     1 
ATOM   8901  O  O     . ARG   B  1 34   ? -2.795  4.563   89.709  1.00 23.69 ? 32   ARG   B O     1 
ATOM   8902  C  CB    . ARG   B  1 34   ? -1.116  2.262   91.370  1.00 22.88 ? 32   ARG   B CB    1 
ATOM   8903  C  CG    . ARG   B  1 34   ? -0.839  1.833   92.801  1.00 23.81 ? 32   ARG   B CG    1 
ATOM   8904  C  CD    . ARG   B  1 34   ? -0.940  3.009   93.775  1.00 25.43 ? 32   ARG   B CD    1 
ATOM   8905  N  NE    . ARG   B  1 34   ? 0.083   4.014   93.511  1.00 24.11 ? 32   ARG   B NE    1 
ATOM   8906  C  CZ    . ARG   B  1 34   ? 1.302   4.003   94.028  1.00 27.31 ? 32   ARG   B CZ    1 
ATOM   8907  N  NH1   . ARG   B  1 34   ? 1.670   3.086   94.913  1.00 28.68 ? 32   ARG   B NH1   1 
ATOM   8908  N  NH2   . ARG   B  1 34   ? 2.170   4.943   93.660  1.00 25.47 ? 32   ARG   B NH2   1 
ATOM   8909  N  N     . ARG   B  1 35   ? -2.783  2.576   88.658  1.00 24.64 ? 33   ARG   B N     1 
ATOM   8910  C  CA    . ARG   B  1 35   ? -2.914  3.219   87.359  1.00 27.03 ? 33   ARG   B CA    1 
ATOM   8911  C  C     . ARG   B  1 35   ? -4.262  3.915   87.220  1.00 23.03 ? 33   ARG   B C     1 
ATOM   8912  O  O     . ARG   B  1 35   ? -4.359  4.928   86.522  1.00 22.97 ? 33   ARG   B O     1 
ATOM   8913  C  CB    . ARG   B  1 35   ? -2.706  2.198   86.235  1.00 26.20 ? 33   ARG   B CB    1 
ATOM   8914  C  CG    . ARG   B  1 35   ? -1.273  1.658   86.185  1.00 31.59 ? 33   ARG   B CG    1 
ATOM   8915  C  CD    . ARG   B  1 35   ? -0.992  0.849   84.928  1.00 34.52 ? 33   ARG   B CD    1 
ATOM   8916  N  NE    . ARG   B  1 35   ? -2.041  -0.126  84.662  1.00 46.75 ? 33   ARG   B NE    1 
ATOM   8917  C  CZ    . ARG   B  1 35   ? -2.031  -1.385  85.085  1.00 45.84 ? 33   ARG   B CZ    1 
ATOM   8918  N  NH1   . ARG   B  1 35   ? -1.029  -1.867  85.808  1.00 42.68 ? 33   ARG   B NH1   1 
ATOM   8919  N  NH2   . ARG   B  1 35   ? -3.050  -2.183  84.773  1.00 40.20 ? 33   ARG   B NH2   1 
ATOM   8920  N  N     . ALA   B  1 36   ? -5.299  3.402   87.891  1.00 21.61 ? 34   ALA   B N     1 
ATOM   8921  C  CA    . ALA   B  1 36   ? -6.602  4.059   87.842  1.00 24.71 ? 34   ALA   B CA    1 
ATOM   8922  C  C     . ALA   B  1 36   ? -6.565  5.392   88.573  1.00 23.28 ? 34   ALA   B C     1 
ATOM   8923  O  O     . ALA   B  1 36   ? -7.205  6.360   88.151  1.00 21.75 ? 34   ALA   B O     1 
ATOM   8924  C  CB    . ALA   B  1 36   ? -7.677  3.154   88.441  1.00 26.27 ? 34   ALA   B CB    1 
ATOM   8925  N  N     . ILE   B  1 37   ? -5.832  5.455   89.683  1.00 22.77 ? 35   ILE   B N     1 
ATOM   8926  C  CA    . ILE   B  1 37   ? -5.598  6.728   90.358  1.00 22.55 ? 35   ILE   B CA    1 
ATOM   8927  C  C     . ILE   B  1 37   ? -4.934  7.718   89.412  1.00 21.67 ? 35   ILE   B C     1 
ATOM   8928  O  O     . ILE   B  1 37   ? -5.409  8.844   89.219  1.00 20.68 ? 35   ILE   B O     1 
ATOM   8929  C  CB    . ILE   B  1 37   ? -4.734  6.503   91.608  1.00 21.57 ? 35   ILE   B CB    1 
ATOM   8930  C  CG1   . ILE   B  1 37   ? -5.509  5.718   92.653  1.00 21.05 ? 35   ILE   B CG1   1 
ATOM   8931  C  CG2   . ILE   B  1 37   ? -4.184  7.841   92.148  1.00 20.64 ? 35   ILE   B CG2   1 
ATOM   8932  C  CD1   . ILE   B  1 37   ? -4.598  5.142   93.741  1.00 22.07 ? 35   ILE   B CD1   1 
ATOM   8933  N  N     . THR   B  1 38   ? -3.810  7.313   88.824  1.00 19.22 ? 36   THR   B N     1 
ATOM   8934  C  CA    . THR   B  1 38   ? -3.054  8.219   87.974  1.00 21.76 ? 36   THR   B CA    1 
ATOM   8935  C  C     . THR   B  1 38   ? -3.896  8.695   86.802  1.00 20.98 ? 36   THR   B C     1 
ATOM   8936  O  O     . THR   B  1 38   ? -3.816  9.865   86.404  1.00 21.03 ? 36   THR   B O     1 
ATOM   8937  C  CB    . THR   B  1 38   ? -1.788  7.525   87.479  1.00 23.74 ? 36   THR   B CB    1 
ATOM   8938  O  OG1   . THR   B  1 38   ? -1.060  7.021   88.608  1.00 22.44 ? 36   THR   B OG1   1 
ATOM   8939  C  CG2   . THR   B  1 38   ? -0.924  8.503   86.698  1.00 22.66 ? 36   THR   B CG2   1 
ATOM   8940  N  N     . ALA   B  1 39   ? -4.708  7.797   86.247  1.00 20.27 ? 37   ALA   B N     1 
ATOM   8941  C  CA    . ALA   B  1 39   ? -5.551  8.133   85.104  1.00 23.32 ? 37   ALA   B CA    1 
ATOM   8942  C  C     . ALA   B  1 39   ? -6.523  9.260   85.428  1.00 23.65 ? 37   ALA   B C     1 
ATOM   8943  O  O     . ALA   B  1 39   ? -6.928  10.007  84.532  1.00 23.00 ? 37   ALA   B O     1 
ATOM   8944  C  CB    . ALA   B  1 39   ? -6.317  6.890   84.651  1.00 22.05 ? 37   ALA   B CB    1 
ATOM   8945  N  N     . ALA   B  1 40   ? -6.913  9.391   86.692  1.00 22.81 ? 38   ALA   B N     1 
ATOM   8946  C  CA    . ALA   B  1 40   ? -7.900  10.374  87.119  1.00 22.68 ? 38   ALA   B CA    1 
ATOM   8947  C  C     . ALA   B  1 40   ? -7.286  11.718  87.479  1.00 22.03 ? 38   ALA   B C     1 
ATOM   8948  O  O     . ALA   B  1 40   ? -8.036  12.664  87.745  1.00 22.77 ? 38   ALA   B O     1 
ATOM   8949  C  CB    . ALA   B  1 40   ? -8.685  9.844   88.330  1.00 18.05 ? 38   ALA   B CB    1 
ATOM   8950  N  N     . TYR   B  1 41   ? -5.950  11.814  87.476  1.00 19.63 ? 39   TYR   B N     1 
ATOM   8951  C  CA    . TYR   B  1 41   ? -5.242  12.954  88.058  1.00 19.23 ? 39   TYR   B CA    1 
ATOM   8952  C  C     . TYR   B  1 41   ? -5.850  14.282  87.611  1.00 21.82 ? 39   TYR   B C     1 
ATOM   8953  O  O     . TYR   B  1 41   ? -6.198  15.133  88.438  1.00 20.05 ? 39   TYR   B O     1 
ATOM   8954  C  CB    . TYR   B  1 41   ? -3.760  12.856  87.666  1.00 17.99 ? 39   TYR   B CB    1 
ATOM   8955  C  CG    . TYR   B  1 41   ? -2.750  13.559  88.549  1.00 17.97 ? 39   TYR   B CG    1 
ATOM   8956  C  CD1   . TYR   B  1 41   ? -3.082  14.699  89.270  1.00 17.80 ? 39   TYR   B CD1   1 
ATOM   8957  C  CD2   . TYR   B  1 41   ? -1.440  13.086  88.632  1.00 20.55 ? 39   TYR   B CD2   1 
ATOM   8958  C  CE1   . TYR   B  1 41   ? -2.140  15.349  90.056  1.00 19.37 ? 39   TYR   B CE1   1 
ATOM   8959  C  CE2   . TYR   B  1 41   ? -0.500  13.716  89.414  1.00 18.25 ? 39   TYR   B CE2   1 
ATOM   8960  C  CZ    . TYR   B  1 41   ? -0.850  14.853  90.116  1.00 18.12 ? 39   TYR   B CZ    1 
ATOM   8961  O  OH    . TYR   B  1 41   ? 0.087   15.489  90.880  1.00 17.87 ? 39   TYR   B OH    1 
ATOM   8962  N  N     . ARG   B  1 42   ? -6.014  14.467  86.304  1.00 20.07 ? 40   ARG   B N     1 
ATOM   8963  C  CA    . ARG   B  1 42   ? -6.519  15.730  85.774  1.00 18.39 ? 40   ARG   B CA    1 
ATOM   8964  C  C     . ARG   B  1 42   ? -7.693  15.493  84.845  1.00 21.04 ? 40   ARG   B C     1 
ATOM   8965  O  O     . ARG   B  1 42   ? -7.846  16.158  83.816  1.00 24.68 ? 40   ARG   B O     1 
ATOM   8966  C  CB    . ARG   B  1 42   ? -5.402  16.512  85.092  1.00 20.23 ? 40   ARG   B CB    1 
ATOM   8967  C  CG    . ARG   B  1 42   ? -4.396  16.972  86.143  1.00 18.96 ? 40   ARG   B CG    1 
ATOM   8968  C  CD    . ARG   B  1 42   ? -3.143  17.539  85.552  1.00 21.29 ? 40   ARG   B CD    1 
ATOM   8969  N  NE    . ARG   B  1 42   ? -2.071  17.451  86.534  1.00 20.27 ? 40   ARG   B NE    1 
ATOM   8970  C  CZ    . ARG   B  1 42   ? -1.853  18.347  87.486  1.00 21.33 ? 40   ARG   B CZ    1 
ATOM   8971  N  NH1   . ARG   B  1 42   ? -2.576  19.451  87.575  1.00 18.84 ? 40   ARG   B NH1   1 
ATOM   8972  N  NH2   . ARG   B  1 42   ? -0.874  18.137  88.360  1.00 19.65 ? 40   ARG   B NH2   1 
ATOM   8973  N  N     . ARG   B  1 43   ? -8.557  14.567  85.233  1.00 19.58 ? 41   ARG   B N     1 
ATOM   8974  C  CA    . ARG   B  1 43   ? -9.703  14.218  84.415  1.00 22.15 ? 41   ARG   B CA    1 
ATOM   8975  C  C     . ARG   B  1 43   ? -10.635 15.422  84.297  1.00 21.45 ? 41   ARG   B C     1 
ATOM   8976  O  O     . ARG   B  1 43   ? -10.830 16.150  85.277  1.00 21.02 ? 41   ARG   B O     1 
ATOM   8977  C  CB    . ARG   B  1 43   ? -10.433 13.030  85.043  1.00 23.13 ? 41   ARG   B CB    1 
ATOM   8978  C  CG    . ARG   B  1 43   ? -11.681 12.569  84.329  1.00 24.28 ? 41   ARG   B CG    1 
ATOM   8979  C  CD    . ARG   B  1 43   ? -12.039 11.173  84.815  1.00 23.79 ? 41   ARG   B CD    1 
ATOM   8980  N  NE    . ARG   B  1 43   ? -11.034 10.205  84.383  1.00 27.64 ? 41   ARG   B NE    1 
ATOM   8981  C  CZ    . ARG   B  1 43   ? -10.703 9.117   85.063  1.00 25.54 ? 41   ARG   B CZ    1 
ATOM   8982  N  NH1   . ARG   B  1 43   ? -11.290 8.814   86.207  1.00 24.12 ? 41   ARG   B NH1   1 
ATOM   8983  N  NH2   . ARG   B  1 43   ? -9.751  8.316   84.586  1.00 26.06 ? 41   ARG   B NH2   1 
ATOM   8984  N  N     . PRO   B  1 44   ? -11.189 15.689  83.113  1.00 22.43 ? 42   PRO   B N     1 
ATOM   8985  C  CA    . PRO   B  1 44   ? -12.147 16.791  82.986  1.00 21.88 ? 42   PRO   B CA    1 
ATOM   8986  C  C     . PRO   B  1 44   ? -13.242 16.698  84.041  1.00 25.10 ? 42   PRO   B C     1 
ATOM   8987  O  O     . PRO   B  1 44   ? -13.734 15.616  84.370  1.00 23.98 ? 42   PRO   B O     1 
ATOM   8988  C  CB    . PRO   B  1 44   ? -12.703 16.609  81.569  1.00 27.16 ? 42   PRO   B CB    1 
ATOM   8989  C  CG    . PRO   B  1 44   ? -11.550 16.011  80.819  1.00 28.08 ? 42   PRO   B CG    1 
ATOM   8990  C  CD    . PRO   B  1 44   ? -10.843 15.104  81.804  1.00 24.31 ? 42   PRO   B CD    1 
ATOM   8991  N  N     . GLU   B  1 45   ? -13.613 17.860  84.576  1.00 23.23 ? 43   GLU   B N     1 
ATOM   8992  C  CA    . GLU   B  1 45   ? -14.612 17.912  85.632  1.00 23.23 ? 43   GLU   B CA    1 
ATOM   8993  C  C     . GLU   B  1 45   ? -15.943 17.336  85.167  1.00 26.29 ? 43   GLU   B C     1 
ATOM   8994  O  O     . GLU   B  1 45   ? -16.646 16.679  85.942  1.00 25.26 ? 43   GLU   B O     1 
ATOM   8995  C  CB    . GLU   B  1 45   ? -14.762 19.358  86.112  1.00 25.32 ? 43   GLU   B CB    1 
ATOM   8996  C  CG    . GLU   B  1 45   ? -14.831 19.480  87.624  1.00 27.80 ? 43   GLU   B CG    1 
ATOM   8997  C  CD    . GLU   B  1 45   ? -14.497 20.869  88.146  1.00 22.80 ? 43   GLU   B CD    1 
ATOM   8998  O  OE1   . GLU   B  1 45   ? -13.761 21.630  87.477  1.00 22.51 ? 43   GLU   B OE1   1 
ATOM   8999  O  OE2   . GLU   B  1 45   ? -14.975 21.185  89.251  1.00 24.95 ? 43   GLU   B OE2   1 
ATOM   9000  N  N     . THR   B  1 46   ? -16.301 17.549  83.896  1.00 26.45 ? 44   THR   B N     1 
ATOM   9001  C  CA    . THR   B  1 46   ? -17.556 16.995  83.396  1.00 26.81 ? 44   THR   B CA    1 
ATOM   9002  C  C     . THR   B  1 46   ? -17.538 15.473  83.330  1.00 26.93 ? 44   THR   B C     1 
ATOM   9003  O  O     . THR   B  1 46   ? -18.604 14.856  83.318  1.00 28.22 ? 44   THR   B O     1 
ATOM   9004  C  CB    . THR   B  1 46   ? -17.875 17.559  82.013  1.00 24.74 ? 44   THR   B CB    1 
ATOM   9005  O  OG1   . THR   B  1 46   ? -16.725 17.414  81.172  1.00 24.87 ? 44   THR   B OG1   1 
ATOM   9006  C  CG2   . THR   B  1 46   ? -18.251 19.043  82.118  1.00 27.21 ? 44   THR   B CG2   1 
ATOM   9007  N  N     . GLU   B  1 47   ? -16.361 14.855  83.271  1.00 23.31 ? 45   GLU   B N     1 
ATOM   9008  C  CA    . GLU   B  1 47   ? -16.280 13.403  83.343  1.00 25.48 ? 45   GLU   B CA    1 
ATOM   9009  C  C     . GLU   B  1 47   ? -16.232 12.898  84.777  1.00 24.84 ? 45   GLU   B C     1 
ATOM   9010  O  O     . GLU   B  1 47   ? -16.712 11.792  85.046  1.00 26.57 ? 45   GLU   B O     1 
ATOM   9011  C  CB    . GLU   B  1 47   ? -15.054 12.909  82.560  1.00 27.27 ? 45   GLU   B CB    1 
ATOM   9012  C  CG    . GLU   B  1 47   ? -15.160 13.183  81.062  1.00 30.62 ? 45   GLU   B CG    1 
ATOM   9013  C  CD    . GLU   B  1 47   ? -13.847 13.021  80.311  1.00 38.54 ? 45   GLU   B CD    1 
ATOM   9014  O  OE1   . GLU   B  1 47   ? -12.973 12.247  80.763  1.00 36.10 ? 45   GLU   B OE1   1 
ATOM   9015  O  OE2   . GLU   B  1 47   ? -13.696 13.672  79.253  1.00 42.91 ? 45   GLU   B OE2   1 
ATOM   9016  N  N     . CYS   B  1 48   ? -15.704 13.700  85.708  1.00 24.40 ? 46   CYS   B N     1 
ATOM   9017  C  CA    . CYS   B  1 48   ? -15.596 13.266  87.105  1.00 25.83 ? 46   CYS   B CA    1 
ATOM   9018  C  C     . CYS   B  1 48   ? -16.952 13.227  87.793  1.00 26.81 ? 46   CYS   B C     1 
ATOM   9019  O  O     . CYS   B  1 48   ? -17.235 12.316  88.578  1.00 24.23 ? 46   CYS   B O     1 
ATOM   9020  C  CB    . CYS   B  1 48   ? -14.685 14.202  87.894  1.00 21.71 ? 46   CYS   B CB    1 
ATOM   9021  S  SG    . CYS   B  1 48   ? -12.967 14.177  87.445  1.00 24.80 ? 46   CYS   B SG    1 
ATOM   9022  N  N     . LEU   B  1 49   ? -17.784 14.212  87.539  1.00 23.90 ? 47   LEU   B N     1 
ATOM   9023  C  CA    . LEU   B  1 49   ? -18.954 14.406  88.385  1.00 28.03 ? 47   LEU   B CA    1 
ATOM   9024  C  C     . LEU   B  1 49   ? -20.072 13.379  88.218  1.00 24.08 ? 47   LEU   B C     1 
ATOM   9025  O  O     . LEU   B  1 49   ? -20.643 12.969  89.231  1.00 26.22 ? 47   LEU   B O     1 
ATOM   9026  C  CB    . LEU   B  1 49   ? -19.516 15.811  88.180  1.00 23.74 ? 47   LEU   B CB    1 
ATOM   9027  C  CG    . LEU   B  1 49   ? -19.079 16.785  89.284  1.00 24.59 ? 47   LEU   B CG    1 
ATOM   9028  C  CD1   . LEU   B  1 49   ? -19.561 16.315  90.660  1.00 24.68 ? 47   LEU   B CD1   1 
ATOM   9029  C  CD2   . LEU   B  1 49   ? -17.562 16.975  89.276  1.00 22.67 ? 47   LEU   B CD2   1 
ATOM   9030  N  N     . PRO   B  1 50   ? -20.436 12.940  87.010  1.00 26.39 ? 48   PRO   B N     1 
ATOM   9031  C  CA    . PRO   B  1 50   ? -21.617 12.053  86.877  1.00 27.28 ? 48   PRO   B CA    1 
ATOM   9032  C  C     . PRO   B  1 50   ? -21.501 10.784  87.712  1.00 28.63 ? 48   PRO   B C     1 
ATOM   9033  O  O     . PRO   B  1 50   ? -22.453 10.438  88.425  1.00 29.60 ? 48   PRO   B O     1 
ATOM   9034  C  CB    . PRO   B  1 50   ? -21.672 11.756  85.369  1.00 27.93 ? 48   PRO   B CB    1 
ATOM   9035  C  CG    . PRO   B  1 50   ? -21.138 13.005  84.767  1.00 26.16 ? 48   PRO   B CG    1 
ATOM   9036  C  CD    . PRO   B  1 50   ? -20.005 13.430  85.686  1.00 27.34 ? 48   PRO   B CD    1 
ATOM   9037  N  N     . PRO   B  1 51   ? -20.371 10.064  87.689  1.00 29.04 ? 49   PRO   B N     1 
ATOM   9038  C  CA    . PRO   B  1 51   ? -20.269 8.908   88.596  1.00 28.56 ? 49   PRO   B CA    1 
ATOM   9039  C  C     . PRO   B  1 51   ? -20.333 9.288   90.068  1.00 30.41 ? 49   PRO   B C     1 
ATOM   9040  O  O     . PRO   B  1 51   ? -20.809 8.487   90.883  1.00 28.66 ? 49   PRO   B O     1 
ATOM   9041  C  CB    . PRO   B  1 51   ? -18.916 8.281   88.228  1.00 31.08 ? 49   PRO   B CB    1 
ATOM   9042  C  CG    . PRO   B  1 51   ? -18.162 9.353   87.546  1.00 30.45 ? 49   PRO   B CG    1 
ATOM   9043  C  CD    . PRO   B  1 51   ? -19.196 10.140  86.800  1.00 27.80 ? 49   PRO   B CD    1 
ATOM   9044  N  N     . LEU   B  1 52   ? -19.887 10.491  90.439  1.00 24.20 ? 50   LEU   B N     1 
ATOM   9045  C  CA    . LEU   B  1 52   ? -19.969 10.888  91.843  1.00 27.23 ? 50   LEU   B CA    1 
ATOM   9046  C  C     . LEU   B  1 52   ? -21.405 11.226  92.232  1.00 29.15 ? 50   LEU   B C     1 
ATOM   9047  O  O     . LEU   B  1 52   ? -21.853 10.873  93.328  1.00 28.31 ? 50   LEU   B O     1 
ATOM   9048  C  CB    . LEU   B  1 52   ? -19.040 12.074  92.121  1.00 27.50 ? 50   LEU   B CB    1 
ATOM   9049  C  CG    . LEU   B  1 52   ? -17.539 11.860  91.895  1.00 23.09 ? 50   LEU   B CG    1 
ATOM   9050  C  CD1   . LEU   B  1 52   ? -16.759 13.177  92.041  1.00 24.42 ? 50   LEU   B CD1   1 
ATOM   9051  C  CD2   . LEU   B  1 52   ? -16.997 10.829  92.863  1.00 28.13 ? 50   LEU   B CD2   1 
ATOM   9052  N  N     . VAL   B  1 53   ? -22.144 11.895  91.339  1.00 27.63 ? 51   VAL   B N     1 
ATOM   9053  C  CA    . VAL   B  1 53   ? -23.557 12.170  91.593  1.00 30.24 ? 51   VAL   B CA    1 
ATOM   9054  C  C     . VAL   B  1 53   ? -24.316 10.871  91.826  1.00 30.61 ? 51   VAL   B C     1 
ATOM   9055  O  O     . VAL   B  1 53   ? -25.106 10.748  92.773  1.00 30.23 ? 51   VAL   B O     1 
ATOM   9056  C  CB    . VAL   B  1 53   ? -24.165 12.971  90.428  1.00 29.57 ? 51   VAL   B CB    1 
ATOM   9057  C  CG1   . VAL   B  1 53   ? -25.690 13.072  90.598  1.00 31.77 ? 51   VAL   B CG1   1 
ATOM   9058  C  CG2   . VAL   B  1 53   ? -23.523 14.350  90.361  1.00 25.35 ? 51   VAL   B CG2   1 
ATOM   9059  N  N     . GLU   B  1 54   ? -24.076 9.876   90.975  1.00 30.70 ? 52   GLU   B N     1 
ATOM   9060  C  CA    . GLU   B  1 54   ? -24.773 8.600   91.121  1.00 34.45 ? 52   GLU   B CA    1 
ATOM   9061  C  C     . GLU   B  1 54   ? -24.440 7.949   92.456  1.00 34.12 ? 52   GLU   B C     1 
ATOM   9062  O  O     . GLU   B  1 54   ? -25.331 7.454   93.157  1.00 33.59 ? 52   GLU   B O     1 
ATOM   9063  C  CB    . GLU   B  1 54   ? -24.414 7.673   89.961  1.00 32.57 ? 52   GLU   B CB    1 
ATOM   9064  N  N     . ALA   B  1 55   ? -23.159 7.960   92.836  1.00 29.98 ? 53   ALA   B N     1 
ATOM   9065  C  CA    . ALA   B  1 55   ? -22.743 7.337   94.092  1.00 33.42 ? 53   ALA   B CA    1 
ATOM   9066  C  C     . ALA   B  1 55   ? -23.294 8.073   95.305  1.00 31.86 ? 53   ALA   B C     1 
ATOM   9067  O  O     . ALA   B  1 55   ? -23.558 7.450   96.339  1.00 34.72 ? 53   ALA   B O     1 
ATOM   9068  C  CB    . ALA   B  1 55   ? -21.216 7.273   94.172  1.00 30.79 ? 53   ALA   B CB    1 
ATOM   9069  N  N     . ALA   B  1 56   ? -23.478 9.383   95.200  1.00 30.26 ? 54   ALA   B N     1 
ATOM   9070  C  CA    . ALA   B  1 56   ? -23.954 10.207  96.302  1.00 31.85 ? 54   ALA   B CA    1 
ATOM   9071  C  C     . ALA   B  1 56   ? -25.469 10.334  96.341  1.00 35.17 ? 54   ALA   B C     1 
ATOM   9072  O  O     . ALA   B  1 56   ? -25.999 10.944  97.274  1.00 36.61 ? 54   ALA   B O     1 
ATOM   9073  C  CB    . ALA   B  1 56   ? -23.329 11.600  96.213  1.00 29.93 ? 54   ALA   B CB    1 
ATOM   9074  N  N     . THR   B  1 57   ? -26.173 9.794   95.348  1.00 35.80 ? 55   THR   B N     1 
ATOM   9075  C  CA    . THR   B  1 57   ? -27.629 9.867   95.331  1.00 36.48 ? 55   THR   B CA    1 
ATOM   9076  C  C     . THR   B  1 57   ? -28.214 9.067   96.483  1.00 38.54 ? 55   THR   B C     1 
ATOM   9077  O  O     . THR   B  1 57   ? -27.769 7.953   96.773  1.00 40.74 ? 55   THR   B O     1 
ATOM   9078  C  CB    . THR   B  1 57   ? -28.168 9.343   93.998  1.00 36.10 ? 55   THR   B CB    1 
ATOM   9079  O  OG1   . THR   B  1 57   ? -27.847 10.280  92.969  1.00 34.01 ? 55   THR   B OG1   1 
ATOM   9080  C  CG2   . THR   B  1 57   ? -29.685 9.162   94.047  1.00 40.50 ? 55   THR   B CG2   1 
ATOM   9081  N  N     . GLN   B  1 58   ? -29.200 9.652   97.159  1.00 38.35 ? 56   GLN   B N     1 
ATOM   9082  C  CA    . GLN   B  1 58   ? -29.910 8.973   98.234  1.00 39.61 ? 56   GLN   B CA    1 
ATOM   9083  C  C     . GLN   B  1 58   ? -31.415 9.108   98.029  1.00 40.24 ? 56   GLN   B C     1 
ATOM   9084  O  O     . GLN   B  1 58   ? -31.888 9.978   97.296  1.00 38.19 ? 56   GLN   B O     1 
ATOM   9085  C  CB    . GLN   B  1 58   ? -29.510 9.523   99.604  1.00 39.07 ? 56   GLN   B CB    1 
ATOM   9086  C  CG    . GLN   B  1 58   ? -28.013 9.451   99.874  1.00 36.09 ? 56   GLN   B CG    1 
ATOM   9087  C  CD    . GLN   B  1 58   ? -27.689 9.628   101.334 1.00 40.08 ? 56   GLN   B CD    1 
ATOM   9088  O  OE1   . GLN   B  1 58   ? -27.785 8.683   102.118 1.00 41.91 ? 56   GLN   B OE1   1 
ATOM   9089  N  NE2   . GLN   B  1 58   ? -27.304 10.841  101.716 1.00 41.51 ? 56   GLN   B NE2   1 
ATOM   9090  N  N     . SER   B  1 59   ? -32.166 8.233   98.699  1.00 39.43 ? 57   SER   B N     1 
ATOM   9091  C  CA    . SER   B  1 59   ? -33.617 8.230   98.579  1.00 43.72 ? 57   SER   B CA    1 
ATOM   9092  C  C     . SER   B  1 59   ? -34.207 9.560   99.040  1.00 44.30 ? 57   SER   B C     1 
ATOM   9093  O  O     . SER   B  1 59   ? -33.566 10.349  99.739  1.00 39.80 ? 57   SER   B O     1 
ATOM   9094  C  CB    . SER   B  1 59   ? -34.216 7.095   99.407  1.00 43.47 ? 57   SER   B CB    1 
ATOM   9095  O  OG    . SER   B  1 59   ? -33.884 7.255   100.778 1.00 42.71 ? 57   SER   B OG    1 
ATOM   9096  N  N     . LYS   B  1 60   ? -35.460 9.799   98.644  1.00 42.08 ? 58   LYS   B N     1 
ATOM   9097  C  CA    . LYS   B  1 60   ? -36.160 10.996  99.102  1.00 42.21 ? 58   LYS   B CA    1 
ATOM   9098  C  C     . LYS   B  1 60   ? -36.350 10.968  100.612 1.00 41.38 ? 58   LYS   B C     1 
ATOM   9099  O  O     . LYS   B  1 60   ? -36.270 12.008  101.278 1.00 44.68 ? 58   LYS   B O     1 
ATOM   9100  C  CB    . LYS   B  1 60   ? -37.513 11.126  98.398  1.00 41.90 ? 58   LYS   B CB    1 
ATOM   9101  N  N     . GLU   B  1 61   ? -36.608 9.787   101.172 1.00 43.49 ? 59   GLU   B N     1 
ATOM   9102  C  CA    . GLU   B  1 61   ? -36.766 9.679   102.617 1.00 40.10 ? 59   GLU   B CA    1 
ATOM   9103  C  C     . GLU   B  1 61   ? -35.499 10.131  103.328 1.00 46.68 ? 59   GLU   B C     1 
ATOM   9104  O  O     . GLU   B  1 61   ? -35.544 10.967  104.238 1.00 46.05 ? 59   GLU   B O     1 
ATOM   9105  C  CB    . GLU   B  1 61   ? -37.130 8.243   103.002 1.00 45.07 ? 59   GLU   B CB    1 
ATOM   9106  N  N     . ILE   B  1 62   ? -34.348 9.608   102.900 1.00 42.94 ? 60   ILE   B N     1 
ATOM   9107  C  CA    . ILE   B  1 62   ? -33.081 9.983   103.522 1.00 42.52 ? 60   ILE   B CA    1 
ATOM   9108  C  C     . ILE   B  1 62   ? -32.791 11.462  103.299 1.00 40.98 ? 60   ILE   B C     1 
ATOM   9109  O  O     . ILE   B  1 62   ? -32.366 12.173  104.220 1.00 43.14 ? 60   ILE   B O     1 
ATOM   9110  C  CB    . ILE   B  1 62   ? -31.952 9.085   102.984 1.00 42.39 ? 60   ILE   B CB    1 
ATOM   9111  C  CG1   . ILE   B  1 62   ? -32.135 7.658   103.505 1.00 41.29 ? 60   ILE   B CG1   1 
ATOM   9112  C  CG2   . ILE   B  1 62   ? -30.577 9.659   103.337 1.00 39.93 ? 60   ILE   B CG2   1 
ATOM   9113  C  CD1   . ILE   B  1 62   ? -31.191 6.652   102.897 1.00 44.80 ? 60   ILE   B CD1   1 
ATOM   9114  N  N     . ARG   B  1 63   ? -33.032 11.954  102.079 1.00 36.27 ? 61   ARG   B N     1 
ATOM   9115  C  CA    . ARG   B  1 63   ? -32.735 13.348  101.766 1.00 37.39 ? 61   ARG   B CA    1 
ATOM   9116  C  C     . ARG   B  1 63   ? -33.573 14.296  102.610 1.00 39.76 ? 61   ARG   B C     1 
ATOM   9117  O  O     . ARG   B  1 63   ? -33.082 15.340  103.055 1.00 39.38 ? 61   ARG   B O     1 
ATOM   9118  C  CB    . ARG   B  1 63   ? -32.964 13.615  100.278 1.00 37.25 ? 61   ARG   B CB    1 
ATOM   9119  C  CG    . ARG   B  1 63   ? -31.780 13.283  99.401  1.00 44.40 ? 61   ARG   B CG    1 
ATOM   9120  C  CD    . ARG   B  1 63   ? -32.232 12.989  97.986  1.00 46.13 ? 61   ARG   B CD    1 
ATOM   9121  N  NE    . ARG   B  1 63   ? -33.318 13.862  97.565  1.00 43.76 ? 61   ARG   B NE    1 
ATOM   9122  C  CZ    . ARG   B  1 63   ? -34.234 13.525  96.670  1.00 46.61 ? 61   ARG   B CZ    1 
ATOM   9123  N  NH1   . ARG   B  1 63   ? -34.232 12.332  96.095  1.00 44.46 ? 61   ARG   B NH1   1 
ATOM   9124  N  NH2   . ARG   B  1 63   ? -35.182 14.401  96.351  1.00 52.06 ? 61   ARG   B NH2   1 
ATOM   9125  N  N     . ASP   B  1 64   ? -34.847 13.958  102.820 1.00 40.01 ? 62   ASP   B N     1 
ATOM   9126  C  CA    . ASP   B  1 64   ? -35.695 14.759  103.693 1.00 40.06 ? 62   ASP   B CA    1 
ATOM   9127  C  C     . ASP   B  1 64   ? -35.226 14.668  105.141 1.00 38.88 ? 62   ASP   B C     1 
ATOM   9128  O  O     . ASP   B  1 64   ? -35.141 15.686  105.838 1.00 41.89 ? 62   ASP   B O     1 
ATOM   9129  C  CB    . ASP   B  1 64   ? -37.155 14.309  103.568 1.00 42.56 ? 62   ASP   B CB    1 
ATOM   9130  C  CG    . ASP   B  1 64   ? -37.707 14.460  102.148 1.00 40.34 ? 62   ASP   B CG    1 
ATOM   9131  O  OD1   . ASP   B  1 64   ? -37.017 15.024  101.283 1.00 43.72 ? 62   ASP   B OD1   1 
ATOM   9132  O  OD2   . ASP   B  1 64   ? -38.845 14.011  101.896 1.00 46.01 ? 62   ASP   B OD2   1 
ATOM   9133  N  N     . ALA   B  1 65   ? -34.914 13.456  105.611 1.00 39.17 ? 63   ALA   B N     1 
ATOM   9134  C  CA    . ALA   B  1 65   ? -34.414 13.292  106.974 1.00 40.42 ? 63   ALA   B CA    1 
ATOM   9135  C  C     . ALA   B  1 65   ? -33.065 13.976  107.171 1.00 41.61 ? 63   ALA   B C     1 
ATOM   9136  O  O     . ALA   B  1 65   ? -32.790 14.499  108.258 1.00 40.81 ? 63   ALA   B O     1 
ATOM   9137  C  CB    . ALA   B  1 65   ? -34.313 11.809  107.322 1.00 41.44 ? 63   ALA   B CB    1 
ATOM   9138  N  N     . ALA   B  1 66   ? -32.217 13.993  106.136 1.00 39.21 ? 64   ALA   B N     1 
ATOM   9139  C  CA    . ALA   B  1 66   ? -30.916 14.643  106.262 1.00 40.81 ? 64   ALA   B CA    1 
ATOM   9140  C  C     . ALA   B  1 66   ? -31.060 16.155  106.321 1.00 37.97 ? 64   ALA   B C     1 
ATOM   9141  O  O     . ALA   B  1 66   ? -30.387 16.817  107.117 1.00 37.12 ? 64   ALA   B O     1 
ATOM   9142  C  CB    . ALA   B  1 66   ? -30.006 14.235  105.105 1.00 33.11 ? 64   ALA   B CB    1 
ATOM   9143  N  N     . ALA   B  1 67   ? -31.952 16.714  105.501 1.00 37.54 ? 65   ALA   B N     1 
ATOM   9144  C  CA    . ALA   B  1 67   ? -32.169 18.155  105.520 1.00 36.67 ? 65   ALA   B CA    1 
ATOM   9145  C  C     . ALA   B  1 67   ? -32.725 18.604  106.862 1.00 40.08 ? 65   ALA   B C     1 
ATOM   9146  O  O     . ALA   B  1 67   ? -32.413 19.705  107.333 1.00 42.37 ? 65   ALA   B O     1 
ATOM   9147  C  CB    . ALA   B  1 67   ? -33.112 18.560  104.387 1.00 37.81 ? 65   ALA   B CB    1 
ATOM   9148  N  N     . SER   B  1 68   ? -33.553 17.765  107.493 1.00 40.25 ? 66   SER   B N     1 
ATOM   9149  C  CA    . SER   B  1 68   ? -34.097 18.111  108.802 1.00 43.74 ? 66   SER   B CA    1 
ATOM   9150  C  C     . SER   B  1 68   ? -33.017 18.026  109.876 1.00 41.21 ? 66   SER   B C     1 
ATOM   9151  O  O     . SER   B  1 68   ? -32.855 18.952  110.680 1.00 44.64 ? 66   SER   B O     1 
ATOM   9152  C  CB    . SER   B  1 68   ? -35.281 17.203  109.140 1.00 40.21 ? 66   SER   B CB    1 
ATOM   9153  N  N     . THR   B  1 69   ? -32.260 16.925  109.896 1.00 42.03 ? 67   THR   B N     1 
ATOM   9154  C  CA    . THR   B  1 69   ? -31.108 16.840  110.788 1.00 36.64 ? 67   THR   B CA    1 
ATOM   9155  C  C     . THR   B  1 69   ? -30.165 18.019  110.573 1.00 39.97 ? 67   THR   B C     1 
ATOM   9156  O  O     . THR   B  1 69   ? -29.760 18.684  111.530 1.00 42.10 ? 67   THR   B O     1 
ATOM   9157  C  CB    . THR   B  1 69   ? -30.369 15.519  110.581 1.00 41.01 ? 67   THR   B CB    1 
ATOM   9158  O  OG1   . THR   B  1 69   ? -31.204 14.426  110.987 1.00 41.56 ? 67   THR   B OG1   1 
ATOM   9159  C  CG2   . THR   B  1 69   ? -29.064 15.497  111.388 1.00 36.35 ? 67   THR   B CG2   1 
ATOM   9160  N  N     . ALA   B  1 70   ? -29.815 18.301  109.310 1.00 36.32 ? 68   ALA   B N     1 
ATOM   9161  C  CA    . ALA   B  1 70   ? -28.976 19.459  109.017 1.00 38.77 ? 68   ALA   B CA    1 
ATOM   9162  C  C     . ALA   B  1 70   ? -29.614 20.750  109.517 1.00 39.50 ? 68   ALA   B C     1 
ATOM   9163  O  O     . ALA   B  1 70   ? -28.919 21.632  110.035 1.00 41.99 ? 68   ALA   B O     1 
ATOM   9164  C  CB    . ALA   B  1 70   ? -28.685 19.551  107.512 1.00 36.30 ? 68   ALA   B CB    1 
ATOM   9165  N  N     . ARG   B  1 71   ? -30.935 20.889  109.367 1.00 40.20 ? 69   ARG   B N     1 
ATOM   9166  C  CA    . ARG   B  1 71   ? -31.593 22.104  109.838 1.00 39.23 ? 69   ARG   B CA    1 
ATOM   9167  C  C     . ARG   B  1 71   ? -31.495 22.231  111.354 1.00 36.32 ? 69   ARG   B C     1 
ATOM   9168  O  O     . ARG   B  1 71   ? -31.226 23.318  111.875 1.00 40.48 ? 69   ARG   B O     1 
ATOM   9169  C  CB    . ARG   B  1 71   ? -33.057 22.131  109.392 1.00 41.67 ? 69   ARG   B CB    1 
ATOM   9170  C  CG    . ARG   B  1 71   ? -33.822 23.333  109.935 1.00 41.80 ? 69   ARG   B CG    1 
ATOM   9171  C  CD    . ARG   B  1 71   ? -35.223 23.481  109.325 1.00 43.96 ? 69   ARG   B CD    1 
ATOM   9172  N  NE    . ARG   B  1 71   ? -35.219 24.237  108.077 1.00 46.14 ? 69   ARG   B NE    1 
ATOM   9173  C  CZ    . ARG   B  1 71   ? -35.020 25.547  107.993 1.00 50.83 ? 69   ARG   B CZ    1 
ATOM   9174  N  NH1   . ARG   B  1 71   ? -34.759 26.279  109.066 1.00 47.77 ? 69   ARG   B NH1   1 
ATOM   9175  N  NH2   . ARG   B  1 71   ? -35.083 26.138  106.803 1.00 52.61 ? 69   ARG   B NH2   1 
ATOM   9176  N  N     . LYS   B  1 72   ? -31.711 21.128  112.077 1.00 42.53 ? 70   LYS   B N     1 
ATOM   9177  C  CA    . LYS   B  1 72   ? -31.589 21.156  113.532 1.00 39.57 ? 70   LYS   B CA    1 
ATOM   9178  C  C     . LYS   B  1 72   ? -30.170 21.516  113.961 1.00 43.21 ? 70   LYS   B C     1 
ATOM   9179  O  O     . LYS   B  1 72   ? -29.980 22.314  114.888 1.00 45.44 ? 70   LYS   B O     1 
ATOM   9180  C  CB    . LYS   B  1 72   ? -32.005 19.808  114.119 1.00 43.10 ? 70   LYS   B CB    1 
ATOM   9181  N  N     . LEU   B  1 73   ? -29.159 20.947  113.294 1.00 43.91 ? 71   LEU   B N     1 
ATOM   9182  C  CA    . LEU   B  1 73   ? -27.773 21.267  113.633 1.00 42.30 ? 71   LEU   B CA    1 
ATOM   9183  C  C     . LEU   B  1 73   ? -27.470 22.744  113.412 1.00 38.87 ? 71   LEU   B C     1 
ATOM   9184  O  O     . LEU   B  1 73   ? -26.814 23.379  114.242 1.00 39.63 ? 71   LEU   B O     1 
ATOM   9185  C  CB    . LEU   B  1 73   ? -26.814 20.400  112.816 1.00 40.25 ? 71   LEU   B CB    1 
ATOM   9186  C  CG    . LEU   B  1 73   ? -26.896 18.897  113.085 1.00 41.70 ? 71   LEU   B CG    1 
ATOM   9187  C  CD1   . LEU   B  1 73   ? -25.910 18.145  112.201 1.00 35.92 ? 71   LEU   B CD1   1 
ATOM   9188  C  CD2   . LEU   B  1 73   ? -26.643 18.606  114.557 1.00 42.98 ? 71   LEU   B CD2   1 
ATOM   9189  N  N     . ILE   B  1 74   ? -27.950 23.311  112.303 1.00 41.13 ? 72   ILE   B N     1 
ATOM   9190  C  CA    . ILE   B  1 74   ? -27.636 24.697  111.970 1.00 37.39 ? 72   ILE   B CA    1 
ATOM   9191  C  C     . ILE   B  1 74   ? -28.368 25.658  112.897 1.00 42.96 ? 72   ILE   B C     1 
ATOM   9192  O  O     . ILE   B  1 74   ? -27.809 26.677  113.327 1.00 44.02 ? 72   ILE   B O     1 
ATOM   9193  C  CB    . ILE   B  1 74   ? -27.963 24.972  110.493 1.00 41.44 ? 72   ILE   B CB    1 
ATOM   9194  C  CG1   . ILE   B  1 74   ? -26.931 24.278  109.602 1.00 40.17 ? 72   ILE   B CG1   1 
ATOM   9195  C  CG2   . ILE   B  1 74   ? -27.985 26.467  110.216 1.00 36.66 ? 72   ILE   B CG2   1 
ATOM   9196  C  CD1   . ILE   B  1 74   ? -27.318 24.218  108.147 1.00 36.30 ? 72   ILE   B CD1   1 
ATOM   9197  N  N     . GLU   B  1 75   ? -29.633 25.368  113.200 1.00 45.52 ? 73   GLU   B N     1 
ATOM   9198  C  CA    . GLU   B  1 75   ? -30.357 26.174  114.175 1.00 45.07 ? 73   GLU   B CA    1 
ATOM   9199  C  C     . GLU   B  1 75   ? -29.644 26.153  115.521 1.00 45.95 ? 73   GLU   B C     1 
ATOM   9200  O  O     . GLU   B  1 75   ? -29.439 27.201  116.147 1.00 47.88 ? 73   GLU   B O     1 
ATOM   9201  C  CB    . GLU   B  1 75   ? -31.793 25.667  114.304 1.00 40.17 ? 73   GLU   B CB    1 
ATOM   9202  N  N     . ALA   B  1 76   ? -29.233 24.964  115.967 1.00 43.30 ? 74   ALA   B N     1 
ATOM   9203  C  CA    . ALA   B  1 76   ? -28.466 24.861  117.203 1.00 45.95 ? 74   ALA   B CA    1 
ATOM   9204  C  C     . ALA   B  1 76   ? -27.200 25.704  117.130 1.00 47.39 ? 74   ALA   B C     1 
ATOM   9205  O  O     . ALA   B  1 76   ? -26.883 26.447  118.065 1.00 47.60 ? 74   ALA   B O     1 
ATOM   9206  C  CB    . ALA   B  1 76   ? -28.132 23.398  117.494 1.00 44.21 ? 74   ALA   B CB    1 
ATOM   9207  N  N     . LEU   B  1 77   ? -26.470 25.614  116.013 1.00 44.96 ? 75   LEU   B N     1 
ATOM   9208  C  CA    . LEU   B  1 77   ? -25.233 26.376  115.868 1.00 45.55 ? 75   LEU   B CA    1 
ATOM   9209  C  C     . LEU   B  1 77   ? -25.496 27.874  115.935 1.00 43.73 ? 75   LEU   B C     1 
ATOM   9210  O  O     . LEU   B  1 77   ? -24.803 28.608  116.647 1.00 44.75 ? 75   LEU   B O     1 
ATOM   9211  C  CB    . LEU   B  1 77   ? -24.541 26.012  114.550 1.00 42.07 ? 75   LEU   B CB    1 
ATOM   9212  C  CG    . LEU   B  1 77   ? -23.716 24.726  114.536 1.00 42.87 ? 75   LEU   B CG    1 
ATOM   9213  C  CD1   . LEU   B  1 77   ? -23.343 24.320  113.117 1.00 36.28 ? 75   LEU   B CD1   1 
ATOM   9214  C  CD2   . LEU   B  1 77   ? -22.475 24.928  115.368 1.00 42.26 ? 75   LEU   B CD2   1 
ATOM   9215  N  N     . ARG   B  1 78   ? -26.494 28.348  115.190 1.00 43.55 ? 76   ARG   B N     1 
ATOM   9216  C  CA    . ARG   B  1 78   ? -26.808 29.770  115.181 1.00 43.57 ? 76   ARG   B CA    1 
ATOM   9217  C  C     . ARG   B  1 78   ? -27.517 30.223  116.454 1.00 44.69 ? 76   ARG   B C     1 
ATOM   9218  O  O     . ARG   B  1 78   ? -27.610 31.431  116.692 1.00 44.45 ? 76   ARG   B O     1 
ATOM   9219  C  CB    . ARG   B  1 78   ? -27.658 30.100  113.957 1.00 44.11 ? 76   ARG   B CB    1 
ATOM   9220  C  CG    . ARG   B  1 78   ? -26.889 30.002  112.658 1.00 44.35 ? 76   ARG   B CG    1 
ATOM   9221  C  CD    . ARG   B  1 78   ? -27.767 30.321  111.469 1.00 44.88 ? 76   ARG   B CD    1 
ATOM   9222  N  NE    . ARG   B  1 78   ? -26.983 30.855  110.364 1.00 44.99 ? 76   ARG   B NE    1 
ATOM   9223  C  CZ    . ARG   B  1 78   ? -27.478 31.190  109.183 1.00 45.47 ? 76   ARG   B CZ    1 
ATOM   9224  N  NH1   . ARG   B  1 78   ? -28.758 31.007  108.893 1.00 49.28 ? 76   ARG   B NH1   1 
ATOM   9225  N  NH2   . ARG   B  1 78   ? -26.672 31.726  108.271 1.00 49.81 ? 76   ARG   B NH2   1 
ATOM   9226  N  N     . GLY   B  1 79   ? -28.016 29.290  117.269 1.00 46.90 ? 77   GLY   B N     1 
ATOM   9227  C  CA    . GLY   B  1 79   ? -28.576 29.657  118.557 1.00 47.75 ? 77   GLY   B CA    1 
ATOM   9228  C  C     . GLY   B  1 79   ? -27.543 30.002  119.607 1.00 50.35 ? 77   GLY   B C     1 
ATOM   9229  O  O     . GLY   B  1 79   ? -27.883 30.644  120.607 1.00 44.98 ? 77   GLY   B O     1 
ATOM   9230  N  N     . LYS   B  1 80   ? -26.292 29.603  119.391 1.00 50.80 ? 78   LYS   B N     1 
ATOM   9231  C  CA    . LYS   B  1 80   ? -25.200 29.834  120.330 1.00 49.68 ? 78   LYS   B CA    1 
ATOM   9232  C  C     . LYS   B  1 80   ? -24.195 30.844  119.769 1.00 55.85 ? 78   LYS   B C     1 
ATOM   9233  O  O     . LYS   B  1 80   ? -23.864 31.840  120.415 1.00 58.15 ? 78   LYS   B O     1 
ATOM   9234  C  CB    . LYS   B  1 80   ? -24.496 28.513  120.644 1.00 50.84 ? 78   LYS   B CB    1 
ATOM   9235  C  CG    . LYS   B  1 80   ? -25.449 27.339  120.795 1.00 49.86 ? 78   LYS   B CG    1 
ATOM   9236  C  CD    . LYS   B  1 80   ? -24.718 26.026  121.057 1.00 48.19 ? 78   LYS   B CD    1 
ATOM   9237  C  CE    . LYS   B  1 80   ? -23.898 25.580  119.856 1.00 48.69 ? 78   LYS   B CE    1 
ATOM   9238  N  NZ    . LYS   B  1 80   ? -23.534 24.137  119.961 1.00 47.78 ? 78   LYS   B NZ    1 
ATOM   9239  N  N     . GLY   B  1 85   ? -14.740 36.295  121.132 1.00 43.87 ? 83   GLY   B N     1 
ATOM   9240  C  CA    . GLY   B  1 85   ? -14.496 37.349  122.096 1.00 47.04 ? 83   GLY   B CA    1 
ATOM   9241  C  C     . GLY   B  1 85   ? -13.872 38.586  121.474 1.00 45.13 ? 83   GLY   B C     1 
ATOM   9242  O  O     . GLY   B  1 85   ? -13.838 39.651  122.091 1.00 42.34 ? 83   GLY   B O     1 
ATOM   9243  N  N     . VAL   B  1 86   ? -13.369 38.440  120.247 1.00 43.82 ? 84   VAL   B N     1 
ATOM   9244  C  CA    . VAL   B  1 86   ? -12.800 39.585  119.543 1.00 45.84 ? 84   VAL   B CA    1 
ATOM   9245  C  C     . VAL   B  1 86   ? -13.889 40.599  119.212 1.00 45.52 ? 84   VAL   B C     1 
ATOM   9246  O  O     . VAL   B  1 86   ? -13.717 41.805  119.428 1.00 44.12 ? 84   VAL   B O     1 
ATOM   9247  C  CB    . VAL   B  1 86   ? -12.046 39.125  118.283 1.00 46.52 ? 84   VAL   B CB    1 
ATOM   9248  C  CG1   . VAL   B  1 86   ? -11.742 40.313  117.383 1.00 46.46 ? 84   VAL   B CG1   1 
ATOM   9249  C  CG2   . VAL   B  1 86   ? -10.751 38.435  118.667 1.00 44.04 ? 84   VAL   B CG2   1 
ATOM   9250  N  N     . GLU   B  1 87   ? -15.033 40.127  118.709 1.00 46.98 ? 85   GLU   B N     1 
ATOM   9251  C  CA    . GLU   B  1 87   ? -16.134 41.029  118.387 1.00 43.63 ? 85   GLU   B CA    1 
ATOM   9252  C  C     . GLU   B  1 87   ? -16.589 41.807  119.613 1.00 46.07 ? 85   GLU   B C     1 
ATOM   9253  O  O     . GLU   B  1 87   ? -16.918 42.996  119.516 1.00 45.92 ? 85   GLU   B O     1 
ATOM   9254  C  CB    . GLU   B  1 87   ? -17.301 40.239  117.795 1.00 52.23 ? 85   GLU   B CB    1 
ATOM   9255  N  N     . GLY   B  1 88   ? -16.616 41.153  120.777 1.00 45.17 ? 86   GLY   B N     1 
ATOM   9256  C  CA    . GLY   B  1 88   ? -17.002 41.846  121.995 1.00 40.50 ? 86   GLY   B CA    1 
ATOM   9257  C  C     . GLY   B  1 88   ? -15.985 42.889  122.410 1.00 40.89 ? 86   GLY   B C     1 
ATOM   9258  O  O     . GLY   B  1 88   ? -16.347 43.957  122.912 1.00 37.33 ? 86   GLY   B O     1 
ATOM   9259  N  N     . LEU   B  1 89   ? -14.699 42.595  122.205 1.00 39.91 ? 87   LEU   B N     1 
ATOM   9260  C  CA    . LEU   B  1 89   ? -13.657 43.582  122.466 1.00 39.84 ? 87   LEU   B CA    1 
ATOM   9261  C  C     . LEU   B  1 89   ? -13.799 44.772  121.525 1.00 32.72 ? 87   LEU   B C     1 
ATOM   9262  O  O     . LEU   B  1 89   ? -13.750 45.928  121.956 1.00 34.28 ? 87   LEU   B O     1 
ATOM   9263  C  CB    . LEU   B  1 89   ? -12.279 42.931  122.317 1.00 39.12 ? 87   LEU   B CB    1 
ATOM   9264  C  CG    . LEU   B  1 89   ? -11.100 43.534  123.081 1.00 41.95 ? 87   LEU   B CG    1 
ATOM   9265  C  CD1   . LEU   B  1 89   ? -9.912  42.582  123.037 1.00 45.74 ? 87   LEU   B CD1   1 
ATOM   9266  C  CD2   . LEU   B  1 89   ? -10.701 44.889  122.518 1.00 38.73 ? 87   LEU   B CD2   1 
ATOM   9267  N  N     . VAL   B  1 90   ? -13.977 44.498  120.233 1.00 36.72 ? 88   VAL   B N     1 
ATOM   9268  C  CA    . VAL   B  1 90   ? -14.159 45.560  119.247 1.00 36.80 ? 88   VAL   B CA    1 
ATOM   9269  C  C     . VAL   B  1 90   ? -15.349 46.440  119.617 1.00 40.79 ? 88   VAL   B C     1 
ATOM   9270  O  O     . VAL   B  1 90   ? -15.282 47.674  119.531 1.00 38.47 ? 88   VAL   B O     1 
ATOM   9271  C  CB    . VAL   B  1 90   ? -14.315 44.948  117.843 1.00 34.34 ? 88   VAL   B CB    1 
ATOM   9272  C  CG1   . VAL   B  1 90   ? -14.849 45.978  116.862 1.00 34.85 ? 88   VAL   B CG1   1 
ATOM   9273  C  CG2   . VAL   B  1 90   ? -12.985 44.390  117.364 1.00 34.53 ? 88   VAL   B CG2   1 
ATOM   9274  N  N     . GLN   B  1 91   ? -16.445 45.824  120.070 1.00 41.04 ? 89   GLN   B N     1 
ATOM   9275  C  CA    . GLN   B  1 91   ? -17.630 46.601  120.423 1.00 36.42 ? 89   GLN   B CA    1 
ATOM   9276  C  C     . GLN   B  1 91   ? -17.436 47.363  121.728 1.00 39.02 ? 89   GLN   B C     1 
ATOM   9277  O  O     . GLN   B  1 91   ? -17.863 48.518  121.846 1.00 38.56 ? 89   GLN   B O     1 
ATOM   9278  C  CB    . GLN   B  1 91   ? -18.848 45.682  120.502 1.00 43.66 ? 89   GLN   B CB    1 
ATOM   9279  N  N     . GLU   B  1 92   ? -16.799 46.742  122.725 1.00 37.48 ? 90   GLU   B N     1 
ATOM   9280  C  CA    . GLU   B  1 92   ? -16.618 47.423  124.002 1.00 39.02 ? 90   GLU   B CA    1 
ATOM   9281  C  C     . GLU   B  1 92   ? -15.780 48.685  123.845 1.00 36.57 ? 90   GLU   B C     1 
ATOM   9282  O  O     . GLU   B  1 92   ? -16.055 49.705  124.487 1.00 34.23 ? 90   GLU   B O     1 
ATOM   9283  C  CB    . GLU   B  1 92   ? -15.974 46.486  125.027 1.00 37.33 ? 90   GLU   B CB    1 
ATOM   9284  C  CG    . GLU   B  1 92   ? -15.961 47.039  126.450 1.00 43.74 ? 90   GLU   B CG    1 
ATOM   9285  C  CD    . GLU   B  1 92   ? -15.141 46.182  127.413 1.00 44.31 ? 90   GLU   B CD    1 
ATOM   9286  O  OE1   . GLU   B  1 92   ? -14.724 45.071  127.020 1.00 45.46 ? 90   GLU   B OE1   1 
ATOM   9287  O  OE2   . GLU   B  1 92   ? -14.909 46.626  128.556 1.00 44.84 ? 90   GLU   B OE2   1 
ATOM   9288  N  N     . TYR   B  1 93   ? -14.751 48.641  123.003 1.00 34.18 ? 91   TYR   B N     1 
ATOM   9289  C  CA    . TYR   B  1 93   ? -13.852 49.775  122.851 1.00 34.69 ? 91   TYR   B CA    1 
ATOM   9290  C  C     . TYR   B  1 93   ? -14.063 50.520  121.543 1.00 32.32 ? 91   TYR   B C     1 
ATOM   9291  O  O     . TYR   B  1 93   ? -13.247 51.382  121.203 1.00 32.22 ? 91   TYR   B O     1 
ATOM   9292  C  CB    . TYR   B  1 93   ? -12.402 49.314  122.993 1.00 28.11 ? 91   TYR   B CB    1 
ATOM   9293  C  CG    . TYR   B  1 93   ? -12.101 48.961  124.424 1.00 31.51 ? 91   TYR   B CG    1 
ATOM   9294  C  CD1   . TYR   B  1 93   ? -11.733 49.944  125.335 1.00 29.94 ? 91   TYR   B CD1   1 
ATOM   9295  C  CD2   . TYR   B  1 93   ? -12.237 47.660  124.882 1.00 34.47 ? 91   TYR   B CD2   1 
ATOM   9296  C  CE1   . TYR   B  1 93   ? -11.484 49.638  126.654 1.00 33.94 ? 91   TYR   B CE1   1 
ATOM   9297  C  CE2   . TYR   B  1 93   ? -11.989 47.343  126.209 1.00 37.12 ? 91   TYR   B CE2   1 
ATOM   9298  C  CZ    . TYR   B  1 93   ? -11.609 48.337  127.084 1.00 34.50 ? 91   TYR   B CZ    1 
ATOM   9299  O  OH    . TYR   B  1 93   ? -11.363 48.030  128.400 1.00 36.47 ? 91   TYR   B OH    1 
ATOM   9300  N  N     . SER   B  1 94   ? -15.140 50.216  120.817 1.00 30.67 ? 92   SER   B N     1 
ATOM   9301  C  CA    . SER   B  1 94   ? -15.493 50.912  119.583 1.00 29.67 ? 92   SER   B CA    1 
ATOM   9302  C  C     . SER   B  1 94   ? -14.312 50.933  118.619 1.00 30.98 ? 92   SER   B C     1 
ATOM   9303  O  O     . SER   B  1 94   ? -13.963 51.967  118.045 1.00 31.84 ? 92   SER   B O     1 
ATOM   9304  C  CB    . SER   B  1 94   ? -15.983 52.332  119.870 1.00 32.33 ? 92   SER   B CB    1 
ATOM   9305  O  OG    . SER   B  1 94   ? -16.974 52.355  120.887 1.00 37.51 ? 92   SER   B OG    1 
ATOM   9306  N  N     . LEU   B  1 95   ? -13.694 49.768  118.442 1.00 28.40 ? 93   LEU   B N     1 
ATOM   9307  C  CA    . LEU   B  1 95   ? -12.521 49.660  117.591 1.00 26.87 ? 93   LEU   B CA    1 
ATOM   9308  C  C     . LEU   B  1 95   ? -12.921 49.550  116.134 1.00 28.44 ? 93   LEU   B C     1 
ATOM   9309  O  O     . LEU   B  1 95   ? -13.876 48.854  115.776 1.00 28.53 ? 93   LEU   B O     1 
ATOM   9310  C  CB    . LEU   B  1 95   ? -11.672 48.442  117.970 1.00 24.66 ? 93   LEU   B CB    1 
ATOM   9311  C  CG    . LEU   B  1 95   ? -11.166 48.346  119.410 1.00 29.70 ? 93   LEU   B CG    1 
ATOM   9312  C  CD1   . LEU   B  1 95   ? -10.239 47.145  119.555 1.00 26.34 ? 93   LEU   B CD1   1 
ATOM   9313  C  CD2   . LEU   B  1 95   ? -10.464 49.632  119.828 1.00 29.35 ? 93   LEU   B CD2   1 
ATOM   9314  N  N     . SER   B  1 96   ? -12.181 50.253  115.293 1.00 23.85 ? 94   SER   B N     1 
ATOM   9315  C  CA    . SER   B  1 96   ? -12.206 49.968  113.880 1.00 23.91 ? 94   SER   B CA    1 
ATOM   9316  C  C     . SER   B  1 96   ? -11.581 48.595  113.639 1.00 24.17 ? 94   SER   B C     1 
ATOM   9317  O  O     . SER   B  1 96   ? -10.930 48.019  114.520 1.00 25.90 ? 94   SER   B O     1 
ATOM   9318  C  CB    . SER   B  1 96   ? -11.445 51.046  113.120 1.00 23.95 ? 94   SER   B CB    1 
ATOM   9319  O  OG    . SER   B  1 96   ? -10.046 50.915  113.330 1.00 23.94 ? 94   SER   B OG    1 
ATOM   9320  N  N     . SER   B  1 97   ? -11.772 48.071  112.428 1.00 22.49 ? 95   SER   B N     1 
ATOM   9321  C  CA    . SER   B  1 97   ? -11.136 46.806  112.080 1.00 24.85 ? 95   SER   B CA    1 
ATOM   9322  C  C     . SER   B  1 97   ? -9.616  46.911  112.161 1.00 25.13 ? 95   SER   B C     1 
ATOM   9323  O  O     . SER   B  1 97   ? -8.957  46.019  112.706 1.00 22.10 ? 95   SER   B O     1 
ATOM   9324  C  CB    . SER   B  1 97   ? -11.566 46.362  110.680 1.00 26.03 ? 95   SER   B CB    1 
ATOM   9325  O  OG    . SER   B  1 97   ? -12.952 46.060  110.680 1.00 29.43 ? 95   SER   B OG    1 
ATOM   9326  N  N     . GLN   B  1 98   ? -9.044  47.993  111.618 1.00 22.01 ? 96   GLN   B N     1 
ATOM   9327  C  CA    . GLN   B  1 98   ? -7.596  48.171  111.671 1.00 23.10 ? 96   GLN   B CA    1 
ATOM   9328  C  C     . GLN   B  1 98   ? -7.116  48.319  113.106 1.00 25.31 ? 96   GLN   B C     1 
ATOM   9329  O  O     . GLN   B  1 98   ? -6.028  47.846  113.458 1.00 20.21 ? 96   GLN   B O     1 
ATOM   9330  C  CB    . GLN   B  1 98   ? -7.178  49.384  110.834 1.00 20.89 ? 96   GLN   B CB    1 
ATOM   9331  C  CG    . GLN   B  1 98   ? -7.198  49.142  109.319 1.00 23.23 ? 96   GLN   B CG    1 
ATOM   9332  C  CD    . GLN   B  1 98   ? -6.202  48.093  108.881 1.00 25.97 ? 96   GLN   B CD    1 
ATOM   9333  O  OE1   . GLN   B  1 98   ? -6.481  46.895  108.947 1.00 26.76 ? 96   GLN   B OE1   1 
ATOM   9334  N  NE2   . GLN   B  1 98   ? -5.029  48.533  108.427 1.00 23.03 ? 96   GLN   B NE2   1 
ATOM   9335  N  N     . GLU   B  1 99   ? -7.911  48.969  113.952 1.00 21.89 ? 97   GLU   B N     1 
ATOM   9336  C  CA    . GLU   B  1 99   ? -7.536  49.060  115.357 1.00 25.23 ? 97   GLU   B CA    1 
ATOM   9337  C  C     . GLU   B  1 99   ? -7.578  47.691  116.015 1.00 25.26 ? 97   GLU   B C     1 
ATOM   9338  O  O     . GLU   B  1 99   ? -6.689  47.352  116.804 1.00 22.85 ? 97   GLU   B O     1 
ATOM   9339  C  CB    . GLU   B  1 99   ? -8.442  50.046  116.090 1.00 22.33 ? 97   GLU   B CB    1 
ATOM   9340  C  CG    . GLU   B  1 99   ? -8.077  51.493  115.795 1.00 22.03 ? 97   GLU   B CG    1 
ATOM   9341  C  CD    . GLU   B  1 99   ? -9.140  52.470  116.216 1.00 24.51 ? 97   GLU   B CD    1 
ATOM   9342  O  OE1   . GLU   B  1 99   ? -10.189 52.027  116.735 1.00 23.12 ? 97   GLU   B OE1   1 
ATOM   9343  O  OE2   . GLU   B  1 99   ? -8.925  53.686  116.022 1.00 24.96 ? 97   GLU   B OE2   1 
ATOM   9344  N  N     . GLY   B  1 100  ? -8.592  46.885  115.686 1.00 22.65 ? 98   GLY   B N     1 
ATOM   9345  C  CA    . GLY   B  1 100  ? -8.650  45.541  116.227 1.00 23.58 ? 98   GLY   B CA    1 
ATOM   9346  C  C     . GLY   B  1 100  ? -7.456  44.710  115.808 1.00 22.56 ? 98   GLY   B C     1 
ATOM   9347  O  O     . GLY   B  1 100  ? -6.854  44.016  116.630 1.00 21.86 ? 98   GLY   B O     1 
ATOM   9348  N  N     . VAL   B  1 101  ? -7.087  44.786  114.530 1.00 22.05 ? 99   VAL   B N     1 
ATOM   9349  C  CA    . VAL   B  1 101  ? -5.908  44.074  114.041 1.00 21.50 ? 99   VAL   B CA    1 
ATOM   9350  C  C     . VAL   B  1 101  ? -4.650  44.587  114.730 1.00 25.19 ? 99   VAL   B C     1 
ATOM   9351  O  O     . VAL   B  1 101  ? -3.809  43.804  115.190 1.00 21.65 ? 99   VAL   B O     1 
ATOM   9352  C  CB    . VAL   B  1 101  ? -5.805  44.205  112.512 1.00 20.22 ? 99   VAL   B CB    1 
ATOM   9353  C  CG1   . VAL   B  1 101  ? -4.487  43.635  112.016 1.00 21.03 ? 99   VAL   B CG1   1 
ATOM   9354  C  CG2   . VAL   B  1 101  ? -6.982  43.495  111.846 1.00 21.34 ? 99   VAL   B CG2   1 
ATOM   9355  N  N     . ALA   B  1 102  ? -4.496  45.913  114.805 1.00 22.65 ? 100  ALA   B N     1 
ATOM   9356  C  CA    . ALA   B  1 102  ? -3.296  46.479  115.426 1.00 20.58 ? 100  ALA   B CA    1 
ATOM   9357  C  C     . ALA   B  1 102  ? -3.205  46.103  116.898 1.00 22.87 ? 100  ALA   B C     1 
ATOM   9358  O  O     . ALA   B  1 102  ? -2.117  45.836  117.412 1.00 23.54 ? 100  ALA   B O     1 
ATOM   9359  C  CB    . ALA   B  1 102  ? -3.283  47.999  115.281 1.00 21.63 ? 100  ALA   B CB    1 
ATOM   9360  N  N     . LEU   B  1 103  ? -4.337  46.090  117.597 1.00 20.46 ? 101  LEU   B N     1 
ATOM   9361  C  CA    . LEU   B  1 103  ? -4.316  45.722  119.005 1.00 24.78 ? 101  LEU   B CA    1 
ATOM   9362  C  C     . LEU   B  1 103  ? -3.873  44.277  119.181 1.00 22.92 ? 101  LEU   B C     1 
ATOM   9363  O  O     . LEU   B  1 103  ? -3.088  43.966  120.084 1.00 21.02 ? 101  LEU   B O     1 
ATOM   9364  C  CB    . LEU   B  1 103  ? -5.696  45.929  119.619 1.00 21.72 ? 101  LEU   B CB    1 
ATOM   9365  C  CG    . LEU   B  1 103  ? -5.879  45.454  121.056 1.00 22.85 ? 101  LEU   B CG    1 
ATOM   9366  C  CD1   . LEU   B  1 103  ? -4.970  46.211  122.020 1.00 23.58 ? 101  LEU   B CD1   1 
ATOM   9367  C  CD2   . LEU   B  1 103  ? -7.334  45.623  121.436 1.00 25.25 ? 101  LEU   B CD2   1 
ATOM   9368  N  N     . MET   B  1 104  ? -4.375  43.381  118.333 1.00 23.00 ? 102  MET   B N     1 
ATOM   9369  C  CA    . MET   B  1 104  ? -4.004  41.974  118.463 1.00 24.02 ? 102  MET   B CA    1 
ATOM   9370  C  C     . MET   B  1 104  ? -2.530  41.766  118.153 1.00 25.98 ? 102  MET   B C     1 
ATOM   9371  O  O     . MET   B  1 104  ? -1.869  40.939  118.795 1.00 24.56 ? 102  MET   B O     1 
ATOM   9372  C  CB    . MET   B  1 104  ? -4.893  41.113  117.564 1.00 23.03 ? 102  MET   B CB    1 
ATOM   9373  C  CG    . MET   B  1 104  ? -6.368  41.190  117.954 1.00 26.78 ? 102  MET   B CG    1 
ATOM   9374  S  SD    . MET   B  1 104  ? -6.666  40.818  119.705 1.00 33.99 ? 102  MET   B SD    1 
ATOM   9375  C  CE    . MET   B  1 104  ? -6.340  39.060  119.705 1.00 36.46 ? 102  MET   B CE    1 
ATOM   9376  N  N     . CYS   B  1 105  ? -1.995  42.524  117.191 1.00 22.19 ? 103  CYS   B N     1 
ATOM   9377  C  CA    . CYS   B  1 105  ? -0.560  42.498  116.929 1.00 22.50 ? 103  CYS   B CA    1 
ATOM   9378  C  C     . CYS   B  1 105  ? 0.227   42.948  118.147 1.00 23.37 ? 103  CYS   B C     1 
ATOM   9379  O  O     . CYS   B  1 105  ? 1.219   42.315  118.527 1.00 20.75 ? 103  CYS   B O     1 
ATOM   9380  C  CB    . CYS   B  1 105  ? -0.230  43.381  115.726 1.00 19.55 ? 103  CYS   B CB    1 
ATOM   9381  S  SG    . CYS   B  1 105  ? -0.837  42.719  114.194 1.00 23.86 ? 103  CYS   B SG    1 
ATOM   9382  N  N     . LEU   B  1 106  ? -0.198  44.050  118.776 1.00 22.30 ? 104  LEU   B N     1 
ATOM   9383  C  CA    . LEU   B  1 106  ? 0.476   44.493  119.985 1.00 20.11 ? 104  LEU   B CA    1 
ATOM   9384  C  C     . LEU   B  1 106  ? 0.364   43.442  121.081 1.00 25.40 ? 104  LEU   B C     1 
ATOM   9385  O  O     . LEU   B  1 106  ? 1.345   43.154  121.778 1.00 24.33 ? 104  LEU   B O     1 
ATOM   9386  C  CB    . LEU   B  1 106  ? -0.107  45.825  120.462 1.00 23.10 ? 104  LEU   B CB    1 
ATOM   9387  C  CG    . LEU   B  1 106  ? 0.371   46.250  121.851 1.00 23.89 ? 104  LEU   B CG    1 
ATOM   9388  C  CD1   . LEU   B  1 106  ? 1.785   46.743  121.755 1.00 25.13 ? 104  LEU   B CD1   1 
ATOM   9389  C  CD2   . LEU   B  1 106  ? -0.544  47.288  122.516 1.00 24.23 ? 104  LEU   B CD2   1 
ATOM   9390  N  N     . ALA   B  1 107  ? -0.828  42.858  121.245 1.00 24.17 ? 105  ALA   B N     1 
ATOM   9391  C  CA    . ALA   B  1 107  ? -1.012  41.828  122.263 1.00 24.91 ? 105  ALA   B CA    1 
ATOM   9392  C  C     . ALA   B  1 107  ? -0.104  40.631  121.999 1.00 25.02 ? 105  ALA   B C     1 
ATOM   9393  O  O     . ALA   B  1 107  ? 0.548   40.126  122.919 1.00 27.72 ? 105  ALA   B O     1 
ATOM   9394  C  CB    . ALA   B  1 107  ? -2.477  41.400  122.308 1.00 26.35 ? 105  ALA   B CB    1 
ATOM   9395  N  N     . GLU   B  1 108  ? -0.026  40.185  120.745 1.00 26.09 ? 106  GLU   B N     1 
ATOM   9396  C  CA    . GLU   B  1 108  ? 0.895   39.108  120.383 1.00 28.55 ? 106  GLU   B CA    1 
ATOM   9397  C  C     . GLU   B  1 108  ? 2.323   39.436  120.803 1.00 28.30 ? 106  GLU   B C     1 
ATOM   9398  O  O     . GLU   B  1 108  ? 2.991   38.633  121.466 1.00 32.60 ? 106  GLU   B O     1 
ATOM   9399  C  CB    . GLU   B  1 108  ? 0.829   38.845  118.877 1.00 30.72 ? 106  GLU   B CB    1 
ATOM   9400  C  CG    . GLU   B  1 108  ? 2.005   38.016  118.330 1.00 29.60 ? 106  GLU   B CG    1 
ATOM   9401  C  CD    . GLU   B  1 108  ? 2.025   37.960  116.814 1.00 34.41 ? 106  GLU   B CD    1 
ATOM   9402  O  OE1   . GLU   B  1 108  ? 1.025   38.374  116.200 1.00 34.07 ? 106  GLU   B OE1   1 
ATOM   9403  O  OE2   . GLU   B  1 108  ? 3.043   37.519  116.228 1.00 41.12 ? 106  GLU   B OE2   1 
ATOM   9404  N  N     . ALA   B  1 109  ? 2.804   40.626  120.440 1.00 27.71 ? 107  ALA   B N     1 
ATOM   9405  C  CA    . ALA   B  1 109  ? 4.156   41.022  120.820 1.00 28.72 ? 107  ALA   B CA    1 
ATOM   9406  C  C     . ALA   B  1 109  ? 4.329   41.048  122.337 1.00 30.93 ? 107  ALA   B C     1 
ATOM   9407  O  O     . ALA   B  1 109  ? 5.371   40.626  122.858 1.00 29.07 ? 107  ALA   B O     1 
ATOM   9408  C  CB    . ALA   B  1 109  ? 4.489   42.385  120.222 1.00 28.61 ? 107  ALA   B CB    1 
ATOM   9409  N  N     . LEU   B  1 110  ? 3.328   41.546  123.066 1.00 26.54 ? 108  LEU   B N     1 
ATOM   9410  C  CA    . LEU   B  1 110  ? 3.453   41.616  124.518 1.00 30.05 ? 108  LEU   B CA    1 
ATOM   9411  C  C     . LEU   B  1 110  ? 3.461   40.231  125.146 1.00 32.48 ? 108  LEU   B C     1 
ATOM   9412  O  O     . LEU   B  1 110  ? 4.038   40.040  126.223 1.00 34.00 ? 108  LEU   B O     1 
ATOM   9413  C  CB    . LEU   B  1 110  ? 2.318   42.452  125.116 1.00 27.33 ? 108  LEU   B CB    1 
ATOM   9414  C  CG    . LEU   B  1 110  ? 2.400   43.961  124.866 1.00 26.13 ? 108  LEU   B CG    1 
ATOM   9415  C  CD1   . LEU   B  1 110  ? 1.082   44.629  125.296 1.00 26.78 ? 108  LEU   B CD1   1 
ATOM   9416  C  CD2   . LEU   B  1 110  ? 3.592   44.555  125.610 1.00 30.99 ? 108  LEU   B CD2   1 
ATOM   9417  N  N     . LEU   B  1 111  ? 2.817   39.265  124.502 1.00 30.86 ? 109  LEU   B N     1 
ATOM   9418  C  CA    . LEU   B  1 111  ? 2.834   37.896  124.989 1.00 37.22 ? 109  LEU   B CA    1 
ATOM   9419  C  C     . LEU   B  1 111  ? 4.145   37.185  124.686 1.00 36.08 ? 109  LEU   B C     1 
ATOM   9420  O  O     . LEU   B  1 111  ? 4.367   36.085  125.202 1.00 33.21 ? 109  LEU   B O     1 
ATOM   9421  C  CB    . LEU   B  1 111  ? 1.652   37.127  124.401 1.00 35.01 ? 109  LEU   B CB    1 
ATOM   9422  C  CG    . LEU   B  1 111  ? 0.334   37.618  124.997 1.00 34.66 ? 109  LEU   B CG    1 
ATOM   9423  C  CD1   . LEU   B  1 111  ? -0.842  37.105  124.209 1.00 37.34 ? 109  LEU   B CD1   1 
ATOM   9424  C  CD2   . LEU   B  1 111  ? 0.219   37.203  126.459 1.00 38.03 ? 109  LEU   B CD2   1 
ATOM   9425  N  N     . ARG   B  1 112  ? 5.019   37.787  123.877 1.00 33.81 ? 110  ARG   B N     1 
ATOM   9426  C  CA    . ARG   B  1 112  ? 6.387   37.293  123.774 1.00 36.39 ? 110  ARG   B CA    1 
ATOM   9427  C  C     . ARG   B  1 112  ? 7.198   37.582  125.033 1.00 39.15 ? 110  ARG   B C     1 
ATOM   9428  O  O     . ARG   B  1 112  ? 8.272   37.001  125.208 1.00 38.21 ? 110  ARG   B O     1 
ATOM   9429  C  CB    . ARG   B  1 112  ? 7.079   37.893  122.549 1.00 32.48 ? 110  ARG   B CB    1 
ATOM   9430  C  CG    . ARG   B  1 112  ? 6.363   37.652  121.222 1.00 36.49 ? 110  ARG   B CG    1 
ATOM   9431  C  CD    . ARG   B  1 112  ? 7.204   38.165  120.048 1.00 39.42 ? 110  ARG   B CD    1 
ATOM   9432  N  NE    . ARG   B  1 112  ? 6.432   38.361  118.825 1.00 43.75 ? 110  ARG   B NE    1 
ATOM   9433  C  CZ    . ARG   B  1 112  ? 6.282   39.527  118.204 1.00 46.72 ? 110  ARG   B CZ    1 
ATOM   9434  N  NH1   . ARG   B  1 112  ? 6.857   40.631  118.654 1.00 48.97 ? 110  ARG   B NH1   1 
ATOM   9435  N  NH2   . ARG   B  1 112  ? 5.550   39.584  117.092 1.00 42.60 ? 110  ARG   B NH2   1 
ATOM   9436  N  N     . ILE   B  1 113  ? 6.718   38.460  125.908 1.00 35.88 ? 111  ILE   B N     1 
ATOM   9437  C  CA    . ILE   B  1 113  ? 7.325   38.674  127.217 1.00 37.99 ? 111  ILE   B CA    1 
ATOM   9438  C  C     . ILE   B  1 113  ? 6.778   37.614  128.165 1.00 42.15 ? 111  ILE   B C     1 
ATOM   9439  O  O     . ILE   B  1 113  ? 5.597   37.674  128.540 1.00 43.57 ? 111  ILE   B O     1 
ATOM   9440  C  CB    . ILE   B  1 113  ? 7.042   40.090  127.737 1.00 38.84 ? 111  ILE   B CB    1 
ATOM   9441  C  CG1   . ILE   B  1 113  ? 7.585   41.134  126.758 1.00 38.03 ? 111  ILE   B CG1   1 
ATOM   9442  C  CG2   . ILE   B  1 113  ? 7.617   40.273  129.126 1.00 35.17 ? 111  ILE   B CG2   1 
ATOM   9443  C  CD1   . ILE   B  1 113  ? 7.202   42.550  127.118 1.00 37.45 ? 111  ILE   B CD1   1 
ATOM   9444  N  N     . PRO   B  1 114  ? 7.592   36.637  128.582 1.00 43.37 ? 112  PRO   B N     1 
ATOM   9445  C  CA    . PRO   B  1 114  ? 7.035   35.475  129.299 1.00 41.38 ? 112  PRO   B CA    1 
ATOM   9446  C  C     . PRO   B  1 114  ? 6.540   35.779  130.701 1.00 36.43 ? 112  PRO   B C     1 
ATOM   9447  O  O     . PRO   B  1 114  ? 5.573   35.151  131.148 1.00 45.62 ? 112  PRO   B O     1 
ATOM   9448  C  CB    . PRO   B  1 114  ? 8.211   34.484  129.328 1.00 37.53 ? 112  PRO   B CB    1 
ATOM   9449  C  CG    . PRO   B  1 114  ? 9.153   34.960  128.284 1.00 41.91 ? 112  PRO   B CG    1 
ATOM   9450  C  CD    . PRO   B  1 114  ? 9.011   36.446  128.248 1.00 40.43 ? 112  PRO   B CD    1 
ATOM   9451  N  N     . ASP   B  1 115  ? 7.165   36.703  131.418 1.00 39.30 ? 113  ASP   B N     1 
ATOM   9452  C  CA    . ASP   B  1 115  ? 6.814   36.949  132.810 1.00 45.27 ? 113  ASP   B CA    1 
ATOM   9453  C  C     . ASP   B  1 115  ? 5.672   37.948  132.890 1.00 44.80 ? 113  ASP   B C     1 
ATOM   9454  O  O     . ASP   B  1 115  ? 5.773   39.056  132.352 1.00 43.85 ? 113  ASP   B O     1 
ATOM   9455  C  CB    . ASP   B  1 115  ? 8.013   37.469  133.600 1.00 40.04 ? 113  ASP   B CB    1 
ATOM   9456  C  CG    . ASP   B  1 115  ? 7.610   38.082  134.925 1.00 47.51 ? 113  ASP   B CG    1 
ATOM   9457  O  OD1   . ASP   B  1 115  ? 6.978   37.382  135.750 1.00 51.35 ? 113  ASP   B OD1   1 
ATOM   9458  O  OD2   . ASP   B  1 115  ? 7.922   39.270  135.145 1.00 48.15 ? 113  ASP   B OD2   1 
ATOM   9459  N  N     . THR   B  1 116  ? 4.600   37.558  133.585 1.00 41.56 ? 114  THR   B N     1 
ATOM   9460  C  CA    . THR   B  1 116  ? 3.413   38.403  133.671 1.00 47.75 ? 114  THR   B CA    1 
ATOM   9461  C  C     . THR   B  1 116  ? 3.746   39.773  134.247 1.00 47.82 ? 114  THR   B C     1 
ATOM   9462  O  O     . THR   B  1 116  ? 3.312   40.800  133.715 1.00 45.49 ? 114  THR   B O     1 
ATOM   9463  C  CB    . THR   B  1 116  ? 2.335   37.714  134.512 1.00 48.22 ? 114  THR   B CB    1 
ATOM   9464  O  OG1   . THR   B  1 116  ? 2.044   36.420  133.967 1.00 51.81 ? 114  THR   B OG1   1 
ATOM   9465  C  CG2   . THR   B  1 116  ? 1.064   38.543  134.528 1.00 49.20 ? 114  THR   B CG2   1 
ATOM   9466  N  N     . ALA   B  1 117  ? 4.536   39.812  135.323 1.00 49.08 ? 115  ALA   B N     1 
ATOM   9467  C  CA    . ALA   B  1 117  ? 4.815   41.084  135.982 1.00 45.68 ? 115  ALA   B CA    1 
ATOM   9468  C  C     . ALA   B  1 117  ? 5.668   41.998  135.106 1.00 43.99 ? 115  ALA   B C     1 
ATOM   9469  O  O     . ALA   B  1 117  ? 5.473   43.220  135.108 1.00 42.76 ? 115  ALA   B O     1 
ATOM   9470  C  CB    . ALA   B  1 117  ? 5.489   40.836  137.334 1.00 50.03 ? 115  ALA   B CB    1 
ATOM   9471  N  N     . THR   B  1 118  ? 6.618   41.434  134.355 1.00 40.15 ? 116  THR   B N     1 
ATOM   9472  C  CA    . THR   B  1 118  ? 7.409   42.247  133.434 1.00 41.50 ? 116  THR   B CA    1 
ATOM   9473  C  C     . THR   B  1 118  ? 6.532   42.810  132.323 1.00 40.83 ? 116  THR   B C     1 
ATOM   9474  O  O     . THR   B  1 118  ? 6.639   43.989  131.959 1.00 37.48 ? 116  THR   B O     1 
ATOM   9475  C  CB    . THR   B  1 118  ? 8.551   41.425  132.831 1.00 41.57 ? 116  THR   B CB    1 
ATOM   9476  O  OG1   . THR   B  1 118  ? 9.425   40.967  133.868 1.00 48.22 ? 116  THR   B OG1   1 
ATOM   9477  C  CG2   . THR   B  1 118  ? 9.348   42.264  131.846 1.00 34.75 ? 116  THR   B CG2   1 
ATOM   9478  N  N     . ARG   B  1 119  ? 5.668   41.966  131.761 1.00 39.23 ? 117  ARG   B N     1 
ATOM   9479  C  CA    . ARG   B  1 119  ? 4.753   42.416  130.719 1.00 41.57 ? 117  ARG   B CA    1 
ATOM   9480  C  C     . ARG   B  1 119  ? 3.800   43.481  131.252 1.00 38.13 ? 117  ARG   B C     1 
ATOM   9481  O  O     . ARG   B  1 119  ? 3.590   44.519  130.612 1.00 37.22 ? 117  ARG   B O     1 
ATOM   9482  C  CB    . ARG   B  1 119  ? 3.979   41.221  130.166 1.00 40.51 ? 117  ARG   B CB    1 
ATOM   9483  C  CG    . ARG   B  1 119  ? 3.110   41.552  128.982 1.00 33.72 ? 117  ARG   B CG    1 
ATOM   9484  C  CD    . ARG   B  1 119  ? 2.104   40.451  128.723 1.00 36.32 ? 117  ARG   B CD    1 
ATOM   9485  N  NE    . ARG   B  1 119  ? 2.717   39.130  128.782 1.00 42.46 ? 117  ARG   B NE    1 
ATOM   9486  C  CZ    . ARG   B  1 119  ? 2.328   38.162  129.602 1.00 44.72 ? 117  ARG   B CZ    1 
ATOM   9487  N  NH1   . ARG   B  1 119  ? 1.299   38.319  130.419 1.00 46.05 ? 117  ARG   B NH1   1 
ATOM   9488  N  NH2   . ARG   B  1 119  ? 2.980   37.003  129.593 1.00 49.30 ? 117  ARG   B NH2   1 
ATOM   9489  N  N     . ASP   B  1 120  ? 3.219   43.240  132.433 1.00 42.37 ? 118  ASP   B N     1 
ATOM   9490  C  CA    . ASP   B  1 120  ? 2.288   44.197  133.026 1.00 41.12 ? 118  ASP   B CA    1 
ATOM   9491  C  C     . ASP   B  1 120  ? 2.965   45.529  133.313 1.00 42.42 ? 118  ASP   B C     1 
ATOM   9492  O  O     . ASP   B  1 120  ? 2.343   46.589  133.176 1.00 41.52 ? 118  ASP   B O     1 
ATOM   9493  C  CB    . ASP   B  1 120  ? 1.681   43.627  134.310 1.00 42.88 ? 118  ASP   B CB    1 
ATOM   9494  C  CG    . ASP   B  1 120  ? 0.736   42.470  134.045 1.00 49.38 ? 118  ASP   B CG    1 
ATOM   9495  O  OD1   . ASP   B  1 120  ? 0.419   42.214  132.859 1.00 47.85 ? 118  ASP   B OD1   1 
ATOM   9496  O  OD2   . ASP   B  1 120  ? 0.320   41.810  135.023 1.00 47.59 ? 118  ASP   B OD2   1 
ATOM   9497  N  N     . ALA   B  1 121  ? 4.236   45.499  133.729 1.00 40.27 ? 119  ALA   B N     1 
ATOM   9498  C  CA    . ALA   B  1 121  ? 4.936   46.751  134.001 1.00 42.39 ? 119  ALA   B CA    1 
ATOM   9499  C  C     . ALA   B  1 121  ? 5.205   47.521  132.713 1.00 43.54 ? 119  ALA   B C     1 
ATOM   9500  O  O     . ALA   B  1 121  ? 5.026   48.743  132.667 1.00 44.17 ? 119  ALA   B O     1 
ATOM   9501  C  CB    . ALA   B  1 121  ? 6.242   46.485  134.752 1.00 41.00 ? 119  ALA   B CB    1 
ATOM   9502  N  N     . LEU   B  1 122  ? 5.628   46.827  131.654 1.00 37.83 ? 120  LEU   B N     1 
ATOM   9503  C  CA    . LEU   B  1 122  ? 5.877   47.512  130.388 1.00 39.38 ? 120  LEU   B CA    1 
ATOM   9504  C  C     . LEU   B  1 122  ? 4.602   48.154  129.860 1.00 40.30 ? 120  LEU   B C     1 
ATOM   9505  O  O     . LEU   B  1 122  ? 4.637   49.257  129.302 1.00 39.26 ? 120  LEU   B O     1 
ATOM   9506  C  CB    . LEU   B  1 122  ? 6.450   46.544  129.354 1.00 41.39 ? 120  LEU   B CB    1 
ATOM   9507  C  CG    . LEU   B  1 122  ? 6.772   47.180  127.996 1.00 38.04 ? 120  LEU   B CG    1 
ATOM   9508  C  CD1   . LEU   B  1 122  ? 7.995   48.086  128.086 1.00 41.57 ? 120  LEU   B CD1   1 
ATOM   9509  C  CD2   . LEU   B  1 122  ? 6.933   46.132  126.886 1.00 39.62 ? 120  LEU   B CD2   1 
ATOM   9510  N  N     . ILE   B  1 123  ? 3.465   47.478  130.039 1.00 35.94 ? 121  ILE   B N     1 
ATOM   9511  C  CA    . ILE   B  1 123  ? 2.189   48.024  129.588 1.00 40.60 ? 121  ILE   B CA    1 
ATOM   9512  C  C     . ILE   B  1 123  ? 1.868   49.313  130.337 1.00 42.73 ? 121  ILE   B C     1 
ATOM   9513  O  O     . ILE   B  1 123  ? 1.592   50.354  129.729 1.00 40.77 ? 121  ILE   B O     1 
ATOM   9514  C  CB    . ILE   B  1 123  ? 1.071   46.976  129.755 1.00 33.71 ? 121  ILE   B CB    1 
ATOM   9515  C  CG1   . ILE   B  1 123  ? 1.287   45.799  128.800 1.00 30.79 ? 121  ILE   B CG1   1 
ATOM   9516  C  CG2   . ILE   B  1 123  ? -0.291  47.610  129.534 1.00 33.06 ? 121  ILE   B CG2   1 
ATOM   9517  C  CD1   . ILE   B  1 123  ? 0.347   44.636  129.047 1.00 32.35 ? 121  ILE   B CD1   1 
ATOM   9518  N  N     . ARG   B  1 124  ? 1.929   49.269  131.671 1.00 38.86 ? 122  ARG   B N     1 
ATOM   9519  C  CA    . ARG   B  1 124  ? 1.498   50.405  132.478 1.00 46.31 ? 122  ARG   B CA    1 
ATOM   9520  C  C     . ARG   B  1 124  ? 2.498   51.554  132.464 1.00 46.48 ? 122  ARG   B C     1 
ATOM   9521  O  O     . ARG   B  1 124  ? 2.128   52.685  132.792 1.00 51.72 ? 122  ARG   B O     1 
ATOM   9522  C  CB    . ARG   B  1 124  ? 1.244   49.959  133.922 1.00 45.82 ? 122  ARG   B CB    1 
ATOM   9523  N  N     . ASP   B  1 125  ? 3.745   51.304  132.084 1.00 46.40 ? 123  ASP   B N     1 
ATOM   9524  C  CA    . ASP   B  1 125  ? 4.783   52.309  132.203 1.00 47.74 ? 123  ASP   B CA    1 
ATOM   9525  C  C     . ASP   B  1 125  ? 5.373   52.753  130.874 1.00 46.54 ? 123  ASP   B C     1 
ATOM   9526  O  O     . ASP   B  1 125  ? 6.123   53.736  130.852 1.00 53.90 ? 123  ASP   B O     1 
ATOM   9527  C  CB    . ASP   B  1 125  ? 5.908   51.795  133.117 1.00 52.60 ? 123  ASP   B CB    1 
ATOM   9528  C  CG    . ASP   B  1 125  ? 5.401   51.409  134.501 1.00 52.88 ? 123  ASP   B CG    1 
ATOM   9529  O  OD1   . ASP   B  1 125  ? 4.555   52.145  135.048 1.00 50.14 ? 123  ASP   B OD1   1 
ATOM   9530  O  OD2   . ASP   B  1 125  ? 5.838   50.368  135.040 1.00 55.00 ? 123  ASP   B OD2   1 
ATOM   9531  N  N     . LYS   B  1 126  ? 5.052   52.083  129.769 1.00 43.30 ? 124  LYS   B N     1 
ATOM   9532  C  CA    . LYS   B  1 126  ? 5.607   52.467  128.481 1.00 43.23 ? 124  LYS   B CA    1 
ATOM   9533  C  C     . LYS   B  1 126  ? 4.553   52.419  127.379 1.00 47.49 ? 124  LYS   B C     1 
ATOM   9534  O  O     . LYS   B  1 126  ? 4.374   53.398  126.647 1.00 48.98 ? 124  LYS   B O     1 
ATOM   9535  C  CB    . LYS   B  1 126  ? 6.794   51.567  128.126 1.00 47.07 ? 124  LYS   B CB    1 
ATOM   9536  N  N     . ILE   B  1 127  ? 3.849   51.293  127.248 1.00 42.55 ? 125  ILE   B N     1 
ATOM   9537  C  CA    . ILE   B  1 127  ? 2.918   51.137  126.132 1.00 40.36 ? 125  ILE   B CA    1 
ATOM   9538  C  C     . ILE   B  1 127  ? 1.692   52.022  126.330 1.00 41.67 ? 125  ILE   B C     1 
ATOM   9539  O  O     . ILE   B  1 127  ? 1.266   52.730  125.412 1.00 40.14 ? 125  ILE   B O     1 
ATOM   9540  C  CB    . ILE   B  1 127  ? 2.518   49.661  125.957 1.00 38.63 ? 125  ILE   B CB    1 
ATOM   9541  C  CG1   . ILE   B  1 127  ? 3.745   48.743  126.048 1.00 37.64 ? 125  ILE   B CG1   1 
ATOM   9542  C  CG2   . ILE   B  1 127  ? 1.784   49.472  124.630 1.00 36.14 ? 125  ILE   B CG2   1 
ATOM   9543  C  CD1   . ILE   B  1 127  ? 4.798   49.016  125.014 1.00 40.13 ? 125  ILE   B CD1   1 
ATOM   9544  N  N     . ALA   B  1 128  ? 1.104   51.996  127.529 1.00 38.61 ? 126  ALA   B N     1 
ATOM   9545  C  CA    . ALA   B  1 128  ? -0.146  52.712  127.749 1.00 38.07 ? 126  ALA   B CA    1 
ATOM   9546  C  C     . ALA   B  1 128  ? 0.010   54.218  127.597 1.00 44.00 ? 126  ALA   B C     1 
ATOM   9547  O  O     . ALA   B  1 128  ? -0.981  54.904  127.324 1.00 42.35 ? 126  ALA   B O     1 
ATOM   9548  C  CB    . ALA   B  1 128  ? -0.720  52.385  129.129 1.00 40.00 ? 126  ALA   B CB    1 
ATOM   9549  N  N     . ASP   B  1 129  ? 1.219   54.741  127.772 1.00 48.65 ? 127  ASP   B N     1 
ATOM   9550  C  CA    . ASP   B  1 129  ? 1.504   56.149  127.549 1.00 52.20 ? 127  ASP   B CA    1 
ATOM   9551  C  C     . ASP   B  1 129  ? 1.864   56.441  126.096 1.00 52.93 ? 127  ASP   B C     1 
ATOM   9552  O  O     . ASP   B  1 129  ? 2.337   57.541  125.792 1.00 55.10 ? 127  ASP   B O     1 
ATOM   9553  C  CB    . ASP   B  1 129  ? 2.630   56.614  128.480 1.00 48.20 ? 127  ASP   B CB    1 
ATOM   9554  N  N     . GLY   B  1 130  ? 1.657   55.477  125.197 1.00 50.47 ? 128  GLY   B N     1 
ATOM   9555  C  CA    . GLY   B  1 130  ? 1.826   55.676  123.777 1.00 48.69 ? 128  GLY   B CA    1 
ATOM   9556  C  C     . GLY   B  1 130  ? 3.177   55.263  123.232 1.00 53.76 ? 128  GLY   B C     1 
ATOM   9557  O  O     . GLY   B  1 130  ? 3.281   54.976  122.034 1.00 51.49 ? 128  GLY   B O     1 
ATOM   9558  N  N     . ASN   B  1 131  ? 4.211   55.222  124.072 1.00 58.99 ? 129  ASN   B N     1 
ATOM   9559  C  CA    . ASN   B  1 131  ? 5.542   54.867  123.600 1.00 58.65 ? 129  ASN   B CA    1 
ATOM   9560  C  C     . ASN   B  1 131  ? 5.608   53.380  123.275 1.00 58.80 ? 129  ASN   B C     1 
ATOM   9561  O  O     . ASN   B  1 131  ? 6.308   52.621  123.953 1.00 62.56 ? 129  ASN   B O     1 
ATOM   9562  C  CB    . ASN   B  1 131  ? 6.600   55.239  124.642 1.00 59.85 ? 129  ASN   B CB    1 
ATOM   9563  N  N     . TRP   B  1 132  ? 4.879   52.949  122.246 1.00 52.79 ? 130  TRP   B N     1 
ATOM   9564  C  CA    . TRP   B  1 132  ? 4.876   51.537  121.894 1.00 49.80 ? 130  TRP   B CA    1 
ATOM   9565  C  C     . TRP   B  1 132  ? 5.945   51.187  120.877 1.00 51.45 ? 130  TRP   B C     1 
ATOM   9566  O  O     . TRP   B  1 132  ? 6.448   50.057  120.886 1.00 54.41 ? 130  TRP   B O     1 
ATOM   9567  C  CB    . TRP   B  1 132  ? 3.497   51.109  121.370 1.00 47.41 ? 130  TRP   B CB    1 
ATOM   9568  C  CG    . TRP   B  1 132  ? 3.020   51.774  120.096 1.00 39.53 ? 130  TRP   B CG    1 
ATOM   9569  C  CD1   . TRP   B  1 132  ? 2.168   52.842  119.996 1.00 39.20 ? 130  TRP   B CD1   1 
ATOM   9570  C  CD2   . TRP   B  1 132  ? 3.331   51.386  118.752 1.00 36.97 ? 130  TRP   B CD2   1 
ATOM   9571  N  NE1   . TRP   B  1 132  ? 1.941   53.150  118.674 1.00 34.78 ? 130  TRP   B NE1   1 
ATOM   9572  C  CE2   . TRP   B  1 132  ? 2.645   52.274  117.890 1.00 33.60 ? 130  TRP   B CE2   1 
ATOM   9573  C  CE3   . TRP   B  1 132  ? 4.130   50.382  118.191 1.00 35.40 ? 130  TRP   B CE3   1 
ATOM   9574  C  CZ2   . TRP   B  1 132  ? 2.735   52.187  116.499 1.00 27.71 ? 130  TRP   B CZ2   1 
ATOM   9575  C  CZ3   . TRP   B  1 132  ? 4.221   50.300  116.811 1.00 35.35 ? 130  TRP   B CZ3   1 
ATOM   9576  C  CH2   . TRP   B  1 132  ? 3.519   51.196  115.979 1.00 31.56 ? 130  TRP   B CH2   1 
ATOM   9577  N  N     . LYS   B  1 133  ? 6.315   52.131  120.009 1.00 54.76 ? 131  LYS   B N     1 
ATOM   9578  C  CA    . LYS   B  1 133  ? 7.261   51.826  118.941 1.00 54.59 ? 131  LYS   B CA    1 
ATOM   9579  C  C     . LYS   B  1 133  ? 8.613   51.404  119.507 1.00 61.80 ? 131  LYS   B C     1 
ATOM   9580  O  O     . LYS   B  1 133  ? 9.181   50.383  119.098 1.00 61.80 ? 131  LYS   B O     1 
ATOM   9581  C  CB    . LYS   B  1 133  ? 7.410   53.035  118.017 1.00 52.38 ? 131  LYS   B CB    1 
ATOM   9582  N  N     . SER   B  1 134  ? 9.133   52.172  120.467 1.00 65.06 ? 132  SER   B N     1 
ATOM   9583  C  CA    . SER   B  1 134  ? 10.476  51.920  120.979 1.00 64.24 ? 132  SER   B CA    1 
ATOM   9584  C  C     . SER   B  1 134  ? 10.544  50.602  121.743 1.00 65.88 ? 132  SER   B C     1 
ATOM   9585  O  O     . SER   B  1 134  ? 11.411  49.760  121.472 1.00 59.88 ? 132  SER   B O     1 
ATOM   9586  C  CB    . SER   B  1 134  ? 10.918  53.084  121.868 1.00 58.70 ? 132  SER   B CB    1 
ATOM   9587  N  N     . HIS   B  1 135  ? 9.628   50.399  122.695 1.00 64.72 ? 133  HIS   B N     1 
ATOM   9588  C  CA    . HIS   B  1 135  ? 9.715   49.276  123.622 1.00 60.97 ? 133  HIS   B CA    1 
ATOM   9589  C  C     . HIS   B  1 135  ? 9.379   47.930  122.987 1.00 60.85 ? 133  HIS   B C     1 
ATOM   9590  O  O     . HIS   B  1 135  ? 9.575   46.897  123.637 1.00 56.83 ? 133  HIS   B O     1 
ATOM   9591  C  CB    . HIS   B  1 135  ? 8.796   49.525  124.818 1.00 58.94 ? 133  HIS   B CB    1 
ATOM   9592  N  N     . LEU   B  1 136  ? 8.879   47.906  121.755 1.00 60.01 ? 134  LEU   B N     1 
ATOM   9593  C  CA    . LEU   B  1 136  ? 8.593   46.641  121.081 1.00 55.54 ? 134  LEU   B CA    1 
ATOM   9594  C  C     . LEU   B  1 136  ? 9.007   46.686  119.614 1.00 56.65 ? 134  LEU   B C     1 
ATOM   9595  O  O     . LEU   B  1 136  ? 8.849   45.703  118.889 1.00 58.58 ? 134  LEU   B O     1 
ATOM   9596  C  CB    . LEU   B  1 136  ? 7.108   46.293  121.190 1.00 48.43 ? 134  LEU   B CB    1 
ATOM   9597  C  CG    . LEU   B  1 136  ? 6.574   45.896  122.564 1.00 47.80 ? 134  LEU   B CG    1 
ATOM   9598  C  CD1   . LEU   B  1 136  ? 5.073   45.820  122.504 1.00 41.03 ? 134  LEU   B CD1   1 
ATOM   9599  C  CD2   . LEU   B  1 136  ? 7.157   44.566  123.021 1.00 44.94 ? 134  LEU   B CD2   1 
ATOM   9600  N  N     . ARG   B  1 140  ? 11.861  44.061  114.726 1.00 48.74 ? 138  ARG   B N     1 
ATOM   9601  C  CA    . ARG   B  1 140  ? 10.969  43.852  113.592 1.00 45.93 ? 138  ARG   B CA    1 
ATOM   9602  C  C     . ARG   B  1 140  ? 9.608   44.506  113.830 1.00 46.37 ? 138  ARG   B C     1 
ATOM   9603  O  O     . ARG   B  1 140  ? 9.244   44.826  114.965 1.00 41.66 ? 138  ARG   B O     1 
ATOM   9604  C  CB    . ARG   B  1 140  ? 10.794  42.353  113.305 1.00 45.46 ? 138  ARG   B CB    1 
ATOM   9605  C  CG    . ARG   B  1 140  ? 10.081  41.564  114.397 1.00 48.26 ? 138  ARG   B CG    1 
ATOM   9606  C  CD    . ARG   B  1 140  ? 9.840   40.124  113.959 1.00 48.64 ? 138  ARG   B CD    1 
ATOM   9607  N  NE    . ARG   B  1 140  ? 8.944   39.423  114.872 1.00 57.10 ? 138  ARG   B NE    1 
ATOM   9608  C  CZ    . ARG   B  1 140  ? 8.473   38.198  114.672 1.00 56.69 ? 138  ARG   B CZ    1 
ATOM   9609  N  NH1   . ARG   B  1 140  ? 8.787   37.503  113.591 1.00 50.88 ? 138  ARG   B NH1   1 
ATOM   9610  N  NH2   . ARG   B  1 140  ? 7.665   37.658  115.582 1.00 57.57 ? 138  ARG   B NH2   1 
ATOM   9611  N  N     . SER   B  1 141  ? 8.871   44.709  112.741 1.00 39.00 ? 139  SER   B N     1 
ATOM   9612  C  CA    . SER   B  1 141  ? 7.570   45.348  112.819 1.00 35.74 ? 139  SER   B CA    1 
ATOM   9613  C  C     . SER   B  1 141  ? 6.666   44.614  113.804 1.00 34.66 ? 139  SER   B C     1 
ATOM   9614  O  O     . SER   B  1 141  ? 6.674   43.382  113.892 1.00 33.20 ? 139  SER   B O     1 
ATOM   9615  C  CB    . SER   B  1 141  ? 6.931   45.387  111.428 1.00 33.53 ? 139  SER   B CB    1 
ATOM   9616  O  OG    . SER   B  1 141  ? 5.623   45.944  111.467 1.00 33.34 ? 139  SER   B OG    1 
ATOM   9617  N  N     . LEU   B  1 142  ? 5.903   45.390  114.575 1.00 34.28 ? 140  LEU   B N     1 
ATOM   9618  C  CA    . LEU   B  1 142  ? 4.845   44.812  115.390 1.00 27.03 ? 140  LEU   B CA    1 
ATOM   9619  C  C     . LEU   B  1 142  ? 3.817   44.079  114.546 1.00 26.11 ? 140  LEU   B C     1 
ATOM   9620  O  O     . LEU   B  1 142  ? 3.059   43.261  115.079 1.00 23.53 ? 140  LEU   B O     1 
ATOM   9621  C  CB    . LEU   B  1 142  ? 4.144   45.911  116.185 1.00 25.67 ? 140  LEU   B CB    1 
ATOM   9622  C  CG    . LEU   B  1 142  ? 3.776   45.563  117.615 1.00 29.86 ? 140  LEU   B CG    1 
ATOM   9623  C  CD1   . LEU   B  1 142  ? 5.033   45.443  118.419 1.00 35.56 ? 140  LEU   B CD1   1 
ATOM   9624  C  CD2   . LEU   B  1 142  ? 2.889   46.640  118.179 1.00 34.96 ? 140  LEU   B CD2   1 
ATOM   9625  N  N     . PHE   B  1 143  ? 3.754   44.381  113.246 1.00 23.99 ? 141  PHE   B N     1 
ATOM   9626  C  CA    . PHE   B  1 143  ? 2.645   43.968  112.398 1.00 22.79 ? 141  PHE   B CA    1 
ATOM   9627  C  C     . PHE   B  1 143  ? 3.036   42.858  111.427 1.00 25.49 ? 141  PHE   B C     1 
ATOM   9628  O  O     . PHE   B  1 143  ? 2.328   42.620  110.444 1.00 22.85 ? 141  PHE   B O     1 
ATOM   9629  C  CB    . PHE   B  1 143  ? 2.095   45.188  111.658 1.00 22.57 ? 141  PHE   B CB    1 
ATOM   9630  C  CG    . PHE   B  1 143  ? 1.781   46.337  112.571 1.00 19.67 ? 141  PHE   B CG    1 
ATOM   9631  C  CD1   . PHE   B  1 143  ? 0.868   46.185  113.595 1.00 19.22 ? 141  PHE   B CD1   1 
ATOM   9632  C  CD2   . PHE   B  1 143  ? 2.409   47.563  112.413 1.00 20.46 ? 141  PHE   B CD2   1 
ATOM   9633  C  CE1   . PHE   B  1 143  ? 0.584   47.234  114.460 1.00 22.46 ? 141  PHE   B CE1   1 
ATOM   9634  C  CE2   . PHE   B  1 143  ? 2.130   48.613  113.261 1.00 18.67 ? 141  PHE   B CE2   1 
ATOM   9635  C  CZ    . PHE   B  1 143  ? 1.221   48.453  114.284 1.00 21.30 ? 141  PHE   B CZ    1 
ATOM   9636  N  N     . VAL   B  1 144  ? 4.141   42.153  111.703 1.00 24.75 ? 142  VAL   B N     1 
ATOM   9637  C  CA    . VAL   B  1 144  ? 4.597   41.090  110.804 1.00 26.80 ? 142  VAL   B CA    1 
ATOM   9638  C  C     . VAL   B  1 144  ? 3.511   40.031  110.606 1.00 27.33 ? 142  VAL   B C     1 
ATOM   9639  O  O     . VAL   B  1 144  ? 3.352   39.483  109.507 1.00 29.12 ? 142  VAL   B O     1 
ATOM   9640  C  CB    . VAL   B  1 144  ? 5.910   40.472  111.324 1.00 28.35 ? 142  VAL   B CB    1 
ATOM   9641  C  CG1   . VAL   B  1 144  ? 7.016   41.505  111.287 1.00 35.01 ? 142  VAL   B CG1   1 
ATOM   9642  C  CG2   . VAL   B  1 144  ? 5.743   39.934  112.739 1.00 35.16 ? 142  VAL   B CG2   1 
ATOM   9643  N  N     . ASN   B  1 145  ? 2.738   39.736  111.650 1.00 23.72 ? 143  ASN   B N     1 
ATOM   9644  C  CA    . ASN   B  1 145  ? 1.672   38.746  111.558 1.00 28.62 ? 143  ASN   B CA    1 
ATOM   9645  C  C     . ASN   B  1 145  ? 0.294   39.378  111.428 1.00 28.22 ? 143  ASN   B C     1 
ATOM   9646  O  O     . ASN   B  1 145  ? -0.711  38.731  111.739 1.00 23.32 ? 143  ASN   B O     1 
ATOM   9647  C  CB    . ASN   B  1 145  ? 1.704   37.817  112.768 1.00 29.33 ? 143  ASN   B CB    1 
ATOM   9648  C  CG    . ASN   B  1 145  ? 2.894   36.899  112.749 1.00 34.51 ? 143  ASN   B CG    1 
ATOM   9649  O  OD1   . ASN   B  1 145  ? 3.259   36.370  111.694 1.00 41.78 ? 143  ASN   B OD1   1 
ATOM   9650  N  ND2   . ASN   B  1 145  ? 3.525   36.710  113.912 1.00 33.00 ? 143  ASN   B ND2   1 
ATOM   9651  N  N     . ALA   B  1 146  ? 0.220   40.626  110.970 1.00 22.90 ? 144  ALA   B N     1 
ATOM   9652  C  CA    . ALA   B  1 146  ? -1.070  41.297  110.908 1.00 23.65 ? 144  ALA   B CA    1 
ATOM   9653  C  C     . ALA   B  1 146  ? -2.022  40.651  109.908 1.00 21.83 ? 144  ALA   B C     1 
ATOM   9654  O  O     . ALA   B  1 146  ? -3.240  40.784  110.067 1.00 24.78 ? 144  ALA   B O     1 
ATOM   9655  C  CB    . ALA   B  1 146  ? -0.880  42.777  110.576 1.00 22.86 ? 144  ALA   B CB    1 
ATOM   9656  N  N     . ALA   B  1 147  ? -1.515  39.959  108.885 1.00 24.50 ? 145  ALA   B N     1 
ATOM   9657  C  CA    . ALA   B  1 147  ? -2.436  39.304  107.960 1.00 27.58 ? 145  ALA   B CA    1 
ATOM   9658  C  C     . ALA   B  1 147  ? -3.226  38.224  108.681 1.00 27.69 ? 145  ALA   B C     1 
ATOM   9659  O  O     . ALA   B  1 147  ? -4.430  38.056  108.449 1.00 26.64 ? 145  ALA   B O     1 
ATOM   9660  C  CB    . ALA   B  1 147  ? -1.682  38.720  106.768 1.00 25.88 ? 145  ALA   B CB    1 
ATOM   9661  N  N     . THR   B  1 148  ? -2.571  37.511  109.592 1.00 26.75 ? 146  THR   B N     1 
ATOM   9662  C  CA    . THR   B  1 148  ? -3.266  36.497  110.374 1.00 26.67 ? 146  THR   B CA    1 
ATOM   9663  C  C     . THR   B  1 148  ? -4.325  37.130  111.266 1.00 27.45 ? 146  THR   B C     1 
ATOM   9664  O  O     . THR   B  1 148  ? -5.469  36.670  111.307 1.00 26.34 ? 146  THR   B O     1 
ATOM   9665  C  CB    . THR   B  1 148  ? -2.261  35.695  111.200 1.00 32.79 ? 146  THR   B CB    1 
ATOM   9666  O  OG1   . THR   B  1 148  ? -1.382  34.982  110.317 1.00 35.49 ? 146  THR   B OG1   1 
ATOM   9667  C  CG2   . THR   B  1 148  ? -2.985  34.709  112.117 1.00 33.50 ? 146  THR   B CG2   1 
ATOM   9668  N  N     . TRP   B  1 149  ? -3.972  38.205  111.975 1.00 25.84 ? 147  TRP   B N     1 
ATOM   9669  C  CA    . TRP   B  1 149  ? -4.968  38.857  112.813 1.00 25.34 ? 147  TRP   B CA    1 
ATOM   9670  C  C     . TRP   B  1 149  ? -6.039  39.546  111.978 1.00 23.38 ? 147  TRP   B C     1 
ATOM   9671  O  O     . TRP   B  1 149  ? -7.189  39.651  112.421 1.00 27.47 ? 147  TRP   B O     1 
ATOM   9672  C  CB    . TRP   B  1 149  ? -4.298  39.853  113.750 1.00 24.38 ? 147  TRP   B CB    1 
ATOM   9673  C  CG    . TRP   B  1 149  ? -3.463  39.189  114.773 1.00 28.13 ? 147  TRP   B CG    1 
ATOM   9674  C  CD1   . TRP   B  1 149  ? -2.109  39.284  114.917 1.00 25.97 ? 147  TRP   B CD1   1 
ATOM   9675  C  CD2   . TRP   B  1 149  ? -3.916  38.293  115.792 1.00 27.22 ? 147  TRP   B CD2   1 
ATOM   9676  N  NE1   . TRP   B  1 149  ? -1.695  38.518  115.980 1.00 23.02 ? 147  TRP   B NE1   1 
ATOM   9677  C  CE2   . TRP   B  1 149  ? -2.785  37.900  116.533 1.00 27.87 ? 147  TRP   B CE2   1 
ATOM   9678  C  CE3   . TRP   B  1 149  ? -5.173  37.800  116.162 1.00 30.81 ? 147  TRP   B CE3   1 
ATOM   9679  C  CZ2   . TRP   B  1 149  ? -2.869  37.025  117.618 1.00 29.52 ? 147  TRP   B CZ2   1 
ATOM   9680  C  CZ3   . TRP   B  1 149  ? -5.254  36.930  117.246 1.00 30.86 ? 147  TRP   B CZ3   1 
ATOM   9681  C  CH2   . TRP   B  1 149  ? -4.109  36.555  117.956 1.00 31.28 ? 147  TRP   B CH2   1 
ATOM   9682  N  N     . GLY   B  1 150  ? -5.675  40.039  110.794 1.00 24.07 ? 148  GLY   B N     1 
ATOM   9683  C  CA    . GLY   B  1 150  ? -6.681  40.569  109.888 1.00 25.21 ? 148  GLY   B CA    1 
ATOM   9684  C  C     . GLY   B  1 150  ? -7.741  39.538  109.558 1.00 29.51 ? 148  GLY   B C     1 
ATOM   9685  O  O     . GLY   B  1 150  ? -8.935  39.843  109.535 1.00 28.01 ? 148  GLY   B O     1 
ATOM   9686  N  N     . LEU   B  1 151  ? -7.316  38.299  109.304 1.00 29.21 ? 149  LEU   B N     1 
ATOM   9687  C  CA    . LEU   B  1 151  ? -8.268  37.211  109.119 1.00 32.06 ? 149  LEU   B CA    1 
ATOM   9688  C  C     . LEU   B  1 151  ? -9.147  37.045  110.350 1.00 30.40 ? 149  LEU   B C     1 
ATOM   9689  O  O     . LEU   B  1 151  ? -10.374 36.960  110.246 1.00 32.25 ? 149  LEU   B O     1 
ATOM   9690  C  CB    . LEU   B  1 151  ? -7.518  35.914  108.819 1.00 32.12 ? 149  LEU   B CB    1 
ATOM   9691  C  CG    . LEU   B  1 151  ? -7.885  35.176  107.532 1.00 42.72 ? 149  LEU   B CG    1 
ATOM   9692  C  CD1   . LEU   B  1 151  ? -7.231  33.805  107.521 1.00 42.43 ? 149  LEU   B CD1   1 
ATOM   9693  C  CD2   . LEU   B  1 151  ? -9.392  35.056  107.386 1.00 36.53 ? 149  LEU   B CD2   1 
ATOM   9694  N  N     . VAL   B  1 152  ? -8.527  37.007  111.531 1.00 29.96 ? 150  VAL   B N     1 
ATOM   9695  C  CA    . VAL   B  1 152  ? -9.266  36.779  112.770 1.00 31.62 ? 150  VAL   B CA    1 
ATOM   9696  C  C     . VAL   B  1 152  ? -10.296 37.875  113.006 1.00 30.61 ? 150  VAL   B C     1 
ATOM   9697  O  O     . VAL   B  1 152  ? -11.425 37.602  113.425 1.00 34.23 ? 150  VAL   B O     1 
ATOM   9698  C  CB    . VAL   B  1 152  ? -8.285  36.668  113.950 1.00 31.20 ? 150  VAL   B CB    1 
ATOM   9699  C  CG1   . VAL   B  1 152  ? -9.019  36.814  115.267 1.00 32.14 ? 150  VAL   B CG1   1 
ATOM   9700  C  CG2   . VAL   B  1 152  ? -7.539  35.349  113.886 1.00 30.91 ? 150  VAL   B CG2   1 
ATOM   9701  N  N     . VAL   B  1 153  ? -9.937  39.125  112.719 1.00 29.74 ? 151  VAL   B N     1 
ATOM   9702  C  CA    . VAL   B  1 153  ? -10.783 40.257  113.092 1.00 29.28 ? 151  VAL   B CA    1 
ATOM   9703  C  C     . VAL   B  1 153  ? -11.855 40.538  112.043 1.00 29.11 ? 151  VAL   B C     1 
ATOM   9704  O  O     . VAL   B  1 153  ? -13.000 40.852  112.381 1.00 27.42 ? 151  VAL   B O     1 
ATOM   9705  C  CB    . VAL   B  1 153  ? -9.900  41.495  113.338 1.00 29.36 ? 151  VAL   B CB    1 
ATOM   9706  C  CG1   . VAL   B  1 153  ? -10.760 42.751  113.509 1.00 30.32 ? 151  VAL   B CG1   1 
ATOM   9707  C  CG2   . VAL   B  1 153  ? -8.995  41.264  114.539 1.00 26.07 ? 151  VAL   B CG2   1 
ATOM   9708  N  N     . THR   B  1 154  ? -11.503 40.462  110.763 1.00 30.44 ? 152  THR   B N     1 
ATOM   9709  C  CA    . THR   B  1 154  ? -12.386 40.882  109.686 1.00 30.83 ? 152  THR   B CA    1 
ATOM   9710  C  C     . THR   B  1 154  ? -12.866 39.738  108.812 1.00 30.46 ? 152  THR   B C     1 
ATOM   9711  O  O     . THR   B  1 154  ? -13.781 39.943  108.009 1.00 34.62 ? 152  THR   B O     1 
ATOM   9712  C  CB    . THR   B  1 154  ? -11.684 41.912  108.779 1.00 31.70 ? 152  THR   B CB    1 
ATOM   9713  O  OG1   . THR   B  1 154  ? -10.754 41.239  107.922 1.00 30.76 ? 152  THR   B OG1   1 
ATOM   9714  C  CG2   . THR   B  1 154  ? -10.924 42.943  109.600 1.00 35.28 ? 152  THR   B CG2   1 
ATOM   9715  N  N     . GLY   B  1 155  ? -12.251 38.560  108.905 1.00 28.99 ? 153  GLY   B N     1 
ATOM   9716  C  CA    . GLY   B  1 155  ? -12.573 37.477  107.999 1.00 30.32 ? 153  GLY   B CA    1 
ATOM   9717  C  C     . GLY   B  1 155  ? -11.966 37.601  106.623 1.00 36.56 ? 153  GLY   B C     1 
ATOM   9718  O  O     . GLY   B  1 155  ? -12.271 36.777  105.753 1.00 39.50 ? 153  GLY   B O     1 
ATOM   9719  N  N     . LYS   B  1 156  ? -11.122 38.602  106.396 1.00 30.49 ? 154  LYS   B N     1 
ATOM   9720  C  CA    . LYS   B  1 156  ? -10.510 38.850  105.102 1.00 31.85 ? 154  LYS   B CA    1 
ATOM   9721  C  C     . LYS   B  1 156  ? -9.013  38.635  105.216 1.00 33.13 ? 154  LYS   B C     1 
ATOM   9722  O  O     . LYS   B  1 156  ? -8.400  39.005  106.222 1.00 29.81 ? 154  LYS   B O     1 
ATOM   9723  C  CB    . LYS   B  1 156  ? -10.806 40.271  104.616 1.00 33.04 ? 154  LYS   B CB    1 
ATOM   9724  N  N     . LEU   B  1 157  ? -8.428  38.026  104.190 1.00 32.29 ? 155  LEU   B N     1 
ATOM   9725  C  CA    . LEU   B  1 157  ? -7.002  37.754  104.152 1.00 34.48 ? 155  LEU   B CA    1 
ATOM   9726  C  C     . LEU   B  1 157  ? -6.361  38.595  103.059 1.00 38.85 ? 155  LEU   B C     1 
ATOM   9727  O  O     . LEU   B  1 157  ? -6.827  38.590  101.916 1.00 41.49 ? 155  LEU   B O     1 
ATOM   9728  C  CB    . LEU   B  1 157  ? -6.730  36.268  103.902 1.00 39.94 ? 155  LEU   B CB    1 
ATOM   9729  C  CG    . LEU   B  1 157  ? -5.261  35.855  103.754 1.00 44.76 ? 155  LEU   B CG    1 
ATOM   9730  C  CD1   . LEU   B  1 157  ? -4.486  36.075  105.050 1.00 38.35 ? 155  LEU   B CD1   1 
ATOM   9731  C  CD2   . LEU   B  1 157  ? -5.151  34.404  103.310 1.00 47.45 ? 155  LEU   B CD2   1 
ATOM   9732  N  N     . THR   B  1 158  ? -5.308  39.325  103.416 1.00 35.98 ? 156  THR   B N     1 
ATOM   9733  C  CA    . THR   B  1 158  ? -4.429  39.977  102.455 1.00 34.77 ? 156  THR   B CA    1 
ATOM   9734  C  C     . THR   B  1 158  ? -3.045  39.351  102.559 1.00 32.54 ? 156  THR   B C     1 
ATOM   9735  O  O     . THR   B  1 158  ? -2.682  38.781  103.590 1.00 31.80 ? 156  THR   B O     1 
ATOM   9736  C  CB    . THR   B  1 158  ? -4.346  41.487  102.704 1.00 35.70 ? 156  THR   B CB    1 
ATOM   9737  O  OG1   . THR   B  1 158  ? -3.659  41.725  103.938 1.00 36.17 ? 156  THR   B OG1   1 
ATOM   9738  C  CG2   . THR   B  1 158  ? -5.737  42.086  102.793 1.00 37.06 ? 156  THR   B CG2   1 
ATOM   9739  N  N     . SER   B  1 159  ? -2.258  39.440  101.484 1.00 30.03 ? 157  SER   B N     1 
ATOM   9740  C  CA    . SER   B  1 159  ? -0.937  38.827  101.549 1.00 29.02 ? 157  SER   B CA    1 
ATOM   9741  C  C     . SER   B  1 159  ? 0.082   39.746  102.207 1.00 30.59 ? 157  SER   B C     1 
ATOM   9742  O  O     . SER   B  1 159  ? 1.061   39.265  102.791 1.00 31.51 ? 157  SER   B O     1 
ATOM   9743  C  CB    . SER   B  1 159  ? -0.447  38.425  100.153 1.00 30.53 ? 157  SER   B CB    1 
ATOM   9744  O  OG    . SER   B  1 159  ? -0.272  39.555  99.320  1.00 37.37 ? 157  SER   B OG    1 
ATOM   9745  N  N     . THR   B  1 160  ? -0.116  41.056  102.119 1.00 28.40 ? 158  THR   B N     1 
ATOM   9746  C  CA    . THR   B  1 160  ? 0.742   42.009  102.803 1.00 25.77 ? 158  THR   B CA    1 
ATOM   9747  C  C     . THR   B  1 160  ? -0.135  42.942  103.631 1.00 24.21 ? 158  THR   B C     1 
ATOM   9748  O  O     . THR   B  1 160  ? -1.360  42.965  103.500 1.00 25.22 ? 158  THR   B O     1 
ATOM   9749  C  CB    . THR   B  1 160  ? 1.611   42.797  101.811 1.00 25.75 ? 158  THR   B CB    1 
ATOM   9750  O  OG1   . THR   B  1 160  ? 0.770   43.546  100.936 1.00 23.27 ? 158  THR   B OG1   1 
ATOM   9751  C  CG2   . THR   B  1 160  ? 2.477   41.859  100.979 1.00 28.81 ? 158  THR   B CG2   1 
ATOM   9752  N  N     . VAL   B  1 161  ? 0.493   43.716  104.505 1.00 21.37 ? 159  VAL   B N     1 
ATOM   9753  C  CA    . VAL   B  1 161  ? -0.254  44.502  105.473 1.00 24.52 ? 159  VAL   B CA    1 
ATOM   9754  C  C     . VAL   B  1 161  ? 0.123   45.964  105.326 1.00 23.93 ? 159  VAL   B C     1 
ATOM   9755  O  O     . VAL   B  1 161  ? 1.276   46.299  105.036 1.00 20.61 ? 159  VAL   B O     1 
ATOM   9756  C  CB    . VAL   B  1 161  ? -0.025  44.014  106.919 1.00 29.04 ? 159  VAL   B CB    1 
ATOM   9757  C  CG1   . VAL   B  1 161  ? -0.183  42.505  106.993 1.00 30.14 ? 159  VAL   B CG1   1 
ATOM   9758  C  CG2   . VAL   B  1 161  ? 1.325   44.443  107.434 1.00 25.52 ? 159  VAL   B CG2   1 
ATOM   9759  N  N     . ASN   B  1 162  ? -0.866  46.829  105.514 1.00 22.05 ? 160  ASN   B N     1 
ATOM   9760  C  CA    . ASN   B  1 162  ? -0.640  48.266  105.468 1.00 22.69 ? 160  ASN   B CA    1 
ATOM   9761  C  C     . ASN   B  1 162  ? -0.154  48.677  106.852 1.00 18.79 ? 160  ASN   B C     1 
ATOM   9762  O  O     . ASN   B  1 162  ? -0.931  48.990  107.755 1.00 18.55 ? 160  ASN   B O     1 
ATOM   9763  C  CB    . ASN   B  1 162  ? -1.905  48.998  105.039 1.00 21.44 ? 160  ASN   B CB    1 
ATOM   9764  C  CG    . ASN   B  1 162  ? -1.675  50.482  104.869 1.00 24.64 ? 160  ASN   B CG    1 
ATOM   9765  O  OD1   . ASN   B  1 162  ? -0.749  51.036  105.455 1.00 22.01 ? 160  ASN   B OD1   1 
ATOM   9766  N  ND2   . ASN   B  1 162  ? -2.521  51.136  104.081 1.00 24.99 ? 160  ASN   B ND2   1 
ATOM   9767  N  N     . ASP   B  1 163  ? 1.166   48.659  107.021 1.00 18.67 ? 161  ASP   B N     1 
ATOM   9768  C  CA    . ASP   B  1 163  ? 1.738   48.925  108.333 1.00 20.11 ? 161  ASP   B CA    1 
ATOM   9769  C  C     . ASP   B  1 163  ? 1.653   50.396  108.726 1.00 17.16 ? 161  ASP   B C     1 
ATOM   9770  O  O     . ASP   B  1 163  ? 1.722   50.702  109.917 1.00 18.80 ? 161  ASP   B O     1 
ATOM   9771  C  CB    . ASP   B  1 163  ? 3.186   48.431  108.381 1.00 20.62 ? 161  ASP   B CB    1 
ATOM   9772  C  CG    . ASP   B  1 163  ? 4.025   48.949  107.227 1.00 23.43 ? 161  ASP   B CG    1 
ATOM   9773  O  OD1   . ASP   B  1 163  ? 3.558   48.908  106.065 1.00 19.63 ? 161  ASP   B OD1   1 
ATOM   9774  O  OD2   . ASP   B  1 163  ? 5.170   49.387  107.487 1.00 25.64 ? 161  ASP   B OD2   1 
ATOM   9775  N  N     . ARG   B  1 164  ? 1.500   51.318  107.769 1.00 18.43 ? 162  ARG   B N     1 
ATOM   9776  C  CA    . ARG   B  1 164  ? 1.252   52.705  108.164 1.00 17.03 ? 162  ARG   B CA    1 
ATOM   9777  C  C     . ARG   B  1 164  ? -0.152  52.866  108.723 1.00 17.83 ? 162  ARG   B C     1 
ATOM   9778  O  O     . ARG   B  1 164  ? -0.366  53.618  109.682 1.00 17.44 ? 162  ARG   B O     1 
ATOM   9779  C  CB    . ARG   B  1 164  ? 1.464   53.648  106.978 1.00 18.31 ? 162  ARG   B CB    1 
ATOM   9780  C  CG    . ARG   B  1 164  ? 2.902   53.660  106.440 1.00 20.75 ? 162  ARG   B CG    1 
ATOM   9781  C  CD    . ARG   B  1 164  ? 3.926   53.756  107.573 1.00 29.12 ? 162  ARG   B CD    1 
ATOM   9782  N  NE    . ARG   B  1 164  ? 3.609   54.803  108.536 1.00 32.28 ? 162  ARG   B NE    1 
ATOM   9783  C  CZ    . ARG   B  1 164  ? 4.025   54.802  109.795 1.00 34.87 ? 162  ARG   B CZ    1 
ATOM   9784  N  NH1   . ARG   B  1 164  ? 4.793   53.832  110.269 1.00 35.29 ? 162  ARG   B NH1   1 
ATOM   9785  N  NH2   . ARG   B  1 164  ? 3.657   55.793  110.598 1.00 32.19 ? 162  ARG   B NH2   1 
ATOM   9786  N  N     . SER   B  1 165  ? -1.126  52.200  108.098 1.00 19.73 ? 163  SER   B N     1 
ATOM   9787  C  CA    . SER   B  1 165  ? -2.490  52.229  108.604 1.00 18.67 ? 163  SER   B CA    1 
ATOM   9788  C  C     . SER   B  1 165  ? -2.573  51.590  109.982 1.00 17.51 ? 163  SER   B C     1 
ATOM   9789  O  O     . SER   B  1 165  ? -3.255  52.099  110.873 1.00 18.00 ? 163  SER   B O     1 
ATOM   9790  C  CB    . SER   B  1 165  ? -3.409  51.505  107.618 1.00 17.27 ? 163  SER   B CB    1 
ATOM   9791  O  OG    . SER   B  1 165  ? -4.675  51.294  108.201 1.00 20.94 ? 163  SER   B OG    1 
ATOM   9792  N  N     . LEU   B  1 166  ? -1.871  50.471  110.171 1.00 19.20 ? 164  LEU   B N     1 
ATOM   9793  C  CA    . LEU   B  1 166  ? -1.886  49.778  111.456 1.00 17.63 ? 164  LEU   B CA    1 
ATOM   9794  C  C     . LEU   B  1 166  ? -1.169  50.574  112.533 1.00 17.75 ? 164  LEU   B C     1 
ATOM   9795  O  O     . LEU   B  1 166  ? -1.618  50.613  113.687 1.00 18.77 ? 164  LEU   B O     1 
ATOM   9796  C  CB    . LEU   B  1 166  ? -1.248  48.406  111.283 1.00 18.71 ? 164  LEU   B CB    1 
ATOM   9797  C  CG    . LEU   B  1 166  ? -2.142  47.460  110.500 1.00 19.77 ? 164  LEU   B CG    1 
ATOM   9798  C  CD1   . LEU   B  1 166  ? -1.374  46.217  110.185 1.00 21.38 ? 164  LEU   B CD1   1 
ATOM   9799  C  CD2   . LEU   B  1 166  ? -3.383  47.158  111.346 1.00 19.14 ? 164  LEU   B CD2   1 
ATOM   9800  N  N     . ALA   B  1 167  ? -0.034  51.191  112.191 1.00 17.56 ? 165  ALA   B N     1 
ATOM   9801  C  CA    . ALA   B  1 167  ? 0.655   52.030  113.170 1.00 20.37 ? 165  ALA   B CA    1 
ATOM   9802  C  C     . ALA   B  1 167  ? -0.202  53.228  113.552 1.00 18.87 ? 165  ALA   B C     1 
ATOM   9803  O  O     . ALA   B  1 167  ? -0.236  53.634  114.713 1.00 19.61 ? 165  ALA   B O     1 
ATOM   9804  C  CB    . ALA   B  1 167  ? 2.009   52.488  112.620 1.00 22.00 ? 165  ALA   B CB    1 
ATOM   9805  N  N     . ALA   B  1 168  ? -0.910  53.806  112.583 1.00 18.39 ? 166  ALA   B N     1 
ATOM   9806  C  CA    . ALA   B  1 168  ? -1.824  54.893  112.910 1.00 18.92 ? 166  ALA   B CA    1 
ATOM   9807  C  C     . ALA   B  1 168  ? -2.952  54.406  113.815 1.00 19.31 ? 166  ALA   B C     1 
ATOM   9808  O  O     . ALA   B  1 168  ? -3.305  55.074  114.785 1.00 19.85 ? 166  ALA   B O     1 
ATOM   9809  C  CB    . ALA   B  1 168  ? -2.376  55.508  111.619 1.00 18.81 ? 166  ALA   B CB    1 
ATOM   9810  N  N     . ALA   B  1 169  ? -3.509  53.228  113.522 1.00 19.08 ? 167  ALA   B N     1 
ATOM   9811  C  CA    . ALA   B  1 169  ? -4.624  52.700  114.304 1.00 19.45 ? 167  ALA   B CA    1 
ATOM   9812  C  C     . ALA   B  1 169  ? -4.188  52.363  115.720 1.00 19.84 ? 167  ALA   B C     1 
ATOM   9813  O  O     . ALA   B  1 169  ? -4.927  52.594  116.680 1.00 23.12 ? 167  ALA   B O     1 
ATOM   9814  C  CB    . ALA   B  1 169  ? -5.193  51.450  113.624 1.00 20.40 ? 167  ALA   B CB    1 
ATOM   9815  N  N     . LEU   B  1 170  ? -2.990  51.814  115.861 1.00 19.62 ? 168  LEU   B N     1 
ATOM   9816  C  CA    . LEU   B  1 170  ? -2.506  51.458  117.187 1.00 20.30 ? 168  LEU   B CA    1 
ATOM   9817  C  C     . LEU   B  1 170  ? -2.251  52.700  118.022 1.00 20.98 ? 168  LEU   B C     1 
ATOM   9818  O  O     . LEU   B  1 170  ? -2.639  52.759  119.191 1.00 20.61 ? 168  LEU   B O     1 
ATOM   9819  C  CB    . LEU   B  1 170  ? -1.248  50.618  117.061 1.00 20.13 ? 168  LEU   B CB    1 
ATOM   9820  C  CG    . LEU   B  1 170  ? -0.683  50.130  118.393 1.00 23.09 ? 168  LEU   B CG    1 
ATOM   9821  C  CD1   . LEU   B  1 170  ? -1.780  49.454  119.227 1.00 19.96 ? 168  LEU   B CD1   1 
ATOM   9822  C  CD2   . LEU   B  1 170  ? 0.419   49.171  118.039 1.00 23.97 ? 168  LEU   B CD2   1 
ATOM   9823  N  N     . THR   B  1 171  ? -1.611  53.709  117.438 1.00 21.27 ? 169  THR   B N     1 
ATOM   9824  C  CA    . THR   B  1 171  ? -1.472  54.978  118.143 1.00 20.53 ? 169  THR   B CA    1 
ATOM   9825  C  C     . THR   B  1 171  ? -2.832  55.520  118.551 1.00 21.94 ? 169  THR   B C     1 
ATOM   9826  O  O     . THR   B  1 171  ? -3.024  55.971  119.685 1.00 21.65 ? 169  THR   B O     1 
ATOM   9827  C  CB    . THR   B  1 171  ? -0.757  55.994  117.261 1.00 21.50 ? 169  THR   B CB    1 
ATOM   9828  O  OG1   . THR   B  1 171  ? 0.572   55.536  117.015 1.00 23.69 ? 169  THR   B OG1   1 
ATOM   9829  C  CG2   . THR   B  1 171  ? -0.719  57.353  117.945 1.00 21.00 ? 169  THR   B CG2   1 
ATOM   9830  N  N     . ARG   B  1 172  ? -3.787  55.491  117.620 1.00 22.36 ? 170  ARG   B N     1 
ATOM   9831  C  CA    . ARG   B  1 172  ? -5.091  56.078  117.888 1.00 21.54 ? 170  ARG   B CA    1 
ATOM   9832  C  C     . ARG   B  1 172  ? -5.781  55.352  119.028 1.00 21.93 ? 170  ARG   B C     1 
ATOM   9833  O  O     . ARG   B  1 172  ? -6.298  55.975  119.959 1.00 22.88 ? 170  ARG   B O     1 
ATOM   9834  C  CB    . ARG   B  1 172  ? -5.950  56.032  116.624 1.00 22.64 ? 170  ARG   B CB    1 
ATOM   9835  C  CG    . ARG   B  1 172  ? -7.197  56.900  116.732 1.00 21.91 ? 170  ARG   B CG    1 
ATOM   9836  C  CD    . ARG   B  1 172  ? -8.075  56.783  115.483 1.00 21.70 ? 170  ARG   B CD    1 
ATOM   9837  N  NE    . ARG   B  1 172  ? -7.324  56.823  114.227 1.00 21.10 ? 170  ARG   B NE    1 
ATOM   9838  C  CZ    . ARG   B  1 172  ? -7.089  55.766  113.463 1.00 20.52 ? 170  ARG   B CZ    1 
ATOM   9839  N  NH1   . ARG   B  1 172  ? -7.431  54.550  113.851 1.00 20.44 ? 170  ARG   B NH1   1 
ATOM   9840  N  NH2   . ARG   B  1 172  ? -6.497  55.934  112.277 1.00 20.05 ? 170  ARG   B NH2   1 
ATOM   9841  N  N     . LEU   B  1 173  ? -5.767  54.025  118.988 1.00 22.39 ? 171  LEU   B N     1 
ATOM   9842  C  CA    . LEU   B  1 173  ? -6.508  53.288  120.000 1.00 22.16 ? 171  LEU   B CA    1 
ATOM   9843  C  C     . LEU   B  1 173  ? -5.851  53.411  121.367 1.00 22.44 ? 171  LEU   B C     1 
ATOM   9844  O  O     . LEU   B  1 173  ? -6.552  53.486  122.377 1.00 22.90 ? 171  LEU   B O     1 
ATOM   9845  C  CB    . LEU   B  1 173  ? -6.672  51.824  119.567 1.00 21.53 ? 171  LEU   B CB    1 
ATOM   9846  C  CG    . LEU   B  1 173  ? -5.527  50.821  119.638 1.00 23.17 ? 171  LEU   B CG    1 
ATOM   9847  C  CD1   . LEU   B  1 173  ? -5.464  50.168  121.029 1.00 22.19 ? 171  LEU   B CD1   1 
ATOM   9848  C  CD2   . LEU   B  1 173  ? -5.724  49.770  118.580 1.00 26.14 ? 171  LEU   B CD2   1 
ATOM   9849  N  N     . ILE   B  1 174  ? -4.518  53.455  121.429 1.00 22.20 ? 172  ILE   B N     1 
ATOM   9850  C  CA    . ILE   B  1 174  ? -3.865  53.593  122.732 1.00 22.36 ? 172  ILE   B CA    1 
ATOM   9851  C  C     . ILE   B  1 174  ? -4.114  54.979  123.314 1.00 22.98 ? 172  ILE   B C     1 
ATOM   9852  O  O     . ILE   B  1 174  ? -4.430  55.119  124.501 1.00 23.55 ? 172  ILE   B O     1 
ATOM   9853  C  CB    . ILE   B  1 174  ? -2.360  53.301  122.628 1.00 21.90 ? 172  ILE   B CB    1 
ATOM   9854  C  CG1   . ILE   B  1 174  ? -2.127  51.840  122.233 1.00 23.26 ? 172  ILE   B CG1   1 
ATOM   9855  C  CG2   . ILE   B  1 174  ? -1.669  53.691  123.949 1.00 25.98 ? 172  ILE   B CG2   1 
ATOM   9856  C  CD1   . ILE   B  1 174  ? -0.670  51.501  121.970 1.00 27.72 ? 172  ILE   B CD1   1 
ATOM   9857  N  N     . SER   B  1 175  ? -3.963  56.027  122.495 1.00 22.91 ? 173  SER   B N     1 
ATOM   9858  C  CA    . SER   B  1 175  ? -4.193  57.376  123.005 1.00 23.53 ? 173  SER   B CA    1 
ATOM   9859  C  C     . SER   B  1 175  ? -5.655  57.583  123.370 1.00 24.10 ? 173  SER   B C     1 
ATOM   9860  O  O     . SER   B  1 175  ? -5.962  58.401  124.239 1.00 26.67 ? 173  SER   B O     1 
ATOM   9861  C  CB    . SER   B  1 175  ? -3.773  58.444  121.988 1.00 24.15 ? 173  SER   B CB    1 
ATOM   9862  O  OG    . SER   B  1 175  ? -2.445  58.260  121.524 1.00 28.12 ? 173  SER   B OG    1 
ATOM   9863  N  N     . ARG   B  1 176  ? -6.567  56.856  122.723 1.00 23.90 ? 174  ARG   B N     1 
ATOM   9864  C  CA    . ARG   B  1 176  ? -7.980  57.021  123.052 1.00 24.47 ? 174  ARG   B CA    1 
ATOM   9865  C  C     . ARG   B  1 176  ? -8.374  56.199  124.274 1.00 24.84 ? 174  ARG   B C     1 
ATOM   9866  O  O     . ARG   B  1 176  ? -9.089  56.693  125.149 1.00 26.97 ? 174  ARG   B O     1 
ATOM   9867  C  CB    . ARG   B  1 176  ? -8.845  56.634  121.846 1.00 24.15 ? 174  ARG   B CB    1 
ATOM   9868  C  CG    . ARG   B  1 176  ? -10.343 56.894  122.025 1.00 25.87 ? 174  ARG   B CG    1 
ATOM   9869  C  CD    . ARG   B  1 176  ? -11.107 56.579  120.734 1.00 26.13 ? 174  ARG   B CD    1 
ATOM   9870  N  NE    . ARG   B  1 176  ? -11.300 55.144  120.535 1.00 25.89 ? 174  ARG   B NE    1 
ATOM   9871  C  CZ    . ARG   B  1 176  ? -10.740 54.405  119.584 1.00 29.89 ? 174  ARG   B CZ    1 
ATOM   9872  N  NH1   . ARG   B  1 176  ? -9.980  54.939  118.628 1.00 25.10 ? 174  ARG   B NH1   1 
ATOM   9873  N  NH2   . ARG   B  1 176  ? -10.955 53.091  119.581 1.00 29.85 ? 174  ARG   B NH2   1 
ATOM   9874  N  N     . CYS   B  1 177  ? -7.902  54.952  124.368 1.00 26.81 ? 175  CYS   B N     1 
ATOM   9875  C  CA    . CYS   B  1 177  ? -8.410  54.028  125.375 1.00 25.94 ? 175  CYS   B CA    1 
ATOM   9876  C  C     . CYS   B  1 177  ? -7.401  53.623  126.443 1.00 28.65 ? 175  CYS   B C     1 
ATOM   9877  O  O     . CYS   B  1 177  ? -7.815  53.104  127.482 1.00 31.44 ? 175  CYS   B O     1 
ATOM   9878  C  CB    . CYS   B  1 177  ? -8.941  52.758  124.701 1.00 28.51 ? 175  CYS   B CB    1 
ATOM   9879  S  SG    . CYS   B  1 177  ? -10.271 53.066  123.502 1.00 34.12 ? 175  CYS   B SG    1 
ATOM   9880  N  N     . GLY   B  1 178  ? -6.107  53.801  126.206 1.00 28.07 ? 176  GLY   B N     1 
ATOM   9881  C  CA    . GLY   B  1 178  ? -5.165  53.633  127.300 1.00 31.37 ? 176  GLY   B CA    1 
ATOM   9882  C  C     . GLY   B  1 178  ? -4.949  52.183  127.706 1.00 31.33 ? 176  GLY   B C     1 
ATOM   9883  O  O     . GLY   B  1 178  ? -5.178  51.239  126.948 1.00 27.85 ? 176  GLY   B O     1 
ATOM   9884  N  N     . GLU   B  1 179  ? -4.487  52.025  128.947 1.00 29.30 ? 177  GLU   B N     1 
ATOM   9885  C  CA    . GLU   B  1 179  ? -4.137  50.695  129.436 1.00 31.30 ? 177  GLU   B CA    1 
ATOM   9886  C  C     . GLU   B  1 179  ? -5.283  49.693  129.382 1.00 28.44 ? 177  GLU   B C     1 
ATOM   9887  O  O     . GLU   B  1 179  ? -5.020  48.529  129.034 1.00 31.17 ? 177  GLU   B O     1 
ATOM   9888  C  CB    . GLU   B  1 179  ? -3.588  50.791  130.868 1.00 31.14 ? 177  GLU   B CB    1 
ATOM   9889  C  CG    . GLU   B  1 179  ? -2.906  49.511  131.312 1.00 33.44 ? 177  GLU   B CG    1 
ATOM   9890  C  CD    . GLU   B  1 179  ? -2.484  49.532  132.759 1.00 43.17 ? 177  GLU   B CD    1 
ATOM   9891  O  OE1   . GLU   B  1 179  ? -2.648  50.579  133.419 1.00 45.56 ? 177  GLU   B OE1   1 
ATOM   9892  O  OE2   . GLU   B  1 179  ? -1.986  48.492  133.235 1.00 48.54 ? 177  GLU   B OE2   1 
ATOM   9893  N  N     . PRO   B  1 180  ? -6.534  50.038  129.711 1.00 28.25 ? 178  PRO   B N     1 
ATOM   9894  C  CA    . PRO   B  1 180  ? -7.571  48.996  129.745 1.00 28.24 ? 178  PRO   B CA    1 
ATOM   9895  C  C     . PRO   B  1 180  ? -7.763  48.267  128.430 1.00 29.47 ? 178  PRO   B C     1 
ATOM   9896  O  O     . PRO   B  1 180  ? -8.037  47.061  128.442 1.00 29.94 ? 178  PRO   B O     1 
ATOM   9897  C  CB    . PRO   B  1 180  ? -8.826  49.775  130.161 1.00 32.53 ? 178  PRO   B CB    1 
ATOM   9898  C  CG    . PRO   B  1 180  ? -8.297  50.878  131.009 1.00 30.06 ? 178  PRO   B CG    1 
ATOM   9899  C  CD    . PRO   B  1 180  ? -7.035  51.300  130.291 1.00 32.03 ? 178  PRO   B CD    1 
ATOM   9900  N  N     . VAL   B  1 181  ? -7.612  48.939  127.289 1.00 24.83 ? 179  VAL   B N     1 
ATOM   9901  C  CA    . VAL   B  1 181  ? -7.811  48.212  126.047 1.00 23.65 ? 179  VAL   B CA    1 
ATOM   9902  C  C     . VAL   B  1 181  ? -6.610  47.317  125.747 1.00 28.30 ? 179  VAL   B C     1 
ATOM   9903  O  O     . VAL   B  1 181  ? -6.765  46.265  125.117 1.00 24.42 ? 179  VAL   B O     1 
ATOM   9904  C  CB    . VAL   B  1 181  ? -8.097  49.175  124.881 1.00 29.46 ? 179  VAL   B CB    1 
ATOM   9905  C  CG1   . VAL   B  1 181  ? -6.831  49.937  124.468 1.00 25.31 ? 179  VAL   B CG1   1 
ATOM   9906  C  CG2   . VAL   B  1 181  ? -8.662  48.413  123.698 1.00 29.47 ? 179  VAL   B CG2   1 
ATOM   9907  N  N     . ILE   B  1 182  ? -5.409  47.715  126.178 1.00 28.57 ? 180  ILE   B N     1 
ATOM   9908  C  CA    . ILE   B  1 182  ? -4.233  46.875  125.987 1.00 27.15 ? 180  ILE   B CA    1 
ATOM   9909  C  C     . ILE   B  1 182  ? -4.364  45.605  126.812 1.00 28.84 ? 180  ILE   B C     1 
ATOM   9910  O  O     . ILE   B  1 182  ? -4.124  44.495  126.317 1.00 30.52 ? 180  ILE   B O     1 
ATOM   9911  C  CB    . ILE   B  1 182  ? -2.950  47.644  126.350 1.00 26.89 ? 180  ILE   B CB    1 
ATOM   9912  C  CG1   . ILE   B  1 182  ? -2.784  48.879  125.463 1.00 27.04 ? 180  ILE   B CG1   1 
ATOM   9913  C  CG2   . ILE   B  1 182  ? -1.724  46.740  126.191 1.00 26.87 ? 180  ILE   B CG2   1 
ATOM   9914  C  CD1   . ILE   B  1 182  ? -1.786  49.888  126.027 1.00 29.45 ? 180  ILE   B CD1   1 
ATOM   9915  N  N     . ARG   B  1 183  ? -4.749  45.754  128.083 1.00 27.23 ? 181  ARG   B N     1 
ATOM   9916  C  CA    . ARG   B  1 183  ? -4.931  44.601  128.955 1.00 29.25 ? 181  ARG   B CA    1 
ATOM   9917  C  C     . ARG   B  1 183  ? -5.982  43.653  128.393 1.00 35.08 ? 181  ARG   B C     1 
ATOM   9918  O  O     . ARG   B  1 183  ? -5.771  42.435  128.341 1.00 35.27 ? 181  ARG   B O     1 
ATOM   9919  C  CB    . ARG   B  1 183  ? -5.315  45.063  130.360 1.00 29.92 ? 181  ARG   B CB    1 
ATOM   9920  N  N     . ARG   B  1 184  ? -7.118  44.201  127.948 1.00 31.03 ? 182  ARG   B N     1 
ATOM   9921  C  CA    . ARG   B  1 184  ? -8.153  43.368  127.337 1.00 32.47 ? 182  ARG   B CA    1 
ATOM   9922  C  C     . ARG   B  1 184  ? -7.632  42.654  126.097 1.00 32.42 ? 182  ARG   B C     1 
ATOM   9923  O  O     . ARG   B  1 184  ? -7.959  41.486  125.867 1.00 34.18 ? 182  ARG   B O     1 
ATOM   9924  C  CB    . ARG   B  1 184  ? -9.381  44.209  126.986 1.00 33.35 ? 182  ARG   B CB    1 
ATOM   9925  C  CG    . ARG   B  1 184  ? -10.312 44.475  128.161 1.00 41.49 ? 182  ARG   B CG    1 
ATOM   9926  C  CD    . ARG   B  1 184  ? -11.357 43.367  128.346 1.00 45.06 ? 182  ARG   B CD    1 
ATOM   9927  N  NE    . ARG   B  1 184  ? -12.524 43.554  127.485 1.00 43.27 ? 182  ARG   B NE    1 
ATOM   9928  C  CZ    . ARG   B  1 184  ? -12.965 42.670  126.599 1.00 45.12 ? 182  ARG   B CZ    1 
ATOM   9929  N  NH1   . ARG   B  1 184  ? -12.373 41.497  126.435 1.00 46.23 ? 182  ARG   B NH1   1 
ATOM   9930  N  NH2   . ARG   B  1 184  ? -14.033 42.967  125.864 1.00 42.41 ? 182  ARG   B NH2   1 
ATOM   9931  N  N     . GLY   B  1 185  ? -6.838  43.344  125.273 1.00 28.56 ? 183  GLY   B N     1 
ATOM   9932  C  CA    . GLY   B  1 185  ? -6.286  42.703  124.089 1.00 28.19 ? 183  GLY   B CA    1 
ATOM   9933  C  C     . GLY   B  1 185  ? -5.311  41.589  124.430 1.00 31.43 ? 183  GLY   B C     1 
ATOM   9934  O  O     . GLY   B  1 185  ? -5.326  40.526  123.802 1.00 31.24 ? 183  GLY   B O     1 
ATOM   9935  N  N     . VAL   B  1 186  ? -4.441  41.825  125.419 1.00 29.23 ? 184  VAL   B N     1 
ATOM   9936  C  CA    . VAL   B  1 186  ? -3.515  40.785  125.875 1.00 30.52 ? 184  VAL   B CA    1 
ATOM   9937  C  C     . VAL   B  1 186  ? -4.288  39.548  126.326 1.00 32.29 ? 184  VAL   B C     1 
ATOM   9938  O  O     . VAL   B  1 186  ? -4.000  38.424  125.899 1.00 34.92 ? 184  VAL   B O     1 
ATOM   9939  C  CB    . VAL   B  1 186  ? -2.610  41.319  127.001 1.00 30.42 ? 184  VAL   B CB    1 
ATOM   9940  C  CG1   . VAL   B  1 186  ? -1.836  40.180  127.660 1.00 29.14 ? 184  VAL   B CG1   1 
ATOM   9941  C  CG2   . VAL   B  1 186  ? -1.645  42.360  126.467 1.00 28.94 ? 184  VAL   B CG2   1 
ATOM   9942  N  N     . ASP   B  1 187  ? -5.288  39.740  127.186 1.00 34.76 ? 185  ASP   B N     1 
ATOM   9943  C  CA    . ASP   B  1 187  ? -6.069  38.605  127.671 1.00 36.52 ? 185  ASP   B CA    1 
ATOM   9944  C  C     . ASP   B  1 187  ? -6.767  37.886  126.529 1.00 40.22 ? 185  ASP   B C     1 
ATOM   9945  O  O     . ASP   B  1 187  ? -6.817  36.650  126.503 1.00 38.25 ? 185  ASP   B O     1 
ATOM   9946  C  CB    . ASP   B  1 187  ? -7.087  39.072  128.703 1.00 34.94 ? 185  ASP   B CB    1 
ATOM   9947  C  CG    . ASP   B  1 187  ? -6.428  39.643  129.943 1.00 46.32 ? 185  ASP   B CG    1 
ATOM   9948  O  OD1   . ASP   B  1 187  ? -5.180  39.577  130.042 1.00 44.69 ? 185  ASP   B OD1   1 
ATOM   9949  O  OD2   . ASP   B  1 187  ? -7.155  40.161  130.813 1.00 40.66 ? 185  ASP   B OD2   1 
ATOM   9950  N  N     . MET   B  1 188  ? -7.308  38.647  125.574 1.00 34.91 ? 186  MET   B N     1 
ATOM   9951  C  CA    . MET   B  1 188  ? -7.956  38.051  124.413 1.00 36.25 ? 186  MET   B CA    1 
ATOM   9952  C  C     . MET   B  1 188  ? -6.972  37.223  123.592 1.00 34.56 ? 186  MET   B C     1 
ATOM   9953  O  O     . MET   B  1 188  ? -7.251  36.072  123.241 1.00 38.31 ? 186  MET   B O     1 
ATOM   9954  C  CB    . MET   B  1 188  ? -8.580  39.152  123.558 1.00 38.51 ? 186  MET   B CB    1 
ATOM   9955  C  CG    . MET   B  1 188  ? -9.322  38.647  122.345 1.00 41.01 ? 186  MET   B CG    1 
ATOM   9956  S  SD    . MET   B  1 188  ? -10.622 37.521  122.856 1.00 52.46 ? 186  MET   B SD    1 
ATOM   9957  C  CE    . MET   B  1 188  ? -11.501 38.518  124.063 1.00 42.78 ? 186  MET   B CE    1 
ATOM   9958  N  N     . ALA   B  1 189  ? -5.813  37.797  123.270 1.00 32.50 ? 187  ALA   B N     1 
ATOM   9959  C  CA    . ALA   B  1 189  ? -4.832  37.061  122.483 1.00 35.34 ? 187  ALA   B CA    1 
ATOM   9960  C  C     . ALA   B  1 189  ? -4.337  35.834  123.238 1.00 39.16 ? 187  ALA   B C     1 
ATOM   9961  O  O     . ALA   B  1 189  ? -4.082  34.784  122.637 1.00 39.63 ? 187  ALA   B O     1 
ATOM   9962  C  CB    . ALA   B  1 189  ? -3.662  37.973  122.110 1.00 32.57 ? 187  ALA   B CB    1 
ATOM   9963  N  N     . MET   B  1 190  ? -4.200  35.948  124.560 1.00 38.23 ? 188  MET   B N     1 
ATOM   9964  C  CA    . MET   B  1 190  ? -3.739  34.819  125.362 1.00 42.17 ? 188  MET   B CA    1 
ATOM   9965  C  C     . MET   B  1 190  ? -4.711  33.648  125.274 1.00 40.51 ? 188  MET   B C     1 
ATOM   9966  O  O     . MET   B  1 190  ? -4.295  32.496  125.104 1.00 42.97 ? 188  MET   B O     1 
ATOM   9967  C  CB    . MET   B  1 190  ? -3.551  35.259  126.813 1.00 37.31 ? 188  MET   B CB    1 
ATOM   9968  C  CG    . MET   B  1 190  ? -2.488  34.487  127.565 1.00 43.92 ? 188  MET   B CG    1 
ATOM   9969  S  SD    . MET   B  1 190  ? -2.461  34.942  129.305 1.00 56.23 ? 188  MET   B SD    1 
ATOM   9970  C  CE    . MET   B  1 190  ? -2.169  36.707  129.213 1.00 42.45 ? 188  MET   B CE    1 
ATOM   9971  N  N     . ARG   B  1 191  ? -6.011  33.927  125.367 1.00 38.13 ? 189  ARG   B N     1 
ATOM   9972  C  CA    . ARG   B  1 191  ? -7.006  32.865  125.266 1.00 43.29 ? 189  ARG   B CA    1 
ATOM   9973  C  C     . ARG   B  1 191  ? -6.990  32.230  123.881 1.00 45.04 ? 189  ARG   B C     1 
ATOM   9974  O  O     . ARG   B  1 191  ? -6.934  31.002  123.747 1.00 43.85 ? 189  ARG   B O     1 
ATOM   9975  C  CB    . ARG   B  1 191  ? -8.392  33.418  125.595 1.00 38.42 ? 189  ARG   B CB    1 
ATOM   9976  N  N     . MET   B  1 192  ? -7.019  33.053  122.833 1.00 43.24 ? 190  MET   B N     1 
ATOM   9977  C  CA    . MET   B  1 192  ? -7.075  32.514  121.480 1.00 38.19 ? 190  MET   B CA    1 
ATOM   9978  C  C     . MET   B  1 192  ? -5.810  31.734  121.139 1.00 41.76 ? 190  MET   B C     1 
ATOM   9979  O  O     . MET   B  1 192  ? -5.879  30.610  120.626 1.00 41.20 ? 190  MET   B O     1 
ATOM   9980  C  CB    . MET   B  1 192  ? -7.292  33.646  120.475 1.00 41.72 ? 190  MET   B CB    1 
ATOM   9981  C  CG    . MET   B  1 192  ? -8.501  34.523  120.759 1.00 39.32 ? 190  MET   B CG    1 
ATOM   9982  S  SD    . MET   B  1 192  ? -8.668  35.746  119.443 1.00 50.61 ? 190  MET   B SD    1 
ATOM   9983  C  CE    . MET   B  1 192  ? -8.820  34.642  118.050 1.00 34.83 ? 190  MET   B CE    1 
ATOM   9984  N  N     . MET   B  1 193  ? -4.639  32.320  121.403 1.00 37.65 ? 191  MET   B N     1 
ATOM   9985  C  CA    . MET   B  1 193  ? -3.399  31.670  121.002 1.00 41.16 ? 191  MET   B CA    1 
ATOM   9986  C  C     . MET   B  1 193  ? -3.050  30.483  121.882 1.00 41.44 ? 191  MET   B C     1 
ATOM   9987  O  O     . MET   B  1 193  ? -2.292  29.612  121.445 1.00 45.12 ? 191  MET   B O     1 
ATOM   9988  C  CB    . MET   B  1 193  ? -2.237  32.661  121.016 1.00 38.50 ? 191  MET   B CB    1 
ATOM   9989  C  CG    . MET   B  1 193  ? -2.272  33.653  119.885 1.00 38.53 ? 191  MET   B CG    1 
ATOM   9990  S  SD    . MET   B  1 193  ? -0.685  34.481  119.709 1.00 49.66 ? 191  MET   B SD    1 
ATOM   9991  C  CE    . MET   B  1 193  ? -0.441  35.088  121.363 1.00 38.37 ? 191  MET   B CE    1 
ATOM   9992  N  N     . GLY   B  1 194  ? -3.573  30.430  123.103 1.00 41.48 ? 192  GLY   B N     1 
ATOM   9993  C  CA    . GLY   B  1 194  ? -3.202  29.372  124.024 1.00 40.75 ? 192  GLY   B CA    1 
ATOM   9994  C  C     . GLY   B  1 194  ? -4.246  28.286  124.187 1.00 42.15 ? 192  GLY   B C     1 
ATOM   9995  O  O     . GLY   B  1 194  ? -3.926  27.182  124.639 1.00 38.90 ? 192  GLY   B O     1 
ATOM   9996  N  N     . GLU   B  1 195  ? -5.496  28.580  123.820 1.00 36.47 ? 193  GLU   B N     1 
ATOM   9997  C  CA    . GLU   B  1 195  ? -6.602  27.685  124.132 1.00 38.77 ? 193  GLU   B CA    1 
ATOM   9998  C  C     . GLU   B  1 195  ? -7.511  27.432  122.935 1.00 39.75 ? 193  GLU   B C     1 
ATOM   9999  O  O     . GLU   B  1 195  ? -8.150  26.379  122.862 1.00 36.50 ? 193  GLU   B O     1 
ATOM   10000 C  CB    . GLU   B  1 195  ? -7.434  28.250  125.286 1.00 41.00 ? 193  GLU   B CB    1 
ATOM   10001 C  CG    . GLU   B  1 195  ? -6.640  28.600  126.533 1.00 48.27 ? 193  GLU   B CG    1 
ATOM   10002 C  CD    . GLU   B  1 195  ? -7.501  29.264  127.584 1.00 49.59 ? 193  GLU   B CD    1 
ATOM   10003 O  OE1   . GLU   B  1 195  ? -8.729  29.028  127.573 1.00 50.05 ? 193  GLU   B OE1   1 
ATOM   10004 O  OE2   . GLU   B  1 195  ? -6.956  30.026  128.413 1.00 57.63 ? 193  GLU   B OE2   1 
ATOM   10005 N  N     . GLN   B  1 196  ? -7.584  28.380  121.998 1.00 41.95 ? 194  GLN   B N     1 
ATOM   10006 C  CA    . GLN   B  1 196  ? -8.465  28.261  120.839 1.00 38.86 ? 194  GLN   B CA    1 
ATOM   10007 C  C     . GLN   B  1 196  ? -7.735  27.848  119.566 1.00 38.91 ? 194  GLN   B C     1 
ATOM   10008 O  O     . GLN   B  1 196  ? -8.231  26.996  118.824 1.00 41.79 ? 194  GLN   B O     1 
ATOM   10009 C  CB    . GLN   B  1 196  ? -9.206  29.578  120.594 1.00 38.02 ? 194  GLN   B CB    1 
ATOM   10010 N  N     . PHE   B  1 197  ? -6.574  28.437  119.282 1.00 33.07 ? 195  PHE   B N     1 
ATOM   10011 C  CA    . PHE   B  1 197  ? -5.793  27.990  118.133 1.00 36.34 ? 195  PHE   B CA    1 
ATOM   10012 C  C     . PHE   B  1 197  ? -5.155  26.636  118.399 1.00 36.06 ? 195  PHE   B C     1 
ATOM   10013 O  O     . PHE   B  1 197  ? -5.109  25.777  117.512 1.00 38.56 ? 195  PHE   B O     1 
ATOM   10014 C  CB    . PHE   B  1 197  ? -4.717  29.018  117.792 1.00 39.49 ? 195  PHE   B CB    1 
ATOM   10015 C  CG    . PHE   B  1 197  ? -5.265  30.344  117.354 1.00 41.38 ? 195  PHE   B CG    1 
ATOM   10016 C  CD1   . PHE   B  1 197  ? -6.550  30.443  116.849 1.00 36.40 ? 195  PHE   B CD1   1 
ATOM   10017 C  CD2   . PHE   B  1 197  ? -4.493  31.494  117.456 1.00 40.90 ? 195  PHE   B CD2   1 
ATOM   10018 C  CE1   . PHE   B  1 197  ? -7.051  31.666  116.441 1.00 43.68 ? 195  PHE   B CE1   1 
ATOM   10019 C  CE2   . PHE   B  1 197  ? -4.987  32.716  117.054 1.00 38.85 ? 195  PHE   B CE2   1 
ATOM   10020 C  CZ    . PHE   B  1 197  ? -6.266  32.804  116.549 1.00 42.62 ? 195  PHE   B CZ    1 
ATOM   10021 N  N     . VAL   B  1 198  ? -4.651  26.429  119.605 1.00 34.17 ? 196  VAL   B N     1 
ATOM   10022 C  CA    . VAL   B  1 198  ? -4.068  25.150  119.974 1.00 30.91 ? 196  VAL   B CA    1 
ATOM   10023 C  C     . VAL   B  1 198  ? -4.827  24.599  121.168 1.00 33.99 ? 196  VAL   B C     1 
ATOM   10024 O  O     . VAL   B  1 198  ? -5.459  25.336  121.938 1.00 31.01 ? 196  VAL   B O     1 
ATOM   10025 C  CB    . VAL   B  1 198  ? -2.560  25.260  120.285 1.00 28.14 ? 196  VAL   B CB    1 
ATOM   10026 C  CG1   . VAL   B  1 198  ? -1.827  25.857  119.100 1.00 30.51 ? 196  VAL   B CG1   1 
ATOM   10027 C  CG2   . VAL   B  1 198  ? -2.332  26.083  121.551 1.00 31.35 ? 196  VAL   B CG2   1 
ATOM   10028 N  N     . THR   B  1 199  ? -4.789  23.276  121.296 1.00 33.20 ? 197  THR   B N     1 
ATOM   10029 C  CA    . THR   B  1 199  ? -5.304  22.649  122.502 1.00 30.20 ? 197  THR   B CA    1 
ATOM   10030 C  C     . THR   B  1 199  ? -4.345  22.855  123.662 1.00 33.29 ? 197  THR   B C     1 
ATOM   10031 O  O     . THR   B  1 199  ? -4.772  22.909  124.817 1.00 33.57 ? 197  THR   B O     1 
ATOM   10032 C  CB    . THR   B  1 199  ? -5.552  21.166  122.238 1.00 31.89 ? 197  THR   B CB    1 
ATOM   10033 O  OG1   . THR   B  1 199  ? -6.317  21.041  121.032 1.00 35.67 ? 197  THR   B OG1   1 
ATOM   10034 C  CG2   . THR   B  1 199  ? -6.324  20.532  123.379 1.00 29.83 ? 197  THR   B CG2   1 
ATOM   10035 N  N     . GLY   B  1 200  ? -3.060  22.998  123.370 1.00 28.64 ? 198  GLY   B N     1 
ATOM   10036 C  CA    . GLY   B  1 200  ? -2.076  23.278  124.393 1.00 31.23 ? 198  GLY   B CA    1 
ATOM   10037 C  C     . GLY   B  1 200  ? -0.770  23.679  123.751 1.00 29.59 ? 198  GLY   B C     1 
ATOM   10038 O  O     . GLY   B  1 200  ? -0.545  23.444  122.564 1.00 28.58 ? 198  GLY   B O     1 
ATOM   10039 N  N     . GLU   B  1 201  ? 0.084   24.314  124.553 1.00 35.18 ? 199  GLU   B N     1 
ATOM   10040 C  CA    . GLU   B  1 201  ? 1.411   24.679  124.078 1.00 35.41 ? 199  GLU   B CA    1 
ATOM   10041 C  C     . GLU   B  1 201  ? 2.387   23.513  124.124 1.00 33.71 ? 199  GLU   B C     1 
ATOM   10042 O  O     . GLU   B  1 201  ? 3.392   23.525  123.406 1.00 36.12 ? 199  GLU   B O     1 
ATOM   10043 C  CB    . GLU   B  1 201  ? 1.959   25.839  124.904 1.00 35.50 ? 199  GLU   B CB    1 
ATOM   10044 C  CG    . GLU   B  1 201  ? 1.217   27.142  124.701 1.00 41.96 ? 199  GLU   B CG    1 
ATOM   10045 C  CD    . GLU   B  1 201  ? 1.912   28.305  125.393 1.00 50.89 ? 199  GLU   B CD    1 
ATOM   10046 O  OE1   . GLU   B  1 201  ? 2.779   28.051  126.262 1.00 49.87 ? 199  GLU   B OE1   1 
ATOM   10047 O  OE2   . GLU   B  1 201  ? 1.598   29.465  125.055 1.00 53.63 ? 199  GLU   B OE2   1 
ATOM   10048 N  N     . THR   B  1 202  ? 2.123   22.525  124.967 1.00 28.76 ? 200  THR   B N     1 
ATOM   10049 C  CA    . THR   B  1 202  ? 2.883   21.291  125.029 1.00 28.96 ? 200  THR   B CA    1 
ATOM   10050 C  C     . THR   B  1 202  ? 1.895   20.139  124.954 1.00 32.58 ? 200  THR   B C     1 
ATOM   10051 O  O     . THR   B  1 202  ? 0.690   20.324  125.156 1.00 28.64 ? 200  THR   B O     1 
ATOM   10052 C  CB    . THR   B  1 202  ? 3.687   21.179  126.325 1.00 32.32 ? 200  THR   B CB    1 
ATOM   10053 O  OG1   . THR   B  1 202  ? 2.773   21.078  127.426 1.00 30.93 ? 200  THR   B OG1   1 
ATOM   10054 C  CG2   . THR   B  1 202  ? 4.581   22.398  126.518 1.00 33.02 ? 200  THR   B CG2   1 
ATOM   10055 N  N     . ILE   B  1 203  ? 2.410   18.940  124.674 1.00 27.69 ? 201  ILE   B N     1 
ATOM   10056 C  CA    . ILE   B  1 203  ? 1.519   17.791  124.547 1.00 25.49 ? 201  ILE   B CA    1 
ATOM   10057 C  C     . ILE   B  1 203  ? 0.923   17.429  125.903 1.00 26.54 ? 201  ILE   B C     1 
ATOM   10058 O  O     . ILE   B  1 203  ? -0.250  17.043  125.999 1.00 27.70 ? 201  ILE   B O     1 
ATOM   10059 C  CB    . ILE   B  1 203  ? 2.251   16.599  123.898 1.00 25.85 ? 201  ILE   B CB    1 
ATOM   10060 C  CG1   . ILE   B  1 203  ? 1.270   15.454  123.641 1.00 24.41 ? 201  ILE   B CG1   1 
ATOM   10061 C  CG2   . ILE   B  1 203  ? 3.409   16.106  124.773 1.00 28.52 ? 201  ILE   B CG2   1 
ATOM   10062 C  CD1   . ILE   B  1 203  ? 0.154   15.833  122.671 1.00 22.66 ? 201  ILE   B CD1   1 
ATOM   10063 N  N     . ARG   B  1 204  ? 1.694   17.575  126.982 1.00 31.47 ? 202  ARG   B N     1 
ATOM   10064 C  CA    . ARG   B  1 204  ? 1.120   17.226  128.275 1.00 30.15 ? 202  ARG   B CA    1 
ATOM   10065 C  C     . ARG   B  1 204  ? 0.036   18.219  128.673 1.00 30.73 ? 202  ARG   B C     1 
ATOM   10066 O  O     . ARG   B  1 204  ? -0.966  17.822  129.271 1.00 32.05 ? 202  ARG   B O     1 
ATOM   10067 C  CB    . ARG   B  1 204  ? 2.206   17.124  129.339 1.00 33.21 ? 202  ARG   B CB    1 
ATOM   10068 C  CG    . ARG   B  1 204  ? 2.709   18.443  129.840 1.00 35.14 ? 202  ARG   B CG    1 
ATOM   10069 C  CD    . ARG   B  1 204  ? 3.652   18.254  131.016 1.00 35.18 ? 202  ARG   B CD    1 
ATOM   10070 N  NE    . ARG   B  1 204  ? 3.886   19.527  131.680 1.00 32.41 ? 202  ARG   B NE    1 
ATOM   10071 C  CZ    . ARG   B  1 204  ? 3.247   19.925  132.769 1.00 38.97 ? 202  ARG   B CZ    1 
ATOM   10072 N  NH1   . ARG   B  1 204  ? 2.359   19.149  133.372 1.00 38.75 ? 202  ARG   B NH1   1 
ATOM   10073 N  NH2   . ARG   B  1 204  ? 3.512   21.129  133.272 1.00 35.85 ? 202  ARG   B NH2   1 
ATOM   10074 N  N     . GLU   B  1 205  ? 0.177   19.494  128.297 1.00 31.84 ? 203  GLU   B N     1 
ATOM   10075 C  CA    . GLU   B  1 205  ? -0.915  20.436  128.513 1.00 31.46 ? 203  GLU   B CA    1 
ATOM   10076 C  C     . GLU   B  1 205  ? -2.114  20.089  127.638 1.00 28.71 ? 203  GLU   B C     1 
ATOM   10077 O  O     . GLU   B  1 205  ? -3.257  20.094  128.105 1.00 31.72 ? 203  GLU   B O     1 
ATOM   10078 C  CB    . GLU   B  1 205  ? -0.459  21.869  128.243 1.00 35.20 ? 203  GLU   B CB    1 
ATOM   10079 C  CG    . GLU   B  1 205  ? -1.598  22.872  128.372 1.00 39.24 ? 203  GLU   B CG    1 
ATOM   10080 C  CD    . GLU   B  1 205  ? -1.176  24.306  128.107 1.00 44.80 ? 203  GLU   B CD    1 
ATOM   10081 O  OE1   . GLU   B  1 205  ? -0.332  24.538  127.216 1.00 44.28 ? 203  GLU   B OE1   1 
ATOM   10082 O  OE2   . GLU   B  1 205  ? -1.695  25.208  128.797 1.00 52.57 ? 203  GLU   B OE2   1 
ATOM   10083 N  N     . ALA   B  1 206  ? -1.871  19.793  126.363 1.00 26.88 ? 204  ALA   B N     1 
ATOM   10084 C  CA    . ALA   B  1 206  ? -2.965  19.398  125.486 1.00 28.49 ? 204  ALA   B CA    1 
ATOM   10085 C  C     . ALA   B  1 206  ? -3.667  18.162  126.025 1.00 30.21 ? 204  ALA   B C     1 
ATOM   10086 O  O     . ALA   B  1 206  ? -4.900  18.101  126.040 1.00 28.69 ? 204  ALA   B O     1 
ATOM   10087 C  CB    . ALA   B  1 206  ? -2.446  19.155  124.072 1.00 25.67 ? 204  ALA   B CB    1 
ATOM   10088 N  N     . LEU   B  1 207  ? -2.900  17.184  126.514 1.00 27.70 ? 205  LEU   B N     1 
ATOM   10089 C  CA    . LEU   B  1 207  ? -3.508  15.965  127.039 1.00 30.03 ? 205  LEU   B CA    1 
ATOM   10090 C  C     . LEU   B  1 207  ? -4.347  16.259  128.274 1.00 33.16 ? 205  LEU   B C     1 
ATOM   10091 O  O     . LEU   B  1 207  ? -5.462  15.738  128.410 1.00 30.54 ? 205  LEU   B O     1 
ATOM   10092 C  CB    . LEU   B  1 207  ? -2.431  14.918  127.344 1.00 28.69 ? 205  LEU   B CB    1 
ATOM   10093 C  CG    . LEU   B  1 207  ? -1.796  14.293  126.091 1.00 29.70 ? 205  LEU   B CG    1 
ATOM   10094 C  CD1   . LEU   B  1 207  ? -0.451  13.632  126.414 1.00 27.76 ? 205  LEU   B CD1   1 
ATOM   10095 C  CD2   . LEU   B  1 207  ? -2.739  13.289  125.426 1.00 24.75 ? 205  LEU   B CD2   1 
ATOM   10096 N  N     . LYS   B  1 208  ? -3.839  17.100  129.181 1.00 30.29 ? 206  LYS   B N     1 
ATOM   10097 C  CA    . LYS   B  1 208  ? -4.621  17.448  130.365 1.00 31.18 ? 206  LYS   B CA    1 
ATOM   10098 C  C     . LYS   B  1 208  ? -5.933  18.126  129.982 1.00 33.02 ? 206  LYS   B C     1 
ATOM   10099 O  O     . LYS   B  1 208  ? -6.988  17.820  130.553 1.00 36.58 ? 206  LYS   B O     1 
ATOM   10100 C  CB    . LYS   B  1 208  ? -3.802  18.343  131.303 1.00 36.12 ? 206  LYS   B CB    1 
ATOM   10101 N  N     . ARG   B  1 209  ? -5.898  19.030  129.003 1.00 31.85 ? 207  ARG   B N     1 
ATOM   10102 C  CA    . ARG   B  1 209  ? -7.120  19.718  128.608 1.00 33.99 ? 207  ARG   B CA    1 
ATOM   10103 C  C     . ARG   B  1 209  ? -8.074  18.826  127.827 1.00 37.41 ? 207  ARG   B C     1 
ATOM   10104 O  O     . ARG   B  1 209  ? -9.242  19.194  127.661 1.00 37.61 ? 207  ARG   B O     1 
ATOM   10105 C  CB    . ARG   B  1 209  ? -6.783  20.956  127.780 1.00 33.05 ? 207  ARG   B CB    1 
ATOM   10106 C  CG    . ARG   B  1 209  ? -6.016  22.005  128.554 1.00 35.15 ? 207  ARG   B CG    1 
ATOM   10107 C  CD    . ARG   B  1 209  ? -5.828  23.256  127.735 1.00 40.00 ? 207  ARG   B CD    1 
ATOM   10108 N  NE    . ARG   B  1 209  ? -5.142  24.284  128.505 1.00 46.67 ? 207  ARG   B NE    1 
ATOM   10109 C  CZ    . ARG   B  1 209  ? -4.629  25.391  127.986 1.00 49.94 ? 207  ARG   B CZ    1 
ATOM   10110 N  NH1   . ARG   B  1 209  ? -4.681  25.635  126.683 1.00 43.29 ? 207  ARG   B NH1   1 
ATOM   10111 N  NH2   . ARG   B  1 209  ? -4.048  26.274  128.793 1.00 49.18 ? 207  ARG   B NH2   1 
ATOM   10112 N  N     . SER   B  1 210  ? -7.615  17.669  127.350 1.00 32.15 ? 208  SER   B N     1 
ATOM   10113 C  CA    . SER   B  1 210  ? -8.488  16.801  126.569 1.00 31.37 ? 208  SER   B CA    1 
ATOM   10114 C  C     . SER   B  1 210  ? -9.476  16.031  127.427 1.00 30.42 ? 208  SER   B C     1 
ATOM   10115 O  O     . SER   B  1 210  ? -10.490 15.558  126.903 1.00 33.31 ? 208  SER   B O     1 
ATOM   10116 C  CB    . SER   B  1 210  ? -7.657  15.817  125.753 1.00 29.32 ? 208  SER   B CB    1 
ATOM   10117 O  OG    . SER   B  1 210  ? -6.848  16.516  124.817 1.00 31.87 ? 208  SER   B OG    1 
ATOM   10118 N  N     . LYS   B  1 211  ? -9.197  15.893  128.725 1.00 34.91 ? 209  LYS   B N     1 
ATOM   10119 C  CA    . LYS   B  1 211  ? -10.020 15.056  129.589 1.00 31.07 ? 209  LYS   B CA    1 
ATOM   10120 C  C     . LYS   B  1 211  ? -11.485 15.482  129.552 1.00 33.19 ? 209  LYS   B C     1 
ATOM   10121 O  O     . LYS   B  1 211  ? -12.385 14.636  129.546 1.00 35.21 ? 209  LYS   B O     1 
ATOM   10122 C  CB    . LYS   B  1 211  ? -9.478  15.111  131.017 1.00 33.16 ? 209  LYS   B CB    1 
ATOM   10123 N  N     . GLU   B  1 212  ? -11.738 16.791  129.493 1.00 33.45 ? 210  GLU   B N     1 
ATOM   10124 C  CA    . GLU   B  1 212  ? -13.098 17.299  129.641 1.00 35.24 ? 210  GLU   B CA    1 
ATOM   10125 C  C     . GLU   B  1 212  ? -14.003 16.787  128.530 1.00 38.23 ? 210  GLU   B C     1 
ATOM   10126 O  O     . GLU   B  1 212  ? -15.068 16.218  128.793 1.00 38.93 ? 210  GLU   B O     1 
ATOM   10127 C  CB    . GLU   B  1 212  ? -13.082 18.825  129.662 1.00 40.28 ? 210  GLU   B CB    1 
ATOM   10128 C  CG    . GLU   B  1 212  ? -14.463 19.455  129.728 1.00 49.24 ? 210  GLU   B CG    1 
ATOM   10129 C  CD    . GLU   B  1 212  ? -14.427 20.960  129.534 1.00 60.68 ? 210  GLU   B CD    1 
ATOM   10130 O  OE1   . GLU   B  1 212  ? -13.375 21.572  129.819 1.00 66.05 ? 210  GLU   B OE1   1 
ATOM   10131 O  OE2   . GLU   B  1 212  ? -15.448 21.530  129.091 1.00 68.25 ? 210  GLU   B OE2   1 
ATOM   10132 N  N     . LEU   B  1 213  ? -13.594 16.975  127.279 1.00 32.55 ? 211  LEU   B N     1 
ATOM   10133 C  CA    . LEU   B  1 213  ? -14.427 16.532  126.172 1.00 38.53 ? 211  LEU   B CA    1 
ATOM   10134 C  C     . LEU   B  1 213  ? -14.343 15.033  125.954 1.00 32.94 ? 211  LEU   B C     1 
ATOM   10135 O  O     . LEU   B  1 213  ? -15.289 14.451  125.414 1.00 35.64 ? 211  LEU   B O     1 
ATOM   10136 C  CB    . LEU   B  1 213  ? -14.056 17.281  124.891 1.00 30.37 ? 211  LEU   B CB    1 
ATOM   10137 C  CG    . LEU   B  1 213  ? -14.484 18.751  124.917 1.00 34.70 ? 211  LEU   B CG    1 
ATOM   10138 C  CD1   . LEU   B  1 213  ? -14.208 19.442  123.603 1.00 34.34 ? 211  LEU   B CD1   1 
ATOM   10139 C  CD2   . LEU   B  1 213  ? -15.953 18.856  125.268 1.00 42.04 ? 211  LEU   B CD2   1 
ATOM   10140 N  N     . GLU   B  1 214  ? -13.249 14.392  126.374 1.00 33.32 ? 212  GLU   B N     1 
ATOM   10141 C  CA    . GLU   B  1 214  ? -13.204 12.935  126.321 1.00 32.93 ? 212  GLU   B CA    1 
ATOM   10142 C  C     . GLU   B  1 214  ? -14.270 12.324  127.215 1.00 35.23 ? 212  GLU   B C     1 
ATOM   10143 O  O     . GLU   B  1 214  ? -14.905 11.329  126.842 1.00 33.24 ? 212  GLU   B O     1 
ATOM   10144 C  CB    . GLU   B  1 214  ? -11.814 12.431  126.698 1.00 34.27 ? 212  GLU   B CB    1 
ATOM   10145 C  CG    . GLU   B  1 214  ? -10.831 12.558  125.542 1.00 30.78 ? 212  GLU   B CG    1 
ATOM   10146 C  CD    . GLU   B  1 214  ? -9.503  11.887  125.816 1.00 31.89 ? 212  GLU   B CD    1 
ATOM   10147 O  OE1   . GLU   B  1 214  ? -9.278  11.464  126.960 1.00 33.94 ? 212  GLU   B OE1   1 
ATOM   10148 O  OE2   . GLU   B  1 214  ? -8.681  11.794  124.883 1.00 31.76 ? 212  GLU   B OE2   1 
ATOM   10149 N  N     . GLU   B  1 215  ? -14.490 12.909  128.396 1.00 33.05 ? 213  GLU   B N     1 
ATOM   10150 C  CA    . GLU   B  1 215  ? -15.557 12.427  129.265 1.00 35.55 ? 213  GLU   B CA    1 
ATOM   10151 C  C     . GLU   B  1 215  ? -16.919 12.581  128.606 1.00 39.77 ? 213  GLU   B C     1 
ATOM   10152 O  O     . GLU   B  1 215  ? -17.831 11.789  128.874 1.00 41.01 ? 213  GLU   B O     1 
ATOM   10153 C  CB    . GLU   B  1 215  ? -15.536 13.166  130.604 1.00 37.57 ? 213  GLU   B CB    1 
ATOM   10154 C  CG    . GLU   B  1 215  ? -14.345 12.828  131.484 1.00 42.32 ? 213  GLU   B CG    1 
ATOM   10155 C  CD    . GLU   B  1 215  ? -14.596 13.115  132.959 1.00 50.20 ? 213  GLU   B CD    1 
ATOM   10156 O  OE1   . GLU   B  1 215  ? -15.771 13.265  133.361 1.00 53.93 ? 213  GLU   B OE1   1 
ATOM   10157 O  OE2   . GLU   B  1 215  ? -13.611 13.179  133.724 1.00 49.03 ? 213  GLU   B OE2   1 
ATOM   10158 N  N     . LYS   B  1 216  ? -17.079 13.591  127.750 1.00 38.23 ? 214  LYS   B N     1 
ATOM   10159 C  CA    . LYS   B  1 216  ? -18.325 13.797  127.026 1.00 36.94 ? 214  LYS   B CA    1 
ATOM   10160 C  C     . LYS   B  1 216  ? -18.413 12.953  125.760 1.00 42.79 ? 214  LYS   B C     1 
ATOM   10161 O  O     . LYS   B  1 216  ? -19.436 13.013  125.071 1.00 41.15 ? 214  LYS   B O     1 
ATOM   10162 C  CB    . LYS   B  1 216  ? -18.497 15.283  126.679 1.00 35.52 ? 214  LYS   B CB    1 
ATOM   10163 N  N     . GLY   B  1 217  ? -17.375 12.174  125.436 1.00 34.19 ? 215  GLY   B N     1 
ATOM   10164 C  CA    . GLY   B  1 217  ? -17.414 11.243  124.324 1.00 33.79 ? 215  GLY   B CA    1 
ATOM   10165 C  C     . GLY   B  1 217  ? -16.584 11.631  123.118 1.00 36.41 ? 215  GLY   B C     1 
ATOM   10166 O  O     . GLY   B  1 217  ? -16.602 10.902  122.118 1.00 34.09 ? 215  GLY   B O     1 
ATOM   10167 N  N     . PHE   B  1 218  ? -15.873 12.750  123.166 1.00 31.52 ? 216  PHE   B N     1 
ATOM   10168 C  CA    . PHE   B  1 218  ? -14.941 13.085  122.104 1.00 34.63 ? 216  PHE   B CA    1 
ATOM   10169 C  C     . PHE   B  1 218  ? -13.670 12.253  122.238 1.00 32.32 ? 216  PHE   B C     1 
ATOM   10170 O  O     . PHE   B  1 218  ? -13.344 11.737  123.308 1.00 29.57 ? 216  PHE   B O     1 
ATOM   10171 C  CB    . PHE   B  1 218  ? -14.581 14.571  122.141 1.00 32.25 ? 216  PHE   B CB    1 
ATOM   10172 C  CG    . PHE   B  1 218  ? -15.702 15.488  121.738 1.00 32.49 ? 216  PHE   B CG    1 
ATOM   10173 C  CD1   . PHE   B  1 218  ? -16.632 15.927  122.671 1.00 35.79 ? 216  PHE   B CD1   1 
ATOM   10174 C  CD2   . PHE   B  1 218  ? -15.809 15.935  120.427 1.00 34.53 ? 216  PHE   B CD2   1 
ATOM   10175 C  CE1   . PHE   B  1 218  ? -17.650 16.785  122.304 1.00 36.94 ? 216  PHE   B CE1   1 
ATOM   10176 C  CE2   . PHE   B  1 218  ? -16.822 16.791  120.049 1.00 35.26 ? 216  PHE   B CE2   1 
ATOM   10177 C  CZ    . PHE   B  1 218  ? -17.752 17.214  120.988 1.00 36.68 ? 216  PHE   B CZ    1 
ATOM   10178 N  N     . SER   B  1 219  ? -12.951 12.121  121.131 1.00 30.93 ? 217  SER   B N     1 
ATOM   10179 C  CA    . SER   B  1 219  ? -11.579 11.633  121.155 1.00 28.55 ? 217  SER   B CA    1 
ATOM   10180 C  C     . SER   B  1 219  ? -10.689 12.691  120.519 1.00 28.52 ? 217  SER   B C     1 
ATOM   10181 O  O     . SER   B  1 219  ? -11.159 13.741  120.074 1.00 25.97 ? 217  SER   B O     1 
ATOM   10182 C  CB    . SER   B  1 219  ? -11.449 10.287  120.439 1.00 31.25 ? 217  SER   B CB    1 
ATOM   10183 O  OG    . SER   B  1 219  ? -11.784 10.420  119.063 1.00 32.52 ? 217  SER   B OG    1 
ATOM   10184 N  N     . TYR   B  1 220  ? -9.389  12.410  120.465 1.00 26.68 ? 218  TYR   B N     1 
ATOM   10185 C  CA    . TYR   B  1 220  ? -8.436  13.413  120.021 1.00 23.00 ? 218  TYR   B CA    1 
ATOM   10186 C  C     . TYR   B  1 220  ? -7.432  12.811  119.055 1.00 22.03 ? 218  TYR   B C     1 
ATOM   10187 O  O     . TYR   B  1 220  ? -7.124  11.619  119.104 1.00 25.87 ? 218  TYR   B O     1 
ATOM   10188 C  CB    . TYR   B  1 220  ? -7.689  14.045  121.211 1.00 24.62 ? 218  TYR   B CB    1 
ATOM   10189 C  CG    . TYR   B  1 220  ? -8.482  15.135  121.877 1.00 25.39 ? 218  TYR   B CG    1 
ATOM   10190 C  CD1   . TYR   B  1 220  ? -9.413  14.839  122.872 1.00 28.08 ? 218  TYR   B CD1   1 
ATOM   10191 C  CD2   . TYR   B  1 220  ? -8.332  16.456  121.487 1.00 23.98 ? 218  TYR   B CD2   1 
ATOM   10192 C  CE1   . TYR   B  1 220  ? -10.168 15.842  123.464 1.00 29.66 ? 218  TYR   B CE1   1 
ATOM   10193 C  CE2   . TYR   B  1 220  ? -9.072  17.463  122.071 1.00 27.63 ? 218  TYR   B CE2   1 
ATOM   10194 C  CZ    . TYR   B  1 220  ? -9.985  17.153  123.059 1.00 27.19 ? 218  TYR   B CZ    1 
ATOM   10195 O  OH    . TYR   B  1 220  ? -10.710 18.161  123.640 1.00 28.97 ? 218  TYR   B OH    1 
ATOM   10196 N  N     . SER   B  1 221  ? -6.931  13.660  118.168 1.00 22.06 ? 219  SER   B N     1 
ATOM   10197 C  CA    . SER   B  1 221  ? -5.760  13.366  117.359 1.00 22.21 ? 219  SER   B CA    1 
ATOM   10198 C  C     . SER   B  1 221  ? -4.876  14.598  117.424 1.00 24.02 ? 219  SER   B C     1 
ATOM   10199 O  O     . SER   B  1 221  ? -5.286  15.677  116.986 1.00 24.23 ? 219  SER   B O     1 
ATOM   10200 C  CB    . SER   B  1 221  ? -6.140  13.046  115.910 1.00 22.51 ? 219  SER   B CB    1 
ATOM   10201 O  OG    . SER   B  1 221  ? -4.987  12.785  115.131 1.00 22.85 ? 219  SER   B OG    1 
ATOM   10202 N  N     . TYR   B  1 222  ? -3.683  14.450  117.994 1.00 21.68 ? 220  TYR   B N     1 
ATOM   10203 C  CA    . TYR   B  1 222  ? -2.821  15.599  118.236 1.00 21.26 ? 220  TYR   B CA    1 
ATOM   10204 C  C     . TYR   B  1 222  ? -1.926  15.870  117.049 1.00 22.34 ? 220  TYR   B C     1 
ATOM   10205 O  O     . TYR   B  1 222  ? -1.349  14.953  116.462 1.00 22.32 ? 220  TYR   B O     1 
ATOM   10206 C  CB    . TYR   B  1 222  ? -1.983  15.387  119.490 1.00 21.94 ? 220  TYR   B CB    1 
ATOM   10207 C  CG    . TYR   B  1 222  ? -2.898  15.247  120.654 1.00 22.25 ? 220  TYR   B CG    1 
ATOM   10208 C  CD1   . TYR   B  1 222  ? -3.458  16.364  121.233 1.00 20.46 ? 220  TYR   B CD1   1 
ATOM   10209 C  CD2   . TYR   B  1 222  ? -3.262  13.997  121.124 1.00 24.80 ? 220  TYR   B CD2   1 
ATOM   10210 C  CE1   . TYR   B  1 222  ? -4.330  16.250  122.271 1.00 25.72 ? 220  TYR   B CE1   1 
ATOM   10211 C  CE2   . TYR   B  1 222  ? -4.135  13.865  122.176 1.00 26.32 ? 220  TYR   B CE2   1 
ATOM   10212 C  CZ    . TYR   B  1 222  ? -4.664  14.997  122.745 1.00 28.81 ? 220  TYR   B CZ    1 
ATOM   10213 O  OH    . TYR   B  1 222  ? -5.546  14.880  123.785 1.00 27.30 ? 220  TYR   B OH    1 
ATOM   10214 N  N     . ASP   B  1 223  ? -1.797  17.150  116.733 1.00 21.07 ? 221  ASP   B N     1 
ATOM   10215 C  CA    . ASP   B  1 223  ? -1.001  17.645  115.623 1.00 22.58 ? 221  ASP   B CA    1 
ATOM   10216 C  C     . ASP   B  1 223  ? 0.123   18.485  116.226 1.00 27.20 ? 221  ASP   B C     1 
ATOM   10217 O  O     . ASP   B  1 223  ? -0.095  19.634  116.623 1.00 25.33 ? 221  ASP   B O     1 
ATOM   10218 C  CB    . ASP   B  1 223  ? -1.885  18.449  114.679 1.00 24.54 ? 221  ASP   B CB    1 
ATOM   10219 C  CG    . ASP   B  1 223  ? -1.094  19.269  113.691 1.00 32.66 ? 221  ASP   B CG    1 
ATOM   10220 O  OD1   . ASP   B  1 223  ? 0.009   18.838  113.301 1.00 28.33 ? 221  ASP   B OD1   1 
ATOM   10221 O  OD2   . ASP   B  1 223  ? -1.587  20.350  113.308 1.00 33.41 ? 221  ASP   B OD2   1 
ATOM   10222 N  N     . MET   B  1 224  ? 1.307   17.894  116.359 1.00 26.01 ? 222  MET   B N     1 
ATOM   10223 C  CA    . MET   B  1 224  ? 2.476   18.672  116.741 1.00 28.28 ? 222  MET   B CA    1 
ATOM   10224 C  C     . MET   B  1 224  ? 2.799   19.596  115.580 1.00 30.26 ? 222  MET   B C     1 
ATOM   10225 O  O     . MET   B  1 224  ? 3.132   19.128  114.488 1.00 32.87 ? 222  MET   B O     1 
ATOM   10226 C  CB    . MET   B  1 224  ? 3.652   17.759  117.076 1.00 30.08 ? 222  MET   B CB    1 
ATOM   10227 C  CG    . MET   B  1 224  ? 3.335   16.739  118.157 1.00 24.03 ? 222  MET   B CG    1 
ATOM   10228 S  SD    . MET   B  1 224  ? 2.678   17.464  119.676 1.00 31.80 ? 222  MET   B SD    1 
ATOM   10229 C  CE    . MET   B  1 224  ? 4.142   18.222  120.339 1.00 26.33 ? 222  MET   B CE    1 
ATOM   10230 N  N     . LEU   B  1 225  ? 2.633   20.896  115.791 1.00 32.77 ? 223  LEU   B N     1 
ATOM   10231 C  CA    . LEU   B  1 225  ? 2.732   21.847  114.693 1.00 30.41 ? 223  LEU   B CA    1 
ATOM   10232 C  C     . LEU   B  1 225  ? 4.076   21.700  114.000 1.00 39.02 ? 223  LEU   B C     1 
ATOM   10233 O  O     . LEU   B  1 225  ? 5.130   21.850  114.629 1.00 40.28 ? 223  LEU   B O     1 
ATOM   10234 C  CB    . LEU   B  1 225  ? 2.543   23.264  115.214 1.00 32.65 ? 223  LEU   B CB    1 
ATOM   10235 C  CG    . LEU   B  1 225  ? 1.124   23.506  115.720 1.00 31.96 ? 223  LEU   B CG    1 
ATOM   10236 C  CD1   . LEU   B  1 225  ? 0.997   24.911  116.281 1.00 41.56 ? 223  LEU   B CD1   1 
ATOM   10237 C  CD2   . LEU   B  1 225  ? 0.129   23.270  114.590 1.00 34.86 ? 223  LEU   B CD2   1 
ATOM   10238 N  N     . GLY   B  1 226  ? 4.028   21.377  112.711 1.00 33.37 ? 224  GLY   B N     1 
ATOM   10239 C  CA    . GLY   B  1 226  ? 5.225   21.044  111.971 1.00 35.59 ? 224  GLY   B CA    1 
ATOM   10240 C  C     . GLY   B  1 226  ? 4.899   20.527  110.587 1.00 31.35 ? 224  GLY   B C     1 
ATOM   10241 O  O     . GLY   B  1 226  ? 4.034   19.661  110.414 1.00 28.63 ? 224  GLY   B O     1 
ATOM   10242 N  N     . GLU   B  1 227  ? 5.579   21.072  109.588 1.00 32.00 ? 225  GLU   B N     1 
ATOM   10243 C  CA    . GLU   B  1 227  ? 5.397   20.655  108.203 1.00 28.81 ? 225  GLU   B CA    1 
ATOM   10244 C  C     . GLU   B  1 227  ? 6.484   21.316  107.376 1.00 27.64 ? 225  GLU   B C     1 
ATOM   10245 O  O     . GLU   B  1 227  ? 7.152   22.252  107.828 1.00 29.27 ? 225  GLU   B O     1 
ATOM   10246 C  CB    . GLU   B  1 227  ? 4.017   21.025  107.662 1.00 32.97 ? 225  GLU   B CB    1 
ATOM   10247 C  CG    . GLU   B  1 227  ? 3.703   22.495  107.704 1.00 33.49 ? 225  GLU   B CG    1 
ATOM   10248 C  CD    . GLU   B  1 227  ? 2.274   22.774  107.262 1.00 40.44 ? 225  GLU   B CD    1 
ATOM   10249 O  OE1   . GLU   B  1 227  ? 1.983   22.649  106.054 1.00 39.46 ? 225  GLU   B OE1   1 
ATOM   10250 O  OE2   . GLU   B  1 227  ? 1.440   23.095  108.131 1.00 40.27 ? 225  GLU   B OE2   1 
ATOM   10251 N  N     . ALA   B  1 228  ? 6.645   20.811  106.156 1.00 24.52 ? 226  ALA   B N     1 
ATOM   10252 C  CA    . ALA   B  1 228  ? 7.543   21.391  105.169 1.00 25.92 ? 226  ALA   B CA    1 
ATOM   10253 C  C     . ALA   B  1 228  ? 8.894   21.717  105.793 1.00 27.84 ? 226  ALA   B C     1 
ATOM   10254 O  O     . ALA   B  1 228  ? 9.321   22.872  105.856 1.00 24.14 ? 226  ALA   B O     1 
ATOM   10255 C  CB    . ALA   B  1 228  ? 6.914   22.631  104.525 1.00 27.72 ? 226  ALA   B CB    1 
ATOM   10256 N  N     . ALA   B  1 229  ? 9.542   20.668  106.299 1.00 23.25 ? 227  ALA   B N     1 
ATOM   10257 C  CA    . ALA   B  1 229  ? 10.935  20.776  106.725 1.00 22.96 ? 227  ALA   B CA    1 
ATOM   10258 C  C     . ALA   B  1 229  ? 11.779  21.391  105.616 1.00 20.26 ? 227  ALA   B C     1 
ATOM   10259 O  O     . ALA   B  1 229  ? 11.682  20.992  104.454 1.00 21.48 ? 227  ALA   B O     1 
ATOM   10260 C  CB    . ALA   B  1 229  ? 11.475  19.394  107.091 1.00 21.19 ? 227  ALA   B CB    1 
ATOM   10261 N  N     . THR   B  1 230  ? 12.582  22.388  105.978 1.00 19.42 ? 228  THR   B N     1 
ATOM   10262 C  CA    . THR   B  1 230  ? 13.484  23.036  105.036 1.00 23.18 ? 228  THR   B CA    1 
ATOM   10263 C  C     . THR   B  1 230  ? 14.882  22.424  105.083 1.00 22.07 ? 228  THR   B C     1 
ATOM   10264 O  O     . THR   B  1 230  ? 15.555  22.327  104.053 1.00 21.88 ? 228  THR   B O     1 
ATOM   10265 C  CB    . THR   B  1 230  ? 13.562  24.533  105.343 1.00 24.03 ? 228  THR   B CB    1 
ATOM   10266 O  OG1   . THR   B  1 230  ? 12.244  25.087  105.335 1.00 29.63 ? 228  THR   B OG1   1 
ATOM   10267 C  CG2   . THR   B  1 230  ? 14.393  25.250  104.299 1.00 23.25 ? 228  THR   B CG2   1 
ATOM   10268 N  N     . THR   B  1 231  ? 15.319  22.012  106.268 1.00 18.88 ? 229  THR   B N     1 
ATOM   10269 C  CA    . THR   B  1 231  ? 16.647  21.458  106.482 1.00 20.92 ? 229  THR   B CA    1 
ATOM   10270 C  C     . THR   B  1 231  ? 16.534  20.087  107.128 1.00 21.79 ? 229  THR   B C     1 
ATOM   10271 O  O     . THR   B  1 231  ? 15.489  19.719  107.671 1.00 20.05 ? 229  THR   B O     1 
ATOM   10272 C  CB    . THR   B  1 231  ? 17.497  22.342  107.389 1.00 20.49 ? 229  THR   B CB    1 
ATOM   10273 O  OG1   . THR   B  1 231  ? 16.989  22.252  108.731 1.00 21.29 ? 229  THR   B OG1   1 
ATOM   10274 C  CG2   . THR   B  1 231  ? 17.456  23.781  106.916 1.00 20.85 ? 229  THR   B CG2   1 
ATOM   10275 N  N     . ALA   B  1 232  ? 17.639  19.340  107.060 1.00 19.71 ? 230  ALA   B N     1 
ATOM   10276 C  CA    . ALA   B  1 232  ? 17.708  18.067  107.767 1.00 21.59 ? 230  ALA   B CA    1 
ATOM   10277 C  C     . ALA   B  1 232  ? 17.441  18.248  109.256 1.00 22.61 ? 230  ALA   B C     1 
ATOM   10278 O  O     . ALA   B  1 232  ? 16.777  17.411  109.881 1.00 21.02 ? 230  ALA   B O     1 
ATOM   10279 C  CB    . ALA   B  1 232  ? 19.074  17.419  107.546 1.00 23.10 ? 230  ALA   B CB    1 
ATOM   10280 N  N     . ALA   B  1 233  ? 17.965  19.330  109.845 1.00 21.59 ? 231  ALA   B N     1 
ATOM   10281 C  CA    . ALA   B  1 233  ? 17.771  19.577  111.271 1.00 22.21 ? 231  ALA   B CA    1 
ATOM   10282 C  C     . ALA   B  1 233  ? 16.304  19.833  111.594 1.00 22.42 ? 231  ALA   B C     1 
ATOM   10283 O  O     . ALA   B  1 233  ? 15.829  19.435  112.659 1.00 20.97 ? 231  ALA   B O     1 
ATOM   10284 C  CB    . ALA   B  1 233  ? 18.634  20.759  111.730 1.00 23.35 ? 231  ALA   B CB    1 
ATOM   10285 N  N     . ASP   B  1 234  ? 15.579  20.517  110.698 1.00 19.88 ? 232  ASP   B N     1 
ATOM   10286 C  CA    . ASP   B  1 234  ? 14.136  20.667  110.870 1.00 20.45 ? 232  ASP   B CA    1 
ATOM   10287 C  C     . ASP   B  1 234  ? 13.456  19.308  110.935 1.00 21.57 ? 232  ASP   B C     1 
ATOM   10288 O  O     . ASP   B  1 234  ? 12.648  19.042  111.832 1.00 21.98 ? 232  ASP   B O     1 
ATOM   10289 C  CB    . ASP   B  1 234  ? 13.526  21.462  109.710 1.00 23.43 ? 232  ASP   B CB    1 
ATOM   10290 C  CG    . ASP   B  1 234  ? 13.949  22.906  109.685 1.00 27.25 ? 232  ASP   B CG    1 
ATOM   10291 O  OD1   . ASP   B  1 234  ? 14.383  23.432  110.730 1.00 28.10 ? 232  ASP   B OD1   1 
ATOM   10292 O  OD2   . ASP   B  1 234  ? 13.818  23.515  108.599 1.00 29.08 ? 232  ASP   B OD2   1 
ATOM   10293 N  N     . ALA   B  1 235  ? 13.738  18.456  109.947 1.00 18.94 ? 233  ALA   B N     1 
ATOM   10294 C  CA    . ALA   B  1 235  ? 13.063  17.169  109.858 1.00 21.40 ? 233  ALA   B CA    1 
ATOM   10295 C  C     . ALA   B  1 235  ? 13.383  16.310  111.070 1.00 19.08 ? 233  ALA   B C     1 
ATOM   10296 O  O     . ALA   B  1 235  ? 12.507  15.612  111.595 1.00 19.97 ? 233  ALA   B O     1 
ATOM   10297 C  CB    . ALA   B  1 235  ? 13.462  16.452  108.567 1.00 22.93 ? 233  ALA   B CB    1 
ATOM   10298 N  N     . GLU   B  1 236  ? 14.631  16.359  111.534 1.00 18.76 ? 234  GLU   B N     1 
ATOM   10299 C  CA    . GLU   B  1 236  ? 15.003  15.581  112.706 1.00 20.72 ? 234  GLU   B CA    1 
ATOM   10300 C  C     . GLU   B  1 236  ? 14.299  16.111  113.945 1.00 21.92 ? 234  GLU   B C     1 
ATOM   10301 O  O     . GLU   B  1 236  ? 13.852  15.330  114.795 1.00 24.35 ? 234  GLU   B O     1 
ATOM   10302 C  CB    . GLU   B  1 236  ? 16.525  15.607  112.880 1.00 22.19 ? 234  GLU   B CB    1 
ATOM   10303 C  CG    . GLU   B  1 236  ? 17.059  14.646  113.917 1.00 24.10 ? 234  GLU   B CG    1 
ATOM   10304 C  CD    . GLU   B  1 236  ? 18.578  14.622  113.936 1.00 32.79 ? 234  GLU   B CD    1 
ATOM   10305 O  OE1   . GLU   B  1 236  ? 19.197  15.044  112.933 1.00 34.97 ? 234  GLU   B OE1   1 
ATOM   10306 O  OE2   . GLU   B  1 236  ? 19.148  14.179  114.952 1.00 36.66 ? 234  GLU   B OE2   1 
ATOM   10307 N  N     . ARG   B  1 237  ? 14.178  17.436  114.054 1.00 18.64 ? 235  ARG   B N     1 
ATOM   10308 C  CA    . ARG   B  1 237  ? 13.437  18.024  115.163 1.00 22.99 ? 235  ARG   B CA    1 
ATOM   10309 C  C     . ARG   B  1 237  ? 11.975  17.591  115.137 1.00 21.99 ? 235  ARG   B C     1 
ATOM   10310 O  O     . ARG   B  1 237  ? 11.429  17.136  116.150 1.00 20.42 ? 235  ARG   B O     1 
ATOM   10311 C  CB    . ARG   B  1 237  ? 13.536  19.550  115.120 1.00 24.09 ? 235  ARG   B CB    1 
ATOM   10312 C  CG    . ARG   B  1 237  ? 12.863  20.223  116.320 1.00 27.48 ? 235  ARG   B CG    1 
ATOM   10313 C  CD    . ARG   B  1 237  ? 12.871  21.756  116.245 1.00 37.10 ? 235  ARG   B CD    1 
ATOM   10314 N  NE    . ARG   B  1 237  ? 12.150  22.260  115.080 1.00 40.24 ? 235  ARG   B NE    1 
ATOM   10315 C  CZ    . ARG   B  1 237  ? 12.721  22.851  114.037 1.00 42.24 ? 235  ARG   B CZ    1 
ATOM   10316 N  NH1   . ARG   B  1 237  ? 14.024  23.087  114.002 1.00 38.13 ? 235  ARG   B NH1   1 
ATOM   10317 N  NH2   . ARG   B  1 237  ? 11.965  23.214  113.003 1.00 41.30 ? 235  ARG   B NH2   1 
ATOM   10318 N  N     . TYR   B  1 238  ? 11.319  17.743  113.986 1.00 20.15 ? 236  TYR   B N     1 
ATOM   10319 C  CA    . TYR   B  1 238  ? 9.927   17.311  113.875 1.00 21.78 ? 236  TYR   B CA    1 
ATOM   10320 C  C     . TYR   B  1 238  ? 9.776   15.830  114.210 1.00 20.36 ? 236  TYR   B C     1 
ATOM   10321 O  O     . TYR   B  1 238  ? 8.809   15.428  114.869 1.00 20.02 ? 236  TYR   B O     1 
ATOM   10322 C  CB    . TYR   B  1 238  ? 9.399   17.598  112.471 1.00 21.07 ? 236  TYR   B CB    1 
ATOM   10323 C  CG    . TYR   B  1 238  ? 9.244   19.070  112.137 1.00 21.64 ? 236  TYR   B CG    1 
ATOM   10324 C  CD1   . TYR   B  1 238  ? 8.850   19.989  113.104 1.00 30.95 ? 236  TYR   B CD1   1 
ATOM   10325 C  CD2   . TYR   B  1 238  ? 9.478   19.535  110.845 1.00 22.93 ? 236  TYR   B CD2   1 
ATOM   10326 C  CE1   . TYR   B  1 238  ? 8.699   21.336  112.795 1.00 34.45 ? 236  TYR   B CE1   1 
ATOM   10327 C  CE2   . TYR   B  1 238  ? 9.327   20.874  110.526 1.00 29.55 ? 236  TYR   B CE2   1 
ATOM   10328 C  CZ    . TYR   B  1 238  ? 8.941   21.771  111.507 1.00 38.15 ? 236  TYR   B CZ    1 
ATOM   10329 O  OH    . TYR   B  1 238  ? 8.794   23.103  111.190 1.00 37.35 ? 236  TYR   B OH    1 
ATOM   10330 N  N     . TYR   B  1 239  ? 10.712  14.998  113.748 1.00 18.55 ? 237  TYR   B N     1 
ATOM   10331 C  CA    . TYR   B  1 239  ? 10.681  13.589  114.118 1.00 19.21 ? 237  TYR   B CA    1 
ATOM   10332 C  C     . TYR   B  1 239  ? 10.696  13.426  115.629 1.00 22.55 ? 237  TYR   B C     1 
ATOM   10333 O  O     . TYR   B  1 239  ? 9.899   12.668  116.200 1.00 19.69 ? 237  TYR   B O     1 
ATOM   10334 C  CB    . TYR   B  1 239  ? 11.874  12.847  113.515 1.00 21.43 ? 237  TYR   B CB    1 
ATOM   10335 C  CG    . TYR   B  1 239  ? 11.916  11.413  113.980 1.00 25.58 ? 237  TYR   B CG    1 
ATOM   10336 C  CD1   . TYR   B  1 239  ? 11.256  10.417  113.273 1.00 26.63 ? 237  TYR   B CD1   1 
ATOM   10337 C  CD2   . TYR   B  1 239  ? 12.573  11.057  115.152 1.00 29.04 ? 237  TYR   B CD2   1 
ATOM   10338 C  CE1   . TYR   B  1 239  ? 11.270  9.109   113.713 1.00 23.72 ? 237  TYR   B CE1   1 
ATOM   10339 C  CE2   . TYR   B  1 239  ? 12.571  9.755   115.601 1.00 29.04 ? 237  TYR   B CE2   1 
ATOM   10340 C  CZ    . TYR   B  1 239  ? 11.925  8.789   114.869 1.00 27.46 ? 237  TYR   B CZ    1 
ATOM   10341 O  OH    . TYR   B  1 239  ? 11.938  7.490   115.304 1.00 31.46 ? 237  TYR   B OH    1 
ATOM   10342 N  N     . ARG   B  1 240  ? 11.629  14.112  116.293 1.00 20.11 ? 238  ARG   B N     1 
ATOM   10343 C  CA    . ARG   B  1 240  ? 11.752  13.980  117.738 1.00 22.24 ? 238  ARG   B CA    1 
ATOM   10344 C  C     . ARG   B  1 240  ? 10.511  14.498  118.446 1.00 21.42 ? 238  ARG   B C     1 
ATOM   10345 O  O     . ARG   B  1 240  ? 10.099  13.937  119.465 1.00 21.53 ? 238  ARG   B O     1 
ATOM   10346 C  CB    . ARG   B  1 240  ? 13.006  14.711  118.221 1.00 20.45 ? 238  ARG   B CB    1 
ATOM   10347 C  CG    . ARG   B  1 240  ? 14.286  14.073  117.708 1.00 24.85 ? 238  ARG   B CG    1 
ATOM   10348 C  CD    . ARG   B  1 240  ? 14.432  12.644  118.208 1.00 27.49 ? 238  ARG   B CD    1 
ATOM   10349 N  NE    . ARG   B  1 240  ? 15.571  11.976  117.593 1.00 32.68 ? 238  ARG   B NE    1 
ATOM   10350 C  CZ    . ARG   B  1 240  ? 15.866  10.695  117.759 1.00 39.42 ? 238  ARG   B CZ    1 
ATOM   10351 N  NH1   . ARG   B  1 240  ? 15.130  9.910   118.530 1.00 32.80 ? 238  ARG   B NH1   1 
ATOM   10352 N  NH2   . ARG   B  1 240  ? 16.929  10.188  117.140 1.00 42.82 ? 238  ARG   B NH2   1 
ATOM   10353 N  N     . ASP   B  1 241  ? 9.902   15.565  117.916 1.00 19.44 ? 239  ASP   B N     1 
ATOM   10354 C  CA    . ASP   B  1 241  ? 8.665   16.076  118.494 1.00 22.11 ? 239  ASP   B CA    1 
ATOM   10355 C  C     . ASP   B  1 241  ? 7.536   15.062  118.361 1.00 20.08 ? 239  ASP   B C     1 
ATOM   10356 O  O     . ASP   B  1 241  ? 6.768   14.856  119.303 1.00 21.16 ? 239  ASP   B O     1 
ATOM   10357 C  CB    . ASP   B  1 241  ? 8.251   17.382  117.819 1.00 23.18 ? 239  ASP   B CB    1 
ATOM   10358 C  CG    . ASP   B  1 241  ? 9.135   18.554  118.194 1.00 28.93 ? 239  ASP   B CG    1 
ATOM   10359 O  OD1   . ASP   B  1 241  ? 9.924   18.444  119.155 1.00 31.84 ? 239  ASP   B OD1   1 
ATOM   10360 O  OD2   . ASP   B  1 241  ? 9.036   19.591  117.498 1.00 36.47 ? 239  ASP   B OD2   1 
ATOM   10361 N  N     . TYR   B  1 242  ? 7.397   14.449  117.180 1.00 21.47 ? 240  TYR   B N     1 
ATOM   10362 C  CA    . TYR   B  1 242  ? 6.408   13.386  117.008 1.00 18.57 ? 240  TYR   B CA    1 
ATOM   10363 C  C     . TYR   B  1 242  ? 6.669   12.243  117.973 1.00 21.38 ? 240  TYR   B C     1 
ATOM   10364 O  O     . TYR   B  1 242  ? 5.747   11.737  118.622 1.00 19.84 ? 240  TYR   B O     1 
ATOM   10365 C  CB    . TYR   B  1 242  ? 6.437   12.847  115.584 1.00 18.26 ? 240  TYR   B CB    1 
ATOM   10366 C  CG    . TYR   B  1 242  ? 5.849   13.742  114.523 1.00 20.59 ? 240  TYR   B CG    1 
ATOM   10367 C  CD1   . TYR   B  1 242  ? 4.786   14.588  114.796 1.00 22.10 ? 240  TYR   B CD1   1 
ATOM   10368 C  CD2   . TYR   B  1 242  ? 6.344   13.711  113.231 1.00 18.66 ? 240  TYR   B CD2   1 
ATOM   10369 C  CE1   . TYR   B  1 242  ? 4.235   15.399  113.802 1.00 20.74 ? 240  TYR   B CE1   1 
ATOM   10370 C  CE2   . TYR   B  1 242  ? 5.808   14.508  112.237 1.00 21.67 ? 240  TYR   B CE2   1 
ATOM   10371 C  CZ    . TYR   B  1 242  ? 4.756   15.350  112.529 1.00 21.77 ? 240  TYR   B CZ    1 
ATOM   10372 O  OH    . TYR   B  1 242  ? 4.219   16.130  111.534 1.00 22.88 ? 240  TYR   B OH    1 
ATOM   10373 N  N     . GLU   B  1 243  ? 7.927   11.800  118.045 1.00 20.77 ? 241  GLU   B N     1 
ATOM   10374 C  CA    . GLU   B  1 243  ? 8.298   10.694  118.917 1.00 20.18 ? 241  GLU   B CA    1 
ATOM   10375 C  C     . GLU   B  1 243  ? 7.946   10.994  120.365 1.00 23.83 ? 241  GLU   B C     1 
ATOM   10376 O  O     . GLU   B  1 243  ? 7.358   10.155  121.065 1.00 20.59 ? 241  GLU   B O     1 
ATOM   10377 C  CB    . GLU   B  1 243  ? 9.791   10.417  118.774 1.00 24.15 ? 241  GLU   B CB    1 
ATOM   10378 C  CG    . GLU   B  1 243  ? 10.317  9.326   119.666 1.00 27.91 ? 241  GLU   B CG    1 
ATOM   10379 C  CD    . GLU   B  1 243  ? 11.829  9.244   119.593 1.00 30.48 ? 241  GLU   B CD    1 
ATOM   10380 O  OE1   . GLU   B  1 243  ? 12.472  10.313  119.545 1.00 29.31 ? 241  GLU   B OE1   1 
ATOM   10381 O  OE2   . GLU   B  1 243  ? 12.366  8.123   119.572 1.00 31.42 ? 241  GLU   B OE2   1 
ATOM   10382 N  N     . SER   B  1 244  ? 8.325   12.182  120.842 1.00 21.30 ? 242  SER   B N     1 
ATOM   10383 C  CA    A SER   B  1 244  ? 7.989   12.570  122.207 0.40 23.02 ? 242  SER   B CA    1 
ATOM   10384 C  CA    B SER   B  1 244  ? 7.988   12.564  122.208 0.24 23.03 ? 242  SER   B CA    1 
ATOM   10385 C  CA    C SER   B  1 244  ? 7.989   12.560  122.210 0.36 23.01 ? 242  SER   B CA    1 
ATOM   10386 C  C     . SER   B  1 244  ? 6.480   12.599  122.408 1.00 23.95 ? 242  SER   B C     1 
ATOM   10387 O  O     . SER   B  1 244  ? 5.971   12.136  123.435 1.00 21.87 ? 242  SER   B O     1 
ATOM   10388 C  CB    A SER   B  1 244  ? 8.608   13.934  122.523 0.40 23.57 ? 242  SER   B CB    1 
ATOM   10389 C  CB    B SER   B  1 244  ? 8.608   13.921  122.542 0.24 23.55 ? 242  SER   B CB    1 
ATOM   10390 C  CB    C SER   B  1 244  ? 8.617   13.912  122.557 0.36 23.58 ? 242  SER   B CB    1 
ATOM   10391 O  OG    A SER   B  1 244  ? 8.178   14.421  123.780 0.40 24.81 ? 242  SER   B OG    1 
ATOM   10392 O  OG    B SER   B  1 244  ? 10.017  13.871  122.422 0.24 24.37 ? 242  SER   B OG    1 
ATOM   10393 O  OG    C SER   B  1 244  ? 8.022   14.967  121.822 0.36 23.08 ? 242  SER   B OG    1 
ATOM   10394 N  N     . ALA   B  1 245  ? 5.747   13.134  121.432 1.00 19.43 ? 243  ALA   B N     1 
ATOM   10395 C  CA    . ALA   B  1 245  ? 4.296   13.189  121.569 1.00 22.55 ? 243  ALA   B CA    1 
ATOM   10396 C  C     . ALA   B  1 245  ? 3.694   11.788  121.631 1.00 20.39 ? 243  ALA   B C     1 
ATOM   10397 O  O     . ALA   B  1 245  ? 2.773   11.538  122.413 1.00 20.66 ? 243  ALA   B O     1 
ATOM   10398 C  CB    . ALA   B  1 245  ? 3.685   13.997  120.428 1.00 22.97 ? 243  ALA   B CB    1 
ATOM   10399 N  N     . ILE   B  1 246  ? 4.214   10.854  120.833 1.00 22.37 ? 244  ILE   B N     1 
ATOM   10400 C  CA    . ILE   B  1 246  ? 3.656   9.501   120.837 1.00 23.02 ? 244  ILE   B CA    1 
ATOM   10401 C  C     . ILE   B  1 246  ? 3.818   8.857   122.207 1.00 22.29 ? 244  ILE   B C     1 
ATOM   10402 O  O     . ILE   B  1 246  ? 2.902   8.188   122.708 1.00 24.44 ? 244  ILE   B O     1 
ATOM   10403 C  CB    . ILE   B  1 246  ? 4.292   8.644   119.727 1.00 20.83 ? 244  ILE   B CB    1 
ATOM   10404 C  CG1   . ILE   B  1 246  ? 3.801   9.111   118.361 1.00 20.84 ? 244  ILE   B CG1   1 
ATOM   10405 C  CG2   . ILE   B  1 246  ? 3.947   7.160   119.927 1.00 23.03 ? 244  ILE   B CG2   1 
ATOM   10406 C  CD1   . ILE   B  1 246  ? 4.527   8.456   117.190 1.00 21.96 ? 244  ILE   B CD1   1 
ATOM   10407 N  N     . HIS   B  1 247  ? 4.971   9.057   122.847 1.00 22.34 ? 245  HIS   B N     1 
ATOM   10408 C  CA    . HIS   B  1 247  ? 5.136   8.527   124.199 1.00 24.86 ? 245  HIS   B CA    1 
ATOM   10409 C  C     . HIS   B  1 247  ? 4.119   9.135   125.156 1.00 22.17 ? 245  HIS   B C     1 
ATOM   10410 O  O     . HIS   B  1 247  ? 3.495   8.415   125.942 1.00 24.10 ? 245  HIS   B O     1 
ATOM   10411 C  CB    . HIS   B  1 247  ? 6.566   8.761   124.695 1.00 23.85 ? 245  HIS   B CB    1 
ATOM   10412 C  CG    . HIS   B  1 247  ? 7.581   7.884   124.027 1.00 23.52 ? 245  HIS   B CG    1 
ATOM   10413 N  ND1   . HIS   B  1 247  ? 7.580   6.510   124.154 1.00 27.23 ? 245  HIS   B ND1   1 
ATOM   10414 C  CD2   . HIS   B  1 247  ? 8.626   8.187   123.220 1.00 25.66 ? 245  HIS   B CD2   1 
ATOM   10415 C  CE1   . HIS   B  1 247  ? 8.582   6.006   123.455 1.00 28.37 ? 245  HIS   B CE1   1 
ATOM   10416 N  NE2   . HIS   B  1 247  ? 9.231   7.001   122.880 1.00 27.27 ? 245  HIS   B NE2   1 
ATOM   10417 N  N     . ALA   B  1 248  ? 3.911   10.450  125.082 1.00 21.34 ? 246  ALA   B N     1 
ATOM   10418 C  CA    . ALA   B  1 248  ? 2.962   11.095  125.986 1.00 22.65 ? 246  ALA   B CA    1 
ATOM   10419 C  C     . ALA   B  1 248  ? 1.540   10.648  125.687 1.00 21.92 ? 246  ALA   B C     1 
ATOM   10420 O  O     . ALA   B  1 248  ? 0.777   10.314  126.601 1.00 23.94 ? 246  ALA   B O     1 
ATOM   10421 C  CB    . ALA   B  1 248  ? 3.071   12.620  125.874 1.00 24.90 ? 246  ALA   B CB    1 
ATOM   10422 N  N     . ILE   B  1 249  ? 1.163   10.665  124.407 1.00 24.58 ? 247  ILE   B N     1 
ATOM   10423 C  CA    . ILE   B  1 249  ? -0.184  10.264  124.022 1.00 24.13 ? 247  ILE   B CA    1 
ATOM   10424 C  C     . ILE   B  1 249  ? -0.400  8.799   124.347 1.00 23.89 ? 247  ILE   B C     1 
ATOM   10425 O  O     . ILE   B  1 249  ? -1.450  8.409   124.870 1.00 25.62 ? 247  ILE   B O     1 
ATOM   10426 C  CB    . ILE   B  1 249  ? -0.420  10.554  122.529 1.00 24.15 ? 247  ILE   B CB    1 
ATOM   10427 C  CG1   . ILE   B  1 249  ? -0.245  12.047  122.240 1.00 22.73 ? 247  ILE   B CG1   1 
ATOM   10428 C  CG2   . ILE   B  1 249  ? -1.804  10.033  122.102 1.00 23.41 ? 247  ILE   B CG2   1 
ATOM   10429 C  CD1   . ILE   B  1 249  ? 0.033   12.355  120.777 1.00 20.31 ? 247  ILE   B CD1   1 
ATOM   10430 N  N     . GLY   B  1 250  ? 0.601   7.966   124.060 1.00 24.67 ? 248  GLY   B N     1 
ATOM   10431 C  CA    . GLY   B  1 250  ? 0.465   6.545   124.323 1.00 26.95 ? 248  GLY   B CA    1 
ATOM   10432 C  C     . GLY   B  1 250  ? 0.236   6.250   125.790 1.00 29.25 ? 248  GLY   B C     1 
ATOM   10433 O  O     . GLY   B  1 250  ? -0.663  5.484   126.154 1.00 28.32 ? 248  GLY   B O     1 
ATOM   10434 N  N     . LYS   B  1 251  ? 1.041   6.865   126.658 1.00 25.92 ? 249  LYS   B N     1 
ATOM   10435 C  CA    . LYS   B  1 251  ? 0.862   6.641   128.085 1.00 26.37 ? 249  LYS   B CA    1 
ATOM   10436 C  C     . LYS   B  1 251  ? -0.480  7.186   128.549 1.00 24.16 ? 249  LYS   B C     1 
ATOM   10437 O  O     . LYS   B  1 251  ? -1.164  6.558   129.362 1.00 28.11 ? 249  LYS   B O     1 
ATOM   10438 C  CB    . LYS   B  1 251  ? 2.011   7.279   128.873 1.00 28.56 ? 249  LYS   B CB    1 
ATOM   10439 N  N     . ALA   B  1 252  ? -0.884  8.345   128.026 1.00 25.18 ? 250  ALA   B N     1 
ATOM   10440 C  CA    . ALA   B  1 252  ? -2.187  8.894   128.387 1.00 27.61 ? 250  ALA   B CA    1 
ATOM   10441 C  C     . ALA   B  1 252  ? -3.321  8.006   127.887 1.00 30.72 ? 250  ALA   B C     1 
ATOM   10442 O  O     . ALA   B  1 252  ? -4.331  7.835   128.578 1.00 30.89 ? 250  ALA   B O     1 
ATOM   10443 C  CB    . ALA   B  1 252  ? -2.340  10.308  127.831 1.00 30.51 ? 250  ALA   B CB    1 
ATOM   10444 N  N     . SER   B  1 253  ? -3.180  7.451   126.679 1.00 30.46 ? 251  SER   B N     1 
ATOM   10445 C  CA    . SER   B  1 253  ? -4.198  6.541   126.163 1.00 30.80 ? 251  SER   B CA    1 
ATOM   10446 C  C     . SER   B  1 253  ? -4.461  5.401   127.137 1.00 31.09 ? 251  SER   B C     1 
ATOM   10447 O  O     . SER   B  1 253  ? -5.612  4.993   127.330 1.00 34.82 ? 251  SER   B O     1 
ATOM   10448 C  CB    . SER   B  1 253  ? -3.776  5.984   124.807 1.00 30.22 ? 251  SER   B CB    1 
ATOM   10449 O  OG    . SER   B  1 253  ? -4.731  5.034   124.360 1.00 30.88 ? 251  SER   B OG    1 
ATOM   10450 N  N     . ALA   B  1 254  ? -3.402  4.870   127.750 1.00 31.00 ? 252  ALA   B N     1 
ATOM   10451 C  CA    . ALA   B  1 254  ? -3.515  3.864   128.807 1.00 33.84 ? 252  ALA   B CA    1 
ATOM   10452 C  C     . ALA   B  1 254  ? -4.340  2.665   128.350 1.00 35.51 ? 252  ALA   B C     1 
ATOM   10453 O  O     . ALA   B  1 254  ? -5.153  2.120   129.100 1.00 33.92 ? 252  ALA   B O     1 
ATOM   10454 C  CB    . ALA   B  1 254  ? -4.098  4.472   130.081 1.00 33.41 ? 252  ALA   B CB    1 
ATOM   10455 N  N     . GLY   B  1 255  ? -4.141  2.265   127.096 1.00 35.46 ? 253  GLY   B N     1 
ATOM   10456 C  CA    . GLY   B  1 255  ? -4.768  1.067   126.578 1.00 37.86 ? 253  GLY   B CA    1 
ATOM   10457 C  C     . GLY   B  1 255  ? -6.198  1.225   126.121 1.00 36.84 ? 253  GLY   B C     1 
ATOM   10458 O  O     . GLY   B  1 255  ? -6.866  0.212   125.880 1.00 36.87 ? 253  GLY   B O     1 
ATOM   10459 N  N     . ARG   B  1 256  ? -6.691  2.456   125.987 1.00 29.60 ? 254  ARG   B N     1 
ATOM   10460 C  CA    . ARG   B  1 256  ? -8.056  2.668   125.525 1.00 33.60 ? 254  ARG   B CA    1 
ATOM   10461 C  C     . ARG   B  1 256  ? -8.248  2.286   124.066 1.00 38.11 ? 254  ARG   B C     1 
ATOM   10462 O  O     . ARG   B  1 256  ? -9.392  2.282   123.591 1.00 34.64 ? 254  ARG   B O     1 
ATOM   10463 C  CB    . ARG   B  1 256  ? -8.463  4.128   125.734 1.00 35.80 ? 254  ARG   B CB    1 
ATOM   10464 C  CG    . ARG   B  1 256  ? -8.879  4.463   127.159 1.00 37.39 ? 254  ARG   B CG    1 
ATOM   10465 C  CD    . ARG   B  1 256  ? -9.263  5.928   127.271 1.00 34.90 ? 254  ARG   B CD    1 
ATOM   10466 N  NE    . ARG   B  1 256  ? -8.090  6.793   127.327 1.00 37.63 ? 254  ARG   B NE    1 
ATOM   10467 C  CZ    . ARG   B  1 256  ? -8.104  8.092   127.059 1.00 37.85 ? 254  ARG   B CZ    1 
ATOM   10468 N  NH1   . ARG   B  1 256  ? -9.213  8.709   126.687 1.00 34.03 ? 254  ARG   B NH1   1 
ATOM   10469 N  NH2   . ARG   B  1 256  ? -6.974  8.787   127.157 1.00 39.65 ? 254  ARG   B NH2   1 
ATOM   10470 N  N     . GLY   B  1 257  ? -7.166  1.980   123.347 1.00 36.27 ? 255  GLY   B N     1 
ATOM   10471 C  CA    . GLY   B  1 257  ? -7.260  1.558   121.967 1.00 31.67 ? 255  GLY   B CA    1 
ATOM   10472 C  C     . GLY   B  1 257  ? -7.435  2.718   121.006 1.00 33.73 ? 255  GLY   B C     1 
ATOM   10473 O  O     . GLY   B  1 257  ? -7.535  3.887   121.380 1.00 31.64 ? 255  GLY   B O     1 
ATOM   10474 N  N     . ILE   B  1 258  ? -7.515  2.366   119.722 1.00 30.72 ? 256  ILE   B N     1 
ATOM   10475 C  CA    . ILE   B  1 258  ? -7.399  3.380   118.676 1.00 33.83 ? 256  ILE   B CA    1 
ATOM   10476 C  C     . ILE   B  1 258  ? -8.682  4.147   118.415 1.00 30.57 ? 256  ILE   B C     1 
ATOM   10477 O  O     . ILE   B  1 258  ? -8.632  5.181   117.742 1.00 29.03 ? 256  ILE   B O     1 
ATOM   10478 C  CB    . ILE   B  1 258  ? -6.909  2.744   117.364 1.00 33.65 ? 256  ILE   B CB    1 
ATOM   10479 C  CG1   . ILE   B  1 258  ? -7.865  1.646   116.914 1.00 34.92 ? 256  ILE   B CG1   1 
ATOM   10480 C  CG2   . ILE   B  1 258  ? -5.514  2.160   117.535 1.00 31.22 ? 256  ILE   B CG2   1 
ATOM   10481 C  CD1   . ILE   B  1 258  ? -7.450  1.013   115.608 1.00 32.13 ? 256  ILE   B CD1   1 
ATOM   10482 N  N     . TYR   B  1 259  ? -9.829  3.686   118.923 1.00 31.45 ? 257  TYR   B N     1 
ATOM   10483 C  CA    . TYR   B  1 259  ? -11.096 4.383   118.712 1.00 29.36 ? 257  TYR   B CA    1 
ATOM   10484 C  C     . TYR   B  1 259  ? -11.475 5.280   119.886 1.00 31.31 ? 257  TYR   B C     1 
ATOM   10485 O  O     . TYR   B  1 259  ? -11.736 6.472   119.692 1.00 34.57 ? 257  TYR   B O     1 
ATOM   10486 C  CB    . TYR   B  1 259  ? -12.219 3.369   118.408 1.00 30.90 ? 257  TYR   B CB    1 
ATOM   10487 C  CG    . TYR   B  1 259  ? -11.829 2.403   117.310 1.00 31.83 ? 257  TYR   B CG    1 
ATOM   10488 C  CD1   . TYR   B  1 259  ? -11.655 2.846   116.006 1.00 35.25 ? 257  TYR   B CD1   1 
ATOM   10489 C  CD2   . TYR   B  1 259  ? -11.598 1.059   117.579 1.00 33.65 ? 257  TYR   B CD2   1 
ATOM   10490 C  CE1   . TYR   B  1 259  ? -11.275 1.983   114.996 1.00 36.22 ? 257  TYR   B CE1   1 
ATOM   10491 C  CE2   . TYR   B  1 259  ? -11.216 0.184   116.569 1.00 33.89 ? 257  TYR   B CE2   1 
ATOM   10492 C  CZ    . TYR   B  1 259  ? -11.057 0.656   115.283 1.00 36.13 ? 257  TYR   B CZ    1 
ATOM   10493 O  OH    . TYR   B  1 259  ? -10.668 -0.192  114.275 1.00 33.72 ? 257  TYR   B OH    1 
ATOM   10494 N  N     . GLU   B  1 260  ? -11.511 4.737   121.107 1.00 29.73 ? 258  GLU   B N     1 
ATOM   10495 C  CA    . GLU   B  1 260  ? -11.784 5.573   122.272 1.00 34.29 ? 258  GLU   B CA    1 
ATOM   10496 C  C     . GLU   B  1 260  ? -10.589 6.461   122.607 1.00 37.61 ? 258  GLU   B C     1 
ATOM   10497 O  O     . GLU   B  1 260  ? -10.755 7.643   122.935 1.00 41.26 ? 258  GLU   B O     1 
ATOM   10498 C  CB    . GLU   B  1 260  ? -12.155 4.698   123.474 1.00 34.75 ? 258  GLU   B CB    1 
ATOM   10499 N  N     . GLY   B  1 261  ? -9.384  5.924   122.501 1.00 34.27 ? 259  GLY   B N     1 
ATOM   10500 C  CA    . GLY   B  1 261  ? -8.204  6.641   122.933 1.00 30.08 ? 259  GLY   B CA    1 
ATOM   10501 C  C     . GLY   B  1 261  ? -7.680  7.594   121.882 1.00 30.59 ? 259  GLY   B C     1 
ATOM   10502 O  O     . GLY   B  1 261  ? -8.035  7.540   120.689 1.00 27.17 ? 259  GLY   B O     1 
ATOM   10503 N  N     . PRO   B  1 262  ? -6.788  8.479   122.319 1.00 28.13 ? 260  PRO   B N     1 
ATOM   10504 C  CA    . PRO   B  1 262  ? -6.260  9.513   121.426 1.00 25.09 ? 260  PRO   B CA    1 
ATOM   10505 C  C     . PRO   B  1 262  ? -5.269  8.952   120.422 1.00 25.64 ? 260  PRO   B C     1 
ATOM   10506 O  O     . PRO   B  1 262  ? -4.709  7.867   120.588 1.00 29.95 ? 260  PRO   B O     1 
ATOM   10507 C  CB    . PRO   B  1 262  ? -5.571  10.480  122.390 1.00 25.30 ? 260  PRO   B CB    1 
ATOM   10508 C  CG    . PRO   B  1 262  ? -5.114  9.576   123.518 1.00 25.10 ? 260  PRO   B CG    1 
ATOM   10509 C  CD    . PRO   B  1 262  ? -6.224  8.572   123.677 1.00 27.65 ? 260  PRO   B CD    1 
ATOM   10510 N  N     . GLY   B  1 263  ? -5.040  9.737   119.371 1.00 23.99 ? 261  GLY   B N     1 
ATOM   10511 C  CA    . GLY   B  1 263  ? -4.039  9.406   118.381 1.00 23.10 ? 261  GLY   B CA    1 
ATOM   10512 C  C     . GLY   B  1 263  ? -3.162  10.589  118.024 1.00 23.26 ? 261  GLY   B C     1 
ATOM   10513 O  O     . GLY   B  1 263  ? -3.238  11.653  118.645 1.00 25.32 ? 261  GLY   B O     1 
ATOM   10514 N  N     . ILE   B  1 264  ? -2.328  10.412  117.014 1.00 21.29 ? 262  ILE   B N     1 
ATOM   10515 C  CA    . ILE   B  1 264  ? -1.450  11.468  116.541 1.00 22.34 ? 262  ILE   B CA    1 
ATOM   10516 C  C     . ILE   B  1 264  ? -1.608  11.590  115.034 1.00 24.34 ? 262  ILE   B C     1 
ATOM   10517 O  O     . ILE   B  1 264  ? -1.974  10.628  114.345 1.00 22.92 ? 262  ILE   B O     1 
ATOM   10518 C  CB    . ILE   B  1 264  ? 0.020   11.195  116.942 1.00 25.56 ? 262  ILE   B CB    1 
ATOM   10519 C  CG1   . ILE   B  1 264  ? 0.881   12.450  116.731 1.00 22.83 ? 262  ILE   B CG1   1 
ATOM   10520 C  CG2   . ILE   B  1 264  ? 0.562   9.975   116.194 1.00 23.92 ? 262  ILE   B CG2   1 
ATOM   10521 C  CD1   . ILE   B  1 264  ? 2.337   12.327  117.251 1.00 22.64 ? 262  ILE   B CD1   1 
ATOM   10522 N  N     . SER   B  1 265  ? -1.367  12.798  114.529 1.00 20.43 ? 263  SER   B N     1 
ATOM   10523 C  CA    . SER   B  1 265  ? -1.389  13.100  113.109 1.00 21.13 ? 263  SER   B CA    1 
ATOM   10524 C  C     . SER   B  1 265  ? -0.030  13.665  112.737 1.00 20.58 ? 263  SER   B C     1 
ATOM   10525 O  O     . SER   B  1 265  ? 0.508   14.508  113.460 1.00 21.31 ? 263  SER   B O     1 
ATOM   10526 C  CB    . SER   B  1 265  ? -2.494  14.099  112.765 1.00 23.45 ? 263  SER   B CB    1 
ATOM   10527 O  OG    . SER   B  1 265  ? -3.762  13.470  112.784 1.00 24.12 ? 263  SER   B OG    1 
ATOM   10528 N  N     . ILE   B  1 266  ? 0.529   13.189  111.628 1.00 19.70 ? 264  ILE   B N     1 
ATOM   10529 C  CA    . ILE   B  1 266  ? 1.835   13.640  111.170 1.00 19.51 ? 264  ILE   B CA    1 
ATOM   10530 C  C     . ILE   B  1 266  ? 1.713   14.082  109.723 1.00 22.64 ? 264  ILE   B C     1 
ATOM   10531 O  O     . ILE   B  1 266  ? 0.809   13.674  108.993 1.00 20.70 ? 264  ILE   B O     1 
ATOM   10532 C  CB    . ILE   B  1 266  ? 2.923   12.548  111.291 1.00 17.71 ? 264  ILE   B CB    1 
ATOM   10533 C  CG1   . ILE   B  1 266  ? 2.620   11.389  110.336 1.00 22.41 ? 264  ILE   B CG1   1 
ATOM   10534 C  CG2   . ILE   B  1 266  ? 3.082   12.071  112.750 1.00 21.14 ? 264  ILE   B CG2   1 
ATOM   10535 C  CD1   . ILE   B  1 266  ? 3.718   10.329  110.292 1.00 26.82 ? 264  ILE   B CD1   1 
ATOM   10536 N  N     . LYS   B  1 267  ? 2.637   14.937  109.312 1.00 20.65 ? 265  LYS   B N     1 
ATOM   10537 C  CA    . LYS   B  1 267  ? 2.779   15.316  107.917 1.00 20.29 ? 265  LYS   B CA    1 
ATOM   10538 C  C     . LYS   B  1 267  ? 4.105   14.770  107.410 1.00 19.88 ? 265  LYS   B C     1 
ATOM   10539 O  O     . LYS   B  1 267  ? 5.139   14.973  108.048 1.00 20.75 ? 265  LYS   B O     1 
ATOM   10540 C  CB    . LYS   B  1 267  ? 2.722   16.836  107.747 1.00 21.66 ? 265  LYS   B CB    1 
ATOM   10541 C  CG    . LYS   B  1 267  ? 1.344   17.415  108.004 1.00 24.05 ? 265  LYS   B CG    1 
ATOM   10542 C  CD    . LYS   B  1 267  ? 1.258   18.877  107.616 1.00 32.95 ? 265  LYS   B CD    1 
ATOM   10543 C  CE    . LYS   B  1 267  ? -0.077  19.473  108.051 1.00 37.65 ? 265  LYS   B CE    1 
ATOM   10544 N  NZ    . LYS   B  1 267  ? -0.392  19.109  109.457 1.00 35.14 ? 265  LYS   B NZ    1 
ATOM   10545 N  N     . LEU   B  1 268  ? 4.069   14.069  106.276 1.00 20.35 ? 266  LEU   B N     1 
ATOM   10546 C  CA    . LEU   B  1 268  ? 5.303   13.523  105.724 1.00 20.12 ? 266  LEU   B CA    1 
ATOM   10547 C  C     . LEU   B  1 268  ? 6.292   14.627  105.356 1.00 19.17 ? 266  LEU   B C     1 
ATOM   10548 O  O     . LEU   B  1 268  ? 7.508   14.431  105.472 1.00 19.12 ? 266  LEU   B O     1 
ATOM   10549 C  CB    . LEU   B  1 268  ? 4.988   12.645  104.510 1.00 15.72 ? 266  LEU   B CB    1 
ATOM   10550 C  CG    . LEU   B  1 268  ? 4.135   11.412  104.831 1.00 20.04 ? 266  LEU   B CG    1 
ATOM   10551 C  CD1   . LEU   B  1 268  ? 3.959   10.559  103.596 1.00 20.53 ? 266  LEU   B CD1   1 
ATOM   10552 C  CD2   . LEU   B  1 268  ? 4.791   10.606  105.937 1.00 22.00 ? 266  LEU   B CD2   1 
ATOM   10553 N  N     . SER   B  1 269  ? 5.797   15.795  104.925 1.00 18.87 ? 267  SER   B N     1 
ATOM   10554 C  CA    . SER   B  1 269  ? 6.701   16.891  104.587 1.00 18.27 ? 267  SER   B CA    1 
ATOM   10555 C  C     . SER   B  1 269  ? 7.472   17.396  105.801 1.00 16.68 ? 267  SER   B C     1 
ATOM   10556 O  O     . SER   B  1 269  ? 8.491   18.073  105.637 1.00 21.54 ? 267  SER   B O     1 
ATOM   10557 C  CB    . SER   B  1 269  ? 5.925   18.049  103.954 1.00 19.14 ? 267  SER   B CB    1 
ATOM   10558 O  OG    . SER   B  1 269  ? 5.149   18.730  104.930 1.00 17.93 ? 267  SER   B OG    1 
ATOM   10559 N  N     . ALA   B  1 270  ? 7.010   17.088  107.009 1.00 16.11 ? 268  ALA   B N     1 
ATOM   10560 C  CA    . ALA   B  1 270  ? 7.752   17.449  108.209 1.00 19.25 ? 268  ALA   B CA    1 
ATOM   10561 C  C     . ALA   B  1 270  ? 8.965   16.565  108.410 1.00 18.41 ? 268  ALA   B C     1 
ATOM   10562 O  O     . ALA   B  1 270  ? 9.894   16.961  109.118 1.00 18.48 ? 268  ALA   B O     1 
ATOM   10563 C  CB    . ALA   B  1 270  ? 6.863   17.341  109.455 1.00 20.47 ? 268  ALA   B CB    1 
ATOM   10564 N  N     . LEU   B  1 271  ? 8.974   15.385  107.803 1.00 16.85 ? 269  LEU   B N     1 
ATOM   10565 C  CA    . LEU   B  1 271  ? 9.936   14.356  108.170 1.00 18.52 ? 269  LEU   B CA    1 
ATOM   10566 C  C     . LEU   B  1 271  ? 11.097  14.270  107.199 1.00 19.87 ? 269  LEU   B C     1 
ATOM   10567 O  O     . LEU   B  1 271  ? 12.011  13.471  107.417 1.00 20.85 ? 269  LEU   B O     1 
ATOM   10568 C  CB    . LEU   B  1 271  ? 9.238   13.001  108.267 1.00 18.12 ? 269  LEU   B CB    1 
ATOM   10569 C  CG    . LEU   B  1 271  ? 8.237   12.966  109.420 1.00 20.93 ? 269  LEU   B CG    1 
ATOM   10570 C  CD1   . LEU   B  1 271  ? 7.457   11.655  109.401 1.00 25.02 ? 269  LEU   B CD1   1 
ATOM   10571 C  CD2   . LEU   B  1 271  ? 8.929   13.192  110.765 1.00 20.99 ? 269  LEU   B CD2   1 
ATOM   10572 N  N     . HIS   B  1 272  ? 11.088  15.081  106.147 1.00 17.71 ? 270  HIS   B N     1 
ATOM   10573 C  CA    . HIS   B  1 272  ? 12.200  15.082  105.223 1.00 19.06 ? 270  HIS   B CA    1 
ATOM   10574 C  C     . HIS   B  1 272  ? 12.193  16.406  104.487 1.00 19.59 ? 270  HIS   B C     1 
ATOM   10575 O  O     . HIS   B  1 272  ? 11.115  16.875  104.093 1.00 19.43 ? 270  HIS   B O     1 
ATOM   10576 C  CB    . HIS   B  1 272  ? 12.094  13.920  104.236 1.00 20.34 ? 270  HIS   B CB    1 
ATOM   10577 C  CG    . HIS   B  1 272  ? 13.391  13.581  103.590 1.00 24.32 ? 270  HIS   B CG    1 
ATOM   10578 N  ND1   . HIS   B  1 272  ? 13.930  14.338  102.574 1.00 21.65 ? 270  HIS   B ND1   1 
ATOM   10579 C  CD2   . HIS   B  1 272  ? 14.275  12.586  103.835 1.00 22.70 ? 270  HIS   B CD2   1 
ATOM   10580 C  CE1   . HIS   B  1 272  ? 15.087  13.814  102.209 1.00 25.01 ? 270  HIS   B CE1   1 
ATOM   10581 N  NE2   . HIS   B  1 272  ? 15.319  12.750  102.959 1.00 26.79 ? 270  HIS   B NE2   1 
ATOM   10582 N  N     . PRO   B  1 273  ? 13.348  17.042  104.293 1.00 19.16 ? 271  PRO   B N     1 
ATOM   10583 C  CA    . PRO   B  1 273  ? 13.352  18.317  103.565 1.00 19.62 ? 271  PRO   B CA    1 
ATOM   10584 C  C     . PRO   B  1 273  ? 13.112  18.164  102.076 1.00 18.55 ? 271  PRO   B C     1 
ATOM   10585 O  O     . PRO   B  1 273  ? 12.788  19.164  101.430 1.00 19.49 ? 271  PRO   B O     1 
ATOM   10586 C  CB    . PRO   B  1 273  ? 14.748  18.895  103.853 1.00 19.60 ? 271  PRO   B CB    1 
ATOM   10587 C  CG    . PRO   B  1 273  ? 15.593  17.695  104.195 1.00 22.57 ? 271  PRO   B CG    1 
ATOM   10588 C  CD    . PRO   B  1 273  ? 14.672  16.685  104.835 1.00 22.33 ? 271  PRO   B CD    1 
ATOM   10589 N  N     . ARG   B  1 274  ? 13.257  16.962  101.506 1.00 18.87 ? 272  ARG   B N     1 
ATOM   10590 C  CA    . ARG   B  1 274  ? 13.035  16.787  100.071 1.00 16.38 ? 272  ARG   B CA    1 
ATOM   10591 C  C     . ARG   B  1 274  ? 11.923  15.780  99.817  1.00 21.64 ? 272  ARG   B C     1 
ATOM   10592 O  O     . ARG   B  1 274  ? 12.139  14.755  99.160  1.00 21.25 ? 272  ARG   B O     1 
ATOM   10593 C  CB    . ARG   B  1 274  ? 14.316  16.330  99.357  1.00 18.65 ? 272  ARG   B CB    1 
ATOM   10594 C  CG    . ARG   B  1 274  ? 15.465  17.336  99.425  1.00 21.58 ? 272  ARG   B CG    1 
ATOM   10595 C  CD    . ARG   B  1 274  ? 15.055  18.708  98.875  1.00 20.52 ? 272  ARG   B CD    1 
ATOM   10596 N  NE    . ARG   B  1 274  ? 14.549  18.645  97.510  1.00 20.00 ? 272  ARG   B NE    1 
ATOM   10597 C  CZ    . ARG   B  1 274  ? 15.297  18.524  96.420  1.00 21.76 ? 272  ARG   B CZ    1 
ATOM   10598 N  NH1   . ARG   B  1 274  ? 16.615  18.372  96.489  1.00 20.64 ? 272  ARG   B NH1   1 
ATOM   10599 N  NH2   . ARG   B  1 274  ? 14.709  18.553  95.228  1.00 18.27 ? 272  ARG   B NH2   1 
ATOM   10600 N  N     . TYR   B  1 275  ? 10.729  16.057  100.327 1.00 18.11 ? 273  TYR   B N     1 
ATOM   10601 C  CA    . TYR   B  1 275  ? 9.610   15.136  100.167 1.00 21.10 ? 273  TYR   B CA    1 
ATOM   10602 C  C     . TYR   B  1 275  ? 8.913   15.462  98.849  1.00 19.18 ? 273  TYR   B C     1 
ATOM   10603 O  O     . TYR   B  1 275  ? 8.082   16.366  98.785  1.00 18.63 ? 273  TYR   B O     1 
ATOM   10604 C  CB    . TYR   B  1 275  ? 8.675   15.245  101.364 1.00 17.80 ? 273  TYR   B CB    1 
ATOM   10605 C  CG    . TYR   B  1 275  ? 7.421   14.439  101.194 1.00 20.27 ? 273  TYR   B CG    1 
ATOM   10606 C  CD1   . TYR   B  1 275  ? 7.476   13.111  100.791 1.00 19.87 ? 273  TYR   B CD1   1 
ATOM   10607 C  CD2   . TYR   B  1 275  ? 6.188   15.006  101.433 1.00 20.32 ? 273  TYR   B CD2   1 
ATOM   10608 C  CE1   . TYR   B  1 275  ? 6.323   12.371  100.631 1.00 21.01 ? 273  TYR   B CE1   1 
ATOM   10609 C  CE2   . TYR   B  1 275  ? 5.026   14.279  101.281 1.00 22.50 ? 273  TYR   B CE2   1 
ATOM   10610 C  CZ    . TYR   B  1 275  ? 5.099   12.966  100.866 1.00 22.14 ? 273  TYR   B CZ    1 
ATOM   10611 O  OH    . TYR   B  1 275  ? 3.953   12.244  100.720 1.00 19.51 ? 273  TYR   B OH    1 
ATOM   10612 N  N     . SER   B  1 276  ? 9.269   14.734  97.787  1.00 17.98 ? 274  SER   B N     1 
ATOM   10613 C  CA    . SER   B  1 276  ? 8.687   14.963  96.467  1.00 21.25 ? 274  SER   B CA    1 
ATOM   10614 C  C     . SER   B  1 276  ? 8.954   13.754  95.591  1.00 21.01 ? 274  SER   B C     1 
ATOM   10615 O  O     . SER   B  1 276  ? 9.889   12.985  95.831  1.00 18.79 ? 274  SER   B O     1 
ATOM   10616 C  CB    . SER   B  1 276  ? 9.276   16.200  95.786  1.00 23.55 ? 274  SER   B CB    1 
ATOM   10617 O  OG    . SER   B  1 276  ? 10.640  15.946  95.490  1.00 21.82 ? 274  SER   B OG    1 
ATOM   10618 N  N     . ARG   B  1 277  ? 8.138   13.626  94.542  1.00 17.83 ? 275  ARG   B N     1 
ATOM   10619 C  CA    . ARG   B  1 277  ? 8.302   12.530  93.595  1.00 17.67 ? 275  ARG   B CA    1 
ATOM   10620 C  C     . ARG   B  1 277  ? 9.684   12.561  92.960  1.00 20.00 ? 275  ARG   B C     1 
ATOM   10621 O  O     . ARG   B  1 277  ? 10.291  11.508  92.731  1.00 18.86 ? 275  ARG   B O     1 
ATOM   10622 C  CB    . ARG   B  1 277  ? 7.215   12.595  92.518  1.00 16.83 ? 275  ARG   B CB    1 
ATOM   10623 C  CG    . ARG   B  1 277  ? 7.406   11.607  91.363  1.00 19.75 ? 275  ARG   B CG    1 
ATOM   10624 C  CD    . ARG   B  1 277  ? 7.490   10.167  91.867  1.00 20.19 ? 275  ARG   B CD    1 
ATOM   10625 N  NE    . ARG   B  1 277  ? 7.645   9.220   90.769  1.00 20.43 ? 275  ARG   B NE    1 
ATOM   10626 C  CZ    . ARG   B  1 277  ? 8.810   8.870   90.244  1.00 19.88 ? 275  ARG   B CZ    1 
ATOM   10627 N  NH1   . ARG   B  1 277  ? 9.950   9.387   90.683  1.00 20.49 ? 275  ARG   B NH1   1 
ATOM   10628 N  NH2   . ARG   B  1 277  ? 8.836   7.975   89.258  1.00 18.75 ? 275  ARG   B NH2   1 
ATOM   10629 N  N     . ALA   B  1 278  ? 10.204  13.759  92.670  1.00 20.11 ? 276  ALA   B N     1 
ATOM   10630 C  CA    . ALA   B  1 278  ? 11.530  13.831  92.057  1.00 21.59 ? 276  ALA   B CA    1 
ATOM   10631 C  C     . ALA   B  1 278  ? 12.594  13.229  92.965  1.00 21.14 ? 276  ALA   B C     1 
ATOM   10632 O  O     . ALA   B  1 278  ? 13.611  12.726  92.480  1.00 20.99 ? 276  ALA   B O     1 
ATOM   10633 C  CB    . ALA   B  1 278  ? 11.884  15.276  91.702  1.00 21.84 ? 276  ALA   B CB    1 
ATOM   10634 N  N     . GLN   B  1 279  ? 12.384  13.264  94.274  1.00 18.62 ? 277  GLN   B N     1 
ATOM   10635 C  CA    . GLN   B  1 279  ? 13.339  12.711  95.231  1.00 18.58 ? 277  GLN   B CA    1 
ATOM   10636 C  C     . GLN   B  1 279  ? 12.832  11.400  95.833  1.00 19.67 ? 277  GLN   B C     1 
ATOM   10637 O  O     . GLN   B  1 279  ? 13.140  11.069  96.981  1.00 19.91 ? 277  GLN   B O     1 
ATOM   10638 C  CB    . GLN   B  1 279  ? 13.645  13.735  96.323  1.00 20.47 ? 277  GLN   B CB    1 
ATOM   10639 C  CG    . GLN   B  1 279  ? 14.279  15.008  95.801  1.00 19.99 ? 277  GLN   B CG    1 
ATOM   10640 C  CD    . GLN   B  1 279  ? 15.629  14.753  95.159  1.00 23.08 ? 277  GLN   B CD    1 
ATOM   10641 O  OE1   . GLN   B  1 279  ? 16.410  13.934  95.643  1.00 27.33 ? 277  GLN   B OE1   1 
ATOM   10642 N  NE2   . GLN   B  1 279  ? 15.907  15.442  94.056  1.00 20.21 ? 277  GLN   B NE2   1 
ATOM   10643 N  N     . ALA   B  1 280  ? 12.082  10.634  95.045  1.00 19.38 ? 278  ALA   B N     1 
ATOM   10644 C  CA    . ALA   B  1 280  ? 11.405  9.446   95.557  1.00 22.13 ? 278  ALA   B CA    1 
ATOM   10645 C  C     . ALA   B  1 280  ? 12.379  8.470   96.208  1.00 22.11 ? 278  ALA   B C     1 
ATOM   10646 O  O     . ALA   B  1 280  ? 12.049  7.840   97.218  1.00 19.68 ? 278  ALA   B O     1 
ATOM   10647 C  CB    . ALA   B  1 280  ? 10.631  8.763   94.425  1.00 18.23 ? 278  ALA   B CB    1 
ATOM   10648 N  N     . ALA   B  1 281  ? 13.588  8.335   95.654  1.00 23.48 ? 279  ALA   B N     1 
ATOM   10649 C  CA    . ALA   B  1 281  ? 14.542  7.389   96.229  1.00 25.37 ? 279  ALA   B CA    1 
ATOM   10650 C  C     . ALA   B  1 281  ? 14.951  7.810   97.637  1.00 21.06 ? 279  ALA   B C     1 
ATOM   10651 O  O     . ALA   B  1 281  ? 14.997  6.984   98.556  1.00 22.12 ? 279  ALA   B O     1 
ATOM   10652 C  CB    . ALA   B  1 281  ? 15.766  7.252   95.322  1.00 24.45 ? 279  ALA   B CB    1 
ATOM   10653 N  N     . ARG   B  1 282  ? 15.250  9.093   97.827  1.00 19.22 ? 280  ARG   B N     1 
ATOM   10654 C  CA    . ARG   B  1 282  ? 15.541  9.580   99.169  1.00 22.99 ? 280  ARG   B CA    1 
ATOM   10655 C  C     . ARG   B  1 282  ? 14.331  9.444   100.081 1.00 21.18 ? 280  ARG   B C     1 
ATOM   10656 O  O     . ARG   B  1 282  ? 14.473  9.182   101.281 1.00 23.17 ? 280  ARG   B O     1 
ATOM   10657 C  CB    . ARG   B  1 282  ? 15.994  11.034  99.109  1.00 25.50 ? 280  ARG   B CB    1 
ATOM   10658 C  CG    . ARG   B  1 282  ? 17.289  11.240  98.351  1.00 24.62 ? 280  ARG   B CG    1 
ATOM   10659 C  CD    . ARG   B  1 282  ? 17.826  12.633  98.625  1.00 24.70 ? 280  ARG   B CD    1 
ATOM   10660 N  NE    . ARG   B  1 282  ? 18.107  12.813  100.045 1.00 26.34 ? 280  ARG   B NE    1 
ATOM   10661 C  CZ    . ARG   B  1 282  ? 18.274  13.989  100.633 1.00 25.38 ? 280  ARG   B CZ    1 
ATOM   10662 N  NH1   . ARG   B  1 282  ? 18.198  15.122  99.948  1.00 24.27 ? 280  ARG   B NH1   1 
ATOM   10663 N  NH2   . ARG   B  1 282  ? 18.521  14.031  101.941 1.00 27.20 ? 280  ARG   B NH2   1 
ATOM   10664 N  N     . VAL   B  1 283  ? 13.133  9.666   99.539  1.00 20.45 ? 281  VAL   B N     1 
ATOM   10665 C  CA    . VAL   B  1 283  ? 11.921  9.549   100.346 1.00 19.47 ? 281  VAL   B CA    1 
ATOM   10666 C  C     . VAL   B  1 283  ? 11.766  8.120   100.854 1.00 21.14 ? 281  VAL   B C     1 
ATOM   10667 O  O     . VAL   B  1 283  ? 11.590  7.886   102.055 1.00 23.05 ? 281  VAL   B O     1 
ATOM   10668 C  CB    . VAL   B  1 283  ? 10.698  10.008  99.531  1.00 20.23 ? 281  VAL   B CB    1 
ATOM   10669 C  CG1   . VAL   B  1 283  ? 9.392   9.603   100.236 1.00 22.66 ? 281  VAL   B CG1   1 
ATOM   10670 C  CG2   . VAL   B  1 283  ? 10.777  11.517  99.307  1.00 18.27 ? 281  VAL   B CG2   1 
ATOM   10671 N  N     . MET   B  1 284  ? 11.861  7.139   99.949  1.00 17.46 ? 282  MET   B N     1 
ATOM   10672 C  CA    . MET   B  1 284  ? 11.735  5.745   100.376 1.00 21.97 ? 282  MET   B CA    1 
ATOM   10673 C  C     . MET   B  1 284  ? 12.899  5.317   101.258 1.00 24.24 ? 282  MET   B C     1 
ATOM   10674 O  O     . MET   B  1 284  ? 12.723  4.487   102.157 1.00 23.93 ? 282  MET   B O     1 
ATOM   10675 C  CB    . MET   B  1 284  ? 11.634  4.820   99.169  1.00 21.91 ? 282  MET   B CB    1 
ATOM   10676 C  CG    . MET   B  1 284  ? 10.461  5.130   98.260  1.00 21.56 ? 282  MET   B CG    1 
ATOM   10677 S  SD    . MET   B  1 284  ? 8.920   5.065   99.172  1.00 26.81 ? 282  MET   B SD    1 
ATOM   10678 C  CE    . MET   B  1 284  ? 8.740   3.297   99.448  1.00 27.24 ? 282  MET   B CE    1 
ATOM   10679 N  N     . GLY   B  1 285  ? 14.090  5.868   101.026 1.00 23.60 ? 283  GLY   B N     1 
ATOM   10680 C  CA    . GLY   B  1 285  ? 15.252  5.443   101.788 1.00 23.14 ? 283  GLY   B CA    1 
ATOM   10681 C  C     . GLY   B  1 285  ? 15.415  6.141   103.121 1.00 26.29 ? 283  GLY   B C     1 
ATOM   10682 O  O     . GLY   B  1 285  ? 15.944  5.550   104.068 1.00 24.39 ? 283  GLY   B O     1 
ATOM   10683 N  N     . GLU   B  1 286  ? 14.953  7.380   103.234 1.00 23.09 ? 284  GLU   B N     1 
ATOM   10684 C  CA    . GLU   B  1 286  ? 15.243  8.189   104.416 1.00 22.31 ? 284  GLU   B CA    1 
ATOM   10685 C  C     . GLU   B  1 286  ? 14.004  8.625   105.171 1.00 21.87 ? 284  GLU   B C     1 
ATOM   10686 O  O     . GLU   B  1 286  ? 14.027  8.686   106.399 1.00 25.94 ? 284  GLU   B O     1 
ATOM   10687 C  CB    . GLU   B  1 286  ? 16.044  9.430   104.003 1.00 21.13 ? 284  GLU   B CB    1 
ATOM   10688 C  CG    . GLU   B  1 286  ? 17.327  9.086   103.265 1.00 23.56 ? 284  GLU   B CG    1 
ATOM   10689 C  CD    . GLU   B  1 286  ? 17.922  10.280  102.542 1.00 29.58 ? 284  GLU   B CD    1 
ATOM   10690 O  OE1   . GLU   B  1 286  ? 17.667  11.424  102.972 1.00 28.67 ? 284  GLU   B OE1   1 
ATOM   10691 O  OE2   . GLU   B  1 286  ? 18.633  10.071  101.533 1.00 34.23 ? 284  GLU   B OE2   1 
ATOM   10692 N  N     . LEU   B  1 287  ? 12.927  8.951   104.463 1.00 22.34 ? 285  LEU   B N     1 
ATOM   10693 C  CA    . LEU   B  1 287  ? 11.684  9.358   105.106 1.00 21.76 ? 285  LEU   B CA    1 
ATOM   10694 C  C     . LEU   B  1 287  ? 10.912  8.148   105.616 1.00 22.88 ? 285  LEU   B C     1 
ATOM   10695 O  O     . LEU   B  1 287  ? 10.488  8.116   106.776 1.00 21.38 ? 285  LEU   B O     1 
ATOM   10696 C  CB    . LEU   B  1 287  ? 10.839  10.162  104.123 1.00 20.80 ? 285  LEU   B CB    1 
ATOM   10697 C  CG    . LEU   B  1 287  ? 9.813   11.162  104.673 1.00 25.36 ? 285  LEU   B CG    1 
ATOM   10698 C  CD1   . LEU   B  1 287  ? 9.210   11.933  103.522 1.00 21.87 ? 285  LEU   B CD1   1 
ATOM   10699 C  CD2   . LEU   B  1 287  ? 8.715   10.498  105.455 1.00 23.58 ? 285  LEU   B CD2   1 
ATOM   10700 N  N     . LEU   B  1 288  ? 10.713  7.148   104.762 1.00 21.74 ? 286  LEU   B N     1 
ATOM   10701 C  CA    . LEU   B  1 288  ? 9.960   5.965   105.169 1.00 23.05 ? 286  LEU   B CA    1 
ATOM   10702 C  C     . LEU   B  1 288  ? 10.469  5.340   106.461 1.00 22.95 ? 286  LEU   B C     1 
ATOM   10703 O  O     . LEU   B  1 288  ? 9.647   5.085   107.355 1.00 22.73 ? 286  LEU   B O     1 
ATOM   10704 C  CB    . LEU   B  1 288  ? 9.961   4.951   104.021 1.00 20.25 ? 286  LEU   B CB    1 
ATOM   10705 C  CG    . LEU   B  1 288  ? 9.319   3.601   104.304 1.00 28.96 ? 286  LEU   B CG    1 
ATOM   10706 C  CD1   . LEU   B  1 288  ? 7.870   3.794   104.746 1.00 25.78 ? 286  LEU   B CD1   1 
ATOM   10707 C  CD2   . LEU   B  1 288  ? 9.404   2.756   103.039 1.00 32.05 ? 286  LEU   B CD2   1 
ATOM   10708 N  N     . PRO   B  1 289  ? 11.769  5.086   106.646 1.00 25.83 ? 287  PRO   B N     1 
ATOM   10709 C  CA    . PRO   B  1 289  ? 12.206  4.495   107.928 1.00 24.78 ? 287  PRO   B CA    1 
ATOM   10710 C  C     . PRO   B  1 289  ? 11.819  5.332   109.135 1.00 25.96 ? 287  PRO   B C     1 
ATOM   10711 O  O     . PRO   B  1 289  ? 11.559  4.780   110.212 1.00 24.45 ? 287  PRO   B O     1 
ATOM   10712 C  CB    . PRO   B  1 289  ? 13.729  4.396   107.763 1.00 29.45 ? 287  PRO   B CB    1 
ATOM   10713 C  CG    . PRO   B  1 289  ? 13.930  4.319   106.275 1.00 26.74 ? 287  PRO   B CG    1 
ATOM   10714 C  CD    . PRO   B  1 289  ? 12.897  5.236   105.705 1.00 25.16 ? 287  PRO   B CD    1 
ATOM   10715 N  N     . ARG   B  1 290  ? 11.748  6.655   108.980 1.00 22.99 ? 288  ARG   B N     1 
ATOM   10716 C  CA    A ARG   B  1 290  ? 11.318  7.502   110.086 0.54 25.75 ? 288  ARG   B CA    1 
ATOM   10717 C  CA    B ARG   B  1 290  ? 11.319  7.502   110.086 0.46 25.75 ? 288  ARG   B CA    1 
ATOM   10718 C  C     . ARG   B  1 290  ? 9.834   7.327   110.378 1.00 22.94 ? 288  ARG   B C     1 
ATOM   10719 O  O     . ARG   B  1 290  ? 9.438   7.228   111.542 1.00 20.64 ? 288  ARG   B O     1 
ATOM   10720 C  CB    A ARG   B  1 290  ? 11.645  8.962   109.784 0.54 24.70 ? 288  ARG   B CB    1 
ATOM   10721 C  CB    B ARG   B  1 290  ? 11.650  8.960   109.780 0.46 24.72 ? 288  ARG   B CB    1 
ATOM   10722 C  CG    A ARG   B  1 290  ? 13.113  9.281   110.005 0.54 28.04 ? 288  ARG   B CG    1 
ATOM   10723 C  CG    B ARG   B  1 290  ? 13.148  9.191   109.674 0.46 27.66 ? 288  ARG   B CG    1 
ATOM   10724 C  CD    A ARG   B  1 290  ? 13.499  10.600  109.380 0.54 28.90 ? 288  ARG   B CD    1 
ATOM   10725 C  CD    B ARG   B  1 290  ? 13.470  10.506  109.011 0.46 28.89 ? 288  ARG   B CD    1 
ATOM   10726 N  NE    A ARG   B  1 290  ? 14.645  11.198  110.052 0.54 30.01 ? 288  ARG   B NE    1 
ATOM   10727 N  NE    B ARG   B  1 290  ? 14.907  10.678  108.831 0.46 27.09 ? 288  ARG   B NE    1 
ATOM   10728 C  CZ    A ARG   B  1 290  ? 15.194  12.360  109.724 0.54 27.45 ? 288  ARG   B CZ    1 
ATOM   10729 C  CZ    B ARG   B  1 290  ? 15.454  11.592  108.043 0.46 28.34 ? 288  ARG   B CZ    1 
ATOM   10730 N  NH1   A ARG   B  1 290  ? 14.739  13.079  108.711 0.54 27.63 ? 288  ARG   B NH1   1 
ATOM   10731 N  NH1   B ARG   B  1 290  ? 14.711  12.425  107.332 0.46 27.33 ? 288  ARG   B NH1   1 
ATOM   10732 N  NH2   A ARG   B  1 290  ? 16.214  12.818  110.437 0.54 28.99 ? 288  ARG   B NH2   1 
ATOM   10733 N  NH2   B ARG   B  1 290  ? 16.778  11.671  107.965 0.46 30.59 ? 288  ARG   B NH2   1 
ATOM   10734 N  N     . VAL   B  1 291  ? 8.994   7.289   109.336 1.00 21.31 ? 289  VAL   B N     1 
ATOM   10735 C  CA    . VAL   B  1 291  ? 7.577   7.016   109.570 1.00 21.93 ? 289  VAL   B CA    1 
ATOM   10736 C  C     . VAL   B  1 291  ? 7.413   5.657   110.220 1.00 21.20 ? 289  VAL   B C     1 
ATOM   10737 O  O     . VAL   B  1 291  ? 6.571   5.472   111.110 1.00 22.41 ? 289  VAL   B O     1 
ATOM   10738 C  CB    . VAL   B  1 291  ? 6.768   7.078   108.262 1.00 24.51 ? 289  VAL   B CB    1 
ATOM   10739 C  CG1   . VAL   B  1 291  ? 5.283   7.011   108.582 1.00 23.48 ? 289  VAL   B CG1   1 
ATOM   10740 C  CG2   . VAL   B  1 291  ? 7.092   8.310   107.479 1.00 25.47 ? 289  VAL   B CG2   1 
ATOM   10741 N  N     . LYS   B  1 292  ? 8.189   4.672   109.764 1.00 21.68 ? 290  LYS   B N     1 
ATOM   10742 C  CA    . LYS   B  1 292  ? 8.021   3.322   110.293 1.00 23.48 ? 290  LYS   B CA    1 
ATOM   10743 C  C     . LYS   B  1 292  ? 8.339   3.285   111.780 1.00 22.88 ? 290  LYS   B C     1 
ATOM   10744 O  O     . LYS   B  1 292  ? 7.634   2.634   112.560 1.00 22.75 ? 290  LYS   B O     1 
ATOM   10745 C  CB    . LYS   B  1 292  ? 8.901   2.333   109.528 1.00 25.65 ? 290  LYS   B CB    1 
ATOM   10746 C  CG    . LYS   B  1 292  ? 8.680   0.871   109.937 1.00 28.97 ? 290  LYS   B CG    1 
ATOM   10747 C  CD    . LYS   B  1 292  ? 9.834   0.324   110.746 1.00 35.63 ? 290  LYS   B CD    1 
ATOM   10748 C  CE    . LYS   B  1 292  ? 9.603   -1.148  111.121 1.00 37.07 ? 290  LYS   B CE    1 
ATOM   10749 N  NZ    . LYS   B  1 292  ? 10.108  -2.123  110.107 1.00 36.30 ? 290  LYS   B NZ    1 
ATOM   10750 N  N     . ALA   B  1 293  ? 9.396   3.987   112.188 1.00 21.50 ? 291  ALA   B N     1 
ATOM   10751 C  CA    . ALA   B  1 293  ? 9.768   4.030   113.597 1.00 25.05 ? 291  ALA   B CA    1 
ATOM   10752 C  C     . ALA   B  1 293  ? 8.663   4.654   114.442 1.00 24.94 ? 291  ALA   B C     1 
ATOM   10753 O  O     . ALA   B  1 293  ? 8.390   4.199   115.563 1.00 24.18 ? 291  ALA   B O     1 
ATOM   10754 C  CB    . ALA   B  1 293  ? 11.074  4.804   113.762 1.00 22.95 ? 291  ALA   B CB    1 
ATOM   10755 N  N     . LEU   B  1 294  ? 8.031   5.711   113.929 1.00 23.39 ? 292  LEU   B N     1 
ATOM   10756 C  CA    . LEU   B  1 294  ? 6.931   6.335   114.657 1.00 21.65 ? 292  LEU   B CA    1 
ATOM   10757 C  C     . LEU   B  1 294  ? 5.726   5.412   114.706 1.00 22.17 ? 292  LEU   B C     1 
ATOM   10758 O  O     . LEU   B  1 294  ? 5.062   5.302   115.740 1.00 24.43 ? 292  LEU   B O     1 
ATOM   10759 C  CB    . LEU   B  1 294  ? 6.549   7.668   114.008 1.00 20.83 ? 292  LEU   B CB    1 
ATOM   10760 C  CG    . LEU   B  1 294  ? 7.625   8.756   114.055 1.00 22.38 ? 292  LEU   B CG    1 
ATOM   10761 C  CD1   . LEU   B  1 294  ? 7.221   9.932   113.164 1.00 21.42 ? 292  LEU   B CD1   1 
ATOM   10762 C  CD2   . LEU   B  1 294  ? 7.907   9.221   115.480 1.00 22.02 ? 292  LEU   B CD2   1 
ATOM   10763 N  N     . ALA   B  1 295  ? 5.419   4.756   113.582 1.00 22.13 ? 293  ALA   B N     1 
ATOM   10764 C  CA    . ALA   B  1 295  ? 4.307   3.815   113.566 1.00 23.64 ? 293  ALA   B CA    1 
ATOM   10765 C  C     . ALA   B  1 295  ? 4.551   2.674   114.540 1.00 24.14 ? 293  ALA   B C     1 
ATOM   10766 O  O     . ALA   B  1 295  ? 3.627   2.213   115.221 1.00 25.69 ? 293  ALA   B O     1 
ATOM   10767 C  CB    . ALA   B  1 295  ? 4.096   3.282   112.149 1.00 21.49 ? 293  ALA   B CB    1 
ATOM   10768 N  N     . LEU   B  1 296  ? 5.799   2.219   114.635 1.00 26.27 ? 294  LEU   B N     1 
ATOM   10769 C  CA    . LEU   B  1 296  ? 6.116   1.160   115.585 1.00 26.81 ? 294  LEU   B CA    1 
ATOM   10770 C  C     . LEU   B  1 296  ? 5.842   1.602   117.018 1.00 28.98 ? 294  LEU   B C     1 
ATOM   10771 O  O     . LEU   B  1 296  ? 5.292   0.835   117.818 1.00 29.17 ? 294  LEU   B O     1 
ATOM   10772 C  CB    . LEU   B  1 296  ? 7.571   0.734   115.416 1.00 28.93 ? 294  LEU   B CB    1 
ATOM   10773 C  CG    . LEU   B  1 296  ? 8.053   -0.368  116.342 1.00 31.88 ? 294  LEU   B CG    1 
ATOM   10774 C  CD1   . LEU   B  1 296  ? 7.132   -1.565  116.228 1.00 36.51 ? 294  LEU   B CD1   1 
ATOM   10775 C  CD2   . LEU   B  1 296  ? 9.487   -0.737  115.979 1.00 36.83 ? 294  LEU   B CD2   1 
ATOM   10776 N  N     . LEU   B  1 297  ? 6.222   2.837   117.361 1.00 24.91 ? 295  LEU   B N     1 
ATOM   10777 C  CA    . LEU   B  1 297  ? 5.877   3.381   118.673 1.00 25.10 ? 295  LEU   B CA    1 
ATOM   10778 C  C     . LEU   B  1 297  ? 4.365   3.465   118.854 1.00 26.77 ? 295  LEU   B C     1 
ATOM   10779 O  O     . LEU   B  1 297  ? 3.825   3.063   119.891 1.00 24.47 ? 295  LEU   B O     1 
ATOM   10780 C  CB    . LEU   B  1 297  ? 6.518   4.759   118.851 1.00 22.92 ? 295  LEU   B CB    1 
ATOM   10781 C  CG    . LEU   B  1 297  ? 8.026   4.765   119.080 1.00 30.34 ? 295  LEU   B CG    1 
ATOM   10782 C  CD1   . LEU   B  1 297  ? 8.546   6.192   119.058 1.00 27.94 ? 295  LEU   B CD1   1 
ATOM   10783 C  CD2   . LEU   B  1 297  ? 8.386   4.099   120.408 1.00 31.30 ? 295  LEU   B CD2   1 
ATOM   10784 N  N     . ALA   B  1 298  ? 3.657   3.980   117.847 1.00 25.02 ? 296  ALA   B N     1 
ATOM   10785 C  CA    . ALA   B  1 298  ? 2.206   4.057   117.956 1.00 24.00 ? 296  ALA   B CA    1 
ATOM   10786 C  C     . ALA   B  1 298  ? 1.606   2.667   118.104 1.00 26.81 ? 296  ALA   B C     1 
ATOM   10787 O  O     . ALA   B  1 298  ? 0.688   2.462   118.905 1.00 28.00 ? 296  ALA   B O     1 
ATOM   10788 C  CB    . ALA   B  1 298  ? 1.613   4.786   116.748 1.00 24.32 ? 296  ALA   B CB    1 
ATOM   10789 N  N     . LYS   B  1 299  ? 2.135   1.690   117.366 1.00 25.33 ? 297  LYS   B N     1 
ATOM   10790 C  CA    . LYS   B  1 299  ? 1.672   0.317   117.540 1.00 27.24 ? 297  LYS   B CA    1 
ATOM   10791 C  C     . LYS   B  1 299  ? 1.889   -0.162  118.971 1.00 29.63 ? 297  LYS   B C     1 
ATOM   10792 O  O     . LYS   B  1 299  ? 0.998   -0.781  119.565 1.00 31.27 ? 297  LYS   B O     1 
ATOM   10793 C  CB    . LYS   B  1 299  ? 2.378   -0.624  116.567 1.00 30.72 ? 297  LYS   B CB    1 
ATOM   10794 C  CG    . LYS   B  1 299  ? 2.129   -2.101  116.892 1.00 35.96 ? 297  LYS   B CG    1 
ATOM   10795 C  CD    . LYS   B  1 299  ? 3.154   -3.006  116.238 1.00 39.27 ? 297  LYS   B CD    1 
ATOM   10796 C  CE    . LYS   B  1 299  ? 2.768   -4.474  116.378 1.00 42.13 ? 297  LYS   B CE    1 
ATOM   10797 N  NZ    . LYS   B  1 299  ? 2.827   -4.949  117.787 1.00 46.43 ? 297  LYS   B NZ    1 
ATOM   10798 N  N     . ASN   B  1 300  ? 3.063   0.123   119.546 1.00 27.31 ? 298  ASN   B N     1 
ATOM   10799 C  CA    . ASN   B  1 300  ? 3.362   -0.387  120.881 1.00 30.85 ? 298  ASN   B CA    1 
ATOM   10800 C  C     . ASN   B  1 300  ? 2.429   0.197   121.929 1.00 28.29 ? 298  ASN   B C     1 
ATOM   10801 O  O     . ASN   B  1 300  ? 2.183   -0.436  122.956 1.00 31.00 ? 298  ASN   B O     1 
ATOM   10802 C  CB    . ASN   B  1 300  ? 4.817   -0.101  121.254 1.00 36.26 ? 298  ASN   B CB    1 
ATOM   10803 C  CG    . ASN   B  1 300  ? 5.799   -0.916  120.434 1.00 38.12 ? 298  ASN   B CG    1 
ATOM   10804 O  OD1   . ASN   B  1 300  ? 5.462   -1.982  119.908 1.00 41.94 ? 298  ASN   B OD1   1 
ATOM   10805 N  ND2   . ASN   B  1 300  ? 7.028   -0.417  120.323 1.00 44.08 ? 298  ASN   B ND2   1 
ATOM   10806 N  N     . TYR   B  1 301  ? 1.905   1.396   121.697 1.00 27.93 ? 299  TYR   B N     1 
ATOM   10807 C  CA    . TYR   B  1 301  ? 0.928   1.987   122.600 1.00 28.37 ? 299  TYR   B CA    1 
ATOM   10808 C  C     . TYR   B  1 301  ? -0.506  1.739   122.159 1.00 26.62 ? 299  TYR   B C     1 
ATOM   10809 O  O     . TYR   B  1 301  ? -1.437  2.067   122.904 1.00 27.92 ? 299  TYR   B O     1 
ATOM   10810 C  CB    . TYR   B  1 301  ? 1.160   3.495   122.716 1.00 27.34 ? 299  TYR   B CB    1 
ATOM   10811 C  CG    . TYR   B  1 301  ? 2.404   3.872   123.493 1.00 26.80 ? 299  TYR   B CG    1 
ATOM   10812 C  CD1   . TYR   B  1 301  ? 2.449   3.744   124.874 1.00 30.09 ? 299  TYR   B CD1   1 
ATOM   10813 C  CD2   . TYR   B  1 301  ? 3.521   4.384   122.842 1.00 26.01 ? 299  TYR   B CD2   1 
ATOM   10814 C  CE1   . TYR   B  1 301  ? 3.585   4.103   125.589 1.00 29.28 ? 299  TYR   B CE1   1 
ATOM   10815 C  CE2   . TYR   B  1 301  ? 4.655   4.746   123.540 1.00 26.30 ? 299  TYR   B CE2   1 
ATOM   10816 C  CZ    . TYR   B  1 301  ? 4.681   4.601   124.911 1.00 31.01 ? 299  TYR   B CZ    1 
ATOM   10817 O  OH    . TYR   B  1 301  ? 5.806   4.969   125.602 1.00 27.05 ? 299  TYR   B OH    1 
ATOM   10818 N  N     . ASP   B  1 302  ? -0.693  1.151   120.985 1.00 25.62 ? 300  ASP   B N     1 
ATOM   10819 C  CA    . ASP   B  1 302  ? -2.006  0.954   120.383 1.00 28.65 ? 300  ASP   B CA    1 
ATOM   10820 C  C     . ASP   B  1 302  ? -2.788  2.263   120.313 1.00 27.65 ? 300  ASP   B C     1 
ATOM   10821 O  O     . ASP   B  1 302  ? -3.917  2.383   120.797 1.00 27.70 ? 300  ASP   B O     1 
ATOM   10822 C  CB    . ASP   B  1 302  ? -2.806  -0.119  121.114 1.00 31.42 ? 300  ASP   B CB    1 
ATOM   10823 C  CG    . ASP   B  1 302  ? -3.895  -0.696  120.236 1.00 33.07 ? 300  ASP   B CG    1 
ATOM   10824 O  OD1   . ASP   B  1 302  ? -3.720  -0.668  118.991 1.00 32.93 ? 300  ASP   B OD1   1 
ATOM   10825 O  OD2   . ASP   B  1 302  ? -4.927  -1.137  120.776 1.00 36.72 ? 300  ASP   B OD2   1 
ATOM   10826 N  N     . ILE   B  1 303  ? -2.164  3.260   119.699 1.00 27.26 ? 301  ILE   B N     1 
ATOM   10827 C  CA    . ILE   B  1 303  ? -2.822  4.510   119.367 1.00 25.46 ? 301  ILE   B CA    1 
ATOM   10828 C  C     . ILE   B  1 303  ? -2.831  4.642   117.849 1.00 25.60 ? 301  ILE   B C     1 
ATOM   10829 O  O     . ILE   B  1 303  ? -2.078  3.975   117.135 1.00 24.14 ? 301  ILE   B O     1 
ATOM   10830 C  CB    . ILE   B  1 303  ? -2.131  5.727   120.019 1.00 24.14 ? 301  ILE   B CB    1 
ATOM   10831 C  CG1   . ILE   B  1 303  ? -0.772  5.990   119.361 1.00 27.44 ? 301  ILE   B CG1   1 
ATOM   10832 C  CG2   . ILE   B  1 303  ? -1.958  5.495   121.501 1.00 26.07 ? 301  ILE   B CG2   1 
ATOM   10833 C  CD1   . ILE   B  1 303  ? -0.131  7.293   119.798 1.00 23.94 ? 301  ILE   B CD1   1 
ATOM   10834 N  N     . GLY   B  1 304  ? -3.694  5.528   117.360 1.00 24.27 ? 302  GLY   B N     1 
ATOM   10835 C  CA    . GLY   B  1 304  ? -3.728  5.811   115.943 1.00 23.76 ? 302  GLY   B CA    1 
ATOM   10836 C  C     . GLY   B  1 304  ? -2.607  6.762   115.552 1.00 24.38 ? 302  GLY   B C     1 
ATOM   10837 O  O     . GLY   B  1 304  ? -2.211  7.643   116.315 1.00 24.48 ? 302  GLY   B O     1 
ATOM   10838 N  N     . LEU   B  1 305  ? -2.068  6.544   114.358 1.00 21.34 ? 303  LEU   B N     1 
ATOM   10839 C  CA    . LEU   B  1 305  ? -1.092  7.451   113.758 1.00 21.44 ? 303  LEU   B CA    1 
ATOM   10840 C  C     . LEU   B  1 305  ? -1.591  7.749   112.354 1.00 23.05 ? 303  LEU   B C     1 
ATOM   10841 O  O     . LEU   B  1 305  ? -1.659  6.845   111.514 1.00 23.80 ? 303  LEU   B O     1 
ATOM   10842 C  CB    . LEU   B  1 305  ? 0.309   6.841   113.740 1.00 22.25 ? 303  LEU   B CB    1 
ATOM   10843 C  CG    . LEU   B  1 305  ? 1.427   7.682   113.098 1.00 24.66 ? 303  LEU   B CG    1 
ATOM   10844 C  CD1   . LEU   B  1 305  ? 2.757   7.462   113.795 1.00 25.52 ? 303  LEU   B CD1   1 
ATOM   10845 C  CD2   . LEU   B  1 305  ? 1.568   7.385   111.609 1.00 26.27 ? 303  LEU   B CD2   1 
ATOM   10846 N  N     . ASN   B  1 306  ? -1.953  9.004   112.106 1.00 21.29 ? 304  ASN   B N     1 
ATOM   10847 C  CA    . ASN   B  1 306  ? -2.587  9.406   110.859 1.00 22.62 ? 304  ASN   B CA    1 
ATOM   10848 C  C     . ASN   B  1 306  ? -1.616  10.200  110.006 1.00 22.73 ? 304  ASN   B C     1 
ATOM   10849 O  O     . ASN   B  1 306  ? -0.992  11.144  110.497 1.00 21.23 ? 304  ASN   B O     1 
ATOM   10850 C  CB    . ASN   B  1 306  ? -3.822  10.264  111.108 1.00 23.49 ? 304  ASN   B CB    1 
ATOM   10851 C  CG    . ASN   B  1 306  ? -4.327  10.886  109.833 1.00 25.14 ? 304  ASN   B CG    1 
ATOM   10852 O  OD1   . ASN   B  1 306  ? -4.003  12.034  109.500 1.00 24.93 ? 304  ASN   B OD1   1 
ATOM   10853 N  ND2   . ASN   B  1 306  ? -5.057  10.105  109.068 1.00 20.49 ? 304  ASN   B ND2   1 
ATOM   10854 N  N     . ILE   B  1 307  ? -1.529  9.847   108.729 1.00 21.04 ? 305  ILE   B N     1 
ATOM   10855 C  CA    . ILE   B  1 307  ? -0.740  10.605  107.763 1.00 22.90 ? 305  ILE   B CA    1 
ATOM   10856 C  C     . ILE   B  1 307  ? -1.646  11.648  107.116 1.00 23.15 ? 305  ILE   B C     1 
ATOM   10857 O  O     . ILE   B  1 307  ? -2.527  11.307  106.319 1.00 19.92 ? 305  ILE   B O     1 
ATOM   10858 C  CB    . ILE   B  1 307  ? -0.119  9.690   106.704 1.00 23.48 ? 305  ILE   B CB    1 
ATOM   10859 C  CG1   . ILE   B  1 307  ? 0.881   8.720   107.354 1.00 24.80 ? 305  ILE   B CG1   1 
ATOM   10860 C  CG2   . ILE   B  1 307  ? 0.513   10.518  105.595 1.00 24.04 ? 305  ILE   B CG2   1 
ATOM   10861 C  CD1   . ILE   B  1 307  ? 1.357   7.627   106.404 1.00 25.24 ? 305  ILE   B CD1   1 
ATOM   10862 N  N     . ASP   B  1 308  ? -1.418  12.920  107.442 1.00 20.86 ? 306  ASP   B N     1 
ATOM   10863 C  CA    . ASP   B  1 308  ? -2.179  14.001  106.826 1.00 20.67 ? 306  ASP   B CA    1 
ATOM   10864 C  C     . ASP   B  1 308  ? -1.892  14.076  105.333 1.00 18.99 ? 306  ASP   B C     1 
ATOM   10865 O  O     . ASP   B  1 308  ? -0.811  13.708  104.860 1.00 19.47 ? 306  ASP   B O     1 
ATOM   10866 C  CB    . ASP   B  1 308  ? -1.834  15.351  107.471 1.00 22.27 ? 306  ASP   B CB    1 
ATOM   10867 C  CG    . ASP   B  1 308  ? -2.386  15.500  108.886 1.00 25.09 ? 306  ASP   B CG    1 
ATOM   10868 O  OD1   . ASP   B  1 308  ? -3.200  14.662  109.340 1.00 21.23 ? 306  ASP   B OD1   1 
ATOM   10869 O  OD2   . ASP   B  1 308  ? -2.008  16.492  109.540 1.00 24.82 ? 306  ASP   B OD2   1 
ATOM   10870 N  N     . ALA   B  1 309  ? -2.869  14.563  104.582 1.00 18.88 ? 307  ALA   B N     1 
ATOM   10871 C  CA    . ALA   B  1 309  ? -2.707  14.714  103.147 1.00 18.11 ? 307  ALA   B CA    1 
ATOM   10872 C  C     . ALA   B  1 309  ? -2.321  16.147  102.819 1.00 19.20 ? 307  ALA   B C     1 
ATOM   10873 O  O     . ALA   B  1 309  ? -2.844  17.099  103.404 1.00 18.71 ? 307  ALA   B O     1 
ATOM   10874 C  CB    . ALA   B  1 309  ? -3.979  14.310  102.405 1.00 19.36 ? 307  ALA   B CB    1 
ATOM   10875 N  N     . GLU   B  1 310  ? -1.391  16.291  101.878 1.00 18.26 ? 308  GLU   B N     1 
ATOM   10876 C  CA    . GLU   B  1 310  ? -0.828  17.593  101.576 1.00 18.74 ? 308  GLU   B CA    1 
ATOM   10877 C  C     . GLU   B  1 310  ? -1.101  17.951  100.121 1.00 17.85 ? 308  GLU   B C     1 
ATOM   10878 O  O     . GLU   B  1 310  ? -2.226  17.761  99.643  1.00 18.01 ? 308  GLU   B O     1 
ATOM   10879 C  CB    . GLU   B  1 310  ? 0.660   17.588  101.918 1.00 19.02 ? 308  GLU   B CB    1 
ATOM   10880 C  CG    . GLU   B  1 310  ? 0.874   17.171  103.383 1.00 21.33 ? 308  GLU   B CG    1 
ATOM   10881 C  CD    . GLU   B  1 310  ? 2.303   17.321  103.843 1.00 18.66 ? 308  GLU   B CD    1 
ATOM   10882 O  OE1   . GLU   B  1 310  ? 2.770   18.466  103.936 1.00 22.09 ? 308  GLU   B OE1   1 
ATOM   10883 O  OE2   . GLU   B  1 310  ? 2.941   16.298  104.138 1.00 19.37 ? 308  GLU   B OE2   1 
ATOM   10884 N  N     . GLU   B  1 311  ? -0.096  18.459  99.410  1.00 16.85 ? 309  GLU   B N     1 
ATOM   10885 C  CA    . GLU   B  1 311  ? -0.321  18.925  98.047  1.00 18.61 ? 309  GLU   B CA    1 
ATOM   10886 C  C     . GLU   B  1 311  ? -0.621  17.765  97.097  1.00 17.08 ? 309  GLU   B C     1 
ATOM   10887 O  O     . GLU   B  1 311  ? -0.260  16.612  97.339  1.00 16.96 ? 309  GLU   B O     1 
ATOM   10888 C  CB    . GLU   B  1 311  ? 0.886   19.713  97.538  1.00 18.42 ? 309  GLU   B CB    1 
ATOM   10889 C  CG    . GLU   B  1 311  ? 1.136   20.995  98.318  1.00 20.14 ? 309  GLU   B CG    1 
ATOM   10890 C  CD    . GLU   B  1 311  ? 1.997   20.787  99.545  1.00 24.19 ? 309  GLU   B CD    1 
ATOM   10891 O  OE1   . GLU   B  1 311  ? 2.276   19.623  99.910  1.00 20.12 ? 309  GLU   B OE1   1 
ATOM   10892 O  OE2   . GLU   B  1 311  ? 2.414   21.798  100.147 1.00 25.53 ? 309  GLU   B OE2   1 
ATOM   10893 N  N     . ALA   B  1 312  ? -1.289  18.098  95.986  1.00 15.05 ? 310  ALA   B N     1 
ATOM   10894 C  CA    . ALA   B  1 312  ? -1.732  17.060  95.059  1.00 17.03 ? 310  ALA   B CA    1 
ATOM   10895 C  C     . ALA   B  1 312  ? -0.563  16.264  94.495  1.00 18.45 ? 310  ALA   B C     1 
ATOM   10896 O  O     . ALA   B  1 312  ? -0.695  15.052  94.264  1.00 17.50 ? 310  ALA   B O     1 
ATOM   10897 C  CB    . ALA   B  1 312  ? -2.552  17.668  93.917  1.00 17.50 ? 310  ALA   B CB    1 
ATOM   10898 N  N     . ASP   B  1 313  ? 0.594   16.906  94.286  1.00 17.16 ? 311  ASP   B N     1 
ATOM   10899 C  CA    . ASP   B  1 313  ? 1.713   16.186  93.694  1.00 17.88 ? 311  ASP   B CA    1 
ATOM   10900 C  C     . ASP   B  1 313  ? 2.440   15.297  94.694  1.00 16.04 ? 311  ASP   B C     1 
ATOM   10901 O  O     . ASP   B  1 313  ? 3.439   14.671  94.335  1.00 18.56 ? 311  ASP   B O     1 
ATOM   10902 C  CB    . ASP   B  1 313  ? 2.690   17.156  93.010  1.00 19.58 ? 311  ASP   B CB    1 
ATOM   10903 C  CG    . ASP   B  1 313  ? 3.351   18.135  93.965  1.00 21.64 ? 311  ASP   B CG    1 
ATOM   10904 O  OD1   . ASP   B  1 313  ? 3.162   18.043  95.191  1.00 21.49 ? 311  ASP   B OD1   1 
ATOM   10905 O  OD2   . ASP   B  1 313  ? 4.092   19.009  93.465  1.00 22.04 ? 311  ASP   B OD2   1 
ATOM   10906 N  N     . ARG   B  1 314  ? 1.936   15.193  95.921  1.00 17.56 ? 312  ARG   B N     1 
ATOM   10907 C  CA    . ARG   B  1 314  ? 2.478   14.271  96.908  1.00 18.42 ? 312  ARG   B CA    1 
ATOM   10908 C  C     . ARG   B  1 314  ? 1.539   13.116  97.197  1.00 16.86 ? 312  ARG   B C     1 
ATOM   10909 O  O     . ARG   B  1 314  ? 1.914   12.197  97.929  1.00 18.27 ? 312  ARG   B O     1 
ATOM   10910 C  CB    . ARG   B  1 314  ? 2.799   15.021  98.206  1.00 18.51 ? 312  ARG   B CB    1 
ATOM   10911 C  CG    . ARG   B  1 314  ? 4.074   15.847  98.096  1.00 18.81 ? 312  ARG   B CG    1 
ATOM   10912 C  CD    . ARG   B  1 314  ? 4.140   16.917  99.156  1.00 19.31 ? 312  ARG   B CD    1 
ATOM   10913 N  NE    . ARG   B  1 314  ? 5.503   17.424  99.295  1.00 19.23 ? 312  ARG   B NE    1 
ATOM   10914 C  CZ    . ARG   B  1 314  ? 5.844   18.430  100.085 1.00 22.54 ? 312  ARG   B CZ    1 
ATOM   10915 N  NH1   . ARG   B  1 314  ? 4.936   19.115  100.764 1.00 18.81 ? 312  ARG   B NH1   1 
ATOM   10916 N  NH2   . ARG   B  1 314  ? 7.130   18.757  100.199 1.00 20.85 ? 312  ARG   B NH2   1 
ATOM   10917 N  N     . LEU   B  1 315  ? 0.340   13.127  96.619  1.00 16.19 ? 313  LEU   B N     1 
ATOM   10918 C  CA    . LEU   B  1 315  ? -0.650  12.107  96.953  1.00 18.07 ? 313  LEU   B CA    1 
ATOM   10919 C  C     . LEU   B  1 315  ? -0.132  10.718  96.600  1.00 21.24 ? 313  LEU   B C     1 
ATOM   10920 O  O     . LEU   B  1 315  ? -0.046  9.830   97.458  1.00 21.10 ? 313  LEU   B O     1 
ATOM   10921 C  CB    . LEU   B  1 315  ? -1.956  12.401  96.214  1.00 18.05 ? 313  LEU   B CB    1 
ATOM   10922 C  CG    . LEU   B  1 315  ? -3.276  11.821  96.736  1.00 19.95 ? 313  LEU   B CG    1 
ATOM   10923 C  CD1   . LEU   B  1 315  ? -4.434  12.331  95.874  1.00 16.19 ? 313  LEU   B CD1   1 
ATOM   10924 C  CD2   . LEU   B  1 315  ? -3.268  10.290  96.768  1.00 20.70 ? 313  LEU   B CD2   1 
ATOM   10925 N  N     . GLU   B  1 316  ? 0.202   10.504  95.331  1.00 18.04 ? 314  GLU   B N     1 
ATOM   10926 C  CA    . GLU   B  1 316  ? 0.538   9.148   94.916  1.00 20.21 ? 314  GLU   B CA    1 
ATOM   10927 C  C     . GLU   B  1 316  ? 1.836   8.688   95.557  1.00 21.14 ? 314  GLU   B C     1 
ATOM   10928 O  O     . GLU   B  1 316  ? 1.961   7.518   95.925  1.00 23.70 ? 314  GLU   B O     1 
ATOM   10929 C  CB    . GLU   B  1 316  ? 0.578   9.070   93.386  1.00 17.12 ? 314  GLU   B CB    1 
ATOM   10930 C  CG    . GLU   B  1 316  ? -0.839  9.144   92.826  1.00 19.75 ? 314  GLU   B CG    1 
ATOM   10931 C  CD    . GLU   B  1 316  ? -0.908  9.061   91.318  1.00 22.49 ? 314  GLU   B CD    1 
ATOM   10932 O  OE1   . GLU   B  1 316  ? -0.253  8.163   90.737  1.00 24.45 ? 314  GLU   B OE1   1 
ATOM   10933 O  OE2   . GLU   B  1 316  ? -1.618  9.894   90.717  1.00 22.52 ? 314  GLU   B OE2   1 
ATOM   10934 N  N     . LEU   B  1 317  ? 2.788   9.604   95.748  1.00 20.67 ? 315  LEU   B N     1 
ATOM   10935 C  CA    . LEU   B  1 317  ? 4.008   9.255   96.467  1.00 21.24 ? 315  LEU   B CA    1 
ATOM   10936 C  C     . LEU   B  1 317  ? 3.697   8.751   97.868  1.00 22.30 ? 315  LEU   B C     1 
ATOM   10937 O  O     . LEU   B  1 317  ? 4.276   7.754   98.312  1.00 22.81 ? 315  LEU   B O     1 
ATOM   10938 C  CB    . LEU   B  1 317  ? 4.946   10.457  96.533  1.00 20.73 ? 315  LEU   B CB    1 
ATOM   10939 C  CG    . LEU   B  1 317  ? 6.236   10.247  97.326  1.00 23.99 ? 315  LEU   B CG    1 
ATOM   10940 C  CD1   . LEU   B  1 317  ? 6.993   9.046   96.773  1.00 25.42 ? 315  LEU   B CD1   1 
ATOM   10941 C  CD2   . LEU   B  1 317  ? 7.094   11.496  97.268  1.00 23.37 ? 315  LEU   B CD2   1 
ATOM   10942 N  N     . SER   B  1 318  ? 2.769   9.411   98.578  1.00 19.08 ? 316  SER   B N     1 
ATOM   10943 C  CA    . SER   B  1 318  ? 2.448   8.971   99.934  1.00 20.44 ? 316  SER   B CA    1 
ATOM   10944 C  C     . SER   B  1 318  ? 1.857   7.568   99.937  1.00 21.90 ? 316  SER   B C     1 
ATOM   10945 O  O     . SER   B  1 318  ? 2.003   6.843   100.921 1.00 20.47 ? 316  SER   B O     1 
ATOM   10946 C  CB    . SER   B  1 318  ? 1.496   9.957   100.621 1.00 20.99 ? 316  SER   B CB    1 
ATOM   10947 O  OG    . SER   B  1 318  ? 0.193   9.916   100.075 1.00 20.22 ? 316  SER   B OG    1 
ATOM   10948 N  N     . LEU   B  1 319  ? 1.215   7.157   98.839  1.00 22.26 ? 317  LEU   B N     1 
ATOM   10949 C  CA    . LEU   B  1 319  ? 0.666   5.804   98.762  1.00 22.44 ? 317  LEU   B CA    1 
ATOM   10950 C  C     . LEU   B  1 319  ? 1.762   4.747   98.762  1.00 24.36 ? 317  LEU   B C     1 
ATOM   10951 O  O     . LEU   B  1 319  ? 1.547   3.639   99.254  1.00 24.94 ? 317  LEU   B O     1 
ATOM   10952 C  CB    . LEU   B  1 319  ? -0.192  5.653   97.501  1.00 21.33 ? 317  LEU   B CB    1 
ATOM   10953 C  CG    . LEU   B  1 319  ? -1.386  6.599   97.407  1.00 23.23 ? 317  LEU   B CG    1 
ATOM   10954 C  CD1   . LEU   B  1 319  ? -2.099  6.399   96.072  1.00 22.69 ? 317  LEU   B CD1   1 
ATOM   10955 C  CD2   . LEU   B  1 319  ? -2.340  6.347   98.564  1.00 23.76 ? 317  LEU   B CD2   1 
ATOM   10956 N  N     . ASP   B  1 320  ? 2.927   5.050   98.190  1.00 22.24 ? 318  ASP   B N     1 
ATOM   10957 C  CA    . ASP   B  1 320  ? 4.018   4.086   98.250  1.00 23.94 ? 318  ASP   B CA    1 
ATOM   10958 C  C     . ASP   B  1 320  ? 4.493   3.884   99.682  1.00 26.82 ? 318  ASP   B C     1 
ATOM   10959 O  O     . ASP   B  1 320  ? 4.869   2.770   100.054 1.00 25.60 ? 318  ASP   B O     1 
ATOM   10960 C  CB    . ASP   B  1 320  ? 5.161   4.537   97.341  1.00 23.29 ? 318  ASP   B CB    1 
ATOM   10961 C  CG    . ASP   B  1 320  ? 4.824   4.349   95.861  1.00 23.53 ? 318  ASP   B CG    1 
ATOM   10962 O  OD1   . ASP   B  1 320  ? 4.490   3.213   95.471  1.00 29.77 ? 318  ASP   B OD1   1 
ATOM   10963 O  OD2   . ASP   B  1 320  ? 4.865   5.331   95.098  1.00 24.60 ? 318  ASP   B OD2   1 
ATOM   10964 N  N     . LEU   B  1 321  ? 4.464   4.936   100.503 1.00 21.62 ? 319  LEU   B N     1 
ATOM   10965 C  CA    . LEU   B  1 321  ? 4.788   4.764   101.918 1.00 21.27 ? 319  LEU   B CA    1 
ATOM   10966 C  C     . LEU   B  1 321  ? 3.704   3.969   102.633 1.00 21.65 ? 319  LEU   B C     1 
ATOM   10967 O  O     . LEU   B  1 321  ? 4.001   3.030   103.382 1.00 24.85 ? 319  LEU   B O     1 
ATOM   10968 C  CB    . LEU   B  1 321  ? 4.985   6.124   102.583 1.00 19.79 ? 319  LEU   B CB    1 
ATOM   10969 C  CG    . LEU   B  1 321  ? 6.341   6.761   102.273 1.00 23.63 ? 319  LEU   B CG    1 
ATOM   10970 C  CD1   . LEU   B  1 321  ? 6.241   7.700   101.103 1.00 23.73 ? 319  LEU   B CD1   1 
ATOM   10971 C  CD2   . LEU   B  1 321  ? 6.891   7.472   103.504 1.00 25.84 ? 319  LEU   B CD2   1 
ATOM   10972 N  N     . LEU   B  1 322  ? 2.437   4.338   102.412 1.00 21.62 ? 320  LEU   B N     1 
ATOM   10973 C  CA    . LEU   B  1 322  ? 1.325   3.603   103.002 1.00 21.88 ? 320  LEU   B CA    1 
ATOM   10974 C  C     . LEU   B  1 322  ? 1.423   2.119   102.682 1.00 24.15 ? 320  LEU   B C     1 
ATOM   10975 O  O     . LEU   B  1 322  ? 1.263   1.267   103.563 1.00 26.03 ? 320  LEU   B O     1 
ATOM   10976 C  CB    . LEU   B  1 322  ? -0.008  4.162   102.489 1.00 20.43 ? 320  LEU   B CB    1 
ATOM   10977 C  CG    . LEU   B  1 322  ? -1.225  3.519   103.161 1.00 22.26 ? 320  LEU   B CG    1 
ATOM   10978 C  CD1   . LEU   B  1 322  ? -1.212  3.837   104.658 1.00 22.84 ? 320  LEU   B CD1   1 
ATOM   10979 C  CD2   . LEU   B  1 322  ? -2.525  3.961   102.497 1.00 22.11 ? 320  LEU   B CD2   1 
ATOM   10980 N  N     . GLU   B  1 323  ? 1.691   1.799   101.414 1.00 23.73 ? 321  GLU   B N     1 
ATOM   10981 C  CA    . GLU   B  1 323  ? 1.824   0.408   100.990 1.00 26.70 ? 321  GLU   B CA    1 
ATOM   10982 C  C     . GLU   B  1 323  ? 2.885   -0.324  101.807 1.00 25.91 ? 321  GLU   B C     1 
ATOM   10983 O  O     . GLU   B  1 323  ? 2.639   -1.422  102.315 1.00 26.01 ? 321  GLU   B O     1 
ATOM   10984 C  CB    . GLU   B  1 323  ? 2.162   0.360   99.498  1.00 25.71 ? 321  GLU   B CB    1 
ATOM   10985 C  CG    . GLU   B  1 323  ? 2.521   -1.021  98.973  1.00 31.58 ? 321  GLU   B CG    1 
ATOM   10986 C  CD    . GLU   B  1 323  ? 1.365   -1.718  98.286  1.00 30.09 ? 321  GLU   B CD    1 
ATOM   10987 O  OE1   . GLU   B  1 323  ? 0.374   -1.042  97.936  1.00 31.12 ? 321  GLU   B OE1   1 
ATOM   10988 O  OE2   . GLU   B  1 323  ? 1.444   -2.950  98.101  1.00 33.24 ? 321  GLU   B OE2   1 
ATOM   10989 N  N     . VAL   B  1 324  ? 4.076   0.267   101.943 1.00 22.94 ? 322  VAL   B N     1 
ATOM   10990 C  CA    . VAL   B  1 324  ? 5.144   -0.408  102.684 1.00 24.75 ? 322  VAL   B CA    1 
ATOM   10991 C  C     . VAL   B  1 324  ? 4.759   -0.580  104.148 1.00 29.71 ? 322  VAL   B C     1 
ATOM   10992 O  O     . VAL   B  1 324  ? 5.029   -1.623  104.763 1.00 30.00 ? 322  VAL   B O     1 
ATOM   10993 C  CB    . VAL   B  1 324  ? 6.470   0.366   102.554 1.00 27.53 ? 322  VAL   B CB    1 
ATOM   10994 C  CG1   . VAL   B  1 324  ? 7.505   -0.212  103.516 1.00 30.98 ? 322  VAL   B CG1   1 
ATOM   10995 C  CG2   . VAL   B  1 324  ? 6.977   0.330   101.117 1.00 25.69 ? 322  VAL   B CG2   1 
ATOM   10996 N  N     . LEU   B  1 325  ? 4.136   0.442   104.735 1.00 25.29 ? 323  LEU   B N     1 
ATOM   10997 C  CA    . LEU   B  1 325  ? 3.779   0.369   106.147 1.00 26.46 ? 323  LEU   B CA    1 
ATOM   10998 C  C     . LEU   B  1 325  ? 2.713   -0.689  106.391 1.00 27.32 ? 323  LEU   B C     1 
ATOM   10999 O  O     . LEU   B  1 325  ? 2.758   -1.407  107.398 1.00 28.35 ? 323  LEU   B O     1 
ATOM   11000 C  CB    . LEU   B  1 325  ? 3.310   1.733   106.637 1.00 24.83 ? 323  LEU   B CB    1 
ATOM   11001 C  CG    . LEU   B  1 325  ? 4.405   2.812   106.645 1.00 24.51 ? 323  LEU   B CG    1 
ATOM   11002 C  CD1   . LEU   B  1 325  ? 3.804   4.200   106.736 1.00 25.48 ? 323  LEU   B CD1   1 
ATOM   11003 C  CD2   . LEU   B  1 325  ? 5.395   2.585   107.796 1.00 24.40 ? 323  LEU   B CD2   1 
ATOM   11004 N  N     . CYS   B  1 326  ? 1.744   -0.807  105.484 1.00 24.68 ? 324  CYS   B N     1 
ATOM   11005 C  CA    . CYS   B  1 326  ? 0.689   -1.787  105.705 1.00 25.53 ? 324  CYS   B CA    1 
ATOM   11006 C  C     . CYS   B  1 326  ? 1.174   -3.218  105.522 1.00 27.35 ? 324  CYS   B C     1 
ATOM   11007 O  O     . CYS   B  1 326  ? 0.584   -4.135  106.106 1.00 27.84 ? 324  CYS   B O     1 
ATOM   11008 C  CB    . CYS   B  1 326  ? -0.493  -1.501  104.779 1.00 29.71 ? 324  CYS   B CB    1 
ATOM   11009 S  SG    . CYS   B  1 326  ? -1.375  -0.014  105.278 1.00 28.98 ? 324  CYS   B SG    1 
ATOM   11010 N  N     . LEU   B  1 327  ? 2.230   -3.430  104.740 1.00 26.66 ? 325  LEU   B N     1 
ATOM   11011 C  CA    . LEU   B  1 327  ? 2.816   -4.755  104.553 1.00 26.39 ? 325  LEU   B CA    1 
ATOM   11012 C  C     . LEU   B  1 327  ? 3.958   -5.044  105.522 1.00 31.53 ? 325  LEU   B C     1 
ATOM   11013 O  O     . LEU   B  1 327  ? 4.545   -6.134  105.473 1.00 29.28 ? 325  LEU   B O     1 
ATOM   11014 C  CB    . LEU   B  1 327  ? 3.308   -4.909  103.112 1.00 28.11 ? 325  LEU   B CB    1 
ATOM   11015 C  CG    . LEU   B  1 327  ? 2.194   -4.747  102.075 1.00 33.30 ? 325  LEU   B CG    1 
ATOM   11016 C  CD1   . LEU   B  1 327  ? 2.741   -4.840  100.662 1.00 36.09 ? 325  LEU   B CD1   1 
ATOM   11017 C  CD2   . LEU   B  1 327  ? 1.132   -5.788  102.302 1.00 36.26 ? 325  LEU   B CD2   1 
ATOM   11018 N  N     . ASP   B  1 328  ? 4.279   -4.103  106.403 1.00 29.24 ? 326  ASP   B N     1 
ATOM   11019 C  CA    . ASP   B  1 328  ? 5.392   -4.272  107.328 1.00 30.97 ? 326  ASP   B CA    1 
ATOM   11020 C  C     . ASP   B  1 328  ? 4.968   -5.167  108.483 1.00 28.60 ? 326  ASP   B C     1 
ATOM   11021 O  O     . ASP   B  1 328  ? 4.100   -4.795  109.280 1.00 32.66 ? 326  ASP   B O     1 
ATOM   11022 C  CB    . ASP   B  1 328  ? 5.861   -2.910  107.833 1.00 33.04 ? 326  ASP   B CB    1 
ATOM   11023 C  CG    . ASP   B  1 328  ? 7.195   -2.979  108.552 1.00 36.90 ? 326  ASP   B CG    1 
ATOM   11024 O  OD1   . ASP   B  1 328  ? 7.483   -4.004  109.202 1.00 33.77 ? 326  ASP   B OD1   1 
ATOM   11025 O  OD2   . ASP   B  1 328  ? 7.961   -1.999  108.461 1.00 39.82 ? 326  ASP   B OD2   1 
ATOM   11026 N  N     . GLY   B  1 329  ? 5.584   -6.348  108.578 1.00 32.97 ? 327  GLY   B N     1 
ATOM   11027 C  CA    . GLY   B  1 329  ? 5.242   -7.282  109.641 1.00 31.40 ? 327  GLY   B CA    1 
ATOM   11028 C  C     . GLY   B  1 329  ? 5.532   -6.770  111.041 1.00 36.07 ? 327  GLY   B C     1 
ATOM   11029 O  O     . GLY   B  1 329  ? 4.880   -7.203  111.998 1.00 34.15 ? 327  GLY   B O     1 
ATOM   11030 N  N     . ASP   B  1 330  ? 6.488   -5.851  111.190 1.00 34.26 ? 328  ASP   B N     1 
ATOM   11031 C  CA    . ASP   B  1 330  ? 6.701   -5.249  112.504 1.00 34.32 ? 328  ASP   B CA    1 
ATOM   11032 C  C     . ASP   B  1 330  ? 5.447   -4.559  113.017 1.00 33.61 ? 328  ASP   B C     1 
ATOM   11033 O  O     . ASP   B  1 330  ? 5.283   -4.422  114.232 1.00 34.54 ? 328  ASP   B O     1 
ATOM   11034 C  CB    . ASP   B  1 330  ? 7.865   -4.254  112.468 1.00 38.06 ? 328  ASP   B CB    1 
ATOM   11035 C  CG    . ASP   B  1 330  ? 9.199   -4.927  112.196 1.00 45.17 ? 328  ASP   B CG    1 
ATOM   11036 O  OD1   . ASP   B  1 330  ? 9.291   -6.163  112.383 1.00 42.68 ? 328  ASP   B OD1   1 
ATOM   11037 O  OD2   . ASP   B  1 330  ? 10.160  -4.227  111.803 1.00 38.32 ? 328  ASP   B OD2   1 
ATOM   11038 N  N     . LEU   B  1 331  ? 4.539   -4.156  112.124 1.00 31.90 ? 329  LEU   B N     1 
ATOM   11039 C  CA    . LEU   B  1 331  ? 3.301   -3.493  112.512 1.00 33.89 ? 329  LEU   B CA    1 
ATOM   11040 C  C     . LEU   B  1 331  ? 2.108   -4.445  112.547 1.00 32.56 ? 329  LEU   B C     1 
ATOM   11041 O  O     . LEU   B  1 331  ? 0.971   -3.987  112.700 1.00 29.54 ? 329  LEU   B O     1 
ATOM   11042 C  CB    . LEU   B  1 331  ? 3.023   -2.316  111.567 1.00 29.78 ? 329  LEU   B CB    1 
ATOM   11043 C  CG    . LEU   B  1 331  ? 4.187   -1.326  111.457 1.00 31.96 ? 329  LEU   B CG    1 
ATOM   11044 C  CD1   . LEU   B  1 331  ? 3.955   -0.262  110.382 1.00 31.53 ? 329  LEU   B CD1   1 
ATOM   11045 C  CD2   . LEU   B  1 331  ? 4.479   -0.683  112.817 1.00 31.68 ? 329  LEU   B CD2   1 
ATOM   11046 N  N     . SER   B  1 332  ? 2.349   -5.754  112.429 1.00 33.72 ? 330  SER   B N     1 
ATOM   11047 C  CA    . SER   B  1 332  ? 1.277   -6.744  112.349 1.00 35.74 ? 330  SER   B CA    1 
ATOM   11048 C  C     . SER   B  1 332  ? 0.327   -6.631  113.533 1.00 36.70 ? 330  SER   B C     1 
ATOM   11049 O  O     . SER   B  1 332  ? 0.757   -6.576  114.686 1.00 40.59 ? 330  SER   B O     1 
ATOM   11050 C  CB    . SER   B  1 332  ? 1.871   -8.158  112.301 1.00 38.33 ? 330  SER   B CB    1 
ATOM   11051 O  OG    . SER   B  1 332  ? 1.244   -8.967  111.312 1.00 40.29 ? 330  SER   B OG    1 
ATOM   11052 N  N     . GLY   B  1 333  ? -0.975  -6.605  113.240 1.00 36.19 ? 331  GLY   B N     1 
ATOM   11053 C  CA    . GLY   B  1 333  ? -1.994  -6.547  114.265 1.00 40.34 ? 331  GLY   B CA    1 
ATOM   11054 C  C     . GLY   B  1 333  ? -2.469  -5.154  114.621 1.00 42.04 ? 331  GLY   B C     1 
ATOM   11055 O  O     . GLY   B  1 333  ? -3.549  -5.009  115.202 1.00 43.56 ? 331  GLY   B O     1 
ATOM   11056 N  N     . TRP   B  1 334  ? -1.706  -4.126  114.271 1.00 35.93 ? 332  TRP   B N     1 
ATOM   11057 C  CA    . TRP   B  1 334  ? -2.033  -2.753  114.625 1.00 34.52 ? 332  TRP   B CA    1 
ATOM   11058 C  C     . TRP   B  1 334  ? -2.945  -2.159  113.564 1.00 36.02 ? 332  TRP   B C     1 
ATOM   11059 O  O     . TRP   B  1 334  ? -2.591  -2.131  112.381 1.00 36.20 ? 332  TRP   B O     1 
ATOM   11060 C  CB    . TRP   B  1 334  ? -0.749  -1.944  114.758 1.00 32.41 ? 332  TRP   B CB    1 
ATOM   11061 C  CG    . TRP   B  1 334  ? -0.942  -0.498  114.976 1.00 31.97 ? 332  TRP   B CG    1 
ATOM   11062 C  CD1   . TRP   B  1 334  ? -1.623  0.102   115.995 1.00 33.45 ? 332  TRP   B CD1   1 
ATOM   11063 C  CD2   . TRP   B  1 334  ? -0.403  0.553   114.175 1.00 32.71 ? 332  TRP   B CD2   1 
ATOM   11064 N  NE1   . TRP   B  1 334  ? -1.557  1.471   115.862 1.00 29.97 ? 332  TRP   B NE1   1 
ATOM   11065 C  CE2   . TRP   B  1 334  ? -0.812  1.771   114.752 1.00 27.03 ? 332  TRP   B CE2   1 
ATOM   11066 C  CE3   . TRP   B  1 334  ? 0.379   0.583   113.019 1.00 27.52 ? 332  TRP   B CE3   1 
ATOM   11067 C  CZ2   . TRP   B  1 334  ? -0.455  3.005   114.216 1.00 24.96 ? 332  TRP   B CZ2   1 
ATOM   11068 C  CZ3   . TRP   B  1 334  ? 0.728   1.805   112.490 1.00 28.60 ? 332  TRP   B CZ3   1 
ATOM   11069 C  CH2   . TRP   B  1 334  ? 0.315   2.999   113.087 1.00 26.89 ? 332  TRP   B CH2   1 
ATOM   11070 N  N     . ASN   B  1 335  ? -4.119  -1.689  113.983 1.00 28.91 ? 333  ASN   B N     1 
ATOM   11071 C  CA    . ASN   B  1 335  ? -5.072  -1.075  113.073 1.00 28.96 ? 333  ASN   B CA    1 
ATOM   11072 C  C     . ASN   B  1 335  ? -5.105  0.440   113.204 1.00 29.45 ? 333  ASN   B C     1 
ATOM   11073 O  O     . ASN   B  1 335  ? -6.051  1.082   112.737 1.00 29.57 ? 333  ASN   B O     1 
ATOM   11074 C  CB    . ASN   B  1 335  ? -6.460  -1.668  113.299 1.00 30.80 ? 333  ASN   B CB    1 
ATOM   11075 C  CG    . ASN   B  1 335  ? -6.515  -3.128  112.941 1.00 37.96 ? 333  ASN   B CG    1 
ATOM   11076 O  OD1   . ASN   B  1 335  ? -5.857  -3.564  111.994 1.00 36.38 ? 333  ASN   B OD1   1 
ATOM   11077 N  ND2   . ASN   B  1 335  ? -7.284  -3.904  113.704 1.00 36.65 ? 333  ASN   B ND2   1 
ATOM   11078 N  N     . GLY   B  1 336  ? -4.089  1.026   113.818 1.00 29.40 ? 334  GLY   B N     1 
ATOM   11079 C  CA    . GLY   B  1 336  ? -4.113  2.453   114.020 1.00 26.51 ? 334  GLY   B CA    1 
ATOM   11080 C  C     . GLY   B  1 336  ? -3.505  3.265   112.912 1.00 27.55 ? 334  GLY   B C     1 
ATOM   11081 O  O     . GLY   B  1 336  ? -3.488  4.496   113.006 1.00 25.36 ? 334  GLY   B O     1 
ATOM   11082 N  N     . MET   B  1 337  ? -2.980  2.627   111.872 1.00 27.58 ? 335  MET   B N     1 
ATOM   11083 C  CA    . MET   B  1 337  ? -2.432  3.374   110.746 1.00 27.26 ? 335  MET   B CA    1 
ATOM   11084 C  C     . MET   B  1 337  ? -3.559  4.132   110.059 1.00 28.68 ? 335  MET   B C     1 
ATOM   11085 O  O     . MET   B  1 337  ? -4.525  3.521   109.591 1.00 26.56 ? 335  MET   B O     1 
ATOM   11086 C  CB    . MET   B  1 337  ? -1.735  2.428   109.769 1.00 27.55 ? 335  MET   B CB    1 
ATOM   11087 C  CG    . MET   B  1 337  ? -1.085  3.111   108.578 1.00 33.11 ? 335  MET   B CG    1 
ATOM   11088 S  SD    . MET   B  1 337  ? 0.249   4.255   109.002 1.00 42.93 ? 335  MET   B SD    1 
ATOM   11089 C  CE    . MET   B  1 337  ? 1.567   3.153   109.465 1.00 38.83 ? 335  MET   B CE    1 
ATOM   11090 N  N     . GLY   B  1 338  ? -3.442  5.458   110.008 1.00 24.44 ? 336  GLY   B N     1 
ATOM   11091 C  CA    . GLY   B  1 338  ? -4.467  6.306   109.427 1.00 22.93 ? 336  GLY   B CA    1 
ATOM   11092 C  C     . GLY   B  1 338  ? -3.967  7.062   108.210 1.00 25.84 ? 336  GLY   B C     1 
ATOM   11093 O  O     . GLY   B  1 338  ? -2.776  7.366   108.094 1.00 25.75 ? 336  GLY   B O     1 
ATOM   11094 N  N     . PHE   B  1 339  ? -4.895  7.377   107.301 1.00 24.29 ? 337  PHE   B N     1 
ATOM   11095 C  CA    . PHE   B  1 339  ? -4.529  8.014   106.043 1.00 21.84 ? 337  PHE   B CA    1 
ATOM   11096 C  C     . PHE   B  1 339  ? -5.631  8.959   105.587 1.00 20.76 ? 337  PHE   B C     1 
ATOM   11097 O  O     . PHE   B  1 339  ? -6.797  8.567   105.511 1.00 24.03 ? 337  PHE   B O     1 
ATOM   11098 C  CB    . PHE   B  1 339  ? -4.265  6.957   104.969 1.00 24.04 ? 337  PHE   B CB    1 
ATOM   11099 C  CG    . PHE   B  1 339  ? -3.511  7.476   103.783 1.00 23.35 ? 337  PHE   B CG    1 
ATOM   11100 C  CD1   . PHE   B  1 339  ? -2.132  7.594   103.816 1.00 23.66 ? 337  PHE   B CD1   1 
ATOM   11101 C  CD2   . PHE   B  1 339  ? -4.181  7.841   102.635 1.00 23.11 ? 337  PHE   B CD2   1 
ATOM   11102 C  CE1   . PHE   B  1 339  ? -1.439  8.065   102.702 1.00 26.06 ? 337  PHE   B CE1   1 
ATOM   11103 C  CE2   . PHE   B  1 339  ? -3.497  8.315   101.529 1.00 23.51 ? 337  PHE   B CE2   1 
ATOM   11104 C  CZ    . PHE   B  1 339  ? -2.126  8.426   101.567 1.00 24.75 ? 337  PHE   B CZ    1 
ATOM   11105 N  N     . VAL   B  1 340  ? -5.257  10.187  105.260 1.00 21.60 ? 338  VAL   B N     1 
ATOM   11106 C  CA    . VAL   B  1 340  ? -6.208  11.194  104.802 1.00 20.89 ? 338  VAL   B CA    1 
ATOM   11107 C  C     . VAL   B  1 340  ? -6.378  11.084  103.294 1.00 21.16 ? 338  VAL   B C     1 
ATOM   11108 O  O     . VAL   B  1 340  ? -5.401  10.914  102.557 1.00 21.72 ? 338  VAL   B O     1 
ATOM   11109 C  CB    . VAL   B  1 340  ? -5.731  12.608  105.184 1.00 19.97 ? 338  VAL   B CB    1 
ATOM   11110 C  CG1   . VAL   B  1 340  ? -6.689  13.647  104.613 1.00 21.65 ? 338  VAL   B CG1   1 
ATOM   11111 C  CG2   . VAL   B  1 340  ? -5.623  12.744  106.702 1.00 19.49 ? 338  VAL   B CG2   1 
ATOM   11112 N  N     . VAL   B  1 341  ? -7.617  11.202  102.829 1.00 20.29 ? 339  VAL   B N     1 
ATOM   11113 C  CA    . VAL   B  1 341  ? -7.908  11.365  101.409 1.00 19.56 ? 339  VAL   B CA    1 
ATOM   11114 C  C     . VAL   B  1 341  ? -8.759  12.615  101.236 1.00 19.72 ? 339  VAL   B C     1 
ATOM   11115 O  O     . VAL   B  1 341  ? -9.687  12.862  102.014 1.00 21.46 ? 339  VAL   B O     1 
ATOM   11116 C  CB    . VAL   B  1 341  ? -8.608  10.123  100.820 1.00 22.03 ? 339  VAL   B CB    1 
ATOM   11117 C  CG1   . VAL   B  1 341  ? -7.708  8.915   100.971 1.00 24.08 ? 339  VAL   B CG1   1 
ATOM   11118 C  CG2   . VAL   B  1 341  ? -9.943  9.870   101.520 1.00 30.38 ? 339  VAL   B CG2   1 
ATOM   11119 N  N     . GLN   B  1 342  ? -8.438  13.397  100.211 1.00 19.36 ? 340  GLN   B N     1 
ATOM   11120 C  CA    . GLN   B  1 342  ? -9.037  14.712  99.992  1.00 19.58 ? 340  GLN   B CA    1 
ATOM   11121 C  C     . GLN   B  1 342  ? -10.112 14.618  98.919  1.00 21.63 ? 340  GLN   B C     1 
ATOM   11122 O  O     . GLN   B  1 342  ? -9.806  14.400  97.740  1.00 19.06 ? 340  GLN   B O     1 
ATOM   11123 C  CB    . GLN   B  1 342  ? -7.965  15.723  99.600  1.00 19.02 ? 340  GLN   B CB    1 
ATOM   11124 C  CG    . GLN   B  1 342  ? -6.918  15.924  100.685 1.00 18.31 ? 340  GLN   B CG    1 
ATOM   11125 C  CD    . GLN   B  1 342  ? -5.556  16.259  100.093 1.00 18.29 ? 340  GLN   B CD    1 
ATOM   11126 O  OE1   . GLN   B  1 342  ? -5.110  15.605  99.155  1.00 18.73 ? 340  GLN   B OE1   1 
ATOM   11127 N  NE2   . GLN   B  1 342  ? -4.897  17.277  100.635 1.00 18.46 ? 340  GLN   B NE2   1 
ATOM   11128 N  N     . ALA   B  1 343  ? -11.364 14.813  99.331  1.00 19.80 ? 341  ALA   B N     1 
ATOM   11129 C  CA    . ALA   B  1 343  ? -12.497 14.713  98.413  1.00 21.15 ? 341  ALA   B CA    1 
ATOM   11130 C  C     . ALA   B  1 343  ? -12.529 15.844  97.392  1.00 19.29 ? 341  ALA   B C     1 
ATOM   11131 O  O     . ALA   B  1 343  ? -13.230 15.720  96.376  1.00 19.94 ? 341  ALA   B O     1 
ATOM   11132 C  CB    . ALA   B  1 343  ? -13.805 14.687  99.205  1.00 20.62 ? 341  ALA   B CB    1 
ATOM   11133 N  N     . TYR   B  1 344  ? -11.809 16.950  97.630  1.00 19.88 ? 342  TYR   B N     1 
ATOM   11134 C  CA    . TYR   B  1 344  ? -11.764 17.911  96.534  1.00 20.53 ? 342  TYR   B CA    1 
ATOM   11135 C  C     . TYR   B  1 344  ? -10.873 17.439  95.404  1.00 18.80 ? 342  TYR   B C     1 
ATOM   11136 O  O     . TYR   B  1 344  ? -10.787 18.123  94.385  1.00 21.29 ? 342  TYR   B O     1 
ATOM   11137 C  CB    . TYR   B  1 344  ? -11.338 19.316  97.013  1.00 19.15 ? 342  TYR   B CB    1 
ATOM   11138 C  CG    . TYR   B  1 344  ? -9.887  19.593  97.418  1.00 20.10 ? 342  TYR   B CG    1 
ATOM   11139 C  CD1   . TYR   B  1 344  ? -8.908  18.599  97.443  1.00 18.82 ? 342  TYR   B CD1   1 
ATOM   11140 C  CD2   . TYR   B  1 344  ? -9.512  20.879  97.803  1.00 18.19 ? 342  TYR   B CD2   1 
ATOM   11141 C  CE1   . TYR   B  1 344  ? -7.597  18.888  97.840  1.00 19.21 ? 342  TYR   B CE1   1 
ATOM   11142 C  CE2   . TYR   B  1 344  ? -8.207  21.180  98.190  1.00 20.43 ? 342  TYR   B CE2   1 
ATOM   11143 C  CZ    . TYR   B  1 344  ? -7.259  20.182  98.202  1.00 20.70 ? 342  TYR   B CZ    1 
ATOM   11144 O  OH    . TYR   B  1 344  ? -5.984  20.476  98.591  1.00 19.13 ? 342  TYR   B OH    1 
ATOM   11145 N  N     . GLY   B  1 345  ? -10.215 16.293  95.563  1.00 20.03 ? 343  GLY   B N     1 
ATOM   11146 C  CA    . GLY   B  1 345  ? -9.318  15.787  94.546  1.00 19.36 ? 343  GLY   B CA    1 
ATOM   11147 C  C     . GLY   B  1 345  ? -10.025 14.802  93.633  1.00 18.99 ? 343  GLY   B C     1 
ATOM   11148 O  O     . GLY   B  1 345  ? -10.820 13.978  94.078  1.00 20.10 ? 343  GLY   B O     1 
ATOM   11149 N  N     . LYS   B  1 346  ? -9.711  14.902  92.345  1.00 16.51 ? 344  LYS   B N     1 
ATOM   11150 C  CA    . LYS   B  1 346  ? -10.357 14.083  91.340  1.00 18.69 ? 344  LYS   B CA    1 
ATOM   11151 C  C     . LYS   B  1 346  ? -10.008 12.613  91.478  1.00 19.37 ? 344  LYS   B C     1 
ATOM   11152 O  O     . LYS   B  1 346  ? -10.753 11.764  90.982  1.00 22.88 ? 344  LYS   B O     1 
ATOM   11153 C  CB    . LYS   B  1 346  ? -9.968  14.594  89.956  1.00 17.94 ? 344  LYS   B CB    1 
ATOM   11154 C  CG    . LYS   B  1 346  ? -10.485 15.995  89.669  1.00 20.98 ? 344  LYS   B CG    1 
ATOM   11155 C  CD    . LYS   B  1 346  ? -9.947  16.514  88.329  1.00 20.48 ? 344  LYS   B CD    1 
ATOM   11156 C  CE    . LYS   B  1 346  ? -10.616 17.814  87.927  1.00 21.08 ? 344  LYS   B CE    1 
ATOM   11157 N  NZ    . LYS   B  1 346  ? -9.936  18.391  86.724  1.00 18.60 ? 344  LYS   B NZ    1 
ATOM   11158 N  N     . ARG   B  1 347  ? -8.897  12.291  92.129  1.00 19.70 ? 345  ARG   B N     1 
ATOM   11159 C  CA    . ARG   B  1 347  ? -8.504  10.900  92.267  1.00 22.69 ? 345  ARG   B CA    1 
ATOM   11160 C  C     . ARG   B  1 347  ? -9.131  10.218  93.476  1.00 22.22 ? 345  ARG   B C     1 
ATOM   11161 O  O     . ARG   B  1 347  ? -8.976  9.001   93.619  1.00 21.36 ? 345  ARG   B O     1 
ATOM   11162 C  CB    . ARG   B  1 347  ? -6.983  10.807  92.341  1.00 19.35 ? 345  ARG   B CB    1 
ATOM   11163 C  CG    . ARG   B  1 347  ? -6.329  11.254  91.052  1.00 18.36 ? 345  ARG   B CG    1 
ATOM   11164 C  CD    . ARG   B  1 347  ? -4.847  11.500  91.254  1.00 20.76 ? 345  ARG   B CD    1 
ATOM   11165 N  NE    . ARG   B  1 347  ? -4.586  12.728  91.994  1.00 21.14 ? 345  ARG   B NE    1 
ATOM   11166 C  CZ    . ARG   B  1 347  ? -3.395  13.059  92.467  1.00 20.34 ? 345  ARG   B CZ    1 
ATOM   11167 N  NH1   . ARG   B  1 347  ? -2.348  12.265  92.300  1.00 16.62 ? 345  ARG   B NH1   1 
ATOM   11168 N  NH2   . ARG   B  1 347  ? -3.251  14.214  93.118  1.00 15.77 ? 345  ARG   B NH2   1 
ATOM   11169 N  N     . CYS   B  1 348  ? -9.840  10.968  94.322  1.00 21.11 ? 346  CYS   B N     1 
ATOM   11170 C  CA    . CYS   B  1 348  ? -10.279 10.474  95.630  1.00 22.45 ? 346  CYS   B CA    1 
ATOM   11171 C  C     . CYS   B  1 348  ? -10.978 9.121   95.593  1.00 23.50 ? 346  CYS   B C     1 
ATOM   11172 O  O     . CYS   B  1 348  ? -10.594 8.238   96.376  1.00 23.32 ? 346  CYS   B O     1 
ATOM   11173 C  CB    . CYS   B  1 348  ? -11.185 11.518  96.302  1.00 21.28 ? 346  CYS   B CB    1 
ATOM   11174 S  SG    . CYS   B  1 348  ? -11.435 11.212  98.090  1.00 27.79 ? 346  CYS   B SG    1 
ATOM   11175 N  N     . PRO   B  1 349  ? -11.993 8.877   94.755  1.00 23.42 ? 347  PRO   B N     1 
ATOM   11176 C  CA    . PRO   B  1 349  ? -12.629 7.552   94.812  1.00 22.64 ? 347  PRO   B CA    1 
ATOM   11177 C  C     . PRO   B  1 349  ? -11.679 6.449   94.405  1.00 24.77 ? 347  PRO   B C     1 
ATOM   11178 O  O     . PRO   B  1 349  ? -11.741 5.346   94.970  1.00 23.35 ? 347  PRO   B O     1 
ATOM   11179 C  CB    . PRO   B  1 349  ? -13.824 7.680   93.853  1.00 23.85 ? 347  PRO   B CB    1 
ATOM   11180 C  CG    . PRO   B  1 349  ? -13.478 8.811   92.957  1.00 23.64 ? 347  PRO   B CG    1 
ATOM   11181 C  CD    . PRO   B  1 349  ? -12.617 9.750   93.744  1.00 21.53 ? 347  PRO   B CD    1 
ATOM   11182 N  N     . PHE   B  1 350  ? -10.776 6.738   93.461  1.00 20.73 ? 348  PHE   B N     1 
ATOM   11183 C  CA    . PHE   B  1 350  ? -9.806  5.746   93.017  1.00 23.89 ? 348  PHE   B CA    1 
ATOM   11184 C  C     . PHE   B  1 350  ? -8.745  5.508   94.077  1.00 22.38 ? 348  PHE   B C     1 
ATOM   11185 O  O     . PHE   B  1 350  ? -8.277  4.374   94.255  1.00 21.01 ? 348  PHE   B O     1 
ATOM   11186 C  CB    . PHE   B  1 350  ? -9.196  6.202   91.697  1.00 22.58 ? 348  PHE   B CB    1 
ATOM   11187 C  CG    . PHE   B  1 350  ? -10.231 6.602   90.702  1.00 23.28 ? 348  PHE   B CG    1 
ATOM   11188 C  CD1   . PHE   B  1 350  ? -10.932 5.638   90.000  1.00 27.63 ? 348  PHE   B CD1   1 
ATOM   11189 C  CD2   . PHE   B  1 350  ? -10.559 7.938   90.518  1.00 24.85 ? 348  PHE   B CD2   1 
ATOM   11190 C  CE1   . PHE   B  1 350  ? -11.916 5.995   89.101  1.00 28.06 ? 348  PHE   B CE1   1 
ATOM   11191 C  CE2   . PHE   B  1 350  ? -11.554 8.301   89.614  1.00 25.34 ? 348  PHE   B CE2   1 
ATOM   11192 C  CZ    . PHE   B  1 350  ? -12.226 7.326   88.908  1.00 26.22 ? 348  PHE   B CZ    1 
ATOM   11193 N  N     . VAL   B  1 351  ? -8.370  6.561   94.805  1.00 24.20 ? 349  VAL   B N     1 
ATOM   11194 C  CA    . VAL   B  1 351  ? -7.475  6.391   95.942  1.00 21.72 ? 349  VAL   B CA    1 
ATOM   11195 C  C     . VAL   B  1 351  ? -8.141  5.539   97.016  1.00 22.90 ? 349  VAL   B C     1 
ATOM   11196 O  O     . VAL   B  1 351  ? -7.509  4.660   97.613  1.00 22.77 ? 349  VAL   B O     1 
ATOM   11197 C  CB    . VAL   B  1 351  ? -7.036  7.760   96.495  1.00 23.75 ? 349  VAL   B CB    1 
ATOM   11198 C  CG1   . VAL   B  1 351  ? -6.162  7.579   97.756  1.00 21.17 ? 349  VAL   B CG1   1 
ATOM   11199 C  CG2   . VAL   B  1 351  ? -6.286  8.557   95.417  1.00 18.96 ? 349  VAL   B CG2   1 
ATOM   11200 N  N     . LEU   B  1 352  ? -9.426  5.774   97.274  1.00 20.67 ? 350  LEU   B N     1 
ATOM   11201 C  CA    . LEU   B  1 352  ? -10.134 4.936   98.236  1.00 24.39 ? 350  LEU   B CA    1 
ATOM   11202 C  C     . LEU   B  1 352  ? -10.203 3.482   97.772  1.00 26.76 ? 350  LEU   B C     1 
ATOM   11203 O  O     . LEU   B  1 352  ? -10.030 2.560   98.580  1.00 24.38 ? 350  LEU   B O     1 
ATOM   11204 C  CB    . LEU   B  1 352  ? -11.537 5.487   98.484  1.00 23.81 ? 350  LEU   B CB    1 
ATOM   11205 C  CG    . LEU   B  1 352  ? -11.582 6.805   99.255  1.00 22.54 ? 350  LEU   B CG    1 
ATOM   11206 C  CD1   . LEU   B  1 352  ? -12.996 7.310   99.289  1.00 24.55 ? 350  LEU   B CD1   1 
ATOM   11207 C  CD2   . LEU   B  1 352  ? -11.070 6.588   100.658 1.00 25.94 ? 350  LEU   B CD2   1 
ATOM   11208 N  N     . ASP   B  1 353  ? -10.480 3.254   96.483  1.00 23.92 ? 351  ASP   B N     1 
ATOM   11209 C  CA    . ASP   B  1 353  ? -10.396 1.902   95.933  1.00 26.61 ? 351  ASP   B CA    1 
ATOM   11210 C  C     . ASP   B  1 353  ? -9.058  1.259   96.280  1.00 27.76 ? 351  ASP   B C     1 
ATOM   11211 O  O     . ASP   B  1 353  ? -9.000  0.113   96.750  1.00 26.05 ? 351  ASP   B O     1 
ATOM   11212 C  CB    . ASP   B  1 353  ? -10.581 1.936   94.413  1.00 24.66 ? 351  ASP   B CB    1 
ATOM   11213 C  CG    . ASP   B  1 353  ? -12.016 2.163   94.000  1.00 31.29 ? 351  ASP   B CG    1 
ATOM   11214 O  OD1   . ASP   B  1 353  ? -12.928 1.934   94.824  1.00 31.19 ? 351  ASP   B OD1   1 
ATOM   11215 O  OD2   . ASP   B  1 353  ? -12.227 2.562   92.835  1.00 33.35 ? 351  ASP   B OD2   1 
ATOM   11216 N  N     . PHE   B  1 354  ? -7.966  1.997   96.058  1.00 23.56 ? 352  PHE   B N     1 
ATOM   11217 C  CA    . PHE   B  1 354  ? -6.638  1.468   96.345  1.00 26.65 ? 352  PHE   B CA    1 
ATOM   11218 C  C     . PHE   B  1 354  ? -6.466  1.171   97.829  1.00 27.62 ? 352  PHE   B C     1 
ATOM   11219 O  O     . PHE   B  1 354  ? -5.930  0.119   98.194  1.00 25.09 ? 352  PHE   B O     1 
ATOM   11220 C  CB    . PHE   B  1 354  ? -5.554  2.443   95.869  1.00 24.90 ? 352  PHE   B CB    1 
ATOM   11221 C  CG    . PHE   B  1 354  ? -4.184  2.109   96.393  1.00 25.58 ? 352  PHE   B CG    1 
ATOM   11222 C  CD1   . PHE   B  1 354  ? -3.395  1.175   95.748  1.00 27.02 ? 352  PHE   B CD1   1 
ATOM   11223 C  CD2   . PHE   B  1 354  ? -3.707  2.693   97.563  1.00 25.00 ? 352  PHE   B CD2   1 
ATOM   11224 C  CE1   . PHE   B  1 354  ? -2.153  0.834   96.248  1.00 25.92 ? 352  PHE   B CE1   1 
ATOM   11225 C  CE2   . PHE   B  1 354  ? -2.468  2.359   98.068  1.00 25.56 ? 352  PHE   B CE2   1 
ATOM   11226 C  CZ    . PHE   B  1 354  ? -1.680  1.439   97.407  1.00 27.66 ? 352  PHE   B CZ    1 
ATOM   11227 N  N     . ILE   B  1 355  ? -6.908  2.088   98.699  1.00 24.38 ? 353  ILE   B N     1 
ATOM   11228 C  CA    . ILE   B  1 355  ? -6.713  1.910   100.137 1.00 23.74 ? 353  ILE   B CA    1 
ATOM   11229 C  C     . ILE   B  1 355  ? -7.561  0.761   100.653 1.00 27.36 ? 353  ILE   B C     1 
ATOM   11230 O  O     . ILE   B  1 355  ? -7.100  -0.053  101.461 1.00 25.02 ? 353  ILE   B O     1 
ATOM   11231 C  CB    . ILE   B  1 355  ? -7.022  3.215   100.897 1.00 23.16 ? 353  ILE   B CB    1 
ATOM   11232 C  CG1   . ILE   B  1 355  ? -6.036  4.311   100.492 1.00 25.21 ? 353  ILE   B CG1   1 
ATOM   11233 C  CG2   . ILE   B  1 355  ? -6.974  2.987   102.409 1.00 24.69 ? 353  ILE   B CG2   1 
ATOM   11234 C  CD1   . ILE   B  1 355  ? -6.393  5.666   101.042 1.00 24.63 ? 353  ILE   B CD1   1 
ATOM   11235 N  N     . ILE   B  1 356  ? -8.813  0.675   100.198 1.00 24.95 ? 354  ILE   B N     1 
ATOM   11236 C  CA    . ILE   B  1 356  ? -9.670  -0.421  100.638 1.00 28.39 ? 354  ILE   B CA    1 
ATOM   11237 C  C     . ILE   B  1 356  ? -9.077  -1.750  100.207 1.00 27.35 ? 354  ILE   B C     1 
ATOM   11238 O  O     . ILE   B  1 356  ? -9.048  -2.717  100.977 1.00 29.50 ? 354  ILE   B O     1 
ATOM   11239 C  CB    . ILE   B  1 356  ? -11.096 -0.233  100.094 1.00 25.79 ? 354  ILE   B CB    1 
ATOM   11240 C  CG1   . ILE   B  1 356  ? -11.765 0.960   100.771 1.00 23.63 ? 354  ILE   B CG1   1 
ATOM   11241 C  CG2   . ILE   B  1 356  ? -11.913 -1.509  100.287 1.00 28.50 ? 354  ILE   B CG2   1 
ATOM   11242 C  CD1   . ILE   B  1 356  ? -13.057 1.405   100.098 1.00 25.94 ? 354  ILE   B CD1   1 
ATOM   11243 N  N     . ASP   B  1 357  ? -8.579  -1.815  98.974  1.00 26.08 ? 355  ASP   B N     1 
ATOM   11244 C  CA    . ASP   B  1 357  ? -7.928  -3.035  98.521  1.00 29.60 ? 355  ASP   B CA    1 
ATOM   11245 C  C     . ASP   B  1 357  ? -6.659  -3.314  99.315  1.00 28.34 ? 355  ASP   B C     1 
ATOM   11246 O  O     . ASP   B  1 357  ? -6.386  -4.464  99.668  1.00 26.43 ? 355  ASP   B O     1 
ATOM   11247 C  CB    . ASP   B  1 357  ? -7.610  -2.946  97.038  1.00 29.25 ? 355  ASP   B CB    1 
ATOM   11248 C  CG    . ASP   B  1 357  ? -6.778  -4.111  96.558  1.00 30.23 ? 355  ASP   B CG    1 
ATOM   11249 O  OD1   . ASP   B  1 357  ? -7.346  -5.207  96.370  1.00 33.16 ? 355  ASP   B OD1   1 
ATOM   11250 O  OD2   . ASP   B  1 357  ? -5.556  -3.932  96.373  1.00 31.36 ? 355  ASP   B OD2   1 
ATOM   11251 N  N     . LEU   B  1 358  ? -5.859  -2.279  99.587  1.00 28.15 ? 356  LEU   B N     1 
ATOM   11252 C  CA    . LEU   B  1 358  ? -4.651  -2.483  100.382 1.00 26.89 ? 356  LEU   B CA    1 
ATOM   11253 C  C     . LEU   B  1 358  ? -4.992  -3.015  101.765 1.00 27.01 ? 356  LEU   B C     1 
ATOM   11254 O  O     . LEU   B  1 358  ? -4.320  -3.919  102.273 1.00 28.58 ? 356  LEU   B O     1 
ATOM   11255 C  CB    . LEU   B  1 358  ? -3.857  -1.178  100.481 1.00 27.59 ? 356  LEU   B CB    1 
ATOM   11256 C  CG    . LEU   B  1 358  ? -2.674  -1.143  101.467 1.00 27.81 ? 356  LEU   B CG    1 
ATOM   11257 C  CD1   . LEU   B  1 358  ? -1.637  -2.202  101.143 1.00 28.67 ? 356  LEU   B CD1   1 
ATOM   11258 C  CD2   . LEU   B  1 358  ? -2.020  0.239   101.456 1.00 26.98 ? 356  LEU   B CD2   1 
ATOM   11259 N  N     . ALA   B  1 359  ? -6.052  -2.486  102.380 1.00 25.66 ? 357  ALA   B N     1 
ATOM   11260 C  CA    . ALA   B  1 359  ? -6.469  -2.974  103.685 1.00 27.75 ? 357  ALA   B CA    1 
ATOM   11261 C  C     . ALA   B  1 359  ? -6.870  -4.439  103.613 1.00 30.95 ? 357  ALA   B C     1 
ATOM   11262 O  O     . ALA   B  1 359  ? -6.500  -5.239  104.479 1.00 30.78 ? 357  ALA   B O     1 
ATOM   11263 C  CB    . ALA   B  1 359  ? -7.626  -2.126  104.213 1.00 28.57 ? 357  ALA   B CB    1 
ATOM   11264 N  N     . ARG   B  1 360  ? -7.606  -4.811  102.564 1.00 32.28 ? 358  ARG   B N     1 
ATOM   11265 C  CA    . ARG   B  1 360  ? -8.062  -6.190  102.425 1.00 35.67 ? 358  ARG   B CA    1 
ATOM   11266 C  C     . ARG   B  1 360  ? -6.890  -7.153  102.309 1.00 29.27 ? 358  ARG   B C     1 
ATOM   11267 O  O     . ARG   B  1 360  ? -6.872  -8.202  102.957 1.00 35.34 ? 358  ARG   B O     1 
ATOM   11268 C  CB    . ARG   B  1 360  ? -8.979  -6.308  101.211 1.00 31.38 ? 358  ARG   B CB    1 
ATOM   11269 C  CG    . ARG   B  1 360  ? -10.347 -5.753  101.473 1.00 33.44 ? 358  ARG   B CG    1 
ATOM   11270 C  CD    . ARG   B  1 360  ? -11.175 -5.667  100.207 1.00 39.94 ? 358  ARG   B CD    1 
ATOM   11271 N  NE    . ARG   B  1 360  ? -12.561 -5.356  100.529 1.00 37.84 ? 358  ARG   B NE    1 
ATOM   11272 C  CZ    . ARG   B  1 360  ? -13.392 -4.721  99.717  1.00 38.39 ? 358  ARG   B CZ    1 
ATOM   11273 N  NH1   . ARG   B  1 360  ? -13.007 -4.307  98.522  1.00 44.04 ? 358  ARG   B NH1   1 
ATOM   11274 N  NH2   . ARG   B  1 360  ? -14.643 -4.495  100.113 1.00 50.76 ? 358  ARG   B NH2   1 
ATOM   11275 N  N     . ARG   B  1 361  ? -5.893  -6.814  101.494 1.00 30.64 ? 359  ARG   B N     1 
ATOM   11276 C  CA    . ARG   B  1 361  ? -4.812  -7.765  101.295 1.00 35.55 ? 359  ARG   B CA    1 
ATOM   11277 C  C     . ARG   B  1 361  ? -3.776  -7.720  102.403 1.00 35.82 ? 359  ARG   B C     1 
ATOM   11278 O  O     . ARG   B  1 361  ? -3.044  -8.700  102.580 1.00 33.60 ? 359  ARG   B O     1 
ATOM   11279 C  CB    . ARG   B  1 361  ? -4.140  -7.546  99.942  1.00 36.49 ? 359  ARG   B CB    1 
ATOM   11280 C  CG    . ARG   B  1 361  ? -3.677  -6.151  99.659  1.00 37.18 ? 359  ARG   B CG    1 
ATOM   11281 C  CD    . ARG   B  1 361  ? -3.414  -6.003  98.159  1.00 32.54 ? 359  ARG   B CD    1 
ATOM   11282 N  NE    . ARG   B  1 361  ? -3.155  -4.616  97.789  1.00 31.27 ? 359  ARG   B NE    1 
ATOM   11283 C  CZ    . ARG   B  1 361  ? -1.964  -4.036  97.816  1.00 29.06 ? 359  ARG   B CZ    1 
ATOM   11284 N  NH1   . ARG   B  1 361  ? -0.880  -4.697  98.195  1.00 27.22 ? 359  ARG   B NH1   1 
ATOM   11285 N  NH2   . ARG   B  1 361  ? -1.858  -2.758  97.460  1.00 27.12 ? 359  ARG   B NH2   1 
ATOM   11286 N  N     . SER   B  1 362  ? -3.706  -6.626  103.159 1.00 33.82 ? 360  SER   B N     1 
ATOM   11287 C  CA    . SER   B  1 362  ? -2.724  -6.520  104.227 1.00 31.68 ? 360  SER   B CA    1 
ATOM   11288 C  C     . SER   B  1 362  ? -3.256  -6.945  105.588 1.00 30.66 ? 360  SER   B C     1 
ATOM   11289 O  O     . SER   B  1 362  ? -2.463  -7.064  106.529 1.00 32.62 ? 360  SER   B O     1 
ATOM   11290 C  CB    . SER   B  1 362  ? -2.194  -5.087  104.328 1.00 30.25 ? 360  SER   B CB    1 
ATOM   11291 O  OG    . SER   B  1 362  ? -3.236  -4.202  104.686 1.00 28.30 ? 360  SER   B OG    1 
ATOM   11292 N  N     . GLY   B  1 363  ? -4.561  -7.170  105.731 1.00 27.34 ? 361  GLY   B N     1 
ATOM   11293 C  CA    . GLY   B  1 363  ? -5.084  -7.526  107.041 1.00 28.56 ? 361  GLY   B CA    1 
ATOM   11294 C  C     . GLY   B  1 363  ? -4.972  -6.401  108.049 1.00 28.85 ? 361  GLY   B C     1 
ATOM   11295 O  O     . GLY   B  1 363  ? -4.846  -6.652  109.253 1.00 33.15 ? 361  GLY   B O     1 
ATOM   11296 N  N     . ARG   B  1 364  ? -5.007  -5.166  107.574 1.00 31.36 ? 362  ARG   B N     1 
ATOM   11297 C  CA    . ARG   B  1 364  ? -4.984  -3.965  108.394 1.00 33.84 ? 362  ARG   B CA    1 
ATOM   11298 C  C     . ARG   B  1 364  ? -6.305  -3.246  108.187 1.00 32.34 ? 362  ARG   B C     1 
ATOM   11299 O  O     . ARG   B  1 364  ? -6.687  -2.979  107.047 1.00 32.39 ? 362  ARG   B O     1 
ATOM   11300 C  CB    . ARG   B  1 364  ? -3.842  -3.027  107.983 1.00 30.11 ? 362  ARG   B CB    1 
ATOM   11301 C  CG    . ARG   B  1 364  ? -2.456  -3.621  108.021 1.00 32.30 ? 362  ARG   B CG    1 
ATOM   11302 C  CD    . ARG   B  1 364  ? -1.899  -3.668  109.449 1.00 34.29 ? 362  ARG   B CD    1 
ATOM   11303 N  NE    . ARG   B  1 364  ? -0.679  -4.463  109.498 1.00 30.80 ? 362  ARG   B NE    1 
ATOM   11304 C  CZ    . ARG   B  1 364  ? 0.537   -3.991  109.260 1.00 31.58 ? 362  ARG   B CZ    1 
ATOM   11305 N  NH1   . ARG   B  1 364  ? 0.746   -2.707  109.009 1.00 30.16 ? 362  ARG   B NH1   1 
ATOM   11306 N  NH2   . ARG   B  1 364  ? 1.568   -4.832  109.259 1.00 33.34 ? 362  ARG   B NH2   1 
ATOM   11307 N  N     . ARG   B  1 365  ? -6.996  -2.917  109.265 1.00 30.19 ? 363  ARG   B N     1 
ATOM   11308 C  CA    . ARG   B  1 365  ? -8.142  -2.028  109.115 1.00 28.96 ? 363  ARG   B CA    1 
ATOM   11309 C  C     . ARG   B  1 365  ? -7.595  -0.608  109.083 1.00 27.54 ? 363  ARG   B C     1 
ATOM   11310 O  O     . ARG   B  1 365  ? -7.196  -0.058  110.108 1.00 29.54 ? 363  ARG   B O     1 
ATOM   11311 C  CB    . ARG   B  1 365  ? -9.152  -2.225  110.234 1.00 34.30 ? 363  ARG   B CB    1 
ATOM   11312 C  CG    . ARG   B  1 365  ? -10.370 -1.334  110.090 1.00 31.33 ? 363  ARG   B CG    1 
ATOM   11313 C  CD    . ARG   B  1 365  ? -11.544 -1.884  110.894 1.00 39.60 ? 363  ARG   B CD    1 
ATOM   11314 N  NE    . ARG   B  1 365  ? -12.784 -1.174  110.598 1.00 37.12 ? 363  ARG   B NE    1 
ATOM   11315 C  CZ    . ARG   B  1 365  ? -13.436 -0.412  111.464 1.00 38.63 ? 363  ARG   B CZ    1 
ATOM   11316 N  NH1   . ARG   B  1 365  ? -13.017 -0.268  112.711 1.00 37.44 ? 363  ARG   B NH1   1 
ATOM   11317 N  NH2   . ARG   B  1 365  ? -14.547 0.209   111.073 1.00 35.43 ? 363  ARG   B NH2   1 
ATOM   11318 N  N     . ILE   B  1 366  ? -7.528  -0.025  107.896 1.00 29.81 ? 364  ILE   B N     1 
ATOM   11319 C  CA    . ILE   B  1 366  ? -6.905  1.282   107.746 1.00 28.07 ? 364  ILE   B CA    1 
ATOM   11320 C  C     . ILE   B  1 366  ? -7.898  2.350   108.175 1.00 28.31 ? 364  ILE   B C     1 
ATOM   11321 O  O     . ILE   B  1 366  ? -9.072  2.320   107.782 1.00 28.90 ? 364  ILE   B O     1 
ATOM   11322 C  CB    . ILE   B  1 366  ? -6.430  1.497   106.301 1.00 22.98 ? 364  ILE   B CB    1 
ATOM   11323 C  CG1   . ILE   B  1 366  ? -5.344  0.478   105.957 1.00 27.89 ? 364  ILE   B CG1   1 
ATOM   11324 C  CG2   . ILE   B  1 366  ? -5.922  2.919   106.106 1.00 23.39 ? 364  ILE   B CG2   1 
ATOM   11325 C  CD1   . ILE   B  1 366  ? -4.949  0.445   104.488 1.00 29.38 ? 364  ILE   B CD1   1 
ATOM   11326 N  N     . MET   B  1 367  ? -7.440  3.288   109.002 1.00 26.78 ? 365  MET   B N     1 
ATOM   11327 C  CA    . MET   B  1 367  ? -8.266  4.435   109.357 1.00 25.54 ? 365  MET   B CA    1 
ATOM   11328 C  C     . MET   B  1 367  ? -8.167  5.450   108.232 1.00 24.47 ? 365  MET   B C     1 
ATOM   11329 O  O     . MET   B  1 367  ? -7.065  5.844   107.842 1.00 24.38 ? 365  MET   B O     1 
ATOM   11330 C  CB    . MET   B  1 367  ? -7.825  5.040   110.688 1.00 23.20 ? 365  MET   B CB    1 
ATOM   11331 C  CG    . MET   B  1 367  ? -7.656  4.008   111.780 1.00 29.68 ? 365  MET   B CG    1 
ATOM   11332 S  SD    . MET   B  1 367  ? -7.000  4.674   113.316 1.00 32.61 ? 365  MET   B SD    1 
ATOM   11333 C  CE    . MET   B  1 367  ? -8.408  5.503   114.040 1.00 33.61 ? 365  MET   B CE    1 
ATOM   11334 N  N     . VAL   B  1 368  ? -9.306  5.839   107.672 1.00 22.20 ? 366  VAL   B N     1 
ATOM   11335 C  CA    . VAL   B  1 368  ? -9.322  6.717   106.511 1.00 21.42 ? 366  VAL   B CA    1 
ATOM   11336 C  C     . VAL   B  1 368  ? -10.043 7.987   106.911 1.00 24.41 ? 366  VAL   B C     1 
ATOM   11337 O  O     . VAL   B  1 368  ? -11.255 7.972   107.157 1.00 26.35 ? 366  VAL   B O     1 
ATOM   11338 C  CB    . VAL   B  1 368  ? -9.989  6.071   105.290 1.00 22.11 ? 366  VAL   B CB    1 
ATOM   11339 C  CG1   . VAL   B  1 368  ? -9.852  6.993   104.093 1.00 25.66 ? 366  VAL   B CG1   1 
ATOM   11340 C  CG2   . VAL   B  1 368  ? -9.361  4.720   105.001 1.00 28.22 ? 366  VAL   B CG2   1 
ATOM   11341 N  N     . ARG   B  1 369  ? -9.314  9.091   106.980 1.00 21.63 ? 367  ARG   B N     1 
ATOM   11342 C  CA    . ARG   B  1 369  ? -9.946  10.374  107.245 1.00 21.13 ? 367  ARG   B CA    1 
ATOM   11343 C  C     . ARG   B  1 369  ? -10.330 10.974  105.901 1.00 23.96 ? 367  ARG   B C     1 
ATOM   11344 O  O     . ARG   B  1 369  ? -9.459  11.287  105.081 1.00 23.79 ? 367  ARG   B O     1 
ATOM   11345 C  CB    . ARG   B  1 369  ? -9.022  11.306  108.024 1.00 23.05 ? 367  ARG   B CB    1 
ATOM   11346 C  CG    . ARG   B  1 369  ? -9.675  12.648  108.309 1.00 21.56 ? 367  ARG   B CG    1 
ATOM   11347 C  CD    . ARG   B  1 369  ? -8.655  13.704  108.702 1.00 21.99 ? 367  ARG   B CD    1 
ATOM   11348 N  NE    . ARG   B  1 369  ? -7.988  13.357  109.951 1.00 23.33 ? 367  ARG   B NE    1 
ATOM   11349 C  CZ    . ARG   B  1 369  ? -6.774  13.770  110.279 1.00 25.46 ? 367  ARG   B CZ    1 
ATOM   11350 N  NH1   . ARG   B  1 369  ? -6.057  14.518  109.456 1.00 23.82 ? 367  ARG   B NH1   1 
ATOM   11351 N  NH2   . ARG   B  1 369  ? -6.260  13.407  111.452 1.00 22.72 ? 367  ARG   B NH2   1 
ATOM   11352 N  N     . LEU   B  1 370  ? -11.631 11.095  105.660 1.00 22.11 ? 368  LEU   B N     1 
ATOM   11353 C  CA    . LEU   B  1 370  ? -12.137 11.755  104.468 1.00 23.06 ? 368  LEU   B CA    1 
ATOM   11354 C  C     . LEU   B  1 370  ? -12.260 13.238  104.780 1.00 21.00 ? 368  LEU   B C     1 
ATOM   11355 O  O     . LEU   B  1 370  ? -12.958 13.625  105.723 1.00 24.95 ? 368  LEU   B O     1 
ATOM   11356 C  CB    . LEU   B  1 370  ? -13.488 11.167  104.056 1.00 23.97 ? 368  LEU   B CB    1 
ATOM   11357 C  CG    . LEU   B  1 370  ? -14.089 11.739  102.771 1.00 25.95 ? 368  LEU   B CG    1 
ATOM   11358 C  CD1   . LEU   B  1 370  ? -13.168 11.470  101.580 1.00 22.35 ? 368  LEU   B CD1   1 
ATOM   11359 C  CD2   . LEU   B  1 370  ? -15.456 11.135  102.541 1.00 22.89 ? 368  LEU   B CD2   1 
ATOM   11360 N  N     . VAL   B  1 371  ? -11.540 14.058  104.029 1.00 21.75 ? 369  VAL   B N     1 
ATOM   11361 C  CA    . VAL   B  1 371  ? -11.610 15.499  104.165 1.00 18.53 ? 369  VAL   B CA    1 
ATOM   11362 C  C     . VAL   B  1 371  ? -11.982 16.061  102.816 1.00 21.60 ? 369  VAL   B C     1 
ATOM   11363 O  O     . VAL   B  1 371  ? -11.967 15.362  101.801 1.00 22.65 ? 369  VAL   B O     1 
ATOM   11364 C  CB    . VAL   B  1 371  ? -10.285 16.116  104.639 1.00 18.04 ? 369  VAL   B CB    1 
ATOM   11365 C  CG1   . VAL   B  1 371  ? -9.796  15.416  105.899 1.00 19.48 ? 369  VAL   B CG1   1 
ATOM   11366 C  CG2   . VAL   B  1 371  ? -9.233  16.069  103.515 1.00 18.28 ? 369  VAL   B CG2   1 
ATOM   11367 N  N     . LYS   B  1 372  ? -12.282 17.355  102.802 1.00 18.07 ? 370  LYS   B N     1 
ATOM   11368 C  CA    . LYS   B  1 372  ? -12.413 18.018  101.516 1.00 18.36 ? 370  LYS   B CA    1 
ATOM   11369 C  C     . LYS   B  1 372  ? -11.040 18.432  101.004 1.00 18.85 ? 370  LYS   B C     1 
ATOM   11370 O  O     . LYS   B  1 372  ? -10.578 17.926  99.984  1.00 19.77 ? 370  LYS   B O     1 
ATOM   11371 C  CB    . LYS   B  1 372  ? -13.399 19.182  101.627 1.00 19.03 ? 370  LYS   B CB    1 
ATOM   11372 C  CG    . LYS   B  1 372  ? -14.809 18.623  101.932 1.00 21.84 ? 370  LYS   B CG    1 
ATOM   11373 C  CD    . LYS   B  1 372  ? -15.911 19.658  101.958 1.00 22.67 ? 370  LYS   B CD    1 
ATOM   11374 C  CE    . LYS   B  1 372  ? -17.210 18.994  102.441 1.00 27.58 ? 370  LYS   B CE    1 
ATOM   11375 N  NZ    . LYS   B  1 372  ? -18.271 19.998  102.752 1.00 24.89 ? 370  LYS   B NZ    1 
ATOM   11376 N  N     . GLY   B  1 373  ? -10.333 19.277  101.737 1.00 20.90 ? 371  GLY   B N     1 
ATOM   11377 C  CA    . GLY   B  1 373  ? -8.969  19.574  101.329 1.00 19.44 ? 371  GLY   B CA    1 
ATOM   11378 C  C     . GLY   B  1 373  ? -8.536  20.986  101.654 1.00 22.57 ? 371  GLY   B C     1 
ATOM   11379 O  O     . GLY   B  1 373  ? -9.321  21.925  101.506 1.00 21.77 ? 371  GLY   B O     1 
ATOM   11380 N  N     . ALA   B  1 374  ? -7.284  21.152  102.086 1.00 19.57 ? 372  ALA   B N     1 
ATOM   11381 C  CA    . ALA   B  1 374  ? -6.832  22.412  102.664 1.00 19.87 ? 372  ALA   B CA    1 
ATOM   11382 C  C     . ALA   B  1 374  ? -6.006  23.273  101.713 1.00 21.68 ? 372  ALA   B C     1 
ATOM   11383 O  O     . ALA   B  1 374  ? -5.599  24.373  102.101 1.00 20.07 ? 372  ALA   B O     1 
ATOM   11384 C  CB    . ALA   B  1 374  ? -6.018  22.133  103.935 1.00 21.16 ? 372  ALA   B CB    1 
ATOM   11385 N  N     . TYR   B  1 375  ? -5.753  22.821  100.479 1.00 16.14 ? 373  TYR   B N     1 
ATOM   11386 C  CA    . TYR   B  1 375  ? -4.780  23.487  99.616  1.00 18.45 ? 373  TYR   B CA    1 
ATOM   11387 C  C     . TYR   B  1 375  ? -5.406  24.016  98.335  1.00 19.31 ? 373  TYR   B C     1 
ATOM   11388 O  O     . TYR   B  1 375  ? -4.697  24.179  97.343  1.00 17.77 ? 373  TYR   B O     1 
ATOM   11389 C  CB    . TYR   B  1 375  ? -3.638  22.539  99.251  1.00 18.93 ? 373  TYR   B CB    1 
ATOM   11390 C  CG    . TYR   B  1 375  ? -2.904  21.979  100.432 1.00 18.54 ? 373  TYR   B CG    1 
ATOM   11391 C  CD1   . TYR   B  1 375  ? -3.402  20.888  101.126 1.00 19.84 ? 373  TYR   B CD1   1 
ATOM   11392 C  CD2   . TYR   B  1 375  ? -1.702  22.539  100.853 1.00 24.54 ? 373  TYR   B CD2   1 
ATOM   11393 C  CE1   . TYR   B  1 375  ? -2.732  20.377  102.218 1.00 23.01 ? 373  TYR   B CE1   1 
ATOM   11394 C  CE2   . TYR   B  1 375  ? -1.025  22.035  101.935 1.00 27.62 ? 373  TYR   B CE2   1 
ATOM   11395 C  CZ    . TYR   B  1 375  ? -1.538  20.952  102.611 1.00 26.03 ? 373  TYR   B CZ    1 
ATOM   11396 O  OH    . TYR   B  1 375  ? -0.864  20.438  103.688 1.00 28.24 ? 373  TYR   B OH    1 
ATOM   11397 N  N     . TRP   B  1 376  ? -6.713  24.290  98.338  1.00 17.67 ? 374  TRP   B N     1 
ATOM   11398 C  CA    . TRP   B  1 376  ? -7.418  24.523  97.081  1.00 18.40 ? 374  TRP   B CA    1 
ATOM   11399 C  C     . TRP   B  1 376  ? -6.818  25.697  96.303  1.00 20.02 ? 374  TRP   B C     1 
ATOM   11400 O  O     . TRP   B  1 376  ? -6.490  25.563  95.122  1.00 19.12 ? 374  TRP   B O     1 
ATOM   11401 C  CB    . TRP   B  1 376  ? -8.908  24.742  97.342  1.00 17.19 ? 374  TRP   B CB    1 
ATOM   11402 C  CG    . TRP   B  1 376  ? -9.661  24.877  96.063  1.00 20.05 ? 374  TRP   B CG    1 
ATOM   11403 C  CD1   . TRP   B  1 376  ? -10.063 23.870  95.230  1.00 18.24 ? 374  TRP   B CD1   1 
ATOM   11404 C  CD2   . TRP   B  1 376  ? -10.051 26.100  95.437  1.00 22.68 ? 374  TRP   B CD2   1 
ATOM   11405 N  NE1   . TRP   B  1 376  ? -10.699 24.397  94.126  1.00 20.34 ? 374  TRP   B NE1   1 
ATOM   11406 C  CE2   . TRP   B  1 376  ? -10.707 25.763  94.232  1.00 21.50 ? 374  TRP   B CE2   1 
ATOM   11407 C  CE3   . TRP   B  1 376  ? -9.924  27.451  95.788  1.00 22.88 ? 374  TRP   B CE3   1 
ATOM   11408 C  CZ2   . TRP   B  1 376  ? -11.235 26.727  93.376  1.00 22.26 ? 374  TRP   B CZ2   1 
ATOM   11409 C  CZ3   . TRP   B  1 376  ? -10.450 28.414  94.931  1.00 25.74 ? 374  TRP   B CZ3   1 
ATOM   11410 C  CH2   . TRP   B  1 376  ? -11.099 28.044  93.741  1.00 24.33 ? 374  TRP   B CH2   1 
ATOM   11411 N  N     . ASP   B  1 377  ? -6.667  26.858  96.946  1.00 18.56 ? 375  ASP   B N     1 
ATOM   11412 C  CA    . ASP   B  1 377  ? -6.156  28.026  96.233  1.00 20.95 ? 375  ASP   B CA    1 
ATOM   11413 C  C     . ASP   B  1 377  ? -4.784  27.750  95.650  1.00 20.21 ? 375  ASP   B C     1 
ATOM   11414 O  O     . ASP   B  1 377  ? -4.482  28.159  94.523  1.00 19.74 ? 375  ASP   B O     1 
ATOM   11415 C  CB    . ASP   B  1 377  ? -6.084  29.237  97.167  1.00 31.30 ? 375  ASP   B CB    1 
ATOM   11416 C  CG    . ASP   B  1 377  ? -7.445  29.843  97.445  1.00 34.95 ? 375  ASP   B CG    1 
ATOM   11417 O  OD1   . ASP   B  1 377  ? -8.132  30.244  96.482  1.00 42.35 ? 375  ASP   B OD1   1 
ATOM   11418 O  OD2   . ASP   B  1 377  ? -7.835  29.912  98.626  1.00 43.82 ? 375  ASP   B OD2   1 
ATOM   11419 N  N     . ALA   B  1 378  ? -3.941  27.051  96.408  1.00 19.54 ? 376  ALA   B N     1 
ATOM   11420 C  CA    . ALA   B  1 378  ? -2.592  26.752  95.943  1.00 19.99 ? 376  ALA   B CA    1 
ATOM   11421 C  C     . ALA   B  1 378  ? -2.614  25.788  94.762  1.00 19.15 ? 376  ALA   B C     1 
ATOM   11422 O  O     . ALA   B  1 378  ? -1.783  25.897  93.852  1.00 17.68 ? 376  ALA   B O     1 
ATOM   11423 C  CB    . ALA   B  1 378  ? -1.771  26.174  97.095  1.00 22.18 ? 376  ALA   B CB    1 
ATOM   11424 N  N     . GLU   B  1 379  ? -3.548  24.832  94.762  1.00 16.96 ? 377  GLU   B N     1 
ATOM   11425 C  CA    . GLU   B  1 379  ? -3.597  23.872  93.660  1.00 18.86 ? 377  GLU   B CA    1 
ATOM   11426 C  C     . GLU   B  1 379  ? -4.041  24.542  92.370  1.00 17.72 ? 377  GLU   B C     1 
ATOM   11427 O  O     . GLU   B  1 379  ? -3.540  24.210  91.288  1.00 17.64 ? 377  GLU   B O     1 
ATOM   11428 C  CB    . GLU   B  1 379  ? -4.530  22.698  93.988  1.00 16.50 ? 377  GLU   B CB    1 
ATOM   11429 C  CG    . GLU   B  1 379  ? -4.141  21.876  95.215  1.00 18.28 ? 377  GLU   B CG    1 
ATOM   11430 C  CD    . GLU   B  1 379  ? -2.841  21.083  95.056  1.00 20.00 ? 377  GLU   B CD    1 
ATOM   11431 O  OE1   . GLU   B  1 379  ? -2.214  21.123  93.969  1.00 19.21 ? 377  GLU   B OE1   1 
ATOM   11432 O  OE2   . GLU   B  1 379  ? -2.455  20.398  96.034  1.00 18.67 ? 377  GLU   B OE2   1 
ATOM   11433 N  N     . ILE   B  1 380  ? -4.984  25.483  92.456  1.00 16.66 ? 378  ILE   B N     1 
ATOM   11434 C  CA    . ILE   B  1 380  ? -5.404  26.203  91.255  1.00 15.22 ? 378  ILE   B CA    1 
ATOM   11435 C  C     . ILE   B  1 380  ? -4.235  26.988  90.679  1.00 17.56 ? 378  ILE   B C     1 
ATOM   11436 O  O     . ILE   B  1 380  ? -3.960  26.940  89.475  1.00 16.53 ? 378  ILE   B O     1 
ATOM   11437 C  CB    . ILE   B  1 380  ? -6.592  27.125  91.568  1.00 17.60 ? 378  ILE   B CB    1 
ATOM   11438 C  CG1   . ILE   B  1 380  ? -7.758  26.310  92.126  1.00 20.04 ? 378  ILE   B CG1   1 
ATOM   11439 C  CG2   . ILE   B  1 380  ? -6.981  27.939  90.317  1.00 17.47 ? 378  ILE   B CG2   1 
ATOM   11440 C  CD1   . ILE   B  1 380  ? -8.321  25.270  91.164  1.00 19.37 ? 378  ILE   B CD1   1 
ATOM   11441 N  N     . LYS   B  1 381  ? -3.537  27.736  91.533  1.00 15.92 ? 379  LYS   B N     1 
ATOM   11442 C  CA    . LYS   B  1 381  ? -2.423  28.546  91.046  1.00 14.81 ? 379  LYS   B CA    1 
ATOM   11443 C  C     . LYS   B  1 381  ? -1.332  27.668  90.451  1.00 16.56 ? 379  LYS   B C     1 
ATOM   11444 O  O     . LYS   B  1 381  ? -0.812  27.955  89.369  1.00 17.61 ? 379  LYS   B O     1 
ATOM   11445 C  CB    . LYS   B  1 381  ? -1.864  29.393  92.182  1.00 17.87 ? 379  LYS   B CB    1 
ATOM   11446 C  CG    . LYS   B  1 381  ? -0.618  30.182  91.771  1.00 17.28 ? 379  LYS   B CG    1 
ATOM   11447 C  CD    . LYS   B  1 381  ? -0.165  31.069  92.922  1.00 17.64 ? 379  LYS   B CD    1 
ATOM   11448 C  CE    . LYS   B  1 381  ? 0.972   31.999  92.499  1.00 19.77 ? 379  LYS   B CE    1 
ATOM   11449 N  NZ    . LYS   B  1 381  ? 1.413   32.856  93.649  1.00 17.36 ? 379  LYS   B NZ    1 
ATOM   11450 N  N     . ARG   B  1 382  ? -1.017  26.561  91.122  1.00 16.96 ? 380  ARG   B N     1 
ATOM   11451 C  CA    . ARG   B  1 382  ? 0.065   25.695  90.659  1.00 20.28 ? 380  ARG   B CA    1 
ATOM   11452 C  C     . ARG   B  1 382  ? -0.252  25.080  89.299  1.00 17.89 ? 380  ARG   B C     1 
ATOM   11453 O  O     . ARG   B  1 382  ? 0.614   25.018  88.417  1.00 17.32 ? 380  ARG   B O     1 
ATOM   11454 C  CB    . ARG   B  1 382  ? 0.323   24.601  91.697  1.00 20.71 ? 380  ARG   B CB    1 
ATOM   11455 C  CG    . ARG   B  1 382  ? 1.518   23.708  91.382  1.00 26.10 ? 380  ARG   B CG    1 
ATOM   11456 C  CD    . ARG   B  1 382  ? 2.818   24.412  91.727  1.00 34.07 ? 380  ARG   B CD    1 
ATOM   11457 N  NE    . ARG   B  1 382  ? 3.522   24.891  90.548  1.00 33.50 ? 380  ARG   B NE    1 
ATOM   11458 C  CZ    . ARG   B  1 382  ? 4.420   25.870  90.556  1.00 39.80 ? 380  ARG   B CZ    1 
ATOM   11459 N  NH1   . ARG   B  1 382  ? 4.698   26.544  91.662  1.00 38.39 ? 380  ARG   B NH1   1 
ATOM   11460 N  NH2   . ARG   B  1 382  ? 5.060   26.177  89.427  1.00 32.30 ? 380  ARG   B NH2   1 
ATOM   11461 N  N     . ALA   B  1 383  ? -1.479  24.608  89.111  1.00 15.32 ? 381  ALA   B N     1 
ATOM   11462 C  CA    . ALA   B  1 383  ? -1.827  24.005  87.827  1.00 17.86 ? 381  ALA   B CA    1 
ATOM   11463 C  C     . ALA   B  1 383  ? -1.786  25.040  86.710  1.00 16.81 ? 381  ALA   B C     1 
ATOM   11464 O  O     . ALA   B  1 383  ? -1.334  24.746  85.592  1.00 13.98 ? 381  ALA   B O     1 
ATOM   11465 C  CB    . ALA   B  1 383  ? -3.204  23.356  87.921  1.00 17.43 ? 381  ALA   B CB    1 
ATOM   11466 N  N     . GLN   B  1 384  ? -2.234  26.264  87.002  1.00 15.15 ? 382  GLN   B N     1 
ATOM   11467 C  CA    . GLN   B  1 384  ? -2.158  27.327  86.011  1.00 17.03 ? 382  GLN   B CA    1 
ATOM   11468 C  C     . GLN   B  1 384  ? -0.713  27.676  85.691  1.00 16.00 ? 382  GLN   B C     1 
ATOM   11469 O  O     . GLN   B  1 384  ? -0.342  27.794  84.517  1.00 16.72 ? 382  GLN   B O     1 
ATOM   11470 C  CB    . GLN   B  1 384  ? -2.914  28.556  86.495  1.00 18.83 ? 382  GLN   B CB    1 
ATOM   11471 C  CG    . GLN   B  1 384  ? -4.410  28.332  86.553  1.00 15.35 ? 382  GLN   B CG    1 
ATOM   11472 C  CD    . GLN   B  1 384  ? -5.129  29.579  87.008  1.00 17.71 ? 382  GLN   B CD    1 
ATOM   11473 O  OE1   . GLN   B  1 384  ? -4.542  30.406  87.702  1.00 19.59 ? 382  GLN   B OE1   1 
ATOM   11474 N  NE2   . GLN   B  1 384  ? -6.397  29.727  86.620  1.00 15.88 ? 382  GLN   B NE2   1 
ATOM   11475 N  N     . LEU   B  1 385  ? 0.124   27.837  86.726  1.00 15.56 ? 383  LEU   B N     1 
ATOM   11476 C  CA    . LEU   B  1 385  ? 1.530   28.154  86.494  1.00 20.26 ? 383  LEU   B CA    1 
ATOM   11477 C  C     . LEU   B  1 385  ? 2.207   27.095  85.637  1.00 20.74 ? 383  LEU   B C     1 
ATOM   11478 O  O     . LEU   B  1 385  ? 3.074   27.409  84.805  1.00 17.66 ? 383  LEU   B O     1 
ATOM   11479 C  CB    . LEU   B  1 385  ? 2.266   28.290  87.826  1.00 19.98 ? 383  LEU   B CB    1 
ATOM   11480 C  CG    . LEU   B  1 385  ? 2.068   29.597  88.600  1.00 21.63 ? 383  LEU   B CG    1 
ATOM   11481 C  CD1   . LEU   B  1 385  ? 2.754   29.512  89.957  1.00 23.99 ? 383  LEU   B CD1   1 
ATOM   11482 C  CD2   . LEU   B  1 385  ? 2.605   30.759  87.795  1.00 26.75 ? 383  LEU   B CD2   1 
ATOM   11483 N  N     . ASP   B  1 386  ? 1.852   25.833  85.850  1.00 17.62 ? 384  ASP   B N     1 
ATOM   11484 C  CA    . ASP   B  1 386  ? 2.561   24.734  85.216  1.00 17.98 ? 384  ASP   B CA    1 
ATOM   11485 C  C     . ASP   B  1 386  ? 1.965   24.372  83.861  1.00 18.30 ? 384  ASP   B C     1 
ATOM   11486 O  O     . ASP   B  1 386  ? 2.479   23.470  83.194  1.00 18.34 ? 384  ASP   B O     1 
ATOM   11487 C  CB    . ASP   B  1 386  ? 2.582   23.515  86.156  1.00 17.59 ? 384  ASP   B CB    1 
ATOM   11488 C  CG    . ASP   B  1 386  ? 3.542   23.706  87.344  1.00 25.57 ? 384  ASP   B CG    1 
ATOM   11489 O  OD1   . ASP   B  1 386  ? 4.349   24.660  87.317  1.00 25.59 ? 384  ASP   B OD1   1 
ATOM   11490 O  OD2   . ASP   B  1 386  ? 3.494   22.905  88.305  1.00 23.94 ? 384  ASP   B OD2   1 
ATOM   11491 N  N     . GLY   B  1 387  ? 0.919   25.078  83.429  1.00 17.30 ? 385  GLY   B N     1 
ATOM   11492 C  CA    . GLY   B  1 387  ? 0.336   24.815  82.127  1.00 15.57 ? 385  GLY   B CA    1 
ATOM   11493 C  C     . GLY   B  1 387  ? -0.186  23.406  81.963  1.00 20.42 ? 385  GLY   B C     1 
ATOM   11494 O  O     . GLY   B  1 387  ? -0.121  22.851  80.860  1.00 18.20 ? 385  GLY   B O     1 
ATOM   11495 N  N     . LEU   B  1 388  ? -0.717  22.807  83.025  1.00 18.59 ? 386  LEU   B N     1 
ATOM   11496 C  CA    . LEU   B  1 388  ? -1.100  21.405  82.943  1.00 19.67 ? 386  LEU   B CA    1 
ATOM   11497 C  C     . LEU   B  1 388  ? -2.511  21.261  82.376  1.00 22.79 ? 386  LEU   B C     1 
ATOM   11498 O  O     . LEU   B  1 388  ? -3.246  22.237  82.204  1.00 19.06 ? 386  LEU   B O     1 
ATOM   11499 C  CB    . LEU   B  1 388  ? -0.954  20.746  84.314  1.00 21.98 ? 386  LEU   B CB    1 
ATOM   11500 C  CG    . LEU   B  1 388  ? 0.504   20.826  84.783  1.00 21.36 ? 386  LEU   B CG    1 
ATOM   11501 C  CD1   . LEU   B  1 388  ? 0.745   20.056  86.066  1.00 21.54 ? 386  LEU   B CD1   1 
ATOM   11502 C  CD2   . LEU   B  1 388  ? 1.484   20.351  83.708  1.00 20.51 ? 386  LEU   B CD2   1 
ATOM   11503 N  N     . ALA   B  1 389  ? -2.882  20.016  82.051  1.00 19.44 ? 387  ALA   B N     1 
ATOM   11504 C  CA    . ALA   B  1 389  ? -4.070  19.810  81.230  1.00 21.77 ? 387  ALA   B CA    1 
ATOM   11505 C  C     . ALA   B  1 389  ? -5.324  20.269  81.955  1.00 21.03 ? 387  ALA   B C     1 
ATOM   11506 O  O     . ALA   B  1 389  ? -6.251  20.810  81.340  1.00 21.35 ? 387  ALA   B O     1 
ATOM   11507 C  CB    . ALA   B  1 389  ? -4.188  18.337  80.834  1.00 23.72 ? 387  ALA   B CB    1 
ATOM   11508 N  N     . ASP   B  1 390  ? -5.365  20.088  83.267  1.00 22.09 ? 388  ASP   B N     1 
ATOM   11509 C  CA    . ASP   B  1 390  ? -6.542  20.456  84.034  1.00 19.25 ? 388  ASP   B CA    1 
ATOM   11510 C  C     . ASP   B  1 390  ? -6.109  20.572  85.488  1.00 19.17 ? 388  ASP   B C     1 
ATOM   11511 O  O     . ASP   B  1 390  ? -4.937  20.386  85.820  1.00 17.56 ? 388  ASP   B O     1 
ATOM   11512 C  CB    . ASP   B  1 390  ? -7.654  19.425  83.831  1.00 20.60 ? 388  ASP   B CB    1 
ATOM   11513 C  CG    . ASP   B  1 390  ? -9.031  19.998  84.043  1.00 24.96 ? 388  ASP   B CG    1 
ATOM   11514 O  OD1   . ASP   B  1 390  ? -9.194  20.839  84.953  1.00 21.84 ? 388  ASP   B OD1   1 
ATOM   11515 O  OD2   . ASP   B  1 390  ? -9.953  19.601  83.298  1.00 24.47 ? 388  ASP   B OD2   1 
ATOM   11516 N  N     . PHE   B  1 391  ? -7.059  20.884  86.349  1.00 16.32 ? 389  PHE   B N     1 
ATOM   11517 C  CA    . PHE   B  1 391  ? -6.694  20.931  87.756  1.00 18.48 ? 389  PHE   B CA    1 
ATOM   11518 C  C     . PHE   B  1 391  ? -6.775  19.542  88.373  1.00 17.11 ? 389  PHE   B C     1 
ATOM   11519 O  O     . PHE   B  1 391  ? -7.515  18.686  87.880  1.00 18.11 ? 389  PHE   B O     1 
ATOM   11520 C  CB    . PHE   B  1 391  ? -7.628  21.876  88.499  1.00 18.07 ? 389  PHE   B CB    1 
ATOM   11521 C  CG    . PHE   B  1 391  ? -7.599  23.256  87.951  1.00 17.99 ? 389  PHE   B CG    1 
ATOM   11522 C  CD1   . PHE   B  1 391  ? -6.561  24.114  88.286  1.00 17.27 ? 389  PHE   B CD1   1 
ATOM   11523 C  CD2   . PHE   B  1 391  ? -8.571  23.686  87.062  1.00 19.51 ? 389  PHE   B CD2   1 
ATOM   11524 C  CE1   . PHE   B  1 391  ? -6.495  25.380  87.755  1.00 18.21 ? 389  PHE   B CE1   1 
ATOM   11525 C  CE2   . PHE   B  1 391  ? -8.513  24.972  86.539  1.00 18.18 ? 389  PHE   B CE2   1 
ATOM   11526 C  CZ    . PHE   B  1 391  ? -7.476  25.816  86.892  1.00 17.73 ? 389  PHE   B CZ    1 
ATOM   11527 N  N     . PRO   B  1 392  ? -6.007  19.290  89.438  1.00 17.62 ? 390  PRO   B N     1 
ATOM   11528 C  CA    . PRO   B  1 392  ? -6.142  18.030  90.182  1.00 18.56 ? 390  PRO   B CA    1 
ATOM   11529 C  C     . PRO   B  1 392  ? -7.226  18.068  91.242  1.00 18.22 ? 390  PRO   B C     1 
ATOM   11530 O  O     . PRO   B  1 392  ? -7.395  17.084  91.977  1.00 19.46 ? 390  PRO   B O     1 
ATOM   11531 C  CB    . PRO   B  1 392  ? -4.773  17.884  90.828  1.00 18.51 ? 390  PRO   B CB    1 
ATOM   11532 C  CG    . PRO   B  1 392  ? -4.402  19.319  91.161  1.00 19.20 ? 390  PRO   B CG    1 
ATOM   11533 C  CD    . PRO   B  1 392  ? -4.945  20.149  89.999  1.00 18.86 ? 390  PRO   B CD    1 
ATOM   11534 N  N     . VAL   B  1 393  ? -7.928  19.190  91.348  1.00 19.29 ? 391  VAL   B N     1 
ATOM   11535 C  CA    . VAL   B  1 393  ? -9.005  19.396  92.303  1.00 17.46 ? 391  VAL   B CA    1 
ATOM   11536 C  C     . VAL   B  1 393  ? -10.187 19.960  91.528  1.00 18.47 ? 391  VAL   B C     1 
ATOM   11537 O  O     . VAL   B  1 393  ? -10.035 20.489  90.425  1.00 19.77 ? 391  VAL   B O     1 
ATOM   11538 C  CB    . VAL   B  1 393  ? -8.593  20.359  93.440  1.00 19.51 ? 391  VAL   B CB    1 
ATOM   11539 C  CG1   . VAL   B  1 393  ? -7.461  19.758  94.287  1.00 17.99 ? 391  VAL   B CG1   1 
ATOM   11540 C  CG2   . VAL   B  1 393  ? -8.182  21.717  92.860  1.00 17.07 ? 391  VAL   B CG2   1 
ATOM   11541 N  N     . PHE   B  1 394  ? -11.371 19.841  92.112  1.00 20.31 ? 392  PHE   B N     1 
ATOM   11542 C  CA    . PHE   B  1 394  ? -12.542 20.459  91.512  1.00 19.31 ? 392  PHE   B CA    1 
ATOM   11543 C  C     . PHE   B  1 394  ? -12.443 21.977  91.609  1.00 20.73 ? 392  PHE   B C     1 
ATOM   11544 O  O     . PHE   B  1 394  ? -11.680 22.531  92.406  1.00 20.12 ? 392  PHE   B O     1 
ATOM   11545 C  CB    . PHE   B  1 394  ? -13.818 19.924  92.176  1.00 19.81 ? 392  PHE   B CB    1 
ATOM   11546 C  CG    . PHE   B  1 394  ? -13.938 18.443  92.069  1.00 21.49 ? 392  PHE   B CG    1 
ATOM   11547 C  CD1   . PHE   B  1 394  ? -14.184 17.850  90.837  1.00 20.58 ? 392  PHE   B CD1   1 
ATOM   11548 C  CD2   . PHE   B  1 394  ? -13.744 17.632  93.175  1.00 20.07 ? 392  PHE   B CD2   1 
ATOM   11549 C  CE1   . PHE   B  1 394  ? -14.255 16.487  90.714  1.00 20.58 ? 392  PHE   B CE1   1 
ATOM   11550 C  CE2   . PHE   B  1 394  ? -13.813 16.260  93.060  1.00 22.59 ? 392  PHE   B CE2   1 
ATOM   11551 C  CZ    . PHE   B  1 394  ? -14.073 15.690  91.819  1.00 20.14 ? 392  PHE   B CZ    1 
ATOM   11552 N  N     . THR   B  1 395  ? -13.194 22.657  90.745  1.00 21.35 ? 393  THR   B N     1 
ATOM   11553 C  CA    . THR   B  1 395  ? -13.182 24.111  90.730  1.00 19.27 ? 393  THR   B CA    1 
ATOM   11554 C  C     . THR   B  1 395  ? -14.480 24.733  91.220  1.00 21.48 ? 393  THR   B C     1 
ATOM   11555 O  O     . THR   B  1 395  ? -14.511 25.947  91.443  1.00 22.98 ? 393  THR   B O     1 
ATOM   11556 C  CB    . THR   B  1 395  ? -12.875 24.628  89.317  1.00 20.64 ? 393  THR   B CB    1 
ATOM   11557 O  OG1   . THR   B  1 395  ? -13.894 24.186  88.415  1.00 22.32 ? 393  THR   B OG1   1 
ATOM   11558 C  CG2   . THR   B  1 395  ? -11.503 24.116  88.859  1.00 20.07 ? 393  THR   B CG2   1 
ATOM   11559 N  N     . ARG   B  1 396  ? -15.544 23.948  91.389  1.00 22.31 ? 394  ARG   B N     1 
ATOM   11560 C  CA    . ARG   B  1 396  ? -16.761 24.396  92.056  1.00 19.06 ? 394  ARG   B CA    1 
ATOM   11561 C  C     . ARG   B  1 396  ? -16.869 23.721  93.411  1.00 22.97 ? 394  ARG   B C     1 
ATOM   11562 O  O     . ARG   B  1 396  ? -16.704 22.501  93.514  1.00 20.99 ? 394  ARG   B O     1 
ATOM   11563 C  CB    . ARG   B  1 396  ? -18.010 24.073  91.233  1.00 19.75 ? 394  ARG   B CB    1 
ATOM   11564 C  CG    . ARG   B  1 396  ? -18.050 24.771  89.887  1.00 24.98 ? 394  ARG   B CG    1 
ATOM   11565 C  CD    . ARG   B  1 396  ? -19.435 24.616  89.225  1.00 25.06 ? 394  ARG   B CD    1 
ATOM   11566 N  NE    . ARG   B  1 396  ? -19.404 25.132  87.858  1.00 30.39 ? 394  ARG   B NE    1 
ATOM   11567 C  CZ    . ARG   B  1 396  ? -20.201 26.085  87.387  1.00 37.08 ? 394  ARG   B CZ    1 
ATOM   11568 N  NH1   . ARG   B  1 396  ? -21.173 26.601  88.125  1.00 42.01 ? 394  ARG   B NH1   1 
ATOM   11569 N  NH2   . ARG   B  1 396  ? -20.021 26.527  86.142  1.00 30.66 ? 394  ARG   B NH2   1 
ATOM   11570 N  N     . LYS   B  1 397  ? -17.173 24.511  94.442  1.00 22.25 ? 395  LYS   B N     1 
ATOM   11571 C  CA    . LYS   B  1 397  ? -17.208 23.968  95.796  1.00 23.75 ? 395  LYS   B CA    1 
ATOM   11572 C  C     . LYS   B  1 397  ? -18.271 22.881  95.932  1.00 23.04 ? 395  LYS   B C     1 
ATOM   11573 O  O     . LYS   B  1 397  ? -18.081 21.898  96.660  1.00 24.74 ? 395  LYS   B O     1 
ATOM   11574 C  CB    . LYS   B  1 397  ? -17.442 25.097  96.795  1.00 24.84 ? 395  LYS   B CB    1 
ATOM   11575 C  CG    . LYS   B  1 397  ? -17.137 24.733  98.230  1.00 25.60 ? 395  LYS   B CG    1 
ATOM   11576 C  CD    . LYS   B  1 397  ? -18.359 24.216  98.943  1.00 28.39 ? 395  LYS   B CD    1 
ATOM   11577 C  CE    . LYS   B  1 397  ? -18.067 23.913  100.404 1.00 27.52 ? 395  LYS   B CE    1 
ATOM   11578 N  NZ    . LYS   B  1 397  ? -19.298 23.491  101.125 1.00 29.55 ? 395  LYS   B NZ    1 
ATOM   11579 N  N     . ILE   B  1 398  ? -19.398 23.033  95.237  1.00 22.00 ? 396  ILE   B N     1 
ATOM   11580 C  CA    . ILE   B  1 398  ? -20.445 22.025  95.310  1.00 23.88 ? 396  ILE   B CA    1 
ATOM   11581 C  C     . ILE   B  1 398  ? -19.967 20.699  94.727  1.00 22.50 ? 396  ILE   B C     1 
ATOM   11582 O  O     . ILE   B  1 398  ? -20.423 19.628  95.144  1.00 23.75 ? 396  ILE   B O     1 
ATOM   11583 C  CB    . ILE   B  1 398  ? -21.712 22.554  94.608  1.00 23.34 ? 396  ILE   B CB    1 
ATOM   11584 C  CG1   . ILE   B  1 398  ? -22.905 21.689  94.959  1.00 31.44 ? 396  ILE   B CG1   1 
ATOM   11585 C  CG2   . ILE   B  1 398  ? -21.500 22.652  93.094  1.00 25.33 ? 396  ILE   B CG2   1 
ATOM   11586 C  CD1   . ILE   B  1 398  ? -24.219 22.375  94.720  1.00 34.84 ? 396  ILE   B CD1   1 
ATOM   11587 N  N     . HIS   B  1 399  ? -19.021 20.741  93.781  1.00 23.96 ? 397  HIS   B N     1 
ATOM   11588 C  CA    . HIS   B  1 399  ? -18.448 19.496  93.275  1.00 23.87 ? 397  HIS   B CA    1 
ATOM   11589 C  C     . HIS   B  1 399  ? -17.693 18.759  94.365  1.00 24.42 ? 397  HIS   B C     1 
ATOM   11590 O  O     . HIS   B  1 399  ? -17.812 17.537  94.494  1.00 26.26 ? 397  HIS   B O     1 
ATOM   11591 C  CB    . HIS   B  1 399  ? -17.534 19.783  92.086  1.00 22.76 ? 397  HIS   B CB    1 
ATOM   11592 C  CG    . HIS   B  1 399  ? -18.279 20.263  90.881  1.00 23.74 ? 397  HIS   B CG    1 
ATOM   11593 N  ND1   . HIS   B  1 399  ? -17.648 20.745  89.758  1.00 23.01 ? 397  HIS   B ND1   1 
ATOM   11594 C  CD2   . HIS   B  1 399  ? -19.609 20.342  90.633  1.00 25.64 ? 397  HIS   B CD2   1 
ATOM   11595 C  CE1   . HIS   B  1 399  ? -18.559 21.103  88.866  1.00 25.24 ? 397  HIS   B CE1   1 
ATOM   11596 N  NE2   . HIS   B  1 399  ? -19.756 20.864  89.370  1.00 22.19 ? 397  HIS   B NE2   1 
ATOM   11597 N  N     . THR   B  1 400  ? -16.899 19.482  95.150  1.00 22.69 ? 398  THR   B N     1 
ATOM   11598 C  CA    . THR   B  1 400  ? -16.199 18.842  96.257  1.00 23.91 ? 398  THR   B CA    1 
ATOM   11599 C  C     . THR   B  1 400  ? -17.180 18.217  97.235  1.00 22.78 ? 398  THR   B C     1 
ATOM   11600 O  O     . THR   B  1 400  ? -16.948 17.111  97.739  1.00 24.06 ? 398  THR   B O     1 
ATOM   11601 C  CB    . THR   B  1 400  ? -15.307 19.863  96.963  1.00 20.48 ? 398  THR   B CB    1 
ATOM   11602 O  OG1   . THR   B  1 400  ? -14.235 20.219  96.084  1.00 19.60 ? 398  THR   B OG1   1 
ATOM   11603 C  CG2   . THR   B  1 400  ? -14.750 19.292  98.267  1.00 20.11 ? 398  THR   B CG2   1 
ATOM   11604 N  N     . ASP   B  1 401  ? -18.285 18.909  97.513  1.00 23.18 ? 399  ASP   B N     1 
ATOM   11605 C  CA    . ASP   B  1 401  ? -19.301 18.362  98.407  1.00 24.40 ? 399  ASP   B CA    1 
ATOM   11606 C  C     . ASP   B  1 401  ? -19.877 17.067  97.858  1.00 26.41 ? 399  ASP   B C     1 
ATOM   11607 O  O     . ASP   B  1 401  ? -20.027 16.081  98.589  1.00 23.96 ? 399  ASP   B O     1 
ATOM   11608 C  CB    . ASP   B  1 401  ? -20.408 19.392  98.633  1.00 26.38 ? 399  ASP   B CB    1 
ATOM   11609 C  CG    . ASP   B  1 401  ? -19.935 20.574  99.458  1.00 29.70 ? 399  ASP   B CG    1 
ATOM   11610 O  OD1   . ASP   B  1 401  ? -18.937 20.410  100.193 1.00 29.14 ? 399  ASP   B OD1   1 
ATOM   11611 O  OD2   . ASP   B  1 401  ? -20.549 21.664  99.370  1.00 27.22 ? 399  ASP   B OD2   1 
ATOM   11612 N  N     . VAL   B  1 402  ? -20.213 17.050  96.567  1.00 24.30 ? 400  VAL   B N     1 
ATOM   11613 C  CA    . VAL   B  1 402  ? -20.741 15.827  95.971  1.00 27.68 ? 400  VAL   B CA    1 
ATOM   11614 C  C     . VAL   B  1 402  ? -19.694 14.726  96.035  1.00 24.63 ? 400  VAL   B C     1 
ATOM   11615 O  O     . VAL   B  1 402  ? -19.994 13.582  96.397  1.00 24.75 ? 400  VAL   B O     1 
ATOM   11616 C  CB    . VAL   B  1 402  ? -21.204 16.088  94.523  1.00 28.47 ? 400  VAL   B CB    1 
ATOM   11617 C  CG1   . VAL   B  1 402  ? -21.588 14.778  93.857  1.00 25.41 ? 400  VAL   B CG1   1 
ATOM   11618 C  CG2   . VAL   B  1 402  ? -22.368 17.079  94.495  1.00 30.16 ? 400  VAL   B CG2   1 
ATOM   11619 N  N     . SER   B  1 403  ? -18.440 15.064  95.719  1.00 21.90 ? 401  SER   B N     1 
ATOM   11620 C  CA    . SER   B  1 403  ? -17.369 14.081  95.795  1.00 24.31 ? 401  SER   B CA    1 
ATOM   11621 C  C     . SER   B  1 403  ? -17.261 13.512  97.202  1.00 24.84 ? 401  SER   B C     1 
ATOM   11622 O  O     . SER   B  1 403  ? -17.139 12.295  97.386  1.00 22.94 ? 401  SER   B O     1 
ATOM   11623 C  CB    . SER   B  1 403  ? -16.050 14.727  95.359  1.00 19.97 ? 401  SER   B CB    1 
ATOM   11624 O  OG    . SER   B  1 403  ? -14.959 13.866  95.610  1.00 22.45 ? 401  SER   B OG    1 
ATOM   11625 N  N     . TYR   B  1 404  ? -17.349 14.379  98.209  1.00 22.61 ? 402  TYR   B N     1 
ATOM   11626 C  CA    . TYR   B  1 404  ? -17.247 13.927  99.592  1.00 24.37 ? 402  TYR   B CA    1 
ATOM   11627 C  C     . TYR   B  1 404  ? -18.335 12.911  99.906  1.00 23.11 ? 402  TYR   B C     1 
ATOM   11628 O  O     . TYR   B  1 404  ? -18.062 11.821  100.421 1.00 26.70 ? 402  TYR   B O     1 
ATOM   11629 C  CB    . TYR   B  1 404  ? -17.338 15.131  100.525 1.00 23.02 ? 402  TYR   B CB    1 
ATOM   11630 C  CG    . TYR   B  1 404  ? -16.951 14.846  101.955 1.00 25.03 ? 402  TYR   B CG    1 
ATOM   11631 C  CD1   . TYR   B  1 404  ? -17.819 14.191  102.814 1.00 25.59 ? 402  TYR   B CD1   1 
ATOM   11632 C  CD2   . TYR   B  1 404  ? -15.730 15.263  102.454 1.00 23.76 ? 402  TYR   B CD2   1 
ATOM   11633 C  CE1   . TYR   B  1 404  ? -17.472 13.940  104.127 1.00 26.76 ? 402  TYR   B CE1   1 
ATOM   11634 C  CE2   . TYR   B  1 404  ? -15.372 15.016  103.774 1.00 23.88 ? 402  TYR   B CE2   1 
ATOM   11635 C  CZ    . TYR   B  1 404  ? -16.246 14.352  104.597 1.00 27.06 ? 402  TYR   B CZ    1 
ATOM   11636 O  OH    . TYR   B  1 404  ? -15.906 14.106  105.912 1.00 25.28 ? 402  TYR   B OH    1 
ATOM   11637 N  N     . ILE   B  1 405  ? -19.577 13.238  99.563  1.00 25.44 ? 403  ILE   B N     1 
ATOM   11638 C  CA    . ILE   B  1 405  ? -20.688 12.349  99.884  1.00 25.25 ? 403  ILE   B CA    1 
ATOM   11639 C  C     . ILE   B  1 405  ? -20.553 11.030  99.134  1.00 26.69 ? 403  ILE   B C     1 
ATOM   11640 O  O     . ILE   B  1 405  ? -20.809 9.959   99.692  1.00 27.21 ? 403  ILE   B O     1 
ATOM   11641 C  CB    . ILE   B  1 405  ? -22.020 13.061  99.586  1.00 29.77 ? 403  ILE   B CB    1 
ATOM   11642 C  CG1   . ILE   B  1 405  ? -22.157 14.301  100.474 1.00 29.94 ? 403  ILE   B CG1   1 
ATOM   11643 C  CG2   . ILE   B  1 405  ? -23.186 12.135  99.782  1.00 31.00 ? 403  ILE   B CG2   1 
ATOM   11644 C  CD1   . ILE   B  1 405  ? -23.275 15.237  100.051 1.00 35.71 ? 403  ILE   B CD1   1 
ATOM   11645 N  N     . ALA   B  1 406  ? -20.140 11.085  97.860  1.00 26.70 ? 404  ALA   B N     1 
ATOM   11646 C  CA    . ALA   B  1 406  ? -19.925 9.862   97.089  1.00 25.01 ? 404  ALA   B CA    1 
ATOM   11647 C  C     . ALA   B  1 406  ? -18.832 8.999   97.710  1.00 26.69 ? 404  ALA   B C     1 
ATOM   11648 O  O     . ALA   B  1 406  ? -18.971 7.775   97.803  1.00 27.80 ? 404  ALA   B O     1 
ATOM   11649 C  CB    . ALA   B  1 406  ? -19.562 10.208  95.642  1.00 27.13 ? 404  ALA   B CB    1 
ATOM   11650 N  N     . CYS   B  1 407  ? -17.733 9.619   98.130  1.00 24.38 ? 405  CYS   B N     1 
ATOM   11651 C  CA    . CYS   B  1 407  ? -16.642 8.854   98.713  1.00 24.88 ? 405  CYS   B CA    1 
ATOM   11652 C  C     . CYS   B  1 407  ? -17.020 8.301   100.083 1.00 26.38 ? 405  CYS   B C     1 
ATOM   11653 O  O     . CYS   B  1 407  ? -16.534 7.235   100.477 1.00 26.45 ? 405  CYS   B O     1 
ATOM   11654 C  CB    . CYS   B  1 407  ? -15.386 9.729   98.778  1.00 25.27 ? 405  CYS   B CB    1 
ATOM   11655 S  SG    . CYS   B  1 407  ? -14.696 10.032  97.107  1.00 28.64 ? 405  CYS   B SG    1 
ATOM   11656 N  N     . ALA   B  1 408  ? -17.891 8.999   100.810 1.00 25.71 ? 406  ALA   B N     1 
ATOM   11657 C  CA    . ALA   B  1 408  ? -18.404 8.461   102.065 1.00 28.11 ? 406  ALA   B CA    1 
ATOM   11658 C  C     . ALA   B  1 408  ? -19.223 7.195   101.831 1.00 25.47 ? 406  ALA   B C     1 
ATOM   11659 O  O     . ALA   B  1 408  ? -19.122 6.230   102.597 1.00 31.17 ? 406  ALA   B O     1 
ATOM   11660 C  CB    . ALA   B  1 408  ? -19.241 9.519   102.779 1.00 30.00 ? 406  ALA   B CB    1 
ATOM   11661 N  N     . ALA   B  1 409  ? -20.034 7.175   100.772 1.00 29.26 ? 407  ALA   B N     1 
ATOM   11662 C  CA    . ALA   B  1 409  ? -20.763 5.956   100.439 1.00 32.11 ? 407  ALA   B CA    1 
ATOM   11663 C  C     . ALA   B  1 409  ? -19.802 4.797   100.213 1.00 29.54 ? 407  ALA   B C     1 
ATOM   11664 O  O     . ALA   B  1 409  ? -20.038 3.675   100.678 1.00 30.44 ? 407  ALA   B O     1 
ATOM   11665 C  CB    . ALA   B  1 409  ? -21.633 6.184   99.199  1.00 29.77 ? 407  ALA   B CB    1 
ATOM   11666 N  N     . LYS   B  1 410  ? -18.700 5.063   99.518  1.00 26.36 ? 408  LYS   B N     1 
ATOM   11667 C  CA    . LYS   B  1 410  ? -17.717 4.027   99.239  1.00 29.18 ? 408  LYS   B CA    1 
ATOM   11668 C  C     . LYS   B  1 410  ? -17.076 3.528   100.529 1.00 31.74 ? 408  LYS   B C     1 
ATOM   11669 O  O     . LYS   B  1 410  ? -16.908 2.317   100.727 1.00 29.23 ? 408  LYS   B O     1 
ATOM   11670 C  CB    . LYS   B  1 410  ? -16.676 4.588   98.270  1.00 29.20 ? 408  LYS   B CB    1 
ATOM   11671 C  CG    . LYS   B  1 410  ? -15.538 3.666   97.931  1.00 28.93 ? 408  LYS   B CG    1 
ATOM   11672 C  CD    . LYS   B  1 410  ? -14.581 4.359   96.978  1.00 31.89 ? 408  LYS   B CD    1 
ATOM   11673 C  CE    . LYS   B  1 410  ? -15.192 4.557   95.603  1.00 31.53 ? 408  LYS   B CE    1 
ATOM   11674 N  NZ    . LYS   B  1 410  ? -15.419 3.251   94.924  1.00 30.71 ? 408  LYS   B NZ    1 
ATOM   11675 N  N     . LEU   B  1 411  ? -16.757 4.448   101.435 1.00 29.07 ? 409  LEU   B N     1 
ATOM   11676 C  CA    . LEU   B  1 411  ? -16.142 4.075   102.705 1.00 25.72 ? 409  LEU   B CA    1 
ATOM   11677 C  C     . LEU   B  1 411  ? -17.090 3.253   103.556 1.00 28.42 ? 409  LEU   B C     1 
ATOM   11678 O  O     . LEU   B  1 411  ? -16.713 2.205   104.097 1.00 29.36 ? 409  LEU   B O     1 
ATOM   11679 C  CB    . LEU   B  1 411  ? -15.718 5.335   103.452 1.00 27.32 ? 409  LEU   B CB    1 
ATOM   11680 C  CG    . LEU   B  1 411  ? -14.395 5.876   102.928 1.00 30.07 ? 409  LEU   B CG    1 
ATOM   11681 C  CD1   . LEU   B  1 411  ? -14.102 7.249   103.513 1.00 28.58 ? 409  LEU   B CD1   1 
ATOM   11682 C  CD2   . LEU   B  1 411  ? -13.296 4.885   103.296 1.00 25.82 ? 409  LEU   B CD2   1 
ATOM   11683 N  N     . LEU   B  1 412  ? -18.328 3.723   103.685 1.00 32.70 ? 410  LEU   B N     1 
ATOM   11684 C  CA    . LEU   B  1 412  ? -19.322 3.039   104.497 1.00 31.22 ? 410  LEU   B CA    1 
ATOM   11685 C  C     . LEU   B  1 412  ? -19.622 1.630   104.000 1.00 32.22 ? 410  LEU   B C     1 
ATOM   11686 O  O     . LEU   B  1 412  ? -20.135 0.816   104.772 1.00 34.49 ? 410  LEU   B O     1 
ATOM   11687 C  CB    . LEU   B  1 412  ? -20.592 3.883   104.540 1.00 33.02 ? 410  LEU   B CB    1 
ATOM   11688 C  CG    . LEU   B  1 412  ? -20.440 5.159   105.373 1.00 33.49 ? 410  LEU   B CG    1 
ATOM   11689 C  CD1   . LEU   B  1 412  ? -21.622 6.101   105.157 1.00 34.06 ? 410  LEU   B CD1   1 
ATOM   11690 C  CD2   . LEU   B  1 412  ? -20.291 4.800   106.848 1.00 31.12 ? 410  LEU   B CD2   1 
ATOM   11691 N  N     . ALA   B  1 413  ? -19.319 1.316   102.744 1.00 31.65 ? 411  ALA   B N     1 
ATOM   11692 C  CA    . ALA   B  1 413  ? -19.508 -0.039  102.242 1.00 33.97 ? 411  ALA   B CA    1 
ATOM   11693 C  C     . ALA   B  1 413  ? -18.319 -0.948  102.535 1.00 35.18 ? 411  ALA   B C     1 
ATOM   11694 O  O     . ALA   B  1 413  ? -18.353 -2.129  102.172 1.00 33.48 ? 411  ALA   B O     1 
ATOM   11695 C  CB    . ALA   B  1 413  ? -19.781 -0.018  100.732 1.00 30.85 ? 411  ALA   B CB    1 
ATOM   11696 N  N     . ALA   B  1 414  ? -17.278 -0.437  103.197 1.00 27.26 ? 412  ALA   B N     1 
ATOM   11697 C  CA    . ALA   B  1 414  ? -16.052 -1.199  103.395 1.00 34.01 ? 412  ALA   B CA    1 
ATOM   11698 C  C     . ALA   B  1 414  ? -15.598 -1.164  104.852 1.00 32.34 ? 412  ALA   B C     1 
ATOM   11699 O  O     . ALA   B  1 414  ? -14.409 -1.329  105.139 1.00 29.06 ? 412  ALA   B O     1 
ATOM   11700 C  CB    . ALA   B  1 414  ? -14.942 -0.683  102.477 1.00 27.09 ? 412  ALA   B CB    1 
ATOM   11701 N  N     . THR   B  1 415  ? -16.533 -0.975  105.786 1.00 31.81 ? 413  THR   B N     1 
ATOM   11702 C  CA    . THR   B  1 415  ? -16.149 -0.758  107.177 1.00 32.68 ? 413  THR   B CA    1 
ATOM   11703 C  C     . THR   B  1 415  ? -15.526 -1.984  107.827 1.00 34.30 ? 413  THR   B C     1 
ATOM   11704 O  O     . THR   B  1 415  ? -14.913 -1.852  108.890 1.00 33.74 ? 413  THR   B O     1 
ATOM   11705 C  CB    . THR   B  1 415  ? -17.349 -0.296  108.002 1.00 30.31 ? 413  THR   B CB    1 
ATOM   11706 O  OG1   . THR   B  1 415  ? -18.433 -1.212  107.825 1.00 33.01 ? 413  THR   B OG1   1 
ATOM   11707 C  CG2   . THR   B  1 415  ? -17.781 1.103   107.556 1.00 25.75 ? 413  THR   B CG2   1 
ATOM   11708 N  N     . ASP   B  1 416  ? -15.671 -3.171  107.234 1.00 33.03 ? 414  ASP   B N     1 
ATOM   11709 C  CA    . ASP   B  1 416  ? -14.948 -4.323  107.761 1.00 31.47 ? 414  ASP   B CA    1 
ATOM   11710 C  C     . ASP   B  1 416  ? -13.445 -4.107  107.653 1.00 32.92 ? 414  ASP   B C     1 
ATOM   11711 O  O     . ASP   B  1 416  ? -12.684 -4.506  108.544 1.00 36.41 ? 414  ASP   B O     1 
ATOM   11712 C  CB    . ASP   B  1 416  ? -15.354 -5.601  107.020 1.00 36.40 ? 414  ASP   B CB    1 
ATOM   11713 C  CG    . ASP   B  1 416  ? -16.637 -6.228  107.560 1.00 42.71 ? 414  ASP   B CG    1 
ATOM   11714 O  OD1   . ASP   B  1 416  ? -17.157 -5.762  108.601 1.00 42.16 ? 414  ASP   B OD1   1 
ATOM   11715 O  OD2   . ASP   B  1 416  ? -17.118 -7.205  106.935 1.00 42.32 ? 414  ASP   B OD2   1 
ATOM   11716 N  N     . VAL   B  1 417  ? -12.994 -3.444  106.588 1.00 31.21 ? 415  VAL   B N     1 
ATOM   11717 C  CA    . VAL   B  1 417  ? -11.562 -3.309  106.342 1.00 33.38 ? 415  VAL   B CA    1 
ATOM   11718 C  C     . VAL   B  1 417  ? -11.056 -1.878  106.432 1.00 30.41 ? 415  VAL   B C     1 
ATOM   11719 O  O     . VAL   B  1 417  ? -9.832  -1.680  106.430 1.00 34.38 ? 415  VAL   B O     1 
ATOM   11720 C  CB    . VAL   B  1 417  ? -11.170 -3.933  104.989 1.00 34.43 ? 415  VAL   B CB    1 
ATOM   11721 C  CG1   . VAL   B  1 417  ? -11.608 -5.397  104.961 1.00 31.59 ? 415  VAL   B CG1   1 
ATOM   11722 C  CG2   . VAL   B  1 417  ? -11.789 -3.155  103.856 1.00 29.76 ? 415  VAL   B CG2   1 
ATOM   11723 N  N     . VAL   B  1 418  ? -11.926 -0.878  106.520 1.00 32.18 ? 416  VAL   B N     1 
ATOM   11724 C  CA    . VAL   B  1 418  ? -11.467 0.481   106.775 1.00 29.25 ? 416  VAL   B CA    1 
ATOM   11725 C  C     . VAL   B  1 418  ? -12.338 1.108   107.849 1.00 32.84 ? 416  VAL   B C     1 
ATOM   11726 O  O     . VAL   B  1 418  ? -13.517 0.775   107.998 1.00 32.20 ? 416  VAL   B O     1 
ATOM   11727 C  CB    . VAL   B  1 418  ? -11.456 1.381   105.517 1.00 29.34 ? 416  VAL   B CB    1 
ATOM   11728 C  CG1   . VAL   B  1 418  ? -10.450 0.870   104.492 1.00 31.46 ? 416  VAL   B CG1   1 
ATOM   11729 C  CG2   . VAL   B  1 418  ? -12.863 1.495   104.924 1.00 28.76 ? 416  VAL   B CG2   1 
ATOM   11730 N  N     . PHE   B  1 419  ? -11.733 2.019   108.614 1.00 28.40 ? 417  PHE   B N     1 
ATOM   11731 C  CA    . PHE   B  1 419  ? -12.433 2.796   109.631 1.00 32.32 ? 417  PHE   B CA    1 
ATOM   11732 C  C     . PHE   B  1 419  ? -12.647 4.205   109.096 1.00 30.64 ? 417  PHE   B C     1 
ATOM   11733 O  O     . PHE   B  1 419  ? -11.712 5.027   109.108 1.00 27.31 ? 417  PHE   B O     1 
ATOM   11734 C  CB    . PHE   B  1 419  ? -11.639 2.823   110.944 1.00 29.12 ? 417  PHE   B CB    1 
ATOM   11735 C  CG    . PHE   B  1 419  ? -12.278 3.643   112.026 1.00 28.17 ? 417  PHE   B CG    1 
ATOM   11736 C  CD1   . PHE   B  1 419  ? -13.534 3.323   112.511 1.00 30.93 ? 417  PHE   B CD1   1 
ATOM   11737 C  CD2   . PHE   B  1 419  ? -11.608 4.723   112.581 1.00 29.15 ? 417  PHE   B CD2   1 
ATOM   11738 C  CE1   . PHE   B  1 419  ? -14.120 4.073   113.519 1.00 32.86 ? 417  PHE   B CE1   1 
ATOM   11739 C  CE2   . PHE   B  1 419  ? -12.192 5.476   113.587 1.00 29.33 ? 417  PHE   B CE2   1 
ATOM   11740 C  CZ    . PHE   B  1 419  ? -13.449 5.153   114.054 1.00 30.19 ? 417  PHE   B CZ    1 
ATOM   11741 N  N     . PRO   B  1 420  ? -13.841 4.528   108.598 1.00 30.75 ? 418  PRO   B N     1 
ATOM   11742 C  CA    . PRO   B  1 420  ? -14.056 5.841   107.978 1.00 28.78 ? 418  PRO   B CA    1 
ATOM   11743 C  C     . PRO   B  1 420  ? -14.139 6.939   109.028 1.00 30.12 ? 418  PRO   B C     1 
ATOM   11744 O  O     . PRO   B  1 420  ? -14.848 6.811   110.030 1.00 30.22 ? 418  PRO   B O     1 
ATOM   11745 C  CB    . PRO   B  1 420  ? -15.389 5.673   107.230 1.00 26.42 ? 418  PRO   B CB    1 
ATOM   11746 C  CG    . PRO   B  1 420  ? -15.603 4.182   107.123 1.00 25.98 ? 418  PRO   B CG    1 
ATOM   11747 C  CD    . PRO   B  1 420  ? -14.996 3.636   108.398 1.00 26.14 ? 418  PRO   B CD    1 
ATOM   11748 N  N     . GLN   B  1 421  ? -13.425 8.033   108.775 1.00 25.89 ? 419  GLN   B N     1 
ATOM   11749 C  CA    . GLN   B  1 421  ? -13.356 9.172   109.688 1.00 28.78 ? 419  GLN   B CA    1 
ATOM   11750 C  C     . GLN   B  1 421  ? -13.779 10.404  108.907 1.00 26.01 ? 419  GLN   B C     1 
ATOM   11751 O  O     . GLN   B  1 421  ? -13.011 10.928  108.101 1.00 25.22 ? 419  GLN   B O     1 
ATOM   11752 C  CB    . GLN   B  1 421  ? -11.949 9.326   110.261 1.00 23.85 ? 419  GLN   B CB    1 
ATOM   11753 C  CG    . GLN   B  1 421  ? -11.514 8.131   111.069 1.00 26.49 ? 419  GLN   B CG    1 
ATOM   11754 C  CD    . GLN   B  1 421  ? -10.031 8.123   111.346 1.00 28.07 ? 419  GLN   B CD    1 
ATOM   11755 O  OE1   . GLN   B  1 421  ? -9.599  8.045   112.502 1.00 27.76 ? 419  GLN   B OE1   1 
ATOM   11756 N  NE2   . GLN   B  1 421  ? -9.239  8.176   110.287 1.00 21.88 ? 419  GLN   B NE2   1 
ATOM   11757 N  N     . PHE   B  1 422  ? -14.998 10.874  109.138 1.00 26.11 ? 420  PHE   B N     1 
ATOM   11758 C  CA    . PHE   B  1 422  ? -15.563 11.930  108.305 1.00 24.53 ? 420  PHE   B CA    1 
ATOM   11759 C  C     . PHE   B  1 422  ? -15.254 13.285  108.930 1.00 25.83 ? 420  PHE   B C     1 
ATOM   11760 O  O     . PHE   B  1 422  ? -15.958 13.747  109.832 1.00 25.65 ? 420  PHE   B O     1 
ATOM   11761 C  CB    . PHE   B  1 422  ? -17.056 11.693  108.119 1.00 25.10 ? 420  PHE   B CB    1 
ATOM   11762 C  CG    . PHE   B  1 422  ? -17.359 10.383  107.464 1.00 28.13 ? 420  PHE   B CG    1 
ATOM   11763 C  CD1   . PHE   B  1 422  ? -16.985 10.159  106.146 1.00 29.45 ? 420  PHE   B CD1   1 
ATOM   11764 C  CD2   . PHE   B  1 422  ? -17.991 9.368   108.160 1.00 29.53 ? 420  PHE   B CD2   1 
ATOM   11765 C  CE1   . PHE   B  1 422  ? -17.251 8.947   105.526 1.00 32.10 ? 420  PHE   B CE1   1 
ATOM   11766 C  CE2   . PHE   B  1 422  ? -18.271 8.151   107.540 1.00 32.98 ? 420  PHE   B CE2   1 
ATOM   11767 C  CZ    . PHE   B  1 422  ? -17.898 7.947   106.217 1.00 29.83 ? 420  PHE   B CZ    1 
ATOM   11768 N  N     . ALA   B  1 423  ? -14.186 13.924  108.444 1.00 23.81 ? 421  ALA   B N     1 
ATOM   11769 C  CA    . ALA   B  1 423  ? -13.774 15.248  108.902 1.00 25.50 ? 421  ALA   B CA    1 
ATOM   11770 C  C     . ALA   B  1 423  ? -14.535 16.310  108.118 1.00 27.02 ? 421  ALA   B C     1 
ATOM   11771 O  O     . ALA   B  1 423  ? -14.305 16.489  106.917 1.00 26.66 ? 421  ALA   B O     1 
ATOM   11772 C  CB    . ALA   B  1 423  ? -12.269 15.439  108.722 1.00 21.25 ? 421  ALA   B CB    1 
ATOM   11773 N  N     . THR   B  1 424  ? -15.414 17.038  108.799 1.00 28.85 ? 422  THR   B N     1 
ATOM   11774 C  CA    . THR   B  1 424  ? -16.107 18.159  108.185 1.00 27.89 ? 422  THR   B CA    1 
ATOM   11775 C  C     . THR   B  1 424  ? -16.704 19.024  109.279 1.00 27.22 ? 422  THR   B C     1 
ATOM   11776 O  O     . THR   B  1 424  ? -17.080 18.527  110.344 1.00 28.05 ? 422  THR   B O     1 
ATOM   11777 C  CB    . THR   B  1 424  ? -17.214 17.707  107.215 1.00 27.81 ? 422  THR   B CB    1 
ATOM   11778 O  OG1   . THR   B  1 424  ? -17.851 18.866  106.662 1.00 25.16 ? 422  THR   B OG1   1 
ATOM   11779 C  CG2   . THR   B  1 424  ? -18.262 16.854  107.935 1.00 27.79 ? 422  THR   B CG2   1 
ATOM   11780 N  N     . HIS   B  1 425  ? -16.767 20.325  109.010 1.00 28.46 ? 423  HIS   B N     1 
ATOM   11781 C  CA    . HIS   B  1 425  ? -17.509 21.264  109.841 1.00 27.71 ? 423  HIS   B CA    1 
ATOM   11782 C  C     . HIS   B  1 425  ? -18.846 21.647  109.230 1.00 33.71 ? 423  HIS   B C     1 
ATOM   11783 O  O     . HIS   B  1 425  ? -19.527 22.532  109.758 1.00 33.86 ? 423  HIS   B O     1 
ATOM   11784 C  CB    . HIS   B  1 425  ? -16.694 22.526  110.075 1.00 26.51 ? 423  HIS   B CB    1 
ATOM   11785 C  CG    . HIS   B  1 425  ? -15.432 22.290  110.839 1.00 31.63 ? 423  HIS   B CG    1 
ATOM   11786 N  ND1   . HIS   B  1 425  ? -14.281 23.016  110.616 1.00 34.51 ? 423  HIS   B ND1   1 
ATOM   11787 C  CD2   . HIS   B  1 425  ? -15.136 21.402  111.816 1.00 30.57 ? 423  HIS   B CD2   1 
ATOM   11788 C  CE1   . HIS   B  1 425  ? -13.331 22.588  111.429 1.00 31.51 ? 423  HIS   B CE1   1 
ATOM   11789 N  NE2   . HIS   B  1 425  ? -13.825 21.610  112.168 1.00 30.09 ? 423  HIS   B NE2   1 
ATOM   11790 N  N     . ASN   B  1 426  ? -19.218 21.024  108.117 1.00 30.53 ? 424  ASN   B N     1 
ATOM   11791 C  CA    . ASN   B  1 426  ? -20.401 21.406  107.362 1.00 30.70 ? 424  ASN   B CA    1 
ATOM   11792 C  C     . ASN   B  1 426  ? -21.579 20.560  107.832 1.00 28.32 ? 424  ASN   B C     1 
ATOM   11793 O  O     . ASN   B  1 426  ? -21.578 19.334  107.662 1.00 28.38 ? 424  ASN   B O     1 
ATOM   11794 C  CB    . ASN   B  1 426  ? -20.134 21.223  105.869 1.00 26.96 ? 424  ASN   B CB    1 
ATOM   11795 C  CG    . ASN   B  1 426  ? -21.238 21.768  105.000 1.00 30.50 ? 424  ASN   B CG    1 
ATOM   11796 O  OD1   . ASN   B  1 426  ? -22.418 21.634  105.315 1.00 30.37 ? 424  ASN   B OD1   1 
ATOM   11797 N  ND2   . ASN   B  1 426  ? -20.859 22.374  103.878 1.00 30.11 ? 424  ASN   B ND2   1 
ATOM   11798 N  N     . ALA   B  1 427  ? -22.587 21.219  108.415 1.00 34.27 ? 425  ALA   B N     1 
ATOM   11799 C  CA    . ALA   B  1 427  ? -23.716 20.496  108.994 1.00 36.71 ? 425  ALA   B CA    1 
ATOM   11800 C  C     . ALA   B  1 427  ? -24.502 19.726  107.942 1.00 30.73 ? 425  ALA   B C     1 
ATOM   11801 O  O     . ALA   B  1 427  ? -25.081 18.671  108.246 1.00 27.58 ? 425  ALA   B O     1 
ATOM   11802 C  CB    . ALA   B  1 427  ? -24.637 21.468  109.732 1.00 37.24 ? 425  ALA   B CB    1 
ATOM   11803 N  N     . GLN   B  1 428  ? -24.535 20.228  106.708 1.00 30.13 ? 426  GLN   B N     1 
ATOM   11804 C  CA    . GLN   B  1 428  ? -25.234 19.509  105.647 1.00 33.44 ? 426  GLN   B CA    1 
ATOM   11805 C  C     . GLN   B  1 428  ? -24.483 18.239  105.273 1.00 32.64 ? 426  GLN   B C     1 
ATOM   11806 O  O     . GLN   B  1 428  ? -25.083 17.162  105.168 1.00 31.11 ? 426  GLN   B O     1 
ATOM   11807 C  CB    . GLN   B  1 428  ? -25.424 20.416  104.429 1.00 32.10 ? 426  GLN   B CB    1 
ATOM   11808 C  CG    . GLN   B  1 428  ? -26.449 19.903  103.410 1.00 36.17 ? 426  GLN   B CG    1 
ATOM   11809 C  CD    . GLN   B  1 428  ? -25.936 18.739  102.575 1.00 35.19 ? 426  GLN   B CD    1 
ATOM   11810 O  OE1   . GLN   B  1 428  ? -24.751 18.680  102.231 1.00 37.36 ? 426  GLN   B OE1   1 
ATOM   11811 N  NE2   . GLN   B  1 428  ? -26.821 17.799  102.261 1.00 34.11 ? 426  GLN   B NE2   1 
ATOM   11812 N  N     . THR   B  1 429  ? -23.163 18.351  105.068 1.00 31.38 ? 427  THR   B N     1 
ATOM   11813 C  CA    . THR   B  1 429  ? -22.344 17.174  104.804 1.00 33.30 ? 427  THR   B CA    1 
ATOM   11814 C  C     . THR   B  1 429  ? -22.497 16.141  105.911 1.00 29.76 ? 427  THR   B C     1 
ATOM   11815 O  O     . THR   B  1 429  ? -22.716 14.951  105.649 1.00 28.66 ? 427  THR   B O     1 
ATOM   11816 C  CB    . THR   B  1 429  ? -20.875 17.581  104.668 1.00 28.50 ? 427  THR   B CB    1 
ATOM   11817 O  OG1   . THR   B  1 429  ? -20.780 18.736  103.834 1.00 29.69 ? 427  THR   B OG1   1 
ATOM   11818 C  CG2   . THR   B  1 429  ? -20.064 16.449  104.072 1.00 29.52 ? 427  THR   B CG2   1 
ATOM   11819 N  N     . LEU   B  1 430  ? -22.360 16.583  107.164 1.00 31.90 ? 428  LEU   B N     1 
ATOM   11820 C  CA    . LEU   B  1 430  ? -22.497 15.684  108.301 1.00 31.46 ? 428  LEU   B CA    1 
ATOM   11821 C  C     . LEU   B  1 430  ? -23.835 14.959  108.256 1.00 31.86 ? 428  LEU   B C     1 
ATOM   11822 O  O     . LEU   B  1 430  ? -23.900 13.729  108.368 1.00 30.60 ? 428  LEU   B O     1 
ATOM   11823 C  CB    . LEU   B  1 430  ? -22.358 16.489  109.594 1.00 32.80 ? 428  LEU   B CB    1 
ATOM   11824 C  CG    . LEU   B  1 430  ? -22.126 15.824  110.950 1.00 31.54 ? 428  LEU   B CG    1 
ATOM   11825 C  CD1   . LEU   B  1 430  ? -21.844 16.911  111.967 1.00 35.69 ? 428  LEU   B CD1   1 
ATOM   11826 C  CD2   . LEU   B  1 430  ? -23.304 14.977  111.414 1.00 35.42 ? 428  LEU   B CD2   1 
ATOM   11827 N  N     . ALA   B  1 431  ? -24.917 15.717  108.087 1.00 30.92 ? 429  ALA   B N     1 
ATOM   11828 C  CA    . ALA   B  1 431  ? -26.250 15.126  108.146 1.00 32.11 ? 429  ALA   B CA    1 
ATOM   11829 C  C     . ALA   B  1 431  ? -26.446 14.089  107.049 1.00 34.22 ? 429  ALA   B C     1 
ATOM   11830 O  O     . ALA   B  1 431  ? -27.029 13.021  107.289 1.00 35.74 ? 429  ALA   B O     1 
ATOM   11831 C  CB    . ALA   B  1 431  ? -27.309 16.221  108.046 1.00 33.33 ? 429  ALA   B CB    1 
ATOM   11832 N  N     . ALA   B  1 432  ? -25.952 14.383  105.838 1.00 34.12 ? 430  ALA   B N     1 
ATOM   11833 C  CA    . ALA   B  1 432  ? -26.089 13.441  104.732 1.00 30.16 ? 430  ALA   B CA    1 
ATOM   11834 C  C     . ALA   B  1 432  ? -25.380 12.133  105.040 1.00 32.73 ? 430  ALA   B C     1 
ATOM   11835 O  O     . ALA   B  1 432  ? -25.868 11.055  104.687 1.00 33.36 ? 430  ALA   B O     1 
ATOM   11836 C  CB    . ALA   B  1 432  ? -25.541 14.058  103.440 1.00 31.17 ? 430  ALA   B CB    1 
ATOM   11837 N  N     . ILE   B  1 433  ? -24.227 12.204  105.707 1.00 33.00 ? 431  ILE   B N     1 
ATOM   11838 C  CA    . ILE   B  1 433  ? -23.507 10.978  106.019 1.00 36.15 ? 431  ILE   B CA    1 
ATOM   11839 C  C     . ILE   B  1 433  ? -24.129 10.280  107.219 1.00 31.76 ? 431  ILE   B C     1 
ATOM   11840 O  O     . ILE   B  1 433  ? -24.264 9.052   107.238 1.00 32.00 ? 431  ILE   B O     1 
ATOM   11841 C  CB    . ILE   B  1 433  ? -22.018 11.285  106.239 1.00 33.33 ? 431  ILE   B CB    1 
ATOM   11842 C  CG1   . ILE   B  1 433  ? -21.409 11.778  104.931 1.00 37.12 ? 431  ILE   B CG1   1 
ATOM   11843 C  CG2   . ILE   B  1 433  ? -21.285 10.047  106.736 1.00 31.65 ? 431  ILE   B CG2   1 
ATOM   11844 C  CD1   . ILE   B  1 433  ? -19.991 12.162  105.073 1.00 34.78 ? 431  ILE   B CD1   1 
ATOM   11845 N  N     . TYR   B  1 434  ? -24.510 11.054  108.233 1.00 31.68 ? 432  TYR   B N     1 
ATOM   11846 C  CA    . TYR   B  1 434  ? -25.194 10.499  109.395 1.00 32.56 ? 432  TYR   B CA    1 
ATOM   11847 C  C     . TYR   B  1 434  ? -26.366 9.614   108.981 1.00 36.57 ? 432  TYR   B C     1 
ATOM   11848 O  O     . TYR   B  1 434  ? -26.493 8.467   109.428 1.00 35.13 ? 432  TYR   B O     1 
ATOM   11849 C  CB    . TYR   B  1 434  ? -25.648 11.656  110.282 1.00 35.62 ? 432  TYR   B CB    1 
ATOM   11850 C  CG    . TYR   B  1 434  ? -26.583 11.276  111.389 1.00 35.05 ? 432  TYR   B CG    1 
ATOM   11851 C  CD1   . TYR   B  1 434  ? -26.138 10.536  112.475 1.00 39.71 ? 432  TYR   B CD1   1 
ATOM   11852 C  CD2   . TYR   B  1 434  ? -27.914 11.673  111.359 1.00 40.38 ? 432  TYR   B CD2   1 
ATOM   11853 C  CE1   . TYR   B  1 434  ? -27.002 10.191  113.504 1.00 41.46 ? 432  TYR   B CE1   1 
ATOM   11854 C  CE2   . TYR   B  1 434  ? -28.776 11.341  112.375 1.00 37.55 ? 432  TYR   B CE2   1 
ATOM   11855 C  CZ    . TYR   B  1 434  ? -28.319 10.600  113.446 1.00 40.38 ? 432  TYR   B CZ    1 
ATOM   11856 O  OH    . TYR   B  1 434  ? -29.183 10.266  114.462 1.00 42.76 ? 432  TYR   B OH    1 
ATOM   11857 N  N     . HIS   B  1 435  ? -27.212 10.114  108.087 1.00 33.92 ? 433  HIS   B N     1 
ATOM   11858 C  CA    . HIS   B  1 435  ? -28.347 9.317   107.641 1.00 38.69 ? 433  HIS   B CA    1 
ATOM   11859 C  C     . HIS   B  1 435  ? -27.927 8.221   106.666 1.00 40.10 ? 433  HIS   B C     1 
ATOM   11860 O  O     . HIS   B  1 435  ? -28.486 7.121   106.693 1.00 35.20 ? 433  HIS   B O     1 
ATOM   11861 C  CB    . HIS   B  1 435  ? -29.402 10.235  107.034 1.00 39.42 ? 433  HIS   B CB    1 
ATOM   11862 C  CG    . HIS   B  1 435  ? -30.126 11.052  108.055 1.00 41.07 ? 433  HIS   B CG    1 
ATOM   11863 N  ND1   . HIS   B  1 435  ? -31.115 10.527  108.857 1.00 42.13 ? 433  HIS   B ND1   1 
ATOM   11864 C  CD2   . HIS   B  1 435  ? -29.979 12.343  108.435 1.00 40.75 ? 433  HIS   B CD2   1 
ATOM   11865 C  CE1   . HIS   B  1 435  ? -31.562 11.464  109.672 1.00 41.80 ? 433  HIS   B CE1   1 
ATOM   11866 N  NE2   . HIS   B  1 435  ? -30.895 12.577  109.432 1.00 41.43 ? 433  HIS   B NE2   1 
ATOM   11867 N  N     . MET   B  1 436  ? -26.925 8.484   105.824 1.00 37.28 ? 434  MET   B N     1 
ATOM   11868 C  CA    . MET   B  1 436  ? -26.463 7.464   104.889 1.00 33.88 ? 434  MET   B CA    1 
ATOM   11869 C  C     . MET   B  1 436  ? -25.935 6.235   105.610 1.00 38.55 ? 434  MET   B C     1 
ATOM   11870 O  O     . MET   B  1 436  ? -26.043 5.116   105.096 1.00 37.60 ? 434  MET   B O     1 
ATOM   11871 C  CB    . MET   B  1 436  ? -25.370 8.038   103.987 1.00 34.99 ? 434  MET   B CB    1 
ATOM   11872 C  CG    . MET   B  1 436  ? -24.745 7.031   103.045 1.00 38.66 ? 434  MET   B CG    1 
ATOM   11873 S  SD    . MET   B  1 436  ? -23.257 7.698   102.270 1.00 42.05 ? 434  MET   B SD    1 
ATOM   11874 C  CE    . MET   B  1 436  ? -23.940 9.138   101.463 1.00 35.99 ? 434  MET   B CE    1 
ATOM   11875 N  N     . ALA   B  1 437  ? -25.357 6.419   106.798 1.00 35.64 ? 435  ALA   B N     1 
ATOM   11876 C  CA    . ALA   B  1 437  ? -24.711 5.306   107.480 1.00 36.75 ? 435  ALA   B CA    1 
ATOM   11877 C  C     . ALA   B  1 437  ? -25.726 4.320   108.043 1.00 42.22 ? 435  ALA   B C     1 
ATOM   11878 O  O     . ALA   B  1 437  ? -25.414 3.135   108.205 1.00 43.86 ? 435  ALA   B O     1 
ATOM   11879 C  CB    . ALA   B  1 437  ? -23.806 5.834   108.590 1.00 37.18 ? 435  ALA   B CB    1 
ATOM   11880 N  N     . GLY   B  1 438  ? -26.932 4.780   108.342 1.00 41.99 ? 436  GLY   B N     1 
ATOM   11881 C  CA    . GLY   B  1 438  ? -27.963 3.910   108.872 1.00 45.33 ? 436  GLY   B CA    1 
ATOM   11882 C  C     . GLY   B  1 438  ? -28.040 3.957   110.384 1.00 50.84 ? 436  GLY   B C     1 
ATOM   11883 O  O     . GLY   B  1 438  ? -27.432 4.796   111.057 1.00 45.83 ? 436  GLY   B O     1 
ATOM   11884 N  N     . LYS   B  1 439  ? -28.806 3.010   110.924 1.00 48.51 ? 437  LYS   B N     1 
ATOM   11885 C  CA    . LYS   B  1 439  ? -29.126 3.000   112.343 1.00 45.57 ? 437  LYS   B CA    1 
ATOM   11886 C  C     . LYS   B  1 439  ? -28.271 2.041   113.165 1.00 50.10 ? 437  LYS   B C     1 
ATOM   11887 O  O     . LYS   B  1 439  ? -28.259 2.153   114.396 1.00 51.04 ? 437  LYS   B O     1 
ATOM   11888 C  CB    . LYS   B  1 439  ? -30.610 2.643   112.538 1.00 45.83 ? 437  LYS   B CB    1 
ATOM   11889 N  N     . ASP   B  1 440  ? -27.572 1.098   112.532 1.00 46.55 ? 438  ASP   B N     1 
ATOM   11890 C  CA    . ASP   B  1 440  ? -26.812 0.083   113.264 1.00 50.78 ? 438  ASP   B CA    1 
ATOM   11891 C  C     . ASP   B  1 440  ? -25.414 0.628   113.515 1.00 53.16 ? 438  ASP   B C     1 
ATOM   11892 O  O     . ASP   B  1 440  ? -24.499 0.430   112.713 1.00 60.51 ? 438  ASP   B O     1 
ATOM   11893 C  CB    . ASP   B  1 440  ? -26.765 -1.228  112.490 1.00 52.38 ? 438  ASP   B CB    1 
ATOM   11894 N  N     . PHE   B  1 441  ? -25.238 1.323   114.639 1.00 46.99 ? 439  PHE   B N     1 
ATOM   11895 C  CA    . PHE   B  1 441  ? -23.967 1.971   114.943 1.00 52.38 ? 439  PHE   B CA    1 
ATOM   11896 C  C     . PHE   B  1 441  ? -23.343 1.398   116.207 1.00 53.94 ? 439  PHE   B C     1 
ATOM   11897 O  O     . PHE   B  1 441  ? -23.999 1.309   117.250 1.00 48.91 ? 439  PHE   B O     1 
ATOM   11898 C  CB    . PHE   B  1 441  ? -24.104 3.488   115.105 1.00 44.57 ? 439  PHE   B CB    1 
ATOM   11899 C  CG    . PHE   B  1 441  ? -22.774 4.187   115.259 1.00 48.41 ? 439  PHE   B CG    1 
ATOM   11900 C  CD1   . PHE   B  1 441  ? -22.166 4.300   116.502 1.00 44.13 ? 439  PHE   B CD1   1 
ATOM   11901 C  CD2   . PHE   B  1 441  ? -22.116 4.695   114.153 1.00 44.32 ? 439  PHE   B CD2   1 
ATOM   11902 C  CE1   . PHE   B  1 441  ? -20.935 4.919   116.639 1.00 42.32 ? 439  PHE   B CE1   1 
ATOM   11903 C  CE2   . PHE   B  1 441  ? -20.891 5.319   114.284 1.00 43.79 ? 439  PHE   B CE2   1 
ATOM   11904 C  CZ    . PHE   B  1 441  ? -20.299 5.425   115.528 1.00 42.19 ? 439  PHE   B CZ    1 
ATOM   11905 N  N     . HIS   B  1 442  ? -22.062 1.049   116.103 1.00 52.91 ? 440  HIS   B N     1 
ATOM   11906 C  CA    . HIS   B  1 442  ? -21.202 0.748   117.234 1.00 49.49 ? 440  HIS   B CA    1 
ATOM   11907 C  C     . HIS   B  1 442  ? -19.949 1.604   117.116 1.00 48.38 ? 440  HIS   B C     1 
ATOM   11908 O  O     . HIS   B  1 442  ? -19.519 1.942   116.010 1.00 46.58 ? 440  HIS   B O     1 
ATOM   11909 C  CB    . HIS   B  1 442  ? -20.822 -0.746  117.276 1.00 51.34 ? 440  HIS   B CB    1 
ATOM   11910 C  CG    . HIS   B  1 442  ? -20.002 -1.200  116.103 1.00 54.31 ? 440  HIS   B CG    1 
ATOM   11911 N  ND1   . HIS   B  1 442  ? -18.622 -1.186  116.106 1.00 53.07 ? 440  HIS   B ND1   1 
ATOM   11912 C  CD2   . HIS   B  1 442  ? -20.370 -1.683  114.890 1.00 51.94 ? 440  HIS   B CD2   1 
ATOM   11913 C  CE1   . HIS   B  1 442  ? -18.175 -1.639  114.948 1.00 48.27 ? 440  HIS   B CE1   1 
ATOM   11914 N  NE2   . HIS   B  1 442  ? -19.215 -1.950  114.193 1.00 53.39 ? 440  HIS   B NE2   1 
ATOM   11915 N  N     . VAL   B  1 443  ? -19.373 1.978   118.262 1.00 46.43 ? 441  VAL   B N     1 
ATOM   11916 C  CA    . VAL   B  1 443  ? -18.088 2.668   118.233 1.00 40.26 ? 441  VAL   B CA    1 
ATOM   11917 C  C     . VAL   B  1 443  ? -17.069 1.754   117.567 1.00 39.10 ? 441  VAL   B C     1 
ATOM   11918 O  O     . VAL   B  1 443  ? -17.029 0.543   117.818 1.00 43.39 ? 441  VAL   B O     1 
ATOM   11919 C  CB    . VAL   B  1 443  ? -17.665 3.087   119.649 1.00 44.85 ? 441  VAL   B CB    1 
ATOM   11920 C  CG1   . VAL   B  1 443  ? -16.314 3.794   119.618 1.00 36.63 ? 441  VAL   B CG1   1 
ATOM   11921 C  CG2   . VAL   B  1 443  ? -18.714 4.006   120.254 1.00 46.00 ? 441  VAL   B CG2   1 
ATOM   11922 N  N     . GLY   B  1 444  ? -16.268 2.322   116.673 1.00 41.22 ? 442  GLY   B N     1 
ATOM   11923 C  CA    . GLY   B  1 444  ? -15.391 1.545   115.828 1.00 37.35 ? 442  GLY   B CA    1 
ATOM   11924 C  C     . GLY   B  1 444  ? -15.922 1.308   114.428 1.00 38.63 ? 442  GLY   B C     1 
ATOM   11925 O  O     . GLY   B  1 444  ? -15.152 0.891   113.556 1.00 35.27 ? 442  GLY   B O     1 
ATOM   11926 N  N     . LYS   B  1 445  ? -17.215 1.542   114.196 1.00 37.48 ? 443  LYS   B N     1 
ATOM   11927 C  CA    . LYS   B  1 445  ? -17.755 1.448   112.843 1.00 37.04 ? 443  LYS   B CA    1 
ATOM   11928 C  C     . LYS   B  1 445  ? -17.221 2.582   111.985 1.00 38.92 ? 443  LYS   B C     1 
ATOM   11929 O  O     . LYS   B  1 445  ? -16.524 2.354   110.991 1.00 34.89 ? 443  LYS   B O     1 
ATOM   11930 C  CB    . LYS   B  1 445  ? -19.283 1.475   112.878 1.00 37.48 ? 443  LYS   B CB    1 
ATOM   11931 N  N     . TYR   B  1 446  ? -17.540 3.814   112.370 1.00 36.90 ? 444  TYR   B N     1 
ATOM   11932 C  CA    . TYR   B  1 446  ? -16.973 5.017   111.787 1.00 35.20 ? 444  TYR   B CA    1 
ATOM   11933 C  C     . TYR   B  1 446  ? -17.005 6.094   112.863 1.00 35.11 ? 444  TYR   B C     1 
ATOM   11934 O  O     . TYR   B  1 446  ? -17.517 5.880   113.968 1.00 35.61 ? 444  TYR   B O     1 
ATOM   11935 C  CB    . TYR   B  1 446  ? -17.742 5.444   110.531 1.00 31.27 ? 444  TYR   B CB    1 
ATOM   11936 C  CG    . TYR   B  1 446  ? -19.127 5.989   110.806 1.00 34.80 ? 444  TYR   B CG    1 
ATOM   11937 C  CD1   . TYR   B  1 446  ? -19.330 7.338   111.070 1.00 37.69 ? 444  TYR   B CD1   1 
ATOM   11938 C  CD2   . TYR   B  1 446  ? -20.238 5.156   110.778 1.00 37.24 ? 444  TYR   B CD2   1 
ATOM   11939 C  CE1   . TYR   B  1 446  ? -20.594 7.835   111.320 1.00 38.35 ? 444  TYR   B CE1   1 
ATOM   11940 C  CE2   . TYR   B  1 446  ? -21.497 5.644   111.021 1.00 41.09 ? 444  TYR   B CE2   1 
ATOM   11941 C  CZ    . TYR   B  1 446  ? -21.672 6.986   111.291 1.00 42.83 ? 444  TYR   B CZ    1 
ATOM   11942 O  OH    . TYR   B  1 446  ? -22.941 7.474   111.530 1.00 44.02 ? 444  TYR   B OH    1 
ATOM   11943 N  N     . GLU   B  1 447  ? -16.467 7.265   112.533 1.00 32.15 ? 445  GLU   B N     1 
ATOM   11944 C  CA    . GLU   B  1 447  ? -16.533 8.403   113.432 1.00 28.99 ? 445  GLU   B CA    1 
ATOM   11945 C  C     . GLU   B  1 447  ? -16.515 9.677   112.609 1.00 29.53 ? 445  GLU   B C     1 
ATOM   11946 O  O     . GLU   B  1 447  ? -16.161 9.670   111.432 1.00 27.95 ? 445  GLU   B O     1 
ATOM   11947 C  CB    . GLU   B  1 447  ? -15.362 8.406   114.414 1.00 25.99 ? 445  GLU   B CB    1 
ATOM   11948 C  CG    . GLU   B  1 447  ? -14.064 8.834   113.736 1.00 25.91 ? 445  GLU   B CG    1 
ATOM   11949 C  CD    . GLU   B  1 447  ? -12.877 8.768   114.664 1.00 29.82 ? 445  GLU   B CD    1 
ATOM   11950 O  OE1   . GLU   B  1 447  ? -13.067 8.369   115.831 1.00 28.22 ? 445  GLU   B OE1   1 
ATOM   11951 O  OE2   . GLU   B  1 447  ? -11.757 9.097   114.215 1.00 27.96 ? 445  GLU   B OE2   1 
ATOM   11952 N  N     . PHE   B  1 448  ? -16.890 10.776  113.243 1.00 29.58 ? 446  PHE   B N     1 
ATOM   11953 C  CA    . PHE   B  1 448  ? -16.682 12.092  112.665 1.00 28.96 ? 446  PHE   B CA    1 
ATOM   11954 C  C     . PHE   B  1 448  ? -15.403 12.710  113.218 1.00 25.53 ? 446  PHE   B C     1 
ATOM   11955 O  O     . PHE   B  1 448  ? -14.830 12.236  114.200 1.00 28.12 ? 446  PHE   B O     1 
ATOM   11956 C  CB    . PHE   B  1 448  ? -17.864 13.007  112.954 1.00 29.57 ? 446  PHE   B CB    1 
ATOM   11957 C  CG    . PHE   B  1 448  ? -19.110 12.612  112.249 1.00 29.28 ? 446  PHE   B CG    1 
ATOM   11958 C  CD1   . PHE   B  1 448  ? -19.266 12.884  110.902 1.00 30.18 ? 446  PHE   B CD1   1 
ATOM   11959 C  CD2   . PHE   B  1 448  ? -20.125 11.964  112.926 1.00 32.81 ? 446  PHE   B CD2   1 
ATOM   11960 C  CE1   . PHE   B  1 448  ? -20.414 12.518  110.235 1.00 30.63 ? 446  PHE   B CE1   1 
ATOM   11961 C  CE2   . PHE   B  1 448  ? -21.276 11.594  112.266 1.00 38.25 ? 446  PHE   B CE2   1 
ATOM   11962 C  CZ    . PHE   B  1 448  ? -21.418 11.877  110.915 1.00 32.55 ? 446  PHE   B CZ    1 
ATOM   11963 N  N     . GLN   B  1 449  ? -14.964 13.791  112.578 1.00 29.47 ? 447  GLN   B N     1 
ATOM   11964 C  CA    . GLN   B  1 449  ? -13.788 14.510  113.041 1.00 27.67 ? 447  GLN   B CA    1 
ATOM   11965 C  C     . GLN   B  1 449  ? -13.974 16.001  112.819 1.00 27.77 ? 447  GLN   B C     1 
ATOM   11966 O  O     . GLN   B  1 449  ? -14.693 16.427  111.913 1.00 28.18 ? 447  GLN   B O     1 
ATOM   11967 C  CB    . GLN   B  1 449  ? -12.518 14.044  112.335 1.00 22.07 ? 447  GLN   B CB    1 
ATOM   11968 C  CG    . GLN   B  1 449  ? -12.167 12.598  112.582 1.00 24.62 ? 447  GLN   B CG    1 
ATOM   11969 C  CD    . GLN   B  1 449  ? -10.710 12.323  112.308 1.00 24.54 ? 447  GLN   B CD    1 
ATOM   11970 O  OE1   . GLN   B  1 449  ? -10.005 13.176  111.772 1.00 25.61 ? 447  GLN   B OE1   1 
ATOM   11971 N  NE2   . GLN   B  1 449  ? -10.246 11.138  112.676 1.00 24.28 ? 447  GLN   B NE2   1 
ATOM   11972 N  N     . CYS   B  1 450  ? -13.318 16.791  113.661 1.00 24.86 ? 448  CYS   B N     1 
ATOM   11973 C  CA    . CYS   B  1 450  ? -13.411 18.238  113.561 1.00 27.91 ? 448  CYS   B CA    1 
ATOM   11974 C  C     . CYS   B  1 450  ? -12.124 18.850  114.085 1.00 25.22 ? 448  CYS   B C     1 
ATOM   11975 O  O     . CYS   B  1 450  ? -11.294 18.177  114.701 1.00 24.55 ? 448  CYS   B O     1 
ATOM   11976 C  CB    . CYS   B  1 450  ? -14.610 18.773  114.336 1.00 28.80 ? 448  CYS   B CB    1 
ATOM   11977 S  SG    . CYS   B  1 450  ? -14.328 18.782  116.123 1.00 28.37 ? 448  CYS   B SG    1 
ATOM   11978 N  N     . LEU   B  1 451  ? -11.951 20.137  113.804 1.00 25.81 ? 449  LEU   B N     1 
ATOM   11979 C  CA    . LEU   B  1 451  ? -10.775 20.867  114.248 1.00 26.60 ? 449  LEU   B CA    1 
ATOM   11980 C  C     . LEU   B  1 451  ? -11.031 21.453  115.628 1.00 32.14 ? 449  LEU   B C     1 
ATOM   11981 O  O     . LEU   B  1 451  ? -12.145 21.892  115.936 1.00 26.20 ? 449  LEU   B O     1 
ATOM   11982 C  CB    . LEU   B  1 451  ? -10.409 21.981  113.260 1.00 29.59 ? 449  LEU   B CB    1 
ATOM   11983 N  N     . HIS   B  1 452  ? -9.995  21.436  116.464 1.00 30.67 ? 450  HIS   B N     1 
ATOM   11984 C  CA    . HIS   B  1 452  ? -10.085 22.051  117.781 1.00 31.96 ? 450  HIS   B CA    1 
ATOM   11985 C  C     . HIS   B  1 452  ? -10.459 23.522  117.660 1.00 27.77 ? 450  HIS   B C     1 
ATOM   11986 O  O     . HIS   B  1 452  ? -9.986  24.230  116.773 1.00 30.27 ? 450  HIS   B O     1 
ATOM   11987 C  CB    . HIS   B  1 452  ? -8.752  21.911  118.526 1.00 26.54 ? 450  HIS   B CB    1 
ATOM   11988 C  CG    . HIS   B  1 452  ? -8.649  22.798  119.729 1.00 29.40 ? 450  HIS   B CG    1 
ATOM   11989 N  ND1   . HIS   B  1 452  ? -9.126  22.431  120.969 1.00 31.43 ? 450  HIS   B ND1   1 
ATOM   11990 C  CD2   . HIS   B  1 452  ? -8.151  24.049  119.872 1.00 30.62 ? 450  HIS   B CD2   1 
ATOM   11991 C  CE1   . HIS   B  1 452  ? -8.916  23.414  121.827 1.00 32.14 ? 450  HIS   B CE1   1 
ATOM   11992 N  NE2   . HIS   B  1 452  ? -8.326  24.407  121.186 1.00 32.12 ? 450  HIS   B NE2   1 
ATOM   11993 N  N     . GLY   B  1 453  ? -11.334 23.981  118.553 1.00 34.45 ? 451  GLY   B N     1 
ATOM   11994 C  CA    . GLY   B  1 453  ? -11.697 25.381  118.605 1.00 33.85 ? 451  GLY   B CA    1 
ATOM   11995 C  C     . GLY   B  1 453  ? -12.649 25.839  117.526 1.00 41.10 ? 451  GLY   B C     1 
ATOM   11996 O  O     . GLY   B  1 453  ? -13.146 26.967  117.600 1.00 47.40 ? 451  GLY   B O     1 
ATOM   11997 N  N     . MET   B  1 454  ? -12.921 25.009  116.534 1.00 39.46 ? 452  MET   B N     1 
ATOM   11998 C  CA    . MET   B  1 454  ? -13.851 25.314  115.459 1.00 37.92 ? 452  MET   B CA    1 
ATOM   11999 C  C     . MET   B  1 454  ? -15.005 24.331  115.393 1.00 35.16 ? 452  MET   B C     1 
ATOM   12000 O  O     . MET   B  1 454  ? -16.151 24.741  115.192 1.00 40.06 ? 452  MET   B O     1 
ATOM   12001 C  CB    . MET   B  1 454  ? -13.105 25.323  114.112 1.00 38.05 ? 452  MET   B CB    1 
ATOM   12002 C  CG    . MET   B  1 454  ? -13.897 25.915  112.945 1.00 38.71 ? 452  MET   B CG    1 
ATOM   12003 S  SD    . MET   B  1 454  ? -14.164 27.680  113.185 1.00 61.95 ? 452  MET   B SD    1 
ATOM   12004 C  CE    . MET   B  1 454  ? -12.500 28.219  113.588 1.00 48.86 ? 452  MET   B CE    1 
ATOM   12005 N  N     . GLY   B  1 455  ? -14.737 23.044  115.593 1.00 31.78 ? 453  GLY   B N     1 
ATOM   12006 C  CA    . GLY   B  1 455  ? -15.735 22.019  115.378 1.00 33.45 ? 453  GLY   B CA    1 
ATOM   12007 C  C     . GLY   B  1 455  ? -16.618 21.675  116.558 1.00 36.23 ? 453  GLY   B C     1 
ATOM   12008 O  O     . GLY   B  1 455  ? -17.678 21.082  116.367 1.00 34.12 ? 453  GLY   B O     1 
ATOM   12009 N  N     . GLU   B  1 456  ? -16.202 22.009  117.780 1.00 39.67 ? 454  GLU   B N     1 
ATOM   12010 C  CA    . GLU   B  1 456  ? -16.972 21.576  118.944 1.00 41.20 ? 454  GLU   B CA    1 
ATOM   12011 C  C     . GLU   B  1 456  ? -18.387 22.145  119.004 1.00 36.71 ? 454  GLU   B C     1 
ATOM   12012 O  O     . GLU   B  1 456  ? -19.292 21.402  119.418 1.00 38.40 ? 454  GLU   B O     1 
ATOM   12013 C  CB    . GLU   B  1 456  ? -16.212 21.904  120.233 1.00 43.24 ? 454  GLU   B CB    1 
ATOM   12014 C  CG    . GLU   B  1 456  ? -14.877 21.200  120.352 1.00 41.73 ? 454  GLU   B CG    1 
ATOM   12015 C  CD    . GLU   B  1 456  ? -13.738 22.047  119.839 1.00 39.16 ? 454  GLU   B CD    1 
ATOM   12016 O  OE1   . GLU   B  1 456  ? -13.947 22.780  118.848 1.00 44.33 ? 454  GLU   B OE1   1 
ATOM   12017 O  OE2   . GLU   B  1 456  ? -12.637 21.986  120.430 1.00 33.48 ? 454  GLU   B OE2   1 
ATOM   12018 N  N     . PRO   B  1 457  ? -18.651 23.410  118.648 1.00 36.17 ? 455  PRO   B N     1 
ATOM   12019 C  CA    . PRO   B  1 457  ? -20.051 23.868  118.604 1.00 38.10 ? 455  PRO   B CA    1 
ATOM   12020 C  C     . PRO   B  1 457  ? -20.957 22.963  117.784 1.00 41.11 ? 455  PRO   B C     1 
ATOM   12021 O  O     . PRO   B  1 457  ? -22.087 22.675  118.200 1.00 42.57 ? 455  PRO   B O     1 
ATOM   12022 C  CB    . PRO   B  1 457  ? -19.932 25.266  117.983 1.00 40.48 ? 455  PRO   B CB    1 
ATOM   12023 C  CG    . PRO   B  1 457  ? -18.601 25.741  118.413 1.00 41.63 ? 455  PRO   B CG    1 
ATOM   12024 C  CD    . PRO   B  1 457  ? -17.713 24.524  118.407 1.00 37.42 ? 455  PRO   B CD    1 
ATOM   12025 N  N     . LEU   B  1 458  ? -20.485 22.491  116.630 1.00 38.84 ? 456  LEU   B N     1 
ATOM   12026 C  CA    . LEU   B  1 458  ? -21.303 21.596  115.820 1.00 35.53 ? 456  LEU   B CA    1 
ATOM   12027 C  C     . LEU   B  1 458  ? -21.351 20.205  116.427 1.00 36.86 ? 456  LEU   B C     1 
ATOM   12028 O  O     . LEU   B  1 458  ? -22.425 19.607  116.555 1.00 36.36 ? 456  LEU   B O     1 
ATOM   12029 C  CB    . LEU   B  1 458  ? -20.770 21.547  114.385 1.00 32.53 ? 456  LEU   B CB    1 
ATOM   12030 C  CG    . LEU   B  1 458  ? -21.335 20.444  113.486 1.00 34.12 ? 456  LEU   B CG    1 
ATOM   12031 C  CD1   . LEU   B  1 458  ? -22.844 20.611  113.310 1.00 36.11 ? 456  LEU   B CD1   1 
ATOM   12032 C  CD2   . LEU   B  1 458  ? -20.631 20.414  112.130 1.00 30.43 ? 456  LEU   B CD2   1 
ATOM   12033 N  N     . TYR   B  1 459  ? -20.202 19.676  116.831 1.00 33.25 ? 457  TYR   B N     1 
ATOM   12034 C  CA    . TYR   B  1 459  ? -20.197 18.298  117.285 1.00 34.31 ? 457  TYR   B CA    1 
ATOM   12035 C  C     . TYR   B  1 459  ? -20.654 18.136  118.727 1.00 35.11 ? 457  TYR   B C     1 
ATOM   12036 O  O     . TYR   B  1 459  ? -20.911 17.005  119.146 1.00 34.50 ? 457  TYR   B O     1 
ATOM   12037 C  CB    . TYR   B  1 459  ? -18.813 17.702  117.055 1.00 33.29 ? 457  TYR   B CB    1 
ATOM   12038 C  CG    . TYR   B  1 459  ? -18.664 17.384  115.596 1.00 31.46 ? 457  TYR   B CG    1 
ATOM   12039 C  CD1   . TYR   B  1 459  ? -19.184 16.211  115.084 1.00 29.97 ? 457  TYR   B CD1   1 
ATOM   12040 C  CD2   . TYR   B  1 459  ? -18.073 18.283  114.720 1.00 33.78 ? 457  TYR   B CD2   1 
ATOM   12041 C  CE1   . TYR   B  1 459  ? -19.091 15.917  113.759 1.00 33.31 ? 457  TYR   B CE1   1 
ATOM   12042 C  CE2   . TYR   B  1 459  ? -17.960 17.989  113.371 1.00 32.51 ? 457  TYR   B CE2   1 
ATOM   12043 C  CZ    . TYR   B  1 459  ? -18.474 16.801  112.901 1.00 28.24 ? 457  TYR   B CZ    1 
ATOM   12044 O  OH    . TYR   B  1 459  ? -18.387 16.475  111.569 1.00 28.02 ? 457  TYR   B OH    1 
ATOM   12045 N  N     . GLU   B  1 460  ? -20.796 19.230  119.479 1.00 33.74 ? 458  GLU   B N     1 
ATOM   12046 C  CA    . GLU   B  1 460  ? -21.510 19.147  120.747 1.00 43.58 ? 458  GLU   B CA    1 
ATOM   12047 C  C     . GLU   B  1 460  ? -22.948 18.688  120.540 1.00 48.32 ? 458  GLU   B C     1 
ATOM   12048 O  O     . GLU   B  1 460  ? -23.576 18.190  121.483 1.00 44.74 ? 458  GLU   B O     1 
ATOM   12049 C  CB    . GLU   B  1 460  ? -21.481 20.501  121.464 1.00 44.68 ? 458  GLU   B CB    1 
ATOM   12050 N  N     . GLU   B  1 461  ? -23.467 18.827  119.319 1.00 45.53 ? 459  GLU   B N     1 
ATOM   12051 C  CA    . GLU   B  1 461  ? -24.801 18.378  118.947 1.00 44.89 ? 459  GLU   B CA    1 
ATOM   12052 C  C     . GLU   B  1 461  ? -24.807 16.990  118.316 1.00 47.28 ? 459  GLU   B C     1 
ATOM   12053 O  O     . GLU   B  1 461  ? -25.827 16.587  117.745 1.00 45.22 ? 459  GLU   B O     1 
ATOM   12054 C  CB    . GLU   B  1 461  ? -25.436 19.384  117.985 1.00 42.15 ? 459  GLU   B CB    1 
ATOM   12055 C  CG    . GLU   B  1 461  ? -25.126 20.843  118.315 1.00 36.84 ? 459  GLU   B CG    1 
ATOM   12056 C  CD    . GLU   B  1 461  ? -25.785 21.307  119.607 1.00 53.45 ? 459  GLU   B CD    1 
ATOM   12057 O  OE1   . GLU   B  1 461  ? -26.622 20.553  120.148 1.00 47.65 ? 459  GLU   B OE1   1 
ATOM   12058 O  OE2   . GLU   B  1 461  ? -25.466 22.423  120.079 1.00 56.40 ? 459  GLU   B OE2   1 
ATOM   12059 N  N     . VAL   B  1 462  ? -23.707 16.243  118.424 1.00 40.83 ? 460  VAL   B N     1 
ATOM   12060 C  CA    . VAL   B  1 462  ? -23.561 14.981  117.708 1.00 41.48 ? 460  VAL   B CA    1 
ATOM   12061 C  C     . VAL   B  1 462  ? -23.159 13.859  118.656 1.00 43.47 ? 460  VAL   B C     1 
ATOM   12062 O  O     . VAL   B  1 462  ? -23.734 12.764  118.621 1.00 38.20 ? 460  VAL   B O     1 
ATOM   12063 C  CB    . VAL   B  1 462  ? -22.529 15.115  116.572 1.00 37.97 ? 460  VAL   B CB    1 
ATOM   12064 C  CG1   . VAL   B  1 462  ? -22.269 13.762  115.923 1.00 36.28 ? 460  VAL   B CG1   1 
ATOM   12065 C  CG2   . VAL   B  1 462  ? -22.986 16.145  115.546 1.00 36.52 ? 460  VAL   B CG2   1 
ATOM   12066 N  N     . VAL   B  1 463  ? -22.144 14.107  119.487 1.00 39.31 ? 461  VAL   B N     1 
ATOM   12067 C  CA    . VAL   B  1 463  ? -21.598 13.058  120.340 1.00 36.93 ? 461  VAL   B CA    1 
ATOM   12068 C  C     . VAL   B  1 463  ? -22.548 12.792  121.498 1.00 42.20 ? 461  VAL   B C     1 
ATOM   12069 O  O     . VAL   B  1 463  ? -23.164 13.716  122.044 1.00 42.15 ? 461  VAL   B O     1 
ATOM   12070 C  CB    . VAL   B  1 463  ? -20.199 13.450  120.843 1.00 37.52 ? 461  VAL   B CB    1 
ATOM   12071 C  CG1   . VAL   B  1 463  ? -19.254 13.656  119.657 1.00 33.43 ? 461  VAL   B CG1   1 
ATOM   12072 C  CG2   . VAL   B  1 463  ? -20.279 14.711  121.671 1.00 43.26 ? 461  VAL   B CG2   1 
ATOM   12073 N  N     . GLY   B  1 464  ? -22.673 11.526  121.865 1.00 38.70 ? 462  GLY   B N     1 
ATOM   12074 C  CA    . GLY   B  1 464  ? -23.323 11.157  123.104 1.00 47.20 ? 462  GLY   B CA    1 
ATOM   12075 C  C     . GLY   B  1 464  ? -24.705 10.568  122.878 1.00 54.48 ? 462  GLY   B C     1 
ATOM   12076 O  O     . GLY   B  1 464  ? -25.397 10.883  121.900 1.00 52.05 ? 462  GLY   B O     1 
ATOM   12077 N  N     . ARG   B  1 465  ? -25.123 9.711   123.816 1.00 56.07 ? 463  ARG   B N     1 
ATOM   12078 C  CA    . ARG   B  1 465  ? -26.447 9.098   123.751 1.00 55.94 ? 463  ARG   B CA    1 
ATOM   12079 C  C     . ARG   B  1 465  ? -27.565 10.132  123.717 1.00 57.99 ? 463  ARG   B C     1 
ATOM   12080 O  O     . ARG   B  1 465  ? -28.663 9.824   123.238 1.00 58.49 ? 463  ARG   B O     1 
ATOM   12081 C  CB    . ARG   B  1 465  ? -26.646 8.152   124.938 1.00 56.97 ? 463  ARG   B CB    1 
ATOM   12082 N  N     . GLY   B  1 466  ? -27.312 11.353  124.199 1.00 52.89 ? 464  GLY   B N     1 
ATOM   12083 C  CA    . GLY   B  1 466  ? -28.334 12.382  124.173 1.00 47.37 ? 464  GLY   B CA    1 
ATOM   12084 C  C     . GLY   B  1 466  ? -28.469 13.107  122.855 1.00 59.64 ? 464  GLY   B C     1 
ATOM   12085 O  O     . GLY   B  1 466  ? -29.501 13.743  122.615 1.00 58.88 ? 464  GLY   B O     1 
ATOM   12086 N  N     . LYS   B  1 467  ? -27.450 13.026  121.995 1.00 57.63 ? 465  LYS   B N     1 
ATOM   12087 C  CA    . LYS   B  1 467  ? -27.450 13.733  120.719 1.00 52.42 ? 465  LYS   B CA    1 
ATOM   12088 C  C     . LYS   B  1 467  ? -27.689 12.771  119.561 1.00 54.14 ? 465  LYS   B C     1 
ATOM   12089 O  O     . LYS   B  1 467  ? -28.737 12.120  119.495 1.00 56.51 ? 465  LYS   B O     1 
ATOM   12090 C  CB    . LYS   B  1 467  ? -26.128 14.478  120.525 1.00 51.65 ? 465  LYS   B CB    1 
ATOM   12091 C  CG    . LYS   B  1 467  ? -25.958 15.675  121.439 1.00 52.51 ? 465  LYS   B CG    1 
ATOM   12092 C  CD    . LYS   B  1 467  ? -27.081 16.677  121.240 1.00 52.40 ? 465  LYS   B CD    1 
ATOM   12093 C  CE    . LYS   B  1 467  ? -26.842 17.932  122.063 1.00 53.42 ? 465  LYS   B CE    1 
ATOM   12094 N  NZ    . LYS   B  1 467  ? -27.712 19.063  121.634 1.00 55.00 ? 465  LYS   B NZ    1 
ATOM   12095 N  N     . LEU   B  1 468  ? -26.731 12.679  118.639 1.00 44.09 ? 466  LEU   B N     1 
ATOM   12096 C  CA    . LEU   B  1 468  ? -26.796 11.688  117.576 1.00 37.18 ? 466  LEU   B CA    1 
ATOM   12097 C  C     . LEU   B  1 468  ? -26.060 10.405  117.934 1.00 43.68 ? 466  LEU   B C     1 
ATOM   12098 O  O     . LEU   B  1 468  ? -26.105 9.442   117.161 1.00 42.75 ? 466  LEU   B O     1 
ATOM   12099 C  CB    . LEU   B  1 468  ? -26.242 12.274  116.273 1.00 45.92 ? 466  LEU   B CB    1 
ATOM   12100 C  CG    . LEU   B  1 468  ? -26.941 13.546  115.778 1.00 41.88 ? 466  LEU   B CG    1 
ATOM   12101 C  CD1   . LEU   B  1 468  ? -26.319 14.082  114.485 1.00 40.31 ? 466  LEU   B CD1   1 
ATOM   12102 C  CD2   . LEU   B  1 468  ? -28.445 13.302  115.602 1.00 45.89 ? 466  LEU   B CD2   1 
ATOM   12103 N  N     . ASP   B  1 469  ? -25.400 10.367  119.094 1.00 45.12 ? 467  ASP   B N     1 
ATOM   12104 C  CA    . ASP   B  1 469  ? -24.664 9.188   119.546 1.00 46.51 ? 467  ASP   B CA    1 
ATOM   12105 C  C     . ASP   B  1 469  ? -23.642 8.759   118.503 1.00 37.91 ? 467  ASP   B C     1 
ATOM   12106 O  O     . ASP   B  1 469  ? -23.482 7.574   118.201 1.00 41.37 ? 467  ASP   B O     1 
ATOM   12107 C  CB    . ASP   B  1 469  ? -25.613 8.038   119.907 1.00 46.84 ? 467  ASP   B CB    1 
ATOM   12108 N  N     . ARG   B  1 470  ? -22.944 9.744   117.945 1.00 41.13 ? 468  ARG   B N     1 
ATOM   12109 C  CA    . ARG   B  1 470  ? -21.865 9.514   117.009 1.00 41.26 ? 468  ARG   B CA    1 
ATOM   12110 C  C     . ARG   B  1 470  ? -20.595 10.163  117.544 1.00 33.26 ? 468  ARG   B C     1 
ATOM   12111 O  O     . ARG   B  1 470  ? -20.624 11.339  117.929 1.00 35.25 ? 468  ARG   B O     1 
ATOM   12112 C  CB    . ARG   B  1 470  ? -22.207 10.085  115.618 1.00 37.48 ? 468  ARG   B CB    1 
ATOM   12113 C  CG    . ARG   B  1 470  ? -23.429 9.447   114.964 1.00 36.54 ? 468  ARG   B CG    1 
ATOM   12114 C  CD    . ARG   B  1 470  ? -23.294 7.934   114.888 1.00 34.10 ? 468  ARG   B CD    1 
ATOM   12115 N  NE    . ARG   B  1 470  ? -24.458 7.294   114.281 1.00 41.85 ? 468  ARG   B NE    1 
ATOM   12116 C  CZ    . ARG   B  1 470  ? -25.530 6.891   114.953 1.00 44.39 ? 468  ARG   B CZ    1 
ATOM   12117 N  NH1   . ARG   B  1 470  ? -25.641 7.080   116.259 1.00 41.79 ? 468  ARG   B NH1   1 
ATOM   12118 N  NH2   . ARG   B  1 470  ? -26.516 6.283   114.299 1.00 42.93 ? 468  ARG   B NH2   1 
ATOM   12119 N  N     . PRO   B  1 471  ? -19.476 9.453   117.582 1.00 36.12 ? 469  PRO   B N     1 
ATOM   12120 C  CA    . PRO   B  1 471  ? -18.256 10.032  118.143 1.00 30.95 ? 469  PRO   B CA    1 
ATOM   12121 C  C     . PRO   B  1 471  ? -17.585 10.993  117.174 1.00 35.37 ? 469  PRO   B C     1 
ATOM   12122 O  O     . PRO   B  1 471  ? -17.773 10.947  115.954 1.00 28.05 ? 469  PRO   B O     1 
ATOM   12123 C  CB    . PRO   B  1 471  ? -17.379 8.806   118.407 1.00 34.92 ? 469  PRO   B CB    1 
ATOM   12124 C  CG    . PRO   B  1 471  ? -17.786 7.852   117.361 1.00 33.91 ? 469  PRO   B CG    1 
ATOM   12125 C  CD    . PRO   B  1 471  ? -19.265 8.072   117.129 1.00 35.11 ? 469  PRO   B CD    1 
ATOM   12126 N  N     . CYS   B  1 472  ? -16.809 11.901  117.756 1.00 33.55 ? 470  CYS   B N     1 
ATOM   12127 C  CA    . CYS   B  1 472  ? -16.048 12.887  117.009 1.00 34.62 ? 470  CYS   B CA    1 
ATOM   12128 C  C     . CYS   B  1 472  ? -14.638 12.929  117.570 1.00 30.25 ? 470  CYS   B C     1 
ATOM   12129 O  O     . CYS   B  1 472  ? -14.453 13.054  118.786 1.00 29.47 ? 470  CYS   B O     1 
ATOM   12130 C  CB    . CYS   B  1 472  ? -16.682 14.275  117.089 1.00 30.39 ? 470  CYS   B CB    1 
ATOM   12131 S  SG    . CYS   B  1 472  ? -15.810 15.503  116.106 1.00 32.10 ? 470  CYS   B SG    1 
ATOM   12132 N  N     . ARG   B  1 473  ? -13.657 12.803  116.691 1.00 28.45 ? 471  ARG   B N     1 
ATOM   12133 C  CA    . ARG   B  1 473  ? -12.253 12.958  117.052 1.00 28.00 ? 471  ARG   B CA    1 
ATOM   12134 C  C     . ARG   B  1 473  ? -11.822 14.377  116.710 1.00 28.42 ? 471  ARG   B C     1 
ATOM   12135 O  O     . ARG   B  1 473  ? -11.955 14.814  115.559 1.00 25.03 ? 471  ARG   B O     1 
ATOM   12136 C  CB    . ARG   B  1 473  ? -11.374 11.943  116.322 1.00 26.30 ? 471  ARG   B CB    1 
ATOM   12137 C  CG    . ARG   B  1 473  ? -9.902  11.978  116.757 1.00 24.14 ? 471  ARG   B CG    1 
ATOM   12138 C  CD    . ARG   B  1 473  ? -9.141  10.838  116.094 1.00 24.08 ? 471  ARG   B CD    1 
ATOM   12139 N  NE    . ARG   B  1 473  ? -9.839  9.576   116.297 1.00 23.66 ? 471  ARG   B NE    1 
ATOM   12140 C  CZ    . ARG   B  1 473  ? -9.708  8.805   117.369 1.00 28.08 ? 471  ARG   B CZ    1 
ATOM   12141 N  NH1   . ARG   B  1 473  ? -8.842  9.095   118.332 1.00 25.45 ? 471  ARG   B NH1   1 
ATOM   12142 N  NH2   . ARG   B  1 473  ? -10.461 7.716   117.477 1.00 27.35 ? 471  ARG   B NH2   1 
ATOM   12143 N  N     . ILE   B  1 474  ? -11.306 15.084  117.709 1.00 26.39 ? 472  ILE   B N     1 
ATOM   12144 C  CA    . ILE   B  1 474  ? -10.882 16.471  117.565 1.00 24.13 ? 472  ILE   B CA    1 
ATOM   12145 C  C     . ILE   B  1 474  ? -9.420  16.503  117.138 1.00 25.99 ? 472  ILE   B C     1 
ATOM   12146 O  O     . ILE   B  1 474  ? -8.541  15.978  117.835 1.00 23.95 ? 472  ILE   B O     1 
ATOM   12147 C  CB    . ILE   B  1 474  ? -11.082 17.245  118.875 1.00 25.40 ? 472  ILE   B CB    1 
ATOM   12148 C  CG1   . ILE   B  1 474  ? -12.561 17.264  119.261 1.00 29.15 ? 472  ILE   B CG1   1 
ATOM   12149 C  CG2   . ILE   B  1 474  ? -10.538 18.647  118.737 1.00 27.31 ? 472  ILE   B CG2   1 
ATOM   12150 C  CD1   . ILE   B  1 474  ? -12.829 17.921  120.594 1.00 32.29 ? 472  ILE   B CD1   1 
ATOM   12151 N  N     . TYR   B  1 475  ? -9.166  17.115  115.991 1.00 24.33 ? 473  TYR   B N     1 
ATOM   12152 C  CA    . TYR   B  1 475  ? -7.808  17.387  115.531 1.00 25.21 ? 473  TYR   B CA    1 
ATOM   12153 C  C     . TYR   B  1 475  ? -7.257  18.532  116.364 1.00 27.85 ? 473  TYR   B C     1 
ATOM   12154 O  O     . TYR   B  1 475  ? -7.777  19.652  116.313 1.00 27.54 ? 473  TYR   B O     1 
ATOM   12155 C  CB    . TYR   B  1 475  ? -7.840  17.732  114.052 1.00 21.28 ? 473  TYR   B CB    1 
ATOM   12156 C  CG    . TYR   B  1 475  ? -6.496  17.825  113.356 1.00 23.52 ? 473  TYR   B CG    1 
ATOM   12157 C  CD1   . TYR   B  1 475  ? -5.782  19.017  113.341 1.00 30.34 ? 473  TYR   B CD1   1 
ATOM   12158 C  CD2   . TYR   B  1 475  ? -5.962  16.731  112.693 1.00 24.62 ? 473  TYR   B CD2   1 
ATOM   12159 C  CE1   . TYR   B  1 475  ? -4.562  19.113  112.692 1.00 27.68 ? 473  TYR   B CE1   1 
ATOM   12160 C  CE2   . TYR   B  1 475  ? -4.738  16.813  112.041 1.00 22.79 ? 473  TYR   B CE2   1 
ATOM   12161 C  CZ    . TYR   B  1 475  ? -4.046  18.008  112.045 1.00 30.61 ? 473  TYR   B CZ    1 
ATOM   12162 O  OH    . TYR   B  1 475  ? -2.839  18.110  111.392 1.00 26.89 ? 473  TYR   B OH    1 
ATOM   12163 N  N     . ALA   B  1 476  ? -6.230  18.246  117.158 1.00 23.99 ? 474  ALA   B N     1 
ATOM   12164 C  CA    . ALA   B  1 476  ? -5.808  19.127  118.245 1.00 24.25 ? 474  ALA   B CA    1 
ATOM   12165 C  C     . ALA   B  1 476  ? -4.392  19.614  117.982 1.00 24.81 ? 474  ALA   B C     1 
ATOM   12166 O  O     . ALA   B  1 476  ? -3.423  18.881  118.244 1.00 22.15 ? 474  ALA   B O     1 
ATOM   12167 C  CB    . ALA   B  1 476  ? -5.891  18.394  119.582 1.00 24.52 ? 474  ALA   B CB    1 
ATOM   12168 N  N     . PRO   B  1 477  ? -4.221  20.819  117.449 1.00 24.14 ? 475  PRO   B N     1 
ATOM   12169 C  CA    . PRO   B  1 477  ? -2.875  21.366  117.298 1.00 24.83 ? 475  PRO   B CA    1 
ATOM   12170 C  C     . PRO   B  1 477  ? -2.236  21.635  118.647 1.00 23.92 ? 475  PRO   B C     1 
ATOM   12171 O  O     . PRO   B  1 477  ? -2.889  22.029  119.619 1.00 25.98 ? 475  PRO   B O     1 
ATOM   12172 C  CB    . PRO   B  1 477  ? -3.102  22.669  116.528 1.00 27.58 ? 475  PRO   B CB    1 
ATOM   12173 C  CG    . PRO   B  1 477  ? -4.476  22.528  115.929 1.00 26.73 ? 475  PRO   B CG    1 
ATOM   12174 C  CD    . PRO   B  1 477  ? -5.241  21.746  116.933 1.00 28.32 ? 475  PRO   B CD    1 
ATOM   12175 N  N     . VAL   B  1 478  ? -0.925  21.437  118.679 1.00 22.30 ? 476  VAL   B N     1 
ATOM   12176 C  CA    . VAL   B  1 478  ? -0.128  21.550  119.886 1.00 23.80 ? 476  VAL   B CA    1 
ATOM   12177 C  C     . VAL   B  1 478  ? 1.161   22.261  119.502 1.00 23.84 ? 476  VAL   B C     1 
ATOM   12178 O  O     . VAL   B  1 478  ? 1.889   21.786  118.625 1.00 24.59 ? 476  VAL   B O     1 
ATOM   12179 C  CB    . VAL   B  1 478  ? 0.197   20.180  120.503 1.00 21.92 ? 476  VAL   B CB    1 
ATOM   12180 C  CG1   . VAL   B  1 478  ? 1.015   20.373  121.755 1.00 27.13 ? 476  VAL   B CG1   1 
ATOM   12181 C  CG2   . VAL   B  1 478  ? -1.073  19.381  120.798 1.00 22.03 ? 476  VAL   B CG2   1 
ATOM   12182 N  N     . GLY   B  1 479  ? 1.442   23.378  120.143 1.00 30.24 ? 477  GLY   B N     1 
ATOM   12183 C  CA    . GLY   B  1 479  ? 2.719   24.033  119.963 1.00 32.26 ? 477  GLY   B CA    1 
ATOM   12184 C  C     . GLY   B  1 479  ? 2.614   25.524  120.197 1.00 35.71 ? 477  GLY   B C     1 
ATOM   12185 O  O     . GLY   B  1 479  ? 1.611   26.027  120.691 1.00 30.78 ? 477  GLY   B O     1 
ATOM   12186 N  N     . THR   B  1 480  ? 3.691   26.217  119.807 1.00 40.74 ? 478  THR   B N     1 
ATOM   12187 C  CA    . THR   B  1 480  ? 3.845   27.656  119.994 1.00 48.70 ? 478  THR   B CA    1 
ATOM   12188 C  C     . THR   B  1 480  ? 4.466   28.368  118.799 1.00 53.35 ? 478  THR   B C     1 
ATOM   12189 O  O     . THR   B  1 480  ? 4.427   29.604  118.761 1.00 52.42 ? 478  THR   B O     1 
ATOM   12190 C  CB    . THR   B  1 480  ? 4.725   27.939  121.218 1.00 47.66 ? 478  THR   B CB    1 
ATOM   12191 O  OG1   . THR   B  1 480  ? 5.986   27.282  121.042 1.00 41.77 ? 478  THR   B OG1   1 
ATOM   12192 C  CG2   . THR   B  1 480  ? 4.074   27.440  122.489 1.00 45.76 ? 478  THR   B CG2   1 
ATOM   12193 N  N     . HIS   B  1 481  ? 5.053   27.644  117.842 1.00 52.10 ? 479  HIS   B N     1 
ATOM   12194 C  CA    . HIS   B  1 481  ? 5.807   28.260  116.757 1.00 52.67 ? 479  HIS   B CA    1 
ATOM   12195 C  C     . HIS   B  1 481  ? 4.934   29.225  115.962 1.00 52.29 ? 479  HIS   B C     1 
ATOM   12196 O  O     . HIS   B  1 481  ? 3.906   28.830  115.397 1.00 48.20 ? 479  HIS   B O     1 
ATOM   12197 C  CB    . HIS   B  1 481  ? 6.380   27.178  115.843 1.00 51.52 ? 479  HIS   B CB    1 
ATOM   12198 N  N     . GLU   B  1 482  ? 5.371   30.487  115.909 1.00 48.48 ? 480  GLU   B N     1 
ATOM   12199 C  CA    . GLU   B  1 482  ? 4.573   31.553  115.308 1.00 51.22 ? 480  GLU   B CA    1 
ATOM   12200 C  C     . GLU   B  1 482  ? 4.208   31.244  113.859 1.00 50.46 ? 480  GLU   B C     1 
ATOM   12201 O  O     . GLU   B  1 482  ? 3.044   31.377  113.461 1.00 51.26 ? 480  GLU   B O     1 
ATOM   12202 C  CB    . GLU   B  1 482  ? 5.330   32.881  115.402 1.00 52.77 ? 480  GLU   B CB    1 
ATOM   12203 N  N     . THR   B  1 483  ? 5.189   30.839  113.047 1.00 49.00 ? 481  THR   B N     1 
ATOM   12204 C  CA    . THR   B  1 483  ? 4.912   30.562  111.637 1.00 52.68 ? 481  THR   B CA    1 
ATOM   12205 C  C     . THR   B  1 483  ? 3.870   29.458  111.486 1.00 50.08 ? 481  THR   B C     1 
ATOM   12206 O  O     . THR   B  1 483  ? 2.892   29.605  110.740 1.00 46.10 ? 481  THR   B O     1 
ATOM   12207 C  CB    . THR   B  1 483  ? 6.202   30.181  110.905 1.00 48.18 ? 481  THR   B CB    1 
ATOM   12208 O  OG1   . THR   B  1 483  ? 7.071   31.317  110.834 1.00 51.51 ? 481  THR   B OG1   1 
ATOM   12209 C  CG2   . THR   B  1 483  ? 5.892   29.698  109.494 1.00 45.04 ? 481  THR   B CG2   1 
ATOM   12210 N  N     . LEU   B  1 484  ? 4.072   28.341  112.192 1.00 51.45 ? 482  LEU   B N     1 
ATOM   12211 C  CA    . LEU   B  1 484  ? 3.120   27.235  112.148 1.00 50.97 ? 482  LEU   B CA    1 
ATOM   12212 C  C     . LEU   B  1 484  ? 1.759   27.658  112.688 1.00 50.52 ? 482  LEU   B C     1 
ATOM   12213 O  O     . LEU   B  1 484  ? 0.717   27.204  112.195 1.00 45.12 ? 482  LEU   B O     1 
ATOM   12214 C  CB    . LEU   B  1 484  ? 3.667   26.045  112.941 1.00 45.77 ? 482  LEU   B CB    1 
ATOM   12215 N  N     . LEU   B  1 485  ? 1.750   28.523  113.707 1.00 47.06 ? 483  LEU   B N     1 
ATOM   12216 C  CA    . LEU   B  1 485  ? 0.491   29.070  114.202 1.00 46.44 ? 483  LEU   B CA    1 
ATOM   12217 C  C     . LEU   B  1 485  ? -0.219  29.883  113.125 1.00 50.16 ? 483  LEU   B C     1 
ATOM   12218 O  O     . LEU   B  1 485  ? -1.436  29.750  112.935 1.00 48.85 ? 483  LEU   B O     1 
ATOM   12219 C  CB    . LEU   B  1 485  ? 0.745   29.927  115.438 1.00 47.36 ? 483  LEU   B CB    1 
ATOM   12220 C  CG    . LEU   B  1 485  ? 0.971   29.135  116.723 1.00 50.79 ? 483  LEU   B CG    1 
ATOM   12221 C  CD1   . LEU   B  1 485  ? 1.368   30.060  117.861 1.00 51.28 ? 483  LEU   B CD1   1 
ATOM   12222 C  CD2   . LEU   B  1 485  ? -0.294  28.372  117.060 1.00 48.86 ? 483  LEU   B CD2   1 
ATOM   12223 N  N     . ALA   B  1 486  ? 0.524   30.732  112.407 1.00 47.94 ? 484  ALA   B N     1 
ATOM   12224 C  CA    . ALA   B  1 486  ? -0.093  31.526  111.350 1.00 45.98 ? 484  ALA   B CA    1 
ATOM   12225 C  C     . ALA   B  1 486  ? -0.691  30.631  110.271 1.00 43.27 ? 484  ALA   B C     1 
ATOM   12226 O  O     . ALA   B  1 486  ? -1.780  30.913  109.751 1.00 44.49 ? 484  ALA   B O     1 
ATOM   12227 C  CB    . ALA   B  1 486  ? 0.929   32.493  110.754 1.00 45.18 ? 484  ALA   B CB    1 
ATOM   12228 N  N     . TYR   B  1 487  ? 0.002   29.539  109.929 1.00 42.39 ? 485  TYR   B N     1 
ATOM   12229 C  CA    . TYR   B  1 487  ? -0.547  28.584  108.974 1.00 41.07 ? 485  TYR   B CA    1 
ATOM   12230 C  C     . TYR   B  1 487  ? -1.805  27.924  109.528 1.00 49.59 ? 485  TYR   B C     1 
ATOM   12231 O  O     . TYR   B  1 487  ? -2.751  27.642  108.782 1.00 43.98 ? 485  TYR   B O     1 
ATOM   12232 C  CB    . TYR   B  1 487  ? 0.505   27.532  108.622 1.00 50.69 ? 485  TYR   B CB    1 
ATOM   12233 N  N     . LEU   B  1 488  ? -1.838  27.689  110.841 1.00 43.88 ? 486  LEU   B N     1 
ATOM   12234 C  CA    . LEU   B  1 488  ? -2.995  27.049  111.460 1.00 48.15 ? 486  LEU   B CA    1 
ATOM   12235 C  C     . LEU   B  1 488  ? -4.216  27.960  111.427 1.00 44.57 ? 486  LEU   B C     1 
ATOM   12236 O  O     . LEU   B  1 488  ? -5.324  27.521  111.090 1.00 42.86 ? 486  LEU   B O     1 
ATOM   12237 C  CB    . LEU   B  1 488  ? -2.658  26.652  112.896 1.00 45.80 ? 486  LEU   B CB    1 
ATOM   12238 C  CG    . LEU   B  1 488  ? -3.810  26.303  113.834 1.00 43.85 ? 486  LEU   B CG    1 
ATOM   12239 C  CD1   . LEU   B  1 488  ? -4.607  25.108  113.321 1.00 47.54 ? 486  LEU   B CD1   1 
ATOM   12240 C  CD2   . LEU   B  1 488  ? -3.231  26.025  115.203 1.00 45.57 ? 486  LEU   B CD2   1 
ATOM   12241 N  N     . VAL   B  1 489  ? -4.032  29.236  111.779 1.00 43.59 ? 487  VAL   B N     1 
ATOM   12242 C  CA    . VAL   B  1 489  ? -5.156  30.168  111.812 1.00 44.04 ? 487  VAL   B CA    1 
ATOM   12243 C  C     . VAL   B  1 489  ? -5.767  30.324  110.424 1.00 45.55 ? 487  VAL   B C     1 
ATOM   12244 O  O     . VAL   B  1 489  ? -6.992  30.445  110.278 1.00 47.87 ? 487  VAL   B O     1 
ATOM   12245 C  CB    . VAL   B  1 489  ? -4.707  31.520  112.392 1.00 45.55 ? 487  VAL   B CB    1 
ATOM   12246 C  CG1   . VAL   B  1 489  ? -5.871  32.498  112.406 1.00 45.64 ? 487  VAL   B CG1   1 
ATOM   12247 C  CG2   . VAL   B  1 489  ? -4.144  31.332  113.793 1.00 41.99 ? 487  VAL   B CG2   1 
ATOM   12248 N  N     . ARG   B  1 490  ? -4.929  30.313  109.383 1.00 38.23 ? 488  ARG   B N     1 
ATOM   12249 C  CA    . ARG   B  1 490  ? -5.444  30.390  108.017 1.00 44.76 ? 488  ARG   B CA    1 
ATOM   12250 C  C     . ARG   B  1 490  ? -6.261  29.150  107.668 1.00 50.72 ? 488  ARG   B C     1 
ATOM   12251 O  O     . ARG   B  1 490  ? -7.302  29.249  107.006 1.00 49.48 ? 488  ARG   B O     1 
ATOM   12252 C  CB    . ARG   B  1 490  ? -4.292  30.577  107.030 1.00 40.39 ? 488  ARG   B CB    1 
ATOM   12253 N  N     . ARG   B  1 491  ? -5.806  27.972  108.109 1.00 40.48 ? 489  ARG   B N     1 
ATOM   12254 C  CA    . ARG   B  1 491  ? -6.573  26.755  107.873 1.00 44.86 ? 489  ARG   B CA    1 
ATOM   12255 C  C     . ARG   B  1 491  ? -7.791  26.695  108.784 1.00 45.06 ? 489  ARG   B C     1 
ATOM   12256 O  O     . ARG   B  1 491  ? -8.856  26.212  108.378 1.00 45.12 ? 489  ARG   B O     1 
ATOM   12257 C  CB    . ARG   B  1 491  ? -5.687  25.523  108.070 1.00 43.83 ? 489  ARG   B CB    1 
ATOM   12258 C  CG    . ARG   B  1 491  ? -4.512  25.446  107.096 1.00 47.73 ? 489  ARG   B CG    1 
ATOM   12259 C  CD    . ARG   B  1 491  ? -3.994  24.017  106.909 1.00 44.07 ? 489  ARG   B CD    1 
ATOM   12260 N  NE    . ARG   B  1 491  ? -2.922  23.968  105.916 1.00 44.01 ? 489  ARG   B NE    1 
ATOM   12261 C  CZ    . ARG   B  1 491  ? -1.652  23.695  106.194 1.00 44.93 ? 489  ARG   B CZ    1 
ATOM   12262 N  NH1   . ARG   B  1 491  ? -1.265  23.375  107.420 1.00 43.15 ? 489  ARG   B NH1   1 
ATOM   12263 N  NH2   . ARG   B  1 491  ? -0.748  23.748  105.220 1.00 40.76 ? 489  ARG   B NH2   1 
ATOM   12264 N  N     . LEU   B  1 492  ? -7.651  27.188  110.017 1.00 45.23 ? 490  LEU   B N     1 
ATOM   12265 C  CA    . LEU   B  1 492  ? -8.763  27.183  110.960 1.00 45.31 ? 490  LEU   B CA    1 
ATOM   12266 C  C     . LEU   B  1 492  ? -9.928  28.022  110.445 1.00 50.59 ? 490  LEU   B C     1 
ATOM   12267 O  O     . LEU   B  1 492  ? -11.097 27.645  110.603 1.00 48.48 ? 490  LEU   B O     1 
ATOM   12268 C  CB    . LEU   B  1 492  ? -8.278  27.692  112.319 1.00 50.32 ? 490  LEU   B CB    1 
ATOM   12269 C  CG    . LEU   B  1 492  ? -8.970  27.232  113.601 1.00 49.84 ? 490  LEU   B CG    1 
ATOM   12270 C  CD1   . LEU   B  1 492  ? -9.066  25.714  113.666 1.00 49.65 ? 490  LEU   B CD1   1 
ATOM   12271 C  CD2   . LEU   B  1 492  ? -8.213  27.765  114.806 1.00 50.74 ? 490  LEU   B CD2   1 
ATOM   12272 N  N     . LEU   B  1 493  ? -9.633  29.159  109.816 1.00 50.17 ? 491  LEU   B N     1 
ATOM   12273 C  CA    . LEU   B  1 493  ? -10.663 30.050  109.302 1.00 48.30 ? 491  LEU   B CA    1 
ATOM   12274 C  C     . LEU   B  1 493  ? -10.900 29.869  107.809 1.00 49.38 ? 491  LEU   B C     1 
ATOM   12275 O  O     . LEU   B  1 493  ? -11.579 30.698  107.196 1.00 53.51 ? 491  LEU   B O     1 
ATOM   12276 C  CB    . LEU   B  1 493  ? -10.305 31.505  109.614 1.00 45.62 ? 491  LEU   B CB    1 
ATOM   12277 C  CG    . LEU   B  1 493  ? -10.216 31.814  111.113 1.00 50.59 ? 491  LEU   B CG    1 
ATOM   12278 C  CD1   . LEU   B  1 493  ? -9.851  33.267  111.363 1.00 44.83 ? 491  LEU   B CD1   1 
ATOM   12279 C  CD2   . LEU   B  1 493  ? -11.523 31.454  111.818 1.00 57.68 ? 491  LEU   B CD2   1 
ATOM   12280 N  N     . GLU   B  1 494  ? -10.359 28.800  107.219 1.00 51.00 ? 492  GLU   B N     1 
ATOM   12281 C  CA    . GLU   B  1 494  ? -10.560 28.476  105.803 1.00 47.49 ? 492  GLU   B CA    1 
ATOM   12282 C  C     . GLU   B  1 494  ? -10.226 29.669  104.910 1.00 49.46 ? 492  GLU   B C     1 
ATOM   12283 O  O     . GLU   B  1 494  ? -10.925 29.958  103.935 1.00 49.53 ? 492  GLU   B O     1 
ATOM   12284 C  CB    . GLU   B  1 494  ? -11.988 27.978  105.552 1.00 45.22 ? 492  GLU   B CB    1 
ATOM   12285 C  CG    . GLU   B  1 494  ? -12.496 26.951  106.572 1.00 43.03 ? 492  GLU   B CG    1 
ATOM   12286 C  CD    . GLU   B  1 494  ? -11.762 25.612  106.509 1.00 44.92 ? 492  GLU   B CD    1 
ATOM   12287 O  OE1   . GLU   B  1 494  ? -10.993 25.399  105.548 1.00 42.52 ? 492  GLU   B OE1   1 
ATOM   12288 O  OE2   . GLU   B  1 494  ? -11.944 24.769  107.427 1.00 41.57 ? 492  GLU   B OE2   1 
ATOM   12289 N  N     . ASN   B  1 495  ? -9.146  30.375  105.260 1.00 47.24 ? 493  ASN   B N     1 
ATOM   12290 C  CA    . ASN   B  1 495  ? -8.689  31.559  104.527 1.00 52.11 ? 493  ASN   B CA    1 
ATOM   12291 C  C     . ASN   B  1 495  ? -9.777  32.621  104.406 1.00 53.15 ? 493  ASN   B C     1 
ATOM   12292 O  O     . ASN   B  1 495  ? -9.760  33.431  103.472 1.00 52.58 ? 493  ASN   B O     1 
ATOM   12293 C  CB    . ASN   B  1 495  ? -8.166  31.190  103.137 1.00 52.13 ? 493  ASN   B CB    1 
ATOM   12294 C  CG    . ASN   B  1 495  ? -6.816  30.526  103.188 1.00 51.97 ? 493  ASN   B CG    1 
ATOM   12295 O  OD1   . ASN   B  1 495  ? -6.395  30.041  104.237 1.00 55.46 ? 493  ASN   B OD1   1 
ATOM   12296 N  ND2   . ASN   B  1 495  ? -6.121  30.502  102.057 1.00 53.54 ? 493  ASN   B ND2   1 
ATOM   12297 N  N     . GLY   B  1 496  ? -10.716 32.631  105.349 1.00 55.41 ? 494  GLY   B N     1 
ATOM   12298 C  CA    . GLY   B  1 496  ? -11.846 33.549  105.287 1.00 58.22 ? 494  GLY   B CA    1 
ATOM   12299 C  C     . GLY   B  1 496  ? -12.649 33.443  104.009 1.00 60.39 ? 494  GLY   B C     1 
ATOM   12300 O  O     . GLY   B  1 496  ? -13.055 34.467  103.446 1.00 60.36 ? 494  GLY   B O     1 
ATOM   12301 N  N     . ALA   B  1 497  ? -12.886 32.221  103.538 1.00 57.81 ? 495  ALA   B N     1 
ATOM   12302 C  CA    . ALA   B  1 497  ? -13.540 32.002  102.254 1.00 51.38 ? 495  ALA   B CA    1 
ATOM   12303 C  C     . ALA   B  1 497  ? -15.045 32.186  102.398 1.00 43.06 ? 495  ALA   B C     1 
ATOM   12304 O  O     . ALA   B  1 497  ? -15.676 31.532  103.234 1.00 46.13 ? 495  ALA   B O     1 
ATOM   12305 C  CB    . ALA   B  1 497  ? -13.218 30.607  101.726 1.00 43.63 ? 495  ALA   B CB    1 
ATOM   12306 N  N     . ASN   B  1 498  ? -15.618 33.066  101.571 1.00 44.70 ? 496  ASN   B N     1 
ATOM   12307 C  CA    . ASN   B  1 498  ? -17.060 33.291  101.598 1.00 48.69 ? 496  ASN   B CA    1 
ATOM   12308 C  C     . ASN   B  1 498  ? -17.837 32.016  101.299 1.00 42.58 ? 496  ASN   B C     1 
ATOM   12309 O  O     . ASN   B  1 498  ? -18.980 31.865  101.744 1.00 45.01 ? 496  ASN   B O     1 
ATOM   12310 C  CB    . ASN   B  1 498  ? -17.438 34.388  100.599 1.00 51.01 ? 496  ASN   B CB    1 
ATOM   12311 N  N     . SER   B  1 499  ? -17.241 31.090  100.552 1.00 40.82 ? 497  SER   B N     1 
ATOM   12312 C  CA    . SER   B  1 499  ? -17.913 29.840  100.224 1.00 42.48 ? 497  SER   B CA    1 
ATOM   12313 C  C     . SER   B  1 499  ? -17.829 28.811  101.339 1.00 36.17 ? 497  SER   B C     1 
ATOM   12314 O  O     . SER   B  1 499  ? -18.443 27.745  101.215 1.00 34.77 ? 497  SER   B O     1 
ATOM   12315 C  CB    . SER   B  1 499  ? -17.314 29.238  98.955  1.00 38.35 ? 497  SER   B CB    1 
ATOM   12316 O  OG    . SER   B  1 499  ? -15.982 28.828  99.207  1.00 37.12 ? 497  SER   B OG    1 
ATOM   12317 N  N     . SER   B  1 500  ? -17.072 29.091  102.401 1.00 35.45 ? 498  SER   B N     1 
ATOM   12318 C  CA    . SER   B  1 500  ? -16.902 28.142  103.491 1.00 34.78 ? 498  SER   B CA    1 
ATOM   12319 C  C     . SER   B  1 500  ? -18.145 28.119  104.371 1.00 39.55 ? 498  SER   B C     1 
ATOM   12320 O  O     . SER   B  1 500  ? -18.747 29.160  104.645 1.00 39.00 ? 498  SER   B O     1 
ATOM   12321 C  CB    . SER   B  1 500  ? -15.675 28.504  104.332 1.00 34.23 ? 498  SER   B CB    1 
ATOM   12322 N  N     . PHE   B  1 501  ? -18.531 26.914  104.801 1.00 35.71 ? 499  PHE   B N     1 
ATOM   12323 C  CA    . PHE   B  1 501  ? -19.606 26.776  105.780 1.00 40.81 ? 499  PHE   B CA    1 
ATOM   12324 C  C     . PHE   B  1 501  ? -19.301 27.555  107.056 1.00 41.49 ? 499  PHE   B C     1 
ATOM   12325 O  O     . PHE   B  1 501  ? -20.216 28.104  107.683 1.00 45.94 ? 499  PHE   B O     1 
ATOM   12326 C  CB    . PHE   B  1 501  ? -19.831 25.293  106.087 1.00 38.06 ? 499  PHE   B CB    1 
ATOM   12327 C  CG    . PHE   B  1 501  ? -20.910 25.024  107.108 1.00 38.27 ? 499  PHE   B CG    1 
ATOM   12328 C  CD1   . PHE   B  1 501  ? -20.637 25.082  108.466 1.00 39.62 ? 499  PHE   B CD1   1 
ATOM   12329 C  CD2   . PHE   B  1 501  ? -22.186 24.677  106.706 1.00 32.54 ? 499  PHE   B CD2   1 
ATOM   12330 C  CE1   . PHE   B  1 501  ? -21.624 24.825  109.400 1.00 41.00 ? 499  PHE   B CE1   1 
ATOM   12331 C  CE2   . PHE   B  1 501  ? -23.180 24.418  107.635 1.00 41.52 ? 499  PHE   B CE2   1 
ATOM   12332 C  CZ    . PHE   B  1 501  ? -22.897 24.488  108.983 1.00 36.17 ? 499  PHE   B CZ    1 
ATOM   12333 N  N     . VAL   B  1 502  ? -18.026 27.618  107.451 1.00 43.47 ? 500  VAL   B N     1 
ATOM   12334 C  CA    . VAL   B  1 502  ? -17.650 28.315  108.679 1.00 49.75 ? 500  VAL   B CA    1 
ATOM   12335 C  C     . VAL   B  1 502  ? -17.836 29.823  108.531 1.00 48.22 ? 500  VAL   B C     1 
ATOM   12336 O  O     . VAL   B  1 502  ? -18.040 30.529  109.527 1.00 53.40 ? 500  VAL   B O     1 
ATOM   12337 C  CB    . VAL   B  1 502  ? -16.203 27.958  109.076 1.00 43.05 ? 500  VAL   B CB    1 
ATOM   12338 N  N     . HIS   B  1 503  ? -17.770 30.346  107.306 1.00 43.69 ? 501  HIS   B N     1 
ATOM   12339 C  CA    . HIS   B  1 503  ? -18.097 31.748  107.073 1.00 41.57 ? 501  HIS   B CA    1 
ATOM   12340 C  C     . HIS   B  1 503  ? -19.584 31.969  106.819 1.00 50.39 ? 501  HIS   B C     1 
ATOM   12341 O  O     . HIS   B  1 503  ? -20.118 33.023  107.191 1.00 48.01 ? 501  HIS   B O     1 
ATOM   12342 C  CB    . HIS   B  1 503  ? -17.293 32.292  105.891 1.00 46.59 ? 501  HIS   B CB    1 
ATOM   12343 C  CG    . HIS   B  1 503  ? -17.700 33.668  105.459 1.00 48.66 ? 501  HIS   B CG    1 
ATOM   12344 N  ND1   . HIS   B  1 503  ? -18.808 33.906  104.670 1.00 48.71 ? 501  HIS   B ND1   1 
ATOM   12345 C  CD2   . HIS   B  1 503  ? -17.139 34.879  105.693 1.00 50.89 ? 501  HIS   B CD2   1 
ATOM   12346 C  CE1   . HIS   B  1 503  ? -18.915 35.203  104.445 1.00 51.48 ? 501  HIS   B CE1   1 
ATOM   12347 N  NE2   . HIS   B  1 503  ? -17.912 35.816  105.051 1.00 53.11 ? 501  HIS   B NE2   1 
ATOM   12348 N  N     . ARG   B  1 504  ? -20.263 30.999  106.198 1.00 44.76 ? 502  ARG   B N     1 
ATOM   12349 C  CA    . ARG   B  1 504  ? -21.661 31.170  105.820 1.00 42.70 ? 502  ARG   B CA    1 
ATOM   12350 C  C     . ARG   B  1 504  ? -22.613 30.990  106.993 1.00 44.62 ? 502  ARG   B C     1 
ATOM   12351 O  O     . ARG   B  1 504  ? -23.674 31.624  107.019 1.00 46.93 ? 502  ARG   B O     1 
ATOM   12352 C  CB    . ARG   B  1 504  ? -22.023 30.192  104.702 1.00 37.53 ? 502  ARG   B CB    1 
ATOM   12353 C  CG    . ARG   B  1 504  ? -21.441 30.576  103.358 1.00 39.63 ? 502  ARG   B CG    1 
ATOM   12354 C  CD    . ARG   B  1 504  ? -21.370 29.395  102.403 1.00 37.71 ? 502  ARG   B CD    1 
ATOM   12355 N  NE    . ARG   B  1 504  ? -22.657 28.747  102.184 1.00 36.06 ? 502  ARG   B NE    1 
ATOM   12356 C  CZ    . ARG   B  1 504  ? -23.563 29.157  101.307 1.00 37.58 ? 502  ARG   B CZ    1 
ATOM   12357 N  NH1   . ARG   B  1 504  ? -23.385 30.259  100.593 1.00 41.53 ? 502  ARG   B NH1   1 
ATOM   12358 N  NH2   . ARG   B  1 504  ? -24.674 28.443  101.141 1.00 33.89 ? 502  ARG   B NH2   1 
ATOM   12359 N  N     . ILE   B  1 505  ? -22.274 30.129  107.957 1.00 46.47 ? 503  ILE   B N     1 
ATOM   12360 C  CA    . ILE   B  1 505  ? -23.135 29.951  109.122 1.00 43.81 ? 503  ILE   B CA    1 
ATOM   12361 C  C     . ILE   B  1 505  ? -23.227 31.229  109.944 1.00 44.54 ? 503  ILE   B C     1 
ATOM   12362 O  O     . ILE   B  1 505  ? -24.188 31.409  110.701 1.00 46.96 ? 503  ILE   B O     1 
ATOM   12363 C  CB    . ILE   B  1 505  ? -22.642 28.780  109.994 1.00 46.23 ? 503  ILE   B CB    1 
ATOM   12364 N  N     . ASN   B  1 506  ? -22.257 32.130  109.801 1.00 43.52 ? 504  ASN   B N     1 
ATOM   12365 C  CA    . ASN   B  1 506  ? -22.248 33.414  110.490 1.00 53.75 ? 504  ASN   B CA    1 
ATOM   12366 C  C     . ASN   B  1 506  ? -22.576 34.576  109.558 1.00 52.18 ? 504  ASN   B C     1 
ATOM   12367 O  O     . ASN   B  1 506  ? -22.335 35.734  109.914 1.00 53.29 ? 504  ASN   B O     1 
ATOM   12368 C  CB    . ASN   B  1 506  ? -20.892 33.642  111.163 1.00 52.68 ? 504  ASN   B CB    1 
ATOM   12369 N  N     . ASP   B  1 507  ? -23.109 34.298  108.371 1.00 47.60 ? 505  ASP   B N     1 
ATOM   12370 C  CA    . ASP   B  1 507  ? -23.546 35.357  107.480 1.00 49.92 ? 505  ASP   B CA    1 
ATOM   12371 C  C     . ASP   B  1 507  ? -25.059 35.473  107.578 1.00 56.72 ? 505  ASP   B C     1 
ATOM   12372 O  O     . ASP   B  1 507  ? -25.769 34.528  107.197 1.00 52.90 ? 505  ASP   B O     1 
ATOM   12373 C  CB    . ASP   B  1 507  ? -23.121 35.063  106.043 1.00 55.40 ? 505  ASP   B CB    1 
ATOM   12374 C  CG    . ASP   B  1 507  ? -23.188 36.287  105.153 1.00 55.69 ? 505  ASP   B CG    1 
ATOM   12375 O  OD1   . ASP   B  1 507  ? -24.128 37.092  105.310 1.00 59.86 ? 505  ASP   B OD1   1 
ATOM   12376 O  OD2   . ASP   B  1 507  ? -22.294 36.448  104.295 1.00 62.59 ? 505  ASP   B OD2   1 
ATOM   12377 N  N     . PRO   B  1 508  ? -25.598 36.583  108.093 1.00 59.74 ? 506  PRO   B N     1 
ATOM   12378 C  CA    . PRO   B  1 508  ? -27.061 36.690  108.226 1.00 57.26 ? 506  PRO   B CA    1 
ATOM   12379 C  C     . PRO   B  1 508  ? -27.791 36.697  106.897 1.00 59.21 ? 506  PRO   B C     1 
ATOM   12380 O  O     . PRO   B  1 508  ? -28.963 36.301  106.844 1.00 60.31 ? 506  PRO   B O     1 
ATOM   12381 C  CB    . PRO   B  1 508  ? -27.251 38.017  108.976 1.00 60.90 ? 506  PRO   B CB    1 
ATOM   12382 C  CG    . PRO   B  1 508  ? -25.928 38.311  109.598 1.00 61.83 ? 506  PRO   B CG    1 
ATOM   12383 C  CD    . PRO   B  1 508  ? -24.903 37.745  108.668 1.00 56.10 ? 506  PRO   B CD    1 
ATOM   12384 N  N     . LYS   B  1 509  ? -27.141 37.142  105.819 1.00 57.25 ? 507  LYS   B N     1 
ATOM   12385 C  CA    . LYS   B  1 509  ? -27.784 37.130  104.511 1.00 57.88 ? 507  LYS   B CA    1 
ATOM   12386 C  C     . LYS   B  1 509  ? -28.038 35.715  104.006 1.00 61.16 ? 507  LYS   B C     1 
ATOM   12387 O  O     . LYS   B  1 509  ? -28.899 35.525  103.140 1.00 61.00 ? 507  LYS   B O     1 
ATOM   12388 C  CB    . LYS   B  1 509  ? -26.933 37.904  103.502 1.00 58.32 ? 507  LYS   B CB    1 
ATOM   12389 N  N     . VAL   B  1 510  ? -27.328 34.723  104.534 1.00 59.19 ? 508  VAL   B N     1 
ATOM   12390 C  CA    . VAL   B  1 510  ? -27.439 33.340  104.086 1.00 55.95 ? 508  VAL   B CA    1 
ATOM   12391 C  C     . VAL   B  1 510  ? -28.431 32.617  104.987 1.00 52.12 ? 508  VAL   B C     1 
ATOM   12392 O  O     . VAL   B  1 510  ? -28.232 32.535  106.203 1.00 52.98 ? 508  VAL   B O     1 
ATOM   12393 C  CB    . VAL   B  1 510  ? -26.072 32.640  104.095 1.00 53.56 ? 508  VAL   B CB    1 
ATOM   12394 C  CG1   . VAL   B  1 510  ? -26.185 31.239  103.512 1.00 52.54 ? 508  VAL   B CG1   1 
ATOM   12395 C  CG2   . VAL   B  1 510  ? -25.056 33.464  103.335 1.00 54.96 ? 508  VAL   B CG2   1 
ATOM   12396 N  N     . SER   B  1 511  ? -29.490 32.078  104.389 1.00 52.73 ? 509  SER   B N     1 
ATOM   12397 C  CA    . SER   B  1 511  ? -30.552 31.417  105.128 1.00 49.72 ? 509  SER   B CA    1 
ATOM   12398 C  C     . SER   B  1 511  ? -30.187 29.966  105.422 1.00 51.53 ? 509  SER   B C     1 
ATOM   12399 O  O     . SER   B  1 511  ? -29.278 29.389  104.817 1.00 52.38 ? 509  SER   B O     1 
ATOM   12400 C  CB    . SER   B  1 511  ? -31.856 31.454  104.336 1.00 51.13 ? 509  SER   B CB    1 
ATOM   12401 O  OG    . SER   B  1 511  ? -31.718 30.711  103.137 1.00 51.87 ? 509  SER   B OG    1 
ATOM   12402 N  N     . ILE   B  1 512  ? -30.928 29.369  106.357 1.00 46.49 ? 510  ILE   B N     1 
ATOM   12403 C  CA    . ILE   B  1 512  ? -30.712 27.958  106.651 1.00 51.86 ? 510  ILE   B CA    1 
ATOM   12404 C  C     . ILE   B  1 512  ? -31.104 27.100  105.454 1.00 49.26 ? 510  ILE   B C     1 
ATOM   12405 O  O     . ILE   B  1 512  ? -30.498 26.047  105.215 1.00 44.76 ? 510  ILE   B O     1 
ATOM   12406 C  CB    . ILE   B  1 512  ? -31.470 27.540  107.926 1.00 41.30 ? 510  ILE   B CB    1 
ATOM   12407 N  N     . ASP   B  1 513  ? -32.104 27.529  104.676 1.00 46.12 ? 511  ASP   B N     1 
ATOM   12408 C  CA    . ASP   B  1 513  ? -32.477 26.780  103.479 1.00 43.20 ? 511  ASP   B CA    1 
ATOM   12409 C  C     . ASP   B  1 513  ? -31.326 26.722  102.483 1.00 44.89 ? 511  ASP   B C     1 
ATOM   12410 O  O     . ASP   B  1 513  ? -31.092 25.683  101.856 1.00 46.32 ? 511  ASP   B O     1 
ATOM   12411 C  CB    . ASP   B  1 513  ? -33.716 27.396  102.826 1.00 48.12 ? 511  ASP   B CB    1 
ATOM   12412 C  CG    . ASP   B  1 513  ? -35.012 26.818  103.365 1.00 54.49 ? 511  ASP   B CG    1 
ATOM   12413 O  OD1   . ASP   B  1 513  ? -35.073 25.592  103.604 1.00 58.25 ? 511  ASP   B OD1   1 
ATOM   12414 O  OD2   . ASP   B  1 513  ? -35.973 27.590  103.548 1.00 63.73 ? 511  ASP   B OD2   1 
ATOM   12415 N  N     . GLU   B  1 514  ? -30.609 27.833  102.308 1.00 39.66 ? 512  GLU   B N     1 
ATOM   12416 C  CA    . GLU   B  1 514  ? -29.407 27.818  101.480 1.00 44.67 ? 512  GLU   B CA    1 
ATOM   12417 C  C     . GLU   B  1 514  ? -28.376 26.833  102.021 1.00 46.15 ? 512  GLU   B C     1 
ATOM   12418 O  O     . GLU   B  1 514  ? -27.774 26.065  101.261 1.00 39.59 ? 512  GLU   B O     1 
ATOM   12419 C  CB    . GLU   B  1 514  ? -28.808 29.223  101.404 1.00 44.26 ? 512  GLU   B CB    1 
ATOM   12420 C  CG    . GLU   B  1 514  ? -29.473 30.151  100.400 1.00 52.23 ? 512  GLU   B CG    1 
ATOM   12421 C  CD    . GLU   B  1 514  ? -29.214 31.619  100.702 1.00 56.56 ? 512  GLU   B CD    1 
ATOM   12422 O  OE1   . GLU   B  1 514  ? -29.820 32.142  101.662 1.00 59.48 ? 512  GLU   B OE1   1 
ATOM   12423 O  OE2   . GLU   B  1 514  ? -28.400 32.247  99.988  1.00 62.46 ? 512  GLU   B OE2   1 
ATOM   12424 N  N     . LEU   B  1 515  ? -28.162 26.836  103.337 1.00 41.00 ? 513  LEU   B N     1 
ATOM   12425 C  CA    . LEU   B  1 515  ? -27.124 25.993  103.916 1.00 40.46 ? 513  LEU   B CA    1 
ATOM   12426 C  C     . LEU   B  1 515  ? -27.480 24.516  103.844 1.00 40.86 ? 513  LEU   B C     1 
ATOM   12427 O  O     . LEU   B  1 515  ? -26.579 23.670  103.836 1.00 39.32 ? 513  LEU   B O     1 
ATOM   12428 C  CB    . LEU   B  1 515  ? -26.872 26.395  105.367 1.00 40.83 ? 513  LEU   B CB    1 
ATOM   12429 C  CG    . LEU   B  1 515  ? -26.310 27.784  105.658 1.00 42.28 ? 513  LEU   B CG    1 
ATOM   12430 C  CD1   . LEU   B  1 515  ? -26.445 28.073  107.143 1.00 44.58 ? 513  LEU   B CD1   1 
ATOM   12431 C  CD2   . LEU   B  1 515  ? -24.845 27.883  105.222 1.00 40.99 ? 513  LEU   B CD2   1 
ATOM   12432 N  N     . ILE   B  1 516  ? -28.773 24.178  103.799 1.00 37.48 ? 514  ILE   B N     1 
ATOM   12433 C  CA    . ILE   B  1 516  ? -29.192 22.779  103.762 1.00 35.97 ? 514  ILE   B CA    1 
ATOM   12434 C  C     . ILE   B  1 516  ? -29.492 22.296  102.352 1.00 33.15 ? 514  ILE   B C     1 
ATOM   12435 O  O     . ILE   B  1 516  ? -29.935 21.153  102.185 1.00 40.32 ? 514  ILE   B O     1 
ATOM   12436 C  CB    . ILE   B  1 516  ? -30.409 22.515  104.671 1.00 44.32 ? 514  ILE   B CB    1 
ATOM   12437 C  CG1   . ILE   B  1 516  ? -31.642 23.263  104.151 1.00 42.21 ? 514  ILE   B CG1   1 
ATOM   12438 C  CG2   . ILE   B  1 516  ? -30.073 22.867  106.113 1.00 38.85 ? 514  ILE   B CG2   1 
ATOM   12439 C  CD1   . ILE   B  1 516  ? -32.930 22.895  104.854 1.00 44.47 ? 514  ILE   B CD1   1 
ATOM   12440 N  N     . ALA   B  1 517  ? -29.258 23.125  101.337 1.00 36.65 ? 515  ALA   B N     1 
ATOM   12441 C  CA    . ALA   B  1 517  ? -29.387 22.684  99.954  1.00 40.75 ? 515  ALA   B CA    1 
ATOM   12442 C  C     . ALA   B  1 517  ? -28.544 21.440  99.710  1.00 40.21 ? 515  ALA   B C     1 
ATOM   12443 O  O     . ALA   B  1 517  ? -27.380 21.372  100.121 1.00 39.56 ? 515  ALA   B O     1 
ATOM   12444 C  CB    . ALA   B  1 517  ? -28.965 23.804  99.004  1.00 37.96 ? 515  ALA   B CB    1 
ATOM   12445 N  N     . ASP   B  1 518  ? -29.149 20.443  99.059  1.00 36.94 ? 516  ASP   B N     1 
ATOM   12446 C  CA    . ASP   B  1 518  ? -28.467 19.185  98.790  1.00 34.46 ? 516  ASP   B CA    1 
ATOM   12447 C  C     . ASP   B  1 518  ? -27.524 19.373  97.608  1.00 33.83 ? 516  ASP   B C     1 
ATOM   12448 O  O     . ASP   B  1 518  ? -27.988 19.550  96.475  1.00 35.00 ? 516  ASP   B O     1 
ATOM   12449 C  CB    . ASP   B  1 518  ? -29.483 18.079  98.510  1.00 33.19 ? 516  ASP   B CB    1 
ATOM   12450 C  CG    . ASP   B  1 518  ? -28.844 16.705  98.387  1.00 37.26 ? 516  ASP   B CG    1 
ATOM   12451 O  OD1   . ASP   B  1 518  ? -27.598 16.607  98.315  1.00 36.22 ? 516  ASP   B OD1   1 
ATOM   12452 O  OD2   . ASP   B  1 518  ? -29.596 15.708  98.357  1.00 42.73 ? 516  ASP   B OD2   1 
ATOM   12453 N  N     . PRO   B  1 519  ? -26.205 19.332  97.819  1.00 31.88 ? 517  PRO   B N     1 
ATOM   12454 C  CA    . PRO   B  1 519  ? -25.290 19.533  96.684  1.00 33.63 ? 517  PRO   B CA    1 
ATOM   12455 C  C     . PRO   B  1 519  ? -25.498 18.522  95.572  1.00 32.45 ? 517  PRO   B C     1 
ATOM   12456 O  O     . PRO   B  1 519  ? -25.337 18.862  94.391  1.00 31.09 ? 517  PRO   B O     1 
ATOM   12457 C  CB    . PRO   B  1 519  ? -23.900 19.399  97.328  1.00 33.60 ? 517  PRO   B CB    1 
ATOM   12458 C  CG    . PRO   B  1 519  ? -24.117 18.607  98.553  1.00 32.75 ? 517  PRO   B CG    1 
ATOM   12459 C  CD    . PRO   B  1 519  ? -25.477 19.009  99.060  1.00 33.72 ? 517  PRO   B CD    1 
ATOM   12460 N  N     . VAL   B  1 520  ? -25.882 17.294  95.921  1.00 32.62 ? 518  VAL   B N     1 
ATOM   12461 C  CA    . VAL   B  1 520  ? -26.072 16.254  94.917  1.00 33.34 ? 518  VAL   B CA    1 
ATOM   12462 C  C     . VAL   B  1 520  ? -27.200 16.638  93.966  1.00 34.18 ? 518  VAL   B C     1 
ATOM   12463 O  O     . VAL   B  1 520  ? -27.061 16.548  92.742  1.00 34.83 ? 518  VAL   B O     1 
ATOM   12464 C  CB    . VAL   B  1 520  ? -26.348 14.902  95.596  1.00 34.41 ? 518  VAL   B CB    1 
ATOM   12465 C  CG1   . VAL   B  1 520  ? -26.410 13.793  94.546  1.00 37.88 ? 518  VAL   B CG1   1 
ATOM   12466 C  CG2   . VAL   B  1 520  ? -25.290 14.618  96.655  1.00 30.17 ? 518  VAL   B CG2   1 
ATOM   12467 N  N     . GLU   B  1 521  ? -28.327 17.084  94.519  1.00 34.76 ? 519  GLU   B N     1 
ATOM   12468 C  CA    . GLU   B  1 521  ? -29.467 17.435  93.681  1.00 35.74 ? 519  GLU   B CA    1 
ATOM   12469 C  C     . GLU   B  1 521  ? -29.242 18.744  92.941  1.00 36.01 ? 519  GLU   B C     1 
ATOM   12470 O  O     . GLU   B  1 521  ? -29.739 18.911  91.820  1.00 37.68 ? 519  GLU   B O     1 
ATOM   12471 C  CB    . GLU   B  1 521  ? -30.742 17.499  94.527  1.00 36.18 ? 519  GLU   B CB    1 
ATOM   12472 C  CG    . GLU   B  1 521  ? -31.094 16.174  95.164  1.00 35.20 ? 519  GLU   B CG    1 
ATOM   12473 C  CD    . GLU   B  1 521  ? -31.186 15.037  94.147  1.00 42.26 ? 519  GLU   B CD    1 
ATOM   12474 O  OE1   . GLU   B  1 521  ? -31.568 15.294  92.986  1.00 42.67 ? 519  GLU   B OE1   1 
ATOM   12475 O  OE2   . GLU   B  1 521  ? -30.873 13.881  94.509  1.00 46.73 ? 519  GLU   B OE2   1 
ATOM   12476 N  N     . VAL   B  1 522  ? -28.501 19.679  93.538  1.00 33.98 ? 520  VAL   B N     1 
ATOM   12477 C  CA    . VAL   B  1 522  ? -28.185 20.909  92.822  1.00 33.99 ? 520  VAL   B CA    1 
ATOM   12478 C  C     . VAL   B  1 522  ? -27.288 20.612  91.628  1.00 37.33 ? 520  VAL   B C     1 
ATOM   12479 O  O     . VAL   B  1 522  ? -27.511 21.131  90.528  1.00 35.90 ? 520  VAL   B O     1 
ATOM   12480 C  CB    . VAL   B  1 522  ? -27.550 21.946  93.765  1.00 35.05 ? 520  VAL   B CB    1 
ATOM   12481 C  CG1   . VAL   B  1 522  ? -27.179 23.196  92.995  1.00 37.89 ? 520  VAL   B CG1   1 
ATOM   12482 C  CG2   . VAL   B  1 522  ? -28.501 22.277  94.916  1.00 42.64 ? 520  VAL   B CG2   1 
ATOM   12483 N  N     . VAL   B  1 523  ? -26.273 19.761  91.808  1.00 30.56 ? 521  VAL   B N     1 
ATOM   12484 C  CA    . VAL   B  1 523  ? -25.419 19.424  90.670  1.00 32.80 ? 521  VAL   B CA    1 
ATOM   12485 C  C     . VAL   B  1 523  ? -26.211 18.661  89.618  1.00 35.07 ? 521  VAL   B C     1 
ATOM   12486 O  O     . VAL   B  1 523  ? -26.082 18.922  88.416  1.00 34.30 ? 521  VAL   B O     1 
ATOM   12487 C  CB    . VAL   B  1 523  ? -24.178 18.636  91.126  1.00 33.03 ? 521  VAL   B CB    1 
ATOM   12488 C  CG1   . VAL   B  1 523  ? -23.419 18.096  89.914  1.00 30.02 ? 521  VAL   B CG1   1 
ATOM   12489 C  CG2   . VAL   B  1 523  ? -23.285 19.537  91.931  1.00 28.52 ? 521  VAL   B CG2   1 
ATOM   12490 N  N     . ARG   B  1 524  ? -27.046 17.715  90.050  1.00 32.40 ? 522  ARG   B N     1 
ATOM   12491 C  CA    . ARG   B  1 524  ? -27.799 16.901  89.103  1.00 33.64 ? 522  ARG   B CA    1 
ATOM   12492 C  C     . ARG   B  1 524  ? -28.661 17.763  88.194  1.00 36.74 ? 522  ARG   B C     1 
ATOM   12493 O  O     . ARG   B  1 524  ? -28.921 17.388  87.045  1.00 39.78 ? 522  ARG   B O     1 
ATOM   12494 C  CB    . ARG   B  1 524  ? -28.673 15.892  89.855  1.00 35.71 ? 522  ARG   B CB    1 
ATOM   12495 C  CG    . ARG   B  1 524  ? -29.353 14.872  88.958  1.00 39.74 ? 522  ARG   B CG    1 
ATOM   12496 C  CD    . ARG   B  1 524  ? -30.511 14.179  89.664  1.00 42.03 ? 522  ARG   B CD    1 
ATOM   12497 N  NE    . ARG   B  1 524  ? -30.130 13.666  90.973  1.00 40.59 ? 522  ARG   B NE    1 
ATOM   12498 C  CZ    . ARG   B  1 524  ? -29.455 12.541  91.169  1.00 42.77 ? 522  ARG   B CZ    1 
ATOM   12499 N  NH1   . ARG   B  1 524  ? -29.038 11.798  90.155  1.00 41.98 ? 522  ARG   B NH1   1 
ATOM   12500 N  NH2   . ARG   B  1 524  ? -29.187 12.153  92.415  1.00 40.89 ? 522  ARG   B NH2   1 
ATOM   12501 N  N     . ALA   B  1 525  ? -29.101 18.920  88.685  1.00 38.07 ? 523  ALA   B N     1 
ATOM   12502 C  CA    . ALA   B  1 525  ? -30.028 19.780  87.968  1.00 38.19 ? 523  ALA   B CA    1 
ATOM   12503 C  C     . ALA   B  1 525  ? -29.337 20.758  87.033  1.00 36.41 ? 523  ALA   B C     1 
ATOM   12504 O  O     . ALA   B  1 525  ? -30.018 21.448  86.269  1.00 39.41 ? 523  ALA   B O     1 
ATOM   12505 C  CB    . ALA   B  1 525  ? -30.896 20.561  88.959  1.00 35.94 ? 523  ALA   B CB    1 
ATOM   12506 N  N     . MET   B  1 526  ? -28.016 20.848  87.073  1.00 37.20 ? 524  MET   B N     1 
ATOM   12507 C  CA    . MET   B  1 526  ? -27.339 21.801  86.221  1.00 37.63 ? 524  MET   B CA    1 
ATOM   12508 C  C     . MET   B  1 526  ? -27.404 21.343  84.764  1.00 38.25 ? 524  MET   B C     1 
ATOM   12509 O  O     . MET   B  1 526  ? -27.518 20.145  84.485  1.00 39.07 ? 524  MET   B O     1 
ATOM   12510 C  CB    . MET   B  1 526  ? -25.896 21.984  86.674  1.00 33.66 ? 524  MET   B CB    1 
ATOM   12511 C  CG    . MET   B  1 526  ? -25.803 22.877  87.889  1.00 37.89 ? 524  MET   B CG    1 
ATOM   12512 S  SD    . MET   B  1 526  ? -24.259 22.671  88.791  1.00 46.41 ? 524  MET   B SD    1 
ATOM   12513 C  CE    . MET   B  1 526  ? -23.317 24.090  88.227  1.00 47.54 ? 524  MET   B CE    1 
ATOM   12514 N  N     . PRO   B  1 527  ? -27.375 22.285  83.815  1.00 39.03 ? 525  PRO   B N     1 
ATOM   12515 C  CA    . PRO   B  1 527  ? -27.487 21.891  82.403  1.00 40.12 ? 525  PRO   B CA    1 
ATOM   12516 C  C     . PRO   B  1 527  ? -26.284 21.116  81.909  1.00 37.57 ? 525  PRO   B C     1 
ATOM   12517 O  O     . PRO   B  1 527  ? -26.422 20.314  80.978  1.00 33.58 ? 525  PRO   B O     1 
ATOM   12518 C  CB    . PRO   B  1 527  ? -27.630 23.234  81.677  1.00 39.17 ? 525  PRO   B CB    1 
ATOM   12519 C  CG    . PRO   B  1 527  ? -26.907 24.198  82.561  1.00 39.54 ? 525  PRO   B CG    1 
ATOM   12520 C  CD    . PRO   B  1 527  ? -27.192 23.740  83.969  1.00 42.12 ? 525  PRO   B CD    1 
ATOM   12521 N  N     . VAL   B  1 528  ? -25.105 21.338  82.487  1.00 31.64 ? 526  VAL   B N     1 
ATOM   12522 C  CA    . VAL   B  1 528  ? -23.917 20.557  82.173  1.00 31.86 ? 526  VAL   B CA    1 
ATOM   12523 C  C     . VAL   B  1 528  ? -23.364 20.078  83.507  1.00 29.87 ? 526  VAL   B C     1 
ATOM   12524 O  O     . VAL   B  1 528  ? -22.740 20.852  84.243  1.00 31.83 ? 526  VAL   B O     1 
ATOM   12525 C  CB    . VAL   B  1 528  ? -22.867 21.353  81.392  1.00 32.71 ? 526  VAL   B CB    1 
ATOM   12526 C  CG1   . VAL   B  1 528  ? -21.592 20.548  81.281  1.00 33.68 ? 526  VAL   B CG1   1 
ATOM   12527 C  CG2   . VAL   B  1 528  ? -23.382 21.704  80.009  1.00 34.48 ? 526  VAL   B CG2   1 
ATOM   12528 N  N     . VAL   B  1 529  ? -23.579 18.806  83.819  1.00 30.57 ? 527  VAL   B N     1 
ATOM   12529 C  CA    . VAL   B  1 529  ? -23.143 18.284  85.105  1.00 27.26 ? 527  VAL   B CA    1 
ATOM   12530 C  C     . VAL   B  1 529  ? -21.623 18.291  85.158  1.00 29.59 ? 527  VAL   B C     1 
ATOM   12531 O  O     . VAL   B  1 529  ? -20.947 17.759  84.265  1.00 28.54 ? 527  VAL   B O     1 
ATOM   12532 C  CB    . VAL   B  1 529  ? -23.710 16.878  85.338  1.00 29.52 ? 527  VAL   B CB    1 
ATOM   12533 C  CG1   . VAL   B  1 529  ? -23.030 16.235  86.548  1.00 28.67 ? 527  VAL   B CG1   1 
ATOM   12534 C  CG2   . VAL   B  1 529  ? -25.219 16.950  85.532  1.00 34.14 ? 527  VAL   B CG2   1 
ATOM   12535 N  N     . GLY   B  1 530  ? -21.079 18.914  86.199  1.00 24.46 ? 528  GLY   B N     1 
ATOM   12536 C  CA    . GLY   B  1 530  ? -19.650 18.952  86.376  1.00 23.46 ? 528  GLY   B CA    1 
ATOM   12537 C  C     . GLY   B  1 530  ? -18.937 20.038  85.612  1.00 25.36 ? 528  GLY   B C     1 
ATOM   12538 O  O     . GLY   B  1 530  ? -17.710 19.977  85.502  1.00 24.81 ? 528  GLY   B O     1 
ATOM   12539 N  N     . ALA   B  1 531  ? -19.655 21.020  85.062  1.00 21.98 ? 529  ALA   B N     1 
ATOM   12540 C  CA    . ALA   B  1 531  ? -18.980 22.096  84.350  1.00 24.01 ? 529  ALA   B CA    1 
ATOM   12541 C  C     . ALA   B  1 531  ? -18.046 22.852  85.283  1.00 24.51 ? 529  ALA   B C     1 
ATOM   12542 O  O     . ALA   B  1 531  ? -18.383 23.133  86.438  1.00 25.03 ? 529  ALA   B O     1 
ATOM   12543 C  CB    . ALA   B  1 531  ? -19.992 23.059  83.730  1.00 28.00 ? 529  ALA   B CB    1 
ATOM   12544 N  N     . LYS   B  1 532  ? -16.853 23.150  84.767  1.00 23.10 ? 530  LYS   B N     1 
ATOM   12545 C  CA    . LYS   B  1 532  ? -15.848 23.927  85.473  1.00 25.95 ? 530  LYS   B CA    1 
ATOM   12546 C  C     . LYS   B  1 532  ? -16.414 25.281  85.874  1.00 29.33 ? 530  LYS   B C     1 
ATOM   12547 O  O     . LYS   B  1 532  ? -17.282 25.841  85.198  1.00 25.68 ? 530  LYS   B O     1 
ATOM   12548 C  CB    . LYS   B  1 532  ? -14.620 24.114  84.576  1.00 25.50 ? 530  LYS   B CB    1 
ATOM   12549 C  CG    . LYS   B  1 532  ? -13.592 25.151  85.046  1.00 31.54 ? 530  LYS   B CG    1 
ATOM   12550 C  CD    . LYS   B  1 532  ? -12.502 25.382  83.999  1.00 25.53 ? 530  LYS   B CD    1 
ATOM   12551 C  CE    . LYS   B  1 532  ? -13.000 26.216  82.823  1.00 29.06 ? 530  LYS   B CE    1 
ATOM   12552 N  NZ    . LYS   B  1 532  ? -13.321 27.633  83.195  1.00 26.12 ? 530  LYS   B NZ    1 
ATOM   12553 N  N     . HIS   B  1 533  ? -15.921 25.794  86.997  1.00 23.34 ? 531  HIS   B N     1 
ATOM   12554 C  CA    . HIS   B  1 533  ? -16.287 27.131  87.440  1.00 25.26 ? 531  HIS   B CA    1 
ATOM   12555 C  C     . HIS   B  1 533  ? -16.060 28.142  86.323  1.00 25.89 ? 531  HIS   B C     1 
ATOM   12556 O  O     . HIS   B  1 533  ? -15.009 28.145  85.674  1.00 26.04 ? 531  HIS   B O     1 
ATOM   12557 C  CB    . HIS   B  1 533  ? -15.464 27.513  88.668  1.00 26.42 ? 531  HIS   B CB    1 
ATOM   12558 C  CG    . HIS   B  1 533  ? -16.024 28.669  89.427  1.00 28.89 ? 531  HIS   B CG    1 
ATOM   12559 N  ND1   . HIS   B  1 533  ? -16.022 29.953  88.930  1.00 28.10 ? 531  HIS   B ND1   1 
ATOM   12560 C  CD2   . HIS   B  1 533  ? -16.621 28.735  90.641  1.00 31.26 ? 531  HIS   B CD2   1 
ATOM   12561 C  CE1   . HIS   B  1 533  ? -16.583 30.764  89.811  1.00 36.86 ? 531  HIS   B CE1   1 
ATOM   12562 N  NE2   . HIS   B  1 533  ? -16.958 30.049  90.856  1.00 32.96 ? 531  HIS   B NE2   1 
ATOM   12563 N  N     . ASP   B  1 534  ? -17.054 29.003  86.107  1.00 26.99 ? 532  ASP   B N     1 
ATOM   12564 C  CA    . ASP   B  1 534  ? -17.011 29.927  84.981  1.00 28.57 ? 532  ASP   B CA    1 
ATOM   12565 C  C     . ASP   B  1 534  ? -15.934 30.989  85.145  1.00 24.34 ? 532  ASP   B C     1 
ATOM   12566 O  O     . ASP   B  1 534  ? -15.556 31.627  84.157  1.00 30.72 ? 532  ASP   B O     1 
ATOM   12567 C  CB    . ASP   B  1 534  ? -18.378 30.598  84.801  1.00 29.89 ? 532  ASP   B CB    1 
ATOM   12568 N  N     . ARG   B  1 535  ? -15.438 31.203  86.360  1.00 22.62 ? 533  ARG   B N     1 
ATOM   12569 C  CA    . ARG   B  1 535  ? -14.496 32.277  86.635  1.00 24.25 ? 533  ARG   B CA    1 
ATOM   12570 C  C     . ARG   B  1 535  ? -13.079 31.776  86.880  1.00 26.14 ? 533  ARG   B C     1 
ATOM   12571 O  O     . ARG   B  1 535  ? -12.219 32.564  87.277  1.00 24.67 ? 533  ARG   B O     1 
ATOM   12572 C  CB    . ARG   B  1 535  ? -14.966 33.099  87.838  1.00 32.00 ? 533  ARG   B CB    1 
ATOM   12573 N  N     . ILE   B  1 536  ? -12.816 30.489  86.685  1.00 21.56 ? 534  ILE   B N     1 
ATOM   12574 C  CA    . ILE   B  1 536  ? -11.482 29.931  86.866  1.00 22.25 ? 534  ILE   B CA    1 
ATOM   12575 C  C     . ILE   B  1 536  ? -11.016 29.429  85.511  1.00 19.90 ? 534  ILE   B C     1 
ATOM   12576 O  O     . ILE   B  1 536  ? -11.681 28.583  84.901  1.00 21.18 ? 534  ILE   B O     1 
ATOM   12577 C  CB    . ILE   B  1 536  ? -11.465 28.800  87.905  1.00 23.47 ? 534  ILE   B CB    1 
ATOM   12578 C  CG1   . ILE   B  1 536  ? -11.975 29.313  89.246  1.00 24.24 ? 534  ILE   B CG1   1 
ATOM   12579 C  CG2   . ILE   B  1 536  ? -10.056 28.223  88.039  1.00 20.20 ? 534  ILE   B CG2   1 
ATOM   12580 C  CD1   . ILE   B  1 536  ? -12.020 28.258  90.314  1.00 28.80 ? 534  ILE   B CD1   1 
ATOM   12581 N  N     . ALA   B  1 537  ? -9.885  29.952  85.041  1.00 20.65 ? 535  ALA   B N     1 
ATOM   12582 C  CA    . ALA   B  1 537  ? -9.383  29.599  83.723  1.00 22.58 ? 535  ALA   B CA    1 
ATOM   12583 C  C     . ALA   B  1 537  ? -8.637  28.274  83.788  1.00 20.63 ? 535  ALA   B C     1 
ATOM   12584 O  O     . ALA   B  1 537  ? -7.794  28.074  84.664  1.00 18.03 ? 535  ALA   B O     1 
ATOM   12585 C  CB    . ALA   B  1 537  ? -8.457  30.691  83.191  1.00 21.27 ? 535  ALA   B CB    1 
ATOM   12586 N  N     . LEU   B  1 538  ? -8.972  27.357  82.885  1.00 18.83 ? 536  LEU   B N     1 
ATOM   12587 C  CA    . LEU   B  1 538  ? -8.081  26.233  82.657  1.00 21.85 ? 536  LEU   B CA    1 
ATOM   12588 C  C     . LEU   B  1 538  ? -6.697  26.774  82.320  1.00 20.20 ? 536  LEU   B C     1 
ATOM   12589 O  O     . LEU   B  1 538  ? -6.583  27.838  81.707  1.00 20.13 ? 536  LEU   B O     1 
ATOM   12590 C  CB    . LEU   B  1 538  ? -8.574  25.362  81.510  1.00 22.64 ? 536  LEU   B CB    1 
ATOM   12591 C  CG    . LEU   B  1 538  ? -9.699  24.373  81.779  1.00 27.21 ? 536  LEU   B CG    1 
ATOM   12592 C  CD1   . LEU   B  1 538  ? -10.157 23.807  80.447  1.00 28.03 ? 536  LEU   B CD1   1 
ATOM   12593 C  CD2   . LEU   B  1 538  ? -9.238  23.264  82.712  1.00 23.68 ? 536  LEU   B CD2   1 
ATOM   12594 N  N     . PRO   B  1 539  ? -5.632  26.077  82.720  1.00 20.17 ? 537  PRO   B N     1 
ATOM   12595 C  CA    . PRO   B  1 539  ? -4.288  26.586  82.409  1.00 20.11 ? 537  PRO   B CA    1 
ATOM   12596 C  C     . PRO   B  1 539  ? -4.134  26.952  80.949  1.00 17.10 ? 537  PRO   B C     1 
ATOM   12597 O  O     . PRO   B  1 539  ? -3.571  28.008  80.643  1.00 19.39 ? 537  PRO   B O     1 
ATOM   12598 C  CB    . PRO   B  1 539  ? -3.369  25.430  82.829  1.00 17.35 ? 537  PRO   B CB    1 
ATOM   12599 C  CG    . PRO   B  1 539  ? -4.136  24.745  83.945  1.00 17.79 ? 537  PRO   B CG    1 
ATOM   12600 C  CD    . PRO   B  1 539  ? -5.592  24.830  83.498  1.00 19.72 ? 537  PRO   B CD    1 
ATOM   12601 N  N     . ALA   B  1 540  ? -4.680  26.139  80.042  1.00 18.95 ? 538  ALA   B N     1 
ATOM   12602 C  CA    . ALA   B  1 540  ? -4.590  26.441  78.616  1.00 19.98 ? 538  ALA   B CA    1 
ATOM   12603 C  C     . ALA   B  1 540  ? -5.275  27.755  78.248  1.00 21.21 ? 538  ALA   B C     1 
ATOM   12604 O  O     . ALA   B  1 540  ? -4.926  28.361  77.223  1.00 20.23 ? 538  ALA   B O     1 
ATOM   12605 C  CB    . ALA   B  1 540  ? -5.202  25.298  77.806  1.00 20.75 ? 538  ALA   B CB    1 
ATOM   12606 N  N     . GLU   B  1 541  ? -6.236  28.209  79.058  1.00 20.96 ? 539  GLU   B N     1 
ATOM   12607 C  CA    . GLU   B  1 541  ? -7.087  29.342  78.718  1.00 21.28 ? 539  GLU   B CA    1 
ATOM   12608 C  C     . GLU   B  1 541  ? -6.738  30.600  79.519  1.00 22.03 ? 539  GLU   B C     1 
ATOM   12609 O  O     . GLU   B  1 541  ? -7.541  31.541  79.576  1.00 19.62 ? 539  GLU   B O     1 
ATOM   12610 C  CB    . GLU   B  1 541  ? -8.560  28.934  78.891  1.00 23.14 ? 539  GLU   B CB    1 
ATOM   12611 C  CG    . GLU   B  1 541  ? -8.998  27.926  77.793  1.00 24.23 ? 539  GLU   B CG    1 
ATOM   12612 C  CD    . GLU   B  1 541  ? -10.336 27.230  78.036  1.00 36.91 ? 539  GLU   B CD    1 
ATOM   12613 O  OE1   . GLU   B  1 541  ? -11.103 27.652  78.923  1.00 38.39 ? 539  GLU   B OE1   1 
ATOM   12614 O  OE2   . GLU   B  1 541  ? -10.624 26.241  77.322  1.00 36.23 ? 539  GLU   B OE2   1 
ATOM   12615 N  N     . LEU   B  1 542  ? -5.534  30.650  80.102  1.00 18.41 ? 540  LEU   B N     1 
ATOM   12616 C  CA    . LEU   B  1 542  ? -5.157  31.759  80.982  1.00 18.28 ? 540  LEU   B CA    1 
ATOM   12617 C  C     . LEU   B  1 542  ? -5.229  33.102  80.281  1.00 23.14 ? 540  LEU   B C     1 
ATOM   12618 O  O     . LEU   B  1 542  ? -5.444  34.129  80.930  1.00 21.33 ? 540  LEU   B O     1 
ATOM   12619 C  CB    . LEU   B  1 542  ? -3.734  31.570  81.510  1.00 22.27 ? 540  LEU   B CB    1 
ATOM   12620 C  CG    . LEU   B  1 542  ? -3.415  30.923  82.854  1.00 25.33 ? 540  LEU   B CG    1 
ATOM   12621 C  CD1   . LEU   B  1 542  ? -1.958  31.236  83.228  1.00 20.75 ? 540  LEU   B CD1   1 
ATOM   12622 C  CD2   . LEU   B  1 542  ? -4.384  31.313  83.967  1.00 22.14 ? 540  LEU   B CD2   1 
ATOM   12623 N  N     . PHE   B  1 543  ? -5.042  33.126  78.966  1.00 18.04 ? 541  PHE   B N     1 
ATOM   12624 C  CA    . PHE   B  1 543  ? -5.011  34.383  78.229  1.00 20.03 ? 541  PHE   B CA    1 
ATOM   12625 C  C     . PHE   B  1 543  ? -6.259  34.568  77.388  1.00 22.32 ? 541  PHE   B C     1 
ATOM   12626 O  O     . PHE   B  1 543  ? -6.307  35.473  76.545  1.00 22.02 ? 541  PHE   B O     1 
ATOM   12627 C  CB    . PHE   B  1 543  ? -3.742  34.446  77.380  1.00 21.00 ? 541  PHE   B CB    1 
ATOM   12628 C  CG    . PHE   B  1 543  ? -2.524  34.091  78.152  1.00 20.54 ? 541  PHE   B CG    1 
ATOM   12629 C  CD1   . PHE   B  1 543  ? -2.195  34.807  79.300  1.00 21.39 ? 541  PHE   B CD1   1 
ATOM   12630 C  CD2   . PHE   B  1 543  ? -1.735  33.022  77.782  1.00 18.57 ? 541  PHE   B CD2   1 
ATOM   12631 C  CE1   . PHE   B  1 543  ? -1.078  34.483  80.047  1.00 21.71 ? 541  PHE   B CE1   1 
ATOM   12632 C  CE2   . PHE   B  1 543  ? -0.614  32.686  78.527  1.00 20.48 ? 541  PHE   B CE2   1 
ATOM   12633 C  CZ    . PHE   B  1 543  ? -0.283  33.422  79.666  1.00 22.57 ? 541  PHE   B CZ    1 
ATOM   12634 N  N     . GLY   B  1 544  ? -7.272  33.738  77.614  1.00 20.68 ? 542  GLY   B N     1 
ATOM   12635 C  CA    . GLY   B  1 544  ? -8.540  33.914  76.929  1.00 23.32 ? 542  GLY   B CA    1 
ATOM   12636 C  C     . GLY   B  1 544  ? -8.391  33.786  75.428  1.00 26.47 ? 542  GLY   B C     1 
ATOM   12637 O  O     . GLY   B  1 544  ? -7.626  32.961  74.914  1.00 23.74 ? 542  GLY   B O     1 
ATOM   12638 N  N     . ASP   B  1 545  ? -9.128  34.628  74.706  1.00 25.54 ? 543  ASP   B N     1 
ATOM   12639 C  CA    . ASP   B  1 545  ? -9.134  34.557  73.253  1.00 30.48 ? 543  ASP   B CA    1 
ATOM   12640 C  C     . ASP   B  1 545  ? -7.853  35.085  72.625  1.00 26.92 ? 543  ASP   B C     1 
ATOM   12641 O  O     . ASP   B  1 545  ? -7.684  34.952  71.408  1.00 26.74 ? 543  ASP   B O     1 
ATOM   12642 C  CB    . ASP   B  1 545  ? -10.326 35.338  72.707  1.00 32.38 ? 543  ASP   B CB    1 
ATOM   12643 C  CG    . ASP   B  1 545  ? -11.623 34.910  73.333  1.00 40.77 ? 543  ASP   B CG    1 
ATOM   12644 O  OD1   . ASP   B  1 545  ? -11.803 33.690  73.546  1.00 43.51 ? 543  ASP   B OD1   1 
ATOM   12645 O  OD2   . ASP   B  1 545  ? -12.454 35.794  73.625  1.00 56.88 ? 543  ASP   B OD2   1 
ATOM   12646 N  N     . ALA   B  1 546  ? -6.958  35.689  73.409  1.00 23.19 ? 544  ALA   B N     1 
ATOM   12647 C  CA    . ALA   B  1 546  ? -5.756  36.267  72.821  1.00 24.05 ? 544  ALA   B CA    1 
ATOM   12648 C  C     . ALA   B  1 546  ? -4.872  35.189  72.216  1.00 27.10 ? 544  ALA   B C     1 
ATOM   12649 O  O     . ALA   B  1 546  ? -4.365  35.335  71.094  1.00 22.89 ? 544  ALA   B O     1 
ATOM   12650 C  CB    . ALA   B  1 546  ? -4.991  37.066  73.879  1.00 25.39 ? 544  ALA   B CB    1 
ATOM   12651 N  N     . ARG   B  1 547  ? -4.702  34.084  72.931  1.00 21.60 ? 545  ARG   B N     1 
ATOM   12652 C  CA    . ARG   B  1 547  ? -3.789  33.040  72.513  1.00 21.03 ? 545  ARG   B CA    1 
ATOM   12653 C  C     . ARG   B  1 547  ? -3.906  31.893  73.500  1.00 20.68 ? 545  ARG   B C     1 
ATOM   12654 O  O     . ARG   B  1 547  ? -4.368  32.060  74.631  1.00 20.70 ? 545  ARG   B O     1 
ATOM   12655 C  CB    . ARG   B  1 547  ? -2.341  33.529  72.462  1.00 23.58 ? 545  ARG   B CB    1 
ATOM   12656 C  CG    . ARG   B  1 547  ? -1.858  34.018  73.797  1.00 21.46 ? 545  ARG   B CG    1 
ATOM   12657 C  CD    . ARG   B  1 547  ? -0.432  34.486  73.705  1.00 21.71 ? 545  ARG   B CD    1 
ATOM   12658 N  NE    . ARG   B  1 547  ? -0.150  35.309  74.864  1.00 20.93 ? 545  ARG   B NE    1 
ATOM   12659 C  CZ    . ARG   B  1 547  ? 0.615   34.944  75.880  1.00 21.91 ? 545  ARG   B CZ    1 
ATOM   12660 N  NH1   . ARG   B  1 547  ? 1.296   33.808  75.863  1.00 19.70 ? 545  ARG   B NH1   1 
ATOM   12661 N  NH2   . ARG   B  1 547  ? 0.710   35.747  76.935  1.00 23.38 ? 545  ARG   B NH2   1 
ATOM   12662 N  N     . THR   B  1 548  ? -3.444  30.740  73.060  1.00 17.26 ? 546  THR   B N     1 
ATOM   12663 C  CA    . THR   B  1 548  ? -3.451  29.533  73.859  1.00 18.41 ? 546  THR   B CA    1 
ATOM   12664 C  C     . THR   B  1 548  ? -2.166  29.457  74.663  1.00 19.10 ? 546  THR   B C     1 
ATOM   12665 O  O     . THR   B  1 548  ? -1.070  29.584  74.109  1.00 17.67 ? 546  THR   B O     1 
ATOM   12666 C  CB    . THR   B  1 548  ? -3.588  28.316  72.954  1.00 17.50 ? 546  THR   B CB    1 
ATOM   12667 O  OG1   . THR   B  1 548  ? -4.789  28.453  72.183  1.00 21.94 ? 546  THR   B OG1   1 
ATOM   12668 C  CG2   . THR   B  1 548  ? -3.652  27.047  73.770  1.00 20.93 ? 546  THR   B CG2   1 
ATOM   12669 N  N     . ASN   B  1 549  ? -2.310  29.275  75.970  1.00 15.52 ? 547  ASN   B N     1 
ATOM   12670 C  CA    . ASN   B  1 549  ? -1.154  29.129  76.835  1.00 16.52 ? 547  ASN   B CA    1 
ATOM   12671 C  C     . ASN   B  1 549  ? -0.404  27.852  76.470  1.00 16.45 ? 547  ASN   B C     1 
ATOM   12672 O  O     . ASN   B  1 549  ? -1.012  26.845  76.092  1.00 16.96 ? 547  ASN   B O     1 
ATOM   12673 C  CB    . ASN   B  1 549  ? -1.626  29.104  78.291  1.00 20.69 ? 547  ASN   B CB    1 
ATOM   12674 C  CG    . ASN   B  1 549  ? -0.492  29.189  79.289  1.00 18.95 ? 547  ASN   B CG    1 
ATOM   12675 O  OD1   . ASN   B  1 549  ? 0.645   29.559  78.960  1.00 17.74 ? 547  ASN   B OD1   1 
ATOM   12676 N  ND2   . ASN   B  1 549  ? -0.806  28.859  80.538  1.00 16.04 ? 547  ASN   B ND2   1 
ATOM   12677 N  N     . SER   B  1 550  ? 0.926   27.912  76.528  1.00 14.98 ? 548  SER   B N     1 
ATOM   12678 C  CA    . SER   B  1 550  ? 1.714   26.700  76.351  1.00 17.38 ? 548  SER   B CA    1 
ATOM   12679 C  C     . SER   B  1 550  ? 1.361   25.697  77.442  1.00 19.21 ? 548  SER   B C     1 
ATOM   12680 O  O     . SER   B  1 550  ? 0.923   26.064  78.534  1.00 19.64 ? 548  SER   B O     1 
ATOM   12681 C  CB    . SER   B  1 550  ? 3.210   27.006  76.401  1.00 17.47 ? 548  SER   B CB    1 
ATOM   12682 O  OG    . SER   B  1 550  ? 3.545   27.610  77.639  1.00 18.40 ? 548  SER   B OG    1 
ATOM   12683 N  N     . ALA   B  1 551  ? 1.544   24.420  77.139  1.00 16.70 ? 549  ALA   B N     1 
ATOM   12684 C  CA    . ALA   B  1 551  ? 1.282   23.355  78.098  1.00 17.08 ? 549  ALA   B CA    1 
ATOM   12685 C  C     . ALA   B  1 551  ? 2.592   22.743  78.556  1.00 19.43 ? 549  ALA   B C     1 
ATOM   12686 O  O     . ALA   B  1 551  ? 3.514   22.557  77.757  1.00 16.95 ? 549  ALA   B O     1 
ATOM   12687 C  CB    . ALA   B  1 551  ? 0.399   22.262  77.503  1.00 18.71 ? 549  ALA   B CB    1 
ATOM   12688 N  N     . GLY   B  1 552  ? 2.661   22.422  79.841  1.00 19.34 ? 550  GLY   B N     1 
ATOM   12689 C  CA    . GLY   B  1 552  ? 3.791   21.716  80.401  1.00 19.20 ? 550  GLY   B CA    1 
ATOM   12690 C  C     . GLY   B  1 552  ? 3.562   20.222  80.475  1.00 17.58 ? 550  GLY   B C     1 
ATOM   12691 O  O     . GLY   B  1 552  ? 2.682   19.659  79.818  1.00 20.71 ? 550  GLY   B O     1 
ATOM   12692 N  N     . LEU   B  1 553  ? 4.387   19.572  81.286  1.00 17.91 ? 551  LEU   B N     1 
ATOM   12693 C  CA    . LEU   B  1 553  ? 4.281   18.147  81.533  1.00 22.65 ? 551  LEU   B CA    1 
ATOM   12694 C  C     . LEU   B  1 553  ? 4.309   17.961  83.038  1.00 17.02 ? 551  LEU   B C     1 
ATOM   12695 O  O     . LEU   B  1 553  ? 5.054   18.649  83.733  1.00 19.69 ? 551  LEU   B O     1 
ATOM   12696 C  CB    . LEU   B  1 553  ? 5.428   17.369  80.852  1.00 20.99 ? 551  LEU   B CB    1 
ATOM   12697 C  CG    . LEU   B  1 553  ? 5.428   17.393  79.319  1.00 21.87 ? 551  LEU   B CG    1 
ATOM   12698 C  CD1   . LEU   B  1 553  ? 6.688   16.758  78.748  1.00 23.03 ? 551  LEU   B CD1   1 
ATOM   12699 C  CD2   . LEU   B  1 553  ? 4.196   16.694  78.789  1.00 22.84 ? 551  LEU   B CD2   1 
ATOM   12700 N  N     . ASP   B  1 554  ? 3.477   17.060  83.538  1.00 18.17 ? 552  ASP   B N     1 
ATOM   12701 C  CA    . ASP   B  1 554  ? 3.360   16.837  84.976  1.00 20.09 ? 552  ASP   B CA    1 
ATOM   12702 C  C     . ASP   B  1 554  ? 4.388   15.783  85.359  1.00 18.69 ? 552  ASP   B C     1 
ATOM   12703 O  O     . ASP   B  1 554  ? 4.186   14.592  85.122  1.00 19.40 ? 552  ASP   B O     1 
ATOM   12704 C  CB    . ASP   B  1 554  ? 1.943   16.398  85.334  1.00 20.56 ? 552  ASP   B CB    1 
ATOM   12705 C  CG    . ASP   B  1 554  ? 1.743   16.213  86.836  1.00 20.22 ? 552  ASP   B CG    1 
ATOM   12706 O  OD1   . ASP   B  1 554  ? 2.722   16.373  87.608  1.00 22.28 ? 552  ASP   B OD1   1 
ATOM   12707 O  OD2   . ASP   B  1 554  ? 0.583   15.922  87.226  1.00 22.30 ? 552  ASP   B OD2   1 
ATOM   12708 N  N     . LEU   B  1 555  ? 5.490   16.224  85.953  1.00 20.87 ? 553  LEU   B N     1 
ATOM   12709 C  CA    . LEU   B  1 555  ? 6.551   15.317  86.355  1.00 18.94 ? 553  LEU   B CA    1 
ATOM   12710 C  C     . LEU   B  1 555  ? 6.230   14.578  87.649  1.00 20.56 ? 553  LEU   B C     1 
ATOM   12711 O  O     . LEU   B  1 555  ? 7.110   13.894  88.176  1.00 21.33 ? 553  LEU   B O     1 
ATOM   12712 C  CB    . LEU   B  1 555  ? 7.870   16.081  86.484  1.00 21.48 ? 553  LEU   B CB    1 
ATOM   12713 C  CG    . LEU   B  1 555  ? 8.367   16.762  85.197  1.00 22.13 ? 553  LEU   B CG    1 
ATOM   12714 C  CD1   . LEU   B  1 555  ? 9.760   17.346  85.426  1.00 19.93 ? 553  LEU   B CD1   1 
ATOM   12715 C  CD2   . LEU   B  1 555  ? 8.366   15.801  84.010  1.00 26.52 ? 553  LEU   B CD2   1 
ATOM   12716 N  N     . SER   B  1 556  ? 5.013   14.718  88.187  1.00 19.33 ? 554  SER   B N     1 
ATOM   12717 C  CA    . SER   B  1 556  ? 4.551   13.857  89.274  1.00 18.04 ? 554  SER   B CA    1 
ATOM   12718 C  C     . SER   B  1 556  ? 3.597   12.783  88.782  1.00 20.21 ? 554  SER   B C     1 
ATOM   12719 O  O     . SER   B  1 556  ? 3.155   11.939  89.569  1.00 21.64 ? 554  SER   B O     1 
ATOM   12720 C  CB    . SER   B  1 556  ? 3.873   14.685  90.380  1.00 21.55 ? 554  SER   B CB    1 
ATOM   12721 O  OG    . SER   B  1 556  ? 2.611   15.177  89.942  1.00 20.76 ? 554  SER   B OG    1 
ATOM   12722 N  N     . ASN   B  1 557  ? 3.284   12.789  87.496  1.00 18.99 ? 555  ASN   B N     1 
ATOM   12723 C  CA    . ASN   B  1 557  ? 2.390   11.819  86.896  1.00 20.26 ? 555  ASN   B CA    1 
ATOM   12724 C  C     . ASN   B  1 557  ? 3.204   10.640  86.367  1.00 21.00 ? 555  ASN   B C     1 
ATOM   12725 O  O     . ASN   B  1 557  ? 4.040   10.813  85.474  1.00 19.96 ? 555  ASN   B O     1 
ATOM   12726 C  CB    . ASN   B  1 557  ? 1.602   12.496  85.778  1.00 19.82 ? 555  ASN   B CB    1 
ATOM   12727 C  CG    . ASN   B  1 557  ? 0.591   11.577  85.144  1.00 22.66 ? 555  ASN   B CG    1 
ATOM   12728 O  OD1   . ASN   B  1 557  ? 0.919   10.472  84.730  1.00 22.90 ? 555  ASN   B OD1   1 
ATOM   12729 N  ND2   . ASN   B  1 557  ? -0.655  12.036  85.062  1.00 22.87 ? 555  ASN   B ND2   1 
ATOM   12730 N  N     . GLU   B  1 558  ? 2.944   9.443   86.896  1.00 22.69 ? 556  GLU   B N     1 
ATOM   12731 C  CA    . GLU   B  1 558  ? 3.738   8.278   86.494  1.00 24.87 ? 556  GLU   B CA    1 
ATOM   12732 C  C     . GLU   B  1 558  ? 3.548   7.917   85.028  1.00 25.68 ? 556  GLU   B C     1 
ATOM   12733 O  O     . GLU   B  1 558  ? 4.479   7.387   84.412  1.00 25.74 ? 556  GLU   B O     1 
ATOM   12734 C  CB    . GLU   B  1 558  ? 3.403   7.049   87.345  1.00 26.29 ? 556  GLU   B CB    1 
ATOM   12735 C  CG    . GLU   B  1 558  ? 3.821   7.137   88.781  1.00 24.37 ? 556  GLU   B CG    1 
ATOM   12736 C  CD    . GLU   B  1 558  ? 5.330   7.223   89.016  1.00 26.78 ? 556  GLU   B CD    1 
ATOM   12737 O  OE1   . GLU   B  1 558  ? 6.168   6.992   88.103  1.00 25.47 ? 556  GLU   B OE1   1 
ATOM   12738 O  OE2   . GLU   B  1 558  ? 5.677   7.536   90.163  1.00 25.75 ? 556  GLU   B OE2   1 
ATOM   12739 N  N     . GLU   B  1 559  ? 2.352   8.126   84.467  1.00 22.47 ? 557  GLU   B N     1 
ATOM   12740 C  CA    . GLU   B  1 559  ? 2.181   7.896   83.031  1.00 24.99 ? 557  GLU   B CA    1 
ATOM   12741 C  C     . GLU   B  1 559  ? 3.092   8.825   82.247  1.00 24.07 ? 557  GLU   B C     1 
ATOM   12742 O  O     . GLU   B  1 559  ? 3.786   8.405   81.310  1.00 23.74 ? 557  GLU   B O     1 
ATOM   12743 C  CB    . GLU   B  1 559  ? 0.732   8.129   82.594  1.00 26.55 ? 557  GLU   B CB    1 
ATOM   12744 C  CG    . GLU   B  1 559  ? -0.314  7.180   83.103  1.00 36.39 ? 557  GLU   B CG    1 
ATOM   12745 C  CD    . GLU   B  1 559  ? -1.703  7.553   82.585  1.00 40.86 ? 557  GLU   B CD    1 
ATOM   12746 O  OE1   . GLU   B  1 559  ? -1.798  8.077   81.452  1.00 46.37 ? 557  GLU   B OE1   1 
ATOM   12747 O  OE2   . GLU   B  1 559  ? -2.697  7.335   83.311  1.00 38.94 ? 557  GLU   B OE2   1 
ATOM   12748 N  N     . THR   B  1 560  ? 3.087   10.105  82.621  1.00 20.87 ? 558  THR   B N     1 
ATOM   12749 C  CA    . THR   B  1 560  ? 3.949   11.079  81.972  1.00 20.91 ? 558  THR   B CA    1 
ATOM   12750 C  C     . THR   B  1 560  ? 5.415   10.697  82.130  1.00 22.17 ? 558  THR   B C     1 
ATOM   12751 O  O     . THR   B  1 560  ? 6.177   10.717  81.161  1.00 21.94 ? 558  THR   B O     1 
ATOM   12752 C  CB    . THR   B  1 560  ? 3.678   12.471  82.547  1.00 20.07 ? 558  THR   B CB    1 
ATOM   12753 O  OG1   . THR   B  1 560  ? 2.287   12.785  82.389  1.00 22.23 ? 558  THR   B OG1   1 
ATOM   12754 C  CG2   . THR   B  1 560  ? 4.494   13.504  81.812  1.00 20.78 ? 558  THR   B CG2   1 
ATOM   12755 N  N     . LEU   B  1 561  ? 5.824   10.323  83.349  1.00 19.18 ? 559  LEU   B N     1 
ATOM   12756 C  CA    . LEU   B  1 561  ? 7.223   9.959   83.564  1.00 23.14 ? 559  LEU   B CA    1 
ATOM   12757 C  C     . LEU   B  1 561  ? 7.619   8.748   82.729  1.00 23.06 ? 559  LEU   B C     1 
ATOM   12758 O  O     . LEU   B  1 561  ? 8.722   8.705   82.174  1.00 21.50 ? 559  LEU   B O     1 
ATOM   12759 C  CB    . LEU   B  1 561  ? 7.486   9.695   85.047  1.00 21.63 ? 559  LEU   B CB    1 
ATOM   12760 C  CG    . LEU   B  1 561  ? 7.413   10.939  85.938  1.00 20.35 ? 559  LEU   B CG    1 
ATOM   12761 C  CD1   . LEU   B  1 561  ? 7.622   10.573  87.394  1.00 17.86 ? 559  LEU   B CD1   1 
ATOM   12762 C  CD2   . LEU   B  1 561  ? 8.432   11.989  85.497  1.00 17.09 ? 559  LEU   B CD2   1 
ATOM   12763 N  N     . ALA   B  1 562  ? 6.737   7.753   82.626  1.00 21.86 ? 560  ALA   B N     1 
ATOM   12764 C  CA    . ALA   B  1 562  ? 7.082   6.566   81.854  1.00 23.30 ? 560  ALA   B CA    1 
ATOM   12765 C  C     . ALA   B  1 562  ? 7.203   6.891   80.366  1.00 25.40 ? 560  ALA   B C     1 
ATOM   12766 O  O     . ALA   B  1 562  ? 8.153   6.459   79.706  1.00 24.61 ? 560  ALA   B O     1 
ATOM   12767 C  CB    . ALA   B  1 562  ? 6.046   5.467   82.087  1.00 23.32 ? 560  ALA   B CB    1 
ATOM   12768 N  N     . SER   B  1 563  ? 6.261   7.656   79.818  1.00 23.52 ? 561  SER   B N     1 
ATOM   12769 C  CA    . SER   B  1 563  ? 6.332   7.957   78.392  1.00 24.22 ? 561  SER   B CA    1 
ATOM   12770 C  C     . SER   B  1 563  ? 7.453   8.950   78.098  1.00 21.97 ? 561  SER   B C     1 
ATOM   12771 O  O     . SER   B  1 563  ? 8.110   8.865   77.050  1.00 22.00 ? 561  SER   B O     1 
ATOM   12772 C  CB    . SER   B  1 563  ? 4.984   8.482   77.900  1.00 29.74 ? 561  SER   B CB    1 
ATOM   12773 O  OG    . SER   B  1 563  ? 4.695   9.722   78.501  1.00 36.47 ? 561  SER   B OG    1 
ATOM   12774 N  N     . LEU   B  1 564  ? 7.690   9.896   79.010  1.00 19.47 ? 562  LEU   B N     1 
ATOM   12775 C  CA    . LEU   B  1 564  ? 8.804   10.821  78.841  1.00 22.78 ? 562  LEU   B CA    1 
ATOM   12776 C  C     . LEU   B  1 564  ? 10.137  10.086  78.910  1.00 21.49 ? 562  LEU   B C     1 
ATOM   12777 O  O     . LEU   B  1 564  ? 11.060  10.385  78.145  1.00 23.87 ? 562  LEU   B O     1 
ATOM   12778 C  CB    . LEU   B  1 564  ? 8.734   11.922  79.898  1.00 22.59 ? 562  LEU   B CB    1 
ATOM   12779 C  CG    . LEU   B  1 564  ? 9.821   12.979  79.846  1.00 25.50 ? 562  LEU   B CG    1 
ATOM   12780 C  CD1   . LEU   B  1 564  ? 9.740   13.716  78.513  1.00 22.99 ? 562  LEU   B CD1   1 
ATOM   12781 C  CD2   . LEU   B  1 564  ? 9.683   13.945  81.034  1.00 27.15 ? 562  LEU   B CD2   1 
ATOM   12782 N  N     . THR   B  1 565  ? 10.257  9.118   79.815  1.00 19.63 ? 563  THR   B N     1 
ATOM   12783 C  CA    . THR   B  1 565  ? 11.464  8.298   79.846  1.00 21.72 ? 563  THR   B CA    1 
ATOM   12784 C  C     . THR   B  1 565  ? 11.753  7.710   78.464  1.00 22.74 ? 563  THR   B C     1 
ATOM   12785 O  O     . THR   B  1 565  ? 12.879  7.786   77.964  1.00 22.98 ? 563  THR   B O     1 
ATOM   12786 C  CB    . THR   B  1 565  ? 11.319  7.192   80.888  1.00 23.68 ? 563  THR   B CB    1 
ATOM   12787 O  OG1   . THR   B  1 565  ? 11.229  7.777   82.192  1.00 22.00 ? 563  THR   B OG1   1 
ATOM   12788 C  CG2   . THR   B  1 565  ? 12.530  6.262   80.851  1.00 23.59 ? 563  THR   B CG2   1 
ATOM   12789 N  N     . GLU   B  1 566  ? 10.732  7.153   77.815  1.00 22.26 ? 564  GLU   B N     1 
ATOM   12790 C  CA    . GLU   B  1 566  ? 10.965  6.517   76.523  1.00 22.15 ? 564  GLU   B CA    1 
ATOM   12791 C  C     . GLU   B  1 566  ? 11.285  7.555   75.450  1.00 24.61 ? 564  GLU   B C     1 
ATOM   12792 O  O     . GLU   B  1 566  ? 12.184  7.341   74.632  1.00 23.99 ? 564  GLU   B O     1 
ATOM   12793 C  CB    . GLU   B  1 566  ? 9.762   5.655   76.123  1.00 26.09 ? 564  GLU   B CB    1 
ATOM   12794 N  N     . ALA   B  1 567  ? 10.591  8.700   75.459  1.00 19.33 ? 565  ALA   B N     1 
ATOM   12795 C  CA    . ALA   B  1 567  ? 10.891  9.756   74.489  1.00 21.13 ? 565  ALA   B CA    1 
ATOM   12796 C  C     . ALA   B  1 567  ? 12.290  10.324  74.690  1.00 22.37 ? 565  ALA   B C     1 
ATOM   12797 O  O     . ALA   B  1 567  ? 12.979  10.662  73.719  1.00 19.89 ? 565  ALA   B O     1 
ATOM   12798 C  CB    . ALA   B  1 567  ? 9.864   10.883  74.591  1.00 21.91 ? 565  ALA   B CB    1 
ATOM   12799 N  N     . LEU   B  1 568  ? 12.704  10.494  75.945  1.00 19.08 ? 566  LEU   B N     1 
ATOM   12800 C  CA    . LEU   B  1 568  ? 14.035  11.024  76.207  1.00 20.38 ? 566  LEU   B CA    1 
ATOM   12801 C  C     . LEU   B  1 568  ? 15.110  10.050  75.739  1.00 23.63 ? 566  LEU   B C     1 
ATOM   12802 O  O     . LEU   B  1 568  ? 16.077  10.454  75.081  1.00 21.99 ? 566  LEU   B O     1 
ATOM   12803 C  CB    . LEU   B  1 568  ? 14.197  11.330  77.694  1.00 18.70 ? 566  LEU   B CB    1 
ATOM   12804 C  CG    . LEU   B  1 568  ? 13.295  12.438  78.249  1.00 21.46 ? 566  LEU   B CG    1 
ATOM   12805 C  CD1   . LEU   B  1 568  ? 13.423  12.522  79.763  1.00 20.41 ? 566  LEU   B CD1   1 
ATOM   12806 C  CD2   . LEU   B  1 568  ? 13.601  13.793  77.600  1.00 19.62 ? 566  LEU   B CD2   1 
ATOM   12807 N  N     . ARG   B  1 569  ? 14.963  8.766   76.085  1.00 20.17 ? 567  ARG   B N     1 
ATOM   12808 C  CA    . ARG   B  1 569  ? 15.878  7.742   75.586  1.00 22.00 ? 567  ARG   B CA    1 
ATOM   12809 C  C     . ARG   B  1 569  ? 15.954  7.766   74.063  1.00 23.25 ? 567  ARG   B C     1 
ATOM   12810 O  O     . ARG   B  1 569  ? 17.046  7.741   73.484  1.00 25.32 ? 567  ARG   B O     1 
ATOM   12811 C  CB    . ARG   B  1 569  ? 15.428  6.360   76.062  1.00 24.54 ? 567  ARG   B CB    1 
ATOM   12812 C  CG    . ARG   B  1 569  ? 15.569  6.140   77.555  1.00 29.57 ? 567  ARG   B CG    1 
ATOM   12813 C  CD    . ARG   B  1 569  ? 15.237  4.708   77.934  1.00 32.40 ? 567  ARG   B CD    1 
ATOM   12814 N  NE    . ARG   B  1 569  ? 15.335  4.486   79.373  1.00 40.08 ? 567  ARG   B NE    1 
ATOM   12815 C  CZ    . ARG   B  1 569  ? 14.761  3.472   80.007  1.00 43.83 ? 567  ARG   B CZ    1 
ATOM   12816 N  NH1   . ARG   B  1 569  ? 13.996  2.604   79.366  1.00 42.94 ? 567  ARG   B NH1   1 
ATOM   12817 N  NH2   . ARG   B  1 569  ? 14.956  3.326   81.315  1.00 42.60 ? 567  ARG   B NH2   1 
ATOM   12818 N  N     . GLU   B  1 570  ? 14.794  7.811   73.401  1.00 24.21 ? 568  GLU   B N     1 
ATOM   12819 C  CA    . GLU   B  1 570  ? 14.765  7.838   71.940  1.00 21.24 ? 568  GLU   B CA    1 
ATOM   12820 C  C     . GLU   B  1 570  ? 15.440  9.090   71.393  1.00 23.66 ? 568  GLU   B C     1 
ATOM   12821 O  O     . GLU   B  1 570  ? 16.098  9.036   70.346  1.00 23.49 ? 568  GLU   B O     1 
ATOM   12822 C  CB    . GLU   B  1 570  ? 13.324  7.750   71.440  1.00 25.96 ? 568  GLU   B CB    1 
ATOM   12823 C  CG    . GLU   B  1 570  ? 12.672  6.402   71.712  1.00 34.53 ? 568  GLU   B CG    1 
ATOM   12824 C  CD    . GLU   B  1 570  ? 11.159  6.430   71.549  1.00 43.54 ? 568  GLU   B CD    1 
ATOM   12825 O  OE1   . GLU   B  1 570  ? 10.605  7.513   71.248  1.00 46.06 ? 568  GLU   B OE1   1 
ATOM   12826 O  OE2   . GLU   B  1 570  ? 10.525  5.365   71.724  1.00 46.88 ? 568  GLU   B OE2   1 
ATOM   12827 N  N     . SER   B  1 571  ? 15.281  10.228  72.086  1.00 21.26 ? 569  SER   B N     1 
ATOM   12828 C  CA    . SER   B  1 571  ? 15.920  11.464  71.639  1.00 21.88 ? 569  SER   B CA    1 
ATOM   12829 C  C     . SER   B  1 571  ? 17.431  11.318  71.641  1.00 25.75 ? 569  SER   B C     1 
ATOM   12830 O  O     . SER   B  1 571  ? 18.121  11.873  70.775  1.00 22.53 ? 569  SER   B O     1 
ATOM   12831 C  CB    . SER   B  1 571  ? 15.511  12.638  72.532  1.00 22.15 ? 569  SER   B CB    1 
ATOM   12832 O  OG    . SER   B  1 571  ? 16.198  12.588  73.785  1.00 24.05 ? 569  SER   B OG    1 
ATOM   12833 N  N     . ALA   B  1 572  ? 17.963  10.569  72.612  1.00 23.67 ? 570  ALA   B N     1 
ATOM   12834 C  CA    . ALA   B  1 572  ? 19.399  10.351  72.692  1.00 25.50 ? 570  ALA   B CA    1 
ATOM   12835 C  C     . ALA   B  1 572  ? 19.913  9.451   71.577  1.00 26.56 ? 570  ALA   B C     1 
ATOM   12836 O  O     . ALA   B  1 572  ? 21.120  9.446   71.308  1.00 28.85 ? 570  ALA   B O     1 
ATOM   12837 C  CB    . ALA   B  1 572  ? 19.763  9.753   74.049  1.00 25.43 ? 570  ALA   B CB    1 
ATOM   12838 N  N     . ALA   B  1 573  ? 19.039  8.685   70.934  1.00 24.19 ? 571  ALA   B N     1 
ATOM   12839 C  CA    . ALA   B  1 573  ? 19.465  7.805   69.856  1.00 27.98 ? 571  ALA   B CA    1 
ATOM   12840 C  C     . ALA   B  1 573  ? 19.374  8.459   68.478  1.00 25.94 ? 571  ALA   B C     1 
ATOM   12841 O  O     . ALA   B  1 573  ? 19.773  7.839   67.493  1.00 25.10 ? 571  ALA   B O     1 
ATOM   12842 C  CB    . ALA   B  1 573  ? 18.643  6.510   69.879  1.00 25.62 ? 571  ALA   B CB    1 
ATOM   12843 N  N     . MET   B  1 574  ? 18.863  9.682   68.385  1.00 22.68 ? 572  MET   B N     1 
ATOM   12844 C  CA    . MET   B  1 574  ? 18.754  10.364  67.101  1.00 20.60 ? 572  MET   B CA    1 
ATOM   12845 C  C     . MET   B  1 574  ? 20.077  11.014  66.719  1.00 24.29 ? 572  MET   B C     1 
ATOM   12846 O  O     . MET   B  1 574  ? 20.865  11.411  67.579  1.00 22.64 ? 572  MET   B O     1 
ATOM   12847 C  CB    . MET   B  1 574  ? 17.667  11.431  67.152  1.00 22.26 ? 572  MET   B CB    1 
ATOM   12848 C  CG    . MET   B  1 574  ? 16.268  10.858  67.320  1.00 25.71 ? 572  MET   B CG    1 
ATOM   12849 S  SD    . MET   B  1 574  ? 15.138  12.151  67.848  1.00 28.12 ? 572  MET   B SD    1 
ATOM   12850 C  CE    . MET   B  1 574  ? 13.600  11.230  68.006  1.00 29.53 ? 572  MET   B CE    1 
ATOM   12851 N  N     . LYS   B  1 575  ? 20.304  11.145  65.412  1.00 20.21 ? 573  LYS   B N     1 
ATOM   12852 C  CA    . LYS   B  1 575  ? 21.468  11.887  64.920  1.00 20.01 ? 573  LYS   B CA    1 
ATOM   12853 C  C     . LYS   B  1 575  ? 21.124  13.374  64.887  1.00 20.82 ? 573  LYS   B C     1 
ATOM   12854 O  O     . LYS   B  1 575  ? 20.413  13.845  63.996  1.00 21.25 ? 573  LYS   B O     1 
ATOM   12855 C  CB    . LYS   B  1 575  ? 21.891  11.392  63.543  1.00 20.49 ? 573  LYS   B CB    1 
ATOM   12856 C  CG    . LYS   B  1 575  ? 23.086  12.149  62.960  1.00 30.91 ? 573  LYS   B CG    1 
ATOM   12857 C  CD    . LYS   B  1 575  ? 23.587  11.479  61.671  1.00 32.43 ? 573  LYS   B CD    1 
ATOM   12858 C  CE    . LYS   B  1 575  ? 24.754  12.238  61.038  1.00 40.58 ? 573  LYS   B CE    1 
ATOM   12859 N  NZ    . LYS   B  1 575  ? 25.941  12.349  61.946  1.00 41.88 ? 573  LYS   B NZ    1 
ATOM   12860 N  N     . TRP   B  1 576  ? 21.645  14.120  65.854  1.00 19.82 ? 574  TRP   B N     1 
ATOM   12861 C  CA    . TRP   B  1 576  ? 21.426  15.557  65.940  1.00 20.10 ? 574  TRP   B CA    1 
ATOM   12862 C  C     . TRP   B  1 576  ? 22.553  16.292  65.231  1.00 21.26 ? 574  TRP   B C     1 
ATOM   12863 O  O     . TRP   B  1 576  ? 23.730  16.101  65.562  1.00 21.93 ? 574  TRP   B O     1 
ATOM   12864 C  CB    . TRP   B  1 576  ? 21.365  15.999  67.392  1.00 22.10 ? 574  TRP   B CB    1 
ATOM   12865 C  CG    . TRP   B  1 576  ? 20.217  15.429  68.106  1.00 21.18 ? 574  TRP   B CG    1 
ATOM   12866 C  CD1   . TRP   B  1 576  ? 20.241  14.442  69.047  1.00 22.45 ? 574  TRP   B CD1   1 
ATOM   12867 C  CD2   . TRP   B  1 576  ? 18.852  15.821  67.957  1.00 18.15 ? 574  TRP   B CD2   1 
ATOM   12868 N  NE1   . TRP   B  1 576  ? 18.962  14.193  69.496  1.00 19.45 ? 574  TRP   B NE1   1 
ATOM   12869 C  CE2   . TRP   B  1 576  ? 18.093  15.029  68.844  1.00 22.23 ? 574  TRP   B CE2   1 
ATOM   12870 C  CE3   . TRP   B  1 576  ? 18.197  16.766  67.162  1.00 21.37 ? 574  TRP   B CE3   1 
ATOM   12871 C  CZ2   . TRP   B  1 576  ? 16.706  15.147  68.952  1.00 20.10 ? 574  TRP   B CZ2   1 
ATOM   12872 C  CZ3   . TRP   B  1 576  ? 16.815  16.889  67.276  1.00 24.13 ? 574  TRP   B CZ3   1 
ATOM   12873 C  CH2   . TRP   B  1 576  ? 16.087  16.084  68.166  1.00 21.30 ? 574  TRP   B CH2   1 
ATOM   12874 N  N     . THR   B  1 577  ? 22.197  17.140  64.275  1.00 20.17 ? 575  THR   B N     1 
ATOM   12875 C  CA    . THR   B  1 577  ? 23.186  17.918  63.547  1.00 21.15 ? 575  THR   B CA    1 
ATOM   12876 C  C     . THR   B  1 577  ? 22.736  19.366  63.470  1.00 20.47 ? 575  THR   B C     1 
ATOM   12877 O  O     . THR   B  1 577  ? 21.561  19.698  63.661  1.00 20.34 ? 575  THR   B O     1 
ATOM   12878 C  CB    . THR   B  1 577  ? 23.433  17.373  62.120  1.00 22.00 ? 575  THR   B CB    1 
ATOM   12879 O  OG1   . THR   B  1 577  ? 22.237  17.507  61.340  1.00 22.93 ? 575  THR   B OG1   1 
ATOM   12880 C  CG2   . THR   B  1 577  ? 23.840  15.910  62.152  1.00 23.91 ? 575  THR   B CG2   1 
ATOM   12881 N  N     . ALA   B  1 578  ? 23.708  20.234  63.217  1.00 18.86 ? 576  ALA   B N     1 
ATOM   12882 C  CA    . ALA   B  1 578  ? 23.446  21.637  62.946  1.00 19.57 ? 576  ALA   B CA    1 
ATOM   12883 C  C     . ALA   B  1 578  ? 24.415  22.041  61.857  1.00 19.35 ? 576  ALA   B C     1 
ATOM   12884 O  O     . ALA   B  1 578  ? 25.609  21.735  61.940  1.00 21.27 ? 576  ALA   B O     1 
ATOM   12885 C  CB    . ALA   B  1 578  ? 23.624  22.519  64.195  1.00 16.43 ? 576  ALA   B CB    1 
ATOM   12886 N  N     . LEU   B  1 579  ? 23.904  22.677  60.820  1.00 20.26 ? 577  LEU   B N     1 
ATOM   12887 C  CA    . LEU   B  1 579  ? 24.742  23.052  59.698  1.00 19.56 ? 577  LEU   B CA    1 
ATOM   12888 C  C     . LEU   B  1 579  ? 24.408  24.475  59.293  1.00 19.06 ? 577  LEU   B C     1 
ATOM   12889 O  O     . LEU   B  1 579  ? 23.366  25.009  59.683  1.00 19.20 ? 577  LEU   B O     1 
ATOM   12890 C  CB    . LEU   B  1 579  ? 24.546  22.103  58.513  1.00 24.35 ? 577  LEU   B CB    1 
ATOM   12891 C  CG    . LEU   B  1 579  ? 25.104  20.708  58.785  1.00 25.90 ? 577  LEU   B CG    1 
ATOM   12892 C  CD1   . LEU   B  1 579  ? 23.937  19.769  58.981  1.00 28.65 ? 577  LEU   B CD1   1 
ATOM   12893 C  CD2   . LEU   B  1 579  ? 25.974  20.283  57.629  1.00 30.38 ? 577  LEU   B CD2   1 
ATOM   12894 N  N     . PRO   B  1 580  ? 25.273  25.113  58.528  1.00 17.24 ? 578  PRO   B N     1 
ATOM   12895 C  CA    . PRO   B  1 580  ? 24.887  26.390  57.935  1.00 17.75 ? 578  PRO   B CA    1 
ATOM   12896 C  C     . PRO   B  1 580  ? 23.781  26.140  56.931  1.00 18.81 ? 578  PRO   B C     1 
ATOM   12897 O  O     . PRO   B  1 580  ? 24.016  25.554  55.872  1.00 20.70 ? 578  PRO   B O     1 
ATOM   12898 C  CB    . PRO   B  1 580  ? 26.177  26.887  57.266  1.00 17.82 ? 578  PRO   B CB    1 
ATOM   12899 C  CG    . PRO   B  1 580  ? 27.293  26.054  57.912  1.00 20.28 ? 578  PRO   B CG    1 
ATOM   12900 C  CD    . PRO   B  1 580  ? 26.654  24.733  58.175  1.00 19.46 ? 578  PRO   B CD    1 
ATOM   12901 N  N     . GLN   B  1 581  ? 22.570  26.530  57.288  1.00 18.30 ? 579  GLN   B N     1 
ATOM   12902 C  CA    . GLN   B  1 581  ? 21.389  26.326  56.453  1.00 19.16 ? 579  GLN   B CA    1 
ATOM   12903 C  C     . GLN   B  1 581  ? 21.121  27.617  55.697  1.00 19.06 ? 579  GLN   B C     1 
ATOM   12904 O  O     . GLN   B  1 581  ? 20.430  28.506  56.187  1.00 21.60 ? 579  GLN   B O     1 
ATOM   12905 C  CB    . GLN   B  1 581  ? 20.186  25.929  57.299  1.00 17.96 ? 579  GLN   B CB    1 
ATOM   12906 C  CG    . GLN   B  1 581  ? 20.371  24.589  57.997  1.00 19.43 ? 579  GLN   B CG    1 
ATOM   12907 C  CD    . GLN   B  1 581  ? 20.449  23.422  57.025  1.00 23.63 ? 579  GLN   B CD    1 
ATOM   12908 O  OE1   . GLN   B  1 581  ? 20.195  23.571  55.819  1.00 23.79 ? 579  GLN   B OE1   1 
ATOM   12909 N  NE2   . GLN   B  1 581  ? 20.805  22.247  57.546  1.00 24.91 ? 579  GLN   B NE2   1 
ATOM   12910 N  N     . LEU   B  1 582  ? 21.682  27.719  54.494  1.00 18.73 ? 580  LEU   B N     1 
ATOM   12911 C  CA    . LEU   B  1 582  ? 21.433  28.890  53.677  1.00 19.00 ? 580  LEU   B CA    1 
ATOM   12912 C  C     . LEU   B  1 582  ? 20.134  28.715  52.899  1.00 21.87 ? 580  LEU   B C     1 
ATOM   12913 O  O     . LEU   B  1 582  ? 19.515  27.647  52.906  1.00 20.51 ? 580  LEU   B O     1 
ATOM   12914 C  CB    . LEU   B  1 582  ? 22.616  29.145  52.738  1.00 20.41 ? 580  LEU   B CB    1 
ATOM   12915 C  CG    . LEU   B  1 582  ? 23.768  29.972  53.350  1.00 24.27 ? 580  LEU   B CG    1 
ATOM   12916 C  CD1   . LEU   B  1 582  ? 24.395  29.355  54.625  1.00 25.30 ? 580  LEU   B CD1   1 
ATOM   12917 C  CD2   . LEU   B  1 582  ? 24.843  30.227  52.314  1.00 30.65 ? 580  LEU   B CD2   1 
ATOM   12918 N  N     . ALA   B  1 583  ? 19.709  29.794  52.231  1.00 17.88 ? 581  ALA   B N     1 
ATOM   12919 C  CA    . ALA   B  1 583  ? 18.475  29.728  51.453  1.00 22.65 ? 581  ALA   B CA    1 
ATOM   12920 C  C     . ALA   B  1 583  ? 18.551  28.646  50.379  1.00 24.38 ? 581  ALA   B C     1 
ATOM   12921 O  O     . ALA   B  1 583  ? 17.543  27.999  50.074  1.00 30.30 ? 581  ALA   B O     1 
ATOM   12922 C  CB    . ALA   B  1 583  ? 18.180  31.090  50.818  1.00 20.85 ? 581  ALA   B CB    1 
ATOM   12923 N  N     . THR   B  1 584  ? 19.738  28.420  49.816  1.00 21.55 ? 582  THR   B N     1 
ATOM   12924 C  CA    . THR   B  1 584  ? 19.950  27.469  48.734  1.00 23.67 ? 582  THR   B CA    1 
ATOM   12925 C  C     . THR   B  1 584  ? 20.294  26.071  49.226  1.00 24.72 ? 582  THR   B C     1 
ATOM   12926 O  O     . THR   B  1 584  ? 20.552  25.182  48.409  1.00 23.42 ? 582  THR   B O     1 
ATOM   12927 C  CB    . THR   B  1 584  ? 21.077  27.971  47.835  1.00 23.81 ? 582  THR   B CB    1 
ATOM   12928 O  OG1   . THR   B  1 584  ? 22.188  28.322  48.670  1.00 24.54 ? 582  THR   B OG1   1 
ATOM   12929 C  CG2   . THR   B  1 584  ? 20.628  29.202  47.085  1.00 30.36 ? 582  THR   B CG2   1 
ATOM   12930 N  N     . GLY   B  1 585  ? 20.338  25.860  50.531  1.00 24.44 ? 583  GLY   B N     1 
ATOM   12931 C  CA    . GLY   B  1 585  ? 20.647  24.563  51.071  1.00 22.42 ? 583  GLY   B CA    1 
ATOM   12932 C  C     . GLY   B  1 585  ? 21.761  24.659  52.083  1.00 25.37 ? 583  GLY   B C     1 
ATOM   12933 O  O     . GLY   B  1 585  ? 22.285  25.745  52.358  1.00 23.07 ? 583  GLY   B O     1 
ATOM   12934 N  N     . PRO   B  1 586  ? 22.144  23.521  52.662  1.00 23.06 ? 584  PRO   B N     1 
ATOM   12935 C  CA    . PRO   B  1 586  ? 23.215  23.529  53.665  1.00 23.13 ? 584  PRO   B CA    1 
ATOM   12936 C  C     . PRO   B  1 586  ? 24.570  23.760  53.016  1.00 22.29 ? 584  PRO   B C     1 
ATOM   12937 O  O     . PRO   B  1 586  ? 24.834  23.310  51.900  1.00 25.07 ? 584  PRO   B O     1 
ATOM   12938 C  CB    . PRO   B  1 586  ? 23.130  22.132  54.290  1.00 23.12 ? 584  PRO   B CB    1 
ATOM   12939 C  CG    . PRO   B  1 586  ? 22.569  21.287  53.195  1.00 24.68 ? 584  PRO   B CG    1 
ATOM   12940 C  CD    . PRO   B  1 586  ? 21.625  22.170  52.409  1.00 21.52 ? 584  PRO   B CD    1 
ATOM   12941 N  N     . ALA   B  1 587  ? 25.427  24.480  53.724  1.00 24.95 ? 585  ALA   B N     1 
ATOM   12942 C  CA    . ALA   B  1 587  ? 26.769  24.779  53.253  1.00 25.26 ? 585  ALA   B CA    1 
ATOM   12943 C  C     . ALA   B  1 587  ? 27.769  23.896  53.977  1.00 23.85 ? 585  ALA   B C     1 
ATOM   12944 O  O     . ALA   B  1 587  ? 27.516  23.409  55.080  1.00 24.87 ? 585  ALA   B O     1 
ATOM   12945 C  CB    . ALA   B  1 587  ? 27.114  26.258  53.475  1.00 24.07 ? 585  ALA   B CB    1 
ATOM   12946 N  N     . ALA   B  1 588  ? 28.910  23.683  53.333  1.00 25.75 ? 586  ALA   B N     1 
ATOM   12947 C  CA    . ALA   B  1 588  ? 29.979  22.913  53.940  1.00 29.84 ? 586  ALA   B CA    1 
ATOM   12948 C  C     . ALA   B  1 588  ? 30.750  23.783  54.925  1.00 29.55 ? 586  ALA   B C     1 
ATOM   12949 O  O     . ALA   B  1 588  ? 30.713  25.014  54.869  1.00 30.10 ? 586  ALA   B O     1 
ATOM   12950 C  CB    . ALA   B  1 588  ? 30.919  22.356  52.869  1.00 27.68 ? 586  ALA   B CB    1 
ATOM   12951 N  N     . GLY   B  1 589  ? 31.441  23.134  55.849  1.00 28.21 ? 587  GLY   B N     1 
ATOM   12952 C  CA    . GLY   B  1 589  ? 32.245  23.881  56.796  1.00 28.77 ? 587  GLY   B CA    1 
ATOM   12953 C  C     . GLY   B  1 589  ? 32.991  22.946  57.716  1.00 28.48 ? 587  GLY   B C     1 
ATOM   12954 O  O     . GLY   B  1 589  ? 32.964  21.728  57.547  1.00 28.68 ? 587  GLY   B O     1 
ATOM   12955 N  N     . GLU   B  1 590  ? 33.650  23.537  58.710  1.00 30.93 ? 588  GLU   B N     1 
ATOM   12956 C  CA    . GLU   B  1 590  ? 34.376  22.762  59.707  1.00 30.56 ? 588  GLU   B CA    1 
ATOM   12957 C  C     . GLU   B  1 590  ? 33.385  22.145  60.682  1.00 29.09 ? 588  GLU   B C     1 
ATOM   12958 O  O     . GLU   B  1 590  ? 32.507  22.837  61.206  1.00 28.89 ? 588  GLU   B O     1 
ATOM   12959 C  CB    . GLU   B  1 590  ? 35.369  23.650  60.454  1.00 29.40 ? 588  GLU   B CB    1 
ATOM   12960 N  N     . THR   B  1 591  ? 33.527  20.847  60.934  1.00 30.86 ? 589  THR   B N     1 
ATOM   12961 C  CA    . THR   B  1 591  ? 32.576  20.112  61.755  1.00 29.75 ? 589  THR   B CA    1 
ATOM   12962 C  C     . THR   B  1 591  ? 33.196  19.791  63.107  1.00 31.94 ? 589  THR   B C     1 
ATOM   12963 O  O     . THR   B  1 591  ? 34.342  19.336  63.177  1.00 30.53 ? 589  THR   B O     1 
ATOM   12964 C  CB    . THR   B  1 591  ? 32.121  18.835  61.050  1.00 33.37 ? 589  THR   B CB    1 
ATOM   12965 O  OG1   . THR   B  1 591  ? 31.458  19.197  59.833  1.00 32.99 ? 589  THR   B OG1   1 
ATOM   12966 C  CG2   . THR   B  1 591  ? 31.143  18.064  61.933  1.00 34.27 ? 589  THR   B CG2   1 
ATOM   12967 N  N     . ARG   B  1 592  ? 32.433  20.040  64.170  1.00 27.19 ? 590  ARG   B N     1 
ATOM   12968 C  CA    . ARG   B  1 592  ? 32.865  19.825  65.540  1.00 29.01 ? 590  ARG   B CA    1 
ATOM   12969 C  C     . ARG   B  1 592  ? 31.823  18.973  66.252  1.00 30.72 ? 590  ARG   B C     1 
ATOM   12970 O  O     . ARG   B  1 592  ? 30.670  18.892  65.832  1.00 25.09 ? 590  ARG   B O     1 
ATOM   12971 C  CB    . ARG   B  1 592  ? 33.050  21.159  66.281  1.00 28.12 ? 590  ARG   B CB    1 
ATOM   12972 N  N     . THR   B  1 593  ? 32.226  18.346  67.349  1.00 26.66 ? 591  THR   B N     1 
ATOM   12973 C  CA    A THR   B  1 593  ? 31.327  17.513  68.133  0.55 26.54 ? 591  THR   B CA    1 
ATOM   12974 C  CA    B THR   B  1 593  ? 31.316  17.517  68.126  0.45 26.55 ? 591  THR   B CA    1 
ATOM   12975 C  C     . THR   B  1 593  ? 30.725  18.325  69.276  1.00 25.76 ? 591  THR   B C     1 
ATOM   12976 O  O     . THR   B  1 593  ? 31.427  19.090  69.943  1.00 28.78 ? 591  THR   B O     1 
ATOM   12977 C  CB    A THR   B  1 593  ? 32.084  16.294  68.666  0.55 28.98 ? 591  THR   B CB    1 
ATOM   12978 C  CB    B THR   B  1 593  ? 32.028  16.274  68.661  0.45 28.97 ? 591  THR   B CB    1 
ATOM   12979 O  OG1   A THR   B  1 593  ? 32.372  15.404  67.581  0.55 30.34 ? 591  THR   B OG1   1 
ATOM   12980 O  OG1   B THR   B  1 593  ? 32.903  16.649  69.729  0.45 27.05 ? 591  THR   B OG1   1 
ATOM   12981 C  CG2   A THR   B  1 593  ? 31.276  15.561  69.701  0.55 27.11 ? 591  THR   B CG2   1 
ATOM   12982 C  CG2   B THR   B  1 593  ? 32.847  15.625  67.555  0.45 29.86 ? 591  THR   B CG2   1 
ATOM   12983 N  N     . VAL   B  1 594  ? 29.418  18.173  69.484  1.00 21.92 ? 592  VAL   B N     1 
ATOM   12984 C  CA    . VAL   B  1 594  ? 28.708  18.860  70.553  1.00 21.22 ? 592  VAL   B CA    1 
ATOM   12985 C  C     . VAL   B  1 594  ? 28.613  17.898  71.723  1.00 22.97 ? 592  VAL   B C     1 
ATOM   12986 O  O     . VAL   B  1 594  ? 28.133  16.769  71.567  1.00 22.18 ? 592  VAL   B O     1 
ATOM   12987 C  CB    . VAL   B  1 594  ? 27.317  19.331  70.100  1.00 21.27 ? 592  VAL   B CB    1 
ATOM   12988 C  CG1   . VAL   B  1 594  ? 26.579  20.040  71.257  1.00 15.96 ? 592  VAL   B CG1   1 
ATOM   12989 C  CG2   . VAL   B  1 594  ? 27.434  20.236  68.867  1.00 21.30 ? 592  VAL   B CG2   1 
ATOM   12990 N  N     . LEU   B  1 595  ? 29.095  18.325  72.883  1.00 25.95 ? 593  LEU   B N     1 
ATOM   12991 C  CA    . LEU   B  1 595  ? 29.209  17.454  74.042  1.00 24.94 ? 593  LEU   B CA    1 
ATOM   12992 C  C     . LEU   B  1 595  ? 28.214  17.855  75.119  1.00 22.41 ? 593  LEU   B C     1 
ATOM   12993 O  O     . LEU   B  1 595  ? 27.756  18.999  75.193  1.00 22.54 ? 593  LEU   B O     1 
ATOM   12994 C  CB    . LEU   B  1 595  ? 30.631  17.486  74.623  1.00 20.37 ? 593  LEU   B CB    1 
ATOM   12995 C  CG    . LEU   B  1 595  ? 31.730  17.011  73.679  1.00 24.37 ? 593  LEU   B CG    1 
ATOM   12996 C  CD1   . LEU   B  1 595  ? 33.091  17.159  74.345  1.00 28.19 ? 593  LEU   B CD1   1 
ATOM   12997 C  CD2   . LEU   B  1 595  ? 31.481  15.563  73.243  1.00 24.38 ? 593  LEU   B CD2   1 
ATOM   12998 N  N     . ASN   B  1 596  ? 27.888  16.878  75.953  1.00 18.52 ? 594  ASN   B N     1 
ATOM   12999 C  CA    . ASN   B  1 596  ? 27.062  17.099  77.131  1.00 23.48 ? 594  ASN   B CA    1 
ATOM   13000 C  C     . ASN   B  1 596  ? 27.895  17.804  78.196  1.00 20.80 ? 594  ASN   B C     1 
ATOM   13001 O  O     . ASN   B  1 596  ? 28.887  17.237  78.651  1.00 20.80 ? 594  ASN   B O     1 
ATOM   13002 C  CB    . ASN   B  1 596  ? 26.568  15.746  77.641  1.00 22.33 ? 594  ASN   B CB    1 
ATOM   13003 C  CG    . ASN   B  1 596  ? 25.504  15.860  78.692  1.00 22.83 ? 594  ASN   B CG    1 
ATOM   13004 O  OD1   . ASN   B  1 596  ? 25.471  16.815  79.457  1.00 20.57 ? 594  ASN   B OD1   1 
ATOM   13005 N  ND2   . ASN   B  1 596  ? 24.623  14.865  78.746  1.00 21.46 ? 594  ASN   B ND2   1 
ATOM   13006 N  N     . PRO   B  1 597  ? 27.538  19.021  78.619  1.00 19.40 ? 595  PRO   B N     1 
ATOM   13007 C  CA    . PRO   B  1 597  ? 28.352  19.694  79.648  1.00 22.67 ? 595  PRO   B CA    1 
ATOM   13008 C  C     . PRO   B  1 597  ? 28.398  18.931  80.957  1.00 18.39 ? 595  PRO   B C     1 
ATOM   13009 O  O     . PRO   B  1 597  ? 29.349  19.113  81.725  1.00 22.19 ? 595  PRO   B O     1 
ATOM   13010 C  CB    . PRO   B  1 597  ? 27.676  21.064  79.816  1.00 22.12 ? 595  PRO   B CB    1 
ATOM   13011 C  CG    . PRO   B  1 597  ? 26.313  20.924  79.181  1.00 22.98 ? 595  PRO   B CG    1 
ATOM   13012 C  CD    . PRO   B  1 597  ? 26.448  19.874  78.112  1.00 18.27 ? 595  PRO   B CD    1 
ATOM   13013 N  N     . GLY   B  1 598  ? 27.397  18.086  81.237  1.00 20.30 ? 596  GLY   B N     1 
ATOM   13014 C  CA    . GLY   B  1 598  ? 27.427  17.257  82.430  1.00 20.20 ? 596  GLY   B CA    1 
ATOM   13015 C  C     . GLY   B  1 598  ? 28.264  16.004  82.306  1.00 21.21 ? 596  GLY   B C     1 
ATOM   13016 O  O     . GLY   B  1 598  ? 28.521  15.328  83.307  1.00 21.33 ? 596  GLY   B O     1 
ATOM   13017 N  N     . ASP   B  1 599  ? 28.719  15.691  81.103  1.00 20.54 ? 597  ASP   B N     1 
ATOM   13018 C  CA    . ASP   B  1 599  ? 29.497  14.484  80.883  1.00 22.94 ? 597  ASP   B CA    1 
ATOM   13019 C  C     . ASP   B  1 599  ? 30.044  14.537  79.467  1.00 24.43 ? 597  ASP   B C     1 
ATOM   13020 O  O     . ASP   B  1 599  ? 29.334  14.218  78.509  1.00 22.82 ? 597  ASP   B O     1 
ATOM   13021 C  CB    . ASP   B  1 599  ? 28.636  13.241  81.103  1.00 23.20 ? 597  ASP   B CB    1 
ATOM   13022 C  CG    . ASP   B  1 599  ? 29.423  11.946  81.017  1.00 29.82 ? 597  ASP   B CG    1 
ATOM   13023 O  OD1   . ASP   B  1 599  ? 30.587  11.955  80.553  1.00 28.24 ? 597  ASP   B OD1   1 
ATOM   13024 O  OD2   . ASP   B  1 599  ? 28.863  10.911  81.431  1.00 30.34 ? 597  ASP   B OD2   1 
ATOM   13025 N  N     . HIS   B  1 600  ? 31.308  14.932  79.335  1.00 23.52 ? 598  HIS   B N     1 
ATOM   13026 C  CA    . HIS   B  1 600  ? 31.915  15.099  78.024  1.00 25.63 ? 598  HIS   B CA    1 
ATOM   13027 C  C     . HIS   B  1 600  ? 32.083  13.785  77.276  1.00 26.40 ? 598  HIS   B C     1 
ATOM   13028 O  O     . HIS   B  1 600  ? 32.383  13.812  76.078  1.00 26.40 ? 598  HIS   B O     1 
ATOM   13029 C  CB    . HIS   B  1 600  ? 33.256  15.827  78.170  1.00 24.01 ? 598  HIS   B CB    1 
ATOM   13030 C  CG    . HIS   B  1 600  ? 33.109  17.294  78.428  1.00 26.10 ? 598  HIS   B CG    1 
ATOM   13031 N  ND1   . HIS   B  1 600  ? 34.178  18.164  78.451  1.00 28.16 ? 598  HIS   B ND1   1 
ATOM   13032 C  CD2   . HIS   B  1 600  ? 32.008  18.047  78.675  1.00 23.89 ? 598  HIS   B CD2   1 
ATOM   13033 C  CE1   . HIS   B  1 600  ? 33.743  19.388  78.697  1.00 26.53 ? 598  HIS   B CE1   1 
ATOM   13034 N  NE2   . HIS   B  1 600  ? 32.430  19.344  78.840  1.00 26.14 ? 598  HIS   B NE2   1 
ATOM   13035 N  N     . ARG   B  1 601  ? 31.879  12.644  77.934  1.00 24.21 ? 599  ARG   B N     1 
ATOM   13036 C  CA    . ARG   B  1 601  ? 31.855  11.387  77.204  1.00 25.31 ? 599  ARG   B CA    1 
ATOM   13037 C  C     . ARG   B  1 601  ? 30.573  11.222  76.406  1.00 24.54 ? 599  ARG   B C     1 
ATOM   13038 O  O     . ARG   B  1 601  ? 30.519  10.374  75.512  1.00 27.13 ? 599  ARG   B O     1 
ATOM   13039 C  CB    . ARG   B  1 601  ? 32.014  10.218  78.166  1.00 30.02 ? 599  ARG   B CB    1 
ATOM   13040 C  CG    . ARG   B  1 601  ? 33.217  10.334  79.062  1.00 30.86 ? 599  ARG   B CG    1 
ATOM   13041 C  CD    . ARG   B  1 601  ? 33.133  9.325   80.176  1.00 32.23 ? 599  ARG   B CD    1 
ATOM   13042 N  NE    . ARG   B  1 601  ? 31.923  9.506   80.966  1.00 32.10 ? 599  ARG   B NE    1 
ATOM   13043 C  CZ    . ARG   B  1 601  ? 31.562  8.714   81.966  1.00 38.41 ? 599  ARG   B CZ    1 
ATOM   13044 N  NH1   . ARG   B  1 601  ? 32.313  7.688   82.339  1.00 34.22 ? 599  ARG   B NH1   1 
ATOM   13045 N  NH2   . ARG   B  1 601  ? 30.424  8.958   82.608  1.00 34.55 ? 599  ARG   B NH2   1 
ATOM   13046 N  N     . ASP   B  1 602  ? 29.539  12.002  76.723  1.00 25.20 ? 600  ASP   B N     1 
ATOM   13047 C  CA    . ASP   B  1 602  ? 28.229  11.874  76.092  1.00 25.87 ? 600  ASP   B CA    1 
ATOM   13048 C  C     . ASP   B  1 602  ? 28.207  12.801  74.886  1.00 26.35 ? 600  ASP   B C     1 
ATOM   13049 O  O     . ASP   B  1 602  ? 28.077  14.020  75.024  1.00 27.51 ? 600  ASP   B O     1 
ATOM   13050 C  CB    . ASP   B  1 602  ? 27.123  12.202  77.088  1.00 26.85 ? 600  ASP   B CB    1 
ATOM   13051 C  CG    . ASP   B  1 602  ? 25.734  12.051  76.497  1.00 27.41 ? 600  ASP   B CG    1 
ATOM   13052 O  OD1   . ASP   B  1 602  ? 25.568  11.315  75.506  1.00 27.13 ? 600  ASP   B OD1   1 
ATOM   13053 O  OD2   . ASP   B  1 602  ? 24.808  12.694  77.019  1.00 26.10 ? 600  ASP   B OD2   1 
ATOM   13054 N  N     . VAL   B  1 603  ? 28.356  12.224  73.698  1.00 24.30 ? 601  VAL   B N     1 
ATOM   13055 C  CA    . VAL   B  1 603  ? 28.350  13.003  72.469  1.00 25.05 ? 601  VAL   B CA    1 
ATOM   13056 C  C     . VAL   B  1 603  ? 26.902  13.251  72.072  1.00 25.22 ? 601  VAL   B C     1 
ATOM   13057 O  O     . VAL   B  1 603  ? 26.134  12.308  71.856  1.00 28.75 ? 601  VAL   B O     1 
ATOM   13058 C  CB    . VAL   B  1 603  ? 29.117  12.283  71.357  1.00 27.10 ? 601  VAL   B CB    1 
ATOM   13059 C  CG1   . VAL   B  1 603  ? 28.910  12.995  70.030  1.00 27.13 ? 601  VAL   B CG1   1 
ATOM   13060 C  CG2   . VAL   B  1 603  ? 30.593  12.210  71.720  1.00 28.18 ? 601  VAL   B CG2   1 
ATOM   13061 N  N     . VAL   B  1 604  ? 26.518  14.517  72.004  1.00 21.21 ? 602  VAL   B N     1 
ATOM   13062 C  CA    . VAL   B  1 604  ? 25.128  14.845  71.707  1.00 19.59 ? 602  VAL   B CA    1 
ATOM   13063 C  C     . VAL   B  1 604  ? 24.880  14.904  70.206  1.00 23.26 ? 602  VAL   B C     1 
ATOM   13064 O  O     . VAL   B  1 604  ? 23.853  14.425  69.724  1.00 23.82 ? 602  VAL   B O     1 
ATOM   13065 C  CB    . VAL   B  1 604  ? 24.738  16.166  72.391  1.00 21.38 ? 602  VAL   B CB    1 
ATOM   13066 C  CG1   . VAL   B  1 604  ? 23.251  16.444  72.177  1.00 18.67 ? 602  VAL   B CG1   1 
ATOM   13067 C  CG2   . VAL   B  1 604  ? 25.051  16.098  73.874  1.00 22.36 ? 602  VAL   B CG2   1 
ATOM   13068 N  N     . GLY   B  1 605  ? 25.815  15.466  69.453  1.00 19.71 ? 603  GLY   B N     1 
ATOM   13069 C  CA    . GLY   B  1 605  ? 25.620  15.611  68.025  1.00 20.64 ? 603  GLY   B CA    1 
ATOM   13070 C  C     . GLY   B  1 605  ? 26.827  16.284  67.418  1.00 25.21 ? 603  GLY   B C     1 
ATOM   13071 O  O     . GLY   B  1 605  ? 27.898  16.317  68.023  1.00 23.67 ? 603  GLY   B O     1 
ATOM   13072 N  N     . SER   B  1 606  ? 26.654  16.832  66.222  1.00 22.45 ? 604  SER   B N     1 
ATOM   13073 C  CA    . SER   B  1 606  ? 27.768  17.469  65.535  1.00 23.68 ? 604  SER   B CA    1 
ATOM   13074 C  C     . SER   B  1 606  ? 27.279  18.747  64.874  1.00 25.40 ? 604  SER   B C     1 
ATOM   13075 O  O     . SER   B  1 606  ? 26.134  18.840  64.422  1.00 22.71 ? 604  SER   B O     1 
ATOM   13076 C  CB    . SER   B  1 606  ? 28.419  16.534  64.503  1.00 29.50 ? 604  SER   B CB    1 
ATOM   13077 O  OG    . SER   B  1 606  ? 27.643  16.424  63.335  1.00 34.57 ? 604  SER   B OG    1 
ATOM   13078 N  N     . VAL   B  1 607  ? 28.149  19.747  64.847  1.00 21.44 ? 605  VAL   B N     1 
ATOM   13079 C  CA    . VAL   B  1 607  ? 27.817  21.036  64.262  1.00 19.13 ? 605  VAL   B CA    1 
ATOM   13080 C  C     . VAL   B  1 607  ? 28.821  21.329  63.157  1.00 24.02 ? 605  VAL   B C     1 
ATOM   13081 O  O     . VAL   B  1 607  ? 30.030  21.127  63.329  1.00 24.09 ? 605  VAL   B O     1 
ATOM   13082 C  CB    . VAL   B  1 607  ? 27.805  22.158  65.315  1.00 22.58 ? 605  VAL   B CB    1 
ATOM   13083 C  CG1   . VAL   B  1 607  ? 29.118  22.171  66.109  1.00 25.16 ? 605  VAL   B CG1   1 
ATOM   13084 C  CG2   . VAL   B  1 607  ? 27.543  23.504  64.631  1.00 19.30 ? 605  VAL   B CG2   1 
ATOM   13085 N  N     . THR   B  1 608  ? 28.318  21.780  62.022  1.00 22.08 ? 606  THR   B N     1 
ATOM   13086 C  CA    . THR   B  1 608  ? 29.158  22.301  60.958  1.00 23.04 ? 606  THR   B CA    1 
ATOM   13087 C  C     . THR   B  1 608  ? 29.071  23.817  61.024  1.00 20.88 ? 606  THR   B C     1 
ATOM   13088 O  O     . THR   B  1 608  ? 27.978  24.389  60.947  1.00 19.42 ? 606  THR   B O     1 
ATOM   13089 C  CB    . THR   B  1 608  ? 28.707  21.770  59.604  1.00 24.14 ? 606  THR   B CB    1 
ATOM   13090 O  OG1   . THR   B  1 608  ? 28.837  20.345  59.607  1.00 24.93 ? 606  THR   B OG1   1 
ATOM   13091 C  CG2   . THR   B  1 608  ? 29.552  22.363  58.487  1.00 24.13 ? 606  THR   B CG2   1 
ATOM   13092 N  N     . GLU   B  1 609  ? 30.204  24.467  61.216  1.00 21.19 ? 607  GLU   B N     1 
ATOM   13093 C  CA    . GLU   B  1 609  ? 30.152  25.893  61.470  1.00 25.10 ? 607  GLU   B CA    1 
ATOM   13094 C  C     . GLU   B  1 609  ? 30.342  26.681  60.178  1.00 19.89 ? 607  GLU   B C     1 
ATOM   13095 O  O     . GLU   B  1 609  ? 30.838  26.169  59.172  1.00 23.77 ? 607  GLU   B O     1 
ATOM   13096 C  CB    . GLU   B  1 609  ? 31.166  26.269  62.549  1.00 26.63 ? 607  GLU   B CB    1 
ATOM   13097 C  CG    . GLU   B  1 609  ? 30.644  25.776  63.898  1.00 24.85 ? 607  GLU   B CG    1 
ATOM   13098 C  CD    . GLU   B  1 609  ? 31.580  26.020  65.072  1.00 33.61 ? 607  GLU   B CD    1 
ATOM   13099 O  OE1   . GLU   B  1 609  ? 32.790  26.271  64.856  1.00 32.07 ? 607  GLU   B OE1   1 
ATOM   13100 O  OE2   . GLU   B  1 609  ? 31.085  25.945  66.217  1.00 29.13 ? 607  GLU   B OE2   1 
ATOM   13101 N  N     . THR   B  1 610  ? 29.891  27.929  60.218  1.00 23.06 ? 608  THR   B N     1 
ATOM   13102 C  CA    . THR   B  1 610  ? 29.707  28.752  59.030  1.00 21.19 ? 608  THR   B CA    1 
ATOM   13103 C  C     . THR   B  1 610  ? 30.982  29.514  58.709  1.00 22.39 ? 608  THR   B C     1 
ATOM   13104 O  O     . THR   B  1 610  ? 31.547  30.175  59.582  1.00 23.20 ? 608  THR   B O     1 
ATOM   13105 C  CB    . THR   B  1 610  ? 28.575  29.748  59.252  1.00 18.48 ? 608  THR   B CB    1 
ATOM   13106 O  OG1   . THR   B  1 610  ? 27.429  29.064  59.769  1.00 20.81 ? 608  THR   B OG1   1 
ATOM   13107 C  CG2   . THR   B  1 610  ? 28.209  30.458  57.937  1.00 19.46 ? 608  THR   B CG2   1 
ATOM   13108 N  N     . SER   B  1 611  ? 31.408  29.457  57.452  1.00 20.54 ? 609  SER   B N     1 
ATOM   13109 C  CA    . SER   B  1 611  ? 32.513  30.307  57.030  1.00 27.66 ? 609  SER   B CA    1 
ATOM   13110 C  C     . SER   B  1 611  ? 32.038  31.751  56.933  1.00 28.75 ? 609  SER   B C     1 
ATOM   13111 O  O     . SER   B  1 611  ? 30.852  32.022  56.722  1.00 22.59 ? 609  SER   B O     1 
ATOM   13112 C  CB    . SER   B  1 611  ? 33.072  29.847  55.682  1.00 25.75 ? 609  SER   B CB    1 
ATOM   13113 O  OG    . SER   B  1 611  ? 32.188  30.209  54.630  1.00 26.10 ? 609  SER   B OG    1 
ATOM   13114 N  N     . GLU   B  1 612  ? 32.971  32.692  57.104  1.00 28.56 ? 610  GLU   B N     1 
ATOM   13115 C  CA    . GLU   B  1 612  ? 32.581  34.098  57.027  1.00 29.37 ? 610  GLU   B CA    1 
ATOM   13116 C  C     . GLU   B  1 612  ? 32.050  34.434  55.639  1.00 25.95 ? 610  GLU   B C     1 
ATOM   13117 O  O     . GLU   B  1 612  ? 31.099  35.210  55.505  1.00 27.86 ? 610  GLU   B O     1 
ATOM   13118 C  CB    . GLU   B  1 612  ? 33.756  35.005  57.401  1.00 32.74 ? 610  GLU   B CB    1 
ATOM   13119 C  CG    . GLU   B  1 612  ? 34.120  34.929  58.876  1.00 34.32 ? 610  GLU   B CG    1 
ATOM   13120 C  CD    . GLU   B  1 612  ? 35.275  35.847  59.260  1.00 46.81 ? 610  GLU   B CD    1 
ATOM   13121 O  OE1   . GLU   B  1 612  ? 35.517  36.853  58.555  1.00 52.46 ? 610  GLU   B OE1   1 
ATOM   13122 O  OE2   . GLU   B  1 612  ? 35.942  35.555  60.274  1.00 43.66 ? 610  GLU   B OE2   1 
ATOM   13123 N  N     . GLU   B  1 613  ? 32.639  33.843  54.595  1.00 26.45 ? 611  GLU   B N     1 
ATOM   13124 C  CA    . GLU   B  1 613  ? 32.110  34.045  53.251  1.00 23.82 ? 611  GLU   B CA    1 
ATOM   13125 C  C     . GLU   B  1 613  ? 30.663  33.567  53.149  1.00 24.81 ? 611  GLU   B C     1 
ATOM   13126 O  O     . GLU   B  1 613  ? 29.829  34.229  52.526  1.00 24.94 ? 611  GLU   B O     1 
ATOM   13127 C  CB    . GLU   B  1 613  ? 32.992  33.334  52.223  1.00 28.54 ? 611  GLU   B CB    1 
ATOM   13128 N  N     . ASP   B  1 614  ? 30.340  32.423  53.760  1.00 24.95 ? 612  ASP   B N     1 
ATOM   13129 C  CA    . ASP   B  1 614  ? 28.957  31.946  53.707  1.00 24.77 ? 612  ASP   B CA    1 
ATOM   13130 C  C     . ASP   B  1 614  ? 28.040  32.782  54.580  1.00 24.35 ? 612  ASP   B C     1 
ATOM   13131 O  O     . ASP   B  1 614  ? 26.846  32.918  54.276  1.00 21.15 ? 612  ASP   B O     1 
ATOM   13132 C  CB    . ASP   B  1 614  ? 28.879  30.481  54.123  1.00 22.13 ? 612  ASP   B CB    1 
ATOM   13133 C  CG    . ASP   B  1 614  ? 29.336  29.545  53.028  1.00 27.78 ? 612  ASP   B CG    1 
ATOM   13134 O  OD1   . ASP   B  1 614  ? 29.186  29.906  51.842  1.00 31.96 ? 612  ASP   B OD1   1 
ATOM   13135 O  OD2   . ASP   B  1 614  ? 29.842  28.456  53.355  1.00 31.01 ? 612  ASP   B OD2   1 
ATOM   13136 N  N     . ALA   B  1 615  ? 28.560  33.323  55.683  1.00 22.28 ? 613  ALA   B N     1 
ATOM   13137 C  CA    . ALA   B  1 615  ? 27.757  34.246  56.474  1.00 23.39 ? 613  ALA   B CA    1 
ATOM   13138 C  C     . ALA   B  1 615  ? 27.359  35.454  55.641  1.00 23.53 ? 613  ALA   B C     1 
ATOM   13139 O  O     . ALA   B  1 615  ? 26.195  35.864  55.646  1.00 19.85 ? 613  ALA   B O     1 
ATOM   13140 C  CB    . ALA   B  1 615  ? 28.519  34.681  57.730  1.00 23.52 ? 613  ALA   B CB    1 
ATOM   13141 N  N     . ARG   B  1 616  ? 28.307  36.021  54.892  1.00 22.34 ? 614  ARG   B N     1 
ATOM   13142 C  CA    . ARG   B  1 616  ? 27.969  37.150  54.031  1.00 23.25 ? 614  ARG   B CA    1 
ATOM   13143 C  C     . ARG   B  1 616  ? 27.023  36.727  52.920  1.00 25.18 ? 614  ARG   B C     1 
ATOM   13144 O  O     . ARG   B  1 616  ? 26.079  37.458  52.592  1.00 24.54 ? 614  ARG   B O     1 
ATOM   13145 C  CB    . ARG   B  1 616  ? 29.236  37.780  53.454  1.00 27.11 ? 614  ARG   B CB    1 
ATOM   13146 C  CG    . ARG   B  1 616  ? 30.009  38.586  54.489  1.00 31.93 ? 614  ARG   B CG    1 
ATOM   13147 C  CD    . ARG   B  1 616  ? 31.197  39.309  53.866  1.00 32.41 ? 614  ARG   B CD    1 
ATOM   13148 N  NE    . ARG   B  1 616  ? 32.267  38.387  53.516  1.00 37.60 ? 614  ARG   B NE    1 
ATOM   13149 C  CZ    . ARG   B  1 616  ? 33.196  37.969  54.365  1.00 41.29 ? 614  ARG   B CZ    1 
ATOM   13150 N  NH1   . ARG   B  1 616  ? 33.203  38.364  55.631  1.00 42.45 ? 614  ARG   B NH1   1 
ATOM   13151 N  NH2   . ARG   B  1 616  ? 34.136  37.132  53.937  1.00 40.81 ? 614  ARG   B NH2   1 
ATOM   13152 N  N     . ARG   B  1 617  ? 27.251  35.546  52.342  1.00 24.19 ? 615  ARG   B N     1 
ATOM   13153 C  CA    . ARG   B  1 617  ? 26.344  35.044  51.315  1.00 24.17 ? 615  ARG   B CA    1 
ATOM   13154 C  C     . ARG   B  1 617  ? 24.930  34.931  51.858  1.00 22.90 ? 615  ARG   B C     1 
ATOM   13155 O  O     . ARG   B  1 617  ? 23.966  35.311  51.184  1.00 23.22 ? 615  ARG   B O     1 
ATOM   13156 C  CB    . ARG   B  1 617  ? 26.837  33.691  50.785  1.00 26.44 ? 615  ARG   B CB    1 
ATOM   13157 C  CG    . ARG   B  1 617  ? 25.950  33.084  49.688  1.00 27.90 ? 615  ARG   B CG    1 
ATOM   13158 C  CD    . ARG   B  1 617  ? 26.726  32.140  48.771  1.00 37.80 ? 615  ARG   B CD    1 
ATOM   13159 N  NE    . ARG   B  1 617  ? 27.090  30.874  49.402  1.00 42.67 ? 615  ARG   B NE    1 
ATOM   13160 C  CZ    . ARG   B  1 617  ? 26.408  29.741  49.261  1.00 48.68 ? 615  ARG   B CZ    1 
ATOM   13161 N  NH1   . ARG   B  1 617  ? 25.297  29.685  48.539  1.00 51.50 ? 615  ARG   B NH1   1 
ATOM   13162 N  NH2   . ARG   B  1 617  ? 26.850  28.636  49.859  1.00 47.56 ? 615  ARG   B NH2   1 
ATOM   13163 N  N     . ALA   B  1 618  ? 24.789  34.448  53.095  1.00 20.24 ? 616  ALA   B N     1 
ATOM   13164 C  CA    . ALA   B  1 618  ? 23.459  34.317  53.685  1.00 20.06 ? 616  ALA   B CA    1 
ATOM   13165 C  C     . ALA   B  1 618  ? 22.757  35.664  53.765  1.00 19.71 ? 616  ALA   B C     1 
ATOM   13166 O  O     . ALA   B  1 618  ? 21.557  35.761  53.493  1.00 20.40 ? 616  ALA   B O     1 
ATOM   13167 C  CB    . ALA   B  1 618  ? 23.547  33.690  55.079  1.00 20.15 ? 616  ALA   B CB    1 
ATOM   13168 N  N     . VAL   B  1 619  ? 23.486  36.718  54.145  1.00 20.36 ? 617  VAL   B N     1 
ATOM   13169 C  CA    . VAL   B  1 619  ? 22.837  38.019  54.261  1.00 19.14 ? 617  VAL   B CA    1 
ATOM   13170 C  C     . VAL   B  1 619  ? 22.409  38.516  52.886  1.00 24.36 ? 617  VAL   B C     1 
ATOM   13171 O  O     . VAL   B  1 619  ? 21.309  39.055  52.724  1.00 21.70 ? 617  VAL   B O     1 
ATOM   13172 C  CB    . VAL   B  1 619  ? 23.749  39.021  54.988  1.00 19.57 ? 617  VAL   B CB    1 
ATOM   13173 C  CG1   . VAL   B  1 619  ? 23.075  40.383  55.074  1.00 22.99 ? 617  VAL   B CG1   1 
ATOM   13174 C  CG2   . VAL   B  1 619  ? 24.046  38.519  56.409  1.00 18.85 ? 617  VAL   B CG2   1 
ATOM   13175 N  N     . ARG   B  1 620  ? 23.250  38.315  51.866  1.00 22.52 ? 618  ARG   B N     1 
ATOM   13176 C  CA    . ARG   B  1 620  ? 22.832  38.669  50.514  1.00 24.91 ? 618  ARG   B CA    1 
ATOM   13177 C  C     . ARG   B  1 620  ? 21.593  37.882  50.100  1.00 23.58 ? 618  ARG   B C     1 
ATOM   13178 O  O     . ARG   B  1 620  ? 20.673  38.439  49.493  1.00 23.46 ? 618  ARG   B O     1 
ATOM   13179 C  CB    . ARG   B  1 620  ? 23.976  38.450  49.522  1.00 29.00 ? 618  ARG   B CB    1 
ATOM   13180 C  CG    . ARG   B  1 620  ? 25.194  39.309  49.800  1.00 31.99 ? 618  ARG   B CG    1 
ATOM   13181 C  CD    . ARG   B  1 620  ? 26.172  39.302  48.619  1.00 36.58 ? 618  ARG   B CD    1 
ATOM   13182 N  NE    . ARG   B  1 620  ? 26.594  37.948  48.280  1.00 42.38 ? 618  ARG   B NE    1 
ATOM   13183 C  CZ    . ARG   B  1 620  ? 27.692  37.361  48.738  1.00 34.87 ? 618  ARG   B CZ    1 
ATOM   13184 N  NH1   . ARG   B  1 620  ? 28.530  37.991  49.549  1.00 35.40 ? 618  ARG   B NH1   1 
ATOM   13185 N  NH2   . ARG   B  1 620  ? 27.957  36.109  48.373  1.00 39.37 ? 618  ARG   B NH2   1 
ATOM   13186 N  N     . LEU   B  1 621  ? 21.535  36.593  50.444  1.00 22.54 ? 619  LEU   B N     1 
ATOM   13187 C  CA    . LEU   B  1 621  ? 20.355  35.797  50.114  1.00 21.44 ? 619  LEU   B CA    1 
ATOM   13188 C  C     . LEU   B  1 621  ? 19.127  36.291  50.865  1.00 22.53 ? 619  LEU   B C     1 
ATOM   13189 O  O     . LEU   B  1 621  ? 18.022  36.323  50.311  1.00 22.36 ? 619  LEU   B O     1 
ATOM   13190 C  CB    . LEU   B  1 621  ? 20.601  34.318  50.417  1.00 21.29 ? 619  LEU   B CB    1 
ATOM   13191 C  CG    . LEU   B  1 621  ? 21.626  33.593  49.536  1.00 23.91 ? 619  LEU   B CG    1 
ATOM   13192 C  CD1   . LEU   B  1 621  ? 21.990  32.249  50.138  1.00 25.47 ? 619  LEU   B CD1   1 
ATOM   13193 C  CD2   . LEU   B  1 621  ? 21.097  33.417  48.110  1.00 28.18 ? 619  LEU   B CD2   1 
ATOM   13194 N  N     . ALA   B  1 622  ? 19.297  36.680  52.128  1.00 17.80 ? 620  ALA   B N     1 
ATOM   13195 C  CA    . ALA   B  1 622  ? 18.164  37.222  52.867  1.00 20.95 ? 620  ALA   B CA    1 
ATOM   13196 C  C     . ALA   B  1 622  ? 17.686  38.522  52.232  1.00 22.10 ? 620  ALA   B C     1 
ATOM   13197 O  O     . ALA   B  1 622  ? 16.478  38.752  52.103  1.00 20.26 ? 620  ALA   B O     1 
ATOM   13198 C  CB    . ALA   B  1 622  ? 18.545  37.439  54.335  1.00 16.26 ? 620  ALA   B CB    1 
ATOM   13199 N  N     . ALA   B  1 623  ? 18.627  39.373  51.805  1.00 20.98 ? 621  ALA   B N     1 
ATOM   13200 C  CA    . ALA   B  1 623  ? 18.254  40.630  51.157  1.00 23.54 ? 621  ALA   B CA    1 
ATOM   13201 C  C     . ALA   B  1 623  ? 17.452  40.379  49.886  1.00 23.94 ? 621  ALA   B C     1 
ATOM   13202 O  O     . ALA   B  1 623  ? 16.451  41.059  49.627  1.00 23.54 ? 621  ALA   B O     1 
ATOM   13203 C  CB    . ALA   B  1 623  ? 19.507  41.446  50.840  1.00 21.83 ? 621  ALA   B CB    1 
ATOM   13204 N  N     . ASP   B  1 624  ? 17.875  39.399  49.089  1.00 23.24 ? 622  ASP   B N     1 
ATOM   13205 C  CA    . ASP   B  1 624  ? 17.165  39.072  47.855  1.00 25.76 ? 622  ASP   B CA    1 
ATOM   13206 C  C     . ASP   B  1 624  ? 15.737  38.638  48.141  1.00 23.71 ? 622  ASP   B C     1 
ATOM   13207 O  O     . ASP   B  1 624  ? 14.817  38.951  47.380  1.00 27.46 ? 622  ASP   B O     1 
ATOM   13208 C  CB    . ASP   B  1 624  ? 17.893  37.953  47.110  1.00 28.96 ? 622  ASP   B CB    1 
ATOM   13209 C  CG    . ASP   B  1 624  ? 19.183  38.409  46.466  1.00 35.99 ? 622  ASP   B CG    1 
ATOM   13210 O  OD1   . ASP   B  1 624  ? 19.340  39.624  46.200  1.00 42.46 ? 622  ASP   B OD1   1 
ATOM   13211 O  OD2   . ASP   B  1 624  ? 20.045  37.534  46.210  1.00 42.52 ? 622  ASP   B OD2   1 
ATOM   13212 N  N     . ALA   B  1 625  ? 15.536  37.907  49.224  1.00 23.53 ? 623  ALA   B N     1 
ATOM   13213 C  CA    . ALA   B  1 625  ? 14.229  37.374  49.563  1.00 27.49 ? 623  ALA   B CA    1 
ATOM   13214 C  C     . ALA   B  1 625  ? 13.410  38.299  50.448  1.00 25.94 ? 623  ALA   B C     1 
ATOM   13215 O  O     . ALA   B  1 625  ? 12.246  37.988  50.728  1.00 25.90 ? 623  ALA   B O     1 
ATOM   13216 C  CB    . ALA   B  1 625  ? 14.387  36.031  50.268  1.00 33.11 ? 623  ALA   B CB    1 
ATOM   13217 N  N     . ALA   B  1 626  ? 13.978  39.415  50.903  1.00 21.72 ? 624  ALA   B N     1 
ATOM   13218 C  CA    . ALA   B  1 626  ? 13.258  40.262  51.854  1.00 23.91 ? 624  ALA   B CA    1 
ATOM   13219 C  C     . ALA   B  1 626  ? 11.929  40.769  51.312  1.00 21.67 ? 624  ALA   B C     1 
ATOM   13220 O  O     . ALA   B  1 626  ? 10.933  40.731  52.056  1.00 25.37 ? 624  ALA   B O     1 
ATOM   13221 C  CB    . ALA   B  1 626  ? 14.146  41.430  52.296  1.00 20.97 ? 624  ALA   B CB    1 
ATOM   13222 N  N     . PRO   B  1 627  ? 11.827  41.253  50.069  1.00 25.52 ? 625  PRO   B N     1 
ATOM   13223 C  CA    . PRO   B  1 627  ? 10.522  41.751  49.613  1.00 23.42 ? 625  PRO   B CA    1 
ATOM   13224 C  C     . PRO   B  1 627  ? 9.456   40.675  49.562  1.00 24.68 ? 625  PRO   B C     1 
ATOM   13225 O  O     . PRO   B  1 627  ? 8.296   40.954  49.887  1.00 24.13 ? 625  PRO   B O     1 
ATOM   13226 C  CB    . PRO   B  1 627  ? 10.833  42.318  48.221  1.00 26.30 ? 625  PRO   B CB    1 
ATOM   13227 C  CG    . PRO   B  1 627  ? 12.257  42.624  48.250  1.00 27.01 ? 625  PRO   B CG    1 
ATOM   13228 C  CD    . PRO   B  1 627  ? 12.882  41.552  49.084  1.00 27.15 ? 625  PRO   B CD    1 
ATOM   13229 N  N     . ASP   B  1 628  ? 9.813   39.450  49.166  1.00 24.16 ? 626  ASP   B N     1 
ATOM   13230 C  CA    . ASP   B  1 628  ? 8.816   38.386  49.089  1.00 24.47 ? 626  ASP   B CA    1 
ATOM   13231 C  C     . ASP   B  1 628  ? 8.258   38.051  50.465  1.00 27.25 ? 626  ASP   B C     1 
ATOM   13232 O  O     . ASP   B  1 628  ? 7.048   37.859  50.623  1.00 23.66 ? 626  ASP   B O     1 
ATOM   13233 C  CB    . ASP   B  1 628  ? 9.417   37.138  48.450  1.00 23.43 ? 626  ASP   B CB    1 
ATOM   13234 C  CG    . ASP   B  1 628  ? 9.739   37.333  46.982  1.00 32.33 ? 626  ASP   B CG    1 
ATOM   13235 O  OD1   . ASP   B  1 628  ? 9.020   38.106  46.317  1.00 30.75 ? 626  ASP   B OD1   1 
ATOM   13236 O  OD2   . ASP   B  1 628  ? 10.709  36.713  46.501  1.00 40.51 ? 626  ASP   B OD2   1 
ATOM   13237 N  N     . TRP   B  1 629  ? 9.124   37.978  51.477  1.00 22.35 ? 627  TRP   B N     1 
ATOM   13238 C  CA    . TRP   B  1 629  ? 8.642   37.689  52.821  1.00 20.73 ? 627  TRP   B CA    1 
ATOM   13239 C  C     . TRP   B  1 629  ? 7.848   38.865  53.388  1.00 19.99 ? 627  TRP   B C     1 
ATOM   13240 O  O     . TRP   B  1 629  ? 6.830   38.673  54.064  1.00 18.27 ? 627  TRP   B O     1 
ATOM   13241 C  CB    . TRP   B  1 629  ? 9.827   37.332  53.729  1.00 21.34 ? 627  TRP   B CB    1 
ATOM   13242 C  CG    . TRP   B  1 629  ? 9.392   37.033  55.134  1.00 17.75 ? 627  TRP   B CG    1 
ATOM   13243 C  CD1   . TRP   B  1 629  ? 9.741   37.716  56.273  1.00 17.32 ? 627  TRP   B CD1   1 
ATOM   13244 C  CD2   . TRP   B  1 629  ? 8.494   36.001  55.545  1.00 18.15 ? 627  TRP   B CD2   1 
ATOM   13245 N  NE1   . TRP   B  1 629  ? 9.122   37.151  57.367  1.00 18.16 ? 627  TRP   B NE1   1 
ATOM   13246 C  CE2   . TRP   B  1 629  ? 8.355   36.097  56.947  1.00 15.47 ? 627  TRP   B CE2   1 
ATOM   13247 C  CE3   . TRP   B  1 629  ? 7.808   34.984  54.870  1.00 18.52 ? 627  TRP   B CE3   1 
ATOM   13248 C  CZ2   . TRP   B  1 629  ? 7.546   35.227  57.677  1.00 14.45 ? 627  TRP   B CZ2   1 
ATOM   13249 C  CZ3   . TRP   B  1 629  ? 6.984   34.133  55.603  1.00 19.89 ? 627  TRP   B CZ3   1 
ATOM   13250 C  CH2   . TRP   B  1 629  ? 6.868   34.259  56.990  1.00 20.03 ? 627  TRP   B CH2   1 
ATOM   13251 N  N     . ALA   B  1 630  ? 8.291   40.092  53.120  1.00 19.55 ? 628  ALA   B N     1 
ATOM   13252 C  CA    . ALA   B  1 630  ? 7.542   41.249  53.593  1.00 24.08 ? 628  ALA   B CA    1 
ATOM   13253 C  C     . ALA   B  1 630  ? 6.139   41.280  53.002  1.00 24.38 ? 628  ALA   B C     1 
ATOM   13254 O  O     . ALA   B  1 630  ? 5.208   41.808  53.626  1.00 22.58 ? 628  ALA   B O     1 
ATOM   13255 C  CB    . ALA   B  1 630  ? 8.294   42.527  53.244  1.00 25.16 ? 628  ALA   B CB    1 
ATOM   13256 N  N     . ALA   B  1 631  ? 5.971   40.717  51.803  1.00 23.87 ? 629  ALA   B N     1 
ATOM   13257 C  CA    . ALA   B  1 631  ? 4.691   40.682  51.110  1.00 25.48 ? 629  ALA   B CA    1 
ATOM   13258 C  C     . ALA   B  1 631  ? 3.752   39.601  51.631  1.00 23.55 ? 629  ALA   B C     1 
ATOM   13259 O  O     . ALA   B  1 631  ? 2.574   39.602  51.259  1.00 20.44 ? 629  ALA   B O     1 
ATOM   13260 C  CB    . ALA   B  1 631  ? 4.915   40.484  49.608  1.00 24.29 ? 629  ALA   B CB    1 
ATOM   13261 N  N     . VAL   B  1 632  ? 4.228   38.681  52.463  1.00 19.11 ? 630  VAL   B N     1 
ATOM   13262 C  CA    . VAL   B  1 632  ? 3.311   37.720  53.087  1.00 19.88 ? 630  VAL   B CA    1 
ATOM   13263 C  C     . VAL   B  1 632  ? 2.451   38.468  54.093  1.00 21.84 ? 630  VAL   B C     1 
ATOM   13264 O  O     . VAL   B  1 632  ? 3.003   39.197  54.940  1.00 21.72 ? 630  VAL   B O     1 
ATOM   13265 C  CB    . VAL   B  1 632  ? 4.094   36.594  53.773  1.00 19.89 ? 630  VAL   B CB    1 
ATOM   13266 C  CG1   . VAL   B  1 632  ? 3.139   35.632  54.484  1.00 18.39 ? 630  VAL   B CG1   1 
ATOM   13267 C  CG2   . VAL   B  1 632  ? 4.969   35.853  52.760  1.00 21.64 ? 630  VAL   B CG2   1 
ATOM   13268 N  N     . PRO   B  1 633  ? 1.127   38.349  54.028  1.00 19.19 ? 631  PRO   B N     1 
ATOM   13269 C  CA    . PRO   B  1 633  ? 0.263   39.110  54.931  1.00 20.00 ? 631  PRO   B CA    1 
ATOM   13270 C  C     . PRO   B  1 633  ? 0.638   38.845  56.375  1.00 20.89 ? 631  PRO   B C     1 
ATOM   13271 O  O     . PRO   B  1 633  ? 1.000   37.715  56.727  1.00 18.54 ? 631  PRO   B O     1 
ATOM   13272 C  CB    . PRO   B  1 633  ? -1.139  38.572  54.613  1.00 20.96 ? 631  PRO   B CB    1 
ATOM   13273 C  CG    . PRO   B  1 633  ? -1.037  38.157  53.174  1.00 23.84 ? 631  PRO   B CG    1 
ATOM   13274 C  CD    . PRO   B  1 633  ? 0.351   37.596  53.027  1.00 20.15 ? 631  PRO   B CD    1 
ATOM   13275 N  N     . PRO   B  1 634  ? 0.577   39.866  57.231  1.00 22.24 ? 632  PRO   B N     1 
ATOM   13276 C  CA    . PRO   B  1 634  ? 0.949   39.661  58.640  1.00 23.10 ? 632  PRO   B CA    1 
ATOM   13277 C  C     . PRO   B  1 634  ? 0.228   38.493  59.280  1.00 17.95 ? 632  PRO   B C     1 
ATOM   13278 O  O     . PRO   B  1 634  ? 0.843   37.735  60.037  1.00 19.24 ? 632  PRO   B O     1 
ATOM   13279 C  CB    . PRO   B  1 634  ? 0.565   40.995  59.299  1.00 21.90 ? 632  PRO   B CB    1 
ATOM   13280 C  CG    . PRO   B  1 634  ? 0.610   41.994  58.185  1.00 27.85 ? 632  PRO   B CG    1 
ATOM   13281 C  CD    . PRO   B  1 634  ? 0.218   41.266  56.932  1.00 21.68 ? 632  PRO   B CD    1 
ATOM   13282 N  N     . SER   B  1 635  ? -1.072  38.337  59.024  1.00 19.38 ? 633  SER   B N     1 
ATOM   13283 C  CA    . SER   B  1 635  ? -1.787  37.231  59.650  1.00 20.15 ? 633  SER   B CA    1 
ATOM   13284 C  C     . SER   B  1 635  ? -1.267  35.888  59.155  1.00 18.50 ? 633  SER   B C     1 
ATOM   13285 O  O     . SER   B  1 635  ? -1.284  34.910  59.907  1.00 19.49 ? 633  SER   B O     1 
ATOM   13286 C  CB    . SER   B  1 635  ? -3.290  37.345  59.402  1.00 24.60 ? 633  SER   B CB    1 
ATOM   13287 O  OG    . SER   B  1 635  ? -3.585  37.193  58.024  1.00 30.68 ? 633  SER   B OG    1 
ATOM   13288 N  N     . GLU   B  1 636  ? -0.812  35.816  57.898  1.00 19.91 ? 634  GLU   B N     1 
ATOM   13289 C  CA    . GLU   B  1 636  ? -0.227  34.569  57.412  1.00 19.94 ? 634  GLU   B CA    1 
ATOM   13290 C  C     . GLU   B  1 636  ? 1.158   34.341  58.012  1.00 18.27 ? 634  GLU   B C     1 
ATOM   13291 O  O     . GLU   B  1 636  ? 1.542   33.199  58.293  1.00 18.64 ? 634  GLU   B O     1 
ATOM   13292 C  CB    . GLU   B  1 636  ? -0.160  34.568  55.884  1.00 18.47 ? 634  GLU   B CB    1 
ATOM   13293 N  N     . ARG   B  1 637  ? 1.927   35.407  58.225  1.00 15.89 ? 635  ARG   B N     1 
ATOM   13294 C  CA    . ARG   B  1 637  ? 3.190   35.216  58.930  1.00 15.80 ? 635  ARG   B CA    1 
ATOM   13295 C  C     . ARG   B  1 637  ? 2.933   34.761  60.360  1.00 18.65 ? 635  ARG   B C     1 
ATOM   13296 O  O     . ARG   B  1 637  ? 3.596   33.841  60.858  1.00 16.81 ? 635  ARG   B O     1 
ATOM   13297 C  CB    . ARG   B  1 637  ? 4.024   36.498  58.905  1.00 15.38 ? 635  ARG   B CB    1 
ATOM   13298 C  CG    . ARG   B  1 637  ? 4.325   37.011  57.505  1.00 14.12 ? 635  ARG   B CG    1 
ATOM   13299 C  CD    . ARG   B  1 637  ? 5.312   38.173  57.521  1.00 16.72 ? 635  ARG   B CD    1 
ATOM   13300 N  NE    . ARG   B  1 637  ? 4.888   39.291  58.359  1.00 17.19 ? 635  ARG   B NE    1 
ATOM   13301 C  CZ    . ARG   B  1 637  ? 4.605   40.509  57.919  1.00 22.77 ? 635  ARG   B CZ    1 
ATOM   13302 N  NH1   . ARG   B  1 637  ? 4.545   40.784  56.622  1.00 26.63 ? 635  ARG   B NH1   1 
ATOM   13303 N  NH2   . ARG   B  1 637  ? 4.401   41.486  58.801  1.00 19.67 ? 635  ARG   B NH2   1 
ATOM   13304 N  N     . ALA   B  1 638  ? 1.952   35.377  61.026  1.00 15.49 ? 636  ALA   B N     1 
ATOM   13305 C  CA    . ALA   B  1 638  ? 1.583   34.949  62.371  1.00 16.76 ? 636  ALA   B CA    1 
ATOM   13306 C  C     . ALA   B  1 638  ? 1.133   33.490  62.388  1.00 15.43 ? 636  ALA   B C     1 
ATOM   13307 O  O     . ALA   B  1 638  ? 1.418   32.760  63.345  1.00 15.22 ? 636  ALA   B O     1 
ATOM   13308 C  CB    . ALA   B  1 638  ? 0.482   35.858  62.917  1.00 15.72 ? 636  ALA   B CB    1 
ATOM   13309 N  N     . ALA   B  1 639  ? 0.416   33.050  61.348  1.00 19.00 ? 637  ALA   B N     1 
ATOM   13310 C  CA    . ALA   B  1 639  ? -0.010  31.652  61.287  1.00 19.33 ? 637  ALA   B CA    1 
ATOM   13311 C  C     . ALA   B  1 639  ? 1.180   30.700  61.255  1.00 17.14 ? 637  ALA   B C     1 
ATOM   13312 O  O     . ALA   B  1 639  ? 1.096   29.593  61.803  1.00 17.07 ? 637  ALA   B O     1 
ATOM   13313 C  CB    . ALA   B  1 639  ? -0.904  31.413  60.067  1.00 18.22 ? 637  ALA   B CB    1 
ATOM   13314 N  N     . CYS   B  1 640  ? 2.295   31.107  60.629  1.00 16.14 ? 638  CYS   B N     1 
ATOM   13315 C  CA    . CYS   B  1 640  ? 3.499   30.278  60.660  1.00 18.86 ? 638  CYS   B CA    1 
ATOM   13316 C  C     . CYS   B  1 640  ? 3.992   30.103  62.088  1.00 15.43 ? 638  CYS   B C     1 
ATOM   13317 O  O     . CYS   B  1 640  ? 4.291   28.988  62.528  1.00 15.26 ? 638  CYS   B O     1 
ATOM   13318 C  CB    . CYS   B  1 640  ? 4.609   30.896  59.809  1.00 16.75 ? 638  CYS   B CB    1 
ATOM   13319 S  SG    . CYS   B  1 640  ? 4.281   30.935  58.045  1.00 19.34 ? 638  CYS   B SG    1 
ATOM   13320 N  N     . LEU   B  1 641  ? 4.072   31.209  62.827  1.00 16.45 ? 639  LEU   B N     1 
ATOM   13321 C  CA    . LEU   B  1 641  ? 4.463   31.139  64.231  1.00 15.21 ? 639  LEU   B CA    1 
ATOM   13322 C  C     . LEU   B  1 641  ? 3.533   30.220  65.007  1.00 15.55 ? 639  LEU   B C     1 
ATOM   13323 O  O     . LEU   B  1 641  ? 3.984   29.387  65.807  1.00 14.62 ? 639  LEU   B O     1 
ATOM   13324 C  CB    . LEU   B  1 641  ? 4.458   32.541  64.842  1.00 13.94 ? 639  LEU   B CB    1 
ATOM   13325 C  CG    . LEU   B  1 641  ? 5.729   33.368  64.708  1.00 14.96 ? 639  LEU   B CG    1 
ATOM   13326 C  CD1   . LEU   B  1 641  ? 6.111   33.611  63.230  1.00 17.68 ? 639  LEU   B CD1   1 
ATOM   13327 C  CD2   . LEU   B  1 641  ? 5.600   34.681  65.472  1.00 15.57 ? 639  LEU   B CD2   1 
ATOM   13328 N  N     . ASP   B  1 642  ? 2.223   30.371  64.800  1.00 16.74 ? 640  ASP   B N     1 
ATOM   13329 C  CA    . ASP   B  1 642  ? 1.276   29.523  65.517  1.00 16.02 ? 640  ASP   B CA    1 
ATOM   13330 C  C     . ASP   B  1 642  ? 1.463   28.047  65.175  1.00 14.34 ? 640  ASP   B C     1 
ATOM   13331 O  O     . ASP   B  1 642  ? 1.373   27.182  66.058  1.00 15.43 ? 640  ASP   B O     1 
ATOM   13332 C  CB    . ASP   B  1 642  ? -0.151  29.954  65.219  1.00 15.14 ? 640  ASP   B CB    1 
ATOM   13333 C  CG    . ASP   B  1 642  ? -0.572  31.159  66.035  1.00 19.09 ? 640  ASP   B CG    1 
ATOM   13334 O  OD1   . ASP   B  1 642  ? 0.109   31.443  67.035  1.00 18.92 ? 640  ASP   B OD1   1 
ATOM   13335 O  OD2   . ASP   B  1 642  ? -1.581  31.814  65.684  1.00 20.32 ? 640  ASP   B OD2   1 
ATOM   13336 N  N     . ARG   B  1 643  ? 1.699   27.736  63.899  1.00 17.17 ? 641  ARG   B N     1 
ATOM   13337 C  CA    . ARG   B  1 643  ? 1.957   26.346  63.526  1.00 18.53 ? 641  ARG   B CA    1 
ATOM   13338 C  C     . ARG   B  1 643  ? 3.243   25.844  64.164  1.00 15.89 ? 641  ARG   B C     1 
ATOM   13339 O  O     . ARG   B  1 643  ? 3.308   24.704  64.638  1.00 16.13 ? 641  ARG   B O     1 
ATOM   13340 C  CB    . ARG   B  1 643  ? 2.011   26.196  62.003  1.00 16.98 ? 641  ARG   B CB    1 
ATOM   13341 C  CG    . ARG   B  1 643  ? 0.625   26.224  61.357  1.00 24.23 ? 641  ARG   B CG    1 
ATOM   13342 C  CD    . ARG   B  1 643  ? 0.674   25.838  59.892  1.00 24.50 ? 641  ARG   B CD    1 
ATOM   13343 N  NE    . ARG   B  1 643  ? 1.446   26.790  59.101  1.00 24.94 ? 641  ARG   B NE    1 
ATOM   13344 C  CZ    . ARG   B  1 643  ? 0.919   27.854  58.517  1.00 25.23 ? 641  ARG   B CZ    1 
ATOM   13345 N  NH1   . ARG   B  1 643  ? -0.375  28.125  58.623  1.00 20.59 ? 641  ARG   B NH1   1 
ATOM   13346 N  NH2   . ARG   B  1 643  ? 1.704   28.654  57.794  1.00 22.99 ? 641  ARG   B NH2   1 
ATOM   13347 N  N     . ALA   B  1 644  ? 4.274   26.688  64.196  1.00 14.76 ? 642  ALA   B N     1 
ATOM   13348 C  CA    . ALA   B  1 644  ? 5.523   26.291  64.834  1.00 14.01 ? 642  ALA   B CA    1 
ATOM   13349 C  C     . ALA   B  1 644  ? 5.300   26.018  66.314  1.00 17.51 ? 642  ALA   B C     1 
ATOM   13350 O  O     . ALA   B  1 644  ? 5.861   25.064  66.867  1.00 16.54 ? 642  ALA   B O     1 
ATOM   13351 C  CB    . ALA   B  1 644  ? 6.585   27.370  64.624  1.00 15.15 ? 642  ALA   B CB    1 
ATOM   13352 N  N     . ALA   B  1 645  ? 4.453   26.823  66.966  1.00 15.71 ? 643  ALA   B N     1 
ATOM   13353 C  CA    . ALA   B  1 645  ? 4.161   26.573  68.372  1.00 16.63 ? 643  ALA   B CA    1 
ATOM   13354 C  C     . ALA   B  1 645  ? 3.505   25.213  68.555  1.00 16.98 ? 643  ALA   B C     1 
ATOM   13355 O  O     . ALA   B  1 645  ? 3.841   24.481  69.495  1.00 16.49 ? 643  ALA   B O     1 
ATOM   13356 C  CB    . ALA   B  1 645  ? 3.282   27.688  68.936  1.00 16.85 ? 643  ALA   B CB    1 
ATOM   13357 N  N     . GLU   B  1 646  ? 2.580   24.853  67.654  1.00 16.95 ? 644  GLU   B N     1 
ATOM   13358 C  CA    . GLU   B  1 646  ? 1.926   23.547  67.741  1.00 22.27 ? 644  GLU   B CA    1 
ATOM   13359 C  C     . GLU   B  1 646  ? 2.937   22.418  67.607  1.00 19.34 ? 644  GLU   B C     1 
ATOM   13360 O  O     . GLU   B  1 646  ? 2.841   21.400  68.301  1.00 17.76 ? 644  GLU   B O     1 
ATOM   13361 C  CB    . GLU   B  1 646  ? 0.866   23.398  66.648  1.00 18.24 ? 644  GLU   B CB    1 
ATOM   13362 C  CG    . GLU   B  1 646  ? -0.310  24.315  66.799  1.00 21.66 ? 644  GLU   B CG    1 
ATOM   13363 C  CD    . GLU   B  1 646  ? -1.051  24.064  68.091  1.00 31.76 ? 644  GLU   B CD    1 
ATOM   13364 O  OE1   . GLU   B  1 646  ? -1.296  22.882  68.423  1.00 37.44 ? 644  GLU   B OE1   1 
ATOM   13365 O  OE2   . GLU   B  1 646  ? -1.374  25.049  68.784  1.00 33.55 ? 644  GLU   B OE2   1 
ATOM   13366 N  N     . LEU   B  1 647  ? 3.894   22.567  66.689  1.00 18.49 ? 645  LEU   B N     1 
ATOM   13367 C  CA    . LEU   B  1 647  ? 4.901   21.525  66.506  1.00 17.37 ? 645  LEU   B CA    1 
ATOM   13368 C  C     . LEU   B  1 647  ? 5.807   21.410  67.723  1.00 19.86 ? 645  LEU   B C     1 
ATOM   13369 O  O     . LEU   B  1 647  ? 6.141   20.300  68.147  1.00 18.95 ? 645  LEU   B O     1 
ATOM   13370 C  CB    . LEU   B  1 647  ? 5.732   21.804  65.260  1.00 17.52 ? 645  LEU   B CB    1 
ATOM   13371 C  CG    . LEU   B  1 647  ? 4.958   21.760  63.945  1.00 20.56 ? 645  LEU   B CG    1 
ATOM   13372 C  CD1   . LEU   B  1 647  ? 5.885   22.136  62.789  1.00 19.83 ? 645  LEU   B CD1   1 
ATOM   13373 C  CD2   . LEU   B  1 647  ? 4.335   20.395  63.725  1.00 23.32 ? 645  LEU   B CD2   1 
ATOM   13374 N  N     . MET   B  1 648  ? 6.233   22.544  68.286  1.00 15.88 ? 646  MET   B N     1 
ATOM   13375 C  CA    . MET   B  1 648  ? 7.047   22.488  69.494  1.00 16.30 ? 646  MET   B CA    1 
ATOM   13376 C  C     . MET   B  1 648  ? 6.283   21.855  70.643  1.00 17.73 ? 646  MET   B C     1 
ATOM   13377 O  O     . MET   B  1 648  ? 6.856   21.094  71.432  1.00 15.99 ? 646  MET   B O     1 
ATOM   13378 C  CB    . MET   B  1 648  ? 7.514   23.876  69.898  1.00 16.42 ? 646  MET   B CB    1 
ATOM   13379 C  CG    . MET   B  1 648  ? 8.506   24.477  68.946  1.00 18.04 ? 646  MET   B CG    1 
ATOM   13380 S  SD    . MET   B  1 648  ? 9.397   25.832  69.728  1.00 19.82 ? 646  MET   B SD    1 
ATOM   13381 C  CE    . MET   B  1 648  ? 10.379  26.361  68.331  1.00 20.59 ? 646  MET   B CE    1 
ATOM   13382 N  N     . GLN   B  1 649  ? 4.996   22.185  70.770  1.00 17.26 ? 647  GLN   B N     1 
ATOM   13383 C  CA    . GLN   B  1 649  ? 4.189   21.592  71.825  1.00 18.45 ? 647  GLN   B CA    1 
ATOM   13384 C  C     . GLN   B  1 649  ? 4.122   20.084  71.664  1.00 17.74 ? 647  GLN   B C     1 
ATOM   13385 O  O     . GLN   B  1 649  ? 4.296   19.338  72.633  1.00 21.29 ? 647  GLN   B O     1 
ATOM   13386 C  CB    . GLN   B  1 649  ? 2.781   22.181  71.808  1.00 17.38 ? 647  GLN   B CB    1 
ATOM   13387 C  CG    . GLN   B  1 649  ? 1.950   21.694  72.970  1.00 18.11 ? 647  GLN   B CG    1 
ATOM   13388 C  CD    . GLN   B  1 649  ? 2.419   22.317  74.277  1.00 19.72 ? 647  GLN   B CD    1 
ATOM   13389 O  OE1   . GLN   B  1 649  ? 2.112   23.475  74.572  1.00 19.24 ? 647  GLN   B OE1   1 
ATOM   13390 N  NE2   . GLN   B  1 649  ? 3.181   21.559  75.056  1.00 16.68 ? 647  GLN   B NE2   1 
ATOM   13391 N  N     . ALA   B  1 650  ? 3.841   19.622  70.443  1.00 17.74 ? 648  ALA   B N     1 
ATOM   13392 C  CA    . ALA   B  1 650  ? 3.693   18.194  70.193  1.00 17.51 ? 648  ALA   B CA    1 
ATOM   13393 C  C     . ALA   B  1 650  ? 5.013   17.464  70.378  1.00 22.33 ? 648  ALA   B C     1 
ATOM   13394 O  O     . ALA   B  1 650  ? 5.033   16.302  70.805  1.00 21.05 ? 648  ALA   B O     1 
ATOM   13395 C  CB    . ALA   B  1 650  ? 3.166   17.966  68.775  1.00 20.41 ? 648  ALA   B CB    1 
ATOM   13396 N  N     . ARG   B  1 651  ? 6.117   18.123  70.057  1.00 18.97 ? 649  ARG   B N     1 
ATOM   13397 C  CA    . ARG   B  1 651  ? 7.424   17.491  70.080  1.00 17.63 ? 649  ARG   B CA    1 
ATOM   13398 C  C     . ARG   B  1 651  ? 8.198   17.823  71.337  1.00 16.87 ? 649  ARG   B C     1 
ATOM   13399 O  O     . ARG   B  1 651  ? 9.376   17.489  71.432  1.00 19.48 ? 649  ARG   B O     1 
ATOM   13400 C  CB    . ARG   B  1 651  ? 8.197   17.892  68.826  1.00 21.95 ? 649  ARG   B CB    1 
ATOM   13401 C  CG    . ARG   B  1 651  ? 7.432   17.458  67.582  1.00 21.86 ? 649  ARG   B CG    1 
ATOM   13402 C  CD    . ARG   B  1 651  ? 8.055   17.917  66.286  1.00 24.54 ? 649  ARG   B CD    1 
ATOM   13403 N  NE    . ARG   B  1 651  ? 7.154   17.618  65.177  1.00 24.24 ? 649  ARG   B NE    1 
ATOM   13404 C  CZ    . ARG   B  1 651  ? 7.320   18.061  63.938  1.00 28.30 ? 649  ARG   B CZ    1 
ATOM   13405 N  NH1   . ARG   B  1 651  ? 8.351   18.823  63.613  1.00 22.21 ? 649  ARG   B NH1   1 
ATOM   13406 N  NH2   . ARG   B  1 651  ? 6.429   17.728  63.002  1.00 25.24 ? 649  ARG   B NH2   1 
ATOM   13407 N  N     . MET   B  1 652  ? 7.547   18.434  72.323  1.00 20.22 ? 650  MET   B N     1 
ATOM   13408 C  CA    . MET   B  1 652  ? 8.237   18.822  73.551  1.00 17.34 ? 650  MET   B CA    1 
ATOM   13409 C  C     . MET   B  1 652  ? 9.060   17.700  74.176  1.00 19.36 ? 650  MET   B C     1 
ATOM   13410 O  O     . MET   B  1 652  ? 10.207  17.964  74.562  1.00 20.55 ? 650  MET   B O     1 
ATOM   13411 C  CB    . MET   B  1 652  ? 7.216   19.385  74.552  1.00 16.98 ? 650  MET   B CB    1 
ATOM   13412 C  CG    . MET   B  1 652  ? 7.854   19.792  75.887  1.00 16.38 ? 650  MET   B CG    1 
ATOM   13413 S  SD    . MET   B  1 652  ? 6.604   20.442  77.022  1.00 22.20 ? 650  MET   B SD    1 
ATOM   13414 C  CE    . MET   B  1 652  ? 6.438   22.111  76.419  1.00 19.63 ? 650  MET   B CE    1 
ATOM   13415 N  N     . PRO   B  1 653  ? 8.570   16.457  74.306  1.00 18.70 ? 651  PRO   B N     1 
ATOM   13416 C  CA    . PRO   B  1 653  ? 9.419   15.421  74.923  1.00 20.23 ? 651  PRO   B CA    1 
ATOM   13417 C  C     . PRO   B  1 653  ? 10.757  15.244  74.237  1.00 19.46 ? 651  PRO   B C     1 
ATOM   13418 O  O     . PRO   B  1 653  ? 11.776  15.144  74.924  1.00 23.57 ? 651  PRO   B O     1 
ATOM   13419 C  CB    . PRO   B  1 653  ? 8.557   14.158  74.816  1.00 18.27 ? 651  PRO   B CB    1 
ATOM   13420 C  CG    . PRO   B  1 653  ? 7.163   14.683  74.870  1.00 19.98 ? 651  PRO   B CG    1 
ATOM   13421 C  CD    . PRO   B  1 653  ? 7.217   15.928  74.024  1.00 18.94 ? 651  PRO   B CD    1 
ATOM   13422 N  N     . THR   B  1 654  ? 10.786  15.232  72.900  1.00 20.01 ? 652  THR   B N     1 
ATOM   13423 C  CA    . THR   B  1 654  ? 12.059  15.104  72.191  1.00 20.69 ? 652  THR   B CA    1 
ATOM   13424 C  C     . THR   B  1 654  ? 12.919  16.351  72.358  1.00 23.03 ? 652  THR   B C     1 
ATOM   13425 O  O     . THR   B  1 654  ? 14.139  16.248  72.544  1.00 22.19 ? 652  THR   B O     1 
ATOM   13426 C  CB    . THR   B  1 654  ? 11.809  14.828  70.710  1.00 21.19 ? 652  THR   B CB    1 
ATOM   13427 O  OG1   . THR   B  1 654  ? 11.033  13.638  70.586  1.00 21.10 ? 652  THR   B OG1   1 
ATOM   13428 C  CG2   . THR   B  1 654  ? 13.138  14.654  69.954  1.00 19.56 ? 652  THR   B CG2   1 
ATOM   13429 N  N     . LEU   B  1 655  ? 12.308  17.537  72.293  1.00 18.71 ? 653  LEU   B N     1 
ATOM   13430 C  CA    . LEU   B  1 655  ? 13.074  18.765  72.496  1.00 22.26 ? 653  LEU   B CA    1 
ATOM   13431 C  C     . LEU   B  1 655  ? 13.700  18.799  73.882  1.00 18.39 ? 653  LEU   B C     1 
ATOM   13432 O  O     . LEU   B  1 655  ? 14.852  19.220  74.033  1.00 20.67 ? 653  LEU   B O     1 
ATOM   13433 C  CB    . LEU   B  1 655  ? 12.193  19.995  72.293  1.00 19.66 ? 653  LEU   B CB    1 
ATOM   13434 C  CG    . LEU   B  1 655  ? 11.485  20.096  70.946  1.00 25.04 ? 653  LEU   B CG    1 
ATOM   13435 C  CD1   . LEU   B  1 655  ? 10.646  21.379  70.862  1.00 22.09 ? 653  LEU   B CD1   1 
ATOM   13436 C  CD2   . LEU   B  1 655  ? 12.515  20.044  69.844  1.00 21.56 ? 653  LEU   B CD2   1 
ATOM   13437 N  N     . LEU   B  1 656  ? 12.954  18.361  74.906  1.00 19.35 ? 654  LEU   B N     1 
ATOM   13438 C  CA    . LEU   B  1 656  ? 13.513  18.261  76.256  1.00 20.83 ? 654  LEU   B CA    1 
ATOM   13439 C  C     . LEU   B  1 656  ? 14.800  17.464  76.264  1.00 21.41 ? 654  LEU   B C     1 
ATOM   13440 O  O     . LEU   B  1 656  ? 15.802  17.882  76.858  1.00 22.56 ? 654  LEU   B O     1 
ATOM   13441 C  CB    . LEU   B  1 656  ? 12.521  17.588  77.210  1.00 21.14 ? 654  LEU   B CB    1 
ATOM   13442 C  CG    . LEU   B  1 656  ? 11.162  18.223  77.359  1.00 23.59 ? 654  LEU   B CG    1 
ATOM   13443 C  CD1   . LEU   B  1 656  ? 10.341  17.505  78.430  1.00 23.63 ? 654  LEU   B CD1   1 
ATOM   13444 C  CD2   . LEU   B  1 656  ? 11.351  19.689  77.668  1.00 21.91 ? 654  LEU   B CD2   1 
ATOM   13445 N  N     . GLY   B  1 657  ? 14.780  16.282  75.644  1.00 18.99 ? 655  GLY   B N     1 
ATOM   13446 C  CA    . GLY   B  1 657  ? 15.947  15.425  75.701  1.00 22.33 ? 655  GLY   B CA    1 
ATOM   13447 C  C     . GLY   B  1 657  ? 17.167  16.092  75.108  1.00 22.80 ? 655  GLY   B C     1 
ATOM   13448 O  O     . GLY   B  1 657  ? 18.275  15.968  75.637  1.00 23.79 ? 655  GLY   B O     1 
ATOM   13449 N  N     . LEU   B  1 658  ? 16.977  16.815  74.000  1.00 19.80 ? 656  LEU   B N     1 
ATOM   13450 C  CA    . LEU   B  1 658  ? 18.085  17.557  73.412  1.00 19.18 ? 656  LEU   B CA    1 
ATOM   13451 C  C     . LEU   B  1 658  ? 18.522  18.709  74.310  1.00 21.29 ? 656  LEU   B C     1 
ATOM   13452 O  O     . LEU   B  1 658  ? 19.722  18.929  74.509  1.00 20.60 ? 656  LEU   B O     1 
ATOM   13453 C  CB    . LEU   B  1 658  ? 17.687  18.060  72.024  1.00 21.35 ? 656  LEU   B CB    1 
ATOM   13454 C  CG    . LEU   B  1 658  ? 18.801  18.759  71.249  1.00 20.75 ? 656  LEU   B CG    1 
ATOM   13455 C  CD1   . LEU   B  1 658  ? 19.978  17.820  71.085  1.00 22.63 ? 656  LEU   B CD1   1 
ATOM   13456 C  CD2   . LEU   B  1 658  ? 18.296  19.234  69.886  1.00 20.07 ? 656  LEU   B CD2   1 
ATOM   13457 N  N     . ILE   B  1 659  ? 17.568  19.459  74.868  1.00 19.31 ? 657  ILE   B N     1 
ATOM   13458 C  CA    . ILE   B  1 659  ? 17.932  20.587  75.725  1.00 17.15 ? 657  ILE   B CA    1 
ATOM   13459 C  C     . ILE   B  1 659  ? 18.651  20.093  76.971  1.00 20.06 ? 657  ILE   B C     1 
ATOM   13460 O  O     . ILE   B  1 659  ? 19.646  20.683  77.411  1.00 18.25 ? 657  ILE   B O     1 
ATOM   13461 C  CB    . ILE   B  1 659  ? 16.686  21.415  76.088  1.00 18.89 ? 657  ILE   B CB    1 
ATOM   13462 C  CG1   . ILE   B  1 659  ? 16.159  22.134  74.859  1.00 15.93 ? 657  ILE   B CG1   1 
ATOM   13463 C  CG2   . ILE   B  1 659  ? 16.992  22.417  77.210  1.00 20.96 ? 657  ILE   B CG2   1 
ATOM   13464 C  CD1   . ILE   B  1 659  ? 14.731  22.668  75.068  1.00 19.10 ? 657  ILE   B CD1   1 
ATOM   13465 N  N     . ILE   B  1 660  ? 18.157  19.002  77.554  1.00 18.22 ? 658  ILE   B N     1 
ATOM   13466 C  CA    . ILE   B  1 660  ? 18.791  18.445  78.744  1.00 18.24 ? 658  ILE   B CA    1 
ATOM   13467 C  C     . ILE   B  1 660  ? 20.243  18.100  78.455  1.00 17.80 ? 658  ILE   B C     1 
ATOM   13468 O  O     . ILE   B  1 660  ? 21.147  18.428  79.235  1.00 17.75 ? 658  ILE   B O     1 
ATOM   13469 C  CB    . ILE   B  1 660  ? 18.000  17.216  79.232  1.00 19.17 ? 658  ILE   B CB    1 
ATOM   13470 C  CG1   . ILE   B  1 660  ? 16.688  17.663  79.878  1.00 19.99 ? 658  ILE   B CG1   1 
ATOM   13471 C  CG2   . ILE   B  1 660  ? 18.855  16.349  80.173  1.00 20.23 ? 658  ILE   B CG2   1 
ATOM   13472 C  CD1   . ILE   B  1 660  ? 15.690  16.521  80.079  1.00 21.30 ? 658  ILE   B CD1   1 
ATOM   13473 N  N     . ARG   B  1 661  ? 20.496  17.456  77.321  1.00 18.57 ? 659  ARG   B N     1 
ATOM   13474 C  CA    . ARG   B  1 661  ? 21.840  16.937  77.095  1.00 19.65 ? 659  ARG   B CA    1 
ATOM   13475 C  C     . ARG   B  1 661  ? 22.770  17.949  76.444  1.00 20.92 ? 659  ARG   B C     1 
ATOM   13476 O  O     . ARG   B  1 661  ? 23.964  17.943  76.743  1.00 20.61 ? 659  ARG   B O     1 
ATOM   13477 C  CB    . ARG   B  1 661  ? 21.789  15.665  76.250  1.00 21.32 ? 659  ARG   B CB    1 
ATOM   13478 C  CG    . ARG   B  1 661  ? 21.292  14.486  77.041  1.00 22.72 ? 659  ARG   B CG    1 
ATOM   13479 C  CD    . ARG   B  1 661  ? 21.129  13.251  76.187  1.00 28.51 ? 659  ARG   B CD    1 
ATOM   13480 N  NE    . ARG   B  1 661  ? 22.369  12.842  75.541  1.00 24.02 ? 659  ARG   B NE    1 
ATOM   13481 C  CZ    . ARG   B  1 661  ? 22.521  12.723  74.231  1.00 27.25 ? 659  ARG   B CZ    1 
ATOM   13482 N  NH1   . ARG   B  1 661  ? 21.544  13.022  73.394  1.00 27.66 ? 659  ARG   B NH1   1 
ATOM   13483 N  NH2   . ARG   B  1 661  ? 23.670  12.255  73.751  1.00 25.44 ? 659  ARG   B NH2   1 
ATOM   13484 N  N     . GLU   B  1 662  ? 22.265  18.822  75.569  1.00 19.10 ? 660  GLU   B N     1 
ATOM   13485 C  CA    . GLU   B  1 662  ? 23.156  19.787  74.932  1.00 19.64 ? 660  GLU   B CA    1 
ATOM   13486 C  C     . GLU   B  1 662  ? 23.435  20.980  75.831  1.00 17.28 ? 660  GLU   B C     1 
ATOM   13487 O  O     . GLU   B  1 662  ? 24.552  21.513  75.840  1.00 19.34 ? 660  GLU   B O     1 
ATOM   13488 C  CB    . GLU   B  1 662  ? 22.566  20.270  73.607  1.00 22.09 ? 660  GLU   B CB    1 
ATOM   13489 C  CG    . GLU   B  1 662  ? 23.368  21.407  72.989  1.00 18.99 ? 660  GLU   B CG    1 
ATOM   13490 C  CD    . GLU   B  1 662  ? 22.806  21.873  71.654  1.00 19.70 ? 660  GLU   B CD    1 
ATOM   13491 O  OE1   . GLU   B  1 662  ? 21.589  22.097  71.554  1.00 19.22 ? 660  GLU   B OE1   1 
ATOM   13492 O  OE2   . GLU   B  1 662  ? 23.598  22.030  70.716  1.00 19.77 ? 660  GLU   B OE2   1 
ATOM   13493 N  N     . ALA   B  1 663  ? 22.426  21.426  76.574  1.00 18.07 ? 661  ALA   B N     1 
ATOM   13494 C  CA    . ALA   B  1 663  ? 22.513  22.649  77.351  1.00 18.10 ? 661  ALA   B CA    1 
ATOM   13495 C  C     . ALA   B  1 663  ? 22.723  22.387  78.834  1.00 18.41 ? 661  ALA   B C     1 
ATOM   13496 O  O     . ALA   B  1 663  ? 22.920  23.341  79.591  1.00 20.02 ? 661  ALA   B O     1 
ATOM   13497 C  CB    . ALA   B  1 663  ? 21.249  23.493  77.151  1.00 18.84 ? 661  ALA   B CB    1 
ATOM   13498 N  N     . GLY   B  1 664  ? 22.677  21.129  79.255  1.00 19.44 ? 662  GLY   B N     1 
ATOM   13499 C  CA    . GLY   B  1 664  ? 22.877  20.795  80.649  1.00 20.21 ? 662  GLY   B CA    1 
ATOM   13500 C  C     . GLY   B  1 664  ? 21.730  21.173  81.554  1.00 20.01 ? 662  GLY   B C     1 
ATOM   13501 O  O     . GLY   B  1 664  ? 21.949  21.441  82.740  1.00 22.74 ? 662  GLY   B O     1 
ATOM   13502 N  N     . LYS   B  1 665  ? 20.511  21.223  81.027  1.00 18.51 ? 663  LYS   B N     1 
ATOM   13503 C  CA    . LYS   B  1 665  ? 19.366  21.649  81.811  1.00 19.56 ? 663  LYS   B CA    1 
ATOM   13504 C  C     . LYS   B  1 665  ? 18.688  20.455  82.463  1.00 20.87 ? 663  LYS   B C     1 
ATOM   13505 O  O     . LYS   B  1 665  ? 18.745  19.330  81.959  1.00 20.96 ? 663  LYS   B O     1 
ATOM   13506 C  CB    . LYS   B  1 665  ? 18.348  22.397  80.947  1.00 19.69 ? 663  LYS   B CB    1 
ATOM   13507 C  CG    . LYS   B  1 665  ? 18.901  23.652  80.340  1.00 22.94 ? 663  LYS   B CG    1 
ATOM   13508 C  CD    . LYS   B  1 665  ? 17.836  24.706  80.180  1.00 25.65 ? 663  LYS   B CD    1 
ATOM   13509 C  CE    . LYS   B  1 665  ? 18.489  26.053  79.933  1.00 25.65 ? 663  LYS   B CE    1 
ATOM   13510 N  NZ    . LYS   B  1 665  ? 17.484  27.144  79.831  1.00 25.24 ? 663  LYS   B NZ    1 
ATOM   13511 N  N     . SER   B  1 666  ? 18.047  20.720  83.595  1.00 19.20 ? 664  SER   B N     1 
ATOM   13512 C  CA    . SER   B  1 666  ? 17.149  19.756  84.205  1.00 21.26 ? 664  SER   B CA    1 
ATOM   13513 C  C     . SER   B  1 666  ? 15.866  19.655  83.386  1.00 21.96 ? 664  SER   B C     1 
ATOM   13514 O  O     . SER   B  1 666  ? 15.540  20.535  82.582  1.00 21.25 ? 664  SER   B O     1 
ATOM   13515 C  CB    . SER   B  1 666  ? 16.810  20.182  85.625  1.00 25.28 ? 664  SER   B CB    1 
ATOM   13516 O  OG    . SER   B  1 666  ? 15.977  21.330  85.579  1.00 24.29 ? 664  SER   B OG    1 
ATOM   13517 N  N     . ALA   B  1 667  ? 15.121  18.571  83.612  1.00 20.13 ? 665  ALA   B N     1 
ATOM   13518 C  CA    . ALA   B  1 667  ? 13.888  18.361  82.864  1.00 19.32 ? 665  ALA   B CA    1 
ATOM   13519 C  C     . ALA   B  1 667  ? 12.912  19.503  83.080  1.00 18.36 ? 665  ALA   B C     1 
ATOM   13520 O  O     . ALA   B  1 667  ? 12.308  20.006  82.124  1.00 18.55 ? 665  ALA   B O     1 
ATOM   13521 C  CB    . ALA   B  1 667  ? 13.251  17.033  83.270  1.00 21.68 ? 665  ALA   B CB    1 
ATOM   13522 N  N     . LEU   B  1 668  ? 12.759  19.937  84.333  1.00 19.80 ? 666  LEU   B N     1 
ATOM   13523 C  CA    . LEU   B  1 668  ? 11.808  21.000  84.633  1.00 22.63 ? 666  LEU   B CA    1 
ATOM   13524 C  C     . LEU   B  1 668  ? 12.185  22.283  83.911  1.00 18.92 ? 666  LEU   B C     1 
ATOM   13525 O  O     . LEU   B  1 668  ? 11.325  22.974  83.354  1.00 18.24 ? 666  LEU   B O     1 
ATOM   13526 C  CB    . LEU   B  1 668  ? 11.753  21.227  86.141  1.00 27.24 ? 666  LEU   B CB    1 
ATOM   13527 C  CG    . LEU   B  1 668  ? 10.457  21.808  86.687  1.00 34.75 ? 666  LEU   B CG    1 
ATOM   13528 C  CD1   . LEU   B  1 668  ? 9.297   20.854  86.428  1.00 30.04 ? 666  LEU   B CD1   1 
ATOM   13529 C  CD2   . LEU   B  1 668  ? 10.624  22.078  88.174  1.00 41.11 ? 666  LEU   B CD2   1 
ATOM   13530 N  N     . ASN   B  1 669  ? 13.475  22.600  83.881  1.00 18.76 ? 667  ASN   B N     1 
ATOM   13531 C  CA    . ASN   B  1 669  ? 13.889  23.810  83.186  1.00 18.07 ? 667  ASN   B CA    1 
ATOM   13532 C  C     . ASN   B  1 669  ? 13.798  23.640  81.681  1.00 18.62 ? 667  ASN   B C     1 
ATOM   13533 O  O     . ASN   B  1 669  ? 13.544  24.615  80.962  1.00 21.80 ? 667  ASN   B O     1 
ATOM   13534 C  CB    . ASN   B  1 669  ? 15.304  24.191  83.603  1.00 20.87 ? 667  ASN   B CB    1 
ATOM   13535 C  CG    . ASN   B  1 669  ? 15.373  24.615  85.064  1.00 25.81 ? 667  ASN   B CG    1 
ATOM   13536 O  OD1   . ASN   B  1 669  ? 16.195  24.120  85.828  1.00 27.30 ? 667  ASN   B OD1   1 
ATOM   13537 N  ND2   . ASN   B  1 669  ? 14.490  25.521  85.453  1.00 29.07 ? 667  ASN   B ND2   1 
ATOM   13538 N  N     . ALA   B  1 670  ? 13.992  22.420  81.178  1.00 16.45 ? 668  ALA   B N     1 
ATOM   13539 C  CA    . ALA   B  1 670  ? 13.812  22.220  79.743  1.00 18.07 ? 668  ALA   B CA    1 
ATOM   13540 C  C     . ALA   B  1 670  ? 12.350  22.380  79.345  1.00 17.30 ? 668  ALA   B C     1 
ATOM   13541 O  O     . ALA   B  1 670  ? 12.054  22.882  78.253  1.00 17.17 ? 668  ALA   B O     1 
ATOM   13542 C  CB    . ALA   B  1 670  ? 14.346  20.852  79.314  1.00 16.66 ? 668  ALA   B CB    1 
ATOM   13543 N  N     . ILE   B  1 671  ? 11.420  21.935  80.204  1.00 15.88 ? 669  ILE   B N     1 
ATOM   13544 C  CA    . ILE   B  1 671  ? 10.000  22.165  79.949  1.00 18.44 ? 669  ILE   B CA    1 
ATOM   13545 C  C     . ILE   B  1 671  ? 9.709   23.658  79.911  1.00 16.73 ? 669  ILE   B C     1 
ATOM   13546 O  O     . ILE   B  1 671  ? 9.044   24.159  78.997  1.00 17.79 ? 669  ILE   B O     1 
ATOM   13547 C  CB    . ILE   B  1 671  ? 9.140   21.458  81.012  1.00 16.60 ? 669  ILE   B CB    1 
ATOM   13548 C  CG1   . ILE   B  1 671  ? 9.240   19.942  80.838  1.00 17.03 ? 669  ILE   B CG1   1 
ATOM   13549 C  CG2   . ILE   B  1 671  ? 7.690   21.958  80.934  1.00 17.25 ? 669  ILE   B CG2   1 
ATOM   13550 C  CD1   . ILE   B  1 671  ? 8.760   19.147  82.019  1.00 22.27 ? 669  ILE   B CD1   1 
ATOM   13551 N  N     . ALA   B  1 672  ? 10.205  24.390  80.914  1.00 17.66 ? 670  ALA   B N     1 
ATOM   13552 C  CA    . ALA   B  1 672  ? 10.039  25.835  80.938  1.00 20.31 ? 670  ALA   B CA    1 
ATOM   13553 C  C     . ALA   B  1 672  ? 10.595  26.464  79.673  1.00 17.95 ? 670  ALA   B C     1 
ATOM   13554 O  O     . ALA   B  1 672  ? 10.021  27.413  79.131  1.00 21.65 ? 670  ALA   B O     1 
ATOM   13555 C  CB    . ALA   B  1 672  ? 10.742  26.421  82.167  1.00 20.37 ? 670  ALA   B CB    1 
ATOM   13556 N  N     . GLU   B  1 673  ? 11.726  25.957  79.197  1.00 17.67 ? 671  GLU   B N     1 
ATOM   13557 C  CA    . GLU   B  1 673  ? 12.330  26.526  78.004  1.00 16.47 ? 671  GLU   B CA    1 
ATOM   13558 C  C     . GLU   B  1 673  ? 11.445  26.322  76.781  1.00 17.80 ? 671  GLU   B C     1 
ATOM   13559 O  O     . GLU   B  1 673  ? 11.182  27.269  76.028  1.00 17.97 ? 671  GLU   B O     1 
ATOM   13560 C  CB    . GLU   B  1 673  ? 13.689  25.905  77.762  1.00 19.46 ? 671  GLU   B CB    1 
ATOM   13561 C  CG    . GLU   B  1 673  ? 14.243  26.332  76.439  1.00 21.28 ? 671  GLU   B CG    1 
ATOM   13562 C  CD    . GLU   B  1 673  ? 15.593  26.979  76.574  1.00 24.33 ? 671  GLU   B CD    1 
ATOM   13563 O  OE1   . GLU   B  1 673  ? 16.352  26.572  77.489  1.00 30.93 ? 671  GLU   B OE1   1 
ATOM   13564 O  OE2   . GLU   B  1 673  ? 15.895  27.876  75.756  1.00 18.64 ? 671  GLU   B OE2   1 
ATOM   13565 N  N     . VAL   B  1 674  ? 10.997  25.085  76.551  1.00 15.23 ? 672  VAL   B N     1 
ATOM   13566 C  CA    . VAL   B  1 674  ? 10.127  24.834  75.401  1.00 17.58 ? 672  VAL   B CA    1 
ATOM   13567 C  C     . VAL   B  1 674  ? 8.823   25.620  75.533  1.00 15.13 ? 672  VAL   B C     1 
ATOM   13568 O  O     . VAL   B  1 674  ? 8.331   26.207  74.560  1.00 14.84 ? 672  VAL   B O     1 
ATOM   13569 C  CB    . VAL   B  1 674  ? 9.866   23.325  75.233  1.00 14.70 ? 672  VAL   B CB    1 
ATOM   13570 C  CG1   . VAL   B  1 674  ? 9.013   23.068  74.007  1.00 15.70 ? 672  VAL   B CG1   1 
ATOM   13571 C  CG2   . VAL   B  1 674  ? 11.190  22.560  75.133  1.00 20.66 ? 672  VAL   B CG2   1 
ATOM   13572 N  N     . ARG   B  1 675  ? 8.241   25.648  76.734  1.00 14.97 ? 673  ARG   B N     1 
ATOM   13573 C  CA    . ARG   B  1 675  ? 7.034   26.445  76.918  1.00 16.20 ? 673  ARG   B CA    1 
ATOM   13574 C  C     . ARG   B  1 675  ? 7.285   27.901  76.568  1.00 17.22 ? 673  ARG   B C     1 
ATOM   13575 O  O     . ARG   B  1 675  ? 6.457   28.537  75.906  1.00 16.08 ? 673  ARG   B O     1 
ATOM   13576 C  CB    . ARG   B  1 675  ? 6.529   26.337  78.355  1.00 16.63 ? 673  ARG   B CB    1 
ATOM   13577 C  CG    . ARG   B  1 675  ? 5.947   24.978  78.696  1.00 15.87 ? 673  ARG   B CG    1 
ATOM   13578 C  CD    . ARG   B  1 675  ? 5.228   25.046  80.039  1.00 17.71 ? 673  ARG   B CD    1 
ATOM   13579 N  NE    . ARG   B  1 675  ? 4.163   26.041  79.982  1.00 16.51 ? 673  ARG   B NE    1 
ATOM   13580 C  CZ    . ARG   B  1 675  ? 3.549   26.553  81.042  1.00 19.18 ? 673  ARG   B CZ    1 
ATOM   13581 N  NH1   . ARG   B  1 675  ? 3.955   26.293  82.280  1.00 18.39 ? 673  ARG   B NH1   1 
ATOM   13582 N  NH2   . ARG   B  1 675  ? 2.513   27.360  80.857  1.00 17.38 ? 673  ARG   B NH2   1 
ATOM   13583 N  N     . GLU   B  1 676  ? 8.410   28.449  77.022  1.00 16.52 ? 674  GLU   B N     1 
ATOM   13584 C  CA    . GLU   B  1 676  ? 8.700   29.847  76.725  1.00 18.47 ? 674  GLU   B CA    1 
ATOM   13585 C  C     . GLU   B  1 676  ? 8.810   30.080  75.227  1.00 16.09 ? 674  GLU   B C     1 
ATOM   13586 O  O     . GLU   B  1 676  ? 8.280   31.071  74.718  1.00 14.85 ? 674  GLU   B O     1 
ATOM   13587 C  CB    . GLU   B  1 676  ? 9.976   30.306  77.424  1.00 17.47 ? 674  GLU   B CB    1 
ATOM   13588 C  CG    . GLU   B  1 676  ? 10.224  31.793  77.207  1.00 18.86 ? 674  GLU   B CG    1 
ATOM   13589 C  CD    . GLU   B  1 676  ? 11.468  32.312  77.919  1.00 30.93 ? 674  GLU   B CD    1 
ATOM   13590 O  OE1   . GLU   B  1 676  ? 12.244  31.494  78.463  1.00 32.82 ? 674  GLU   B OE1   1 
ATOM   13591 O  OE2   . GLU   B  1 676  ? 11.667  33.547  77.933  1.00 38.49 ? 674  GLU   B OE2   1 
ATOM   13592 N  N     . ALA   B  1 677  ? 9.490   29.180  74.501  1.00 14.54 ? 675  ALA   B N     1 
ATOM   13593 C  CA    . ALA   B  1 677  ? 9.522   29.277  73.039  1.00 16.13 ? 675  ALA   B CA    1 
ATOM   13594 C  C     . ALA   B  1 677  ? 8.115   29.260  72.443  1.00 17.05 ? 675  ALA   B C     1 
ATOM   13595 O  O     . ALA   B  1 677  ? 7.791   30.054  71.552  1.00 15.64 ? 675  ALA   B O     1 
ATOM   13596 C  CB    . ALA   B  1 677  ? 10.349  28.133  72.446  1.00 14.50 ? 675  ALA   B CB    1 
ATOM   13597 N  N     . ILE   B  1 678  ? 7.272   28.334  72.904  1.00 16.04 ? 676  ILE   B N     1 
ATOM   13598 C  CA    . ILE   B  1 678  ? 5.894   28.274  72.421  1.00 13.93 ? 676  ILE   B CA    1 
ATOM   13599 C  C     . ILE   B  1 678  ? 5.165   29.580  72.720  1.00 16.19 ? 676  ILE   B C     1 
ATOM   13600 O  O     . ILE   B  1 678  ? 4.429   30.103  71.878  1.00 15.69 ? 676  ILE   B O     1 
ATOM   13601 C  CB    . ILE   B  1 678  ? 5.168   27.071  73.045  1.00 16.54 ? 676  ILE   B CB    1 
ATOM   13602 C  CG1   . ILE   B  1 678  ? 5.716   25.755  72.502  1.00 16.63 ? 676  ILE   B CG1   1 
ATOM   13603 C  CG2   . ILE   B  1 678  ? 3.659   27.186  72.817  1.00 14.80 ? 676  ILE   B CG2   1 
ATOM   13604 C  CD1   . ILE   B  1 678  ? 5.573   24.586  73.482  1.00 18.37 ? 676  ILE   B CD1   1 
ATOM   13605 N  N     . ASP   B  1 679  ? 5.344   30.115  73.927  1.00 14.81 ? 677  ASP   B N     1 
ATOM   13606 C  CA    . ASP   B  1 679  ? 4.661   31.355  74.291  1.00 16.48 ? 677  ASP   B CA    1 
ATOM   13607 C  C     . ASP   B  1 679  ? 5.146   32.532  73.449  1.00 15.02 ? 677  ASP   B C     1 
ATOM   13608 O  O     . ASP   B  1 679  ? 4.336   33.364  73.031  1.00 15.60 ? 677  ASP   B O     1 
ATOM   13609 C  CB    . ASP   B  1 679  ? 4.857   31.664  75.776  1.00 15.65 ? 677  ASP   B CB    1 
ATOM   13610 C  CG    . ASP   B  1 679  ? 4.151   30.667  76.687  1.00 19.57 ? 677  ASP   B CG    1 
ATOM   13611 O  OD1   . ASP   B  1 679  ? 3.130   30.092  76.262  1.00 20.80 ? 677  ASP   B OD1   1 
ATOM   13612 O  OD2   . ASP   B  1 679  ? 4.636   30.464  77.824  1.00 21.06 ? 677  ASP   B OD2   1 
ATOM   13613 N  N     . PHE   B  1 680  ? 6.455   32.631  73.199  1.00 13.15 ? 678  PHE   B N     1 
ATOM   13614 C  CA    . PHE   B  1 680  ? 6.955   33.681  72.311  1.00 16.54 ? 678  PHE   B CA    1 
ATOM   13615 C  C     . PHE   B  1 680  ? 6.277   33.601  70.955  1.00 15.44 ? 678  PHE   B C     1 
ATOM   13616 O  O     . PHE   B  1 680  ? 5.818   34.609  70.410  1.00 14.77 ? 678  PHE   B O     1 
ATOM   13617 C  CB    . PHE   B  1 680  ? 8.472   33.552  72.106  1.00 12.26 ? 678  PHE   B CB    1 
ATOM   13618 C  CG    . PHE   B  1 680  ? 9.314   34.213  73.162  1.00 15.44 ? 678  PHE   B CG    1 
ATOM   13619 C  CD1   . PHE   B  1 680  ? 9.074   35.523  73.571  1.00 15.99 ? 678  PHE   B CD1   1 
ATOM   13620 C  CD2   . PHE   B  1 680  ? 10.373  33.519  73.728  1.00 14.23 ? 678  PHE   B CD2   1 
ATOM   13621 C  CE1   . PHE   B  1 680  ? 9.875   36.126  74.535  1.00 18.23 ? 678  PHE   B CE1   1 
ATOM   13622 C  CE2   . PHE   B  1 680  ? 11.186  34.110  74.679  1.00 16.03 ? 678  PHE   B CE2   1 
ATOM   13623 C  CZ    . PHE   B  1 680  ? 10.934  35.416  75.098  1.00 15.14 ? 678  PHE   B CZ    1 
ATOM   13624 N  N     . LEU   B  1 681  ? 6.248   32.402  70.375  1.00 14.31 ? 679  LEU   B N     1 
ATOM   13625 C  CA    . LEU   B  1 681  ? 5.640   32.225  69.063  1.00 12.69 ? 679  LEU   B CA    1 
ATOM   13626 C  C     . LEU   B  1 681  ? 4.194   32.705  69.061  1.00 14.76 ? 679  LEU   B C     1 
ATOM   13627 O  O     . LEU   B  1 681  ? 3.786   33.485  68.190  1.00 14.79 ? 679  LEU   B O     1 
ATOM   13628 C  CB    . LEU   B  1 681  ? 5.725   30.752  68.644  1.00 14.29 ? 679  LEU   B CB    1 
ATOM   13629 C  CG    . LEU   B  1 681  ? 7.138   30.258  68.328  1.00 16.28 ? 679  LEU   B CG    1 
ATOM   13630 C  CD1   . LEU   B  1 681  ? 7.186   28.732  68.371  1.00 16.00 ? 679  LEU   B CD1   1 
ATOM   13631 C  CD2   . LEU   B  1 681  ? 7.594   30.769  66.937  1.00 14.19 ? 679  LEU   B CD2   1 
ATOM   13632 N  N     . ARG   B  1 682  ? 3.402   32.247  70.031  1.00 13.45 ? 680  ARG   B N     1 
ATOM   13633 C  CA    . ARG   B  1 682  ? 1.987   32.598  70.035  1.00 15.29 ? 680  ARG   B CA    1 
ATOM   13634 C  C     . ARG   B  1 682  ? 1.769   34.044  70.439  1.00 15.44 ? 680  ARG   B C     1 
ATOM   13635 O  O     . ARG   B  1 682  ? 0.837   34.698  69.950  1.00 15.72 ? 680  ARG   B O     1 
ATOM   13636 C  CB    . ARG   B  1 682  ? 1.233   31.666  70.964  1.00 15.07 ? 680  ARG   B CB    1 
ATOM   13637 C  CG    . ARG   B  1 682  ? 1.145   30.265  70.399  1.00 13.63 ? 680  ARG   B CG    1 
ATOM   13638 C  CD    . ARG   B  1 682  ? 0.582   29.345  71.443  1.00 15.32 ? 680  ARG   B CD    1 
ATOM   13639 N  NE    . ARG   B  1 682  ? 0.323   28.013  70.921  1.00 16.33 ? 680  ARG   B NE    1 
ATOM   13640 C  CZ    . ARG   B  1 682  ? 0.092   26.961  71.691  1.00 17.39 ? 680  ARG   B CZ    1 
ATOM   13641 N  NH1   . ARG   B  1 682  ? 0.043   27.073  73.010  1.00 17.43 ? 680  ARG   B NH1   1 
ATOM   13642 N  NH2   . ARG   B  1 682  ? -0.063  25.768  71.125  1.00 17.22 ? 680  ARG   B NH2   1 
ATOM   13643 N  N     . TYR   B  1 683  ? 2.609   34.561  71.322  1.00 16.40 ? 681  TYR   B N     1 
ATOM   13644 C  CA    . TYR   B  1 683  ? 2.450   35.948  71.724  1.00 17.41 ? 681  TYR   B CA    1 
ATOM   13645 C  C     . TYR   B  1 683  ? 2.763   36.892  70.573  1.00 16.04 ? 681  TYR   B C     1 
ATOM   13646 O  O     . TYR   B  1 683  ? 1.982   37.801  70.281  1.00 15.60 ? 681  TYR   B O     1 
ATOM   13647 C  CB    . TYR   B  1 683  ? 3.335   36.243  72.918  1.00 13.76 ? 681  TYR   B CB    1 
ATOM   13648 C  CG    . TYR   B  1 683  ? 3.270   37.683  73.353  1.00 17.72 ? 681  TYR   B CG    1 
ATOM   13649 C  CD1   . TYR   B  1 683  ? 2.201   38.146  74.105  1.00 17.24 ? 681  TYR   B CD1   1 
ATOM   13650 C  CD2   . TYR   B  1 683  ? 4.276   38.582  73.005  1.00 14.33 ? 681  TYR   B CD2   1 
ATOM   13651 C  CE1   . TYR   B  1 683  ? 2.128   39.476  74.503  1.00 17.51 ? 681  TYR   B CE1   1 
ATOM   13652 C  CE2   . TYR   B  1 683  ? 4.214   39.914  73.400  1.00 16.24 ? 681  TYR   B CE2   1 
ATOM   13653 C  CZ    . TYR   B  1 683  ? 3.136   40.352  74.152  1.00 17.68 ? 681  TYR   B CZ    1 
ATOM   13654 O  OH    . TYR   B  1 683  ? 3.041   41.674  74.558  1.00 16.35 ? 681  TYR   B OH    1 
ATOM   13655 N  N     . TYR   B  1 684  ? 3.912   36.708  69.916  1.00 14.41 ? 682  TYR   B N     1 
ATOM   13656 C  CA    . TYR   B  1 684  ? 4.235   37.595  68.804  1.00 15.04 ? 682  TYR   B CA    1 
ATOM   13657 C  C     . TYR   B  1 684  ? 3.252   37.407  67.654  1.00 15.70 ? 682  TYR   B C     1 
ATOM   13658 O  O     . TYR   B  1 684  ? 2.972   38.355  66.924  1.00 15.86 ? 682  TYR   B O     1 
ATOM   13659 C  CB    . TYR   B  1 684  ? 5.676   37.366  68.338  1.00 15.03 ? 682  TYR   B CB    1 
ATOM   13660 C  CG    . TYR   B  1 684  ? 6.692   37.743  69.395  1.00 14.83 ? 682  TYR   B CG    1 
ATOM   13661 C  CD1   . TYR   B  1 684  ? 6.527   38.892  70.165  1.00 14.88 ? 682  TYR   B CD1   1 
ATOM   13662 C  CD2   . TYR   B  1 684  ? 7.807   36.953  69.623  1.00 17.15 ? 682  TYR   B CD2   1 
ATOM   13663 C  CE1   . TYR   B  1 684  ? 7.442   39.235  71.139  1.00 15.95 ? 682  TYR   B CE1   1 
ATOM   13664 C  CE2   . TYR   B  1 684  ? 8.726   37.287  70.592  1.00 14.68 ? 682  TYR   B CE2   1 
ATOM   13665 C  CZ    . TYR   B  1 684  ? 8.544   38.428  71.341  1.00 17.74 ? 682  TYR   B CZ    1 
ATOM   13666 O  OH    . TYR   B  1 684  ? 9.462   38.746  72.313  1.00 15.49 ? 682  TYR   B OH    1 
ATOM   13667 N  N     . ALA   B  1 685  ? 2.695   36.209  67.500  1.00 15.01 ? 683  ALA   B N     1 
ATOM   13668 C  CA    . ALA   B  1 685  ? 1.668   36.005  66.488  1.00 15.81 ? 683  ALA   B CA    1 
ATOM   13669 C  C     . ALA   B  1 685  ? 0.435   36.835  66.812  1.00 15.64 ? 683  ALA   B C     1 
ATOM   13670 O  O     . ALA   B  1 685  ? -0.095  37.557  65.958  1.00 15.66 ? 683  ALA   B O     1 
ATOM   13671 C  CB    . ALA   B  1 685  ? 1.318   34.522  66.400  1.00 12.97 ? 683  ALA   B CB    1 
ATOM   13672 N  N     . GLU   B  1 686  ? -0.017  36.770  68.059  1.00 15.15 ? 684  GLU   B N     1 
ATOM   13673 C  CA    . GLU   B  1 686  ? -1.188  37.554  68.426  1.00 15.64 ? 684  GLU   B CA    1 
ATOM   13674 C  C     . GLU   B  1 686  ? -0.888  39.042  68.366  1.00 15.35 ? 684  GLU   B C     1 
ATOM   13675 O  O     . GLU   B  1 686  ? -1.693  39.815  67.843  1.00 16.74 ? 684  GLU   B O     1 
ATOM   13676 C  CB    . GLU   B  1 686  ? -1.689  37.164  69.810  1.00 17.68 ? 684  GLU   B CB    1 
ATOM   13677 C  CG    . GLU   B  1 686  ? -2.780  38.118  70.343  1.00 19.08 ? 684  GLU   B CG    1 
ATOM   13678 C  CD    . GLU   B  1 686  ? -4.094  38.050  69.567  1.00 26.79 ? 684  GLU   B CD    1 
ATOM   13679 O  OE1   . GLU   B  1 686  ? -4.258  37.148  68.711  1.00 23.29 ? 684  GLU   B OE1   1 
ATOM   13680 O  OE2   . GLU   B  1 686  ? -4.976  38.908  69.826  1.00 24.58 ? 684  GLU   B OE2   1 
ATOM   13681 N  N     . GLN   B  1 687  ? 0.279   39.464  68.861  1.00 15.69 ? 685  GLN   B N     1 
ATOM   13682 C  CA    . GLN   B  1 687  ? 0.605   40.883  68.787  1.00 16.09 ? 685  GLN   B CA    1 
ATOM   13683 C  C     . GLN   B  1 687  ? 0.618   41.363  67.347  1.00 16.77 ? 685  GLN   B C     1 
ATOM   13684 O  O     . GLN   B  1 687  ? 0.173   42.480  67.056  1.00 17.40 ? 685  GLN   B O     1 
ATOM   13685 C  CB    . GLN   B  1 687  ? 1.942   41.167  69.467  1.00 19.23 ? 685  GLN   B CB    1 
ATOM   13686 C  CG    . GLN   B  1 687  ? 1.854   40.982  70.971  1.00 17.18 ? 685  GLN   B CG    1 
ATOM   13687 C  CD    . GLN   B  1 687  ? 0.819   41.893  71.601  1.00 18.39 ? 685  GLN   B CD    1 
ATOM   13688 O  OE1   . GLN   B  1 687  ? 0.850   43.110  71.412  1.00 19.60 ? 685  GLN   B OE1   1 
ATOM   13689 N  NE2   . GLN   B  1 687  ? -0.115  41.305  72.339  1.00 21.31 ? 685  GLN   B NE2   1 
ATOM   13690 N  N     . THR   B  1 688  ? 1.087   40.520  66.425  1.00 15.32 ? 686  THR   B N     1 
ATOM   13691 C  CA    . THR   B  1 688  ? 1.023   40.866  65.007  1.00 14.49 ? 686  THR   B CA    1 
ATOM   13692 C  C     . THR   B  1 688  ? -0.419  41.019  64.541  1.00 16.17 ? 686  THR   B C     1 
ATOM   13693 O  O     . THR   B  1 688  ? -0.777  42.015  63.903  1.00 18.20 ? 686  THR   B O     1 
ATOM   13694 C  CB    . THR   B  1 688  ? 1.744   39.793  64.192  1.00 17.45 ? 686  THR   B CB    1 
ATOM   13695 O  OG1   . THR   B  1 688  ? 3.135   39.845  64.518  1.00 17.33 ? 686  THR   B OG1   1 
ATOM   13696 C  CG2   . THR   B  1 688  ? 1.546   40.006  62.690  1.00 16.40 ? 686  THR   B CG2   1 
ATOM   13697 N  N     . ARG   B  1 689  ? -1.259  40.028  64.834  1.00 15.22 ? 687  ARG   B N     1 
ATOM   13698 C  CA    . ARG   B  1 689  ? -2.669  40.119  64.453  1.00 18.10 ? 687  ARG   B CA    1 
ATOM   13699 C  C     . ARG   B  1 689  ? -3.344  41.365  65.025  1.00 20.26 ? 687  ARG   B C     1 
ATOM   13700 O  O     . ARG   B  1 689  ? -4.293  41.886  64.426  1.00 18.98 ? 687  ARG   B O     1 
ATOM   13701 C  CB    . ARG   B  1 689  ? -3.413  38.868  64.909  1.00 17.17 ? 687  ARG   B CB    1 
ATOM   13702 C  CG    . ARG   B  1 689  ? -3.132  37.641  64.041  1.00 18.45 ? 687  ARG   B CG    1 
ATOM   13703 C  CD    . ARG   B  1 689  ? -4.061  36.511  64.428  1.00 20.15 ? 687  ARG   B CD    1 
ATOM   13704 N  NE    . ARG   B  1 689  ? -3.860  36.103  65.813  1.00 18.94 ? 687  ARG   B NE    1 
ATOM   13705 C  CZ    . ARG   B  1 689  ? -3.078  35.099  66.188  1.00 22.54 ? 687  ARG   B CZ    1 
ATOM   13706 N  NH1   . ARG   B  1 689  ? -2.413  34.377  65.300  1.00 19.76 ? 687  ARG   B NH1   1 
ATOM   13707 N  NH2   . ARG   B  1 689  ? -2.967  34.809  67.485  1.00 18.98 ? 687  ARG   B NH2   1 
ATOM   13708 N  N     . ARG   B  1 690  ? -2.880  41.858  66.176  1.00 17.04 ? 688  ARG   B N     1 
ATOM   13709 C  CA    . ARG   B  1 690  ? -3.467  43.066  66.745  1.00 17.39 ? 688  ARG   B CA    1 
ATOM   13710 C  C     . ARG   B  1 690  ? -2.953  44.353  66.100  1.00 17.90 ? 688  ARG   B C     1 
ATOM   13711 O  O     . ARG   B  1 690  ? -3.606  45.396  66.242  1.00 18.94 ? 688  ARG   B O     1 
ATOM   13712 C  CB    . ARG   B  1 690  ? -3.185  43.127  68.251  1.00 18.01 ? 688  ARG   B CB    1 
ATOM   13713 C  CG    . ARG   B  1 690  ? -3.813  42.000  69.046  1.00 18.46 ? 688  ARG   B CG    1 
ATOM   13714 C  CD    . ARG   B  1 690  ? -5.333  42.191  69.207  1.00 22.52 ? 688  ARG   B CD    1 
ATOM   13715 N  NE    . ARG   B  1 690  ? -5.615  43.446  69.901  1.00 24.54 ? 688  ARG   B NE    1 
ATOM   13716 C  CZ    . ARG   B  1 690  ? -6.205  44.492  69.339  1.00 26.61 ? 688  ARG   B CZ    1 
ATOM   13717 N  NH1   . ARG   B  1 690  ? -6.680  44.436  68.105  1.00 23.62 ? 688  ARG   B NH1   1 
ATOM   13718 N  NH2   . ARG   B  1 690  ? -6.337  45.617  70.037  1.00 23.98 ? 688  ARG   B NH2   1 
ATOM   13719 N  N     . THR   B  1 691  ? -1.796  44.322  65.417  1.00 17.56 ? 689  THR   B N     1 
ATOM   13720 C  CA    . THR   B  1 691  ? -1.171  45.614  65.114  1.00 19.34 ? 689  THR   B CA    1 
ATOM   13721 C  C     . THR   B  1 691  ? -0.721  45.810  63.673  1.00 19.40 ? 689  THR   B C     1 
ATOM   13722 O  O     . THR   B  1 691  ? -0.854  46.916  63.155  1.00 25.23 ? 689  THR   B O     1 
ATOM   13723 C  CB    . THR   B  1 691  ? 0.049   45.852  66.015  1.00 19.67 ? 689  THR   B CB    1 
ATOM   13724 O  OG1   . THR   B  1 691  ? 1.019   44.812  65.809  1.00 17.28 ? 689  THR   B OG1   1 
ATOM   13725 C  CG2   . THR   B  1 691  ? -0.368  45.882  67.484  1.00 18.89 ? 689  THR   B CG2   1 
ATOM   13726 N  N     . LEU   B  1 692  ? -0.141  44.803  63.030  1.00 18.74 ? 690  LEU   B N     1 
ATOM   13727 C  CA    . LEU   B  1 692  ? 0.659   45.079  61.840  1.00 18.75 ? 690  LEU   B CA    1 
ATOM   13728 C  C     . LEU   B  1 692  ? -0.187  45.246  60.581  1.00 20.28 ? 690  LEU   B C     1 
ATOM   13729 O  O     . LEU   B  1 692  ? -1.047  44.418  60.271  1.00 22.77 ? 690  LEU   B O     1 
ATOM   13730 C  CB    . LEU   B  1 692  ? 1.701   43.981  61.637  1.00 18.58 ? 690  LEU   B CB    1 
ATOM   13731 C  CG    . LEU   B  1 692  ? 2.757   43.955  62.747  1.00 19.43 ? 690  LEU   B CG    1 
ATOM   13732 C  CD1   . LEU   B  1 692  ? 3.905   43.038  62.363  1.00 17.73 ? 690  LEU   B CD1   1 
ATOM   13733 C  CD2   . LEU   B  1 692  ? 3.254   45.360  63.061  1.00 19.16 ? 690  LEU   B CD2   1 
ATOM   13734 N  N     . GLY   B  1 693  ? 0.074   46.326  59.856  1.00 22.73 ? 691  GLY   B N     1 
ATOM   13735 C  CA    . GLY   B  1 693  ? -0.587  46.603  58.605  1.00 24.19 ? 691  GLY   B CA    1 
ATOM   13736 C  C     . GLY   B  1 693  ? 0.424   46.980  57.542  1.00 24.76 ? 691  GLY   B C     1 
ATOM   13737 O  O     . GLY   B  1 693  ? 1.635   47.002  57.785  1.00 24.63 ? 691  GLY   B O     1 
ATOM   13738 N  N     . PRO   B  1 694  ? -0.055  47.306  56.339  1.00 29.13 ? 692  PRO   B N     1 
ATOM   13739 C  CA    . PRO   B  1 694  ? 0.885   47.560  55.234  1.00 29.24 ? 692  PRO   B CA    1 
ATOM   13740 C  C     . PRO   B  1 694  ? 1.817   48.735  55.485  1.00 29.21 ? 692  PRO   B C     1 
ATOM   13741 O  O     . PRO   B  1 694  ? 2.943   48.736  54.972  1.00 31.59 ? 692  PRO   B O     1 
ATOM   13742 C  CB    . PRO   B  1 694  ? -0.039  47.798  54.030  1.00 34.12 ? 692  PRO   B CB    1 
ATOM   13743 C  CG    . PRO   B  1 694  ? -1.377  48.097  54.598  1.00 34.39 ? 692  PRO   B CG    1 
ATOM   13744 C  CD    . PRO   B  1 694  ? -1.464  47.414  55.925  1.00 30.86 ? 692  PRO   B CD    1 
ATOM   13745 N  N     . GLY   B  1 695  ? 1.410   49.719  56.286  1.00 26.49 ? 693  GLY   B N     1 
ATOM   13746 C  CA    . GLY   B  1 695  ? 2.288   50.837  56.560  1.00 26.06 ? 693  GLY   B CA    1 
ATOM   13747 C  C     . GLY   B  1 695  ? 3.405   50.547  57.540  1.00 29.08 ? 693  GLY   B C     1 
ATOM   13748 O  O     . GLY   B  1 695  ? 4.230   51.432  57.784  1.00 25.44 ? 693  GLY   B O     1 
ATOM   13749 N  N     . HIS   B  1 696  ? 3.437   49.355  58.132  1.00 24.53 ? 694  HIS   B N     1 
ATOM   13750 C  CA    . HIS   B  1 696  ? 4.487   49.009  59.086  1.00 22.11 ? 694  HIS   B CA    1 
ATOM   13751 C  C     . HIS   B  1 696  ? 5.528   48.148  58.377  1.00 23.92 ? 694  HIS   B C     1 
ATOM   13752 O  O     . HIS   B  1 696  ? 5.627   46.935  58.558  1.00 25.51 ? 694  HIS   B O     1 
ATOM   13753 C  CB    . HIS   B  1 696  ? 3.886   48.318  60.304  1.00 21.89 ? 694  HIS   B CB    1 
ATOM   13754 C  CG    . HIS   B  1 696  ? 2.761   49.092  60.914  1.00 20.71 ? 694  HIS   B CG    1 
ATOM   13755 N  ND1   . HIS   B  1 696  ? 1.469   48.617  60.965  1.00 21.65 ? 694  HIS   B ND1   1 
ATOM   13756 C  CD2   . HIS   B  1 696  ? 2.726   50.334  61.450  1.00 23.58 ? 694  HIS   B CD2   1 
ATOM   13757 C  CE1   . HIS   B  1 696  ? 0.689   49.524  61.524  1.00 21.59 ? 694  HIS   B CE1   1 
ATOM   13758 N  NE2   . HIS   B  1 696  ? 1.427   50.575  61.829  1.00 22.42 ? 694  HIS   B NE2   1 
ATOM   13759 N  N     . GLY   B  1 697  ? 6.309   48.824  57.543  1.00 27.47 ? 695  GLY   B N     1 
ATOM   13760 C  CA    . GLY   B  1 697  ? 7.247   48.158  56.674  1.00 25.45 ? 695  GLY   B CA    1 
ATOM   13761 C  C     . GLY   B  1 697  ? 8.369   47.498  57.442  1.00 23.22 ? 695  GLY   B C     1 
ATOM   13762 O  O     . GLY   B  1 697  ? 8.780   47.952  58.511  1.00 22.50 ? 695  GLY   B O     1 
ATOM   13763 N  N     . PRO   B  1 698  ? 8.902   46.415  56.902  1.00 24.99 ? 696  PRO   B N     1 
ATOM   13764 C  CA    . PRO   B  1 698  ? 9.973   45.707  57.599  1.00 21.93 ? 696  PRO   B CA    1 
ATOM   13765 C  C     . PRO   B  1 698  ? 11.284  46.456  57.479  1.00 21.12 ? 696  PRO   B C     1 
ATOM   13766 O  O     . PRO   B  1 698  ? 11.458  47.338  56.641  1.00 20.60 ? 696  PRO   B O     1 
ATOM   13767 C  CB    . PRO   B  1 698  ? 10.044  44.367  56.861  1.00 26.61 ? 696  PRO   B CB    1 
ATOM   13768 C  CG    . PRO   B  1 698  ? 9.688   44.749  55.461  1.00 30.49 ? 696  PRO   B CG    1 
ATOM   13769 C  CD    . PRO   B  1 698  ? 8.570   45.777  55.618  1.00 27.16 ? 696  PRO   B CD    1 
ATOM   13770 N  N     . LEU   B  1 699  ? 12.211  46.088  58.357  1.00 19.22 ? 697  LEU   B N     1 
ATOM   13771 C  CA    . LEU   B  1 699  ? 13.565  46.612  58.251  1.00 18.49 ? 697  LEU   B CA    1 
ATOM   13772 C  C     . LEU   B  1 699  ? 14.320  45.974  57.099  1.00 20.44 ? 697  LEU   B C     1 
ATOM   13773 O  O     . LEU   B  1 699  ? 15.064  46.657  56.391  1.00 20.94 ? 697  LEU   B O     1 
ATOM   13774 C  CB    . LEU   B  1 699  ? 14.326  46.369  59.551  1.00 20.11 ? 697  LEU   B CB    1 
ATOM   13775 C  CG    . LEU   B  1 699  ? 13.759  47.011  60.814  1.00 21.68 ? 697  LEU   B CG    1 
ATOM   13776 C  CD1   . LEU   B  1 699  ? 14.636  46.633  62.007  1.00 22.30 ? 697  LEU   B CD1   1 
ATOM   13777 C  CD2   . LEU   B  1 699  ? 13.695  48.520  60.643  1.00 22.50 ? 697  LEU   B CD2   1 
ATOM   13778 N  N     . GLY   B  1 700  ? 14.151  44.668  56.906  1.00 20.17 ? 698  GLY   B N     1 
ATOM   13779 C  CA    . GLY   B  1 700  ? 15.014  43.911  56.030  1.00 20.22 ? 698  GLY   B CA    1 
ATOM   13780 C  C     . GLY   B  1 700  ? 15.702  42.836  56.840  1.00 21.32 ? 698  GLY   B C     1 
ATOM   13781 O  O     . GLY   B  1 700  ? 15.275  42.520  57.956  1.00 18.70 ? 698  GLY   B O     1 
ATOM   13782 N  N     . PRO   B  1 701  ? 16.793  42.275  56.316  1.00 20.12 ? 699  PRO   B N     1 
ATOM   13783 C  CA    . PRO   B  1 701  ? 17.453  41.153  56.996  1.00 20.14 ? 699  PRO   B CA    1 
ATOM   13784 C  C     . PRO   B  1 701  ? 17.853  41.507  58.419  1.00 22.18 ? 699  PRO   B C     1 
ATOM   13785 O  O     . PRO   B  1 701  ? 18.505  42.517  58.673  1.00 18.46 ? 699  PRO   B O     1 
ATOM   13786 C  CB    . PRO   B  1 701  ? 18.682  40.883  56.123  1.00 20.13 ? 699  PRO   B CB    1 
ATOM   13787 C  CG    . PRO   B  1 701  ? 18.276  41.376  54.766  1.00 21.21 ? 699  PRO   B CG    1 
ATOM   13788 C  CD    . PRO   B  1 701  ? 17.459  42.609  55.044  1.00 19.55 ? 699  PRO   B CD    1 
ATOM   13789 N  N     . ILE   B  1 702  ? 17.458  40.659  59.352  1.00 20.16 ? 700  ILE   B N     1 
ATOM   13790 C  CA    . ILE   B  1 702  ? 17.767  40.862  60.756  1.00 17.52 ? 700  ILE   B CA    1 
ATOM   13791 C  C     . ILE   B  1 702  ? 18.678  39.739  61.203  1.00 17.34 ? 700  ILE   B C     1 
ATOM   13792 O  O     . ILE   B  1 702  ? 18.399  38.561  60.962  1.00 17.78 ? 700  ILE   B O     1 
ATOM   13793 C  CB    . ILE   B  1 702  ? 16.489  40.937  61.610  1.00 20.49 ? 700  ILE   B CB    1 
ATOM   13794 C  CG1   . ILE   B  1 702  ? 15.756  42.247  61.287  1.00 18.26 ? 700  ILE   B CG1   1 
ATOM   13795 C  CG2   . ILE   B  1 702  ? 16.816  40.800  63.106  1.00 22.30 ? 700  ILE   B CG2   1 
ATOM   13796 C  CD1   . ILE   B  1 702  ? 14.522  42.483  62.130  1.00 23.68 ? 700  ILE   B CD1   1 
ATOM   13797 N  N     . VAL   B  1 703  ? 19.763  40.107  61.856  1.00 16.70 ? 701  VAL   B N     1 
ATOM   13798 C  CA    . VAL   B  1 703  ? 20.691  39.140  62.413  1.00 17.91 ? 701  VAL   B CA    1 
ATOM   13799 C  C     . VAL   B  1 703  ? 20.271  38.899  63.854  1.00 18.14 ? 701  VAL   B C     1 
ATOM   13800 O  O     . VAL   B  1 703  ? 20.176  39.844  64.642  1.00 17.30 ? 701  VAL   B O     1 
ATOM   13801 C  CB    . VAL   B  1 703  ? 22.128  39.659  62.321  1.00 16.19 ? 701  VAL   B CB    1 
ATOM   13802 C  CG1   . VAL   B  1 703  ? 23.070  38.763  63.113  1.00 18.70 ? 701  VAL   B CG1   1 
ATOM   13803 C  CG2   . VAL   B  1 703  ? 22.554  39.728  60.859  1.00 16.21 ? 701  VAL   B CG2   1 
ATOM   13804 N  N     . CYS   B  1 704  ? 20.000  37.644  64.195  1.00 15.52 ? 702  CYS   B N     1 
ATOM   13805 C  CA    . CYS   B  1 704  ? 19.517  37.276  65.523  1.00 15.98 ? 702  CYS   B CA    1 
ATOM   13806 C  C     . CYS   B  1 704  ? 20.613  36.438  66.150  1.00 16.02 ? 702  CYS   B C     1 
ATOM   13807 O  O     . CYS   B  1 704  ? 20.919  35.350  65.657  1.00 16.29 ? 702  CYS   B O     1 
ATOM   13808 C  CB    . CYS   B  1 704  ? 18.204  36.496  65.459  1.00 16.14 ? 702  CYS   B CB    1 
ATOM   13809 S  SG    . CYS   B  1 704  ? 16.807  37.416  64.801  1.00 18.44 ? 702  CYS   B SG    1 
ATOM   13810 N  N     . ILE   B  1 705  ? 21.223  36.960  67.208  1.00 17.03 ? 703  ILE   B N     1 
ATOM   13811 C  CA    . ILE   B  1 705  ? 22.344  36.302  67.881  1.00 14.36 ? 703  ILE   B CA    1 
ATOM   13812 C  C     . ILE   B  1 705  ? 21.856  35.925  69.267  1.00 16.38 ? 703  ILE   B C     1 
ATOM   13813 O  O     . ILE   B  1 705  ? 21.396  36.790  70.023  1.00 18.74 ? 703  ILE   B O     1 
ATOM   13814 C  CB    . ILE   B  1 705  ? 23.578  37.208  67.958  1.00 15.21 ? 703  ILE   B CB    1 
ATOM   13815 C  CG1   . ILE   B  1 705  ? 24.082  37.519  66.543  1.00 18.90 ? 703  ILE   B CG1   1 
ATOM   13816 C  CG2   . ILE   B  1 705  ? 24.688  36.537  68.787  1.00 18.82 ? 703  ILE   B CG2   1 
ATOM   13817 C  CD1   . ILE   B  1 705  ? 25.191  38.558  66.506  1.00 23.50 ? 703  ILE   B CD1   1 
ATOM   13818 N  N     . SER   B  1 706  ? 21.908  34.644  69.581  1.00 17.41 ? 704  SER   B N     1 
ATOM   13819 C  CA    . SER   B  1 706  ? 21.249  34.131  70.766  1.00 17.37 ? 704  SER   B CA    1 
ATOM   13820 C  C     . SER   B  1 706  ? 22.262  33.466  71.688  1.00 16.96 ? 704  SER   B C     1 
ATOM   13821 O  O     . SER   B  1 706  ? 23.354  33.073  71.258  1.00 16.34 ? 704  SER   B O     1 
ATOM   13822 C  CB    . SER   B  1 706  ? 20.144  33.136  70.389  1.00 18.50 ? 704  SER   B CB    1 
ATOM   13823 O  OG    . SER   B  1 706  ? 20.649  32.122  69.547  1.00 16.25 ? 704  SER   B OG    1 
ATOM   13824 N  N     . PRO   B  1 707  ? 21.928  33.326  72.963  1.00 20.16 ? 705  PRO   B N     1 
ATOM   13825 C  CA    . PRO   B  1 707  ? 22.874  32.790  73.938  1.00 20.83 ? 705  PRO   B CA    1 
ATOM   13826 C  C     . PRO   B  1 707  ? 22.703  31.288  74.142  1.00 19.90 ? 705  PRO   B C     1 
ATOM   13827 O  O     . PRO   B  1 707  ? 21.775  30.658  73.632  1.00 20.47 ? 705  PRO   B O     1 
ATOM   13828 C  CB    . PRO   B  1 707  ? 22.508  33.567  75.206  1.00 19.24 ? 705  PRO   B CB    1 
ATOM   13829 C  CG    . PRO   B  1 707  ? 21.055  33.727  75.120  1.00 18.70 ? 705  PRO   B CG    1 
ATOM   13830 C  CD    . PRO   B  1 707  ? 20.721  33.860  73.621  1.00 22.03 ? 705  PRO   B CD    1 
ATOM   13831 N  N     . TRP   B  1 708  ? 23.635  30.718  74.895  1.00 18.67 ? 706  TRP   B N     1 
ATOM   13832 C  CA    . TRP   B  1 708  ? 23.602  29.289  75.177  1.00 19.06 ? 706  TRP   B CA    1 
ATOM   13833 C  C     . TRP   B  1 708  ? 22.746  28.947  76.385  1.00 18.08 ? 706  TRP   B C     1 
ATOM   13834 O  O     . TRP   B  1 708  ? 22.483  27.764  76.618  1.00 19.21 ? 706  TRP   B O     1 
ATOM   13835 C  CB    . TRP   B  1 708  ? 25.023  28.765  75.412  1.00 16.96 ? 706  TRP   B CB    1 
ATOM   13836 C  CG    . TRP   B  1 708  ? 25.776  29.632  76.386  1.00 20.04 ? 706  TRP   B CG    1 
ATOM   13837 C  CD1   . TRP   B  1 708  ? 26.671  30.622  76.084  1.00 23.32 ? 706  TRP   B CD1   1 
ATOM   13838 C  CD2   . TRP   B  1 708  ? 25.668  29.612  77.811  1.00 16.17 ? 706  TRP   B CD2   1 
ATOM   13839 N  NE1   . TRP   B  1 708  ? 27.138  31.205  77.239  1.00 23.17 ? 706  TRP   B NE1   1 
ATOM   13840 C  CE2   . TRP   B  1 708  ? 26.524  30.613  78.310  1.00 20.75 ? 706  TRP   B CE2   1 
ATOM   13841 C  CE3   . TRP   B  1 708  ? 24.936  28.839  78.716  1.00 20.59 ? 706  TRP   B CE3   1 
ATOM   13842 C  CZ2   . TRP   B  1 708  ? 26.675  30.854  79.679  1.00 21.79 ? 706  TRP   B CZ2   1 
ATOM   13843 C  CZ3   . TRP   B  1 708  ? 25.076  29.086  80.073  1.00 19.69 ? 706  TRP   B CZ3   1 
ATOM   13844 C  CH2   . TRP   B  1 708  ? 25.939  30.086  80.540  1.00 20.56 ? 706  TRP   B CH2   1 
ATOM   13845 N  N     . ASN   B  1 709  ? 22.316  29.940  77.167  1.00 19.48 ? 707  ASN   B N     1 
ATOM   13846 C  CA    . ASN   B  1 709  ? 21.629  29.635  78.413  1.00 19.44 ? 707  ASN   B CA    1 
ATOM   13847 C  C     . ASN   B  1 709  ? 20.124  29.493  78.243  1.00 21.56 ? 707  ASN   B C     1 
ATOM   13848 O  O     . ASN   B  1 709  ? 19.485  28.821  79.057  1.00 21.96 ? 707  ASN   B O     1 
ATOM   13849 C  CB    . ASN   B  1 709  ? 21.952  30.691  79.491  1.00 18.03 ? 707  ASN   B CB    1 
ATOM   13850 C  CG    . ASN   B  1 709  ? 21.405  32.070  79.162  1.00 26.30 ? 707  ASN   B CG    1 
ATOM   13851 O  OD1   . ASN   B  1 709  ? 21.241  32.429  78.002  1.00 27.33 ? 707  ASN   B OD1   1 
ATOM   13852 N  ND2   . ASN   B  1 709  ? 21.131  32.853  80.195  1.00 22.80 ? 707  ASN   B ND2   1 
ATOM   13853 N  N     . PHE   B  1 710  ? 19.547  30.089  77.203  1.00 20.26 ? 708  PHE   B N     1 
ATOM   13854 C  CA    . PHE   B  1 710  ? 18.180  29.787  76.780  1.00 20.16 ? 708  PHE   B CA    1 
ATOM   13855 C  C     . PHE   B  1 710  ? 18.240  29.483  75.294  1.00 18.48 ? 708  PHE   B C     1 
ATOM   13856 O  O     . PHE   B  1 710  ? 17.761  30.259  74.460  1.00 17.15 ? 708  PHE   B O     1 
ATOM   13857 C  CB    . PHE   B  1 710  ? 17.221  30.933  77.091  1.00 21.27 ? 708  PHE   B CB    1 
ATOM   13858 C  CG    . PHE   B  1 710  ? 17.054  31.164  78.550  1.00 23.80 ? 708  PHE   B CG    1 
ATOM   13859 C  CD1   . PHE   B  1 710  ? 16.244  30.330  79.301  1.00 27.18 ? 708  PHE   B CD1   1 
ATOM   13860 C  CD2   . PHE   B  1 710  ? 17.747  32.181  79.182  1.00 26.95 ? 708  PHE   B CD2   1 
ATOM   13861 C  CE1   . PHE   B  1 710  ? 16.114  30.523  80.666  1.00 30.38 ? 708  PHE   B CE1   1 
ATOM   13862 C  CE2   . PHE   B  1 710  ? 17.616  32.382  80.535  1.00 30.43 ? 708  PHE   B CE2   1 
ATOM   13863 C  CZ    . PHE   B  1 710  ? 16.805  31.549  81.281  1.00 27.47 ? 708  PHE   B CZ    1 
ATOM   13864 N  N     . PRO   B  1 711  ? 18.835  28.340  74.937  1.00 17.79 ? 709  PRO   B N     1 
ATOM   13865 C  CA    . PRO   B  1 711  ? 19.204  28.085  73.540  1.00 17.03 ? 709  PRO   B CA    1 
ATOM   13866 C  C     . PRO   B  1 711  ? 18.029  27.795  72.621  1.00 18.46 ? 709  PRO   B C     1 
ATOM   13867 O  O     . PRO   B  1 711  ? 18.221  27.740  71.397  1.00 16.91 ? 709  PRO   B O     1 
ATOM   13868 C  CB    . PRO   B  1 711  ? 20.120  26.866  73.660  1.00 18.73 ? 709  PRO   B CB    1 
ATOM   13869 C  CG    . PRO   B  1 711  ? 19.573  26.131  74.835  1.00 19.59 ? 709  PRO   B CG    1 
ATOM   13870 C  CD    . PRO   B  1 711  ? 19.192  27.210  75.815  1.00 18.14 ? 709  PRO   B CD    1 
ATOM   13871 N  N     . LEU   B  1 712  ? 16.836  27.571  73.158  1.00 19.96 ? 710  LEU   B N     1 
ATOM   13872 C  CA    . LEU   B  1 712  ? 15.634  27.496  72.345  1.00 16.72 ? 710  LEU   B CA    1 
ATOM   13873 C  C     . LEU   B  1 712  ? 14.723  28.692  72.537  1.00 17.85 ? 710  LEU   B C     1 
ATOM   13874 O  O     . LEU   B  1 712  ? 14.226  29.246  71.553  1.00 17.37 ? 710  LEU   B O     1 
ATOM   13875 C  CB    . LEU   B  1 712  ? 14.846  26.218  72.658  1.00 16.69 ? 710  LEU   B CB    1 
ATOM   13876 C  CG    . LEU   B  1 712  ? 13.603  26.071  71.768  1.00 15.19 ? 710  LEU   B CG    1 
ATOM   13877 C  CD1   . LEU   B  1 712  ? 13.989  25.961  70.282  1.00 15.91 ? 710  LEU   B CD1   1 
ATOM   13878 C  CD2   . LEU   B  1 712  ? 12.734  24.865  72.210  1.00 18.13 ? 710  LEU   B CD2   1 
ATOM   13879 N  N     . ALA   B  1 713  ? 14.502  29.105  73.787  1.00 16.78 ? 711  ALA   B N     1 
ATOM   13880 C  CA    . ALA   B  1 713  ? 13.487  30.112  74.069  1.00 17.73 ? 711  ALA   B CA    1 
ATOM   13881 C  C     . ALA   B  1 713  ? 13.895  31.479  73.529  1.00 17.83 ? 711  ALA   B C     1 
ATOM   13882 O  O     . ALA   B  1 713  ? 13.120  32.135  72.829  1.00 16.54 ? 711  ALA   B O     1 
ATOM   13883 C  CB    . ALA   B  1 713  ? 13.227  30.187  75.575  1.00 17.22 ? 711  ALA   B CB    1 
ATOM   13884 N  N     . ILE   B  1 714  ? 15.096  31.943  73.873  1.00 16.48 ? 712  ILE   B N     1 
ATOM   13885 C  CA    . ILE   B  1 714  ? 15.511  33.261  73.403  1.00 16.15 ? 712  ILE   B CA    1 
ATOM   13886 C  C     . ILE   B  1 714  ? 15.851  33.202  71.925  1.00 17.51 ? 712  ILE   B C     1 
ATOM   13887 O  O     . ILE   B  1 714  ? 15.515  34.111  71.157  1.00 16.37 ? 712  ILE   B O     1 
ATOM   13888 C  CB    . ILE   B  1 714  ? 16.680  33.778  74.255  1.00 20.27 ? 712  ILE   B CB    1 
ATOM   13889 C  CG1   . ILE   B  1 714  ? 16.139  34.182  75.628  1.00 19.54 ? 712  ILE   B CG1   1 
ATOM   13890 C  CG2   . ILE   B  1 714  ? 17.397  34.940  73.572  1.00 18.85 ? 712  ILE   B CG2   1 
ATOM   13891 C  CD1   . ILE   B  1 714  ? 17.202  34.765  76.548  1.00 26.36 ? 712  ILE   B CD1   1 
ATOM   13892 N  N     . PHE   B  1 715  ? 16.477  32.109  71.503  1.00 15.95 ? 713  PHE   B N     1 
ATOM   13893 C  CA    . PHE   B  1 715  ? 16.652  31.838  70.083  1.00 15.71 ? 713  PHE   B CA    1 
ATOM   13894 C  C     . PHE   B  1 715  ? 15.342  32.020  69.326  1.00 15.49 ? 713  PHE   B C     1 
ATOM   13895 O  O     . PHE   B  1 715  ? 15.276  32.776  68.355  1.00 14.12 ? 713  PHE   B O     1 
ATOM   13896 C  CB    . PHE   B  1 715  ? 17.178  30.419  69.912  1.00 17.34 ? 713  PHE   B CB    1 
ATOM   13897 C  CG    . PHE   B  1 715  ? 17.340  30.005  68.494  1.00 17.40 ? 713  PHE   B CG    1 
ATOM   13898 C  CD1   . PHE   B  1 715  ? 18.487  30.346  67.798  1.00 16.56 ? 713  PHE   B CD1   1 
ATOM   13899 C  CD2   . PHE   B  1 715  ? 16.362  29.253  67.857  1.00 19.81 ? 713  PHE   B CD2   1 
ATOM   13900 C  CE1   . PHE   B  1 715  ? 18.657  29.952  66.479  1.00 18.10 ? 713  PHE   B CE1   1 
ATOM   13901 C  CE2   . PHE   B  1 715  ? 16.523  28.862  66.535  1.00 17.17 ? 713  PHE   B CE2   1 
ATOM   13902 C  CZ    . PHE   B  1 715  ? 17.672  29.215  65.847  1.00 20.50 ? 713  PHE   B CZ    1 
ATOM   13903 N  N     . THR   B  1 716  ? 14.278  31.356  69.792  1.00 14.93 ? 714  THR   B N     1 
ATOM   13904 C  CA    . THR   B  1 716  ? 12.995  31.388  69.093  1.00 15.41 ? 714  THR   B CA    1 
ATOM   13905 C  C     . THR   B  1 716  ? 12.331  32.749  69.215  1.00 16.07 ? 714  THR   B C     1 
ATOM   13906 O  O     . THR   B  1 716  ? 11.749  33.240  68.243  1.00 14.81 ? 714  THR   B O     1 
ATOM   13907 C  CB    . THR   B  1 716  ? 12.068  30.305  69.649  1.00 12.85 ? 714  THR   B CB    1 
ATOM   13908 O  OG1   . THR   B  1 716  ? 12.642  29.019  69.394  1.00 16.70 ? 714  THR   B OG1   1 
ATOM   13909 C  CG2   . THR   B  1 716  ? 10.671  30.387  69.012  1.00 18.05 ? 714  THR   B CG2   1 
ATOM   13910 N  N     . GLY   B  1 717  ? 12.383  33.356  70.407  1.00 15.18 ? 715  GLY   B N     1 
ATOM   13911 C  CA    . GLY   B  1 717  ? 11.720  34.640  70.602  1.00 15.25 ? 715  GLY   B CA    1 
ATOM   13912 C  C     . GLY   B  1 717  ? 12.238  35.717  69.665  1.00 16.79 ? 715  GLY   B C     1 
ATOM   13913 O  O     . GLY   B  1 717  ? 11.463  36.390  68.979  1.00 14.66 ? 715  GLY   B O     1 
ATOM   13914 N  N     . GLN   B  1 718  ? 13.562  35.899  69.618  1.00 14.39 ? 716  GLN   B N     1 
ATOM   13915 C  CA    . GLN   B  1 718  ? 14.116  36.909  68.717  1.00 14.01 ? 716  GLN   B CA    1 
ATOM   13916 C  C     . GLN   B  1 718  ? 13.750  36.613  67.268  1.00 15.52 ? 716  GLN   B C     1 
ATOM   13917 O  O     . GLN   B  1 718  ? 13.305  37.501  66.531  1.00 15.52 ? 716  GLN   B O     1 
ATOM   13918 C  CB    . GLN   B  1 718  ? 15.637  36.992  68.884  1.00 14.52 ? 716  GLN   B CB    1 
ATOM   13919 C  CG    . GLN   B  1 718  ? 16.071  37.347  70.320  1.00 15.51 ? 716  GLN   B CG    1 
ATOM   13920 C  CD    . GLN   B  1 718  ? 17.568  37.558  70.450  1.00 19.02 ? 716  GLN   B CD    1 
ATOM   13921 O  OE1   . GLN   B  1 718  ? 18.013  38.476  71.141  1.00 21.38 ? 716  GLN   B OE1   1 
ATOM   13922 N  NE2   . GLN   B  1 718  ? 18.354  36.699  69.800  1.00 18.53 ? 716  GLN   B NE2   1 
ATOM   13923 N  N     . ILE   B  1 719  ? 13.936  35.364  66.840  1.00 14.41 ? 717  ILE   B N     1 
ATOM   13924 C  CA    . ILE   B  1 719  ? 13.692  35.001  65.447  1.00 16.67 ? 717  ILE   B CA    1 
ATOM   13925 C  C     . ILE   B  1 719  ? 12.221  35.157  65.099  1.00 14.40 ? 717  ILE   B C     1 
ATOM   13926 O  O     . ILE   B  1 719  ? 11.869  35.715  64.052  1.00 17.05 ? 717  ILE   B O     1 
ATOM   13927 C  CB    . ILE   B  1 719  ? 14.177  33.567  65.188  1.00 14.28 ? 717  ILE   B CB    1 
ATOM   13928 C  CG1   . ILE   B  1 719  ? 15.700  33.541  65.181  1.00 14.02 ? 717  ILE   B CG1   1 
ATOM   13929 C  CG2   . ILE   B  1 719  ? 13.590  33.023  63.906  1.00 19.00 ? 717  ILE   B CG2   1 
ATOM   13930 C  CD1   . ILE   B  1 719  ? 16.202  32.150  65.361  1.00 18.05 ? 717  ILE   B CD1   1 
ATOM   13931 N  N     . ALA   B  1 720  ? 11.341  34.666  65.972  1.00 15.19 ? 718  ALA   B N     1 
ATOM   13932 C  CA    . ALA   B  1 720  ? 9.907   34.741  65.695  1.00 14.91 ? 718  ALA   B CA    1 
ATOM   13933 C  C     . ALA   B  1 720  ? 9.456   36.185  65.543  1.00 15.10 ? 718  ALA   B C     1 
ATOM   13934 O  O     . ALA   B  1 720  ? 8.692   36.521  64.627  1.00 14.81 ? 718  ALA   B O     1 
ATOM   13935 C  CB    . ALA   B  1 720  ? 9.127   34.057  66.816  1.00 15.62 ? 718  ALA   B CB    1 
ATOM   13936 N  N     . ALA   B  1 721  ? 9.913   37.050  66.447  1.00 14.80 ? 719  ALA   B N     1 
ATOM   13937 C  CA    . ALA   B  1 721  ? 9.545   38.460  66.382  1.00 16.33 ? 719  ALA   B CA    1 
ATOM   13938 C  C     . ALA   B  1 721  ? 10.025  39.090  65.088  1.00 14.44 ? 719  ALA   B C     1 
ATOM   13939 O  O     . ALA   B  1 721  ? 9.279   39.813  64.423  1.00 14.82 ? 719  ALA   B O     1 
ATOM   13940 C  CB    . ALA   B  1 721  ? 10.130  39.204  67.583  1.00 16.93 ? 719  ALA   B CB    1 
ATOM   13941 N  N     . ALA   B  1 722  ? 11.284  38.843  64.721  1.00 12.20 ? 720  ALA   B N     1 
ATOM   13942 C  CA    . ALA   B  1 722  ? 11.801  39.454  63.506  1.00 16.67 ? 720  ALA   B CA    1 
ATOM   13943 C  C     . ALA   B  1 722  ? 11.045  38.941  62.288  1.00 15.56 ? 720  ALA   B C     1 
ATOM   13944 O  O     . ALA   B  1 722  ? 10.662  39.722  61.412  1.00 15.38 ? 720  ALA   B O     1 
ATOM   13945 C  CB    . ALA   B  1 722  ? 13.301  39.182  63.374  1.00 12.19 ? 720  ALA   B CB    1 
ATOM   13946 N  N     . LEU   B  1 723  ? 10.807  37.628  62.229  1.00 15.32 ? 721  LEU   B N     1 
ATOM   13947 C  CA    . LEU   B  1 723  ? 10.081  37.047  61.100  1.00 15.62 ? 721  LEU   B CA    1 
ATOM   13948 C  C     . LEU   B  1 723  ? 8.672   37.599  60.997  1.00 15.10 ? 721  LEU   B C     1 
ATOM   13949 O  O     . LEU   B  1 723  ? 8.218   37.980  59.907  1.00 17.51 ? 721  LEU   B O     1 
ATOM   13950 C  CB    . LEU   B  1 723  ? 10.013  35.528  61.236  1.00 15.74 ? 721  LEU   B CB    1 
ATOM   13951 C  CG    . LEU   B  1 723  ? 11.299  34.749  60.971  1.00 17.03 ? 721  LEU   B CG    1 
ATOM   13952 C  CD1   . LEU   B  1 723  ? 11.072  33.311  61.405  1.00 17.11 ? 721  LEU   B CD1   1 
ATOM   13953 C  CD2   . LEU   B  1 723  ? 11.698  34.822  59.498  1.00 17.18 ? 721  LEU   B CD2   1 
ATOM   13954 N  N     . VAL   B  1 724  ? 7.939   37.616  62.113  1.00 14.34 ? 722  VAL   B N     1 
ATOM   13955 C  CA    . VAL   B  1 724  ? 6.533   37.971  62.007  1.00 16.43 ? 722  VAL   B CA    1 
ATOM   13956 C  C     . VAL   B  1 724  ? 6.382   39.460  61.721  1.00 16.45 ? 722  VAL   B C     1 
ATOM   13957 O  O     . VAL   B  1 724  ? 5.369   39.882  61.154  1.00 16.90 ? 722  VAL   B O     1 
ATOM   13958 C  CB    . VAL   B  1 724  ? 5.767   37.531  63.274  1.00 14.70 ? 722  VAL   B CB    1 
ATOM   13959 C  CG1   . VAL   B  1 724  ? 6.009   38.506  64.446  1.00 16.49 ? 722  VAL   B CG1   1 
ATOM   13960 C  CG2   . VAL   B  1 724  ? 4.264   37.325  62.955  1.00 15.34 ? 722  VAL   B CG2   1 
ATOM   13961 N  N     . ALA   B  1 725  ? 7.386   40.263  62.051  1.00 15.79 ? 723  ALA   B N     1 
ATOM   13962 C  CA    . ALA   B  1 725  ? 7.373   41.665  61.656  1.00 17.26 ? 723  ALA   B CA    1 
ATOM   13963 C  C     . ALA   B  1 725  ? 7.690   41.852  60.177  1.00 19.09 ? 723  ALA   B C     1 
ATOM   13964 O  O     . ALA   B  1 725  ? 7.686   42.990  59.698  1.00 20.16 ? 723  ALA   B O     1 
ATOM   13965 C  CB    . ALA   B  1 725  ? 8.351   42.462  62.523  1.00 18.40 ? 723  ALA   B CB    1 
ATOM   13966 N  N     . GLY   B  1 726  ? 7.967   40.772  59.448  1.00 18.70 ? 724  GLY   B N     1 
ATOM   13967 C  CA    . GLY   B  1 726  ? 8.187   40.846  58.019  1.00 16.82 ? 724  GLY   B CA    1 
ATOM   13968 C  C     . GLY   B  1 726  ? 9.634   40.870  57.569  1.00 18.96 ? 724  GLY   B C     1 
ATOM   13969 O  O     . GLY   B  1 726  ? 9.893   41.226  56.414  1.00 19.74 ? 724  GLY   B O     1 
ATOM   13970 N  N     . ASN   B  1 727  ? 10.571  40.498  58.429  1.00 15.25 ? 725  ASN   B N     1 
ATOM   13971 C  CA    . ASN   B  1 727  ? 11.991  40.513  58.129  1.00 16.79 ? 725  ASN   B CA    1 
ATOM   13972 C  C     . ASN   B  1 727  ? 12.512  39.103  57.946  1.00 16.39 ? 725  ASN   B C     1 
ATOM   13973 O  O     . ASN   B  1 727  ? 12.203  38.228  58.761  1.00 16.85 ? 725  ASN   B O     1 
ATOM   13974 C  CB    . ASN   B  1 727  ? 12.763  41.180  59.259  1.00 17.04 ? 725  ASN   B CB    1 
ATOM   13975 C  CG    . ASN   B  1 727  ? 12.185  42.517  59.636  1.00 21.88 ? 725  ASN   B CG    1 
ATOM   13976 O  OD1   . ASN   B  1 727  ? 12.396  43.505  58.930  1.00 19.86 ? 725  ASN   B OD1   1 
ATOM   13977 N  ND2   . ASN   B  1 727  ? 11.445  42.561  60.754  1.00 18.70 ? 725  ASN   B ND2   1 
ATOM   13978 N  N     . PRO   B  1 728  ? 13.311  38.847  56.917  1.00 17.15 ? 726  PRO   B N     1 
ATOM   13979 C  CA    . PRO   B  1 728  ? 14.060  37.594  56.881  1.00 18.74 ? 726  PRO   B CA    1 
ATOM   13980 C  C     . PRO   B  1 728  ? 15.143  37.625  57.947  1.00 17.64 ? 726  PRO   B C     1 
ATOM   13981 O  O     . PRO   B  1 728  ? 15.647  38.688  58.322  1.00 17.88 ? 726  PRO   B O     1 
ATOM   13982 C  CB    . PRO   B  1 728  ? 14.650  37.575  55.471  1.00 17.18 ? 726  PRO   B CB    1 
ATOM   13983 C  CG    . PRO   B  1 728  ? 14.839  39.046  55.147  1.00 18.98 ? 726  PRO   B CG    1 
ATOM   13984 C  CD    . PRO   B  1 728  ? 13.728  39.784  55.856  1.00 16.76 ? 726  PRO   B CD    1 
ATOM   13985 N  N     . VAL   B  1 729  ? 15.486  36.444  58.449  1.00 16.43 ? 727  VAL   B N     1 
ATOM   13986 C  CA    . VAL   B  1 729  ? 16.352  36.320  59.617  1.00 18.27 ? 727  VAL   B CA    1 
ATOM   13987 C  C     . VAL   B  1 729  ? 17.597  35.514  59.286  1.00 17.25 ? 727  VAL   B C     1 
ATOM   13988 O  O     . VAL   B  1 729  ? 17.523  34.468  58.627  1.00 15.47 ? 727  VAL   B O     1 
ATOM   13989 C  CB    . VAL   B  1 729  ? 15.601  35.677  60.794  1.00 17.40 ? 727  VAL   B CB    1 
ATOM   13990 C  CG1   . VAL   B  1 729  ? 16.565  35.247  61.894  1.00 19.75 ? 727  VAL   B CG1   1 
ATOM   13991 C  CG2   . VAL   B  1 729  ? 14.560  36.661  61.319  1.00 15.70 ? 727  VAL   B CG2   1 
ATOM   13992 N  N     . LEU   B  1 730  ? 18.735  36.006  59.771  1.00 16.80 ? 728  LEU   B N     1 
ATOM   13993 C  CA    . LEU   B  1 730  ? 19.977  35.246  59.875  1.00 14.02 ? 728  LEU   B CA    1 
ATOM   13994 C  C     . LEU   B  1 730  ? 20.131  34.862  61.342  1.00 16.55 ? 728  LEU   B C     1 
ATOM   13995 O  O     . LEU   B  1 730  ? 20.345  35.729  62.198  1.00 18.43 ? 728  LEU   B O     1 
ATOM   13996 C  CB    . LEU   B  1 730  ? 21.177  36.059  59.397  1.00 16.74 ? 728  LEU   B CB    1 
ATOM   13997 C  CG    . LEU   B  1 730  ? 21.192  36.559  57.953  1.00 15.78 ? 728  LEU   B CG    1 
ATOM   13998 C  CD1   . LEU   B  1 730  ? 20.763  35.458  56.969  1.00 17.77 ? 728  LEU   B CD1   1 
ATOM   13999 C  CD2   . LEU   B  1 730  ? 20.343  37.815  57.779  1.00 17.97 ? 728  LEU   B CD2   1 
ATOM   14000 N  N     . ALA   B  1 731  ? 19.995  33.573  61.635  1.00 16.88 ? 729  ALA   B N     1 
ATOM   14001 C  CA    . ALA   B  1 731  ? 19.998  33.081  63.007  1.00 14.66 ? 729  ALA   B CA    1 
ATOM   14002 C  C     . ALA   B  1 731  ? 21.386  32.547  63.341  1.00 18.04 ? 729  ALA   B C     1 
ATOM   14003 O  O     . ALA   B  1 731  ? 21.825  31.535  62.781  1.00 18.67 ? 729  ALA   B O     1 
ATOM   14004 C  CB    . ALA   B  1 731  ? 18.935  32.001  63.203  1.00 17.12 ? 729  ALA   B CB    1 
ATOM   14005 N  N     . LYS   B  1 732  ? 22.065  33.215  64.273  1.00 15.73 ? 730  LYS   B N     1 
ATOM   14006 C  CA    . LYS   B  1 732  ? 23.392  32.795  64.703  1.00 15.35 ? 730  LYS   B CA    1 
ATOM   14007 C  C     . LYS   B  1 732  ? 23.286  32.300  66.136  1.00 18.46 ? 730  LYS   B C     1 
ATOM   14008 O  O     . LYS   B  1 732  ? 23.262  33.113  67.072  1.00 18.27 ? 730  LYS   B O     1 
ATOM   14009 C  CB    . LYS   B  1 732  ? 24.389  33.951  64.603  1.00 16.93 ? 730  LYS   B CB    1 
ATOM   14010 C  CG    . LYS   B  1 732  ? 25.810  33.510  64.205  1.00 19.61 ? 730  LYS   B CG    1 
ATOM   14011 C  CD    . LYS   B  1 732  ? 26.440  32.642  65.263  1.00 23.58 ? 730  LYS   B CD    1 
ATOM   14012 C  CE    . LYS   B  1 732  ? 26.837  33.443  66.482  1.00 21.34 ? 730  LYS   B CE    1 
ATOM   14013 N  NZ    . LYS   B  1 732  ? 27.431  32.520  67.479  1.00 19.85 ? 730  LYS   B NZ    1 
ATOM   14014 N  N     . PRO   B  1 733  ? 23.205  30.994  66.360  1.00 19.70 ? 731  PRO   B N     1 
ATOM   14015 C  CA    . PRO   B  1 733  ? 23.089  30.478  67.723  1.00 20.19 ? 731  PRO   B CA    1 
ATOM   14016 C  C     . PRO   B  1 733  ? 24.433  30.466  68.427  1.00 18.72 ? 731  PRO   B C     1 
ATOM   14017 O  O     . PRO   B  1 733  ? 25.492  30.511  67.806  1.00 18.53 ? 731  PRO   B O     1 
ATOM   14018 C  CB    . PRO   B  1 733  ? 22.585  29.051  67.507  1.00 17.66 ? 731  PRO   B CB    1 
ATOM   14019 C  CG    . PRO   B  1 733  ? 23.264  28.640  66.213  1.00 19.02 ? 731  PRO   B CG    1 
ATOM   14020 C  CD    . PRO   B  1 733  ? 23.295  29.910  65.364  1.00 18.13 ? 731  PRO   B CD    1 
ATOM   14021 N  N     . ALA   B  1 734  ? 24.369  30.403  69.752  1.00 18.94 ? 732  ALA   B N     1 
ATOM   14022 C  CA    . ALA   B  1 734  ? 25.586  30.288  70.542  1.00 19.28 ? 732  ALA   B CA    1 
ATOM   14023 C  C     . ALA   B  1 734  ? 26.410  29.093  70.085  1.00 19.99 ? 732  ALA   B C     1 
ATOM   14024 O  O     . ALA   B  1 734  ? 25.876  28.065  69.660  1.00 19.65 ? 732  ALA   B O     1 
ATOM   14025 C  CB    . ALA   B  1 734  ? 25.253  30.140  72.027  1.00 18.47 ? 732  ALA   B CB    1 
ATOM   14026 N  N     . GLU   B  1 735  ? 27.735  29.241  70.181  1.00 18.03 ? 733  GLU   B N     1 
ATOM   14027 C  CA    . GLU   B  1 735  ? 28.634  28.170  69.764  1.00 17.64 ? 733  GLU   B CA    1 
ATOM   14028 C  C     . GLU   B  1 735  ? 28.388  26.885  70.552  1.00 20.76 ? 733  GLU   B C     1 
ATOM   14029 O  O     . GLU   B  1 735  ? 28.521  25.778  70.011  1.00 18.39 ? 733  GLU   B O     1 
ATOM   14030 C  CB    . GLU   B  1 735  ? 30.095  28.629  69.920  1.00 22.44 ? 733  GLU   B CB    1 
ATOM   14031 C  CG    . GLU   B  1 735  ? 31.098  27.594  69.467  1.00 27.16 ? 733  GLU   B CG    1 
ATOM   14032 C  CD    . GLU   B  1 735  ? 32.546  28.042  69.612  1.00 33.75 ? 733  GLU   B CD    1 
ATOM   14033 O  OE1   . GLU   B  1 735  ? 32.787  29.198  70.026  1.00 36.13 ? 733  GLU   B OE1   1 
ATOM   14034 O  OE2   . GLU   B  1 735  ? 33.436  27.222  69.308  1.00 35.46 ? 733  GLU   B OE2   1 
ATOM   14035 N  N     . GLU   B  1 736  ? 28.005  27.014  71.820  1.00 20.62 ? 734  GLU   B N     1 
ATOM   14036 C  CA    . GLU   B  1 736  ? 27.837  25.860  72.687  1.00 20.94 ? 734  GLU   B CA    1 
ATOM   14037 C  C     . GLU   B  1 736  ? 26.568  25.065  72.402  1.00 21.01 ? 734  GLU   B C     1 
ATOM   14038 O  O     . GLU   B  1 736  ? 26.509  23.885  72.758  1.00 19.17 ? 734  GLU   B O     1 
ATOM   14039 C  CB    . GLU   B  1 736  ? 27.825  26.320  74.145  1.00 21.24 ? 734  GLU   B CB    1 
ATOM   14040 C  CG    . GLU   B  1 736  ? 29.110  27.024  74.574  1.00 23.84 ? 734  GLU   B CG    1 
ATOM   14041 C  CD    . GLU   B  1 736  ? 29.141  28.519  74.262  1.00 28.82 ? 734  GLU   B CD    1 
ATOM   14042 O  OE1   . GLU   B  1 736  ? 28.296  29.025  73.489  1.00 24.57 ? 734  GLU   B OE1   1 
ATOM   14043 O  OE2   . GLU   B  1 736  ? 30.040  29.199  74.796  1.00 33.13 ? 734  GLU   B OE2   1 
ATOM   14044 N  N     . THR   B  1 737  ? 25.536  25.677  71.808  1.00 16.80 ? 735  THR   B N     1 
ATOM   14045 C  CA    . THR   B  1 737  ? 24.210  25.050  71.749  1.00 19.31 ? 735  THR   B CA    1 
ATOM   14046 C  C     . THR   B  1 737  ? 23.581  25.131  70.357  1.00 18.68 ? 735  THR   B C     1 
ATOM   14047 O  O     . THR   B  1 737  ? 22.443  25.574  70.200  1.00 18.17 ? 735  THR   B O     1 
ATOM   14048 C  CB    . THR   B  1 737  ? 23.283  25.685  72.782  1.00 18.29 ? 735  THR   B CB    1 
ATOM   14049 O  OG1   . THR   B  1 737  ? 23.214  27.099  72.569  1.00 17.59 ? 735  THR   B OG1   1 
ATOM   14050 C  CG2   . THR   B  1 737  ? 23.771  25.421  74.205  1.00 20.64 ? 735  THR   B CG2   1 
ATOM   14051 N  N     . PRO   B  1 738  ? 24.284  24.676  69.322  1.00 19.77 ? 736  PRO   B N     1 
ATOM   14052 C  CA    . PRO   B  1 738  ? 23.737  24.821  67.969  1.00 17.40 ? 736  PRO   B CA    1 
ATOM   14053 C  C     . PRO   B  1 738  ? 22.660  23.809  67.653  1.00 17.43 ? 736  PRO   B C     1 
ATOM   14054 O  O     . PRO   B  1 738  ? 21.835  24.073  66.770  1.00 17.52 ? 736  PRO   B O     1 
ATOM   14055 C  CB    . PRO   B  1 738  ? 24.963  24.607  67.077  1.00 16.05 ? 736  PRO   B CB    1 
ATOM   14056 C  CG    . PRO   B  1 738  ? 25.727  23.587  67.816  1.00 17.61 ? 736  PRO   B CG    1 
ATOM   14057 C  CD    . PRO   B  1 738  ? 25.579  23.970  69.295  1.00 18.32 ? 736  PRO   B CD    1 
ATOM   14058 N  N     . LEU   B  1 739  ? 22.633  22.661  68.336  1.00 17.10 ? 737  LEU   B N     1 
ATOM   14059 C  CA    . LEU   B  1 739  ? 21.728  21.602  67.898  1.00 17.67 ? 737  LEU   B CA    1 
ATOM   14060 C  C     . LEU   B  1 739  ? 20.278  21.974  68.148  1.00 18.13 ? 737  LEU   B C     1 
ATOM   14061 O  O     . LEU   B  1 739  ? 19.426  21.747  67.283  1.00 17.21 ? 737  LEU   B O     1 
ATOM   14062 C  CB    . LEU   B  1 739  ? 22.050  20.289  68.595  1.00 17.97 ? 737  LEU   B CB    1 
ATOM   14063 C  CG    . LEU   B  1 739  ? 23.498  19.862  68.430  1.00 16.76 ? 737  LEU   B CG    1 
ATOM   14064 C  CD1   . LEU   B  1 739  ? 23.756  18.575  69.228  1.00 16.62 ? 737  LEU   B CD1   1 
ATOM   14065 C  CD2   . LEU   B  1 739  ? 23.825  19.694  66.946  1.00 20.20 ? 737  LEU   B CD2   1 
ATOM   14066 N  N     . ILE   B  1 740  ? 19.970  22.515  69.330  1.00 16.36 ? 738  ILE   B N     1 
ATOM   14067 C  CA    . ILE   B  1 740  ? 18.575  22.864  69.588  1.00 17.00 ? 738  ILE   B CA    1 
ATOM   14068 C  C     . ILE   B  1 740  ? 18.168  24.030  68.700  1.00 18.06 ? 738  ILE   B C     1 
ATOM   14069 O  O     . ILE   B  1 740  ? 17.016  24.111  68.259  1.00 16.28 ? 738  ILE   B O     1 
ATOM   14070 C  CB    . ILE   B  1 740  ? 18.326  23.146  71.086  1.00 19.27 ? 738  ILE   B CB    1 
ATOM   14071 C  CG1   . ILE   B  1 740  ? 16.833  23.324  71.376  1.00 16.42 ? 738  ILE   B CG1   1 
ATOM   14072 C  CG2   . ILE   B  1 740  ? 19.054  24.388  71.541  1.00 19.14 ? 738  ILE   B CG2   1 
ATOM   14073 C  CD1   . ILE   B  1 740  ? 16.011  22.076  71.084  1.00 18.13 ? 738  ILE   B CD1   1 
ATOM   14074 N  N     . ALA   B  1 741  ? 19.110  24.917  68.379  1.00 17.93 ? 739  ALA   B N     1 
ATOM   14075 C  CA    . ALA   B  1 741  ? 18.832  25.978  67.418  1.00 17.37 ? 739  ALA   B CA    1 
ATOM   14076 C  C     . ALA   B  1 741  ? 18.462  25.408  66.052  1.00 15.93 ? 739  ALA   B C     1 
ATOM   14077 O  O     . ALA   B  1 741  ? 17.486  25.849  65.427  1.00 18.51 ? 739  ALA   B O     1 
ATOM   14078 C  CB    . ALA   B  1 741  ? 20.042  26.892  67.295  1.00 17.94 ? 739  ALA   B CB    1 
ATOM   14079 N  N     . ALA   B  1 742  ? 19.259  24.451  65.557  1.00 15.89 ? 740  ALA   B N     1 
ATOM   14080 C  CA    . ALA   B  1 742  ? 18.934  23.798  64.291  1.00 17.15 ? 740  ALA   B CA    1 
ATOM   14081 C  C     . ALA   B  1 742  ? 17.539  23.194  64.335  1.00 18.15 ? 740  ALA   B C     1 
ATOM   14082 O  O     . ALA   B  1 742  ? 16.774  23.296  63.364  1.00 17.53 ? 740  ALA   B O     1 
ATOM   14083 C  CB    . ALA   B  1 742  ? 19.973  22.719  63.968  1.00 16.05 ? 740  ALA   B CB    1 
ATOM   14084 N  N     . GLU   B  1 743  ? 17.184  22.571  65.459  1.00 16.36 ? 741  GLU   B N     1 
ATOM   14085 C  CA    . GLU   B  1 743  ? 15.845  22.008  65.584  1.00 16.43 ? 741  GLU   B CA    1 
ATOM   14086 C  C     . GLU   B  1 743  ? 14.785  23.100  65.558  1.00 16.14 ? 741  GLU   B C     1 
ATOM   14087 O  O     . GLU   B  1 743  ? 13.736  22.924  64.938  1.00 15.99 ? 741  GLU   B O     1 
ATOM   14088 C  CB    . GLU   B  1 743  ? 15.735  21.180  66.863  1.00 19.73 ? 741  GLU   B CB    1 
ATOM   14089 C  CG    . GLU   B  1 743  ? 14.360  20.582  67.054  1.00 21.84 ? 741  GLU   B CG    1 
ATOM   14090 C  CD    . GLU   B  1 743  ? 14.055  19.437  66.102  1.00 22.33 ? 741  GLU   B CD    1 
ATOM   14091 O  OE1   . GLU   B  1 743  ? 14.943  19.015  65.329  1.00 21.05 ? 741  GLU   B OE1   1 
ATOM   14092 O  OE2   . GLU   B  1 743  ? 12.911  18.951  66.139  1.00 22.89 ? 741  GLU   B OE2   1 
ATOM   14093 N  N     . GLY   B  1 744  ? 15.043  24.228  66.229  1.00 18.35 ? 742  GLY   B N     1 
ATOM   14094 C  CA    . GLY   B  1 744  ? 14.149  25.368  66.123  1.00 17.08 ? 742  GLY   B CA    1 
ATOM   14095 C  C     . GLY   B  1 744  ? 13.928  25.805  64.687  1.00 18.21 ? 742  GLY   B C     1 
ATOM   14096 O  O     . GLY   B  1 744  ? 12.801  26.100  64.286  1.00 15.00 ? 742  GLY   B O     1 
ATOM   14097 N  N     . VAL   B  1 745  ? 15.002  25.854  63.893  1.00 14.98 ? 743  VAL   B N     1 
ATOM   14098 C  CA    . VAL   B  1 745  ? 14.868  26.295  62.510  1.00 16.26 ? 743  VAL   B CA    1 
ATOM   14099 C  C     . VAL   B  1 745  ? 14.116  25.255  61.684  1.00 17.30 ? 743  VAL   B C     1 
ATOM   14100 O  O     . VAL   B  1 745  ? 13.275  25.609  60.848  1.00 15.70 ? 743  VAL   B O     1 
ATOM   14101 C  CB    . VAL   B  1 745  ? 16.251  26.613  61.912  1.00 18.46 ? 743  VAL   B CB    1 
ATOM   14102 C  CG1   . VAL   B  1 745  ? 16.141  26.832  60.404  1.00 16.11 ? 743  VAL   B CG1   1 
ATOM   14103 C  CG2   . VAL   B  1 745  ? 16.835  27.852  62.594  1.00 17.50 ? 743  VAL   B CG2   1 
ATOM   14104 N  N     . ARG   B  1 746  ? 14.382  23.964  61.914  1.00 14.50 ? 744  ARG   B N     1 
ATOM   14105 C  CA    . ARG   B  1 746  ? 13.599  22.922  61.240  1.00 16.87 ? 744  ARG   B CA    1 
ATOM   14106 C  C     . ARG   B  1 746  ? 12.113  23.120  61.484  1.00 17.00 ? 744  ARG   B C     1 
ATOM   14107 O  O     . ARG   B  1 746  ? 11.293  23.007  60.567  1.00 16.47 ? 744  ARG   B O     1 
ATOM   14108 C  CB    . ARG   B  1 746  ? 13.971  21.526  61.735  1.00 19.11 ? 744  ARG   B CB    1 
ATOM   14109 C  CG    . ARG   B  1 746  ? 15.355  21.058  61.412  1.00 21.32 ? 744  ARG   B CG    1 
ATOM   14110 C  CD    . ARG   B  1 746  ? 15.565  19.675  61.983  1.00 20.42 ? 744  ARG   B CD    1 
ATOM   14111 N  NE    . ARG   B  1 746  ? 16.965  19.328  61.833  1.00 23.41 ? 744  ARG   B NE    1 
ATOM   14112 C  CZ    . ARG   B  1 746  ? 17.862  19.342  62.802  1.00 20.48 ? 744  ARG   B CZ    1 
ATOM   14113 N  NH1   . ARG   B  1 746  ? 17.506  19.412  64.079  1.00 18.78 ? 744  ARG   B NH1   1 
ATOM   14114 N  NH2   . ARG   B  1 746  ? 19.152  19.260  62.485  1.00 19.72 ? 744  ARG   B NH2   1 
ATOM   14115 N  N     . ILE   B  1 747  ? 11.752  23.400  62.733  1.00 16.60 ? 745  ILE   B N     1 
ATOM   14116 C  CA    . ILE   B  1 747  ? 10.339  23.489  63.072  1.00 16.32 ? 745  ILE   B CA    1 
ATOM   14117 C  C     . ILE   B  1 747  ? 9.719   24.728  62.450  1.00 16.74 ? 745  ILE   B C     1 
ATOM   14118 O  O     . ILE   B  1 747  ? 8.605   24.682  61.915  1.00 16.94 ? 745  ILE   B O     1 
ATOM   14119 C  CB    . ILE   B  1 747  ? 10.173  23.478  64.597  1.00 15.79 ? 745  ILE   B CB    1 
ATOM   14120 C  CG1   . ILE   B  1 747  ? 10.483  22.065  65.121  1.00 19.85 ? 745  ILE   B CG1   1 
ATOM   14121 C  CG2   . ILE   B  1 747  ? 8.784   23.989  64.976  1.00 16.52 ? 745  ILE   B CG2   1 
ATOM   14122 C  CD1   . ILE   B  1 747  ? 10.481  21.940  66.631  1.00 20.37 ? 745  ILE   B CD1   1 
ATOM   14123 N  N     . LEU   B  1 748  ? 10.417  25.857  62.530  1.00 16.18 ? 746  LEU   B N     1 
ATOM   14124 C  CA    . LEU   B  1 748  ? 9.895   27.072  61.920  1.00 14.37 ? 746  LEU   B CA    1 
ATOM   14125 C  C     . LEU   B  1 748  ? 9.776   26.918  60.411  1.00 14.60 ? 746  LEU   B C     1 
ATOM   14126 O  O     . LEU   B  1 748  ? 8.795   27.368  59.811  1.00 14.76 ? 746  LEU   B O     1 
ATOM   14127 C  CB    . LEU   B  1 748  ? 10.769  28.264  62.278  1.00 15.92 ? 746  LEU   B CB    1 
ATOM   14128 C  CG    . LEU   B  1 748  ? 10.441  28.885  63.647  1.00 18.18 ? 746  LEU   B CG    1 
ATOM   14129 C  CD1   . LEU   B  1 748  ? 11.646  29.693  64.156  1.00 20.28 ? 746  LEU   B CD1   1 
ATOM   14130 C  CD2   . LEU   B  1 748  ? 9.224   29.746  63.564  1.00 21.31 ? 746  LEU   B CD2   1 
ATOM   14131 N  N     . ARG   B  1 749  ? 10.757  26.280  59.777  1.00 15.24 ? 747  ARG   B N     1 
ATOM   14132 C  CA    . ARG   B  1 749  ? 10.626  26.025  58.348  1.00 15.67 ? 747  ARG   B CA    1 
ATOM   14133 C  C     . ARG   B  1 749  ? 9.478   25.074  58.061  1.00 15.89 ? 747  ARG   B C     1 
ATOM   14134 O  O     . ARG   B  1 749  ? 8.730   25.278  57.098  1.00 16.23 ? 747  ARG   B O     1 
ATOM   14135 C  CB    . ARG   B  1 749  ? 11.925  25.462  57.789  1.00 13.95 ? 747  ARG   B CB    1 
ATOM   14136 C  CG    . ARG   B  1 749  ? 13.034  26.497  57.727  1.00 15.39 ? 747  ARG   B CG    1 
ATOM   14137 C  CD    . ARG   B  1 749  ? 14.187  25.946  56.905  1.00 16.16 ? 747  ARG   B CD    1 
ATOM   14138 N  NE    . ARG   B  1 749  ? 15.241  26.924  56.669  1.00 19.48 ? 747  ARG   B NE    1 
ATOM   14139 C  CZ    . ARG   B  1 749  ? 16.285  26.684  55.885  1.00 20.82 ? 747  ARG   B CZ    1 
ATOM   14140 N  NH1   . ARG   B  1 749  ? 16.422  25.524  55.259  1.00 21.30 ? 747  ARG   B NH1   1 
ATOM   14141 N  NH2   . ARG   B  1 749  ? 17.205  27.631  55.715  1.00 18.51 ? 747  ARG   B NH2   1 
ATOM   14142 N  N     . GLU   B  1 750  ? 9.337   24.015  58.863  1.00 16.03 ? 748  GLU   B N     1 
ATOM   14143 C  CA    . GLU   B  1 750  ? 8.233   23.083  58.640  1.00 16.97 ? 748  GLU   B CA    1 
ATOM   14144 C  C     . GLU   B  1 750  ? 6.900   23.789  58.788  1.00 15.02 ? 748  GLU   B C     1 
ATOM   14145 O  O     . GLU   B  1 750  ? 5.938   23.469  58.079  1.00 17.25 ? 748  GLU   B O     1 
ATOM   14146 C  CB    . GLU   B  1 750  ? 8.314   21.907  59.616  1.00 16.01 ? 748  GLU   B CB    1 
ATOM   14147 C  CG    . GLU   B  1 750  ? 7.197   20.867  59.445  1.00 17.94 ? 748  GLU   B CG    1 
ATOM   14148 C  CD    . GLU   B  1 750  ? 7.343   19.693  60.400  1.00 21.76 ? 748  GLU   B CD    1 
ATOM   14149 O  OE1   . GLU   B  1 750  ? 8.403   19.573  61.041  1.00 21.65 ? 748  GLU   B OE1   1 
ATOM   14150 O  OE2   . GLU   B  1 750  ? 6.398   18.895  60.523  1.00 24.71 ? 748  GLU   B OE2   1 
ATOM   14151 N  N     . ALA   B  1 751  ? 6.837   24.764  59.688  1.00 16.93 ? 749  ALA   B N     1 
ATOM   14152 C  CA    . ALA   B  1 751  ? 5.633   25.535  59.948  1.00 16.38 ? 749  ALA   B CA    1 
ATOM   14153 C  C     . ALA   B  1 751  ? 5.326   26.545  58.857  1.00 16.58 ? 749  ALA   B C     1 
ATOM   14154 O  O     . ALA   B  1 751  ? 4.274   27.188  58.918  1.00 18.25 ? 749  ALA   B O     1 
ATOM   14155 C  CB    . ALA   B  1 751  ? 5.769   26.273  61.270  1.00 19.37 ? 749  ALA   B CB    1 
ATOM   14156 N  N     . GLY   B  1 752  ? 6.225   26.737  57.898  1.00 15.99 ? 750  GLY   B N     1 
ATOM   14157 C  CA    . GLY   B  1 752  ? 5.937   27.568  56.746  1.00 16.76 ? 750  GLY   B CA    1 
ATOM   14158 C  C     . GLY   B  1 752  ? 6.869   28.741  56.542  1.00 15.90 ? 750  GLY   B C     1 
ATOM   14159 O  O     . GLY   B  1 752  ? 6.705   29.466  55.554  1.00 16.87 ? 750  GLY   B O     1 
ATOM   14160 N  N     . ILE   B  1 753  ? 7.830   28.985  57.426  1.00 18.75 ? 751  ILE   B N     1 
ATOM   14161 C  CA    . ILE   B  1 753  ? 8.816   30.034  57.178  1.00 17.40 ? 751  ILE   B CA    1 
ATOM   14162 C  C     . ILE   B  1 753  ? 9.691   29.573  56.017  1.00 18.41 ? 751  ILE   B C     1 
ATOM   14163 O  O     . ILE   B  1 753  ? 10.338  28.521  56.113  1.00 16.58 ? 751  ILE   B O     1 
ATOM   14164 C  CB    . ILE   B  1 753  ? 9.678   30.317  58.420  1.00 15.53 ? 751  ILE   B CB    1 
ATOM   14165 C  CG1   . ILE   B  1 753  ? 8.803   30.676  59.629  1.00 16.86 ? 751  ILE   B CG1   1 
ATOM   14166 C  CG2   . ILE   B  1 753  ? 10.663  31.409  58.103  1.00 15.43 ? 751  ILE   B CG2   1 
ATOM   14167 C  CD1   . ILE   B  1 753  ? 8.002   31.963  59.428  1.00 15.67 ? 751  ILE   B CD1   1 
ATOM   14168 N  N     . PRO   B  1 754  ? 9.748   30.326  54.923  1.00 16.67 ? 752  PRO   B N     1 
ATOM   14169 C  CA    . PRO   B  1 754  ? 10.574  29.918  53.783  1.00 18.44 ? 752  PRO   B CA    1 
ATOM   14170 C  C     . PRO   B  1 754  ? 12.034  29.845  54.182  1.00 19.52 ? 752  PRO   B C     1 
ATOM   14171 O  O     . PRO   B  1 754  ? 12.504  30.610  55.028  1.00 17.67 ? 752  PRO   B O     1 
ATOM   14172 C  CB    . PRO   B  1 754  ? 10.349  31.032  52.752  1.00 20.54 ? 752  PRO   B CB    1 
ATOM   14173 C  CG    . PRO   B  1 754  ? 9.171   31.798  53.222  1.00 23.35 ? 752  PRO   B CG    1 
ATOM   14174 C  CD    . PRO   B  1 754  ? 9.058   31.604  54.697  1.00 18.60 ? 752  PRO   B CD    1 
ATOM   14175 N  N     . ALA   B  1 755  ? 12.757  28.921  53.537  1.00 18.79 ? 753  ALA   B N     1 
ATOM   14176 C  CA    . ALA   B  1 755  ? 14.183  28.777  53.803  1.00 20.19 ? 753  ALA   B CA    1 
ATOM   14177 C  C     . ALA   B  1 755  ? 14.938  30.077  53.555  1.00 22.18 ? 753  ALA   B C     1 
ATOM   14178 O  O     . ALA   B  1 755  ? 15.907  30.382  54.263  1.00 21.80 ? 753  ALA   B O     1 
ATOM   14179 C  CB    . ALA   B  1 755  ? 14.756  27.647  52.946  1.00 22.55 ? 753  ALA   B CB    1 
ATOM   14180 N  N     . SER   B  1 756  ? 14.505  30.869  52.576  1.00 20.54 ? 754  SER   B N     1 
ATOM   14181 C  CA    . SER   B  1 756  ? 15.173  32.140  52.332  1.00 18.61 ? 754  SER   B CA    1 
ATOM   14182 C  C     . SER   B  1 756  ? 14.905  33.146  53.439  1.00 20.28 ? 754  SER   B C     1 
ATOM   14183 O  O     . SER   B  1 756  ? 15.676  34.097  53.601  1.00 20.57 ? 754  SER   B O     1 
ATOM   14184 C  CB    . SER   B  1 756  ? 14.734  32.713  50.989  1.00 21.52 ? 754  SER   B CB    1 
ATOM   14185 O  OG    . SER   B  1 756  ? 13.349  33.034  51.027  1.00 25.75 ? 754  SER   B OG    1 
ATOM   14186 N  N     . ALA   B  1 757  ? 13.824  32.967  54.193  1.00 17.37 ? 755  ALA   B N     1 
ATOM   14187 C  CA    . ALA   B  1 757  ? 13.497  33.883  55.269  1.00 16.85 ? 755  ALA   B CA    1 
ATOM   14188 C  C     . ALA   B  1 757  ? 14.110  33.487  56.604  1.00 17.40 ? 755  ALA   B C     1 
ATOM   14189 O  O     . ALA   B  1 757  ? 14.105  34.298  57.529  1.00 17.26 ? 755  ALA   B O     1 
ATOM   14190 C  CB    . ALA   B  1 757  ? 11.977  33.993  55.429  1.00 18.08 ? 755  ALA   B CB    1 
ATOM   14191 N  N     . LEU   B  1 758  ? 14.634  32.273  56.741  1.00 16.21 ? 756  LEU   B N     1 
ATOM   14192 C  CA    . LEU   B  1 758  ? 15.210  31.850  58.018  1.00 17.68 ? 756  LEU   B CA    1 
ATOM   14193 C  C     . LEU   B  1 758  ? 16.410  30.974  57.700  1.00 19.98 ? 756  LEU   B C     1 
ATOM   14194 O  O     . LEU   B  1 758  ? 16.262  29.804  57.334  1.00 17.70 ? 756  LEU   B O     1 
ATOM   14195 C  CB    . LEU   B  1 758  ? 14.204  31.109  58.886  1.00 15.40 ? 756  LEU   B CB    1 
ATOM   14196 C  CG    . LEU   B  1 758  ? 14.819  30.543  60.166  1.00 16.81 ? 756  LEU   B CG    1 
ATOM   14197 C  CD1   . LEU   B  1 758  ? 15.425  31.658  61.002  1.00 17.41 ? 756  LEU   B CD1   1 
ATOM   14198 C  CD2   . LEU   B  1 758  ? 13.779  29.773  60.965  1.00 16.73 ? 756  LEU   B CD2   1 
ATOM   14199 N  N     . GLN   B  1 759  ? 17.594  31.548  57.816  1.00 16.06 ? 757  GLN   B N     1 
ATOM   14200 C  CA    . GLN   B  1 759  ? 18.822  30.810  57.593  1.00 16.02 ? 757  GLN   B CA    1 
ATOM   14201 C  C     . GLN   B  1 759  ? 19.527  30.622  58.925  1.00 17.75 ? 757  GLN   B C     1 
ATOM   14202 O  O     . GLN   B  1 759  ? 19.451  31.492  59.795  1.00 18.81 ? 757  GLN   B O     1 
ATOM   14203 C  CB    . GLN   B  1 759  ? 19.712  31.544  56.595  1.00 17.62 ? 757  GLN   B CB    1 
ATOM   14204 C  CG    . GLN   B  1 759  ? 19.074  31.636  55.223  1.00 14.91 ? 757  GLN   B CG    1 
ATOM   14205 C  CD    . GLN   B  1 759  ? 19.862  32.497  54.279  1.00 16.40 ? 757  GLN   B CD    1 
ATOM   14206 O  OE1   . GLN   B  1 759  ? 20.702  32.004  53.537  1.00 17.88 ? 757  GLN   B OE1   1 
ATOM   14207 N  NE2   . GLN   B  1 759  ? 19.605  33.793  54.307  1.00 17.63 ? 757  GLN   B NE2   1 
ATOM   14208 N  N     . LEU   B  1 760  ? 20.174  29.470  59.099  1.00 17.01 ? 758  LEU   B N     1 
ATOM   14209 C  CA    . LEU   B  1 760  ? 20.905  29.154  60.322  1.00 17.11 ? 758  LEU   B CA    1 
ATOM   14210 C  C     . LEU   B  1 760  ? 22.397  29.197  60.032  1.00 15.87 ? 758  LEU   B C     1 
ATOM   14211 O  O     . LEU   B  1 760  ? 22.859  28.543  59.098  1.00 18.51 ? 758  LEU   B O     1 
ATOM   14212 C  CB    . LEU   B  1 760  ? 20.524  27.770  60.854  1.00 16.72 ? 758  LEU   B CB    1 
ATOM   14213 C  CG    . LEU   B  1 760  ? 21.210  27.387  62.163  1.00 17.66 ? 758  LEU   B CG    1 
ATOM   14214 C  CD1   . LEU   B  1 760  ? 20.525  28.092  63.333  1.00 16.05 ? 758  LEU   B CD1   1 
ATOM   14215 C  CD2   . LEU   B  1 760  ? 21.194  25.871  62.353  1.00 18.25 ? 758  LEU   B CD2   1 
ATOM   14216 N  N     . LEU   B  1 761  ? 23.150  29.949  60.834  1.00 17.64 ? 759  LEU   B N     1 
ATOM   14217 C  CA    . LEU   B  1 761  ? 24.598  30.083  60.656  1.00 17.26 ? 759  LEU   B CA    1 
ATOM   14218 C  C     . LEU   B  1 761  ? 25.274  29.720  61.967  1.00 16.82 ? 759  LEU   B C     1 
ATOM   14219 O  O     . LEU   B  1 761  ? 25.587  30.601  62.777  1.00 19.85 ? 759  LEU   B O     1 
ATOM   14220 C  CB    . LEU   B  1 761  ? 25.000  31.497  60.232  1.00 16.78 ? 759  LEU   B CB    1 
ATOM   14221 C  CG    . LEU   B  1 761  ? 24.426  32.101  58.950  1.00 19.33 ? 759  LEU   B CG    1 
ATOM   14222 C  CD1   . LEU   B  1 761  ? 24.524  31.110  57.780  1.00 22.43 ? 759  LEU   B CD1   1 
ATOM   14223 C  CD2   . LEU   B  1 761  ? 22.998  32.583  59.153  1.00 17.10 ? 759  LEU   B CD2   1 
ATOM   14224 N  N     . PRO   B  1 762  ? 25.496  28.435  62.216  1.00 18.90 ? 760  PRO   B N     1 
ATOM   14225 C  CA    . PRO   B  1 762  ? 26.228  28.032  63.424  1.00 19.63 ? 760  PRO   B CA    1 
ATOM   14226 C  C     . PRO   B  1 762  ? 27.658  28.552  63.411  1.00 20.16 ? 760  PRO   B C     1 
ATOM   14227 O  O     . PRO   B  1 762  ? 28.269  28.734  62.356  1.00 20.27 ? 760  PRO   B O     1 
ATOM   14228 C  CB    . PRO   B  1 762  ? 26.206  26.497  63.361  1.00 18.72 ? 760  PRO   B CB    1 
ATOM   14229 C  CG    . PRO   B  1 762  ? 25.106  26.144  62.397  1.00 18.83 ? 760  PRO   B CG    1 
ATOM   14230 C  CD    . PRO   B  1 762  ? 25.103  27.280  61.391  1.00 18.21 ? 760  PRO   B CD    1 
ATOM   14231 N  N     . GLY   B  1 763  ? 28.204  28.767  64.596  1.00 21.14 ? 761  GLY   B N     1 
ATOM   14232 C  CA    . GLY   B  1 763  ? 29.610  29.102  64.712  1.00 20.86 ? 761  GLY   B CA    1 
ATOM   14233 C  C     . GLY   B  1 763  ? 29.863  29.988  65.916  1.00 22.20 ? 761  GLY   B C     1 
ATOM   14234 O  O     . GLY   B  1 763  ? 29.015  30.154  66.786  1.00 22.64 ? 761  GLY   B O     1 
ATOM   14235 N  N     . ASP   B  1 764  ? 31.050  30.573  65.934  1.00 25.61 ? 762  ASP   B N     1 
ATOM   14236 C  CA    . ASP   B  1 764  ? 31.494  31.345  67.078  1.00 23.13 ? 762  ASP   B CA    1 
ATOM   14237 C  C     . ASP   B  1 764  ? 31.223  32.832  66.833  1.00 26.98 ? 762  ASP   B C     1 
ATOM   14238 O  O     . ASP   B  1 764  ? 30.443  33.202  65.942  1.00 24.72 ? 762  ASP   B O     1 
ATOM   14239 C  CB    . ASP   B  1 764  ? 32.973  31.028  67.361  1.00 26.16 ? 762  ASP   B CB    1 
ATOM   14240 C  CG    . ASP   B  1 764  ? 33.894  31.428  66.218  1.00 32.13 ? 762  ASP   B CG    1 
ATOM   14241 O  OD1   . ASP   B  1 764  ? 33.440  32.117  65.285  1.00 30.51 ? 762  ASP   B OD1   1 
ATOM   14242 O  OD2   . ASP   B  1 764  ? 35.087  31.039  66.244  1.00 35.23 ? 762  ASP   B OD2   1 
ATOM   14243 N  N     . GLY   B  1 765  ? 31.869  33.698  67.618  1.00 26.80 ? 763  GLY   B N     1 
ATOM   14244 C  CA    . GLY   B  1 765  ? 31.616  35.119  67.493  1.00 30.45 ? 763  GLY   B CA    1 
ATOM   14245 C  C     . GLY   B  1 765  ? 32.092  35.711  66.187  1.00 26.79 ? 763  GLY   B C     1 
ATOM   14246 O  O     . GLY   B  1 765  ? 31.589  36.759  65.778  1.00 29.73 ? 763  GLY   B O     1 
ATOM   14247 N  N     . ARG   B  1 766  ? 33.059  35.072  65.529  1.00 26.08 ? 764  ARG   B N     1 
ATOM   14248 C  CA    . ARG   B  1 766  ? 33.482  35.543  64.218  1.00 27.51 ? 764  ARG   B CA    1 
ATOM   14249 C  C     . ARG   B  1 766  ? 32.342  35.436  63.213  1.00 28.33 ? 764  ARG   B C     1 
ATOM   14250 O  O     . ARG   B  1 766  ? 32.205  36.282  62.323  1.00 24.20 ? 764  ARG   B O     1 
ATOM   14251 C  CB    . ARG   B  1 766  ? 34.700  34.750  63.743  1.00 32.05 ? 764  ARG   B CB    1 
ATOM   14252 N  N     . VAL   B  1 767  ? 31.513  34.401  63.342  1.00 26.64 ? 765  VAL   B N     1 
ATOM   14253 C  CA    . VAL   B  1 767  ? 30.352  34.281  62.468  1.00 22.62 ? 765  VAL   B CA    1 
ATOM   14254 C  C     . VAL   B  1 767  ? 29.359  35.388  62.766  1.00 23.78 ? 765  VAL   B C     1 
ATOM   14255 O  O     . VAL   B  1 767  ? 28.826  36.029  61.852  1.00 23.11 ? 765  VAL   B O     1 
ATOM   14256 C  CB    . VAL   B  1 767  ? 29.707  32.895  62.614  1.00 21.73 ? 765  VAL   B CB    1 
ATOM   14257 C  CG1   . VAL   B  1 767  ? 28.489  32.794  61.694  1.00 20.83 ? 765  VAL   B CG1   1 
ATOM   14258 C  CG2   . VAL   B  1 767  ? 30.725  31.815  62.275  1.00 20.93 ? 765  VAL   B CG2   1 
ATOM   14259 N  N     . GLY   B  1 768  ? 29.085  35.625  64.051  1.00 20.38 ? 766  GLY   B N     1 
ATOM   14260 C  CA    . GLY   B  1 768  ? 28.195  36.714  64.400  1.00 23.68 ? 766  GLY   B CA    1 
ATOM   14261 C  C     . GLY   B  1 768  ? 28.717  38.046  63.904  1.00 20.57 ? 766  GLY   B C     1 
ATOM   14262 O  O     . GLY   B  1 768  ? 27.958  38.874  63.394  1.00 19.96 ? 766  GLY   B O     1 
ATOM   14263 N  N     . ALA   B  1 769  ? 30.026  38.263  64.033  1.00 23.90 ? 767  ALA   B N     1 
ATOM   14264 C  CA    . ALA   B  1 769  ? 30.615  39.525  63.600  1.00 23.20 ? 767  ALA   B CA    1 
ATOM   14265 C  C     . ALA   B  1 769  ? 30.466  39.718  62.094  1.00 24.80 ? 767  ALA   B C     1 
ATOM   14266 O  O     . ALA   B  1 769  ? 30.150  40.822  61.627  1.00 21.17 ? 767  ALA   B O     1 
ATOM   14267 C  CB    . ALA   B  1 769  ? 32.087  39.568  64.005  1.00 26.11 ? 767  ALA   B CB    1 
ATOM   14268 N  N     . ALA   B  1 770  ? 30.690  38.653  61.323  1.00 20.42 ? 768  ALA   B N     1 
ATOM   14269 C  CA    . ALA   B  1 770  ? 30.515  38.729  59.879  1.00 22.66 ? 768  ALA   B CA    1 
ATOM   14270 C  C     . ALA   B  1 770  ? 29.073  39.059  59.502  1.00 23.34 ? 768  ALA   B C     1 
ATOM   14271 O  O     . ALA   B  1 770  ? 28.828  39.806  58.545  1.00 20.53 ? 768  ALA   B O     1 
ATOM   14272 C  CB    . ALA   B  1 770  ? 30.962  37.414  59.236  1.00 24.05 ? 768  ALA   B CB    1 
ATOM   14273 N  N     . LEU   B  1 771  ? 28.098  38.504  60.228  1.00 19.99 ? 769  LEU   B N     1 
ATOM   14274 C  CA    . LEU   B  1 771  ? 26.710  38.810  59.902  1.00 19.81 ? 769  LEU   B CA    1 
ATOM   14275 C  C     . LEU   B  1 771  ? 26.372  40.258  60.229  1.00 22.12 ? 769  LEU   B C     1 
ATOM   14276 O  O     . LEU   B  1 771  ? 25.732  40.952  59.431  1.00 20.66 ? 769  LEU   B O     1 
ATOM   14277 C  CB    . LEU   B  1 771  ? 25.771  37.867  60.651  1.00 20.87 ? 769  LEU   B CB    1 
ATOM   14278 C  CG    . LEU   B  1 771  ? 25.894  36.399  60.255  1.00 20.17 ? 769  LEU   B CG    1 
ATOM   14279 C  CD1   . LEU   B  1 771  ? 25.163  35.550  61.301  1.00 18.51 ? 769  LEU   B CD1   1 
ATOM   14280 C  CD2   . LEU   B  1 771  ? 25.306  36.158  58.877  1.00 19.30 ? 769  LEU   B CD2   1 
ATOM   14281 N  N     . VAL   B  1 772  ? 26.791  40.726  61.403  1.00 19.07 ? 770  VAL   B N     1 
ATOM   14282 C  CA    . VAL   B  1 772  ? 26.488  42.092  61.819  1.00 20.54 ? 770  VAL   B CA    1 
ATOM   14283 C  C     . VAL   B  1 772  ? 27.069  43.101  60.840  1.00 22.02 ? 770  VAL   B C     1 
ATOM   14284 O  O     . VAL   B  1 772  ? 26.430  44.108  60.515  1.00 20.54 ? 770  VAL   B O     1 
ATOM   14285 C  CB    . VAL   B  1 772  ? 27.017  42.323  63.242  1.00 20.70 ? 770  VAL   B CB    1 
ATOM   14286 C  CG1   . VAL   B  1 772  ? 27.072  43.800  63.554  1.00 20.91 ? 770  VAL   B CG1   1 
ATOM   14287 C  CG2   . VAL   B  1 772  ? 26.136  41.565  64.255  1.00 21.62 ? 770  VAL   B CG2   1 
ATOM   14288 N  N     . ALA   B  1 773  ? 28.297  42.857  60.373  1.00 23.11 ? 771  ALA   B N     1 
ATOM   14289 C  CA    . ALA   B  1 773  ? 29.009  43.780  59.498  1.00 24.57 ? 771  ALA   B CA    1 
ATOM   14290 C  C     . ALA   B  1 773  ? 28.522  43.739  58.057  1.00 29.77 ? 771  ALA   B C     1 
ATOM   14291 O  O     . ALA   B  1 773  ? 28.900  44.614  57.267  1.00 26.66 ? 771  ALA   B O     1 
ATOM   14292 C  CB    . ALA   B  1 773  ? 30.508  43.472  59.534  1.00 25.67 ? 771  ALA   B CB    1 
ATOM   14293 N  N     . ALA   B  1 774  ? 27.705  42.751  57.696  1.00 24.28 ? 772  ALA   B N     1 
ATOM   14294 C  CA    . ALA   B  1 774  ? 27.285  42.595  56.310  1.00 25.14 ? 772  ALA   B CA    1 
ATOM   14295 C  C     . ALA   B  1 774  ? 26.494  43.807  55.836  1.00 23.95 ? 772  ALA   B C     1 
ATOM   14296 O  O     . ALA   B  1 774  ? 25.696  44.387  56.577  1.00 22.80 ? 772  ALA   B O     1 
ATOM   14297 C  CB    . ALA   B  1 774  ? 26.454  41.324  56.143  1.00 24.54 ? 772  ALA   B CB    1 
ATOM   14298 N  N     . ALA   B  1 775  ? 26.721  44.172  54.572  1.00 25.47 ? 773  ALA   B N     1 
ATOM   14299 C  CA    . ALA   B  1 775  ? 26.165  45.400  54.012  1.00 29.49 ? 773  ALA   B CA    1 
ATOM   14300 C  C     . ALA   B  1 775  ? 24.646  45.454  54.132  1.00 26.26 ? 773  ALA   B C     1 
ATOM   14301 O  O     . ALA   B  1 775  ? 24.081  46.511  54.431  1.00 28.07 ? 773  ALA   B O     1 
ATOM   14302 C  CB    . ALA   B  1 775  ? 26.585  45.531  52.548  1.00 30.40 ? 773  ALA   B CB    1 
ATOM   14303 N  N     . GLU   B  1 776  ? 23.966  44.334  53.898  1.00 24.37 ? 774  GLU   B N     1 
ATOM   14304 C  CA    . GLU   B  1 776  ? 22.509  44.331  53.844  1.00 23.23 ? 774  GLU   B CA    1 
ATOM   14305 C  C     . GLU   B  1 776  ? 21.857  44.099  55.199  1.00 21.90 ? 774  GLU   B C     1 
ATOM   14306 O  O     . GLU   B  1 776  ? 20.627  44.062  55.277  1.00 21.04 ? 774  GLU   B O     1 
ATOM   14307 C  CB    . GLU   B  1 776  ? 22.014  43.265  52.862  1.00 24.13 ? 774  GLU   B CB    1 
ATOM   14308 C  CG    . GLU   B  1 776  ? 22.603  43.345  51.452  1.00 27.29 ? 774  GLU   B CG    1 
ATOM   14309 C  CD    . GLU   B  1 776  ? 23.950  42.640  51.304  1.00 33.34 ? 774  GLU   B CD    1 
ATOM   14310 O  OE1   . GLU   B  1 776  ? 24.557  42.208  52.317  1.00 28.93 ? 774  GLU   B OE1   1 
ATOM   14311 O  OE2   . GLU   B  1 776  ? 24.415  42.525  50.155  1.00 39.31 ? 774  GLU   B OE2   1 
ATOM   14312 N  N     . THR   B  1 777  ? 22.634  43.936  56.265  1.00 21.22 ? 775  THR   B N     1 
ATOM   14313 C  CA    . THR   B  1 777  ? 22.033  43.745  57.580  1.00 20.74 ? 775  THR   B CA    1 
ATOM   14314 C  C     . THR   B  1 777  ? 21.286  45.005  57.999  1.00 22.28 ? 775  THR   B C     1 
ATOM   14315 O  O     . THR   B  1 777  ? 21.844  46.110  57.984  1.00 19.25 ? 775  THR   B O     1 
ATOM   14316 C  CB    . THR   B  1 777  ? 23.112  43.383  58.598  1.00 19.72 ? 775  THR   B CB    1 
ATOM   14317 O  OG1   . THR   B  1 777  ? 23.600  42.071  58.294  1.00 19.97 ? 775  THR   B OG1   1 
ATOM   14318 C  CG2   . THR   B  1 777  ? 22.560  43.417  60.037  1.00 19.61 ? 775  THR   B CG2   1 
ATOM   14319 N  N     . ALA   B  1 778  ? 20.012  44.837  58.352  1.00 19.26 ? 776  ALA   B N     1 
ATOM   14320 C  CA    . ALA   B  1 778  ? 19.110  45.954  58.599  1.00 21.99 ? 776  ALA   B CA    1 
ATOM   14321 C  C     . ALA   B  1 778  ? 18.713  46.072  60.061  1.00 20.86 ? 776  ALA   B C     1 
ATOM   14322 O  O     . ALA   B  1 778  ? 18.017  47.023  60.430  1.00 20.74 ? 776  ALA   B O     1 
ATOM   14323 C  CB    . ALA   B  1 778  ? 17.850  45.814  57.739  1.00 21.60 ? 776  ALA   B CB    1 
ATOM   14324 N  N     . GLY   B  1 779  ? 19.126  45.126  60.886  1.00 19.85 ? 777  GLY   B N     1 
ATOM   14325 C  CA    . GLY   B  1 779  ? 18.837  45.168  62.302  1.00 19.30 ? 777  GLY   B CA    1 
ATOM   14326 C  C     . GLY   B  1 779  ? 19.508  43.981  62.951  1.00 18.05 ? 777  GLY   B C     1 
ATOM   14327 O  O     . GLY   B  1 779  ? 19.824  42.984  62.297  1.00 18.50 ? 777  GLY   B O     1 
ATOM   14328 N  N     . VAL   B  1 780  ? 19.768  44.121  64.243  1.00 15.89 ? 778  VAL   B N     1 
ATOM   14329 C  CA    . VAL   B  1 780  ? 20.428  43.062  64.995  1.00 17.33 ? 778  VAL   B CA    1 
ATOM   14330 C  C     . VAL   B  1 780  ? 19.672  42.877  66.294  1.00 19.02 ? 778  VAL   B C     1 
ATOM   14331 O  O     . VAL   B  1 780  ? 19.319  43.856  66.961  1.00 18.84 ? 778  VAL   B O     1 
ATOM   14332 C  CB    . VAL   B  1 780  ? 21.914  43.364  65.277  1.00 18.17 ? 778  VAL   B CB    1 
ATOM   14333 C  CG1   . VAL   B  1 780  ? 22.524  42.279  66.184  1.00 17.91 ? 778  VAL   B CG1   1 
ATOM   14334 C  CG2   . VAL   B  1 780  ? 22.725  43.484  63.966  1.00 18.31 ? 778  VAL   B CG2   1 
ATOM   14335 N  N     . MET   B  1 781  ? 19.398  41.630  66.630  1.00 17.49 ? 779  MET   B N     1 
ATOM   14336 C  CA    . MET   B  1 781  ? 18.816  41.269  67.912  1.00 19.09 ? 779  MET   B CA    1 
ATOM   14337 C  C     . MET   B  1 781  ? 19.846  40.414  68.615  1.00 19.56 ? 779  MET   B C     1 
ATOM   14338 O  O     . MET   B  1 781  ? 20.255  39.372  68.089  1.00 21.27 ? 779  MET   B O     1 
ATOM   14339 C  CB    . MET   B  1 781  ? 17.493  40.530  67.733  1.00 17.30 ? 779  MET   B CB    1 
ATOM   14340 C  CG    . MET   B  1 781  ? 16.516  41.317  66.891  1.00 17.33 ? 779  MET   B CG    1 
ATOM   14341 S  SD    . MET   B  1 781  ? 15.050  40.372  66.541  1.00 20.35 ? 779  MET   B SD    1 
ATOM   14342 C  CE    . MET   B  1 781  ? 14.152  40.536  68.085  1.00 18.75 ? 779  MET   B CE    1 
ATOM   14343 N  N     . PHE   B  1 782  ? 20.309  40.883  69.765  1.00 17.63 ? 780  PHE   B N     1 
ATOM   14344 C  CA    . PHE   B  1 782  ? 21.415  40.250  70.452  1.00 16.79 ? 780  PHE   B CA    1 
ATOM   14345 C  C     . PHE   B  1 782  ? 21.038  40.014  71.904  1.00 20.78 ? 780  PHE   B C     1 
ATOM   14346 O  O     . PHE   B  1 782  ? 20.520  40.915  72.560  1.00 19.04 ? 780  PHE   B O     1 
ATOM   14347 C  CB    . PHE   B  1 782  ? 22.676  41.125  70.384  1.00 18.97 ? 780  PHE   B CB    1 
ATOM   14348 C  CG    . PHE   B  1 782  ? 23.788  40.609  71.232  1.00 21.75 ? 780  PHE   B CG    1 
ATOM   14349 C  CD1   . PHE   B  1 782  ? 24.574  39.558  70.781  1.00 19.23 ? 780  PHE   B CD1   1 
ATOM   14350 C  CD2   . PHE   B  1 782  ? 24.032  41.143  72.501  1.00 19.35 ? 780  PHE   B CD2   1 
ATOM   14351 C  CE1   . PHE   B  1 782  ? 25.595  39.052  71.564  1.00 21.49 ? 780  PHE   B CE1   1 
ATOM   14352 C  CE2   . PHE   B  1 782  ? 25.051  40.639  73.290  1.00 19.09 ? 780  PHE   B CE2   1 
ATOM   14353 C  CZ    . PHE   B  1 782  ? 25.838  39.599  72.820  1.00 20.32 ? 780  PHE   B CZ    1 
ATOM   14354 N  N     . THR   B  1 783  ? 21.329  38.817  72.407  1.00 19.02 ? 781  THR   B N     1 
ATOM   14355 C  CA    . THR   B  1 783  ? 21.232  38.525  73.830  1.00 20.44 ? 781  THR   B CA    1 
ATOM   14356 C  C     . THR   B  1 783  ? 22.530  37.857  74.237  1.00 20.03 ? 781  THR   B C     1 
ATOM   14357 O  O     . THR   B  1 783  ? 22.936  36.861  73.631  1.00 21.88 ? 781  THR   B O     1 
ATOM   14358 C  CB    . THR   B  1 783  ? 20.022  37.634  74.160  1.00 19.14 ? 781  THR   B CB    1 
ATOM   14359 O  OG1   . THR   B  1 783  ? 18.819  38.290  73.750  1.00 19.43 ? 781  THR   B OG1   1 
ATOM   14360 C  CG2   . THR   B  1 783  ? 19.937  37.403  75.662  1.00 21.69 ? 781  THR   B CG2   1 
ATOM   14361 N  N     . GLY   B  1 784  ? 23.196  38.425  75.231  1.00 20.68 ? 782  GLY   B N     1 
ATOM   14362 C  CA    . GLY   B  1 784  ? 24.497  37.944  75.633  1.00 20.21 ? 782  GLY   B CA    1 
ATOM   14363 C  C     . GLY   B  1 784  ? 25.194  39.005  76.468  1.00 20.05 ? 782  GLY   B C     1 
ATOM   14364 O  O     . GLY   B  1 784  ? 24.544  39.825  77.113  1.00 21.69 ? 782  GLY   B O     1 
ATOM   14365 N  N     . SER   B  1 785  ? 26.518  38.987  76.405  1.00 21.59 ? 783  SER   B N     1 
ATOM   14366 C  CA    . SER   B  1 785  ? 27.317  39.820  77.298  1.00 24.87 ? 783  SER   B CA    1 
ATOM   14367 C  C     . SER   B  1 785  ? 27.239  41.296  76.911  1.00 27.86 ? 783  SER   B C     1 
ATOM   14368 O  O     . SER   B  1 785  ? 27.049  41.656  75.745  1.00 21.47 ? 783  SER   B O     1 
ATOM   14369 C  CB    . SER   B  1 785  ? 28.768  39.368  77.280  1.00 21.79 ? 783  SER   B CB    1 
ATOM   14370 O  OG    . SER   B  1 785  ? 29.356  39.666  76.034  1.00 25.84 ? 783  SER   B OG    1 
ATOM   14371 N  N     . THR   B  1 786  ? 27.402  42.162  77.913  1.00 25.87 ? 784  THR   B N     1 
ATOM   14372 C  CA    . THR   B  1 786  ? 27.445  43.593  77.633  1.00 25.41 ? 784  THR   B CA    1 
ATOM   14373 C  C     . THR   B  1 786  ? 28.603  43.926  76.707  1.00 24.29 ? 784  THR   B C     1 
ATOM   14374 O  O     . THR   B  1 786  ? 28.470  44.776  75.820  1.00 23.89 ? 784  THR   B O     1 
ATOM   14375 C  CB    . THR   B  1 786  ? 27.565  44.399  78.934  1.00 28.25 ? 784  THR   B CB    1 
ATOM   14376 O  OG1   . THR   B  1 786  ? 28.766  44.021  79.621  1.00 37.08 ? 784  THR   B OG1   1 
ATOM   14377 C  CG2   . THR   B  1 786  ? 26.391  44.149  79.838  1.00 26.78 ? 784  THR   B CG2   1 
ATOM   14378 N  N     . GLU   B  1 787  ? 29.754  43.269  76.906  1.00 21.60 ? 785  GLU   B N     1 
ATOM   14379 C  CA    . GLU   B  1 787  ? 30.933  43.573  76.109  1.00 24.78 ? 785  GLU   B CA    1 
ATOM   14380 C  C     . GLU   B  1 787  ? 30.673  43.344  74.625  1.00 25.16 ? 785  GLU   B C     1 
ATOM   14381 O  O     . GLU   B  1 787  ? 31.038  44.176  73.785  1.00 23.44 ? 785  GLU   B O     1 
ATOM   14382 C  CB    . GLU   B  1 787  ? 32.122  42.727  76.578  1.00 31.54 ? 785  GLU   B CB    1 
ATOM   14383 N  N     . VAL   B  1 788  ? 30.068  42.203  74.282  1.00 21.74 ? 786  VAL   B N     1 
ATOM   14384 C  CA    . VAL   B  1 788  ? 29.809  41.909  72.876  1.00 22.55 ? 786  VAL   B CA    1 
ATOM   14385 C  C     . VAL   B  1 788  ? 28.748  42.848  72.326  1.00 21.70 ? 786  VAL   B C     1 
ATOM   14386 O  O     . VAL   B  1 788  ? 28.837  43.299  71.177  1.00 23.23 ? 786  VAL   B O     1 
ATOM   14387 C  CB    . VAL   B  1 788  ? 29.417  40.430  72.704  1.00 24.45 ? 786  VAL   B CB    1 
ATOM   14388 C  CG1   . VAL   B  1 788  ? 28.933  40.155  71.286  1.00 24.95 ? 786  VAL   B CG1   1 
ATOM   14389 C  CG2   . VAL   B  1 788  ? 30.615  39.537  73.032  1.00 24.21 ? 786  VAL   B CG2   1 
ATOM   14390 N  N     . ALA   B  1 789  ? 27.730  43.167  73.138  1.00 20.76 ? 787  ALA   B N     1 
ATOM   14391 C  CA    . ALA   B  1 789  ? 26.719  44.127  72.705  1.00 20.00 ? 787  ALA   B CA    1 
ATOM   14392 C  C     . ALA   B  1 789  ? 27.360  45.444  72.294  1.00 20.78 ? 787  ALA   B C     1 
ATOM   14393 O  O     . ALA   B  1 789  ? 26.977  46.039  71.283  1.00 18.46 ? 787  ALA   B O     1 
ATOM   14394 C  CB    . ALA   B  1 789  ? 25.694  44.361  73.813  1.00 19.41 ? 787  ALA   B CB    1 
ATOM   14395 N  N     . ARG   B  1 790  ? 28.334  45.921  73.075  1.00 22.04 ? 788  ARG   B N     1 
ATOM   14396 C  CA    . ARG   B  1 790  ? 29.021  47.162  72.719  1.00 21.42 ? 788  ARG   B CA    1 
ATOM   14397 C  C     . ARG   B  1 790  ? 29.776  47.012  71.409  1.00 22.49 ? 788  ARG   B C     1 
ATOM   14398 O  O     . ARG   B  1 790  ? 29.812  47.941  70.593  1.00 24.26 ? 788  ARG   B O     1 
ATOM   14399 C  CB    . ARG   B  1 790  ? 29.988  47.587  73.829  1.00 22.99 ? 788  ARG   B CB    1 
ATOM   14400 C  CG    . ARG   B  1 790  ? 29.373  47.834  75.184  1.00 28.88 ? 788  ARG   B CG    1 
ATOM   14401 C  CD    . ARG   B  1 790  ? 28.159  48.751  75.126  1.00 35.08 ? 788  ARG   B CD    1 
ATOM   14402 N  NE    . ARG   B  1 790  ? 28.396  50.017  74.439  1.00 36.80 ? 788  ARG   B NE    1 
ATOM   14403 C  CZ    . ARG   B  1 790  ? 28.697  51.158  75.045  1.00 34.68 ? 788  ARG   B CZ    1 
ATOM   14404 N  NH1   . ARG   B  1 790  ? 28.797  51.236  76.362  1.00 34.49 ? 788  ARG   B NH1   1 
ATOM   14405 N  NH2   . ARG   B  1 790  ? 28.913  52.246  74.309  1.00 33.02 ? 788  ARG   B NH2   1 
ATOM   14406 N  N     . LEU   B  1 791  ? 30.396  45.854  71.189  1.00 19.34 ? 789  LEU   B N     1 
ATOM   14407 C  CA    . LEU   B  1 791  ? 31.137  45.655  69.949  1.00 22.59 ? 789  LEU   B CA    1 
ATOM   14408 C  C     . LEU   B  1 791  ? 30.202  45.684  68.753  1.00 23.16 ? 789  LEU   B C     1 
ATOM   14409 O  O     . LEU   B  1 791  ? 30.535  46.240  67.700  1.00 21.86 ? 789  LEU   B O     1 
ATOM   14410 C  CB    . LEU   B  1 791  ? 31.890  44.329  69.997  1.00 21.31 ? 789  LEU   B CB    1 
ATOM   14411 C  CG    . LEU   B  1 791  ? 33.020  44.229  71.017  1.00 27.33 ? 789  LEU   B CG    1 
ATOM   14412 C  CD1   . LEU   B  1 791  ? 33.584  42.839  70.983  1.00 29.44 ? 789  LEU   B CD1   1 
ATOM   14413 C  CD2   . LEU   B  1 791  ? 34.104  45.261  70.714  1.00 30.95 ? 789  LEU   B CD2   1 
ATOM   14414 N  N     . ILE   B  1 792  ? 29.029  45.076  68.901  1.00 22.11 ? 790  ILE   B N     1 
ATOM   14415 C  CA    . ILE   B  1 792  ? 28.037  45.070  67.833  1.00 20.90 ? 790  ILE   B CA    1 
ATOM   14416 C  C     . ILE   B  1 792  ? 27.548  46.482  67.567  1.00 23.16 ? 790  ILE   B C     1 
ATOM   14417 O  O     . ILE   B  1 792  ? 27.426  46.913  66.415  1.00 24.57 ? 790  ILE   B O     1 
ATOM   14418 C  CB    . ILE   B  1 792  ? 26.873  44.135  68.209  1.00 18.13 ? 790  ILE   B CB    1 
ATOM   14419 C  CG1   . ILE   B  1 792  ? 27.334  42.683  68.162  1.00 19.13 ? 790  ILE   B CG1   1 
ATOM   14420 C  CG2   . ILE   B  1 792  ? 25.682  44.369  67.309  1.00 19.27 ? 790  ILE   B CG2   1 
ATOM   14421 C  CD1   . ILE   B  1 792  ? 26.360  41.713  68.783  1.00 20.84 ? 790  ILE   B CD1   1 
ATOM   14422 N  N     . GLN   B  1 793  ? 27.229  47.207  68.640  1.00 19.09 ? 791  GLN   B N     1 
ATOM   14423 C  CA    . GLN   B  1 793  ? 26.811  48.593  68.521  1.00 23.25 ? 791  GLN   B CA    1 
ATOM   14424 C  C     . GLN   B  1 793  ? 27.838  49.412  67.750  1.00 21.94 ? 791  GLN   B C     1 
ATOM   14425 O  O     . GLN   B  1 793  ? 27.478  50.207  66.876  1.00 22.62 ? 791  GLN   B O     1 
ATOM   14426 C  CB    . GLN   B  1 793  ? 26.596  49.172  69.922  1.00 24.07 ? 791  GLN   B CB    1 
ATOM   14427 C  CG    . GLN   B  1 793  ? 26.213  50.632  69.962  1.00 24.88 ? 791  GLN   B CG    1 
ATOM   14428 C  CD    . GLN   B  1 793  ? 26.552  51.259  71.300  1.00 28.62 ? 791  GLN   B CD    1 
ATOM   14429 O  OE1   . GLN   B  1 793  ? 27.618  50.991  71.873  1.00 27.78 ? 791  GLN   B OE1   1 
ATOM   14430 N  NE2   . GLN   B  1 793  ? 25.642  52.084  71.817  1.00 30.53 ? 791  GLN   B NE2   1 
ATOM   14431 N  N     . ALA   B  1 794  ? 29.126  49.221  68.052  1.00 20.55 ? 792  ALA   B N     1 
ATOM   14432 C  CA    . ALA   B  1 794  ? 30.158  49.984  67.360  1.00 26.22 ? 792  ALA   B CA    1 
ATOM   14433 C  C     . ALA   B  1 794  ? 30.223  49.605  65.889  1.00 28.45 ? 792  ALA   B C     1 
ATOM   14434 O  O     . ALA   B  1 794  ? 30.398  50.472  65.025  1.00 23.98 ? 792  ALA   B O     1 
ATOM   14435 C  CB    . ALA   B  1 794  ? 31.518  49.762  68.023  1.00 25.93 ? 792  ALA   B CB    1 
ATOM   14436 N  N     . GLN   B  1 795  ? 30.076  48.316  65.582  1.00 25.23 ? 793  GLN   B N     1 
ATOM   14437 C  CA    . GLN   B  1 795  ? 30.090  47.905  64.182  1.00 23.39 ? 793  GLN   B CA    1 
ATOM   14438 C  C     . GLN   B  1 795  ? 28.915  48.511  63.423  1.00 23.79 ? 793  GLN   B C     1 
ATOM   14439 O  O     . GLN   B  1 795  ? 29.078  48.986  62.292  1.00 25.10 ? 793  GLN   B O     1 
ATOM   14440 C  CB    . GLN   B  1 795  ? 30.068  46.379  64.080  1.00 27.02 ? 793  GLN   B CB    1 
ATOM   14441 C  CG    . GLN   B  1 795  ? 30.085  45.887  62.631  1.00 32.50 ? 793  GLN   B CG    1 
ATOM   14442 C  CD    . GLN   B  1 795  ? 31.386  46.241  61.920  1.00 37.60 ? 793  GLN   B CD    1 
ATOM   14443 O  OE1   . GLN   B  1 795  ? 31.389  46.922  60.889  1.00 40.52 ? 793  GLN   B OE1   1 
ATOM   14444 N  NE2   . GLN   B  1 795  ? 32.499  45.781  62.474  1.00 39.55 ? 793  GLN   B NE2   1 
ATOM   14445 N  N     . LEU   B  1 796  ? 27.718  48.494  64.030  1.00 20.53 ? 794  LEU   B N     1 
ATOM   14446 C  CA    . LEU   B  1 796  ? 26.521  48.995  63.359  1.00 23.60 ? 794  LEU   B CA    1 
ATOM   14447 C  C     . LEU   B  1 796  ? 26.569  50.503  63.165  1.00 26.17 ? 794  LEU   B C     1 
ATOM   14448 O  O     . LEU   B  1 796  ? 26.018  51.014  62.184  1.00 25.91 ? 794  LEU   B O     1 
ATOM   14449 C  CB    . LEU   B  1 796  ? 25.268  48.628  64.151  1.00 21.37 ? 794  LEU   B CB    1 
ATOM   14450 C  CG    . LEU   B  1 796  ? 24.882  47.150  64.215  1.00 20.66 ? 794  LEU   B CG    1 
ATOM   14451 C  CD1   . LEU   B  1 796  ? 23.633  46.945  65.075  1.00 20.95 ? 794  LEU   B CD1   1 
ATOM   14452 C  CD2   . LEU   B  1 796  ? 24.673  46.608  62.800  1.00 20.26 ? 794  LEU   B CD2   1 
ATOM   14453 N  N     . ALA   B  1 797  ? 27.214  51.222  64.089  1.00 23.46 ? 795  ALA   B N     1 
ATOM   14454 C  CA    . ALA   B  1 797  ? 27.297  52.676  64.014  1.00 27.81 ? 795  ALA   B CA    1 
ATOM   14455 C  C     . ALA   B  1 797  ? 28.084  53.149  62.803  1.00 26.39 ? 795  ALA   B C     1 
ATOM   14456 O  O     . ALA   B  1 797  ? 28.023  54.333  62.462  1.00 30.54 ? 795  ALA   B O     1 
ATOM   14457 C  CB    . ALA   B  1 797  ? 27.944  53.235  65.284  1.00 29.54 ? 795  ALA   B CB    1 
ATOM   14458 N  N     . ASP   B  1 798  ? 28.828  52.258  62.155  1.00 28.37 ? 796  ASP   B N     1 
ATOM   14459 C  CA    . ASP   B  1 798  ? 29.548  52.630  60.947  1.00 28.51 ? 796  ASP   B CA    1 
ATOM   14460 C  C     . ASP   B  1 798  ? 28.626  52.761  59.740  1.00 30.72 ? 796  ASP   B C     1 
ATOM   14461 O  O     . ASP   B  1 798  ? 29.014  53.382  58.744  1.00 35.02 ? 796  ASP   B O     1 
ATOM   14462 C  CB    . ASP   B  1 798  ? 30.634  51.595  60.667  1.00 30.91 ? 796  ASP   B CB    1 
ATOM   14463 C  CG    . ASP   B  1 798  ? 31.682  52.094  59.696  1.00 42.34 ? 796  ASP   B CG    1 
ATOM   14464 O  OD1   . ASP   B  1 798  ? 32.130  53.251  59.848  1.00 43.56 ? 796  ASP   B OD1   1 
ATOM   14465 O  OD2   . ASP   B  1 798  ? 32.066  51.321  58.791  1.00 41.73 ? 796  ASP   B OD2   1 
ATOM   14466 N  N     . ARG   B  1 799  ? 27.421  52.208  59.810  1.00 29.44 ? 797  ARG   B N     1 
ATOM   14467 C  CA    . ARG   B  1 799  ? 26.525  52.118  58.667  1.00 30.01 ? 797  ARG   B CA    1 
ATOM   14468 C  C     . ARG   B  1 799  ? 25.194  52.793  58.959  1.00 28.42 ? 797  ARG   B C     1 
ATOM   14469 O  O     . ARG   B  1 799  ? 24.852  53.096  60.103  1.00 26.90 ? 797  ARG   B O     1 
ATOM   14470 C  CB    . ARG   B  1 799  ? 26.277  50.659  58.274  1.00 32.10 ? 797  ARG   B CB    1 
ATOM   14471 C  CG    . ARG   B  1 799  ? 27.293  50.117  57.294  1.00 40.08 ? 797  ARG   B CG    1 
ATOM   14472 C  CD    . ARG   B  1 799  ? 26.892  48.750  56.796  1.00 42.62 ? 797  ARG   B CD    1 
ATOM   14473 N  NE    . ARG   B  1 799  ? 27.059  47.739  57.830  1.00 42.91 ? 797  ARG   B NE    1 
ATOM   14474 C  CZ    . ARG   B  1 799  ? 26.068  47.117  58.454  1.00 36.45 ? 797  ARG   B CZ    1 
ATOM   14475 N  NH1   . ARG   B  1 799  ? 24.794  47.361  58.161  1.00 33.52 ? 797  ARG   B NH1   1 
ATOM   14476 N  NH2   . ARG   B  1 799  ? 26.362  46.226  59.395  1.00 33.09 ? 797  ARG   B NH2   1 
ATOM   14477 N  N     . LEU   B  1 800  ? 24.439  53.011  57.890  1.00 26.62 ? 798  LEU   B N     1 
ATOM   14478 C  CA    . LEU   B  1 800  ? 23.071  53.489  57.979  1.00 27.75 ? 798  LEU   B CA    1 
ATOM   14479 C  C     . LEU   B  1 800  ? 22.166  52.556  57.190  1.00 28.59 ? 798  LEU   B C     1 
ATOM   14480 O  O     . LEU   B  1 800  ? 22.614  51.839  56.289  1.00 30.61 ? 798  LEU   B O     1 
ATOM   14481 C  CB    . LEU   B  1 800  ? 22.930  54.918  57.452  1.00 29.69 ? 798  LEU   B CB    1 
ATOM   14482 C  CG    . LEU   B  1 800  ? 23.599  56.014  58.271  1.00 28.70 ? 798  LEU   B CG    1 
ATOM   14483 C  CD1   . LEU   B  1 800  ? 23.457  57.341  57.544  1.00 30.14 ? 798  LEU   B CD1   1 
ATOM   14484 C  CD2   . LEU   B  1 800  ? 22.945  56.065  59.631  1.00 24.28 ? 798  LEU   B CD2   1 
ATOM   14485 N  N     . SER   B  1 801  ? 20.878  52.568  57.556  1.00 27.86 ? 799  SER   B N     1 
ATOM   14486 C  CA    . SER   B  1 801  ? 19.836  51.822  56.861  1.00 29.26 ? 799  SER   B CA    1 
ATOM   14487 C  C     . SER   B  1 801  ? 19.715  52.319  55.426  1.00 37.60 ? 799  SER   B C     1 
ATOM   14488 O  O     . SER   B  1 801  ? 20.275  53.371  55.090  1.00 31.11 ? 799  SER   B O     1 
ATOM   14489 C  CB    . SER   B  1 801  ? 18.499  51.969  57.587  1.00 32.17 ? 799  SER   B CB    1 
ATOM   14490 O  OG    . SER   B  1 801  ? 17.958  53.271  57.418  1.00 31.41 ? 799  SER   B OG    1 
ATOM   14491 N  N     . PRO   B  1 802  ? 19.019  51.590  54.546  1.00 35.70 ? 800  PRO   B N     1 
ATOM   14492 C  CA    . PRO   B  1 802  ? 18.717  52.153  53.219  1.00 38.76 ? 800  PRO   B CA    1 
ATOM   14493 C  C     . PRO   B  1 802  ? 18.092  53.536  53.295  1.00 39.46 ? 800  PRO   B C     1 
ATOM   14494 O  O     . PRO   B  1 802  ? 18.382  54.397  52.454  1.00 41.08 ? 800  PRO   B O     1 
ATOM   14495 C  CB    . PRO   B  1 802  ? 17.750  51.123  52.622  1.00 42.51 ? 800  PRO   B CB    1 
ATOM   14496 C  CG    . PRO   B  1 802  ? 18.140  49.831  53.267  1.00 42.69 ? 800  PRO   B CG    1 
ATOM   14497 C  CD    . PRO   B  1 802  ? 18.642  50.166  54.651  1.00 38.47 ? 800  PRO   B CD    1 
ATOM   14498 N  N     . ALA   B  1 803  ? 17.251  53.777  54.301  1.00 36.00 ? 801  ALA   B N     1 
ATOM   14499 C  CA    . ALA   B  1 803  ? 16.595  55.061  54.488  1.00 33.54 ? 801  ALA   B CA    1 
ATOM   14500 C  C     . ALA   B  1 803  ? 17.473  56.089  55.201  1.00 34.08 ? 801  ALA   B C     1 
ATOM   14501 O  O     . ALA   B  1 803  ? 16.980  57.173  55.524  1.00 39.29 ? 801  ALA   B O     1 
ATOM   14502 C  CB    . ALA   B  1 803  ? 15.287  54.867  55.260  1.00 35.68 ? 801  ALA   B CB    1 
ATOM   14503 N  N     . GLY   B  1 804  ? 18.742  55.783  55.467  1.00 33.38 ? 802  GLY   B N     1 
ATOM   14504 C  CA    . GLY   B  1 804  ? 19.619  56.748  56.111  1.00 31.65 ? 802  GLY   B CA    1 
ATOM   14505 C  C     . GLY   B  1 804  ? 19.426  56.905  57.605  1.00 30.37 ? 802  GLY   B C     1 
ATOM   14506 O  O     . GLY   B  1 804  ? 19.609  58.005  58.137  1.00 29.13 ? 802  GLY   B O     1 
ATOM   14507 N  N     . ARG   B  1 805  ? 19.074  55.832  58.301  1.00 28.97 ? 803  ARG   B N     1 
ATOM   14508 C  CA    . ARG   B  1 805  ? 18.731  55.855  59.711  1.00 28.09 ? 803  ARG   B CA    1 
ATOM   14509 C  C     . ARG   B  1 805  ? 19.592  54.845  60.457  1.00 25.97 ? 803  ARG   B C     1 
ATOM   14510 O  O     . ARG   B  1 805  ? 20.092  53.883  59.862  1.00 25.92 ? 803  ARG   B O     1 
ATOM   14511 C  CB    . ARG   B  1 805  ? 17.244  55.529  59.924  1.00 28.99 ? 803  ARG   B CB    1 
ATOM   14512 C  CG    . ARG   B  1 805  ? 16.270  56.504  59.251  1.00 32.41 ? 803  ARG   B CG    1 
ATOM   14513 C  CD    . ARG   B  1 805  ? 16.380  57.900  59.841  1.00 36.17 ? 803  ARG   B CD    1 
ATOM   14514 N  NE    . ARG   B  1 805  ? 15.410  58.849  59.290  1.00 42.49 ? 803  ARG   B NE    1 
ATOM   14515 C  CZ    . ARG   B  1 805  ? 15.730  59.904  58.549  1.00 34.92 ? 803  ARG   B CZ    1 
ATOM   14516 N  NH1   . ARG   B  1 805  ? 16.985  60.155  58.210  1.00 36.67 ? 803  ARG   B NH1   1 
ATOM   14517 N  NH2   . ARG   B  1 805  ? 14.770  60.747  58.165  1.00 32.44 ? 803  ARG   B NH2   1 
ATOM   14518 N  N     . PRO   B  1 806  ? 19.802  55.041  61.755  1.00 24.02 ? 804  PRO   B N     1 
ATOM   14519 C  CA    . PRO   B  1 806  ? 20.580  54.059  62.514  1.00 23.72 ? 804  PRO   B CA    1 
ATOM   14520 C  C     . PRO   B  1 806  ? 19.981  52.667  62.368  1.00 23.24 ? 804  PRO   B C     1 
ATOM   14521 O  O     . PRO   B  1 806  ? 18.761  52.503  62.286  1.00 23.21 ? 804  PRO   B O     1 
ATOM   14522 C  CB    . PRO   B  1 806  ? 20.490  54.571  63.956  1.00 25.47 ? 804  PRO   B CB    1 
ATOM   14523 C  CG    . PRO   B  1 806  ? 20.297  56.053  63.806  1.00 27.99 ? 804  PRO   B CG    1 
ATOM   14524 C  CD    . PRO   B  1 806  ? 19.392  56.185  62.589  1.00 25.03 ? 804  PRO   B CD    1 
ATOM   14525 N  N     . ILE   B  1 807  ? 20.860  51.671  62.290  1.00 21.65 ? 805  ILE   B N     1 
ATOM   14526 C  CA    . ILE   B  1 807  ? 20.474  50.261  62.248  1.00 21.33 ? 805  ILE   B CA    1 
ATOM   14527 C  C     . ILE   B  1 807  ? 20.006  49.856  63.641  1.00 23.35 ? 805  ILE   B C     1 
ATOM   14528 O  O     . ILE   B  1 807  ? 20.766  49.995  64.614  1.00 20.79 ? 805  ILE   B O     1 
ATOM   14529 C  CB    . ILE   B  1 807  ? 21.642  49.367  61.792  1.00 22.43 ? 805  ILE   B CB    1 
ATOM   14530 C  CG1   . ILE   B  1 807  ? 22.167  49.782  60.406  1.00 28.91 ? 805  ILE   B CG1   1 
ATOM   14531 C  CG2   . ILE   B  1 807  ? 21.213  47.899  61.820  1.00 22.49 ? 805  ILE   B CG2   1 
ATOM   14532 C  CD1   . ILE   B  1 807  ? 21.223  49.474  59.274  1.00 29.58 ? 805  ILE   B CD1   1 
ATOM   14533 N  N     . PRO   B  1 808  ? 18.780  49.362  63.792  1.00 20.65 ? 806  PRO   B N     1 
ATOM   14534 C  CA    . PRO   B  1 808  ? 18.281  49.045  65.135  1.00 23.09 ? 806  PRO   B CA    1 
ATOM   14535 C  C     . PRO   B  1 808  ? 19.064  47.909  65.762  1.00 25.21 ? 806  PRO   B C     1 
ATOM   14536 O  O     . PRO   B  1 808  ? 19.387  46.915  65.108  1.00 22.26 ? 806  PRO   B O     1 
ATOM   14537 C  CB    . PRO   B  1 808  ? 16.826  48.639  64.883  1.00 22.46 ? 806  PRO   B CB    1 
ATOM   14538 C  CG    . PRO   B  1 808  ? 16.463  49.319  63.617  1.00 26.90 ? 806  PRO   B CG    1 
ATOM   14539 C  CD    . PRO   B  1 808  ? 17.716  49.285  62.780  1.00 21.62 ? 806  PRO   B CD    1 
ATOM   14540 N  N     . LEU   B  1 809  ? 19.393  48.073  67.037  1.00 22.19 ? 807  LEU   B N     1 
ATOM   14541 C  CA    . LEU   B  1 809  ? 19.998  47.009  67.821  1.00 21.62 ? 807  LEU   B CA    1 
ATOM   14542 C  C     . LEU   B  1 809  ? 19.131  46.798  69.047  1.00 21.19 ? 807  LEU   B C     1 
ATOM   14543 O  O     . LEU   B  1 809  ? 18.935  47.730  69.834  1.00 23.21 ? 807  LEU   B O     1 
ATOM   14544 C  CB    . LEU   B  1 809  ? 21.433  47.348  68.233  1.00 20.70 ? 807  LEU   B CB    1 
ATOM   14545 C  CG    . LEU   B  1 809  ? 22.063  46.447  69.296  1.00 22.34 ? 807  LEU   B CG    1 
ATOM   14546 C  CD1   . LEU   B  1 809  ? 22.092  44.979  68.858  1.00 21.77 ? 807  LEU   B CD1   1 
ATOM   14547 C  CD2   . LEU   B  1 809  ? 23.487  46.928  69.631  1.00 22.21 ? 807  LEU   B CD2   1 
ATOM   14548 N  N     . ILE   B  1 810  ? 18.603  45.593  69.198  1.00 17.79 ? 808  ILE   B N     1 
ATOM   14549 C  CA    . ILE   B  1 810  ? 17.911  45.196  70.416  1.00 19.42 ? 808  ILE   B CA    1 
ATOM   14550 C  C     . ILE   B  1 810  ? 18.868  44.291  71.159  1.00 20.17 ? 808  ILE   B C     1 
ATOM   14551 O  O     . ILE   B  1 810  ? 19.241  43.222  70.656  1.00 21.58 ? 808  ILE   B O     1 
ATOM   14552 C  CB    . ILE   B  1 810  ? 16.584  44.478  70.129  1.00 17.83 ? 808  ILE   B CB    1 
ATOM   14553 C  CG1   . ILE   B  1 810  ? 15.661  45.370  69.303  1.00 21.71 ? 808  ILE   B CG1   1 
ATOM   14554 C  CG2   . ILE   B  1 810  ? 15.923  44.053  71.437  1.00 21.23 ? 808  ILE   B CG2   1 
ATOM   14555 C  CD1   . ILE   B  1 810  ? 14.334  44.713  69.028  1.00 25.70 ? 808  ILE   B CD1   1 
ATOM   14556 N  N     . ALA   B  1 811  ? 19.309  44.734  72.332  1.00 17.99 ? 809  ALA   B N     1 
ATOM   14557 C  CA    . ALA   B  1 811  ? 20.328  44.011  73.071  1.00 21.07 ? 809  ALA   B CA    1 
ATOM   14558 C  C     . ALA   B  1 811  ? 19.818  43.777  74.485  1.00 25.61 ? 809  ALA   B C     1 
ATOM   14559 O  O     . ALA   B  1 811  ? 19.385  44.716  75.155  1.00 24.25 ? 809  ALA   B O     1 
ATOM   14560 C  CB    . ALA   B  1 811  ? 21.657  44.784  73.061  1.00 18.98 ? 809  ALA   B CB    1 
ATOM   14561 N  N     . GLU   B  1 812  ? 19.828  42.525  74.924  1.00 22.18 ? 810  GLU   B N     1 
ATOM   14562 C  CA    . GLU   B  1 812  ? 19.507  42.183  76.304  1.00 24.00 ? 810  GLU   B CA    1 
ATOM   14563 C  C     . GLU   B  1 812  ? 20.780  41.629  76.910  1.00 23.17 ? 810  GLU   B C     1 
ATOM   14564 O  O     . GLU   B  1 812  ? 21.344  40.664  76.388  1.00 21.01 ? 810  GLU   B O     1 
ATOM   14565 C  CB    . GLU   B  1 812  ? 18.360  41.168  76.400  1.00 23.66 ? 810  GLU   B CB    1 
ATOM   14566 C  CG    . GLU   B  1 812  ? 17.776  41.046  77.825  1.00 30.91 ? 810  GLU   B CG    1 
ATOM   14567 C  CD    . GLU   B  1 812  ? 18.245  39.803  78.580  1.00 35.52 ? 810  GLU   B CD    1 
ATOM   14568 O  OE1   . GLU   B  1 812  ? 17.703  38.698  78.327  1.00 32.58 ? 810  GLU   B OE1   1 
ATOM   14569 O  OE2   . GLU   B  1 812  ? 19.152  39.929  79.435  1.00 37.84 ? 810  GLU   B OE2   1 
ATOM   14570 N  N     . THR   B  1 813  ? 21.258  42.262  77.985  1.00 23.12 ? 811  THR   B N     1 
ATOM   14571 C  CA    . THR   B  1 813  ? 22.625  42.021  78.415  1.00 22.16 ? 811  THR   B CA    1 
ATOM   14572 C  C     . THR   B  1 813  ? 22.744  41.736  79.910  1.00 26.68 ? 811  THR   B C     1 
ATOM   14573 O  O     . THR   B  1 813  ? 23.777  42.022  80.514  1.00 28.42 ? 811  THR   B O     1 
ATOM   14574 C  CB    . THR   B  1 813  ? 23.527  43.194  78.017  1.00 25.03 ? 811  THR   B CB    1 
ATOM   14575 O  OG1   . THR   B  1 813  ? 22.936  44.437  78.434  1.00 22.03 ? 811  THR   B OG1   1 
ATOM   14576 C  CG2   . THR   B  1 813  ? 23.706  43.215  76.503  1.00 26.13 ? 811  THR   B CG2   1 
ATOM   14577 N  N     . GLY   B  1 814  ? 21.731  41.138  80.521  1.00 26.03 ? 812  GLY   B N     1 
ATOM   14578 C  CA    . GLY   B  1 814  ? 21.967  40.570  81.846  1.00 31.51 ? 812  GLY   B CA    1 
ATOM   14579 C  C     . GLY   B  1 814  ? 21.936  41.587  82.976  1.00 29.10 ? 812  GLY   B C     1 
ATOM   14580 O  O     . GLY   B  1 814  ? 21.541  42.740  82.809  1.00 25.94 ? 812  GLY   B O     1 
ATOM   14581 N  N     . GLY   B  1 815  ? 22.348  41.133  84.160  1.00 26.42 ? 813  GLY   B N     1 
ATOM   14582 C  CA    . GLY   B  1 815  ? 22.118  41.955  85.337  1.00 25.46 ? 813  GLY   B CA    1 
ATOM   14583 C  C     . GLY   B  1 815  ? 22.998  41.552  86.496  1.00 27.22 ? 813  GLY   B C     1 
ATOM   14584 O  O     . GLY   B  1 815  ? 23.684  40.530  86.468  1.00 32.39 ? 813  GLY   B O     1 
ATOM   14585 N  N     . GLN   B  1 816  ? 22.963  42.380  87.532  1.00 24.43 ? 814  GLN   B N     1 
ATOM   14586 C  CA    . GLN   B  1 816  ? 23.571  42.071  88.825  1.00 22.55 ? 814  GLN   B CA    1 
ATOM   14587 C  C     . GLN   B  1 816  ? 22.425  42.078  89.830  1.00 21.88 ? 814  GLN   B C     1 
ATOM   14588 O  O     . GLN   B  1 816  ? 22.257  43.023  90.597  1.00 21.32 ? 814  GLN   B O     1 
ATOM   14589 C  CB    . GLN   B  1 816  ? 24.646  43.073  89.175  1.00 23.93 ? 814  GLN   B CB    1 
ATOM   14590 C  CG    . GLN   B  1 816  ? 25.528  42.651  90.314  1.00 27.67 ? 814  GLN   B CG    1 
ATOM   14591 C  CD    . GLN   B  1 816  ? 26.427  41.490  89.945  1.00 32.11 ? 814  GLN   B CD    1 
ATOM   14592 O  OE1   . GLN   B  1 816  ? 25.993  40.340  89.936  1.00 28.44 ? 814  GLN   B OE1   1 
ATOM   14593 N  NE2   . GLN   B  1 816  ? 27.689  41.784  89.637  1.00 34.48 ? 814  GLN   B NE2   1 
ATOM   14594 N  N     . ASN   B  1 817  ? 21.623  41.023  89.808  1.00 20.13 ? 815  ASN   B N     1 
ATOM   14595 C  CA    . ASN   B  1 817  ? 20.271  41.096  90.354  1.00 16.71 ? 815  ASN   B CA    1 
ATOM   14596 C  C     . ASN   B  1 817  ? 20.283  40.860  91.850  1.00 17.50 ? 815  ASN   B C     1 
ATOM   14597 O  O     . ASN   B  1 817  ? 20.929  39.929  92.338  1.00 17.47 ? 815  ASN   B O     1 
ATOM   14598 C  CB    . ASN   B  1 817  ? 19.380  40.072  89.674  1.00 16.79 ? 815  ASN   B CB    1 
ATOM   14599 C  CG    . ASN   B  1 817  ? 19.510  40.137  88.182  1.00 19.00 ? 815  ASN   B CG    1 
ATOM   14600 O  OD1   . ASN   B  1 817  ? 19.306  41.200  87.588  1.00 18.25 ? 815  ASN   B OD1   1 
ATOM   14601 N  ND2   . ASN   B  1 817  ? 19.917  39.026  87.569  1.00 16.51 ? 815  ASN   B ND2   1 
ATOM   14602 N  N     . ALA   B  1 818  ? 19.560  41.703  92.565  1.00 17.82 ? 816  ALA   B N     1 
ATOM   14603 C  CA    . ALA   B  1 818  ? 19.494  41.665  94.015  1.00 18.79 ? 816  ALA   B CA    1 
ATOM   14604 C  C     . ALA   B  1 818  ? 18.103  41.261  94.459  1.00 15.45 ? 816  ALA   B C     1 
ATOM   14605 O  O     . ALA   B  1 818  ? 17.117  41.436  93.740  1.00 18.60 ? 816  ALA   B O     1 
ATOM   14606 C  CB    . ALA   B  1 818  ? 19.828  43.027  94.631  1.00 15.83 ? 816  ALA   B CB    1 
ATOM   14607 N  N     . MET   B  1 819  ? 18.045  40.726  95.671  1.00 15.32 ? 817  MET   B N     1 
ATOM   14608 C  CA    . MET   B  1 819  ? 16.804  40.522  96.395  1.00 16.20 ? 817  MET   B CA    1 
ATOM   14609 C  C     . MET   B  1 819  ? 17.017  41.102  97.779  1.00 20.40 ? 817  MET   B C     1 
ATOM   14610 O  O     . MET   B  1 819  ? 18.033  40.809  98.421  1.00 18.90 ? 817  MET   B O     1 
ATOM   14611 C  CB    . MET   B  1 819  ? 16.418  39.047  96.496  1.00 14.93 ? 817  MET   B CB    1 
ATOM   14612 C  CG    . MET   B  1 819  ? 15.177  38.827  97.387  1.00 17.22 ? 817  MET   B CG    1 
ATOM   14613 S  SD    . MET   B  1 819  ? 14.923  37.073  97.688  1.00 22.09 ? 817  MET   B SD    1 
ATOM   14614 C  CE    . MET   B  1 819  ? 14.345  36.561  96.073  1.00 19.08 ? 817  MET   B CE    1 
ATOM   14615 N  N     . ILE   B  1 820  ? 16.087  41.950  98.215  1.00 15.95 ? 818  ILE   B N     1 
ATOM   14616 C  CA    . ILE   B  1 820  ? 16.108  42.517  99.559  1.00 16.91 ? 818  ILE   B CA    1 
ATOM   14617 C  C     . ILE   B  1 820  ? 15.065  41.799  100.394 1.00 19.54 ? 818  ILE   B C     1 
ATOM   14618 O  O     . ILE   B  1 820  ? 13.916  41.641  99.964  1.00 20.08 ? 818  ILE   B O     1 
ATOM   14619 C  CB    . ILE   B  1 820  ? 15.845  44.031  99.538  1.00 17.14 ? 818  ILE   B CB    1 
ATOM   14620 C  CG1   . ILE   B  1 820  ? 16.980  44.756  98.823  1.00 18.72 ? 818  ILE   B CG1   1 
ATOM   14621 C  CG2   . ILE   B  1 820  ? 15.722  44.562  100.964 1.00 16.97 ? 818  ILE   B CG2   1 
ATOM   14622 C  CD1   . ILE   B  1 820  ? 16.741  46.263  98.701  1.00 20.74 ? 818  ILE   B CD1   1 
ATOM   14623 N  N     . VAL   B  1 821  ? 15.468  41.357  101.583 1.00 18.69 ? 819  VAL   B N     1 
ATOM   14624 C  CA    . VAL   B  1 821  ? 14.614  40.612  102.498 1.00 17.86 ? 819  VAL   B CA    1 
ATOM   14625 C  C     . VAL   B  1 821  ? 14.631  41.354  103.824 1.00 18.57 ? 819  VAL   B C     1 
ATOM   14626 O  O     . VAL   B  1 821  ? 15.707  41.575  104.390 1.00 17.21 ? 819  VAL   B O     1 
ATOM   14627 C  CB    . VAL   B  1 821  ? 15.112  39.170  102.692 1.00 20.07 ? 819  VAL   B CB    1 
ATOM   14628 C  CG1   . VAL   B  1 821  ? 14.217  38.428  103.672 1.00 19.02 ? 819  VAL   B CG1   1 
ATOM   14629 C  CG2   . VAL   B  1 821  ? 15.171  38.436  101.348 1.00 17.07 ? 819  VAL   B CG2   1 
ATOM   14630 N  N     . ASP   B  1 822  ? 13.458  41.735  104.327 1.00 20.04 ? 820  ASP   B N     1 
ATOM   14631 C  CA    . ASP   B  1 822  ? 13.448  42.410  105.613 1.00 21.98 ? 820  ASP   B CA    1 
ATOM   14632 C  C     . ASP   B  1 822  ? 13.006  41.429  106.699 1.00 20.92 ? 820  ASP   B C     1 
ATOM   14633 O  O     . ASP   B  1 822  ? 12.758  40.249  106.444 1.00 19.63 ? 820  ASP   B O     1 
ATOM   14634 C  CB    . ASP   B  1 822  ? 12.601  43.692  105.557 1.00 18.75 ? 820  ASP   B CB    1 
ATOM   14635 C  CG    . ASP   B  1 822  ? 11.103  43.446  105.524 1.00 21.86 ? 820  ASP   B CG    1 
ATOM   14636 O  OD1   . ASP   B  1 822  ? 10.624  42.313  105.721 1.00 21.02 ? 820  ASP   B OD1   1 
ATOM   14637 O  OD2   . ASP   B  1 822  ? 10.380  44.439  105.289 1.00 24.65 ? 820  ASP   B OD2   1 
ATOM   14638 N  N     . SER   B  1 823  ? 12.904  41.929  107.930 1.00 20.94 ? 821  SER   B N     1 
ATOM   14639 C  CA    . SER   B  1 823  ? 12.634  41.046  109.062 1.00 24.26 ? 821  SER   B CA    1 
ATOM   14640 C  C     . SER   B  1 823  ? 11.185  40.572  109.114 1.00 28.70 ? 821  SER   B C     1 
ATOM   14641 O  O     . SER   B  1 823  ? 10.850  39.735  109.959 1.00 26.14 ? 821  SER   B O     1 
ATOM   14642 C  CB    . SER   B  1 823  ? 13.009  41.758  110.366 1.00 23.42 ? 821  SER   B CB    1 
ATOM   14643 O  OG    . SER   B  1 823  ? 12.303  42.982  110.482 1.00 26.01 ? 821  SER   B OG    1 
ATOM   14644 N  N     . SER   B  1 824  ? 10.316  41.074  108.244 1.00 19.53 ? 822  SER   B N     1 
ATOM   14645 C  CA    . SER   B  1 824  ? 8.943   40.586  108.218 1.00 21.38 ? 822  SER   B CA    1 
ATOM   14646 C  C     . SER   B  1 824  ? 8.751   39.417  107.264 1.00 23.07 ? 822  SER   B C     1 
ATOM   14647 O  O     . SER   B  1 824  ? 7.690   38.783  107.290 1.00 23.35 ? 822  SER   B O     1 
ATOM   14648 C  CB    . SER   B  1 824  ? 7.976   41.707  107.824 1.00 23.37 ? 822  SER   B CB    1 
ATOM   14649 O  OG    . SER   B  1 824  ? 8.035   41.977  106.434 1.00 22.10 ? 822  SER   B OG    1 
ATOM   14650 N  N     . ALA   B  1 825  ? 9.724   39.141  106.402 1.00 18.69 ? 823  ALA   B N     1 
ATOM   14651 C  CA    . ALA   B  1 825  ? 9.562   38.079  105.419 1.00 22.31 ? 823  ALA   B CA    1 
ATOM   14652 C  C     . ALA   B  1 825  ? 9.498   36.714  106.099 1.00 24.05 ? 823  ALA   B C     1 
ATOM   14653 O  O     . ALA   B  1 825  ? 10.043  36.510  107.184 1.00 23.14 ? 823  ALA   B O     1 
ATOM   14654 C  CB    . ALA   B  1 825  ? 10.716  38.104  104.413 1.00 20.20 ? 823  ALA   B CB    1 
ATOM   14655 N  N     . LEU   B  1 826  ? 8.833   35.771  105.441 1.00 22.02 ? 824  LEU   B N     1 
ATOM   14656 C  CA    . LEU   B  1 826  ? 8.777   34.395  105.926 1.00 25.67 ? 824  LEU   B CA    1 
ATOM   14657 C  C     . LEU   B  1 826  ? 10.040  33.663  105.482 1.00 24.84 ? 824  LEU   B C     1 
ATOM   14658 O  O     . LEU   B  1 826  ? 10.239  33.438  104.284 1.00 24.58 ? 824  LEU   B O     1 
ATOM   14659 C  CB    . LEU   B  1 826  ? 7.531   33.693  105.397 1.00 31.18 ? 824  LEU   B CB    1 
ATOM   14660 C  CG    . LEU   B  1 826  ? 7.354   32.253  105.868 1.00 31.74 ? 824  LEU   B CG    1 
ATOM   14661 C  CD1   . LEU   B  1 826  ? 7.391   32.219  107.378 1.00 34.68 ? 824  LEU   B CD1   1 
ATOM   14662 C  CD2   . LEU   B  1 826  ? 6.046   31.686  105.354 1.00 41.63 ? 824  LEU   B CD2   1 
ATOM   14663 N  N     . ALA   B  1 827  ? 10.877  33.267  106.446 1.00 22.36 ? 825  ALA   B N     1 
ATOM   14664 C  CA    . ALA   B  1 827  ? 12.184  32.690  106.126 1.00 24.70 ? 825  ALA   B CA    1 
ATOM   14665 C  C     . ALA   B  1 827  ? 12.076  31.514  105.155 1.00 24.23 ? 825  ALA   B C     1 
ATOM   14666 O  O     . ALA   B  1 827  ? 12.845  31.420  104.190 1.00 24.10 ? 825  ALA   B O     1 
ATOM   14667 C  CB    . ALA   B  1 827  ? 12.885  32.251  107.411 1.00 23.96 ? 825  ALA   B CB    1 
ATOM   14668 N  N     . GLU   B  1 828  ? 11.142  30.591  105.407 1.00 22.48 ? 826  GLU   B N     1 
ATOM   14669 C  CA    . GLU   B  1 828  ? 11.035  29.405  104.556 1.00 24.92 ? 826  GLU   B CA    1 
ATOM   14670 C  C     . GLU   B  1 828  ? 10.711  29.780  103.121 1.00 25.83 ? 826  GLU   B C     1 
ATOM   14671 O  O     . GLU   B  1 828  ? 11.209  29.152  102.182 1.00 22.58 ? 826  GLU   B O     1 
ATOM   14672 C  CB    . GLU   B  1 828  ? 9.965   28.449  105.081 1.00 28.12 ? 826  GLU   B CB    1 
ATOM   14673 C  CG    . GLU   B  1 828  ? 10.360  27.685  106.330 1.00 31.31 ? 826  GLU   B CG    1 
ATOM   14674 C  CD    . GLU   B  1 828  ? 10.275  28.521  107.594 1.00 35.31 ? 826  GLU   B CD    1 
ATOM   14675 O  OE1   . GLU   B  1 828  ? 9.765   29.668  107.538 1.00 32.43 ? 826  GLU   B OE1   1 
ATOM   14676 O  OE2   . GLU   B  1 828  ? 10.724  28.020  108.648 1.00 37.18 ? 826  GLU   B OE2   1 
ATOM   14677 N  N     . GLN   B  1 829  ? 9.845   30.771  102.929 1.00 22.52 ? 827  GLN   B N     1 
ATOM   14678 C  CA    . GLN   B  1 829  ? 9.540   31.208  101.571 1.00 20.39 ? 827  GLN   B CA    1 
ATOM   14679 C  C     . GLN   B  1 829  ? 10.741  31.906  100.956 1.00 21.85 ? 827  GLN   B C     1 
ATOM   14680 O  O     . GLN   B  1 829  ? 11.033  31.718  99.770  1.00 21.43 ? 827  GLN   B O     1 
ATOM   14681 C  CB    . GLN   B  1 829  ? 8.316   32.132  101.571 1.00 23.95 ? 827  GLN   B CB    1 
ATOM   14682 N  N     . VAL   B  1 830  ? 11.448  32.718  101.749 1.00 21.97 ? 828  VAL   B N     1 
ATOM   14683 C  CA    . VAL   B  1 830  ? 12.676  33.348  101.263 1.00 20.63 ? 828  VAL   B CA    1 
ATOM   14684 C  C     . VAL   B  1 830  ? 13.655  32.292  100.776 1.00 22.22 ? 828  VAL   B C     1 
ATOM   14685 O  O     . VAL   B  1 830  ? 14.188  32.375  99.662  1.00 21.03 ? 828  VAL   B O     1 
ATOM   14686 C  CB    . VAL   B  1 830  ? 13.314  34.217  102.360 1.00 20.88 ? 828  VAL   B CB    1 
ATOM   14687 C  CG1   . VAL   B  1 830  ? 14.719  34.646  101.939 1.00 20.76 ? 828  VAL   B CG1   1 
ATOM   14688 C  CG2   . VAL   B  1 830  ? 12.448  35.425  102.649 1.00 22.45 ? 828  VAL   B CG2   1 
ATOM   14689 N  N     . VAL   B  1 831  ? 13.902  31.278  101.606 1.00 20.15 ? 829  VAL   B N     1 
ATOM   14690 C  CA    . VAL   B  1 831  ? 14.935  30.301  101.277 1.00 21.63 ? 829  VAL   B CA    1 
ATOM   14691 C  C     . VAL   B  1 831  ? 14.564  29.549  100.006 1.00 20.22 ? 829  VAL   B C     1 
ATOM   14692 O  O     . VAL   B  1 831  ? 15.404  29.353  99.118  1.00 20.75 ? 829  VAL   B O     1 
ATOM   14693 C  CB    . VAL   B  1 831  ? 15.173  29.352  102.466 1.00 20.98 ? 829  VAL   B CB    1 
ATOM   14694 C  CG1   . VAL   B  1 831  ? 15.960  28.133  102.030 1.00 20.58 ? 829  VAL   B CG1   1 
ATOM   14695 C  CG2   . VAL   B  1 831  ? 15.933  30.077  103.572 1.00 22.71 ? 829  VAL   B CG2   1 
ATOM   14696 N  N     . GLY   B  1 832  ? 13.302  29.136  99.889  1.00 19.87 ? 830  GLY   B N     1 
ATOM   14697 C  CA    . GLY   B  1 832  ? 12.864  28.504  98.654  1.00 20.20 ? 830  GLY   B CA    1 
ATOM   14698 C  C     . GLY   B  1 832  ? 13.100  29.395  97.450  1.00 20.59 ? 830  GLY   B C     1 
ATOM   14699 O  O     . GLY   B  1 832  ? 13.634  28.957  96.426  1.00 19.22 ? 830  GLY   B O     1 
ATOM   14700 N  N     . ASP   B  1 833  ? 12.743  30.673  97.574  1.00 20.14 ? 831  ASP   B N     1 
ATOM   14701 C  CA    . ASP   B  1 833  ? 12.854  31.572  96.431  1.00 19.63 ? 831  ASP   B CA    1 
ATOM   14702 C  C     . ASP   B  1 833  ? 14.297  31.940  96.143  1.00 18.60 ? 831  ASP   B C     1 
ATOM   14703 O  O     . ASP   B  1 833  ? 14.651  32.183  94.987  1.00 19.31 ? 831  ASP   B O     1 
ATOM   14704 C  CB    . ASP   B  1 833  ? 12.006  32.811  96.678  1.00 16.77 ? 831  ASP   B CB    1 
ATOM   14705 C  CG    . ASP   B  1 833  ? 10.531  32.491  96.673  1.00 21.81 ? 831  ASP   B CG    1 
ATOM   14706 O  OD1   . ASP   B  1 833  ? 10.183  31.401  96.164  1.00 22.18 ? 831  ASP   B OD1   1 
ATOM   14707 O  OD2   . ASP   B  1 833  ? 9.728   33.302  97.181  1.00 21.98 ? 831  ASP   B OD2   1 
ATOM   14708 N  N     . VAL   B  1 834  ? 15.144  31.963  97.168  1.00 16.97 ? 832  VAL   B N     1 
ATOM   14709 C  CA    . VAL   B  1 834  ? 16.556  32.250  96.957  1.00 15.94 ? 832  VAL   B CA    1 
ATOM   14710 C  C     . VAL   B  1 834  ? 17.243  31.063  96.297  1.00 17.30 ? 832  VAL   B C     1 
ATOM   14711 O  O     . VAL   B  1 834  ? 18.033  31.230  95.358  1.00 18.78 ? 832  VAL   B O     1 
ATOM   14712 C  CB    . VAL   B  1 834  ? 17.219  32.628  98.294  1.00 18.43 ? 832  VAL   B CB    1 
ATOM   14713 C  CG1   . VAL   B  1 834  ? 18.730  32.591  98.173  1.00 17.78 ? 832  VAL   B CG1   1 
ATOM   14714 C  CG2   . VAL   B  1 834  ? 16.736  34.011  98.735  1.00 19.57 ? 832  VAL   B CG2   1 
ATOM   14715 N  N     . ILE   B  1 835  ? 16.978  29.848  96.795  1.00 17.06 ? 833  ILE   B N     1 
ATOM   14716 C  CA    . ILE   B  1 835  ? 17.605  28.658  96.218  1.00 18.95 ? 833  ILE   B CA    1 
ATOM   14717 C  C     . ILE   B  1 835  ? 17.258  28.556  94.744  1.00 19.85 ? 833  ILE   B C     1 
ATOM   14718 O  O     . ILE   B  1 835  ? 18.123  28.317  93.895  1.00 21.45 ? 833  ILE   B O     1 
ATOM   14719 C  CB    . ILE   B  1 835  ? 17.186  27.384  96.978  1.00 22.10 ? 833  ILE   B CB    1 
ATOM   14720 C  CG1   . ILE   B  1 835  ? 17.736  27.371  98.402  1.00 25.66 ? 833  ILE   B CG1   1 
ATOM   14721 C  CG2   . ILE   B  1 835  ? 17.660  26.115  96.219  1.00 24.21 ? 833  ILE   B CG2   1 
ATOM   14722 C  CD1   . ILE   B  1 835  ? 19.133  26.834  98.516  1.00 30.20 ? 833  ILE   B CD1   1 
ATOM   14723 N  N     . THR   B  1 836  ? 15.983  28.754  94.417  1.00 17.59 ? 834  THR   B N     1 
ATOM   14724 C  CA    . THR   B  1 836  ? 15.559  28.747  93.021  1.00 18.68 ? 834  THR   B CA    1 
ATOM   14725 C  C     . THR   B  1 836  ? 16.212  29.880  92.238  1.00 21.14 ? 834  THR   B C     1 
ATOM   14726 O  O     . THR   B  1 836  ? 16.781  29.655  91.167  1.00 21.57 ? 834  THR   B O     1 
ATOM   14727 C  CB    . THR   B  1 836  ? 14.034  28.849  92.947  1.00 21.80 ? 834  THR   B CB    1 
ATOM   14728 O  OG1   . THR   B  1 836  ? 13.458  27.666  93.513  1.00 27.74 ? 834  THR   B OG1   1 
ATOM   14729 C  CG2   . THR   B  1 836  ? 13.570  28.979  91.504  1.00 26.00 ? 834  THR   B CG2   1 
ATOM   14730 N  N     . SER   B  1 837  ? 16.155  31.110  92.755  1.00 18.16 ? 835  SER   B N     1 
ATOM   14731 C  CA    . SER   B  1 837  ? 16.624  32.237  91.948  1.00 16.37 ? 835  SER   B CA    1 
ATOM   14732 C  C     . SER   B  1 837  ? 18.126  32.191  91.726  1.00 19.22 ? 835  SER   B C     1 
ATOM   14733 O  O     . SER   B  1 837  ? 18.614  32.590  90.664  1.00 18.02 ? 835  SER   B O     1 
ATOM   14734 C  CB    . SER   B  1 837  ? 16.243  33.559  92.602  1.00 15.73 ? 835  SER   B CB    1 
ATOM   14735 O  OG    . SER   B  1 837  ? 14.841  33.637  92.746  1.00 17.81 ? 835  SER   B OG    1 
ATOM   14736 N  N     . ALA   B  1 838  ? 18.878  31.746  92.724  1.00 16.47 ? 836  ALA   B N     1 
ATOM   14737 C  CA    . ALA   B  1 838  ? 20.330  31.793  92.646  1.00 16.16 ? 836  ALA   B CA    1 
ATOM   14738 C  C     . ALA   B  1 838  ? 20.932  30.569  91.973  1.00 17.22 ? 836  ALA   B C     1 
ATOM   14739 O  O     . ALA   B  1 838  ? 21.964  30.692  91.302  1.00 19.95 ? 836  ALA   B O     1 
ATOM   14740 C  CB    . ALA   B  1 838  ? 20.935  31.923  94.053  1.00 17.30 ? 836  ALA   B CB    1 
ATOM   14741 N  N     . PHE   B  1 839  ? 20.328  29.390  92.137  1.00 16.19 ? 837  PHE   B N     1 
ATOM   14742 C  CA    . PHE   B  1 839  ? 21.006  28.159  91.755  1.00 20.52 ? 837  PHE   B CA    1 
ATOM   14743 C  C     . PHE   B  1 839  ? 20.273  27.341  90.706  1.00 22.22 ? 837  PHE   B C     1 
ATOM   14744 O  O     . PHE   B  1 839  ? 20.875  26.420  90.137  1.00 21.39 ? 837  PHE   B O     1 
ATOM   14745 C  CB    . PHE   B  1 839  ? 21.271  27.286  92.993  1.00 18.81 ? 837  PHE   B CB    1 
ATOM   14746 C  CG    . PHE   B  1 839  ? 21.980  28.018  94.088  1.00 19.16 ? 837  PHE   B CG    1 
ATOM   14747 C  CD1   . PHE   B  1 839  ? 23.212  28.616  93.857  1.00 20.44 ? 837  PHE   B CD1   1 
ATOM   14748 C  CD2   . PHE   B  1 839  ? 21.423  28.113  95.352  1.00 20.41 ? 837  PHE   B CD2   1 
ATOM   14749 C  CE1   . PHE   B  1 839  ? 23.875  29.311  94.870  1.00 19.89 ? 837  PHE   B CE1   1 
ATOM   14750 C  CE2   . PHE   B  1 839  ? 22.085  28.810  96.368  1.00 22.87 ? 837  PHE   B CE2   1 
ATOM   14751 C  CZ    . PHE   B  1 839  ? 23.310  29.400  96.123  1.00 23.19 ? 837  PHE   B CZ    1 
ATOM   14752 N  N     . ASP   B  1 840  ? 19.007  27.631  90.436  1.00 21.01 ? 838  ASP   B N     1 
ATOM   14753 C  CA    . ASP   B  1 840  ? 18.348  27.014  89.297  1.00 21.03 ? 838  ASP   B CA    1 
ATOM   14754 C  C     . ASP   B  1 840  ? 19.173  27.259  88.045  1.00 22.82 ? 838  ASP   B C     1 
ATOM   14755 O  O     . ASP   B  1 840  ? 19.722  28.349  87.850  1.00 19.69 ? 838  ASP   B O     1 
ATOM   14756 C  CB    . ASP   B  1 840  ? 16.941  27.582  89.121  1.00 26.29 ? 838  ASP   B CB    1 
ATOM   14757 C  CG    . ASP   B  1 840  ? 16.223  27.012  87.920  1.00 26.58 ? 838  ASP   B CG    1 
ATOM   14758 O  OD1   . ASP   B  1 840  ? 16.429  27.507  86.795  1.00 24.98 ? 838  ASP   B OD1   1 
ATOM   14759 O  OD2   . ASP   B  1 840  ? 15.442  26.067  88.110  1.00 31.54 ? 838  ASP   B OD2   1 
ATOM   14760 N  N     . SER   B  1 841  ? 19.276  26.225  87.209  1.00 21.48 ? 839  SER   B N     1 
ATOM   14761 C  CA    . SER   B  1 841  ? 20.043  26.296  85.969  1.00 23.05 ? 839  SER   B CA    1 
ATOM   14762 C  C     . SER   B  1 841  ? 21.488  26.680  86.245  1.00 18.87 ? 839  SER   B C     1 
ATOM   14763 O  O     . SER   B  1 841  ? 22.125  27.381  85.454  1.00 19.24 ? 839  SER   B O     1 
ATOM   14764 C  CB    . SER   B  1 841  ? 19.401  27.269  84.978  1.00 22.09 ? 839  SER   B CB    1 
ATOM   14765 O  OG    . SER   B  1 841  ? 18.042  26.939  84.816  1.00 24.78 ? 839  SER   B OG    1 
ATOM   14766 N  N     . ALA   B  1 842  ? 21.993  26.237  87.396  1.00 19.75 ? 840  ALA   B N     1 
ATOM   14767 C  CA    . ALA   B  1 842  ? 23.360  26.521  87.818  1.00 18.43 ? 840  ALA   B CA    1 
ATOM   14768 C  C     . ALA   B  1 842  ? 23.630  28.022  87.817  1.00 17.26 ? 840  ALA   B C     1 
ATOM   14769 O  O     . ALA   B  1 842  ? 24.741  28.463  87.538  1.00 18.17 ? 840  ALA   B O     1 
ATOM   14770 C  CB    . ALA   B  1 842  ? 24.375  25.776  86.940  1.00 20.50 ? 840  ALA   B CB    1 
ATOM   14771 N  N     . GLY   B  1 843  ? 22.605  28.817  88.132  1.00 17.47 ? 841  GLY   B N     1 
ATOM   14772 C  CA    . GLY   B  1 843  ? 22.766  30.255  88.145  1.00 18.60 ? 841  GLY   B CA    1 
ATOM   14773 C  C     . GLY   B  1 843  ? 23.029  30.862  86.784  1.00 19.90 ? 841  GLY   B C     1 
ATOM   14774 O  O     . GLY   B  1 843  ? 23.505  31.999  86.704  1.00 20.48 ? 841  GLY   B O     1 
ATOM   14775 N  N     . GLN   B  1 844  ? 22.729  30.132  85.707  1.00 17.68 ? 842  GLN   B N     1 
ATOM   14776 C  CA    . GLN   B  1 844  ? 23.015  30.590  84.352  1.00 19.78 ? 842  GLN   B CA    1 
ATOM   14777 C  C     . GLN   B  1 844  ? 21.820  31.274  83.709  1.00 21.72 ? 842  GLN   B C     1 
ATOM   14778 O  O     . GLN   B  1 844  ? 21.623  31.181  82.502  1.00 23.58 ? 842  GLN   B O     1 
ATOM   14779 C  CB    . GLN   B  1 844  ? 23.503  29.427  83.497  1.00 18.24 ? 842  GLN   B CB    1 
ATOM   14780 C  CG    . GLN   B  1 844  ? 24.818  28.880  84.037  1.00 16.71 ? 842  GLN   B CG    1 
ATOM   14781 C  CD    . GLN   B  1 844  ? 25.335  27.726  83.219  1.00 16.41 ? 842  GLN   B CD    1 
ATOM   14782 O  OE1   . GLN   B  1 844  ? 26.503  27.684  82.886  1.00 18.18 ? 842  GLN   B OE1   1 
ATOM   14783 N  NE2   . GLN   B  1 844  ? 24.458  26.786  82.886  1.00 21.93 ? 842  GLN   B NE2   1 
ATOM   14784 N  N     . ARG   B  1 845  ? 21.003  31.934  84.502  1.00 21.97 ? 843  ARG   B N     1 
ATOM   14785 C  CA    . ARG   B  1 845  ? 19.941  32.786  84.001  1.00 20.27 ? 843  ARG   B CA    1 
ATOM   14786 C  C     . ARG   B  1 845  ? 20.408  34.225  84.097  1.00 20.60 ? 843  ARG   B C     1 
ATOM   14787 O  O     . ARG   B  1 845  ? 21.055  34.606  85.074  1.00 21.95 ? 843  ARG   B O     1 
ATOM   14788 C  CB    . ARG   B  1 845  ? 18.669  32.613  84.829  1.00 21.09 ? 843  ARG   B CB    1 
ATOM   14789 C  CG    . ARG   B  1 845  ? 18.087  31.235  84.799  1.00 21.17 ? 843  ARG   B CG    1 
ATOM   14790 C  CD    . ARG   B  1 845  ? 16.818  31.207  85.641  1.00 25.66 ? 843  ARG   B CD    1 
ATOM   14791 N  NE    . ARG   B  1 845  ? 16.144  29.923  85.555  1.00 25.50 ? 843  ARG   B NE    1 
ATOM   14792 C  CZ    . ARG   B  1 845  ? 15.088  29.683  84.792  1.00 27.30 ? 843  ARG   B CZ    1 
ATOM   14793 N  NH1   . ARG   B  1 845  ? 14.541  30.632  84.044  1.00 26.71 ? 843  ARG   B NH1   1 
ATOM   14794 N  NH2   . ARG   B  1 845  ? 14.568  28.458  84.775  1.00 32.62 ? 843  ARG   B NH2   1 
ATOM   14795 N  N     . CYS   B  1 846  ? 20.065  35.040  83.101  1.00 19.34 ? 844  CYS   B N     1 
ATOM   14796 C  CA    A CYS   B  1 846  ? 20.383  36.457  83.220  0.55 22.23 ? 844  CYS   B CA    1 
ATOM   14797 C  CA    B CYS   B  1 846  ? 20.372  36.463  83.210  0.45 22.24 ? 844  CYS   B CA    1 
ATOM   14798 C  C     . CYS   B  1 846  ? 19.638  37.087  84.387  1.00 19.83 ? 844  CYS   B C     1 
ATOM   14799 O  O     . CYS   B  1 846  ? 20.114  38.062  84.969  1.00 18.48 ? 844  CYS   B O     1 
ATOM   14800 C  CB    A CYS   B  1 846  ? 20.067  37.178  81.913  0.55 26.08 ? 844  CYS   B CB    1 
ATOM   14801 C  CB    B CYS   B  1 846  ? 20.000  37.185  81.919  0.45 26.04 ? 844  CYS   B CB    1 
ATOM   14802 S  SG    A CYS   B  1 846  ? 21.216  36.703  80.602  0.55 32.34 ? 844  CYS   B SG    1 
ATOM   14803 S  SG    B CYS   B  1 846  ? 18.269  37.029  81.518  0.45 25.19 ? 844  CYS   B SG    1 
ATOM   14804 N  N     . SER   B  1 847  ? 18.489  36.527  84.745  1.00 18.76 ? 845  SER   B N     1 
ATOM   14805 C  CA    . SER   B  1 847  ? 17.658  36.948  85.860  1.00 17.96 ? 845  SER   B CA    1 
ATOM   14806 C  C     . SER   B  1 847  ? 18.120  36.409  87.207  1.00 17.33 ? 845  SER   B C     1 
ATOM   14807 O  O     . SER   B  1 847  ? 17.512  36.754  88.222  1.00 15.88 ? 845  SER   B O     1 
ATOM   14808 C  CB    . SER   B  1 847  ? 16.239  36.458  85.620  1.00 19.11 ? 845  SER   B CB    1 
ATOM   14809 O  OG    . SER   B  1 847  ? 16.304  35.063  85.366  1.00 23.28 ? 845  SER   B OG    1 
ATOM   14810 N  N     . ALA   B  1 848  ? 19.134  35.550  87.240  1.00 18.24 ? 846  ALA   B N     1 
ATOM   14811 C  CA    . ALA   B  1 848  ? 19.511  34.862  88.470  1.00 16.41 ? 846  ALA   B CA    1 
ATOM   14812 C  C     . ALA   B  1 848  ? 19.845  35.836  89.599  1.00 18.62 ? 846  ALA   B C     1 
ATOM   14813 O  O     . ALA   B  1 848  ? 20.428  36.906  89.392  1.00 17.47 ? 846  ALA   B O     1 
ATOM   14814 C  CB    . ALA   B  1 848  ? 20.713  33.946  88.212  1.00 17.93 ? 846  ALA   B CB    1 
ATOM   14815 N  N     . LEU   B  1 849  ? 19.496  35.428  90.816  1.00 18.88 ? 847  LEU   B N     1 
ATOM   14816 C  CA    . LEU   B  1 849  ? 19.837  36.186  92.014  1.00 17.52 ? 847  LEU   B CA    1 
ATOM   14817 C  C     . LEU   B  1 849  ? 21.338  36.145  92.258  1.00 18.09 ? 847  LEU   B C     1 
ATOM   14818 O  O     . LEU   B  1 849  ? 21.906  35.069  92.463  1.00 19.77 ? 847  LEU   B O     1 
ATOM   14819 C  CB    . LEU   B  1 849  ? 19.101  35.602  93.211  1.00 17.56 ? 847  LEU   B CB    1 
ATOM   14820 C  CG    . LEU   B  1 849  ? 19.404  36.233  94.565  1.00 17.89 ? 847  LEU   B CG    1 
ATOM   14821 C  CD1   . LEU   B  1 849  ? 19.130  37.743  94.521  1.00 16.81 ? 847  LEU   B CD1   1 
ATOM   14822 C  CD2   . LEU   B  1 849  ? 18.569  35.534  95.621  1.00 19.25 ? 847  LEU   B CD2   1 
ATOM   14823 N  N     . ARG   B  1 850  ? 21.972  37.315  92.265  1.00 17.75 ? 848  ARG   B N     1 
ATOM   14824 C  CA    . ARG   B  1 850  ? 23.405  37.420  92.517  1.00 18.47 ? 848  ARG   B CA    1 
ATOM   14825 C  C     . ARG   B  1 850  ? 23.733  37.941  93.901  1.00 19.24 ? 848  ARG   B C     1 
ATOM   14826 O  O     . ARG   B  1 850  ? 24.740  37.532  94.477  1.00 21.06 ? 848  ARG   B O     1 
ATOM   14827 C  CB    . ARG   B  1 850  ? 24.058  38.348  91.491  1.00 18.34 ? 848  ARG   B CB    1 
ATOM   14828 C  CG    . ARG   B  1 850  ? 23.690  37.989  90.064  1.00 19.76 ? 848  ARG   B CG    1 
ATOM   14829 C  CD    . ARG   B  1 850  ? 24.005  36.532  89.788  1.00 19.71 ? 848  ARG   B CD    1 
ATOM   14830 N  NE    . ARG   B  1 850  ? 23.858  36.223  88.371  1.00 21.10 ? 848  ARG   B NE    1 
ATOM   14831 C  CZ    . ARG   B  1 850  ? 23.983  35.004  87.867  1.00 20.50 ? 848  ARG   B CZ    1 
ATOM   14832 N  NH1   . ARG   B  1 850  ? 24.234  33.963  88.643  1.00 17.86 ? 848  ARG   B NH1   1 
ATOM   14833 N  NH2   . ARG   B  1 850  ? 23.847  34.827  86.553  1.00 20.20 ? 848  ARG   B NH2   1 
ATOM   14834 N  N     . VAL   B  1 851  ? 22.926  38.846  94.437  1.00 18.07 ? 849  VAL   B N     1 
ATOM   14835 C  CA    . VAL   B  1 851  ? 23.203  39.463  95.729  1.00 19.79 ? 849  VAL   B CA    1 
ATOM   14836 C  C     . VAL   B  1 851  ? 21.943  39.382  96.579  1.00 21.15 ? 849  VAL   B C     1 
ATOM   14837 O  O     . VAL   B  1 851  ? 20.942  40.046  96.285  1.00 18.83 ? 849  VAL   B O     1 
ATOM   14838 C  CB    . VAL   B  1 851  ? 23.671  40.915  95.591  1.00 22.35 ? 849  VAL   B CB    1 
ATOM   14839 C  CG1   . VAL   B  1 851  ? 24.040  41.467  96.960  1.00 21.91 ? 849  VAL   B CG1   1 
ATOM   14840 C  CG2   . VAL   B  1 851  ? 24.850  41.012  94.627  1.00 24.40 ? 849  VAL   B CG2   1 
ATOM   14841 N  N     . LEU   B  1 852  ? 22.000  38.592  97.642  1.00 20.36 ? 850  LEU   B N     1 
ATOM   14842 C  CA    . LEU   B  1 852  ? 20.917  38.509  98.605  1.00 19.60 ? 850  LEU   B CA    1 
ATOM   14843 C  C     . LEU   B  1 852  ? 21.211  39.489  99.728  1.00 21.08 ? 850  LEU   B C     1 
ATOM   14844 O  O     . LEU   B  1 852  ? 22.277  39.422  100.350 1.00 22.27 ? 850  LEU   B O     1 
ATOM   14845 C  CB    . LEU   B  1 852  ? 20.794  37.092  99.153  1.00 19.40 ? 850  LEU   B CB    1 
ATOM   14846 C  CG    . LEU   B  1 852  ? 19.750  36.911  100.246 1.00 17.92 ? 850  LEU   B CG    1 
ATOM   14847 C  CD1   . LEU   B  1 852  ? 18.339  37.297  99.740  1.00 19.50 ? 850  LEU   B CD1   1 
ATOM   14848 C  CD2   . LEU   B  1 852  ? 19.779  35.475  100.710 1.00 18.25 ? 850  LEU   B CD2   1 
ATOM   14849 N  N     . CYS   B  1 853  ? 20.277  40.398  99.979  1.00 19.10 ? 851  CYS   B N     1 
ATOM   14850 C  CA    . CYS   B  1 853  ? 20.438  41.441  100.989 1.00 21.02 ? 851  CYS   B CA    1 
ATOM   14851 C  C     . CYS   B  1 853  ? 19.492  41.144  102.146 1.00 18.68 ? 851  CYS   B C     1 
ATOM   14852 O  O     . CYS   B  1 853  ? 18.275  41.262  102.000 1.00 19.22 ? 851  CYS   B O     1 
ATOM   14853 C  CB    . CYS   B  1 853  ? 20.147  42.816  100.397 1.00 20.56 ? 851  CYS   B CB    1 
ATOM   14854 S  SG    . CYS   B  1 853  ? 21.050  43.156  98.899  1.00 22.28 ? 851  CYS   B SG    1 
ATOM   14855 N  N     . LEU   B  1 854  ? 20.050  40.786  103.302 1.00 21.23 ? 852  LEU   B N     1 
ATOM   14856 C  CA    . LEU   B  1 854  ? 19.255  40.355  104.444 1.00 19.55 ? 852  LEU   B CA    1 
ATOM   14857 C  C     . LEU   B  1 854  ? 19.305  41.418  105.528 1.00 22.90 ? 852  LEU   B C     1 
ATOM   14858 O  O     . LEU   B  1 854  ? 20.391  41.881  105.893 1.00 22.13 ? 852  LEU   B O     1 
ATOM   14859 C  CB    . LEU   B  1 854  ? 19.775  39.025  105.004 1.00 21.66 ? 852  LEU   B CB    1 
ATOM   14860 C  CG    . LEU   B  1 854  ? 19.804  37.845  104.032 1.00 21.23 ? 852  LEU   B CG    1 
ATOM   14861 C  CD1   . LEU   B  1 854  ? 20.494  36.635  104.657 1.00 20.02 ? 852  LEU   B CD1   1 
ATOM   14862 C  CD2   . LEU   B  1 854  ? 18.389  37.488  103.585 1.00 19.66 ? 852  LEU   B CD2   1 
ATOM   14863 N  N     . GLN   B  1 855  ? 18.141  41.787  106.052 1.00 20.62 ? 853  GLN   B N     1 
ATOM   14864 C  CA    . GLN   B  1 855  ? 18.124  42.664  107.214 1.00 21.36 ? 853  GLN   B CA    1 
ATOM   14865 C  C     . GLN   B  1 855  ? 18.905  42.010  108.344 1.00 22.81 ? 853  GLN   B C     1 
ATOM   14866 O  O     . GLN   B  1 855  ? 18.757  40.810  108.604 1.00 21.99 ? 853  GLN   B O     1 
ATOM   14867 C  CB    . GLN   B  1 855  ? 16.694  42.957  107.661 1.00 20.99 ? 853  GLN   B CB    1 
ATOM   14868 C  CG    . GLN   B  1 855  ? 16.626  44.107  108.657 1.00 25.13 ? 853  GLN   B CG    1 
ATOM   14869 C  CD    . GLN   B  1 855  ? 15.219  44.412  109.107 1.00 25.31 ? 853  GLN   B CD    1 
ATOM   14870 O  OE1   . GLN   B  1 855  ? 14.289  44.413  108.309 1.00 26.62 ? 853  GLN   B OE1   1 
ATOM   14871 N  NE2   . GLN   B  1 855  ? 15.054  44.671  110.398 1.00 30.15 ? 853  GLN   B NE2   1 
ATOM   14872 N  N     . GLU   B  1 856  ? 19.744  42.815  109.004 1.00 24.77 ? 854  GLU   B N     1 
ATOM   14873 C  CA    . GLU   B  1 856  ? 20.734  42.288  109.945 1.00 23.97 ? 854  GLU   B CA    1 
ATOM   14874 C  C     . GLU   B  1 856  ? 20.095  41.397  111.003 1.00 26.67 ? 854  GLU   B C     1 
ATOM   14875 O  O     . GLU   B  1 856  ? 20.659  40.364  111.377 1.00 28.15 ? 854  GLU   B O     1 
ATOM   14876 C  CB    . GLU   B  1 856  ? 21.488  43.448  110.602 1.00 27.88 ? 854  GLU   B CB    1 
ATOM   14877 N  N     . ASP   B  1 857  ? 18.896  41.762  111.472 1.00 26.05 ? 855  ASP   B N     1 
ATOM   14878 C  CA    . ASP   B  1 857  ? 18.250  41.048  112.572 1.00 26.59 ? 855  ASP   B CA    1 
ATOM   14879 C  C     . ASP   B  1 857  ? 17.810  39.636  112.200 1.00 27.93 ? 855  ASP   B C     1 
ATOM   14880 O  O     . ASP   B  1 857  ? 17.632  38.804  113.095 1.00 31.21 ? 855  ASP   B O     1 
ATOM   14881 C  CB    . ASP   B  1 857  ? 17.042  41.847  113.078 1.00 31.84 ? 855  ASP   B CB    1 
ATOM   14882 N  N     . VAL   B  1 858  ? 17.607  39.333  110.918 1.00 25.69 ? 856  VAL   B N     1 
ATOM   14883 C  CA    . VAL   B  1 858  ? 17.211  37.987  110.524 1.00 23.76 ? 856  VAL   B CA    1 
ATOM   14884 C  C     . VAL   B  1 858  ? 18.264  37.285  109.690 1.00 23.15 ? 856  VAL   B C     1 
ATOM   14885 O  O     . VAL   B  1 858  ? 18.050  36.126  109.307 1.00 23.68 ? 856  VAL   B O     1 
ATOM   14886 C  CB    . VAL   B  1 858  ? 15.860  37.982  109.784 1.00 26.52 ? 856  VAL   B CB    1 
ATOM   14887 C  CG1   . VAL   B  1 858  ? 14.750  38.443  110.713 1.00 28.36 ? 856  VAL   B CG1   1 
ATOM   14888 C  CG2   . VAL   B  1 858  ? 15.927  38.839  108.527 1.00 23.06 ? 856  VAL   B CG2   1 
ATOM   14889 N  N     . ALA   B  1 859  ? 19.404  37.933  109.419 1.00 22.99 ? 857  ALA   B N     1 
ATOM   14890 C  CA    . ALA   B  1 859  ? 20.357  37.395  108.452 1.00 23.84 ? 857  ALA   B CA    1 
ATOM   14891 C  C     . ALA   B  1 859  ? 20.884  36.026  108.873 1.00 24.72 ? 857  ALA   B C     1 
ATOM   14892 O  O     . ALA   B  1 859  ? 20.949  35.102  108.053 1.00 23.11 ? 857  ALA   B O     1 
ATOM   14893 C  CB    . ALA   B  1 859  ? 21.509  38.379  108.253 1.00 23.99 ? 857  ALA   B CB    1 
ATOM   14894 N  N     . ASP   B  1 860  ? 21.253  35.872  110.151 1.00 28.70 ? 858  ASP   B N     1 
ATOM   14895 C  CA    . ASP   B  1 860  ? 21.836  34.612  110.606 1.00 26.43 ? 858  ASP   B CA    1 
ATOM   14896 C  C     . ASP   B  1 860  ? 20.856  33.454  110.486 1.00 22.81 ? 858  ASP   B C     1 
ATOM   14897 O  O     . ASP   B  1 860  ? 21.232  32.371  110.022 1.00 27.14 ? 858  ASP   B O     1 
ATOM   14898 C  CB    . ASP   B  1 860  ? 22.326  34.737  112.050 1.00 29.97 ? 858  ASP   B CB    1 
ATOM   14899 C  CG    . ASP   B  1 860  ? 23.630  35.498  112.153 1.00 31.99 ? 858  ASP   B CG    1 
ATOM   14900 O  OD1   . ASP   B  1 860  ? 24.447  35.423  111.208 1.00 37.09 ? 858  ASP   B OD1   1 
ATOM   14901 O  OD2   . ASP   B  1 860  ? 23.831  36.181  113.172 1.00 42.08 ? 858  ASP   B OD2   1 
ATOM   14902 N  N     . ARG   B  1 861  ? 19.600  33.651  110.909 1.00 21.41 ? 859  ARG   B N     1 
ATOM   14903 C  CA    . ARG   B  1 861  ? 18.631  32.562  110.846 1.00 22.21 ? 859  ARG   B CA    1 
ATOM   14904 C  C     . ARG   B  1 861  ? 18.357  32.161  109.401 1.00 22.69 ? 859  ARG   B C     1 
ATOM   14905 O  O     . ARG   B  1 861  ? 18.276  30.968  109.077 1.00 23.13 ? 859  ARG   B O     1 
ATOM   14906 C  CB    . ARG   B  1 861  ? 17.331  32.962  111.543 1.00 24.17 ? 859  ARG   B CB    1 
ATOM   14907 N  N     . ILE   B  1 862  ? 18.232  33.143  108.513 1.00 21.86 ? 860  ILE   B N     1 
ATOM   14908 C  CA    . ILE   B  1 862  ? 17.960  32.819  107.118 1.00 19.17 ? 860  ILE   B CA    1 
ATOM   14909 C  C     . ILE   B  1 862  ? 19.166  32.141  106.483 1.00 20.04 ? 860  ILE   B C     1 
ATOM   14910 O  O     . ILE   B  1 862  ? 19.022  31.176  105.725 1.00 22.96 ? 860  ILE   B O     1 
ATOM   14911 C  CB    . ILE   B  1 862  ? 17.532  34.089  106.365 1.00 21.84 ? 860  ILE   B CB    1 
ATOM   14912 C  CG1   . ILE   B  1 862  ? 16.181  34.562  106.917 1.00 25.03 ? 860  ILE   B CG1   1 
ATOM   14913 C  CG2   . ILE   B  1 862  ? 17.440  33.823  104.864 1.00 22.24 ? 860  ILE   B CG2   1 
ATOM   14914 C  CD1   . ILE   B  1 862  ? 15.690  35.874  106.332 1.00 24.53 ? 860  ILE   B CD1   1 
ATOM   14915 N  N     . LEU   B  1 863  ? 20.374  32.619  106.789 1.00 21.91 ? 861  LEU   B N     1 
ATOM   14916 C  CA    . LEU   B  1 863  ? 21.573  31.986  106.248 1.00 24.31 ? 861  LEU   B CA    1 
ATOM   14917 C  C     . LEU   B  1 863  ? 21.700  30.542  106.721 1.00 23.10 ? 861  LEU   B C     1 
ATOM   14918 O  O     . LEU   B  1 863  ? 22.037  29.650  105.933 1.00 22.45 ? 861  LEU   B O     1 
ATOM   14919 C  CB    . LEU   B  1 863  ? 22.816  32.788  106.640 1.00 22.78 ? 861  LEU   B CB    1 
ATOM   14920 C  CG    . LEU   B  1 863  ? 23.063  34.070  105.850 1.00 26.55 ? 861  LEU   B CG    1 
ATOM   14921 C  CD1   . LEU   B  1 863  ? 24.181  34.883  106.500 1.00 25.32 ? 861  LEU   B CD1   1 
ATOM   14922 C  CD2   . LEU   B  1 863  ? 23.395  33.738  104.398 1.00 27.95 ? 861  LEU   B CD2   1 
ATOM   14923 N  N     . THR   B  1 864  ? 21.433  30.291  108.005 1.00 21.83 ? 862  THR   B N     1 
ATOM   14924 C  CA    . THR   B  1 864  ? 21.470  28.921  108.507 1.00 22.94 ? 862  THR   B CA    1 
ATOM   14925 C  C     . THR   B  1 864  ? 20.490  28.033  107.747 1.00 23.88 ? 862  THR   B C     1 
ATOM   14926 O  O     . THR   B  1 864  ? 20.837  26.927  107.316 1.00 21.74 ? 862  THR   B O     1 
ATOM   14927 C  CB    . THR   B  1 864  ? 21.158  28.912  109.999 1.00 26.91 ? 862  THR   B CB    1 
ATOM   14928 O  OG1   . THR   B  1 864  ? 22.170  29.654  110.674 1.00 23.97 ? 862  THR   B OG1   1 
ATOM   14929 C  CG2   . THR   B  1 864  ? 21.129  27.489  110.534 1.00 30.28 ? 862  THR   B CG2   1 
ATOM   14930 N  N     . MET   B  1 865  ? 19.260  28.514  107.563 1.00 20.68 ? 863  MET   B N     1 
ATOM   14931 C  CA    . MET   B  1 865  ? 18.260  27.755  106.822 1.00 21.95 ? 863  MET   B CA    1 
ATOM   14932 C  C     . MET   B  1 865  ? 18.668  27.591  105.364 1.00 21.54 ? 863  MET   B C     1 
ATOM   14933 O  O     . MET   B  1 865  ? 18.521  26.510  104.778 1.00 19.02 ? 863  MET   B O     1 
ATOM   14934 C  CB    . MET   B  1 865  ? 16.912  28.470  106.920 1.00 20.80 ? 863  MET   B CB    1 
ATOM   14935 C  CG    . MET   B  1 865  ? 15.745  27.700  106.349 1.00 27.13 ? 863  MET   B CG    1 
ATOM   14936 S  SD    . MET   B  1 865  ? 14.176  28.570  106.602 1.00 31.58 ? 863  MET   B SD    1 
ATOM   14937 C  CE    . MET   B  1 865  ? 14.428  29.134  108.288 1.00 26.02 ? 863  MET   B CE    1 
ATOM   14938 N  N     . LEU   B  1 866  ? 19.173  28.666  104.762 1.00 20.02 ? 864  LEU   B N     1 
ATOM   14939 C  CA    . LEU   B  1 866  ? 19.601  28.609  103.369 1.00 20.55 ? 864  LEU   B CA    1 
ATOM   14940 C  C     . LEU   B  1 866  ? 20.712  27.587  103.189 1.00 22.33 ? 864  LEU   B C     1 
ATOM   14941 O  O     . LEU   B  1 866  ? 20.691  26.779  102.251 1.00 21.69 ? 864  LEU   B O     1 
ATOM   14942 C  CB    . LEU   B  1 866  ? 20.065  29.996  102.921 1.00 21.71 ? 864  LEU   B CB    1 
ATOM   14943 C  CG    . LEU   B  1 866  ? 20.617  30.074  101.507 1.00 23.77 ? 864  LEU   B CG    1 
ATOM   14944 C  CD1   . LEU   B  1 866  ? 19.510  29.763  100.529 1.00 25.46 ? 864  LEU   B CD1   1 
ATOM   14945 C  CD2   . LEU   B  1 866  ? 21.183  31.461  101.251 1.00 27.74 ? 864  LEU   B CD2   1 
ATOM   14946 N  N     . LYS   B  1 867  ? 21.693  27.601  104.095 1.00 21.09 ? 865  LYS   B N     1 
ATOM   14947 C  CA    . LYS   B  1 867  ? 22.781  26.632  104.019 1.00 21.14 ? 865  LYS   B CA    1 
ATOM   14948 C  C     . LYS   B  1 867  ? 22.272  25.211  104.211 1.00 24.42 ? 865  LYS   B C     1 
ATOM   14949 O  O     . LYS   B  1 867  ? 22.729  24.286  103.531 1.00 20.79 ? 865  LYS   B O     1 
ATOM   14950 C  CB    . LYS   B  1 867  ? 23.854  26.963  105.056 1.00 22.04 ? 865  LYS   B CB    1 
ATOM   14951 C  CG    . LYS   B  1 867  ? 24.611  28.234  104.731 1.00 21.51 ? 865  LYS   B CG    1 
ATOM   14952 C  CD    . LYS   B  1 867  ? 25.533  28.612  105.858 1.00 27.94 ? 865  LYS   B CD    1 
ATOM   14953 C  CE    . LYS   B  1 867  ? 26.318  29.871  105.538 1.00 35.40 ? 865  LYS   B CE    1 
ATOM   14954 N  NZ    . LYS   B  1 867  ? 27.134  30.282  106.714 1.00 39.42 ? 865  LYS   B NZ    1 
ATOM   14955 N  N     . GLY   B  1 868  ? 21.322  25.013  105.127 1.00 21.53 ? 866  GLY   B N     1 
ATOM   14956 C  CA    . GLY   B  1 868  ? 20.765  23.681  105.300 1.00 21.44 ? 866  GLY   B CA    1 
ATOM   14957 C  C     . GLY   B  1 868  ? 20.028  23.210  104.064 1.00 21.57 ? 866  GLY   B C     1 
ATOM   14958 O  O     . GLY   B  1 868  ? 20.147  22.052  103.656 1.00 22.11 ? 866  GLY   B O     1 
ATOM   14959 N  N     . ALA   B  1 869  ? 19.280  24.114  103.433 1.00 17.89 ? 867  ALA   B N     1 
ATOM   14960 C  CA    . ALA   B  1 869  ? 18.566  23.767  102.209 1.00 19.74 ? 867  ALA   B CA    1 
ATOM   14961 C  C     . ALA   B  1 869  ? 19.538  23.477  101.077 1.00 20.83 ? 867  ALA   B C     1 
ATOM   14962 O  O     . ALA   B  1 869  ? 19.303  22.575  100.265 1.00 22.14 ? 867  ALA   B O     1 
ATOM   14963 C  CB    . ALA   B  1 869  ? 17.623  24.905  101.814 1.00 20.67 ? 867  ALA   B CB    1 
ATOM   14964 N  N     . LEU   B  1 870  ? 20.633  24.239  101.007 1.00 18.44 ? 868  LEU   B N     1 
ATOM   14965 C  CA    . LEU   B  1 870  ? 21.621  24.028  99.952  1.00 21.08 ? 868  LEU   B CA    1 
ATOM   14966 C  C     . LEU   B  1 870  ? 22.177  22.616  100.006 1.00 22.92 ? 868  LEU   B C     1 
ATOM   14967 O  O     . LEU   B  1 870  ? 22.385  21.982  98.970  1.00 22.17 ? 868  LEU   B O     1 
ATOM   14968 C  CB    . LEU   B  1 870  ? 22.758  25.052  100.072 1.00 22.87 ? 868  LEU   B CB    1 
ATOM   14969 N  N     . HIS   B  1 871  ? 22.383  22.085  101.206 1.00 18.76 ? 869  HIS   B N     1 
ATOM   14970 C  CA    . HIS   B  1 871  ? 23.006  20.779  101.282 1.00 23.94 ? 869  HIS   B CA    1 
ATOM   14971 C  C     . HIS   B  1 871  ? 22.054  19.649  100.918 1.00 22.80 ? 869  HIS   B C     1 
ATOM   14972 O  O     . HIS   B  1 871  ? 22.500  18.508  100.802 1.00 22.77 ? 869  HIS   B O     1 
ATOM   14973 C  CB    . HIS   B  1 871  ? 23.618  20.588  102.671 1.00 28.80 ? 869  HIS   B CB    1 
ATOM   14974 C  CG    . HIS   B  1 871  ? 24.871  21.389  102.871 1.00 34.34 ? 869  HIS   B CG    1 
ATOM   14975 N  ND1   . HIS   B  1 871  ? 26.063  21.071  102.250 1.00 35.45 ? 869  HIS   B ND1   1 
ATOM   14976 C  CD2   . HIS   B  1 871  ? 25.113  22.511  103.593 1.00 30.56 ? 869  HIS   B CD2   1 
ATOM   14977 C  CE1   . HIS   B  1 871  ? 26.984  21.954  102.591 1.00 35.71 ? 869  HIS   B CE1   1 
ATOM   14978 N  NE2   . HIS   B  1 871  ? 26.435  22.837  103.405 1.00 35.62 ? 869  HIS   B NE2   1 
ATOM   14979 N  N     . GLU   B  1 872  ? 20.777  19.939  100.692 1.00 18.12 ? 870  GLU   B N     1 
ATOM   14980 C  CA    . GLU   B  1 872  ? 19.842  18.925  100.218 1.00 18.55 ? 870  GLU   B CA    1 
ATOM   14981 C  C     . GLU   B  1 872  ? 19.757  18.861  98.703  1.00 22.66 ? 870  GLU   B C     1 
ATOM   14982 O  O     . GLU   B  1 872  ? 18.985  18.057  98.177  1.00 20.07 ? 870  GLU   B O     1 
ATOM   14983 C  CB    . GLU   B  1 872  ? 18.446  19.176  100.801 1.00 20.33 ? 870  GLU   B CB    1 
ATOM   14984 C  CG    . GLU   B  1 872  ? 18.424  19.126  102.321 1.00 21.92 ? 870  GLU   B CG    1 
ATOM   14985 C  CD    . GLU   B  1 872  ? 18.781  17.751  102.871 1.00 23.98 ? 870  GLU   B CD    1 
ATOM   14986 O  OE1   . GLU   B  1 872  ? 18.590  16.743  102.153 1.00 25.34 ? 870  GLU   B OE1   1 
ATOM   14987 O  OE2   . GLU   B  1 872  ? 19.245  17.678  104.030 1.00 26.27 ? 870  GLU   B OE2   1 
ATOM   14988 N  N     . LEU   B  1 873  ? 20.521  19.686  97.997  1.00 19.46 ? 871  LEU   B N     1 
ATOM   14989 C  CA    . LEU   B  1 873  ? 20.445  19.732  96.545  1.00 22.04 ? 871  LEU   B CA    1 
ATOM   14990 C  C     . LEU   B  1 873  ? 21.284  18.627  95.933  1.00 23.28 ? 871  LEU   B C     1 
ATOM   14991 O  O     . LEU   B  1 873  ? 22.379  18.327  96.406  1.00 21.52 ? 871  LEU   B O     1 
ATOM   14992 C  CB    . LEU   B  1 873  ? 20.932  21.084  96.031  1.00 20.36 ? 871  LEU   B CB    1 
ATOM   14993 C  CG    . LEU   B  1 873  ? 20.092  22.301  96.387  1.00 22.94 ? 871  LEU   B CG    1 
ATOM   14994 C  CD1   . LEU   B  1 873  ? 20.723  23.548  95.773  1.00 22.08 ? 871  LEU   B CD1   1 
ATOM   14995 C  CD2   . LEU   B  1 873  ? 18.640  22.116  95.924  1.00 24.27 ? 871  LEU   B CD2   1 
ATOM   14996 N  N     . HIS   B  1 874  ? 20.779  18.046  94.856  1.00 21.69 ? 872  HIS   B N     1 
ATOM   14997 C  CA    . HIS   B  1 874  ? 21.483  17.010  94.118  1.00 23.46 ? 872  HIS   B CA    1 
ATOM   14998 C  C     . HIS   B  1 874  ? 22.064  17.625  92.844  1.00 21.38 ? 872  HIS   B C     1 
ATOM   14999 O  O     . HIS   B  1 874  ? 21.323  18.131  91.996  1.00 19.14 ? 872  HIS   B O     1 
ATOM   15000 C  CB    . HIS   B  1 874  ? 20.525  15.860  93.814  1.00 22.51 ? 872  HIS   B CB    1 
ATOM   15001 C  CG    . HIS   B  1 874  ? 21.130  14.752  93.020  1.00 23.64 ? 872  HIS   B CG    1 
ATOM   15002 N  ND1   . HIS   B  1 874  ? 20.408  13.648  92.625  1.00 29.36 ? 872  HIS   B ND1   1 
ATOM   15003 C  CD2   . HIS   B  1 874  ? 22.387  14.569  92.551  1.00 27.91 ? 872  HIS   B CD2   1 
ATOM   15004 C  CE1   . HIS   B  1 874  ? 21.191  12.837  91.938  1.00 27.04 ? 872  HIS   B CE1   1 
ATOM   15005 N  NE2   . HIS   B  1 874  ? 22.395  13.375  91.876  1.00 30.14 ? 872  HIS   B NE2   1 
ATOM   15006 N  N     . ILE   B  1 875  ? 23.389  17.605  92.723  1.00 21.24 ? 873  ILE   B N     1 
ATOM   15007 C  CA    . ILE   B  1 875  ? 24.086  18.158  91.567  1.00 23.50 ? 873  ILE   B CA    1 
ATOM   15008 C  C     . ILE   B  1 875  ? 24.608  17.002  90.731  1.00 24.61 ? 873  ILE   B C     1 
ATOM   15009 O  O     . ILE   B  1 875  ? 25.224  16.075  91.271  1.00 22.99 ? 873  ILE   B O     1 
ATOM   15010 C  CB    . ILE   B  1 875  ? 25.238  19.080  91.998  1.00 21.74 ? 873  ILE   B CB    1 
ATOM   15011 C  CG1   . ILE   B  1 875  ? 24.690  20.297  92.744  1.00 29.42 ? 873  ILE   B CG1   1 
ATOM   15012 C  CG2   . ILE   B  1 875  ? 26.058  19.525  90.800  1.00 19.78 ? 873  ILE   B CG2   1 
ATOM   15013 C  CD1   . ILE   B  1 875  ? 24.709  20.143  94.255  1.00 34.77 ? 873  ILE   B CD1   1 
ATOM   15014 N  N     . GLY   B  1 876  ? 24.377  17.050  89.422  1.00 20.33 ? 874  GLY   B N     1 
ATOM   15015 C  CA    . GLY   B  1 876  ? 24.904  16.001  88.572  1.00 24.30 ? 874  GLY   B CA    1 
ATOM   15016 C  C     . GLY   B  1 876  ? 24.365  16.109  87.161  1.00 23.40 ? 874  GLY   B C     1 
ATOM   15017 O  O     . GLY   B  1 876  ? 23.743  17.107  86.785  1.00 19.03 ? 874  GLY   B O     1 
ATOM   15018 N  N     . ARG   B  1 877  ? 24.650  15.069  86.379  1.00 24.22 ? 875  ARG   B N     1 
ATOM   15019 C  CA    . ARG   B  1 877  ? 24.171  15.026  85.005  1.00 23.64 ? 875  ARG   B CA    1 
ATOM   15020 C  C     . ARG   B  1 877  ? 22.651  15.007  85.011  1.00 20.47 ? 875  ARG   B C     1 
ATOM   15021 O  O     . ARG   B  1 877  ? 22.038  14.275  85.792  1.00 21.31 ? 875  ARG   B O     1 
ATOM   15022 C  CB    . ARG   B  1 877  ? 24.727  13.798  84.293  1.00 26.10 ? 875  ARG   B CB    1 
ATOM   15023 C  CG    . ARG   B  1 877  ? 24.715  13.906  82.791  1.00 27.89 ? 875  ARG   B CG    1 
ATOM   15024 C  CD    . ARG   B  1 877  ? 25.413  12.699  82.182  1.00 29.36 ? 875  ARG   B CD    1 
ATOM   15025 N  NE    . ARG   B  1 877  ? 24.514  11.562  82.069  1.00 27.32 ? 875  ARG   B NE    1 
ATOM   15026 C  CZ    . ARG   B  1 877  ? 24.839  10.411  81.498  1.00 37.94 ? 875  ARG   B CZ    1 
ATOM   15027 N  NH1   . ARG   B  1 877  ? 26.065  10.182  81.054  1.00 33.62 ? 875  ARG   B NH1   1 
ATOM   15028 N  NH2   . ARG   B  1 877  ? 23.909  9.468   81.366  1.00 37.77 ? 875  ARG   B NH2   1 
ATOM   15029 N  N     . THR   B  1 878  ? 22.045  15.834  84.160  1.00 19.09 ? 876  THR   B N     1 
ATOM   15030 C  CA    . THR   B  1 878  ? 20.642  16.200  84.304  1.00 20.37 ? 876  THR   B CA    1 
ATOM   15031 C  C     . THR   B  1 878  ? 19.680  15.240  83.623  1.00 20.17 ? 876  THR   B C     1 
ATOM   15032 O  O     . THR   B  1 878  ? 18.486  15.546  83.536  1.00 21.57 ? 876  THR   B O     1 
ATOM   15033 C  CB    . THR   B  1 878  ? 20.416  17.615  83.776  1.00 19.35 ? 876  THR   B CB    1 
ATOM   15034 O  OG1   . THR   B  1 878  ? 20.986  17.737  82.468  1.00 23.51 ? 876  THR   B OG1   1 
ATOM   15035 C  CG2   . THR   B  1 878  ? 21.081  18.614  84.680  1.00 20.07 ? 876  THR   B CG2   1 
ATOM   15036 N  N     . ASP   B  1 879  ? 20.150  14.078  83.158  1.00 23.97 ? 877  ASP   B N     1 
ATOM   15037 C  CA    . ASP   B  1 879  ? 19.237  13.056  82.655  1.00 22.38 ? 877  ASP   B CA    1 
ATOM   15038 C  C     . ASP   B  1 879  ? 18.691  12.165  83.771  1.00 21.29 ? 877  ASP   B C     1 
ATOM   15039 O  O     . ASP   B  1 879  ? 18.314  11.008  83.524  1.00 23.01 ? 877  ASP   B O     1 
ATOM   15040 C  CB    . ASP   B  1 879  ? 19.907  12.226  81.557  1.00 24.36 ? 877  ASP   B CB    1 
ATOM   15041 C  CG    . ASP   B  1 879  ? 21.084  11.415  82.056  1.00 27.74 ? 877  ASP   B CG    1 
ATOM   15042 O  OD1   . ASP   B  1 879  ? 21.787  11.857  82.993  1.00 30.92 ? 877  ASP   B OD1   1 
ATOM   15043 O  OD2   . ASP   B  1 879  ? 21.304  10.326  81.494  1.00 29.40 ? 877  ASP   B OD2   1 
ATOM   15044 N  N     . ARG   B  1 880  ? 18.613  12.697  84.990  1.00 23.50 ? 878  ARG   B N     1 
ATOM   15045 C  CA    . ARG   B  1 880  ? 17.929  12.071  86.115  1.00 23.37 ? 878  ARG   B CA    1 
ATOM   15046 C  C     . ARG   B  1 880  ? 16.980  13.089  86.727  1.00 20.08 ? 878  ARG   B C     1 
ATOM   15047 O  O     . ARG   B  1 880  ? 17.374  14.229  86.995  1.00 20.36 ? 878  ARG   B O     1 
ATOM   15048 C  CB    . ARG   B  1 880  ? 18.906  11.574  87.184  1.00 22.72 ? 878  ARG   B CB    1 
ATOM   15049 C  CG    . ARG   B  1 880  ? 19.699  10.331  86.796  1.00 33.91 ? 878  ARG   B CG    1 
ATOM   15050 C  CD    . ARG   B  1 880  ? 20.584  9.860   87.955  1.00 34.85 ? 878  ARG   B CD    1 
ATOM   15051 N  NE    . ARG   B  1 880  ? 21.487  8.786   87.554  1.00 48.83 ? 878  ARG   B NE    1 
ATOM   15052 C  CZ    . ARG   B  1 880  ? 21.308  7.501   87.835  1.00 52.34 ? 878  ARG   B CZ    1 
ATOM   15053 N  NH1   . ARG   B  1 880  ? 20.276  7.085   88.552  1.00 54.08 ? 878  ARG   B NH1   1 
ATOM   15054 N  NH2   . ARG   B  1 880  ? 22.188  6.610   87.384  1.00 54.05 ? 878  ARG   B NH2   1 
ATOM   15055 N  N     . LEU   B  1 881  ? 15.731  12.676  86.935  1.00 19.64 ? 879  LEU   B N     1 
ATOM   15056 C  CA    . LEU   B  1 881  ? 14.737  13.566  87.528  1.00 19.88 ? 879  LEU   B CA    1 
ATOM   15057 C  C     . LEU   B  1 881  ? 15.191  14.095  88.884  1.00 21.23 ? 879  LEU   B C     1 
ATOM   15058 O  O     . LEU   B  1 881  ? 14.885  15.236  89.244  1.00 20.01 ? 879  LEU   B O     1 
ATOM   15059 C  CB    . LEU   B  1 881  ? 13.409  12.820  87.663  1.00 20.76 ? 879  LEU   B CB    1 
ATOM   15060 C  CG    . LEU   B  1 881  ? 12.234  13.611  88.242  1.00 23.84 ? 879  LEU   B CG    1 
ATOM   15061 C  CD1   . LEU   B  1 881  ? 11.815  14.714  87.282  1.00 24.57 ? 879  LEU   B CD1   1 
ATOM   15062 C  CD2   . LEU   B  1 881  ? 11.078  12.671  88.552  1.00 21.02 ? 879  LEU   B CD2   1 
ATOM   15063 N  N     . SER   B  1 882  ? 15.939  13.295  89.638  1.00 17.82 ? 880  SER   B N     1 
ATOM   15064 C  CA    . SER   B  1 882  ? 16.354  13.695  90.974  1.00 21.54 ? 880  SER   B CA    1 
ATOM   15065 C  C     . SER   B  1 882  ? 17.417  14.785  90.973  1.00 19.70 ? 880  SER   B C     1 
ATOM   15066 O  O     . SER   B  1 882  ? 17.774  15.275  92.048  1.00 21.73 ? 880  SER   B O     1 
ATOM   15067 C  CB    . SER   B  1 882  ? 16.870  12.473  91.738  1.00 22.56 ? 880  SER   B CB    1 
ATOM   15068 O  OG    . SER   B  1 882  ? 18.016  11.931  91.110  1.00 22.92 ? 880  SER   B OG    1 
ATOM   15069 N  N     . VAL   B  1 883  ? 17.942  15.175  89.815  1.00 19.02 ? 881  VAL   B N     1 
ATOM   15070 C  CA    . VAL   B  1 883  ? 18.984  16.198  89.789  1.00 16.13 ? 881  VAL   B CA    1 
ATOM   15071 C  C     . VAL   B  1 883  ? 18.344  17.576  89.866  1.00 16.63 ? 881  VAL   B C     1 
ATOM   15072 O  O     . VAL   B  1 883  ? 17.457  17.919  89.073  1.00 19.81 ? 881  VAL   B O     1 
ATOM   15073 C  CB    . VAL   B  1 883  ? 19.868  16.053  88.540  1.00 19.59 ? 881  VAL   B CB    1 
ATOM   15074 C  CG1   . VAL   B  1 883  ? 20.757  17.287  88.375  1.00 19.06 ? 881  VAL   B CG1   1 
ATOM   15075 C  CG2   . VAL   B  1 883  ? 20.714  14.801  88.669  1.00 19.47 ? 881  VAL   B CG2   1 
ATOM   15076 N  N     . ASP   B  1 884  ? 18.803  18.370  90.824  1.00 19.25 ? 882  ASP   B N     1 
ATOM   15077 C  CA    . ASP   B  1 884  ? 18.329  19.729  91.026  1.00 20.57 ? 882  ASP   B CA    1 
ATOM   15078 C  C     . ASP   B  1 884  ? 19.123  20.738  90.216  1.00 23.38 ? 882  ASP   B C     1 
ATOM   15079 O  O     . ASP   B  1 884  ? 18.545  21.647  89.609  1.00 22.12 ? 882  ASP   B O     1 
ATOM   15080 C  CB    . ASP   B  1 884  ? 18.418  20.076  92.515  1.00 19.51 ? 882  ASP   B CB    1 
ATOM   15081 C  CG    . ASP   B  1 884  ? 17.577  19.141  93.370  1.00 20.53 ? 882  ASP   B CG    1 
ATOM   15082 O  OD1   . ASP   B  1 884  ? 16.375  18.986  93.059  1.00 21.27 ? 882  ASP   B OD1   1 
ATOM   15083 O  OD2   . ASP   B  1 884  ? 18.126  18.543  94.323  1.00 20.91 ? 882  ASP   B OD2   1 
ATOM   15084 N  N     . VAL   B  1 885  ? 20.443  20.589  90.204  1.00 20.75 ? 883  VAL   B N     1 
ATOM   15085 C  CA    . VAL   B  1 885  ? 21.348  21.555  89.597  1.00 23.30 ? 883  VAL   B CA    1 
ATOM   15086 C  C     . VAL   B  1 885  ? 22.297  20.802  88.678  1.00 20.97 ? 883  VAL   B C     1 
ATOM   15087 O  O     . VAL   B  1 885  ? 22.955  19.848  89.108  1.00 19.89 ? 883  VAL   B O     1 
ATOM   15088 C  CB    . VAL   B  1 885  ? 22.128  22.341  90.663  1.00 26.08 ? 883  VAL   B CB    1 
ATOM   15089 C  CG1   . VAL   B  1 885  ? 23.134  23.304  90.010  1.00 23.48 ? 883  VAL   B CG1   1 
ATOM   15090 C  CG2   . VAL   B  1 885  ? 21.149  23.091  91.573  1.00 24.53 ? 883  VAL   B CG2   1 
ATOM   15091 N  N     . GLY   B  1 886  ? 22.353  21.218  87.420  1.00 18.67 ? 884  GLY   B N     1 
ATOM   15092 C  CA    . GLY   B  1 886  ? 23.224  20.590  86.460  1.00 20.09 ? 884  GLY   B CA    1 
ATOM   15093 C  C     . GLY   B  1 886  ? 24.552  21.303  86.348  1.00 17.42 ? 884  GLY   B C     1 
ATOM   15094 O  O     . GLY   B  1 886  ? 24.957  22.074  87.227  1.00 18.37 ? 884  GLY   B O     1 
ATOM   15095 N  N     . PRO   B  1 887  ? 25.247  21.066  85.244  1.00 19.73 ? 885  PRO   B N     1 
ATOM   15096 C  CA    . PRO   B  1 887  ? 26.581  21.641  85.055  1.00 17.63 ? 885  PRO   B CA    1 
ATOM   15097 C  C     . PRO   B  1 887  ? 26.507  23.082  84.577  1.00 18.93 ? 885  PRO   B C     1 
ATOM   15098 O  O     . PRO   B  1 887  ? 25.474  23.561  84.108  1.00 16.19 ? 885  PRO   B O     1 
ATOM   15099 C  CB    . PRO   B  1 887  ? 27.179  20.753  83.965  1.00 18.20 ? 885  PRO   B CB    1 
ATOM   15100 C  CG    . PRO   B  1 887  ? 25.960  20.377  83.136  1.00 17.89 ? 885  PRO   B CG    1 
ATOM   15101 C  CD    . PRO   B  1 887  ? 24.887  20.138  84.161  1.00 16.49 ? 885  PRO   B CD    1 
ATOM   15102 N  N     . VAL   B  1 888  ? 27.654  23.757  84.656  1.00 19.30 ? 886  VAL   B N     1 
ATOM   15103 C  CA    . VAL   B  1 888  ? 27.810  24.975  83.880  1.00 19.03 ? 886  VAL   B CA    1 
ATOM   15104 C  C     . VAL   B  1 888  ? 28.231  24.614  82.461  1.00 18.98 ? 886  VAL   B C     1 
ATOM   15105 O  O     . VAL   B  1 888  ? 28.679  23.501  82.179  1.00 21.01 ? 886  VAL   B O     1 
ATOM   15106 C  CB    . VAL   B  1 888  ? 28.791  25.960  84.535  1.00 19.06 ? 886  VAL   B CB    1 
ATOM   15107 C  CG1   . VAL   B  1 888  ? 28.242  26.411  85.895  1.00 18.91 ? 886  VAL   B CG1   1 
ATOM   15108 C  CG2   . VAL   B  1 888  ? 30.166  25.361  84.654  1.00 18.76 ? 886  VAL   B CG2   1 
ATOM   15109 N  N     . ILE   B  1 889  ? 28.065  25.571  81.548  1.00 18.04 ? 887  ILE   B N     1 
ATOM   15110 C  CA    . ILE   B  1 889  ? 27.993  25.218  80.130  1.00 17.48 ? 887  ILE   B CA    1 
ATOM   15111 C  C     . ILE   B  1 889  ? 29.338  24.714  79.593  1.00 19.46 ? 887  ILE   B C     1 
ATOM   15112 O  O     . ILE   B  1 889  ? 29.371  23.811  78.749  1.00 17.57 ? 887  ILE   B O     1 
ATOM   15113 C  CB    . ILE   B  1 889  ? 27.450  26.416  79.325  1.00 16.38 ? 887  ILE   B CB    1 
ATOM   15114 C  CG1   . ILE   B  1 889  ? 27.222  26.027  77.860  1.00 18.70 ? 887  ILE   B CG1   1 
ATOM   15115 C  CG2   . ILE   B  1 889  ? 28.385  27.633  79.443  1.00 19.64 ? 887  ILE   B CG2   1 
ATOM   15116 C  CD1   . ILE   B  1 889  ? 26.145  24.972  77.684  1.00 18.47 ? 887  ILE   B CD1   1 
ATOM   15117 N  N     . THR   B  1 890  ? 30.462  25.261  80.069  1.00 20.06 ? 888  THR   B N     1 
ATOM   15118 C  CA    . THR   B  1 890  ? 31.775  24.920  79.519  1.00 19.20 ? 888  THR   B CA    1 
ATOM   15119 C  C     . THR   B  1 890  ? 32.835  24.947  80.610  1.00 20.86 ? 888  THR   B C     1 
ATOM   15120 O  O     . THR   B  1 890  ? 32.624  25.497  81.690  1.00 19.77 ? 888  THR   B O     1 
ATOM   15121 C  CB    . THR   B  1 890  ? 32.237  25.905  78.434  1.00 21.13 ? 888  THR   B CB    1 
ATOM   15122 O  OG1   . THR   B  1 890  ? 32.296  27.221  78.993  1.00 20.88 ? 888  THR   B OG1   1 
ATOM   15123 C  CG2   . THR   B  1 890  ? 31.326  25.903  77.205  1.00 19.57 ? 888  THR   B CG2   1 
ATOM   15124 N  N     . SER   B  1 891  ? 34.015  24.391  80.287  1.00 24.34 ? 889  SER   B N     1 
ATOM   15125 C  CA    A SER   B  1 891  ? 35.168  24.505  81.182  0.52 21.72 ? 889  SER   B CA    1 
ATOM   15126 C  CA    B SER   B  1 891  ? 35.142  24.505  81.206  0.48 21.72 ? 889  SER   B CA    1 
ATOM   15127 C  C     . SER   B  1 891  ? 35.565  25.959  81.376  1.00 21.52 ? 889  SER   B C     1 
ATOM   15128 O  O     . SER   B  1 891  ? 35.966  26.363  82.470  1.00 24.72 ? 889  SER   B O     1 
ATOM   15129 C  CB    A SER   B  1 891  ? 36.368  23.722  80.633  0.52 21.51 ? 889  SER   B CB    1 
ATOM   15130 C  CB    B SER   B  1 891  ? 36.319  23.657  80.721  0.48 21.53 ? 889  SER   B CB    1 
ATOM   15131 O  OG    A SER   B  1 891  ? 36.125  22.331  80.553  0.52 25.44 ? 889  SER   B OG    1 
ATOM   15132 O  OG    B SER   B  1 891  ? 36.820  24.145  79.492  0.48 22.57 ? 889  SER   B OG    1 
ATOM   15133 N  N     . GLU   B  1 892  ? 35.484  26.759  80.303  1.00 20.90 ? 890  GLU   B N     1 
ATOM   15134 C  CA    . GLU   B  1 892  ? 35.847  28.170  80.401  1.00 24.15 ? 890  GLU   B CA    1 
ATOM   15135 C  C     . GLU   B  1 892  ? 34.938  28.890  81.382  1.00 26.01 ? 890  GLU   B C     1 
ATOM   15136 O  O     . GLU   B  1 892  ? 35.402  29.689  82.205  1.00 25.52 ? 890  GLU   B O     1 
ATOM   15137 C  CB    . GLU   B  1 892  ? 35.782  28.840  79.026  1.00 28.78 ? 890  GLU   B CB    1 
ATOM   15138 N  N     . ALA   B  1 893  ? 33.632  28.619  81.308  1.00 23.79 ? 891  ALA   B N     1 
ATOM   15139 C  CA    . ALA   B  1 893  ? 32.708  29.193  82.277  1.00 22.71 ? 891  ALA   B CA    1 
ATOM   15140 C  C     . ALA   B  1 893  ? 33.066  28.744  83.686  1.00 22.50 ? 891  ALA   B C     1 
ATOM   15141 O  O     . ALA   B  1 893  ? 33.120  29.555  84.617  1.00 21.87 ? 891  ALA   B O     1 
ATOM   15142 C  CB    . ALA   B  1 893  ? 31.273  28.790  81.934  1.00 21.72 ? 891  ALA   B CB    1 
ATOM   15143 N  N     . LYS   B  1 894  ? 33.298  27.442  83.859  1.00 19.46 ? 892  LYS   B N     1 
ATOM   15144 C  CA    . LYS   B  1 894  ? 33.665  26.924  85.167  1.00 22.87 ? 892  LYS   B CA    1 
ATOM   15145 C  C     . LYS   B  1 894  ? 34.919  27.612  85.688  1.00 25.64 ? 892  LYS   B C     1 
ATOM   15146 O  O     . LYS   B  1 894  ? 34.971  28.025  86.851  1.00 23.66 ? 892  LYS   B O     1 
ATOM   15147 C  CB    . LYS   B  1 894  ? 33.863  25.409  85.087  1.00 21.99 ? 892  LYS   B CB    1 
ATOM   15148 C  CG    . LYS   B  1 894  ? 34.394  24.790  86.380  1.00 23.49 ? 892  LYS   B CG    1 
ATOM   15149 C  CD    . LYS   B  1 894  ? 34.477  23.281  86.273  1.00 23.78 ? 892  LYS   B CD    1 
ATOM   15150 C  CE    . LYS   B  1 894  ? 35.084  22.690  87.548  1.00 26.18 ? 892  LYS   B CE    1 
ATOM   15151 N  NZ    . LYS   B  1 894  ? 35.134  21.220  87.509  1.00 36.96 ? 892  LYS   B NZ    1 
ATOM   15152 N  N     . ASP   B  1 895  ? 35.936  27.764  84.834  1.00 23.34 ? 893  ASP   B N     1 
ATOM   15153 C  CA    . ASP   B  1 895  ? 37.163  28.416  85.280  1.00 25.00 ? 893  ASP   B CA    1 
ATOM   15154 C  C     . ASP   B  1 895  ? 36.906  29.862  85.684  1.00 24.68 ? 893  ASP   B C     1 
ATOM   15155 O  O     . ASP   B  1 895  ? 37.457  30.343  86.681  1.00 27.53 ? 893  ASP   B O     1 
ATOM   15156 C  CB    . ASP   B  1 895  ? 38.225  28.363  84.182  1.00 25.71 ? 893  ASP   B CB    1 
ATOM   15157 C  CG    . ASP   B  1 895  ? 38.750  26.972  83.949  1.00 30.71 ? 893  ASP   B CG    1 
ATOM   15158 O  OD1   . ASP   B  1 895  ? 38.546  26.101  84.817  1.00 34.40 ? 893  ASP   B OD1   1 
ATOM   15159 O  OD2   . ASP   B  1 895  ? 39.381  26.753  82.898  1.00 32.53 ? 893  ASP   B OD2   1 
ATOM   15160 N  N     . ASN   B  1 896  ? 36.091  30.572  84.905  1.00 23.96 ? 894  ASN   B N     1 
ATOM   15161 C  CA    . ASN   B  1 896  ? 35.804  31.971  85.194  1.00 22.96 ? 894  ASN   B CA    1 
ATOM   15162 C  C     . ASN   B  1 896  ? 35.089  32.110  86.531  1.00 26.31 ? 894  ASN   B C     1 
ATOM   15163 O  O     . ASN   B  1 896  ? 35.426  32.986  87.337  1.00 24.33 ? 894  ASN   B O     1 
ATOM   15164 C  CB    . ASN   B  1 896  ? 34.975  32.561  84.049  1.00 28.17 ? 894  ASN   B CB    1 
ATOM   15165 C  CG    . ASN   B  1 896  ? 34.495  33.978  84.324  1.00 38.68 ? 894  ASN   B CG    1 
ATOM   15166 O  OD1   . ASN   B  1 896  ? 33.622  34.201  85.161  1.00 41.08 ? 894  ASN   B OD1   1 
ATOM   15167 N  ND2   . ASN   B  1 896  ? 35.032  34.938  83.581  1.00 45.79 ? 894  ASN   B ND2   1 
ATOM   15168 N  N     . ILE   B  1 897  ? 34.101  31.246  86.782  1.00 21.77 ? 895  ILE   B N     1 
ATOM   15169 C  CA    . ILE   B  1 897  ? 33.373  31.270  88.050  1.00 27.73 ? 895  ILE   B CA    1 
ATOM   15170 C  C     . ILE   B  1 897  ? 34.301  30.910  89.205  1.00 27.34 ? 895  ILE   B C     1 
ATOM   15171 O  O     . ILE   B  1 897  ? 34.330  31.588  90.243  1.00 26.84 ? 895  ILE   B O     1 
ATOM   15172 C  CB    . ILE   B  1 897  ? 32.173  30.309  87.994  1.00 21.28 ? 895  ILE   B CB    1 
ATOM   15173 C  CG1   . ILE   B  1 897  ? 31.190  30.741  86.913  1.00 21.92 ? 895  ILE   B CG1   1 
ATOM   15174 C  CG2   . ILE   B  1 897  ? 31.516  30.210  89.365  1.00 21.70 ? 895  ILE   B CG2   1 
ATOM   15175 C  CD1   . ILE   B  1 897  ? 30.326  29.591  86.375  1.00 20.57 ? 895  ILE   B CD1   1 
ATOM   15176 N  N     . GLU   B  1 898  ? 35.054  29.819  89.052  1.00 24.50 ? 896  GLU   B N     1 
ATOM   15177 C  CA    . GLU   B  1 898  ? 35.933  29.390  90.132  1.00 28.94 ? 896  GLU   B CA    1 
ATOM   15178 C  C     . GLU   B  1 898  ? 37.004  30.430  90.420  1.00 27.49 ? 896  GLU   B C     1 
ATOM   15179 O  O     . GLU   B  1 898  ? 37.407  30.599  91.576  1.00 29.00 ? 896  GLU   B O     1 
ATOM   15180 C  CB    . GLU   B  1 898  ? 36.569  28.038  89.796  1.00 30.32 ? 896  GLU   B CB    1 
ATOM   15181 C  CG    . GLU   B  1 898  ? 35.580  26.881  89.778  1.00 29.47 ? 896  GLU   B CG    1 
ATOM   15182 C  CD    . GLU   B  1 898  ? 36.257  25.550  89.501  1.00 34.83 ? 896  GLU   B CD    1 
ATOM   15183 O  OE1   . GLU   B  1 898  ? 37.311  25.539  88.819  1.00 40.03 ? 896  GLU   B OE1   1 
ATOM   15184 O  OE2   . GLU   B  1 898  ? 35.747  24.520  89.979  1.00 42.91 ? 896  GLU   B OE2   1 
ATOM   15185 N  N     . LYS   B  1 899  ? 37.473  31.139  89.390  1.00 28.21 ? 897  LYS   B N     1 
ATOM   15186 C  CA    . LYS   B  1 899  ? 38.437  32.214  89.611  1.00 26.89 ? 897  LYS   B CA    1 
ATOM   15187 C  C     . LYS   B  1 899  ? 37.849  33.294  90.510  1.00 30.71 ? 897  LYS   B C     1 
ATOM   15188 O  O     . LYS   B  1 899  ? 38.524  33.796  91.418  1.00 28.84 ? 897  LYS   B O     1 
ATOM   15189 C  CB    . LYS   B  1 899  ? 38.863  32.811  88.276  1.00 32.33 ? 897  LYS   B CB    1 
ATOM   15190 C  CG    . LYS   B  1 899  ? 39.902  33.922  88.368  1.00 31.46 ? 897  LYS   B CG    1 
ATOM   15191 C  CD    . LYS   B  1 899  ? 39.787  34.782  87.127  1.00 39.10 ? 897  LYS   B CD    1 
ATOM   15192 C  CE    . LYS   B  1 899  ? 40.924  35.763  86.986  1.00 42.61 ? 897  LYS   B CE    1 
ATOM   15193 N  NZ    . LYS   B  1 899  ? 40.682  36.589  85.771  1.00 43.38 ? 897  LYS   B NZ    1 
ATOM   15194 N  N     . HIS   B  1 900  ? 36.584  33.656  90.279  1.00 26.89 ? 898  HIS   B N     1 
ATOM   15195 C  CA    . HIS   B  1 900  ? 35.921  34.613  91.155  1.00 27.08 ? 898  HIS   B CA    1 
ATOM   15196 C  C     . HIS   B  1 900  ? 35.827  34.074  92.573  1.00 26.85 ? 898  HIS   B C     1 
ATOM   15197 O  O     . HIS   B  1 900  ? 36.095  34.789  93.544  1.00 32.26 ? 898  HIS   B O     1 
ATOM   15198 C  CB    . HIS   B  1 900  ? 34.528  34.943  90.624  1.00 31.24 ? 898  HIS   B CB    1 
ATOM   15199 C  CG    . HIS   B  1 900  ? 33.690  35.716  91.592  1.00 30.09 ? 898  HIS   B CG    1 
ATOM   15200 N  ND1   . HIS   B  1 900  ? 33.869  37.064  91.815  1.00 32.92 ? 898  HIS   B ND1   1 
ATOM   15201 C  CD2   . HIS   B  1 900  ? 32.680  35.330  92.407  1.00 29.51 ? 898  HIS   B CD2   1 
ATOM   15202 C  CE1   . HIS   B  1 900  ? 32.998  37.479  92.719  1.00 30.37 ? 898  HIS   B CE1   1 
ATOM   15203 N  NE2   . HIS   B  1 900  ? 32.268  36.446  93.096  1.00 28.79 ? 898  HIS   B NE2   1 
ATOM   15204 N  N     . ILE   B  1 901  ? 35.426  32.810  92.710  1.00 26.25 ? 899  ILE   B N     1 
ATOM   15205 C  CA    . ILE   B  1 901  ? 35.236  32.225  94.030  1.00 25.34 ? 899  ILE   B CA    1 
ATOM   15206 C  C     . ILE   B  1 901  ? 36.547  32.223  94.790  1.00 36.80 ? 899  ILE   B C     1 
ATOM   15207 O  O     . ILE   B  1 901  ? 36.603  32.584  95.974  1.00 35.33 ? 899  ILE   B O     1 
ATOM   15208 C  CB    . ILE   B  1 901  ? 34.653  30.809  93.902  1.00 27.57 ? 899  ILE   B CB    1 
ATOM   15209 C  CG1   . ILE   B  1 901  ? 33.241  30.870  93.299  1.00 23.37 ? 899  ILE   B CG1   1 
ATOM   15210 C  CG2   . ILE   B  1 901  ? 34.650  30.086  95.247  1.00 27.51 ? 899  ILE   B CG2   1 
ATOM   15211 C  CD1   . ILE   B  1 901  ? 32.583  29.514  93.208  1.00 24.56 ? 899  ILE   B CD1   1 
ATOM   15212 N  N     . GLU   B  1 902  ? 37.626  31.838  94.114  1.00 33.07 ? 900  GLU   B N     1 
ATOM   15213 C  CA    . GLU   B  1 902  ? 38.932  31.824  94.761  1.00 33.50 ? 900  GLU   B CA    1 
ATOM   15214 C  C     . GLU   B  1 902  ? 39.386  33.232  95.114  1.00 32.96 ? 900  GLU   B C     1 
ATOM   15215 O  O     . GLU   B  1 902  ? 40.002  33.438  96.162  1.00 39.42 ? 900  GLU   B O     1 
ATOM   15216 C  CB    . GLU   B  1 902  ? 39.954  31.128  93.863  1.00 34.59 ? 900  GLU   B CB    1 
ATOM   15217 C  CG    . GLU   B  1 902  ? 39.742  29.627  93.797  1.00 38.64 ? 900  GLU   B CG    1 
ATOM   15218 C  CD    . GLU   B  1 902  ? 39.526  29.020  95.174  1.00 42.52 ? 900  GLU   B CD    1 
ATOM   15219 O  OE1   . GLU   B  1 902  ? 40.384  29.227  96.060  1.00 50.37 ? 900  GLU   B OE1   1 
ATOM   15220 O  OE2   . GLU   B  1 902  ? 38.489  28.351  95.379  1.00 42.17 ? 900  GLU   B OE2   1 
ATOM   15221 N  N     . ARG   B  1 903  ? 39.092  34.213  94.256  1.00 31.59 ? 901  ARG   B N     1 
ATOM   15222 C  CA    . ARG   B  1 903  ? 39.395  35.597  94.601  1.00 36.09 ? 901  ARG   B CA    1 
ATOM   15223 C  C     . ARG   B  1 903  ? 38.649  36.020  95.863  1.00 40.72 ? 901  ARG   B C     1 
ATOM   15224 O  O     . ARG   B  1 903  ? 39.234  36.630  96.764  1.00 44.03 ? 901  ARG   B O     1 
ATOM   15225 C  CB    . ARG   B  1 903  ? 39.052  36.525  93.436  1.00 38.85 ? 901  ARG   B CB    1 
ATOM   15226 C  CG    . ARG   B  1 903  ? 39.431  37.970  93.698  1.00 44.04 ? 901  ARG   B CG    1 
ATOM   15227 C  CD    . ARG   B  1 903  ? 38.610  38.953  92.862  1.00 48.29 ? 901  ARG   B CD    1 
ATOM   15228 N  NE    . ARG   B  1 903  ? 38.929  40.332  93.217  1.00 55.57 ? 901  ARG   B NE    1 
ATOM   15229 C  CZ    . ARG   B  1 903  ? 39.940  41.023  92.705  1.00 61.24 ? 901  ARG   B CZ    1 
ATOM   15230 N  NH1   . ARG   B  1 903  ? 40.706  40.522  91.747  1.00 62.53 ? 901  ARG   B NH1   1 
ATOM   15231 N  NH2   . ARG   B  1 903  ? 40.195  42.244  93.171  1.00 54.20 ? 901  ARG   B NH2   1 
ATOM   15232 N  N     . MET   B  1 904  ? 37.352  35.701  95.948  1.00 39.43 ? 902  MET   B N     1 
ATOM   15233 C  CA    . MET   B  1 904  ? 36.596  36.009  97.158  1.00 37.79 ? 902  MET   B CA    1 
ATOM   15234 C  C     . MET   B  1 904  ? 37.171  35.276  98.361  1.00 39.57 ? 902  MET   B C     1 
ATOM   15235 O  O     . MET   B  1 904  ? 37.396  35.875  99.419  1.00 40.50 ? 902  MET   B O     1 
ATOM   15236 C  CB    . MET   B  1 904  ? 35.119  35.652  96.975  1.00 34.52 ? 902  MET   B CB    1 
ATOM   15237 C  CG    . MET   B  1 904  ? 34.402  36.487  95.934  1.00 35.21 ? 902  MET   B CG    1 
ATOM   15238 S  SD    . MET   B  1 904  ? 34.450  38.247  96.292  1.00 45.21 ? 902  MET   B SD    1 
ATOM   15239 C  CE    . MET   B  1 904  ? 35.661  38.805  95.099  1.00 43.93 ? 902  MET   B CE    1 
ATOM   15240 N  N     . ARG   B  1 905  ? 37.405  33.970  98.218  1.00 39.12 ? 903  ARG   B N     1 
ATOM   15241 C  CA    . ARG   B  1 905  ? 38.028  33.203  99.293  1.00 42.58 ? 903  ARG   B CA    1 
ATOM   15242 C  C     . ARG   B  1 905  ? 39.390  33.779  99.661  1.00 44.49 ? 903  ARG   B C     1 
ATOM   15243 O  O     . ARG   B  1 905  ? 39.726  33.898  100.845 1.00 45.03 ? 903  ARG   B O     1 
ATOM   15244 C  CB    . ARG   B  1 905  ? 38.166  31.738  98.879  1.00 41.83 ? 903  ARG   B CB    1 
ATOM   15245 C  CG    . ARG   B  1 905  ? 37.606  30.761  99.890  1.00 45.87 ? 903  ARG   B CG    1 
ATOM   15246 C  CD    . ARG   B  1 905  ? 38.060  29.342  99.608  1.00 50.91 ? 903  ARG   B CD    1 
ATOM   15247 N  NE    . ARG   B  1 905  ? 37.376  28.721  98.480  1.00 43.40 ? 903  ARG   B NE    1 
ATOM   15248 C  CZ    . ARG   B  1 905  ? 36.379  27.855  98.596  1.00 39.43 ? 903  ARG   B CZ    1 
ATOM   15249 N  NH1   . ARG   B  1 905  ? 35.877  27.533  99.777  1.00 47.77 ? 903  ARG   B NH1   1 
ATOM   15250 N  NH2   . ARG   B  1 905  ? 35.884  27.284  97.502  1.00 42.72 ? 903  ARG   B NH2   1 
ATOM   15251 N  N     . GLY   B  1 906  ? 40.185  34.153  98.657  1.00 43.50 ? 904  GLY   B N     1 
ATOM   15252 C  CA    . GLY   B  1 906  ? 41.489  34.738  98.917  1.00 46.32 ? 904  GLY   B CA    1 
ATOM   15253 C  C     . GLY   B  1 906  ? 41.423  36.068  99.634  1.00 50.72 ? 904  GLY   B C     1 
ATOM   15254 O  O     . GLY   B  1 906  ? 42.399  36.464  100.283 1.00 45.65 ? 904  GLY   B O     1 
ATOM   15255 N  N     . LEU   B  1 907  ? 40.294  36.764  99.543  1.00 47.81 ? 905  LEU   B N     1 
ATOM   15256 C  CA    . LEU   B  1 907  ? 40.117  38.042  100.215 1.00 46.22 ? 905  LEU   B CA    1 
ATOM   15257 C  C     . LEU   B  1 907  ? 39.584  37.896  101.636 1.00 47.48 ? 905  LEU   B C     1 
ATOM   15258 O  O     . LEU   B  1 907  ? 39.426  38.907  102.328 1.00 54.11 ? 905  LEU   B O     1 
ATOM   15259 C  CB    . LEU   B  1 907  ? 39.185  38.942  99.396  1.00 40.81 ? 905  LEU   B CB    1 
ATOM   15260 N  N     . GLY   B  1 908  ? 39.298  36.673  102.086 1.00 48.16 ? 906  GLY   B N     1 
ATOM   15261 C  CA    . GLY   B  1 908  ? 38.851  36.423  103.441 1.00 44.24 ? 906  GLY   B CA    1 
ATOM   15262 C  C     . GLY   B  1 908  ? 37.363  36.170  103.603 1.00 48.97 ? 906  GLY   B C     1 
ATOM   15263 O  O     . GLY   B  1 908  ? 36.935  35.789  104.702 1.00 42.29 ? 906  GLY   B O     1 
ATOM   15264 N  N     . ARG   B  1 909  ? 36.567  36.363  102.550 1.00 45.70 ? 907  ARG   B N     1 
ATOM   15265 C  CA    . ARG   B  1 909  ? 35.120  36.226  102.658 1.00 38.19 ? 907  ARG   B CA    1 
ATOM   15266 C  C     . ARG   B  1 909  ? 34.738  34.782  102.950 1.00 40.17 ? 907  ARG   B C     1 
ATOM   15267 O  O     . ARG   B  1 909  ? 35.399  33.842  102.506 1.00 45.57 ? 907  ARG   B O     1 
ATOM   15268 C  CB    . ARG   B  1 909  ? 34.454  36.708  101.370 1.00 37.84 ? 907  ARG   B CB    1 
ATOM   15269 N  N     . LYS   B  1 910  ? 33.664  34.606  103.720 1.00 35.45 ? 908  LYS   B N     1 
ATOM   15270 C  CA    . LYS   B  1 910  ? 33.192  33.266  104.051 1.00 38.31 ? 908  LYS   B CA    1 
ATOM   15271 C  C     . LYS   B  1 910  ? 32.487  32.639  102.851 1.00 44.96 ? 908  LYS   B C     1 
ATOM   15272 O  O     . LYS   B  1 910  ? 31.569  33.235  102.276 1.00 39.55 ? 908  LYS   B O     1 
ATOM   15273 C  CB    . LYS   B  1 910  ? 32.246  33.309  105.252 1.00 36.50 ? 908  LYS   B CB    1 
ATOM   15274 N  N     . VAL   B  1 911  ? 32.897  31.419  102.499 1.00 43.23 ? 909  VAL   B N     1 
ATOM   15275 C  CA    . VAL   B  1 911  ? 32.441  30.726  101.297 1.00 36.81 ? 909  VAL   B CA    1 
ATOM   15276 C  C     . VAL   B  1 911  ? 31.886  29.365  101.704 1.00 37.13 ? 909  VAL   B C     1 
ATOM   15277 O  O     . VAL   B  1 911  ? 32.636  28.498  102.165 1.00 44.79 ? 909  VAL   B O     1 
ATOM   15278 C  CB    . VAL   B  1 911  ? 33.573  30.559  100.275 1.00 38.70 ? 909  VAL   B CB    1 
ATOM   15279 C  CG1   . VAL   B  1 911  ? 33.084  29.775  99.058  1.00 36.24 ? 909  VAL   B CG1   1 
ATOM   15280 C  CG2   . VAL   B  1 911  ? 34.125  31.910  99.870  1.00 35.85 ? 909  VAL   B CG2   1 
ATOM   15281 N  N     . GLU   B  1 912  ? 30.583  29.177  101.541 1.00 36.09 ? 910  GLU   B N     1 
ATOM   15282 C  CA    . GLU   B  1 912  ? 29.935  27.887  101.731 1.00 31.39 ? 910  GLU   B CA    1 
ATOM   15283 C  C     . GLU   B  1 912  ? 29.725  27.232  100.369 1.00 39.75 ? 910  GLU   B C     1 
ATOM   15284 O  O     . GLU   B  1 912  ? 29.315  27.897  99.413  1.00 31.95 ? 910  GLU   B O     1 
ATOM   15285 C  CB    . GLU   B  1 912  ? 28.593  28.053  102.451 1.00 37.68 ? 910  GLU   B CB    1 
ATOM   15286 C  CG    . GLU   B  1 912  ? 27.835  26.756  102.758 1.00 36.83 ? 910  GLU   B CG    1 
ATOM   15287 C  CD    . GLU   B  1 912  ? 28.201  26.154  104.116 1.00 41.14 ? 910  GLU   B CD    1 
ATOM   15288 O  OE1   . GLU   B  1 912  ? 28.921  26.817  104.896 1.00 37.42 ? 910  GLU   B OE1   1 
ATOM   15289 O  OE2   . GLU   B  1 912  ? 27.763  25.020  104.406 1.00 41.44 ? 910  GLU   B OE2   1 
ATOM   15290 N  N     . GLN   B  1 913  ? 30.022  25.932  100.277 1.00 34.28 ? 911  GLN   B N     1 
ATOM   15291 C  CA    . GLN   B  1 913  ? 29.841  25.188  99.038  1.00 32.17 ? 911  GLN   B CA    1 
ATOM   15292 C  C     . GLN   B  1 913  ? 29.303  23.793  99.324  1.00 36.37 ? 911  GLN   B C     1 
ATOM   15293 O  O     . GLN   B  1 913  ? 29.699  23.153  100.301 1.00 37.93 ? 911  GLN   B O     1 
ATOM   15294 C  CB    . GLN   B  1 913  ? 31.153  25.080  98.247  1.00 31.55 ? 911  GLN   B CB    1 
ATOM   15295 C  CG    . GLN   B  1 913  ? 31.583  26.369  97.578  1.00 32.26 ? 911  GLN   B CG    1 
ATOM   15296 C  CD    . GLN   B  1 913  ? 32.691  26.166  96.561  1.00 34.27 ? 911  GLN   B CD    1 
ATOM   15297 O  OE1   . GLN   B  1 913  ? 33.727  25.574  96.859  1.00 35.69 ? 911  GLN   B OE1   1 
ATOM   15298 N  NE2   . GLN   B  1 913  ? 32.473  26.660  95.349  1.00 28.81 ? 911  GLN   B NE2   1 
ATOM   15299 N  N     . ILE   B  1 914  ? 28.396  23.330  98.461  1.00 34.69 ? 912  ILE   B N     1 
ATOM   15300 C  CA    . ILE   B  1 914  ? 27.972  21.937  98.489  1.00 30.47 ? 912  ILE   B CA    1 
ATOM   15301 C  C     . ILE   B  1 914  ? 29.104  21.047  97.980  1.00 39.66 ? 912  ILE   B C     1 
ATOM   15302 O  O     . ILE   B  1 914  ? 29.875  21.425  97.086  1.00 32.80 ? 912  ILE   B O     1 
ATOM   15303 C  CB    . ILE   B  1 914  ? 26.694  21.749  97.649  1.00 36.68 ? 912  ILE   B CB    1 
ATOM   15304 N  N     . GLY   B  1 915  ? 29.224  19.856  98.564  1.00 41.21 ? 913  GLY   B N     1 
ATOM   15305 C  CA    . GLY   B  1 915  ? 30.191  18.886  98.075  1.00 37.67 ? 913  GLY   B CA    1 
ATOM   15306 C  C     . GLY   B  1 915  ? 29.643  18.180  96.849  1.00 38.80 ? 913  GLY   B C     1 
ATOM   15307 O  O     . GLY   B  1 915  ? 28.481  17.762  96.829  1.00 42.04 ? 913  GLY   B O     1 
ATOM   15308 N  N     . LEU   B  1 916  ? 30.471  18.053  95.818  1.00 33.99 ? 914  LEU   B N     1 
ATOM   15309 C  CA    . LEU   B  1 916  ? 30.045  17.438  94.567  1.00 35.89 ? 914  LEU   B CA    1 
ATOM   15310 C  C     . LEU   B  1 916  ? 30.471  15.977  94.526  1.00 36.70 ? 914  LEU   B C     1 
ATOM   15311 O  O     . LEU   B  1 916  ? 31.542  15.619  95.026  1.00 35.66 ? 914  LEU   B O     1 
ATOM   15312 C  CB    . LEU   B  1 916  ? 30.620  18.183  93.362  1.00 31.12 ? 914  LEU   B CB    1 
ATOM   15313 C  CG    . LEU   B  1 916  ? 30.137  19.620  93.142  1.00 32.85 ? 914  LEU   B CG    1 
ATOM   15314 C  CD1   . LEU   B  1 916  ? 30.557  20.116  91.769  1.00 32.34 ? 914  LEU   B CD1   1 
ATOM   15315 C  CD2   . LEU   B  1 916  ? 28.625  19.736  93.323  1.00 32.72 ? 914  LEU   B CD2   1 
ATOM   15316 N  N     . ALA   B  1 917  ? 29.624  15.139  93.931  1.00 34.77 ? 915  ALA   B N     1 
ATOM   15317 C  CA    . ALA   B  1 917  ? 29.938  13.727  93.783  1.00 36.51 ? 915  ALA   B CA    1 
ATOM   15318 C  C     . ALA   B  1 917  ? 31.084  13.532  92.792  1.00 37.79 ? 915  ALA   B C     1 
ATOM   15319 O  O     . ALA   B  1 917  ? 31.347  14.373  91.928  1.00 30.32 ? 915  ALA   B O     1 
ATOM   15320 C  CB    . ALA   B  1 917  ? 28.709  12.945  93.319  1.00 37.45 ? 915  ALA   B CB    1 
ATOM   15321 N  N     . SER   B  1 918  ? 31.772  12.392  92.932  1.00 33.58 ? 916  SER   B N     1 
ATOM   15322 C  CA    . SER   B  1 918  ? 32.875  12.065  92.034  1.00 36.53 ? 916  SER   B CA    1 
ATOM   15323 C  C     . SER   B  1 918  ? 32.425  12.018  90.577  1.00 36.03 ? 916  SER   B C     1 
ATOM   15324 O  O     . SER   B  1 918  ? 33.200  12.364  89.678  1.00 34.00 ? 916  SER   B O     1 
ATOM   15325 C  CB    . SER   B  1 918  ? 33.486  10.726  92.439  1.00 37.82 ? 916  SER   B CB    1 
ATOM   15326 O  OG    . SER   B  1 918  ? 32.519  9.692   92.320  1.00 42.55 ? 916  SER   B OG    1 
ATOM   15327 N  N     . GLU   B  1 919  ? 31.175  11.616  90.329  1.00 33.86 ? 917  GLU   B N     1 
ATOM   15328 C  CA    . GLU   B  1 919  ? 30.674  11.477  88.965  1.00 37.51 ? 917  GLU   B CA    1 
ATOM   15329 C  C     . GLU   B  1 919  ? 30.613  12.806  88.218  1.00 37.51 ? 917  GLU   B C     1 
ATOM   15330 O  O     . GLU   B  1 919  ? 30.486  12.804  86.988  1.00 35.36 ? 917  GLU   B O     1 
ATOM   15331 C  CB    . GLU   B  1 919  ? 29.283  10.835  88.976  1.00 35.72 ? 917  GLU   B CB    1 
ATOM   15332 N  N     . THR   B  1 920  ? 30.683  13.938  88.926  1.00 31.66 ? 918  THR   B N     1 
ATOM   15333 C  CA    . THR   B  1 920  ? 30.700  15.233  88.253  1.00 30.20 ? 918  THR   B CA    1 
ATOM   15334 C  C     . THR   B  1 920  ? 32.012  15.497  87.519  1.00 29.35 ? 918  THR   B C     1 
ATOM   15335 O  O     . THR   B  1 920  ? 32.053  16.382  86.660  1.00 28.44 ? 918  THR   B O     1 
ATOM   15336 C  CB    . THR   B  1 920  ? 30.445  16.366  89.255  1.00 29.52 ? 918  THR   B CB    1 
ATOM   15337 O  OG1   . THR   B  1 920  ? 31.506  16.401  90.213  1.00 28.62 ? 918  THR   B OG1   1 
ATOM   15338 C  CG2   . THR   B  1 920  ? 29.103  16.182  89.974  1.00 26.87 ? 918  THR   B CG2   1 
ATOM   15339 N  N     . GLY   B  1 921  ? 33.079  14.751  87.829  1.00 27.58 ? 919  GLY   B N     1 
ATOM   15340 C  CA    . GLY   B  1 921  ? 34.384  15.007  87.232  1.00 28.99 ? 919  GLY   B CA    1 
ATOM   15341 C  C     . GLY   B  1 921  ? 34.423  14.888  85.718  1.00 28.97 ? 919  GLY   B C     1 
ATOM   15342 O  O     . GLY   B  1 921  ? 35.317  15.455  85.085  1.00 30.14 ? 919  GLY   B O     1 
ATOM   15343 N  N     . VAL   B  1 922  ? 33.475  14.165  85.119  1.00 23.98 ? 920  VAL   B N     1 
ATOM   15344 C  CA    . VAL   B  1 922  ? 33.457  14.025  83.663  1.00 24.99 ? 920  VAL   B CA    1 
ATOM   15345 C  C     . VAL   B  1 922  ? 32.780  15.197  82.971  1.00 24.38 ? 920  VAL   B C     1 
ATOM   15346 O  O     . VAL   B  1 922  ? 32.828  15.294  81.740  1.00 23.77 ? 920  VAL   B O     1 
ATOM   15347 C  CB    . VAL   B  1 922  ? 32.766  12.710  83.256  1.00 27.29 ? 920  VAL   B CB    1 
ATOM   15348 C  CG1   . VAL   B  1 922  ? 33.633  11.510  83.657  1.00 29.29 ? 920  VAL   B CG1   1 
ATOM   15349 C  CG2   . VAL   B  1 922  ? 31.380  12.629  83.890  1.00 27.86 ? 920  VAL   B CG2   1 
ATOM   15350 N  N     . GLY   B  1 923  ? 32.142  16.081  83.726  1.00 20.55 ? 921  GLY   B N     1 
ATOM   15351 C  CA    . GLY   B  1 923  ? 31.516  17.263  83.170  1.00 22.76 ? 921  GLY   B CA    1 
ATOM   15352 C  C     . GLY   B  1 923  ? 32.104  18.506  83.800  1.00 23.31 ? 921  GLY   B C     1 
ATOM   15353 O  O     . GLY   B  1 923  ? 33.125  18.424  84.487  1.00 23.20 ? 921  GLY   B O     1 
ATOM   15354 N  N     . THR   B  1 924  ? 31.480  19.661  83.590  1.00 20.88 ? 922  THR   B N     1 
ATOM   15355 C  CA    . THR   B  1 924  ? 31.976  20.922  84.128  1.00 20.39 ? 922  THR   B CA    1 
ATOM   15356 C  C     . THR   B  1 924  ? 30.946  21.433  85.130  1.00 20.22 ? 922  THR   B C     1 
ATOM   15357 O  O     . THR   B  1 924  ? 29.977  22.092  84.753  1.00 22.19 ? 922  THR   B O     1 
ATOM   15358 C  CB    . THR   B  1 924  ? 32.221  21.925  83.011  1.00 19.36 ? 922  THR   B CB    1 
ATOM   15359 O  OG1   . THR   B  1 924  ? 31.043  22.031  82.212  1.00 22.51 ? 922  THR   B OG1   1 
ATOM   15360 C  CG2   . THR   B  1 924  ? 33.357  21.458  82.124  1.00 18.95 ? 922  THR   B CG2   1 
ATOM   15361 N  N     . PHE   B  1 925  ? 31.156  21.131  86.406  1.00 20.31 ? 923  PHE   B N     1 
ATOM   15362 C  CA    . PHE   B  1 925  ? 30.230  21.544  87.446  1.00 19.83 ? 923  PHE   B CA    1 
ATOM   15363 C  C     . PHE   B  1 925  ? 30.880  22.566  88.360  1.00 19.58 ? 923  PHE   B C     1 
ATOM   15364 O  O     . PHE   B  1 925  ? 32.085  22.512  88.629  1.00 20.35 ? 923  PHE   B O     1 
ATOM   15365 C  CB    . PHE   B  1 925  ? 29.759  20.341  88.266  1.00 20.81 ? 923  PHE   B CB    1 
ATOM   15366 C  CG    . PHE   B  1 925  ? 28.897  19.376  87.494  1.00 22.27 ? 923  PHE   B CG    1 
ATOM   15367 C  CD1   . PHE   B  1 925  ? 29.463  18.419  86.663  1.00 20.64 ? 923  PHE   B CD1   1 
ATOM   15368 C  CD2   . PHE   B  1 925  ? 27.516  19.434  87.595  1.00 20.03 ? 923  PHE   B CD2   1 
ATOM   15369 C  CE1   . PHE   B  1 925  ? 28.661  17.529  85.954  1.00 22.96 ? 923  PHE   B CE1   1 
ATOM   15370 C  CE2   . PHE   B  1 925  ? 26.704  18.551  86.893  1.00 20.57 ? 923  PHE   B CE2   1 
ATOM   15371 C  CZ    . PHE   B  1 925  ? 27.272  17.599  86.073  1.00 22.21 ? 923  PHE   B CZ    1 
ATOM   15372 N  N     . VAL   B  1 926  ? 30.071  23.513  88.827  1.00 19.67 ? 924  VAL   B N     1 
ATOM   15373 C  CA    . VAL   B  1 926  ? 30.424  24.387  89.933  1.00 21.50 ? 924  VAL   B CA    1 
ATOM   15374 C  C     . VAL   B  1 926  ? 29.402  24.136  91.029  1.00 21.96 ? 924  VAL   B C     1 
ATOM   15375 O  O     . VAL   B  1 926  ? 28.202  24.235  90.771  1.00 20.19 ? 924  VAL   B O     1 
ATOM   15376 C  CB    . VAL   B  1 926  ? 30.415  25.877  89.546  1.00 19.86 ? 924  VAL   B CB    1 
ATOM   15377 C  CG1   . VAL   B  1 926  ? 30.743  26.714  90.775  1.00 21.01 ? 924  VAL   B CG1   1 
ATOM   15378 C  CG2   . VAL   B  1 926  ? 31.420  26.143  88.437  1.00 19.37 ? 924  VAL   B CG2   1 
ATOM   15379 N  N     . PRO   B  1 927  ? 29.819  23.821  92.246  1.00 22.95 ? 925  PRO   B N     1 
ATOM   15380 C  CA    . PRO   B  1 927  ? 28.862  23.607  93.310  1.00 23.93 ? 925  PRO   B CA    1 
ATOM   15381 C  C     . PRO   B  1 927  ? 28.173  24.905  93.666  1.00 23.21 ? 925  PRO   B C     1 
ATOM   15382 O  O     . PRO   B  1 927  ? 28.804  25.977  93.661  1.00 20.87 ? 925  PRO   B O     1 
ATOM   15383 C  CB    . PRO   B  1 927  ? 29.731  23.108  94.471  1.00 27.10 ? 925  PRO   B CB    1 
ATOM   15384 C  CG    . PRO   B  1 927  ? 31.059  23.714  94.210  1.00 24.54 ? 925  PRO   B CG    1 
ATOM   15385 C  CD    . PRO   B  1 927  ? 31.207  23.678  92.716  1.00 23.35 ? 925  PRO   B CD    1 
ATOM   15386 N  N     . PRO   B  1 928  ? 26.878  24.849  93.953  1.00 24.02 ? 926  PRO   B N     1 
ATOM   15387 C  CA    . PRO   B  1 928  ? 26.202  26.012  94.517  1.00 25.13 ? 926  PRO   B CA    1 
ATOM   15388 C  C     . PRO   B  1 928  ? 27.014  26.577  95.665  1.00 25.18 ? 926  PRO   B C     1 
ATOM   15389 O  O     . PRO   B  1 928  ? 27.494  25.844  96.535  1.00 28.48 ? 926  PRO   B O     1 
ATOM   15390 C  CB    . PRO   B  1 928  ? 24.858  25.443  94.973  1.00 23.81 ? 926  PRO   B CB    1 
ATOM   15391 C  CG    . PRO   B  1 928  ? 24.597  24.363  93.975  1.00 32.16 ? 926  PRO   B CG    1 
ATOM   15392 C  CD    . PRO   B  1 928  ? 25.952  23.728  93.731  1.00 23.67 ? 926  PRO   B CD    1 
ATOM   15393 N  N     . THR   B  1 929  ? 27.209  27.885  95.631  1.00 24.02 ? 927  THR   B N     1 
ATOM   15394 C  CA    . THR   B  1 929  ? 28.151  28.572  96.492  1.00 24.96 ? 927  THR   B CA    1 
ATOM   15395 C  C     . THR   B  1 929  ? 27.478  29.782  97.117  1.00 29.35 ? 927  THR   B C     1 
ATOM   15396 O  O     . THR   B  1 929  ? 26.717  30.487  96.456  1.00 24.76 ? 927  THR   B O     1 
ATOM   15397 C  CB    . THR   B  1 929  ? 29.367  28.993  95.678  1.00 25.04 ? 927  THR   B CB    1 
ATOM   15398 O  OG1   . THR   B  1 929  ? 29.976  27.813  95.137  1.00 24.78 ? 927  THR   B OG1   1 
ATOM   15399 C  CG2   . THR   B  1 929  ? 30.373  29.755  96.526  1.00 27.30 ? 927  THR   B CG2   1 
ATOM   15400 N  N     . ILE   B  1 930  ? 27.751  30.014  98.395  1.00 25.76 ? 928  ILE   B N     1 
ATOM   15401 C  CA    . ILE   B  1 930  ? 27.255  31.193  99.096  1.00 30.62 ? 928  ILE   B CA    1 
ATOM   15402 C  C     . ILE   B  1 930  ? 28.467  31.960  99.587  1.00 31.88 ? 928  ILE   B C     1 
ATOM   15403 O  O     . ILE   B  1 930  ? 29.336  31.391  100.265 1.00 34.88 ? 928  ILE   B O     1 
ATOM   15404 C  CB    . ILE   B  1 930  ? 26.314  30.819  100.253 1.00 26.75 ? 928  ILE   B CB    1 
ATOM   15405 C  CG1   . ILE   B  1 930  ? 25.079  30.092  99.720  1.00 27.81 ? 928  ILE   B CG1   1 
ATOM   15406 C  CG2   . ILE   B  1 930  ? 25.919  32.065  101.043 1.00 30.87 ? 928  ILE   B CG2   1 
ATOM   15407 C  CD1   . ILE   B  1 930  ? 24.236  29.450  100.810 1.00 27.28 ? 928  ILE   B CD1   1 
ATOM   15408 N  N     . ILE   B  1 931  ? 28.559  33.231  99.212  1.00 27.68 ? 929  ILE   B N     1 
ATOM   15409 C  CA    . ILE   B  1 931  ? 29.689  34.072  99.584  1.00 29.02 ? 929  ILE   B CA    1 
ATOM   15410 C  C     . ILE   B  1 931  ? 29.149  35.271  100.345 1.00 34.45 ? 929  ILE   B C     1 
ATOM   15411 O  O     . ILE   B  1 931  ? 28.383  36.068  99.793  1.00 28.33 ? 929  ILE   B O     1 
ATOM   15412 C  CB    . ILE   B  1 931  ? 30.501  34.526  98.362  1.00 30.76 ? 929  ILE   B CB    1 
ATOM   15413 C  CG1   . ILE   B  1 931  ? 31.014  33.320  97.574  1.00 30.02 ? 929  ILE   B CG1   1 
ATOM   15414 C  CG2   . ILE   B  1 931  ? 31.671  35.410  98.788  1.00 31.25 ? 929  ILE   B CG2   1 
ATOM   15415 C  CD1   . ILE   B  1 931  ? 31.887  33.702  96.403  1.00 30.16 ? 929  ILE   B CD1   1 
ATOM   15416 N  N     . GLU   B  1 932  ? 29.552  35.411  101.601 1.00 31.99 ? 930  GLU   B N     1 
ATOM   15417 C  CA    . GLU   B  1 932  ? 29.105  36.533  102.416 1.00 33.24 ? 930  GLU   B CA    1 
ATOM   15418 C  C     . GLU   B  1 932  ? 30.038  37.716  102.189 1.00 33.19 ? 930  GLU   B C     1 
ATOM   15419 O  O     . GLU   B  1 932  ? 31.243  37.617  102.442 1.00 37.51 ? 930  GLU   B O     1 
ATOM   15420 C  CB    . GLU   B  1 932  ? 29.044  36.119  103.884 1.00 31.16 ? 930  GLU   B CB    1 
ATOM   15421 C  CG    . GLU   B  1 932  ? 28.074  34.962  104.086 1.00 39.63 ? 930  GLU   B CG    1 
ATOM   15422 C  CD    . GLU   B  1 932  ? 28.027  34.454  105.504 1.00 43.75 ? 930  GLU   B CD    1 
ATOM   15423 O  OE1   . GLU   B  1 932  ? 28.072  35.290  106.426 1.00 40.44 ? 930  GLU   B OE1   1 
ATOM   15424 O  OE2   . GLU   B  1 932  ? 27.945  33.216  105.690 1.00 43.64 ? 930  GLU   B OE2   1 
ATOM   15425 N  N     . LEU   B  1 933  ? 29.488  38.820  101.690 1.00 34.06 ? 931  LEU   B N     1 
ATOM   15426 C  CA    . LEU   B  1 933  ? 30.264  40.010  101.378 1.00 33.84 ? 931  LEU   B CA    1 
ATOM   15427 C  C     . LEU   B  1 933  ? 30.196  41.029  102.509 1.00 41.10 ? 931  LEU   B C     1 
ATOM   15428 O  O     . LEU   B  1 933  ? 29.378  40.929  103.425 1.00 41.84 ? 931  LEU   B O     1 
ATOM   15429 C  CB    . LEU   B  1 933  ? 29.772  40.665  100.087 1.00 36.51 ? 931  LEU   B CB    1 
ATOM   15430 C  CG    . LEU   B  1 933  ? 29.747  39.814  98.822  1.00 34.92 ? 931  LEU   B CG    1 
ATOM   15431 C  CD1   . LEU   B  1 933  ? 29.277  40.671  97.654  1.00 37.85 ? 931  LEU   B CD1   1 
ATOM   15432 C  CD2   . LEU   B  1 933  ? 31.111  39.216  98.558  1.00 37.18 ? 931  LEU   B CD2   1 
ATOM   15433 N  N     . GLU   B  1 934  ? 31.065  42.039  102.408 1.00 42.64 ? 932  GLU   B N     1 
ATOM   15434 C  CA    . GLU   B  1 934  ? 31.055  43.199  103.295 1.00 43.70 ? 932  GLU   B CA    1 
ATOM   15435 C  C     . GLU   B  1 934  ? 30.227  44.332  102.698 1.00 47.82 ? 932  GLU   B C     1 
ATOM   15436 O  O     . GLU   B  1 934  ? 29.274  44.809  103.321 1.00 53.03 ? 932  GLU   B O     1 
ATOM   15437 C  CB    . GLU   B  1 934  ? 32.489  43.671  103.568 1.00 49.55 ? 932  GLU   B CB    1 
ATOM   15438 N  N     . LYS   B  1 935  ? 30.579  44.766  101.491 1.00 49.84 ? 933  LYS   B N     1 
ATOM   15439 C  CA    . LYS   B  1 935  ? 29.829  45.769  100.753 1.00 50.55 ? 933  LYS   B CA    1 
ATOM   15440 C  C     . LYS   B  1 935  ? 29.465  45.215  99.384  1.00 46.85 ? 933  LYS   B C     1 
ATOM   15441 O  O     . LYS   B  1 935  ? 30.134  44.317  98.865  1.00 48.60 ? 933  LYS   B O     1 
ATOM   15442 C  CB    . LYS   B  1 935  ? 30.632  47.070  100.588 1.00 52.28 ? 933  LYS   B CB    1 
ATOM   15443 N  N     . LEU   B  1 936  ? 28.391  45.750  98.801  1.00 46.14 ? 934  LEU   B N     1 
ATOM   15444 C  CA    . LEU   B  1 936  ? 28.022  45.334  97.455  1.00 48.32 ? 934  LEU   B CA    1 
ATOM   15445 C  C     . LEU   B  1 936  ? 29.114  45.674  96.451  1.00 51.92 ? 934  LEU   B C     1 
ATOM   15446 O  O     . LEU   B  1 936  ? 29.212  45.019  95.408  1.00 48.97 ? 934  LEU   B O     1 
ATOM   15447 C  CB    . LEU   B  1 936  ? 26.690  45.972  97.052  1.00 46.15 ? 934  LEU   B CB    1 
ATOM   15448 C  CG    . LEU   B  1 936  ? 25.748  45.149  96.164  1.00 47.55 ? 934  LEU   B CG    1 
ATOM   15449 C  CD1   . LEU   B  1 936  ? 24.291  45.506  96.450  1.00 40.47 ? 934  LEU   B CD1   1 
ATOM   15450 C  CD2   . LEU   B  1 936  ? 26.054  45.350  94.686  1.00 41.92 ? 934  LEU   B CD2   1 
ATOM   15451 N  N     . SER   B  1 937  ? 29.958  46.661  96.761  1.00 53.42 ? 935  SER   B N     1 
ATOM   15452 C  CA    . SER   B  1 937  ? 31.081  47.013  95.903  1.00 54.32 ? 935  SER   B CA    1 
ATOM   15453 C  C     . SER   B  1 937  ? 32.158  45.934  95.862  1.00 47.64 ? 935  SER   B C     1 
ATOM   15454 O  O     . SER   B  1 937  ? 33.069  46.033  95.035  1.00 50.07 ? 935  SER   B O     1 
ATOM   15455 C  CB    . SER   B  1 937  ? 31.690  48.343  96.359  1.00 56.65 ? 935  SER   B CB    1 
ATOM   15456 N  N     . ASP   B  1 938  ? 32.083  44.915  96.726  1.00 49.61 ? 936  ASP   B N     1 
ATOM   15457 C  CA    . ASP   B  1 938  ? 32.985  43.772  96.613  1.00 48.78 ? 936  ASP   B CA    1 
ATOM   15458 C  C     . ASP   B  1 938  ? 32.738  42.965  95.345  1.00 49.70 ? 936  ASP   B C     1 
ATOM   15459 O  O     . ASP   B  1 938  ? 33.600  42.172  94.950  1.00 44.53 ? 936  ASP   B O     1 
ATOM   15460 C  CB    . ASP   B  1 938  ? 32.843  42.839  97.817  1.00 46.59 ? 936  ASP   B CB    1 
ATOM   15461 C  CG    . ASP   B  1 938  ? 33.306  43.470  99.110  1.00 55.20 ? 936  ASP   B CG    1 
ATOM   15462 O  OD1   . ASP   B  1 938  ? 33.537  44.702  99.134  1.00 54.12 ? 936  ASP   B OD1   1 
ATOM   15463 O  OD2   . ASP   B  1 938  ? 33.441  42.723  100.107 1.00 57.02 ? 936  ASP   B OD2   1 
ATOM   15464 N  N     . LEU   B  1 939  ? 31.578  43.130  94.718  1.00 48.48 ? 937  LEU   B N     1 
ATOM   15465 C  CA    . LEU   B  1 939  ? 31.216  42.406  93.503  1.00 45.09 ? 937  LEU   B CA    1 
ATOM   15466 C  C     . LEU   B  1 939  ? 31.385  43.374  92.338  1.00 48.75 ? 937  LEU   B C     1 
ATOM   15467 O  O     . LEU   B  1 939  ? 30.558  44.265  92.131  1.00 51.04 ? 937  LEU   B O     1 
ATOM   15468 C  CB    . LEU   B  1 939  ? 29.793  41.863  93.600  1.00 42.64 ? 937  LEU   B CB    1 
ATOM   15469 N  N     . GLN   B  1 940  ? 32.465  43.198  91.576  1.00 46.37 ? 938  GLN   B N     1 
ATOM   15470 C  CA    . GLN   B  1 940  ? 32.822  44.122  90.507  1.00 49.15 ? 938  GLN   B CA    1 
ATOM   15471 C  C     . GLN   B  1 940  ? 32.378  43.657  89.125  1.00 51.14 ? 938  GLN   B C     1 
ATOM   15472 O  O     . GLN   B  1 940  ? 32.447  44.446  88.175  1.00 52.05 ? 938  GLN   B O     1 
ATOM   15473 C  CB    . GLN   B  1 940  ? 34.340  44.361  90.498  1.00 49.16 ? 938  GLN   B CB    1 
ATOM   15474 N  N     . ARG   B  1 941  ? 31.922  42.414  88.983  1.00 44.66 ? 939  ARG   B N     1 
ATOM   15475 C  CA    . ARG   B  1 941  ? 31.516  41.914  87.678  1.00 43.22 ? 939  ARG   B CA    1 
ATOM   15476 C  C     . ARG   B  1 941  ? 30.413  40.879  87.849  1.00 38.36 ? 939  ARG   B C     1 
ATOM   15477 O  O     . ARG   B  1 941  ? 30.260  40.269  88.910  1.00 36.58 ? 939  ARG   B O     1 
ATOM   15478 C  CB    . ARG   B  1 941  ? 32.703  41.307  86.914  1.00 42.69 ? 939  ARG   B CB    1 
ATOM   15479 C  CG    . ARG   B  1 941  ? 33.354  40.103  87.591  1.00 45.14 ? 939  ARG   B CG    1 
ATOM   15480 C  CD    . ARG   B  1 941  ? 34.471  39.520  86.730  1.00 44.09 ? 939  ARG   B CD    1 
ATOM   15481 N  NE    . ARG   B  1 941  ? 35.099  38.350  87.338  1.00 49.59 ? 939  ARG   B NE    1 
ATOM   15482 C  CZ    . ARG   B  1 941  ? 34.837  37.091  87.005  1.00 43.50 ? 939  ARG   B CZ    1 
ATOM   15483 N  NH1   . ARG   B  1 941  ? 33.944  36.790  86.077  1.00 43.64 ? 939  ARG   B NH1   1 
ATOM   15484 N  NH2   . ARG   B  1 941  ? 35.493  36.107  87.616  1.00 38.93 ? 939  ARG   B NH2   1 
ATOM   15485 N  N     . GLU   B  1 942  ? 29.639  40.693  86.786  1.00 38.16 ? 940  GLU   B N     1 
ATOM   15486 C  CA    . GLU   B  1 942  ? 28.646  39.631  86.773  1.00 37.40 ? 940  GLU   B CA    1 
ATOM   15487 C  C     . GLU   B  1 942  ? 29.356  38.281  86.754  1.00 34.98 ? 940  GLU   B C     1 
ATOM   15488 O  O     . GLU   B  1 942  ? 30.229  38.038  85.914  1.00 36.69 ? 940  GLU   B O     1 
ATOM   15489 C  CB    . GLU   B  1 942  ? 27.729  39.789  85.559  1.00 40.49 ? 940  GLU   B CB    1 
ATOM   15490 C  CG    . GLU   B  1 942  ? 26.490  38.902  85.548  1.00 38.25 ? 940  GLU   B CG    1 
ATOM   15491 C  CD    . GLU   B  1 942  ? 25.717  39.025  84.243  1.00 41.37 ? 940  GLU   B CD    1 
ATOM   15492 O  OE1   . GLU   B  1 942  ? 26.316  39.482  83.242  1.00 46.48 ? 940  GLU   B OE1   1 
ATOM   15493 O  OE2   . GLU   B  1 942  ? 24.513  38.682  84.211  1.00 38.52 ? 940  GLU   B OE2   1 
ATOM   15494 N  N     . VAL   B  1 943  ? 29.013  37.417  87.703  1.00 29.49 ? 941  VAL   B N     1 
ATOM   15495 C  CA    . VAL   B  1 943  ? 29.570  36.071  87.790  1.00 29.54 ? 941  VAL   B CA    1 
ATOM   15496 C  C     . VAL   B  1 943  ? 28.444  35.108  87.441  1.00 25.57 ? 941  VAL   B C     1 
ATOM   15497 O  O     . VAL   B  1 943  ? 27.513  34.901  88.227  1.00 24.05 ? 941  VAL   B O     1 
ATOM   15498 C  CB    . VAL   B  1 943  ? 30.167  35.779  89.171  1.00 31.38 ? 941  VAL   B CB    1 
ATOM   15499 C  CG1   . VAL   B  1 943  ? 30.694  34.349  89.246  1.00 27.65 ? 941  VAL   B CG1   1 
ATOM   15500 C  CG2   . VAL   B  1 943  ? 31.283  36.774  89.467  1.00 29.68 ? 941  VAL   B CG2   1 
ATOM   15501 N  N     . PHE   B  1 944  ? 28.540  34.516  86.257  1.00 25.48 ? 942  PHE   B N     1 
ATOM   15502 C  CA    . PHE   B  1 944  ? 27.414  33.846  85.617  1.00 23.37 ? 942  PHE   B CA    1 
ATOM   15503 C  C     . PHE   B  1 944  ? 27.417  32.359  85.978  1.00 26.31 ? 942  PHE   B C     1 
ATOM   15504 O  O     . PHE   B  1 944  ? 27.714  31.475  85.174  1.00 22.68 ? 942  PHE   B O     1 
ATOM   15505 C  CB    . PHE   B  1 944  ? 27.486  34.070  84.115  1.00 22.34 ? 942  PHE   B CB    1 
ATOM   15506 C  CG    . PHE   B  1 944  ? 26.158  34.078  83.452  1.00 24.71 ? 942  PHE   B CG    1 
ATOM   15507 C  CD1   . PHE   B  1 944  ? 25.333  35.188  83.546  1.00 28.63 ? 942  PHE   B CD1   1 
ATOM   15508 C  CD2   . PHE   B  1 944  ? 25.733  32.990  82.716  1.00 24.31 ? 942  PHE   B CD2   1 
ATOM   15509 C  CE1   . PHE   B  1 944  ? 24.104  35.202  82.925  1.00 25.11 ? 942  PHE   B CE1   1 
ATOM   15510 C  CE2   . PHE   B  1 944  ? 24.506  33.002  82.100  1.00 22.82 ? 942  PHE   B CE2   1 
ATOM   15511 C  CZ    . PHE   B  1 944  ? 23.692  34.113  82.202  1.00 25.31 ? 942  PHE   B CZ    1 
ATOM   15512 N  N     . GLY   B  1 945  ? 27.078  32.091  87.230  1.00 20.56 ? 943  GLY   B N     1 
ATOM   15513 C  CA    . GLY   B  1 945  ? 27.193  30.755  87.761  1.00 20.04 ? 943  GLY   B CA    1 
ATOM   15514 C  C     . GLY   B  1 945  ? 26.447  30.658  89.070  1.00 19.20 ? 943  GLY   B C     1 
ATOM   15515 O  O     . GLY   B  1 945  ? 25.827  31.619  89.518  1.00 17.22 ? 943  GLY   B O     1 
ATOM   15516 N  N     . PRO   B  1 946  ? 26.494  29.504  89.709  1.00 18.79 ? 944  PRO   B N     1 
ATOM   15517 C  CA    . PRO   B  1 946  ? 25.674  29.299  90.916  1.00 19.76 ? 944  PRO   B CA    1 
ATOM   15518 C  C     . PRO   B  1 946  ? 26.357  29.870  92.155  1.00 20.88 ? 944  PRO   B C     1 
ATOM   15519 O  O     . PRO   B  1 946  ? 26.731  29.158  93.082  1.00 21.94 ? 944  PRO   B O     1 
ATOM   15520 C  CB    . PRO   B  1 946  ? 25.525  27.772  90.949  1.00 19.20 ? 944  PRO   B CB    1 
ATOM   15521 C  CG    . PRO   B  1 946  ? 26.857  27.275  90.385  1.00 24.38 ? 944  PRO   B CG    1 
ATOM   15522 C  CD    . PRO   B  1 946  ? 27.281  28.312  89.344  1.00 19.73 ? 944  PRO   B CD    1 
ATOM   15523 N  N     . VAL   B  1 947  ? 26.532  31.186  92.166  1.00 18.96 ? 945  VAL   B N     1 
ATOM   15524 C  CA    . VAL   B  1 947  ? 27.296  31.864  93.204  1.00 19.53 ? 945  VAL   B CA    1 
ATOM   15525 C  C     . VAL   B  1 947  ? 26.416  32.970  93.772  1.00 24.90 ? 945  VAL   B C     1 
ATOM   15526 O  O     . VAL   B  1 947  ? 26.213  34.010  93.134  1.00 23.39 ? 945  VAL   B O     1 
ATOM   15527 C  CB    . VAL   B  1 947  ? 28.623  32.415  92.682  1.00 24.58 ? 945  VAL   B CB    1 
ATOM   15528 C  CG1   . VAL   B  1 947  ? 29.465  32.979  93.837  1.00 24.21 ? 945  VAL   B CG1   1 
ATOM   15529 C  CG2   . VAL   B  1 947  ? 29.399  31.313  91.981  1.00 21.90 ? 945  VAL   B CG2   1 
ATOM   15530 N  N     . LEU   B  1 948  ? 25.882  32.743  94.963  1.00 20.31 ? 946  LEU   B N     1 
ATOM   15531 C  CA    . LEU   B  1 948  ? 25.064  33.734  95.639  1.00 20.63 ? 946  LEU   B CA    1 
ATOM   15532 C  C     . LEU   B  1 948  ? 25.928  34.556  96.576  1.00 22.68 ? 946  LEU   B C     1 
ATOM   15533 O  O     . LEU   B  1 948  ? 26.679  34.003  97.384  1.00 25.20 ? 946  LEU   B O     1 
ATOM   15534 C  CB    . LEU   B  1 948  ? 23.954  33.058  96.431  1.00 20.71 ? 946  LEU   B CB    1 
ATOM   15535 C  CG    . LEU   B  1 948  ? 23.047  33.982  97.251  1.00 21.55 ? 946  LEU   B CG    1 
ATOM   15536 C  CD1   . LEU   B  1 948  ? 22.163  34.848  96.351  1.00 19.51 ? 946  LEU   B CD1   1 
ATOM   15537 C  CD2   . LEU   B  1 948  ? 22.218  33.114  98.141  1.00 19.73 ? 946  LEU   B CD2   1 
ATOM   15538 N  N     . HIS   B  1 949  ? 25.820  35.867  96.471  1.00 21.28 ? 947  HIS   B N     1 
ATOM   15539 C  CA    . HIS   B  1 949  ? 26.520  36.756  97.384  1.00 24.43 ? 947  HIS   B CA    1 
ATOM   15540 C  C     . HIS   B  1 949  ? 25.513  37.284  98.393  1.00 23.10 ? 947  HIS   B C     1 
ATOM   15541 O  O     . HIS   B  1 949  ? 24.365  37.560  98.044  1.00 21.82 ? 947  HIS   B O     1 
ATOM   15542 C  CB    . HIS   B  1 949  ? 27.198  37.880  96.611  1.00 23.25 ? 947  HIS   B CB    1 
ATOM   15543 C  CG    . HIS   B  1 949  ? 28.133  37.380  95.554  1.00 29.09 ? 947  HIS   B CG    1 
ATOM   15544 N  ND1   . HIS   B  1 949  ? 27.705  37.009  94.297  1.00 22.27 ? 947  HIS   B ND1   1 
ATOM   15545 C  CD2   . HIS   B  1 949  ? 29.465  37.139  95.584  1.00 28.82 ? 947  HIS   B CD2   1 
ATOM   15546 C  CE1   . HIS   B  1 949  ? 28.737  36.585  93.589  1.00 26.16 ? 947  HIS   B CE1   1 
ATOM   15547 N  NE2   . HIS   B  1 949  ? 29.816  36.649  94.347  1.00 28.50 ? 947  HIS   B NE2   1 
ATOM   15548 N  N     . VAL   B  1 950  ? 25.914  37.363  99.656  1.00 24.34 ? 948  VAL   B N     1 
ATOM   15549 C  CA    . VAL   B  1 950  ? 24.998  37.785  100.712 1.00 23.14 ? 948  VAL   B CA    1 
ATOM   15550 C  C     . VAL   B  1 950  ? 25.583  39.004  101.401 1.00 26.39 ? 948  VAL   B C     1 
ATOM   15551 O  O     . VAL   B  1 950  ? 26.763  39.008  101.770 1.00 28.18 ? 948  VAL   B O     1 
ATOM   15552 C  CB    . VAL   B  1 950  ? 24.725  36.665  101.733 1.00 26.96 ? 948  VAL   B CB    1 
ATOM   15553 C  CG1   . VAL   B  1 950  ? 23.743  37.156  102.779 1.00 26.78 ? 948  VAL   B CG1   1 
ATOM   15554 C  CG2   . VAL   B  1 950  ? 24.174  35.430  101.045 1.00 25.14 ? 948  VAL   B CG2   1 
ATOM   15555 N  N     . ILE   B  1 951  ? 24.771  40.045  101.546 1.00 21.88 ? 949  ILE   B N     1 
ATOM   15556 C  CA    . ILE   B  1 951  ? 25.156  41.204  102.335 1.00 22.74 ? 949  ILE   B CA    1 
ATOM   15557 C  C     . ILE   B  1 951  ? 24.072  41.439  103.371 1.00 26.56 ? 949  ILE   B C     1 
ATOM   15558 O  O     . ILE   B  1 951  ? 22.907  41.075  103.178 1.00 24.11 ? 949  ILE   B O     1 
ATOM   15559 C  CB    . ILE   B  1 951  ? 25.389  42.470  101.480 1.00 30.65 ? 949  ILE   B CB    1 
ATOM   15560 C  CG1   . ILE   B  1 951  ? 24.095  42.965  100.860 1.00 29.50 ? 949  ILE   B CG1   1 
ATOM   15561 C  CG2   . ILE   B  1 951  ? 26.412  42.215  100.385 1.00 40.36 ? 949  ILE   B CG2   1 
ATOM   15562 C  CD1   . ILE   B  1 951  ? 24.325  44.087  99.867  1.00 40.78 ? 949  ILE   B CD1   1 
ATOM   15563 N  N     . ARG   B  1 952  ? 24.469  42.025  104.493 1.00 22.77 ? 950  ARG   B N     1 
ATOM   15564 C  CA    . ARG   B  1 952  ? 23.552  42.317  105.583 1.00 24.18 ? 950  ARG   B CA    1 
ATOM   15565 C  C     . ARG   B  1 952  ? 23.373  43.822  105.659 1.00 25.05 ? 950  ARG   B C     1 
ATOM   15566 O  O     . ARG   B  1 952  ? 24.317  44.577  105.406 1.00 26.18 ? 950  ARG   B O     1 
ATOM   15567 C  CB    . ARG   B  1 952  ? 24.092  41.776  106.910 1.00 27.01 ? 950  ARG   B CB    1 
ATOM   15568 C  CG    . ARG   B  1 952  ? 24.599  40.353  106.800 1.00 28.82 ? 950  ARG   B CG    1 
ATOM   15569 C  CD    . ARG   B  1 952  ? 25.626  40.058  107.878 1.00 35.23 ? 950  ARG   B CD    1 
ATOM   15570 N  NE    . ARG   B  1 952  ? 24.995  39.727  109.148 1.00 37.13 ? 950  ARG   B NE    1 
ATOM   15571 C  CZ    . ARG   B  1 952  ? 24.879  38.493  109.617 1.00 37.10 ? 950  ARG   B CZ    1 
ATOM   15572 N  NH1   . ARG   B  1 952  ? 25.331  37.452  108.938 1.00 34.59 ? 950  ARG   B NH1   1 
ATOM   15573 N  NH2   . ARG   B  1 952  ? 24.294  38.299  110.797 1.00 41.52 ? 950  ARG   B NH2   1 
ATOM   15574 N  N     . TYR   B  1 953  ? 22.164  44.265  105.987 1.00 23.94 ? 951  TYR   B N     1 
ATOM   15575 C  CA    . TYR   B  1 953  ? 21.925  45.696  106.053 1.00 22.60 ? 951  TYR   B CA    1 
ATOM   15576 C  C     . TYR   B  1 953  ? 21.099  46.020  107.285 1.00 23.24 ? 951  TYR   B C     1 
ATOM   15577 O  O     . TYR   B  1 953  ? 20.326  45.191  107.772 1.00 21.41 ? 951  TYR   B O     1 
ATOM   15578 C  CB    . TYR   B  1 953  ? 21.225  46.219  104.792 1.00 23.37 ? 951  TYR   B CB    1 
ATOM   15579 C  CG    . TYR   B  1 953  ? 19.779  45.824  104.686 1.00 19.68 ? 951  TYR   B CG    1 
ATOM   15580 C  CD1   . TYR   B  1 953  ? 19.411  44.573  104.189 1.00 22.28 ? 951  TYR   B CD1   1 
ATOM   15581 C  CD2   . TYR   B  1 953  ? 18.772  46.706  105.058 1.00 21.07 ? 951  TYR   B CD2   1 
ATOM   15582 C  CE1   . TYR   B  1 953  ? 18.085  44.214  104.082 1.00 20.43 ? 951  TYR   B CE1   1 
ATOM   15583 C  CE2   . TYR   B  1 953  ? 17.437  46.349  104.955 1.00 25.22 ? 951  TYR   B CE2   1 
ATOM   15584 C  CZ    . TYR   B  1 953  ? 17.105  45.100  104.468 1.00 22.05 ? 951  TYR   B CZ    1 
ATOM   15585 O  OH    . TYR   B  1 953  ? 15.785  44.743  104.366 1.00 22.75 ? 951  TYR   B OH    1 
ATOM   15586 N  N     . ARG   B  1 954  ? 21.308  47.230  107.801 1.00 25.10 ? 952  ARG   B N     1 
ATOM   15587 C  CA    . ARG   B  1 954  ? 20.480  47.765  108.867 1.00 28.67 ? 952  ARG   B CA    1 
ATOM   15588 C  C     . ARG   B  1 954  ? 19.232  48.389  108.258 1.00 27.38 ? 952  ARG   B C     1 
ATOM   15589 O  O     . ARG   B  1 954  ? 19.303  49.042  107.213 1.00 27.35 ? 952  ARG   B O     1 
ATOM   15590 C  CB    . ARG   B  1 954  ? 21.264  48.798  109.685 1.00 29.40 ? 952  ARG   B CB    1 
ATOM   15591 N  N     . ARG   B  1 955  ? 18.080  48.169  108.909 1.00 30.39 ? 953  ARG   B N     1 
ATOM   15592 C  CA    . ARG   B  1 955  ? 16.813  48.664  108.375 1.00 31.39 ? 953  ARG   B CA    1 
ATOM   15593 C  C     . ARG   B  1 955  ? 16.888  50.149  108.028 1.00 31.36 ? 953  ARG   B C     1 
ATOM   15594 O  O     . ARG   B  1 955  ? 16.322  50.592  107.020 1.00 30.18 ? 953  ARG   B O     1 
ATOM   15595 C  CB    . ARG   B  1 955  ? 15.685  48.401  109.377 1.00 34.64 ? 953  ARG   B CB    1 
ATOM   15596 N  N     . ASP   B  1 956  ? 17.597  50.929  108.844 1.00 30.79 ? 954  ASP   B N     1 
ATOM   15597 C  CA    . ASP   B  1 956  ? 17.753  52.358  108.595 1.00 34.66 ? 954  ASP   B CA    1 
ATOM   15598 C  C     . ASP   B  1 956  ? 18.533  52.653  107.325 1.00 31.48 ? 954  ASP   B C     1 
ATOM   15599 O  O     . ASP   B  1 956  ? 18.487  53.788  106.839 1.00 33.65 ? 954  ASP   B O     1 
ATOM   15600 C  CB    . ASP   B  1 956  ? 18.468  53.030  109.771 1.00 36.95 ? 954  ASP   B CB    1 
ATOM   15601 C  CG    . ASP   B  1 956  ? 17.648  53.009  111.034 1.00 42.71 ? 954  ASP   B CG    1 
ATOM   15602 O  OD1   . ASP   B  1 956  ? 16.406  52.875  110.927 1.00 42.94 ? 954  ASP   B OD1   1 
ATOM   15603 O  OD2   . ASP   B  1 956  ? 18.245  53.130  112.126 1.00 45.92 ? 954  ASP   B OD2   1 
ATOM   15604 N  N     . ASP   B  1 957  ? 19.282  51.680  106.810 1.00 28.34 ? 955  ASP   B N     1 
ATOM   15605 C  CA    . ASP   B  1 957  ? 20.096  51.868  105.617 1.00 29.54 ? 955  ASP   B CA    1 
ATOM   15606 C  C     . ASP   B  1 957  ? 19.409  51.359  104.355 1.00 25.19 ? 955  ASP   B C     1 
ATOM   15607 O  O     . ASP   B  1 957  ? 20.058  51.264  103.311 1.00 26.35 ? 955  ASP   B O     1 
ATOM   15608 C  CB    . ASP   B  1 957  ? 21.450  51.173  105.779 1.00 28.61 ? 955  ASP   B CB    1 
ATOM   15609 C  CG    . ASP   B  1 957  ? 22.355  51.864  106.793 1.00 38.96 ? 955  ASP   B CG    1 
ATOM   15610 O  OD1   . ASP   B  1 957  ? 22.291  53.108  106.912 1.00 42.53 ? 955  ASP   B OD1   1 
ATOM   15611 O  OD2   . ASP   B  1 957  ? 23.141  51.157  107.466 1.00 35.76 ? 955  ASP   B OD2   1 
ATOM   15612 N  N     . LEU   B  1 958  ? 18.112  51.038  104.430 1.00 24.90 ? 956  LEU   B N     1 
ATOM   15613 C  CA    . LEU   B  1 958  ? 17.407  50.477  103.283 1.00 25.89 ? 956  LEU   B CA    1 
ATOM   15614 C  C     . LEU   B  1 958  ? 17.531  51.370  102.056 1.00 24.49 ? 956  LEU   B C     1 
ATOM   15615 O  O     . LEU   B  1 958  ? 17.861  50.901  100.962 1.00 26.08 ? 956  LEU   B O     1 
ATOM   15616 C  CB    . LEU   B  1 958  ? 15.937  50.271  103.638 1.00 26.18 ? 956  LEU   B CB    1 
ATOM   15617 C  CG    . LEU   B  1 958  ? 15.093  49.628  102.549 1.00 25.93 ? 956  LEU   B CG    1 
ATOM   15618 C  CD1   . LEU   B  1 958  ? 15.747  48.335  102.078 1.00 24.08 ? 956  LEU   B CD1   1 
ATOM   15619 C  CD2   . LEU   B  1 958  ? 13.715  49.373  103.113 1.00 27.10 ? 956  LEU   B CD2   1 
ATOM   15620 N  N     . ASP   B  1 959  ? 17.284  52.670  102.223 1.00 25.64 ? 957  ASP   B N     1 
ATOM   15621 C  CA    . ASP   B  1 959  ? 17.328  53.563  101.072 1.00 26.92 ? 957  ASP   B CA    1 
ATOM   15622 C  C     . ASP   B  1 959  ? 18.728  53.611  100.471 1.00 27.20 ? 957  ASP   B C     1 
ATOM   15623 O  O     . ASP   B  1 959  ? 18.886  53.598  99.243  1.00 24.77 ? 957  ASP   B O     1 
ATOM   15624 C  CB    . ASP   B  1 959  ? 16.853  54.959  101.469 1.00 26.17 ? 957  ASP   B CB    1 
ATOM   15625 C  CG    . ASP   B  1 959  ? 16.375  55.749  100.285 1.00 27.66 ? 957  ASP   B CG    1 
ATOM   15626 O  OD1   . ASP   B  1 959  ? 15.640  55.169  99.453  1.00 26.74 ? 957  ASP   B OD1   1 
ATOM   15627 O  OD2   . ASP   B  1 959  ? 16.732  56.940  100.179 1.00 28.86 ? 957  ASP   B OD2   1 
ATOM   15628 N  N     . ARG   B  1 960  ? 19.758  53.650  101.323 1.00 25.01 ? 958  ARG   B N     1 
ATOM   15629 C  CA    . ARG   B  1 960  ? 21.131  53.615  100.834 1.00 22.88 ? 958  ARG   B CA    1 
ATOM   15630 C  C     . ARG   B  1 960  ? 21.443  52.282  100.168 1.00 24.47 ? 958  ARG   B C     1 
ATOM   15631 O  O     . ARG   B  1 960  ? 22.183  52.233  99.176  1.00 26.65 ? 958  ARG   B O     1 
ATOM   15632 C  CB    . ARG   B  1 960  ? 22.108  53.884  101.979 1.00 24.46 ? 958  ARG   B CB    1 
ATOM   15633 N  N     . LEU   B  1 961  ? 20.882  51.189  100.694 1.00 22.40 ? 959  LEU   B N     1 
ATOM   15634 C  CA    . LEU   B  1 961  ? 21.086  49.886  100.069 1.00 22.46 ? 959  LEU   B CA    1 
ATOM   15635 C  C     . LEU   B  1 961  ? 20.511  49.869  98.660  1.00 26.26 ? 959  LEU   B C     1 
ATOM   15636 O  O     . LEU   B  1 961  ? 21.149  49.372  97.724  1.00 26.61 ? 959  LEU   B O     1 
ATOM   15637 C  CB    . LEU   B  1 961  ? 20.453  48.785  100.922 1.00 22.74 ? 959  LEU   B CB    1 
ATOM   15638 C  CG    . LEU   B  1 961  ? 20.445  47.365  100.321 1.00 22.68 ? 959  LEU   B CG    1 
ATOM   15639 C  CD1   . LEU   B  1 961  ? 21.865  46.812  100.170 1.00 22.84 ? 959  LEU   B CD1   1 
ATOM   15640 C  CD2   . LEU   B  1 961  ? 19.550  46.380  101.103 1.00 20.87 ? 959  LEU   B CD2   1 
ATOM   15641 N  N     . VAL   B  1 962  ? 19.314  50.424  98.489  1.00 22.22 ? 960  VAL   B N     1 
ATOM   15642 C  CA    . VAL   B  1 962  ? 18.714  50.499  97.163  1.00 22.19 ? 960  VAL   B CA    1 
ATOM   15643 C  C     . VAL   B  1 962  ? 19.600  51.303  96.219  1.00 24.24 ? 960  VAL   B C     1 
ATOM   15644 O  O     . VAL   B  1 962  ? 19.776  50.933  95.054  1.00 23.16 ? 960  VAL   B O     1 
ATOM   15645 C  CB    . VAL   B  1 962  ? 17.297  51.086  97.263  1.00 24.00 ? 960  VAL   B CB    1 
ATOM   15646 C  CG1   . VAL   B  1 962  ? 16.750  51.345  95.880  1.00 23.82 ? 960  VAL   B CG1   1 
ATOM   15647 C  CG2   . VAL   B  1 962  ? 16.401  50.126  98.026  1.00 20.91 ? 960  VAL   B CG2   1 
ATOM   15648 N  N     . ASP   B  1 963  ? 20.180  52.407  96.707  1.00 24.42 ? 961  ASP   B N     1 
ATOM   15649 C  CA    . ASP   B  1 963  ? 21.169  53.139  95.918  1.00 26.60 ? 961  ASP   B CA    1 
ATOM   15650 C  C     . ASP   B  1 963  ? 22.315  52.239  95.499  1.00 25.89 ? 961  ASP   B C     1 
ATOM   15651 O  O     . ASP   B  1 963  ? 22.767  52.290  94.349  1.00 28.79 ? 961  ASP   B O     1 
ATOM   15652 C  CB    . ASP   B  1 963  ? 21.738  54.309  96.713  1.00 29.03 ? 961  ASP   B CB    1 
ATOM   15653 C  CG    . ASP   B  1 963  ? 20.830  55.491  96.738  1.00 35.05 ? 961  ASP   B CG    1 
ATOM   15654 O  OD1   . ASP   B  1 963  ? 19.852  55.512  95.966  1.00 37.59 ? 961  ASP   B OD1   1 
ATOM   15655 O  OD2   . ASP   B  1 963  ? 21.106  56.412  97.541  1.00 38.94 ? 961  ASP   B OD2   1 
ATOM   15656 N  N     . ASP   B  1 964  ? 22.821  51.431  96.432  1.00 23.07 ? 962  ASP   B N     1 
ATOM   15657 C  CA    . ASP   B  1 964  ? 23.938  50.551  96.121  1.00 28.02 ? 962  ASP   B CA    1 
ATOM   15658 C  C     . ASP   B  1 964  ? 23.558  49.531  95.057  1.00 26.66 ? 962  ASP   B C     1 
ATOM   15659 O  O     . ASP   B  1 964  ? 24.374  49.191  94.195  1.00 24.55 ? 962  ASP   B O     1 
ATOM   15660 C  CB    . ASP   B  1 964  ? 24.415  49.846  97.387  1.00 29.07 ? 962  ASP   B CB    1 
ATOM   15661 C  CG    . ASP   B  1 964  ? 25.135  50.776  98.333  1.00 33.61 ? 962  ASP   B CG    1 
ATOM   15662 O  OD1   . ASP   B  1 964  ? 25.411  51.934  97.940  1.00 31.73 ? 962  ASP   B OD1   1 
ATOM   15663 O  OD2   . ASP   B  1 964  ? 25.423  50.342  99.470  1.00 40.37 ? 962  ASP   B OD2   1 
ATOM   15664 N  N     . VAL   B  1 965  ? 22.330  49.013  95.109  1.00 26.01 ? 963  VAL   B N     1 
ATOM   15665 C  CA    . VAL   B  1 965  ? 21.900  48.082  94.070  1.00 23.88 ? 963  VAL   B CA    1 
ATOM   15666 C  C     . VAL   B  1 965  ? 21.832  48.797  92.729  1.00 21.99 ? 963  VAL   B C     1 
ATOM   15667 O  O     . VAL   B  1 965  ? 22.320  48.290  91.712  1.00 26.55 ? 963  VAL   B O     1 
ATOM   15668 C  CB    . VAL   B  1 965  ? 20.551  47.438  94.437  1.00 24.12 ? 963  VAL   B CB    1 
ATOM   15669 C  CG1   . VAL   B  1 965  ? 19.990  46.649  93.237  1.00 21.21 ? 963  VAL   B CG1   1 
ATOM   15670 C  CG2   . VAL   B  1 965  ? 20.726  46.528  95.661  1.00 24.04 ? 963  VAL   B CG2   1 
ATOM   15671 N  N     . ASN   B  1 966  ? 21.226  49.986  92.712  1.00 22.83 ? 964  ASN   B N     1 
ATOM   15672 C  CA    . ASN   B  1 966  ? 21.129  50.772  91.488  1.00 23.61 ? 964  ASN   B CA    1 
ATOM   15673 C  C     . ASN   B  1 966  ? 22.496  51.174  90.958  1.00 27.86 ? 964  ASN   B C     1 
ATOM   15674 O  O     . ASN   B  1 966  ? 22.660  51.361  89.748  1.00 24.05 ? 964  ASN   B O     1 
ATOM   15675 C  CB    . ASN   B  1 966  ? 20.307  52.039  91.729  1.00 24.70 ? 964  ASN   B CB    1 
ATOM   15676 C  CG    . ASN   B  1 966  ? 18.836  51.761  91.944  1.00 24.81 ? 964  ASN   B CG    1 
ATOM   15677 O  OD1   . ASN   B  1 966  ? 18.314  50.732  91.524  1.00 22.77 ? 964  ASN   B OD1   1 
ATOM   15678 N  ND2   . ASN   B  1 966  ? 18.156  52.696  92.584  1.00 21.37 ? 964  ASN   B ND2   1 
ATOM   15679 N  N     . ALA   B  1 967  ? 23.477  51.345  91.844  1.00 24.98 ? 965  ALA   B N     1 
ATOM   15680 C  CA    . ALA   B  1 967  ? 24.771  51.903  91.452  1.00 26.15 ? 965  ALA   B CA    1 
ATOM   15681 C  C     . ALA   B  1 967  ? 25.599  50.984  90.557  1.00 28.85 ? 965  ALA   B C     1 
ATOM   15682 O  O     . ALA   B  1 967  ? 26.582  51.457  89.974  1.00 28.80 ? 965  ALA   B O     1 
ATOM   15683 C  CB    . ALA   B  1 967  ? 25.580  52.256  92.700  1.00 27.38 ? 965  ALA   B CB    1 
ATOM   15684 N  N     . THR   B  1 968  ? 25.267  49.691  90.452  1.00 26.36 ? 966  THR   B N     1 
ATOM   15685 C  CA    . THR   B  1 968  ? 25.978  48.835  89.507  1.00 26.42 ? 966  THR   B CA    1 
ATOM   15686 C  C     . THR   B  1 968  ? 25.747  49.258  88.060  1.00 28.32 ? 966  THR   B C     1 
ATOM   15687 O  O     . THR   B  1 968  ? 26.524  48.866  87.183  1.00 29.33 ? 966  THR   B O     1 
ATOM   15688 C  CB    . THR   B  1 968  ? 25.557  47.369  89.651  1.00 30.12 ? 966  THR   B CB    1 
ATOM   15689 O  OG1   . THR   B  1 968  ? 24.246  47.188  89.093  1.00 27.91 ? 966  THR   B OG1   1 
ATOM   15690 C  CG2   . THR   B  1 968  ? 25.558  46.935  91.117  1.00 30.37 ? 966  THR   B CG2   1 
ATOM   15691 N  N     . GLY   B  1 969  ? 24.701  50.041  87.790  1.00 25.69 ? 967  GLY   B N     1 
ATOM   15692 C  CA    . GLY   B  1 969  ? 24.326  50.380  86.436  1.00 25.51 ? 967  GLY   B CA    1 
ATOM   15693 C  C     . GLY   B  1 969  ? 23.474  49.342  85.741  1.00 27.54 ? 967  GLY   B C     1 
ATOM   15694 O  O     . GLY   B  1 969  ? 22.958  49.616  84.654  1.00 26.06 ? 967  GLY   B O     1 
ATOM   15695 N  N     . TYR   B  1 970  ? 23.310  48.165  86.329  1.00 22.94 ? 968  TYR   B N     1 
ATOM   15696 C  CA    . TYR   B  1 970  ? 22.393  47.162  85.819  1.00 24.70 ? 968  TYR   B CA    1 
ATOM   15697 C  C     . TYR   B  1 970  ? 20.993  47.426  86.353  1.00 25.98 ? 968  TYR   B C     1 
ATOM   15698 O  O     . TYR   B  1 970  ? 20.789  48.174  87.309  1.00 25.70 ? 968  TYR   B O     1 
ATOM   15699 C  CB    . TYR   B  1 970  ? 22.852  45.760  86.221  1.00 23.37 ? 968  TYR   B CB    1 
ATOM   15700 C  CG    . TYR   B  1 970  ? 24.073  45.280  85.466  1.00 28.73 ? 968  TYR   B CG    1 
ATOM   15701 C  CD1   . TYR   B  1 970  ? 23.951  44.738  84.191  1.00 28.21 ? 968  TYR   B CD1   1 
ATOM   15702 C  CD2   . TYR   B  1 970  ? 25.342  45.346  86.036  1.00 32.11 ? 968  TYR   B CD2   1 
ATOM   15703 C  CE1   . TYR   B  1 970  ? 25.059  44.289  83.493  1.00 32.25 ? 968  TYR   B CE1   1 
ATOM   15704 C  CE2   . TYR   B  1 970  ? 26.464  44.893  85.340  1.00 35.63 ? 968  TYR   B CE2   1 
ATOM   15705 C  CZ    . TYR   B  1 970  ? 26.309  44.369  84.070  1.00 38.42 ? 968  TYR   B CZ    1 
ATOM   15706 O  OH    . TYR   B  1 970  ? 27.404  43.914  83.367  1.00 45.90 ? 968  TYR   B OH    1 
ATOM   15707 N  N     . GLY   B  1 971  ? 20.015  46.790  85.734  1.00 24.55 ? 969  GLY   B N     1 
ATOM   15708 C  CA    . GLY   B  1 971  ? 18.670  46.930  86.233  1.00 21.20 ? 969  GLY   B CA    1 
ATOM   15709 C  C     . GLY   B  1 971  ? 17.772  45.936  85.544  1.00 20.55 ? 969  GLY   B C     1 
ATOM   15710 O  O     . GLY   B  1 971  ? 16.843  46.315  84.828  1.00 19.53 ? 969  GLY   B O     1 
ATOM   15711 N  N     . LEU   B  1 972  ? 18.052  44.655  85.749  1.00 21.40 ? 970  LEU   B N     1 
ATOM   15712 C  CA    . LEU   B  1 972  ? 17.279  43.611  85.093  1.00 17.85 ? 970  LEU   B CA    1 
ATOM   15713 C  C     . LEU   B  1 972  ? 16.184  43.106  86.028  1.00 19.03 ? 970  LEU   B C     1 
ATOM   15714 O  O     . LEU   B  1 972  ? 15.053  43.602  85.982  1.00 20.22 ? 970  LEU   B O     1 
ATOM   15715 C  CB    . LEU   B  1 972  ? 18.198  42.472  84.640  1.00 20.30 ? 970  LEU   B CB    1 
ATOM   15716 C  CG    . LEU   B  1 972  ? 17.517  41.465  83.706  1.00 22.91 ? 970  LEU   B CG    1 
ATOM   15717 C  CD1   . LEU   B  1 972  ? 16.835  42.192  82.540  1.00 22.49 ? 970  LEU   B CD1   1 
ATOM   15718 C  CD2   . LEU   B  1 972  ? 18.536  40.459  83.194  1.00 22.65 ? 970  LEU   B CD2   1 
ATOM   15719 N  N     . THR   B  1 973  ? 16.493  42.136  86.883  1.00 17.79 ? 971  THR   B N     1 
ATOM   15720 C  CA    . THR   B  1 973  ? 15.513  41.660  87.849  1.00 15.89 ? 971  THR   B CA    1 
ATOM   15721 C  C     . THR   B  1 973  ? 15.869  42.111  89.261  1.00 16.90 ? 971  THR   B C     1 
ATOM   15722 O  O     . THR   B  1 973  ? 17.025  42.412  89.592  1.00 18.16 ? 971  THR   B O     1 
ATOM   15723 C  CB    . THR   B  1 973  ? 15.372  40.138  87.820  1.00 18.47 ? 971  THR   B CB    1 
ATOM   15724 O  OG1   . THR   B  1 973  ? 16.635  39.543  88.143  1.00 19.50 ? 971  THR   B OG1   1 
ATOM   15725 C  CG2   . THR   B  1 973  ? 14.915  39.673  86.445  1.00 20.18 ? 971  THR   B CG2   1 
ATOM   15726 N  N     . PHE   B  1 974  ? 14.833  42.153  90.094  1.00 17.59 ? 972  PHE   B N     1 
ATOM   15727 C  CA    . PHE   B  1 974  ? 14.963  42.603  91.468  1.00 17.90 ? 972  PHE   B CA    1 
ATOM   15728 C  C     . PHE   B  1 974  ? 13.864  41.946  92.271  1.00 18.32 ? 972  PHE   B C     1 
ATOM   15729 O  O     . PHE   B  1 974  ? 12.709  41.964  91.847  1.00 15.73 ? 972  PHE   B O     1 
ATOM   15730 C  CB    . PHE   B  1 974  ? 14.835  44.121  91.593  1.00 16.38 ? 972  PHE   B CB    1 
ATOM   15731 C  CG    . PHE   B  1 974  ? 14.782  44.583  93.016  1.00 15.23 ? 972  PHE   B CG    1 
ATOM   15732 C  CD1   . PHE   B  1 974  ? 15.959  44.707  93.750  1.00 18.21 ? 972  PHE   B CD1   1 
ATOM   15733 C  CD2   . PHE   B  1 974  ? 13.560  44.858  93.633  1.00 18.41 ? 972  PHE   B CD2   1 
ATOM   15734 C  CE1   . PHE   B  1 974  ? 15.928  45.116  95.075  1.00 19.70 ? 972  PHE   B CE1   1 
ATOM   15735 C  CE2   . PHE   B  1 974  ? 13.516  45.260  94.954  1.00 18.03 ? 972  PHE   B CE2   1 
ATOM   15736 C  CZ    . PHE   B  1 974  ? 14.700  45.389  95.678  1.00 20.36 ? 972  PHE   B CZ    1 
ATOM   15737 N  N     . GLY   B  1 975  ? 14.210  41.410  93.439  1.00 16.83 ? 973  GLY   B N     1 
ATOM   15738 C  CA    . GLY   B  1 975  ? 13.238  40.784  94.309  1.00 16.34 ? 973  GLY   B CA    1 
ATOM   15739 C  C     . GLY   B  1 975  ? 13.141  41.512  95.634  1.00 15.90 ? 973  GLY   B C     1 
ATOM   15740 O  O     . GLY   B  1 975  ? 14.115  42.080  96.119  1.00 14.96 ? 973  GLY   B O     1 
ATOM   15741 N  N     . LEU   B  1 976  ? 11.942  41.505  96.210  1.00 15.30 ? 974  LEU   B N     1 
ATOM   15742 C  CA    . LEU   B  1 976  ? 11.718  42.093  97.525  1.00 15.50 ? 974  LEU   B CA    1 
ATOM   15743 C  C     . LEU   B  1 976  ? 10.832  41.143  98.306  1.00 18.38 ? 974  LEU   B C     1 
ATOM   15744 O  O     . LEU   B  1 976  ? 9.756   40.771  97.830  1.00 19.09 ? 974  LEU   B O     1 
ATOM   15745 C  CB    . LEU   B  1 976  ? 11.056  43.468  97.429  1.00 19.21 ? 974  LEU   B CB    1 
ATOM   15746 C  CG    . LEU   B  1 976  ? 10.646  44.080  98.772  1.00 21.48 ? 974  LEU   B CG    1 
ATOM   15747 C  CD1   . LEU   B  1 976  ? 11.876  44.398  99.630  1.00 18.36 ? 974  LEU   B CD1   1 
ATOM   15748 C  CD2   . LEU   B  1 976  ? 9.799   45.326  98.564  1.00 20.07 ? 974  LEU   B CD2   1 
ATOM   15749 N  N     . HIS   B  1 977  ? 11.284  40.736  99.484  1.00 19.71 ? 975  HIS   B N     1 
ATOM   15750 C  CA    . HIS   B  1 977  ? 10.487  39.896  100.374 1.00 18.10 ? 975  HIS   B CA    1 
ATOM   15751 C  C     . HIS   B  1 977  ? 10.155  40.696  101.621 1.00 15.30 ? 975  HIS   B C     1 
ATOM   15752 O  O     . HIS   B  1 977  ? 11.045  41.044  102.404 1.00 17.18 ? 975  HIS   B O     1 
ATOM   15753 C  CB    . HIS   B  1 977  ? 11.220  38.610  100.742 1.00 18.61 ? 975  HIS   B CB    1 
ATOM   15754 C  CG    . HIS   B  1 977  ? 10.918  37.469  99.827  1.00 19.39 ? 975  HIS   B CG    1 
ATOM   15755 N  ND1   . HIS   B  1 977  ? 10.047  36.457  100.165 1.00 25.17 ? 975  HIS   B ND1   1 
ATOM   15756 C  CD2   . HIS   B  1 977  ? 11.358  37.189  98.578  1.00 24.98 ? 975  HIS   B CD2   1 
ATOM   15757 C  CE1   . HIS   B  1 977  ? 9.983   35.587  99.172  1.00 22.19 ? 975  HIS   B CE1   1 
ATOM   15758 N  NE2   . HIS   B  1 977  ? 10.765  36.009  98.197  1.00 24.88 ? 975  HIS   B NE2   1 
ATOM   15759 N  N     . THR   B  1 978  ? 8.875   40.977  101.800 1.00 17.72 ? 976  THR   B N     1 
ATOM   15760 C  CA    . THR   B  1 978  ? 8.410   41.747  102.936 1.00 20.40 ? 976  THR   B CA    1 
ATOM   15761 C  C     . THR   B  1 978  ? 6.908   41.593  103.004 1.00 21.11 ? 976  THR   B C     1 
ATOM   15762 O  O     . THR   B  1 978  ? 6.247   41.383  101.983 1.00 20.55 ? 976  THR   B O     1 
ATOM   15763 C  CB    . THR   B  1 978  ? 8.775   43.230  102.826 1.00 21.11 ? 976  THR   B CB    1 
ATOM   15764 O  OG1   . THR   B  1 978  ? 8.263   43.932  103.968 1.00 20.45 ? 976  THR   B OG1   1 
ATOM   15765 C  CG2   . THR   B  1 978  ? 8.170   43.831  101.572 1.00 21.15 ? 976  THR   B CG2   1 
ATOM   15766 N  N     . ARG   B  1 979  ? 6.380   41.684  104.214 1.00 20.14 ? 977  ARG   B N     1 
ATOM   15767 C  CA    . ARG   B  1 979  ? 4.942   41.717  104.391 1.00 21.29 ? 977  ARG   B CA    1 
ATOM   15768 C  C     . ARG   B  1 979  ? 4.408   43.136  104.529 1.00 19.80 ? 977  ARG   B C     1 
ATOM   15769 O  O     . ARG   B  1 979  ? 3.199   43.306  104.684 1.00 20.63 ? 977  ARG   B O     1 
ATOM   15770 C  CB    . ARG   B  1 979  ? 4.545   40.881  105.615 1.00 23.81 ? 977  ARG   B CB    1 
ATOM   15771 N  N     . LEU   B  1 980  ? 5.267   44.155  104.449 1.00 19.82 ? 978  LEU   B N     1 
ATOM   15772 C  CA    . LEU   B  1 980  ? 4.889   45.519  104.818 1.00 18.91 ? 978  LEU   B CA    1 
ATOM   15773 C  C     . LEU   B  1 980  ? 4.700   46.378  103.575 1.00 19.93 ? 978  LEU   B C     1 
ATOM   15774 O  O     . LEU   B  1 980  ? 5.640   46.565  102.794 1.00 20.23 ? 978  LEU   B O     1 
ATOM   15775 C  CB    . LEU   B  1 980  ? 5.943   46.137  105.733 1.00 18.79 ? 978  LEU   B CB    1 
ATOM   15776 C  CG    . LEU   B  1 980  ? 6.316   45.223  106.894 1.00 20.30 ? 978  LEU   B CG    1 
ATOM   15777 C  CD1   . LEU   B  1 980  ? 7.435   45.864  107.710 1.00 23.43 ? 978  LEU   B CD1   1 
ATOM   15778 C  CD2   . LEU   B  1 980  ? 5.098   45.001  107.762 1.00 23.44 ? 978  LEU   B CD2   1 
ATOM   15779 N  N     . ASP   B  1 981  ? 3.494   46.924  103.414 1.00 18.44 ? 979  ASP   B N     1 
ATOM   15780 C  CA    . ASP   B  1 981  ? 3.190   47.745  102.241 1.00 18.24 ? 979  ASP   B CA    1 
ATOM   15781 C  C     . ASP   B  1 981  ? 4.075   48.987  102.162 1.00 18.31 ? 979  ASP   B C     1 
ATOM   15782 O  O     . ASP   B  1 981  ? 4.454   49.414  101.064 1.00 19.74 ? 979  ASP   B O     1 
ATOM   15783 C  CB    . ASP   B  1 981  ? 1.713   48.149  102.256 1.00 20.31 ? 979  ASP   B CB    1 
ATOM   15784 C  CG    . ASP   B  1 981  ? 0.794   46.992  101.953 1.00 23.52 ? 979  ASP   B CG    1 
ATOM   15785 O  OD1   . ASP   B  1 981  ? 1.278   45.984  101.402 1.00 23.87 ? 979  ASP   B OD1   1 
ATOM   15786 O  OD2   . ASP   B  1 981  ? -0.411  47.098  102.258 1.00 25.99 ? 979  ASP   B OD2   1 
ATOM   15787 N  N     . GLU   B  1 982  ? 4.399   49.606  103.302 1.00 20.11 ? 980  GLU   B N     1 
ATOM   15788 C  CA    . GLU   B  1 982  ? 5.265   50.782  103.226 1.00 19.84 ? 980  GLU   B CA    1 
ATOM   15789 C  C     . GLU   B  1 982  ? 6.618   50.416  102.641 1.00 19.29 ? 980  GLU   B C     1 
ATOM   15790 O  O     . GLU   B  1 982  ? 7.172   51.153  101.818 1.00 20.85 ? 980  GLU   B O     1 
ATOM   15791 C  CB    . GLU   B  1 982  ? 5.448   51.433  104.599 1.00 21.22 ? 980  GLU   B CB    1 
ATOM   15792 C  CG    . GLU   B  1 982  ? 6.462   52.569  104.547 1.00 24.55 ? 980  GLU   B CG    1 
ATOM   15793 C  CD    . GLU   B  1 982  ? 6.818   53.129  105.910 1.00 34.64 ? 980  GLU   B CD    1 
ATOM   15794 O  OE1   . GLU   B  1 982  ? 6.794   52.374  106.903 1.00 40.91 ? 980  GLU   B OE1   1 
ATOM   15795 O  OE2   . GLU   B  1 982  ? 7.111   54.337  105.990 1.00 31.50 ? 980  GLU   B OE2   1 
ATOM   15796 N  N     . THR   B  1 983  ? 7.151   49.258  103.027 1.00 20.56 ? 981  THR   B N     1 
ATOM   15797 C  CA    . THR   B  1 983  ? 8.424   48.821  102.470 1.00 18.82 ? 981  THR   B CA    1 
ATOM   15798 C  C     . THR   B  1 983  ? 8.298   48.514  100.981 1.00 20.20 ? 981  THR   B C     1 
ATOM   15799 O  O     . THR   B  1 983  ? 9.192   48.846  100.190 1.00 18.72 ? 981  THR   B O     1 
ATOM   15800 C  CB    . THR   B  1 983  ? 8.933   47.606  103.249 1.00 17.72 ? 981  THR   B CB    1 
ATOM   15801 O  OG1   . THR   B  1 983  ? 9.198   48.006  104.601 1.00 23.07 ? 981  THR   B OG1   1 
ATOM   15802 C  CG2   . THR   B  1 983  ? 10.211  47.064  102.612 1.00 18.24 ? 981  THR   B CG2   1 
ATOM   15803 N  N     . ILE   B  1 984  ? 7.205   47.871  100.578 1.00 16.17 ? 982  ILE   B N     1 
ATOM   15804 C  CA    . ILE   B  1 984  ? 7.003   47.620  99.157  1.00 18.16 ? 982  ILE   B CA    1 
ATOM   15805 C  C     . ILE   B  1 984  ? 6.981   48.930  98.386  1.00 18.51 ? 982  ILE   B C     1 
ATOM   15806 O  O     . ILE   B  1 984  ? 7.660   49.081  97.362  1.00 21.06 ? 982  ILE   B O     1 
ATOM   15807 C  CB    . ILE   B  1 984  ? 5.713   46.819  98.933  1.00 19.87 ? 982  ILE   B CB    1 
ATOM   15808 C  CG1   . ILE   B  1 984  ? 5.892   45.407  99.495  1.00 20.65 ? 982  ILE   B CG1   1 
ATOM   15809 C  CG2   . ILE   B  1 984  ? 5.375   46.784  97.445  1.00 22.34 ? 982  ILE   B CG2   1 
ATOM   15810 C  CD1   . ILE   B  1 984  ? 4.612   44.639  99.606  1.00 22.94 ? 982  ILE   B CD1   1 
ATOM   15811 N  N     . ALA   B  1 985  ? 6.191   49.893  98.861  1.00 18.81 ? 983  ALA   B N     1 
ATOM   15812 C  CA    . ALA   B  1 985  ? 6.082   51.169  98.164  1.00 19.45 ? 983  ALA   B CA    1 
ATOM   15813 C  C     . ALA   B  1 985  ? 7.430   51.876  98.122  1.00 21.56 ? 983  ALA   B C     1 
ATOM   15814 O  O     . ALA   B  1 985  ? 7.856   52.361  97.071  1.00 19.34 ? 983  ALA   B O     1 
ATOM   15815 C  CB    . ALA   B  1 985  ? 5.033   52.049  98.841  1.00 20.91 ? 983  ALA   B CB    1 
ATOM   15816 N  N     . HIS   B  1 986  ? 8.119   51.934  99.264  1.00 19.19 ? 984  HIS   B N     1 
ATOM   15817 C  CA    . HIS   B  1 986  ? 9.429   52.577  99.311  1.00 20.97 ? 984  HIS   B CA    1 
ATOM   15818 C  C     . HIS   B  1 986  ? 10.380  51.937  98.305  1.00 18.62 ? 984  HIS   B C     1 
ATOM   15819 O  O     . HIS   B  1 986  ? 10.914  52.608  97.416  1.00 19.67 ? 984  HIS   B O     1 
ATOM   15820 C  CB    . HIS   B  1 986  ? 9.986   52.487  100.739 1.00 21.64 ? 984  HIS   B CB    1 
ATOM   15821 C  CG    . HIS   B  1 986  ? 11.386  53.006  100.901 1.00 28.32 ? 984  HIS   B CG    1 
ATOM   15822 N  ND1   . HIS   B  1 986  ? 11.977  53.141  102.139 1.00 29.06 ? 984  HIS   B ND1   1 
ATOM   15823 C  CD2   . HIS   B  1 986  ? 12.311  53.415  99.998  1.00 27.87 ? 984  HIS   B CD2   1 
ATOM   15824 C  CE1   . HIS   B  1 986  ? 13.204  53.610  101.992 1.00 31.13 ? 984  HIS   B CE1   1 
ATOM   15825 N  NE2   . HIS   B  1 986  ? 13.434  53.782  100.703 1.00 26.53 ? 984  HIS   B NE2   1 
ATOM   15826 N  N     . VAL   B  1 987  ? 10.577  50.629  98.411  1.00 18.03 ? 985  VAL   B N     1 
ATOM   15827 C  CA    . VAL   B  1 987  ? 11.608  49.968  97.613  1.00 18.51 ? 985  VAL   B CA    1 
ATOM   15828 C  C     . VAL   B  1 987  ? 11.258  50.002  96.124  1.00 19.24 ? 985  VAL   B C     1 
ATOM   15829 O  O     . VAL   B  1 987  ? 12.113  50.299  95.279  1.00 20.59 ? 985  VAL   B O     1 
ATOM   15830 C  CB    . VAL   B  1 987  ? 11.828  48.532  98.117  1.00 20.60 ? 985  VAL   B CB    1 
ATOM   15831 C  CG1   . VAL   B  1 987  ? 12.704  47.760  97.146  1.00 20.28 ? 985  VAL   B CG1   1 
ATOM   15832 C  CG2   . VAL   B  1 987  ? 12.477  48.552  99.508  1.00 18.39 ? 985  VAL   B CG2   1 
ATOM   15833 N  N     . THR   B  1 988  ? 10.011  49.684  95.776  1.00 17.43 ? 986  THR   B N     1 
ATOM   15834 C  CA    . THR   B  1 988  ? 9.647   49.664  94.362  1.00 21.60 ? 986  THR   B CA    1 
ATOM   15835 C  C     . THR   B  1 988  ? 9.627   51.061  93.750  1.00 22.36 ? 986  THR   B C     1 
ATOM   15836 O  O     . THR   B  1 988  ? 9.768   51.183  92.534  1.00 24.56 ? 986  THR   B O     1 
ATOM   15837 C  CB    . THR   B  1 988  ? 8.294   48.972  94.133  1.00 23.14 ? 986  THR   B CB    1 
ATOM   15838 O  OG1   . THR   B  1 988  ? 7.239   49.695  94.779  1.00 21.89 ? 986  THR   B OG1   1 
ATOM   15839 C  CG2   . THR   B  1 988  ? 8.327   47.531  94.643  1.00 24.35 ? 986  THR   B CG2   1 
ATOM   15840 N  N     . SER   B  1 989  ? 9.495   52.113  94.557  1.00 23.73 ? 987  SER   B N     1 
ATOM   15841 C  CA    . SER   B  1 989  ? 9.585   53.468  94.026  1.00 23.99 ? 987  SER   B CA    1 
ATOM   15842 C  C     . SER   B  1 989  ? 11.021  53.914  93.792  1.00 28.51 ? 987  SER   B C     1 
ATOM   15843 O  O     . SER   B  1 989  ? 11.240  54.875  93.048  1.00 29.49 ? 987  SER   B O     1 
ATOM   15844 C  CB    . SER   B  1 989  ? 8.900   54.466  94.965  1.00 24.30 ? 987  SER   B CB    1 
ATOM   15845 O  OG    . SER   B  1 989  ? 9.585   54.569  96.212  1.00 27.90 ? 987  SER   B OG    1 
ATOM   15846 N  N     . ARG   B  1 990  ? 12.000  53.252  94.403  1.00 22.33 ? 988  ARG   B N     1 
ATOM   15847 C  CA    . ARG   B  1 990  ? 13.384  53.707  94.324  1.00 22.67 ? 988  ARG   B CA    1 
ATOM   15848 C  C     . ARG   B  1 990  ? 14.290  52.788  93.520  1.00 23.86 ? 988  ARG   B C     1 
ATOM   15849 O  O     . ARG   B  1 990  ? 15.295  53.251  92.974  1.00 23.18 ? 988  ARG   B O     1 
ATOM   15850 C  CB    . ARG   B  1 990  ? 13.965  53.867  95.732  1.00 20.83 ? 988  ARG   B CB    1 
ATOM   15851 C  CG    . ARG   B  1 990  ? 13.103  54.739  96.658  1.00 28.68 ? 988  ARG   B CG    1 
ATOM   15852 C  CD    . ARG   B  1 990  ? 13.321  56.217  96.420  1.00 26.78 ? 988  ARG   B CD    1 
ATOM   15853 N  NE    . ARG   B  1 990  ? 14.465  56.720  97.174  1.00 28.51 ? 988  ARG   B NE    1 
ATOM   15854 C  CZ    . ARG   B  1 990  ? 14.923  57.963  97.097  1.00 27.43 ? 988  ARG   B CZ    1 
ATOM   15855 N  NH1   . ARG   B  1 990  ? 14.406  58.840  96.254  1.00 30.17 ? 988  ARG   B NH1   1 
ATOM   15856 N  NH2   . ARG   B  1 990  ? 15.919  58.337  97.891  1.00 24.16 ? 988  ARG   B NH2   1 
ATOM   15857 N  N     . ILE   B  1 991  ? 13.972  51.497  93.447  1.00 19.69 ? 989  ILE   B N     1 
ATOM   15858 C  CA    . ILE   B  1 991  ? 14.789  50.572  92.671  1.00 20.22 ? 989  ILE   B CA    1 
ATOM   15859 C  C     . ILE   B  1 991  ? 14.630  50.889  91.188  1.00 22.57 ? 989  ILE   B C     1 
ATOM   15860 O  O     . ILE   B  1 991  ? 13.562  51.307  90.731  1.00 21.74 ? 989  ILE   B O     1 
ATOM   15861 C  CB    . ILE   B  1 991  ? 14.395  49.118  92.994  1.00 21.14 ? 989  ILE   B CB    1 
ATOM   15862 C  CG1   . ILE   B  1 991  ? 15.452  48.140  92.469  1.00 23.46 ? 989  ILE   B CG1   1 
ATOM   15863 C  CG2   . ILE   B  1 991  ? 13.019  48.779  92.432  1.00 25.19 ? 989  ILE   B CG2   1 
ATOM   15864 C  CD1   . ILE   B  1 991  ? 16.729  48.169  93.298  1.00 20.32 ? 989  ILE   B CD1   1 
ATOM   15865 N  N     . LYS   B  1 992  ? 15.699  50.720  90.425  1.00 19.91 ? 990  LYS   B N     1 
ATOM   15866 C  CA    . LYS   B  1 992  ? 15.649  50.976  88.988  1.00 22.88 ? 990  LYS   B CA    1 
ATOM   15867 C  C     . LYS   B  1 992  ? 15.899  49.651  88.275  1.00 23.38 ? 990  LYS   B C     1 
ATOM   15868 O  O     . LYS   B  1 992  ? 17.001  49.384  87.805  1.00 28.64 ? 990  LYS   B O     1 
ATOM   15869 C  CB    . LYS   B  1 992  ? 16.696  52.072  88.583  1.00 21.42 ? 990  LYS   B CB    1 
ATOM   15870 N  N     . ALA   B  1 993  ? 14.883  48.802  88.226  1.00 24.27 ? 991  ALA   B N     1 
ATOM   15871 C  CA    . ALA   B  1 993  ? 15.000  47.524  87.541  1.00 19.27 ? 991  ALA   B CA    1 
ATOM   15872 C  C     . ALA   B  1 993  ? 13.783  47.310  86.652  1.00 18.96 ? 991  ALA   B C     1 
ATOM   15873 O  O     . ALA   B  1 993  ? 12.692  47.823  86.919  1.00 21.33 ? 991  ALA   B O     1 
ATOM   15874 C  CB    . ALA   B  1 993  ? 15.155  46.352  88.526  1.00 18.40 ? 991  ALA   B CB    1 
ATOM   15875 N  N     . GLY   B  1 994  ? 13.990  46.554  85.576  1.00 19.11 ? 992  GLY   B N     1 
ATOM   15876 C  CA    . GLY   B  1 994  ? 12.921  46.351  84.618  1.00 18.51 ? 992  GLY   B CA    1 
ATOM   15877 C  C     . GLY   B  1 994  ? 11.910  45.310  85.035  1.00 17.92 ? 992  GLY   B C     1 
ATOM   15878 O  O     . GLY   B  1 994  ? 10.756  45.365  84.607  1.00 17.50 ? 992  GLY   B O     1 
ATOM   15879 N  N     . ASN   B  1 995  ? 12.320  44.350  85.855  1.00 17.24 ? 993  ASN   B N     1 
ATOM   15880 C  CA    . ASN   B  1 995  ? 11.457  43.254  86.275  1.00 16.95 ? 993  ASN   B CA    1 
ATOM   15881 C  C     . ASN   B  1 995  ? 11.530  43.151  87.789  1.00 18.72 ? 993  ASN   B C     1 
ATOM   15882 O  O     . ASN   B  1 995  ? 12.564  42.750  88.328  1.00 18.62 ? 993  ASN   B O     1 
ATOM   15883 C  CB    . ASN   B  1 995  ? 11.874  41.946  85.606  1.00 14.60 ? 993  ASN   B CB    1 
ATOM   15884 C  CG    . ASN   B  1 995  ? 11.342  41.839  84.185  1.00 16.50 ? 993  ASN   B CG    1 
ATOM   15885 O  OD1   . ASN   B  1 995  ? 11.946  42.353  83.242  1.00 16.87 ? 993  ASN   B OD1   1 
ATOM   15886 N  ND2   . ASN   B  1 995  ? 10.192  41.185  84.031  1.00 18.44 ? 993  ASN   B ND2   1 
ATOM   15887 N  N     . LEU   B  1 996  ? 10.437  43.518  88.464  1.00 16.86 ? 994  LEU   B N     1 
ATOM   15888 C  CA    . LEU   B  1 996  ? 10.363  43.479  89.912  1.00 14.85 ? 994  LEU   B CA    1 
ATOM   15889 C  C     . LEU   B  1 996  ? 9.523   42.289  90.343  1.00 14.93 ? 994  LEU   B C     1 
ATOM   15890 O  O     . LEU   B  1 996  ? 8.527   41.950  89.698  1.00 18.33 ? 994  LEU   B O     1 
ATOM   15891 C  CB    . LEU   B  1 996  ? 9.753   44.765  90.474  1.00 14.74 ? 994  LEU   B CB    1 
ATOM   15892 C  CG    . LEU   B  1 996  ? 10.268  46.058  89.865  1.00 17.92 ? 994  LEU   B CG    1 
ATOM   15893 C  CD1   . LEU   B  1 996  ? 9.560   47.248  90.508  1.00 22.81 ? 994  LEU   B CD1   1 
ATOM   15894 C  CD2   . LEU   B  1 996  ? 11.772  46.154  90.044  1.00 20.64 ? 994  LEU   B CD2   1 
ATOM   15895 N  N     . TYR   B  1 997  ? 9.920   41.664  91.444  1.00 16.62 ? 995  TYR   B N     1 
ATOM   15896 C  CA    . TYR   B  1 997  ? 9.209   40.505  91.956  1.00 15.19 ? 995  TYR   B CA    1 
ATOM   15897 C  C     . TYR   B  1 997  ? 9.044   40.679  93.449  1.00 15.07 ? 995  TYR   B C     1 
ATOM   15898 O  O     . TYR   B  1 997  ? 10.012  40.973  94.156  1.00 18.90 ? 995  TYR   B O     1 
ATOM   15899 C  CB    . TYR   B  1 997  ? 9.949   39.204  91.654  1.00 15.49 ? 995  TYR   B CB    1 
ATOM   15900 C  CG    . TYR   B  1 997  ? 10.174  38.983  90.187  1.00 15.40 ? 995  TYR   B CG    1 
ATOM   15901 C  CD1   . TYR   B  1 997  ? 9.225   38.332  89.409  1.00 19.10 ? 995  TYR   B CD1   1 
ATOM   15902 C  CD2   . TYR   B  1 997  ? 11.329  39.446  89.570  1.00 17.87 ? 995  TYR   B CD2   1 
ATOM   15903 C  CE1   . TYR   B  1 997  ? 9.427   38.133  88.045  1.00 18.48 ? 995  TYR   B CE1   1 
ATOM   15904 C  CE2   . TYR   B  1 997  ? 11.537  39.245  88.198  1.00 19.11 ? 995  TYR   B CE2   1 
ATOM   15905 C  CZ    . TYR   B  1 997  ? 10.588  38.594  87.458  1.00 20.48 ? 995  TYR   B CZ    1 
ATOM   15906 O  OH    . TYR   B  1 997  ? 10.784  38.398  86.114  1.00 25.79 ? 995  TYR   B OH    1 
ATOM   15907 N  N     . ILE   B  1 998  ? 7.823   40.502  93.924  1.00 16.19 ? 996  ILE   B N     1 
ATOM   15908 C  CA    . ILE   B  1 998  ? 7.497   40.737  95.319  1.00 16.72 ? 996  ILE   B CA    1 
ATOM   15909 C  C     . ILE   B  1 998  ? 7.036   39.416  95.916  1.00 16.72 ? 996  ILE   B C     1 
ATOM   15910 O  O     . ILE   B  1 998  ? 6.009   38.860  95.493  1.00 18.26 ? 996  ILE   B O     1 
ATOM   15911 C  CB    . ILE   B  1 998  ? 6.420   41.820  95.477  1.00 20.35 ? 996  ILE   B CB    1 
ATOM   15912 C  CG1   . ILE   B  1 998  ? 6.863   43.126  94.795  1.00 20.24 ? 996  ILE   B CG1   1 
ATOM   15913 C  CG2   . ILE   B  1 998  ? 6.093   42.039  96.967  1.00 19.97 ? 996  ILE   B CG2   1 
ATOM   15914 C  CD1   . ILE   B  1 998  ? 8.061   43.751  95.426  1.00 23.29 ? 996  ILE   B CD1   1 
ATOM   15915 N  N     . ASN   B  1 999  ? 7.790   38.927  96.905  1.00 17.24 ? 997  ASN   B N     1 
ATOM   15916 C  CA    . ASN   B  1 999  ? 7.412   37.749  97.687  1.00 18.42 ? 997  ASN   B CA    1 
ATOM   15917 C  C     . ASN   B  1 999  ? 7.352   36.494  96.823  1.00 16.79 ? 997  ASN   B C     1 
ATOM   15918 O  O     . ASN   B  1 999  ? 6.535   35.598  97.047  1.00 16.80 ? 997  ASN   B O     1 
ATOM   15919 C  CB    . ASN   B  1 999  ? 6.100   37.994  98.440  1.00 18.04 ? 997  ASN   B CB    1 
ATOM   15920 C  CG    . ASN   B  1 999  ? 6.280   39.029  99.543  1.00 16.79 ? 997  ASN   B CG    1 
ATOM   15921 O  OD1   . ASN   B  1 999  ? 7.356   39.119  100.112 1.00 19.26 ? 997  ASN   B OD1   1 
ATOM   15922 N  ND2   . ASN   B  1 999  ? 5.245   39.810  99.838  1.00 19.25 ? 997  ASN   B ND2   1 
ATOM   15923 N  N     . ARG   B  1 1000 ? 8.267   36.409  95.862  1.00 16.43 ? 998  ARG   B N     1 
ATOM   15924 C  CA    . ARG   B  1 1000 ? 8.398   35.240  95.001  1.00 17.51 ? 998  ARG   B CA    1 
ATOM   15925 C  C     . ARG   B  1 1000 ? 9.821   35.216  94.458  1.00 18.26 ? 998  ARG   B C     1 
ATOM   15926 O  O     . ARG   B  1 1000 ? 10.629  36.108  94.740  1.00 18.22 ? 998  ARG   B O     1 
ATOM   15927 C  CB    . ARG   B  1 1000 ? 7.371   35.263  93.863  1.00 17.07 ? 998  ARG   B CB    1 
ATOM   15928 C  CG    . ARG   B  1 1000 ? 7.314   36.596  93.139  1.00 16.66 ? 998  ARG   B CG    1 
ATOM   15929 C  CD    . ARG   B  1 1000 ? 6.844   36.410  91.690  1.00 17.07 ? 998  ARG   B CD    1 
ATOM   15930 N  NE    . ARG   B  1 1000 ? 7.794   35.604  90.926  1.00 15.71 ? 998  ARG   B NE    1 
ATOM   15931 C  CZ    . ARG   B  1 1000 ? 7.619   35.264  89.657  1.00 17.01 ? 998  ARG   B CZ    1 
ATOM   15932 N  NH1   . ARG   B  1 1000 ? 6.558   35.661  88.980  1.00 16.65 ? 998  ARG   B NH1   1 
ATOM   15933 N  NH2   . ARG   B  1 1000 ? 8.538   34.517  89.049  1.00 17.29 ? 998  ARG   B NH2   1 
ATOM   15934 N  N     . ASN   B  1 1001 ? 10.127  34.191  93.662  1.00 15.92 ? 999  ASN   B N     1 
ATOM   15935 C  CA    . ASN   B  1 1001 ? 11.460  34.156  93.073  1.00 17.22 ? 999  ASN   B CA    1 
ATOM   15936 C  C     . ASN   B  1 1001 ? 11.567  35.244  92.003  1.00 16.09 ? 999  ASN   B C     1 
ATOM   15937 O  O     . ASN   B  1 1001 ? 10.589  35.903  91.662  1.00 15.95 ? 999  ASN   B O     1 
ATOM   15938 C  CB    . ASN   B  1 1001 ? 11.781  32.760  92.525  1.00 16.42 ? 999  ASN   B CB    1 
ATOM   15939 C  CG    . ASN   B  1 1001 ? 10.937  32.377  91.326  1.00 19.64 ? 999  ASN   B CG    1 
ATOM   15940 O  OD1   . ASN   B  1 1001 ? 10.749  33.162  90.402  1.00 18.61 ? 999  ASN   B OD1   1 
ATOM   15941 N  ND2   . ASN   B  1 1001 ? 10.430  31.149  91.333  1.00 24.26 ? 999  ASN   B ND2   1 
ATOM   15942 N  N     . ILE   B  1 1002 ? 12.773  35.453  91.484  1.00 16.17 ? 1000 ILE   B N     1 
ATOM   15943 C  CA    . ILE   B  1 1002 ? 12.983  36.531  90.524  1.00 16.64 ? 1000 ILE   B CA    1 
ATOM   15944 C  C     . ILE   B  1 1002 ? 13.306  36.006  89.128  1.00 16.48 ? 1000 ILE   B C     1 
ATOM   15945 O  O     . ILE   B  1 1002 ? 13.842  36.748  88.304  1.00 18.30 ? 1000 ILE   B O     1 
ATOM   15946 C  CB    . ILE   B  1 1002 ? 14.065  37.513  91.001  1.00 14.91 ? 1000 ILE   B CB    1 
ATOM   15947 C  CG1   . ILE   B  1 1002 ? 15.440  36.834  91.114  1.00 14.13 ? 1000 ILE   B CG1   1 
ATOM   15948 C  CG2   . ILE   B  1 1002 ? 13.649  38.115  92.328  1.00 15.04 ? 1000 ILE   B CG2   1 
ATOM   15949 C  CD1   . ILE   B  1 1002 ? 16.557  37.850  91.275  1.00 15.60 ? 1000 ILE   B CD1   1 
ATOM   15950 N  N     . ILE   B  1 1003 ? 12.974  34.754  88.836  1.00 17.44 ? 1001 ILE   B N     1 
ATOM   15951 C  CA    . ILE   B  1 1003 ? 13.367  34.129  87.579  1.00 16.79 ? 1001 ILE   B CA    1 
ATOM   15952 C  C     . ILE   B  1 1003 ? 12.125  33.649  86.824  1.00 22.25 ? 1001 ILE   B C     1 
ATOM   15953 O  O     . ILE   B  1 1003 ? 11.009  33.633  87.347  1.00 25.53 ? 1001 ILE   B O     1 
ATOM   15954 C  CB    . ILE   B  1 1003 ? 14.346  32.960  87.785  1.00 21.32 ? 1001 ILE   B CB    1 
ATOM   15955 C  CG1   . ILE   B  1 1003 ? 13.681  31.831  88.569  1.00 24.43 ? 1001 ILE   B CG1   1 
ATOM   15956 C  CG2   . ILE   B  1 1003 ? 15.617  33.433  88.478  1.00 17.11 ? 1001 ILE   B CG2   1 
ATOM   15957 C  CD1   . ILE   B  1 1003 ? 14.489  30.522  88.514  1.00 25.60 ? 1001 ILE   B CD1   1 
ATOM   15958 N  N     . GLY   B  1 1004 ? 12.346  33.235  85.582  1.00 20.28 ? 1002 GLY   B N     1 
ATOM   15959 C  CA    . GLY   B  1 1004 ? 11.302  32.562  84.832  1.00 23.23 ? 1002 GLY   B CA    1 
ATOM   15960 C  C     . GLY   B  1 1004 ? 10.194  33.491  84.397  1.00 25.53 ? 1002 GLY   B C     1 
ATOM   15961 O  O     . GLY   B  1 1004 ? 9.011   33.126  84.483  1.00 23.88 ? 1002 GLY   B O     1 
ATOM   15962 N  N     . ALA   B  1 1005 ? 10.548  34.700  83.962  1.00 23.33 ? 1003 ALA   B N     1 
ATOM   15963 C  CA    . ALA   B  1 1005 ? 9.562   35.644  83.466  1.00 18.25 ? 1003 ALA   B CA    1 
ATOM   15964 C  C     . ALA   B  1 1005 ? 8.732   35.025  82.353  1.00 23.14 ? 1003 ALA   B C     1 
ATOM   15965 O  O     . ALA   B  1 1005 ? 9.260   34.373  81.451  1.00 26.26 ? 1003 ALA   B O     1 
ATOM   15966 C  CB    . ALA   B  1 1005 ? 10.251  36.904  82.950  1.00 24.56 ? 1003 ALA   B CB    1 
ATOM   15967 N  N     . VAL   B  1 1006 ? 7.428   35.255  82.418  1.00 16.72 ? 1004 VAL   B N     1 
ATOM   15968 C  CA    . VAL   B  1 1006 ? 6.450   34.611  81.546  1.00 17.84 ? 1004 VAL   B CA    1 
ATOM   15969 C  C     . VAL   B  1 1006 ? 6.074   35.579  80.437  1.00 16.41 ? 1004 VAL   B C     1 
ATOM   15970 O  O     . VAL   B  1 1006 ? 5.762   36.747  80.698  1.00 16.70 ? 1004 VAL   B O     1 
ATOM   15971 C  CB    . VAL   B  1 1006 ? 5.213   34.163  82.346  1.00 18.59 ? 1004 VAL   B CB    1 
ATOM   15972 C  CG1   . VAL   B  1 1006 ? 4.074   33.714  81.417  1.00 20.10 ? 1004 VAL   B CG1   1 
ATOM   15973 C  CG2   . VAL   B  1 1006 ? 5.610   33.038  83.289  1.00 21.03 ? 1004 VAL   B CG2   1 
ATOM   15974 N  N     . VAL   B  1 1007 ? 6.094   35.088  79.199  1.00 15.87 ? 1005 VAL   B N     1 
ATOM   15975 C  CA    . VAL   B  1 1007 ? 5.789   35.929  78.048  1.00 17.47 ? 1005 VAL   B CA    1 
ATOM   15976 C  C     . VAL   B  1 1007 ? 4.409   36.562  78.201  1.00 16.83 ? 1005 VAL   B C     1 
ATOM   15977 O  O     . VAL   B  1 1007 ? 3.417   35.886  78.509  1.00 16.97 ? 1005 VAL   B O     1 
ATOM   15978 C  CB    . VAL   B  1 1007 ? 5.894   35.101  76.759  1.00 14.94 ? 1005 VAL   B CB    1 
ATOM   15979 C  CG1   . VAL   B  1 1007 ? 5.361   35.916  75.572  1.00 15.86 ? 1005 VAL   B CG1   1 
ATOM   15980 C  CG2   . VAL   B  1 1007 ? 7.352   34.661  76.514  1.00 16.90 ? 1005 VAL   B CG2   1 
ATOM   15981 N  N     . GLY   B  1 1008 ? 4.338   37.876  77.990  1.00 17.84 ? 1006 GLY   B N     1 
ATOM   15982 C  CA    . GLY   B  1 1008 ? 3.076   38.589  78.070  1.00 16.73 ? 1006 GLY   B CA    1 
ATOM   15983 C  C     . GLY   B  1 1008 ? 2.481   38.700  79.458  1.00 16.65 ? 1006 GLY   B C     1 
ATOM   15984 O  O     . GLY   B  1 1008 ? 1.364   39.211  79.599  1.00 18.82 ? 1006 GLY   B O     1 
ATOM   15985 N  N     . VAL   B  1 1009 ? 3.187   38.236  80.480  1.00 15.77 ? 1007 VAL   B N     1 
ATOM   15986 C  CA    . VAL   B  1 1009 ? 2.752   38.332  81.869  1.00 17.93 ? 1007 VAL   B CA    1 
ATOM   15987 C  C     . VAL   B  1 1009 ? 3.773   39.096  82.705  1.00 17.08 ? 1007 VAL   B C     1 
ATOM   15988 O  O     . VAL   B  1 1009 ? 3.421   40.017  83.458  1.00 16.95 ? 1007 VAL   B O     1 
ATOM   15989 C  CB    . VAL   B  1 1009 ? 2.494   36.932  82.470  1.00 19.63 ? 1007 VAL   B CB    1 
ATOM   15990 C  CG1   . VAL   B  1 1009 ? 2.068   37.033  83.942  1.00 18.75 ? 1007 VAL   B CG1   1 
ATOM   15991 C  CG2   . VAL   B  1 1009 ? 1.455   36.180  81.627  1.00 18.05 ? 1007 VAL   B CG2   1 
ATOM   15992 N  N     . GLN   B  1 1010 ? 5.051   38.724  82.585  1.00 15.64 ? 1008 GLN   B N     1 
ATOM   15993 C  CA    . GLN   B  1 1010 ? 6.178   39.551  83.002  1.00 18.19 ? 1008 GLN   B CA    1 
ATOM   15994 C  C     . GLN   B  1 1010 ? 7.030   39.790  81.764  1.00 16.26 ? 1008 GLN   B C     1 
ATOM   15995 O  O     . GLN   B  1 1010 ? 8.069   39.141  81.591  1.00 18.64 ? 1008 GLN   B O     1 
ATOM   15996 C  CB    . GLN   B  1 1010 ? 7.012   38.904  84.107  1.00 16.23 ? 1008 GLN   B CB    1 
ATOM   15997 C  CG    . GLN   B  1 1010 ? 6.218   38.581  85.350  1.00 17.29 ? 1008 GLN   B CG    1 
ATOM   15998 C  CD    . GLN   B  1 1010 ? 5.828   37.129  85.408  1.00 16.52 ? 1008 GLN   B CD    1 
ATOM   15999 O  OE1   . GLN   B  1 1010 ? 6.520   36.271  84.858  1.00 20.26 ? 1008 GLN   B OE1   1 
ATOM   16000 N  NE2   . GLN   B  1 1010 ? 4.706   36.839  86.066  1.00 17.31 ? 1008 GLN   B NE2   1 
ATOM   16001 N  N     . PRO   B  1 1011 ? 6.610   40.688  80.878  1.00 18.04 ? 1009 PRO   B N     1 
ATOM   16002 C  CA    . PRO   B  1 1011 ? 7.502   41.138  79.803  1.00 16.48 ? 1009 PRO   B CA    1 
ATOM   16003 C  C     . PRO   B  1 1011 ? 8.884   41.430  80.365  1.00 17.46 ? 1009 PRO   B C     1 
ATOM   16004 O  O     . PRO   B  1 1011 ? 9.035   42.079  81.411  1.00 18.05 ? 1009 PRO   B O     1 
ATOM   16005 C  CB    . PRO   B  1 1011 ? 6.819   42.404  79.284  1.00 16.67 ? 1009 PRO   B CB    1 
ATOM   16006 C  CG    . PRO   B  1 1011 ? 5.382   42.235  79.648  1.00 18.48 ? 1009 PRO   B CG    1 
ATOM   16007 C  CD    . PRO   B  1 1011 ? 5.397   41.518  80.976  1.00 15.55 ? 1009 PRO   B CD    1 
ATOM   16008 N  N     . PHE   B  1 1012 ? 9.901   40.924  79.690  1.00 18.27 ? 1010 PHE   B N     1 
ATOM   16009 C  CA    . PHE   B  1 1012 ? 11.209  40.773  80.302  1.00 17.29 ? 1010 PHE   B CA    1 
ATOM   16010 C  C     . PHE   B  1 1012 ? 12.228  41.689  79.644  1.00 18.56 ? 1010 PHE   B C     1 
ATOM   16011 O  O     . PHE   B  1 1012 ? 12.379  41.684  78.421  1.00 18.73 ? 1010 PHE   B O     1 
ATOM   16012 C  CB    . PHE   B  1 1012 ? 11.684  39.329  80.215  1.00 16.28 ? 1010 PHE   B CB    1 
ATOM   16013 C  CG    . PHE   B  1 1012 ? 12.967  39.085  80.954  1.00 19.42 ? 1010 PHE   B CG    1 
ATOM   16014 C  CD1   . PHE   B  1 1012 ? 12.953  38.889  82.323  1.00 20.10 ? 1010 PHE   B CD1   1 
ATOM   16015 C  CD2   . PHE   B  1 1012 ? 14.185  39.086  80.290  1.00 21.53 ? 1010 PHE   B CD2   1 
ATOM   16016 C  CE1   . PHE   B  1 1012 ? 14.120  38.673  83.016  1.00 19.27 ? 1010 PHE   B CE1   1 
ATOM   16017 C  CE2   . PHE   B  1 1012 ? 15.375  38.872  80.986  1.00 22.40 ? 1010 PHE   B CE2   1 
ATOM   16018 C  CZ    . PHE   B  1 1012 ? 15.332  38.666  82.347  1.00 22.40 ? 1010 PHE   B CZ    1 
ATOM   16019 N  N     . GLY   B  1 1013 ? 12.954  42.424  80.460  1.00 16.80 ? 1011 GLY   B N     1 
ATOM   16020 C  CA    . GLY   B  1 1013 ? 14.032  43.250  79.959  1.00 22.00 ? 1011 GLY   B CA    1 
ATOM   16021 C  C     . GLY   B  1 1013 ? 14.218  44.418  80.894  1.00 23.80 ? 1011 GLY   B C     1 
ATOM   16022 O  O     . GLY   B  1 1013 ? 13.287  44.908  81.530  1.00 21.93 ? 1011 GLY   B O     1 
ATOM   16023 N  N     . GLY   B  1 1014 ? 15.457  44.880  80.978  1.00 24.96 ? 1012 GLY   B N     1 
ATOM   16024 C  CA    . GLY   B  1 1014 ? 15.796  45.926  81.911  1.00 22.21 ? 1012 GLY   B CA    1 
ATOM   16025 C  C     . GLY   B  1 1014 ? 16.366  47.159  81.252  1.00 26.30 ? 1012 GLY   B C     1 
ATOM   16026 O  O     . GLY   B  1 1014 ? 16.263  47.338  80.035  1.00 29.78 ? 1012 GLY   B O     1 
ATOM   16027 N  N     . ARG   B  1 1015 ? 16.979  48.008  82.059  1.00 26.12 ? 1013 ARG   B N     1 
ATOM   16028 C  CA    . ARG   B  1 1015 ? 17.518  49.292  81.647  1.00 29.06 ? 1013 ARG   B CA    1 
ATOM   16029 C  C     . ARG   B  1 1015 ? 19.004  49.347  81.982  1.00 27.87 ? 1013 ARG   B C     1 
ATOM   16030 O  O     . ARG   B  1 1015 ? 19.573  48.412  82.556  1.00 26.36 ? 1013 ARG   B O     1 
ATOM   16031 C  CB    . ARG   B  1 1015 ? 16.770  50.429  82.342  1.00 31.48 ? 1013 ARG   B CB    1 
ATOM   16032 C  CG    . ARG   B  1 1015 ? 16.629  50.216  83.847  1.00 30.87 ? 1013 ARG   B CG    1 
ATOM   16033 C  CD    . ARG   B  1 1015 ? 16.626  51.528  84.610  1.00 36.15 ? 1013 ARG   B CD    1 
ATOM   16034 N  NE    . ARG   B  1 1015 ? 17.938  52.168  84.565  1.00 37.79 ? 1013 ARG   B NE    1 
ATOM   16035 C  CZ    . ARG   B  1 1015 ? 18.996  51.769  85.261  1.00 36.09 ? 1013 ARG   B CZ    1 
ATOM   16036 N  NH1   . ARG   B  1 1015 ? 18.938  50.728  86.080  1.00 31.95 ? 1013 ARG   B NH1   1 
ATOM   16037 N  NH2   . ARG   B  1 1015 ? 20.148  52.424  85.125  1.00 37.01 ? 1013 ARG   B NH2   1 
ATOM   16038 N  N     . GLY   B  1 1016 ? 19.627  50.471  81.640  1.00 26.16 ? 1014 GLY   B N     1 
ATOM   16039 C  CA    . GLY   B  1 1016 ? 21.024  50.648  81.987  1.00 25.07 ? 1014 GLY   B CA    1 
ATOM   16040 C  C     . GLY   B  1 1016 ? 21.878  49.633  81.270  1.00 25.83 ? 1014 GLY   B C     1 
ATOM   16041 O  O     . GLY   B  1 1016 ? 21.695  49.370  80.077  1.00 24.76 ? 1014 GLY   B O     1 
ATOM   16042 N  N     . LEU   B  1 1017 ? 22.810  49.029  82.011  1.00 26.56 ? 1015 LEU   B N     1 
ATOM   16043 C  CA    . LEU   B  1 1017 ? 23.680  48.003  81.456  1.00 24.01 ? 1015 LEU   B CA    1 
ATOM   16044 C  C     . LEU   B  1 1017 ? 22.939  46.723  81.104  1.00 26.61 ? 1015 LEU   B C     1 
ATOM   16045 O  O     . LEU   B  1 1017 ? 23.548  45.823  80.517  1.00 23.01 ? 1015 LEU   B O     1 
ATOM   16046 C  CB    . LEU   B  1 1017 ? 24.803  47.673  82.440  1.00 25.22 ? 1015 LEU   B CB    1 
ATOM   16047 C  CG    . LEU   B  1 1017 ? 25.813  48.794  82.741  1.00 30.04 ? 1015 LEU   B CG    1 
ATOM   16048 C  CD1   . LEU   B  1 1017 ? 26.894  48.300  83.690  1.00 35.13 ? 1015 LEU   B CD1   1 
ATOM   16049 C  CD2   . LEU   B  1 1017 ? 26.424  49.331  81.453  1.00 28.45 ? 1015 LEU   B CD2   1 
ATOM   16050 N  N     . SER   B  1 1018 ? 21.662  46.610  81.462  1.00 20.99 ? 1016 SER   B N     1 
ATOM   16051 C  CA    . SER   B  1 1018 ? 20.902  45.394  81.214  1.00 22.97 ? 1016 SER   B CA    1 
ATOM   16052 C  C     . SER   B  1 1018 ? 20.266  45.342  79.837  1.00 25.33 ? 1016 SER   B C     1 
ATOM   16053 O  O     . SER   B  1 1018 ? 19.794  44.277  79.431  1.00 23.02 ? 1016 SER   B O     1 
ATOM   16054 C  CB    . SER   B  1 1018 ? 19.815  45.232  82.284  1.00 21.41 ? 1016 SER   B CB    1 
ATOM   16055 O  OG    . SER   B  1 1018 ? 20.424  44.860  83.515  1.00 24.02 ? 1016 SER   B OG    1 
ATOM   16056 N  N     . GLY   B  1 1019 ? 20.211  46.445  79.119  1.00 26.64 ? 1017 GLY   B N     1 
ATOM   16057 C  CA    . GLY   B  1 1019 ? 19.860  46.355  77.720  1.00 26.72 ? 1017 GLY   B CA    1 
ATOM   16058 C  C     . GLY   B  1 1019 ? 19.251  47.635  77.199  1.00 25.58 ? 1017 GLY   B C     1 
ATOM   16059 O  O     . GLY   B  1 1019 ? 19.179  48.650  77.878  1.00 22.98 ? 1017 GLY   B O     1 
ATOM   16060 N  N     . THR   B  1 1020 ? 18.810  47.547  75.953  1.00 18.93 ? 1018 THR   B N     1 
ATOM   16061 C  CA    . THR   B  1 1020 ? 18.205  48.666  75.257  1.00 22.72 ? 1018 THR   B CA    1 
ATOM   16062 C  C     . THR   B  1 1020 ? 16.699  48.697  75.401  1.00 22.18 ? 1018 THR   B C     1 
ATOM   16063 O  O     . THR   B  1 1020 ? 16.091  49.758  75.234  1.00 25.54 ? 1018 THR   B O     1 
ATOM   16064 C  CB    . THR   B  1 1020 ? 18.540  48.573  73.772  1.00 22.43 ? 1018 THR   B CB    1 
ATOM   16065 O  OG1   . THR   B  1 1020 ? 18.034  47.325  73.276  1.00 21.73 ? 1018 THR   B OG1   1 
ATOM   16066 C  CG2   . THR   B  1 1020 ? 20.056  48.603  73.574  1.00 20.83 ? 1018 THR   B CG2   1 
ATOM   16067 N  N     . GLY   B  1 1021 ? 16.084  47.559  75.666  1.00 20.72 ? 1019 GLY   B N     1 
ATOM   16068 C  CA    . GLY   B  1 1021 ? 14.676  47.424  75.407  1.00 22.07 ? 1019 GLY   B CA    1 
ATOM   16069 C  C     . GLY   B  1 1021 ? 14.437  47.414  73.910  1.00 21.14 ? 1019 GLY   B C     1 
ATOM   16070 O  O     . GLY   B  1 1021 ? 15.374  47.496  73.102  1.00 21.41 ? 1019 GLY   B O     1 
ATOM   16071 N  N     . PRO   B  1 1022 ? 13.173  47.288  73.509  1.00 18.63 ? 1020 PRO   B N     1 
ATOM   16072 C  CA    . PRO   B  1 1022 ? 11.995  47.088  74.368  1.00 19.83 ? 1020 PRO   B CA    1 
ATOM   16073 C  C     . PRO   B  1 1022 ? 11.978  45.686  74.967  1.00 19.18 ? 1020 PRO   B C     1 
ATOM   16074 O  O     . PRO   B  1 1022 ? 12.766  44.823  74.567  1.00 19.55 ? 1020 PRO   B O     1 
ATOM   16075 C  CB    . PRO   B  1 1022 ? 10.823  47.304  73.404  1.00 18.19 ? 1020 PRO   B CB    1 
ATOM   16076 C  CG    . PRO   B  1 1022 ? 11.376  46.823  72.065  1.00 19.23 ? 1020 PRO   B CG    1 
ATOM   16077 C  CD    . PRO   B  1 1022 ? 12.832  47.244  72.074  1.00 20.86 ? 1020 PRO   B CD    1 
ATOM   16078 N  N     . LYS   B  1 1023 ? 11.089  45.441  75.928  1.00 17.20 ? 1021 LYS   B N     1 
ATOM   16079 C  CA    . LYS   B  1 1023 ? 11.042  44.148  76.593  1.00 15.82 ? 1021 LYS   B CA    1 
ATOM   16080 C  C     . LYS   B  1 1023 ? 10.616  43.045  75.643  1.00 18.79 ? 1021 LYS   B C     1 
ATOM   16081 O  O     . LYS   B  1 1023 ? 9.645   43.189  74.900  1.00 15.09 ? 1021 LYS   B O     1 
ATOM   16082 C  CB    . LYS   B  1 1023 ? 10.061  44.175  77.753  1.00 14.66 ? 1021 LYS   B CB    1 
ATOM   16083 C  CG    . LYS   B  1 1023 ? 10.537  44.916  78.960  1.00 15.05 ? 1021 LYS   B CG    1 
ATOM   16084 C  CD    . LYS   B  1 1023 ? 9.360   45.069  79.901  1.00 17.23 ? 1021 LYS   B CD    1 
ATOM   16085 C  CE    . LYS   B  1 1023 ? 9.815   45.503  81.276  1.00 17.54 ? 1021 LYS   B CE    1 
ATOM   16086 N  NZ    . LYS   B  1 1023 ? 10.426  44.361  82.024  1.00 15.67 ? 1021 LYS   B NZ    1 
ATOM   16087 N  N     . ALA   B  1 1024 ? 11.329  41.924  75.718  1.00 18.73 ? 1022 ALA   B N     1 
ATOM   16088 C  CA    . ALA   B  1 1024 ? 10.874  40.684  75.108  1.00 18.02 ? 1022 ALA   B CA    1 
ATOM   16089 C  C     . ALA   B  1 1024 ? 9.563   40.221  75.732  1.00 17.77 ? 1022 ALA   B C     1 
ATOM   16090 O  O     . ALA   B  1 1024 ? 9.321   40.396  76.932  1.00 16.77 ? 1022 ALA   B O     1 
ATOM   16091 C  CB    . ALA   B  1 1024 ? 11.953  39.599  75.270  1.00 17.71 ? 1022 ALA   B CB    1 
ATOM   16092 N  N     . GLY   B  1 1025 ? 8.705   39.630  74.905  1.00 15.34 ? 1023 GLY   B N     1 
ATOM   16093 C  CA    . GLY   B  1 1025 ? 7.438   39.155  75.416  1.00 13.98 ? 1023 GLY   B CA    1 
ATOM   16094 C  C     . GLY   B  1 1025 ? 6.558   40.287  75.895  1.00 14.59 ? 1023 GLY   B C     1 
ATOM   16095 O  O     . GLY   B  1 1025 ? 5.700   40.083  76.752  1.00 17.66 ? 1023 GLY   B O     1 
ATOM   16096 N  N     . GLY   B  1 1026 ? 6.748   41.476  75.344  1.00 15.92 ? 1024 GLY   B N     1 
ATOM   16097 C  CA    . GLY   B  1 1026 ? 5.939   42.616  75.688  1.00 13.91 ? 1024 GLY   B CA    1 
ATOM   16098 C  C     . GLY   B  1 1026 ? 5.479   43.320  74.431  1.00 14.97 ? 1024 GLY   B C     1 
ATOM   16099 O  O     . GLY   B  1 1026 ? 5.950   43.041  73.322  1.00 14.53 ? 1024 GLY   B O     1 
ATOM   16100 N  N     . PRO   B  1 1027 ? 4.572   44.285  74.606  1.00 16.05 ? 1025 PRO   B N     1 
ATOM   16101 C  CA    . PRO   B  1 1027 ? 3.816   44.837  73.475  1.00 14.40 ? 1025 PRO   B CA    1 
ATOM   16102 C  C     . PRO   B  1 1027 ? 4.573   45.851  72.632  1.00 16.60 ? 1025 PRO   B C     1 
ATOM   16103 O  O     . PRO   B  1 1027 ? 4.069   46.228  71.566  1.00 17.19 ? 1025 PRO   B O     1 
ATOM   16104 C  CB    . PRO   B  1 1027 ? 2.616   45.495  74.170  1.00 16.90 ? 1025 PRO   B CB    1 
ATOM   16105 C  CG    . PRO   B  1 1027 ? 3.178   45.913  75.525  1.00 19.37 ? 1025 PRO   B CG    1 
ATOM   16106 C  CD    . PRO   B  1 1027 ? 4.085   44.783  75.907  1.00 17.73 ? 1025 PRO   B CD    1 
ATOM   16107 N  N     . LEU   B  1 1028 ? 5.736   46.325  73.079  1.00 15.93 ? 1026 LEU   B N     1 
ATOM   16108 C  CA    . LEU   B  1 1028 ? 6.535   47.267  72.302  1.00 16.47 ? 1026 LEU   B CA    1 
ATOM   16109 C  C     . LEU   B  1 1028 ? 7.545   46.578  71.406  1.00 14.80 ? 1026 LEU   B C     1 
ATOM   16110 O  O     . LEU   B  1 1028 ? 8.183   47.247  70.582  1.00 17.96 ? 1026 LEU   B O     1 
ATOM   16111 C  CB    . LEU   B  1 1028 ? 7.277   48.233  73.226  1.00 17.38 ? 1026 LEU   B CB    1 
ATOM   16112 C  CG    . LEU   B  1 1028 ? 6.380   49.113  74.093  1.00 21.64 ? 1026 LEU   B CG    1 
ATOM   16113 C  CD1   . LEU   B  1 1028 ? 7.217   50.063  74.937  1.00 23.19 ? 1026 LEU   B CD1   1 
ATOM   16114 C  CD2   . LEU   B  1 1028 ? 5.428   49.875  73.211  1.00 24.42 ? 1026 LEU   B CD2   1 
ATOM   16115 N  N     . TYR   B  1 1029 ? 7.689   45.262  71.542  1.00 15.62 ? 1027 TYR   B N     1 
ATOM   16116 C  CA    . TYR   B  1 1029 ? 8.814   44.555  70.934  1.00 15.57 ? 1027 TYR   B CA    1 
ATOM   16117 C  C     . TYR   B  1 1029 ? 8.748   44.602  69.417  1.00 17.52 ? 1027 TYR   B C     1 
ATOM   16118 O  O     . TYR   B  1 1029 ? 9.734   44.942  68.759  1.00 15.99 ? 1027 TYR   B O     1 
ATOM   16119 C  CB    . TYR   B  1 1029 ? 8.823   43.106  71.412  1.00 15.08 ? 1027 TYR   B CB    1 
ATOM   16120 C  CG    . TYR   B  1 1029 ? 10.132  42.358  71.311  1.00 17.83 ? 1027 TYR   B CG    1 
ATOM   16121 C  CD1   . TYR   B  1 1029 ? 11.215  42.685  72.124  1.00 17.16 ? 1027 TYR   B CD1   1 
ATOM   16122 C  CD2   . TYR   B  1 1029 ? 10.248  41.243  70.487  1.00 17.45 ? 1027 TYR   B CD2   1 
ATOM   16123 C  CE1   . TYR   B  1 1029 ? 12.389  41.952  72.079  1.00 17.72 ? 1027 TYR   B CE1   1 
ATOM   16124 C  CE2   . TYR   B  1 1029 ? 11.421  40.502  70.446  1.00 16.82 ? 1027 TYR   B CE2   1 
ATOM   16125 C  CZ    . TYR   B  1 1029 ? 12.480  40.862  71.240  1.00 20.71 ? 1027 TYR   B CZ    1 
ATOM   16126 O  OH    . TYR   B  1 1029 ? 13.633  40.120  71.195  1.00 21.95 ? 1027 TYR   B OH    1 
ATOM   16127 N  N     . LEU   B  1 1030 ? 7.600   44.239  68.840  1.00 16.14 ? 1028 LEU   B N     1 
ATOM   16128 C  CA    . LEU   B  1 1030 ? 7.528   44.152  67.380  1.00 16.29 ? 1028 LEU   B CA    1 
ATOM   16129 C  C     . LEU   B  1 1030 ? 7.709   45.514  66.725  1.00 18.49 ? 1028 LEU   B C     1 
ATOM   16130 O  O     . LEU   B  1 1030 ? 8.242   45.598  65.609  1.00 15.78 ? 1028 LEU   B O     1 
ATOM   16131 C  CB    . LEU   B  1 1030 ? 6.200   43.537  66.961  1.00 17.95 ? 1028 LEU   B CB    1 
ATOM   16132 C  CG    . LEU   B  1 1030 ? 5.969   42.092  67.401  1.00 17.87 ? 1028 LEU   B CG    1 
ATOM   16133 C  CD1   . LEU   B  1 1030 ? 4.612   41.636  66.883  1.00 18.12 ? 1028 LEU   B CD1   1 
ATOM   16134 C  CD2   . LEU   B  1 1030 ? 7.074   41.188  66.861  1.00 16.22 ? 1028 LEU   B CD2   1 
ATOM   16135 N  N     . GLY   B  1 1031 ? 7.287   46.583  67.407  1.00 17.77 ? 1029 GLY   B N     1 
ATOM   16136 C  CA    . GLY   B  1 1031 ? 7.419   47.929  66.872  1.00 18.92 ? 1029 GLY   B CA    1 
ATOM   16137 C  C     . GLY   B  1 1031 ? 8.843   48.327  66.566  1.00 18.77 ? 1029 GLY   B C     1 
ATOM   16138 O  O     . GLY   B  1 1031 ? 9.070   49.219  65.748  1.00 21.00 ? 1029 GLY   B O     1 
ATOM   16139 N  N     . ARG   B  1 1032 ? 9.812   47.699  67.219  1.00 17.35 ? 1030 ARG   B N     1 
ATOM   16140 C  CA    . ARG   B  1 1032 ? 11.203  48.009  66.961  1.00 16.59 ? 1030 ARG   B CA    1 
ATOM   16141 C  C     . ARG   B  1 1032 ? 11.712  47.351  65.691  1.00 18.99 ? 1030 ARG   B C     1 
ATOM   16142 O  O     . ARG   B  1 1032 ? 12.767  47.746  65.171  1.00 20.64 ? 1030 ARG   B O     1 
ATOM   16143 C  CB    . ARG   B  1 1032 ? 12.052  47.565  68.159  1.00 18.88 ? 1030 ARG   B CB    1 
ATOM   16144 C  CG    . ARG   B  1 1032 ? 13.466  48.063  68.118  1.00 22.43 ? 1030 ARG   B CG    1 
ATOM   16145 C  CD    . ARG   B  1 1032 ? 13.536  49.531  68.453  1.00 25.37 ? 1030 ARG   B CD    1 
ATOM   16146 N  NE    . ARG   B  1 1032 ? 14.920  49.915  68.678  1.00 24.50 ? 1030 ARG   B NE    1 
ATOM   16147 C  CZ    . ARG   B  1 1032 ? 15.595  50.786  67.941  1.00 25.93 ? 1030 ARG   B CZ    1 
ATOM   16148 N  NH1   . ARG   B  1 1032 ? 15.017  51.458  66.960  1.00 29.61 ? 1030 ARG   B NH1   1 
ATOM   16149 N  NH2   . ARG   B  1 1032 ? 16.878  50.994  68.204  1.00 27.24 ? 1030 ARG   B NH2   1 
ATOM   16150 N  N     . LEU   B  1 1033 ? 10.987  46.364  65.177  1.00 18.82 ? 1031 LEU   B N     1 
ATOM   16151 C  CA    . LEU   B  1 1033 ? 11.447  45.556  64.056  1.00 18.86 ? 1031 LEU   B CA    1 
ATOM   16152 C  C     . LEU   B  1 1033 ? 10.790  45.974  62.743  1.00 21.69 ? 1031 LEU   B C     1 
ATOM   16153 O  O     . LEU   B  1 1033 ? 10.826  45.223  61.764  1.00 17.76 ? 1031 LEU   B O     1 
ATOM   16154 C  CB    . LEU   B  1 1033 ? 11.191  44.081  64.363  1.00 16.79 ? 1031 LEU   B CB    1 
ATOM   16155 C  CG    . LEU   B  1 1033 ? 11.836  43.700  65.707  1.00 19.18 ? 1031 LEU   B CG    1 
ATOM   16156 C  CD1   . LEU   B  1 1033 ? 11.417  42.315  66.199  1.00 18.56 ? 1031 LEU   B CD1   1 
ATOM   16157 C  CD2   . LEU   B  1 1033 ? 13.350  43.787  65.643  1.00 23.79 ? 1031 LEU   B CD2   1 
ATOM   16158 N  N     . VAL   B  1 1034 ? 10.178  47.158  62.719  1.00 17.24 ? 1032 VAL   B N     1 
ATOM   16159 C  CA    . VAL   B  1 1034 ? 9.551   47.728  61.535  1.00 18.21 ? 1032 VAL   B CA    1 
ATOM   16160 C  C     . VAL   B  1 1034 ? 9.985   49.180  61.445  1.00 20.44 ? 1032 VAL   B C     1 
ATOM   16161 O  O     . VAL   B  1 1034 ? 10.447  49.773  62.422  1.00 20.72 ? 1032 VAL   B O     1 
ATOM   16162 C  CB    . VAL   B  1 1034 ? 8.012   47.635  61.564  1.00 19.88 ? 1032 VAL   B CB    1 
ATOM   16163 C  CG1   . VAL   B  1 1034 ? 7.558   46.198  61.342  1.00 20.59 ? 1032 VAL   B CG1   1 
ATOM   16164 C  CG2   . VAL   B  1 1034 ? 7.471   48.204  62.875  1.00 19.42 ? 1032 VAL   B CG2   1 
ATOM   16165 N  N     . THR   B  1 1035 ? 9.856   49.755  60.251  1.00 19.38 ? 1033 THR   B N     1 
ATOM   16166 C  CA    . THR   B  1 1035 ? 10.346  51.117  60.087  1.00 22.52 ? 1033 THR   B CA    1 
ATOM   16167 C  C     . THR   B  1 1035 ? 9.360   52.151  60.605  1.00 24.10 ? 1033 THR   B C     1 
ATOM   16168 O  O     . THR   B  1 1035 ? 9.779   53.258  60.961  1.00 27.57 ? 1033 THR   B O     1 
ATOM   16169 C  CB    . THR   B  1 1035 ? 10.686  51.406  58.623  1.00 23.93 ? 1033 THR   B CB    1 
ATOM   16170 O  OG1   . THR   B  1 1035 ? 9.624   50.958  57.781  1.00 29.39 ? 1033 THR   B OG1   1 
ATOM   16171 C  CG2   . THR   B  1 1035 ? 11.975  50.689  58.236  1.00 29.03 ? 1033 THR   B CG2   1 
ATOM   16172 N  N     . THR   B  1 1036 ? 8.078   51.812  60.665  1.00 23.50 ? 1034 THR   B N     1 
ATOM   16173 C  CA    . THR   B  1 1036 ? 7.063   52.634  61.317  1.00 24.44 ? 1034 THR   B CA    1 
ATOM   16174 C  C     . THR   B  1 1036 ? 6.380   51.780  62.372  1.00 20.65 ? 1034 THR   B C     1 
ATOM   16175 O  O     . THR   B  1 1036 ? 5.771   50.761  62.040  1.00 19.55 ? 1034 THR   B O     1 
ATOM   16176 C  CB    . THR   B  1 1036 ? 6.028   53.144  60.321  1.00 25.47 ? 1034 THR   B CB    1 
ATOM   16177 O  OG1   . THR   B  1 1036 ? 6.694   53.807  59.248  1.00 28.45 ? 1034 THR   B OG1   1 
ATOM   16178 C  CG2   . THR   B  1 1036 ? 5.059   54.111  61.018  1.00 26.00 ? 1034 THR   B CG2   1 
ATOM   16179 N  N     . ALA   B  1 1037 ? 6.484   52.190  63.619  1.00 22.91 ? 1035 ALA   B N     1 
ATOM   16180 C  CA    . ALA   B  1 1037 ? 5.957   51.348  64.682  1.00 22.22 ? 1035 ALA   B CA    1 
ATOM   16181 C  C     . ALA   B  1 1037 ? 4.439   51.486  64.765  1.00 23.21 ? 1035 ALA   B C     1 
ATOM   16182 O  O     . ALA   B  1 1037 ? 3.904   52.580  64.591  1.00 21.59 ? 1035 ALA   B O     1 
ATOM   16183 C  CB    . ALA   B  1 1037 ? 6.589   51.716  66.020  1.00 21.62 ? 1035 ALA   B CB    1 
ATOM   16184 N  N     . PRO   B  1 1038 ? 3.728   50.392  65.009  1.00 18.29 ? 1036 PRO   B N     1 
ATOM   16185 C  CA    . PRO   B  1 1038 ? 2.287   50.471  65.247  1.00 22.14 ? 1036 PRO   B CA    1 
ATOM   16186 C  C     . PRO   B  1 1038 ? 1.999   50.930  66.671  1.00 20.05 ? 1036 PRO   B C     1 
ATOM   16187 O  O     . PRO   B  1 1038 ? 2.879   51.024  67.521  1.00 19.37 ? 1036 PRO   B O     1 
ATOM   16188 C  CB    . PRO   B  1 1038 ? 1.821   49.027  65.037  1.00 19.63 ? 1036 PRO   B CB    1 
ATOM   16189 C  CG    . PRO   B  1 1038 ? 2.999   48.215  65.538  1.00 19.26 ? 1036 PRO   B CG    1 
ATOM   16190 C  CD    . PRO   B  1 1038 ? 4.235   49.010  65.109  1.00 18.98 ? 1036 PRO   B CD    1 
ATOM   16191 N  N     . VAL   B  1 1039 ? 0.726   51.213  66.915  1.00 21.52 ? 1037 VAL   B N     1 
ATOM   16192 C  CA    . VAL   B  1 1039 ? 0.248   51.463  68.270  1.00 20.25 ? 1037 VAL   B CA    1 
ATOM   16193 C  C     . VAL   B  1 1039 ? -0.022  50.110  68.914  1.00 17.49 ? 1037 VAL   B C     1 
ATOM   16194 O  O     . VAL   B  1 1039 ? -0.910  49.379  68.454  1.00 19.34 ? 1037 VAL   B O     1 
ATOM   16195 C  CB    . VAL   B  1 1039 ? -1.023  52.325  68.259  1.00 20.44 ? 1037 VAL   B CB    1 
ATOM   16196 C  CG1   . VAL   B  1 1039 ? -1.446  52.637  69.700  1.00 20.05 ? 1037 VAL   B CG1   1 
ATOM   16197 C  CG2   . VAL   B  1 1039 ? -0.785  53.593  67.460  1.00 19.99 ? 1037 VAL   B CG2   1 
ATOM   16198 N  N     . PRO   B  1 1040 ? 0.702   49.726  69.957  1.00 20.15 ? 1038 PRO   B N     1 
ATOM   16199 C  CA    . PRO   B  1 1040 ? 0.458   48.424  70.584  1.00 18.43 ? 1038 PRO   B CA    1 
ATOM   16200 C  C     . PRO   B  1 1040 ? -0.922  48.371  71.209  1.00 18.04 ? 1038 PRO   B C     1 
ATOM   16201 O  O     . PRO   B  1 1040 ? -1.517  49.417  71.515  1.00 19.09 ? 1038 PRO   B O     1 
ATOM   16202 C  CB    . PRO   B  1 1040 ? 1.563   48.334  71.654  1.00 19.47 ? 1038 PRO   B CB    1 
ATOM   16203 C  CG    . PRO   B  1 1040 ? 2.616   49.261  71.169  1.00 19.86 ? 1038 PRO   B CG    1 
ATOM   16204 C  CD    . PRO   B  1 1040 ? 1.865   50.403  70.547  1.00 20.11 ? 1038 PRO   B CD    1 
ATOM   16205 N  N     . PRO   B  1 1041 ? -1.472  47.173  71.398  1.00 17.45 ? 1039 PRO   B N     1 
ATOM   16206 C  CA    . PRO   B  1 1041 ? -2.721  47.048  72.154  1.00 17.59 ? 1039 PRO   B CA    1 
ATOM   16207 C  C     . PRO   B  1 1041 ? -2.593  47.703  73.521  1.00 19.41 ? 1039 PRO   B C     1 
ATOM   16208 O  O     . PRO   B  1 1041 ? -1.538  47.649  74.162  1.00 19.27 ? 1039 PRO   B O     1 
ATOM   16209 C  CB    . PRO   B  1 1041 ? -2.919  45.535  72.273  1.00 22.60 ? 1039 PRO   B CB    1 
ATOM   16210 C  CG    . PRO   B  1 1041 ? -2.036  44.928  71.221  1.00 21.49 ? 1039 PRO   B CG    1 
ATOM   16211 C  CD    . PRO   B  1 1041 ? -0.883  45.866  71.061  1.00 20.91 ? 1039 PRO   B CD    1 
ATOM   16212 N  N     . GLN   B  1 1042 ? -3.667  48.363  73.943  1.00 17.53 ? 1040 GLN   B N     1 
ATOM   16213 C  CA    . GLN   B  1 1042 ? -3.795  48.984  75.260  1.00 21.07 ? 1040 GLN   B CA    1 
ATOM   16214 C  C     . GLN   B  1 1042 ? -2.730  50.042  75.536  1.00 20.75 ? 1040 GLN   B C     1 
ATOM   16215 O  O     . GLN   B  1 1042 ? -2.541  50.442  76.693  1.00 20.92 ? 1040 GLN   B O     1 
ATOM   16216 C  CB    . GLN   B  1 1042 ? -3.767  47.923  76.366  1.00 24.50 ? 1040 GLN   B CB    1 
ATOM   16217 C  CG    . GLN   B  1 1042 ? -4.820  46.832  76.217  1.00 23.22 ? 1040 GLN   B CG    1 
ATOM   16218 C  CD    . GLN   B  1 1042 ? -4.885  45.969  77.459  1.00 34.44 ? 1040 GLN   B CD    1 
ATOM   16219 O  OE1   . GLN   B  1 1042 ? -4.290  44.902  77.515  1.00 38.81 ? 1040 GLN   B OE1   1 
ATOM   16220 N  NE2   . GLN   B  1 1042 ? -5.573  46.458  78.481  1.00 36.03 ? 1040 GLN   B NE2   1 
ATOM   16221 N  N     . HIS   B  1 1043 ? -2.027  50.511  74.514  1.00 18.84 ? 1041 HIS   B N     1 
ATOM   16222 C  CA    . HIS   B  1 1043 ? -0.898  51.417  74.703  1.00 18.13 ? 1041 HIS   B CA    1 
ATOM   16223 C  C     . HIS   B  1 1043 ? -1.401  52.848  74.609  1.00 21.56 ? 1041 HIS   B C     1 
ATOM   16224 O  O     . HIS   B  1 1043 ? -1.470  53.437  73.528  1.00 21.90 ? 1041 HIS   B O     1 
ATOM   16225 C  CB    . HIS   B  1 1043 ? 0.177   51.130  73.665  1.00 16.20 ? 1041 HIS   B CB    1 
ATOM   16226 C  CG    . HIS   B  1 1043 ? 1.362   52.038  73.742  1.00 21.17 ? 1041 HIS   B CG    1 
ATOM   16227 N  ND1   . HIS   B  1 1043 ? 2.481   51.734  74.484  1.00 20.84 ? 1041 HIS   B ND1   1 
ATOM   16228 C  CD2   . HIS   B  1 1043 ? 1.616   53.228  73.145  1.00 22.27 ? 1041 HIS   B CD2   1 
ATOM   16229 C  CE1   . HIS   B  1 1043 ? 3.375   52.697  74.343  1.00 22.57 ? 1041 HIS   B CE1   1 
ATOM   16230 N  NE2   . HIS   B  1 1043 ? 2.872   53.619  73.540  1.00 19.39 ? 1041 HIS   B NE2   1 
ATOM   16231 N  N     . SER   B  1 1044 ? -1.777  53.412  75.753  1.00 18.22 ? 1042 SER   B N     1 
ATOM   16232 C  CA    . SER   B  1 1044 ? -2.188  54.806  75.804  1.00 17.39 ? 1042 SER   B CA    1 
ATOM   16233 C  C     . SER   B  1 1044 ? -2.123  55.244  77.257  1.00 18.82 ? 1042 SER   B C     1 
ATOM   16234 O  O     . SER   B  1 1044 ? -1.910  54.432  78.157  1.00 19.63 ? 1042 SER   B O     1 
ATOM   16235 C  CB    . SER   B  1 1044 ? -3.600  55.001  75.243  1.00 19.87 ? 1042 SER   B CB    1 
ATOM   16236 O  OG    . SER   B  1 1044 ? -4.545  54.438  76.133  1.00 18.71 ? 1042 SER   B OG    1 
ATOM   16237 N  N     . SER   B  1 1045 ? -2.337  56.533  77.479  1.00 18.98 ? 1043 SER   B N     1 
ATOM   16238 C  CA    . SER   B  1 1045 ? -2.357  57.050  78.836  1.00 17.59 ? 1043 SER   B CA    1 
ATOM   16239 C  C     . SER   B  1 1045 ? -3.157  58.334  78.841  1.00 17.34 ? 1043 SER   B C     1 
ATOM   16240 O  O     . SER   B  1 1045 ? -3.030  59.138  77.922  1.00 18.31 ? 1043 SER   B O     1 
ATOM   16241 C  CB    . SER   B  1 1045 ? -0.941  57.328  79.352  1.00 18.83 ? 1043 SER   B CB    1 
ATOM   16242 O  OG    . SER   B  1 1045 ? -0.989  57.947  80.640  1.00 19.92 ? 1043 SER   B OG    1 
ATOM   16243 N  N     . VAL   B  1 1046 ? -3.964  58.532  79.887  1.00 17.33 ? 1044 VAL   B N     1 
ATOM   16244 C  CA    . VAL   B  1 1046 ? -4.692  59.783  80.018  1.00 19.97 ? 1044 VAL   B CA    1 
ATOM   16245 C  C     . VAL   B  1 1046 ? -3.859  60.846  80.705  1.00 19.96 ? 1044 VAL   B C     1 
ATOM   16246 O  O     . VAL   B  1 1046 ? -4.317  61.990  80.833  1.00 20.26 ? 1044 VAL   B O     1 
ATOM   16247 C  CB    . VAL   B  1 1046 ? -6.030  59.564  80.756  1.00 19.57 ? 1044 VAL   B CB    1 
ATOM   16248 C  CG1   . VAL   B  1 1046 ? -6.875  58.558  79.988  1.00 21.45 ? 1044 VAL   B CG1   1 
ATOM   16249 C  CG2   . VAL   B  1 1046 ? -5.788  59.078  82.165  1.00 18.85 ? 1044 VAL   B CG2   1 
ATOM   16250 N  N     . HIS   B  1 1047 ? -2.650  60.507  81.142  1.00 19.38 ? 1045 HIS   B N     1 
ATOM   16251 C  CA    . HIS   B  1 1047 ? -1.780  61.462  81.812  1.00 19.87 ? 1045 HIS   B CA    1 
ATOM   16252 C  C     . HIS   B  1 1047 ? -1.085  62.329  80.772  1.00 20.68 ? 1045 HIS   B C     1 
ATOM   16253 O  O     . HIS   B  1 1047 ? -0.671  61.842  79.718  1.00 21.89 ? 1045 HIS   B O     1 
ATOM   16254 C  CB    . HIS   B  1 1047 ? -0.744  60.723  82.667  1.00 22.79 ? 1045 HIS   B CB    1 
ATOM   16255 C  CG    . HIS   B  1 1047 ? 0.416   61.570  83.102  1.00 27.38 ? 1045 HIS   B CG    1 
ATOM   16256 N  ND1   . HIS   B  1 1047 ? 0.315   62.522  84.100  1.00 26.98 ? 1045 HIS   B ND1   1 
ATOM   16257 C  CD2   . HIS   B  1 1047 ? 1.706   61.599  82.682  1.00 27.13 ? 1045 HIS   B CD2   1 
ATOM   16258 C  CE1   . HIS   B  1 1047 ? 1.494   63.102  84.271  1.00 27.74 ? 1045 HIS   B CE1   1 
ATOM   16259 N  NE2   . HIS   B  1 1047 ? 2.354   62.561  83.421  1.00 20.09 ? 1045 HIS   B NE2   1 
ATOM   16260 N  N     . THR   B  1 1048 ? -0.957  63.616  81.068  1.00 21.47 ? 1046 THR   B N     1 
ATOM   16261 C  CA    . THR   B  1 1048 ? -0.158  64.515  80.245  1.00 23.84 ? 1046 THR   B CA    1 
ATOM   16262 C  C     . THR   B  1 1048 ? 0.953   65.095  81.107  1.00 21.79 ? 1046 THR   B C     1 
ATOM   16263 O  O     . THR   B  1 1048 ? 0.688   65.644  82.183  1.00 23.09 ? 1046 THR   B O     1 
ATOM   16264 C  CB    . THR   B  1 1048 ? -1.008  65.636  79.648  1.00 23.82 ? 1046 THR   B CB    1 
ATOM   16265 O  OG1   . THR   B  1 1048 ? -2.148  65.070  78.999  1.00 24.73 ? 1046 THR   B OG1   1 
ATOM   16266 C  CG2   . THR   B  1 1048 ? -0.196  66.450  78.626  1.00 24.86 ? 1046 THR   B CG2   1 
ATOM   16267 N  N     . ASP   B  1 1049 ? 2.186   64.971  80.638  1.00 19.53 ? 1047 ASP   B N     1 
ATOM   16268 C  CA    . ASP   B  1 1049 ? 3.305   65.472  81.409  1.00 19.00 ? 1047 ASP   B CA    1 
ATOM   16269 C  C     . ASP   B  1 1049 ? 3.142   66.974  81.623  1.00 18.05 ? 1047 ASP   B C     1 
ATOM   16270 O  O     . ASP   B  1 1049 ? 2.886   67.711  80.662  1.00 20.39 ? 1047 ASP   B O     1 
ATOM   16271 C  CB    . ASP   B  1 1049 ? 4.624   65.160  80.711  1.00 20.05 ? 1047 ASP   B CB    1 
ATOM   16272 C  CG    . ASP   B  1 1049 ? 5.809   65.630  81.514  1.00 18.79 ? 1047 ASP   B CG    1 
ATOM   16273 O  OD1   . ASP   B  1 1049 ? 6.151   66.828  81.413  1.00 20.68 ? 1047 ASP   B OD1   1 
ATOM   16274 O  OD2   . ASP   B  1 1049 ? 6.343   64.817  82.283  1.00 20.72 ? 1047 ASP   B OD2   1 
ATOM   16275 N  N     . PRO   B  1 1050 ? 3.220   67.459  82.862  1.00 19.31 ? 1048 PRO   B N     1 
ATOM   16276 C  CA    . PRO   B  1 1050 ? 2.945   68.883  83.090  1.00 23.24 ? 1048 PRO   B CA    1 
ATOM   16277 C  C     . PRO   B  1 1050 ? 4.049   69.784  82.566  1.00 21.49 ? 1048 PRO   B C     1 
ATOM   16278 O  O     . PRO   B  1 1050 ? 3.783   70.940  82.215  1.00 23.58 ? 1048 PRO   B O     1 
ATOM   16279 C  CB    . PRO   B  1 1050 ? 2.808   68.967  84.616  1.00 26.32 ? 1048 PRO   B CB    1 
ATOM   16280 C  CG    . PRO   B  1 1050 ? 3.660   67.862  85.115  1.00 23.05 ? 1048 PRO   B CG    1 
ATOM   16281 C  CD    . PRO   B  1 1050 ? 3.464   66.739  84.121  1.00 20.92 ? 1048 PRO   B CD    1 
ATOM   16282 N  N     . VAL   B  1 1051 ? 5.284   69.291  82.510  1.00 23.76 ? 1049 VAL   B N     1 
ATOM   16283 C  CA    . VAL   B  1 1051 ? 6.365   70.100  81.960  1.00 23.13 ? 1049 VAL   B CA    1 
ATOM   16284 C  C     . VAL   B  1 1051 ? 6.221   70.216  80.450  1.00 20.13 ? 1049 VAL   B C     1 
ATOM   16285 O  O     . VAL   B  1 1051 ? 6.448   71.284  79.869  1.00 23.01 ? 1049 VAL   B O     1 
ATOM   16286 C  CB    . VAL   B  1 1051 ? 7.726   69.515  82.369  1.00 21.29 ? 1049 VAL   B CB    1 
ATOM   16287 C  CG1   . VAL   B  1 1051 ? 8.846   70.354  81.767  1.00 23.80 ? 1049 VAL   B CG1   1 
ATOM   16288 C  CG2   . VAL   B  1 1051 ? 7.842   69.477  83.885  1.00 23.39 ? 1049 VAL   B CG2   1 
ATOM   16289 N  N     . LEU   B  1 1052 ? 5.815   69.131  79.792  1.00 20.64 ? 1050 LEU   B N     1 
ATOM   16290 C  CA    . LEU   B  1 1052 ? 5.419   69.228  78.390  1.00 19.88 ? 1050 LEU   B CA    1 
ATOM   16291 C  C     . LEU   B  1 1052 ? 4.391   70.334  78.198  1.00 23.47 ? 1050 LEU   B C     1 
ATOM   16292 O  O     . LEU   B  1 1052 ? 4.511   71.162  77.288  1.00 21.02 ? 1050 LEU   B O     1 
ATOM   16293 C  CB    . LEU   B  1 1052 ? 4.871   67.880  77.899  1.00 16.92 ? 1050 LEU   B CB    1 
ATOM   16294 C  CG    . LEU   B  1 1052 ? 4.312   67.716  76.462  1.00 18.40 ? 1050 LEU   B CG    1 
ATOM   16295 C  CD1   . LEU   B  1 1052 ? 2.908   68.295  76.293  1.00 21.93 ? 1050 LEU   B CD1   1 
ATOM   16296 C  CD2   . LEU   B  1 1052 ? 5.274   68.311  75.409  1.00 20.74 ? 1050 LEU   B CD2   1 
ATOM   16297 N  N     . LEU   B  1 1053 ? 3.359   70.357  79.044  1.00 21.20 ? 1051 LEU   B N     1 
ATOM   16298 C  CA    . LEU   B  1 1053 ? 2.334   71.386  78.911  1.00 24.15 ? 1051 LEU   B CA    1 
ATOM   16299 C  C     . LEU   B  1 1053 ? 2.936   72.779  79.078  1.00 21.23 ? 1051 LEU   B C     1 
ATOM   16300 O  O     . LEU   B  1 1053 ? 2.638   73.693  78.304  1.00 25.72 ? 1051 LEU   B O     1 
ATOM   16301 C  CB    . LEU   B  1 1053 ? 1.214   71.144  79.929  1.00 24.90 ? 1051 LEU   B CB    1 
ATOM   16302 C  CG    . LEU   B  1 1053 ? 0.269   69.968  79.615  1.00 23.55 ? 1051 LEU   B CG    1 
ATOM   16303 C  CD1   . LEU   B  1 1053 ? -0.621  69.678  80.812  1.00 27.67 ? 1051 LEU   B CD1   1 
ATOM   16304 C  CD2   . LEU   B  1 1053 ? -0.577  70.249  78.395  1.00 26.66 ? 1051 LEU   B CD2   1 
ATOM   16305 N  N     . ASP   B  1 1054 ? 3.783   72.956  80.094  1.00 24.87 ? 1052 ASP   B N     1 
ATOM   16306 C  CA    . ASP   B  1 1054 ? 4.447   74.241  80.297  1.00 29.14 ? 1052 ASP   B CA    1 
ATOM   16307 C  C     . ASP   B  1 1054 ? 5.270   74.630  79.076  1.00 25.98 ? 1052 ASP   B C     1 
ATOM   16308 O  O     . ASP   B  1 1054 ? 5.257   75.793  78.648  1.00 27.19 ? 1052 ASP   B O     1 
ATOM   16309 C  CB    . ASP   B  1 1054 ? 5.330   74.178  81.541  1.00 25.71 ? 1052 ASP   B CB    1 
ATOM   16310 C  CG    . ASP   B  1 1054 ? 4.524   74.194  82.825  1.00 31.03 ? 1052 ASP   B CG    1 
ATOM   16311 O  OD1   . ASP   B  1 1054 ? 3.311   74.459  82.747  1.00 29.29 ? 1052 ASP   B OD1   1 
ATOM   16312 O  OD2   . ASP   B  1 1054 ? 5.093   73.939  83.906  1.00 33.14 ? 1052 ASP   B OD2   1 
ATOM   16313 N  N     . PHE   B  1 1055 ? 5.975   73.660  78.495  1.00 25.54 ? 1053 PHE   B N     1 
ATOM   16314 C  CA    . PHE   B  1 1055 ? 6.737   73.905  77.275  1.00 23.79 ? 1053 PHE   B CA    1 
ATOM   16315 C  C     . PHE   B  1 1055 ? 5.831   74.327  76.127  1.00 27.33 ? 1053 PHE   B C     1 
ATOM   16316 O  O     . PHE   B  1 1055 ? 6.149   75.267  75.384  1.00 23.45 ? 1053 PHE   B O     1 
ATOM   16317 C  CB    . PHE   B  1 1055 ? 7.522   72.650  76.908  1.00 23.28 ? 1053 PHE   B CB    1 
ATOM   16318 C  CG    . PHE   B  1 1055 ? 8.396   72.811  75.706  1.00 20.57 ? 1053 PHE   B CG    1 
ATOM   16319 C  CD1   . PHE   B  1 1055 ? 9.324   73.841  75.639  1.00 25.83 ? 1053 PHE   B CD1   1 
ATOM   16320 C  CD2   . PHE   B  1 1055 ? 8.316   71.913  74.649  1.00 23.88 ? 1053 PHE   B CD2   1 
ATOM   16321 C  CE1   . PHE   B  1 1055 ? 10.138  73.992  74.519  1.00 25.20 ? 1053 PHE   B CE1   1 
ATOM   16322 C  CE2   . PHE   B  1 1055 ? 9.134   72.054  73.534  1.00 22.32 ? 1053 PHE   B CE2   1 
ATOM   16323 C  CZ    . PHE   B  1 1055 ? 10.046  73.095  73.474  1.00 22.69 ? 1053 PHE   B CZ    1 
ATOM   16324 N  N     . ALA   B  1 1056 ? 4.688   73.655  75.966  1.00 23.91 ? 1054 ALA   B N     1 
ATOM   16325 C  CA    . ALA   B  1 1056 ? 3.792   74.006  74.866  1.00 26.56 ? 1054 ALA   B CA    1 
ATOM   16326 C  C     . ALA   B  1 1056 ? 3.269   75.430  75.011  1.00 24.55 ? 1054 ALA   B C     1 
ATOM   16327 O  O     . ALA   B  1 1056 ? 3.138   76.152  74.015  1.00 28.55 ? 1054 ALA   B O     1 
ATOM   16328 C  CB    . ALA   B  1 1056 ? 2.626   73.019  74.783  1.00 25.40 ? 1054 ALA   B CB    1 
ATOM   16329 N  N     . LYS   B  1 1057 ? 2.946   75.844  76.239  1.00 29.03 ? 1055 LYS   B N     1 
ATOM   16330 C  CA    . LYS   B  1 1057 ? 2.480   77.212  76.460  1.00 31.94 ? 1055 LYS   B CA    1 
ATOM   16331 C  C     . LYS   B  1 1057 ? 3.577   78.215  76.143  1.00 33.44 ? 1055 LYS   B C     1 
ATOM   16332 O  O     . LYS   B  1 1057 ? 3.321   79.265  75.539  1.00 32.53 ? 1055 LYS   B O     1 
ATOM   16333 C  CB    . LYS   B  1 1057 ? 2.018   77.391  77.907  1.00 33.26 ? 1055 LYS   B CB    1 
ATOM   16334 C  CG    . LYS   B  1 1057 ? 0.595   76.964  78.178  1.00 37.07 ? 1055 LYS   B CG    1 
ATOM   16335 C  CD    . LYS   B  1 1057 ? 0.210   77.229  79.628  1.00 35.07 ? 1055 LYS   B CD    1 
ATOM   16336 C  CE    . LYS   B  1 1057 ? 1.213   76.594  80.570  1.00 32.31 ? 1055 LYS   B CE    1 
ATOM   16337 N  NZ    . LYS   B  1 1057 ? 0.667   76.458  81.944  1.00 35.12 ? 1055 LYS   B NZ    1 
ATOM   16338 N  N     . TRP   B  1 1058 ? 4.805   77.908  76.568  1.00 31.20 ? 1056 TRP   B N     1 
ATOM   16339 C  CA    . TRP   B  1 1058 ? 5.957   78.741  76.236  1.00 31.03 ? 1056 TRP   B CA    1 
ATOM   16340 C  C     . TRP   B  1 1058 ? 6.121   78.879  74.727  1.00 31.54 ? 1056 TRP   B C     1 
ATOM   16341 O  O     . TRP   B  1 1058 ? 6.362   79.980  74.220  1.00 36.46 ? 1056 TRP   B O     1 
ATOM   16342 C  CB    . TRP   B  1 1058 ? 7.210   78.140  76.879  1.00 28.58 ? 1056 TRP   B CB    1 
ATOM   16343 C  CG    . TRP   B  1 1058 ? 8.477   78.864  76.569  1.00 36.17 ? 1056 TRP   B CG    1 
ATOM   16344 C  CD1   . TRP   B  1 1058 ? 8.952   79.984  77.185  1.00 37.58 ? 1056 TRP   B CD1   1 
ATOM   16345 C  CD2   . TRP   B  1 1058 ? 9.440   78.516  75.568  1.00 32.28 ? 1056 TRP   B CD2   1 
ATOM   16346 N  NE1   . TRP   B  1 1058 ? 10.153  80.354  76.631  1.00 35.96 ? 1056 TRP   B NE1   1 
ATOM   16347 C  CE2   . TRP   B  1 1058 ? 10.476  79.469  75.637  1.00 36.79 ? 1056 TRP   B CE2   1 
ATOM   16348 C  CE3   . TRP   B  1 1058 ? 9.533   77.487  74.626  1.00 32.24 ? 1056 TRP   B CE3   1 
ATOM   16349 C  CZ2   . TRP   B  1 1058 ? 11.589  79.426  74.800  1.00 35.02 ? 1056 TRP   B CZ2   1 
ATOM   16350 C  CZ3   . TRP   B  1 1058 ? 10.643  77.449  73.788  1.00 38.14 ? 1056 TRP   B CZ3   1 
ATOM   16351 C  CH2   . TRP   B  1 1058 ? 11.656  78.411  73.886  1.00 31.16 ? 1056 TRP   B CH2   1 
ATOM   16352 N  N     . LEU   B  1 1059 ? 5.982   77.774  73.990  1.00 28.31 ? 1057 LEU   B N     1 
ATOM   16353 C  CA    . LEU   B  1 1059 ? 6.049   77.838  72.533  1.00 29.66 ? 1057 LEU   B CA    1 
ATOM   16354 C  C     . LEU   B  1 1059 ? 4.956   78.728  71.964  1.00 37.39 ? 1057 LEU   B C     1 
ATOM   16355 O  O     . LEU   B  1 1059 ? 5.191   79.484  71.014  1.00 37.21 ? 1057 LEU   B O     1 
ATOM   16356 C  CB    . LEU   B  1 1059 ? 5.930   76.440  71.937  1.00 28.41 ? 1057 LEU   B CB    1 
ATOM   16357 C  CG    . LEU   B  1 1059 ? 7.107   75.502  72.161  1.00 28.17 ? 1057 LEU   B CG    1 
ATOM   16358 C  CD1   . LEU   B  1 1059 ? 6.765   74.150  71.575  1.00 28.12 ? 1057 LEU   B CD1   1 
ATOM   16359 C  CD2   . LEU   B  1 1059 ? 8.342   76.085  71.499  1.00 28.60 ? 1057 LEU   B CD2   1 
ATOM   16360 N  N     . ASP   B  1 1060 ? 3.746   78.636  72.517  1.00 35.68 ? 1058 ASP   B N     1 
ATOM   16361 C  CA    . ASP   B  1 1060 ? 2.654   79.457  72.004  1.00 37.53 ? 1058 ASP   B CA    1 
ATOM   16362 C  C     . ASP   B  1 1060 ? 2.889   80.934  72.294  1.00 38.03 ? 1058 ASP   B C     1 
ATOM   16363 O  O     . ASP   B  1 1060 ? 2.671   81.783  71.421  1.00 43.04 ? 1058 ASP   B O     1 
ATOM   16364 C  CB    . ASP   B  1 1060 ? 1.323   78.994  72.592  1.00 36.52 ? 1058 ASP   B CB    1 
ATOM   16365 C  CG    . ASP   B  1 1060 ? 0.582   78.063  71.666  1.00 37.30 ? 1058 ASP   B CG    1 
ATOM   16366 O  OD1   . ASP   B  1 1060 ? 0.646   78.267  70.432  1.00 47.19 ? 1058 ASP   B OD1   1 
ATOM   16367 O  OD2   . ASP   B  1 1060 ? -0.058  77.122  72.169  1.00 40.66 ? 1058 ASP   B OD2   1 
ATOM   16368 N  N     . GLY   B  1 1061 ? 3.334   81.261  73.509  1.00 36.86 ? 1059 GLY   B N     1 
ATOM   16369 C  CA    . GLY   B  1 1061 ? 3.671   82.639  73.818  1.00 42.54 ? 1059 GLY   B CA    1 
ATOM   16370 C  C     . GLY   B  1 1061 ? 4.791   83.176  72.959  1.00 45.83 ? 1059 GLY   B C     1 
ATOM   16371 O  O     . GLY   B  1 1061 ? 4.950   84.393  72.840  1.00 50.86 ? 1059 GLY   B O     1 
ATOM   16372 N  N     . LYS   B  1 1062 ? 5.558   82.285  72.348  1.00 42.79 ? 1060 LYS   B N     1 
ATOM   16373 C  CA    . LYS   B  1 1062 ? 6.662   82.606  71.465  1.00 43.78 ? 1060 LYS   B CA    1 
ATOM   16374 C  C     . LYS   B  1 1062 ? 6.238   82.688  70.004  1.00 47.10 ? 1060 LYS   B C     1 
ATOM   16375 O  O     . LYS   B  1 1062 ? 7.036   83.109  69.160  1.00 51.21 ? 1060 LYS   B O     1 
ATOM   16376 C  CB    . LYS   B  1 1062 ? 7.746   81.540  71.648  1.00 42.14 ? 1060 LYS   B CB    1 
ATOM   16377 C  CG    . LYS   B  1 1062 ? 9.096   81.858  71.094  1.00 51.49 ? 1060 LYS   B CG    1 
ATOM   16378 C  CD    . LYS   B  1 1062 ? 10.076  80.780  71.503  1.00 43.44 ? 1060 LYS   B CD    1 
ATOM   16379 C  CE    . LYS   B  1 1062 ? 11.481  81.170  71.110  1.00 44.02 ? 1060 LYS   B CE    1 
ATOM   16380 N  NZ    . LYS   B  1 1062 ? 11.638  81.138  69.632  1.00 47.10 ? 1060 LYS   B NZ    1 
ATOM   16381 N  N     . GLY   B  1 1063 ? 5.004   82.305  69.687  1.00 44.98 ? 1061 GLY   B N     1 
ATOM   16382 C  CA    . GLY   B  1 1063 ? 4.531   82.317  68.323  1.00 40.00 ? 1061 GLY   B CA    1 
ATOM   16383 C  C     . GLY   B  1 1063 ? 4.907   81.102  67.512  1.00 46.50 ? 1061 GLY   B C     1 
ATOM   16384 O  O     . GLY   B  1 1063 ? 4.604   81.062  66.313  1.00 46.79 ? 1061 GLY   B O     1 
ATOM   16385 N  N     . ALA   B  1 1064 ? 5.556   80.109  68.123  1.00 44.36 ? 1062 ALA   B N     1 
ATOM   16386 C  CA    . ALA   B  1 1064 ? 5.943   78.885  67.423  1.00 39.99 ? 1062 ALA   B CA    1 
ATOM   16387 C  C     . ALA   B  1 1064 ? 4.750   77.930  67.418  1.00 43.23 ? 1062 ALA   B C     1 
ATOM   16388 O  O     . ALA   B  1 1064 ? 4.727   76.896  68.092  1.00 36.60 ? 1062 ALA   B O     1 
ATOM   16389 C  CB    . ALA   B  1 1064 ? 7.168   78.260  68.076  1.00 35.47 ? 1062 ALA   B CB    1 
ATOM   16390 N  N     . ARG   B  1 1065 ? 3.741   78.306  66.622  1.00 45.94 ? 1063 ARG   B N     1 
ATOM   16391 C  CA    . ARG   B  1 1065 ? 2.434   77.655  66.704  1.00 43.42 ? 1063 ARG   B CA    1 
ATOM   16392 C  C     . ARG   B  1 1065 ? 2.482   76.228  66.177  1.00 40.62 ? 1063 ARG   B C     1 
ATOM   16393 O  O     . ARG   B  1 1065 ? 1.775   75.351  66.687  1.00 41.48 ? 1063 ARG   B O     1 
ATOM   16394 C  CB    . ARG   B  1 1065 ? 1.387   78.472  65.941  1.00 44.51 ? 1063 ARG   B CB    1 
ATOM   16395 N  N     . ALA   B  1 1066 ? 3.294   75.974  65.152  1.00 36.24 ? 1064 ALA   B N     1 
ATOM   16396 C  CA    . ALA   B  1 1066 ? 3.446   74.605  64.673  1.00 35.58 ? 1064 ALA   B CA    1 
ATOM   16397 C  C     . ALA   B  1 1066 ? 4.070   73.720  65.746  1.00 37.53 ? 1064 ALA   B C     1 
ATOM   16398 O  O     . ALA   B  1 1066 ? 3.610   72.596  65.981  1.00 33.43 ? 1064 ALA   B O     1 
ATOM   16399 C  CB    . ALA   B  1 1066 ? 4.293   74.574  63.402  1.00 38.28 ? 1064 ALA   B CB    1 
ATOM   16400 N  N     . GLU   B  1 1067 ? 5.116   74.213  66.411  1.00 32.52 ? 1065 GLU   B N     1 
ATOM   16401 C  CA    . GLU   B  1 1067 ? 5.776   73.403  67.427  1.00 33.95 ? 1065 GLU   B CA    1 
ATOM   16402 C  C     . GLU   B  1 1067 ? 4.898   73.243  68.661  1.00 30.68 ? 1065 GLU   B C     1 
ATOM   16403 O  O     . GLU   B  1 1067 ? 4.849   72.157  69.247  1.00 30.64 ? 1065 GLU   B O     1 
ATOM   16404 C  CB    . GLU   B  1 1067 ? 7.131   74.008  67.799  1.00 34.10 ? 1065 GLU   B CB    1 
ATOM   16405 C  CG    . GLU   B  1 1067 ? 8.206   73.831  66.727  1.00 27.84 ? 1065 GLU   B CG    1 
ATOM   16406 C  CD    . GLU   B  1 1067 ? 8.062   74.830  65.604  1.00 36.72 ? 1065 GLU   B CD    1 
ATOM   16407 O  OE1   . GLU   B  1 1067 ? 7.184   75.715  65.711  1.00 34.95 ? 1065 GLU   B OE1   1 
ATOM   16408 O  OE2   . GLU   B  1 1067 ? 8.817   74.730  64.612  1.00 35.65 ? 1065 GLU   B OE2   1 
ATOM   16409 N  N     . ALA   B  1 1068 ? 4.203   74.311  69.073  1.00 31.31 ? 1066 ALA   B N     1 
ATOM   16410 C  CA    . ALA   B  1 1068 ? 3.273   74.188  70.192  1.00 32.56 ? 1066 ALA   B CA    1 
ATOM   16411 C  C     . ALA   B  1 1068 ? 2.220   73.129  69.903  1.00 31.93 ? 1066 ALA   B C     1 
ATOM   16412 O  O     . ALA   B  1 1068 ? 1.890   72.312  70.773  1.00 29.89 ? 1066 ALA   B O     1 
ATOM   16413 C  CB    . ALA   B  1 1068 ? 2.612   75.532  70.488  1.00 31.40 ? 1066 ALA   B CB    1 
ATOM   16414 N  N     . GLU   B  1 1069 ? 1.701   73.123  68.674  1.00 32.35 ? 1067 GLU   B N     1 
ATOM   16415 C  CA    . GLU   B  1 1069 ? 0.776   72.085  68.238  1.00 34.87 ? 1067 GLU   B CA    1 
ATOM   16416 C  C     . GLU   B  1 1069 ? 1.428   70.711  68.304  1.00 33.55 ? 1067 GLU   B C     1 
ATOM   16417 O  O     . GLU   B  1 1069 ? 0.851   69.759  68.845  1.00 30.24 ? 1067 GLU   B O     1 
ATOM   16418 C  CB    . GLU   B  1 1069 ? 0.298   72.395  66.817  1.00 36.41 ? 1067 GLU   B CB    1 
ATOM   16419 C  CG    . GLU   B  1 1069 ? -0.487  71.282  66.150  1.00 37.33 ? 1067 GLU   B CG    1 
ATOM   16420 C  CD    . GLU   B  1 1069 ? -1.901  71.163  66.684  1.00 49.34 ? 1067 GLU   B CD    1 
ATOM   16421 O  OE1   . GLU   B  1 1069 ? -2.282  71.975  67.558  1.00 51.62 ? 1067 GLU   B OE1   1 
ATOM   16422 O  OE2   . GLU   B  1 1069 ? -2.632  70.253  66.227  1.00 56.65 ? 1067 GLU   B OE2   1 
ATOM   16423 N  N     . ALA   B  1 1070 ? 2.642   70.589  67.761  1.00 29.43 ? 1068 ALA   B N     1 
ATOM   16424 C  CA    . ALA   B  1 1070 ? 3.355   69.320  67.822  1.00 32.12 ? 1068 ALA   B CA    1 
ATOM   16425 C  C     . ALA   B  1 1070 ? 3.609   68.901  69.264  1.00 25.09 ? 1068 ALA   B C     1 
ATOM   16426 O  O     . ALA   B  1 1070 ? 3.518   67.714  69.594  1.00 25.39 ? 1068 ALA   B O     1 
ATOM   16427 C  CB    . ALA   B  1 1070 ? 4.673   69.420  67.053  1.00 34.55 ? 1068 ALA   B CB    1 
ATOM   16428 N  N     . ALA   B  1 1071 ? 3.917   69.861  70.138  1.00 25.68 ? 1069 ALA   B N     1 
ATOM   16429 C  CA    . ALA   B  1 1071 ? 4.176   69.519  71.532  1.00 24.62 ? 1069 ALA   B CA    1 
ATOM   16430 C  C     . ALA   B  1 1071 ? 2.918   68.962  72.191  1.00 23.97 ? 1069 ALA   B C     1 
ATOM   16431 O  O     . ALA   B  1 1071 ? 2.963   67.911  72.843  1.00 23.16 ? 1069 ALA   B O     1 
ATOM   16432 C  CB    . ALA   B  1 1071 ? 4.697   70.740  72.290  1.00 23.19 ? 1069 ALA   B CB    1 
ATOM   16433 N  N     . ARG   B  1 1072 ? 1.777   69.640  72.003  1.00 22.88 ? 1070 ARG   B N     1 
ATOM   16434 C  CA    A ARG   B  1 1072 ? 0.515   69.157  72.564  0.53 25.60 ? 1070 ARG   B CA    1 
ATOM   16435 C  CA    B ARG   B  1 1072 ? 0.530   69.147  72.581  0.47 25.60 ? 1070 ARG   B CA    1 
ATOM   16436 C  C     . ARG   B  1 1072 ? 0.183   67.762  72.053  1.00 24.13 ? 1070 ARG   B C     1 
ATOM   16437 O  O     . ARG   B  1 1072 ? -0.268  66.900  72.818  1.00 24.37 ? 1070 ARG   B O     1 
ATOM   16438 C  CB    A ARG   B  1 1072 ? -0.629  70.121  72.223  0.53 28.26 ? 1070 ARG   B CB    1 
ATOM   16439 C  CB    B ARG   B  1 1072 ? -0.608  70.132  72.308  0.47 28.27 ? 1070 ARG   B CB    1 
ATOM   16440 C  CG    A ARG   B  1 1072 ? -0.518  71.504  72.856  0.53 28.91 ? 1070 ARG   B CG    1 
ATOM   16441 C  CG    B ARG   B  1 1072 ? -0.366  71.471  72.965  0.47 28.87 ? 1070 ARG   B CG    1 
ATOM   16442 C  CD    A ARG   B  1 1072 ? -1.764  72.349  72.584  0.53 28.43 ? 1070 ARG   B CD    1 
ATOM   16443 C  CD    B ARG   B  1 1072 ? -1.614  72.318  73.098  0.47 28.83 ? 1070 ARG   B CD    1 
ATOM   16444 N  NE    A ARG   B  1 1072 ? -2.000  72.554  71.159  0.53 30.68 ? 1070 ARG   B NE    1 
ATOM   16445 N  NE    B ARG   B  1 1072 ? -1.343  73.408  74.024  0.47 28.35 ? 1070 ARG   B NE    1 
ATOM   16446 C  CZ    A ARG   B  1 1072 ? -1.682  73.659  70.498  0.53 31.41 ? 1070 ARG   B CZ    1 
ATOM   16447 C  CZ    B ARG   B  1 1072 ? -0.889  74.597  73.662  0.47 28.65 ? 1070 ARG   B CZ    1 
ATOM   16448 N  NH1   A ARG   B  1 1072 ? -1.158  74.706  71.112  0.53 28.03 ? 1070 ARG   B NH1   1 
ATOM   16449 N  NH1   B ARG   B  1 1072 ? -0.760  74.928  72.389  0.47 30.73 ? 1070 ARG   B NH1   1 
ATOM   16450 N  NH2   A ARG   B  1 1072 ? -1.897  73.715  69.187  0.53 33.80 ? 1070 ARG   B NH2   1 
ATOM   16451 N  NH2   B ARG   B  1 1072 ? -0.548  75.474  74.602  0.47 32.36 ? 1070 ARG   B NH2   1 
ATOM   16452 N  N     . ASN   B  1 1073 ? 0.389   67.529  70.756  1.00 22.93 ? 1071 ASN   B N     1 
ATOM   16453 C  CA    . ASN   B  1 1073 ? 0.108   66.219  70.175  1.00 24.84 ? 1071 ASN   B CA    1 
ATOM   16454 C  C     . ASN   B  1 1073 ? 1.033   65.153  70.742  1.00 25.98 ? 1071 ASN   B C     1 
ATOM   16455 O  O     . ASN   B  1 1073 ? 0.621   64.006  70.938  1.00 23.72 ? 1071 ASN   B O     1 
ATOM   16456 C  CB    . ASN   B  1 1073 ? 0.226   66.282  68.657  1.00 25.48 ? 1071 ASN   B CB    1 
ATOM   16457 C  CG    . ASN   B  1 1073 ? -0.942  67.014  68.016  1.00 33.63 ? 1071 ASN   B CG    1 
ATOM   16458 O  OD1   . ASN   B  1 1073 ? -1.947  67.283  68.671  1.00 39.08 ? 1071 ASN   B OD1   1 
ATOM   16459 N  ND2   . ASN   B  1 1073 ? -0.815  67.337  66.734  1.00 33.60 ? 1071 ASN   B ND2   1 
ATOM   16460 N  N     . ALA   B  1 1074 ? 2.290   65.506  71.009  1.00 24.60 ? 1072 ALA   B N     1 
ATOM   16461 C  CA    . ALA   B  1 1074 ? 3.178   64.560  71.667  1.00 20.92 ? 1072 ALA   B CA    1 
ATOM   16462 C  C     . ALA   B  1 1074 ? 2.688   64.244  73.078  1.00 18.36 ? 1072 ALA   B C     1 
ATOM   16463 O  O     . ALA   B  1 1074 ? 2.715   63.084  73.509  1.00 20.58 ? 1072 ALA   B O     1 
ATOM   16464 C  CB    . ALA   B  1 1074 ? 4.597   65.123  71.700  1.00 20.89 ? 1072 ALA   B CB    1 
ATOM   16465 N  N     . GLY   B  1 1075 ? 2.272   65.274  73.821  1.00 19.87 ? 1073 GLY   B N     1 
ATOM   16466 C  CA    . GLY   B  1 1075 ? 1.766   65.050  75.166  1.00 23.45 ? 1073 GLY   B CA    1 
ATOM   16467 C  C     . GLY   B  1 1075 ? 0.582   64.103  75.183  1.00 26.86 ? 1073 GLY   B C     1 
ATOM   16468 O  O     . GLY   B  1 1075 ? 0.445   63.274  76.091  1.00 26.00 ? 1073 GLY   B O     1 
ATOM   16469 N  N     . SER   B  1 1076 ? -0.272  64.187  74.161  1.00 23.34 ? 1074 SER   B N     1 
ATOM   16470 C  CA    . SER   B  1 1076 ? -1.418  63.294  74.097  1.00 21.22 ? 1074 SER   B CA    1 
ATOM   16471 C  C     . SER   B  1 1076 ? -1.018  61.892  73.659  1.00 24.70 ? 1074 SER   B C     1 
ATOM   16472 O  O     . SER   B  1 1076 ? -1.511  60.906  74.214  1.00 26.34 ? 1074 SER   B O     1 
ATOM   16473 C  CB    . SER   B  1 1076 ? -2.482  63.879  73.164  1.00 27.83 ? 1074 SER   B CB    1 
ATOM   16474 O  OG    . SER   B  1 1076 ? -3.100  65.000  73.779  1.00 28.21 ? 1074 SER   B OG    1 
ATOM   16475 N  N     . SER   B  1 1077 ? -0.124  61.767  72.683  1.00 23.20 ? 1075 SER   B N     1 
ATOM   16476 C  CA    . SER   B  1 1077 ? 0.150   60.432  72.165  1.00 26.72 ? 1075 SER   B CA    1 
ATOM   16477 C  C     . SER   B  1 1077 ? 1.118   59.659  73.052  1.00 22.45 ? 1075 SER   B C     1 
ATOM   16478 O  O     . SER   B  1 1077 ? 1.183   58.428  72.954  1.00 22.83 ? 1075 SER   B O     1 
ATOM   16479 C  CB    . SER   B  1 1077 ? 0.674   60.521  70.733  1.00 29.61 ? 1075 SER   B CB    1 
ATOM   16480 O  OG    . SER   B  1 1077 ? 1.737   61.435  70.658  1.00 39.00 ? 1075 SER   B OG    1 
ATOM   16481 N  N     . SER   B  1 1078 ? 1.837   60.349  73.930  1.00 18.83 ? 1076 SER   B N     1 
ATOM   16482 C  CA    . SER   B  1 1078 ? 2.682   59.675  74.909  1.00 19.16 ? 1076 SER   B CA    1 
ATOM   16483 C  C     . SER   B  1 1078 ? 1.864   58.686  75.723  1.00 19.82 ? 1076 SER   B C     1 
ATOM   16484 O  O     . SER   B  1 1078 ? 0.728   58.968  76.110  1.00 19.58 ? 1076 SER   B O     1 
ATOM   16485 C  CB    . SER   B  1 1078 ? 3.322   60.695  75.850  1.00 17.15 ? 1076 SER   B CB    1 
ATOM   16486 O  OG    . SER   B  1 1078 ? 3.994   60.026  76.919  1.00 18.20 ? 1076 SER   B OG    1 
ATOM   16487 N  N     . ALA   B  1 1079 ? 2.452   57.527  75.998  1.00 16.42 ? 1077 ALA   B N     1 
ATOM   16488 C  CA    . ALA   B  1 1079 ? 1.826   56.548  76.869  1.00 19.43 ? 1077 ALA   B CA    1 
ATOM   16489 C  C     . ALA   B  1 1079 ? 2.455   56.551  78.257  1.00 18.47 ? 1077 ALA   B C     1 
ATOM   16490 O  O     . ALA   B  1 1079 ? 2.227   55.626  79.041  1.00 17.66 ? 1077 ALA   B O     1 
ATOM   16491 C  CB    . ALA   B  1 1079 ? 1.896   55.156  76.235  1.00 21.64 ? 1077 ALA   B CB    1 
ATOM   16492 N  N     . LEU   B  1 1080 ? 3.227   57.587  78.575  1.00 16.58 ? 1078 LEU   B N     1 
ATOM   16493 C  CA    . LEU   B  1 1080 ? 3.735   57.771  79.926  1.00 17.27 ? 1078 LEU   B CA    1 
ATOM   16494 C  C     . LEU   B  1 1080 ? 2.606   57.703  80.945  1.00 16.82 ? 1078 LEU   B C     1 
ATOM   16495 O  O     . LEU   B  1 1080 ? 1.583   58.382  80.810  1.00 17.38 ? 1078 LEU   B O     1 
ATOM   16496 C  CB    . LEU   B  1 1080 ? 4.439   59.121  80.029  1.00 17.62 ? 1078 LEU   B CB    1 
ATOM   16497 C  CG    . LEU   B  1 1080 ? 4.847   59.497  81.446  1.00 16.50 ? 1078 LEU   B CG    1 
ATOM   16498 C  CD1   . LEU   B  1 1080 ? 6.004   58.602  81.901  1.00 16.19 ? 1078 LEU   B CD1   1 
ATOM   16499 C  CD2   . LEU   B  1 1080 ? 5.231   60.975  81.501  1.00 19.93 ? 1078 LEU   B CD2   1 
ATOM   16500 N  N     . GLY   B  1 1081 ? 2.809   56.901  81.986  1.00 19.26 ? 1079 GLY   B N     1 
ATOM   16501 C  CA    . GLY   B  1 1081 ? 1.790   56.743  83.001  1.00 19.28 ? 1079 GLY   B CA    1 
ATOM   16502 C  C     . GLY   B  1 1081 ? 0.868   55.566  82.783  1.00 22.50 ? 1079 GLY   B C     1 
ATOM   16503 O  O     . GLY   B  1 1081 ? -0.014  55.322  83.626  1.00 18.51 ? 1079 GLY   B O     1 
ATOM   16504 N  N     . LEU   B  1 1082 ? 1.014   54.855  81.665  1.00 17.32 ? 1080 LEU   B N     1 
ATOM   16505 C  CA    A LEU   B  1 1082 ? 0.275   53.618  81.460  0.50 19.63 ? 1080 LEU   B CA    1 
ATOM   16506 C  CA    B LEU   B  1 1082 ? 0.272   53.619  81.461  0.50 19.63 ? 1080 LEU   B CA    1 
ATOM   16507 C  C     . LEU   B  1 1082 ? 0.467   52.698  82.658  1.00 19.94 ? 1080 LEU   B C     1 
ATOM   16508 O  O     . LEU   B  1 1082 ? 1.575   52.549  83.173  1.00 17.24 ? 1080 LEU   B O     1 
ATOM   16509 C  CB    A LEU   B  1 1082 ? 0.748   52.927  80.178  0.50 17.35 ? 1080 LEU   B CB    1 
ATOM   16510 C  CB    B LEU   B  1 1082 ? 0.739   52.935  80.171  0.50 17.22 ? 1080 LEU   B CB    1 
ATOM   16511 C  CG    A LEU   B  1 1082 ? 0.099   51.582  79.838  0.50 18.63 ? 1080 LEU   B CG    1 
ATOM   16512 C  CG    B LEU   B  1 1082 ? 0.146   51.581  79.763  0.50 18.64 ? 1080 LEU   B CG    1 
ATOM   16513 C  CD1   A LEU   B  1 1082 ? -1.395  51.757  79.753  0.50 17.94 ? 1080 LEU   B CD1   1 
ATOM   16514 C  CD1   B LEU   B  1 1082 ? 0.211   51.442  78.253  0.50 17.42 ? 1080 LEU   B CD1   1 
ATOM   16515 C  CD2   A LEU   B  1 1082 ? 0.632   51.042  78.522  0.50 17.75 ? 1080 LEU   B CD2   1 
ATOM   16516 C  CD2   B LEU   B  1 1082 ? 0.884   50.429  80.412  0.50 16.60 ? 1080 LEU   B CD2   1 
ATOM   16517 N  N     . ASP   B  1 1083 ? -0.621  52.075  83.098  1.00 17.16 ? 1081 ASP   B N     1 
ATOM   16518 C  CA    . ASP   B  1 1083 ? -0.573  51.273  84.320  1.00 20.81 ? 1081 ASP   B CA    1 
ATOM   16519 C  C     . ASP   B  1 1083 ? -1.609  50.163  84.168  1.00 22.14 ? 1081 ASP   B C     1 
ATOM   16520 O  O     . ASP   B  1 1083 ? -2.797  50.388  84.414  1.00 24.39 ? 1081 ASP   B O     1 
ATOM   16521 C  CB    . ASP   B  1 1083 ? -0.847  52.160  85.529  1.00 23.51 ? 1081 ASP   B CB    1 
ATOM   16522 C  CG    . ASP   B  1 1083 ? -0.788  51.418  86.852  1.00 33.38 ? 1081 ASP   B CG    1 
ATOM   16523 O  OD1   . ASP   B  1 1083 ? -0.191  50.322  86.926  1.00 33.28 ? 1081 ASP   B OD1   1 
ATOM   16524 O  OD2   . ASP   B  1 1083 ? -1.352  51.952  87.832  1.00 34.28 ? 1081 ASP   B OD2   1 
ATOM   16525 N  N     . LEU   B  1 1084 ? -1.156  48.982  83.754  1.00 21.07 ? 1082 LEU   B N     1 
ATOM   16526 C  CA    . LEU   B  1 1084 ? -2.037  47.897  83.347  1.00 21.35 ? 1082 LEU   B CA    1 
ATOM   16527 C  C     . LEU   B  1 1084 ? -1.813  46.678  84.223  1.00 22.09 ? 1082 LEU   B C     1 
ATOM   16528 O  O     . LEU   B  1 1084 ? -0.695  46.418  84.669  1.00 19.93 ? 1082 LEU   B O     1 
ATOM   16529 C  CB    . LEU   B  1 1084 ? -1.790  47.483  81.888  1.00 20.93 ? 1082 LEU   B CB    1 
ATOM   16530 C  CG    . LEU   B  1 1084 ? -2.109  48.505  80.816  1.00 26.06 ? 1082 LEU   B CG    1 
ATOM   16531 C  CD1   . LEU   B  1 1084 ? -1.782  47.937  79.447  1.00 26.14 ? 1082 LEU   B CD1   1 
ATOM   16532 C  CD2   . LEU   B  1 1084 ? -3.581  48.918  80.927  1.00 28.92 ? 1082 LEU   B CD2   1 
ATOM   16533 N  N     . GLU   B  1 1085 ? -2.871  45.904  84.445  1.00 18.78 ? 1083 GLU   B N     1 
ATOM   16534 C  CA    . GLU   B  1 1085 ? -2.689  44.573  85.001  1.00 19.57 ? 1083 GLU   B CA    1 
ATOM   16535 C  C     . GLU   B  1 1085 ? -2.773  43.557  83.868  1.00 21.18 ? 1083 GLU   B C     1 
ATOM   16536 O  O     . GLU   B  1 1085 ? -3.723  43.575  83.083  1.00 24.65 ? 1083 GLU   B O     1 
ATOM   16537 C  CB    . GLU   B  1 1085 ? -3.708  44.257  86.093  1.00 20.06 ? 1083 GLU   B CB    1 
ATOM   16538 C  CG    . GLU   B  1 1085 ? -3.519  42.839  86.599  1.00 24.84 ? 1083 GLU   B CG    1 
ATOM   16539 C  CD    . GLU   B  1 1085 ? -4.220  42.556  87.901  1.00 30.08 ? 1083 GLU   B CD    1 
ATOM   16540 O  OE1   . GLU   B  1 1085 ? -4.829  43.485  88.480  1.00 29.23 ? 1083 GLU   B OE1   1 
ATOM   16541 O  OE2   . GLU   B  1 1085 ? -4.145  41.391  88.351  1.00 29.37 ? 1083 GLU   B OE2   1 
ATOM   16542 N  N     . LEU   B  1 1086 ? -1.805  42.708  83.783  1.00 19.28 ? 1084 LEU   B N     1 
ATOM   16543 C  CA    . LEU   B  1 1086 ? -1.795  41.704  82.729  1.00 19.25 ? 1084 LEU   B CA    1 
ATOM   16544 C  C     . LEU   B  1 1086 ? -2.431  40.411  83.226  1.00 24.09 ? 1084 LEU   B C     1 
ATOM   16545 O  O     . LEU   B  1 1086 ? -2.304  40.065  84.404  1.00 22.74 ? 1084 LEU   B O     1 
ATOM   16546 C  CB    . LEU   B  1 1086 ? -0.367  41.423  82.268  1.00 18.34 ? 1084 LEU   B CB    1 
ATOM   16547 C  CG    . LEU   B  1 1086 ? 0.393   42.635  81.732  1.00 20.52 ? 1084 LEU   B CG    1 
ATOM   16548 C  CD1   . LEU   B  1 1086 ? 1.797   42.260  81.295  1.00 16.54 ? 1084 LEU   B CD1   1 
ATOM   16549 C  CD2   . LEU   B  1 1086 ? -0.377  43.257  80.569  1.00 20.04 ? 1084 LEU   B CD2   1 
ATOM   16550 N  N     . PRO   B  1 1087 ? -3.133  39.699  82.345  1.00 26.17 ? 1085 PRO   B N     1 
ATOM   16551 C  CA    . PRO   B  1 1087 ? -3.742  38.425  82.747  1.00 23.70 ? 1085 PRO   B CA    1 
ATOM   16552 C  C     . PRO   B  1 1087 ? -2.683  37.394  83.072  1.00 24.65 ? 1085 PRO   B C     1 
ATOM   16553 O  O     . PRO   B  1 1087 ? -1.655  37.290  82.397  1.00 27.60 ? 1085 PRO   B O     1 
ATOM   16554 C  CB    . PRO   B  1 1087 ? -4.559  38.010  81.515  1.00 26.67 ? 1085 PRO   B CB    1 
ATOM   16555 C  CG    . PRO   B  1 1087 ? -4.818  39.283  80.776  1.00 27.69 ? 1085 PRO   B CG    1 
ATOM   16556 C  CD    . PRO   B  1 1087 ? -3.597  40.140  81.014  1.00 29.71 ? 1085 PRO   B CD    1 
ATOM   16557 N  N     . GLY   B  1 1088 ? -2.942  36.627  84.122  1.00 22.83 ? 1086 GLY   B N     1 
ATOM   16558 C  CA    . GLY   B  1 1088 ? -2.016  35.610  84.550  1.00 22.75 ? 1086 GLY   B CA    1 
ATOM   16559 C  C     . GLY   B  1 1088 ? -2.705  34.629  85.467  1.00 20.07 ? 1086 GLY   B C     1 
ATOM   16560 O  O     . GLY   B  1 1088 ? -3.934  34.523  85.491  1.00 21.48 ? 1086 GLY   B O     1 
ATOM   16561 N  N     . PRO   B  1 1089 ? -1.924  33.929  86.282  1.00 21.62 ? 1087 PRO   B N     1 
ATOM   16562 C  CA    . PRO   B  1 1089 ? -2.511  32.950  87.200  1.00 20.79 ? 1087 PRO   B CA    1 
ATOM   16563 C  C     . PRO   B  1 1089 ? -3.188  33.636  88.374  1.00 20.53 ? 1087 PRO   B C     1 
ATOM   16564 O  O     . PRO   B  1 1089 ? -2.893  34.787  88.715  1.00 19.12 ? 1087 PRO   B O     1 
ATOM   16565 C  CB    . PRO   B  1 1089 ? -1.295  32.136  87.666  1.00 22.50 ? 1087 PRO   B CB    1 
ATOM   16566 C  CG    . PRO   B  1 1089 ? -0.165  33.136  87.625  1.00 25.91 ? 1087 PRO   B CG    1 
ATOM   16567 C  CD    . PRO   B  1 1089 ? -0.461  34.041  86.435  1.00 22.29 ? 1087 PRO   B CD    1 
ATOM   16568 N  N     . VAL   B  1 1090 ? -4.108  32.901  89.005  1.00 20.52 ? 1088 VAL   B N     1 
ATOM   16569 C  CA    . VAL   B  1 1090 ? -4.607  33.341  90.300  1.00 18.33 ? 1088 VAL   B CA    1 
ATOM   16570 C  C     . VAL   B  1 1090 ? -3.435  33.460  91.288  1.00 22.19 ? 1088 VAL   B C     1 
ATOM   16571 O  O     . VAL   B  1 1090 ? -2.354  32.876  91.107  1.00 17.99 ? 1088 VAL   B O     1 
ATOM   16572 C  CB    . VAL   B  1 1090 ? -5.692  32.401  90.855  1.00 22.50 ? 1088 VAL   B CB    1 
ATOM   16573 C  CG1   . VAL   B  1 1090 ? -6.860  32.252  89.867  1.00 24.49 ? 1088 VAL   B CG1   1 
ATOM   16574 C  CG2   . VAL   B  1 1090 ? -5.101  31.036  91.216  1.00 19.02 ? 1088 VAL   B CG2   1 
ATOM   16575 N  N     . GLY   B  1 1091 ? -3.662  34.229  92.352  1.00 19.87 ? 1089 GLY   B N     1 
ATOM   16576 C  CA    . GLY   B  1 1091 ? -2.665  34.316  93.404  1.00 19.93 ? 1089 GLY   B CA    1 
ATOM   16577 C  C     . GLY   B  1 1091 ? -1.446  35.114  93.017  1.00 20.19 ? 1089 GLY   B C     1 
ATOM   16578 O  O     . GLY   B  1 1091 ? -0.421  35.044  93.688  1.00 19.97 ? 1089 GLY   B O     1 
ATOM   16579 N  N     . GLU   B  1 1092 ? -1.546  35.892  91.953  1.00 17.09 ? 1090 GLU   B N     1 
ATOM   16580 C  CA    . GLU   B  1 1092 ? -0.454  36.705  91.471  1.00 19.01 ? 1090 GLU   B CA    1 
ATOM   16581 C  C     . GLU   B  1 1092 ? -1.051  37.926  90.805  1.00 19.66 ? 1090 GLU   B C     1 
ATOM   16582 O  O     . GLU   B  1 1092 ? -2.112  37.841  90.178  1.00 20.68 ? 1090 GLU   B O     1 
ATOM   16583 C  CB    . GLU   B  1 1092 ? 0.405   35.919  90.485  1.00 22.93 ? 1090 GLU   B CB    1 
ATOM   16584 C  CG    . GLU   B  1 1092 ? 1.806   36.372  90.387  1.00 24.95 ? 1090 GLU   B CG    1 
ATOM   16585 C  CD    . GLU   B  1 1092 ? 2.615   35.454  89.493  1.00 24.27 ? 1090 GLU   B CD    1 
ATOM   16586 O  OE1   . GLU   B  1 1092 ? 2.352   35.450  88.270  1.00 21.28 ? 1090 GLU   B OE1   1 
ATOM   16587 O  OE2   . GLU   B  1 1092 ? 3.486   34.725  90.020  1.00 26.72 ? 1090 GLU   B OE2   1 
ATOM   16588 N  N     . ARG   B  1 1093 ? -0.390  39.065  90.968  1.00 18.35 ? 1091 ARG   B N     1 
ATOM   16589 C  CA    . ARG   B  1 1093 ? -0.800  40.290  90.296  1.00 17.60 ? 1091 ARG   B CA    1 
ATOM   16590 C  C     . ARG   B  1 1093 ? 0.377   40.744  89.461  1.00 18.24 ? 1091 ARG   B C     1 
ATOM   16591 O  O     . ARG   B  1 1093 ? 1.477   40.952  89.984  1.00 19.52 ? 1091 ARG   B O     1 
ATOM   16592 C  CB    . ARG   B  1 1093 ? -1.239  41.377  91.284  1.00 19.82 ? 1091 ARG   B CB    1 
ATOM   16593 N  N     . ASN   B  1 1094 ? 0.160   40.852  88.164  1.00 17.06 ? 1092 ASN   B N     1 
ATOM   16594 C  CA    . ASN   B  1 1094 ? 1.247   41.118  87.236  1.00 17.40 ? 1092 ASN   B CA    1 
ATOM   16595 C  C     . ASN   B  1 1094 ? 0.962   42.455  86.578  1.00 18.70 ? 1092 ASN   B C     1 
ATOM   16596 O  O     . ASN   B  1 1094 ? -0.030  42.602  85.860  1.00 18.19 ? 1092 ASN   B O     1 
ATOM   16597 C  CB    . ASN   B  1 1094 ? 1.375   39.976  86.236  1.00 17.20 ? 1092 ASN   B CB    1 
ATOM   16598 C  CG    . ASN   B  1 1094 ? 1.940   38.735  86.896  1.00 17.60 ? 1092 ASN   B CG    1 
ATOM   16599 O  OD1   . ASN   B  1 1094 ? 3.106   38.713  87.269  1.00 17.71 ? 1092 ASN   B OD1   1 
ATOM   16600 N  ND2   . ASN   B  1 1094 ? 1.113   37.719  87.077  1.00 19.71 ? 1092 ASN   B ND2   1 
ATOM   16601 N  N     . LEU   B  1 1095 ? 1.815   43.428  86.866  1.00 17.20 ? 1093 LEU   B N     1 
ATOM   16602 C  CA    . LEU   B  1 1095 ? 1.581   44.817  86.519  1.00 17.39 ? 1093 LEU   B CA    1 
ATOM   16603 C  C     . LEU   B  1 1095 ? 2.597   45.248  85.482  1.00 16.98 ? 1093 LEU   B C     1 
ATOM   16604 O  O     . LEU   B  1 1095 ? 3.740   44.796  85.490  1.00 17.31 ? 1093 LEU   B O     1 
ATOM   16605 C  CB    . LEU   B  1 1095 ? 1.690   45.716  87.757  1.00 18.30 ? 1093 LEU   B CB    1 
ATOM   16606 C  CG    . LEU   B  1 1095 ? 0.786   45.264  88.911  1.00 22.72 ? 1093 LEU   B CG    1 
ATOM   16607 C  CD1   . LEU   B  1 1095 ? 0.936   46.186  90.125  1.00 27.28 ? 1093 LEU   B CD1   1 
ATOM   16608 C  CD2   . LEU   B  1 1095 ? -0.651  45.212  88.432  1.00 22.77 ? 1093 LEU   B CD2   1 
ATOM   16609 N  N     . TYR   B  1 1096 ? 2.166   46.138  84.597  1.00 18.02 ? 1094 TYR   B N     1 
ATOM   16610 C  CA    . TYR   B  1 1096 ? 3.008   46.619  83.512  1.00 16.15 ? 1094 TYR   B CA    1 
ATOM   16611 C  C     . TYR   B  1 1096 ? 2.788   48.113  83.432  1.00 15.62 ? 1094 TYR   B C     1 
ATOM   16612 O  O     . TYR   B  1 1096 ? 1.647   48.567  83.316  1.00 16.02 ? 1094 TYR   B O     1 
ATOM   16613 C  CB    . TYR   B  1 1096 ? 2.649   45.921  82.196  1.00 17.74 ? 1094 TYR   B CB    1 
ATOM   16614 C  CG    . TYR   B  1 1096 ? 3.333   46.450  80.962  1.00 15.86 ? 1094 TYR   B CG    1 
ATOM   16615 C  CD1   . TYR   B  1 1096 ? 4.603   46.027  80.603  1.00 16.42 ? 1094 TYR   B CD1   1 
ATOM   16616 C  CD2   . TYR   B  1 1096 ? 2.669   47.343  80.126  1.00 18.34 ? 1094 TYR   B CD2   1 
ATOM   16617 C  CE1   . TYR   B  1 1096 ? 5.204   46.498  79.437  1.00 19.37 ? 1094 TYR   B CE1   1 
ATOM   16618 C  CE2   . TYR   B  1 1096 ? 3.255   47.824  78.980  1.00 19.74 ? 1094 TYR   B CE2   1 
ATOM   16619 C  CZ    . TYR   B  1 1096 ? 4.512   47.407  78.639  1.00 17.34 ? 1094 TYR   B CZ    1 
ATOM   16620 O  OH    . TYR   B  1 1096 ? 5.075   47.900  77.489  1.00 17.60 ? 1094 TYR   B OH    1 
ATOM   16621 N  N     . THR   B  1 1097 ? 3.864   48.875  83.557  1.00 16.16 ? 1095 THR   B N     1 
ATOM   16622 C  CA    . THR   B  1 1097 ? 3.766   50.325  83.671  1.00 16.83 ? 1095 THR   B CA    1 
ATOM   16623 C  C     . THR   B  1 1097 ? 4.806   50.983  82.778  1.00 14.11 ? 1095 THR   B C     1 
ATOM   16624 O  O     . THR   B  1 1097 ? 5.882   50.429  82.539  1.00 16.23 ? 1095 THR   B O     1 
ATOM   16625 C  CB    . THR   B  1 1097 ? 3.972   50.808  85.128  1.00 18.89 ? 1095 THR   B CB    1 
ATOM   16626 O  OG1   . THR   B  1 1097 ? 5.214   50.304  85.628  1.00 22.74 ? 1095 THR   B OG1   1 
ATOM   16627 C  CG2   . THR   B  1 1097 ? 2.857   50.326  86.039  1.00 21.66 ? 1095 THR   B CG2   1 
ATOM   16628 N  N     . LEU   B  1 1098 ? 4.473   52.173  82.284  1.00 14.13 ? 1096 LEU   B N     1 
ATOM   16629 C  CA    . LEU   B  1 1098 ? 5.390   52.949  81.462  1.00 16.76 ? 1096 LEU   B CA    1 
ATOM   16630 C  C     . LEU   B  1 1098 ? 5.806   54.197  82.221  1.00 17.15 ? 1096 LEU   B C     1 
ATOM   16631 O  O     . LEU   B  1 1098 ? 4.961   55.026  82.571  1.00 16.02 ? 1096 LEU   B O     1 
ATOM   16632 C  CB    . LEU   B  1 1098 ? 4.752   53.324  80.128  1.00 16.17 ? 1096 LEU   B CB    1 
ATOM   16633 C  CG    . LEU   B  1 1098 ? 4.421   52.135  79.238  1.00 15.42 ? 1096 LEU   B CG    1 
ATOM   16634 C  CD1   . LEU   B  1 1098 ? 3.790   52.667  77.948  1.00 15.86 ? 1096 LEU   B CD1   1 
ATOM   16635 C  CD2   . LEU   B  1 1098 ? 5.668   51.302  78.976  1.00 15.32 ? 1096 LEU   B CD2   1 
ATOM   16636 N  N     . HIS   B  1 1099 ? 7.113   54.352  82.419  1.00 16.87 ? 1097 HIS   B N     1 
ATOM   16637 C  CA    . HIS   B  1 1099 ? 7.694   55.451  83.165  1.00 18.39 ? 1097 HIS   B CA    1 
ATOM   16638 C  C     . HIS   B  1 1099 ? 8.595   56.266  82.256  1.00 15.25 ? 1097 HIS   B C     1 
ATOM   16639 O  O     . HIS   B  1 1099 ? 8.873   55.891  81.116  1.00 16.58 ? 1097 HIS   B O     1 
ATOM   16640 C  CB    . HIS   B  1 1099 ? 8.520   54.940  84.343  1.00 19.90 ? 1097 HIS   B CB    1 
ATOM   16641 C  CG    . HIS   B  1 1099 ? 7.766   54.052  85.277  1.00 22.02 ? 1097 HIS   B CG    1 
ATOM   16642 N  ND1   . HIS   B  1 1099 ? 7.391   54.455  86.541  1.00 22.89 ? 1097 HIS   B ND1   1 
ATOM   16643 C  CD2   . HIS   B  1 1099 ? 7.318   52.783  85.134  1.00 21.70 ? 1097 HIS   B CD2   1 
ATOM   16644 C  CE1   . HIS   B  1 1099 ? 6.752   53.466  87.141  1.00 26.26 ? 1097 HIS   B CE1   1 
ATOM   16645 N  NE2   . HIS   B  1 1099 ? 6.696   52.440  86.310  1.00 21.97 ? 1097 HIS   B NE2   1 
ATOM   16646 N  N     . ALA   B  1 1100 ? 9.076   57.378  82.789  1.00 18.68 ? 1098 ALA   B N     1 
ATOM   16647 C  CA    . ALA   B  1 1100 ? 10.091  58.127  82.075  1.00 19.33 ? 1098 ALA   B CA    1 
ATOM   16648 C  C     . ALA   B  1 1100 ? 11.361  57.296  81.999  1.00 22.73 ? 1098 ALA   B C     1 
ATOM   16649 O  O     . ALA   B  1 1100 ? 11.659  56.501  82.892  1.00 19.82 ? 1098 ALA   B O     1 
ATOM   16650 C  CB    . ALA   B  1 1100 ? 10.369  59.460  82.771  1.00 21.86 ? 1098 ALA   B CB    1 
ATOM   16651 N  N     . ARG   B  1 1101 ? 12.104  57.469  80.910  1.00 20.07 ? 1099 ARG   B N     1 
ATOM   16652 C  CA    . ARG   B  1 1101 ? 13.346  56.720  80.766  1.00 22.37 ? 1099 ARG   B CA    1 
ATOM   16653 C  C     . ARG   B  1 1101 ? 14.469  57.315  81.599  1.00 22.09 ? 1099 ARG   B C     1 
ATOM   16654 O  O     . ARG   B  1 1101 ? 15.312  56.578  82.124  1.00 23.35 ? 1099 ARG   B O     1 
ATOM   16655 C  CB    . ARG   B  1 1101 ? 13.763  56.671  79.306  1.00 23.01 ? 1099 ARG   B CB    1 
ATOM   16656 C  CG    . ARG   B  1 1101 ? 13.321  55.417  78.636  1.00 28.82 ? 1099 ARG   B CG    1 
ATOM   16657 C  CD    . ARG   B  1 1101 ? 13.761  55.403  77.214  1.00 25.90 ? 1099 ARG   B CD    1 
ATOM   16658 N  NE    . ARG   B  1 1101 ? 14.857  54.473  76.989  1.00 31.01 ? 1099 ARG   B NE    1 
ATOM   16659 C  CZ    . ARG   B  1 1101 ? 14.704  53.226  76.567  1.00 35.83 ? 1099 ARG   B CZ    1 
ATOM   16660 N  NH1   . ARG   B  1 1101 ? 13.505  52.705  76.373  1.00 31.74 ? 1099 ARG   B NH1   1 
ATOM   16661 N  NH2   . ARG   B  1 1101 ? 15.780  52.488  76.320  1.00 31.86 ? 1099 ARG   B NH2   1 
ATOM   16662 N  N     . GLY   B  1 1102 ? 14.508  58.640  81.717  1.00 18.23 ? 1100 GLY   B N     1 
ATOM   16663 C  CA    . GLY   B  1 1102 ? 15.601  59.302  82.395  1.00 19.93 ? 1100 GLY   B CA    1 
ATOM   16664 C  C     . GLY   B  1 1102 ? 15.986  60.569  81.664  1.00 23.37 ? 1100 GLY   B C     1 
ATOM   16665 O  O     . GLY   B  1 1102 ? 15.124  61.399  81.367  1.00 21.15 ? 1100 GLY   B O     1 
ATOM   16666 N  N     . ARG   B  1 1103 ? 17.266  60.745  81.363  1.00 22.35 ? 1101 ARG   B N     1 
ATOM   16667 C  CA    . ARG   B  1 1103 ? 17.719  61.934  80.654  1.00 23.54 ? 1101 ARG   B CA    1 
ATOM   16668 C  C     . ARG   B  1 1103 ? 18.023  61.549  79.214  1.00 19.61 ? 1101 ARG   B C     1 
ATOM   16669 O  O     . ARG   B  1 1103 ? 18.810  60.635  78.967  1.00 20.18 ? 1101 ARG   B O     1 
ATOM   16670 C  CB    . ARG   B  1 1103 ? 18.947  62.559  81.319  1.00 23.57 ? 1101 ARG   B CB    1 
ATOM   16671 C  CG    . ARG   B  1 1103 ? 19.286  63.945  80.740  1.00 24.27 ? 1101 ARG   B CG    1 
ATOM   16672 C  CD    . ARG   B  1 1103 ? 20.363  64.655  81.551  1.00 27.38 ? 1101 ARG   B CD    1 
ATOM   16673 N  NE    . ARG   B  1 1103 ? 19.952  64.876  82.935  1.00 31.30 ? 1101 ARG   B NE    1 
ATOM   16674 C  CZ    . ARG   B  1 1103 ? 19.373  65.981  83.394  1.00 35.73 ? 1101 ARG   B CZ    1 
ATOM   16675 N  NH1   . ARG   B  1 1103 ? 19.097  67.013  82.597  1.00 28.89 ? 1101 ARG   B NH1   1 
ATOM   16676 N  NH2   . ARG   B  1 1103 ? 19.071  66.061  84.687  1.00 33.77 ? 1101 ARG   B NH2   1 
ATOM   16677 N  N     . ILE   B  1 1104 ? 17.389  62.230  78.271  1.00 18.04 ? 1102 ILE   B N     1 
ATOM   16678 C  CA    . ILE   B  1 1104 ? 17.563  61.925  76.858  1.00 18.57 ? 1102 ILE   B CA    1 
ATOM   16679 C  C     . ILE   B  1 1104 ? 18.587  62.880  76.269  1.00 19.27 ? 1102 ILE   B C     1 
ATOM   16680 O  O     . ILE   B  1 1104 ? 18.476  64.098  76.430  1.00 19.17 ? 1102 ILE   B O     1 
ATOM   16681 C  CB    . ILE   B  1 1104 ? 16.232  62.013  76.099  1.00 18.72 ? 1102 ILE   B CB    1 
ATOM   16682 C  CG1   . ILE   B  1 1104 ? 15.171  61.168  76.817  1.00 16.73 ? 1102 ILE   B CG1   1 
ATOM   16683 C  CG2   . ILE   B  1 1104 ? 16.417  61.567  74.654  1.00 18.22 ? 1102 ILE   B CG2   1 
ATOM   16684 C  CD1   . ILE   B  1 1104 ? 15.505  59.702  76.914  1.00 17.37 ? 1102 ILE   B CD1   1 
ATOM   16685 N  N     . LEU   B  1 1105 ? 19.583  62.327  75.586  1.00 17.36 ? 1103 LEU   B N     1 
ATOM   16686 C  CA    . LEU   B  1 1105 ? 20.526  63.150  74.843  1.00 16.59 ? 1103 LEU   B CA    1 
ATOM   16687 C  C     . LEU   B  1 1105 ? 19.841  63.696  73.593  1.00 16.70 ? 1103 LEU   B C     1 
ATOM   16688 O  O     . LEU   B  1 1105 ? 19.340  62.928  72.770  1.00 17.62 ? 1103 LEU   B O     1 
ATOM   16689 C  CB    . LEU   B  1 1105 ? 21.745  62.311  74.462  1.00 17.25 ? 1103 LEU   B CB    1 
ATOM   16690 C  CG    . LEU   B  1 1105 ? 22.783  62.972  73.560  1.00 21.37 ? 1103 LEU   B CG    1 
ATOM   16691 C  CD1   . LEU   B  1 1105 ? 23.434  64.142  74.253  1.00 18.54 ? 1103 LEU   B CD1   1 
ATOM   16692 C  CD2   . LEU   B  1 1105 ? 23.813  61.940  73.123  1.00 20.30 ? 1103 LEU   B CD2   1 
ATOM   16693 N  N     . LEU   B  1 1106 ? 19.825  65.012  73.445  1.00 17.73 ? 1104 LEU   B N     1 
ATOM   16694 C  CA    . LEU   B  1 1106 ? 19.258  65.656  72.272  1.00 17.16 ? 1104 LEU   B CA    1 
ATOM   16695 C  C     . LEU   B  1 1106 ? 20.398  66.182  71.426  1.00 17.06 ? 1104 LEU   B C     1 
ATOM   16696 O  O     . LEU   B  1 1106 ? 21.244  66.927  71.923  1.00 20.30 ? 1104 LEU   B O     1 
ATOM   16697 C  CB    . LEU   B  1 1106 ? 18.332  66.815  72.643  1.00 16.49 ? 1104 LEU   B CB    1 
ATOM   16698 C  CG    . LEU   B  1 1106 ? 17.124  66.466  73.510  1.00 19.24 ? 1104 LEU   B CG    1 
ATOM   16699 C  CD1   . LEU   B  1 1106 ? 16.123  67.615  73.485  1.00 17.01 ? 1104 LEU   B CD1   1 
ATOM   16700 C  CD2   . LEU   B  1 1106 ? 16.512  65.147  73.093  1.00 20.71 ? 1104 LEU   B CD2   1 
ATOM   16701 N  N     . VAL   B  1 1107 ? 20.407  65.805  70.154  1.00 17.49 ? 1105 VAL   B N     1 
ATOM   16702 C  CA    . VAL   B  1 1107 ? 21.432  66.289  69.237  1.00 16.57 ? 1105 VAL   B CA    1 
ATOM   16703 C  C     . VAL   B  1 1107 ? 20.699  66.989  68.107  1.00 16.76 ? 1105 VAL   B C     1 
ATOM   16704 O  O     . VAL   B  1 1107 ? 20.521  66.406  67.030  1.00 20.37 ? 1105 VAL   B O     1 
ATOM   16705 C  CB    . VAL   B  1 1107 ? 22.317  65.145  68.724  1.00 18.87 ? 1105 VAL   B CB    1 
ATOM   16706 C  CG1   . VAL   B  1 1107 ? 23.526  65.703  67.989  1.00 18.96 ? 1105 VAL   B CG1   1 
ATOM   16707 C  CG2   . VAL   B  1 1107 ? 22.754  64.265  69.889  1.00 17.92 ? 1105 VAL   B CG2   1 
ATOM   16708 N  N     . PRO   B  1 1108 ? 20.225  68.207  68.321  1.00 18.03 ? 1106 PRO   B N     1 
ATOM   16709 C  CA    . PRO   B  1 1108 ? 19.489  68.910  67.275  1.00 21.28 ? 1106 PRO   B CA    1 
ATOM   16710 C  C     . PRO   B  1 1108 ? 20.424  69.562  66.267  1.00 23.53 ? 1106 PRO   B C     1 
ATOM   16711 O  O     . PRO   B  1 1108 ? 21.613  69.772  66.512  1.00 24.28 ? 1106 PRO   B O     1 
ATOM   16712 C  CB    . PRO   B  1 1108 ? 18.711  69.967  68.063  1.00 18.52 ? 1106 PRO   B CB    1 
ATOM   16713 C  CG    . PRO   B  1 1108 ? 19.660  70.293  69.191  1.00 22.56 ? 1106 PRO   B CG    1 
ATOM   16714 C  CD    . PRO   B  1 1108 ? 20.278  68.981  69.575  1.00 18.49 ? 1106 PRO   B CD    1 
ATOM   16715 N  N     . ALA   B  1 1109 ? 19.853  69.882  65.112  1.00 23.34 ? 1107 ALA   B N     1 
ATOM   16716 C  CA    . ALA   B  1 1109 ? 20.521  70.700  64.111  1.00 25.16 ? 1107 ALA   B CA    1 
ATOM   16717 C  C     . ALA   B  1 1109 ? 19.882  72.068  63.953  1.00 26.60 ? 1107 ALA   B C     1 
ATOM   16718 O  O     . ALA   B  1 1109 ? 20.580  73.040  63.655  1.00 28.26 ? 1107 ALA   B O     1 
ATOM   16719 C  CB    . ALA   B  1 1109 ? 20.517  69.988  62.752  1.00 25.22 ? 1107 ALA   B CB    1 
ATOM   16720 N  N     . THR   B  1 1110 ? 18.574  72.167  64.167  1.00 24.21 ? 1108 THR   B N     1 
ATOM   16721 C  CA    . THR   B  1 1110 ? 17.835  73.396  63.939  1.00 23.26 ? 1108 THR   B CA    1 
ATOM   16722 C  C     . THR   B  1 1110 ? 16.972  73.713  65.150  1.00 25.13 ? 1108 THR   B C     1 
ATOM   16723 O  O     . THR   B  1 1110 ? 16.658  72.841  65.969  1.00 23.75 ? 1108 THR   B O     1 
ATOM   16724 C  CB    . THR   B  1 1110 ? 16.946  73.287  62.689  1.00 26.61 ? 1108 THR   B CB    1 
ATOM   16725 O  OG1   . THR   B  1 1110 ? 15.957  72.262  62.887  1.00 26.89 ? 1108 THR   B OG1   1 
ATOM   16726 C  CG2   . THR   B  1 1110 ? 17.787  72.940  61.469  1.00 26.34 ? 1108 THR   B CG2   1 
ATOM   16727 N  N     . GLU   B  1 1111 ? 16.566  74.980  65.242  1.00 26.09 ? 1109 GLU   B N     1 
ATOM   16728 C  CA    . GLU   B  1 1111 ? 15.733  75.391  66.364  1.00 28.46 ? 1109 GLU   B CA    1 
ATOM   16729 C  C     . GLU   B  1 1111 ? 14.446  74.579  66.407  1.00 25.43 ? 1109 GLU   B C     1 
ATOM   16730 O  O     . GLU   B  1 1111 ? 14.058  74.064  67.462  1.00 24.26 ? 1109 GLU   B O     1 
ATOM   16731 C  CB    . GLU   B  1 1111 ? 15.430  76.884  66.278  1.00 29.10 ? 1109 GLU   B CB    1 
ATOM   16732 C  CG    . GLU   B  1 1111 ? 14.460  77.353  67.337  1.00 28.85 ? 1109 GLU   B CG    1 
ATOM   16733 C  CD    . GLU   B  1 1111 ? 14.233  78.848  67.267  1.00 30.93 ? 1109 GLU   B CD    1 
ATOM   16734 O  OE1   . GLU   B  1 1111 ? 15.052  79.596  67.837  1.00 33.34 ? 1109 GLU   B OE1   1 
ATOM   16735 O  OE2   . GLU   B  1 1111 ? 13.244  79.269  66.636  1.00 33.07 ? 1109 GLU   B OE2   1 
ATOM   16736 N  N     . SER   B  1 1112 ? 13.785  74.431  65.257  1.00 24.13 ? 1110 SER   B N     1 
ATOM   16737 C  CA    . SER   B  1 1112 ? 12.546  73.667  65.217  1.00 25.99 ? 1110 SER   B CA    1 
ATOM   16738 C  C     . SER   B  1 1112 ? 12.794  72.207  65.558  1.00 26.77 ? 1110 SER   B C     1 
ATOM   16739 O  O     . SER   B  1 1112 ? 12.001  71.585  66.276  1.00 24.87 ? 1110 SER   B O     1 
ATOM   16740 C  CB    . SER   B  1 1112 ? 11.894  73.790  63.844  1.00 30.35 ? 1110 SER   B CB    1 
ATOM   16741 O  OG    . SER   B  1 1112 ? 10.614  73.188  63.869  1.00 30.15 ? 1110 SER   B OG    1 
ATOM   16742 N  N     . GLY   B  1 1113 ? 13.891  71.641  65.051  1.00 21.81 ? 1111 GLY   B N     1 
ATOM   16743 C  CA    . GLY   B  1 1113 ? 14.252  70.290  65.441  1.00 22.91 ? 1111 GLY   B CA    1 
ATOM   16744 C  C     . GLY   B  1 1113 ? 14.377  70.153  66.943  1.00 22.07 ? 1111 GLY   B C     1 
ATOM   16745 O  O     . GLY   B  1 1113 ? 13.880  69.190  67.532  1.00 21.78 ? 1111 GLY   B O     1 
ATOM   16746 N  N     . LEU   B  1 1114 ? 15.028  71.131  67.581  1.00 20.04 ? 1112 LEU   B N     1 
ATOM   16747 C  CA    . LEU   B  1 1114 ? 15.196  71.117  69.030  1.00 20.60 ? 1112 LEU   B CA    1 
ATOM   16748 C  C     . LEU   B  1 1114 ? 13.849  71.167  69.735  1.00 20.63 ? 1112 LEU   B C     1 
ATOM   16749 O  O     . LEU   B  1 1114 ? 13.608  70.421  70.689  1.00 18.27 ? 1112 LEU   B O     1 
ATOM   16750 C  CB    . LEU   B  1 1114 ? 16.062  72.301  69.462  1.00 21.78 ? 1112 LEU   B CB    1 
ATOM   16751 C  CG    . LEU   B  1 1114 ? 16.202  72.523  70.977  1.00 24.33 ? 1112 LEU   B CG    1 
ATOM   16752 C  CD1   . LEU   B  1 1114 ? 16.702  71.259  71.696  1.00 19.63 ? 1112 LEU   B CD1   1 
ATOM   16753 C  CD2   . LEU   B  1 1114 ? 17.099  73.725  71.253  1.00 24.80 ? 1112 LEU   B CD2   1 
ATOM   16754 N  N     . TYR   B  1 1115 ? 12.957  72.054  69.282  1.00 22.86 ? 1113 TYR   B N     1 
ATOM   16755 C  CA    . TYR   B  1 1115 ? 11.630  72.110  69.887  1.00 21.40 ? 1113 TYR   B CA    1 
ATOM   16756 C  C     . TYR   B  1 1115 ? 10.911  70.777  69.746  1.00 17.23 ? 1113 TYR   B C     1 
ATOM   16757 O  O     . TYR   B  1 1115 ? 10.288  70.302  70.700  1.00 21.13 ? 1113 TYR   B O     1 
ATOM   16758 C  CB    . TYR   B  1 1115 ? 10.800  73.233  69.266  1.00 25.01 ? 1113 TYR   B CB    1 
ATOM   16759 C  CG    . TYR   B  1 1115 ? 11.315  74.627  69.547  1.00 22.70 ? 1113 TYR   B CG    1 
ATOM   16760 C  CD1   . TYR   B  1 1115 ? 12.241  74.867  70.551  1.00 23.69 ? 1113 TYR   B CD1   1 
ATOM   16761 C  CD2   . TYR   B  1 1115 ? 10.863  75.704  68.806  1.00 30.55 ? 1113 TYR   B CD2   1 
ATOM   16762 C  CE1   . TYR   B  1 1115 ? 12.711  76.145  70.793  1.00 29.00 ? 1113 TYR   B CE1   1 
ATOM   16763 C  CE2   . TYR   B  1 1115 ? 11.315  76.976  69.044  1.00 30.11 ? 1113 TYR   B CE2   1 
ATOM   16764 C  CZ    . TYR   B  1 1115 ? 12.237  77.196  70.034  1.00 32.31 ? 1113 TYR   B CZ    1 
ATOM   16765 O  OH    . TYR   B  1 1115 ? 12.683  78.483  70.242  1.00 33.97 ? 1113 TYR   B OH    1 
ATOM   16766 N  N     . HIS   B  1 1116 ? 10.994  70.149  68.570  1.00 16.86 ? 1114 HIS   B N     1 
ATOM   16767 C  CA    . HIS   B  1 1116 ? 10.333  68.859  68.394  1.00 19.76 ? 1114 HIS   B CA    1 
ATOM   16768 C  C     . HIS   B  1 1116 ? 10.961  67.784  69.278  1.00 22.77 ? 1114 HIS   B C     1 
ATOM   16769 O  O     . HIS   B  1 1116 ? 10.241  67.004  69.909  1.00 19.69 ? 1114 HIS   B O     1 
ATOM   16770 C  CB    . HIS   B  1 1116 ? 10.360  68.438  66.925  1.00 21.67 ? 1114 HIS   B CB    1 
ATOM   16771 C  CG    . HIS   B  1 1116 ? 9.342   69.133  66.078  1.00 25.27 ? 1114 HIS   B CG    1 
ATOM   16772 N  ND1   . HIS   B  1 1116 ? 9.524   70.407  65.586  1.00 28.26 ? 1114 HIS   B ND1   1 
ATOM   16773 C  CD2   . HIS   B  1 1116 ? 8.126   68.730  65.639  1.00 26.92 ? 1114 HIS   B CD2   1 
ATOM   16774 C  CE1   . HIS   B  1 1116 ? 8.465   70.759  64.879  1.00 30.14 ? 1114 HIS   B CE1   1 
ATOM   16775 N  NE2   . HIS   B  1 1116 ? 7.603   69.759  64.894  1.00 32.44 ? 1114 HIS   B NE2   1 
ATOM   16776 N  N     . GLN   B  1 1117 ? 12.300  67.727  69.348  1.00 17.63 ? 1115 GLN   B N     1 
ATOM   16777 C  CA    . GLN   B  1 1117 ? 12.945  66.742  70.215  1.00 17.91 ? 1115 GLN   B CA    1 
ATOM   16778 C  C     . GLN   B  1 1117 ? 12.597  66.983  71.669  1.00 18.17 ? 1115 GLN   B C     1 
ATOM   16779 O  O     . GLN   B  1 1117 ? 12.349  66.034  72.423  1.00 20.09 ? 1115 GLN   B O     1 
ATOM   16780 C  CB    . GLN   B  1 1117 ? 14.471  66.783  70.054  1.00 17.20 ? 1115 GLN   B CB    1 
ATOM   16781 C  CG    . GLN   B  1 1117 ? 14.967  66.337  68.705  1.00 19.40 ? 1115 GLN   B CG    1 
ATOM   16782 C  CD    . GLN   B  1 1117 ? 16.474  66.533  68.551  1.00 21.26 ? 1115 GLN   B CD    1 
ATOM   16783 O  OE1   . GLN   B  1 1117 ? 17.108  67.204  69.366  1.00 19.65 ? 1115 GLN   B OE1   1 
ATOM   16784 N  NE2   . GLN   B  1 1117 ? 17.049  65.930  67.517  1.00 16.91 ? 1115 GLN   B NE2   1 
ATOM   16785 N  N     . LEU   B  1 1118 ? 12.634  68.242  72.100  1.00 18.35 ? 1116 LEU   B N     1 
ATOM   16786 C  CA    . LEU   B  1 1118 ? 12.310  68.536  73.488  1.00 18.44 ? 1116 LEU   B CA    1 
ATOM   16787 C  C     . LEU   B  1 1118 ? 10.869  68.137  73.796  1.00 19.54 ? 1116 LEU   B C     1 
ATOM   16788 O  O     . LEU   B  1 1118 ? 10.599  67.505  74.824  1.00 19.67 ? 1116 LEU   B O     1 
ATOM   16789 C  CB    . LEU   B  1 1118 ? 12.547  70.018  73.775  1.00 21.29 ? 1116 LEU   B CB    1 
ATOM   16790 C  CG    . LEU   B  1 1118 ? 12.523  70.484  75.237  1.00 26.91 ? 1116 LEU   B CG    1 
ATOM   16791 C  CD1   . LEU   B  1 1118 ? 13.441  69.633  76.121  1.00 28.24 ? 1116 LEU   B CD1   1 
ATOM   16792 C  CD2   . LEU   B  1 1118 ? 12.911  71.948  75.330  1.00 29.39 ? 1116 LEU   B CD2   1 
ATOM   16793 N  N     . ALA   B  1 1119 ? 9.938   68.472  72.899  1.00 19.57 ? 1117 ALA   B N     1 
ATOM   16794 C  CA    . ALA   B  1 1119 ? 8.543   68.061  73.079  1.00 21.56 ? 1117 ALA   B CA    1 
ATOM   16795 C  C     . ALA   B  1 1119 ? 8.429   66.551  73.248  1.00 20.94 ? 1117 ALA   B C     1 
ATOM   16796 O  O     . ALA   B  1 1119 ? 7.767   66.065  74.173  1.00 19.00 ? 1117 ALA   B O     1 
ATOM   16797 C  CB    . ALA   B  1 1119 ? 7.697   68.524  71.892  1.00 19.56 ? 1117 ALA   B CB    1 
ATOM   16798 N  N     . ALA   B  1 1120 ? 9.079   65.794  72.359  1.00 19.94 ? 1118 ALA   B N     1 
ATOM   16799 C  CA    . ALA   B  1 1120 ? 9.046   64.335  72.447  1.00 20.98 ? 1118 ALA   B CA    1 
ATOM   16800 C  C     . ALA   B  1 1120 ? 9.575   63.853  73.791  1.00 21.48 ? 1118 ALA   B C     1 
ATOM   16801 O  O     . ALA   B  1 1120 ? 8.970   62.987  74.433  1.00 16.39 ? 1118 ALA   B O     1 
ATOM   16802 C  CB    . ALA   B  1 1120 ? 9.860   63.720  71.305  1.00 20.44 ? 1118 ALA   B CB    1 
ATOM   16803 N  N     . ALA   B  1 1121 ? 10.713  64.398  74.231  1.00 17.40 ? 1119 ALA   B N     1 
ATOM   16804 C  CA    . ALA   B  1 1121 ? 11.322  63.932  75.475  1.00 17.20 ? 1119 ALA   B CA    1 
ATOM   16805 C  C     . ALA   B  1 1121 ? 10.514  64.371  76.692  1.00 17.29 ? 1119 ALA   B C     1 
ATOM   16806 O  O     . ALA   B  1 1121 ? 10.351  63.601  77.646  1.00 17.21 ? 1119 ALA   B O     1 
ATOM   16807 C  CB    . ALA   B  1 1121 ? 12.758  64.440  75.584  1.00 17.89 ? 1119 ALA   B CB    1 
ATOM   16808 N  N     . LEU   B  1 1122 ? 10.002  65.602  76.679  1.00 17.01 ? 1120 LEU   B N     1 
ATOM   16809 C  CA    . LEU   B  1 1122 ? 9.221   66.077  77.815  1.00 17.29 ? 1120 LEU   B CA    1 
ATOM   16810 C  C     . LEU   B  1 1122 ? 7.895   65.336  77.908  1.00 18.22 ? 1120 LEU   B C     1 
ATOM   16811 O  O     . LEU   B  1 1122 ? 7.434   65.019  79.007  1.00 19.71 ? 1120 LEU   B O     1 
ATOM   16812 C  CB    . LEU   B  1 1122 ? 8.971   67.577  77.698  1.00 18.55 ? 1120 LEU   B CB    1 
ATOM   16813 C  CG    . LEU   B  1 1122 ? 10.184  68.493  77.810  1.00 20.20 ? 1120 LEU   B CG    1 
ATOM   16814 C  CD1   . LEU   B  1 1122 ? 9.715   69.901  77.578  1.00 20.46 ? 1120 LEU   B CD1   1 
ATOM   16815 C  CD2   . LEU   B  1 1122 ? 10.833  68.358  79.179  1.00 19.96 ? 1120 LEU   B CD2   1 
ATOM   16816 N  N     . ALA   B  1 1123 ? 7.276   65.051  76.758  1.00 16.75 ? 1121 ALA   B N     1 
ATOM   16817 C  CA    . ALA   B  1 1123 ? 5.986   64.364  76.742  1.00 20.57 ? 1121 ALA   B CA    1 
ATOM   16818 C  C     . ALA   B  1 1123 ? 6.077   62.986  77.369  1.00 21.34 ? 1121 ALA   B C     1 
ATOM   16819 O  O     . ALA   B  1 1123 ? 5.066   62.460  77.853  1.00 19.65 ? 1121 ALA   B O     1 
ATOM   16820 C  CB    . ALA   B  1 1123 ? 5.462   64.233  75.309  1.00 18.91 ? 1121 ALA   B CB    1 
ATOM   16821 N  N     . THR   B  1 1124 ? 7.264   62.388  77.356  1.00 16.50 ? 1122 THR   B N     1 
ATOM   16822 C  CA    . THR   B  1 1124 ? 7.475   61.076  77.937  1.00 17.79 ? 1122 THR   B CA    1 
ATOM   16823 C  C     . THR   B  1 1124 ? 8.143   61.158  79.305  1.00 15.51 ? 1122 THR   B C     1 
ATOM   16824 O  O     . THR   B  1 1124 ? 8.674   60.155  79.790  1.00 18.33 ? 1122 THR   B O     1 
ATOM   16825 C  CB    . THR   B  1 1124 ? 8.273   60.198  76.965  1.00 17.89 ? 1122 THR   B CB    1 
ATOM   16826 O  OG1   . THR   B  1 1124 ? 9.349   60.949  76.398  1.00 19.04 ? 1122 THR   B OG1   1 
ATOM   16827 C  CG2   . THR   B  1 1124 ? 7.370   59.762  75.810  1.00 19.42 ? 1122 THR   B CG2   1 
ATOM   16828 N  N     . GLY   B  1 1125 ? 8.105   62.325  79.940  1.00 17.44 ? 1123 GLY   B N     1 
ATOM   16829 C  CA    . GLY   B  1 1125 ? 8.527   62.462  81.325  1.00 18.40 ? 1123 GLY   B CA    1 
ATOM   16830 C  C     . GLY   B  1 1125 ? 10.014  62.620  81.531  1.00 19.51 ? 1123 GLY   B C     1 
ATOM   16831 O  O     . GLY   B  1 1125 ? 10.470  62.638  82.682  1.00 19.03 ? 1123 GLY   B O     1 
ATOM   16832 N  N     . ASN   B  1 1126 ? 10.781  62.753  80.460  1.00 16.95 ? 1124 ASN   B N     1 
ATOM   16833 C  CA    . ASN   B  1 1126 ? 12.230  62.751  80.566  1.00 19.11 ? 1124 ASN   B CA    1 
ATOM   16834 C  C     . ASN   B  1 1126 ? 12.772  64.152  80.794  1.00 18.44 ? 1124 ASN   B C     1 
ATOM   16835 O  O     . ASN   B  1 1126 ? 12.108  65.156  80.536  1.00 17.97 ? 1124 ASN   B O     1 
ATOM   16836 C  CB    . ASN   B  1 1126 ? 12.852  62.170  79.306  1.00 16.42 ? 1124 ASN   B CB    1 
ATOM   16837 C  CG    . ASN   B  1 1126 ? 12.388  60.770  79.037  1.00 16.64 ? 1124 ASN   B CG    1 
ATOM   16838 O  OD1   . ASN   B  1 1126 ? 12.729  59.841  79.767  1.00 20.04 ? 1124 ASN   B OD1   1 
ATOM   16839 N  ND2   . ASN   B  1 1126 ? 11.603  60.603  77.979  1.00 18.12 ? 1124 ASN   B ND2   1 
ATOM   16840 N  N     . SER   B  1 1127 ? 13.992  64.199  81.318  1.00 19.63 ? 1125 SER   B N     1 
ATOM   16841 C  CA    . SER   B  1 1127 ? 14.832  65.376  81.226  1.00 19.69 ? 1125 SER   B CA    1 
ATOM   16842 C  C     . SER   B  1 1127 ? 15.715  65.227  79.992  1.00 19.49 ? 1125 SER   B C     1 
ATOM   16843 O  O     . SER   B  1 1127 ? 15.693  64.203  79.308  1.00 18.77 ? 1125 SER   B O     1 
ATOM   16844 C  CB    . SER   B  1 1127 ? 15.678  65.537  82.486  1.00 19.43 ? 1125 SER   B CB    1 
ATOM   16845 O  OG    . SER   B  1 1127 ? 16.563  64.439  82.613  1.00 24.74 ? 1125 SER   B OG    1 
ATOM   16846 N  N     . VAL   B  1 1128 ? 16.474  66.269  79.678  1.00 19.76 ? 1126 VAL   B N     1 
ATOM   16847 C  CA    . VAL   B  1 1128 ? 17.290  66.236  78.472  1.00 19.77 ? 1126 VAL   B CA    1 
ATOM   16848 C  C     . VAL   B  1 1128 ? 18.657  66.827  78.759  1.00 19.83 ? 1126 VAL   B C     1 
ATOM   16849 O  O     . VAL   B  1 1128 ? 18.837  67.628  79.682  1.00 21.67 ? 1126 VAL   B O     1 
ATOM   16850 C  CB    . VAL   B  1 1128 ? 16.650  66.989  77.287  1.00 19.82 ? 1126 VAL   B CB    1 
ATOM   16851 C  CG1   . VAL   B  1 1128 ? 15.267  66.427  76.979  1.00 17.99 ? 1126 VAL   B CG1   1 
ATOM   16852 C  CG2   . VAL   B  1 1128 ? 16.590  68.490  77.574  1.00 22.36 ? 1126 VAL   B CG2   1 
ATOM   16853 N  N     . ALA   B  1 1129 ? 19.621  66.402  77.957  1.00 20.95 ? 1127 ALA   B N     1 
ATOM   16854 C  CA    . ALA   B  1 1129 ? 20.900  67.081  77.813  1.00 18.15 ? 1127 ALA   B CA    1 
ATOM   16855 C  C     . ALA   B  1 1129 ? 21.015  67.414  76.341  1.00 20.88 ? 1127 ALA   B C     1 
ATOM   16856 O  O     . ALA   B  1 1129 ? 20.954  66.513  75.496  1.00 19.56 ? 1127 ALA   B O     1 
ATOM   16857 C  CB    . ALA   B  1 1129 ? 22.059  66.196  78.266  1.00 23.42 ? 1127 ALA   B CB    1 
ATOM   16858 N  N     . ILE   B  1 1130 ? 21.130  68.697  76.032  1.00 19.06 ? 1128 ILE   B N     1 
ATOM   16859 C  CA    . ILE   B  1 1130 ? 21.161  69.162  74.659  1.00 19.43 ? 1128 ILE   B CA    1 
ATOM   16860 C  C     . ILE   B  1 1130 ? 22.605  69.361  74.254  1.00 19.65 ? 1128 ILE   B C     1 
ATOM   16861 O  O     . ILE   B  1 1130 ? 23.376  70.023  74.966  1.00 19.38 ? 1128 ILE   B O     1 
ATOM   16862 C  CB    . ILE   B  1 1130 ? 20.372  70.465  74.482  1.00 22.01 ? 1128 ILE   B CB    1 
ATOM   16863 C  CG1   . ILE   B  1 1130 ? 18.949  70.309  75.041  1.00 19.53 ? 1128 ILE   B CG1   1 
ATOM   16864 C  CG2   . ILE   B  1 1130 ? 20.309  70.820  73.006  1.00 20.82 ? 1128 ILE   B CG2   1 
ATOM   16865 C  CD1   . ILE   B  1 1130 ? 18.217  71.603  75.063  1.00 20.51 ? 1128 ILE   B CD1   1 
ATOM   16866 N  N     . ASP   B  1 1131 ? 22.961  68.807  73.100  1.00 20.98 ? 1129 ASP   B N     1 
ATOM   16867 C  CA    . ASP   B  1 1131 ? 24.301  68.977  72.553  1.00 21.77 ? 1129 ASP   B CA    1 
ATOM   16868 C  C     . ASP   B  1 1131 ? 24.654  70.454  72.422  1.00 23.09 ? 1129 ASP   B C     1 
ATOM   16869 O  O     . ASP   B  1 1131 ? 24.051  71.176  71.622  1.00 22.98 ? 1129 ASP   B O     1 
ATOM   16870 C  CB    . ASP   B  1 1131 ? 24.395  68.283  71.195  1.00 23.75 ? 1129 ASP   B CB    1 
ATOM   16871 C  CG    . ASP   B  1 1131 ? 25.756  68.435  70.569  1.00 24.61 ? 1129 ASP   B CG    1 
ATOM   16872 O  OD1   . ASP   B  1 1131 ? 26.736  68.353  71.331  1.00 22.16 ? 1129 ASP   B OD1   1 
ATOM   16873 O  OD2   . ASP   B  1 1131 ? 25.831  68.620  69.335  1.00 23.11 ? 1129 ASP   B OD2   1 
ATOM   16874 N  N     . ALA   B  1 1132 ? 25.645  70.907  73.195  1.00 24.74 ? 1130 ALA   B N     1 
ATOM   16875 C  CA    . ALA   B  1 1132 ? 26.005  72.323  73.195  1.00 20.89 ? 1130 ALA   B CA    1 
ATOM   16876 C  C     . ALA   B  1 1132 ? 26.596  72.767  71.863  1.00 26.13 ? 1130 ALA   B C     1 
ATOM   16877 O  O     . ALA   B  1 1132 ? 26.490  73.944  71.509  1.00 25.38 ? 1130 ALA   B O     1 
ATOM   16878 C  CB    . ALA   B  1 1132 ? 26.983  72.615  74.333  1.00 24.03 ? 1130 ALA   B CB    1 
ATOM   16879 N  N     . ALA   B  1 1133 ? 27.216  71.852  71.114  1.00 23.80 ? 1131 ALA   B N     1 
ATOM   16880 C  CA    . ALA   B  1 1133 ? 27.795  72.202  69.819  1.00 26.20 ? 1131 ALA   B CA    1 
ATOM   16881 C  C     . ALA   B  1 1133 ? 26.737  72.562  68.789  1.00 27.08 ? 1131 ALA   B C     1 
ATOM   16882 O  O     . ALA   B  1 1133 ? 27.080  73.130  67.746  1.00 28.56 ? 1131 ALA   B O     1 
ATOM   16883 C  CB    . ALA   B  1 1133 ? 28.657  71.050  69.293  1.00 27.67 ? 1131 ALA   B CB    1 
ATOM   16884 N  N     . SER   B  1 1134 ? 25.465  72.251  69.060  1.00 25.46 ? 1132 SER   B N     1 
ATOM   16885 C  CA    . SER   B  1 1134 ? 24.383  72.664  68.173  1.00 24.99 ? 1132 SER   B CA    1 
ATOM   16886 C  C     . SER   B  1 1134 ? 24.329  74.177  68.019  1.00 24.54 ? 1132 SER   B C     1 
ATOM   16887 O  O     . SER   B  1 1134 ? 23.825  74.676  67.010  1.00 26.32 ? 1132 SER   B O     1 
ATOM   16888 C  CB    . SER   B  1 1134 ? 23.042  72.156  68.710  1.00 24.50 ? 1132 SER   B CB    1 
ATOM   16889 O  OG    . SER   B  1 1134 ? 22.765  72.765  69.971  1.00 23.51 ? 1132 SER   B OG    1 
ATOM   16890 N  N     . GLY   B  1 1135 ? 24.823  74.914  69.006  1.00 22.99 ? 1133 GLY   B N     1 
ATOM   16891 C  CA    . GLY   B  1 1135 ? 24.786  76.357  68.982  1.00 27.10 ? 1133 GLY   B CA    1 
ATOM   16892 C  C     . GLY   B  1 1135 ? 23.413  76.957  69.169  1.00 32.24 ? 1133 GLY   B C     1 
ATOM   16893 O  O     . GLY   B  1 1135 ? 23.216  78.130  68.844  1.00 28.53 ? 1133 GLY   B O     1 
ATOM   16894 N  N     . LEU   B  1 1136 ? 22.453  76.188  69.690  1.00 26.89 ? 1134 LEU   B N     1 
ATOM   16895 C  CA    . LEU   B  1 1136 ? 21.057  76.609  69.747  1.00 25.32 ? 1134 LEU   B CA    1 
ATOM   16896 C  C     . LEU   B  1 1136 ? 20.656  77.140  71.118  1.00 27.72 ? 1134 LEU   B C     1 
ATOM   16897 O  O     . LEU   B  1 1136 ? 19.458  77.235  71.412  1.00 28.22 ? 1134 LEU   B O     1 
ATOM   16898 C  CB    . LEU   B  1 1136 ? 20.147  75.447  69.338  1.00 25.12 ? 1134 LEU   B CB    1 
ATOM   16899 C  CG    . LEU   B  1 1136 ? 20.337  74.990  67.895  1.00 24.66 ? 1134 LEU   B CG    1 
ATOM   16900 C  CD1   . LEU   B  1 1136 ? 19.686  73.643  67.640  1.00 24.66 ? 1134 LEU   B CD1   1 
ATOM   16901 C  CD2   . LEU   B  1 1136 ? 19.793  76.044  66.946  1.00 31.22 ? 1134 LEU   B CD2   1 
ATOM   16902 N  N     . GLN   B  1 1137 ? 21.634  77.518  71.948  1.00 29.06 ? 1135 GLN   B N     1 
ATOM   16903 C  CA    . GLN   B  1 1137 ? 21.340  77.943  73.315  1.00 29.52 ? 1135 GLN   B CA    1 
ATOM   16904 C  C     . GLN   B  1 1137 ? 20.341  79.096  73.342  1.00 32.54 ? 1135 GLN   B C     1 
ATOM   16905 O  O     . GLN   B  1 1137 ? 19.455  79.138  74.204  1.00 34.65 ? 1135 GLN   B O     1 
ATOM   16906 C  CB    . GLN   B  1 1137 ? 22.633  78.341  74.032  1.00 32.06 ? 1135 GLN   B CB    1 
ATOM   16907 C  CG    . GLN   B  1 1137 ? 23.540  77.175  74.421  1.00 30.51 ? 1135 GLN   B CG    1 
ATOM   16908 C  CD    . GLN   B  1 1137 ? 24.414  76.698  73.275  1.00 29.88 ? 1135 GLN   B CD    1 
ATOM   16909 O  OE1   . GLN   B  1 1137 ? 24.222  77.084  72.119  1.00 29.91 ? 1135 GLN   B OE1   1 
ATOM   16910 N  NE2   . GLN   B  1 1137 ? 25.387  75.855  73.593  1.00 31.79 ? 1135 GLN   B NE2   1 
ATOM   16911 N  N     . ALA   B  1 1138 ? 20.456  80.033  72.400  1.00 31.55 ? 1136 ALA   B N     1 
ATOM   16912 C  CA    . ALA   B  1 1138 ? 19.551  81.181  72.393  1.00 33.23 ? 1136 ALA   B CA    1 
ATOM   16913 C  C     . ALA   B  1 1138 ? 18.106  80.802  72.094  1.00 35.81 ? 1136 ALA   B C     1 
ATOM   16914 O  O     . ALA   B  1 1138 ? 17.216  81.637  72.283  1.00 35.61 ? 1136 ALA   B O     1 
ATOM   16915 C  CB    . ALA   B  1 1138 ? 20.019  82.221  71.378  1.00 31.75 ? 1136 ALA   B CB    1 
ATOM   16916 N  N     . SER   B  1 1139 ? 17.850  79.577  71.636  1.00 33.49 ? 1137 SER   B N     1 
ATOM   16917 C  CA    . SER   B  1 1139 ? 16.496  79.161  71.294  1.00 31.21 ? 1137 SER   B CA    1 
ATOM   16918 C  C     . SER   B  1 1139 ? 15.655  78.826  72.514  1.00 33.34 ? 1137 SER   B C     1 
ATOM   16919 O  O     . SER   B  1 1139 ? 14.434  78.684  72.383  1.00 33.50 ? 1137 SER   B O     1 
ATOM   16920 C  CB    . SER   B  1 1139 ? 16.537  77.953  70.360  1.00 24.56 ? 1137 SER   B CB    1 
ATOM   16921 O  OG    . SER   B  1 1139 ? 17.018  78.322  69.077  1.00 30.23 ? 1137 SER   B OG    1 
ATOM   16922 N  N     . LEU   B  1 1140 ? 16.270  78.689  73.681  1.00 31.44 ? 1138 LEU   B N     1 
ATOM   16923 C  CA    . LEU   B  1 1140 ? 15.571  78.350  74.911  1.00 35.86 ? 1138 LEU   B CA    1 
ATOM   16924 C  C     . LEU   B  1 1140 ? 15.681  79.490  75.911  1.00 33.24 ? 1138 LEU   B C     1 
ATOM   16925 O  O     . LEU   B  1 1140 ? 15.836  79.281  77.114  1.00 37.37 ? 1138 LEU   B O     1 
ATOM   16926 C  CB    . LEU   B  1 1140 ? 16.100  77.044  75.497  1.00 30.81 ? 1138 LEU   B CB    1 
ATOM   16927 C  CG    . LEU   B  1 1140 ? 15.920  75.843  74.564  1.00 29.88 ? 1138 LEU   B CG    1 
ATOM   16928 C  CD1   . LEU   B  1 1140 ? 16.352  74.556  75.248  1.00 31.03 ? 1138 LEU   B CD1   1 
ATOM   16929 C  CD2   . LEU   B  1 1140 ? 14.479  75.733  74.096  1.00 34.55 ? 1138 LEU   B CD2   1 
ATOM   16930 N  N     . LYS   B  1 1141 ? 15.609  80.718  75.408  1.00 35.69 ? 1139 LYS   B N     1 
ATOM   16931 C  CA    . LYS   B  1 1141 ? 15.646  81.882  76.279  1.00 39.15 ? 1139 LYS   B CA    1 
ATOM   16932 C  C     . LYS   B  1 1141 ? 14.308  82.040  76.990  1.00 40.75 ? 1139 LYS   B C     1 
ATOM   16933 O  O     . LYS   B  1 1141 ? 13.247  81.843  76.396  1.00 43.95 ? 1139 LYS   B O     1 
ATOM   16934 C  CB    . LYS   B  1 1141 ? 15.975  83.139  75.471  1.00 39.06 ? 1139 LYS   B CB    1 
ATOM   16935 N  N     . ASN   B  1 1142 ? 14.368  82.378  78.278  1.00 41.04 ? 1140 ASN   B N     1 
ATOM   16936 C  CA    . ASN   B  1 1142 ? 13.180  82.655  79.088  1.00 42.14 ? 1140 ASN   B CA    1 
ATOM   16937 C  C     . ASN   B  1 1142 ? 12.278  81.429  79.225  1.00 38.99 ? 1140 ASN   B C     1 
ATOM   16938 O  O     . ASN   B  1 1142 ? 11.054  81.556  79.310  1.00 39.24 ? 1140 ASN   B O     1 
ATOM   16939 C  CB    . ASN   B  1 1142 ? 12.386  83.841  78.533  1.00 41.81 ? 1140 ASN   B CB    1 
ATOM   16940 N  N     . LEU   B  1 1143 ? 12.874  80.238  79.240  1.00 40.78 ? 1141 LEU   B N     1 
ATOM   16941 C  CA    . LEU   B  1 1143 ? 12.116  79.029  79.517  1.00 38.66 ? 1141 LEU   B CA    1 
ATOM   16942 C  C     . LEU   B  1 1143 ? 11.444  79.141  80.881  1.00 36.36 ? 1141 LEU   B C     1 
ATOM   16943 O  O     . LEU   B  1 1143 ? 11.998  79.741  81.804  1.00 41.46 ? 1141 LEU   B O     1 
ATOM   16944 C  CB    . LEU   B  1 1143 ? 13.021  77.797  79.522  1.00 36.96 ? 1141 LEU   B CB    1 
ATOM   16945 C  CG    . LEU   B  1 1143 ? 13.216  76.933  78.283  1.00 37.16 ? 1141 LEU   B CG    1 
ATOM   16946 C  CD1   . LEU   B  1 1143 ? 13.910  75.637  78.694  1.00 31.83 ? 1141 LEU   B CD1   1 
ATOM   16947 C  CD2   . LEU   B  1 1143 ? 11.905  76.644  77.580  1.00 28.87 ? 1141 LEU   B CD2   1 
ATOM   16948 N  N     . PRO   B  1 1144 ? 10.256  78.564  81.042  1.00 37.74 ? 1142 PRO   B N     1 
ATOM   16949 C  CA    . PRO   B  1 1144 ? 9.699   78.432  82.388  1.00 35.03 ? 1142 PRO   B CA    1 
ATOM   16950 C  C     . PRO   B  1 1144 ? 10.628  77.593  83.243  1.00 34.21 ? 1142 PRO   B C     1 
ATOM   16951 O  O     . PRO   B  1 1144 ? 11.272  76.656  82.760  1.00 32.28 ? 1142 PRO   B O     1 
ATOM   16952 C  CB    . PRO   B  1 1144 ? 8.355   77.730  82.157  1.00 37.57 ? 1142 PRO   B CB    1 
ATOM   16953 C  CG    . PRO   B  1 1144 ? 8.030   77.998  80.717  1.00 39.67 ? 1142 PRO   B CG    1 
ATOM   16954 C  CD    . PRO   B  1 1144 ? 9.353   78.027  80.011  1.00 37.94 ? 1142 PRO   B CD    1 
ATOM   16955 N  N     . GLN   B  1 1145 ? 10.700  77.948  84.529  1.00 34.19 ? 1143 GLN   B N     1 
ATOM   16956 C  CA    . GLN   B  1 1145 ? 11.549  77.213  85.460  1.00 32.45 ? 1143 GLN   B CA    1 
ATOM   16957 C  C     . GLN   B  1 1145 ? 11.225  75.726  85.466  1.00 33.03 ? 1143 GLN   B C     1 
ATOM   16958 O  O     . GLN   B  1 1145 ? 12.123  74.896  85.642  1.00 28.74 ? 1143 GLN   B O     1 
ATOM   16959 C  CB    . GLN   B  1 1145 ? 11.404  77.796  86.869  1.00 33.53 ? 1143 GLN   B CB    1 
ATOM   16960 N  N     . THR   B  1 1146 ? 9.951   75.369  85.280  1.00 33.67 ? 1144 THR   B N     1 
ATOM   16961 C  CA    . THR   B  1 1146 ? 9.572   73.960  85.242  1.00 33.54 ? 1144 THR   B CA    1 
ATOM   16962 C  C     . THR   B  1 1146 ? 10.265  73.239  84.100  1.00 28.37 ? 1144 THR   B C     1 
ATOM   16963 O  O     . THR   B  1 1146 ? 10.717  72.097  84.258  1.00 32.89 ? 1144 THR   B O     1 
ATOM   16964 C  CB    . THR   B  1 1146 ? 8.058   73.821  85.090  1.00 31.47 ? 1144 THR   B CB    1 
ATOM   16965 O  OG1   . THR   B  1 1146 ? 7.620   74.692  84.044  1.00 33.55 ? 1144 THR   B OG1   1 
ATOM   16966 C  CG2   . THR   B  1 1146 ? 7.352   74.188  86.380  1.00 38.97 ? 1144 THR   B CG2   1 
ATOM   16967 N  N     . VAL   B  1 1147 ? 10.355  73.886  82.939  1.00 26.00 ? 1145 VAL   B N     1 
ATOM   16968 C  CA    . VAL   B  1 1147 ? 11.018  73.256  81.802  1.00 27.16 ? 1145 VAL   B CA    1 
ATOM   16969 C  C     . VAL   B  1 1147 ? 12.530  73.346  81.952  1.00 28.99 ? 1145 VAL   B C     1 
ATOM   16970 O  O     . VAL   B  1 1147 ? 13.248  72.368  81.711  1.00 25.79 ? 1145 VAL   B O     1 
ATOM   16971 C  CB    . VAL   B  1 1147 ? 10.542  73.890  80.480  1.00 26.60 ? 1145 VAL   B CB    1 
ATOM   16972 C  CG1   . VAL   B  1 1147 ? 11.111  73.115  79.291  1.00 26.00 ? 1145 VAL   B CG1   1 
ATOM   16973 C  CG2   . VAL   B  1 1147 ? 9.003   73.936  80.411  1.00 26.59 ? 1145 VAL   B CG2   1 
ATOM   16974 N  N     . GLY   B  1 1148 ? 13.038  74.513  82.354  1.00 27.45 ? 1146 GLY   B N     1 
ATOM   16975 C  CA    . GLY   B  1 1148 ? 14.476  74.666  82.513  1.00 29.05 ? 1146 GLY   B CA    1 
ATOM   16976 C  C     . GLY   B  1 1148 ? 15.082  73.668  83.476  1.00 28.38 ? 1146 GLY   B C     1 
ATOM   16977 O  O     . GLY   B  1 1148 ? 16.221  73.232  83.290  1.00 29.07 ? 1146 GLY   B O     1 
ATOM   16978 N  N     . LEU   B  1 1149 ? 14.335  73.280  84.515  1.00 26.70 ? 1147 LEU   B N     1 
ATOM   16979 C  CA    . LEU   B  1 1149 ? 14.867  72.316  85.468  1.00 25.96 ? 1147 LEU   B CA    1 
ATOM   16980 C  C     . LEU   B  1 1149 ? 15.064  70.948  84.835  1.00 24.13 ? 1147 LEU   B C     1 
ATOM   16981 O  O     . LEU   B  1 1149 ? 15.850  70.146  85.348  1.00 26.36 ? 1147 LEU   B O     1 
ATOM   16982 C  CB    . LEU   B  1 1149 ? 13.952  72.213  86.693  1.00 31.92 ? 1147 LEU   B CB    1 
ATOM   16983 N  N     . ARG   B  1 1150 ? 14.397  70.672  83.723  1.00 23.83 ? 1148 ARG   B N     1 
ATOM   16984 C  CA    . ARG   B  1 1150 ? 14.607  69.424  83.001  1.00 23.40 ? 1148 ARG   B CA    1 
ATOM   16985 C  C     . ARG   B  1 1150 ? 15.657  69.525  81.909  1.00 23.85 ? 1148 ARG   B C     1 
ATOM   16986 O  O     . ARG   B  1 1150 ? 15.909  68.526  81.232  1.00 21.06 ? 1148 ARG   B O     1 
ATOM   16987 C  CB    . ARG   B  1 1150 ? 13.314  68.956  82.352  1.00 23.03 ? 1148 ARG   B CB    1 
ATOM   16988 C  CG    . ARG   B  1 1150 ? 12.291  68.498  83.342  1.00 25.17 ? 1148 ARG   B CG    1 
ATOM   16989 C  CD    . ARG   B  1 1150 ? 11.587  67.355  82.740  1.00 26.60 ? 1148 ARG   B CD    1 
ATOM   16990 N  NE    . ARG   B  1 1150 ? 10.414  66.972  83.506  1.00 24.87 ? 1148 ARG   B NE    1 
ATOM   16991 C  CZ    . ARG   B  1 1150 ? 9.402   66.309  82.976  1.00 24.72 ? 1148 ARG   B CZ    1 
ATOM   16992 N  NH1   . ARG   B  1 1150 ? 9.423   65.935  81.706  1.00 20.48 ? 1148 ARG   B NH1   1 
ATOM   16993 N  NH2   . ARG   B  1 1150 ? 8.343   66.026  83.735  1.00 21.87 ? 1148 ARG   B NH2   1 
ATOM   16994 N  N     . VAL   B  1 1151 ? 16.231  70.702  81.689  1.00 24.88 ? 1149 VAL   B N     1 
ATOM   16995 C  CA    . VAL   B  1 1151 ? 17.092  70.958  80.541  1.00 24.82 ? 1149 VAL   B CA    1 
ATOM   16996 C  C     . VAL   B  1 1151 ? 18.498  71.225  81.043  1.00 27.49 ? 1149 VAL   B C     1 
ATOM   16997 O  O     . VAL   B  1 1151 ? 18.704  72.094  81.896  1.00 27.15 ? 1149 VAL   B O     1 
ATOM   16998 C  CB    . VAL   B  1 1151 ? 16.591  72.148  79.706  1.00 26.45 ? 1149 VAL   B CB    1 
ATOM   16999 C  CG1   . VAL   B  1 1151 ? 17.662  72.572  78.686  1.00 28.11 ? 1149 VAL   B CG1   1 
ATOM   17000 C  CG2   . VAL   B  1 1151 ? 15.277  71.808  79.008  1.00 27.13 ? 1149 VAL   B CG2   1 
ATOM   17001 N  N     . SER   B  1 1152 ? 19.461  70.482  80.512  1.00 25.96 ? 1150 SER   B N     1 
ATOM   17002 C  CA    . SER   B  1 1152 ? 20.865  70.805  80.681  1.00 25.00 ? 1150 SER   B CA    1 
ATOM   17003 C  C     . SER   B  1 1152 ? 21.497  70.849  79.297  1.00 25.14 ? 1150 SER   B C     1 
ATOM   17004 O  O     . SER   B  1 1152 ? 20.911  70.399  78.311  1.00 22.26 ? 1150 SER   B O     1 
ATOM   17005 C  CB    . SER   B  1 1152 ? 21.569  69.798  81.592  1.00 23.82 ? 1150 SER   B CB    1 
ATOM   17006 O  OG    . SER   B  1 1152 ? 21.488  68.497  81.056  1.00 29.13 ? 1150 SER   B OG    1 
ATOM   17007 N  N     . TRP   B  1 1153 ? 22.675  71.448  79.220  1.00 20.29 ? 1151 TRP   B N     1 
ATOM   17008 C  CA    . TRP   B  1 1153 ? 23.433  71.509  77.983  1.00 22.30 ? 1151 TRP   B CA    1 
ATOM   17009 C  C     . TRP   B  1 1153 ? 24.724  70.745  78.203  1.00 24.66 ? 1151 TRP   B C     1 
ATOM   17010 O  O     . TRP   B  1 1153 ? 25.333  70.841  79.274  1.00 22.78 ? 1151 TRP   B O     1 
ATOM   17011 C  CB    . TRP   B  1 1153 ? 23.721  72.952  77.579  1.00 23.28 ? 1151 TRP   B CB    1 
ATOM   17012 C  CG    . TRP   B  1 1153 ? 22.479  73.699  77.181  1.00 26.40 ? 1151 TRP   B CG    1 
ATOM   17013 C  CD1   . TRP   B  1 1153 ? 21.587  74.307  78.014  1.00 25.00 ? 1151 TRP   B CD1   1 
ATOM   17014 C  CD2   . TRP   B  1 1153 ? 21.985  73.895  75.850  1.00 25.70 ? 1151 TRP   B CD2   1 
ATOM   17015 N  NE1   . TRP   B  1 1153 ? 20.571  74.874  77.286  1.00 26.34 ? 1151 TRP   B NE1   1 
ATOM   17016 C  CE2   . TRP   B  1 1153 ? 20.793  74.641  75.955  1.00 29.38 ? 1151 TRP   B CE2   1 
ATOM   17017 C  CE3   . TRP   B  1 1153 ? 22.435  73.520  74.580  1.00 24.34 ? 1151 TRP   B CE3   1 
ATOM   17018 C  CZ2   . TRP   B  1 1153 ? 20.052  75.019  74.841  1.00 28.71 ? 1151 TRP   B CZ2   1 
ATOM   17019 C  CZ3   . TRP   B  1 1153 ? 21.696  73.904  73.471  1.00 24.85 ? 1151 TRP   B CZ3   1 
ATOM   17020 C  CH2   . TRP   B  1 1153 ? 20.515  74.636  73.612  1.00 25.80 ? 1151 TRP   B CH2   1 
ATOM   17021 N  N     . SER   B  1 1154 ? 25.134  69.970  77.203  1.00 21.04 ? 1152 SER   B N     1 
ATOM   17022 C  CA    . SER   B  1 1154 ? 26.305  69.117  77.350  1.00 20.27 ? 1152 SER   B CA    1 
ATOM   17023 C  C     . SER   B  1 1154 ? 27.293  69.387  76.233  1.00 21.47 ? 1152 SER   B C     1 
ATOM   17024 O  O     . SER   B  1 1154 ? 26.944  69.286  75.051  1.00 21.44 ? 1152 SER   B O     1 
ATOM   17025 C  CB    . SER   B  1 1154 ? 25.926  67.640  77.346  1.00 20.53 ? 1152 SER   B CB    1 
ATOM   17026 O  OG    . SER   B  1 1154 ? 27.096  66.861  77.530  1.00 21.92 ? 1152 SER   B OG    1 
ATOM   17027 N  N     . LYS   B  1 1155 ? 28.532  69.692  76.615  1.00 22.64 ? 1153 LYS   B N     1 
ATOM   17028 C  CA    . LYS   B  1 1155 ? 29.656  69.712  75.694  1.00 23.52 ? 1153 LYS   B CA    1 
ATOM   17029 C  C     . LYS   B  1 1155 ? 30.469  68.428  75.763  1.00 26.62 ? 1153 LYS   B C     1 
ATOM   17030 O  O     . LYS   B  1 1155 ? 31.434  68.270  75.006  1.00 33.72 ? 1153 LYS   B O     1 
ATOM   17031 C  CB    . LYS   B  1 1155 ? 30.566  70.913  75.993  1.00 26.85 ? 1153 LYS   B CB    1 
ATOM   17032 N  N     . ASP   B  1 1156 ? 30.100  67.513  76.653  1.00 22.78 ? 1154 ASP   B N     1 
ATOM   17033 C  CA    . ASP   B  1 1156 ? 30.883  66.312  76.954  1.00 21.66 ? 1154 ASP   B CA    1 
ATOM   17034 C  C     . ASP   B  1 1156 ? 29.871  65.212  77.275  1.00 20.26 ? 1154 ASP   B C     1 
ATOM   17035 O  O     . ASP   B  1 1156 ? 29.516  65.004  78.435  1.00 18.83 ? 1154 ASP   B O     1 
ATOM   17036 C  CB    . ASP   B  1 1156 ? 31.830  66.569  78.118  1.00 20.92 ? 1154 ASP   B CB    1 
ATOM   17037 C  CG    . ASP   B  1 1156 ? 32.806  65.430  78.345  1.00 18.32 ? 1154 ASP   B CG    1 
ATOM   17038 O  OD1   . ASP   B  1 1156 ? 32.512  64.290  77.929  1.00 20.20 ? 1154 ASP   B OD1   1 
ATOM   17039 O  OD2   . ASP   B  1 1156 ? 33.864  65.703  78.940  1.00 23.10 ? 1154 ASP   B OD2   1 
ATOM   17040 N  N     . TRP   B  1 1157 ? 29.424  64.505  76.233  1.00 17.26 ? 1155 TRP   B N     1 
ATOM   17041 C  CA    . TRP   B  1 1157 ? 28.329  63.557  76.420  1.00 19.69 ? 1155 TRP   B CA    1 
ATOM   17042 C  C     . TRP   B  1 1157 ? 28.729  62.438  77.363  1.00 20.85 ? 1155 TRP   B C     1 
ATOM   17043 O  O     . TRP   B  1 1157 ? 27.929  62.003  78.196  1.00 20.75 ? 1155 TRP   B O     1 
ATOM   17044 C  CB    . TRP   B  1 1157 ? 27.886  62.973  75.080  1.00 19.22 ? 1155 TRP   B CB    1 
ATOM   17045 C  CG    . TRP   B  1 1157 ? 27.483  63.977  74.051  1.00 18.77 ? 1155 TRP   B CG    1 
ATOM   17046 C  CD1   . TRP   B  1 1157 ? 27.287  65.315  74.228  1.00 18.23 ? 1155 TRP   B CD1   1 
ATOM   17047 C  CD2   . TRP   B  1 1157 ? 27.220  63.710  72.669  1.00 19.78 ? 1155 TRP   B CD2   1 
ATOM   17048 N  NE1   . TRP   B  1 1157 ? 26.923  65.894  73.039  1.00 20.33 ? 1155 TRP   B NE1   1 
ATOM   17049 C  CE2   . TRP   B  1 1157 ? 26.885  64.929  72.066  1.00 19.12 ? 1155 TRP   B CE2   1 
ATOM   17050 C  CE3   . TRP   B  1 1157 ? 27.232  62.550  71.889  1.00 20.69 ? 1155 TRP   B CE3   1 
ATOM   17051 C  CZ2   . TRP   B  1 1157 ? 26.554  65.029  70.713  1.00 20.17 ? 1155 TRP   B CZ2   1 
ATOM   17052 C  CZ3   . TRP   B  1 1157 ? 26.911  62.647  70.556  1.00 23.06 ? 1155 TRP   B CZ3   1 
ATOM   17053 C  CH2   . TRP   B  1 1157 ? 26.572  63.881  69.979  1.00 21.50 ? 1155 TRP   B CH2   1 
ATOM   17054 N  N     . ALA   B  1 1158 ? 29.964  61.949  77.242  1.00 18.64 ? 1156 ALA   B N     1 
ATOM   17055 C  CA    . ALA   B  1 1158 ? 30.377  60.817  78.055  1.00 21.92 ? 1156 ALA   B CA    1 
ATOM   17056 C  C     . ALA   B  1 1158 ? 30.452  61.197  79.528  1.00 20.93 ? 1156 ALA   B C     1 
ATOM   17057 O  O     . ALA   B  1 1158 ? 30.132  60.381  80.395  1.00 22.84 ? 1156 ALA   B O     1 
ATOM   17058 C  CB    . ALA   B  1 1158 ? 31.722  60.279  77.564  1.00 18.48 ? 1156 ALA   B CB    1 
ATOM   17059 N  N     . ALA   B  1 1159 ? 30.873  62.429  79.830  1.00 19.43 ? 1157 ALA   B N     1 
ATOM   17060 C  CA    . ALA   B  1 1159 ? 30.993  62.849  81.219  1.00 21.02 ? 1157 ALA   B CA    1 
ATOM   17061 C  C     . ALA   B  1 1159 ? 29.645  63.204  81.825  1.00 23.90 ? 1157 ALA   B C     1 
ATOM   17062 O  O     . ALA   B  1 1159 ? 29.492  63.141  83.048  1.00 22.71 ? 1157 ALA   B O     1 
ATOM   17063 C  CB    . ALA   B  1 1159 ? 31.929  64.051  81.342  1.00 19.96 ? 1157 ALA   B CB    1 
ATOM   17064 N  N     . ASP   B  1 1160 ? 28.669  63.542  80.994  1.00 21.91 ? 1158 ASP   B N     1 
ATOM   17065 C  CA    . ASP   B  1 1160 ? 27.388  64.071  81.443  1.00 23.91 ? 1158 ASP   B CA    1 
ATOM   17066 C  C     . ASP   B  1 1160 ? 26.284  63.029  81.489  1.00 26.21 ? 1158 ASP   B C     1 
ATOM   17067 O  O     . ASP   B  1 1160 ? 25.159  63.359  81.876  1.00 27.13 ? 1158 ASP   B O     1 
ATOM   17068 C  CB    . ASP   B  1 1160 ? 26.961  65.224  80.534  1.00 21.79 ? 1158 ASP   B CB    1 
ATOM   17069 C  CG    . ASP   B  1 1160 ? 27.826  66.449  80.712  1.00 23.91 ? 1158 ASP   B CG    1 
ATOM   17070 O  OD1   . ASP   B  1 1160 ? 28.579  66.497  81.703  1.00 27.86 ? 1158 ASP   B OD1   1 
ATOM   17071 O  OD2   . ASP   B  1 1160 ? 27.759  67.358  79.859  1.00 23.94 ? 1158 ASP   B OD2   1 
ATOM   17072 N  N     . GLY   B  1 1161 ? 26.562  61.796  81.089  1.00 21.38 ? 1159 GLY   B N     1 
ATOM   17073 C  CA    . GLY   B  1 1161 ? 25.577  60.751  81.162  1.00 21.32 ? 1159 GLY   B CA    1 
ATOM   17074 C  C     . GLY   B  1 1161 ? 25.561  60.087  82.525  1.00 24.29 ? 1159 GLY   B C     1 
ATOM   17075 O  O     . GLY   B  1 1161 ? 26.027  60.646  83.523  1.00 27.04 ? 1159 GLY   B O     1 
ATOM   17076 N  N     . PRO   B  1 1162 ? 25.029  58.862  82.591  1.00 27.98 ? 1160 PRO   B N     1 
ATOM   17077 C  CA    . PRO   B  1 1162 ? 24.502  58.066  81.479  1.00 24.22 ? 1160 PRO   B CA    1 
ATOM   17078 C  C     . PRO   B  1 1162 ? 23.177  58.629  80.987  1.00 23.58 ? 1160 PRO   B C     1 
ATOM   17079 O  O     . PRO   B  1 1162 ? 22.373  59.159  81.753  1.00 23.04 ? 1160 PRO   B O     1 
ATOM   17080 C  CB    . PRO   B  1 1162 ? 24.336  56.675  82.107  1.00 28.08 ? 1160 PRO   B CB    1 
ATOM   17081 C  CG    . PRO   B  1 1162 ? 23.949  56.988  83.531  1.00 26.87 ? 1160 PRO   B CG    1 
ATOM   17082 C  CD    . PRO   B  1 1162 ? 24.779  58.210  83.892  1.00 27.68 ? 1160 PRO   B CD    1 
ATOM   17083 N  N     . PHE   B  1 1163 ? 22.930  58.570  79.691  1.00 17.98 ? 1161 PHE   B N     1 
ATOM   17084 C  CA    . PHE   B  1 1163 ? 21.628  58.932  79.169  1.00 19.50 ? 1161 PHE   B CA    1 
ATOM   17085 C  C     . PHE   B  1 1163 ? 20.800  57.673  78.998  1.00 19.88 ? 1161 PHE   B C     1 
ATOM   17086 O  O     . PHE   B  1 1163 ? 21.281  56.551  79.170  1.00 20.28 ? 1161 PHE   B O     1 
ATOM   17087 C  CB    . PHE   B  1 1163 ? 21.781  59.713  77.862  1.00 17.14 ? 1161 PHE   B CB    1 
ATOM   17088 C  CG    . PHE   B  1 1163 ? 22.700  60.880  77.999  1.00 20.77 ? 1161 PHE   B CG    1 
ATOM   17089 C  CD1   . PHE   B  1 1163 ? 22.346  61.959  78.795  1.00 23.58 ? 1161 PHE   B CD1   1 
ATOM   17090 C  CD2   . PHE   B  1 1163 ? 23.937  60.886  77.384  1.00 22.28 ? 1161 PHE   B CD2   1 
ATOM   17091 C  CE1   . PHE   B  1 1163 ? 23.197  63.024  78.959  1.00 25.77 ? 1161 PHE   B CE1   1 
ATOM   17092 C  CE2   . PHE   B  1 1163 ? 24.785  61.956  77.546  1.00 21.77 ? 1161 PHE   B CE2   1 
ATOM   17093 C  CZ    . PHE   B  1 1163 ? 24.414  63.026  78.333  1.00 21.17 ? 1161 PHE   B CZ    1 
ATOM   17094 N  N     . ALA   B  1 1164 ? 19.525  57.876  78.695  1.00 21.44 ? 1162 ALA   B N     1 
ATOM   17095 C  CA    . ALA   B  1 1164 ? 18.575  56.784  78.572  1.00 22.18 ? 1162 ALA   B CA    1 
ATOM   17096 C  C     . ALA   B  1 1164 ? 18.039  56.674  77.153  1.00 25.96 ? 1162 ALA   B C     1 
ATOM   17097 O  O     . ALA   B  1 1164 ? 17.107  55.903  76.910  1.00 27.01 ? 1162 ALA   B O     1 
ATOM   17098 C  CB    . ALA   B  1 1164 ? 17.431  56.977  79.572  1.00 21.09 ? 1162 ALA   B CB    1 
ATOM   17099 N  N     . GLY   B  1 1165 ? 18.610  57.420  76.221  1.00 19.94 ? 1163 GLY   B N     1 
ATOM   17100 C  CA    . GLY   B  1 1165 ? 18.152  57.437  74.844  1.00 19.45 ? 1163 GLY   B CA    1 
ATOM   17101 C  C     . GLY   B  1 1165 ? 18.709  58.662  74.160  1.00 18.90 ? 1163 GLY   B C     1 
ATOM   17102 O  O     . GLY   B  1 1165 ? 19.319  59.524  74.782  1.00 17.95 ? 1163 GLY   B O     1 
ATOM   17103 N  N     . ALA   B  1 1166 ? 18.505  58.727  72.851  1.00 18.08 ? 1164 ALA   B N     1 
ATOM   17104 C  CA    . ALA   B  1 1166 ? 19.007  59.882  72.136  1.00 18.64 ? 1164 ALA   B CA    1 
ATOM   17105 C  C     . ALA   B  1 1166 ? 18.108  60.177  70.955  1.00 20.43 ? 1164 ALA   B C     1 
ATOM   17106 O  O     . ALA   B  1 1166 ? 17.543  59.273  70.337  1.00 19.83 ? 1164 ALA   B O     1 
ATOM   17107 C  CB    . ALA   B  1 1166 ? 20.454  59.692  71.668  1.00 17.61 ? 1164 ALA   B CB    1 
ATOM   17108 N  N     . LEU   B  1 1167 ? 17.963  61.466  70.678  1.00 18.12 ? 1165 LEU   B N     1 
ATOM   17109 C  CA    . LEU   B  1 1167 ? 17.236  61.968  69.521  1.00 17.12 ? 1165 LEU   B CA    1 
ATOM   17110 C  C     . LEU   B  1 1167 ? 18.206  62.789  68.693  1.00 18.81 ? 1165 LEU   B C     1 
ATOM   17111 O  O     . LEU   B  1 1167 ? 18.872  63.682  69.225  1.00 17.91 ? 1165 LEU   B O     1 
ATOM   17112 C  CB    . LEU   B  1 1167 ? 16.050  62.841  69.950  1.00 17.62 ? 1165 LEU   B CB    1 
ATOM   17113 C  CG    . LEU   B  1 1167 ? 15.002  62.143  70.822  1.00 18.52 ? 1165 LEU   B CG    1 
ATOM   17114 C  CD1   . LEU   B  1 1167 ? 13.895  63.127  71.196  1.00 20.08 ? 1165 LEU   B CD1   1 
ATOM   17115 C  CD2   . LEU   B  1 1167 ? 14.425  60.945  70.071  1.00 19.24 ? 1165 LEU   B CD2   1 
ATOM   17116 N  N     . VAL   B  1 1168 ? 18.277  62.506  67.397  1.00 18.82 ? 1166 VAL   B N     1 
ATOM   17117 C  CA    . VAL   B  1 1168 ? 19.276  63.128  66.538  1.00 20.36 ? 1166 VAL   B CA    1 
ATOM   17118 C  C     . VAL   B  1 1168 ? 18.579  63.716  65.324  1.00 19.28 ? 1166 VAL   B C     1 
ATOM   17119 O  O     . VAL   B  1 1168 ? 17.680  63.094  64.747  1.00 18.85 ? 1166 VAL   B O     1 
ATOM   17120 C  CB    . VAL   B  1 1168 ? 20.366  62.122  66.113  1.00 20.63 ? 1166 VAL   B CB    1 
ATOM   17121 C  CG1   . VAL   B  1 1168 ? 21.471  62.820  65.297  1.00 21.01 ? 1166 VAL   B CG1   1 
ATOM   17122 C  CG2   . VAL   B  1 1168 ? 20.945  61.405  67.340  1.00 19.30 ? 1166 VAL   B CG2   1 
ATOM   17123 N  N     . GLU   B  1 1169 ? 18.973  64.930  64.965  1.00 19.69 ? 1167 GLU   B N     1 
ATOM   17124 C  CA    . GLU   B  1 1169 ? 18.524  65.607  63.758  1.00 19.41 ? 1167 GLU   B CA    1 
ATOM   17125 C  C     . GLU   B  1 1169 ? 19.742  65.877  62.885  1.00 23.92 ? 1167 GLU   B C     1 
ATOM   17126 O  O     . GLU   B  1 1169 ? 20.730  66.435  63.367  1.00 21.39 ? 1167 GLU   B O     1 
ATOM   17127 C  CB    . GLU   B  1 1169 ? 17.827  66.921  64.106  1.00 20.81 ? 1167 GLU   B CB    1 
ATOM   17128 C  CG    . GLU   B  1 1169 ? 17.427  67.750  62.905  1.00 23.35 ? 1167 GLU   B CG    1 
ATOM   17129 C  CD    . GLU   B  1 1169 ? 17.032  69.152  63.298  1.00 20.49 ? 1167 GLU   B CD    1 
ATOM   17130 O  OE1   . GLU   B  1 1169 ? 17.284  69.530  64.461  1.00 24.14 ? 1167 GLU   B OE1   1 
ATOM   17131 O  OE2   . GLU   B  1 1169 ? 16.461  69.875  62.459  1.00 25.10 ? 1167 GLU   B OE2   1 
ATOM   17132 N  N     . GLY   B  1 1170 ? 19.678  65.485  61.618  1.00 22.10 ? 1168 GLY   B N     1 
ATOM   17133 C  CA    . GLY   B  1 1170 ? 20.745  65.808  60.691  1.00 24.91 ? 1168 GLY   B CA    1 
ATOM   17134 C  C     . GLY   B  1 1170 ? 20.562  65.056  59.392  1.00 26.58 ? 1168 GLY   B C     1 
ATOM   17135 O  O     . GLY   B  1 1170 ? 19.632  64.256  59.232  1.00 21.93 ? 1168 GLY   B O     1 
ATOM   17136 N  N     . ASP   B  1 1171 ? 21.471  65.329  58.457  1.00 24.13 ? 1169 ASP   B N     1 
ATOM   17137 C  CA    . ASP   B  1 1171 ? 21.507  64.527  57.249  1.00 26.38 ? 1169 ASP   B CA    1 
ATOM   17138 C  C     . ASP   B  1 1171 ? 22.252  63.225  57.535  1.00 28.90 ? 1169 ASP   B C     1 
ATOM   17139 O  O     . ASP   B  1 1171 ? 22.727  62.984  58.650  1.00 25.74 ? 1169 ASP   B O     1 
ATOM   17140 C  CB    . ASP   B  1 1171 ? 22.123  65.312  56.090  1.00 28.03 ? 1169 ASP   B CB    1 
ATOM   17141 C  CG    . ASP   B  1 1171 ? 23.583  65.710  56.324  1.00 30.96 ? 1169 ASP   B CG    1 
ATOM   17142 O  OD1   . ASP   B  1 1171 ? 24.242  65.232  57.269  1.00 27.80 ? 1169 ASP   B OD1   1 
ATOM   17143 O  OD2   . ASP   B  1 1171 ? 24.086  66.530  55.526  1.00 35.00 ? 1169 ASP   B OD2   1 
ATOM   17144 N  N     . ALA   B  1 1172 ? 22.349  62.375  56.510  1.00 27.98 ? 1170 ALA   B N     1 
ATOM   17145 C  CA    . ALA   B  1 1172 ? 22.939  61.050  56.680  1.00 29.76 ? 1170 ALA   B CA    1 
ATOM   17146 C  C     . ALA   B  1 1172 ? 24.339  61.119  57.291  1.00 25.37 ? 1170 ALA   B C     1 
ATOM   17147 O  O     . ALA   B  1 1172 ? 24.656  60.378  58.230  1.00 24.58 ? 1170 ALA   B O     1 
ATOM   17148 C  CB    . ALA   B  1 1172 ? 22.974  60.322  55.335  1.00 30.70 ? 1170 ALA   B CB    1 
ATOM   17149 N  N     . GLU   B  1 1173 ? 25.197  62.001  56.770  1.00 27.04 ? 1171 GLU   B N     1 
ATOM   17150 C  CA    . GLU   B  1 1173 ? 26.557  62.075  57.295  1.00 24.91 ? 1171 GLU   B CA    1 
ATOM   17151 C  C     . GLU   B  1 1173 ? 26.552  62.492  58.760  1.00 23.70 ? 1171 GLU   B C     1 
ATOM   17152 O  O     . GLU   B  1 1173 ? 27.304  61.940  59.576  1.00 27.56 ? 1171 GLU   B O     1 
ATOM   17153 C  CB    . GLU   B  1 1173 ? 27.407  63.042  56.460  1.00 31.94 ? 1171 GLU   B CB    1 
ATOM   17154 N  N     . ARG   B  1 1174 ? 25.708  63.462  59.115  1.00 24.80 ? 1172 ARG   B N     1 
ATOM   17155 C  CA    . ARG   B  1 1174 ? 25.619  63.895  60.506  1.00 24.03 ? 1172 ARG   B CA    1 
ATOM   17156 C  C     . ARG   B  1 1174 ? 25.116  62.768  61.397  1.00 22.22 ? 1172 ARG   B C     1 
ATOM   17157 O  O     . ARG   B  1 1174 ? 25.661  62.528  62.481  1.00 22.74 ? 1172 ARG   B O     1 
ATOM   17158 C  CB    . ARG   B  1 1174 ? 24.697  65.112  60.612  1.00 26.76 ? 1172 ARG   B CB    1 
ATOM   17159 C  CG    . ARG   B  1 1174 ? 24.437  65.580  62.039  1.00 24.82 ? 1172 ARG   B CG    1 
ATOM   17160 C  CD    . ARG   B  1 1174 ? 25.708  66.097  62.672  1.00 27.96 ? 1172 ARG   B CD    1 
ATOM   17161 N  NE    . ARG   B  1 1174 ? 25.466  66.647  64.000  1.00 28.54 ? 1172 ARG   B NE    1 
ATOM   17162 C  CZ    . ARG   B  1 1174 ? 26.392  66.760  64.941  1.00 26.65 ? 1172 ARG   B CZ    1 
ATOM   17163 N  NH1   . ARG   B  1 1174 ? 27.640  66.353  64.741  1.00 25.54 ? 1172 ARG   B NH1   1 
ATOM   17164 N  NH2   . ARG   B  1 1174 ? 26.056  67.279  66.116  1.00 28.23 ? 1172 ARG   B NH2   1 
ATOM   17165 N  N     . ILE   B  1 1175 ? 24.069  62.076  60.956  1.00 23.26 ? 1173 ILE   B N     1 
ATOM   17166 C  CA    . ILE   B  1 1175 ? 23.515  60.966  61.726  1.00 23.74 ? 1173 ILE   B CA    1 
ATOM   17167 C  C     . ILE   B  1 1175 ? 24.577  59.901  61.963  1.00 23.56 ? 1173 ILE   B C     1 
ATOM   17168 O  O     . ILE   B  1 1175 ? 24.745  59.408  63.084  1.00 20.97 ? 1173 ILE   B O     1 
ATOM   17169 C  CB    . ILE   B  1 1175 ? 22.283  60.387  61.011  1.00 24.19 ? 1173 ILE   B CB    1 
ATOM   17170 C  CG1   . ILE   B  1 1175 ? 21.123  61.392  61.047  1.00 23.70 ? 1173 ILE   B CG1   1 
ATOM   17171 C  CG2   . ILE   B  1 1175 ? 21.877  59.094  61.663  1.00 20.69 ? 1173 ILE   B CG2   1 
ATOM   17172 C  CD1   . ILE   B  1 1175 ? 19.955  60.998  60.167  1.00 24.90 ? 1173 ILE   B CD1   1 
ATOM   17173 N  N     . ARG   B  1 1176 ? 25.319  59.531  60.913  1.00 23.89 ? 1174 ARG   B N     1 
ATOM   17174 C  CA    . ARG   B  1 1176 ? 26.362  58.523  61.086  1.00 21.45 ? 1174 ARG   B CA    1 
ATOM   17175 C  C     . ARG   B  1 1176 ? 27.406  58.987  62.090  1.00 23.45 ? 1174 ARG   B C     1 
ATOM   17176 O  O     . ARG   B  1 1176 ? 27.819  58.220  62.969  1.00 22.13 ? 1174 ARG   B O     1 
ATOM   17177 C  CB    . ARG   B  1 1176 ? 27.029  58.190  59.741  1.00 25.41 ? 1174 ARG   B CB    1 
ATOM   17178 C  CG    . ARG   B  1 1176 ? 27.995  56.997  59.827  1.00 30.42 ? 1174 ARG   B CG    1 
ATOM   17179 C  CD    . ARG   B  1 1176 ? 28.902  56.819  58.590  1.00 31.27 ? 1174 ARG   B CD    1 
ATOM   17180 N  NE    . ARG   B  1 1176 ? 28.250  57.213  57.343  1.00 41.26 ? 1174 ARG   B NE    1 
ATOM   17181 C  CZ    . ARG   B  1 1176 ? 27.515  56.412  56.577  1.00 45.88 ? 1174 ARG   B CZ    1 
ATOM   17182 N  NH1   . ARG   B  1 1176 ? 27.333  55.134  56.880  1.00 41.98 ? 1174 ARG   B NH1   1 
ATOM   17183 N  NH2   . ARG   B  1 1176 ? 26.946  56.905  55.479  1.00 44.37 ? 1174 ARG   B NH2   1 
ATOM   17184 N  N     . ALA   B  1 1177 ? 27.847  60.244  61.975  1.00 23.51 ? 1175 ALA   B N     1 
ATOM   17185 C  CA    . ALA   B  1 1177 ? 28.862  60.754  62.888  1.00 24.27 ? 1175 ALA   B CA    1 
ATOM   17186 C  C     . ALA   B  1 1177 ? 28.356  60.756  64.323  1.00 23.13 ? 1175 ALA   B C     1 
ATOM   17187 O  O     . ALA   B  1 1177 ? 29.077  60.361  65.247  1.00 20.39 ? 1175 ALA   B O     1 
ATOM   17188 C  CB    . ALA   B  1 1177 ? 29.289  62.163  62.467  1.00 19.56 ? 1175 ALA   B CB    1 
ATOM   17189 N  N     . VAL   B  1 1178 ? 27.105  61.174  64.525  1.00 21.55 ? 1176 VAL   B N     1 
ATOM   17190 C  CA    . VAL   B  1 1178 ? 26.550  61.204  65.872  1.00 22.54 ? 1176 VAL   B CA    1 
ATOM   17191 C  C     . VAL   B  1 1178 ? 26.362  59.792  66.392  1.00 21.39 ? 1176 VAL   B C     1 
ATOM   17192 O  O     . VAL   B  1 1178 ? 26.654  59.499  67.554  1.00 22.32 ? 1176 VAL   B O     1 
ATOM   17193 C  CB    . VAL   B  1 1178 ? 25.235  62.008  65.883  1.00 20.08 ? 1176 VAL   B CB    1 
ATOM   17194 C  CG1   . VAL   B  1 1178 ? 24.565  61.931  67.248  1.00 21.62 ? 1176 VAL   B CG1   1 
ATOM   17195 C  CG2   . VAL   B  1 1178 ? 25.522  63.453  65.525  1.00 19.75 ? 1176 VAL   B CG2   1 
ATOM   17196 N  N     . ASN   B  1 1179 ? 25.879  58.892  65.537  1.00 21.77 ? 1177 ASN   B N     1 
ATOM   17197 C  CA    . ASN   B  1 1179 ? 25.651  57.515  65.958  1.00 24.37 ? 1177 ASN   B CA    1 
ATOM   17198 C  C     . ASN   B  1 1179 ? 26.951  56.868  66.402  1.00 23.41 ? 1177 ASN   B C     1 
ATOM   17199 O  O     . ASN   B  1 1179 ? 26.989  56.146  67.409  1.00 22.84 ? 1177 ASN   B O     1 
ATOM   17200 C  CB    . ASN   B  1 1179 ? 25.021  56.727  64.810  1.00 24.01 ? 1177 ASN   B CB    1 
ATOM   17201 C  CG    . ASN   B  1 1179 ? 24.260  55.517  65.282  1.00 26.93 ? 1177 ASN   B CG    1 
ATOM   17202 O  OD1   . ASN   B  1 1179 ? 23.739  55.488  66.397  1.00 25.43 ? 1177 ASN   B OD1   1 
ATOM   17203 N  ND2   . ASN   B  1 1179 ? 24.183  54.506  64.427  1.00 28.35 ? 1177 ASN   B ND2   1 
ATOM   17204 N  N     . LYS   B  1 1180 ? 28.032  57.125  65.664  1.00 21.27 ? 1178 LYS   B N     1 
ATOM   17205 C  CA    . LYS   B  1 1180 ? 29.335  56.602  66.049  1.00 21.19 ? 1178 LYS   B CA    1 
ATOM   17206 C  C     . LYS   B  1 1180 ? 29.787  57.181  67.385  1.00 21.70 ? 1178 LYS   B C     1 
ATOM   17207 O  O     . LYS   B  1 1180 ? 30.346  56.466  68.223  1.00 20.44 ? 1178 LYS   B O     1 
ATOM   17208 C  CB    . LYS   B  1 1180 ? 30.356  56.892  64.945  1.00 21.29 ? 1178 LYS   B CB    1 
ATOM   17209 N  N     . ALA   B  1 1181 ? 29.529  58.469  67.616  1.00 20.61 ? 1179 ALA   B N     1 
ATOM   17210 C  CA    . ALA   B  1 1181 ? 29.923  59.066  68.890  1.00 22.44 ? 1179 ALA   B CA    1 
ATOM   17211 C  C     . ALA   B  1 1181 ? 29.113  58.480  70.036  1.00 21.91 ? 1179 ALA   B C     1 
ATOM   17212 O  O     . ALA   B  1 1181 ? 29.637  58.259  71.140  1.00 21.44 ? 1179 ALA   B O     1 
ATOM   17213 C  CB    . ALA   B  1 1181 ? 29.754  60.583  68.830  1.00 21.72 ? 1179 ALA   B CB    1 
ATOM   17214 N  N     . ILE   B  1 1182 ? 27.831  58.217  69.787  1.00 18.74 ? 1180 ILE   B N     1 
ATOM   17215 C  CA    . ILE   B  1 1182 ? 26.988  57.646  70.823  1.00 20.01 ? 1180 ILE   B CA    1 
ATOM   17216 C  C     . ILE   B  1 1182 ? 27.431  56.231  71.141  1.00 21.71 ? 1180 ILE   B C     1 
ATOM   17217 O  O     . ILE   B  1 1182 ? 27.452  55.823  72.309  1.00 21.66 ? 1180 ILE   B O     1 
ATOM   17218 C  CB    . ILE   B  1 1182 ? 25.516  57.708  70.389  1.00 22.17 ? 1180 ILE   B CB    1 
ATOM   17219 C  CG1   . ILE   B  1 1182 ? 24.994  59.149  70.521  1.00 23.57 ? 1180 ILE   B CG1   1 
ATOM   17220 C  CG2   . ILE   B  1 1182 ? 24.676  56.705  71.174  1.00 23.76 ? 1180 ILE   B CG2   1 
ATOM   17221 C  CD1   . ILE   B  1 1182 ? 23.674  59.387  69.821  1.00 22.31 ? 1180 ILE   B CD1   1 
ATOM   17222 N  N     . ALA   B  1 1183 ? 27.808  55.460  70.114  1.00 23.48 ? 1181 ALA   B N     1 
ATOM   17223 C  CA    . ALA   B  1 1183 ? 28.296  54.105  70.353  1.00 25.13 ? 1181 ALA   B CA    1 
ATOM   17224 C  C     . ALA   B  1 1183 ? 29.567  54.084  71.184  1.00 28.90 ? 1181 ALA   B C     1 
ATOM   17225 O  O     . ALA   B  1 1183 ? 29.854  53.065  71.821  1.00 29.93 ? 1181 ALA   B O     1 
ATOM   17226 C  CB    . ALA   B  1 1183 ? 28.550  53.370  69.036  1.00 27.56 ? 1181 ALA   B CB    1 
ATOM   17227 N  N     . ALA   B  1 1184 ? 30.339  55.173  71.188  1.00 26.83 ? 1182 ALA   B N     1 
ATOM   17228 C  CA    . ALA   B  1 1184 ? 31.538  55.261  72.008  1.00 26.77 ? 1182 ALA   B CA    1 
ATOM   17229 C  C     . ALA   B  1 1184 ? 31.249  55.707  73.433  1.00 25.97 ? 1182 ALA   B C     1 
ATOM   17230 O  O     . ALA   B  1 1184 ? 32.185  55.800  74.234  1.00 25.96 ? 1182 ALA   B O     1 
ATOM   17231 C  CB    . ALA   B  1 1184 ? 32.547  56.214  71.368  1.00 24.65 ? 1182 ALA   B CB    1 
ATOM   17232 N  N     . LEU   B  1 1185 ? 30.000  56.006  73.771  1.00 20.86 ? 1183 LEU   B N     1 
ATOM   17233 C  CA    . LEU   B  1 1185 ? 29.719  56.446  75.127  1.00 22.02 ? 1183 LEU   B CA    1 
ATOM   17234 C  C     . LEU   B  1 1185 ? 29.864  55.269  76.085  1.00 27.43 ? 1183 LEU   B C     1 
ATOM   17235 O  O     . LEU   B  1 1185 ? 29.528  54.135  75.731  1.00 26.76 ? 1183 LEU   B O     1 
ATOM   17236 C  CB    . LEU   B  1 1185 ? 28.310  57.038  75.252  1.00 21.35 ? 1183 LEU   B CB    1 
ATOM   17237 C  CG    . LEU   B  1 1185 ? 28.015  58.317  74.462  1.00 22.64 ? 1183 LEU   B CG    1 
ATOM   17238 C  CD1   . LEU   B  1 1185 ? 26.558  58.766  74.675  1.00 16.71 ? 1183 LEU   B CD1   1 
ATOM   17239 C  CD2   . LEU   B  1 1185 ? 28.984  59.431  74.825  1.00 21.02 ? 1183 LEU   B CD2   1 
ATOM   17240 N  N     . PRO   B  1 1186 ? 30.362  55.504  77.292  1.00 25.26 ? 1184 PRO   B N     1 
ATOM   17241 C  CA    . PRO   B  1 1186 ? 30.440  54.435  78.284  1.00 27.05 ? 1184 PRO   B CA    1 
ATOM   17242 C  C     . PRO   B  1 1186 ? 29.066  54.149  78.867  1.00 23.95 ? 1184 PRO   B C     1 
ATOM   17243 O  O     . PRO   B  1 1186 ? 28.148  54.967  78.805  1.00 26.20 ? 1184 PRO   B O     1 
ATOM   17244 C  CB    . PRO   B  1 1186 ? 31.375  55.013  79.350  1.00 31.28 ? 1184 PRO   B CB    1 
ATOM   17245 C  CG    . PRO   B  1 1186 ? 31.117  56.490  79.287  1.00 27.96 ? 1184 PRO   B CG    1 
ATOM   17246 C  CD    . PRO   B  1 1186 ? 30.814  56.801  77.833  1.00 25.57 ? 1184 PRO   B CD    1 
ATOM   17247 N  N     . GLY   B  1 1187 ? 28.940  52.959  79.441  1.00 27.13 ? 1185 GLY   B N     1 
ATOM   17248 C  CA    . GLY   B  1 1187 ? 27.735  52.594  80.139  1.00 26.93 ? 1185 GLY   B CA    1 
ATOM   17249 C  C     . GLY   B  1 1187 ? 26.689  52.007  79.211  1.00 24.06 ? 1185 GLY   B C     1 
ATOM   17250 O  O     . GLY   B  1 1187 ? 26.983  51.146  78.380  1.00 26.16 ? 1185 GLY   B O     1 
ATOM   17251 N  N     . PRO   B  1 1188 ? 25.453  52.481  79.325  1.00 22.92 ? 1186 PRO   B N     1 
ATOM   17252 C  CA    . PRO   B  1 1188 ? 24.344  51.825  78.618  1.00 28.26 ? 1186 PRO   B CA    1 
ATOM   17253 C  C     . PRO   B  1 1188 ? 24.412  52.065  77.123  1.00 26.21 ? 1186 PRO   B C     1 
ATOM   17254 O  O     . PRO   B  1 1188 ? 24.899  53.099  76.660  1.00 23.89 ? 1186 PRO   B O     1 
ATOM   17255 C  CB    . PRO   B  1 1188 ? 23.100  52.486  79.216  1.00 26.15 ? 1186 PRO   B CB    1 
ATOM   17256 C  CG    . PRO   B  1 1188 ? 23.584  53.853  79.639  1.00 31.83 ? 1186 PRO   B CG    1 
ATOM   17257 C  CD    . PRO   B  1 1188 ? 25.012  53.653  80.097  1.00 27.62 ? 1186 PRO   B CD    1 
ATOM   17258 N  N     . LEU   B  1 1189 ? 23.919  51.082  76.366  1.00 21.13 ? 1187 LEU   B N     1 
ATOM   17259 C  CA    . LEU   B  1 1189 ? 23.742  51.233  74.926  1.00 23.74 ? 1187 LEU   B CA    1 
ATOM   17260 C  C     . LEU   B  1 1189 ? 22.508  52.084  74.678  1.00 26.00 ? 1187 LEU   B C     1 
ATOM   17261 O  O     . LEU   B  1 1189 ? 21.397  51.665  75.015  1.00 24.71 ? 1187 LEU   B O     1 
ATOM   17262 C  CB    . LEU   B  1 1189 ? 23.557  49.880  74.245  1.00 25.07 ? 1187 LEU   B CB    1 
ATOM   17263 C  CG    . LEU   B  1 1189 ? 24.729  48.931  74.119  1.00 31.44 ? 1187 LEU   B CG    1 
ATOM   17264 C  CD1   . LEU   B  1 1189 ? 24.863  48.166  75.403  1.00 38.59 ? 1187 LEU   B CD1   1 
ATOM   17265 C  CD2   . LEU   B  1 1189 ? 24.475  47.989  72.974  1.00 31.18 ? 1187 LEU   B CD2   1 
ATOM   17266 N  N     . LEU   B  1 1190 ? 22.688  53.261  74.089  1.00 22.29 ? 1188 LEU   B N     1 
ATOM   17267 C  CA    . LEU   B  1 1190 ? 21.561  54.163  73.908  1.00 23.39 ? 1188 LEU   B CA    1 
ATOM   17268 C  C     . LEU   B  1 1190 ? 20.703  53.735  72.731  1.00 24.99 ? 1188 LEU   B C     1 
ATOM   17269 O  O     . LEU   B  1 1190 ? 21.210  53.363  71.668  1.00 23.28 ? 1188 LEU   B O     1 
ATOM   17270 C  CB    . LEU   B  1 1190 ? 22.027  55.600  73.687  1.00 20.96 ? 1188 LEU   B CB    1 
ATOM   17271 C  CG    . LEU   B  1 1190 ? 22.814  56.231  74.834  1.00 22.11 ? 1188 LEU   B CG    1 
ATOM   17272 C  CD1   . LEU   B  1 1190 ? 22.851  57.729  74.646  1.00 23.61 ? 1188 LEU   B CD1   1 
ATOM   17273 C  CD2   . LEU   B  1 1190 ? 22.242  55.856  76.191  1.00 23.24 ? 1188 LEU   B CD2   1 
ATOM   17274 N  N     . LEU   B  1 1191 ? 19.390  53.808  72.924  1.00 23.08 ? 1189 LEU   B N     1 
ATOM   17275 C  CA    . LEU   B  1 1191 ? 18.454  53.652  71.822  1.00 22.46 ? 1189 LEU   B CA    1 
ATOM   17276 C  C     . LEU   B  1 1191 ? 18.397  54.985  71.087  1.00 24.97 ? 1189 LEU   B C     1 
ATOM   17277 O  O     . LEU   B  1 1191 ? 17.892  55.976  71.622  1.00 24.09 ? 1189 LEU   B O     1 
ATOM   17278 C  CB    . LEU   B  1 1191 ? 17.084  53.221  72.345  1.00 26.02 ? 1189 LEU   B CB    1 
ATOM   17279 C  CG    . LEU   B  1 1191 ? 16.103  52.600  71.339  1.00 28.09 ? 1189 LEU   B CG    1 
ATOM   17280 C  CD1   . LEU   B  1 1191 ? 14.932  51.973  72.077  1.00 24.91 ? 1189 LEU   B CD1   1 
ATOM   17281 C  CD2   . LEU   B  1 1191 ? 15.594  53.623  70.335  1.00 24.42 ? 1189 LEU   B CD2   1 
ATOM   17282 N  N     . VAL   B  1 1192 ? 18.921  55.015  69.866  1.00 22.23 ? 1190 VAL   B N     1 
ATOM   17283 C  CA    . VAL   B  1 1192 ? 19.054  56.245  69.094  1.00 24.43 ? 1190 VAL   B CA    1 
ATOM   17284 C  C     . VAL   B  1 1192 ? 17.930  56.309  68.073  1.00 24.88 ? 1190 VAL   B C     1 
ATOM   17285 O  O     . VAL   B  1 1192 ? 17.665  55.329  67.367  1.00 27.54 ? 1190 VAL   B O     1 
ATOM   17286 C  CB    . VAL   B  1 1192 ? 20.421  56.322  68.398  1.00 23.62 ? 1190 VAL   B CB    1 
ATOM   17287 C  CG1   . VAL   B  1 1192 ? 20.596  57.674  67.703  1.00 24.22 ? 1190 VAL   B CG1   1 
ATOM   17288 C  CG2   . VAL   B  1 1192 ? 21.550  56.064  69.409  1.00 25.04 ? 1190 VAL   B CG2   1 
ATOM   17289 N  N     . GLN   B  1 1193 ? 17.269  57.457  68.000  1.00 20.55 ? 1191 GLN   B N     1 
ATOM   17290 C  CA    . GLN   B  1 1193 ? 16.333  57.759  66.930  1.00 19.65 ? 1191 GLN   B CA    1 
ATOM   17291 C  C     . GLN   B  1 1193 ? 16.832  58.976  66.185  1.00 19.79 ? 1191 GLN   B C     1 
ATOM   17292 O  O     . GLN   B  1 1193 ? 17.232  59.964  66.805  1.00 21.52 ? 1191 GLN   B O     1 
ATOM   17293 C  CB    . GLN   B  1 1193 ? 14.950  58.060  67.451  1.00 19.46 ? 1191 GLN   B CB    1 
ATOM   17294 C  CG    . GLN   B  1 1193 ? 14.349  56.973  68.256  1.00 21.45 ? 1191 GLN   B CG    1 
ATOM   17295 C  CD    . GLN   B  1 1193 ? 12.922  57.302  68.556  1.00 22.26 ? 1191 GLN   B CD    1 
ATOM   17296 O  OE1   . GLN   B  1 1193 ? 12.072  57.285  67.660  1.00 25.48 ? 1191 GLN   B OE1   1 
ATOM   17297 N  NE2   . GLN   B  1 1193 ? 12.646  57.644  69.806  1.00 21.95 ? 1191 GLN   B NE2   1 
ATOM   17298 N  N     . ALA   B  1 1194 ? 16.782  58.919  64.862  1.00 19.65 ? 1192 ALA   B N     1 
ATOM   17299 C  CA    . ALA   B  1 1194 ? 17.306  60.000  64.044  1.00 21.25 ? 1192 ALA   B CA    1 
ATOM   17300 C  C     . ALA   B  1 1194 ? 16.291  60.391  62.984  1.00 21.93 ? 1192 ALA   B C     1 
ATOM   17301 O  O     . ALA   B  1 1194 ? 15.503  59.562  62.517  1.00 23.61 ? 1192 ALA   B O     1 
ATOM   17302 C  CB    . ALA   B  1 1194 ? 18.625  59.614  63.378  1.00 22.29 ? 1192 ALA   B CB    1 
ATOM   17303 N  N     . ALA   B  1 1195 ? 16.315  61.669  62.624  1.00 20.17 ? 1193 ALA   B N     1 
ATOM   17304 C  CA    . ALA   B  1 1195 ? 15.440  62.210  61.597  1.00 20.91 ? 1193 ALA   B CA    1 
ATOM   17305 C  C     . ALA   B  1 1195 ? 16.138  63.377  60.921  1.00 26.37 ? 1193 ALA   B C     1 
ATOM   17306 O  O     . ALA   B  1 1195 ? 16.932  64.089  61.541  1.00 21.24 ? 1193 ALA   B O     1 
ATOM   17307 C  CB    . ALA   B  1 1195 ? 14.101  62.682  62.174  1.00 24.27 ? 1193 ALA   B CB    1 
ATOM   17308 N  N     . SER   B  1 1196 ? 15.833  63.569  59.642  1.00 25.59 ? 1194 SER   B N     1 
ATOM   17309 C  CA    . SER   B  1 1196 ? 16.287  64.770  58.968  1.00 26.85 ? 1194 SER   B CA    1 
ATOM   17310 C  C     . SER   B  1 1196 ? 15.402  65.944  59.368  1.00 26.25 ? 1194 SER   B C     1 
ATOM   17311 O  O     . SER   B  1 1196 ? 14.284  65.766  59.857  1.00 28.40 ? 1194 SER   B O     1 
ATOM   17312 C  CB    . SER   B  1 1196 ? 16.246  64.581  57.458  1.00 27.62 ? 1194 SER   B CB    1 
ATOM   17313 O  OG    . SER   B  1 1196 ? 14.905  64.414  57.036  1.00 28.72 ? 1194 SER   B OG    1 
ATOM   17314 N  N     . SER   B  1 1197 ? 15.925  67.159  59.178  1.00 25.73 ? 1195 SER   B N     1 
ATOM   17315 C  CA    . SER   B  1 1197 ? 15.110  68.345  59.416  1.00 27.07 ? 1195 SER   B CA    1 
ATOM   17316 C  C     . SER   B  1 1197 ? 13.819  68.276  58.612  1.00 27.41 ? 1195 SER   B C     1 
ATOM   17317 O  O     . SER   B  1 1197 ? 12.751  68.666  59.097  1.00 26.97 ? 1195 SER   B O     1 
ATOM   17318 C  CB    . SER   B  1 1197 ? 15.894  69.610  59.068  1.00 31.19 ? 1195 SER   B CB    1 
ATOM   17319 O  OG    . SER   B  1 1197 ? 17.102  69.688  59.811  1.00 30.01 ? 1195 SER   B OG    1 
ATOM   17320 N  N     . GLY   B  1 1198 ? 13.899  67.759  57.386  1.00 28.41 ? 1196 GLY   B N     1 
ATOM   17321 C  CA    . GLY   B  1 1198 ? 12.709  67.668  56.557  1.00 32.18 ? 1196 GLY   B CA    1 
ATOM   17322 C  C     . GLY   B  1 1198 ? 11.712  66.647  57.070  1.00 30.73 ? 1196 GLY   B C     1 
ATOM   17323 O  O     . GLY   B  1 1198 ? 10.499  66.851  56.970  1.00 34.86 ? 1196 GLY   B O     1 
ATOM   17324 N  N     . GLU   B  1 1199 ? 12.204  65.527  57.610  1.00 30.59 ? 1197 GLU   B N     1 
ATOM   17325 C  CA    . GLU   B  1 1199 ? 11.298  64.533  58.176  1.00 28.56 ? 1197 GLU   B CA    1 
ATOM   17326 C  C     . GLU   B  1 1199 ? 10.591  65.086  59.405  1.00 29.28 ? 1197 GLU   B C     1 
ATOM   17327 O  O     . GLU   B  1 1199 ? 9.399   64.836  59.610  1.00 31.34 ? 1197 GLU   B O     1 
ATOM   17328 C  CB    . GLU   B  1 1199 ? 12.063  63.254  58.525  1.00 31.88 ? 1197 GLU   B CB    1 
ATOM   17329 N  N     . ILE   B  1 1200 ? 11.312  65.843  60.233  1.00 29.03 ? 1198 ILE   B N     1 
ATOM   17330 C  CA    . ILE   B  1 1200 ? 10.702  66.454  61.409  1.00 26.83 ? 1198 ILE   B CA    1 
ATOM   17331 C  C     . ILE   B  1 1200 ? 9.580   67.395  60.992  1.00 31.33 ? 1198 ILE   B C     1 
ATOM   17332 O  O     . ILE   B  1 1200 ? 8.513   67.438  61.619  1.00 30.14 ? 1198 ILE   B O     1 
ATOM   17333 C  CB    . ILE   B  1 1200 ? 11.772  67.187  62.240  1.00 26.44 ? 1198 ILE   B CB    1 
ATOM   17334 C  CG1   . ILE   B  1 1200 ? 12.781  66.189  62.807  1.00 24.67 ? 1198 ILE   B CG1   1 
ATOM   17335 C  CG2   . ILE   B  1 1200 ? 11.129  68.015  63.352  1.00 23.67 ? 1198 ILE   B CG2   1 
ATOM   17336 C  CD1   . ILE   B  1 1200 ? 13.917  66.867  63.550  1.00 22.96 ? 1198 ILE   B CD1   1 
ATOM   17337 N  N     . ALA   B  1 1201 ? 9.798   68.151  59.917  1.00 29.75 ? 1199 ALA   B N     1 
ATOM   17338 C  CA    . ALA   B  1 1201 ? 8.800   69.116  59.463  1.00 29.36 ? 1199 ALA   B CA    1 
ATOM   17339 C  C     . ALA   B  1 1201 ? 7.574   68.427  58.878  1.00 32.97 ? 1199 ALA   B C     1 
ATOM   17340 O  O     . ALA   B  1 1201 ? 6.449   68.912  59.041  1.00 37.36 ? 1199 ALA   B O     1 
ATOM   17341 C  CB    . ALA   B  1 1201 ? 9.419   70.057  58.431  1.00 30.00 ? 1199 ALA   B CB    1 
ATOM   17342 N  N     . ARG   B  1 1202 ? 7.764   67.299  58.195  1.00 34.58 ? 1200 ARG   B N     1 
ATOM   17343 C  CA    . ARG   B  1 1202 ? 6.674   66.701  57.437  1.00 35.22 ? 1200 ARG   B CA    1 
ATOM   17344 C  C     . ARG   B  1 1202 ? 6.028   65.506  58.124  1.00 38.36 ? 1200 ARG   B C     1 
ATOM   17345 O  O     . ARG   B  1 1202 ? 4.880   65.179  57.807  1.00 41.48 ? 1200 ARG   B O     1 
ATOM   17346 C  CB    . ARG   B  1 1202 ? 7.169   66.279  56.047  1.00 34.80 ? 1200 ARG   B CB    1 
ATOM   17347 C  CG    . ARG   B  1 1202 ? 7.767   64.892  55.997  1.00 39.53 ? 1200 ARG   B CG    1 
ATOM   17348 C  CD    . ARG   B  1 1202 ? 8.161   64.510  54.576  1.00 47.72 ? 1200 ARG   B CD    1 
ATOM   17349 N  NE    . ARG   B  1 1202 ? 9.275   65.314  54.088  1.00 41.93 ? 1200 ARG   B NE    1 
ATOM   17350 C  CZ    . ARG   B  1 1202 ? 10.549  64.952  54.162  1.00 43.86 ? 1200 ARG   B CZ    1 
ATOM   17351 N  NH1   . ARG   B  1 1202 ? 10.910  63.788  54.682  1.00 41.94 ? 1200 ARG   B NH1   1 
ATOM   17352 N  NH2   . ARG   B  1 1202 ? 11.484  65.780  53.707  1.00 43.15 ? 1200 ARG   B NH2   1 
ATOM   17353 N  N     . ASN   B  1 1203 ? 6.711   64.862  59.059  1.00 32.63 ? 1201 ASN   B N     1 
ATOM   17354 C  CA    . ASN   B  1 1203 ? 6.203   63.641  59.686  1.00 33.57 ? 1201 ASN   B CA    1 
ATOM   17355 C  C     . ASN   B  1 1203 ? 6.055   63.845  61.187  1.00 34.21 ? 1201 ASN   B C     1 
ATOM   17356 O  O     . ASN   B  1 1203 ? 7.071   63.860  61.911  1.00 30.82 ? 1201 ASN   B O     1 
ATOM   17357 C  CB    . ASN   B  1 1203 ? 7.136   62.467  59.375  1.00 32.40 ? 1201 ASN   B CB    1 
ATOM   17358 C  CG    . ASN   B  1 1203 ? 6.708   61.166  60.050  1.00 33.88 ? 1201 ASN   B CG    1 
ATOM   17359 O  OD1   . ASN   B  1 1203 ? 5.633   61.075  60.652  1.00 35.79 ? 1201 ASN   B OD1   1 
ATOM   17360 N  ND2   . ASN   B  1 1203 ? 7.557   60.150  59.947  1.00 34.83 ? 1201 ASN   B ND2   1 
ATOM   17361 N  N     . PRO   B  1 1204 ? 4.831   63.988  61.703  1.00 31.77 ? 1202 PRO   B N     1 
ATOM   17362 C  CA    . PRO   B  1 1204 ? 4.656   64.153  63.157  1.00 30.58 ? 1202 PRO   B CA    1 
ATOM   17363 C  C     . PRO   B  1 1204 ? 5.199   62.992  63.973  1.00 30.84 ? 1202 PRO   B C     1 
ATOM   17364 O  O     . PRO   B  1 1204 ? 5.482   63.168  65.164  1.00 32.90 ? 1202 PRO   B O     1 
ATOM   17365 C  CB    . PRO   B  1 1204 ? 3.133   64.291  63.316  1.00 35.64 ? 1202 PRO   B CB    1 
ATOM   17366 C  CG    . PRO   B  1 1204 ? 2.553   63.718  62.049  1.00 38.45 ? 1202 PRO   B CG    1 
ATOM   17367 C  CD    . PRO   B  1 1204 ? 3.548   64.016  60.975  1.00 35.95 ? 1202 PRO   B CD    1 
ATOM   17368 N  N     . ASP   B  1 1205 ? 5.363   61.812  63.375  1.00 29.18 ? 1203 ASP   B N     1 
ATOM   17369 C  CA    . ASP   B  1 1205 ? 5.920   60.658  64.066  1.00 29.88 ? 1203 ASP   B CA    1 
ATOM   17370 C  C     . ASP   B  1 1205 ? 7.388   60.440  63.723  1.00 30.78 ? 1203 ASP   B C     1 
ATOM   17371 O  O     . ASP   B  1 1205 ? 7.883   59.311  63.815  1.00 30.38 ? 1203 ASP   B O     1 
ATOM   17372 C  CB    . ASP   B  1 1205 ? 5.105   59.405  63.749  1.00 34.73 ? 1203 ASP   B CB    1 
ATOM   17373 C  CG    . ASP   B  1 1205 ? 3.691   59.470  64.306  1.00 37.34 ? 1203 ASP   B CG    1 
ATOM   17374 O  OD1   . ASP   B  1 1205 ? 3.507   59.989  65.430  1.00 38.73 ? 1203 ASP   B OD1   1 
ATOM   17375 O  OD2   . ASP   B  1 1205 ? 2.766   58.995  63.618  1.00 43.54 ? 1203 ASP   B OD2   1 
ATOM   17376 N  N     . ALA   B  1 1206 ? 8.093   61.503  63.315  1.00 26.86 ? 1204 ALA   B N     1 
ATOM   17377 C  CA    . ALA   B  1 1206 ? 9.510   61.367  62.983  1.00 28.79 ? 1204 ALA   B CA    1 
ATOM   17378 C  C     . ALA   B  1 1206 ? 10.287  60.760  64.144  1.00 25.88 ? 1204 ALA   B C     1 
ATOM   17379 O  O     . ALA   B  1 1206 ? 11.212  59.969  63.934  1.00 25.75 ? 1204 ALA   B O     1 
ATOM   17380 C  CB    . ALA   B  1 1206 ? 10.092  62.725  62.591  1.00 30.15 ? 1204 ALA   B CB    1 
ATOM   17381 N  N     . TYR   B  1 1207 ? 9.920   61.110  65.374  1.00 21.58 ? 1205 TYR   B N     1 
ATOM   17382 C  CA    . TYR   B  1 1207 ? 10.436  60.451  66.566  1.00 23.41 ? 1205 TYR   B CA    1 
ATOM   17383 C  C     . TYR   B  1 1207 ? 9.316   59.661  67.222  1.00 25.48 ? 1205 TYR   B C     1 
ATOM   17384 O  O     . TYR   B  1 1207 ? 8.227   60.193  67.455  1.00 29.12 ? 1205 TYR   B O     1 
ATOM   17385 C  CB    . TYR   B  1 1207 ? 11.018  61.453  67.558  1.00 22.94 ? 1205 TYR   B CB    1 
ATOM   17386 C  CG    . TYR   B  1 1207 ? 12.183  62.226  66.997  1.00 22.01 ? 1205 TYR   B CG    1 
ATOM   17387 C  CD1   . TYR   B  1 1207 ? 13.360  61.578  66.640  1.00 21.10 ? 1205 TYR   B CD1   1 
ATOM   17388 C  CD2   . TYR   B  1 1207 ? 12.106  63.603  66.818  1.00 22.16 ? 1205 TYR   B CD2   1 
ATOM   17389 C  CE1   . TYR   B  1 1207 ? 14.425  62.281  66.120  1.00 19.55 ? 1205 TYR   B CE1   1 
ATOM   17390 C  CE2   . TYR   B  1 1207 ? 13.181  64.318  66.299  1.00 23.93 ? 1205 TYR   B CE2   1 
ATOM   17391 C  CZ    . TYR   B  1 1207 ? 14.331  63.650  65.953  1.00 19.92 ? 1205 TYR   B CZ    1 
ATOM   17392 O  OH    . TYR   B  1 1207 ? 15.402  64.356  65.437  1.00 20.97 ? 1205 TYR   B OH    1 
ATOM   17393 N  N     . CYS   B  1 1208 ? 9.596   58.407  67.534  1.00 22.68 ? 1206 CYS   B N     1 
ATOM   17394 C  CA    . CYS   B  1 1208 ? 8.597   57.506  68.088  1.00 19.30 ? 1206 CYS   B CA    1 
ATOM   17395 C  C     . CYS   B  1 1208 ? 8.633   57.570  69.614  1.00 20.87 ? 1206 CYS   B C     1 
ATOM   17396 O  O     . CYS   B  1 1208 ? 9.672   57.314  70.229  1.00 20.05 ? 1206 CYS   B O     1 
ATOM   17397 C  CB    . CYS   B  1 1208 ? 8.851   56.086  67.602  1.00 23.89 ? 1206 CYS   B CB    1 
ATOM   17398 S  SG    . CYS   B  1 1208 ? 7.609   54.939  68.196  1.00 26.51 ? 1206 CYS   B SG    1 
ATOM   17399 N  N     . LEU   B  1 1209 ? 7.497   57.905  70.228  1.00 19.18 ? 1207 LEU   B N     1 
ATOM   17400 C  CA    . LEU   B  1 1209 ? 7.462   57.998  71.685  1.00 21.64 ? 1207 LEU   B CA    1 
ATOM   17401 C  C     . LEU   B  1 1209 ? 7.543   56.642  72.374  1.00 19.41 ? 1207 LEU   B C     1 
ATOM   17402 O  O     . LEU   B  1 1209 ? 7.769   56.605  73.593  1.00 19.32 ? 1207 LEU   B O     1 
ATOM   17403 C  CB    . LEU   B  1 1209 ? 6.194   58.728  72.144  1.00 16.08 ? 1207 LEU   B CB    1 
ATOM   17404 C  CG    . LEU   B  1 1209 ? 6.054   60.139  71.564  1.00 19.85 ? 1207 LEU   B CG    1 
ATOM   17405 C  CD1   . LEU   B  1 1209 ? 4.858   60.837  72.194  1.00 23.44 ? 1207 LEU   B CD1   1 
ATOM   17406 C  CD2   . LEU   B  1 1209 ? 7.341   60.969  71.756  1.00 21.17 ? 1207 LEU   B CD2   1 
ATOM   17407 N  N     . ASN   B  1 1210 ? 7.360   55.539  71.639  1.00 20.07 ? 1208 ASN   B N     1 
ATOM   17408 C  CA    . ASN   B  1 1210 ? 7.488   54.215  72.248  1.00 21.47 ? 1208 ASN   B CA    1 
ATOM   17409 C  C     . ASN   B  1 1210 ? 8.834   54.051  72.934  1.00 23.93 ? 1208 ASN   B C     1 
ATOM   17410 O  O     . ASN   B  1 1210 ? 8.935   53.416  73.992  1.00 22.95 ? 1208 ASN   B O     1 
ATOM   17411 C  CB    . ASN   B  1 1210 ? 7.341   53.112  71.192  1.00 25.33 ? 1208 ASN   B CB    1 
ATOM   17412 C  CG    . ASN   B  1 1210 ? 5.943   53.006  70.621  1.00 26.32 ? 1208 ASN   B CG    1 
ATOM   17413 O  OD1   . ASN   B  1 1210 ? 5.132   53.919  70.732  1.00 30.96 ? 1208 ASN   B OD1   1 
ATOM   17414 N  ND2   . ASN   B  1 1210 ? 5.669   51.883  69.970  1.00 32.02 ? 1208 ASN   B ND2   1 
ATOM   17415 N  N     . TRP   B  1 1211 ? 9.889   54.602  72.335  1.00 19.99 ? 1209 TRP   B N     1 
ATOM   17416 C  CA    . TRP   B  1 1211 ? 11.250  54.317  72.770  1.00 19.79 ? 1209 TRP   B CA    1 
ATOM   17417 C  C     . TRP   B  1 1211 ? 11.751  55.315  73.795  1.00 22.86 ? 1209 TRP   B C     1 
ATOM   17418 O  O     . TRP   B  1 1211 ? 12.892  55.191  74.251  1.00 24.04 ? 1209 TRP   B O     1 
ATOM   17419 C  CB    . TRP   B  1 1211 ? 12.186  54.291  71.559  1.00 21.15 ? 1209 TRP   B CB    1 
ATOM   17420 C  CG    . TRP   B  1 1211 ? 11.550  53.623  70.383  1.00 24.05 ? 1209 TRP   B CG    1 
ATOM   17421 C  CD1   . TRP   B  1 1211 ? 11.410  54.130  69.123  1.00 25.41 ? 1209 TRP   B CD1   1 
ATOM   17422 C  CD2   . TRP   B  1 1211 ? 10.919  52.338  70.371  1.00 24.02 ? 1209 TRP   B CD2   1 
ATOM   17423 N  NE1   . TRP   B  1 1211 ? 10.751  53.228  68.318  1.00 23.23 ? 1209 TRP   B NE1   1 
ATOM   17424 C  CE2   . TRP   B  1 1211 ? 10.438  52.121  69.060  1.00 24.76 ? 1209 TRP   B CE2   1 
ATOM   17425 C  CE3   . TRP   B  1 1211 ? 10.724  51.343  71.337  1.00 23.22 ? 1209 TRP   B CE3   1 
ATOM   17426 C  CZ2   . TRP   B  1 1211 ? 9.766   50.953  68.693  1.00 25.94 ? 1209 TRP   B CZ2   1 
ATOM   17427 C  CZ3   . TRP   B  1 1211 ? 10.066  50.179  70.970  1.00 22.43 ? 1209 TRP   B CZ3   1 
ATOM   17428 C  CH2   . TRP   B  1 1211 ? 9.585   49.998  69.660  1.00 25.37 ? 1209 TRP   B CH2   1 
ATOM   17429 N  N     . LEU   B  1 1212 ? 10.922  56.288  74.162  1.00 18.10 ? 1210 LEU   B N     1 
ATOM   17430 C  CA    . LEU   B  1 1212 ? 11.259  57.317  75.135  1.00 17.12 ? 1210 LEU   B CA    1 
ATOM   17431 C  C     . LEU   B  1 1212 ? 10.625  57.069  76.495  1.00 17.90 ? 1210 LEU   B C     1 
ATOM   17432 O  O     . LEU   B  1 1212 ? 10.782  57.893  77.399  1.00 20.03 ? 1210 LEU   B O     1 
ATOM   17433 C  CB    . LEU   B  1 1212 ? 10.842  58.692  74.596  1.00 17.08 ? 1210 LEU   B CB    1 
ATOM   17434 C  CG    . LEU   B  1 1212 ? 11.703  59.127  73.400  1.00 19.32 ? 1210 LEU   B CG    1 
ATOM   17435 C  CD1   . LEU   B  1 1212 ? 11.082  60.315  72.661  1.00 20.44 ? 1210 LEU   B CD1   1 
ATOM   17436 C  CD2   . LEU   B  1 1212 ? 13.121  59.451  73.868  1.00 20.13 ? 1210 LEU   B CD2   1 
ATOM   17437 N  N     . VAL   B  1 1213 ? 9.912   55.958  76.665  1.00 20.81 ? 1211 VAL   B N     1 
ATOM   17438 C  CA    . VAL   B  1 1213 ? 9.437   55.542  77.976  1.00 19.05 ? 1211 VAL   B CA    1 
ATOM   17439 C  C     . VAL   B  1 1213 ? 10.166  54.263  78.345  1.00 18.39 ? 1211 VAL   B C     1 
ATOM   17440 O  O     . VAL   B  1 1213 ? 10.759  53.581  77.502  1.00 20.26 ? 1211 VAL   B O     1 
ATOM   17441 C  CB    . VAL   B  1 1213 ? 7.913   55.322  78.023  1.00 18.08 ? 1211 VAL   B CB    1 
ATOM   17442 C  CG1   . VAL   B  1 1213 ? 7.163   56.650  77.847  1.00 17.30 ? 1211 VAL   B CG1   1 
ATOM   17443 C  CG2   . VAL   B  1 1213 ? 7.505   54.317  76.949  1.00 18.55 ? 1211 VAL   B CG2   1 
ATOM   17444 N  N     . GLU   B  1 1214 ? 10.134  53.948  79.629  1.00 20.69 ? 1212 GLU   B N     1 
ATOM   17445 C  CA    . GLU   B  1 1214 ? 10.725  52.720  80.139  1.00 23.41 ? 1212 GLU   B CA    1 
ATOM   17446 C  C     . GLU   B  1 1214 ? 9.620   51.808  80.645  1.00 17.99 ? 1212 GLU   B C     1 
ATOM   17447 O  O     . GLU   B  1 1214 ? 8.763   52.231  81.428  1.00 18.27 ? 1212 GLU   B O     1 
ATOM   17448 C  CB    . GLU   B  1 1214 ? 11.708  52.998  81.265  1.00 22.55 ? 1212 GLU   B CB    1 
ATOM   17449 C  CG    . GLU   B  1 1214 ? 12.235  51.716  81.900  1.00 27.57 ? 1212 GLU   B CG    1 
ATOM   17450 C  CD    . GLU   B  1 1214 ? 13.224  51.983  83.008  1.00 38.00 ? 1212 GLU   B CD    1 
ATOM   17451 O  OE1   . GLU   B  1 1214 ? 14.105  52.840  82.801  1.00 39.92 ? 1212 GLU   B OE1   1 
ATOM   17452 O  OE2   . GLU   B  1 1214 ? 13.121  51.339  84.079  1.00 49.32 ? 1212 GLU   B OE2   1 
ATOM   17453 N  N     . GLU   B  1 1215 ? 9.645   50.564  80.198  1.00 18.57 ? 1213 GLU   B N     1 
ATOM   17454 C  CA    . GLU   B  1 1215 ? 8.686   49.587  80.679  1.00 14.18 ? 1213 GLU   B CA    1 
ATOM   17455 C  C     . GLU   B  1 1215 ? 9.165   48.998  81.992  1.00 17.09 ? 1213 GLU   B C     1 
ATOM   17456 O  O     . GLU   B  1 1215 ? 10.350  48.696  82.156  1.00 16.43 ? 1213 GLU   B O     1 
ATOM   17457 C  CB    . GLU   B  1 1215 ? 8.523   48.467  79.665  1.00 17.86 ? 1213 GLU   B CB    1 
ATOM   17458 C  CG    . GLU   B  1 1215 ? 8.300   48.927  78.265  1.00 21.13 ? 1213 GLU   B CG    1 
ATOM   17459 C  CD    . GLU   B  1 1215 ? 8.481   47.778  77.307  1.00 18.66 ? 1213 GLU   B CD    1 
ATOM   17460 O  OE1   . GLU   B  1 1215 ? 7.517   47.013  77.105  1.00 17.83 ? 1213 GLU   B OE1   1 
ATOM   17461 O  OE2   . GLU   B  1 1215 ? 9.602   47.623  76.797  1.00 20.57 ? 1213 GLU   B OE2   1 
ATOM   17462 N  N     . VAL   B  1 1216 ? 8.233   48.805  82.915  1.00 16.80 ? 1214 VAL   B N     1 
ATOM   17463 C  CA    . VAL   B  1 1216 ? 8.527   48.149  84.180  1.00 16.13 ? 1214 VAL   B CA    1 
ATOM   17464 C  C     . VAL   B  1 1216 ? 7.480   47.076  84.397  1.00 15.13 ? 1214 VAL   B C     1 
ATOM   17465 O  O     . VAL   B  1 1216 ? 6.282   47.343  84.302  1.00 17.76 ? 1214 VAL   B O     1 
ATOM   17466 C  CB    . VAL   B  1 1216 ? 8.554   49.137  85.355  1.00 17.84 ? 1214 VAL   B CB    1 
ATOM   17467 C  CG1   . VAL   B  1 1216 ? 8.728   48.388  86.678  1.00 18.55 ? 1214 VAL   B CG1   1 
ATOM   17468 C  CG2   . VAL   B  1 1216 ? 9.693   50.136  85.147  1.00 18.57 ? 1214 VAL   B CG2   1 
ATOM   17469 N  N     . SER   B  1 1217 ? 7.938   45.862  84.645  1.00 15.22 ? 1215 SER   B N     1 
ATOM   17470 C  CA    . SER   B  1 1217 ? 7.081   44.747  84.994  1.00 15.06 ? 1215 SER   B CA    1 
ATOM   17471 C  C     . SER   B  1 1217 ? 7.236   44.484  86.482  1.00 15.82 ? 1215 SER   B C     1 
ATOM   17472 O  O     . SER   B  1 1217 ? 8.354   44.512  87.010  1.00 14.81 ? 1215 SER   B O     1 
ATOM   17473 C  CB    . SER   B  1 1217 ? 7.461   43.497  84.195  1.00 16.02 ? 1215 SER   B CB    1 
ATOM   17474 O  OG    . SER   B  1 1217 ? 6.964   42.322  84.824  1.00 20.21 ? 1215 SER   B OG    1 
ATOM   17475 N  N     . ALA   B  1 1218 ? 6.113   44.256  87.159  1.00 15.25 ? 1216 ALA   B N     1 
ATOM   17476 C  CA    . ALA   B  1 1218 ? 6.124   43.926  88.578  1.00 16.85 ? 1216 ALA   B CA    1 
ATOM   17477 C  C     . ALA   B  1 1218 ? 5.212   42.732  88.785  1.00 18.45 ? 1216 ALA   B C     1 
ATOM   17478 O  O     . ALA   B  1 1218 ? 4.053   42.760  88.370  1.00 16.90 ? 1216 ALA   B O     1 
ATOM   17479 C  CB    . ALA   B  1 1218 ? 5.665   45.111  89.444  1.00 17.34 ? 1216 ALA   B CB    1 
ATOM   17480 N  N     . SER   B  1 1219 ? 5.735   41.678  89.408  1.00 15.27 ? 1217 SER   B N     1 
ATOM   17481 C  CA    . SER   B  1 1219 ? 4.948   40.481  89.663  1.00 14.38 ? 1217 SER   B CA    1 
ATOM   17482 C  C     . SER   B  1 1219 ? 4.859   40.311  91.167  1.00 15.21 ? 1217 SER   B C     1 
ATOM   17483 O  O     . SER   B  1 1219 ? 5.884   40.148  91.828  1.00 15.21 ? 1217 SER   B O     1 
ATOM   17484 C  CB    . SER   B  1 1219 ? 5.587   39.246  89.031  1.00 15.98 ? 1217 SER   B CB    1 
ATOM   17485 O  OG    . SER   B  1 1219 ? 4.778   38.105  89.280  1.00 19.00 ? 1217 SER   B OG    1 
ATOM   17486 N  N     . ILE   B  1 1220 ? 3.644   40.348  91.703  1.00 16.86 ? 1218 ILE   B N     1 
ATOM   17487 C  CA    . ILE   B  1 1220 ? 3.434   40.270  93.141  1.00 18.45 ? 1218 ILE   B CA    1 
ATOM   17488 C  C     . ILE   B  1 1220 ? 2.713   38.966  93.431  1.00 18.66 ? 1218 ILE   B C     1 
ATOM   17489 O  O     . ILE   B  1 1220 ? 1.628   38.717  92.894  1.00 18.60 ? 1218 ILE   B O     1 
ATOM   17490 C  CB    . ILE   B  1 1220 ? 2.621   41.459  93.671  1.00 21.04 ? 1218 ILE   B CB    1 
ATOM   17491 C  CG1   . ILE   B  1 1220 ? 3.340   42.774  93.372  1.00 25.42 ? 1218 ILE   B CG1   1 
ATOM   17492 C  CG2   . ILE   B  1 1220 ? 2.368   41.285  95.178  1.00 23.88 ? 1218 ILE   B CG2   1 
ATOM   17493 C  CD1   . ILE   B  1 1220 ? 2.812   43.504  92.164  1.00 30.53 ? 1218 ILE   B CD1   1 
ATOM   17494 N  N     . ASN   B  1 1221 ? 3.314   38.147  94.286  1.00 18.43 ? 1219 ASN   B N     1 
ATOM   17495 C  CA    . ASN   B  1 1221 ? 2.683   36.936  94.796  1.00 17.88 ? 1219 ASN   B CA    1 
ATOM   17496 C  C     . ASN   B  1 1221 ? 1.672   37.333  95.866  1.00 19.76 ? 1219 ASN   B C     1 
ATOM   17497 O  O     . ASN   B  1 1221 ? 2.058   37.721  96.970  1.00 22.43 ? 1219 ASN   B O     1 
ATOM   17498 C  CB    . ASN   B  1 1221 ? 3.757   36.005  95.360  1.00 16.21 ? 1219 ASN   B CB    1 
ATOM   17499 C  CG    . ASN   B  1 1221 ? 3.184   34.721  95.938  1.00 22.14 ? 1219 ASN   B CG    1 
ATOM   17500 O  OD1   . ASN   B  1 1221 ? 1.985   34.444  95.814  1.00 19.72 ? 1219 ASN   B OD1   1 
ATOM   17501 N  ND2   . ASN   B  1 1221 ? 4.046   33.921  96.561  1.00 21.21 ? 1219 ASN   B ND2   1 
ATOM   17502 N  N     . THR   B  1 1222 ? 0.386   37.225  95.547  1.00 19.27 ? 1220 THR   B N     1 
ATOM   17503 C  CA    . THR   B  1 1222 ? -0.686  37.599  96.460  1.00 21.55 ? 1220 THR   B CA    1 
ATOM   17504 C  C     . THR   B  1 1222 ? -1.227  36.399  97.222  1.00 24.22 ? 1220 THR   B C     1 
ATOM   17505 O  O     . THR   B  1 1222 ? -2.245  36.512  97.922  1.00 28.14 ? 1220 THR   B O     1 
ATOM   17506 C  CB    . THR   B  1 1222 ? -1.804  38.303  95.695  1.00 24.69 ? 1220 THR   B CB    1 
ATOM   17507 O  OG1   . THR   B  1 1222 ? -2.346  37.431  94.691  1.00 25.07 ? 1220 THR   B OG1   1 
ATOM   17508 C  CG2   . THR   B  1 1222 ? -1.261  39.550  95.017  1.00 25.11 ? 1220 THR   B CG2   1 
ATOM   17509 N  N     . ALA   B  1 1223 ? -0.579  35.254  97.084  1.00 22.67 ? 1221 ALA   B N     1 
ATOM   17510 C  CA    . ALA   B  1 1223 ? -0.884  34.090  97.896  1.00 28.86 ? 1221 ALA   B CA    1 
ATOM   17511 C  C     . ALA   B  1 1223 ? 0.013   34.117  99.131  1.00 33.62 ? 1221 ALA   B C     1 
ATOM   17512 O  O     . ALA   B  1 1223 ? -0.011  33.192  99.933  1.00 43.17 ? 1221 ALA   B O     1 
ATOM   17513 C  CB    . ALA   B  1 1223 ? -0.679  32.813  97.106  1.00 26.78 ? 1221 ALA   B CB    1 
HETATM 17514 P  PA    . FAD   C  2 .    ? -37.436 43.685  82.340  1.00 24.34 ? 2001 FAD   A PA    1 
HETATM 17515 O  O1A   . FAD   C  2 .    ? -35.971 43.235  82.168  1.00 26.38 ? 2001 FAD   A O1A   1 
HETATM 17516 O  O2A   . FAD   C  2 .    ? -38.425 42.710  82.714  1.00 24.04 ? 2001 FAD   A O2A   1 
HETATM 17517 O  O5B   . FAD   C  2 .    ? -37.679 44.699  83.391  1.00 22.38 ? 2001 FAD   A O5B   1 
HETATM 17518 C  C5B   . FAD   C  2 .    ? -36.672 45.684  83.604  1.00 20.08 ? 2001 FAD   A C5B   1 
HETATM 17519 C  C4B   . FAD   C  2 .    ? -37.169 46.759  84.561  1.00 21.64 ? 2001 FAD   A C4B   1 
HETATM 17520 O  O4B   . FAD   C  2 .    ? -37.162 46.299  85.877  1.00 20.35 ? 2001 FAD   A O4B   1 
HETATM 17521 C  C3B   . FAD   C  2 .    ? -36.332 48.007  84.571  1.00 22.73 ? 2001 FAD   A C3B   1 
HETATM 17522 O  O3B   . FAD   C  2 .    ? -36.530 48.854  83.493  1.00 22.14 ? 2001 FAD   A O3B   1 
HETATM 17523 C  C2B   . FAD   C  2 .    ? -36.783 48.615  85.844  1.00 19.49 ? 2001 FAD   A C2B   1 
HETATM 17524 O  O2B   . FAD   C  2 .    ? -38.021 49.228  85.735  1.00 20.60 ? 2001 FAD   A O2B   1 
HETATM 17525 C  C1B   . FAD   C  2 .    ? -36.956 47.406  86.697  1.00 20.57 ? 2001 FAD   A C1B   1 
HETATM 17526 N  N9A   . FAD   C  2 .    ? -35.840 47.133  87.550  1.00 23.07 ? 2001 FAD   A N9A   1 
HETATM 17527 C  C8A   . FAD   C  2 .    ? -34.553 46.779  87.194  1.00 23.81 ? 2001 FAD   A C8A   1 
HETATM 17528 N  N7A   . FAD   C  2 .    ? -33.819 46.612  88.304  1.00 23.70 ? 2001 FAD   A N7A   1 
HETATM 17529 C  C5A   . FAD   C  2 .    ? -34.618 46.859  89.416  1.00 20.31 ? 2001 FAD   A C5A   1 
HETATM 17530 C  C6A   . FAD   C  2 .    ? -34.436 46.845  90.784  1.00 20.32 ? 2001 FAD   A C6A   1 
HETATM 17531 N  N6A   . FAD   C  2 .    ? -33.161 46.512  91.358  1.00 18.78 ? 2001 FAD   A N6A   1 
HETATM 17532 N  N1A   . FAD   C  2 .    ? -35.467 47.139  91.589  1.00 20.63 ? 2001 FAD   A N1A   1 
HETATM 17533 C  C2A   . FAD   C  2 .    ? -36.698 47.448  91.124  1.00 19.09 ? 2001 FAD   A C2A   1 
HETATM 17534 N  N3A   . FAD   C  2 .    ? -36.912 47.479  89.792  1.00 22.03 ? 2001 FAD   A N3A   1 
HETATM 17535 C  C4A   . FAD   C  2 .    ? -35.910 47.195  88.945  1.00 20.59 ? 2001 FAD   A C4A   1 
HETATM 17536 N  N1    . FAD   C  2 .    ? -40.845 53.760  81.325  1.00 19.74 ? 2001 FAD   A N1    1 
HETATM 17537 C  C2    . FAD   C  2 .    ? -41.105 55.004  81.955  1.00 16.04 ? 2001 FAD   A C2    1 
HETATM 17538 O  O2    . FAD   C  2 .    ? -40.528 55.230  83.125  1.00 17.07 ? 2001 FAD   A O2    1 
HETATM 17539 N  N3    . FAD   C  2 .    ? -41.933 55.943  81.393  1.00 16.67 ? 2001 FAD   A N3    1 
HETATM 17540 C  C4    . FAD   C  2 .    ? -42.505 55.676  80.172  1.00 18.23 ? 2001 FAD   A C4    1 
HETATM 17541 O  O4    . FAD   C  2 .    ? -43.342 56.597  79.646  1.00 18.20 ? 2001 FAD   A O4    1 
HETATM 17542 C  C4X   . FAD   C  2 .    ? -42.271 54.389  79.461  1.00 18.28 ? 2001 FAD   A C4X   1 
HETATM 17543 N  N5    . FAD   C  2 .    ? -42.847 54.058  78.240  1.00 19.29 ? 2001 FAD   A N5    1 
HETATM 17544 C  C5X   . FAD   C  2 .    ? -42.608 52.813  77.666  1.00 19.29 ? 2001 FAD   A C5X   1 
HETATM 17545 C  C6    . FAD   C  2 .    ? -43.200 52.470  76.440  1.00 18.62 ? 2001 FAD   A C6    1 
HETATM 17546 C  C7    . FAD   C  2 .    ? -42.945 51.222  75.885  1.00 19.71 ? 2001 FAD   A C7    1 
HETATM 17547 C  C7M   . FAD   C  2 .    ? -43.577 50.843  74.575  1.00 22.77 ? 2001 FAD   A C7M   1 
HETATM 17548 C  C8    . FAD   C  2 .    ? -42.107 50.315  76.521  1.00 21.42 ? 2001 FAD   A C8    1 
HETATM 17549 C  C8M   . FAD   C  2 .    ? -41.829 48.969  75.925  1.00 20.52 ? 2001 FAD   A C8M   1 
HETATM 17550 C  C9    . FAD   C  2 .    ? -41.517 50.639  77.740  1.00 22.86 ? 2001 FAD   A C9    1 
HETATM 17551 C  C9A   . FAD   C  2 .    ? -41.772 51.889  78.303  1.00 23.12 ? 2001 FAD   A C9A   1 
HETATM 17552 N  N10   . FAD   C  2 .    ? -41.158 52.214  79.540  1.00 24.15 ? 2001 FAD   A N10   1 
HETATM 17553 C  C10   . FAD   C  2 .    ? -41.411 53.455  80.124  1.00 18.17 ? 2001 FAD   A C10   1 
HETATM 17554 C  "C1'" . FAD   C  2 .    ? -40.341 51.199  80.262  1.00 25.00 ? 2001 FAD   A "C1'" 1 
HETATM 17555 C  "C2'" . FAD   C  2 .    ? -38.846 51.337  80.333  1.00 26.03 ? 2001 FAD   A "C2'" 1 
HETATM 17556 O  "O2'" . FAD   C  2 .    ? -38.440 52.160  79.325  1.00 25.58 ? 2001 FAD   A "O2'" 1 
HETATM 17557 C  "C3'" . FAD   C  2 .    ? -38.266 49.916  80.186  1.00 27.92 ? 2001 FAD   A "C3'" 1 
HETATM 17558 O  "O3'" . FAD   C  2 .    ? -38.449 49.472  78.893  1.00 29.73 ? 2001 FAD   A "O3'" 1 
HETATM 17559 C  "C4'" . FAD   C  2 .    ? -38.948 48.852  81.019  1.00 24.92 ? 2001 FAD   A "C4'" 1 
HETATM 17560 O  "O4'" . FAD   C  2 .    ? -38.944 49.195  82.353  1.00 24.91 ? 2001 FAD   A "O4'" 1 
HETATM 17561 C  "C5'" . FAD   C  2 .    ? -38.284 47.497  80.749  1.00 25.14 ? 2001 FAD   A "C5'" 1 
HETATM 17562 O  "O5'" . FAD   C  2 .    ? -39.074 46.519  81.370  1.00 25.34 ? 2001 FAD   A "O5'" 1 
HETATM 17563 P  P     . FAD   C  2 .    ? -39.383 45.044  80.799  1.00 23.72 ? 2001 FAD   A P     1 
HETATM 17564 O  O1P   . FAD   C  2 .    ? -40.720 44.374  81.255  1.00 26.38 ? 2001 FAD   A O1P   1 
HETATM 17565 O  O2P   . FAD   C  2 .    ? -39.197 45.267  79.266  1.00 22.60 ? 2001 FAD   A O2P   1 
HETATM 17566 O  O3P   . FAD   C  2 .    ? -38.013 44.245  81.081  1.00 25.09 ? 2001 FAD   A O3P   1 
HETATM 17567 C  C1    . PGE   D  3 .    ? 2.732   60.047  94.430  1.00 43.26 ? 2002 PGE   A C1    1 
HETATM 17568 O  O1    . PGE   D  3 .    ? 2.447   58.720  94.835  1.00 44.89 ? 2002 PGE   A O1    1 
HETATM 17569 C  C2    . PGE   D  3 .    ? 2.601   60.995  95.602  1.00 36.18 ? 2002 PGE   A C2    1 
HETATM 17570 O  O2    . PGE   D  3 .    ? 1.512   61.875  95.406  1.00 38.68 ? 2002 PGE   A O2    1 
HETATM 17571 C  C3    . PGE   D  3 .    ? 1.131   62.638  96.526  1.00 29.29 ? 2002 PGE   A C3    1 
HETATM 17572 C  C4    . PGE   D  3 .    ? -0.319  63.066  96.530  1.00 25.12 ? 2002 PGE   A C4    1 
HETATM 17573 O  O4    . PGE   D  3 .    ? -3.016  60.197  95.081  1.00 39.63 ? 2002 PGE   A O4    1 
HETATM 17574 C  C6    . PGE   D  3 .    ? -3.278  61.575  95.246  1.00 33.23 ? 2002 PGE   A C6    1 
HETATM 17575 C  C5    . PGE   D  3 .    ? -2.487  62.105  96.431  1.00 30.79 ? 2002 PGE   A C5    1 
HETATM 17576 O  O3    . PGE   D  3 .    ? -1.114  61.972  96.152  1.00 29.20 ? 2002 PGE   A O3    1 
HETATM 17577 C  C     . FMT   E  4 .    ? -66.470 72.450  80.189  1.00 34.29 ? 2003 FMT   A C     1 
HETATM 17578 O  O1    . FMT   E  4 .    ? -65.539 71.683  80.513  1.00 33.45 ? 2003 FMT   A O1    1 
HETATM 17579 O  O2    . FMT   E  4 .    ? -67.668 72.405  80.544  1.00 39.87 ? 2003 FMT   A O2    1 
HETATM 17580 C  C1    . PEG   F  5 .    ? -51.994 76.859  74.011  1.00 29.22 ? 2004 PEG   A C1    1 
HETATM 17581 O  O1    . PEG   F  5 .    ? -52.241 78.183  74.430  1.00 37.93 ? 2004 PEG   A O1    1 
HETATM 17582 C  C2    . PEG   F  5 .    ? -51.182 76.859  72.743  1.00 33.59 ? 2004 PEG   A C2    1 
HETATM 17583 O  O2    . PEG   F  5 .    ? -49.851 76.522  73.033  1.00 35.07 ? 2004 PEG   A O2    1 
HETATM 17584 C  C3    . PEG   F  5 .    ? -48.998 76.513  71.909  1.00 32.38 ? 2004 PEG   A C3    1 
HETATM 17585 C  C4    . PEG   F  5 .    ? -48.004 77.641  71.994  1.00 36.22 ? 2004 PEG   A C4    1 
HETATM 17586 O  O4    . PEG   F  5 .    ? -46.909 77.309  72.830  1.00 41.96 ? 2004 PEG   A O4    1 
HETATM 17587 C  C1    . PGE   G  3 .    ? -30.511 58.662  118.911 1.00 41.20 ? 2005 PGE   A C1    1 
HETATM 17588 O  O1    . PGE   G  3 .    ? -31.108 57.442  119.295 1.00 51.80 ? 2005 PGE   A O1    1 
HETATM 17589 C  C2    . PGE   G  3 .    ? -29.251 58.890  119.705 1.00 41.18 ? 2005 PGE   A C2    1 
HETATM 17590 O  O2    . PGE   G  3 .    ? -29.337 60.154  120.328 1.00 41.85 ? 2005 PGE   A O2    1 
HETATM 17591 C  C3    . PGE   G  3 .    ? -28.228 60.552  121.091 1.00 39.89 ? 2005 PGE   A C3    1 
HETATM 17592 C  C4    . PGE   G  3 .    ? -27.380 59.411  121.615 1.00 42.27 ? 2005 PGE   A C4    1 
HETATM 17593 O  O4    . PGE   G  3 .    ? -28.342 60.527  125.601 1.00 43.35 ? 2005 PGE   A O4    1 
HETATM 17594 C  C6    . PGE   G  3 .    ? -27.306 59.905  124.872 1.00 37.43 ? 2005 PGE   A C6    1 
HETATM 17595 C  C5    . PGE   G  3 .    ? -27.143 60.669  123.570 1.00 37.96 ? 2005 PGE   A C5    1 
HETATM 17596 O  O3    . PGE   G  3 .    ? -26.507 59.852  122.623 1.00 41.83 ? 2005 PGE   A O3    1 
HETATM 17597 O  O1    . PG4   H  6 .    ? -25.789 53.547  113.734 1.00 45.82 ? 2006 PG4   A O1    1 
HETATM 17598 C  C1    . PG4   H  6 .    ? -25.824 54.956  113.759 1.00 37.54 ? 2006 PG4   A C1    1 
HETATM 17599 C  C2    . PG4   H  6 .    ? -24.583 55.478  114.431 1.00 37.28 ? 2006 PG4   A C2    1 
HETATM 17600 O  O2    . PG4   H  6 .    ? -24.869 55.858  115.753 1.00 46.74 ? 2006 PG4   A O2    1 
HETATM 17601 C  C3    . PG4   H  6 .    ? -23.794 56.503  116.389 1.00 37.23 ? 2006 PG4   A C3    1 
HETATM 17602 C  C4    . PG4   H  6 .    ? -23.550 55.883  117.743 1.00 37.81 ? 2006 PG4   A C4    1 
HETATM 17603 O  O3    . PG4   H  6 .    ? -22.372 55.111  117.699 1.00 43.91 ? 2006 PG4   A O3    1 
HETATM 17604 C  C5    . PG4   H  6 .    ? -21.701 55.030  118.935 1.00 36.89 ? 2006 PG4   A C5    1 
HETATM 17605 C  C6    . PG4   H  6 .    ? -20.458 54.179  118.803 1.00 40.79 ? 2006 PG4   A C6    1 
HETATM 17606 O  O4    . PG4   H  6 .    ? -19.524 54.801  117.949 1.00 36.85 ? 2006 PG4   A O4    1 
HETATM 17607 C  C7    . PG4   H  6 .    ? -18.194 54.626  118.358 1.00 36.33 ? 2006 PG4   A C7    1 
HETATM 17608 C  C8    . PG4   H  6 .    ? -17.226 55.040  117.272 1.00 32.91 ? 2006 PG4   A C8    1 
HETATM 17609 O  O5    . PG4   H  6 .    ? -17.421 54.250  116.120 1.00 39.57 ? 2006 PG4   A O5    1 
HETATM 17610 C  C1    . PEG   I  5 .    ? -39.073 80.416  120.433 1.00 42.40 ? 2007 PEG   A C1    1 
HETATM 17611 O  O1    . PEG   I  5 .    ? -39.005 81.751  120.883 1.00 48.79 ? 2007 PEG   A O1    1 
HETATM 17612 C  C2    . PEG   I  5 .    ? -38.410 79.524  121.451 1.00 46.69 ? 2007 PEG   A C2    1 
HETATM 17613 O  O2    . PEG   I  5 .    ? -38.703 78.173  121.182 1.00 50.11 ? 2007 PEG   A O2    1 
HETATM 17614 C  C3    . PEG   I  5 .    ? -38.726 77.366  122.339 1.00 44.61 ? 2007 PEG   A C3    1 
HETATM 17615 C  C4    . PEG   I  5 .    ? -39.148 75.956  121.988 1.00 43.14 ? 2007 PEG   A C4    1 
HETATM 17616 O  O4    . PEG   I  5 .    ? -40.246 75.987  121.094 1.00 52.35 ? 2007 PEG   A O4    1 
HETATM 17617 C  C10   . A1BDA J  7 .    ? -14.101 92.122  112.550 1.00 32.16 ? 2008 A1BDA A C10   1 
HETATM 17618 C  C11   . A1BDA J  7 .    ? -12.784 92.361  112.952 1.00 35.08 ? 2008 A1BDA A C11   1 
HETATM 17619 C  C02   . A1BDA J  7 .    ? -12.190 91.493  113.876 1.00 34.11 ? 2008 A1BDA A C02   1 
HETATM 17620 C  C03   . A1BDA J  7 .    ? -12.913 90.404  114.396 1.00 30.87 ? 2008 A1BDA A C03   1 
HETATM 17621 C  C04   . A1BDA J  7 .    ? -14.216 90.159  113.993 1.00 28.96 ? 2008 A1BDA A C04   1 
HETATM 17622 C  C05   . A1BDA J  7 .    ? -14.808 91.028  113.073 1.00 33.53 ? 2008 A1BDA A C05   1 
HETATM 17623 C  C06   . A1BDA J  7 .    ? -16.202 90.992  112.453 1.00 38.37 ? 2008 A1BDA A C06   1 
HETATM 17624 C  C08   . A1BDA J  7 .    ? -16.278 92.075  111.416 1.00 35.37 ? 2008 A1BDA A C08   1 
HETATM 17625 C  C09   . A1BDA J  7 .    ? -14.999 92.876  111.570 1.00 36.58 ? 2008 A1BDA A C09   1 
HETATM 17626 O  O07   . A1BDA J  7 .    ? -17.046 90.214  112.731 1.00 47.15 ? 2008 A1BDA A O07   1 
HETATM 17627 CL CL01  . A1BDA J  7 .    ? -10.506 91.742  114.418 1.00 39.20 ? 2008 A1BDA A CL01  1 
HETATM 17628 C  C     . FMT   K  4 .    ? -22.246 52.412  103.761 1.00 40.53 ? 2009 FMT   A C     1 
HETATM 17629 O  O1    . FMT   K  4 .    ? -21.536 52.368  104.785 1.00 41.31 ? 2009 FMT   A O1    1 
HETATM 17630 O  O2    . FMT   K  4 .    ? -23.405 51.975  103.595 1.00 43.83 ? 2009 FMT   A O2    1 
HETATM 17631 C  C1    . PEG   L  5 .    ? -43.311 68.424  108.825 1.00 38.10 ? 2010 PEG   A C1    1 
HETATM 17632 O  O1    . PEG   L  5 .    ? -43.621 68.177  107.471 1.00 41.14 ? 2010 PEG   A O1    1 
HETATM 17633 C  C2    . PEG   L  5 .    ? -44.042 69.661  109.288 1.00 31.53 ? 2010 PEG   A C2    1 
HETATM 17634 O  O2    . PEG   L  5 .    ? -44.832 69.406  110.437 1.00 45.52 ? 2010 PEG   A O2    1 
HETATM 17635 C  C3    . PEG   L  5 .    ? -44.092 69.249  111.629 1.00 37.84 ? 2010 PEG   A C3    1 
HETATM 17636 C  C4    . PEG   L  5 .    ? -44.485 70.261  112.676 1.00 39.14 ? 2010 PEG   A C4    1 
HETATM 17637 O  O4    . PEG   L  5 .    ? -43.413 70.507  113.566 1.00 37.82 ? 2010 PEG   A O4    1 
HETATM 17638 S  S     . SO4   M  8 .    ? -12.516 75.752  69.662  0.71 30.73 ? 2011 SO4   A S     1 
HETATM 17639 O  O1    . SO4   M  8 .    ? -12.002 74.487  69.036  0.71 34.44 ? 2011 SO4   A O1    1 
HETATM 17640 O  O2    . SO4   M  8 .    ? -12.939 76.714  68.592  0.71 35.19 ? 2011 SO4   A O2    1 
HETATM 17641 O  O3    . SO4   M  8 .    ? -13.701 75.436  70.524  0.71 26.89 ? 2011 SO4   A O3    1 
HETATM 17642 O  O4    . SO4   M  8 .    ? -11.431 76.340  70.478  0.71 30.17 ? 2011 SO4   A O4    1 
HETATM 17643 S  S     . SO4   N  8 .    ? -9.042  53.246  110.797 1.00 22.53 ? 2012 SO4   A S     1 
HETATM 17644 O  O1    . SO4   N  8 .    ? -7.939  53.566  109.860 1.00 23.82 ? 2012 SO4   A O1    1 
HETATM 17645 O  O2    . SO4   N  8 .    ? -10.016 52.368  110.092 1.00 22.25 ? 2012 SO4   A O2    1 
HETATM 17646 O  O3    . SO4   N  8 .    ? -8.530  52.523  112.001 1.00 20.28 ? 2012 SO4   A O3    1 
HETATM 17647 O  O4    . SO4   N  8 .    ? -9.674  54.531  111.197 1.00 22.97 ? 2012 SO4   A O4    1 
HETATM 17648 S  S     . SO4   O  8 .    ? -69.201 64.744  72.488  0.68 22.24 ? 2013 SO4   A S     1 
HETATM 17649 O  O1    . SO4   O  8 .    ? -67.808 65.157  72.173  0.68 39.42 ? 2013 SO4   A O1    1 
HETATM 17650 O  O2    . SO4   O  8 .    ? -69.678 63.780  71.432  0.68 26.63 ? 2013 SO4   A O2    1 
HETATM 17651 O  O3    . SO4   O  8 .    ? -69.352 64.217  73.874  0.68 21.06 ? 2013 SO4   A O3    1 
HETATM 17652 O  O4    . SO4   O  8 .    ? -70.058 65.975  72.396  0.68 30.19 ? 2013 SO4   A O4    1 
HETATM 17653 S  S     . SO4   P  8 .    ? -21.864 75.121  99.854  0.65 26.74 ? 2014 SO4   A S     1 
HETATM 17654 O  O1    . SO4   P  8 .    ? -20.958 73.941  99.650  0.65 26.83 ? 2014 SO4   A O1    1 
HETATM 17655 O  O2    . SO4   P  8 .    ? -22.509 75.519  98.591  0.65 22.95 ? 2014 SO4   A O2    1 
HETATM 17656 O  O3    . SO4   P  8 .    ? -22.905 74.778  100.876 0.65 32.80 ? 2014 SO4   A O3    1 
HETATM 17657 O  O4    . SO4   P  8 .    ? -21.049 76.292  100.333 0.65 33.29 ? 2014 SO4   A O4    1 
HETATM 17658 S  S     . SO4   Q  8 .    ? 13.108  75.412  125.552 0.82 37.34 ? 2015 SO4   A S     1 
HETATM 17659 O  O1    . SO4   Q  8 .    ? 13.779  75.857  124.281 0.82 40.52 ? 2015 SO4   A O1    1 
HETATM 17660 O  O2    . SO4   Q  8 .    ? 11.677  75.040  125.304 0.82 34.07 ? 2015 SO4   A O2    1 
HETATM 17661 O  O3    . SO4   Q  8 .    ? 13.851  74.212  126.066 0.82 37.41 ? 2015 SO4   A O3    1 
HETATM 17662 O  O4    . SO4   Q  8 .    ? 13.149  76.530  126.549 0.82 49.15 ? 2015 SO4   A O4    1 
HETATM 17663 S  S     . SO4   R  8 .    ? -31.172 68.612  100.521 0.64 27.99 ? 2016 SO4   A S     1 
HETATM 17664 O  O1    . SO4   R  8 .    ? -29.896 69.203  100.980 0.64 35.46 ? 2016 SO4   A O1    1 
HETATM 17665 O  O2    . SO4   R  8 .    ? -30.845 67.738  99.344  0.64 33.80 ? 2016 SO4   A O2    1 
HETATM 17666 O  O3    . SO4   R  8 .    ? -31.823 67.788  101.572 0.64 21.17 ? 2016 SO4   A O3    1 
HETATM 17667 O  O4    . SO4   R  8 .    ? -32.110 69.705  100.093 0.64 29.43 ? 2016 SO4   A O4    1 
HETATM 17668 S  S     . SO4   S  8 .    ? 11.165  89.789  105.732 0.61 34.38 ? 2017 SO4   A S     1 
HETATM 17669 O  O1    . SO4   S  8 .    ? 11.948  91.034  106.017 0.61 42.10 ? 2017 SO4   A O1    1 
HETATM 17670 O  O2    . SO4   S  8 .    ? 10.686  89.811  104.317 0.61 32.17 ? 2017 SO4   A O2    1 
HETATM 17671 O  O3    . SO4   S  8 .    ? 12.061  88.614  105.961 0.61 36.43 ? 2017 SO4   A O3    1 
HETATM 17672 O  O4    . SO4   S  8 .    ? 9.981   89.695  106.649 0.61 36.12 ? 2017 SO4   A O4    1 
HETATM 17673 S  S     . SO4   T  8 .    ? -33.554 25.243  79.538  0.75 43.92 ? 2018 SO4   A S     1 
HETATM 17674 O  O1    . SO4   T  8 .    ? -32.811 26.467  79.086  0.75 42.29 ? 2018 SO4   A O1    1 
HETATM 17675 O  O2    . SO4   T  8 .    ? -34.318 24.679  78.382  0.75 40.12 ? 2018 SO4   A O2    1 
HETATM 17676 O  O3    . SO4   T  8 .    ? -32.543 24.250  80.022  0.75 53.01 ? 2018 SO4   A O3    1 
HETATM 17677 O  O4    . SO4   T  8 .    ? -34.485 25.578  80.666  0.75 42.85 ? 2018 SO4   A O4    1 
HETATM 17678 S  S     . SO4   U  8 .    ? -27.606 67.930  102.678 0.47 28.32 ? 2019 SO4   A S     1 
HETATM 17679 O  O1    . SO4   U  8 .    ? -27.560 67.878  101.183 0.47 29.03 ? 2019 SO4   A O1    1 
HETATM 17680 O  O2    . SO4   U  8 .    ? -29.024 68.044  103.098 0.47 29.23 ? 2019 SO4   A O2    1 
HETATM 17681 O  O3    . SO4   U  8 .    ? -27.036 66.660  103.251 0.47 24.71 ? 2019 SO4   A O3    1 
HETATM 17682 O  O4    . SO4   U  8 .    ? -26.844 69.117  103.192 0.47 23.50 ? 2019 SO4   A O4    1 
HETATM 17683 P  PA    . FAD   V  2 .    ? -16.836 23.490  103.786 1.00 24.91 ? 2001 FAD   B PA    1 
HETATM 17684 O  O1A   . FAD   V  2 .    ? -17.149 24.997  103.827 1.00 27.89 ? 2001 FAD   B O1A   1 
HETATM 17685 O  O2A   . FAD   V  2 .    ? -17.914 22.551  103.556 1.00 25.45 ? 2001 FAD   B O2A   1 
HETATM 17686 O  O5B   . FAD   V  2 .    ? -15.932 23.025  102.690 1.00 25.98 ? 2001 FAD   B O5B   1 
HETATM 17687 C  C5B   . FAD   V  2 .    ? -14.882 23.902  102.296 1.00 21.50 ? 2001 FAD   B C5B   1 
HETATM 17688 C  C4B   . FAD   V  2 .    ? -13.919 23.169  101.359 1.00 22.75 ? 2001 FAD   B C4B   1 
HETATM 17689 O  O4B   . FAD   V  2 .    ? -14.434 23.135  100.065 1.00 20.46 ? 2001 FAD   B O4B   1 
HETATM 17690 C  C3B   . FAD   V  2 .    ? -12.577 23.817  101.209 1.00 21.24 ? 2001 FAD   B C3B   1 
HETATM 17691 O  O3B   . FAD   V  2 .    ? -11.700 23.571  102.256 1.00 22.70 ? 2001 FAD   B O3B   1 
HETATM 17692 C  C2B   . FAD   V  2 .    ? -12.093 23.197  99.943  1.00 18.36 ? 2001 FAD   B C2B   1 
HETATM 17693 O  O2B   . FAD   V  2 .    ? -11.650 21.904  100.151 1.00 19.76 ? 2001 FAD   B O2B   1 
HETATM 17694 C  C1B   . FAD   V  2 .    ? -13.354 23.124  99.163  1.00 21.18 ? 2001 FAD   B C1B   1 
HETATM 17695 N  N9A   . FAD   V  2 .    ? -13.571 24.192  98.225  1.00 22.23 ? 2001 FAD   B N9A   1 
HETATM 17696 C  C8A   . FAD   V  2 .    ? -13.715 25.536  98.488  1.00 21.67 ? 2001 FAD   B C8A   1 
HETATM 17697 N  N7A   . FAD   V  2 .    ? -13.911 26.192  97.340  1.00 20.21 ? 2001 FAD   B N7A   1 
HETATM 17698 C  C5A   . FAD   V  2 .    ? -13.915 25.286  96.286  1.00 21.67 ? 2001 FAD   B C5A   1 
HETATM 17699 C  C6A   . FAD   V  2 .    ? -14.070 25.379  94.917  1.00 19.22 ? 2001 FAD   B C6A   1 
HETATM 17700 N  N6A   . FAD   V  2 .    ? -14.301 26.653  94.286  1.00 18.99 ? 2001 FAD   B N6A   1 
HETATM 17701 N  N1A   . FAD   V  2 .    ? -14.007 24.269  94.170  1.00 18.92 ? 2001 FAD   B N1A   1 
HETATM 17702 C  C2A   . FAD   V  2 .    ? -13.784 23.043  94.696  1.00 20.26 ? 2001 FAD   B C2A   1 
HETATM 17703 N  N3A   . FAD   V  2 .    ? -13.634 22.919  96.038  1.00 19.96 ? 2001 FAD   B N3A   1 
HETATM 17704 C  C4A   . FAD   V  2 .    ? -13.691 24.002  96.832  1.00 20.37 ? 2001 FAD   B C4A   1 
HETATM 17705 N  N1    . FAD   V  2 .    ? -7.279  18.906  104.524 1.00 20.85 ? 2001 FAD   B N1    1 
HETATM 17706 C  C2    . FAD   V  2 .    ? -6.123  18.396  103.864 1.00 18.25 ? 2001 FAD   B C2    1 
HETATM 17707 O  O2    . FAD   V  2 .    ? -5.846  18.830  102.621 1.00 21.14 ? 2001 FAD   B O2    1 
HETATM 17708 N  N3    . FAD   V  2 .    ? -5.297  17.477  104.466 1.00 20.25 ? 2001 FAD   B N3    1 
HETATM 17709 C  C4    . FAD   V  2 .    ? -5.553  17.044  105.744 1.00 20.36 ? 2001 FAD   B C4    1 
HETATM 17710 O  O4    . FAD   V  2 .    ? -4.737  16.122  106.331 1.00 19.90 ? 2001 FAD   B O4    1 
HETATM 17711 C  C4X   . FAD   V  2 .    ? -6.753  17.526  106.466 1.00 20.61 ? 2001 FAD   B C4X   1 
HETATM 17712 N  N5    . FAD   V  2 .    ? -7.067  17.069  107.732 1.00 21.63 ? 2001 FAD   B N5    1 
HETATM 17713 C  C5X   . FAD   V  2 .    ? -8.218  17.524  108.358 1.00 19.49 ? 2001 FAD   B C5X   1 
HETATM 17714 C  C6    . FAD   V  2 .    ? -8.538  17.054  109.639 1.00 19.58 ? 2001 FAD   B C6    1 
HETATM 17715 C  C7    . FAD   V  2 .    ? -9.693  17.522  110.249 1.00 20.88 ? 2001 FAD   B C7    1 
HETATM 17716 C  C7M   . FAD   V  2 .    ? -10.059 17.029  111.623 1.00 23.99 ? 2001 FAD   B C7M   1 
HETATM 17717 C  C8    . FAD   V  2 .    ? -10.519 18.427  109.631 1.00 24.09 ? 2001 FAD   B C8    1 
HETATM 17718 C  C8M   . FAD   V  2 .    ? -11.760 18.905  110.324 1.00 25.29 ? 2001 FAD   B C8M   1 
HETATM 17719 C  C9    . FAD   V  2 .    ? -10.214 18.896  108.352 1.00 21.97 ? 2001 FAD   B C9    1 
HETATM 17720 C  C9A   . FAD   V  2 .    ? -9.064  18.440  107.730 1.00 22.64 ? 2001 FAD   B C9A   1 
HETATM 17721 N  N10   . FAD   V  2 .    ? -8.752  18.928  106.431 1.00 23.88 ? 2001 FAD   B N10   1 
HETATM 17722 C  C10   . FAD   V  2 .    ? -7.602  18.464  105.786 1.00 20.18 ? 2001 FAD   B C10   1 
HETATM 17723 C  "C1'" . FAD   V  2 .    ? -9.689  19.835  105.731 1.00 22.74 ? 2001 FAD   B "C1'" 1 
HETATM 17724 C  "C2'" . FAD   V  2 .    ? -9.340  21.288  105.577 1.00 24.94 ? 2001 FAD   B "C2'" 1 
HETATM 17725 O  "O2'" . FAD   V  2 .    ? -8.445  21.641  106.547 1.00 28.75 ? 2001 FAD   B "O2'" 1 
HETATM 17726 C  "C3'" . FAD   V  2 .    ? -10.647 22.063  105.741 1.00 26.90 ? 2001 FAD   B "C3'" 1 
HETATM 17727 O  "O3'" . FAD   V  2 .    ? -10.979 22.043  107.076 1.00 26.04 ? 2001 FAD   B "O3'" 1 
HETATM 17728 C  "C4'" . FAD   V  2 .    ? -11.823 21.468  104.994 1.00 27.34 ? 2001 FAD   B "C4'" 1 
HETATM 17729 O  "O4'" . FAD   V  2 .    ? -11.530 21.352  103.646 1.00 25.93 ? 2001 FAD   B "O4'" 1 
HETATM 17730 C  "C5'" . FAD   V  2 .    ? -13.103 22.277  105.229 1.00 22.58 ? 2001 FAD   B "C5'" 1 
HETATM 17731 O  "O5'" . FAD   V  2 .    ? -14.178 21.470  104.793 1.00 25.01 ? 2001 FAD   B "O5'" 1 
HETATM 17732 P  P     . FAD   V  2 .    ? -15.655 21.483  105.434 1.00 26.83 ? 2001 FAD   B P     1 
HETATM 17733 O  O1P   . FAD   V  2 .    ? -16.569 20.233  105.153 1.00 29.13 ? 2001 FAD   B O1P   1 
HETATM 17734 O  O2P   . FAD   V  2 .    ? -15.312 21.846  106.921 1.00 29.70 ? 2001 FAD   B O2P   1 
HETATM 17735 O  O3P   . FAD   V  2 .    ? -16.183 22.962  105.033 1.00 24.91 ? 2001 FAD   B O3P   1 
HETATM 17736 C  C1    . PEG   W  5 .    ? 28.737  67.374  68.896  1.00 29.72 ? 2002 PEG   B C1    1 
HETATM 17737 O  O1    . PEG   W  5 .    ? 27.896  67.906  67.891  1.00 29.22 ? 2002 PEG   B O1    1 
HETATM 17738 C  C2    . PEG   W  5 .    ? 29.854  66.569  68.286  1.00 34.83 ? 2002 PEG   B C2    1 
HETATM 17739 O  O2    . PEG   W  5 .    ? 29.366  65.755  67.251  1.00 36.60 ? 2002 PEG   B O2    1 
HETATM 17740 C  C3    . PEG   W  5 .    ? 29.804  64.426  67.366  1.00 31.52 ? 2002 PEG   B C3    1 
HETATM 17741 C  C4    . PEG   W  5 .    ? 29.805  63.798  65.998  1.00 31.43 ? 2002 PEG   B C4    1 
HETATM 17742 O  O4    . PEG   W  5 .    ? 30.927  64.254  65.280  1.00 40.07 ? 2002 PEG   B O4    1 
HETATM 17743 C  C1    . PGE   X  3 .    ? 2.438   60.588  86.570  1.00 37.13 ? 2003 PGE   B C1    1 
HETATM 17744 O  O1    . PGE   X  3 .    ? 1.133   60.425  87.077  1.00 42.52 ? 2003 PGE   B O1    1 
HETATM 17745 C  C2    . PGE   X  3 .    ? 2.698   59.442  85.636  1.00 38.99 ? 2003 PGE   B C2    1 
HETATM 17746 O  O2    . PGE   X  3 .    ? 4.072   59.329  85.373  1.00 40.87 ? 2003 PGE   B O2    1 
HETATM 17747 C  C3    . PGE   X  3 .    ? 4.730   58.278  86.023  1.00 41.64 ? 2003 PGE   B C3    1 
HETATM 17748 C  C4    . PGE   X  3 .    ? 4.628   56.955  85.311  1.00 28.52 ? 2003 PGE   B C4    1 
HETATM 17749 O  O4    . PGE   X  3 .    ? 2.044   54.203  87.929  1.00 42.02 ? 2003 PGE   B O4    1 
HETATM 17750 C  C6    . PGE   X  3 .    ? 2.530   54.287  86.607  1.00 31.95 ? 2003 PGE   B C6    1 
HETATM 17751 C  C5    . PGE   X  3 .    ? 3.753   55.190  86.575  1.00 33.68 ? 2003 PGE   B C5    1 
HETATM 17752 O  O3    . PGE   X  3 .    ? 3.474   56.283  85.737  1.00 30.37 ? 2003 PGE   B O3    1 
HETATM 17753 C  C1    . PEG   Y  5 .    ? 37.855  38.491  84.393  1.00 48.14 ? 2004 PEG   B C1    1 
HETATM 17754 O  O1    . PEG   Y  5 .    ? 38.145  37.865  85.622  1.00 48.01 ? 2004 PEG   B O1    1 
HETATM 17755 C  C2    . PEG   Y  5 .    ? 37.341  37.466  83.413  1.00 46.47 ? 2004 PEG   B C2    1 
HETATM 17756 O  O2    . PEG   Y  5 .    ? 38.178  36.333  83.389  1.00 46.13 ? 2004 PEG   B O2    1 
HETATM 17757 C  C3    . PEG   Y  5 .    ? 38.838  36.195  82.154  1.00 44.52 ? 2004 PEG   B C3    1 
HETATM 17758 C  C4    . PEG   Y  5 .    ? 39.777  35.014  82.167  1.00 41.22 ? 2004 PEG   B C4    1 
HETATM 17759 O  O4    . PEG   Y  5 .    ? 40.274  34.825  83.469  1.00 43.71 ? 2004 PEG   B O4    1 
HETATM 17760 C  C1    . PEG   Z  5 .    ? 15.354  10.293  113.103 1.00 40.50 ? 2005 PEG   B C1    1 
HETATM 17761 O  O1    . PEG   Z  5 .    ? 16.545  10.994  112.808 1.00 41.94 ? 2005 PEG   B O1    1 
HETATM 17762 C  C2    . PEG   Z  5 .    ? 15.642  9.157   114.057 1.00 44.01 ? 2005 PEG   B C2    1 
HETATM 17763 O  O2    . PEG   Z  5 .    ? 16.011  7.993   113.353 1.00 50.72 ? 2005 PEG   B O2    1 
HETATM 17764 C  C3    . PEG   Z  5 .    ? 14.992  7.019   113.327 1.00 43.89 ? 2005 PEG   B C3    1 
HETATM 17765 C  C4    . PEG   Z  5 .    ? 14.720  6.564   111.912 1.00 40.55 ? 2005 PEG   B C4    1 
HETATM 17766 O  O4    . PEG   Z  5 .    ? 15.641  5.567   111.524 1.00 51.09 ? 2005 PEG   B O4    1 
HETATM 17767 O  O1    . PG4   AA 6 .    ? -8.471  31.060  71.458  1.00 39.06 ? 2006 PG4   B O1    1 
HETATM 17768 C  C1    . PG4   AA 6 .    ? -7.073  31.231  71.362  1.00 27.57 ? 2006 PG4   B C1    1 
HETATM 17769 C  C2    . PG4   AA 6 .    ? -6.652  31.115  69.918  1.00 29.95 ? 2006 PG4   B C2    1 
HETATM 17770 O  O2    . PG4   AA 6 .    ? -6.210  32.370  69.448  1.00 38.44 ? 2006 PG4   B O2    1 
HETATM 17771 C  C3    . PG4   AA 6 .    ? -5.397  32.311  68.303  1.00 30.11 ? 2006 PG4   B C3    1 
HETATM 17772 C  C4    . PG4   AA 6 .    ? -6.189  32.628  67.052  1.00 33.37 ? 2006 PG4   B C4    1 
HETATM 17773 O  O3    . PG4   AA 6 .    ? -6.740  33.928  67.109  1.00 43.80 ? 2006 PG4   B O3    1 
HETATM 17774 C  C5    . PG4   AA 6 .    ? -7.122  34.441  65.848  1.00 34.11 ? 2006 PG4   B C5    1 
HETATM 17775 C  C6    . PG4   AA 6 .    ? -7.856  35.760  65.990  1.00 39.49 ? 2006 PG4   B C6    1 
HETATM 17776 O  O4    . PG4   AA 6 .    ? -6.960  36.817  66.276  1.00 37.73 ? 2006 PG4   B O4    1 
HETATM 17777 C  C7    . PG4   AA 6 .    ? -7.604  38.056  66.417  1.00 36.25 ? 2006 PG4   B C7    1 
HETATM 17778 C  C8    . PG4   AA 6 .    ? -6.717  39.079  67.091  1.00 29.65 ? 2006 PG4   B C8    1 
HETATM 17779 O  O5    . PG4   AA 6 .    ? -7.017  39.077  68.472  1.00 38.56 ? 2006 PG4   B O5    1 
HETATM 17780 C  C     . FMT   BA 4 .    ? -9.323  8.721   81.312  1.00 43.31 ? 2007 FMT   B C     1 
HETATM 17781 O  O1    . FMT   BA 4 .    ? -10.266 8.222   80.672  1.00 47.16 ? 2007 FMT   B O1    1 
HETATM 17782 O  O2    . FMT   BA 4 .    ? -9.223  9.877   81.773  1.00 47.65 ? 2007 FMT   B O2    1 
HETATM 17783 C  C1    . PEG   CA 5 .    ? 2.844   13.064  77.564  1.00 40.31 ? 2008 PEG   B C1    1 
HETATM 17784 O  O1    . PEG   CA 5 .    ? 2.793   11.850  78.291  1.00 42.31 ? 2008 PEG   B O1    1 
HETATM 17785 C  C2    . PEG   CA 5 .    ? 4.258   13.408  77.154  1.00 34.52 ? 2008 PEG   B C2    1 
HETATM 17786 O  O2    . PEG   CA 5 .    ? 5.192   12.522  77.733  1.00 40.25 ? 2008 PEG   B O2    1 
HETATM 17787 C  C3    . PEG   CA 5 .    ? 6.155   12.040  76.823  1.00 30.10 ? 2008 PEG   B C3    1 
HETATM 17788 C  C4    . PEG   CA 5 .    ? 5.512   11.585  75.531  1.00 37.23 ? 2008 PEG   B C4    1 
HETATM 17789 O  O4    . PEG   CA 5 .    ? 6.474   10.971  74.704  1.00 36.32 ? 2008 PEG   B O4    1 
HETATM 17790 C  C     . FMT   DA 4 .    ? 24.272  25.422  49.164  1.00 37.75 ? 2009 FMT   B C     1 
HETATM 17791 O  O1    . FMT   DA 4 .    ? 25.432  25.153  48.783  1.00 44.29 ? 2009 FMT   B O1    1 
HETATM 17792 O  O2    . FMT   DA 4 .    ? 23.911  26.262  50.016  1.00 35.95 ? 2009 FMT   B O2    1 
HETATM 17793 C  C     . FMT   EA 4 .    ? -3.200  56.228  82.162  1.00 25.50 ? 2010 FMT   B C     1 
HETATM 17794 O  O1    . FMT   EA 4 .    ? -2.816  55.494  83.093  1.00 32.28 ? 2010 FMT   B O1    1 
HETATM 17795 O  O2    . FMT   EA 4 .    ? -4.279  56.163  81.523  1.00 31.84 ? 2010 FMT   B O2    1 
HETATM 17796 C  C1    . PEG   FA 5 .    ? 15.842  66.569  54.612  1.00 40.11 ? 2011 PEG   B C1    1 
HETATM 17797 O  O1    . PEG   FA 5 .    ? 15.828  67.629  55.543  1.00 38.19 ? 2011 PEG   B O1    1 
HETATM 17798 C  C2    . PEG   FA 5 .    ? 14.619  66.588  53.735  1.00 43.33 ? 2011 PEG   B C2    1 
HETATM 17799 O  O2    . PEG   FA 5 .    ? 14.507  65.364  53.056  1.00 49.41 ? 2011 PEG   B O2    1 
HETATM 17800 C  C3    . PEG   FA 5 .    ? 14.501  64.254  53.918  1.00 45.04 ? 2011 PEG   B C3    1 
HETATM 17801 C  C4    . PEG   FA 5 .    ? 15.509  63.226  53.462  1.00 48.80 ? 2011 PEG   B C4    1 
HETATM 17802 O  O4    . PEG   FA 5 .    ? 15.627  62.216  54.443  1.00 51.76 ? 2011 PEG   B O4    1 
HETATM 17803 C  C     . FMT   GA 4 .    ? 42.084  39.714  86.086  1.00 41.59 ? 2012 FMT   B C     1 
HETATM 17804 O  O1    . FMT   GA 4 .    ? 42.720  38.714  86.476  1.00 45.43 ? 2012 FMT   B O1    1 
HETATM 17805 O  O2    . FMT   GA 4 .    ? 40.910  39.766  85.659  1.00 43.30 ? 2012 FMT   B O2    1 
HETATM 17806 S  S     . SO4   HA 8 .    ? 3.880   15.663  64.841  0.67 33.57 ? 2013 SO4   B S     1 
HETATM 17807 O  O1    . SO4   HA 8 .    ? 3.973   16.412  63.542  0.67 32.27 ? 2013 SO4   B O1    1 
HETATM 17808 O  O2    . SO4   HA 8 .    ? 2.582   15.979  65.519  0.67 37.94 ? 2013 SO4   B O2    1 
HETATM 17809 O  O3    . SO4   HA 8 .    ? 3.965   14.196  64.545  0.67 29.30 ? 2013 SO4   B O3    1 
HETATM 17810 O  O4    . SO4   HA 8 .    ? 5.005   16.042  65.752  0.67 29.35 ? 2013 SO4   B O4    1 
HETATM 17811 S  S     . SO4   IA 8 .    ? -7.068  47.896  72.892  1.00 20.52 ? 2014 SO4   B S     1 
HETATM 17812 O  O1    . SO4   IA 8 .    ? -5.809  47.185  72.514  1.00 24.95 ? 2014 SO4   B O1    1 
HETATM 17813 O  O2    . SO4   IA 8 .    ? -7.783  48.341  71.667  1.00 18.68 ? 2014 SO4   B O2    1 
HETATM 17814 O  O3    . SO4   IA 8 .    ? -7.959  46.954  73.625  1.00 21.89 ? 2014 SO4   B O3    1 
HETATM 17815 O  O4    . SO4   IA 8 .    ? -6.705  49.063  73.740  1.00 23.12 ? 2014 SO4   B O4    1 
HETATM 17816 S  S     . SO4   JA 8 .    ? 0.271   20.667  135.808 0.84 46.14 ? 2015 SO4   B S     1 
HETATM 17817 O  O1    . SO4   JA 8 .    ? 1.639   21.214  135.529 0.84 48.27 ? 2015 SO4   B O1    1 
HETATM 17818 O  O2    . SO4   JA 8 .    ? -0.056  19.591  134.821 0.84 50.54 ? 2015 SO4   B O2    1 
HETATM 17819 O  O3    . SO4   JA 8 .    ? 0.248   20.083  137.186 0.84 50.67 ? 2015 SO4   B O3    1 
HETATM 17820 O  O4    . SO4   JA 8 .    ? -0.725  21.779  135.711 0.84 46.67 ? 2015 SO4   B O4    1 
HETATM 17821 S  S     . SO4   KA 8 .    ? 34.276  33.743  70.119  0.65 40.61 ? 2016 SO4   B S     1 
HETATM 17822 O  O1    . SO4   KA 8 .    ? 34.715  34.203  68.761  0.65 35.45 ? 2016 SO4   B O1    1 
HETATM 17823 O  O2    . SO4   KA 8 .    ? 32.800  33.481  70.136  0.65 36.11 ? 2016 SO4   B O2    1 
HETATM 17824 O  O3    . SO4   KA 8 .    ? 35.020  32.489  70.477  0.65 41.16 ? 2016 SO4   B O3    1 
HETATM 17825 O  O4    . SO4   KA 8 .    ? 34.589  34.804  71.133  0.65 40.94 ? 2016 SO4   B O4    1 
HETATM 17826 S  S     . SO4   LA 8 .    ? 7.282   25.480  84.001  0.60 23.98 ? 2017 SO4   B S     1 
HETATM 17827 O  O1    . SO4   LA 8 .    ? 8.320   24.504  84.480  0.60 36.79 ? 2017 SO4   B O1    1 
HETATM 17828 O  O2    . SO4   LA 8 .    ? 6.324   24.780  83.105  0.60 21.69 ? 2017 SO4   B O2    1 
HETATM 17829 O  O3    . SO4   LA 8 .    ? 6.542   25.997  85.203  0.60 32.22 ? 2017 SO4   B O3    1 
HETATM 17830 O  O4    . SO4   LA 8 .    ? 7.942   26.647  83.359  0.60 34.41 ? 2017 SO4   B O4    1 
HETATM 17831 S  S     . SO4   MA 8 .    ? 14.497  34.135  83.313  0.55 26.87 ? 2018 SO4   B S     1 
HETATM 17832 O  O1    . SO4   MA 8 .    ? 15.707  34.712  82.632  0.55 29.62 ? 2018 SO4   B O1    1 
HETATM 17833 O  O2    . SO4   MA 8 .    ? 13.852  33.111  82.427  0.55 35.33 ? 2018 SO4   B O2    1 
HETATM 17834 O  O3    . SO4   MA 8 .    ? 14.917  33.469  84.565  0.55 24.83 ? 2018 SO4   B O3    1 
HETATM 17835 O  O4    . SO4   MA 8 .    ? 13.510  35.222  83.604  0.55 26.00 ? 2018 SO4   B O4    1 
HETATM 17836 S  S     . SO4   NA 8 .    ? 6.717   28.893  81.489  0.49 31.77 ? 2019 SO4   B S     1 
HETATM 17837 O  O1    . SO4   NA 8 .    ? 7.942   29.288  80.729  0.49 24.66 ? 2019 SO4   B O1    1 
HETATM 17838 O  O2    . SO4   NA 8 .    ? 5.517   29.585  80.908  0.49 28.20 ? 2019 SO4   B O2    1 
HETATM 17839 O  O3    . SO4   NA 8 .    ? 6.493   27.424  81.381  0.49 32.01 ? 2019 SO4   B O3    1 
HETATM 17840 O  O4    . SO4   NA 8 .    ? 6.880   29.233  82.939  0.49 30.12 ? 2019 SO4   B O4    1 
HETATM 17841 S  S     . SO4   OA 8 .    ? 17.035  6.411   117.828 0.68 55.13 ? 2020 SO4   B S     1 
HETATM 17842 O  O1    . SO4   OA 8 .    ? 17.294  5.573   116.611 0.68 54.07 ? 2020 SO4   B O1    1 
HETATM 17843 O  O2    . SO4   OA 8 .    ? 15.692  7.068   117.708 0.68 45.91 ? 2020 SO4   B O2    1 
HETATM 17844 O  O3    . SO4   OA 8 .    ? 17.052  5.538   119.048 0.68 54.88 ? 2020 SO4   B O3    1 
HETATM 17845 O  O4    . SO4   OA 8 .    ? 18.106  7.455   117.940 0.68 54.66 ? 2020 SO4   B O4    1 
HETATM 17846 S  S     . SO4   PA 8 .    ? 18.314  45.674  112.310 0.54 36.75 ? 2021 SO4   B S     1 
HETATM 17847 O  O1    . SO4   PA 8 .    ? 18.935  46.718  111.444 0.54 29.41 ? 2021 SO4   B O1    1 
HETATM 17848 O  O2    . SO4   PA 8 .    ? 17.828  44.513  111.493 0.54 27.77 ? 2021 SO4   B O2    1 
HETATM 17849 O  O3    . SO4   PA 8 .    ? 19.326  45.189  113.308 0.54 36.82 ? 2021 SO4   B O3    1 
HETATM 17850 O  O4    . SO4   PA 8 .    ? 17.147  46.279  113.032 0.54 38.26 ? 2021 SO4   B O4    1 
HETATM 17851 S  S     . SO4   QA 8 .    ? -34.406 30.304  107.212 0.74 59.53 ? 2022 SO4   B S     1 
HETATM 17852 O  O1    . SO4   QA 8 .    ? -32.979 30.630  107.541 0.74 51.50 ? 2022 SO4   B O1    1 
HETATM 17853 O  O2    . SO4   QA 8 .    ? -34.462 29.268  106.126 0.74 51.56 ? 2022 SO4   B O2    1 
HETATM 17854 O  O3    . SO4   QA 8 .    ? -35.071 29.742  108.434 0.74 56.74 ? 2022 SO4   B O3    1 
HETATM 17855 O  O4    . SO4   QA 8 .    ? -35.088 31.566  106.758 0.74 48.68 ? 2022 SO4   B O4    1 
HETATM 17856 O  O     . HOH   RA 9 .    ? -62.681 67.340  66.567  1.00 33.15 ? 2101 HOH   A O     1 
HETATM 17857 O  O     . HOH   RA 9 .    ? -30.304 50.529  104.555 1.00 27.12 ? 2102 HOH   A O     1 
HETATM 17858 O  O     . HOH   RA 9 .    ? -57.912 66.983  61.718  1.00 28.67 ? 2103 HOH   A O     1 
HETATM 17859 O  O     . HOH   RA 9 .    ? -46.828 77.596  69.109  1.00 24.02 ? 2104 HOH   A O     1 
HETATM 17860 O  O     . HOH   RA 9 .    ? -68.945 62.181  74.904  1.00 23.98 ? 2105 HOH   A O     1 
HETATM 17861 O  O     . HOH   RA 9 .    ? -41.116 63.346  73.507  1.00 30.15 ? 2106 HOH   A O     1 
HETATM 17862 O  O     . HOH   RA 9 .    ? -28.905 38.344  84.964  1.00 41.41 ? 2107 HOH   A O     1 
HETATM 17863 O  O     . HOH   RA 9 .    ? -4.751  71.891  95.359  1.00 39.34 ? 2108 HOH   A O     1 
HETATM 17864 O  O     . HOH   RA 9 .    ? -0.437  60.143  94.806  1.00 43.87 ? 2109 HOH   A O     1 
HETATM 17865 O  O     . HOH   RA 9 .    ? 13.957  87.211  98.726  1.00 35.46 ? 2110 HOH   A O     1 
HETATM 17866 O  O     . HOH   RA 9 .    ? -51.469 74.019  68.455  1.00 27.37 ? 2111 HOH   A O     1 
HETATM 17867 O  O     . HOH   RA 9 .    ? -15.460 93.305  130.967 1.00 37.64 ? 2112 HOH   A O     1 
HETATM 17868 O  O     . HOH   RA 9 .    ? -52.572 64.467  100.736 1.00 30.71 ? 2113 HOH   A O     1 
HETATM 17869 O  O     . HOH   RA 9 .    ? -10.065 81.465  90.913  1.00 27.34 ? 2114 HOH   A O     1 
HETATM 17870 O  O     . HOH   RA 9 .    ? -30.418 91.611  112.339 1.00 36.56 ? 2115 HOH   A O     1 
HETATM 17871 O  O     . HOH   RA 9 .    ? -14.447 64.670  50.829  1.00 45.98 ? 2116 HOH   A O     1 
HETATM 17872 O  O     . HOH   RA 9 .    ? 1.997   63.901  119.307 1.00 43.53 ? 2117 HOH   A O     1 
HETATM 17873 O  O     . HOH   RA 9 .    ? -25.247 50.772  104.576 1.00 44.57 ? 2118 HOH   A O     1 
HETATM 17874 O  O     . HOH   RA 9 .    ? -34.284 38.950  95.856  1.00 44.59 ? 2119 HOH   A O     1 
HETATM 17875 O  O     . HOH   RA 9 .    ? -0.473  83.856  109.469 1.00 31.69 ? 2120 HOH   A O     1 
HETATM 17876 O  O     . HOH   RA 9 .    ? -13.360 56.031  81.174  1.00 32.28 ? 2121 HOH   A O     1 
HETATM 17877 O  O     . HOH   RA 9 .    ? -23.966 48.214  98.381  1.00 38.53 ? 2122 HOH   A O     1 
HETATM 17878 O  O     . HOH   RA 9 .    ? 7.600   91.230  113.592 1.00 36.78 ? 2123 HOH   A O     1 
HETATM 17879 O  O     . HOH   RA 9 .    ? -57.668 64.649  91.387  1.00 29.81 ? 2124 HOH   A O     1 
HETATM 17880 O  O     . HOH   RA 9 .    ? -20.165 59.923  78.842  1.00 38.73 ? 2125 HOH   A O     1 
HETATM 17881 O  O     . HOH   RA 9 .    ? -17.759 83.079  96.249  1.00 27.18 ? 2126 HOH   A O     1 
HETATM 17882 O  O     . HOH   RA 9 .    ? -60.919 68.671  68.841  1.00 26.38 ? 2127 HOH   A O     1 
HETATM 17883 O  O     . HOH   RA 9 .    ? -25.045 67.199  86.170  1.00 33.06 ? 2128 HOH   A O     1 
HETATM 17884 O  O     . HOH   RA 9 .    ? -12.678 87.143  98.736  1.00 42.49 ? 2129 HOH   A O     1 
HETATM 17885 O  O     . HOH   RA 9 .    ? -19.288 73.023  97.301  1.00 21.32 ? 2130 HOH   A O     1 
HETATM 17886 O  O     . HOH   RA 9 .    ? -48.461 54.690  61.104  1.00 24.41 ? 2131 HOH   A O     1 
HETATM 17887 O  O     . HOH   RA 9 .    ? -0.364  63.877  109.590 1.00 25.02 ? 2132 HOH   A O     1 
HETATM 17888 O  O     . HOH   RA 9 .    ? -0.498  77.125  117.080 1.00 36.15 ? 2133 HOH   A O     1 
HETATM 17889 O  O     . HOH   RA 9 .    ? -52.111 60.923  102.122 1.00 26.15 ? 2134 HOH   A O     1 
HETATM 17890 O  O     . HOH   RA 9 .    ? -16.546 56.047  112.087 1.00 26.92 ? 2135 HOH   A O     1 
HETATM 17891 O  O     . HOH   RA 9 .    ? 0.301   80.167  81.602  1.00 45.65 ? 2136 HOH   A O     1 
HETATM 17892 O  O     . HOH   RA 9 .    ? -38.421 77.584  69.921  1.00 34.18 ? 2137 HOH   A O     1 
HETATM 17893 O  O     . HOH   RA 9 .    ? -24.609 65.346  94.399  1.00 28.10 ? 2138 HOH   A O     1 
HETATM 17894 O  O     . HOH   RA 9 .    ? -8.542  53.473  104.515 1.00 37.20 ? 2139 HOH   A O     1 
HETATM 17895 O  O     . HOH   RA 9 .    ? 1.120   74.695  107.175 1.00 29.60 ? 2140 HOH   A O     1 
HETATM 17896 O  O     . HOH   RA 9 .    ? 18.594  59.356  95.877  1.00 39.10 ? 2141 HOH   A O     1 
HETATM 17897 O  O     . HOH   RA 9 .    ? -42.037 38.828  84.785  1.00 28.16 ? 2142 HOH   A O     1 
HETATM 17898 O  O     . HOH   RA 9 .    ? -38.310 38.226  87.683  1.00 38.23 ? 2143 HOH   A O     1 
HETATM 17899 O  O     . HOH   RA 9 .    ? -10.470 49.915  109.874 1.00 20.39 ? 2144 HOH   A O     1 
HETATM 17900 O  O     . HOH   RA 9 .    ? -7.059  50.848  76.432  1.00 29.13 ? 2145 HOH   A O     1 
HETATM 17901 O  O     . HOH   RA 9 .    ? 25.633  79.686  107.577 1.00 34.90 ? 2146 HOH   A O     1 
HETATM 17902 O  O     . HOH   RA 9 .    ? -13.185 94.891  85.016  1.00 50.05 ? 2147 HOH   A O     1 
HETATM 17903 O  O     . HOH   RA 9 .    ? -24.160 92.931  126.740 1.00 29.62 ? 2148 HOH   A O     1 
HETATM 17904 O  O     . HOH   RA 9 .    ? -20.578 55.251  115.453 1.00 38.56 ? 2149 HOH   A O     1 
HETATM 17905 O  O     . HOH   RA 9 .    ? -61.779 57.391  63.833  1.00 31.29 ? 2150 HOH   A O     1 
HETATM 17906 O  O     . HOH   RA 9 .    ? -43.813 62.356  70.109  1.00 27.66 ? 2151 HOH   A O     1 
HETATM 17907 O  O     . HOH   RA 9 .    ? -18.744 61.723  85.203  1.00 24.94 ? 2152 HOH   A O     1 
HETATM 17908 O  O     . HOH   RA 9 .    ? -36.400 61.895  74.743  1.00 35.02 ? 2153 HOH   A O     1 
HETATM 17909 O  O     . HOH   RA 9 .    ? -43.600 41.926  104.393 1.00 34.96 ? 2154 HOH   A O     1 
HETATM 17910 O  O     . HOH   RA 9 .    ? -6.414  58.807  119.754 1.00 21.72 ? 2155 HOH   A O     1 
HETATM 17911 O  O     . HOH   RA 9 .    ? -46.868 75.621  67.003  1.00 31.82 ? 2156 HOH   A O     1 
HETATM 17912 O  O     . HOH   RA 9 .    ? -4.982  70.672  75.891  1.00 41.18 ? 2157 HOH   A O     1 
HETATM 17913 O  O     . HOH   RA 9 .    ? 29.531  67.481  108.253 1.00 39.51 ? 2158 HOH   A O     1 
HETATM 17914 O  O     . HOH   RA 9 .    ? -15.928 92.237  104.956 1.00 36.44 ? 2159 HOH   A O     1 
HETATM 17915 O  O     . HOH   RA 9 .    ? -11.693 68.893  76.335  1.00 29.75 ? 2160 HOH   A O     1 
HETATM 17916 O  O     . HOH   RA 9 .    ? -46.525 35.247  87.000  1.00 33.04 ? 2161 HOH   A O     1 
HETATM 17917 O  O     . HOH   RA 9 .    ? -19.507 89.602  112.635 1.00 35.68 ? 2162 HOH   A O     1 
HETATM 17918 O  O     . HOH   RA 9 .    ? -58.573 33.729  72.674  1.00 43.24 ? 2163 HOH   A O     1 
HETATM 17919 O  O     . HOH   RA 9 .    ? 8.572   69.273  125.175 1.00 35.31 ? 2164 HOH   A O     1 
HETATM 17920 O  O     . HOH   RA 9 .    ? -28.771 57.691  115.368 1.00 31.66 ? 2165 HOH   A O     1 
HETATM 17921 O  O     . HOH   RA 9 .    ? -23.058 63.937  97.681  1.00 20.01 ? 2166 HOH   A O     1 
HETATM 17922 O  O     . HOH   RA 9 .    ? -42.785 48.581  59.816  1.00 31.74 ? 2167 HOH   A O     1 
HETATM 17923 O  O     . HOH   RA 9 .    ? -5.503  53.829  110.565 1.00 18.40 ? 2168 HOH   A O     1 
HETATM 17924 O  O     . HOH   RA 9 .    ? -48.320 81.583  84.858  1.00 36.66 ? 2169 HOH   A O     1 
HETATM 17925 O  O     . HOH   RA 9 .    ? -25.702 96.188  123.940 1.00 30.98 ? 2170 HOH   A O     1 
HETATM 17926 O  O     . HOH   RA 9 .    ? -42.616 61.376  100.032 1.00 24.25 ? 2171 HOH   A O     1 
HETATM 17927 O  O     . HOH   RA 9 .    ? 6.976   54.331  101.206 1.00 22.46 ? 2172 HOH   A O     1 
HETATM 17928 O  O     . HOH   RA 9 .    ? -36.730 82.915  120.887 1.00 30.85 ? 2173 HOH   A O     1 
HETATM 17929 O  O     . HOH   RA 9 .    ? -32.334 82.407  97.342  1.00 24.36 ? 2174 HOH   A O     1 
HETATM 17930 O  O     . HOH   RA 9 .    ? -38.713 64.923  96.287  1.00 28.73 ? 2175 HOH   A O     1 
HETATM 17931 O  O     . HOH   RA 9 .    ? -67.435 66.108  69.828  1.00 40.01 ? 2176 HOH   A O     1 
HETATM 17932 O  O     . HOH   RA 9 .    ? -14.713 64.196  98.983  1.00 26.41 ? 2177 HOH   A O     1 
HETATM 17933 O  O     . HOH   RA 9 .    ? -27.001 97.191  88.840  1.00 32.58 ? 2178 HOH   A O     1 
HETATM 17934 O  O     . HOH   RA 9 .    ? -6.589  68.311  77.833  1.00 41.91 ? 2179 HOH   A O     1 
HETATM 17935 O  O     . HOH   RA 9 .    ? -28.364 62.078  116.717 1.00 21.94 ? 2180 HOH   A O     1 
HETATM 17936 O  O     . HOH   RA 9 .    ? -25.188 87.496  132.957 1.00 36.78 ? 2181 HOH   A O     1 
HETATM 17937 O  O     . HOH   RA 9 .    ? -13.706 78.105  110.886 1.00 21.03 ? 2182 HOH   A O     1 
HETATM 17938 O  O     . HOH   RA 9 .    ? -55.852 34.771  86.596  1.00 33.86 ? 2183 HOH   A O     1 
HETATM 17939 O  O     . HOH   RA 9 .    ? -37.718 62.295  81.200  1.00 32.76 ? 2184 HOH   A O     1 
HETATM 17940 O  O     . HOH   RA 9 .    ? 8.596   90.416  102.937 1.00 39.96 ? 2185 HOH   A O     1 
HETATM 17941 O  O     . HOH   RA 9 .    ? -45.436 89.489  106.016 1.00 36.73 ? 2186 HOH   A O     1 
HETATM 17942 O  O     . HOH   RA 9 .    ? -36.507 63.560  95.825  1.00 24.63 ? 2187 HOH   A O     1 
HETATM 17943 O  O     . HOH   RA 9 .    ? -2.165  85.408  113.173 1.00 33.89 ? 2188 HOH   A O     1 
HETATM 17944 O  O     . HOH   RA 9 .    ? -19.848 59.526  75.802  1.00 21.96 ? 2189 HOH   A O     1 
HETATM 17945 O  O     . HOH   RA 9 .    ? -27.990 78.155  100.997 1.00 26.95 ? 2190 HOH   A O     1 
HETATM 17946 O  O     . HOH   RA 9 .    ? -31.185 58.830  115.382 1.00 33.37 ? 2191 HOH   A O     1 
HETATM 17947 O  O     . HOH   RA 9 .    ? -49.323 72.722  115.666 1.00 44.95 ? 2192 HOH   A O     1 
HETATM 17948 O  O     . HOH   RA 9 .    ? -38.341 49.667  102.399 1.00 26.30 ? 2193 HOH   A O     1 
HETATM 17949 O  O     . HOH   RA 9 .    ? -47.066 67.707  59.841  1.00 26.00 ? 2194 HOH   A O     1 
HETATM 17950 O  O     . HOH   RA 9 .    ? -43.303 80.343  89.888  1.00 28.29 ? 2195 HOH   A O     1 
HETATM 17951 O  O     . HOH   RA 9 .    ? -14.811 55.961  121.587 1.00 35.06 ? 2196 HOH   A O     1 
HETATM 17952 O  O     . HOH   RA 9 .    ? -22.776 59.150  75.014  1.00 32.74 ? 2197 HOH   A O     1 
HETATM 17953 O  O     . HOH   RA 9 .    ? -3.277  89.863  108.658 1.00 28.00 ? 2198 HOH   A O     1 
HETATM 17954 O  O     . HOH   RA 9 .    ? -49.238 66.628  94.084  1.00 20.12 ? 2199 HOH   A O     1 
HETATM 17955 O  O     . HOH   RA 9 .    ? -45.091 89.413  109.314 1.00 38.08 ? 2200 HOH   A O     1 
HETATM 17956 O  O     . HOH   RA 9 .    ? -61.805 67.334  60.909  1.00 39.83 ? 2201 HOH   A O     1 
HETATM 17957 O  O     . HOH   RA 9 .    ? -17.302 86.996  91.968  1.00 29.76 ? 2202 HOH   A O     1 
HETATM 17958 O  O     . HOH   RA 9 .    ? -26.275 73.760  103.499 1.00 33.07 ? 2203 HOH   A O     1 
HETATM 17959 O  O     . HOH   RA 9 .    ? 14.449  86.959  110.048 1.00 32.05 ? 2204 HOH   A O     1 
HETATM 17960 O  O     . HOH   RA 9 .    ? -9.343  65.221  75.961  1.00 24.53 ? 2205 HOH   A O     1 
HETATM 17961 O  O     . HOH   RA 9 .    ? -31.977 80.003  99.394  1.00 29.89 ? 2206 HOH   A O     1 
HETATM 17962 O  O     . HOH   RA 9 .    ? -0.762  50.553  57.786  1.00 29.77 ? 2207 HOH   A O     1 
HETATM 17963 O  O     . HOH   RA 9 .    ? -17.420 72.976  111.008 1.00 18.06 ? 2208 HOH   A O     1 
HETATM 17964 O  O     . HOH   RA 9 .    ? 20.674  83.615  100.957 1.00 40.86 ? 2209 HOH   A O     1 
HETATM 17965 O  O     . HOH   RA 9 .    ? -41.641 79.984  79.980  1.00 27.01 ? 2210 HOH   A O     1 
HETATM 17966 O  O     . HOH   RA 9 .    ? -51.854 47.489  68.804  1.00 30.81 ? 2211 HOH   A O     1 
HETATM 17967 O  O     . HOH   RA 9 .    ? -26.082 56.716  107.861 1.00 21.41 ? 2212 HOH   A O     1 
HETATM 17968 O  O     . HOH   RA 9 .    ? -61.645 58.091  70.152  1.00 22.67 ? 2213 HOH   A O     1 
HETATM 17969 O  O     . HOH   RA 9 .    ? -14.232 61.653  107.212 1.00 27.04 ? 2214 HOH   A O     1 
HETATM 17970 O  O     . HOH   RA 9 .    ? -13.112 59.535  122.099 1.00 29.32 ? 2215 HOH   A O     1 
HETATM 17971 O  O     . HOH   RA 9 .    ? -11.391 63.507  112.929 1.00 18.21 ? 2216 HOH   A O     1 
HETATM 17972 O  O     . HOH   RA 9 .    ? -4.400  71.547  126.472 1.00 40.78 ? 2217 HOH   A O     1 
HETATM 17973 O  O     . HOH   RA 9 .    ? -11.844 77.238  102.645 1.00 29.01 ? 2218 HOH   A O     1 
HETATM 17974 O  O     . HOH   RA 9 .    ? -9.819  68.122  124.801 1.00 34.43 ? 2219 HOH   A O     1 
HETATM 17975 O  O     . HOH   RA 9 .    ? -59.540 39.786  79.098  1.00 40.85 ? 2220 HOH   A O     1 
HETATM 17976 O  O     . HOH   RA 9 .    ? -33.513 72.049  76.730  1.00 32.65 ? 2221 HOH   A O     1 
HETATM 17977 O  O     . HOH   RA 9 .    ? -58.209 65.346  94.517  1.00 26.91 ? 2222 HOH   A O     1 
HETATM 17978 O  O     . HOH   RA 9 .    ? -3.481  70.784  117.161 1.00 24.72 ? 2223 HOH   A O     1 
HETATM 17979 O  O     . HOH   RA 9 .    ? -43.242 77.341  67.724  1.00 25.80 ? 2224 HOH   A O     1 
HETATM 17980 O  O     . HOH   RA 9 .    ? 6.395   90.780  106.626 1.00 35.87 ? 2225 HOH   A O     1 
HETATM 17981 O  O     . HOH   RA 9 .    ? -43.506 75.438  113.934 1.00 27.99 ? 2226 HOH   A O     1 
HETATM 17982 O  O     . HOH   RA 9 .    ? -51.049 69.934  93.956  1.00 24.47 ? 2227 HOH   A O     1 
HETATM 17983 O  O     . HOH   RA 9 .    ? -66.730 67.451  71.575  1.00 31.35 ? 2228 HOH   A O     1 
HETATM 17984 O  O     . HOH   RA 9 .    ? -35.454 73.458  83.589  1.00 27.04 ? 2229 HOH   A O     1 
HETATM 17985 O  O     . HOH   RA 9 .    ? -3.999  79.350  103.694 1.00 26.63 ? 2230 HOH   A O     1 
HETATM 17986 O  O     . HOH   RA 9 .    ? -54.363 47.670  67.297  1.00 34.88 ? 2231 HOH   A O     1 
HETATM 17987 O  O     . HOH   RA 9 .    ? -59.381 54.242  74.761  1.00 21.13 ? 2232 HOH   A O     1 
HETATM 17988 O  O     . HOH   RA 9 .    ? -33.885 97.471  98.189  1.00 37.96 ? 2233 HOH   A O     1 
HETATM 17989 O  O     . HOH   RA 9 .    ? -6.167  82.652  103.119 1.00 28.36 ? 2234 HOH   A O     1 
HETATM 17990 O  O     . HOH   RA 9 .    ? -5.783  65.271  114.064 1.00 23.19 ? 2235 HOH   A O     1 
HETATM 17991 O  O     . HOH   RA 9 .    ? 25.161  77.366  108.988 1.00 35.90 ? 2236 HOH   A O     1 
HETATM 17992 O  O     . HOH   RA 9 .    ? -47.927 85.106  102.008 1.00 33.16 ? 2237 HOH   A O     1 
HETATM 17993 O  O     . HOH   RA 9 .    ? -38.795 77.714  97.233  1.00 21.88 ? 2238 HOH   A O     1 
HETATM 17994 O  O     . HOH   RA 9 .    ? -64.323 59.715  92.710  1.00 38.82 ? 2239 HOH   A O     1 
HETATM 17995 O  O     . HOH   RA 9 .    ? -24.866 88.288  78.953  1.00 25.32 ? 2240 HOH   A O     1 
HETATM 17996 O  O     . HOH   RA 9 .    ? -39.769 57.442  87.926  1.00 16.16 ? 2241 HOH   A O     1 
HETATM 17997 O  O     . HOH   RA 9 .    ? -37.428 64.271  66.720  1.00 34.42 ? 2242 HOH   A O     1 
HETATM 17998 O  O     . HOH   RA 9 .    ? -24.367 97.716  114.165 1.00 47.54 ? 2243 HOH   A O     1 
HETATM 17999 O  O     . HOH   RA 9 .    ? -47.753 72.404  112.891 1.00 35.13 ? 2244 HOH   A O     1 
HETATM 18000 O  O     . HOH   RA 9 .    ? -44.230 30.361  96.175  1.00 34.30 ? 2245 HOH   A O     1 
HETATM 18001 O  O     . HOH   RA 9 .    ? -59.156 75.933  77.310  1.00 38.56 ? 2246 HOH   A O     1 
HETATM 18002 O  O     . HOH   RA 9 .    ? 2.319   85.614  117.983 1.00 31.51 ? 2247 HOH   A O     1 
HETATM 18003 O  O     . HOH   RA 9 .    ? -17.159 80.665  134.452 1.00 33.11 ? 2248 HOH   A O     1 
HETATM 18004 O  O     . HOH   RA 9 .    ? -31.982 62.002  111.450 1.00 23.08 ? 2249 HOH   A O     1 
HETATM 18005 O  O     . HOH   RA 9 .    ? -56.439 31.809  80.836  1.00 34.09 ? 2250 HOH   A O     1 
HETATM 18006 O  O     . HOH   RA 9 .    ? -33.505 61.688  114.481 1.00 36.19 ? 2251 HOH   A O     1 
HETATM 18007 O  O     . HOH   RA 9 .    ? -38.456 27.700  86.264  1.00 42.51 ? 2252 HOH   A O     1 
HETATM 18008 O  O     . HOH   RA 9 .    ? -37.706 41.115  71.341  1.00 29.06 ? 2253 HOH   A O     1 
HETATM 18009 O  O     . HOH   RA 9 .    ? -8.503  81.017  74.588  1.00 29.73 ? 2254 HOH   A O     1 
HETATM 18010 O  O     . HOH   RA 9 .    ? -60.203 61.432  92.796  1.00 23.00 ? 2255 HOH   A O     1 
HETATM 18011 O  O     . HOH   RA 9 .    ? -51.280 55.290  75.889  1.00 19.44 ? 2256 HOH   A O     1 
HETATM 18012 O  O     . HOH   RA 9 .    ? -48.446 33.387  88.923  1.00 39.59 ? 2257 HOH   A O     1 
HETATM 18013 O  O     . HOH   RA 9 .    ? -63.821 73.172  78.603  1.00 31.62 ? 2258 HOH   A O     1 
HETATM 18014 O  O     . HOH   RA 9 .    ? 17.219  69.295  117.457 1.00 31.10 ? 2259 HOH   A O     1 
HETATM 18015 O  O     . HOH   RA 9 .    ? 0.529   85.372  102.765 1.00 26.02 ? 2260 HOH   A O     1 
HETATM 18016 O  O     . HOH   RA 9 .    ? -28.177 62.200  102.020 1.00 19.31 ? 2261 HOH   A O     1 
HETATM 18017 O  O     . HOH   RA 9 .    ? -35.975 98.868  105.684 1.00 46.22 ? 2262 HOH   A O     1 
HETATM 18018 O  O     . HOH   RA 9 .    ? -23.926 59.809  121.430 1.00 28.48 ? 2263 HOH   A O     1 
HETATM 18019 O  O     . HOH   RA 9 .    ? -14.609 55.304  50.699  1.00 41.45 ? 2264 HOH   A O     1 
HETATM 18020 O  O     . HOH   RA 9 .    ? -23.978 83.404  112.005 1.00 22.77 ? 2265 HOH   A O     1 
HETATM 18021 O  O     . HOH   RA 9 .    ? -54.916 56.511  64.744  1.00 20.87 ? 2266 HOH   A O     1 
HETATM 18022 O  O     . HOH   RA 9 .    ? 12.017  75.524  94.793  1.00 37.26 ? 2267 HOH   A O     1 
HETATM 18023 O  O     . HOH   RA 9 .    ? -10.543 63.373  72.341  1.00 35.07 ? 2268 HOH   A O     1 
HETATM 18024 O  O     . HOH   RA 9 .    ? -30.717 91.082  106.855 1.00 23.45 ? 2269 HOH   A O     1 
HETATM 18025 O  O     . HOH   RA 9 .    ? -38.928 61.060  74.534  1.00 41.67 ? 2270 HOH   A O     1 
HETATM 18026 O  O     . HOH   RA 9 .    ? -11.648 88.959  128.582 1.00 30.91 ? 2271 HOH   A O     1 
HETATM 18027 O  O     . HOH   RA 9 .    ? -51.077 64.806  94.871  1.00 21.65 ? 2272 HOH   A O     1 
HETATM 18028 O  O     . HOH   RA 9 .    ? -11.485 37.775  64.761  1.00 40.95 ? 2273 HOH   A O     1 
HETATM 18029 O  O     . HOH   RA 9 .    ? -44.558 63.396  81.443  1.00 18.49 ? 2274 HOH   A O     1 
HETATM 18030 O  O     . HOH   RA 9 .    ? -51.860 49.221  62.680  1.00 37.51 ? 2275 HOH   A O     1 
HETATM 18031 O  O     . HOH   RA 9 .    ? -31.855 82.702  75.307  1.00 22.41 ? 2276 HOH   A O     1 
HETATM 18032 O  O     . HOH   RA 9 .    ? -5.408  77.935  94.819  1.00 31.89 ? 2277 HOH   A O     1 
HETATM 18033 O  O     . HOH   RA 9 .    ? -60.339 59.614  90.458  1.00 21.91 ? 2278 HOH   A O     1 
HETATM 18034 O  O     . HOH   RA 9 .    ? -41.386 85.825  113.746 1.00 25.25 ? 2279 HOH   A O     1 
HETATM 18035 O  O     . HOH   RA 9 .    ? 23.205  65.883  114.799 1.00 32.53 ? 2280 HOH   A O     1 
HETATM 18036 O  O     . HOH   RA 9 .    ? -32.218 79.515  96.025  1.00 22.66 ? 2281 HOH   A O     1 
HETATM 18037 O  O     . HOH   RA 9 .    ? -50.500 50.548  57.295  1.00 37.85 ? 2282 HOH   A O     1 
HETATM 18038 O  O     . HOH   RA 9 .    ? -49.302 78.187  77.576  1.00 31.52 ? 2283 HOH   A O     1 
HETATM 18039 O  O     . HOH   RA 9 .    ? -57.371 57.802  101.141 1.00 28.82 ? 2284 HOH   A O     1 
HETATM 18040 O  O     . HOH   RA 9 .    ? -7.311  42.931  61.803  1.00 28.39 ? 2285 HOH   A O     1 
HETATM 18041 O  O     . HOH   RA 9 .    ? -55.479 75.297  91.340  1.00 37.40 ? 2286 HOH   A O     1 
HETATM 18042 O  O     . HOH   RA 9 .    ? -45.906 30.631  85.536  1.00 33.08 ? 2287 HOH   A O     1 
HETATM 18043 O  O     . HOH   RA 9 .    ? -44.758 63.620  84.268  1.00 19.67 ? 2288 HOH   A O     1 
HETATM 18044 O  O     . HOH   RA 9 .    ? -14.238 76.013  109.433 1.00 18.31 ? 2289 HOH   A O     1 
HETATM 18045 O  O     . HOH   RA 9 .    ? -6.060  76.293  110.849 1.00 21.89 ? 2290 HOH   A O     1 
HETATM 18046 O  O     . HOH   RA 9 .    ? -11.425 73.455  128.064 1.00 25.90 ? 2291 HOH   A O     1 
HETATM 18047 O  O     . HOH   RA 9 .    ? -18.986 59.362  104.118 1.00 23.49 ? 2292 HOH   A O     1 
HETATM 18048 O  O     . HOH   RA 9 .    ? -11.428 84.797  135.833 1.00 44.63 ? 2293 HOH   A O     1 
HETATM 18049 O  O     . HOH   RA 9 .    ? -46.662 59.834  102.099 1.00 23.33 ? 2294 HOH   A O     1 
HETATM 18050 O  O     . HOH   RA 9 .    ? -38.671 52.752  105.184 1.00 36.29 ? 2295 HOH   A O     1 
HETATM 18051 O  O     . HOH   RA 9 .    ? -4.079  78.317  121.978 1.00 28.20 ? 2296 HOH   A O     1 
HETATM 18052 O  O     . HOH   RA 9 .    ? -22.916 60.631  115.606 1.00 20.83 ? 2297 HOH   A O     1 
HETATM 18053 O  O     . HOH   RA 9 .    ? -14.470 48.928  75.572  1.00 33.54 ? 2298 HOH   A O     1 
HETATM 18054 O  O     . HOH   RA 9 .    ? -42.222 47.821  80.950  1.00 22.81 ? 2299 HOH   A O     1 
HETATM 18055 O  O     . HOH   RA 9 .    ? -0.614  58.417  109.995 1.00 29.24 ? 2300 HOH   A O     1 
HETATM 18056 O  O     . HOH   RA 9 .    ? -19.610 55.353  106.668 1.00 34.11 ? 2301 HOH   A O     1 
HETATM 18057 O  O     . HOH   RA 9 .    ? -27.223 82.463  129.361 1.00 27.24 ? 2302 HOH   A O     1 
HETATM 18058 O  O     . HOH   RA 9 .    ? 17.695  78.543  119.934 1.00 38.12 ? 2303 HOH   A O     1 
HETATM 18059 O  O     . HOH   RA 9 .    ? -27.239 73.343  129.410 1.00 31.04 ? 2304 HOH   A O     1 
HETATM 18060 O  O     . HOH   RA 9 .    ? -27.568 44.800  103.789 1.00 44.01 ? 2305 HOH   A O     1 
HETATM 18061 O  O     . HOH   RA 9 .    ? -34.953 63.497  116.072 1.00 33.81 ? 2306 HOH   A O     1 
HETATM 18062 O  O     . HOH   RA 9 .    ? -53.699 55.462  68.410  1.00 20.71 ? 2307 HOH   A O     1 
HETATM 18063 O  O     . HOH   RA 9 .    ? -31.782 94.810  126.935 1.00 42.88 ? 2308 HOH   A O     1 
HETATM 18064 O  O     . HOH   RA 9 .    ? -14.026 74.931  105.558 1.00 30.15 ? 2309 HOH   A O     1 
HETATM 18065 O  O     . HOH   RA 9 .    ? -26.423 82.757  112.737 1.00 21.75 ? 2310 HOH   A O     1 
HETATM 18066 O  O     . HOH   RA 9 .    ? -39.811 47.419  106.417 1.00 36.14 ? 2311 HOH   A O     1 
HETATM 18067 O  O     . HOH   RA 9 .    ? 13.901  82.148  113.998 1.00 26.89 ? 2312 HOH   A O     1 
HETATM 18068 O  O     . HOH   RA 9 .    ? -32.381 93.069  103.689 1.00 25.17 ? 2313 HOH   A O     1 
HETATM 18069 O  O     . HOH   RA 9 .    ? -45.707 76.118  94.484  1.00 27.25 ? 2314 HOH   A O     1 
HETATM 18070 O  O     . HOH   RA 9 .    ? -56.547 46.069  71.073  1.00 23.21 ? 2315 HOH   A O     1 
HETATM 18071 O  O     . HOH   RA 9 .    ? -36.639 64.740  82.833  1.00 36.69 ? 2316 HOH   A O     1 
HETATM 18072 O  O     . HOH   RA 9 .    ? -16.384 60.647  106.161 1.00 23.24 ? 2317 HOH   A O     1 
HETATM 18073 O  O     . HOH   RA 9 .    ? -49.487 76.059  101.402 1.00 23.40 ? 2318 HOH   A O     1 
HETATM 18074 O  O     . HOH   RA 9 .    ? -48.005 66.372  57.821  1.00 30.01 ? 2319 HOH   A O     1 
HETATM 18075 O  O     . HOH   RA 9 .    ? -23.177 54.813  101.103 1.00 26.16 ? 2320 HOH   A O     1 
HETATM 18076 O  O     . HOH   RA 9 .    ? -51.615 73.186  105.659 1.00 30.66 ? 2321 HOH   A O     1 
HETATM 18077 O  O     . HOH   RA 9 .    ? -20.060 79.001  69.998  1.00 25.75 ? 2322 HOH   A O     1 
HETATM 18078 O  O     . HOH   RA 9 .    ? -12.344 75.097  107.458 1.00 27.27 ? 2323 HOH   A O     1 
HETATM 18079 O  O     . HOH   RA 9 .    ? -58.259 38.177  76.377  1.00 32.90 ? 2324 HOH   A O     1 
HETATM 18080 O  O     . HOH   RA 9 .    ? -19.716 85.475  75.335  1.00 34.34 ? 2325 HOH   A O     1 
HETATM 18081 O  O     . HOH   RA 9 .    ? 20.730  58.562  110.883 1.00 35.47 ? 2326 HOH   A O     1 
HETATM 18082 O  O     . HOH   RA 9 .    ? -26.869 54.167  109.598 1.00 30.12 ? 2327 HOH   A O     1 
HETATM 18083 O  O     . HOH   RA 9 .    ? -19.898 87.171  111.716 1.00 35.07 ? 2328 HOH   A O     1 
HETATM 18084 O  O     . HOH   RA 9 .    ? -34.139 82.674  118.600 1.00 22.63 ? 2329 HOH   A O     1 
HETATM 18085 O  O     . HOH   RA 9 .    ? -20.532 55.052  90.780  1.00 38.11 ? 2330 HOH   A O     1 
HETATM 18086 O  O     . HOH   RA 9 .    ? -4.992  54.671  107.947 1.00 22.88 ? 2331 HOH   A O     1 
HETATM 18087 O  O     . HOH   RA 9 .    ? -31.716 84.288  99.180  1.00 22.09 ? 2332 HOH   A O     1 
HETATM 18088 O  O     . HOH   RA 9 .    ? 5.214   67.329  95.729  1.00 26.65 ? 2333 HOH   A O     1 
HETATM 18089 O  O     . HOH   RA 9 .    ? 5.874   63.226  96.980  1.00 21.39 ? 2334 HOH   A O     1 
HETATM 18090 O  O     . HOH   RA 9 .    ? -33.248 45.776  84.402  1.00 32.24 ? 2335 HOH   A O     1 
HETATM 18091 O  O     . HOH   RA 9 .    ? -40.745 49.180  63.837  1.00 28.84 ? 2336 HOH   A O     1 
HETATM 18092 O  O     . HOH   RA 9 .    ? 19.523  82.181  112.978 1.00 32.37 ? 2337 HOH   A O     1 
HETATM 18093 O  O     . HOH   RA 9 .    ? -32.285 59.998  109.498 1.00 26.30 ? 2338 HOH   A O     1 
HETATM 18094 O  O     . HOH   RA 9 .    ? -27.045 89.480  77.313  1.00 26.61 ? 2339 HOH   A O     1 
HETATM 18095 O  O     . HOH   RA 9 .    ? -39.229 39.851  98.585  1.00 30.01 ? 2340 HOH   A O     1 
HETATM 18096 O  O     . HOH   RA 9 .    ? -3.145  90.349  100.664 1.00 36.47 ? 2341 HOH   A O     1 
HETATM 18097 O  O     . HOH   RA 9 .    ? -48.232 82.988  111.216 1.00 29.35 ? 2342 HOH   A O     1 
HETATM 18098 O  O     . HOH   RA 9 .    ? -10.109 69.390  133.032 1.00 34.18 ? 2343 HOH   A O     1 
HETATM 18099 O  O     . HOH   RA 9 .    ? 14.671  87.995  105.818 1.00 34.45 ? 2344 HOH   A O     1 
HETATM 18100 O  O     . HOH   RA 9 .    ? -48.660 29.478  74.133  1.00 42.80 ? 2345 HOH   A O     1 
HETATM 18101 O  O     . HOH   RA 9 .    ? -22.709 67.611  97.263  1.00 20.11 ? 2346 HOH   A O     1 
HETATM 18102 O  O     . HOH   RA 9 .    ? -37.910 50.568  98.356  1.00 25.78 ? 2347 HOH   A O     1 
HETATM 18103 O  O     . HOH   RA 9 .    ? -23.283 63.981  105.985 1.00 18.59 ? 2348 HOH   A O     1 
HETATM 18104 O  O     . HOH   RA 9 .    ? -46.740 82.353  101.398 1.00 23.34 ? 2349 HOH   A O     1 
HETATM 18105 O  O     . HOH   RA 9 .    ? -24.788 89.129  99.419  1.00 19.19 ? 2350 HOH   A O     1 
HETATM 18106 O  O     . HOH   RA 9 .    ? 21.577  67.898  116.547 1.00 38.04 ? 2351 HOH   A O     1 
HETATM 18107 O  O     . HOH   RA 9 .    ? 9.382   57.241  97.228  1.00 31.56 ? 2352 HOH   A O     1 
HETATM 18108 O  O     . HOH   RA 9 .    ? -9.561  87.091  128.633 1.00 30.55 ? 2353 HOH   A O     1 
HETATM 18109 O  O     . HOH   RA 9 .    ? -23.431 62.803  66.067  1.00 41.25 ? 2354 HOH   A O     1 
HETATM 18110 O  O     . HOH   RA 9 .    ? -55.908 55.779  94.923  1.00 20.61 ? 2355 HOH   A O     1 
HETATM 18111 O  O     . HOH   RA 9 .    ? 11.159  67.359  116.520 1.00 26.79 ? 2356 HOH   A O     1 
HETATM 18112 O  O     . HOH   RA 9 .    ? -41.933 67.911  91.077  1.00 20.53 ? 2357 HOH   A O     1 
HETATM 18113 O  O     . HOH   RA 9 .    ? -18.038 57.669  96.926  1.00 20.12 ? 2358 HOH   A O     1 
HETATM 18114 O  O     . HOH   RA 9 .    ? -44.225 73.827  74.947  1.00 26.25 ? 2359 HOH   A O     1 
HETATM 18115 O  O     . HOH   RA 9 .    ? -16.573 95.803  89.797  1.00 37.19 ? 2360 HOH   A O     1 
HETATM 18116 O  O     . HOH   RA 9 .    ? -13.766 75.002  135.361 1.00 36.80 ? 2361 HOH   A O     1 
HETATM 18117 O  O     . HOH   RA 9 .    ? -6.344  68.864  92.200  1.00 33.59 ? 2362 HOH   A O     1 
HETATM 18118 O  O     . HOH   RA 9 .    ? -6.771  42.298  66.125  1.00 28.31 ? 2363 HOH   A O     1 
HETATM 18119 O  O     . HOH   RA 9 .    ? -1.971  53.956  104.385 1.00 28.59 ? 2364 HOH   A O     1 
HETATM 18120 O  O     . HOH   RA 9 .    ? -52.835 63.664  98.387  1.00 20.77 ? 2365 HOH   A O     1 
HETATM 18121 O  O     . HOH   RA 9 .    ? -45.415 86.923  111.496 1.00 38.32 ? 2366 HOH   A O     1 
HETATM 18122 O  O     . HOH   RA 9 .    ? -49.088 83.372  108.637 1.00 34.18 ? 2367 HOH   A O     1 
HETATM 18123 O  O     . HOH   RA 9 .    ? -2.748  62.948  77.294  1.00 27.86 ? 2368 HOH   A O     1 
HETATM 18124 O  O     . HOH   RA 9 .    ? -8.610  60.269  106.902 1.00 20.99 ? 2369 HOH   A O     1 
HETATM 18125 O  O     . HOH   RA 9 .    ? -39.677 84.934  103.787 1.00 29.50 ? 2370 HOH   A O     1 
HETATM 18126 O  O     . HOH   RA 9 .    ? -20.696 70.936  75.130  1.00 25.95 ? 2371 HOH   A O     1 
HETATM 18127 O  O     . HOH   RA 9 .    ? -6.186  54.906  105.048 1.00 36.92 ? 2372 HOH   A O     1 
HETATM 18128 O  O     . HOH   RA 9 .    ? -50.692 69.858  100.280 1.00 20.82 ? 2373 HOH   A O     1 
HETATM 18129 O  O     . HOH   RA 9 .    ? -49.781 68.594  92.059  1.00 20.54 ? 2374 HOH   A O     1 
HETATM 18130 O  O     . HOH   RA 9 .    ? -41.086 71.717  114.301 1.00 29.00 ? 2375 HOH   A O     1 
HETATM 18131 O  O     . HOH   RA 9 .    ? -18.147 79.756  127.031 1.00 21.40 ? 2376 HOH   A O     1 
HETATM 18132 O  O     . HOH   RA 9 .    ? -47.727 80.097  95.758  1.00 39.57 ? 2377 HOH   A O     1 
HETATM 18133 O  O     . HOH   RA 9 .    ? -30.649 81.900  129.347 1.00 37.43 ? 2378 HOH   A O     1 
HETATM 18134 O  O     . HOH   RA 9 .    ? -24.375 93.049  104.875 1.00 34.79 ? 2379 HOH   A O     1 
HETATM 18135 O  O     . HOH   RA 9 .    ? 8.451   89.839  119.845 1.00 37.67 ? 2380 HOH   A O     1 
HETATM 18136 O  O     . HOH   RA 9 .    ? -25.772 63.922  104.509 1.00 21.93 ? 2381 HOH   A O     1 
HETATM 18137 O  O     . HOH   RA 9 .    ? -18.017 74.402  131.810 1.00 36.16 ? 2382 HOH   A O     1 
HETATM 18138 O  O     . HOH   RA 9 .    ? -0.351  82.427  113.123 1.00 35.39 ? 2383 HOH   A O     1 
HETATM 18139 O  O     . HOH   RA 9 .    ? 4.066   58.016  104.705 1.00 23.48 ? 2384 HOH   A O     1 
HETATM 18140 O  O     . HOH   RA 9 .    ? -34.629 75.863  83.145  1.00 35.66 ? 2385 HOH   A O     1 
HETATM 18141 O  O     . HOH   RA 9 .    ? -11.663 72.189  76.167  1.00 28.56 ? 2386 HOH   A O     1 
HETATM 18142 O  O     . HOH   RA 9 .    ? -0.534  75.903  122.583 1.00 32.68 ? 2387 HOH   A O     1 
HETATM 18143 O  O     . HOH   RA 9 .    ? -2.188  74.815  83.762  1.00 33.51 ? 2388 HOH   A O     1 
HETATM 18144 O  O     . HOH   RA 9 .    ? 18.293  57.505  105.101 1.00 33.79 ? 2389 HOH   A O     1 
HETATM 18145 O  O     . HOH   RA 9 .    ? -47.092 60.321  85.122  1.00 18.58 ? 2390 HOH   A O     1 
HETATM 18146 O  O     . HOH   RA 9 .    ? -25.241 62.736  109.780 1.00 23.15 ? 2391 HOH   A O     1 
HETATM 18147 O  O     . HOH   RA 9 .    ? -13.949 58.742  109.870 1.00 37.89 ? 2392 HOH   A O     1 
HETATM 18148 O  O     . HOH   RA 9 .    ? -42.176 56.806  89.334  1.00 18.28 ? 2393 HOH   A O     1 
HETATM 18149 O  O     . HOH   RA 9 .    ? 9.458   79.236  122.094 1.00 30.07 ? 2394 HOH   A O     1 
HETATM 18150 O  O     . HOH   RA 9 .    ? -8.978  45.188  55.985  1.00 37.61 ? 2395 HOH   A O     1 
HETATM 18151 O  O     . HOH   RA 9 .    ? -23.689 63.685  91.376  1.00 19.89 ? 2396 HOH   A O     1 
HETATM 18152 O  O     . HOH   RA 9 .    ? -0.453  66.199  94.057  1.00 35.89 ? 2397 HOH   A O     1 
HETATM 18153 O  O     . HOH   RA 9 .    ? -49.512 32.878  91.559  1.00 42.23 ? 2398 HOH   A O     1 
HETATM 18154 O  O     . HOH   RA 9 .    ? -55.261 36.518  76.188  1.00 34.25 ? 2399 HOH   A O     1 
HETATM 18155 O  O     . HOH   RA 9 .    ? -46.473 66.574  93.875  1.00 20.27 ? 2400 HOH   A O     1 
HETATM 18156 O  O     . HOH   RA 9 .    ? -10.448 67.188  127.458 1.00 36.81 ? 2401 HOH   A O     1 
HETATM 18157 O  O     . HOH   RA 9 .    ? -61.168 36.466  78.704  1.00 42.40 ? 2402 HOH   A O     1 
HETATM 18158 O  O     . HOH   RA 9 .    ? -36.927 80.696  78.781  1.00 20.38 ? 2403 HOH   A O     1 
HETATM 18159 O  O     . HOH   RA 9 .    ? -32.471 87.208  76.324  1.00 32.35 ? 2404 HOH   A O     1 
HETATM 18160 O  O     . HOH   RA 9 .    ? -52.121 53.922  100.257 1.00 21.98 ? 2405 HOH   A O     1 
HETATM 18161 O  O     . HOH   RA 9 .    ? -16.551 76.839  108.309 1.00 21.73 ? 2406 HOH   A O     1 
HETATM 18162 O  O     . HOH   RA 9 .    ? -42.857 66.315  63.296  1.00 33.99 ? 2407 HOH   A O     1 
HETATM 18163 O  O     . HOH   RA 9 .    ? -38.134 62.447  105.309 1.00 29.79 ? 2408 HOH   A O     1 
HETATM 18164 O  O     . HOH   RA 9 .    ? -67.381 60.379  69.866  1.00 27.16 ? 2409 HOH   A O     1 
HETATM 18165 O  O     . HOH   RA 9 .    ? -59.170 51.940  66.037  1.00 21.97 ? 2410 HOH   A O     1 
HETATM 18166 O  O     . HOH   RA 9 .    ? -31.161 71.668  82.703  1.00 35.27 ? 2411 HOH   A O     1 
HETATM 18167 O  O     . HOH   RA 9 .    ? -30.627 96.006  104.736 1.00 25.23 ? 2412 HOH   A O     1 
HETATM 18168 O  O     . HOH   RA 9 .    ? -25.401 58.641  118.197 1.00 38.53 ? 2413 HOH   A O     1 
HETATM 18169 O  O     . HOH   RA 9 .    ? -8.801  78.407  131.304 1.00 36.15 ? 2414 HOH   A O     1 
HETATM 18170 O  O     . HOH   RA 9 .    ? -61.148 55.379  67.544  1.00 21.88 ? 2415 HOH   A O     1 
HETATM 18171 O  O     . HOH   RA 9 .    ? -1.522  58.236  96.254  1.00 35.47 ? 2416 HOH   A O     1 
HETATM 18172 O  O     . HOH   RA 9 .    ? -44.849 85.436  99.669  1.00 32.30 ? 2417 HOH   A O     1 
HETATM 18173 O  O     . HOH   RA 9 .    ? -39.307 88.916  90.808  1.00 30.06 ? 2418 HOH   A O     1 
HETATM 18174 O  O     . HOH   RA 9 .    ? -52.233 61.953  94.762  1.00 20.11 ? 2419 HOH   A O     1 
HETATM 18175 O  O     . HOH   RA 9 .    ? -8.728  92.797  82.295  1.00 49.57 ? 2420 HOH   A O     1 
HETATM 18176 O  O     . HOH   RA 9 .    ? -7.936  77.450  91.700  1.00 27.32 ? 2421 HOH   A O     1 
HETATM 18177 O  O     . HOH   RA 9 .    ? -10.646 67.989  107.776 1.00 17.55 ? 2422 HOH   A O     1 
HETATM 18178 O  O     . HOH   RA 9 .    ? -8.209  60.157  93.901  1.00 33.95 ? 2423 HOH   A O     1 
HETATM 18179 O  O     . HOH   RA 9 .    ? -34.454 66.747  101.478 1.00 21.66 ? 2424 HOH   A O     1 
HETATM 18180 O  O     . HOH   RA 9 .    ? -41.678 88.775  96.688  1.00 27.80 ? 2425 HOH   A O     1 
HETATM 18181 O  O     . HOH   RA 9 .    ? -6.524  93.671  113.133 1.00 30.70 ? 2426 HOH   A O     1 
HETATM 18182 O  O     . HOH   RA 9 .    ? -41.442 70.745  95.329  1.00 25.56 ? 2427 HOH   A O     1 
HETATM 18183 O  O     . HOH   RA 9 .    ? 7.241   84.930  94.117  1.00 39.17 ? 2428 HOH   A O     1 
HETATM 18184 O  O     . HOH   RA 9 .    ? -27.196 65.215  99.941  1.00 24.07 ? 2429 HOH   A O     1 
HETATM 18185 O  O     . HOH   RA 9 .    ? -23.442 86.471  73.537  1.00 40.03 ? 2430 HOH   A O     1 
HETATM 18186 O  O     . HOH   RA 9 .    ? -36.408 59.082  94.024  1.00 18.32 ? 2431 HOH   A O     1 
HETATM 18187 O  O     . HOH   RA 9 .    ? -45.781 78.332  96.048  1.00 20.78 ? 2432 HOH   A O     1 
HETATM 18188 O  O     . HOH   RA 9 .    ? -32.953 78.122  74.287  1.00 29.20 ? 2433 HOH   A O     1 
HETATM 18189 O  O     . HOH   RA 9 .    ? -22.424 96.062  129.529 1.00 36.35 ? 2434 HOH   A O     1 
HETATM 18190 O  O     . HOH   RA 9 .    ? -25.174 82.888  72.268  1.00 38.52 ? 2435 HOH   A O     1 
HETATM 18191 O  O     . HOH   RA 9 .    ? -9.635  74.507  103.828 1.00 30.51 ? 2436 HOH   A O     1 
HETATM 18192 O  O     . HOH   RA 9 .    ? -59.618 60.791  75.921  1.00 18.70 ? 2437 HOH   A O     1 
HETATM 18193 O  O     . HOH   RA 9 .    ? 17.058  71.464  118.878 1.00 35.16 ? 2438 HOH   A O     1 
HETATM 18194 O  O     . HOH   RA 9 .    ? -19.740 91.239  96.975  1.00 35.60 ? 2439 HOH   A O     1 
HETATM 18195 O  O     . HOH   RA 9 .    ? -46.063 56.062  87.362  1.00 16.80 ? 2440 HOH   A O     1 
HETATM 18196 O  O     . HOH   RA 9 .    ? -4.010  79.390  110.932 1.00 32.18 ? 2441 HOH   A O     1 
HETATM 18197 O  O     . HOH   RA 9 .    ? -25.795 94.123  77.909  1.00 30.97 ? 2442 HOH   A O     1 
HETATM 18198 O  O     . HOH   RA 9 .    ? -45.993 72.760  64.377  1.00 19.16 ? 2443 HOH   A O     1 
HETATM 18199 O  O     . HOH   RA 9 .    ? -40.611 81.887  110.602 1.00 25.20 ? 2444 HOH   A O     1 
HETATM 18200 O  O     . HOH   RA 9 .    ? -3.006  44.276  58.329  1.00 27.82 ? 2445 HOH   A O     1 
HETATM 18201 O  O     . HOH   RA 9 .    ? 21.138  57.489  104.870 1.00 35.15 ? 2446 HOH   A O     1 
HETATM 18202 O  O     . HOH   RA 9 .    ? -4.011  55.124  61.373  1.00 33.29 ? 2447 HOH   A O     1 
HETATM 18203 O  O     . HOH   RA 9 .    ? -43.051 85.377  97.207  1.00 28.94 ? 2448 HOH   A O     1 
HETATM 18204 O  O     . HOH   RA 9 .    ? 14.628  55.463  110.601 1.00 41.53 ? 2449 HOH   A O     1 
HETATM 18205 O  O     . HOH   RA 9 .    ? -61.565 70.211  83.148  1.00 25.10 ? 2450 HOH   A O     1 
HETATM 18206 O  O     . HOH   RA 9 .    ? -34.515 76.629  95.996  1.00 35.58 ? 2451 HOH   A O     1 
HETATM 18207 O  O     . HOH   RA 9 .    ? -8.019  93.061  105.688 1.00 28.61 ? 2452 HOH   A O     1 
HETATM 18208 O  O     . HOH   RA 9 .    ? -43.903 55.790  94.971  1.00 17.55 ? 2453 HOH   A O     1 
HETATM 18209 O  O     . HOH   RA 9 .    ? -7.109  62.578  106.895 1.00 20.74 ? 2454 HOH   A O     1 
HETATM 18210 O  O     . HOH   RA 9 .    ? -63.547 52.536  89.920  1.00 31.29 ? 2455 HOH   A O     1 
HETATM 18211 O  O     . HOH   RA 9 .    ? -31.473 59.134  63.376  1.00 36.31 ? 2456 HOH   A O     1 
HETATM 18212 O  O     . HOH   RA 9 .    ? -0.659  70.269  95.725  1.00 34.84 ? 2457 HOH   A O     1 
HETATM 18213 O  O     . HOH   RA 9 .    ? -50.576 52.174  63.870  1.00 22.60 ? 2458 HOH   A O     1 
HETATM 18214 O  O     . HOH   RA 9 .    ? -36.418 95.072  93.783  1.00 27.44 ? 2459 HOH   A O     1 
HETATM 18215 O  O     . HOH   RA 9 .    ? -0.913  83.794  117.489 1.00 27.60 ? 2460 HOH   A O     1 
HETATM 18216 O  O     . HOH   RA 9 .    ? -60.995 52.886  91.215  1.00 28.11 ? 2461 HOH   A O     1 
HETATM 18217 O  O     . HOH   RA 9 .    ? -27.968 88.101  74.323  1.00 42.92 ? 2462 HOH   A O     1 
HETATM 18218 O  O     . HOH   RA 9 .    ? -55.375 75.231  75.000  1.00 22.56 ? 2463 HOH   A O     1 
HETATM 18219 O  O     . HOH   RA 9 .    ? -35.265 51.956  85.139  1.00 17.39 ? 2464 HOH   A O     1 
HETATM 18220 O  O     . HOH   RA 9 .    ? -1.317  77.068  87.463  1.00 30.44 ? 2465 HOH   A O     1 
HETATM 18221 O  O     . HOH   RA 9 .    ? -22.058 67.637  80.995  1.00 30.75 ? 2466 HOH   A O     1 
HETATM 18222 O  O     . HOH   RA 9 .    ? -4.284  59.588  118.136 1.00 20.90 ? 2467 HOH   A O     1 
HETATM 18223 O  O     . HOH   RA 9 .    ? -1.105  77.854  114.556 1.00 35.63 ? 2468 HOH   A O     1 
HETATM 18224 O  O     . HOH   RA 9 .    ? 16.768  58.013  102.741 1.00 26.86 ? 2469 HOH   A O     1 
HETATM 18225 O  O     . HOH   RA 9 .    ? -38.777 35.456  85.379  1.00 35.52 ? 2470 HOH   A O     1 
HETATM 18226 O  O     . HOH   RA 9 .    ? -34.105 69.590  76.145  1.00 30.62 ? 2471 HOH   A O     1 
HETATM 18227 O  O     . HOH   RA 9 .    ? -65.402 64.654  81.231  1.00 22.62 ? 2472 HOH   A O     1 
HETATM 18228 O  O     . HOH   RA 9 .    ? -45.695 65.269  91.767  1.00 19.12 ? 2473 HOH   A O     1 
HETATM 18229 O  O     . HOH   RA 9 .    ? -18.227 61.248  66.585  1.00 36.58 ? 2474 HOH   A O     1 
HETATM 18230 O  O     . HOH   RA 9 .    ? -53.699 44.949  91.934  1.00 35.94 ? 2475 HOH   A O     1 
HETATM 18231 O  O     . HOH   RA 9 .    ? -47.785 57.769  86.285  1.00 16.05 ? 2476 HOH   A O     1 
HETATM 18232 O  O     . HOH   RA 9 .    ? -11.935 64.633  129.563 1.00 32.42 ? 2477 HOH   A O     1 
HETATM 18233 O  O     . HOH   RA 9 .    ? -38.546 73.334  90.178  1.00 30.72 ? 2478 HOH   A O     1 
HETATM 18234 O  O     . HOH   RA 9 .    ? -20.103 86.881  91.232  1.00 23.27 ? 2479 HOH   A O     1 
HETATM 18235 O  O     . HOH   RA 9 .    ? -41.104 27.927  70.256  1.00 39.86 ? 2480 HOH   A O     1 
HETATM 18236 O  O     . HOH   RA 9 .    ? -65.623 59.079  75.726  1.00 27.08 ? 2481 HOH   A O     1 
HETATM 18237 O  O     . HOH   RA 9 .    ? -41.435 64.206  103.591 1.00 22.63 ? 2482 HOH   A O     1 
HETATM 18238 O  O     . HOH   RA 9 .    ? 12.931  67.369  93.121  1.00 35.93 ? 2483 HOH   A O     1 
HETATM 18239 O  O     . HOH   RA 9 .    ? 15.285  83.127  110.989 1.00 27.85 ? 2484 HOH   A O     1 
HETATM 18240 O  O     . HOH   RA 9 .    ? -61.994 61.763  68.057  1.00 28.84 ? 2485 HOH   A O     1 
HETATM 18241 O  O     . HOH   RA 9 .    ? -0.132  85.638  106.142 1.00 36.63 ? 2486 HOH   A O     1 
HETATM 18242 O  O     . HOH   RA 9 .    ? -1.164  79.339  99.511  1.00 29.75 ? 2487 HOH   A O     1 
HETATM 18243 O  O     . HOH   RA 9 .    ? -31.855 88.578  95.052  1.00 21.89 ? 2488 HOH   A O     1 
HETATM 18244 O  O     . HOH   RA 9 .    ? -54.934 47.729  69.767  1.00 24.60 ? 2489 HOH   A O     1 
HETATM 18245 O  O     . HOH   RA 9 .    ? -14.645 67.629  72.796  1.00 26.48 ? 2490 HOH   A O     1 
HETATM 18246 O  O     . HOH   RA 9 .    ? 20.767  62.070  98.836  1.00 28.82 ? 2491 HOH   A O     1 
HETATM 18247 O  O     . HOH   RA 9 .    ? -63.633 70.880  70.880  1.00 28.43 ? 2492 HOH   A O     1 
HETATM 18248 O  O     . HOH   RA 9 .    ? 5.413   55.366  96.724  1.00 31.54 ? 2493 HOH   A O     1 
HETATM 18249 O  O     . HOH   RA 9 .    ? -6.647  70.632  93.865  1.00 29.52 ? 2494 HOH   A O     1 
HETATM 18250 O  O     . HOH   RA 9 .    ? -26.501 80.584  101.475 1.00 27.11 ? 2495 HOH   A O     1 
HETATM 18251 O  O     . HOH   RA 9 .    ? -24.747 69.505  74.368  1.00 32.30 ? 2496 HOH   A O     1 
HETATM 18252 O  O     . HOH   RA 9 .    ? 6.883   61.137  102.957 1.00 20.54 ? 2497 HOH   A O     1 
HETATM 18253 O  O     . HOH   RA 9 .    ? -39.358 78.435  99.736  1.00 23.59 ? 2498 HOH   A O     1 
HETATM 18254 O  O     . HOH   RA 9 .    ? 7.073   80.339  122.943 1.00 35.19 ? 2499 HOH   A O     1 
HETATM 18255 O  O     . HOH   RA 9 .    ? -30.677 66.613  126.883 1.00 33.87 ? 2500 HOH   A O     1 
HETATM 18256 O  O     . HOH   RA 9 .    ? -54.670 29.624  80.271  1.00 38.21 ? 2501 HOH   A O     1 
HETATM 18257 O  O     . HOH   RA 9 .    ? -59.991 47.133  88.625  1.00 29.65 ? 2502 HOH   A O     1 
HETATM 18258 O  O     . HOH   RA 9 .    ? -15.638 44.199  76.467  1.00 42.65 ? 2503 HOH   A O     1 
HETATM 18259 O  O     . HOH   RA 9 .    ? -49.907 72.451  101.022 1.00 23.55 ? 2504 HOH   A O     1 
HETATM 18260 O  O     . HOH   RA 9 .    ? -4.075  73.544  76.611  1.00 31.16 ? 2505 HOH   A O     1 
HETATM 18261 O  O     . HOH   RA 9 .    ? -64.240 45.064  78.166  1.00 37.98 ? 2506 HOH   A O     1 
HETATM 18262 O  O     . HOH   RA 9 .    ? -47.723 59.210  82.708  1.00 16.18 ? 2507 HOH   A O     1 
HETATM 18263 O  O     . HOH   RA 9 .    ? -30.196 81.298  123.002 1.00 25.00 ? 2508 HOH   A O     1 
HETATM 18264 O  O     . HOH   RA 9 .    ? -3.976  76.773  124.274 1.00 30.19 ? 2509 HOH   A O     1 
HETATM 18265 O  O     . HOH   RA 9 .    ? -20.771 81.652  115.855 1.00 21.21 ? 2510 HOH   A O     1 
HETATM 18266 O  O     . HOH   RA 9 .    ? 10.847  67.075  111.518 1.00 33.58 ? 2511 HOH   A O     1 
HETATM 18267 O  O     . HOH   RA 9 .    ? -28.974 76.984  72.554  1.00 33.65 ? 2512 HOH   A O     1 
HETATM 18268 O  O     . HOH   RA 9 .    ? 8.024   67.812  114.245 1.00 29.97 ? 2513 HOH   A O     1 
HETATM 18269 O  O     . HOH   RA 9 .    ? -25.036 90.220  132.979 1.00 39.33 ? 2514 HOH   A O     1 
HETATM 18270 O  O     . HOH   RA 9 .    ? -38.399 70.522  81.665  1.00 28.29 ? 2515 HOH   A O     1 
HETATM 18271 O  O     . HOH   RA 9 .    ? 11.210  61.226  115.017 1.00 36.86 ? 2516 HOH   A O     1 
HETATM 18272 O  O     . HOH   RA 9 .    ? -42.363 78.010  75.795  1.00 27.47 ? 2517 HOH   A O     1 
HETATM 18273 O  O     . HOH   RA 9 .    ? -21.163 59.555  122.210 1.00 25.83 ? 2518 HOH   A O     1 
HETATM 18274 O  O     . HOH   RA 9 .    ? -27.636 71.086  89.701  1.00 25.81 ? 2519 HOH   A O     1 
HETATM 18275 O  O     . HOH   RA 9 .    ? -38.279 61.691  91.792  1.00 19.20 ? 2520 HOH   A O     1 
HETATM 18276 O  O     . HOH   RA 9 .    ? -52.523 72.708  64.526  1.00 25.48 ? 2521 HOH   A O     1 
HETATM 18277 O  O     . HOH   RA 9 .    ? -22.579 98.572  99.922  1.00 30.00 ? 2522 HOH   A O     1 
HETATM 18278 O  O     . HOH   RA 9 .    ? -47.368 70.740  111.133 1.00 33.94 ? 2523 HOH   A O     1 
HETATM 18279 O  O     . HOH   RA 9 .    ? -6.346  71.309  103.506 1.00 29.80 ? 2524 HOH   A O     1 
HETATM 18280 O  O     . HOH   RA 9 .    ? -55.007 47.587  94.862  1.00 39.31 ? 2525 HOH   A O     1 
HETATM 18281 O  O     . HOH   RA 9 .    ? -46.649 49.016  93.091  1.00 19.28 ? 2526 HOH   A O     1 
HETATM 18282 O  O     . HOH   RA 9 .    ? -4.256  70.029  106.299 1.00 31.71 ? 2527 HOH   A O     1 
HETATM 18283 O  O     . HOH   RA 9 .    ? -20.293 66.335  80.791  1.00 25.76 ? 2528 HOH   A O     1 
HETATM 18284 O  O     . HOH   RA 9 .    ? -40.625 58.540  79.931  1.00 28.65 ? 2529 HOH   A O     1 
HETATM 18285 O  O     . HOH   RA 9 .    ? -9.615  91.949  117.555 1.00 37.36 ? 2530 HOH   A O     1 
HETATM 18286 O  O     . HOH   RA 9 .    ? -18.776 59.951  69.554  1.00 26.75 ? 2531 HOH   A O     1 
HETATM 18287 O  O     . HOH   RA 9 .    ? -15.678 56.633  83.949  1.00 42.34 ? 2532 HOH   A O     1 
HETATM 18288 O  O     . HOH   RA 9 .    ? -35.100 66.173  94.249  1.00 41.02 ? 2533 HOH   A O     1 
HETATM 18289 O  O     . HOH   RA 9 .    ? -8.462  65.460  113.657 1.00 18.98 ? 2534 HOH   A O     1 
HETATM 18290 O  O     . HOH   RA 9 .    ? -39.662 61.636  94.465  1.00 19.85 ? 2535 HOH   A O     1 
HETATM 18291 O  O     . HOH   RA 9 .    ? -19.882 52.808  77.992  1.00 33.04 ? 2536 HOH   A O     1 
HETATM 18292 O  O     . HOH   RA 9 .    ? 14.151  78.291  120.953 1.00 29.98 ? 2537 HOH   A O     1 
HETATM 18293 O  O     . HOH   RA 9 .    ? -24.302 60.021  77.720  1.00 47.31 ? 2538 HOH   A O     1 
HETATM 18294 O  O     . HOH   RA 9 .    ? -3.998  73.558  116.620 1.00 29.49 ? 2539 HOH   A O     1 
HETATM 18295 O  O     . HOH   RA 9 .    ? -46.283 54.378  89.702  1.00 18.57 ? 2540 HOH   A O     1 
HETATM 18296 O  O     . HOH   RA 9 .    ? -7.829  75.656  70.029  1.00 36.16 ? 2541 HOH   A O     1 
HETATM 18297 O  O     . HOH   RA 9 .    ? -47.286 49.117  95.779  1.00 20.34 ? 2542 HOH   A O     1 
HETATM 18298 O  O     . HOH   RA 9 .    ? -23.955 67.722  104.961 1.00 20.01 ? 2543 HOH   A O     1 
HETATM 18299 O  O     . HOH   RA 9 .    ? -32.088 89.268  108.742 1.00 27.22 ? 2544 HOH   A O     1 
HETATM 18300 O  O     . HOH   RA 9 .    ? -15.806 68.318  96.448  1.00 17.54 ? 2545 HOH   A O     1 
HETATM 18301 O  O     . HOH   RA 9 .    ? -45.268 62.697  92.612  1.00 15.77 ? 2546 HOH   A O     1 
HETATM 18302 O  O     . HOH   RA 9 .    ? -41.786 55.352  104.839 1.00 34.76 ? 2547 HOH   A O     1 
HETATM 18303 O  O     . HOH   RA 9 .    ? -45.096 57.426  101.959 1.00 25.81 ? 2548 HOH   A O     1 
HETATM 18304 O  O     . HOH   RA 9 .    ? -25.486 70.445  131.203 1.00 34.83 ? 2549 HOH   A O     1 
HETATM 18305 O  O     . HOH   RA 9 .    ? -13.409 55.451  103.321 1.00 36.91 ? 2550 HOH   A O     1 
HETATM 18306 O  O     . HOH   RA 9 .    ? -18.670 86.242  109.065 1.00 31.11 ? 2551 HOH   A O     1 
HETATM 18307 O  O     . HOH   RA 9 .    ? -41.101 90.688  98.588  1.00 27.77 ? 2552 HOH   A O     1 
HETATM 18308 O  O     . HOH   RA 9 .    ? -28.547 55.053  111.361 1.00 33.72 ? 2553 HOH   A O     1 
HETATM 18309 O  O     . HOH   RA 9 .    ? 16.424  65.216  119.389 1.00 29.37 ? 2554 HOH   A O     1 
HETATM 18310 O  O     . HOH   RA 9 .    ? 23.227  63.243  115.231 1.00 23.30 ? 2555 HOH   A O     1 
HETATM 18311 O  O     . HOH   RA 9 .    ? -50.005 56.670  71.683  1.00 25.34 ? 2556 HOH   A O     1 
HETATM 18312 O  O     . HOH   RA 9 .    ? -38.756 71.181  84.437  1.00 29.34 ? 2557 HOH   A O     1 
HETATM 18313 O  O     . HOH   RA 9 .    ? -47.774 64.278  96.778  1.00 22.63 ? 2558 HOH   A O     1 
HETATM 18314 O  O     . HOH   RA 9 .    ? -57.987 57.904  63.054  1.00 25.25 ? 2559 HOH   A O     1 
HETATM 18315 O  O     . HOH   RA 9 .    ? -3.203  82.416  97.107  1.00 29.59 ? 2560 HOH   A O     1 
HETATM 18316 O  O     . HOH   RA 9 .    ? -33.966 90.685  122.119 1.00 27.67 ? 2561 HOH   A O     1 
HETATM 18317 O  O     . HOH   RA 9 .    ? 0.494   85.150  111.393 1.00 32.56 ? 2562 HOH   A O     1 
HETATM 18318 O  O     . HOH   RA 9 .    ? -54.240 42.785  97.165  1.00 36.55 ? 2563 HOH   A O     1 
HETATM 18319 O  O     . HOH   RA 9 .    ? -57.106 60.226  61.070  1.00 20.43 ? 2564 HOH   A O     1 
HETATM 18320 O  O     . HOH   RA 9 .    ? 10.879  57.409  105.528 1.00 32.13 ? 2565 HOH   A O     1 
HETATM 18321 O  O     . HOH   RA 9 .    ? -12.378 77.567  90.716  1.00 18.81 ? 2566 HOH   A O     1 
HETATM 18322 O  O     . HOH   RA 9 .    ? -28.390 75.712  102.224 1.00 32.38 ? 2567 HOH   A O     1 
HETATM 18323 O  O     . HOH   RA 9 .    ? -26.453 84.583  73.761  1.00 33.48 ? 2568 HOH   A O     1 
HETATM 18324 O  O     . HOH   RA 9 .    ? -48.263 75.277  95.407  1.00 20.32 ? 2569 HOH   A O     1 
HETATM 18325 O  O     . HOH   RA 9 .    ? -14.361 85.445  76.905  1.00 33.39 ? 2570 HOH   A O     1 
HETATM 18326 O  O     . HOH   RA 9 .    ? -35.462 76.164  92.531  1.00 36.46 ? 2571 HOH   A O     1 
HETATM 18327 O  O     . HOH   RA 9 .    ? -41.368 71.626  64.235  1.00 31.45 ? 2572 HOH   A O     1 
HETATM 18328 O  O     . HOH   RA 9 .    ? -45.054 73.126  114.513 1.00 43.23 ? 2573 HOH   A O     1 
HETATM 18329 O  O     . HOH   RA 9 .    ? -35.132 94.995  96.091  1.00 23.92 ? 2574 HOH   A O     1 
HETATM 18330 O  O     . HOH   RA 9 .    ? -50.282 66.484  106.366 1.00 33.44 ? 2575 HOH   A O     1 
HETATM 18331 O  O     . HOH   RA 9 .    ? -34.040 56.521  105.136 1.00 23.90 ? 2576 HOH   A O     1 
HETATM 18332 O  O     . HOH   RA 9 .    ? -18.715 59.674  108.021 1.00 33.55 ? 2577 HOH   A O     1 
HETATM 18333 O  O     . HOH   RA 9 .    ? -30.885 61.257  90.326  1.00 23.70 ? 2578 HOH   A O     1 
HETATM 18334 O  O     . HOH   RA 9 .    ? -37.877 36.732  82.515  1.00 36.42 ? 2579 HOH   A O     1 
HETATM 18335 O  O     . HOH   RA 9 .    ? -26.377 73.346  101.203 1.00 35.44 ? 2580 HOH   A O     1 
HETATM 18336 O  O     . HOH   RA 9 .    ? -18.997 97.807  127.017 1.00 37.13 ? 2581 HOH   A O     1 
HETATM 18337 O  O     . HOH   RA 9 .    ? -34.572 80.657  120.385 1.00 24.69 ? 2582 HOH   A O     1 
HETATM 18338 O  O     . HOH   RA 9 .    ? -41.179 29.681  89.199  1.00 36.56 ? 2583 HOH   A O     1 
HETATM 18339 O  O     . HOH   RA 9 .    ? -40.719 80.204  87.590  1.00 20.07 ? 2584 HOH   A O     1 
HETATM 18340 O  O     . HOH   RA 9 .    ? -12.590 66.081  112.497 1.00 18.02 ? 2585 HOH   A O     1 
HETATM 18341 O  O     . HOH   RA 9 .    ? -9.487  64.112  95.887  1.00 20.82 ? 2586 HOH   A O     1 
HETATM 18342 O  O     . HOH   RA 9 .    ? -12.035 79.451  94.186  1.00 22.08 ? 2587 HOH   A O     1 
HETATM 18343 O  O     . HOH   RA 9 .    ? 14.129  86.489  120.512 1.00 35.83 ? 2588 HOH   A O     1 
HETATM 18344 O  O     . HOH   RA 9 .    ? -31.370 60.156  105.387 1.00 23.96 ? 2589 HOH   A O     1 
HETATM 18345 O  O     . HOH   RA 9 .    ? -31.885 52.959  85.701  1.00 31.86 ? 2590 HOH   A O     1 
HETATM 18346 O  O     . HOH   RA 9 .    ? -65.016 54.354  90.753  1.00 31.68 ? 2591 HOH   A O     1 
HETATM 18347 O  O     . HOH   RA 9 .    ? -24.911 79.487  94.830  1.00 18.92 ? 2592 HOH   A O     1 
HETATM 18348 O  O     . HOH   RA 9 .    ? -19.502 91.224  76.702  1.00 26.88 ? 2593 HOH   A O     1 
HETATM 18349 O  O     . HOH   RA 9 .    ? -39.521 88.879  119.164 1.00 31.87 ? 2594 HOH   A O     1 
HETATM 18350 O  O     . HOH   RA 9 .    ? 2.790   64.976  112.783 1.00 27.74 ? 2595 HOH   A O     1 
HETATM 18351 O  O     . HOH   RA 9 .    ? -39.244 76.672  93.149  1.00 24.16 ? 2596 HOH   A O     1 
HETATM 18352 O  O     . HOH   RA 9 .    ? -24.990 60.883  127.733 1.00 36.55 ? 2597 HOH   A O     1 
HETATM 18353 O  O     . HOH   RA 9 .    ? -19.911 79.209  114.735 1.00 19.62 ? 2598 HOH   A O     1 
HETATM 18354 O  O     . HOH   RA 9 .    ? -30.410 86.665  101.982 1.00 21.17 ? 2599 HOH   A O     1 
HETATM 18355 O  O     . HOH   RA 9 .    ? -3.517  57.888  72.504  1.00 29.21 ? 2600 HOH   A O     1 
HETATM 18356 O  O     . HOH   RA 9 .    ? -1.760  77.942  105.002 1.00 26.00 ? 2601 HOH   A O     1 
HETATM 18357 O  O     . HOH   RA 9 .    ? -36.695 45.731  78.022  1.00 29.09 ? 2602 HOH   A O     1 
HETATM 18358 O  O     . HOH   RA 9 .    ? -37.675 69.325  123.107 1.00 34.60 ? 2603 HOH   A O     1 
HETATM 18359 O  O     . HOH   RA 9 .    ? -21.740 42.815  60.699  1.00 43.12 ? 2604 HOH   A O     1 
HETATM 18360 O  O     . HOH   RA 9 .    ? -10.581 65.104  125.050 1.00 39.15 ? 2605 HOH   A O     1 
HETATM 18361 O  O     . HOH   RA 9 .    ? 9.976   68.048  93.678  1.00 33.12 ? 2606 HOH   A O     1 
HETATM 18362 O  O     . HOH   RA 9 .    ? -15.961 52.016  115.161 1.00 39.99 ? 2607 HOH   A O     1 
HETATM 18363 O  O     . HOH   RA 9 .    ? -21.896 89.678  109.174 1.00 37.77 ? 2608 HOH   A O     1 
HETATM 18364 O  O     . HOH   RA 9 .    ? -28.711 83.869  104.110 1.00 24.94 ? 2609 HOH   A O     1 
HETATM 18365 O  O     . HOH   RA 9 .    ? -43.745 59.544  87.519  1.00 18.05 ? 2610 HOH   A O     1 
HETATM 18366 O  O     . HOH   RA 9 .    ? -32.076 64.773  122.040 1.00 30.50 ? 2611 HOH   A O     1 
HETATM 18367 O  O     . HOH   RA 9 .    ? -56.833 53.535  96.224  1.00 21.89 ? 2612 HOH   A O     1 
HETATM 18368 O  O     . HOH   RA 9 .    ? -6.700  80.763  127.425 1.00 31.27 ? 2613 HOH   A O     1 
HETATM 18369 O  O     . HOH   RA 9 .    ? -36.555 69.500  119.172 1.00 33.12 ? 2614 HOH   A O     1 
HETATM 18370 O  O     . HOH   RA 9 .    ? -53.574 68.724  93.529  1.00 25.87 ? 2615 HOH   A O     1 
HETATM 18371 O  O     . HOH   RA 9 .    ? -67.536 64.045  85.307  1.00 38.73 ? 2616 HOH   A O     1 
HETATM 18372 O  O     . HOH   RA 9 .    ? -4.902  55.934  100.912 1.00 27.39 ? 2617 HOH   A O     1 
HETATM 18373 O  O     . HOH   RA 9 .    ? 17.152  80.761  96.415  1.00 35.84 ? 2618 HOH   A O     1 
HETATM 18374 O  O     . HOH   RA 9 .    ? -19.996 89.048  74.769  1.00 32.54 ? 2619 HOH   A O     1 
HETATM 18375 O  O     . HOH   RA 9 .    ? -22.719 83.633  91.307  1.00 19.45 ? 2620 HOH   A O     1 
HETATM 18376 O  O     . HOH   RA 9 .    ? -42.786 50.151  55.522  1.00 33.32 ? 2621 HOH   A O     1 
HETATM 18377 O  O     . HOH   RA 9 .    ? -52.346 78.532  87.660  1.00 32.83 ? 2622 HOH   A O     1 
HETATM 18378 O  O     . HOH   RA 9 .    ? 0.096   52.935  62.841  1.00 26.26 ? 2623 HOH   A O     1 
HETATM 18379 O  O     . HOH   RA 9 .    ? -49.520 38.065  100.178 1.00 39.38 ? 2624 HOH   A O     1 
HETATM 18380 O  O     . HOH   RA 9 .    ? -65.836 64.207  88.359  1.00 27.94 ? 2625 HOH   A O     1 
HETATM 18381 O  O     . HOH   RA 9 .    ? -68.665 69.797  79.963  1.00 28.72 ? 2626 HOH   A O     1 
HETATM 18382 O  O     . HOH   RA 9 .    ? -59.607 50.112  90.534  1.00 34.23 ? 2627 HOH   A O     1 
HETATM 18383 O  O     . HOH   RA 9 .    ? -59.431 62.904  77.692  1.00 21.30 ? 2628 HOH   A O     1 
HETATM 18384 O  O     . HOH   RA 9 .    ? -35.995 71.756  121.213 1.00 38.71 ? 2629 HOH   A O     1 
HETATM 18385 O  O     . HOH   RA 9 .    ? 1.302   66.499  96.278  1.00 22.60 ? 2630 HOH   A O     1 
HETATM 18386 O  O     . HOH   RA 9 .    ? -63.055 54.095  72.188  1.00 32.79 ? 2631 HOH   A O     1 
HETATM 18387 O  O     . HOH   RA 9 .    ? -66.145 61.426  75.759  1.00 22.55 ? 2632 HOH   A O     1 
HETATM 18388 O  O     . HOH   RA 9 .    ? -37.110 88.286  82.960  1.00 35.40 ? 2633 HOH   A O     1 
HETATM 18389 O  O     . HOH   RA 9 .    ? -27.201 62.280  88.805  1.00 21.53 ? 2634 HOH   A O     1 
HETATM 18390 O  O     . HOH   RA 9 .    ? -53.943 37.523  89.358  1.00 34.12 ? 2635 HOH   A O     1 
HETATM 18391 O  O     . HOH   RA 9 .    ? -44.641 61.138  85.446  1.00 16.30 ? 2636 HOH   A O     1 
HETATM 18392 O  O     . HOH   RA 9 .    ? -0.213  68.070  117.503 1.00 29.36 ? 2637 HOH   A O     1 
HETATM 18393 O  O     . HOH   RA 9 .    ? 1.975   86.146  124.934 1.00 43.51 ? 2638 HOH   A O     1 
HETATM 18394 O  O     . HOH   RA 9 .    ? -37.275 75.592  97.751  1.00 24.18 ? 2639 HOH   A O     1 
HETATM 18395 O  O     . HOH   RA 9 .    ? -7.316  51.016  52.776  1.00 33.62 ? 2640 HOH   A O     1 
HETATM 18396 O  O     . HOH   RA 9 .    ? -19.789 77.000  66.931  1.00 39.38 ? 2641 HOH   A O     1 
HETATM 18397 O  O     . HOH   RA 9 .    ? -52.937 66.766  104.455 1.00 41.78 ? 2642 HOH   A O     1 
HETATM 18398 O  O     . HOH   RA 9 .    ? 22.908  76.129  114.735 1.00 29.23 ? 2643 HOH   A O     1 
HETATM 18399 O  O     . HOH   RA 9 .    ? -26.725 63.332  86.332  1.00 26.77 ? 2644 HOH   A O     1 
HETATM 18400 O  O     . HOH   RA 9 .    ? -49.447 49.067  99.675  1.00 24.44 ? 2645 HOH   A O     1 
HETATM 18401 O  O     . HOH   RA 9 .    ? 18.815  73.256  117.993 1.00 29.88 ? 2646 HOH   A O     1 
HETATM 18402 O  O     . HOH   RA 9 .    ? -43.972 31.747  84.054  1.00 29.74 ? 2647 HOH   A O     1 
HETATM 18403 O  O     . HOH   RA 9 .    ? 2.726   84.120  101.431 1.00 25.00 ? 2648 HOH   A O     1 
HETATM 18404 O  O     . HOH   RA 9 .    ? -46.118 32.064  70.321  1.00 42.18 ? 2649 HOH   A O     1 
HETATM 18405 O  O     . HOH   RA 9 .    ? -42.317 37.835  105.198 1.00 39.49 ? 2650 HOH   A O     1 
HETATM 18406 O  O     . HOH   RA 9 .    ? -27.313 90.825  115.697 1.00 23.54 ? 2651 HOH   A O     1 
HETATM 18407 O  O     . HOH   RA 9 .    ? 21.708  73.042  115.646 1.00 31.02 ? 2652 HOH   A O     1 
HETATM 18408 O  O     . HOH   RA 9 .    ? -22.878 53.956  91.989  1.00 34.00 ? 2653 HOH   A O     1 
HETATM 18409 O  O     . HOH   RA 9 .    ? -6.833  38.565  63.265  1.00 32.51 ? 2654 HOH   A O     1 
HETATM 18410 O  O     . HOH   RA 9 .    ? -36.801 68.634  83.189  1.00 31.96 ? 2655 HOH   A O     1 
HETATM 18411 O  O     . HOH   RA 9 .    ? -32.987 84.355  127.894 1.00 33.38 ? 2656 HOH   A O     1 
HETATM 18412 O  O     . HOH   RA 9 .    ? -13.904 42.231  70.854  1.00 36.51 ? 2657 HOH   A O     1 
HETATM 18413 O  O     . HOH   RA 9 .    ? -10.181 63.976  115.362 1.00 20.49 ? 2658 HOH   A O     1 
HETATM 18414 O  O     . HOH   RA 9 .    ? -2.019  78.738  75.521  1.00 36.09 ? 2659 HOH   A O     1 
HETATM 18415 O  O     . HOH   RA 9 .    ? -11.034 92.484  124.232 1.00 32.49 ? 2660 HOH   A O     1 
HETATM 18416 O  O     . HOH   RA 9 .    ? -33.625 83.855  123.370 1.00 27.70 ? 2661 HOH   A O     1 
HETATM 18417 O  O     . HOH   RA 9 .    ? -30.036 71.585  88.917  1.00 41.33 ? 2662 HOH   A O     1 
HETATM 18418 O  O     . HOH   RA 9 .    ? -28.824 95.089  89.003  1.00 29.91 ? 2663 HOH   A O     1 
HETATM 18419 O  O     . HOH   RA 9 .    ? -31.994 75.431  126.391 1.00 30.37 ? 2664 HOH   A O     1 
HETATM 18420 O  O     . HOH   RA 9 .    ? 2.922   78.037  97.921  1.00 27.38 ? 2665 HOH   A O     1 
HETATM 18421 O  O     . HOH   RA 9 .    ? -46.803 33.363  85.400  1.00 39.50 ? 2666 HOH   A O     1 
HETATM 18422 O  O     . HOH   RA 9 .    ? -41.476 88.809  93.637  1.00 33.26 ? 2667 HOH   A O     1 
HETATM 18423 O  O     . HOH   RA 9 .    ? -36.735 60.625  96.112  1.00 21.01 ? 2668 HOH   A O     1 
HETATM 18424 O  O     . HOH   RA 9 .    ? -42.236 28.862  86.420  1.00 41.10 ? 2669 HOH   A O     1 
HETATM 18425 O  O     . HOH   RA 9 .    ? 13.045  88.821  115.896 1.00 37.21 ? 2670 HOH   A O     1 
HETATM 18426 O  O     . HOH   RA 9 .    ? -48.755 47.752  97.336  1.00 20.19 ? 2671 HOH   A O     1 
HETATM 18427 O  O     . HOH   RA 9 .    ? -60.545 41.435  80.699  1.00 41.52 ? 2672 HOH   A O     1 
HETATM 18428 O  O     . HOH   RA 9 .    ? -11.612 60.066  84.553  1.00 35.03 ? 2673 HOH   A O     1 
HETATM 18429 O  O     . HOH   RA 9 .    ? -2.356  60.637  119.760 1.00 32.30 ? 2674 HOH   A O     1 
HETATM 18430 O  O     . HOH   RA 9 .    ? -7.706  72.664  99.934  1.00 33.90 ? 2675 HOH   A O     1 
HETATM 18431 O  O     . HOH   RA 9 .    ? -65.843 72.362  72.186  1.00 41.95 ? 2676 HOH   A O     1 
HETATM 18432 O  O     . HOH   RA 9 .    ? -31.328 91.344  80.220  1.00 30.66 ? 2677 HOH   A O     1 
HETATM 18433 O  O     . HOH   RA 9 .    ? -59.005 58.386  76.893  1.00 18.95 ? 2678 HOH   A O     1 
HETATM 18434 O  O     . HOH   RA 9 .    ? -2.467  56.002  99.606  1.00 33.44 ? 2679 HOH   A O     1 
HETATM 18435 O  O     . HOH   RA 9 .    ? 2.789   74.496  109.184 1.00 26.83 ? 2680 HOH   A O     1 
HETATM 18436 O  O     . HOH   RA 9 .    ? -67.159 69.542  72.946  1.00 36.91 ? 2681 HOH   A O     1 
HETATM 18437 O  O     . HOH   RA 9 .    ? -37.320 86.173  101.896 1.00 26.01 ? 2682 HOH   A O     1 
HETATM 18438 O  O     . HOH   RA 9 .    ? -14.691 53.370  75.584  1.00 35.24 ? 2683 HOH   A O     1 
HETATM 18439 O  O     . HOH   RA 9 .    ? -43.538 85.605  94.828  1.00 36.23 ? 2684 HOH   A O     1 
HETATM 18440 O  O     . HOH   RA 9 .    ? -36.296 38.037  102.036 1.00 37.01 ? 2685 HOH   A O     1 
HETATM 18441 O  O     . HOH   RA 9 .    ? -53.573 72.456  68.350  1.00 27.18 ? 2686 HOH   A O     1 
HETATM 18442 O  O     . HOH   RA 9 .    ? -12.638 90.230  101.548 1.00 35.13 ? 2687 HOH   A O     1 
HETATM 18443 O  O     . HOH   RA 9 .    ? -32.387 92.084  110.265 1.00 34.10 ? 2688 HOH   A O     1 
HETATM 18444 O  O     . HOH   RA 9 .    ? -46.735 77.257  91.991  1.00 25.88 ? 2689 HOH   A O     1 
HETATM 18445 O  O     . HOH   RA 9 .    ? -23.313 95.040  118.297 1.00 35.10 ? 2690 HOH   A O     1 
HETATM 18446 O  O     . HOH   RA 9 .    ? -46.571 81.440  92.899  1.00 37.13 ? 2691 HOH   A O     1 
HETATM 18447 O  O     . HOH   RA 9 .    ? -53.327 49.485  60.286  1.00 37.20 ? 2692 HOH   A O     1 
HETATM 18448 O  O     . HOH   RA 9 .    ? -58.596 42.649  89.520  1.00 37.22 ? 2693 HOH   A O     1 
HETATM 18449 O  O     . HOH   RA 9 .    ? -1.873  90.508  105.131 1.00 34.75 ? 2694 HOH   A O     1 
HETATM 18450 O  O     . HOH   RA 9 .    ? -6.070  71.197  105.790 1.00 34.88 ? 2695 HOH   A O     1 
HETATM 18451 O  O     . HOH   RA 9 .    ? -34.404 77.604  84.924  1.00 22.30 ? 2696 HOH   A O     1 
HETATM 18452 O  O     . HOH   RA 9 .    ? -30.889 84.138  123.259 1.00 23.82 ? 2697 HOH   A O     1 
HETATM 18453 O  O     . HOH   RA 9 .    ? -11.358 43.762  73.830  1.00 31.84 ? 2698 HOH   A O     1 
HETATM 18454 O  O     . HOH   RA 9 .    ? -18.368 69.044  104.221 1.00 25.64 ? 2699 HOH   A O     1 
HETATM 18455 O  O     . HOH   RA 9 .    ? -25.549 88.820  116.037 1.00 23.89 ? 2700 HOH   A O     1 
HETATM 18456 O  O     . HOH   RA 9 .    ? -9.368  56.503  82.441  1.00 35.99 ? 2701 HOH   A O     1 
HETATM 18457 O  O     . HOH   RA 9 .    ? 0.537   64.361  106.969 1.00 22.67 ? 2702 HOH   A O     1 
HETATM 18458 O  O     . HOH   RA 9 .    ? -37.139 63.637  93.103  1.00 34.45 ? 2703 HOH   A O     1 
HETATM 18459 O  O     . HOH   RA 9 .    ? -28.304 69.749  85.782  1.00 30.51 ? 2704 HOH   A O     1 
HETATM 18460 O  O     . HOH   RA 9 .    ? -35.238 43.938  79.324  1.00 31.98 ? 2705 HOH   A O     1 
HETATM 18461 O  O     . HOH   RA 9 .    ? -32.057 56.420  85.826  1.00 25.66 ? 2706 HOH   A O     1 
HETATM 18462 O  O     . HOH   RA 9 .    ? -1.473  80.281  111.871 1.00 33.80 ? 2707 HOH   A O     1 
HETATM 18463 O  O     . HOH   RA 9 .    ? -45.593 63.287  105.031 1.00 38.67 ? 2708 HOH   A O     1 
HETATM 18464 O  O     . HOH   RA 9 .    ? -35.680 37.678  83.314  1.00 36.10 ? 2709 HOH   A O     1 
HETATM 18465 O  O     . HOH   RA 9 .    ? -39.585 38.055  84.969  1.00 33.01 ? 2710 HOH   A O     1 
HETATM 18466 O  O     . HOH   RA 9 .    ? -16.714 54.011  75.867  1.00 35.88 ? 2711 HOH   A O     1 
HETATM 18467 O  O     . HOH   RA 9 .    ? -1.894  63.018  113.327 1.00 35.85 ? 2712 HOH   A O     1 
HETATM 18468 O  O     . HOH   RA 9 .    ? -34.080 98.258  93.248  1.00 42.78 ? 2713 HOH   A O     1 
HETATM 18469 O  O     . HOH   RA 9 .    ? -54.266 79.214  81.612  1.00 38.50 ? 2714 HOH   A O     1 
HETATM 18470 O  O     . HOH   RA 9 .    ? 4.780   85.971  100.641 1.00 31.27 ? 2715 HOH   A O     1 
HETATM 18471 O  O     . HOH   RA 9 .    ? -44.082 76.461  74.556  1.00 33.11 ? 2716 HOH   A O     1 
HETATM 18472 O  O     . HOH   RA 9 .    ? -21.854 92.768  110.703 1.00 42.71 ? 2717 HOH   A O     1 
HETATM 18473 O  O     . HOH   RA 9 .    ? -13.508 54.500  77.038  1.00 28.48 ? 2718 HOH   A O     1 
HETATM 18474 O  O     . HOH   RA 9 .    ? -10.541 76.940  106.115 1.00 26.41 ? 2719 HOH   A O     1 
HETATM 18475 O  O     . HOH   RA 9 .    ? -36.643 45.683  104.061 1.00 24.55 ? 2720 HOH   A O     1 
HETATM 18476 O  O     . HOH   RA 9 .    ? -36.144 35.617  85.168  1.00 45.96 ? 2721 HOH   A O     1 
HETATM 18477 O  O     . HOH   RA 9 .    ? -0.119  67.196  86.068  1.00 39.86 ? 2722 HOH   A O     1 
HETATM 18478 O  O     . HOH   RA 9 .    ? 9.130   65.001  94.009  1.00 33.88 ? 2723 HOH   A O     1 
HETATM 18479 O  O     . HOH   RA 9 .    ? -26.257 39.460  77.069  1.00 42.37 ? 2724 HOH   A O     1 
HETATM 18480 O  O     . HOH   RA 9 .    ? 23.217  72.909  97.964  1.00 37.42 ? 2725 HOH   A O     1 
HETATM 18481 O  O     . HOH   RA 9 .    ? -12.572 53.793  110.387 1.00 33.80 ? 2726 HOH   A O     1 
HETATM 18482 O  O     . HOH   RA 9 .    ? -25.150 59.559  114.307 1.00 24.08 ? 2727 HOH   A O     1 
HETATM 18483 O  O     . HOH   RA 9 .    ? -14.856 59.336  126.453 1.00 26.35 ? 2728 HOH   A O     1 
HETATM 18484 O  O     . HOH   RA 9 .    ? 2.425   75.942  116.594 1.00 27.16 ? 2729 HOH   A O     1 
HETATM 18485 O  O     . HOH   RA 9 .    ? 16.035  62.028  116.152 1.00 35.65 ? 2730 HOH   A O     1 
HETATM 18486 O  O     . HOH   RA 9 .    ? -36.105 80.775  75.694  1.00 23.83 ? 2731 HOH   A O     1 
HETATM 18487 O  O     . HOH   RA 9 .    ? -48.532 61.827  56.747  1.00 29.40 ? 2732 HOH   A O     1 
HETATM 18488 O  O     . HOH   RA 9 .    ? -48.974 35.549  87.918  1.00 32.14 ? 2733 HOH   A O     1 
HETATM 18489 O  O     . HOH   RA 9 .    ? -66.093 68.837  84.087  1.00 32.33 ? 2734 HOH   A O     1 
HETATM 18490 O  O     . HOH   RA 9 .    ? -16.474 75.876  105.652 1.00 28.33 ? 2735 HOH   A O     1 
HETATM 18491 O  O     . HOH   RA 9 .    ? -22.340 77.160  69.978  1.00 28.35 ? 2736 HOH   A O     1 
HETATM 18492 O  O     . HOH   RA 9 .    ? 15.498  64.354  116.442 1.00 40.34 ? 2737 HOH   A O     1 
HETATM 18493 O  O     . HOH   RA 9 .    ? -20.729 58.393  96.976  1.00 23.56 ? 2738 HOH   A O     1 
HETATM 18494 O  O     . HOH   RA 9 .    ? -2.769  78.008  101.071 1.00 35.37 ? 2739 HOH   A O     1 
HETATM 18495 O  O     . HOH   RA 9 .    ? -13.923 86.913  100.647 1.00 37.51 ? 2740 HOH   A O     1 
HETATM 18496 O  O     . HOH   RA 9 .    ? -48.198 94.931  99.708  1.00 47.21 ? 2741 HOH   A O     1 
HETATM 18497 O  O     . HOH   RA 9 .    ? -25.741 70.057  95.401  1.00 29.93 ? 2742 HOH   A O     1 
HETATM 18498 O  O     . HOH   RA 9 .    ? -10.944 54.131  99.972  1.00 27.91 ? 2743 HOH   A O     1 
HETATM 18499 O  O     . HOH   RA 9 .    ? -40.704 70.599  92.818  1.00 27.63 ? 2744 HOH   A O     1 
HETATM 18500 O  O     . HOH   RA 9 .    ? -26.469 92.502  132.088 1.00 37.34 ? 2745 HOH   A O     1 
HETATM 18501 O  O     . HOH   RA 9 .    ? -21.214 101.314 89.450  1.00 35.99 ? 2746 HOH   A O     1 
HETATM 18502 O  O     . HOH   RA 9 .    ? -53.112 56.866  54.932  1.00 39.06 ? 2747 HOH   A O     1 
HETATM 18503 O  O     . HOH   RA 9 .    ? 1.295   57.545  107.389 1.00 20.12 ? 2748 HOH   A O     1 
HETATM 18504 O  O     . HOH   RA 9 .    ? -36.521 49.955  100.447 1.00 28.99 ? 2749 HOH   A O     1 
HETATM 18505 O  O     . HOH   RA 9 .    ? 1.219   70.356  87.288  1.00 42.29 ? 2750 HOH   A O     1 
HETATM 18506 O  O     . HOH   RA 9 .    ? -21.592 55.061  96.436  1.00 36.19 ? 2751 HOH   A O     1 
HETATM 18507 O  O     . HOH   RA 9 .    ? -25.393 68.327  90.561  1.00 27.92 ? 2752 HOH   A O     1 
HETATM 18508 O  O     . HOH   RA 9 .    ? -45.349 55.117  92.053  1.00 16.91 ? 2753 HOH   A O     1 
HETATM 18509 O  O     . HOH   RA 9 .    ? -49.374 54.442  73.945  1.00 21.52 ? 2754 HOH   A O     1 
HETATM 18510 O  O     . HOH   RA 9 .    ? -30.009 63.165  91.582  1.00 37.87 ? 2755 HOH   A O     1 
HETATM 18511 O  O     . HOH   RA 9 .    ? -54.620 26.712  91.978  1.00 41.31 ? 2756 HOH   A O     1 
HETATM 18512 O  O     . HOH   RA 9 .    ? -2.546  87.729  104.480 1.00 40.39 ? 2757 HOH   A O     1 
HETATM 18513 O  O     . HOH   RA 9 .    ? -56.378 40.195  91.437  1.00 43.02 ? 2758 HOH   A O     1 
HETATM 18514 O  O     . HOH   RA 9 .    ? -17.827 85.730  77.138  1.00 28.99 ? 2759 HOH   A O     1 
HETATM 18515 O  O     . HOH   RA 9 .    ? -44.189 91.527  110.989 1.00 33.54 ? 2760 HOH   A O     1 
HETATM 18516 O  O     . HOH   RA 9 .    ? -27.649 56.385  90.164  1.00 33.00 ? 2761 HOH   A O     1 
HETATM 18517 O  O     . HOH   RA 9 .    ? -2.787  76.415  76.905  1.00 29.03 ? 2762 HOH   A O     1 
HETATM 18518 O  O     . HOH   RA 9 .    ? 20.881  75.746  99.654  1.00 40.69 ? 2763 HOH   A O     1 
HETATM 18519 O  O     . HOH   RA 9 .    ? -1.019  70.350  116.112 1.00 27.56 ? 2764 HOH   A O     1 
HETATM 18520 O  O     . HOH   RA 9 .    ? -42.548 77.839  78.386  1.00 24.80 ? 2765 HOH   A O     1 
HETATM 18521 O  O     . HOH   RA 9 .    ? 7.051   55.410  98.485  1.00 22.48 ? 2766 HOH   A O     1 
HETATM 18522 O  O     . HOH   RA 9 .    ? -2.038  77.137  120.395 1.00 33.41 ? 2767 HOH   A O     1 
HETATM 18523 O  O     . HOH   RA 9 .    ? -39.462 86.346  89.100  1.00 27.26 ? 2768 HOH   A O     1 
HETATM 18524 O  O     . HOH   RA 9 .    ? -42.917 56.397  91.917  1.00 16.43 ? 2769 HOH   A O     1 
HETATM 18525 O  O     . HOH   RA 9 .    ? 19.913  64.685  92.968  1.00 37.90 ? 2770 HOH   A O     1 
HETATM 18526 O  O     . HOH   RA 9 .    ? -48.488 78.511  75.081  1.00 38.49 ? 2771 HOH   A O     1 
HETATM 18527 O  O     . HOH   RA 9 .    ? -38.949 66.678  94.419  1.00 30.52 ? 2772 HOH   A O     1 
HETATM 18528 O  O     . HOH   RA 9 .    ? 11.444  85.153  124.445 1.00 35.58 ? 2773 HOH   A O     1 
HETATM 18529 O  O     . HOH   RA 9 .    ? 1.435   62.553  110.954 1.00 30.33 ? 2774 HOH   A O     1 
HETATM 18530 O  O     . HOH   RA 9 .    ? -36.877 51.741  60.762  1.00 32.46 ? 2775 HOH   A O     1 
HETATM 18531 O  O     . HOH   RA 9 .    ? -0.448  73.090  119.815 1.00 40.77 ? 2776 HOH   A O     1 
HETATM 18532 O  O     . HOH   RA 9 .    ? -37.892 72.835  87.298  1.00 28.35 ? 2777 HOH   A O     1 
HETATM 18533 O  O     . HOH   RA 9 .    ? -51.712 77.359  101.593 1.00 38.42 ? 2778 HOH   A O     1 
HETATM 18534 O  O     . HOH   RA 9 .    ? -9.231  60.696  84.116  1.00 29.93 ? 2779 HOH   A O     1 
HETATM 18535 O  O     . HOH   RA 9 .    ? -5.645  75.135  102.921 1.00 33.03 ? 2780 HOH   A O     1 
HETATM 18536 O  O     . HOH   RA 9 .    ? -47.707 22.844  76.607  1.00 47.72 ? 2781 HOH   A O     1 
HETATM 18537 O  O     . HOH   RA 9 .    ? -23.065 76.358  133.196 1.00 30.09 ? 2782 HOH   A O     1 
HETATM 18538 O  O     . HOH   RA 9 .    ? -3.950  60.637  68.545  1.00 37.54 ? 2783 HOH   A O     1 
HETATM 18539 O  O     . HOH   RA 9 .    ? 26.503  74.025  97.734  1.00 45.57 ? 2784 HOH   A O     1 
HETATM 18540 O  O     . HOH   RA 9 .    ? 7.344   57.313  112.172 1.00 40.51 ? 2785 HOH   A O     1 
HETATM 18541 O  O     . HOH   RA 9 .    ? -64.618 55.063  80.806  1.00 29.26 ? 2786 HOH   A O     1 
HETATM 18542 O  O     . HOH   RA 9 .    ? -18.335 51.428  84.870  1.00 42.43 ? 2787 HOH   A O     1 
HETATM 18543 O  O     . HOH   RA 9 .    ? -61.824 59.808  96.071  1.00 27.10 ? 2788 HOH   A O     1 
HETATM 18544 O  O     . HOH   RA 9 .    ? -30.724 41.510  97.835  1.00 38.05 ? 2789 HOH   A O     1 
HETATM 18545 O  O     . HOH   RA 9 .    ? -8.292  82.332  104.689 1.00 31.53 ? 2790 HOH   A O     1 
HETATM 18546 O  O     . HOH   RA 9 .    ? -44.644 93.182  88.863  1.00 43.01 ? 2791 HOH   A O     1 
HETATM 18547 O  O     . HOH   RA 9 .    ? 25.924  64.526  102.335 1.00 33.95 ? 2792 HOH   A O     1 
HETATM 18548 O  O     . HOH   RA 9 .    ? -25.695 74.960  132.550 1.00 33.39 ? 2793 HOH   A O     1 
HETATM 18549 O  O     . HOH   RA 9 .    ? -16.217 43.439  71.661  1.00 37.81 ? 2794 HOH   A O     1 
HETATM 18550 O  O     . HOH   RA 9 .    ? 10.641  81.749  125.391 1.00 32.80 ? 2795 HOH   A O     1 
HETATM 18551 O  O     . HOH   RA 9 .    ? -40.521 65.243  62.089  1.00 30.64 ? 2796 HOH   A O     1 
HETATM 18552 O  O     . HOH   RA 9 .    ? 17.806  85.281  98.361  1.00 39.35 ? 2797 HOH   A O     1 
HETATM 18553 O  O     . HOH   RA 9 .    ? -8.782  52.080  107.315 1.00 33.25 ? 2798 HOH   A O     1 
HETATM 18554 O  O     . HOH   RA 9 .    ? -21.528 90.666  111.700 1.00 33.37 ? 2799 HOH   A O     1 
HETATM 18555 O  O     . HOH   RA 9 .    ? -56.030 68.979  100.083 1.00 35.38 ? 2800 HOH   A O     1 
HETATM 18556 O  O     . HOH   RA 9 .    ? -32.621 98.335  124.188 1.00 42.32 ? 2801 HOH   A O     1 
HETATM 18557 O  O     . HOH   RA 9 .    ? 15.048  82.335  119.212 1.00 34.09 ? 2802 HOH   A O     1 
HETATM 18558 O  O     . HOH   RA 9 .    ? -13.972 95.960  119.937 1.00 35.69 ? 2803 HOH   A O     1 
HETATM 18559 O  O     . HOH   RA 9 .    ? -19.309 95.094  111.596 1.00 45.93 ? 2804 HOH   A O     1 
HETATM 18560 O  O     . HOH   RA 9 .    ? -64.219 71.043  83.216  1.00 36.25 ? 2805 HOH   A O     1 
HETATM 18561 O  O     . HOH   RA 9 .    ? -45.793 78.334  89.960  1.00 23.60 ? 2806 HOH   A O     1 
HETATM 18562 O  O     . HOH   RA 9 .    ? -30.997 38.695  98.910  1.00 46.13 ? 2807 HOH   A O     1 
HETATM 18563 O  O     . HOH   RA 9 .    ? -65.451 69.155  69.198  1.00 36.99 ? 2808 HOH   A O     1 
HETATM 18564 O  O     . HOH   RA 9 .    ? -59.773 64.105  92.300  1.00 31.41 ? 2809 HOH   A O     1 
HETATM 18565 O  O     . HOH   RA 9 .    ? -39.120 47.373  103.874 1.00 27.99 ? 2810 HOH   A O     1 
HETATM 18566 O  O     . HOH   RA 9 .    ? 0.834   72.071  125.050 1.00 44.66 ? 2811 HOH   A O     1 
HETATM 18567 O  O     . HOH   RA 9 .    ? -49.845 72.892  62.853  1.00 23.23 ? 2812 HOH   A O     1 
HETATM 18568 O  O     . HOH   RA 9 .    ? -32.311 98.438  99.241  1.00 38.74 ? 2813 HOH   A O     1 
HETATM 18569 O  O     . HOH   RA 9 .    ? -8.387  72.944  102.933 1.00 37.33 ? 2814 HOH   A O     1 
HETATM 18570 O  O     . HOH   RA 9 .    ? -0.274  52.746  58.902  1.00 39.52 ? 2815 HOH   A O     1 
HETATM 18571 O  O     . HOH   RA 9 .    ? -37.430 40.435  74.128  1.00 35.28 ? 2816 HOH   A O     1 
HETATM 18572 O  O     . HOH   RA 9 .    ? -61.337 42.055  66.837  1.00 41.67 ? 2817 HOH   A O     1 
HETATM 18573 O  O     . HOH   RA 9 .    ? -9.139  84.222  80.582  1.00 41.98 ? 2818 HOH   A O     1 
HETATM 18574 O  O     . HOH   RA 9 .    ? -20.762 90.357  104.932 1.00 40.63 ? 2819 HOH   A O     1 
HETATM 18575 O  O     . HOH   RA 9 .    ? -36.068 98.518  96.763  1.00 43.06 ? 2820 HOH   A O     1 
HETATM 18576 O  O     . HOH   RA 9 .    ? -34.596 75.800  126.031 1.00 34.90 ? 2821 HOH   A O     1 
HETATM 18577 O  O     . HOH   RA 9 .    ? -1.627  54.749  101.354 1.00 29.56 ? 2822 HOH   A O     1 
HETATM 18578 O  O     . HOH   RA 9 .    ? -31.625 28.188  75.320  1.00 43.72 ? 2823 HOH   A O     1 
HETATM 18579 O  O     . HOH   RA 9 .    ? -56.349 32.437  88.229  1.00 39.76 ? 2824 HOH   A O     1 
HETATM 18580 O  O     . HOH   RA 9 .    ? -64.201 63.234  68.634  1.00 34.14 ? 2825 HOH   A O     1 
HETATM 18581 O  O     . HOH   RA 9 .    ? -1.034  80.128  87.855  1.00 40.79 ? 2826 HOH   A O     1 
HETATM 18582 O  O     . HOH   RA 9 .    ? -55.485 25.174  89.057  1.00 44.14 ? 2827 HOH   A O     1 
HETATM 18583 O  O     . HOH   RA 9 .    ? -29.660 42.825  72.394  1.00 46.78 ? 2828 HOH   A O     1 
HETATM 18584 O  O     . HOH   RA 9 .    ? -40.230 97.588  103.159 1.00 35.67 ? 2829 HOH   A O     1 
HETATM 18585 O  O     . HOH   RA 9 .    ? -20.724 50.595  108.167 1.00 40.42 ? 2830 HOH   A O     1 
HETATM 18586 O  O     . HOH   RA 9 .    ? -61.865 35.758  71.387  1.00 40.29 ? 2831 HOH   A O     1 
HETATM 18587 O  O     . HOH   RA 9 .    ? -31.821 45.031  103.354 1.00 39.74 ? 2832 HOH   A O     1 
HETATM 18588 O  O     . HOH   RA 9 .    ? 22.698  65.594  92.562  1.00 43.21 ? 2833 HOH   A O     1 
HETATM 18589 O  O     . HOH   RA 9 .    ? -1.827  83.380  115.168 1.00 35.41 ? 2834 HOH   A O     1 
HETATM 18590 O  O     . HOH   RA 9 .    ? -43.518 90.632  99.773  1.00 29.96 ? 2835 HOH   A O     1 
HETATM 18591 O  O     . HOH   RA 9 .    ? -3.273  56.342  95.499  1.00 43.49 ? 2836 HOH   A O     1 
HETATM 18592 O  O     . HOH   RA 9 .    ? -20.291 55.075  98.333  1.00 31.31 ? 2837 HOH   A O     1 
HETATM 18593 O  O     . HOH   RA 9 .    ? -56.841 73.394  96.281  1.00 37.39 ? 2838 HOH   A O     1 
HETATM 18594 O  O     . HOH   RA 9 .    ? -34.006 59.378  106.117 1.00 25.57 ? 2839 HOH   A O     1 
HETATM 18595 O  O     . HOH   RA 9 .    ? -10.651 63.351  68.652  1.00 35.19 ? 2840 HOH   A O     1 
HETATM 18596 O  O     . HOH   RA 9 .    ? -51.627 41.573  101.613 1.00 41.63 ? 2841 HOH   A O     1 
HETATM 18597 O  O     . HOH   RA 9 .    ? -26.188 68.148  94.025  1.00 37.18 ? 2842 HOH   A O     1 
HETATM 18598 O  O     . HOH   RA 9 .    ? 7.806   89.355  122.616 1.00 43.95 ? 2843 HOH   A O     1 
HETATM 18599 O  O     . HOH   RA 9 .    ? -15.821 53.609  100.357 1.00 42.32 ? 2844 HOH   A O     1 
HETATM 18600 O  O     . HOH   RA 9 .    ? -31.292 74.486  87.527  1.00 34.65 ? 2845 HOH   A O     1 
HETATM 18601 O  O     . HOH   RA 9 .    ? -20.941 87.189  107.250 1.00 34.50 ? 2846 HOH   A O     1 
HETATM 18602 O  O     . HOH   RA 9 .    ? -1.847  80.334  97.106  1.00 37.58 ? 2847 HOH   A O     1 
HETATM 18603 O  O     . HOH   RA 9 .    ? -64.637 57.781  70.772  1.00 36.84 ? 2848 HOH   A O     1 
HETATM 18604 O  O     . HOH   RA 9 .    ? -8.232  87.901  92.600  1.00 43.29 ? 2849 HOH   A O     1 
HETATM 18605 O  O     . HOH   RA 9 .    ? -0.075  87.018  124.364 1.00 40.98 ? 2850 HOH   A O     1 
HETATM 18606 O  O     . HOH   RA 9 .    ? -41.480 64.951  58.483  1.00 26.69 ? 2851 HOH   A O     1 
HETATM 18607 O  O     . HOH   RA 9 .    ? -60.484 59.774  62.176  1.00 35.73 ? 2852 HOH   A O     1 
HETATM 18608 O  O     . HOH   RA 9 .    ? 21.359  71.497  94.776  1.00 41.93 ? 2853 HOH   A O     1 
HETATM 18609 O  O     . HOH   RA 9 .    ? -27.219 92.305  76.696  1.00 37.83 ? 2854 HOH   A O     1 
HETATM 18610 O  O     . HOH   RA 9 .    ? -22.602 67.564  129.889 1.00 40.93 ? 2855 HOH   A O     1 
HETATM 18611 O  O     . HOH   RA 9 .    ? -9.106  92.527  125.240 1.00 40.33 ? 2856 HOH   A O     1 
HETATM 18612 O  O     . HOH   RA 9 .    ? -46.937 80.396  75.363  1.00 47.86 ? 2857 HOH   A O     1 
HETATM 18613 O  O     . HOH   RA 9 .    ? -28.304 67.616  93.049  1.00 42.66 ? 2858 HOH   A O     1 
HETATM 18614 O  O     . HOH   RA 9 .    ? -12.635 69.149  73.536  1.00 40.44 ? 2859 HOH   A O     1 
HETATM 18615 O  O     . HOH   RA 9 .    ? -1.367  76.134  125.341 1.00 41.91 ? 2860 HOH   A O     1 
HETATM 18616 O  O     . HOH   RA 9 .    ? 16.956  87.099  111.612 1.00 37.64 ? 2861 HOH   A O     1 
HETATM 18617 O  O     . HOH   RA 9 .    ? -28.034 82.761  101.738 1.00 26.52 ? 2862 HOH   A O     1 
HETATM 18618 O  O     . HOH   RA 9 .    ? -7.223  53.087  81.597  1.00 39.78 ? 2863 HOH   A O     1 
HETATM 18619 O  O     . HOH   RA 9 .    ? 19.544  71.267  91.558  1.00 44.49 ? 2864 HOH   A O     1 
HETATM 18620 O  O     . HOH   RA 9 .    ? -28.423 57.832  88.635  1.00 32.05 ? 2865 HOH   A O     1 
HETATM 18621 O  O     . HOH   RA 9 .    ? -10.525 60.655  127.553 1.00 41.27 ? 2866 HOH   A O     1 
HETATM 18622 O  O     . HOH   RA 9 .    ? -51.881 55.200  70.554  1.00 25.62 ? 2867 HOH   A O     1 
HETATM 18623 O  O     . HOH   RA 9 .    ? -22.681 74.493  69.632  1.00 33.32 ? 2868 HOH   A O     1 
HETATM 18624 O  O     . HOH   RA 9 .    ? -39.962 67.954  89.127  1.00 33.41 ? 2869 HOH   A O     1 
HETATM 18625 O  O     . HOH   RA 9 .    ? -21.713 74.389  134.209 1.00 39.60 ? 2870 HOH   A O     1 
HETATM 18626 O  O     . HOH   RA 9 .    ? -31.564 62.063  122.046 1.00 37.59 ? 2871 HOH   A O     1 
HETATM 18627 O  O     . HOH   RA 9 .    ? -26.695 66.729  98.089  1.00 26.10 ? 2872 HOH   A O     1 
HETATM 18628 O  O     . HOH   RA 9 .    ? -25.359 100.634 91.099  1.00 35.69 ? 2873 HOH   A O     1 
HETATM 18629 O  O     . HOH   RA 9 .    ? 12.544  88.476  118.543 1.00 40.78 ? 2874 HOH   A O     1 
HETATM 18630 O  O     . HOH   RA 9 .    ? -30.351 92.236  78.021  1.00 42.62 ? 2875 HOH   A O     1 
HETATM 18631 O  O     . HOH   RA 9 .    ? -38.708 35.865  88.693  1.00 35.30 ? 2876 HOH   A O     1 
HETATM 18632 O  O     . HOH   RA 9 .    ? -29.545 72.491  98.284  1.00 41.59 ? 2877 HOH   A O     1 
HETATM 18633 O  O     . HOH   RA 9 .    ? -9.939  66.640  73.864  1.00 38.46 ? 2878 HOH   A O     1 
HETATM 18634 O  O     . HOH   RA 9 .    ? -44.777 28.834  86.850  1.00 38.33 ? 2879 HOH   A O     1 
HETATM 18635 O  O     . HOH   RA 9 .    ? -60.847 72.614  82.276  1.00 40.88 ? 2880 HOH   A O     1 
HETATM 18636 O  O     . HOH   RA 9 .    ? 18.851  73.625  92.632  1.00 40.79 ? 2881 HOH   A O     1 
HETATM 18637 O  O     . HOH   RA 9 .    ? 11.435  64.618  114.994 1.00 40.56 ? 2882 HOH   A O     1 
HETATM 18638 O  O     . HOH   RA 9 .    ? -29.293 69.929  92.575  1.00 40.88 ? 2883 HOH   A O     1 
HETATM 18639 O  O     . HOH   RA 9 .    ? -62.636 60.909  93.571  1.00 34.59 ? 2884 HOH   A O     1 
HETATM 18640 O  O     . HOH   RA 9 .    ? -17.713 54.186  98.739  1.00 39.30 ? 2885 HOH   A O     1 
HETATM 18641 O  O     . HOH   RA 9 .    ? -21.047 91.576  107.091 1.00 44.65 ? 2886 HOH   A O     1 
HETATM 18642 O  O     . HOH   RA 9 .    ? -54.918 57.409  102.434 1.00 35.89 ? 2887 HOH   A O     1 
HETATM 18643 O  O     . HOH   RA 9 .    ? 4.259   87.809  94.975  1.00 48.41 ? 2888 HOH   A O     1 
HETATM 18644 O  O     . HOH   RA 9 .    ? -18.842 71.530  132.505 1.00 33.61 ? 2889 HOH   A O     1 
HETATM 18645 O  O     . HOH   RA 9 .    ? -33.252 84.485  76.862  1.00 27.50 ? 2890 HOH   A O     1 
HETATM 18646 O  O     . HOH   RA 9 .    ? -22.742 71.311  73.671  1.00 37.27 ? 2891 HOH   A O     1 
HETATM 18647 O  O     . HOH   RA 9 .    ? -30.390 82.326  100.397 1.00 27.76 ? 2892 HOH   A O     1 
HETATM 18648 O  O     . HOH   RA 9 .    ? -10.386 78.945  92.139  1.00 25.40 ? 2893 HOH   A O     1 
HETATM 18649 O  O     . HOH   RA 9 .    ? -12.290 69.631  136.960 1.00 45.49 ? 2894 HOH   A O     1 
HETATM 18650 O  O     . HOH   RA 9 .    ? -42.420 86.536  89.612  1.00 43.00 ? 2895 HOH   A O     1 
HETATM 18651 O  O     . HOH   RA 9 .    ? -52.333 74.087  62.089  1.00 24.47 ? 2896 HOH   A O     1 
HETATM 18652 O  O     . HOH   RA 9 .    ? -37.090 63.513  114.128 1.00 34.84 ? 2897 HOH   A O     1 
HETATM 18653 O  O     . HOH   RA 9 .    ? -27.561 64.278  90.473  1.00 35.26 ? 2898 HOH   A O     1 
HETATM 18654 O  O     . HOH   RA 9 .    ? -34.241 37.208  100.318 1.00 45.97 ? 2899 HOH   A O     1 
HETATM 18655 O  O     . HOH   RA 9 .    ? -10.615 63.952  127.634 1.00 39.03 ? 2900 HOH   A O     1 
HETATM 18656 O  O     . HOH   RA 9 .    ? -44.448 82.371  88.742  1.00 39.44 ? 2901 HOH   A O     1 
HETATM 18657 O  O     . HOH   RA 9 .    ? -9.479  67.355  132.043 1.00 38.39 ? 2902 HOH   A O     1 
HETATM 18658 O  O     . HOH   RA 9 .    ? -27.051 51.384  109.501 1.00 36.83 ? 2903 HOH   A O     1 
HETATM 18659 O  O     . HOH   RA 9 .    ? 8.463   55.010  111.281 1.00 47.12 ? 2904 HOH   A O     1 
HETATM 18660 O  O     . HOH   RA 9 .    ? -27.696 71.420  98.988  1.00 39.86 ? 2905 HOH   A O     1 
HETATM 18661 O  O     . HOH   RA 9 .    ? -53.026 50.307  101.734 1.00 41.57 ? 2906 HOH   A O     1 
HETATM 18662 O  O     . HOH   RA 9 .    ? -67.562 62.705  68.559  1.00 40.94 ? 2907 HOH   A O     1 
HETATM 18663 O  O     . HOH   RA 9 .    ? 23.597  62.534  99.608  1.00 44.41 ? 2908 HOH   A O     1 
HETATM 18664 O  O     . HOH   RA 9 .    ? -2.987  69.630  94.623  1.00 44.40 ? 2909 HOH   A O     1 
HETATM 18665 O  O     . HOH   RA 9 .    ? -10.437 41.196  57.174  1.00 44.51 ? 2910 HOH   A O     1 
HETATM 18666 O  O     . HOH   RA 9 .    ? -24.501 66.079  96.880  1.00 29.32 ? 2911 HOH   A O     1 
HETATM 18667 O  O     . HOH   RA 9 .    ? -33.607 81.010  74.422  1.00 25.38 ? 2912 HOH   A O     1 
HETATM 18668 O  O     . HOH   RA 9 .    ? -34.351 76.180  87.262  1.00 31.06 ? 2913 HOH   A O     1 
HETATM 18669 O  O     . HOH   RA 9 .    ? -68.391 35.482  74.561  1.00 49.50 ? 2914 HOH   A O     1 
HETATM 18670 O  O     . HOH   RA 9 .    ? 16.992  87.014  114.114 1.00 46.45 ? 2915 HOH   A O     1 
HETATM 18671 O  O     . HOH   RA 9 .    ? -17.580 97.691  91.729  1.00 37.53 ? 2916 HOH   A O     1 
HETATM 18672 O  O     . HOH   RA 9 .    ? -65.707 54.335  78.318  1.00 31.75 ? 2917 HOH   A O     1 
HETATM 18673 O  O     . HOH   RA 9 .    ? 22.994  70.370  115.739 1.00 33.53 ? 2918 HOH   A O     1 
HETATM 18674 O  O     . HOH   RA 9 .    ? -36.328 63.166  118.310 1.00 38.92 ? 2919 HOH   A O     1 
HETATM 18675 O  O     . HOH   RA 9 .    ? -66.853 65.930  83.352  1.00 31.03 ? 2920 HOH   A O     1 
HETATM 18676 O  O     . HOH   RA 9 .    ? -25.757 63.345  101.797 1.00 29.85 ? 2921 HOH   A O     1 
HETATM 18677 O  O     . HOH   RA 9 .    ? -33.674 81.096  122.502 1.00 33.19 ? 2922 HOH   A O     1 
HETATM 18678 O  O     . HOH   RA 9 .    ? -8.761  74.542  128.687 1.00 34.49 ? 2923 HOH   A O     1 
HETATM 18679 O  O     . HOH   RA 9 .    ? -25.240 65.428  91.498  1.00 33.08 ? 2924 HOH   A O     1 
HETATM 18680 O  O     . HOH   RA 9 .    ? -14.778 58.018  123.613 1.00 36.67 ? 2925 HOH   A O     1 
HETATM 18681 O  O     . HOH   RA 9 .    ? 11.192  79.474  128.155 1.00 42.44 ? 2926 HOH   A O     1 
HETATM 18682 O  O     . HOH   RA 9 .    ? 18.216  73.678  122.390 1.00 39.65 ? 2927 HOH   A O     1 
HETATM 18683 O  O     . HOH   RA 9 .    ? -58.772 30.198  86.621  1.00 46.19 ? 2928 HOH   A O     1 
HETATM 18684 O  O     . HOH   RA 9 .    ? -47.482 64.045  56.169  1.00 38.75 ? 2929 HOH   A O     1 
HETATM 18685 O  O     . HOH   RA 9 .    ? -52.689 45.613  94.579  1.00 38.62 ? 2930 HOH   A O     1 
HETATM 18686 O  O     . HOH   RA 9 .    ? -26.940 59.571  116.286 1.00 29.02 ? 2931 HOH   A O     1 
HETATM 18687 O  O     . HOH   RA 9 .    ? 3.061   90.022  95.730  1.00 54.69 ? 2932 HOH   A O     1 
HETATM 18688 O  O     . HOH   RA 9 .    ? -52.734 81.985  73.516  1.00 44.83 ? 2933 HOH   A O     1 
HETATM 18689 O  O     . HOH   RA 9 .    ? -22.771 91.647  103.100 1.00 39.84 ? 2934 HOH   A O     1 
HETATM 18690 O  O     . HOH   RA 9 .    ? 20.566  61.757  96.219  1.00 41.27 ? 2935 HOH   A O     1 
HETATM 18691 O  O     . HOH   RA 9 .    ? -8.270  61.809  86.798  1.00 40.12 ? 2936 HOH   A O     1 
HETATM 18692 O  O     . HOH   RA 9 .    ? -8.833  62.659  69.780  1.00 42.51 ? 2937 HOH   A O     1 
HETATM 18693 O  O     . HOH   RA 9 .    ? -25.904 83.325  69.408  1.00 42.00 ? 2938 HOH   A O     1 
HETATM 18694 O  O     . HOH   RA 9 .    ? -53.378 54.585  54.663  1.00 44.71 ? 2939 HOH   A O     1 
HETATM 18695 O  O     . HOH   RA 9 .    ? 10.732  79.239  124.379 1.00 37.69 ? 2940 HOH   A O     1 
HETATM 18696 O  O     . HOH   RA 9 .    ? -67.872 33.114  74.257  1.00 48.84 ? 2941 HOH   A O     1 
HETATM 18697 O  O     . HOH   RA 9 .    ? -18.586 74.335  105.991 1.00 27.87 ? 2942 HOH   A O     1 
HETATM 18698 O  O     . HOH   RA 9 .    ? -22.731 90.421  100.651 1.00 33.57 ? 2943 HOH   A O     1 
HETATM 18699 O  O     . HOH   RA 9 .    ? -35.743 90.426  123.986 1.00 38.06 ? 2944 HOH   A O     1 
HETATM 18700 O  O     . HOH   RA 9 .    ? -14.410 96.384  114.104 1.00 44.64 ? 2945 HOH   A O     1 
HETATM 18701 O  O     . HOH   RA 9 .    ? -29.725 60.434  85.729  1.00 38.40 ? 2946 HOH   A O     1 
HETATM 18702 O  O     . HOH   RA 9 .    ? -10.316 68.998  136.100 1.00 48.06 ? 2947 HOH   A O     1 
HETATM 18703 O  O     . HOH   RA 9 .    ? -14.472 52.270  111.679 1.00 41.97 ? 2948 HOH   A O     1 
HETATM 18704 O  O     . HOH   RA 9 .    ? -9.019  62.413  94.011  1.00 33.45 ? 2949 HOH   A O     1 
HETATM 18705 O  O     . HOH   RA 9 .    ? -40.778 68.502  93.617  1.00 35.00 ? 2950 HOH   A O     1 
HETATM 18706 O  O     . HOH   RA 9 .    ? -32.156 66.196  124.510 1.00 33.03 ? 2951 HOH   A O     1 
HETATM 18707 O  O     . HOH   RA 9 .    ? -18.507 74.772  109.025 1.00 25.43 ? 2952 HOH   A O     1 
HETATM 18708 O  O     . HOH   RA 9 .    ? -21.167 98.693  128.913 1.00 47.95 ? 2953 HOH   A O     1 
HETATM 18709 O  O     . HOH   RA 9 .    ? -9.348  63.924  91.135  1.00 43.29 ? 2954 HOH   A O     1 
HETATM 18710 O  O     . HOH   RA 9 .    ? -0.612  61.250  112.348 1.00 40.63 ? 2955 HOH   A O     1 
HETATM 18711 O  O     . HOH   RA 9 .    ? -41.389 63.766  106.285 1.00 33.73 ? 2956 HOH   A O     1 
HETATM 18712 O  O     . HOH   RA 9 .    ? -1.755  63.671  87.646  1.00 39.20 ? 2957 HOH   A O     1 
HETATM 18713 O  O     . HOH   RA 9 .    ? 5.761   55.919  94.221  1.00 40.53 ? 2958 HOH   A O     1 
HETATM 18714 O  O     . HOH   RA 9 .    ? -29.630 92.594  108.663 1.00 36.65 ? 2959 HOH   A O     1 
HETATM 18715 O  O     . HOH   RA 9 .    ? -3.279  83.564  111.768 1.00 38.99 ? 2960 HOH   A O     1 
HETATM 18716 O  O     . HOH   RA 9 .    ? -24.895 97.481  126.032 1.00 40.72 ? 2961 HOH   A O     1 
HETATM 18717 O  O     . HOH   RA 9 .    ? -19.262 57.921  106.389 1.00 31.44 ? 2962 HOH   A O     1 
HETATM 18718 O  O     . HOH   RA 9 .    ? -24.764 97.264  121.582 1.00 39.30 ? 2963 HOH   A O     1 
HETATM 18719 O  O     . HOH   RA 9 .    ? -21.006 53.375  100.443 1.00 36.78 ? 2964 HOH   A O     1 
HETATM 18720 O  O     . HOH   RA 9 .    ? -34.657 38.989  104.070 1.00 41.23 ? 2965 HOH   A O     1 
HETATM 18721 O  O     . HOH   RA 9 .    ? 0.665   65.582  115.322 1.00 41.65 ? 2966 HOH   A O     1 
HETATM 18722 O  O     . HOH   RA 9 .    ? -51.975 73.381  102.624 1.00 29.62 ? 2967 HOH   A O     1 
HETATM 18723 O  O     . HOH   RA 9 .    ? -8.308  77.001  129.077 1.00 33.81 ? 2968 HOH   A O     1 
HETATM 18724 O  O     . HOH   RA 9 .    ? -28.507 77.941  70.124  1.00 36.90 ? 2969 HOH   A O     1 
HETATM 18725 O  O     . HOH   RA 9 .    ? 10.440  68.506  114.193 1.00 31.42 ? 2970 HOH   A O     1 
HETATM 18726 O  O     . HOH   RA 9 .    ? -24.206 62.550  99.882  1.00 30.79 ? 2971 HOH   A O     1 
HETATM 18727 O  O     . HOH   RA 9 .    ? -30.759 84.470  73.259  1.00 34.95 ? 2972 HOH   A O     1 
HETATM 18728 O  O     . HOH   RA 9 .    ? -62.886 55.372  69.982  1.00 36.79 ? 2973 HOH   A O     1 
HETATM 18729 O  O     . HOH   RA 9 .    ? 6.945   62.904  94.547  1.00 28.71 ? 2974 HOH   A O     1 
HETATM 18730 O  O     . HOH   RA 9 .    ? -53.166 69.418  100.944 1.00 34.56 ? 2975 HOH   A O     1 
HETATM 18731 O  O     . HOH   RA 9 .    ? 3.965   65.338  96.161  1.00 29.80 ? 2976 HOH   A O     1 
HETATM 18732 O  O     . HOH   RA 9 .    ? -62.419 53.629  65.916  1.00 36.42 ? 2977 HOH   A O     1 
HETATM 18733 O  O     . HOH   RA 9 .    ? 17.496  78.271  122.752 1.00 46.30 ? 2978 HOH   A O     1 
HETATM 18734 O  O     . HOH   RA 9 .    ? -28.529 92.541  134.001 1.00 41.08 ? 2979 HOH   A O     1 
HETATM 18735 O  O     . HOH   RA 9 .    ? -33.116 58.814  113.531 1.00 42.01 ? 2980 HOH   A O     1 
HETATM 18736 O  O     . HOH   RA 9 .    ? -54.408 59.095  104.303 1.00 39.70 ? 2981 HOH   A O     1 
HETATM 18737 O  O     . HOH   RA 9 .    ? -1.612  91.695  97.890  1.00 44.61 ? 2982 HOH   A O     1 
HETATM 18738 O  O     . HOH   RA 9 .    ? -12.842 53.532  80.882  1.00 42.26 ? 2983 HOH   A O     1 
HETATM 18739 O  O     . HOH   RA 9 .    ? -36.807 82.680  76.936  1.00 35.92 ? 2984 HOH   A O     1 
HETATM 18740 O  O     . HOH   RA 9 .    ? -32.049 75.205  85.229  1.00 36.49 ? 2985 HOH   A O     1 
HETATM 18741 O  O     . HOH   RA 9 .    ? -1.994  74.751  118.557 1.00 39.02 ? 2986 HOH   A O     1 
HETATM 18742 O  O     . HOH   RA 9 .    ? -61.498 50.729  66.131  1.00 40.65 ? 2987 HOH   A O     1 
HETATM 18743 O  O     . HOH   RA 9 .    ? -61.257 70.423  85.763  1.00 36.09 ? 2988 HOH   A O     1 
HETATM 18744 O  O     . HOH   RA 9 .    ? -53.023 75.370  101.508 1.00 41.03 ? 2989 HOH   A O     1 
HETATM 18745 O  O     . HOH   RA 9 .    ? -39.957 89.518  121.960 1.00 42.11 ? 2990 HOH   A O     1 
HETATM 18746 O  O     . HOH   RA 9 .    ? -62.909 57.103  96.586  1.00 35.64 ? 2991 HOH   A O     1 
HETATM 18747 O  O     . HOH   RA 9 .    ? -29.138 60.306  88.497  1.00 23.15 ? 2992 HOH   A O     1 
HETATM 18748 O  O     . HOH   RA 9 .    ? -30.461 86.748  74.287  1.00 44.48 ? 2993 HOH   A O     1 
HETATM 18749 O  O     . HOH   RA 9 .    ? 7.075   60.054  93.995  1.00 39.65 ? 2994 HOH   A O     1 
HETATM 18750 O  O     . HOH   RA 9 .    ? -8.593  52.922  101.531 1.00 46.49 ? 2995 HOH   A O     1 
HETATM 18751 O  O     . HOH   RA 9 .    ? -58.286 59.550  103.125 1.00 38.48 ? 2996 HOH   A O     1 
HETATM 18752 O  O     . HOH   RA 9 .    ? -56.668 52.726  98.664  1.00 32.30 ? 2997 HOH   A O     1 
HETATM 18753 O  O     . HOH   RA 9 .    ? 20.114  74.612  119.938 1.00 34.85 ? 2998 HOH   A O     1 
HETATM 18754 O  O     . HOH   RA 9 .    ? -55.206 46.103  65.309  1.00 43.47 ? 2999 HOH   A O     1 
HETATM 18755 O  O     . HOH   RA 9 .    ? -8.525  43.510  57.721  1.00 37.20 ? 3000 HOH   A O     1 
HETATM 18756 O  O     . HOH   RA 9 .    ? -51.435 47.153  96.726  1.00 27.59 ? 3001 HOH   A O     1 
HETATM 18757 O  O     . HOH   RA 9 .    ? -56.734 71.767  100.242 1.00 42.89 ? 3002 HOH   A O     1 
HETATM 18758 O  O     . HOH   RA 9 .    ? -21.603 68.774  132.035 1.00 38.88 ? 3003 HOH   A O     1 
HETATM 18759 O  O     . HOH   RA 9 .    ? -2.131  84.725  96.077  1.00 36.82 ? 3004 HOH   A O     1 
HETATM 18760 O  O     . HOH   RA 9 .    ? -37.925 69.316  95.818  1.00 34.76 ? 3005 HOH   A O     1 
HETATM 18761 O  O     . HOH   RA 9 .    ? -47.098 37.110  100.672 1.00 38.33 ? 3006 HOH   A O     1 
HETATM 18762 O  O     . HOH   RA 9 .    ? -23.398 102.329 90.121  1.00 39.70 ? 3007 HOH   A O     1 
HETATM 18763 O  O     . HOH   RA 9 .    ? -56.007 78.837  77.098  1.00 38.12 ? 3008 HOH   A O     1 
HETATM 18764 O  O     . HOH   RA 9 .    ? -54.631 52.965  100.766 1.00 33.99 ? 3009 HOH   A O     1 
HETATM 18765 O  O     . HOH   RA 9 .    ? -35.278 39.737  73.207  1.00 40.06 ? 3010 HOH   A O     1 
HETATM 18766 O  O     . HOH   RA 9 .    ? -57.939 46.828  63.823  1.00 49.06 ? 3011 HOH   A O     1 
HETATM 18767 O  O     . HOH   RA 9 .    ? -14.724 39.362  70.046  1.00 46.72 ? 3012 HOH   A O     1 
HETATM 18768 O  O     . HOH   RA 9 .    ? -34.621 63.989  121.545 1.00 40.04 ? 3013 HOH   A O     1 
HETATM 18769 O  O     . HOH   RA 9 .    ? -61.895 53.082  93.904  1.00 44.89 ? 3014 HOH   A O     1 
HETATM 18770 O  O     . HOH   RA 9 .    ? -22.721 102.666 94.921  1.00 46.17 ? 3015 HOH   A O     1 
HETATM 18771 O  O     . HOH   RA 9 .    ? -36.431 34.729  89.500  1.00 41.16 ? 3016 HOH   A O     1 
HETATM 18772 O  O     . HOH   RA 9 .    ? -32.734 57.485  110.955 1.00 30.79 ? 3017 HOH   A O     1 
HETATM 18773 O  O     . HOH   RA 9 .    ? -61.854 55.229  97.649  1.00 41.49 ? 3018 HOH   A O     1 
HETATM 18774 O  O     . HOH   RA 9 .    ? -52.988 78.813  90.783  1.00 43.87 ? 3019 HOH   A O     1 
HETATM 18775 O  O     . HOH   RA 9 .    ? -65.696 68.482  86.838  1.00 43.72 ? 3020 HOH   A O     1 
HETATM 18776 O  O     . HOH   RA 9 .    ? -53.973 71.658  102.329 1.00 38.15 ? 3021 HOH   A O     1 
HETATM 18777 O  O     . HOH   RA 9 .    ? -36.000 32.053  90.852  1.00 47.29 ? 3022 HOH   A O     1 
HETATM 18778 O  O     . HOH   RA 9 .    ? -53.200 47.546  98.801  1.00 36.19 ? 3023 HOH   A O     1 
HETATM 18779 O  O     . HOH   RA 9 .    ? -35.890 81.633  70.222  1.00 36.73 ? 3024 HOH   A O     1 
HETATM 18780 O  O     . HOH   RA 9 .    ? -33.819 81.537  71.618  1.00 35.65 ? 3025 HOH   A O     1 
HETATM 18781 O  O     . HOH   SA 9 .    ? -11.041 28.075  81.012  1.00 28.06 ? 2101 HOH   B O     1 
HETATM 18782 O  O     . HOH   SA 9 .    ? 15.518  53.831  81.506  1.00 32.78 ? 2102 HOH   B O     1 
HETATM 18783 O  O     . HOH   SA 9 .    ? 2.948   12.318  65.166  1.00 42.43 ? 2103 HOH   B O     1 
HETATM 18784 O  O     . HOH   SA 9 .    ? -0.417  46.844  133.028 1.00 40.99 ? 2104 HOH   B O     1 
HETATM 18785 O  O     . HOH   SA 9 .    ? -2.499  5.373   84.561  1.00 30.83 ? 2105 HOH   B O     1 
HETATM 18786 O  O     . HOH   SA 9 .    ? -0.056  76.061  67.971  1.00 40.47 ? 2106 HOH   B O     1 
HETATM 18787 O  O     . HOH   SA 9 .    ? -0.958  22.681  70.748  1.00 28.69 ? 2107 HOH   B O     1 
HETATM 18788 O  O     . HOH   SA 9 .    ? 26.237  8.557   78.607  1.00 40.92 ? 2108 HOH   B O     1 
HETATM 18789 O  O     . HOH   SA 9 .    ? 22.677  10.277  84.547  1.00 38.16 ? 2109 HOH   B O     1 
HETATM 18790 O  O     . HOH   SA 9 .    ? 21.192  40.376  47.533  1.00 33.59 ? 2110 HOH   B O     1 
HETATM 18791 O  O     . HOH   SA 9 .    ? 14.001  81.513  69.274  1.00 34.60 ? 2111 HOH   B O     1 
HETATM 18792 O  O     . HOH   SA 9 .    ? -5.596  37.582  77.502  1.00 30.72 ? 2112 HOH   B O     1 
HETATM 18793 O  O     . HOH   SA 9 .    ? 4.107   72.405  85.506  1.00 36.66 ? 2113 HOH   B O     1 
HETATM 18794 O  O     . HOH   SA 9 .    ? 28.665  69.433  72.331  1.00 29.39 ? 2114 HOH   B O     1 
HETATM 18795 O  O     . HOH   SA 9 .    ? 11.039  79.955  67.391  1.00 41.21 ? 2115 HOH   B O     1 
HETATM 18796 O  O     . HOH   SA 9 .    ? 23.040  37.625  85.840  1.00 26.70 ? 2116 HOH   B O     1 
HETATM 18797 O  O     . HOH   SA 9 .    ? -2.333  45.605  102.396 1.00 32.17 ? 2117 HOH   B O     1 
HETATM 18798 O  O     . HOH   SA 9 .    ? -22.438 19.287  101.729 1.00 36.48 ? 2118 HOH   B O     1 
HETATM 18799 O  O     . HOH   SA 9 .    ? -29.760 12.382  96.086  1.00 41.47 ? 2119 HOH   B O     1 
HETATM 18800 O  O     . HOH   SA 9 .    ? -0.766  -8.287  101.774 1.00 35.82 ? 2120 HOH   B O     1 
HETATM 18801 O  O     . HOH   SA 9 .    ? 2.754   18.022  112.101 1.00 30.10 ? 2121 HOH   B O     1 
HETATM 18802 O  O     . HOH   SA 9 .    ? -6.316  48.734  79.071  1.00 36.66 ? 2122 HOH   B O     1 
HETATM 18803 O  O     . HOH   SA 9 .    ? 13.098  50.052  64.355  1.00 29.44 ? 2123 HOH   B O     1 
HETATM 18804 O  O     . HOH   SA 9 .    ? -9.060  10.530  122.789 1.00 25.43 ? 2124 HOH   B O     1 
HETATM 18805 O  O     . HOH   SA 9 .    ? -10.471 1.941   121.383 1.00 35.38 ? 2125 HOH   B O     1 
HETATM 18806 O  O     . HOH   SA 9 .    ? 12.940  6.799   117.553 1.00 34.70 ? 2126 HOH   B O     1 
HETATM 18807 O  O     . HOH   SA 9 .    ? 0.959   0.240   95.891  1.00 32.80 ? 2127 HOH   B O     1 
HETATM 18808 O  O     . HOH   SA 9 .    ? -31.857 17.853  91.064  1.00 38.71 ? 2128 HOH   B O     1 
HETATM 18809 O  O     . HOH   SA 9 .    ? 28.603  40.295  50.482  1.00 39.77 ? 2129 HOH   B O     1 
HETATM 18810 O  O     . HOH   SA 9 .    ? 12.033  16.929  67.293  1.00 32.95 ? 2130 HOH   B O     1 
HETATM 18811 O  O     . HOH   SA 9 .    ? 30.044  27.615  55.690  1.00 25.89 ? 2131 HOH   B O     1 
HETATM 18812 O  O     . HOH   SA 9 .    ? -4.597  27.352  69.957  1.00 26.96 ? 2132 HOH   B O     1 
HETATM 18813 O  O     . HOH   SA 9 .    ? 4.955   32.776  89.503  1.00 30.29 ? 2133 HOH   B O     1 
HETATM 18814 O  O     . HOH   SA 9 .    ? -28.156 6.300   101.473 1.00 37.93 ? 2134 HOH   B O     1 
HETATM 18815 O  O     . HOH   SA 9 .    ? -7.100  -0.763  119.593 1.00 32.67 ? 2135 HOH   B O     1 
HETATM 18816 O  O     . HOH   SA 9 .    ? 18.675  13.053  95.024  1.00 30.39 ? 2136 HOH   B O     1 
HETATM 18817 O  O     . HOH   SA 9 .    ? 1.343   38.991  105.269 1.00 35.30 ? 2137 HOH   B O     1 
HETATM 18818 O  O     . HOH   SA 9 .    ? 7.339   32.888  97.835  1.00 33.62 ? 2138 HOH   B O     1 
HETATM 18819 O  O     . HOH   SA 9 .    ? 12.788  36.953  85.663  1.00 21.86 ? 2139 HOH   B O     1 
HETATM 18820 O  O     . HOH   SA 9 .    ? -12.334 20.312  83.683  1.00 25.45 ? 2140 HOH   B O     1 
HETATM 18821 O  O     . HOH   SA 9 .    ? 33.250  29.772  61.394  1.00 33.43 ? 2141 HOH   B O     1 
HETATM 18822 O  O     . HOH   SA 9 .    ? -6.817  8.736   110.708 1.00 26.48 ? 2142 HOH   B O     1 
HETATM 18823 O  O     . HOH   SA 9 .    ? -29.926 16.224  122.766 1.00 40.18 ? 2143 HOH   B O     1 
HETATM 18824 O  O     . HOH   SA 9 .    ? 9.660   31.189  109.547 1.00 39.49 ? 2144 HOH   B O     1 
HETATM 18825 O  O     . HOH   SA 9 .    ? 1.524   15.456  115.743 1.00 26.67 ? 2145 HOH   B O     1 
HETATM 18826 O  O     . HOH   SA 9 .    ? 6.763   6.021   91.869  1.00 24.05 ? 2146 HOH   B O     1 
HETATM 18827 O  O     . HOH   SA 9 .    ? 2.658   44.360  70.160  1.00 18.90 ? 2147 HOH   B O     1 
HETATM 18828 O  O     . HOH   SA 9 .    ? 33.258  19.546  87.203  1.00 24.44 ? 2148 HOH   B O     1 
HETATM 18829 O  O     . HOH   SA 9 .    ? 3.815   21.830  102.261 1.00 37.61 ? 2149 HOH   B O     1 
HETATM 18830 O  O     . HOH   SA 9 .    ? -32.949 33.125  107.080 1.00 50.12 ? 2150 HOH   B O     1 
HETATM 18831 O  O     . HOH   SA 9 .    ? 2.898   22.323  129.634 1.00 33.87 ? 2151 HOH   B O     1 
HETATM 18832 O  O     . HOH   SA 9 .    ? -10.736 20.302  122.276 1.00 33.48 ? 2152 HOH   B O     1 
HETATM 18833 O  O     . HOH   SA 9 .    ? 1.798   20.807  103.783 1.00 35.42 ? 2153 HOH   B O     1 
HETATM 18834 O  O     . HOH   SA 9 .    ? 11.127  18.676  64.351  1.00 22.51 ? 2154 HOH   B O     1 
HETATM 18835 O  O     . HOH   SA 9 .    ? -16.163 52.451  123.298 1.00 41.50 ? 2155 HOH   B O     1 
HETATM 18836 O  O     . HOH   SA 9 .    ? 6.507   6.004   85.780  1.00 21.74 ? 2156 HOH   B O     1 
HETATM 18837 O  O     . HOH   SA 9 .    ? 20.018  51.294  77.127  1.00 25.94 ? 2157 HOH   B O     1 
HETATM 18838 O  O     . HOH   SA 9 .    ? -1.172  14.897  85.685  1.00 23.21 ? 2158 HOH   B O     1 
HETATM 18839 O  O     . HOH   SA 9 .    ? 22.462  45.867  90.350  1.00 27.35 ? 2159 HOH   B O     1 
HETATM 18840 O  O     . HOH   SA 9 .    ? 25.563  30.292  108.726 1.00 41.91 ? 2160 HOH   B O     1 
HETATM 18841 O  O     . HOH   SA 9 .    ? 7.106   8.207   74.796  1.00 32.88 ? 2161 HOH   B O     1 
HETATM 18842 O  O     . HOH   SA 9 .    ? -18.085 -3.541  109.459 1.00 42.01 ? 2162 HOH   B O     1 
HETATM 18843 O  O     . HOH   SA 9 .    ? -5.053  -1.530  123.299 1.00 41.46 ? 2163 HOH   B O     1 
HETATM 18844 O  O     . HOH   SA 9 .    ? -3.258  10.784  84.077  1.00 28.44 ? 2164 HOH   B O     1 
HETATM 18845 O  O     . HOH   SA 9 .    ? 19.290  70.730  58.969  1.00 36.82 ? 2165 HOH   B O     1 
HETATM 18846 O  O     . HOH   SA 9 .    ? 21.313  50.666  87.625  1.00 34.23 ? 2166 HOH   B O     1 
HETATM 18847 O  O     . HOH   SA 9 .    ? 5.841   55.952  104.452 1.00 27.62 ? 2167 HOH   B O     1 
HETATM 18848 O  O     . HOH   SA 9 .    ? 34.365  62.567  78.359  1.00 18.54 ? 2168 HOH   B O     1 
HETATM 18849 O  O     . HOH   SA 9 .    ? 19.670  5.554   76.581  1.00 34.54 ? 2169 HOH   B O     1 
HETATM 18850 O  O     . HOH   SA 9 .    ? 11.124  46.703  106.247 1.00 27.75 ? 2170 HOH   B O     1 
HETATM 18851 O  O     . HOH   SA 9 .    ? 19.877  60.158  56.761  1.00 33.64 ? 2171 HOH   B O     1 
HETATM 18852 O  O     . HOH   SA 9 .    ? 10.330  49.754  55.624  1.00 32.25 ? 2172 HOH   B O     1 
HETATM 18853 O  O     . HOH   SA 9 .    ? -6.206  51.362  72.707  1.00 17.70 ? 2173 HOH   B O     1 
HETATM 18854 O  O     . HOH   SA 9 .    ? -4.001  19.058  97.777  1.00 15.36 ? 2174 HOH   B O     1 
HETATM 18855 O  O     . HOH   SA 9 .    ? -20.178 25.951  101.832 1.00 38.97 ? 2175 HOH   B O     1 
HETATM 18856 O  O     . HOH   SA 9 .    ? 32.806  19.162  57.530  1.00 37.50 ? 2176 HOH   B O     1 
HETATM 18857 O  O     . HOH   SA 9 .    ? 10.630  17.088  121.222 1.00 36.49 ? 2177 HOH   B O     1 
HETATM 18858 O  O     . HOH   SA 9 .    ? 23.427  48.689  106.805 1.00 34.05 ? 2178 HOH   B O     1 
HETATM 18859 O  O     . HOH   SA 9 .    ? -1.201  67.448  75.151  1.00 31.86 ? 2179 HOH   B O     1 
HETATM 18860 O  O     . HOH   SA 9 .    ? -14.135 9.576   118.449 1.00 38.13 ? 2180 HOH   B O     1 
HETATM 18861 O  O     . HOH   SA 9 .    ? -10.217 40.117  126.693 1.00 42.48 ? 2181 HOH   B O     1 
HETATM 18862 O  O     . HOH   SA 9 .    ? 15.539  38.778  76.935  1.00 27.78 ? 2182 HOH   B O     1 
HETATM 18863 O  O     . HOH   SA 9 .    ? 17.788  53.000  66.274  1.00 32.03 ? 2183 HOH   B O     1 
HETATM 18864 O  O     . HOH   SA 9 .    ? 4.476   42.475  84.172  1.00 23.00 ? 2184 HOH   B O     1 
HETATM 18865 O  O     . HOH   SA 9 .    ? 25.971  55.404  77.085  1.00 27.03 ? 2185 HOH   B O     1 
HETATM 18866 O  O     . HOH   SA 9 .    ? 2.665   39.764  98.420  1.00 23.29 ? 2186 HOH   B O     1 
HETATM 18867 O  O     . HOH   SA 9 .    ? 8.536   45.715  132.228 1.00 41.30 ? 2187 HOH   B O     1 
HETATM 18868 O  O     . HOH   SA 9 .    ? -23.642 23.257  84.006  1.00 36.70 ? 2188 HOH   B O     1 
HETATM 18869 O  O     . HOH   SA 9 .    ? 9.253   23.825  108.756 1.00 31.05 ? 2189 HOH   B O     1 
HETATM 18870 O  O     . HOH   SA 9 .    ? -16.426 5.216   116.211 1.00 32.86 ? 2190 HOH   B O     1 
HETATM 18871 O  O     . HOH   SA 9 .    ? -14.294 40.260  124.558 1.00 45.19 ? 2191 HOH   B O     1 
HETATM 18872 O  O     . HOH   SA 9 .    ? 4.468   21.726  118.524 1.00 35.84 ? 2192 HOH   B O     1 
HETATM 18873 O  O     . HOH   SA 9 .    ? 39.265  26.922  87.852  1.00 42.95 ? 2193 HOH   B O     1 
HETATM 18874 O  O     . HOH   SA 9 .    ? 17.910  13.128  116.961 1.00 26.26 ? 2194 HOH   B O     1 
HETATM 18875 O  O     . HOH   SA 9 .    ? 35.965  38.310  90.962  1.00 43.59 ? 2195 HOH   B O     1 
HETATM 18876 O  O     . HOH   SA 9 .    ? 3.460   34.168  86.319  1.00 22.08 ? 2196 HOH   B O     1 
HETATM 18877 O  O     . HOH   SA 9 .    ? 33.768  12.586  74.273  1.00 38.16 ? 2197 HOH   B O     1 
HETATM 18878 O  O     . HOH   SA 9 .    ? -13.044 54.390  122.287 1.00 30.18 ? 2198 HOH   B O     1 
HETATM 18879 O  O     . HOH   SA 9 .    ? 15.325  40.742  73.047  1.00 19.96 ? 2199 HOH   B O     1 
HETATM 18880 O  O     . HOH   SA 9 .    ? 8.368   8.072   72.417  1.00 38.46 ? 2200 HOH   B O     1 
HETATM 18881 O  O     . HOH   SA 9 .    ? -4.579  50.994  78.185  1.00 35.64 ? 2201 HOH   B O     1 
HETATM 18882 O  O     . HOH   SA 9 .    ? 3.155   18.614  88.824  1.00 30.26 ? 2202 HOH   B O     1 
HETATM 18883 O  O     . HOH   SA 9 .    ? 16.665  14.998  108.953 1.00 31.47 ? 2203 HOH   B O     1 
HETATM 18884 O  O     . HOH   SA 9 .    ? 1.132   42.396  76.150  1.00 25.90 ? 2204 HOH   B O     1 
HETATM 18885 O  O     . HOH   SA 9 .    ? 27.230  62.649  84.637  1.00 32.38 ? 2205 HOH   B O     1 
HETATM 18886 O  O     . HOH   SA 9 .    ? 31.850  54.400  67.796  1.00 32.34 ? 2206 HOH   B O     1 
HETATM 18887 O  O     . HOH   SA 9 .    ? 17.342  40.976  71.277  1.00 19.28 ? 2207 HOH   B O     1 
HETATM 18888 O  O     . HOH   SA 9 .    ? -8.779  45.796  108.467 1.00 36.35 ? 2208 HOH   B O     1 
HETATM 18889 O  O     . HOH   SA 9 .    ? 7.206   51.768  57.312  1.00 33.46 ? 2209 HOH   B O     1 
HETATM 18890 O  O     . HOH   SA 9 .    ? 14.613  41.397  77.134  1.00 25.25 ? 2210 HOH   B O     1 
HETATM 18891 O  O     . HOH   SA 9 .    ? 8.348   30.686  85.068  1.00 35.66 ? 2211 HOH   B O     1 
HETATM 18892 O  O     . HOH   SA 9 .    ? -18.738 50.540  120.310 1.00 39.52 ? 2212 HOH   B O     1 
HETATM 18893 O  O     . HOH   SA 9 .    ? -25.438 22.417  101.492 1.00 41.40 ? 2213 HOH   B O     1 
HETATM 18894 O  O     . HOH   SA 9 .    ? 6.666   44.649  57.891  1.00 30.82 ? 2214 HOH   B O     1 
HETATM 18895 O  O     . HOH   SA 9 .    ? -4.830  -5.939  111.753 1.00 36.43 ? 2215 HOH   B O     1 
HETATM 18896 O  O     . HOH   SA 9 .    ? -17.661 26.370  82.682  1.00 36.51 ? 2216 HOH   B O     1 
HETATM 18897 O  O     . HOH   SA 9 .    ? 16.315  43.579  50.250  1.00 32.04 ? 2217 HOH   B O     1 
HETATM 18898 O  O     . HOH   SA 9 .    ? -35.268 16.908  100.895 1.00 40.53 ? 2218 HOH   B O     1 
HETATM 18899 O  O     . HOH   SA 9 .    ? -2.251  24.559  76.059  1.00 22.35 ? 2219 HOH   B O     1 
HETATM 18900 O  O     . HOH   SA 9 .    ? 10.541  24.985  103.371 1.00 36.44 ? 2220 HOH   B O     1 
HETATM 18901 O  O     . HOH   SA 9 .    ? 16.355  16.347  84.797  1.00 24.91 ? 2221 HOH   B O     1 
HETATM 18902 O  O     . HOH   SA 9 .    ? -13.381 18.362  105.364 1.00 25.35 ? 2222 HOH   B O     1 
HETATM 18903 O  O     . HOH   SA 9 .    ? 12.100  11.369  71.286  1.00 25.63 ? 2223 HOH   B O     1 
HETATM 18904 O  O     . HOH   SA 9 .    ? -2.109  49.189  63.348  1.00 20.30 ? 2224 HOH   B O     1 
HETATM 18905 O  O     . HOH   SA 9 .    ? -4.494  60.340  125.169 1.00 33.57 ? 2225 HOH   B O     1 
HETATM 18906 O  O     . HOH   SA 9 .    ? 11.878  37.798  72.100  1.00 18.87 ? 2226 HOH   B O     1 
HETATM 18907 O  O     . HOH   SA 9 .    ? 12.829  50.564  75.053  1.00 37.02 ? 2227 HOH   B O     1 
HETATM 18908 O  O     . HOH   SA 9 .    ? -6.626  35.631  69.127  1.00 31.81 ? 2228 HOH   B O     1 
HETATM 18909 O  O     . HOH   SA 9 .    ? 9.755   26.357  54.786  1.00 22.30 ? 2229 HOH   B O     1 
HETATM 18910 O  O     . HOH   SA 9 .    ? 7.253   34.291  86.389  1.00 24.42 ? 2230 HOH   B O     1 
HETATM 18911 O  O     . HOH   SA 9 .    ? 15.562  52.868  58.367  1.00 30.90 ? 2231 HOH   B O     1 
HETATM 18912 O  O     . HOH   SA 9 .    ? 28.234  29.939  83.130  1.00 18.26 ? 2232 HOH   B O     1 
HETATM 18913 O  O     . HOH   SA 9 .    ? 11.693  34.973  51.580  1.00 34.35 ? 2233 HOH   B O     1 
HETATM 18914 O  O     . HOH   SA 9 .    ? -6.539  52.738  107.083 1.00 31.72 ? 2234 HOH   B O     1 
HETATM 18915 O  O     . HOH   SA 9 .    ? -7.351  27.510  99.527  1.00 33.22 ? 2235 HOH   B O     1 
HETATM 18916 O  O     . HOH   SA 9 .    ? 5.524   36.597  48.919  1.00 37.26 ? 2236 HOH   B O     1 
HETATM 18917 O  O     . HOH   SA 9 .    ? -1.113  38.491  80.008  1.00 31.37 ? 2237 HOH   B O     1 
HETATM 18918 O  O     . HOH   SA 9 .    ? 10.374  51.214  64.601  1.00 27.23 ? 2238 HOH   B O     1 
HETATM 18919 O  O     . HOH   SA 9 .    ? 7.364   43.365  49.501  1.00 31.98 ? 2239 HOH   B O     1 
HETATM 18920 O  O     . HOH   SA 9 .    ? 20.057  43.702  87.677  1.00 21.06 ? 2240 HOH   B O     1 
HETATM 18921 O  O     . HOH   SA 9 .    ? 1.840   13.547  101.540 1.00 20.40 ? 2241 HOH   B O     1 
HETATM 18922 O  O     . HOH   SA 9 .    ? 22.839  48.836  77.785  1.00 26.53 ? 2242 HOH   B O     1 
HETATM 18923 O  O     . HOH   SA 9 .    ? 16.205  48.767  70.649  1.00 20.78 ? 2243 HOH   B O     1 
HETATM 18924 O  O     . HOH   SA 9 .    ? 0.580   36.262  109.145 1.00 38.56 ? 2244 HOH   B O     1 
HETATM 18925 O  O     . HOH   SA 9 .    ? 17.212  43.914  79.176  1.00 29.79 ? 2245 HOH   B O     1 
HETATM 18926 O  O     . HOH   SA 9 .    ? 37.721  32.821  103.165 1.00 47.04 ? 2246 HOH   B O     1 
HETATM 18927 O  O     . HOH   SA 9 .    ? -6.183  12.572  125.065 1.00 33.62 ? 2247 HOH   B O     1 
HETATM 18928 O  O     . HOH   SA 9 .    ? 11.387  6.239   121.595 1.00 30.61 ? 2248 HOH   B O     1 
HETATM 18929 O  O     . HOH   SA 9 .    ? -10.515 46.832  74.204  1.00 21.53 ? 2249 HOH   B O     1 
HETATM 18930 O  O     . HOH   SA 9 .    ? 19.031  25.317  54.011  1.00 23.96 ? 2250 HOH   B O     1 
HETATM 18931 O  O     . HOH   SA 9 .    ? 10.417  50.818  90.018  1.00 39.16 ? 2251 HOH   B O     1 
HETATM 18932 O  O     . HOH   SA 9 .    ? 4.052   55.712  72.484  1.00 26.90 ? 2252 HOH   B O     1 
HETATM 18933 O  O     . HOH   SA 9 .    ? -2.167  42.411  61.539  1.00 24.16 ? 2253 HOH   B O     1 
HETATM 18934 O  O     . HOH   SA 9 .    ? 11.971  1.142   94.523  1.00 38.61 ? 2254 HOH   B O     1 
HETATM 18935 O  O     . HOH   SA 9 .    ? 14.977  20.813  91.794  1.00 37.41 ? 2255 HOH   B O     1 
HETATM 18936 O  O     . HOH   SA 9 .    ? 3.868   8.246   91.930  1.00 22.97 ? 2256 HOH   B O     1 
HETATM 18937 O  O     . HOH   SA 9 .    ? 29.333  69.379  79.275  1.00 22.88 ? 2257 HOH   B O     1 
HETATM 18938 O  O     . HOH   SA 9 .    ? 23.485  52.519  62.272  1.00 24.82 ? 2258 HOH   B O     1 
HETATM 18939 O  O     . HOH   SA 9 .    ? 21.735  79.994  69.961  1.00 37.20 ? 2259 HOH   B O     1 
HETATM 18940 O  O     . HOH   SA 9 .    ? -1.865  54.515  87.541  1.00 42.20 ? 2260 HOH   B O     1 
HETATM 18941 O  O     . HOH   SA 9 .    ? 1.058   55.926  110.218 1.00 29.80 ? 2261 HOH   B O     1 
HETATM 18942 O  O     . HOH   SA 9 .    ? 10.955  19.890  61.602  1.00 26.18 ? 2262 HOH   B O     1 
HETATM 18943 O  O     . HOH   SA 9 .    ? -13.990 54.590  117.824 1.00 31.51 ? 2263 HOH   B O     1 
HETATM 18944 O  O     . HOH   SA 9 .    ? -14.458 24.197  107.959 1.00 32.34 ? 2264 HOH   B O     1 
HETATM 18945 O  O     . HOH   SA 9 .    ? 33.912  19.014  70.813  1.00 41.01 ? 2265 HOH   B O     1 
HETATM 18946 O  O     . HOH   SA 9 .    ? -18.686 24.248  114.669 1.00 35.86 ? 2266 HOH   B O     1 
HETATM 18947 O  O     . HOH   SA 9 .    ? -1.641  11.574  100.987 1.00 20.91 ? 2267 HOH   B O     1 
HETATM 18948 O  O     . HOH   SA 9 .    ? -27.771 4.038   116.173 1.00 50.89 ? 2268 HOH   B O     1 
HETATM 18949 O  O     . HOH   SA 9 .    ? 16.850  53.398  63.866  1.00 32.70 ? 2269 HOH   B O     1 
HETATM 18950 O  O     . HOH   SA 9 .    ? 32.886  28.794  52.518  1.00 34.60 ? 2270 HOH   B O     1 
HETATM 18951 O  O     . HOH   SA 9 .    ? -4.282  -1.633  96.583  1.00 27.34 ? 2271 HOH   B O     1 
HETATM 18952 O  O     . HOH   SA 9 .    ? 21.746  30.197  71.036  1.00 19.49 ? 2272 HOH   B O     1 
HETATM 18953 O  O     . HOH   SA 9 .    ? 33.299  18.202  89.505  1.00 28.85 ? 2273 HOH   B O     1 
HETATM 18954 O  O     . HOH   SA 9 .    ? -2.375  21.842  91.345  1.00 18.48 ? 2274 HOH   B O     1 
HETATM 18955 O  O     . HOH   SA 9 .    ? 19.106  6.119   73.791  1.00 30.18 ? 2275 HOH   B O     1 
HETATM 18956 O  O     . HOH   SA 9 .    ? 28.712  9.620   73.448  1.00 36.13 ? 2276 HOH   B O     1 
HETATM 18957 O  O     . HOH   SA 9 .    ? -4.096  64.620  80.766  1.00 20.59 ? 2277 HOH   B O     1 
HETATM 18958 O  O     . HOH   SA 9 .    ? 13.614  10.617  90.891  1.00 29.16 ? 2278 HOH   B O     1 
HETATM 18959 O  O     . HOH   SA 9 .    ? 4.509   -8.270  103.917 1.00 30.10 ? 2279 HOH   B O     1 
HETATM 18960 O  O     . HOH   SA 9 .    ? -2.183  39.786  87.030  1.00 21.93 ? 2280 HOH   B O     1 
HETATM 18961 O  O     . HOH   SA 9 .    ? -5.333  5.620   121.853 1.00 28.59 ? 2281 HOH   B O     1 
HETATM 18962 O  O     . HOH   SA 9 .    ? 1.138   29.019  82.699  1.00 18.53 ? 2282 HOH   B O     1 
HETATM 18963 O  O     . HOH   SA 9 .    ? 10.283  51.740  75.532  1.00 28.54 ? 2283 HOH   B O     1 
HETATM 18964 O  O     . HOH   SA 9 .    ? -0.282  56.180  86.115  1.00 34.99 ? 2284 HOH   B O     1 
HETATM 18965 O  O     . HOH   SA 9 .    ? 4.954   63.280  83.930  1.00 21.68 ? 2285 HOH   B O     1 
HETATM 18966 O  O     . HOH   SA 9 .    ? -2.512  27.288  59.942  1.00 36.41 ? 2286 HOH   B O     1 
HETATM 18967 O  O     . HOH   SA 9 .    ? 15.310  56.170  73.800  1.00 28.58 ? 2287 HOH   B O     1 
HETATM 18968 O  O     . HOH   SA 9 .    ? 21.160  5.584   67.486  1.00 36.41 ? 2288 HOH   B O     1 
HETATM 18969 O  O     . HOH   SA 9 .    ? 25.588  55.215  61.911  1.00 23.89 ? 2289 HOH   B O     1 
HETATM 18970 O  O     . HOH   SA 9 .    ? 1.838   13.901  104.366 1.00 20.16 ? 2290 HOH   B O     1 
HETATM 18971 O  O     . HOH   SA 9 .    ? 27.322  38.051  89.820  1.00 30.47 ? 2291 HOH   B O     1 
HETATM 18972 O  O     . HOH   SA 9 .    ? 22.396  25.008  108.274 1.00 26.30 ? 2292 HOH   B O     1 
HETATM 18973 O  O     . HOH   SA 9 .    ? -8.090  24.206  105.976 1.00 33.83 ? 2293 HOH   B O     1 
HETATM 18974 O  O     . HOH   SA 9 .    ? 0.174   18.838  80.088  1.00 28.64 ? 2294 HOH   B O     1 
HETATM 18975 O  O     . HOH   SA 9 .    ? 11.398  25.053  107.849 1.00 36.49 ? 2295 HOH   B O     1 
HETATM 18976 O  O     . HOH   SA 9 .    ? 19.256  79.592  68.419  1.00 33.68 ? 2296 HOH   B O     1 
HETATM 18977 O  O     . HOH   SA 9 .    ? 22.859  67.585  64.463  1.00 24.01 ? 2297 HOH   B O     1 
HETATM 18978 O  O     . HOH   SA 9 .    ? 23.578  12.153  89.835  1.00 35.33 ? 2298 HOH   B O     1 
HETATM 18979 O  O     . HOH   SA 9 .    ? 0.198   4.676   88.009  1.00 23.88 ? 2299 HOH   B O     1 
HETATM 18980 O  O     . HOH   SA 9 .    ? -0.290  27.407  68.209  1.00 17.48 ? 2300 HOH   B O     1 
HETATM 18981 O  O     . HOH   SA 9 .    ? 12.330  53.655  61.600  1.00 31.60 ? 2301 HOH   B O     1 
HETATM 18982 O  O     . HOH   SA 9 .    ? 5.449   43.797  55.377  1.00 31.21 ? 2302 HOH   B O     1 
HETATM 18983 O  O     . HOH   SA 9 .    ? 15.565  17.050  87.416  1.00 24.57 ? 2303 HOH   B O     1 
HETATM 18984 O  O     . HOH   SA 9 .    ? 36.549  20.085  89.457  1.00 46.04 ? 2304 HOH   B O     1 
HETATM 18985 O  O     . HOH   SA 9 .    ? 12.803  2.499   110.792 1.00 31.24 ? 2305 HOH   B O     1 
HETATM 18986 O  O     . HOH   SA 9 .    ? -7.402  24.531  116.207 1.00 39.66 ? 2306 HOH   B O     1 
HETATM 18987 O  O     . HOH   SA 9 .    ? -10.405 52.783  128.018 1.00 39.68 ? 2307 HOH   B O     1 
HETATM 18988 O  O     . HOH   SA 9 .    ? 23.020  73.388  64.821  1.00 36.09 ? 2308 HOH   B O     1 
HETATM 18989 O  O     . HOH   SA 9 .    ? 18.668  7.712   100.294 1.00 36.42 ? 2309 HOH   B O     1 
HETATM 18990 O  O     . HOH   SA 9 .    ? -11.492 18.742  126.305 1.00 30.91 ? 2310 HOH   B O     1 
HETATM 18991 O  O     . HOH   SA 9 .    ? 18.574  9.404   91.758  1.00 37.41 ? 2311 HOH   B O     1 
HETATM 18992 O  O     . HOH   SA 9 .    ? 12.256  56.006  65.326  1.00 35.56 ? 2312 HOH   B O     1 
HETATM 18993 O  O     . HOH   SA 9 .    ? 24.874  57.824  78.023  1.00 22.85 ? 2313 HOH   B O     1 
HETATM 18994 O  O     . HOH   SA 9 .    ? -30.983 16.498  101.884 1.00 36.65 ? 2314 HOH   B O     1 
HETATM 18995 O  O     . HOH   SA 9 .    ? 1.336   10.976  129.125 1.00 31.99 ? 2315 HOH   B O     1 
HETATM 18996 O  O     . HOH   SA 9 .    ? 34.348  55.428  75.753  1.00 37.82 ? 2316 HOH   B O     1 
HETATM 18997 O  O     . HOH   SA 9 .    ? -5.000  42.970  72.455  1.00 31.12 ? 2317 HOH   B O     1 
HETATM 18998 O  O     . HOH   SA 9 .    ? 24.166  69.098  67.302  1.00 22.40 ? 2318 HOH   B O     1 
HETATM 18999 O  O     . HOH   SA 9 .    ? 18.400  43.960  91.280  1.00 18.41 ? 2319 HOH   B O     1 
HETATM 19000 O  O     . HOH   SA 9 .    ? 7.629   49.370  106.443 1.00 23.79 ? 2320 HOH   B O     1 
HETATM 19001 O  O     . HOH   SA 9 .    ? 4.302   29.749  84.413  1.00 25.26 ? 2321 HOH   B O     1 
HETATM 19002 O  O     . HOH   SA 9 .    ? 2.239   40.858  114.247 1.00 26.23 ? 2322 HOH   B O     1 
HETATM 19003 O  O     . HOH   SA 9 .    ? 7.013   28.984  52.944  1.00 27.71 ? 2323 HOH   B O     1 
HETATM 19004 O  O     . HOH   SA 9 .    ? 15.708  55.891  92.882  1.00 34.58 ? 2324 HOH   B O     1 
HETATM 19005 O  O     . HOH   SA 9 .    ? 14.859  22.789  101.512 1.00 27.80 ? 2325 HOH   B O     1 
HETATM 19006 O  O     . HOH   SA 9 .    ? 16.936  27.612  82.472  1.00 29.34 ? 2326 HOH   B O     1 
HETATM 19007 O  O     . HOH   SA 9 .    ? -1.618  -8.924  108.262 1.00 31.42 ? 2327 HOH   B O     1 
HETATM 19008 O  O     . HOH   SA 9 .    ? 22.725  46.426  76.651  1.00 34.72 ? 2328 HOH   B O     1 
HETATM 19009 O  O     . HOH   SA 9 .    ? -7.458  30.371  75.582  1.00 26.12 ? 2329 HOH   B O     1 
HETATM 19010 O  O     . HOH   SA 9 .    ? 1.072   39.119  108.146 1.00 28.11 ? 2330 HOH   B O     1 
HETATM 19011 O  O     . HOH   SA 9 .    ? -2.681  31.706  63.241  1.00 25.85 ? 2331 HOH   B O     1 
HETATM 19012 O  O     . HOH   SA 9 .    ? 1.376   -0.511  92.236  1.00 30.76 ? 2332 HOH   B O     1 
HETATM 19013 O  O     . HOH   SA 9 .    ? -2.631  -1.976  94.227  1.00 32.72 ? 2333 HOH   B O     1 
HETATM 19014 O  O     . HOH   SA 9 .    ? 2.770   30.919  79.871  1.00 19.58 ? 2334 HOH   B O     1 
HETATM 19015 O  O     . HOH   SA 9 .    ? 31.005  34.549  84.680  1.00 33.32 ? 2335 HOH   B O     1 
HETATM 19016 O  O     . HOH   SA 9 .    ? -8.493  24.696  76.796  1.00 39.90 ? 2336 HOH   B O     1 
HETATM 19017 O  O     . HOH   SA 9 .    ? 19.167  15.129  104.871 1.00 38.08 ? 2337 HOH   B O     1 
HETATM 19018 O  O     . HOH   SA 9 .    ? 9.635   37.715  131.104 1.00 40.58 ? 2338 HOH   B O     1 
HETATM 19019 O  O     . HOH   SA 9 .    ? 23.579  53.096  70.422  1.00 34.08 ? 2339 HOH   B O     1 
HETATM 19020 O  O     . HOH   SA 9 .    ? -3.776  25.149  69.990  1.00 38.59 ? 2340 HOH   B O     1 
HETATM 19021 O  O     . HOH   SA 9 .    ? -5.180  40.306  72.115  1.00 28.55 ? 2341 HOH   B O     1 
HETATM 19022 O  O     . HOH   SA 9 .    ? 22.800  23.492  84.396  1.00 21.20 ? 2342 HOH   B O     1 
HETATM 19023 O  O     . HOH   SA 9 .    ? 22.082  53.492  67.110  1.00 30.11 ? 2343 HOH   B O     1 
HETATM 19024 O  O     . HOH   SA 9 .    ? 12.484  13.324  110.177 1.00 32.31 ? 2344 HOH   B O     1 
HETATM 19025 O  O     . HOH   SA 9 .    ? -6.791  15.984  81.345  1.00 36.18 ? 2345 HOH   B O     1 
HETATM 19026 O  O     . HOH   SA 9 .    ? -0.363  24.257  73.856  1.00 21.12 ? 2346 HOH   B O     1 
HETATM 19027 O  O     . HOH   SA 9 .    ? 11.970  12.542  121.123 1.00 28.28 ? 2347 HOH   B O     1 
HETATM 19028 O  O     . HOH   SA 9 .    ? 6.094   48.373  110.395 1.00 38.09 ? 2348 HOH   B O     1 
HETATM 19029 O  O     . HOH   SA 9 .    ? 36.857  27.816  93.300  1.00 36.40 ? 2349 HOH   B O     1 
HETATM 19030 O  O     . HOH   SA 9 .    ? 17.368  49.342  59.215  1.00 24.97 ? 2350 HOH   B O     1 
HETATM 19031 O  O     . HOH   SA 9 .    ? 27.001  42.408  49.397  1.00 43.53 ? 2351 HOH   B O     1 
HETATM 19032 O  O     . HOH   SA 9 .    ? 25.931  45.604  107.309 1.00 42.42 ? 2352 HOH   B O     1 
HETATM 19033 O  O     . HOH   SA 9 .    ? 20.792  27.756  70.577  1.00 17.94 ? 2353 HOH   B O     1 
HETATM 19034 O  O     . HOH   SA 9 .    ? -13.414 12.865  93.632  1.00 22.20 ? 2354 HOH   B O     1 
HETATM 19035 O  O     . HOH   SA 9 .    ? -6.320  0.748   85.871  1.00 32.59 ? 2355 HOH   B O     1 
HETATM 19036 O  O     . HOH   SA 9 .    ? 18.898  35.121  45.804  1.00 43.48 ? 2356 HOH   B O     1 
HETATM 19037 O  O     . HOH   SA 9 .    ? 11.052  38.547  95.825  1.00 25.61 ? 2357 HOH   B O     1 
HETATM 19038 O  O     . HOH   SA 9 .    ? 19.935  19.918  105.376 1.00 20.55 ? 2358 HOH   B O     1 
HETATM 19039 O  O     . HOH   SA 9 .    ? 8.498   15.390  89.949  1.00 28.73 ? 2359 HOH   B O     1 
HETATM 19040 O  O     . HOH   SA 9 .    ? -4.415  11.149  100.050 1.00 20.17 ? 2360 HOH   B O     1 
HETATM 19041 O  O     . HOH   SA 9 .    ? 5.006   22.444  83.450  1.00 23.58 ? 2361 HOH   B O     1 
HETATM 19042 O  O     . HOH   SA 9 .    ? -1.740  3.105   125.451 1.00 30.83 ? 2362 HOH   B O     1 
HETATM 19043 O  O     . HOH   SA 9 .    ? 12.738  6.362   84.122  1.00 23.76 ? 2363 HOH   B O     1 
HETATM 19044 O  O     . HOH   SA 9 .    ? 27.149  35.437  90.853  1.00 24.35 ? 2364 HOH   B O     1 
HETATM 19045 O  O     . HOH   SA 9 .    ? -0.939  -2.391  118.578 1.00 36.94 ? 2365 HOH   B O     1 
HETATM 19046 O  O     . HOH   SA 9 .    ? 1.832   6.504   91.476  1.00 21.10 ? 2366 HOH   B O     1 
HETATM 19047 O  O     . HOH   SA 9 .    ? 21.439  54.196  83.539  1.00 32.90 ? 2367 HOH   B O     1 
HETATM 19048 O  O     . HOH   SA 9 .    ? 7.978   63.028  66.200  1.00 33.57 ? 2368 HOH   B O     1 
HETATM 19049 O  O     . HOH   SA 9 .    ? -12.174 25.184  110.273 1.00 40.12 ? 2369 HOH   B O     1 
HETATM 19050 O  O     . HOH   SA 9 .    ? 1.140   31.088  74.533  1.00 21.56 ? 2370 HOH   B O     1 
HETATM 19051 O  O     . HOH   SA 9 .    ? 11.597  42.032  54.468  1.00 23.39 ? 2371 HOH   B O     1 
HETATM 19052 O  O     . HOH   SA 9 .    ? 14.110  72.620  60.936  1.00 30.35 ? 2372 HOH   B O     1 
HETATM 19053 O  O     . HOH   SA 9 .    ? 20.964  37.843  112.325 1.00 27.44 ? 2373 HOH   B O     1 
HETATM 19054 O  O     . HOH   SA 9 .    ? -5.180  51.969  75.212  1.00 22.49 ? 2374 HOH   B O     1 
HETATM 19055 O  O     . HOH   SA 9 .    ? 8.548   41.083  86.642  1.00 17.06 ? 2375 HOH   B O     1 
HETATM 19056 O  O     . HOH   SA 9 .    ? 33.770  67.783  80.679  1.00 25.00 ? 2376 HOH   B O     1 
HETATM 19057 O  O     . HOH   SA 9 .    ? -0.825  67.088  83.912  1.00 33.42 ? 2377 HOH   B O     1 
HETATM 19058 O  O     . HOH   SA 9 .    ? 11.705  18.286  94.621  1.00 35.24 ? 2378 HOH   B O     1 
HETATM 19059 O  O     . HOH   SA 9 .    ? -4.739  31.068  77.139  1.00 20.28 ? 2379 HOH   B O     1 
HETATM 19060 O  O     . HOH   SA 9 .    ? 1.422   9.668   89.220  1.00 22.83 ? 2380 HOH   B O     1 
HETATM 19061 O  O     . HOH   SA 9 .    ? 39.759  29.431  87.795  1.00 36.82 ? 2381 HOH   B O     1 
HETATM 19062 O  O     . HOH   SA 9 .    ? 9.275   4.130   80.537  1.00 26.25 ? 2382 HOH   B O     1 
HETATM 19063 O  O     . HOH   SA 9 .    ? 18.463  15.561  97.243  1.00 24.54 ? 2383 HOH   B O     1 
HETATM 19064 O  O     . HOH   SA 9 .    ? 31.792  60.347  65.172  1.00 26.52 ? 2384 HOH   B O     1 
HETATM 19065 O  O     . HOH   SA 9 .    ? 11.779  49.942  88.354  1.00 25.51 ? 2385 HOH   B O     1 
HETATM 19066 O  O     . HOH   SA 9 .    ? 5.762   7.635   93.971  1.00 26.90 ? 2386 HOH   B O     1 
HETATM 19067 O  O     . HOH   SA 9 .    ? 7.791   65.922  63.756  1.00 29.28 ? 2387 HOH   B O     1 
HETATM 19068 O  O     . HOH   SA 9 .    ? -7.836  12.789  96.786  1.00 21.05 ? 2388 HOH   B O     1 
HETATM 19069 O  O     . HOH   SA 9 .    ? 5.035   49.683  68.504  1.00 22.76 ? 2389 HOH   B O     1 
HETATM 19070 O  O     . HOH   SA 9 .    ? 15.655  10.293  89.095  1.00 22.36 ? 2390 HOH   B O     1 
HETATM 19071 O  O     . HOH   SA 9 .    ? 22.539  54.559  92.866  1.00 33.32 ? 2391 HOH   B O     1 
HETATM 19072 O  O     . HOH   SA 9 .    ? 0.809   31.021  56.794  1.00 28.92 ? 2392 HOH   B O     1 
HETATM 19073 O  O     . HOH   SA 9 .    ? -8.659  24.393  100.569 1.00 21.09 ? 2393 HOH   B O     1 
HETATM 19074 O  O     . HOH   SA 9 .    ? 18.154  24.265  110.146 1.00 28.87 ? 2394 HOH   B O     1 
HETATM 19075 O  O     . HOH   SA 9 .    ? -5.321  55.334  78.584  1.00 28.31 ? 2395 HOH   B O     1 
HETATM 19076 O  O     . HOH   SA 9 .    ? -13.453 12.083  90.816  1.00 20.86 ? 2396 HOH   B O     1 
HETATM 19077 O  O     . HOH   SA 9 .    ? 0.358   -6.809  106.574 1.00 28.93 ? 2397 HOH   B O     1 
HETATM 19078 O  O     . HOH   SA 9 .    ? 22.327  12.320  70.881  1.00 33.24 ? 2398 HOH   B O     1 
HETATM 19079 O  O     . HOH   SA 9 .    ? 10.856  29.739  94.113  1.00 24.94 ? 2399 HOH   B O     1 
HETATM 19080 O  O     . HOH   SA 9 .    ? -4.461  38.175  93.143  1.00 38.83 ? 2400 HOH   B O     1 
HETATM 19081 O  O     . HOH   SA 9 .    ? 26.991  21.891  74.685  1.00 25.89 ? 2401 HOH   B O     1 
HETATM 19082 O  O     . HOH   SA 9 .    ? 29.684  29.427  105.076 1.00 41.28 ? 2402 HOH   B O     1 
HETATM 19083 O  O     . HOH   SA 9 .    ? 16.711  46.760  54.221  1.00 30.56 ? 2403 HOH   B O     1 
HETATM 19084 O  O     . HOH   SA 9 .    ? -11.797 7.847   126.797 1.00 43.09 ? 2404 HOH   B O     1 
HETATM 19085 O  O     . HOH   SA 9 .    ? -16.192 25.842  106.494 1.00 32.56 ? 2405 HOH   B O     1 
HETATM 19086 O  O     . HOH   SA 9 .    ? 30.742  40.838  56.899  1.00 29.52 ? 2406 HOH   B O     1 
HETATM 19087 O  O     . HOH   SA 9 .    ? 14.940  17.139  91.656  1.00 25.91 ? 2407 HOH   B O     1 
HETATM 19088 O  O     . HOH   SA 9 .    ? 3.750   34.051  92.651  1.00 19.91 ? 2408 HOH   B O     1 
HETATM 19089 O  O     . HOH   SA 9 .    ? 27.093  49.129  94.428  1.00 39.01 ? 2409 HOH   B O     1 
HETATM 19090 O  O     . HOH   SA 9 .    ? 7.363   37.903  102.556 1.00 30.24 ? 2410 HOH   B O     1 
HETATM 19091 O  O     . HOH   SA 9 .    ? -1.222  32.987  68.851  1.00 18.14 ? 2411 HOH   B O     1 
HETATM 19092 O  O     . HOH   SA 9 .    ? 0.287   12.685  93.321  1.00 17.88 ? 2412 HOH   B O     1 
HETATM 19093 O  O     . HOH   SA 9 .    ? 17.605  28.890  110.718 1.00 32.68 ? 2413 HOH   B O     1 
HETATM 19094 O  O     . HOH   SA 9 .    ? 12.305  77.851  64.498  1.00 39.05 ? 2414 HOH   B O     1 
HETATM 19095 O  O     . HOH   SA 9 .    ? 28.335  13.659  85.462  1.00 30.09 ? 2415 HOH   B O     1 
HETATM 19096 O  O     . HOH   SA 9 .    ? 30.578  50.435  71.405  1.00 27.48 ? 2416 HOH   B O     1 
HETATM 19097 O  O     . HOH   SA 9 .    ? -10.176 32.098  80.040  1.00 34.92 ? 2417 HOH   B O     1 
HETATM 19098 O  O     . HOH   SA 9 .    ? 3.958   10.908  91.971  1.00 23.18 ? 2418 HOH   B O     1 
HETATM 19099 O  O     . HOH   SA 9 .    ? 7.782   57.003  87.455  1.00 33.55 ? 2419 HOH   B O     1 
HETATM 19100 O  O     . HOH   SA 9 .    ? 21.940  7.506   82.888  1.00 38.41 ? 2420 HOH   B O     1 
HETATM 19101 O  O     . HOH   SA 9 .    ? 9.853   43.999  109.806 1.00 34.51 ? 2421 HOH   B O     1 
HETATM 19102 O  O     . HOH   SA 9 .    ? 27.137  16.078  93.230  1.00 33.96 ? 2422 HOH   B O     1 
HETATM 19103 O  O     . HOH   SA 9 .    ? -21.043 15.695  82.398  1.00 30.68 ? 2423 HOH   B O     1 
HETATM 19104 O  O     . HOH   SA 9 .    ? 19.468  55.257  93.266  1.00 29.45 ? 2424 HOH   B O     1 
HETATM 19105 O  O     . HOH   SA 9 .    ? 12.173  70.858  60.636  1.00 34.09 ? 2425 HOH   B O     1 
HETATM 19106 O  O     . HOH   SA 9 .    ? 6.315   28.175  88.033  1.00 36.87 ? 2426 HOH   B O     1 
HETATM 19107 O  O     . HOH   SA 9 .    ? -7.900  2.785   92.054  1.00 23.68 ? 2427 HOH   B O     1 
HETATM 19108 O  O     . HOH   SA 9 .    ? 20.743  19.399  60.036  1.00 22.50 ? 2428 HOH   B O     1 
HETATM 19109 O  O     . HOH   SA 9 .    ? 25.645  54.112  73.661  1.00 24.09 ? 2429 HOH   B O     1 
HETATM 19110 O  O     . HOH   SA 9 .    ? 7.749   45.254  75.012  1.00 15.47 ? 2430 HOH   B O     1 
HETATM 19111 O  O     . HOH   SA 9 .    ? 2.903   12.001  93.993  1.00 22.07 ? 2431 HOH   B O     1 
HETATM 19112 O  O     . HOH   SA 9 .    ? -0.740  56.109  121.507 1.00 34.34 ? 2432 HOH   B O     1 
HETATM 19113 O  O     . HOH   SA 9 .    ? 12.303  8.067   90.061  1.00 23.81 ? 2433 HOH   B O     1 
HETATM 19114 O  O     . HOH   SA 9 .    ? 18.229  69.222  84.335  1.00 34.02 ? 2434 HOH   B O     1 
HETATM 19115 O  O     . HOH   SA 9 .    ? 14.442  27.164  81.454  1.00 31.22 ? 2435 HOH   B O     1 
HETATM 19116 O  O     . HOH   SA 9 .    ? 18.153  23.794  87.940  1.00 25.81 ? 2436 HOH   B O     1 
HETATM 19117 O  O     . HOH   SA 9 .    ? 9.281   -0.552  106.534 1.00 45.98 ? 2437 HOH   B O     1 
HETATM 19118 O  O     . HOH   SA 9 .    ? 30.144  35.792  50.288  1.00 34.66 ? 2438 HOH   B O     1 
HETATM 19119 O  O     . HOH   SA 9 .    ? 5.438   43.038  70.621  1.00 16.28 ? 2439 HOH   B O     1 
HETATM 19120 O  O     . HOH   SA 9 .    ? -22.214 20.859  88.138  1.00 32.48 ? 2440 HOH   B O     1 
HETATM 19121 O  O     . HOH   SA 9 .    ? -0.993  21.000  89.205  1.00 20.81 ? 2441 HOH   B O     1 
HETATM 19122 O  O     . HOH   SA 9 .    ? 22.902  12.174  87.345  1.00 28.94 ? 2442 HOH   B O     1 
HETATM 19123 O  O     . HOH   SA 9 .    ? 28.948  23.106  76.122  1.00 21.14 ? 2443 HOH   B O     1 
HETATM 19124 O  O     . HOH   SA 9 .    ? -5.182  -1.668  116.883 1.00 32.41 ? 2444 HOH   B O     1 
HETATM 19125 O  O     . HOH   SA 9 .    ? 42.833  34.866  84.486  1.00 39.47 ? 2445 HOH   B O     1 
HETATM 19126 O  O     . HOH   SA 9 .    ? -5.986  13.008  98.878  1.00 19.37 ? 2446 HOH   B O     1 
HETATM 19127 O  O     . HOH   SA 9 .    ? 23.391  56.356  99.080  1.00 36.69 ? 2447 HOH   B O     1 
HETATM 19128 O  O     . HOH   SA 9 .    ? 20.881  23.279  86.332  1.00 23.94 ? 2448 HOH   B O     1 
HETATM 19129 O  O     . HOH   SA 9 .    ? -0.085  18.250  91.000  1.00 25.49 ? 2449 HOH   B O     1 
HETATM 19130 O  O     . HOH   SA 9 .    ? -13.345 -5.553  111.009 1.00 40.02 ? 2450 HOH   B O     1 
HETATM 19131 O  O     . HOH   SA 9 .    ? -5.892  34.871  83.549  1.00 25.32 ? 2451 HOH   B O     1 
HETATM 19132 O  O     . HOH   SA 9 .    ? -6.419  14.630  91.178  1.00 19.13 ? 2452 HOH   B O     1 
HETATM 19133 O  O     . HOH   SA 9 .    ? 2.905   33.194  78.185  1.00 17.88 ? 2453 HOH   B O     1 
HETATM 19134 O  O     . HOH   SA 9 .    ? 21.219  47.931  56.007  1.00 32.64 ? 2454 HOH   B O     1 
HETATM 19135 O  O     . HOH   SA 9 .    ? 12.458  21.899  101.250 1.00 33.25 ? 2455 HOH   B O     1 
HETATM 19136 O  O     . HOH   SA 9 .    ? 1.597   15.436  82.040  1.00 22.01 ? 2456 HOH   B O     1 
HETATM 19137 O  O     . HOH   SA 9 .    ? -11.054 58.625  125.330 1.00 32.02 ? 2457 HOH   B O     1 
HETATM 19138 O  O     . HOH   SA 9 .    ? 29.184  31.506  70.813  1.00 29.28 ? 2458 HOH   B O     1 
HETATM 19139 O  O     . HOH   SA 9 .    ? 7.745   20.909  101.819 1.00 30.16 ? 2459 HOH   B O     1 
HETATM 19140 O  O     . HOH   SA 9 .    ? 25.362  14.020  64.758  1.00 33.22 ? 2460 HOH   B O     1 
HETATM 19141 O  O     . HOH   SA 9 .    ? -2.924  24.998  103.349 1.00 36.92 ? 2461 HOH   B O     1 
HETATM 19142 O  O     . HOH   SA 9 .    ? -5.029  10.052  114.696 1.00 25.97 ? 2462 HOH   B O     1 
HETATM 19143 O  O     . HOH   SA 9 .    ? -6.353  6.671   118.239 1.00 28.96 ? 2463 HOH   B O     1 
HETATM 19144 O  O     . HOH   SA 9 .    ? -1.575  25.620  79.642  1.00 24.46 ? 2464 HOH   B O     1 
HETATM 19145 O  O     . HOH   SA 9 .    ? 9.167   62.343  85.108  1.00 25.05 ? 2465 HOH   B O     1 
HETATM 19146 O  O     . HOH   SA 9 .    ? 5.450   3.741   92.676  1.00 25.94 ? 2466 HOH   B O     1 
HETATM 19147 O  O     . HOH   SA 9 .    ? 19.839  19.392  65.809  1.00 18.48 ? 2467 HOH   B O     1 
HETATM 19148 O  O     . HOH   SA 9 .    ? -1.234  5.779   91.751  1.00 20.96 ? 2468 HOH   B O     1 
HETATM 19149 O  O     . HOH   SA 9 .    ? -10.247 2.123   90.947  1.00 26.49 ? 2469 HOH   B O     1 
HETATM 19150 O  O     . HOH   SA 9 .    ? 44.250  37.063  88.093  1.00 37.56 ? 2470 HOH   B O     1 
HETATM 19151 O  O     . HOH   SA 9 .    ? 1.751   20.997  89.308  1.00 25.24 ? 2471 HOH   B O     1 
HETATM 19152 O  O     . HOH   SA 9 .    ? -0.908  60.985  77.081  1.00 24.30 ? 2472 HOH   B O     1 
HETATM 19153 O  O     . HOH   SA 9 .    ? -4.221  54.153  130.706 1.00 34.07 ? 2473 HOH   B O     1 
HETATM 19154 O  O     . HOH   SA 9 .    ? 31.039  21.667  79.462  1.00 22.44 ? 2474 HOH   B O     1 
HETATM 19155 O  O     . HOH   SA 9 .    ? 0.194   19.799  93.588  1.00 20.77 ? 2475 HOH   B O     1 
HETATM 19156 O  O     . HOH   SA 9 .    ? -14.268 7.546   120.062 1.00 38.45 ? 2476 HOH   B O     1 
HETATM 19157 O  O     . HOH   SA 9 .    ? 27.215  59.324  78.346  1.00 25.76 ? 2477 HOH   B O     1 
HETATM 19158 O  O     . HOH   SA 9 .    ? -9.589  6.279   86.729  1.00 25.36 ? 2478 HOH   B O     1 
HETATM 19159 O  O     . HOH   SA 9 .    ? 18.560  67.155  58.300  1.00 32.94 ? 2479 HOH   B O     1 
HETATM 19160 O  O     . HOH   SA 9 .    ? 10.095  18.979  100.776 1.00 29.53 ? 2480 HOH   B O     1 
HETATM 19161 O  O     . HOH   SA 9 .    ? 6.652   -3.725  103.946 1.00 32.94 ? 2481 HOH   B O     1 
HETATM 19162 O  O     . HOH   SA 9 .    ? 30.932  42.960  63.220  1.00 31.20 ? 2482 HOH   B O     1 
HETATM 19163 O  O     . HOH   SA 9 .    ? 15.185  7.204   68.466  1.00 38.52 ? 2483 HOH   B O     1 
HETATM 19164 O  O     . HOH   SA 9 .    ? 27.595  19.113  100.690 1.00 40.96 ? 2484 HOH   B O     1 
HETATM 19165 O  O     . HOH   SA 9 .    ? 10.390  2.885   116.978 1.00 28.41 ? 2485 HOH   B O     1 
HETATM 19166 O  O     . HOH   SA 9 .    ? 18.545  23.476  84.487  1.00 26.02 ? 2486 HOH   B O     1 
HETATM 19167 O  O     . HOH   SA 9 .    ? -11.076 20.919  87.627  1.00 26.74 ? 2487 HOH   B O     1 
HETATM 19168 O  O     . HOH   SA 9 .    ? 19.302  8.410   83.640  1.00 26.14 ? 2488 HOH   B O     1 
HETATM 19169 O  O     . HOH   SA 9 .    ? -5.734  40.595  62.426  1.00 36.24 ? 2489 HOH   B O     1 
HETATM 19170 O  O     . HOH   SA 9 .    ? 28.240  31.779  73.090  1.00 30.26 ? 2490 HOH   B O     1 
HETATM 19171 O  O     . HOH   SA 9 .    ? 33.528  26.549  58.564  1.00 30.16 ? 2491 HOH   B O     1 
HETATM 19172 O  O     . HOH   SA 9 .    ? 28.473  25.759  67.163  1.00 18.73 ? 2492 HOH   B O     1 
HETATM 19173 O  O     . HOH   SA 9 .    ? 27.257  23.244  88.275  1.00 21.00 ? 2493 HOH   B O     1 
HETATM 19174 O  O     . HOH   SA 9 .    ? 31.993  38.838  76.385  1.00 36.62 ? 2494 HOH   B O     1 
HETATM 19175 O  O     . HOH   SA 9 .    ? 6.090   15.529  94.300  1.00 20.85 ? 2495 HOH   B O     1 
HETATM 19176 O  O     . HOH   SA 9 .    ? 0.464   20.550  69.482  1.00 25.88 ? 2496 HOH   B O     1 
HETATM 19177 O  O     . HOH   SA 9 .    ? 4.806   78.019  80.265  1.00 30.55 ? 2497 HOH   B O     1 
HETATM 19178 O  O     . HOH   SA 9 .    ? 19.032  31.016  88.280  1.00 23.10 ? 2498 HOH   B O     1 
HETATM 19179 O  O     . HOH   SA 9 .    ? 35.683  25.808  77.564  1.00 25.24 ? 2499 HOH   B O     1 
HETATM 19180 O  O     . HOH   SA 9 .    ? 24.722  16.402  94.857  1.00 28.55 ? 2500 HOH   B O     1 
HETATM 19181 O  O     . HOH   SA 9 .    ? 5.073   58.115  68.864  1.00 25.54 ? 2501 HOH   B O     1 
HETATM 19182 O  O     . HOH   SA 9 .    ? 13.659  18.801  86.717  1.00 27.25 ? 2502 HOH   B O     1 
HETATM 19183 O  O     . HOH   SA 9 .    ? -1.238  55.861  72.166  1.00 30.84 ? 2503 HOH   B O     1 
HETATM 19184 O  O     . HOH   SA 9 .    ? -20.942 5.744   90.390  1.00 39.01 ? 2504 HOH   B O     1 
HETATM 19185 O  O     . HOH   SA 9 .    ? -5.412  46.853  83.789  1.00 25.33 ? 2505 HOH   B O     1 
HETATM 19186 O  O     . HOH   SA 9 .    ? 23.493  12.724  67.541  1.00 26.35 ? 2506 HOH   B O     1 
HETATM 19187 O  O     . HOH   SA 9 .    ? -5.579  39.552  106.392 1.00 34.46 ? 2507 HOH   B O     1 
HETATM 19188 O  O     . HOH   SA 9 .    ? -14.421 6.454   117.347 1.00 31.69 ? 2508 HOH   B O     1 
HETATM 19189 O  O     . HOH   SA 9 .    ? -6.457  9.489   81.773  1.00 34.43 ? 2509 HOH   B O     1 
HETATM 19190 O  O     . HOH   SA 9 .    ? 4.840   47.834  86.878  1.00 20.03 ? 2510 HOH   B O     1 
HETATM 19191 O  O     . HOH   SA 9 .    ? 33.177  45.851  74.436  1.00 33.13 ? 2511 HOH   B O     1 
HETATM 19192 O  O     . HOH   SA 9 .    ? -3.665  30.148  66.520  1.00 35.98 ? 2512 HOH   B O     1 
HETATM 19193 O  O     . HOH   SA 9 .    ? 2.074   30.956  95.593  1.00 21.61 ? 2513 HOH   B O     1 
HETATM 19194 O  O     . HOH   SA 9 .    ? 8.225   32.173  93.282  1.00 26.59 ? 2514 HOH   B O     1 
HETATM 19195 O  O     . HOH   SA 9 .    ? 17.348  34.802  55.733  1.00 18.27 ? 2515 HOH   B O     1 
HETATM 19196 O  O     . HOH   SA 9 .    ? -8.406  -5.291  106.529 1.00 33.84 ? 2516 HOH   B O     1 
HETATM 19197 O  O     . HOH   SA 9 .    ? 16.629  22.147  99.554  1.00 28.02 ? 2517 HOH   B O     1 
HETATM 19198 O  O     . HOH   SA 9 .    ? 0.002   40.458  77.493  1.00 22.40 ? 2518 HOH   B O     1 
HETATM 19199 O  O     . HOH   SA 9 .    ? 12.106  21.394  58.425  1.00 17.96 ? 2519 HOH   B O     1 
HETATM 19200 O  O     . HOH   SA 9 .    ? -15.243 47.467  113.760 1.00 33.18 ? 2520 HOH   B O     1 
HETATM 19201 O  O     . HOH   SA 9 .    ? -5.472  12.910  84.036  1.00 30.76 ? 2521 HOH   B O     1 
HETATM 19202 O  O     . HOH   SA 9 .    ? 2.543   63.659  78.097  1.00 20.66 ? 2522 HOH   B O     1 
HETATM 19203 O  O     . HOH   SA 9 .    ? 26.570  27.713  66.617  1.00 20.83 ? 2523 HOH   B O     1 
HETATM 19204 O  O     . HOH   SA 9 .    ? 0.327   48.000  76.227  1.00 21.19 ? 2524 HOH   B O     1 
HETATM 19205 O  O     . HOH   SA 9 .    ? 29.698  60.634  58.919  1.00 30.85 ? 2525 HOH   B O     1 
HETATM 19206 O  O     . HOH   SA 9 .    ? 4.876   47.087  69.020  1.00 17.60 ? 2526 HOH   B O     1 
HETATM 19207 O  O     . HOH   SA 9 .    ? 23.542  33.094  91.325  1.00 19.53 ? 2527 HOH   B O     1 
HETATM 19208 O  O     . HOH   SA 9 .    ? 20.305  52.738  68.985  1.00 31.26 ? 2528 HOH   B O     1 
HETATM 19209 O  O     . HOH   SA 9 .    ? 26.545  40.274  52.761  1.00 28.33 ? 2529 HOH   B O     1 
HETATM 19210 O  O     . HOH   SA 9 .    ? 3.248   44.759  58.292  1.00 33.07 ? 2530 HOH   B O     1 
HETATM 19211 O  O     . HOH   SA 9 .    ? -26.687 14.619  100.078 1.00 33.65 ? 2531 HOH   B O     1 
HETATM 19212 O  O     . HOH   SA 9 .    ? -0.990  51.349  64.695  1.00 21.41 ? 2532 HOH   B O     1 
HETATM 19213 O  O     . HOH   SA 9 .    ? -4.232  2.362   123.650 1.00 31.73 ? 2533 HOH   B O     1 
HETATM 19214 O  O     . HOH   SA 9 .    ? 0.556   27.316  94.494  1.00 23.49 ? 2534 HOH   B O     1 
HETATM 19215 O  O     . HOH   SA 9 .    ? 19.619  16.415  63.179  1.00 20.79 ? 2535 HOH   B O     1 
HETATM 19216 O  O     . HOH   SA 9 .    ? 12.550  37.704  107.628 1.00 26.05 ? 2536 HOH   B O     1 
HETATM 19217 O  O     . HOH   SA 9 .    ? 19.870  33.114  67.003  1.00 18.72 ? 2537 HOH   B O     1 
HETATM 19218 O  O     . HOH   SA 9 .    ? 13.159  48.551  82.071  1.00 32.92 ? 2538 HOH   B O     1 
HETATM 19219 O  O     . HOH   SA 9 .    ? 19.126  46.063  53.987  1.00 30.34 ? 2539 HOH   B O     1 
HETATM 19220 O  O     . HOH   SA 9 .    ? 37.737  31.138  81.592  1.00 34.66 ? 2540 HOH   B O     1 
HETATM 19221 O  O     . HOH   SA 9 .    ? -4.872  16.740  96.588  1.00 17.75 ? 2541 HOH   B O     1 
HETATM 19222 O  O     . HOH   SA 9 .    ? 1.531   49.633  89.046  1.00 40.01 ? 2542 HOH   B O     1 
HETATM 19223 O  O     . HOH   SA 9 .    ? 15.597  4.281   98.030  1.00 33.76 ? 2543 HOH   B O     1 
HETATM 19224 O  O     . HOH   SA 9 .    ? -6.980  28.327  73.955  1.00 30.12 ? 2544 HOH   B O     1 
HETATM 19225 O  O     . HOH   SA 9 .    ? 11.799  26.445  101.651 1.00 35.37 ? 2545 HOH   B O     1 
HETATM 19226 O  O     . HOH   SA 9 .    ? 23.579  52.126  83.524  1.00 34.34 ? 2546 HOH   B O     1 
HETATM 19227 O  O     . HOH   SA 9 .    ? 15.740  49.289  57.152  1.00 24.11 ? 2547 HOH   B O     1 
HETATM 19228 O  O     . HOH   SA 9 .    ? 8.668   35.827  102.624 1.00 34.64 ? 2548 HOH   B O     1 
HETATM 19229 O  O     . HOH   SA 9 .    ? -0.052  73.652  77.448  1.00 29.98 ? 2549 HOH   B O     1 
HETATM 19230 O  O     . HOH   SA 9 .    ? 33.230  46.524  66.902  1.00 32.90 ? 2550 HOH   B O     1 
HETATM 19231 O  O     . HOH   SA 9 .    ? 9.482   29.428  98.064  1.00 35.89 ? 2551 HOH   B O     1 
HETATM 19232 O  O     . HOH   SA 9 .    ? 10.060  71.508  61.663  1.00 36.74 ? 2552 HOH   B O     1 
HETATM 19233 O  O     . HOH   SA 9 .    ? -16.395 0.168   98.962  1.00 31.04 ? 2553 HOH   B O     1 
HETATM 19234 O  O     . HOH   SA 9 .    ? 17.315  55.046  97.125  1.00 30.46 ? 2554 HOH   B O     1 
HETATM 19235 O  O     . HOH   SA 9 .    ? -1.896  -6.857  110.386 1.00 29.74 ? 2555 HOH   B O     1 
HETATM 19236 O  O     . HOH   SA 9 .    ? -24.991 17.127  82.032  1.00 31.61 ? 2556 HOH   B O     1 
HETATM 19237 O  O     . HOH   SA 9 .    ? -9.057  1.027   112.292 1.00 33.66 ? 2557 HOH   B O     1 
HETATM 19238 O  O     . HOH   SA 9 .    ? 3.546   56.710  62.140  1.00 43.78 ? 2558 HOH   B O     1 
HETATM 19239 O  O     . HOH   SA 9 .    ? 18.781  13.740  73.936  1.00 26.80 ? 2559 HOH   B O     1 
HETATM 19240 O  O     . HOH   SA 9 .    ? 9.188   6.365   84.660  1.00 23.35 ? 2560 HOH   B O     1 
HETATM 19241 O  O     . HOH   SA 9 .    ? 2.718   49.278  75.878  1.00 19.77 ? 2561 HOH   B O     1 
HETATM 19242 O  O     . HOH   SA 9 .    ? 15.182  21.769  88.265  1.00 35.78 ? 2562 HOH   B O     1 
HETATM 19243 O  O     . HOH   SA 9 .    ? 31.248  29.486  77.347  1.00 33.24 ? 2563 HOH   B O     1 
HETATM 19244 O  O     . HOH   SA 9 .    ? -16.689 16.798  131.049 1.00 42.13 ? 2564 HOH   B O     1 
HETATM 19245 O  O     . HOH   SA 9 .    ? 3.161   45.337  67.598  1.00 18.55 ? 2565 HOH   B O     1 
HETATM 19246 O  O     . HOH   SA 9 .    ? 27.325  18.665  61.330  1.00 25.43 ? 2566 HOH   B O     1 
HETATM 19247 O  O     . HOH   SA 9 .    ? -5.425  23.408  80.297  1.00 24.08 ? 2567 HOH   B O     1 
HETATM 19248 O  O     . HOH   SA 9 .    ? 1.687   57.409  87.642  1.00 35.44 ? 2568 HOH   B O     1 
HETATM 19249 O  O     . HOH   SA 9 .    ? 18.874  35.748  112.692 1.00 31.49 ? 2569 HOH   B O     1 
HETATM 19250 O  O     . HOH   SA 9 .    ? -25.008 10.790  87.219  1.00 38.77 ? 2570 HOH   B O     1 
HETATM 19251 O  O     . HOH   SA 9 .    ? 6.604   32.298  78.944  1.00 20.44 ? 2571 HOH   B O     1 
HETATM 19252 O  O     . HOH   SA 9 .    ? 16.689  44.566  76.061  1.00 25.77 ? 2572 HOH   B O     1 
HETATM 19253 O  O     . HOH   SA 9 .    ? 12.253  29.685  82.633  1.00 36.39 ? 2573 HOH   B O     1 
HETATM 19254 O  O     . HOH   SA 9 .    ? 8.016   58.261  85.283  1.00 25.74 ? 2574 HOH   B O     1 
HETATM 19255 O  O     . HOH   SA 9 .    ? 22.459  26.119  79.145  1.00 25.49 ? 2575 HOH   B O     1 
HETATM 19256 O  O     . HOH   SA 9 .    ? 16.041  38.439  74.375  1.00 21.13 ? 2576 HOH   B O     1 
HETATM 19257 O  O     . HOH   SA 9 .    ? 18.659  48.244  89.829  1.00 25.74 ? 2577 HOH   B O     1 
HETATM 19258 O  O     . HOH   SA 9 .    ? 2.115   20.581  92.131  1.00 30.11 ? 2578 HOH   B O     1 
HETATM 19259 O  O     . HOH   SA 9 .    ? -7.330  24.541  124.889 1.00 40.61 ? 2579 HOH   B O     1 
HETATM 19260 O  O     . HOH   SA 9 .    ? -2.850  40.100  57.648  1.00 24.67 ? 2580 HOH   B O     1 
HETATM 19261 O  O     . HOH   SA 9 .    ? 3.035   6.061   79.858  1.00 30.64 ? 2581 HOH   B O     1 
HETATM 19262 O  O     . HOH   SA 9 .    ? 24.905  51.449  66.735  1.00 25.91 ? 2582 HOH   B O     1 
HETATM 19263 O  O     . HOH   SA 9 .    ? 19.552  29.023  81.910  1.00 24.78 ? 2583 HOH   B O     1 
HETATM 19264 O  O     . HOH   SA 9 .    ? -9.294  45.835  130.701 1.00 36.14 ? 2584 HOH   B O     1 
HETATM 19265 O  O     . HOH   SA 9 .    ? 14.796  42.840  74.934  1.00 25.25 ? 2585 HOH   B O     1 
HETATM 19266 O  O     . HOH   SA 9 .    ? 4.910   56.642  74.825  1.00 19.74 ? 2586 HOH   B O     1 
HETATM 19267 O  O     . HOH   SA 9 .    ? 18.920  62.356  57.210  1.00 31.18 ? 2587 HOH   B O     1 
HETATM 19268 O  O     . HOH   SA 9 .    ? 16.533  14.490  106.543 1.00 30.49 ? 2588 HOH   B O     1 
HETATM 19269 O  O     . HOH   SA 9 .    ? -3.286  52.686  82.243  1.00 28.39 ? 2589 HOH   B O     1 
HETATM 19270 O  O     . HOH   SA 9 .    ? -15.149 10.604  89.540  1.00 20.84 ? 2590 HOH   B O     1 
HETATM 19271 O  O     . HOH   SA 9 .    ? -2.179  18.858  105.684 1.00 32.64 ? 2591 HOH   B O     1 
HETATM 19272 O  O     . HOH   SA 9 .    ? 31.617  60.052  72.178  1.00 23.81 ? 2592 HOH   B O     1 
HETATM 19273 O  O     . HOH   SA 9 .    ? 26.424  13.529  90.725  1.00 37.99 ? 2593 HOH   B O     1 
HETATM 19274 O  O     . HOH   SA 9 .    ? 2.430   42.504  53.776  1.00 34.08 ? 2594 HOH   B O     1 
HETATM 19275 O  O     . HOH   SA 9 .    ? 3.245   35.785  121.240 1.00 34.63 ? 2595 HOH   B O     1 
HETATM 19276 O  O     . HOH   SA 9 .    ? 15.952  56.389  63.794  1.00 24.49 ? 2596 HOH   B O     1 
HETATM 19277 O  O     . HOH   SA 9 .    ? 3.201   31.611  98.039  1.00 29.28 ? 2597 HOH   B O     1 
HETATM 19278 O  O     . HOH   SA 9 .    ? 11.502  49.452  78.311  1.00 36.00 ? 2598 HOH   B O     1 
HETATM 19279 O  O     . HOH   SA 9 .    ? -10.770 36.378  76.284  1.00 40.57 ? 2599 HOH   B O     1 
HETATM 19280 O  O     . HOH   SA 9 .    ? 27.297  42.467  104.745 1.00 36.68 ? 2600 HOH   B O     1 
HETATM 19281 O  O     . HOH   SA 9 .    ? 25.075  24.251  81.347  1.00 18.72 ? 2601 HOH   B O     1 
HETATM 19282 O  O     . HOH   SA 9 .    ? 7.859   54.619  64.303  1.00 30.22 ? 2602 HOH   B O     1 
HETATM 19283 O  O     . HOH   SA 9 .    ? 34.214  38.033  61.244  1.00 32.05 ? 2603 HOH   B O     1 
HETATM 19284 O  O     . HOH   SA 9 .    ? -30.545 6.078   99.698  1.00 41.92 ? 2604 HOH   B O     1 
HETATM 19285 O  O     . HOH   SA 9 .    ? -2.687  11.292  103.440 1.00 21.26 ? 2605 HOH   B O     1 
HETATM 19286 O  O     . HOH   SA 9 .    ? 18.410  12.344  105.598 1.00 41.30 ? 2606 HOH   B O     1 
HETATM 19287 O  O     . HOH   SA 9 .    ? 25.413  51.146  109.238 1.00 52.57 ? 2607 HOH   B O     1 
HETATM 19288 O  O     . HOH   SA 9 .    ? 8.665   16.175  92.353  1.00 28.36 ? 2608 HOH   B O     1 
HETATM 19289 O  O     . HOH   SA 9 .    ? 10.508  33.786  109.257 1.00 30.77 ? 2609 HOH   B O     1 
HETATM 19290 O  O     . HOH   SA 9 .    ? 14.262  75.988  62.876  1.00 30.48 ? 2610 HOH   B O     1 
HETATM 19291 O  O     . HOH   SA 9 .    ? 41.000  38.390  83.123  1.00 45.65 ? 2611 HOH   B O     1 
HETATM 19292 O  O     . HOH   SA 9 .    ? 15.335  29.493  48.964  1.00 34.49 ? 2612 HOH   B O     1 
HETATM 19293 O  O     . HOH   SA 9 .    ? -3.475  46.053  106.493 1.00 28.29 ? 2613 HOH   B O     1 
HETATM 19294 O  O     . HOH   SA 9 .    ? 11.256  20.914  119.859 1.00 34.41 ? 2614 HOH   B O     1 
HETATM 19295 O  O     . HOH   SA 9 .    ? -18.372 6.209   95.445  1.00 38.47 ? 2615 HOH   B O     1 
HETATM 19296 O  O     . HOH   SA 9 .    ? -4.340  0.397   110.197 1.00 28.93 ? 2616 HOH   B O     1 
HETATM 19297 O  O     . HOH   SA 9 .    ? 8.553   37.753  79.098  1.00 21.27 ? 2617 HOH   B O     1 
HETATM 19298 O  O     . HOH   SA 9 .    ? -2.738  34.109  62.279  1.00 22.95 ? 2618 HOH   B O     1 
HETATM 19299 O  O     . HOH   SA 9 .    ? -11.315 -1.599  96.440  1.00 35.34 ? 2619 HOH   B O     1 
HETATM 19300 O  O     . HOH   SA 9 .    ? 23.284  73.226  81.426  1.00 30.53 ? 2620 HOH   B O     1 
HETATM 19301 O  O     . HOH   SA 9 .    ? 20.884  22.196  60.444  1.00 18.82 ? 2621 HOH   B O     1 
HETATM 19302 O  O     . HOH   SA 9 .    ? 7.843   66.057  68.580  1.00 35.51 ? 2622 HOH   B O     1 
HETATM 19303 O  O     . HOH   SA 9 .    ? 35.288  32.679  54.387  1.00 32.67 ? 2623 HOH   B O     1 
HETATM 19304 O  O     . HOH   SA 9 .    ? -6.598  44.395  73.483  1.00 29.83 ? 2624 HOH   B O     1 
HETATM 19305 O  O     . HOH   SA 9 .    ? 13.459  57.944  93.661  1.00 42.19 ? 2625 HOH   B O     1 
HETATM 19306 O  O     . HOH   SA 9 .    ? 30.725  41.755  79.187  1.00 37.21 ? 2626 HOH   B O     1 
HETATM 19307 O  O     . HOH   SA 9 .    ? 14.627  76.184  86.379  1.00 40.08 ? 2627 HOH   B O     1 
HETATM 19308 O  O     . HOH   SA 9 .    ? -0.365  -7.433  99.045  1.00 35.68 ? 2628 HOH   B O     1 
HETATM 19309 O  O     . HOH   SA 9 .    ? 29.264  65.622  62.438  1.00 31.22 ? 2629 HOH   B O     1 
HETATM 19310 O  O     . HOH   SA 9 .    ? 34.170  22.994  77.735  1.00 22.99 ? 2630 HOH   B O     1 
HETATM 19311 O  O     . HOH   SA 9 .    ? -3.641  30.947  94.704  1.00 31.25 ? 2631 HOH   B O     1 
HETATM 19312 O  O     . HOH   SA 9 .    ? -0.685  13.937  100.305 1.00 19.62 ? 2632 HOH   B O     1 
HETATM 19313 O  O     . HOH   SA 9 .    ? 26.565  13.229  87.590  1.00 30.10 ? 2633 HOH   B O     1 
HETATM 19314 O  O     . HOH   SA 9 .    ? 4.687   -3.395  94.892  1.00 40.89 ? 2634 HOH   B O     1 
HETATM 19315 O  O     . HOH   SA 9 .    ? 19.454  54.705  104.030 1.00 30.61 ? 2635 HOH   B O     1 
HETATM 19316 O  O     . HOH   SA 9 .    ? -1.768  37.107  87.333  1.00 23.71 ? 2636 HOH   B O     1 
HETATM 19317 O  O     . HOH   SA 9 .    ? -7.190  13.488  94.184  1.00 20.94 ? 2637 HOH   B O     1 
HETATM 19318 O  O     . HOH   SA 9 .    ? -9.779  18.677  130.768 1.00 32.58 ? 2638 HOH   B O     1 
HETATM 19319 O  O     . HOH   SA 9 .    ? 29.079  24.576  50.550  1.00 40.55 ? 2639 HOH   B O     1 
HETATM 19320 O  O     . HOH   SA 9 .    ? -2.293  30.928  70.374  1.00 19.37 ? 2640 HOH   B O     1 
HETATM 19321 O  O     . HOH   SA 9 .    ? -11.869 22.136  85.298  1.00 29.48 ? 2641 HOH   B O     1 
HETATM 19322 O  O     . HOH   SA 9 .    ? 16.377  53.786  104.805 1.00 30.65 ? 2642 HOH   B O     1 
HETATM 19323 O  O     . HOH   SA 9 .    ? 1.784   67.389  65.379  1.00 44.04 ? 2643 HOH   B O     1 
HETATM 19324 O  O     . HOH   SA 9 .    ? -9.090  40.928  69.405  1.00 41.11 ? 2644 HOH   B O     1 
HETATM 19325 O  O     . HOH   SA 9 .    ? -2.342  14.820  98.374  1.00 17.39 ? 2645 HOH   B O     1 
HETATM 19326 O  O     . HOH   SA 9 .    ? -4.633  -3.450  91.360  1.00 30.75 ? 2646 HOH   B O     1 
HETATM 19327 O  O     . HOH   SA 9 .    ? 9.467   19.515  103.213 1.00 33.39 ? 2647 HOH   B O     1 
HETATM 19328 O  O     . HOH   SA 9 .    ? -6.050  35.910  92.677  1.00 32.78 ? 2648 HOH   B O     1 
HETATM 19329 O  O     . HOH   SA 9 .    ? -1.857  58.070  74.904  1.00 16.97 ? 2649 HOH   B O     1 
HETATM 19330 O  O     . HOH   SA 9 .    ? 18.235  50.074  111.586 1.00 37.28 ? 2650 HOH   B O     1 
HETATM 19331 O  O     . HOH   SA 9 .    ? 5.153   19.263  123.656 1.00 32.23 ? 2651 HOH   B O     1 
HETATM 19332 O  O     . HOH   SA 9 .    ? 23.889  17.360  82.131  1.00 26.56 ? 2652 HOH   B O     1 
HETATM 19333 O  O     . HOH   SA 9 .    ? 17.779  34.362  68.099  1.00 18.19 ? 2653 HOH   B O     1 
HETATM 19334 O  O     . HOH   SA 9 .    ? -0.068  4.101   130.567 1.00 43.16 ? 2654 HOH   B O     1 
HETATM 19335 O  O     . HOH   SA 9 .    ? 3.660   19.919  60.142  1.00 29.17 ? 2655 HOH   B O     1 
HETATM 19336 O  O     . HOH   SA 9 .    ? 23.120  51.708  65.083  1.00 24.69 ? 2656 HOH   B O     1 
HETATM 19337 O  O     . HOH   SA 9 .    ? 18.608  53.494  75.750  1.00 30.16 ? 2657 HOH   B O     1 
HETATM 19338 O  O     . HOH   SA 9 .    ? 1.518   23.021  63.002  1.00 29.86 ? 2658 HOH   B O     1 
HETATM 19339 O  O     . HOH   SA 9 .    ? -19.581 29.100  87.638  1.00 33.64 ? 2659 HOH   B O     1 
HETATM 19340 O  O     . HOH   SA 9 .    ? -29.592 18.274  103.179 1.00 37.63 ? 2660 HOH   B O     1 
HETATM 19341 O  O     . HOH   SA 9 .    ? -7.679  25.925  103.525 1.00 42.62 ? 2661 HOH   B O     1 
HETATM 19342 O  O     . HOH   SA 9 .    ? 22.957  9.814   68.934  1.00 40.23 ? 2662 HOH   B O     1 
HETATM 19343 O  O     . HOH   SA 9 .    ? 8.153   13.993  71.178  1.00 25.27 ? 2663 HOH   B O     1 
HETATM 19344 O  O     . HOH   SA 9 .    ? 13.479  26.029  95.995  1.00 35.47 ? 2664 HOH   B O     1 
HETATM 19345 O  O     . HOH   SA 9 .    ? 25.838  75.472  76.498  1.00 33.72 ? 2665 HOH   B O     1 
HETATM 19346 O  O     . HOH   SA 9 .    ? -22.485 25.993  103.268 1.00 38.50 ? 2666 HOH   B O     1 
HETATM 19347 O  O     . HOH   SA 9 .    ? 32.922  29.134  64.087  1.00 32.47 ? 2667 HOH   B O     1 
HETATM 19348 O  O     . HOH   SA 9 .    ? 14.161  46.695  105.902 1.00 33.04 ? 2668 HOH   B O     1 
HETATM 19349 O  O     . HOH   SA 9 .    ? -7.235  10.847  112.604 1.00 23.01 ? 2669 HOH   B O     1 
HETATM 19350 O  O     . HOH   SA 9 .    ? -2.389  42.464  73.862  1.00 35.92 ? 2670 HOH   B O     1 
HETATM 19351 O  O     . HOH   SA 9 .    ? -13.953 9.806   87.078  1.00 27.84 ? 2671 HOH   B O     1 
HETATM 19352 O  O     . HOH   SA 9 .    ? 18.363  23.375  60.852  1.00 21.82 ? 2672 HOH   B O     1 
HETATM 19353 O  O     . HOH   SA 9 .    ? -19.343 24.176  112.229 1.00 37.17 ? 2673 HOH   B O     1 
HETATM 19354 O  O     . HOH   SA 9 .    ? 20.403  20.747  108.898 1.00 23.97 ? 2674 HOH   B O     1 
HETATM 19355 O  O     . HOH   SA 9 .    ? 26.282  20.716  51.734  1.00 30.48 ? 2675 HOH   B O     1 
HETATM 19356 O  O     . HOH   SA 9 .    ? 17.170  34.161  48.451  1.00 34.88 ? 2676 HOH   B O     1 
HETATM 19357 O  O     . HOH   SA 9 .    ? 2.988   23.649  58.433  1.00 30.93 ? 2677 HOH   B O     1 
HETATM 19358 O  O     . HOH   SA 9 .    ? 14.711  9.610   93.209  1.00 24.25 ? 2678 HOH   B O     1 
HETATM 19359 O  O     . HOH   SA 9 .    ? 4.904   0.712   86.347  1.00 33.53 ? 2679 HOH   B O     1 
HETATM 19360 O  O     . HOH   SA 9 .    ? 4.584   19.914  97.020  1.00 37.57 ? 2680 HOH   B O     1 
HETATM 19361 O  O     . HOH   SA 9 .    ? -4.183  53.017  79.462  1.00 34.82 ? 2681 HOH   B O     1 
HETATM 19362 O  O     . HOH   SA 9 .    ? -4.174  46.510  132.835 1.00 43.80 ? 2682 HOH   B O     1 
HETATM 19363 O  O     . HOH   SA 9 .    ? 10.190  67.320  86.461  1.00 36.67 ? 2683 HOH   B O     1 
HETATM 19364 O  O     . HOH   SA 9 .    ? 25.275  79.494  67.168  1.00 49.81 ? 2684 HOH   B O     1 
HETATM 19365 O  O     . HOH   SA 9 .    ? -1.033  37.963  75.920  1.00 29.99 ? 2685 HOH   B O     1 
HETATM 19366 O  O     . HOH   SA 9 .    ? 34.901  13.582  80.431  1.00 38.51 ? 2686 HOH   B O     1 
HETATM 19367 O  O     . HOH   SA 9 .    ? -5.618  15.789  94.053  1.00 20.11 ? 2687 HOH   B O     1 
HETATM 19368 O  O     . HOH   SA 9 .    ? 31.297  51.112  79.456  1.00 37.23 ? 2688 HOH   B O     1 
HETATM 19369 O  O     . HOH   SA 9 .    ? -16.135 22.095  82.055  1.00 32.41 ? 2689 HOH   B O     1 
HETATM 19370 O  O     . HOH   SA 9 .    ? 15.025  57.647  71.632  1.00 28.18 ? 2690 HOH   B O     1 
HETATM 19371 O  O     . HOH   SA 9 .    ? 3.040   57.200  70.943  1.00 32.07 ? 2691 HOH   B O     1 
HETATM 19372 O  O     . HOH   SA 9 .    ? 22.198  49.677  54.251  1.00 44.15 ? 2692 HOH   B O     1 
HETATM 19373 O  O     . HOH   SA 9 .    ? -5.036  37.794  85.928  1.00 31.38 ? 2693 HOH   B O     1 
HETATM 19374 O  O     . HOH   SA 9 .    ? -2.762  64.875  83.109  1.00 22.03 ? 2694 HOH   B O     1 
HETATM 19375 O  O     . HOH   SA 9 .    ? 19.395  58.815  82.237  1.00 23.78 ? 2695 HOH   B O     1 
HETATM 19376 O  O     . HOH   SA 9 .    ? 15.796  49.918  78.562  1.00 38.35 ? 2696 HOH   B O     1 
HETATM 19377 O  O     . HOH   SA 9 .    ? 10.091  53.599  65.405  1.00 28.71 ? 2697 HOH   B O     1 
HETATM 19378 O  O     . HOH   SA 9 .    ? 29.029  59.801  56.014  1.00 37.83 ? 2698 HOH   B O     1 
HETATM 19379 O  O     . HOH   SA 9 .    ? 16.471  51.580  60.561  1.00 30.24 ? 2699 HOH   B O     1 
HETATM 19380 O  O     . HOH   SA 9 .    ? -31.555 14.458  113.985 1.00 44.25 ? 2700 HOH   B O     1 
HETATM 19381 O  O     . HOH   SA 9 .    ? 27.312  38.809  104.733 1.00 36.83 ? 2701 HOH   B O     1 
HETATM 19382 O  O     . HOH   SA 9 .    ? 24.668  63.472  54.186  1.00 34.95 ? 2702 HOH   B O     1 
HETATM 19383 O  O     . HOH   SA 9 .    ? 34.560  26.174  93.220  1.00 35.51 ? 2703 HOH   B O     1 
HETATM 19384 O  O     . HOH   SA 9 .    ? -14.451 27.068  101.129 1.00 31.58 ? 2704 HOH   B O     1 
HETATM 19385 O  O     . HOH   SA 9 .    ? 12.896  29.842  50.232  1.00 25.46 ? 2705 HOH   B O     1 
HETATM 19386 O  O     . HOH   SA 9 .    ? 5.498   67.225  61.521  1.00 40.78 ? 2706 HOH   B O     1 
HETATM 19387 O  O     . HOH   SA 9 .    ? -2.047  42.828  100.102 1.00 38.49 ? 2707 HOH   B O     1 
HETATM 19388 O  O     . HOH   SA 9 .    ? 31.361  67.535  82.284  1.00 32.91 ? 2708 HOH   B O     1 
HETATM 19389 O  O     . HOH   SA 9 .    ? -4.701  9.133   131.287 1.00 45.91 ? 2709 HOH   B O     1 
HETATM 19390 O  O     . HOH   SA 9 .    ? -22.792 21.645  101.666 1.00 33.28 ? 2710 HOH   B O     1 
HETATM 19391 O  O     . HOH   SA 9 .    ? -4.418  44.813  108.181 1.00 36.34 ? 2711 HOH   B O     1 
HETATM 19392 O  O     . HOH   SA 9 .    ? 25.323  53.774  68.330  1.00 28.92 ? 2712 HOH   B O     1 
HETATM 19393 O  O     . HOH   SA 9 .    ? 5.008   18.222  90.683  1.00 31.35 ? 2713 HOH   B O     1 
HETATM 19394 O  O     . HOH   SA 9 .    ? 29.318  22.943  70.738  1.00 33.73 ? 2714 HOH   B O     1 
HETATM 19395 O  O     . HOH   SA 9 .    ? 17.815  76.935  63.286  1.00 34.02 ? 2715 HOH   B O     1 
HETATM 19396 O  O     . HOH   SA 9 .    ? 15.056  7.484   120.824 1.00 48.42 ? 2716 HOH   B O     1 
HETATM 19397 O  O     . HOH   SA 9 .    ? 29.123  31.533  103.450 1.00 39.37 ? 2717 HOH   B O     1 
HETATM 19398 O  O     . HOH   SA 9 .    ? 22.942  67.879  59.227  1.00 30.67 ? 2718 HOH   B O     1 
HETATM 19399 O  O     . HOH   SA 9 .    ? 11.574  26.346  85.749  1.00 39.64 ? 2719 HOH   B O     1 
HETATM 19400 O  O     . HOH   SA 9 .    ? 13.917  46.210  78.443  1.00 33.46 ? 2720 HOH   B O     1 
HETATM 19401 O  O     . HOH   SA 9 .    ? -2.687  23.110  79.224  1.00 24.54 ? 2721 HOH   B O     1 
HETATM 19402 O  O     . HOH   SA 9 .    ? 22.243  15.098  80.646  1.00 33.79 ? 2722 HOH   B O     1 
HETATM 19403 O  O     . HOH   SA 9 .    ? 36.288  17.163  76.480  1.00 43.46 ? 2723 HOH   B O     1 
HETATM 19404 O  O     . HOH   SA 9 .    ? -2.476  63.135  85.186  1.00 25.72 ? 2724 HOH   B O     1 
HETATM 19405 O  O     . HOH   SA 9 .    ? 31.337  10.559  95.343  1.00 44.10 ? 2725 HOH   B O     1 
HETATM 19406 O  O     . HOH   SA 9 .    ? 36.447  35.126  53.974  1.00 41.48 ? 2726 HOH   B O     1 
HETATM 19407 O  O     . HOH   SA 9 .    ? 26.807  20.582  54.145  1.00 34.19 ? 2727 HOH   B O     1 
HETATM 19408 O  O     . HOH   SA 9 .    ? 24.284  32.131  110.082 1.00 36.59 ? 2728 HOH   B O     1 
HETATM 19409 O  O     . HOH   SA 9 .    ? 4.047   37.059  107.770 1.00 49.39 ? 2729 HOH   B O     1 
HETATM 19410 O  O     . HOH   SA 9 .    ? 18.275  75.123  81.675  1.00 40.54 ? 2730 HOH   B O     1 
HETATM 19411 O  O     . HOH   SA 9 .    ? 11.487  18.928  97.458  1.00 32.88 ? 2731 HOH   B O     1 
HETATM 19412 O  O     . HOH   SA 9 .    ? -27.900 14.881  85.585  1.00 43.35 ? 2732 HOH   B O     1 
HETATM 19413 O  O     . HOH   SA 9 .    ? 1.578   46.851  98.466  1.00 34.65 ? 2733 HOH   B O     1 
HETATM 19414 O  O     . HOH   SA 9 .    ? -6.026  41.605  83.615  1.00 38.30 ? 2734 HOH   B O     1 
HETATM 19415 O  O     . HOH   SA 9 .    ? 30.886  20.115  55.616  1.00 32.02 ? 2735 HOH   B O     1 
HETATM 19416 O  O     . HOH   SA 9 .    ? 5.928   24.305  118.902 1.00 46.90 ? 2736 HOH   B O     1 
HETATM 19417 O  O     . HOH   SA 9 .    ? 35.855  13.821  90.235  1.00 44.40 ? 2737 HOH   B O     1 
HETATM 19418 O  O     . HOH   SA 9 .    ? 4.883   55.110  119.405 1.00 48.04 ? 2738 HOH   B O     1 
HETATM 19419 O  O     . HOH   SA 9 .    ? 2.450   49.111  98.741  1.00 27.82 ? 2739 HOH   B O     1 
HETATM 19420 O  O     . HOH   SA 9 .    ? -13.965 49.281  110.627 1.00 33.90 ? 2740 HOH   B O     1 
HETATM 19421 O  O     . HOH   SA 9 .    ? -6.995  55.267  82.690  1.00 39.19 ? 2741 HOH   B O     1 
HETATM 19422 O  O     . HOH   SA 9 .    ? 4.779   17.718  127.112 1.00 35.78 ? 2742 HOH   B O     1 
HETATM 19423 O  O     . HOH   SA 9 .    ? 23.586  8.384   72.856  1.00 42.51 ? 2743 HOH   B O     1 
HETATM 19424 O  O     . HOH   SA 9 .    ? -1.420  49.639  100.798 1.00 34.44 ? 2744 HOH   B O     1 
HETATM 19425 O  O     . HOH   SA 9 .    ? -4.010  27.010  99.508  1.00 28.98 ? 2745 HOH   B O     1 
HETATM 19426 O  O     . HOH   SA 9 .    ? 37.743  37.304  89.383  1.00 34.73 ? 2746 HOH   B O     1 
HETATM 19427 O  O     . HOH   SA 9 .    ? 29.643  21.372  73.079  1.00 30.81 ? 2747 HOH   B O     1 
HETATM 19428 O  O     . HOH   SA 9 .    ? -14.981 19.775  82.184  1.00 28.12 ? 2748 HOH   B O     1 
HETATM 19429 O  O     . HOH   SA 9 .    ? 35.243  7.112   81.443  1.00 45.86 ? 2749 HOH   B O     1 
HETATM 19430 O  O     . HOH   SA 9 .    ? -22.018 8.188   85.800  1.00 44.36 ? 2750 HOH   B O     1 
HETATM 19431 O  O     . HOH   SA 9 .    ? 21.843  58.516  95.337  1.00 48.01 ? 2751 HOH   B O     1 
HETATM 19432 O  O     . HOH   SA 9 .    ? 25.746  52.641  55.060  1.00 42.46 ? 2752 HOH   B O     1 
HETATM 19433 O  O     . HOH   SA 9 .    ? 29.910  20.896  76.484  1.00 31.94 ? 2753 HOH   B O     1 
HETATM 19434 O  O     . HOH   SA 9 .    ? 27.968  11.015  84.449  1.00 36.74 ? 2754 HOH   B O     1 
HETATM 19435 O  O     . HOH   SA 9 .    ? 35.352  18.230  67.718  1.00 38.80 ? 2755 HOH   B O     1 
HETATM 19436 O  O     . HOH   SA 9 .    ? 35.801  31.723  58.100  1.00 32.98 ? 2756 HOH   B O     1 
HETATM 19437 O  O     . HOH   SA 9 .    ? 4.354   34.392  134.722 1.00 45.15 ? 2757 HOH   B O     1 
HETATM 19438 O  O     . HOH   SA 9 .    ? 9.841   -5.661  107.879 1.00 47.29 ? 2758 HOH   B O     1 
HETATM 19439 O  O     . HOH   SA 9 .    ? 14.963  19.865  89.454  1.00 37.39 ? 2759 HOH   B O     1 
HETATM 19440 O  O     . HOH   SA 9 .    ? 23.399  66.023  81.673  1.00 38.69 ? 2760 HOH   B O     1 
HETATM 19441 O  O     . HOH   SA 9 .    ? 4.764   26.197  127.931 1.00 44.75 ? 2761 HOH   B O     1 
HETATM 19442 O  O     . HOH   SA 9 .    ? 9.432   31.013  88.305  1.00 33.60 ? 2762 HOH   B O     1 
HETATM 19443 O  O     . HOH   SA 9 .    ? 28.701  42.231  52.984  1.00 37.96 ? 2763 HOH   B O     1 
HETATM 19444 O  O     . HOH   SA 9 .    ? 29.532  9.084   85.674  1.00 44.32 ? 2764 HOH   B O     1 
HETATM 19445 O  O     . HOH   SA 9 .    ? 9.152   52.364  109.064 1.00 51.33 ? 2765 HOH   B O     1 
HETATM 19446 O  O     . HOH   SA 9 .    ? 25.827  33.164  75.058  1.00 27.89 ? 2766 HOH   B O     1 
HETATM 19447 O  O     . HOH   SA 9 .    ? -2.154  30.303  57.069  1.00 37.76 ? 2767 HOH   B O     1 
HETATM 19448 O  O     . HOH   SA 9 .    ? -11.325 11.684  130.243 1.00 41.18 ? 2768 HOH   B O     1 
HETATM 19449 O  O     . HOH   SA 9 .    ? 17.059  25.431  51.945  1.00 32.55 ? 2769 HOH   B O     1 
HETATM 19450 O  O     . HOH   SA 9 .    ? 8.962   -2.867  105.493 1.00 41.02 ? 2770 HOH   B O     1 
HETATM 19451 O  O     . HOH   SA 9 .    ? -24.439 3.547   111.394 1.00 42.37 ? 2771 HOH   B O     1 
HETATM 19452 O  O     . HOH   SA 9 .    ? 21.464  27.224  81.648  1.00 28.15 ? 2772 HOH   B O     1 
HETATM 19453 O  O     . HOH   SA 9 .    ? -15.280 -3.465  111.712 1.00 45.52 ? 2773 HOH   B O     1 
HETATM 19454 O  O     . HOH   SA 9 .    ? 5.613   50.543  54.384  1.00 39.52 ? 2774 HOH   B O     1 
HETATM 19455 O  O     . HOH   SA 9 .    ? 18.846  66.359  55.683  1.00 34.50 ? 2775 HOH   B O     1 
HETATM 19456 O  O     . HOH   SA 9 .    ? 10.900  10.744  122.913 1.00 32.19 ? 2776 HOH   B O     1 
HETATM 19457 O  O     . HOH   SA 9 .    ? 28.568  76.378  70.723  1.00 41.67 ? 2777 HOH   B O     1 
HETATM 19458 O  O     . HOH   SA 9 .    ? 6.355   48.633  114.187 1.00 41.25 ? 2778 HOH   B O     1 
HETATM 19459 O  O     . HOH   SA 9 .    ? -6.478  8.637   116.074 1.00 29.38 ? 2779 HOH   B O     1 
HETATM 19460 O  O     . HOH   SA 9 .    ? -4.835  51.892  101.845 1.00 41.31 ? 2780 HOH   B O     1 
HETATM 19461 O  O     . HOH   SA 9 .    ? 19.843  78.263  77.373  1.00 45.86 ? 2781 HOH   B O     1 
HETATM 19462 O  O     . HOH   SA 9 .    ? 6.348   17.936  96.085  1.00 34.15 ? 2782 HOH   B O     1 
HETATM 19463 O  O     . HOH   SA 9 .    ? 16.204  10.603  95.023  1.00 29.11 ? 2783 HOH   B O     1 
HETATM 19464 O  O     . HOH   SA 9 .    ? 8.558   15.185  62.703  1.00 32.72 ? 2784 HOH   B O     1 
HETATM 19465 O  O     . HOH   SA 9 .    ? 3.627   67.770  60.414  1.00 44.29 ? 2785 HOH   B O     1 
HETATM 19466 O  O     . HOH   SA 9 .    ? 32.492  37.631  50.260  1.00 49.53 ? 2786 HOH   B O     1 
HETATM 19467 O  O     . HOH   SA 9 .    ? -2.287  60.753  123.806 1.00 37.49 ? 2787 HOH   B O     1 
HETATM 19468 O  O     . HOH   SA 9 .    ? 4.835   61.500  68.154  1.00 40.85 ? 2788 HOH   B O     1 
HETATM 19469 O  O     . HOH   SA 9 .    ? 6.858   61.250  85.126  1.00 30.53 ? 2789 HOH   B O     1 
HETATM 19470 O  O     . HOH   SA 9 .    ? 6.528   13.790  69.081  1.00 40.37 ? 2790 HOH   B O     1 
HETATM 19471 O  O     . HOH   SA 9 .    ? 17.918  76.172  78.978  1.00 40.95 ? 2791 HOH   B O     1 
HETATM 19472 O  O     . HOH   SA 9 .    ? -5.556  7.202   113.041 1.00 37.92 ? 2792 HOH   B O     1 
HETATM 19473 O  O     . HOH   SA 9 .    ? 6.092   30.185  86.126  1.00 29.43 ? 2793 HOH   B O     1 
HETATM 19474 O  O     . HOH   SA 9 .    ? -1.142  38.165  73.232  1.00 27.16 ? 2794 HOH   B O     1 
HETATM 19475 O  O     . HOH   SA 9 .    ? 31.345  32.340  83.367  1.00 36.70 ? 2795 HOH   B O     1 
HETATM 19476 O  O     . HOH   SA 9 .    ? 7.991   -6.741  106.142 1.00 44.81 ? 2796 HOH   B O     1 
HETATM 19477 O  O     . HOH   SA 9 .    ? -2.408  30.142  96.446  1.00 34.02 ? 2797 HOH   B O     1 
HETATM 19478 O  O     . HOH   SA 9 .    ? 15.125  51.750  56.143  1.00 36.65 ? 2798 HOH   B O     1 
HETATM 19479 O  O     . HOH   SA 9 .    ? -25.023 23.005  98.172  1.00 42.32 ? 2799 HOH   B O     1 
HETATM 19480 O  O     . HOH   SA 9 .    ? 11.140  45.818  108.853 1.00 40.75 ? 2800 HOH   B O     1 
HETATM 19481 O  O     . HOH   SA 9 .    ? 23.943  23.286  106.629 1.00 37.95 ? 2801 HOH   B O     1 
HETATM 19482 O  O     . HOH   SA 9 .    ? 0.279   -1.672  94.378  1.00 36.35 ? 2802 HOH   B O     1 
HETATM 19483 O  O     . HOH   SA 9 .    ? 15.875  35.825  113.555 1.00 43.26 ? 2803 HOH   B O     1 
HETATM 19484 O  O     . HOH   SA 9 .    ? 9.087   64.421  86.746  1.00 41.44 ? 2804 HOH   B O     1 
HETATM 19485 O  O     . HOH   SA 9 .    ? -2.569  51.850  100.658 1.00 35.86 ? 2805 HOH   B O     1 
HETATM 19486 O  O     . HOH   SA 9 .    ? -22.202 4.252   95.862  1.00 45.47 ? 2806 HOH   B O     1 
HETATM 19487 O  O     . HOH   SA 9 .    ? -6.318  3.009   84.323  1.00 33.95 ? 2807 HOH   B O     1 
HETATM 19488 O  O     . HOH   SA 9 .    ? 7.317   31.092  89.689  1.00 38.32 ? 2808 HOH   B O     1 
HETATM 19489 O  O     . HOH   SA 9 .    ? 2.655   43.741  56.245  1.00 35.70 ? 2809 HOH   B O     1 
HETATM 19490 O  O     . HOH   SA 9 .    ? 21.301  18.743  57.561  1.00 31.90 ? 2810 HOH   B O     1 
HETATM 19491 O  O     . HOH   SA 9 .    ? 18.648  63.962  55.052  1.00 36.58 ? 2811 HOH   B O     1 
HETATM 19492 O  O     . HOH   SA 9 .    ? -20.556 -7.419  107.910 1.00 48.28 ? 2812 HOH   B O     1 
HETATM 19493 O  O     . HOH   SA 9 .    ? 22.286  77.965  77.917  1.00 40.94 ? 2813 HOH   B O     1 
HETATM 19494 O  O     . HOH   SA 9 .    ? 19.940  45.618  89.689  1.00 25.17 ? 2814 HOH   B O     1 
HETATM 19495 O  O     . HOH   SA 9 .    ? 17.161  26.492  109.694 1.00 35.87 ? 2815 HOH   B O     1 
HETATM 19496 O  O     . HOH   SA 9 .    ? 12.153  27.571  88.018  1.00 41.87 ? 2816 HOH   B O     1 
HETATM 19497 O  O     . HOH   SA 9 .    ? 17.681  76.450  84.082  1.00 50.44 ? 2817 HOH   B O     1 
HETATM 19498 O  O     . HOH   SA 9 .    ? 20.905  24.905  82.959  1.00 24.95 ? 2818 HOH   B O     1 
HETATM 19499 O  O     . HOH   SA 9 .    ? -34.472 26.316  112.686 1.00 46.98 ? 2819 HOH   B O     1 
HETATM 19500 O  O     . HOH   SA 9 .    ? -7.106  12.933  82.308  1.00 40.29 ? 2820 HOH   B O     1 
HETATM 19501 O  O     . HOH   SA 9 .    ? -7.208  22.509  78.269  1.00 31.66 ? 2821 HOH   B O     1 
HETATM 19502 O  O     . HOH   SA 9 .    ? -12.868 9.755   129.417 1.00 45.45 ? 2822 HOH   B O     1 
HETATM 19503 O  O     . HOH   SA 9 .    ? 33.130  58.980  67.394  1.00 30.43 ? 2823 HOH   B O     1 
HETATM 19504 O  O     . HOH   SA 9 .    ? -10.124 30.506  75.990  1.00 34.53 ? 2824 HOH   B O     1 
HETATM 19505 O  O     . HOH   SA 9 .    ? 30.307  36.124  82.779  1.00 43.51 ? 2825 HOH   B O     1 
HETATM 19506 O  O     . HOH   SA 9 .    ? -0.848  -5.036  117.785 1.00 43.05 ? 2826 HOH   B O     1 
HETATM 19507 O  O     . HOH   SA 9 .    ? 6.946   29.444  91.173  1.00 38.60 ? 2827 HOH   B O     1 
HETATM 19508 O  O     . HOH   SA 9 .    ? 21.584  18.883  110.514 1.00 39.65 ? 2828 HOH   B O     1 
HETATM 19509 O  O     . HOH   SA 9 .    ? 4.935   44.206  50.808  1.00 35.31 ? 2829 HOH   B O     1 
HETATM 19510 O  O     . HOH   SA 9 .    ? -3.209  40.082  73.990  1.00 34.66 ? 2830 HOH   B O     1 
HETATM 19511 O  O     . HOH   SA 9 .    ? 1.265   15.107  79.255  1.00 41.91 ? 2831 HOH   B O     1 
HETATM 19512 O  O     . HOH   SA 9 .    ? -2.193  62.627  68.919  1.00 42.39 ? 2832 HOH   B O     1 
HETATM 19513 O  O     . HOH   SA 9 .    ? -15.471 8.328   85.647  1.00 42.09 ? 2833 HOH   B O     1 
HETATM 19514 O  O     . HOH   SA 9 .    ? 20.485  23.250  109.560 1.00 32.26 ? 2834 HOH   B O     1 
HETATM 19515 O  O     . HOH   SA 9 .    ? 20.791  68.997  58.441  1.00 39.42 ? 2835 HOH   B O     1 
HETATM 19516 O  O     . HOH   SA 9 .    ? 4.093   30.245  93.727  1.00 34.34 ? 2836 HOH   B O     1 
HETATM 19517 O  O     . HOH   SA 9 .    ? 2.503   31.020  82.604  1.00 31.74 ? 2837 HOH   B O     1 
HETATM 19518 O  O     . HOH   SA 9 .    ? -2.780  29.781  98.733  1.00 38.56 ? 2838 HOH   B O     1 
HETATM 19519 O  O     . HOH   SA 9 .    ? -7.654  -2.522  117.196 1.00 44.26 ? 2839 HOH   B O     1 
HETATM 19520 O  O     . HOH   SA 9 .    ? -2.436  26.305  101.360 1.00 41.78 ? 2840 HOH   B O     1 
HETATM 19521 O  O     . HOH   SA 9 .    ? 13.927  25.435  100.371 1.00 32.09 ? 2841 HOH   B O     1 
HETATM 19522 O  O     . HOH   SA 9 .    ? -15.773 7.207   122.178 1.00 42.82 ? 2842 HOH   B O     1 
HETATM 19523 O  O     . HOH   SA 9 .    ? 2.671   4.050   84.486  1.00 37.93 ? 2843 HOH   B O     1 
HETATM 19524 O  O     . HOH   SA 9 .    ? 0.310   18.670  71.474  1.00 32.11 ? 2844 HOH   B O     1 
HETATM 19525 O  O     . HOH   SA 9 .    ? -4.185  64.379  69.674  1.00 46.23 ? 2845 HOH   B O     1 
HETATM 19526 O  O     . HOH   SA 9 .    ? 12.445  44.408  53.492  1.00 28.29 ? 2846 HOH   B O     1 
HETATM 19527 O  O     . HOH   SA 9 .    ? 20.215  34.329  114.633 1.00 36.19 ? 2847 HOH   B O     1 
HETATM 19528 O  O     . HOH   SA 9 .    ? -14.414 -2.671  115.376 1.00 48.06 ? 2848 HOH   B O     1 
HETATM 19529 O  O     . HOH   SA 9 .    ? 5.151   32.362  92.565  1.00 31.23 ? 2849 HOH   B O     1 
HETATM 19530 O  O     . HOH   SA 9 .    ? 10.214  15.306  67.212  1.00 35.79 ? 2850 HOH   B O     1 
HETATM 19531 O  O     . HOH   SA 9 .    ? -2.525  28.943  68.498  1.00 24.32 ? 2851 HOH   B O     1 
HETATM 19532 O  O     . HOH   SA 9 .    ? 5.494   32.482  86.954  1.00 32.44 ? 2852 HOH   B O     1 
HETATM 19533 O  O     . HOH   SA 9 .    ? 31.255  23.056  69.328  1.00 44.22 ? 2853 HOH   B O     1 
HETATM 19534 O  O     . HOH   SA 9 .    ? 0.713   4.704   85.459  1.00 33.42 ? 2854 HOH   B O     1 
HETATM 19535 O  O     . HOH   SA 9 .    ? -3.826  20.194  106.892 1.00 42.16 ? 2855 HOH   B O     1 
HETATM 19536 O  O     . HOH   SA 9 .    ? 24.473  72.081  82.904  1.00 44.06 ? 2856 HOH   B O     1 
HETATM 19537 O  O     . HOH   SA 9 .    ? 15.064  22.531  97.193  1.00 31.53 ? 2857 HOH   B O     1 
HETATM 19538 O  O     . HOH   SA 9 .    ? 32.274  21.073  75.311  1.00 43.15 ? 2858 HOH   B O     1 
HETATM 19539 O  O     . HOH   SA 9 .    ? 35.826  12.872  77.733  1.00 46.02 ? 2859 HOH   B O     1 
HETATM 19540 O  O     . HOH   SA 9 .    ? -0.536  19.042  67.962  1.00 39.72 ? 2860 HOH   B O     1 
HETATM 19541 O  O     . HOH   SA 9 .    ? 7.151   2.628   79.371  1.00 40.88 ? 2861 HOH   B O     1 
HETATM 19542 O  O     . HOH   SA 9 .    ? 5.614   45.762  53.561  1.00 35.55 ? 2862 HOH   B O     1 
HETATM 19543 O  O     . HOH   SA 9 .    ? 13.439  36.963  76.932  1.00 24.81 ? 2863 HOH   B O     1 
HETATM 19544 O  O     . HOH   SA 9 .    ? -3.832  40.853  60.424  1.00 34.81 ? 2864 HOH   B O     1 
HETATM 19545 O  O     . HOH   SA 9 .    ? 12.748  18.515  91.426  1.00 37.59 ? 2865 HOH   B O     1 
HETATM 19546 O  O     . HOH   SA 9 .    ? -7.709  39.786  72.644  1.00 39.59 ? 2866 HOH   B O     1 
HETATM 19547 O  O     . HOH   SA 9 .    ? -19.867 4.080   95.794  1.00 42.73 ? 2867 HOH   B O     1 
HETATM 19548 O  O     . HOH   SA 9 .    ? -17.551 6.953   92.695  1.00 40.61 ? 2868 HOH   B O     1 
HETATM 19549 O  O     . HOH   SA 9 .    ? 12.618  55.630  105.248 1.00 38.51 ? 2869 HOH   B O     1 
HETATM 19550 O  O     . HOH   SA 9 .    ? 10.814  1.174   106.888 1.00 36.39 ? 2870 HOH   B O     1 
HETATM 19551 O  O     . HOH   SA 9 .    ? 6.585   16.287  91.557  1.00 32.01 ? 2871 HOH   B O     1 
HETATM 19552 O  O     . HOH   SA 9 .    ? 11.912  4.422   117.928 1.00 39.45 ? 2872 HOH   B O     1 
HETATM 19553 O  O     . HOH   SA 9 .    ? 2.313   -7.168  98.189  1.00 43.91 ? 2873 HOH   B O     1 
HETATM 19554 O  O     . HOH   SA 9 .    ? 18.587  3.260   77.316  1.00 45.92 ? 2874 HOH   B O     1 
HETATM 19555 O  O     . HOH   SA 9 .    ? 29.572  31.745  81.593  1.00 28.08 ? 2875 HOH   B O     1 
HETATM 19556 O  O     . HOH   SA 9 .    ? 6.835   63.666  69.009  1.00 41.04 ? 2876 HOH   B O     1 
HETATM 19557 O  O     . HOH   SA 9 .    ? 30.988  31.063  79.044  1.00 37.30 ? 2877 HOH   B O     1 
HETATM 19558 O  O     . HOH   SA 9 .    ? 9.642   4.205   83.301  1.00 30.84 ? 2878 HOH   B O     1 
HETATM 19559 O  O     . HOH   SA 9 .    ? -2.408  41.308  77.883  1.00 35.00 ? 2879 HOH   B O     1 
HETATM 19560 O  O     . HOH   SA 9 .    ? 3.467   74.578  87.588  1.00 48.07 ? 2880 HOH   B O     1 
HETATM 19561 O  O     . HOH   SA 9 .    ? -4.337  46.435  103.242 1.00 43.56 ? 2881 HOH   B O     1 
HETATM 19562 O  O     . HOH   SA 9 .    ? 15.271  44.730  52.773  1.00 33.78 ? 2882 HOH   B O     1 
HETATM 19563 O  O     . HOH   SA 9 .    ? 1.716   44.829  97.140  1.00 39.28 ? 2883 HOH   B O     1 
HETATM 19564 O  O     . HOH   SA 9 .    ? -6.916  25.704  74.760  1.00 37.37 ? 2884 HOH   B O     1 
HETATM 19565 O  O     . HOH   SA 9 .    ? 13.124  56.233  63.117  1.00 37.35 ? 2885 HOH   B O     1 
HETATM 19566 O  O     . HOH   SA 9 .    ? 8.896   65.323  66.093  1.00 31.82 ? 2886 HOH   B O     1 
HETATM 19567 O  O     . HOH   SA 9 .    ? -8.872  42.416  72.267  1.00 35.81 ? 2887 HOH   B O     1 
HETATM 19568 O  O     . HOH   SA 9 .    ? -11.290 -4.945  113.294 1.00 42.94 ? 2888 HOH   B O     1 
HETATM 19569 O  O     . HOH   SA 9 .    ? 13.889  36.790  73.895  1.00 24.10 ? 2889 HOH   B O     1 
HETATM 19570 O  O     . HOH   SA 9 .    ? 21.814  20.030  106.889 1.00 32.28 ? 2890 HOH   B O     1 
HETATM 19571 O  O     . HOH   SA 9 .    ? 8.131   58.147  94.642  1.00 36.33 ? 2891 HOH   B O     1 
HETATM 19572 O  O     . HOH   SA 9 .    ? 5.530   50.445  112.680 1.00 45.48 ? 2892 HOH   B O     1 
HETATM 19573 O  O     . HOH   SA 9 .    ? 6.433   -4.246  101.731 1.00 35.31 ? 2893 HOH   B O     1 
HETATM 19574 O  O     . HOH   SA 9 .    ? 30.515  23.882  74.178  1.00 35.59 ? 2894 HOH   B O     1 
HETATM 19575 O  O     . HOH   SA 9 .    ? 12.676  0.841   108.466 1.00 40.90 ? 2895 HOH   B O     1 
HETATM 19576 O  O     . HOH   SA 9 .    ? 12.617  52.138  54.984  1.00 38.64 ? 2896 HOH   B O     1 
HETATM 19577 O  O     . HOH   SA 9 .    ? 33.724  19.883  53.774  1.00 32.80 ? 2897 HOH   B O     1 
HETATM 19578 O  O     . HOH   SA 9 .    ? 1.168   2.490   128.588 1.00 43.19 ? 2898 HOH   B O     1 
HETATM 19579 O  O     . HOH   SA 9 .    ? 5.683   3.350   85.319  1.00 32.00 ? 2899 HOH   B O     1 
HETATM 19580 O  O     . HOH   SA 9 .    ? 32.615  60.274  62.762  1.00 34.15 ? 2900 HOH   B O     1 
HETATM 19581 O  O     . HOH   SA 9 .    ? 34.614  26.799  56.029  1.00 35.29 ? 2901 HOH   B O     1 
HETATM 19582 O  O     . HOH   SA 9 .    ? 14.467  52.028  62.593  1.00 30.21 ? 2902 HOH   B O     1 
HETATM 19583 O  O     . HOH   SA 9 .    ? 34.717  27.555  60.975  1.00 36.70 ? 2903 HOH   B O     1 
HETATM 19584 O  O     . HOH   SA 9 .    ? 9.637   17.234  89.434  1.00 36.08 ? 2904 HOH   B O     1 
HETATM 19585 O  O     . HOH   SA 9 .    ? 4.829   64.458  86.487  1.00 33.06 ? 2905 HOH   B O     1 
HETATM 19586 O  O     . HOH   SA 9 .    ? 25.826  52.855  83.990  1.00 40.97 ? 2906 HOH   B O     1 
HETATM 19587 O  O     . HOH   SA 9 .    ? 14.279  24.879  97.893  1.00 34.15 ? 2907 HOH   B O     1 
HETATM 19588 O  O     . HOH   SA 9 .    ? 19.912  11.204  96.228  1.00 39.76 ? 2908 HOH   B O     1 
HETATM 19589 O  O     . HOH   SA 9 .    ? 8.339   53.326  112.816 1.00 47.52 ? 2909 HOH   B O     1 
HETATM 19590 O  O     . HOH   SA 9 .    ? -0.678  80.640  76.758  1.00 44.16 ? 2910 HOH   B O     1 
HETATM 19591 O  O     . HOH   SA 9 .    ? 3.454   48.311  89.166  1.00 35.61 ? 2911 HOH   B O     1 
HETATM 19592 O  O     . HOH   SA 9 .    ? -3.886  23.269  72.010  1.00 37.93 ? 2912 HOH   B O     1 
HETATM 19593 O  O     . HOH   SA 9 .    ? -9.291  0.234   86.443  1.00 44.86 ? 2913 HOH   B O     1 
HETATM 19594 O  O     . HOH   SA 9 .    ? 22.921  50.596  68.632  1.00 34.63 ? 2914 HOH   B O     1 
HETATM 19595 O  O     . HOH   SA 9 .    ? 9.475   49.423  108.874 1.00 41.95 ? 2915 HOH   B O     1 
HETATM 19596 O  O     . HOH   SA 9 .    ? -8.393  4.083   84.419  1.00 41.45 ? 2916 HOH   B O     1 
HETATM 19597 O  O     . HOH   SA 9 .    ? 2.564   22.360  60.782  1.00 37.36 ? 2917 HOH   B O     1 
HETATM 19598 O  O     . HOH   SA 9 .    ? 11.375  54.419  55.535  1.00 49.20 ? 2918 HOH   B O     1 
HETATM 19599 O  O     . HOH   SA 9 .    ? -25.361 13.106  86.300  1.00 39.72 ? 2919 HOH   B O     1 
HETATM 19600 O  O     . HOH   SA 9 .    ? -11.361 2.275   88.446  1.00 36.62 ? 2920 HOH   B O     1 
HETATM 19601 O  O     . HOH   SA 9 .    ? 18.879  79.602  65.190  1.00 46.71 ? 2921 HOH   B O     1 
HETATM 19602 O  O     . HOH   SA 9 .    ? 21.159  26.123  44.052  1.00 35.21 ? 2922 HOH   B O     1 
HETATM 19603 O  O     . HOH   SA 9 .    ? -1.664  19.274  77.780  1.00 36.56 ? 2923 HOH   B O     1 
HETATM 19604 O  O     . HOH   SA 9 .    ? 0.092   29.247  96.211  1.00 27.49 ? 2924 HOH   B O     1 
HETATM 19605 O  O     . HOH   SA 9 .    ? -11.185 47.196  76.771  1.00 38.92 ? 2925 HOH   B O     1 
HETATM 19606 O  O     . HOH   SA 9 .    ? 16.713  2.306   75.670  1.00 49.12 ? 2926 HOH   B O     1 
HETATM 19607 O  O     . HOH   SA 9 .    ? 23.118  82.686  69.162  1.00 47.41 ? 2927 HOH   B O     1 
HETATM 19608 O  O     . HOH   SA 9 .    ? -10.532 3.839   86.234  1.00 40.51 ? 2928 HOH   B O     1 
HETATM 19609 O  O     . HOH   SA 9 .    ? 24.502  76.946  78.705  1.00 46.48 ? 2929 HOH   B O     1 
HETATM 19610 O  O     . HOH   SA 9 .    ? -1.063  23.566  63.415  1.00 35.96 ? 2930 HOH   B O     1 
HETATM 19611 O  O     . HOH   SA 9 .    ? 2.220   32.454  84.658  1.00 32.50 ? 2931 HOH   B O     1 
HETATM 19612 O  O     . HOH   SA 9 .    ? -15.896 8.009   90.311  1.00 34.92 ? 2932 HOH   B O     1 
HETATM 19613 O  O     . HOH   SA 9 .    ? -23.441 14.458  82.017  1.00 36.84 ? 2933 HOH   B O     1 
HETATM 19614 O  O     . HOH   SA 9 .    ? -27.449 15.824  82.597  1.00 43.52 ? 2934 HOH   B O     1 
HETATM 19615 O  O     . HOH   SA 9 .    ? 28.357  6.898   86.402  1.00 47.84 ? 2935 HOH   B O     1 
HETATM 19616 O  O     . HOH   SA 9 .    ? 3.123   3.594   81.799  1.00 41.43 ? 2936 HOH   B O     1 
HETATM 19617 O  O     . HOH   SA 9 .    ? -4.606  23.915  74.589  1.00 34.70 ? 2937 HOH   B O     1 
HETATM 19618 O  O     . HOH   SA 9 .    ? 34.749  48.395  69.010  1.00 44.03 ? 2938 HOH   B O     1 
HETATM 19619 O  O     . HOH   SA 9 .    ? -16.083 4.334   123.246 1.00 43.14 ? 2939 HOH   B O     1 
HETATM 19620 O  O     . HOH   SA 9 .    ? 28.933  34.361  80.813  1.00 37.77 ? 2940 HOH   B O     1 
HETATM 19621 O  O     . HOH   SA 9 .    ? -26.127 24.975  96.536  1.00 41.54 ? 2941 HOH   B O     1 
HETATM 19622 O  O     . HOH   SA 9 .    ? 32.431  70.201  69.049  1.00 35.06 ? 2942 HOH   B O     1 
HETATM 19623 O  O     . HOH   SA 9 .    ? 22.908  29.741  43.663  1.00 41.62 ? 2943 HOH   B O     1 
HETATM 19624 O  O     . HOH   SA 9 .    ? -24.709 13.180  83.775  1.00 37.81 ? 2944 HOH   B O     1 
HETATM 19625 O  O     . HOH   SA 9 .    ? -9.490  -2.297  85.376  1.00 42.20 ? 2945 HOH   B O     1 
HETATM 19626 O  O     . HOH   SA 9 .    ? 7.521   2.341   83.938  1.00 33.11 ? 2946 HOH   B O     1 
HETATM 19627 O  O     . HOH   SA 9 .    ? -15.795 6.054   88.538  1.00 38.92 ? 2947 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   . ALA A 16   ? 0.6378 0.6071 0.6794 0.0607  -0.0113 -0.0512 14   ALA A N   
2     C CA  . ALA A 16   ? 0.5894 0.5597 0.6262 0.0573  -0.0086 -0.0482 14   ALA A CA  
3     C C   . ALA A 16   ? 0.5885 0.5664 0.6222 0.0558  -0.0043 -0.0454 14   ALA A C   
4     O O   . ALA A 16   ? 0.6049 0.5910 0.6379 0.0580  -0.0024 -0.0483 14   ALA A O   
5     C CB  . ALA A 16   ? 0.5676 0.5396 0.6030 0.0590  -0.0090 -0.0525 14   ALA A CB  
6     N N   . PRO A 17   ? 0.5635 0.5388 0.5953 0.0520  -0.0028 -0.0399 15   PRO A N   
7     C CA  . PRO A 17   ? 0.4745 0.4563 0.5036 0.0502  0.0010  -0.0370 15   PRO A CA  
8     C C   . PRO A 17   ? 0.4809 0.4683 0.5061 0.0499  0.0036  -0.0379 15   PRO A C   
9     O O   . PRO A 17   ? 0.4956 0.4799 0.5188 0.0490  0.0031  -0.0381 15   PRO A O   
10    C CB  . PRO A 17   ? 0.4718 0.4482 0.4999 0.0462  0.0013  -0.0314 15   PRO A CB  
11    C CG  . PRO A 17   ? 0.4908 0.4588 0.5219 0.0463  -0.0025 -0.0314 15   PRO A CG  
12    C CD  . PRO A 17   ? 0.5102 0.4768 0.5424 0.0490  -0.0046 -0.0361 15   PRO A CD  
13    N N   . ALA A 18   ? 0.4381 0.4341 0.4622 0.0506  0.0064  -0.0383 16   ALA A N   
14    C CA  . ALA A 18   ? 0.4226 0.4247 0.4428 0.0503  0.0090  -0.0388 16   ALA A CA  
15    C C   . ALA A 18   ? 0.3664 0.3651 0.3830 0.0463  0.0106  -0.0340 16   ALA A C   
16    O O   . ALA A 18   ? 0.3414 0.3376 0.3580 0.0435  0.0113  -0.0298 16   ALA A O   
17    C CB  . ALA A 18   ? 0.3607 0.3728 0.3807 0.0513  0.0119  -0.0392 16   ALA A CB  
18    N N   . PRO A 19   ? 0.3474 0.3460 0.3610 0.0459  0.0109  -0.0346 17   PRO A N   
19    C CA  . PRO A 19   ? 0.3054 0.3003 0.3159 0.0423  0.0119  -0.0303 17   PRO A CA  
20    C C   . PRO A 19   ? 0.3298 0.3291 0.3383 0.0399  0.0151  -0.0262 17   PRO A C   
21    O O   . PRO A 19   ? 0.3198 0.3268 0.3271 0.0408  0.0173  -0.0269 17   PRO A O   
22    C CB  . PRO A 19   ? 0.3478 0.3440 0.3555 0.0431  0.0119  -0.0325 17   PRO A CB  
23    C CG  . PRO A 19   ? 0.3594 0.3564 0.3697 0.0469  0.0095  -0.0381 17   PRO A CG  
24    C CD  . PRO A 19   ? 0.3675 0.3692 0.3806 0.0489  0.0100  -0.0395 17   PRO A CD  
25    N N   . PHE A 20   ? 0.2663 0.2607 0.2745 0.0368  0.0153  -0.0220 18   PHE A N   
26    C CA  . PHE A 20   ? 0.2745 0.2713 0.2809 0.0340  0.0179  -0.0179 18   PHE A CA  
27    C C   . PHE A 20   ? 0.3240 0.3259 0.3325 0.0345  0.0192  -0.0176 18   PHE A C   
28    O O   . PHE A 20   ? 0.2881 0.2932 0.2954 0.0324  0.0214  -0.0145 18   PHE A O   
29    C CB  . PHE A 20   ? 0.2565 0.2576 0.2590 0.0333  0.0201  -0.0169 18   PHE A CB  
30    C CG  . PHE A 20   ? 0.2579 0.2544 0.2581 0.0325  0.0191  -0.0168 18   PHE A CG  
31    C CD1 . PHE A 20   ? 0.2475 0.2382 0.2469 0.0296  0.0188  -0.0134 18   PHE A CD1 
32    C CD2 . PHE A 20   ? 0.2694 0.2678 0.2683 0.0346  0.0184  -0.0202 18   PHE A CD2 
33    C CE1 . PHE A 20   ? 0.2763 0.2631 0.2738 0.0289  0.0179  -0.0133 18   PHE A CE1 
34    C CE2 . PHE A 20   ? 0.2610 0.2552 0.2580 0.0338  0.0174  -0.0201 18   PHE A CE2 
35    C CZ  . PHE A 20   ? 0.2791 0.2678 0.2755 0.0310  0.0172  -0.0166 18   PHE A CZ  
36    N N   . ALA A 21   ? 0.3309 0.3337 0.3427 0.0372  0.0176  -0.0207 19   ALA A N   
37    C CA  . ALA A 21   ? 0.3521 0.3603 0.3662 0.0378  0.0187  -0.0206 19   ALA A CA  
38    C C   . ALA A 21   ? 0.3544 0.3590 0.3696 0.0350  0.0188  -0.0167 19   ALA A C   
39    O O   . ALA A 21   ? 0.3855 0.3947 0.4019 0.0344  0.0203  -0.0154 19   ALA A O   
40    C CB  . ALA A 21   ? 0.3650 0.3747 0.3827 0.0416  0.0168  -0.0251 19   ALA A CB  
41    N N   . ASP A 22   ? 0.2846 0.2815 0.2994 0.0333  0.0172  -0.0148 20   ASP A N   
42    C CA  . ASP A 22   ? 0.3526 0.3460 0.3681 0.0308  0.0172  -0.0112 20   ASP A CA  
43    C C   . ASP A 22   ? 0.3167 0.3059 0.3291 0.0277  0.0178  -0.0081 20   ASP A C   
44    O O   . ASP A 22   ? 0.2940 0.2778 0.3068 0.0260  0.0166  -0.0060 20   ASP A O   
45    C CB  . ASP A 22   ? 0.3360 0.3245 0.3547 0.0319  0.0143  -0.0120 20   ASP A CB  
46    C CG  . ASP A 22   ? 0.4973 0.4898 0.5193 0.0351  0.0135  -0.0153 20   ASP A CG  
47    O OD1 . ASP A 22   ? 0.5484 0.5468 0.5714 0.0351  0.0151  -0.0149 20   ASP A OD1 
48    O OD2 . ASP A 22   ? 0.5918 0.5819 0.6156 0.0377  0.0111  -0.0184 20   ASP A OD2 
49    N N   . PHE A 23   ? 0.2395 0.2315 0.2490 0.0271  0.0196  -0.0076 21   PHE A N   
50    C CA  . PHE A 23   ? 0.2354 0.2234 0.2421 0.0247  0.0199  -0.0052 21   PHE A CA  
51    C C   . PHE A 23   ? 0.2418 0.2277 0.2484 0.0218  0.0205  -0.0016 21   PHE A C   
52    O O   . PHE A 23   ? 0.2472 0.2277 0.2536 0.0204  0.0194  -0.0001 21   PHE A O   
53    C CB  . PHE A 23   ? 0.2301 0.2220 0.2337 0.0246  0.0217  -0.0052 21   PHE A CB  
54    C CG  . PHE A 23   ? 0.2282 0.2163 0.2291 0.0223  0.0220  -0.0027 21   PHE A CG  
55    C CD1 . PHE A 23   ? 0.2534 0.2360 0.2539 0.0223  0.0201  -0.0034 21   PHE A CD1 
56    C CD2 . PHE A 23   ? 0.2605 0.2504 0.2595 0.0202  0.0239  0.0003  21   PHE A CD2 
57    C CE1 . PHE A 23   ? 0.2715 0.2509 0.2697 0.0204  0.0203  -0.0012 21   PHE A CE1 
58    C CE2 . PHE A 23   ? 0.2621 0.2483 0.2588 0.0183  0.0239  0.0024  21   PHE A CE2 
59    C CZ  . PHE A 23   ? 0.3071 0.2883 0.3034 0.0185  0.0222  0.0015  21   PHE A CZ  
60    N N   . ALA A 24   ? 0.2559 0.2463 0.2628 0.0208  0.0224  -0.0001 22   ALA A N   
61    C CA  . ALA A 24   ? 0.2734 0.2621 0.2804 0.0181  0.0230  0.0031  22   ALA A CA  
62    C C   . ALA A 24   ? 0.2731 0.2670 0.2819 0.0177  0.0243  0.0038  22   ALA A C   
63    O O   . ALA A 24   ? 0.2446 0.2407 0.2525 0.0157  0.0260  0.0061  22   ALA A O   
64    C CB  . ALA A 24   ? 0.2611 0.2483 0.2651 0.0160  0.0240  0.0053  22   ALA A CB  
65    N N   . PRO A 25   ? 0.2951 0.2912 0.3069 0.0195  0.0236  0.0020  23   PRO A N   
66    C CA  . PRO A 25   ? 0.2847 0.2862 0.2986 0.0190  0.0248  0.0026  23   PRO A CA  
67    C C   . PRO A 25   ? 0.2558 0.2551 0.2700 0.0162  0.0250  0.0056  23   PRO A C   
68    O O   . PRO A 25   ? 0.2766 0.2705 0.2908 0.0154  0.0235  0.0064  23   PRO A O   
69    C CB  . PRO A 25   ? 0.2835 0.2860 0.3006 0.0217  0.0232  -0.0001 23   PRO A CB  
70    C CG  . PRO A 25   ? 0.3430 0.3386 0.3599 0.0223  0.0208  -0.0006 23   PRO A CG  
71    C CD  . PRO A 25   ? 0.2850 0.2779 0.2986 0.0217  0.0212  -0.0003 23   PRO A CD  
72    N N   . PRO A 26   ? 0.2564 0.2599 0.2709 0.0144  0.0268  0.0074  24   PRO A N   
73    C CA  . PRO A 26   ? 0.2637 0.2651 0.2787 0.0117  0.0269  0.0099  24   PRO A CA  
74    C C   . PRO A 26   ? 0.2504 0.2518 0.2685 0.0121  0.0256  0.0094  24   PRO A C   
75    O O   . PRO A 26   ? 0.2525 0.2567 0.2728 0.0143  0.0250  0.0073  24   PRO A O   
76    C CB  . PRO A 26   ? 0.2963 0.3029 0.3113 0.0099  0.0291  0.0117  24   PRO A CB  
77    C CG  . PRO A 26   ? 0.2887 0.3019 0.3048 0.0121  0.0300  0.0096  24   PRO A CG  
78    C CD  . PRO A 26   ? 0.2786 0.2891 0.2930 0.0147  0.0289  0.0071  24   PRO A CD  
79    N N   . VAL A 27   ? 0.2424 0.2405 0.2607 0.0100  0.0250  0.0112  25   VAL A N   
80    C CA  . VAL A 27   ? 0.2681 0.2661 0.2890 0.0102  0.0236  0.0110  25   VAL A CA  
81    C C   . VAL A 27   ? 0.2738 0.2785 0.2978 0.0105  0.0246  0.0105  25   VAL A C   
82    O O   . VAL A 27   ? 0.2845 0.2909 0.3110 0.0122  0.0235  0.0091  25   VAL A O   
83    C CB  . VAL A 27   ? 0.3296 0.3238 0.3500 0.0079  0.0230  0.0129  25   VAL A CB  
84    C CG1 . VAL A 27   ? 0.2646 0.2595 0.2876 0.0080  0.0217  0.0128  25   VAL A CG1 
85    C CG2 . VAL A 27   ? 0.2859 0.2742 0.3036 0.0079  0.0219  0.0131  25   VAL A CG2 
86    N N   . ARG A 28   ? 0.2560 0.2647 0.2798 0.0089  0.0266  0.0116  26   ARG A N   
87    C CA  . ARG A 28   ? 0.2893 0.3050 0.3160 0.0089  0.0278  0.0113  26   ARG A CA  
88    C C   . ARG A 28   ? 0.3194 0.3395 0.3448 0.0080  0.0301  0.0122  26   ARG A C   
89    O O   . ARG A 28   ? 0.2670 0.2839 0.2895 0.0068  0.0306  0.0137  26   ARG A O   
90    C CB  . ARG A 28   ? 0.3151 0.3314 0.3441 0.0066  0.0275  0.0128  26   ARG A CB  
91    C CG  . ARG A 28   ? 0.3434 0.3575 0.3710 0.0034  0.0284  0.0154  26   ARG A CG  
92    C CD  . ARG A 28   ? 0.3925 0.4065 0.4225 0.0013  0.0277  0.0164  26   ARG A CD  
93    N NE  . ARG A 28   ? 0.4563 0.4644 0.4853 0.0013  0.0258  0.0163  26   ARG A NE  
94    C CZ  . ARG A 28   ? 0.4462 0.4541 0.4768 0.0024  0.0242  0.0153  26   ARG A CZ  
95    N NH1 . ARG A 28   ? 0.4849 0.4979 0.5187 0.0036  0.0241  0.0142  26   ARG A NH1 
96    N NH2 . ARG A 28   ? 0.4148 0.4176 0.4440 0.0023  0.0226  0.0155  26   ARG A NH2 
97    N N   . PRO A 29   ? 0.3290 0.3566 0.3565 0.0086  0.0314  0.0115  27   PRO A N   
98    C CA  . PRO A 29   ? 0.3258 0.3582 0.3522 0.0072  0.0337  0.0130  27   PRO A CA  
99    C C   . PRO A 29   ? 0.2494 0.2795 0.2754 0.0035  0.0343  0.0164  27   PRO A C   
100   O O   . PRO A 29   ? 0.2988 0.3276 0.3270 0.0018  0.0335  0.0173  27   PRO A O   
101   C CB  . PRO A 29   ? 0.3071 0.3485 0.3368 0.0082  0.0348  0.0118  27   PRO A CB  
102   C CG  . PRO A 29   ? 0.3260 0.3668 0.3576 0.0114  0.0330  0.0087  27   PRO A CG  
103   C CD  . PRO A 29   ? 0.3244 0.3568 0.3554 0.0107  0.0309  0.0093  27   PRO A CD  
104   N N   . GLN A 30   ? 0.2775 0.3069 0.3006 0.0022  0.0354  0.0182  28   GLN A N   
105   C CA  . GLN A 30   ? 0.2851 0.3111 0.3075 -0.0011 0.0357  0.0214  28   GLN A CA  
106   C C   . GLN A 30   ? 0.2916 0.3238 0.3166 -0.0036 0.0372  0.0235  28   GLN A C   
107   O O   . GLN A 30   ? 0.2902 0.3286 0.3148 -0.0037 0.0390  0.0242  28   GLN A O   
108   C CB  . GLN A 30   ? 0.2670 0.2897 0.2854 -0.0012 0.0361  0.0225  28   GLN A CB  
109   C CG  . GLN A 30   ? 0.2599 0.2767 0.2759 0.0011  0.0345  0.0205  28   GLN A CG  
110   C CD  . GLN A 30   ? 0.2922 0.3025 0.3088 0.0003  0.0327  0.0205  28   GLN A CD  
111   O OE1 . GLN A 30   ? 0.2790 0.2849 0.2944 -0.0016 0.0324  0.0224  28   GLN A OE1 
112   N NE2 . GLN A 30   ? 0.2719 0.2817 0.2903 0.0018  0.0314  0.0186  28   GLN A NE2 
113   N N   . SER A 31   ? 0.2707 0.3016 0.2985 -0.0057 0.0365  0.0245  29   SER A N   
114   C CA  . SER A 31   ? 0.2930 0.3291 0.3237 -0.0086 0.0377  0.0267  29   SER A CA  
115   C C   . SER A 31   ? 0.2651 0.3001 0.2939 -0.0113 0.0387  0.0302  29   SER A C   
116   O O   . SER A 31   ? 0.2744 0.3037 0.2998 -0.0110 0.0383  0.0308  29   SER A O   
117   C CB  . SER A 31   ? 0.2532 0.2872 0.2872 -0.0103 0.0363  0.0268  29   SER A CB  
118   O OG  . SER A 31   ? 0.2699 0.2964 0.3025 -0.0120 0.0351  0.0282  29   SER A OG  
119   N N   . THR A 32   ? 0.2344 0.2749 0.2656 -0.0140 0.0401  0.0326  30   THR A N   
120   C CA  . THR A 32   ? 0.2341 0.2733 0.2642 -0.0170 0.0408  0.0364  30   THR A CA  
121   C C   . THR A 32   ? 0.2551 0.2850 0.2844 -0.0184 0.0390  0.0373  30   THR A C   
122   O O   . THR A 32   ? 0.2361 0.2617 0.2624 -0.0189 0.0388  0.0390  30   THR A O   
123   C CB  . THR A 32   ? 0.3055 0.3514 0.3392 -0.0201 0.0422  0.0390  30   THR A CB  
124   O OG1 . THR A 32   ? 0.3361 0.3914 0.3703 -0.0186 0.0441  0.0379  30   THR A OG1 
125   C CG2 . THR A 32   ? 0.3275 0.3718 0.3602 -0.0235 0.0427  0.0434  30   THR A CG2 
126   N N   . LEU A 33   ? 0.2215 0.2485 0.2534 -0.0189 0.0374  0.0361  31   LEU A N   
127   C CA  . LEU A 33   ? 0.2600 0.2789 0.2916 -0.0202 0.0355  0.0365  31   LEU A CA  
128   C C   . LEU A 33   ? 0.2636 0.2766 0.2912 -0.0175 0.0346  0.0348  31   LEU A C   
129   O O   . LEU A 33   ? 0.2297 0.2367 0.2554 -0.0183 0.0337  0.0359  31   LEU A O   
130   C CB  . LEU A 33   ? 0.2684 0.2865 0.3036 -0.0210 0.0341  0.0352  31   LEU A CB  
131   C CG  . LEU A 33   ? 0.2970 0.3192 0.3364 -0.0244 0.0346  0.0373  31   LEU A CG  
132   C CD1 . LEU A 33   ? 0.2891 0.3119 0.3320 -0.0245 0.0333  0.0353  31   LEU A CD1 
133   C CD2 . LEU A 33   ? 0.2959 0.3133 0.3355 -0.0275 0.0340  0.0403  31   LEU A CD2 
134   N N   . ARG A 34   ? 0.2297 0.2442 0.2562 -0.0144 0.0346  0.0320  32   ARG A N   
135   C CA  . ARG A 34   ? 0.2241 0.2334 0.2471 -0.0121 0.0337  0.0305  32   ARG A CA  
136   C C   . ARG A 34   ? 0.2559 0.2649 0.2754 -0.0118 0.0347  0.0319  32   ARG A C   
137   O O   . ARG A 34   ? 0.2429 0.2464 0.2598 -0.0114 0.0339  0.0320  32   ARG A O   
138   C CB  . ARG A 34   ? 0.2438 0.2548 0.2667 -0.0090 0.0333  0.0274  32   ARG A CB  
139   C CG  . ARG A 34   ? 0.2574 0.2670 0.2829 -0.0089 0.0318  0.0258  32   ARG A CG  
140   C CD  . ARG A 34   ? 0.2647 0.2670 0.2886 -0.0091 0.0300  0.0255  32   ARG A CD  
141   N NE  . ARG A 34   ? 0.2717 0.2706 0.2924 -0.0067 0.0295  0.0242  32   ARG A NE  
142   C CZ  . ARG A 34   ? 0.2916 0.2894 0.3122 -0.0046 0.0284  0.0222  32   ARG A CZ  
143   N NH1 . ARG A 34   ? 0.3005 0.3005 0.3237 -0.0042 0.0277  0.0211  32   ARG A NH1 
144   N NH2 . ARG A 34   ? 0.2689 0.2636 0.2868 -0.0029 0.0280  0.0212  32   ARG A NH2 
145   N N   . ARG A 35   ? 0.2126 0.2282 0.2322 -0.0119 0.0366  0.0330  33   ARG A N   
146   C CA  . ARG A 35   ? 0.2323 0.2483 0.2484 -0.0116 0.0375  0.0344  33   ARG A CA  
147   C C   . ARG A 35   ? 0.2729 0.2847 0.2885 -0.0144 0.0372  0.0378  33   ARG A C   
148   O O   . ARG A 35   ? 0.2564 0.2652 0.2687 -0.0139 0.0371  0.0386  33   ARG A O   
149   C CB  . ARG A 35   ? 0.2602 0.2849 0.2764 -0.0112 0.0396  0.0348  33   ARG A CB  
150   C CG  . ARG A 35   ? 0.2961 0.3248 0.3126 -0.0079 0.0398  0.0311  33   ARG A CG  
151   C CD  . ARG A 35   ? 0.4116 0.4488 0.4273 -0.0069 0.0419  0.0312  33   ARG A CD  
152   N NE  . ARG A 35   ? 0.5397 0.5756 0.5512 -0.0055 0.0421  0.0312  33   ARG A NE  
153   C CZ  . ARG A 35   ? 0.5524 0.5949 0.5620 -0.0045 0.0437  0.0313  33   ARG A CZ  
154   N NH1 . ARG A 35   ? 0.5175 0.5689 0.5290 -0.0048 0.0454  0.0314  33   ARG A NH1 
155   N NH2 . ARG A 35   ? 0.5201 0.5606 0.5258 -0.0033 0.0436  0.0311  33   ARG A NH2 
156   N N   . ALA A 36   ? 0.2224 0.2339 0.2411 -0.0172 0.0369  0.0396  34   ALA A N   
157   C CA  . ALA A 36   ? 0.2535 0.2604 0.2721 -0.0199 0.0362  0.0427  34   ALA A CA  
158   C C   . ALA A 36   ? 0.2541 0.2527 0.2711 -0.0190 0.0343  0.0414  34   ALA A C   
159   O O   . ALA A 36   ? 0.2376 0.2320 0.2528 -0.0197 0.0337  0.0432  34   ALA A O   
160   C CB  . ALA A 36   ? 0.2496 0.2581 0.2726 -0.0232 0.0361  0.0446  34   ALA A CB  
161   N N   . ILE A 37   ? 0.2270 0.2237 0.2448 -0.0174 0.0332  0.0383  35   ILE A N   
162   C CA  . ILE A 37   ? 0.2282 0.2182 0.2442 -0.0162 0.0315  0.0367  35   ILE A CA  
163   C C   . ILE A 37   ? 0.2244 0.2131 0.2364 -0.0141 0.0318  0.0364  35   ILE A C   
164   O O   . ILE A 37   ? 0.2263 0.2104 0.2364 -0.0143 0.0311  0.0373  35   ILE A O   
165   C CB  . ILE A 37   ? 0.2260 0.2153 0.2434 -0.0149 0.0305  0.0337  35   ILE A CB  
166   C CG1 . ILE A 37   ? 0.2291 0.2188 0.2504 -0.0172 0.0298  0.0341  35   ILE A CG1 
167   C CG2 . ILE A 37   ? 0.2110 0.1945 0.2261 -0.0134 0.0290  0.0320  35   ILE A CG2 
168   C CD1 . ILE A 37   ? 0.2286 0.2191 0.2515 -0.0160 0.0289  0.0315  35   ILE A CD1 
169   N N   . THR A 38   ? 0.2142 0.2070 0.2249 -0.0120 0.0329  0.0348  36   THR A N   
170   C CA  . THR A 38   ? 0.2512 0.2429 0.2583 -0.0098 0.0330  0.0339  36   THR A CA  
171   C C   . THR A 38   ? 0.2424 0.2344 0.2473 -0.0109 0.0337  0.0368  36   THR A C   
172   O O   . THR A 38   ? 0.2434 0.2318 0.2456 -0.0099 0.0331  0.0368  36   THR A O   
173   C CB  . THR A 38   ? 0.2384 0.2351 0.2452 -0.0075 0.0338  0.0316  36   THR A CB  
174   O OG1 . THR A 38   ? 0.2442 0.2410 0.2534 -0.0068 0.0331  0.0295  36   THR A OG1 
175   C CG2 . THR A 38   ? 0.2458 0.2405 0.2492 -0.0051 0.0335  0.0300  36   THR A CG2 
176   N N   . ALA A 39   ? 0.2193 0.2158 0.2256 -0.0128 0.0350  0.0394  37   ALA A N   
177   C CA  . ALA A 39   ? 0.2492 0.2464 0.2535 -0.0140 0.0356  0.0426  37   ALA A CA  
178   C C   . ALA A 39   ? 0.2576 0.2476 0.2614 -0.0152 0.0340  0.0443  37   ALA A C   
179   O O   . ALA A 39   ? 0.2541 0.2427 0.2553 -0.0151 0.0340  0.0461  37   ALA A O   
180   C CB  . ALA A 39   ? 0.2637 0.2671 0.2700 -0.0163 0.0372  0.0455  37   ALA A CB  
181   N N   . ALA A 40   ? 0.2388 0.2244 0.2452 -0.0163 0.0326  0.0436  38   ALA A N   
182   C CA  . ALA A 40   ? 0.2450 0.2240 0.2516 -0.0174 0.0309  0.0447  38   ALA A CA  
183   C C   . ALA A 40   ? 0.2394 0.2134 0.2436 -0.0151 0.0296  0.0422  38   ALA A C   
184   O O   . ALA A 40   ? 0.2633 0.2322 0.2673 -0.0155 0.0282  0.0429  38   ALA A O   
185   C CB  . ALA A 40   ? 0.2376 0.2146 0.2482 -0.0195 0.0299  0.0447  38   ALA A CB  
186   N N   . TYR A 41   ? 0.2337 0.2095 0.2365 -0.0127 0.0300  0.0394  39   TYR A N   
187   C CA  . TYR A 41   ? 0.2303 0.2019 0.2315 -0.0108 0.0288  0.0368  39   TYR A CA  
188   C C   . TYR A 41   ? 0.2421 0.2095 0.2412 -0.0106 0.0279  0.0379  39   TYR A C   
189   O O   . TYR A 41   ? 0.2632 0.2259 0.2627 -0.0105 0.0264  0.0371  39   TYR A O   
190   C CB  . TYR A 41   ? 0.2307 0.2054 0.2301 -0.0084 0.0295  0.0345  39   TYR A CB  
191   C CG  . TYR A 41   ? 0.2282 0.2001 0.2272 -0.0068 0.0284  0.0316  39   TYR A CG  
192   C CD1 . TYR A 41   ? 0.2283 0.1952 0.2269 -0.0068 0.0270  0.0311  39   TYR A CD1 
193   C CD2 . TYR A 41   ? 0.2399 0.2144 0.2391 -0.0052 0.0288  0.0294  39   TYR A CD2 
194   C CE1 . TYR A 41   ? 0.2370 0.2021 0.2351 -0.0054 0.0261  0.0287  39   TYR A CE1 
195   C CE2 . TYR A 41   ? 0.2347 0.2067 0.2336 -0.0039 0.0277  0.0272  39   TYR A CE2 
196   C CZ  . TYR A 41   ? 0.2456 0.2130 0.2438 -0.0041 0.0265  0.0269  39   TYR A CZ  
197   O OH  . TYR A 41   ? 0.2308 0.1964 0.2288 -0.0031 0.0255  0.0250  39   TYR A OH  
198   N N   . ARG A 42   ? 0.2512 0.2205 0.2479 -0.0103 0.0287  0.0398  40   ARG A N   
199   C CA  . ARG A 42   ? 0.2253 0.1909 0.2197 -0.0099 0.0278  0.0409  40   ARG A CA  
200   C C   . ARG A 42   ? 0.2809 0.2472 0.2752 -0.0117 0.0281  0.0449  40   ARG A C   
201   O O   . ARG A 42   ? 0.2790 0.2447 0.2706 -0.0111 0.0280  0.0464  40   ARG A O   
202   C CB  . ARG A 42   ? 0.2535 0.2202 0.2447 -0.0074 0.0280  0.0391  40   ARG A CB  
203   C CG  . ARG A 42   ? 0.2492 0.2142 0.2409 -0.0060 0.0273  0.0356  40   ARG A CG  
204   C CD  . ARG A 42   ? 0.2992 0.2651 0.2883 -0.0037 0.0274  0.0335  40   ARG A CD  
205   N NE  . ARG A 42   ? 0.2534 0.2188 0.2436 -0.0028 0.0270  0.0307  40   ARG A NE  
206   C CZ  . ARG A 42   ? 0.2789 0.2406 0.2695 -0.0026 0.0258  0.0292  40   ARG A CZ  
207   N NH1 . ARG A 42   ? 0.2649 0.2231 0.2550 -0.0028 0.0247  0.0299  40   ARG A NH1 
208   N NH2 . ARG A 42   ? 0.2444 0.2064 0.2362 -0.0020 0.0255  0.0272  40   ARG A NH2 
209   N N   . ARG A 43   ? 0.2733 0.2407 0.2705 -0.0141 0.0284  0.0468  41   ARG A N   
210   C CA  . ARG A 43   ? 0.2830 0.2511 0.2805 -0.0162 0.0287  0.0511  41   ARG A CA  
211   C C   . ARG A 43   ? 0.2903 0.2522 0.2872 -0.0164 0.0268  0.0526  41   ARG A C   
212   O O   . ARG A 43   ? 0.2711 0.2279 0.2694 -0.0160 0.0251  0.0507  41   ARG A O   
213   C CB  . ARG A 43   ? 0.2649 0.2344 0.2663 -0.0190 0.0289  0.0525  41   ARG A CB  
214   C CG  . ARG A 43   ? 0.2703 0.2405 0.2727 -0.0218 0.0291  0.0573  41   ARG A CG  
215   C CD  . ARG A 43   ? 0.3057 0.2792 0.3120 -0.0243 0.0299  0.0584  41   ARG A CD  
216   N NE  . ARG A 43   ? 0.3001 0.2811 0.3058 -0.0235 0.0320  0.0571  41   ARG A NE  
217   C CZ  . ARG A 43   ? 0.2747 0.2590 0.2834 -0.0242 0.0327  0.0557  41   ARG A CZ  
218   N NH1 . ARG A 43   ? 0.2909 0.2719 0.3033 -0.0259 0.0314  0.0553  41   ARG A NH1 
219   N NH2 . ARG A 43   ? 0.3148 0.3060 0.3229 -0.0230 0.0345  0.0543  41   ARG A NH2 
220   N N   . PRO A 44   ? 0.3022 0.2646 0.2969 -0.0168 0.0269  0.0559  42   PRO A N   
221   C CA  . PRO A 44   ? 0.3292 0.2856 0.3234 -0.0168 0.0249  0.0575  42   PRO A CA  
222   C C   . PRO A 44   ? 0.2990 0.2502 0.2972 -0.0188 0.0232  0.0582  42   PRO A C   
223   O O   . PRO A 44   ? 0.2997 0.2526 0.3009 -0.0212 0.0237  0.0596  42   PRO A O   
224   C CB  . PRO A 44   ? 0.3377 0.2968 0.3296 -0.0177 0.0257  0.0619  42   PRO A CB  
225   C CG  . PRO A 44   ? 0.3315 0.2982 0.3213 -0.0167 0.0281  0.0610  42   PRO A CG  
226   C CD  . PRO A 44   ? 0.3328 0.3017 0.3252 -0.0170 0.0289  0.0582  42   PRO A CD  
227   N N   . GLU A 45   ? 0.3680 0.3131 0.3664 -0.0177 0.0210  0.0569  43   GLU A N   
228   C CA  . GLU A 45   ? 0.3103 0.2502 0.3125 -0.0191 0.0191  0.0565  43   GLU A CA  
229   C C   . GLU A 45   ? 0.3091 0.2476 0.3136 -0.0221 0.0184  0.0611  43   GLU A C   
230   O O   . GLU A 45   ? 0.3187 0.2556 0.3270 -0.0242 0.0176  0.0614  43   GLU A O   
231   C CB  . GLU A 45   ? 0.3539 0.2883 0.3555 -0.0169 0.0169  0.0540  43   GLU A CB  
232   C CG  . GLU A 45   ? 0.3634 0.2938 0.3685 -0.0171 0.0152  0.0511  43   GLU A CG  
233   C CD  . GLU A 45   ? 0.2958 0.2236 0.2998 -0.0143 0.0139  0.0472  43   GLU A CD  
234   O OE1 . GLU A 45   ? 0.3249 0.2542 0.3256 -0.0123 0.0146  0.0463  43   GLU A OE1 
235   O OE2 . GLU A 45   ? 0.3247 0.2492 0.3314 -0.0143 0.0123  0.0448  43   GLU A OE2 
236   N N   . THR A 46   ? 0.3081 0.2473 0.3102 -0.0224 0.0187  0.0650  44   THR A N   
237   C CA  . THR A 46   ? 0.3356 0.2738 0.3397 -0.0255 0.0181  0.0702  44   THR A CA  
238   C C   . THR A 46   ? 0.3502 0.2940 0.3563 -0.0282 0.0201  0.0720  44   THR A C   
239   O O   . THR A 46   ? 0.3940 0.3366 0.4032 -0.0314 0.0194  0.0756  44   THR A O   
240   C CB  . THR A 46   ? 0.3399 0.2787 0.3406 -0.0252 0.0182  0.0741  44   THR A CB  
241   O OG1 . THR A 46   ? 0.3266 0.2724 0.3234 -0.0237 0.0207  0.0734  44   THR A OG1 
242   C CG2 . THR A 46   ? 0.3462 0.2786 0.3458 -0.0229 0.0157  0.0730  44   THR A CG2 
243   N N   . GLU A 47   ? 0.3243 0.2745 0.3289 -0.0272 0.0224  0.0697  45   GLU A N   
244   C CA  . GLU A 47   ? 0.3142 0.2704 0.3210 -0.0294 0.0243  0.0708  45   GLU A CA  
245   C C   . GLU A 47   ? 0.3214 0.2763 0.3320 -0.0300 0.0237  0.0675  45   GLU A C   
246   O O   . GLU A 47   ? 0.3195 0.2769 0.3334 -0.0327 0.0243  0.0691  45   GLU A O   
247   C CB  . GLU A 47   ? 0.3371 0.3011 0.3404 -0.0278 0.0270  0.0698  45   GLU A CB  
248   C CG  . GLU A 47   ? 0.4042 0.3705 0.4036 -0.0272 0.0277  0.0731  45   GLU A CG  
249   C CD  . GLU A 47   ? 0.4673 0.4412 0.4633 -0.0252 0.0301  0.0714  45   GLU A CD  
250   O OE1 . GLU A 47   ? 0.4550 0.4329 0.4521 -0.0247 0.0314  0.0685  45   GLU A OE1 
251   O OE2 . GLU A 47   ? 0.5567 0.5323 0.5488 -0.0239 0.0305  0.0728  45   GLU A OE2 
252   N N   . CYS A 48   ? 0.2864 0.2375 0.2968 -0.0276 0.0225  0.0630  46   CYS A N   
253   C CA  . CYS A 48   ? 0.2955 0.2456 0.3093 -0.0280 0.0219  0.0599  46   CYS A CA  
254   C C   . CYS A 48   ? 0.2983 0.2429 0.3163 -0.0304 0.0195  0.0612  46   CYS A C   
255   O O   . CYS A 48   ? 0.2746 0.2200 0.2963 -0.0324 0.0193  0.0606  46   CYS A O   
256   C CB  . CYS A 48   ? 0.3047 0.2527 0.3169 -0.0249 0.0212  0.0550  46   CYS A CB  
257   S SG  . CYS A 48   ? 0.3258 0.2796 0.3341 -0.0221 0.0235  0.0526  46   CYS A SG  
258   N N   . LEU A 49   ? 0.3125 0.2512 0.3301 -0.0303 0.0176  0.0627  47   LEU A N   
259   C CA  . LEU A 49   ? 0.3278 0.2601 0.3494 -0.0317 0.0148  0.0625  47   LEU A CA  
260   C C   . LEU A 49   ? 0.3130 0.2452 0.3386 -0.0357 0.0144  0.0667  47   LEU A C   
261   O O   . LEU A 49   ? 0.3432 0.2728 0.3730 -0.0372 0.0128  0.0653  47   LEU A O   
262   C CB  . LEU A 49   ? 0.3324 0.2580 0.3527 -0.0300 0.0125  0.0625  47   LEU A CB  
263   C CG  . LEU A 49   ? 0.3557 0.2783 0.3756 -0.0270 0.0112  0.0571  47   LEU A CG  
264   C CD1 . LEU A 49   ? 0.3474 0.2672 0.3718 -0.0280 0.0094  0.0543  47   LEU A CD1 
265   C CD2 . LEU A 49   ? 0.3092 0.2370 0.3258 -0.0246 0.0134  0.0540  47   LEU A CD2 
266   N N   . PRO A 50   ? 0.3457 0.2808 0.3703 -0.0377 0.0156  0.0717  48   PRO A N   
267   C CA  . PRO A 50   ? 0.3333 0.2681 0.3621 -0.0419 0.0150  0.0761  48   PRO A CA  
268   C C   . PRO A 50   ? 0.3133 0.2520 0.3460 -0.0438 0.0158  0.0744  48   PRO A C   
269   O O   . PRO A 50   ? 0.3433 0.2781 0.3807 -0.0462 0.0138  0.0748  48   PRO A O   
270   C CB  . PRO A 50   ? 0.3601 0.2999 0.3861 -0.0431 0.0170  0.0813  48   PRO A CB  
271   C CG  . PRO A 50   ? 0.3319 0.2697 0.3531 -0.0398 0.0168  0.0806  48   PRO A CG  
272   C CD  . PRO A 50   ? 0.3502 0.2882 0.3701 -0.0363 0.0171  0.0742  48   PRO A CD  
273   N N   . PRO A 51   ? 0.3332 0.2792 0.3643 -0.0428 0.0185  0.0725  49   PRO A N   
274   C CA  . PRO A 51   ? 0.3292 0.2787 0.3642 -0.0445 0.0189  0.0707  49   PRO A CA  
275   C C   . PRO A 51   ? 0.3491 0.2936 0.3866 -0.0434 0.0167  0.0660  49   PRO A C   
276   O O   . PRO A 51   ? 0.3422 0.2870 0.3841 -0.0455 0.0159  0.0653  49   PRO A O   
277   C CB  . PRO A 51   ? 0.3307 0.2885 0.3628 -0.0427 0.0220  0.0692  49   PRO A CB  
278   C CG  . PRO A 51   ? 0.3623 0.3191 0.3893 -0.0392 0.0225  0.0678  49   PRO A CG  
279   C CD  . PRO A 51   ? 0.3302 0.2818 0.3563 -0.0400 0.0210  0.0715  49   PRO A CD  
280   N N   . LEU A 52   ? 0.3421 0.2825 0.3769 -0.0400 0.0156  0.0626  50   LEU A N   
281   C CA  . LEU A 52   ? 0.2985 0.2345 0.3355 -0.0389 0.0134  0.0581  50   LEU A CA  
282   C C   . LEU A 52   ? 0.3462 0.2751 0.3871 -0.0410 0.0103  0.0593  50   LEU A C   
283   O O   . LEU A 52   ? 0.3015 0.2287 0.3465 -0.0422 0.0087  0.0572  50   LEU A O   
284   C CB  . LEU A 52   ? 0.2857 0.2199 0.3187 -0.0349 0.0132  0.0543  50   LEU A CB  
285   C CG  . LEU A 52   ? 0.2883 0.2287 0.3177 -0.0328 0.0159  0.0527  50   LEU A CG  
286   C CD1 . LEU A 52   ? 0.2702 0.2083 0.2956 -0.0292 0.0156  0.0498  50   LEU A CD1 
287   C CD2 . LEU A 52   ? 0.2885 0.2329 0.3201 -0.0331 0.0165  0.0499  50   LEU A CD2 
288   N N   . VAL A 53   ? 0.3371 0.2618 0.3770 -0.0413 0.0093  0.0626  51   VAL A N   
289   C CA  . VAL A 53   ? 0.3444 0.2622 0.3883 -0.0435 0.0062  0.0646  51   VAL A CA  
290   C C   . VAL A 53   ? 0.3879 0.3079 0.4368 -0.0477 0.0062  0.0670  51   VAL A C   
291   O O   . VAL A 53   ? 0.3533 0.2692 0.4069 -0.0491 0.0038  0.0653  51   VAL A O   
292   C CB  . VAL A 53   ? 0.3724 0.2866 0.4143 -0.0436 0.0056  0.0690  51   VAL A CB  
293   C CG1 . VAL A 53   ? 0.4118 0.3190 0.4585 -0.0464 0.0023  0.0718  51   VAL A CG1 
294   C CG2 . VAL A 53   ? 0.3378 0.2494 0.3755 -0.0395 0.0051  0.0662  51   VAL A CG2 
295   N N   . GLU A 54   ? 0.3313 0.2581 0.3794 -0.0497 0.0090  0.0707  52   GLU A N   
296   C CA  . GLU A 54   ? 0.3924 0.3218 0.4453 -0.0539 0.0091  0.0734  52   GLU A CA  
297   C C   . GLU A 54   ? 0.3726 0.3041 0.4287 -0.0539 0.0088  0.0688  52   GLU A C   
298   O O   . GLU A 54   ? 0.3600 0.2893 0.4214 -0.0567 0.0069  0.0689  52   GLU A O   
299   C CB  . GLU A 54   ? 0.3771 0.3147 0.4283 -0.0558 0.0124  0.0780  52   GLU A CB  
300   N N   . ALA A 55   ? 0.3277 0.2632 0.3806 -0.0507 0.0105  0.0646  53   ALA A N   
301   C CA  . ALA A 55   ? 0.3303 0.2684 0.3857 -0.0505 0.0103  0.0604  53   ALA A CA  
302   C C   . ALA A 55   ? 0.3368 0.2681 0.3947 -0.0496 0.0070  0.0563  53   ALA A C   
303   O O   . ALA A 55   ? 0.3614 0.2934 0.4232 -0.0508 0.0059  0.0539  53   ALA A O   
304   C CB  . ALA A 55   ? 0.3337 0.2777 0.3850 -0.0472 0.0128  0.0573  53   ALA A CB  
305   N N   . ALA A 56   ? 0.3530 0.2781 0.4088 -0.0473 0.0053  0.0553  54   ALA A N   
306   C CA  . ALA A 56   ? 0.3287 0.2477 0.3863 -0.0459 0.0022  0.0510  54   ALA A CA  
307   C C   . ALA A 56   ? 0.4307 0.3430 0.4933 -0.0486 -0.0010 0.0528  54   ALA A C   
308   O O   . ALA A 56   ? 0.3638 0.2709 0.4288 -0.0476 -0.0039 0.0491  54   ALA A O   
309   C CB  . ALA A 56   ? 0.3364 0.2526 0.3895 -0.0418 0.0020  0.0486  54   ALA A CB  
310   N N   . THR A 57   ? 0.4518 0.3643 0.5163 -0.0521 -0.0006 0.0585  55   THR A N   
311   C CA  . THR A 57   ? 0.4370 0.3426 0.5062 -0.0549 -0.0038 0.0610  55   THR A CA  
312   C C   . THR A 57   ? 0.4107 0.3158 0.4859 -0.0573 -0.0057 0.0585  55   THR A C   
313   O O   . THR A 57   ? 0.3869 0.2985 0.4635 -0.0589 -0.0039 0.0584  55   THR A O   
314   C CB  . THR A 57   ? 0.3936 0.3006 0.4630 -0.0583 -0.0025 0.0682  55   THR A CB  
315   O OG1 . THR A 57   ? 0.4330 0.3399 0.4970 -0.0559 -0.0012 0.0702  55   THR A OG1 
316   C CG2 . THR A 57   ? 0.4116 0.3114 0.4866 -0.0618 -0.0059 0.0713  55   THR A CG2 
317   N N   . GLN A 58   ? 0.3896 0.2869 0.4684 -0.0572 -0.0096 0.0561  56   GLN A N   
318   C CA  . GLN A 58   ? 0.4102 0.3060 0.4950 -0.0594 -0.0120 0.0536  56   GLN A CA  
319   C C   . GLN A 58   ? 0.4120 0.2997 0.5020 -0.0624 -0.0156 0.0567  56   GLN A C   
320   O O   . GLN A 58   ? 0.3825 0.2650 0.4710 -0.0618 -0.0166 0.0595  56   GLN A O   
321   C CB  . GLN A 58   ? 0.4450 0.3399 0.5297 -0.0560 -0.0136 0.0462  56   GLN A CB  
322   C CG  . GLN A 58   ? 0.4030 0.3051 0.4825 -0.0528 -0.0104 0.0432  56   GLN A CG  
323   C CD  . GLN A 58   ? 0.3680 0.2712 0.4486 -0.0508 -0.0118 0.0366  56   GLN A CD  
324   O OE1 . GLN A 58   ? 0.4143 0.3199 0.4988 -0.0529 -0.0124 0.0353  56   GLN A OE1 
325   N NE2 . GLN A 58   ? 0.4056 0.3072 0.4826 -0.0467 -0.0123 0.0325  56   GLN A NE2 
326   N N   . SER A 59   ? 0.4258 0.3125 0.5220 -0.0657 -0.0176 0.0560  57   SER A N   
327   C CA  . SER A 59   ? 0.4875 0.3666 0.5894 -0.0691 -0.0212 0.0591  57   SER A CA  
328   C C   . SER A 59   ? 0.5026 0.3724 0.6052 -0.0662 -0.0251 0.0558  57   SER A C   
329   O O   . SER A 59   ? 0.4482 0.3177 0.5478 -0.0618 -0.0254 0.0499  57   SER A O   
330   C CB  . SER A 59   ? 0.4734 0.3536 0.5821 -0.0728 -0.0228 0.0579  57   SER A CB  
331   O OG  . SER A 59   ? 0.4773 0.3558 0.5875 -0.0702 -0.0251 0.0505  57   SER A OG  
332   N N   . LYS A 60   ? 0.4251 0.2871 0.5316 -0.0687 -0.0282 0.0597  58   LYS A N   
333   C CA  . LYS A 60   ? 0.4981 0.3505 0.6062 -0.0661 -0.0325 0.0564  58   LYS A CA  
334   C C   . LYS A 60   ? 0.4761 0.3270 0.5879 -0.0646 -0.0353 0.0486  58   LYS A C   
335   O O   . LYS A 60   ? 0.4753 0.3233 0.5853 -0.0602 -0.0369 0.0430  58   LYS A O   
336   C CB  . LYS A 60   ? 0.4108 0.2550 0.5237 -0.0697 -0.0358 0.0620  58   LYS A CB  
337   N N   . GLU A 61   ? 0.4444 0.2977 0.5613 -0.0681 -0.0358 0.0482  59   GLU A N   
338   C CA  . GLU A 61   ? 0.4499 0.3021 0.5704 -0.0669 -0.0386 0.0409  59   GLU A CA  
339   C C   . GLU A 61   ? 0.4558 0.3143 0.5708 -0.0622 -0.0362 0.0349  59   GLU A C   
340   O O   . GLU A 61   ? 0.4578 0.3136 0.5730 -0.0587 -0.0386 0.0284  59   GLU A O   
341   C CB  . GLU A 61   ? 0.4582 0.3133 0.5846 -0.0717 -0.0390 0.0420  59   GLU A CB  
342   N N   . ILE A 62   ? 0.3977 0.2649 0.5080 -0.0621 -0.0316 0.0369  60   ILE A N   
343   C CA  . ILE A 62   ? 0.4365 0.3096 0.5415 -0.0579 -0.0293 0.0319  60   ILE A CA  
344   C C   . ILE A 62   ? 0.4459 0.3157 0.5461 -0.0533 -0.0296 0.0300  60   ILE A C   
345   O O   . ILE A 62   ? 0.4265 0.2971 0.5247 -0.0495 -0.0302 0.0239  60   ILE A O   
346   C CB  . ILE A 62   ? 0.4407 0.3233 0.5421 -0.0589 -0.0246 0.0350  60   ILE A CB  
347   C CG1 . ILE A 62   ? 0.4954 0.3826 0.6015 -0.0623 -0.0245 0.0345  60   ILE A CG1 
348   C CG2 . ILE A 62   ? 0.3955 0.2831 0.4904 -0.0543 -0.0220 0.0313  60   ILE A CG2 
349   C CD1 . ILE A 62   ? 0.4593 0.3559 0.5626 -0.0634 -0.0201 0.0374  60   ILE A CD1 
350   N N   . ARG A 63   ? 0.4176 0.2839 0.5159 -0.0537 -0.0291 0.0351  61   ARG A N   
351   C CA  . ARG A 63   ? 0.4129 0.2762 0.5068 -0.0494 -0.0294 0.0335  61   ARG A CA  
352   C C   . ARG A 63   ? 0.4434 0.2995 0.5407 -0.0471 -0.0340 0.0282  61   ARG A C   
353   O O   . ARG A 63   ? 0.4047 0.2609 0.4988 -0.0427 -0.0342 0.0234  61   ARG A O   
354   C CB  . ARG A 63   ? 0.4142 0.2751 0.5059 -0.0505 -0.0283 0.0403  61   ARG A CB  
355   C CG  . ARG A 63   ? 0.4889 0.3579 0.5759 -0.0514 -0.0235 0.0445  61   ARG A CG  
356   C CD  . ARG A 63   ? 0.5176 0.3850 0.6010 -0.0513 -0.0223 0.0501  61   ARG A CD  
357   N NE  . ARG A 63   ? 0.5115 0.3756 0.5987 -0.0557 -0.0233 0.0566  61   ARG A NE  
358   C CZ  . ARG A 63   ? 0.5641 0.4200 0.6535 -0.0562 -0.0265 0.0591  61   ARG A CZ  
359   N NH1 . ARG A 63   ? 0.6179 0.4681 0.7064 -0.0524 -0.0291 0.0555  61   ARG A NH1 
360   N NH2 . ARG A 63   ? 0.4893 0.3429 0.5819 -0.0606 -0.0272 0.0657  61   ARG A NH2 
361   N N   . ASP A 64   ? 0.4608 0.3106 0.5647 -0.0500 -0.0377 0.0288  62   ASP A N   
362   C CA  . ASP A 64   ? 0.4659 0.3089 0.5737 -0.0478 -0.0424 0.0230  62   ASP A CA  
363   C C   . ASP A 64   ? 0.4349 0.2825 0.5429 -0.0456 -0.0426 0.0155  62   ASP A C   
364   O O   . ASP A 64   ? 0.4442 0.2903 0.5513 -0.0415 -0.0445 0.0096  62   ASP A O   
365   C CB  . ASP A 64   ? 0.4865 0.3217 0.6018 -0.0518 -0.0464 0.0255  62   ASP A CB  
366   C CG  . ASP A 64   ? 0.4967 0.3259 0.6122 -0.0535 -0.0471 0.0326  62   ASP A CG  
367   O OD1 . ASP A 64   ? 0.5116 0.3426 0.6214 -0.0514 -0.0446 0.0352  62   ASP A OD1 
368   O OD2 . ASP A 64   ? 0.5542 0.3768 0.6758 -0.0569 -0.0504 0.0355  62   ASP A OD2 
369   N N   . ALA A 65   ? 0.4054 0.2589 0.5146 -0.0483 -0.0409 0.0156  63   ALA A N   
370   C CA  . ALA A 65   ? 0.4487 0.3073 0.5579 -0.0463 -0.0411 0.0089  63   ALA A CA  
371   C C   . ALA A 65   ? 0.4254 0.2897 0.5275 -0.0418 -0.0382 0.0060  63   ALA A C   
372   O O   . ALA A 65   ? 0.4088 0.2743 0.5101 -0.0385 -0.0395 -0.0005 63   ALA A O   
373   C CB  . ALA A 65   ? 0.4442 0.3087 0.5557 -0.0501 -0.0395 0.0103  63   ALA A CB  
374   N N   . ALA A 66   ? 0.4231 0.2911 0.5200 -0.0418 -0.0343 0.0107  64   ALA A N   
375   C CA  . ALA A 66   ? 0.4439 0.3171 0.5342 -0.0378 -0.0315 0.0084  64   ALA A CA  
376   C C   . ALA A 66   ? 0.4233 0.2919 0.5120 -0.0339 -0.0334 0.0053  64   ALA A C   
377   O O   . ALA A 66   ? 0.3843 0.2561 0.4702 -0.0303 -0.0332 0.0001  64   ALA A O   
378   C CB  . ALA A 66   ? 0.4007 0.2786 0.4864 -0.0388 -0.0271 0.0142  64   ALA A CB  
379   N N   . ALA A 67   ? 0.4156 0.2770 0.5060 -0.0344 -0.0354 0.0085  65   ALA A N   
380   C CA  . ALA A 67   ? 0.4389 0.2956 0.5284 -0.0305 -0.0376 0.0054  65   ALA A CA  
381   C C   . ALA A 67   ? 0.4430 0.2977 0.5361 -0.0284 -0.0413 -0.0021 65   ALA A C   
382   O O   . ALA A 67   ? 0.4543 0.3098 0.5450 -0.0242 -0.0420 -0.0069 65   ALA A O   
383   C CB  . ALA A 67   ? 0.4049 0.2536 0.4964 -0.0319 -0.0396 0.0104  65   ALA A CB  
384   N N   . SER A 68   ? 0.4558 0.3085 0.5545 -0.0311 -0.0438 -0.0033 66   SER A N   
385   C CA  . SER A 68   ? 0.4641 0.3153 0.5665 -0.0292 -0.0474 -0.0107 66   SER A CA  
386   C C   . SER A 68   ? 0.4631 0.3230 0.5619 -0.0267 -0.0454 -0.0160 66   SER A C   
387   O O   . SER A 68   ? 0.4426 0.3032 0.5407 -0.0229 -0.0470 -0.0223 66   SER A O   
388   C CB  . SER A 68   ? 0.4994 0.3462 0.6090 -0.0331 -0.0506 -0.0104 66   SER A CB  
389   O OG  . SER A 68   ? 0.6043 0.4524 0.7168 -0.0316 -0.0532 -0.0178 66   SER A OG  
390   N N   . THR A 69   ? 0.4285 0.2952 0.5249 -0.0288 -0.0419 -0.0134 67   THR A N   
391   C CA  . THR A 69   ? 0.4247 0.2998 0.5173 -0.0266 -0.0397 -0.0176 67   THR A CA  
392   C C   . THR A 69   ? 0.4033 0.2812 0.4897 -0.0226 -0.0376 -0.0187 67   THR A C   
393   O O   . THR A 69   ? 0.3977 0.2796 0.4821 -0.0194 -0.0379 -0.0242 67   THR A O   
394   C CB  . THR A 69   ? 0.3796 0.2610 0.4709 -0.0295 -0.0364 -0.0139 67   THR A CB  
395   O OG1 . THR A 69   ? 0.4328 0.3122 0.5301 -0.0332 -0.0385 -0.0134 67   THR A OG1 
396   C CG2 . THR A 69   ? 0.3629 0.2528 0.4500 -0.0272 -0.0343 -0.0178 67   THR A CG2 
397   N N   . ALA A 70   ? 0.3850 0.2613 0.4684 -0.0228 -0.0355 -0.0134 68   ALA A N   
398   C CA  . ALA A 70   ? 0.4034 0.2824 0.4812 -0.0192 -0.0336 -0.0142 68   ALA A CA  
399   C C   . ALA A 70   ? 0.4313 0.3063 0.5104 -0.0156 -0.0369 -0.0194 68   ALA A C   
400   O O   . ALA A 70   ? 0.3668 0.2461 0.4425 -0.0121 -0.0361 -0.0234 68   ALA A O   
401   C CB  . ALA A 70   ? 0.3339 0.2115 0.4087 -0.0202 -0.0310 -0.0076 68   ALA A CB  
402   N N   . ARG A 71   ? 0.4303 0.2973 0.5145 -0.0164 -0.0406 -0.0193 69   ARG A N   
403   C CA  . ARG A 71   ? 0.4785 0.3414 0.5647 -0.0129 -0.0442 -0.0248 69   ARG A CA  
404   C C   . ARG A 71   ? 0.3999 0.2675 0.4869 -0.0108 -0.0455 -0.0323 69   ARG A C   
405   O O   . ARG A 71   ? 0.4557 0.3262 0.5405 -0.0068 -0.0459 -0.0372 69   ARG A O   
406   C CB  . ARG A 71   ? 0.4150 0.2681 0.5074 -0.0144 -0.0484 -0.0234 69   ARG A CB  
407   C CG  . ARG A 71   ? 0.4564 0.3051 0.5519 -0.0108 -0.0528 -0.0300 69   ARG A CG  
408   C CD  . ARG A 71   ? 0.4498 0.2879 0.5506 -0.0118 -0.0568 -0.0277 69   ARG A CD  
409   N NE  . ARG A 71   ? 0.5103 0.3453 0.6082 -0.0106 -0.0559 -0.0233 69   ARG A NE  
410   C CZ  . ARG A 71   ? 0.5591 0.3945 0.6546 -0.0062 -0.0563 -0.0266 69   ARG A CZ  
411   N NH1 . ARG A 71   ? 0.5790 0.4180 0.6745 -0.0025 -0.0576 -0.0343 69   ARG A NH1 
412   N NH2 . ARG A 71   ? 0.5381 0.3708 0.6310 -0.0055 -0.0555 -0.0221 69   ARG A NH2 
413   N N   . LYS A 72   ? 0.3773 0.2464 0.4675 -0.0134 -0.0462 -0.0333 70   LYS A N   
414   C CA  . LYS A 72   ? 0.4123 0.2861 0.5033 -0.0116 -0.0477 -0.0403 70   LYS A CA  
415   C C   . LYS A 72   ? 0.4746 0.3579 0.5594 -0.0091 -0.0441 -0.0421 70   LYS A C   
416   O O   . LYS A 72   ? 0.4491 0.3360 0.5328 -0.0057 -0.0452 -0.0483 70   LYS A O   
417   C CB  . LYS A 72   ? 0.4886 0.3629 0.5838 -0.0152 -0.0486 -0.0402 70   LYS A CB  
418   N N   . LEU A 73   ? 0.4074 0.2947 0.4879 -0.0108 -0.0400 -0.0368 71   LEU A N   
419   C CA  . LEU A 73   ? 0.4232 0.3189 0.4978 -0.0087 -0.0367 -0.0378 71   LEU A CA  
420   C C   . LEU A 73   ? 0.4174 0.3133 0.4888 -0.0049 -0.0365 -0.0397 71   LEU A C   
421   O O   . LEU A 73   ? 0.4201 0.3220 0.4887 -0.0021 -0.0359 -0.0441 71   LEU A O   
422   C CB  . LEU A 73   ? 0.3838 0.2828 0.4549 -0.0112 -0.0326 -0.0315 71   LEU A CB  
423   C CG  . LEU A 73   ? 0.3936 0.2941 0.4673 -0.0149 -0.0322 -0.0295 71   LEU A CG  
424   C CD1 . LEU A 73   ? 0.3956 0.2982 0.4663 -0.0171 -0.0284 -0.0229 71   LEU A CD1 
425   C CD2 . LEU A 73   ? 0.4031 0.3104 0.4761 -0.0139 -0.0323 -0.0344 71   LEU A CD2 
426   N N   . ILE A 74   ? 0.4044 0.2942 0.4762 -0.0049 -0.0369 -0.0363 72   ILE A N   
427   C CA  . ILE A 74   ? 0.4283 0.3184 0.4971 -0.0014 -0.0365 -0.0376 72   ILE A CA  
428   C C   . ILE A 74   ? 0.4378 0.3265 0.5094 0.0020  -0.0402 -0.0447 72   ILE A C   
429   O O   . ILE A 74   ? 0.4533 0.3465 0.5220 0.0054  -0.0397 -0.0484 72   ILE A O   
430   C CB  . ILE A 74   ? 0.4449 0.3288 0.5133 -0.0023 -0.0361 -0.0318 72   ILE A CB  
431   C CG1 . ILE A 74   ? 0.4416 0.3289 0.5062 -0.0049 -0.0319 -0.0255 72   ILE A CG1 
432   C CG2 . ILE A 74   ? 0.4222 0.3054 0.4887 0.0014  -0.0366 -0.0336 72   ILE A CG2 
433   C CD1 . ILE A 74   ? 0.4836 0.3652 0.5483 -0.0066 -0.0314 -0.0193 72   ILE A CD1 
434   N N   . GLU A 75   ? 0.4839 0.3666 0.5613 0.0011  -0.0441 -0.0468 73   GLU A N   
435   C CA  . GLU A 75   ? 0.4904 0.3721 0.5709 0.0044  -0.0479 -0.0543 73   GLU A CA  
436   C C   . GLU A 75   ? 0.4541 0.3450 0.5323 0.0063  -0.0471 -0.0599 73   GLU A C   
437   O O   . GLU A 75   ? 0.5069 0.4014 0.5839 0.0101  -0.0479 -0.0653 73   GLU A O   
438   C CB  . GLU A 75   ? 0.4690 0.3425 0.5565 0.0026  -0.0523 -0.0554 73   GLU A CB  
439   C CG  . GLU A 75   ? 0.5080 0.3718 0.5982 0.0024  -0.0545 -0.0518 73   GLU A CG  
440   C CD  . GLU A 75   ? 0.5545 0.4096 0.6516 -0.0005 -0.0584 -0.0509 73   GLU A CD  
441   O OE1 . GLU A 75   ? 0.5099 0.3662 0.6097 -0.0029 -0.0591 -0.0521 73   GLU A OE1 
442   O OE2 . GLU A 75   ? 0.5662 0.4131 0.6661 -0.0003 -0.0608 -0.0487 73   GLU A OE2 
443   N N   . ALA A 76   ? 0.4716 0.3669 0.5490 0.0036  -0.0454 -0.0586 74   ALA A N   
444   C CA  . ALA A 76   ? 0.5063 0.4110 0.5808 0.0051  -0.0441 -0.0630 74   ALA A CA  
445   C C   . ALA A 76   ? 0.4783 0.3896 0.5467 0.0075  -0.0407 -0.0623 74   ALA A C   
446   O O   . ALA A 76   ? 0.5239 0.4412 0.5905 0.0106  -0.0410 -0.0677 74   ALA A O   
447   C CB  . ALA A 76   ? 0.4470 0.3551 0.5214 0.0017  -0.0425 -0.0605 74   ALA A CB  
448   N N   . LEU A 77   ? 0.4800 0.3906 0.5451 0.0059  -0.0375 -0.0559 75   LEU A N   
449   C CA  . LEU A 77   ? 0.5049 0.4216 0.5644 0.0077  -0.0342 -0.0548 75   LEU A CA  
450   C C   . LEU A 77   ? 0.5514 0.4681 0.6107 0.0117  -0.0357 -0.0589 75   LEU A C   
451   O O   . LEU A 77   ? 0.5192 0.4432 0.5753 0.0142  -0.0346 -0.0623 75   LEU A O   
452   C CB  . LEU A 77   ? 0.4632 0.3778 0.5200 0.0054  -0.0311 -0.0474 75   LEU A CB  
453   C CG  . LEU A 77   ? 0.4612 0.3801 0.5157 0.0026  -0.0281 -0.0434 75   LEU A CG  
454   C CD1 . LEU A 77   ? 0.4897 0.4064 0.5416 0.0010  -0.0253 -0.0368 75   LEU A CD1 
455   C CD2 . LEU A 77   ? 0.4574 0.3854 0.5079 0.0041  -0.0263 -0.0462 75   LEU A CD2 
456   N N   . ARG A 78   ? 0.4964 0.4049 0.5590 0.0122  -0.0382 -0.0585 76   ARG A N   
457   C CA  . ARG A 78   ? 0.5328 0.4408 0.5955 0.0161  -0.0397 -0.0621 76   ARG A CA  
458   C C   . ARG A 78   ? 0.5558 0.4661 0.6212 0.0191  -0.0430 -0.0702 76   ARG A C   
459   O O   . ARG A 78   ? 0.5866 0.4989 0.6517 0.0228  -0.0439 -0.0743 76   ARG A O   
460   C CB  . ARG A 78   ? 0.4839 0.3823 0.5494 0.0157  -0.0416 -0.0587 76   ARG A CB  
461   C CG  . ARG A 78   ? 0.4886 0.3860 0.5504 0.0138  -0.0382 -0.0515 76   ARG A CG  
462   C CD  . ARG A 78   ? 0.4712 0.3599 0.5353 0.0139  -0.0401 -0.0483 76   ARG A CD  
463   N NE  . ARG A 78   ? 0.4757 0.3653 0.5355 0.0136  -0.0370 -0.0431 76   ARG A NE  
464   C CZ  . ARG A 78   ? 0.4818 0.3651 0.5422 0.0135  -0.0377 -0.0392 76   ARG A CZ  
465   N NH1 . ARG A 78   ? 0.5183 0.3932 0.5835 0.0134  -0.0415 -0.0393 76   ARG A NH1 
466   N NH2 . ARG A 78   ? 0.4983 0.3836 0.5545 0.0134  -0.0348 -0.0350 76   ARG A NH2 
467   N N   . GLY A 79   ? 0.5464 0.4570 0.6147 0.0178  -0.0447 -0.0730 77   GLY A N   
468   C CA  . GLY A 79   ? 0.5957 0.5092 0.6665 0.0207  -0.0478 -0.0811 77   GLY A CA  
469   C C   . GLY A 79   ? 0.5943 0.5191 0.6612 0.0216  -0.0456 -0.0841 77   GLY A C   
470   O O   . GLY A 79   ? 0.6428 0.5712 0.7115 0.0232  -0.0479 -0.0905 77   GLY A O   
471   N N   . LYS A 80   ? 0.6091 0.5395 0.6706 0.0205  -0.0414 -0.0796 78   LYS A N   
472   C CA  . LYS A 80   ? 0.6502 0.5914 0.7075 0.0213  -0.0392 -0.0818 78   LYS A CA  
473   C C   . LYS A 80   ? 0.5837 0.5297 0.6357 0.0221  -0.0355 -0.0784 78   LYS A C   
474   O O   . LYS A 80   ? 0.6810 0.6360 0.7296 0.0239  -0.0340 -0.0810 78   LYS A O   
475   C CB  . LYS A 80   ? 0.6266 0.5700 0.6833 0.0180  -0.0380 -0.0794 78   LYS A CB  
476   C CG  . LYS A 80   ? 0.6029 0.5430 0.6579 0.0145  -0.0350 -0.0714 78   LYS A CG  
477   C CD  . LYS A 80   ? 0.5365 0.4812 0.5900 0.0118  -0.0333 -0.0692 78   LYS A CD  
478   C CE  . LYS A 80   ? 0.5017 0.4403 0.5600 0.0089  -0.0354 -0.0682 78   LYS A CE  
479   N NZ  . LYS A 80   ? 0.4232 0.3646 0.4798 0.0058  -0.0329 -0.0637 78   LYS A NZ  
480   N N   . GLY A 85   ? 0.6771 0.6823 0.6976 0.0299  -0.0151 -0.0727 83   GLY A N   
481   C CA  . GLY A 85   ? 0.5472 0.5619 0.5635 0.0288  -0.0124 -0.0708 83   GLY A CA  
482   C C   . GLY A 85   ? 0.5757 0.5951 0.5902 0.0299  -0.0106 -0.0699 83   GLY A C   
483   O O   . GLY A 85   ? 0.5311 0.5576 0.5457 0.0325  -0.0110 -0.0745 83   GLY A O   
484   N N   . VAL A 86   ? 0.5740 0.5896 0.5869 0.0277  -0.0086 -0.0640 84   VAL A N   
485   C CA  . VAL A 86   ? 0.5230 0.5421 0.5345 0.0285  -0.0070 -0.0628 84   VAL A CA  
486   C C   . VAL A 86   ? 0.4619 0.4785 0.4764 0.0318  -0.0091 -0.0672 84   VAL A C   
487   O O   . VAL A 86   ? 0.4375 0.4606 0.4515 0.0337  -0.0086 -0.0694 84   VAL A O   
488   C CB  . VAL A 86   ? 0.5252 0.5392 0.5351 0.0257  -0.0049 -0.0560 84   VAL A CB  
489   N N   . GLU A 87   ? 0.5070 0.5146 0.5249 0.0325  -0.0117 -0.0685 85   GLU A N   
490   C CA  . GLU A 87   ? 0.4890 0.4932 0.5100 0.0357  -0.0140 -0.0724 85   GLU A CA  
491   C C   . GLU A 87   ? 0.4909 0.5027 0.5132 0.0391  -0.0157 -0.0797 85   GLU A C   
492   O O   . GLU A 87   ? 0.5033 0.5174 0.5269 0.0421  -0.0166 -0.0831 85   GLU A O   
493   C CB  . GLU A 87   ? 0.6164 0.6088 0.6407 0.0354  -0.0165 -0.0717 85   GLU A CB  
494   N N   . GLY A 88   ? 0.4849 0.5012 0.5069 0.0389  -0.0161 -0.0825 86   GLY A N   
495   C CA  . GLY A 88   ? 0.4360 0.4608 0.4588 0.0422  -0.0175 -0.0896 86   GLY A CA  
496   C C   . GLY A 88   ? 0.4520 0.4888 0.4717 0.0428  -0.0150 -0.0899 86   GLY A C   
497   O O   . GLY A 88   ? 0.3808 0.4243 0.4016 0.0462  -0.0159 -0.0954 86   GLY A O   
498   N N   . LEU A 89   ? 0.4077 0.4474 0.4237 0.0396  -0.0118 -0.0840 87   LEU A N   
499   C CA  . LEU A 89   ? 0.4068 0.4573 0.4199 0.0397  -0.0093 -0.0833 87   LEU A CA  
500   C C   . LEU A 89   ? 0.3572 0.4068 0.3716 0.0415  -0.0092 -0.0835 87   LEU A C   
501   O O   . LEU A 89   ? 0.3623 0.4207 0.3769 0.0440  -0.0091 -0.0875 87   LEU A O   
502   C CB  . LEU A 89   ? 0.4011 0.4531 0.4105 0.0356  -0.0063 -0.0764 87   LEU A CB  
503   C CG  . LEU A 89   ? 0.4471 0.5099 0.4532 0.0346  -0.0035 -0.0743 87   LEU A CG  
504   C CD1 . LEU A 89   ? 0.5000 0.5747 0.5058 0.0371  -0.0039 -0.0802 87   LEU A CD1 
505   C CD2 . LEU A 89   ? 0.4722 0.5353 0.4752 0.0307  -0.0014 -0.0681 87   LEU A CD2 
506   N N   . VAL A 90   ? 0.3794 0.4187 0.3948 0.0403  -0.0094 -0.0794 88   VAL A N   
507   C CA  . VAL A 90   ? 0.3650 0.4022 0.3818 0.0421  -0.0097 -0.0795 88   VAL A CA  
508   C C   . VAL A 90   ? 0.4044 0.4426 0.4246 0.0465  -0.0126 -0.0867 88   VAL A C   
509   O O   . VAL A 90   ? 0.3911 0.4349 0.4120 0.0489  -0.0124 -0.0892 88   VAL A O   
510   C CB  . VAL A 90   ? 0.3246 0.3496 0.3420 0.0402  -0.0099 -0.0742 88   VAL A CB  
511   C CG1 . VAL A 90   ? 0.3629 0.3845 0.3823 0.0425  -0.0110 -0.0751 88   VAL A CG1 
512   C CG2 . VAL A 90   ? 0.3572 0.3824 0.3712 0.0362  -0.0069 -0.0675 88   VAL A CG2 
513   N N   . GLN A 91   ? 0.4126 0.4454 0.4355 0.0478  -0.0154 -0.0903 89   GLN A N   
514   C CA  . GLN A 91   ? 0.4114 0.4446 0.4380 0.0522  -0.0186 -0.0975 89   GLN A CA  
515   C C   . GLN A 91   ? 0.4037 0.4507 0.4295 0.0546  -0.0181 -0.1032 89   GLN A C   
516   O O   . GLN A 91   ? 0.3967 0.4484 0.4241 0.0581  -0.0190 -0.1078 89   GLN A O   
517   C CB  . GLN A 91   ? 0.4355 0.4596 0.4653 0.0525  -0.0218 -0.0998 89   GLN A CB  
518   N N   . GLU A 92   ? 0.3876 0.4414 0.4107 0.0528  -0.0166 -0.1030 90   GLU A N   
519   C CA  . GLU A 92   ? 0.4236 0.4907 0.4458 0.0551  -0.0164 -0.1087 90   GLU A CA  
520   C C   . GLU A 92   ? 0.3728 0.4500 0.3932 0.0557  -0.0139 -0.1081 90   GLU A C   
521   O O   . GLU A 92   ? 0.3613 0.4478 0.3828 0.0592  -0.0145 -0.1141 90   GLU A O   
522   C CB  . GLU A 92   ? 0.4294 0.5020 0.4487 0.0527  -0.0151 -0.1076 90   GLU A CB  
523   C CG  . GLU A 92   ? 0.4723 0.5594 0.4902 0.0548  -0.0147 -0.1132 90   GLU A CG  
524   C CD  . GLU A 92   ? 0.5342 0.6269 0.5487 0.0521  -0.0132 -0.1112 90   GLU A CD  
525   O OE1 . GLU A 92   ? 0.5332 0.6179 0.5469 0.0489  -0.0129 -0.1060 90   GLU A OE1 
526   O OE2 . GLU A 92   ? 0.5034 0.6090 0.5160 0.0533  -0.0125 -0.1146 90   GLU A OE2 
527   N N   . TYR A 93   ? 0.3537 0.4293 0.3717 0.0525  -0.0112 -0.1011 91   TYR A N   
528   C CA  . TYR A 93   ? 0.3216 0.4068 0.3381 0.0525  -0.0088 -0.0999 91   TYR A CA  
529   C C   . TYR A 93   ? 0.3153 0.3943 0.3337 0.0535  -0.0092 -0.0984 91   TYR A C   
530   O O   . TYR A 93   ? 0.3484 0.4337 0.3655 0.0529  -0.0071 -0.0963 91   TYR A O   
531   C CB  . TYR A 93   ? 0.3240 0.4139 0.3361 0.0481  -0.0053 -0.0934 91   TYR A CB  
532   C CG  . TYR A 93   ? 0.3598 0.4597 0.3696 0.0477  -0.0046 -0.0955 91   TYR A CG  
533   C CD1 . TYR A 93   ? 0.3069 0.4213 0.3156 0.0491  -0.0034 -0.0988 91   TYR A CD1 
534   C CD2 . TYR A 93   ? 0.3486 0.4441 0.3577 0.0459  -0.0053 -0.0944 91   TYR A CD2 
535   C CE1 . TYR A 93   ? 0.3565 0.4806 0.3629 0.0488  -0.0028 -0.1008 91   TYR A CE1 
536   C CE2 . TYR A 93   ? 0.4158 0.5206 0.4227 0.0457  -0.0048 -0.0964 91   TYR A CE2 
537   C CZ  . TYR A 93   ? 0.3919 0.5110 0.3974 0.0472  -0.0036 -0.0996 91   TYR A CZ  
538   O OH  . TYR A 93   ? 0.4345 0.5633 0.4376 0.0470  -0.0031 -0.1014 91   TYR A OH  
539   N N   . SER A 94   ? 0.3022 0.3694 0.3237 0.0550  -0.0120 -0.0994 92   SER A N   
540   C CA  . SER A 94   ? 0.3230 0.3839 0.3465 0.0563  -0.0128 -0.0983 92   SER A CA  
541   C C   . SER A 94   ? 0.2969 0.3567 0.3177 0.0527  -0.0099 -0.0910 92   SER A C   
542   O O   . SER A 94   ? 0.3153 0.3780 0.3364 0.0536  -0.0092 -0.0904 92   SER A O   
543   C CB  . SER A 94   ? 0.3915 0.4605 0.4174 0.0608  -0.0140 -0.1046 92   SER A CB  
544   O OG  . SER A 94   ? 0.4367 0.5069 0.4652 0.0643  -0.0169 -0.1119 92   SER A OG  
545   N N   . LEU A 95   ? 0.2872 0.3429 0.3055 0.0488  -0.0083 -0.0855 93   LEU A N   
546   C CA  . LEU A 95   ? 0.3041 0.3587 0.3197 0.0452  -0.0056 -0.0787 93   LEU A CA  
547   C C   . LEU A 95   ? 0.2971 0.3403 0.3142 0.0451  -0.0067 -0.0756 93   LEU A C   
548   O O   . LEU A 95   ? 0.2769 0.3103 0.2959 0.0457  -0.0089 -0.0760 93   LEU A O   
549   C CB  . LEU A 95   ? 0.2633 0.3174 0.2760 0.0413  -0.0038 -0.0741 93   LEU A CB  
550   C CG  . LEU A 95   ? 0.2925 0.3577 0.3034 0.0411  -0.0028 -0.0765 93   LEU A CG  
551   C CD1 . LEU A 95   ? 0.3344 0.3982 0.3423 0.0370  -0.0011 -0.0712 93   LEU A CD1 
552   C CD2 . LEU A 95   ? 0.2582 0.3359 0.2682 0.0419  -0.0011 -0.0779 93   LEU A CD2 
553   N N   . SER A 96   ? 0.2573 0.3018 0.2735 0.0442  -0.0051 -0.0724 94   SER A N   
554   C CA  . SER A 96   ? 0.2957 0.3300 0.3122 0.0431  -0.0054 -0.0679 94   SER A CA  
555   C C   . SER A 96   ? 0.2622 0.2911 0.2763 0.0391  -0.0040 -0.0623 94   SER A C   
556   O O   . SER A 96   ? 0.2691 0.3030 0.2811 0.0370  -0.0024 -0.0613 94   SER A O   
557   C CB  . SER A 96   ? 0.2443 0.2824 0.2602 0.0430  -0.0040 -0.0660 94   SER A CB  
558   O OG  . SER A 96   ? 0.2428 0.2872 0.2557 0.0397  -0.0011 -0.0623 94   SER A OG  
559   N N   . SER A 97   ? 0.2605 0.2793 0.2748 0.0380  -0.0045 -0.0585 95   SER A N   
560   C CA  . SER A 97   ? 0.3102 0.3239 0.3223 0.0343  -0.0030 -0.0530 95   SER A CA  
561   C C   . SER A 97   ? 0.2693 0.2896 0.2784 0.0316  0.0000  -0.0495 95   SER A C   
562   O O   . SER A 97   ? 0.2590 0.2806 0.2663 0.0291  0.0013  -0.0472 95   SER A O   
563   C CB  . SER A 97   ? 0.3524 0.3556 0.3652 0.0338  -0.0038 -0.0495 95   SER A CB  
564   O OG  . SER A 97   ? 0.4401 0.4360 0.4553 0.0353  -0.0064 -0.0516 95   SER A OG  
565   N N   . GLN A 98   ? 0.2296 0.2541 0.2385 0.0319  0.0009  -0.0489 96   GLN A N   
566   C CA  . GLN A 98   ? 0.2293 0.2597 0.2357 0.0291  0.0035  -0.0454 96   GLN A CA  
567   C C   . GLN A 98   ? 0.2303 0.2706 0.2356 0.0286  0.0046  -0.0472 96   GLN A C   
568   O O   . GLN A 98   ? 0.2168 0.2598 0.2199 0.0257  0.0064  -0.0438 96   GLN A O   
569   C CB  . GLN A 98   ? 0.2254 0.2588 0.2322 0.0296  0.0041  -0.0448 96   GLN A CB  
570   C CG  . GLN A 98   ? 0.2513 0.2756 0.2581 0.0291  0.0037  -0.0413 96   GLN A CG  
571   C CD  . GLN A 98   ? 0.2542 0.2743 0.2589 0.0255  0.0053  -0.0360 96   GLN A CD  
572   O OE1 . GLN A 98   ? 0.2931 0.3075 0.2973 0.0245  0.0049  -0.0348 96   GLN A OE1 
573   N NE2 . GLN A 98   ? 0.2502 0.2734 0.2536 0.0235  0.0070  -0.0329 96   GLN A NE2 
574   N N   . GLU A 99   ? 0.2251 0.2713 0.2320 0.0316  0.0034  -0.0527 97   GLU A N   
575   C CA  . GLU A 99   ? 0.2216 0.2777 0.2273 0.0314  0.0043  -0.0549 97   GLU A CA  
576   C C   . GLU A 99   ? 0.2358 0.2887 0.2404 0.0298  0.0041  -0.0538 97   GLU A C   
577   O O   . GLU A 99   ? 0.2247 0.2835 0.2270 0.0276  0.0057  -0.0519 97   GLU A O   
578   C CB  . GLU A 99   ? 0.2246 0.2871 0.2325 0.0354  0.0027  -0.0617 97   GLU A CB  
579   C CG  . GLU A 99   ? 0.2241 0.2935 0.2328 0.0367  0.0034  -0.0629 97   GLU A CG  
580   C CD  . GLU A 99   ? 0.2274 0.3017 0.2388 0.0412  0.0015  -0.0698 97   GLU A CD  
581   O OE1 . GLU A 99   ? 0.2441 0.3159 0.2568 0.0433  -0.0005 -0.0739 97   GLU A OE1 
582   O OE2 . GLU A 99   ? 0.2492 0.3298 0.2616 0.0426  0.0019  -0.0714 97   GLU A OE2 
583   N N   . GLY A 100  ? 0.2319 0.2755 0.2380 0.0307  0.0022  -0.0547 98   GLY A N   
584   C CA  . GLY A 100  ? 0.2238 0.2641 0.2291 0.0290  0.0020  -0.0536 98   GLY A CA  
585   C C   . GLY A 100  ? 0.2368 0.2747 0.2395 0.0252  0.0040  -0.0473 98   GLY A C   
586   O O   . GLY A 100  ? 0.2371 0.2785 0.2381 0.0234  0.0049  -0.0458 98   GLY A O   
587   N N   . VAL A 101  ? 0.2189 0.2509 0.2215 0.0241  0.0046  -0.0435 99   VAL A N   
588   C CA  . VAL A 101  ? 0.2306 0.2604 0.2311 0.0207  0.0064  -0.0378 99   VAL A CA  
589   C C   . VAL A 101  ? 0.2483 0.2877 0.2468 0.0191  0.0083  -0.0363 99   VAL A C   
590   O O   . VAL A 101  ? 0.2184 0.2593 0.2150 0.0166  0.0094  -0.0333 99   VAL A O   
591   C CB  . VAL A 101  ? 0.2276 0.2502 0.2285 0.0203  0.0065  -0.0347 99   VAL A CB  
592   C CG1 . VAL A 101  ? 0.2238 0.2450 0.2227 0.0170  0.0083  -0.0293 99   VAL A CG1 
593   C CG2 . VAL A 101  ? 0.2607 0.2738 0.2635 0.0215  0.0046  -0.0355 99   VAL A CG2 
594   N N   . ALA A 102  ? 0.2142 0.2605 0.2131 0.0203  0.0088  -0.0382 100  ALA A N   
595   C CA  . ALA A 102  ? 0.2127 0.2686 0.2099 0.0185  0.0106  -0.0364 100  ALA A CA  
596   C C   . ALA A 102  ? 0.2247 0.2877 0.2205 0.0182  0.0109  -0.0379 100  ALA A C   
597   O O   . ALA A 102  ? 0.2125 0.2800 0.2063 0.0155  0.0124  -0.0344 100  ALA A O   
598   C CB  . ALA A 102  ? 0.2150 0.2776 0.2133 0.0201  0.0109  -0.0387 100  ALA A CB  
599   N N   . LEU A 103  ? 0.2162 0.2807 0.2133 0.0209  0.0093  -0.0431 101  LEU A N   
600   C CA  . LEU A 103  ? 0.2174 0.2887 0.2133 0.0210  0.0093  -0.0450 101  LEU A CA  
601   C C   . LEU A 103  ? 0.2361 0.3023 0.2304 0.0184  0.0095  -0.0412 101  LEU A C   
602   O O   . LEU A 103  ? 0.2440 0.3165 0.2362 0.0167  0.0105  -0.0395 101  LEU A O   
603   C CB  . LEU A 103  ? 0.2262 0.2981 0.2241 0.0246  0.0072  -0.0516 101  LEU A CB  
604   C CG  . LEU A 103  ? 0.2223 0.3005 0.2191 0.0249  0.0068  -0.0543 101  LEU A CG  
605   C CD1 . LEU A 103  ? 0.2219 0.3134 0.2166 0.0242  0.0086  -0.0541 101  LEU A CD1 
606   C CD2 . LEU A 103  ? 0.2299 0.3070 0.2292 0.0286  0.0043  -0.0610 101  LEU A CD2 
607   N N   . MET A 104  ? 0.2396 0.2950 0.2350 0.0182  0.0085  -0.0399 102  MET A N   
608   C CA  . MET A 104  ? 0.2803 0.3311 0.2746 0.0159  0.0087  -0.0365 102  MET A CA  
609   C C   . MET A 104  ? 0.2655 0.3173 0.2576 0.0127  0.0106  -0.0306 102  MET A C   
610   O O   . MET A 104  ? 0.2867 0.3400 0.2772 0.0108  0.0111  -0.0281 102  MET A O   
611   C CB  . MET A 104  ? 0.2536 0.2931 0.2497 0.0163  0.0073  -0.0362 102  MET A CB  
612   C CG  . MET A 104  ? 0.2583 0.2958 0.2568 0.0191  0.0051  -0.0417 102  MET A CG  
613   S SD  . MET A 104  ? 0.3991 0.4449 0.3970 0.0201  0.0043  -0.0460 102  MET A SD  
614   C CE  . MET A 104  ? 0.3826 0.4239 0.3793 0.0172  0.0046  -0.0418 102  MET A CE  
615   N N   . CYS A 105  ? 0.2268 0.2777 0.2191 0.0122  0.0115  -0.0285 103  CYS A N   
616   C CA  . CYS A 105  ? 0.2847 0.3370 0.2754 0.0092  0.0131  -0.0233 103  CYS A CA  
617   C C   . CYS A 105  ? 0.3219 0.3851 0.3108 0.0081  0.0142  -0.0228 103  CYS A C   
618   O O   . CYS A 105  ? 0.2969 0.3613 0.2841 0.0055  0.0150  -0.0187 103  CYS A O   
619   C CB  . CYS A 105  ? 0.2732 0.3230 0.2647 0.0089  0.0137  -0.0217 103  CYS A CB  
620   S SG  . CYS A 105  ? 0.2653 0.3027 0.2583 0.0096  0.0127  -0.0210 103  CYS A SG  
621   N N   . LEU A 106  ? 0.2645 0.3360 0.2539 0.0100  0.0142  -0.0269 104  LEU A N   
622   C CA  . LEU A 106  ? 0.2683 0.3512 0.2559 0.0091  0.0152  -0.0268 104  LEU A CA  
623   C C   . LEU A 106  ? 0.3046 0.3889 0.2906 0.0086  0.0147  -0.0268 104  LEU A C   
624   O O   . LEU A 106  ? 0.3236 0.4131 0.3075 0.0063  0.0157  -0.0233 104  LEU A O   
625   C CB  . LEU A 106  ? 0.2526 0.3441 0.2412 0.0118  0.0150  -0.0320 104  LEU A CB  
626   C CG  . LEU A 106  ? 0.2670 0.3715 0.2537 0.0113  0.0160  -0.0327 104  LEU A CG  
627   C CD1 . LEU A 106  ? 0.2975 0.4067 0.2826 0.0077  0.0179  -0.0269 104  LEU A CD1 
628   C CD2 . LEU A 106  ? 0.2863 0.3994 0.2741 0.0145  0.0157  -0.0388 104  LEU A CD2 
629   N N   . ALA A 107  ? 0.2343 0.3142 0.2215 0.0108  0.0131  -0.0306 105  ALA A N   
630   C CA  . ALA A 107  ? 0.3240 0.4055 0.3100 0.0106  0.0124  -0.0312 105  ALA A CA  
631   C C   . ALA A 107  ? 0.3752 0.4513 0.3599 0.0077  0.0129  -0.0256 105  ALA A C   
632   O O   . ALA A 107  ? 0.3426 0.4236 0.3252 0.0062  0.0133  -0.0236 105  ALA A O   
633   C CB  . ALA A 107  ? 0.2760 0.3527 0.2640 0.0133  0.0104  -0.0364 105  ALA A CB  
634   N N   . GLU A 108  ? 0.3449 0.4111 0.3307 0.0069  0.0129  -0.0230 106  GLU A N   
635   C CA  . GLU A 108  ? 0.3535 0.4144 0.3384 0.0043  0.0133  -0.0177 106  GLU A CA  
636   C C   . GLU A 108  ? 0.4089 0.4761 0.3917 0.0017  0.0147  -0.0133 106  GLU A C   
637   O O   . GLU A 108  ? 0.3854 0.4538 0.3668 0.0000  0.0148  -0.0101 106  GLU A O   
638   C CB  . GLU A 108  ? 0.3401 0.3907 0.3265 0.0040  0.0132  -0.0159 106  GLU A CB  
639   C CG  . GLU A 108  ? 0.4151 0.4606 0.4008 0.0015  0.0138  -0.0106 106  GLU A CG  
640   C CD  . GLU A 108  ? 0.4726 0.5103 0.4595 0.0012  0.0140  -0.0087 106  GLU A CD  
641   O OE1 . GLU A 108  ? 0.4266 0.4613 0.4151 0.0031  0.0135  -0.0116 106  GLU A OE1 
642   O OE2 . GLU A 108  ? 0.4917 0.5264 0.4780 -0.0008 0.0146  -0.0045 106  GLU A OE2 
643   N N   . ALA A 109  ? 0.3519 0.4234 0.3350 0.0015  0.0157  -0.0129 107  ALA A N   
644   C CA  . ALA A 109  ? 0.4329 0.5104 0.4144 -0.0012 0.0169  -0.0086 107  ALA A CA  
645   C C   . ALA A 109  ? 0.4432 0.5309 0.4226 -0.0016 0.0172  -0.0090 107  ALA A C   
646   O O   . ALA A 109  ? 0.4086 0.4985 0.3862 -0.0040 0.0175  -0.0046 107  ALA A O   
647   C CB  . ALA A 109  ? 0.4293 0.5101 0.4117 -0.0013 0.0178  -0.0088 107  ALA A CB  
648   N N   . LEU A 110  ? 0.3628 0.4570 0.3423 0.0009  0.0168  -0.0143 108  LEU A N   
649   C CA  . LEU A 110  ? 0.3865 0.4911 0.3639 0.0010  0.0169  -0.0153 108  LEU A CA  
650   C C   . LEU A 110  ? 0.4267 0.5283 0.4028 0.0003  0.0160  -0.0138 108  LEU A C   
651   O O   . LEU A 110  ? 0.4478 0.5567 0.4216 -0.0010 0.0163  -0.0118 108  LEU A O   
652   C CB  . LEU A 110  ? 0.3229 0.4338 0.3010 0.0043  0.0163  -0.0222 108  LEU A CB  
653   C CG  . LEU A 110  ? 0.3695 0.4874 0.3484 0.0049  0.0174  -0.0236 108  LEU A CG  
654   C CD1 . LEU A 110  ? 0.3216 0.4428 0.3020 0.0088  0.0165  -0.0309 108  LEU A CD1 
655   C CD2 . LEU A 110  ? 0.4034 0.5331 0.3799 0.0026  0.0190  -0.0204 108  LEU A CD2 
656   N N   . LEU A 111  ? 0.4675 0.5589 0.4451 0.0011  0.0149  -0.0147 109  LEU A N   
657   C CA  . LEU A 111  ? 0.4719 0.5602 0.4488 0.0005  0.0140  -0.0132 109  LEU A CA  
658   C C   . LEU A 111  ? 0.4892 0.5740 0.4650 -0.0026 0.0145  -0.0066 109  LEU A C   
659   O O   . LEU A 111  ? 0.5338 0.6182 0.5085 -0.0034 0.0139  -0.0047 109  LEU A O   
660   C CB  . LEU A 111  ? 0.4162 0.4952 0.3953 0.0023  0.0126  -0.0164 109  LEU A CB  
661   C CG  . LEU A 111  ? 0.4045 0.4873 0.3845 0.0053  0.0115  -0.0231 109  LEU A CG  
662   C CD1 . LEU A 111  ? 0.4122 0.4854 0.3950 0.0068  0.0101  -0.0260 109  LEU A CD1 
663   C CD2 . LEU A 111  ? 0.4283 0.5197 0.4064 0.0056  0.0110  -0.0248 109  LEU A CD2 
664   N N   . ARG A 112  ? 0.5019 0.5843 0.4782 -0.0041 0.0155  -0.0032 110  ARG A N   
665   C CA  . ARG A 112  ? 0.5135 0.5941 0.4888 -0.0070 0.0159  0.0029  110  ARG A CA  
666   C C   . ARG A 112  ? 0.5941 0.6850 0.5669 -0.0087 0.0165  0.0056  110  ARG A C   
667   O O   . ARG A 112  ? 0.6222 0.7122 0.5941 -0.0112 0.0165  0.0110  110  ARG A O   
668   C CB  . ARG A 112  ? 0.5325 0.6078 0.5091 -0.0082 0.0166  0.0056  110  ARG A CB  
669   C CG  . ARG A 112  ? 0.5079 0.5725 0.4867 -0.0070 0.0160  0.0041  110  ARG A CG  
670   C CD  . ARG A 112  ? 0.6010 0.6598 0.5808 -0.0086 0.0165  0.0076  110  ARG A CD  
671   N NE  . ARG A 112  ? 0.6461 0.7076 0.6268 -0.0082 0.0173  0.0063  110  ARG A NE  
672   C CZ  . ARG A 112  ? 0.6820 0.7389 0.6643 -0.0064 0.0172  0.0033  110  ARG A CZ  
673   N NH1 . ARG A 112  ? 0.6623 0.7119 0.6455 -0.0048 0.0163  0.0013  110  ARG A NH1 
674   N NH2 . ARG A 112  ? 0.6287 0.6886 0.6117 -0.0063 0.0178  0.0025  110  ARG A NH2 
675   N N   . ILE A 113  ? 0.5849 0.6857 0.5566 -0.0075 0.0168  0.0021  111  ILE A N   
676   C CA  . ILE A 113  ? 0.5698 0.6816 0.5389 -0.0089 0.0173  0.0042  111  ILE A CA  
677   C C   . ILE A 113  ? 0.6468 0.7599 0.6145 -0.0080 0.0161  0.0030  111  ILE A C   
678   O O   . ILE A 113  ? 0.6499 0.7642 0.6181 -0.0053 0.0154  -0.0028 111  ILE A O   
679   C CB  . ILE A 113  ? 0.5806 0.7033 0.5492 -0.0078 0.0183  0.0008  111  ILE A CB  
680   C CG1 . ILE A 113  ? 0.5274 0.6497 0.4975 -0.0091 0.0195  0.0027  111  ILE A CG1 
681   C CG2 . ILE A 113  ? 0.6026 0.7378 0.5683 -0.0089 0.0188  0.0024  111  ILE A CG2 
682   C CD1 . ILE A 113  ? 0.4203 0.5526 0.3905 -0.0077 0.0204  -0.0012 111  ILE A CD1 
683   N N   . PRO A 114  ? 0.6884 0.8014 0.6545 -0.0101 0.0157  0.0079  112  PRO A N   
684   C CA  . PRO A 114  ? 0.6747 0.7877 0.6397 -0.0091 0.0144  0.0066  112  PRO A CA  
685   C C   . PRO A 114  ? 0.6469 0.7719 0.6097 -0.0079 0.0143  0.0033  112  PRO A C   
686   O O   . PRO A 114  ? 0.6706 0.7955 0.6336 -0.0057 0.0132  -0.0012 112  PRO A O   
687   C CB  . PRO A 114  ? 0.7464 0.8561 0.7105 -0.0118 0.0140  0.0134  112  PRO A CB  
688   C CG  . PRO A 114  ? 0.7069 0.8106 0.6725 -0.0136 0.0148  0.0172  112  PRO A CG  
689   C CD  . PRO A 114  ? 0.7097 0.8198 0.6755 -0.0132 0.0161  0.0148  112  PRO A CD  
690   N N   . ASP A 115  ? 0.6501 0.7856 0.6108 -0.0092 0.0155  0.0053  113  ASP A N   
691   C CA  . ASP A 115  ? 0.6394 0.7875 0.5975 -0.0082 0.0155  0.0027  113  ASP A CA  
692   C C   . ASP A 115  ? 0.6393 0.7924 0.5985 -0.0052 0.0157  -0.0046 113  ASP A C   
693   O O   . ASP A 115  ? 0.6541 0.8102 0.6141 -0.0053 0.0170  -0.0052 113  ASP A O   
694   C CB  . ASP A 115  ? 0.6079 0.7658 0.5632 -0.0111 0.0166  0.0083  113  ASP A CB  
695   N N   . THR A 116  ? 0.5733 0.7274 0.5325 -0.0025 0.0144  -0.0103 114  THR A N   
696   C CA  . THR A 116  ? 0.5958 0.7530 0.5566 0.0008  0.0142  -0.0179 114  THR A CA  
697   C C   . THR A 116  ? 0.6400 0.8108 0.5992 0.0010  0.0156  -0.0193 114  THR A C   
698   O O   . THR A 116  ? 0.6312 0.8029 0.5922 0.0024  0.0163  -0.0225 114  THR A O   
699   C CB  . THR A 116  ? 0.5959 0.7532 0.5568 0.0033  0.0123  -0.0234 114  THR A CB  
700   O OG1 . THR A 116  ? 0.5905 0.7345 0.5538 0.0035  0.0110  -0.0233 114  THR A OG1 
701   C CG2 . THR A 116  ? 0.5729 0.7360 0.5350 0.0068  0.0119  -0.0314 114  THR A CG2 
702   N N   . ALA A 117  ? 0.6054 0.7874 0.5612 -0.0002 0.0161  -0.0168 115  ALA A N   
703   C CA  . ALA A 117  ? 0.5851 0.7811 0.5391 -0.0003 0.0176  -0.0177 115  ALA A CA  
704   C C   . ALA A 117  ? 0.5767 0.7718 0.5319 -0.0026 0.0194  -0.0134 115  ALA A C   
705   O O   . ALA A 117  ? 0.6312 0.8337 0.5870 -0.0015 0.0205  -0.0163 115  ALA A O   
706   C CB  . ALA A 117  ? 0.5612 0.7690 0.5112 -0.0018 0.0179  -0.0145 115  ALA A CB  
707   N N   . THR A 118  ? 0.5928 0.7787 0.5484 -0.0056 0.0195  -0.0067 116  THR A N   
708   C CA  . THR A 118  ? 0.5945 0.7783 0.5515 -0.0079 0.0209  -0.0026 116  THR A CA  
709   C C   . THR A 118  ? 0.5992 0.7762 0.5597 -0.0055 0.0208  -0.0075 116  THR A C   
710   O O   . THR A 118  ? 0.5423 0.7238 0.5039 -0.0057 0.0221  -0.0080 116  THR A O   
711   C CB  . THR A 118  ? 0.6151 0.7894 0.5723 -0.0112 0.0206  0.0049  116  THR A CB  
712   O OG1 . THR A 118  ? 0.6723 0.8519 0.6263 -0.0131 0.0203  0.0092  116  THR A OG1 
713   C CG2 . THR A 118  ? 0.5420 0.7156 0.5003 -0.0139 0.0220  0.0095  116  THR A CG2 
714   N N   . ARG A 119  ? 0.5748 0.7411 0.5371 -0.0033 0.0193  -0.0110 117  ARG A N   
715   C CA  . ARG A 119  ? 0.5937 0.7530 0.5593 -0.0010 0.0190  -0.0155 117  ARG A CA  
716   C C   . ARG A 119  ? 0.5465 0.7150 0.5126 0.0023  0.0190  -0.0226 117  ARG A C   
717   O O   . ARG A 119  ? 0.5215 0.6907 0.4896 0.0034  0.0196  -0.0248 117  ARG A O   
718   C CB  . ARG A 119  ? 0.5504 0.6967 0.5176 0.0003  0.0173  -0.0171 117  ARG A CB  
719   C CG  . ARG A 119  ? 0.4912 0.6287 0.4618 0.0026  0.0167  -0.0211 117  ARG A CG  
720   C CD  . ARG A 119  ? 0.4489 0.5771 0.4207 0.0042  0.0148  -0.0238 117  ARG A CD  
721   N NE  . ARG A 119  ? 0.5275 0.6504 0.4981 0.0018  0.0145  -0.0186 117  ARG A NE  
722   C CZ  . ARG A 119  ? 0.5417 0.6630 0.5118 0.0024  0.0132  -0.0197 117  ARG A CZ  
723   N NH1 . ARG A 119  ? 0.5149 0.6394 0.4855 0.0051  0.0120  -0.0259 117  ARG A NH1 
724   N NH2 . ARG A 119  ? 0.6848 0.8013 0.6540 0.0002  0.0130  -0.0147 117  ARG A NH2 
725   N N   . ASP A 120  ? 0.5655 0.7416 0.5300 0.0041  0.0183  -0.0265 118  ASP A N   
726   C CA  . ASP A 120  ? 0.5431 0.7284 0.5081 0.0076  0.0181  -0.0339 118  ASP A CA  
727   C C   . ASP A 120  ? 0.5434 0.7415 0.5074 0.0066  0.0201  -0.0327 118  ASP A C   
728   O O   . ASP A 120  ? 0.5102 0.7131 0.4758 0.0091  0.0203  -0.0379 118  ASP A O   
729   C CB  . ASP A 120  ? 0.5429 0.7340 0.5061 0.0095  0.0168  -0.0381 118  ASP A CB  
730   C CG  . ASP A 120  ? 0.6234 0.8024 0.5882 0.0107  0.0147  -0.0400 118  ASP A CG  
731   O OD1 . ASP A 120  ? 0.5548 0.7216 0.5225 0.0108  0.0142  -0.0396 118  ASP A OD1 
732   O OD2 . ASP A 120  ? 0.6757 0.8575 0.6391 0.0114  0.0135  -0.0419 118  ASP A OD2 
733   N N   . ALA A 121  ? 0.5417 0.7455 0.5030 0.0029  0.0215  -0.0259 119  ALA A N   
734   C CA  . ALA A 121  ? 0.5528 0.7685 0.5133 0.0013  0.0235  -0.0239 119  ALA A CA  
735   C C   . ALA A 121  ? 0.5058 0.7154 0.4694 0.0006  0.0243  -0.0226 119  ALA A C   
736   O O   . ALA A 121  ? 0.4905 0.7085 0.4551 0.0015  0.0254  -0.0250 119  ALA A O   
737   C CB  . ALA A 121  ? 0.5643 0.7864 0.5216 -0.0028 0.0246  -0.0163 119  ALA A CB  
738   N N   . LEU A 122  ? 0.5157 0.7111 0.4807 -0.0009 0.0236  -0.0188 120  LEU A N   
739   C CA  . LEU A 122  ? 0.4943 0.6833 0.4621 -0.0016 0.0242  -0.0176 120  LEU A CA  
740   C C   . LEU A 122  ? 0.4624 0.6498 0.4330 0.0026  0.0235  -0.0251 120  LEU A C   
741   O O   . LEU A 122  ? 0.4415 0.6324 0.4139 0.0030  0.0243  -0.0263 120  LEU A O   
742   C CB  . LEU A 122  ? 0.4868 0.6608 0.4555 -0.0036 0.0235  -0.0128 120  LEU A CB  
743   C CG  . LEU A 122  ? 0.5372 0.7062 0.5081 -0.0054 0.0243  -0.0096 120  LEU A CG  
744   C CD1 . LEU A 122  ? 0.4997 0.6791 0.4695 -0.0088 0.0260  -0.0046 120  LEU A CD1 
745   C CD2 . LEU A 122  ? 0.5246 0.6788 0.4964 -0.0069 0.0234  -0.0057 120  LEU A CD2 
746   N N   . ILE A 123  ? 0.4756 0.6578 0.4468 0.0057  0.0217  -0.0303 121  ILE A N   
747   C CA  . ILE A 123  ? 0.4449 0.6247 0.4188 0.0098  0.0206  -0.0374 121  ILE A CA  
748   C C   . ILE A 123  ? 0.4938 0.6884 0.4677 0.0120  0.0214  -0.0423 121  ILE A C   
749   O O   . ILE A 123  ? 0.3954 0.5918 0.3716 0.0134  0.0218  -0.0448 121  ILE A O   
750   C CB  . ILE A 123  ? 0.4257 0.5977 0.4003 0.0124  0.0184  -0.0417 121  ILE A CB  
751   C CG1 . ILE A 123  ? 0.4268 0.5839 0.4021 0.0105  0.0177  -0.0372 121  ILE A CG1 
752   C CG2 . ILE A 123  ? 0.4203 0.5914 0.3977 0.0168  0.0170  -0.0495 121  ILE A CG2 
753   C CD1 . ILE A 123  ? 0.4003 0.5503 0.3760 0.0122  0.0157  -0.0402 121  ILE A CD1 
754   N N   . ARG A 124  ? 0.4880 0.6940 0.4592 0.0122  0.0217  -0.0436 122  ARG A N   
755   C CA  . ARG A 124  ? 0.5128 0.7338 0.4838 0.0146  0.0223  -0.0490 122  ARG A CA  
756   C C   . ARG A 124  ? 0.5004 0.7306 0.4715 0.0123  0.0246  -0.0454 122  ARG A C   
757   O O   . ARG A 124  ? 0.5036 0.7415 0.4764 0.0147  0.0251  -0.0501 122  ARG A O   
758   C CB  . ARG A 124  ? 0.4320 0.6635 0.3998 0.0150  0.0222  -0.0505 122  ARG A CB  
759   N N   . ASP A 125  ? 0.4834 0.7129 0.4527 0.0077  0.0260  -0.0373 123  ASP A N   
760   C CA  . ASP A 125  ? 0.5106 0.7507 0.4797 0.0049  0.0282  -0.0333 123  ASP A CA  
761   C C   . ASP A 125  ? 0.4851 0.7169 0.4569 0.0032  0.0286  -0.0301 123  ASP A C   
762   O O   . ASP A 125  ? 0.5848 0.8255 0.5576 0.0021  0.0302  -0.0293 123  ASP A O   
763   C CB  . ASP A 125  ? 0.6004 0.8466 0.5659 0.0005  0.0293  -0.0261 123  ASP A CB  
764   C CG  . ASP A 125  ? 0.5927 0.8483 0.5550 0.0020  0.0289  -0.0288 123  ASP A CG  
765   O OD1 . ASP A 125  ? 0.5680 0.8325 0.5306 0.0058  0.0287  -0.0361 123  ASP A OD1 
766   O OD2 . ASP A 125  ? 0.6576 0.9119 0.6172 -0.0006 0.0288  -0.0237 123  ASP A OD2 
767   N N   . LYS A 126  ? 0.4375 0.6534 0.4107 0.0029  0.0274  -0.0283 124  LYS A N   
768   C CA  . LYS A 126  ? 0.5102 0.7186 0.4857 0.0010  0.0278  -0.0249 124  LYS A CA  
769   C C   . LYS A 126  ? 0.4858 0.6820 0.4643 0.0043  0.0262  -0.0293 124  LYS A C   
770   O O   . LYS A 126  ? 0.4853 0.6813 0.4663 0.0053  0.0265  -0.0310 124  LYS A O   
771   C CB  . LYS A 126  ? 0.5292 0.7303 0.5035 -0.0036 0.0281  -0.0166 124  LYS A CB  
772   N N   . ILE A 127  ? 0.4513 0.6373 0.4296 0.0059  0.0245  -0.0310 125  ILE A N   
773   C CA  . ILE A 127  ? 0.4359 0.6092 0.4169 0.0084  0.0230  -0.0341 125  ILE A CA  
774   C C   . ILE A 127  ? 0.4574 0.6355 0.4405 0.0129  0.0222  -0.0419 125  ILE A C   
775   O O   . ILE A 127  ? 0.4885 0.6628 0.4742 0.0144  0.0219  -0.0437 125  ILE A O   
776   C CB  . ILE A 127  ? 0.4399 0.6017 0.4202 0.0087  0.0214  -0.0336 125  ILE A CB  
777   C CG1 . ILE A 127  ? 0.4648 0.6234 0.4429 0.0045  0.0221  -0.0262 125  ILE A CG1 
778   C CG2 . ILE A 127  ? 0.4193 0.5678 0.4023 0.0106  0.0200  -0.0356 125  ILE A CG2 
779   C CD1 . ILE A 127  ? 0.4685 0.6215 0.4475 0.0014  0.0230  -0.0205 125  ILE A CD1 
780   N N   . ALA A 128  ? 0.4124 0.5988 0.3945 0.0154  0.0217  -0.0468 126  ALA A N   
781   C CA  . ALA A 128  ? 0.4116 0.6026 0.3958 0.0200  0.0206  -0.0548 126  ALA A CA  
782   C C   . ALA A 128  ? 0.4772 0.6785 0.4629 0.0206  0.0220  -0.0561 126  ALA A C   
783   O O   . ALA A 128  ? 0.4610 0.6643 0.4492 0.0245  0.0209  -0.0624 126  ALA A O   
784   C CB  . ALA A 128  ? 0.3797 0.5792 0.3624 0.0223  0.0199  -0.0596 126  ALA A CB  
785   N N   . ASP A 129  ? 0.4712 0.6789 0.4556 0.0166  0.0241  -0.0503 127  ASP A N   
786   C CA  . ASP A 129  ? 0.5088 0.7266 0.4947 0.0165  0.0256  -0.0508 127  ASP A CA  
787   C C   . ASP A 129  ? 0.5342 0.7429 0.5224 0.0151  0.0257  -0.0474 127  ASP A C   
788   O O   . ASP A 129  ? 0.5619 0.7781 0.5514 0.0140  0.0270  -0.0464 127  ASP A O   
789   C CB  . ASP A 129  ? 0.5670 0.7990 0.5503 0.0130  0.0279  -0.0465 127  ASP A CB  
790   N N   . GLY A 130  ? 0.5551 0.7482 0.5439 0.0149  0.0243  -0.0458 128  GLY A N   
791   C CA  . GLY A 130  ? 0.5348 0.7186 0.5257 0.0140  0.0241  -0.0432 128  GLY A CA  
792   C C   . GLY A 130  ? 0.5926 0.7715 0.5823 0.0090  0.0252  -0.0352 128  GLY A C   
793   O O   . GLY A 130  ? 0.5528 0.7209 0.5438 0.0082  0.0247  -0.0328 128  GLY A O   
794   N N   . ASN A 131  ? 0.6189 0.8054 0.6061 0.0057  0.0266  -0.0309 129  ASN A N   
795   C CA  . ASN A 131  ? 0.6271 0.8092 0.6132 0.0009  0.0274  -0.0232 129  ASN A CA  
796   C C   . ASN A 131  ? 0.6448 0.8148 0.6295 0.0003  0.0262  -0.0210 129  ASN A C   
797   O O   . ASN A 131  ? 0.6730 0.8454 0.6552 -0.0010 0.0264  -0.0189 129  ASN A O   
798   C CB  . ASN A 131  ? 0.6176 0.8130 0.6019 -0.0025 0.0293  -0.0194 129  ASN A CB  
799   N N   . TRP A 132  ? 0.6225 0.7794 0.6088 0.0015  0.0250  -0.0214 130  TRP A N   
800   C CA  . TRP A 132  ? 0.6099 0.7548 0.5953 0.0011  0.0239  -0.0195 130  TRP A CA  
801   C C   . TRP A 132  ? 0.6470 0.7825 0.6326 -0.0022 0.0240  -0.0135 130  TRP A C   
802   O O   . TRP A 132  ? 0.6885 0.8165 0.6729 -0.0035 0.0235  -0.0105 130  TRP A O   
803   C CB  . TRP A 132  ? 0.5835 0.7202 0.5703 0.0051  0.0221  -0.0250 130  TRP A CB  
804   C CG  . TRP A 132  ? 0.4960 0.6280 0.4855 0.0071  0.0216  -0.0273 130  TRP A CG  
805   C CD1 . TRP A 132  ? 0.4208 0.5587 0.4122 0.0103  0.0213  -0.0327 130  TRP A CD1 
806   C CD2 . TRP A 132  ? 0.3931 0.5138 0.3838 0.0061  0.0212  -0.0245 130  TRP A CD2 
807   N NE1 . TRP A 132  ? 0.4265 0.5572 0.4201 0.0113  0.0207  -0.0331 130  TRP A NE1 
808   C CE2 . TRP A 132  ? 0.3871 0.5074 0.3802 0.0088  0.0206  -0.0282 130  TRP A CE2 
809   C CE3 . TRP A 132  ? 0.4422 0.5535 0.4322 0.0035  0.0211  -0.0194 130  TRP A CE3 
810   C CZ2 . TRP A 132  ? 0.3535 0.4645 0.3481 0.0087  0.0201  -0.0267 130  TRP A CZ2 
811   C CZ3 . TRP A 132  ? 0.3911 0.4933 0.3826 0.0034  0.0206  -0.0182 130  TRP A CZ3 
812   C CH2 . TRP A 132  ? 0.3453 0.4474 0.3389 0.0060  0.0201  -0.0218 130  TRP A CH2 
813   N N   . LYS A 133  ? 0.7164 0.8522 0.7037 -0.0033 0.0246  -0.0120 131  LYS A N   
814   C CA  . LYS A 133  ? 0.7601 0.8872 0.7480 -0.0063 0.0246  -0.0068 131  LYS A CA  
815   C C   . LYS A 133  ? 0.8140 0.9457 0.8005 -0.0106 0.0256  -0.0007 131  LYS A C   
816   O O   . LYS A 133  ? 0.8765 1.0001 0.8625 -0.0129 0.0252  0.0037  131  LYS A O   
817   C CB  . LYS A 133  ? 0.7351 0.8608 0.7255 -0.0059 0.0247  -0.0076 131  LYS A CB  
818   N N   . SER A 134  ? 0.8760 1.0207 0.8618 -0.0117 0.0268  -0.0004 132  SER A N   
819   C CA  . SER A 134  ? 0.8670 1.0169 0.8517 -0.0161 0.0277  0.0057  132  SER A CA  
820   C C   . SER A 134  ? 0.8823 1.0303 0.8642 -0.0170 0.0272  0.0082  132  SER A C   
821   O O   . SER A 134  ? 0.8805 1.0285 0.8615 -0.0207 0.0275  0.0141  132  SER A O   
822   C CB  . SER A 134  ? 0.8629 1.0282 0.8475 -0.0170 0.0292  0.0052  132  SER A CB  
823   N N   . HIS A 135  ? 0.8762 1.0223 0.8570 -0.0138 0.0265  0.0040  133  HIS A N   
824   C CA  . HIS A 135  ? 0.8301 0.9759 0.8084 -0.0144 0.0260  0.0057  133  HIS A CA  
825   C C   . HIS A 135  ? 0.8508 0.9828 0.8291 -0.0138 0.0246  0.0064  133  HIS A C   
826   O O   . HIS A 135  ? 0.8729 1.0036 0.8494 -0.0146 0.0241  0.0087  133  HIS A O   
827   C CB  . HIS A 135  ? 0.7655 0.9205 0.7423 -0.0115 0.0261  0.0005  133  HIS A CB  
828   N N   . LEU A 136  ? 0.8254 0.9477 0.8058 -0.0123 0.0240  0.0047  134  LEU A N   
829   C CA  . LEU A 136  ? 0.8154 0.9254 0.7959 -0.0114 0.0227  0.0049  134  LEU A CA  
830   C C   . LEU A 136  ? 0.8212 0.9210 0.8036 -0.0124 0.0224  0.0071  134  LEU A C   
831   O O   . LEU A 136  ? 0.8474 0.9485 0.8314 -0.0125 0.0229  0.0066  134  LEU A O   
832   C CB  . LEU A 136  ? 0.7379 0.8458 0.7188 -0.0075 0.0218  -0.0013 134  LEU A CB  
833   C CG  . LEU A 136  ? 0.6110 0.7272 0.5901 -0.0060 0.0217  -0.0043 134  LEU A CG  
834   C CD1 . LEU A 136  ? 0.5285 0.6443 0.5088 -0.0020 0.0209  -0.0112 134  LEU A CD1 
835   C CD2 . LEU A 136  ? 0.6282 0.7406 0.6056 -0.0071 0.0210  -0.0016 134  LEU A CD2 
836   N N   . ARG A 140  ? 0.3691 0.4277 0.3566 -0.0174 0.0201  0.0186  138  ARG A N   
837   C CA  . ARG A 140  ? 0.4071 0.4587 0.3949 -0.0144 0.0196  0.0152  138  ARG A CA  
838   C C   . ARG A 140  ? 0.4363 0.4925 0.4242 -0.0116 0.0198  0.0102  138  ARG A C   
839   O O   . ARG A 140  ? 0.4301 0.4944 0.4171 -0.0112 0.0203  0.0087  138  ARG A O   
840   C CB  . ARG A 140  ? 0.4557 0.5025 0.4423 -0.0140 0.0189  0.0159  138  ARG A CB  
841   N N   . SER A 141  ? 0.3924 0.4435 0.3816 -0.0096 0.0195  0.0076  139  SER A N   
842   C CA  . SER A 141  ? 0.3813 0.4353 0.3709 -0.0066 0.0194  0.0028  139  SER A CA  
843   C C   . SER A 141  ? 0.3665 0.4215 0.3551 -0.0049 0.0189  0.0002  139  SER A C   
844   O O   . SER A 141  ? 0.3106 0.3600 0.2986 -0.0051 0.0184  0.0014  139  SER A O   
845   C CB  . SER A 141  ? 0.3498 0.3964 0.3407 -0.0048 0.0187  0.0011  139  SER A CB  
846   O OG  . SER A 141  ? 0.3254 0.3733 0.3169 -0.0017 0.0183  -0.0035 139  SER A OG  
847   N N   . LEU A 142  ? 0.3240 0.3866 0.3128 -0.0031 0.0191  -0.0034 140  LEU A N   
848   C CA  . LEU A 142  ? 0.2993 0.3624 0.2876 -0.0010 0.0184  -0.0069 140  LEU A CA  
849   C C   . LEU A 142  ? 0.2860 0.3392 0.2752 0.0010  0.0172  -0.0087 140  LEU A C   
850   O O   . LEU A 142  ? 0.2794 0.3305 0.2682 0.0020  0.0165  -0.0102 140  LEU A O   
851   C CB  . LEU A 142  ? 0.3021 0.3743 0.2908 0.0011  0.0185  -0.0113 140  LEU A CB  
852   C CG  . LEU A 142  ? 0.3585 0.4380 0.3459 0.0017  0.0185  -0.0133 140  LEU A CG  
853   C CD1 . LEU A 142  ? 0.4366 0.5229 0.4222 -0.0015 0.0196  -0.0090 140  LEU A CD1 
854   C CD2 . LEU A 142  ? 0.3717 0.4585 0.3600 0.0046  0.0183  -0.0187 140  LEU A CD2 
855   N N   . PHE A 143  ? 0.2561 0.3035 0.2464 0.0015  0.0170  -0.0084 141  PHE A N   
856   C CA  . PHE A 143  ? 0.2576 0.2970 0.2490 0.0036  0.0159  -0.0106 141  PHE A CA  
857   C C   . PHE A 143  ? 0.2709 0.3012 0.2621 0.0024  0.0158  -0.0073 141  PHE A C   
858   O O   . PHE A 143  ? 0.2695 0.2931 0.2616 0.0037  0.0151  -0.0081 141  PHE A O   
859   C CB  . PHE A 143  ? 0.2667 0.3069 0.2596 0.0056  0.0156  -0.0132 141  PHE A CB  
860   C CG  . PHE A 143  ? 0.2441 0.2942 0.2373 0.0068  0.0159  -0.0164 141  PHE A CG  
861   C CD1 . PHE A 143  ? 0.2061 0.2595 0.1994 0.0089  0.0152  -0.0203 141  PHE A CD1 
862   C CD2 . PHE A 143  ? 0.2442 0.3009 0.2377 0.0059  0.0168  -0.0156 141  PHE A CD2 
863   C CE1 . PHE A 143  ? 0.2341 0.2974 0.2278 0.0101  0.0154  -0.0235 141  PHE A CE1 
864   C CE2 . PHE A 143  ? 0.2388 0.3055 0.2328 0.0070  0.0172  -0.0186 141  PHE A CE2 
865   C CZ  . PHE A 143  ? 0.2468 0.3170 0.2408 0.0092  0.0165  -0.0226 141  PHE A CZ  
866   N N   . VAL A 144  ? 0.2827 0.3128 0.2727 -0.0001 0.0164  -0.0036 142  VAL A N   
867   C CA  . VAL A 144  ? 0.2917 0.3137 0.2817 -0.0011 0.0162  -0.0007 142  VAL A CA  
868   C C   . VAL A 144  ? 0.2801 0.2958 0.2704 0.0003  0.0154  -0.0022 142  VAL A C   
869   O O   . VAL A 144  ? 0.3348 0.3437 0.3256 0.0005  0.0152  -0.0011 142  VAL A O   
870   C CB  . VAL A 144  ? 0.2917 0.3147 0.2807 -0.0038 0.0167  0.0033  142  VAL A CB  
871   C CG1 . VAL A 144  ? 0.3410 0.3688 0.3300 -0.0056 0.0174  0.0054  142  VAL A CG1 
872   C CG2 . VAL A 144  ? 0.3313 0.3586 0.3192 -0.0040 0.0166  0.0028  142  VAL A CG2 
873   N N   . ASN A 145  ? 0.2730 0.2913 0.2633 0.0014  0.0149  -0.0048 143  ASN A N   
874   C CA  . ASN A 145  ? 0.2920 0.3047 0.2830 0.0026  0.0140  -0.0062 143  ASN A CA  
875   C C   . ASN A 145  ? 0.3193 0.3312 0.3117 0.0052  0.0130  -0.0103 143  ASN A C   
876   O O   . ASN A 145  ? 0.2885 0.2974 0.2817 0.0062  0.0120  -0.0122 143  ASN A O   
877   C CB  . ASN A 145  ? 0.3846 0.3994 0.3748 0.0019  0.0138  -0.0060 143  ASN A CB  
878   C CG  . ASN A 145  ? 0.3857 0.3988 0.3749 -0.0003 0.0144  -0.0019 143  ASN A CG  
879   O OD1 . ASN A 145  ? 0.4336 0.4406 0.4232 -0.0009 0.0145  0.0002  143  ASN A OD1 
880   N ND2 . ASN A 145  ? 0.3649 0.3838 0.3530 -0.0016 0.0147  -0.0006 143  ASN A ND2 
881   N N   . ALA A 146  ? 0.2658 0.2802 0.2586 0.0062  0.0131  -0.0116 144  ALA A N   
882   C CA  . ALA A 146  ? 0.2957 0.3099 0.2901 0.0088  0.0120  -0.0156 144  ALA A CA  
883   C C   . ALA A 146  ? 0.2724 0.2778 0.2679 0.0098  0.0109  -0.0157 144  ALA A C   
884   O O   . ALA A 146  ? 0.3005 0.3042 0.2974 0.0118  0.0096  -0.0188 144  ALA A O   
885   C CB  . ALA A 146  ? 0.2399 0.2584 0.2347 0.0097  0.0123  -0.0166 144  ALA A CB  
886   N N   . ALA A 147  ? 0.2912 0.2910 0.2862 0.0084  0.0115  -0.0122 145  ALA A N   
887   C CA  . ALA A 147  ? 0.3214 0.3134 0.3172 0.0090  0.0106  -0.0118 145  ALA A CA  
888   C C   . ALA A 147  ? 0.3215 0.3111 0.3181 0.0091  0.0097  -0.0130 145  ALA A C   
889   O O   . ALA A 147  ? 0.3487 0.3340 0.3468 0.0105  0.0085  -0.0146 145  ALA A O   
890   C CB  . ALA A 147  ? 0.3290 0.3165 0.3239 0.0074  0.0115  -0.0079 145  ALA A CB  
891   N N   . THR A 148  ? 0.2919 0.2846 0.2876 0.0078  0.0103  -0.0122 146  THR A N   
892   C CA  . THR A 148  ? 0.2855 0.2770 0.2820 0.0078  0.0094  -0.0135 146  THR A CA  
893   C C   . THR A 148  ? 0.2930 0.2877 0.2908 0.0099  0.0081  -0.0181 146  THR A C   
894   O O   . THR A 148  ? 0.2919 0.2826 0.2915 0.0109  0.0067  -0.0201 146  THR A O   
895   C CB  . THR A 148  ? 0.3896 0.3844 0.3847 0.0060  0.0103  -0.0115 146  THR A CB  
896   O OG1 . THR A 148  ? 0.4234 0.4149 0.4176 0.0043  0.0113  -0.0075 146  THR A OG1 
897   C CG2 . THR A 148  ? 0.3556 0.3494 0.3515 0.0059  0.0094  -0.0128 146  THR A CG2 
898   N N   . TRP A 149  ? 0.2685 0.2706 0.2656 0.0105  0.0085  -0.0198 147  TRP A N   
899   C CA  . TRP A 149  ? 0.2752 0.2812 0.2735 0.0128  0.0073  -0.0246 147  TRP A CA  
900   C C   . TRP A 149  ? 0.2647 0.2663 0.2650 0.0150  0.0059  -0.0268 147  TRP A C   
901   O O   . TRP A 149  ? 0.3111 0.3117 0.3132 0.0169  0.0042  -0.0306 147  TRP A O   
902   C CB  . TRP A 149  ? 0.2817 0.2973 0.2786 0.0130  0.0082  -0.0258 147  TRP A CB  
903   C CG  . TRP A 149  ? 0.2946 0.3149 0.2898 0.0111  0.0091  -0.0241 147  TRP A CG  
904   C CD1 . TRP A 149  ? 0.2991 0.3231 0.2923 0.0089  0.0107  -0.0205 147  TRP A CD1 
905   C CD2 . TRP A 149  ? 0.3077 0.3291 0.3029 0.0112  0.0083  -0.0258 147  TRP A CD2 
906   N NE1 . TRP A 149  ? 0.3313 0.3589 0.3233 0.0078  0.0109  -0.0197 147  TRP A NE1 
907   C CE2 . TRP A 149  ? 0.3504 0.3766 0.3434 0.0091  0.0095  -0.0230 147  TRP A CE2 
908   C CE3 . TRP A 149  ? 0.3276 0.3465 0.3246 0.0127  0.0065  -0.0294 147  TRP A CE3 
909   C CZ2 . TRP A 149  ? 0.3692 0.3980 0.3617 0.0087  0.0090  -0.0237 147  TRP A CZ2 
910   C CZ3 . TRP A 149  ? 0.4045 0.4260 0.4011 0.0122  0.0061  -0.0303 147  TRP A CZ3 
911   C CH2 . TRP A 149  ? 0.3875 0.4139 0.3817 0.0103  0.0073  -0.0275 147  TRP A CH2 
912   N N   . GLY A 150  ? 0.2590 0.2577 0.2590 0.0148  0.0065  -0.0246 148  GLY A N   
913   C CA  . GLY A 150  ? 0.2662 0.2600 0.2680 0.0168  0.0051  -0.0261 148  GLY A CA  
914   C C   . GLY A 150  ? 0.3321 0.3181 0.3354 0.0169  0.0037  -0.0260 148  GLY A C   
915   O O   . GLY A 150  ? 0.3308 0.3141 0.3363 0.0189  0.0017  -0.0290 148  GLY A O   
916   N N   . LEU A 151  ? 0.3165 0.2989 0.3189 0.0146  0.0045  -0.0225 149  LEU A N   
917   C CA  . LEU A 151  ? 0.3376 0.3134 0.3417 0.0142  0.0033  -0.0221 149  LEU A CA  
918   C C   . LEU A 151  ? 0.3162 0.2937 0.3219 0.0152  0.0018  -0.0260 149  LEU A C   
919   O O   . LEU A 151  ? 0.3740 0.3468 0.3821 0.0164  -0.0002 -0.0280 149  LEU A O   
920   C CB  . LEU A 151  ? 0.3609 0.3341 0.3637 0.0117  0.0047  -0.0179 149  LEU A CB  
921   C CG  . LEU A 151  ? 0.4232 0.3894 0.4274 0.0108  0.0039  -0.0162 149  LEU A CG  
922   C CD1 . LEU A 151  ? 0.4139 0.3748 0.4193 0.0120  0.0028  -0.0160 149  LEU A CD1 
923   C CD2 . LEU A 151  ? 0.4216 0.3865 0.4243 0.0085  0.0056  -0.0121 149  LEU A CD2 
924   N N   . VAL A 152  ? 0.3241 0.3083 0.3286 0.0149  0.0025  -0.0273 150  VAL A N   
925   C CA  . VAL A 152  ? 0.3249 0.3119 0.3308 0.0159  0.0010  -0.0314 150  VAL A CA  
926   C C   . VAL A 152  ? 0.3652 0.3529 0.3731 0.0189  -0.0008 -0.0361 150  VAL A C   
927   O O   . VAL A 152  ? 0.3497 0.3342 0.3601 0.0201  -0.0030 -0.0391 150  VAL A O   
928   C CB  . VAL A 152  ? 0.3510 0.3461 0.3547 0.0151  0.0022  -0.0316 150  VAL A CB  
929   C CG1 . VAL A 152  ? 0.3927 0.3922 0.3976 0.0167  0.0007  -0.0367 150  VAL A CG1 
930   C CG2 . VAL A 152  ? 0.3132 0.3069 0.3156 0.0124  0.0035  -0.0275 150  VAL A CG2 
931   N N   . VAL A 153  ? 0.3164 0.3084 0.3235 0.0202  -0.0002 -0.0368 151  VAL A N   
932   C CA  . VAL A 153  ? 0.3342 0.3286 0.3431 0.0233  -0.0019 -0.0418 151  VAL A CA  
933   C C   . VAL A 153  ? 0.3484 0.3347 0.3597 0.0247  -0.0037 -0.0420 151  VAL A C   
934   O O   . VAL A 153  ? 0.3801 0.3644 0.3941 0.0270  -0.0061 -0.0461 151  VAL A O   
935   C CB  . VAL A 153  ? 0.2945 0.2974 0.3018 0.0241  -0.0004 -0.0426 151  VAL A CB  
936   C CG1 . VAL A 153  ? 0.3192 0.3245 0.3287 0.0275  -0.0021 -0.0477 151  VAL A CG1 
937   C CG2 . VAL A 153  ? 0.2915 0.3029 0.2968 0.0228  0.0010  -0.0428 151  VAL A CG2 
938   N N   . THR A 154  ? 0.3368 0.3185 0.3472 0.0235  -0.0027 -0.0377 152  THR A N   
939   C CA  . THR A 154  ? 0.3652 0.3402 0.3774 0.0249  -0.0043 -0.0375 152  THR A CA  
940   C C   . THR A 154  ? 0.3862 0.3523 0.3991 0.0232  -0.0048 -0.0339 152  THR A C   
941   O O   . THR A 154  ? 0.4211 0.3812 0.4358 0.0243  -0.0065 -0.0337 152  THR A O   
942   C CB  . THR A 154  ? 0.3463 0.3231 0.3570 0.0253  -0.0031 -0.0356 152  THR A CB  
943   O OG1 . THR A 154  ? 0.3652 0.3404 0.3736 0.0225  -0.0010 -0.0305 152  THR A OG1 
944   C CG2 . THR A 154  ? 0.3748 0.3613 0.3848 0.0265  -0.0022 -0.0386 152  THR A CG2 
945   N N   . GLY A 155  ? 0.3548 0.3203 0.3664 0.0205  -0.0035 -0.0310 153  GLY A N   
946   C CA  . GLY A 155  ? 0.3683 0.3265 0.3804 0.0187  -0.0036 -0.0272 153  GLY A CA  
947   C C   . GLY A 155  ? 0.4430 0.3986 0.4533 0.0178  -0.0023 -0.0230 153  GLY A C   
948   O O   . GLY A 155  ? 0.4534 0.4032 0.4641 0.0165  -0.0023 -0.0198 153  GLY A O   
949   N N   . LYS A 156  ? 0.3498 0.3099 0.3585 0.0186  -0.0011 -0.0230 154  LYS A N   
950   C CA  . LYS A 156  ? 0.4020 0.3602 0.4090 0.0179  0.0001  -0.0195 154  LYS A CA  
951   C C   . LYS A 156  ? 0.3885 0.3514 0.3929 0.0160  0.0025  -0.0172 154  LYS A C   
952   O O   . LYS A 156  ? 0.3351 0.3041 0.3389 0.0160  0.0033  -0.0190 154  LYS A O   
953   C CB  . LYS A 156  ? 0.3865 0.3454 0.3941 0.0204  -0.0009 -0.0212 154  LYS A CB  
954   N N   . LEU A 157  ? 0.4306 0.3906 0.4336 0.0145  0.0037  -0.0134 155  LEU A N   
955   C CA  . LEU A 157  ? 0.4467 0.4099 0.4475 0.0127  0.0058  -0.0110 155  LEU A CA  
956   C C   . LEU A 157  ? 0.4781 0.4424 0.4778 0.0132  0.0064  -0.0099 155  LEU A C   
957   O O   . LEU A 157  ? 0.4654 0.4256 0.4652 0.0140  0.0057  -0.0089 155  LEU A O   
958   C CB  . LEU A 157  ? 0.4539 0.4135 0.4542 0.0106  0.0066  -0.0077 155  LEU A CB  
959   C CG  . LEU A 157  ? 0.5172 0.4794 0.5155 0.0088  0.0085  -0.0053 155  LEU A CG  
960   C CD1 . LEU A 157  ? 0.4260 0.3940 0.4239 0.0084  0.0089  -0.0068 155  LEU A CD1 
961   C CD2 . LEU A 157  ? 0.5880 0.5464 0.5861 0.0072  0.0090  -0.0025 155  LEU A CD2 
962   N N   . THR A 158  ? 0.4338 0.4037 0.4323 0.0127  0.0076  -0.0100 156  THR A N   
963   C CA  . THR A 158  ? 0.4472 0.4184 0.4446 0.0124  0.0084  -0.0084 156  THR A CA  
964   C C   . THR A 158  ? 0.4022 0.3748 0.3980 0.0101  0.0101  -0.0057 156  THR A C   
965   O O   . THR A 158  ? 0.4233 0.3981 0.4189 0.0090  0.0105  -0.0057 156  THR A O   
966   C CB  . THR A 158  ? 0.4773 0.4543 0.4751 0.0138  0.0083  -0.0110 156  THR A CB  
967   O OG1 . THR A 158  ? 0.5176 0.5005 0.5152 0.0131  0.0089  -0.0123 156  THR A OG1 
968   C CG2 . THR A 158  ? 0.4843 0.4599 0.4838 0.0165  0.0064  -0.0140 156  THR A CG2 
969   N N   . SER A 159  ? 0.3482 0.3192 0.3429 0.0095  0.0107  -0.0035 157  SER A N   
970   C CA  . SER A 159  ? 0.3813 0.3535 0.3749 0.0074  0.0120  -0.0011 157  SER A CA  
971   C C   . SER A 159  ? 0.3857 0.3640 0.3791 0.0068  0.0126  -0.0017 157  SER A C   
972   O O   . SER A 159  ? 0.4328 0.4133 0.4257 0.0051  0.0133  -0.0005 157  SER A O   
973   C CB  . SER A 159  ? 0.4390 0.4077 0.4317 0.0070  0.0124  0.0012  157  SER A CB  
974   O OG  . SER A 159  ? 0.5129 0.4831 0.5055 0.0079  0.0121  0.0006  157  SER A OG  
975   N N   . THR A 160  ? 0.3359 0.3174 0.3299 0.0080  0.0122  -0.0035 158  THR A N   
976   C CA  . THR A 160  ? 0.3069 0.2949 0.3008 0.0073  0.0128  -0.0040 158  THR A CA  
977   C C   . THR A 160  ? 0.3262 0.3189 0.3212 0.0091  0.0122  -0.0074 158  THR A C   
978   O O   . THR A 160  ? 0.3678 0.3580 0.3636 0.0111  0.0111  -0.0094 158  THR A O   
979   C CB  . THR A 160  ? 0.3250 0.3137 0.3187 0.0069  0.0132  -0.0028 158  THR A CB  
980   O OG1 . THR A 160  ? 0.3458 0.3327 0.3401 0.0089  0.0122  -0.0043 158  THR A OG1 
981   C CG2 . THR A 160  ? 0.3936 0.3782 0.3864 0.0053  0.0137  0.0001  158  THR A CG2 
982   N N   . VAL A 161  ? 0.2627 0.2622 0.2576 0.0083  0.0129  -0.0078 159  VAL A N   
983   C CA  . VAL A 161  ? 0.2672 0.2729 0.2628 0.0095  0.0127  -0.0109 159  VAL A CA  
984   C C   . VAL A 161  ? 0.2616 0.2727 0.2580 0.0102  0.0128  -0.0123 159  VAL A C   
985   O O   . VAL A 161  ? 0.2358 0.2492 0.2319 0.0085  0.0136  -0.0102 159  VAL A O   
986   C CB  . VAL A 161  ? 0.2649 0.2750 0.2596 0.0075  0.0136  -0.0098 159  VAL A CB  
987   C CG1 . VAL A 161  ? 0.2803 0.2989 0.2754 0.0082  0.0137  -0.0124 159  VAL A CG1 
988   C CG2 . VAL A 161  ? 0.3782 0.3836 0.3725 0.0073  0.0132  -0.0094 159  VAL A CG2 
989   N N   . ASN A 162  ? 0.2427 0.2558 0.2405 0.0129  0.0118  -0.0159 160  ASN A N   
990   C CA  . ASN A 162  ? 0.2523 0.2718 0.2510 0.0138  0.0119  -0.0176 160  ASN A CA  
991   C C   . ASN A 162  ? 0.2248 0.2534 0.2233 0.0130  0.0128  -0.0187 160  ASN A C   
992   O O   . ASN A 162  ? 0.2073 0.2400 0.2066 0.0149  0.0122  -0.0223 160  ASN A O   
993   C CB  . ASN A 162  ? 0.2510 0.2691 0.2513 0.0171  0.0103  -0.0210 160  ASN A CB  
994   C CG  . ASN A 162  ? 0.2421 0.2672 0.2437 0.0181  0.0104  -0.0228 160  ASN A CG  
995   O OD1 . ASN A 162  ? 0.2067 0.2393 0.2081 0.0166  0.0116  -0.0224 160  ASN A OD1 
996   N ND2 . ASN A 162  ? 0.2826 0.3052 0.2855 0.0207  0.0090  -0.0247 160  ASN A ND2 
997   N N   . ASP A 163  ? 0.2226 0.2546 0.2202 0.0101  0.0141  -0.0156 161  ASP A N   
998   C CA  . ASP A 163  ? 0.2026 0.2432 0.1997 0.0088  0.0151  -0.0159 161  ASP A CA  
999   C C   . ASP A 163  ? 0.2031 0.2527 0.2015 0.0102  0.0153  -0.0188 161  ASP A C   
1000  O O   . ASP A 163  ? 0.2153 0.2728 0.2136 0.0103  0.0158  -0.0205 161  ASP A O   
1001  C CB  . ASP A 163  ? 0.2365 0.2777 0.2324 0.0052  0.0163  -0.0114 161  ASP A CB  
1002  C CG  . ASP A 163  ? 0.2893 0.3282 0.2857 0.0038  0.0165  -0.0089 161  ASP A CG  
1003  O OD1 . ASP A 163  ? 0.2454 0.2785 0.2424 0.0052  0.0158  -0.0094 161  ASP A OD1 
1004  O OD2 . ASP A 163  ? 0.2858 0.3288 0.2821 0.0011  0.0174  -0.0062 161  ASP A OD2 
1005  N N   . ARG A 164  ? 0.2052 0.2546 0.2050 0.0113  0.0149  -0.0196 162  ARG A N   
1006  C CA  . ARG A 164  ? 0.2035 0.2618 0.2047 0.0128  0.0150  -0.0227 162  ARG A CA  
1007  C C   . ARG A 164  ? 0.2054 0.2647 0.2077 0.0165  0.0137  -0.0277 162  ARG A C   
1008  O O   . ARG A 164  ? 0.2062 0.2744 0.2091 0.0177  0.0140  -0.0307 162  ARG A O   
1009  C CB  . ARG A 164  ? 0.2122 0.2702 0.2148 0.0130  0.0148  -0.0223 162  ARG A CB  
1010  C CG  . ARG A 164  ? 0.2233 0.2821 0.2255 0.0093  0.0159  -0.0180 162  ARG A CG  
1011  C CD  . ARG A 164  ? 0.3436 0.4098 0.3449 0.0064  0.0174  -0.0160 162  ARG A CD  
1012  N NE  . ARG A 164  ? 0.3513 0.4285 0.3535 0.0074  0.0179  -0.0189 162  ARG A NE  
1013  C CZ  . ARG A 164  ? 0.3746 0.4588 0.3758 0.0060  0.0189  -0.0184 162  ARG A CZ  
1014  N NH1 . ARG A 164  ? 0.3991 0.4802 0.3985 0.0035  0.0194  -0.0150 162  ARG A NH1 
1015  N NH2 . ARG A 164  ? 0.3232 0.4181 0.3253 0.0071  0.0194  -0.0214 162  ARG A NH2 
1016  N N   . SER A 165  ? 0.2067 0.2570 0.2093 0.0185  0.0122  -0.0286 163  SER A N   
1017  C CA  . SER A 165  ? 0.2296 0.2792 0.2334 0.0218  0.0107  -0.0331 163  SER A CA  
1018  C C   . SER A 165  ? 0.2151 0.2686 0.2180 0.0214  0.0110  -0.0343 163  SER A C   
1019  O O   . SER A 165  ? 0.2110 0.2702 0.2148 0.0238  0.0104  -0.0387 163  SER A O   
1020  C CB  . SER A 165  ? 0.2158 0.2542 0.2199 0.0232  0.0090  -0.0327 163  SER A CB  
1021  O OG  . SER A 165  ? 0.2675 0.3043 0.2728 0.0261  0.0074  -0.0367 163  SER A OG  
1022  N N   . LEU A 166  ? 0.2081 0.2582 0.2091 0.0187  0.0119  -0.0307 164  LEU A N   
1023  C CA  . LEU A 166  ? 0.2087 0.2622 0.2086 0.0182  0.0122  -0.0315 164  LEU A CA  
1024  C C   . LEU A 166  ? 0.2085 0.2741 0.2079 0.0173  0.0135  -0.0323 164  LEU A C   
1025  O O   . LEU A 166  ? 0.2099 0.2814 0.2092 0.0186  0.0133  -0.0355 164  LEU A O   
1026  C CB  . LEU A 166  ? 0.2075 0.2549 0.2056 0.0153  0.0127  -0.0272 164  LEU A CB  
1027  C CG  . LEU A 166  ? 0.2146 0.2512 0.2133 0.0163  0.0114  -0.0270 164  LEU A CG  
1028  C CD1 . LEU A 166  ? 0.2332 0.2647 0.2302 0.0135  0.0122  -0.0226 164  LEU A CD1 
1029  C CD2 . LEU A 166  ? 0.2225 0.2582 0.2223 0.0189  0.0098  -0.0313 164  LEU A CD2 
1030  N N   . ALA A 167  ? 0.2069 0.2765 0.2060 0.0151  0.0149  -0.0293 165  ALA A N   
1031  C CA  . ALA A 167  ? 0.2069 0.2886 0.2057 0.0140  0.0162  -0.0295 165  ALA A CA  
1032  C C   . ALA A 167  ? 0.2084 0.2976 0.2090 0.0173  0.0157  -0.0350 165  ALA A C   
1033  O O   . ALA A 167  ? 0.2094 0.3082 0.2097 0.0179  0.0162  -0.0374 165  ALA A O   
1034  C CB  . ALA A 167  ? 0.2052 0.2890 0.2038 0.0107  0.0176  -0.0251 165  ALA A CB  
1035  N N   . ALA A 168  ? 0.2086 0.2941 0.2112 0.0197  0.0146  -0.0370 166  ALA A N   
1036  C CA  . ALA A 168  ? 0.2186 0.3104 0.2232 0.0234  0.0137  -0.0426 166  ALA A CA  
1037  C C   . ALA A 168  ? 0.2127 0.3042 0.2174 0.0261  0.0123  -0.0469 166  ALA A C   
1038  O O   . ALA A 168  ? 0.2141 0.3152 0.2195 0.0280  0.0124  -0.0511 166  ALA A O   
1039  C CB  . ALA A 168  ? 0.2106 0.2967 0.2172 0.0255  0.0123  -0.0437 166  ALA A CB  
1040  N N   . ALA A 169  ? 0.2132 0.2941 0.2175 0.0262  0.0111  -0.0461 167  ALA A N   
1041  C CA  . ALA A 169  ? 0.2156 0.2950 0.2205 0.0288  0.0095  -0.0503 167  ALA A CA  
1042  C C   . ALA A 169  ? 0.2159 0.3035 0.2190 0.0276  0.0106  -0.0508 167  ALA A C   
1043  O O   . ALA A 169  ? 0.2181 0.3111 0.2220 0.0302  0.0097  -0.0558 167  ALA A O   
1044  C CB  . ALA A 169  ? 0.2161 0.2823 0.2210 0.0286  0.0082  -0.0486 167  ALA A CB  
1045  N N   . LEU A 170  ? 0.2138 0.3027 0.2146 0.0238  0.0124  -0.0458 168  LEU A N   
1046  C CA  . LEU A 170  ? 0.2142 0.3109 0.2130 0.0224  0.0134  -0.0457 168  LEU A CA  
1047  C C   . LEU A 170  ? 0.2150 0.3257 0.2140 0.0233  0.0144  -0.0485 168  LEU A C   
1048  O O   . LEU A 170  ? 0.2168 0.3349 0.2155 0.0249  0.0142  -0.0523 168  LEU A O   
1049  C CB  . LEU A 170  ? 0.2122 0.3065 0.2087 0.0181  0.0149  -0.0392 168  LEU A CB  
1050  C CG  . LEU A 170  ? 0.2297 0.3311 0.2239 0.0164  0.0158  -0.0382 168  LEU A CG  
1051  C CD1 . LEU A 170  ? 0.2243 0.3228 0.2185 0.0186  0.0142  -0.0419 168  LEU A CD1 
1052  C CD2 . LEU A 170  ? 0.2740 0.3720 0.2663 0.0123  0.0170  -0.0316 168  LEU A CD2 
1053  N N   . THR A 171  ? 0.2136 0.3286 0.2134 0.0223  0.0155  -0.0467 169  THR A N   
1054  C CA  . THR A 171  ? 0.2144 0.3429 0.2148 0.0233  0.0165  -0.0496 169  THR A CA  
1055  C C   . THR A 171  ? 0.2169 0.3481 0.2195 0.0282  0.0147  -0.0569 169  THR A C   
1056  O O   . THR A 171  ? 0.2186 0.3605 0.2209 0.0297  0.0150  -0.0608 169  THR A O   
1057  C CB  . THR A 171  ? 0.2214 0.3523 0.2230 0.0218  0.0176  -0.0471 169  THR A CB  
1058  O OG1 . THR A 171  ? 0.2647 0.3935 0.2645 0.0172  0.0190  -0.0404 169  THR A OG1 
1059  C CG2 . THR A 171  ? 0.2222 0.3678 0.2249 0.0230  0.0185  -0.0503 169  THR A CG2 
1060  N N   . ARG A 172  ? 0.2175 0.3389 0.2222 0.0308  0.0128  -0.0590 170  ARG A N   
1061  C CA  . ARG A 172  ? 0.2233 0.3462 0.2305 0.0356  0.0107  -0.0659 170  ARG A CA  
1062  C C   . ARG A 172  ? 0.2227 0.3467 0.2293 0.0372  0.0097  -0.0696 170  ARG A C   
1063  O O   . ARG A 172  ? 0.2250 0.3581 0.2324 0.0401  0.0092  -0.0752 170  ARG A O   
1064  C CB  . ARG A 172  ? 0.2210 0.3317 0.2303 0.0377  0.0086  -0.0665 170  ARG A CB  
1065  C CG  . ARG A 172  ? 0.2242 0.3366 0.2367 0.0428  0.0063  -0.0736 170  ARG A CG  
1066  C CD  . ARG A 172  ? 0.2253 0.3251 0.2400 0.0448  0.0040  -0.0737 170  ARG A CD  
1067  N NE  . ARG A 172  ? 0.2226 0.3170 0.2366 0.0422  0.0050  -0.0682 170  ARG A NE  
1068  C CZ  . ARG A 172  ? 0.2212 0.3050 0.2338 0.0396  0.0051  -0.0633 170  ARG A CZ  
1069  N NH1 . ARG A 172  ? 0.2220 0.2993 0.2336 0.0390  0.0044  -0.0628 170  ARG A NH1 
1070  N NH2 . ARG A 172  ? 0.2191 0.2989 0.2312 0.0376  0.0059  -0.0590 170  ARG A NH2 
1071  N N   . LEU A 173  ? 0.2223 0.3374 0.2273 0.0352  0.0093  -0.0667 171  LEU A N   
1072  C CA  . LEU A 173  ? 0.2247 0.3398 0.2295 0.0369  0.0080  -0.0704 171  LEU A CA  
1073  C C   . LEU A 173  ? 0.2250 0.3532 0.2274 0.0358  0.0096  -0.0710 171  LEU A C   
1074  O O   . LEU A 173  ? 0.2276 0.3616 0.2305 0.0384  0.0086  -0.0764 171  LEU A O   
1075  C CB  . LEU A 173  ? 0.2318 0.3342 0.2358 0.0351  0.0071  -0.0672 171  LEU A CB  
1076  C CG  . LEU A 173  ? 0.2587 0.3594 0.2597 0.0307  0.0089  -0.0607 171  LEU A CG  
1077  C CD1 . LEU A 173  ? 0.2530 0.3596 0.2522 0.0302  0.0091  -0.0620 171  LEU A CD1 
1078  C CD2 . LEU A 173  ? 0.2519 0.3386 0.2532 0.0293  0.0081  -0.0571 171  LEU A CD2 
1079  N N   . ILE A 174  ? 0.2225 0.3556 0.2226 0.0319  0.0121  -0.0654 172  ILE A N   
1080  C CA  . ILE A 174  ? 0.2231 0.3692 0.2208 0.0306  0.0137  -0.0654 172  ILE A CA  
1081  C C   . ILE A 174  ? 0.2376 0.3969 0.2366 0.0333  0.0140  -0.0706 172  ILE A C   
1082  O O   . ILE A 174  ? 0.2633 0.4326 0.2616 0.0350  0.0140  -0.0747 172  ILE A O   
1083  C CB  . ILE A 174  ? 0.2526 0.4002 0.2477 0.0256  0.0160  -0.0578 172  ILE A CB  
1084  C CG1 . ILE A 174  ? 0.2225 0.3592 0.2161 0.0233  0.0155  -0.0537 172  ILE A CG1 
1085  C CG2 . ILE A 174  ? 0.2538 0.4166 0.2467 0.0242  0.0178  -0.0575 172  ILE A CG2 
1086  C CD1 . ILE A 174  ? 0.2567 0.3908 0.2485 0.0188  0.0172  -0.0462 172  ILE A CD1 
1087  N N   . SER A 175  ? 0.2236 0.3840 0.2247 0.0340  0.0144  -0.0706 173  SER A N   
1088  C CA  . SER A 175  ? 0.2251 0.3986 0.2276 0.0367  0.0148  -0.0756 173  SER A CA  
1089  C C   . SER A 175  ? 0.2446 0.4183 0.2495 0.0420  0.0123  -0.0838 173  SER A C   
1090  O O   . SER A 175  ? 0.2628 0.4491 0.2683 0.0446  0.0124  -0.0890 173  SER A O   
1091  C CB  . SER A 175  ? 0.2235 0.3976 0.2280 0.0363  0.0155  -0.0739 173  SER A CB  
1092  O OG  . SER A 175  ? 0.3121 0.4876 0.3147 0.0314  0.0178  -0.0668 173  SER A OG  
1093  N N   . ARG A 176  ? 0.2293 0.3893 0.2357 0.0438  0.0098  -0.0851 174  ARG A N   
1094  C CA  . ARG A 176  ? 0.2451 0.4035 0.2542 0.0488  0.0070  -0.0928 174  ARG A CA  
1095  C C   . ARG A 176  ? 0.2687 0.4290 0.2765 0.0495  0.0061  -0.0958 174  ARG A C   
1096  O O   . ARG A 176  ? 0.2763 0.4439 0.2855 0.0533  0.0048  -0.1028 174  ARG A O   
1097  C CB  . ARG A 176  ? 0.2788 0.4215 0.2904 0.0502  0.0046  -0.0925 174  ARG A CB  
1098  C CG  . ARG A 176  ? 0.2818 0.4211 0.2969 0.0554  0.0013  -0.1001 174  ARG A CG  
1099  C CD  . ARG A 176  ? 0.2384 0.3621 0.2558 0.0562  -0.0009 -0.0986 174  ARG A CD  
1100  N NE  . ARG A 176  ? 0.2376 0.3494 0.2539 0.0538  -0.0016 -0.0950 174  ARG A NE  
1101  C CZ  . ARG A 176  ? 0.2555 0.3581 0.2703 0.0503  -0.0006 -0.0883 174  ARG A CZ  
1102  N NH1 . ARG A 176  ? 0.2320 0.3350 0.2463 0.0486  0.0010  -0.0842 174  ARG A NH1 
1103  N NH2 . ARG A 176  ? 0.3034 0.3963 0.3174 0.0485  -0.0014 -0.0858 174  ARG A NH2 
1104  N N   . CYS A 177  ? 0.2540 0.4083 0.2593 0.0460  0.0067  -0.0908 175  CYS A N   
1105  C CA  . CYS A 177  ? 0.2657 0.4198 0.2699 0.0466  0.0056  -0.0934 175  CYS A CA  
1106  C C   . CYS A 177  ? 0.3409 0.5049 0.3411 0.0434  0.0078  -0.0902 175  CYS A C   
1107  O O   . CYS A 177  ? 0.3215 0.4901 0.3208 0.0447  0.0070  -0.0939 175  CYS A O   
1108  C CB  . CYS A 177  ? 0.2642 0.4021 0.2690 0.0457  0.0038  -0.0911 175  CYS A CB  
1109  S SG  . CYS A 177  ? 0.3361 0.4610 0.3454 0.0490  0.0008  -0.0940 175  CYS A SG  
1110  N N   . GLY A 178  ? 0.3114 0.4785 0.3094 0.0394  0.0105  -0.0835 176  GLY A N   
1111  C CA  . GLY A 178  ? 0.3334 0.5112 0.3278 0.0366  0.0126  -0.0805 176  GLY A CA  
1112  C C   . GLY A 178  ? 0.2639 0.4359 0.2560 0.0344  0.0122  -0.0776 176  GLY A C   
1113  O O   . GLY A 178  ? 0.2753 0.4338 0.2682 0.0337  0.0109  -0.0756 176  GLY A O   
1114  N N   . GLU A 179  ? 0.3346 0.5177 0.3238 0.0333  0.0133  -0.0773 177  GLU A N   
1115  C CA  . GLU A 179  ? 0.2744 0.4539 0.2610 0.0309  0.0131  -0.0740 177  GLU A CA  
1116  C C   . GLU A 179  ? 0.2640 0.4329 0.2523 0.0331  0.0104  -0.0778 177  GLU A C   
1117  O O   . GLU A 179  ? 0.2893 0.4486 0.2767 0.0307  0.0101  -0.0735 177  GLU A O   
1118  C CB  . GLU A 179  ? 0.2628 0.4577 0.2462 0.0303  0.0144  -0.0745 177  GLU A CB  
1119  C CG  . GLU A 179  ? 0.3888 0.5816 0.3692 0.0275  0.0145  -0.0704 177  GLU A CG  
1120  C CD  . GLU A 179  ? 0.5150 0.7235 0.4919 0.0268  0.0158  -0.0704 177  GLU A CD  
1121  O OE1 . GLU A 179  ? 0.5881 0.8092 0.5649 0.0279  0.0170  -0.0728 177  GLU A OE1 
1122  O OE2 . GLU A 179  ? 0.6027 0.8113 0.5770 0.0251  0.0156  -0.0679 177  GLU A OE2 
1123  N N   . PRO A 180  ? 0.2502 0.4200 0.2410 0.0375  0.0082  -0.0857 178  PRO A N   
1124  C CA  . PRO A 180  ? 0.2709 0.4305 0.2634 0.0391  0.0055  -0.0889 178  PRO A CA  
1125  C C   . PRO A 180  ? 0.3097 0.4530 0.3039 0.0376  0.0047  -0.0848 178  PRO A C   
1126  O O   . PRO A 180  ? 0.2962 0.4315 0.2902 0.0363  0.0036  -0.0833 178  PRO A O   
1127  C CB  . PRO A 180  ? 0.3020 0.4654 0.2975 0.0442  0.0033  -0.0979 178  PRO A CB  
1128  C CG  . PRO A 180  ? 0.2812 0.4615 0.2750 0.0450  0.0051  -0.0999 178  PRO A CG  
1129  C CD  . PRO A 180  ? 0.2956 0.4775 0.2876 0.0411  0.0081  -0.0923 178  PRO A CD  
1130  N N   . VAL A 181  ? 0.2611 0.3995 0.2570 0.0376  0.0051  -0.0830 179  VAL A N   
1131  C CA  . VAL A 181  ? 0.2861 0.4095 0.2835 0.0362  0.0044  -0.0791 179  VAL A CA  
1132  C C   . VAL A 181  ? 0.2581 0.3782 0.2526 0.0316  0.0063  -0.0713 179  VAL A C   
1133  O O   . VAL A 181  ? 0.3026 0.4116 0.2975 0.0301  0.0056  -0.0684 179  VAL A O   
1134  C CB  . VAL A 181  ? 0.2877 0.4073 0.2875 0.0376  0.0043  -0.0795 179  VAL A CB  
1135  C CG1 . VAL A 181  ? 0.2731 0.3988 0.2711 0.0350  0.0071  -0.0745 179  VAL A CG1 
1136  C CG2 . VAL A 181  ? 0.3136 0.4177 0.3155 0.0373  0.0028  -0.0774 179  VAL A CG2 
1137  N N   . ILE A 182  ? 0.2594 0.3892 0.2511 0.0292  0.0087  -0.0676 180  ILE A N   
1138  C CA  . ILE A 182  ? 0.2918 0.4188 0.2809 0.0250  0.0103  -0.0603 180  ILE A CA  
1139  C C   . ILE A 182  ? 0.3092 0.4348 0.2968 0.0243  0.0094  -0.0602 180  ILE A C   
1140  O O   . ILE A 182  ? 0.2851 0.4014 0.2724 0.0222  0.0092  -0.0561 180  ILE A O   
1141  C CB  . ILE A 182  ? 0.2617 0.4000 0.2485 0.0226  0.0128  -0.0566 180  ILE A CB  
1142  C CG1 . ILE A 182  ? 0.2413 0.3809 0.2298 0.0232  0.0136  -0.0567 180  ILE A CG1 
1143  C CG2 . ILE A 182  ? 0.2821 0.4170 0.2664 0.0183  0.0142  -0.0489 180  ILE A CG2 
1144  C CD1 . ILE A 182  ? 0.3105 0.4635 0.2973 0.0216  0.0159  -0.0547 180  ILE A CD1 
1145  N N   . ARG A 183  ? 0.2826 0.4179 0.2694 0.0262  0.0089  -0.0650 181  ARG A N   
1146  C CA  . ARG A 183  ? 0.3143 0.4493 0.2998 0.0257  0.0078  -0.0655 181  ARG A CA  
1147  C C   . ARG A 183  ? 0.3403 0.4622 0.3285 0.0268  0.0055  -0.0674 181  ARG A C   
1148  O O   . ARG A 183  ? 0.3532 0.4689 0.3407 0.0248  0.0052  -0.0641 181  ARG A O   
1149  C CB  . ARG A 183  ? 0.2905 0.4386 0.2749 0.0281  0.0074  -0.0712 181  ARG A CB  
1150  N N   . ARG A 184  ? 0.3285 0.4461 0.3200 0.0299  0.0038  -0.0724 182  ARG A N   
1151  C CA  . ARG A 184  ? 0.3381 0.4430 0.3325 0.0307  0.0016  -0.0739 182  ARG A CA  
1152  C C   . ARG A 184  ? 0.3283 0.4220 0.3227 0.0278  0.0024  -0.0672 182  ARG A C   
1153  O O   . ARG A 184  ? 0.3473 0.4325 0.3424 0.0266  0.0014  -0.0656 182  ARG A O   
1154  C CB  . ARG A 184  ? 0.3694 0.4720 0.3674 0.0346  -0.0005 -0.0801 182  ARG A CB  
1155  C CG  . ARG A 184  ? 0.4157 0.5249 0.4148 0.0379  -0.0025 -0.0878 182  ARG A CG  
1156  C CD  . ARG A 184  ? 0.4290 0.5293 0.4301 0.0382  -0.0050 -0.0898 182  ARG A CD  
1157  N NE  . ARG A 184  ? 0.5084 0.5992 0.5138 0.0407  -0.0076 -0.0935 182  ARG A NE  
1158  C CZ  . ARG A 184  ? 0.5050 0.5828 0.5125 0.0395  -0.0086 -0.0907 182  ARG A CZ  
1159  N NH1 . ARG A 184  ? 0.5000 0.5725 0.5059 0.0359  -0.0074 -0.0846 182  ARG A NH1 
1160  N NH2 . ARG A 184  ? 0.4885 0.5586 0.4999 0.0419  -0.0111 -0.0942 182  ARG A NH2 
1161  N N   . GLY A 185  ? 0.2789 0.3729 0.2727 0.0265  0.0042  -0.0634 183  GLY A N   
1162  C CA  . GLY A 185  ? 0.3027 0.3870 0.2963 0.0238  0.0051  -0.0572 183  GLY A CA  
1163  C C   . GLY A 185  ? 0.3233 0.4075 0.3143 0.0205  0.0062  -0.0521 183  GLY A C   
1164  O O   . GLY A 185  ? 0.3071 0.3821 0.2987 0.0190  0.0058  -0.0490 183  GLY A O   
1165  N N   . VAL A 186  ? 0.3003 0.3952 0.2886 0.0195  0.0075  -0.0510 184  VAL A N   
1166  C CA  . VAL A 186  ? 0.3245 0.4201 0.3103 0.0165  0.0084  -0.0460 184  VAL A CA  
1167  C C   . VAL A 186  ? 0.3542 0.4452 0.3406 0.0170  0.0066  -0.0480 184  VAL A C   
1168  O O   . VAL A 186  ? 0.3767 0.4609 0.3628 0.0149  0.0066  -0.0440 184  VAL A O   
1169  C CB  . VAL A 186  ? 0.3856 0.4943 0.3684 0.0155  0.0099  -0.0449 184  VAL A CB  
1170  C CG1 . VAL A 186  ? 0.3211 0.4313 0.3014 0.0132  0.0101  -0.0412 184  VAL A CG1 
1171  C CG2 . VAL A 186  ? 0.3394 0.4510 0.3215 0.0138  0.0118  -0.0409 184  VAL A CG2 
1172  N N   . ASP A 187  ? 0.3433 0.4382 0.3309 0.0198  0.0049  -0.0544 185  ASP A N   
1173  C CA  . ASP A 187  ? 0.3608 0.4518 0.3493 0.0202  0.0030  -0.0566 185  ASP A CA  
1174  C C   . ASP A 187  ? 0.3901 0.4676 0.3815 0.0200  0.0018  -0.0558 185  ASP A C   
1175  O O   . ASP A 187  ? 0.3939 0.4661 0.3857 0.0185  0.0012  -0.0538 185  ASP A O   
1176  C CB  . ASP A 187  ? 0.3830 0.4809 0.3725 0.0234  0.0013  -0.0641 185  ASP A CB  
1177  C CG  . ASP A 187  ? 0.4850 0.5971 0.4711 0.0235  0.0025  -0.0649 185  ASP A CG  
1178  O OD1 . ASP A 187  ? 0.5823 0.6978 0.5654 0.0207  0.0041  -0.0594 185  ASP A OD1 
1179  O OD2 . ASP A 187  ? 0.5161 0.6360 0.5027 0.0264  0.0017  -0.0709 185  ASP A OD2 
1180  N N   . MET A 188  ? 0.3679 0.4404 0.3616 0.0213  0.0015  -0.0570 186  MET A N   
1181  C CA  . MET A 188  ? 0.3721 0.4322 0.3685 0.0210  0.0005  -0.0558 186  MET A CA  
1182  C C   . MET A 188  ? 0.3977 0.4522 0.3927 0.0178  0.0021  -0.0488 186  MET A C   
1183  O O   . MET A 188  ? 0.4125 0.4596 0.4086 0.0166  0.0014  -0.0470 186  MET A O   
1184  C CB  . MET A 188  ? 0.3987 0.4554 0.3974 0.0231  -0.0001 -0.0581 186  MET A CB  
1185  C CG  . MET A 188  ? 0.4669 0.5113 0.4684 0.0230  -0.0013 -0.0571 186  MET A CG  
1186  S SD  . MET A 188  ? 0.6988 0.7384 0.7037 0.0248  -0.0046 -0.0626 186  MET A SD  
1187  C CE  . MET A 188  ? 0.5688 0.6156 0.5751 0.0290  -0.0060 -0.0700 186  MET A CE  
1188  N N   . ALA A 189  ? 0.3838 0.4419 0.3767 0.0163  0.0042  -0.0448 187  ALA A N   
1189  C CA  . ALA A 189  ? 0.4193 0.4720 0.4111 0.0135  0.0056  -0.0385 187  ALA A CA  
1190  C C   . ALA A 189  ? 0.4277 0.4816 0.4179 0.0117  0.0056  -0.0361 187  ALA A C   
1191  O O   . ALA A 189  ? 0.3994 0.4461 0.3900 0.0100  0.0057  -0.0327 187  ALA A O   
1192  C CB  . ALA A 189  ? 0.3793 0.4363 0.3694 0.0123  0.0075  -0.0351 187  ALA A CB  
1193  N N   . MET A 190  ? 0.3821 0.4453 0.3705 0.0120  0.0056  -0.0379 188  MET A N   
1194  C CA  . MET A 190  ? 0.4391 0.5042 0.4259 0.0104  0.0055  -0.0356 188  MET A CA  
1195  C C   . MET A 190  ? 0.4388 0.4969 0.4278 0.0108  0.0037  -0.0376 188  MET A C   
1196  O O   . MET A 190  ? 0.4657 0.5197 0.4546 0.0090  0.0037  -0.0341 188  MET A O   
1197  C CB  . MET A 190  ? 0.4208 0.4977 0.4052 0.0110  0.0056  -0.0377 188  MET A CB  
1198  C CG  . MET A 190  ? 0.4977 0.5781 0.4798 0.0091  0.0058  -0.0344 188  MET A CG  
1199  S SD  . MET A 190  ? 0.6652 0.7596 0.6447 0.0104  0.0054  -0.0382 188  MET A SD  
1200  C CE  . MET A 190  ? 0.5804 0.6839 0.5579 0.0100  0.0075  -0.0365 188  MET A CE  
1201  N N   . ARG A 191  ? 0.4180 0.4749 0.4095 0.0132  0.0019  -0.0432 189  ARG A N   
1202  C CA  . ARG A 191  ? 0.4679 0.5179 0.4621 0.0134  0.0000  -0.0451 189  ARG A CA  
1203  C C   . ARG A 191  ? 0.4942 0.5334 0.4902 0.0120  0.0003  -0.0415 189  ARG A C   
1204  O O   . ARG A 191  ? 0.4545 0.4887 0.4516 0.0107  -0.0002 -0.0398 189  ARG A O   
1205  C CB  . ARG A 191  ? 0.4281 0.4786 0.4248 0.0163  -0.0021 -0.0520 189  ARG A CB  
1206  N N   . MET A 192  ? 0.4321 0.4681 0.4284 0.0124  0.0012  -0.0403 190  MET A N   
1207  C CA  . MET A 192  ? 0.4335 0.4597 0.4314 0.0113  0.0014  -0.0371 190  MET A CA  
1208  C C   . MET A 192  ? 0.4729 0.4975 0.4690 0.0087  0.0030  -0.0312 190  MET A C   
1209  O O   . MET A 192  ? 0.4363 0.4545 0.4337 0.0075  0.0028  -0.0291 190  MET A O   
1210  C CB  . MET A 192  ? 0.4356 0.4594 0.4342 0.0124  0.0019  -0.0374 190  MET A CB  
1211  C CG  . MET A 192  ? 0.4279 0.4511 0.4291 0.0151  -0.0001 -0.0430 190  MET A CG  
1212  S SD  . MET A 192  ? 0.5745 0.5930 0.5766 0.0162  0.0003  -0.0424 190  MET A SD  
1213  C CE  . MET A 192  ? 0.4164 0.4232 0.4206 0.0147  -0.0002 -0.0390 190  MET A CE  
1214  N N   . MET A 193  ? 0.4277 0.4582 0.4211 0.0078  0.0046  -0.0286 191  MET A N   
1215  C CA  . MET A 193  ? 0.4880 0.5166 0.4799 0.0055  0.0059  -0.0231 191  MET A CA  
1216  C C   . MET A 193  ? 0.4476 0.4784 0.4387 0.0044  0.0055  -0.0219 191  MET A C   
1217  O O   . MET A 193  ? 0.4668 0.4936 0.4578 0.0028  0.0060  -0.0180 191  MET A O   
1218  C CB  . MET A 193  ? 0.4273 0.4609 0.4170 0.0048  0.0076  -0.0204 191  MET A CB  
1219  C CG  . MET A 193  ? 0.4452 0.4760 0.4356 0.0055  0.0081  -0.0207 191  MET A CG  
1220  S SD  . MET A 193  ? 0.6193 0.6547 0.6074 0.0040  0.0100  -0.0167 191  MET A SD  
1221  C CE  . MET A 193  ? 0.4658 0.5135 0.4520 0.0045  0.0102  -0.0188 191  MET A CE  
1222  N N   . GLY A 194  ? 0.4340 0.4712 0.4246 0.0054  0.0045  -0.0253 192  GLY A N   
1223  C CA  . GLY A 194  ? 0.4692 0.5094 0.4588 0.0045  0.0040  -0.0243 192  GLY A CA  
1224  C C   . GLY A 194  ? 0.5066 0.5425 0.4988 0.0049  0.0023  -0.0269 192  GLY A C   
1225  O O   . GLY A 194  ? 0.4510 0.4869 0.4429 0.0038  0.0019  -0.0251 192  GLY A O   
1226  N N   . GLU A 195  ? 0.4275 0.4597 0.4222 0.0064  0.0011  -0.0310 193  GLU A N   
1227  C CA  . GLU A 195  ? 0.4468 0.4759 0.4444 0.0068  -0.0008 -0.0341 193  GLU A CA  
1228  C C   . GLU A 195  ? 0.3984 0.4181 0.3992 0.0068  -0.0015 -0.0344 193  GLU A C   
1229  O O   . GLU A 195  ? 0.3331 0.3490 0.3364 0.0063  -0.0028 -0.0353 193  GLU A O   
1230  C CB  . GLU A 195  ? 0.4849 0.5199 0.4827 0.0088  -0.0025 -0.0400 193  GLU A CB  
1231  C CG  . GLU A 195  ? 0.5440 0.5894 0.5386 0.0090  -0.0020 -0.0403 193  GLU A CG  
1232  C CD  . GLU A 195  ? 0.5938 0.6455 0.5886 0.0114  -0.0034 -0.0466 193  GLU A CD  
1233  O OE1 . GLU A 195  ? 0.5982 0.6464 0.5961 0.0126  -0.0055 -0.0510 193  GLU A OE1 
1234  O OE2 . GLU A 195  ? 0.6721 0.7323 0.6642 0.0121  -0.0025 -0.0472 193  GLU A OE2 
1235  N N   . GLN A 196  ? 0.4723 0.4885 0.4734 0.0073  -0.0008 -0.0338 194  GLN A N   
1236  C CA  . GLN A 196  ? 0.4263 0.4341 0.4304 0.0074  -0.0015 -0.0340 194  GLN A CA  
1237  C C   . GLN A 196  ? 0.4270 0.4291 0.4307 0.0058  0.0001  -0.0287 194  GLN A C   
1238  O O   . GLN A 196  ? 0.4776 0.4732 0.4835 0.0049  -0.0003 -0.0275 194  GLN A O   
1239  C CB  . GLN A 196  ? 0.4569 0.4645 0.4619 0.0096  -0.0022 -0.0376 194  GLN A CB  
1240  N N   . PHE A 197  ? 0.3660 0.3706 0.3671 0.0053  0.0020  -0.0257 195  PHE A N   
1241  C CA  . PHE A 197  ? 0.3617 0.3615 0.3623 0.0038  0.0034  -0.0210 195  PHE A CA  
1242  C C   . PHE A 197  ? 0.3819 0.3817 0.3821 0.0021  0.0038  -0.0181 195  PHE A C   
1243  O O   . PHE A 197  ? 0.4374 0.4321 0.4384 0.0010  0.0043  -0.0152 195  PHE A O   
1244  C CB  . PHE A 197  ? 0.3856 0.3880 0.3838 0.0038  0.0050  -0.0188 195  PHE A CB  
1245  C CG  . PHE A 197  ? 0.4018 0.4043 0.4005 0.0055  0.0047  -0.0214 195  PHE A CG  
1246  C CD1 . PHE A 197  ? 0.4526 0.4499 0.4538 0.0067  0.0034  -0.0240 195  PHE A CD1 
1247  C CD2 . PHE A 197  ? 0.4418 0.4493 0.4385 0.0059  0.0058  -0.0211 195  PHE A CD2 
1248  C CE1 . PHE A 197  ? 0.4477 0.4451 0.4496 0.0084  0.0029  -0.0264 195  PHE A CE1 
1249  C CE2 . PHE A 197  ? 0.4867 0.4947 0.4840 0.0076  0.0055  -0.0236 195  PHE A CE2 
1250  C CZ  . PHE A 197  ? 0.4392 0.4420 0.4391 0.0090  0.0041  -0.0263 195  PHE A CZ  
1251  N N   . VAL A 198  ? 0.3333 0.3392 0.3321 0.0021  0.0035  -0.0188 196  VAL A N   
1252  C CA  . VAL A 198  ? 0.3403 0.3469 0.3388 0.0007  0.0036  -0.0163 196  VAL A CA  
1253  C C   . VAL A 198  ? 0.3100 0.3199 0.3094 0.0011  0.0019  -0.0197 196  VAL A C   
1254  O O   . VAL A 198  ? 0.3701 0.3843 0.3694 0.0025  0.0010  -0.0236 196  VAL A O   
1255  C CB  . VAL A 198  ? 0.3215 0.3325 0.3169 -0.0002 0.0049  -0.0127 196  VAL A CB  
1256  C CG1 . VAL A 198  ? 0.3586 0.3662 0.3532 -0.0006 0.0063  -0.0097 196  VAL A CG1 
1257  C CG2 . VAL A 198  ? 0.3524 0.3715 0.3457 0.0006  0.0046  -0.0148 196  VAL A CG2 
1258  N N   . THR A 199  ? 0.2826 0.2910 0.2832 0.0001  0.0015  -0.0184 197  THR A N   
1259  C CA  . THR A 199  ? 0.2919 0.3043 0.2932 0.0003  -0.0001 -0.0212 197  THR A CA  
1260  C C   . THR A 199  ? 0.3231 0.3434 0.3211 0.0005  0.0002  -0.0206 197  THR A C   
1261  O O   . THR A 199  ? 0.3837 0.4095 0.3813 0.0014  -0.0010 -0.0241 197  THR A O   
1262  C CB  . THR A 199  ? 0.3392 0.3479 0.3428 -0.0009 -0.0006 -0.0198 197  THR A CB  
1263  O OG1 . THR A 199  ? 0.3435 0.3452 0.3500 -0.0013 -0.0008 -0.0200 197  THR A OG1 
1264  C CG2 . THR A 199  ? 0.3046 0.3174 0.3092 -0.0007 -0.0024 -0.0229 197  THR A CG2 
1265  N N   . GLY A 200  ? 0.3144 0.3355 0.3102 -0.0004 0.0016  -0.0162 198  GLY A N   
1266  C CA  . GLY A 200  ? 0.3428 0.3714 0.3355 -0.0006 0.0019  -0.0149 198  GLY A CA  
1267  C C   . GLY A 200  ? 0.3409 0.3687 0.3316 -0.0015 0.0036  -0.0103 198  GLY A C   
1268  O O   . GLY A 200  ? 0.3095 0.3310 0.3013 -0.0021 0.0044  -0.0080 198  GLY A O   
1269  N N   . GLU A 201  ? 0.3350 0.3694 0.3228 -0.0017 0.0040  -0.0090 199  GLU A N   
1270  C CA  . GLU A 201  ? 0.3916 0.4255 0.3778 -0.0028 0.0054  -0.0045 199  GLU A CA  
1271  C C   . GLU A 201  ? 0.3089 0.3409 0.2949 -0.0040 0.0052  -0.0003 199  GLU A C   
1272  O O   . GLU A 201  ? 0.3202 0.3486 0.3060 -0.0049 0.0061  0.0034  199  GLU A O   
1273  C CB  . GLU A 201  ? 0.3956 0.4375 0.3790 -0.0028 0.0059  -0.0042 199  GLU A CB  
1274  C CG  . GLU A 201  ? 0.5114 0.5546 0.4950 -0.0016 0.0064  -0.0076 199  GLU A CG  
1275  C CD  . GLU A 201  ? 0.6068 0.6585 0.5878 -0.0017 0.0071  -0.0073 199  GLU A CD  
1276  O OE1 . GLU A 201  ? 0.6350 0.6919 0.6138 -0.0028 0.0071  -0.0045 199  GLU A OE1 
1277  O OE2 . GLU A 201  ? 0.6473 0.7006 0.6285 -0.0007 0.0076  -0.0098 199  GLU A OE2 
1278  N N   . THR A 202  ? 0.2903 0.3247 0.2765 -0.0039 0.0040  -0.0010 200  THR A N   
1279  C CA  . THR A 202  ? 0.2895 0.3222 0.2758 -0.0048 0.0036  0.0025  200  THR A CA  
1280  C C   . THR A 202  ? 0.3102 0.3403 0.2992 -0.0044 0.0025  0.0000  200  THR A C   
1281  O O   . THR A 202  ? 0.2808 0.3120 0.2710 -0.0035 0.0017  -0.0042 200  THR A O   
1282  C CB  . THR A 202  ? 0.2863 0.3261 0.2700 -0.0053 0.0030  0.0046  200  THR A CB  
1283  O OG1 . THR A 202  ? 0.2942 0.3398 0.2774 -0.0043 0.0019  0.0007  200  THR A OG1 
1284  C CG2 . THR A 202  ? 0.3402 0.3835 0.3213 -0.0060 0.0041  0.0071  200  THR A CG2 
1285  N N   . ILE A 203  ? 0.2738 0.3007 0.2640 -0.0050 0.0022  0.0027  201  ILE A N   
1286  C CA  . ILE A 203  ? 0.2705 0.2954 0.2635 -0.0048 0.0012  0.0006  201  ILE A CA  
1287  C C   . ILE A 203  ? 0.2690 0.3002 0.2614 -0.0043 -0.0003 -0.0021 201  ILE A C   
1288  O O   . ILE A 203  ? 0.2984 0.3292 0.2930 -0.0039 -0.0013 -0.0058 201  ILE A O   
1289  C CB  . ILE A 203  ? 0.2768 0.2979 0.2712 -0.0054 0.0012  0.0039  201  ILE A CB  
1290  C CG1 . ILE A 203  ? 0.2510 0.2699 0.2488 -0.0054 0.0004  0.0017  201  ILE A CG1 
1291  C CG2 . ILE A 203  ? 0.3466 0.3718 0.3390 -0.0056 0.0005  0.0071  201  ILE A CG2 
1292  C CD1 . ILE A 203  ? 0.2452 0.2598 0.2452 -0.0053 0.0008  -0.0011 201  ILE A CD1 
1293  N N   . ARG A 204  ? 0.2969 0.3343 0.2863 -0.0043 -0.0007 -0.0004 202  ARG A N   
1294  C CA  . ARG A 204  ? 0.2992 0.3434 0.2877 -0.0037 -0.0021 -0.0031 202  ARG A CA  
1295  C C   . ARG A 204  ? 0.3094 0.3558 0.2982 -0.0028 -0.0023 -0.0082 202  ARG A C   
1296  O O   . ARG A 204  ? 0.3053 0.3533 0.2957 -0.0021 -0.0037 -0.0122 202  ARG A O   
1297  C CB  . ARG A 204  ? 0.3403 0.3911 0.3252 -0.0041 -0.0023 0.0000  202  ARG A CB  
1298  N N   . GLU A 205  ? 0.3044 0.3508 0.2920 -0.0025 -0.0011 -0.0084 203  GLU A N   
1299  C CA  . GLU A 205  ? 0.3397 0.3880 0.3277 -0.0013 -0.0014 -0.0134 203  GLU A CA  
1300  C C   . GLU A 205  ? 0.3207 0.3620 0.3125 -0.0010 -0.0019 -0.0164 203  GLU A C   
1301  O O   . GLU A 205  ? 0.3303 0.3730 0.3237 -0.0001 -0.0033 -0.0211 203  GLU A O   
1302  C CB  . GLU A 205  ? 0.3577 0.4074 0.3437 -0.0012 0.0001  -0.0126 203  GLU A CB  
1303  C CG  . GLU A 205  ? 0.4051 0.4572 0.3916 0.0004  -0.0002 -0.0179 203  GLU A CG  
1304  C CD  . GLU A 205  ? 0.4597 0.5139 0.4443 0.0005  0.0013  -0.0170 203  GLU A CD  
1305  O OE1 . GLU A 205  ? 0.4684 0.5165 0.4540 0.0000  0.0024  -0.0150 203  GLU A OE1 
1306  O OE2 . GLU A 205  ? 0.5394 0.6018 0.5216 0.0011  0.0014  -0.0183 203  GLU A OE2 
1307  N N   . ALA A 206  ? 0.2983 0.3324 0.2919 -0.0018 -0.0010 -0.0136 204  ALA A N   
1308  C CA  . ALA A 206  ? 0.3135 0.3411 0.3107 -0.0018 -0.0015 -0.0158 204  ALA A CA  
1309  C C   . ALA A 206  ? 0.3059 0.3340 0.3055 -0.0020 -0.0032 -0.0179 204  ALA A C   
1310  O O   . ALA A 206  ? 0.2659 0.2922 0.2681 -0.0016 -0.0044 -0.0218 204  ALA A O   
1311  C CB  . ALA A 206  ? 0.2793 0.3000 0.2775 -0.0028 -0.0001 -0.0120 204  ALA A CB  
1312  N N   . LEU A 207  ? 0.2756 0.3061 0.2745 -0.0026 -0.0035 -0.0154 205  LEU A N   
1313  C CA  . LEU A 207  ? 0.2631 0.2947 0.2642 -0.0028 -0.0051 -0.0173 205  LEU A CA  
1314  C C   . LEU A 207  ? 0.3107 0.3480 0.3115 -0.0017 -0.0068 -0.0222 205  LEU A C   
1315  O O   . LEU A 207  ? 0.3138 0.3500 0.3176 -0.0017 -0.0083 -0.0258 205  LEU A O   
1316  C CB  . LEU A 207  ? 0.3300 0.3638 0.3301 -0.0034 -0.0052 -0.0135 205  LEU A CB  
1317  C CG  . LEU A 207  ? 0.2841 0.3120 0.2856 -0.0044 -0.0040 -0.0095 205  LEU A CG  
1318  C CD1 . LEU A 207  ? 0.3022 0.3327 0.3020 -0.0046 -0.0041 -0.0056 205  LEU A CD1 
1319  C CD2 . LEU A 207  ? 0.2394 0.2629 0.2452 -0.0050 -0.0046 -0.0110 205  LEU A CD2 
1320  N N   . LYS A 208  ? 0.2958 0.3397 0.2929 -0.0009 -0.0066 -0.0225 206  LYS A N   
1321  C CA  . LYS A 208  ? 0.3367 0.3869 0.3333 0.0003  -0.0081 -0.0275 206  LYS A CA  
1322  C C   . LYS A 208  ? 0.3099 0.3564 0.3092 0.0012  -0.0088 -0.0323 206  LYS A C   
1323  O O   . LYS A 208  ? 0.3554 0.4033 0.3568 0.0019  -0.0107 -0.0370 206  LYS A O   
1324  C CB  . LYS A 208  ? 0.3705 0.4284 0.3626 0.0010  -0.0073 -0.0266 206  LYS A CB  
1325  N N   . ARG A 209  ? 0.3441 0.3857 0.3437 0.0012  -0.0074 -0.0312 207  ARG A N   
1326  C CA  . ARG A 209  ? 0.3592 0.3972 0.3612 0.0022  -0.0081 -0.0354 207  ARG A CA  
1327  C C   . ARG A 209  ? 0.3797 0.4100 0.3863 0.0013  -0.0091 -0.0361 207  ARG A C   
1328  O O   . ARG A 209  ? 0.3875 0.4144 0.3967 0.0020  -0.0101 -0.0397 207  ARG A O   
1329  C CB  . ARG A 209  ? 0.3490 0.3851 0.3496 0.0027  -0.0064 -0.0340 207  ARG A CB  
1330  C CG  . ARG A 209  ? 0.4165 0.4608 0.4132 0.0036  -0.0057 -0.0343 207  ARG A CG  
1331  C CD  . ARG A 209  ? 0.3869 0.4292 0.3824 0.0038  -0.0039 -0.0326 207  ARG A CD  
1332  N NE  . ARG A 209  ? 0.5135 0.5642 0.5055 0.0046  -0.0032 -0.0328 207  ARG A NE  
1333  C CZ  . ARG A 209  ? 0.5407 0.5918 0.5309 0.0045  -0.0015 -0.0307 207  ARG A CZ  
1334  N NH1 . ARG A 209  ? 0.4808 0.5245 0.4724 0.0039  -0.0005 -0.0282 207  ARG A NH1 
1335  N NH2 . ARG A 209  ? 0.5731 0.6327 0.5603 0.0050  -0.0008 -0.0309 207  ARG A NH2 
1336  N N   . SER A 210  ? 0.3359 0.3636 0.3435 -0.0002 -0.0087 -0.0326 208  SER A N   
1337  C CA  . SER A 210  ? 0.3191 0.3401 0.3311 -0.0014 -0.0095 -0.0328 208  SER A CA  
1338  C C   . SER A 210  ? 0.3675 0.3904 0.3824 -0.0014 -0.0119 -0.0368 208  SER A C   
1339  O O   . SER A 210  ? 0.3241 0.3417 0.3431 -0.0023 -0.0129 -0.0381 208  SER A O   
1340  C CB  . SER A 210  ? 0.2913 0.3090 0.3035 -0.0029 -0.0080 -0.0276 208  SER A CB  
1341  O OG  . SER A 210  ? 0.3078 0.3233 0.3178 -0.0029 -0.0059 -0.0242 208  SER A OG  
1342  N N   . LYS A 211  ? 0.3594 0.3898 0.3723 -0.0006 -0.0129 -0.0388 209  LYS A N   
1343  C CA  . LYS A 211  ? 0.3782 0.4110 0.3936 -0.0006 -0.0153 -0.0427 209  LYS A CA  
1344  C C   . LYS A 211  ? 0.3487 0.3781 0.3679 0.0000  -0.0172 -0.0479 209  LYS A C   
1345  O O   . LYS A 211  ? 0.3671 0.3937 0.3904 -0.0010 -0.0190 -0.0499 209  LYS A O   
1346  C CB  . LYS A 211  ? 0.3530 0.3952 0.3650 0.0005  -0.0160 -0.0442 209  LYS A CB  
1347  N N   . GLU A 212  ? 0.3763 0.4056 0.3942 0.0015  -0.0170 -0.0502 210  GLU A N   
1348  C CA  . GLU A 212  ? 0.4437 0.4702 0.4650 0.0026  -0.0192 -0.0557 210  GLU A CA  
1349  C C   . GLU A 212  ? 0.4081 0.4254 0.4342 0.0009  -0.0197 -0.0546 210  GLU A C   
1350  O O   . GLU A 212  ? 0.4304 0.4456 0.4607 0.0004  -0.0221 -0.0580 210  GLU A O   
1351  C CB  . GLU A 212  ? 0.4346 0.4626 0.4537 0.0046  -0.0186 -0.0577 210  GLU A CB  
1352  C CG  . GLU A 212  ? 0.5171 0.5421 0.5397 0.0060  -0.0209 -0.0635 210  GLU A CG  
1353  C CD  . GLU A 212  ? 0.5866 0.6132 0.6071 0.0082  -0.0203 -0.0655 210  GLU A CD  
1354  O OE1 . GLU A 212  ? 0.6353 0.6668 0.6515 0.0086  -0.0181 -0.0627 210  GLU A OE1 
1355  O OE2 . GLU A 212  ? 0.6411 0.6641 0.6646 0.0096  -0.0221 -0.0698 210  GLU A OE2 
1356  N N   . LEU A 213  ? 0.3766 0.3885 0.4022 -0.0001 -0.0176 -0.0499 211  LEU A N   
1357  C CA  . LEU A 213  ? 0.3711 0.3746 0.4010 -0.0017 -0.0180 -0.0486 211  LEU A CA  
1358  C C   . LEU A 213  ? 0.3242 0.3267 0.3564 -0.0040 -0.0179 -0.0458 211  LEU A C   
1359  O O   . LEU A 213  ? 0.3845 0.3816 0.4212 -0.0055 -0.0190 -0.0459 211  LEU A O   
1360  C CB  . LEU A 213  ? 0.3532 0.3518 0.3818 -0.0018 -0.0158 -0.0448 211  LEU A CB  
1361  C CG  . LEU A 213  ? 0.3945 0.3931 0.4221 0.0004  -0.0163 -0.0482 211  LEU A CG  
1362  C CD1 . LEU A 213  ? 0.3639 0.3568 0.3908 0.0003  -0.0146 -0.0448 211  LEU A CD1 
1363  C CD2 . LEU A 213  ? 0.3902 0.3867 0.4218 0.0013  -0.0194 -0.0539 211  LEU A CD2 
1364  N N   . GLU A 214  ? 0.3320 0.3397 0.3616 -0.0043 -0.0168 -0.0433 212  GLU A N   
1365  C CA  . GLU A 214  ? 0.3600 0.3677 0.3921 -0.0062 -0.0171 -0.0414 212  GLU A CA  
1366  C C   . GLU A 214  ? 0.3903 0.3996 0.4260 -0.0064 -0.0201 -0.0463 212  GLU A C   
1367  O O   . GLU A 214  ? 0.3871 0.3936 0.4270 -0.0083 -0.0210 -0.0458 212  GLU A O   
1368  C CB  . GLU A 214  ? 0.3359 0.3488 0.3644 -0.0062 -0.0156 -0.0379 212  GLU A CB  
1369  C CG  . GLU A 214  ? 0.3277 0.3380 0.3538 -0.0065 -0.0129 -0.0327 212  GLU A CG  
1370  C CD  . GLU A 214  ? 0.3645 0.3793 0.3877 -0.0065 -0.0117 -0.0292 212  GLU A CD  
1371  O OE1 . GLU A 214  ? 0.4064 0.4271 0.4284 -0.0059 -0.0130 -0.0309 212  GLU A OE1 
1372  O OE2 . GLU A 214  ? 0.3936 0.4058 0.4156 -0.0071 -0.0098 -0.0249 212  GLU A OE2 
1373  N N   . GLU A 215  ? 0.3687 0.3829 0.4031 -0.0045 -0.0217 -0.0511 213  GLU A N   
1374  C CA  . GLU A 215  ? 0.4137 0.4294 0.4517 -0.0045 -0.0248 -0.0563 213  GLU A CA  
1375  C C   . GLU A 215  ? 0.4488 0.4569 0.4918 -0.0053 -0.0265 -0.0586 213  GLU A C   
1376  O O   . GLU A 215  ? 0.4968 0.5038 0.5443 -0.0063 -0.0289 -0.0615 213  GLU A O   
1377  C CB  . GLU A 215  ? 0.4186 0.4418 0.4536 -0.0020 -0.0261 -0.0610 213  GLU A CB  
1378  N N   . LYS A 216  ? 0.4395 0.4423 0.4822 -0.0048 -0.0255 -0.0574 214  LYS A N   
1379  C CA  . LYS A 216  ? 0.4375 0.4324 0.4849 -0.0056 -0.0271 -0.0589 214  LYS A CA  
1380  C C   . LYS A 216  ? 0.4709 0.4596 0.5210 -0.0084 -0.0258 -0.0537 214  LYS A C   
1381  O O   . LYS A 216  ? 0.4919 0.4738 0.5460 -0.0094 -0.0270 -0.0539 214  LYS A O   
1382  C CB  . LYS A 216  ? 0.3741 0.3666 0.4199 -0.0035 -0.0269 -0.0605 214  LYS A CB  
1383  N N   . GLY A 217  ? 0.3988 0.3898 0.4471 -0.0097 -0.0236 -0.0490 215  GLY A N   
1384  C CA  . GLY A 217  ? 0.3770 0.3635 0.4281 -0.0123 -0.0224 -0.0444 215  GLY A CA  
1385  C C   . GLY A 217  ? 0.4066 0.3905 0.4547 -0.0125 -0.0193 -0.0392 215  GLY A C   
1386  O O   . GLY A 217  ? 0.3415 0.3218 0.3917 -0.0145 -0.0182 -0.0354 215  GLY A O   
1387  N N   . PHE A 218  ? 0.3322 0.3180 0.3756 -0.0104 -0.0179 -0.0389 216  PHE A N   
1388  C CA  . PHE A 218  ? 0.3476 0.3315 0.3881 -0.0105 -0.0151 -0.0341 216  PHE A CA  
1389  C C   . PHE A 218  ? 0.2916 0.2802 0.3296 -0.0109 -0.0133 -0.0308 216  PHE A C   
1390  O O   . PHE A 218  ? 0.3128 0.3070 0.3501 -0.0104 -0.0141 -0.0324 216  PHE A O   
1391  C CB  . PHE A 218  ? 0.2928 0.2770 0.3295 -0.0082 -0.0143 -0.0350 216  PHE A CB  
1392  C CG  . PHE A 218  ? 0.3074 0.2862 0.3463 -0.0076 -0.0157 -0.0374 216  PHE A CG  
1393  C CD1 . PHE A 218  ? 0.3742 0.3537 0.4152 -0.0065 -0.0184 -0.0429 216  PHE A CD1 
1394  C CD2 . PHE A 218  ? 0.2927 0.2659 0.3316 -0.0081 -0.0144 -0.0343 216  PHE A CD2 
1395  C CE1 . PHE A 218  ? 0.3902 0.3644 0.4334 -0.0057 -0.0200 -0.0452 216  PHE A CE1 
1396  C CE2 . PHE A 218  ? 0.3475 0.3155 0.3883 -0.0073 -0.0159 -0.0363 216  PHE A CE2 
1397  C CZ  . PHE A 218  ? 0.3244 0.2927 0.3675 -0.0061 -0.0187 -0.0418 216  PHE A CZ  
1398  N N   . SER A 219  ? 0.2536 0.2399 0.2902 -0.0115 -0.0110 -0.0262 217  SER A N   
1399  C CA  . SER A 219  ? 0.2517 0.2419 0.2853 -0.0113 -0.0092 -0.0230 217  SER A CA  
1400  C C   . SER A 219  ? 0.2464 0.2356 0.2760 -0.0101 -0.0072 -0.0207 217  SER A C   
1401  O O   . SER A 219  ? 0.2524 0.2383 0.2817 -0.0095 -0.0072 -0.0217 217  SER A O   
1402  C CB  . SER A 219  ? 0.2779 0.2671 0.3141 -0.0133 -0.0083 -0.0198 217  SER A CB  
1403  O OG  . SER A 219  ? 0.2818 0.2654 0.3193 -0.0143 -0.0071 -0.0173 217  SER A OG  
1404  N N   . TYR A 220  ? 0.2515 0.2435 0.2783 -0.0099 -0.0056 -0.0177 218  TYR A N   
1405  C CA  . TYR A 220  ? 0.2240 0.2158 0.2469 -0.0088 -0.0039 -0.0156 218  TYR A CA  
1406  C C   . TYR A 220  ? 0.2330 0.2236 0.2551 -0.0094 -0.0020 -0.0112 218  TYR A C   
1407  O O   . TYR A 220  ? 0.2400 0.2324 0.2634 -0.0102 -0.0020 -0.0099 218  TYR A O   
1408  C CB  . TYR A 220  ? 0.2610 0.2585 0.2804 -0.0074 -0.0042 -0.0169 218  TYR A CB  
1409  C CG  . TYR A 220  ? 0.2530 0.2515 0.2720 -0.0061 -0.0055 -0.0211 218  TYR A CG  
1410  C CD1 . TYR A 220  ? 0.2611 0.2617 0.2822 -0.0060 -0.0077 -0.0252 218  TYR A CD1 
1411  C CD2 . TYR A 220  ? 0.2763 0.2737 0.2930 -0.0051 -0.0046 -0.0211 218  TYR A CD2 
1412  C CE1 . TYR A 220  ? 0.2832 0.2848 0.3042 -0.0046 -0.0089 -0.0294 218  TYR A CE1 
1413  C CE2 . TYR A 220  ? 0.2846 0.2832 0.3011 -0.0037 -0.0057 -0.0252 218  TYR A CE2 
1414  C CZ  . TYR A 220  ? 0.2949 0.2957 0.3136 -0.0034 -0.0079 -0.0294 218  TYR A CZ  
1415  O OH  . TYR A 220  ? 0.3006 0.3027 0.3193 -0.0018 -0.0092 -0.0338 218  TYR A OH  
1416  N N   . SER A 221  ? 0.2286 0.2164 0.2487 -0.0090 -0.0004 -0.0092 219  SER A N   
1417  C CA  . SER A 221  ? 0.2375 0.2247 0.2559 -0.0091 0.0014  -0.0054 219  SER A CA  
1418  C C   . SER A 221  ? 0.2325 0.2208 0.2472 -0.0079 0.0022  -0.0048 219  SER A C   
1419  O O   . SER A 221  ? 0.2651 0.2510 0.2790 -0.0074 0.0025  -0.0056 219  SER A O   
1420  C CB  . SER A 221  ? 0.2590 0.2415 0.2793 -0.0100 0.0025  -0.0034 219  SER A CB  
1421  O OG  . SER A 221  ? 0.2856 0.2680 0.3044 -0.0099 0.0041  -0.0002 219  SER A OG  
1422  N N   . TYR A 222  ? 0.2454 0.2372 0.2577 -0.0075 0.0025  -0.0032 220  TYR A N   
1423  C CA  . TYR A 222  ? 0.2248 0.2184 0.2336 -0.0066 0.0031  -0.0026 220  TYR A CA  
1424  C C   . TYR A 222  ? 0.2537 0.2443 0.2614 -0.0066 0.0047  0.0006  220  TYR A C   
1425  O O   . TYR A 222  ? 0.2512 0.2406 0.2597 -0.0071 0.0053  0.0029  220  TYR A O   
1426  C CB  . TYR A 222  ? 0.2387 0.2379 0.2456 -0.0063 0.0024  -0.0023 220  TYR A CB  
1427  C CG  . TYR A 222  ? 0.2436 0.2463 0.2514 -0.0060 0.0008  -0.0058 220  TYR A CG  
1428  C CD1 . TYR A 222  ? 0.2273 0.2322 0.2338 -0.0052 0.0002  -0.0088 220  TYR A CD1 
1429  C CD2 . TYR A 222  ? 0.2167 0.2207 0.2270 -0.0066 -0.0004 -0.0065 220  TYR A CD2 
1430  C CE1 . TYR A 222  ? 0.2411 0.2493 0.2487 -0.0048 -0.0015 -0.0125 220  TYR A CE1 
1431  C CE2 . TYR A 222  ? 0.2127 0.2198 0.2240 -0.0064 -0.0021 -0.0101 220  TYR A CE2 
1432  C CZ  . TYR A 222  ? 0.2254 0.2345 0.2353 -0.0054 -0.0026 -0.0131 220  TYR A CZ  
1433  O OH  . TYR A 222  ? 0.2536 0.2660 0.2646 -0.0050 -0.0045 -0.0171 220  TYR A OH  
1434  N N   . ASP A 223  ? 0.2589 0.2483 0.2648 -0.0061 0.0054  0.0004  221  ASP A N   
1435  C CA  . ASP A 223  ? 0.2903 0.2770 0.2950 -0.0061 0.0068  0.0029  221  ASP A CA  
1436  C C   . ASP A 223  ? 0.3178 0.3078 0.3195 -0.0057 0.0070  0.0040  221  ASP A C   
1437  O O   . ASP A 223  ? 0.3123 0.3042 0.3127 -0.0052 0.0069  0.0023  221  ASP A O   
1438  C CB  . ASP A 223  ? 0.2943 0.2770 0.2996 -0.0059 0.0072  0.0019  221  ASP A CB  
1439  C CG  . ASP A 223  ? 0.3684 0.3488 0.3721 -0.0057 0.0086  0.0041  221  ASP A CG  
1440  O OD1 . ASP A 223  ? 0.3872 0.3681 0.3898 -0.0058 0.0092  0.0065  221  ASP A OD1 
1441  O OD2 . ASP A 223  ? 0.4670 0.4449 0.4707 -0.0053 0.0088  0.0033  221  ASP A OD2 
1442  N N   . MET A 224  ? 0.2957 0.2866 0.2966 -0.0059 0.0073  0.0067  222  MET A N   
1443  C CA  . MET A 224  ? 0.3041 0.2973 0.3024 -0.0059 0.0076  0.0085  222  MET A CA  
1444  C C   . MET A 224  ? 0.3545 0.3443 0.3522 -0.0058 0.0087  0.0095  222  MET A C   
1445  O O   . MET A 224  ? 0.4834 0.4696 0.4819 -0.0060 0.0093  0.0112  222  MET A O   
1446  C CB  . MET A 224  ? 0.3147 0.3091 0.3127 -0.0062 0.0072  0.0112  222  MET A CB  
1447  C CG  . MET A 224  ? 0.3378 0.3353 0.3369 -0.0062 0.0060  0.0102  222  MET A CG  
1448  S SD  . MET A 224  ? 0.4031 0.4068 0.4004 -0.0060 0.0050  0.0078  222  MET A SD  
1449  C CE  . MET A 224  ? 0.3625 0.3694 0.3566 -0.0063 0.0052  0.0111  222  MET A CE  
1450  N N   . LEU A 225  ? 0.3768 0.3679 0.3732 -0.0055 0.0090  0.0082  223  LEU A N   
1451  C CA  . LEU A 225  ? 0.4309 0.4189 0.4269 -0.0053 0.0099  0.0087  223  LEU A CA  
1452  C C   . LEU A 225  ? 0.4700 0.4564 0.4653 -0.0058 0.0105  0.0118  223  LEU A C   
1453  O O   . LEU A 225  ? 0.5449 0.5341 0.5386 -0.0062 0.0104  0.0135  223  LEU A O   
1454  C CB  . LEU A 225  ? 0.3871 0.3780 0.3818 -0.0049 0.0100  0.0068  223  LEU A CB  
1455  C CG  . LEU A 225  ? 0.3658 0.3570 0.3617 -0.0042 0.0092  0.0032  223  LEU A CG  
1456  C CD1 . LEU A 225  ? 0.3708 0.3658 0.3655 -0.0034 0.0091  0.0009  223  LEU A CD1 
1457  C CD2 . LEU A 225  ? 0.3830 0.3687 0.3809 -0.0040 0.0094  0.0027  223  LEU A CD2 
1458  N N   . GLY A 226  ? 0.4317 0.4138 0.4281 -0.0057 0.0111  0.0127  224  GLY A N   
1459  C CA  . GLY A 226  ? 0.4456 0.4258 0.4419 -0.0059 0.0114  0.0153  224  GLY A CA  
1460  C C   . GLY A 226  ? 0.3819 0.3579 0.3795 -0.0056 0.0121  0.0154  224  GLY A C   
1461  O O   . GLY A 226  ? 0.3729 0.3477 0.3720 -0.0056 0.0121  0.0145  224  GLY A O   
1462  N N   . GLU A 227  ? 0.3626 0.3365 0.3594 -0.0055 0.0127  0.0164  225  GLU A N   
1463  C CA  . GLU A 227  ? 0.3150 0.2854 0.3127 -0.0051 0.0134  0.0167  225  GLU A CA  
1464  C C   . GLU A 227  ? 0.3262 0.2952 0.3230 -0.0050 0.0137  0.0179  225  GLU A C   
1465  O O   . GLU A 227  ? 0.3301 0.3006 0.3257 -0.0054 0.0134  0.0185  225  GLU A O   
1466  C CB  . GLU A 227  ? 0.3427 0.3116 0.3408 -0.0049 0.0138  0.0151  225  GLU A CB  
1467  C CG  . GLU A 227  ? 0.4377 0.4071 0.4345 -0.0047 0.0139  0.0140  225  GLU A CG  
1468  C CD  . GLU A 227  ? 0.4417 0.4094 0.4393 -0.0044 0.0139  0.0124  225  GLU A CD  
1469  O OE1 . GLU A 227  ? 0.4876 0.4525 0.4852 -0.0041 0.0145  0.0128  225  GLU A OE1 
1470  O OE2 . GLU A 227  ? 0.4551 0.4242 0.4533 -0.0044 0.0133  0.0107  225  GLU A OE2 
1471  N N   . ALA A 228  ? 0.2913 0.2577 0.2887 -0.0046 0.0142  0.0183  226  ALA A N   
1472  C CA  . ALA A 228  ? 0.3154 0.2800 0.3121 -0.0043 0.0144  0.0191  226  ALA A CA  
1473  C C   . ALA A 228  ? 0.3077 0.2731 0.3041 -0.0048 0.0137  0.0206  226  ALA A C   
1474  O O   . ALA A 228  ? 0.3150 0.2807 0.3104 -0.0052 0.0136  0.0210  226  ALA A O   
1475  C CB  . ALA A 228  ? 0.2852 0.2492 0.2808 -0.0043 0.0149  0.0181  226  ALA A CB  
1476  N N   . ALA A 229  ? 0.2807 0.2464 0.2779 -0.0048 0.0130  0.0215  227  ALA A N   
1477  C CA  . ALA A 229  ? 0.2727 0.2385 0.2699 -0.0052 0.0120  0.0233  227  ALA A CA  
1478  C C   . ALA A 229  ? 0.2676 0.2307 0.2648 -0.0050 0.0120  0.0237  227  ALA A C   
1479  O O   . ALA A 229  ? 0.2342 0.1953 0.2321 -0.0041 0.0125  0.0228  227  ALA A O   
1480  C CB  . ALA A 229  ? 0.2610 0.2270 0.2595 -0.0048 0.0111  0.0242  227  ALA A CB  
1481  N N   . THR A 230  ? 0.2417 0.2052 0.2383 -0.0058 0.0115  0.0250  228  THR A N   
1482  C CA  . THR A 230  ? 0.2858 0.2468 0.2826 -0.0059 0.0112  0.0253  228  THR A CA  
1483  C C   . THR A 230  ? 0.2691 0.2283 0.2672 -0.0059 0.0098  0.0270  228  THR A C   
1484  O O   . THR A 230  ? 0.2806 0.2371 0.2797 -0.0054 0.0094  0.0267  228  THR A O   
1485  C CB  . THR A 230  ? 0.3040 0.2667 0.2997 -0.0070 0.0114  0.0257  228  THR A CB  
1486  O OG1 . THR A 230  ? 0.3977 0.3621 0.3924 -0.0067 0.0125  0.0240  228  THR A OG1 
1487  C CG2 . THR A 230  ? 0.3785 0.3388 0.3747 -0.0071 0.0111  0.0259  228  THR A CG2 
1488  N N   . THR A 231  ? 0.2593 0.2200 0.2577 -0.0064 0.0089  0.0286  229  THR A N   
1489  C CA  . THR A 231  ? 0.2596 0.2184 0.2593 -0.0065 0.0073  0.0305  229  THR A CA  
1490  C C   . THR A 231  ? 0.2104 0.1700 0.2109 -0.0058 0.0066  0.0310  229  THR A C   
1491  O O   . THR A 231  ? 0.2414 0.2036 0.2412 -0.0057 0.0074  0.0301  229  THR A O   
1492  C CB  . THR A 231  ? 0.2997 0.2597 0.2988 -0.0084 0.0064  0.0331  229  THR A CB  
1493  O OG1 . THR A 231  ? 0.2751 0.2391 0.2730 -0.0091 0.0066  0.0339  229  THR A OG1 
1494  C CG2 . THR A 231  ? 0.2748 0.2350 0.2732 -0.0093 0.0072  0.0326  229  THR A CG2 
1495  N N   . ALA A 232  ? 0.2492 0.2065 0.2514 -0.0053 0.0050  0.0322  230  ALA A N   
1496  C CA  . ALA A 232  ? 0.2481 0.2064 0.2511 -0.0046 0.0041  0.0329  230  ALA A CA  
1497  C C   . ALA A 232  ? 0.2852 0.2473 0.2868 -0.0060 0.0039  0.0346  230  ALA A C   
1498  O O   . ALA A 232  ? 0.2642 0.2288 0.2656 -0.0056 0.0041  0.0341  230  ALA A O   
1499  C CB  . ALA A 232  ? 0.2616 0.2167 0.2668 -0.0039 0.0021  0.0342  230  ALA A CB  
1500  N N   . ALA A 233  ? 0.2898 0.2527 0.2902 -0.0076 0.0036  0.0366  231  ALA A N   
1501  C CA  . ALA A 233  ? 0.3100 0.2771 0.3088 -0.0089 0.0034  0.0383  231  ALA A CA  
1502  C C   . ALA A 233  ? 0.3047 0.2755 0.3020 -0.0088 0.0050  0.0360  231  ALA A C   
1503  O O   . ALA A 233  ? 0.3086 0.2829 0.3052 -0.0089 0.0048  0.0361  231  ALA A O   
1504  C CB  . ALA A 233  ? 0.3309 0.2988 0.3288 -0.0108 0.0029  0.0409  231  ALA A CB  
1505  N N   . ASP A 234  ? 0.2787 0.2487 0.2757 -0.0085 0.0064  0.0338  232  ASP A N   
1506  C CA  . ASP A 234  ? 0.2904 0.2631 0.2863 -0.0083 0.0077  0.0314  232  ASP A CA  
1507  C C   . ASP A 234  ? 0.2392 0.2117 0.2362 -0.0071 0.0078  0.0299  232  ASP A C   
1508  O O   . ASP A 234  ? 0.2573 0.2328 0.2537 -0.0072 0.0081  0.0288  232  ASP A O   
1509  C CB  . ASP A 234  ? 0.2849 0.2564 0.2804 -0.0082 0.0090  0.0297  232  ASP A CB  
1510  C CG  . ASP A 234  ? 0.3607 0.3341 0.3549 -0.0096 0.0092  0.0307  232  ASP A CG  
1511  O OD1 . ASP A 234  ? 0.4359 0.4126 0.4292 -0.0107 0.0086  0.0325  232  ASP A OD1 
1512  O OD2 . ASP A 234  ? 0.5331 0.5050 0.5273 -0.0096 0.0099  0.0298  232  ASP A OD2 
1513  N N   . ALA A 235  ? 0.2414 0.2107 0.2401 -0.0061 0.0076  0.0296  233  ALA A N   
1514  C CA  . ALA A 235  ? 0.2543 0.2239 0.2544 -0.0050 0.0077  0.0282  233  ALA A CA  
1515  C C   . ALA A 235  ? 0.2709 0.2431 0.2712 -0.0051 0.0065  0.0295  233  ALA A C   
1516  O O   . ALA A 235  ? 0.2331 0.2076 0.2338 -0.0049 0.0066  0.0282  233  ALA A O   
1517  C CB  . ALA A 235  ? 0.2470 0.2133 0.2488 -0.0038 0.0077  0.0277  233  ALA A CB  
1518  N N   . GLU A 236  ? 0.2552 0.2269 0.2555 -0.0055 0.0051  0.0320  234  GLU A N   
1519  C CA  . GLU A 236  ? 0.3077 0.2819 0.3080 -0.0056 0.0037  0.0336  234  GLU A CA  
1520  C C   . GLU A 236  ? 0.2669 0.2458 0.2651 -0.0066 0.0040  0.0334  234  GLU A C   
1521  O O   . GLU A 236  ? 0.2597 0.2416 0.2580 -0.0064 0.0035  0.0331  234  GLU A O   
1522  C CB  . GLU A 236  ? 0.2968 0.2691 0.2974 -0.0059 0.0020  0.0367  234  GLU A CB  
1523  C CG  . GLU A 236  ? 0.4144 0.3888 0.4153 -0.0058 0.0002  0.0387  234  GLU A CG  
1524  C CD  . GLU A 236  ? 0.4708 0.4454 0.4736 -0.0042 -0.0002 0.0372  234  GLU A CD  
1525  O OE1 . GLU A 236  ? 0.5129 0.4845 0.5177 -0.0029 0.0001  0.0358  234  GLU A OE1 
1526  O OE2 . GLU A 236  ? 0.4566 0.4347 0.4591 -0.0042 -0.0008 0.0374  234  GLU A OE2 
1527  N N   . ARG A 237  ? 0.2651 0.2450 0.2616 -0.0076 0.0049  0.0334  235  ARG A N   
1528  C CA  . ARG A 237  ? 0.3013 0.2861 0.2959 -0.0084 0.0053  0.0327  235  ARG A CA  
1529  C C   . ARG A 237  ? 0.2881 0.2740 0.2832 -0.0077 0.0061  0.0294  235  ARG A C   
1530  O O   . ARG A 237  ? 0.2918 0.2815 0.2863 -0.0077 0.0057  0.0286  235  ARG A O   
1531  C CB  . ARG A 237  ? 0.2923 0.2780 0.2853 -0.0095 0.0061  0.0330  235  ARG A CB  
1532  C CG  . ARG A 237  ? 0.3632 0.3543 0.3543 -0.0099 0.0067  0.0317  235  ARG A CG  
1533  C CD  . ARG A 237  ? 0.4214 0.4146 0.4109 -0.0112 0.0072  0.0329  235  ARG A CD  
1534  N NE  . ARG A 237  ? 0.5010 0.4906 0.4912 -0.0111 0.0081  0.0319  235  ARG A NE  
1535  C CZ  . ARG A 237  ? 0.5632 0.5527 0.5534 -0.0104 0.0092  0.0289  235  ARG A CZ  
1536  N NH1 . ARG A 237  ? 0.5955 0.5880 0.5852 -0.0098 0.0095  0.0265  235  ARG A NH1 
1537  N NH2 . ARG A 237  ? 0.5191 0.5051 0.5099 -0.0102 0.0099  0.0284  235  ARG A NH2 
1538  N N   . TYR A 238  ? 0.2509 0.2336 0.2470 -0.0071 0.0071  0.0275  236  TYR A N   
1539  C CA  . TYR A 238  ? 0.2239 0.2072 0.2209 -0.0066 0.0077  0.0247  236  TYR A CA  
1540  C C   . TYR A 238  ? 0.2493 0.2333 0.2480 -0.0060 0.0069  0.0247  236  TYR A C   
1541  O O   . TYR A 238  ? 0.2795 0.2659 0.2786 -0.0060 0.0068  0.0229  236  TYR A O   
1542  C CB  . TYR A 238  ? 0.2257 0.2054 0.2235 -0.0061 0.0090  0.0233  236  TYR A CB  
1543  C CG  . TYR A 238  ? 0.2551 0.2344 0.2514 -0.0065 0.0098  0.0228  236  TYR A CG  
1544  C CD1 . TYR A 238  ? 0.3511 0.3341 0.3459 -0.0070 0.0098  0.0221  236  TYR A CD1 
1545  C CD2 . TYR A 238  ? 0.2616 0.2376 0.2582 -0.0063 0.0105  0.0229  236  TYR A CD2 
1546  C CE1 . TYR A 238  ? 0.3828 0.3660 0.3765 -0.0073 0.0105  0.0215  236  TYR A CE1 
1547  C CE2 . TYR A 238  ? 0.2975 0.2734 0.2928 -0.0066 0.0112  0.0224  236  TYR A CE2 
1548  C CZ  . TYR A 238  ? 0.3645 0.3440 0.3585 -0.0071 0.0112  0.0217  236  TYR A CZ  
1549  O OH  . TYR A 238  ? 0.4280 0.4079 0.4211 -0.0073 0.0118  0.0211  236  TYR A OH  
1550  N N   . TYR A 239  ? 0.2370 0.2190 0.2369 -0.0055 0.0062  0.0264  237  TYR A N   
1551  C CA  . TYR A 239  ? 0.2701 0.2532 0.2718 -0.0048 0.0053  0.0263  237  TYR A CA  
1552  C C   . TYR A 239  ? 0.2546 0.2419 0.2551 -0.0052 0.0041  0.0270  237  TYR A C   
1553  O O   . TYR A 239  ? 0.2223 0.2121 0.2237 -0.0050 0.0038  0.0254  237  TYR A O   
1554  C CB  . TYR A 239  ? 0.2646 0.2450 0.2677 -0.0040 0.0045  0.0281  237  TYR A CB  
1555  C CG  . TYR A 239  ? 0.2495 0.2314 0.2546 -0.0031 0.0035  0.0278  237  TYR A CG  
1556  C CD1 . TYR A 239  ? 0.2621 0.2466 0.2668 -0.0031 0.0019  0.0294  237  TYR A CD1 
1557  C CD2 . TYR A 239  ? 0.2568 0.2380 0.2641 -0.0024 0.0042  0.0261  237  TYR A CD2 
1558  C CE1 . TYR A 239  ? 0.3056 0.2918 0.3123 -0.0023 0.0009  0.0291  237  TYR A CE1 
1559  C CE2 . TYR A 239  ? 0.2528 0.2360 0.2622 -0.0017 0.0034  0.0257  237  TYR A CE2 
1560  C CZ  . TYR A 239  ? 0.3356 0.3211 0.3447 -0.0015 0.0017  0.0271  237  TYR A CZ  
1561  O OH  . TYR A 239  ? 0.3089 0.2966 0.3202 -0.0007 0.0007  0.0267  237  TYR A OH  
1562  N N   . ARG A 240  ? 0.2542 0.2428 0.2529 -0.0058 0.0034  0.0293  238  ARG A N   
1563  C CA  . ARG A 240  ? 0.2783 0.2716 0.2759 -0.0061 0.0022  0.0300  238  ARG A CA  
1564  C C   . ARG A 240  ? 0.2430 0.2400 0.2392 -0.0066 0.0029  0.0275  238  ARG A C   
1565  O O   . ARG A 240  ? 0.2507 0.2516 0.2466 -0.0065 0.0020  0.0268  238  ARG A O   
1566  C CB  . ARG A 240  ? 0.3157 0.3097 0.3117 -0.0068 0.0012  0.0336  238  ARG A CB  
1567  C CG  . ARG A 240  ? 0.3101 0.3043 0.3041 -0.0079 0.0020  0.0344  238  ARG A CG  
1568  C CD  . ARG A 240  ? 0.3051 0.3006 0.2978 -0.0089 0.0008  0.0384  238  ARG A CD  
1569  N NE  . ARG A 240  ? 0.3542 0.3499 0.3455 -0.0101 0.0017  0.0393  238  ARG A NE  
1570  C CZ  . ARG A 240  ? 0.3479 0.3391 0.3400 -0.0105 0.0018  0.0407  238  ARG A CZ  
1571  N NH1 . ARG A 240  ? 0.3242 0.3106 0.3184 -0.0096 0.0009  0.0414  238  ARG A NH1 
1572  N NH2 . ARG A 240  ? 0.3901 0.3822 0.3810 -0.0117 0.0027  0.0412  238  ARG A NH2 
1573  N N   . ASP A 241  ? 0.2598 0.2557 0.2554 -0.0069 0.0042  0.0259  239  ASP A N   
1574  C CA  . ASP A 241  ? 0.2453 0.2441 0.2403 -0.0069 0.0047  0.0229  239  ASP A CA  
1575  C C   . ASP A 241  ? 0.2541 0.2524 0.2514 -0.0064 0.0045  0.0204  239  ASP A C   
1576  O O   . ASP A 241  ? 0.2454 0.2472 0.2426 -0.0064 0.0039  0.0185  239  ASP A O   
1577  C CB  . ASP A 241  ? 0.3231 0.3201 0.3173 -0.0072 0.0060  0.0217  239  ASP A CB  
1578  C CG  . ASP A 241  ? 0.4204 0.4191 0.4124 -0.0079 0.0062  0.0238  239  ASP A CG  
1579  O OD1 . ASP A 241  ? 0.4515 0.4531 0.4424 -0.0084 0.0053  0.0262  239  ASP A OD1 
1580  O OD2 . ASP A 241  ? 0.4611 0.4582 0.4527 -0.0081 0.0072  0.0231  239  ASP A OD2 
1581  N N   . TYR A 242  ? 0.2050 0.1992 0.2044 -0.0061 0.0051  0.0203  240  TYR A N   
1582  C CA  . TYR A 242  ? 0.2164 0.2103 0.2182 -0.0058 0.0050  0.0184  240  TYR A CA  
1583  C C   . TYR A 242  ? 0.2054 0.2024 0.2080 -0.0056 0.0036  0.0189  240  TYR A C   
1584  O O   . TYR A 242  ? 0.2183 0.2177 0.2220 -0.0056 0.0030  0.0169  240  TYR A O   
1585  C CB  . TYR A 242  ? 0.2196 0.2093 0.2234 -0.0055 0.0059  0.0186  240  TYR A CB  
1586  C CG  . TYR A 242  ? 0.2182 0.2048 0.2216 -0.0057 0.0073  0.0176  240  TYR A CG  
1587  C CD1 . TYR A 242  ? 0.2505 0.2379 0.2533 -0.0060 0.0076  0.0155  240  TYR A CD1 
1588  C CD2 . TYR A 242  ? 0.2250 0.2081 0.2289 -0.0054 0.0082  0.0187  240  TYR A CD2 
1589  C CE1 . TYR A 242  ? 0.2797 0.2641 0.2824 -0.0061 0.0086  0.0148  240  TYR A CE1 
1590  C CE2 . TYR A 242  ? 0.2397 0.2202 0.2432 -0.0055 0.0093  0.0179  240  TYR A CE2 
1591  C CZ  . TYR A 242  ? 0.2368 0.2179 0.2397 -0.0059 0.0095  0.0161  240  TYR A CZ  
1592  O OH  . TYR A 242  ? 0.2267 0.2050 0.2293 -0.0058 0.0105  0.0154  240  TYR A OH  
1593  N N   . GLU A 243  ? 0.2064 0.2032 0.2087 -0.0052 0.0028  0.0216  241  GLU A N   
1594  C CA  . GLU A 243  ? 0.2076 0.2071 0.2109 -0.0048 0.0013  0.0223  241  GLU A CA  
1595  C C   . GLU A 243  ? 0.2335 0.2382 0.2351 -0.0051 0.0003  0.0217  241  GLU A C   
1596  O O   . GLU A 243  ? 0.2093 0.2168 0.2120 -0.0049 -0.0006 0.0201  241  GLU A O   
1597  C CB  . GLU A 243  ? 0.2184 0.2163 0.2217 -0.0042 0.0005  0.0255  241  GLU A CB  
1598  C CG  . GLU A 243  ? 0.2272 0.2281 0.2311 -0.0037 -0.0014 0.0267  241  GLU A CG  
1599  C CD  . GLU A 243  ? 0.2890 0.2880 0.2926 -0.0032 -0.0026 0.0302  241  GLU A CD  
1600  O OE1 . GLU A 243  ? 0.3656 0.3630 0.3674 -0.0038 -0.0023 0.0320  241  GLU A OE1 
1601  O OE2 . GLU A 243  ? 0.3284 0.3276 0.3338 -0.0022 -0.0039 0.0310  241  GLU A OE2 
1602  N N   . SER A 244  ? 0.2395 0.2457 0.2381 -0.0056 0.0005  0.0226  242  SER A N   
1603  C CA  . SER A 244  ? 0.2440 0.2558 0.2406 -0.0059 -0.0004 0.0219  242  SER A CA  
1604  C C   . SER A 244  ? 0.2420 0.2555 0.2395 -0.0059 -0.0001 0.0178  242  SER A C   
1605  O O   . SER A 244  ? 0.2358 0.2536 0.2332 -0.0057 -0.0012 0.0162  242  SER A O   
1606  C CB  . SER A 244  ? 0.2599 0.2735 0.2534 -0.0065 0.0000  0.0238  242  SER A CB  
1607  O OG  . SER A 244  ? 0.2917 0.3032 0.2848 -0.0068 0.0015  0.0224  242  SER A OG  
1608  N N   . ALA A 245  ? 0.2321 0.2419 0.2306 -0.0060 0.0013  0.0160  243  ALA A N   
1609  C CA  . ALA A 245  ? 0.2221 0.2325 0.2218 -0.0060 0.0013  0.0122  243  ALA A CA  
1610  C C   . ALA A 245  ? 0.2083 0.2185 0.2110 -0.0059 0.0005  0.0109  243  ALA A C   
1611  O O   . ALA A 245  ? 0.2145 0.2274 0.2181 -0.0060 -0.0003 0.0081  243  ALA A O   
1612  C CB  . ALA A 245  ? 0.2475 0.2536 0.2476 -0.0061 0.0028  0.0111  243  ALA A CB  
1613  N N   . ILE A 246  ? 0.2073 0.2147 0.2120 -0.0058 0.0008  0.0127  244  ILE A N   
1614  C CA  . ILE A 246  ? 0.2072 0.2151 0.2150 -0.0058 0.0001  0.0115  244  ILE A CA  
1615  C C   . ILE A 246  ? 0.2237 0.2369 0.2311 -0.0056 -0.0017 0.0112  244  ILE A C   
1616  O O   . ILE A 246  ? 0.2111 0.2264 0.2204 -0.0058 -0.0025 0.0087  244  ILE A O   
1617  C CB  . ILE A 246  ? 0.2061 0.2109 0.2159 -0.0055 0.0007  0.0135  244  ILE A CB  
1618  C CG1 . ILE A 246  ? 0.2046 0.2048 0.2150 -0.0058 0.0024  0.0133  244  ILE A CG1 
1619  C CG2 . ILE A 246  ? 0.2393 0.2459 0.2524 -0.0055 -0.0002 0.0126  244  ILE A CG2 
1620  C CD1 . ILE A 246  ? 0.2226 0.2200 0.2347 -0.0054 0.0031  0.0151  244  ILE A CD1 
1621  N N   . HIS A 247  ? 0.2295 0.2448 0.2345 -0.0052 -0.0023 0.0138  245  HIS A N   
1622  C CA  . HIS A 247  ? 0.2164 0.2370 0.2205 -0.0049 -0.0041 0.0137  245  HIS A CA  
1623  C C   . HIS A 247  ? 0.2289 0.2535 0.2319 -0.0051 -0.0045 0.0104  245  HIS A C   
1624  O O   . HIS A 247  ? 0.2505 0.2786 0.2546 -0.0050 -0.0059 0.0083  245  HIS A O   
1625  C CB  . HIS A 247  ? 0.2440 0.2661 0.2455 -0.0046 -0.0048 0.0174  245  HIS A CB  
1626  C CG  . HIS A 247  ? 0.2135 0.2329 0.2167 -0.0040 -0.0051 0.0202  245  HIS A CG  
1627  N ND1 . HIS A 247  ? 0.2298 0.2507 0.2353 -0.0034 -0.0065 0.0202  245  HIS A ND1 
1628  C CD2 . HIS A 247  ? 0.2373 0.2525 0.2402 -0.0039 -0.0046 0.0230  245  HIS A CD2 
1629  C CE1 . HIS A 247  ? 0.2716 0.2895 0.2783 -0.0027 -0.0066 0.0226  245  HIS A CE1 
1630  N NE2 . HIS A 247  ? 0.2388 0.2531 0.2440 -0.0030 -0.0055 0.0243  245  HIS A NE2 
1631  N N   . ALA A 248  ? 0.2230 0.2472 0.2238 -0.0053 -0.0036 0.0098  246  ALA A N   
1632  C CA  . ALA A 248  ? 0.2446 0.2728 0.2442 -0.0053 -0.0041 0.0064  246  ALA A CA  
1633  C C   . ALA A 248  ? 0.2702 0.2969 0.2730 -0.0054 -0.0043 0.0025  246  ALA A C   
1634  O O   . ALA A 248  ? 0.2323 0.2630 0.2356 -0.0053 -0.0057 -0.0005 246  ALA A O   
1635  C CB  . ALA A 248  ? 0.2475 0.2756 0.2443 -0.0053 -0.0029 0.0066  246  ALA A CB  
1636  N N   . ILE A 249  ? 0.2409 0.2619 0.2460 -0.0058 -0.0032 0.0024  247  ILE A N   
1637  C CA  . ILE A 249  ? 0.2332 0.2521 0.2417 -0.0063 -0.0034 -0.0007 247  ILE A CA  
1638  C C   . ILE A 249  ? 0.2152 0.2360 0.2265 -0.0065 -0.0047 -0.0011 247  ILE A C   
1639  O O   . ILE A 249  ? 0.2390 0.2613 0.2525 -0.0068 -0.0059 -0.0043 247  ILE A O   
1640  C CB  . ILE A 249  ? 0.2217 0.2345 0.2317 -0.0068 -0.0018 0.0002  247  ILE A CB  
1641  C CG1 . ILE A 249  ? 0.2410 0.2521 0.2484 -0.0065 -0.0007 0.0003  247  ILE A CG1 
1642  C CG2 . ILE A 249  ? 0.2200 0.2304 0.2339 -0.0075 -0.0022 -0.0024 247  ILE A CG2 
1643  C CD1 . ILE A 249  ? 0.2077 0.2133 0.2157 -0.0067 0.0010  0.0025  247  ILE A CD1 
1644  N N   . GLY A 250  ? 0.2112 0.2320 0.2229 -0.0064 -0.0046 0.0019  248  GLY A N   
1645  C CA  . GLY A 250  ? 0.2371 0.2600 0.2516 -0.0065 -0.0058 0.0015  248  GLY A CA  
1646  C C   . GLY A 250  ? 0.2211 0.2500 0.2344 -0.0060 -0.0078 0.0000  248  GLY A C   
1647  O O   . GLY A 250  ? 0.2181 0.2492 0.2341 -0.0064 -0.0090 -0.0024 248  GLY A O   
1648  N N   . LYS A 251  ? 0.2257 0.2577 0.2351 -0.0054 -0.0080 0.0014  249  LYS A N   
1649  C CA  . LYS A 251  ? 0.2318 0.2702 0.2396 -0.0049 -0.0098 -0.0001 249  LYS A CA  
1650  C C   . LYS A 251  ? 0.2446 0.2845 0.2532 -0.0051 -0.0104 -0.0049 249  LYS A C   
1651  O O   . LYS A 251  ? 0.2445 0.2885 0.2544 -0.0050 -0.0122 -0.0075 249  LYS A O   
1652  C CB  . LYS A 251  ? 0.2650 0.3064 0.2682 -0.0045 -0.0096 0.0024  249  LYS A CB  
1653  C CG  . LYS A 251  ? 0.2678 0.3090 0.2698 -0.0042 -0.0098 0.0070  249  LYS A CG  
1654  C CD  . LYS A 251  ? 0.3116 0.3563 0.3091 -0.0041 -0.0098 0.0091  249  LYS A CD  
1655  C CE  . LYS A 251  ? 0.3556 0.3984 0.3518 -0.0040 -0.0096 0.0141  249  LYS A CE  
1656  N NZ  . LYS A 251  ? 0.2905 0.3365 0.2825 -0.0043 -0.0092 0.0159  249  LYS A NZ  
1657  N N   . ALA A 252  ? 0.2195 0.2563 0.2276 -0.0053 -0.0093 -0.0063 250  ALA A N   
1658  C CA  . ALA A 252  ? 0.2253 0.2629 0.2346 -0.0053 -0.0100 -0.0110 250  ALA A CA  
1659  C C   . ALA A 252  ? 0.2822 0.3166 0.2964 -0.0062 -0.0106 -0.0131 250  ALA A C   
1660  O O   . ALA A 252  ? 0.3078 0.3443 0.3239 -0.0063 -0.0122 -0.0170 250  ALA A O   
1661  C CB  . ALA A 252  ? 0.2578 0.2925 0.2655 -0.0051 -0.0087 -0.0117 250  ALA A CB  
1662  N N   . SER A 253  ? 0.2312 0.2607 0.2477 -0.0070 -0.0094 -0.0106 251  SER A N   
1663  C CA  . SER A 253  ? 0.2589 0.2857 0.2801 -0.0081 -0.0098 -0.0122 251  SER A CA  
1664  C C   . SER A 253  ? 0.2906 0.3221 0.3139 -0.0082 -0.0118 -0.0139 251  SER A C   
1665  O O   . SER A 253  ? 0.2746 0.3061 0.3013 -0.0090 -0.0131 -0.0172 251  SER A O   
1666  C CB  . SER A 253  ? 0.2416 0.2640 0.2646 -0.0087 -0.0082 -0.0088 251  SER A CB  
1667  O OG  . SER A 253  ? 0.2564 0.2773 0.2839 -0.0100 -0.0086 -0.0101 251  SER A OG  
1668  N N   . ALA A 254  ? 0.2586 0.2942 0.2802 -0.0075 -0.0123 -0.0117 252  ALA A N   
1669  C CA  . ALA A 254  ? 0.2807 0.3216 0.3034 -0.0073 -0.0144 -0.0132 252  ALA A CA  
1670  C C   . ALA A 254  ? 0.3016 0.3413 0.3297 -0.0085 -0.0150 -0.0145 252  ALA A C   
1671  O O   . ALA A 254  ? 0.2967 0.3393 0.3272 -0.0090 -0.0169 -0.0179 252  ALA A O   
1672  C CB  . ALA A 254  ? 0.3086 0.3542 0.3294 -0.0067 -0.0160 -0.0170 252  ALA A CB  
1673  N N   . GLY A 255  ? 0.2780 0.3137 0.3082 -0.0092 -0.0134 -0.0119 253  GLY A N   
1674  C CA  . GLY A 255  ? 0.2720 0.3072 0.3074 -0.0105 -0.0138 -0.0125 253  GLY A CA  
1675  C C   . GLY A 255  ? 0.2941 0.3257 0.3328 -0.0121 -0.0138 -0.0151 253  GLY A C   
1676  O O   . GLY A 255  ? 0.3116 0.3434 0.3548 -0.0135 -0.0144 -0.0160 253  GLY A O   
1677  N N   . ARG A 256  ? 0.2640 0.2921 0.3007 -0.0120 -0.0131 -0.0161 254  ARG A N   
1678  C CA  . ARG A 256  ? 0.2537 0.2777 0.2939 -0.0135 -0.0133 -0.0183 254  ARG A CA  
1679  C C   . ARG A 256  ? 0.2972 0.3167 0.3400 -0.0149 -0.0115 -0.0156 254  ARG A C   
1680  O O   . ARG A 256  ? 0.2878 0.3041 0.3342 -0.0165 -0.0118 -0.0168 254  ARG A O   
1681  C CB  . ARG A 256  ? 0.2384 0.2600 0.2758 -0.0127 -0.0132 -0.0202 254  ARG A CB  
1682  C CG  . ARG A 256  ? 0.2737 0.2990 0.3107 -0.0121 -0.0156 -0.0247 254  ARG A CG  
1683  C CD  . ARG A 256  ? 0.2896 0.3131 0.3239 -0.0110 -0.0154 -0.0266 254  ARG A CD  
1684  N NE  . ARG A 256  ? 0.3203 0.3460 0.3494 -0.0095 -0.0141 -0.0243 254  ARG A NE  
1685  C CZ  . ARG A 256  ? 0.3603 0.3850 0.3863 -0.0085 -0.0134 -0.0250 254  ARG A CZ  
1686  N NH1 . ARG A 256  ? 0.3615 0.3826 0.3891 -0.0086 -0.0138 -0.0278 254  ARG A NH1 
1687  N NH2 . ARG A 256  ? 0.3212 0.3488 0.3428 -0.0074 -0.0123 -0.0227 254  ARG A NH2 
1688  N N   . GLY A 257  ? 0.2706 0.2898 0.3119 -0.0143 -0.0097 -0.0119 255  GLY A N   
1689  C CA  . GLY A 257  ? 0.2736 0.2895 0.3172 -0.0155 -0.0080 -0.0095 255  GLY A CA  
1690  C C   . GLY A 257  ? 0.2504 0.2608 0.2923 -0.0156 -0.0064 -0.0084 255  GLY A C   
1691  O O   . GLY A 257  ? 0.2978 0.3068 0.3368 -0.0147 -0.0065 -0.0096 255  GLY A O   
1692  N N   . ILE A 258  ? 0.2658 0.2735 0.3097 -0.0167 -0.0047 -0.0062 256  ILE A N   
1693  C CA  . ILE A 258  ? 0.2495 0.2525 0.2912 -0.0165 -0.0030 -0.0045 256  ILE A CA  
1694  C C   . ILE A 258  ? 0.2448 0.2436 0.2878 -0.0176 -0.0035 -0.0062 256  ILE A C   
1695  O O   . ILE A 258  ? 0.2573 0.2524 0.2979 -0.0170 -0.0025 -0.0055 256  ILE A O   
1696  C CB  . ILE A 258  ? 0.2526 0.2546 0.2954 -0.0169 -0.0010 -0.0013 256  ILE A CB  
1697  C CG1 . ILE A 258  ? 0.2579 0.2604 0.3058 -0.0192 -0.0011 -0.0013 256  ILE A CG1 
1698  C CG2 . ILE A 258  ? 0.2075 0.2130 0.2487 -0.0154 -0.0006 0.0004  256  ILE A CG2 
1699  C CD1 . ILE A 258  ? 0.2925 0.2951 0.3416 -0.0196 0.0009  0.0016  256  ILE A CD1 
1700  N N   . TYR A 259  ? 0.2392 0.2384 0.2861 -0.0191 -0.0051 -0.0084 257  TYR A N   
1701  C CA  . TYR A 259  ? 0.2416 0.2362 0.2903 -0.0202 -0.0059 -0.0100 257  TYR A CA  
1702  C C   . TYR A 259  ? 0.2601 0.2552 0.3075 -0.0190 -0.0078 -0.0138 257  TYR A C   
1703  O O   . TYR A 259  ? 0.3237 0.3154 0.3692 -0.0183 -0.0078 -0.0147 257  TYR A O   
1704  C CB  . TYR A 259  ? 0.2879 0.2819 0.3421 -0.0228 -0.0066 -0.0100 257  TYR A CB  
1705  C CG  . TYR A 259  ? 0.2519 0.2466 0.3076 -0.0239 -0.0046 -0.0064 257  TYR A CG  
1706  C CD1 . TYR A 259  ? 0.2512 0.2427 0.3051 -0.0238 -0.0024 -0.0034 257  TYR A CD1 
1707  C CD2 . TYR A 259  ? 0.3085 0.3077 0.3673 -0.0249 -0.0049 -0.0061 257  TYR A CD2 
1708  C CE1 . TYR A 259  ? 0.2681 0.2609 0.3232 -0.0247 -0.0006 -0.0004 257  TYR A CE1 
1709  C CE2 . TYR A 259  ? 0.2768 0.2775 0.3371 -0.0257 -0.0030 -0.0030 257  TYR A CE2 
1710  C CZ  . TYR A 259  ? 0.2358 0.2333 0.2942 -0.0256 -0.0008 -0.0003 257  TYR A CZ  
1711  O OH  . TYR A 259  ? 0.2659 0.2654 0.3256 -0.0262 0.0010  0.0025  257  TYR A OH  
1712  N N   . GLU A 260  ? 0.2792 0.2789 0.3274 -0.0187 -0.0096 -0.0163 258  GLU A N   
1713  C CA  . GLU A 260  ? 0.3023 0.3033 0.3490 -0.0175 -0.0116 -0.0203 258  GLU A CA  
1714  C C   . GLU A 260  ? 0.3189 0.3224 0.3601 -0.0152 -0.0108 -0.0199 258  GLU A C   
1715  O O   . GLU A 260  ? 0.3613 0.3648 0.4005 -0.0140 -0.0116 -0.0226 258  GLU A O   
1716  C CB  . GLU A 260  ? 0.3385 0.3440 0.3881 -0.0180 -0.0139 -0.0233 258  GLU A CB  
1717  N N   . GLY A 261  ? 0.2744 0.2802 0.3133 -0.0146 -0.0092 -0.0167 259  GLY A N   
1718  C CA  . GLY A 261  ? 0.2171 0.2255 0.2511 -0.0127 -0.0086 -0.0159 259  GLY A CA  
1719  C C   . GLY A 261  ? 0.2764 0.2810 0.3076 -0.0122 -0.0066 -0.0133 259  GLY A C   
1720  O O   . GLY A 261  ? 0.2684 0.2685 0.3012 -0.0132 -0.0054 -0.0116 259  GLY A O   
1721  N N   . PRO A 262  ? 0.2401 0.2466 0.2670 -0.0107 -0.0061 -0.0129 260  PRO A N   
1722  C CA  . PRO A 262  ? 0.2135 0.2168 0.2377 -0.0101 -0.0043 -0.0108 260  PRO A CA  
1723  C C   . PRO A 262  ? 0.2415 0.2433 0.2652 -0.0103 -0.0026 -0.0068 260  PRO A C   
1724  O O   . PRO A 262  ? 0.2377 0.2421 0.2623 -0.0105 -0.0028 -0.0054 260  PRO A O   
1725  C CB  . PRO A 262  ? 0.2246 0.2317 0.2448 -0.0087 -0.0046 -0.0118 260  PRO A CB  
1726  C CG  . PRO A 262  ? 0.2567 0.2694 0.2767 -0.0085 -0.0059 -0.0121 260  PRO A CG  
1727  C CD  . PRO A 262  ? 0.2759 0.2882 0.3003 -0.0096 -0.0073 -0.0143 260  PRO A CD  
1728  N N   . GLY A 263  ? 0.2232 0.2211 0.2457 -0.0102 -0.0010 -0.0051 261  GLY A N   
1729  C CA  . GLY A 263  ? 0.2177 0.2141 0.2394 -0.0102 0.0006  -0.0016 261  GLY A CA  
1730  C C   . GLY A 263  ? 0.2276 0.2225 0.2457 -0.0092 0.0018  -0.0001 261  GLY A C   
1731  O O   . GLY A 263  ? 0.2080 0.2040 0.2240 -0.0086 0.0014  -0.0017 261  GLY A O   
1732  N N   . ILE A 264  ? 0.2180 0.2109 0.2354 -0.0091 0.0032  0.0027  262  ILE A N   
1733  C CA  . ILE A 264  ? 0.2117 0.2032 0.2261 -0.0084 0.0043  0.0043  262  ILE A CA  
1734  C C   . ILE A 264  ? 0.2340 0.2211 0.2491 -0.0087 0.0058  0.0057  262  ILE A C   
1735  O O   . ILE A 264  ? 0.2035 0.1896 0.2212 -0.0094 0.0061  0.0063  262  ILE A O   
1736  C CB  . ILE A 264  ? 0.2100 0.2038 0.2224 -0.0077 0.0043  0.0066  262  ILE A CB  
1737  C CG1 . ILE A 264  ? 0.2187 0.2116 0.2278 -0.0071 0.0050  0.0078  262  ILE A CG1 
1738  C CG2 . ILE A 264  ? 0.2033 0.1962 0.2174 -0.0077 0.0048  0.0086  262  ILE A CG2 
1739  C CD1 . ILE A 264  ? 0.2568 0.2518 0.2640 -0.0066 0.0047  0.0103  262  ILE A CD1 
1740  N N   . SER A 265  ? 0.2035 0.1883 0.2164 -0.0082 0.0066  0.0060  263  SER A N   
1741  C CA  . SER A 265  ? 0.2027 0.1837 0.2157 -0.0083 0.0079  0.0075  263  SER A CA  
1742  C C   . SER A 265  ? 0.2267 0.2074 0.2370 -0.0076 0.0088  0.0095  263  SER A C   
1743  O O   . SER A 265  ? 0.2690 0.2513 0.2771 -0.0071 0.0084  0.0093  263  SER A O   
1744  C CB  . SER A 265  ? 0.2287 0.2069 0.2418 -0.0085 0.0080  0.0060  263  SER A CB  
1745  O OG  . SER A 265  ? 0.2673 0.2448 0.2833 -0.0094 0.0072  0.0045  263  SER A OG  
1746  N N   . ILE A 266  ? 0.2263 0.2052 0.2371 -0.0075 0.0098  0.0113  264  ILE A N   
1747  C CA  . ILE A 266  ? 0.2082 0.1864 0.2169 -0.0067 0.0104  0.0131  264  ILE A CA  
1748  C C   . ILE A 266  ? 0.2380 0.2129 0.2465 -0.0066 0.0116  0.0138  264  ILE A C   
1749  O O   . ILE A 266  ? 0.2066 0.1801 0.2167 -0.0072 0.0121  0.0135  264  ILE A O   
1750  C CB  . ILE A 266  ? 0.2252 0.2050 0.2347 -0.0063 0.0101  0.0146  264  ILE A CB  
1751  C CG1 . ILE A 266  ? 0.2127 0.1919 0.2247 -0.0065 0.0107  0.0148  264  ILE A CG1 
1752  C CG2 . ILE A 266  ? 0.2265 0.2098 0.2361 -0.0064 0.0087  0.0141  264  ILE A CG2 
1753  C CD1 . ILE A 266  ? 0.2560 0.2363 0.2689 -0.0056 0.0105  0.0162  264  ILE A CD1 
1754  N N   . LYS A 267  ? 0.2095 0.1833 0.2159 -0.0061 0.0120  0.0148  265  LYS A N   
1755  C CA  . LYS A 267  ? 0.2273 0.1983 0.2332 -0.0058 0.0131  0.0155  265  LYS A CA  
1756  C C   . LYS A 267  ? 0.2322 0.2030 0.2379 -0.0051 0.0133  0.0170  265  LYS A C   
1757  O O   . LYS A 267  ? 0.2185 0.1902 0.2233 -0.0048 0.0127  0.0177  265  LYS A O   
1758  C CB  . LYS A 267  ? 0.2503 0.2200 0.2541 -0.0056 0.0133  0.0150  265  LYS A CB  
1759  C CG  . LYS A 267  ? 0.2870 0.2561 0.2914 -0.0060 0.0131  0.0134  265  LYS A CG  
1760  C CD  . LYS A 267  ? 0.3275 0.2958 0.3300 -0.0056 0.0132  0.0127  265  LYS A CD  
1761  C CE  . LYS A 267  ? 0.4035 0.3705 0.4068 -0.0057 0.0129  0.0110  265  LYS A CE  
1762  N NZ  . LYS A 267  ? 0.3739 0.3431 0.3784 -0.0060 0.0118  0.0092  265  LYS A NZ  
1763  N N   . LEU A 268  ? 0.2046 0.1744 0.2115 -0.0049 0.0142  0.0174  266  LEU A N   
1764  C CA  . LEU A 268  ? 0.2054 0.1751 0.2125 -0.0040 0.0142  0.0183  266  LEU A CA  
1765  C C   . LEU A 268  ? 0.2332 0.2011 0.2383 -0.0035 0.0142  0.0189  266  LEU A C   
1766  O O   . LEU A 268  ? 0.2206 0.1883 0.2257 -0.0029 0.0136  0.0197  266  LEU A O   
1767  C CB  . LEU A 268  ? 0.2155 0.1852 0.2241 -0.0037 0.0152  0.0184  266  LEU A CB  
1768  C CG  . LEU A 268  ? 0.2474 0.2193 0.2585 -0.0044 0.0153  0.0180  266  LEU A CG  
1769  C CD1 . LEU A 268  ? 0.2846 0.2571 0.2969 -0.0042 0.0164  0.0182  266  LEU A CD1 
1770  C CD2 . LEU A 268  ? 0.2362 0.2104 0.2484 -0.0040 0.0141  0.0181  266  LEU A CD2 
1771  N N   . SER A 269  ? 0.2249 0.1913 0.2286 -0.0038 0.0147  0.0185  267  SER A N   
1772  C CA  . SER A 269  ? 0.2194 0.1843 0.2214 -0.0034 0.0147  0.0190  267  SER A CA  
1773  C C   . SER A 269  ? 0.2364 0.2026 0.2375 -0.0038 0.0137  0.0197  267  SER A C   
1774  O O   . SER A 269  ? 0.2313 0.1965 0.2316 -0.0037 0.0134  0.0205  267  SER A O   
1775  C CB  . SER A 269  ? 0.2582 0.2218 0.2590 -0.0036 0.0154  0.0184  267  SER A CB  
1776  O OG  . SER A 269  ? 0.2428 0.2075 0.2431 -0.0042 0.0150  0.0177  267  SER A OG  
1777  N N   . ALA A 270  ? 0.2059 0.1744 0.2074 -0.0043 0.0131  0.0194  268  ALA A N   
1778  C CA  . ALA A 270  ? 0.2268 0.1971 0.2272 -0.0047 0.0121  0.0203  268  ALA A CA  
1779  C C   . ALA A 270  ? 0.2204 0.1908 0.2217 -0.0043 0.0112  0.0218  268  ALA A C   
1780  O O   . ALA A 270  ? 0.2282 0.1994 0.2286 -0.0046 0.0104  0.0232  268  ALA A O   
1781  C CB  . ALA A 270  ? 0.2282 0.2014 0.2285 -0.0052 0.0117  0.0192  268  ALA A CB  
1782  N N   . LEU A 271  ? 0.2266 0.1964 0.2297 -0.0036 0.0113  0.0216  269  LEU A N   
1783  C CA  . LEU A 271  ? 0.2157 0.1860 0.2200 -0.0030 0.0102  0.0227  269  LEU A CA  
1784  C C   . LEU A 271  ? 0.2139 0.1816 0.2187 -0.0021 0.0100  0.0233  269  LEU A C   
1785  O O   . LEU A 271  ? 0.2248 0.1924 0.2308 -0.0014 0.0089  0.0242  269  LEU A O   
1786  C CB  . LEU A 271  ? 0.2280 0.2001 0.2342 -0.0027 0.0102  0.0218  269  LEU A CB  
1787  C CG  . LEU A 271  ? 0.2389 0.2137 0.2449 -0.0036 0.0099  0.0211  269  LEU A CG  
1788  C CD1 . LEU A 271  ? 0.2787 0.2552 0.2869 -0.0035 0.0099  0.0201  269  LEU A CD1 
1789  C CD2 . LEU A 271  ? 0.2469 0.2235 0.2518 -0.0038 0.0085  0.0225  269  LEU A CD2 
1790  N N   . HIS A 272  ? 0.2145 0.1801 0.2186 -0.0020 0.0109  0.0228  270  HIS A N   
1791  C CA  . HIS A 272  ? 0.2144 0.1776 0.2190 -0.0011 0.0106  0.0231  270  HIS A CA  
1792  C C   . HIS A 272  ? 0.2348 0.1963 0.2379 -0.0015 0.0113  0.0228  270  HIS A C   
1793  O O   . HIS A 272  ? 0.2283 0.1901 0.2306 -0.0018 0.0125  0.0218  270  HIS A O   
1794  C CB  . HIS A 272  ? 0.2246 0.1879 0.2310 0.0002  0.0111  0.0220  270  HIS A CB  
1795  C CG  . HIS A 272  ? 0.2822 0.2436 0.2897 0.0015  0.0101  0.0220  270  HIS A CG  
1796  N ND1 . HIS A 272  ? 0.3163 0.2754 0.3232 0.0019  0.0104  0.0216  270  HIS A ND1 
1797  C CD2 . HIS A 272  ? 0.3017 0.2630 0.3110 0.0026  0.0088  0.0224  270  HIS A CD2 
1798  C CE1 . HIS A 272  ? 0.3224 0.2799 0.3306 0.0031  0.0091  0.0215  270  HIS A CE1 
1799  N NE2 . HIS A 272  ? 0.3063 0.2650 0.3162 0.0037  0.0081  0.0220  270  HIS A NE2 
1800  N N   . PRO A 273  ? 0.2520 0.2116 0.2548 -0.0015 0.0104  0.0237  271  PRO A N   
1801  C CA  . PRO A 273  ? 0.2211 0.1794 0.2225 -0.0019 0.0110  0.0234  271  PRO A CA  
1802  C C   . PRO A 273  ? 0.2598 0.2167 0.2615 -0.0008 0.0119  0.0219  271  PRO A C   
1803  O O   . PRO A 273  ? 0.2654 0.2215 0.2659 -0.0011 0.0125  0.0214  271  PRO A O   
1804  C CB  . PRO A 273  ? 0.2457 0.2026 0.2473 -0.0024 0.0097  0.0249  271  PRO A CB  
1805  C CG  . PRO A 273  ? 0.2519 0.2079 0.2553 -0.0015 0.0083  0.0255  271  PRO A CG  
1806  C CD  . PRO A 273  ? 0.2398 0.1984 0.2437 -0.0013 0.0087  0.0252  271  PRO A CD  
1807  N N   . ARG A 274  ? 0.2326 0.1895 0.2357 0.0004  0.0119  0.0212  272  ARG A N   
1808  C CA  . ARG A 274  ? 0.2338 0.1902 0.2370 0.0015  0.0128  0.0198  272  ARG A CA  
1809  C C   . ARG A 274  ? 0.2700 0.2285 0.2738 0.0018  0.0140  0.0191  272  ARG A C   
1810  O O   . ARG A 274  ? 0.2564 0.2156 0.2615 0.0031  0.0141  0.0183  272  ARG A O   
1811  C CB  . ARG A 274  ? 0.2357 0.1904 0.2402 0.0028  0.0117  0.0192  272  ARG A CB  
1812  C CG  . ARG A 274  ? 0.2355 0.1877 0.2397 0.0023  0.0104  0.0200  272  ARG A CG  
1813  C CD  . ARG A 274  ? 0.2755 0.2272 0.2779 0.0015  0.0112  0.0197  272  ARG A CD  
1814  N NE  . ARG A 274  ? 0.2878 0.2397 0.2896 0.0026  0.0124  0.0180  272  ARG A NE  
1815  C CZ  . ARG A 274  ? 0.2648 0.2156 0.2672 0.0039  0.0119  0.0168  272  ARG A CZ  
1816  N NH1 . ARG A 274  ? 0.2879 0.2365 0.2917 0.0043  0.0102  0.0168  272  ARG A NH1 
1817  N NH2 . ARG A 274  ? 0.2832 0.2349 0.2848 0.0048  0.0131  0.0154  272  ARG A NH2 
1818  N N   . TYR A 275  ? 0.2303 0.1900 0.2334 0.0007  0.0147  0.0193  273  TYR A N   
1819  C CA  . TYR A 275  ? 0.2032 0.1648 0.2072 0.0007  0.0157  0.0189  273  TYR A CA  
1820  C C   . TYR A 275  ? 0.2185 0.1799 0.2216 0.0009  0.0170  0.0183  273  TYR A C   
1821  O O   . TYR A 275  ? 0.2411 0.2018 0.2429 0.0001  0.0175  0.0185  273  TYR A O   
1822  C CB  . TYR A 275  ? 0.2402 0.2029 0.2441 -0.0006 0.0156  0.0193  273  TYR A CB  
1823  C CG  . TYR A 275  ? 0.2072 0.1714 0.2121 -0.0010 0.0166  0.0189  273  TYR A CG  
1824  C CD1 . TYR A 275  ? 0.2155 0.1816 0.2223 -0.0004 0.0169  0.0187  273  TYR A CD1 
1825  C CD2 . TYR A 275  ? 0.2033 0.1674 0.2077 -0.0021 0.0170  0.0188  273  TYR A CD2 
1826  C CE1 . TYR A 275  ? 0.2469 0.2147 0.2549 -0.0011 0.0177  0.0187  273  TYR A CE1 
1827  C CE2 . TYR A 275  ? 0.2105 0.1757 0.2161 -0.0027 0.0176  0.0187  273  TYR A CE2 
1828  C CZ  . TYR A 275  ? 0.2362 0.2034 0.2436 -0.0024 0.0180  0.0188  273  TYR A CZ  
1829  O OH  . TYR A 275  ? 0.2470 0.2156 0.2559 -0.0033 0.0187  0.0189  273  TYR A OH  
1830  N N   . SER A 276  ? 0.2240 0.1860 0.2277 0.0021  0.0175  0.0177  274  SER A N   
1831  C CA  . SER A 276  ? 0.2253 0.1876 0.2279 0.0023  0.0187  0.0173  274  SER A CA  
1832  C C   . SER A 276  ? 0.2547 0.2194 0.2586 0.0036  0.0193  0.0166  274  SER A C   
1833  O O   . SER A 276  ? 0.2051 0.1706 0.2106 0.0045  0.0185  0.0160  274  SER A O   
1834  C CB  . SER A 276  ? 0.2744 0.2346 0.2752 0.0028  0.0184  0.0169  274  SER A CB  
1835  O OG  . SER A 276  ? 0.2805 0.2402 0.2821 0.0041  0.0175  0.0161  274  SER A OG  
1836  N N   . ARG A 277  ? 0.2305 0.1968 0.2337 0.0035  0.0206  0.0166  275  ARG A N   
1837  C CA  . ARG A 277  ? 0.2415 0.2109 0.2456 0.0047  0.0214  0.0159  275  ARG A CA  
1838  C C   . ARG A 277  ? 0.2340 0.2029 0.2381 0.0066  0.0206  0.0143  275  ARG A C   
1839  O O   . ARG A 277  ? 0.2238 0.1950 0.2296 0.0080  0.0205  0.0132  275  ARG A O   
1840  C CB  . ARG A 277  ? 0.2025 0.1735 0.2052 0.0042  0.0230  0.0165  275  ARG A CB  
1841  C CG  . ARG A 277  ? 0.2156 0.1907 0.2189 0.0054  0.0240  0.0157  275  ARG A CG  
1842  C CD  . ARG A 277  ? 0.2226 0.2011 0.2288 0.0056  0.0242  0.0155  275  ARG A CD  
1843  N NE  . ARG A 277  ? 0.2268 0.2099 0.2335 0.0069  0.0253  0.0145  275  ARG A NE  
1844  C CZ  . ARG A 277  ? 0.2439 0.2283 0.2512 0.0091  0.0247  0.0124  275  ARG A CZ  
1845  N NH1 . ARG A 277  ? 0.2188 0.1996 0.2261 0.0103  0.0231  0.0113  275  ARG A NH1 
1846  N NH2 . ARG A 277  ? 0.2210 0.2105 0.2289 0.0103  0.0259  0.0114  275  ARG A NH2 
1847  N N   . ALA A 278  ? 0.2410 0.2071 0.2434 0.0068  0.0200  0.0140  276  ALA A N   
1848  C CA  . ALA A 278  ? 0.2555 0.2208 0.2582 0.0086  0.0190  0.0123  276  ALA A CA  
1849  C C   . ALA A 278  ? 0.2267 0.1910 0.2316 0.0093  0.0175  0.0119  276  ALA A C   
1850  O O   . ALA A 278  ? 0.2669 0.2314 0.2730 0.0111  0.0166  0.0103  276  ALA A O   
1851  C CB  . ALA A 278  ? 0.2611 0.2233 0.2619 0.0083  0.0184  0.0122  276  ALA A CB  
1852  N N   . GLN A 279  ? 0.2335 0.1968 0.2391 0.0080  0.0169  0.0133  277  GLN A N   
1853  C CA  . GLN A 279  ? 0.2113 0.1735 0.2187 0.0084  0.0153  0.0135  277  GLN A CA  
1854  C C   . GLN A 279  ? 0.2745 0.2398 0.2839 0.0084  0.0157  0.0137  277  GLN A C   
1855  O O   . GLN A 279  ? 0.2228 0.1875 0.2332 0.0080  0.0146  0.0146  277  GLN A O   
1856  C CB  . GLN A 279  ? 0.2489 0.2082 0.2555 0.0069  0.0143  0.0150  277  GLN A CB  
1857  C CG  . GLN A 279  ? 0.2166 0.1734 0.2218 0.0068  0.0139  0.0147  277  GLN A CG  
1858  C CD  . GLN A 279  ? 0.2893 0.2443 0.2957 0.0083  0.0124  0.0135  277  GLN A CD  
1859  O OE1 . GLN A 279  ? 0.3446 0.2987 0.3529 0.0089  0.0109  0.0137  277  GLN A OE1 
1860  N NE2 . GLN A 279  ? 0.2409 0.1954 0.2465 0.0092  0.0126  0.0120  277  GLN A NE2 
1861  N N   . ALA A 280  ? 0.2290 0.1977 0.2387 0.0089  0.0172  0.0130  278  ALA A N   
1862  C CA  . ALA A 280  ? 0.2433 0.2152 0.2547 0.0085  0.0178  0.0134  278  ALA A CA  
1863  C C   . ALA A 280  ? 0.2317 0.2043 0.2458 0.0098  0.0163  0.0128  278  ALA A C   
1864  O O   . ALA A 280  ? 0.2196 0.1934 0.2349 0.0091  0.0159  0.0136  278  ALA A O   
1865  C CB  . ALA A 280  ? 0.2281 0.2041 0.2397 0.0086  0.0196  0.0129  278  ALA A CB  
1866  N N   . ALA A 281  ? 0.2164 0.1881 0.2312 0.0119  0.0152  0.0113  279  ALA A N   
1867  C CA  . ALA A 281  ? 0.2561 0.2280 0.2735 0.0135  0.0135  0.0106  279  ALA A CA  
1868  C C   . ALA A 281  ? 0.2822 0.2509 0.2996 0.0124  0.0118  0.0124  279  ALA A C   
1869  O O   . ALA A 281  ? 0.2315 0.2015 0.2508 0.0126  0.0109  0.0129  279  ALA A O   
1870  C CB  . ALA A 281  ? 0.2847 0.2556 0.3031 0.0160  0.0124  0.0085  279  ALA A CB  
1871  N N   . ARG A 282  ? 0.2186 0.1837 0.2341 0.0112  0.0113  0.0135  280  ARG A N   
1872  C CA  . ARG A 282  ? 0.2458 0.2086 0.2610 0.0100  0.0099  0.0154  280  ARG A CA  
1873  C C   . ARG A 282  ? 0.2745 0.2395 0.2891 0.0082  0.0109  0.0166  280  ARG A C   
1874  O O   . ARG A 282  ? 0.2555 0.2206 0.2707 0.0077  0.0097  0.0178  280  ARG A O   
1875  C CB  . ARG A 282  ? 0.2695 0.2286 0.2828 0.0090  0.0093  0.0162  280  ARG A CB  
1876  C CG  . ARG A 282  ? 0.2926 0.2488 0.3067 0.0105  0.0079  0.0152  280  ARG A CG  
1877  C CD  . ARG A 282  ? 0.2753 0.2281 0.2879 0.0091  0.0071  0.0165  280  ARG A CD  
1878  N NE  . ARG A 282  ? 0.2639 0.2161 0.2765 0.0076  0.0060  0.0189  280  ARG A NE  
1879  C CZ  . ARG A 282  ? 0.3075 0.2581 0.3187 0.0059  0.0056  0.0206  280  ARG A CZ  
1880  N NH1 . ARG A 282  ? 0.2330 0.1820 0.2428 0.0053  0.0060  0.0203  280  ARG A NH1 
1881  N NH2 . ARG A 282  ? 0.2595 0.2105 0.2706 0.0047  0.0047  0.0228  280  ARG A NH2 
1882  N N   . VAL A 283  ? 0.2295 0.1961 0.2430 0.0073  0.0128  0.0163  281  VAL A N   
1883  C CA  . VAL A 283  ? 0.2021 0.1705 0.2153 0.0056  0.0135  0.0172  281  VAL A CA  
1884  C C   . VAL A 283  ? 0.2130 0.1846 0.2287 0.0061  0.0132  0.0169  281  VAL A C   
1885  O O   . VAL A 283  ? 0.2116 0.1839 0.2278 0.0053  0.0124  0.0178  281  VAL A O   
1886  C CB  . VAL A 283  ? 0.2015 0.1707 0.2133 0.0046  0.0154  0.0170  281  VAL A CB  
1887  C CG1 . VAL A 283  ? 0.2101 0.1814 0.2226 0.0031  0.0161  0.0175  281  VAL A CG1 
1888  C CG2 . VAL A 283  ? 0.2149 0.1810 0.2242 0.0038  0.0154  0.0175  281  VAL A CG2 
1889  N N   . MET A 284  ? 0.2084 0.1824 0.2258 0.0076  0.0138  0.0157  282  MET A N   
1890  C CA  . MET A 284  ? 0.2488 0.2265 0.2689 0.0082  0.0136  0.0152  282  MET A CA  
1891  C C   . MET A 284  ? 0.2617 0.2385 0.2833 0.0094  0.0113  0.0155  282  MET A C   
1892  O O   . MET A 284  ? 0.2423 0.2212 0.2655 0.0093  0.0107  0.0158  282  MET A O   
1893  C CB  . MET A 284  ? 0.2299 0.2111 0.2515 0.0095  0.0148  0.0137  282  MET A CB  
1894  C CG  . MET A 284  ? 0.2305 0.2131 0.2507 0.0082  0.0170  0.0139  282  MET A CG  
1895  S SD  . MET A 284  ? 0.2837 0.2673 0.3039 0.0053  0.0178  0.0154  282  MET A SD  
1896  C CE  . MET A 284  ? 0.2428 0.2319 0.2667 0.0057  0.0179  0.0148  282  MET A CE  
1897  N N   . GLY A 285  ? 0.2261 0.1995 0.2473 0.0106  0.0100  0.0153  283  GLY A N   
1898  C CA  . GLY A 285  ? 0.2488 0.2207 0.2715 0.0119  0.0077  0.0158  283  GLY A CA  
1899  C C   . GLY A 285  ? 0.2522 0.2220 0.2735 0.0103  0.0064  0.0180  283  GLY A C   
1900  O O   . GLY A 285  ? 0.2375 0.2076 0.2602 0.0109  0.0047  0.0189  283  GLY A O   
1901  N N   . GLU A 286  ? 0.2158 0.1839 0.2345 0.0085  0.0073  0.0190  284  GLU A N   
1902  C CA  . GLU A 286  ? 0.2294 0.1959 0.2467 0.0071  0.0061  0.0210  284  GLU A CA  
1903  C C   . GLU A 286  ? 0.2852 0.2536 0.3008 0.0052  0.0072  0.0215  284  GLU A C   
1904  O O   . GLU A 286  ? 0.2768 0.2460 0.2920 0.0044  0.0061  0.0228  284  GLU A O   
1905  C CB  . GLU A 286  ? 0.2653 0.2279 0.2810 0.0068  0.0056  0.0217  284  GLU A CB  
1906  C CG  . GLU A 286  ? 0.2842 0.2444 0.3015 0.0087  0.0044  0.0208  284  GLU A CG  
1907  C CD  . GLU A 286  ? 0.3299 0.2865 0.3458 0.0083  0.0042  0.0210  284  GLU A CD  
1908  O OE1 . GLU A 286  ? 0.3265 0.2826 0.3403 0.0064  0.0047  0.0223  284  GLU A OE1 
1909  O OE2 . GLU A 286  ? 0.3078 0.2626 0.3249 0.0098  0.0035  0.0196  284  GLU A OE2 
1910  N N   . LEU A 287  ? 0.2304 0.1994 0.2451 0.0044  0.0091  0.0206  285  LEU A N   
1911  C CA  . LEU A 287  ? 0.2433 0.2138 0.2568 0.0027  0.0099  0.0208  285  LEU A CA  
1912  C C   . LEU A 287  ? 0.2512 0.2251 0.2667 0.0026  0.0100  0.0202  285  LEU A C   
1913  O O   . LEU A 287  ? 0.2402 0.2156 0.2555 0.0016  0.0094  0.0207  285  LEU A O   
1914  C CB  . LEU A 287  ? 0.2276 0.1972 0.2397 0.0020  0.0117  0.0201  285  LEU A CB  
1915  C CG  . LEU A 287  ? 0.3259 0.2964 0.3371 0.0004  0.0127  0.0198  285  LEU A CG  
1916  C CD1 . LEU A 287  ? 0.3452 0.3165 0.3557 -0.0006 0.0117  0.0205  285  LEU A CD1 
1917  C CD2 . LEU A 287  ? 0.2805 0.2489 0.2897 -0.0001 0.0138  0.0196  285  LEU A CD2 
1918  N N   . LEU A 288  ? 0.2261 0.2019 0.2437 0.0035  0.0108  0.0192  286  LEU A N   
1919  C CA  . LEU A 288  ? 0.2539 0.2333 0.2737 0.0033  0.0110  0.0186  286  LEU A CA  
1920  C C   . LEU A 288  ? 0.2209 0.2018 0.2418 0.0036  0.0091  0.0192  286  LEU A C   
1921  O O   . LEU A 288  ? 0.2295 0.2126 0.2510 0.0025  0.0090  0.0192  286  LEU A O   
1922  C CB  . LEU A 288  ? 0.2268 0.2084 0.2487 0.0045  0.0120  0.0175  286  LEU A CB  
1923  C CG  . LEU A 288  ? 0.2860 0.2720 0.3108 0.0044  0.0122  0.0169  286  LEU A CG  
1924  C CD1 . LEU A 288  ? 0.2584 0.2458 0.2832 0.0022  0.0131  0.0171  286  LEU A CD1 
1925  C CD2 . LEU A 288  ? 0.3326 0.3211 0.3592 0.0058  0.0133  0.0158  286  LEU A CD2 
1926  N N   . PRO A 289  ? 0.2347 0.2143 0.2561 0.0051  0.0075  0.0198  287  PRO A N   
1927  C CA  . PRO A 289  ? 0.2744 0.2555 0.2966 0.0054  0.0056  0.0207  287  PRO A CA  
1928  C C   . PRO A 289  ? 0.2041 0.1850 0.2241 0.0037  0.0052  0.0218  287  PRO A C   
1929  O O   . PRO A 289  ? 0.2178 0.2014 0.2384 0.0034  0.0042  0.0221  287  PRO A O   
1930  C CB  . PRO A 289  ? 0.2821 0.2607 0.3049 0.0072  0.0039  0.0215  287  PRO A CB  
1931  C CG  . PRO A 289  ? 0.3133 0.2907 0.3368 0.0084  0.0050  0.0201  287  PRO A CG  
1932  C CD  . PRO A 289  ? 0.2256 0.2026 0.2471 0.0067  0.0071  0.0197  287  PRO A CD  
1933  N N   . ARG A 290  ? 0.2553 0.2337 0.2727 0.0027  0.0058  0.0224  288  ARG A N   
1934  C CA  . ARG A 290  ? 0.2211 0.2001 0.2363 0.0013  0.0055  0.0231  288  ARG A CA  
1935  C C   . ARG A 290  ? 0.2091 0.1905 0.2247 0.0001  0.0065  0.0218  288  ARG A C   
1936  O O   . ARG A 290  ? 0.2097 0.1934 0.2249 -0.0006 0.0057  0.0218  288  ARG A O   
1937  C CB  . ARG A 290  ? 0.2682 0.2442 0.2808 0.0006  0.0060  0.0238  288  ARG A CB  
1938  C CG  . ARG A 290  ? 0.2699 0.2432 0.2824 0.0014  0.0048  0.0253  288  ARG A CG  
1939  C CD  . ARG A 290  ? 0.2773 0.2480 0.2875 0.0006  0.0054  0.0260  288  ARG A CD  
1940  N NE  . ARG A 290  ? 0.3799 0.3477 0.3905 0.0013  0.0040  0.0273  288  ARG A NE  
1941  C CZ  . ARG A 290  ? 0.4261 0.3910 0.4360 0.0013  0.0044  0.0273  288  ARG A CZ  
1942  N NH1 . ARG A 290  ? 0.3412 0.3057 0.3498 0.0006  0.0061  0.0261  288  ARG A NH1 
1943  N NH2 . ARG A 290  ? 0.4377 0.3998 0.4485 0.0019  0.0029  0.0284  288  ARG A NH2 
1944  N N   . VAL A 291  ? 0.2131 0.1941 0.2294 -0.0002 0.0081  0.0205  289  VAL A N   
1945  C CA  . VAL A 291  ? 0.2197 0.2028 0.2369 -0.0014 0.0088  0.0194  289  VAL A CA  
1946  C C   . VAL A 291  ? 0.2247 0.2112 0.2444 -0.0012 0.0079  0.0189  289  VAL A C   
1947  O O   . VAL A 291  ? 0.2137 0.2024 0.2338 -0.0022 0.0074  0.0183  289  VAL A O   
1948  C CB  . VAL A 291  ? 0.2466 0.2285 0.2642 -0.0019 0.0106  0.0186  289  VAL A CB  
1949  C CG1 . VAL A 291  ? 0.2386 0.2221 0.2572 -0.0034 0.0110  0.0176  289  VAL A CG1 
1950  C CG2 . VAL A 291  ? 0.2526 0.2313 0.2677 -0.0019 0.0113  0.0190  289  VAL A CG2 
1951  N N   . LYS A 292  ? 0.2048 0.1922 0.2265 0.0002  0.0076  0.0190  290  LYS A N   
1952  C CA  . LYS A 292  ? 0.2009 0.1920 0.2254 0.0006  0.0067  0.0186  290  LYS A CA  
1953  C C   . LYS A 292  ? 0.2020 0.1944 0.2256 0.0005  0.0048  0.0193  290  LYS A C   
1954  O O   . LYS A 292  ? 0.2020 0.1975 0.2268 -0.0001 0.0042  0.0186  290  LYS A O   
1955  C CB  . LYS A 292  ? 0.2014 0.1932 0.2281 0.0025  0.0065  0.0186  290  LYS A CB  
1956  C CG  . LYS A 292  ? 0.2258 0.2217 0.2554 0.0032  0.0052  0.0181  290  LYS A CG  
1957  C CD  . LYS A 292  ? 0.2340 0.2310 0.2661 0.0053  0.0050  0.0177  290  LYS A CD  
1958  C CE  . LYS A 292  ? 0.2415 0.2430 0.2767 0.0060  0.0039  0.0171  290  LYS A CE  
1959  N NZ  . LYS A 292  ? 0.2425 0.2460 0.2806 0.0081  0.0039  0.0162  290  LYS A NZ  
1960  N N   . ALA A 293  ? 0.2032 0.1934 0.2245 0.0011  0.0038  0.0208  291  ALA A N   
1961  C CA  . ALA A 293  ? 0.2046 0.1964 0.2248 0.0010  0.0020  0.0219  291  ALA A CA  
1962  C C   . ALA A 293  ? 0.2041 0.1976 0.2228 -0.0006 0.0023  0.0210  291  ALA A C   
1963  O O   . ALA A 293  ? 0.2047 0.2015 0.2238 -0.0008 0.0011  0.0207  291  ALA A O   
1964  C CB  . ALA A 293  ? 0.2062 0.1953 0.2243 0.0016  0.0011  0.0240  291  ALA A CB  
1965  N N   . LEU A 294  ? 0.2064 0.1979 0.2235 -0.0016 0.0037  0.0204  292  LEU A N   
1966  C CA  . LEU A 294  ? 0.2028 0.1957 0.2187 -0.0029 0.0038  0.0191  292  LEU A CA  
1967  C C   . LEU A 294  ? 0.2021 0.1974 0.2209 -0.0035 0.0039  0.0173  292  LEU A C   
1968  O O   . LEU A 294  ? 0.2063 0.2042 0.2251 -0.0041 0.0030  0.0162  292  LEU A O   
1969  C CB  . LEU A 294  ? 0.2053 0.1953 0.2193 -0.0036 0.0052  0.0188  292  LEU A CB  
1970  C CG  . LEU A 294  ? 0.2027 0.1906 0.2139 -0.0033 0.0050  0.0206  292  LEU A CG  
1971  C CD1 . LEU A 294  ? 0.2017 0.1870 0.2116 -0.0039 0.0065  0.0200  292  LEU A CD1 
1972  C CD2 . LEU A 294  ? 0.2214 0.2120 0.2307 -0.0036 0.0037  0.0213  292  LEU A CD2 
1973  N N   . ALA A 295  ? 0.2012 0.1957 0.2223 -0.0034 0.0051  0.0169  293  ALA A N   
1974  C CA  . ALA A 295  ? 0.2008 0.1977 0.2249 -0.0043 0.0052  0.0154  293  ALA A CA  
1975  C C   . ALA A 295  ? 0.2133 0.2141 0.2393 -0.0038 0.0036  0.0152  293  ALA A C   
1976  O O   . ALA A 295  ? 0.2027 0.2061 0.2304 -0.0047 0.0030  0.0138  293  ALA A O   
1977  C CB  . ALA A 295  ? 0.1999 0.1959 0.2260 -0.0043 0.0068  0.0154  293  ALA A CB  
1978  N N   . LEU A 296  ? 0.2022 0.2034 0.2282 -0.0022 0.0027  0.0166  294  LEU A N   
1979  C CA  . LEU A 296  ? 0.2129 0.2178 0.2406 -0.0015 0.0010  0.0166  294  LEU A CA  
1980  C C   . LEU A 296  ? 0.2304 0.2374 0.2563 -0.0021 -0.0004 0.0163  294  LEU A C   
1981  O O   . LEU A 296  ? 0.2108 0.2215 0.2383 -0.0023 -0.0016 0.0152  294  LEU A O   
1982  C CB  . LEU A 296  ? 0.2054 0.2098 0.2332 0.0004  0.0000  0.0182  294  LEU A CB  
1983  C CG  . LEU A 296  ? 0.2368 0.2407 0.2672 0.0015  0.0010  0.0180  294  LEU A CG  
1984  C CD1 . LEU A 296  ? 0.2440 0.2464 0.2742 0.0036  -0.0002 0.0195  294  LEU A CD1 
1985  C CD2 . LEU A 296  ? 0.2350 0.2432 0.2693 0.0014  0.0010  0.0166  294  LEU A CD2 
1986  N N   . LEU A 297  ? 0.2047 0.2097 0.2270 -0.0024 -0.0004 0.0171  295  LEU A N   
1987  C CA  . LEU A 297  ? 0.2058 0.2133 0.2260 -0.0029 -0.0015 0.0166  295  LEU A CA  
1988  C C   . LEU A 297  ? 0.2264 0.2350 0.2477 -0.0043 -0.0011 0.0139  295  LEU A C   
1989  O O   . LEU A 297  ? 0.2083 0.2206 0.2300 -0.0046 -0.0024 0.0125  295  LEU A O   
1990  C CB  . LEU A 297  ? 0.2065 0.2120 0.2228 -0.0029 -0.0013 0.0181  295  LEU A CB  
1991  N N   . ALA A 298  ? 0.2040 0.2096 0.2259 -0.0051 0.0005  0.0131  296  ALA A N   
1992  C CA  . ALA A 298  ? 0.2039 0.2100 0.2272 -0.0064 0.0007  0.0106  296  ALA A CA  
1993  C C   . ALA A 298  ? 0.2286 0.2376 0.2558 -0.0069 0.0000  0.0095  296  ALA A C   
1994  O O   . ALA A 298  ? 0.2095 0.2207 0.2379 -0.0077 -0.0010 0.0074  296  ALA A O   
1995  C CB  . ALA A 298  ? 0.2030 0.2049 0.2263 -0.0072 0.0024  0.0104  296  ALA A CB  
1996  N N   . LYS A 299  ? 0.2033 0.2126 0.2326 -0.0063 0.0004  0.0107  297  LYS A N   
1997  C CA  . LYS A 299  ? 0.2060 0.2188 0.2392 -0.0066 -0.0002 0.0098  297  LYS A CA  
1998  C C   . LYS A 299  ? 0.2482 0.2652 0.2813 -0.0061 -0.0024 0.0091  297  LYS A C   
1999  O O   . LYS A 299  ? 0.2263 0.2462 0.2619 -0.0071 -0.0033 0.0072  297  LYS A O   
2000  C CB  . LYS A 299  ? 0.2236 0.2367 0.2588 -0.0056 0.0005  0.0111  297  LYS A CB  
2001  C CG  . LYS A 299  ? 0.2072 0.2249 0.2460 -0.0052 -0.0006 0.0106  297  LYS A CG  
2002  C CD  . LYS A 299  ? 0.2292 0.2475 0.2705 -0.0043 0.0005  0.0114  297  LYS A CD  
2003  C CE  . LYS A 299  ? 0.2615 0.2846 0.3058 -0.0032 -0.0010 0.0110  297  LYS A CE  
2004  N NZ  . LYS A 299  ? 0.3458 0.3702 0.3927 -0.0020 -0.0001 0.0115  297  LYS A NZ  
2005  N N   . ASN A 300  ? 0.2075 0.2250 0.2379 -0.0047 -0.0033 0.0107  298  ASN A N   
2006  C CA  A ASN A 300  ? 0.2277 0.2494 0.2577 -0.0041 -0.0055 0.0105  298  ASN A CA  
2007  C CA  B ASN A 300  ? 0.2274 0.2492 0.2576 -0.0042 -0.0055 0.0103  298  ASN A CA  
2008  C C   . ASN A 300  ? 0.2389 0.2625 0.2679 -0.0052 -0.0063 0.0081  298  ASN A C   
2009  O O   . ASN A 300  ? 0.2783 0.3061 0.3086 -0.0053 -0.0079 0.0067  298  ASN A O   
2010  C CB  A ASN A 300  ? 0.2719 0.2932 0.2988 -0.0027 -0.0063 0.0131  298  ASN A CB  
2011  C CB  B ASN A 300  ? 0.2758 0.2977 0.3033 -0.0026 -0.0065 0.0129  298  ASN A CB  
2012  C CG  A ASN A 300  ? 0.2829 0.3031 0.3115 -0.0012 -0.0062 0.0149  298  ASN A CG  
2013  C CG  B ASN A 300  ? 0.3082 0.3349 0.3364 -0.0018 -0.0087 0.0129  298  ASN A CG  
2014  O OD1 A ASN A 300  ? 0.3156 0.3367 0.3477 -0.0011 -0.0058 0.0141  298  ASN A OD1 
2015  O OD1 B ASN A 300  ? 0.3603 0.3889 0.3917 -0.0010 -0.0094 0.0131  298  ASN A OD1 
2016  N ND2 A ASN A 300  ? 0.3058 0.3241 0.3319 -0.0001 -0.0067 0.0174  298  ASN A ND2 
2017  N ND2 B ASN A 300  ? 0.2930 0.3223 0.3185 -0.0020 -0.0100 0.0126  298  ASN A ND2 
2018  N N   . TYR A 301  ? 0.2120 0.2328 0.2387 -0.0059 -0.0053 0.0076  299  TYR A N   
2019  C CA  . TYR A 301  ? 0.2088 0.2313 0.2347 -0.0067 -0.0061 0.0049  299  TYR A CA  
2020  C C   . TYR A 301  ? 0.2305 0.2516 0.2598 -0.0082 -0.0057 0.0024  299  TYR A C   
2021  O O   . TYR A 301  ? 0.2426 0.2649 0.2720 -0.0088 -0.0066 -0.0002 299  TYR A O   
2022  C CB  . TYR A 301  ? 0.2091 0.2296 0.2309 -0.0065 -0.0054 0.0052  299  TYR A CB  
2023  C CG  . TYR A 301  ? 0.2102 0.2329 0.2284 -0.0055 -0.0062 0.0073  299  TYR A CG  
2024  C CD1 . TYR A 301  ? 0.2121 0.2398 0.2289 -0.0051 -0.0080 0.0064  299  TYR A CD1 
2025  C CD2 . TYR A 301  ? 0.2408 0.2607 0.2570 -0.0049 -0.0053 0.0103  299  TYR A CD2 
2026  C CE1 . TYR A 301  ? 0.2286 0.2587 0.2419 -0.0044 -0.0087 0.0087  299  TYR A CE1 
2027  C CE2 . TYR A 301  ? 0.2381 0.2598 0.2512 -0.0042 -0.0061 0.0126  299  TYR A CE2 
2028  C CZ  . TYR A 301  ? 0.2706 0.2975 0.2822 -0.0040 -0.0078 0.0120  299  TYR A CZ  
2029  O OH  . TYR A 301  ? 0.2612 0.2902 0.2695 -0.0035 -0.0086 0.0147  299  TYR A OH  
2030  N N   . ASP A 302  ? 0.2239 0.2427 0.2560 -0.0087 -0.0043 0.0033  300  ASP A N   
2031  C CA  . ASP A 302  ? 0.2221 0.2392 0.2575 -0.0104 -0.0037 0.0017  300  ASP A CA  
2032  C C   . ASP A 302  ? 0.2513 0.2650 0.2850 -0.0111 -0.0033 0.0003  300  ASP A C   
2033  O O   . ASP A 302  ? 0.2216 0.2356 0.2569 -0.0121 -0.0043 -0.0023 300  ASP A O   
2034  C CB  . ASP A 302  ? 0.2296 0.2506 0.2688 -0.0113 -0.0054 -0.0004 300  ASP A CB  
2035  C CG  . ASP A 302  ? 0.2916 0.3113 0.3352 -0.0132 -0.0046 -0.0009 300  ASP A CG  
2036  O OD1 . ASP A 302  ? 0.2819 0.2994 0.3261 -0.0134 -0.0028 0.0011  300  ASP A OD1 
2037  O OD2 . ASP A 302  ? 0.2762 0.2973 0.3227 -0.0146 -0.0059 -0.0032 300  ASP A OD2 
2038  N N   . ILE A 303  ? 0.2340 0.2445 0.2645 -0.0104 -0.0020 0.0019  301  ILE A N   
2039  C CA  . ILE A 303  ? 0.2071 0.2141 0.2361 -0.0108 -0.0014 0.0009  301  ILE A CA  
2040  C C   . ILE A 303  ? 0.2106 0.2134 0.2403 -0.0113 0.0005  0.0026  301  ILE A C   
2041  O O   . ILE A 303  ? 0.2054 0.2081 0.2357 -0.0110 0.0015  0.0047  301  ILE A O   
2042  C CB  . ILE A 303  ? 0.2214 0.2289 0.2460 -0.0096 -0.0016 0.0010  301  ILE A CB  
2043  C CG1 . ILE A 303  ? 0.2149 0.2207 0.2370 -0.0087 -0.0003 0.0042  301  ILE A CG1 
2044  C CG2 . ILE A 303  ? 0.2296 0.2422 0.2532 -0.0090 -0.0035 -0.0004 301  ILE A CG2 
2045  C CD1 . ILE A 303  ? 0.2136 0.2195 0.2315 -0.0079 -0.0002 0.0046  301  ILE A CD1 
2046  N N   . GLY A 304  ? 0.2185 0.2178 0.2479 -0.0119 0.0010  0.0017  302  GLY A N   
2047  C CA  . GLY A 304  ? 0.2431 0.2384 0.2726 -0.0123 0.0027  0.0034  302  GLY A CA  
2048  C C   . GLY A 304  ? 0.2080 0.2018 0.2337 -0.0110 0.0039  0.0052  302  GLY A C   
2049  O O   . GLY A 304  ? 0.2285 0.2231 0.2514 -0.0101 0.0034  0.0048  302  GLY A O   
2050  N N   . LEU A 305  ? 0.2224 0.2144 0.2484 -0.0109 0.0054  0.0073  303  LEU A N   
2051  C CA  . LEU A 305  ? 0.2022 0.1921 0.2251 -0.0098 0.0065  0.0089  303  LEU A CA  
2052  C C   . LEU A 305  ? 0.2018 0.1883 0.2252 -0.0104 0.0080  0.0098  303  LEU A C   
2053  O O   . LEU A 305  ? 0.2279 0.2146 0.2533 -0.0108 0.0088  0.0108  303  LEU A O   
2054  C CB  . LEU A 305  ? 0.2013 0.1930 0.2237 -0.0087 0.0065  0.0107  303  LEU A CB  
2055  C CG  . LEU A 305  ? 0.2248 0.2142 0.2442 -0.0076 0.0073  0.0123  303  LEU A CG  
2056  C CD1 . LEU A 305  ? 0.2880 0.2793 0.3060 -0.0066 0.0064  0.0134  303  LEU A CD1 
2057  C CD2 . LEU A 305  ? 0.2773 0.2645 0.2975 -0.0075 0.0089  0.0135  303  LEU A CD2 
2058  N N   . ASN A 306  ? 0.2066 0.1902 0.2282 -0.0104 0.0083  0.0093  304  ASN A N   
2059  C CA  . ASN A 306  ? 0.2024 0.1825 0.2242 -0.0110 0.0094  0.0100  304  ASN A CA  
2060  C C   . ASN A 306  ? 0.2013 0.1796 0.2203 -0.0099 0.0106  0.0115  304  ASN A C   
2061  O O   . ASN A 306  ? 0.2109 0.1891 0.2273 -0.0090 0.0103  0.0113  304  ASN A O   
2062  C CB  . ASN A 306  ? 0.2165 0.1945 0.2386 -0.0116 0.0087  0.0083  304  ASN A CB  
2063  C CG  . ASN A 306  ? 0.2433 0.2175 0.2650 -0.0119 0.0098  0.0093  304  ASN A CG  
2064  O OD1 . ASN A 306  ? 0.2706 0.2429 0.2896 -0.0110 0.0102  0.0095  304  ASN A OD1 
2065  N ND2 . ASN A 306  ? 0.2160 0.1892 0.2402 -0.0133 0.0102  0.0101  304  ASN A ND2 
2066  N N   . ILE A 307  ? 0.2009 0.1780 0.2204 -0.0100 0.0119  0.0130  305  ILE A N   
2067  C CA  . ILE A 307  ? 0.2002 0.1752 0.2172 -0.0091 0.0130  0.0142  305  ILE A CA  
2068  C C   . ILE A 307  ? 0.2290 0.2008 0.2452 -0.0095 0.0134  0.0140  305  ILE A C   
2069  O O   . ILE A 307  ? 0.2109 0.1816 0.2286 -0.0104 0.0140  0.0146  305  ILE A O   
2070  C CB  . ILE A 307  ? 0.2139 0.1897 0.2317 -0.0086 0.0141  0.0156  305  ILE A CB  
2071  C CG1 . ILE A 307  ? 0.2186 0.1976 0.2376 -0.0080 0.0134  0.0156  305  ILE A CG1 
2072  C CG2 . ILE A 307  ? 0.2256 0.1992 0.2409 -0.0076 0.0151  0.0164  305  ILE A CG2 
2073  C CD1 . ILE A 307  ? 0.2584 0.2389 0.2788 -0.0074 0.0144  0.0165  305  ILE A CD1 
2074  N N   . ASP A 308  ? 0.2157 0.1862 0.2295 -0.0088 0.0131  0.0134  306  ASP A N   
2075  C CA  . ASP A 308  ? 0.2038 0.1713 0.2166 -0.0089 0.0133  0.0131  306  ASP A CA  
2076  C C   . ASP A 308  ? 0.2263 0.1921 0.2384 -0.0086 0.0146  0.0147  306  ASP A C   
2077  O O   . ASP A 308  ? 0.2303 0.1970 0.2416 -0.0080 0.0154  0.0158  306  ASP A O   
2078  C CB  . ASP A 308  ? 0.2306 0.1980 0.2410 -0.0080 0.0128  0.0121  306  ASP A CB  
2079  C CG  . ASP A 308  ? 0.2744 0.2435 0.2854 -0.0081 0.0114  0.0100  306  ASP A CG  
2080  O OD1 . ASP A 308  ? 0.2904 0.2599 0.3037 -0.0090 0.0107  0.0091  306  ASP A OD1 
2081  O OD2 . ASP A 308  ? 0.3238 0.2939 0.3327 -0.0074 0.0110  0.0091  306  ASP A OD2 
2082  N N   . ALA A 309  ? 0.2027 0.1659 0.2150 -0.0091 0.0149  0.0150  307  ALA A N   
2083  C CA  . ALA A 309  ? 0.2140 0.1758 0.2254 -0.0089 0.0161  0.0166  307  ALA A CA  
2084  C C   . ALA A 309  ? 0.2435 0.2034 0.2521 -0.0078 0.0162  0.0163  307  ALA A C   
2085  O O   . ALA A 309  ? 0.2281 0.1869 0.2363 -0.0077 0.0153  0.0150  307  ALA A O   
2086  C CB  . ALA A 309  ? 0.2104 0.1707 0.2235 -0.0102 0.0163  0.0175  307  ALA A CB  
2087  N N   . GLU A 310  ? 0.2203 0.1802 0.2274 -0.0071 0.0171  0.0173  308  GLU A N   
2088  C CA  . GLU A 310  ? 0.2336 0.1922 0.2383 -0.0061 0.0172  0.0170  308  GLU A CA  
2089  C C   . GLU A 310  ? 0.2265 0.1834 0.2302 -0.0058 0.0180  0.0182  308  GLU A C   
2090  O O   . GLU A 310  ? 0.2172 0.1729 0.2218 -0.0066 0.0181  0.0188  308  GLU A O   
2091  C CB  . GLU A 310  ? 0.2167 0.1768 0.2203 -0.0053 0.0171  0.0170  308  GLU A CB  
2092  C CG  . GLU A 310  ? 0.2583 0.2204 0.2627 -0.0056 0.0162  0.0162  308  GLU A CG  
2093  C CD  . GLU A 310  ? 0.2729 0.2362 0.2761 -0.0050 0.0159  0.0165  308  GLU A CD  
2094  O OE1 . GLU A 310  ? 0.2633 0.2261 0.2648 -0.0047 0.0158  0.0163  308  GLU A OE1 
2095  O OE2 . GLU A 310  ? 0.2546 0.2193 0.2588 -0.0049 0.0158  0.0170  308  GLU A OE2 
2096  N N   . GLU A 311  ? 0.2119 0.1687 0.2138 -0.0049 0.0185  0.0185  309  GLU A N   
2097  C CA  . GLU A 311  ? 0.2165 0.1720 0.2171 -0.0045 0.0192  0.0193  309  GLU A CA  
2098  C C   . GLU A 311  ? 0.2401 0.1968 0.2417 -0.0050 0.0202  0.0207  309  GLU A C   
2099  O O   . GLU A 311  ? 0.2077 0.1666 0.2107 -0.0052 0.0205  0.0208  309  GLU A O   
2100  C CB  . GLU A 311  ? 0.2390 0.1945 0.2377 -0.0034 0.0194  0.0191  309  GLU A CB  
2101  C CG  . GLU A 311  ? 0.2798 0.2346 0.2775 -0.0030 0.0186  0.0180  309  GLU A CG  
2102  C CD  . GLU A 311  ? 0.2866 0.2429 0.2846 -0.0031 0.0181  0.0175  309  GLU A CD  
2103  O OE1 . GLU A 311  ? 0.2626 0.2202 0.2620 -0.0034 0.0181  0.0177  309  GLU A OE1 
2104  O OE2 . GLU A 311  ? 0.3521 0.3086 0.3492 -0.0029 0.0176  0.0168  309  GLU A OE2 
2105  N N   . ALA A 312  ? 0.2391 0.1947 0.2400 -0.0051 0.0207  0.0218  310  ALA A N   
2106  C CA  . ALA A 312  ? 0.2315 0.1886 0.2331 -0.0058 0.0217  0.0233  310  ALA A CA  
2107  C C   . ALA A 312  ? 0.2047 0.1647 0.2058 -0.0048 0.0226  0.0232  310  ALA A C   
2108  O O   . ALA A 312  ? 0.2281 0.1907 0.2306 -0.0053 0.0234  0.0239  310  ALA A O   
2109  C CB  . ALA A 312  ? 0.2241 0.1797 0.2245 -0.0059 0.0219  0.0248  310  ALA A CB  
2110  N N   . ASP A 313  ? 0.2036 0.1633 0.2032 -0.0035 0.0224  0.0221  311  ASP A N   
2111  C CA  . ASP A 313  ? 0.2401 0.2021 0.2395 -0.0024 0.0231  0.0217  311  ASP A CA  
2112  C C   . ASP A 313  ? 0.2358 0.1992 0.2369 -0.0023 0.0227  0.0209  311  ASP A C   
2113  O O   . ASP A 313  ? 0.2190 0.1842 0.2204 -0.0012 0.0229  0.0203  311  ASP A O   
2114  C CB  . ASP A 313  ? 0.2322 0.1931 0.2294 -0.0010 0.0229  0.0209  311  ASP A CB  
2115  C CG  . ASP A 313  ? 0.2576 0.2166 0.2544 -0.0008 0.0217  0.0199  311  ASP A CG  
2116  O OD1 . ASP A 313  ? 0.2607 0.2194 0.2587 -0.0015 0.0211  0.0198  311  ASP A OD1 
2117  O OD2 . ASP A 313  ? 0.3182 0.2763 0.3136 0.0001  0.0215  0.0193  311  ASP A OD2 
2118  N N   . ARG A 314  ? 0.2015 0.1644 0.2040 -0.0032 0.0219  0.0208  312  ARG A N   
2119  C CA  . ARG A 314  ? 0.2004 0.1650 0.2047 -0.0032 0.0215  0.0203  312  ARG A CA  
2120  C C   . ARG A 314  ? 0.2031 0.1697 0.2098 -0.0045 0.0218  0.0208  312  ARG A C   
2121  O O   . ARG A 314  ? 0.2291 0.1977 0.2375 -0.0044 0.0215  0.0204  312  ARG A O   
2122  C CB  . ARG A 314  ? 0.2273 0.1905 0.2313 -0.0033 0.0203  0.0196  312  ARG A CB  
2123  C CG  . ARG A 314  ? 0.2410 0.2029 0.2432 -0.0023 0.0199  0.0191  312  ARG A CG  
2124  C CD  . ARG A 314  ? 0.2159 0.1766 0.2173 -0.0026 0.0189  0.0187  312  ARG A CD  
2125  N NE  . ARG A 314  ? 0.2554 0.2157 0.2561 -0.0019 0.0183  0.0186  312  ARG A NE  
2126  C CZ  . ARG A 314  ? 0.2625 0.2222 0.2622 -0.0021 0.0176  0.0185  312  ARG A CZ  
2127  N NH1 . ARG A 314  ? 0.2323 0.1918 0.2315 -0.0028 0.0174  0.0181  312  ARG A NH1 
2128  N NH2 . ARG A 314  ? 0.2617 0.2211 0.2611 -0.0017 0.0169  0.0187  312  ARG A NH2 
2129  N N   . LEU A 315  ? 0.2021 0.1682 0.2090 -0.0056 0.0223  0.0219  313  LEU A N   
2130  C CA  . LEU A 315  ? 0.2028 0.1707 0.2123 -0.0071 0.0225  0.0226  313  LEU A CA  
2131  C C   . LEU A 315  ? 0.2171 0.1891 0.2282 -0.0068 0.0234  0.0227  313  LEU A C   
2132  O O   . LEU A 315  ? 0.2017 0.1756 0.2150 -0.0071 0.0229  0.0221  313  LEU A O   
2133  C CB  . LEU A 315  ? 0.2168 0.1835 0.2263 -0.0084 0.0230  0.0242  313  LEU A CB  
2134  C CG  . LEU A 315  ? 0.2171 0.1838 0.2293 -0.0105 0.0226  0.0249  313  LEU A CG  
2135  C CD1 . LEU A 315  ? 0.2428 0.2074 0.2547 -0.0116 0.0228  0.0267  313  LEU A CD1 
2136  C CD2 . LEU A 315  ? 0.2410 0.2119 0.2559 -0.0113 0.0232  0.0252  313  LEU A CD2 
2137  N N   . GLU A 316  ? 0.2224 0.1962 0.2325 -0.0060 0.0245  0.0232  314  GLU A N   
2138  C CA  . GLU A 316  ? 0.2212 0.1996 0.2332 -0.0057 0.0254  0.0232  314  GLU A CA  
2139  C C   . GLU A 316  ? 0.2179 0.1973 0.2306 -0.0041 0.0247  0.0215  314  GLU A C   
2140  O O   . GLU A 316  ? 0.2148 0.1975 0.2298 -0.0040 0.0248  0.0212  314  GLU A O   
2141  C CB  . GLU A 316  ? 0.2268 0.2075 0.2375 -0.0052 0.0269  0.0239  314  GLU A CB  
2142  C CG  . GLU A 316  ? 0.2364 0.2166 0.2470 -0.0072 0.0276  0.0262  314  GLU A CG  
2143  C CD  . GLU A 316  ? 0.2766 0.2596 0.2857 -0.0069 0.0290  0.0273  314  GLU A CD  
2144  O OE1 . GLU A 316  ? 0.2613 0.2489 0.2709 -0.0058 0.0300  0.0266  314  GLU A OE1 
2145  O OE2 . GLU A 316  ? 0.2563 0.2371 0.2636 -0.0076 0.0291  0.0288  314  GLU A OE2 
2146  N N   . LEU A 317  ? 0.2013 0.1779 0.2120 -0.0027 0.0239  0.0206  315  LEU A N   
2147  C CA  . LEU A 317  ? 0.2221 0.1990 0.2336 -0.0014 0.0228  0.0194  315  LEU A CA  
2148  C C   . LEU A 317  ? 0.2240 0.2012 0.2374 -0.0023 0.0219  0.0194  315  LEU A C   
2149  O O   . LEU A 317  ? 0.2202 0.1997 0.2355 -0.0016 0.0214  0.0188  315  LEU A O   
2150  C CB  . LEU A 317  ? 0.2501 0.2235 0.2593 -0.0004 0.0220  0.0188  315  LEU A CB  
2151  C CG  . LEU A 317  ? 0.2358 0.2086 0.2457 0.0008  0.0206  0.0180  315  LEU A CG  
2152  C CD1 . LEU A 317  ? 0.2648 0.2403 0.2762 0.0025  0.0207  0.0171  315  LEU A CD1 
2153  C CD2 . LEU A 317  ? 0.2913 0.2607 0.2990 0.0013  0.0198  0.0178  315  LEU A CD2 
2154  N N   . SER A 318  ? 0.2243 0.1995 0.2374 -0.0038 0.0214  0.0198  316  SER A N   
2155  C CA  . SER A 318  ? 0.2365 0.2121 0.2512 -0.0047 0.0204  0.0195  316  SER A CA  
2156  C C   . SER A 318  ? 0.2508 0.2302 0.2686 -0.0056 0.0209  0.0197  316  SER A C   
2157  O O   . SER A 318  ? 0.2072 0.1883 0.2268 -0.0057 0.0200  0.0192  316  SER A O   
2158  C CB  . SER A 318  ? 0.2327 0.2056 0.2466 -0.0060 0.0198  0.0195  316  SER A CB  
2159  O OG  . SER A 318  ? 0.2003 0.1730 0.2150 -0.0074 0.0205  0.0203  316  SER A OG  
2160  N N   . LEU A 319  ? 0.2000 0.1810 0.2183 -0.0063 0.0223  0.0206  317  LEU A N   
2161  C CA  . LEU A 319  ? 0.2012 0.1863 0.2225 -0.0073 0.0229  0.0210  317  LEU A CA  
2162  C C   . LEU A 319  ? 0.2247 0.2135 0.2475 -0.0056 0.0229  0.0201  317  LEU A C   
2163  O O   . LEU A 319  ? 0.2130 0.2051 0.2386 -0.0060 0.0226  0.0198  317  LEU A O   
2164  C CB  . LEU A 319  ? 0.2017 0.1882 0.2230 -0.0084 0.0245  0.0225  317  LEU A CB  
2165  C CG  . LEU A 319  ? 0.2354 0.2185 0.2560 -0.0102 0.0244  0.0237  317  LEU A CG  
2166  C CD1 . LEU A 319  ? 0.2230 0.2078 0.2434 -0.0112 0.0259  0.0256  317  LEU A CD1 
2167  C CD2 . LEU A 319  ? 0.2150 0.1976 0.2382 -0.0120 0.0233  0.0236  317  LEU A CD2 
2168  N N   . ASP A 320  ? 0.2316 0.2198 0.2527 -0.0035 0.0229  0.0194  318  ASP A N   
2169  C CA  . ASP A 320  ? 0.2325 0.2236 0.2551 -0.0016 0.0226  0.0182  318  ASP A CA  
2170  C C   . ASP A 320  ? 0.2405 0.2309 0.2643 -0.0013 0.0208  0.0177  318  ASP A C   
2171  O O   . ASP A 320  ? 0.2403 0.2341 0.2666 -0.0006 0.0204  0.0171  318  ASP A O   
2172  C CB  . ASP A 320  ? 0.2396 0.2297 0.2604 0.0006  0.0227  0.0174  318  ASP A CB  
2173  C CG  . ASP A 320  ? 0.2946 0.2875 0.3149 0.0008  0.0245  0.0176  318  ASP A CG  
2174  O OD1 . ASP A 320  ? 0.3238 0.3217 0.3464 0.0006  0.0254  0.0176  318  ASP A OD1 
2175  O OD2 . ASP A 320  ? 0.3339 0.3244 0.3515 0.0010  0.0249  0.0178  318  ASP A OD2 
2176  N N   . LEU A 321  ? 0.2033 0.1897 0.2251 -0.0018 0.0198  0.0179  319  LEU A N   
2177  C CA  . LEU A 321  ? 0.2023 0.1884 0.2248 -0.0017 0.0182  0.0176  319  LEU A CA  
2178  C C   . LEU A 321  ? 0.2187 0.2074 0.2437 -0.0033 0.0180  0.0177  319  LEU A C   
2179  O O   . LEU A 321  ? 0.2396 0.2309 0.2667 -0.0029 0.0171  0.0172  319  LEU A O   
2180  C CB  . LEU A 321  ? 0.2371 0.2192 0.2569 -0.0019 0.0172  0.0179  319  LEU A CB  
2181  C CG  . LEU A 321  ? 0.3000 0.2798 0.3180 -0.0002 0.0167  0.0178  319  LEU A CG  
2182  C CD1 . LEU A 321  ? 0.3372 0.3149 0.3532 -0.0002 0.0179  0.0179  319  LEU A CD1 
2183  C CD2 . LEU A 321  ? 0.3083 0.2859 0.3249 -0.0003 0.0153  0.0182  319  LEU A CD2 
2184  N N   . LEU A 322  ? 0.2189 0.2068 0.2439 -0.0052 0.0188  0.0182  320  LEU A N   
2185  C CA  . LEU A 322  ? 0.2196 0.2097 0.2472 -0.0070 0.0185  0.0182  320  LEU A CA  
2186  C C   . LEU A 322  ? 0.2057 0.2009 0.2366 -0.0069 0.0191  0.0181  320  LEU A C   
2187  O O   . LEU A 322  ? 0.2240 0.2218 0.2573 -0.0073 0.0182  0.0175  320  LEU A O   
2188  C CB  . LEU A 322  ? 0.2198 0.2081 0.2472 -0.0091 0.0192  0.0190  320  LEU A CB  
2189  C CG  . LEU A 322  ? 0.2000 0.1898 0.2305 -0.0112 0.0187  0.0189  320  LEU A CG  
2190  C CD1 . LEU A 322  ? 0.2090 0.1977 0.2393 -0.0112 0.0169  0.0176  320  LEU A CD1 
2191  C CD2 . LEU A 322  ? 0.2030 0.1906 0.2334 -0.0131 0.0194  0.0200  320  LEU A CD2 
2192  N N   . GLU A 323  ? 0.2537 0.2507 0.2845 -0.0061 0.0205  0.0184  321  GLU A N   
2193  C CA  A GLU A 323  ? 0.2442 0.2468 0.2781 -0.0059 0.0213  0.0182  321  GLU A CA  
2194  C CA  B GLU A 323  ? 0.2446 0.2472 0.2786 -0.0060 0.0213  0.0182  321  GLU A CA  
2195  C C   . GLU A 323  ? 0.2585 0.2631 0.2939 -0.0039 0.0200  0.0170  321  GLU A C   
2196  O O   . GLU A 323  ? 0.2243 0.2329 0.2628 -0.0043 0.0196  0.0165  321  GLU A O   
2197  C CB  A GLU A 323  ? 0.2719 0.2765 0.3052 -0.0053 0.0231  0.0186  321  GLU A CB  
2198  C CB  B GLU A 323  ? 0.2720 0.2768 0.3055 -0.0055 0.0231  0.0187  321  GLU A CB  
2199  C CG  A GLU A 323  ? 0.2354 0.2465 0.2717 -0.0044 0.0239  0.0180  321  GLU A CG  
2200  C CG  B GLU A 323  ? 0.2868 0.2971 0.3235 -0.0071 0.0244  0.0193  321  GLU A CG  
2201  C CD  A GLU A 323  ? 0.3072 0.3223 0.3446 -0.0060 0.0260  0.0192  321  GLU A CD  
2202  C CD  B GLU A 323  ? 0.3081 0.3233 0.3454 -0.0056 0.0259  0.0190  321  GLU A CD  
2203  O OE1 A GLU A 323  ? 0.2951 0.3081 0.3319 -0.0085 0.0264  0.0208  321  GLU A OE1 
2204  O OE1 B GLU A 323  ? 0.2995 0.3129 0.3340 -0.0039 0.0264  0.0187  321  GLU A OE1 
2205  O OE2 A GLU A 323  ? 0.3829 0.4034 0.4217 -0.0049 0.0271  0.0186  321  GLU A OE2 
2206  O OE2 B GLU A 323  ? 0.3221 0.3431 0.3625 -0.0060 0.0266  0.0189  321  GLU A OE2 
2207  N N   . VAL A 324  ? 0.2238 0.2258 0.2571 -0.0017 0.0192  0.0164  322  VAL A N   
2208  C CA  . VAL A 324  ? 0.2028 0.2061 0.2374 0.0003  0.0177  0.0155  322  VAL A CA  
2209  C C   . VAL A 324  ? 0.2229 0.2263 0.2585 -0.0007 0.0161  0.0155  322  VAL A C   
2210  O O   . VAL A 324  ? 0.2291 0.2362 0.2675 -0.0001 0.0153  0.0150  322  VAL A O   
2211  C CB  . VAL A 324  ? 0.2260 0.2255 0.2581 0.0024  0.0169  0.0152  322  VAL A CB  
2212  C CG1 . VAL A 324  ? 0.2768 0.2772 0.3105 0.0044  0.0150  0.0146  322  VAL A CG1 
2213  C CG2 . VAL A 324  ? 0.2695 0.2694 0.3008 0.0036  0.0183  0.0148  322  VAL A CG2 
2214  N N   . LEU A 325  ? 0.1979 0.1976 0.2313 -0.0020 0.0156  0.0161  323  LEU A N   
2215  C CA  . LEU A 325  ? 0.2152 0.2151 0.2492 -0.0029 0.0140  0.0159  323  LEU A CA  
2216  C C   . LEU A 325  ? 0.2225 0.2267 0.2601 -0.0044 0.0142  0.0155  323  LEU A C   
2217  O O   . LEU A 325  ? 0.1980 0.2049 0.2376 -0.0041 0.0129  0.0149  323  LEU A O   
2218  C CB  . LEU A 325  ? 0.2090 0.2049 0.2402 -0.0040 0.0137  0.0162  323  LEU A CB  
2219  C CG  . LEU A 325  ? 0.1996 0.1917 0.2275 -0.0027 0.0133  0.0166  323  LEU A CG  
2220  C CD1 . LEU A 325  ? 0.2027 0.1914 0.2280 -0.0040 0.0135  0.0168  323  LEU A CD1 
2221  C CD2 . LEU A 325  ? 0.2240 0.2166 0.2518 -0.0014 0.0114  0.0167  323  LEU A CD2 
2222  N N   . CYS A 326  ? 0.2155 0.2202 0.2539 -0.0063 0.0157  0.0159  324  CYS A N   
2223  C CA  . CYS A 326  ? 0.2109 0.2192 0.2529 -0.0082 0.0158  0.0158  324  CYS A CA  
2224  C C   . CYS A 326  ? 0.2513 0.2654 0.2967 -0.0073 0.0161  0.0153  324  CYS A C   
2225  O O   . CYS A 326  ? 0.2368 0.2546 0.2855 -0.0085 0.0156  0.0149  324  CYS A O   
2226  C CB  . CYS A 326  ? 0.2219 0.2292 0.2641 -0.0106 0.0172  0.0167  324  CYS A CB  
2227  S SG  . CYS A 326  ? 0.2671 0.2684 0.3066 -0.0119 0.0163  0.0167  324  CYS A SG  
2228  N N   . LEU A 327  ? 0.2053 0.2203 0.2500 -0.0051 0.0168  0.0152  325  LEU A N   
2229  C CA  . LEU A 327  ? 0.2151 0.2358 0.2630 -0.0037 0.0171  0.0145  325  LEU A CA  
2230  C C   . LEU A 327  ? 0.2273 0.2484 0.2756 -0.0012 0.0151  0.0135  325  LEU A C   
2231  O O   . LEU A 327  ? 0.2218 0.2476 0.2730 0.0002  0.0149  0.0127  325  LEU A O   
2232  C CB  . LEU A 327  ? 0.2564 0.2787 0.3038 -0.0026 0.0189  0.0145  325  LEU A CB  
2233  C CG  . LEU A 327  ? 0.3069 0.3299 0.3542 -0.0050 0.0210  0.0158  325  LEU A CG  
2234  C CD1 . LEU A 327  ? 0.3415 0.3660 0.3876 -0.0035 0.0227  0.0157  325  LEU A CD1 
2235  C CD2 . LEU A 327  ? 0.3103 0.3387 0.3617 -0.0073 0.0215  0.0162  325  LEU A CD2 
2236  N N   . ASP A 328  ? 0.2162 0.2326 0.2617 -0.0007 0.0136  0.0138  326  ASP A N   
2237  C CA  . ASP A 328  ? 0.2229 0.2391 0.2684 0.0016  0.0115  0.0134  326  ASP A CA  
2238  C C   . ASP A 328  ? 0.2260 0.2456 0.2741 0.0008  0.0101  0.0130  326  ASP A C   
2239  O O   . ASP A 328  ? 0.2101 0.2284 0.2574 -0.0010 0.0095  0.0132  326  ASP A O   
2240  C CB  . ASP A 328  ? 0.2341 0.2445 0.2756 0.0020  0.0106  0.0142  326  ASP A CB  
2241  C CG  . ASP A 328  ? 0.2697 0.2794 0.3111 0.0045  0.0085  0.0143  326  ASP A CG  
2242  O OD1 . ASP A 328  ? 0.2763 0.2891 0.3199 0.0051  0.0071  0.0139  326  ASP A OD1 
2243  O OD2 . ASP A 328  ? 0.2875 0.2933 0.3266 0.0058  0.0083  0.0147  326  ASP A OD2 
2244  N N   . GLY A 329  ? 0.2184 0.2426 0.2697 0.0025  0.0094  0.0122  327  GLY A N   
2245  C CA  . GLY A 329  ? 0.2432 0.2713 0.2973 0.0018  0.0080  0.0116  327  GLY A CA  
2246  C C   . GLY A 329  ? 0.2216 0.2473 0.2737 0.0021  0.0057  0.0120  327  GLY A C   
2247  O O   . GLY A 329  ? 0.2165 0.2447 0.2701 0.0009  0.0047  0.0116  327  GLY A O   
2248  N N   . ASP A 330  ? 0.2298 0.2510 0.2786 0.0036  0.0049  0.0129  328  ASP A N   
2249  C CA  . ASP A 330  ? 0.2201 0.2393 0.2666 0.0036  0.0029  0.0136  328  ASP A CA  
2250  C C   . ASP A 330  ? 0.2081 0.2260 0.2529 0.0010  0.0032  0.0135  328  ASP A C   
2251  O O   . ASP A 330  ? 0.2174 0.2357 0.2611 0.0007  0.0016  0.0136  328  ASP A O   
2252  C CB  . ASP A 330  ? 0.2103 0.2247 0.2535 0.0052  0.0022  0.0149  328  ASP A CB  
2253  C CG  . ASP A 330  ? 0.2883 0.3033 0.3332 0.0080  0.0011  0.0149  328  ASP A CG  
2254  O OD1 . ASP A 330  ? 0.3299 0.3494 0.3781 0.0090  0.0001  0.0142  328  ASP A OD1 
2255  O OD2 . ASP A 330  ? 0.2727 0.2838 0.3159 0.0093  0.0010  0.0156  328  ASP A OD2 
2256  N N   . LEU A 331  ? 0.1999 0.2164 0.2444 -0.0007 0.0052  0.0133  329  LEU A N   
2257  C CA  . LEU A 331  ? 0.1997 0.2146 0.2429 -0.0030 0.0055  0.0130  329  LEU A CA  
2258  C C   . LEU A 331  ? 0.2376 0.2561 0.2844 -0.0050 0.0056  0.0120  329  LEU A C   
2259  O O   . LEU A 331  ? 0.2211 0.2383 0.2675 -0.0070 0.0058  0.0115  329  LEU A O   
2260  C CB  . LEU A 331  ? 0.1992 0.2096 0.2398 -0.0037 0.0072  0.0136  329  LEU A CB  
2261  C CG  . LEU A 331  ? 0.2177 0.2240 0.2543 -0.0025 0.0067  0.0146  329  LEU A CG  
2262  C CD1 . LEU A 331  ? 0.1990 0.2015 0.2335 -0.0028 0.0085  0.0151  329  LEU A CD1 
2263  C CD2 . LEU A 331  ? 0.2002 0.2057 0.2346 -0.0031 0.0053  0.0145  329  LEU A CD2 
2264  N N   . SER A 332  ? 0.2114 0.2346 0.2619 -0.0045 0.0055  0.0115  330  SER A N   
2265  C CA  . SER A 332  ? 0.2323 0.2593 0.2866 -0.0066 0.0058  0.0106  330  SER A CA  
2266  C C   . SER A 332  ? 0.2199 0.2479 0.2746 -0.0078 0.0039  0.0096  330  SER A C   
2267  O O   . SER A 332  ? 0.2311 0.2589 0.2840 -0.0064 0.0022  0.0095  330  SER A O   
2268  C CB  . SER A 332  ? 0.2347 0.2673 0.2930 -0.0056 0.0060  0.0103  330  SER A CB  
2269  O OG  . SER A 332  ? 0.2724 0.3070 0.3311 -0.0035 0.0040  0.0099  330  SER A OG  
2270  N N   . GLY A 333  ? 0.2159 0.2451 0.2733 -0.0103 0.0042  0.0088  331  GLY A N   
2271  C CA  . GLY A 333  ? 0.2405 0.2709 0.2988 -0.0115 0.0023  0.0073  331  GLY A CA  
2272  C C   . GLY A 333  ? 0.2337 0.2596 0.2887 -0.0123 0.0018  0.0068  331  GLY A C   
2273  O O   . GLY A 333  ? 0.2442 0.2711 0.2997 -0.0132 0.0002  0.0052  331  GLY A O   
2274  N N   . TRP A 334  ? 0.2017 0.2230 0.2535 -0.0120 0.0032  0.0079  332  TRP A N   
2275  C CA  . TRP A 334  ? 0.2054 0.2225 0.2540 -0.0125 0.0029  0.0074  332  TRP A CA  
2276  C C   . TRP A 334  ? 0.2022 0.2158 0.2510 -0.0141 0.0047  0.0081  332  TRP A C   
2277  O O   . TRP A 334  ? 0.2109 0.2237 0.2593 -0.0136 0.0064  0.0096  332  TRP A O   
2278  C CB  . TRP A 334  ? 0.2236 0.2386 0.2678 -0.0104 0.0027  0.0084  332  TRP A CB  
2279  C CG  . TRP A 334  ? 0.2022 0.2129 0.2426 -0.0106 0.0029  0.0083  332  TRP A CG  
2280  C CD1 . TRP A 334  ? 0.2099 0.2203 0.2491 -0.0112 0.0017  0.0067  332  TRP A CD1 
2281  C CD2 . TRP A 334  ? 0.2082 0.2149 0.2456 -0.0099 0.0043  0.0096  332  TRP A CD2 
2282  N NE1 . TRP A 334  ? 0.2136 0.2201 0.2493 -0.0109 0.0023  0.0070  332  TRP A NE1 
2283  C CE2 . TRP A 334  ? 0.2020 0.2062 0.2367 -0.0102 0.0039  0.0089  332  TRP A CE2 
2284  C CE3 . TRP A 334  ? 0.2005 0.2059 0.2375 -0.0090 0.0059  0.0112  332  TRP A CE3 
2285  C CZ2 . TRP A 334  ? 0.2016 0.2019 0.2331 -0.0097 0.0050  0.0098  332  TRP A CZ2 
2286  C CZ3 . TRP A 334  ? 0.2144 0.2157 0.2481 -0.0085 0.0069  0.0121  332  TRP A CZ3 
2287  C CH2 . TRP A 334  ? 0.2087 0.2075 0.2397 -0.0089 0.0065  0.0114  332  TRP A CH2 
2288  N N   . ASN A 335  ? 0.2090 0.2206 0.2584 -0.0159 0.0041  0.0069  333  ASN A N   
2289  C CA  . ASN A 335  ? 0.2077 0.2155 0.2572 -0.0175 0.0054  0.0077  333  ASN A CA  
2290  C C   . ASN A 335  ? 0.2340 0.2371 0.2796 -0.0170 0.0054  0.0073  333  ASN A C   
2291  O O   . ASN A 335  ? 0.2281 0.2278 0.2740 -0.0183 0.0058  0.0074  333  ASN A O   
2292  C CB  . ASN A 335  ? 0.2576 0.2663 0.3115 -0.0202 0.0048  0.0068  333  ASN A CB  
2293  C CG  . ASN A 335  ? 0.2490 0.2620 0.3070 -0.0212 0.0056  0.0077  333  ASN A CG  
2294  O OD1 . ASN A 335  ? 0.2447 0.2588 0.3022 -0.0204 0.0073  0.0094  333  ASN A OD1 
2295  N ND2 . ASN A 335  ? 0.2858 0.3016 0.3480 -0.0230 0.0043  0.0065  333  ASN A ND2 
2296  N N   . GLY A 336  ? 0.2036 0.2066 0.2458 -0.0150 0.0048  0.0071  334  GLY A N   
2297  C CA  . GLY A 336  ? 0.2040 0.2034 0.2426 -0.0145 0.0046  0.0066  334  GLY A CA  
2298  C C   . GLY A 336  ? 0.2147 0.2106 0.2505 -0.0137 0.0063  0.0083  334  GLY A C   
2299  O O   . GLY A 336  ? 0.2150 0.2079 0.2481 -0.0134 0.0063  0.0079  334  GLY A O   
2300  N N   . MET A 337  ? 0.2034 0.1998 0.2398 -0.0134 0.0078  0.0101  335  MET A N   
2301  C CA  A MET A 337  ? 0.2073 0.2006 0.2412 -0.0126 0.0093  0.0115  335  MET A CA  
2302  C CA  B MET A 337  ? 0.2075 0.2007 0.2414 -0.0126 0.0093  0.0115  335  MET A CA  
2303  C C   . MET A 337  ? 0.2114 0.2013 0.2456 -0.0141 0.0100  0.0116  335  MET A C   
2304  O O   . MET A 337  ? 0.2032 0.1937 0.2405 -0.0159 0.0102  0.0118  335  MET A O   
2305  C CB  A MET A 337  ? 0.2186 0.2137 0.2534 -0.0118 0.0106  0.0130  335  MET A CB  
2306  C CB  B MET A 337  ? 0.2187 0.2137 0.2534 -0.0118 0.0106  0.0130  335  MET A CB  
2307  C CG  A MET A 337  ? 0.2461 0.2383 0.2783 -0.0109 0.0120  0.0142  335  MET A CG  
2308  C CG  B MET A 337  ? 0.2462 0.2382 0.2786 -0.0112 0.0122  0.0142  335  MET A CG  
2309  S SD  A MET A 337  ? 0.3416 0.3316 0.3696 -0.0090 0.0114  0.0143  335  MET A SD  
2310  S SD  B MET A 337  ? 0.2698 0.2625 0.3004 -0.0087 0.0125  0.0151  335  MET A SD  
2311  C CE  A MET A 337  ? 0.2516 0.2449 0.2806 -0.0072 0.0108  0.0148  335  MET A CE  
2312  C CE  B MET A 337  ? 0.2426 0.2347 0.2709 -0.0078 0.0107  0.0145  335  MET A CE  
2313  N N   . GLY A 338  ? 0.2033 0.1897 0.2343 -0.0135 0.0102  0.0117  336  GLY A N   
2314  C CA  . GLY A 338  ? 0.2035 0.1864 0.2346 -0.0146 0.0106  0.0118  336  GLY A CA  
2315  C C   . GLY A 338  ? 0.2327 0.2129 0.2609 -0.0137 0.0121  0.0133  336  GLY A C   
2316  O O   . GLY A 338  ? 0.2123 0.1929 0.2383 -0.0122 0.0126  0.0138  336  GLY A O   
2317  N N   . PHE A 339  ? 0.2046 0.1820 0.2332 -0.0148 0.0127  0.0139  337  PHE A N   
2318  C CA  . PHE A 339  ? 0.2041 0.1794 0.2305 -0.0141 0.0141  0.0155  337  PHE A CA  
2319  C C   . PHE A 339  ? 0.2140 0.1854 0.2402 -0.0151 0.0140  0.0157  337  PHE A C   
2320  O O   . PHE A 339  ? 0.2073 0.1782 0.2363 -0.0168 0.0135  0.0159  337  PHE A O   
2321  C CB  . PHE A 339  ? 0.2078 0.1855 0.2355 -0.0144 0.0156  0.0172  337  PHE A CB  
2322  C CG  . PHE A 339  ? 0.2193 0.1959 0.2444 -0.0132 0.0170  0.0184  337  PHE A CG  
2323  C CD1 . PHE A 339  ? 0.2054 0.1828 0.2285 -0.0113 0.0173  0.0182  337  PHE A CD1 
2324  C CD2 . PHE A 339  ? 0.2061 0.1808 0.2308 -0.0141 0.0180  0.0198  337  PHE A CD2 
2325  C CE1 . PHE A 339  ? 0.2391 0.2155 0.2600 -0.0102 0.0184  0.0191  337  PHE A CE1 
2326  C CE2 . PHE A 339  ? 0.2383 0.2123 0.2606 -0.0129 0.0192  0.0208  337  PHE A CE2 
2327  C CZ  . PHE A 339  ? 0.2146 0.1895 0.2350 -0.0110 0.0194  0.0203  337  PHE A CZ  
2328  N N   . VAL A 340  ? 0.2112 0.1800 0.2344 -0.0139 0.0142  0.0156  338  VAL A N   
2329  C CA  . VAL A 340  ? 0.2073 0.1723 0.2300 -0.0143 0.0139  0.0157  338  VAL A CA  
2330  C C   . VAL A 340  ? 0.2076 0.1717 0.2300 -0.0148 0.0154  0.0181  338  VAL A C   
2331  O O   . VAL A 340  ? 0.2090 0.1745 0.2296 -0.0138 0.0167  0.0191  338  VAL A O   
2332  C CB  . VAL A 340  ? 0.2137 0.1769 0.2335 -0.0128 0.0134  0.0145  338  VAL A CB  
2333  C CG1 . VAL A 340  ? 0.2085 0.1678 0.2279 -0.0130 0.0130  0.0145  338  VAL A CG1 
2334  C CG2 . VAL A 340  ? 0.2061 0.1710 0.2260 -0.0124 0.0120  0.0122  338  VAL A CG2 
2335  N N   . VAL A 341  ? 0.2101 0.1717 0.2340 -0.0162 0.0151  0.0190  339  VAL A N   
2336  C CA  . VAL A 341  ? 0.2112 0.1715 0.2342 -0.0166 0.0163  0.0214  339  VAL A CA  
2337  C C   . VAL A 341  ? 0.2134 0.1691 0.2357 -0.0166 0.0152  0.0212  339  VAL A C   
2338  O O   . VAL A 341  ? 0.2152 0.1687 0.2393 -0.0172 0.0136  0.0198  339  VAL A O   
2339  C CB  . VAL A 341  ? 0.2211 0.1834 0.2470 -0.0187 0.0171  0.0235  339  VAL A CB  
2340  C CG1 . VAL A 341  ? 0.2302 0.1975 0.2572 -0.0185 0.0179  0.0232  339  VAL A CG1 
2341  C CG2 . VAL A 341  ? 0.2947 0.2551 0.3240 -0.0207 0.0155  0.0233  339  VAL A CG2 
2342  N N   . GLN A 342  ? 0.2232 0.1774 0.2428 -0.0156 0.0161  0.0224  340  GLN A N   
2343  C CA  . GLN A 342  ? 0.2205 0.1706 0.2390 -0.0150 0.0151  0.0220  340  GLN A CA  
2344  C C   . GLN A 342  ? 0.2184 0.1662 0.2378 -0.0164 0.0152  0.0247  340  GLN A C   
2345  O O   . GLN A 342  ? 0.2215 0.1706 0.2395 -0.0164 0.0167  0.0269  340  GLN A O   
2346  C CB  . GLN A 342  ? 0.2133 0.1633 0.2281 -0.0129 0.0158  0.0215  340  GLN A CB  
2347  C CG  . GLN A 342  ? 0.2104 0.1628 0.2242 -0.0117 0.0157  0.0194  340  GLN A CG  
2348  C CD  . GLN A 342  ? 0.2083 0.1620 0.2192 -0.0102 0.0169  0.0198  340  GLN A CD  
2349  O OE1 . GLN A 342  ? 0.2120 0.1671 0.2224 -0.0103 0.0182  0.0214  340  GLN A OE1 
2350  N NE2 . GLN A 342  ? 0.2247 0.1780 0.2336 -0.0089 0.0164  0.0183  340  GLN A NE2 
2351  N N   . ALA A 343  ? 0.2214 0.1659 0.2432 -0.0175 0.0135  0.0244  341  ALA A N   
2352  C CA  . ALA A 343  ? 0.2251 0.1671 0.2483 -0.0191 0.0133  0.0272  341  ALA A CA  
2353  C C   . ALA A 343  ? 0.2315 0.1707 0.2518 -0.0179 0.0134  0.0285  341  ALA A C   
2354  O O   . ALA A 343  ? 0.2292 0.1671 0.2499 -0.0191 0.0136  0.0315  341  ALA A O   
2355  C CB  . ALA A 343  ? 0.2376 0.1761 0.2645 -0.0206 0.0110  0.0263  341  ALA A CB  
2356  N N   . TYR A 344  ? 0.2300 0.1689 0.2476 -0.0156 0.0133  0.0264  342  TYR A N   
2357  C CA  . TYR A 344  ? 0.2365 0.1736 0.2515 -0.0145 0.0136  0.0278  342  TYR A CA  
2358  C C   . TYR A 344  ? 0.2287 0.1691 0.2412 -0.0143 0.0158  0.0299  342  TYR A C   
2359  O O   . TYR A 344  ? 0.2318 0.1713 0.2421 -0.0135 0.0162  0.0312  342  TYR A O   
2360  C CB  . TYR A 344  ? 0.2240 0.1596 0.2371 -0.0122 0.0127  0.0250  342  TYR A CB  
2361  C CG  . TYR A 344  ? 0.2430 0.1818 0.2536 -0.0106 0.0138  0.0231  342  TYR A CG  
2362  C CD1 . TYR A 344  ? 0.2172 0.1599 0.2275 -0.0109 0.0152  0.0234  342  TYR A CD1 
2363  C CD2 . TYR A 344  ? 0.2400 0.1780 0.2489 -0.0087 0.0131  0.0210  342  TYR A CD2 
2364  C CE1 . TYR A 344  ? 0.2140 0.1591 0.2223 -0.0095 0.0159  0.0219  342  TYR A CE1 
2365  C CE2 . TYR A 344  ? 0.2395 0.1802 0.2465 -0.0075 0.0139  0.0195  342  TYR A CE2 
2366  C CZ  . TYR A 344  ? 0.2253 0.1693 0.2320 -0.0080 0.0152  0.0201  342  TYR A CZ  
2367  O OH  . TYR A 344  ? 0.2452 0.1914 0.2501 -0.0069 0.0157  0.0189  342  TYR A OH  
2368  N N   . GLY A 345  ? 0.2328 0.1773 0.2460 -0.0150 0.0171  0.0301  343  GLY A N   
2369  C CA  . GLY A 345  ? 0.2201 0.1683 0.2313 -0.0145 0.0191  0.0315  343  GLY A CA  
2370  C C   . GLY A 345  ? 0.2294 0.1792 0.2419 -0.0166 0.0200  0.0347  343  GLY A C   
2371  O O   . GLY A 345  ? 0.2304 0.1804 0.2461 -0.0185 0.0196  0.0354  343  GLY A O   
2372  N N   . LYS A 346  ? 0.2233 0.1747 0.2334 -0.0161 0.0213  0.0367  344  LYS A N   
2373  C CA  . LYS A 346  ? 0.2260 0.1796 0.2368 -0.0180 0.0223  0.0401  344  LYS A CA  
2374  C C   . LYS A 346  ? 0.2355 0.1944 0.2484 -0.0191 0.0237  0.0403  344  LYS A C   
2375  O O   . LYS A 346  ? 0.2607 0.2217 0.2754 -0.0213 0.0243  0.0430  344  LYS A O   
2376  C CB  . LYS A 346  ? 0.2267 0.1817 0.2340 -0.0168 0.0234  0.0417  344  LYS A CB  
2377  C CG  . LYS A 346  ? 0.2468 0.1968 0.2524 -0.0159 0.0220  0.0420  344  LYS A CG  
2378  C CD  . LYS A 346  ? 0.2583 0.2101 0.2604 -0.0146 0.0230  0.0433  344  LYS A CD  
2379  C CE  . LYS A 346  ? 0.2730 0.2200 0.2735 -0.0137 0.0215  0.0437  344  LYS A CE  
2380  N NZ  . LYS A 346  ? 0.2780 0.2271 0.2747 -0.0120 0.0224  0.0443  344  LYS A NZ  
2381  N N   . ARG A 347  ? 0.2224 0.1835 0.2352 -0.0177 0.0240  0.0375  345  ARG A N   
2382  C CA  . ARG A 347  ? 0.2466 0.2129 0.2613 -0.0184 0.0252  0.0374  345  ARG A CA  
2383  C C   . ARG A 347  ? 0.2300 0.1957 0.2485 -0.0201 0.0241  0.0367  345  ARG A C   
2384  O O   . ARG A 347  ? 0.2263 0.1964 0.2471 -0.0210 0.0249  0.0369  345  ARG A O   
2385  C CB  . ARG A 347  ? 0.2377 0.2066 0.2506 -0.0159 0.0259  0.0349  345  ARG A CB  
2386  C CG  . ARG A 347  ? 0.2163 0.1872 0.2259 -0.0144 0.0273  0.0357  345  ARG A CG  
2387  C CD  . ARG A 347  ? 0.2133 0.1853 0.2212 -0.0119 0.0274  0.0330  345  ARG A CD  
2388  N NE  . ARG A 347  ? 0.2123 0.1796 0.2188 -0.0108 0.0260  0.0313  345  ARG A NE  
2389  C CZ  . ARG A 347  ? 0.2401 0.2071 0.2456 -0.0091 0.0257  0.0291  345  ARG A CZ  
2390  N NH1 . ARG A 347  ? 0.2154 0.1858 0.2210 -0.0079 0.0264  0.0280  345  ARG A NH1 
2391  N NH2 . ARG A 347  ? 0.2092 0.1725 0.2137 -0.0084 0.0244  0.0278  345  ARG A NH2 
2392  N N   . CYS A 348  ? 0.2240 0.1849 0.2435 -0.0204 0.0222  0.0357  346  CYS A N   
2393  C CA  . CYS A 348  ? 0.2224 0.1827 0.2452 -0.0215 0.0209  0.0341  346  CYS A CA  
2394  C C   . CYS A 348  ? 0.2393 0.2028 0.2658 -0.0241 0.0214  0.0359  346  CYS A C   
2395  O O   . CYS A 348  ? 0.2204 0.1871 0.2488 -0.0243 0.0215  0.0344  346  CYS A O   
2396  C CB  . CYS A 348  ? 0.2531 0.2077 0.2765 -0.0217 0.0188  0.0331  346  CYS A CB  
2397  S SG  . CYS A 348  ? 0.2925 0.2467 0.3190 -0.0221 0.0170  0.0300  346  CYS A SG  
2398  N N   . PRO A 349  ? 0.2252 0.1883 0.2529 -0.0263 0.0217  0.0391  347  PRO A N   
2399  C CA  . PRO A 349  ? 0.2436 0.2103 0.2752 -0.0291 0.0221  0.0408  347  PRO A CA  
2400  C C   . PRO A 349  ? 0.2242 0.1979 0.2556 -0.0286 0.0242  0.0408  347  PRO A C   
2401  O O   . PRO A 349  ? 0.2393 0.2166 0.2740 -0.0299 0.0243  0.0404  347  PRO A O   
2402  C CB  . PRO A 349  ? 0.2801 0.2448 0.3124 -0.0314 0.0220  0.0447  347  PRO A CB  
2403  C CG  . PRO A 349  ? 0.2959 0.2580 0.3239 -0.0295 0.0223  0.0454  347  PRO A CG  
2404  C CD  . PRO A 349  ? 0.2412 0.2007 0.2669 -0.0266 0.0215  0.0415  347  PRO A CD  
2405  N N   . PHE A 350  ? 0.2229 0.1988 0.2508 -0.0266 0.0258  0.0411  348  PHE A N   
2406  C CA  . PHE A 350  ? 0.2513 0.2339 0.2790 -0.0257 0.0277  0.0407  348  PHE A CA  
2407  C C   . PHE A 350  ? 0.2171 0.2007 0.2452 -0.0237 0.0271  0.0372  348  PHE A C   
2408  O O   . PHE A 350  ? 0.2251 0.2139 0.2551 -0.0236 0.0279  0.0365  348  PHE A O   
2409  C CB  . PHE A 350  ? 0.2398 0.2241 0.2637 -0.0241 0.0292  0.0417  348  PHE A CB  
2410  C CG  . PHE A 350  ? 0.2764 0.2593 0.2996 -0.0259 0.0294  0.0453  348  PHE A CG  
2411  C CD1 . PHE A 350  ? 0.2533 0.2408 0.2784 -0.0284 0.0307  0.0485  348  PHE A CD1 
2412  C CD2 . PHE A 350  ? 0.2592 0.2360 0.2800 -0.0252 0.0282  0.0457  348  PHE A CD2 
2413  C CE1 . PHE A 350  ? 0.3042 0.2902 0.3287 -0.0303 0.0307  0.0523  348  PHE A CE1 
2414  C CE2 . PHE A 350  ? 0.2863 0.2614 0.3066 -0.0269 0.0282  0.0492  348  PHE A CE2 
2415  C CZ  . PHE A 350  ? 0.3081 0.2877 0.3302 -0.0295 0.0294  0.0527  348  PHE A CZ  
2416  N N   . VAL A 351  ? 0.2158 0.1947 0.2419 -0.0220 0.0258  0.0351  349  VAL A N   
2417  C CA  . VAL A 351  ? 0.2129 0.1923 0.2395 -0.0205 0.0249  0.0321  349  VAL A CA  
2418  C C   . VAL A 351  ? 0.2207 0.2011 0.2514 -0.0224 0.0240  0.0316  349  VAL A C   
2419  O O   . VAL A 351  ? 0.2195 0.2037 0.2519 -0.0219 0.0240  0.0302  349  VAL A O   
2420  C CB  . VAL A 351  ? 0.2119 0.1862 0.2359 -0.0187 0.0236  0.0303  349  VAL A CB  
2421  C CG1 . VAL A 351  ? 0.2094 0.1843 0.2338 -0.0175 0.0227  0.0276  349  VAL A CG1 
2422  C CG2 . VAL A 351  ? 0.2195 0.1932 0.2397 -0.0169 0.0246  0.0306  349  VAL A CG2 
2423  N N   . LEU A 352  ? 0.2257 0.2029 0.2583 -0.0246 0.0228  0.0327  350  LEU A N   
2424  C CA  . LEU A 352  ? 0.2253 0.2034 0.2621 -0.0266 0.0217  0.0321  350  LEU A CA  
2425  C C   . LEU A 352  ? 0.2393 0.2236 0.2790 -0.0282 0.0231  0.0336  350  LEU A C   
2426  O O   . LEU A 352  ? 0.2306 0.2181 0.2730 -0.0285 0.0227  0.0322  350  LEU A O   
2427  C CB  . LEU A 352  ? 0.2424 0.2153 0.2809 -0.0286 0.0200  0.0329  350  LEU A CB  
2428  C CG  . LEU A 352  ? 0.2586 0.2263 0.2953 -0.0271 0.0182  0.0304  350  LEU A CG  
2429  C CD1 . LEU A 352  ? 0.2607 0.2232 0.2990 -0.0289 0.0167  0.0315  350  LEU A CD1 
2430  C CD2 . LEU A 352  ? 0.2364 0.2054 0.2744 -0.0263 0.0171  0.0273  350  LEU A CD2 
2431  N N   . ASP A 353  ? 0.2275 0.2141 0.2667 -0.0292 0.0248  0.0365  351  ASP A N   
2432  C CA  . ASP A 353  ? 0.2185 0.2122 0.2602 -0.0304 0.0264  0.0378  351  ASP A CA  
2433  C C   . ASP A 353  ? 0.2173 0.2156 0.2587 -0.0279 0.0270  0.0353  351  ASP A C   
2434  O O   . ASP A 353  ? 0.2305 0.2335 0.2751 -0.0286 0.0272  0.0347  351  ASP A O   
2435  C CB  . ASP A 353  ? 0.2425 0.2387 0.2827 -0.0312 0.0283  0.0410  351  ASP A CB  
2436  C CG  . ASP A 353  ? 0.2964 0.2893 0.3379 -0.0343 0.0277  0.0443  351  ASP A CG  
2437  O OD1 . ASP A 353  ? 0.2938 0.2840 0.3388 -0.0364 0.0261  0.0442  351  ASP A OD1 
2438  O OD2 . ASP A 353  ? 0.3287 0.3218 0.3680 -0.0346 0.0289  0.0469  351  ASP A OD2 
2439  N N   . PHE A 354  ? 0.2131 0.2099 0.2506 -0.0249 0.0273  0.0338  352  PHE A N   
2440  C CA  . PHE A 354  ? 0.2103 0.2108 0.2474 -0.0223 0.0277  0.0316  352  PHE A CA  
2441  C C   . PHE A 354  ? 0.2238 0.2236 0.2629 -0.0220 0.0260  0.0293  352  PHE A C   
2442  O O   . PHE A 354  ? 0.2184 0.2229 0.2597 -0.0215 0.0261  0.0282  352  PHE A O   
2443  C CB  . PHE A 354  ? 0.2135 0.2117 0.2462 -0.0194 0.0280  0.0306  352  PHE A CB  
2444  C CG  . PHE A 354  ? 0.2322 0.2323 0.2645 -0.0167 0.0277  0.0281  352  PHE A CG  
2445  C CD1 . PHE A 354  ? 0.2494 0.2552 0.2822 -0.0153 0.0291  0.0277  352  PHE A CD1 
2446  C CD2 . PHE A 354  ? 0.2265 0.2229 0.2580 -0.0156 0.0260  0.0262  352  PHE A CD2 
2447  C CE1 . PHE A 354  ? 0.2533 0.2605 0.2861 -0.0127 0.0285  0.0254  352  PHE A CE1 
2448  C CE2 . PHE A 354  ? 0.2610 0.2589 0.2922 -0.0132 0.0256  0.0243  352  PHE A CE2 
2449  C CZ  . PHE A 354  ? 0.2631 0.2660 0.2951 -0.0118 0.0267  0.0239  352  PHE A CZ  
2450  N N   . ILE A 355  ? 0.2090 0.2032 0.2472 -0.0222 0.0242  0.0284  353  ILE A N   
2451  C CA  . ILE A 355  ? 0.2078 0.2014 0.2475 -0.0218 0.0225  0.0261  353  ILE A CA  
2452  C C   . ILE A 355  ? 0.2112 0.2081 0.2556 -0.0242 0.0220  0.0263  353  ILE A C   
2453  O O   . ILE A 355  ? 0.2074 0.2076 0.2537 -0.0236 0.0214  0.0248  353  ILE A O   
2454  C CB  . ILE A 355  ? 0.2082 0.1957 0.2461 -0.0216 0.0209  0.0251  353  ILE A CB  
2455  C CG1 . ILE A 355  ? 0.2142 0.1990 0.2476 -0.0191 0.0212  0.0245  353  ILE A CG1 
2456  C CG2 . ILE A 355  ? 0.2237 0.2112 0.2633 -0.0216 0.0190  0.0228  353  ILE A CG2 
2457  C CD1 . ILE A 355  ? 0.2210 0.2004 0.2525 -0.0188 0.0198  0.0236  353  ILE A CD1 
2458  N N   . ILE A 356  ? 0.2114 0.2075 0.2578 -0.0271 0.0222  0.0284  354  ILE A N   
2459  C CA  . ILE A 356  ? 0.2127 0.2119 0.2640 -0.0297 0.0217  0.0287  354  ILE A CA  
2460  C C   . ILE A 356  ? 0.2148 0.2216 0.2681 -0.0295 0.0232  0.0291  354  ILE A C   
2461  O O   . ILE A 356  ? 0.2108 0.2212 0.2673 -0.0299 0.0225  0.0278  354  ILE A O   
2462  C CB  . ILE A 356  ? 0.2248 0.2215 0.2779 -0.0329 0.0215  0.0313  354  ILE A CB  
2463  C CG1 . ILE A 356  ? 0.2177 0.2071 0.2699 -0.0331 0.0194  0.0303  354  ILE A CG1 
2464  C CG2 . ILE A 356  ? 0.2178 0.2189 0.2763 -0.0361 0.0215  0.0324  354  ILE A CG2 
2465  C CD1 . ILE A 356  ? 0.2215 0.2068 0.2744 -0.0355 0.0192  0.0330  354  ILE A CD1 
2466  N N   . ASP A 357  ? 0.2149 0.2244 0.2663 -0.0286 0.0253  0.0305  355  ASP A N   
2467  C CA  . ASP A 357  ? 0.2196 0.2367 0.2727 -0.0278 0.0267  0.0304  355  ASP A CA  
2468  C C   . ASP A 357  ? 0.2375 0.2559 0.2901 -0.0248 0.0259  0.0274  355  ASP A C   
2469  O O   . ASP A 357  ? 0.2254 0.2494 0.2810 -0.0246 0.0259  0.0265  355  ASP A O   
2470  C CB  . ASP A 357  ? 0.2402 0.2600 0.2909 -0.0270 0.0290  0.0320  355  ASP A CB  
2471  C CG  . ASP A 357  ? 0.2489 0.2768 0.3011 -0.0257 0.0305  0.0314  355  ASP A CG  
2472  O OD1 . ASP A 357  ? 0.2438 0.2774 0.2998 -0.0279 0.0313  0.0326  355  ASP A OD1 
2473  O OD2 . ASP A 357  ? 0.2537 0.2824 0.3037 -0.0224 0.0307  0.0295  355  ASP A OD2 
2474  N N   . LEU A 358  ? 0.2115 0.2250 0.2603 -0.0224 0.0251  0.0261  356  LEU A N   
2475  C CA  . LEU A 358  ? 0.2272 0.2414 0.2754 -0.0197 0.0241  0.0237  356  LEU A CA  
2476  C C   . LEU A 358  ? 0.2051 0.2197 0.2562 -0.0206 0.0222  0.0224  356  LEU A C   
2477  O O   . LEU A 358  ? 0.2148 0.2333 0.2677 -0.0193 0.0217  0.0210  356  LEU A O   
2478  C CB  . LEU A 358  ? 0.2031 0.2118 0.2468 -0.0174 0.0235  0.0229  356  LEU A CB  
2479  C CG  . LEU A 358  ? 0.2255 0.2337 0.2682 -0.0149 0.0222  0.0209  356  LEU A CG  
2480  C CD1 . LEU A 358  ? 0.2415 0.2551 0.2856 -0.0129 0.0228  0.0201  356  LEU A CD1 
2481  C CD2 . LEU A 358  ? 0.2009 0.2034 0.2393 -0.0133 0.0217  0.0206  356  LEU A CD2 
2482  N N   . ALA A 359  ? 0.2232 0.2340 0.2750 -0.0228 0.0211  0.0226  357  ALA A N   
2483  C CA  . ALA A 359  ? 0.2125 0.2240 0.2674 -0.0239 0.0193  0.0212  357  ALA A CA  
2484  C C   . ALA A 359  ? 0.2239 0.2422 0.2836 -0.0255 0.0198  0.0216  357  ALA A C   
2485  O O   . ALA A 359  ? 0.2281 0.2497 0.2899 -0.0249 0.0187  0.0200  357  ALA A O   
2486  C CB  . ALA A 359  ? 0.2219 0.2282 0.2771 -0.0261 0.0179  0.0213  357  ALA A CB  
2487  N N   . ARG A 360  ? 0.2366 0.2573 0.2978 -0.0275 0.0215  0.0239  358  ARG A N   
2488  C CA  . ARG A 360  ? 0.2187 0.2465 0.2846 -0.0292 0.0222  0.0244  358  ARG A CA  
2489  C C   . ARG A 360  ? 0.2579 0.2916 0.3241 -0.0264 0.0229  0.0231  358  ARG A C   
2490  O O   . ARG A 360  ? 0.2838 0.3223 0.3535 -0.0265 0.0223  0.0219  358  ARG A O   
2491  C CB  . ARG A 360  ? 0.2257 0.2553 0.2928 -0.0319 0.0241  0.0275  358  ARG A CB  
2492  C CG  . ARG A 360  ? 0.2960 0.3201 0.3639 -0.0351 0.0230  0.0290  358  ARG A CG  
2493  C CD  . ARG A 360  ? 0.3550 0.3818 0.4250 -0.0383 0.0247  0.0324  358  ARG A CD  
2494  N NE  . ARG A 360  ? 0.3866 0.4066 0.4562 -0.0406 0.0237  0.0341  358  ARG A NE  
2495  C CZ  . ARG A 360  ? 0.4321 0.4497 0.5054 -0.0435 0.0219  0.0343  358  ARG A CZ  
2496  N NH1 . ARG A 360  ? 0.3836 0.4052 0.4614 -0.0447 0.0209  0.0329  358  ARG A NH1 
2497  N NH2 . ARG A 360  ? 0.4397 0.4507 0.5125 -0.0452 0.0209  0.0357  358  ARG A NH2 
2498  N N   . ARG A 361  ? 0.2348 0.2681 0.2974 -0.0238 0.0242  0.0232  359  ARG A N   
2499  C CA  . ARG A 361  ? 0.2596 0.2981 0.3225 -0.0208 0.0247  0.0218  359  ARG A CA  
2500  C C   . ARG A 361  ? 0.2392 0.2766 0.3021 -0.0186 0.0226  0.0194  359  ARG A C   
2501  O O   . ARG A 361  ? 0.2717 0.3145 0.3374 -0.0174 0.0223  0.0182  359  ARG A O   
2502  C CB  . ARG A 361  ? 0.2527 0.2899 0.3116 -0.0184 0.0261  0.0220  359  ARG A CB  
2503  C CG  . ARG A 361  ? 0.2999 0.3396 0.3585 -0.0201 0.0284  0.0243  359  ARG A CG  
2504  C CD  . ARG A 361  ? 0.3299 0.3693 0.3848 -0.0172 0.0296  0.0239  359  ARG A CD  
2505  N NE  . ARG A 361  ? 0.2823 0.3140 0.3328 -0.0166 0.0290  0.0242  359  ARG A NE  
2506  C CZ  . ARG A 361  ? 0.2897 0.3180 0.3371 -0.0136 0.0283  0.0226  359  ARG A CZ  
2507  N NH1 . ARG A 361  ? 0.2678 0.2988 0.3161 -0.0109 0.0277  0.0205  359  ARG A NH1 
2508  N NH2 . ARG A 361  ? 0.2833 0.3053 0.3269 -0.0133 0.0280  0.0231  359  ARG A NH2 
2509  N N   . SER A 362  ? 0.2354 0.2663 0.2951 -0.0180 0.0212  0.0189  360  SER A N   
2510  C CA  . SER A 362  ? 0.2235 0.2531 0.2825 -0.0158 0.0192  0.0171  360  SER A CA  
2511  C C   . SER A 362  ? 0.2388 0.2700 0.3012 -0.0176 0.0175  0.0162  360  SER A C   
2512  O O   . SER A 362  ? 0.2585 0.2908 0.3212 -0.0159 0.0159  0.0148  360  SER A O   
2513  C CB  . SER A 362  ? 0.2493 0.2720 0.3037 -0.0146 0.0184  0.0169  360  SER A CB  
2514  O OG  . SER A 362  ? 0.2356 0.2539 0.2893 -0.0169 0.0179  0.0174  360  SER A OG  
2515  N N   . GLY A 363  ? 0.2262 0.2571 0.2907 -0.0208 0.0176  0.0171  361  GLY A N   
2516  C CA  . GLY A 363  ? 0.2535 0.2849 0.3209 -0.0225 0.0157  0.0160  361  GLY A CA  
2517  C C   . GLY A 363  ? 0.2820 0.3077 0.3465 -0.0219 0.0138  0.0147  361  GLY A C   
2518  O O   . GLY A 363  ? 0.3016 0.3280 0.3680 -0.0226 0.0120  0.0133  361  GLY A O   
2519  N N   . ARG A 364  ? 0.2713 0.2918 0.3314 -0.0206 0.0142  0.0152  362  ARG A N   
2520  C CA  . ARG A 364  ? 0.2438 0.2593 0.3008 -0.0200 0.0127  0.0141  362  ARG A CA  
2521  C C   . ARG A 364  ? 0.2696 0.2807 0.3265 -0.0224 0.0127  0.0146  362  ARG A C   
2522  O O   . ARG A 364  ? 0.2793 0.2888 0.3355 -0.0232 0.0143  0.0164  362  ARG A O   
2523  C CB  . ARG A 364  ? 0.2527 0.2654 0.3052 -0.0172 0.0130  0.0142  362  ARG A CB  
2524  C CG  . ARG A 364  ? 0.3308 0.3471 0.3833 -0.0147 0.0132  0.0141  362  ARG A CG  
2525  C CD  . ARG A 364  ? 0.2816 0.2974 0.3325 -0.0128 0.0113  0.0129  362  ARG A CD  
2526  N NE  . ARG A 364  ? 0.2333 0.2529 0.2852 -0.0106 0.0112  0.0128  362  ARG A NE  
2527  C CZ  . ARG A 364  ? 0.2346 0.2526 0.2839 -0.0081 0.0112  0.0131  362  ARG A CZ  
2528  N NH1 . ARG A 364  ? 0.1985 0.2115 0.2439 -0.0076 0.0113  0.0136  362  ARG A NH1 
2529  N NH2 . ARG A 364  ? 0.2055 0.2270 0.2565 -0.0061 0.0109  0.0128  362  ARG A NH2 
2530  N N   . ARG A 365  ? 0.2360 0.2452 0.2937 -0.0233 0.0108  0.0131  363  ARG A N   
2531  C CA  . ARG A 365  ? 0.2461 0.2506 0.3039 -0.0253 0.0103  0.0132  363  ARG A CA  
2532  C C   . ARG A 365  ? 0.2448 0.2443 0.2978 -0.0235 0.0104  0.0130  363  ARG A C   
2533  O O   . ARG A 365  ? 0.2647 0.2625 0.3160 -0.0226 0.0088  0.0111  363  ARG A O   
2534  C CB  . ARG A 365  ? 0.2091 0.2139 0.2702 -0.0270 0.0081  0.0112  363  ARG A CB  
2535  C CG  . ARG A 365  ? 0.2198 0.2196 0.2817 -0.0291 0.0074  0.0113  363  ARG A CG  
2536  C CD  . ARG A 365  ? 0.2554 0.2564 0.3223 -0.0318 0.0057  0.0101  363  ARG A CD  
2537  N NE  . ARG A 365  ? 0.2860 0.2816 0.3540 -0.0337 0.0049  0.0103  363  ARG A NE  
2538  C CZ  . ARG A 365  ? 0.2442 0.2361 0.3116 -0.0334 0.0028  0.0078  363  ARG A CZ  
2539  N NH1 . ARG A 365  ? 0.2632 0.2567 0.3291 -0.0315 0.0014  0.0050  363  ARG A NH1 
2540  N NH2 . ARG A 365  ? 0.2852 0.2720 0.3537 -0.0349 0.0020  0.0081  363  ARG A NH2 
2541  N N   . ILE A 366  ? 0.2127 0.2104 0.2634 -0.0230 0.0122  0.0149  364  ILE A N   
2542  C CA  . ILE A 366  ? 0.2058 0.1995 0.2520 -0.0212 0.0124  0.0148  364  ILE A CA  
2543  C C   . ILE A 366  ? 0.2141 0.2031 0.2598 -0.0221 0.0111  0.0138  364  ILE A C   
2544  O O   . ILE A 366  ? 0.2098 0.1970 0.2578 -0.0243 0.0110  0.0145  364  ILE A O   
2545  C CB  . ILE A 366  ? 0.2086 0.2018 0.2529 -0.0205 0.0145  0.0169  364  ILE A CB  
2546  C CG1 . ILE A 366  ? 0.2214 0.2194 0.2663 -0.0192 0.0155  0.0173  364  ILE A CG1 
2547  C CG2 . ILE A 366  ? 0.2145 0.2032 0.2543 -0.0189 0.0146  0.0168  364  ILE A CG2 
2548  C CD1 . ILE A 366  ? 0.2140 0.2127 0.2576 -0.0186 0.0176  0.0191  364  ILE A CD1 
2549  N N   . MET A 367  ? 0.2071 0.1942 0.2498 -0.0205 0.0101  0.0122  365  MET A N   
2550  C CA  . MET A 367  ? 0.2089 0.1917 0.2507 -0.0208 0.0089  0.0109  365  MET A CA  
2551  C C   . MET A 367  ? 0.2231 0.2020 0.2622 -0.0203 0.0102  0.0125  365  MET A C   
2552  O O   . MET A 367  ? 0.2389 0.2178 0.2747 -0.0186 0.0112  0.0131  365  MET A O   
2553  C CB  . MET A 367  ? 0.2083 0.1917 0.2481 -0.0193 0.0074  0.0085  365  MET A CB  
2554  C CG  . MET A 367  ? 0.2315 0.2192 0.2737 -0.0195 0.0061  0.0070  365  MET A CG  
2555  S SD  . MET A 367  ? 0.2771 0.2663 0.3165 -0.0177 0.0044  0.0045  365  MET A SD  
2556  C CE  . MET A 367  ? 0.2733 0.2605 0.3148 -0.0189 0.0023  0.0014  365  MET A CE  
2557  N N   . VAL A 368  ? 0.2148 0.1905 0.2553 -0.0219 0.0101  0.0133  366  VAL A N   
2558  C CA  . VAL A 368  ? 0.2116 0.1840 0.2498 -0.0216 0.0113  0.0151  366  VAL A CA  
2559  C C   . VAL A 368  ? 0.2134 0.1813 0.2506 -0.0213 0.0098  0.0135  366  VAL A C   
2560  O O   . VAL A 368  ? 0.2374 0.2032 0.2775 -0.0229 0.0084  0.0128  366  VAL A O   
2561  C CB  . VAL A 368  ? 0.2131 0.1857 0.2535 -0.0236 0.0124  0.0178  366  VAL A CB  
2562  C CG1 . VAL A 368  ? 0.2279 0.1972 0.2654 -0.0230 0.0135  0.0196  366  VAL A CG1 
2563  C CG2 . VAL A 368  ? 0.2225 0.2004 0.2640 -0.0237 0.0139  0.0189  366  VAL A CG2 
2564  N N   . ARG A 369  ? 0.2121 0.1787 0.2456 -0.0193 0.0100  0.0128  367  ARG A N   
2565  C CA  . ARG A 369  ? 0.2197 0.1824 0.2521 -0.0186 0.0088  0.0112  367  ARG A CA  
2566  C C   . ARG A 369  ? 0.2149 0.1741 0.2463 -0.0189 0.0097  0.0135  367  ARG A C   
2567  O O   . ARG A 369  ? 0.2307 0.1902 0.2593 -0.0178 0.0112  0.0149  367  ARG A O   
2568  C CB  . ARG A 369  ? 0.2343 0.1979 0.2633 -0.0165 0.0085  0.0094  367  ARG A CB  
2569  C CG  . ARG A 369  ? 0.2536 0.2139 0.2818 -0.0157 0.0072  0.0074  367  ARG A CG  
2570  C CD  . ARG A 369  ? 0.2573 0.2185 0.2817 -0.0136 0.0075  0.0064  367  ARG A CD  
2571  N NE  . ARG A 369  ? 0.2598 0.2251 0.2837 -0.0130 0.0070  0.0049  367  ARG A NE  
2572  C CZ  . ARG A 369  ? 0.2773 0.2448 0.2982 -0.0117 0.0077  0.0051  367  ARG A CZ  
2573  N NH1 . ARG A 369  ? 0.2635 0.2295 0.2817 -0.0108 0.0088  0.0064  367  ARG A NH1 
2574  N NH2 . ARG A 369  ? 0.2305 0.2017 0.2510 -0.0113 0.0070  0.0040  367  ARG A NH2 
2575  N N   . LEU A 370  ? 0.2182 0.1739 0.2520 -0.0204 0.0086  0.0137  368  LEU A N   
2576  C CA  . LEU A 370  ? 0.2301 0.1822 0.2631 -0.0206 0.0091  0.0158  368  LEU A CA  
2577  C C   . LEU A 370  ? 0.2262 0.1751 0.2570 -0.0188 0.0080  0.0138  368  LEU A C   
2578  O O   . LEU A 370  ? 0.2236 0.1709 0.2560 -0.0186 0.0060  0.0112  368  LEU A O   
2579  C CB  . LEU A 370  ? 0.2395 0.1892 0.2763 -0.0232 0.0083  0.0174  368  LEU A CB  
2580  C CG  . LEU A 370  ? 0.2401 0.1861 0.2759 -0.0236 0.0087  0.0202  368  LEU A CG  
2581  C CD1 . LEU A 370  ? 0.2597 0.2088 0.2931 -0.0233 0.0113  0.0230  368  LEU A CD1 
2582  C CD2 . LEU A 370  ? 0.2304 0.1736 0.2705 -0.0263 0.0074  0.0218  368  LEU A CD2 
2583  N N   . VAL A 371  ? 0.2193 0.1675 0.2467 -0.0173 0.0092  0.0149  369  VAL A N   
2584  C CA  . VAL A 371  ? 0.2198 0.1654 0.2451 -0.0155 0.0084  0.0132  369  VAL A CA  
2585  C C   . VAL A 371  ? 0.2214 0.1638 0.2457 -0.0156 0.0090  0.0157  369  VAL A C   
2586  O O   . VAL A 371  ? 0.2436 0.1865 0.2680 -0.0168 0.0103  0.0187  369  VAL A O   
2587  C CB  . VAL A 371  ? 0.2164 0.1649 0.2384 -0.0135 0.0092  0.0118  369  VAL A CB  
2588  C CG1 . VAL A 371  ? 0.2236 0.1757 0.2463 -0.0136 0.0087  0.0100  369  VAL A CG1 
2589  C CG2 . VAL A 371  ? 0.2583 0.2080 0.2778 -0.0131 0.0112  0.0143  369  VAL A CG2 
2590  N N   . LYS A 372  ? 0.2260 0.1654 0.2491 -0.0142 0.0079  0.0145  370  LYS A N   
2591  C CA  . LYS A 372  ? 0.2240 0.1608 0.2455 -0.0139 0.0085  0.0168  370  LYS A CA  
2592  C C   . LYS A 372  ? 0.2333 0.1726 0.2510 -0.0124 0.0104  0.0174  370  LYS A C   
2593  O O   . LYS A 372  ? 0.2334 0.1740 0.2501 -0.0129 0.0120  0.0200  370  LYS A O   
2594  C CB  . LYS A 372  ? 0.2613 0.1937 0.2836 -0.0130 0.0065  0.0154  370  LYS A CB  
2595  C CG  . LYS A 372  ? 0.2395 0.1688 0.2659 -0.0149 0.0046  0.0154  370  LYS A CG  
2596  C CD  . LYS A 372  ? 0.2355 0.1596 0.2634 -0.0142 0.0023  0.0143  370  LYS A CD  
2597  C CE  . LYS A 372  ? 0.2995 0.2209 0.3321 -0.0163 0.0002  0.0141  370  LYS A CE  
2598  N NZ  . LYS A 372  ? 0.2936 0.2098 0.3283 -0.0153 -0.0026 0.0120  370  LYS A NZ  
2599  N N   . GLY A 373  ? 0.2198 0.1603 0.2356 -0.0106 0.0102  0.0151  371  GLY A N   
2600  C CA  . GLY A 373  ? 0.2155 0.1586 0.2283 -0.0095 0.0117  0.0155  371  GLY A CA  
2601  C C   . GLY A 373  ? 0.2235 0.1664 0.2342 -0.0076 0.0112  0.0135  371  GLY A C   
2602  O O   . GLY A 373  ? 0.2396 0.1798 0.2506 -0.0069 0.0101  0.0127  371  GLY A O   
2603  N N   . ALA A 374  ? 0.2360 0.1820 0.2447 -0.0068 0.0121  0.0129  372  ALA A N   
2604  C CA  . ALA A 374  ? 0.2452 0.1921 0.2522 -0.0053 0.0116  0.0108  372  ALA A CA  
2605  C C   . ALA A 374  ? 0.2614 0.2083 0.2658 -0.0043 0.0126  0.0118  372  ALA A C   
2606  O O   . ALA A 374  ? 0.2764 0.2242 0.2796 -0.0032 0.0123  0.0103  372  ALA A O   
2607  C CB  . ALA A 374  ? 0.2283 0.1789 0.2351 -0.0052 0.0116  0.0093  372  ALA A CB  
2608  N N   . TYR A 375  ? 0.2135 0.1598 0.2173 -0.0047 0.0138  0.0142  373  TYR A N   
2609  C CA  . TYR A 375  ? 0.2240 0.1708 0.2253 -0.0038 0.0147  0.0149  373  TYR A CA  
2610  C C   . TYR A 375  ? 0.2125 0.1568 0.2131 -0.0034 0.0147  0.0163  373  TYR A C   
2611  O O   . TYR A 375  ? 0.2481 0.1928 0.2469 -0.0030 0.0156  0.0174  373  TYR A O   
2612  C CB  . TYR A 375  ? 0.2488 0.1978 0.2494 -0.0041 0.0159  0.0162  373  TYR A CB  
2613  C CG  . TYR A 375  ? 0.2291 0.1806 0.2303 -0.0044 0.0158  0.0152  373  TYR A CG  
2614  C CD1 . TYR A 375  ? 0.2517 0.2038 0.2549 -0.0054 0.0155  0.0151  373  TYR A CD1 
2615  C CD2 . TYR A 375  ? 0.2572 0.2105 0.2569 -0.0038 0.0159  0.0146  373  TYR A CD2 
2616  C CE1 . TYR A 375  ? 0.2314 0.1861 0.2351 -0.0056 0.0153  0.0143  373  TYR A CE1 
2617  C CE2 . TYR A 375  ? 0.2792 0.2349 0.2794 -0.0041 0.0157  0.0141  373  TYR A CE2 
2618  C CZ  . TYR A 375  ? 0.2965 0.2529 0.2986 -0.0049 0.0154  0.0139  373  TYR A CZ  
2619  O OH  . TYR A 375  ? 0.3129 0.2718 0.3153 -0.0051 0.0150  0.0134  373  TYR A OH  
2620  N N   . TRP A 376  ? 0.2168 0.1584 0.2188 -0.0035 0.0135  0.0160  374  TRP A N   
2621  C CA  . TRP A 376  ? 0.2535 0.1924 0.2550 -0.0035 0.0135  0.0180  374  TRP A CA  
2622  C C   . TRP A 376  ? 0.2795 0.2186 0.2786 -0.0020 0.0138  0.0180  374  TRP A C   
2623  O O   . TRP A 376  ? 0.2560 0.1953 0.2536 -0.0020 0.0147  0.0199  374  TRP A O   
2624  C CB  . TRP A 376  ? 0.2385 0.1740 0.2421 -0.0037 0.0118  0.0177  374  TRP A CB  
2625  C CG  . TRP A 376  ? 0.2688 0.2015 0.2721 -0.0039 0.0116  0.0202  374  TRP A CG  
2626  C CD1 . TRP A 376  ? 0.2633 0.1956 0.2673 -0.0055 0.0122  0.0231  374  TRP A CD1 
2627  C CD2 . TRP A 376  ? 0.2882 0.2189 0.2904 -0.0025 0.0108  0.0203  374  TRP A CD2 
2628  N NE1 . TRP A 376  ? 0.2352 0.1651 0.2383 -0.0052 0.0118  0.0252  374  TRP A NE1 
2629  C CE2 . TRP A 376  ? 0.2798 0.2084 0.2818 -0.0033 0.0108  0.0235  374  TRP A CE2 
2630  C CE3 . TRP A 376  ? 0.3209 0.2515 0.3223 -0.0006 0.0099  0.0181  374  TRP A CE3 
2631  C CZ2 . TRP A 376  ? 0.2595 0.1858 0.2605 -0.0023 0.0100  0.0246  374  TRP A CZ2 
2632  C CZ3 . TRP A 376  ? 0.3284 0.2567 0.3289 0.0005  0.0091  0.0189  374  TRP A CZ3 
2633  C CH2 . TRP A 376  ? 0.3317 0.2577 0.3320 -0.0003 0.0091  0.0222  374  TRP A CH2 
2634  N N   . ASP A 377  ? 0.2604 0.1999 0.2591 -0.0008 0.0130  0.0158  375  ASP A N   
2635  C CA  . ASP A 377  ? 0.3103 0.2502 0.3069 0.0005  0.0131  0.0156  375  ASP A CA  
2636  C C   . ASP A 377  ? 0.2766 0.2189 0.2714 0.0004  0.0146  0.0165  375  ASP A C   
2637  O O   . ASP A 377  ? 0.2732 0.2153 0.2664 0.0010  0.0150  0.0176  375  ASP A O   
2638  C CB  . ASP A 377  ? 0.3340 0.2753 0.3307 0.0017  0.0123  0.0128  375  ASP A CB  
2639  C CG  . ASP A 377  ? 0.4776 0.4165 0.4759 0.0025  0.0106  0.0115  375  ASP A CG  
2640  O OD1 . ASP A 377  ? 0.5294 0.4653 0.5278 0.0028  0.0100  0.0128  375  ASP A OD1 
2641  O OD2 . ASP A 377  ? 0.5647 0.5047 0.5641 0.0029  0.0098  0.0090  375  ASP A OD2 
2642  N N   . ALA A 378  ? 0.2717 0.2162 0.2669 -0.0003 0.0152  0.0161  376  ALA A N   
2643  C CA  . ALA A 378  ? 0.2677 0.2141 0.2615 -0.0003 0.0163  0.0167  376  ALA A CA  
2644  C C   . ALA A 378  ? 0.2482 0.1942 0.2415 -0.0007 0.0172  0.0187  376  ALA A C   
2645  O O   . ALA A 378  ? 0.2500 0.1969 0.2418 -0.0002 0.0179  0.0192  376  ALA A O   
2646  C CB  . ALA A 378  ? 0.2440 0.1926 0.2385 -0.0008 0.0166  0.0159  376  ALA A CB  
2647  N N   . GLU A 379  ? 0.2277 0.1727 0.2224 -0.0017 0.0173  0.0198  377  GLU A N   
2648  C CA  . GLU A 379  ? 0.2256 0.1712 0.2200 -0.0022 0.0183  0.0219  377  GLU A CA  
2649  C C   . GLU A 379  ? 0.2499 0.1942 0.2427 -0.0015 0.0182  0.0231  377  GLU A C   
2650  O O   . GLU A 379  ? 0.2530 0.1987 0.2443 -0.0012 0.0191  0.0242  377  GLU A O   
2651  C CB  . GLU A 379  ? 0.2703 0.2155 0.2669 -0.0037 0.0183  0.0230  377  GLU A CB  
2652  C CG  . GLU A 379  ? 0.2411 0.1879 0.2394 -0.0043 0.0182  0.0218  377  GLU A CG  
2653  C CD  . GLU A 379  ? 0.2291 0.1787 0.2269 -0.0041 0.0193  0.0218  377  GLU A CD  
2654  O OE1 . GLU A 379  ? 0.2643 0.2148 0.2605 -0.0035 0.0202  0.0225  377  GLU A OE1 
2655  O OE2 . GLU A 379  ? 0.2291 0.1800 0.2282 -0.0046 0.0192  0.0210  377  GLU A OE2 
2656  N N   . ILE A 380  ? 0.2185 0.1603 0.2116 -0.0011 0.0170  0.0229  378  ILE A N   
2657  C CA  . ILE A 380  ? 0.2337 0.1742 0.2252 -0.0004 0.0167  0.0242  378  ILE A CA  
2658  C C   . ILE A 380  ? 0.2409 0.1832 0.2303 0.0009  0.0172  0.0232  378  ILE A C   
2659  O O   . ILE A 380  ? 0.2601 0.2033 0.2477 0.0013  0.0178  0.0244  378  ILE A O   
2660  C CB  . ILE A 380  ? 0.2194 0.1568 0.2119 0.0001  0.0151  0.0237  378  ILE A CB  
2661  C CG1 . ILE A 380  ? 0.2487 0.1839 0.2437 -0.0012 0.0144  0.0245  378  ILE A CG1 
2662  C CG2 . ILE A 380  ? 0.2568 0.1930 0.2476 0.0011  0.0146  0.0252  378  ILE A CG2 
2663  C CD1 . ILE A 380  ? 0.2756 0.2107 0.2708 -0.0027 0.0151  0.0277  378  ILE A CD1 
2664  N N   . LYS A 381  ? 0.2233 0.1663 0.2127 0.0015  0.0168  0.0210  379  LYS A N   
2665  C CA  . LYS A 381  ? 0.2571 0.2016 0.2449 0.0025  0.0170  0.0201  379  LYS A CA  
2666  C C   . LYS A 381  ? 0.2530 0.1995 0.2399 0.0023  0.0182  0.0206  379  LYS A C   
2667  O O   . LYS A 381  ? 0.2194 0.1668 0.2047 0.0031  0.0185  0.0207  379  LYS A O   
2668  C CB  . LYS A 381  ? 0.2191 0.1645 0.2075 0.0028  0.0165  0.0180  379  LYS A CB  
2669  C CG  . LYS A 381  ? 0.2451 0.1922 0.2323 0.0034  0.0167  0.0171  379  LYS A CG  
2670  C CD  . LYS A 381  ? 0.2516 0.2000 0.2395 0.0035  0.0161  0.0153  379  LYS A CD  
2671  C CE  . LYS A 381  ? 0.2681 0.2181 0.2550 0.0039  0.0161  0.0145  379  LYS A CE  
2672  N NZ  . LYS A 381  ? 0.2434 0.1953 0.2311 0.0038  0.0157  0.0131  379  LYS A NZ  
2673  N N   . ARG A 382  ? 0.2512 0.1987 0.2394 0.0014  0.0188  0.0206  380  ARG A N   
2674  C CA  . ARG A 382  ? 0.2494 0.1989 0.2372 0.0015  0.0197  0.0207  380  ARG A CA  
2675  C C   . ARG A 382  ? 0.2525 0.2028 0.2391 0.0017  0.0204  0.0222  380  ARG A C   
2676  O O   . ARG A 382  ? 0.2477 0.1995 0.2329 0.0025  0.0209  0.0218  380  ARG A O   
2677  C CB  . ARG A 382  ? 0.2578 0.2081 0.2474 0.0006  0.0200  0.0205  380  ARG A CB  
2678  C CG  . ARG A 382  ? 0.3327 0.2849 0.3221 0.0009  0.0206  0.0202  380  ARG A CG  
2679  C CD  . ARG A 382  ? 0.4928 0.4451 0.4819 0.0014  0.0201  0.0188  380  ARG A CD  
2680  N NE  . ARG A 382  ? 0.5152 0.4680 0.5029 0.0024  0.0202  0.0183  380  ARG A NE  
2681  C CZ  . ARG A 382  ? 0.5644 0.5169 0.5516 0.0028  0.0195  0.0173  380  ARG A CZ  
2682  N NH1 . ARG A 382  ? 0.5940 0.5463 0.5820 0.0023  0.0189  0.0168  380  ARG A NH1 
2683  N NH2 . ARG A 382  ? 0.4638 0.4168 0.4499 0.0037  0.0195  0.0167  380  ARG A NH2 
2684  N N   . ALA A 383  ? 0.2388 0.1883 0.2258 0.0009  0.0206  0.0239  381  ALA A N   
2685  C CA  . ALA A 383  ? 0.2276 0.1786 0.2135 0.0009  0.0214  0.0257  381  ALA A CA  
2686  C C   . ALA A 383  ? 0.2160 0.1668 0.1996 0.0021  0.0211  0.0259  381  ALA A C   
2687  O O   . ALA A 383  ? 0.2309 0.1839 0.2128 0.0027  0.0218  0.0264  381  ALA A O   
2688  C CB  . ALA A 383  ? 0.2284 0.1783 0.2156 -0.0005 0.0214  0.0279  381  ALA A CB  
2689  N N   . GLN A 384  ? 0.2173 0.1657 0.2008 0.0025  0.0199  0.0254  382  GLN A N   
2690  C CA  . GLN A 384  ? 0.2180 0.1664 0.1994 0.0038  0.0194  0.0253  382  GLN A CA  
2691  C C   . GLN A 384  ? 0.2364 0.1867 0.2167 0.0048  0.0196  0.0234  382  GLN A C   
2692  O O   . GLN A 384  ? 0.2703 0.2223 0.2488 0.0056  0.0199  0.0235  382  GLN A O   
2693  C CB  . GLN A 384  ? 0.2274 0.1732 0.2093 0.0042  0.0180  0.0249  382  GLN A CB  
2694  C CG  . GLN A 384  ? 0.2308 0.1740 0.2135 0.0035  0.0174  0.0270  382  GLN A CG  
2695  C CD  . GLN A 384  ? 0.2543 0.1949 0.2378 0.0043  0.0158  0.0262  382  GLN A CD  
2696  O OE1 . GLN A 384  ? 0.2829 0.2237 0.2667 0.0050  0.0153  0.0238  382  GLN A OE1 
2697  N NE2 . GLN A 384  ? 0.2677 0.2058 0.2515 0.0042  0.0149  0.0282  382  GLN A NE2 
2698  N N   . LEU A 385  ? 0.2305 0.1808 0.2122 0.0046  0.0194  0.0216  383  LEU A N   
2699  C CA  . LEU A 385  ? 0.2533 0.2050 0.2345 0.0053  0.0194  0.0199  383  LEU A CA  
2700  C C   . LEU A 385  ? 0.2785 0.2324 0.2589 0.0056  0.0203  0.0199  383  LEU A C   
2701  O O   . LEU A 385  ? 0.2626 0.2178 0.2418 0.0066  0.0202  0.0189  383  LEU A O   
2702  C CB  . LEU A 385  ? 0.2656 0.2169 0.2484 0.0047  0.0191  0.0185  383  LEU A CB  
2703  C CG  . LEU A 385  ? 0.2681 0.2184 0.2514 0.0047  0.0181  0.0176  383  LEU A CG  
2704  C CD1 . LEU A 385  ? 0.2953 0.2459 0.2801 0.0040  0.0180  0.0167  383  LEU A CD1 
2705  C CD2 . LEU A 385  ? 0.3049 0.2558 0.2870 0.0057  0.0176  0.0167  383  LEU A CD2 
2706  N N   . ASP A 386  ? 0.2489 0.2035 0.2303 0.0048  0.0212  0.0210  384  ASP A N   
2707  C CA  . ASP A 386  ? 0.2297 0.1869 0.2108 0.0052  0.0221  0.0207  384  ASP A CA  
2708  C C   . ASP A 386  ? 0.2580 0.2173 0.2373 0.0056  0.0228  0.0222  384  ASP A C   
2709  O O   . ASP A 386  ? 0.2454 0.2078 0.2244 0.0061  0.0236  0.0219  384  ASP A O   
2710  C CB  . ASP A 386  ? 0.2687 0.2264 0.2520 0.0042  0.0226  0.0210  384  ASP A CB  
2711  C CG  . ASP A 386  ? 0.3432 0.2997 0.3281 0.0040  0.0219  0.0195  384  ASP A CG  
2712  O OD1 . ASP A 386  ? 0.3790 0.3347 0.3633 0.0047  0.0212  0.0182  384  ASP A OD1 
2713  O OD2 . ASP A 386  ? 0.3156 0.2721 0.3022 0.0032  0.0221  0.0197  384  ASP A OD2 
2714  N N   . GLY A 387  ? 0.2400 0.1982 0.2181 0.0055  0.0224  0.0237  385  GLY A N   
2715  C CA  . GLY A 387  ? 0.2329 0.1932 0.2089 0.0058  0.0230  0.0255  385  GLY A CA  
2716  C C   . GLY A 387  ? 0.2496 0.2123 0.2262 0.0048  0.0243  0.0273  385  GLY A C   
2717  O O   . GLY A 387  ? 0.2756 0.2420 0.2507 0.0053  0.0252  0.0278  385  GLY A O   
2718  N N   . LEU A 388  ? 0.2438 0.2050 0.2228 0.0033  0.0244  0.0282  386  LEU A N   
2719  C CA  . LEU A 388  ? 0.2543 0.2180 0.2343 0.0022  0.0256  0.0297  386  LEU A CA  
2720  C C   . LEU A 388  ? 0.2815 0.2451 0.2610 0.0010  0.0258  0.0331  386  LEU A C   
2721  O O   . LEU A 388  ? 0.2756 0.2362 0.2543 0.0010  0.0248  0.0342  386  LEU A O   
2722  C CB  . LEU A 388  ? 0.2378 0.2004 0.2207 0.0012  0.0256  0.0289  386  LEU A CB  
2723  C CG  . LEU A 388  ? 0.2723 0.2353 0.2556 0.0024  0.0253  0.0259  386  LEU A CG  
2724  C CD1 . LEU A 388  ? 0.2432 0.2054 0.2292 0.0016  0.0251  0.0252  386  LEU A CD1 
2725  C CD2 . LEU A 388  ? 0.2970 0.2640 0.2792 0.0038  0.0261  0.0247  386  LEU A CD2 
2726  N N   . ALA A 389  ? 0.2703 0.2372 0.2504 -0.0001 0.0271  0.0349  387  ALA A N   
2727  C CA  . ALA A 389  ? 0.3032 0.2708 0.2824 -0.0014 0.0274  0.0385  387  ALA A CA  
2728  C C   . ALA A 389  ? 0.3002 0.2629 0.2812 -0.0029 0.0261  0.0403  387  ALA A C   
2729  O O   . ALA A 389  ? 0.3039 0.2650 0.2838 -0.0033 0.0255  0.0430  387  ALA A O   
2730  C CB  . ALA A 389  ? 0.2859 0.2587 0.2660 -0.0025 0.0291  0.0400  387  ALA A CB  
2731  N N   . ASP A 390  ? 0.2771 0.2371 0.2608 -0.0035 0.0255  0.0389  388  ASP A N   
2732  C CA  . ASP A 390  ? 0.2750 0.2306 0.2608 -0.0049 0.0243  0.0402  388  ASP A CA  
2733  C C   . ASP A 390  ? 0.2569 0.2106 0.2449 -0.0048 0.0237  0.0373  388  ASP A C   
2734  O O   . ASP A 390  ? 0.2637 0.2193 0.2514 -0.0037 0.0242  0.0349  388  ASP A O   
2735  C CB  . ASP A 390  ? 0.2672 0.2240 0.2546 -0.0072 0.0249  0.0435  388  ASP A CB  
2736  C CG  . ASP A 390  ? 0.3399 0.2918 0.3286 -0.0085 0.0233  0.0458  388  ASP A CG  
2737  O OD1 . ASP A 390  ? 0.3115 0.2590 0.3013 -0.0079 0.0217  0.0440  388  ASP A OD1 
2738  O OD2 . ASP A 390  ? 0.3597 0.3122 0.3484 -0.0101 0.0235  0.0495  388  ASP A OD2 
2739  N N   . PHE A 391  ? 0.2524 0.2023 0.2424 -0.0057 0.0224  0.0376  389  PHE A N   
2740  C CA  . PHE A 391  ? 0.2601 0.2085 0.2521 -0.0057 0.0218  0.0350  389  PHE A CA  
2741  C C   . PHE A 391  ? 0.2606 0.2110 0.2551 -0.0073 0.0225  0.0354  389  PHE A C   
2742  O O   . PHE A 391  ? 0.2639 0.2157 0.2593 -0.0089 0.0231  0.0380  389  PHE A O   
2743  C CB  . PHE A 391  ? 0.2556 0.1994 0.2489 -0.0058 0.0199  0.0346  389  PHE A CB  
2744  C CG  . PHE A 391  ? 0.2479 0.1899 0.2390 -0.0041 0.0190  0.0342  389  PHE A CG  
2745  C CD1 . PHE A 391  ? 0.2362 0.1785 0.2261 -0.0025 0.0189  0.0315  389  PHE A CD1 
2746  C CD2 . PHE A 391  ? 0.2590 0.1991 0.2493 -0.0043 0.0184  0.0368  389  PHE A CD2 
2747  C CE1 . PHE A 391  ? 0.2722 0.2133 0.2602 -0.0010 0.0181  0.0311  389  PHE A CE1 
2748  C CE2 . PHE A 391  ? 0.2456 0.1843 0.2339 -0.0026 0.0175  0.0364  389  PHE A CE2 
2749  C CZ  . PHE A 391  ? 0.2539 0.1932 0.2411 -0.0010 0.0174  0.0334  389  PHE A CZ  
2750  N N   . PRO A 392  ? 0.2530 0.2041 0.2487 -0.0070 0.0225  0.0329  390  PRO A N   
2751  C CA  . PRO A 392  ? 0.2499 0.2027 0.2483 -0.0084 0.0229  0.0329  390  PRO A CA  
2752  C C   . PRO A 392  ? 0.2315 0.1811 0.2325 -0.0097 0.0214  0.0327  390  PRO A C   
2753  O O   . PRO A 392  ? 0.2432 0.1941 0.2467 -0.0109 0.0215  0.0325  390  PRO A O   
2754  C CB  . PRO A 392  ? 0.2144 0.1693 0.2126 -0.0071 0.0232  0.0304  390  PRO A CB  
2755  C CG  . PRO A 392  ? 0.2273 0.1794 0.2237 -0.0057 0.0222  0.0286  390  PRO A CG  
2756  C CD  . PRO A 392  ? 0.2197 0.1703 0.2142 -0.0053 0.0220  0.0302  390  PRO A CD  
2757  N N   . VAL A 393  ? 0.2465 0.1922 0.2471 -0.0093 0.0200  0.0326  391  VAL A N   
2758  C CA  . VAL A 393  ? 0.2261 0.1683 0.2292 -0.0102 0.0184  0.0322  391  VAL A CA  
2759  C C   . VAL A 393  ? 0.2612 0.2002 0.2643 -0.0107 0.0175  0.0345  391  VAL A C   
2760  O O   . VAL A 393  ? 0.2461 0.1852 0.2467 -0.0099 0.0179  0.0359  391  VAL A O   
2761  C CB  . VAL A 393  ? 0.2463 0.1870 0.2494 -0.0088 0.0172  0.0289  391  VAL A CB  
2762  C CG1 . VAL A 393  ? 0.2449 0.1885 0.2485 -0.0086 0.0178  0.0269  391  VAL A CG1 
2763  C CG2 . VAL A 393  ? 0.2249 0.1647 0.2253 -0.0069 0.0170  0.0282  391  VAL A CG2 
2764  N N   . PHE A 394  ? 0.2405 0.1763 0.2464 -0.0120 0.0160  0.0349  392  PHE A N   
2765  C CA  . PHE A 394  ? 0.2499 0.1817 0.2562 -0.0124 0.0146  0.0370  392  PHE A CA  
2766  C C   . PHE A 394  ? 0.2593 0.1884 0.2640 -0.0101 0.0133  0.0349  392  PHE A C   
2767  O O   . PHE A 394  ? 0.2690 0.1990 0.2731 -0.0086 0.0133  0.0318  392  PHE A O   
2768  C CB  . PHE A 394  ? 0.2547 0.1835 0.2649 -0.0144 0.0130  0.0375  392  PHE A CB  
2769  C CG  . PHE A 394  ? 0.2366 0.1684 0.2487 -0.0168 0.0143  0.0396  392  PHE A CG  
2770  C CD1 . PHE A 394  ? 0.2671 0.2011 0.2783 -0.0181 0.0156  0.0434  392  PHE A CD1 
2771  C CD2 . PHE A 394  ? 0.2588 0.1922 0.2733 -0.0176 0.0143  0.0376  392  PHE A CD2 
2772  C CE1 . PHE A 394  ? 0.2447 0.1824 0.2576 -0.0203 0.0169  0.0452  392  PHE A CE1 
2773  C CE2 . PHE A 394  ? 0.2625 0.1994 0.2789 -0.0197 0.0155  0.0393  392  PHE A CE2 
2774  C CZ  . PHE A 394  ? 0.2499 0.1889 0.2656 -0.0211 0.0169  0.0431  392  PHE A CZ  
2775  N N   . THR A 395  ? 0.2777 0.2038 0.2817 -0.0098 0.0123  0.0369  393  THR A N   
2776  C CA  . THR A 395  ? 0.2684 0.1922 0.2712 -0.0075 0.0110  0.0351  393  THR A CA  
2777  C C   . THR A 395  ? 0.2705 0.1890 0.2759 -0.0075 0.0084  0.0347  393  THR A C   
2778  O O   . THR A 395  ? 0.2830 0.1997 0.2878 -0.0054 0.0071  0.0326  393  THR A O   
2779  C CB  . THR A 395  ? 0.2836 0.2082 0.2830 -0.0065 0.0117  0.0371  393  THR A CB  
2780  O OG1 . THR A 395  ? 0.2848 0.2077 0.2846 -0.0080 0.0113  0.0412  393  THR A OG1 
2781  C CG2 . THR A 395  ? 0.2976 0.2273 0.2945 -0.0062 0.0140  0.0369  393  THR A CG2 
2782  N N   . ARG A 396  ? 0.2814 0.1975 0.2897 -0.0096 0.0075  0.0365  394  ARG A N   
2783  C CA  . ARG A 396  ? 0.3268 0.2377 0.3383 -0.0096 0.0047  0.0355  394  ARG A CA  
2784  C C   . ARG A 396  ? 0.3183 0.2296 0.3328 -0.0106 0.0043  0.0328  394  ARG A C   
2785  O O   . ARG A 396  ? 0.3304 0.2441 0.3459 -0.0127 0.0055  0.0342  394  ARG A O   
2786  C CB  . ARG A 396  ? 0.3234 0.2306 0.3365 -0.0114 0.0035  0.0398  394  ARG A CB  
2787  C CG  . ARG A 396  ? 0.3622 0.2684 0.3724 -0.0103 0.0034  0.0425  394  ARG A CG  
2788  C CD  . ARG A 396  ? 0.3618 0.2637 0.3738 -0.0121 0.0019  0.0469  394  ARG A CD  
2789  N NE  . ARG A 396  ? 0.4403 0.3425 0.4491 -0.0113 0.0022  0.0501  394  ARG A NE  
2790  C CZ  . ARG A 396  ? 0.5627 0.4601 0.5719 -0.0104 -0.0002 0.0517  394  ARG A CZ  
2791  N NH1 . ARG A 396  ? 0.6368 0.5284 0.6496 -0.0103 -0.0031 0.0505  394  ARG A NH1 
2792  N NH2 . ARG A 396  ? 0.4795 0.3779 0.4853 -0.0096 0.0003  0.0545  394  ARG A NH2 
2793  N N   . LYS A 397  ? 0.2803 0.1896 0.2963 -0.0090 0.0025  0.0290  395  LYS A N   
2794  C CA  . LYS A 397  ? 0.2805 0.1906 0.2991 -0.0096 0.0019  0.0260  395  LYS A CA  
2795  C C   . LYS A 397  ? 0.2775 0.1852 0.2998 -0.0125 0.0009  0.0281  395  LYS A C   
2796  O O   . LYS A 397  ? 0.2794 0.1896 0.3033 -0.0140 0.0017  0.0274  395  LYS A O   
2797  C CB  . LYS A 397  ? 0.3420 0.2501 0.3617 -0.0074 -0.0003 0.0216  395  LYS A CB  
2798  C CG  . LYS A 397  ? 0.3356 0.2462 0.3569 -0.0073 -0.0005 0.0177  395  LYS A CG  
2799  C CD  . LYS A 397  ? 0.3306 0.2376 0.3562 -0.0087 -0.0028 0.0169  395  LYS A CD  
2800  C CE  . LYS A 397  ? 0.3192 0.2289 0.3461 -0.0084 -0.0032 0.0126  395  LYS A CE  
2801  N NZ  . LYS A 397  ? 0.2867 0.1929 0.3182 -0.0098 -0.0057 0.0116  395  LYS A NZ  
2802  N N   . ILE A 398  ? 0.2656 0.1685 0.2895 -0.0133 -0.0007 0.0309  396  ILE A N   
2803  C CA  . ILE A 398  ? 0.2998 0.2001 0.3276 -0.0162 -0.0019 0.0332  396  ILE A CA  
2804  C C   . ILE A 398  ? 0.2569 0.1617 0.2841 -0.0188 0.0008  0.0365  396  ILE A C   
2805  O O   . ILE A 398  ? 0.2928 0.1978 0.3231 -0.0212 0.0005  0.0372  396  ILE A O   
2806  C CB  . ILE A 398  ? 0.2806 0.1747 0.3100 -0.0166 -0.0043 0.0360  396  ILE A CB  
2807  C CG1 . ILE A 398  ? 0.4008 0.2910 0.4351 -0.0195 -0.0062 0.0374  396  ILE A CG1 
2808  C CG2 . ILE A 398  ? 0.3229 0.2182 0.3491 -0.0170 -0.0026 0.0408  396  ILE A CG2 
2809  C CD1 . ILE A 398  ? 0.4435 0.3264 0.4806 -0.0190 -0.0098 0.0378  396  ILE A CD1 
2810  N N   . HIS A 399  ? 0.2986 0.2073 0.3218 -0.0181 0.0032  0.0383  397  HIS A N   
2811  C CA  . HIS A 399  ? 0.2906 0.2042 0.3131 -0.0201 0.0058  0.0410  397  HIS A CA  
2812  C C   . HIS A 399  ? 0.2816 0.1993 0.3050 -0.0202 0.0068  0.0379  397  HIS A C   
2813  O O   . HIS A 399  ? 0.2699 0.1898 0.2955 -0.0225 0.0076  0.0392  397  HIS A O   
2814  C CB  . HIS A 399  ? 0.3049 0.2219 0.3229 -0.0189 0.0080  0.0429  397  HIS A CB  
2815  C CG  . HIS A 399  ? 0.3060 0.2201 0.3229 -0.0191 0.0073  0.0467  397  HIS A CG  
2816  N ND1 . HIS A 399  ? 0.2921 0.2084 0.3050 -0.0177 0.0087  0.0482  397  HIS A ND1 
2817  C CD2 . HIS A 399  ? 0.3424 0.2515 0.3619 -0.0207 0.0052  0.0495  397  HIS A CD2 
2818  C CE1 . HIS A 399  ? 0.3074 0.2205 0.3202 -0.0183 0.0075  0.0518  397  HIS A CE1 
2819  N NE2 . HIS A 399  ? 0.3098 0.2183 0.3266 -0.0201 0.0054  0.0528  397  HIS A NE2 
2820  N N   . THR A 400  ? 0.2693 0.1880 0.2911 -0.0178 0.0068  0.0339  398  THR A N   
2821  C CA  . THR A 400  ? 0.2703 0.1924 0.2930 -0.0177 0.0073  0.0309  398  THR A CA  
2822  C C   . THR A 400  ? 0.2742 0.1941 0.3013 -0.0195 0.0054  0.0297  398  THR A C   
2823  O O   . THR A 400  ? 0.2537 0.1767 0.2825 -0.0209 0.0062  0.0294  398  THR A O   
2824  C CB  . THR A 400  ? 0.2428 0.1659 0.2632 -0.0149 0.0072  0.0271  398  THR A CB  
2825  O OG1 . THR A 400  ? 0.2359 0.1614 0.2524 -0.0137 0.0092  0.0282  398  THR A OG1 
2826  C CG2 . THR A 400  ? 0.2394 0.1656 0.2607 -0.0149 0.0075  0.0240  398  THR A CG2 
2827  N N   . ASP A 401  ? 0.2740 0.1886 0.3034 -0.0193 0.0028  0.0290  399  ASP A N   
2828  C CA  . ASP A 401  ? 0.2499 0.1620 0.2838 -0.0210 0.0007  0.0277  399  ASP A CA  
2829  C C   . ASP A 401  ? 0.2739 0.1866 0.3105 -0.0245 0.0013  0.0317  399  ASP A C   
2830  O O   . ASP A 401  ? 0.2834 0.1977 0.3230 -0.0262 0.0010  0.0307  399  ASP A O   
2831  C CB  . ASP A 401  ? 0.2547 0.1605 0.2907 -0.0201 -0.0024 0.0262  399  ASP A CB  
2832  C CG  . ASP A 401  ? 0.3142 0.2201 0.3486 -0.0168 -0.0033 0.0215  399  ASP A CG  
2833  O OD1 . ASP A 401  ? 0.3349 0.2454 0.3676 -0.0157 -0.0020 0.0188  399  ASP A OD1 
2834  O OD2 . ASP A 401  ? 0.3405 0.2421 0.3753 -0.0152 -0.0053 0.0205  399  ASP A OD2 
2835  N N   . VAL A 402  ? 0.2591 0.1708 0.2947 -0.0256 0.0020  0.0362  400  VAL A N   
2836  C CA  . VAL A 402  ? 0.2570 0.1701 0.2949 -0.0290 0.0028  0.0403  400  VAL A CA  
2837  C C   . VAL A 402  ? 0.2733 0.1934 0.3101 -0.0296 0.0056  0.0403  400  VAL A C   
2838  O O   . VAL A 402  ? 0.2769 0.1993 0.3169 -0.0320 0.0058  0.0410  400  VAL A O   
2839  C CB  . VAL A 402  ? 0.3001 0.2115 0.3365 -0.0299 0.0033  0.0454  400  VAL A CB  
2840  C CG1 . VAL A 402  ? 0.2758 0.1902 0.3142 -0.0335 0.0046  0.0498  400  VAL A CG1 
2841  C CG2 . VAL A 402  ? 0.3189 0.2228 0.3572 -0.0296 0.0001  0.0456  400  VAL A CG2 
2842  N N   . SER A 403  ? 0.2557 0.1794 0.2882 -0.0273 0.0077  0.0395  401  SER A N   
2843  C CA  . SER A 403  ? 0.2677 0.1979 0.2992 -0.0274 0.0101  0.0390  401  SER A CA  
2844  C C   . SER A 403  ? 0.2999 0.2314 0.3341 -0.0276 0.0093  0.0356  401  SER A C   
2845  O O   . SER A 403  ? 0.2433 0.1787 0.2796 -0.0294 0.0102  0.0363  401  SER A O   
2846  C CB  . SER A 403  ? 0.2390 0.1717 0.2658 -0.0245 0.0118  0.0379  401  SER A CB  
2847  O OG  . SER A 403  ? 0.2540 0.1923 0.2800 -0.0242 0.0137  0.0369  401  SER A OG  
2848  N N   . TYR A 404  ? 0.2466 0.1752 0.2809 -0.0258 0.0074  0.0318  402  TYR A N   
2849  C CA  . TYR A 404  ? 0.2659 0.1960 0.3025 -0.0259 0.0065  0.0283  402  TYR A CA  
2850  C C   . TYR A 404  ? 0.2499 0.1791 0.2914 -0.0290 0.0052  0.0293  402  TYR A C   
2851  O O   . TYR A 404  ? 0.2407 0.1739 0.2840 -0.0301 0.0058  0.0287  402  TYR A O   
2852  C CB  . TYR A 404  ? 0.2589 0.1860 0.2948 -0.0235 0.0045  0.0243  402  TYR A CB  
2853  C CG  . TYR A 404  ? 0.2405 0.1701 0.2775 -0.0229 0.0038  0.0203  402  TYR A CG  
2854  C CD1 . TYR A 404  ? 0.2646 0.1929 0.3058 -0.0245 0.0018  0.0187  402  TYR A CD1 
2855  C CD2 . TYR A 404  ? 0.2428 0.1760 0.2765 -0.0207 0.0050  0.0182  402  TYR A CD2 
2856  C CE1 . TYR A 404  ? 0.2854 0.2165 0.3274 -0.0238 0.0011  0.0150  402  TYR A CE1 
2857  C CE2 . TYR A 404  ? 0.2340 0.1698 0.2685 -0.0201 0.0042  0.0148  402  TYR A CE2 
2858  C CZ  . TYR A 404  ? 0.2422 0.1771 0.2808 -0.0216 0.0023  0.0132  402  TYR A CZ  
2859  O OH  . TYR A 404  ? 0.2829 0.2208 0.3221 -0.0210 0.0015  0.0098  402  TYR A OH  
2860  N N   . ILE A 405  ? 0.2523 0.1762 0.2962 -0.0304 0.0033  0.0310  403  ILE A N   
2861  C CA  . ILE A 405  ? 0.2515 0.1740 0.3006 -0.0335 0.0018  0.0320  403  ILE A CA  
2862  C C   . ILE A 405  ? 0.2586 0.1857 0.3086 -0.0362 0.0040  0.0360  403  ILE A C   
2863  O O   . ILE A 405  ? 0.2511 0.1809 0.3047 -0.0383 0.0038  0.0357  403  ILE A O   
2864  C CB  . ILE A 405  ? 0.2577 0.1729 0.3091 -0.0343 -0.0010 0.0331  403  ILE A CB  
2865  C CG1 . ILE A 405  ? 0.2990 0.2105 0.3501 -0.0314 -0.0033 0.0282  403  ILE A CG1 
2866  C CG2 . ILE A 405  ? 0.3166 0.2300 0.3736 -0.0379 -0.0026 0.0347  403  ILE A CG2 
2867  C CD1 . ILE A 405  ? 0.3452 0.2493 0.3979 -0.0312 -0.0061 0.0289  403  ILE A CD1 
2868  N N   . ALA A 406  ? 0.2574 0.1863 0.3042 -0.0360 0.0061  0.0395  404  ALA A N   
2869  C CA  . ALA A 406  ? 0.2836 0.2180 0.3309 -0.0383 0.0085  0.0431  404  ALA A CA  
2870  C C   . ALA A 406  ? 0.2702 0.2110 0.3173 -0.0376 0.0102  0.0407  404  ALA A C   
2871  O O   . ALA A 406  ? 0.2726 0.2176 0.3226 -0.0399 0.0110  0.0420  404  ALA A O   
2872  C CB  . ALA A 406  ? 0.2851 0.2206 0.3283 -0.0375 0.0105  0.0465  404  ALA A CB  
2873  N N   . CYS A 407  ? 0.2684 0.2102 0.3121 -0.0344 0.0106  0.0374  405  CYS A N   
2874  C CA  . CYS A 407  ? 0.2401 0.1876 0.2834 -0.0335 0.0120  0.0354  405  CYS A CA  
2875  C C   . CYS A 407  ? 0.2670 0.2146 0.3140 -0.0344 0.0102  0.0325  405  CYS A C   
2876  O O   . CYS A 407  ? 0.2681 0.2207 0.3166 -0.0350 0.0111  0.0319  405  CYS A O   
2877  C CB  . CYS A 407  ? 0.2345 0.1828 0.2732 -0.0301 0.0129  0.0331  405  CYS A CB  
2878  S SG  . CYS A 407  ? 0.3097 0.2595 0.3440 -0.0290 0.0153  0.0361  405  CYS A SG  
2879  N N   . ALA A 408  ? 0.2389 0.1812 0.2877 -0.0344 0.0076  0.0304  406  ALA A N   
2880  C CA  . ALA A 408  ? 0.2398 0.1821 0.2926 -0.0355 0.0056  0.0277  406  ALA A CA  
2881  C C   . ALA A 408  ? 0.2425 0.1865 0.2999 -0.0392 0.0055  0.0303  406  ALA A C   
2882  O O   . ALA A 408  ? 0.2718 0.2193 0.3320 -0.0402 0.0053  0.0288  406  ALA A O   
2883  C CB  . ALA A 408  ? 0.2756 0.2117 0.3294 -0.0346 0.0026  0.0249  406  ALA A CB  
2884  N N   . ALA A 409  ? 0.2674 0.2092 0.3259 -0.0413 0.0058  0.0345  407  ALA A N   
2885  C CA  . ALA A 409  ? 0.3116 0.2554 0.3744 -0.0452 0.0060  0.0376  407  ALA A CA  
2886  C C   . ALA A 409  ? 0.3170 0.2689 0.3795 -0.0455 0.0087  0.0385  407  ALA A C   
2887  O O   . ALA A 409  ? 0.2648 0.2202 0.3313 -0.0478 0.0086  0.0386  407  ALA A O   
2888  C CB  . ALA A 409  ? 0.3037 0.2442 0.3669 -0.0472 0.0060  0.0424  407  ALA A CB  
2889  N N   . LYS A 410  ? 0.2586 0.2137 0.3164 -0.0431 0.0111  0.0390  408  LYS A N   
2890  C CA  . LYS A 410  ? 0.2782 0.2409 0.3355 -0.0429 0.0136  0.0394  408  LYS A CA  
2891  C C   . LYS A 410  ? 0.2852 0.2507 0.3439 -0.0418 0.0128  0.0354  408  LYS A C   
2892  O O   . LYS A 410  ? 0.2542 0.2251 0.3157 -0.0431 0.0135  0.0355  408  LYS A O   
2893  C CB  . LYS A 410  ? 0.2630 0.2277 0.3151 -0.0402 0.0158  0.0401  408  LYS A CB  
2894  C CG  . LYS A 410  ? 0.2951 0.2676 0.3467 -0.0396 0.0183  0.0403  408  LYS A CG  
2895  C CD  . LYS A 410  ? 0.3189 0.2926 0.3654 -0.0368 0.0202  0.0406  408  LYS A CD  
2896  C CE  . LYS A 410  ? 0.2896 0.2613 0.3343 -0.0378 0.0209  0.0443  408  LYS A CE  
2897  N NZ  . LYS A 410  ? 0.3100 0.2873 0.3570 -0.0405 0.0226  0.0479  408  LYS A NZ  
2898  N N   . LEU A 411  ? 0.2477 0.2098 0.3042 -0.0392 0.0114  0.0319  409  LEU A N   
2899  C CA  . LEU A 411  ? 0.2304 0.1950 0.2877 -0.0380 0.0105  0.0281  409  LEU A CA  
2900  C C   . LEU A 411  ? 0.2483 0.2130 0.3110 -0.0406 0.0085  0.0271  409  LEU A C   
2901  O O   . LEU A 411  ? 0.2638 0.2332 0.3285 -0.0409 0.0086  0.0257  409  LEU A O   
2902  C CB  . LEU A 411  ? 0.2332 0.1942 0.2870 -0.0349 0.0094  0.0249  409  LEU A CB  
2903  C CG  . LEU A 411  ? 0.2612 0.2238 0.3099 -0.0320 0.0113  0.0249  409  LEU A CG  
2904  C CD1 . LEU A 411  ? 0.2609 0.2192 0.3066 -0.0296 0.0100  0.0224  409  LEU A CD1 
2905  C CD2 . LEU A 411  ? 0.2458 0.2142 0.2943 -0.0309 0.0123  0.0236  409  LEU A CD2 
2906  N N   . LEU A 412  ? 0.2447 0.2038 0.3098 -0.0424 0.0065  0.0275  410  LEU A N   
2907  C CA  . LEU A 412  ? 0.2918 0.2501 0.3623 -0.0449 0.0042  0.0262  410  LEU A CA  
2908  C C   . LEU A 412  ? 0.2881 0.2513 0.3627 -0.0482 0.0053  0.0291  410  LEU A C   
2909  O O   . LEU A 412  ? 0.3130 0.2779 0.3921 -0.0501 0.0038  0.0276  410  LEU A O   
2910  C CB  . LEU A 412  ? 0.2742 0.2250 0.3467 -0.0459 0.0016  0.0261  410  LEU A CB  
2911  C CG  . LEU A 412  ? 0.2804 0.2270 0.3503 -0.0428 -0.0002 0.0219  410  LEU A CG  
2912  C CD1 . LEU A 412  ? 0.3287 0.2677 0.4004 -0.0435 -0.0028 0.0219  410  LEU A CD1 
2913  C CD2 . LEU A 412  ? 0.3139 0.2634 0.3850 -0.0418 -0.0016 0.0174  410  LEU A CD2 
2914  N N   . ALA A 413  ? 0.2437 0.2096 0.3168 -0.0489 0.0078  0.0330  411  ALA A N   
2915  C CA  . ALA A 413  ? 0.2823 0.2544 0.3589 -0.0518 0.0093  0.0358  411  ALA A CA  
2916  C C   . ALA A 413  ? 0.3225 0.3020 0.3983 -0.0501 0.0110  0.0341  411  ALA A C   
2917  O O   . ALA A 413  ? 0.2614 0.2470 0.3402 -0.0521 0.0123  0.0359  411  ALA A O   
2918  C CB  . ALA A 413  ? 0.3130 0.2858 0.3883 -0.0533 0.0114  0.0407  411  ALA A CB  
2919  N N   . ALA A 414  ? 0.2804 0.2599 0.3526 -0.0465 0.0108  0.0307  412  ALA A N   
2920  C CA  . ALA A 414  ? 0.3042 0.2902 0.3753 -0.0445 0.0123  0.0293  412  ALA A CA  
2921  C C   . ALA A 414  ? 0.2680 0.2539 0.3391 -0.0427 0.0104  0.0250  412  ALA A C   
2922  O O   . ALA A 414  ? 0.2602 0.2493 0.3287 -0.0400 0.0112  0.0234  412  ALA A O   
2923  C CB  . ALA A 414  ? 0.2712 0.2584 0.3371 -0.0417 0.0146  0.0303  412  ALA A CB  
2924  N N   . THR A 415  ? 0.2763 0.2585 0.3503 -0.0440 0.0078  0.0230  413  THR A N   
2925  C CA  . THR A 415  ? 0.2666 0.2489 0.3403 -0.0422 0.0059  0.0189  413  THR A CA  
2926  C C   . THR A 415  ? 0.2746 0.2639 0.3506 -0.0422 0.0061  0.0178  413  THR A C   
2927  O O   . THR A 415  ? 0.2563 0.2471 0.3311 -0.0401 0.0050  0.0147  413  THR A O   
2928  C CB  . THR A 415  ? 0.3271 0.3044 0.4038 -0.0436 0.0028  0.0167  413  THR A CB  
2929  O OG1 . THR A 415  ? 0.3030 0.2814 0.3855 -0.0474 0.0020  0.0181  413  THR A OG1 
2930  C CG2 . THR A 415  ? 0.3057 0.2759 0.3799 -0.0430 0.0022  0.0172  413  THR A CG2 
2931  N N   . ASP A 416  ? 0.3087 0.3028 0.3881 -0.0445 0.0075  0.0202  414  ASP A N   
2932  C CA  . ASP A 416  ? 0.3529 0.3540 0.4344 -0.0441 0.0077  0.0190  414  ASP A CA  
2933  C C   . ASP A 416  ? 0.2984 0.3027 0.3755 -0.0406 0.0095  0.0187  414  ASP A C   
2934  O O   . ASP A 416  ? 0.3084 0.3167 0.3857 -0.0391 0.0090  0.0167  414  ASP A O   
2935  C CB  . ASP A 416  ? 0.3464 0.3524 0.4329 -0.0475 0.0087  0.0216  414  ASP A CB  
2936  C CG  . ASP A 416  ? 0.3940 0.4012 0.4792 -0.0482 0.0114  0.0255  414  ASP A CG  
2937  O OD1 . ASP A 416  ? 0.4178 0.4199 0.4990 -0.0472 0.0120  0.0266  414  ASP A OD1 
2938  O OD2 . ASP A 416  ? 0.5237 0.5373 0.6117 -0.0498 0.0130  0.0274  414  ASP A OD2 
2939  N N   . VAL A 417  ? 0.2657 0.2680 0.3387 -0.0392 0.0114  0.0206  415  VAL A N   
2940  C CA  . VAL A 417  ? 0.2801 0.2853 0.3495 -0.0360 0.0130  0.0204  415  VAL A CA  
2941  C C   . VAL A 417  ? 0.2323 0.2326 0.2963 -0.0331 0.0127  0.0192  415  VAL A C   
2942  O O   . VAL A 417  ? 0.2613 0.2636 0.3225 -0.0304 0.0133  0.0185  415  VAL A O   
2943  C CB  . VAL A 417  ? 0.3381 0.3471 0.4073 -0.0364 0.0157  0.0234  415  VAL A CB  
2944  C CG1 . VAL A 417  ? 0.3588 0.3741 0.4334 -0.0391 0.0161  0.0244  415  VAL A CG1 
2945  C CG2 . VAL A 417  ? 0.3014 0.3057 0.3685 -0.0374 0.0165  0.0259  415  VAL A CG2 
2946  N N   . VAL A 418  ? 0.2269 0.2212 0.2896 -0.0336 0.0116  0.0190  416  VAL A N   
2947  C CA  . VAL A 418  ? 0.2146 0.2048 0.2727 -0.0310 0.0111  0.0176  416  VAL A CA  
2948  C C   . VAL A 418  ? 0.2166 0.2028 0.2756 -0.0315 0.0086  0.0152  416  VAL A C   
2949  O O   . VAL A 418  ? 0.2331 0.2183 0.2960 -0.0340 0.0073  0.0150  416  VAL A O   
2950  C CB  . VAL A 418  ? 0.2320 0.2187 0.2866 -0.0303 0.0127  0.0197  416  VAL A CB  
2951  C CG1 . VAL A 418  ? 0.2514 0.2424 0.3048 -0.0294 0.0151  0.0216  416  VAL A CG1 
2952  C CG2 . VAL A 418  ? 0.2334 0.2163 0.2899 -0.0329 0.0124  0.0216  416  VAL A CG2 
2953  N N   . PHE A 419  ? 0.2177 0.2019 0.2731 -0.0291 0.0079  0.0132  417  PHE A N   
2954  C CA  . PHE A 419  ? 0.2227 0.2034 0.2782 -0.0290 0.0056  0.0104  417  PHE A CA  
2955  C C   . PHE A 419  ? 0.2232 0.1985 0.2756 -0.0281 0.0058  0.0109  417  PHE A C   
2956  O O   . PHE A 419  ? 0.2303 0.2052 0.2786 -0.0257 0.0065  0.0105  417  PHE A O   
2957  C CB  . PHE A 419  ? 0.2154 0.1989 0.2693 -0.0269 0.0046  0.0077  417  PHE A CB  
2958  C CG  . PHE A 419  ? 0.2397 0.2206 0.2933 -0.0264 0.0023  0.0045  417  PHE A CG  
2959  C CD1 . PHE A 419  ? 0.2446 0.2241 0.3022 -0.0284 0.0003  0.0029  417  PHE A CD1 
2960  C CD2 . PHE A 419  ? 0.2160 0.1962 0.2653 -0.0240 0.0021  0.0030  417  PHE A CD2 
2961  C CE1 . PHE A 419  ? 0.2300 0.2076 0.2875 -0.0277 -0.0019 -0.0004 417  PHE A CE1 
2962  C CE2 . PHE A 419  ? 0.2309 0.2096 0.2800 -0.0234 0.0001  -0.0001 417  PHE A CE2 
2963  C CZ  . PHE A 419  ? 0.2501 0.2274 0.3032 -0.0251 -0.0019 -0.0020 417  PHE A CZ  
2964  N N   . PRO A 420  ? 0.2214 0.1925 0.2758 -0.0299 0.0051  0.0118  418  PRO A N   
2965  C CA  . PRO A 420  ? 0.2224 0.1885 0.2740 -0.0289 0.0052  0.0122  418  PRO A CA  
2966  C C   . PRO A 420  ? 0.2473 0.2112 0.2973 -0.0271 0.0033  0.0086  418  PRO A C   
2967  O O   . PRO A 420  ? 0.2531 0.2174 0.3056 -0.0276 0.0013  0.0059  418  PRO A O   
2968  C CB  . PRO A 420  ? 0.2263 0.1888 0.2813 -0.0316 0.0046  0.0143  418  PRO A CB  
2969  C CG  . PRO A 420  ? 0.2265 0.1932 0.2853 -0.0341 0.0053  0.0160  418  PRO A CG  
2970  C CD  . PRO A 420  ? 0.2284 0.1995 0.2879 -0.0332 0.0045  0.0131  418  PRO A CD  
2971  N N   . GLN A 421  ? 0.2217 0.1836 0.2676 -0.0250 0.0040  0.0086  419  GLN A N   
2972  C CA  . GLN A 421  ? 0.2370 0.1976 0.2809 -0.0230 0.0026  0.0054  419  GLN A CA  
2973  C C   . GLN A 421  ? 0.2429 0.1985 0.2851 -0.0224 0.0026  0.0062  419  GLN A C   
2974  O O   . GLN A 421  ? 0.2446 0.1999 0.2835 -0.0213 0.0044  0.0081  419  GLN A O   
2975  C CB  . GLN A 421  ? 0.2228 0.1872 0.2630 -0.0209 0.0034  0.0045  419  GLN A CB  
2976  C CG  . GLN A 421  ? 0.2281 0.1974 0.2699 -0.0213 0.0034  0.0041  419  GLN A CG  
2977  C CD  . GLN A 421  ? 0.2474 0.2202 0.2857 -0.0194 0.0046  0.0046  419  GLN A CD  
2978  O OE1 . GLN A 421  ? 0.2213 0.1940 0.2576 -0.0189 0.0064  0.0069  419  GLN A OE1 
2979  N NE2 . GLN A 421  ? 0.2147 0.1905 0.2523 -0.0184 0.0034  0.0023  419  GLN A NE2 
2980  N N   . PHE A 422  ? 0.2270 0.1786 0.2715 -0.0230 0.0006  0.0046  420  PHE A N   
2981  C CA  . PHE A 422  ? 0.2305 0.1770 0.2742 -0.0226 0.0003  0.0056  420  PHE A CA  
2982  C C   . PHE A 422  ? 0.2480 0.1938 0.2888 -0.0199 -0.0005 0.0025  420  PHE A C   
2983  O O   . PHE A 422  ? 0.2472 0.1916 0.2896 -0.0194 -0.0027 -0.0009 420  PHE A O   
2984  C CB  . PHE A 422  ? 0.2446 0.1868 0.2928 -0.0248 -0.0016 0.0059  420  PHE A CB  
2985  C CG  . PHE A 422  ? 0.2560 0.1995 0.3072 -0.0278 -0.0007 0.0092  420  PHE A CG  
2986  C CD1 . PHE A 422  ? 0.2590 0.2029 0.3087 -0.0285 0.0016  0.0134  420  PHE A CD1 
2987  C CD2 . PHE A 422  ? 0.2432 0.1882 0.2987 -0.0297 -0.0020 0.0081  420  PHE A CD2 
2988  C CE1 . PHE A 422  ? 0.2530 0.1989 0.3053 -0.0311 0.0026  0.0164  420  PHE A CE1 
2989  C CE2 . PHE A 422  ? 0.2605 0.2074 0.3189 -0.0325 -0.0011 0.0112  420  PHE A CE2 
2990  C CZ  . PHE A 422  ? 0.2664 0.2139 0.3232 -0.0332 0.0013  0.0154  420  PHE A CZ  
2991  N N   . ALA A 423  ? 0.2259 0.1728 0.2626 -0.0183 0.0013  0.0036  421  ALA A N   
2992  C CA  . ALA A 423  ? 0.2251 0.1721 0.2588 -0.0158 0.0009  0.0012  421  ALA A CA  
2993  C C   . ALA A 423  ? 0.2831 0.2250 0.3168 -0.0153 0.0002  0.0015  421  ALA A C   
2994  O O   . ALA A 423  ? 0.2661 0.2064 0.2983 -0.0155 0.0016  0.0046  421  ALA A O   
2995  C CB  . ALA A 423  ? 0.2621 0.2127 0.2918 -0.0145 0.0030  0.0023  421  ALA A CB  
2996  N N   . THR A 424  ? 0.2720 0.2116 0.3073 -0.0144 -0.0021 -0.0018 422  THR A N   
2997  C CA  . THR A 424  ? 0.2523 0.1871 0.2876 -0.0135 -0.0031 -0.0018 422  THR A CA  
2998  C C   . THR A 424  ? 0.2872 0.2212 0.3238 -0.0118 -0.0056 -0.0066 422  THR A C   
2999  O O   . THR A 424  ? 0.2791 0.2144 0.3180 -0.0123 -0.0071 -0.0094 422  THR A O   
3000  C CB  . THR A 424  ? 0.2721 0.2020 0.3103 -0.0156 -0.0037 0.0013  422  THR A CB  
3001  O OG1 . THR A 424  ? 0.3140 0.2392 0.3518 -0.0144 -0.0047 0.0013  422  THR A OG1 
3002  C CG2 . THR A 424  ? 0.2905 0.2188 0.3336 -0.0175 -0.0059 -0.0002 422  THR A CG2 
3003  N N   . HIS A 425  ? 0.2524 0.1845 0.2872 -0.0098 -0.0060 -0.0077 423  HIS A N   
3004  C CA  . HIS A 425  ? 0.2960 0.2268 0.3323 -0.0079 -0.0085 -0.0122 423  HIS A CA  
3005  C C   . HIS A 425  ? 0.3350 0.2590 0.3744 -0.0082 -0.0106 -0.0118 423  HIS A C   
3006  O O   . HIS A 425  ? 0.3337 0.2558 0.3747 -0.0064 -0.0130 -0.0156 423  HIS A O   
3007  C CB  . HIS A 425  ? 0.2514 0.1854 0.2839 -0.0052 -0.0077 -0.0141 423  HIS A CB  
3008  C CG  . HIS A 425  ? 0.2979 0.2385 0.3274 -0.0049 -0.0059 -0.0146 423  HIS A CG  
3009  N ND1 . HIS A 425  ? 0.3330 0.2766 0.3587 -0.0038 -0.0038 -0.0132 423  HIS A ND1 
3010  C CD2 . HIS A 425  ? 0.3187 0.2633 0.3487 -0.0056 -0.0060 -0.0160 423  HIS A CD2 
3011  C CE1 . HIS A 425  ? 0.3789 0.3279 0.4028 -0.0039 -0.0028 -0.0136 423  HIS A CE1 
3012  N NE2 . HIS A 425  ? 0.3030 0.2528 0.3294 -0.0049 -0.0041 -0.0153 423  HIS A NE2 
3013  N N   . ASN A 426  ? 0.2855 0.2060 0.3259 -0.0103 -0.0099 -0.0073 424  ASN A N   
3014  C CA  . ASN A 426  ? 0.3376 0.2514 0.3806 -0.0108 -0.0118 -0.0059 424  ASN A CA  
3015  C C   . ASN A 426  ? 0.3210 0.2318 0.3691 -0.0129 -0.0142 -0.0068 424  ASN A C   
3016  O O   . ASN A 426  ? 0.3230 0.2349 0.3725 -0.0156 -0.0133 -0.0043 424  ASN A O   
3017  C CB  . ASN A 426  ? 0.3199 0.2321 0.3611 -0.0121 -0.0097 -0.0004 424  ASN A CB  
3018  C CG  . ASN A 426  ? 0.3557 0.2612 0.3990 -0.0125 -0.0116 0.0017  424  ASN A CG  
3019  O OD1 . ASN A 426  ? 0.3538 0.2550 0.4014 -0.0136 -0.0142 0.0008  424  ASN A OD1 
3020  N ND2 . ASN A 426  ? 0.3412 0.2457 0.3816 -0.0117 -0.0103 0.0046  424  ASN A ND2 
3021  N N   . ALA A 427  ? 0.3196 0.2267 0.3707 -0.0116 -0.0174 -0.0107 425  ALA A N   
3022  C CA  . ALA A 427  ? 0.3365 0.2406 0.3927 -0.0134 -0.0202 -0.0124 425  ALA A CA  
3023  C C   . ALA A 427  ? 0.3076 0.2065 0.3669 -0.0166 -0.0206 -0.0073 425  ALA A C   
3024  O O   . ALA A 427  ? 0.3178 0.2159 0.3811 -0.0192 -0.0217 -0.0070 425  ALA A O   
3025  C CB  . ALA A 427  ? 0.3711 0.2720 0.4299 -0.0110 -0.0237 -0.0178 425  ALA A CB  
3026  N N   . GLN A 428  ? 0.3454 0.2411 0.4030 -0.0166 -0.0197 -0.0033 426  GLN A N   
3027  C CA  . GLN A 428  ? 0.3413 0.2328 0.4014 -0.0198 -0.0199 0.0020  426  GLN A CA  
3028  C C   . GLN A 428  ? 0.3048 0.2012 0.3637 -0.0224 -0.0168 0.0058  426  GLN A C   
3029  O O   . GLN A 428  ? 0.3195 0.2150 0.3820 -0.0257 -0.0172 0.0080  426  GLN A O   
3030  C CB  . GLN A 428  ? 0.3391 0.2264 0.3973 -0.0188 -0.0198 0.0053  426  GLN A CB  
3031  C CG  . GLN A 428  ? 0.3490 0.2306 0.4104 -0.0219 -0.0210 0.0104  426  GLN A CG  
3032  C CD  . GLN A 428  ? 0.4194 0.3046 0.4798 -0.0251 -0.0179 0.0158  426  GLN A CD  
3033  O OE1 . GLN A 428  ? 0.3944 0.2850 0.4504 -0.0243 -0.0147 0.0169  426  GLN A OE1 
3034  N NE2 . GLN A 428  ? 0.3557 0.2383 0.4203 -0.0287 -0.0190 0.0189  426  GLN A NE2 
3035  N N   . THR A 429  ? 0.3381 0.2399 0.3921 -0.0211 -0.0136 0.0065  427  THR A N   
3036  C CA  . THR A 429  ? 0.2968 0.2040 0.3495 -0.0230 -0.0107 0.0092  427  THR A CA  
3037  C C   . THR A 429  ? 0.3354 0.2454 0.3913 -0.0245 -0.0115 0.0068  427  THR A C   
3038  O O   . THR A 429  ? 0.3144 0.2255 0.3728 -0.0274 -0.0109 0.0095  427  THR A O   
3039  C CB  . THR A 429  ? 0.3387 0.2510 0.3859 -0.0207 -0.0079 0.0089  427  THR A CB  
3040  O OG1 . THR A 429  ? 0.3149 0.2246 0.3593 -0.0189 -0.0076 0.0102  427  THR A OG1 
3041  C CG2 . THR A 429  ? 0.2987 0.2156 0.3445 -0.0224 -0.0050 0.0123  427  THR A CG2 
3042  N N   . LEU A 430  ? 0.2843 0.1960 0.3401 -0.0224 -0.0128 0.0016  428  LEU A N   
3043  C CA  . LEU A 430  ? 0.2989 0.2133 0.3575 -0.0234 -0.0140 -0.0014 428  LEU A CA  
3044  C C   . LEU A 430  ? 0.3278 0.2378 0.3923 -0.0264 -0.0164 -0.0005 428  LEU A C   
3045  O O   . LEU A 430  ? 0.3172 0.2296 0.3841 -0.0290 -0.0160 0.0009  428  LEU A O   
3046  C CB  . LEU A 430  ? 0.2956 0.2115 0.3533 -0.0204 -0.0156 -0.0073 428  LEU A CB  
3047  C CG  . LEU A 430  ? 0.3571 0.2778 0.4160 -0.0203 -0.0164 -0.0114 428  LEU A CG  
3048  C CD1 . LEU A 430  ? 0.3683 0.2909 0.4252 -0.0169 -0.0175 -0.0166 428  LEU A CD1 
3049  C CD2 . LEU A 430  ? 0.3701 0.2883 0.4349 -0.0227 -0.0191 -0.0126 428  LEU A CD2 
3050  N N   . ALA A 431  ? 0.3109 0.2143 0.3779 -0.0260 -0.0192 -0.0014 429  ALA A N   
3051  C CA  . ALA A 431  ? 0.3174 0.2158 0.3904 -0.0289 -0.0220 -0.0008 429  ALA A CA  
3052  C C   . ALA A 431  ? 0.2968 0.1949 0.3712 -0.0326 -0.0204 0.0055  429  ALA A C   
3053  O O   . ALA A 431  ? 0.3197 0.2181 0.3985 -0.0357 -0.0213 0.0064  429  ALA A O   
3054  C CB  . ALA A 431  ? 0.3499 0.2408 0.4251 -0.0275 -0.0254 -0.0024 429  ALA A CB  
3055  N N   . ALA A 432  ? 0.3209 0.2192 0.3917 -0.0324 -0.0180 0.0099  430  ALA A N   
3056  C CA  . ALA A 432  ? 0.3373 0.2362 0.4090 -0.0358 -0.0161 0.0160  430  ALA A CA  
3057  C C   . ALA A 432  ? 0.3276 0.2333 0.3996 -0.0376 -0.0140 0.0165  430  ALA A C   
3058  O O   . ALA A 432  ? 0.3463 0.2525 0.4220 -0.0412 -0.0140 0.0195  430  ALA A O   
3059  C CB  . ALA A 432  ? 0.3107 0.2099 0.3774 -0.0347 -0.0136 0.0199  430  ALA A CB  
3060  N N   . ILE A 433  ? 0.3005 0.2118 0.3690 -0.0353 -0.0123 0.0136  431  ILE A N   
3061  C CA  . ILE A 433  ? 0.3335 0.2515 0.4019 -0.0365 -0.0103 0.0140  431  ILE A CA  
3062  C C   . ILE A 433  ? 0.3143 0.2331 0.3874 -0.0378 -0.0126 0.0106  431  ILE A C   
3063  O O   . ILE A 433  ? 0.3049 0.2272 0.3808 -0.0405 -0.0119 0.0121  431  ILE A O   
3064  C CB  . ILE A 433  ? 0.3455 0.2686 0.4084 -0.0334 -0.0078 0.0124  431  ILE A CB  
3065  C CG1 . ILE A 433  ? 0.3126 0.2356 0.3714 -0.0328 -0.0053 0.0164  431  ILE A CG1 
3066  C CG2 . ILE A 433  ? 0.3158 0.2455 0.3788 -0.0339 -0.0064 0.0116  431  ILE A CG2 
3067  C CD1 . ILE A 433  ? 0.3599 0.2866 0.4136 -0.0297 -0.0034 0.0150  431  ILE A CD1 
3068  N N   . TYR A 434  ? 0.2978 0.2138 0.3720 -0.0360 -0.0154 0.0056  432  TYR A N   
3069  C CA  . TYR A 434  ? 0.3234 0.2396 0.4023 -0.0371 -0.0180 0.0019  432  TYR A CA  
3070  C C   . TYR A 434  ? 0.3129 0.2258 0.3977 -0.0413 -0.0195 0.0050  432  TYR A C   
3071  O O   . TYR A 434  ? 0.3541 0.2701 0.4423 -0.0437 -0.0198 0.0048  432  TYR A O   
3072  C CB  . TYR A 434  ? 0.3199 0.2328 0.3991 -0.0343 -0.0210 -0.0037 432  TYR A CB  
3073  C CG  . TYR A 434  ? 0.3287 0.2406 0.4132 -0.0354 -0.0244 -0.0079 432  TYR A CG  
3074  C CD1 . TYR A 434  ? 0.3436 0.2616 0.4284 -0.0354 -0.0242 -0.0108 432  TYR A CD1 
3075  C CD2 . TYR A 434  ? 0.3367 0.2415 0.4258 -0.0362 -0.0280 -0.0092 432  TYR A CD2 
3076  C CE1 . TYR A 434  ? 0.3653 0.2826 0.4549 -0.0363 -0.0275 -0.0150 432  TYR A CE1 
3077  C CE2 . TYR A 434  ? 0.3873 0.2909 0.4814 -0.0371 -0.0313 -0.0135 432  TYR A CE2 
3078  C CZ  . TYR A 434  ? 0.4028 0.3129 0.4972 -0.0371 -0.0310 -0.0164 432  TYR A CZ  
3079  O OH  . TYR A 434  ? 0.4224 0.3316 0.5218 -0.0380 -0.0345 -0.0208 432  TYR A OH  
3080  N N   . HIS A 435  ? 0.3395 0.2459 0.4255 -0.0423 -0.0205 0.0081  433  HIS A N   
3081  C CA  . HIS A 435  ? 0.3415 0.2445 0.4332 -0.0466 -0.0220 0.0115  433  HIS A CA  
3082  C C   . HIS A 435  ? 0.3580 0.2657 0.4492 -0.0495 -0.0187 0.0173  433  HIS A C   
3083  O O   . HIS A 435  ? 0.3475 0.2561 0.4435 -0.0532 -0.0192 0.0194  433  HIS A O   
3084  C CB  . HIS A 435  ? 0.4230 0.3173 0.5165 -0.0467 -0.0246 0.0128  433  HIS A CB  
3085  C CG  . HIS A 435  ? 0.3885 0.2779 0.4847 -0.0447 -0.0286 0.0069  433  HIS A CG  
3086  N ND1 . HIS A 435  ? 0.4162 0.3025 0.5188 -0.0469 -0.0321 0.0047  433  HIS A ND1 
3087  C CD2 . HIS A 435  ? 0.4177 0.3054 0.5110 -0.0405 -0.0298 0.0024  433  HIS A CD2 
3088  C CE1 . HIS A 435  ? 0.4086 0.2912 0.5122 -0.0441 -0.0353 -0.0011 433  HIS A CE1 
3089  N NE2 . HIS A 435  ? 0.4254 0.3090 0.5235 -0.0402 -0.0339 -0.0025 433  HIS A NE2 
3090  N N   . MET A 436  ? 0.3496 0.2605 0.4353 -0.0478 -0.0154 0.0198  434  MET A N   
3091  C CA  . MET A 436  ? 0.3240 0.2404 0.4088 -0.0500 -0.0121 0.0246  434  MET A CA  
3092  C C   . MET A 436  ? 0.3222 0.2454 0.4088 -0.0510 -0.0113 0.0227  434  MET A C   
3093  O O   . MET A 436  ? 0.3648 0.2916 0.4542 -0.0542 -0.0101 0.0260  434  MET A O   
3094  C CB  . MET A 436  ? 0.3232 0.2421 0.4015 -0.0474 -0.0089 0.0264  434  MET A CB  
3095  C CG  . MET A 436  ? 0.3896 0.3145 0.4668 -0.0492 -0.0055 0.0310  434  MET A CG  
3096  S SD  . MET A 436  ? 0.3675 0.2955 0.4373 -0.0458 -0.0021 0.0322  434  MET A SD  
3097  C CE  . MET A 436  ? 0.3827 0.3033 0.4513 -0.0458 -0.0032 0.0355  434  MET A CE  
3098  N N   . ALA A 437  ? 0.2948 0.2202 0.3799 -0.0482 -0.0120 0.0175  435  ALA A N   
3099  C CA  . ALA A 437  ? 0.3221 0.2541 0.4086 -0.0487 -0.0113 0.0155  435  ALA A CA  
3100  C C   . ALA A 437  ? 0.3761 0.3073 0.4694 -0.0522 -0.0139 0.0147  435  ALA A C   
3101  O O   . ALA A 437  ? 0.3426 0.2797 0.4380 -0.0538 -0.0130 0.0148  435  ALA A O   
3102  C CB  . ALA A 437  ? 0.3366 0.2710 0.4196 -0.0449 -0.0116 0.0103  435  ALA A CB  
3103  N N   . GLY A 438  ? 0.3794 0.3036 0.4764 -0.0533 -0.0171 0.0139  436  GLY A N   
3104  C CA  . GLY A 438  ? 0.3861 0.3089 0.4900 -0.0568 -0.0198 0.0132  436  GLY A CA  
3105  C C   . GLY A 438  ? 0.4224 0.3476 0.5279 -0.0554 -0.0219 0.0071  436  GLY A C   
3106  O O   . GLY A 438  ? 0.3885 0.3158 0.4898 -0.0517 -0.0216 0.0031  436  GLY A O   
3107  N N   . LYS A 439  ? 0.4278 0.3531 0.5397 -0.0587 -0.0241 0.0064  437  LYS A N   
3108  C CA  . LYS A 439  ? 0.4404 0.3664 0.5552 -0.0579 -0.0272 0.0003  437  LYS A CA  
3109  C C   . LYS A 439  ? 0.4591 0.3937 0.5724 -0.0570 -0.0256 -0.0019 437  LYS A C   
3110  O O   . LYS A 439  ? 0.5115 0.4478 0.6244 -0.0547 -0.0274 -0.0074 437  LYS A O   
3111  C CB  . LYS A 439  ? 0.4881 0.4098 0.6108 -0.0620 -0.0306 0.0003  437  LYS A CB  
3112  N N   . ASP A 440  ? 0.4678 0.4083 0.5804 -0.0585 -0.0224 0.0021  438  ASP A N   
3113  C CA  . ASP A 440  ? 0.4183 0.3671 0.5299 -0.0577 -0.0211 0.0003  438  ASP A CA  
3114  C C   . ASP A 440  ? 0.4141 0.3657 0.5186 -0.0531 -0.0191 -0.0014 438  ASP A C   
3115  O O   . ASP A 440  ? 0.4105 0.3624 0.5106 -0.0520 -0.0163 0.0020  438  ASP A O   
3116  C CB  . ASP A 440  ? 0.4423 0.3966 0.5559 -0.0607 -0.0184 0.0051  438  ASP A CB  
3117  C CG  . ASP A 440  ? 0.5074 0.4617 0.6287 -0.0652 -0.0205 0.0058  438  ASP A CG  
3118  O OD1 . ASP A 440  ? 0.5081 0.4584 0.6332 -0.0658 -0.0242 0.0020  438  ASP A OD1 
3119  O OD2 . ASP A 440  ? 0.6321 0.5906 0.7557 -0.0682 -0.0186 0.0100  438  ASP A OD2 
3120  N N   . PHE A 441  ? 0.4015 0.3553 0.5048 -0.0506 -0.0207 -0.0066 439  PHE A N   
3121  C CA  . PHE A 441  ? 0.3577 0.3146 0.4545 -0.0466 -0.0190 -0.0082 439  PHE A CA  
3122  C C   . PHE A 441  ? 0.3689 0.3325 0.4655 -0.0454 -0.0195 -0.0116 439  PHE A C   
3123  O O   . PHE A 441  ? 0.3425 0.3068 0.4434 -0.0466 -0.0223 -0.0149 439  PHE A O   
3124  C CB  . PHE A 441  ? 0.3321 0.2838 0.4257 -0.0437 -0.0204 -0.0112 439  PHE A CB  
3125  C CG  . PHE A 441  ? 0.3420 0.2969 0.4289 -0.0399 -0.0184 -0.0121 439  PHE A CG  
3126  C CD1 . PHE A 441  ? 0.3663 0.3215 0.4491 -0.0391 -0.0153 -0.0080 439  PHE A CD1 
3127  C CD2 . PHE A 441  ? 0.3387 0.2969 0.4236 -0.0373 -0.0197 -0.0168 439  PHE A CD2 
3128  C CE1 . PHE A 441  ? 0.2732 0.2314 0.3502 -0.0359 -0.0135 -0.0086 439  PHE A CE1 
3129  C CE2 . PHE A 441  ? 0.3116 0.2730 0.3905 -0.0341 -0.0178 -0.0171 439  PHE A CE2 
3130  C CZ  . PHE A 441  ? 0.2689 0.2301 0.3441 -0.0335 -0.0147 -0.0129 439  PHE A CZ  
3131  N N   . HIS A 442  ? 0.3273 0.2957 0.4189 -0.0430 -0.0171 -0.0108 440  HIS A N   
3132  C CA  . HIS A 442  ? 0.3392 0.3137 0.4292 -0.0411 -0.0176 -0.0141 440  HIS A CA  
3133  C C   . HIS A 442  ? 0.3593 0.3355 0.4425 -0.0376 -0.0154 -0.0136 440  HIS A C   
3134  O O   . HIS A 442  ? 0.3064 0.2811 0.3868 -0.0373 -0.0129 -0.0100 440  HIS A O   
3135  C CB  . HIS A 442  ? 0.3594 0.3400 0.4527 -0.0431 -0.0169 -0.0127 440  HIS A CB  
3136  C CG  . HIS A 442  ? 0.3230 0.3060 0.4150 -0.0437 -0.0135 -0.0078 440  HIS A CG  
3137  N ND1 . HIS A 442  ? 0.3459 0.3332 0.4332 -0.0412 -0.0113 -0.0068 440  HIS A ND1 
3138  C CD2 . HIS A 442  ? 0.3234 0.3051 0.4180 -0.0465 -0.0120 -0.0036 440  HIS A CD2 
3139  C CE1 . HIS A 442  ? 0.3199 0.3085 0.4071 -0.0422 -0.0086 -0.0026 440  HIS A CE1 
3140  N NE2 . HIS A 442  ? 0.3613 0.3469 0.4527 -0.0454 -0.0089 -0.0005 440  HIS A NE2 
3141  N N   . VAL A 443  ? 0.3537 0.3332 0.4343 -0.0351 -0.0164 -0.0173 441  VAL A N   
3142  C CA  . VAL A 443  ? 0.3733 0.3547 0.4476 -0.0320 -0.0146 -0.0167 441  VAL A CA  
3143  C C   . VAL A 443  ? 0.3610 0.3463 0.4340 -0.0322 -0.0118 -0.0128 441  VAL A C   
3144  O O   . VAL A 443  ? 0.3427 0.3327 0.4183 -0.0332 -0.0119 -0.0126 441  VAL A O   
3145  C CB  . VAL A 443  ? 0.4185 0.4038 0.4905 -0.0296 -0.0162 -0.0210 441  VAL A CB  
3146  C CG1 . VAL A 443  ? 0.3689 0.3571 0.4349 -0.0269 -0.0142 -0.0197 441  VAL A CG1 
3147  C CG2 . VAL A 443  ? 0.4451 0.4265 0.5176 -0.0288 -0.0187 -0.0251 441  VAL A CG2 
3148  N N   . GLY A 444  ? 0.2903 0.2736 0.3595 -0.0311 -0.0094 -0.0098 442  GLY A N   
3149  C CA  . GLY A 444  ? 0.2905 0.2766 0.3585 -0.0312 -0.0067 -0.0060 442  GLY A CA  
3150  C C   . GLY A 444  ? 0.2402 0.2234 0.3102 -0.0334 -0.0051 -0.0023 442  GLY A C   
3151  O O   . GLY A 444  ? 0.2840 0.2691 0.3524 -0.0331 -0.0027 0.0008  442  GLY A O   
3152  N N   . LYS A 445  ? 0.2661 0.2448 0.3395 -0.0355 -0.0065 -0.0025 443  LYS A N   
3153  C CA  . LYS A 445  ? 0.2443 0.2203 0.3194 -0.0377 -0.0051 0.0014  443  LYS A CA  
3154  C C   . LYS A 445  ? 0.2533 0.2255 0.3238 -0.0360 -0.0035 0.0033  443  LYS A C   
3155  O O   . LYS A 445  ? 0.2558 0.2289 0.3248 -0.0362 -0.0010 0.0068  443  LYS A O   
3156  C CB  . LYS A 445  ? 0.3066 0.2787 0.3870 -0.0407 -0.0073 0.0010  443  LYS A CB  
3157  C CG  . LYS A 445  ? 0.3089 0.2795 0.3918 -0.0437 -0.0059 0.0055  443  LYS A CG  
3158  C CD  . LYS A 445  ? 0.3773 0.3438 0.4659 -0.0469 -0.0084 0.0054  443  LYS A CD  
3159  C CE  . LYS A 445  ? 0.4597 0.4261 0.5511 -0.0502 -0.0068 0.0104  443  LYS A CE  
3160  N NZ  . LYS A 445  ? 0.4383 0.4010 0.5359 -0.0539 -0.0094 0.0106  443  LYS A NZ  
3161  N N   . TYR A 446  ? 0.2630 0.2312 0.3313 -0.0343 -0.0049 0.0008  444  TYR A N   
3162  C CA  . TYR A 446  ? 0.2564 0.2217 0.3199 -0.0321 -0.0035 0.0018  444  TYR A CA  
3163  C C   . TYR A 446  ? 0.2487 0.2123 0.3101 -0.0298 -0.0054 -0.0023 444  TYR A C   
3164  O O   . TYR A 446  ? 0.2379 0.2024 0.3018 -0.0300 -0.0077 -0.0058 444  TYR A O   
3165  C CB  . TYR A 446  ? 0.2628 0.2231 0.3271 -0.0337 -0.0029 0.0050  444  TYR A CB  
3166  C CG  . TYR A 446  ? 0.2906 0.2456 0.3587 -0.0352 -0.0057 0.0035  444  TYR A CG  
3167  C CD1 . TYR A 446  ? 0.2950 0.2455 0.3614 -0.0333 -0.0073 0.0009  444  TYR A CD1 
3168  C CD2 . TYR A 446  ? 0.3171 0.2717 0.3906 -0.0385 -0.0069 0.0044  444  TYR A CD2 
3169  C CE1 . TYR A 446  ? 0.3528 0.2982 0.4229 -0.0344 -0.0101 -0.0008 444  TYR A CE1 
3170  C CE2 . TYR A 446  ? 0.3506 0.2999 0.4280 -0.0399 -0.0097 0.0030  444  TYR A CE2 
3171  C CZ  . TYR A 446  ? 0.3672 0.3118 0.4429 -0.0378 -0.0113 0.0003  444  TYR A CZ  
3172  O OH  . TYR A 446  ? 0.4902 0.4293 0.5701 -0.0390 -0.0144 -0.0013 444  TYR A OH  
3173  N N   . GLU A 447  ? 0.2362 0.1979 0.2933 -0.0276 -0.0045 -0.0021 445  GLU A N   
3174  C CA  . GLU A 447  ? 0.2456 0.2060 0.3009 -0.0255 -0.0061 -0.0059 445  GLU A CA  
3175  C C   . GLU A 447  ? 0.2522 0.2081 0.3047 -0.0243 -0.0054 -0.0047 445  GLU A C   
3176  O O   . GLU A 447  ? 0.2518 0.2064 0.3030 -0.0247 -0.0034 -0.0010 445  GLU A O   
3177  C CB  . GLU A 447  ? 0.2320 0.1976 0.2839 -0.0233 -0.0058 -0.0078 445  GLU A CB  
3178  C CG  . GLU A 447  ? 0.2424 0.2096 0.2898 -0.0219 -0.0031 -0.0050 445  GLU A CG  
3179  C CD  . GLU A 447  ? 0.2611 0.2333 0.3053 -0.0200 -0.0028 -0.0062 445  GLU A CD  
3180  O OE1 . GLU A 447  ? 0.2463 0.2219 0.2919 -0.0200 -0.0044 -0.0088 445  GLU A OE1 
3181  O OE2 . GLU A 447  ? 0.2460 0.2189 0.2864 -0.0185 -0.0011 -0.0046 445  GLU A OE2 
3182  N N   . PHE A 448  ? 0.2432 0.1969 0.2950 -0.0226 -0.0072 -0.0080 446  PHE A N   
3183  C CA  . PHE A 448  ? 0.2539 0.2046 0.3023 -0.0208 -0.0065 -0.0075 446  PHE A CA  
3184  C C   . PHE A 448  ? 0.2327 0.1876 0.2764 -0.0183 -0.0053 -0.0087 446  PHE A C   
3185  O O   . PHE A 448  ? 0.2621 0.2217 0.3053 -0.0179 -0.0055 -0.0104 446  PHE A O   
3186  C CB  . PHE A 448  ? 0.2498 0.1956 0.3003 -0.0203 -0.0090 -0.0104 446  PHE A CB  
3187  C CG  . PHE A 448  ? 0.2414 0.1822 0.2965 -0.0228 -0.0103 -0.0087 446  PHE A CG  
3188  C CD1 . PHE A 448  ? 0.2836 0.2202 0.3383 -0.0236 -0.0093 -0.0050 446  PHE A CD1 
3189  C CD2 . PHE A 448  ? 0.2597 0.2001 0.3196 -0.0246 -0.0126 -0.0108 446  PHE A CD2 
3190  C CE1 . PHE A 448  ? 0.3390 0.2711 0.3980 -0.0261 -0.0105 -0.0029 446  PHE A CE1 
3191  C CE2 . PHE A 448  ? 0.3148 0.2504 0.3792 -0.0273 -0.0139 -0.0088 446  PHE A CE2 
3192  C CZ  . PHE A 448  ? 0.3191 0.2505 0.3830 -0.0281 -0.0128 -0.0047 446  PHE A CZ  
3193  N N   . GLN A 449  ? 0.2282 0.1814 0.2686 -0.0168 -0.0041 -0.0077 447  GLN A N   
3194  C CA  . GLN A 449  ? 0.2253 0.1821 0.2614 -0.0145 -0.0031 -0.0087 447  GLN A CA  
3195  C C   . GLN A 449  ? 0.2446 0.1986 0.2789 -0.0127 -0.0036 -0.0101 447  GLN A C   
3196  O O   . GLN A 449  ? 0.2411 0.1902 0.2767 -0.0131 -0.0039 -0.0090 447  GLN A O   
3197  C CB  . GLN A 449  ? 0.2215 0.1807 0.2547 -0.0145 -0.0005 -0.0051 447  GLN A CB  
3198  C CG  . GLN A 449  ? 0.2468 0.2093 0.2818 -0.0160 -0.0001 -0.0039 447  GLN A CG  
3199  C CD  . GLN A 449  ? 0.2475 0.2132 0.2794 -0.0153 0.0020  -0.0016 447  GLN A CD  
3200  O OE1 . GLN A 449  ? 0.2460 0.2109 0.2747 -0.0141 0.0032  -0.0003 447  GLN A OE1 
3201  N NE2 . GLN A 449  ? 0.2384 0.2077 0.2715 -0.0160 0.0021  -0.0011 447  GLN A NE2 
3202  N N   . CYS A 450  ? 0.2480 0.2054 0.2794 -0.0108 -0.0036 -0.0124 448  CYS A N   
3203  C CA  . CYS A 450  ? 0.2637 0.2198 0.2934 -0.0088 -0.0039 -0.0140 448  CYS A CA  
3204  C C   . CYS A 450  ? 0.2863 0.2473 0.3118 -0.0073 -0.0026 -0.0143 448  CYS A C   
3205  O O   . CYS A 450  ? 0.2733 0.2387 0.2976 -0.0076 -0.0020 -0.0138 448  CYS A O   
3206  C CB  . CYS A 450  ? 0.2748 0.2293 0.3069 -0.0080 -0.0066 -0.0185 448  CYS A CB  
3207  S SG  . CYS A 450  ? 0.3112 0.2726 0.3428 -0.0068 -0.0080 -0.0232 448  CYS A SG  
3208  N N   . LEU A 451  ? 0.2567 0.2172 0.2801 -0.0056 -0.0023 -0.0151 449  LEU A N   
3209  C CA  . LEU A 451  ? 0.2870 0.2522 0.3067 -0.0043 -0.0012 -0.0153 449  LEU A CA  
3210  C C   . LEU A 451  ? 0.2693 0.2387 0.2887 -0.0028 -0.0027 -0.0198 449  LEU A C   
3211  O O   . LEU A 451  ? 0.3030 0.2705 0.3245 -0.0019 -0.0046 -0.0231 449  LEU A O   
3212  C CB  . LEU A 451  ? 0.2889 0.2521 0.3065 -0.0033 0.0000  -0.0137 449  LEU A CB  
3213  C CG  . LEU A 451  ? 0.3667 0.3344 0.3807 -0.0020 0.0012  -0.0138 449  LEU A CG  
3214  C CD1 . LEU A 451  ? 0.3685 0.3399 0.3804 -0.0029 0.0027  -0.0112 449  LEU A CD1 
3215  C CD2 . LEU A 451  ? 0.4438 0.4088 0.4564 -0.0013 0.0021  -0.0124 449  LEU A CD2 
3216  N N   . HIS A 452  ? 0.2753 0.2506 0.2922 -0.0024 -0.0020 -0.0198 450  HIS A N   
3217  C CA  . HIS A 452  ? 0.2886 0.2692 0.3044 -0.0009 -0.0031 -0.0237 450  HIS A CA  
3218  C C   . HIS A 452  ? 0.3102 0.2905 0.3254 0.0009  -0.0034 -0.0260 450  HIS A C   
3219  O O   . HIS A 452  ? 0.2961 0.2745 0.3097 0.0012  -0.0020 -0.0237 450  HIS A O   
3220  C CB  . HIS A 452  ? 0.2748 0.2617 0.2873 -0.0010 -0.0018 -0.0221 450  HIS A CB  
3221  C CG  . HIS A 452  ? 0.2742 0.2674 0.2848 0.0006  -0.0024 -0.0255 450  HIS A CG  
3222  N ND1 . HIS A 452  ? 0.3096 0.3070 0.3209 0.0011  -0.0040 -0.0290 450  HIS A ND1 
3223  C CD2 . HIS A 452  ? 0.3026 0.2989 0.3108 0.0019  -0.0017 -0.0261 450  HIS A CD2 
3224  C CE1 . HIS A 452  ? 0.3610 0.3641 0.3701 0.0026  -0.0042 -0.0315 450  HIS A CE1 
3225  N NE2 . HIS A 452  ? 0.3003 0.3029 0.3076 0.0031  -0.0027 -0.0298 450  HIS A NE2 
3226  N N   . GLY A 453  ? 0.3666 0.3490 0.3830 0.0024  -0.0053 -0.0308 451  GLY A N   
3227  C CA  . GLY A 453  ? 0.3599 0.3429 0.3757 0.0045  -0.0058 -0.0336 451  GLY A CA  
3228  C C   . GLY A 453  ? 0.4295 0.4053 0.4473 0.0047  -0.0062 -0.0329 451  GLY A C   
3229  O O   . GLY A 453  ? 0.5163 0.4924 0.5332 0.0063  -0.0060 -0.0338 451  GLY A O   
3230  N N   . MET A 454  ? 0.3991 0.3689 0.4196 0.0031  -0.0067 -0.0310 452  MET A N   
3231  C CA  . MET A 454  ? 0.4167 0.3795 0.4391 0.0031  -0.0073 -0.0299 452  MET A CA  
3232  C C   . MET A 454  ? 0.3882 0.3458 0.4149 0.0018  -0.0093 -0.0304 452  MET A C   
3233  O O   . MET A 454  ? 0.3849 0.3381 0.4144 0.0026  -0.0113 -0.0327 452  MET A O   
3234  C CB  . MET A 454  ? 0.3705 0.3313 0.3909 0.0020  -0.0049 -0.0247 452  MET A CB  
3235  C CG  . MET A 454  ? 0.4472 0.4011 0.4692 0.0020  -0.0054 -0.0231 452  MET A CG  
3236  S SD  . MET A 454  ? 0.6432 0.5962 0.6658 0.0049  -0.0071 -0.0272 452  MET A SD  
3237  C CE  . MET A 454  ? 0.5412 0.5011 0.5592 0.0062  -0.0049 -0.0269 452  MET A CE  
3238  N N   . GLY A 455  ? 0.3396 0.2977 0.3670 -0.0003 -0.0088 -0.0284 453  GLY A N   
3239  C CA  . GLY A 455  ? 0.3054 0.2588 0.3369 -0.0020 -0.0104 -0.0283 453  GLY A CA  
3240  C C   . GLY A 455  ? 0.3179 0.2730 0.3523 -0.0018 -0.0129 -0.0328 453  GLY A C   
3241  O O   . GLY A 455  ? 0.3273 0.2779 0.3658 -0.0032 -0.0148 -0.0333 453  GLY A O   
3242  N N   . GLU A 456  ? 0.3509 0.3125 0.3833 -0.0004 -0.0131 -0.0361 454  GLU A N   
3243  C CA  . GLU A 456  ? 0.3752 0.3390 0.4103 -0.0001 -0.0155 -0.0406 454  GLU A CA  
3244  C C   . GLU A 456  ? 0.3556 0.3146 0.3947 0.0009  -0.0186 -0.0448 454  GLU A C   
3245  O O   . GLU A 456  ? 0.3973 0.3544 0.4402 -0.0002 -0.0208 -0.0468 454  GLU A O   
3246  C CB  . GLU A 456  ? 0.3844 0.3567 0.4162 0.0016  -0.0152 -0.0436 454  GLU A CB  
3247  C CG  . GLU A 456  ? 0.3979 0.3749 0.4265 0.0004  -0.0129 -0.0400 454  GLU A CG  
3248  C CD  . GLU A 456  ? 0.3926 0.3715 0.4171 0.0011  -0.0103 -0.0369 454  GLU A CD  
3249  O OE1 . GLU A 456  ? 0.4023 0.3770 0.4268 0.0017  -0.0100 -0.0362 454  GLU A OE1 
3250  O OE2 . GLU A 456  ? 0.3995 0.3839 0.4207 0.0009  -0.0088 -0.0353 454  GLU A OE2 
3251  N N   . PRO A 457  ? 0.3357 0.2926 0.3744 0.0030  -0.0191 -0.0463 455  PRO A N   
3252  C CA  . PRO A 457  ? 0.4118 0.3633 0.4548 0.0040  -0.0224 -0.0502 455  PRO A CA  
3253  C C   . PRO A 457  ? 0.3906 0.3343 0.4378 0.0014  -0.0236 -0.0474 455  PRO A C   
3254  O O   . PRO A 457  ? 0.3657 0.3062 0.4173 0.0010  -0.0265 -0.0505 455  PRO A O   
3255  C CB  . PRO A 457  ? 0.3663 0.3167 0.4077 0.0065  -0.0222 -0.0510 455  PRO A CB  
3256  C CG  . PRO A 457  ? 0.4059 0.3636 0.4423 0.0073  -0.0193 -0.0498 455  PRO A CG  
3257  C CD  . PRO A 457  ? 0.3344 0.2938 0.3691 0.0046  -0.0171 -0.0451 455  PRO A CD  
3258  N N   . LEU A 458  ? 0.3706 0.3113 0.4166 -0.0005 -0.0213 -0.0414 456  LEU A N   
3259  C CA  . LEU A 458  ? 0.3720 0.3063 0.4218 -0.0033 -0.0221 -0.0382 456  LEU A CA  
3260  C C   . LEU A 458  ? 0.3360 0.2725 0.3879 -0.0056 -0.0225 -0.0382 456  LEU A C   
3261  O O   . LEU A 458  ? 0.3385 0.2709 0.3951 -0.0071 -0.0250 -0.0394 456  LEU A O   
3262  C CB  . LEU A 458  ? 0.3497 0.2814 0.3973 -0.0047 -0.0194 -0.0320 456  LEU A CB  
3263  C CG  . LEU A 458  ? 0.3792 0.3059 0.4299 -0.0080 -0.0194 -0.0276 456  LEU A CG  
3264  C CD1 . LEU A 458  ? 0.3732 0.2930 0.4292 -0.0086 -0.0229 -0.0293 456  LEU A CD1 
3265  C CD2 . LEU A 458  ? 0.3802 0.3052 0.4282 -0.0088 -0.0167 -0.0220 456  LEU A CD2 
3266  N N   . TYR A 459  ? 0.3403 0.2830 0.3889 -0.0061 -0.0201 -0.0367 457  TYR A N   
3267  C CA  . TYR A 459  ? 0.3354 0.2802 0.3860 -0.0084 -0.0202 -0.0361 457  TYR A CA  
3268  C C   . TYR A 459  ? 0.3468 0.2952 0.3993 -0.0075 -0.0227 -0.0417 457  TYR A C   
3269  O O   . TYR A 459  ? 0.3824 0.3318 0.4376 -0.0094 -0.0236 -0.0419 457  TYR A O   
3270  C CB  . TYR A 459  ? 0.3118 0.2614 0.3586 -0.0092 -0.0170 -0.0320 457  TYR A CB  
3271  C CG  . TYR A 459  ? 0.2845 0.2301 0.3311 -0.0110 -0.0150 -0.0264 457  TYR A CG  
3272  C CD1 . TYR A 459  ? 0.2903 0.2329 0.3406 -0.0138 -0.0153 -0.0237 457  TYR A CD1 
3273  C CD2 . TYR A 459  ? 0.3175 0.2622 0.3605 -0.0098 -0.0130 -0.0239 457  TYR A CD2 
3274  C CE1 . TYR A 459  ? 0.2784 0.2178 0.3285 -0.0154 -0.0135 -0.0187 457  TYR A CE1 
3275  C CE2 . TYR A 459  ? 0.3124 0.2537 0.3552 -0.0114 -0.0113 -0.0190 457  TYR A CE2 
3276  C CZ  . TYR A 459  ? 0.3178 0.2566 0.3640 -0.0141 -0.0115 -0.0164 457  TYR A CZ  
3277  O OH  . TYR A 459  ? 0.2978 0.2338 0.3437 -0.0157 -0.0098 -0.0115 457  TYR A OH  
3278  N N   . GLU A 460  ? 0.3529 0.3035 0.4042 -0.0045 -0.0240 -0.0466 458  GLU A N   
3279  C CA  . GLU A 460  ? 0.3897 0.3425 0.4436 -0.0036 -0.0271 -0.0526 458  GLU A CA  
3280  C C   . GLU A 460  ? 0.4189 0.3644 0.4790 -0.0050 -0.0302 -0.0540 458  GLU A C   
3281  O O   . GLU A 460  ? 0.4259 0.3725 0.4893 -0.0053 -0.0328 -0.0581 458  GLU A O   
3282  C CB  . GLU A 460  ? 0.3888 0.3453 0.4404 0.0000  -0.0279 -0.0576 458  GLU A CB  
3283  N N   . GLU A 461  ? 0.3678 0.3060 0.4296 -0.0060 -0.0302 -0.0506 459  GLU A N   
3284  C CA  . GLU A 461  ? 0.4135 0.3441 0.4812 -0.0079 -0.0331 -0.0506 459  GLU A CA  
3285  C C   . GLU A 461  ? 0.4375 0.3664 0.5074 -0.0119 -0.0320 -0.0456 459  GLU A C   
3286  O O   . GLU A 461  ? 0.3833 0.3058 0.4581 -0.0141 -0.0341 -0.0445 459  GLU A O   
3287  C CB  . GLU A 461  ? 0.4196 0.3432 0.4880 -0.0069 -0.0338 -0.0494 459  GLU A CB  
3288  C CG  . GLU A 461  ? 0.4611 0.3865 0.5274 -0.0029 -0.0346 -0.0541 459  GLU A CG  
3289  C CD  . GLU A 461  ? 0.4861 0.4122 0.5557 -0.0011 -0.0384 -0.0614 459  GLU A CD  
3290  O OE1 . GLU A 461  ? 0.4581 0.3803 0.5329 -0.0031 -0.0410 -0.0625 459  GLU A OE1 
3291  O OE2 . GLU A 461  ? 0.5188 0.4498 0.5861 0.0022  -0.0387 -0.0661 459  GLU A OE2 
3292  N N   . VAL A 462  ? 0.3906 0.3250 0.4571 -0.0128 -0.0289 -0.0424 460  VAL A N   
3293  C CA  . VAL A 462  ? 0.3691 0.3031 0.4373 -0.0163 -0.0275 -0.0375 460  VAL A CA  
3294  C C   . VAL A 462  ? 0.3840 0.3243 0.4526 -0.0172 -0.0274 -0.0390 460  VAL A C   
3295  O O   . VAL A 462  ? 0.4034 0.3427 0.4764 -0.0199 -0.0287 -0.0386 460  VAL A O   
3296  C CB  . VAL A 462  ? 0.3526 0.2869 0.4166 -0.0167 -0.0238 -0.0316 460  VAL A CB  
3297  C CG1 . VAL A 462  ? 0.3441 0.2792 0.4097 -0.0201 -0.0221 -0.0269 460  VAL A CG1 
3298  C CG2 . VAL A 462  ? 0.3562 0.2842 0.4202 -0.0161 -0.0239 -0.0297 460  VAL A CG2 
3299  N N   . VAL A 463  ? 0.3592 0.3064 0.4233 -0.0151 -0.0260 -0.0406 461  VAL A N   
3300  C CA  . VAL A 463  ? 0.3732 0.3269 0.4370 -0.0157 -0.0258 -0.0417 461  VAL A CA  
3301  C C   . VAL A 463  ? 0.4216 0.3757 0.4894 -0.0155 -0.0295 -0.0475 461  VAL A C   
3302  O O   . VAL A 463  ? 0.4387 0.3911 0.5072 -0.0134 -0.0317 -0.0521 461  VAL A O   
3303  C CB  . VAL A 463  ? 0.3624 0.3229 0.4201 -0.0133 -0.0236 -0.0418 461  VAL A CB  
3304  C CG1 . VAL A 463  ? 0.4084 0.3757 0.4658 -0.0137 -0.0237 -0.0431 461  VAL A CG1 
3305  C CG2 . VAL A 463  ? 0.3155 0.2753 0.3697 -0.0137 -0.0202 -0.0362 461  VAL A CG2 
3306  N N   . GLY A 464  ? 0.4037 0.3603 0.4744 -0.0176 -0.0302 -0.0476 462  GLY A N   
3307  C CA  . GLY A 464  ? 0.4557 0.4143 0.5296 -0.0172 -0.0335 -0.0534 462  GLY A CA  
3308  C C   . GLY A 464  ? 0.4847 0.4370 0.5655 -0.0199 -0.0363 -0.0539 462  GLY A C   
3309  O O   . GLY A 464  ? 0.4432 0.3884 0.5262 -0.0211 -0.0366 -0.0514 462  GLY A O   
3310  N N   . ARG A 465  ? 0.4821 0.4372 0.5665 -0.0209 -0.0387 -0.0573 463  ARG A N   
3311  C CA  . ARG A 465  ? 0.4641 0.4138 0.5556 -0.0239 -0.0416 -0.0580 463  ARG A CA  
3312  C C   . ARG A 465  ? 0.4799 0.4223 0.5746 -0.0229 -0.0447 -0.0613 463  ARG A C   
3313  O O   . ARG A 465  ? 0.5413 0.4769 0.6415 -0.0256 -0.0465 -0.0599 463  ARG A O   
3314  C CB  . ARG A 465  ? 0.5099 0.4648 0.6044 -0.0246 -0.0438 -0.0620 463  ARG A CB  
3315  N N   . GLY A 466  ? 0.4796 0.4231 0.5711 -0.0191 -0.0453 -0.0656 464  GLY A N   
3316  C CA  . GLY A 466  ? 0.5064 0.4432 0.6008 -0.0177 -0.0483 -0.0691 464  GLY A CA  
3317  C C   . GLY A 466  ? 0.5356 0.4658 0.6289 -0.0177 -0.0469 -0.0646 464  GLY A C   
3318  O O   . GLY A 466  ? 0.5173 0.4412 0.6134 -0.0166 -0.0495 -0.0669 464  GLY A O   
3319  N N   . LYS A 467  ? 0.4721 0.4038 0.5616 -0.0188 -0.0429 -0.0583 465  LYS A N   
3320  C CA  . LYS A 467  ? 0.4348 0.3611 0.5226 -0.0187 -0.0412 -0.0538 465  LYS A CA  
3321  C C   . LYS A 467  ? 0.4607 0.3837 0.5508 -0.0228 -0.0398 -0.0472 465  LYS A C   
3322  O O   . LYS A 467  ? 0.4915 0.4108 0.5875 -0.0256 -0.0422 -0.0472 465  LYS A O   
3323  C CB  . LYS A 467  ? 0.4522 0.3833 0.5329 -0.0158 -0.0381 -0.0529 465  LYS A CB  
3324  C CG  . LYS A 467  ? 0.4895 0.4249 0.5680 -0.0119 -0.0395 -0.0595 465  LYS A CG  
3325  C CD  . LYS A 467  ? 0.4808 0.4098 0.5619 -0.0099 -0.0424 -0.0630 465  LYS A CD  
3326  C CE  . LYS A 467  ? 0.5148 0.4488 0.5932 -0.0057 -0.0434 -0.0694 465  LYS A CE  
3327  N NZ  . LYS A 467  ? 0.5466 0.4751 0.6261 -0.0033 -0.0451 -0.0715 465  LYS A NZ  
3328  N N   . LEU A 468  ? 0.4273 0.3521 0.5133 -0.0233 -0.0359 -0.0416 466  LEU A N   
3329  C CA  . LEU A 468  ? 0.4211 0.3441 0.5088 -0.0270 -0.0342 -0.0353 466  LEU A CA  
3330  C C   . LEU A 468  ? 0.4182 0.3482 0.5053 -0.0286 -0.0323 -0.0340 466  LEU A C   
3331  O O   . LEU A 468  ? 0.3872 0.3169 0.4764 -0.0318 -0.0310 -0.0294 466  LEU A O   
3332  C CB  . LEU A 468  ? 0.4015 0.3223 0.4853 -0.0266 -0.0312 -0.0301 466  LEU A CB  
3333  C CG  . LEU A 468  ? 0.3806 0.2949 0.4642 -0.0247 -0.0326 -0.0308 466  LEU A CG  
3334  C CD1 . LEU A 468  ? 0.4137 0.3263 0.4936 -0.0249 -0.0296 -0.0250 466  LEU A CD1 
3335  C CD2 . LEU A 468  ? 0.4049 0.3116 0.4951 -0.0265 -0.0366 -0.0320 466  LEU A CD2 
3336  N N   . ASP A 469  ? 0.3985 0.3351 0.4829 -0.0264 -0.0322 -0.0379 467  ASP A N   
3337  C CA  . ASP A 469  ? 0.4069 0.3504 0.4909 -0.0275 -0.0309 -0.0373 467  ASP A CA  
3338  C C   . ASP A 469  ? 0.3309 0.2767 0.4118 -0.0286 -0.0270 -0.0312 467  ASP A C   
3339  O O   . ASP A 469  ? 0.3248 0.2729 0.4078 -0.0312 -0.0261 -0.0285 467  ASP A O   
3340  C CB  . ASP A 469  ? 0.3931 0.3357 0.4836 -0.0305 -0.0336 -0.0388 467  ASP A CB  
3341  C CG  . ASP A 469  ? 0.4636 0.4138 0.5539 -0.0307 -0.0334 -0.0404 467  ASP A CG  
3342  O OD1 . ASP A 469  ? 0.4769 0.4330 0.5622 -0.0281 -0.0320 -0.0418 467  ASP A OD1 
3343  O OD2 . ASP A 469  ? 0.5661 0.5168 0.6615 -0.0337 -0.0347 -0.0402 467  ASP A OD2 
3344  N N   . ARG A 470  ? 0.3331 0.2784 0.4090 -0.0266 -0.0247 -0.0292 468  ARG A N   
3345  C CA  . ARG A 470  ? 0.3301 0.2782 0.4024 -0.0270 -0.0211 -0.0242 468  ARG A CA  
3346  C C   . ARG A 470  ? 0.3221 0.2751 0.3884 -0.0238 -0.0194 -0.0255 468  ARG A C   
3347  O O   . ARG A 470  ? 0.3219 0.2737 0.3860 -0.0213 -0.0202 -0.0284 468  ARG A O   
3348  C CB  . ARG A 470  ? 0.2872 0.2298 0.3592 -0.0280 -0.0196 -0.0196 468  ARG A CB  
3349  C CG  . ARG A 470  ? 0.3267 0.2643 0.4045 -0.0314 -0.0212 -0.0175 468  ARG A CG  
3350  C CD  . ARG A 470  ? 0.3317 0.2731 0.4121 -0.0344 -0.0200 -0.0147 468  ARG A CD  
3351  N NE  . ARG A 470  ? 0.3428 0.2799 0.4289 -0.0380 -0.0214 -0.0125 468  ARG A NE  
3352  C CZ  . ARG A 470  ? 0.3538 0.2899 0.4454 -0.0398 -0.0244 -0.0152 468  ARG A CZ  
3353  N NH1 . ARG A 470  ? 0.3445 0.2836 0.4365 -0.0383 -0.0264 -0.0205 468  ARG A NH1 
3354  N NH2 . ARG A 470  ? 0.3840 0.3161 0.4807 -0.0434 -0.0255 -0.0124 468  ARG A NH2 
3355  N N   . PRO A 471  ? 0.3038 0.2622 0.3676 -0.0238 -0.0172 -0.0234 469  PRO A N   
3356  C CA  . PRO A 471  ? 0.2528 0.2160 0.3112 -0.0211 -0.0159 -0.0244 469  PRO A CA  
3357  C C   . PRO A 471  ? 0.2760 0.2370 0.3303 -0.0197 -0.0136 -0.0216 469  PRO A C   
3358  O O   . PRO A 471  ? 0.2487 0.2056 0.3037 -0.0210 -0.0125 -0.0180 469  PRO A O   
3359  C CB  . PRO A 471  ? 0.2700 0.2388 0.3279 -0.0219 -0.0145 -0.0226 469  PRO A CB  
3360  C CG  . PRO A 471  ? 0.2771 0.2436 0.3385 -0.0248 -0.0137 -0.0188 469  PRO A CG  
3361  C CD  . PRO A 471  ? 0.3046 0.2654 0.3707 -0.0263 -0.0160 -0.0201 469  PRO A CD  
3362  N N   . CYS A 472  ? 0.2855 0.2497 0.3354 -0.0172 -0.0130 -0.0232 470  CYS A N   
3363  C CA  . CYS A 472  ? 0.2614 0.2243 0.3072 -0.0158 -0.0110 -0.0210 470  CYS A CA  
3364  C C   . CYS A 472  ? 0.2594 0.2282 0.3008 -0.0142 -0.0094 -0.0205 470  CYS A C   
3365  O O   . CYS A 472  ? 0.2999 0.2731 0.3403 -0.0130 -0.0105 -0.0237 470  CYS A O   
3366  C CB  . CYS A 472  ? 0.2561 0.2156 0.3015 -0.0140 -0.0123 -0.0238 470  CYS A CB  
3367  S SG  . CYS A 472  ? 0.2979 0.2561 0.3386 -0.0123 -0.0099 -0.0211 470  CYS A SG  
3368  N N   . ARG A 473  ? 0.2400 0.2089 0.2788 -0.0144 -0.0069 -0.0165 471  ARG A N   
3369  C CA  . ARG A 473  ? 0.2383 0.2119 0.2730 -0.0130 -0.0054 -0.0155 471  ARG A CA  
3370  C C   . ARG A 473  ? 0.2495 0.2219 0.2806 -0.0112 -0.0045 -0.0155 471  ARG A C   
3371  O O   . ARG A 473  ? 0.2609 0.2291 0.2918 -0.0114 -0.0036 -0.0135 471  ARG A O   
3372  C CB  . ARG A 473  ? 0.2300 0.2047 0.2642 -0.0140 -0.0034 -0.0114 471  ARG A CB  
3373  C CG  . ARG A 473  ? 0.2399 0.2191 0.2702 -0.0127 -0.0022 -0.0104 471  ARG A CG  
3374  C CD  . ARG A 473  ? 0.2211 0.2014 0.2517 -0.0136 -0.0007 -0.0069 471  ARG A CD  
3375  N NE  . ARG A 473  ? 0.2255 0.2065 0.2601 -0.0152 -0.0015 -0.0072 471  ARG A NE  
3376  C CZ  . ARG A 473  ? 0.2538 0.2392 0.2895 -0.0153 -0.0027 -0.0087 471  ARG A CZ  
3377  N NH1 . ARG A 473  ? 0.2282 0.2176 0.2610 -0.0138 -0.0031 -0.0096 471  ARG A NH1 
3378  N NH2 . ARG A 473  ? 0.2559 0.2416 0.2957 -0.0170 -0.0037 -0.0092 471  ARG A NH2 
3379  N N   . ILE A 474  ? 0.2714 0.2481 0.2997 -0.0095 -0.0048 -0.0177 472  ILE A N   
3380  C CA  . ILE A 474  ? 0.2519 0.2287 0.2770 -0.0078 -0.0041 -0.0181 472  ILE A CA  
3381  C C   . ILE A 474  ? 0.2688 0.2474 0.2904 -0.0076 -0.0018 -0.0144 472  ILE A C   
3382  O O   . ILE A 474  ? 0.2719 0.2549 0.2921 -0.0076 -0.0015 -0.0137 472  ILE A O   
3383  C CB  . ILE A 474  ? 0.2481 0.2291 0.2720 -0.0061 -0.0055 -0.0224 472  ILE A CB  
3384  C CG1 . ILE A 474  ? 0.3108 0.2892 0.3384 -0.0060 -0.0080 -0.0265 472  ILE A CG1 
3385  C CG2 . ILE A 474  ? 0.2462 0.2284 0.2665 -0.0045 -0.0044 -0.0223 472  ILE A CG2 
3386  C CD1 . ILE A 474  ? 0.3197 0.3033 0.3468 -0.0045 -0.0098 -0.0312 472  ILE A CD1 
3387  N N   . TYR A 475  ? 0.2285 0.2037 0.2489 -0.0075 -0.0004 -0.0122 473  TYR A N   
3388  C CA  . TYR A 475  ? 0.2622 0.2387 0.2793 -0.0071 0.0015  -0.0091 473  TYR A CA  
3389  C C   . TYR A 475  ? 0.2830 0.2633 0.2971 -0.0056 0.0015  -0.0108 473  TYR A C   
3390  O O   . TYR A 475  ? 0.2731 0.2522 0.2868 -0.0045 0.0011  -0.0128 473  TYR A O   
3391  C CB  . TYR A 475  ? 0.2844 0.2561 0.3014 -0.0074 0.0028  -0.0066 473  TYR A CB  
3392  C CG  . TYR A 475  ? 0.3034 0.2756 0.3177 -0.0073 0.0047  -0.0033 473  TYR A CG  
3393  C CD1 . TYR A 475  ? 0.3760 0.3489 0.3875 -0.0061 0.0054  -0.0032 473  TYR A CD1 
3394  C CD2 . TYR A 475  ? 0.2859 0.2579 0.3009 -0.0082 0.0057  -0.0006 473  TYR A CD2 
3395  C CE1 . TYR A 475  ? 0.3898 0.3627 0.3991 -0.0061 0.0070  -0.0003 473  TYR A CE1 
3396  C CE2 . TYR A 475  ? 0.3043 0.2765 0.3171 -0.0079 0.0073  0.0021  473  TYR A CE2 
3397  C CZ  . TYR A 475  ? 0.3761 0.3484 0.3861 -0.0069 0.0078  0.0022  473  TYR A CZ  
3398  O OH  . TYR A 475  ? 0.3948 0.3671 0.4030 -0.0067 0.0091  0.0047  473  TYR A OH  
3399  N N   . ALA A 476  ? 0.2557 0.2407 0.2676 -0.0054 0.0019  -0.0099 474  ALA A N   
3400  C CA  . ALA A 476  ? 0.2660 0.2561 0.2754 -0.0043 0.0016  -0.0117 474  ALA A CA  
3401  C C   . ALA A 476  ? 0.2536 0.2451 0.2598 -0.0041 0.0032  -0.0086 474  ALA A C   
3402  O O   . ALA A 476  ? 0.2539 0.2474 0.2592 -0.0047 0.0036  -0.0061 474  ALA A O   
3403  C CB  . ALA A 476  ? 0.2469 0.2420 0.2565 -0.0043 0.0003  -0.0134 474  ALA A CB  
3404  N N   . PRO A 477  ? 0.2706 0.2611 0.2754 -0.0034 0.0039  -0.0085 475  PRO A N   
3405  C CA  . PRO A 477  ? 0.2495 0.2416 0.2515 -0.0034 0.0053  -0.0058 475  PRO A CA  
3406  C C   . PRO A 477  ? 0.2737 0.2724 0.2735 -0.0032 0.0049  -0.0061 475  PRO A C   
3407  O O   . PRO A 477  ? 0.2676 0.2702 0.2674 -0.0025 0.0039  -0.0094 475  PRO A O   
3408  C CB  . PRO A 477  ? 0.3036 0.2938 0.3051 -0.0026 0.0058  -0.0066 475  PRO A CB  
3409  C CG  . PRO A 477  ? 0.3177 0.3035 0.3219 -0.0024 0.0049  -0.0088 475  PRO A CG  
3410  C CD  . PRO A 477  ? 0.2773 0.2651 0.2832 -0.0026 0.0034  -0.0111 475  PRO A CD  
3411  N N   . VAL A 478  ? 0.2548 0.2549 0.2528 -0.0038 0.0057  -0.0028 476  VAL A N   
3412  C CA  . VAL A 478  ? 0.2742 0.2805 0.2700 -0.0039 0.0055  -0.0021 476  VAL A CA  
3413  C C   . VAL A 478  ? 0.2890 0.2959 0.2826 -0.0043 0.0067  0.0010  476  VAL A C   
3414  O O   . VAL A 478  ? 0.2781 0.2811 0.2720 -0.0049 0.0074  0.0039  476  VAL A O   
3415  C CB  . VAL A 478  ? 0.3154 0.3231 0.3117 -0.0045 0.0047  -0.0008 476  VAL A CB  
3416  C CG1 . VAL A 478  ? 0.2929 0.3071 0.2866 -0.0045 0.0044  0.0003  476  VAL A CG1 
3417  C CG2 . VAL A 478  ? 0.2611 0.2683 0.2599 -0.0042 0.0035  -0.0040 476  VAL A CG2 
3418  N N   . GLY A 479  ? 0.3050 0.3169 0.2965 -0.0040 0.0068  0.0003  477  GLY A N   
3419  C CA  . GLY A 479  ? 0.3376 0.3508 0.3272 -0.0047 0.0078  0.0035  477  GLY A CA  
3420  C C   . GLY A 479  ? 0.4106 0.4285 0.3987 -0.0042 0.0082  0.0019  477  GLY A C   
3421  O O   . GLY A 479  ? 0.3309 0.3512 0.3193 -0.0031 0.0077  -0.0019 477  GLY A O   
3422  N N   . THR A 480  ? 0.3912 0.4104 0.3777 -0.0051 0.0091  0.0049  478  THR A N   
3423  C CA  . THR A 480  ? 0.4693 0.4934 0.4545 -0.0048 0.0097  0.0039  478  THR A CA  
3424  C C   . THR A 480  ? 0.5524 0.5721 0.5383 -0.0047 0.0106  0.0041  478  THR A C   
3425  O O   . THR A 480  ? 0.7405 0.7636 0.7255 -0.0047 0.0113  0.0039  478  THR A O   
3426  C CB  . THR A 480  ? 0.4799 0.5099 0.4628 -0.0061 0.0100  0.0071  478  THR A CB  
3427  O OG1 . THR A 480  ? 0.5728 0.5987 0.5558 -0.0075 0.0105  0.0113  478  THR A OG1 
3428  C CG2 . THR A 480  ? 0.5178 0.5516 0.4997 -0.0064 0.0090  0.0076  478  THR A CG2 
3429  N N   . ALA A 497  ? 0.6463 0.5804 0.6584 0.0084  -0.0010 -0.0075 495  ALA A N   
3430  C CA  . ALA A 497  ? 0.5336 0.4622 0.5464 0.0076  -0.0015 -0.0042 495  ALA A CA  
3431  C C   . ALA A 497  ? 0.4286 0.3521 0.4448 0.0083  -0.0043 -0.0057 495  ALA A C   
3432  O O   . ALA A 497  ? 0.5011 0.4237 0.5196 0.0076  -0.0054 -0.0074 495  ALA A O   
3433  C CB  . ALA A 497  ? 0.4929 0.4209 0.5051 0.0050  0.0001  -0.0006 495  ALA A CB  
3434  N N   . ASN A 498  ? 0.4656 0.3855 0.4821 0.0097  -0.0056 -0.0051 496  ASN A N   
3435  C CA  . ASN A 498  ? 0.4962 0.4106 0.5162 0.0104  -0.0086 -0.0063 496  ASN A CA  
3436  C C   . ASN A 498  ? 0.4838 0.3936 0.5058 0.0078  -0.0091 -0.0032 496  ASN A C   
3437  O O   . ASN A 498  ? 0.5102 0.4155 0.5357 0.0079  -0.0117 -0.0044 496  ASN A O   
3438  C CB  . ASN A 498  ? 0.5627 0.4742 0.5824 0.0125  -0.0098 -0.0057 496  ASN A CB  
3439  N N   . SER A 499  ? 0.4826 0.3934 0.5027 0.0055  -0.0068 0.0008  497  SER A N   
3440  C CA  . SER A 499  ? 0.4617 0.3692 0.4836 0.0028  -0.0069 0.0040  497  SER A CA  
3441  C C   . SER A 499  ? 0.4753 0.3847 0.4991 0.0014  -0.0069 0.0020  497  SER A C   
3442  O O   . SER A 499  ? 0.4161 0.3226 0.4424 -0.0008 -0.0076 0.0038  497  SER A O   
3443  C CB  . SER A 499  ? 0.4358 0.3444 0.4550 0.0011  -0.0044 0.0087  497  SER A CB  
3444  O OG  . SER A 499  ? 0.4794 0.3937 0.4956 0.0013  -0.0019 0.0082  497  SER A OG  
3445  N N   . SER A 500  ? 0.4539 0.3685 0.4766 0.0025  -0.0062 -0.0014 498  SER A N   
3446  C CA  . SER A 500  ? 0.4113 0.3285 0.4351 0.0013  -0.0060 -0.0031 498  SER A CA  
3447  C C   . SER A 500  ? 0.4487 0.3629 0.4766 0.0015  -0.0089 -0.0064 498  SER A C   
3448  O O   . SER A 500  ? 0.4359 0.3482 0.4651 0.0038  -0.0110 -0.0095 498  SER A O   
3449  C CB  . SER A 500  ? 0.4327 0.3565 0.4540 0.0024  -0.0045 -0.0057 498  SER A CB  
3450  O OG  . SER A 500  ? 0.5391 0.4657 0.5571 0.0018  -0.0018 -0.0028 498  SER A OG  
3451  N N   . PHE A 501  ? 0.3907 0.3045 0.4208 -0.0007 -0.0092 -0.0060 499  PHE A N   
3452  C CA  . PHE A 501  ? 0.4258 0.3371 0.4600 -0.0006 -0.0121 -0.0094 499  PHE A CA  
3453  C C   . PHE A 501  ? 0.4539 0.3691 0.4877 0.0021  -0.0130 -0.0151 499  PHE A C   
3454  O O   . PHE A 501  ? 0.4698 0.3824 0.5064 0.0037  -0.0158 -0.0187 499  PHE A O   
3455  C CB  . PHE A 501  ? 0.3716 0.2833 0.4079 -0.0034 -0.0119 -0.0083 499  PHE A CB  
3456  C CG  . PHE A 501  ? 0.4118 0.3207 0.4525 -0.0035 -0.0150 -0.0119 499  PHE A CG  
3457  C CD1 . PHE A 501  ? 0.4015 0.3037 0.4461 -0.0048 -0.0174 -0.0105 499  PHE A CD1 
3458  C CD2 . PHE A 501  ? 0.4139 0.3272 0.4550 -0.0024 -0.0157 -0.0167 499  PHE A CD2 
3459  C CE1 . PHE A 501  ? 0.4274 0.3268 0.4765 -0.0050 -0.0205 -0.0139 499  PHE A CE1 
3460  C CE2 . PHE A 501  ? 0.4160 0.3270 0.4613 -0.0024 -0.0187 -0.0204 499  PHE A CE2 
3461  C CZ  . PHE A 501  ? 0.4519 0.3558 0.5014 -0.0037 -0.0212 -0.0191 499  PHE A CZ  
3462  N N   . VAL A 502  ? 0.4407 0.3624 0.4713 0.0025  -0.0108 -0.0158 500  VAL A N   
3463  C CA  . VAL A 502  ? 0.4982 0.4248 0.5282 0.0048  -0.0114 -0.0208 500  VAL A CA  
3464  C C   . VAL A 502  ? 0.4963 0.4223 0.5260 0.0077  -0.0126 -0.0232 500  VAL A C   
3465  O O   . VAL A 502  ? 0.6029 0.5306 0.6338 0.0098  -0.0144 -0.0282 500  VAL A O   
3466  C CB  . VAL A 502  ? 0.5487 0.4823 0.5751 0.0044  -0.0087 -0.0202 500  VAL A CB  
3467  N N   . HIS A 503  ? 0.4959 0.4197 0.5239 0.0079  -0.0116 -0.0200 501  HIS A N   
3468  C CA  . HIS A 503  ? 0.4513 0.3741 0.4793 0.0107  -0.0128 -0.0221 501  HIS A CA  
3469  C C   . HIS A 503  ? 0.5383 0.4542 0.5704 0.0114  -0.0161 -0.0233 501  HIS A C   
3470  O O   . HIS A 503  ? 0.5054 0.4211 0.5392 0.0141  -0.0184 -0.0278 501  HIS A O   
3471  C CB  . HIS A 503  ? 0.4948 0.4177 0.5197 0.0107  -0.0107 -0.0182 501  HIS A CB  
3472  C CG  . HIS A 503  ? 0.5803 0.5023 0.6052 0.0134  -0.0119 -0.0198 501  HIS A CG  
3473  N ND1 . HIS A 503  ? 0.5748 0.4902 0.6016 0.0140  -0.0139 -0.0185 501  HIS A ND1 
3474  C CD2 . HIS A 503  ? 0.5317 0.4586 0.5549 0.0158  -0.0115 -0.0227 501  HIS A CD2 
3475  C CE1 . HIS A 503  ? 0.5925 0.5088 0.6189 0.0168  -0.0147 -0.0205 501  HIS A CE1 
3476  N NE2 . HIS A 503  ? 0.5737 0.4971 0.5980 0.0178  -0.0132 -0.0232 501  HIS A NE2 
3477  N N   . ARG A 504  ? 0.4455 0.3555 0.4792 0.0091  -0.0166 -0.0194 502  ARG A N   
3478  C CA  . ARG A 504  ? 0.4762 0.3789 0.5140 0.0094  -0.0199 -0.0197 502  ARG A CA  
3479  C C   . ARG A 504  ? 0.5310 0.4328 0.5727 0.0100  -0.0227 -0.0246 502  ARG A C   
3480  O O   . ARG A 504  ? 0.5222 0.4196 0.5670 0.0119  -0.0259 -0.0275 502  ARG A O   
3481  C CB  . ARG A 504  ? 0.4672 0.3649 0.5057 0.0063  -0.0195 -0.0138 502  ARG A CB  
3482  C CG  . ARG A 504  ? 0.4739 0.3720 0.5087 0.0061  -0.0171 -0.0092 502  ARG A CG  
3483  C CD  . ARG A 504  ? 0.5305 0.4263 0.5651 0.0027  -0.0157 -0.0035 502  ARG A CD  
3484  N NE  . ARG A 504  ? 0.4781 0.3674 0.5169 0.0010  -0.0183 -0.0021 502  ARG A NE  
3485  C CZ  . ARG A 504  ? 0.5454 0.4286 0.5860 0.0015  -0.0205 -0.0002 502  ARG A CZ  
3486  N NH1 . ARG A 504  ? 0.5291 0.4119 0.5676 0.0038  -0.0206 0.0001  502  ARG A NH1 
3487  N NH2 . ARG A 504  ? 0.6126 0.4900 0.6571 -0.0006 -0.0227 0.0016  502  ARG A NH2 
3488  N N   . ILE A 505  ? 0.5035 0.4094 0.5452 0.0086  -0.0218 -0.0260 503  ILE A N   
3489  C CA  . ILE A 505  ? 0.5082 0.4137 0.5535 0.0092  -0.0246 -0.0311 503  ILE A CA  
3490  C C   . ILE A 505  ? 0.5357 0.4443 0.5810 0.0131  -0.0261 -0.0370 503  ILE A C   
3491  O O   . ILE A 505  ? 0.5308 0.4367 0.5800 0.0147  -0.0294 -0.0415 503  ILE A O   
3492  C CB  . ILE A 505  ? 0.5076 0.4179 0.5523 0.0072  -0.0231 -0.0313 503  ILE A CB  
3493  C CG1 . ILE A 505  ? 0.5288 0.4387 0.5775 0.0077  -0.0261 -0.0366 503  ILE A CG1 
3494  C CG2 . ILE A 505  ? 0.5224 0.4411 0.5625 0.0081  -0.0201 -0.0320 503  ILE A CG2 
3495  C CD1 . ILE A 505  ? 0.4796 0.3815 0.5332 0.0058  -0.0289 -0.0354 503  ILE A CD1 
3496  N N   . ASN A 506  ? 0.5068 0.4212 0.5481 0.0148  -0.0238 -0.0373 504  ASN A N   
3497  C CA  . ASN A 506  ? 0.5230 0.4416 0.5642 0.0184  -0.0249 -0.0428 504  ASN A CA  
3498  C C   . ASN A 506  ? 0.5884 0.5027 0.6304 0.0208  -0.0264 -0.0428 504  ASN A C   
3499  O O   . ASN A 506  ? 0.5846 0.5020 0.6269 0.0241  -0.0275 -0.0475 504  ASN A O   
3500  C CB  . ASN A 506  ? 0.5720 0.4997 0.6087 0.0189  -0.0217 -0.0432 504  ASN A CB  
3501  C CG  . ASN A 506  ? 0.5721 0.5051 0.6082 0.0176  -0.0209 -0.0449 504  ASN A CG  
3502  O OD1 . ASN A 506  ? 0.6112 0.5428 0.6505 0.0177  -0.0233 -0.0483 504  ASN A OD1 
3503  N ND2 . ASN A 506  ? 0.6091 0.5480 0.6414 0.0163  -0.0177 -0.0424 504  ASN A ND2 
3504  N N   . ASP A 507  ? 0.5640 0.4719 0.6064 0.0193  -0.0264 -0.0377 505  ASP A N   
3505  C CA  . ASP A 507  ? 0.5819 0.4855 0.6249 0.0214  -0.0279 -0.0371 505  ASP A CA  
3506  C C   . ASP A 507  ? 0.5930 0.4892 0.6412 0.0225  -0.0323 -0.0397 505  ASP A C   
3507  O O   . ASP A 507  ? 0.5396 0.4295 0.5903 0.0199  -0.0334 -0.0365 505  ASP A O   
3508  C CB  . ASP A 507  ? 0.5847 0.4852 0.6254 0.0193  -0.0260 -0.0303 505  ASP A CB  
3509  C CG  . ASP A 507  ? 0.6244 0.5225 0.6648 0.0217  -0.0269 -0.0297 505  ASP A CG  
3510  O OD1 . ASP A 507  ? 0.6089 0.5036 0.6525 0.0244  -0.0302 -0.0332 505  ASP A OD1 
3511  O OD2 . ASP A 507  ? 0.5870 0.4865 0.6239 0.0210  -0.0245 -0.0257 505  ASP A OD2 
3512  N N   . PRO A 508  ? 0.6393 0.5359 0.6895 0.0263  -0.0348 -0.0452 506  PRO A N   
3513  C CA  . PRO A 508  ? 0.5965 0.4857 0.6522 0.0275  -0.0394 -0.0481 506  PRO A CA  
3514  C C   . PRO A 508  ? 0.5789 0.4588 0.6364 0.0265  -0.0411 -0.0430 506  PRO A C   
3515  O O   . PRO A 508  ? 0.6344 0.5069 0.6965 0.0256  -0.0444 -0.0431 506  PRO A O   
3516  C CB  . PRO A 508  ? 0.6353 0.5283 0.6921 0.0321  -0.0412 -0.0550 506  PRO A CB  
3517  C CG  . PRO A 508  ? 0.6725 0.5761 0.7245 0.0328  -0.0375 -0.0562 506  PRO A CG  
3518  C CD  . PRO A 508  ? 0.6060 0.5100 0.6540 0.0296  -0.0338 -0.0491 506  PRO A CD  
3519  N N   . LYS A 509  ? 0.5391 0.4194 0.5934 0.0264  -0.0391 -0.0386 507  LYS A N   
3520  C CA  . LYS A 509  ? 0.6084 0.4804 0.6638 0.0254  -0.0405 -0.0334 507  LYS A CA  
3521  C C   . LYS A 509  ? 0.6351 0.5033 0.6905 0.0208  -0.0394 -0.0272 507  LYS A C   
3522  O O   . LYS A 509  ? 0.6332 0.4946 0.6898 0.0195  -0.0406 -0.0225 507  LYS A O   
3523  C CB  . LYS A 509  ? 0.6592 0.5335 0.7108 0.0269  -0.0387 -0.0308 507  LYS A CB  
3524  N N   . VAL A 510  ? 0.6160 0.4886 0.6702 0.0183  -0.0370 -0.0271 508  VAL A N   
3525  C CA  . VAL A 510  ? 0.5580 0.4279 0.6125 0.0139  -0.0358 -0.0218 508  VAL A CA  
3526  C C   . VAL A 510  ? 0.5322 0.3980 0.5919 0.0127  -0.0389 -0.0244 508  VAL A C   
3527  O O   . VAL A 510  ? 0.5573 0.4274 0.6177 0.0134  -0.0390 -0.0293 508  VAL A O   
3528  C CB  . VAL A 510  ? 0.5607 0.4381 0.6109 0.0119  -0.0314 -0.0197 508  VAL A CB  
3529  C CG1 . VAL A 510  ? 0.5052 0.3802 0.5561 0.0076  -0.0303 -0.0146 508  VAL A CG1 
3530  C CG2 . VAL A 510  ? 0.5130 0.3943 0.5584 0.0130  -0.0286 -0.0172 508  VAL A CG2 
3531  N N   . SER A 511  ? 0.4885 0.3461 0.5519 0.0109  -0.0415 -0.0209 509  SER A N   
3532  C CA  . SER A 511  ? 0.5077 0.3606 0.5764 0.0095  -0.0446 -0.0231 509  SER A CA  
3533  C C   . SER A 511  ? 0.5281 0.3843 0.5964 0.0055  -0.0422 -0.0209 509  SER A C   
3534  O O   . SER A 511  ? 0.5004 0.3611 0.5646 0.0036  -0.0383 -0.0166 509  SER A O   
3535  C CB  . SER A 511  ? 0.5616 0.4044 0.6346 0.0084  -0.0483 -0.0197 509  SER A CB  
3536  O OG  . SER A 511  ? 0.4959 0.3370 0.5672 0.0048  -0.0461 -0.0119 509  SER A OG  
3537  N N   . ILE A 512  ? 0.5012 0.3553 0.5740 0.0044  -0.0447 -0.0240 510  ILE A N   
3538  C CA  . ILE A 512  ? 0.5244 0.3807 0.5978 0.0005  -0.0431 -0.0218 510  ILE A CA  
3539  C C   . ILE A 512  ? 0.5340 0.3857 0.6081 -0.0034 -0.0424 -0.0140 510  ILE A C   
3540  O O   . ILE A 512  ? 0.4809 0.3365 0.5525 -0.0063 -0.0390 -0.0100 510  ILE A O   
3541  C CB  . ILE A 512  ? 0.4978 0.3525 0.5764 0.0004  -0.0464 -0.0272 510  ILE A CB  
3542  C CG1 . ILE A 512  ? 0.4496 0.3104 0.5268 0.0044  -0.0467 -0.0349 510  ILE A CG1 
3543  C CG2 . ILE A 512  ? 0.4993 0.3560 0.5789 -0.0038 -0.0450 -0.0248 510  ILE A CG2 
3544  C CD1 . ILE A 512  ? 0.5031 0.3645 0.5843 0.0043  -0.0492 -0.0405 510  ILE A CD1 
3545  N N   . ASP A 513  ? 0.5275 0.3709 0.6047 -0.0035 -0.0454 -0.0117 511  ASP A N   
3546  C CA  . ASP A 513  ? 0.5265 0.3656 0.6041 -0.0072 -0.0448 -0.0039 511  ASP A CA  
3547  C C   . ASP A 513  ? 0.5131 0.3577 0.5845 -0.0077 -0.0402 0.0009  511  ASP A C   
3548  O O   . ASP A 513  ? 0.5211 0.3670 0.5915 -0.0113 -0.0379 0.0063  511  ASP A O   
3549  C CB  . ASP A 513  ? 0.5500 0.3798 0.6310 -0.0063 -0.0489 -0.0023 511  ASP A CB  
3550  C CG  . ASP A 513  ? 0.6746 0.4976 0.7626 -0.0071 -0.0536 -0.0053 511  ASP A CG  
3551  O OD1 . ASP A 513  ? 0.6765 0.5004 0.7671 -0.0102 -0.0535 -0.0053 511  ASP A OD1 
3552  O OD2 . ASP A 513  ? 0.7207 0.5373 0.8118 -0.0044 -0.0576 -0.0078 511  ASP A OD2 
3553  N N   . GLU A 514  ? 0.4769 0.3249 0.5443 -0.0041 -0.0390 -0.0012 512  GLU A N   
3554  C CA  . GLU A 514  ? 0.4964 0.3499 0.5580 -0.0043 -0.0347 0.0026  512  GLU A CA  
3555  C C   . GLU A 514  ? 0.4772 0.3382 0.5364 -0.0060 -0.0312 0.0021  512  GLU A C   
3556  O O   . GLU A 514  ? 0.5170 0.3812 0.5733 -0.0082 -0.0280 0.0069  512  GLU A O   
3557  C CB  . GLU A 514  ? 0.4982 0.3541 0.5563 -0.0001 -0.0343 -0.0002 512  GLU A CB  
3558  C CG  . GLU A 514  ? 0.6150 0.4640 0.6750 0.0020  -0.0376 0.0004  512  GLU A CG  
3559  C CD  . GLU A 514  ? 0.6393 0.4916 0.6962 0.0062  -0.0371 -0.0029 512  GLU A CD  
3560  O OE1 . GLU A 514  ? 0.7515 0.6088 0.8035 0.0064  -0.0337 -0.0005 512  GLU A OE1 
3561  O OE2 . GLU A 514  ? 0.6731 0.5231 0.7325 0.0094  -0.0402 -0.0080 512  GLU A OE2 
3562  N N   . LEU A 515  ? 0.5139 0.3781 0.5743 -0.0049 -0.0318 -0.0036 513  LEU A N   
3563  C CA  . LEU A 515  ? 0.4689 0.3406 0.5269 -0.0060 -0.0287 -0.0044 513  LEU A CA  
3564  C C   . LEU A 515  ? 0.4497 0.3209 0.5103 -0.0102 -0.0282 -0.0011 513  LEU A C   
3565  O O   . LEU A 515  ? 0.4102 0.2871 0.4683 -0.0118 -0.0251 0.0005  513  LEU A O   
3566  C CB  . LEU A 515  ? 0.4775 0.3531 0.5359 -0.0034 -0.0296 -0.0115 513  LEU A CB  
3567  C CG  . LEU A 515  ? 0.4979 0.3771 0.5531 0.0006  -0.0291 -0.0152 513  LEU A CG  
3568  C CD1 . LEU A 515  ? 0.4888 0.3714 0.5454 0.0028  -0.0307 -0.0222 513  LEU A CD1 
3569  C CD2 . LEU A 515  ? 0.4482 0.3337 0.4978 0.0005  -0.0249 -0.0125 513  LEU A CD2 
3570  N N   . ILE A 516  ? 0.4423 0.3068 0.5079 -0.0121 -0.0314 -0.0001 514  ILE A N   
3571  C CA  . ILE A 516  ? 0.4488 0.3128 0.5174 -0.0163 -0.0311 0.0030  514  ILE A CA  
3572  C C   . ILE A 516  ? 0.4538 0.3147 0.5224 -0.0193 -0.0302 0.0104  514  ILE A C   
3573  O O   . ILE A 516  ? 0.4652 0.3249 0.5368 -0.0230 -0.0304 0.0137  514  ILE A O   
3574  C CB  . ILE A 516  ? 0.4510 0.3104 0.5258 -0.0170 -0.0352 -0.0007 514  ILE A CB  
3575  C CG1 . ILE A 516  ? 0.4428 0.2931 0.5214 -0.0166 -0.0391 0.0002  514  ILE A CG1 
3576  C CG2 . ILE A 516  ? 0.4086 0.2722 0.4831 -0.0139 -0.0359 -0.0083 514  ILE A CG2 
3577  C CD1 . ILE A 516  ? 0.4900 0.3347 0.5754 -0.0182 -0.0433 -0.0021 514  ILE A CD1 
3578  N N   . ALA A 517  ? 0.4434 0.3033 0.5085 -0.0177 -0.0293 0.0132  515  ALA A N   
3579  C CA  . ALA A 517  ? 0.4870 0.3452 0.5510 -0.0202 -0.0280 0.0203  515  ALA A CA  
3580  C C   . ALA A 517  ? 0.4651 0.3299 0.5269 -0.0230 -0.0240 0.0235  515  ALA A C   
3581  O O   . ALA A 517  ? 0.4138 0.2852 0.4721 -0.0216 -0.0213 0.0212  515  ALA A O   
3582  C CB  . ALA A 517  ? 0.4804 0.3379 0.5404 -0.0175 -0.0273 0.0219  515  ALA A CB  
3583  N N   . ASP A 518  ? 0.4573 0.3206 0.5212 -0.0268 -0.0238 0.0290  516  ASP A N   
3584  C CA  . ASP A 518  ? 0.4409 0.3104 0.5035 -0.0297 -0.0204 0.0322  516  ASP A CA  
3585  C C   . ASP A 518  ? 0.3910 0.2645 0.4480 -0.0290 -0.0170 0.0361  516  ASP A C   
3586  O O   . ASP A 518  ? 0.3609 0.2316 0.4175 -0.0303 -0.0171 0.0412  516  ASP A O   
3587  C CB  . ASP A 518  ? 0.4447 0.3113 0.5122 -0.0342 -0.0216 0.0363  516  ASP A CB  
3588  C CG  . ASP A 518  ? 0.4515 0.3249 0.5185 -0.0371 -0.0184 0.0390  516  ASP A CG  
3589  O OD1 . ASP A 518  ? 0.4318 0.3119 0.4946 -0.0356 -0.0152 0.0376  516  ASP A OD1 
3590  O OD2 . ASP A 518  ? 0.4822 0.3543 0.5531 -0.0410 -0.0190 0.0426  516  ASP A OD2 
3591  N N   . PRO A 519  ? 0.4018 0.2818 0.4546 -0.0272 -0.0140 0.0340  517  PRO A N   
3592  C CA  . PRO A 519  ? 0.3929 0.2765 0.4405 -0.0264 -0.0110 0.0373  517  PRO A CA  
3593  C C   . PRO A 519  ? 0.3743 0.2598 0.4220 -0.0299 -0.0092 0.0434  517  PRO A C   
3594  O O   . PRO A 519  ? 0.3604 0.2462 0.4050 -0.0297 -0.0080 0.0473  517  PRO A O   
3595  C CB  . PRO A 519  ? 0.3908 0.2810 0.4350 -0.0244 -0.0085 0.0335  517  PRO A CB  
3596  C CG  . PRO A 519  ? 0.3648 0.2565 0.4125 -0.0257 -0.0091 0.0306  517  PRO A CG  
3597  C CD  . PRO A 519  ? 0.4141 0.2989 0.4668 -0.0265 -0.0131 0.0293  517  PRO A CD  
3598  N N   . VAL A 520  ? 0.3875 0.2746 0.4386 -0.0331 -0.0090 0.0444  518  VAL A N   
3599  C CA  . VAL A 520  ? 0.4065 0.2962 0.4581 -0.0366 -0.0072 0.0503  518  VAL A CA  
3600  C C   . VAL A 520  ? 0.4280 0.3119 0.4809 -0.0382 -0.0091 0.0552  518  VAL A C   
3601  O O   . VAL A 520  ? 0.4086 0.2947 0.4587 -0.0390 -0.0073 0.0600  518  VAL A O   
3602  C CB  . VAL A 520  ? 0.4227 0.3148 0.4788 -0.0398 -0.0072 0.0499  518  VAL A CB  
3603  C CG1 . VAL A 520  ? 0.4193 0.3150 0.4760 -0.0436 -0.0052 0.0560  518  VAL A CG1 
3604  C CG2 . VAL A 520  ? 0.3704 0.2680 0.4251 -0.0380 -0.0056 0.0450  518  VAL A CG2 
3605  N N   . GLU A 521  ? 0.4356 0.3121 0.4928 -0.0385 -0.0129 0.0540  519  GLU A N   
3606  C CA  . GLU A 521  ? 0.4300 0.3003 0.4890 -0.0401 -0.0152 0.0589  519  GLU A CA  
3607  C C   . GLU A 521  ? 0.4568 0.3242 0.5119 -0.0367 -0.0158 0.0591  519  GLU A C   
3608  O O   . GLU A 521  ? 0.4397 0.3044 0.4942 -0.0378 -0.0163 0.0644  519  GLU A O   
3609  C CB  . GLU A 521  ? 0.4115 0.2745 0.4770 -0.0417 -0.0194 0.0576  519  GLU A CB  
3610  C CG  . GLU A 521  ? 0.4861 0.3515 0.5560 -0.0456 -0.0191 0.0582  519  GLU A CG  
3611  C CD  . GLU A 521  ? 0.5308 0.4003 0.6004 -0.0497 -0.0166 0.0652  519  GLU A CD  
3612  O OE1 . GLU A 521  ? 0.5334 0.4009 0.6013 -0.0504 -0.0166 0.0705  519  GLU A OE1 
3613  O OE2 . GLU A 521  ? 0.5762 0.4513 0.6474 -0.0521 -0.0147 0.0654  519  GLU A OE2 
3614  N N   . VAL A 522  ? 0.4105 0.2786 0.4632 -0.0326 -0.0158 0.0535  520  VAL A N   
3615  C CA  . VAL A 522  ? 0.4026 0.2695 0.4512 -0.0293 -0.0159 0.0536  520  VAL A CA  
3616  C C   . VAL A 522  ? 0.4573 0.3303 0.5009 -0.0297 -0.0122 0.0577  520  VAL A C   
3617  O O   . VAL A 522  ? 0.4359 0.3071 0.4773 -0.0294 -0.0124 0.0616  520  VAL A O   
3618  C CB  . VAL A 522  ? 0.4207 0.2883 0.4678 -0.0251 -0.0163 0.0467  520  VAL A CB  
3619  C CG1 . VAL A 522  ? 0.3805 0.2477 0.4234 -0.0218 -0.0161 0.0469  520  VAL A CG1 
3620  C CG2 . VAL A 522  ? 0.4394 0.3013 0.4915 -0.0245 -0.0202 0.0424  520  VAL A CG2 
3621  N N   . VAL A 523  ? 0.3638 0.2439 0.4054 -0.0304 -0.0089 0.0569  521  VAL A N   
3622  C CA  . VAL A 523  ? 0.3793 0.2656 0.4163 -0.0306 -0.0054 0.0602  521  VAL A CA  
3623  C C   . VAL A 523  ? 0.4090 0.2952 0.4469 -0.0342 -0.0051 0.0671  521  VAL A C   
3624  O O   . VAL A 523  ? 0.4172 0.3049 0.4516 -0.0339 -0.0040 0.0709  521  VAL A O   
3625  C CB  . VAL A 523  ? 0.3631 0.2568 0.3984 -0.0304 -0.0023 0.0575  521  VAL A CB  
3626  C CG1 . VAL A 523  ? 0.3646 0.2647 0.3963 -0.0313 0.0011  0.0614  521  VAL A CG1 
3627  C CG2 . VAL A 523  ? 0.3746 0.2692 0.4075 -0.0265 -0.0022 0.0518  521  VAL A CG2 
3628  N N   . ARG A 524  ? 0.4167 0.3015 0.4594 -0.0377 -0.0061 0.0688  522  ARG A N   
3629  C CA  . ARG A 524  ? 0.4612 0.3465 0.5052 -0.0416 -0.0057 0.0757  522  ARG A CA  
3630  C C   . ARG A 524  ? 0.5264 0.4057 0.5698 -0.0413 -0.0080 0.0797  522  ARG A C   
3631  O O   . ARG A 524  ? 0.5331 0.4146 0.5745 -0.0432 -0.0068 0.0856  522  ARG A O   
3632  C CB  . ARG A 524  ? 0.4321 0.3157 0.4821 -0.0454 -0.0071 0.0765  522  ARG A CB  
3633  C CG  . ARG A 524  ? 0.4732 0.3596 0.5246 -0.0500 -0.0059 0.0834  522  ARG A CG  
3634  C CD  . ARG A 524  ? 0.4750 0.3571 0.5332 -0.0538 -0.0085 0.0847  522  ARG A CD  
3635  N NE  . ARG A 524  ? 0.5209 0.4047 0.5819 -0.0536 -0.0085 0.0792  522  ARG A NE  
3636  C CZ  . ARG A 524  ? 0.4725 0.3639 0.5340 -0.0554 -0.0057 0.0789  522  ARG A CZ  
3637  N NH1 . ARG A 524  ? 0.5000 0.3983 0.5591 -0.0572 -0.0025 0.0835  522  ARG A NH1 
3638  N NH2 . ARG A 524  ? 0.4721 0.3642 0.5364 -0.0552 -0.0063 0.0739  522  ARG A NH2 
3639  N N   . ALA A 525  ? 0.4923 0.3643 0.5372 -0.0389 -0.0114 0.0767  523  ALA A N   
3640  C CA  . ALA A 525  ? 0.5282 0.3936 0.5733 -0.0385 -0.0142 0.0802  523  ALA A CA  
3641  C C   . ALA A 525  ? 0.5196 0.3865 0.5589 -0.0349 -0.0132 0.0801  523  ALA A C   
3642  O O   . ALA A 525  ? 0.4933 0.3553 0.5322 -0.0343 -0.0154 0.0833  523  ALA A O   
3643  C CB  . ALA A 525  ? 0.4872 0.3437 0.5371 -0.0374 -0.0187 0.0767  523  ALA A CB  
3644  N N   . MET A 526  ? 0.4580 0.3315 0.4931 -0.0325 -0.0101 0.0767  524  MET A N   
3645  C CA  . MET A 526  ? 0.5345 0.4095 0.5645 -0.0292 -0.0093 0.0763  524  MET A CA  
3646  C C   . MET A 526  ? 0.5391 0.4174 0.5658 -0.0308 -0.0076 0.0829  524  MET A C   
3647  O O   . MET A 526  ? 0.5012 0.3836 0.5285 -0.0343 -0.0057 0.0868  524  MET A O   
3648  C CB  . MET A 526  ? 0.5233 0.4044 0.5501 -0.0265 -0.0066 0.0710  524  MET A CB  
3649  C CG  . MET A 526  ? 0.5110 0.3893 0.5403 -0.0244 -0.0083 0.0646  524  MET A CG  
3650  S SD  . MET A 526  ? 0.6311 0.5162 0.6564 -0.0214 -0.0053 0.0590  524  MET A SD  
3651  C CE  . MET A 526  ? 0.6044 0.4851 0.6330 -0.0190 -0.0082 0.0523  524  MET A CE  
3652  N N   . PRO A 527  ? 0.5089 0.3860 0.5322 -0.0284 -0.0083 0.0843  525  PRO A N   
3653  C CA  . PRO A 527  ? 0.5354 0.4158 0.5552 -0.0299 -0.0069 0.0907  525  PRO A CA  
3654  C C   . PRO A 527  ? 0.5613 0.4514 0.5776 -0.0307 -0.0025 0.0911  525  PRO A C   
3655  O O   . PRO A 527  ? 0.5552 0.4491 0.5710 -0.0337 -0.0010 0.0965  525  PRO A O   
3656  C CB  . PRO A 527  ? 0.5424 0.4203 0.5590 -0.0263 -0.0084 0.0903  525  PRO A CB  
3657  C CG  . PRO A 527  ? 0.5571 0.4329 0.5744 -0.0227 -0.0094 0.0830  525  PRO A CG  
3658  C CD  . PRO A 527  ? 0.5561 0.4288 0.5786 -0.0243 -0.0105 0.0802  525  PRO A CD  
3659  N N   . VAL A 528  ? 0.5298 0.4241 0.5438 -0.0281 -0.0006 0.0857  526  VAL A N   
3660  C CA  . VAL A 528  ? 0.4638 0.3668 0.4749 -0.0285 0.0033  0.0853  526  VAL A CA  
3661  C C   . VAL A 528  ? 0.4486 0.3530 0.4622 -0.0284 0.0041  0.0800  526  VAL A C   
3662  O O   . VAL A 528  ? 0.3979 0.3012 0.4110 -0.0255 0.0037  0.0747  526  VAL A O   
3663  C CB  . VAL A 528  ? 0.4798 0.3871 0.4854 -0.0254 0.0050  0.0840  526  VAL A CB  
3664  C CG1 . VAL A 528  ? 0.4681 0.3842 0.4713 -0.0256 0.0087  0.0828  526  VAL A CG1 
3665  C CG2 . VAL A 528  ? 0.5416 0.4482 0.5446 -0.0255 0.0041  0.0893  526  VAL A CG2 
3666  N N   . VAL A 529  ? 0.4063 0.3133 0.4228 -0.0316 0.0052  0.0816  527  VAL A N   
3667  C CA  . VAL A 529  ? 0.4130 0.3213 0.4321 -0.0318 0.0058  0.0770  527  VAL A CA  
3668  C C   . VAL A 529  ? 0.3993 0.3140 0.4146 -0.0292 0.0086  0.0733  527  VAL A C   
3669  O O   . VAL A 529  ? 0.3918 0.3129 0.4040 -0.0295 0.0112  0.0753  527  VAL A O   
3670  C CB  . VAL A 529  ? 0.3721 0.2826 0.3951 -0.0359 0.0065  0.0799  527  VAL A CB  
3671  C CG1 . VAL A 529  ? 0.4091 0.3223 0.4341 -0.0358 0.0074  0.0751  527  VAL A CG1 
3672  C CG2 . VAL A 529  ? 0.4653 0.3685 0.4927 -0.0384 0.0032  0.0831  527  VAL A CG2 
3673  N N   . GLY A 530  ? 0.3529 0.2660 0.3684 -0.0267 0.0079  0.0678  528  GLY A N   
3674  C CA  . GLY A 530  ? 0.3324 0.2508 0.3447 -0.0244 0.0102  0.0642  528  GLY A CA  
3675  C C   . GLY A 530  ? 0.3550 0.2741 0.3628 -0.0215 0.0106  0.0635  528  GLY A C   
3676  O O   . GLY A 530  ? 0.2952 0.2190 0.3002 -0.0198 0.0126  0.0611  528  GLY A O   
3677  N N   . ALA A 531  ? 0.3711 0.2856 0.3782 -0.0207 0.0086  0.0655  529  ALA A N   
3678  C CA  . ALA A 531  ? 0.3532 0.2683 0.3563 -0.0177 0.0087  0.0644  529  ALA A CA  
3679  C C   . ALA A 531  ? 0.3629 0.2785 0.3653 -0.0150 0.0088  0.0586  529  ALA A C   
3680  O O   . ALA A 531  ? 0.3298 0.2421 0.3351 -0.0147 0.0073  0.0555  529  ALA A O   
3681  C CB  . ALA A 531  ? 0.3622 0.2714 0.3655 -0.0170 0.0059  0.0667  529  ALA A CB  
3682  N N   . LYS A 532  ? 0.3253 0.2453 0.3240 -0.0131 0.0106  0.0572  530  LYS A N   
3683  C CA  . LYS A 532  ? 0.3662 0.2868 0.3639 -0.0105 0.0107  0.0523  530  LYS A CA  
3684  C C   . LYS A 532  ? 0.3545 0.2699 0.3531 -0.0086 0.0081  0.0504  530  LYS A C   
3685  O O   . LYS A 532  ? 0.3440 0.2558 0.3425 -0.0085 0.0064  0.0530  530  LYS A O   
3686  C CB  . LYS A 532  ? 0.3877 0.3134 0.3813 -0.0089 0.0127  0.0518  530  LYS A CB  
3687  C CG  . LYS A 532  ? 0.4651 0.3912 0.4574 -0.0063 0.0126  0.0473  530  LYS A CG  
3688  C CD  . LYS A 532  ? 0.3796 0.3100 0.3680 -0.0048 0.0142  0.0470  530  LYS A CD  
3689  C CE  . LYS A 532  ? 0.4296 0.3592 0.4157 -0.0040 0.0133  0.0497  530  LYS A CE  
3690  N NZ  . LYS A 532  ? 0.3957 0.3208 0.3822 -0.0022 0.0110  0.0482  530  LYS A NZ  
3691  N N   . HIS A 533  ? 0.3112 0.2262 0.3106 -0.0071 0.0077  0.0459  531  HIS A N   
3692  C CA  . HIS A 533  ? 0.3435 0.2547 0.3435 -0.0049 0.0054  0.0434  531  HIS A CA  
3693  C C   . HIS A 533  ? 0.3490 0.2605 0.3458 -0.0030 0.0052  0.0445  531  HIS A C   
3694  O O   . HIS A 533  ? 0.3661 0.2820 0.3598 -0.0023 0.0071  0.0444  531  HIS A O   
3695  C CB  . HIS A 533  ? 0.3529 0.2656 0.3536 -0.0035 0.0056  0.0384  531  HIS A CB  
3696  C CG  . HIS A 533  ? 0.4099 0.3189 0.4122 -0.0016 0.0031  0.0355  531  HIS A CG  
3697  N ND1 . HIS A 533  ? 0.4271 0.3353 0.4278 0.0008  0.0022  0.0347  531  HIS A ND1 
3698  C CD2 . HIS A 533  ? 0.4694 0.3756 0.4751 -0.0015 0.0014  0.0329  531  HIS A CD2 
3699  C CE1 . HIS A 533  ? 0.4257 0.3309 0.4286 0.0023  -0.0001 0.0318  531  HIS A CE1 
3700  N NE2 . HIS A 533  ? 0.4835 0.3874 0.4894 0.0010  -0.0006 0.0306  531  HIS A NE2 
3701  N N   . ASP A 534  ? 0.3673 0.2742 0.3651 -0.0020 0.0027  0.0454  532  ASP A N   
3702  C CA  . ASP A 534  ? 0.4325 0.3392 0.4276 -0.0002 0.0020  0.0467  532  ASP A CA  
3703  C C   . ASP A 534  ? 0.3916 0.3015 0.3844 0.0023  0.0027  0.0429  532  ASP A C   
3704  O O   . ASP A 534  ? 0.3982 0.3103 0.3880 0.0035  0.0032  0.0440  532  ASP A O   
3705  C CB  . ASP A 534  ? 0.4646 0.3653 0.4618 0.0007  -0.0012 0.0477  532  ASP A CB  
3706  C CG  . ASP A 534  ? 0.6226 0.5202 0.6208 -0.0016 -0.0020 0.0531  532  ASP A CG  
3707  O OD1 . ASP A 534  ? 0.6502 0.5513 0.6469 -0.0038 0.0001  0.0561  532  ASP A OD1 
3708  O OD2 . ASP A 534  ? 0.7593 0.6513 0.7598 -0.0013 -0.0049 0.0542  532  ASP A OD2 
3709  N N   . ARG A 535  ? 0.3458 0.2563 0.3402 0.0032  0.0027  0.0386  533  ARG A N   
3710  C CA  . ARG A 535  ? 0.3502 0.2632 0.3431 0.0055  0.0030  0.0351  533  ARG A CA  
3711  C C   . ARG A 535  ? 0.3791 0.2972 0.3703 0.0050  0.0055  0.0335  533  ARG A C   
3712  O O   . ARG A 535  ? 0.4050 0.3255 0.3953 0.0065  0.0059  0.0306  533  ARG A O   
3713  C CB  . ARG A 535  ? 0.4234 0.3341 0.4190 0.0070  0.0010  0.0313  533  ARG A CB  
3714  N N   . ILE A 536  ? 0.3346 0.2546 0.3255 0.0030  0.0072  0.0355  534  ILE A N   
3715  C CA  . ILE A 536  ? 0.3618 0.2863 0.3512 0.0026  0.0095  0.0341  534  ILE A CA  
3716  C C   . ILE A 536  ? 0.3337 0.2611 0.3203 0.0022  0.0110  0.0368  534  ILE A C   
3717  O O   . ILE A 536  ? 0.3488 0.2758 0.3355 0.0007  0.0113  0.0402  534  ILE A O   
3718  C CB  . ILE A 536  ? 0.3532 0.2782 0.3449 0.0009  0.0103  0.0333  534  ILE A CB  
3719  C CG1 . ILE A 536  ? 0.3696 0.2926 0.3638 0.0016  0.0088  0.0300  534  ILE A CG1 
3720  C CG2 . ILE A 536  ? 0.3681 0.2976 0.3583 0.0006  0.0124  0.0323  534  ILE A CG2 
3721  C CD1 . ILE A 536  ? 0.3910 0.3135 0.3878 -0.0001 0.0089  0.0296  534  ILE A CD1 
3722  N N   . ALA A 537  ? 0.2877 0.2181 0.2719 0.0036  0.0118  0.0354  535  ALA A N   
3723  C CA  . ALA A 537  ? 0.3021 0.2357 0.2835 0.0035  0.0131  0.0374  535  ALA A CA  
3724  C C   . ALA A 537  ? 0.2992 0.2362 0.2806 0.0022  0.0152  0.0374  535  ALA A C   
3725  O O   . ALA A 537  ? 0.2791 0.2172 0.2615 0.0022  0.0158  0.0348  535  ALA A O   
3726  C CB  . ALA A 537  ? 0.3192 0.2548 0.2983 0.0055  0.0131  0.0355  535  ALA A CB  
3727  N N   . LEU A 538  ? 0.2729 0.2118 0.2532 0.0011  0.0162  0.0405  536  LEU A N   
3728  C CA  . LEU A 538  ? 0.2688 0.2121 0.2484 0.0005  0.0182  0.0402  536  LEU A CA  
3729  C C   . LEU A 538  ? 0.2910 0.2368 0.2686 0.0023  0.0187  0.0374  536  LEU A C   
3730  O O   . LEU A 538  ? 0.3031 0.2484 0.2791 0.0037  0.0178  0.0369  536  LEU A O   
3731  C CB  . LEU A 538  ? 0.2775 0.2235 0.2558 -0.0006 0.0193  0.0438  536  LEU A CB  
3732  C CG  . LEU A 538  ? 0.2901 0.2342 0.2706 -0.0029 0.0191  0.0469  536  LEU A CG  
3733  C CD1 . LEU A 538  ? 0.3880 0.3349 0.3666 -0.0039 0.0199  0.0510  536  LEU A CD1 
3734  C CD2 . LEU A 538  ? 0.3390 0.2842 0.3221 -0.0043 0.0200  0.0456  536  LEU A CD2 
3735  N N   . PRO A 539  ? 0.2668 0.2154 0.2448 0.0022  0.0199  0.0355  537  PRO A N   
3736  C CA  . PRO A 539  ? 0.2695 0.2203 0.2459 0.0038  0.0202  0.0328  537  PRO A CA  
3737  C C   . PRO A 539  ? 0.2321 0.1852 0.2055 0.0049  0.0203  0.0338  537  PRO A C   
3738  O O   . PRO A 539  ? 0.2899 0.2430 0.2620 0.0063  0.0196  0.0321  537  PRO A O   
3739  C CB  . PRO A 539  ? 0.2567 0.2101 0.2341 0.0032  0.0215  0.0316  537  PRO A CB  
3740  C CG  . PRO A 539  ? 0.2355 0.1869 0.2157 0.0016  0.0214  0.0322  537  PRO A CG  
3741  C CD  . PRO A 539  ? 0.2581 0.2076 0.2384 0.0007  0.0209  0.0353  537  PRO A CD  
3742  N N   . ALA A 540  ? 0.2389 0.1943 0.2110 0.0042  0.0212  0.0366  538  ALA A N   
3743  C CA  . ALA A 540  ? 0.2726 0.2309 0.2415 0.0053  0.0214  0.0376  538  ALA A CA  
3744  C C   . ALA A 540  ? 0.3189 0.2745 0.2867 0.0062  0.0197  0.0385  538  ALA A C   
3745  O O   . ALA A 540  ? 0.3416 0.2993 0.3068 0.0076  0.0194  0.0383  538  ALA A O   
3746  C CB  . ALA A 540  ? 0.3502 0.3119 0.3181 0.0042  0.0226  0.0408  538  ALA A CB  
3747  N N   . GLU A 541  ? 0.2900 0.2410 0.2597 0.0056  0.0184  0.0394  539  GLU A N   
3748  C CA  . GLU A 541  ? 0.3314 0.2796 0.3005 0.0065  0.0166  0.0405  539  GLU A CA  
3749  C C   . GLU A 541  ? 0.3424 0.2881 0.3129 0.0077  0.0153  0.0374  539  GLU A C   
3750  O O   . GLU A 541  ? 0.3033 0.2459 0.2742 0.0085  0.0136  0.0378  539  GLU A O   
3751  C CB  . GLU A 541  ? 0.3336 0.2787 0.3039 0.0050  0.0159  0.0442  539  GLU A CB  
3752  C CG  . GLU A 541  ? 0.4225 0.3709 0.3916 0.0035  0.0174  0.0477  539  GLU A CG  
3753  C CD  . GLU A 541  ? 0.5503 0.4956 0.5212 0.0016  0.0167  0.0515  539  GLU A CD  
3754  O OE1 . GLU A 541  ? 0.5772 0.5174 0.5503 0.0016  0.0149  0.0514  539  GLU A OE1 
3755  O OE2 . GLU A 541  ? 0.5900 0.5380 0.5602 0.0000  0.0179  0.0547  539  GLU A OE2 
3756  N N   . LEU A 542  ? 0.2943 0.2414 0.2654 0.0080  0.0160  0.0341  540  LEU A N   
3757  C CA  . LEU A 542  ? 0.3380 0.2836 0.3105 0.0089  0.0150  0.0312  540  LEU A CA  
3758  C C   . LEU A 542  ? 0.3332 0.2785 0.3042 0.0106  0.0136  0.0307  540  LEU A C   
3759  O O   . LEU A 542  ? 0.3468 0.2901 0.3192 0.0114  0.0124  0.0293  540  LEU A O   
3760  C CB  . LEU A 542  ? 0.3022 0.2500 0.2751 0.0089  0.0160  0.0283  540  LEU A CB  
3761  C CG  . LEU A 542  ? 0.3800 0.3267 0.3554 0.0078  0.0164  0.0269  540  LEU A CG  
3762  C CD1 . LEU A 542  ? 0.2930 0.2415 0.2687 0.0083  0.0166  0.0240  540  LEU A CD1 
3763  C CD2 . LEU A 542  ? 0.3135 0.2569 0.2909 0.0077  0.0152  0.0269  540  LEU A CD2 
3764  N N   . PHE A 543  ? 0.2937 0.2416 0.2620 0.0114  0.0138  0.0317  541  PHE A N   
3765  C CA  . PHE A 543  ? 0.3025 0.2508 0.2693 0.0132  0.0125  0.0311  541  PHE A CA  
3766  C C   . PHE A 543  ? 0.3432 0.2902 0.3086 0.0136  0.0114  0.0345  541  PHE A C   
3767  O O   . PHE A 543  ? 0.3674 0.3151 0.3312 0.0151  0.0103  0.0344  541  PHE A O   
3768  C CB  . PHE A 543  ? 0.2848 0.2372 0.2496 0.0140  0.0132  0.0293  541  PHE A CB  
3769  C CG  . PHE A 543  ? 0.3192 0.2726 0.2855 0.0134  0.0141  0.0264  541  PHE A CG  
3770  C CD1 . PHE A 543  ? 0.3416 0.2933 0.3102 0.0133  0.0135  0.0243  541  PHE A CD1 
3771  C CD2 . PHE A 543  ? 0.2925 0.2487 0.2580 0.0130  0.0155  0.0259  541  PHE A CD2 
3772  C CE1 . PHE A 543  ? 0.3039 0.2564 0.2740 0.0127  0.0143  0.0221  541  PHE A CE1 
3773  C CE2 . PHE A 543  ? 0.2816 0.2383 0.2487 0.0126  0.0161  0.0235  541  PHE A CE2 
3774  C CZ  . PHE A 543  ? 0.2952 0.2498 0.2645 0.0123  0.0155  0.0218  541  PHE A CZ  
3775  N N   . GLY A 544  ? 0.3249 0.2698 0.2910 0.0122  0.0116  0.0375  542  GLY A N   
3776  C CA  . GLY A 544  ? 0.3531 0.2960 0.3184 0.0123  0.0104  0.0411  542  GLY A CA  
3777  C C   . GLY A 544  ? 0.3554 0.3020 0.3170 0.0130  0.0106  0.0430  542  GLY A C   
3778  O O   . GLY A 544  ? 0.3255 0.2762 0.2854 0.0126  0.0123  0.0430  542  GLY A O   
3779  N N   . ASP A 545  ? 0.3788 0.3242 0.3392 0.0144  0.0088  0.0444  543  ASP A N   
3780  C CA  . ASP A 545  ? 0.4188 0.3677 0.3756 0.0152  0.0088  0.0465  543  ASP A CA  
3781  C C   . ASP A 545  ? 0.3841 0.3372 0.3389 0.0168  0.0092  0.0431  543  ASP A C   
3782  O O   . ASP A 545  ? 0.4488 0.4058 0.4004 0.0175  0.0094  0.0443  543  ASP A O   
3783  C CB  . ASP A 545  ? 0.4188 0.3646 0.3750 0.0163  0.0064  0.0493  543  ASP A CB  
3784  C CG  . ASP A 545  ? 0.5888 0.5302 0.5469 0.0146  0.0058  0.0532  543  ASP A CG  
3785  O OD1 . ASP A 545  ? 0.5816 0.5238 0.5401 0.0125  0.0074  0.0549  543  ASP A OD1 
3786  O OD2 . ASP A 545  ? 0.7290 0.6659 0.6884 0.0154  0.0035  0.0543  543  ASP A OD2 
3787  N N   . ALA A 546  ? 0.3816 0.3343 0.3383 0.0173  0.0092  0.0390  544  ALA A N   
3788  C CA  . ALA A 546  ? 0.3817 0.3382 0.3371 0.0187  0.0093  0.0357  544  ALA A CA  
3789  C C   . ALA A 546  ? 0.4070 0.3679 0.3605 0.0181  0.0112  0.0354  544  ALA A C   
3790  O O   . ALA A 546  ? 0.3678 0.3326 0.3184 0.0192  0.0111  0.0351  544  ALA A O   
3791  C CB  . ALA A 546  ? 0.3226 0.2777 0.2807 0.0189  0.0090  0.0318  544  ALA A CB  
3792  N N   . ARG A 547  ? 0.3771 0.3377 0.3321 0.0166  0.0127  0.0352  545  ARG A N   
3793  C CA  . ARG A 547  ? 0.3118 0.2766 0.2656 0.0162  0.0145  0.0342  545  ARG A CA  
3794  C C   . ARG A 547  ? 0.3048 0.2684 0.2608 0.0144  0.0159  0.0350  545  ARG A C   
3795  O O   . ARG A 547  ? 0.3064 0.2660 0.2650 0.0135  0.0155  0.0351  545  ARG A O   
3796  C CB  . ARG A 547  ? 0.3527 0.3195 0.3067 0.0173  0.0144  0.0299  545  ARG A CB  
3797  C CG  . ARG A 547  ? 0.3675 0.3311 0.3249 0.0168  0.0141  0.0274  545  ARG A CG  
3798  C CD  . ARG A 547  ? 0.3785 0.3436 0.3362 0.0177  0.0136  0.0235  545  ARG A CD  
3799  N NE  . ARG A 547  ? 0.4302 0.3923 0.3909 0.0172  0.0130  0.0218  545  ARG A NE  
3800  C CZ  . ARG A 547  ? 0.3348 0.2963 0.2976 0.0162  0.0138  0.0201  545  ARG A CZ  
3801  N NH1 . ARG A 547  ? 0.3259 0.2892 0.2885 0.0158  0.0150  0.0196  545  ARG A NH1 
3802  N NH2 . ARG A 547  ? 0.3442 0.3035 0.3095 0.0157  0.0132  0.0189  545  ARG A NH2 
3803  N N   . THR A 548  ? 0.3027 0.2702 0.2575 0.0139  0.0175  0.0353  546  THR A N   
3804  C CA  . THR A 548  ? 0.2792 0.2466 0.2359 0.0123  0.0190  0.0360  546  THR A CA  
3805  C C   . THR A 548  ? 0.2752 0.2424 0.2341 0.0124  0.0194  0.0321  546  THR A C   
3806  O O   . THR A 548  ? 0.2510 0.2209 0.2088 0.0136  0.0195  0.0293  546  THR A O   
3807  C CB  . THR A 548  ? 0.3129 0.2853 0.2674 0.0118  0.0205  0.0380  546  THR A CB  
3808  O OG1 . THR A 548  ? 0.3305 0.3030 0.2831 0.0115  0.0201  0.0422  546  THR A OG1 
3809  C CG2 . THR A 548  ? 0.2785 0.2514 0.2353 0.0102  0.0221  0.0385  546  THR A CG2 
3810  N N   . ASN A 549  ? 0.2605 0.2242 0.2222 0.0112  0.0195  0.0319  547  ASN A N   
3811  C CA  . ASN A 549  ? 0.2463 0.2097 0.2101 0.0111  0.0198  0.0286  547  ASN A CA  
3812  C C   . ASN A 549  ? 0.2667 0.2341 0.2301 0.0111  0.0213  0.0279  547  ASN A C   
3813  O O   . ASN A 549  ? 0.2870 0.2567 0.2497 0.0103  0.0224  0.0303  547  ASN A O   
3814  C CB  . ASN A 549  ? 0.2715 0.2311 0.2384 0.0097  0.0196  0.0289  547  ASN A CB  
3815  C CG  . ASN A 549  ? 0.2576 0.2164 0.2264 0.0097  0.0196  0.0258  547  ASN A CG  
3816  O OD1 . ASN A 549  ? 0.2716 0.2320 0.2400 0.0107  0.0194  0.0234  547  ASN A OD1 
3817  N ND2 . ASN A 549  ? 0.2524 0.2088 0.2237 0.0085  0.0196  0.0259  547  ASN A ND2 
3818  N N   . SER A 550  ? 0.2445 0.2130 0.2085 0.0119  0.0213  0.0246  548  SER A N   
3819  C CA  . SER A 550  ? 0.2270 0.1988 0.1913 0.0120  0.0225  0.0234  548  SER A CA  
3820  C C   . SER A 550  ? 0.2600 0.2306 0.2268 0.0104  0.0234  0.0245  548  SER A C   
3821  O O   . SER A 550  ? 0.2479 0.2146 0.2166 0.0095  0.0228  0.0249  548  SER A O   
3822  C CB  . SER A 550  ? 0.2676 0.2400 0.2326 0.0132  0.0219  0.0196  548  SER A CB  
3823  O OG  . SER A 550  ? 0.2576 0.2260 0.2250 0.0126  0.0211  0.0184  548  SER A OG  
3824  N N   . ALA A 551  ? 0.2618 0.2360 0.2286 0.0103  0.0247  0.0248  549  ALA A N   
3825  C CA  . ALA A 551  ? 0.2698 0.2436 0.2391 0.0088  0.0256  0.0257  549  ALA A CA  
3826  C C   . ALA A 551  ? 0.2540 0.2285 0.2251 0.0095  0.0257  0.0226  549  ALA A C   
3827  O O   . ALA A 551  ? 0.2641 0.2415 0.2343 0.0110  0.0257  0.0204  549  ALA A O   
3828  C CB  . ALA A 551  ? 0.2739 0.2515 0.2424 0.0080  0.0270  0.0285  549  ALA A CB  
3829  N N   . GLY A 552  ? 0.2708 0.2426 0.2445 0.0084  0.0255  0.0225  550  GLY A N   
3830  C CA  . GLY A 552  ? 0.2417 0.2140 0.2174 0.0089  0.0256  0.0201  550  GLY A CA  
3831  C C   . GLY A 552  ? 0.2495 0.2249 0.2265 0.0083  0.0269  0.0210  550  GLY A C   
3832  O O   . GLY A 552  ? 0.2867 0.2651 0.2627 0.0077  0.0280  0.0232  550  GLY A O   
3833  N N   . LEU A 553  ? 0.2513 0.2262 0.2306 0.0083  0.0267  0.0194  551  LEU A N   
3834  C CA  . LEU A 553  ? 0.2599 0.2378 0.2410 0.0079  0.0278  0.0197  551  LEU A CA  
3835  C C   . LEU A 553  ? 0.2582 0.2329 0.2420 0.0068  0.0272  0.0198  551  LEU A C   
3836  O O   . LEU A 553  ? 0.2687 0.2401 0.2530 0.0071  0.0260  0.0184  551  LEU A O   
3837  C CB  . LEU A 553  ? 0.2777 0.2594 0.2590 0.0098  0.0280  0.0170  551  LEU A CB  
3838  C CG  . LEU A 553  ? 0.2861 0.2724 0.2649 0.0111  0.0288  0.0166  551  LEU A CG  
3839  C CD1 . LEU A 553  ? 0.3049 0.2944 0.2844 0.0133  0.0286  0.0131  551  LEU A CD1 
3840  C CD2 . LEU A 553  ? 0.2956 0.2857 0.2734 0.0099  0.0304  0.0197  551  LEU A CD2 
3841  N N   . ASP A 554  ? 0.2322 0.2082 0.2176 0.0054  0.0280  0.0214  552  ASP A N   
3842  C CA  . ASP A 554  ? 0.2709 0.2442 0.2587 0.0043  0.0275  0.0215  552  ASP A CA  
3843  C C   . ASP A 554  ? 0.2442 0.2195 0.2340 0.0052  0.0275  0.0197  552  ASP A C   
3844  O O   . ASP A 554  ? 0.2367 0.2159 0.2277 0.0050  0.0285  0.0201  552  ASP A O   
3845  C CB  . ASP A 554  ? 0.2507 0.2239 0.2395 0.0022  0.0280  0.0242  552  ASP A CB  
3846  C CG  . ASP A 554  ? 0.2634 0.2340 0.2546 0.0011  0.0273  0.0241  552  ASP A CG  
3847  O OD1 . ASP A 554  ? 0.2720 0.2410 0.2639 0.0019  0.0264  0.0223  552  ASP A OD1 
3848  O OD2 . ASP A 554  ? 0.2774 0.2476 0.2698 -0.0006 0.0275  0.0259  552  ASP A OD2 
3849  N N   . LEU A 555  ? 0.2676 0.2405 0.2580 0.0061  0.0263  0.0177  553  LEU A N   
3850  C CA  . LEU A 555  ? 0.2494 0.2237 0.2418 0.0071  0.0260  0.0160  553  LEU A CA  
3851  C C   . LEU A 555  ? 0.2509 0.2249 0.2458 0.0059  0.0259  0.0168  553  LEU A C   
3852  O O   . LEU A 555  ? 0.2683 0.2428 0.2650 0.0067  0.0253  0.0155  553  LEU A O   
3853  C CB  . LEU A 555  ? 0.2436 0.2152 0.2359 0.0084  0.0245  0.0139  553  LEU A CB  
3854  C CG  . LEU A 555  ? 0.2597 0.2319 0.2499 0.0097  0.0243  0.0126  553  LEU A CG  
3855  C CD1 . LEU A 555  ? 0.3304 0.2997 0.3211 0.0108  0.0227  0.0105  553  LEU A CD1 
3856  C CD2 . LEU A 555  ? 0.3018 0.2791 0.2916 0.0111  0.0255  0.0117  553  LEU A CD2 
3857  N N   . SER A 556  ? 0.2861 0.2589 0.2810 0.0040  0.0262  0.0188  554  SER A N   
3858  C CA  . SER A 556  ? 0.2841 0.2574 0.2815 0.0028  0.0262  0.0195  554  SER A CA  
3859  C C   . SER A 556  ? 0.2594 0.2366 0.2577 0.0019  0.0276  0.0209  554  SER A C   
3860  O O   . SER A 556  ? 0.2580 0.2361 0.2585 0.0007  0.0277  0.0216  554  SER A O   
3861  C CB  . SER A 556  ? 0.2753 0.2447 0.2728 0.0014  0.0254  0.0204  554  SER A CB  
3862  O OG  . SER A 556  ? 0.3282 0.2970 0.3247 0.0002  0.0259  0.0222  554  SER A OG  
3863  N N   . ASN A 557  ? 0.2501 0.2298 0.2467 0.0022  0.0287  0.0216  555  ASN A N   
3864  C CA  . ASN A 557  ? 0.2253 0.2092 0.2225 0.0011  0.0301  0.0233  555  ASN A CA  
3865  C C   . ASN A 557  ? 0.2514 0.2407 0.2497 0.0026  0.0310  0.0218  555  ASN A C   
3866  O O   . ASN A 557  ? 0.2266 0.2175 0.2234 0.0046  0.0310  0.0201  555  ASN A O   
3867  C CB  . ASN A 557  ? 0.2508 0.2349 0.2455 0.0007  0.0308  0.0252  555  ASN A CB  
3868  C CG  . ASN A 557  ? 0.2337 0.2221 0.2289 -0.0009 0.0322  0.0276  555  ASN A CG  
3869  O OD1 . ASN A 557  ? 0.2489 0.2426 0.2450 -0.0003 0.0333  0.0271  555  ASN A OD1 
3870  N ND2 . ASN A 557  ? 0.2362 0.2222 0.2310 -0.0028 0.0322  0.0304  555  ASN A ND2 
3871  N N   . GLU A 558  ? 0.2704 0.2628 0.2715 0.0018  0.0315  0.0222  556  GLU A N   
3872  C CA  . GLU A 558  ? 0.2608 0.2586 0.2633 0.0034  0.0321  0.0203  556  GLU A CA  
3873  C C   . GLU A 558  ? 0.2641 0.2674 0.2650 0.0041  0.0337  0.0207  556  GLU A C   
3874  O O   . GLU A 558  ? 0.2661 0.2730 0.2669 0.0064  0.0340  0.0183  556  GLU A O   
3875  C CB  . GLU A 558  ? 0.2933 0.2938 0.2992 0.0023  0.0324  0.0208  556  GLU A CB  
3876  C CG  . GLU A 558  ? 0.3248 0.3212 0.3325 0.0022  0.0308  0.0200  556  GLU A CG  
3877  C CD  . GLU A 558  ? 0.2915 0.2864 0.2995 0.0047  0.0295  0.0172  556  GLU A CD  
3878  O OE1 . GLU A 558  ? 0.2884 0.2860 0.2958 0.0068  0.0297  0.0154  556  GLU A OE1 
3879  O OE2 . GLU A 558  ? 0.2494 0.2407 0.2583 0.0045  0.0281  0.0169  556  GLU A OE2 
3880  N N   . GLU A 559  ? 0.2486 0.2528 0.2482 0.0021  0.0347  0.0236  557  GLU A N   
3881  C CA  . GLU A 559  ? 0.2728 0.2825 0.2704 0.0027  0.0362  0.0241  557  GLU A CA  
3882  C C   . GLU A 559  ? 0.2500 0.2584 0.2447 0.0051  0.0356  0.0221  557  GLU A C   
3883  O O   . GLU A 559  ? 0.2451 0.2584 0.2390 0.0071  0.0362  0.0200  557  GLU A O   
3884  C CB  . GLU A 559  ? 0.2797 0.2901 0.2765 0.0000  0.0372  0.0281  557  GLU A CB  
3885  C CG  . GLU A 559  ? 0.3446 0.3565 0.3444 -0.0025 0.0378  0.0303  557  GLU A CG  
3886  C CD  . GLU A 559  ? 0.5108 0.5310 0.5126 -0.0022 0.0393  0.0298  557  GLU A CD  
3887  O OE1 . GLU A 559  ? 0.5312 0.5566 0.5313 -0.0003 0.0403  0.0285  557  GLU A OE1 
3888  O OE2 . GLU A 559  ? 0.5020 0.5237 0.5071 -0.0038 0.0395  0.0305  557  GLU A OE2 
3889  N N   . THR A 560  ? 0.2594 0.2613 0.2526 0.0048  0.0343  0.0223  558  THR A N   
3890  C CA  . THR A 560  ? 0.3003 0.3004 0.2910 0.0069  0.0335  0.0202  558  THR A CA  
3891  C C   . THR A 560  ? 0.2525 0.2532 0.2445 0.0093  0.0326  0.0165  558  THR A C   
3892  O O   . THR A 560  ? 0.2624 0.2660 0.2531 0.0115  0.0327  0.0142  558  THR A O   
3893  C CB  . THR A 560  ? 0.2542 0.2474 0.2438 0.0060  0.0321  0.0210  558  THR A CB  
3894  O OG1 . THR A 560  ? 0.2676 0.2601 0.2562 0.0040  0.0327  0.0244  558  THR A OG1 
3895  C CG2 . THR A 560  ? 0.2585 0.2500 0.2458 0.0080  0.0312  0.0189  558  THR A CG2 
3896  N N   . LEU A 561  ? 0.2318 0.2299 0.2265 0.0092  0.0317  0.0157  559  LEU A N   
3897  C CA  . LEU A 561  ? 0.2299 0.2280 0.2262 0.0115  0.0306  0.0124  559  LEU A CA  
3898  C C   . LEU A 561  ? 0.2473 0.2524 0.2444 0.0133  0.0316  0.0105  559  LEU A C   
3899  O O   . LEU A 561  ? 0.2526 0.2587 0.2496 0.0158  0.0309  0.0075  559  LEU A O   
3900  C CB  . LEU A 561  ? 0.2345 0.2291 0.2334 0.0108  0.0295  0.0124  559  LEU A CB  
3901  C CG  . LEU A 561  ? 0.2214 0.2093 0.2195 0.0096  0.0282  0.0134  559  LEU A CG  
3902  C CD1 . LEU A 561  ? 0.2494 0.2349 0.2501 0.0088  0.0271  0.0136  559  LEU A CD1 
3903  C CD2 . LEU A 561  ? 0.2414 0.2264 0.2379 0.0111  0.0269  0.0115  559  LEU A CD2 
3904  N N   . ALA A 562  ? 0.2565 0.2667 0.2547 0.0120  0.0333  0.0123  560  ALA A N   
3905  C CA  . ALA A 562  ? 0.2704 0.2882 0.2696 0.0137  0.0344  0.0105  560  ALA A CA  
3906  C C   . ALA A 562  ? 0.2845 0.3063 0.2806 0.0151  0.0353  0.0097  560  ALA A C   
3907  O O   . ALA A 562  ? 0.2934 0.3191 0.2897 0.0178  0.0351  0.0064  560  ALA A O   
3908  C CB  . ALA A 562  ? 0.3010 0.3237 0.3022 0.0117  0.0360  0.0129  560  ALA A CB  
3909  N N   . SER A 563  ? 0.2677 0.2887 0.2611 0.0132  0.0361  0.0127  561  SER A N   
3910  C CA  . SER A 563  ? 0.3018 0.3263 0.2918 0.0144  0.0367  0.0122  561  SER A CA  
3911  C C   . SER A 563  ? 0.3024 0.3231 0.2912 0.0168  0.0350  0.0088  561  SER A C   
3912  O O   . SER A 563  ? 0.3018 0.3269 0.2894 0.0192  0.0351  0.0061  561  SER A O   
3913  C CB  . SER A 563  ? 0.3683 0.3911 0.3558 0.0118  0.0374  0.0164  561  SER A CB  
3914  O OG  . SER A 563  ? 0.5020 0.5280 0.4860 0.0129  0.0380  0.0163  561  SER A OG  
3915  N N   . LEU A 564  ? 0.2930 0.3061 0.2822 0.0163  0.0333  0.0088  562  LEU A N   
3916  C CA  . LEU A 564  ? 0.2820 0.2913 0.2703 0.0182  0.0315  0.0059  562  LEU A CA  
3917  C C   . LEU A 564  ? 0.2738 0.2846 0.2645 0.0209  0.0305  0.0018  562  LEU A C   
3918  O O   . LEU A 564  ? 0.2817 0.2934 0.2716 0.0232  0.0296  -0.0013 562  LEU A O   
3919  C CB  . LEU A 564  ? 0.2769 0.2782 0.2654 0.0166  0.0301  0.0073  562  LEU A CB  
3920  C CG  . LEU A 564  ? 0.3109 0.3075 0.2985 0.0178  0.0282  0.0052  562  LEU A CG  
3921  C CD1 . LEU A 564  ? 0.3039 0.3028 0.2883 0.0186  0.0286  0.0048  562  LEU A CD1 
3922  C CD2 . LEU A 564  ? 0.3149 0.3050 0.3029 0.0158  0.0273  0.0072  562  LEU A CD2 
3923  N N   . THR A 565  ? 0.2625 0.2737 0.2564 0.0207  0.0304  0.0017  563  THR A N   
3924  C CA  . THR A 565  ? 0.3051 0.3180 0.3015 0.0235  0.0294  -0.0021 563  THR A CA  
3925  C C   . THR A 565  ? 0.2784 0.2989 0.2739 0.0259  0.0303  -0.0048 563  THR A C   
3926  O O   . THR A 565  ? 0.2709 0.2913 0.2668 0.0287  0.0289  -0.0087 563  THR A O   
3927  C CB  . THR A 565  ? 0.2530 0.2670 0.2529 0.0229  0.0296  -0.0014 563  THR A CB  
3928  O OG1 . THR A 565  ? 0.2720 0.2789 0.2728 0.0211  0.0283  0.0004  563  THR A OG1 
3929  C CG2 . THR A 565  ? 0.2703 0.2869 0.2729 0.0260  0.0285  -0.0054 563  THR A CG2 
3930  N N   . GLU A 566  ? 0.2729 0.3000 0.2670 0.0249  0.0326  -0.0028 564  GLU A N   
3931  C CA  . GLU A 566  ? 0.2861 0.3215 0.2790 0.0272  0.0338  -0.0052 564  GLU A CA  
3932  C C   . GLU A 566  ? 0.2948 0.3294 0.2844 0.0284  0.0331  -0.0068 564  GLU A C   
3933  O O   . GLU A 566  ? 0.2891 0.3271 0.2787 0.0315  0.0324  -0.0110 564  GLU A O   
3934  C CB  . GLU A 566  ? 0.3003 0.3431 0.2925 0.0253  0.0365  -0.0020 564  GLU A CB  
3935  N N   . ALA A 567  ? 0.2792 0.3096 0.2662 0.0263  0.0331  -0.0037 565  ALA A N   
3936  C CA  . ALA A 567  ? 0.3181 0.3476 0.3019 0.0274  0.0324  -0.0050 565  ALA A CA  
3937  C C   . ALA A 567  ? 0.2830 0.3072 0.2682 0.0295  0.0298  -0.0091 565  ALA A C   
3938  O O   . ALA A 567  ? 0.2786 0.3048 0.2626 0.0318  0.0290  -0.0124 565  ALA A O   
3939  C CB  . ALA A 567  ? 0.2932 0.3186 0.2744 0.0246  0.0327  -0.0008 565  ALA A CB  
3940  N N   . LEU A 568  ? 0.2312 0.2486 0.2192 0.0286  0.0284  -0.0087 566  LEU A N   
3941  C CA  . LEU A 568  ? 0.2645 0.2764 0.2542 0.0302  0.0257  -0.0120 566  LEU A CA  
3942  C C   . LEU A 568  ? 0.2677 0.2836 0.2595 0.0336  0.0249  -0.0167 566  LEU A C   
3943  O O   . LEU A 568  ? 0.2607 0.2757 0.2524 0.0358  0.0232  -0.0204 566  LEU A O   
3944  C CB  . LEU A 568  ? 0.2374 0.2420 0.2294 0.0284  0.0245  -0.0100 566  LEU A CB  
3945  C CG  . LEU A 568  ? 0.2738 0.2736 0.2640 0.0254  0.0248  -0.0061 566  LEU A CG  
3946  C CD1 . LEU A 568  ? 0.2654 0.2592 0.2580 0.0237  0.0238  -0.0044 566  LEU A CD1 
3947  C CD2 . LEU A 568  ? 0.2366 0.2337 0.2245 0.0258  0.0237  -0.0071 566  LEU A CD2 
3948  N N   . ARG A 569  ? 0.2823 0.3025 0.2763 0.0341  0.0259  -0.0168 567  ARG A N   
3949  C CA  . ARG A 569  ? 0.2433 0.2683 0.2396 0.0375  0.0253  -0.0214 567  ARG A CA  
3950  C C   . ARG A 569  ? 0.2948 0.3266 0.2884 0.0397  0.0260  -0.0242 567  ARG A C   
3951  O O   . ARG A 569  ? 0.3094 0.3418 0.3040 0.0428  0.0243  -0.0290 567  ARG A O   
3952  C CB  . ARG A 569  ? 0.2559 0.2859 0.2546 0.0374  0.0268  -0.0206 567  ARG A CB  
3953  C CG  . ARG A 569  ? 0.2833 0.3072 0.2853 0.0362  0.0255  -0.0191 567  ARG A CG  
3954  C CD  . ARG A 569  ? 0.3066 0.3361 0.3111 0.0361  0.0269  -0.0184 567  ARG A CD  
3955  N NE  . ARG A 569  ? 0.3851 0.4092 0.3923 0.0347  0.0259  -0.0164 567  ARG A NE  
3956  C CZ  . ARG A 569  ? 0.5096 0.5373 0.5190 0.0338  0.0270  -0.0150 567  ARG A CZ  
3957  N NH1 . ARG A 569  ? 0.4589 0.4955 0.4682 0.0340  0.0293  -0.0149 567  ARG A NH1 
3958  N NH2 . ARG A 569  ? 0.5160 0.5386 0.5277 0.0327  0.0258  -0.0135 567  ARG A NH2 
3959  N N   . GLU A 570  ? 0.2752 0.3122 0.2654 0.0381  0.0284  -0.0213 568  GLU A N   
3960  C CA  . GLU A 570  ? 0.3003 0.3444 0.2876 0.0401  0.0292  -0.0237 568  GLU A CA  
3961  C C   . GLU A 570  ? 0.3379 0.3773 0.3236 0.0412  0.0271  -0.0261 568  GLU A C   
3962  O O   . GLU A 570  ? 0.3045 0.3478 0.2897 0.0442  0.0263  -0.0307 568  GLU A O   
3963  C CB  . GLU A 570  ? 0.3703 0.4202 0.3543 0.0377  0.0321  -0.0192 568  GLU A CB  
3964  C CG  . GLU A 570  ? 0.4420 0.4991 0.4277 0.0372  0.0344  -0.0177 568  GLU A CG  
3965  C CD  . GLU A 570  ? 0.5377 0.5984 0.5208 0.0339  0.0370  -0.0121 568  GLU A CD  
3966  O OE1 . GLU A 570  ? 0.5692 0.6261 0.5494 0.0320  0.0369  -0.0091 568  GLU A OE1 
3967  O OE2 . GLU A 570  ? 0.5567 0.6241 0.5410 0.0332  0.0389  -0.0107 568  GLU A OE2 
3968  N N   . SER A 571  ? 0.2951 0.3262 0.2802 0.0388  0.0261  -0.0233 569  SER A N   
3969  C CA  . SER A 571  ? 0.3160 0.3425 0.2999 0.0396  0.0240  -0.0254 569  SER A CA  
3970  C C   . SER A 571  ? 0.3076 0.3312 0.2949 0.0423  0.0213  -0.0306 569  SER A C   
3971  O O   . SER A 571  ? 0.2827 0.3060 0.2692 0.0442  0.0197  -0.0341 569  SER A O   
3972  C CB  . SER A 571  ? 0.2990 0.3175 0.2823 0.0365  0.0235  -0.0215 569  SER A CB  
3973  O OG  . SER A 571  ? 0.2985 0.3101 0.2854 0.0359  0.0217  -0.0216 569  SER A OG  
3974  N N   . ALA A 572  ? 0.2959 0.3173 0.2870 0.0427  0.0205  -0.0312 570  ALA A N   
3975  C CA  . ALA A 572  ? 0.3110 0.3289 0.3057 0.0453  0.0176  -0.0358 570  ALA A CA  
3976  C C   . ALA A 572  ? 0.3792 0.4047 0.3746 0.0492  0.0175  -0.0411 570  ALA A C   
3977  O O   . ALA A 572  ? 0.3929 0.4160 0.3909 0.0519  0.0149  -0.0458 570  ALA A O   
3978  C CB  . ALA A 572  ? 0.3278 0.3404 0.3263 0.0444  0.0167  -0.0343 570  ALA A CB  
3979  N N   . ALA A 573  ? 0.3374 0.3721 0.3307 0.0496  0.0203  -0.0405 571  ALA A N   
3980  C CA  . ALA A 573  ? 0.3400 0.3835 0.3334 0.0533  0.0206  -0.0455 571  ALA A CA  
3981  C C   . ALA A 573  ? 0.4389 0.4863 0.4285 0.0545  0.0206  -0.0476 571  ALA A C   
3982  O O   . ALA A 573  ? 0.4559 0.5109 0.4450 0.0578  0.0207  -0.0521 571  ALA A O   
3983  C CB  . ALA A 573  ? 0.3488 0.4015 0.3419 0.0531  0.0236  -0.0437 571  ALA A CB  
3984  N N   . MET A 574  ? 0.3688 0.4113 0.3555 0.0521  0.0204  -0.0446 572  MET A N   
3985  C CA  . MET A 574  ? 0.4082 0.4545 0.3911 0.0531  0.0205  -0.0462 572  MET A CA  
3986  C C   . MET A 574  ? 0.3364 0.3784 0.3211 0.0556  0.0170  -0.0518 572  MET A C   
3987  O O   . MET A 574  ? 0.3825 0.4156 0.3705 0.0550  0.0146  -0.0522 572  MET A O   
3988  C CB  . MET A 574  ? 0.3820 0.4253 0.3613 0.0496  0.0217  -0.0407 572  MET A CB  
3989  C CG  . MET A 574  ? 0.3992 0.4482 0.3761 0.0473  0.0250  -0.0356 572  MET A CG  
3990  S SD  . MET A 574  ? 0.4278 0.4716 0.4016 0.0432  0.0260  -0.0290 572  MET A SD  
3991  C CE  . MET A 574  ? 0.4763 0.5271 0.4485 0.0410  0.0296  -0.0238 572  MET A CE  
3992  N N   . LYS A 575  ? 0.3943 0.4428 0.3768 0.0583  0.0168  -0.0560 573  LYS A N   
3993  C CA  . LYS A 575  ? 0.3284 0.3737 0.3125 0.0609  0.0134  -0.0618 573  LYS A CA  
3994  C C   . LYS A 575  ? 0.3525 0.3936 0.3337 0.0590  0.0127  -0.0600 573  LYS A C   
3995  O O   . LYS A 575  ? 0.3680 0.4142 0.3460 0.0603  0.0127  -0.0621 573  LYS A O   
3996  C CB  . LYS A 575  ? 0.4440 0.4989 0.4276 0.0652  0.0133  -0.0680 573  LYS A CB  
3997  N N   . TRP A 576  ? 0.3246 0.3565 0.3071 0.0559  0.0119  -0.0560 574  TRP A N   
3998  C CA  . TRP A 576  ? 0.3279 0.3551 0.3083 0.0538  0.0111  -0.0540 574  TRP A CA  
3999  C C   . TRP A 576  ? 0.2853 0.3107 0.2668 0.0561  0.0079  -0.0597 574  TRP A C   
4000  O O   . TRP A 576  ? 0.3085 0.3304 0.2942 0.0579  0.0053  -0.0639 574  TRP A O   
4001  C CB  . TRP A 576  ? 0.2999 0.3177 0.2824 0.0503  0.0106  -0.0495 574  TRP A CB  
4002  C CG  . TRP A 576  ? 0.2895 0.3082 0.2710 0.0478  0.0135  -0.0438 574  TRP A CG  
4003  C CD1 . TRP A 576  ? 0.3029 0.3197 0.2874 0.0472  0.0139  -0.0424 574  TRP A CD1 
4004  C CD2 . TRP A 576  ? 0.2584 0.2798 0.2359 0.0455  0.0160  -0.0389 574  TRP A CD2 
4005  N NE1 . TRP A 576  ? 0.3020 0.3202 0.2847 0.0446  0.0166  -0.0370 574  TRP A NE1 
4006  C CE2 . TRP A 576  ? 0.2842 0.3050 0.2626 0.0435  0.0179  -0.0347 574  TRP A CE2 
4007  C CE3 . TRP A 576  ? 0.2988 0.3229 0.2721 0.0450  0.0167  -0.0376 574  TRP A CE3 
4008  C CZ2 . TRP A 576  ? 0.2754 0.2980 0.2510 0.0410  0.0203  -0.0294 574  TRP A CZ2 
4009  C CZ3 . TRP A 576  ? 0.3029 0.3286 0.2732 0.0425  0.0191  -0.0321 574  TRP A CZ3 
4010  C CH2 . TRP A 576  ? 0.2842 0.3091 0.2558 0.0405  0.0209  -0.0281 574  TRP A CH2 
4011  N N   . THR A 577  ? 0.2906 0.3185 0.2685 0.0560  0.0079  -0.0599 575  THR A N   
4012  C CA  . THR A 577  ? 0.3051 0.3312 0.2838 0.0578  0.0048  -0.0650 575  THR A CA  
4013  C C   . THR A 577  ? 0.3095 0.3321 0.2858 0.0553  0.0045  -0.0621 575  THR A C   
4014  O O   . THR A 577  ? 0.2851 0.3092 0.2581 0.0530  0.0069  -0.0568 575  THR A O   
4015  C CB  . THR A 577  ? 0.3578 0.3933 0.3345 0.0616  0.0047  -0.0707 575  THR A CB  
4016  O OG1 . THR A 577  ? 0.3058 0.3490 0.2770 0.0611  0.0075  -0.0676 575  THR A OG1 
4017  C CG2 . THR A 577  ? 0.3893 0.4291 0.3686 0.0645  0.0050  -0.0742 575  THR A CG2 
4018  N N   . ALA A 578  ? 0.2945 0.3125 0.2729 0.0557  0.0014  -0.0656 576  ALA A N   
4019  C CA  . ALA A 578  ? 0.2655 0.2815 0.2418 0.0541  0.0006  -0.0642 576  ALA A CA  
4020  C C   . ALA A 578  ? 0.2910 0.3093 0.2676 0.0570  -0.0021 -0.0707 576  ALA A C   
4021  O O   . ALA A 578  ? 0.3046 0.3200 0.2853 0.0587  -0.0048 -0.0756 576  ALA A O   
4022  C CB  . ALA A 578  ? 0.2627 0.2689 0.2420 0.0508  -0.0007 -0.0609 576  ALA A CB  
4023  N N   . LEU A 579  ? 0.3236 0.3474 0.2959 0.0575  -0.0015 -0.0710 577  LEU A N   
4024  C CA  . LEU A 579  ? 0.3516 0.3790 0.3234 0.0603  -0.0039 -0.0772 577  LEU A CA  
4025  C C   . LEU A 579  ? 0.2912 0.3167 0.2611 0.0586  -0.0049 -0.0759 577  LEU A C   
4026  O O   . LEU A 579  ? 0.2939 0.3185 0.2613 0.0560  -0.0030 -0.0700 577  LEU A O   
4027  C CB  . LEU A 579  ? 0.3372 0.3759 0.3050 0.0635  -0.0021 -0.0798 577  LEU A CB  
4028  C CG  . LEU A 579  ? 0.3860 0.4290 0.3547 0.0651  -0.0003 -0.0803 577  LEU A CG  
4029  C CD1 . LEU A 579  ? 0.4398 0.4948 0.4040 0.0680  0.0015  -0.0827 577  LEU A CD1 
4030  C CD2 . LEU A 579  ? 0.3979 0.4358 0.3724 0.0669  -0.0032 -0.0855 577  LEU A CD2 
4031  N N   . PRO A 580  ? 0.3037 0.3288 0.2750 0.0602  -0.0081 -0.0813 578  PRO A N   
4032  C CA  . PRO A 580  ? 0.3053 0.3311 0.2741 0.0593  -0.0089 -0.0807 578  PRO A CA  
4033  C C   . PRO A 580  ? 0.3584 0.3938 0.3209 0.0605  -0.0063 -0.0791 578  PRO A C   
4034  O O   . PRO A 580  ? 0.3602 0.4033 0.3207 0.0638  -0.0064 -0.0836 578  PRO A O   
4035  C CB  . PRO A 580  ? 0.3229 0.3475 0.2948 0.0613  -0.0128 -0.0879 578  PRO A CB  
4036  C CG  . PRO A 580  ? 0.2986 0.3190 0.2756 0.0626  -0.0144 -0.0913 578  PRO A CG  
4037  C CD  . PRO A 580  ? 0.3218 0.3465 0.2970 0.0632  -0.0111 -0.0886 578  PRO A CD  
4038  N N   . GLN A 581  ? 0.2982 0.3335 0.2575 0.0580  -0.0040 -0.0727 579  GLN A N   
4039  C CA  . GLN A 581  ? 0.3068 0.3507 0.2601 0.0588  -0.0015 -0.0700 579  GLN A CA  
4040  C C   . GLN A 581  ? 0.3379 0.3827 0.2887 0.0584  -0.0028 -0.0700 579  GLN A C   
4041  O O   . GLN A 581  ? 0.3009 0.3419 0.2509 0.0558  -0.0023 -0.0650 579  GLN A O   
4042  C CB  . GLN A 581  ? 0.2741 0.3173 0.2258 0.0563  0.0018  -0.0629 579  GLN A CB  
4043  C CG  . GLN A 581  ? 0.3155 0.3585 0.2695 0.0566  0.0033  -0.0628 579  GLN A CG  
4044  C CD  . GLN A 581  ? 0.3628 0.4159 0.3144 0.0598  0.0045  -0.0661 579  GLN A CD  
4045  O OE1 . GLN A 581  ? 0.3616 0.4220 0.3092 0.0617  0.0045  -0.0680 579  GLN A OE1 
4046  N NE2 . GLN A 581  ? 0.3614 0.4152 0.3152 0.0605  0.0056  -0.0667 579  GLN A NE2 
4047  N N   . LEU A 582  ? 0.3102 0.3603 0.2598 0.0613  -0.0048 -0.0758 580  LEU A N   
4048  C CA  . LEU A 582  ? 0.3487 0.4007 0.2957 0.0614  -0.0062 -0.0763 580  LEU A CA  
4049  C C   . LEU A 582  ? 0.3587 0.4193 0.2992 0.0620  -0.0037 -0.0726 580  LEU A C   
4050  O O   . LEU A 582  ? 0.3582 0.4241 0.2961 0.0626  -0.0011 -0.0706 580  LEU A O   
4051  C CB  . LEU A 582  ? 0.3504 0.4042 0.2993 0.0641  -0.0096 -0.0843 580  LEU A CB  
4052  C CG  . LEU A 582  ? 0.4098 0.4543 0.3646 0.0626  -0.0129 -0.0869 580  LEU A CG  
4053  C CD1 . LEU A 582  ? 0.4048 0.4419 0.3648 0.0613  -0.0128 -0.0861 580  LEU A CD1 
4054  C CD2 . LEU A 582  ? 0.4534 0.5004 0.4098 0.0654  -0.0165 -0.0949 580  LEU A CD2 
4055  N N   . ALA A 583  ? 0.3185 0.3803 0.2562 0.0616  -0.0047 -0.0715 581  ALA A N   
4056  C CA  . ALA A 583  ? 0.3304 0.4003 0.2618 0.0622  -0.0028 -0.0679 581  ALA A CA  
4057  C C   . ALA A 583  ? 0.3933 0.4736 0.3214 0.0656  -0.0021 -0.0720 581  ALA A C   
4058  O O   . ALA A 583  ? 0.4251 0.5125 0.3485 0.0659  0.0005  -0.0683 581  ALA A O   
4059  C CB  . ALA A 583  ? 0.3537 0.4238 0.2830 0.0619  -0.0046 -0.0674 581  ALA A CB  
4060  N N   . THR A 584  ? 0.3671 0.4485 0.2978 0.0682  -0.0045 -0.0796 582  THR A N   
4061  C CA  . THR A 584  ? 0.4075 0.4991 0.3354 0.0719  -0.0044 -0.0848 582  THR A CA  
4062  C C   . THR A 584  ? 0.4643 0.5581 0.3939 0.0729  -0.0026 -0.0859 582  THR A C   
4063  O O   . THR A 584  ? 0.4667 0.5694 0.3944 0.0761  -0.0023 -0.0904 582  THR A O   
4064  C CB  . THR A 584  ? 0.4184 0.5101 0.3487 0.0743  -0.0083 -0.0930 582  THR A CB  
4065  O OG1 . THR A 584  ? 0.4526 0.5342 0.3898 0.0732  -0.0105 -0.0956 582  THR A OG1 
4066  C CG2 . THR A 584  ? 0.4276 0.5196 0.3555 0.0737  -0.0101 -0.0923 582  THR A CG2 
4067  N N   . GLY A 585  ? 0.3639 0.4501 0.2970 0.0703  -0.0013 -0.0819 583  GLY A N   
4068  C CA  . GLY A 585  ? 0.4002 0.4876 0.3354 0.0711  0.0004  -0.0827 583  GLY A CA  
4069  C C   . GLY A 585  ? 0.3565 0.4340 0.2986 0.0704  -0.0017 -0.0853 583  GLY A C   
4070  O O   . GLY A 585  ? 0.3778 0.4477 0.3231 0.0693  -0.0044 -0.0868 583  GLY A O   
4071  N N   . PRO A 586  ? 0.4304 0.5079 0.3749 0.0710  -0.0004 -0.0859 584  PRO A N   
4072  C CA  . PRO A 586  ? 0.3813 0.4495 0.3324 0.0705  -0.0024 -0.0883 584  PRO A CA  
4073  C C   . PRO A 586  ? 0.4212 0.4884 0.3755 0.0733  -0.0063 -0.0966 584  PRO A C   
4074  O O   . PRO A 586  ? 0.4157 0.4913 0.3677 0.0767  -0.0070 -0.1019 584  PRO A O   
4075  C CB  . PRO A 586  ? 0.4300 0.5011 0.3821 0.0712  -0.0001 -0.0876 584  PRO A CB  
4076  C CG  . PRO A 586  ? 0.4402 0.5242 0.3870 0.0736  0.0022  -0.0883 584  PRO A CG  
4077  C CD  . PRO A 586  ? 0.4025 0.4890 0.3441 0.0722  0.0028  -0.0843 584  PRO A CD  
4078  N N   . ALA A 587  ? 0.3871 0.4441 0.3467 0.0718  -0.0091 -0.0976 585  ALA A N   
4079  C CA  . ALA A 587  ? 0.3879 0.4423 0.3513 0.0739  -0.0132 -0.1052 585  ALA A CA  
4080  C C   . ALA A 587  ? 0.4290 0.4791 0.3981 0.0753  -0.0146 -0.1089 585  ALA A C   
4081  O O   . ALA A 587  ? 0.3845 0.4304 0.3555 0.0735  -0.0130 -0.1047 585  ALA A O   
4082  C CB  . ALA A 587  ? 0.4371 0.4832 0.4028 0.0712  -0.0157 -0.1042 585  ALA A CB  
4083  N N   . ALA A 588  ? 0.4314 0.4827 0.4031 0.0787  -0.0179 -0.1169 586  ALA A N   
4084  C CA  . ALA A 588  ? 0.4682 0.5141 0.4461 0.0801  -0.0201 -0.1210 586  ALA A CA  
4085  C C   . ALA A 588  ? 0.4081 0.4413 0.3914 0.0769  -0.0229 -0.1194 586  ALA A C   
4086  O O   . ALA A 588  ? 0.4589 0.4887 0.4419 0.0746  -0.0241 -0.1178 586  ALA A O   
4087  C CB  . ALA A 588  ? 0.4770 0.5283 0.4561 0.0849  -0.0230 -0.1304 586  ALA A CB  
4088  N N   . GLY A 589  ? 0.4167 0.4434 0.4051 0.0767  -0.0239 -0.1195 587  GLY A N   
4089  C CA  . GLY A 589  ? 0.4324 0.4474 0.4262 0.0737  -0.0267 -0.1179 587  GLY A CA  
4090  C C   . GLY A 589  ? 0.4412 0.4504 0.4404 0.0744  -0.0279 -0.1189 587  GLY A C   
4091  O O   . GLY A 589  ? 0.4447 0.4590 0.4437 0.0775  -0.0269 -0.1215 587  GLY A O   
4092  N N   . GLU A 590  ? 0.3970 0.3956 0.4010 0.0714  -0.0302 -0.1166 588  GLU A N   
4093  C CA  . GLU A 590  ? 0.4346 0.4265 0.4440 0.0715  -0.0317 -0.1167 588  GLU A CA  
4094  C C   . GLU A 590  ? 0.4329 0.4250 0.4403 0.0694  -0.0277 -0.1096 588  GLU A C   
4095  O O   . GLU A 590  ? 0.3971 0.3873 0.4021 0.0657  -0.0255 -0.1032 588  GLU A O   
4096  C CB  . GLU A 590  ? 0.4868 0.4675 0.5019 0.0689  -0.0356 -0.1165 588  GLU A CB  
4097  N N   . THR A 591  ? 0.4100 0.4045 0.4186 0.0719  -0.0269 -0.1111 589  THR A N   
4098  C CA  . THR A 591  ? 0.3957 0.3920 0.4023 0.0706  -0.0231 -0.1053 589  THR A CA  
4099  C C   . THR A 591  ? 0.3855 0.3729 0.3974 0.0693  -0.0247 -0.1033 589  THR A C   
4100  O O   . THR A 591  ? 0.4276 0.4116 0.4444 0.0718  -0.0281 -0.1083 589  THR A O   
4101  C CB  . THR A 591  ? 0.4150 0.4221 0.4184 0.0742  -0.0206 -0.1080 589  THR A CB  
4102  O OG1 . THR A 591  ? 0.4154 0.4310 0.4135 0.0752  -0.0191 -0.1093 589  THR A OG1 
4103  C CG2 . THR A 591  ? 0.4117 0.4208 0.4133 0.0726  -0.0167 -0.1019 589  THR A CG2 
4104  N N   . ARG A 592  ? 0.3893 0.3730 0.4004 0.0655  -0.0225 -0.0961 590  ARG A N   
4105  C CA  . ARG A 592  ? 0.4202 0.3965 0.4358 0.0642  -0.0235 -0.0933 590  ARG A CA  
4106  C C   . ARG A 592  ? 0.3812 0.3604 0.3939 0.0625  -0.0193 -0.0873 590  ARG A C   
4107  O O   . ARG A 592  ? 0.3390 0.3238 0.3465 0.0613  -0.0160 -0.0842 590  ARG A O   
4108  C CB  . ARG A 592  ? 0.4981 0.4642 0.5170 0.0605  -0.0261 -0.0906 590  ARG A CB  
4109  C CG  . ARG A 592  ? 0.5372 0.5033 0.5526 0.0569  -0.0245 -0.0862 590  ARG A CG  
4110  C CD  . ARG A 592  ? 0.6086 0.5652 0.6274 0.0529  -0.0264 -0.0823 590  ARG A CD  
4111  N NE  . ARG A 592  ? 0.6529 0.6064 0.6721 0.0505  -0.0245 -0.0763 590  ARG A NE  
4112  C CZ  . ARG A 592  ? 0.6517 0.6053 0.6679 0.0472  -0.0217 -0.0702 590  ARG A CZ  
4113  N NH1 . ARG A 592  ? 0.5817 0.5379 0.5945 0.0457  -0.0205 -0.0690 590  ARG A NH1 
4114  N NH2 . ARG A 592  ? 0.5876 0.5387 0.6043 0.0454  -0.0202 -0.0655 590  ARG A NH2 
4115  N N   . THR A 593  ? 0.3626 0.3375 0.3786 0.0623  -0.0198 -0.0856 591  THR A N   
4116  C CA  . THR A 593  ? 0.3475 0.3249 0.3614 0.0607  -0.0162 -0.0802 591  THR A CA  
4117  C C   . THR A 593  ? 0.3875 0.3589 0.4007 0.0560  -0.0152 -0.0733 591  THR A C   
4118  O O   . THR A 593  ? 0.4139 0.3777 0.4300 0.0539  -0.0178 -0.0726 591  THR A O   
4119  C CB  . THR A 593  ? 0.4127 0.3891 0.4304 0.0629  -0.0170 -0.0817 591  THR A CB  
4120  O OG1 . THR A 593  ? 0.4454 0.4120 0.4684 0.0619  -0.0207 -0.0816 591  THR A OG1 
4121  C CG2 . THR A 593  ? 0.4173 0.4005 0.4356 0.0679  -0.0179 -0.0889 591  THR A CG2 
4122  N N   . VAL A 594  ? 0.3002 0.2754 0.3096 0.0542  -0.0114 -0.0684 592  VAL A N   
4123  C CA  . VAL A 594  ? 0.3119 0.2826 0.3205 0.0499  -0.0101 -0.0619 592  VAL A CA  
4124  C C   . VAL A 594  ? 0.3183 0.2870 0.3288 0.0493  -0.0092 -0.0588 592  VAL A C   
4125  O O   . VAL A 594  ? 0.3071 0.2816 0.3166 0.0511  -0.0071 -0.0592 592  VAL A O   
4126  C CB  . VAL A 594  ? 0.2989 0.2749 0.3020 0.0484  -0.0067 -0.0586 592  VAL A CB  
4127  C CG1 . VAL A 594  ? 0.2899 0.2614 0.2921 0.0443  -0.0054 -0.0523 592  VAL A CG1 
4128  C CG2 . VAL A 594  ? 0.3230 0.3014 0.3240 0.0493  -0.0077 -0.0618 592  VAL A CG2 
4129  N N   . LEU A 595  ? 0.3002 0.2612 0.3137 0.0468  -0.0108 -0.0558 593  LEU A N   
4130  C CA  . LEU A 595  ? 0.2926 0.2509 0.3086 0.0464  -0.0107 -0.0534 593  LEU A CA  
4131  C C   . LEU A 595  ? 0.3140 0.2707 0.3280 0.0425  -0.0084 -0.0468 593  LEU A C   
4132  O O   . LEU A 595  ? 0.2866 0.2412 0.2990 0.0398  -0.0081 -0.0443 593  LEU A O   
4133  C CB  . LEU A 595  ? 0.3257 0.2763 0.3471 0.0467  -0.0148 -0.0550 593  LEU A CB  
4134  C CG  . LEU A 595  ? 0.3386 0.2892 0.3630 0.0505  -0.0180 -0.0618 593  LEU A CG  
4135  C CD1 . LEU A 595  ? 0.3696 0.3115 0.3997 0.0503  -0.0222 -0.0625 593  LEU A CD1 
4136  C CD2 . LEU A 595  ? 0.3252 0.2832 0.3489 0.0543  -0.0165 -0.0653 593  LEU A CD2 
4137  N N   . ASN A 596  ? 0.2867 0.2448 0.3010 0.0424  -0.0068 -0.0445 594  ASN A N   
4138  C CA  . ASN A 596  ? 0.2924 0.2486 0.3054 0.0391  -0.0049 -0.0386 594  ASN A CA  
4139  C C   . ASN A 596  ? 0.2609 0.2091 0.2770 0.0368  -0.0075 -0.0365 594  ASN A C   
4140  O O   . ASN A 596  ? 0.2758 0.2202 0.2958 0.0380  -0.0100 -0.0380 594  ASN A O   
4141  C CB  . ASN A 596  ? 0.2620 0.2217 0.2752 0.0399  -0.0030 -0.0374 594  ASN A CB  
4142  C CG  . ASN A 596  ? 0.2847 0.2435 0.2965 0.0367  -0.0009 -0.0317 594  ASN A CG  
4143  O OD1 . ASN A 596  ? 0.2805 0.2343 0.2924 0.0339  -0.0015 -0.0286 594  ASN A OD1 
4144  N ND2 . ASN A 596  ? 0.2837 0.2476 0.2941 0.0371  0.0017  -0.0305 594  ASN A ND2 
4145  N N   . PRO A 597  ? 0.2716 0.2171 0.2862 0.0336  -0.0071 -0.0331 595  PRO A N   
4146  C CA  . PRO A 597  ? 0.2786 0.2171 0.2962 0.0312  -0.0094 -0.0308 595  PRO A CA  
4147  C C   . PRO A 597  ? 0.2717 0.2081 0.2910 0.0304  -0.0093 -0.0277 595  PRO A C   
4148  O O   . PRO A 597  ? 0.2758 0.2065 0.2984 0.0293  -0.0119 -0.0265 595  PRO A O   
4149  C CB  . PRO A 597  ? 0.2642 0.2023 0.2792 0.0280  -0.0081 -0.0275 595  PRO A CB  
4150  C CG  . PRO A 597  ? 0.3162 0.2604 0.3269 0.0284  -0.0048 -0.0271 595  PRO A CG  
4151  C CD  . PRO A 597  ? 0.2728 0.2218 0.2831 0.0320  -0.0044 -0.0311 595  PRO A CD  
4152  N N   . GLY A 598  ? 0.2531 0.1940 0.2706 0.0309  -0.0067 -0.0263 596  GLY A N   
4153  C CA  . GLY A 598  ? 0.2427 0.1819 0.2619 0.0303  -0.0067 -0.0236 596  GLY A CA  
4154  C C   . GLY A 598  ? 0.2583 0.1972 0.2809 0.0334  -0.0086 -0.0267 596  GLY A C   
4155  O O   . GLY A 598  ? 0.2802 0.2171 0.3048 0.0331  -0.0093 -0.0247 596  GLY A O   
4156  N N   . ASP A 599  ? 0.2748 0.2159 0.2982 0.0365  -0.0096 -0.0316 597  ASP A N   
4157  C CA  . ASP A 599  ? 0.2534 0.1951 0.2800 0.0400  -0.0113 -0.0353 597  ASP A CA  
4158  C C   . ASP A 599  ? 0.2556 0.1994 0.2825 0.0429  -0.0125 -0.0410 597  ASP A C   
4159  O O   . ASP A 599  ? 0.2808 0.2314 0.3049 0.0445  -0.0102 -0.0431 597  ASP A O   
4160  C CB  . ASP A 599  ? 0.2649 0.2126 0.2903 0.0411  -0.0086 -0.0346 597  ASP A CB  
4161  C CG  . ASP A 599  ? 0.3247 0.2731 0.3538 0.0446  -0.0104 -0.0381 597  ASP A CG  
4162  O OD1 . ASP A 599  ? 0.2896 0.2347 0.3219 0.0468  -0.0137 -0.0419 597  ASP A OD1 
4163  O OD2 . ASP A 599  ? 0.3506 0.3031 0.3797 0.0453  -0.0087 -0.0370 597  ASP A OD2 
4164  N N   . HIS A 600  ? 0.2958 0.2339 0.3261 0.0436  -0.0162 -0.0435 598  HIS A N   
4165  C CA  . HIS A 600  ? 0.3207 0.2604 0.3514 0.0463  -0.0177 -0.0491 598  HIS A CA  
4166  C C   . HIS A 600  ? 0.3388 0.2841 0.3705 0.0507  -0.0177 -0.0541 598  HIS A C   
4167  O O   . HIS A 600  ? 0.3487 0.2974 0.3799 0.0533  -0.0183 -0.0591 598  HIS A O   
4168  C CB  . HIS A 600  ? 0.2967 0.2285 0.3313 0.0458  -0.0220 -0.0505 598  HIS A CB  
4169  C CG  . HIS A 600  ? 0.3218 0.2496 0.3552 0.0417  -0.0220 -0.0466 598  HIS A CG  
4170  N ND1 . HIS A 600  ? 0.3784 0.2997 0.4150 0.0405  -0.0255 -0.0473 598  HIS A ND1 
4171  C CD2 . HIS A 600  ? 0.3153 0.2451 0.3449 0.0385  -0.0190 -0.0421 598  HIS A CD2 
4172  C CE1 . HIS A 600  ? 0.3848 0.3046 0.4195 0.0367  -0.0245 -0.0434 598  HIS A CE1 
4173  N NE2 . HIS A 600  ? 0.3589 0.2837 0.3893 0.0356  -0.0206 -0.0403 598  HIS A NE2 
4174  N N   . ARG A 601  ? 0.3093 0.2561 0.3424 0.0518  -0.0171 -0.0532 599  ARG A N   
4175  C CA  . ARG A 601  ? 0.3323 0.2859 0.3660 0.0560  -0.0164 -0.0577 599  ARG A CA  
4176  C C   . ARG A 601  ? 0.3117 0.2746 0.3405 0.0561  -0.0122 -0.0576 599  ARG A C   
4177  O O   . ARG A 601  ? 0.3049 0.2747 0.3335 0.0595  -0.0115 -0.0619 599  ARG A O   
4178  C CB  . ARG A 601  ? 0.3337 0.2868 0.3702 0.0569  -0.0168 -0.0563 599  ARG A CB  
4179  C CG  . ARG A 601  ? 0.3651 0.3090 0.4064 0.0567  -0.0210 -0.0558 599  ARG A CG  
4180  C CD  . ARG A 601  ? 0.3489 0.2926 0.3922 0.0568  -0.0208 -0.0530 599  ARG A CD  
4181  N NE  . ARG A 601  ? 0.3628 0.3091 0.4024 0.0534  -0.0171 -0.0474 599  ARG A NE  
4182  C CZ  . ARG A 601  ? 0.4500 0.3970 0.4903 0.0527  -0.0162 -0.0443 599  ARG A CZ  
4183  N NH1 . ARG A 601  ? 0.4350 0.3805 0.4794 0.0553  -0.0186 -0.0459 599  ARG A NH1 
4184  N NH2 . ARG A 601  ? 0.3797 0.3290 0.4166 0.0495  -0.0130 -0.0396 599  ARG A NH2 
4185  N N   . ASP A 602  ? 0.2967 0.2598 0.3217 0.0524  -0.0096 -0.0527 600  ASP A N   
4186  C CA  . ASP A 602  ? 0.2987 0.2698 0.3191 0.0519  -0.0056 -0.0515 600  ASP A CA  
4187  C C   . ASP A 602  ? 0.3282 0.3010 0.3459 0.0522  -0.0057 -0.0538 600  ASP A C   
4188  O O   . ASP A 602  ? 0.3058 0.2746 0.3220 0.0493  -0.0058 -0.0512 600  ASP A O   
4189  C CB  . ASP A 602  ? 0.2948 0.2650 0.3130 0.0481  -0.0031 -0.0451 600  ASP A CB  
4190  C CG  . ASP A 602  ? 0.3459 0.3235 0.3595 0.0473  0.0008  -0.0434 600  ASP A CG  
4191  O OD1 . ASP A 602  ? 0.3328 0.3177 0.3454 0.0500  0.0019  -0.0467 600  ASP A OD1 
4192  O OD2 . ASP A 602  ? 0.3263 0.3027 0.3375 0.0440  0.0026  -0.0387 600  ASP A OD2 
4193  N N   . VAL A 603  ? 0.3338 0.3129 0.3510 0.0556  -0.0056 -0.0589 601  VAL A N   
4194  C CA  . VAL A 603  ? 0.3308 0.3126 0.3453 0.0564  -0.0057 -0.0617 601  VAL A CA  
4195  C C   . VAL A 603  ? 0.3074 0.2957 0.3166 0.0546  -0.0017 -0.0583 601  VAL A C   
4196  O O   . VAL A 603  ? 0.2961 0.2916 0.3038 0.0556  0.0009  -0.0580 601  VAL A O   
4197  C CB  . VAL A 603  ? 0.3313 0.3176 0.3474 0.0610  -0.0074 -0.0688 601  VAL A CB  
4198  C CG1 . VAL A 603  ? 0.3378 0.3269 0.3511 0.0618  -0.0078 -0.0719 601  VAL A CG1 
4199  C CG2 . VAL A 603  ? 0.3396 0.3190 0.3615 0.0627  -0.0115 -0.0720 601  VAL A CG2 
4200  N N   . VAL A 604  ? 0.2679 0.2539 0.2745 0.0521  -0.0013 -0.0558 602  VAL A N   
4201  C CA  . VAL A 604  ? 0.2663 0.2574 0.2681 0.0502  0.0021  -0.0520 602  VAL A CA  
4202  C C   . VAL A 604  ? 0.2867 0.2852 0.2852 0.0524  0.0029  -0.0555 602  VAL A C   
4203  O O   . VAL A 604  ? 0.2805 0.2862 0.2754 0.0524  0.0059  -0.0539 602  VAL A O   
4204  C CB  . VAL A 604  ? 0.2677 0.2527 0.2682 0.0463  0.0022  -0.0473 602  VAL A CB  
4205  C CG1 . VAL A 604  ? 0.2649 0.2544 0.2609 0.0444  0.0056  -0.0431 602  VAL A CG1 
4206  C CG2 . VAL A 604  ? 0.2695 0.2474 0.2733 0.0443  0.0012  -0.0442 602  VAL A CG2 
4207  N N   . GLY A 605  ? 0.2676 0.2646 0.2672 0.0543  0.0002  -0.0602 603  GLY A N   
4208  C CA  . GLY A 605  ? 0.2640 0.2680 0.2602 0.0563  0.0008  -0.0635 603  GLY A CA  
4209  C C   . GLY A 605  ? 0.2729 0.2737 0.2713 0.0582  -0.0029 -0.0690 603  GLY A C   
4210  O O   . GLY A 605  ? 0.2958 0.2897 0.2988 0.0585  -0.0059 -0.0708 603  GLY A O   
4211  N N   . SER A 606  ? 0.2917 0.2977 0.2868 0.0595  -0.0027 -0.0715 604  SER A N   
4212  C CA  . SER A 606  ? 0.3009 0.3051 0.2978 0.0615  -0.0061 -0.0772 604  SER A CA  
4213  C C   . SER A 606  ? 0.2862 0.2901 0.2797 0.0597  -0.0060 -0.0757 604  SER A C   
4214  O O   . SER A 606  ? 0.2833 0.2929 0.2720 0.0588  -0.0031 -0.0727 604  SER A O   
4215  C CB  . SER A 606  ? 0.3484 0.3606 0.3451 0.0661  -0.0066 -0.0839 604  SER A CB  
4216  O OG  . SER A 606  ? 0.4809 0.4922 0.4817 0.0682  -0.0076 -0.0863 604  SER A OG  
4217  N N   . VAL A 607  ? 0.3107 0.3081 0.3069 0.0590  -0.0093 -0.0777 605  VAL A N   
4218  C CA  . VAL A 607  ? 0.3016 0.2989 0.2951 0.0576  -0.0096 -0.0771 605  VAL A CA  
4219  C C   . VAL A 607  ? 0.3225 0.3211 0.3175 0.0605  -0.0129 -0.0842 605  VAL A C   
4220  O O   . VAL A 607  ? 0.3236 0.3173 0.3234 0.0619  -0.0161 -0.0882 605  VAL A O   
4221  C CB  . VAL A 607  ? 0.2713 0.2601 0.2666 0.0535  -0.0104 -0.0724 605  VAL A CB  
4222  C CG1 . VAL A 607  ? 0.3018 0.2822 0.3030 0.0531  -0.0138 -0.0741 605  VAL A CG1 
4223  C CG2 . VAL A 607  ? 0.2738 0.2631 0.2667 0.0524  -0.0111 -0.0725 605  VAL A CG2 
4224  N N   . THR A 608  ? 0.3148 0.3202 0.3055 0.0617  -0.0121 -0.0859 606  THR A N   
4225  C CA  . THR A 608  ? 0.3185 0.3252 0.3099 0.0640  -0.0151 -0.0922 606  THR A CA  
4226  C C   . THR A 608  ? 0.3122 0.3146 0.3031 0.0610  -0.0161 -0.0898 606  THR A C   
4227  O O   . THR A 608  ? 0.3173 0.3222 0.3038 0.0590  -0.0136 -0.0850 606  THR A O   
4228  C CB  . THR A 608  ? 0.3107 0.3286 0.2975 0.0674  -0.0136 -0.0957 606  THR A CB  
4229  O OG1 . THR A 608  ? 0.3446 0.3669 0.3323 0.0701  -0.0125 -0.0979 606  THR A OG1 
4230  C CG2 . THR A 608  ? 0.3724 0.3922 0.3598 0.0699  -0.0168 -0.1025 606  THR A CG2 
4231  N N   . GLU A 609  ? 0.3350 0.3307 0.3303 0.0606  -0.0199 -0.0929 607  GLU A N   
4232  C CA  . GLU A 609  ? 0.3513 0.3419 0.3471 0.0572  -0.0209 -0.0900 607  GLU A CA  
4233  C C   . GLU A 609  ? 0.3503 0.3449 0.3443 0.0587  -0.0227 -0.0944 607  GLU A C   
4234  O O   . GLU A 609  ? 0.3653 0.3644 0.3595 0.0623  -0.0243 -0.1008 607  GLU A O   
4235  C CB  . GLU A 609  ? 0.3882 0.3686 0.3902 0.0550  -0.0238 -0.0894 607  GLU A CB  
4236  C CG  . GLU A 609  ? 0.3906 0.3673 0.3932 0.0526  -0.0215 -0.0832 607  GLU A CG  
4237  C CD  . GLU A 609  ? 0.5132 0.4803 0.5215 0.0503  -0.0240 -0.0818 607  GLU A CD  
4238  O OE1 . GLU A 609  ? 0.5500 0.5131 0.5628 0.0515  -0.0278 -0.0865 607  GLU A OE1 
4239  O OE2 . GLU A 609  ? 0.4739 0.4374 0.4822 0.0471  -0.0223 -0.0758 607  GLU A OE2 
4240  N N   . THR A 610  ? 0.3267 0.3203 0.3188 0.0559  -0.0222 -0.0909 608  THR A N   
4241  C CA  . THR A 610  ? 0.3255 0.3238 0.3149 0.0569  -0.0232 -0.0938 608  THR A CA  
4242  C C   . THR A 610  ? 0.3473 0.3406 0.3416 0.0570  -0.0277 -0.0989 608  THR A C   
4243  O O   . THR A 610  ? 0.3649 0.3501 0.3638 0.0541  -0.0295 -0.0969 608  THR A O   
4244  C CB  . THR A 610  ? 0.3398 0.3387 0.3255 0.0540  -0.0210 -0.0878 608  THR A CB  
4245  O OG1 . THR A 610  ? 0.2946 0.2966 0.2767 0.0535  -0.0171 -0.0826 608  THR A OG1 
4246  C CG2 . THR A 610  ? 0.3226 0.3278 0.3047 0.0553  -0.0217 -0.0903 608  THR A CG2 
4247  N N   . SER A 611  ? 0.3663 0.3647 0.3598 0.0601  -0.0297 -0.1053 609  SER A N   
4248  C CA  . SER A 611  ? 0.3914 0.3857 0.3893 0.0601  -0.0341 -0.1103 609  SER A CA  
4249  C C   . SER A 611  ? 0.3788 0.3720 0.3756 0.0569  -0.0342 -0.1071 609  SER A C   
4250  O O   . SER A 611  ? 0.3701 0.3680 0.3618 0.0562  -0.0313 -0.1029 609  SER A O   
4251  C CB  . SER A 611  ? 0.4102 0.4112 0.4072 0.0645  -0.0361 -0.1183 609  SER A CB  
4252  O OG  . SER A 611  ? 0.3733 0.3826 0.3644 0.0655  -0.0345 -0.1182 609  SER A OG  
4253  N N   . GLU A 612  ? 0.3796 0.3663 0.3817 0.0550  -0.0378 -0.1089 610  GLU A N   
4254  C CA  . GLU A 612  ? 0.4294 0.4157 0.4310 0.0523  -0.0384 -0.1068 610  GLU A CA  
4255  C C   . GLU A 612  ? 0.3872 0.3822 0.3837 0.0548  -0.0381 -0.1098 610  GLU A C   
4256  O O   . GLU A 612  ? 0.3822 0.3799 0.3753 0.0532  -0.0365 -0.1061 610  GLU A O   
4257  C CB  . GLU A 612  ? 0.4514 0.4302 0.4598 0.0502  -0.0427 -0.1093 610  GLU A CB  
4258  N N   . GLU A 613  ? 0.3341 0.3341 0.3299 0.0588  -0.0396 -0.1165 611  GLU A N   
4259  C CA  . GLU A 613  ? 0.3813 0.3904 0.3720 0.0614  -0.0394 -0.1195 611  GLU A CA  
4260  C C   . GLU A 613  ? 0.3682 0.3841 0.3518 0.0618  -0.0348 -0.1143 611  GLU A C   
4261  O O   . GLU A 613  ? 0.4035 0.4241 0.3829 0.0614  -0.0338 -0.1123 611  GLU A O   
4262  C CB  . GLU A 613  ? 0.3767 0.3900 0.3681 0.0658  -0.0419 -0.1281 611  GLU A CB  
4263  N N   . ASP A 614  ? 0.3853 0.4017 0.3677 0.0624  -0.0321 -0.1117 612  ASP A N   
4264  C CA  . ASP A 614  ? 0.3592 0.3819 0.3353 0.0627  -0.0278 -0.1066 612  ASP A CA  
4265  C C   . ASP A 614  ? 0.3283 0.3474 0.3033 0.0587  -0.0258 -0.0990 612  ASP A C   
4266  O O   . ASP A 614  ? 0.3356 0.3599 0.3053 0.0586  -0.0234 -0.0953 612  ASP A O   
4267  C CB  . ASP A 614  ? 0.3889 0.4132 0.3647 0.0642  -0.0256 -0.1061 612  ASP A CB  
4268  C CG  . ASP A 614  ? 0.4402 0.4720 0.4147 0.0688  -0.0265 -0.1131 612  ASP A CG  
4269  O OD1 . ASP A 614  ? 0.4674 0.5056 0.4388 0.0708  -0.0275 -0.1167 612  ASP A OD1 
4270  O OD2 . ASP A 614  ? 0.4318 0.4634 0.4083 0.0705  -0.0262 -0.1152 612  ASP A OD2 
4271  N N   . ALA A 615  ? 0.3250 0.3352 0.3049 0.0556  -0.0268 -0.0965 613  ALA A N   
4272  C CA  . ALA A 615  ? 0.3495 0.3564 0.3289 0.0519  -0.0253 -0.0900 613  ALA A CA  
4273  C C   . ALA A 615  ? 0.3286 0.3390 0.3058 0.0518  -0.0264 -0.0907 613  ALA A C   
4274  O O   . ALA A 615  ? 0.3288 0.3420 0.3018 0.0508  -0.0242 -0.0860 613  ALA A O   
4275  C CB  . ALA A 615  ? 0.3733 0.3708 0.3588 0.0487  -0.0268 -0.0883 613  ALA A CB  
4276  N N   . ARG A 616  ? 0.3421 0.3523 0.3221 0.0527  -0.0300 -0.0965 614  ARG A N   
4277  C CA  . ARG A 616  ? 0.3662 0.3800 0.3443 0.0527  -0.0313 -0.0976 614  ARG A CA  
4278  C C   . ARG A 616  ? 0.3588 0.3822 0.3300 0.0557  -0.0296 -0.0981 614  ARG A C   
4279  O O   . ARG A 616  ? 0.3340 0.3608 0.3016 0.0552  -0.0288 -0.0954 614  ARG A O   
4280  C CB  . ARG A 616  ? 0.4096 0.4212 0.3926 0.0531  -0.0358 -0.1042 614  ARG A CB  
4281  C CG  . ARG A 616  ? 0.4630 0.4653 0.4529 0.0496  -0.0378 -0.1031 614  ARG A CG  
4282  C CD  . ARG A 616  ? 0.4927 0.4930 0.4874 0.0495  -0.0423 -0.1091 614  ARG A CD  
4283  N NE  . ARG A 616  ? 0.5935 0.5959 0.5890 0.0532  -0.0445 -0.1163 614  ARG A NE  
4284  C CZ  . ARG A 616  ? 0.5733 0.5702 0.5740 0.0535  -0.0466 -0.1194 614  ARG A CZ  
4285  N NH1 . ARG A 616  ? 0.6141 0.6027 0.6196 0.0502  -0.0468 -0.1157 614  ARG A NH1 
4286  N NH2 . ARG A 616  ? 0.5358 0.5355 0.5370 0.0573  -0.0486 -0.1264 614  ARG A NH2 
4287  N N   . ARG A 617  ? 0.3354 0.3633 0.3047 0.0589  -0.0290 -0.1015 615  ARG A N   
4288  C CA  . ARG A 617  ? 0.3442 0.3819 0.3068 0.0616  -0.0271 -0.1015 615  ARG A CA  
4289  C C   . ARG A 617  ? 0.3305 0.3694 0.2888 0.0600  -0.0231 -0.0936 615  ARG A C   
4290  O O   . ARG A 617  ? 0.3194 0.3642 0.2724 0.0606  -0.0219 -0.0912 615  ARG A O   
4291  C CB  . ARG A 617  ? 0.3573 0.3999 0.3192 0.0653  -0.0271 -0.1067 615  ARG A CB  
4292  C CG  . ARG A 617  ? 0.4513 0.5050 0.4064 0.0683  -0.0255 -0.1076 615  ARG A CG  
4293  C CD  . ARG A 617  ? 0.5348 0.5941 0.4900 0.0724  -0.0270 -0.1153 615  ARG A CD  
4294  N NE  . ARG A 617  ? 0.5358 0.5927 0.4937 0.0729  -0.0258 -0.1158 615  ARG A NE  
4295  C CZ  . ARG A 617  ? 0.6100 0.6721 0.5642 0.0739  -0.0224 -0.1128 615  ARG A CZ  
4296  N NH1 . ARG A 617  ? 0.5361 0.6058 0.4839 0.0742  -0.0196 -0.1088 615  ARG A NH1 
4297  N NH2 . ARG A 617  ? 0.5047 0.5643 0.4620 0.0745  -0.0217 -0.1139 615  ARG A NH2 
4298  N N   . ALA A 618  ? 0.3244 0.3575 0.2849 0.0579  -0.0212 -0.0895 616  ALA A N   
4299  C CA  . ALA A 618  ? 0.2933 0.3267 0.2504 0.0562  -0.0177 -0.0821 616  ALA A CA  
4300  C C   . ALA A 618  ? 0.3095 0.3417 0.2654 0.0540  -0.0178 -0.0781 616  ALA A C   
4301  O O   . ALA A 618  ? 0.2915 0.3278 0.2425 0.0541  -0.0157 -0.0738 616  ALA A O   
4302  C CB  . ALA A 618  ? 0.2821 0.3088 0.2427 0.0541  -0.0162 -0.0788 616  ALA A CB  
4303  N N   . VAL A 619  ? 0.3076 0.3343 0.2679 0.0522  -0.0204 -0.0795 617  VAL A N   
4304  C CA  . VAL A 619  ? 0.3173 0.3433 0.2767 0.0503  -0.0205 -0.0761 617  VAL A CA  
4305  C C   . VAL A 619  ? 0.2873 0.3211 0.2419 0.0526  -0.0213 -0.0779 617  VAL A C   
4306  O O   . VAL A 619  ? 0.3025 0.3388 0.2535 0.0522  -0.0200 -0.0736 617  VAL A O   
4307  C CB  . VAL A 619  ? 0.3035 0.3228 0.2689 0.0478  -0.0232 -0.0774 617  VAL A CB  
4308  C CG1 . VAL A 619  ? 0.3136 0.3331 0.2781 0.0461  -0.0233 -0.0741 617  VAL A CG1 
4309  C CG2 . VAL A 619  ? 0.3202 0.3321 0.2899 0.0454  -0.0224 -0.0750 617  VAL A CG2 
4310  N N   . ARG A 620  ? 0.2892 0.3271 0.2439 0.0553  -0.0235 -0.0844 618  ARG A N   
4311  C CA  . ARG A 620  ? 0.3388 0.3846 0.2887 0.0576  -0.0243 -0.0864 618  ARG A CA  
4312  C C   . ARG A 620  ? 0.3362 0.3888 0.2796 0.0592  -0.0212 -0.0826 618  ARG A C   
4313  O O   . ARG A 620  ? 0.3301 0.3874 0.2690 0.0597  -0.0207 -0.0801 618  ARG A O   
4314  C CB  . ARG A 620  ? 0.3256 0.3747 0.2771 0.0603  -0.0274 -0.0946 618  ARG A CB  
4315  C CG  . ARG A 620  ? 0.4460 0.4896 0.4035 0.0586  -0.0310 -0.0982 618  ARG A CG  
4316  C CD  . ARG A 620  ? 0.5141 0.5607 0.4734 0.0613  -0.0345 -0.1066 618  ARG A CD  
4317  N NE  . ARG A 620  ? 0.5661 0.6068 0.5312 0.0610  -0.0361 -0.1103 618  ARG A NE  
4318  C CZ  . ARG A 620  ? 0.5095 0.5525 0.4742 0.0637  -0.0358 -0.1140 618  ARG A CZ  
4319  N NH1 . ARG A 620  ? 0.6077 0.6595 0.5665 0.0668  -0.0340 -0.1149 618  ARG A NH1 
4320  N NH2 . ARG A 620  ? 0.5136 0.5501 0.4840 0.0633  -0.0374 -0.1170 618  ARG A NH2 
4321  N N   . LEU A 621  ? 0.2924 0.3455 0.2353 0.0598  -0.0190 -0.0819 619  LEU A N   
4322  C CA  . LEU A 621  ? 0.3270 0.3863 0.2641 0.0608  -0.0158 -0.0777 619  LEU A CA  
4323  C C   . LEU A 621  ? 0.3380 0.3942 0.2734 0.0582  -0.0137 -0.0699 619  LEU A C   
4324  O O   . LEU A 621  ? 0.3324 0.3940 0.2625 0.0588  -0.0122 -0.0662 619  LEU A O   
4325  C CB  . LEU A 621  ? 0.3029 0.3630 0.2405 0.0618  -0.0140 -0.0787 619  LEU A CB  
4326  C CG  . LEU A 621  ? 0.3397 0.4049 0.2777 0.0651  -0.0157 -0.0863 619  LEU A CG  
4327  C CD1 . LEU A 621  ? 0.3826 0.4463 0.3230 0.0655  -0.0142 -0.0870 619  LEU A CD1 
4328  C CD2 . LEU A 621  ? 0.3744 0.4506 0.3060 0.0679  -0.0150 -0.0872 619  LEU A CD2 
4329  N N   . ALA A 622  ? 0.2926 0.3403 0.2324 0.0553  -0.0135 -0.0673 620  ALA A N   
4330  C CA  . ALA A 622  ? 0.2908 0.3352 0.2297 0.0529  -0.0118 -0.0604 620  ALA A CA  
4331  C C   . ALA A 622  ? 0.3157 0.3621 0.2526 0.0530  -0.0133 -0.0596 620  ALA A C   
4332  O O   . ALA A 622  ? 0.3124 0.3607 0.2455 0.0526  -0.0119 -0.0545 620  ALA A O   
4333  C CB  . ALA A 622  ? 0.2765 0.3119 0.2208 0.0500  -0.0117 -0.0587 620  ALA A CB  
4334  N N   . ALA A 623  ? 0.2929 0.3388 0.2325 0.0533  -0.0164 -0.0645 621  ALA A N   
4335  C CA  . ALA A 623  ? 0.3107 0.3591 0.2486 0.0536  -0.0180 -0.0642 621  ALA A CA  
4336  C C   . ALA A 623  ? 0.3199 0.3770 0.2512 0.0562  -0.0174 -0.0636 621  ALA A C   
4337  O O   . ALA A 623  ? 0.3224 0.3814 0.2504 0.0561  -0.0171 -0.0596 621  ALA A O   
4338  C CB  . ALA A 623  ? 0.3318 0.3789 0.2740 0.0537  -0.0215 -0.0702 621  ALA A CB  
4339  N N   . ASP A 624  ? 0.3467 0.4094 0.2760 0.0587  -0.0173 -0.0675 622  ASP A N   
4340  C CA  . ASP A 624  ? 0.3865 0.4584 0.3092 0.0612  -0.0167 -0.0671 622  ASP A CA  
4341  C C   . ASP A 624  ? 0.3816 0.4546 0.3002 0.0603  -0.0135 -0.0596 622  ASP A C   
4342  O O   . ASP A 624  ? 0.4683 0.5462 0.3820 0.0611  -0.0132 -0.0564 622  ASP A O   
4343  C CB  . ASP A 624  ? 0.4082 0.4860 0.3299 0.0640  -0.0170 -0.0730 622  ASP A CB  
4344  C CG  . ASP A 624  ? 0.5241 0.6015 0.4496 0.0652  -0.0206 -0.0808 622  ASP A CG  
4345  O OD1 . ASP A 624  ? 0.5720 0.6472 0.4993 0.0643  -0.0229 -0.0815 622  ASP A OD1 
4346  O OD2 . ASP A 624  ? 0.6280 0.7074 0.5548 0.0670  -0.0213 -0.0863 622  ASP A OD2 
4347  N N   . ALA A 625  ? 0.4012 0.4694 0.3219 0.0586  -0.0112 -0.0567 623  ALA A N   
4348  C CA  . ALA A 625  ? 0.4352 0.5039 0.3526 0.0575  -0.0082 -0.0497 623  ALA A CA  
4349  C C   . ALA A 625  ? 0.3879 0.4506 0.3063 0.0551  -0.0079 -0.0440 623  ALA A C   
4350  O O   . ALA A 625  ? 0.3738 0.4365 0.2895 0.0542  -0.0058 -0.0381 623  ALA A O   
4351  C CB  . ALA A 625  ? 0.4625 0.5291 0.3818 0.0568  -0.0060 -0.0493 623  ALA A CB  
4352  N N   . ALA A 626  ? 0.3743 0.4320 0.2966 0.0540  -0.0101 -0.0457 624  ALA A N   
4353  C CA  . ALA A 626  ? 0.3274 0.3792 0.2513 0.0518  -0.0097 -0.0408 624  ALA A CA  
4354  C C   . ALA A 626  ? 0.3496 0.4048 0.2686 0.0523  -0.0093 -0.0358 624  ALA A C   
4355  O O   . ALA A 626  ? 0.3873 0.4391 0.3060 0.0508  -0.0077 -0.0301 624  ALA A O   
4356  C CB  . ALA A 626  ? 0.3334 0.3806 0.2622 0.0507  -0.0123 -0.0440 624  ALA A CB  
4357  N N   . PRO A 627  ? 0.3971 0.4588 0.3124 0.0545  -0.0109 -0.0374 625  PRO A N   
4358  C CA  . PRO A 627  ? 0.4098 0.4743 0.3204 0.0549  -0.0106 -0.0320 625  PRO A CA  
4359  C C   . PRO A 627  ? 0.3966 0.4633 0.3034 0.0547  -0.0078 -0.0268 625  PRO A C   
4360  O O   . PRO A 627  ? 0.4238 0.4887 0.3289 0.0538  -0.0070 -0.0208 625  PRO A O   
4361  C CB  . PRO A 627  ? 0.4484 0.5205 0.3558 0.0576  -0.0129 -0.0357 625  PRO A CB  
4362  C CG  . PRO A 627  ? 0.4255 0.4959 0.3374 0.0578  -0.0150 -0.0427 625  PRO A CG  
4363  C CD  . PRO A 627  ? 0.3995 0.4656 0.3150 0.0565  -0.0134 -0.0441 625  PRO A CD  
4364  N N   . ASP A 628  ? 0.4009 0.4717 0.3065 0.0555  -0.0063 -0.0288 626  ASP A N   
4365  C CA  . ASP A 628  ? 0.4037 0.4773 0.3057 0.0551  -0.0036 -0.0238 626  ASP A CA  
4366  C C   . ASP A 628  ? 0.4188 0.4848 0.3240 0.0524  -0.0017 -0.0193 626  ASP A C   
4367  O O   . ASP A 628  ? 0.4089 0.4744 0.3118 0.0513  -0.0003 -0.0131 626  ASP A O   
4368  C CB  . ASP A 628  ? 0.3975 0.4777 0.2979 0.0567  -0.0025 -0.0276 626  ASP A CB  
4369  C CG  . ASP A 628  ? 0.5046 0.5941 0.4006 0.0596  -0.0039 -0.0311 626  ASP A CG  
4370  O OD1 . ASP A 628  ? 0.5590 0.6496 0.4531 0.0602  -0.0058 -0.0303 626  ASP A OD1 
4371  O OD2 . ASP A 628  ? 0.5121 0.6081 0.4066 0.0613  -0.0032 -0.0347 626  ASP A OD2 
4372  N N   . TRP A 629  ? 0.3628 0.4226 0.2733 0.0511  -0.0019 -0.0222 627  TRP A N   
4373  C CA  . TRP A 629  ? 0.3100 0.3628 0.2236 0.0486  -0.0002 -0.0182 627  TRP A CA  
4374  C C   . TRP A 629  ? 0.3764 0.4241 0.2909 0.0474  -0.0011 -0.0143 627  TRP A C   
4375  O O   . TRP A 629  ? 0.3331 0.3776 0.2473 0.0459  0.0003  -0.0090 627  TRP A O   
4376  C CB  . TRP A 629  ? 0.3233 0.3712 0.2421 0.0477  -0.0003 -0.0223 627  TRP A CB  
4377  C CG  . TRP A 629  ? 0.3087 0.3498 0.2306 0.0452  0.0013  -0.0185 627  TRP A CG  
4378  C CD1 . TRP A 629  ? 0.2780 0.3119 0.2044 0.0435  0.0006  -0.0187 627  TRP A CD1 
4379  C CD2 . TRP A 629  ? 0.3028 0.3438 0.2232 0.0441  0.0039  -0.0138 627  TRP A CD2 
4380  N NE1 . TRP A 629  ? 0.2769 0.3064 0.2047 0.0415  0.0025  -0.0147 627  TRP A NE1 
4381  C CE2 . TRP A 629  ? 0.2682 0.3018 0.1926 0.0419  0.0045  -0.0117 627  TRP A CE2 
4382  C CE3 . TRP A 629  ? 0.3048 0.3518 0.2211 0.0447  0.0057  -0.0112 627  TRP A CE3 
4383  C CZ2 . TRP A 629  ? 0.2821 0.3136 0.2066 0.0402  0.0067  -0.0073 627  TRP A CZ2 
4384  C CZ3 . TRP A 629  ? 0.3322 0.3772 0.2488 0.0430  0.0080  -0.0066 627  TRP A CZ3 
4385  C CH2 . TRP A 629  ? 0.3375 0.3747 0.2583 0.0408  0.0084  -0.0048 627  TRP A CH2 
4386  N N   . ALA A 630  ? 0.3365 0.3836 0.2521 0.0481  -0.0036 -0.0171 628  ALA A N   
4387  C CA  . ALA A 630  ? 0.3730 0.4162 0.2895 0.0473  -0.0047 -0.0138 628  ALA A CA  
4388  C C   . ALA A 630  ? 0.3749 0.4209 0.2865 0.0479  -0.0042 -0.0082 628  ALA A C   
4389  O O   . ALA A 630  ? 0.3649 0.4067 0.2772 0.0469  -0.0043 -0.0039 628  ALA A O   
4390  C CB  . ALA A 630  ? 0.3650 0.4086 0.2833 0.0482  -0.0074 -0.0181 628  ALA A CB  
4391  N N   . ALA A 631  ? 0.3566 0.4100 0.2634 0.0495  -0.0038 -0.0081 629  ALA A N   
4392  C CA  . ALA A 631  ? 0.4113 0.4681 0.3132 0.0501  -0.0036 -0.0026 629  ALA A CA  
4393  C C   . ALA A 631  ? 0.3628 0.4179 0.2638 0.0483  -0.0010 0.0031  629  ALA A C   
4394  O O   . ALA A 631  ? 0.3813 0.4372 0.2792 0.0482  -0.0008 0.0087  629  ALA A O   
4395  C CB  . ALA A 631  ? 0.4302 0.4964 0.3271 0.0525  -0.0042 -0.0046 629  ALA A CB  
4396  N N   . VAL A 632  ? 0.3807 0.4334 0.2845 0.0470  0.0009  0.0019  630  VAL A N   
4397  C CA  . VAL A 632  ? 0.3417 0.3920 0.2454 0.0451  0.0033  0.0071  630  VAL A CA  
4398  C C   . VAL A 632  ? 0.3686 0.4111 0.2751 0.0435  0.0027  0.0109  630  VAL A C   
4399  O O   . VAL A 632  ? 0.3410 0.3780 0.2517 0.0429  0.0017  0.0081  630  VAL A O   
4400  C CB  . VAL A 632  ? 0.3577 0.4074 0.2641 0.0443  0.0052  0.0044  630  VAL A CB  
4401  C CG1 . VAL A 632  ? 0.3252 0.3719 0.2322 0.0420  0.0075  0.0096  630  VAL A CG1 
4402  C CG2 . VAL A 632  ? 0.3278 0.3861 0.2312 0.0462  0.0056  0.0005  630  VAL A CG2 
4403  N N   . PRO A 633  ? 0.3648 0.4065 0.2690 0.0428  0.0030  0.0170  631  PRO A N   
4404  C CA  . PRO A 633  ? 0.3160 0.3504 0.2228 0.0417  0.0021  0.0203  631  PRO A CA  
4405  C C   . PRO A 633  ? 0.3641 0.3919 0.2759 0.0397  0.0032  0.0193  631  PRO A C   
4406  O O   . PRO A 633  ? 0.3032 0.3316 0.2157 0.0387  0.0053  0.0190  631  PRO A O   
4407  C CB  . PRO A 633  ? 0.3730 0.4082 0.2764 0.0411  0.0026  0.0272  631  PRO A CB  
4408  C CG  . PRO A 633  ? 0.3486 0.3927 0.2469 0.0424  0.0031  0.0274  631  PRO A CG  
4409  C CD  . PRO A 633  ? 0.3527 0.4004 0.2520 0.0430  0.0042  0.0214  631  PRO A CD  
4410  N N   . PRO A 634  ? 0.3100 0.3318 0.2254 0.0393  0.0019  0.0186  632  PRO A N   
4411  C CA  . PRO A 634  ? 0.2969 0.3129 0.2170 0.0375  0.0029  0.0174  632  PRO A CA  
4412  C C   . PRO A 634  ? 0.2976 0.3114 0.2181 0.0356  0.0050  0.0213  632  PRO A C   
4413  O O   . PRO A 634  ? 0.2855 0.2975 0.2087 0.0344  0.0065  0.0195  632  PRO A O   
4414  C CB  . PRO A 634  ? 0.3157 0.3266 0.2386 0.0375  0.0011  0.0176  632  PRO A CB  
4415  C CG  . PRO A 634  ? 0.3686 0.3834 0.2890 0.0396  -0.0011 0.0164  632  PRO A CG  
4416  C CD  . PRO A 634  ? 0.3198 0.3408 0.2351 0.0406  -0.0006 0.0186  632  PRO A CD  
4417  N N   . SER A 635  ? 0.3017 0.3153 0.2199 0.0352  0.0052  0.0268  633  SER A N   
4418  C CA  . SER A 635  ? 0.3313 0.3426 0.2501 0.0332  0.0071  0.0307  633  SER A CA  
4419  C C   . SER A 635  ? 0.3248 0.3415 0.2419 0.0329  0.0092  0.0300  633  SER A C   
4420  O O   . SER A 635  ? 0.2900 0.3048 0.2091 0.0312  0.0110  0.0310  633  SER A O   
4421  C CB  . SER A 635  ? 0.3738 0.3839 0.2905 0.0328  0.0064  0.0369  633  SER A CB  
4422  O OG  . SER A 635  ? 0.4644 0.4812 0.3762 0.0340  0.0063  0.0387  633  SER A OG  
4423  N N   . GLU A 636  ? 0.2845 0.3081 0.1981 0.0346  0.0091  0.0281  634  GLU A N   
4424  C CA  . GLU A 636  ? 0.3160 0.3456 0.2281 0.0347  0.0111  0.0266  634  GLU A CA  
4425  C C   . GLU A 636  ? 0.2921 0.3205 0.2077 0.0349  0.0114  0.0207  634  GLU A C   
4426  O O   . GLU A 636  ? 0.3061 0.3354 0.2229 0.0341  0.0132  0.0201  634  GLU A O   
4427  C CB  . GLU A 636  ? 0.3363 0.3742 0.2434 0.0366  0.0107  0.0263  634  GLU A CB  
4428  N N   . ARG A 637  ? 0.2964 0.3225 0.2138 0.0359  0.0095  0.0166  635  ARG A N   
4429  C CA  . ARG A 637  ? 0.2885 0.3121 0.2099 0.0357  0.0096  0.0116  635  ARG A CA  
4430  C C   . ARG A 637  ? 0.2727 0.2901 0.1979 0.0335  0.0108  0.0134  635  ARG A C   
4431  O O   . ARG A 637  ? 0.2927 0.3097 0.2200 0.0329  0.0120  0.0113  635  ARG A O   
4432  C CB  . ARG A 637  ? 0.2793 0.3012 0.2024 0.0367  0.0073  0.0076  635  ARG A CB  
4433  C CG  . ARG A 637  ? 0.3034 0.3315 0.2229 0.0390  0.0058  0.0055  635  ARG A CG  
4434  C CD  . ARG A 637  ? 0.3104 0.3373 0.2322 0.0399  0.0036  0.0005  635  ARG A CD  
4435  N NE  . ARG A 637  ? 0.3136 0.3347 0.2382 0.0389  0.0024  0.0016  635  ARG A NE  
4436  C CZ  . ARG A 637  ? 0.3261 0.3476 0.2500 0.0399  0.0005  0.0017  635  ARG A CZ  
4437  N NH1 . ARG A 637  ? 0.3629 0.3900 0.2829 0.0418  -0.0006 0.0012  635  ARG A NH1 
4438  N NH2 . ARG A 637  ? 0.3353 0.3517 0.2624 0.0390  -0.0005 0.0022  635  ARG A NH2 
4439  N N   . ALA A 638  ? 0.2866 0.2992 0.2127 0.0324  0.0103  0.0173  636  ALA A N   
4440  C CA  . ALA A 638  ? 0.2687 0.2756 0.1981 0.0303  0.0114  0.0191  636  ALA A CA  
4441  C C   . ALA A 638  ? 0.2809 0.2899 0.2094 0.0292  0.0136  0.0219  636  ALA A C   
4442  O O   . ALA A 638  ? 0.2580 0.2645 0.1894 0.0278  0.0148  0.0214  636  ALA A O   
4443  C CB  . ALA A 638  ? 0.2754 0.2772 0.2058 0.0296  0.0103  0.0225  636  ALA A CB  
4444  N N   . ALA A 639  ? 0.2968 0.3108 0.2214 0.0296  0.0142  0.0251  637  ALA A N   
4445  C CA  . ALA A 639  ? 0.2925 0.3097 0.2161 0.0284  0.0164  0.0278  637  ALA A CA  
4446  C C   . ALA A 639  ? 0.2965 0.3174 0.2211 0.0290  0.0176  0.0234  637  ALA A C   
4447  O O   . ALA A 639  ? 0.2868 0.3077 0.2130 0.0277  0.0193  0.0242  637  ALA A O   
4448  C CB  . ALA A 639  ? 0.3033 0.3261 0.2223 0.0288  0.0167  0.0320  637  ALA A CB  
4449  N N   . CYS A 640  ? 0.2650 0.2890 0.1887 0.0311  0.0166  0.0185  638  CYS A N   
4450  C CA  . CYS A 640  ? 0.2668 0.2933 0.1921 0.0319  0.0173  0.0138  638  CYS A CA  
4451  C C   . CYS A 640  ? 0.2944 0.3144 0.2246 0.0304  0.0175  0.0125  638  CYS A C   
4452  O O   . CYS A 640  ? 0.2749 0.2957 0.2068 0.0299  0.0190  0.0117  638  CYS A O   
4453  C CB  . CYS A 640  ? 0.3017 0.3312 0.2262 0.0342  0.0156  0.0085  638  CYS A CB  
4454  S SG  . CYS A 640  ? 0.3325 0.3713 0.2512 0.0363  0.0155  0.0088  638  CYS A SG  
4455  N N   . LEU A 641  ? 0.2608 0.2746 0.1932 0.0299  0.0160  0.0122  639  LEU A N   
4456  C CA  . LEU A 641  ? 0.2517 0.2596 0.1885 0.0284  0.0161  0.0113  639  LEU A CA  
4457  C C   . LEU A 641  ? 0.2632 0.2694 0.2010 0.0265  0.0179  0.0153  639  LEU A C   
4458  O O   . LEU A 641  ? 0.2483 0.2532 0.1887 0.0257  0.0189  0.0141  639  LEU A O   
4459  C CB  . LEU A 641  ? 0.2498 0.2523 0.1885 0.0281  0.0144  0.0109  639  LEU A CB  
4460  C CG  . LEU A 641  ? 0.2871 0.2890 0.2275 0.0291  0.0128  0.0059  639  LEU A CG  
4461  C CD1 . LEU A 641  ? 0.2746 0.2824 0.2120 0.0312  0.0119  0.0034  639  LEU A CD1 
4462  C CD2 . LEU A 641  ? 0.2560 0.2531 0.1986 0.0284  0.0113  0.0060  639  LEU A CD2 
4463  N N   . ASP A 642  ? 0.2847 0.2906 0.2206 0.0257  0.0182  0.0201  640  ASP A N   
4464  C CA  . ASP A 642  ? 0.2907 0.2945 0.2278 0.0236  0.0196  0.0240  640  ASP A CA  
4465  C C   . ASP A 642  ? 0.2840 0.2932 0.2204 0.0235  0.0216  0.0240  640  ASP A C   
4466  O O   . ASP A 642  ? 0.2628 0.2704 0.2017 0.0220  0.0228  0.0249  640  ASP A O   
4467  C CB  . ASP A 642  ? 0.2909 0.2933 0.2262 0.0228  0.0192  0.0291  640  ASP A CB  
4468  C CG  . ASP A 642  ? 0.3283 0.3241 0.2656 0.0224  0.0175  0.0295  640  ASP A CG  
4469  O OD1 . ASP A 642  ? 0.3074 0.2993 0.2481 0.0220  0.0172  0.0269  640  ASP A OD1 
4470  O OD2 . ASP A 642  ? 0.3263 0.3212 0.2618 0.0227  0.0164  0.0325  640  ASP A OD2 
4471  N N   . ARG A 643  ? 0.2800 0.2962 0.2130 0.0250  0.0220  0.0231  641  ARG A N   
4472  C CA  . ARG A 643  ? 0.2882 0.3105 0.2206 0.0251  0.0239  0.0227  641  ARG A CA  
4473  C C   . ARG A 643  ? 0.2654 0.2869 0.2010 0.0258  0.0241  0.0177  641  ARG A C   
4474  O O   . ARG A 643  ? 0.3031 0.3263 0.2404 0.0251  0.0257  0.0179  641  ARG A O   
4475  C CB  . ARG A 643  ? 0.2737 0.3042 0.2017 0.0269  0.0242  0.0224  641  ARG A CB  
4476  C CG  . ARG A 643  ? 0.3359 0.3692 0.2606 0.0258  0.0249  0.0283  641  ARG A CG  
4477  C CD  . ARG A 643  ? 0.3278 0.3704 0.2479 0.0274  0.0254  0.0282  641  ARG A CD  
4478  N NE  . ARG A 643  ? 0.3309 0.3750 0.2492 0.0299  0.0236  0.0241  641  ARG A NE  
4479  C CZ  . ARG A 643  ? 0.3321 0.3760 0.2476 0.0305  0.0221  0.0260  641  ARG A CZ  
4480  N NH1 . ARG A 643  ? 0.3272 0.3694 0.2412 0.0290  0.0221  0.0320  641  ARG A NH1 
4481  N NH2 . ARG A 643  ? 0.3339 0.3793 0.2481 0.0328  0.0204  0.0217  641  ARG A NH2 
4482  N N   . ALA A 644  ? 0.2537 0.2729 0.1905 0.0272  0.0224  0.0134  642  ALA A N   
4483  C CA  . ALA A 644  ? 0.2497 0.2671 0.1899 0.0277  0.0222  0.0089  642  ALA A CA  
4484  C C   . ALA A 644  ? 0.2610 0.2723 0.2048 0.0256  0.0226  0.0106  642  ALA A C   
4485  O O   . ALA A 644  ? 0.2449 0.2563 0.1912 0.0254  0.0234  0.0090  642  ALA A O   
4486  C CB  . ALA A 644  ? 0.2828 0.2983 0.2237 0.0292  0.0200  0.0044  642  ALA A CB  
4487  N N   . ALA A 645  ? 0.2529 0.2591 0.1973 0.0241  0.0221  0.0138  643  ALA A N   
4488  C CA  . ALA A 645  ? 0.2569 0.2576 0.2045 0.0221  0.0225  0.0155  643  ALA A CA  
4489  C C   . ALA A 645  ? 0.2661 0.2694 0.2140 0.0209  0.0245  0.0182  643  ALA A C   
4490  O O   . ALA A 645  ? 0.2759 0.2775 0.2268 0.0200  0.0251  0.0175  643  ALA A O   
4491  C CB  . ALA A 645  ? 0.2718 0.2673 0.2197 0.0210  0.0215  0.0183  643  ALA A CB  
4492  N N   . GLU A 646  ? 0.2711 0.2787 0.2160 0.0206  0.0254  0.0215  644  GLU A N   
4493  C CA  . GLU A 646  ? 0.2929 0.3039 0.2381 0.0193  0.0274  0.0243  644  GLU A CA  
4494  C C   . GLU A 646  ? 0.2908 0.3066 0.2369 0.0205  0.0284  0.0207  644  GLU A C   
4495  O O   . GLU A 646  ? 0.2839 0.3000 0.2324 0.0194  0.0296  0.0213  644  GLU A O   
4496  C CB  . GLU A 646  ? 0.3165 0.3321 0.2581 0.0189  0.0282  0.0285  644  GLU A CB  
4497  C CG  . GLU A 646  ? 0.3903 0.4011 0.3311 0.0177  0.0270  0.0325  644  GLU A CG  
4498  C CD  . GLU A 646  ? 0.4332 0.4383 0.3772 0.0153  0.0272  0.0353  644  GLU A CD  
4499  O OE1 . GLU A 646  ? 0.4802 0.4875 0.4254 0.0139  0.0288  0.0369  644  GLU A OE1 
4500  O OE2 . GLU A 646  ? 0.4123 0.4110 0.3577 0.0149  0.0257  0.0356  644  GLU A OE2 
4501  N N   . LEU A 647  ? 0.2974 0.3173 0.2418 0.0229  0.0279  0.0169  645  LEU A N   
4502  C CA  . LEU A 647  ? 0.2833 0.3079 0.2288 0.0244  0.0286  0.0129  645  LEU A CA  
4503  C C   . LEU A 647  ? 0.3083 0.3276 0.2581 0.0243  0.0279  0.0101  645  LEU A C   
4504  O O   . LEU A 647  ? 0.2809 0.3022 0.2327 0.0243  0.0289  0.0090  645  LEU A O   
4505  C CB  . LEU A 647  ? 0.2747 0.3042 0.2177 0.0271  0.0277  0.0090  645  LEU A CB  
4506  C CG  . LEU A 647  ? 0.3182 0.3550 0.2565 0.0277  0.0286  0.0113  645  LEU A CG  
4507  C CD1 . LEU A 647  ? 0.2945 0.3354 0.2306 0.0305  0.0273  0.0069  645  LEU A CD1 
4508  C CD2 . LEU A 647  ? 0.3230 0.3669 0.2610 0.0273  0.0310  0.0129  645  LEU A CD2 
4509  N N   . MET A 648  ? 0.2511 0.2639 0.2021 0.0242  0.0261  0.0088  646  MET A N   
4510  C CA  . MET A 648  ? 0.3042 0.3119 0.2592 0.0238  0.0253  0.0066  646  MET A CA  
4511  C C   . MET A 648  ? 0.2749 0.2799 0.2321 0.0216  0.0264  0.0098  646  MET A C   
4512  O O   . MET A 648  ? 0.2827 0.2866 0.2428 0.0215  0.0266  0.0083  646  MET A O   
4513  C CB  . MET A 648  ? 0.2671 0.2690 0.2230 0.0238  0.0233  0.0052  646  MET A CB  
4514  C CG  . MET A 648  ? 0.2918 0.2957 0.2467 0.0259  0.0219  0.0011  646  MET A CG  
4515  S SD  . MET A 648  ? 0.2941 0.2910 0.2518 0.0256  0.0195  -0.0013 646  MET A SD  
4516  C CE  . MET A 648  ? 0.3085 0.3093 0.2643 0.0281  0.0180  -0.0057 646  MET A CE  
4517  N N   . GLN A 649  ? 0.2733 0.2769 0.2293 0.0198  0.0270  0.0142  647  GLN A N   
4518  C CA  . GLN A 649  ? 0.2498 0.2507 0.2080 0.0176  0.0279  0.0172  647  GLN A CA  
4519  C C   . GLN A 649  ? 0.2821 0.2885 0.2408 0.0175  0.0297  0.0176  647  GLN A C   
4520  O O   . GLN A 649  ? 0.2780 0.2831 0.2398 0.0167  0.0301  0.0172  647  GLN A O   
4521  C CB  . GLN A 649  ? 0.2799 0.2784 0.2367 0.0159  0.0279  0.0217  647  GLN A CB  
4522  C CG  . GLN A 649  ? 0.2606 0.2559 0.2201 0.0136  0.0285  0.0245  647  GLN A CG  
4523  C CD  . GLN A 649  ? 0.2770 0.2658 0.2393 0.0131  0.0273  0.0231  647  GLN A CD  
4524  O OE1 . GLN A 649  ? 0.2902 0.2749 0.2523 0.0127  0.0261  0.0239  647  GLN A OE1 
4525  N NE2 . GLN A 649  ? 0.2805 0.2689 0.2454 0.0131  0.0275  0.0210  647  GLN A NE2 
4526  N N   . ALA A 650  ? 0.2763 0.2895 0.2322 0.0183  0.0307  0.0183  648  ALA A N   
4527  C CA  . ALA A 650  ? 0.3475 0.3672 0.3039 0.0183  0.0326  0.0186  648  ALA A CA  
4528  C C   . ALA A 650  ? 0.3111 0.3323 0.2698 0.0202  0.0324  0.0137  648  ALA A C   
4529  O O   . ALA A 650  ? 0.3615 0.3850 0.3224 0.0198  0.0335  0.0136  648  ALA A O   
4530  C CB  . ALA A 650  ? 0.2816 0.3088 0.2341 0.0190  0.0337  0.0200  648  ALA A CB  
4531  N N   . ARG A 651  ? 0.2876 0.3074 0.2459 0.0223  0.0308  0.0096  649  ARG A N   
4532  C CA  . ARG A 651  ? 0.3000 0.3211 0.2606 0.0244  0.0302  0.0048  649  ARG A CA  
4533  C C   . ARG A 651  ? 0.2920 0.3058 0.2563 0.0237  0.0289  0.0035  649  ARG A C   
4534  O O   . ARG A 651  ? 0.2803 0.2938 0.2468 0.0254  0.0279  -0.0004 649  ARG A O   
4535  C CB  . ARG A 651  ? 0.3257 0.3493 0.2842 0.0269  0.0290  0.0008  649  ARG A CB  
4536  C CG  . ARG A 651  ? 0.4293 0.4571 0.3892 0.0296  0.0288  -0.0041 649  ARG A CG  
4537  C CD  . ARG A 651  ? 0.4175 0.4519 0.3741 0.0320  0.0286  -0.0068 649  ARG A CD  
4538  N NE  . ARG A 651  ? 0.3857 0.4227 0.3442 0.0348  0.0277  -0.0125 649  ARG A NE  
4539  C CZ  . ARG A 651  ? 0.4307 0.4734 0.3904 0.0361  0.0288  -0.0143 649  ARG A CZ  
4540  N NH1 . ARG A 651  ? 0.4511 0.4978 0.4106 0.0345  0.0311  -0.0106 649  ARG A NH1 
4541  N NH2 . ARG A 651  ? 0.4596 0.5043 0.4210 0.0390  0.0276  -0.0199 649  ARG A NH2 
4542  N N   . MET A 652  ? 0.2820 0.2900 0.2470 0.0215  0.0287  0.0067  650  MET A N   
4543  C CA  . MET A 652  ? 0.2483 0.2497 0.2165 0.0208  0.0273  0.0057  650  MET A CA  
4544  C C   . MET A 652  ? 0.2719 0.2739 0.2433 0.0215  0.0274  0.0035  650  MET A C   
4545  O O   . MET A 652  ? 0.2935 0.2922 0.2668 0.0225  0.0258  0.0004  650  MET A O   
4546  C CB  . MET A 652  ? 0.2618 0.2583 0.2304 0.0183  0.0274  0.0096  650  MET A CB  
4547  C CG  . MET A 652  ? 0.2774 0.2680 0.2491 0.0175  0.0263  0.0087  650  MET A CG  
4548  S SD  . MET A 652  ? 0.3360 0.3214 0.3083 0.0148  0.0263  0.0126  650  MET A SD  
4549  C CE  . MET A 652  ? 0.2929 0.2756 0.2630 0.0153  0.0249  0.0123  650  MET A CE  
4550  N N   . PRO A 653  ? 0.2766 0.2826 0.2488 0.0210  0.0290  0.0048  651  PRO A N   
4551  C CA  . PRO A 653  ? 0.2904 0.2969 0.2660 0.0218  0.0288  0.0025  651  PRO A CA  
4552  C C   . PRO A 653  ? 0.2738 0.2824 0.2499 0.0248  0.0277  -0.0024 651  PRO A C   
4553  O O   . PRO A 653  ? 0.2839 0.2889 0.2628 0.0256  0.0262  -0.0048 651  PRO A O   
4554  C CB  . PRO A 653  ? 0.2963 0.3085 0.2721 0.0209  0.0310  0.0048  651  PRO A CB  
4555  C CG  . PRO A 653  ? 0.3224 0.3337 0.2960 0.0186  0.0319  0.0093  651  PRO A CG  
4556  C CD  . PRO A 653  ? 0.2764 0.2867 0.2470 0.0195  0.0310  0.0086  651  PRO A CD  
4557  N N   . THR A 654  ? 0.2551 0.2696 0.2287 0.0265  0.0282  -0.0039 652  THR A N   
4558  C CA  . THR A 654  ? 0.2735 0.2900 0.2475 0.0295  0.0269  -0.0090 652  THR A CA  
4559  C C   . THR A 654  ? 0.2823 0.2923 0.2569 0.0298  0.0245  -0.0110 652  THR A C   
4560  O O   . THR A 654  ? 0.2621 0.2697 0.2393 0.0313  0.0227  -0.0145 652  THR A O   
4561  C CB  . THR A 654  ? 0.2921 0.3167 0.2629 0.0311  0.0281  -0.0101 652  THR A CB  
4562  O OG1 . THR A 654  ? 0.2697 0.3007 0.2402 0.0305  0.0304  -0.0079 652  THR A OG1 
4563  C CG2 . THR A 654  ? 0.2923 0.3194 0.2639 0.0345  0.0266  -0.0159 652  THR A CG2 
4564  N N   . LEU A 655  ? 0.2524 0.2596 0.2247 0.0284  0.0243  -0.0087 653  LEU A N   
4565  C CA  . LEU A 655  ? 0.2641 0.2654 0.2370 0.0284  0.0221  -0.0102 653  LEU A CA  
4566  C C   . LEU A 655  ? 0.2857 0.2806 0.2622 0.0272  0.0209  -0.0100 653  LEU A C   
4567  O O   . LEU A 655  ? 0.2680 0.2592 0.2465 0.0280  0.0189  -0.0128 653  LEU A O   
4568  C CB  . LEU A 655  ? 0.2373 0.2370 0.2074 0.0269  0.0222  -0.0073 653  LEU A CB  
4569  C CG  . LEU A 655  ? 0.2804 0.2861 0.2467 0.0280  0.0230  -0.0073 653  LEU A CG  
4570  C CD1 . LEU A 655  ? 0.2695 0.2728 0.2333 0.0267  0.0228  -0.0044 653  LEU A CD1 
4571  C CD2 . LEU A 655  ? 0.2998 0.3082 0.2659 0.0308  0.0216  -0.0124 653  LEU A CD2 
4572  N N   . LEU A 656  ? 0.2804 0.2739 0.2579 0.0253  0.0221  -0.0067 654  LEU A N   
4573  C CA  . LEU A 656  ? 0.2948 0.2829 0.2755 0.0242  0.0211  -0.0063 654  LEU A CA  
4574  C C   . LEU A 656  ? 0.3063 0.2946 0.2899 0.0262  0.0198  -0.0100 654  LEU A C   
4575  O O   . LEU A 656  ? 0.2951 0.2784 0.2810 0.0262  0.0179  -0.0113 654  LEU A O   
4576  C CB  . LEU A 656  ? 0.3006 0.2886 0.2820 0.0223  0.0227  -0.0028 654  LEU A CB  
4577  C CG  . LEU A 656  ? 0.2932 0.2803 0.2726 0.0201  0.0237  0.0011  654  LEU A CG  
4578  C CD1 . LEU A 656  ? 0.2788 0.2652 0.2598 0.0182  0.0248  0.0039  654  LEU A CD1 
4579  C CD2 . LEU A 656  ? 0.3093 0.2914 0.2883 0.0193  0.0223  0.0014  654  LEU A CD2 
4580  N N   . GLY A 657  ? 0.2668 0.2609 0.2505 0.0280  0.0209  -0.0116 655  GLY A N   
4581  C CA  . GLY A 657  ? 0.2748 0.2693 0.2615 0.0301  0.0196  -0.0152 655  GLY A CA  
4582  C C   . GLY A 657  ? 0.2476 0.2399 0.2349 0.0320  0.0172  -0.0192 655  GLY A C   
4583  O O   . GLY A 657  ? 0.2760 0.2647 0.2665 0.0329  0.0152  -0.0214 655  GLY A O   
4584  N N   . LEU A 658  ? 0.2519 0.2463 0.2363 0.0325  0.0173  -0.0201 656  LEU A N   
4585  C CA  . LEU A 658  ? 0.2506 0.2432 0.2357 0.0342  0.0149  -0.0241 656  LEU A CA  
4586  C C   . LEU A 658  ? 0.2350 0.2199 0.2218 0.0324  0.0130  -0.0230 656  LEU A C   
4587  O O   . LEU A 658  ? 0.2561 0.2372 0.2458 0.0332  0.0106  -0.0257 656  LEU A O   
4588  C CB  . LEU A 658  ? 0.2430 0.2405 0.2243 0.0353  0.0155  -0.0251 656  LEU A CB  
4589  C CG  . LEU A 658  ? 0.2767 0.2733 0.2584 0.0372  0.0131  -0.0296 656  LEU A CG  
4590  C CD1 . LEU A 658  ? 0.2524 0.2494 0.2374 0.0398  0.0114  -0.0343 656  LEU A CD1 
4591  C CD2 . LEU A 658  ? 0.2416 0.2444 0.2192 0.0383  0.0141  -0.0304 656  LEU A CD2 
4592  N N   . ILE A 659  ? 0.2634 0.2460 0.2485 0.0298  0.0139  -0.0190 657  ILE A N   
4593  C CA  . ILE A 659  ? 0.2565 0.2327 0.2430 0.0278  0.0124  -0.0177 657  ILE A CA  
4594  C C   . ILE A 659  ? 0.2338 0.2058 0.2240 0.0272  0.0114  -0.0173 657  ILE A C   
4595  O O   . ILE A 659  ? 0.2450 0.2122 0.2375 0.0268  0.0092  -0.0182 657  ILE A O   
4596  C CB  . ILE A 659  ? 0.2273 0.2027 0.2115 0.0254  0.0138  -0.0136 657  ILE A CB  
4597  C CG1 . ILE A 659  ? 0.2557 0.2348 0.2363 0.0262  0.0144  -0.0141 657  ILE A CG1 
4598  C CG2 . ILE A 659  ? 0.2554 0.2249 0.2412 0.0234  0.0125  -0.0122 657  ILE A CG2 
4599  C CD1 . ILE A 659  ? 0.2920 0.2710 0.2701 0.0243  0.0158  -0.0102 657  ILE A CD1 
4600  N N   . ILE A 660  ? 0.2334 0.2072 0.2241 0.0270  0.0129  -0.0157 658  ILE A N   
4601  C CA  . ILE A 660  ? 0.2268 0.1972 0.2209 0.0266  0.0119  -0.0152 658  ILE A CA  
4602  C C   . ILE A 660  ? 0.2500 0.2189 0.2470 0.0288  0.0095  -0.0192 658  ILE A C   
4603  O O   . ILE A 660  ? 0.2703 0.2339 0.2700 0.0281  0.0074  -0.0191 658  ILE A O   
4604  C CB  . ILE A 660  ? 0.2336 0.2073 0.2278 0.0264  0.0139  -0.0133 658  ILE A CB  
4605  C CG1 . ILE A 660  ? 0.2470 0.2203 0.2393 0.0237  0.0157  -0.0090 658  ILE A CG1 
4606  C CG2 . ILE A 660  ? 0.2533 0.2246 0.2510 0.0269  0.0126  -0.0139 658  ILE A CG2 
4607  C CD1 . ILE A 660  ? 0.3032 0.2805 0.2951 0.0234  0.0178  -0.0073 658  ILE A CD1 
4608  N N   . ARG A 661  ? 0.2322 0.2057 0.2287 0.0315  0.0096  -0.0227 659  ARG A N   
4609  C CA  . ARG A 661  ? 0.2691 0.2415 0.2688 0.0340  0.0072  -0.0269 659  ARG A CA  
4610  C C   . ARG A 661  ? 0.2925 0.2617 0.2927 0.0346  0.0048  -0.0296 659  ARG A C   
4611  O O   . ARG A 661  ? 0.2747 0.2395 0.2784 0.0352  0.0021  -0.0316 659  ARG A O   
4612  C CB  . ARG A 661  ? 0.2646 0.2438 0.2641 0.0370  0.0082  -0.0299 659  ARG A CB  
4613  C CG  . ARG A 661  ? 0.2848 0.2661 0.2855 0.0368  0.0097  -0.0280 659  ARG A CG  
4614  C CD  . ARG A 661  ? 0.2626 0.2517 0.2631 0.0396  0.0110  -0.0308 659  ARG A CD  
4615  N NE  . ARG A 661  ? 0.2953 0.2852 0.2981 0.0430  0.0088  -0.0363 659  ARG A NE  
4616  C CZ  . ARG A 661  ? 0.2887 0.2839 0.2897 0.0454  0.0090  -0.0400 659  ARG A CZ  
4617  N NH1 . ARG A 661  ? 0.3133 0.3134 0.3102 0.0446  0.0112  -0.0385 659  ARG A NH1 
4618  N NH2 . ARG A 661  ? 0.2726 0.2683 0.2762 0.0487  0.0067  -0.0453 659  ARG A NH2 
4619  N N   . GLU A 662  ? 0.2379 0.2095 0.2350 0.0342  0.0055  -0.0298 660  GLU A N   
4620  C CA  . GLU A 662  ? 0.2598 0.2290 0.2575 0.0348  0.0032  -0.0327 660  GLU A CA  
4621  C C   . GLU A 662  ? 0.2394 0.2020 0.2383 0.0320  0.0018  -0.0301 660  GLU A C   
4622  O O   . GLU A 662  ? 0.2461 0.2045 0.2478 0.0321  -0.0009 -0.0322 660  GLU A O   
4623  C CB  . GLU A 662  ? 0.2805 0.2549 0.2743 0.0357  0.0043  -0.0340 660  GLU A CB  
4624  C CG  . GLU A 662  ? 0.2886 0.2608 0.2831 0.0363  0.0018  -0.0372 660  GLU A CG  
4625  C CD  . GLU A 662  ? 0.2919 0.2694 0.2825 0.0374  0.0026  -0.0387 660  GLU A CD  
4626  O OE1 . GLU A 662  ? 0.2952 0.2761 0.2823 0.0363  0.0051  -0.0354 660  GLU A OE1 
4627  O OE2 . GLU A 662  ? 0.2938 0.2721 0.2850 0.0393  0.0007  -0.0431 660  GLU A OE2 
4628  N N   . ALA A 663  ? 0.2535 0.2155 0.2507 0.0294  0.0036  -0.0257 661  ALA A N   
4629  C CA  . ALA A 663  ? 0.2623 0.2194 0.2603 0.0266  0.0027  -0.0232 661  ALA A CA  
4630  C C   . ALA A 663  ? 0.2785 0.2316 0.2789 0.0248  0.0024  -0.0202 661  ALA A C   
4631  O O   . ALA A 663  ? 0.2875 0.2367 0.2888 0.0224  0.0015  -0.0181 661  ALA A O   
4632  C CB  . ALA A 663  ? 0.2525 0.2117 0.2470 0.0251  0.0046  -0.0206 661  ALA A CB  
4633  N N   . GLY A 664  ? 0.2624 0.2166 0.2638 0.0258  0.0031  -0.0200 662  GLY A N   
4634  C CA  . GLY A 664  ? 0.2712 0.2219 0.2748 0.0242  0.0027  -0.0173 662  GLY A CA  
4635  C C   . GLY A 664  ? 0.2593 0.2101 0.2610 0.0217  0.0047  -0.0130 662  GLY A C   
4636  O O   . GLY A 664  ? 0.2909 0.2384 0.2941 0.0198  0.0041  -0.0105 662  GLY A O   
4637  N N   . LYS A 665  ? 0.2915 0.2462 0.2899 0.0216  0.0070  -0.0120 663  LYS A N   
4638  C CA  . LYS A 665  ? 0.2687 0.2235 0.2654 0.0193  0.0088  -0.0083 663  LYS A CA  
4639  C C   . LYS A 665  ? 0.2653 0.2222 0.2620 0.0192  0.0104  -0.0066 663  LYS A C   
4640  O O   . LYS A 665  ? 0.2295 0.1895 0.2265 0.0211  0.0109  -0.0083 663  LYS A O   
4641  C CB  . LYS A 665  ? 0.2711 0.2287 0.2645 0.0192  0.0101  -0.0080 663  LYS A CB  
4642  C CG  . LYS A 665  ? 0.2826 0.2384 0.2758 0.0190  0.0085  -0.0095 663  LYS A CG  
4643  C CD  . LYS A 665  ? 0.3953 0.3528 0.3855 0.0180  0.0098  -0.0078 663  LYS A CD  
4644  C CE  . LYS A 665  ? 0.3894 0.3446 0.3801 0.0170  0.0083  -0.0082 663  LYS A CE  
4645  N NZ  . LYS A 665  ? 0.3674 0.3240 0.3554 0.0161  0.0095  -0.0065 663  LYS A NZ  
4646  N N   . SER A 666  ? 0.2798 0.2353 0.2762 0.0171  0.0112  -0.0034 664  SER A N   
4647  C CA  . SER A 666  ? 0.2510 0.2086 0.2472 0.0168  0.0129  -0.0016 664  SER A CA  
4648  C C   . SER A 666  ? 0.2937 0.2554 0.2871 0.0169  0.0150  -0.0010 664  SER A C   
4649  O O   . SER A 666  ? 0.2627 0.2251 0.2541 0.0170  0.0153  -0.0013 664  SER A O   
4650  C CB  . SER A 666  ? 0.2937 0.2488 0.2905 0.0145  0.0129  0.0013  664  SER A CB  
4651  O OG  . SER A 666  ? 0.3160 0.2708 0.3108 0.0130  0.0137  0.0029  664  SER A OG  
4652  N N   . ALA A 667  ? 0.2408 0.2053 0.2344 0.0169  0.0165  0.0001  665  ALA A N   
4653  C CA  . ALA A 667  ? 0.2740 0.2424 0.2652 0.0168  0.0185  0.0012  665  ALA A CA  
4654  C C   . ALA A 667  ? 0.2836 0.2503 0.2728 0.0150  0.0190  0.0035  665  ALA A C   
4655  O O   . ALA A 667  ? 0.2313 0.1997 0.2181 0.0153  0.0197  0.0036  665  ALA A O   
4656  C CB  . ALA A 667  ? 0.2837 0.2549 0.2758 0.0166  0.0199  0.0023  665  ALA A CB  
4657  N N   . LEU A 668  ? 0.2329 0.1964 0.2230 0.0133  0.0186  0.0053  666  LEU A N   
4658  C CA  . LEU A 668  ? 0.2563 0.2185 0.2448 0.0117  0.0190  0.0073  666  LEU A CA  
4659  C C   . LEU A 668  ? 0.2859 0.2469 0.2731 0.0121  0.0182  0.0062  666  LEU A C   
4660  O O   . LEU A 668  ? 0.2677 0.2294 0.2528 0.0119  0.0188  0.0071  666  LEU A O   
4661  C CB  . LEU A 668  ? 0.3272 0.2865 0.3171 0.0101  0.0186  0.0089  666  LEU A CB  
4662  C CG  . LEU A 668  ? 0.4353 0.3954 0.4251 0.0088  0.0198  0.0110  666  LEU A CG  
4663  C CD1 . LEU A 668  ? 0.4738 0.4319 0.4653 0.0076  0.0192  0.0119  666  LEU A CD1 
4664  C CD2 . LEU A 668  ? 0.4221 0.3823 0.4098 0.0082  0.0205  0.0122  666  LEU A CD2 
4665  N N   . ASN A 669  ? 0.2643 0.2236 0.2529 0.0127  0.0166  0.0043  667  ASN A N   
4666  C CA  . ASN A 669  ? 0.2842 0.2426 0.2718 0.0130  0.0156  0.0031  667  ASN A CA  
4667  C C   . ASN A 669  ? 0.2533 0.2148 0.2390 0.0147  0.0160  0.0014  667  ASN A C   
4668  O O   . ASN A 669  ? 0.2598 0.2217 0.2438 0.0148  0.0158  0.0012  667  ASN A O   
4669  C CB  . ASN A 669  ? 0.2742 0.2297 0.2641 0.0129  0.0136  0.0017  667  ASN A CB  
4670  C CG  . ASN A 669  ? 0.3788 0.3316 0.3701 0.0109  0.0132  0.0037  667  ASN A CG  
4671  O OD1 . ASN A 669  ? 0.3813 0.3322 0.3749 0.0107  0.0121  0.0036  667  ASN A OD1 
4672  N ND2 . ASN A 669  ? 0.3822 0.3350 0.3722 0.0096  0.0139  0.0055  667  ASN A ND2 
4673  N N   . ALA A 670  ? 0.2314 0.1957 0.2174 0.0162  0.0165  0.0002  668  ALA A N   
4674  C CA  . ALA A 670  ? 0.2431 0.2113 0.2270 0.0179  0.0171  -0.0013 668  ALA A CA  
4675  C C   . ALA A 670  ? 0.2712 0.2417 0.2524 0.0171  0.0188  0.0012  668  ALA A C   
4676  O O   . ALA A 670  ? 0.2574 0.2299 0.2362 0.0178  0.0189  0.0008  668  ALA A O   
4677  C CB  . ALA A 670  ? 0.3048 0.2761 0.2899 0.0197  0.0174  -0.0034 668  ALA A CB  
4678  N N   . ILE A 671  ? 0.2515 0.2218 0.2331 0.0157  0.0200  0.0039  669  ILE A N   
4679  C CA  . ILE A 671  ? 0.2459 0.2173 0.2253 0.0148  0.0213  0.0066  669  ILE A CA  
4680  C C   . ILE A 671  ? 0.2582 0.2272 0.2363 0.0142  0.0205  0.0071  669  ILE A C   
4681  O O   . ILE A 671  ? 0.2549 0.2255 0.2306 0.0146  0.0208  0.0079  669  ILE A O   
4682  C CB  . ILE A 671  ? 0.2586 0.2292 0.2392 0.0131  0.0222  0.0091  669  ILE A CB  
4683  C CG1 . ILE A 671  ? 0.2648 0.2390 0.2466 0.0138  0.0232  0.0086  669  ILE A CG1 
4684  C CG2 . ILE A 671  ? 0.2290 0.1997 0.2079 0.0120  0.0231  0.0119  669  ILE A CG2 
4685  C CD1 . ILE A 671  ? 0.2716 0.2447 0.2553 0.0123  0.0238  0.0104  669  ILE A CD1 
4686  N N   . ALA A 672  ? 0.2507 0.2161 0.2305 0.0133  0.0194  0.0069  670  ALA A N   
4687  C CA  . ALA A 672  ? 0.2559 0.2193 0.2348 0.0127  0.0186  0.0074  670  ALA A CA  
4688  C C   . ALA A 672  ? 0.2402 0.2051 0.2177 0.0141  0.0178  0.0053  670  ALA A C   
4689  O O   . ALA A 672  ? 0.2497 0.2148 0.2254 0.0142  0.0176  0.0060  670  ALA A O   
4690  C CB  . ALA A 672  ? 0.2878 0.2479 0.2689 0.0115  0.0176  0.0073  670  ALA A CB  
4691  N N   . GLU A 673  ? 0.2579 0.2236 0.2362 0.0153  0.0171  0.0028  671  GLU A N   
4692  C CA  . GLU A 673  ? 0.2595 0.2267 0.2367 0.0168  0.0161  0.0004  671  GLU A CA  
4693  C C   . GLU A 673  ? 0.2768 0.2481 0.2509 0.0179  0.0172  0.0007  671  GLU A C   
4694  O O   . GLU A 673  ? 0.2474 0.2198 0.2197 0.0185  0.0167  0.0004  671  GLU A O   
4695  C CB  . GLU A 673  ? 0.2492 0.2161 0.2285 0.0179  0.0149  -0.0027 671  GLU A CB  
4696  C CG  . GLU A 673  ? 0.3265 0.2959 0.3045 0.0197  0.0140  -0.0057 671  GLU A CG  
4697  C CD  . GLU A 673  ? 0.3581 0.3247 0.3385 0.0199  0.0118  -0.0084 671  GLU A CD  
4698  O OE1 . GLU A 673  ? 0.3971 0.3611 0.3804 0.0194  0.0112  -0.0086 671  GLU A OE1 
4699  O OE2 . GLU A 673  ? 0.3041 0.2713 0.2838 0.0205  0.0107  -0.0102 671  GLU A OE2 
4700  N N   . VAL A 674  ? 0.2338 0.2080 0.2074 0.0183  0.0186  0.0015  672  VAL A N   
4701  C CA  . VAL A 674  ? 0.2390 0.2176 0.2096 0.0191  0.0197  0.0025  672  VAL A CA  
4702  C C   . VAL A 674  ? 0.2403 0.2177 0.2092 0.0179  0.0201  0.0057  672  VAL A C   
4703  O O   . VAL A 674  ? 0.2253 0.2047 0.1916 0.0185  0.0201  0.0062  672  VAL A O   
4704  C CB  . VAL A 674  ? 0.2437 0.2261 0.2143 0.0195  0.0213  0.0029  672  VAL A CB  
4705  C CG1 . VAL A 674  ? 0.2268 0.2142 0.1940 0.0202  0.0225  0.0044  672  VAL A CG1 
4706  C CG2 . VAL A 674  ? 0.2433 0.2271 0.2158 0.0212  0.0206  -0.0008 672  VAL A CG2 
4707  N N   . ARG A 675  ? 0.2216 0.1956 0.1920 0.0162  0.0204  0.0079  673  ARG A N   
4708  C CA  . ARG A 675  ? 0.2355 0.2079 0.2047 0.0151  0.0205  0.0107  673  ARG A CA  
4709  C C   . ARG A 675  ? 0.2340 0.2051 0.2024 0.0156  0.0192  0.0097  673  ARG A C   
4710  O O   . ARG A 675  ? 0.2359 0.2077 0.2022 0.0158  0.0191  0.0112  673  ARG A O   
4711  C CB  . ARG A 675  ? 0.2273 0.1963 0.1987 0.0134  0.0208  0.0124  673  ARG A CB  
4712  C CG  . ARG A 675  ? 0.2189 0.1893 0.1909 0.0126  0.0222  0.0142  673  ARG A CG  
4713  C CD  . ARG A 675  ? 0.2551 0.2222 0.2289 0.0109  0.0222  0.0160  673  ARG A CD  
4714  N NE  . ARG A 675  ? 0.2793 0.2448 0.2519 0.0104  0.0219  0.0181  673  ARG A NE  
4715  C CZ  . ARG A 675  ? 0.2855 0.2477 0.2594 0.0093  0.0214  0.0190  673  ARG A CZ  
4716  N NH1 . ARG A 675  ? 0.2532 0.2138 0.2294 0.0085  0.0213  0.0182  673  ARG A NH1 
4717  N NH2 . ARG A 675  ? 0.2514 0.2122 0.2243 0.0091  0.0210  0.0206  673  ARG A NH2 
4718  N N   . GLU A 676  ? 0.2523 0.2216 0.2224 0.0157  0.0179  0.0073  674  GLU A N   
4719  C CA  . GLU A 676  ? 0.2227 0.1910 0.1925 0.0160  0.0166  0.0062  674  GLU A CA  
4720  C C   . GLU A 676  ? 0.2234 0.1951 0.1907 0.0177  0.0162  0.0048  674  GLU A C   
4721  O O   . GLU A 676  ? 0.2244 0.1965 0.1901 0.0180  0.0156  0.0054  674  GLU A O   
4722  C CB  . GLU A 676  ? 0.2193 0.1853 0.1918 0.0155  0.0154  0.0040  674  GLU A CB  
4723  C CG  . GLU A 676  ? 0.3055 0.2706 0.2781 0.0154  0.0140  0.0031  674  GLU A CG  
4724  C CD  . GLU A 676  ? 0.3859 0.3489 0.3614 0.0145  0.0127  0.0014  674  GLU A CD  
4725  O OE1 . GLU A 676  ? 0.4656 0.4275 0.4430 0.0142  0.0128  0.0009  674  GLU A OE1 
4726  O OE2 . GLU A 676  ? 0.5208 0.4832 0.4969 0.0142  0.0117  0.0008  674  GLU A OE2 
4727  N N   . ALA A 677  ? 0.2248 0.1994 0.1917 0.0189  0.0165  0.0030  675  ALA A N   
4728  C CA  . ALA A 677  ? 0.2276 0.2062 0.1919 0.0206  0.0162  0.0015  675  ALA A CA  
4729  C C   . ALA A 677  ? 0.2403 0.2212 0.2014 0.0207  0.0172  0.0047  675  ALA A C   
4730  O O   . ALA A 677  ? 0.2312 0.2137 0.1900 0.0215  0.0166  0.0047  675  ALA A O   
4731  C CB  . ALA A 677  ? 0.2290 0.2106 0.1936 0.0220  0.0164  -0.0012 675  ALA A CB  
4732  N N   . ILE A 678  ? 0.2469 0.2279 0.2080 0.0197  0.0187  0.0075  676  ILE A N   
4733  C CA  . ILE A 678  ? 0.2313 0.2139 0.1900 0.0193  0.0196  0.0110  676  ILE A CA  
4734  C C   . ILE A 678  ? 0.2411 0.2205 0.1995 0.0188  0.0186  0.0126  676  ILE A C   
4735  O O   . ILE A 678  ? 0.2336 0.2145 0.1894 0.0193  0.0183  0.0142  676  ILE A O   
4736  C CB  . ILE A 678  ? 0.2332 0.2158 0.1928 0.0179  0.0212  0.0137  676  ILE A CB  
4737  C CG1 . ILE A 678  ? 0.2545 0.2416 0.2140 0.0188  0.0224  0.0122  676  ILE A CG1 
4738  C CG2 . ILE A 678  ? 0.2352 0.2178 0.1929 0.0170  0.0218  0.0179  676  ILE A CG2 
4739  C CD1 . ILE A 678  ? 0.2520 0.2387 0.2135 0.0174  0.0237  0.0140  676  ILE A CD1 
4740  N N   . ASP A 679  ? 0.2277 0.2028 0.1887 0.0177  0.0180  0.0124  677  ASP A N   
4741  C CA  . ASP A 679  ? 0.2412 0.2134 0.2024 0.0172  0.0170  0.0136  677  ASP A CA  
4742  C C   . ASP A 679  ? 0.2352 0.2086 0.1952 0.0186  0.0156  0.0116  677  ASP A C   
4743  O O   . ASP A 679  ? 0.2300 0.2033 0.1885 0.0190  0.0149  0.0131  677  ASP A O   
4744  C CB  . ASP A 679  ? 0.2242 0.1925 0.1885 0.0159  0.0167  0.0131  677  ASP A CB  
4745  C CG  . ASP A 679  ? 0.2846 0.2514 0.2503 0.0146  0.0179  0.0152  677  ASP A CG  
4746  O OD1 . ASP A 679  ? 0.2686 0.2364 0.2329 0.0143  0.0188  0.0177  677  ASP A OD1 
4747  O OD2 . ASP A 679  ? 0.3183 0.2831 0.2865 0.0137  0.0179  0.0143  677  ASP A OD2 
4748  N N   . PHE A 680  ? 0.2282 0.2026 0.1891 0.0192  0.0149  0.0083  678  PHE A N   
4749  C CA  . PHE A 680  ? 0.2355 0.2114 0.1953 0.0204  0.0135  0.0062  678  PHE A CA  
4750  C C   . PHE A 680  ? 0.2328 0.2125 0.1889 0.0218  0.0136  0.0073  678  PHE A C   
4751  O O   . PHE A 680  ? 0.2354 0.2155 0.1900 0.0225  0.0126  0.0079  678  PHE A O   
4752  C CB  . PHE A 680  ? 0.2554 0.2321 0.2167 0.0210  0.0127  0.0024  678  PHE A CB  
4753  C CG  . PHE A 680  ? 0.2266 0.1999 0.1912 0.0198  0.0118  0.0010  678  PHE A CG  
4754  C CD1 . PHE A 680  ? 0.2257 0.1974 0.1911 0.0192  0.0108  0.0014  678  PHE A CD1 
4755  C CD2 . PHE A 680  ? 0.2259 0.1979 0.1930 0.0193  0.0118  -0.0008 678  PHE A CD2 
4756  C CE1 . PHE A 680  ? 0.2623 0.2317 0.2308 0.0180  0.0101  0.0002  678  PHE A CE1 
4757  C CE2 . PHE A 680  ? 0.2667 0.2358 0.2368 0.0180  0.0108  -0.0017 678  PHE A CE2 
4758  C CZ  . PHE A 680  ? 0.2477 0.2157 0.2185 0.0173  0.0101  -0.0011 678  PHE A CZ  
4759  N N   . LEU A 681  ? 0.2343 0.2172 0.1889 0.0223  0.0148  0.0075  679  LEU A N   
4760  C CA  . LEU A 681  ? 0.2378 0.2252 0.1887 0.0236  0.0151  0.0087  679  LEU A CA  
4761  C C   . LEU A 681  ? 0.2578 0.2440 0.2071 0.0230  0.0151  0.0129  679  LEU A C   
4762  O O   . LEU A 681  ? 0.2433 0.2311 0.1902 0.0240  0.0142  0.0135  679  LEU A O   
4763  C CB  . LEU A 681  ? 0.2389 0.2301 0.1888 0.0238  0.0167  0.0088  679  LEU A CB  
4764  C CG  . LEU A 681  ? 0.2389 0.2324 0.1896 0.0251  0.0164  0.0044  679  LEU A CG  
4765  C CD1 . LEU A 681  ? 0.2391 0.2356 0.1900 0.0250  0.0182  0.0048  679  LEU A CD1 
4766  C CD2 . LEU A 681  ? 0.2568 0.2547 0.2049 0.0271  0.0154  0.0021  679  LEU A CD2 
4767  N N   . ARG A 682  ? 0.2379 0.2211 0.1886 0.0214  0.0161  0.0157  680  ARG A N   
4768  C CA  . ARG A 682  ? 0.2396 0.2211 0.1893 0.0209  0.0159  0.0196  680  ARG A CA  
4769  C C   . ARG A 682  ? 0.2389 0.2170 0.1896 0.0211  0.0142  0.0192  680  ARG A C   
4770  O O   . ARG A 682  ? 0.2456 0.2236 0.1947 0.0216  0.0134  0.0215  680  ARG A O   
4771  C CB  . ARG A 682  ? 0.2386 0.2176 0.1899 0.0191  0.0171  0.0223  680  ARG A CB  
4772  C CG  . ARG A 682  ? 0.2443 0.2273 0.1943 0.0188  0.0188  0.0236  680  ARG A CG  
4773  C CD  . ARG A 682  ? 0.2674 0.2480 0.2196 0.0169  0.0200  0.0257  680  ARG A CD  
4774  N NE  . ARG A 682  ? 0.2701 0.2551 0.2211 0.0165  0.0217  0.0274  680  ARG A NE  
4775  C CZ  . ARG A 682  ? 0.2680 0.2525 0.2209 0.0150  0.0230  0.0287  680  ARG A CZ  
4776  N NH1 . ARG A 682  ? 0.2365 0.2162 0.1925 0.0138  0.0227  0.0286  680  ARG A NH1 
4777  N NH2 . ARG A 682  ? 0.2793 0.2687 0.2311 0.0147  0.0245  0.0300  680  ARG A NH2 
4778  N N   . TYR A 683  ? 0.2356 0.2114 0.1892 0.0208  0.0136  0.0164  681  TYR A N   
4779  C CA  . TYR A 683  ? 0.2355 0.2088 0.1902 0.0210  0.0121  0.0159  681  TYR A CA  
4780  C C   . TYR A 683  ? 0.2545 0.2306 0.2073 0.0226  0.0107  0.0144  681  TYR A C   
4781  O O   . TYR A 683  ? 0.2385 0.2140 0.1905 0.0233  0.0096  0.0158  681  TYR A O   
4782  C CB  . TYR A 683  ? 0.2435 0.2144 0.2017 0.0200  0.0120  0.0135  681  TYR A CB  
4783  C CG  . TYR A 683  ? 0.2649 0.2342 0.2246 0.0202  0.0105  0.0126  681  TYR A CG  
4784  C CD1 . TYR A 683  ? 0.2650 0.2315 0.2257 0.0197  0.0103  0.0145  681  TYR A CD1 
4785  C CD2 . TYR A 683  ? 0.2575 0.2283 0.2177 0.0208  0.0094  0.0097  681  TYR A CD2 
4786  C CE1 . TYR A 683  ? 0.2624 0.2281 0.2247 0.0201  0.0090  0.0134  681  TYR A CE1 
4787  C CE2 . TYR A 683  ? 0.2502 0.2203 0.2121 0.0209  0.0082  0.0089  681  TYR A CE2 
4788  C CZ  . TYR A 683  ? 0.2516 0.2193 0.2144 0.0206  0.0081  0.0107  681  TYR A CZ  
4789  O OH  . TYR A 683  ? 0.2530 0.2206 0.2174 0.0209  0.0069  0.0096  681  TYR A OH  
4790  N N   . TYR A 684  ? 0.2504 0.2295 0.2026 0.0234  0.0106  0.0114  682  TYR A N   
4791  C CA  . TYR A 684  ? 0.2511 0.2331 0.2015 0.0250  0.0092  0.0097  682  TYR A CA  
4792  C C   . TYR A 684  ? 0.2769 0.2620 0.2234 0.0261  0.0092  0.0124  682  TYR A C   
4793  O O   . TYR A 684  ? 0.2539 0.2404 0.1988 0.0273  0.0078  0.0125  682  TYR A O   
4794  C CB  . TYR A 684  ? 0.2389 0.2233 0.1899 0.0255  0.0088  0.0056  682  TYR A CB  
4795  C CG  . TYR A 684  ? 0.2460 0.2274 0.2009 0.0244  0.0084  0.0031  682  TYR A CG  
4796  C CD1 . TYR A 684  ? 0.2453 0.2242 0.2024 0.0237  0.0074  0.0032  682  TYR A CD1 
4797  C CD2 . TYR A 684  ? 0.2373 0.2187 0.1938 0.0240  0.0088  0.0007  682  TYR A CD2 
4798  C CE1 . TYR A 684  ? 0.2354 0.2122 0.1960 0.0224  0.0071  0.0012  682  TYR A CE1 
4799  C CE2 . TYR A 684  ? 0.2316 0.2103 0.1917 0.0228  0.0083  -0.0011 682  TYR A CE2 
4800  C CZ  . TYR A 684  ? 0.2444 0.2209 0.2064 0.0219  0.0075  -0.0007 682  TYR A CZ  
4801  O OH  . TYR A 684  ? 0.2486 0.2229 0.2140 0.0205  0.0070  -0.0022 682  TYR A OH  
4802  N N   . ALA A 685  ? 0.2445 0.2307 0.1894 0.0256  0.0108  0.0149  683  ALA A N   
4803  C CA  . ALA A 685  ? 0.2486 0.2375 0.1899 0.0263  0.0109  0.0183  683  ALA A CA  
4804  C C   . ALA A 685  ? 0.2912 0.2766 0.2327 0.0261  0.0098  0.0214  683  ALA A C   
4805  O O   . ALA A 685  ? 0.2529 0.2399 0.1920 0.0273  0.0086  0.0227  683  ALA A O   
4806  C CB  . ALA A 685  ? 0.2497 0.2405 0.1899 0.0254  0.0129  0.0207  683  ALA A CB  
4807  N N   . GLU A 686  ? 0.2473 0.2280 0.1918 0.0246  0.0102  0.0226  684  GLU A N   
4808  C CA  . GLU A 686  ? 0.2948 0.2719 0.2398 0.0246  0.0090  0.0253  684  GLU A CA  
4809  C C   . GLU A 686  ? 0.2572 0.2341 0.2030 0.0259  0.0071  0.0230  684  GLU A C   
4810  O O   . GLU A 686  ? 0.2551 0.2317 0.1995 0.0270  0.0057  0.0249  684  GLU A O   
4811  C CB  . GLU A 686  ? 0.2936 0.2661 0.2419 0.0229  0.0097  0.0263  684  GLU A CB  
4812  C CG  . GLU A 686  ? 0.3116 0.2799 0.2612 0.0230  0.0083  0.0281  684  GLU A CG  
4813  C CD  . GLU A 686  ? 0.3455 0.3136 0.2928 0.0234  0.0076  0.0325  684  GLU A CD  
4814  O OE1 . GLU A 686  ? 0.3456 0.3168 0.2901 0.0232  0.0085  0.0347  684  GLU A OE1 
4815  O OE2 . GLU A 686  ? 0.3942 0.3591 0.3424 0.0240  0.0060  0.0339  684  GLU A OE2 
4816  N N   . GLN A 687  ? 0.2617 0.2387 0.2097 0.0258  0.0069  0.0191  685  GLN A N   
4817  C CA  . GLN A 687  ? 0.2655 0.2427 0.2145 0.0269  0.0051  0.0168  685  GLN A CA  
4818  C C   . GLN A 687  ? 0.2477 0.2290 0.1934 0.0287  0.0040  0.0165  685  GLN A C   
4819  O O   . GLN A 687  ? 0.2658 0.2473 0.2114 0.0299  0.0023  0.0166  685  GLN A O   
4820  C CB  . GLN A 687  ? 0.2428 0.2200 0.1947 0.0262  0.0052  0.0128  685  GLN A CB  
4821  C CG  . GLN A 687  ? 0.2369 0.2102 0.1921 0.0245  0.0061  0.0130  685  GLN A CG  
4822  C CD  . GLN A 687  ? 0.3038 0.2745 0.2603 0.0248  0.0051  0.0145  685  GLN A CD  
4823  O OE1 . GLN A 687  ? 0.2778 0.2493 0.2349 0.0258  0.0036  0.0132  685  GLN A OE1 
4824  N NE2 . GLN A 687  ? 0.3196 0.2873 0.2766 0.0240  0.0058  0.0171  685  GLN A NE2 
4825  N N   . THR A 688  ? 0.2521 0.2371 0.1953 0.0291  0.0048  0.0161  686  THR A N   
4826  C CA  . THR A 688  ? 0.2657 0.2551 0.2054 0.0308  0.0038  0.0161  686  THR A CA  
4827  C C   . THR A 688  ? 0.2638 0.2527 0.2011 0.0314  0.0032  0.0207  686  THR A C   
4828  O O   . THR A 688  ? 0.2778 0.2681 0.2136 0.0329  0.0014  0.0210  686  THR A O   
4829  C CB  . THR A 688  ? 0.2733 0.2671 0.2107 0.0311  0.0050  0.0149  686  THR A CB  
4830  O OG1 . THR A 688  ? 0.2578 0.2518 0.1976 0.0308  0.0050  0.0104  686  THR A OG1 
4831  C CG2 . THR A 688  ? 0.2586 0.2576 0.1918 0.0329  0.0040  0.0152  686  THR A CG2 
4832  N N   . ARG A 689  ? 0.2705 0.2574 0.2073 0.0302  0.0045  0.0244  687  ARG A N   
4833  C CA  . ARG A 689  ? 0.2797 0.2656 0.2144 0.0304  0.0037  0.0291  687  ARG A CA  
4834  C C   . ARG A 689  ? 0.3134 0.2953 0.2504 0.0311  0.0018  0.0296  687  ARG A C   
4835  O O   . ARG A 689  ? 0.3062 0.2879 0.2413 0.0322  0.0003  0.0324  687  ARG A O   
4836  C CB  . ARG A 689  ? 0.2972 0.2813 0.2320 0.0286  0.0055  0.0329  687  ARG A CB  
4837  C CG  . ARG A 689  ? 0.3343 0.3235 0.2661 0.0283  0.0073  0.0337  687  ARG A CG  
4838  C CD  . ARG A 689  ? 0.2932 0.2807 0.2252 0.0263  0.0087  0.0380  687  ARG A CD  
4839  N NE  . ARG A 689  ? 0.3142 0.2974 0.2502 0.0248  0.0097  0.0368  687  ARG A NE  
4840  C CZ  . ARG A 689  ? 0.3509 0.3356 0.2880 0.0238  0.0115  0.0349  687  ARG A CZ  
4841  N NH1 . ARG A 689  ? 0.3409 0.3311 0.2755 0.0244  0.0126  0.0336  687  ARG A NH1 
4842  N NH2 . ARG A 689  ? 0.3134 0.2940 0.2540 0.0224  0.0122  0.0341  687  ARG A NH2 
4843  N N   . ARG A 690  ? 0.2752 0.2541 0.2160 0.0305  0.0018  0.0268  688  ARG A N   
4844  C CA  . ARG A 690  ? 0.2825 0.2582 0.2256 0.0312  0.0000  0.0265  688  ARG A CA  
4845  C C   . ARG A 690  ? 0.3089 0.2875 0.2517 0.0331  -0.0018 0.0237  688  ARG A C   
4846  O O   . ARG A 690  ? 0.2959 0.2729 0.2398 0.0342  -0.0036 0.0242  688  ARG A O   
4847  C CB  . ARG A 690  ? 0.2697 0.2419 0.2170 0.0299  0.0007  0.0245  688  ARG A CB  
4848  C CG  . ARG A 690  ? 0.3000 0.2687 0.2484 0.0281  0.0022  0.0271  688  ARG A CG  
4849  C CD  . ARG A 690  ? 0.3666 0.3316 0.3151 0.0284  0.0010  0.0309  688  ARG A CD  
4850  N NE  . ARG A 690  ? 0.3714 0.3340 0.3226 0.0295  -0.0008 0.0293  688  ARG A NE  
4851  C CZ  . ARG A 690  ? 0.3878 0.3507 0.3383 0.0314  -0.0029 0.0299  688  ARG A CZ  
4852  N NH1 . ARG A 690  ? 0.3638 0.3289 0.3107 0.0324  -0.0036 0.0323  688  ARG A NH1 
4853  N NH2 . ARG A 690  ? 0.3184 0.2795 0.2717 0.0324  -0.0043 0.0280  688  ARG A NH2 
4854  N N   . THR A 691  ? 0.2651 0.2480 0.2067 0.0335  -0.0016 0.0207  689  THR A N   
4855  C CA  . THR A 691  ? 0.2601 0.2452 0.2026 0.0348  -0.0033 0.0174  689  THR A CA  
4856  C C   . THR A 691  ? 0.3244 0.3147 0.2635 0.0364  -0.0042 0.0165  689  THR A C   
4857  O O   . THR A 691  ? 0.3107 0.3027 0.2494 0.0380  -0.0062 0.0159  689  THR A O   
4858  C CB  . THR A 691  ? 0.3121 0.2970 0.2582 0.0336  -0.0028 0.0133  689  THR A CB  
4859  O OG1 . THR A 691  ? 0.2902 0.2764 0.2355 0.0326  -0.0011 0.0120  689  THR A OG1 
4860  C CG2 . THR A 691  ? 0.2830 0.2635 0.2327 0.0325  -0.0023 0.0137  689  THR A CG2 
4861  N N   . LEU A 692  ? 0.3106 0.3040 0.2474 0.0361  -0.0030 0.0158  690  LEU A N   
4862  C CA  . LEU A 692  ? 0.2844 0.2831 0.2190 0.0375  -0.0039 0.0130  690  LEU A CA  
4863  C C   . LEU A 692  ? 0.2924 0.2944 0.2225 0.0392  -0.0050 0.0159  690  LEU A C   
4864  O O   . LEU A 692  ? 0.3152 0.3171 0.2427 0.0389  -0.0040 0.0200  690  LEU A O   
4865  C CB  . LEU A 692  ? 0.3266 0.3276 0.2608 0.0367  -0.0024 0.0105  690  LEU A CB  
4866  C CG  . LEU A 692  ? 0.3228 0.3211 0.2613 0.0352  -0.0018 0.0071  690  LEU A CG  
4867  C CD1 . LEU A 692  ? 0.3289 0.3298 0.2670 0.0350  -0.0007 0.0042  690  LEU A CD1 
4868  C CD2 . LEU A 692  ? 0.2972 0.2954 0.2386 0.0356  -0.0036 0.0040  690  LEU A CD2 
4869  N N   . GLY A 693  ? 0.3345 0.3396 0.2639 0.0409  -0.0070 0.0140  691  GLY A N   
4870  C CA  . GLY A 693  ? 0.3310 0.3398 0.2561 0.0427  -0.0084 0.0163  691  GLY A CA  
4871  C C   . GLY A 693  ? 0.4098 0.4244 0.3332 0.0441  -0.0094 0.0122  691  GLY A C   
4872  O O   . GLY A 693  ? 0.3908 0.4062 0.3163 0.0435  -0.0089 0.0078  691  GLY A O   
4873  N N   . PRO A 694  ? 0.4376 0.4564 0.3573 0.0461  -0.0110 0.0134  692  PRO A N   
4874  C CA  . PRO A 694  ? 0.4487 0.4736 0.3665 0.0475  -0.0120 0.0093  692  PRO A CA  
4875  C C   . PRO A 694  ? 0.4142 0.4392 0.3357 0.0479  -0.0139 0.0045  692  PRO A C   
4876  O O   . PRO A 694  ? 0.4653 0.4941 0.3868 0.0484  -0.0144 0.0000  692  PRO A O   
4877  C CB  . PRO A 694  ? 0.5171 0.5463 0.4297 0.0494  -0.0133 0.0127  692  PRO A CB  
4878  C CG  . PRO A 694  ? 0.4714 0.4959 0.3846 0.0493  -0.0139 0.0177  692  PRO A CG  
4879  C CD  . PRO A 694  ? 0.4398 0.4581 0.3567 0.0470  -0.0120 0.0187  692  PRO A CD  
4880  N N   . GLY A 695  ? 0.3929 0.4140 0.3177 0.0477  -0.0149 0.0052  693  GLY A N   
4881  C CA  . GLY A 695  ? 0.4403 0.4619 0.3691 0.0478  -0.0164 0.0008  693  GLY A CA  
4882  C C   . GLY A 695  ? 0.4215 0.4407 0.3545 0.0456  -0.0151 -0.0027 693  GLY A C   
4883  O O   . GLY A 695  ? 0.3783 0.3982 0.3147 0.0454  -0.0163 -0.0064 693  GLY A O   
4884  N N   . HIS A 696  ? 0.3478 0.3642 0.2808 0.0441  -0.0128 -0.0014 694  HIS A N   
4885  C CA  . HIS A 696  ? 0.3478 0.3616 0.2848 0.0421  -0.0116 -0.0042 694  HIS A CA  
4886  C C   . HIS A 696  ? 0.3703 0.3873 0.3057 0.0422  -0.0111 -0.0072 694  HIS A C   
4887  O O   . HIS A 696  ? 0.3807 0.3971 0.3149 0.0415  -0.0092 -0.0061 694  HIS A O   
4888  C CB  . HIS A 696  ? 0.3395 0.3481 0.2780 0.0404  -0.0096 -0.0011 694  HIS A CB  
4889  C CG  . HIS A 696  ? 0.3435 0.3491 0.2830 0.0406  -0.0102 0.0020  694  HIS A CG  
4890  N ND1 . HIS A 696  ? 0.3174 0.3209 0.2546 0.0409  -0.0096 0.0067  694  HIS A ND1 
4891  C CD2 . HIS A 696  ? 0.3272 0.3318 0.2700 0.0408  -0.0115 0.0009  694  HIS A CD2 
4892  C CE1 . HIS A 696  ? 0.3223 0.3233 0.2614 0.0413  -0.0106 0.0082  694  HIS A CE1 
4893  N NE2 . HIS A 696  ? 0.3290 0.3307 0.2714 0.0413  -0.0118 0.0046  694  HIS A NE2 
4894  N N   . GLY A 697  ? 0.3332 0.3540 0.2688 0.0432  -0.0129 -0.0112 695  GLY A N   
4895  C CA  . GLY A 697  ? 0.3339 0.3586 0.2678 0.0439  -0.0130 -0.0145 695  GLY A CA  
4896  C C   . GLY A 697  ? 0.3140 0.3360 0.2514 0.0421  -0.0119 -0.0175 695  GLY A C   
4897  O O   . GLY A 697  ? 0.3113 0.3296 0.2533 0.0404  -0.0120 -0.0185 695  GLY A O   
4898  N N   . PRO A 698  ? 0.3469 0.3709 0.2824 0.0426  -0.0110 -0.0189 696  PRO A N   
4899  C CA  . PRO A 698  ? 0.3235 0.3448 0.2624 0.0411  -0.0102 -0.0217 696  PRO A CA  
4900  C C   . PRO A 698  ? 0.3171 0.3388 0.2598 0.0408  -0.0123 -0.0268 696  PRO A C   
4901  O O   . PRO A 698  ? 0.3201 0.3455 0.2620 0.0421  -0.0144 -0.0291 696  PRO A O   
4902  C CB  . PRO A 698  ? 0.3568 0.3816 0.2922 0.0423  -0.0090 -0.0222 696  PRO A CB  
4903  C CG  . PRO A 698  ? 0.4480 0.4788 0.3789 0.0446  -0.0102 -0.0225 696  PRO A CG  
4904  C CD  . PRO A 698  ? 0.4218 0.4513 0.3520 0.0446  -0.0108 -0.0185 696  PRO A CD  
4905  N N   . LEU A 699  ? 0.2909 0.3085 0.2378 0.0389  -0.0119 -0.0285 697  LEU A N   
4906  C CA  . LEU A 699  ? 0.2846 0.3020 0.2353 0.0383  -0.0139 -0.0333 697  LEU A CA  
4907  C C   . LEU A 699  ? 0.3113 0.3327 0.2603 0.0401  -0.0149 -0.0376 697  LEU A C   
4908  O O   . LEU A 699  ? 0.2916 0.3156 0.2417 0.0408  -0.0172 -0.0416 697  LEU A O   
4909  C CB  . LEU A 699  ? 0.2836 0.2956 0.2393 0.0357  -0.0132 -0.0335 697  LEU A CB  
4910  C CG  . LEU A 699  ? 0.2928 0.3011 0.2509 0.0338  -0.0123 -0.0300 697  LEU A CG  
4911  C CD1 . LEU A 699  ? 0.2801 0.2837 0.2423 0.0314  -0.0115 -0.0302 697  LEU A CD1 
4912  C CD2 . LEU A 699  ? 0.3207 0.3306 0.2808 0.0335  -0.0143 -0.0311 697  LEU A CD2 
4913  N N   . GLY A 700  ? 0.2999 0.3222 0.2463 0.0409  -0.0132 -0.0370 698  GLY A N   
4914  C CA  . GLY A 700  ? 0.2807 0.3063 0.2263 0.0425  -0.0140 -0.0416 698  GLY A CA  
4915  C C   . GLY A 700  ? 0.2787 0.3006 0.2269 0.0415  -0.0127 -0.0423 698  GLY A C   
4916  O O   . GLY A 700  ? 0.2924 0.3101 0.2417 0.0398  -0.0109 -0.0386 698  GLY A O   
4917  N N   . PRO A 701  ? 0.2908 0.3141 0.2401 0.0426  -0.0139 -0.0473 699  PRO A N   
4918  C CA  . PRO A 701  ? 0.2678 0.2879 0.2194 0.0420  -0.0128 -0.0481 699  PRO A CA  
4919  C C   . PRO A 701  ? 0.2622 0.2752 0.2188 0.0391  -0.0127 -0.0465 699  PRO A C   
4920  O O   . PRO A 701  ? 0.2712 0.2819 0.2315 0.0377  -0.0146 -0.0481 699  PRO A O   
4921  C CB  . PRO A 701  ? 0.3026 0.3251 0.2554 0.0438  -0.0150 -0.0546 699  PRO A CB  
4922  C CG  . PRO A 701  ? 0.3101 0.3392 0.2590 0.0460  -0.0163 -0.0563 699  PRO A CG  
4923  C CD  . PRO A 701  ? 0.2911 0.3189 0.2397 0.0446  -0.0164 -0.0525 699  PRO A CD  
4924  N N   . ILE A 702  ? 0.2736 0.2836 0.2305 0.0380  -0.0104 -0.0432 700  ILE A N   
4925  C CA  . ILE A 702  ? 0.2663 0.2700 0.2274 0.0352  -0.0100 -0.0412 700  ILE A CA  
4926  C C   . ILE A 702  ? 0.2860 0.2870 0.2498 0.0351  -0.0098 -0.0432 700  ILE A C   
4927  O O   . ILE A 702  ? 0.2567 0.2598 0.2182 0.0365  -0.0083 -0.0430 700  ILE A O   
4928  C CB  . ILE A 702  ? 0.2998 0.3019 0.2594 0.0340  -0.0077 -0.0355 700  ILE A CB  
4929  C CG1 . ILE A 702  ? 0.2677 0.2717 0.2257 0.0341  -0.0084 -0.0338 700  ILE A CG1 
4930  C CG2 . ILE A 702  ? 0.2539 0.2503 0.2176 0.0314  -0.0071 -0.0337 700  ILE A CG2 
4931  C CD1 . ILE A 702  ? 0.3337 0.3354 0.2912 0.0328  -0.0068 -0.0288 700  ILE A CD1 
4932  N N   . VAL A 703  ? 0.2709 0.2675 0.2397 0.0333  -0.0115 -0.0450 701  VAL A N   
4933  C CA  . VAL A 703  ? 0.2553 0.2483 0.2272 0.0330  -0.0116 -0.0466 701  VAL A CA  
4934  C C   . VAL A 703  ? 0.2733 0.2621 0.2465 0.0307  -0.0096 -0.0420 701  VAL A C   
4935  O O   . VAL A 703  ? 0.2852 0.2712 0.2605 0.0284  -0.0098 -0.0397 701  VAL A O   
4936  C CB  . VAL A 703  ? 0.2572 0.2474 0.2340 0.0322  -0.0147 -0.0508 701  VAL A CB  
4937  C CG1 . VAL A 703  ? 0.2584 0.2441 0.2387 0.0316  -0.0149 -0.0517 701  VAL A CG1 
4938  C CG2 . VAL A 703  ? 0.2630 0.2577 0.2386 0.0347  -0.0168 -0.0560 701  VAL A CG2 
4939  N N   . CYS A 704  ? 0.2507 0.2393 0.2226 0.0314  -0.0077 -0.0407 702  CYS A N   
4940  C CA  . CYS A 704  ? 0.2577 0.2426 0.2308 0.0294  -0.0059 -0.0366 702  CYS A CA  
4941  C C   . CYS A 704  ? 0.2655 0.2467 0.2424 0.0291  -0.0066 -0.0385 702  CYS A C   
4942  O O   . CYS A 704  ? 0.2495 0.2325 0.2256 0.0310  -0.0064 -0.0408 702  CYS A O   
4943  C CB  . CYS A 704  ? 0.2461 0.2336 0.2150 0.0302  -0.0031 -0.0331 702  CYS A CB  
4944  S SG  . CYS A 704  ? 0.2672 0.2588 0.2317 0.0308  -0.0024 -0.0304 702  CYS A SG  
4945  N N   . ILE A 705  ? 0.2531 0.2294 0.2340 0.0266  -0.0076 -0.0375 703  ILE A N   
4946  C CA  . ILE A 705  ? 0.2560 0.2280 0.2409 0.0259  -0.0085 -0.0387 703  ILE A CA  
4947  C C   . ILE A 705  ? 0.2460 0.2151 0.2313 0.0240  -0.0065 -0.0342 703  ILE A C   
4948  O O   . ILE A 705  ? 0.2766 0.2442 0.2624 0.0218  -0.0060 -0.0311 703  ILE A O   
4949  C CB  . ILE A 705  ? 0.2919 0.2606 0.2813 0.0243  -0.0115 -0.0410 703  ILE A CB  
4950  C CG1 . ILE A 705  ? 0.2713 0.2430 0.2604 0.0264  -0.0136 -0.0461 703  ILE A CG1 
4951  C CG2 . ILE A 705  ? 0.2999 0.2635 0.2935 0.0232  -0.0125 -0.0413 703  ILE A CG2 
4952  C CD1 . ILE A 705  ? 0.2898 0.2591 0.2829 0.0248  -0.0165 -0.0482 703  ILE A CD1 
4953  N N   . SER A 706  ? 0.2714 0.2402 0.2564 0.0249  -0.0053 -0.0339 704  SER A N   
4954  C CA  . SER A 706  ? 0.2576 0.2245 0.2424 0.0235  -0.0032 -0.0298 704  SER A CA  
4955  C C   . SER A 706  ? 0.2680 0.2304 0.2568 0.0226  -0.0042 -0.0300 704  SER A C   
4956  O O   . SER A 706  ? 0.2847 0.2459 0.2759 0.0236  -0.0062 -0.0336 704  SER A O   
4957  C CB  . SER A 706  ? 0.2600 0.2308 0.2410 0.0252  -0.0008 -0.0285 704  SER A CB  
4958  O OG  . SER A 706  ? 0.2757 0.2490 0.2564 0.0278  -0.0014 -0.0323 704  SER A OG  
4959  N N   . PRO A 707  ? 0.2829 0.2427 0.2726 0.0206  -0.0029 -0.0263 705  PRO A N   
4960  C CA  . PRO A 707  ? 0.2883 0.2437 0.2818 0.0194  -0.0040 -0.0260 705  PRO A CA  
4961  C C   . PRO A 707  ? 0.2729 0.2286 0.2660 0.0208  -0.0027 -0.0257 705  PRO A C   
4962  O O   . PRO A 707  ? 0.2651 0.2245 0.2549 0.0222  -0.0007 -0.0252 705  PRO A O   
4963  C CB  . PRO A 707  ? 0.2906 0.2438 0.2850 0.0164  -0.0033 -0.0219 705  PRO A CB  
4964  C CG  . PRO A 707  ? 0.2806 0.2372 0.2711 0.0168  -0.0008 -0.0196 705  PRO A CG  
4965  C CD  . PRO A 707  ? 0.2765 0.2371 0.2642 0.0191  -0.0010 -0.0222 705  PRO A CD  
4966  N N   . TRP A 708  ? 0.2781 0.2300 0.2746 0.0203  -0.0040 -0.0261 706  TRP A N   
4967  C CA  . TRP A 708  ? 0.2762 0.2284 0.2729 0.0218  -0.0031 -0.0261 706  TRP A CA  
4968  C C   . TRP A 708  ? 0.2846 0.2363 0.2803 0.0201  -0.0009 -0.0218 706  TRP A C   
4969  O O   . TRP A 708  ? 0.2983 0.2514 0.2935 0.0213  0.0004  -0.0214 706  TRP A O   
4970  C CB  . TRP A 708  ? 0.2717 0.2199 0.2726 0.0222  -0.0057 -0.0285 706  TRP A CB  
4971  C CG  . TRP A 708  ? 0.2926 0.2358 0.2968 0.0194  -0.0074 -0.0265 706  TRP A CG  
4972  C CD1 . TRP A 708  ? 0.3789 0.3199 0.3856 0.0184  -0.0099 -0.0282 706  TRP A CD1 
4973  C CD2 . TRP A 708  ? 0.2701 0.2106 0.2754 0.0170  -0.0067 -0.0224 706  TRP A CD2 
4974  N NE1 . TRP A 708  ? 0.3657 0.3027 0.3750 0.0154  -0.0107 -0.0251 706  TRP A NE1 
4975  C CE2 . TRP A 708  ? 0.3029 0.2397 0.3114 0.0146  -0.0088 -0.0216 706  TRP A CE2 
4976  C CE3 . TRP A 708  ? 0.2767 0.2177 0.2809 0.0167  -0.0046 -0.0194 706  TRP A CE3 
4977  C CZ2 . TRP A 708  ? 0.3125 0.2465 0.3226 0.0118  -0.0087 -0.0177 706  TRP A CZ2 
4978  C CZ3 . TRP A 708  ? 0.2680 0.2061 0.2738 0.0141  -0.0047 -0.0159 706  TRP A CZ3 
4979  C CH2 . TRP A 708  ? 0.3238 0.2586 0.3324 0.0118  -0.0066 -0.0150 706  TRP A CH2 
4980  N N   . ASN A 709  ? 0.2749 0.2251 0.2707 0.0176  -0.0005 -0.0186 707  ASN A N   
4981  C CA  . ASN A 709  ? 0.2973 0.2468 0.2927 0.0161  0.0013  -0.0148 707  ASN A CA  
4982  C C   . ASN A 709  ? 0.2994 0.2525 0.2911 0.0165  0.0038  -0.0130 707  ASN A C   
4983  O O   . ASN A 709  ? 0.3012 0.2542 0.2924 0.0159  0.0054  -0.0105 707  ASN A O   
4984  C CB  . ASN A 709  ? 0.2827 0.2293 0.2799 0.0132  0.0006  -0.0123 707  ASN A CB  
4985  C CG  . ASN A 709  ? 0.2994 0.2477 0.2950 0.0123  0.0009  -0.0118 707  ASN A CG  
4986  O OD1 . ASN A 709  ? 0.3539 0.3045 0.3480 0.0137  0.0006  -0.0141 707  ASN A OD1 
4987  N ND2 . ASN A 709  ? 0.3074 0.2550 0.3034 0.0100  0.0014  -0.0090 707  ASN A ND2 
4988  N N   . PHE A 710  ? 0.2845 0.2405 0.2736 0.0175  0.0042  -0.0140 708  PHE A N   
4989  C CA  . PHE A 710  ? 0.2607 0.2202 0.2462 0.0182  0.0064  -0.0125 708  PHE A CA  
4990  C C   . PHE A 710  ? 0.2849 0.2481 0.2685 0.0207  0.0062  -0.0155 708  PHE A C   
4991  O O   . PHE A 710  ? 0.2492 0.2147 0.2305 0.0211  0.0062  -0.0158 708  PHE A O   
4992  C CB  . PHE A 710  ? 0.2830 0.2426 0.2670 0.0167  0.0071  -0.0099 708  PHE A CB  
4993  C CG  . PHE A 710  ? 0.3085 0.2654 0.2941 0.0145  0.0076  -0.0071 708  PHE A CG  
4994  C CD1 . PHE A 710  ? 0.3727 0.3296 0.3578 0.0142  0.0092  -0.0049 708  PHE A CD1 
4995  C CD2 . PHE A 710  ? 0.3592 0.3139 0.3468 0.0128  0.0064  -0.0067 708  PHE A CD2 
4996  C CE1 . PHE A 710  ? 0.3869 0.3418 0.3734 0.0123  0.0095  -0.0025 708  PHE A CE1 
4997  C CE2 . PHE A 710  ? 0.4350 0.3879 0.4239 0.0108  0.0068  -0.0042 708  PHE A CE2 
4998  C CZ  . PHE A 710  ? 0.3997 0.3527 0.3879 0.0106  0.0084  -0.0022 708  PHE A CZ  
4999  N N   . PRO A 711  ? 0.2635 0.2278 0.2479 0.0224  0.0060  -0.0177 709  PRO A N   
5000  C CA  . PRO A 711  ? 0.2729 0.2407 0.2561 0.0249  0.0053  -0.0215 709  PRO A CA  
5001  C C   . PRO A 711  ? 0.2578 0.2309 0.2368 0.0261  0.0072  -0.0206 709  PRO A C   
5002  O O   . PRO A 711  ? 0.2578 0.2345 0.2352 0.0280  0.0067  -0.0235 709  PRO A O   
5003  C CB  . PRO A 711  ? 0.2691 0.2364 0.2548 0.0263  0.0046  -0.0239 709  PRO A CB  
5004  C CG  . PRO A 711  ? 0.2322 0.1981 0.2185 0.0250  0.0062  -0.0205 709  PRO A CG  
5005  C CD  . PRO A 711  ? 0.2540 0.2166 0.2405 0.0223  0.0063  -0.0171 709  PRO A CD  
5006  N N   . LEU A 712  ? 0.2952 0.2689 0.2725 0.0249  0.0093  -0.0168 710  LEU A N   
5007  C CA  . LEU A 712  ? 0.2474 0.2257 0.2209 0.0255  0.0110  -0.0152 710  LEU A CA  
5008  C C   . LEU A 712  ? 0.2520 0.2289 0.2239 0.0240  0.0113  -0.0123 710  LEU A C   
5009  O O   . LEU A 712  ? 0.2462 0.2260 0.2154 0.0248  0.0113  -0.0124 710  LEU A O   
5010  C CB  . LEU A 712  ? 0.2456 0.2261 0.2182 0.0255  0.0132  -0.0130 710  LEU A CB  
5011  C CG  . LEU A 712  ? 0.2743 0.2596 0.2431 0.0259  0.0149  -0.0108 710  LEU A CG  
5012  C CD1 . LEU A 712  ? 0.2351 0.2257 0.2016 0.0284  0.0146  -0.0140 710  LEU A CD1 
5013  C CD2 . LEU A 712  ? 0.2810 0.2679 0.2496 0.0252  0.0170  -0.0081 710  LEU A CD2 
5014  N N   . ALA A 713  ? 0.2348 0.2077 0.2085 0.0219  0.0114  -0.0099 711  ALA A N   
5015  C CA  . ALA A 713  ? 0.2413 0.2135 0.2135 0.0207  0.0118  -0.0071 711  ALA A CA  
5016  C C   . ALA A 713  ? 0.2509 0.2227 0.2231 0.0208  0.0101  -0.0087 711  ALA A C   
5017  O O   . ALA A 713  ? 0.2511 0.2250 0.2208 0.0214  0.0102  -0.0079 711  ALA A O   
5018  C CB  . ALA A 713  ? 0.2574 0.2260 0.2315 0.0187  0.0124  -0.0044 711  ALA A CB  
5019  N N   . ILE A 714  ? 0.2804 0.2495 0.2556 0.0202  0.0085  -0.0107 712  ILE A N   
5020  C CA  . ILE A 714  ? 0.2583 0.2273 0.2338 0.0201  0.0068  -0.0122 712  ILE A CA  
5021  C C   . ILE A 714  ? 0.2609 0.2335 0.2347 0.0223  0.0060  -0.0153 712  ILE A C   
5022  O O   . ILE A 714  ? 0.2796 0.2540 0.2517 0.0228  0.0053  -0.0158 712  ILE A O   
5023  C CB  . ILE A 714  ? 0.2788 0.2441 0.2583 0.0185  0.0052  -0.0132 712  ILE A CB  
5024  C CG1 . ILE A 714  ? 0.3035 0.2663 0.2840 0.0164  0.0062  -0.0099 712  ILE A CG1 
5025  C CG2 . ILE A 714  ? 0.2468 0.2126 0.2270 0.0185  0.0033  -0.0154 712  ILE A CG2 
5026  C CD1 . ILE A 714  ? 0.3555 0.3154 0.3395 0.0144  0.0047  -0.0100 712  ILE A CD1 
5027  N N   . PHE A 715  ? 0.2430 0.2170 0.2170 0.0238  0.0060  -0.0176 713  PHE A N   
5028  C CA  . PHE A 715  ? 0.2638 0.2421 0.2357 0.0261  0.0054  -0.0207 713  PHE A CA  
5029  C C   . PHE A 715  ? 0.2908 0.2731 0.2583 0.0269  0.0068  -0.0185 713  PHE A C   
5030  O O   . PHE A 715  ? 0.2623 0.2470 0.2279 0.0278  0.0059  -0.0198 713  PHE A O   
5031  C CB  . PHE A 715  ? 0.2599 0.2396 0.2325 0.0276  0.0057  -0.0228 713  PHE A CB  
5032  C CG  . PHE A 715  ? 0.2466 0.2316 0.2167 0.0303  0.0055  -0.0260 713  PHE A CG  
5033  C CD1 . PHE A 715  ? 0.2717 0.2569 0.2433 0.0316  0.0032  -0.0306 713  PHE A CD1 
5034  C CD2 . PHE A 715  ? 0.2828 0.2729 0.2494 0.0314  0.0075  -0.0246 713  PHE A CD2 
5035  C CE1 . PHE A 715  ? 0.2974 0.2881 0.2666 0.0343  0.0029  -0.0341 713  PHE A CE1 
5036  C CE2 . PHE A 715  ? 0.2672 0.2630 0.2314 0.0339  0.0074  -0.0275 713  PHE A CE2 
5037  C CZ  . PHE A 715  ? 0.3043 0.3005 0.2697 0.0355  0.0050  -0.0325 713  PHE A CZ  
5038  N N   . THR A 716  ? 0.2350 0.2180 0.2011 0.0263  0.0089  -0.0151 714  THR A N   
5039  C CA  . THR A 716  ? 0.2360 0.2225 0.1981 0.0268  0.0102  -0.0125 714  THR A CA  
5040  C C   . THR A 716  ? 0.2444 0.2293 0.2058 0.0259  0.0095  -0.0107 714  THR A C   
5041  O O   . THR A 716  ? 0.2599 0.2479 0.2185 0.0270  0.0092  -0.0105 714  THR A O   
5042  C CB  . THR A 716  ? 0.2681 0.2549 0.2295 0.0261  0.0124  -0.0091 714  THR A CB  
5043  O OG1 . THR A 716  ? 0.2591 0.2482 0.2210 0.0272  0.0130  -0.0110 714  THR A OG1 
5044  C CG2 . THR A 716  ? 0.2498 0.2399 0.2073 0.0263  0.0135  -0.0060 714  THR A CG2 
5045  N N   . GLY A 717  ? 0.2487 0.2292 0.2128 0.0241  0.0092  -0.0094 715  GLY A N   
5046  C CA  . GLY A 717  ? 0.2459 0.2253 0.2096 0.0233  0.0087  -0.0076 715  GLY A CA  
5047  C C   . GLY A 717  ? 0.2680 0.2490 0.2312 0.0243  0.0068  -0.0103 715  GLY A C   
5048  O O   . GLY A 717  ? 0.2532 0.2363 0.2141 0.0250  0.0066  -0.0092 715  GLY A O   
5049  N N   . GLN A 718  ? 0.2470 0.2272 0.2128 0.0243  0.0054  -0.0137 716  GLN A N   
5050  C CA  . GLN A 718  ? 0.2688 0.2508 0.2346 0.0252  0.0034  -0.0166 716  GLN A CA  
5051  C C   . GLN A 718  ? 0.2545 0.2414 0.2163 0.0275  0.0034  -0.0177 716  GLN A C   
5052  O O   . GLN A 718  ? 0.2461 0.2353 0.2060 0.0282  0.0026  -0.0177 716  GLN A O   
5053  C CB  . GLN A 718  ? 0.2530 0.2329 0.2224 0.0247  0.0017  -0.0201 716  GLN A CB  
5054  C CG  . GLN A 718  ? 0.2355 0.2109 0.2087 0.0223  0.0014  -0.0188 716  GLN A CG  
5055  C CD  . GLN A 718  ? 0.2937 0.2669 0.2707 0.0216  -0.0006 -0.0220 716  GLN A CD  
5056  O OE1 . GLN A 718  ? 0.3017 0.2727 0.2815 0.0197  -0.0016 -0.0216 716  GLN A OE1 
5057  N NE2 . GLN A 718  ? 0.2742 0.2482 0.2515 0.0231  -0.0013 -0.0250 716  GLN A NE2 
5058  N N   . ILE A 719  ? 0.2405 0.2296 0.2012 0.0287  0.0043  -0.0188 717  ILE A N   
5059  C CA  . ILE A 719  ? 0.2440 0.2387 0.2010 0.0309  0.0043  -0.0201 717  ILE A CA  
5060  C C   . ILE A 719  ? 0.2527 0.2496 0.2060 0.0310  0.0056  -0.0160 717  ILE A C   
5061  O O   . ILE A 719  ? 0.2669 0.2675 0.2172 0.0324  0.0049  -0.0163 717  ILE A O   
5062  C CB  . ILE A 719  ? 0.2602 0.2572 0.2171 0.0322  0.0052  -0.0221 717  ILE A CB  
5063  C CG1 . ILE A 719  ? 0.2457 0.2406 0.2062 0.0325  0.0032  -0.0267 717  ILE A CG1 
5064  C CG2 . ILE A 719  ? 0.3101 0.3137 0.2625 0.0343  0.0058  -0.0225 717  ILE A CG2 
5065  C CD1 . ILE A 719  ? 0.3433 0.3382 0.3053 0.0331  0.0039  -0.0281 717  ILE A CD1 
5066  N N   . ALA A 720  ? 0.2466 0.2412 0.1999 0.0296  0.0074  -0.0120 718  ALA A N   
5067  C CA  . ALA A 720  ? 0.2666 0.2628 0.2166 0.0296  0.0085  -0.0079 718  ALA A CA  
5068  C C   . ALA A 720  ? 0.2516 0.2469 0.2011 0.0296  0.0071  -0.0070 718  ALA A C   
5069  O O   . ALA A 720  ? 0.2459 0.2443 0.1921 0.0306  0.0069  -0.0055 718  ALA A O   
5070  C CB  . ALA A 720  ? 0.2433 0.2365 0.1942 0.0279  0.0103  -0.0042 718  ALA A CB  
5071  N N   . ALA A 721  ? 0.2458 0.2371 0.1987 0.0283  0.0061  -0.0078 719  ALA A N   
5072  C CA  . ALA A 721  ? 0.2408 0.2317 0.1937 0.0283  0.0048  -0.0073 719  ALA A CA  
5073  C C   . ALA A 721  ? 0.2438 0.2387 0.1949 0.0301  0.0031  -0.0103 719  ALA A C   
5074  O O   . ALA A 721  ? 0.2457 0.2429 0.1943 0.0311  0.0025  -0.0090 719  ALA A O   
5075  C CB  . ALA A 721  ? 0.2376 0.2244 0.1946 0.0266  0.0041  -0.0080 719  ALA A CB  
5076  N N   . ALA A 722  ? 0.2444 0.2402 0.1970 0.0306  0.0021  -0.0144 720  ALA A N   
5077  C CA  . ALA A 722  ? 0.2473 0.2470 0.1986 0.0323  0.0003  -0.0178 720  ALA A CA  
5078  C C   . ALA A 722  ? 0.2536 0.2586 0.2000 0.0342  0.0009  -0.0167 720  ALA A C   
5079  O O   . ALA A 722  ? 0.2530 0.2611 0.1970 0.0354  -0.0002 -0.0166 720  ALA A O   
5080  C CB  . ALA A 722  ? 0.2477 0.2472 0.2018 0.0325  -0.0009 -0.0225 720  ALA A CB  
5081  N N   . LEU A 723  ? 0.2540 0.2604 0.1989 0.0345  0.0027  -0.0158 721  LEU A N   
5082  C CA  . LEU A 723  ? 0.2547 0.2667 0.1949 0.0361  0.0036  -0.0143 721  LEU A CA  
5083  C C   . LEU A 723  ? 0.2555 0.2675 0.1930 0.0359  0.0039  -0.0095 721  LEU A C   
5084  O O   . LEU A 723  ? 0.2662 0.2826 0.2002 0.0373  0.0033  -0.0089 721  LEU A O   
5085  C CB  . LEU A 723  ? 0.2594 0.2727 0.1990 0.0360  0.0057  -0.0135 721  LEU A CB  
5086  C CG  . LEU A 723  ? 0.2786 0.2936 0.2198 0.0371  0.0054  -0.0183 721  LEU A CG  
5087  C CD1 . LEU A 723  ? 0.2546 0.2706 0.1956 0.0367  0.0077  -0.0166 721  LEU A CD1 
5088  C CD2 . LEU A 723  ? 0.2592 0.2804 0.1976 0.0395  0.0042  -0.0220 721  LEU A CD2 
5089  N N   . VAL A 724  ? 0.2662 0.2734 0.2054 0.0341  0.0049  -0.0060 722  VAL A N   
5090  C CA  . VAL A 724  ? 0.2728 0.2799 0.2096 0.0339  0.0052  -0.0012 722  VAL A CA  
5091  C C   . VAL A 724  ? 0.2623 0.2691 0.1991 0.0346  0.0032  -0.0016 722  VAL A C   
5092  O O   . VAL A 724  ? 0.2982 0.3066 0.2321 0.0353  0.0028  0.0014  722  VAL A O   
5093  C CB  . VAL A 724  ? 0.2514 0.2536 0.1902 0.0319  0.0067  0.0024  722  VAL A CB  
5094  C CG1 . VAL A 724  ? 0.2643 0.2613 0.2069 0.0307  0.0058  0.0019  722  VAL A CG1 
5095  C CG2 . VAL A 724  ? 0.2593 0.2623 0.1950 0.0319  0.0075  0.0075  722  VAL A CG2 
5096  N N   . ALA A 725  ? 0.2528 0.2579 0.1928 0.0343  0.0017  -0.0052 723  ALA A N   
5097  C CA  . ALA A 725  ? 0.2623 0.2681 0.2025 0.0351  -0.0004 -0.0065 723  ALA A CA  
5098  C C   . ALA A 725  ? 0.2783 0.2900 0.2152 0.0373  -0.0016 -0.0088 723  ALA A C   
5099  O O   . ALA A 725  ? 0.2928 0.3059 0.2297 0.0381  -0.0035 -0.0101 723  ALA A O   
5100  C CB  . ALA A 725  ? 0.2685 0.2713 0.2135 0.0339  -0.0014 -0.0096 723  ALA A CB  
5101  N N   . GLY A 726  ? 0.2896 0.3051 0.2239 0.0382  -0.0007 -0.0097 724  GLY A N   
5102  C CA  . GLY A 726  ? 0.3009 0.3226 0.2317 0.0404  -0.0018 -0.0119 724  GLY A CA  
5103  C C   . GLY A 726  ? 0.2739 0.2976 0.2066 0.0412  -0.0031 -0.0179 724  GLY A C   
5104  O O   . GLY A 726  ? 0.3242 0.3528 0.2545 0.0431  -0.0046 -0.0205 724  GLY A O   
5105  N N   . ASN A 727  ? 0.2637 0.2835 0.2005 0.0399  -0.0029 -0.0202 725  ASN A N   
5106  C CA  . ASN A 727  ? 0.2617 0.2822 0.2009 0.0405  -0.0045 -0.0259 725  ASN A CA  
5107  C C   . ASN A 727  ? 0.2701 0.2926 0.2089 0.0412  -0.0033 -0.0279 725  ASN A C   
5108  O O   . ASN A 727  ? 0.2841 0.3042 0.2234 0.0401  -0.0013 -0.0254 725  ASN A O   
5109  C CB  . ASN A 727  ? 0.2824 0.2973 0.2271 0.0384  -0.0054 -0.0273 725  ASN A CB  
5110  C CG  . ASN A 727  ? 0.2732 0.2861 0.2189 0.0375  -0.0062 -0.0251 725  ASN A CG  
5111  O OD1 . ASN A 727  ? 0.2806 0.2960 0.2260 0.0384  -0.0082 -0.0270 725  ASN A OD1 
5112  N ND2 . ASN A 727  ? 0.2635 0.2722 0.2106 0.0358  -0.0048 -0.0213 725  ASN A ND2 
5113  N N   . PRO A 728  ? 0.2656 0.2924 0.2036 0.0431  -0.0046 -0.0327 726  PRO A N   
5114  C CA  . PRO A 728  ? 0.2664 0.2944 0.2050 0.0439  -0.0038 -0.0356 726  PRO A CA  
5115  C C   . PRO A 728  ? 0.2636 0.2854 0.2079 0.0423  -0.0046 -0.0380 726  PRO A C   
5116  O O   . PRO A 728  ? 0.2813 0.2997 0.2289 0.0412  -0.0064 -0.0394 726  PRO A O   
5117  C CB  . PRO A 728  ? 0.2708 0.3055 0.2071 0.0466  -0.0054 -0.0404 726  PRO A CB  
5118  C CG  . PRO A 728  ? 0.3023 0.3363 0.2395 0.0465  -0.0079 -0.0418 726  PRO A CG  
5119  C CD  . PRO A 728  ? 0.2702 0.3008 0.2071 0.0447  -0.0070 -0.0362 726  PRO A CD  
5120  N N   . VAL A 729  ? 0.2722 0.2928 0.2178 0.0422  -0.0032 -0.0383 727  VAL A N   
5121  C CA  . VAL A 729  ? 0.2598 0.2740 0.2105 0.0404  -0.0035 -0.0391 727  VAL A CA  
5122  C C   . VAL A 729  ? 0.2649 0.2799 0.2178 0.0418  -0.0046 -0.0443 727  VAL A C   
5123  O O   . VAL A 729  ? 0.2784 0.2982 0.2288 0.0438  -0.0036 -0.0457 727  VAL A O   
5124  C CB  . VAL A 729  ? 0.2564 0.2673 0.2074 0.0386  -0.0010 -0.0341 727  VAL A CB  
5125  C CG1 . VAL A 729  ? 0.2540 0.2592 0.2099 0.0371  -0.0012 -0.0352 727  VAL A CG1 
5126  C CG2 . VAL A 729  ? 0.2543 0.2630 0.2045 0.0370  -0.0005 -0.0295 727  VAL A CG2 
5127  N N   . LEU A 730  ? 0.2613 0.2715 0.2189 0.0408  -0.0067 -0.0472 728  LEU A N   
5128  C CA  . LEU A 730  ? 0.2627 0.2713 0.2237 0.0416  -0.0079 -0.0516 728  LEU A CA  
5129  C C   . LEU A 730  ? 0.2592 0.2614 0.2237 0.0393  -0.0069 -0.0488 728  LEU A C   
5130  O O   . LEU A 730  ? 0.2705 0.2677 0.2380 0.0369  -0.0077 -0.0471 728  LEU A O   
5131  C CB  . LEU A 730  ? 0.2652 0.2725 0.2294 0.0420  -0.0113 -0.0568 728  LEU A CB  
5132  C CG  . LEU A 730  ? 0.2689 0.2821 0.2302 0.0441  -0.0128 -0.0602 728  LEU A CG  
5133  C CD1 . LEU A 730  ? 0.2716 0.2921 0.2283 0.0471  -0.0115 -0.0615 728  LEU A CD1 
5134  C CD2 . LEU A 730  ? 0.2863 0.3004 0.2456 0.0430  -0.0128 -0.0569 728  LEU A CD2 
5135  N N   . ALA A 731  ? 0.2623 0.2653 0.2263 0.0400  -0.0051 -0.0480 729  ALA A N   
5136  C CA  . ALA A 731  ? 0.2554 0.2532 0.2220 0.0380  -0.0038 -0.0448 729  ALA A CA  
5137  C C   . ALA A 731  ? 0.2703 0.2644 0.2415 0.0383  -0.0057 -0.0487 729  ALA A C   
5138  O O   . ALA A 731  ? 0.2842 0.2812 0.2553 0.0406  -0.0058 -0.0520 729  ALA A O   
5139  C CB  . ALA A 731  ? 0.2682 0.2689 0.2318 0.0383  -0.0008 -0.0413 729  ALA A CB  
5140  N N   . LYS A 732  ? 0.2624 0.2504 0.2379 0.0360  -0.0072 -0.0482 730  LYS A N   
5141  C CA  . LYS A 732  ? 0.2566 0.2401 0.2369 0.0359  -0.0092 -0.0512 730  LYS A CA  
5142  C C   . LYS A 732  ? 0.2830 0.2618 0.2653 0.0338  -0.0079 -0.0473 730  LYS A C   
5143  O O   . LYS A 732  ? 0.2641 0.2388 0.2484 0.0311  -0.0080 -0.0442 730  LYS A O   
5144  C CB  . LYS A 732  ? 0.2910 0.2711 0.2749 0.0346  -0.0123 -0.0536 730  LYS A CB  
5145  C CG  . LYS A 732  ? 0.3525 0.3310 0.3400 0.0362  -0.0153 -0.0593 730  LYS A CG  
5146  C CD  . LYS A 732  ? 0.3609 0.3347 0.3519 0.0359  -0.0155 -0.0591 730  LYS A CD  
5147  C CE  . LYS A 732  ? 0.4159 0.3833 0.4104 0.0323  -0.0158 -0.0552 730  LYS A CE  
5148  N NZ  . LYS A 732  ? 0.3375 0.3001 0.3359 0.0321  -0.0167 -0.0555 730  LYS A NZ  
5149  N N   . PRO A 733  ? 0.2814 0.2612 0.2635 0.0351  -0.0065 -0.0472 731  PRO A N   
5150  C CA  . PRO A 733  ? 0.2577 0.2333 0.2417 0.0332  -0.0053 -0.0436 731  PRO A CA  
5151  C C   . PRO A 733  ? 0.2728 0.2425 0.2621 0.0323  -0.0078 -0.0453 731  PRO A C   
5152  O O   . PRO A 733  ? 0.2712 0.2401 0.2628 0.0336  -0.0104 -0.0499 731  PRO A O   
5153  C CB  . PRO A 733  ? 0.2712 0.2509 0.2531 0.0352  -0.0032 -0.0436 731  PRO A CB  
5154  C CG  . PRO A 733  ? 0.3040 0.2881 0.2852 0.0384  -0.0046 -0.0490 731  PRO A CG  
5155  C CD  . PRO A 733  ? 0.2663 0.2516 0.2463 0.0383  -0.0061 -0.0507 731  PRO A CD  
5156  N N   . ALA A 734  ? 0.2488 0.2141 0.2401 0.0300  -0.0071 -0.0416 732  ALA A N   
5157  C CA  . ALA A 734  ? 0.2681 0.2277 0.2643 0.0289  -0.0094 -0.0424 732  ALA A CA  
5158  C C   . ALA A 734  ? 0.2670 0.2270 0.2649 0.0318  -0.0106 -0.0467 732  ALA A C   
5159  O O   . ALA A 734  ? 0.2897 0.2538 0.2852 0.0338  -0.0088 -0.0470 732  ALA A O   
5160  C CB  . ALA A 734  ? 0.2750 0.2309 0.2722 0.0264  -0.0080 -0.0376 732  ALA A CB  
5161  N N   . GLU A 735  ? 0.2817 0.2374 0.2839 0.0319  -0.0139 -0.0498 733  GLU A N   
5162  C CA  . GLU A 735  ? 0.3129 0.2683 0.3174 0.0347  -0.0156 -0.0542 733  GLU A CA  
5163  C C   . GLU A 735  ? 0.2974 0.2523 0.3023 0.0352  -0.0140 -0.0521 733  GLU A C   
5164  O O   . GLU A 735  ? 0.2849 0.2426 0.2899 0.0382  -0.0140 -0.0554 733  GLU A O   
5165  C CB  . GLU A 735  ? 0.3648 0.3141 0.3747 0.0340  -0.0195 -0.0568 733  GLU A CB  
5166  C CG  . GLU A 735  ? 0.4663 0.4148 0.4791 0.0372  -0.0220 -0.0623 733  GLU A CG  
5167  C CD  . GLU A 735  ? 0.5202 0.4621 0.5386 0.0361  -0.0262 -0.0645 733  GLU A CD  
5168  O OE1 . GLU A 735  ? 0.5584 0.4966 0.5782 0.0327  -0.0269 -0.0615 733  GLU A OE1 
5169  O OE2 . GLU A 735  ? 0.6551 0.5955 0.6765 0.0388  -0.0288 -0.0693 733  GLU A OE2 
5170  N N   . GLU A 736  ? 0.3025 0.2545 0.3077 0.0324  -0.0126 -0.0469 734  GLU A N   
5171  C CA  . GLU A 736  ? 0.3173 0.2683 0.3232 0.0326  -0.0113 -0.0449 734  GLU A CA  
5172  C C   . GLU A 736  ? 0.3113 0.2686 0.3131 0.0338  -0.0079 -0.0435 734  GLU A C   
5173  O O   . GLU A 736  ? 0.3035 0.2617 0.3059 0.0351  -0.0070 -0.0434 734  GLU A O   
5174  C CB  . GLU A 736  ? 0.3007 0.2466 0.3084 0.0291  -0.0112 -0.0399 734  GLU A CB  
5175  C CG  . GLU A 736  ? 0.3436 0.2831 0.3561 0.0274  -0.0146 -0.0405 734  GLU A CG  
5176  C CD  . GLU A 736  ? 0.3925 0.3312 0.4049 0.0252  -0.0155 -0.0400 734  GLU A CD  
5177  O OE1 . GLU A 736  ? 0.3335 0.2766 0.3423 0.0257  -0.0141 -0.0405 734  GLU A OE1 
5178  O OE2 . GLU A 736  ? 0.4765 0.4101 0.4925 0.0229  -0.0178 -0.0390 734  GLU A OE2 
5179  N N   . THR A 737  ? 0.2603 0.2219 0.2579 0.0335  -0.0060 -0.0423 735  THR A N   
5180  C CA  . THR A 737  ? 0.2769 0.2435 0.2706 0.0339  -0.0026 -0.0397 735  THR A CA  
5181  C C   . THR A 737  ? 0.2761 0.2494 0.2659 0.0358  -0.0016 -0.0417 735  THR A C   
5182  O O   . THR A 737  ? 0.2873 0.2632 0.2735 0.0347  0.0004  -0.0387 735  THR A O   
5183  C CB  . THR A 737  ? 0.2850 0.2495 0.2775 0.0307  -0.0009 -0.0342 735  THR A CB  
5184  O OG1 . THR A 737  ? 0.2799 0.2433 0.2717 0.0292  -0.0017 -0.0336 735  THR A OG1 
5185  C CG2 . THR A 737  ? 0.2787 0.2378 0.2747 0.0289  -0.0016 -0.0320 735  THR A CG2 
5186  N N   . PRO A 738  ? 0.2649 0.2411 0.2550 0.0388  -0.0030 -0.0469 736  PRO A N   
5187  C CA  . PRO A 738  ? 0.2669 0.2500 0.2530 0.0407  -0.0021 -0.0489 736  PRO A CA  
5188  C C   . PRO A 738  ? 0.2938 0.2835 0.2763 0.0418  0.0010  -0.0472 736  PRO A C   
5189  O O   . PRO A 738  ? 0.2778 0.2730 0.2563 0.0424  0.0024  -0.0468 736  PRO A O   
5190  C CB  . PRO A 738  ? 0.2859 0.2698 0.2742 0.0437  -0.0049 -0.0554 736  PRO A CB  
5191  C CG  . PRO A 738  ? 0.2586 0.2390 0.2510 0.0443  -0.0058 -0.0564 736  PRO A CG  
5192  C CD  . PRO A 738  ? 0.2675 0.2413 0.2618 0.0407  -0.0055 -0.0512 736  PRO A CD  
5193  N N   . LEU A 739  ? 0.2512 0.2408 0.2353 0.0420  0.0022  -0.0461 737  LEU A N   
5194  C CA  . LEU A 739  ? 0.2509 0.2476 0.2321 0.0433  0.0049  -0.0452 737  LEU A CA  
5195  C C   . LEU A 739  ? 0.2673 0.2656 0.2449 0.0409  0.0076  -0.0396 737  LEU A C   
5196  O O   . LEU A 739  ? 0.2734 0.2781 0.2471 0.0417  0.0093  -0.0390 737  LEU A O   
5197  C CB  . LEU A 739  ? 0.2563 0.2525 0.2405 0.0440  0.0053  -0.0455 737  LEU A CB  
5198  C CG  . LEU A 739  ? 0.2604 0.2549 0.2486 0.0466  0.0024  -0.0511 737  LEU A CG  
5199  C CD1 . LEU A 739  ? 0.2531 0.2464 0.2443 0.0470  0.0027  -0.0507 737  LEU A CD1 
5200  C CD2 . LEU A 739  ? 0.2631 0.2646 0.2495 0.0501  0.0020  -0.0565 737  LEU A CD2 
5201  N N   . ILE A 740  ? 0.2568 0.2494 0.2356 0.0380  0.0079  -0.0355 738  ILE A N   
5202  C CA  . ILE A 740  ? 0.2529 0.2464 0.2286 0.0359  0.0101  -0.0305 738  ILE A CA  
5203  C C   . ILE A 740  ? 0.2594 0.2544 0.2321 0.0358  0.0097  -0.0305 738  ILE A C   
5204  O O   . ILE A 740  ? 0.2491 0.2477 0.2182 0.0353  0.0115  -0.0275 738  ILE A O   
5205  C CB  . ILE A 740  ? 0.2919 0.2792 0.2698 0.0330  0.0103  -0.0266 738  ILE A CB  
5206  C CG1 . ILE A 740  ? 0.2806 0.2688 0.2556 0.0310  0.0126  -0.0216 738  ILE A CG1 
5207  C CG2 . ILE A 740  ? 0.2750 0.2562 0.2554 0.0319  0.0079  -0.0275 738  ILE A CG2 
5208  C CD1 . ILE A 740  ? 0.2724 0.2659 0.2458 0.0315  0.0151  -0.0198 738  ILE A CD1 
5209  N N   . ALA A 741  ? 0.2636 0.2560 0.2377 0.0364  0.0072  -0.0337 739  ALA A N   
5210  C CA  . ALA A 741  ? 0.2622 0.2567 0.2336 0.0367  0.0065  -0.0344 739  ALA A CA  
5211  C C   . ALA A 741  ? 0.2768 0.2793 0.2445 0.0392  0.0075  -0.0363 739  ALA A C   
5212  O O   . ALA A 741  ? 0.2669 0.2729 0.2308 0.0390  0.0087  -0.0341 739  ALA A O   
5213  C CB  . ALA A 741  ? 0.2669 0.2574 0.2412 0.0368  0.0035  -0.0380 739  ALA A CB  
5214  N N   . ALA A 742  ? 0.2650 0.2706 0.2339 0.0417  0.0070  -0.0406 740  ALA A N   
5215  C CA  . ALA A 742  ? 0.2544 0.2686 0.2199 0.0442  0.0080  -0.0427 740  ALA A CA  
5216  C C   . ALA A 742  ? 0.2590 0.2777 0.2211 0.0433  0.0112  -0.0379 740  ALA A C   
5217  O O   . ALA A 742  ? 0.2947 0.3197 0.2527 0.0441  0.0124  -0.0371 740  ALA A O   
5218  C CB  . ALA A 742  ? 0.2872 0.3038 0.2550 0.0471  0.0070  -0.0482 740  ALA A CB  
5219  N N   . GLU A 743  ? 0.2522 0.2681 0.2163 0.0416  0.0126  -0.0348 741  GLU A N   
5220  C CA  . GLU A 743  ? 0.2684 0.2878 0.2298 0.0403  0.0155  -0.0299 741  GLU A CA  
5221  C C   . GLU A 743  ? 0.2845 0.3021 0.2431 0.0382  0.0160  -0.0254 741  GLU A C   
5222  O O   . GLU A 743  ? 0.2590 0.2815 0.2141 0.0379  0.0178  -0.0224 741  GLU A O   
5223  C CB  . GLU A 743  ? 0.2660 0.2821 0.2305 0.0390  0.0165  -0.0279 741  GLU A CB  
5224  C CG  . GLU A 743  ? 0.3104 0.3294 0.2731 0.0372  0.0193  -0.0228 741  GLU A CG  
5225  C CD  . GLU A 743  ? 0.3334 0.3617 0.2933 0.0388  0.0212  -0.0232 741  GLU A CD  
5226  O OE1 . GLU A 743  ? 0.3459 0.3791 0.3054 0.0416  0.0205  -0.0279 741  GLU A OE1 
5227  O OE2 . GLU A 743  ? 0.3901 0.4211 0.3483 0.0372  0.0234  -0.0186 741  GLU A OE2 
5228  N N   . GLY A 744  ? 0.2777 0.2885 0.2381 0.0367  0.0145  -0.0248 742  GLY A N   
5229  C CA  . GLY A 744  ? 0.2528 0.2622 0.2108 0.0351  0.0147  -0.0211 742  GLY A CA  
5230  C C   . GLY A 744  ? 0.2483 0.2630 0.2025 0.0368  0.0142  -0.0225 742  GLY A C   
5231  O O   . GLY A 744  ? 0.2668 0.2842 0.2176 0.0362  0.0154  -0.0189 742  GLY A O   
5232  N N   . VAL A 745  ? 0.2655 0.2819 0.2203 0.0389  0.0124  -0.0278 743  VAL A N   
5233  C CA  . VAL A 745  ? 0.2674 0.2896 0.2185 0.0408  0.0118  -0.0296 743  VAL A CA  
5234  C C   . VAL A 745  ? 0.2679 0.2984 0.2154 0.0420  0.0140  -0.0285 743  VAL A C   
5235  O O   . VAL A 745  ? 0.2736 0.3086 0.2170 0.0422  0.0147  -0.0263 743  VAL A O   
5236  C CB  . VAL A 745  ? 0.2821 0.3044 0.2351 0.0429  0.0092  -0.0360 743  VAL A CB  
5237  C CG1 . VAL A 745  ? 0.2821 0.3121 0.2311 0.0454  0.0088  -0.0386 743  VAL A CG1 
5238  C CG2 . VAL A 745  ? 0.2692 0.2843 0.2250 0.0414  0.0069  -0.0363 743  VAL A CG2 
5239  N N   . ARG A 746  ? 0.2832 0.3162 0.2322 0.0428  0.0152  -0.0298 744  ARG A N   
5240  C CA  . ARG A 746  ? 0.2882 0.3295 0.2340 0.0437  0.0175  -0.0284 744  ARG A CA  
5241  C C   . ARG A 746  ? 0.2799 0.3213 0.2232 0.0412  0.0195  -0.0216 744  ARG A C   
5242  O O   . ARG A 746  ? 0.3131 0.3609 0.2521 0.0416  0.0208  -0.0195 744  ARG A O   
5243  C CB  . ARG A 746  ? 0.3097 0.3528 0.2583 0.0446  0.0184  -0.0304 744  ARG A CB  
5244  C CG  . ARG A 746  ? 0.3595 0.4126 0.3052 0.0460  0.0207  -0.0303 744  ARG A CG  
5245  C CD  . ARG A 746  ? 0.3585 0.4129 0.3071 0.0460  0.0221  -0.0305 744  ARG A CD  
5246  N NE  . ARG A 746  ? 0.3709 0.4199 0.3211 0.0428  0.0234  -0.0250 744  ARG A NE  
5247  C CZ  . ARG A 746  ? 0.4009 0.4524 0.3486 0.0408  0.0256  -0.0194 744  ARG A CZ  
5248  N NH1 . ARG A 746  ? 0.4342 0.4935 0.3775 0.0414  0.0269  -0.0180 744  ARG A NH1 
5249  N NH2 . ARG A 746  ? 0.3738 0.4197 0.3234 0.0380  0.0264  -0.0151 744  ARG A NH2 
5250  N N   . ILE A 747  ? 0.2890 0.3232 0.2347 0.0386  0.0198  -0.0181 745  ILE A N   
5251  C CA  . ILE A 747  ? 0.2608 0.2940 0.2047 0.0362  0.0214  -0.0118 745  ILE A CA  
5252  C C   . ILE A 747  ? 0.2697 0.3028 0.2104 0.0360  0.0205  -0.0098 745  ILE A C   
5253  O O   . ILE A 747  ? 0.2562 0.2931 0.1933 0.0355  0.0218  -0.0059 745  ILE A O   
5254  C CB  . ILE A 747  ? 0.3005 0.3260 0.2480 0.0338  0.0216  -0.0094 745  ILE A CB  
5255  C CG1 . ILE A 747  ? 0.3089 0.3362 0.2588 0.0338  0.0230  -0.0098 745  ILE A CG1 
5256  C CG2 . ILE A 747  ? 0.2821 0.3047 0.2282 0.0314  0.0223  -0.0036 745  ILE A CG2 
5257  C CD1 . ILE A 747  ? 0.2915 0.3115 0.2454 0.0319  0.0228  -0.0086 745  ILE A CD1 
5258  N N   . LEU A 748  ? 0.2568 0.2853 0.1986 0.0364  0.0183  -0.0124 746  LEU A N   
5259  C CA  . LEU A 748  ? 0.2600 0.2886 0.1991 0.0364  0.0172  -0.0109 746  LEU A CA  
5260  C C   . LEU A 748  ? 0.3115 0.3486 0.2462 0.0386  0.0174  -0.0122 746  LEU A C   
5261  O O   . LEU A 748  ? 0.2868 0.3262 0.2179 0.0383  0.0177  -0.0087 746  LEU A O   
5262  C CB  . LEU A 748  ? 0.2615 0.2846 0.2030 0.0365  0.0148  -0.0140 746  LEU A CB  
5263  C CG  . LEU A 748  ? 0.3206 0.3358 0.2653 0.0341  0.0145  -0.0114 746  LEU A CG  
5264  C CD1 . LEU A 748  ? 0.3487 0.3592 0.2967 0.0342  0.0122  -0.0153 746  LEU A CD1 
5265  C CD2 . LEU A 748  ? 0.3179 0.3319 0.2603 0.0329  0.0147  -0.0069 746  LEU A CD2 
5266  N N   . ARG A 749  ? 0.2855 0.3273 0.2204 0.0409  0.0171  -0.0172 747  ARG A N   
5267  C CA  . ARG A 749  ? 0.2968 0.3476 0.2273 0.0430  0.0174  -0.0185 747  ARG A CA  
5268  C C   . ARG A 749  ? 0.3333 0.3899 0.2608 0.0422  0.0201  -0.0137 747  ARG A C   
5269  O O   . ARG A 749  ? 0.3068 0.3687 0.2300 0.0425  0.0206  -0.0110 747  ARG A O   
5270  C CB  . ARG A 749  ? 0.3010 0.3558 0.2327 0.0458  0.0164  -0.0254 747  ARG A CB  
5271  C CG  . ARG A 749  ? 0.3437 0.3953 0.2768 0.0470  0.0134  -0.0301 747  ARG A CG  
5272  C CD  . ARG A 749  ? 0.3706 0.4254 0.3053 0.0498  0.0121  -0.0371 747  ARG A CD  
5273  N NE  . ARG A 749  ? 0.3302 0.3821 0.2666 0.0508  0.0091  -0.0418 747  ARG A NE  
5274  C CZ  . ARG A 749  ? 0.3536 0.4086 0.2911 0.0535  0.0074  -0.0483 747  ARG A CZ  
5275  N NH1 . ARG A 749  ? 0.3662 0.4273 0.3033 0.0556  0.0084  -0.0511 747  ARG A NH1 
5276  N NH2 . ARG A 749  ? 0.3270 0.3789 0.2662 0.0541  0.0045  -0.0523 747  ARG A NH2 
5277  N N   . GLU A 750  ? 0.2900 0.3457 0.2199 0.0410  0.0219  -0.0122 748  GLU A N   
5278  C CA  . GLU A 750  ? 0.3052 0.3662 0.2328 0.0397  0.0244  -0.0072 748  GLU A CA  
5279  C C   . GLU A 750  ? 0.3209 0.3787 0.2464 0.0374  0.0247  -0.0008 748  GLU A C   
5280  O O   . GLU A 750  ? 0.3063 0.3697 0.2280 0.0370  0.0260  0.0032  748  GLU A O   
5281  C CB  . GLU A 750  ? 0.2809 0.3404 0.2119 0.0386  0.0260  -0.0066 748  GLU A CB  
5282  C CG  . GLU A 750  ? 0.3246 0.3899 0.2537 0.0371  0.0287  -0.0016 748  GLU A CG  
5283  C CD  . GLU A 750  ? 0.3405 0.4041 0.2733 0.0357  0.0302  -0.0007 748  GLU A CD  
5284  O OE1 . GLU A 750  ? 0.4586 0.5185 0.3952 0.0365  0.0293  -0.0049 748  GLU A OE1 
5285  O OE2 . GLU A 750  ? 0.3941 0.4600 0.3262 0.0336  0.0321  0.0043  748  GLU A OE2 
5286  N N   . ALA A 751  ? 0.2950 0.3439 0.2228 0.0361  0.0233  0.0001  749  ALA A N   
5287  C CA  . ALA A 751  ? 0.3002 0.3452 0.2266 0.0342  0.0231  0.0056  749  ALA A CA  
5288  C C   . ALA A 751  ? 0.3012 0.3495 0.2236 0.0355  0.0218  0.0060  749  ALA A C   
5289  O O   . ALA A 751  ? 0.2883 0.3341 0.2091 0.0342  0.0215  0.0107  749  ALA A O   
5290  C CB  . ALA A 751  ? 0.2886 0.3240 0.2190 0.0327  0.0218  0.0057  749  ALA A CB  
5291  N N   . GLY A 752  ? 0.2780 0.3315 0.1987 0.0380  0.0209  0.0012  750  GLY A N   
5292  C CA  . GLY A 752  ? 0.3057 0.3633 0.2223 0.0394  0.0196  0.0014  750  GLY A CA  
5293  C C   . GLY A 752  ? 0.3285 0.3832 0.2462 0.0410  0.0170  -0.0035 750  GLY A C   
5294  O O   . GLY A 752  ? 0.3217 0.3802 0.2360 0.0424  0.0158  -0.0039 750  GLY A O   
5295  N N   . ILE A 753  ? 0.2690 0.3173 0.1912 0.0407  0.0159  -0.0070 751  ILE A N   
5296  C CA  . ILE A 753  ? 0.3155 0.3620 0.2390 0.0421  0.0133  -0.0119 751  ILE A CA  
5297  C C   . ILE A 753  ? 0.2886 0.3426 0.2103 0.0449  0.0128  -0.0173 751  ILE A C   
5298  O O   . ILE A 753  ? 0.3141 0.3702 0.2374 0.0457  0.0136  -0.0203 751  ILE A O   
5299  C CB  . ILE A 753  ? 0.3112 0.3496 0.2401 0.0410  0.0123  -0.0144 751  ILE A CB  
5300  C CG1 . ILE A 753  ? 0.2951 0.3265 0.2259 0.0383  0.0129  -0.0095 751  ILE A CG1 
5301  C CG2 . ILE A 753  ? 0.2959 0.3328 0.2261 0.0422  0.0096  -0.0191 751  ILE A CG2 
5302  C CD1 . ILE A 753  ? 0.2618 0.2911 0.1911 0.0378  0.0117  -0.0066 751  ILE A CD1 
5303  N N   . PRO A 754  ? 0.3129 0.3712 0.2315 0.0466  0.0113  -0.0189 752  PRO A N   
5304  C CA  . PRO A 754  ? 0.3295 0.3953 0.2463 0.0495  0.0106  -0.0245 752  PRO A CA  
5305  C C   . PRO A 754  ? 0.3361 0.3985 0.2576 0.0504  0.0089  -0.0311 752  PRO A C   
5306  O O   . PRO A 754  ? 0.2780 0.3324 0.2034 0.0491  0.0075  -0.0317 752  PRO A O   
5307  C CB  . PRO A 754  ? 0.3645 0.4339 0.2776 0.0507  0.0089  -0.0246 752  PRO A CB  
5308  C CG  . PRO A 754  ? 0.3810 0.4469 0.2925 0.0486  0.0095  -0.0177 752  PRO A CG  
5309  C CD  . PRO A 754  ? 0.3267 0.3837 0.2428 0.0461  0.0102  -0.0156 752  PRO A CD  
5310  N N   . ALA A 755  ? 0.3364 0.4050 0.2574 0.0528  0.0090  -0.0360 753  ALA A N   
5311  C CA  . ALA A 755  ? 0.3254 0.3910 0.2508 0.0541  0.0071  -0.0425 753  ALA A CA  
5312  C C   . ALA A 755  ? 0.3274 0.3891 0.2546 0.0543  0.0040  -0.0459 753  ALA A C   
5313  O O   . ALA A 755  ? 0.3443 0.3993 0.2763 0.0537  0.0023  -0.0488 753  ALA A O   
5314  C CB  . ALA A 755  ? 0.2953 0.3695 0.2193 0.0571  0.0074  -0.0476 753  ALA A CB  
5315  N N   . SER A 756  ? 0.3161 0.3821 0.2394 0.0552  0.0031  -0.0454 754  SER A N   
5316  C CA  . SER A 756  ? 0.3186 0.3817 0.2434 0.0555  0.0001  -0.0487 754  SER A CA  
5317  C C   . SER A 756  ? 0.3186 0.3728 0.2463 0.0526  -0.0004 -0.0449 754  SER A C   
5318  O O   . SER A 756  ? 0.3531 0.4030 0.2841 0.0523  -0.0028 -0.0479 754  SER A O   
5319  C CB  . SER A 756  ? 0.3340 0.4048 0.2536 0.0574  -0.0007 -0.0491 754  SER A CB  
5320  O OG  . SER A 756  ? 0.3873 0.4591 0.3031 0.0561  0.0010  -0.0422 754  SER A OG  
5321  N N   . ALA A 757  ? 0.2880 0.3397 0.2150 0.0506  0.0018  -0.0386 755  ALA A N   
5322  C CA  . ALA A 757  ? 0.2768 0.3205 0.2065 0.0480  0.0015  -0.0352 755  ALA A CA  
5323  C C   . ALA A 757  ? 0.2730 0.3096 0.2080 0.0463  0.0017  -0.0358 755  ALA A C   
5324  O O   . ALA A 757  ? 0.2656 0.2958 0.2037 0.0443  0.0010  -0.0344 755  ALA A O   
5325  C CB  . ALA A 757  ? 0.3068 0.3507 0.2334 0.0466  0.0033  -0.0282 755  ALA A CB  
5326  N N   . LEU A 758  ? 0.2760 0.3140 0.2122 0.0470  0.0028  -0.0378 756  LEU A N   
5327  C CA  . LEU A 758  ? 0.2947 0.3263 0.2357 0.0454  0.0030  -0.0380 756  LEU A CA  
5328  C C   . LEU A 758  ? 0.2944 0.3279 0.2374 0.0474  0.0022  -0.0438 756  LEU A C   
5329  O O   . LEU A 758  ? 0.2914 0.3300 0.2327 0.0488  0.0038  -0.0443 756  LEU A O   
5330  C CB  . LEU A 758  ? 0.2867 0.3167 0.2271 0.0437  0.0058  -0.0325 756  LEU A CB  
5331  C CG  . LEU A 758  ? 0.2782 0.3022 0.2234 0.0422  0.0061  -0.0327 756  LEU A CG  
5332  C CD1 . LEU A 758  ? 0.2703 0.2871 0.2195 0.0407  0.0040  -0.0338 756  LEU A CD1 
5333  C CD2 . LEU A 758  ? 0.3295 0.3520 0.2739 0.0403  0.0086  -0.0270 756  LEU A CD2 
5334  N N   . GLN A 759  ? 0.2675 0.2969 0.2144 0.0476  -0.0004 -0.0482 757  GLN A N   
5335  C CA  . GLN A 759  ? 0.2898 0.3201 0.2394 0.0495  -0.0018 -0.0541 757  GLN A CA  
5336  C C   . GLN A 759  ? 0.2795 0.3018 0.2344 0.0477  -0.0024 -0.0540 757  GLN A C   
5337  O O   . GLN A 759  ? 0.2937 0.3098 0.2511 0.0453  -0.0031 -0.0518 757  GLN A O   
5338  C CB  . GLN A 759  ? 0.3176 0.3497 0.2676 0.0513  -0.0049 -0.0597 757  GLN A CB  
5339  C CG  . GLN A 759  ? 0.2852 0.3260 0.2297 0.0535  -0.0046 -0.0604 757  GLN A CG  
5340  C CD  . GLN A 759  ? 0.2799 0.3222 0.2249 0.0550  -0.0077 -0.0659 757  GLN A CD  
5341  O OE1 . GLN A 759  ? 0.3252 0.3710 0.2709 0.0575  -0.0092 -0.0718 757  GLN A OE1 
5342  N NE2 . GLN A 759  ? 0.2796 0.3194 0.2246 0.0535  -0.0089 -0.0641 757  GLN A NE2 
5343  N N   . LEU A 760  ? 0.2736 0.2966 0.2303 0.0490  -0.0019 -0.0563 758  LEU A N   
5344  C CA  . LEU A 760  ? 0.3100 0.3260 0.2717 0.0475  -0.0024 -0.0562 758  LEU A CA  
5345  C C   . LEU A 760  ? 0.2681 0.2819 0.2339 0.0491  -0.0056 -0.0626 758  LEU A C   
5346  O O   . LEU A 760  ? 0.2891 0.3081 0.2541 0.0521  -0.0063 -0.0674 758  LEU A O   
5347  C CB  . LEU A 760  ? 0.2650 0.2827 0.2264 0.0478  0.0001  -0.0541 758  LEU A CB  
5348  C CG  . LEU A 760  ? 0.2616 0.2721 0.2280 0.0464  -0.0004 -0.0538 758  LEU A CG  
5349  C CD1 . LEU A 760  ? 0.2790 0.2834 0.2464 0.0429  0.0005  -0.0481 758  LEU A CD1 
5350  C CD2 . LEU A 760  ? 0.2845 0.2982 0.2513 0.0479  0.0011  -0.0545 758  LEU A CD2 
5351  N N   . LEU A 761  ? 0.2762 0.2824 0.2465 0.0470  -0.0076 -0.0626 759  LEU A N   
5352  C CA  . LEU A 761  ? 0.2861 0.2889 0.2608 0.0479  -0.0110 -0.0681 759  LEU A CA  
5353  C C   . LEU A 761  ? 0.2776 0.2729 0.2573 0.0462  -0.0117 -0.0670 759  LEU A C   
5354  O O   . LEU A 761  ? 0.2799 0.2690 0.2626 0.0434  -0.0129 -0.0650 759  LEU A O   
5355  C CB  . LEU A 761  ? 0.2710 0.2720 0.2465 0.0469  -0.0134 -0.0695 759  LEU A CB  
5356  C CG  . LEU A 761  ? 0.3078 0.3158 0.2789 0.0486  -0.0136 -0.0713 759  LEU A CG  
5357  C CD1 . LEU A 761  ? 0.3099 0.3252 0.2783 0.0524  -0.0133 -0.0756 759  LEU A CD1 
5358  C CD2 . LEU A 761  ? 0.3427 0.3529 0.3095 0.0471  -0.0111 -0.0654 759  LEU A CD2 
5359  N N   . PRO A 762  ? 0.3095 0.3055 0.2903 0.0477  -0.0109 -0.0681 760  PRO A N   
5360  C CA  . PRO A 762  ? 0.2862 0.2752 0.2719 0.0463  -0.0119 -0.0673 760  PRO A CA  
5361  C C   . PRO A 762  ? 0.3244 0.3081 0.3150 0.0465  -0.0159 -0.0718 760  PRO A C   
5362  O O   . PRO A 762  ? 0.3297 0.3162 0.3205 0.0488  -0.0180 -0.0772 760  PRO A O   
5363  C CB  . PRO A 762  ? 0.3008 0.2933 0.2860 0.0487  -0.0103 -0.0685 760  PRO A CB  
5364  C CG  . PRO A 762  ? 0.2685 0.2700 0.2480 0.0505  -0.0078 -0.0681 760  PRO A CG  
5365  C CD  . PRO A 762  ? 0.2822 0.2860 0.2598 0.0508  -0.0092 -0.0702 760  PRO A CD  
5366  N N   . GLY A 763  ? 0.3100 0.2862 0.3050 0.0441  -0.0170 -0.0697 761  GLY A N   
5367  C CA  . GLY A 763  ? 0.3465 0.3170 0.3468 0.0439  -0.0210 -0.0734 761  GLY A CA  
5368  C C   . GLY A 763  ? 0.3805 0.3437 0.3841 0.0398  -0.0218 -0.0692 761  GLY A C   
5369  O O   . GLY A 763  ? 0.3692 0.3317 0.3711 0.0374  -0.0193 -0.0636 761  GLY A O   
5370  N N   . ASP A 764  ? 0.4086 0.3666 0.4170 0.0391  -0.0254 -0.0720 762  ASP A N   
5371  C CA  . ASP A 764  ? 0.4325 0.3836 0.4448 0.0353  -0.0266 -0.0683 762  ASP A CA  
5372  C C   . ASP A 764  ? 0.4979 0.4496 0.5095 0.0329  -0.0270 -0.0671 762  ASP A C   
5373  O O   . ASP A 764  ? 0.4218 0.3793 0.4291 0.0340  -0.0256 -0.0677 762  ASP A O   
5374  C CB  . ASP A 764  ? 0.4844 0.4290 0.5028 0.0355  -0.0304 -0.0714 762  ASP A CB  
5375  C CG  . ASP A 764  ? 0.5015 0.4469 0.5219 0.0377  -0.0339 -0.0782 762  ASP A CG  
5376  O OD1 . ASP A 764  ? 0.5086 0.4580 0.5267 0.0380  -0.0339 -0.0799 762  ASP A OD1 
5377  O OD2 . ASP A 764  ? 0.5508 0.4926 0.5753 0.0394  -0.0367 -0.0821 762  ASP A OD2 
5378  N N   . GLY A 765  ? 0.4704 0.4164 0.4862 0.0296  -0.0290 -0.0653 763  GLY A N   
5379  C CA  . GLY A 765  ? 0.4495 0.3962 0.4651 0.0272  -0.0293 -0.0639 763  GLY A CA  
5380  C C   . GLY A 765  ? 0.3989 0.3484 0.4148 0.0289  -0.0317 -0.0693 763  GLY A C   
5381  O O   . GLY A 765  ? 0.4708 0.4234 0.4847 0.0279  -0.0313 -0.0687 763  GLY A O   
5382  N N   . ARG A 766  ? 0.3836 0.3321 0.4019 0.0315  -0.0344 -0.0749 764  ARG A N   
5383  C CA  . ARG A 766  ? 0.4506 0.4024 0.4686 0.0335  -0.0367 -0.0807 764  ARG A CA  
5384  C C   . ARG A 766  ? 0.3987 0.3589 0.4103 0.0358  -0.0340 -0.0810 764  ARG A C   
5385  O O   . ARG A 766  ? 0.3496 0.3132 0.3596 0.0360  -0.0347 -0.0828 764  ARG A O   
5386  C CB  . ARG A 766  ? 0.4220 0.3719 0.4435 0.0365  -0.0399 -0.0870 764  ARG A CB  
5387  N N   . VAL A 767  ? 0.3899 0.3533 0.3974 0.0375  -0.0308 -0.0790 765  VAL A N   
5388  C CA  . VAL A 767  ? 0.3640 0.3351 0.3652 0.0394  -0.0280 -0.0784 765  VAL A CA  
5389  C C   . VAL A 767  ? 0.3172 0.2890 0.3163 0.0366  -0.0262 -0.0733 765  VAL A C   
5390  O O   . VAL A 767  ? 0.3743 0.3509 0.3702 0.0373  -0.0260 -0.0741 765  VAL A O   
5391  C CB  . VAL A 767  ? 0.3678 0.3422 0.3658 0.0415  -0.0251 -0.0771 765  VAL A CB  
5392  C CG1 . VAL A 767  ? 0.3181 0.3003 0.3096 0.0430  -0.0222 -0.0758 765  VAL A CG1 
5393  C CG2 . VAL A 767  ? 0.3585 0.3330 0.3588 0.0448  -0.0270 -0.0829 765  VAL A CG2 
5394  N N   . GLY A 768  ? 0.3198 0.2870 0.3205 0.0334  -0.0250 -0.0681 766  GLY A N   
5395  C CA  . GLY A 768  ? 0.3277 0.2955 0.3269 0.0308  -0.0235 -0.0636 766  GLY A CA  
5396  C C   . GLY A 768  ? 0.3342 0.3019 0.3356 0.0295  -0.0261 -0.0657 766  GLY A C   
5397  O O   . GLY A 768  ? 0.3046 0.2762 0.3030 0.0294  -0.0253 -0.0646 766  GLY A O   
5398  N N   . ALA A 769  ? 0.3177 0.2808 0.3244 0.0286  -0.0294 -0.0687 767  ALA A N   
5399  C CA  . ALA A 769  ? 0.3279 0.2906 0.3375 0.0270  -0.0322 -0.0708 767  ALA A CA  
5400  C C   . ALA A 769  ? 0.3649 0.3336 0.3715 0.0300  -0.0332 -0.0756 767  ALA A C   
5401  O O   . ALA A 769  ? 0.3424 0.3139 0.3481 0.0293  -0.0336 -0.0756 767  ALA A O   
5402  C CB  . ALA A 769  ? 0.3255 0.2818 0.3417 0.0255  -0.0357 -0.0731 767  ALA A CB  
5403  N N   . ALA A 770  ? 0.3437 0.3149 0.3486 0.0336  -0.0335 -0.0798 768  ALA A N   
5404  C CA  . ALA A 770  ? 0.3642 0.3419 0.3658 0.0367  -0.0343 -0.0843 768  ALA A CA  
5405  C C   . ALA A 770  ? 0.3537 0.3373 0.3492 0.0371  -0.0312 -0.0807 768  ALA A C   
5406  O O   . ALA A 770  ? 0.3195 0.3073 0.3131 0.0378  -0.0321 -0.0824 768  ALA A O   
5407  C CB  . ALA A 770  ? 0.3504 0.3304 0.3510 0.0405  -0.0347 -0.0890 768  ALA A CB  
5408  N N   . LEU A 771  ? 0.3156 0.2994 0.3082 0.0366  -0.0278 -0.0756 769  LEU A N   
5409  C CA  . LEU A 771  ? 0.3551 0.3438 0.3422 0.0370  -0.0250 -0.0719 769  LEU A CA  
5410  C C   . LEU A 771  ? 0.2964 0.2842 0.2845 0.0342  -0.0254 -0.0691 769  LEU A C   
5411  O O   . LEU A 771  ? 0.3501 0.3426 0.3351 0.0351  -0.0254 -0.0693 769  LEU A O   
5412  C CB  . LEU A 771  ? 0.3003 0.2886 0.2849 0.0367  -0.0215 -0.0670 769  LEU A CB  
5413  C CG  . LEU A 771  ? 0.3319 0.3229 0.3145 0.0397  -0.0206 -0.0694 769  LEU A CG  
5414  C CD1 . LEU A 771  ? 0.3104 0.2998 0.2918 0.0388  -0.0175 -0.0645 769  LEU A CD1 
5415  C CD2 . LEU A 771  ? 0.2915 0.2905 0.2689 0.0428  -0.0201 -0.0717 769  LEU A CD2 
5416  N N   . VAL A 772  ? 0.2898 0.2719 0.2823 0.0310  -0.0258 -0.0665 770  VAL A N   
5417  C CA  . VAL A 772  ? 0.2787 0.2601 0.2725 0.0282  -0.0260 -0.0637 770  VAL A CA  
5418  C C   . VAL A 772  ? 0.3085 0.2923 0.3038 0.0286  -0.0290 -0.0680 770  VAL A C   
5419  O O   . VAL A 772  ? 0.3368 0.3239 0.3305 0.0282  -0.0288 -0.0668 770  VAL A O   
5420  C CB  . VAL A 772  ? 0.2857 0.2609 0.2843 0.0247  -0.0261 -0.0606 770  VAL A CB  
5421  C CG1 . VAL A 772  ? 0.3521 0.3269 0.3532 0.0218  -0.0269 -0.0589 770  VAL A CG1 
5422  C CG2 . VAL A 772  ? 0.2922 0.2660 0.2885 0.0243  -0.0228 -0.0558 770  VAL A CG2 
5423  N N   . ALA A 773  ? 0.3343 0.3166 0.3329 0.0294  -0.0319 -0.0732 771  ALA A N   
5424  C CA  . ALA A 773  ? 0.3081 0.2919 0.3090 0.0295  -0.0352 -0.0777 771  ALA A CA  
5425  C C   . ALA A 773  ? 0.3798 0.3707 0.3759 0.0331  -0.0354 -0.0811 771  ALA A C   
5426  O O   . ALA A 773  ? 0.4013 0.3945 0.3986 0.0333  -0.0380 -0.0848 771  ALA A O   
5427  C CB  . ALA A 773  ? 0.3794 0.3585 0.3861 0.0290  -0.0386 -0.0821 771  ALA A CB  
5428  N N   . ALA A 774  ? 0.3765 0.3712 0.3672 0.0357  -0.0329 -0.0801 772  ALA A N   
5429  C CA  . ALA A 774  ? 0.3571 0.3589 0.3430 0.0391  -0.0332 -0.0834 772  ALA A CA  
5430  C C   . ALA A 774  ? 0.3450 0.3508 0.3285 0.0386  -0.0331 -0.0814 772  ALA A C   
5431  O O   . ALA A 774  ? 0.3515 0.3562 0.3340 0.0367  -0.0310 -0.0761 772  ALA A O   
5432  C CB  . ALA A 774  ? 0.3198 0.3252 0.3005 0.0417  -0.0303 -0.0820 772  ALA A CB  
5433  N N   . ALA A 775  ? 0.3838 0.3942 0.3664 0.0405  -0.0355 -0.0861 773  ALA A N   
5434  C CA  . ALA A 775  ? 0.4013 0.4154 0.3825 0.0400  -0.0360 -0.0850 773  ALA A CA  
5435  C C   . ALA A 775  ? 0.3789 0.3966 0.3541 0.0408  -0.0328 -0.0796 773  ALA A C   
5436  O O   . ALA A 775  ? 0.4136 0.4314 0.3886 0.0393  -0.0323 -0.0762 773  ALA A O   
5437  C CB  . ALA A 775  ? 0.4234 0.4427 0.4039 0.0425  -0.0390 -0.0912 773  ALA A CB  
5438  N N   . GLU A 776  ? 0.3169 0.3373 0.2875 0.0432  -0.0307 -0.0787 774  GLU A N   
5439  C CA  . GLU A 776  ? 0.3162 0.3402 0.2811 0.0440  -0.0279 -0.0737 774  GLU A CA  
5440  C C   . GLU A 776  ? 0.3230 0.3422 0.2882 0.0418  -0.0250 -0.0678 774  GLU A C   
5441  O O   . GLU A 776  ? 0.3183 0.3397 0.2793 0.0423  -0.0226 -0.0633 774  GLU A O   
5442  C CB  . GLU A 776  ? 0.3803 0.4108 0.3396 0.0474  -0.0271 -0.0754 774  GLU A CB  
5443  C CG  . GLU A 776  ? 0.4348 0.4715 0.3918 0.0496  -0.0295 -0.0794 774  GLU A CG  
5444  C CD  . GLU A 776  ? 0.5347 0.5774 0.4884 0.0530  -0.0299 -0.0839 774  GLU A CD  
5445  O OE1 . GLU A 776  ? 0.5048 0.5455 0.4608 0.0535  -0.0301 -0.0870 774  GLU A OE1 
5446  O OE2 . GLU A 776  ? 0.6429 0.6926 0.5917 0.0552  -0.0302 -0.0845 774  GLU A OE2 
5447  N N   . THR A 777  ? 0.2831 0.2961 0.2534 0.0394  -0.0252 -0.0676 775  THR A N   
5448  C CA  . THR A 777  ? 0.3227 0.3314 0.2936 0.0373  -0.0226 -0.0621 775  THR A CA  
5449  C C   . THR A 777  ? 0.2913 0.2998 0.2622 0.0356  -0.0222 -0.0583 775  THR A C   
5450  O O   . THR A 777  ? 0.3024 0.3099 0.2770 0.0340  -0.0242 -0.0597 775  THR A O   
5451  C CB  . THR A 777  ? 0.3076 0.3099 0.2840 0.0352  -0.0233 -0.0630 775  THR A CB  
5452  O OG1 . THR A 777  ? 0.3239 0.3265 0.2998 0.0372  -0.0232 -0.0660 775  THR A OG1 
5453  C CG2 . THR A 777  ? 0.2947 0.2927 0.2722 0.0326  -0.0209 -0.0574 775  THR A CG2 
5454  N N   . ALA A 778  ? 0.2630 0.2727 0.2300 0.0359  -0.0197 -0.0537 776  ALA A N   
5455  C CA  . ALA A 778  ? 0.2610 0.2714 0.2274 0.0350  -0.0195 -0.0504 776  ALA A CA  
5456  C C   . ALA A 778  ? 0.2662 0.2718 0.2350 0.0324  -0.0177 -0.0460 776  ALA A C   
5457  O O   . ALA A 778  ? 0.3100 0.3157 0.2793 0.0314  -0.0176 -0.0436 776  ALA A O   
5458  C CB  . ALA A 778  ? 0.2790 0.2944 0.2394 0.0374  -0.0184 -0.0482 776  ALA A CB  
5459  N N   . GLY A 779  ? 0.2732 0.2750 0.2435 0.0314  -0.0164 -0.0451 777  GLY A N   
5460  C CA  . GLY A 779  ? 0.2536 0.2510 0.2260 0.0290  -0.0147 -0.0412 777  GLY A CA  
5461  C C   . GLY A 779  ? 0.2577 0.2512 0.2320 0.0282  -0.0140 -0.0415 777  GLY A C   
5462  O O   . GLY A 779  ? 0.2651 0.2600 0.2378 0.0300  -0.0139 -0.0437 777  GLY A O   
5463  N N   . VAL A 780  ? 0.2584 0.2476 0.2364 0.0256  -0.0135 -0.0394 778  VAL A N   
5464  C CA  . VAL A 780  ? 0.2586 0.2438 0.2387 0.0247  -0.0129 -0.0394 778  VAL A CA  
5465  C C   . VAL A 780  ? 0.2538 0.2365 0.2339 0.0231  -0.0106 -0.0346 778  VAL A C   
5466  O O   . VAL A 780  ? 0.2742 0.2562 0.2558 0.0213  -0.0104 -0.0325 778  VAL A O   
5467  C CB  . VAL A 780  ? 0.2923 0.2742 0.2777 0.0230  -0.0153 -0.0422 778  VAL A CB  
5468  C CG1 . VAL A 780  ? 0.2656 0.2432 0.2532 0.0222  -0.0147 -0.0416 778  VAL A CG1 
5469  C CG2 . VAL A 780  ? 0.2527 0.2371 0.2384 0.0247  -0.0178 -0.0473 778  VAL A CG2 
5470  N N   . MET A 781  ? 0.2846 0.2662 0.2630 0.0238  -0.0088 -0.0332 779  MET A N   
5471  C CA  . MET A 781  ? 0.2411 0.2199 0.2200 0.0222  -0.0068 -0.0293 779  MET A CA  
5472  C C   . MET A 781  ? 0.2494 0.2243 0.2315 0.0212  -0.0071 -0.0302 779  MET A C   
5473  O O   . MET A 781  ? 0.2526 0.2279 0.2341 0.0228  -0.0073 -0.0324 779  MET A O   
5474  C CB  . MET A 781  ? 0.2834 0.2642 0.2578 0.0237  -0.0045 -0.0266 779  MET A CB  
5475  C CG  . MET A 781  ? 0.2884 0.2728 0.2595 0.0249  -0.0045 -0.0258 779  MET A CG  
5476  S SD  . MET A 781  ? 0.2826 0.2697 0.2485 0.0267  -0.0022 -0.0227 779  MET A SD  
5477  C CE  . MET A 781  ? 0.2744 0.2577 0.2415 0.0245  -0.0003 -0.0181 779  MET A CE  
5478  N N   . PHE A 782  ? 0.2580 0.2295 0.2437 0.0186  -0.0074 -0.0286 780  PHE A N   
5479  C CA  . PHE A 782  ? 0.2604 0.2280 0.2496 0.0174  -0.0082 -0.0293 780  PHE A CA  
5480  C C   . PHE A 782  ? 0.2913 0.2562 0.2813 0.0154  -0.0064 -0.0253 780  PHE A C   
5481  O O   . PHE A 782  ? 0.2476 0.2128 0.2382 0.0137  -0.0060 -0.0230 780  PHE A O   
5482  C CB  . PHE A 782  ? 0.2718 0.2375 0.2653 0.0158  -0.0109 -0.0316 780  PHE A CB  
5483  C CG  . PHE A 782  ? 0.2633 0.2244 0.2608 0.0142  -0.0118 -0.0315 780  PHE A CG  
5484  C CD1 . PHE A 782  ? 0.2673 0.2268 0.2657 0.0158  -0.0129 -0.0344 780  PHE A CD1 
5485  C CD2 . PHE A 782  ? 0.2569 0.2154 0.2572 0.0112  -0.0116 -0.0285 780  PHE A CD2 
5486  C CE1 . PHE A 782  ? 0.3046 0.2595 0.3068 0.0144  -0.0140 -0.0342 780  PHE A CE1 
5487  C CE2 . PHE A 782  ? 0.3015 0.2558 0.3054 0.0096  -0.0126 -0.0280 780  PHE A CE2 
5488  C CZ  . PHE A 782  ? 0.2906 0.2427 0.2955 0.0112  -0.0139 -0.0308 780  PHE A CZ  
5489  N N   . THR A 783  ? 0.2712 0.2340 0.2613 0.0158  -0.0056 -0.0247 781  THR A N   
5490  C CA  . THR A 783  ? 0.3044 0.2644 0.2961 0.0138  -0.0045 -0.0214 781  THR A CA  
5491  C C   . THR A 783  ? 0.2788 0.2351 0.2740 0.0132  -0.0060 -0.0227 781  THR A C   
5492  O O   . THR A 783  ? 0.2687 0.2248 0.2636 0.0151  -0.0063 -0.0250 781  THR A O   
5493  C CB  . THR A 783  ? 0.2682 0.2292 0.2566 0.0147  -0.0019 -0.0189 781  THR A CB  
5494  O OG1 . THR A 783  ? 0.2857 0.2498 0.2712 0.0153  -0.0009 -0.0176 781  THR A OG1 
5495  C CG2 . THR A 783  ? 0.2778 0.2361 0.2678 0.0127  -0.0008 -0.0157 781  THR A CG2 
5496  N N   . GLY A 784  ? 0.2726 0.2261 0.2713 0.0105  -0.0069 -0.0213 782  GLY A N   
5497  C CA  . GLY A 784  ? 0.3001 0.2496 0.3025 0.0097  -0.0088 -0.0223 782  GLY A CA  
5498  C C   . GLY A 784  ? 0.2939 0.2413 0.3000 0.0064  -0.0099 -0.0203 782  GLY A C   
5499  O O   . GLY A 784  ? 0.3153 0.2643 0.3207 0.0047  -0.0086 -0.0176 782  GLY A O   
5500  N N   . SER A 785  ? 0.2935 0.2374 0.3035 0.0054  -0.0124 -0.0217 783  SER A N   
5501  C CA  . SER A 785  ? 0.3388 0.2805 0.3526 0.0020  -0.0136 -0.0196 783  SER A CA  
5502  C C   . SER A 785  ? 0.3627 0.3073 0.3771 0.0006  -0.0142 -0.0201 783  SER A C   
5503  O O   . SER A 785  ? 0.2965 0.2433 0.3099 0.0023  -0.0150 -0.0233 783  SER A O   
5504  C CB  . SER A 785  ? 0.3316 0.2686 0.3497 0.0013  -0.0165 -0.0211 783  SER A CB  
5505  O OG  . SER A 785  ? 0.3673 0.3043 0.3865 0.0028  -0.0188 -0.0256 783  SER A OG  
5506  N N   . THR A 786  ? 0.3379 0.2828 0.3541 -0.0025 -0.0139 -0.0169 784  THR A N   
5507  C CA  . THR A 786  ? 0.3424 0.2901 0.3600 -0.0043 -0.0147 -0.0172 784  THR A CA  
5508  C C   . THR A 786  ? 0.3395 0.2854 0.3607 -0.0047 -0.0179 -0.0205 784  THR A C   
5509  O O   . THR A 786  ? 0.3345 0.2833 0.3559 -0.0045 -0.0187 -0.0226 784  THR A O   
5510  C CB  . THR A 786  ? 0.4069 0.3553 0.4265 -0.0077 -0.0139 -0.0132 784  THR A CB  
5511  O OG1 . THR A 786  ? 0.4146 0.3650 0.4309 -0.0071 -0.0111 -0.0106 784  THR A OG1 
5512  C CG2 . THR A 786  ? 0.4236 0.3756 0.4450 -0.0096 -0.0147 -0.0135 784  THR A CG2 
5513  N N   . GLU A 787  ? 0.3405 0.2816 0.3649 -0.0053 -0.0198 -0.0210 785  GLU A N   
5514  C CA  . GLU A 787  ? 0.3501 0.2889 0.3786 -0.0061 -0.0232 -0.0240 785  GLU A CA  
5515  C C   . GLU A 787  ? 0.3104 0.2506 0.3369 -0.0025 -0.0241 -0.0291 785  GLU A C   
5516  O O   . GLU A 787  ? 0.3004 0.2419 0.3287 -0.0028 -0.0261 -0.0319 785  GLU A O   
5517  C CB  . GLU A 787  ? 0.3649 0.2977 0.3974 -0.0075 -0.0253 -0.0233 785  GLU A CB  
5518  C CG  . GLU A 787  ? 0.4559 0.3861 0.4868 -0.0045 -0.0249 -0.0244 785  GLU A CG  
5519  C CD  . GLU A 787  ? 0.5294 0.4540 0.5638 -0.0062 -0.0265 -0.0221 785  GLU A CD  
5520  O OE1 . GLU A 787  ? 0.6104 0.5339 0.6474 -0.0099 -0.0268 -0.0184 785  GLU A OE1 
5521  O OE2 . GLU A 787  ? 0.5039 0.4255 0.5385 -0.0039 -0.0273 -0.0240 785  GLU A OE2 
5522  N N   . VAL A 788  ? 0.3139 0.2546 0.3367 0.0008  -0.0226 -0.0302 786  VAL A N   
5523  C CA  . VAL A 788  ? 0.2991 0.2421 0.3197 0.0042  -0.0232 -0.0348 786  VAL A CA  
5524  C C   . VAL A 788  ? 0.2631 0.2116 0.2803 0.0049  -0.0218 -0.0349 786  VAL A C   
5525  O O   . VAL A 788  ? 0.3002 0.2511 0.3171 0.0063  -0.0233 -0.0385 786  VAL A O   
5526  C CB  . VAL A 788  ? 0.3591 0.3016 0.3769 0.0073  -0.0220 -0.0358 786  VAL A CB  
5527  C CG1 . VAL A 788  ? 0.3346 0.2812 0.3488 0.0109  -0.0218 -0.0398 786  VAL A CG1 
5528  C CG2 . VAL A 788  ? 0.3555 0.2927 0.3773 0.0073  -0.0244 -0.0373 786  VAL A CG2 
5529  N N   . ALA A 789  ? 0.2649 0.2156 0.2796 0.0040  -0.0191 -0.0310 787  ALA A N   
5530  C CA  . ALA A 789  ? 0.2814 0.2369 0.2934 0.0045  -0.0180 -0.0308 787  ALA A CA  
5531  C C   . ALA A 789  ? 0.2670 0.2237 0.2824 0.0025  -0.0202 -0.0323 787  ALA A C   
5532  O O   . ALA A 789  ? 0.2624 0.2227 0.2764 0.0039  -0.0208 -0.0346 787  ALA A O   
5533  C CB  . ALA A 789  ? 0.2767 0.2336 0.2865 0.0035  -0.0151 -0.0265 787  ALA A CB  
5534  N N   . ARG A 790  ? 0.2690 0.2228 0.2890 -0.0008 -0.0215 -0.0307 788  ARG A N   
5535  C CA  . ARG A 790  ? 0.2654 0.2203 0.2893 -0.0032 -0.0237 -0.0318 788  ARG A CA  
5536  C C   . ARG A 790  ? 0.2947 0.2488 0.3203 -0.0017 -0.0267 -0.0369 788  ARG A C   
5537  O O   . ARG A 790  ? 0.3034 0.2604 0.3299 -0.0019 -0.0281 -0.0390 788  ARG A O   
5538  C CB  . ARG A 790  ? 0.3503 0.3022 0.3788 -0.0073 -0.0244 -0.0285 788  ARG A CB  
5539  C CG  . ARG A 790  ? 0.4581 0.4124 0.4903 -0.0106 -0.0256 -0.0277 788  ARG A CG  
5540  C CD  . ARG A 790  ? 0.3968 0.3488 0.4327 -0.0147 -0.0256 -0.0234 788  ARG A CD  
5541  N NE  . ARG A 790  ? 0.4472 0.4025 0.4807 -0.0156 -0.0225 -0.0194 788  ARG A NE  
5542  C CZ  . ARG A 790  ? 0.4138 0.3671 0.4467 -0.0165 -0.0209 -0.0159 788  ARG A CZ  
5543  N NH1 . ARG A 790  ? 0.4849 0.4328 0.5192 -0.0166 -0.0220 -0.0156 788  ARG A NH1 
5544  N NH2 . ARG A 790  ? 0.4599 0.4169 0.4907 -0.0171 -0.0183 -0.0129 788  ARG A NH2 
5545  N N   . LEU A 791  ? 0.2751 0.2254 0.3011 0.0000  -0.0278 -0.0390 789  LEU A N   
5546  C CA  . LEU A 791  ? 0.3126 0.2624 0.3397 0.0020  -0.0307 -0.0444 789  LEU A CA  
5547  C C   . LEU A 791  ? 0.3044 0.2595 0.3267 0.0054  -0.0297 -0.0471 789  LEU A C   
5548  O O   . LEU A 791  ? 0.3005 0.2576 0.3236 0.0063  -0.0319 -0.0510 789  LEU A O   
5549  C CB  . LEU A 791  ? 0.2734 0.2185 0.3018 0.0035  -0.0318 -0.0462 789  LEU A CB  
5550  C CG  . LEU A 791  ? 0.3550 0.2940 0.3888 0.0003  -0.0338 -0.0443 789  LEU A CG  
5551  C CD1 . LEU A 791  ? 0.3535 0.2883 0.3877 0.0025  -0.0345 -0.0460 789  LEU A CD1 
5552  C CD2 . LEU A 791  ? 0.3538 0.2915 0.3929 -0.0019 -0.0374 -0.0467 789  LEU A CD2 
5553  N N   . ILE A 792  ? 0.2624 0.2198 0.2797 0.0074  -0.0266 -0.0451 790  ILE A N   
5554  C CA  . ILE A 792  ? 0.3029 0.2654 0.3153 0.0105  -0.0256 -0.0469 790  ILE A CA  
5555  C C   . ILE A 792  ? 0.2587 0.2252 0.2712 0.0094  -0.0258 -0.0463 790  ILE A C   
5556  O O   . ILE A 792  ? 0.3001 0.2700 0.3114 0.0110  -0.0272 -0.0496 790  ILE A O   
5557  C CB  . ILE A 792  ? 0.2696 0.2333 0.2770 0.0124  -0.0223 -0.0442 790  ILE A CB  
5558  C CG1 . ILE A 792  ? 0.2628 0.2236 0.2702 0.0142  -0.0225 -0.0457 790  ILE A CG1 
5559  C CG2 . ILE A 792  ? 0.2609 0.2301 0.2633 0.0150  -0.0212 -0.0449 790  ILE A CG2 
5560  C CD1 . ILE A 792  ? 0.2810 0.2420 0.2848 0.0152  -0.0193 -0.0424 790  ILE A CD1 
5561  N N   . GLN A 793  ? 0.2752 0.2415 0.2889 0.0066  -0.0245 -0.0423 791  GLN A N   
5562  C CA  . GLN A 793  ? 0.2594 0.2297 0.2736 0.0054  -0.0246 -0.0416 791  GLN A CA  
5563  C C   . GLN A 793  ? 0.3123 0.2831 0.3305 0.0043  -0.0279 -0.0453 791  GLN A C   
5564  O O   . GLN A 793  ? 0.3064 0.2815 0.3237 0.0053  -0.0287 -0.0473 791  GLN A O   
5565  C CB  . GLN A 793  ? 0.2748 0.2446 0.2907 0.0023  -0.0230 -0.0371 791  GLN A CB  
5566  C CG  . GLN A 793  ? 0.3344 0.3085 0.3517 0.0007  -0.0232 -0.0363 791  GLN A CG  
5567  C CD  . GLN A 793  ? 0.4549 0.4283 0.4757 -0.0032 -0.0225 -0.0326 791  GLN A CD  
5568  O OE1 . GLN A 793  ? 0.4665 0.4360 0.4908 -0.0055 -0.0234 -0.0316 791  GLN A OE1 
5569  N NE2 . GLN A 793  ? 0.4583 0.4359 0.4783 -0.0037 -0.0210 -0.0306 791  GLN A NE2 
5570  N N   . ALA A 794  ? 0.3217 0.2880 0.3446 0.0023  -0.0301 -0.0464 792  ALA A N   
5571  C CA  . ALA A 794  ? 0.3299 0.2962 0.3574 0.0010  -0.0335 -0.0499 792  ALA A CA  
5572  C C   . ALA A 794  ? 0.3325 0.3007 0.3579 0.0046  -0.0352 -0.0553 792  ALA A C   
5573  O O   . ALA A 794  ? 0.3315 0.3027 0.3581 0.0045  -0.0373 -0.0582 792  ALA A O   
5574  C CB  . ALA A 794  ? 0.3365 0.2969 0.3696 -0.0020 -0.0356 -0.0495 792  ALA A CB  
5575  N N   . GLN A 795  ? 0.3207 0.2879 0.3426 0.0077  -0.0344 -0.0566 793  GLN A N   
5576  C CA  . GLN A 795  ? 0.3432 0.3132 0.3624 0.0113  -0.0357 -0.0616 793  GLN A CA  
5577  C C   . GLN A 795  ? 0.3346 0.3109 0.3491 0.0132  -0.0343 -0.0614 793  GLN A C   
5578  O O   . GLN A 795  ? 0.3322 0.3121 0.3463 0.0146  -0.0362 -0.0652 793  GLN A O   
5579  C CB  . GLN A 795  ? 0.3616 0.3298 0.3782 0.0142  -0.0349 -0.0629 793  GLN A CB  
5580  C CG  . GLN A 795  ? 0.4731 0.4356 0.4945 0.0134  -0.0373 -0.0651 793  GLN A CG  
5581  C CD  . GLN A 795  ? 0.5816 0.5440 0.6068 0.0135  -0.0413 -0.0705 793  GLN A CD  
5582  O OE1 . GLN A 795  ? 0.5526 0.5195 0.5752 0.0162  -0.0421 -0.0745 793  GLN A OE1 
5583  N NE2 . GLN A 795  ? 0.5484 0.5057 0.5799 0.0103  -0.0439 -0.0706 793  GLN A NE2 
5584  N N   . LEU A 796  ? 0.3436 0.3214 0.3546 0.0133  -0.0311 -0.0569 794  LEU A N   
5585  C CA  . LEU A 796  ? 0.3683 0.3516 0.3748 0.0152  -0.0299 -0.0562 794  LEU A CA  
5586  C C   . LEU A 796  ? 0.3732 0.3594 0.3824 0.0133  -0.0313 -0.0564 794  LEU A C   
5587  O O   . LEU A 796  ? 0.3959 0.3869 0.4023 0.0152  -0.0315 -0.0576 794  LEU A O   
5588  C CB  . LEU A 796  ? 0.2915 0.2750 0.2942 0.0155  -0.0264 -0.0513 794  LEU A CB  
5589  C CG  . LEU A 796  ? 0.3353 0.3173 0.3344 0.0177  -0.0246 -0.0508 794  LEU A CG  
5590  C CD1 . LEU A 796  ? 0.2977 0.2803 0.2935 0.0178  -0.0213 -0.0460 794  LEU A CD1 
5591  C CD2 . LEU A 796  ? 0.3516 0.3373 0.3472 0.0212  -0.0255 -0.0548 794  LEU A CD2 
5592  N N   . ALA A 797  ? 0.3229 0.3064 0.3374 0.0096  -0.0323 -0.0553 795  ALA A N   
5593  C CA  . ALA A 797  ? 0.4051 0.3919 0.4225 0.0076  -0.0334 -0.0552 795  ALA A CA  
5594  C C   . ALA A 797  ? 0.4082 0.3978 0.4269 0.0087  -0.0366 -0.0603 795  ALA A C   
5595  O O   . ALA A 797  ? 0.4750 0.4688 0.4945 0.0082  -0.0374 -0.0608 795  ALA A O   
5596  C CB  . ALA A 797  ? 0.3801 0.3639 0.4031 0.0032  -0.0338 -0.0527 795  ALA A CB  
5597  N N   . ASP A 798  ? 0.4400 0.4276 0.4590 0.0103  -0.0384 -0.0643 796  ASP A N   
5598  C CA  . ASP A 798  ? 0.4265 0.4166 0.4465 0.0116  -0.0416 -0.0697 796  ASP A CA  
5599  C C   . ASP A 798  ? 0.4816 0.4776 0.4957 0.0155  -0.0410 -0.0713 796  ASP A C   
5600  O O   . ASP A 798  ? 0.4666 0.4661 0.4814 0.0165  -0.0436 -0.0755 796  ASP A O   
5601  C CB  . ASP A 798  ? 0.4098 0.3957 0.4323 0.0122  -0.0439 -0.0738 796  ASP A CB  
5602  N N   . ARG A 799  ? 0.4318 0.4291 0.4404 0.0175  -0.0379 -0.0681 797  ARG A N   
5603  C CA  . ARG A 799  ? 0.3885 0.3909 0.3912 0.0213  -0.0374 -0.0694 797  ARG A CA  
5604  C C   . ARG A 799  ? 0.4085 0.4144 0.4079 0.0216  -0.0353 -0.0654 797  ARG A C   
5605  O O   . ARG A 799  ? 0.3509 0.3550 0.3517 0.0195  -0.0335 -0.0612 797  ARG A O   
5606  C CB  . ARG A 799  ? 0.4897 0.4909 0.4881 0.0239  -0.0357 -0.0694 797  ARG A CB  
5607  C CG  . ARG A 799  ? 0.4933 0.4905 0.4950 0.0239  -0.0375 -0.0732 797  ARG A CG  
5608  C CD  . ARG A 799  ? 0.4945 0.4940 0.4914 0.0277  -0.0370 -0.0758 797  ARG A CD  
5609  N NE  . ARG A 799  ? 0.5351 0.5355 0.5269 0.0290  -0.0334 -0.0714 797  ARG A NE  
5610  C CZ  . ARG A 799  ? 0.5001 0.4966 0.4919 0.0285  -0.0315 -0.0689 797  ARG A CZ  
5611  N NH1 . ARG A 799  ? 0.4722 0.4636 0.4685 0.0270  -0.0327 -0.0704 797  ARG A NH1 
5612  N NH2 . ARG A 799  ? 0.4434 0.4411 0.4306 0.0294  -0.0283 -0.0648 797  ARG A NH2 
5613  N N   . LEU A 800  ? 0.3659 0.3771 0.3611 0.0246  -0.0358 -0.0668 798  LEU A N   
5614  C CA  . LEU A 800  ? 0.3773 0.3919 0.3686 0.0257  -0.0340 -0.0633 798  LEU A CA  
5615  C C   . LEU A 800  ? 0.3471 0.3644 0.3317 0.0293  -0.0328 -0.0630 798  LEU A C   
5616  O O   . LEU A 800  ? 0.3647 0.3833 0.3477 0.0313  -0.0338 -0.0666 798  LEU A O   
5617  C CB  . LEU A 800  ? 0.4157 0.4349 0.4087 0.0255  -0.0361 -0.0647 798  LEU A CB  
5618  C CG  . LEU A 800  ? 0.4152 0.4328 0.4147 0.0217  -0.0370 -0.0642 798  LEU A CG  
5619  C CD1 . LEU A 800  ? 0.3854 0.4082 0.3866 0.0217  -0.0393 -0.0665 798  LEU A CD1 
5620  C CD2 . LEU A 800  ? 0.3562 0.3715 0.3559 0.0199  -0.0342 -0.0590 798  LEU A CD2 
5621  N N   . SER A 801  ? 0.3815 0.3999 0.3625 0.0302  -0.0305 -0.0586 799  SER A N   
5622  C CA  . SER A 801  ? 0.4026 0.4239 0.3772 0.0333  -0.0292 -0.0574 799  SER A CA  
5623  C C   . SER A 801  ? 0.4624 0.4898 0.4346 0.0357  -0.0314 -0.0604 799  SER A C   
5624  O O   . SER A 801  ? 0.4478 0.4768 0.4232 0.0349  -0.0338 -0.0630 799  SER A O   
5625  C CB  . SER A 801  ? 0.4140 0.4344 0.3859 0.0333  -0.0266 -0.0518 799  SER A CB  
5626  O OG  . SER A 801  ? 0.4219 0.4450 0.3940 0.0334  -0.0273 -0.0506 799  SER A OG  
5627  N N   . PRO A 802  ? 0.4814 0.5123 0.4476 0.0387  -0.0308 -0.0602 800  PRO A N   
5628  C CA  . PRO A 802  ? 0.5155 0.5527 0.4788 0.0411  -0.0328 -0.0623 800  PRO A CA  
5629  C C   . PRO A 802  ? 0.5083 0.5472 0.4724 0.0407  -0.0334 -0.0601 800  PRO A C   
5630  O O   . PRO A 802  ? 0.5218 0.5648 0.4866 0.0415  -0.0359 -0.0631 800  PRO A O   
5631  C CB  . PRO A 802  ? 0.5230 0.5632 0.4795 0.0439  -0.0311 -0.0604 800  PRO A CB  
5632  C CG  . PRO A 802  ? 0.5144 0.5507 0.4713 0.0433  -0.0292 -0.0603 800  PRO A CG  
5633  C CD  . PRO A 802  ? 0.4838 0.5139 0.4462 0.0400  -0.0285 -0.0585 800  PRO A CD  
5634  N N   . ALA A 803  ? 0.4558 0.4918 0.4201 0.0396  -0.0313 -0.0552 801  ALA A N   
5635  C CA  . ALA A 803  ? 0.4691 0.5065 0.4346 0.0392  -0.0319 -0.0532 801  ALA A CA  
5636  C C   . ALA A 803  ? 0.4931 0.5287 0.4654 0.0362  -0.0330 -0.0547 801  ALA A C   
5637  O O   . ALA A 803  ? 0.5126 0.5492 0.4866 0.0356  -0.0332 -0.0529 801  ALA A O   
5638  C CB  . ALA A 803  ? 0.5013 0.5366 0.4641 0.0395  -0.0294 -0.0475 801  ALA A CB  
5639  N N   . GLY A 804  ? 0.4948 0.5278 0.4710 0.0343  -0.0337 -0.0578 802  GLY A N   
5640  C CA  . GLY A 804  ? 0.4330 0.4645 0.4157 0.0311  -0.0349 -0.0590 802  GLY A CA  
5641  C C   . GLY A 804  ? 0.4186 0.4458 0.4041 0.0284  -0.0327 -0.0552 802  GLY A C   
5642  O O   . GLY A 804  ? 0.3680 0.3954 0.3583 0.0260  -0.0333 -0.0551 802  GLY A O   
5643  N N   . ARG A 805  ? 0.3650 0.3888 0.3478 0.0288  -0.0301 -0.0520 803  ARG A N   
5644  C CA  . ARG A 805  ? 0.3638 0.3837 0.3488 0.0264  -0.0280 -0.0484 803  ARG A CA  
5645  C C   . ARG A 805  ? 0.3531 0.3681 0.3406 0.0244  -0.0274 -0.0490 803  ARG A C   
5646  O O   . ARG A 805  ? 0.3251 0.3396 0.3114 0.0255  -0.0281 -0.0517 803  ARG A O   
5647  C CB  . ARG A 805  ? 0.3664 0.3855 0.3469 0.0280  -0.0255 -0.0440 803  ARG A CB  
5648  C CG  . ARG A 805  ? 0.4801 0.5032 0.4583 0.0300  -0.0261 -0.0427 803  ARG A CG  
5649  C CD  . ARG A 805  ? 0.4750 0.4962 0.4510 0.0305  -0.0238 -0.0381 803  ARG A CD  
5650  N NE  . ARG A 805  ? 0.5958 0.6204 0.5691 0.0329  -0.0245 -0.0368 803  ARG A NE  
5651  C CZ  . ARG A 805  ? 0.6870 0.7134 0.6550 0.0357  -0.0246 -0.0359 803  ARG A CZ  
5652  N NH1 . ARG A 805  ? 0.6397 0.6652 0.6047 0.0364  -0.0238 -0.0362 803  ARG A NH1 
5653  N NH2 . ARG A 805  ? 0.6834 0.7128 0.6494 0.0378  -0.0256 -0.0347 803  ARG A NH2 
5654  N N   . PRO A 806  ? 0.3069 0.3187 0.2981 0.0215  -0.0263 -0.0468 804  PRO A N   
5655  C CA  . PRO A 806  ? 0.3407 0.3475 0.3337 0.0198  -0.0255 -0.0466 804  PRO A CA  
5656  C C   . PRO A 806  ? 0.3331 0.3381 0.3214 0.0219  -0.0236 -0.0453 804  PRO A C   
5657  O O   . PRO A 806  ? 0.3303 0.3366 0.3144 0.0237  -0.0220 -0.0426 804  PRO A O   
5658  C CB  . PRO A 806  ? 0.3451 0.3498 0.3416 0.0168  -0.0241 -0.0434 804  PRO A CB  
5659  C CG  . PRO A 806  ? 0.3324 0.3414 0.3308 0.0163  -0.0251 -0.0435 804  PRO A CG  
5660  C CD  . PRO A 806  ? 0.3807 0.3936 0.3745 0.0198  -0.0257 -0.0444 804  PRO A CD  
5661  N N   . ILE A 807  ? 0.2989 0.3010 0.2880 0.0217  -0.0239 -0.0472 805  ILE A N   
5662  C CA  . ILE A 807  ? 0.2991 0.2996 0.2843 0.0235  -0.0221 -0.0461 805  ILE A CA  
5663  C C   . ILE A 807  ? 0.3177 0.3146 0.3034 0.0218  -0.0196 -0.0417 805  ILE A C   
5664  O O   . ILE A 807  ? 0.3162 0.3097 0.3060 0.0191  -0.0197 -0.0412 805  ILE A O   
5665  C CB  . ILE A 807  ? 0.3081 0.3067 0.2947 0.0239  -0.0234 -0.0499 805  ILE A CB  
5666  C CG1 . ILE A 807  ? 0.3485 0.3507 0.3352 0.0254  -0.0263 -0.0548 805  ILE A CG1 
5667  C CG2 . ILE A 807  ? 0.2857 0.2835 0.2683 0.0258  -0.0215 -0.0488 805  ILE A CG2 
5668  C CD1 . ILE A 807  ? 0.3219 0.3293 0.3030 0.0287  -0.0260 -0.0552 805  ILE A CD1 
5669  N N   . PRO A 808  ? 0.2973 0.2947 0.2788 0.0232  -0.0174 -0.0385 806  PRO A N   
5670  C CA  . PRO A 808  ? 0.3174 0.3114 0.2994 0.0217  -0.0152 -0.0346 806  PRO A CA  
5671  C C   . PRO A 808  ? 0.3042 0.2942 0.2879 0.0206  -0.0146 -0.0349 806  PRO A C   
5672  O O   . PRO A 808  ? 0.2854 0.2754 0.2673 0.0222  -0.0147 -0.0368 806  PRO A O   
5673  C CB  . PRO A 808  ? 0.2868 0.2824 0.2638 0.0238  -0.0134 -0.0317 806  PRO A CB  
5674  C CG  . PRO A 808  ? 0.3133 0.3134 0.2879 0.0259  -0.0148 -0.0334 806  PRO A CG  
5675  C CD  . PRO A 808  ? 0.3050 0.3062 0.2814 0.0261  -0.0171 -0.0380 806  PRO A CD  
5676  N N   . LEU A 809  ? 0.3124 0.2992 0.2995 0.0180  -0.0139 -0.0329 807  LEU A N   
5677  C CA  . LEU A 809  ? 0.3023 0.2850 0.2909 0.0168  -0.0131 -0.0322 807  LEU A CA  
5678  C C   . LEU A 809  ? 0.2934 0.2745 0.2813 0.0158  -0.0107 -0.0280 807  LEU A C   
5679  O O   . LEU A 809  ? 0.2721 0.2537 0.2617 0.0142  -0.0105 -0.0262 807  LEU A O   
5680  C CB  . LEU A 809  ? 0.3193 0.2995 0.3132 0.0143  -0.0150 -0.0339 807  LEU A CB  
5681  C CG  . LEU A 809  ? 0.2772 0.2528 0.2732 0.0127  -0.0143 -0.0325 807  LEU A CG  
5682  C CD1 . LEU A 809  ? 0.2868 0.2610 0.2808 0.0149  -0.0141 -0.0342 807  LEU A CD1 
5683  C CD2 . LEU A 809  ? 0.3058 0.2789 0.3072 0.0097  -0.0162 -0.0333 807  LEU A CD2 
5684  N N   . ILE A 810  ? 0.2536 0.2332 0.2389 0.0169  -0.0090 -0.0266 808  ILE A N   
5685  C CA  . ILE A 810  ? 0.2652 0.2427 0.2502 0.0158  -0.0069 -0.0229 808  ILE A CA  
5686  C C   . ILE A 810  ? 0.3054 0.2792 0.2930 0.0144  -0.0069 -0.0231 808  ILE A C   
5687  O O   . ILE A 810  ? 0.2840 0.2569 0.2705 0.0158  -0.0068 -0.0244 808  ILE A O   
5688  C CB  . ILE A 810  ? 0.2319 0.2103 0.2125 0.0178  -0.0050 -0.0209 808  ILE A CB  
5689  C CG1 . ILE A 810  ? 0.2879 0.2697 0.2657 0.0194  -0.0053 -0.0206 808  ILE A CG1 
5690  C CG2 . ILE A 810  ? 0.2825 0.2585 0.2633 0.0165  -0.0030 -0.0173 808  ILE A CG2 
5691  C CD1 . ILE A 810  ? 0.3210 0.3035 0.2947 0.0211  -0.0035 -0.0181 808  ILE A CD1 
5692  N N   . ALA A 811  ? 0.2743 0.2461 0.2654 0.0118  -0.0070 -0.0217 809  ALA A N   
5693  C CA  . ALA A 811  ? 0.2829 0.2510 0.2769 0.0102  -0.0074 -0.0217 809  ALA A CA  
5694  C C   . ALA A 811  ? 0.3216 0.2881 0.3159 0.0087  -0.0055 -0.0180 809  ALA A C   
5695  O O   . ALA A 811  ? 0.3121 0.2796 0.3076 0.0070  -0.0052 -0.0163 809  ALA A O   
5696  C CB  . ALA A 811  ? 0.3112 0.2783 0.3096 0.0082  -0.0098 -0.0235 809  ALA A CB  
5697  N N   . GLU A 812  ? 0.2916 0.2560 0.2846 0.0093  -0.0043 -0.0170 810  GLU A N   
5698  C CA  . GLU A 812  ? 0.3413 0.3038 0.3348 0.0079  -0.0027 -0.0139 810  GLU A CA  
5699  C C   . GLU A 812  ? 0.3250 0.2841 0.3219 0.0063  -0.0038 -0.0140 810  GLU A C   
5700  O O   . GLU A 812  ? 0.2878 0.2452 0.2847 0.0076  -0.0045 -0.0159 810  GLU A O   
5701  C CB  . GLU A 812  ? 0.3733 0.3360 0.3634 0.0096  -0.0007 -0.0124 810  GLU A CB  
5702  C CG  . GLU A 812  ? 0.4690 0.4308 0.4591 0.0082  0.0010  -0.0091 810  GLU A CG  
5703  C CD  . GLU A 812  ? 0.4775 0.4362 0.4689 0.0073  0.0015  -0.0079 810  GLU A CD  
5704  O OE1 . GLU A 812  ? 0.4577 0.4159 0.4475 0.0088  0.0024  -0.0080 810  GLU A OE1 
5705  O OE2 . GLU A 812  ? 0.4628 0.4202 0.4570 0.0051  0.0010  -0.0068 810  GLU A OE2 
5706  N N   . THR A 813  ? 0.2996 0.2577 0.2992 0.0036  -0.0040 -0.0122 811  THR A N   
5707  C CA  . THR A 813  ? 0.3122 0.2671 0.3155 0.0018  -0.0055 -0.0121 811  THR A CA  
5708  C C   . THR A 813  ? 0.3414 0.2949 0.3452 0.0001  -0.0041 -0.0087 811  THR A C   
5709  O O   . THR A 813  ? 0.3229 0.2774 0.3241 0.0008  -0.0021 -0.0070 811  THR A O   
5710  C CB  . THR A 813  ? 0.3291 0.2842 0.3357 -0.0001 -0.0076 -0.0135 811  THR A CB  
5711  O OG1 . THR A 813  ? 0.3192 0.2776 0.3259 -0.0015 -0.0069 -0.0120 811  THR A OG1 
5712  C CG2 . THR A 813  ? 0.3022 0.2582 0.3083 0.0020  -0.0092 -0.0174 811  THR A CG2 
5713  N N   . GLY A 814  ? 0.3448 0.2959 0.3521 -0.0023 -0.0054 -0.0077 812  GLY A N   
5714  C CA  . GLY A 814  ? 0.4475 0.3970 0.4552 -0.0036 -0.0044 -0.0047 812  GLY A CA  
5715  C C   . GLY A 814  ? 0.4402 0.3926 0.4473 -0.0052 -0.0028 -0.0020 812  GLY A C   
5716  O O   . GLY A 814  ? 0.3815 0.3373 0.3878 -0.0052 -0.0024 -0.0024 812  GLY A O   
5717  N N   . GLY A 815  ? 0.3606 0.3120 0.3678 -0.0064 -0.0019 0.0006  813  GLY A N   
5718  C CA  . GLY A 815  ? 0.3415 0.2957 0.3487 -0.0082 -0.0006 0.0032  813  GLY A CA  
5719  C C   . GLY A 815  ? 0.3190 0.2713 0.3282 -0.0105 -0.0010 0.0058  813  GLY A C   
5720  O O   . GLY A 815  ? 0.3891 0.3379 0.3988 -0.0099 -0.0016 0.0060  813  GLY A O   
5721  N N   . GLN A 816  ? 0.3196 0.2747 0.3302 -0.0130 -0.0007 0.0080  814  GLN A N   
5722  C CA  . GLN A 816  ? 0.2888 0.2433 0.3007 -0.0152 -0.0007 0.0111  814  GLN A CA  
5723  C C   . GLN A 816  ? 0.2667 0.2245 0.2761 -0.0148 0.0016  0.0125  814  GLN A C   
5724  O O   . GLN A 816  ? 0.2549 0.2168 0.2647 -0.0166 0.0023  0.0140  814  GLN A O   
5725  C CB  . GLN A 816  ? 0.2938 0.2494 0.3091 -0.0186 -0.0020 0.0127  814  GLN A CB  
5726  C CG  . GLN A 816  ? 0.3667 0.3210 0.3836 -0.0210 -0.0024 0.0161  814  GLN A CG  
5727  C CD  . GLN A 816  ? 0.4813 0.4297 0.4998 -0.0206 -0.0044 0.0159  814  GLN A CD  
5728  O OE1 . GLN A 816  ? 0.3779 0.3238 0.3946 -0.0183 -0.0039 0.0150  814  GLN A OE1 
5729  N NE2 . GLN A 816  ? 0.3951 0.3411 0.4172 -0.0229 -0.0066 0.0166  814  GLN A NE2 
5730  N N   . ASN A 817  ? 0.2522 0.2085 0.2591 -0.0125 0.0027  0.0119  815  ASN A N   
5731  C CA  . ASN A 817  ? 0.2568 0.2161 0.2612 -0.0114 0.0046  0.0122  815  ASN A CA  
5732  C C   . ASN A 817  ? 0.2423 0.2030 0.2468 -0.0130 0.0054  0.0149  815  ASN A C   
5733  O O   . ASN A 817  ? 0.2448 0.2027 0.2500 -0.0137 0.0048  0.0163  815  ASN A O   
5734  C CB  . ASN A 817  ? 0.2234 0.1807 0.2253 -0.0085 0.0054  0.0107  815  ASN A CB  
5735  C CG  . ASN A 817  ? 0.2450 0.2010 0.2466 -0.0069 0.0045  0.0081  815  ASN A CG  
5736  O OD1 . ASN A 817  ? 0.2452 0.2035 0.2469 -0.0069 0.0042  0.0070  815  ASN A OD1 
5737  N ND2 . ASN A 817  ? 0.2300 0.1828 0.2314 -0.0055 0.0039  0.0071  815  ASN A ND2 
5738  N N   . ALA A 818  ? 0.2405 0.2056 0.2443 -0.0136 0.0065  0.0154  816  ALA A N   
5739  C CA  . ALA A 818  ? 0.2173 0.1848 0.2211 -0.0151 0.0073  0.0177  816  ALA A CA  
5740  C C   . ALA A 818  ? 0.2065 0.1755 0.2078 -0.0133 0.0089  0.0172  816  ALA A C   
5741  O O   . ALA A 818  ? 0.2211 0.1904 0.2210 -0.0112 0.0094  0.0152  816  ALA A O   
5742  C CB  . ALA A 818  ? 0.2697 0.2421 0.2751 -0.0175 0.0073  0.0188  816  ALA A CB  
5743  N N   . MET A 819  ? 0.2346 0.2045 0.2355 -0.0141 0.0094  0.0190  817  MET A N   
5744  C CA  . MET A 819  ? 0.2200 0.1922 0.2191 -0.0129 0.0107  0.0186  817  MET A CA  
5745  C C   . MET A 819  ? 0.2410 0.2180 0.2405 -0.0149 0.0112  0.0204  817  MET A C   
5746  O O   . MET A 819  ? 0.2382 0.2148 0.2387 -0.0169 0.0106  0.0228  817  MET A O   
5747  C CB  . MET A 819  ? 0.2167 0.1854 0.2145 -0.0116 0.0110  0.0187  817  MET A CB  
5748  C CG  . MET A 819  ? 0.2227 0.1936 0.2190 -0.0106 0.0122  0.0184  817  MET A CG  
5749  S SD  . MET A 819  ? 0.2792 0.2464 0.2745 -0.0095 0.0124  0.0188  817  MET A SD  
5750  C CE  . MET A 819  ? 0.2650 0.2283 0.2596 -0.0072 0.0124  0.0169  817  MET A CE  
5751  N N   . ILE A 820  ? 0.2281 0.2096 0.2268 -0.0143 0.0121  0.0193  818  ILE A N   
5752  C CA  . ILE A 820  ? 0.2062 0.1932 0.2050 -0.0159 0.0127  0.0206  818  ILE A CA  
5753  C C   . ILE A 820  ? 0.2311 0.2188 0.2281 -0.0144 0.0136  0.0200  818  ILE A C   
5754  O O   . ILE A 820  ? 0.2052 0.1916 0.2011 -0.0121 0.0140  0.0179  818  ILE A O   
5755  C CB  . ILE A 820  ? 0.2333 0.2259 0.2329 -0.0162 0.0131  0.0195  818  ILE A CB  
5756  C CG1 . ILE A 820  ? 0.2434 0.2357 0.2450 -0.0180 0.0121  0.0202  818  ILE A CG1 
5757  C CG2 . ILE A 820  ? 0.2359 0.2351 0.2354 -0.0176 0.0139  0.0206  818  ILE A CG2 
5758  C CD1 . ILE A 820  ? 0.2408 0.2390 0.2436 -0.0184 0.0124  0.0191  818  ILE A CD1 
5759  N N   . VAL A 821  ? 0.2178 0.2075 0.2147 -0.0159 0.0137  0.0221  819  VAL A N   
5760  C CA  . VAL A 821  ? 0.2319 0.2222 0.2273 -0.0148 0.0143  0.0217  819  VAL A CA  
5761  C C   . VAL A 821  ? 0.2611 0.2584 0.2562 -0.0161 0.0149  0.0225  819  VAL A C   
5762  O O   . VAL A 821  ? 0.2500 0.2494 0.2458 -0.0185 0.0146  0.0252  819  VAL A O   
5763  C CB  . VAL A 821  ? 0.2150 0.2007 0.2101 -0.0150 0.0138  0.0234  819  VAL A CB  
5764  C CG1 . VAL A 821  ? 0.2221 0.2093 0.2160 -0.0142 0.0143  0.0231  819  VAL A CG1 
5765  C CG2 . VAL A 821  ? 0.2219 0.2015 0.2173 -0.0136 0.0133  0.0224  819  VAL A CG2 
5766  N N   . ASP A 822  ? 0.2364 0.2373 0.2306 -0.0145 0.0157  0.0202  820  ASP A N   
5767  C CA  . ASP A 822  ? 0.2305 0.2388 0.2243 -0.0155 0.0163  0.0205  820  ASP A CA  
5768  C C   . ASP A 822  ? 0.2661 0.2749 0.2585 -0.0149 0.0164  0.0206  820  ASP A C   
5769  O O   . ASP A 822  ? 0.2456 0.2491 0.2376 -0.0139 0.0161  0.0205  820  ASP A O   
5770  C CB  . ASP A 822  ? 0.2627 0.2763 0.2569 -0.0143 0.0168  0.0177  820  ASP A CB  
5771  C CG  . ASP A 822  ? 0.2569 0.2691 0.2503 -0.0112 0.0170  0.0144  820  ASP A CG  
5772  O OD1 . ASP A 822  ? 0.2680 0.2765 0.2604 -0.0103 0.0168  0.0141  820  ASP A OD1 
5773  O OD2 . ASP A 822  ? 0.2584 0.2733 0.2523 -0.0098 0.0171  0.0119  820  ASP A OD2 
5774  N N   . SER A 823  ? 0.2435 0.2594 0.2354 -0.0157 0.0170  0.0209  821  SER A N   
5775  C CA  . SER A 823  ? 0.2800 0.2971 0.2705 -0.0154 0.0170  0.0211  821  SER A CA  
5776  C C   . SER A 823  ? 0.2769 0.2926 0.2668 -0.0126 0.0171  0.0176  821  SER A C   
5777  O O   . SER A 823  ? 0.2868 0.3031 0.2757 -0.0122 0.0170  0.0174  821  SER A O   
5778  C CB  . SER A 823  ? 0.2692 0.2951 0.2591 -0.0170 0.0175  0.0223  821  SER A CB  
5779  O OG  . SER A 823  ? 0.2710 0.3029 0.2611 -0.0160 0.0182  0.0196  821  SER A OG  
5780  N N   . SER A 824  ? 0.2645 0.2782 0.2550 -0.0108 0.0171  0.0149  822  SER A N   
5781  C CA  . SER A 824  ? 0.2251 0.2364 0.2153 -0.0083 0.0170  0.0119  822  SER A CA  
5782  C C   . SER A 824  ? 0.2786 0.2818 0.2688 -0.0076 0.0165  0.0123  822  SER A C   
5783  O O   . SER A 824  ? 0.2902 0.2909 0.2802 -0.0060 0.0163  0.0105  822  SER A O   
5784  C CB  . SER A 824  ? 0.2705 0.2838 0.2613 -0.0065 0.0170  0.0087  822  SER A CB  
5785  O OG  . SER A 824  ? 0.2408 0.2494 0.2323 -0.0062 0.0168  0.0090  822  SER A OG  
5786  N N   . ALA A 825  ? 0.2440 0.2434 0.2346 -0.0088 0.0163  0.0146  823  ALA A N   
5787  C CA  . ALA A 825  ? 0.2757 0.2682 0.2664 -0.0081 0.0160  0.0149  823  ALA A CA  
5788  C C   . ALA A 825  ? 0.2535 0.2446 0.2438 -0.0082 0.0158  0.0158  823  ALA A C   
5789  O O   . ALA A 825  ? 0.2949 0.2894 0.2847 -0.0094 0.0158  0.0172  823  ALA A O   
5790  C CB  . ALA A 825  ? 0.2656 0.2550 0.2570 -0.0092 0.0157  0.0169  823  ALA A CB  
5791  N N   . LEU A 826  ? 0.2659 0.2520 0.2562 -0.0070 0.0157  0.0151  824  LEU A N   
5792  C CA  . LEU A 826  ? 0.3238 0.3080 0.3140 -0.0071 0.0155  0.0159  824  LEU A CA  
5793  C C   . LEU A 826  ? 0.3247 0.3057 0.3152 -0.0082 0.0151  0.0184  824  LEU A C   
5794  O O   . LEU A 826  ? 0.2887 0.2657 0.2797 -0.0077 0.0150  0.0185  824  LEU A O   
5795  C CB  . LEU A 826  ? 0.3438 0.3245 0.3341 -0.0055 0.0155  0.0141  824  LEU A CB  
5796  C CG  . LEU A 826  ? 0.4577 0.4368 0.4482 -0.0055 0.0152  0.0145  824  LEU A CG  
5797  C CD1 . LEU A 826  ? 0.5245 0.5083 0.5145 -0.0061 0.0150  0.0146  824  LEU A CD1 
5798  C CD2 . LEU A 826  ? 0.5219 0.4980 0.5129 -0.0041 0.0152  0.0128  824  LEU A CD2 
5799  N N   . ALA A 827  ? 0.2921 0.2751 0.2826 -0.0095 0.0148  0.0205  825  ALA A N   
5800  C CA  . ALA A 827  ? 0.3045 0.2846 0.2956 -0.0106 0.0141  0.0230  825  ALA A CA  
5801  C C   . ALA A 827  ? 0.3078 0.2826 0.2995 -0.0095 0.0139  0.0226  825  ALA A C   
5802  O O   . ALA A 827  ? 0.2953 0.2669 0.2878 -0.0096 0.0136  0.0233  825  ALA A O   
5803  C CB  . ALA A 827  ? 0.3470 0.3298 0.3379 -0.0119 0.0136  0.0252  825  ALA A CB  
5804  N N   . GLU A 828  ? 0.2972 0.2712 0.2888 -0.0084 0.0142  0.0215  826  GLU A N   
5805  C CA  . GLU A 828  ? 0.3180 0.2877 0.3101 -0.0075 0.0141  0.0213  826  GLU A CA  
5806  C C   . GLU A 828  ? 0.3049 0.2719 0.2971 -0.0065 0.0145  0.0201  826  GLU A C   
5807  O O   . GLU A 828  ? 0.2761 0.2401 0.2689 -0.0061 0.0143  0.0204  826  GLU A O   
5808  C CB  . GLU A 828  ? 0.3587 0.3288 0.3509 -0.0067 0.0143  0.0202  826  GLU A CB  
5809  C CG  . GLU A 828  ? 0.4255 0.3975 0.4177 -0.0074 0.0137  0.0215  826  GLU A CG  
5810  C CD  . GLU A 828  ? 0.5051 0.4820 0.4965 -0.0082 0.0137  0.0216  826  GLU A CD  
5811  O OE1 . GLU A 828  ? 0.4617 0.4405 0.4524 -0.0082 0.0141  0.0204  826  GLU A OE1 
5812  O OE2 . GLU A 828  ? 0.6076 0.5867 0.5987 -0.0089 0.0131  0.0229  826  GLU A OE2 
5813  N N   . GLN A 829  ? 0.2720 0.2403 0.2637 -0.0060 0.0150  0.0185  827  GLN A N   
5814  C CA  . GLN A 829  ? 0.2697 0.2358 0.2613 -0.0051 0.0152  0.0175  827  GLN A CA  
5815  C C   . GLN A 829  ? 0.2545 0.2201 0.2463 -0.0058 0.0148  0.0184  827  GLN A C   
5816  O O   . GLN A 829  ? 0.2786 0.2414 0.2706 -0.0052 0.0147  0.0182  827  GLN A O   
5817  C CB  . GLN A 829  ? 0.3262 0.2939 0.3173 -0.0043 0.0155  0.0158  827  GLN A CB  
5818  N N   . VAL A 830  ? 0.2631 0.2317 0.2552 -0.0071 0.0146  0.0193  828  VAL A N   
5819  C CA  . VAL A 830  ? 0.2407 0.2090 0.2334 -0.0082 0.0140  0.0203  828  VAL A CA  
5820  C C   . VAL A 830  ? 0.2362 0.2009 0.2298 -0.0083 0.0133  0.0215  828  VAL A C   
5821  O O   . VAL A 830  ? 0.2349 0.1971 0.2290 -0.0081 0.0129  0.0212  828  VAL A O   
5822  C CB  . VAL A 830  ? 0.2376 0.2102 0.2305 -0.0099 0.0139  0.0217  828  VAL A CB  
5823  C CG1 . VAL A 830  ? 0.2664 0.2380 0.2604 -0.0114 0.0131  0.0233  828  VAL A CG1 
5824  C CG2 . VAL A 830  ? 0.2716 0.2481 0.2639 -0.0095 0.0145  0.0200  828  VAL A CG2 
5825  N N   . VAL A 831  ? 0.2508 0.2152 0.2446 -0.0086 0.0130  0.0227  829  VAL A N   
5826  C CA  . VAL A 831  ? 0.2391 0.2004 0.2341 -0.0087 0.0121  0.0238  829  VAL A CA  
5827  C C   . VAL A 831  ? 0.2527 0.2107 0.2477 -0.0070 0.0123  0.0223  829  VAL A C   
5828  O O   . VAL A 831  ? 0.2411 0.1966 0.2371 -0.0067 0.0115  0.0222  829  VAL A O   
5829  C CB  . VAL A 831  ? 0.2506 0.2127 0.2457 -0.0092 0.0116  0.0254  829  VAL A CB  
5830  C CG1 . VAL A 831  ? 0.2570 0.2155 0.2535 -0.0087 0.0106  0.0261  829  VAL A CG1 
5831  C CG2 . VAL A 831  ? 0.2865 0.2518 0.2815 -0.0111 0.0112  0.0274  829  VAL A CG2 
5832  N N   . GLY A 832  ? 0.2295 0.1878 0.2237 -0.0058 0.0132  0.0210  830  GLY A N   
5833  C CA  . GLY A 832  ? 0.2533 0.2093 0.2474 -0.0044 0.0136  0.0197  830  GLY A CA  
5834  C C   . GLY A 832  ? 0.2868 0.2420 0.2807 -0.0040 0.0136  0.0188  830  GLY A C   
5835  O O   . GLY A 832  ? 0.2498 0.2029 0.2440 -0.0032 0.0132  0.0182  830  GLY A O   
5836  N N   . ASP A 833  ? 0.2122 0.1692 0.2054 -0.0044 0.0138  0.0184  831  ASP A N   
5837  C CA  . ASP A 833  ? 0.2545 0.2110 0.2475 -0.0040 0.0137  0.0174  831  ASP A CA  
5838  C C   . ASP A 833  ? 0.2121 0.1677 0.2063 -0.0049 0.0126  0.0179  831  ASP A C   
5839  O O   . ASP A 833  ? 0.2403 0.1945 0.2347 -0.0043 0.0122  0.0169  831  ASP A O   
5840  C CB  . ASP A 833  ? 0.2434 0.2024 0.2356 -0.0041 0.0142  0.0167  831  ASP A CB  
5841  C CG  . ASP A 833  ? 0.2612 0.2202 0.2524 -0.0029 0.0149  0.0159  831  ASP A CG  
5842  O OD1 . ASP A 833  ? 0.2669 0.2240 0.2579 -0.0021 0.0152  0.0158  831  ASP A OD1 
5843  O OD2 . ASP A 833  ? 0.2965 0.2575 0.2873 -0.0028 0.0152  0.0153  831  ASP A OD2 
5844  N N   . VAL A 834  ? 0.2252 0.1815 0.2203 -0.0064 0.0120  0.0196  832  VAL A N   
5845  C CA  . VAL A 834  ? 0.2221 0.1771 0.2188 -0.0076 0.0107  0.0204  832  VAL A CA  
5846  C C   . VAL A 834  ? 0.2368 0.1883 0.2345 -0.0066 0.0098  0.0201  832  VAL A C   
5847  O O   . VAL A 834  ? 0.2302 0.1797 0.2288 -0.0062 0.0089  0.0192  832  VAL A O   
5848  C CB  . VAL A 834  ? 0.2350 0.1919 0.2324 -0.0097 0.0102  0.0227  832  VAL A CB  
5849  C CG1 . VAL A 834  ? 0.2318 0.1867 0.2312 -0.0109 0.0086  0.0241  832  VAL A CG1 
5850  C CG2 . VAL A 834  ? 0.2510 0.2121 0.2477 -0.0106 0.0109  0.0227  832  VAL A CG2 
5851  N N   . ILE A 835  ? 0.2130 0.1638 0.2107 -0.0060 0.0100  0.0206  833  ILE A N   
5852  C CA  . ILE A 835  ? 0.2385 0.1865 0.2372 -0.0048 0.0092  0.0200  833  ILE A CA  
5853  C C   . ILE A 835  ? 0.2492 0.1964 0.2473 -0.0030 0.0097  0.0178  833  ILE A C   
5854  O O   . ILE A 835  ? 0.2389 0.1840 0.2382 -0.0023 0.0086  0.0167  833  ILE A O   
5855  C CB  . ILE A 835  ? 0.2784 0.2269 0.2771 -0.0042 0.0097  0.0207  833  ILE A CB  
5856  C CG1 . ILE A 835  ? 0.2961 0.2452 0.2954 -0.0059 0.0088  0.0231  833  ILE A CG1 
5857  C CG2 . ILE A 835  ? 0.2808 0.2272 0.2804 -0.0025 0.0092  0.0195  833  ILE A CG2 
5858  C CD1 . ILE A 835  ? 0.2979 0.2444 0.2993 -0.0065 0.0069  0.0243  833  ILE A CD1 
5859  N N   . THR A 836  ? 0.2368 0.1856 0.2332 -0.0023 0.0111  0.0169  834  THR A N   
5860  C CA  . THR A 836  ? 0.2485 0.1969 0.2439 -0.0007 0.0115  0.0151  834  THR A CA  
5861  C C   . THR A 836  ? 0.2518 0.1998 0.2476 -0.0010 0.0108  0.0142  834  THR A C   
5862  O O   . THR A 836  ? 0.2480 0.1947 0.2442 0.0001  0.0101  0.0127  834  THR A O   
5863  C CB  . THR A 836  ? 0.2832 0.2332 0.2769 -0.0002 0.0130  0.0149  834  THR A CB  
5864  O OG1 . THR A 836  ? 0.3392 0.2895 0.3331 0.0001  0.0136  0.0155  834  THR A OG1 
5865  C CG2 . THR A 836  ? 0.2747 0.2248 0.2673 0.0012  0.0135  0.0135  834  THR A CG2 
5866  N N   . SER A 837  ? 0.2102 0.1596 0.2058 -0.0023 0.0107  0.0149  835  SER A N   
5867  C CA  . SER A 837  ? 0.2411 0.1906 0.2370 -0.0025 0.0101  0.0139  835  SER A CA  
5868  C C   . SER A 837  ? 0.2418 0.1891 0.2397 -0.0031 0.0084  0.0138  835  SER A C   
5869  O O   . SER A 837  ? 0.2246 0.1711 0.2230 -0.0025 0.0076  0.0121  835  SER A O   
5870  C CB  . SER A 837  ? 0.2059 0.1580 0.2015 -0.0039 0.0104  0.0146  835  SER A CB  
5871  O OG  . SER A 837  ? 0.2306 0.1843 0.2244 -0.0030 0.0117  0.0143  835  SER A OG  
5872  N N   . ALA A 838  ? 0.2101 0.1564 0.2096 -0.0043 0.0076  0.0154  836  ALA A N   
5873  C CA  . ALA A 838  ? 0.2188 0.1625 0.2207 -0.0052 0.0056  0.0157  836  ALA A CA  
5874  C C   . ALA A 838  ? 0.2440 0.1849 0.2468 -0.0034 0.0047  0.0142  836  ALA A C   
5875  O O   . ALA A 838  ? 0.2552 0.1939 0.2597 -0.0032 0.0031  0.0130  836  ALA A O   
5876  C CB  . ALA A 838  ? 0.2136 0.1574 0.2167 -0.0074 0.0050  0.0185  836  ALA A CB  
5877  N N   . PHE A 839  ? 0.2409 0.1820 0.2429 -0.0020 0.0056  0.0141  837  PHE A N   
5878  C CA  . PHE A 839  ? 0.2438 0.1827 0.2471 -0.0005 0.0046  0.0129  837  PHE A CA  
5879  C C   . PHE A 839  ? 0.2569 0.1969 0.2588 0.0019  0.0057  0.0106  837  PHE A C   
5880  O O   . PHE A 839  ? 0.2308 0.1695 0.2339 0.0036  0.0048  0.0089  837  PHE A O   
5881  C CB  . PHE A 839  ? 0.2282 0.1664 0.2325 -0.0010 0.0043  0.0149  837  PHE A CB  
5882  C CG  . PHE A 839  ? 0.2518 0.1893 0.2574 -0.0034 0.0031  0.0176  837  PHE A CG  
5883  C CD1 . PHE A 839  ? 0.2544 0.1894 0.2621 -0.0044 0.0012  0.0177  837  PHE A CD1 
5884  C CD2 . PHE A 839  ? 0.2547 0.1942 0.2595 -0.0047 0.0040  0.0199  837  PHE A CD2 
5885  C CE1 . PHE A 839  ? 0.2450 0.1798 0.2540 -0.0070 0.0002  0.0205  837  PHE A CE1 
5886  C CE2 . PHE A 839  ? 0.2332 0.1727 0.2389 -0.0071 0.0031  0.0226  837  PHE A CE2 
5887  C CZ  . PHE A 839  ? 0.2334 0.1706 0.2412 -0.0083 0.0012  0.0231  837  PHE A CZ  
5888  N N   . ASP A 840  ? 0.2563 0.1988 0.2558 0.0022  0.0075  0.0105  838  ASP A N   
5889  C CA  . ASP A 840  ? 0.2753 0.2192 0.2734 0.0042  0.0086  0.0087  838  ASP A CA  
5890  C C   . ASP A 840  ? 0.2458 0.1887 0.2445 0.0054  0.0073  0.0062  838  ASP A C   
5891  O O   . ASP A 840  ? 0.2757 0.2177 0.2750 0.0045  0.0062  0.0059  838  ASP A O   
5892  C CB  . ASP A 840  ? 0.2766 0.2227 0.2722 0.0040  0.0102  0.0091  838  ASP A CB  
5893  C CG  . ASP A 840  ? 0.3247 0.2725 0.3186 0.0059  0.0113  0.0077  838  ASP A CG  
5894  O OD1 . ASP A 840  ? 0.3082 0.2563 0.3015 0.0068  0.0109  0.0060  838  ASP A OD1 
5895  O OD2 . ASP A 840  ? 0.3688 0.3177 0.3620 0.0063  0.0125  0.0084  838  ASP A OD2 
5896  N N   . SER A 841  ? 0.2353 0.1787 0.2340 0.0075  0.0074  0.0043  839  SER A N   
5897  C CA  . SER A 841  ? 0.2818 0.2247 0.2811 0.0090  0.0061  0.0014  839  SER A CA  
5898  C C   . SER A 841  ? 0.2332 0.1727 0.2354 0.0082  0.0037  0.0010  839  SER A C   
5899  O O   . SER A 841  ? 0.2478 0.1865 0.2508 0.0085  0.0023  -0.0009 839  SER A O   
5900  C CB  . SER A 841  ? 0.2897 0.2346 0.2868 0.0093  0.0068  0.0004  839  SER A CB  
5901  O OG  . SER A 841  ? 0.2896 0.2372 0.2841 0.0097  0.0089  0.0013  839  SER A OG  
5902  N N   . ALA A 842  ? 0.2366 0.1741 0.2407 0.0071  0.0029  0.0030  840  ALA A N   
5903  C CA  . ALA A 842  ? 0.2313 0.1652 0.2384 0.0060  0.0005  0.0033  840  ALA A CA  
5904  C C   . ALA A 842  ? 0.2398 0.1732 0.2471 0.0040  -0.0002 0.0040  840  ALA A C   
5905  O O   . ALA A 842  ? 0.2694 0.2003 0.2791 0.0035  -0.0023 0.0031  840  ALA A O   
5906  C CB  . ALA A 842  ? 0.2744 0.2064 0.2837 0.0082  -0.0015 0.0002  840  ALA A CB  
5907  N N   . GLY A 843  ? 0.2448 0.1809 0.2499 0.0028  0.0016  0.0055  841  GLY A N   
5908  C CA  . GLY A 843  ? 0.2207 0.1572 0.2260 0.0010  0.0012  0.0061  841  GLY A CA  
5909  C C   . GLY A 843  ? 0.2549 0.1915 0.2601 0.0020  0.0004  0.0032  841  GLY A C   
5910  O O   . GLY A 843  ? 0.2895 0.2259 0.2958 0.0004  -0.0006 0.0033  841  GLY A O   
5911  N N   . GLN A 844  ? 0.2228 0.1602 0.2270 0.0045  0.0007  0.0005  842  GLN A N   
5912  C CA  . GLN A 844  ? 0.2554 0.1933 0.2593 0.0058  -0.0002 -0.0025 842  GLN A CA  
5913  C C   . GLN A 844  ? 0.2789 0.2203 0.2796 0.0062  0.0016  -0.0026 842  GLN A C   
5914  O O   . GLN A 844  ? 0.3749 0.3180 0.3742 0.0081  0.0017  -0.0051 842  GLN A O   
5915  C CB  . GLN A 844  ? 0.2268 0.1642 0.2313 0.0084  -0.0010 -0.0055 842  GLN A CB  
5916  C CG  . GLN A 844  ? 0.2341 0.1675 0.2422 0.0081  -0.0033 -0.0056 842  GLN A CG  
5917  C CD  . GLN A 844  ? 0.2580 0.1909 0.2671 0.0110  -0.0043 -0.0090 842  GLN A CD  
5918  O OE1 . GLN A 844  ? 0.2688 0.1988 0.2809 0.0115  -0.0069 -0.0111 842  GLN A OE1 
5919  N NE2 . GLN A 844  ? 0.2799 0.2160 0.2867 0.0130  -0.0024 -0.0097 842  GLN A NE2 
5920  N N   . ARG A 845  ? 0.2783 0.2210 0.2779 0.0047  0.0030  -0.0001 843  ARG A N   
5921  C CA  . ARG A 845  ? 0.2726 0.2181 0.2697 0.0049  0.0042  0.0000  843  ARG A CA  
5922  C C   . ARG A 845  ? 0.2797 0.2253 0.2781 0.0031  0.0031  0.0001  843  ARG A C   
5923  O O   . ARG A 845  ? 0.2964 0.2406 0.2970 0.0010  0.0023  0.0017  843  ARG A O   
5924  C CB  . ARG A 845  ? 0.2645 0.2114 0.2597 0.0045  0.0063  0.0023  843  ARG A CB  
5925  C CG  . ARG A 845  ? 0.2871 0.2345 0.2810 0.0060  0.0075  0.0024  843  ARG A CG  
5926  C CD  . ARG A 845  ? 0.2987 0.2474 0.2911 0.0054  0.0093  0.0046  843  ARG A CD  
5927  N NE  . ARG A 845  ? 0.3651 0.3145 0.3564 0.0066  0.0105  0.0048  843  ARG A NE  
5928  C CZ  . ARG A 845  ? 0.3272 0.2784 0.3162 0.0078  0.0117  0.0046  843  ARG A CZ  
5929  N NH1 . ARG A 845  ? 0.3695 0.3220 0.3569 0.0082  0.0117  0.0041  843  ARG A NH1 
5930  N NH2 . ARG A 845  ? 0.3665 0.3186 0.3549 0.0085  0.0128  0.0051  843  ARG A NH2 
5931  N N   . CYS A 846  ? 0.2848 0.2323 0.2819 0.0039  0.0031  -0.0015 844  CYS A N   
5932  C CA  A CYS A 846  ? 0.3125 0.2609 0.3109 0.0022  0.0022  -0.0013 844  CYS A CA  
5933  C CA  B CYS A 846  ? 0.3124 0.2607 0.3107 0.0022  0.0022  -0.0013 844  CYS A CA  
5934  C C   . CYS A 846  ? 0.2498 0.1996 0.2478 0.0005  0.0035  0.0014  844  CYS A C   
5935  O O   . CYS A 846  ? 0.2506 0.2009 0.2505 -0.0015 0.0028  0.0023  844  CYS A O   
5936  C CB  A CYS A 846  ? 0.3456 0.2961 0.3424 0.0036  0.0019  -0.0035 844  CYS A CB  
5937  C CB  B CYS A 846  ? 0.3452 0.2957 0.3419 0.0036  0.0020  -0.0035 844  CYS A CB  
5938  S SG  A CYS A 846  ? 0.5003 0.4498 0.4979 0.0055  0.0001  -0.0072 844  CYS A SG  
5939  S SG  B CYS A 846  ? 0.3193 0.2724 0.3120 0.0057  0.0042  -0.0029 844  CYS A SG  
5940  N N   . SER A 847  ? 0.2401 0.1909 0.2360 0.0014  0.0052  0.0025  845  SER A N   
5941  C CA  . SER A 847  ? 0.2330 0.1852 0.2283 0.0002  0.0065  0.0047  845  SER A CA  
5942  C C   . SER A 847  ? 0.2529 0.2039 0.2497 -0.0014 0.0065  0.0067  845  SER A C   
5943  O O   . SER A 847  ? 0.2257 0.1782 0.2221 -0.0023 0.0075  0.0084  845  SER A O   
5944  C CB  . SER A 847  ? 0.2879 0.2412 0.2804 0.0019  0.0081  0.0049  845  SER A CB  
5945  O OG  . SER A 847  ? 0.3449 0.2967 0.3369 0.0029  0.0084  0.0048  845  SER A OG  
5946  N N   . ALA A 848  ? 0.2315 0.1799 0.2299 -0.0015 0.0054  0.0066  846  ALA A N   
5947  C CA  . ALA A 848  ? 0.2438 0.1909 0.2432 -0.0025 0.0055  0.0086  846  ALA A CA  
5948  C C   . ALA A 848  ? 0.2148 0.1631 0.2156 -0.0051 0.0053  0.0107  846  ALA A C   
5949  O O   . ALA A 848  ? 0.2416 0.1908 0.2436 -0.0064 0.0044  0.0105  846  ALA A O   
5950  C CB  . ALA A 848  ? 0.2428 0.1866 0.2441 -0.0021 0.0040  0.0079  846  ALA A CB  
5951  N N   . LEU A 849  ? 0.2114 0.1604 0.2118 -0.0059 0.0062  0.0127  847  LEU A N   
5952  C CA  . LEU A 849  ? 0.2112 0.1620 0.2126 -0.0083 0.0061  0.0149  847  LEU A CA  
5953  C C   . LEU A 849  ? 0.2261 0.1747 0.2303 -0.0101 0.0042  0.0162  847  LEU A C   
5954  O O   . LEU A 849  ? 0.2442 0.1900 0.2493 -0.0099 0.0035  0.0168  847  LEU A O   
5955  C CB  . LEU A 849  ? 0.2094 0.1617 0.2096 -0.0084 0.0074  0.0165  847  LEU A CB  
5956  C CG  . LEU A 849  ? 0.2268 0.1817 0.2277 -0.0108 0.0074  0.0189  847  LEU A CG  
5957  C CD1 . LEU A 849  ? 0.2191 0.1777 0.2199 -0.0115 0.0079  0.0183  847  LEU A CD1 
5958  C CD2 . LEU A 849  ? 0.2253 0.1815 0.2250 -0.0106 0.0085  0.0200  847  LEU A CD2 
5959  N N   . ARG A 850  ? 0.2149 0.1647 0.2208 -0.0120 0.0034  0.0166  848  ARG A N   
5960  C CA  . ARG A 850  ? 0.2585 0.2060 0.2674 -0.0141 0.0014  0.0180  848  ARG A CA  
5961  C C   . ARG A 850  ? 0.2336 0.1836 0.2433 -0.0169 0.0016  0.0214  848  ARG A C   
5962  O O   . ARG A 850  ? 0.2221 0.1697 0.2336 -0.0185 0.0002  0.0235  848  ARG A O   
5963  C CB  . ARG A 850  ? 0.2313 0.1784 0.2420 -0.0146 0.0000  0.0163  848  ARG A CB  
5964  C CG  . ARG A 850  ? 0.2508 0.1963 0.2603 -0.0119 -0.0001 0.0129  848  ARG A CG  
5965  C CD  . ARG A 850  ? 0.2578 0.1995 0.2675 -0.0101 -0.0008 0.0120  848  ARG A CD  
5966  N NE  . ARG A 850  ? 0.2702 0.2110 0.2790 -0.0075 -0.0010 0.0087  848  ARG A NE  
5967  C CZ  . ARG A 850  ? 0.3037 0.2421 0.3122 -0.0054 -0.0014 0.0071  848  ARG A CZ  
5968  N NH1 . ARG A 850  ? 0.2470 0.1836 0.2562 -0.0054 -0.0015 0.0086  848  ARG A NH1 
5969  N NH2 . ARG A 850  ? 0.2387 0.1772 0.2464 -0.0032 -0.0016 0.0040  848  ARG A NH2 
5970  N N   . VAL A 851  ? 0.2257 0.1804 0.2340 -0.0175 0.0031  0.0219  849  VAL A N   
5971  C CA  . VAL A 851  ? 0.2596 0.2179 0.2686 -0.0202 0.0034  0.0249  849  VAL A CA  
5972  C C   . VAL A 851  ? 0.2366 0.1988 0.2429 -0.0194 0.0054  0.0250  849  VAL A C   
5973  O O   . VAL A 851  ? 0.2315 0.1965 0.2364 -0.0182 0.0066  0.0232  849  VAL A O   
5974  C CB  . VAL A 851  ? 0.2542 0.2157 0.2650 -0.0225 0.0030  0.0253  849  VAL A CB  
5975  C CG1 . VAL A 851  ? 0.2690 0.2344 0.2804 -0.0254 0.0033  0.0287  849  VAL A CG1 
5976  C CG2 . VAL A 851  ? 0.3107 0.2682 0.3243 -0.0233 0.0008  0.0247  849  VAL A CG2 
5977  N N   . LEU A 852  ? 0.2450 0.2074 0.2508 -0.0200 0.0057  0.0272  850  LEU A N   
5978  C CA  . LEU A 852  ? 0.2320 0.1983 0.2356 -0.0194 0.0073  0.0274  850  LEU A CA  
5979  C C   . LEU A 852  ? 0.2370 0.2086 0.2412 -0.0220 0.0076  0.0298  850  LEU A C   
5980  O O   . LEU A 852  ? 0.2405 0.2117 0.2462 -0.0243 0.0066  0.0327  850  LEU A O   
5981  C CB  . LEU A 852  ? 0.2112 0.1750 0.2138 -0.0183 0.0074  0.0281  850  LEU A CB  
5982  C CG  . LEU A 852  ? 0.2324 0.2001 0.2331 -0.0179 0.0089  0.0283  850  LEU A CG  
5983  C CD1 . LEU A 852  ? 0.2114 0.1805 0.2104 -0.0157 0.0102  0.0255  850  LEU A CD1 
5984  C CD2 . LEU A 852  ? 0.2309 0.1960 0.2311 -0.0172 0.0086  0.0293  850  LEU A CD2 
5985  N N   . CYS A 853  ? 0.2147 0.1915 0.2177 -0.0217 0.0090  0.0286  851  CYS A N   
5986  C CA  . CYS A 853  ? 0.2412 0.2243 0.2446 -0.0240 0.0096  0.0305  851  CYS A CA  
5987  C C   . CYS A 853  ? 0.2396 0.2265 0.2408 -0.0231 0.0109  0.0305  851  CYS A C   
5988  O O   . CYS A 853  ? 0.2524 0.2404 0.2521 -0.0209 0.0119  0.0278  851  CYS A O   
5989  C CB  . CYS A 853  ? 0.2286 0.2155 0.2327 -0.0242 0.0100  0.0289  851  CYS A CB  
5990  S SG  . CYS A 853  ? 0.2706 0.2529 0.2770 -0.0245 0.0084  0.0278  851  CYS A SG  
5991  N N   . LEU A 854  ? 0.2376 0.2263 0.2388 -0.0249 0.0107  0.0334  852  LEU A N   
5992  C CA  . LEU A 854  ? 0.2109 0.2026 0.2100 -0.0242 0.0116  0.0336  852  LEU A CA  
5993  C C   . LEU A 854  ? 0.2447 0.2445 0.2435 -0.0260 0.0124  0.0348  852  LEU A C   
5994  O O   . LEU A 854  ? 0.2348 0.2368 0.2349 -0.0288 0.0119  0.0380  852  LEU A O   
5995  C CB  . LEU A 854  ? 0.2472 0.2353 0.2463 -0.0246 0.0107  0.0359  852  LEU A CB  
5996  C CG  . LEU A 854  ? 0.2787 0.2596 0.2779 -0.0225 0.0100  0.0345  852  LEU A CG  
5997  C CD1 . LEU A 854  ? 0.2275 0.2053 0.2268 -0.0228 0.0090  0.0368  852  LEU A CD1 
5998  C CD2 . LEU A 854  ? 0.2403 0.2212 0.2378 -0.0197 0.0112  0.0311  852  LEU A CD2 
5999  N N   . GLN A 855  ? 0.2390 0.2435 0.2363 -0.0244 0.0137  0.0325  853  GLN A N   
6000  C CA  . GLN A 855  ? 0.2334 0.2464 0.2303 -0.0259 0.0146  0.0334  853  GLN A CA  
6001  C C   . GLN A 855  ? 0.2440 0.2585 0.2403 -0.0278 0.0142  0.0371  853  GLN A C   
6002  O O   . GLN A 855  ? 0.2625 0.2736 0.2577 -0.0267 0.0139  0.0372  853  GLN A O   
6003  C CB  . GLN A 855  ? 0.2361 0.2534 0.2315 -0.0235 0.0158  0.0299  853  GLN A CB  
6004  C CG  . GLN A 855  ? 0.2462 0.2732 0.2414 -0.0248 0.0167  0.0303  853  GLN A CG  
6005  C CD  . GLN A 855  ? 0.2536 0.2849 0.2474 -0.0222 0.0176  0.0265  853  GLN A CD  
6006  O OE1 . GLN A 855  ? 0.2942 0.3224 0.2881 -0.0197 0.0177  0.0233  853  GLN A OE1 
6007  N NE2 . GLN A 855  ? 0.2984 0.3371 0.2911 -0.0228 0.0183  0.0270  853  GLN A NE2 
6008  N N   . GLU A 856  ? 0.2543 0.2743 0.2513 -0.0308 0.0142  0.0401  854  GLU A N   
6009  C CA  . GLU A 856  ? 0.3043 0.3252 0.3010 -0.0331 0.0135  0.0444  854  GLU A CA  
6010  C C   . GLU A 856  ? 0.2858 0.3085 0.2800 -0.0317 0.0139  0.0440  854  GLU A C   
6011  O O   . GLU A 856  ? 0.3230 0.3420 0.3170 -0.0321 0.0129  0.0464  854  GLU A O   
6012  C CB  . GLU A 856  ? 0.3002 0.3287 0.2977 -0.0365 0.0139  0.0475  854  GLU A CB  
6013  C CG  . GLU A 856  ? 0.3615 0.3923 0.3585 -0.0391 0.0132  0.0525  854  GLU A CG  
6014  C CD  . GLU A 856  ? 0.3970 0.4191 0.3955 -0.0401 0.0112  0.0555  854  GLU A CD  
6015  O OE1 . GLU A 856  ? 0.3949 0.4112 0.3957 -0.0404 0.0103  0.0550  854  GLU A OE1 
6016  O OE2 . GLU A 856  ? 0.4474 0.4684 0.4448 -0.0406 0.0105  0.0581  854  GLU A OE2 
6017  N N   . ASP A 857  ? 0.3032 0.3314 0.2959 -0.0298 0.0153  0.0408  855  ASP A N   
6018  C CA  . ASP A 857  ? 0.3045 0.3357 0.2950 -0.0286 0.0156  0.0403  855  ASP A CA  
6019  C C   . ASP A 857  ? 0.3316 0.3551 0.3217 -0.0266 0.0148  0.0392  855  ASP A C   
6020  O O   . ASP A 857  ? 0.3350 0.3593 0.3237 -0.0264 0.0146  0.0401  855  ASP A O   
6021  C CB  . ASP A 857  ? 0.3498 0.3879 0.3391 -0.0268 0.0169  0.0364  855  ASP A CB  
6022  N N   . VAL A 858  ? 0.2585 0.2749 0.2497 -0.0251 0.0145  0.0372  856  VAL A N   
6023  C CA  . VAL A 858  ? 0.2755 0.2850 0.2665 -0.0232 0.0139  0.0361  856  VAL A CA  
6024  C C   . VAL A 858  ? 0.2810 0.2834 0.2737 -0.0240 0.0126  0.0383  856  VAL A C   
6025  O O   . VAL A 858  ? 0.2857 0.2823 0.2784 -0.0224 0.0121  0.0375  856  VAL A O   
6026  C CB  . VAL A 858  ? 0.3104 0.3177 0.3012 -0.0203 0.0146  0.0317  856  VAL A CB  
6027  C CG1 . VAL A 858  ? 0.3481 0.3617 0.3374 -0.0191 0.0155  0.0292  856  VAL A CG1 
6028  C CG2 . VAL A 858  ? 0.3027 0.3081 0.2948 -0.0202 0.0147  0.0305  856  VAL A CG2 
6029  N N   . ALA A 859  ? 0.2638 0.2663 0.2579 -0.0264 0.0120  0.0411  857  ALA A N   
6030  C CA  . ALA A 859  ? 0.2769 0.2723 0.2729 -0.0269 0.0105  0.0425  857  ALA A CA  
6031  C C   . ALA A 859  ? 0.3204 0.3117 0.3164 -0.0269 0.0093  0.0446  857  ALA A C   
6032  O O   . ALA A 859  ? 0.3078 0.2927 0.3048 -0.0255 0.0085  0.0437  857  ALA A O   
6033  C CB  . ALA A 859  ? 0.2711 0.2680 0.2690 -0.0299 0.0099  0.0452  857  ALA A CB  
6034  N N   . ASP A 860  ? 0.2872 0.2826 0.2822 -0.0283 0.0091  0.0475  858  ASP A N   
6035  C CA  . ASP A 860  ? 0.3449 0.3366 0.3401 -0.0283 0.0077  0.0499  858  ASP A CA  
6036  C C   . ASP A 860  ? 0.2639 0.2527 0.2582 -0.0254 0.0080  0.0470  858  ASP A C   
6037  O O   . ASP A 860  ? 0.3140 0.2970 0.3094 -0.0244 0.0068  0.0472  858  ASP A O   
6038  C CB  . ASP A 860  ? 0.3393 0.3367 0.3333 -0.0304 0.0074  0.0537  858  ASP A CB  
6039  C CG  . ASP A 860  ? 0.4404 0.4392 0.4359 -0.0337 0.0066  0.0577  858  ASP A CG  
6040  O OD1 . ASP A 860  ? 0.4459 0.4388 0.4438 -0.0344 0.0053  0.0586  858  ASP A OD1 
6041  O OD2 . ASP A 860  ? 0.5014 0.5075 0.4957 -0.0357 0.0072  0.0600  858  ASP A OD2 
6042  N N   . ARG A 861  ? 0.2818 0.2748 0.2744 -0.0240 0.0094  0.0442  859  ARG A N   
6043  C CA  . ARG A 861  ? 0.3047 0.2952 0.2965 -0.0214 0.0097  0.0415  859  ARG A CA  
6044  C C   . ARG A 861  ? 0.2856 0.2698 0.2787 -0.0198 0.0097  0.0391  859  ARG A C   
6045  O O   . ARG A 861  ? 0.2690 0.2490 0.2627 -0.0184 0.0091  0.0385  859  ARG A O   
6046  C CB  . ARG A 861  ? 0.3185 0.3146 0.3086 -0.0204 0.0111  0.0387  859  ARG A CB  
6047  C CG  . ARG A 861  ? 0.4017 0.3951 0.3915 -0.0180 0.0114  0.0358  859  ARG A CG  
6048  C CD  . ARG A 861  ? 0.5452 0.5440 0.5333 -0.0171 0.0122  0.0336  859  ARG A CD  
6049  N NE  . ARG A 861  ? 0.6360 0.6318 0.6242 -0.0151 0.0122  0.0312  859  ARG A NE  
6050  C CZ  . ARG A 861  ? 0.5610 0.5549 0.5495 -0.0135 0.0129  0.0280  859  ARG A CZ  
6051  N NH1 . ARG A 861  ? 0.5935 0.5885 0.5821 -0.0134 0.0136  0.0265  859  ARG A NH1 
6052  N NH2 . ARG A 861  ? 0.5668 0.5579 0.5556 -0.0121 0.0128  0.0263  859  ARG A NH2 
6053  N N   . ILE A 862  ? 0.2439 0.2280 0.2375 -0.0198 0.0103  0.0375  860  ILE A N   
6054  C CA  . ILE A 862  ? 0.2428 0.2216 0.2373 -0.0182 0.0103  0.0353  860  ILE A CA  
6055  C C   . ILE A 862  ? 0.2668 0.2402 0.2631 -0.0187 0.0087  0.0370  860  ILE A C   
6056  O O   . ILE A 862  ? 0.2639 0.2327 0.2609 -0.0170 0.0084  0.0357  860  ILE A O   
6057  C CB  . ILE A 862  ? 0.2685 0.2489 0.2630 -0.0180 0.0112  0.0333  860  ILE A CB  
6058  C CG1 . ILE A 862  ? 0.2989 0.2836 0.2919 -0.0168 0.0125  0.0308  860  ILE A CG1 
6059  C CG2 . ILE A 862  ? 0.2567 0.2318 0.2521 -0.0167 0.0109  0.0314  860  ILE A CG2 
6060  C CD1 . ILE A 862  ? 0.3290 0.3170 0.3220 -0.0169 0.0132  0.0292  860  ILE A CD1 
6061  N N   . LEU A 863  ? 0.2557 0.2297 0.2531 -0.0209 0.0077  0.0401  861  LEU A N   
6062  C CA  . LEU A 863  ? 0.2627 0.2313 0.2622 -0.0214 0.0059  0.0418  861  LEU A CA  
6063  C C   . LEU A 863  ? 0.2621 0.2280 0.2617 -0.0203 0.0050  0.0425  861  LEU A C   
6064  O O   . LEU A 863  ? 0.2467 0.2074 0.2476 -0.0190 0.0040  0.0417  861  LEU A O   
6065  C CB  . LEU A 863  ? 0.2499 0.2200 0.2506 -0.0245 0.0048  0.0454  861  LEU A CB  
6066  C CG  . LEU A 863  ? 0.4255 0.3908 0.4289 -0.0257 0.0030  0.0467  861  LEU A CG  
6067  C CD1 . LEU A 863  ? 0.3298 0.2908 0.3341 -0.0237 0.0030  0.0432  861  LEU A CD1 
6068  C CD2 . LEU A 863  ? 0.4088 0.3781 0.4128 -0.0287 0.0030  0.0491  861  LEU A CD2 
6069  N N   . THR A 864  ? 0.2531 0.2228 0.2512 -0.0207 0.0053  0.0440  862  THR A N   
6070  C CA  . THR A 864  ? 0.2471 0.2148 0.2454 -0.0196 0.0044  0.0447  862  THR A CA  
6071  C C   . THR A 864  ? 0.2496 0.2147 0.2478 -0.0169 0.0051  0.0412  862  THR A C   
6072  O O   . THR A 864  ? 0.2557 0.2166 0.2552 -0.0156 0.0041  0.0409  862  THR A O   
6073  C CB  . THR A 864  ? 0.2635 0.2366 0.2600 -0.0204 0.0047  0.0465  862  THR A CB  
6074  O OG1 . THR A 864  ? 0.2857 0.2610 0.2824 -0.0231 0.0038  0.0504  862  THR A OG1 
6075  C CG2 . THR A 864  ? 0.2913 0.2629 0.2878 -0.0190 0.0038  0.0468  862  THR A CG2 
6076  N N   . MET A 865  ? 0.2507 0.2183 0.2475 -0.0160 0.0068  0.0385  863  MET A N   
6077  C CA  A MET A 865  ? 0.2538 0.2192 0.2505 -0.0138 0.0076  0.0354  863  MET A CA  
6078  C CA  B MET A 865  ? 0.2538 0.2192 0.2505 -0.0138 0.0076  0.0354  863  MET A CA  
6079  C C   . MET A 865  ? 0.2424 0.2031 0.2405 -0.0129 0.0072  0.0341  863  MET A C   
6080  O O   . MET A 865  ? 0.2373 0.1952 0.2361 -0.0112 0.0071  0.0327  863  MET A O   
6081  C CB  A MET A 865  ? 0.2600 0.2290 0.2551 -0.0133 0.0093  0.0331  863  MET A CB  
6082  C CB  B MET A 865  ? 0.2594 0.2282 0.2545 -0.0132 0.0093  0.0331  863  MET A CB  
6083  C CG  A MET A 865  ? 0.2779 0.2453 0.2727 -0.0113 0.0101  0.0305  863  MET A CG  
6084  C CG  B MET A 865  ? 0.2962 0.2693 0.2900 -0.0133 0.0097  0.0332  863  MET A CG  
6085  S SD  A MET A 865  ? 0.3473 0.3184 0.3406 -0.0108 0.0116  0.0280  863  MET A SD  
6086  S SD  B MET A 865  ? 0.3499 0.3267 0.3423 -0.0127 0.0113  0.0303  863  MET A SD  
6087  C CE  A MET A 865  ? 0.3228 0.2987 0.3151 -0.0114 0.0115  0.0288  863  MET A CE  
6088  C CE  B MET A 865  ? 0.3410 0.3130 0.3340 -0.0108 0.0119  0.0276  863  MET A CE  
6089  N N   . LEU A 866  ? 0.2525 0.2129 0.2512 -0.0139 0.0070  0.0344  864  LEU A N   
6090  C CA  A LEU A 866  ? 0.2461 0.2023 0.2460 -0.0131 0.0065  0.0330  864  LEU A CA  
6091  C CA  B LEU A 866  ? 0.2474 0.2036 0.2474 -0.0131 0.0065  0.0330  864  LEU A CA  
6092  C C   . LEU A 866  ? 0.2198 0.1717 0.2217 -0.0127 0.0047  0.0340  864  LEU A C   
6093  O O   . LEU A 866  ? 0.2438 0.1926 0.2465 -0.0109 0.0044  0.0321  864  LEU A O   
6094  C CB  A LEU A 866  ? 0.2689 0.2259 0.2692 -0.0145 0.0065  0.0332  864  LEU A CB  
6095  C CB  B LEU A 866  ? 0.2684 0.2253 0.2688 -0.0146 0.0064  0.0333  864  LEU A CB  
6096  C CG  A LEU A 866  ? 0.2637 0.2169 0.2654 -0.0138 0.0058  0.0316  864  LEU A CG  
6097  C CG  B LEU A 866  ? 0.2519 0.2108 0.2511 -0.0140 0.0079  0.0309  864  LEU A CG  
6098  C CD1 A LEU A 866  ? 0.2567 0.2095 0.2572 -0.0116 0.0071  0.0285  864  LEU A CD1 
6099  C CD1 B LEU A 866  ? 0.2643 0.2235 0.2646 -0.0156 0.0073  0.0316  864  LEU A CD1 
6100  C CD2 A LEU A 866  ? 0.2618 0.2164 0.2642 -0.0157 0.0055  0.0323  864  LEU A CD2 
6101  C CD2 B LEU A 866  ? 0.2478 0.2039 0.2468 -0.0117 0.0083  0.0282  864  LEU A CD2 
6102  N N   . LYS A 867  ? 0.2350 0.1869 0.2377 -0.0144 0.0033  0.0372  865  LYS A N   
6103  C CA  . LYS A 867  ? 0.2325 0.1802 0.2374 -0.0139 0.0012  0.0382  865  LYS A CA  
6104  C C   . LYS A 867  ? 0.2667 0.2139 0.2714 -0.0117 0.0014  0.0370  865  LYS A C   
6105  O O   . LYS A 867  ? 0.2575 0.2012 0.2638 -0.0100 0.0004  0.0358  865  LYS A O   
6106  C CB  . LYS A 867  ? 0.2593 0.2073 0.2651 -0.0162 -0.0004 0.0423  865  LYS A CB  
6107  C CG  . LYS A 867  ? 0.2685 0.2170 0.2750 -0.0186 -0.0008 0.0437  865  LYS A CG  
6108  C CD  . LYS A 867  ? 0.3322 0.2817 0.3393 -0.0212 -0.0022 0.0483  865  LYS A CD  
6109  C CE  . LYS A 867  ? 0.3783 0.3289 0.3863 -0.0239 -0.0025 0.0498  865  LYS A CE  
6110  N NZ  . LYS A 867  ? 0.3982 0.3508 0.4066 -0.0269 -0.0036 0.0546  865  LYS A NZ  
6111  N N   . GLY A 868  ? 0.2399 0.1909 0.2428 -0.0117 0.0027  0.0372  866  GLY A N   
6112  C CA  . GLY A 868  ? 0.2398 0.1908 0.2427 -0.0099 0.0029  0.0360  866  GLY A CA  
6113  C C   . GLY A 868  ? 0.2643 0.2138 0.2673 -0.0078 0.0040  0.0327  866  GLY A C   
6114  O O   . GLY A 868  ? 0.2597 0.2073 0.2639 -0.0061 0.0035  0.0317  866  GLY A O   
6115  N N   . ALA A 869  ? 0.2333 0.1839 0.2351 -0.0080 0.0054  0.0311  867  ALA A N   
6116  C CA  . ALA A 869  ? 0.2526 0.2021 0.2543 -0.0062 0.0065  0.0283  867  ALA A CA  
6117  C C   . ALA A 869  ? 0.2504 0.1962 0.2538 -0.0052 0.0053  0.0273  867  ALA A C   
6118  O O   . ALA A 869  ? 0.2364 0.1811 0.2402 -0.0034 0.0056  0.0253  867  ALA A O   
6119  C CB  . ALA A 869  ? 0.2353 0.1869 0.2353 -0.0066 0.0080  0.0270  867  ALA A CB  
6120  N N   . LEU A 870  ? 0.2362 0.1802 0.2406 -0.0065 0.0039  0.0286  868  LEU A N   
6121  C CA  . LEU A 870  ? 0.2485 0.1888 0.2549 -0.0056 0.0024  0.0276  868  LEU A CA  
6122  C C   . LEU A 870  ? 0.2443 0.1825 0.2523 -0.0038 0.0013  0.0271  868  LEU A C   
6123  O O   . LEU A 870  ? 0.2411 0.1776 0.2501 -0.0019 0.0010  0.0247  868  LEU A O   
6124  C CB  . LEU A 870  ? 0.2197 0.1583 0.2275 -0.0077 0.0007  0.0297  868  LEU A CB  
6125  C CG  . LEU A 870  ? 0.2676 0.2020 0.2778 -0.0071 -0.0012 0.0286  868  LEU A CG  
6126  C CD1 . LEU A 870  ? 0.3112 0.2462 0.3204 -0.0070 -0.0002 0.0263  868  LEU A CD1 
6127  C CD2 . LEU A 870  ? 0.3023 0.2343 0.3145 -0.0092 -0.0035 0.0315  868  LEU A CD2 
6128  N N   . HIS A 871  ? 0.2263 0.1651 0.2348 -0.0043 0.0005  0.0293  869  HIS A N   
6129  C CA  . HIS A 871  ? 0.2310 0.1679 0.2414 -0.0026 -0.0009 0.0290  869  HIS A CA  
6130  C C   . HIS A 871  ? 0.2469 0.1859 0.2567 -0.0006 0.0006  0.0268  869  HIS A C   
6131  O O   . HIS A 871  ? 0.2928 0.2309 0.3044 0.0010  -0.0004 0.0262  869  HIS A O   
6132  C CB  . HIS A 871  ? 0.2609 0.1978 0.2719 -0.0039 -0.0024 0.0324  869  HIS A CB  
6133  C CG  . HIS A 871  ? 0.2634 0.1976 0.2758 -0.0057 -0.0044 0.0348  869  HIS A CG  
6134  N ND1 . HIS A 871  ? 0.3091 0.2386 0.3243 -0.0048 -0.0067 0.0343  869  HIS A ND1 
6135  C CD2 . HIS A 871  ? 0.3015 0.2369 0.3129 -0.0084 -0.0045 0.0375  869  HIS A CD2 
6136  C CE1 . HIS A 871  ? 0.3423 0.2700 0.3584 -0.0071 -0.0082 0.0369  869  HIS A CE1 
6137  N NE2 . HIS A 871  ? 0.3314 0.2629 0.3452 -0.0093 -0.0068 0.0390  869  HIS A NE2 
6138  N N   . GLU A 872  ? 0.2324 0.1742 0.2402 -0.0008 0.0029  0.0257  870  GLU A N   
6139  C CA  . GLU A 872  ? 0.2571 0.2008 0.2645 0.0008  0.0043  0.0237  870  GLU A CA  
6140  C C   . GLU A 872  ? 0.2591 0.2020 0.2666 0.0024  0.0049  0.0210  870  GLU A C   
6141  O O   . GLU A 872  ? 0.2465 0.1912 0.2537 0.0037  0.0062  0.0194  870  GLU A O   
6142  C CB  . GLU A 872  ? 0.2322 0.1792 0.2375 -0.0002 0.0062  0.0240  870  GLU A CB  
6143  C CG  . GLU A 872  ? 0.2556 0.2042 0.2606 -0.0015 0.0056  0.0264  870  GLU A CG  
6144  C CD  . GLU A 872  ? 0.3028 0.2514 0.3094 -0.0003 0.0046  0.0267  870  GLU A CD  
6145  O OE1 . GLU A 872  ? 0.3023 0.2510 0.3101 0.0014  0.0050  0.0249  870  GLU A OE1 
6146  O OE2 . GLU A 872  ? 0.2952 0.2444 0.3021 -0.0012 0.0035  0.0289  870  GLU A OE2 
6147  N N   . LEU A 873  ? 0.2549 0.1954 0.2629 0.0023  0.0040  0.0204  871  LEU A N   
6148  C CA  . LEU A 873  ? 0.2404 0.1806 0.2483 0.0039  0.0045  0.0177  871  LEU A CA  
6149  C C   . LEU A 873  ? 0.2473 0.1861 0.2575 0.0061  0.0032  0.0159  871  LEU A C   
6150  O O   . LEU A 873  ? 0.2456 0.1819 0.2579 0.0063  0.0010  0.0167  871  LEU A O   
6151  C CB  . LEU A 873  ? 0.2158 0.1543 0.2234 0.0029  0.0039  0.0175  871  LEU A CB  
6152  C CG  . LEU A 873  ? 0.2186 0.1589 0.2241 0.0009  0.0052  0.0189  871  LEU A CG  
6153  C CD1 . LEU A 873  ? 0.2487 0.1874 0.2544 -0.0003 0.0043  0.0190  871  LEU A CD1 
6154  C CD2 . LEU A 873  ? 0.2941 0.2371 0.2975 0.0015  0.0074  0.0178  871  LEU A CD2 
6155  N N   . HIS A 874  ? 0.2701 0.2107 0.2799 0.0079  0.0044  0.0135  872  HIS A N   
6156  C CA  . HIS A 874  ? 0.2812 0.2215 0.2930 0.0104  0.0034  0.0111  872  HIS A CA  
6157  C C   . HIS A 874  ? 0.2392 0.1780 0.2512 0.0114  0.0027  0.0087  872  HIS A C   
6158  O O   . HIS A 874  ? 0.2309 0.1717 0.2408 0.0115  0.0043  0.0076  872  HIS A O   
6159  C CB  . HIS A 874  ? 0.2680 0.2122 0.2793 0.0117  0.0052  0.0101  872  HIS A CB  
6160  C CG  . HIS A 874  ? 0.3015 0.2466 0.3149 0.0144  0.0045  0.0074  872  HIS A CG  
6161  N ND1 . HIS A 874  ? 0.3113 0.2604 0.3249 0.0157  0.0060  0.0065  872  HIS A ND1 
6162  C CD2 . HIS A 874  ? 0.3919 0.3347 0.4075 0.0162  0.0024  0.0054  872  HIS A CD2 
6163  C CE1 . HIS A 874  ? 0.3585 0.3081 0.3742 0.0182  0.0050  0.0039  872  HIS A CE1 
6164  N NE2 . HIS A 874  ? 0.3439 0.2895 0.3609 0.0187  0.0027  0.0031  872  HIS A NE2 
6165  N N   . ILE A 875  ? 0.2493 0.1847 0.2637 0.0122  0.0002  0.0079  873  ILE A N   
6166  C CA  . ILE A 875  ? 0.2654 0.1991 0.2805 0.0133  -0.0010 0.0053  873  ILE A CA  
6167  C C   . ILE A 875  ? 0.2642 0.1985 0.2812 0.0164  -0.0018 0.0020  873  ILE A C   
6168  O O   . ILE A 875  ? 0.3085 0.2417 0.3279 0.0174  -0.0032 0.0022  873  ILE A O   
6169  C CB  . ILE A 875  ? 0.3051 0.2342 0.3220 0.0117  -0.0035 0.0066  873  ILE A CB  
6170  C CG1 . ILE A 875  ? 0.3382 0.2675 0.3530 0.0088  -0.0025 0.0090  873  ILE A CG1 
6171  C CG2 . ILE A 875  ? 0.3029 0.2297 0.3216 0.0133  -0.0053 0.0033  873  ILE A CG2 
6172  C CD1 . ILE A 875  ? 0.3060 0.2374 0.3192 0.0069  -0.0009 0.0121  873  ILE A CD1 
6173  N N   . GLY A 876  ? 0.2695 0.2061 0.2856 0.0181  -0.0009 -0.0011 874  GLY A N   
6174  C CA  . GLY A 876  ? 0.2595 0.1974 0.2774 0.0213  -0.0017 -0.0047 874  GLY A CA  
6175  C C   . GLY A 876  ? 0.2920 0.2334 0.3079 0.0227  -0.0003 -0.0077 874  GLY A C   
6176  O O   . GLY A 876  ? 0.2594 0.2015 0.2727 0.0212  0.0010  -0.0069 874  GLY A O   
6177  N N   . ARG A 877  ? 0.2873 0.2311 0.3046 0.0257  -0.0007 -0.0111 875  ARG A N   
6178  C CA  . ARG A 877  ? 0.2870 0.2352 0.3022 0.0274  0.0008  -0.0140 875  ARG A CA  
6179  C C   . ARG A 877  ? 0.2364 0.1891 0.2483 0.0260  0.0041  -0.0118 875  ARG A C   
6180  O O   . ARG A 877  ? 0.2460 0.2003 0.2579 0.0253  0.0054  -0.0097 875  ARG A O   
6181  C CB  . ARG A 877  ? 0.2800 0.2310 0.2973 0.0309  0.0001  -0.0180 875  ARG A CB  
6182  C CG  . ARG A 877  ? 0.3141 0.2689 0.3299 0.0329  0.0007  -0.0217 875  ARG A CG  
6183  C CD  . ARG A 877  ? 0.3315 0.2893 0.3495 0.0366  -0.0003 -0.0261 875  ARG A CD  
6184  N NE  . ARG A 877  ? 0.3143 0.2782 0.3318 0.0375  0.0021  -0.0257 875  ARG A NE  
6185  C CZ  . ARG A 877  ? 0.4278 0.3959 0.4472 0.0407  0.0018  -0.0292 875  ARG A CZ  
6186  N NH1 . ARG A 877  ? 0.3868 0.3531 0.4089 0.0435  -0.0009 -0.0334 875  ARG A NH1 
6187  N NH2 . ARG A 877  ? 0.4002 0.3745 0.4189 0.0411  0.0043  -0.0286 875  ARG A NH2 
6188  N N   . THR A 878  ? 0.2586 0.2130 0.2676 0.0255  0.0054  -0.0122 876  THR A N   
6189  C CA  . THR A 878  ? 0.2656 0.2226 0.2716 0.0235  0.0080  -0.0094 876  THR A CA  
6190  C C   . THR A 878  ? 0.2614 0.2244 0.2658 0.0247  0.0104  -0.0099 876  THR A C   
6191  O O   . THR A 878  ? 0.2715 0.2368 0.2734 0.0232  0.0125  -0.0077 876  THR A O   
6192  C CB  . THR A 878  ? 0.2491 0.2049 0.2527 0.0223  0.0081  -0.0090 876  THR A CB  
6193  O OG1 . THR A 878  ? 0.2657 0.2228 0.2691 0.0244  0.0073  -0.0126 876  THR A OG1 
6194  C CG2 . THR A 878  ? 0.2817 0.2322 0.2865 0.0202  0.0064  -0.0072 876  THR A CG2 
6195  N N   . ASP A 879  ? 0.2425 0.2085 0.2487 0.0272  0.0101  -0.0126 877  ASP A N   
6196  C CA  . ASP A 879  ? 0.2838 0.2563 0.2889 0.0280  0.0125  -0.0128 877  ASP A CA  
6197  C C   . ASP A 879  ? 0.2781 0.2513 0.2844 0.0269  0.0134  -0.0102 877  ASP A C   
6198  O O   . ASP A 879  ? 0.2792 0.2573 0.2863 0.0281  0.0145  -0.0110 877  ASP A O   
6199  C CB  . ASP A 879  ? 0.2910 0.2676 0.2972 0.0314  0.0120  -0.0171 877  ASP A CB  
6200  C CG  . ASP A 879  ? 0.3319 0.3063 0.3421 0.0333  0.0097  -0.0191 877  ASP A CG  
6201  O OD1 . ASP A 879  ? 0.3425 0.3108 0.3544 0.0322  0.0077  -0.0180 877  ASP A OD1 
6202  O OD2 . ASP A 879  ? 0.3171 0.2962 0.3287 0.0358  0.0100  -0.0218 877  ASP A OD2 
6203  N N   . ARG A 880  ? 0.2817 0.2505 0.2882 0.0245  0.0129  -0.0073 878  ARG A N   
6204  C CA  . ARG A 880  ? 0.2779 0.2473 0.2853 0.0230  0.0137  -0.0046 878  ARG A CA  
6205  C C   . ARG A 880  ? 0.2584 0.2256 0.2636 0.0201  0.0147  -0.0013 878  ARG A C   
6206  O O   . ARG A 880  ? 0.2525 0.2156 0.2571 0.0191  0.0136  -0.0007 878  ARG A O   
6207  C CB  . ARG A 880  ? 0.3319 0.2978 0.3425 0.0235  0.0116  -0.0046 878  ARG A CB  
6208  C CG  . ARG A 880  ? 0.4069 0.3756 0.4203 0.0262  0.0108  -0.0073 878  ARG A CG  
6209  C CD  . ARG A 880  ? 0.4075 0.3720 0.4239 0.0264  0.0084  -0.0066 878  ARG A CD  
6210  N NE  . ARG A 880  ? 0.5944 0.5608 0.6138 0.0293  0.0072  -0.0093 878  ARG A NE  
6211  C CZ  . ARG A 880  ? 0.5821 0.5517 0.6032 0.0299  0.0077  -0.0090 878  ARG A CZ  
6212  N NH1 . ARG A 880  ? 0.6187 0.5900 0.6388 0.0276  0.0094  -0.0060 878  ARG A NH1 
6213  N NH2 . ARG A 880  ? 0.6003 0.5715 0.6245 0.0328  0.0063  -0.0118 878  ARG A NH2 
6214  N N   . LEU A 881  ? 0.2624 0.2326 0.2667 0.0188  0.0167  0.0006  879  LEU A N   
6215  C CA  . LEU A 881  ? 0.2313 0.1997 0.2338 0.0163  0.0175  0.0035  879  LEU A CA  
6216  C C   . LEU A 881  ? 0.2312 0.1952 0.2347 0.0149  0.0161  0.0050  879  LEU A C   
6217  O O   . LEU A 881  ? 0.2122 0.1737 0.2143 0.0132  0.0160  0.0066  879  LEU A O   
6218  C CB  . LEU A 881  ? 0.2102 0.1822 0.2121 0.0152  0.0196  0.0052  879  LEU A CB  
6219  C CG  . LEU A 881  ? 0.2380 0.2085 0.2383 0.0127  0.0204  0.0079  879  LEU A CG  
6220  C CD1 . LEU A 881  ? 0.2906 0.2601 0.2882 0.0125  0.0208  0.0080  879  LEU A CD1 
6221  C CD2 . LEU A 881  ? 0.2412 0.2153 0.2419 0.0118  0.0221  0.0094  879  LEU A CD2 
6222  N N   . SER A 882  ? 0.2459 0.2093 0.2520 0.0157  0.0148  0.0046  880  SER A N   
6223  C CA  . SER A 882  ? 0.2450 0.2047 0.2521 0.0144  0.0134  0.0063  880  SER A CA  
6224  C C   . SER A 882  ? 0.2713 0.2268 0.2783 0.0142  0.0116  0.0060  880  SER A C   
6225  O O   . SER A 882  ? 0.2737 0.2264 0.2811 0.0127  0.0105  0.0078  880  SER A O   
6226  C CB  . SER A 882  ? 0.2885 0.2489 0.2984 0.0155  0.0124  0.0060  880  SER A CB  
6227  O OG  . SER A 882  ? 0.2815 0.2416 0.2931 0.0179  0.0110  0.0034  880  SER A OG  
6228  N N   . VAL A 883  ? 0.2348 0.1900 0.2415 0.0155  0.0111  0.0039  881  VAL A N   
6229  C CA  . VAL A 883  ? 0.2489 0.2000 0.2560 0.0152  0.0092  0.0036  881  VAL A CA  
6230  C C   . VAL A 883  ? 0.2539 0.2040 0.2586 0.0131  0.0100  0.0052  881  VAL A C   
6231  O O   . VAL A 883  ? 0.2916 0.2440 0.2942 0.0131  0.0116  0.0049  881  VAL A O   
6232  C CB  . VAL A 883  ? 0.2657 0.2167 0.2736 0.0175  0.0081  0.0003  881  VAL A CB  
6233  C CG1 . VAL A 883  ? 0.2341 0.1811 0.2420 0.0166  0.0064  0.0001  881  VAL A CG1 
6234  C CG2 . VAL A 883  ? 0.2932 0.2440 0.3041 0.0196  0.0066  -0.0014 881  VAL A CG2 
6235  N N   . ASP A 884  ? 0.2200 0.1671 0.2252 0.0114  0.0088  0.0070  882  ASP A N   
6236  C CA  . ASP A 884  ? 0.2643 0.2107 0.2676 0.0095  0.0094  0.0084  882  ASP A CA  
6237  C C   . ASP A 884  ? 0.2737 0.2181 0.2770 0.0096  0.0082  0.0071  882  ASP A C   
6238  O O   . ASP A 884  ? 0.2930 0.2381 0.2944 0.0091  0.0090  0.0070  882  ASP A O   
6239  C CB  . ASP A 884  ? 0.2652 0.2103 0.2689 0.0075  0.0089  0.0110  882  ASP A CB  
6240  C CG  . ASP A 884  ? 0.2745 0.2216 0.2782 0.0073  0.0099  0.0122  882  ASP A CG  
6241  O OD1 . ASP A 884  ? 0.2997 0.2492 0.3019 0.0072  0.0117  0.0122  882  ASP A OD1 
6242  O OD2 . ASP A 884  ? 0.2727 0.2189 0.2780 0.0071  0.0088  0.0133  882  ASP A OD2 
6243  N N   . VAL A 885  ? 0.2325 0.1742 0.2381 0.0103  0.0060  0.0062  883  VAL A N   
6244  C CA  . VAL A 885  ? 0.2480 0.1873 0.2543 0.0101  0.0045  0.0050  883  VAL A CA  
6245  C C   . VAL A 885  ? 0.2535 0.1920 0.2618 0.0125  0.0030  0.0020  883  VAL A C   
6246  O O   . VAL A 885  ? 0.2487 0.1858 0.2592 0.0134  0.0017  0.0018  883  VAL A O   
6247  C CB  . VAL A 885  ? 0.3102 0.2465 0.3179 0.0078  0.0029  0.0074  883  VAL A CB  
6248  C CG1 . VAL A 885  ? 0.2583 0.1920 0.2671 0.0076  0.0011  0.0061  883  VAL A CG1 
6249  C CG2 . VAL A 885  ? 0.2823 0.2201 0.2880 0.0056  0.0045  0.0101  883  VAL A CG2 
6250  N N   . GLY A 886  ? 0.2483 0.1876 0.2557 0.0136  0.0030  -0.0006 884  GLY A N   
6251  C CA  . GLY A 886  ? 0.2528 0.1918 0.2619 0.0162  0.0015  -0.0041 884  GLY A CA  
6252  C C   . GLY A 886  ? 0.2415 0.1762 0.2532 0.0158  -0.0014 -0.0051 884  GLY A C   
6253  O O   . GLY A 886  ? 0.2510 0.1828 0.2635 0.0135  -0.0023 -0.0026 884  GLY A O   
6254  N N   . PRO A 887  ? 0.2434 0.1779 0.2563 0.0181  -0.0028 -0.0088 885  PRO A N   
6255  C CA  . PRO A 887  ? 0.2361 0.1661 0.2518 0.0180  -0.0058 -0.0102 885  PRO A CA  
6256  C C   . PRO A 887  ? 0.2432 0.1730 0.2576 0.0163  -0.0058 -0.0102 885  PRO A C   
6257  O O   . PRO A 887  ? 0.2358 0.1691 0.2470 0.0161  -0.0036 -0.0101 885  PRO A O   
6258  C CB  . PRO A 887  ? 0.2392 0.1701 0.2564 0.0214  -0.0070 -0.0148 885  PRO A CB  
6259  C CG  . PRO A 887  ? 0.2638 0.2007 0.2775 0.0228  -0.0041 -0.0160 885  PRO A CG  
6260  C CD  . PRO A 887  ? 0.2813 0.2200 0.2930 0.0210  -0.0016 -0.0121 885  PRO A CD  
6261  N N   . VAL A 888  ? 0.2428 0.1683 0.2600 0.0151  -0.0085 -0.0103 886  VAL A N   
6262  C CA  . VAL A 888  ? 0.2395 0.1649 0.2562 0.0143  -0.0091 -0.0116 886  VAL A CA  
6263  C C   . VAL A 888  ? 0.2423 0.1688 0.2596 0.0173  -0.0102 -0.0166 886  VAL A C   
6264  O O   . VAL A 888  ? 0.2721 0.1984 0.2908 0.0199  -0.0111 -0.0191 886  VAL A O   
6265  C CB  . VAL A 888  ? 0.2767 0.1978 0.2963 0.0114  -0.0113 -0.0095 886  VAL A CB  
6266  C CG1 . VAL A 888  ? 0.2866 0.2080 0.3051 0.0086  -0.0098 -0.0047 886  VAL A CG1 
6267  C CG2 . VAL A 888  ? 0.2591 0.1752 0.2829 0.0121  -0.0147 -0.0107 886  VAL A CG2 
6268  N N   . ILE A 889  ? 0.2549 0.1827 0.2708 0.0172  -0.0102 -0.0184 887  ILE A N   
6269  C CA  . ILE A 889  ? 0.2752 0.2062 0.2901 0.0202  -0.0103 -0.0229 887  ILE A CA  
6270  C C   . ILE A 889  ? 0.2775 0.2054 0.2961 0.0223  -0.0135 -0.0270 887  ILE A C   
6271  O O   . ILE A 889  ? 0.2989 0.2295 0.3172 0.0255  -0.0135 -0.0308 887  ILE A O   
6272  C CB  . ILE A 889  ? 0.2752 0.2088 0.2875 0.0195  -0.0095 -0.0235 887  ILE A CB  
6273  C CG1 . ILE A 889  ? 0.2884 0.2263 0.2987 0.0227  -0.0090 -0.0278 887  ILE A CG1 
6274  C CG2 . ILE A 889  ? 0.2451 0.1747 0.2601 0.0172  -0.0120 -0.0233 887  ILE A CG2 
6275  C CD1 . ILE A 889  ? 0.2889 0.2316 0.2960 0.0242  -0.0061 -0.0271 887  ILE A CD1 
6276  N N   . THR A 890  ? 0.2550 0.1774 0.2774 0.0206  -0.0164 -0.0264 888  THR A N   
6277  C CA  . THR A 890  ? 0.2728 0.1917 0.2992 0.0224  -0.0200 -0.0304 888  THR A CA  
6278  C C   . THR A 890  ? 0.2854 0.1979 0.3160 0.0205  -0.0226 -0.0278 888  THR A C   
6279  O O   . THR A 890  ? 0.2648 0.1758 0.2951 0.0173  -0.0218 -0.0230 888  THR A O   
6280  C CB  . THR A 890  ? 0.2815 0.2002 0.3085 0.0225  -0.0217 -0.0337 888  THR A CB  
6281  O OG1 . THR A 890  ? 0.2868 0.2033 0.3142 0.0186  -0.0220 -0.0302 888  THR A OG1 
6282  C CG2 . THR A 890  ? 0.3392 0.2643 0.3619 0.0246  -0.0195 -0.0365 888  THR A CG2 
6283  N N   . SER A 891  ? 0.3127 0.2212 0.3473 0.0224  -0.0260 -0.0312 889  SER A N   
6284  C CA  A SER A 891  ? 0.3234 0.2251 0.3625 0.0206  -0.0292 -0.0289 889  SER A CA  
6285  C CA  B SER A 891  ? 0.3233 0.2251 0.3624 0.0206  -0.0291 -0.0288 889  SER A CA  
6286  C C   . SER A 891  ? 0.3179 0.2167 0.3585 0.0167  -0.0305 -0.0265 889  SER A C   
6287  O O   . SER A 891  ? 0.3221 0.2172 0.3646 0.0137  -0.0314 -0.0220 889  SER A O   
6288  C CB  A SER A 891  ? 0.3242 0.2221 0.3677 0.0236  -0.0329 -0.0335 889  SER A CB  
6289  C CB  B SER A 891  ? 0.3243 0.2223 0.3677 0.0237  -0.0328 -0.0334 889  SER A CB  
6290  O OG  A SER A 891  ? 0.3458 0.2467 0.3885 0.0271  -0.0318 -0.0355 889  SER A OG  
6291  O OG  B SER A 891  ? 0.3460 0.2443 0.3904 0.0250  -0.0346 -0.0383 889  SER A OG  
6292  N N   . GLU A 892  ? 0.3179 0.2185 0.3576 0.0168  -0.0306 -0.0294 890  GLU A N   
6293  C CA  . GLU A 892  ? 0.3247 0.2231 0.3659 0.0131  -0.0318 -0.0273 890  GLU A CA  
6294  C C   . GLU A 892  ? 0.3110 0.2122 0.3491 0.0099  -0.0287 -0.0219 890  GLU A C   
6295  O O   . GLU A 892  ? 0.3024 0.2009 0.3425 0.0063  -0.0296 -0.0180 890  GLU A O   
6296  C CB  . GLU A 892  ? 0.3326 0.2332 0.3734 0.0141  -0.0326 -0.0318 890  GLU A CB  
6297  C CG  . GLU A 892  ? 0.4364 0.3361 0.4792 0.0181  -0.0351 -0.0382 890  GLU A CG  
6298  C CD  . GLU A 892  ? 0.4096 0.3155 0.4482 0.0220  -0.0323 -0.0411 890  GLU A CD  
6299  O OE1 . GLU A 892  ? 0.6404 0.5516 0.6751 0.0225  -0.0301 -0.0423 890  GLU A OE1 
6300  O OE2 . GLU A 892  ? 0.3446 0.2503 0.3838 0.0244  -0.0323 -0.0421 890  GLU A OE2 
6301  N N   . ALA A 893  ? 0.2893 0.1960 0.3227 0.0111  -0.0250 -0.0215 891  ALA A N   
6302  C CA  . ALA A 893  ? 0.2854 0.1948 0.3160 0.0084  -0.0221 -0.0167 891  ALA A CA  
6303  C C   . ALA A 893  ? 0.3220 0.2284 0.3542 0.0067  -0.0225 -0.0124 891  ALA A C   
6304  O O   . ALA A 893  ? 0.3205 0.2259 0.3532 0.0033  -0.0224 -0.0082 891  ALA A O   
6305  C CB  . ALA A 893  ? 0.2684 0.1837 0.2941 0.0104  -0.0185 -0.0172 891  ALA A CB  
6306  N N   . LYS A 894  ? 0.2654 0.1704 0.2985 0.0091  -0.0231 -0.0134 892  LYS A N   
6307  C CA  . LYS A 894  ? 0.3165 0.2184 0.3513 0.0078  -0.0238 -0.0095 892  LYS A CA  
6308  C C   . LYS A 894  ? 0.3460 0.2425 0.3850 0.0048  -0.0270 -0.0072 892  LYS A C   
6309  O O   . LYS A 894  ? 0.3288 0.2246 0.3678 0.0017  -0.0266 -0.0023 892  LYS A O   
6310  C CB  . LYS A 894  ? 0.2881 0.1891 0.3240 0.0113  -0.0246 -0.0120 892  LYS A CB  
6311  C CG  . LYS A 894  ? 0.3008 0.1983 0.3389 0.0104  -0.0259 -0.0084 892  LYS A CG  
6312  C CD  . LYS A 894  ? 0.3006 0.1982 0.3395 0.0142  -0.0263 -0.0110 892  LYS A CD  
6313  C CE  . LYS A 894  ? 0.3483 0.2421 0.3897 0.0134  -0.0280 -0.0075 892  LYS A CE  
6314  N NZ  . LYS A 894  ? 0.4525 0.3437 0.4972 0.0170  -0.0306 -0.0111 892  LYS A NZ  
6315  N N   . ASP A 895  ? 0.3212 0.2138 0.3638 0.0057  -0.0303 -0.0106 893  ASP A N   
6316  C CA  . ASP A 895  ? 0.3596 0.2466 0.4068 0.0027  -0.0338 -0.0084 893  ASP A CA  
6317  C C   . ASP A 895  ? 0.3369 0.2256 0.3832 -0.0015 -0.0327 -0.0048 893  ASP A C   
6318  O O   . ASP A 895  ? 0.3280 0.2142 0.3763 -0.0049 -0.0338 -0.0002 893  ASP A O   
6319  C CB  . ASP A 895  ? 0.3957 0.2785 0.4469 0.0045  -0.0375 -0.0133 893  ASP A CB  
6320  C CG  . ASP A 895  ? 0.5077 0.3875 0.5610 0.0082  -0.0396 -0.0163 893  ASP A CG  
6321  O OD1 . ASP A 895  ? 0.5857 0.4652 0.6386 0.0087  -0.0388 -0.0136 893  ASP A OD1 
6322  O OD2 . ASP A 895  ? 0.5659 0.4439 0.6216 0.0108  -0.0420 -0.0216 893  ASP A OD2 
6323  N N   . ASN A 896  ? 0.3117 0.2049 0.3553 -0.0013 -0.0307 -0.0069 894  ASN A N   
6324  C CA  . ASN A 896  ? 0.3098 0.2054 0.3525 -0.0049 -0.0295 -0.0039 894  ASN A CA  
6325  C C   . ASN A 896  ? 0.3506 0.2490 0.3908 -0.0071 -0.0269 0.0013  894  ASN A C   
6326  O O   . ASN A 896  ? 0.3178 0.2158 0.3594 -0.0108 -0.0272 0.0054  894  ASN A O   
6327  C CB  . ASN A 896  ? 0.3423 0.2427 0.3822 -0.0037 -0.0277 -0.0074 894  ASN A CB  
6328  C CG  . ASN A 896  ? 0.4837 0.3874 0.5225 -0.0071 -0.0263 -0.0046 894  ASN A CG  
6329  O OD1 . ASN A 896  ? 0.5354 0.4431 0.5710 -0.0080 -0.0233 -0.0016 894  ASN A OD1 
6330  N ND2 . ASN A 896  ? 0.4916 0.3939 0.5334 -0.0089 -0.0285 -0.0057 894  ASN A ND2 
6331  N N   . ILE A 897  ? 0.3111 0.2125 0.3477 -0.0048 -0.0242 0.0011  895  ILE A N   
6332  C CA  . ILE A 897  ? 0.2990 0.2033 0.3331 -0.0066 -0.0216 0.0056  895  ILE A CA  
6333  C C   . ILE A 897  ? 0.3305 0.2308 0.3674 -0.0084 -0.0236 0.0096  895  ILE A C   
6334  O O   . ILE A 897  ? 0.3018 0.2033 0.3385 -0.0117 -0.0229 0.0141  895  ILE A O   
6335  C CB  . ILE A 897  ? 0.2887 0.1967 0.3188 -0.0036 -0.0187 0.0043  895  ILE A CB  
6336  C CG1 . ILE A 897  ? 0.2913 0.2035 0.3185 -0.0022 -0.0167 0.0011  895  ILE A CG1 
6337  C CG2 . ILE A 897  ? 0.2717 0.1823 0.2997 -0.0053 -0.0165 0.0086  895  ILE A CG2 
6338  C CD1 . ILE A 897  ? 0.2840 0.1989 0.3082 0.0013  -0.0147 -0.0014 895  ILE A CD1 
6339  N N   . GLU A 898  ? 0.3057 0.2015 0.3451 -0.0064 -0.0260 0.0081  896  GLU A N   
6340  C CA  . GLU A 898  ? 0.3155 0.2075 0.3576 -0.0079 -0.0280 0.0119  896  GLU A CA  
6341  C C   . GLU A 898  ? 0.3336 0.2222 0.3792 -0.0118 -0.0306 0.0149  896  GLU A C   
6342  O O   . GLU A 898  ? 0.3474 0.2350 0.3939 -0.0145 -0.0312 0.0199  896  GLU A O   
6343  C CB  . GLU A 898  ? 0.3686 0.2566 0.4128 -0.0044 -0.0302 0.0092  896  GLU A CB  
6344  C CG  . GLU A 898  ? 0.3738 0.2657 0.4145 -0.0014 -0.0274 0.0078  896  GLU A CG  
6345  C CD  . GLU A 898  ? 0.4027 0.2917 0.4454 0.0023  -0.0292 0.0050  896  GLU A CD  
6346  O OE1 . GLU A 898  ? 0.4576 0.3421 0.5041 0.0034  -0.0325 0.0021  896  GLU A OE1 
6347  O OE2 . GLU A 898  ? 0.5183 0.4098 0.5591 0.0040  -0.0275 0.0054  896  GLU A OE2 
6348  N N   . LYS A 899  ? 0.3109 0.1979 0.3588 -0.0122 -0.0323 0.0121  897  LYS A N   
6349  C CA  . LYS A 899  ? 0.3333 0.2175 0.3848 -0.0162 -0.0347 0.0151  897  LYS A CA  
6350  C C   . LYS A 899  ? 0.3383 0.2277 0.3874 -0.0198 -0.0321 0.0195  897  LYS A C   
6351  O O   . LYS A 899  ? 0.3757 0.2639 0.4268 -0.0235 -0.0332 0.0244  897  LYS A O   
6352  C CB  . LYS A 899  ? 0.3330 0.2152 0.3872 -0.0159 -0.0369 0.0108  897  LYS A CB  
6353  N N   . HIS A 900  ? 0.3241 0.2195 0.3690 -0.0188 -0.0285 0.0180  898  HIS A N   
6354  C CA  . HIS A 900  ? 0.3417 0.2425 0.3842 -0.0218 -0.0259 0.0218  898  HIS A CA  
6355  C C   . HIS A 900  ? 0.3407 0.2422 0.3820 -0.0229 -0.0250 0.0265  898  HIS A C   
6356  O O   . HIS A 900  ? 0.3140 0.2169 0.3560 -0.0265 -0.0251 0.0311  898  HIS A O   
6357  C CB  . HIS A 900  ? 0.3372 0.2437 0.3754 -0.0200 -0.0225 0.0190  898  HIS A CB  
6358  C CG  . HIS A 900  ? 0.3423 0.2546 0.3779 -0.0223 -0.0198 0.0224  898  HIS A CG  
6359  N ND1 . HIS A 900  ? 0.3343 0.2491 0.3713 -0.0258 -0.0199 0.0243  898  HIS A ND1 
6360  C CD2 . HIS A 900  ? 0.3283 0.2446 0.3602 -0.0217 -0.0169 0.0240  898  HIS A CD2 
6361  C CE1 . HIS A 900  ? 0.3909 0.3111 0.4250 -0.0270 -0.0171 0.0268  898  HIS A CE1 
6362  N NE2 . HIS A 900  ? 0.3432 0.2643 0.3742 -0.0246 -0.0154 0.0266  898  HIS A NE2 
6363  N N   . ILE A 901  ? 0.3020 0.2029 0.3414 -0.0198 -0.0243 0.0253  899  ILE A N   
6364  C CA  . ILE A 901  ? 0.3224 0.2245 0.3604 -0.0206 -0.0234 0.0294  899  ILE A CA  
6365  C C   . ILE A 901  ? 0.3487 0.2463 0.3905 -0.0232 -0.0265 0.0336  899  ILE A C   
6366  O O   . ILE A 901  ? 0.3393 0.2390 0.3804 -0.0261 -0.0259 0.0385  899  ILE A O   
6367  C CB  . ILE A 901  ? 0.2915 0.1935 0.3276 -0.0166 -0.0223 0.0270  899  ILE A CB  
6368  C CG1 . ILE A 901  ? 0.3013 0.2081 0.3335 -0.0144 -0.0191 0.0236  899  ILE A CG1 
6369  C CG2 . ILE A 901  ? 0.3251 0.2280 0.3601 -0.0174 -0.0218 0.0311  899  ILE A CG2 
6370  C CD1 . ILE A 901  ? 0.2706 0.1772 0.3014 -0.0104 -0.0183 0.0204  899  ILE A CD1 
6371  N N   . GLU A 902  ? 0.3255 0.2167 0.3713 -0.0224 -0.0300 0.0318  900  GLU A N   
6372  C CA  . GLU A 902  ? 0.3831 0.2691 0.4328 -0.0249 -0.0334 0.0359  900  GLU A CA  
6373  C C   . GLU A 902  ? 0.3528 0.2399 0.4043 -0.0297 -0.0340 0.0396  900  GLU A C   
6374  O O   . GLU A 902  ? 0.3735 0.2598 0.4265 -0.0329 -0.0353 0.0450  900  GLU A O   
6375  C CB  . GLU A 902  ? 0.3820 0.2607 0.4359 -0.0225 -0.0373 0.0326  900  GLU A CB  
6376  C CG  . GLU A 902  ? 0.4259 0.3036 0.4786 -0.0181 -0.0370 0.0298  900  GLU A CG  
6377  C CD  . GLU A 902  ? 0.4746 0.3545 0.5250 -0.0185 -0.0356 0.0341  900  GLU A CD  
6378  O OE1 . GLU A 902  ? 0.4842 0.3614 0.5367 -0.0211 -0.0377 0.0390  900  GLU A OE1 
6379  O OE2 . GLU A 902  ? 0.4694 0.3539 0.5159 -0.0163 -0.0325 0.0327  900  GLU A OE2 
6380  N N   . ARG A 903  ? 0.3607 0.2501 0.4122 -0.0304 -0.0332 0.0370  901  ARG A N   
6381  C CA  . ARG A 903  ? 0.3669 0.2587 0.4200 -0.0350 -0.0334 0.0405  901  ARG A CA  
6382  C C   . ARG A 903  ? 0.4227 0.3212 0.4724 -0.0373 -0.0303 0.0450  901  ARG A C   
6383  O O   . ARG A 903  ? 0.3884 0.2875 0.4396 -0.0412 -0.0312 0.0503  901  ARG A O   
6384  C CB  . ARG A 903  ? 0.3827 0.2766 0.4361 -0.0349 -0.0328 0.0364  901  ARG A CB  
6385  N N   . MET A 904  ? 0.3909 0.2946 0.4359 -0.0349 -0.0268 0.0431  902  MET A N   
6386  C CA  . MET A 904  ? 0.3882 0.2983 0.4298 -0.0365 -0.0239 0.0467  902  MET A CA  
6387  C C   . MET A 904  ? 0.3895 0.2977 0.4314 -0.0376 -0.0251 0.0514  902  MET A C   
6388  O O   . MET A 904  ? 0.3944 0.3061 0.4361 -0.0410 -0.0247 0.0563  902  MET A O   
6389  C CB  . MET A 904  ? 0.3410 0.2559 0.3780 -0.0333 -0.0204 0.0434  902  MET A CB  
6390  C CG  . MET A 904  ? 0.3667 0.2846 0.4026 -0.0325 -0.0189 0.0395  902  MET A CG  
6391  S SD  . MET A 904  ? 0.4577 0.3815 0.4943 -0.0368 -0.0179 0.0421  902  MET A SD  
6392  C CE  . MET A 904  ? 0.4659 0.3841 0.5079 -0.0386 -0.0216 0.0411  902  MET A CE  
6393  N N   . ARG A 905  ? 0.3435 0.2467 0.3861 -0.0346 -0.0267 0.0499  903  ARG A N   
6394  C CA  . ARG A 905  ? 0.3738 0.2748 0.4169 -0.0352 -0.0281 0.0542  903  ARG A CA  
6395  C C   . ARG A 905  ? 0.3934 0.2907 0.4407 -0.0393 -0.0314 0.0589  903  ARG A C   
6396  O O   . ARG A 905  ? 0.3937 0.2925 0.4407 -0.0418 -0.0316 0.0644  903  ARG A O   
6397  C CB  . ARG A 905  ? 0.3690 0.2650 0.4128 -0.0311 -0.0295 0.0512  903  ARG A CB  
6398  C CG  . ARG A 905  ? 0.4040 0.2996 0.4468 -0.0308 -0.0300 0.0549  903  ARG A CG  
6399  C CD  . ARG A 905  ? 0.4229 0.3127 0.4676 -0.0270 -0.0323 0.0523  903  ARG A CD  
6400  N NE  . ARG A 905  ? 0.4287 0.3190 0.4720 -0.0231 -0.0308 0.0461  903  ARG A NE  
6401  C CZ  . ARG A 905  ? 0.3936 0.2880 0.4333 -0.0204 -0.0279 0.0440  903  ARG A CZ  
6402  N NH1 . ARG A 905  ? 0.4328 0.3315 0.4696 -0.0213 -0.0260 0.0472  903  ARG A NH1 
6403  N NH2 . ARG A 905  ? 0.4669 0.3612 0.5060 -0.0169 -0.0271 0.0386  903  ARG A NH2 
6404  N N   . GLY A 906  ? 0.3725 0.2651 0.4238 -0.0400 -0.0339 0.0570  904  GLY A N   
6405  C CA  . GLY A 906  ? 0.3751 0.2637 0.4308 -0.0440 -0.0372 0.0615  904  GLY A CA  
6406  C C   . GLY A 906  ? 0.4399 0.3349 0.4950 -0.0488 -0.0356 0.0660  904  GLY A C   
6407  O O   . GLY A 906  ? 0.4618 0.3554 0.5194 -0.0526 -0.0376 0.0717  904  GLY A O   
6408  N N   . LEU A 907  ? 0.4263 0.3285 0.4781 -0.0485 -0.0320 0.0638  905  LEU A N   
6409  C CA  . LEU A 907  ? 0.4381 0.3476 0.4888 -0.0526 -0.0300 0.0675  905  LEU A CA  
6410  C C   . LEU A 907  ? 0.4253 0.3407 0.4723 -0.0534 -0.0278 0.0717  905  LEU A C   
6411  O O   . LEU A 907  ? 0.4884 0.4108 0.5341 -0.0565 -0.0259 0.0748  905  LEU A O   
6412  C CB  . LEU A 907  ? 0.4283 0.3432 0.4771 -0.0517 -0.0272 0.0632  905  LEU A CB  
6413  C CG  . LEU A 907  ? 0.4673 0.3780 0.5200 -0.0518 -0.0294 0.0596  905  LEU A CG  
6414  C CD1 . LEU A 907  ? 0.4909 0.4072 0.5414 -0.0507 -0.0267 0.0554  905  LEU A CD1 
6415  C CD2 . LEU A 907  ? 0.4744 0.3828 0.5319 -0.0567 -0.0323 0.0642  905  LEU A CD2 
6416  N N   . GLY A 908  ? 0.4053 0.3182 0.4505 -0.0505 -0.0280 0.0716  906  GLY A N   
6417  C CA  . GLY A 908  ? 0.4276 0.3458 0.4693 -0.0510 -0.0261 0.0753  906  GLY A CA  
6418  C C   . GLY A 908  ? 0.4057 0.3305 0.4425 -0.0484 -0.0221 0.0719  906  GLY A C   
6419  O O   . GLY A 908  ? 0.3837 0.3139 0.4175 -0.0489 -0.0204 0.0746  906  GLY A O   
6420  N N   . ARG A 909  ? 0.4060 0.3308 0.4421 -0.0456 -0.0208 0.0663  907  ARG A N   
6421  C CA  . ARG A 909  ? 0.3468 0.2770 0.3784 -0.0429 -0.0173 0.0631  907  ARG A CA  
6422  C C   . ARG A 909  ? 0.3919 0.3199 0.4216 -0.0396 -0.0172 0.0621  907  ARG A C   
6423  O O   . ARG A 909  ? 0.4105 0.3318 0.4424 -0.0378 -0.0196 0.0611  907  ARG A O   
6424  C CB  . ARG A 909  ? 0.3627 0.2929 0.3942 -0.0407 -0.0162 0.0575  907  ARG A CB  
6425  C CG  . ARG A 909  ? 0.3868 0.3193 0.4202 -0.0436 -0.0163 0.0577  907  ARG A CG  
6426  C CD  . ARG A 909  ? 0.4758 0.4165 0.5076 -0.0468 -0.0142 0.0613  907  ARG A CD  
6427  N NE  . ARG A 909  ? 0.5487 0.4925 0.5823 -0.0492 -0.0140 0.0609  907  ARG A NE  
6428  C CZ  . ARG A 909  ? 0.6423 0.5853 0.6795 -0.0532 -0.0160 0.0644  907  ARG A CZ  
6429  N NH1 . ARG A 909  ? 0.6016 0.5407 0.6410 -0.0553 -0.0184 0.0689  907  ARG A NH1 
6430  N NH2 . ARG A 909  ? 0.6638 0.6102 0.7027 -0.0551 -0.0156 0.0636  907  ARG A NH2 
6431  N N   . LYS A 910  ? 0.3352 0.2691 0.3612 -0.0387 -0.0145 0.0623  908  LYS A N   
6432  C CA  . LYS A 910  ? 0.3593 0.2919 0.3833 -0.0356 -0.0141 0.0610  908  LYS A CA  
6433  C C   . LYS A 910  ? 0.3414 0.2712 0.3650 -0.0318 -0.0134 0.0553  908  LYS A C   
6434  O O   . LYS A 910  ? 0.3422 0.2752 0.3643 -0.0310 -0.0113 0.0522  908  LYS A O   
6435  C CB  . LYS A 910  ? 0.3580 0.2978 0.3782 -0.0357 -0.0115 0.0623  908  LYS A CB  
6436  C CG  . LYS A 910  ? 0.4633 0.4070 0.4833 -0.0393 -0.0119 0.0679  908  LYS A CG  
6437  C CD  . LYS A 910  ? 0.4397 0.3904 0.4558 -0.0388 -0.0094 0.0685  908  LYS A CD  
6438  C CE  . LYS A 910  ? 0.4660 0.4143 0.4807 -0.0352 -0.0093 0.0662  908  LYS A CE  
6439  N NZ  . LYS A 910  ? 0.6599 0.6146 0.6712 -0.0352 -0.0076 0.0676  908  LYS A NZ  
6440  N N   . VAL A 911  ? 0.3412 0.2654 0.3664 -0.0294 -0.0153 0.0540  909  VAL A N   
6441  C CA  . VAL A 911  ? 0.3044 0.2258 0.3294 -0.0257 -0.0149 0.0488  909  VAL A CA  
6442  C C   . VAL A 911  ? 0.3342 0.2559 0.3575 -0.0229 -0.0142 0.0480  909  VAL A C   
6443  O O   . VAL A 911  ? 0.3265 0.2457 0.3510 -0.0230 -0.0161 0.0505  909  VAL A O   
6444  C CB  . VAL A 911  ? 0.3379 0.2525 0.3670 -0.0251 -0.0181 0.0472  909  VAL A CB  
6445  C CG1 . VAL A 911  ? 0.3097 0.2223 0.3384 -0.0211 -0.0176 0.0418  909  VAL A CG1 
6446  C CG2 . VAL A 911  ? 0.3202 0.2346 0.3513 -0.0281 -0.0189 0.0479  909  VAL A CG2 
6447  N N   . GLU A 912  ? 0.2668 0.1917 0.2874 -0.0207 -0.0116 0.0446  910  GLU A N   
6448  C CA  . GLU A 912  ? 0.2703 0.1957 0.2893 -0.0180 -0.0108 0.0433  910  GLU A CA  
6449  C C   . GLU A 912  ? 0.2840 0.2065 0.3037 -0.0148 -0.0108 0.0386  910  GLU A C   
6450  O O   . GLU A 912  ? 0.2684 0.1920 0.2874 -0.0142 -0.0096 0.0358  910  GLU A O   
6451  C CB  . GLU A 912  ? 0.3262 0.2577 0.3416 -0.0181 -0.0077 0.0432  910  GLU A CB  
6452  C CG  . GLU A 912  ? 0.3013 0.2338 0.3153 -0.0158 -0.0069 0.0424  910  GLU A CG  
6453  C CD  . GLU A 912  ? 0.3428 0.2752 0.3574 -0.0168 -0.0084 0.0462  910  GLU A CD  
6454  O OE1 . GLU A 912  ? 0.3703 0.3031 0.3855 -0.0196 -0.0095 0.0499  910  GLU A OE1 
6455  O OE2 . GLU A 912  ? 0.3758 0.3079 0.3901 -0.0149 -0.0085 0.0457  910  GLU A OE2 
6456  N N   . GLN A 913  ? 0.2932 0.2126 0.3145 -0.0126 -0.0123 0.0378  911  GLN A N   
6457  C CA  . GLN A 913  ? 0.2714 0.1887 0.2933 -0.0094 -0.0124 0.0334  911  GLN A CA  
6458  C C   . GLN A 913  ? 0.3090 0.2270 0.3304 -0.0068 -0.0118 0.0324  911  GLN A C   
6459  O O   . GLN A 913  ? 0.3233 0.2405 0.3455 -0.0071 -0.0131 0.0350  911  GLN A O   
6460  C CB  . GLN A 913  ? 0.3185 0.2301 0.3443 -0.0089 -0.0155 0.0323  911  GLN A CB  
6461  C CG  . GLN A 913  ? 0.3337 0.2442 0.3606 -0.0112 -0.0163 0.0325  911  GLN A CG  
6462  C CD  . GLN A 913  ? 0.3488 0.2537 0.3794 -0.0100 -0.0193 0.0302  911  GLN A CD  
6463  O OE1 . GLN A 913  ? 0.3961 0.2966 0.4297 -0.0101 -0.0222 0.0318  911  GLN A OE1 
6464  N NE2 . GLN A 913  ? 0.2951 0.2001 0.3255 -0.0088 -0.0188 0.0263  911  GLN A NE2 
6465  N N   . ILE A 914  ? 0.3083 0.2282 0.3284 -0.0044 -0.0100 0.0287  912  ILE A N   
6466  C CA  . ILE A 914  ? 0.3058 0.2263 0.3258 -0.0018 -0.0097 0.0272  912  ILE A CA  
6467  C C   . ILE A 914  ? 0.3737 0.2896 0.3972 0.0003  -0.0125 0.0257  912  ILE A C   
6468  O O   . ILE A 914  ? 0.3182 0.2311 0.3435 0.0007  -0.0140 0.0237  912  ILE A O   
6469  C CB  . ILE A 914  ? 0.3642 0.2882 0.3819 -0.0001 -0.0069 0.0240  912  ILE A CB  
6470  N N   . GLY A 915  ? 0.3663 0.2817 0.3910 0.0016  -0.0136 0.0264  913  GLY A N   
6471  C CA  . GLY A 915  ? 0.3627 0.2741 0.3907 0.0041  -0.0162 0.0244  913  GLY A CA  
6472  C C   . GLY A 915  ? 0.3242 0.2376 0.3520 0.0073  -0.0149 0.0197  913  GLY A C   
6473  O O   . GLY A 915  ? 0.3683 0.2861 0.3937 0.0080  -0.0122 0.0188  913  GLY A O   
6474  N N   . LEU A 916  ? 0.3428 0.2530 0.3730 0.0092  -0.0168 0.0165  914  LEU A N   
6475  C CA  . LEU A 916  ? 0.3636 0.2760 0.3935 0.0122  -0.0156 0.0118  914  LEU A CA  
6476  C C   . LEU A 916  ? 0.4075 0.3195 0.4400 0.0154  -0.0171 0.0099  914  LEU A C   
6477  O O   . LEU A 916  ? 0.3831 0.2909 0.4187 0.0158  -0.0201 0.0110  914  LEU A O   
6478  C CB  . LEU A 916  ? 0.3781 0.2882 0.4091 0.0127  -0.0167 0.0089  914  LEU A CB  
6479  C CG  . LEU A 916  ? 0.3591 0.2704 0.3876 0.0100  -0.0151 0.0099  914  LEU A CG  
6480  C CD1 . LEU A 916  ? 0.3882 0.2984 0.4174 0.0113  -0.0158 0.0059  914  LEU A CD1 
6481  C CD2 . LEU A 916  ? 0.3486 0.2654 0.3731 0.0094  -0.0114 0.0106  914  LEU A CD2 
6482  N N   . ALA A 917  ? 0.3715 0.2880 0.4028 0.0177  -0.0149 0.0069  915  ALA A N   
6483  C CA  . ALA A 917  ? 0.4171 0.3342 0.4508 0.0210  -0.0160 0.0046  915  ALA A CA  
6484  C C   . ALA A 917  ? 0.4074 0.3211 0.4443 0.0236  -0.0187 0.0007  915  ALA A C   
6485  O O   . ALA A 917  ? 0.3724 0.2849 0.4090 0.0232  -0.0189 -0.0011 915  ALA A O   
6486  C CB  . ALA A 917  ? 0.4080 0.3315 0.4397 0.0225  -0.0128 0.0027  915  ALA A CB  
6487  N N   . SER A 918  ? 0.4189 0.3315 0.4591 0.0264  -0.0209 -0.0009 916  SER A N   
6488  C CA  . SER A 918  ? 0.4024 0.3115 0.4461 0.0292  -0.0240 -0.0049 916  SER A CA  
6489  C C   . SER A 918  ? 0.3357 0.2489 0.3782 0.0314  -0.0222 -0.0099 916  SER A C   
6490  O O   . SER A 918  ? 0.3615 0.2720 0.4056 0.0325  -0.0241 -0.0130 916  SER A O   
6491  C CB  . SER A 918  ? 0.4266 0.3342 0.4740 0.0321  -0.0265 -0.0058 916  SER A CB  
6492  O OG  . SER A 918  ? 0.5217 0.4358 0.5682 0.0343  -0.0241 -0.0079 916  SER A OG  
6493  N N   . GLU A 919  ? 0.3897 0.3095 0.4293 0.0318  -0.0186 -0.0105 917  GLU A N   
6494  C CA  . GLU A 919  ? 0.4012 0.3257 0.4391 0.0338  -0.0167 -0.0147 917  GLU A CA  
6495  C C   . GLU A 919  ? 0.4202 0.3433 0.4561 0.0320  -0.0162 -0.0150 917  GLU A C   
6496  O O   . GLU A 919  ? 0.4200 0.3456 0.4553 0.0339  -0.0157 -0.0190 917  GLU A O   
6497  C CB  . GLU A 919  ? 0.4466 0.3783 0.4816 0.0337  -0.0128 -0.0141 917  GLU A CB  
6498  C CG  . GLU A 919  ? 0.5936 0.5285 0.6305 0.0362  -0.0128 -0.0152 917  GLU A CG  
6499  C CD  . GLU A 919  ? 0.5968 0.5305 0.6342 0.0345  -0.0130 -0.0109 917  GLU A CD  
6500  O OE1 . GLU A 919  ? 0.5256 0.4543 0.5630 0.0318  -0.0144 -0.0074 917  GLU A OE1 
6501  O OE2 . GLU A 919  ? 0.6824 0.6204 0.7202 0.0356  -0.0118 -0.0111 917  GLU A OE2 
6502  N N   . THR A 920  ? 0.3537 0.2735 0.3885 0.0284  -0.0163 -0.0110 918  THR A N   
6503  C CA  . THR A 920  ? 0.3388 0.2575 0.3720 0.0268  -0.0161 -0.0115 918  THR A CA  
6504  C C   . THR A 920  ? 0.3640 0.2780 0.4006 0.0283  -0.0196 -0.0148 918  THR A C   
6505  O O   . THR A 920  ? 0.3120 0.2259 0.3477 0.0278  -0.0196 -0.0165 918  THR A O   
6506  C CB  . THR A 920  ? 0.3430 0.2597 0.3746 0.0227  -0.0155 -0.0066 918  THR A CB  
6507  O OG1 . THR A 920  ? 0.3365 0.2479 0.3710 0.0214  -0.0184 -0.0038 918  THR A OG1 
6508  C CG2 . THR A 920  ? 0.3389 0.2603 0.3670 0.0213  -0.0120 -0.0039 918  THR A CG2 
6509  N N   . GLY A 921  ? 0.3532 0.2637 0.3939 0.0303  -0.0228 -0.0160 919  GLY A N   
6510  C CA  . GLY A 921  ? 0.3628 0.2680 0.4071 0.0316  -0.0266 -0.0189 919  GLY A CA  
6511  C C   . GLY A 921  ? 0.3148 0.2230 0.3588 0.0344  -0.0264 -0.0247 919  GLY A C   
6512  O O   . GLY A 921  ? 0.3773 0.2818 0.4233 0.0346  -0.0288 -0.0271 919  GLY A O   
6513  N N   . VAL A 922  ? 0.3155 0.2306 0.3571 0.0367  -0.0235 -0.0271 920  VAL A N   
6514  C CA  . VAL A 922  ? 0.3167 0.2356 0.3577 0.0397  -0.0231 -0.0327 920  VAL A CA  
6515  C C   . VAL A 922  ? 0.2952 0.2163 0.3326 0.0377  -0.0211 -0.0326 920  VAL A C   
6516  O O   . VAL A 922  ? 0.3057 0.2296 0.3423 0.0398  -0.0211 -0.0370 920  VAL A O   
6517  C CB  . VAL A 922  ? 0.3381 0.2642 0.3780 0.0427  -0.0208 -0.0352 920  VAL A CB  
6518  C CG1 . VAL A 922  ? 0.3639 0.2882 0.4082 0.0457  -0.0234 -0.0369 920  VAL A CG1 
6519  C CG2 . VAL A 922  ? 0.3141 0.2447 0.3503 0.0404  -0.0168 -0.0308 920  VAL A CG2 
6520  N N   . GLY A 923  ? 0.2870 0.2072 0.3220 0.0339  -0.0194 -0.0277 921  GLY A N   
6521  C CA  . GLY A 923  ? 0.2838 0.2055 0.3156 0.0319  -0.0179 -0.0273 921  GLY A CA  
6522  C C   . GLY A 923  ? 0.3009 0.2169 0.3339 0.0284  -0.0196 -0.0240 921  GLY A C   
6523  O O   . GLY A 923  ? 0.3040 0.2143 0.3406 0.0278  -0.0226 -0.0229 921  GLY A O   
6524  N N   . THR A 924  ? 0.2764 0.1939 0.3063 0.0259  -0.0177 -0.0222 922  THR A N   
6525  C CA  . THR A 924  ? 0.2911 0.2041 0.3221 0.0225  -0.0192 -0.0195 922  THR A CA  
6526  C C   . THR A 924  ? 0.2852 0.2001 0.3132 0.0194  -0.0165 -0.0144 922  THR A C   
6527  O O   . THR A 924  ? 0.2792 0.1977 0.3038 0.0184  -0.0140 -0.0139 922  THR A O   
6528  C CB  . THR A 924  ? 0.2779 0.1910 0.3086 0.0226  -0.0201 -0.0226 922  THR A CB  
6529  O OG1 . THR A 924  ? 0.2787 0.1979 0.3052 0.0235  -0.0169 -0.0238 922  THR A OG1 
6530  C CG2 . THR A 924  ? 0.3006 0.2113 0.3349 0.0257  -0.0234 -0.0277 922  THR A CG2 
6531  N N   . PHE A 925  ? 0.2628 0.1752 0.2921 0.0179  -0.0171 -0.0107 923  PHE A N   
6532  C CA  . PHE A 925  ? 0.2804 0.1947 0.3071 0.0151  -0.0146 -0.0061 923  PHE A CA  
6533  C C   . PHE A 925  ? 0.2772 0.1875 0.3055 0.0117  -0.0163 -0.0023 923  PHE A C   
6534  O O   . PHE A 925  ? 0.2683 0.1737 0.3002 0.0114  -0.0194 -0.0018 923  PHE A O   
6535  C CB  . PHE A 925  ? 0.2614 0.1773 0.2878 0.0161  -0.0135 -0.0046 923  PHE A CB  
6536  C CG  . PHE A 925  ? 0.2600 0.1809 0.2846 0.0190  -0.0114 -0.0076 923  PHE A CG  
6537  C CD1 . PHE A 925  ? 0.2662 0.1872 0.2928 0.0224  -0.0128 -0.0118 923  PHE A CD1 
6538  C CD2 . PHE A 925  ? 0.2708 0.1964 0.2918 0.0182  -0.0080 -0.0061 923  PHE A CD2 
6539  C CE1 . PHE A 925  ? 0.2576 0.1839 0.2824 0.0249  -0.0107 -0.0143 923  PHE A CE1 
6540  C CE2 . PHE A 925  ? 0.2527 0.1830 0.2721 0.0206  -0.0060 -0.0084 923  PHE A CE2 
6541  C CZ  . PHE A 925  ? 0.2703 0.2013 0.2915 0.0238  -0.0072 -0.0124 923  PHE A CZ  
6542  N N   . VAL A 926  ? 0.2790 0.1916 0.3047 0.0091  -0.0142 0.0004  924  VAL A N   
6543  C CA  . VAL A 926  ? 0.2935 0.2042 0.3199 0.0055  -0.0149 0.0048  924  VAL A CA  
6544  C C   . VAL A 926  ? 0.2645 0.1783 0.2883 0.0045  -0.0124 0.0081  924  VAL A C   
6545  O O   . VAL A 926  ? 0.2732 0.1913 0.2938 0.0050  -0.0096 0.0075  924  VAL A O   
6546  C CB  . VAL A 926  ? 0.2576 0.1688 0.2833 0.0033  -0.0147 0.0050  924  VAL A CB  
6547  C CG1 . VAL A 926  ? 0.2877 0.1980 0.3140 -0.0005 -0.0150 0.0097  924  VAL A CG1 
6548  C CG2 . VAL A 926  ? 0.2861 0.1941 0.3147 0.0043  -0.0174 0.0015  924  VAL A CG2 
6549  N N   . PRO A 927  ? 0.2797 0.1917 0.3048 0.0031  -0.0135 0.0115  925  PRO A N   
6550  C CA  . PRO A 927  ? 0.2976 0.2129 0.3203 0.0021  -0.0112 0.0144  925  PRO A CA  
6551  C C   . PRO A 927  ? 0.2353 0.1535 0.2556 -0.0005 -0.0093 0.0163  925  PRO A C   
6552  O O   . PRO A 927  ? 0.2419 0.1586 0.2633 -0.0027 -0.0105 0.0175  925  PRO A O   
6553  C CB  . PRO A 927  ? 0.2930 0.2052 0.3180 0.0011  -0.0134 0.0176  925  PRO A CB  
6554  C CG  . PRO A 927  ? 0.3403 0.2476 0.3687 0.0003  -0.0166 0.0176  925  PRO A CG  
6555  C CD  . PRO A 927  ? 0.3078 0.2146 0.3367 0.0022  -0.0169 0.0130  925  PRO A CD  
6556  N N   . PRO A 928  ? 0.2796 0.2019 0.2967 -0.0003 -0.0065 0.0165  926  PRO A N   
6557  C CA  . PRO A 928  ? 0.2690 0.1943 0.2840 -0.0027 -0.0048 0.0187  926  PRO A CA  
6558  C C   . PRO A 928  ? 0.2527 0.1769 0.2689 -0.0056 -0.0061 0.0226  926  PRO A C   
6559  O O   . PRO A 928  ? 0.2513 0.1742 0.2685 -0.0057 -0.0071 0.0246  926  PRO A O   
6560  C CB  . PRO A 928  ? 0.2579 0.1870 0.2701 -0.0018 -0.0022 0.0186  926  PRO A CB  
6561  C CG  . PRO A 928  ? 0.3093 0.2382 0.3217 0.0012  -0.0020 0.0153  926  PRO A CG  
6562  C CD  . PRO A 928  ? 0.2583 0.1831 0.2739 0.0021  -0.0048 0.0146  926  PRO A CD  
6563  N N   . THR A 929  ? 0.2497 0.1747 0.2658 -0.0079 -0.0061 0.0237  927  THR A N   
6564  C CA  . THR A 929  ? 0.2607 0.1844 0.2787 -0.0108 -0.0077 0.0273  927  THR A CA  
6565  C C   . THR A 929  ? 0.2665 0.1948 0.2825 -0.0132 -0.0059 0.0291  927  THR A C   
6566  O O   . THR A 929  ? 0.2583 0.1889 0.2727 -0.0127 -0.0043 0.0271  927  THR A O   
6567  C CB  . THR A 929  ? 0.2582 0.1777 0.2795 -0.0114 -0.0104 0.0264  927  THR A CB  
6568  O OG1 . THR A 929  ? 0.2906 0.2059 0.3139 -0.0090 -0.0123 0.0244  927  THR A OG1 
6569  C CG2 . THR A 929  ? 0.2615 0.1799 0.2848 -0.0149 -0.0121 0.0305  927  THR A CG2 
6570  N N   . ILE A 930  ? 0.2574 0.1872 0.2732 -0.0155 -0.0060 0.0329  928  ILE A N   
6571  C CA  . ILE A 930  ? 0.2613 0.1958 0.2756 -0.0179 -0.0045 0.0348  928  ILE A CA  
6572  C C   . ILE A 930  ? 0.2705 0.2039 0.2873 -0.0211 -0.0065 0.0383  928  ILE A C   
6573  O O   . ILE A 930  ? 0.2813 0.2121 0.2996 -0.0218 -0.0083 0.0410  928  ILE A O   
6574  C CB  . ILE A 930  ? 0.2269 0.1656 0.2386 -0.0179 -0.0027 0.0363  928  ILE A CB  
6575  C CG1 . ILE A 930  ? 0.2288 0.1685 0.2384 -0.0150 -0.0008 0.0331  928  ILE A CG1 
6576  C CG2 . ILE A 930  ? 0.2901 0.2341 0.3005 -0.0203 -0.0013 0.0382  928  ILE A CG2 
6577  C CD1 . ILE A 930  ? 0.2941 0.2365 0.3018 -0.0146 0.0004  0.0342  928  ILE A CD1 
6578  N N   . ILE A 931  ? 0.2569 0.1921 0.2742 -0.0229 -0.0062 0.0383  929  ILE A N   
6579  C CA  . ILE A 931  ? 0.2846 0.2193 0.3044 -0.0264 -0.0080 0.0416  929  ILE A CA  
6580  C C   . ILE A 931  ? 0.2951 0.2366 0.3133 -0.0287 -0.0060 0.0435  929  ILE A C   
6581  O O   . ILE A 931  ? 0.2934 0.2382 0.3101 -0.0281 -0.0043 0.0411  929  ILE A O   
6582  C CB  . ILE A 931  ? 0.3218 0.2528 0.3446 -0.0267 -0.0099 0.0397  929  ILE A CB  
6583  C CG1 . ILE A 931  ? 0.2710 0.1958 0.2953 -0.0239 -0.0117 0.0370  929  ILE A CG1 
6584  C CG2 . ILE A 931  ? 0.3017 0.2320 0.3275 -0.0306 -0.0118 0.0436  929  ILE A CG2 
6585  C CD1 . ILE A 931  ? 0.3104 0.2316 0.3375 -0.0237 -0.0136 0.0343  929  ILE A CD1 
6586  N N   . GLU A 932  ? 0.2728 0.2164 0.2911 -0.0313 -0.0064 0.0478  930  GLU A N   
6587  C CA  . GLU A 932  ? 0.3075 0.2582 0.3243 -0.0336 -0.0046 0.0498  930  GLU A CA  
6588  C C   . GLU A 932  ? 0.3001 0.2515 0.3198 -0.0369 -0.0058 0.0516  930  GLU A C   
6589  O O   . GLU A 932  ? 0.3286 0.2765 0.3510 -0.0391 -0.0081 0.0548  930  GLU A O   
6590  C CB  . GLU A 932  ? 0.2909 0.2447 0.3062 -0.0347 -0.0043 0.0535  930  GLU A CB  
6591  C CG  . GLU A 932  ? 0.3091 0.2633 0.3216 -0.0315 -0.0029 0.0513  930  GLU A CG  
6592  C CD  . GLU A 932  ? 0.3963 0.3522 0.4077 -0.0322 -0.0031 0.0546  930  GLU A CD  
6593  O OE1 . GLU A 932  ? 0.4058 0.3671 0.4162 -0.0346 -0.0025 0.0577  930  GLU A OE1 
6594  O OE2 . GLU A 932  ? 0.3510 0.3031 0.3624 -0.0302 -0.0040 0.0542  930  GLU A OE2 
6595  N N   . LEU A 933  ? 0.2978 0.2532 0.3170 -0.0371 -0.0043 0.0495  931  LEU A N   
6596  C CA  . LEU A 933  ? 0.3412 0.2977 0.3631 -0.0401 -0.0053 0.0508  931  LEU A CA  
6597  C C   . LEU A 933  ? 0.3878 0.3523 0.4088 -0.0431 -0.0038 0.0539  931  LEU A C   
6598  O O   . LEU A 933  ? 0.3281 0.2979 0.3461 -0.0420 -0.0016 0.0536  931  LEU A O   
6599  C CB  . LEU A 933  ? 0.3398 0.2961 0.3621 -0.0386 -0.0049 0.0464  931  LEU A CB  
6600  C CG  . LEU A 933  ? 0.3941 0.3433 0.4172 -0.0357 -0.0063 0.0428  931  LEU A CG  
6601  C CD1 . LEU A 933  ? 0.4028 0.3528 0.4262 -0.0345 -0.0058 0.0389  931  LEU A CD1 
6602  C CD2 . LEU A 933  ? 0.4064 0.3493 0.4331 -0.0372 -0.0094 0.0449  931  LEU A CD2 
6603  N N   . GLU A 934  ? 0.4048 0.3704 0.4288 -0.0468 -0.0050 0.0569  932  GLU A N   
6604  C CA  . GLU A 934  ? 0.4542 0.4283 0.4777 -0.0498 -0.0036 0.0598  932  GLU A CA  
6605  C C   . GLU A 934  ? 0.5531 0.5326 0.5760 -0.0490 -0.0017 0.0562  932  GLU A C   
6606  O O   . GLU A 934  ? 0.5231 0.5097 0.5434 -0.0483 0.0007  0.0555  932  GLU A O   
6607  C CB  . GLU A 934  ? 0.5552 0.5289 0.5824 -0.0544 -0.0056 0.0646  932  GLU A CB  
6608  C CG  . GLU A 934  ? 0.5563 0.5257 0.5841 -0.0556 -0.0075 0.0689  932  GLU A CG  
6609  C CD  . GLU A 934  ? 0.6675 0.6429 0.6918 -0.0555 -0.0057 0.0714  932  GLU A CD  
6610  O OE1 . GLU A 934  ? 0.7859 0.7697 0.8093 -0.0580 -0.0042 0.0737  932  GLU A OE1 
6611  O OE2 . GLU A 934  ? 0.7007 0.6728 0.7229 -0.0530 -0.0058 0.0708  932  GLU A OE2 
6612  N N   . LYS A 935  ? 0.5207 0.4970 0.5460 -0.0488 -0.0028 0.0537  933  LYS A N   
6613  C CA  . LYS A 935  ? 0.5775 0.5584 0.6025 -0.0479 -0.0013 0.0503  933  LYS A CA  
6614  C C   . LYS A 935  ? 0.5058 0.4808 0.5307 -0.0445 -0.0020 0.0456  933  LYS A C   
6615  O O   . LYS A 935  ? 0.4499 0.4176 0.4763 -0.0438 -0.0040 0.0452  933  LYS A O   
6616  C CB  . LYS A 935  ? 0.5554 0.5400 0.5838 -0.0518 -0.0021 0.0523  933  LYS A CB  
6617  N N   . LEU A 936  ? 0.5144 0.4930 0.5374 -0.0421 -0.0002 0.0419  934  LEU A N   
6618  C CA  . LEU A 936  ? 0.5391 0.5131 0.5619 -0.0390 -0.0007 0.0376  934  LEU A CA  
6619  C C   . LEU A 936  ? 0.5324 0.5024 0.5589 -0.0406 -0.0032 0.0371  934  LEU A C   
6620  O O   . LEU A 936  ? 0.5035 0.4680 0.5302 -0.0383 -0.0043 0.0342  934  LEU A O   
6621  C CB  . LEU A 936  ? 0.5452 0.5242 0.5658 -0.0368 0.0013  0.0343  934  LEU A CB  
6622  N N   . SER A 937  ? 0.5538 0.5266 0.5833 -0.0445 -0.0040 0.0400  935  SER A N   
6623  C CA  . SER A 937  ? 0.5403 0.5094 0.5739 -0.0464 -0.0065 0.0398  935  SER A CA  
6624  C C   . SER A 937  ? 0.5201 0.4810 0.5557 -0.0469 -0.0092 0.0413  935  SER A C   
6625  O O   . SER A 937  ? 0.5291 0.4853 0.5679 -0.0475 -0.0116 0.0400  935  SER A O   
6626  C CB  . SER A 937  ? 0.5728 0.5479 0.6092 -0.0508 -0.0066 0.0427  935  SER A CB  
6627  O OG  . SER A 937  ? 0.5540 0.5337 0.5895 -0.0531 -0.0054 0.0470  935  SER A OG  
6628  N N   . ASP A 938  ? 0.5006 0.4598 0.5346 -0.0465 -0.0089 0.0437  936  ASP A N   
6629  C CA  . ASP A 938  ? 0.5079 0.4590 0.5436 -0.0463 -0.0114 0.0447  936  ASP A CA  
6630  C C   . ASP A 938  ? 0.5184 0.4639 0.5537 -0.0423 -0.0123 0.0398  936  ASP A C   
6631  O O   . ASP A 938  ? 0.5269 0.4656 0.5647 -0.0421 -0.0149 0.0394  936  ASP A O   
6632  C CB  . ASP A 938  ? 0.5226 0.4735 0.5562 -0.0460 -0.0108 0.0478  936  ASP A CB  
6633  C CG  . ASP A 938  ? 0.6185 0.5758 0.6518 -0.0496 -0.0097 0.0526  936  ASP A CG  
6634  O OD1 . ASP A 938  ? 0.6248 0.5854 0.6607 -0.0529 -0.0101 0.0543  936  ASP A OD1 
6635  O OD2 . ASP A 938  ? 0.6083 0.5677 0.6390 -0.0490 -0.0084 0.0545  936  ASP A OD2 
6636  N N   . LEU A 939  ? 0.4731 0.4214 0.5053 -0.0393 -0.0102 0.0361  937  LEU A N   
6637  C CA  . LEU A 939  ? 0.4891 0.4332 0.5203 -0.0354 -0.0106 0.0316  937  LEU A CA  
6638  C C   . LEU A 939  ? 0.5048 0.4497 0.5376 -0.0355 -0.0114 0.0284  937  LEU A C   
6639  O O   . LEU A 939  ? 0.5374 0.4878 0.5689 -0.0355 -0.0096 0.0274  937  LEU A O   
6640  C CB  . LEU A 939  ? 0.4488 0.3954 0.4755 -0.0321 -0.0079 0.0298  937  LEU A CB  
6641  C CG  . LEU A 939  ? 0.4936 0.4360 0.5190 -0.0282 -0.0082 0.0258  937  LEU A CG  
6642  C CD1 . LEU A 939  ? 0.4596 0.3957 0.4867 -0.0278 -0.0103 0.0266  937  LEU A CD1 
6643  C CD2 . LEU A 939  ? 0.4255 0.3709 0.4467 -0.0255 -0.0055 0.0245  937  LEU A CD2 
6644  N N   . GLN A 940  ? 0.5183 0.4576 0.5542 -0.0354 -0.0141 0.0267  938  GLN A N   
6645  C CA  . GLN A 940  ? 0.5380 0.4777 0.5763 -0.0361 -0.0154 0.0242  938  GLN A CA  
6646  C C   . GLN A 940  ? 0.5953 0.5322 0.6326 -0.0323 -0.0161 0.0190  938  GLN A C   
6647  O O   . GLN A 940  ? 0.5886 0.5257 0.6279 -0.0326 -0.0174 0.0165  938  GLN A O   
6648  C CB  . GLN A 940  ? 0.5581 0.4944 0.6015 -0.0399 -0.0185 0.0266  938  GLN A CB  
6649  N N   . ARG A 941  ? 0.5392 0.4740 0.5736 -0.0289 -0.0152 0.0174  939  ARG A N   
6650  C CA  . ARG A 941  ? 0.5446 0.4774 0.5779 -0.0252 -0.0157 0.0126  939  ARG A CA  
6651  C C   . ARG A 941  ? 0.4741 0.4072 0.5033 -0.0219 -0.0135 0.0117  939  ARG A C   
6652  O O   . ARG A 941  ? 0.4747 0.4068 0.5032 -0.0222 -0.0129 0.0144  939  ARG A O   
6653  C CB  . ARG A 941  ? 0.5334 0.4600 0.5704 -0.0251 -0.0191 0.0107  939  ARG A CB  
6654  N N   . GLU A 942  ? 0.4673 0.4019 0.4938 -0.0188 -0.0125 0.0082  940  GLU A N   
6655  C CA  . GLU A 942  ? 0.4394 0.3744 0.4622 -0.0157 -0.0105 0.0073  940  GLU A CA  
6656  C C   . GLU A 942  ? 0.4433 0.3733 0.4672 -0.0141 -0.0120 0.0065  940  GLU A C   
6657  O O   . GLU A 942  ? 0.4592 0.3860 0.4852 -0.0131 -0.0142 0.0037  940  GLU A O   
6658  C CB  . GLU A 942  ? 0.4619 0.3995 0.4819 -0.0129 -0.0094 0.0038  940  GLU A CB  
6659  C CG  . GLU A 942  ? 0.4841 0.4225 0.5002 -0.0100 -0.0072 0.0032  940  GLU A CG  
6660  C CD  . GLU A 942  ? 0.4905 0.4306 0.5041 -0.0071 -0.0066 -0.0003 940  GLU A CD  
6661  O OE1 . GLU A 942  ? 0.5691 0.5079 0.5840 -0.0062 -0.0084 -0.0033 940  GLU A OE1 
6662  O OE2 . GLU A 942  ? 0.4671 0.4100 0.4774 -0.0056 -0.0044 -0.0001 940  GLU A OE2 
6663  N N   . VAL A 943  ? 0.3827 0.3121 0.4053 -0.0138 -0.0109 0.0088  941  VAL A N   
6664  C CA  . VAL A 943  ? 0.3745 0.2996 0.3982 -0.0122 -0.0121 0.0082  941  VAL A CA  
6665  C C   . VAL A 943  ? 0.3720 0.2988 0.3921 -0.0089 -0.0100 0.0063  941  VAL A C   
6666  O O   . VAL A 943  ? 0.2984 0.2276 0.3159 -0.0089 -0.0078 0.0083  941  VAL A O   
6667  C CB  . VAL A 943  ? 0.3573 0.2804 0.3826 -0.0145 -0.0128 0.0123  941  VAL A CB  
6668  C CG1 . VAL A 943  ? 0.4072 0.3261 0.4333 -0.0123 -0.0140 0.0116  941  VAL A CG1 
6669  C CG2 . VAL A 943  ? 0.3826 0.3040 0.4117 -0.0180 -0.0150 0.0144  941  VAL A CG2 
6670  N N   . PHE A 944  ? 0.3047 0.2302 0.3246 -0.0062 -0.0108 0.0025  942  PHE A N   
6671  C CA  . PHE A 944  ? 0.3286 0.2567 0.3449 -0.0032 -0.0087 0.0004  942  PHE A CA  
6672  C C   . PHE A 944  ? 0.3112 0.2377 0.3274 -0.0014 -0.0085 0.0005  942  PHE A C   
6673  O O   . PHE A 944  ? 0.3296 0.2549 0.3461 0.0012  -0.0093 -0.0025 942  PHE A O   
6674  C CB  . PHE A 944  ? 0.3276 0.2565 0.3436 -0.0012 -0.0094 -0.0037 942  PHE A CB  
6675  C CG  . PHE A 944  ? 0.3229 0.2558 0.3348 0.0008  -0.0070 -0.0049 942  PHE A CG  
6676  C CD1 . PHE A 944  ? 0.3151 0.2514 0.3251 -0.0003 -0.0054 -0.0035 942  PHE A CD1 
6677  C CD2 . PHE A 944  ? 0.3161 0.2497 0.3262 0.0039  -0.0064 -0.0073 942  PHE A CD2 
6678  C CE1 . PHE A 944  ? 0.3332 0.2728 0.3396 0.0015  -0.0034 -0.0043 942  PHE A CE1 
6679  C CE2 . PHE A 944  ? 0.3036 0.2409 0.3101 0.0055  -0.0042 -0.0079 942  PHE A CE2 
6680  C CZ  . PHE A 944  ? 0.2796 0.2197 0.2842 0.0043  -0.0028 -0.0063 942  PHE A CZ  
6681  N N   . GLY A 945  ? 0.2631 0.1898 0.2787 -0.0027 -0.0074 0.0039  943  GLY A N   
6682  C CA  . GLY A 945  ? 0.2763 0.2017 0.2920 -0.0013 -0.0072 0.0044  943  GLY A CA  
6683  C C   . GLY A 945  ? 0.2575 0.1849 0.2716 -0.0027 -0.0053 0.0080  943  GLY A C   
6684  O O   . GLY A 945  ? 0.2665 0.1966 0.2790 -0.0044 -0.0039 0.0097  943  GLY A O   
6685  N N   . PRO A 946  ? 0.2416 0.1677 0.2560 -0.0019 -0.0054 0.0090  944  PRO A N   
6686  C CA  . PRO A 946  ? 0.2267 0.1551 0.2394 -0.0028 -0.0035 0.0118  944  PRO A CA  
6687  C C   . PRO A 946  ? 0.2472 0.1746 0.2614 -0.0057 -0.0045 0.0155  944  PRO A C   
6688  O O   . PRO A 946  ? 0.2469 0.1727 0.2622 -0.0061 -0.0053 0.0175  944  PRO A O   
6689  C CB  . PRO A 946  ? 0.2586 0.1861 0.2712 -0.0004 -0.0034 0.0109  944  PRO A CB  
6690  C CG  . PRO A 946  ? 0.2552 0.1787 0.2711 0.0006  -0.0062 0.0091  944  PRO A CG  
6691  C CD  . PRO A 946  ? 0.2395 0.1623 0.2561 0.0001  -0.0073 0.0072  944  PRO A CD  
6692  N N   . VAL A 947  ? 0.2402 0.1688 0.2545 -0.0079 -0.0045 0.0165  945  VAL A N   
6693  C CA  . VAL A 947  ? 0.2296 0.1577 0.2457 -0.0111 -0.0057 0.0200  945  VAL A CA  
6694  C C   . VAL A 947  ? 0.2564 0.1893 0.2705 -0.0128 -0.0037 0.0215  945  VAL A C   
6695  O O   . VAL A 947  ? 0.3026 0.2372 0.3165 -0.0133 -0.0033 0.0202  945  VAL A O   
6696  C CB  . VAL A 947  ? 0.2719 0.1966 0.2915 -0.0124 -0.0084 0.0196  945  VAL A CB  
6697  C CG1 . VAL A 947  ? 0.2840 0.2085 0.3054 -0.0159 -0.0095 0.0238  945  VAL A CG1 
6698  C CG2 . VAL A 947  ? 0.2745 0.1944 0.2963 -0.0102 -0.0106 0.0175  945  VAL A CG2 
6699  N N   . LEU A 948  ? 0.2516 0.1867 0.2644 -0.0137 -0.0025 0.0241  946  LEU A N   
6700  C CA  . LEU A 948  ? 0.2224 0.1624 0.2334 -0.0152 -0.0007 0.0254  946  LEU A CA  
6701  C C   . LEU A 948  ? 0.2462 0.1872 0.2589 -0.0186 -0.0017 0.0289  946  LEU A C   
6702  O O   . LEU A 948  ? 0.2739 0.2131 0.2879 -0.0196 -0.0029 0.0315  946  LEU A O   
6703  C CB  . LEU A 948  ? 0.2228 0.1653 0.2312 -0.0142 0.0012  0.0259  946  LEU A CB  
6704  C CG  . LEU A 948  ? 0.2372 0.1848 0.2438 -0.0155 0.0030  0.0270  946  LEU A CG  
6705  C CD1 . LEU A 948  ? 0.2175 0.1671 0.2231 -0.0145 0.0041  0.0244  946  LEU A CD1 
6706  C CD2 . LEU A 948  ? 0.2636 0.2131 0.2683 -0.0147 0.0043  0.0277  946  LEU A CD2 
6707  N N   . HIS A 949  ? 0.2419 0.1860 0.2548 -0.0202 -0.0013 0.0290  947  HIS A N   
6708  C CA  . HIS A 949  ? 0.2537 0.2001 0.2680 -0.0236 -0.0018 0.0325  947  HIS A CA  
6709  C C   . HIS A 949  ? 0.2414 0.1938 0.2532 -0.0241 0.0005  0.0335  947  HIS A C   
6710  O O   . HIS A 949  ? 0.2684 0.2235 0.2782 -0.0224 0.0022  0.0311  947  HIS A O   
6711  C CB  . HIS A 949  ? 0.2559 0.2023 0.2726 -0.0253 -0.0029 0.0320  947  HIS A CB  
6712  C CG  . HIS A 949  ? 0.2923 0.2329 0.3115 -0.0245 -0.0052 0.0302  947  HIS A CG  
6713  N ND1 . HIS A 949  ? 0.2910 0.2298 0.3093 -0.0215 -0.0051 0.0262  947  HIS A ND1 
6714  C CD2 . HIS A 949  ? 0.3226 0.2587 0.3450 -0.0260 -0.0079 0.0317  947  HIS A CD2 
6715  C CE1 . HIS A 949  ? 0.3131 0.2470 0.3341 -0.0212 -0.0074 0.0250  947  HIS A CE1 
6716  N NE2 . HIS A 949  ? 0.3072 0.2391 0.3309 -0.0238 -0.0093 0.0282  947  HIS A NE2 
6717  N N   . VAL A 950  ? 0.2742 0.2290 0.2862 -0.0264 0.0004  0.0371  948  VAL A N   
6718  C CA  . VAL A 950  ? 0.2581 0.2189 0.2678 -0.0269 0.0023  0.0381  948  VAL A CA  
6719  C C   . VAL A 950  ? 0.2779 0.2433 0.2888 -0.0303 0.0022  0.0410  948  VAL A C   
6720  O O   . VAL A 950  ? 0.2609 0.2245 0.2738 -0.0327 0.0006  0.0442  948  VAL A O   
6721  C CB  . VAL A 950  ? 0.2661 0.2266 0.2743 -0.0261 0.0026  0.0396  948  VAL A CB  
6722  C CG1 . VAL A 950  ? 0.2667 0.2338 0.2725 -0.0264 0.0045  0.0401  948  VAL A CG1 
6723  C CG2 . VAL A 950  ? 0.2251 0.1814 0.2325 -0.0229 0.0027  0.0368  948  VAL A CG2 
6724  N N   . ILE A 951  ? 0.2742 0.2455 0.2839 -0.0305 0.0039  0.0399  949  ILE A N   
6725  C CA  . ILE A 951  ? 0.2885 0.2658 0.2990 -0.0336 0.0042  0.0427  949  ILE A CA  
6726  C C   . ILE A 951  ? 0.2947 0.2786 0.3024 -0.0330 0.0064  0.0424  949  ILE A C   
6727  O O   . ILE A 951  ? 0.2668 0.2507 0.2724 -0.0301 0.0075  0.0394  949  ILE A O   
6728  C CB  . ILE A 951  ? 0.3326 0.3115 0.3451 -0.0349 0.0040  0.0416  949  ILE A CB  
6729  C CG1 . ILE A 951  ? 0.3067 0.2879 0.3175 -0.0323 0.0055  0.0375  949  ILE A CG1 
6730  C CG2 . ILE A 951  ? 0.3695 0.3416 0.3849 -0.0354 0.0017  0.0415  949  ILE A CG2 
6731  C CD1 . ILE A 951  ? 0.4047 0.3873 0.4175 -0.0332 0.0051  0.0362  949  ILE A CD1 
6732  N N   . ARG A 952  ? 0.2474 0.2372 0.2553 -0.0357 0.0067  0.0455  950  ARG A N   
6733  C CA  . ARG A 952  ? 0.2729 0.2699 0.2784 -0.0353 0.0086  0.0452  950  ARG A CA  
6734  C C   . ARG A 952  ? 0.2572 0.2614 0.2633 -0.0367 0.0096  0.0448  950  ARG A C   
6735  O O   . ARG A 952  ? 0.2546 0.2594 0.2632 -0.0394 0.0087  0.0467  950  ARG A O   
6736  C CB  . ARG A 952  ? 0.3284 0.3276 0.3331 -0.0371 0.0082  0.0492  950  ARG A CB  
6737  C CG  . ARG A 952  ? 0.3720 0.3637 0.3769 -0.0362 0.0067  0.0504  950  ARG A CG  
6738  C CD  . ARG A 952  ? 0.4008 0.3933 0.4062 -0.0391 0.0055  0.0554  950  ARG A CD  
6739  N NE  . ARG A 952  ? 0.3846 0.3832 0.3874 -0.0390 0.0068  0.0565  950  ARG A NE  
6740  C CZ  . ARG A 952  ? 0.4135 0.4101 0.4148 -0.0375 0.0065  0.0567  950  ARG A CZ  
6741  N NH1 . ARG A 952  ? 0.4106 0.3995 0.4128 -0.0359 0.0051  0.0562  950  ARG A NH1 
6742  N NH2 . ARG A 952  ? 0.3293 0.3323 0.3282 -0.0374 0.0076  0.0574  950  ARG A NH2 
6743  N N   . TYR A 953  ? 0.2681 0.2780 0.2724 -0.0350 0.0113  0.0422  951  TYR A N   
6744  C CA  . TYR A 953  ? 0.2920 0.3095 0.2971 -0.0360 0.0123  0.0414  951  TYR A CA  
6745  C C   . TYR A 953  ? 0.2761 0.3019 0.2790 -0.0356 0.0139  0.0411  951  TYR A C   
6746  O O   . TYR A 953  ? 0.2754 0.3003 0.2761 -0.0333 0.0144  0.0396  951  TYR A O   
6747  C CB  . TYR A 953  ? 0.2689 0.2847 0.2744 -0.0337 0.0125  0.0373  951  TYR A CB  
6748  C CG  . TYR A 953  ? 0.2554 0.2707 0.2586 -0.0300 0.0135  0.0335  951  TYR A CG  
6749  C CD1 . TYR A 953  ? 0.2247 0.2327 0.2268 -0.0277 0.0131  0.0322  951  TYR A CD1 
6750  C CD2 . TYR A 953  ? 0.2874 0.3097 0.2897 -0.0287 0.0149  0.0311  951  TYR A CD2 
6751  C CE1 . TYR A 953  ? 0.2307 0.2382 0.2310 -0.0245 0.0139  0.0290  951  TYR A CE1 
6752  C CE2 . TYR A 953  ? 0.2611 0.2825 0.2617 -0.0254 0.0155  0.0277  951  TYR A CE2 
6753  C CZ  . TYR A 953  ? 0.2574 0.2712 0.2570 -0.0234 0.0150  0.0268  951  TYR A CZ  
6754  O OH  . TYR A 953  ? 0.2589 0.2717 0.2569 -0.0203 0.0156  0.0237  951  TYR A OH  
6755  N N   . ARG A 954  ? 0.2893 0.3234 0.2930 -0.0379 0.0147  0.0424  952  ARG A N   
6756  C CA  . ARG A 954  ? 0.3166 0.3597 0.3185 -0.0372 0.0163  0.0413  952  ARG A CA  
6757  C C   . ARG A 954  ? 0.3018 0.3469 0.3033 -0.0339 0.0172  0.0362  952  ARG A C   
6758  O O   . ARG A 954  ? 0.3413 0.3847 0.3445 -0.0335 0.0169  0.0345  952  ARG A O   
6759  C CB  . ARG A 954  ? 0.3246 0.3768 0.3276 -0.0408 0.0168  0.0446  952  ARG A CB  
6760  C CG  . ARG A 954  ? 0.4211 0.4730 0.4241 -0.0441 0.0160  0.0501  952  ARG A CG  
6761  C CD  . ARG A 954  ? 0.4636 0.5120 0.4639 -0.0423 0.0158  0.0502  952  ARG A CD  
6762  N NE  . ARG A 954  ? 0.5784 0.6341 0.5770 -0.0440 0.0164  0.0533  952  ARG A NE  
6763  C CZ  . ARG A 954  ? 0.6119 0.6683 0.6112 -0.0476 0.0155  0.0587  952  ARG A CZ  
6764  N NH1 . ARG A 954  ? 0.6332 0.6839 0.6353 -0.0500 0.0140  0.0616  952  ARG A NH1 
6765  N NH2 . ARG A 954  ? 0.6204 0.6836 0.6177 -0.0488 0.0161  0.0613  952  ARG A NH2 
6766  N N   . ARG A 955  ? 0.2991 0.3478 0.2984 -0.0315 0.0182  0.0337  953  ARG A N   
6767  C CA  . ARG A 955  ? 0.3059 0.3556 0.3048 -0.0281 0.0188  0.0288  953  ARG A CA  
6768  C C   . ARG A 955  ? 0.3444 0.3998 0.3454 -0.0287 0.0192  0.0276  953  ARG A C   
6769  O O   . ARG A 955  ? 0.3493 0.4013 0.3512 -0.0269 0.0188  0.0249  953  ARG A O   
6770  C CB  . ARG A 955  ? 0.3683 0.4232 0.3651 -0.0260 0.0197  0.0265  953  ARG A CB  
6771  C CG  . ARG A 955  ? 0.4656 0.5222 0.4623 -0.0225 0.0201  0.0214  953  ARG A CG  
6772  C CD  . ARG A 955  ? 0.4876 0.5347 0.4848 -0.0205 0.0193  0.0196  953  ARG A CD  
6773  N NE  . ARG A 955  ? 0.5737 0.6208 0.5709 -0.0171 0.0193  0.0152  953  ARG A NE  
6774  C CZ  . ARG A 955  ? 0.5844 0.6324 0.5831 -0.0162 0.0192  0.0133  953  ARG A CZ  
6775  N NH1 . ARG A 955  ? 0.5548 0.6050 0.5552 -0.0186 0.0191  0.0152  953  ARG A NH1 
6776  N NH2 . ARG A 955  ? 0.5406 0.5872 0.5392 -0.0129 0.0190  0.0095  953  ARG A NH2 
6777  N N   . ASP A 956  ? 0.3149 0.3792 0.3166 -0.0314 0.0199  0.0297  954  ASP A N   
6778  C CA  . ASP A 956  ? 0.3107 0.3814 0.3145 -0.0319 0.0204  0.0283  954  ASP A CA  
6779  C C   . ASP A 956  ? 0.3347 0.4001 0.3410 -0.0335 0.0193  0.0294  954  ASP A C   
6780  O O   . ASP A 956  ? 0.3800 0.4492 0.3882 -0.0333 0.0195  0.0276  954  ASP A O   
6781  C CB  . ASP A 956  ? 0.3381 0.4202 0.3422 -0.0347 0.0215  0.0306  954  ASP A CB  
6782  C CG  . ASP A 956  ? 0.4174 0.5066 0.4193 -0.0327 0.0226  0.0285  954  ASP A CG  
6783  O OD1 . ASP A 956  ? 0.4167 0.5028 0.4173 -0.0289 0.0226  0.0244  954  ASP A OD1 
6784  O OD2 . ASP A 956  ? 0.4722 0.5703 0.4736 -0.0350 0.0235  0.0309  954  ASP A OD2 
6785  N N   . ASP A 957  ? 0.2794 0.3363 0.2860 -0.0348 0.0181  0.0321  955  ASP A N   
6786  C CA  . ASP A 957  ? 0.3087 0.3601 0.3176 -0.0362 0.0168  0.0328  955  ASP A CA  
6787  C C   . ASP A 957  ? 0.2789 0.3219 0.2874 -0.0328 0.0160  0.0295  955  ASP A C   
6788  O O   . ASP A 957  ? 0.2730 0.3102 0.2831 -0.0336 0.0148  0.0299  955  ASP A O   
6789  C CB  . ASP A 957  ? 0.3249 0.3720 0.3349 -0.0396 0.0156  0.0376  955  ASP A CB  
6790  C CG  . ASP A 957  ? 0.3774 0.4327 0.3886 -0.0436 0.0161  0.0416  955  ASP A CG  
6791  O OD1 . ASP A 957  ? 0.4173 0.4814 0.4294 -0.0443 0.0171  0.0406  955  ASP A OD1 
6792  O OD2 . ASP A 957  ? 0.4326 0.4856 0.4439 -0.0462 0.0153  0.0458  955  ASP A OD2 
6793  N N   . LEU A 958  ? 0.2919 0.3340 0.2982 -0.0293 0.0167  0.0263  956  LEU A N   
6794  C CA  . LEU A 958  ? 0.2742 0.3086 0.2798 -0.0262 0.0160  0.0235  956  LEU A CA  
6795  C C   . LEU A 958  ? 0.2664 0.3005 0.2740 -0.0260 0.0154  0.0218  956  LEU A C   
6796  O O   . LEU A 958  ? 0.2709 0.2980 0.2790 -0.0256 0.0143  0.0216  956  LEU A O   
6797  C CB  . LEU A 958  ? 0.2555 0.2906 0.2590 -0.0227 0.0168  0.0202  956  LEU A CB  
6798  C CG  . LEU A 958  ? 0.2981 0.3258 0.3007 -0.0195 0.0162  0.0175  956  LEU A CG  
6799  C CD1 . LEU A 958  ? 0.2946 0.3137 0.2967 -0.0200 0.0153  0.0193  956  LEU A CD1 
6800  C CD2 . LEU A 958  ? 0.3164 0.3451 0.3171 -0.0164 0.0168  0.0147  956  LEU A CD2 
6801  N N   . ASP A 959  ? 0.2813 0.3234 0.2901 -0.0262 0.0161  0.0205  957  ASP A N   
6802  C CA  . ASP A 959  ? 0.3071 0.3493 0.3178 -0.0257 0.0154  0.0186  957  ASP A CA  
6803  C C   . ASP A 959  ? 0.2903 0.3296 0.3033 -0.0289 0.0143  0.0211  957  ASP A C   
6804  O O   . ASP A 959  ? 0.3011 0.3354 0.3150 -0.0280 0.0132  0.0198  957  ASP A O   
6805  C CB  . ASP A 959  ? 0.3014 0.3534 0.3132 -0.0252 0.0163  0.0166  957  ASP A CB  
6806  C CG  . ASP A 959  ? 0.3314 0.3830 0.3446 -0.0234 0.0156  0.0137  957  ASP A CG  
6807  O OD1 . ASP A 959  ? 0.3358 0.3813 0.3475 -0.0203 0.0151  0.0114  957  ASP A OD1 
6808  O OD2 . ASP A 959  ? 0.3676 0.4248 0.3833 -0.0252 0.0156  0.0138  957  ASP A OD2 
6809  N N   . ARG A 960  ? 0.2894 0.3318 0.3037 -0.0326 0.0143  0.0248  958  ARG A N   
6810  C CA  . ARG A 960  ? 0.2761 0.3148 0.2929 -0.0358 0.0129  0.0275  958  ARG A CA  
6811  C C   . ARG A 960  ? 0.2979 0.3262 0.3138 -0.0347 0.0116  0.0277  958  ARG A C   
6812  O O   . ARG A 960  ? 0.3270 0.3503 0.3447 -0.0355 0.0101  0.0277  958  ARG A O   
6813  C CB  . ARG A 960  ? 0.3023 0.3460 0.3205 -0.0400 0.0131  0.0319  958  ARG A CB  
6814  N N   . LEU A 961  ? 0.2745 0.2995 0.2877 -0.0329 0.0121  0.0277  959  LEU A N   
6815  C CA  . LEU A 961  ? 0.2808 0.2964 0.2931 -0.0317 0.0110  0.0278  959  LEU A CA  
6816  C C   . LEU A 961  ? 0.2681 0.2794 0.2802 -0.0288 0.0105  0.0243  959  LEU A C   
6817  O O   . LEU A 961  ? 0.2903 0.2956 0.3033 -0.0290 0.0091  0.0242  959  LEU A O   
6818  C CB  . LEU A 961  ? 0.2755 0.2896 0.2851 -0.0302 0.0118  0.0282  959  LEU A CB  
6819  C CG  . LEU A 961  ? 0.2336 0.2387 0.2421 -0.0284 0.0109  0.0277  959  LEU A CG  
6820  C CD1 . LEU A 961  ? 0.2933 0.2937 0.3039 -0.0310 0.0093  0.0305  959  LEU A CD1 
6821  C CD2 . LEU A 961  ? 0.2980 0.3024 0.3039 -0.0268 0.0118  0.0278  959  LEU A CD2 
6822  N N   . VAL A 962  ? 0.2568 0.2712 0.2674 -0.0261 0.0115  0.0213  960  VAL A N   
6823  C CA  . VAL A 962  ? 0.2647 0.2758 0.2750 -0.0234 0.0109  0.0182  960  VAL A CA  
6824  C C   . VAL A 962  ? 0.3112 0.3227 0.3242 -0.0251 0.0097  0.0181  960  VAL A C   
6825  O O   . VAL A 962  ? 0.3081 0.3143 0.3214 -0.0241 0.0086  0.0168  960  VAL A O   
6826  C CB  . VAL A 962  ? 0.2868 0.3018 0.2956 -0.0205 0.0120  0.0154  960  VAL A CB  
6827  C CG1 . VAL A 962  ? 0.3107 0.3230 0.3193 -0.0179 0.0113  0.0125  960  VAL A CG1 
6828  C CG2 . VAL A 962  ? 0.2476 0.2608 0.2538 -0.0187 0.0129  0.0153  960  VAL A CG2 
6829  N N   . ASP A 963  ? 0.2936 0.3118 0.3090 -0.0278 0.0099  0.0194  961  ASP A N   
6830  C CA  . ASP A 963  ? 0.3188 0.3378 0.3373 -0.0301 0.0087  0.0197  961  ASP A CA  
6831  C C   . ASP A 963  ? 0.3506 0.3623 0.3704 -0.0319 0.0070  0.0214  961  ASP A C   
6832  O O   . ASP A 963  ? 0.3723 0.3805 0.3935 -0.0317 0.0056  0.0200  961  ASP A O   
6833  C CB  . ASP A 963  ? 0.3549 0.3824 0.3757 -0.0334 0.0093  0.0216  961  ASP A CB  
6834  C CG  . ASP A 963  ? 0.4151 0.4502 0.4360 -0.0318 0.0103  0.0191  961  ASP A CG  
6835  O OD1 . ASP A 963  ? 0.4440 0.4773 0.4635 -0.0283 0.0103  0.0158  961  ASP A OD1 
6836  O OD2 . ASP A 963  ? 0.4665 0.5098 0.4889 -0.0340 0.0112  0.0204  961  ASP A OD2 
6837  N N   . ASP A 964  ? 0.3321 0.3417 0.3515 -0.0336 0.0070  0.0245  962  ASP A N   
6838  C CA  . ASP A 964  ? 0.3765 0.3791 0.3973 -0.0351 0.0053  0.0263  962  ASP A CA  
6839  C C   . ASP A 964  ? 0.3639 0.3591 0.3831 -0.0319 0.0046  0.0237  962  ASP A C   
6840  O O   . ASP A 964  ? 0.3620 0.3520 0.3829 -0.0323 0.0028  0.0232  962  ASP A O   
6841  C CB  . ASP A 964  ? 0.3609 0.3632 0.3815 -0.0372 0.0055  0.0301  962  ASP A CB  
6842  C CG  . ASP A 964  ? 0.4232 0.4328 0.4457 -0.0410 0.0059  0.0333  962  ASP A CG  
6843  O OD1 . ASP A 964  ? 0.4455 0.4597 0.4703 -0.0425 0.0058  0.0326  962  ASP A OD1 
6844  O OD2 . ASP A 964  ? 0.5102 0.5212 0.5320 -0.0426 0.0064  0.0364  962  ASP A OD2 
6845  N N   . VAL A 965  ? 0.2957 0.2903 0.3117 -0.0287 0.0059  0.0221  963  VAL A N   
6846  C CA  . VAL A 965  ? 0.3625 0.3509 0.3767 -0.0256 0.0054  0.0197  963  VAL A CA  
6847  C C   . VAL A 965  ? 0.3664 0.3547 0.3815 -0.0245 0.0046  0.0169  963  VAL A C   
6848  O O   . VAL A 965  ? 0.3581 0.3413 0.3736 -0.0237 0.0032  0.0156  963  VAL A O   
6849  C CB  . VAL A 965  ? 0.3374 0.3260 0.3483 -0.0227 0.0070  0.0186  963  VAL A CB  
6850  C CG1 . VAL A 965  ? 0.2893 0.2727 0.2984 -0.0196 0.0067  0.0162  963  VAL A CG1 
6851  C CG2 . VAL A 965  ? 0.3030 0.2910 0.3130 -0.0237 0.0076  0.0212  963  VAL A CG2 
6852  N N   . ASN A 966  ? 0.3135 0.3077 0.3288 -0.0242 0.0053  0.0156  964  ASN A N   
6853  C CA  . ASN A 966  ? 0.3027 0.2974 0.3187 -0.0230 0.0044  0.0129  964  ASN A CA  
6854  C C   . ASN A 966  ? 0.3266 0.3199 0.3460 -0.0257 0.0025  0.0135  964  ASN A C   
6855  O O   . ASN A 966  ? 0.3148 0.3054 0.3348 -0.0245 0.0012  0.0112  964  ASN A O   
6856  C CB  . ASN A 966  ? 0.3165 0.3183 0.3326 -0.0223 0.0054  0.0116  964  ASN A CB  
6857  C CG  . ASN A 966  ? 0.2891 0.2914 0.3020 -0.0189 0.0068  0.0102  964  ASN A CG  
6858  O OD1 . ASN A 966  ? 0.2943 0.2914 0.3049 -0.0167 0.0068  0.0094  964  ASN A OD1 
6859  N ND2 . ASN A 966  ? 0.3195 0.3282 0.3325 -0.0186 0.0078  0.0097  964  ASN A ND2 
6860  N N   . ALA A 967  ? 0.2890 0.2840 0.3109 -0.0293 0.0022  0.0165  965  ALA A N   
6861  C CA  . ALA A 967  ? 0.3785 0.3728 0.4043 -0.0324 0.0003  0.0173  965  ALA A CA  
6862  C C   . ALA A 967  ? 0.3586 0.3449 0.3851 -0.0320 -0.0016 0.0167  965  ALA A C   
6863  O O   . ALA A 967  ? 0.4130 0.3979 0.4427 -0.0339 -0.0036 0.0164  965  ALA A O   
6864  C CB  . ALA A 967  ? 0.3812 0.3792 0.4092 -0.0365 0.0005  0.0213  965  ALA A CB  
6865  N N   . THR A 968  ? 0.3847 0.3660 0.4086 -0.0296 -0.0013 0.0163  966  THR A N   
6866  C CA  . THR A 968  ? 0.3434 0.3177 0.3679 -0.0287 -0.0032 0.0150  966  THR A CA  
6867  C C   . THR A 968  ? 0.3749 0.3487 0.3995 -0.0267 -0.0042 0.0113  966  THR A C   
6868  O O   . THR A 968  ? 0.4155 0.3846 0.4416 -0.0265 -0.0062 0.0098  966  THR A O   
6869  C CB  . THR A 968  ? 0.3939 0.3639 0.4154 -0.0261 -0.0024 0.0149  966  THR A CB  
6870  O OG1 . THR A 968  ? 0.4010 0.3724 0.4191 -0.0227 -0.0009 0.0125  966  THR A OG1 
6871  C CG2 . THR A 968  ? 0.3905 0.3614 0.4115 -0.0277 -0.0014 0.0185  966  THR A CG2 
6872  N N   . GLY A 969  ? 0.3771 0.3556 0.4001 -0.0250 -0.0030 0.0095  967  GLY A N   
6873  C CA  . GLY A 969  ? 0.3642 0.3424 0.3866 -0.0227 -0.0038 0.0060  967  GLY A CA  
6874  C C   . GLY A 969  ? 0.3359 0.3107 0.3545 -0.0189 -0.0032 0.0041  967  GLY A C   
6875  O O   . GLY A 969  ? 0.3373 0.3126 0.3545 -0.0166 -0.0035 0.0014  967  GLY A O   
6876  N N   . TYR A 970  ? 0.3058 0.2773 0.3226 -0.0182 -0.0024 0.0055  968  TYR A N   
6877  C CA  . TYR A 970  ? 0.3490 0.3179 0.3623 -0.0148 -0.0015 0.0041  968  TYR A CA  
6878  C C   . TYR A 970  ? 0.3062 0.2788 0.3168 -0.0132 0.0005  0.0043  968  TYR A C   
6879  O O   . TYR A 970  ? 0.3450 0.3220 0.3563 -0.0146 0.0013  0.0055  968  TYR A O   
6880  C CB  . TYR A 970  ? 0.3065 0.2708 0.3196 -0.0149 -0.0015 0.0055  968  TYR A CB  
6881  C CG  . TYR A 970  ? 0.3823 0.3422 0.3978 -0.0156 -0.0038 0.0047  968  TYR A CG  
6882  C CD1 . TYR A 970  ? 0.3936 0.3507 0.4081 -0.0131 -0.0046 0.0018  968  TYR A CD1 
6883  C CD2 . TYR A 970  ? 0.4069 0.3654 0.4259 -0.0188 -0.0051 0.0068  968  TYR A CD2 
6884  C CE1 . TYR A 970  ? 0.4484 0.4015 0.4654 -0.0135 -0.0069 0.0005  968  TYR A CE1 
6885  C CE2 . TYR A 970  ? 0.4231 0.3771 0.4447 -0.0194 -0.0075 0.0058  968  TYR A CE2 
6886  C CZ  . TYR A 970  ? 0.5049 0.4562 0.5256 -0.0166 -0.0084 0.0025  968  TYR A CZ  
6887  O OH  . TYR A 970  ? 0.5634 0.5102 0.5869 -0.0169 -0.0109 0.0011  968  TYR A OH  
6888  N N   . GLY A 971  ? 0.2850 0.2559 0.2925 -0.0102 0.0013  0.0031  969  GLY A N   
6889  C CA  . GLY A 971  ? 0.2905 0.2640 0.2955 -0.0086 0.0029  0.0032  969  GLY A CA  
6890  C C   . GLY A 971  ? 0.2839 0.2547 0.2857 -0.0057 0.0036  0.0024  969  GLY A C   
6891  O O   . GLY A 971  ? 0.2837 0.2558 0.2837 -0.0036 0.0038  0.0011  969  GLY A O   
6892  N N   . LEU A 972  ? 0.2895 0.2567 0.2907 -0.0056 0.0039  0.0032  970  LEU A N   
6893  C CA  . LEU A 972  ? 0.2575 0.2224 0.2559 -0.0030 0.0045  0.0025  970  LEU A CA  
6894  C C   . LEU A 972  ? 0.2805 0.2458 0.2771 -0.0024 0.0062  0.0040  970  LEU A C   
6895  O O   . LEU A 972  ? 0.2658 0.2330 0.2610 -0.0011 0.0069  0.0037  970  LEU A O   
6896  C CB  . LEU A 972  ? 0.2785 0.2397 0.2774 -0.0029 0.0037  0.0020  970  LEU A CB  
6897  C CG  . LEU A 972  ? 0.2818 0.2414 0.2780 -0.0003 0.0042  0.0009  970  LEU A CG  
6898  C CD1 . LEU A 972  ? 0.2885 0.2502 0.2829 0.0016  0.0041  -0.0008 970  LEU A CD1 
6899  C CD2 . LEU A 972  ? 0.3406 0.2972 0.3380 -0.0001 0.0030  -0.0002 970  LEU A CD2 
6900  N N   . THR A 973  ? 0.2905 0.2539 0.2875 -0.0033 0.0066  0.0055  971  THR A N   
6901  C CA  . THR A 973  ? 0.2262 0.1898 0.2217 -0.0029 0.0080  0.0068  971  THR A CA  
6902  C C   . THR A 973  ? 0.2153 0.1811 0.2124 -0.0051 0.0083  0.0085  971  THR A C   
6903  O O   . THR A 973  ? 0.2246 0.1903 0.2239 -0.0072 0.0075  0.0093  971  THR A O   
6904  C CB  . THR A 973  ? 0.2308 0.1913 0.2252 -0.0020 0.0085  0.0072  971  THR A CB  
6905  O OG1 . THR A 973  ? 0.2683 0.2268 0.2647 -0.0034 0.0076  0.0078  971  THR A OG1 
6906  C CG2 . THR A 973  ? 0.2535 0.2128 0.2461 0.0002  0.0084  0.0057  971  THR A CG2 
6907  N N   . PHE A 974  ? 0.2089 0.1766 0.2050 -0.0047 0.0095  0.0090  972  PHE A N   
6908  C CA  . PHE A 974  ? 0.2155 0.1861 0.2126 -0.0065 0.0099  0.0104  972  PHE A CA  
6909  C C   . PHE A 974  ? 0.2026 0.1730 0.1981 -0.0055 0.0110  0.0108  972  PHE A C   
6910  O O   . PHE A 974  ? 0.2144 0.1845 0.2085 -0.0035 0.0115  0.0098  972  PHE A O   
6911  C CB  . PHE A 974  ? 0.2034 0.1787 0.2016 -0.0071 0.0098  0.0097  972  PHE A CB  
6912  C CG  . PHE A 974  ? 0.2026 0.1818 0.2015 -0.0087 0.0105  0.0110  972  PHE A CG  
6913  C CD1 . PHE A 974  ? 0.2035 0.1837 0.2041 -0.0113 0.0102  0.0129  972  PHE A CD1 
6914  C CD2 . PHE A 974  ? 0.2326 0.2144 0.2304 -0.0074 0.0114  0.0103  972  PHE A CD2 
6915  C CE1 . PHE A 974  ? 0.2420 0.2263 0.2431 -0.0128 0.0109  0.0142  972  PHE A CE1 
6916  C CE2 . PHE A 974  ? 0.2161 0.2022 0.2145 -0.0087 0.0121  0.0112  972  PHE A CE2 
6917  C CZ  . PHE A 974  ? 0.2731 0.2607 0.2729 -0.0114 0.0119  0.0132  972  PHE A CZ  
6918  N N   . GLY A 975  ? 0.2222 0.1931 0.2181 -0.0069 0.0114  0.0124  973  GLY A N   
6919  C CA  . GLY A 975  ? 0.2157 0.1868 0.2105 -0.0061 0.0123  0.0127  973  GLY A CA  
6920  C C   . GLY A 975  ? 0.2086 0.1843 0.2039 -0.0073 0.0128  0.0134  973  GLY A C   
6921  O O   . GLY A 975  ? 0.2066 0.1846 0.2032 -0.0094 0.0125  0.0146  973  GLY A O   
6922  N N   . LEU A 976  ? 0.1997 0.1767 0.1939 -0.0061 0.0135  0.0125  974  LEU A N   
6923  C CA  . LEU A 976  ? 0.1992 0.1809 0.1937 -0.0069 0.0140  0.0127  974  LEU A CA  
6924  C C   . LEU A 976  ? 0.2243 0.2050 0.2177 -0.0059 0.0145  0.0126  974  LEU A C   
6925  O O   . LEU A 976  ? 0.1985 0.1768 0.1910 -0.0041 0.0146  0.0114  974  LEU A O   
6926  C CB  . LEU A 976  ? 0.2360 0.2220 0.2309 -0.0061 0.0141  0.0110  974  LEU A CB  
6927  C CG  . LEU A 976  ? 0.2505 0.2421 0.2456 -0.0064 0.0147  0.0105  974  LEU A CG  
6928  C CD1 . LEU A 976  ? 0.2429 0.2385 0.2390 -0.0091 0.0148  0.0126  974  LEU A CD1 
6929  C CD2 . LEU A 976  ? 0.2096 0.2046 0.2051 -0.0048 0.0146  0.0082  974  LEU A CD2 
6930  N N   . HIS A 977  ? 0.2299 0.2124 0.2234 -0.0073 0.0148  0.0140  975  HIS A N   
6931  C CA  . HIS A 977  ? 0.2113 0.1937 0.2039 -0.0067 0.0152  0.0138  975  HIS A CA  
6932  C C   . HIS A 977  ? 0.2180 0.2064 0.2107 -0.0071 0.0155  0.0132  975  HIS A C   
6933  O O   . HIS A 977  ? 0.2063 0.1984 0.1994 -0.0090 0.0156  0.0148  975  HIS A O   
6934  C CB  . HIS A 977  ? 0.2268 0.2066 0.2193 -0.0077 0.0150  0.0158  975  HIS A CB  
6935  C CG  . HIS A 977  ? 0.2445 0.2191 0.2366 -0.0065 0.0149  0.0155  975  HIS A CG  
6936  N ND1 . HIS A 977  ? 0.3075 0.2806 0.2990 -0.0056 0.0152  0.0152  975  HIS A ND1 
6937  C CD2 . HIS A 977  ? 0.2915 0.2624 0.2837 -0.0060 0.0146  0.0155  975  HIS A CD2 
6938  C CE1 . HIS A 977  ? 0.2812 0.2502 0.2725 -0.0047 0.0151  0.0152  975  HIS A CE1 
6939  N NE2 . HIS A 977  ? 0.2733 0.2410 0.2649 -0.0049 0.0148  0.0153  975  HIS A NE2 
6940  N N   . THR A 978  ? 0.2060 0.1956 0.1983 -0.0052 0.0157  0.0109  976  THR A N   
6941  C CA  . THR A 978  ? 0.2208 0.2164 0.2132 -0.0051 0.0160  0.0096  976  THR A CA  
6942  C C   . THR A 978  ? 0.2195 0.2138 0.2116 -0.0027 0.0158  0.0071  976  THR A C   
6943  O O   . THR A 978  ? 0.2351 0.2249 0.2272 -0.0013 0.0155  0.0064  976  THR A O   
6944  C CB  . THR A 978  ? 0.2332 0.2340 0.2265 -0.0056 0.0161  0.0091  976  THR A CB  
6945  O OG1 . THR A 978  ? 0.2252 0.2324 0.2186 -0.0052 0.0165  0.0075  976  THR A OG1 
6946  C CG2 . THR A 978  ? 0.2480 0.2466 0.2417 -0.0038 0.0157  0.0073  976  THR A CG2 
6947  N N   . ARG A 979  ? 0.2460 0.2444 0.2380 -0.0023 0.0160  0.0058  977  ARG A N   
6948  C CA  . ARG A 979  ? 0.2934 0.2911 0.2855 0.0000  0.0156  0.0030  977  ARG A CA  
6949  C C   . ARG A 979  ? 0.2625 0.2654 0.2554 0.0013  0.0154  0.0004  977  ARG A C   
6950  O O   . ARG A 979  ? 0.2783 0.2809 0.2717 0.0034  0.0148  -0.0022 977  ARG A O   
6951  C CB  . ARG A 979  ? 0.3190 0.3174 0.3107 -0.0001 0.0155  0.0026  977  ARG A CB  
6952  C CG  . ARG A 979  ? 0.3851 0.3783 0.3763 -0.0010 0.0155  0.0048  977  ARG A CG  
6953  C CD  . ARG A 979  ? 0.4550 0.4480 0.4460 -0.0006 0.0153  0.0040  977  ARG A CD  
6954  N NE  . ARG A 979  ? 0.5050 0.5017 0.4954 -0.0023 0.0156  0.0055  977  ARG A NE  
6955  C CZ  . ARG A 979  ? 0.5238 0.5215 0.5139 -0.0023 0.0154  0.0051  977  ARG A CZ  
6956  N NH1 . ARG A 979  ? 0.4807 0.4761 0.4714 -0.0008 0.0149  0.0029  977  ARG A NH1 
6957  N NH2 . ARG A 979  ? 0.6024 0.6036 0.5918 -0.0038 0.0156  0.0069  977  ARG A NH2 
6958  N N   . LEU A 980  ? 0.2139 0.2214 0.2072 0.0001  0.0158  0.0011  978  LEU A N   
6959  C CA  . LEU A 980  ? 0.2326 0.2468 0.2267 0.0011  0.0159  -0.0013 978  LEU A CA  
6960  C C   . LEU A 980  ? 0.2391 0.2521 0.2342 0.0023  0.0154  -0.0022 978  LEU A C   
6961  O O   . LEU A 980  ? 0.2289 0.2409 0.2242 0.0008  0.0156  -0.0003 978  LEU A O   
6962  C CB  . LEU A 980  ? 0.2345 0.2560 0.2287 -0.0012 0.0167  0.0002  978  LEU A CB  
6963  C CG  . LEU A 980  ? 0.2598 0.2828 0.2529 -0.0026 0.0171  0.0016  978  LEU A CG  
6964  C CD1 . LEU A 980  ? 0.2686 0.2990 0.2617 -0.0051 0.0179  0.0037  978  LEU A CD1 
6965  C CD2 . LEU A 980  ? 0.2715 0.2961 0.2644 -0.0004 0.0168  -0.0015 978  LEU A CD2 
6966  N N   . ASP A 981  ? 0.2405 0.2535 0.2362 0.0049  0.0147  -0.0052 979  ASP A N   
6967  C CA  . ASP A 981  ? 0.2318 0.2434 0.2283 0.0063  0.0141  -0.0062 979  ASP A CA  
6968  C C   . ASP A 981  ? 0.2032 0.2212 0.2007 0.0052  0.0145  -0.0059 979  ASP A C   
6969  O O   . ASP A 981  ? 0.2499 0.2663 0.2478 0.0051  0.0142  -0.0053 979  ASP A O   
6970  C CB  . ASP A 981  ? 0.2707 0.2820 0.2681 0.0095  0.0130  -0.0095 979  ASP A CB  
6971  C CG  . ASP A 981  ? 0.2767 0.2806 0.2735 0.0106  0.0122  -0.0095 979  ASP A CG  
6972  O OD1 . ASP A 981  ? 0.3065 0.3053 0.3022 0.0092  0.0126  -0.0069 979  ASP A OD1 
6973  O OD2 . ASP A 981  ? 0.3333 0.3366 0.3309 0.0129  0.0113  -0.0121 979  ASP A OD2 
6974  N N   . GLU A 982  ? 0.2156 0.2413 0.2136 0.0043  0.0153  -0.0065 980  GLU A N   
6975  C CA  . GLU A 982  ? 0.2406 0.2729 0.2397 0.0028  0.0158  -0.0061 980  GLU A CA  
6976  C C   . GLU A 982  ? 0.2489 0.2787 0.2478 -0.0002 0.0161  -0.0025 980  GLU A C   
6977  O O   . GLU A 982  ? 0.2369 0.2681 0.2369 -0.0009 0.0160  -0.0020 980  GLU A O   
6978  C CB  . GLU A 982  ? 0.2618 0.3033 0.2611 0.0021  0.0166  -0.0069 980  GLU A CB  
6979  C CG  . GLU A 982  ? 0.2960 0.3451 0.2968 0.0002  0.0173  -0.0061 980  GLU A CG  
6980  C CD  . GLU A 982  ? 0.3521 0.4104 0.3528 -0.0016 0.0184  -0.0055 980  GLU A CD  
6981  O OE1 . GLU A 982  ? 0.4287 0.4860 0.4280 -0.0032 0.0188  -0.0034 980  GLU A OE1 
6982  O OE2 . GLU A 982  ? 0.2710 0.3379 0.2731 -0.0013 0.0188  -0.0072 980  GLU A OE2 
6983  N N   . THR A 983  ? 0.2354 0.2612 0.2331 -0.0018 0.0164  0.0000  981  THR A N   
6984  C CA  . THR A 983  ? 0.2485 0.2713 0.2462 -0.0044 0.0164  0.0032  981  THR A CA  
6985  C C   . THR A 983  ? 0.2043 0.2199 0.2019 -0.0033 0.0157  0.0032  981  THR A C   
6986  O O   . THR A 983  ? 0.2319 0.2469 0.2303 -0.0047 0.0154  0.0044  981  THR A O   
6987  C CB  . THR A 983  ? 0.2778 0.2985 0.2744 -0.0060 0.0168  0.0056  981  THR A CB  
6988  O OG1 . THR A 983  ? 0.2532 0.2813 0.2498 -0.0072 0.0175  0.0059  981  THR A OG1 
6989  C CG2 . THR A 983  ? 0.2612 0.2779 0.2580 -0.0085 0.0165  0.0088  981  THR A CG2 
6990  N N   . ILE A 984  ? 0.2050 0.2156 0.2017 -0.0010 0.0152  0.0018  982  ILE A N   
6991  C CA  . ILE A 984  ? 0.2494 0.2541 0.2458 0.0002  0.0145  0.0017  982  ILE A CA  
6992  C C   . ILE A 984  ? 0.2331 0.2406 0.2306 0.0010  0.0140  0.0003  982  ILE A C   
6993  O O   . ILE A 984  ? 0.2163 0.2218 0.2141 0.0004  0.0136  0.0012  982  ILE A O   
6994  C CB  . ILE A 984  ? 0.2310 0.2307 0.2263 0.0025  0.0141  0.0006  982  ILE A CB  
6995  C CG1 . ILE A 984  ? 0.2255 0.2221 0.2198 0.0015  0.0145  0.0022  982  ILE A CG1 
6996  C CG2 . ILE A 984  ? 0.2298 0.2244 0.2247 0.0038  0.0134  0.0006  982  ILE A CG2 
6997  C CD1 . ILE A 984  ? 0.2771 0.2692 0.2707 0.0034  0.0141  0.0012  982  ILE A CD1 
6998  N N   . ALA A 985  ? 0.2158 0.2283 0.2142 0.0027  0.0139  -0.0021 983  ALA A N   
6999  C CA  . ALA A 985  ? 0.2470 0.2627 0.2467 0.0038  0.0134  -0.0037 983  ALA A CA  
7000  C C   . ALA A 985  ? 0.2611 0.2812 0.2621 0.0011  0.0137  -0.0023 983  ALA A C   
7001  O O   . ALA A 985  ? 0.2524 0.2715 0.2541 0.0009  0.0132  -0.0022 983  ALA A O   
7002  C CB  . ALA A 985  ? 0.2375 0.2584 0.2382 0.0061  0.0132  -0.0068 983  ALA A CB  
7003  N N   . HIS A 986  ? 0.2437 0.2685 0.2451 -0.0012 0.0146  -0.0010 984  HIS A N   
7004  C CA  . HIS A 986  ? 0.2651 0.2942 0.2679 -0.0042 0.0150  0.0008  984  HIS A CA  
7005  C C   . HIS A 986  ? 0.2692 0.2922 0.2719 -0.0058 0.0144  0.0030  984  HIS A C   
7006  O O   . HIS A 986  ? 0.2868 0.3104 0.2908 -0.0065 0.0138  0.0030  984  HIS A O   
7007  C CB  . HIS A 986  ? 0.2861 0.3206 0.2889 -0.0064 0.0160  0.0023  984  HIS A CB  
7008  C CG  . HIS A 986  ? 0.2834 0.3214 0.2877 -0.0100 0.0162  0.0050  984  HIS A CG  
7009  N ND1 . HIS A 986  ? 0.3463 0.3877 0.3504 -0.0127 0.0170  0.0075  984  HIS A ND1 
7010  C CD2 . HIS A 986  ? 0.2844 0.3233 0.2905 -0.0115 0.0157  0.0056  984  HIS A CD2 
7011  C CE1 . HIS A 986  ? 0.3725 0.4164 0.3784 -0.0157 0.0169  0.0098  984  HIS A CE1 
7012  N NE2 . HIS A 986  ? 0.3396 0.3820 0.3468 -0.0151 0.0161  0.0086  984  HIS A NE2 
7013  N N   . VAL A 987  ? 0.2312 0.2486 0.2325 -0.0064 0.0145  0.0047  985  VAL A N   
7014  C CA  . VAL A 987  ? 0.2493 0.2613 0.2505 -0.0080 0.0140  0.0068  985  VAL A CA  
7015  C C   . VAL A 987  ? 0.2586 0.2662 0.2596 -0.0062 0.0131  0.0054  985  VAL A C   
7016  O O   . VAL A 987  ? 0.2605 0.2673 0.2626 -0.0073 0.0124  0.0059  985  VAL A O   
7017  C CB  . VAL A 987  ? 0.2307 0.2382 0.2306 -0.0087 0.0143  0.0086  985  VAL A CB  
7018  C CG1 . VAL A 987  ? 0.2213 0.2229 0.2213 -0.0098 0.0135  0.0102  985  VAL A CG1 
7019  C CG2 . VAL A 987  ? 0.2451 0.2574 0.2453 -0.0110 0.0150  0.0104  985  VAL A CG2 
7020  N N   . THR A 988  ? 0.2437 0.2484 0.2433 -0.0034 0.0130  0.0038  986  THR A N   
7021  C CA  . THR A 988  ? 0.2672 0.2677 0.2661 -0.0016 0.0121  0.0029  986  THR A CA  
7022  C C   . THR A 988  ? 0.3385 0.3431 0.3389 -0.0009 0.0115  0.0013  986  THR A C   
7023  O O   . THR A 988  ? 0.3499 0.3519 0.3501 -0.0002 0.0107  0.0009  986  THR A O   
7024  C CB  . THR A 988  ? 0.3038 0.3002 0.3010 0.0011  0.0121  0.0020  986  THR A CB  
7025  O OG1 . THR A 988  ? 0.2887 0.2888 0.2862 0.0027  0.0121  0.0001  986  THR A OG1 
7026  C CG2 . THR A 988  ? 0.2994 0.2917 0.2953 0.0004  0.0126  0.0035  986  THR A CG2 
7027  N N   . SER A 989  ? 0.2816 0.2927 0.2833 -0.0011 0.0119  0.0003  987  SER A N   
7028  C CA  . SER A 989  ? 0.3197 0.3351 0.3231 -0.0006 0.0112  -0.0013 987  SER A CA  
7029  C C   . SER A 989  ? 0.3471 0.3648 0.3524 -0.0036 0.0110  0.0001  987  SER A C   
7030  O O   . SER A 989  ? 0.3991 0.4188 0.4057 -0.0034 0.0102  -0.0010 987  SER A O   
7031  C CB  . SER A 989  ? 0.3090 0.3312 0.3135 0.0008  0.0116  -0.0033 987  SER A CB  
7032  O OG  . SER A 989  ? 0.4138 0.4415 0.4193 -0.0016 0.0126  -0.0023 987  SER A OG  
7033  N N   . ARG A 990  ? 0.3023 0.3196 0.3079 -0.0064 0.0115  0.0024  988  ARG A N   
7034  C CA  . ARG A 990  ? 0.3218 0.3411 0.3295 -0.0096 0.0112  0.0040  988  ARG A CA  
7035  C C   . ARG A 990  ? 0.3067 0.3193 0.3141 -0.0107 0.0104  0.0053  988  ARG A C   
7036  O O   . ARG A 990  ? 0.3048 0.3177 0.3141 -0.0124 0.0095  0.0056  988  ARG A O   
7037  C CB  . ARG A 990  ? 0.2882 0.3124 0.2968 -0.0124 0.0122  0.0059  988  ARG A CB  
7038  C CG  . ARG A 990  ? 0.3641 0.3960 0.3731 -0.0114 0.0131  0.0044  988  ARG A CG  
7039  C CD  . ARG A 990  ? 0.4300 0.4687 0.4417 -0.0122 0.0128  0.0034  988  ARG A CD  
7040  N NE  . ARG A 990  ? 0.4049 0.4500 0.4184 -0.0157 0.0135  0.0056  988  ARG A NE  
7041  C CZ  . ARG A 990  ? 0.3660 0.4178 0.3822 -0.0175 0.0135  0.0055  988  ARG A CZ  
7042  N NH1 . ARG A 990  ? 0.3832 0.4361 0.4008 -0.0161 0.0126  0.0033  988  ARG A NH1 
7043  N NH2 . ARG A 990  ? 0.3064 0.3644 0.3240 -0.0209 0.0142  0.0079  988  ARG A NH2 
7044  N N   . ILE A 991  ? 0.2818 0.2885 0.2871 -0.0097 0.0106  0.0060  989  ILE A N   
7045  C CA  . ILE A 991  ? 0.2475 0.2481 0.2525 -0.0104 0.0098  0.0069  989  ILE A CA  
7046  C C   . ILE A 991  ? 0.2701 0.2686 0.2749 -0.0087 0.0087  0.0050  989  ILE A C   
7047  O O   . ILE A 991  ? 0.3100 0.3091 0.3136 -0.0061 0.0087  0.0033  989  ILE A O   
7048  C CB  . ILE A 991  ? 0.2841 0.2797 0.2869 -0.0094 0.0103  0.0078  989  ILE A CB  
7049  C CG1 . ILE A 991  ? 0.2737 0.2640 0.2767 -0.0107 0.0096  0.0091  989  ILE A CG1 
7050  C CG2 . ILE A 991  ? 0.2841 0.2774 0.2847 -0.0061 0.0105  0.0060  989  ILE A CG2 
7051  C CD1 . ILE A 991  ? 0.3035 0.2954 0.3087 -0.0140 0.0092  0.0113  989  ILE A CD1 
7052  N N   . LYS A 992  ? 0.2408 0.2367 0.2468 -0.0101 0.0076  0.0054  990  LYS A N   
7053  C CA  . LYS A 992  ? 0.2691 0.2632 0.2749 -0.0085 0.0065  0.0035  990  LYS A CA  
7054  C C   . LYS A 992  ? 0.2995 0.2872 0.3038 -0.0078 0.0061  0.0037  990  LYS A C   
7055  O O   . LYS A 992  ? 0.3543 0.3396 0.3600 -0.0094 0.0051  0.0042  990  LYS A O   
7056  C CB  . LYS A 992  ? 0.2960 0.2932 0.3047 -0.0106 0.0054  0.0031  990  LYS A CB  
7057  N N   . ALA A 993  ? 0.2779 0.2629 0.2794 -0.0054 0.0067  0.0034  991  ALA A N   
7058  C CA  . ALA A 993  ? 0.2585 0.2382 0.2584 -0.0044 0.0066  0.0035  991  ALA A CA  
7059  C C   . ALA A 993  ? 0.2545 0.2330 0.2518 -0.0014 0.0067  0.0023  991  ALA A C   
7060  O O   . ALA A 993  ? 0.2744 0.2550 0.2709 -0.0001 0.0073  0.0020  991  ALA A O   
7061  C CB  . ALA A 993  ? 0.2651 0.2424 0.2645 -0.0053 0.0074  0.0053  991  ALA A CB  
7062  N N   . GLY A 994  ? 0.2232 0.1982 0.2191 -0.0003 0.0062  0.0017  992  GLY A N   
7063  C CA  . GLY A 994  ? 0.2273 0.2013 0.2207 0.0023  0.0063  0.0009  992  GLY A CA  
7064  C C   . GLY A 994  ? 0.2369 0.2088 0.2283 0.0034  0.0075  0.0021  992  GLY A C   
7065  O O   . GLY A 994  ? 0.2233 0.1951 0.2129 0.0053  0.0077  0.0019  992  GLY A O   
7066  N N   . ASN A 995  ? 0.2072 0.1773 0.1990 0.0022  0.0082  0.0033  993  ASN A N   
7067  C CA  . ASN A 995  ? 0.2277 0.1955 0.2178 0.0030  0.0092  0.0044  993  ASN A CA  
7068  C C   . ASN A 995  ? 0.2155 0.1843 0.2068 0.0015  0.0100  0.0056  993  ASN A C   
7069  O O   . ASN A 995  ? 0.2510 0.2192 0.2436 -0.0003 0.0098  0.0064  993  ASN A O   
7070  C CB  . ASN A 995  ? 0.2067 0.1714 0.1958 0.0034  0.0093  0.0045  993  ASN A CB  
7071  C CG  . ASN A 995  ? 0.2418 0.2060 0.2289 0.0055  0.0090  0.0036  993  ASN A CG  
7072  O OD1 . ASN A 995  ? 0.2515 0.2165 0.2387 0.0058  0.0080  0.0023  993  ASN A OD1 
7073  N ND2 . ASN A 995  ? 0.2327 0.1958 0.2178 0.0068  0.0098  0.0045  993  ASN A ND2 
7074  N N   . LEU A 996  ? 0.2051 0.1753 0.1959 0.0022  0.0105  0.0057  994  LEU A N   
7075  C CA  . LEU A 996  ? 0.2150 0.1866 0.2066 0.0010  0.0112  0.0065  994  LEU A CA  
7076  C C   . LEU A 996  ? 0.2020 0.1710 0.1924 0.0017  0.0120  0.0073  994  LEU A C   
7077  O O   . LEU A 996  ? 0.2042 0.1713 0.1931 0.0034  0.0120  0.0070  994  LEU A O   
7078  C CB  . LEU A 996  ? 0.2018 0.1774 0.1941 0.0014  0.0112  0.0056  994  LEU A CB  
7079  C CG  . LEU A 996  ? 0.2723 0.2510 0.2660 0.0011  0.0104  0.0046  994  LEU A CG  
7080  C CD1 . LEU A 996  ? 0.2665 0.2497 0.2610 0.0016  0.0105  0.0036  994  LEU A CD1 
7081  C CD2 . LEU A 996  ? 0.2828 0.2620 0.2781 -0.0014 0.0101  0.0054  994  LEU A CD2 
7082  N N   . TYR A 997  ? 0.2097 0.1788 0.2006 0.0004  0.0125  0.0083  995  TYR A N   
7083  C CA  . TYR A 997  ? 0.2100 0.1769 0.2000 0.0008  0.0131  0.0090  995  TYR A CA  
7084  C C   . TYR A 997  ? 0.2166 0.1860 0.2073 -0.0001 0.0135  0.0094  995  TYR A C   
7085  O O   . TYR A 997  ? 0.2056 0.1769 0.1974 -0.0018 0.0135  0.0101  995  TYR A O   
7086  C CB  . TYR A 997  ? 0.2013 0.1653 0.1913 0.0002  0.0132  0.0100  995  TYR A CB  
7087  C CG  . TYR A 997  ? 0.2162 0.1782 0.2053 0.0013  0.0128  0.0094  995  TYR A CG  
7088  C CD1 . TYR A 997  ? 0.2426 0.2028 0.2301 0.0029  0.0131  0.0093  995  TYR A CD1 
7089  C CD2 . TYR A 997  ? 0.2032 0.1654 0.1932 0.0007  0.0120  0.0089  995  TYR A CD2 
7090  C CE1 . TYR A 997  ? 0.2514 0.2105 0.2379 0.0039  0.0128  0.0088  995  TYR A CE1 
7091  C CE2 . TYR A 997  ? 0.2366 0.1974 0.2257 0.0018  0.0115  0.0080  995  TYR A CE2 
7092  C CZ  . TYR A 997  ? 0.2641 0.2237 0.2514 0.0035  0.0120  0.0080  995  TYR A CZ  
7093  O OH  . TYR A 997  ? 0.3155 0.2744 0.3016 0.0047  0.0116  0.0071  995  TYR A OH  
7094  N N   . ILE A 998  ? 0.1999 0.1693 0.1901 0.0010  0.0139  0.0088  996  ILE A N   
7095  C CA  . ILE A 998  ? 0.2028 0.1751 0.1936 0.0005  0.0142  0.0086  996  ILE A CA  
7096  C C   . ILE A 998  ? 0.1991 0.1691 0.1894 0.0005  0.0146  0.0094  996  ILE A C   
7097  O O   . ILE A 998  ? 0.2058 0.1730 0.1954 0.0017  0.0146  0.0091  996  ILE A O   
7098  C CB  . ILE A 998  ? 0.2271 0.2019 0.2181 0.0019  0.0139  0.0069  996  ILE A CB  
7099  C CG1 . ILE A 998  ? 0.2466 0.2239 0.2382 0.0021  0.0135  0.0061  996  ILE A CG1 
7100  C CG2 . ILE A 998  ? 0.2039 0.1823 0.1954 0.0015  0.0143  0.0063  996  ILE A CG2 
7101  C CD1 . ILE A 998  ? 0.3135 0.2945 0.3063 0.0001  0.0136  0.0067  996  ILE A CD1 
7102  N N   . ASN A 999  ? 0.1986 0.1699 0.1893 -0.0010 0.0148  0.0104  997  ASN A N   
7103  C CA  . ASN A 999  ? 0.2381 0.2080 0.2285 -0.0012 0.0152  0.0110  997  ASN A CA  
7104  C C   . ASN A 999  ? 0.2233 0.1889 0.2132 -0.0008 0.0153  0.0118  997  ASN A C   
7105  O O   . ASN A 999  ? 0.2036 0.1676 0.1933 -0.0003 0.0155  0.0118  997  ASN A O   
7106  C CB  . ASN A 999  ? 0.2324 0.2037 0.2229 -0.0002 0.0152  0.0096  997  ASN A CB  
7107  C CG  . ASN A 999  ? 0.2359 0.2122 0.2268 -0.0007 0.0152  0.0088  997  ASN A CG  
7108  O OD1 . ASN A 999  ? 0.2425 0.2214 0.2338 -0.0023 0.0154  0.0100  997  ASN A OD1 
7109  N ND2 . ASN A 999  ? 0.2397 0.2179 0.2308 0.0007  0.0150  0.0068  997  ASN A ND2 
7110  N N   . ARG A 1000 ? 0.2357 0.1999 0.2256 -0.0010 0.0151  0.0123  998  ARG A N   
7111  C CA  . ARG A 1000 ? 0.2186 0.1795 0.2081 -0.0006 0.0152  0.0129  998  ARG A CA  
7112  C C   . ARG A 1000 ? 0.2177 0.1780 0.2078 -0.0013 0.0147  0.0133  998  ARG A C   
7113  O O   . ARG A 1000 ? 0.2182 0.1802 0.2090 -0.0024 0.0143  0.0135  998  ARG A O   
7114  C CB  . ARG A 1000 ? 0.2021 0.1613 0.1906 0.0010  0.0153  0.0122  998  ARG A CB  
7115  C CG  . ARG A 1000 ? 0.2133 0.1737 0.2016 0.0016  0.0148  0.0113  998  ARG A CG  
7116  C CD  . ARG A 1000 ? 0.2228 0.1813 0.2099 0.0029  0.0147  0.0111  998  ARG A CD  
7117  N NE  . ARG A 1000 ? 0.2336 0.1908 0.2205 0.0027  0.0147  0.0114  998  ARG A NE  
7118  C CZ  . ARG A 1000 ? 0.2313 0.1873 0.2170 0.0038  0.0148  0.0113  998  ARG A CZ  
7119  N NH1 . ARG A 1000 ? 0.2351 0.1908 0.2197 0.0049  0.0148  0.0113  998  ARG A NH1 
7120  N NH2 . ARG A 1000 ? 0.2308 0.1861 0.2166 0.0038  0.0147  0.0112  998  ARG A NH2 
7121  N N   . ASN A 1001 ? 0.2268 0.1846 0.2166 -0.0008 0.0147  0.0135  999  ASN A N   
7122  C CA  . ASN A 1001 ? 0.2279 0.1847 0.2185 -0.0012 0.0140  0.0136  999  ASN A CA  
7123  C C   . ASN A 1001 ? 0.2325 0.1898 0.2228 -0.0006 0.0136  0.0124  999  ASN A C   
7124  O O   . ASN A 1001 ? 0.2205 0.1787 0.2098 0.0003  0.0139  0.0118  999  ASN A O   
7125  C CB  . ASN A 1001 ? 0.2266 0.1812 0.2172 -0.0005 0.0141  0.0137  999  ASN A CB  
7126  C CG  . ASN A 1001 ? 0.2543 0.2081 0.2435 0.0011  0.0146  0.0129  999  ASN A CG  
7127  O OD1 . ASN A 1001 ? 0.2724 0.2265 0.2608 0.0018  0.0144  0.0121  999  ASN A OD1 
7128  N ND2 . ASN A 1001 ? 0.3165 0.2696 0.3054 0.0016  0.0152  0.0133  999  ASN A ND2 
7129  N N   . ILE A 1002 ? 0.2255 0.1821 0.2166 -0.0011 0.0128  0.0121  1000 ILE A N   
7130  C CA  . ILE A 1002 ? 0.2046 0.1620 0.1957 -0.0008 0.0121  0.0110  1000 ILE A CA  
7131  C C   . ILE A 1002 ? 0.2567 0.2123 0.2472 0.0005  0.0117  0.0099  1000 ILE A C   
7132  O O   . ILE A 1002 ? 0.2215 0.1775 0.2124 0.0007  0.0109  0.0087  1000 ILE A O   
7133  C CB  . ILE A 1002 ? 0.2257 0.1845 0.2186 -0.0026 0.0113  0.0113  1000 ILE A CB  
7134  C CG1 . ILE A 1002 ? 0.2054 0.1619 0.1999 -0.0036 0.0103  0.0119  1000 ILE A CG1 
7135  C CG2 . ILE A 1002 ? 0.2309 0.1924 0.2242 -0.0038 0.0118  0.0124  1000 ILE A CG2 
7136  C CD1 . ILE A 1002 ? 0.2063 0.1640 0.2029 -0.0056 0.0093  0.0124  1000 ILE A CD1 
7137  N N   . ILE A 1003 ? 0.2367 0.1909 0.2264 0.0015  0.0123  0.0100  1001 ILE A N   
7138  C CA  . ILE A 1003 ? 0.2528 0.2060 0.2420 0.0028  0.0120  0.0088  1001 ILE A CA  
7139  C C   . ILE A 1003 ? 0.2899 0.2435 0.2770 0.0043  0.0130  0.0088  1001 ILE A C   
7140  O O   . ILE A 1003 ? 0.3044 0.2584 0.2908 0.0043  0.0138  0.0098  1001 ILE A O   
7141  C CB  . ILE A 1003 ? 0.2319 0.1834 0.2224 0.0026  0.0116  0.0089  1001 ILE A CB  
7142  C CG1 . ILE A 1003 ? 0.2886 0.2399 0.2788 0.0026  0.0126  0.0102  1001 ILE A CG1 
7143  C CG2 . ILE A 1003 ? 0.2140 0.1647 0.2068 0.0010  0.0103  0.0092  1001 ILE A CG2 
7144  C CD1 . ILE A 1003 ? 0.3022 0.2521 0.2933 0.0032  0.0124  0.0099  1001 ILE A CD1 
7145  N N   . GLY A 1004 ? 0.2806 0.2343 0.2668 0.0056  0.0128  0.0076  1002 GLY A N   
7146  C CA  . GLY A 1004 ? 0.2984 0.2527 0.2825 0.0069  0.0138  0.0079  1002 GLY A CA  
7147  C C   . GLY A 1004 ? 0.3289 0.2842 0.3114 0.0074  0.0139  0.0082  1002 GLY A C   
7148  O O   . GLY A 1004 ? 0.3169 0.2722 0.2984 0.0077  0.0148  0.0095  1002 GLY A O   
7149  N N   . ALA A 1005 ? 0.2883 0.2443 0.2709 0.0075  0.0130  0.0072  1003 ALA A N   
7150  C CA  . ALA A 1005 ? 0.2775 0.2345 0.2588 0.0082  0.0129  0.0074  1003 ALA A CA  
7151  C C   . ALA A 1005 ? 0.3148 0.2724 0.2938 0.0097  0.0134  0.0078  1003 ALA A C   
7152  O O   . ALA A 1005 ? 0.3301 0.2883 0.3084 0.0105  0.0134  0.0069  1003 ALA A O   
7153  C CB  . ALA A 1005 ? 0.3271 0.2853 0.3090 0.0082  0.0117  0.0059  1003 ALA A CB  
7154  N N   . VAL A 1006 ? 0.2478 0.2053 0.2256 0.0101  0.0138  0.0091  1004 VAL A N   
7155  C CA  . VAL A 1006 ? 0.2605 0.2183 0.2361 0.0110  0.0144  0.0103  1004 VAL A CA  
7156  C C   . VAL A 1006 ? 0.2354 0.1945 0.2094 0.0123  0.0136  0.0100  1004 VAL A C   
7157  O O   . VAL A 1006 ? 0.2309 0.1899 0.2053 0.0124  0.0129  0.0098  1004 VAL A O   
7158  C CB  . VAL A 1006 ? 0.2367 0.1931 0.2125 0.0105  0.0151  0.0123  1004 VAL A CB  
7159  C CG1 . VAL A 1006 ? 0.2704 0.2272 0.2440 0.0113  0.0156  0.0140  1004 VAL A CG1 
7160  C CG2 . VAL A 1006 ? 0.2394 0.1950 0.2167 0.0094  0.0159  0.0126  1004 VAL A CG2 
7161  N N   . VAL A 1007 ? 0.2494 0.2101 0.2214 0.0134  0.0138  0.0099  1005 VAL A N   
7162  C CA  . VAL A 1007 ? 0.2195 0.1817 0.1895 0.0147  0.0130  0.0096  1005 VAL A CA  
7163  C C   . VAL A 1007 ? 0.2197 0.1809 0.1890 0.0149  0.0127  0.0116  1005 VAL A C   
7164  O O   . VAL A 1007 ? 0.2629 0.2229 0.2319 0.0145  0.0135  0.0137  1005 VAL A O   
7165  C CB  . VAL A 1007 ? 0.2393 0.2038 0.2070 0.0157  0.0135  0.0096  1005 VAL A CB  
7166  C CG1 . VAL A 1007 ? 0.2292 0.1956 0.1944 0.0171  0.0126  0.0097  1005 VAL A CG1 
7167  C CG2 . VAL A 1007 ? 0.2268 0.1923 0.1955 0.0158  0.0133  0.0070  1005 VAL A CG2 
7168  N N   . GLY A 1008 ? 0.2464 0.2082 0.2158 0.0156  0.0116  0.0107  1006 GLY A N   
7169  C CA  . GLY A 1008 ? 0.2249 0.1857 0.1938 0.0162  0.0110  0.0122  1006 GLY A CA  
7170  C C   . GLY A 1008 ? 0.2539 0.2125 0.2249 0.0153  0.0111  0.0128  1006 GLY A C   
7171  O O   . GLY A 1008 ? 0.2627 0.2201 0.2337 0.0159  0.0105  0.0139  1006 GLY A O   
7172  N N   . VAL A 1009 ? 0.2327 0.1908 0.2055 0.0140  0.0118  0.0120  1007 VAL A N   
7173  C CA  . VAL A 1009 ? 0.2156 0.1722 0.1905 0.0131  0.0120  0.0123  1007 VAL A CA  
7174  C C   . VAL A 1009 ? 0.2282 0.1859 0.2051 0.0123  0.0117  0.0104  1007 VAL A C   
7175  O O   . VAL A 1009 ? 0.2468 0.2049 0.2249 0.0125  0.0111  0.0098  1007 VAL A O   
7176  C CB  . VAL A 1009 ? 0.2711 0.2262 0.2463 0.0121  0.0132  0.0136  1007 VAL A CB  
7177  C CG1 . VAL A 1009 ? 0.2690 0.2228 0.2462 0.0112  0.0133  0.0135  1007 VAL A CG1 
7178  C CG2 . VAL A 1009 ? 0.2505 0.2049 0.2238 0.0125  0.0136  0.0158  1007 VAL A CG2 
7179  N N   . GLN A 1010 ? 0.2122 0.1706 0.1895 0.0116  0.0120  0.0095  1008 GLN A N   
7180  C CA  . GLN A 1010 ? 0.2191 0.1789 0.1981 0.0108  0.0114  0.0078  1008 GLN A CA  
7181  C C   . GLN A 1010 ? 0.2160 0.1771 0.1943 0.0114  0.0107  0.0066  1008 GLN A C   
7182  O O   . GLN A 1010 ? 0.2658 0.2267 0.2446 0.0108  0.0109  0.0059  1008 GLN A O   
7183  C CB  . GLN A 1010 ? 0.2496 0.2089 0.2304 0.0091  0.0120  0.0079  1008 GLN A CB  
7184  C CG  . GLN A 1010 ? 0.2438 0.2021 0.2253 0.0085  0.0127  0.0089  1008 GLN A CG  
7185  C CD  . GLN A 1010 ? 0.2761 0.2325 0.2568 0.0084  0.0136  0.0102  1008 GLN A CD  
7186  O OE1 . GLN A 1010 ? 0.2647 0.2210 0.2450 0.0084  0.0139  0.0102  1008 GLN A OE1 
7187  N NE2 . GLN A 1010 ? 0.2499 0.2053 0.2308 0.0084  0.0139  0.0112  1008 GLN A NE2 
7188  N N   . PRO A 1011 ? 0.2574 0.2198 0.2346 0.0127  0.0099  0.0061  1009 PRO A N   
7189  C CA  . PRO A 1011 ? 0.2150 0.1790 0.1918 0.0132  0.0090  0.0045  1009 PRO A CA  
7190  C C   . PRO A 1011 ? 0.2722 0.2367 0.2515 0.0117  0.0086  0.0030  1009 PRO A C   
7191  O O   . PRO A 1011 ? 0.2337 0.1985 0.2149 0.0105  0.0086  0.0031  1009 PRO A O   
7192  C CB  . PRO A 1011 ? 0.2200 0.1856 0.1961 0.0145  0.0080  0.0041  1009 PRO A CB  
7193  C CG  . PRO A 1011 ? 0.2544 0.2185 0.2295 0.0152  0.0084  0.0061  1009 PRO A CG  
7194  C CD  . PRO A 1011 ? 0.2258 0.1883 0.2025 0.0137  0.0095  0.0068  1009 PRO A CD  
7195  N N   . PHE A 1012 ? 0.2634 0.2279 0.2427 0.0117  0.0082  0.0018  1010 PHE A N   
7196  C CA  . PHE A 1012 ? 0.2445 0.2082 0.2261 0.0101  0.0079  0.0010  1010 PHE A CA  
7197  C C   . PHE A 1012 ? 0.2586 0.2237 0.2416 0.0099  0.0064  -0.0011 1010 PHE A C   
7198  O O   . PHE A 1012 ? 0.2665 0.2327 0.2481 0.0112  0.0057  -0.0024 1010 PHE A O   
7199  C CB  . PHE A 1012 ? 0.2692 0.2312 0.2505 0.0101  0.0085  0.0011  1010 PHE A CB  
7200  C CG  . PHE A 1012 ? 0.2870 0.2478 0.2710 0.0085  0.0081  0.0007  1010 PHE A CG  
7201  C CD1 . PHE A 1012 ? 0.3041 0.2639 0.2895 0.0070  0.0087  0.0022  1010 PHE A CD1 
7202  C CD2 . PHE A 1012 ? 0.3074 0.2679 0.2925 0.0085  0.0069  -0.0013 1010 PHE A CD2 
7203  C CE1 . PHE A 1012 ? 0.2953 0.2539 0.2831 0.0054  0.0081  0.0022  1010 PHE A CE1 
7204  C CE2 . PHE A 1012 ? 0.3278 0.2866 0.3156 0.0069  0.0062  -0.0014 1010 PHE A CE2 
7205  C CZ  . PHE A 1012 ? 0.2617 0.2196 0.2507 0.0053  0.0069  0.0005  1010 PHE A CZ  
7206  N N   . GLY A 1013 ? 0.2762 0.2415 0.2618 0.0080  0.0059  -0.0012 1011 GLY A N   
7207  C CA  . GLY A 1013 ? 0.3142 0.2808 0.3016 0.0074  0.0044  -0.0030 1011 GLY A CA  
7208  C C   . GLY A 1013 ? 0.3031 0.2714 0.2931 0.0056  0.0042  -0.0025 1011 GLY A C   
7209  O O   . GLY A 1013 ? 0.2813 0.2509 0.2709 0.0057  0.0050  -0.0015 1011 GLY A O   
7210  N N   . GLY A 1014 ? 0.2831 0.2515 0.2758 0.0039  0.0031  -0.0034 1012 GLY A N   
7211  C CA  . GLY A 1014 ? 0.3380 0.3084 0.3332 0.0017  0.0029  -0.0026 1012 GLY A CA  
7212  C C   . GLY A 1014 ? 0.3428 0.3159 0.3399 0.0012  0.0015  -0.0043 1012 GLY A C   
7213  O O   . GLY A 1014 ? 0.3527 0.3266 0.3486 0.0029  0.0006  -0.0060 1012 GLY A O   
7214  N N   . ARG A 1015 ? 0.2894 0.2641 0.2895 -0.0013 0.0011  -0.0036 1013 ARG A N   
7215  C CA  . ARG A 1015 ? 0.3182 0.2964 0.3207 -0.0023 -0.0001 -0.0048 1013 ARG A CA  
7216  C C   . ARG A 1015 ? 0.3201 0.2972 0.3260 -0.0053 -0.0012 -0.0045 1013 ARG A C   
7217  O O   . ARG A 1015 ? 0.3074 0.2813 0.3139 -0.0064 -0.0010 -0.0032 1013 ARG A O   
7218  C CB  . ARG A 1015 ? 0.3026 0.2851 0.3054 -0.0025 0.0008  -0.0041 1013 ARG A CB  
7219  C CG  . ARG A 1015 ? 0.3293 0.3120 0.3329 -0.0044 0.0021  -0.0018 1013 ARG A CG  
7220  C CD  . ARG A 1015 ? 0.4516 0.4396 0.4566 -0.0052 0.0027  -0.0014 1013 ARG A CD  
7221  N NE  . ARG A 1015 ? 0.4524 0.4441 0.4592 -0.0054 0.0015  -0.0030 1013 ARG A NE  
7222  C CZ  . ARG A 1015 ? 0.5147 0.5079 0.5247 -0.0080 0.0004  -0.0031 1013 ARG A CZ  
7223  N NH1 . ARG A 1015 ? 0.4937 0.4849 0.5055 -0.0107 0.0003  -0.0014 1013 ARG A NH1 
7224  N NH2 . ARG A 1015 ? 0.4700 0.4668 0.4817 -0.0079 -0.0007 -0.0048 1013 ARG A NH2 
7225  N N   . GLY A 1016 ? 0.3365 0.3165 0.3450 -0.0067 -0.0025 -0.0055 1014 GLY A N   
7226  C CA  . GLY A 1016 ? 0.3459 0.3251 0.3583 -0.0098 -0.0038 -0.0049 1014 GLY A CA  
7227  C C   . GLY A 1016 ? 0.3539 0.3281 0.3665 -0.0094 -0.0051 -0.0061 1014 GLY A C   
7228  O O   . GLY A 1016 ? 0.3394 0.3126 0.3504 -0.0071 -0.0059 -0.0085 1014 GLY A O   
7229  N N   . LEU A 1017 ? 0.2981 0.2692 0.3127 -0.0116 -0.0055 -0.0044 1015 LEU A N   
7230  C CA  . LEU A 1017 ? 0.3033 0.2694 0.3186 -0.0112 -0.0070 -0.0056 1015 LEU A CA  
7231  C C   . LEU A 1017 ? 0.3087 0.2724 0.3203 -0.0081 -0.0059 -0.0062 1015 LEU A C   
7232  O O   . LEU A 1017 ? 0.3168 0.2769 0.3286 -0.0072 -0.0070 -0.0077 1015 LEU A O   
7233  C CB  . LEU A 1017 ? 0.3007 0.2641 0.3192 -0.0142 -0.0077 -0.0032 1015 LEU A CB  
7234  C CG  . LEU A 1017 ? 0.3651 0.3307 0.3877 -0.0178 -0.0090 -0.0021 1015 LEU A CG  
7235  C CD1 . LEU A 1017 ? 0.2946 0.2571 0.3198 -0.0207 -0.0095 0.0009  1015 LEU A CD1 
7236  C CD2 . LEU A 1017 ? 0.3597 0.3248 0.3846 -0.0179 -0.0114 -0.0051 1015 LEU A CD2 
7237  N N   . SER A 1018 ? 0.2633 0.2288 0.2718 -0.0066 -0.0038 -0.0052 1016 SER A N   
7238  C CA  . SER A 1018 ? 0.2745 0.2379 0.2797 -0.0041 -0.0027 -0.0053 1016 SER A CA  
7239  C C   . SER A 1018 ? 0.2965 0.2610 0.2989 -0.0011 -0.0028 -0.0077 1016 SER A C   
7240  O O   . SER A 1018 ? 0.3139 0.2769 0.3137 0.0009  -0.0020 -0.0080 1016 SER A O   
7241  C CB  . SER A 1018 ? 0.2860 0.2503 0.2894 -0.0041 -0.0006 -0.0028 1016 SER A CB  
7242  O OG  . SER A 1018 ? 0.3077 0.2710 0.3132 -0.0066 -0.0004 -0.0005 1016 SER A OG  
7243  N N   . GLY A 1019 ? 0.2945 0.2619 0.2973 -0.0009 -0.0037 -0.0092 1017 GLY A N   
7244  C CA  . GLY A 1019 ? 0.3302 0.2988 0.3301 0.0020  -0.0038 -0.0113 1017 GLY A CA  
7245  C C   . GLY A 1019 ? 0.3133 0.2857 0.3132 0.0023  -0.0044 -0.0123 1017 GLY A C   
7246  O O   . GLY A 1019 ? 0.3028 0.2776 0.3046 0.0006  -0.0043 -0.0114 1017 GLY A O   
7247  N N   . THR A 1020 ? 0.2755 0.2490 0.2732 0.0047  -0.0051 -0.0144 1018 THR A N   
7248  C CA  . THR A 1020 ? 0.2623 0.2396 0.2592 0.0058  -0.0057 -0.0155 1018 THR A CA  
7249  C C   . THR A 1020 ? 0.2823 0.2610 0.2759 0.0077  -0.0041 -0.0139 1018 THR A C   
7250  O O   . THR A 1020 ? 0.3145 0.2962 0.3079 0.0082  -0.0044 -0.0140 1018 THR A O   
7251  C CB  . THR A 1020 ? 0.2720 0.2499 0.2678 0.0076  -0.0073 -0.0186 1018 THR A CB  
7252  O OG1 . THR A 1020 ? 0.2488 0.2252 0.2409 0.0099  -0.0063 -0.0185 1018 THR A OG1 
7253  C CG2 . THR A 1020 ? 0.3089 0.2853 0.3084 0.0059  -0.0092 -0.0206 1018 THR A CG2 
7254  N N   . GLY A 1021 ? 0.3116 0.2880 0.3027 0.0087  -0.0026 -0.0124 1019 GLY A N   
7255  C CA  . GLY A 1021 ? 0.2712 0.2484 0.2588 0.0109  -0.0016 -0.0113 1019 GLY A CA  
7256  C C   . GLY A 1021 ? 0.2940 0.2729 0.2791 0.0132  -0.0026 -0.0131 1019 GLY A C   
7257  O O   . GLY A 1021 ? 0.2725 0.2522 0.2587 0.0132  -0.0041 -0.0155 1019 GLY A O   
7258  N N   . PRO A 1022 ? 0.2481 0.2278 0.2299 0.0152  -0.0019 -0.0118 1020 PRO A N   
7259  C CA  . PRO A 1022 ? 0.2849 0.2635 0.2655 0.0155  -0.0004 -0.0091 1020 PRO A CA  
7260  C C   . PRO A 1022 ? 0.3082 0.2837 0.2880 0.0149  0.0011  -0.0077 1020 PRO A C   
7261  O O   . PRO A 1022 ? 0.2843 0.2587 0.2641 0.0149  0.0010  -0.0087 1020 PRO A O   
7262  C CB  . PRO A 1022 ? 0.2420 0.2222 0.2192 0.0179  -0.0006 -0.0086 1020 PRO A CB  
7263  C CG  . PRO A 1022 ? 0.2765 0.2580 0.2521 0.0191  -0.0016 -0.0106 1020 PRO A CG  
7264  C CD  . PRO A 1022 ? 0.2705 0.2523 0.2495 0.0175  -0.0028 -0.0132 1020 PRO A CD  
7265  N N   . LYS A 1023 ? 0.2541 0.2283 0.2336 0.0147  0.0024  -0.0054 1021 LYS A N   
7266  C CA  . LYS A 1023 ? 0.2680 0.2395 0.2471 0.0141  0.0038  -0.0039 1021 LYS A CA  
7267  C C   . LYS A 1023 ? 0.2627 0.2338 0.2387 0.0156  0.0043  -0.0036 1021 LYS A C   
7268  O O   . LYS A 1023 ? 0.2231 0.1954 0.1966 0.0172  0.0043  -0.0028 1021 LYS A O   
7269  C CB  . LYS A 1023 ? 0.2639 0.2344 0.2433 0.0136  0.0049  -0.0018 1021 LYS A CB  
7270  C CG  . LYS A 1023 ? 0.2582 0.2292 0.2407 0.0117  0.0049  -0.0019 1021 LYS A CG  
7271  C CD  . LYS A 1023 ? 0.2577 0.2280 0.2400 0.0117  0.0059  -0.0001 1021 LYS A CD  
7272  C CE  . LYS A 1023 ? 0.2780 0.2492 0.2630 0.0098  0.0061  0.0000  1021 LYS A CE  
7273  N NZ  . LYS A 1023 ? 0.2625 0.2317 0.2486 0.0081  0.0068  0.0007  1021 LYS A NZ  
7274  N N   . ALA A 1024 ? 0.2339 0.2036 0.2102 0.0152  0.0049  -0.0039 1022 ALA A N   
7275  C CA  . ALA A 1024 ? 0.2570 0.2267 0.2306 0.0165  0.0058  -0.0033 1022 ALA A CA  
7276  C C   . ALA A 1024 ? 0.2387 0.2071 0.2111 0.0164  0.0072  -0.0003 1022 ALA A C   
7277  O O   . ALA A 1024 ? 0.2678 0.2347 0.2420 0.0151  0.0077  0.0008  1022 ALA A O   
7278  C CB  . ALA A 1024 ? 0.2665 0.2351 0.2412 0.0160  0.0059  -0.0045 1022 ALA A CB  
7279  N N   . GLY A 1025 ? 0.2358 0.2051 0.2052 0.0177  0.0078  0.0009  1023 GLY A N   
7280  C CA  . GLY A 1025 ? 0.2221 0.1901 0.1908 0.0175  0.0089  0.0037  1023 GLY A CA  
7281  C C   . GLY A 1025 ? 0.2324 0.1998 0.2015 0.0176  0.0084  0.0047  1023 GLY A C   
7282  O O   . GLY A 1025 ? 0.2383 0.2038 0.2079 0.0170  0.0090  0.0066  1023 GLY A O   
7283  N N   . GLY A 1026 ? 0.2349 0.2040 0.2041 0.0183  0.0070  0.0033  1024 GLY A N   
7284  C CA  . GLY A 1026 ? 0.2223 0.1915 0.1921 0.0187  0.0063  0.0039  1024 GLY A CA  
7285  C C   . GLY A 1026 ? 0.2277 0.1990 0.1953 0.0205  0.0051  0.0038  1024 GLY A C   
7286  O O   . GLY A 1026 ? 0.2291 0.2022 0.1948 0.0214  0.0048  0.0030  1024 GLY A O   
7287  N N   . PRO A 1027 ? 0.2674 0.2388 0.2353 0.0213  0.0043  0.0045  1025 PRO A N   
7288  C CA  . PRO A 1027 ? 0.2444 0.2173 0.2099 0.0232  0.0032  0.0051  1025 PRO A CA  
7289  C C   . PRO A 1027 ? 0.2304 0.2064 0.1961 0.0240  0.0017  0.0027  1025 PRO A C   
7290  O O   . PRO A 1027 ? 0.2414 0.2191 0.2048 0.0257  0.0007  0.0031  1025 PRO A O   
7291  C CB  . PRO A 1027 ? 0.2287 0.1999 0.1951 0.0237  0.0027  0.0067  1025 PRO A CB  
7292  C CG  . PRO A 1027 ? 0.2639 0.2346 0.2337 0.0223  0.0031  0.0052  1025 PRO A CG  
7293  C CD  . PRO A 1027 ? 0.2473 0.2172 0.2176 0.0206  0.0044  0.0049  1025 PRO A CD  
7294  N N   . LEU A 1028 ? 0.2272 0.2042 0.1955 0.0228  0.0014  0.0003  1026 LEU A N   
7295  C CA  . LEU A 1028 ? 0.2278 0.2078 0.1967 0.0233  0.0000  -0.0023 1026 LEU A CA  
7296  C C   . LEU A 1028 ? 0.2290 0.2101 0.1967 0.0233  -0.0001 -0.0039 1026 LEU A C   
7297  O O   . LEU A 1028 ? 0.2385 0.2222 0.2064 0.0239  -0.0015 -0.0062 1026 LEU A O   
7298  C CB  . LEU A 1028 ? 0.2252 0.2060 0.1981 0.0218  -0.0004 -0.0040 1026 LEU A CB  
7299  C CG  . LEU A 1028 ? 0.2601 0.2413 0.2342 0.0223  -0.0008 -0.0032 1026 LEU A CG  
7300  C CD1 . LEU A 1028 ? 0.3184 0.3009 0.2963 0.0205  -0.0008 -0.0047 1026 LEU A CD1 
7301  C CD2 . LEU A 1028 ? 0.2932 0.2769 0.2659 0.0245  -0.0024 -0.0036 1026 LEU A CD2 
7302  N N   . TYR A 1029 ? 0.2288 0.2082 0.1956 0.0228  0.0012  -0.0031 1027 TYR A N   
7303  C CA  . TYR A 1029 ? 0.2370 0.2172 0.2034 0.0227  0.0011  -0.0051 1027 TYR A CA  
7304  C C   . TYR A 1029 ? 0.2329 0.2164 0.1963 0.0247  0.0002  -0.0062 1027 TYR A C   
7305  O O   . TYR A 1029 ? 0.2339 0.2193 0.1979 0.0250  -0.0011 -0.0091 1027 TYR A O   
7306  C CB  . TYR A 1029 ? 0.2472 0.2252 0.2131 0.0220  0.0028  -0.0038 1027 TYR A CB  
7307  C CG  . TYR A 1029 ? 0.2287 0.2065 0.1959 0.0214  0.0029  -0.0060 1027 TYR A CG  
7308  C CD1 . TYR A 1029 ? 0.2716 0.2479 0.2423 0.0197  0.0023  -0.0076 1027 TYR A CD1 
7309  C CD2 . TYR A 1029 ? 0.2366 0.2156 0.2014 0.0225  0.0034  -0.0064 1027 TYR A CD2 
7310  C CE1 . TYR A 1029 ? 0.2591 0.2346 0.2311 0.0192  0.0021  -0.0095 1027 TYR A CE1 
7311  C CE2 . TYR A 1029 ? 0.2724 0.2510 0.2385 0.0222  0.0034  -0.0087 1027 TYR A CE2 
7312  C CZ  . TYR A 1029 ? 0.3164 0.2930 0.2862 0.0206  0.0026  -0.0102 1027 TYR A CZ  
7313  O OH  . TYR A 1029 ? 0.2713 0.2471 0.2426 0.0204  0.0023  -0.0124 1027 TYR A OH  
7314  N N   . LEU A 1030 ? 0.2350 0.2191 0.1950 0.0260  0.0007  -0.0037 1028 LEU A N   
7315  C CA  . LEU A 1030 ? 0.2579 0.2455 0.2145 0.0279  -0.0001 -0.0043 1028 LEU A CA  
7316  C C   . LEU A 1030 ? 0.2500 0.2402 0.2070 0.0289  -0.0021 -0.0063 1028 LEU A C   
7317  O O   . LEU A 1030 ? 0.2495 0.2429 0.2050 0.0300  -0.0032 -0.0086 1028 LEU A O   
7318  C CB  . LEU A 1030 ? 0.2555 0.2434 0.2085 0.0289  0.0008  -0.0007 1028 LEU A CB  
7319  C CG  . LEU A 1030 ? 0.2600 0.2462 0.2123 0.0280  0.0028  0.0013  1028 LEU A CG  
7320  C CD1 . LEU A 1030 ? 0.2494 0.2364 0.1982 0.0288  0.0034  0.0051  1028 LEU A CD1 
7321  C CD2 . LEU A 1030 ? 0.2691 0.2572 0.2211 0.0281  0.0032  -0.0013 1028 LEU A CD2 
7322  N N   . GLY A 1031 ? 0.2515 0.2407 0.2104 0.0285  -0.0027 -0.0056 1029 GLY A N   
7323  C CA  . GLY A 1031 ? 0.2671 0.2591 0.2267 0.0295  -0.0047 -0.0073 1029 GLY A CA  
7324  C C   . GLY A 1031 ? 0.2922 0.2859 0.2541 0.0288  -0.0058 -0.0112 1029 GLY A C   
7325  O O   . GLY A 1031 ? 0.2550 0.2518 0.2169 0.0298  -0.0076 -0.0132 1029 GLY A O   
7326  N N   . ARG A 1032 ? 0.2367 0.2283 0.2011 0.0270  -0.0051 -0.0124 1030 ARG A N   
7327  C CA  . ARG A 1032 ? 0.2547 0.2473 0.2217 0.0262  -0.0063 -0.0160 1030 ARG A CA  
7328  C C   . ARG A 1032 ? 0.2867 0.2816 0.2512 0.0276  -0.0069 -0.0182 1030 ARG A C   
7329  O O   . ARG A 1032 ? 0.2580 0.2542 0.2242 0.0275  -0.0085 -0.0216 1030 ARG A O   
7330  C CB  . ARG A 1032 ? 0.2432 0.2325 0.2136 0.0238  -0.0054 -0.0161 1030 ARG A CB  
7331  C CG  . ARG A 1032 ? 0.2900 0.2794 0.2640 0.0223  -0.0068 -0.0193 1030 ARG A CG  
7332  C CD  . ARG A 1032 ? 0.2923 0.2837 0.2692 0.0215  -0.0081 -0.0200 1030 ARG A CD  
7333  N NE  . ARG A 1032 ? 0.3031 0.2940 0.2841 0.0194  -0.0093 -0.0224 1030 ARG A NE  
7334  C CZ  . ARG A 1032 ? 0.3989 0.3924 0.3818 0.0193  -0.0113 -0.0252 1030 ARG A CZ  
7335  N NH1 . ARG A 1032 ? 0.3136 0.3106 0.2945 0.0212  -0.0124 -0.0261 1030 ARG A NH1 
7336  N NH2 . ARG A 1032 ? 0.3246 0.3170 0.3116 0.0170  -0.0124 -0.0269 1030 ARG A NH2 
7337  N N   . LEU A 1033 ? 0.2494 0.2449 0.2099 0.0291  -0.0058 -0.0164 1031 LEU A N   
7338  C CA  . LEU A 1033 ? 0.2567 0.2548 0.2147 0.0305  -0.0060 -0.0184 1031 LEU A CA  
7339  C C   . LEU A 1033 ? 0.3019 0.3044 0.2560 0.0328  -0.0071 -0.0184 1031 LEU A C   
7340  O O   . LEU A 1033 ? 0.2610 0.2665 0.2120 0.0343  -0.0070 -0.0193 1031 LEU A O   
7341  C CB  . LEU A 1033 ? 0.2439 0.2405 0.2004 0.0303  -0.0040 -0.0166 1031 LEU A CB  
7342  C CG  . LEU A 1033 ? 0.2811 0.2733 0.2413 0.0281  -0.0030 -0.0164 1031 LEU A CG  
7343  C CD1 . LEU A 1033 ? 0.2403 0.2312 0.1990 0.0280  -0.0010 -0.0146 1031 LEU A CD1 
7344  C CD2 . LEU A 1033 ? 0.2797 0.2713 0.2434 0.0273  -0.0045 -0.0203 1031 LEU A CD2 
7345  N N   . VAL A 1034 ? 0.2614 0.2648 0.2157 0.0332  -0.0082 -0.0174 1032 VAL A N   
7346  C CA  . VAL A 1034 ? 0.2512 0.2586 0.2021 0.0353  -0.0095 -0.0173 1032 VAL A CA  
7347  C C   . VAL A 1034 ? 0.2801 0.2890 0.2338 0.0352  -0.0116 -0.0197 1032 VAL A C   
7348  O O   . VAL A 1034 ? 0.2839 0.2904 0.2418 0.0334  -0.0117 -0.0202 1032 VAL A O   
7349  C CB  . VAL A 1034 ? 0.2576 0.2646 0.2054 0.0362  -0.0086 -0.0126 1032 VAL A CB  
7350  C CG1 . VAL A 1034 ? 0.2571 0.2637 0.2017 0.0364  -0.0066 -0.0102 1032 VAL A CG1 
7351  C CG2 . VAL A 1034 ? 0.2539 0.2570 0.2046 0.0349  -0.0081 -0.0104 1032 VAL A CG2 
7352  N N   . THR A 1035 ? 0.3034 0.3166 0.2549 0.0372  -0.0133 -0.0211 1033 THR A N   
7353  C CA  . THR A 1035 ? 0.3388 0.3540 0.2930 0.0371  -0.0155 -0.0238 1033 THR A CA  
7354  C C   . THR A 1035 ? 0.3342 0.3488 0.2893 0.0373  -0.0158 -0.0212 1033 THR A C   
7355  O O   . THR A 1035 ? 0.4018 0.4170 0.3605 0.0365  -0.0171 -0.0229 1033 THR A O   
7356  C CB  . THR A 1035 ? 0.4123 0.4327 0.3639 0.0392  -0.0175 -0.0266 1033 THR A CB  
7357  O OG1 . THR A 1035 ? 0.4223 0.4449 0.3687 0.0413  -0.0171 -0.0236 1033 THR A OG1 
7358  C CG2 . THR A 1035 ? 0.3797 0.4008 0.3317 0.0390  -0.0176 -0.0303 1033 THR A CG2 
7359  N N   . THR A 1036 ? 0.3106 0.3241 0.2628 0.0383  -0.0148 -0.0171 1034 THR A N   
7360  C CA  . THR A 1036 ? 0.2937 0.3059 0.2468 0.0386  -0.0151 -0.0146 1034 THR A CA  
7361  C C   . THR A 1036 ? 0.3026 0.3102 0.2558 0.0375  -0.0130 -0.0111 1034 THR A C   
7362  O O   . THR A 1036 ? 0.3093 0.3160 0.2589 0.0381  -0.0119 -0.0084 1034 THR A O   
7363  C CB  . THR A 1036 ? 0.3315 0.3468 0.2811 0.0412  -0.0167 -0.0130 1034 THR A CB  
7364  O OG1 . THR A 1036 ? 0.3867 0.4066 0.3363 0.0422  -0.0188 -0.0166 1034 THR A OG1 
7365  C CG2 . THR A 1036 ? 0.4483 0.4620 0.3996 0.0417  -0.0172 -0.0108 1034 THR A CG2 
7366  N N   . ALA A 1037 ? 0.2986 0.3035 0.2557 0.0358  -0.0124 -0.0112 1035 ALA A N   
7367  C CA  . ALA A 1037 ? 0.2822 0.2828 0.2398 0.0346  -0.0103 -0.0085 1035 ALA A CA  
7368  C C   . ALA A 1037 ? 0.2831 0.2821 0.2387 0.0360  -0.0104 -0.0048 1035 ALA A C   
7369  O O   . ALA A 1037 ? 0.2843 0.2847 0.2405 0.0373  -0.0119 -0.0047 1035 ALA A O   
7370  C CB  . ALA A 1037 ? 0.2769 0.2756 0.2392 0.0324  -0.0098 -0.0097 1035 ALA A CB  
7371  N N   . PRO A 1038 ? 0.2998 0.2961 0.2532 0.0357  -0.0088 -0.0017 1036 PRO A N   
7372  C CA  . PRO A 1038 ? 0.2824 0.2764 0.2347 0.0367  -0.0089 0.0020  1036 PRO A CA  
7373  C C   . PRO A 1038 ? 0.2816 0.2725 0.2377 0.0356  -0.0085 0.0021  1036 PRO A C   
7374  O O   . PRO A 1038 ? 0.2896 0.2801 0.2489 0.0339  -0.0077 0.0000  1036 PRO A O   
7375  C CB  . PRO A 1038 ? 0.2790 0.2713 0.2281 0.0363  -0.0073 0.0049  1036 PRO A CB  
7376  C CG  . PRO A 1038 ? 0.2754 0.2673 0.2262 0.0344  -0.0057 0.0027  1036 PRO A CG  
7377  C CD  . PRO A 1038 ? 0.2646 0.2597 0.2170 0.0345  -0.0070 -0.0015 1036 PRO A CD  
7378  N N   . VAL A 1039 ? 0.2651 0.2539 0.2209 0.0368  -0.0092 0.0047  1037 VAL A N   
7379  C CA  . VAL A 1039 ? 0.2901 0.2758 0.2491 0.0361  -0.0087 0.0051  1037 VAL A CA  
7380  C C   . VAL A 1039 ? 0.2624 0.2443 0.2209 0.0345  -0.0067 0.0073  1037 VAL A C   
7381  O O   . VAL A 1039 ? 0.2721 0.2523 0.2280 0.0349  -0.0065 0.0105  1037 VAL A O   
7382  C CB  . VAL A 1039 ? 0.3235 0.3083 0.2827 0.0381  -0.0105 0.0067  1037 VAL A CB  
7383  C CG1 . VAL A 1039 ? 0.3133 0.2952 0.2760 0.0376  -0.0101 0.0066  1037 VAL A CG1 
7384  C CG2 . VAL A 1039 ? 0.3177 0.3067 0.2774 0.0398  -0.0126 0.0045  1037 VAL A CG2 
7385  N N   . PRO A 1040 ? 0.2689 0.2497 0.2300 0.0325  -0.0052 0.0059  1038 PRO A N   
7386  C CA  . PRO A 1040 ? 0.2740 0.2516 0.2347 0.0310  -0.0033 0.0078  1038 PRO A CA  
7387  C C   . PRO A 1040 ? 0.2498 0.2238 0.2109 0.0314  -0.0035 0.0105  1038 PRO A C   
7388  O O   . PRO A 1040 ? 0.2733 0.2470 0.2360 0.0326  -0.0048 0.0101  1038 PRO A O   
7389  C CB  . PRO A 1040 ? 0.2710 0.2485 0.2348 0.0290  -0.0022 0.0054  1038 PRO A CB  
7390  C CG  . PRO A 1040 ? 0.2777 0.2588 0.2426 0.0292  -0.0033 0.0023  1038 PRO A CG  
7391  C CD  . PRO A 1040 ? 0.2520 0.2349 0.2163 0.0313  -0.0052 0.0025  1038 PRO A CD  
7392  N N   . PRO A 1041 ? 0.2684 0.2396 0.2281 0.0305  -0.0022 0.0131  1039 PRO A N   
7393  C CA  . PRO A 1041 ? 0.2425 0.2098 0.2032 0.0305  -0.0023 0.0154  1039 PRO A CA  
7394  C C   . PRO A 1041 ? 0.2442 0.2105 0.2087 0.0300  -0.0023 0.0133  1039 PRO A C   
7395  O O   . PRO A 1041 ? 0.2656 0.2331 0.2318 0.0286  -0.0012 0.0111  1039 PRO A O   
7396  C CB  . PRO A 1041 ? 0.2979 0.2632 0.2572 0.0290  -0.0005 0.0178  1039 PRO A CB  
7397  C CG  . PRO A 1041 ? 0.3075 0.2762 0.2641 0.0289  0.0001  0.0173  1039 PRO A CG  
7398  C CD  . PRO A 1041 ? 0.2780 0.2497 0.2359 0.0292  -0.0005 0.0136  1039 PRO A CD  
7399  N N   . GLN A 1042 ? 0.2465 0.2108 0.2123 0.0313  -0.0036 0.0139  1040 GLN A N   
7400  C CA  . GLN A 1042 ? 0.2567 0.2202 0.2260 0.0311  -0.0037 0.0121  1040 GLN A CA  
7401  C C   . GLN A 1042 ? 0.2940 0.2617 0.2655 0.0311  -0.0039 0.0086  1040 GLN A C   
7402  O O   . GLN A 1042 ? 0.2854 0.2535 0.2597 0.0305  -0.0036 0.0068  1040 GLN A O   
7403  C CB  . GLN A 1042 ? 0.2953 0.2563 0.2658 0.0291  -0.0020 0.0126  1040 GLN A CB  
7404  C CG  . GLN A 1042 ? 0.3333 0.2902 0.3024 0.0289  -0.0019 0.0159  1040 GLN A CG  
7405  C CD  . GLN A 1042 ? 0.4134 0.3679 0.3842 0.0272  -0.0005 0.0160  1040 GLN A CD  
7406  O OE1 . GLN A 1042 ? 0.4164 0.3705 0.3862 0.0255  0.0011  0.0169  1040 GLN A OE1 
7407  N NE2 . GLN A 1042 ? 0.4364 0.3894 0.4099 0.0277  -0.0012 0.0148  1040 GLN A NE2 
7408  N N   . HIS A 1043 ? 0.2631 0.2340 0.2333 0.0317  -0.0045 0.0075  1041 HIS A N   
7409  C CA  . HIS A 1043 ? 0.2518 0.2268 0.2241 0.0312  -0.0047 0.0044  1041 HIS A CA  
7410  C C   . HIS A 1043 ? 0.2618 0.2390 0.2356 0.0333  -0.0066 0.0031  1041 HIS A C   
7411  O O   . HIS A 1043 ? 0.2659 0.2449 0.2382 0.0349  -0.0081 0.0032  1041 HIS A O   
7412  C CB  . HIS A 1043 ? 0.2464 0.2238 0.2170 0.0305  -0.0044 0.0037  1041 HIS A CB  
7413  C CG  . HIS A 1043 ? 0.2714 0.2526 0.2442 0.0297  -0.0046 0.0006  1041 HIS A CG  
7414  N ND1 . HIS A 1043 ? 0.2461 0.2277 0.2208 0.0274  -0.0033 -0.0007 1041 HIS A ND1 
7415  C CD2 . HIS A 1043 ? 0.2576 0.2425 0.2312 0.0308  -0.0062 -0.0013 1041 HIS A CD2 
7416  C CE1 . HIS A 1043 ? 0.2734 0.2586 0.2501 0.0269  -0.0040 -0.0031 1041 HIS A CE1 
7417  N NE2 . HIS A 1043 ? 0.2758 0.2633 0.2519 0.0290  -0.0057 -0.0036 1041 HIS A NE2 
7418  N N   . SER A 1044 ? 0.2501 0.2277 0.2270 0.0334  -0.0067 0.0017  1042 SER A N   
7419  C CA  . SER A 1044 ? 0.2562 0.2364 0.2352 0.0355  -0.0085 0.0000  1042 SER A CA  
7420  C C   . SER A 1044 ? 0.2635 0.2448 0.2459 0.0348  -0.0078 -0.0019 1042 SER A C   
7421  O O   . SER A 1044 ? 0.2534 0.2325 0.2361 0.0331  -0.0062 -0.0013 1042 SER A O   
7422  C CB  . SER A 1044 ? 0.2510 0.2285 0.2288 0.0381  -0.0104 0.0018  1042 SER A CB  
7423  O OG  . SER A 1044 ? 0.2823 0.2554 0.2607 0.0382  -0.0101 0.0032  1042 SER A OG  
7424  N N   . SER A 1045 ? 0.2413 0.2266 0.2263 0.0362  -0.0089 -0.0042 1043 SER A N   
7425  C CA  . SER A 1045 ? 0.2692 0.2565 0.2574 0.0359  -0.0084 -0.0062 1043 SER A CA  
7426  C C   . SER A 1045 ? 0.2304 0.2201 0.2206 0.0389  -0.0105 -0.0079 1043 SER A C   
7427  O O   . SER A 1045 ? 0.2544 0.2470 0.2445 0.0402  -0.0119 -0.0086 1043 SER A O   
7428  C CB  . SER A 1045 ? 0.2353 0.2272 0.2254 0.0334  -0.0070 -0.0080 1043 SER A CB  
7429  O OG  . SER A 1045 ? 0.2598 0.2542 0.2527 0.0332  -0.0065 -0.0097 1043 SER A OG  
7430  N N   . VAL A 1046 ? 0.2308 0.2196 0.2230 0.0401  -0.0108 -0.0088 1044 VAL A N   
7431  C CA  . VAL A 1046 ? 0.2595 0.2511 0.2542 0.0431  -0.0128 -0.0110 1044 VAL A CA  
7432  C C   . VAL A 1046 ? 0.2445 0.2433 0.2424 0.0424  -0.0121 -0.0142 1044 VAL A C   
7433  O O   . VAL A 1046 ? 0.2657 0.2682 0.2660 0.0448  -0.0136 -0.0165 1044 VAL A O   
7434  C CB  . VAL A 1046 ? 0.2637 0.2510 0.2593 0.0451  -0.0138 -0.0109 1044 VAL A CB  
7435  C CG1 . VAL A 1046 ? 0.3148 0.2951 0.3074 0.0457  -0.0147 -0.0073 1044 VAL A CG1 
7436  C CG2 . VAL A 1046 ? 0.2324 0.2199 0.2294 0.0434  -0.0120 -0.0119 1044 VAL A CG2 
7437  N N   . HIS A 1047 ? 0.2521 0.2533 0.2502 0.0392  -0.0100 -0.0144 1045 HIS A N   
7438  C CA  A HIS A 1047 ? 0.2808 0.2892 0.2820 0.0380  -0.0091 -0.0169 1045 HIS A CA  
7439  C CA  B HIS A 1047 ? 0.2807 0.2891 0.2819 0.0381  -0.0092 -0.0170 1045 HIS A CA  
7440  C C   . HIS A 1047 ? 0.2642 0.2772 0.2659 0.0375  -0.0097 -0.0177 1045 HIS A C   
7441  O O   . HIS A 1047 ? 0.2762 0.2868 0.2756 0.0365  -0.0097 -0.0161 1045 HIS A O   
7442  C CB  A HIS A 1047 ? 0.2955 0.3041 0.2967 0.0345  -0.0067 -0.0163 1045 HIS A CB  
7443  C CB  B HIS A 1047 ? 0.2952 0.3039 0.2967 0.0350  -0.0069 -0.0166 1045 HIS A CB  
7444  C CG  A HIS A 1047 ? 0.2753 0.2908 0.2789 0.0322  -0.0057 -0.0178 1045 HIS A CG  
7445  C CG  B HIS A 1047 ? 0.2779 0.2823 0.2790 0.0356  -0.0065 -0.0160 1045 HIS A CG  
7446  N ND1 A HIS A 1047 ? 0.2821 0.3039 0.2888 0.0326  -0.0054 -0.0202 1045 HIS A ND1 
7447  N ND1 B HIS A 1047 ? 0.2716 0.2774 0.2748 0.0380  -0.0074 -0.0181 1045 HIS A ND1 
7448  C CD2 A HIS A 1047 ? 0.2877 0.3050 0.2913 0.0294  -0.0049 -0.0172 1045 HIS A CD2 
7449  C CD2 B HIS A 1047 ? 0.3029 0.3016 0.3018 0.0342  -0.0054 -0.0138 1045 HIS A CD2 
7450  C CE1 A HIS A 1047 ? 0.2873 0.3146 0.2957 0.0299  -0.0045 -0.0207 1045 HIS A CE1 
7451  C CE1 B HIS A 1047 ? 0.2743 0.2754 0.2768 0.0380  -0.0070 -0.0173 1045 HIS A CE1 
7452  N NE2 A HIS A 1047 ? 0.2149 0.2392 0.2215 0.0279  -0.0042 -0.0189 1045 HIS A NE2 
7453  N NE2 B HIS A 1047 ? 0.2976 0.2943 0.2974 0.0356  -0.0057 -0.0146 1045 HIS A NE2 
7454  N N   . THR A 1048 ? 0.2592 0.2790 0.2641 0.0383  -0.0103 -0.0203 1046 THR A N   
7455  C CA  . THR A 1048 ? 0.2780 0.3032 0.2842 0.0377  -0.0110 -0.0215 1046 THR A CA  
7456  C C   . THR A 1048 ? 0.2564 0.2880 0.2654 0.0347  -0.0093 -0.0228 1046 THR A C   
7457  O O   . THR A 1048 ? 0.2601 0.2956 0.2715 0.0351  -0.0087 -0.0244 1046 THR A O   
7458  C CB  . THR A 1048 ? 0.2636 0.2920 0.2713 0.0413  -0.0133 -0.0233 1046 THR A CB  
7459  O OG1 . THR A 1048 ? 0.2645 0.2866 0.2696 0.0441  -0.0149 -0.0217 1046 THR A OG1 
7460  C CG2 . THR A 1048 ? 0.2492 0.2822 0.2576 0.0407  -0.0142 -0.0242 1046 THR A CG2 
7461  N N   . ASP A 1049 ? 0.2494 0.2820 0.2583 0.0318  -0.0086 -0.0221 1047 ASP A N   
7462  C CA  . ASP A 1049 ? 0.2366 0.2753 0.2484 0.0286  -0.0073 -0.0230 1047 ASP A CA  
7463  C C   . ASP A 1049 ? 0.2136 0.2605 0.2291 0.0301  -0.0081 -0.0257 1047 ASP A C   
7464  O O   . ASP A 1049 ? 0.2203 0.2692 0.2363 0.0321  -0.0099 -0.0269 1047 ASP A O   
7465  C CB  . ASP A 1049 ? 0.2130 0.2514 0.2245 0.0255  -0.0070 -0.0220 1047 ASP A CB  
7466  C CG  . ASP A 1049 ? 0.2288 0.2729 0.2435 0.0219  -0.0057 -0.0223 1047 ASP A CG  
7467  O OD1 . ASP A 1049 ? 0.2486 0.2998 0.2665 0.0216  -0.0062 -0.0241 1047 ASP A OD1 
7468  O OD2 . ASP A 1049 ? 0.2570 0.2985 0.2710 0.0193  -0.0041 -0.0207 1047 ASP A OD2 
7469  N N   . PRO A 1050 ? 0.2139 0.2662 0.2319 0.0292  -0.0069 -0.0269 1048 PRO A N   
7470  C CA  . PRO A 1050 ? 0.2119 0.2728 0.2336 0.0309  -0.0077 -0.0297 1048 PRO A CA  
7471  C C   . PRO A 1050 ? 0.2215 0.2890 0.2458 0.0285  -0.0078 -0.0304 1048 PRO A C   
7472  O O   . PRO A 1050 ? 0.2252 0.2991 0.2523 0.0303  -0.0091 -0.0327 1048 PRO A O   
7473  C CB  . PRO A 1050 ? 0.2821 0.3468 0.3053 0.0304  -0.0060 -0.0305 1048 PRO A CB  
7474  C CG  . PRO A 1050 ? 0.2399 0.3003 0.2612 0.0267  -0.0041 -0.0279 1048 PRO A CG  
7475  C CD  . PRO A 1050 ? 0.2379 0.2890 0.2555 0.0271  -0.0048 -0.0257 1048 PRO A CD  
7476  N N   . VAL A 1051 ? 0.2126 0.2789 0.2367 0.0245  -0.0068 -0.0286 1049 VAL A N   
7477  C CA  . VAL A 1051 ? 0.2202 0.2922 0.2471 0.0221  -0.0072 -0.0292 1049 VAL A CA  
7478  C C   . VAL A 1051 ? 0.2111 0.2807 0.2368 0.0239  -0.0094 -0.0297 1049 VAL A C   
7479  O O   . VAL A 1051 ? 0.2115 0.2870 0.2399 0.0242  -0.0106 -0.0315 1049 VAL A O   
7480  C CB  . VAL A 1051 ? 0.2077 0.2788 0.2349 0.0172  -0.0056 -0.0271 1049 VAL A CB  
7481  C CG1 . VAL A 1051 ? 0.2606 0.3371 0.2910 0.0145  -0.0063 -0.0277 1049 VAL A CG1 
7482  C CG2 . VAL A 1051 ? 0.2149 0.2895 0.2433 0.0155  -0.0035 -0.0265 1049 VAL A CG2 
7483  N N   . LEU A 1052 ? 0.2125 0.2736 0.2342 0.0253  -0.0099 -0.0282 1050 LEU A N   
7484  C CA  . LEU A 1052 ? 0.2149 0.2738 0.2349 0.0278  -0.0120 -0.0287 1050 LEU A CA  
7485  C C   . LEU A 1052 ? 0.2162 0.2799 0.2380 0.0316  -0.0137 -0.0309 1050 LEU A C   
7486  O O   . LEU A 1052 ? 0.2173 0.2849 0.2405 0.0326  -0.0154 -0.0324 1050 LEU A O   
7487  C CB  . LEU A 1052 ? 0.2164 0.2662 0.2317 0.0291  -0.0121 -0.0266 1050 LEU A CB  
7488  C CG  . LEU A 1052 ? 0.2217 0.2683 0.2342 0.0319  -0.0142 -0.0264 1050 LEU A CG  
7489  C CD1 . LEU A 1052 ? 0.2216 0.2688 0.2340 0.0363  -0.0159 -0.0273 1050 LEU A CD1 
7490  C CD2 . LEU A 1052 ? 0.2197 0.2703 0.2337 0.0307  -0.0154 -0.0277 1050 LEU A CD2 
7491  N N   . LEU A 1053 ? 0.2164 0.2798 0.2382 0.0340  -0.0133 -0.0314 1051 LEU A N   
7492  C CA  . LEU A 1053 ? 0.2283 0.2957 0.2519 0.0380  -0.0151 -0.0337 1051 LEU A CA  
7493  C C   . LEU A 1053 ? 0.2167 0.2946 0.2451 0.0371  -0.0152 -0.0362 1051 LEU A C   
7494  O O   . LEU A 1053 ? 0.2182 0.3001 0.2482 0.0396  -0.0172 -0.0380 1051 LEU A O   
7495  C CB  . LEU A 1053 ? 0.2368 0.3019 0.2601 0.0404  -0.0147 -0.0339 1051 LEU A CB  
7496  C CG  . LEU A 1053 ? 0.2351 0.2903 0.2542 0.0422  -0.0152 -0.0317 1051 LEU A CG  
7497  C CD1 . LEU A 1053 ? 0.2444 0.2978 0.2638 0.0441  -0.0148 -0.0323 1051 LEU A CD1 
7498  C CD2 . LEU A 1053 ? 0.2412 0.2936 0.2585 0.0454  -0.0178 -0.0314 1051 LEU A CD2 
7499  N N   . ASP A 1054 ? 0.2210 0.3036 0.2516 0.0336  -0.0132 -0.0362 1052 ASP A N   
7500  C CA  . ASP A 1054 ? 0.2129 0.3060 0.2482 0.0322  -0.0131 -0.0383 1052 ASP A CA  
7501  C C   . ASP A 1054 ? 0.2135 0.3080 0.2496 0.0308  -0.0145 -0.0384 1052 ASP A C   
7502  O O   . ASP A 1054 ? 0.2300 0.3317 0.2692 0.0319  -0.0158 -0.0406 1052 ASP A O   
7503  C CB  . ASP A 1054 ? 0.2103 0.3078 0.2476 0.0281  -0.0106 -0.0376 1052 ASP A CB  
7504  C CG  . ASP A 1054 ? 0.2757 0.3740 0.3129 0.0297  -0.0093 -0.0382 1052 ASP A CG  
7505  O OD1 . ASP A 1054 ? 0.2592 0.3565 0.2959 0.0341  -0.0106 -0.0399 1052 ASP A OD1 
7506  O OD2 . ASP A 1054 ? 0.3028 0.4029 0.3404 0.0265  -0.0072 -0.0370 1052 ASP A OD2 
7507  N N   . PHE A 1055 ? 0.2136 0.3016 0.2470 0.0283  -0.0142 -0.0362 1053 PHE A N   
7508  C CA  . PHE A 1055 ? 0.2144 0.3033 0.2485 0.0270  -0.0157 -0.0366 1053 PHE A CA  
7509  C C   . PHE A 1055 ? 0.2171 0.3053 0.2498 0.0313  -0.0183 -0.0379 1053 PHE A C   
7510  O O   . PHE A 1055 ? 0.2221 0.3158 0.2573 0.0314  -0.0199 -0.0397 1053 PHE A O   
7511  C CB  . PHE A 1055 ? 0.2144 0.2957 0.2455 0.0240  -0.0150 -0.0342 1053 PHE A CB  
7512  C CG  . PHE A 1055 ? 0.2155 0.2973 0.2472 0.0226  -0.0165 -0.0348 1053 PHE A CG  
7513  C CD1 . PHE A 1055 ? 0.2382 0.3277 0.2745 0.0200  -0.0170 -0.0363 1053 PHE A CD1 
7514  C CD2 . PHE A 1055 ? 0.2174 0.2923 0.2451 0.0238  -0.0176 -0.0340 1053 PHE A CD2 
7515  C CE1 . PHE A 1055 ? 0.2540 0.3439 0.2911 0.0186  -0.0186 -0.0371 1053 PHE A CE1 
7516  C CE2 . PHE A 1055 ? 0.2187 0.2943 0.2469 0.0226  -0.0192 -0.0349 1053 PHE A CE2 
7517  C CZ  . PHE A 1055 ? 0.2181 0.3010 0.2511 0.0201  -0.0198 -0.0366 1053 PHE A CZ  
7518  N N   . ALA A 1056 ? 0.2188 0.3004 0.2478 0.0347  -0.0189 -0.0370 1054 ALA A N   
7519  C CA  . ALA A 1056 ? 0.2218 0.3026 0.2494 0.0388  -0.0215 -0.0378 1054 ALA A CA  
7520  C C   . ALA A 1056 ? 0.2413 0.3306 0.2731 0.0415  -0.0228 -0.0407 1054 ALA A C   
7521  O O   . ALA A 1056 ? 0.2485 0.3410 0.2811 0.0433  -0.0249 -0.0421 1054 ALA A O   
7522  C CB  . ALA A 1056 ? 0.2426 0.3148 0.2658 0.0418  -0.0218 -0.0359 1054 ALA A CB  
7523  N N   . LYS A 1057 ? 0.2305 0.3238 0.2648 0.0417  -0.0215 -0.0417 1055 LYS A N   
7524  C CA  . LYS A 1057 ? 0.2425 0.3449 0.2810 0.0441  -0.0225 -0.0448 1055 LYS A CA  
7525  C C   . LYS A 1057 ? 0.2652 0.3764 0.3079 0.0411  -0.0226 -0.0463 1055 LYS A C   
7526  O O   . LYS A 1057 ? 0.2950 0.4124 0.3403 0.0433  -0.0245 -0.0486 1055 LYS A O   
7527  C CB  . LYS A 1057 ? 0.2481 0.3536 0.2886 0.0447  -0.0209 -0.0458 1055 LYS A CB  
7528  C CG  . LYS A 1057 ? 0.3284 0.4268 0.3661 0.0488  -0.0217 -0.0454 1055 LYS A CG  
7529  C CD  . LYS A 1057 ? 0.3154 0.4183 0.3556 0.0501  -0.0206 -0.0474 1055 LYS A CD  
7530  C CE  . LYS A 1057 ? 0.3017 0.4060 0.3422 0.0456  -0.0175 -0.0462 1055 LYS A CE  
7531  N NZ  . LYS A 1057 ? 0.3455 0.4513 0.3869 0.0473  -0.0165 -0.0476 1055 LYS A NZ  
7532  N N   . TRP A 1058 ? 0.2354 0.3473 0.2788 0.0361  -0.0206 -0.0450 1056 TRP A N   
7533  C CA  . TRP A 1058 ? 0.2604 0.3798 0.3078 0.0328  -0.0207 -0.0460 1056 TRP A CA  
7534  C C   . TRP A 1058 ? 0.2870 0.4048 0.3334 0.0337  -0.0232 -0.0465 1056 TRP A C   
7535  O O   . TRP A 1058 ? 0.2880 0.4135 0.3381 0.0337  -0.0246 -0.0486 1056 TRP A O   
7536  C CB  . TRP A 1058 ? 0.2567 0.3751 0.3045 0.0272  -0.0184 -0.0439 1056 TRP A CB  
7537  C CG  . TRP A 1058 ? 0.2718 0.3966 0.3237 0.0232  -0.0187 -0.0445 1056 TRP A CG  
7538  C CD1 . TRP A 1058 ? 0.3309 0.4661 0.3879 0.0209  -0.0178 -0.0457 1056 TRP A CD1 
7539  C CD2 . TRP A 1058 ? 0.3132 0.4349 0.3646 0.0210  -0.0199 -0.0440 1056 TRP A CD2 
7540  N NE1 . TRP A 1058 ? 0.3545 0.4928 0.4144 0.0171  -0.0186 -0.0457 1056 TRP A NE1 
7541  C CE2 . TRP A 1058 ? 0.3053 0.4351 0.3618 0.0172  -0.0199 -0.0449 1056 TRP A CE2 
7542  C CE3 . TRP A 1058 ? 0.2559 0.3687 0.3030 0.0218  -0.0211 -0.0430 1056 TRP A CE3 
7543  C CZ2 . TRP A 1058 ? 0.3085 0.4376 0.3662 0.0142  -0.0212 -0.0449 1056 TRP A CZ2 
7544  C CZ3 . TRP A 1058 ? 0.2790 0.3915 0.3271 0.0191  -0.0223 -0.0432 1056 TRP A CZ3 
7545  C CH2 . TRP A 1058 ? 0.3006 0.4210 0.3541 0.0154  -0.0224 -0.0443 1056 TRP A CH2 
7546  N N   . LEU A 1059 ? 0.2465 0.3550 0.2881 0.0344  -0.0238 -0.0446 1057 LEU A N   
7547  C CA  . LEU A 1059 ? 0.2427 0.3498 0.2828 0.0355  -0.0262 -0.0452 1057 LEU A CA  
7548  C C   . LEU A 1059 ? 0.2989 0.4103 0.3400 0.0402  -0.0286 -0.0473 1057 LEU A C   
7549  O O   . LEU A 1059 ? 0.3350 0.4518 0.3784 0.0404  -0.0305 -0.0491 1057 LEU A O   
7550  C CB  . LEU A 1059 ? 0.2409 0.3375 0.2752 0.0362  -0.0262 -0.0427 1057 LEU A CB  
7551  C CG  . LEU A 1059 ? 0.2423 0.3345 0.2755 0.0316  -0.0245 -0.0410 1057 LEU A CG  
7552  C CD1 . LEU A 1059 ? 0.2426 0.3250 0.2701 0.0328  -0.0243 -0.0387 1057 LEU A CD1 
7553  C CD2 . LEU A 1059 ? 0.2351 0.3310 0.2707 0.0289  -0.0258 -0.0424 1057 LEU A CD2 
7554  N N   . ASP A 1060 ? 0.2555 0.3647 0.2953 0.0441  -0.0289 -0.0472 1058 ASP A N   
7555  C CA  . ASP A 1060 ? 0.3452 0.4583 0.3862 0.0489  -0.0314 -0.0492 1058 ASP A CA  
7556  C C   . ASP A 1060 ? 0.3535 0.4784 0.4007 0.0483  -0.0316 -0.0522 1058 ASP A C   
7557  O O   . ASP A 1060 ? 0.3684 0.4985 0.4175 0.0505  -0.0339 -0.0542 1058 ASP A O   
7558  C CB  . ASP A 1060 ? 0.3496 0.4580 0.3887 0.0528  -0.0315 -0.0485 1058 ASP A CB  
7559  C CG  . ASP A 1060 ? 0.3674 0.4666 0.4012 0.0555  -0.0330 -0.0462 1058 ASP A CG  
7560  O OD1 . ASP A 1060 ? 0.3969 0.4961 0.4292 0.0563  -0.0350 -0.0462 1058 ASP A OD1 
7561  O OD2 . ASP A 1060 ? 0.3472 0.4395 0.3782 0.0567  -0.0323 -0.0444 1058 ASP A OD2 
7562  N N   . GLY A 1061 ? 0.3276 0.4570 0.3778 0.0454  -0.0291 -0.0526 1059 GLY A N   
7563  C CA  . GLY A 1061 ? 0.3266 0.4678 0.3827 0.0443  -0.0290 -0.0553 1059 GLY A CA  
7564  C C   . GLY A 1061 ? 0.3527 0.4985 0.4112 0.0413  -0.0301 -0.0560 1059 GLY A C   
7565  O O   . GLY A 1061 ? 0.3351 0.4901 0.3979 0.0421  -0.0314 -0.0586 1059 GLY A O   
7566  N N   . LYS A 1062 ? 0.3250 0.4646 0.3809 0.0380  -0.0297 -0.0539 1060 LYS A N   
7567  C CA  . LYS A 1062 ? 0.3419 0.4850 0.4000 0.0350  -0.0308 -0.0547 1060 LYS A CA  
7568  C C   . LYS A 1062 ? 0.3600 0.5014 0.4160 0.0384  -0.0340 -0.0558 1060 LYS A C   
7569  O O   . LYS A 1062 ? 0.3843 0.5293 0.4424 0.0364  -0.0354 -0.0570 1060 LYS A O   
7570  C CB  . LYS A 1062 ? 0.3460 0.4833 0.4026 0.0300  -0.0293 -0.0524 1060 LYS A CB  
7571  C CG  . LYS A 1062 ? 0.3557 0.4962 0.4153 0.0255  -0.0264 -0.0513 1060 LYS A CG  
7572  C CD  . LYS A 1062 ? 0.3968 0.5490 0.4629 0.0228  -0.0265 -0.0532 1060 LYS A CD  
7573  C CE  . LYS A 1062 ? 0.4397 0.5950 0.5085 0.0178  -0.0238 -0.0515 1060 LYS A CE  
7574  N NZ  . LYS A 1062 ? 0.4390 0.6063 0.5143 0.0149  -0.0237 -0.0530 1060 LYS A NZ  
7575  N N   . GLY A 1063 ? 0.3167 0.4530 0.3688 0.0432  -0.0352 -0.0553 1061 GLY A N   
7576  C CA  . GLY A 1063 ? 0.3560 0.4904 0.4056 0.0466  -0.0382 -0.0558 1061 GLY A CA  
7577  C C   . GLY A 1063 ? 0.3835 0.5083 0.4274 0.0460  -0.0383 -0.0535 1061 GLY A C   
7578  O O   . GLY A 1063 ? 0.3680 0.4909 0.4091 0.0488  -0.0407 -0.0536 1061 GLY A O   
7579  N N   . ALA A 1064 ? 0.2995 0.4185 0.3415 0.0426  -0.0358 -0.0514 1062 ALA A N   
7580  C CA  . ALA A 1064 ? 0.2918 0.4020 0.3286 0.0419  -0.0357 -0.0492 1062 ALA A CA  
7581  C C   . ALA A 1064 ? 0.3299 0.4326 0.3617 0.0456  -0.0357 -0.0470 1062 ALA A C   
7582  O O   . ALA A 1064 ? 0.2703 0.3669 0.2997 0.0446  -0.0336 -0.0448 1062 ALA A O   
7583  C CB  . ALA A 1064 ? 0.2725 0.3800 0.3099 0.0367  -0.0333 -0.0480 1062 ALA A CB  
7584  N N   . ARG A 1065 ? 0.2978 0.4013 0.3283 0.0501  -0.0382 -0.0476 1063 ARG A N   
7585  C CA  . ARG A 1065 ? 0.3029 0.4005 0.3297 0.0539  -0.0386 -0.0456 1063 ARG A CA  
7586  C C   . ARG A 1065 ? 0.2905 0.3789 0.3114 0.0535  -0.0379 -0.0426 1063 ARG A C   
7587  O O   . ARG A 1065 ? 0.3181 0.4003 0.3365 0.0541  -0.0366 -0.0403 1063 ARG A O   
7588  C CB  . ARG A 1065 ? 0.3384 0.4392 0.3655 0.0587  -0.0417 -0.0467 1063 ARG A CB  
7589  C CG  . ARG A 1065 ? 0.4058 0.5166 0.4389 0.0593  -0.0426 -0.0501 1063 ARG A CG  
7590  C CD  . ARG A 1065 ? 0.4279 0.5408 0.4643 0.0591  -0.0406 -0.0507 1063 ARG A CD  
7591  N NE  . ARG A 1065 ? 0.4891 0.6123 0.5312 0.0600  -0.0415 -0.0540 1063 ARG A NE  
7592  C CZ  . ARG A 1065 ? 0.4776 0.6046 0.5230 0.0613  -0.0406 -0.0553 1063 ARG A CZ  
7593  N NH1 . ARG A 1065 ? 0.4599 0.5812 0.5035 0.0617  -0.0390 -0.0538 1063 ARG A NH1 
7594  N NH2 . ARG A 1065 ? 0.4303 0.5675 0.4811 0.0622  -0.0415 -0.0585 1063 ARG A NH2 
7595  N N   . ALA A 1066 ? 0.2928 0.3806 0.3114 0.0526  -0.0389 -0.0426 1064 ALA A N   
7596  C CA  . ALA A 1066 ? 0.2822 0.3621 0.2953 0.0522  -0.0383 -0.0399 1064 ALA A CA  
7597  C C   . ALA A 1066 ? 0.2934 0.3691 0.3063 0.0483  -0.0352 -0.0387 1064 ALA A C   
7598  O O   . ALA A 1066 ? 0.2772 0.3459 0.2863 0.0486  -0.0340 -0.0360 1064 ALA A O   
7599  C CB  . ALA A 1066 ? 0.2816 0.3627 0.2926 0.0520  -0.0400 -0.0408 1064 ALA A CB  
7600  N N   . GLU A 1067 ? 0.2686 0.3486 0.2859 0.0447  -0.0341 -0.0404 1065 GLU A N   
7601  C CA  . GLU A 1067 ? 0.2711 0.3474 0.2885 0.0409  -0.0313 -0.0391 1065 GLU A CA  
7602  C C   . GLU A 1067 ? 0.2559 0.3299 0.2735 0.0417  -0.0295 -0.0377 1065 GLU A C   
7603  O O   . GLU A 1067 ? 0.2694 0.3373 0.2846 0.0404  -0.0276 -0.0356 1065 GLU A O   
7604  C CB  . GLU A 1067 ? 0.2771 0.3590 0.2995 0.0368  -0.0308 -0.0411 1065 GLU A CB  
7605  C CG  . GLU A 1067 ? 0.2575 0.3403 0.2798 0.0353  -0.0323 -0.0425 1065 GLU A CG  
7606  C CD  . GLU A 1067 ? 0.3648 0.4546 0.3893 0.0372  -0.0350 -0.0451 1065 GLU A CD  
7607  O OE1 . GLU A 1067 ? 0.3142 0.4076 0.3397 0.0404  -0.0360 -0.0457 1065 GLU A OE1 
7608  O OE2 . GLU A 1067 ? 0.4258 0.5175 0.4512 0.0355  -0.0364 -0.0468 1065 GLU A OE2 
7609  N N   . ALA A 1068 ? 0.2487 0.3276 0.2693 0.0440  -0.0303 -0.0391 1066 ALA A N   
7610  C CA  . ALA A 1068 ? 0.2411 0.3182 0.2620 0.0453  -0.0290 -0.0382 1066 ALA A CA  
7611  C C   . ALA A 1068 ? 0.2936 0.3624 0.3095 0.0479  -0.0292 -0.0356 1066 ALA A C   
7612  O O   . ALA A 1068 ? 0.2791 0.3430 0.2937 0.0472  -0.0274 -0.0339 1066 ALA A O   
7613  C CB  . ALA A 1068 ? 0.2715 0.3559 0.2966 0.0479  -0.0302 -0.0406 1066 ALA A CB  
7614  N N   . GLU A 1069 ? 0.2674 0.3348 0.2806 0.0510  -0.0316 -0.0351 1067 GLU A N   
7615  C CA  . GLU A 1069 ? 0.2877 0.3473 0.2960 0.0532  -0.0319 -0.0322 1067 GLU A CA  
7616  C C   . GLU A 1069 ? 0.2985 0.3522 0.3034 0.0503  -0.0299 -0.0300 1067 GLU A C   
7617  O O   . GLU A 1069 ? 0.2787 0.3262 0.2811 0.0504  -0.0287 -0.0276 1067 GLU A O   
7618  C CB  . GLU A 1069 ? 0.3364 0.3964 0.3423 0.0566  -0.0349 -0.0319 1067 GLU A CB  
7619  C CG  . GLU A 1069 ? 0.3950 0.4473 0.3955 0.0585  -0.0353 -0.0284 1067 GLU A CG  
7620  C CD  . GLU A 1069 ? 0.5117 0.5603 0.5124 0.0613  -0.0358 -0.0271 1067 GLU A CD  
7621  O OE1 . GLU A 1069 ? 0.5735 0.6262 0.5784 0.0626  -0.0362 -0.0293 1067 GLU A OE1 
7622  O OE2 . GLU A 1069 ? 0.5672 0.6091 0.5641 0.0622  -0.0357 -0.0239 1067 GLU A OE2 
7623  N N   . ALA A 1070 ? 0.2831 0.3384 0.2879 0.0476  -0.0297 -0.0309 1068 ALA A N   
7624  C CA  . ALA A 1070 ? 0.2744 0.3246 0.2764 0.0448  -0.0278 -0.0292 1068 ALA A CA  
7625  C C   . ALA A 1070 ? 0.2744 0.3228 0.2782 0.0421  -0.0252 -0.0286 1068 ALA A C   
7626  O O   . ALA A 1070 ? 0.2835 0.3260 0.2846 0.0410  -0.0236 -0.0264 1068 ALA A O   
7627  C CB  . ALA A 1070 ? 0.3195 0.3725 0.3220 0.0426  -0.0284 -0.0309 1068 ALA A CB  
7628  N N   . ALA A 1071 ? 0.2506 0.3045 0.2591 0.0408  -0.0247 -0.0305 1069 ALA A N   
7629  C CA  . ALA A 1071 ? 0.2369 0.2898 0.2471 0.0384  -0.0223 -0.0299 1069 ALA A CA  
7630  C C   . ALA A 1071 ? 0.2783 0.3265 0.2866 0.0407  -0.0217 -0.0282 1069 ALA A C   
7631  O O   . ALA A 1071 ? 0.2322 0.2752 0.2387 0.0392  -0.0199 -0.0263 1069 ALA A O   
7632  C CB  . ALA A 1071 ? 0.2295 0.2904 0.2451 0.0369  -0.0220 -0.0323 1069 ALA A CB  
7633  N N   . ARG A 1072 ? 0.2726 0.3221 0.2813 0.0444  -0.0235 -0.0288 1070 ARG A N   
7634  C CA  . ARG A 1072 ? 0.2503 0.2948 0.2574 0.0468  -0.0233 -0.0273 1070 ARG A CA  
7635  C C   . ARG A 1072 ? 0.2402 0.2768 0.2424 0.0470  -0.0231 -0.0242 1070 ARG A C   
7636  O O   . ARG A 1072 ? 0.2831 0.3146 0.2839 0.0465  -0.0217 -0.0224 1070 ARG A O   
7637  C CB  . ARG A 1072 ? 0.2348 0.2819 0.2433 0.0511  -0.0258 -0.0286 1070 ARG A CB  
7638  C CG  . ARG A 1072 ? 0.2941 0.3490 0.3078 0.0513  -0.0257 -0.0317 1070 ARG A CG  
7639  C CD  . ARG A 1072 ? 0.3505 0.4072 0.3657 0.0558  -0.0281 -0.0330 1070 ARG A CD  
7640  N NE  . ARG A 1072 ? 0.3629 0.4214 0.3772 0.0580  -0.0307 -0.0333 1070 ARG A NE  
7641  C CZ  . ARG A 1072 ? 0.3638 0.4301 0.3812 0.0580  -0.0317 -0.0359 1070 ARG A CZ  
7642  N NH1 . ARG A 1072 ? 0.3775 0.4508 0.3993 0.0560  -0.0305 -0.0383 1070 ARG A NH1 
7643  N NH2 . ARG A 1072 ? 0.3878 0.4551 0.4040 0.0601  -0.0342 -0.0359 1070 ARG A NH2 
7644  N N   . ASN A 1073 ? 0.2469 0.2828 0.2462 0.0475  -0.0244 -0.0235 1071 ASN A N   
7645  C CA  . ASN A 1073 ? 0.2702 0.2996 0.2648 0.0474  -0.0240 -0.0206 1071 ASN A CA  
7646  C C   . ASN A 1073 ? 0.3041 0.3305 0.2980 0.0438  -0.0214 -0.0197 1071 ASN A C   
7647  O O   . ASN A 1073 ? 0.2802 0.3009 0.2715 0.0436  -0.0202 -0.0173 1071 ASN A O   
7648  C CB  . ASN A 1073 ? 0.3216 0.3521 0.3135 0.0486  -0.0258 -0.0205 1071 ASN A CB  
7649  C CG  . ASN A 1073 ? 0.3974 0.4290 0.3888 0.0525  -0.0284 -0.0202 1071 ASN A CG  
7650  O OD1 . ASN A 1073 ? 0.4519 0.4810 0.4437 0.0547  -0.0290 -0.0192 1071 ASN A OD1 
7651  N ND2 . ASN A 1073 ? 0.4449 0.4802 0.4355 0.0536  -0.0303 -0.0212 1071 ASN A ND2 
7652  N N   . ALA A 1074 ? 0.2372 0.2674 0.2336 0.0409  -0.0205 -0.0216 1072 ALA A N   
7653  C CA  . ALA A 1074 ? 0.2300 0.2574 0.2261 0.0375  -0.0182 -0.0207 1072 ALA A CA  
7654  C C   . ALA A 1074 ? 0.2299 0.2552 0.2272 0.0369  -0.0165 -0.0199 1072 ALA A C   
7655  O O   . ALA A 1074 ? 0.2462 0.2665 0.2415 0.0355  -0.0149 -0.0180 1072 ALA A O   
7656  C CB  . ALA A 1074 ? 0.2706 0.3027 0.2699 0.0345  -0.0179 -0.0228 1072 ALA A CB  
7657  N N   . GLY A 1075 ? 0.2417 0.2708 0.2421 0.0381  -0.0169 -0.0213 1073 GLY A N   
7658  C CA  . GLY A 1075 ? 0.2604 0.2880 0.2619 0.0379  -0.0155 -0.0209 1073 GLY A CA  
7659  C C   . GLY A 1075 ? 0.2692 0.2899 0.2675 0.0397  -0.0155 -0.0185 1073 GLY A C   
7660  O O   . GLY A 1075 ? 0.2498 0.2669 0.2475 0.0384  -0.0138 -0.0173 1073 GLY A O   
7661  N N   . SER A 1076 ? 0.2521 0.2710 0.2483 0.0427  -0.0175 -0.0177 1074 SER A N   
7662  C CA  . SER A 1076 ? 0.3037 0.3161 0.2970 0.0444  -0.0178 -0.0151 1074 SER A CA  
7663  C C   . SER A 1076 ? 0.2838 0.2914 0.2733 0.0425  -0.0165 -0.0126 1074 SER A C   
7664  O O   . SER A 1076 ? 0.3099 0.3124 0.2979 0.0420  -0.0155 -0.0105 1074 SER A O   
7665  C CB  . SER A 1076 ? 0.3019 0.3139 0.2941 0.0481  -0.0205 -0.0146 1074 SER A CB  
7666  O OG  . SER A 1076 ? 0.3759 0.3906 0.3714 0.0503  -0.0217 -0.0166 1074 SER A OG  
7667  N N   . SER A 1077 ? 0.2608 0.2703 0.2490 0.0414  -0.0167 -0.0129 1075 SER A N   
7668  C CA  . SER A 1077 ? 0.3001 0.3059 0.2848 0.0400  -0.0157 -0.0109 1075 SER A CA  
7669  C C   . SER A 1077 ? 0.3094 0.3137 0.2949 0.0367  -0.0133 -0.0109 1075 SER A C   
7670  O O   . SER A 1077 ? 0.2822 0.2823 0.2651 0.0357  -0.0121 -0.0089 1075 SER A O   
7671  C CB  . SER A 1077 ? 0.3252 0.3338 0.3084 0.0401  -0.0168 -0.0118 1075 SER A CB  
7672  O OG  . SER A 1077 ? 0.4346 0.4442 0.4163 0.0432  -0.0190 -0.0114 1075 SER A OG  
7673  N N   . SER A 1078 ? 0.2284 0.2362 0.2175 0.0351  -0.0125 -0.0129 1076 SER A N   
7674  C CA  . SER A 1078 ? 0.2325 0.2390 0.2225 0.0320  -0.0104 -0.0126 1076 SER A CA  
7675  C C   . SER A 1078 ? 0.2490 0.2503 0.2375 0.0322  -0.0092 -0.0105 1076 SER A C   
7676  O O   . SER A 1078 ? 0.2494 0.2497 0.2382 0.0342  -0.0099 -0.0101 1076 SER A O   
7677  C CB  . SER A 1078 ? 0.2402 0.2517 0.2344 0.0305  -0.0099 -0.0146 1076 SER A CB  
7678  O OG  . SER A 1078 ? 0.2265 0.2366 0.2214 0.0276  -0.0079 -0.0140 1076 SER A OG  
7679  N N   . ALA A 1079 ? 0.2242 0.2224 0.2113 0.0300  -0.0076 -0.0092 1077 ALA A N   
7680  C CA  . ALA A 1079 ? 0.2286 0.2224 0.2148 0.0297  -0.0064 -0.0074 1077 ALA A CA  
7681  C C   . ALA A 1079 ? 0.2405 0.2355 0.2294 0.0274  -0.0048 -0.0081 1077 ALA A C   
7682  O O   . ALA A 1079 ? 0.2197 0.2114 0.2080 0.0265  -0.0035 -0.0068 1077 ALA A O   
7683  C CB  . ALA A 1079 ? 0.2577 0.2471 0.2405 0.0291  -0.0056 -0.0052 1077 ALA A CB  
7684  N N   . LEU A 1080 ? 0.2404 0.2405 0.2322 0.0262  -0.0049 -0.0101 1078 LEU A N   
7685  C CA  . LEU A 1080 ? 0.2160 0.2182 0.2103 0.0241  -0.0035 -0.0107 1078 LEU A CA  
7686  C C   . LEU A 1080 ? 0.2308 0.2318 0.2255 0.0255  -0.0032 -0.0105 1078 LEU A C   
7687  O O   . LEU A 1080 ? 0.2329 0.2348 0.2281 0.0282  -0.0045 -0.0114 1078 LEU A O   
7688  C CB  . LEU A 1080 ? 0.2155 0.2242 0.2131 0.0232  -0.0040 -0.0128 1078 LEU A CB  
7689  C CG  . LEU A 1080 ? 0.2124 0.2246 0.2128 0.0213  -0.0027 -0.0134 1078 LEU A CG  
7690  C CD1 . LEU A 1080 ? 0.2107 0.2213 0.2111 0.0179  -0.0012 -0.0121 1078 LEU A CD1 
7691  C CD2 . LEU A 1080 ? 0.2278 0.2474 0.2316 0.0213  -0.0034 -0.0155 1078 LEU A CD2 
7692  N N   . GLY A 1081 ? 0.2145 0.2133 0.2091 0.0239  -0.0017 -0.0095 1079 GLY A N   
7693  C CA  . GLY A 1081 ? 0.2583 0.2559 0.2534 0.0250  -0.0014 -0.0096 1079 GLY A CA  
7694  C C   . GLY A 1081 ? 0.2751 0.2663 0.2676 0.0260  -0.0014 -0.0076 1079 GLY A C   
7695  O O   . GLY A 1081 ? 0.2393 0.2286 0.2322 0.0268  -0.0013 -0.0075 1079 GLY A O   
7696  N N   . LEU A 1082 ? 0.2178 0.2058 0.2077 0.0260  -0.0016 -0.0060 1080 LEU A N   
7697  C CA  A LEU A 1082 ? 0.2289 0.2113 0.2163 0.0263  -0.0013 -0.0037 1080 LEU A CA  
7698  C CA  B LEU A 1082 ? 0.2310 0.2133 0.2184 0.0264  -0.0013 -0.0037 1080 LEU A CA  
7699  C C   . LEU A 1082 ? 0.2342 0.2147 0.2220 0.0244  0.0003  -0.0031 1080 LEU A C   
7700  O O   . LEU A 1082 ? 0.2231 0.2055 0.2118 0.0222  0.0015  -0.0035 1080 LEU A O   
7701  C CB  A LEU A 1082 ? 0.2205 0.2011 0.2052 0.0259  -0.0013 -0.0023 1080 LEU A CB  
7702  C CB  B LEU A 1082 ? 0.2205 0.2012 0.2052 0.0260  -0.0014 -0.0023 1080 LEU A CB  
7703  C CG  A LEU A 1082 ? 0.2339 0.2096 0.2160 0.0260  -0.0008 0.0003  1080 LEU A CG  
7704  C CG  B LEU A 1082 ? 0.2331 0.2087 0.2151 0.0261  -0.0009 0.0003  1080 LEU A CG  
7705  C CD1 A LEU A 1082 ? 0.2547 0.2277 0.2362 0.0283  -0.0021 0.0013  1080 LEU A CD1 
7706  C CD1 B LEU A 1082 ? 0.2344 0.2096 0.2137 0.0271  -0.0017 0.0013  1080 LEU A CD1 
7707  C CD2 A LEU A 1082 ? 0.2285 0.2039 0.2080 0.0257  -0.0008 0.0011  1080 LEU A CD2 
7708  C CD2 B LEU A 1082 ? 0.2229 0.1969 0.2046 0.0236  0.0010  0.0010  1080 LEU A CD2 
7709  N N   . ASP A 1083 ? 0.2403 0.2172 0.2277 0.0253  0.0003  -0.0021 1081 ASP A N   
7710  C CA  . ASP A 1083 ? 0.2854 0.2608 0.2734 0.0237  0.0016  -0.0017 1081 ASP A CA  
7711  C C   . ASP A 1083 ? 0.2741 0.2440 0.2604 0.0242  0.0016  0.0004  1081 ASP A C   
7712  O O   . ASP A 1083 ? 0.3131 0.2810 0.2999 0.0260  0.0005  0.0004  1081 ASP A O   
7713  C CB  . ASP A 1083 ? 0.2880 0.2667 0.2786 0.0242  0.0015  -0.0039 1081 ASP A CB  
7714  C CG  . ASP A 1083 ? 0.3682 0.3464 0.3595 0.0225  0.0029  -0.0037 1081 ASP A CG  
7715  O OD1 . ASP A 1083 ? 0.3978 0.3735 0.3877 0.0207  0.0040  -0.0021 1081 ASP A OD1 
7716  O OD2 . ASP A 1083 ? 0.4618 0.4423 0.4549 0.0232  0.0028  -0.0055 1081 ASP A OD2 
7717  N N   . LEU A 1084 ? 0.2545 0.2221 0.2389 0.0227  0.0027  0.0023  1082 LEU A N   
7718  C CA  . LEU A 1084 ? 0.2532 0.2161 0.2359 0.0229  0.0027  0.0046  1082 LEU A CA  
7719  C C   . LEU A 1084 ? 0.2621 0.2233 0.2449 0.0210  0.0042  0.0054  1082 LEU A C   
7720  O O   . LEU A 1084 ? 0.2769 0.2400 0.2602 0.0192  0.0054  0.0048  1082 LEU A O   
7721  C CB  . LEU A 1084 ? 0.2727 0.2349 0.2528 0.0231  0.0026  0.0063  1082 LEU A CB  
7722  C CG  . LEU A 1084 ? 0.3069 0.2706 0.2864 0.0252  0.0009  0.0059  1082 LEU A CG  
7723  C CD1 . LEU A 1084 ? 0.3454 0.3087 0.3220 0.0253  0.0009  0.0076  1082 LEU A CD1 
7724  C CD2 . LEU A 1084 ? 0.3482 0.3096 0.3285 0.0272  -0.0006 0.0063  1082 LEU A CD2 
7725  N N   . GLU A 1085 ? 0.2863 0.2438 0.2689 0.0212  0.0041  0.0069  1083 GLU A N   
7726  C CA  . GLU A 1085 ? 0.2906 0.2460 0.2729 0.0194  0.0055  0.0081  1083 GLU A CA  
7727  C C   . GLU A 1085 ? 0.2805 0.2336 0.2604 0.0191  0.0059  0.0107  1083 GLU A C   
7728  O O   . GLU A 1085 ? 0.3273 0.2785 0.3062 0.0203  0.0048  0.0122  1083 GLU A O   
7729  C CB  . GLU A 1085 ? 0.3151 0.2684 0.2991 0.0195  0.0052  0.0079  1083 GLU A CB  
7730  C CG  . GLU A 1085 ? 0.3194 0.2709 0.3031 0.0176  0.0066  0.0091  1083 GLU A CG  
7731  C CD  . GLU A 1085 ? 0.3585 0.3086 0.3442 0.0175  0.0063  0.0084  1083 GLU A CD  
7732  O OE1 . GLU A 1085 ? 0.4275 0.3784 0.4147 0.0189  0.0052  0.0065  1083 GLU A OE1 
7733  O OE2 . GLU A 1085 ? 0.4066 0.3551 0.3922 0.0161  0.0073  0.0094  1083 GLU A OE2 
7734  N N   . LEU A 1086 ? 0.2593 0.2130 0.2384 0.0175  0.0073  0.0112  1084 LEU A N   
7735  C CA  . LEU A 1086 ? 0.2696 0.2222 0.2465 0.0172  0.0078  0.0133  1084 LEU A CA  
7736  C C   . LEU A 1086 ? 0.3150 0.2649 0.2920 0.0161  0.0087  0.0151  1084 LEU A C   
7737  O O   . LEU A 1086 ? 0.2821 0.2317 0.2607 0.0150  0.0094  0.0143  1084 LEU A O   
7738  C CB  . LEU A 1086 ? 0.2595 0.2145 0.2356 0.0164  0.0087  0.0125  1084 LEU A CB  
7739  C CG  . LEU A 1086 ? 0.2626 0.2204 0.2388 0.0172  0.0078  0.0106  1084 LEU A CG  
7740  C CD1 . LEU A 1086 ? 0.2635 0.2231 0.2392 0.0163  0.0085  0.0097  1084 LEU A CD1 
7741  C CD2 . LEU A 1086 ? 0.2983 0.2561 0.2729 0.0191  0.0065  0.0113  1084 LEU A CD2 
7742  N N   . PRO A 1087 ? 0.3099 0.2579 0.2854 0.0163  0.0086  0.0175  1085 PRO A N   
7743  C CA  . PRO A 1087 ? 0.3025 0.2483 0.2784 0.0150  0.0094  0.0194  1085 PRO A CA  
7744  C C   . PRO A 1087 ? 0.3262 0.2733 0.3019 0.0136  0.0110  0.0191  1085 PRO A C   
7745  O O   . PRO A 1087 ? 0.3253 0.2746 0.2996 0.0136  0.0116  0.0187  1085 PRO A O   
7746  C CB  . PRO A 1087 ? 0.3614 0.3060 0.3353 0.0155  0.0090  0.0223  1085 PRO A CB  
7747  C CG  . PRO A 1087 ? 0.3933 0.3385 0.3662 0.0173  0.0075  0.0219  1085 PRO A CG  
7748  C CD  . PRO A 1087 ? 0.3387 0.2869 0.3122 0.0177  0.0076  0.0189  1085 PRO A CD  
7749  N N   . GLY A 1088 ? 0.3072 0.2532 0.2846 0.0124  0.0116  0.0190  1086 GLY A N   
7750  C CA  . GLY A 1088 ? 0.3284 0.2754 0.3060 0.0110  0.0130  0.0189  1086 GLY A CA  
7751  C C   . GLY A 1088 ? 0.2595 0.2046 0.2386 0.0099  0.0134  0.0198  1086 GLY A C   
7752  O O   . GLY A 1088 ? 0.2677 0.2105 0.2474 0.0099  0.0127  0.0211  1086 GLY A O   
7753  N N   . PRO A 1089 ? 0.3123 0.2583 0.2923 0.0088  0.0143  0.0190  1087 PRO A N   
7754  C CA  . PRO A 1089 ? 0.2605 0.2050 0.2421 0.0076  0.0147  0.0197  1087 PRO A CA  
7755  C C   . PRO A 1089 ? 0.3328 0.2761 0.3162 0.0078  0.0137  0.0185  1087 PRO A C   
7756  O O   . PRO A 1089 ? 0.2964 0.2406 0.2801 0.0086  0.0130  0.0167  1087 PRO A O   
7757  C CB  . PRO A 1089 ? 0.2791 0.2254 0.2612 0.0067  0.0158  0.0190  1087 PRO A CB  
7758  C CG  . PRO A 1089 ? 0.3021 0.2502 0.2838 0.0073  0.0155  0.0172  1087 PRO A CG  
7759  C CD  . PRO A 1089 ? 0.3273 0.2755 0.3074 0.0085  0.0149  0.0174  1087 PRO A CD  
7760  N N   . VAL A 1090 ? 0.2675 0.2088 0.2523 0.0070  0.0135  0.0193  1088 VAL A N   
7761  C CA  . VAL A 1090 ? 0.2567 0.1973 0.2435 0.0071  0.0127  0.0176  1088 VAL A CA  
7762  C C   . VAL A 1090 ? 0.2501 0.1933 0.2373 0.0066  0.0133  0.0157  1088 VAL A C   
7763  O O   . VAL A 1090 ? 0.2597 0.2045 0.2462 0.0059  0.0144  0.0161  1088 VAL A O   
7764  C CB  . VAL A 1090 ? 0.3036 0.2417 0.2920 0.0061  0.0123  0.0186  1088 VAL A CB  
7765  C CG1 . VAL A 1090 ? 0.3258 0.2609 0.3139 0.0063  0.0115  0.0209  1088 VAL A CG1 
7766  C CG2 . VAL A 1090 ? 0.2855 0.2248 0.2742 0.0046  0.0137  0.0194  1088 VAL A CG2 
7767  N N   . GLY A 1091 ? 0.2413 0.1852 0.2297 0.0071  0.0126  0.0137  1089 GLY A N   
7768  C CA  . GLY A 1091 ? 0.2864 0.2331 0.2753 0.0065  0.0131  0.0122  1089 GLY A CA  
7769  C C   . GLY A 1091 ? 0.2689 0.2182 0.2569 0.0067  0.0135  0.0116  1089 GLY A C   
7770  O O   . GLY A 1091 ? 0.2507 0.2022 0.2388 0.0059  0.0140  0.0111  1089 GLY A O   
7771  N N   . GLU A 1092 ? 0.2482 0.1972 0.2352 0.0078  0.0130  0.0118  1090 GLU A N   
7772  C CA  . GLU A 1092 ? 0.2489 0.2003 0.2351 0.0080  0.0132  0.0111  1090 GLU A CA  
7773  C C   . GLU A 1092 ? 0.2628 0.2142 0.2488 0.0095  0.0121  0.0104  1090 GLU A C   
7774  O O   . GLU A 1092 ? 0.2610 0.2101 0.2466 0.0104  0.0115  0.0114  1090 GLU A O   
7775  C CB  . GLU A 1092 ? 0.2800 0.2312 0.2650 0.0074  0.0140  0.0124  1090 GLU A CB  
7776  C CG  . GLU A 1092 ? 0.3406 0.2940 0.3254 0.0071  0.0142  0.0117  1090 GLU A CG  
7777  C CD  . GLU A 1092 ? 0.3383 0.2913 0.3221 0.0067  0.0148  0.0126  1090 GLU A CD  
7778  O OE1 . GLU A 1092 ? 0.2898 0.2422 0.2722 0.0075  0.0147  0.0132  1090 GLU A OE1 
7779  O OE2 . GLU A 1092 ? 0.3346 0.2879 0.3190 0.0056  0.0154  0.0128  1090 GLU A OE2 
7780  N N   . ARG A 1093 ? 0.2249 0.1792 0.2112 0.0099  0.0119  0.0090  1091 ARG A N   
7781  C CA  . ARG A 1093 ? 0.2228 0.1778 0.2090 0.0114  0.0109  0.0081  1091 ARG A CA  
7782  C C   . ARG A 1093 ? 0.2388 0.1957 0.2241 0.0112  0.0111  0.0081  1091 ARG A C   
7783  O O   . ARG A 1093 ? 0.2401 0.1994 0.2260 0.0100  0.0116  0.0075  1091 ARG A O   
7784  C CB  . ARG A 1093 ? 0.2551 0.2124 0.2429 0.0122  0.0102  0.0060  1091 ARG A CB  
7785  N N   . ASN A 1094 ? 0.2351 0.1908 0.2190 0.0121  0.0107  0.0089  1092 ASN A N   
7786  C CA  . ASN A 1094 ? 0.2428 0.2001 0.2258 0.0120  0.0108  0.0088  1092 ASN A CA  
7787  C C   . ASN A 1094 ? 0.2298 0.1887 0.2128 0.0135  0.0096  0.0078  1092 ASN A C   
7788  O O   . ASN A 1094 ? 0.2572 0.2145 0.2393 0.0149  0.0088  0.0084  1092 ASN A O   
7789  C CB  . ASN A 1094 ? 0.2131 0.1686 0.1943 0.0118  0.0113  0.0104  1092 ASN A CB  
7790  C CG  . ASN A 1094 ? 0.2740 0.2288 0.2556 0.0103  0.0124  0.0110  1092 ASN A CG  
7791  O OD1 . ASN A 1094 ? 0.2422 0.1984 0.2244 0.0093  0.0128  0.0103  1092 ASN A OD1 
7792  N ND2 . ASN A 1094 ? 0.2655 0.2182 0.2469 0.0101  0.0129  0.0124  1092 ASN A ND2 
7793  N N   . LEU A 1095 ? 0.2359 0.1980 0.2200 0.0131  0.0095  0.0062  1093 LEU A N   
7794  C CA  . LEU A 1095 ? 0.2483 0.2127 0.2329 0.0145  0.0084  0.0049  1093 LEU A CA  
7795  C C   . LEU A 1095 ? 0.2477 0.2138 0.2317 0.0143  0.0082  0.0045  1093 LEU A C   
7796  O O   . LEU A 1095 ? 0.2429 0.2095 0.2271 0.0128  0.0088  0.0046  1093 LEU A O   
7797  C CB  . LEU A 1095 ? 0.2200 0.1878 0.2068 0.0142  0.0083  0.0032  1093 LEU A CB  
7798  C CG  . LEU A 1095 ? 0.3008 0.2672 0.2883 0.0143  0.0086  0.0031  1093 LEU A CG  
7799  C CD1 . LEU A 1095 ? 0.3440 0.3146 0.3334 0.0143  0.0085  0.0012  1093 LEU A CD1 
7800  C CD2 . LEU A 1095 ? 0.3120 0.2750 0.2989 0.0162  0.0076  0.0037  1093 LEU A CD2 
7801  N N   . TYR A 1096 ? 0.2380 0.2051 0.2216 0.0159  0.0070  0.0039  1094 TYR A N   
7802  C CA  . TYR A 1096 ? 0.2167 0.1855 0.1997 0.0160  0.0065  0.0034  1094 TYR A CA  
7803  C C   . TYR A 1096 ? 0.2369 0.2089 0.2211 0.0172  0.0054  0.0017  1094 TYR A C   
7804  O O   . TYR A 1096 ? 0.2317 0.2032 0.2158 0.0190  0.0045  0.0017  1094 TYR A O   
7805  C CB  . TYR A 1096 ? 0.2578 0.2244 0.2382 0.0170  0.0063  0.0047  1094 TYR A CB  
7806  C CG  . TYR A 1096 ? 0.2271 0.1956 0.2066 0.0176  0.0055  0.0039  1094 TYR A CG  
7807  C CD1 . TYR A 1096 ? 0.2152 0.1842 0.1944 0.0165  0.0059  0.0034  1094 TYR A CD1 
7808  C CD2 . TYR A 1096 ? 0.2293 0.1990 0.2082 0.0195  0.0041  0.0035  1094 TYR A CD2 
7809  C CE1 . TYR A 1096 ? 0.2509 0.2218 0.2294 0.0171  0.0050  0.0023  1094 TYR A CE1 
7810  C CE2 . TYR A 1096 ? 0.2628 0.2346 0.2408 0.0201  0.0033  0.0026  1094 TYR A CE2 
7811  C CZ  . TYR A 1096 ? 0.2491 0.2215 0.2269 0.0189  0.0037  0.0019  1094 TYR A CZ  
7812  O OH  . TYR A 1096 ? 0.2517 0.2262 0.2288 0.0195  0.0027  0.0007  1094 TYR A OH  
7813  N N   . THR A 1097 ? 0.2316 0.2071 0.2174 0.0161  0.0053  0.0004  1095 THR A N   
7814  C CA  . THR A 1097 ? 0.2315 0.2110 0.2191 0.0169  0.0044  -0.0013 1095 THR A CA  
7815  C C   . THR A 1097 ? 0.2194 0.2015 0.2074 0.0164  0.0037  -0.0023 1095 THR A C   
7816  O O   . THR A 1097 ? 0.2257 0.2072 0.2136 0.0147  0.0041  -0.0021 1095 THR A O   
7817  C CB  . THR A 1097 ? 0.2636 0.2460 0.2536 0.0158  0.0050  -0.0022 1095 THR A CB  
7818  O OG1 . THR A 1097 ? 0.3020 0.2850 0.2927 0.0132  0.0060  -0.0017 1095 THR A OG1 
7819  C CG2 . THR A 1097 ? 0.2806 0.2606 0.2704 0.0166  0.0054  -0.0017 1095 THR A CG2 
7820  N N   . LEU A 1098 ? 0.2162 0.2013 0.2050 0.0179  0.0025  -0.0037 1096 LEU A N   
7821  C CA  . LEU A 1098 ? 0.2177 0.2059 0.2074 0.0174  0.0016  -0.0049 1096 LEU A CA  
7822  C C   . LEU A 1098 ? 0.2110 0.2043 0.2039 0.0165  0.0016  -0.0064 1096 LEU A C   
7823  O O   . LEU A 1098 ? 0.2201 0.2158 0.2140 0.0180  0.0011  -0.0073 1096 LEU A O   
7824  C CB  . LEU A 1098 ? 0.2150 0.2032 0.2030 0.0198  0.0002  -0.0052 1096 LEU A CB  
7825  C CG  . LEU A 1098 ? 0.2169 0.2009 0.2016 0.0206  0.0003  -0.0036 1096 LEU A CG  
7826  C CD1 . LEU A 1098 ? 0.2196 0.2045 0.2027 0.0230  -0.0013 -0.0038 1096 LEU A CD1 
7827  C CD2 . LEU A 1098 ? 0.2162 0.1990 0.2003 0.0187  0.0010  -0.0034 1096 LEU A CD2 
7828  N N   . HIS A 1099 ? 0.2353 0.2305 0.2298 0.0139  0.0019  -0.0067 1097 HIS A N   
7829  C CA  . HIS A 1099 ? 0.2269 0.2274 0.2245 0.0124  0.0020  -0.0077 1097 HIS A CA  
7830  C C   . HIS A 1099 ? 0.2140 0.2174 0.2131 0.0116  0.0008  -0.0089 1097 HIS A C   
7831  O O   . HIS A 1099 ? 0.2404 0.2415 0.2380 0.0121  0.0000  -0.0091 1097 HIS A O   
7832  C CB  . HIS A 1099 ? 0.2372 0.2375 0.2359 0.0095  0.0034  -0.0066 1097 HIS A CB  
7833  C CG  . HIS A 1099 ? 0.2868 0.2845 0.2843 0.0101  0.0045  -0.0055 1097 HIS A CG  
7834  N ND1 . HIS A 1099 ? 0.3067 0.3076 0.3055 0.0100  0.0051  -0.0059 1097 HIS A ND1 
7835  C CD2 . HIS A 1099 ? 0.2805 0.2729 0.2756 0.0107  0.0049  -0.0042 1097 HIS A CD2 
7836  C CE1 . HIS A 1099 ? 0.3108 0.3082 0.3081 0.0105  0.0059  -0.0049 1097 HIS A CE1 
7837  N NE2 . HIS A 1099 ? 0.3098 0.3021 0.3050 0.0109  0.0058  -0.0038 1097 HIS A NE2 
7838  N N   . ALA A 1100 ? 0.2081 0.2170 0.2103 0.0102  0.0008  -0.0099 1098 ALA A N   
7839  C CA  . ALA A 1100 ? 0.2410 0.2528 0.2453 0.0087  -0.0002 -0.0109 1098 ALA A CA  
7840  C C   . ALA A 1100 ? 0.2692 0.2777 0.2736 0.0060  0.0000  -0.0099 1098 ALA A C   
7841  O O   . ALA A 1100 ? 0.2538 0.2598 0.2578 0.0046  0.0012  -0.0083 1098 ALA A O   
7842  C CB  . ALA A 1100 ? 0.2286 0.2474 0.2365 0.0074  -0.0002 -0.0118 1098 ALA A CB  
7843  N N   . ARG A 1101 ? 0.2588 0.2673 0.2638 0.0055  -0.0013 -0.0109 1099 ARG A N   
7844  C CA  . ARG A 1101 ? 0.2537 0.2591 0.2594 0.0031  -0.0015 -0.0103 1099 ARG A CA  
7845  C C   . ARG A 1101 ? 0.2974 0.3060 0.3069 -0.0005 -0.0013 -0.0096 1099 ARG A C   
7846  O O   . ARG A 1101 ? 0.2706 0.2764 0.2805 -0.0027 -0.0007 -0.0081 1099 ARG A O   
7847  C CB  . ARG A 1101 ? 0.2926 0.2969 0.2978 0.0039  -0.0032 -0.0119 1099 ARG A CB  
7848  C CG  . ARG A 1101 ? 0.3034 0.3038 0.3046 0.0067  -0.0032 -0.0120 1099 ARG A CG  
7849  C CD  . ARG A 1101 ? 0.3541 0.3539 0.3548 0.0073  -0.0049 -0.0138 1099 ARG A CD  
7850  N NE  . ARG A 1101 ? 0.3538 0.3498 0.3546 0.0058  -0.0050 -0.0138 1099 ARG A NE  
7851  C CZ  . ARG A 1101 ? 0.4080 0.4000 0.4058 0.0071  -0.0045 -0.0133 1099 ARG A CZ  
7852  N NH1 . ARG A 1101 ? 0.3589 0.3497 0.3534 0.0095  -0.0036 -0.0122 1099 ARG A NH1 
7853  N NH2 . ARG A 1101 ? 0.3358 0.3248 0.3341 0.0061  -0.0050 -0.0139 1099 ARG A NH2 
7854  N N   . GLY A 1102 ? 0.2350 0.2495 0.2471 -0.0011 -0.0017 -0.0106 1100 GLY A N   
7855  C CA  . GLY A 1102 ? 0.2306 0.2489 0.2465 -0.0047 -0.0016 -0.0098 1100 GLY A CA  
7856  C C   . GLY A 1102 ? 0.2903 0.3139 0.3092 -0.0053 -0.0031 -0.0117 1100 GLY A C   
7857  O O   . GLY A 1102 ? 0.2519 0.2795 0.2707 -0.0030 -0.0033 -0.0131 1100 GLY A O   
7858  N N   . ARG A 1103 ? 0.2232 0.2467 0.2449 -0.0082 -0.0042 -0.0116 1101 ARG A N   
7859  C CA  . ARG A 1103 ? 0.2249 0.2533 0.2498 -0.0092 -0.0057 -0.0134 1101 ARG A CA  
7860  C C   . ARG A 1103 ? 0.2417 0.2663 0.2654 -0.0077 -0.0076 -0.0154 1101 ARG A C   
7861  O O   . ARG A 1103 ? 0.2519 0.2713 0.2754 -0.0089 -0.0081 -0.0150 1101 ARG A O   
7862  C CB  . ARG A 1103 ? 0.2703 0.3020 0.2998 -0.0137 -0.0059 -0.0121 1101 ARG A CB  
7863  C CG  . ARG A 1103 ? 0.2451 0.2832 0.2784 -0.0148 -0.0073 -0.0139 1101 ARG A CG  
7864  C CD  . ARG A 1103 ? 0.3031 0.3459 0.3410 -0.0195 -0.0071 -0.0121 1101 ARG A CD  
7865  N NE  . ARG A 1103 ? 0.3490 0.3961 0.3868 -0.0202 -0.0049 -0.0102 1101 ARG A NE  
7866  C CZ  . ARG A 1103 ? 0.4157 0.4709 0.4550 -0.0196 -0.0042 -0.0109 1101 ARG A CZ  
7867  N NH1 . ARG A 1103 ? 0.3414 0.4015 0.3826 -0.0185 -0.0053 -0.0134 1101 ARG A NH1 
7868  N NH2 . ARG A 1103 ? 0.4401 0.4987 0.4790 -0.0202 -0.0022 -0.0093 1101 ARG A NH2 
7869  N N   . ILE A 1104 ? 0.2200 0.2474 0.2431 -0.0051 -0.0086 -0.0175 1102 ILE A N   
7870  C CA  . ILE A 1104 ? 0.2593 0.2842 0.2811 -0.0035 -0.0104 -0.0196 1102 ILE A CA  
7871  C C   . ILE A 1104 ? 0.2207 0.2494 0.2469 -0.0059 -0.0123 -0.0213 1102 ILE A C   
7872  O O   . ILE A 1104 ? 0.2178 0.2529 0.2468 -0.0067 -0.0125 -0.0218 1102 ILE A O   
7873  C CB  . ILE A 1104 ? 0.2242 0.2499 0.2426 0.0008  -0.0107 -0.0209 1102 ILE A CB  
7874  C CG1 . ILE A 1104 ? 0.2235 0.2457 0.2381 0.0029  -0.0088 -0.0191 1102 ILE A CG1 
7875  C CG2 . ILE A 1104 ? 0.2225 0.2458 0.2391 0.0025  -0.0125 -0.0229 1102 ILE A CG2 
7876  C CD1 . ILE A 1104 ? 0.2292 0.2446 0.2413 0.0025  -0.0081 -0.0178 1102 ILE A CD1 
7877  N N   . LEU A 1105 ? 0.2208 0.2456 0.2476 -0.0070 -0.0138 -0.0222 1103 LEU A N   
7878  C CA  . LEU A 1105 ? 0.2298 0.2575 0.2605 -0.0089 -0.0160 -0.0243 1103 LEU A CA  
7879  C C   . LEU A 1105 ? 0.2237 0.2542 0.2528 -0.0056 -0.0175 -0.0271 1103 LEU A C   
7880  O O   . LEU A 1105 ? 0.2323 0.2593 0.2574 -0.0026 -0.0178 -0.0281 1103 LEU A O   
7881  C CB  . LEU A 1105 ? 0.2253 0.2474 0.2572 -0.0109 -0.0174 -0.0247 1103 LEU A CB  
7882  C CG  . LEU A 1105 ? 0.2280 0.2520 0.2639 -0.0127 -0.0201 -0.0272 1103 LEU A CG  
7883  C CD1 . LEU A 1105 ? 0.2511 0.2807 0.2924 -0.0166 -0.0202 -0.0261 1103 LEU A CD1 
7884  C CD2 . LEU A 1105 ? 0.2638 0.2813 0.3003 -0.0138 -0.0215 -0.0280 1103 LEU A CD2 
7885  N N   . LEU A 1106 ? 0.2235 0.2606 0.2557 -0.0062 -0.0183 -0.0282 1104 LEU A N   
7886  C CA  . LEU A 1106 ? 0.2245 0.2650 0.2557 -0.0032 -0.0199 -0.0309 1104 LEU A CA  
7887  C C   . LEU A 1106 ? 0.2429 0.2850 0.2779 -0.0053 -0.0224 -0.0333 1104 LEU A C   
7888  O O   . LEU A 1106 ? 0.2573 0.3029 0.2973 -0.0089 -0.0227 -0.0330 1104 LEU A O   
7889  C CB  . LEU A 1106 ? 0.2227 0.2698 0.2547 -0.0018 -0.0192 -0.0309 1104 LEU A CB  
7890  C CG  . LEU A 1106 ? 0.2550 0.3013 0.2838 0.0005  -0.0170 -0.0289 1104 LEU A CG  
7891  C CD1 . LEU A 1106 ? 0.2357 0.2884 0.2650 0.0031  -0.0173 -0.0301 1104 LEU A CD1 
7892  C CD2 . LEU A 1106 ? 0.2408 0.2804 0.2642 0.0033  -0.0166 -0.0283 1104 LEU A CD2 
7893  N N   . VAL A 1107 ? 0.2294 0.2693 0.2622 -0.0031 -0.0241 -0.0357 1105 VAL A N   
7894  C CA  . VAL A 1107 ? 0.2321 0.2737 0.2684 -0.0046 -0.0268 -0.0386 1105 VAL A CA  
7895  C C   . VAL A 1107 ? 0.2331 0.2791 0.2676 -0.0011 -0.0284 -0.0412 1105 VAL A C   
7896  O O   . VAL A 1107 ? 0.2608 0.3044 0.2917 0.0016  -0.0295 -0.0430 1105 VAL A O   
7897  C CB  . VAL A 1107 ? 0.2453 0.2804 0.2810 -0.0054 -0.0280 -0.0396 1105 VAL A CB  
7898  C CG1 . VAL A 1107 ? 0.2415 0.2783 0.2820 -0.0078 -0.0309 -0.0425 1105 VAL A CG1 
7899  C CG2 . VAL A 1107 ? 0.2857 0.3159 0.3219 -0.0080 -0.0262 -0.0366 1105 VAL A CG2 
7900  N N   . PRO A 1108 ? 0.2318 0.2845 0.2685 -0.0010 -0.0284 -0.0414 1106 PRO A N   
7901  C CA  . PRO A 1108 ? 0.2391 0.2960 0.2741 0.0025  -0.0300 -0.0436 1106 PRO A CA  
7902  C C   . PRO A 1108 ? 0.2684 0.3283 0.3069 0.0013  -0.0329 -0.0470 1106 PRO A C   
7903  O O   . PRO A 1108 ? 0.2806 0.3403 0.3237 -0.0027 -0.0338 -0.0475 1106 PRO A O   
7904  C CB  . PRO A 1108 ? 0.2493 0.3123 0.2862 0.0028  -0.0288 -0.0425 1106 PRO A CB  
7905  C CG  . PRO A 1108 ? 0.2291 0.2938 0.2713 -0.0020 -0.0279 -0.0412 1106 PRO A CG  
7906  C CD  . PRO A 1108 ? 0.2295 0.2866 0.2704 -0.0040 -0.0271 -0.0395 1106 PRO A CD  
7907  N N   . ALA A 1109 ? 0.2373 0.3000 0.2734 0.0047  -0.0346 -0.0493 1107 ALA A N   
7908  C CA  . ALA A 1109 ? 0.2747 0.3415 0.3140 0.0041  -0.0376 -0.0528 1107 ALA A CA  
7909  C C   . ALA A 1109 ? 0.2969 0.3718 0.3383 0.0055  -0.0385 -0.0539 1107 ALA A C   
7910  O O   . ALA A 1109 ? 0.3305 0.4105 0.3770 0.0032  -0.0403 -0.0559 1107 ALA A O   
7911  C CB  . ALA A 1109 ? 0.2830 0.3469 0.3181 0.0070  -0.0393 -0.0553 1107 ALA A CB  
7912  N N   . THR A 1110 ? 0.2472 0.3234 0.2849 0.0091  -0.0373 -0.0525 1108 THR A N   
7913  C CA  . THR A 1110 ? 0.2529 0.3365 0.2922 0.0111  -0.0382 -0.0535 1108 THR A CA  
7914  C C   . THR A 1110 ? 0.2471 0.3323 0.2869 0.0113  -0.0357 -0.0508 1108 THR A C   
7915  O O   . THR A 1110 ? 0.2513 0.3314 0.2887 0.0109  -0.0334 -0.0482 1108 THR A O   
7916  C CB  . THR A 1110 ? 0.2614 0.3453 0.2956 0.0160  -0.0397 -0.0547 1108 THR A CB  
7917  O OG1 . THR A 1110 ? 0.2549 0.3335 0.2834 0.0188  -0.0379 -0.0520 1108 THR A OG1 
7918  C CG2 . THR A 1110 ? 0.2933 0.3757 0.3263 0.0162  -0.0421 -0.0575 1108 THR A CG2 
7919  N N   . GLU A 1111 ? 0.2486 0.3414 0.2916 0.0120  -0.0363 -0.0518 1109 GLU A N   
7920  C CA  . GLU A 1111 ? 0.2665 0.3617 0.3100 0.0128  -0.0342 -0.0498 1109 GLU A CA  
7921  C C   . GLU A 1111 ? 0.2482 0.3382 0.2856 0.0170  -0.0331 -0.0480 1109 GLU A C   
7922  O O   . GLU A 1111 ? 0.2562 0.3434 0.2924 0.0167  -0.0308 -0.0456 1109 GLU A O   
7923  C CB  . GLU A 1111 ? 0.3141 0.4186 0.3618 0.0135  -0.0354 -0.0517 1109 GLU A CB  
7924  C CG  . GLU A 1111 ? 0.3005 0.4079 0.3481 0.0157  -0.0337 -0.0504 1109 GLU A CG  
7925  C CD  . GLU A 1111 ? 0.3421 0.4593 0.3945 0.0163  -0.0348 -0.0524 1109 GLU A CD  
7926  O OE1 . GLU A 1111 ? 0.3506 0.4734 0.4084 0.0124  -0.0343 -0.0528 1109 GLU A OE1 
7927  O OE2 . GLU A 1111 ? 0.3780 0.4976 0.4287 0.0207  -0.0364 -0.0537 1109 GLU A OE2 
7928  N N   . SER A 1112 ? 0.2540 0.3432 0.2875 0.0208  -0.0349 -0.0490 1110 SER A N   
7929  C CA  . SER A 1112 ? 0.2460 0.3304 0.2739 0.0247  -0.0341 -0.0470 1110 SER A CA  
7930  C C   . SER A 1112 ? 0.2668 0.3431 0.2912 0.0234  -0.0323 -0.0448 1110 SER A C   
7931  O O   . SER A 1112 ? 0.2418 0.3142 0.2634 0.0247  -0.0304 -0.0424 1110 SER A O   
7932  C CB  . SER A 1112 ? 0.2759 0.3610 0.3002 0.0287  -0.0366 -0.0482 1110 SER A CB  
7933  O OG  . SER A 1112 ? 0.2933 0.3737 0.3124 0.0322  -0.0358 -0.0458 1110 SER A OG  
7934  N N   . GLY A 1113 ? 0.2446 0.3184 0.2691 0.0211  -0.0329 -0.0458 1111 GLY A N   
7935  C CA  . GLY A 1113 ? 0.2337 0.3002 0.2555 0.0197  -0.0311 -0.0439 1111 GLY A CA  
7936  C C   . GLY A 1113 ? 0.2315 0.2967 0.2556 0.0169  -0.0286 -0.0417 1111 GLY A C   
7937  O O   . GLY A 1113 ? 0.2295 0.2896 0.2505 0.0176  -0.0267 -0.0394 1111 GLY A O   
7938  N N   . LEU A 1114 ? 0.2292 0.2994 0.2589 0.0137  -0.0286 -0.0425 1112 LEU A N   
7939  C CA  . LEU A 1114 ? 0.2603 0.3305 0.2923 0.0110  -0.0263 -0.0403 1112 LEU A CA  
7940  C C   . LEU A 1114 ? 0.2248 0.2952 0.2546 0.0140  -0.0247 -0.0387 1112 LEU A C   
7941  O O   . LEU A 1114 ? 0.2232 0.2897 0.2515 0.0133  -0.0226 -0.0365 1112 LEU A O   
7942  C CB  . LEU A 1114 ? 0.2494 0.3265 0.2879 0.0074  -0.0267 -0.0413 1112 LEU A CB  
7943  C CG  . LEU A 1114 ? 0.2560 0.3349 0.2969 0.0050  -0.0242 -0.0391 1112 LEU A CG  
7944  C CD1 . LEU A 1114 ? 0.2222 0.2939 0.2614 0.0026  -0.0225 -0.0367 1112 LEU A CD1 
7945  C CD2 . LEU A 1114 ? 0.2711 0.3579 0.3184 0.0014  -0.0246 -0.0400 1112 LEU A CD2 
7946  N N   . TYR A 1115 ? 0.2292 0.3041 0.2588 0.0173  -0.0260 -0.0400 1113 TYR A N   
7947  C CA  . TYR A 1115 ? 0.2244 0.2994 0.2524 0.0202  -0.0248 -0.0388 1113 TYR A CA  
7948  C C   . TYR A 1115 ? 0.2252 0.2922 0.2474 0.0225  -0.0240 -0.0367 1113 TYR A C   
7949  O O   . TYR A 1115 ? 0.2237 0.2881 0.2447 0.0230  -0.0222 -0.0349 1113 TYR A O   
7950  C CB  . TYR A 1115 ? 0.2255 0.3065 0.2545 0.0237  -0.0267 -0.0406 1113 TYR A CB  
7951  C CG  . TYR A 1115 ? 0.2245 0.3144 0.2595 0.0218  -0.0273 -0.0427 1113 TYR A CG  
7952  C CD1 . TYR A 1115 ? 0.2275 0.3202 0.2666 0.0174  -0.0257 -0.0422 1113 TYR A CD1 
7953  C CD2 . TYR A 1115 ? 0.2456 0.3415 0.2821 0.0244  -0.0295 -0.0449 1113 TYR A CD2 
7954  C CE1 . TYR A 1115 ? 0.2342 0.3358 0.2790 0.0155  -0.0262 -0.0438 1113 TYR A CE1 
7955  C CE2 . TYR A 1115 ? 0.2444 0.3492 0.2867 0.0226  -0.0301 -0.0468 1113 TYR A CE2 
7956  C CZ  . TYR A 1115 ? 0.2584 0.3660 0.3047 0.0181  -0.0284 -0.0462 1113 TYR A CZ  
7957  O OH  . TYR A 1115 ? 0.2888 0.4057 0.3409 0.0162  -0.0288 -0.0479 1113 TYR A OH  
7958  N N   . HIS A 1116 ? 0.2301 0.2937 0.2487 0.0240  -0.0254 -0.0370 1114 HIS A N   
7959  C CA  . HIS A 1116 ? 0.2286 0.2851 0.2419 0.0259  -0.0245 -0.0349 1114 HIS A CA  
7960  C C   . HIS A 1116 ? 0.2449 0.2963 0.2579 0.0228  -0.0223 -0.0332 1114 HIS A C   
7961  O O   . HIS A 1116 ? 0.2319 0.2787 0.2420 0.0238  -0.0208 -0.0310 1114 HIS A O   
7962  C CB  . HIS A 1116 ? 0.2540 0.3089 0.2637 0.0278  -0.0264 -0.0358 1114 HIS A CB  
7963  C CG  . HIS A 1116 ? 0.2637 0.3216 0.2719 0.0317  -0.0283 -0.0364 1114 HIS A CG  
7964  N ND1 . HIS A 1116 ? 0.2976 0.3620 0.3088 0.0322  -0.0304 -0.0389 1114 HIS A ND1 
7965  C CD2 . HIS A 1116 ? 0.2765 0.3317 0.2805 0.0353  -0.0286 -0.0347 1114 HIS A CD2 
7966  C CE1 . HIS A 1116 ? 0.2799 0.3456 0.2888 0.0361  -0.0320 -0.0388 1114 HIS A CE1 
7967  N NE2 . HIS A 1116 ? 0.3092 0.3692 0.3137 0.0380  -0.0310 -0.0361 1114 HIS A NE2 
7968  N N   . GLN A 1117 ? 0.2264 0.2782 0.2421 0.0193  -0.0224 -0.0341 1115 GLN A N   
7969  C CA  . GLN A 1117 ? 0.2249 0.2721 0.2407 0.0163  -0.0205 -0.0324 1115 GLN A CA  
7970  C C   . GLN A 1117 ? 0.2222 0.2704 0.2398 0.0152  -0.0185 -0.0307 1115 GLN A C   
7971  O O   . GLN A 1117 ? 0.2211 0.2647 0.2365 0.0150  -0.0167 -0.0286 1115 GLN A O   
7972  C CB  . GLN A 1117 ? 0.2254 0.2731 0.2446 0.0127  -0.0213 -0.0337 1115 GLN A CB  
7973  C CG  . GLN A 1117 ? 0.2283 0.2742 0.2457 0.0135  -0.0233 -0.0356 1115 GLN A CG  
7974  C CD  . GLN A 1117 ? 0.2677 0.3140 0.2892 0.0097  -0.0243 -0.0371 1115 GLN A CD  
7975  O OE1 . GLN A 1117 ? 0.2622 0.3115 0.2883 0.0065  -0.0238 -0.0367 1115 GLN A OE1 
7976  N NE2 . GLN A 1117 ? 0.2352 0.2788 0.2553 0.0100  -0.0257 -0.0388 1115 GLN A NE2 
7977  N N   . LEU A 1118 ? 0.2211 0.2760 0.2428 0.0143  -0.0187 -0.0317 1116 LEU A N   
7978  C CA  A LEU A 1118 ? 0.2187 0.2758 0.2422 0.0134  -0.0168 -0.0305 1116 LEU A CA  
7979  C CA  B LEU A 1118 ? 0.2187 0.2760 0.2423 0.0135  -0.0169 -0.0305 1116 LEU A CA  
7980  C C   . LEU A 1118 ? 0.2185 0.2729 0.2385 0.0171  -0.0161 -0.0294 1116 LEU A C   
7981  O O   . LEU A 1118 ? 0.2207 0.2725 0.2399 0.0164  -0.0142 -0.0277 1116 LEU A O   
7982  C CB  A LEU A 1118 ? 0.2179 0.2837 0.2464 0.0123  -0.0174 -0.0321 1116 LEU A CB  
7983  C CB  B LEU A 1118 ? 0.2180 0.2841 0.2464 0.0127  -0.0175 -0.0322 1116 LEU A CB  
7984  C CG  A LEU A 1118 ? 0.2155 0.2853 0.2467 0.0107  -0.0154 -0.0311 1116 LEU A CG  
7985  C CG  B LEU A 1118 ? 0.2173 0.2872 0.2506 0.0079  -0.0174 -0.0324 1116 LEU A CG  
7986  C CD1 A LEU A 1118 ? 0.2143 0.2797 0.2452 0.0073  -0.0136 -0.0288 1116 LEU A CD1 
7987  C CD1 B LEU A 1118 ? 0.2170 0.2962 0.2549 0.0077  -0.0183 -0.0344 1116 LEU A CD1 
7988  C CD2 A LEU A 1118 ? 0.2361 0.3150 0.2727 0.0087  -0.0161 -0.0327 1116 LEU A CD2 
7989  C CD2 B LEU A 1118 ? 0.2341 0.3025 0.2680 0.0051  -0.0150 -0.0300 1116 LEU A CD2 
7990  N N   . ALA A 1119 ? 0.2406 0.2954 0.2586 0.0208  -0.0176 -0.0303 1117 ALA A N   
7991  C CA  . ALA A 1119 ? 0.2391 0.2907 0.2539 0.0242  -0.0172 -0.0291 1117 ALA A CA  
7992  C C   . ALA A 1119 ? 0.2220 0.2658 0.2328 0.0239  -0.0159 -0.0268 1117 ALA A C   
7993  O O   . ALA A 1119 ? 0.2400 0.2810 0.2496 0.0244  -0.0145 -0.0253 1117 ALA A O   
7994  C CB  . ALA A 1119 ? 0.2235 0.2762 0.2365 0.0282  -0.0195 -0.0301 1117 ALA A CB  
7995  N N   . ALA A 1120 ? 0.2222 0.2626 0.2309 0.0231  -0.0164 -0.0267 1118 ALA A N   
7996  C CA  . ALA A 1120 ? 0.2278 0.2613 0.2328 0.0228  -0.0151 -0.0246 1118 ALA A CA  
7997  C C   . ALA A 1120 ? 0.2198 0.2516 0.2264 0.0198  -0.0130 -0.0233 1118 ALA A C   
7998  O O   . ALA A 1120 ? 0.2192 0.2467 0.2236 0.0203  -0.0116 -0.0214 1118 ALA A O   
7999  C CB  . ALA A 1120 ? 0.2243 0.2555 0.2273 0.0224  -0.0161 -0.0252 1118 ALA A CB  
8000  N N   . ALA A 1121 ? 0.2185 0.2539 0.2291 0.0166  -0.0129 -0.0242 1119 ALA A N   
8001  C CA  . ALA A 1121 ? 0.2165 0.2505 0.2285 0.0135  -0.0110 -0.0227 1119 ALA A CA  
8002  C C   . ALA A 1121 ? 0.2253 0.2616 0.2382 0.0141  -0.0097 -0.0220 1119 ALA A C   
8003  O O   . ALA A 1121 ? 0.2139 0.2469 0.2257 0.0134  -0.0080 -0.0203 1119 ALA A O   
8004  C CB  . ALA A 1121 ? 0.2161 0.2534 0.2323 0.0098  -0.0114 -0.0235 1119 ALA A CB  
8005  N N   . LEU A 1122 ? 0.2146 0.2569 0.2297 0.0156  -0.0104 -0.0235 1120 LEU A N   
8006  C CA  . LEU A 1122 ? 0.2131 0.2584 0.2295 0.0164  -0.0093 -0.0234 1120 LEU A CA  
8007  C C   . LEU A 1122 ? 0.2139 0.2541 0.2266 0.0197  -0.0091 -0.0224 1120 LEU A C   
8008  O O   . LEU A 1122 ? 0.2557 0.2949 0.2682 0.0196  -0.0076 -0.0215 1120 LEU A O   
8009  C CB  . LEU A 1122 ? 0.2458 0.2991 0.2656 0.0175  -0.0104 -0.0256 1120 LEU A CB  
8010  C CG  . LEU A 1122 ? 0.2123 0.2719 0.2365 0.0140  -0.0105 -0.0265 1120 LEU A CG  
8011  C CD1 . LEU A 1122 ? 0.2362 0.3036 0.2633 0.0159  -0.0116 -0.0288 1120 LEU A CD1 
8012  C CD2 . LEU A 1122 ? 0.2312 0.2920 0.2571 0.0104  -0.0085 -0.0250 1120 LEU A CD2 
8013  N N   . ALA A 1123 ? 0.2161 0.2534 0.2260 0.0225  -0.0105 -0.0225 1121 ALA A N   
8014  C CA  . ALA A 1123 ? 0.2174 0.2497 0.2240 0.0255  -0.0105 -0.0213 1121 ALA A CA  
8015  C C   . ALA A 1123 ? 0.2353 0.2615 0.2395 0.0240  -0.0088 -0.0191 1121 ALA A C   
8016  O O   . ALA A 1123 ? 0.2341 0.2566 0.2364 0.0258  -0.0084 -0.0180 1121 ALA A O   
8017  C CB  . ALA A 1123 ? 0.2395 0.2698 0.2434 0.0283  -0.0124 -0.0213 1121 ALA A CB  
8018  N N   . THR A 1124 ? 0.2157 0.2404 0.2200 0.0210  -0.0081 -0.0185 1122 THR A N   
8019  C CA  . THR A 1124 ? 0.2149 0.2342 0.2172 0.0195  -0.0065 -0.0166 1122 THR A CA  
8020  C C   . THR A 1124 ? 0.2124 0.2337 0.2174 0.0166  -0.0049 -0.0161 1122 THR A C   
8021  O O   . THR A 1124 ? 0.2197 0.2372 0.2237 0.0146  -0.0037 -0.0146 1122 THR A O   
8022  C CB  . THR A 1124 ? 0.2160 0.2319 0.2164 0.0185  -0.0069 -0.0162 1122 THR A CB  
8023  O OG1 . THR A 1124 ? 0.2233 0.2430 0.2263 0.0168  -0.0079 -0.0178 1122 THR A OG1 
8024  C CG2 . THR A 1124 ? 0.2186 0.2317 0.2154 0.0216  -0.0080 -0.0159 1122 THR A CG2 
8025  N N   . GLY A 1125 ? 0.2114 0.2388 0.2195 0.0163  -0.0049 -0.0174 1123 GLY A N   
8026  C CA  . GLY A 1125 ? 0.2097 0.2398 0.2199 0.0139  -0.0033 -0.0169 1123 GLY A CA  
8027  C C   . GLY A 1125 ? 0.2164 0.2490 0.2293 0.0099  -0.0029 -0.0165 1123 GLY A C   
8028  O O   . GLY A 1125 ? 0.2195 0.2543 0.2340 0.0076  -0.0016 -0.0156 1123 GLY A O   
8029  N N   . ASN A 1126 ? 0.2176 0.2500 0.2310 0.0091  -0.0042 -0.0171 1124 ASN A N   
8030  C CA  . ASN A 1126 ? 0.2095 0.2425 0.2253 0.0053  -0.0041 -0.0166 1124 ASN A CA  
8031  C C   . ASN A 1126 ? 0.2090 0.2499 0.2291 0.0034  -0.0045 -0.0177 1124 ASN A C   
8032  O O   . ASN A 1126 ? 0.2133 0.2591 0.2345 0.0055  -0.0053 -0.0194 1124 ASN A O   
8033  C CB  . ASN A 1126 ? 0.2113 0.2402 0.2258 0.0052  -0.0055 -0.0171 1124 ASN A CB  
8034  C CG  . ASN A 1126 ? 0.2128 0.2346 0.2233 0.0068  -0.0050 -0.0159 1124 ASN A CG  
8035  O OD1 . ASN A 1126 ? 0.2290 0.2472 0.2388 0.0051  -0.0038 -0.0142 1124 ASN A OD1 
8036  N ND2 . ASN A 1126 ? 0.2133 0.2331 0.2208 0.0099  -0.0059 -0.0166 1124 ASN A ND2 
8037  N N   . SER A 1127 ? 0.2149 0.2571 0.2376 -0.0005 -0.0040 -0.0165 1125 SER A N   
8038  C CA  . SER A 1127 ? 0.2218 0.2705 0.2489 -0.0031 -0.0048 -0.0173 1125 SER A CA  
8039  C C   . SER A 1127 ? 0.2108 0.2567 0.2385 -0.0040 -0.0066 -0.0182 1125 SER A C   
8040  O O   . SER A 1127 ? 0.2350 0.2742 0.2597 -0.0029 -0.0071 -0.0181 1125 SER A O   
8041  C CB  . SER A 1127 ? 0.2491 0.3007 0.2789 -0.0072 -0.0034 -0.0152 1125 SER A CB  
8042  O OG  . SER A 1127 ? 0.2691 0.3140 0.2977 -0.0092 -0.0032 -0.0133 1125 SER A OG  
8043  N N   . VAL A 1128 ? 0.2115 0.2628 0.2431 -0.0061 -0.0078 -0.0193 1126 VAL A N   
8044  C CA  . VAL A 1128 ? 0.2136 0.2629 0.2462 -0.0068 -0.0098 -0.0207 1126 VAL A CA  
8045  C C   . VAL A 1128 ? 0.2510 0.3035 0.2885 -0.0115 -0.0104 -0.0201 1126 VAL A C   
8046  O O   . VAL A 1128 ? 0.2133 0.2721 0.2539 -0.0137 -0.0094 -0.0192 1126 VAL A O   
8047  C CB  . VAL A 1128 ? 0.2356 0.2882 0.2679 -0.0037 -0.0115 -0.0235 1126 VAL A CB  
8048  C CG1 . VAL A 1128 ? 0.2143 0.2633 0.2418 0.0009  -0.0112 -0.0238 1126 VAL A CG1 
8049  C CG2 . VAL A 1128 ? 0.2374 0.2991 0.2736 -0.0043 -0.0115 -0.0244 1126 VAL A CG2 
8050  N N   . ALA A 1129 ? 0.2341 0.2823 0.2724 -0.0131 -0.0120 -0.0206 1127 ALA A N   
8051  C CA  . ALA A 1129 ? 0.2788 0.3298 0.3222 -0.0172 -0.0133 -0.0207 1127 ALA A CA  
8052  C C   . ALA A 1129 ? 0.2745 0.3258 0.3184 -0.0157 -0.0158 -0.0239 1127 ALA A C   
8053  O O   . ALA A 1129 ? 0.2424 0.2879 0.2832 -0.0135 -0.0167 -0.0250 1127 ALA A O   
8054  C CB  . ALA A 1129 ? 0.2687 0.3140 0.3132 -0.0207 -0.0134 -0.0185 1127 ALA A CB  
8055  N N   . ILE A 1130 ? 0.2314 0.2900 0.2791 -0.0166 -0.0168 -0.0253 1128 ILE A N   
8056  C CA  . ILE A 1130 ? 0.2688 0.3288 0.3170 -0.0149 -0.0192 -0.0286 1128 ILE A CA  
8057  C C   . ILE A 1130 ? 0.2982 0.3579 0.3511 -0.0189 -0.0213 -0.0293 1128 ILE A C   
8058  O O   . ILE A 1130 ? 0.2833 0.3470 0.3409 -0.0231 -0.0210 -0.0278 1128 ILE A O   
8059  C CB  . ILE A 1130 ? 0.2425 0.3108 0.2919 -0.0128 -0.0194 -0.0302 1128 ILE A CB  
8060  C CG1 . ILE A 1130 ? 0.2543 0.3230 0.2998 -0.0091 -0.0175 -0.0295 1128 ILE A CG1 
8061  C CG2 . ILE A 1130 ? 0.2301 0.2993 0.2794 -0.0106 -0.0220 -0.0336 1128 ILE A CG2 
8062  C CD1 . ILE A 1130 ? 0.2686 0.3461 0.3161 -0.0074 -0.0175 -0.0309 1128 ILE A CD1 
8063  N N   . ASP A 1131 ? 0.2944 0.3496 0.3462 -0.0177 -0.0234 -0.0316 1129 ASP A N   
8064  C CA  . ASP A 1131 ? 0.2734 0.3278 0.3297 -0.0211 -0.0258 -0.0329 1129 ASP A CA  
8065  C C   . ASP A 1131 ? 0.3026 0.3656 0.3643 -0.0235 -0.0268 -0.0338 1129 ASP A C   
8066  O O   . ASP A 1131 ? 0.2826 0.3506 0.3440 -0.0208 -0.0277 -0.0363 1129 ASP A O   
8067  C CB  . ASP A 1131 ? 0.2880 0.3379 0.3419 -0.0184 -0.0280 -0.0361 1129 ASP A CB  
8068  C CG  . ASP A 1131 ? 0.3387 0.3873 0.3974 -0.0217 -0.0309 -0.0379 1129 ASP A CG  
8069  O OD1 . ASP A 1131 ? 0.3080 0.3561 0.3711 -0.0263 -0.0309 -0.0359 1129 ASP A OD1 
8070  O OD2 . ASP A 1131 ? 0.3304 0.3785 0.3883 -0.0197 -0.0331 -0.0414 1129 ASP A OD2 
8071  N N   . ALA A 1132 ? 0.3106 0.3758 0.3774 -0.0285 -0.0267 -0.0317 1130 ALA A N   
8072  C CA  . ALA A 1132 ? 0.3497 0.4234 0.4221 -0.0313 -0.0276 -0.0325 1130 ALA A CA  
8073  C C   . ALA A 1132 ? 0.3247 0.3984 0.3999 -0.0316 -0.0310 -0.0361 1130 ALA A C   
8074  O O   . ALA A 1132 ? 0.3787 0.4600 0.4574 -0.0321 -0.0321 -0.0378 1130 ALA A O   
8075  C CB  . ALA A 1132 ? 0.3503 0.4260 0.4275 -0.0369 -0.0267 -0.0289 1130 ALA A CB  
8076  N N   . ALA A 1133 ? 0.3484 0.4142 0.4221 -0.0310 -0.0327 -0.0375 1131 ALA A N   
8077  C CA  . ALA A 1133 ? 0.3740 0.4397 0.4501 -0.0310 -0.0361 -0.0413 1131 ALA A CA  
8078  C C   . ALA A 1133 ? 0.3610 0.4302 0.4336 -0.0260 -0.0368 -0.0447 1131 ALA A C   
8079  O O   . ALA A 1133 ? 0.3689 0.4402 0.4437 -0.0259 -0.0396 -0.0481 1131 ALA A O   
8080  C CB  . ALA A 1133 ? 0.3771 0.4335 0.4523 -0.0314 -0.0377 -0.0422 1131 ALA A CB  
8081  N N   . SER A 1134 ? 0.3559 0.4259 0.4233 -0.0220 -0.0346 -0.0438 1132 SER A N   
8082  C CA  . SER A 1134 ? 0.3017 0.3752 0.3659 -0.0173 -0.0354 -0.0464 1132 SER A CA  
8083  C C   . SER A 1134 ? 0.3480 0.4311 0.4167 -0.0181 -0.0364 -0.0479 1132 SER A C   
8084  O O   . SER A 1134 ? 0.2538 0.3401 0.3212 -0.0149 -0.0381 -0.0508 1132 SER A O   
8085  C CB  . SER A 1134 ? 0.3426 0.4149 0.4009 -0.0133 -0.0328 -0.0446 1132 SER A CB  
8086  O OG  . SER A 1134 ? 0.3119 0.3896 0.3722 -0.0146 -0.0306 -0.0422 1132 SER A OG  
8087  N N   . GLY A 1135 ? 0.2990 0.3870 0.3728 -0.0222 -0.0354 -0.0459 1133 GLY A N   
8088  C CA  . GLY A 1135 ? 0.3499 0.4479 0.4283 -0.0231 -0.0361 -0.0472 1133 GLY A CA  
8089  C C   . GLY A 1135 ? 0.3363 0.4398 0.4119 -0.0189 -0.0347 -0.0474 1133 GLY A C   
8090  O O   . GLY A 1135 ? 0.3262 0.4379 0.4048 -0.0183 -0.0357 -0.0493 1133 GLY A O   
8091  N N   . LEU A 1136 ? 0.2846 0.3839 0.3547 -0.0158 -0.0325 -0.0456 1134 LEU A N   
8092  C CA  . LEU A 1136 ? 0.3405 0.4437 0.4076 -0.0112 -0.0315 -0.0460 1134 LEU A CA  
8093  C C   . LEU A 1136 ? 0.3240 0.4324 0.3928 -0.0124 -0.0288 -0.0437 1134 LEU A C   
8094  O O   . LEU A 1136 ? 0.3105 0.4200 0.3761 -0.0086 -0.0275 -0.0434 1134 LEU A O   
8095  C CB  . LEU A 1136 ? 0.3020 0.3976 0.3619 -0.0067 -0.0310 -0.0457 1134 LEU A CB  
8096  C CG  . LEU A 1136 ? 0.3109 0.4027 0.3681 -0.0043 -0.0336 -0.0484 1134 LEU A CG  
8097  C CD1 . LEU A 1136 ? 0.2761 0.3600 0.3265 -0.0009 -0.0326 -0.0473 1134 LEU A CD1 
8098  C CD2 . LEU A 1136 ? 0.3314 0.4300 0.3895 -0.0015 -0.0357 -0.0513 1134 LEU A CD2 
8099  N N   . GLN A 1137 ? 0.3159 0.4275 0.3897 -0.0175 -0.0281 -0.0419 1135 GLN A N   
8100  C CA  . GLN A 1137 ? 0.3177 0.4348 0.3930 -0.0188 -0.0254 -0.0397 1135 GLN A CA  
8101  C C   . GLN A 1137 ? 0.3122 0.4389 0.3889 -0.0158 -0.0254 -0.0417 1135 GLN A C   
8102  O O   . GLN A 1137 ? 0.3337 0.4628 0.4086 -0.0135 -0.0234 -0.0408 1135 GLN A O   
8103  C CB  . GLN A 1137 ? 0.3140 0.4342 0.3949 -0.0251 -0.0250 -0.0375 1135 GLN A CB  
8104  C CG  . GLN A 1137 ? 0.3312 0.4423 0.4107 -0.0280 -0.0243 -0.0347 1135 GLN A CG  
8105  C CD  . GLN A 1137 ? 0.2923 0.3978 0.3734 -0.0301 -0.0271 -0.0360 1135 GLN A CD  
8106  O OE1 . GLN A 1137 ? 0.3686 0.4743 0.4495 -0.0278 -0.0294 -0.0393 1135 GLN A OE1 
8107  N NE2 . GLN A 1137 ? 0.4165 0.5170 0.4994 -0.0344 -0.0271 -0.0335 1135 GLN A NE2 
8108  N N   . ALA A 1138 ? 0.3270 0.4592 0.4070 -0.0156 -0.0278 -0.0445 1136 ALA A N   
8109  C CA  . ALA A 1138 ? 0.2905 0.4319 0.3720 -0.0126 -0.0280 -0.0466 1136 ALA A CA  
8110  C C   . ALA A 1138 ? 0.3219 0.4602 0.3978 -0.0062 -0.0279 -0.0475 1136 ALA A C   
8111  O O   . ALA A 1138 ? 0.3140 0.4593 0.3908 -0.0032 -0.0278 -0.0489 1136 ALA A O   
8112  C CB  . ALA A 1138 ? 0.3202 0.4678 0.4063 -0.0134 -0.0308 -0.0495 1136 ALA A CB  
8113  N N   . SER A 1139 ? 0.3013 0.4295 0.3714 -0.0041 -0.0279 -0.0467 1137 SER A N   
8114  C CA  . SER A 1139 ? 0.3320 0.4568 0.3967 0.0016  -0.0280 -0.0472 1137 SER A CA  
8115  C C   . SER A 1139 ? 0.2529 0.3765 0.3154 0.0029  -0.0252 -0.0451 1137 SER A C   
8116  O O   . SER A 1139 ? 0.2976 0.4191 0.3563 0.0076  -0.0252 -0.0454 1137 SER A O   
8117  C CB  . SER A 1139 ? 0.3245 0.4398 0.3842 0.0034  -0.0291 -0.0472 1137 SER A CB  
8118  O OG  . SER A 1139 ? 0.3576 0.4743 0.4187 0.0032  -0.0319 -0.0497 1137 SER A OG  
8119  N N   . LEU A 1140 ? 0.3145 0.4393 0.3793 -0.0011 -0.0231 -0.0429 1138 LEU A N   
8120  C CA  . LEU A 1140 ? 0.2990 0.4231 0.3618 -0.0002 -0.0206 -0.0411 1138 LEU A CA  
8121  C C   . LEU A 1140 ? 0.3289 0.4634 0.3966 -0.0022 -0.0191 -0.0411 1138 LEU A C   
8122  O O   . LEU A 1140 ? 0.3962 0.5312 0.4640 -0.0043 -0.0168 -0.0390 1138 LEU A O   
8123  C CB  . LEU A 1140 ? 0.3170 0.4325 0.3771 -0.0027 -0.0190 -0.0381 1138 LEU A CB  
8124  C CG  . LEU A 1140 ? 0.3074 0.4123 0.3617 -0.0001 -0.0196 -0.0377 1138 LEU A CG  
8125  C CD1 . LEU A 1140 ? 0.3593 0.4576 0.4116 -0.0025 -0.0176 -0.0347 1138 LEU A CD1 
8126  C CD2 . LEU A 1140 ? 0.2363 0.3398 0.2867 0.0056  -0.0199 -0.0387 1138 LEU A CD2 
8127  N N   . LYS A 1141 ? 0.3126 0.4560 0.3843 -0.0016 -0.0205 -0.0435 1139 LYS A N   
8128  C CA  . LYS A 1141 ? 0.4461 0.6007 0.5224 -0.0030 -0.0191 -0.0439 1139 LYS A CA  
8129  C C   . LYS A 1141 ? 0.4262 0.5820 0.5000 0.0013  -0.0177 -0.0443 1139 LYS A C   
8130  O O   . LYS A 1141 ? 0.3899 0.5413 0.4600 0.0064  -0.0187 -0.0456 1139 LYS A O   
8131  C CB  . LYS A 1141 ? 0.3963 0.5603 0.4775 -0.0029 -0.0211 -0.0467 1139 LYS A CB  
8132  N N   . ASN A 1142 ? 0.4049 0.5665 0.4807 -0.0007 -0.0153 -0.0431 1140 ASN A N   
8133  C CA  . ASN A 1142 ? 0.4026 0.5684 0.4776 0.0031  -0.0140 -0.0443 1140 ASN A CA  
8134  C C   . ASN A 1142 ? 0.3789 0.5342 0.4479 0.0067  -0.0136 -0.0434 1140 ASN A C   
8135  O O   . ASN A 1142 ? 0.3617 0.5168 0.4289 0.0117  -0.0142 -0.0452 1140 ASN A O   
8136  C CB  . ASN A 1142 ? 0.4261 0.6000 0.5037 0.0072  -0.0157 -0.0479 1140 ASN A CB  
8137  C CG  . ASN A 1142 ? 0.5387 0.7228 0.6223 0.0038  -0.0165 -0.0491 1140 ASN A CG  
8138  O OD1 . ASN A 1142 ? 0.5268 0.7127 0.6119 0.0055  -0.0189 -0.0512 1140 ASN A OD1 
8139  N ND2 . ASN A 1142 ? 0.5109 0.7022 0.5982 -0.0010 -0.0145 -0.0475 1140 ASN A ND2 
8140  N N   . LEU A 1143 ? 0.3771 0.5237 0.4431 0.0040  -0.0126 -0.0405 1141 LEU A N   
8141  C CA  . LEU A 1143 ? 0.3444 0.4815 0.4049 0.0069  -0.0119 -0.0394 1141 LEU A CA  
8142  C C   . LEU A 1143 ? 0.3668 0.5081 0.4273 0.0081  -0.0099 -0.0394 1141 LEU A C   
8143  O O   . LEU A 1143 ? 0.3226 0.4717 0.3864 0.0049  -0.0082 -0.0388 1141 LEU A O   
8144  C CB  . LEU A 1143 ? 0.3397 0.4674 0.3975 0.0036  -0.0113 -0.0364 1141 LEU A CB  
8145  C CG  . LEU A 1143 ? 0.3245 0.4447 0.3804 0.0035  -0.0133 -0.0364 1141 LEU A CG  
8146  C CD1 . LEU A 1143 ? 0.3116 0.4240 0.3655 0.0000  -0.0122 -0.0334 1141 LEU A CD1 
8147  C CD2 . LEU A 1143 ? 0.3208 0.4353 0.3724 0.0090  -0.0147 -0.0376 1141 LEU A CD2 
8148  N N   . PRO A 1144 ? 0.3570 0.4932 0.4139 0.0127  -0.0100 -0.0401 1142 PRO A N   
8149  C CA  . PRO A 1144 ? 0.3710 0.5091 0.4272 0.0136  -0.0080 -0.0399 1142 PRO A CA  
8150  C C   . PRO A 1144 ? 0.3426 0.4776 0.3979 0.0088  -0.0058 -0.0366 1142 PRO A C   
8151  O O   . PRO A 1144 ? 0.3023 0.4294 0.3555 0.0066  -0.0061 -0.0345 1142 PRO A O   
8152  C CB  . PRO A 1144 ? 0.3575 0.4872 0.4094 0.0187  -0.0089 -0.0405 1142 PRO A CB  
8153  C CG  . PRO A 1144 ? 0.3572 0.4843 0.4085 0.0213  -0.0115 -0.0418 1142 PRO A CG  
8154  C CD  . PRO A 1144 ? 0.3351 0.4630 0.3882 0.0169  -0.0119 -0.0407 1142 PRO A CD  
8155  N N   . GLN A 1145 ? 0.3091 0.4510 0.3660 0.0074  -0.0038 -0.0364 1143 GLN A N   
8156  C CA  . GLN A 1145 ? 0.3307 0.4705 0.3868 0.0029  -0.0018 -0.0331 1143 GLN A CA  
8157  C C   . GLN A 1145 ? 0.3161 0.4435 0.3672 0.0038  -0.0017 -0.0311 1143 GLN A C   
8158  O O   . GLN A 1145 ? 0.2896 0.4117 0.3396 0.0001  -0.0011 -0.0282 1143 GLN A O   
8159  C CB  . GLN A 1145 ? 0.3891 0.5380 0.4468 0.0023  0.0003  -0.0333 1143 GLN A CB  
8160  N N   . THR A 1146 ? 0.2977 0.4201 0.3457 0.0086  -0.0023 -0.0326 1144 THR A N   
8161  C CA  . THR A 1146 ? 0.3299 0.4410 0.3733 0.0094  -0.0021 -0.0308 1144 THR A CA  
8162  C C   . THR A 1146 ? 0.3205 0.4239 0.3623 0.0078  -0.0033 -0.0292 1144 THR A C   
8163  O O   . THR A 1146 ? 0.2936 0.3895 0.3328 0.0059  -0.0026 -0.0268 1144 THR A O   
8164  C CB  . THR A 1146 ? 0.3196 0.4267 0.3604 0.0149  -0.0030 -0.0326 1144 THR A CB  
8165  O OG1 . THR A 1146 ? 0.3333 0.4425 0.3753 0.0179  -0.0052 -0.0350 1144 THR A OG1 
8166  C CG2 . THR A 1146 ? 0.3342 0.4470 0.3758 0.0166  -0.0018 -0.0341 1144 THR A CG2 
8167  N N   . VAL A 1147 ? 0.2790 0.3842 0.3223 0.0089  -0.0052 -0.0309 1145 VAL A N   
8168  C CA  . VAL A 1147 ? 0.2335 0.3323 0.2756 0.0075  -0.0066 -0.0299 1145 VAL A CA  
8169  C C   . VAL A 1147 ? 0.2686 0.3700 0.3137 0.0021  -0.0061 -0.0283 1145 VAL A C   
8170  O O   . VAL A 1147 ? 0.2530 0.3475 0.2965 -0.0002 -0.0062 -0.0264 1145 VAL A O   
8171  C CB  . VAL A 1147 ? 0.2889 0.3889 0.3314 0.0108  -0.0090 -0.0323 1145 VAL A CB  
8172  C CG1 . VAL A 1147 ? 0.2300 0.3233 0.2706 0.0098  -0.0104 -0.0316 1145 VAL A CG1 
8173  C CG2 . VAL A 1147 ? 0.2563 0.3541 0.2962 0.0161  -0.0096 -0.0337 1145 VAL A CG2 
8174  N N   . GLY A 1148 ? 0.2984 0.4098 0.3480 0.0000  -0.0056 -0.0290 1146 GLY A N   
8175  C CA  . GLY A 1148 ? 0.2847 0.3990 0.3375 -0.0055 -0.0052 -0.0271 1146 GLY A CA  
8176  C C   . GLY A 1148 ? 0.2480 0.3570 0.2990 -0.0086 -0.0035 -0.0239 1146 GLY A C   
8177  O O   . GLY A 1148 ? 0.2905 0.3955 0.3422 -0.0122 -0.0040 -0.0220 1146 GLY A O   
8178  N N   . LEU A 1149 ? 0.2441 0.3527 0.2928 -0.0070 -0.0018 -0.0233 1147 LEU A N   
8179  C CA  . LEU A 1149 ? 0.3091 0.4127 0.3559 -0.0096 -0.0003 -0.0202 1147 LEU A CA  
8180  C C   . LEU A 1149 ? 0.2747 0.3669 0.3183 -0.0095 -0.0012 -0.0190 1147 LEU A C   
8181  O O   . LEU A 1149 ? 0.3162 0.4041 0.3593 -0.0127 -0.0006 -0.0164 1147 LEU A O   
8182  C CB  . LEU A 1149 ? 0.3317 0.4362 0.3762 -0.0072 0.0014  -0.0203 1147 LEU A CB  
8183  C CG  . LEU A 1149 ? 0.3901 0.5061 0.4374 -0.0073 0.0027  -0.0214 1147 LEU A CG  
8184  C CD1 . LEU A 1149 ? 0.3879 0.5033 0.4324 -0.0039 0.0038  -0.0223 1147 LEU A CD1 
8185  C CD2 . LEU A 1149 ? 0.4350 0.5568 0.4853 -0.0128 0.0040  -0.0187 1147 LEU A CD2 
8186  N N   . ARG A 1150 ? 0.2804 0.3679 0.3217 -0.0058 -0.0028 -0.0209 1148 ARG A N   
8187  C CA  . ARG A 1150 ? 0.2660 0.3434 0.3040 -0.0053 -0.0036 -0.0200 1148 ARG A CA  
8188  C C   . ARG A 1150 ? 0.2550 0.3309 0.2949 -0.0075 -0.0053 -0.0203 1148 ARG A C   
8189  O O   . ARG A 1150 ? 0.2857 0.3539 0.3233 -0.0075 -0.0060 -0.0197 1148 ARG A O   
8190  C CB  . ARG A 1150 ? 0.2884 0.3612 0.3225 -0.0003 -0.0042 -0.0215 1148 ARG A CB  
8191  C CG  . ARG A 1150 ? 0.2827 0.3537 0.3142 0.0019  -0.0027 -0.0209 1148 ARG A CG  
8192  C CD  . ARG A 1150 ? 0.2788 0.3404 0.3058 0.0044  -0.0031 -0.0204 1148 ARG A CD  
8193  N NE  . ARG A 1150 ? 0.2695 0.3293 0.2942 0.0072  -0.0021 -0.0203 1148 ARG A NE  
8194  C CZ  . ARG A 1150 ? 0.2776 0.3321 0.2992 0.0107  -0.0029 -0.0208 1148 ARG A CZ  
8195  N NH1 . ARG A 1150 ? 0.2489 0.2994 0.2688 0.0120  -0.0044 -0.0211 1148 ARG A NH1 
8196  N NH2 . ARG A 1150 ? 0.2407 0.2938 0.2607 0.0130  -0.0021 -0.0208 1148 ARG A NH2 
8197  N N   . VAL A 1151 ? 0.2266 0.3100 0.2708 -0.0094 -0.0062 -0.0214 1149 VAL A N   
8198  C CA  . VAL A 1151 ? 0.2666 0.3490 0.3128 -0.0110 -0.0082 -0.0224 1149 VAL A CA  
8199  C C   . VAL A 1151 ? 0.3303 0.4150 0.3806 -0.0166 -0.0080 -0.0204 1149 VAL A C   
8200  O O   . VAL A 1151 ? 0.2819 0.3744 0.3355 -0.0190 -0.0069 -0.0195 1149 VAL A O   
8201  C CB  . VAL A 1151 ? 0.2679 0.3567 0.3161 -0.0086 -0.0098 -0.0254 1149 VAL A CB  
8202  C CG1 . VAL A 1151 ? 0.3319 0.4209 0.3830 -0.0109 -0.0119 -0.0265 1149 VAL A CG1 
8203  C CG2 . VAL A 1151 ? 0.3018 0.3868 0.3457 -0.0033 -0.0104 -0.0270 1149 VAL A CG2 
8204  N N   . SER A 1152 ? 0.2862 0.3642 0.3364 -0.0186 -0.0092 -0.0196 1150 SER A N   
8205  C CA  . SER A 1152 ? 0.3042 0.3832 0.3587 -0.0238 -0.0098 -0.0180 1150 SER A CA  
8206  C C   . SER A 1152 ? 0.2947 0.3715 0.3509 -0.0241 -0.0125 -0.0202 1150 SER A C   
8207  O O   . SER A 1152 ? 0.2693 0.3412 0.3222 -0.0206 -0.0136 -0.0222 1150 SER A O   
8208  C CB  . SER A 1152 ? 0.3044 0.3767 0.3577 -0.0263 -0.0089 -0.0148 1150 SER A CB  
8209  N N   . TRP A 1153 ? 0.2775 0.3584 0.3390 -0.0284 -0.0136 -0.0198 1151 TRP A N   
8210  C CA  . TRP A 1153 ? 0.3170 0.3958 0.3808 -0.0293 -0.0164 -0.0219 1151 TRP A CA  
8211  C C   . TRP A 1153 ? 0.3790 0.4514 0.4446 -0.0335 -0.0172 -0.0197 1151 TRP A C   
8212  O O   . TRP A 1153 ? 0.3517 0.4261 0.4199 -0.0376 -0.0161 -0.0166 1151 TRP A O   
8213  C CB  . TRP A 1153 ? 0.3200 0.4081 0.3888 -0.0310 -0.0175 -0.0235 1151 TRP A CB  
8214  C CG  . TRP A 1153 ? 0.3160 0.4094 0.3832 -0.0264 -0.0175 -0.0264 1151 TRP A CG  
8215  C CD1 . TRP A 1153 ? 0.2879 0.3883 0.3548 -0.0246 -0.0157 -0.0263 1151 TRP A CD1 
8216  C CD2 . TRP A 1153 ? 0.2780 0.3701 0.3437 -0.0228 -0.0196 -0.0298 1151 TRP A CD2 
8217  N NE1 . TRP A 1153 ? 0.3387 0.4419 0.4043 -0.0201 -0.0167 -0.0294 1151 TRP A NE1 
8218  C CE2 . TRP A 1153 ? 0.3034 0.4016 0.3680 -0.0191 -0.0191 -0.0314 1151 TRP A CE2 
8219  C CE3 . TRP A 1153 ? 0.2792 0.3657 0.3443 -0.0224 -0.0221 -0.0317 1151 TRP A CE3 
8220  C CZ2 . TRP A 1153 ? 0.2755 0.3744 0.3385 -0.0150 -0.0209 -0.0344 1151 TRP A CZ2 
8221  C CZ3 . TRP A 1153 ? 0.3056 0.3933 0.3689 -0.0184 -0.0237 -0.0349 1151 TRP A CZ3 
8222  C CH2 . TRP A 1153 ? 0.3000 0.3937 0.3622 -0.0148 -0.0231 -0.0361 1151 TRP A CH2 
8223  N N   . SER A 1154 ? 0.3263 0.3913 0.3905 -0.0324 -0.0191 -0.0214 1152 SER A N   
8224  C CA  . SER A 1154 ? 0.3048 0.3623 0.3700 -0.0354 -0.0200 -0.0197 1152 SER A CA  
8225  C C   . SER A 1154 ? 0.3274 0.3834 0.3963 -0.0371 -0.0232 -0.0222 1152 SER A C   
8226  O O   . SER A 1154 ? 0.2809 0.3350 0.3478 -0.0337 -0.0248 -0.0256 1152 SER A O   
8227  C CB  . SER A 1154 ? 0.3219 0.3708 0.3815 -0.0321 -0.0193 -0.0195 1152 SER A CB  
8228  O OG  . SER A 1154 ? 0.3334 0.3754 0.3942 -0.0350 -0.0201 -0.0177 1152 SER A OG  
8229  N N   . LYS A 1155 ? 0.3173 0.3742 0.3917 -0.0423 -0.0243 -0.0204 1153 LYS A N   
8230  C CA  . LYS A 1155 ? 0.3132 0.3667 0.3915 -0.0444 -0.0276 -0.0224 1153 LYS A CA  
8231  C C   . LYS A 1155 ? 0.3616 0.4048 0.4385 -0.0448 -0.0285 -0.0216 1153 LYS A C   
8232  O O   . LYS A 1155 ? 0.4180 0.4561 0.4945 -0.0431 -0.0309 -0.0248 1153 LYS A O   
8233  C CB  . LYS A 1155 ? 0.3339 0.3932 0.4193 -0.0501 -0.0285 -0.0207 1153 LYS A CB  
8234  N N   . ASP A 1156 ? 0.3310 0.3714 0.4073 -0.0467 -0.0268 -0.0177 1154 ASP A N   
8235  C CA  . ASP A 1156 ? 0.3467 0.3777 0.4221 -0.0473 -0.0276 -0.0164 1154 ASP A CA  
8236  C C   . ASP A 1156 ? 0.3334 0.3610 0.4021 -0.0430 -0.0251 -0.0159 1154 ASP A C   
8237  O O   . ASP A 1156 ? 0.3434 0.3721 0.4106 -0.0437 -0.0227 -0.0125 1154 ASP A O   
8238  C CB  . ASP A 1156 ? 0.3298 0.3602 0.4096 -0.0529 -0.0276 -0.0119 1154 ASP A CB  
8239  C CG  . ASP A 1156 ? 0.4567 0.4773 0.5364 -0.0538 -0.0288 -0.0105 1154 ASP A CG  
8240  O OD1 . ASP A 1156 ? 0.4618 0.4763 0.5375 -0.0498 -0.0291 -0.0128 1154 ASP A OD1 
8241  O OD2 . ASP A 1156 ? 0.4358 0.4549 0.5197 -0.0586 -0.0296 -0.0070 1154 ASP A OD2 
8242  N N   . TRP A 1157 ? 0.3380 0.3617 0.4029 -0.0385 -0.0258 -0.0193 1155 TRP A N   
8243  C CA  . TRP A 1157 ? 0.3186 0.3398 0.3772 -0.0343 -0.0236 -0.0191 1155 TRP A CA  
8244  C C   . TRP A 1157 ? 0.3520 0.3671 0.4093 -0.0355 -0.0225 -0.0158 1155 TRP A C   
8245  O O   . TRP A 1157 ? 0.3768 0.3925 0.4307 -0.0341 -0.0199 -0.0137 1155 TRP A O   
8246  C CB  . TRP A 1157 ? 0.3170 0.3347 0.3719 -0.0299 -0.0249 -0.0230 1155 TRP A CB  
8247  C CG  . TRP A 1157 ? 0.3246 0.3478 0.3800 -0.0280 -0.0261 -0.0264 1155 TRP A CG  
8248  C CD1 . TRP A 1157 ? 0.2924 0.3234 0.3506 -0.0294 -0.0259 -0.0264 1155 TRP A CD1 
8249  C CD2 . TRP A 1157 ? 0.3342 0.3556 0.3869 -0.0244 -0.0277 -0.0304 1155 TRP A CD2 
8250  N NE1 . TRP A 1157 ? 0.3298 0.3639 0.3874 -0.0267 -0.0275 -0.0301 1155 TRP A NE1 
8251  C CE2 . TRP A 1157 ? 0.3291 0.3574 0.3832 -0.0237 -0.0286 -0.0325 1155 TRP A CE2 
8252  C CE3 . TRP A 1157 ? 0.3381 0.3533 0.3875 -0.0216 -0.0285 -0.0323 1155 TRP A CE3 
8253  C CZ2 . TRP A 1157 ? 0.3400 0.3689 0.3921 -0.0204 -0.0303 -0.0364 1155 TRP A CZ2 
8254  C CZ3 . TRP A 1157 ? 0.3089 0.3252 0.3563 -0.0184 -0.0301 -0.0362 1155 TRP A CZ3 
8255  C CH2 . TRP A 1157 ? 0.2934 0.3163 0.3420 -0.0178 -0.0310 -0.0381 1155 TRP A CH2 
8256  N N   . ALA A 1158 ? 0.3753 0.3846 0.4356 -0.0379 -0.0246 -0.0155 1156 ALA A N   
8257  C CA  . ALA A 1158 ? 0.4108 0.4141 0.4702 -0.0390 -0.0239 -0.0125 1156 ALA A CA  
8258  C C   . ALA A 1158 ? 0.4018 0.4089 0.4627 -0.0425 -0.0219 -0.0078 1156 ALA A C   
8259  O O   . ALA A 1158 ? 0.4733 0.4772 0.5320 -0.0424 -0.0204 -0.0051 1156 ALA A O   
8260  C CB  . ALA A 1158 ? 0.4020 0.3983 0.4650 -0.0409 -0.0269 -0.0132 1156 ALA A CB  
8261  N N   . ALA A 1159 ? 0.3974 0.4116 0.4620 -0.0455 -0.0219 -0.0069 1157 ALA A N   
8262  C CA  . ALA A 1159 ? 0.4131 0.4322 0.4792 -0.0488 -0.0199 -0.0025 1157 ALA A CA  
8263  C C   . ALA A 1159 ? 0.4515 0.4762 0.5134 -0.0460 -0.0168 -0.0022 1157 ALA A C   
8264  O O   . ALA A 1159 ? 0.4740 0.5012 0.5353 -0.0476 -0.0147 0.0013  1157 ALA A O   
8265  C CB  . ALA A 1159 ? 0.3659 0.3911 0.4380 -0.0535 -0.0211 -0.0016 1157 ALA A CB  
8266  N N   . ASP A 1160 ? 0.4213 0.4479 0.4802 -0.0417 -0.0164 -0.0057 1158 ASP A N   
8267  C CA  . ASP A 1160 ? 0.3878 0.4202 0.4435 -0.0390 -0.0139 -0.0058 1158 ASP A CA  
8268  C C   . ASP A 1160 ? 0.3990 0.4264 0.4489 -0.0346 -0.0125 -0.0064 1158 ASP A C   
8269  O O   . ASP A 1160 ? 0.3935 0.4245 0.4404 -0.0318 -0.0107 -0.0069 1158 ASP A O   
8270  C CB  . ASP A 1160 ? 0.3959 0.4349 0.4529 -0.0376 -0.0146 -0.0089 1158 ASP A CB  
8271  C CG  . ASP A 1160 ? 0.4547 0.4996 0.5177 -0.0422 -0.0158 -0.0082 1158 ASP A CG  
8272  O OD1 . ASP A 1160 ? 0.5107 0.5571 0.5763 -0.0462 -0.0150 -0.0045 1158 ASP A OD1 
8273  O OD2 . ASP A 1160 ? 0.3864 0.4346 0.4517 -0.0419 -0.0174 -0.0110 1158 ASP A OD2 
8274  N N   . GLY A 1161 ? 0.3909 0.4101 0.4393 -0.0340 -0.0135 -0.0064 1159 GLY A N   
8275  C CA  . GLY A 1161 ? 0.3734 0.3879 0.4166 -0.0303 -0.0122 -0.0067 1159 GLY A CA  
8276  C C   . GLY A 1161 ? 0.4544 0.4678 0.4964 -0.0316 -0.0102 -0.0031 1159 GLY A C   
8277  O O   . GLY A 1161 ? 0.4302 0.4472 0.4750 -0.0352 -0.0097 -0.0002 1159 GLY A O   
8278  N N   . PRO A 1162 ? 0.4120 0.4205 0.4499 -0.0287 -0.0092 -0.0030 1160 PRO A N   
8279  C CA  . PRO A 1162 ? 0.3759 0.3800 0.4103 -0.0247 -0.0097 -0.0058 1160 PRO A CA  
8280  C C   . PRO A 1162 ? 0.3572 0.3653 0.3889 -0.0212 -0.0089 -0.0080 1160 PRO A C   
8281  O O   . PRO A 1162 ? 0.3249 0.3379 0.3558 -0.0207 -0.0073 -0.0072 1160 PRO A O   
8282  C CB  . PRO A 1162 ? 0.3834 0.3821 0.4147 -0.0236 -0.0085 -0.0041 1160 PRO A CB  
8283  C CG  . PRO A 1162 ? 0.4496 0.4521 0.4811 -0.0255 -0.0065 -0.0010 1160 PRO A CG  
8284  C CD  . PRO A 1162 ? 0.4222 0.4294 0.4585 -0.0296 -0.0074 0.0002  1160 PRO A CD  
8285  N N   . PHE A 1163 ? 0.2846 0.2910 0.3149 -0.0187 -0.0103 -0.0109 1161 PHE A N   
8286  C CA  . PHE A 1163 ? 0.2335 0.2423 0.2606 -0.0149 -0.0097 -0.0128 1161 PHE A CA  
8287  C C   . PHE A 1163 ? 0.2588 0.2627 0.2811 -0.0117 -0.0087 -0.0127 1161 PHE A C   
8288  O O   . PHE A 1163 ? 0.3295 0.3282 0.3510 -0.0122 -0.0085 -0.0117 1161 PHE A O   
8289  C CB  . PHE A 1163 ? 0.2473 0.2580 0.2757 -0.0140 -0.0119 -0.0159 1161 PHE A CB  
8290  C CG  . PHE A 1163 ? 0.2650 0.2802 0.2985 -0.0175 -0.0131 -0.0161 1161 PHE A CG  
8291  C CD1 . PHE A 1163 ? 0.2728 0.2948 0.3082 -0.0187 -0.0120 -0.0151 1161 PHE A CD1 
8292  C CD2 . PHE A 1163 ? 0.2725 0.2853 0.3092 -0.0197 -0.0154 -0.0172 1161 PHE A CD2 
8293  C CE1 . PHE A 1163 ? 0.2784 0.3052 0.3188 -0.0222 -0.0131 -0.0149 1161 PHE A CE1 
8294  C CE2 . PHE A 1163 ? 0.2950 0.3121 0.3369 -0.0233 -0.0166 -0.0171 1161 PHE A CE2 
8295  C CZ  . PHE A 1163 ? 0.3244 0.3486 0.3681 -0.0246 -0.0154 -0.0159 1161 PHE A CZ  
8296  N N   . ALA A 1164 ? 0.2562 0.2621 0.2755 -0.0085 -0.0079 -0.0135 1162 ALA A N   
8297  C CA  . ALA A 1164 ? 0.2795 0.2814 0.2943 -0.0055 -0.0068 -0.0132 1162 ALA A CA  
8298  C C   . ALA A 1164 ? 0.2752 0.2767 0.2875 -0.0023 -0.0079 -0.0156 1162 ALA A C   
8299  O O   . ALA A 1164 ? 0.2969 0.2959 0.3053 0.0004  -0.0071 -0.0153 1162 ALA A O   
8300  C CB  . ALA A 1164 ? 0.2816 0.2857 0.2948 -0.0044 -0.0049 -0.0116 1162 ALA A CB  
8301  N N   . GLY A 1165 ? 0.2235 0.2276 0.2377 -0.0026 -0.0098 -0.0178 1163 GLY A N   
8302  C CA  . GLY A 1165 ? 0.2216 0.2260 0.2335 0.0003  -0.0111 -0.0201 1163 GLY A CA  
8303  C C   . GLY A 1165 ? 0.2436 0.2525 0.2588 -0.0006 -0.0130 -0.0223 1163 GLY A C   
8304  O O   . GLY A 1165 ? 0.2355 0.2474 0.2547 -0.0036 -0.0132 -0.0218 1163 GLY A O   
8305  N N   . ALA A 1166 ? 0.2315 0.2412 0.2449 0.0018  -0.0145 -0.0247 1164 ALA A N   
8306  C CA  . ALA A 1166 ? 0.2380 0.2520 0.2544 0.0011  -0.0165 -0.0271 1164 ALA A CA  
8307  C C   . ALA A 1166 ? 0.2405 0.2570 0.2539 0.0048  -0.0174 -0.0288 1164 ALA A C   
8308  O O   . ALA A 1166 ? 0.2693 0.2830 0.2784 0.0074  -0.0172 -0.0289 1164 ALA A O   
8309  C CB  . ALA A 1166 ? 0.2555 0.2673 0.2748 -0.0011 -0.0185 -0.0289 1164 ALA A CB  
8310  N N   . LEU A 1167 ? 0.2324 0.2544 0.2479 0.0048  -0.0185 -0.0301 1165 LEU A N   
8311  C CA  . LEU A 1167 ? 0.2287 0.2537 0.2420 0.0080  -0.0199 -0.0320 1165 LEU A CA  
8312  C C   . LEU A 1167 ? 0.2496 0.2779 0.2665 0.0067  -0.0224 -0.0350 1165 LEU A C   
8313  O O   . LEU A 1167 ? 0.2527 0.2842 0.2744 0.0037  -0.0228 -0.0351 1165 LEU A O   
8314  C CB  . LEU A 1167 ? 0.2270 0.2561 0.2398 0.0099  -0.0192 -0.0311 1165 LEU A CB  
8315  C CG  . LEU A 1167 ? 0.2462 0.2723 0.2561 0.0112  -0.0169 -0.0283 1165 LEU A CG  
8316  C CD1 . LEU A 1167 ? 0.2243 0.2546 0.2345 0.0129  -0.0166 -0.0278 1165 LEU A CD1 
8317  C CD2 . LEU A 1167 ? 0.2431 0.2647 0.2477 0.0138  -0.0167 -0.0277 1165 LEU A CD2 
8318  N N   . VAL A 1168 ? 0.2335 0.2613 0.2482 0.0087  -0.0241 -0.0374 1166 VAL A N   
8319  C CA  . VAL A 1168 ? 0.2360 0.2662 0.2538 0.0075  -0.0267 -0.0407 1166 VAL A CA  
8320  C C   . VAL A 1168 ? 0.2495 0.2840 0.2650 0.0109  -0.0283 -0.0427 1166 VAL A C   
8321  O O   . VAL A 1168 ? 0.2465 0.2798 0.2569 0.0142  -0.0279 -0.0422 1166 VAL A O   
8322  C CB  . VAL A 1168 ? 0.2398 0.2652 0.2576 0.0066  -0.0277 -0.0422 1166 VAL A CB  
8323  C CG1 . VAL A 1168 ? 0.2637 0.2917 0.2852 0.0055  -0.0307 -0.0460 1166 VAL A CG1 
8324  C CG2 . VAL A 1168 ? 0.2802 0.3012 0.3002 0.0034  -0.0262 -0.0399 1166 VAL A CG2 
8325  N N   . GLU A 1169 ? 0.2481 0.2878 0.2675 0.0099  -0.0303 -0.0449 1167 GLU A N   
8326  C CA  . GLU A 1169 ? 0.2496 0.2936 0.2673 0.0128  -0.0323 -0.0473 1167 GLU A CA  
8327  C C   . GLU A 1169 ? 0.2814 0.3268 0.3022 0.0114  -0.0350 -0.0510 1167 GLU A C   
8328  O O   . GLU A 1169 ? 0.2548 0.3007 0.2810 0.0077  -0.0358 -0.0517 1167 GLU A O   
8329  C CB  . GLU A 1169 ? 0.2397 0.2897 0.2594 0.0134  -0.0323 -0.0468 1167 GLU A CB  
8330  C CG  . GLU A 1169 ? 0.2508 0.3059 0.2694 0.0163  -0.0346 -0.0492 1167 GLU A CG  
8331  C CD  . GLU A 1169 ? 0.2465 0.3080 0.2688 0.0160  -0.0350 -0.0494 1167 GLU A CD  
8332  O OE1 . GLU A 1169 ? 0.2723 0.3348 0.2985 0.0132  -0.0337 -0.0480 1167 GLU A OE1 
8333  O OE2 . GLU A 1169 ? 0.2958 0.3618 0.3172 0.0187  -0.0368 -0.0509 1167 GLU A OE2 
8334  N N   . GLY A 1170 ? 0.2693 0.3152 0.2865 0.0143  -0.0367 -0.0534 1168 GLY A N   
8335  C CA  . GLY A 1170 ? 0.2927 0.3406 0.3127 0.0135  -0.0396 -0.0575 1168 GLY A CA  
8336  C C   . GLY A 1170 ? 0.3118 0.3589 0.3267 0.0168  -0.0408 -0.0598 1168 GLY A C   
8337  O O   . GLY A 1170 ? 0.3133 0.3584 0.3227 0.0196  -0.0392 -0.0579 1168 GLY A O   
8338  N N   . ASP A 1171 ? 0.3187 0.3678 0.3358 0.0165  -0.0437 -0.0639 1169 ASP A N   
8339  C CA  . ASP A 1171 ? 0.3049 0.3534 0.3176 0.0194  -0.0449 -0.0667 1169 ASP A CA  
8340  C C   . ASP A 1171 ? 0.3519 0.3941 0.3643 0.0183  -0.0441 -0.0668 1169 ASP A C   
8341  O O   . ASP A 1171 ? 0.3249 0.3630 0.3405 0.0152  -0.0427 -0.0647 1169 ASP A O   
8342  C CB  . ASP A 1171 ? 0.3338 0.3872 0.3488 0.0198  -0.0485 -0.0714 1169 ASP A CB  
8343  C CG  . ASP A 1171 ? 0.3638 0.4160 0.3859 0.0157  -0.0504 -0.0741 1169 ASP A CG  
8344  O OD1 . ASP A 1171 ? 0.3443 0.3914 0.3692 0.0127  -0.0492 -0.0725 1169 ASP A OD1 
8345  O OD2 . ASP A 1171 ? 0.4080 0.4644 0.4330 0.0154  -0.0533 -0.0777 1169 ASP A OD2 
8346  N N   . ALA A 1172 ? 0.3396 0.3812 0.3481 0.0209  -0.0450 -0.0694 1170 ALA A N   
8347  C CA  . ALA A 1172 ? 0.3580 0.3940 0.3654 0.0206  -0.0441 -0.0695 1170 ALA A CA  
8348  C C   . ALA A 1172 ? 0.3307 0.3630 0.3446 0.0167  -0.0453 -0.0711 1170 ALA A C   
8349  O O   . ALA A 1172 ? 0.3262 0.3532 0.3411 0.0150  -0.0437 -0.0690 1170 ALA A O   
8350  C CB  . ALA A 1172 ? 0.3969 0.4344 0.3995 0.0241  -0.0452 -0.0727 1170 ALA A CB  
8351  N N   . GLU A 1173 ? 0.3497 0.3846 0.3684 0.0152  -0.0484 -0.0748 1171 GLU A N   
8352  C CA  . GLU A 1173 ? 0.3676 0.3987 0.3928 0.0112  -0.0499 -0.0761 1171 GLU A CA  
8353  C C   . GLU A 1173 ? 0.3570 0.3863 0.3861 0.0075  -0.0479 -0.0716 1171 GLU A C   
8354  O O   . GLU A 1173 ? 0.3505 0.3745 0.3825 0.0048  -0.0474 -0.0704 1171 GLU A O   
8355  C CB  . GLU A 1173 ? 0.3423 0.3770 0.3721 0.0102  -0.0537 -0.0808 1171 GLU A CB  
8356  N N   . ARG A 1174 ? 0.3180 0.3518 0.3469 0.0074  -0.0468 -0.0692 1172 ARG A N   
8357  C CA  . ARG A 1174 ? 0.3065 0.3397 0.3387 0.0041  -0.0448 -0.0651 1172 ARG A CA  
8358  C C   . ARG A 1174 ? 0.3117 0.3400 0.3403 0.0047  -0.0416 -0.0612 1172 ARG A C   
8359  O O   . ARG A 1174 ? 0.2885 0.3132 0.3202 0.0015  -0.0405 -0.0587 1172 ARG A O   
8360  C CB  . ARG A 1174 ? 0.3016 0.3413 0.3341 0.0046  -0.0443 -0.0639 1172 ARG A CB  
8361  C CG  . ARG A 1174 ? 0.2983 0.3385 0.3336 0.0018  -0.0420 -0.0598 1172 ARG A CG  
8362  C CD  . ARG A 1174 ? 0.3648 0.4038 0.4071 -0.0032 -0.0431 -0.0597 1172 ARG A CD  
8363  N NE  . ARG A 1174 ? 0.3555 0.3961 0.4004 -0.0060 -0.0409 -0.0558 1172 ARG A NE  
8364  C CZ  . ARG A 1174 ? 0.3637 0.4025 0.4137 -0.0105 -0.0408 -0.0541 1172 ARG A CZ  
8365  N NH1 . ARG A 1174 ? 0.3318 0.3665 0.3853 -0.0129 -0.0429 -0.0558 1172 ARG A NH1 
8366  N NH2 . ARG A 1174 ? 0.2860 0.3273 0.3377 -0.0126 -0.0386 -0.0506 1172 ARG A NH2 
8367  N N   . ILE A 1175 ? 0.2961 0.3244 0.3183 0.0085  -0.0401 -0.0605 1173 ILE A N   
8368  C CA  . ILE A 1175 ? 0.2928 0.3167 0.3115 0.0092  -0.0372 -0.0569 1173 ILE A CA  
8369  C C   . ILE A 1175 ? 0.3089 0.3269 0.3291 0.0078  -0.0375 -0.0577 1173 ILE A C   
8370  O O   . ILE A 1175 ? 0.2834 0.2973 0.3046 0.0058  -0.0357 -0.0547 1173 ILE A O   
8371  C CB  . ILE A 1175 ? 0.2931 0.3184 0.3049 0.0136  -0.0360 -0.0563 1173 ILE A CB  
8372  C CG1 . ILE A 1175 ? 0.2980 0.3283 0.3084 0.0150  -0.0354 -0.0546 1173 ILE A CG1 
8373  C CG2 . ILE A 1175 ? 0.2667 0.2870 0.2749 0.0143  -0.0333 -0.0534 1173 ILE A CG2 
8374  C CD1 . ILE A 1175 ? 0.2861 0.3180 0.2899 0.0193  -0.0349 -0.0542 1173 ILE A CD1 
8375  N N   . ARG A 1176 ? 0.3220 0.3393 0.3424 0.0088  -0.0399 -0.0620 1174 ARG A N   
8376  C CA  . ARG A 1176 ? 0.3129 0.3246 0.3349 0.0078  -0.0406 -0.0633 1174 ARG A CA  
8377  C C   . ARG A 1176 ? 0.3085 0.3172 0.3372 0.0032  -0.0413 -0.0621 1174 ARG A C   
8378  O O   . ARG A 1176 ? 0.3465 0.3500 0.3761 0.0016  -0.0401 -0.0598 1174 ARG A O   
8379  C CB  . ARG A 1176 ? 0.3045 0.3169 0.3260 0.0100  -0.0435 -0.0688 1174 ARG A CB  
8380  C CG  . ARG A 1176 ? 0.4040 0.4110 0.4254 0.0105  -0.0438 -0.0704 1174 ARG A CG  
8381  C CD  . ARG A 1176 ? 0.4249 0.4328 0.4469 0.0122  -0.0472 -0.0765 1174 ARG A CD  
8382  N NE  . ARG A 1176 ? 0.5124 0.5264 0.5298 0.0157  -0.0477 -0.0787 1174 ARG A NE  
8383  C CZ  . ARG A 1176 ? 0.5623 0.5781 0.5734 0.0196  -0.0465 -0.0792 1174 ARG A CZ  
8384  N NH1 . ARG A 1176 ? 0.5353 0.5475 0.5439 0.0206  -0.0445 -0.0778 1174 ARG A NH1 
8385  N NH2 . ARG A 1176 ? 0.4997 0.5214 0.5070 0.0224  -0.0473 -0.0810 1174 ARG A NH2 
8386  N N   . ALA A 1177 ? 0.2830 0.2950 0.3164 0.0008  -0.0432 -0.0633 1175 ALA A N   
8387  C CA  . ALA A 1177 ? 0.3331 0.3429 0.3732 -0.0040 -0.0441 -0.0619 1175 ALA A CA  
8388  C C   . ALA A 1177 ? 0.3058 0.3150 0.3459 -0.0060 -0.0410 -0.0565 1175 ALA A C   
8389  O O   . ALA A 1177 ? 0.3047 0.3097 0.3481 -0.0092 -0.0407 -0.0543 1175 ALA A O   
8390  C CB  . ALA A 1177 ? 0.3338 0.3484 0.3788 -0.0061 -0.0467 -0.0642 1175 ALA A CB  
8391  N N   . VAL A 1178 ? 0.3028 0.3163 0.3395 -0.0043 -0.0388 -0.0544 1176 VAL A N   
8392  C CA  . VAL A 1178 ? 0.2922 0.3055 0.3287 -0.0059 -0.0359 -0.0497 1176 VAL A CA  
8393  C C   . VAL A 1178 ? 0.3097 0.3173 0.3427 -0.0048 -0.0338 -0.0476 1176 VAL A C   
8394  O O   . VAL A 1178 ? 0.3085 0.3132 0.3434 -0.0074 -0.0325 -0.0444 1176 VAL A O   
8395  C CB  . VAL A 1178 ? 0.2683 0.2874 0.3021 -0.0039 -0.0343 -0.0484 1176 VAL A CB  
8396  C CG1 . VAL A 1178 ? 0.2423 0.2608 0.2753 -0.0049 -0.0312 -0.0438 1176 VAL A CG1 
8397  C CG2 . VAL A 1178 ? 0.2871 0.3123 0.3251 -0.0054 -0.0362 -0.0502 1176 VAL A CG2 
8398  N N   . ASN A 1179 ? 0.3106 0.3169 0.3386 -0.0010 -0.0336 -0.0492 1177 ASN A N   
8399  C CA  . ASN A 1179 ? 0.3228 0.3242 0.3473 0.0003  -0.0317 -0.0475 1177 ASN A CA  
8400  C C   . ASN A 1179 ? 0.3421 0.3378 0.3704 -0.0022 -0.0329 -0.0478 1177 ASN A C   
8401  O O   . ASN A 1179 ? 0.3646 0.3564 0.3925 -0.0031 -0.0312 -0.0450 1177 ASN A O   
8402  C CB  . ASN A 1179 ? 0.3592 0.3612 0.3781 0.0047  -0.0316 -0.0496 1177 ASN A CB  
8403  C CG  . ASN A 1179 ? 0.4264 0.4255 0.4407 0.0065  -0.0289 -0.0469 1177 ASN A CG  
8404  O OD1 . ASN A 1179 ? 0.4558 0.4537 0.4700 0.0052  -0.0267 -0.0432 1177 ASN A OD1 
8405  N ND2 . ASN A 1179 ? 0.4533 0.4516 0.4636 0.0096  -0.0290 -0.0489 1177 ASN A ND2 
8406  N N   . LYS A 1180 ? 0.3071 0.3023 0.3394 -0.0035 -0.0360 -0.0514 1178 LYS A N   
8407  C CA  . LYS A 1180 ? 0.3767 0.3663 0.4134 -0.0061 -0.0376 -0.0517 1178 LYS A CA  
8408  C C   . LYS A 1180 ? 0.3329 0.3217 0.3743 -0.0106 -0.0370 -0.0478 1178 LYS A C   
8409  O O   . LYS A 1180 ? 0.3697 0.3536 0.4126 -0.0124 -0.0366 -0.0455 1178 LYS A O   
8410  C CB  . LYS A 1180 ? 0.3523 0.3416 0.3924 -0.0061 -0.0415 -0.0568 1178 LYS A CB  
8411  C CG  . LYS A 1180 ? 0.3869 0.3760 0.4228 -0.0017 -0.0423 -0.0610 1178 LYS A CG  
8412  C CD  . LYS A 1180 ? 0.3770 0.3676 0.4159 -0.0015 -0.0461 -0.0665 1178 LYS A CD  
8413  C CE  . LYS A 1180 ? 0.5149 0.5006 0.5609 -0.0052 -0.0490 -0.0676 1178 LYS A CE  
8414  N NZ  . LYS A 1180 ? 0.5455 0.5336 0.5957 -0.0061 -0.0527 -0.0720 1178 LYS A NZ  
8415  N N   . ALA A 1181 ? 0.2610 0.2550 0.3046 -0.0126 -0.0370 -0.0468 1179 ALA A N   
8416  C CA  . ALA A 1181 ? 0.3115 0.3061 0.3593 -0.0169 -0.0361 -0.0429 1179 ALA A CA  
8417  C C   . ALA A 1181 ? 0.3327 0.3265 0.3772 -0.0165 -0.0327 -0.0386 1179 ALA A C   
8418  O O   . ALA A 1181 ? 0.3186 0.3099 0.3655 -0.0197 -0.0319 -0.0353 1179 ALA A O   
8419  C CB  . ALA A 1181 ? 0.2826 0.2841 0.3333 -0.0186 -0.0367 -0.0431 1179 ALA A CB  
8420  N N   . ILE A 1182 ? 0.3018 0.2976 0.3406 -0.0128 -0.0306 -0.0385 1180 ILE A N   
8421  C CA  . ILE A 1182 ? 0.2724 0.2675 0.3081 -0.0123 -0.0274 -0.0346 1180 ILE A CA  
8422  C C   . ILE A 1182 ? 0.2981 0.2866 0.3326 -0.0121 -0.0270 -0.0337 1180 ILE A C   
8423  O O   . ILE A 1182 ? 0.3013 0.2879 0.3359 -0.0137 -0.0252 -0.0301 1180 ILE A O   
8424  C CB  . ILE A 1182 ? 0.3119 0.3106 0.3422 -0.0085 -0.0257 -0.0348 1180 ILE A CB  
8425  C CG1 . ILE A 1182 ? 0.3164 0.3218 0.3483 -0.0090 -0.0258 -0.0349 1180 ILE A CG1 
8426  C CG2 . ILE A 1182 ? 0.3319 0.3285 0.3584 -0.0073 -0.0227 -0.0314 1180 ILE A CG2 
8427  C CD1 . ILE A 1182 ? 0.3200 0.3289 0.3471 -0.0049 -0.0248 -0.0356 1180 ILE A CD1 
8428  N N   . ALA A 1183 ? 0.2793 0.2647 0.3126 -0.0099 -0.0286 -0.0370 1181 ALA A N   
8429  C CA  . ALA A 1183 ? 0.3618 0.3412 0.3942 -0.0093 -0.0284 -0.0365 1181 ALA A CA  
8430  C C   . ALA A 1183 ? 0.3956 0.3711 0.4334 -0.0134 -0.0297 -0.0347 1181 ALA A C   
8431  O O   . ALA A 1183 ? 0.3640 0.3350 0.4014 -0.0138 -0.0288 -0.0327 1181 ALA A O   
8432  C CB  . ALA A 1183 ? 0.3037 0.2814 0.3342 -0.0061 -0.0301 -0.0409 1181 ALA A CB  
8433  N N   . ALA A 1184 ? 0.3119 0.2890 0.3547 -0.0165 -0.0317 -0.0353 1182 ALA A N   
8434  C CA  . ALA A 1184 ? 0.3652 0.3388 0.4135 -0.0208 -0.0332 -0.0333 1182 ALA A CA  
8435  C C   . ALA A 1184 ? 0.3740 0.3498 0.4232 -0.0239 -0.0308 -0.0282 1182 ALA A C   
8436  O O   . ALA A 1184 ? 0.3667 0.3398 0.4200 -0.0276 -0.0317 -0.0256 1182 ALA A O   
8437  C CB  . ALA A 1184 ? 0.3425 0.3171 0.3963 -0.0233 -0.0365 -0.0359 1182 ALA A CB  
8438  N N   . LEU A 1185 ? 0.3505 0.3310 0.3959 -0.0224 -0.0281 -0.0266 1183 LEU A N   
8439  C CA  . LEU A 1185 ? 0.3602 0.3433 0.4063 -0.0250 -0.0258 -0.0222 1183 LEU A CA  
8440  C C   . LEU A 1185 ? 0.3976 0.3756 0.4421 -0.0251 -0.0245 -0.0193 1183 LEU A C   
8441  O O   . LEU A 1185 ? 0.3628 0.3379 0.4032 -0.0217 -0.0236 -0.0203 1183 LEU A O   
8442  C CB  . LEU A 1185 ? 0.2914 0.2807 0.3340 -0.0229 -0.0234 -0.0218 1183 LEU A CB  
8443  C CG  . LEU A 1185 ? 0.3449 0.3400 0.3890 -0.0227 -0.0246 -0.0243 1183 LEU A CG  
8444  C CD1 . LEU A 1185 ? 0.3004 0.3009 0.3408 -0.0201 -0.0223 -0.0238 1183 LEU A CD1 
8445  C CD2 . LEU A 1185 ? 0.3117 0.3096 0.3620 -0.0275 -0.0260 -0.0231 1183 LEU A CD2 
8446  N N   . PRO A 1186 ? 0.3737 0.3509 0.4215 -0.0289 -0.0243 -0.0156 1184 PRO A N   
8447  C CA  . PRO A 1186 ? 0.3971 0.3699 0.4432 -0.0290 -0.0230 -0.0126 1184 PRO A CA  
8448  C C   . PRO A 1186 ? 0.3437 0.3191 0.3848 -0.0265 -0.0197 -0.0111 1184 PRO A C   
8449  O O   . PRO A 1186 ? 0.3477 0.3290 0.3875 -0.0261 -0.0182 -0.0109 1184 PRO A O   
8450  C CB  . PRO A 1186 ? 0.4223 0.3952 0.4731 -0.0341 -0.0236 -0.0087 1184 PRO A CB  
8451  C CG  . PRO A 1186 ? 0.5073 0.4870 0.5608 -0.0362 -0.0238 -0.0089 1184 PRO A CG  
8452  C CD  . PRO A 1186 ? 0.4340 0.4144 0.4870 -0.0335 -0.0254 -0.0138 1184 PRO A CD  
8453  N N   . GLY A 1187 ? 0.3823 0.3533 0.4206 -0.0249 -0.0188 -0.0102 1185 GLY A N   
8454  C CA  . GLY A 1187 ? 0.3887 0.3615 0.4228 -0.0230 -0.0158 -0.0084 1185 GLY A CA  
8455  C C   . GLY A 1187 ? 0.3577 0.3299 0.3871 -0.0185 -0.0150 -0.0111 1185 GLY A C   
8456  O O   . GLY A 1187 ? 0.3506 0.3189 0.3792 -0.0166 -0.0163 -0.0135 1185 GLY A O   
8457  N N   . PRO A 1188 ? 0.3220 0.2984 0.3482 -0.0168 -0.0129 -0.0107 1186 PRO A N   
8458  C CA  . PRO A 1188 ? 0.3395 0.3152 0.3609 -0.0127 -0.0118 -0.0122 1186 PRO A CA  
8459  C C   . PRO A 1188 ? 0.3406 0.3170 0.3614 -0.0105 -0.0134 -0.0160 1186 PRO A C   
8460  O O   . PRO A 1188 ? 0.2897 0.2690 0.3131 -0.0116 -0.0150 -0.0176 1186 PRO A O   
8461  C CB  . PRO A 1188 ? 0.3599 0.3401 0.3791 -0.0120 -0.0095 -0.0106 1186 PRO A CB  
8462  C CG  . PRO A 1188 ? 0.3951 0.3800 0.4180 -0.0148 -0.0101 -0.0100 1186 PRO A CG  
8463  C CD  . PRO A 1188 ? 0.3394 0.3216 0.3665 -0.0184 -0.0116 -0.0089 1186 PRO A CD  
8464  N N   . LEU A 1189 ? 0.2790 0.2532 0.2961 -0.0073 -0.0131 -0.0175 1187 LEU A N   
8465  C CA  . LEU A 1189 ? 0.3078 0.2835 0.3232 -0.0047 -0.0142 -0.0210 1187 LEU A CA  
8466  C C   . LEU A 1189 ? 0.3401 0.3206 0.3532 -0.0032 -0.0131 -0.0208 1187 LEU A C   
8467  O O   . LEU A 1189 ? 0.4387 0.4196 0.4485 -0.0016 -0.0111 -0.0190 1187 LEU A O   
8468  C CB  . LEU A 1189 ? 0.3441 0.3167 0.3562 -0.0017 -0.0140 -0.0223 1187 LEU A CB  
8469  C CG  . LEU A 1189 ? 0.3662 0.3345 0.3804 -0.0020 -0.0159 -0.0244 1187 LEU A CG  
8470  C CD1 . LEU A 1189 ? 0.4257 0.3903 0.4430 -0.0049 -0.0159 -0.0218 1187 LEU A CD1 
8471  C CD2 . LEU A 1189 ? 0.3709 0.3379 0.3812 0.0014  -0.0154 -0.0261 1187 LEU A CD2 
8472  N N   . LEU A 1190 ? 0.3032 0.2874 0.3183 -0.0036 -0.0146 -0.0226 1188 LEU A N   
8473  C CA  . LEU A 1190 ? 0.3229 0.3119 0.3363 -0.0023 -0.0138 -0.0224 1188 LEU A CA  
8474  C C   . LEU A 1190 ? 0.3401 0.3298 0.3492 0.0015  -0.0140 -0.0243 1188 LEU A C   
8475  O O   . LEU A 1190 ? 0.2940 0.2830 0.3029 0.0026  -0.0157 -0.0271 1188 LEU A O   
8476  C CB  . LEU A 1190 ? 0.3182 0.3115 0.3357 -0.0044 -0.0154 -0.0235 1188 LEU A CB  
8477  C CG  . LEU A 1190 ? 0.3284 0.3221 0.3503 -0.0085 -0.0152 -0.0213 1188 LEU A CG  
8478  C CD1 . LEU A 1190 ? 0.3310 0.3305 0.3563 -0.0101 -0.0162 -0.0221 1188 LEU A CD1 
8479  C CD2 . LEU A 1190 ? 0.3258 0.3193 0.3461 -0.0088 -0.0127 -0.0179 1188 LEU A CD2 
8480  N N   . LEU A 1191 ? 0.2881 0.2792 0.2939 0.0035  -0.0122 -0.0227 1189 LEU A N   
8481  C CA  . LEU A 1191 ? 0.3093 0.3020 0.3111 0.0069  -0.0124 -0.0240 1189 LEU A CA  
8482  C C   . LEU A 1191 ? 0.3200 0.3175 0.3233 0.0072  -0.0140 -0.0258 1189 LEU A C   
8483  O O   . LEU A 1191 ? 0.2975 0.2981 0.3020 0.0067  -0.0135 -0.0246 1189 LEU A O   
8484  C CB  . LEU A 1191 ? 0.3025 0.2947 0.3007 0.0087  -0.0103 -0.0214 1189 LEU A CB  
8485  C CG  . LEU A 1191 ? 0.3418 0.3338 0.3353 0.0120  -0.0101 -0.0217 1189 LEU A CG  
8486  C CD1 . LEU A 1191 ? 0.3148 0.3049 0.3054 0.0129  -0.0079 -0.0188 1189 LEU A CD1 
8487  C CD2 . LEU A 1191 ? 0.2916 0.2877 0.2841 0.0138  -0.0114 -0.0232 1189 LEU A CD2 
8488  N N   . VAL A 1192 ? 0.3090 0.3074 0.3124 0.0080  -0.0160 -0.0288 1190 VAL A N   
8489  C CA  . VAL A 1192 ? 0.2958 0.2987 0.3010 0.0082  -0.0179 -0.0310 1190 VAL A CA  
8490  C C   . VAL A 1192 ? 0.3023 0.3076 0.3030 0.0118  -0.0181 -0.0317 1190 VAL A C   
8491  O O   . VAL A 1192 ? 0.3073 0.3108 0.3043 0.0140  -0.0179 -0.0322 1190 VAL A O   
8492  C CB  . VAL A 1192 ? 0.2972 0.2997 0.3058 0.0066  -0.0203 -0.0341 1190 VAL A CB  
8493  C CG1 . VAL A 1192 ? 0.3290 0.3367 0.3399 0.0064  -0.0223 -0.0363 1190 VAL A CG1 
8494  C CG2 . VAL A 1192 ? 0.3072 0.3067 0.3201 0.0029  -0.0202 -0.0329 1190 VAL A CG2 
8495  N N   . GLN A 1193 ? 0.2754 0.2851 0.2766 0.0126  -0.0186 -0.0318 1191 GLN A N   
8496  C CA  . GLN A 1193 ? 0.2346 0.2471 0.2323 0.0159  -0.0194 -0.0327 1191 GLN A CA  
8497  C C   . GLN A 1193 ? 0.2512 0.2683 0.2515 0.0157  -0.0218 -0.0356 1191 GLN A C   
8498  O O   . GLN A 1193 ? 0.2464 0.2660 0.2511 0.0134  -0.0223 -0.0358 1191 GLN A O   
8499  C CB  . GLN A 1193 ? 0.2413 0.2548 0.2368 0.0176  -0.0180 -0.0301 1191 GLN A CB  
8500  C CG  . GLN A 1193 ? 0.2515 0.2608 0.2440 0.0181  -0.0158 -0.0272 1191 GLN A CG  
8501  C CD  . GLN A 1193 ? 0.2810 0.2912 0.2713 0.0202  -0.0149 -0.0250 1191 GLN A CD  
8502  O OE1 . GLN A 1193 ? 0.3079 0.3192 0.2948 0.0229  -0.0156 -0.0249 1191 GLN A OE1 
8503  N NE2 . GLN A 1193 ? 0.2718 0.2815 0.2639 0.0189  -0.0136 -0.0232 1191 GLN A NE2 
8504  N N   . ALA A 1194 ? 0.2449 0.2637 0.2426 0.0180  -0.0234 -0.0378 1192 ALA A N   
8505  C CA  . ALA A 1194 ? 0.2733 0.2965 0.2735 0.0180  -0.0259 -0.0410 1192 ALA A CA  
8506  C C   . ALA A 1194 ? 0.2471 0.2740 0.2434 0.0215  -0.0269 -0.0414 1192 ALA A C   
8507  O O   . ALA A 1194 ? 0.2635 0.2891 0.2548 0.0241  -0.0260 -0.0401 1192 ALA A O   
8508  C CB  . ALA A 1194 ? 0.2437 0.2656 0.2455 0.0169  -0.0277 -0.0443 1192 ALA A CB  
8509  N N   . ALA A 1195 ? 0.2550 0.2868 0.2538 0.0216  -0.0286 -0.0430 1193 ALA A N   
8510  C CA  . ALA A 1195 ? 0.2692 0.3051 0.2650 0.0249  -0.0299 -0.0436 1193 ALA A CA  
8511  C C   . ALA A 1195 ? 0.3182 0.3591 0.3176 0.0242  -0.0326 -0.0471 1193 ALA A C   
8512  O O   . ALA A 1195 ? 0.3078 0.3498 0.3126 0.0212  -0.0329 -0.0479 1193 ALA A O   
8513  C CB  . ALA A 1195 ? 0.2831 0.3197 0.2774 0.0264  -0.0287 -0.0405 1193 ALA A CB  
8514  N N   . SER A 1196 ? 0.2549 0.2991 0.2515 0.0270  -0.0345 -0.0490 1194 SER A N   
8515  C CA  . SER A 1196 ? 0.2541 0.3038 0.2540 0.0268  -0.0371 -0.0522 1194 SER A CA  
8516  C C   . SER A 1196 ? 0.2613 0.3149 0.2626 0.0276  -0.0371 -0.0507 1194 SER A C   
8517  O O   . SER A 1196 ? 0.2534 0.3055 0.2520 0.0292  -0.0354 -0.0475 1194 SER A O   
8518  C CB  . SER A 1196 ? 0.3699 0.4223 0.3660 0.0297  -0.0393 -0.0548 1194 SER A CB  
8519  O OG  . SER A 1196 ? 0.3194 0.3730 0.3104 0.0332  -0.0389 -0.0525 1194 SER A OG  
8520  N N   . SER A 1197 ? 0.2498 0.3085 0.2555 0.0266  -0.0391 -0.0532 1195 SER A N   
8521  C CA  . SER A 1197 ? 0.2677 0.3311 0.2749 0.0279  -0.0394 -0.0523 1195 SER A CA  
8522  C C   . SER A 1197 ? 0.2920 0.3564 0.2937 0.0323  -0.0400 -0.0511 1195 SER A C   
8523  O O   . SER A 1197 ? 0.2735 0.3383 0.2743 0.0340  -0.0391 -0.0487 1195 SER A O   
8524  C CB  . SER A 1197 ? 0.2900 0.3594 0.3026 0.0263  -0.0418 -0.0556 1195 SER A CB  
8525  O OG  . SER A 1197 ? 0.3167 0.3850 0.3346 0.0219  -0.0414 -0.0564 1195 SER A OG  
8526  N N   . GLY A 1198 ? 0.3116 0.3765 0.3094 0.0343  -0.0415 -0.0528 1196 GLY A N   
8527  C CA  . GLY A 1198 ? 0.2869 0.3530 0.2792 0.0384  -0.0422 -0.0513 1196 GLY A CA  
8528  C C   . GLY A 1198 ? 0.3072 0.3680 0.2950 0.0396  -0.0397 -0.0471 1196 GLY A C   
8529  O O   . GLY A 1198 ? 0.2838 0.3449 0.2688 0.0423  -0.0397 -0.0446 1196 GLY A O   
8530  N N   . GLU A 1199 ? 0.2920 0.3478 0.2793 0.0376  -0.0378 -0.0464 1197 GLU A N   
8531  C CA  . GLU A 1199 ? 0.3158 0.3666 0.2995 0.0383  -0.0353 -0.0425 1197 GLU A CA  
8532  C C   . GLU A 1199 ? 0.3310 0.3807 0.3171 0.0378  -0.0339 -0.0400 1197 GLU A C   
8533  O O   . GLU A 1199 ? 0.2624 0.3099 0.2455 0.0397  -0.0329 -0.0368 1197 GLU A O   
8534  C CB  . GLU A 1199 ? 0.3137 0.3598 0.2969 0.0362  -0.0337 -0.0426 1197 GLU A CB  
8535  C CG  . GLU A 1199 ? 0.3922 0.4335 0.3712 0.0370  -0.0313 -0.0388 1197 GLU A CG  
8536  C CD  . GLU A 1199 ? 0.4600 0.5020 0.4328 0.0402  -0.0317 -0.0377 1197 GLU A CD  
8537  O OE1 . GLU A 1199 ? 0.4306 0.4768 0.4020 0.0418  -0.0340 -0.0401 1197 GLU A OE1 
8538  O OE2 . GLU A 1199 ? 0.5083 0.5466 0.4775 0.0409  -0.0299 -0.0344 1197 GLU A OE2 
8539  N N   . ILE A 1200 ? 0.2608 0.3122 0.2526 0.0351  -0.0338 -0.0414 1198 ILE A N   
8540  C CA  . ILE A 1200 ? 0.2756 0.3271 0.2699 0.0347  -0.0326 -0.0395 1198 ILE A CA  
8541  C C   . ILE A 1200 ? 0.3344 0.3895 0.3276 0.0381  -0.0341 -0.0390 1198 ILE A C   
8542  O O   . ILE A 1200 ? 0.2869 0.3404 0.2793 0.0396  -0.0332 -0.0365 1198 ILE A O   
8543  C CB  . ILE A 1200 ? 0.2578 0.3118 0.2586 0.0311  -0.0324 -0.0412 1198 ILE A CB  
8544  C CG1 . ILE A 1200 ? 0.2646 0.3140 0.2663 0.0278  -0.0308 -0.0410 1198 ILE A CG1 
8545  C CG2 . ILE A 1200 ? 0.2553 0.3111 0.2588 0.0312  -0.0314 -0.0398 1198 ILE A CG2 
8546  C CD1 . ILE A 1200 ? 0.2533 0.3049 0.2612 0.0239  -0.0307 -0.0422 1198 ILE A CD1 
8547  N N   . ALA A 1201 ? 0.2868 0.3467 0.2801 0.0396  -0.0367 -0.0414 1199 ALA A N   
8548  C CA  . ALA A 1201 ? 0.3129 0.3765 0.3054 0.0430  -0.0385 -0.0411 1199 ALA A CA  
8549  C C   . ALA A 1201 ? 0.2997 0.3600 0.2859 0.0462  -0.0384 -0.0380 1199 ALA A C   
8550  O O   . ALA A 1201 ? 0.3155 0.3758 0.3008 0.0488  -0.0389 -0.0360 1199 ALA A O   
8551  C CB  . ALA A 1201 ? 0.3060 0.3759 0.3002 0.0436  -0.0413 -0.0446 1199 ALA A CB  
8552  N N   . ARG A 1202 ? 0.2586 0.3163 0.2406 0.0462  -0.0380 -0.0376 1200 ARG A N   
8553  C CA  . ARG A 1202 ? 0.2913 0.3467 0.2672 0.0490  -0.0381 -0.0347 1200 ARG A CA  
8554  C C   . ARG A 1202 ? 0.3426 0.3918 0.3163 0.0487  -0.0356 -0.0309 1200 ARG A C   
8555  O O   . ARG A 1202 ? 0.3513 0.3987 0.3217 0.0511  -0.0357 -0.0277 1200 ARG A O   
8556  C CB  . ARG A 1202 ? 0.2754 0.3319 0.2475 0.0494  -0.0389 -0.0362 1200 ARG A CB  
8557  C CG  . ARG A 1202 ? 0.3014 0.3641 0.2740 0.0507  -0.0418 -0.0396 1200 ARG A CG  
8558  C CD  . ARG A 1202 ? 0.2986 0.3621 0.2664 0.0516  -0.0424 -0.0406 1200 ARG A CD  
8559  N NE  . ARG A 1202 ? 0.3096 0.3700 0.2784 0.0489  -0.0408 -0.0421 1200 ARG A NE  
8560  C CZ  . ARG A 1202 ? 0.3471 0.4093 0.3197 0.0467  -0.0417 -0.0462 1200 ARG A CZ  
8561  N NH1 . ARG A 1202 ? 0.3087 0.3762 0.2842 0.0470  -0.0443 -0.0495 1200 ARG A NH1 
8562  N NH2 . ARG A 1202 ? 0.3639 0.4224 0.3377 0.0442  -0.0402 -0.0471 1200 ARG A NH2 
8563  N N   . ASN A 1203 ? 0.2847 0.3305 0.2603 0.0457  -0.0334 -0.0311 1201 ASN A N   
8564  C CA  . ASN A 1203 ? 0.3204 0.3605 0.2934 0.0452  -0.0310 -0.0277 1201 ASN A CA  
8565  C C   . ASN A 1203 ? 0.3530 0.3907 0.3298 0.0436  -0.0293 -0.0267 1201 ASN A C   
8566  O O   . ASN A 1203 ? 0.3216 0.3595 0.3024 0.0407  -0.0284 -0.0285 1201 ASN A O   
8567  C CB  . ASN A 1203 ? 0.3574 0.3953 0.3288 0.0434  -0.0297 -0.0285 1201 ASN A CB  
8568  C CG  . ASN A 1203 ? 0.3805 0.4129 0.3493 0.0428  -0.0273 -0.0252 1201 ASN A CG  
8569  O OD1 . ASN A 1203 ? 0.3756 0.4055 0.3434 0.0439  -0.0266 -0.0221 1201 ASN A OD1 
8570  N ND2 . ASN A 1203 ? 0.3593 0.3896 0.3271 0.0413  -0.0261 -0.0259 1201 ASN A ND2 
8571  N N   . PRO A 1204 ? 0.3733 0.4088 0.3491 0.0453  -0.0290 -0.0239 1202 PRO A N   
8572  C CA  . PRO A 1204 ? 0.3524 0.3859 0.3316 0.0440  -0.0274 -0.0232 1202 PRO A CA  
8573  C C   . PRO A 1204 ? 0.3546 0.3838 0.3340 0.0411  -0.0249 -0.0224 1202 PRO A C   
8574  O O   . PRO A 1204 ? 0.3411 0.3699 0.3241 0.0391  -0.0236 -0.0227 1202 PRO A O   
8575  C CB  . PRO A 1204 ? 0.4021 0.4332 0.3793 0.0468  -0.0278 -0.0202 1202 PRO A CB  
8576  C CG  . PRO A 1204 ? 0.4472 0.4769 0.4189 0.0486  -0.0286 -0.0182 1202 PRO A CG  
8577  C CD  . PRO A 1204 ? 0.3928 0.4271 0.3642 0.0485  -0.0300 -0.0210 1202 PRO A CD  
8578  N N   . ASP A 1205 ? 0.3794 0.4060 0.3551 0.0408  -0.0242 -0.0215 1203 ASP A N   
8579  C CA  . ASP A 1205 ? 0.3704 0.3931 0.3461 0.0382  -0.0219 -0.0208 1203 ASP A CA  
8580  C C   . ASP A 1205 ? 0.3465 0.3707 0.3237 0.0361  -0.0221 -0.0238 1203 ASP A C   
8581  O O   . ASP A 1205 ? 0.3379 0.3591 0.3139 0.0348  -0.0208 -0.0234 1203 ASP A O   
8582  C CB  . ASP A 1205 ? 0.4102 0.4289 0.3811 0.0393  -0.0208 -0.0177 1203 ASP A CB  
8583  C CG  . ASP A 1205 ? 0.4363 0.4527 0.4059 0.0413  -0.0208 -0.0146 1203 ASP A CG  
8584  O OD1 . ASP A 1205 ? 0.4747 0.4907 0.4476 0.0409  -0.0205 -0.0146 1203 ASP A OD1 
8585  O OD2 . ASP A 1205 ? 0.5446 0.5599 0.5102 0.0432  -0.0213 -0.0122 1203 ASP A OD2 
8586  N N   . ALA A 1206 ? 0.3114 0.3403 0.2914 0.0359  -0.0240 -0.0267 1204 ALA A N   
8587  C CA  . ALA A 1206 ? 0.2859 0.3159 0.2680 0.0338  -0.0245 -0.0297 1204 ALA A CA  
8588  C C   . ALA A 1206 ? 0.3353 0.3618 0.3200 0.0306  -0.0225 -0.0293 1204 ALA A C   
8589  O O   . ALA A 1206 ? 0.3312 0.3557 0.3155 0.0292  -0.0222 -0.0303 1204 ALA A O   
8590  C CB  . ALA A 1206 ? 0.3140 0.3495 0.3001 0.0334  -0.0265 -0.0327 1204 ALA A CB  
8591  N N   . TYR A 1207 ? 0.2594 0.2852 0.2467 0.0295  -0.0213 -0.0279 1205 TYR A N   
8592  C CA  . TYR A 1207 ? 0.2594 0.2817 0.2486 0.0267  -0.0192 -0.0267 1205 TYR A CA  
8593  C C   . TYR A 1207 ? 0.3092 0.3276 0.2955 0.0279  -0.0174 -0.0235 1205 TYR A C   
8594  O O   . TYR A 1207 ? 0.3643 0.3836 0.3505 0.0295  -0.0175 -0.0223 1205 TYR A O   
8595  C CB  . TYR A 1207 ? 0.2635 0.2887 0.2580 0.0244  -0.0191 -0.0276 1205 TYR A CB  
8596  C CG  . TYR A 1207 ? 0.2477 0.2766 0.2456 0.0228  -0.0209 -0.0306 1205 TYR A CG  
8597  C CD1 . TYR A 1207 ? 0.2899 0.3168 0.2882 0.0210  -0.0213 -0.0320 1205 TYR A CD1 
8598  C CD2 . TYR A 1207 ? 0.2689 0.3034 0.2697 0.0231  -0.0224 -0.0322 1205 TYR A CD2 
8599  C CE1 . TYR A 1207 ? 0.2424 0.2723 0.2441 0.0194  -0.0231 -0.0349 1205 TYR A CE1 
8600  C CE2 . TYR A 1207 ? 0.2735 0.3115 0.2778 0.0214  -0.0241 -0.0350 1205 TYR A CE2 
8601  C CZ  . TYR A 1207 ? 0.2695 0.3049 0.2742 0.0195  -0.0245 -0.0363 1205 TYR A CZ  
8602  O OH  . TYR A 1207 ? 0.2655 0.3040 0.2738 0.0177  -0.0265 -0.0391 1205 TYR A OH  
8603  N N   . CYS A 1208 ? 0.2588 0.2730 0.2430 0.0271  -0.0160 -0.0223 1206 CYS A N   
8604  C CA  . CYS A 1208 ? 0.2834 0.2938 0.2649 0.0281  -0.0144 -0.0192 1206 CYS A CA  
8605  C C   . CYS A 1208 ? 0.2985 0.3071 0.2828 0.0261  -0.0127 -0.0181 1206 CYS A C   
8606  O O   . CYS A 1208 ? 0.2644 0.2722 0.2511 0.0234  -0.0120 -0.0188 1206 CYS A O   
8607  C CB  . CYS A 1208 ? 0.2985 0.3058 0.2763 0.0283  -0.0136 -0.0184 1206 CYS A CB  
8608  S SG  . CYS A 1208 ? 0.3493 0.3519 0.3240 0.0291  -0.0116 -0.0146 1206 CYS A SG  
8609  N N   . LEU A 1209 ? 0.2550 0.2631 0.2391 0.0273  -0.0123 -0.0164 1207 LEU A N   
8610  C CA  . LEU A 1209 ? 0.2478 0.2550 0.2345 0.0257  -0.0108 -0.0156 1207 LEU A CA  
8611  C C   . LEU A 1209 ? 0.2299 0.2323 0.2151 0.0244  -0.0089 -0.0137 1207 LEU A C   
8612  O O   . LEU A 1209 ? 0.2374 0.2392 0.2249 0.0226  -0.0076 -0.0132 1207 LEU A O   
8613  C CB  . LEU A 1209 ? 0.2347 0.2431 0.2219 0.0277  -0.0112 -0.0150 1207 LEU A CB  
8614  C CG  . LEU A 1209 ? 0.2277 0.2413 0.2168 0.0292  -0.0131 -0.0169 1207 LEU A CG  
8615  C CD1 . LEU A 1209 ? 0.2527 0.2672 0.2429 0.0312  -0.0134 -0.0164 1207 LEU A CD1 
8616  C CD2 . LEU A 1209 ? 0.2468 0.2645 0.2398 0.0268  -0.0134 -0.0192 1207 LEU A CD2 
8617  N N   . ASN A 1210 ? 0.2769 0.2765 0.2585 0.0253  -0.0086 -0.0126 1208 ASN A N   
8618  C CA  . ASN A 1210 ? 0.3139 0.3094 0.2944 0.0240  -0.0068 -0.0110 1208 ASN A CA  
8619  C C   . ASN A 1210 ? 0.2736 0.2689 0.2571 0.0211  -0.0062 -0.0122 1208 ASN A C   
8620  O O   . ASN A 1210 ? 0.2754 0.2682 0.2596 0.0196  -0.0047 -0.0109 1208 ASN A O   
8621  C CB  . ASN A 1210 ? 0.2935 0.2871 0.2700 0.0252  -0.0067 -0.0101 1208 ASN A CB  
8622  C CG  . ASN A 1210 ? 0.3653 0.3584 0.3386 0.0278  -0.0072 -0.0082 1208 ASN A CG  
8623  O OD1 . ASN A 1210 ? 0.4390 0.4332 0.4131 0.0291  -0.0081 -0.0079 1208 ASN A OD1 
8624  N ND2 . ASN A 1210 ? 0.4420 0.4337 0.4118 0.0286  -0.0068 -0.0069 1208 ASN A ND2 
8625  N N   . TRP A 1211 ? 0.2603 0.2581 0.2454 0.0203  -0.0075 -0.0145 1209 TRP A N   
8626  C CA  . TRP A 1211 ? 0.2751 0.2722 0.2629 0.0176  -0.0073 -0.0155 1209 TRP A CA  
8627  C C   . TRP A 1211 ? 0.2757 0.2754 0.2678 0.0154  -0.0073 -0.0160 1209 TRP A C   
8628  O O   . TRP A 1211 ? 0.2927 0.2921 0.2874 0.0129  -0.0074 -0.0166 1209 TRP A O   
8629  C CB  . TRP A 1211 ? 0.2500 0.2480 0.2375 0.0178  -0.0088 -0.0178 1209 TRP A CB  
8630  C CG  . TRP A 1211 ? 0.2741 0.2714 0.2571 0.0205  -0.0090 -0.0176 1209 TRP A CG  
8631  C CD1 . TRP A 1211 ? 0.3113 0.3114 0.2925 0.0224  -0.0106 -0.0191 1209 TRP A CD1 
8632  C CD2 . TRP A 1211 ? 0.2750 0.2691 0.2546 0.0214  -0.0075 -0.0155 1209 TRP A CD2 
8633  N NE1 . TRP A 1211 ? 0.3230 0.3220 0.2999 0.0245  -0.0102 -0.0179 1209 TRP A NE1 
8634  C CE2 . TRP A 1211 ? 0.2851 0.2804 0.2610 0.0238  -0.0083 -0.0156 1209 TRP A CE2 
8635  C CE3 . TRP A 1211 ? 0.2937 0.2843 0.2732 0.0203  -0.0057 -0.0134 1209 TRP A CE3 
8636  C CZ2 . TRP A 1211 ? 0.3093 0.3026 0.2815 0.0250  -0.0071 -0.0137 1209 TRP A CZ2 
8637  C CZ3 . TRP A 1211 ? 0.2701 0.2586 0.2461 0.0216  -0.0046 -0.0116 1209 TRP A CZ3 
8638  C CH2 . TRP A 1211 ? 0.2876 0.2776 0.2601 0.0238  -0.0053 -0.0117 1209 TRP A CH2 
8639  N N   . LEU A 1212 ? 0.2312 0.2335 0.2241 0.0163  -0.0073 -0.0156 1210 LEU A N   
8640  C CA  . LEU A 1212 ? 0.2332 0.2390 0.2299 0.0144  -0.0071 -0.0160 1210 LEU A CA  
8641  C C   . LEU A 1212 ? 0.2356 0.2404 0.2326 0.0140  -0.0054 -0.0141 1210 LEU A C   
8642  O O   . LEU A 1212 ? 0.2291 0.2373 0.2291 0.0127  -0.0051 -0.0143 1210 LEU A O   
8643  C CB  . LEU A 1212 ? 0.2193 0.2302 0.2174 0.0159  -0.0086 -0.0176 1210 LEU A CB  
8644  C CG  . LEU A 1212 ? 0.2401 0.2532 0.2392 0.0155  -0.0104 -0.0198 1210 LEU A CG  
8645  C CD1 . LEU A 1212 ? 0.2604 0.2780 0.2598 0.0178  -0.0121 -0.0213 1210 LEU A CD1 
8646  C CD2 . LEU A 1212 ? 0.2497 0.2642 0.2530 0.0119  -0.0105 -0.0206 1210 LEU A CD2 
8647  N N   . VAL A 1213 ? 0.2166 0.2172 0.2106 0.0152  -0.0044 -0.0125 1211 VAL A N   
8648  C CA  . VAL A 1213 ? 0.2230 0.2221 0.2173 0.0145  -0.0028 -0.0108 1211 VAL A CA  
8649  C C   . VAL A 1213 ? 0.2656 0.2606 0.2591 0.0127  -0.0017 -0.0097 1211 VAL A C   
8650  O O   . VAL A 1213 ? 0.2527 0.2457 0.2450 0.0126  -0.0021 -0.0101 1211 VAL A O   
8651  C CB  . VAL A 1213 ? 0.2623 0.2597 0.2542 0.0172  -0.0025 -0.0098 1211 VAL A CB  
8652  C CG1 . VAL A 1213 ? 0.2340 0.2355 0.2271 0.0191  -0.0037 -0.0110 1211 VAL A CG1 
8653  C CG2 . VAL A 1213 ? 0.2240 0.2176 0.2122 0.0188  -0.0027 -0.0088 1211 VAL A CG2 
8654  N N   . GLU A 1214 ? 0.2456 0.2397 0.2400 0.0114  -0.0003 -0.0084 1212 GLU A N   
8655  C CA  . GLU A 1214 ? 0.3233 0.3137 0.3172 0.0098  0.0008  -0.0071 1212 GLU A CA  
8656  C C   . GLU A 1214 ? 0.2380 0.2253 0.2296 0.0110  0.0019  -0.0055 1212 GLU A C   
8657  O O   . GLU A 1214 ? 0.2289 0.2174 0.2209 0.0116  0.0024  -0.0052 1212 GLU A O   
8658  C CB  . GLU A 1214 ? 0.3006 0.2929 0.2977 0.0068  0.0013  -0.0067 1212 GLU A CB  
8659  C CG  . GLU A 1214 ? 0.3953 0.3839 0.3923 0.0050  0.0020  -0.0055 1212 GLU A CG  
8660  C CD  . GLU A 1214 ? 0.5143 0.5051 0.5145 0.0019  0.0023  -0.0048 1212 GLU A CD  
8661  O OE1 . GLU A 1214 ? 0.5344 0.5276 0.5371 0.0003  0.0012  -0.0057 1212 GLU A OE1 
8662  O OE2 . GLU A 1214 ? 0.5819 0.5724 0.5822 0.0010  0.0035  -0.0033 1212 GLU A OE2 
8663  N N   . GLU A 1215 ? 0.2351 0.2186 0.2244 0.0114  0.0023  -0.0047 1213 GLU A N   
8664  C CA  . GLU A 1215 ? 0.2158 0.1963 0.2032 0.0122  0.0034  -0.0030 1213 GLU A CA  
8665  C C   . GLU A 1215 ? 0.2422 0.2217 0.2310 0.0102  0.0046  -0.0020 1213 GLU A C   
8666  O O   . GLU A 1215 ? 0.2183 0.1974 0.2084 0.0083  0.0047  -0.0021 1213 GLU A O   
8667  C CB  . GLU A 1215 ? 0.2330 0.2105 0.2176 0.0133  0.0035  -0.0024 1213 GLU A CB  
8668  C CG  . GLU A 1215 ? 0.2421 0.2208 0.2249 0.0153  0.0023  -0.0032 1213 GLU A CG  
8669  C CD  . GLU A 1215 ? 0.2366 0.2133 0.2168 0.0159  0.0025  -0.0029 1213 GLU A CD  
8670  O OE1 . GLU A 1215 ? 0.2713 0.2483 0.2521 0.0152  0.0020  -0.0043 1213 GLU A OE1 
8671  O OE2 . GLU A 1215 ? 0.2624 0.2373 0.2402 0.0172  0.0031  -0.0013 1213 GLU A OE2 
8672  N N   . VAL A 1216 ? 0.2112 0.1901 0.1998 0.0106  0.0054  -0.0011 1214 VAL A N   
8673  C CA  . VAL A 1216 ? 0.2077 0.1855 0.1971 0.0089  0.0066  0.0000  1214 VAL A CA  
8674  C C   . VAL A 1216 ? 0.2181 0.1927 0.2056 0.0100  0.0073  0.0012  1214 VAL A C   
8675  O O   . VAL A 1216 ? 0.2236 0.1979 0.2102 0.0117  0.0071  0.0013  1214 VAL A O   
8676  C CB  . VAL A 1216 ? 0.2269 0.2085 0.2186 0.0078  0.0068  -0.0005 1214 VAL A CB  
8677  C CG1 . VAL A 1216 ? 0.2054 0.1860 0.1975 0.0064  0.0080  0.0008  1214 VAL A CG1 
8678  C CG2 . VAL A 1216 ? 0.2662 0.2512 0.2602 0.0061  0.0062  -0.0013 1214 VAL A CG2 
8679  N N   . SER A 1217 ? 0.2136 0.1856 0.2007 0.0089  0.0081  0.0023  1215 SER A N   
8680  C CA  . SER A 1217 ? 0.2075 0.1766 0.1931 0.0094  0.0090  0.0036  1215 SER A CA  
8681  C C   . SER A 1217 ? 0.2171 0.1865 0.2041 0.0079  0.0098  0.0041  1215 SER A C   
8682  O O   . SER A 1217 ? 0.2339 0.2044 0.2223 0.0061  0.0099  0.0042  1215 SER A O   
8683  C CB  . SER A 1217 ? 0.2197 0.1862 0.2038 0.0095  0.0093  0.0043  1215 SER A CB  
8684  O OG  . SER A 1217 ? 0.2818 0.2459 0.2651 0.0093  0.0102  0.0056  1215 SER A OG  
8685  N N   . ALA A 1218 ? 0.2085 0.1772 0.1953 0.0086  0.0102  0.0046  1216 ALA A N   
8686  C CA  . ALA A 1218 ? 0.2211 0.1903 0.2089 0.0074  0.0109  0.0049  1216 ALA A CA  
8687  C C   . ALA A 1218 ? 0.2598 0.2258 0.2464 0.0079  0.0114  0.0060  1216 ALA A C   
8688  O O   . ALA A 1218 ? 0.2565 0.2210 0.2423 0.0095  0.0111  0.0061  1216 ALA A O   
8689  C CB  . ALA A 1218 ? 0.2230 0.1957 0.2121 0.0077  0.0107  0.0038  1216 ALA A CB  
8690  N N   . SER A 1219 ? 0.2203 0.1851 0.2071 0.0066  0.0122  0.0069  1217 SER A N   
8691  C CA  . SER A 1219 ? 0.2041 0.1662 0.1901 0.0068  0.0127  0.0079  1217 SER A CA  
8692  C C   . SER A 1219 ? 0.2129 0.1761 0.2001 0.0059  0.0132  0.0079  1217 SER A C   
8693  O O   . SER A 1219 ? 0.2532 0.2175 0.2411 0.0044  0.0135  0.0082  1217 SER A O   
8694  C CB  . SER A 1219 ? 0.2296 0.1896 0.2148 0.0063  0.0132  0.0089  1217 SER A CB  
8695  O OG  . SER A 1219 ? 0.2372 0.1949 0.2218 0.0065  0.0138  0.0100  1217 SER A OG  
8696  N N   . ILE A 1220 ? 0.2034 0.1662 0.1907 0.0067  0.0130  0.0075  1218 ILE A N   
8697  C CA  . ILE A 1220 ? 0.2205 0.1848 0.2088 0.0061  0.0133  0.0070  1218 ILE A CA  
8698  C C   . ILE A 1220 ? 0.2036 0.1649 0.1916 0.0060  0.0136  0.0079  1218 ILE A C   
8699  O O   . ILE A 1220 ? 0.2217 0.1805 0.2094 0.0071  0.0132  0.0082  1218 ILE A O   
8700  C CB  . ILE A 1220 ? 0.2518 0.2185 0.2410 0.0073  0.0126  0.0053  1218 ILE A CB  
8701  C CG1 . ILE A 1220 ? 0.3305 0.3007 0.3203 0.0074  0.0123  0.0044  1218 ILE A CG1 
8702  C CG2 . ILE A 1220 ? 0.2951 0.2639 0.2852 0.0068  0.0129  0.0046  1218 ILE A CG2 
8703  C CD1 . ILE A 1220 ? 0.3822 0.3520 0.3717 0.0092  0.0114  0.0036  1218 ILE A CD1 
8704  N N   . ASN A 1221 ? 0.2295 0.1913 0.2179 0.0047  0.0142  0.0086  1219 ASN A N   
8705  C CA  . ASN A 1221 ? 0.2478 0.2075 0.2362 0.0044  0.0145  0.0092  1219 ASN A CA  
8706  C C   . ASN A 1221 ? 0.2570 0.2178 0.2464 0.0050  0.0140  0.0079  1219 ASN A C   
8707  O O   . ASN A 1221 ? 0.2824 0.2463 0.2724 0.0044  0.0141  0.0070  1219 ASN A O   
8708  C CB  . ASN A 1221 ? 0.2524 0.2125 0.2410 0.0029  0.0151  0.0102  1219 ASN A CB  
8709  C CG  . ASN A 1221 ? 0.2838 0.2423 0.2727 0.0026  0.0154  0.0108  1219 ASN A CG  
8710  O OD1 . ASN A 1221 ? 0.2421 0.1988 0.2311 0.0033  0.0151  0.0107  1219 ASN A OD1 
8711  N ND2 . ASN A 1221 ? 0.3065 0.2656 0.2958 0.0014  0.0157  0.0116  1219 ASN A ND2 
8712  N N   . THR A 1222 ? 0.2721 0.2303 0.2615 0.0061  0.0135  0.0076  1220 THR A N   
8713  C CA  . THR A 1222 ? 0.2921 0.2508 0.2827 0.0069  0.0128  0.0060  1220 THR A CA  
8714  C C   . THR A 1222 ? 0.3100 0.2669 0.3012 0.0062  0.0128  0.0064  1220 THR A C   
8715  O O   . THR A 1222 ? 0.3535 0.3100 0.3458 0.0069  0.0120  0.0050  1220 THR A O   
8716  C CB  . THR A 1222 ? 0.3015 0.2582 0.2923 0.0086  0.0117  0.0054  1220 THR A CB  
8717  O OG1 . THR A 1222 ? 0.2785 0.2312 0.2686 0.0086  0.0117  0.0072  1220 THR A OG1 
8718  C CG2 . THR A 1222 ? 0.2798 0.2388 0.2701 0.0094  0.0115  0.0047  1220 THR A CG2 
8719  N N   . ALA A 1223 ? 0.2500 0.2060 0.2408 0.0050  0.0136  0.0081  1221 ALA A N   
8720  C CA  . ALA A 1223 ? 0.3787 0.3341 0.3702 0.0041  0.0138  0.0083  1221 ALA A CA  
8721  C C   . ALA A 1223 ? 0.4563 0.4151 0.4479 0.0032  0.0142  0.0079  1221 ALA A C   
8722  O O   . ALA A 1223 ? 0.5611 0.5201 0.5533 0.0025  0.0143  0.0079  1221 ALA A O   
8723  C CB  . ALA A 1223 ? 0.3407 0.2935 0.3318 0.0034  0.0144  0.0104  1221 ALA A CB  
8724  N N   . ALA A 1224 ? 0.4970 0.4588 0.4881 0.0031  0.0144  0.0075  1222 ALA A N   
8725  C CA  . ALA A 1224 ? 0.4939 0.4588 0.4849 0.0019  0.0148  0.0080  1222 ALA A CA  
8726  C C   . ALA A 1224 ? 0.5760 0.5437 0.5675 0.0017  0.0146  0.0067  1222 ALA A C   
8727  O O   . ALA A 1224 ? 0.5908 0.5605 0.5823 0.0005  0.0149  0.0076  1222 ALA A O   
8728  C CB  . ALA A 1224 ? 0.4063 0.3737 0.3969 0.0017  0.0149  0.0079  1222 ALA A CB  
8729  N N   . ALA A 1225 ? 0.5686 0.5368 0.5608 0.0029  0.0139  0.0046  1223 ALA A N   
8730  C CA  . ALA A 1225 ? 0.5976 0.5686 0.5904 0.0029  0.0136  0.0030  1223 ALA A CA  
8731  C C   . ALA A 1225 ? 0.6613 0.6296 0.6547 0.0025  0.0133  0.0034  1223 ALA A C   
8732  O O   . ALA A 1225 ? 0.7019 0.6722 0.6960 0.0026  0.0129  0.0018  1223 ALA A O   
8733  C CB  . ALA A 1225 ? 0.5297 0.5025 0.5233 0.0046  0.0127  0.0002  1223 ALA A CB  
8734  N N   . GLY A 1226 ? 0.6201 0.5844 0.6135 0.0021  0.0136  0.0052  1224 GLY A N   
8735  C CA  . GLY A 1226 ? 0.6457 0.6079 0.6398 0.0014  0.0136  0.0058  1224 GLY A CA  
8736  C C   . GLY A 1226 ? 0.6503 0.6083 0.6454 0.0020  0.0130  0.0059  1224 GLY A C   
8737  O O   . GLY A 1226 ? 0.6867 0.6426 0.6824 0.0012  0.0132  0.0071  1224 GLY A O   
8738  N N   . GLY A 1227 ? 0.6255 0.5823 0.6208 0.0032  0.0123  0.0048  1225 GLY A N   
8739  C CA  . GLY A 1227 ? 0.6353 0.5879 0.6315 0.0036  0.0116  0.0051  1225 GLY A CA  
8740  C C   . GLY A 1227 ? 0.6371 0.5884 0.6327 0.0049  0.0113  0.0052  1225 GLY A C   
8741  O O   . GLY A 1227 ? 0.6792 0.6330 0.6738 0.0054  0.0116  0.0047  1225 GLY A O   
8742  N N   . ASN A 1228 ? 0.6267 0.5741 0.6230 0.0052  0.0106  0.0061  1226 ASN A N   
8743  C CA  . ASN A 1228 ? 0.6877 0.6332 0.6833 0.0064  0.0101  0.0065  1226 ASN A CA  
8744  C C   . ASN A 1228 ? 0.7321 0.6759 0.7295 0.0078  0.0083  0.0045  1226 ASN A C   
8745  O O   . ASN A 1228 ? 0.7038 0.6443 0.7027 0.0075  0.0074  0.0048  1226 ASN A O   
8746  C CB  . ASN A 1228 ? 0.6607 0.6032 0.6555 0.0057  0.0106  0.0094  1226 ASN A CB  
8747  C CG  . ASN A 1228 ? 0.6992 0.6404 0.6931 0.0069  0.0102  0.0102  1226 ASN A CG  
8748  O OD1 . ASN A 1228 ? 0.7100 0.6514 0.7044 0.0084  0.0091  0.0085  1226 ASN A OD1 
8749  N ND2 . ASN A 1228 ? 0.6591 0.5993 0.6516 0.0064  0.0110  0.0126  1226 ASN A ND2 
8750  N N   . ALA A 1229 ? 0.7173 0.6634 0.7147 0.0094  0.0077  0.0023  1227 ALA A N   
8751  C CA  . ALA A 1229 ? 0.7103 0.6551 0.7095 0.0111  0.0059  -0.0001 1227 ALA A CA  
8752  C C   . ALA A 1229 ? 0.7905 0.7299 0.7903 0.0116  0.0046  0.0015  1227 ALA A C   
8753  O O   . ALA A 1229 ? 0.7982 0.7342 0.7999 0.0117  0.0032  0.0011  1227 ALA A O   
8754  C CB  . ALA A 1229 ? 0.6430 0.5918 0.6418 0.0127  0.0056  -0.0025 1227 ALA A CB  
8755  N N   . SER A 1230 ? 0.7511 0.6898 0.7494 0.0120  0.0050  0.0035  1228 SER A N   
8756  C CA  . SER A 1230 ? 0.7041 0.6381 0.7027 0.0126  0.0038  0.0053  1228 SER A CA  
8757  C C   . SER A 1230 ? 0.7850 0.7154 0.7840 0.0107  0.0039  0.0081  1228 SER A C   
8758  O O   . SER A 1230 ? 0.8018 0.7279 0.8021 0.0109  0.0025  0.0093  1228 SER A O   
8759  C CB  . SER A 1230 ? 0.7160 0.6508 0.7124 0.0132  0.0043  0.0070  1228 SER A CB  
8760  N N   . LEU A 1231 ? 0.7616 0.6938 0.7600 0.0089  0.0056  0.0091  1229 LEU A N   
8761  C CA  . LEU A 1231 ? 0.7375 0.6671 0.7366 0.0071  0.0059  0.0115  1229 LEU A CA  
8762  C C   . LEU A 1231 ? 0.7747 0.7042 0.7761 0.0064  0.0052  0.0095  1229 LEU A C   
8763  O O   . LEU A 1231 ? 0.8699 0.7958 0.8735 0.0060  0.0039  0.0100  1229 LEU A O   
8764  C CB  . LEU A 1231 ? 0.6773 0.6091 0.6744 0.0057  0.0080  0.0137  1229 LEU A CB  
8765  C CG  . LEU A 1231 ? 0.6131 0.5441 0.6082 0.0056  0.0087  0.0166  1229 LEU A CG  
8766  C CD1 . LEU A 1231 ? 0.5734 0.5064 0.5674 0.0040  0.0106  0.0183  1229 LEU A CD1 
8767  C CD2 . LEU A 1231 ? 0.6328 0.5595 0.6289 0.0054  0.0074  0.0188  1229 LEU A CD2 
8768  N N   . ALA B 16   ? 0.6386 0.5439 0.6162 0.0847  -0.0410 -0.0469 14   ALA B N   
8769  C CA  . ALA B 16   ? 0.6334 0.5437 0.6134 0.0773  -0.0394 -0.0448 14   ALA B CA  
8770  C C   . ALA B 16   ? 0.6474 0.5465 0.6184 0.0720  -0.0419 -0.0439 14   ALA B C   
8771  O O   . ALA B 16   ? 0.6735 0.5641 0.6373 0.0732  -0.0426 -0.0457 14   ALA B O   
8772  C CB  . ALA B 16   ? 0.5812 0.5022 0.5665 0.0772  -0.0345 -0.0456 14   ALA B CB  
8773  N N   . PRO B 17   ? 0.6730 0.5721 0.6444 0.0660  -0.0432 -0.0411 15   PRO B N   
8774  C CA  . PRO B 17   ? 0.6214 0.5116 0.5852 0.0602  -0.0453 -0.0399 15   PRO B CA  
8775  C C   . PRO B 17   ? 0.6176 0.5099 0.5802 0.0580  -0.0424 -0.0409 15   PRO B C   
8776  O O   . PRO B 17   ? 0.5964 0.4996 0.5656 0.0580  -0.0385 -0.0411 15   PRO B O   
8777  C CB  . PRO B 17   ? 0.6218 0.5161 0.5887 0.0546  -0.0458 -0.0368 15   PRO B CB  
8778  C CG  . PRO B 17   ? 0.6587 0.5597 0.6325 0.0582  -0.0458 -0.0365 15   PRO B CG  
8779  C CD  . PRO B 17   ? 0.6098 0.5176 0.5885 0.0641  -0.0429 -0.0390 15   PRO B CD  
8780  N N   . ALA B 18   ? 0.5582 0.4397 0.5120 0.0562  -0.0446 -0.0414 16   ALA B N   
8781  C CA  . ALA B 18   ? 0.5109 0.3934 0.4626 0.0536  -0.0425 -0.0421 16   ALA B CA  
8782  C C   . ALA B 18   ? 0.4932 0.3845 0.4499 0.0474  -0.0403 -0.0396 16   ALA B C   
8783  O O   . ALA B 18   ? 0.4383 0.3288 0.3950 0.0431  -0.0421 -0.0371 16   ALA B O   
8784  C CB  . ALA B 18   ? 0.5264 0.3949 0.4675 0.0517  -0.0459 -0.0427 16   ALA B CB  
8785  N N   . PRO B 19   ? 0.4011 0.3009 0.3618 0.0469  -0.0365 -0.0402 17   PRO B N   
8786  C CA  . PRO B 19   ? 0.4113 0.3194 0.3767 0.0414  -0.0345 -0.0380 17   PRO B CA  
8787  C C   . PRO B 19   ? 0.3805 0.2821 0.3403 0.0352  -0.0371 -0.0359 17   PRO B C   
8788  O O   . PRO B 19   ? 0.3839 0.2768 0.3363 0.0342  -0.0390 -0.0367 17   PRO B O   
8789  C CB  . PRO B 19   ? 0.3600 0.2750 0.3281 0.0425  -0.0306 -0.0393 17   PRO B CB  
8790  C CG  . PRO B 19   ? 0.4379 0.3522 0.4059 0.0493  -0.0297 -0.0421 17   PRO B CG  
8791  C CD  . PRO B 19   ? 0.4342 0.3361 0.3949 0.0515  -0.0339 -0.0430 17   PRO B CD  
8792  N N   . PHE B 20   ? 0.3832 0.2890 0.3462 0.0311  -0.0373 -0.0333 18   PHE B N   
8793  C CA  . PHE B 20   ? 0.3843 0.2872 0.3438 0.0247  -0.0390 -0.0309 18   PHE B CA  
8794  C C   . PHE B 20   ? 0.4136 0.3039 0.3647 0.0233  -0.0435 -0.0303 18   PHE B C   
8795  O O   . PHE B 20   ? 0.3768 0.2637 0.3241 0.0178  -0.0451 -0.0283 18   PHE B O   
8796  C CB  . PHE B 20   ? 0.3468 0.2525 0.3055 0.0216  -0.0371 -0.0309 18   PHE B CB  
8797  C CG  . PHE B 20   ? 0.3169 0.2344 0.2832 0.0223  -0.0329 -0.0311 18   PHE B CG  
8798  C CD1 . PHE B 20   ? 0.3107 0.2363 0.2827 0.0195  -0.0314 -0.0290 18   PHE B CD1 
8799  C CD2 . PHE B 20   ? 0.3058 0.2259 0.2733 0.0259  -0.0304 -0.0333 18   PHE B CD2 
8800  C CE1 . PHE B 20   ? 0.3362 0.2719 0.3148 0.0201  -0.0277 -0.0292 18   PHE B CE1 
8801  C CE2 . PHE B 20   ? 0.3236 0.2542 0.2979 0.0263  -0.0267 -0.0333 18   PHE B CE2 
8802  C CZ  . PHE B 20   ? 0.3368 0.2750 0.3167 0.0234  -0.0254 -0.0313 18   PHE B CZ  
8803  N N   . ALA B 21   ? 0.4094 0.2927 0.3577 0.0282  -0.0455 -0.0319 19   ALA B N   
8804  C CA  . ALA B 21   ? 0.4617 0.3320 0.4017 0.0271  -0.0501 -0.0314 19   ALA B CA  
8805  C C   . ALA B 21   ? 0.5041 0.3734 0.4435 0.0221  -0.0522 -0.0280 19   ALA B C   
8806  O O   . ALA B 21   ? 0.5408 0.4012 0.4734 0.0181  -0.0555 -0.0265 19   ALA B O   
8807  C CB  . ALA B 21   ? 0.5136 0.3775 0.4514 0.0340  -0.0517 -0.0337 19   ALA B CB  
8808  N N   . ASP B 22   ? 0.4353 0.3138 0.3816 0.0221  -0.0504 -0.0268 20   ASP B N   
8809  C CA  . ASP B 22   ? 0.4513 0.3301 0.3972 0.0174  -0.0520 -0.0236 20   ASP B CA  
8810  C C   . ASP B 22   ? 0.3712 0.2618 0.3235 0.0139  -0.0486 -0.0221 20   ASP B C   
8811  O O   . ASP B 22   ? 0.3593 0.2557 0.3159 0.0136  -0.0479 -0.0209 20   ASP B O   
8812  C CB  . ASP B 22   ? 0.4799 0.3567 0.4267 0.0207  -0.0539 -0.0233 20   ASP B CB  
8813  N N   . PHE B 23   ? 0.3392 0.2334 0.2920 0.0114  -0.0465 -0.0223 21   PHE B N   
8814  C CA  . PHE B 23   ? 0.3184 0.2241 0.2777 0.0091  -0.0430 -0.0213 21   PHE B CA  
8815  C C   . PHE B 23   ? 0.3115 0.2191 0.2703 0.0038  -0.0438 -0.0182 21   PHE B C   
8816  O O   . PHE B 23   ? 0.2955 0.2105 0.2593 0.0037  -0.0421 -0.0173 21   PHE B O   
8817  C CB  . PHE B 23   ? 0.2957 0.2044 0.2552 0.0078  -0.0409 -0.0222 21   PHE B CB  
8818  C CG  . PHE B 23   ? 0.3387 0.2581 0.3040 0.0051  -0.0377 -0.0209 21   PHE B CG  
8819  C CD1 . PHE B 23   ? 0.2737 0.2018 0.2460 0.0079  -0.0347 -0.0217 21   PHE B CD1 
8820  C CD2 . PHE B 23   ? 0.3022 0.2229 0.2658 -0.0002 -0.0378 -0.0189 21   PHE B CD2 
8821  C CE1 . PHE B 23   ? 0.3108 0.2481 0.2881 0.0056  -0.0319 -0.0206 21   PHE B CE1 
8822  C CE2 . PHE B 23   ? 0.3146 0.2452 0.2835 -0.0023 -0.0348 -0.0178 21   PHE B CE2 
8823  C CZ  . PHE B 23   ? 0.3081 0.2466 0.2836 0.0007  -0.0320 -0.0187 21   PHE B CZ  
8824  N N   . ALA B 24   ? 0.3028 0.2041 0.2556 -0.0007 -0.0462 -0.0164 22   ALA B N   
8825  C CA  . ALA B 24   ? 0.3340 0.2377 0.2863 -0.0059 -0.0468 -0.0132 22   ALA B CA  
8826  C C   . ALA B 24   ? 0.3421 0.2355 0.2865 -0.0099 -0.0508 -0.0113 22   ALA B C   
8827  O O   . ALA B 24   ? 0.3165 0.2108 0.2589 -0.0151 -0.0511 -0.0093 22   ALA B O   
8828  C CB  . ALA B 24   ? 0.2860 0.1995 0.2425 -0.0091 -0.0436 -0.0123 22   ALA B CB  
8829  N N   . PRO B 25   ? 0.3587 0.2422 0.2983 -0.0077 -0.0541 -0.0117 23   PRO B N   
8830  C CA  . PRO B 25   ? 0.3769 0.2496 0.3084 -0.0117 -0.0582 -0.0097 23   PRO B CA  
8831  C C   . PRO B 25   ? 0.3415 0.2174 0.2725 -0.0175 -0.0587 -0.0059 23   PRO B C   
8832  O O   . PRO B 25   ? 0.3702 0.2519 0.3048 -0.0169 -0.0574 -0.0049 23   PRO B O   
8833  C CB  . PRO B 25   ? 0.3793 0.2423 0.3071 -0.0071 -0.0613 -0.0110 23   PRO B CB  
8834  C CG  . PRO B 25   ? 0.3898 0.2607 0.3245 -0.0025 -0.0588 -0.0121 23   PRO B CG  
8835  C CD  . PRO B 25   ? 0.3591 0.2412 0.3006 -0.0017 -0.0544 -0.0136 23   PRO B CD  
8836  N N   . PRO B 26   ? 0.3614 0.2340 0.2879 -0.0234 -0.0604 -0.0036 24   PRO B N   
8837  C CA  . PRO B 26   ? 0.3654 0.2416 0.2913 -0.0292 -0.0607 0.0003  24   PRO B CA  
8838  C C   . PRO B 26   ? 0.3838 0.2525 0.3052 -0.0293 -0.0638 0.0020  24   PRO B C   
8839  O O   . PRO B 26   ? 0.3762 0.2344 0.2932 -0.0262 -0.0668 0.0007  24   PRO B O   
8840  C CB  . PRO B 26   ? 0.3663 0.2390 0.2878 -0.0351 -0.0624 0.0021  24   PRO B CB  
8841  C CG  . PRO B 26   ? 0.4035 0.2646 0.3198 -0.0324 -0.0652 -0.0005 24   PRO B CG  
8842  C CD  . PRO B 26   ? 0.3817 0.2466 0.3030 -0.0251 -0.0624 -0.0044 24   PRO B CD  
8843  N N   . VAL B 27   ? 0.3643 0.2388 0.2868 -0.0329 -0.0630 0.0051  25   VAL B N   
8844  C CA  . VAL B 27   ? 0.4011 0.2691 0.3191 -0.0338 -0.0660 0.0073  25   VAL B CA  
8845  C C   . VAL B 27   ? 0.4146 0.2690 0.3240 -0.0370 -0.0708 0.0088  25   VAL B C   
8846  O O   . VAL B 27   ? 0.4295 0.2736 0.3341 -0.0347 -0.0742 0.0087  25   VAL B O   
8847  C CB  . VAL B 27   ? 0.3772 0.2540 0.2972 -0.0378 -0.0642 0.0105  25   VAL B CB  
8848  C CG1 . VAL B 27   ? 0.4172 0.2868 0.3315 -0.0396 -0.0676 0.0133  25   VAL B CG1 
8849  C CG2 . VAL B 27   ? 0.3783 0.2667 0.3061 -0.0339 -0.0601 0.0086  25   VAL B CG2 
8850  N N   . ARG B 28   ? 0.4081 0.2618 0.3152 -0.0421 -0.0713 0.0102  26   ARG B N   
8851  C CA  . ARG B 28   ? 0.4263 0.2671 0.3250 -0.0462 -0.0760 0.0119  26   ARG B CA  
8852  C C   . ARG B 28   ? 0.4509 0.2914 0.3490 -0.0485 -0.0759 0.0109  26   ARG B C   
8853  O O   . ARG B 28   ? 0.4014 0.2531 0.3056 -0.0487 -0.0722 0.0101  26   ARG B O   
8854  C CB  . ARG B 28   ? 0.4699 0.3102 0.3649 -0.0530 -0.0778 0.0168  26   ARG B CB  
8855  C CG  . ARG B 28   ? 0.4658 0.3180 0.3645 -0.0590 -0.0750 0.0195  26   ARG B CG  
8856  C CD  . ARG B 28   ? 0.4770 0.3303 0.3727 -0.0650 -0.0761 0.0244  26   ARG B CD  
8857  N NE  . ARG B 28   ? 0.4983 0.3568 0.3967 -0.0620 -0.0743 0.0246  26   ARG B NE  
8858  C CZ  . ARG B 28   ? 0.5541 0.4041 0.4478 -0.0605 -0.0772 0.0255  26   ARG B CZ  
8859  N NH1 . ARG B 28   ? 0.5383 0.3738 0.4242 -0.0620 -0.0821 0.0264  26   ARG B NH1 
8860  N NH2 . ARG B 28   ? 0.5107 0.3665 0.4074 -0.0577 -0.0753 0.0254  26   ARG B NH2 
8861  N N   . PRO B 29   ? 0.4549 0.2822 0.3454 -0.0503 -0.0802 0.0108  27   PRO B N   
8862  C CA  . PRO B 29   ? 0.4484 0.2751 0.3375 -0.0537 -0.0806 0.0104  27   PRO B CA  
8863  C C   . PRO B 29   ? 0.4417 0.2784 0.3335 -0.0612 -0.0792 0.0144  27   PRO B C   
8864  O O   . PRO B 29   ? 0.4574 0.2947 0.3474 -0.0659 -0.0803 0.0182  27   PRO B O   
8865  C CB  . PRO B 29   ? 0.4868 0.2960 0.3660 -0.0552 -0.0862 0.0105  27   PRO B CB  
8866  C CG  . PRO B 29   ? 0.5218 0.3230 0.3986 -0.0493 -0.0879 0.0090  27   PRO B CG  
8867  C CD  . PRO B 29   ? 0.4754 0.2873 0.3579 -0.0491 -0.0850 0.0110  27   PRO B CD  
8868  N N   . GLN B 30   ? 0.4116 0.2566 0.3077 -0.0621 -0.0766 0.0134  28   GLN B N   
8869  C CA  . GLN B 30   ? 0.4405 0.2974 0.3406 -0.0682 -0.0745 0.0168  28   GLN B CA  
8870  C C   . GLN B 30   ? 0.4593 0.3093 0.3531 -0.0759 -0.0786 0.0199  28   GLN B C   
8871  O O   . GLN B 30   ? 0.4536 0.2976 0.3442 -0.0767 -0.0806 0.0183  28   GLN B O   
8872  C CB  . GLN B 30   ? 0.4430 0.3120 0.3506 -0.0657 -0.0702 0.0146  28   GLN B CB  
8873  C CG  . GLN B 30   ? 0.3911 0.2665 0.3048 -0.0584 -0.0663 0.0115  28   GLN B CG  
8874  C CD  . GLN B 30   ? 0.3781 0.2626 0.2959 -0.0589 -0.0639 0.0138  28   GLN B CD  
8875  O OE1 . GLN B 30   ? 0.3797 0.2757 0.3021 -0.0618 -0.0611 0.0157  28   GLN B OE1 
8876  N NE2 . GLN B 30   ? 0.4029 0.2822 0.3189 -0.0558 -0.0649 0.0134  28   GLN B NE2 
8877  N N   . SER B 31   ? 0.4286 0.2797 0.3206 -0.0817 -0.0799 0.0244  29   SER B N   
8878  C CA  . SER B 31   ? 0.4487 0.2949 0.3353 -0.0900 -0.0836 0.0281  29   SER B CA  
8879  C C   . SER B 31   ? 0.4535 0.3108 0.3449 -0.0939 -0.0816 0.0289  29   SER B C   
8880  O O   . SER B 31   ? 0.4359 0.3053 0.3348 -0.0904 -0.0771 0.0271  29   SER B O   
8881  C CB  . SER B 31   ? 0.4849 0.3325 0.3697 -0.0953 -0.0845 0.0330  29   SER B CB  
8882  O OG  . SER B 31   ? 0.4459 0.3105 0.3385 -0.0964 -0.0798 0.0348  29   SER B OG  
8883  N N   . THR B 32   ? 0.4410 0.2941 0.3280 -0.1014 -0.0852 0.0320  30   THR B N   
8884  C CA  . THR B 32   ? 0.4576 0.3216 0.3490 -0.1061 -0.0838 0.0335  30   THR B CA  
8885  C C   . THR B 32   ? 0.4085 0.2904 0.3082 -0.1072 -0.0790 0.0361  30   THR B C   
8886  O O   . THR B 32   ? 0.4256 0.3196 0.3321 -0.1057 -0.0754 0.0350  30   THR B O   
8887  C CB  . THR B 32   ? 0.5040 0.3601 0.3888 -0.1147 -0.0889 0.0370  30   THR B CB  
8888  O OG1 . THR B 32   ? 0.5420 0.3808 0.4187 -0.1131 -0.0934 0.0341  30   THR B OG1 
8889  C CG2 . THR B 32   ? 0.5224 0.3901 0.4119 -0.1199 -0.0878 0.0389  30   THR B CG2 
8890  N N   . LEU B 33   ? 0.3936 0.2772 0.2924 -0.1096 -0.0788 0.0394  31   LEU B N   
8891  C CA  . LEU B 33   ? 0.4220 0.3222 0.3280 -0.1105 -0.0742 0.0418  31   LEU B CA  
8892  C C   . LEU B 33   ? 0.3982 0.3062 0.3106 -0.1022 -0.0694 0.0380  31   LEU B C   
8893  O O   . LEU B 33   ? 0.3804 0.3029 0.3001 -0.1015 -0.0652 0.0382  31   LEU B O   
8894  C CB  . LEU B 33   ? 0.3739 0.2733 0.2766 -0.1149 -0.0753 0.0462  31   LEU B CB  
8895  C CG  . LEU B 33   ? 0.4423 0.3379 0.3401 -0.1243 -0.0793 0.0510  31   LEU B CG  
8896  C CD1 . LEU B 33   ? 0.4007 0.2917 0.2935 -0.1283 -0.0812 0.0550  31   LEU B CD1 
8897  C CD2 . LEU B 33   ? 0.4334 0.3449 0.3377 -0.1289 -0.0767 0.0535  31   LEU B CD2 
8898  N N   . ARG B 34   ? 0.3736 0.2724 0.2837 -0.0960 -0.0699 0.0345  32   ARG B N   
8899  C CA  . ARG B 34   ? 0.3986 0.3046 0.3150 -0.0884 -0.0656 0.0308  32   ARG B CA  
8900  C C   . ARG B 34   ? 0.4070 0.3181 0.3279 -0.0858 -0.0637 0.0278  32   ARG B C   
8901  O O   . ARG B 34   ? 0.3498 0.2728 0.2777 -0.0827 -0.0593 0.0267  32   ARG B O   
8902  C CB  . ARG B 34   ? 0.3537 0.2489 0.2667 -0.0825 -0.0670 0.0279  32   ARG B CB  
8903  C CG  . ARG B 34   ? 0.3676 0.2598 0.2774 -0.0837 -0.0681 0.0306  32   ARG B CG  
8904  C CD  . ARG B 34   ? 0.3814 0.2873 0.2974 -0.0821 -0.0635 0.0314  32   ARG B CD  
8905  N NE  . ARG B 34   ? 0.3618 0.2713 0.2829 -0.0744 -0.0604 0.0271  32   ARG B NE  
8906  C CZ  . ARG B 34   ? 0.4044 0.3087 0.3246 -0.0694 -0.0607 0.0251  32   ARG B CZ  
8907  N NH1 . ARG B 34   ? 0.4266 0.3220 0.3409 -0.0707 -0.0639 0.0270  32   ARG B NH1 
8908  N NH2 . ARG B 34   ? 0.3781 0.2864 0.3033 -0.0629 -0.0580 0.0213  32   ARG B NH2 
8909  N N   . ARG B 35   ? 0.3727 0.2745 0.2891 -0.0871 -0.0669 0.0266  33   ARG B N   
8910  C CA  . ARG B 35   ? 0.4002 0.3064 0.3203 -0.0847 -0.0653 0.0238  33   ARG B CA  
8911  C C   . ARG B 35   ? 0.3430 0.2632 0.2687 -0.0892 -0.0630 0.0265  33   ARG B C   
8912  O O   . ARG B 35   ? 0.3375 0.2663 0.2689 -0.0861 -0.0599 0.0245  33   ARG B O   
8913  C CB  . ARG B 35   ? 0.3965 0.2891 0.3099 -0.0853 -0.0695 0.0219  33   ARG B CB  
8914  C CG  . ARG B 35   ? 0.4705 0.3503 0.3793 -0.0793 -0.0711 0.0184  33   ARG B CG  
8915  C CD  . ARG B 35   ? 0.5138 0.3813 0.4165 -0.0784 -0.0745 0.0157  33   ARG B CD  
8916  N NE  . ARG B 35   ? 0.6726 0.5342 0.5696 -0.0860 -0.0787 0.0185  33   ARG B NE  
8917  C CZ  . ARG B 35   ? 0.6680 0.5166 0.5571 -0.0896 -0.0834 0.0203  33   ARG B CZ  
8918  N NH1 . ARG B 35   ? 0.6320 0.4720 0.5177 -0.0860 -0.0846 0.0195  33   ARG B NH1 
8919  N NH2 . ARG B 35   ? 0.5996 0.4438 0.4841 -0.0970 -0.0872 0.0230  33   ARG B NH2 
8920  N N   . ALA B 36   ? 0.3247 0.2475 0.2489 -0.0963 -0.0646 0.0311  34   ALA B N   
8921  C CA  . ALA B 36   ? 0.3573 0.2944 0.2872 -0.1004 -0.0624 0.0339  34   ALA B CA  
8922  C C   . ALA B 36   ? 0.3321 0.2830 0.2694 -0.0965 -0.0570 0.0337  34   ALA B C   
8923  O O   . ALA B 36   ? 0.3066 0.2695 0.2502 -0.0959 -0.0540 0.0336  34   ALA B O   
8924  C CB  . ALA B 36   ? 0.3782 0.3152 0.3047 -0.1091 -0.0653 0.0391  34   ALA B CB  
8925  N N   . ILE B 37   ? 0.3265 0.2756 0.2629 -0.0939 -0.0560 0.0337  35   ILE B N   
8926  C CA  . ILE B 37   ? 0.3180 0.2783 0.2607 -0.0893 -0.0512 0.0327  35   ILE B CA  
8927  C C   . ILE B 37   ? 0.3045 0.2672 0.2517 -0.0827 -0.0487 0.0283  35   ILE B C   
8928  O O   . ILE B 37   ? 0.2859 0.2603 0.2394 -0.0810 -0.0451 0.0280  35   ILE B O   
8929  C CB  . ILE B 37   ? 0.3081 0.2635 0.2480 -0.0872 -0.0513 0.0329  35   ILE B CB  
8930  C CG1 . ILE B 37   ? 0.3026 0.2582 0.2388 -0.0939 -0.0531 0.0378  35   ILE B CG1 
8931  C CG2 . ILE B 37   ? 0.2914 0.2557 0.2371 -0.0812 -0.0467 0.0307  35   ILE B CG2 
8932  C CD1 . ILE B 37   ? 0.3202 0.2670 0.2514 -0.0926 -0.0547 0.0381  35   ILE B CD1 
8933  N N   . THR B 38   ? 0.2784 0.2298 0.2222 -0.0787 -0.0504 0.0249  36   THR B N   
8934  C CA  . THR B 38   ? 0.3086 0.2618 0.2564 -0.0723 -0.0480 0.0208  36   THR B CA  
8935  C C   . THR B 38   ? 0.2955 0.2552 0.2466 -0.0736 -0.0471 0.0205  36   THR B C   
8936  O O   . THR B 38   ? 0.2914 0.2593 0.2482 -0.0697 -0.0436 0.0187  36   THR B O   
8937  C CB  . THR B 38   ? 0.3397 0.2795 0.2827 -0.0684 -0.0504 0.0175  36   THR B CB  
8938  O OG1 . THR B 38   ? 0.3263 0.2601 0.2662 -0.0675 -0.0516 0.0181  36   THR B OG1 
8939  C CG2 . THR B 38   ? 0.3237 0.2662 0.2711 -0.0618 -0.0476 0.0134  36   THR B CG2 
8940  N N   . ALA B 39   ? 0.2891 0.2448 0.2364 -0.0792 -0.0504 0.0225  37   ALA B N   
8941  C CA  . ALA B 39   ? 0.3250 0.2863 0.2748 -0.0809 -0.0502 0.0225  37   ALA B CA  
8942  C C   . ALA B 39   ? 0.3214 0.2986 0.2785 -0.0817 -0.0465 0.0245  37   ALA B C   
8943  O O   . ALA B 39   ? 0.3096 0.2935 0.2708 -0.0805 -0.0448 0.0235  37   ALA B O   
8944  C CB  . ALA B 39   ? 0.3132 0.2673 0.2573 -0.0877 -0.0548 0.0247  37   ALA B CB  
8945  N N   . ALA B 40   ? 0.3082 0.2915 0.2668 -0.0837 -0.0451 0.0273  38   ALA B N   
8946  C CA  . ALA B 40   ? 0.2993 0.2978 0.2644 -0.0846 -0.0416 0.0295  38   ALA B CA  
8947  C C   . ALA B 40   ? 0.2872 0.2924 0.2575 -0.0780 -0.0372 0.0270  38   ALA B C   
8948  O O   . ALA B 40   ? 0.2905 0.3082 0.2663 -0.0776 -0.0341 0.0283  38   ALA B O   
8949  C CB  . ALA B 40   ? 0.2399 0.2423 0.2037 -0.0902 -0.0422 0.0340  38   ALA B CB  
8950  N N   . TYR B 41   ? 0.2599 0.2573 0.2287 -0.0728 -0.0370 0.0236  39   TYR B N   
8951  C CA  . TYR B 41   ? 0.2520 0.2541 0.2247 -0.0671 -0.0333 0.0216  39   TYR B CA  
8952  C C   . TYR B 41   ? 0.2785 0.2926 0.2579 -0.0648 -0.0298 0.0211  39   TYR B C   
8953  O O   . TYR B 41   ? 0.2518 0.2750 0.2349 -0.0636 -0.0268 0.0220  39   TYR B O   
8954  C CB  . TYR B 41   ? 0.2402 0.2324 0.2109 -0.0619 -0.0341 0.0177  39   TYR B CB  
8955  C CG  . TYR B 41   ? 0.2392 0.2319 0.2116 -0.0570 -0.0318 0.0159  39   TYR B CG  
8956  C CD1 . TYR B 41   ? 0.2320 0.2352 0.2092 -0.0553 -0.0283 0.0164  39   TYR B CD1 
8957  C CD2 . TYR B 41   ? 0.2763 0.2591 0.2456 -0.0538 -0.0333 0.0136  39   TYR B CD2 
8958  C CE1 . TYR B 41   ? 0.2514 0.2546 0.2298 -0.0510 -0.0265 0.0146  39   TYR B CE1 
8959  C CE2 . TYR B 41   ? 0.2463 0.2297 0.2173 -0.0495 -0.0316 0.0119  39   TYR B CE2 
8960  C CZ  . TYR B 41   ? 0.2399 0.2334 0.2154 -0.0483 -0.0282 0.0124  39   TYR B CZ  
8961  O OH  . TYR B 41   ? 0.2361 0.2299 0.2131 -0.0442 -0.0267 0.0107  39   TYR B OH  
8962  N N   . ARG B 42   ? 0.2560 0.2701 0.2366 -0.0642 -0.0302 0.0197  40   ARG B N   
8963  C CA  . ARG B 42   ? 0.2291 0.2536 0.2158 -0.0617 -0.0271 0.0191  40   ARG B CA  
8964  C C   . ARG B 42   ? 0.2610 0.2898 0.2486 -0.0658 -0.0284 0.0211  40   ARG B C   
8965  O O   . ARG B 42   ? 0.3051 0.3372 0.2956 -0.0637 -0.0275 0.0197  40   ARG B O   
8966  C CB  . ARG B 42   ? 0.2530 0.2744 0.2414 -0.0556 -0.0255 0.0152  40   ARG B CB  
8967  C CG  . ARG B 42   ? 0.2371 0.2571 0.2260 -0.0516 -0.0237 0.0137  40   ARG B CG  
8968  C CD  . ARG B 42   ? 0.2679 0.2835 0.2577 -0.0461 -0.0227 0.0100  40   ARG B CD  
8969  N NE  . ARG B 42   ? 0.2570 0.2678 0.2454 -0.0437 -0.0226 0.0088  40   ARG B NE  
8970  C CZ  . ARG B 42   ? 0.2678 0.2837 0.2590 -0.0412 -0.0201 0.0086  40   ARG B CZ  
8971  N NH1 . ARG B 42   ? 0.2315 0.2572 0.2271 -0.0403 -0.0173 0.0091  40   ARG B NH1 
8972  N NH2 . ARG B 42   ? 0.2488 0.2597 0.2381 -0.0394 -0.0206 0.0076  40   ARG B NH2 
8973  N N   . ARG B 43   ? 0.2431 0.2724 0.2283 -0.0719 -0.0307 0.0245  41   ARG B N   
8974  C CA  . ARG B 43   ? 0.2742 0.3075 0.2600 -0.0766 -0.0326 0.0266  41   ARG B CA  
8975  C C   . ARG B 43   ? 0.2582 0.3058 0.2510 -0.0753 -0.0293 0.0277  41   ARG B C   
8976  O O   . ARG B 43   ? 0.2489 0.3047 0.2452 -0.0735 -0.0263 0.0285  41   ARG B O   
8977  C CB  . ARG B 43   ? 0.2884 0.3200 0.2705 -0.0836 -0.0355 0.0305  41   ARG B CB  
8978  C CG  . ARG B 43   ? 0.3013 0.3372 0.2839 -0.0896 -0.0379 0.0333  41   ARG B CG  
8979  C CD  . ARG B 43   ? 0.2992 0.3287 0.2762 -0.0965 -0.0417 0.0364  41   ARG B CD  
8980  N NE  . ARG B 43   ? 0.3557 0.3690 0.3256 -0.0960 -0.0452 0.0340  41   ARG B NE  
8981  C CZ  . ARG B 43   ? 0.3343 0.3380 0.2983 -0.0991 -0.0479 0.0352  41   ARG B CZ  
8982  N NH1 . ARG B 43   ? 0.3147 0.3231 0.2787 -0.1033 -0.0478 0.0390  41   ARG B NH1 
8983  N NH2 . ARG B 43   ? 0.3478 0.3368 0.3055 -0.0977 -0.0509 0.0326  41   ARG B NH2 
8984  N N   . PRO B 44   ? 0.2689 0.3198 0.2637 -0.0758 -0.0299 0.0275  42   PRO B N   
8985  C CA  . PRO B 44   ? 0.2550 0.3198 0.2565 -0.0746 -0.0271 0.0288  42   PRO B CA  
8986  C C   . PRO B 44   ? 0.2915 0.3667 0.2955 -0.0785 -0.0262 0.0328  42   PRO B C   
8987  O O   . PRO B 44   ? 0.2791 0.3522 0.2800 -0.0845 -0.0289 0.0356  42   PRO B O   
8988  C CB  . PRO B 44   ? 0.3219 0.3867 0.3234 -0.0767 -0.0294 0.0289  42   PRO B CB  
8989  C CG  . PRO B 44   ? 0.3402 0.3908 0.3360 -0.0751 -0.0316 0.0256  42   PRO B CG  
8990  C CD  . PRO B 44   ? 0.2969 0.3387 0.2879 -0.0763 -0.0329 0.0256  42   PRO B CD  
8991  N N   . GLU B 45   ? 0.2623 0.3485 0.2718 -0.0750 -0.0224 0.0330  43   GLU B N   
8992  C CA  . GLU B 45   ? 0.2577 0.3549 0.2699 -0.0778 -0.0208 0.0366  43   GLU B CA  
8993  C C   . GLU B 45   ? 0.2935 0.3979 0.3074 -0.0841 -0.0230 0.0404  43   GLU B C   
8994  O O   . GLU B 45   ? 0.2792 0.3879 0.2925 -0.0892 -0.0236 0.0440  43   GLU B O   
8995  C CB  . GLU B 45   ? 0.2789 0.3864 0.2967 -0.0720 -0.0163 0.0357  43   GLU B CB  
8996  C CG  . GLU B 45   ? 0.3089 0.4209 0.3265 -0.0718 -0.0139 0.0370  43   GLU B CG  
8997  C CD  . GLU B 45   ? 0.2427 0.3598 0.2637 -0.0649 -0.0097 0.0347  43   GLU B CD  
8998  O OE1 . GLU B 45   ? 0.2401 0.3531 0.2620 -0.0599 -0.0090 0.0313  43   GLU B OE1 
8999  O OE2 . GLU B 45   ? 0.2668 0.3919 0.2892 -0.0645 -0.0073 0.0363  43   GLU B OE2 
9000  N N   . THR B 46   ? 0.2945 0.4002 0.3101 -0.0841 -0.0242 0.0398  44   THR B N   
9001  C CA  . THR B 46   ? 0.2963 0.4087 0.3135 -0.0903 -0.0267 0.0434  44   THR B CA  
9002  C C   . THR B 46   ? 0.3033 0.4058 0.3143 -0.0972 -0.0313 0.0451  44   THR B C   
9003  O O   . THR B 46   ? 0.3174 0.4258 0.3292 -0.1036 -0.0333 0.0489  44   THR B O   
9004  C CB  . THR B 46   ? 0.2683 0.3835 0.2883 -0.0886 -0.0273 0.0422  44   THR B CB  
9005  O OG1 . THR B 46   ? 0.2759 0.3778 0.2914 -0.0857 -0.0288 0.0384  44   THR B OG1 
9006  C CG2 . THR B 46   ? 0.2932 0.4207 0.3202 -0.0828 -0.0231 0.0417  44   THR B CG2 
9007  N N   . GLU B 47   ? 0.2644 0.3521 0.2691 -0.0961 -0.0330 0.0424  45   GLU B N   
9008  C CA  . GLU B 47   ? 0.2976 0.3749 0.2958 -0.1023 -0.0374 0.0439  45   GLU B CA  
9009  C C   . GLU B 47   ? 0.2902 0.3673 0.2864 -0.1047 -0.0368 0.0462  45   GLU B C   
9010  O O   . GLU B 47   ? 0.3143 0.3884 0.3070 -0.1115 -0.0400 0.0494  45   GLU B O   
9011  C CB  . GLU B 47   ? 0.3277 0.3888 0.3197 -0.0998 -0.0398 0.0399  45   GLU B CB  
9012  C CG  . GLU B 47   ? 0.3702 0.4303 0.3628 -0.0986 -0.0410 0.0380  45   GLU B CG  
9013  C CD  . GLU B 47   ? 0.4768 0.5231 0.4645 -0.0942 -0.0420 0.0335  45   GLU B CD  
9014  O OE1 . GLU B 47   ? 0.4516 0.4864 0.4337 -0.0941 -0.0435 0.0323  45   GLU B OE1 
9015  O OE2 . GLU B 47   ? 0.5313 0.5784 0.5206 -0.0907 -0.0413 0.0312  45   GLU B OE2 
9016  N N   . CYS B 48   ? 0.2828 0.3632 0.2811 -0.0996 -0.0329 0.0449  46   CYS B N   
9017  C CA  . CYS B 48   ? 0.3018 0.3818 0.2978 -0.1015 -0.0322 0.0470  46   CYS B CA  
9018  C C   . CYS B 48   ? 0.3083 0.4023 0.3081 -0.1065 -0.0312 0.0519  46   CYS B C   
9019  O O   . CYS B 48   ? 0.2773 0.3696 0.2737 -0.1120 -0.0328 0.0551  46   CYS B O   
9020  C CB  . CYS B 48   ? 0.2491 0.3294 0.2463 -0.0944 -0.0284 0.0441  46   CYS B CB  
9021  S SG  . CYS B 48   ? 0.2949 0.3595 0.2877 -0.0887 -0.0293 0.0389  46   CYS B SG  
9022  N N   . LEU B 49   ? 0.2645 0.3724 0.2711 -0.1046 -0.0284 0.0525  47   LEU B N   
9023  C CA  . LEU B 49   ? 0.3104 0.4333 0.3214 -0.1076 -0.0262 0.0567  47   LEU B CA  
9024  C C   . LEU B 49   ? 0.2591 0.3860 0.2698 -0.1165 -0.0295 0.0616  47   LEU B C   
9025  O O   . LEU B 49   ? 0.2842 0.4172 0.2948 -0.1208 -0.0289 0.0653  47   LEU B O   
9026  C CB  . LEU B 49   ? 0.2488 0.3857 0.2674 -0.1023 -0.0221 0.0559  47   LEU B CB  
9027  C CG  . LEU B 49   ? 0.2576 0.3989 0.2778 -0.0961 -0.0175 0.0543  47   LEU B CG  
9028  C CD1 . LEU B 49   ? 0.2572 0.4043 0.2762 -0.1000 -0.0163 0.0580  47   LEU B CD1 
9029  C CD2 . LEU B 49   ? 0.2393 0.3667 0.2552 -0.0908 -0.0174 0.0497  47   LEU B CD2 
9030  N N   . PRO B 50   ? 0.2895 0.4135 0.2998 -0.1199 -0.0331 0.0618  48   PRO B N   
9031  C CA  . PRO B 50   ? 0.2986 0.4283 0.3095 -0.1287 -0.0362 0.0667  48   PRO B CA  
9032  C C   . PRO B 50   ? 0.3206 0.4421 0.3251 -0.1352 -0.0389 0.0696  48   PRO B C   
9033  O O   . PRO B 50   ? 0.3289 0.4604 0.3354 -0.1408 -0.0387 0.0744  48   PRO B O   
9034  C CB  . PRO B 50   ? 0.3094 0.4327 0.3190 -0.1302 -0.0401 0.0652  48   PRO B CB  
9035  C CG  . PRO B 50   ? 0.2853 0.4103 0.2985 -0.1217 -0.0370 0.0609  48   PRO B CG  
9036  C CD  . PRO B 50   ? 0.3029 0.4221 0.3139 -0.1157 -0.0339 0.0580  48   PRO B CD  
9037  N N   . PRO B 51   ? 0.3341 0.4382 0.3310 -0.1346 -0.0415 0.0671  49   PRO B N   
9038  C CA  . PRO B 51   ? 0.3325 0.4292 0.3235 -0.1404 -0.0440 0.0700  49   PRO B CA  
9039  C C   . PRO B 51   ? 0.3526 0.4576 0.3452 -0.1391 -0.0400 0.0719  49   PRO B C   
9040  O O   . PRO B 51   ? 0.3309 0.4370 0.3210 -0.1455 -0.0412 0.0762  49   PRO B O   
9041  C CB  . PRO B 51   ? 0.3737 0.4504 0.3568 -0.1380 -0.0470 0.0660  49   PRO B CB  
9042  C CG  . PRO B 51   ? 0.3650 0.4410 0.3509 -0.1294 -0.0443 0.0609  49   PRO B CG  
9043  C CD  . PRO B 51   ? 0.3243 0.4145 0.3176 -0.1294 -0.0429 0.0618  49   PRO B CD  
9044  N N   . LEU B 52   ? 0.2709 0.3816 0.2672 -0.1312 -0.0352 0.0689  50   LEU B N   
9045  C CA  . LEU B 52   ? 0.3061 0.4247 0.3036 -0.1298 -0.0313 0.0706  50   LEU B CA  
9046  C C   . LEU B 52   ? 0.3220 0.4597 0.3260 -0.1333 -0.0289 0.0751  50   LEU B C   
9047  O O   . LEU B 52   ? 0.3097 0.4532 0.3129 -0.1370 -0.0278 0.0789  50   LEU B O   
9048  C CB  . LEU B 52   ? 0.3091 0.4274 0.3083 -0.1203 -0.0272 0.0659  50   LEU B CB  
9049  C CG  . LEU B 52   ? 0.2610 0.3620 0.2545 -0.1161 -0.0290 0.0614  50   LEU B CG  
9050  C CD1 . LEU B 52   ? 0.2761 0.3790 0.2726 -0.1070 -0.0249 0.0569  50   LEU B CD1 
9051  C CD2 . LEU B 52   ? 0.3304 0.4213 0.3169 -0.1194 -0.0311 0.0629  50   LEU B CD2 
9052  N N   . VAL B 53   ? 0.2971 0.4451 0.3075 -0.1321 -0.0280 0.0750  51   VAL B N   
9053  C CA  . VAL B 53   ? 0.3218 0.4885 0.3388 -0.1356 -0.0260 0.0794  51   VAL B CA  
9054  C C   . VAL B 53   ? 0.3273 0.4942 0.3417 -0.1459 -0.0297 0.0849  51   VAL B C   
9055  O O   . VAL B 53   ? 0.3179 0.4965 0.3344 -0.1496 -0.0278 0.0893  51   VAL B O   
9056  C CB  . VAL B 53   ? 0.3081 0.4836 0.3318 -0.1330 -0.0255 0.0783  51   VAL B CB  
9057  C CG1 . VAL B 53   ? 0.3272 0.5221 0.3579 -0.1376 -0.0243 0.0834  51   VAL B CG1 
9058  C CG2 . VAL B 53   ? 0.2531 0.4303 0.2799 -0.1229 -0.0214 0.0735  51   VAL B CG2 
9059  N N   . GLU B 54   ? 0.3343 0.4882 0.3439 -0.1507 -0.0351 0.0848  52   GLU B N   
9060  C CA  . GLU B 54   ? 0.3836 0.5355 0.3897 -0.1602 -0.0393 0.0896  52   GLU B CA  
9061  C C   . GLU B 54   ? 0.3829 0.5300 0.3835 -0.1628 -0.0389 0.0919  52   GLU B C   
9062  O O   . GLU B 54   ? 0.3742 0.5279 0.3742 -0.1665 -0.0390 0.0959  52   GLU B O   
9063  C CB  . GLU B 54   ? 0.3670 0.5031 0.3675 -0.1638 -0.0452 0.0882  52   GLU B CB  
9064  N N   . ALA B 55   ? 0.3364 0.4706 0.3319 -0.1585 -0.0386 0.0884  53   ALA B N   
9065  C CA  . ALA B 55   ? 0.3838 0.5123 0.3736 -0.1607 -0.0385 0.0904  53   ALA B CA  
9066  C C   . ALA B 55   ? 0.3572 0.5020 0.3513 -0.1590 -0.0331 0.0928  53   ALA B C   
9067  O O   . ALA B 55   ? 0.3939 0.5402 0.3850 -0.1639 -0.0331 0.0969  53   ALA B O   
9068  C CB  . ALA B 55   ? 0.3585 0.4695 0.3419 -0.1548 -0.0393 0.0855  53   ALA B CB  
9069  N N   . ALA B 56   ? 0.3306 0.4875 0.3316 -0.1519 -0.0284 0.0904  54   ALA B N   
9070  C CA  . ALA B 56   ? 0.3443 0.5165 0.3494 -0.1490 -0.0229 0.0918  54   ALA B CA  
9071  C C   . ALA B 56   ? 0.3783 0.5683 0.3896 -0.1520 -0.0215 0.0959  54   ALA B C   
9072  O O   . ALA B 56   ? 0.3913 0.5941 0.4055 -0.1491 -0.0171 0.0971  54   ALA B O   
9073  C CB  . ALA B 56   ? 0.3181 0.4925 0.3266 -0.1384 -0.0186 0.0864  54   ALA B CB  
9074  N N   . THR B 57   ? 0.3863 0.5756 0.3985 -0.1558 -0.0254 0.0971  55   THR B N   
9075  C CA  . THR B 57   ? 0.3884 0.5923 0.4054 -0.1572 -0.0247 0.1001  55   THR B CA  
9076  C C   . THR B 57   ? 0.4146 0.6215 0.4282 -0.1620 -0.0250 0.1044  55   THR B C   
9077  O O   . THR B 57   ? 0.4491 0.6434 0.4556 -0.1673 -0.0287 0.1059  55   THR B O   
9078  C CB  . THR B 57   ? 0.3845 0.5851 0.4021 -0.1609 -0.0294 0.1006  55   THR B CB  
9079  O OG1 . THR B 57   ? 0.3561 0.5579 0.3783 -0.1557 -0.0283 0.0968  55   THR B OG1 
9080  C CG2 . THR B 57   ? 0.4344 0.6486 0.4557 -0.1639 -0.0296 0.1046  55   THR B CG2 
9081  N N   . GLN B 58   ? 0.4050 0.6286 0.4236 -0.1599 -0.0212 0.1064  56   GLN B N   
9082  C CA  . GLN B 58   ? 0.4199 0.6488 0.4363 -0.1643 -0.0212 0.1107  56   GLN B CA  
9083  C C   . GLN B 58   ? 0.4207 0.6653 0.4431 -0.1655 -0.0207 0.1136  56   GLN B C   
9084  O O   . GLN B 58   ? 0.3896 0.6431 0.4183 -0.1613 -0.0190 0.1121  56   GLN B O   
9085  C CB  . GLN B 58   ? 0.4119 0.6454 0.4274 -0.1604 -0.0163 0.1103  56   GLN B CB  
9086  C CG  . GLN B 58   ? 0.3810 0.5996 0.3906 -0.1589 -0.0165 0.1075  56   GLN B CG  
9087  C CD  . GLN B 58   ? 0.4317 0.6528 0.4383 -0.1571 -0.0129 0.1082  56   GLN B CD  
9088  O OE1 . GLN B 58   ? 0.4580 0.6751 0.4594 -0.1623 -0.0147 0.1114  56   GLN B OE1 
9089  N NE2 . GLN B 58   ? 0.4468 0.6743 0.4563 -0.1497 -0.0077 0.1052  56   GLN B NE2 
9090  N N   . SER B 59   ? 0.4100 0.6580 0.4302 -0.1714 -0.0223 0.1180  57   SER B N   
9091  C CA  . SER B 59   ? 0.4578 0.7205 0.4831 -0.1735 -0.0222 0.1214  57   SER B CA  
9092  C C   . SER B 59   ? 0.4568 0.7371 0.4895 -0.1662 -0.0161 0.1204  57   SER B C   
9093  O O   . SER B 59   ? 0.3993 0.6808 0.4321 -0.1603 -0.0118 0.1178  57   SER B O   
9094  C CB  . SER B 59   ? 0.4557 0.7190 0.4769 -0.1808 -0.0245 0.1263  57   SER B CB  
9095  O OG  . SER B 59   ? 0.4459 0.7117 0.4650 -0.1791 -0.0209 0.1267  57   SER B OG  
9096  N N   . LYS B 60   ? 0.4221 0.7159 0.4607 -0.1665 -0.0159 0.1225  58   LYS B N   
9097  C CA  . LYS B 60   ? 0.4159 0.7267 0.4612 -0.1597 -0.0104 0.1220  58   LYS B CA  
9098  C C   . LYS B 60   ? 0.4036 0.7214 0.4475 -0.1594 -0.0069 0.1240  58   LYS B C   
9099  O O   . LYS B 60   ? 0.4417 0.7675 0.4883 -0.1524 -0.0018 0.1219  58   LYS B O   
9100  C CB  . LYS B 60   ? 0.4056 0.7292 0.4571 -0.1608 -0.0113 0.1245  58   LYS B CB  
9101  N N   . GLU B 61   ? 0.4329 0.7475 0.4722 -0.1670 -0.0098 0.1280  59   GLU B N   
9102  C CA  . GLU B 61   ? 0.3886 0.7091 0.4259 -0.1674 -0.0068 0.1301  59   GLU B CA  
9103  C C   . GLU B 61   ? 0.4761 0.7882 0.5092 -0.1626 -0.0039 0.1266  59   GLU B C   
9104  O O   . GLU B 61   ? 0.4647 0.7856 0.4995 -0.1569 0.0012  0.1255  59   GLU B O   
9105  C CB  . GLU B 61   ? 0.4547 0.7708 0.4870 -0.1769 -0.0111 0.1349  59   GLU B CB  
9106  N N   . ILE B 62   ? 0.4364 0.7313 0.4640 -0.1647 -0.0072 0.1247  60   ILE B N   
9107  C CA  . ILE B 62   ? 0.4354 0.7214 0.4587 -0.1606 -0.0049 0.1215  60   ILE B CA  
9108  C C   . ILE B 62   ? 0.4122 0.7044 0.4405 -0.1512 -0.0001 0.1170  60   ILE B C   
9109  O O   . ILE B 62   ? 0.4389 0.7339 0.4663 -0.1459 0.0043  0.1152  60   ILE B O   
9110  C CB  . ILE B 62   ? 0.4427 0.7088 0.4593 -0.1649 -0.0098 0.1205  60   ILE B CB  
9111  C CG1 . ILE B 62   ? 0.4332 0.6924 0.4435 -0.1735 -0.0140 0.1248  60   ILE B CG1 
9112  C CG2 . ILE B 62   ? 0.4157 0.6727 0.4289 -0.1597 -0.0074 0.1165  60   ILE B CG2 
9113  C CD1 . ILE B 62   ? 0.4865 0.7259 0.4899 -0.1782 -0.0195 0.1242  60   ILE B CD1 
9114  N N   . ARG B 63   ? 0.3501 0.6443 0.3835 -0.1489 -0.0010 0.1152  61   ARG B N   
9115  C CA  . ARG B 63   ? 0.3612 0.6602 0.3992 -0.1400 0.0030  0.1109  61   ARG B CA  
9116  C C   . ARG B 63   ? 0.3842 0.6998 0.4268 -0.1343 0.0084  0.1111  61   ARG B C   
9117  O O   . ARG B 63   ? 0.3784 0.6961 0.4217 -0.1269 0.0127  0.1077  61   ARG B O   
9118  C CB  . ARG B 63   ? 0.3580 0.6566 0.4006 -0.1393 0.0007  0.1094  61   ARG B CB  
9119  C CG  . ARG B 63   ? 0.4553 0.7373 0.4942 -0.1406 -0.0027 0.1068  61   ARG B CG  
9120  C CD  . ARG B 63   ? 0.4770 0.7573 0.5185 -0.1435 -0.0068 0.1071  61   ARG B CD  
9121  N NE  . ARG B 63   ? 0.4394 0.7347 0.4885 -0.1393 -0.0045 0.1072  61   ARG B NE  
9122  C CZ  . ARG B 63   ? 0.4731 0.7726 0.5251 -0.1428 -0.0076 0.1093  61   ARG B CZ  
9123  N NH1 . ARG B 63   ? 0.4505 0.7403 0.4985 -0.1504 -0.0130 0.1114  61   ARG B NH1 
9124  N NH2 . ARG B 63   ? 0.5353 0.8486 0.5942 -0.1384 -0.0052 0.1094  61   ARG B NH2 
9125  N N   . ASP B 64   ? 0.3824 0.7097 0.4280 -0.1375 0.0081  0.1150  62   ASP B N   
9126  C CA  . ASP B 64   ? 0.3765 0.7196 0.4259 -0.1325 0.0130  0.1156  62   ASP B CA  
9127  C C   . ASP B 64   ? 0.3637 0.7056 0.4080 -0.1319 0.0159  0.1159  62   ASP B C   
9128  O O   . ASP B 64   ? 0.3993 0.7475 0.4447 -0.1246 0.0208  0.1134  62   ASP B O   
9129  C CB  . ASP B 64   ? 0.4026 0.7582 0.4562 -0.1370 0.0117  0.1201  62   ASP B CB  
9130  C CG  . ASP B 64   ? 0.3720 0.7299 0.4308 -0.1373 0.0090  0.1200  62   ASP B CG  
9131  O OD1 . ASP B 64   ? 0.4168 0.7678 0.4765 -0.1334 0.0086  0.1162  62   ASP B OD1 
9132  O OD2 . ASP B 64   ? 0.4398 0.8066 0.5017 -0.1416 0.0072  0.1237  62   ASP B OD2 
9133  N N   . ALA B 65   ? 0.3722 0.7055 0.4104 -0.1394 0.0128  0.1188  63   ALA B N   
9134  C CA  . ALA B 65   ? 0.3908 0.7218 0.4234 -0.1393 0.0151  0.1192  63   ALA B CA  
9135  C C   . ALA B 65   ? 0.4102 0.7314 0.4393 -0.1334 0.0173  0.1145  63   ALA B C   
9136  O O   . ALA B 65   ? 0.3999 0.7240 0.4266 -0.1291 0.0213  0.1134  63   ALA B O   
9137  C CB  . ALA B 65   ? 0.4086 0.7309 0.4351 -0.1487 0.0107  0.1233  63   ALA B CB  
9138  N N   . ALA B 66   ? 0.3838 0.6936 0.4123 -0.1332 0.0147  0.1119  64   ALA B N   
9139  C CA  . ALA B 66   ? 0.4082 0.7088 0.4336 -0.1278 0.0166  0.1075  64   ALA B CA  
9140  C C   . ALA B 66   ? 0.3674 0.6777 0.3976 -0.1181 0.0218  0.1038  64   ALA B C   
9141  O O   . ALA B 66   ? 0.3580 0.6670 0.3853 -0.1129 0.0253  0.1012  64   ALA B O   
9142  C CB  . ALA B 66   ? 0.3160 0.6022 0.3397 -0.1303 0.0124  0.1058  64   ALA B CB  
9143  N N   . ALA B 67   ? 0.3564 0.6764 0.3937 -0.1156 0.0221  0.1035  65   ALA B N   
9144  C CA  . ALA B 67   ? 0.3407 0.6698 0.3826 -0.1062 0.0267  0.1000  65   ALA B CA  
9145  C C   . ALA B 67   ? 0.3806 0.7203 0.4219 -0.1027 0.0312  0.1007  65   ALA B C   
9146  O O   . ALA B 67   ? 0.4088 0.7511 0.4501 -0.0947 0.0354  0.0972  65   ALA B O   
9147  C CB  . ALA B 67   ? 0.3499 0.6873 0.3993 -0.1049 0.0258  0.1002  65   ALA B CB  
9148  N N   . SER B 68   ? 0.3809 0.7269 0.4215 -0.1084 0.0304  0.1052  66   SER B N   
9149  C CA  . SER B 68   ? 0.4221 0.7782 0.4617 -0.1055 0.0347  0.1062  66   SER B CA  
9150  C C   . SER B 68   ? 0.3956 0.7428 0.4275 -0.1047 0.0363  0.1048  66   SER B C   
9151  O O   . SER B 68   ? 0.4381 0.7892 0.4688 -0.0977 0.0407  0.1021  66   SER B O   
9152  C CB  . SER B 68   ? 0.3737 0.7391 0.4149 -0.1123 0.0332  0.1116  66   SER B CB  
9153  N N   . THR B 69   ? 0.4121 0.7467 0.4383 -0.1116 0.0325  0.1065  67   THR B N   
9154  C CA  . THR B 69   ? 0.3497 0.6742 0.3683 -0.1108 0.0335  0.1050  67   THR B CA  
9155  C C   . THR B 69   ? 0.3935 0.7134 0.4118 -0.1025 0.0361  0.0995  67   THR B C   
9156  O O   . THR B 69   ? 0.4214 0.7420 0.4361 -0.0972 0.0399  0.0972  67   THR B O   
9157  C CB  . THR B 69   ? 0.4117 0.7218 0.4247 -0.1191 0.0284  0.1073  67   THR B CB  
9158  O OG1 . THR B 69   ? 0.4177 0.7316 0.4298 -0.1267 0.0262  0.1124  67   THR B OG1 
9159  C CG2 . THR B 69   ? 0.3593 0.6577 0.3641 -0.1178 0.0292  0.1054  67   THR B CG2 
9160  N N   . ALA B 70   ? 0.3476 0.6628 0.3695 -0.1013 0.0342  0.0972  68   ALA B N   
9161  C CA  . ALA B 70   ? 0.3799 0.6913 0.4021 -0.0934 0.0366  0.0920  68   ALA B CA  
9162  C C   . ALA B 70   ? 0.3839 0.7075 0.4095 -0.0847 0.0416  0.0896  68   ALA B C   
9163  O O   . ALA B 70   ? 0.4173 0.7383 0.4400 -0.0781 0.0447  0.0858  68   ALA B O   
9164  C CB  . ALA B 70   ? 0.3489 0.6550 0.3753 -0.0937 0.0337  0.0904  68   ALA B CB  
9165  N N   . ARG B 71   ? 0.3865 0.7230 0.4180 -0.0845 0.0424  0.0917  69   ARG B N   
9166  C CA  . ARG B 71   ? 0.3694 0.7172 0.4040 -0.0761 0.0471  0.0895  69   ARG B CA  
9167  C C   . ARG B 71   ? 0.3336 0.6836 0.3626 -0.0740 0.0505  0.0895  69   ARG B C   
9168  O O   . ARG B 71   ? 0.3863 0.7377 0.4139 -0.0660 0.0543  0.0856  69   ARG B O   
9169  C CB  . ARG B 71   ? 0.3934 0.7548 0.4352 -0.0769 0.0469  0.0922  69   ARG B CB  
9170  C CG  . ARG B 71   ? 0.3900 0.7634 0.4349 -0.0684 0.0516  0.0903  69   ARG B CG  
9171  C CD  . ARG B 71   ? 0.4103 0.7969 0.4629 -0.0684 0.0514  0.0926  69   ARG B CD  
9172  N NE  . ARG B 71   ? 0.4366 0.8223 0.4943 -0.0641 0.0505  0.0899  69   ARG B NE  
9173  C CZ  . ARG B 71   ? 0.4954 0.8817 0.5544 -0.0550 0.0534  0.0855  69   ARG B CZ  
9174  N NH1 . ARG B 71   ? 0.4576 0.8447 0.5128 -0.0488 0.0574  0.0829  69   ARG B NH1 
9175  N NH2 . ARG B 71   ? 0.5165 0.9020 0.5802 -0.0519 0.0521  0.0836  69   ARG B NH2 
9176  N N   . LYS B 72   ? 0.4135 0.7637 0.4389 -0.0812 0.0492  0.0937  70   LYS B N   
9177  C CA  . LYS B 72   ? 0.3775 0.7292 0.3969 -0.0798 0.0523  0.0939  70   LYS B CA  
9178  C C   . LYS B 72   ? 0.4301 0.7694 0.4424 -0.0764 0.0531  0.0901  70   LYS B C   
9179  O O   . LYS B 72   ? 0.4588 0.8000 0.4676 -0.0701 0.0569  0.0875  70   LYS B O   
9180  C CB  . LYS B 72   ? 0.4228 0.7753 0.4394 -0.0888 0.0500  0.0994  70   LYS B CB  
9181  N N   . LEU B 73   ? 0.4441 0.7705 0.4539 -0.0803 0.0495  0.0898  71   LEU B N   
9182  C CA  . LEU B 73   ? 0.4298 0.7444 0.4329 -0.0773 0.0500  0.0863  71   LEU B CA  
9183  C C   . LEU B 73   ? 0.3853 0.7012 0.3903 -0.0674 0.0532  0.0808  71   LEU B C   
9184  O O   . LEU B 73   ? 0.3979 0.7105 0.3974 -0.0623 0.0559  0.0777  71   LEU B O   
9185  C CB  . LEU B 73   ? 0.4092 0.7102 0.4100 -0.0833 0.0453  0.0870  71   LEU B CB  
9186  C CG  . LEU B 73   ? 0.4304 0.7265 0.4275 -0.0931 0.0415  0.0921  71   LEU B CG  
9187  C CD1 . LEU B 73   ? 0.3628 0.6445 0.3576 -0.0981 0.0369  0.0923  71   LEU B CD1 
9188  C CD2 . LEU B 73   ? 0.4496 0.7443 0.4390 -0.0938 0.0432  0.0934  71   LEU B CD2 
9189  N N   . ILE B 74   ? 0.4099 0.7305 0.4225 -0.0647 0.0530  0.0795  72   ILE B N   
9190  C CA  . ILE B 74   ? 0.3618 0.6825 0.3763 -0.0554 0.0555  0.0742  72   ILE B CA  
9191  C C   . ILE B 74   ? 0.4289 0.7597 0.4436 -0.0483 0.0600  0.0726  72   ILE B C   
9192  O O   . ILE B 74   ? 0.4444 0.7723 0.4559 -0.0409 0.0627  0.0682  72   ILE B O   
9193  C CB  . ILE B 74   ? 0.4099 0.7323 0.4322 -0.0549 0.0536  0.0736  72   ILE B CB  
9194  C CG1 . ILE B 74   ? 0.3984 0.7085 0.4193 -0.0600 0.0496  0.0736  72   ILE B CG1 
9195  C CG2 . ILE B 74   ? 0.3474 0.6727 0.3727 -0.0450 0.0565  0.0687  72   ILE B CG2 
9196  C CD1 . ILE B 74   ? 0.3466 0.6579 0.3747 -0.0617 0.0469  0.0741  72   ILE B CD1 
9197  N N   . GLU B 75   ? 0.4563 0.7989 0.4745 -0.0503 0.0609  0.0761  73   GLU B N   
9198  C CA  . GLU B 75   ? 0.4474 0.7997 0.4653 -0.0441 0.0652  0.0750  73   GLU B CA  
9199  C C   . GLU B 75   ? 0.4634 0.8104 0.4723 -0.0429 0.0672  0.0739  73   GLU B C   
9200  O O   . GLU B 75   ? 0.4887 0.8359 0.4947 -0.0351 0.0705  0.0699  73   GLU B O   
9201  C CB  . GLU B 75   ? 0.3792 0.7449 0.4020 -0.0478 0.0654  0.0796  73   GLU B CB  
9202  N N   . ALA B 76   ? 0.4332 0.7747 0.4372 -0.0507 0.0650  0.0773  74   ALA B N   
9203  C CA  . ALA B 76   ? 0.4718 0.8072 0.4667 -0.0502 0.0664  0.0764  74   ALA B CA  
9204  C C   . ALA B 76   ? 0.4952 0.8198 0.4855 -0.0441 0.0669  0.0710  74   ALA B C   
9205  O O   . ALA B 76   ? 0.5000 0.8235 0.4849 -0.0382 0.0699  0.0679  74   ALA B O   
9206  C CB  . ALA B 76   ? 0.4533 0.7825 0.4438 -0.0599 0.0631  0.0810  74   ALA B CB  
9207  N N   . LEU B 77   ? 0.4665 0.7829 0.4588 -0.0455 0.0640  0.0698  75   LEU B N   
9208  C CA  . LEU B 77   ? 0.4788 0.7849 0.4671 -0.0403 0.0643  0.0648  75   LEU B CA  
9209  C C   . LEU B 77   ? 0.4535 0.7642 0.4438 -0.0301 0.0678  0.0599  75   LEU B C   
9210  O O   . LEU B 77   ? 0.4703 0.7758 0.4543 -0.0244 0.0697  0.0560  75   LEU B O   
9211  C CB  . LEU B 77   ? 0.4364 0.7345 0.4277 -0.0437 0.0607  0.0647  75   LEU B CB  
9212  C CG  . LEU B 77   ? 0.4515 0.7395 0.4378 -0.0521 0.0569  0.0677  75   LEU B CG  
9213  C CD1 . LEU B 77   ? 0.3694 0.6484 0.3605 -0.0551 0.0522  0.0672  75   LEU B CD1 
9214  C CD2 . LEU B 77   ? 0.4515 0.7252 0.4290 -0.0489 0.0559  0.0639  75   LEU B CD2 
9215  N N   . ARG B 78   ? 0.4455 0.7652 0.4440 -0.0276 0.0684  0.0601  76   ARG B N   
9216  C CA  . ARG B 78   ? 0.4438 0.7673 0.4445 -0.0180 0.0714  0.0557  76   ARG B CA  
9217  C C   . ARG B 78   ? 0.4564 0.7876 0.4540 -0.0138 0.0751  0.0554  76   ARG B C   
9218  O O   . ARG B 78   ? 0.4532 0.7854 0.4502 -0.0053 0.0777  0.0512  76   ARG B O   
9219  C CB  . ARG B 78   ? 0.4451 0.7755 0.4553 -0.0169 0.0706  0.0562  76   ARG B CB  
9220  C CG  . ARG B 78   ? 0.4499 0.7721 0.4630 -0.0187 0.0674  0.0551  76   ARG B CG  
9221  C CD  . ARG B 78   ? 0.4514 0.7804 0.4735 -0.0176 0.0665  0.0557  76   ARG B CD  
9222  N NE  . ARG B 78   ? 0.4547 0.7758 0.4789 -0.0149 0.0649  0.0524  76   ARG B NE  
9223  C CZ  . ARG B 78   ? 0.4573 0.7816 0.4887 -0.0138 0.0636  0.0524  76   ARG B CZ  
9224  N NH1 . ARG B 78   ? 0.4999 0.8351 0.5372 -0.0154 0.0635  0.0555  76   ARG B NH1 
9225  N NH2 . ARG B 78   ? 0.5145 0.8310 0.5472 -0.0110 0.0624  0.0491  76   ARG B NH2 
9226  N N   . GLY B 79   ? 0.4835 0.8197 0.4788 -0.0195 0.0754  0.0597  77   GLY B N   
9227  C CA  . GLY B 79   ? 0.4933 0.8361 0.4848 -0.0159 0.0790  0.0595  77   GLY B CA  
9228  C C   . GLY B 79   ? 0.5327 0.8663 0.5142 -0.0125 0.0803  0.0561  77   GLY B C   
9229  O O   . GLY B 79   ? 0.4646 0.8021 0.4424 -0.0072 0.0836  0.0543  77   GLY B O   
9230  N N   . LYS B 80   ? 0.5439 0.8654 0.5208 -0.0154 0.0777  0.0552  78   LYS B N   
9231  C CA  . LYS B 80   ? 0.5363 0.8480 0.5031 -0.0130 0.0783  0.0522  78   LYS B CA  
9232  C C   . LYS B 80   ? 0.6182 0.9203 0.5835 -0.0066 0.0778  0.0464  78   LYS B C   
9233  O O   . LYS B 80   ? 0.6501 0.9490 0.6103 0.0007  0.0799  0.0419  78   LYS B O   
9234  C CB  . LYS B 80   ? 0.5553 0.8599 0.5166 -0.0216 0.0754  0.0559  78   LYS B CB  
9235  C CG  . LYS B 80   ? 0.5391 0.8518 0.5037 -0.0295 0.0746  0.0621  78   LYS B CG  
9236  C CD  . LYS B 80   ? 0.5227 0.8269 0.4816 -0.0381 0.0713  0.0658  78   LYS B CD  
9237  C CE  . LYS B 80   ? 0.5313 0.8263 0.4923 -0.0420 0.0673  0.0658  78   LYS B CE  
9238  N NZ  . LYS B 80   ? 0.5231 0.8118 0.4806 -0.0515 0.0637  0.0706  78   LYS B NZ  
9239  N N   . GLY B 85   ? 0.5176 0.7101 0.4391 0.0266  0.0625  0.0054  83   GLY B N   
9240  C CA  . GLY B 85   ? 0.5616 0.7505 0.4752 0.0332  0.0641  0.0008  83   GLY B CA  
9241  C C   . GLY B 85   ? 0.5402 0.7195 0.4552 0.0391  0.0625  -0.0047 83   GLY B C   
9242  O O   . GLY B 85   ? 0.5074 0.6844 0.4168 0.0456  0.0642  -0.0089 83   GLY B O   
9243  N N   . VAL B 86   ? 0.5232 0.6966 0.4452 0.0367  0.0592  -0.0046 84   VAL B N   
9244  C CA  . VAL B 86   ? 0.5511 0.7157 0.4750 0.0417  0.0576  -0.0093 84   VAL B CA  
9245  C C   . VAL B 86   ? 0.5427 0.7168 0.4702 0.0481  0.0616  -0.0107 84   VAL B C   
9246  O O   . VAL B 86   ? 0.5277 0.6969 0.4517 0.0547  0.0622  -0.0153 84   VAL B O   
9247  C CB  . VAL B 86   ? 0.5599 0.7170 0.4906 0.0374  0.0534  -0.0085 84   VAL B CB  
9248  C CG1 . VAL B 86   ? 0.5599 0.7110 0.4942 0.0425  0.0525  -0.0125 84   VAL B CG1 
9249  C CG2 . VAL B 86   ? 0.5339 0.6791 0.4601 0.0331  0.0492  -0.0086 84   VAL B CG2 
9250  N N   . GLU B 87   ? 0.5545 0.7421 0.4886 0.0463  0.0642  -0.0067 85   GLU B N   
9251  C CA  . GLU B 87   ? 0.5072 0.7051 0.4453 0.0524  0.0680  -0.0076 85   GLU B CA  
9252  C C   . GLU B 87   ? 0.5393 0.7413 0.4697 0.0589  0.0719  -0.0102 85   GLU B C   
9253  O O   . GLU B 87   ? 0.5375 0.7399 0.4676 0.0662  0.0737  -0.0138 85   GLU B O   
9254  C CB  . GLU B 87   ? 0.6084 0.8214 0.5545 0.0485  0.0701  -0.0023 85   GLU B CB  
9255  N N   . GLY B 88   ? 0.5292 0.7340 0.4529 0.0563  0.0731  -0.0085 86   GLY B N   
9256  C CA  . GLY B 88   ? 0.4718 0.6800 0.3872 0.0623  0.0767  -0.0110 86   GLY B CA  
9257  C C   . GLY B 88   ? 0.4842 0.6774 0.3921 0.0675  0.0745  -0.0171 86   GLY B C   
9258  O O   . GLY B 88   ? 0.4403 0.6344 0.3436 0.0750  0.0772  -0.0209 86   GLY B O   
9259  N N   . LEU B 89   ? 0.4770 0.6560 0.3834 0.0635  0.0696  -0.0182 87   LEU B N   
9260  C CA  . LEU B 89   ? 0.4831 0.6473 0.3834 0.0677  0.0668  -0.0238 87   LEU B CA  
9261  C C   . LEU B 89   ? 0.3924 0.5537 0.2973 0.0735  0.0668  -0.0271 87   LEU B C   
9262  O O   . LEU B 89   ? 0.4156 0.5720 0.3149 0.0804  0.0677  -0.0318 87   LEU B O   
9263  C CB  . LEU B 89   ? 0.4786 0.6297 0.3779 0.0617  0.0614  -0.0236 87   LEU B CB  
9264  C CG  . LEU B 89   ? 0.5224 0.6590 0.4127 0.0638  0.0584  -0.0282 87   LEU B CG  
9265  C CD1 . LEU B 89   ? 0.5735 0.7009 0.4635 0.0569  0.0536  -0.0266 87   LEU B CD1 
9266  C CD2 . LEU B 89   ? 0.4843 0.6120 0.3752 0.0696  0.0570  -0.0332 87   LEU B CD2 
9267  N N   . VAL B 90   ? 0.4388 0.6028 0.3535 0.0709  0.0657  -0.0248 88   VAL B N   
9268  C CA  . VAL B 90   ? 0.4389 0.6008 0.3587 0.0759  0.0656  -0.0274 88   VAL B CA  
9269  C C   . VAL B 90   ? 0.4865 0.6584 0.4050 0.0836  0.0705  -0.0289 88   VAL B C   
9270  O O   . VAL B 90   ? 0.4598 0.6258 0.3759 0.0904  0.0705  -0.0333 88   VAL B O   
9271  C CB  . VAL B 90   ? 0.4029 0.5684 0.3335 0.0712  0.0641  -0.0238 88   VAL B CB  
9272  C CG1 . VAL B 90   ? 0.4069 0.5742 0.3432 0.0767  0.0650  -0.0256 88   VAL B CG1 
9273  C CG2 . VAL B 90   ? 0.4093 0.5621 0.3407 0.0654  0.0590  -0.0237 88   VAL B CG2 
9274  N N   . GLN B 91   ? 0.4841 0.6713 0.4038 0.0828  0.0745  -0.0253 89   GLN B N   
9275  C CA  . GLN B 91   ? 0.4223 0.6194 0.3420 0.0896  0.0788  -0.0262 89   GLN B CA  
9276  C C   . GLN B 91   ? 0.4611 0.6512 0.3703 0.0946  0.0795  -0.0302 89   GLN B C   
9277  O O   . GLN B 91   ? 0.4565 0.6439 0.3647 0.1012  0.0802  -0.0333 89   GLN B O   
9278  C CB  . GLN B 91   ? 0.5066 0.7197 0.4325 0.0855  0.0816  -0.0204 89   GLN B CB  
9279  N N   . GLU B 92   ? 0.4454 0.6322 0.3464 0.0915  0.0791  -0.0302 90   GLU B N   
9280  C CA  . GLU B 92   ? 0.4706 0.6507 0.3613 0.0958  0.0796  -0.0339 90   GLU B CA  
9281  C C   . GLU B 92   ? 0.4461 0.6111 0.3321 0.1014  0.0769  -0.0400 90   GLU B C   
9282  O O   . GLU B 92   ? 0.4196 0.5804 0.3006 0.1073  0.0777  -0.0434 90   GLU B O   
9283  C CB  . GLU B 92   ? 0.4524 0.6308 0.3350 0.0910  0.0790  -0.0327 90   GLU B CB  
9284  C CG  . GLU B 92   ? 0.5387 0.7125 0.4107 0.0948  0.0800  -0.0357 90   GLU B CG  
9285  C CD  . GLU B 92   ? 0.5502 0.7199 0.4133 0.0902  0.0787  -0.0349 90   GLU B CD  
9286  O OE1 . GLU B 92   ? 0.5632 0.7351 0.4290 0.0836  0.0772  -0.0313 90   GLU B OE1 
9287  O OE2 . GLU B 92   ? 0.5622 0.7260 0.4157 0.0930  0.0787  -0.0379 90   GLU B OE2 
9288  N N   . TYR B 93   ? 0.4183 0.5743 0.3060 0.0993  0.0734  -0.0413 91   TYR B N   
9289  C CA  . TYR B 93   ? 0.4315 0.5716 0.3150 0.1034  0.0700  -0.0466 91   TYR B CA  
9290  C C   . TYR B 93   ? 0.3993 0.5380 0.2908 0.1063  0.0692  -0.0475 91   TYR B C   
9291  O O   . TYR B 93   ? 0.4032 0.5282 0.2927 0.1084  0.0659  -0.0513 91   TYR B O   
9292  C CB  . TYR B 93   ? 0.3537 0.4801 0.2341 0.0973  0.0647  -0.0472 91   TYR B CB  
9293  C CG  . TYR B 93   ? 0.4009 0.5255 0.2708 0.0965  0.0651  -0.0479 91   TYR B CG  
9294  C CD1 . TYR B 93   ? 0.3876 0.5030 0.2469 0.1021  0.0647  -0.0531 91   TYR B CD1 
9295  C CD2 . TYR B 93   ? 0.4358 0.5681 0.3059 0.0903  0.0659  -0.0433 91   TYR B CD2 
9296  C CE1 . TYR B 93   ? 0.4422 0.5561 0.2914 0.1015  0.0651  -0.0538 91   TYR B CE1 
9297  C CE2 . TYR B 93   ? 0.4731 0.6040 0.3333 0.0896  0.0663  -0.0438 91   TYR B CE2 
9298  C CZ  . TYR B 93   ? 0.4464 0.5682 0.2962 0.0953  0.0659  -0.0491 91   TYR B CZ  
9299  O OH  . TYR B 93   ? 0.4753 0.5956 0.3147 0.0947  0.0662  -0.0496 91   TYR B OH  
9300  N N   . SER B 94   ? 0.3709 0.5231 0.2713 0.1062  0.0721  -0.0439 92   SER B N   
9301  C CA  . SER B 94   ? 0.3556 0.5077 0.2641 0.1090  0.0715  -0.0442 92   SER B CA  
9302  C C   . SER B 94   ? 0.3754 0.5147 0.2870 0.1052  0.0666  -0.0450 92   SER B C   
9303  O O   . SER B 94   ? 0.3893 0.5193 0.3011 0.1091  0.0646  -0.0483 92   SER B O   
9304  C CB  . SER B 94   ? 0.3919 0.5390 0.2975 0.1166  0.0720  -0.0479 92   SER B CB  
9305  O OG  . SER B 94   ? 0.4556 0.6111 0.3586 0.1188  0.0753  -0.0469 92   SER B OG  
9306  N N   . LEU B 95   ? 0.3421 0.4806 0.2565 0.0970  0.0642  -0.0417 93   LEU B N   
9307  C CA  . LEU B 95   ? 0.3256 0.4521 0.2433 0.0925  0.0593  -0.0420 93   LEU B CA  
9308  C C   . LEU B 95   ? 0.3404 0.4716 0.2687 0.0910  0.0589  -0.0394 93   LEU B C   
9309  O O   . LEU B 95   ? 0.3350 0.4795 0.2695 0.0890  0.0615  -0.0354 93   LEU B O   
9310  C CB  . LEU B 95   ? 0.2991 0.4225 0.2155 0.0846  0.0567  -0.0396 93   LEU B CB  
9311  C CG  . LEU B 95   ? 0.3681 0.4865 0.2739 0.0847  0.0565  -0.0415 93   LEU B CG  
9312  C CD1 . LEU B 95   ? 0.3269 0.4412 0.2328 0.0768  0.0532  -0.0389 93   LEU B CD1 
9313  C CD2 . LEU B 95   ? 0.3706 0.4757 0.2689 0.0901  0.0546  -0.0472 93   LEU B CD2 
9314  N N   . SER B 96   ? 0.2851 0.4054 0.2155 0.0917  0.0557  -0.0416 94   SER B N   
9315  C CA  . SER B 96   ? 0.2822 0.4041 0.2221 0.0885  0.0543  -0.0390 94   SER B CA  
9316  C C   . SER B 96   ? 0.2844 0.4063 0.2275 0.0800  0.0520  -0.0355 94   SER B C   
9317  O O   . SER B 96   ? 0.3094 0.4273 0.2471 0.0768  0.0508  -0.0356 94   SER B O   
9318  C CB  . SER B 96   ? 0.2869 0.3960 0.2272 0.0911  0.0512  -0.0423 94   SER B CB  
9319  O OG  . SER B 96   ? 0.2923 0.3886 0.2289 0.0872  0.0472  -0.0439 94   SER B OG  
9320  N N   . SER B 97   ? 0.2590 0.3849 0.2107 0.0763  0.0512  -0.0324 95   SER B N   
9321  C CA  . SER B 97   ? 0.2882 0.4130 0.2430 0.0685  0.0487  -0.0292 95   SER B CA  
9322  C C   . SER B 97   ? 0.2979 0.4078 0.2492 0.0662  0.0445  -0.0317 95   SER B C   
9323  O O   . SER B 97   ? 0.2613 0.3685 0.2099 0.0615  0.0429  -0.0305 95   SER B O   
9324  C CB  . SER B 97   ? 0.2982 0.4285 0.2624 0.0656  0.0484  -0.0260 95   SER B CB  
9325  O OG  . SER B 97   ? 0.3352 0.4802 0.3029 0.0666  0.0520  -0.0232 95   SER B OG  
9326  N N   . GLN B 98   ? 0.2615 0.3620 0.2128 0.0695  0.0427  -0.0348 96   GLN B N   
9327  C CA  . GLN B 98   ? 0.2808 0.3678 0.2292 0.0673  0.0386  -0.0371 96   GLN B CA  
9328  C C   . GLN B 98   ? 0.3136 0.3954 0.2527 0.0685  0.0383  -0.0396 96   GLN B C   
9329  O O   . GLN B 98   ? 0.2522 0.3267 0.1889 0.0646  0.0353  -0.0399 96   GLN B O   
9330  C CB  . GLN B 98   ? 0.2550 0.3336 0.2051 0.0707  0.0369  -0.0399 96   GLN B CB  
9331  C CG  . GLN B 98   ? 0.2812 0.3614 0.2401 0.0681  0.0359  -0.0375 96   GLN B CG  
9332  C CD  . GLN B 98   ? 0.3161 0.3926 0.2779 0.0613  0.0330  -0.0355 96   GLN B CD  
9333  O OE1 . GLN B 98   ? 0.3231 0.4065 0.2871 0.0571  0.0336  -0.0323 96   GLN B OE1 
9334  N NE2 . GLN B 98   ? 0.2824 0.3482 0.2445 0.0602  0.0297  -0.0373 96   GLN B NE2 
9335  N N   . GLU B 99   ? 0.2707 0.3564 0.2046 0.0740  0.0413  -0.0415 97   GLU B N   
9336  C CA  . GLU B 99   ? 0.3176 0.3991 0.2421 0.0752  0.0412  -0.0438 97   GLU B CA  
9337  C C   . GLU B 99   ? 0.3162 0.4039 0.2397 0.0699  0.0417  -0.0404 97   GLU B C   
9338  O O   . GLU B 99   ? 0.2898 0.3707 0.2078 0.0673  0.0394  -0.0412 97   GLU B O   
9339  C CB  . GLU B 99   ? 0.2816 0.3664 0.2005 0.0826  0.0446  -0.0465 97   GLU B CB  
9340  C CG  . GLU B 99   ? 0.2820 0.3563 0.1985 0.0879  0.0430  -0.0509 97   GLU B CG  
9341  C CD  . GLU B 99   ? 0.3133 0.3919 0.2260 0.0959  0.0466  -0.0533 97   GLU B CD  
9342  O OE1 . GLU B 99   ? 0.2918 0.3827 0.2042 0.0973  0.0506  -0.0515 97   GLU B OE1 
9343  O OE2 . GLU B 99   ? 0.3228 0.3925 0.2329 0.1007  0.0454  -0.0570 97   GLU B OE2 
9344  N N   . GLY B 100  ? 0.2773 0.3775 0.2060 0.0679  0.0445  -0.0364 98   GLY B N   
9345  C CA  . GLY B 100  ? 0.2874 0.3932 0.2154 0.0624  0.0448  -0.0327 98   GLY B CA  
9346  C C   . GLY B 100  ? 0.2764 0.3742 0.2066 0.0561  0.0405  -0.0315 98   GLY B C   
9347  O O   . GLY B 100  ? 0.2702 0.3648 0.1956 0.0528  0.0390  -0.0308 98   GLY B O   
9348  N N   . VAL B 101  ? 0.2686 0.3632 0.2059 0.0546  0.0385  -0.0311 99   VAL B N   
9349  C CA  . VAL B 101  ? 0.2634 0.3503 0.2031 0.0492  0.0345  -0.0301 99   VAL B CA  
9350  C C   . VAL B 101  ? 0.3162 0.3910 0.2497 0.0500  0.0313  -0.0337 99   VAL B C   
9351  O O   . VAL B 101  ? 0.2737 0.3441 0.2048 0.0459  0.0288  -0.0328 99   VAL B O   
9352  C CB  . VAL B 101  ? 0.2447 0.3307 0.1928 0.0483  0.0333  -0.0294 99   VAL B CB  
9353  C CG1 . VAL B 101  ? 0.2572 0.3345 0.2073 0.0436  0.0292  -0.0291 99   VAL B CG1 
9354  C CG2 . VAL B 101  ? 0.2529 0.3509 0.2071 0.0465  0.0358  -0.0255 99   VAL B CG2 
9355  N N   . ALA B 102  ? 0.2870 0.3559 0.2176 0.0551  0.0312  -0.0376 100  ALA B N   
9356  C CA  . ALA B 102  ? 0.2668 0.3239 0.1915 0.0556  0.0279  -0.0410 100  ALA B CA  
9357  C C   . ALA B 102  ? 0.2986 0.3556 0.2148 0.0554  0.0282  -0.0415 100  ALA B C   
9358  O O   . ALA B 102  ? 0.3109 0.3601 0.2235 0.0527  0.0248  -0.0423 100  ALA B O   
9359  C CB  . ALA B 102  ? 0.2828 0.3337 0.2054 0.0613  0.0279  -0.0451 100  ALA B CB  
9360  N N   . LEU B 103  ? 0.2664 0.3320 0.1791 0.0581  0.0321  -0.0409 101  LEU B N   
9361  C CA  . LEU B 103  ? 0.3237 0.3898 0.2279 0.0579  0.0327  -0.0411 101  LEU B CA  
9362  C C   . LEU B 103  ? 0.2994 0.3670 0.2047 0.0513  0.0309  -0.0374 101  LEU B C   
9363  O O   . LEU B 103  ? 0.2793 0.3411 0.1784 0.0495  0.0286  -0.0380 101  LEU B O   
9364  C CB  . LEU B 103  ? 0.2824 0.3592 0.1835 0.0620  0.0376  -0.0407 101  LEU B CB  
9365  C CG  . LEU B 103  ? 0.2987 0.3782 0.1911 0.0617  0.0390  -0.0403 101  LEU B CG  
9366  C CD1 . LEU B 103  ? 0.3150 0.3831 0.1980 0.0642  0.0365  -0.0448 101  LEU B CD1 
9367  C CD2 . LEU B 103  ? 0.3254 0.4173 0.2167 0.0656  0.0444  -0.0394 101  LEU B CD2 
9368  N N   . MET B 104  ? 0.2954 0.3704 0.2082 0.0477  0.0319  -0.0334 102  MET B N   
9369  C CA  . MET B 104  ? 0.3076 0.3836 0.2213 0.0415  0.0302  -0.0297 102  MET B CA  
9370  C C   . MET B 104  ? 0.3359 0.4009 0.2505 0.0385  0.0253  -0.0306 102  MET B C   
9371  O O   . MET B 104  ? 0.3201 0.3818 0.2313 0.0349  0.0230  -0.0294 102  MET B O   
9372  C CB  . MET B 104  ? 0.2893 0.3751 0.2106 0.0384  0.0321  -0.0254 102  MET B CB  
9373  C CG  . MET B 104  ? 0.3330 0.4311 0.2535 0.0409  0.0370  -0.0239 102  MET B CG  
9374  S SD  . MET B 104  ? 0.4266 0.5280 0.3368 0.0410  0.0388  -0.0233 102  MET B SD  
9375  C CE  . MET B 104  ? 0.4570 0.5594 0.3688 0.0328  0.0366  -0.0182 102  MET B CE  
9376  N N   . CYS B 105  ? 0.2882 0.3475 0.2075 0.0399  0.0236  -0.0328 103  CYS B N   
9377  C CA  . CYS B 105  ? 0.2952 0.3443 0.2154 0.0376  0.0191  -0.0341 103  CYS B CA  
9378  C C   . CYS B 105  ? 0.3116 0.3531 0.2233 0.0389  0.0169  -0.0370 103  CYS B C   
9379  O O   . CYS B 105  ? 0.2807 0.3170 0.1907 0.0356  0.0136  -0.0365 103  CYS B O   
9380  C CB  . CYS B 105  ? 0.2571 0.3022 0.1833 0.0394  0.0181  -0.0359 103  CYS B CB  
9381  S SG  . CYS B 105  ? 0.3061 0.3582 0.2425 0.0369  0.0194  -0.0324 103  CYS B SG  
9382  N N   . LEU B 106  ? 0.3002 0.3407 0.2062 0.0439  0.0187  -0.0403 104  LEU B N   
9383  C CA  . LEU B 106  ? 0.2780 0.3113 0.1750 0.0453  0.0167  -0.0432 104  LEU B CA  
9384  C C   . LEU B 106  ? 0.3457 0.3824 0.2371 0.0426  0.0170  -0.0409 104  LEU B C   
9385  O O   . LEU B 106  ? 0.3358 0.3659 0.2227 0.0405  0.0136  -0.0415 104  LEU B O   
9386  C CB  . LEU B 106  ? 0.3180 0.3501 0.2094 0.0515  0.0189  -0.0470 104  LEU B CB  
9387  C CG  . LEU B 106  ? 0.3338 0.3594 0.2145 0.0533  0.0174  -0.0501 104  LEU B CG  
9388  C CD1 . LEU B 106  ? 0.3537 0.3675 0.2338 0.0520  0.0124  -0.0526 104  LEU B CD1 
9389  C CD2 . LEU B 106  ? 0.3398 0.3671 0.2136 0.0596  0.0208  -0.0532 104  LEU B CD2 
9390  N N   . ALA B 107  ? 0.3265 0.3736 0.2182 0.0425  0.0210  -0.0380 105  ALA B N   
9391  C CA  . ALA B 107  ? 0.3364 0.3873 0.2228 0.0396  0.0215  -0.0353 105  ALA B CA  
9392  C C   . ALA B 107  ? 0.3379 0.3854 0.2274 0.0338  0.0178  -0.0324 105  ALA B C   
9393  O O   . ALA B 107  ? 0.3754 0.4188 0.2590 0.0317  0.0154  -0.0321 105  ALA B O   
9394  C CB  . ALA B 107  ? 0.3501 0.4136 0.2377 0.0400  0.0264  -0.0323 105  ALA B CB  
9395  N N   . GLU B 108  ? 0.3480 0.3968 0.2465 0.0313  0.0171  -0.0304 106  GLU B N   
9396  C CA  . GLU B 108  ? 0.3794 0.4242 0.2812 0.0262  0.0134  -0.0281 106  GLU B CA  
9397  C C   . GLU B 108  ? 0.3808 0.4151 0.2795 0.0261  0.0089  -0.0308 106  GLU B C   
9398  O O   . GLU B 108  ? 0.4375 0.4686 0.3326 0.0232  0.0063  -0.0294 106  GLU B O   
9399  C CB  . GLU B 108  ? 0.4029 0.4497 0.3147 0.0246  0.0133  -0.0265 106  GLU B CB  
9400  C CG  . GLU B 108  ? 0.3894 0.4301 0.3051 0.0205  0.0091  -0.0252 106  GLU B CG  
9401  C CD  . GLU B 108  ? 0.4470 0.4886 0.3719 0.0196  0.0090  -0.0245 106  GLU B CD  
9402  O OE1 . GLU B 108  ? 0.4395 0.4873 0.3679 0.0214  0.0122  -0.0242 106  GLU B OE1 
9403  O OE2 . GLU B 108  ? 0.5324 0.5688 0.4611 0.0173  0.0057  -0.0242 106  GLU B OE2 
9404  N N   . ALA B 109  ? 0.3748 0.4036 0.2745 0.0292  0.0079  -0.0345 107  ALA B N   
9405  C CA  . ALA B 109  ? 0.3917 0.4108 0.2887 0.0290  0.0035  -0.0371 107  ALA B CA  
9406  C C   . ALA B 109  ? 0.4241 0.4405 0.3107 0.0297  0.0027  -0.0383 107  ALA B C   
9407  O O   . ALA B 109  ? 0.4033 0.4140 0.2873 0.0273  -0.0012 -0.0383 107  ALA B O   
9408  C CB  . ALA B 109  ? 0.3913 0.4053 0.2905 0.0322  0.0028  -0.0408 107  ALA B CB  
9409  N N   . LEU B 110  ? 0.3692 0.3897 0.2497 0.0330  0.0062  -0.0394 108  LEU B N   
9410  C CA  . LEU B 110  ? 0.4179 0.4359 0.2879 0.0340  0.0057  -0.0407 108  LEU B CA  
9411  C C   . LEU B 110  ? 0.4486 0.4697 0.3160 0.0298  0.0051  -0.0367 108  LEU B C   
9412  O O   . LEU B 110  ? 0.4717 0.4885 0.3317 0.0290  0.0027  -0.0373 108  LEU B O   
9413  C CB  . LEU B 110  ? 0.3839 0.4064 0.2480 0.0389  0.0100  -0.0427 108  LEU B CB  
9414  C CG  . LEU B 110  ? 0.3708 0.3879 0.2340 0.0437  0.0100  -0.0474 108  LEU B CG  
9415  C CD1 . LEU B 110  ? 0.3785 0.4020 0.2372 0.0489  0.0150  -0.0487 108  LEU B CD1 
9416  C CD2 . LEU B 110  ? 0.4383 0.4443 0.2948 0.0441  0.0055  -0.0509 108  LEU B CD2 
9417  N N   . LEU B 111  ? 0.4236 0.4519 0.2969 0.0270  0.0070  -0.0327 109  LEU B N   
9418  C CA  . LEU B 111  ? 0.5040 0.5346 0.3754 0.0226  0.0062  -0.0286 109  LEU B CA  
9419  C C   . LEU B 111  ? 0.4910 0.5146 0.3655 0.0190  0.0011  -0.0276 109  LEU B C   
9420  O O   . LEU B 111  ? 0.4555 0.4789 0.3274 0.0156  -0.0005 -0.0246 109  LEU B O   
9421  C CB  . LEU B 111  ? 0.4711 0.5116 0.3475 0.0207  0.0099  -0.0246 109  LEU B CB  
9422  C CG  . LEU B 111  ? 0.4655 0.5143 0.3374 0.0240  0.0150  -0.0248 109  LEU B CG  
9423  C CD1 . LEU B 111  ? 0.4937 0.5528 0.3722 0.0226  0.0186  -0.0213 109  LEU B CD1 
9424  C CD2 . LEU B 111  ? 0.5112 0.5607 0.3729 0.0233  0.0154  -0.0238 109  LEU B CD2 
9425  N N   . ARG B 112  ? 0.4623 0.4802 0.3423 0.0198  -0.0015 -0.0300 110  ARG B N   
9426  C CA  . ARG B 112  ? 0.4967 0.5075 0.3785 0.0171  -0.0065 -0.0298 110  ARG B CA  
9427  C C   . ARG B 112  ? 0.5366 0.5410 0.4098 0.0177  -0.0096 -0.0319 110  ARG B C   
9428  O O   . ARG B 112  ? 0.5263 0.5258 0.3997 0.0152  -0.0139 -0.0312 110  ARG B O   
9429  C CB  . ARG B 112  ? 0.4455 0.4528 0.3357 0.0177  -0.0081 -0.0317 110  ARG B CB  
9430  C CG  . ARG B 112  ? 0.4915 0.5045 0.3903 0.0172  -0.0054 -0.0298 110  ARG B CG  
9431  C CD  . ARG B 112  ? 0.5274 0.5363 0.4340 0.0174  -0.0075 -0.0314 110  ARG B CD  
9432  N NE  . ARG B 112  ? 0.5782 0.5921 0.4919 0.0181  -0.0045 -0.0308 110  ARG B NE  
9433  C CZ  . ARG B 112  ? 0.6152 0.6284 0.5317 0.0210  -0.0033 -0.0334 110  ARG B CZ  
9434  N NH1 . ARG B 112  ? 0.6468 0.6541 0.5597 0.0235  -0.0049 -0.0369 110  ARG B NH1 
9435  N NH2 . ARG B 112  ? 0.5592 0.5772 0.4820 0.0214  -0.0007 -0.0323 110  ARG B NH2 
9436  N N   . ILE B 113  ? 0.4978 0.5022 0.3634 0.0209  -0.0078 -0.0346 111  ILE B N   
9437  C CA  . ILE B 113  ? 0.5295 0.5284 0.3856 0.0214  -0.0104 -0.0364 111  ILE B CA  
9438  C C   . ILE B 113  ? 0.5828 0.5860 0.4325 0.0194  -0.0092 -0.0329 111  ILE B C   
9439  O O   . ILE B 113  ? 0.6000 0.6097 0.4460 0.0209  -0.0047 -0.0322 111  ILE B O   
9440  C CB  . ILE B 113  ? 0.5432 0.5396 0.3931 0.0261  -0.0090 -0.0409 111  ILE B CB  
9441  C CG1 . ILE B 113  ? 0.5323 0.5241 0.3885 0.0278  -0.0104 -0.0440 111  ILE B CG1 
9442  C CG2 . ILE B 113  ? 0.5021 0.4929 0.3413 0.0265  -0.0118 -0.0427 111  ILE B CG2 
9443  C CD1 . ILE B 113  ? 0.5277 0.5167 0.3784 0.0325  -0.0089 -0.0484 111  ILE B CD1 
9444  N N   . PRO B 114  ? 0.6000 0.5997 0.4481 0.0159  -0.0130 -0.0307 112  PRO B N   
9445  C CA  . PRO B 114  ? 0.5750 0.5789 0.4183 0.0132  -0.0118 -0.0265 112  PRO B CA  
9446  C C   . PRO B 114  ? 0.5159 0.5208 0.3476 0.0150  -0.0102 -0.0275 112  PRO B C   
9447  O O   . PRO B 114  ? 0.6312 0.6426 0.4594 0.0139  -0.0069 -0.0244 112  PRO B O   
9448  C CB  . PRO B 114  ? 0.5275 0.5259 0.3724 0.0097  -0.0171 -0.0245 112  PRO B CB  
9449  C CG  . PRO B 114  ? 0.5816 0.5757 0.4350 0.0101  -0.0198 -0.0266 112  PRO B CG  
9450  C CD  . PRO B 114  ? 0.5638 0.5565 0.4160 0.0141  -0.0184 -0.0312 112  PRO B CD  
9451  N N   . ASP B 115  ? 0.5564 0.5550 0.3818 0.0175  -0.0124 -0.0315 113  ASP B N   
9452  C CA  . ASP B 115  ? 0.6360 0.6346 0.4494 0.0192  -0.0113 -0.0325 113  ASP B CA  
9453  C C   . ASP B 115  ? 0.6293 0.6329 0.4399 0.0236  -0.0060 -0.0350 113  ASP B C   
9454  O O   . ASP B 115  ? 0.6172 0.6182 0.4308 0.0268  -0.0058 -0.0388 113  ASP B O   
9455  C CB  . ASP B 115  ? 0.5751 0.5643 0.3821 0.0198  -0.0164 -0.0357 113  ASP B CB  
9456  C CG  . ASP B 115  ? 0.6741 0.6625 0.4685 0.0227  -0.0149 -0.0381 113  ASP B CG  
9457  O OD1 . ASP B 115  ? 0.7235 0.7164 0.5112 0.0216  -0.0128 -0.0353 113  ASP B OD1 
9458  O OD2 . ASP B 115  ? 0.6853 0.6683 0.4760 0.0260  -0.0159 -0.0429 113  ASP B OD2 
9459  N N   . THR B 116  ? 0.5878 0.5987 0.3927 0.0238  -0.0018 -0.0328 114  THR B N   
9460  C CA  . THR B 116  ? 0.6647 0.6821 0.4673 0.0283  0.0036  -0.0347 114  THR B CA  
9461  C C   . THR B 116  ? 0.6702 0.6809 0.4656 0.0331  0.0028  -0.0405 114  THR B C   
9462  O O   . THR B 116  ? 0.6397 0.6510 0.4378 0.0372  0.0051  -0.0436 114  THR B O   
9463  C CB  . THR B 116  ? 0.6699 0.6960 0.4662 0.0275  0.0079  -0.0313 114  THR B CB  
9464  O OG1 . THR B 116  ? 0.7113 0.7429 0.5141 0.0225  0.0082  -0.0258 114  THR B OG1 
9465  C CG2 . THR B 116  ? 0.6801 0.7141 0.4751 0.0322  0.0138  -0.0330 114  THR B CG2 
9466  N N   . ALA B 117  ? 0.6917 0.6953 0.4778 0.0327  -0.0008 -0.0420 115  ALA B N   
9467  C CA  . ALA B 117  ? 0.6536 0.6504 0.4315 0.0372  -0.0018 -0.0475 115  ALA B CA  
9468  C C   . ALA B 117  ? 0.6327 0.6217 0.4169 0.0383  -0.0052 -0.0511 115  ALA B C   
9469  O O   . ALA B 117  ? 0.6192 0.6050 0.4006 0.0428  -0.0042 -0.0555 115  ALA B O   
9470  C CB  . ALA B 117  ? 0.7145 0.7055 0.4809 0.0360  -0.0052 -0.0480 115  ALA B CB  
9471  N N   . THR B 118  ? 0.5824 0.5681 0.3750 0.0344  -0.0093 -0.0493 116  THR B N   
9472  C CA  . THR B 118  ? 0.5992 0.5786 0.3988 0.0350  -0.0123 -0.0522 116  THR B CA  
9473  C C   . THR B 118  ? 0.5865 0.5710 0.3938 0.0376  -0.0080 -0.0527 116  THR B C   
9474  O O   . THR B 118  ? 0.5454 0.5254 0.3534 0.0409  -0.0083 -0.0566 116  THR B O   
9475  C CB  . THR B 118  ? 0.5985 0.5749 0.4060 0.0303  -0.0170 -0.0497 116  THR B CB  
9476  O OG1 . THR B 118  ? 0.6868 0.6580 0.4872 0.0281  -0.0214 -0.0493 116  THR B OG1 
9477  C CG2 . THR B 118  ? 0.5116 0.4823 0.3266 0.0308  -0.0198 -0.0524 116  THR B CG2 
9478  N N   . ARG B 119  ? 0.5612 0.5550 0.3745 0.0361  -0.0043 -0.0487 117  ARG B N   
9479  C CA  . ARG B 119  ? 0.5864 0.5860 0.4071 0.0385  -0.0002 -0.0488 117  ARG B CA  
9480  C C   . ARG B 119  ? 0.5445 0.5461 0.3582 0.0442  0.0039  -0.0521 117  ARG B C   
9481  O O   . ARG B 119  ? 0.5325 0.5324 0.3492 0.0477  0.0049  -0.0551 117  ARG B O   
9482  C CB  . ARG B 119  ? 0.5675 0.5769 0.3947 0.0354  0.0028  -0.0435 117  ARG B CB  
9483  C CG  . ARG B 119  ? 0.4765 0.4923 0.3125 0.0371  0.0066  -0.0431 117  ARG B CG  
9484  C CD  . ARG B 119  ? 0.5045 0.5310 0.3444 0.0345  0.0102  -0.0381 117  ARG B CD  
9485  N NE  . ARG B 119  ? 0.5822 0.6076 0.4236 0.0290  0.0072  -0.0343 117  ARG B NE  
9486  C CZ  . ARG B 119  ? 0.6110 0.6407 0.4473 0.0264  0.0082  -0.0309 117  ARG B CZ  
9487  N NH1 . ARG B 119  ? 0.6280 0.6643 0.4576 0.0286  0.0124  -0.0306 117  ARG B NH1 
9488  N NH2 . ARG B 119  ? 0.6693 0.6967 0.5071 0.0216  0.0049  -0.0275 117  ARG B NH2 
9489  N N   . ASP B 120  ? 0.6002 0.6053 0.4043 0.0453  0.0062  -0.0517 118  ASP B N   
9490  C CA  . ASP B 120  ? 0.5861 0.5936 0.3827 0.0511  0.0103  -0.0549 118  ASP B CA  
9491  C C   . ASP B 120  ? 0.6082 0.6046 0.3990 0.0548  0.0073  -0.0607 118  ASP B C   
9492  O O   . ASP B 120  ? 0.5973 0.5937 0.3865 0.0601  0.0100  -0.0640 118  ASP B O   
9493  C CB  . ASP B 120  ? 0.6099 0.6227 0.3965 0.0511  0.0129  -0.0532 118  ASP B CB  
9494  C CG  . ASP B 120  ? 0.6864 0.7115 0.4782 0.0482  0.0168  -0.0476 118  ASP B CG  
9495  O OD1 . ASP B 120  ? 0.6619 0.6916 0.4646 0.0468  0.0180  -0.0454 118  ASP B OD1 
9496  O OD2 . ASP B 120  ? 0.6646 0.6943 0.4492 0.0470  0.0186  -0.0452 118  ASP B OD2 
9497  N N   . ALA B 121  ? 0.5853 0.5721 0.3728 0.0522  0.0017  -0.0619 119  ALA B N   
9498  C CA  . ALA B 121  ? 0.6176 0.5934 0.3997 0.0552  -0.0017 -0.0673 119  ALA B CA  
9499  C C   . ALA B 121  ? 0.6302 0.6024 0.4217 0.0560  -0.0027 -0.0690 119  ALA B C   
9500  O O   . ALA B 121  ? 0.6410 0.6082 0.4292 0.0606  -0.0023 -0.0732 119  ALA B O   
9501  C CB  . ALA B 121  ? 0.6047 0.5717 0.3814 0.0518  -0.0077 -0.0679 119  ALA B CB  
9502  N N   . LEU B 122  ? 0.5533 0.5278 0.3562 0.0518  -0.0041 -0.0657 120  LEU B N   
9503  C CA  . LEU B 122  ? 0.5709 0.5426 0.3829 0.0524  -0.0050 -0.0669 120  LEU B CA  
9504  C C   . LEU B 122  ? 0.5799 0.5575 0.3939 0.0572  0.0004  -0.0677 120  LEU B C   
9505  O O   . LEU B 122  ? 0.5678 0.5404 0.3834 0.0602  0.0000  -0.0709 120  LEU B O   
9506  C CB  . LEU B 122  ? 0.5915 0.5659 0.4151 0.0472  -0.0068 -0.0628 120  LEU B CB  
9507  C CG  . LEU B 122  ? 0.5468 0.5186 0.3801 0.0473  -0.0078 -0.0637 120  LEU B CG  
9508  C CD1 . LEU B 122  ? 0.5959 0.5562 0.4272 0.0471  -0.0131 -0.0673 120  LEU B CD1 
9509  C CD2 . LEU B 122  ? 0.5611 0.5384 0.4060 0.0431  -0.0078 -0.0593 120  LEU B CD2 
9510  N N   . ILE B 123  ? 0.5210 0.5094 0.3351 0.0578  0.0053  -0.0648 121  ILE B N   
9511  C CA  . ILE B 123  ? 0.5771 0.5725 0.3932 0.0625  0.0106  -0.0654 121  ILE B CA  
9512  C C   . ILE B 123  ? 0.6091 0.5992 0.4152 0.0688  0.0116  -0.0706 121  ILE B C   
9513  O O   . ILE B 123  ? 0.5846 0.5719 0.3927 0.0728  0.0124  -0.0733 121  ILE B O   
9514  C CB  . ILE B 123  ? 0.4849 0.4935 0.3026 0.0614  0.0154  -0.0609 121  ILE B CB  
9515  C CG1 . ILE B 123  ? 0.4427 0.4561 0.2711 0.0557  0.0145  -0.0560 121  ILE B CG1 
9516  C CG2 . ILE B 123  ? 0.4739 0.4903 0.2920 0.0670  0.0210  -0.0618 121  ILE B CG2 
9517  C CD1 . ILE B 123  ? 0.4583 0.4834 0.2876 0.0534  0.0183  -0.0513 121  ILE B CD1 
9518  N N   . ARG B 124  ? 0.5647 0.5526 0.3593 0.0698  0.0114  -0.0720 122  ARG B N   
9519  C CA  . ARG B 124  ? 0.6640 0.6477 0.4479 0.0762  0.0129  -0.0769 122  ARG B CA  
9520  C C   . ARG B 124  ? 0.6722 0.6415 0.4524 0.0775  0.0079  -0.0818 122  ARG B C   
9521  O O   . ARG B 124  ? 0.7425 0.7070 0.5157 0.0833  0.0090  -0.0862 122  ARG B O   
9522  C CB  . ARG B 124  ? 0.6608 0.6469 0.4331 0.0767  0.0142  -0.0768 122  ARG B CB  
9523  N N   . ASP B 125  ? 0.6719 0.6344 0.4566 0.0724  0.0025  -0.0811 123  ASP B N   
9524  C CA  . ASP B 125  ? 0.6948 0.6437 0.4754 0.0728  -0.0028 -0.0854 123  ASP B CA  
9525  C C   . ASP B 125  ? 0.6774 0.6221 0.4686 0.0710  -0.0053 -0.0853 123  ASP B C   
9526  O O   . ASP B 125  ? 0.7753 0.7089 0.5637 0.0717  -0.0093 -0.0889 123  ASP B O   
9527  C CB  . ASP B 125  ? 0.7603 0.7033 0.5350 0.0685  -0.0078 -0.0852 123  ASP B CB  
9528  C CG  . ASP B 125  ? 0.7667 0.7128 0.5298 0.0702  -0.0057 -0.0855 123  ASP B CG  
9529  O OD1 . ASP B 125  ? 0.7346 0.6809 0.4894 0.0760  -0.0023 -0.0886 123  ASP B OD1 
9530  O OD2 . ASP B 125  ? 0.7931 0.7415 0.5550 0.0660  -0.0073 -0.0825 123  ASP B OD2 
9531  N N   . LYS B 126  ? 0.6298 0.5827 0.4327 0.0687  -0.0032 -0.0813 124  LYS B N   
9532  C CA  . LYS B 126  ? 0.6268 0.5762 0.4397 0.0669  -0.0055 -0.0810 124  LYS B CA  
9533  C C   . LYS B 126  ? 0.6748 0.6331 0.4965 0.0689  -0.0007 -0.0789 124  LYS B C   
9534  O O   . LYS B 126  ? 0.6940 0.6486 0.5184 0.0718  -0.0005 -0.0810 124  LYS B O   
9535  C CB  . LYS B 126  ? 0.6735 0.6218 0.4932 0.0603  -0.0098 -0.0781 124  LYS B CB  
9536  N N   . ILE B 127  ? 0.6069 0.5767 0.4331 0.0671  0.0028  -0.0747 125  ILE B N   
9537  C CA  . ILE B 127  ? 0.5731 0.5518 0.4086 0.0681  0.0068  -0.0722 125  ILE B CA  
9538  C C   . ILE B 127  ? 0.5901 0.5719 0.4211 0.0750  0.0113  -0.0747 125  ILE B C   
9539  O O   . ILE B 127  ? 0.5691 0.5510 0.4052 0.0778  0.0126  -0.0755 125  ILE B O   
9540  C CB  . ILE B 127  ? 0.5456 0.5354 0.3868 0.0640  0.0090  -0.0670 125  ILE B CB  
9541  C CG1 . ILE B 127  ? 0.5336 0.5197 0.3769 0.0579  0.0044  -0.0649 125  ILE B CG1 
9542  C CG2 . ILE B 127  ? 0.5078 0.5054 0.3599 0.0640  0.0119  -0.0643 125  ILE B CG2 
9543  C CD1 . ILE B 127  ? 0.5648 0.5443 0.4158 0.0552  0.0004  -0.0651 125  ILE B CD1 
9544  N N   . ALA B 128  ? 0.5537 0.5382 0.3750 0.0780  0.0137  -0.0759 126  ALA B N   
9545  C CA  . ALA B 128  ? 0.5466 0.5359 0.3639 0.0848  0.0186  -0.0778 126  ALA B CA  
9546  C C   . ALA B 128  ? 0.6266 0.6054 0.4400 0.0899  0.0171  -0.0829 126  ALA B C   
9547  O O   . ALA B 128  ? 0.6045 0.5868 0.4179 0.0956  0.0207  -0.0843 126  ALA B O   
9548  C CB  . ALA B 128  ? 0.5729 0.5670 0.3799 0.0868  0.0214  -0.0782 126  ALA B CB  
9549  N N   . ASP B 129  ? 0.6910 0.6568 0.5008 0.0881  0.0116  -0.0857 127  ASP B N   
9550  C CA  . ASP B 129  ? 0.7410 0.6952 0.5473 0.0920  0.0094  -0.0903 127  ASP B CA  
9551  C C   . ASP B 129  ? 0.7473 0.6993 0.5647 0.0899  0.0076  -0.0890 127  ASP B C   
9552  O O   . ASP B 129  ? 0.7790 0.7202 0.5946 0.0917  0.0047  -0.0923 127  ASP B O   
9553  C CB  . ASP B 129  ? 0.6978 0.6390 0.4944 0.0907  0.0041  -0.0939 127  ASP B CB  
9554  N N   . GLY B 130  ? 0.7091 0.6709 0.5375 0.0861  0.0093  -0.0843 128  GLY B N   
9555  C CA  . GLY B 130  ? 0.6832 0.6446 0.5221 0.0845  0.0084  -0.0827 128  GLY B CA  
9556  C C   . GLY B 130  ? 0.7473 0.7033 0.5921 0.0779  0.0035  -0.0812 128  GLY B C   
9557  O O   . GLY B 130  ? 0.7140 0.6733 0.5690 0.0753  0.0035  -0.0784 128  GLY B O   
9558  N N   . ASN B 131  ? 0.8181 0.7664 0.6569 0.0753  -0.0006 -0.0827 129  ASN B N   
9559  C CA  . ASN B 131  ? 0.8135 0.7570 0.6579 0.0693  -0.0055 -0.0813 129  ASN B CA  
9560  C C   . ASN B 131  ? 0.8097 0.7628 0.6616 0.0644  -0.0045 -0.0764 129  ASN B C   
9561  O O   . ASN B 131  ? 0.8583 0.8108 0.7079 0.0607  -0.0069 -0.0754 129  ASN B O   
9562  C CB  . ASN B 131  ? 0.8352 0.7680 0.6707 0.0679  -0.0103 -0.0843 129  ASN B CB  
9563  N N   . TRP B 132  ? 0.7278 0.6896 0.5885 0.0643  -0.0012 -0.0734 130  TRP B N   
9564  C CA  . TRP B 132  ? 0.6847 0.6553 0.5523 0.0597  -0.0003 -0.0688 130  TRP B CA  
9565  C C   . TRP B 132  ? 0.7034 0.6714 0.5800 0.0548  -0.0037 -0.0669 130  TRP B C   
9566  O O   . TRP B 132  ? 0.7387 0.7100 0.6187 0.0504  -0.0050 -0.0640 130  TRP B O   
9567  C CB  . TRP B 132  ? 0.6491 0.6312 0.5212 0.0617  0.0051  -0.0662 130  TRP B CB  
9568  C CG  . TRP B 132  ? 0.5465 0.5298 0.4258 0.0639  0.0067  -0.0662 130  TRP B CG  
9569  C CD1 . TRP B 132  ? 0.5433 0.5261 0.4200 0.0696  0.0091  -0.0687 130  TRP B CD1 
9570  C CD2 . TRP B 132  ? 0.5098 0.4952 0.3997 0.0605  0.0059  -0.0635 130  TRP B CD2 
9571  N NE1 . TRP B 132  ? 0.4839 0.4683 0.3691 0.0699  0.0098  -0.0675 130  TRP B NE1 
9572  C CE2 . TRP B 132  ? 0.4658 0.4518 0.3590 0.0642  0.0079  -0.0644 130  TRP B CE2 
9573  C CE3 . TRP B 132  ? 0.4873 0.4739 0.3838 0.0549  0.0037  -0.0604 130  TRP B CE3 
9574  C CZ2 . TRP B 132  ? 0.3875 0.3753 0.2902 0.0623  0.0077  -0.0623 130  TRP B CZ2 
9575  C CZ3 . TRP B 132  ? 0.4828 0.4713 0.3888 0.0532  0.0037  -0.0585 130  TRP B CZ3 
9576  C CH2 . TRP B 132  ? 0.4337 0.4229 0.3427 0.0568  0.0057  -0.0594 130  TRP B CH2 
9577  N N   . LYS B 133  ? 0.7460 0.7083 0.6264 0.0556  -0.0053 -0.0685 131  LYS B N   
9578  C CA  . LYS B 133  ? 0.7412 0.7021 0.6307 0.0512  -0.0080 -0.0665 131  LYS B CA  
9579  C C   . LYS B 133  ? 0.8349 0.7905 0.7229 0.0470  -0.0127 -0.0665 131  LYS B C   
9580  O O   . LYS B 133  ? 0.8316 0.7907 0.7257 0.0428  -0.0139 -0.0635 131  LYS B O   
9581  C CB  . LYS B 133  ? 0.7143 0.6692 0.6068 0.0529  -0.0089 -0.0683 131  LYS B CB  
9582  N N   . SER B 134  ? 0.8818 0.8289 0.7614 0.0481  -0.0156 -0.0700 132  SER B N   
9583  C CA  . SER B 134  ? 0.8736 0.8152 0.7519 0.0442  -0.0206 -0.0703 132  SER B CA  
9584  C C   . SER B 134  ? 0.8933 0.8402 0.7697 0.0418  -0.0205 -0.0678 132  SER B C   
9585  O O   . SER B 134  ? 0.8150 0.7632 0.6969 0.0376  -0.0230 -0.0654 132  SER B O   
9586  C CB  . SER B 134  ? 0.8101 0.7412 0.6790 0.0461  -0.0237 -0.0746 132  SER B CB  
9587  N N   . HIS B 135  ? 0.8800 0.8303 0.7489 0.0445  -0.0176 -0.0683 133  HIS B N   
9588  C CA  . HIS B 135  ? 0.8326 0.7864 0.6976 0.0424  -0.0179 -0.0663 133  HIS B CA  
9589  C C   . HIS B 135  ? 0.8254 0.7885 0.6982 0.0396  -0.0157 -0.0617 133  HIS B C   
9590  O O   . HIS B 135  ? 0.7744 0.7401 0.6450 0.0371  -0.0165 -0.0596 133  HIS B O   
9591  C CB  . HIS B 135  ? 0.8102 0.7650 0.6644 0.0463  -0.0152 -0.0682 133  HIS B CB  
9592  N N   . LEU B 136  ? 0.8104 0.7782 0.6916 0.0398  -0.0132 -0.0601 134  LEU B N   
9593  C CA  . LEU B 136  ? 0.7487 0.7245 0.6372 0.0369  -0.0115 -0.0558 134  LEU B CA  
9594  C C   . LEU B 136  ? 0.7591 0.7352 0.6580 0.0352  -0.0122 -0.0546 134  LEU B C   
9595  O O   . LEU B 136  ? 0.7794 0.7612 0.6850 0.0328  -0.0111 -0.0513 134  LEU B O   
9596  C CB  . LEU B 136  ? 0.6562 0.6407 0.5433 0.0392  -0.0063 -0.0543 134  LEU B CB  
9597  C CG  . LEU B 136  ? 0.6505 0.6375 0.5283 0.0401  -0.0049 -0.0542 134  LEU B CG  
9598  C CD1 . LEU B 136  ? 0.5619 0.5577 0.4393 0.0429  0.0006  -0.0530 134  LEU B CD1 
9599  C CD2 . LEU B 136  ? 0.6139 0.6021 0.4915 0.0357  -0.0070 -0.0512 134  LEU B CD2 
9600  N N   . ARG B 140  ? 0.6438 0.6260 0.5820 0.0221  -0.0177 -0.0450 138  ARG B N   
9601  C CA  . ARG B 140  ? 0.6045 0.5922 0.5483 0.0226  -0.0143 -0.0432 138  ARG B CA  
9602  C C   . ARG B 140  ? 0.6105 0.6010 0.5504 0.0261  -0.0105 -0.0442 138  ARG B C   
9603  O O   . ARG B 140  ? 0.5538 0.5431 0.4861 0.0279  -0.0101 -0.0458 138  ARG B O   
9604  C CB  . ARG B 140  ? 0.5958 0.5888 0.5428 0.0201  -0.0136 -0.0398 138  ARG B CB  
9605  C CG  . ARG B 140  ? 0.6324 0.6284 0.5731 0.0199  -0.0124 -0.0385 138  ARG B CG  
9606  C CD  . ARG B 140  ? 0.6344 0.6351 0.5787 0.0172  -0.0117 -0.0350 138  ARG B CD  
9607  N NE  . ARG B 140  ? 0.7421 0.7466 0.6807 0.0170  -0.0099 -0.0333 138  ARG B NE  
9608  C CZ  . ARG B 140  ? 0.7350 0.7438 0.6751 0.0147  -0.0090 -0.0301 138  ARG B CZ  
9609  N NH1 . ARG B 140  ? 0.6590 0.6685 0.6057 0.0127  -0.0097 -0.0284 138  ARG B NH1 
9610  N NH2 . ARG B 140  ? 0.7469 0.7590 0.6814 0.0143  -0.0074 -0.0286 138  ARG B NH2 
9611  N N   . SER B 141  ? 0.5142 0.5086 0.4592 0.0271  -0.0078 -0.0433 139  SER B N   
9612  C CA  . SER B 141  ? 0.4726 0.4703 0.4149 0.0306  -0.0042 -0.0441 139  SER B CA  
9613  C C   . SER B 141  ? 0.4589 0.4619 0.3960 0.0310  -0.0020 -0.0429 139  SER B C   
9614  O O   . SER B 141  ? 0.4388 0.4454 0.3771 0.0281  -0.0021 -0.0402 139  SER B O   
9615  C CB  . SER B 141  ? 0.4407 0.4429 0.3902 0.0310  -0.0019 -0.0426 139  SER B CB  
9616  O OG  . SER B 141  ? 0.4375 0.4440 0.3852 0.0345  0.0017  -0.0431 139  SER B OG  
9617  N N   . LEU B 142  ? 0.4562 0.4594 0.3870 0.0347  0.0000  -0.0449 140  LEU B N   
9618  C CA  . LEU B 142  ? 0.3637 0.3734 0.2900 0.0355  0.0030  -0.0436 140  LEU B CA  
9619  C C   . LEU B 142  ? 0.3470 0.3657 0.2791 0.0346  0.0061  -0.0403 140  LEU B C   
9620  O O   . LEU B 142  ? 0.3131 0.3380 0.2430 0.0337  0.0082  -0.0381 140  LEU B O   
9621  C CB  . LEU B 142  ? 0.3491 0.3579 0.2684 0.0403  0.0050  -0.0466 140  LEU B CB  
9622  C CG  . LEU B 142  ? 0.4044 0.4149 0.3151 0.0410  0.0059  -0.0468 140  LEU B CG  
9623  C CD1 . LEU B 142  ? 0.4807 0.4835 0.3869 0.0390  0.0017  -0.0481 140  LEU B CD1 
9624  C CD2 . LEU B 142  ? 0.4708 0.4820 0.3757 0.0464  0.0087  -0.0496 140  LEU B CD2 
9625  N N   . PHE B 143  ? 0.3177 0.3371 0.2569 0.0347  0.0065  -0.0399 141  PHE B N   
9626  C CA  . PHE B 143  ? 0.2980 0.3257 0.2423 0.0347  0.0097  -0.0374 141  PHE B CA  
9627  C C   . PHE B 143  ? 0.3294 0.3588 0.2804 0.0303  0.0084  -0.0344 141  PHE B C   
9628  O O   . PHE B 143  ? 0.2923 0.3271 0.2487 0.0300  0.0103  -0.0325 141  PHE B O   
9629  C CB  . PHE B 143  ? 0.2944 0.3221 0.2411 0.0386  0.0114  -0.0391 141  PHE B CB  
9630  C CG  . PHE B 143  ? 0.2609 0.2857 0.2007 0.0432  0.0123  -0.0424 141  PHE B CG  
9631  C CD1 . PHE B 143  ? 0.2554 0.2855 0.1896 0.0452  0.0150  -0.0423 141  PHE B CD1 
9632  C CD2 . PHE B 143  ? 0.2741 0.2907 0.2126 0.0456  0.0104  -0.0456 141  PHE B CD2 
9633  C CE1 . PHE B 143  ? 0.2997 0.3269 0.2269 0.0499  0.0159  -0.0456 141  PHE B CE1 
9634  C CE2 . PHE B 143  ? 0.2549 0.2679 0.1864 0.0500  0.0110  -0.0489 141  PHE B CE2 
9635  C CZ  . PHE B 143  ? 0.2884 0.3067 0.2142 0.0523  0.0138  -0.0490 141  PHE B CZ  
9636  N N   . VAL B 144  ? 0.3216 0.3465 0.2721 0.0272  0.0053  -0.0339 142  VAL B N   
9637  C CA  . VAL B 144  ? 0.3454 0.3711 0.3018 0.0234  0.0039  -0.0313 142  VAL B CA  
9638  C C   . VAL B 144  ? 0.3489 0.3826 0.3068 0.0216  0.0063  -0.0280 142  VAL B C   
9639  O O   . VAL B 144  ? 0.3689 0.4051 0.3326 0.0198  0.0065  -0.0260 142  VAL B O   
9640  C CB  . VAL B 144  ? 0.3674 0.3874 0.3222 0.0208  0.0001  -0.0314 142  VAL B CB  
9641  C CG1 . VAL B 144  ? 0.4542 0.4670 0.4091 0.0221  -0.0024 -0.0344 142  VAL B CG1 
9642  C CG2 . VAL B 144  ? 0.4560 0.4765 0.4036 0.0203  0.0000  -0.0309 142  VAL B CG2 
9643  N N   . ASN B 145  ? 0.3036 0.3414 0.2562 0.0220  0.0081  -0.0271 143  ASN B N   
9644  C CA  . ASN B 145  ? 0.3627 0.4083 0.3164 0.0199  0.0103  -0.0237 143  ASN B CA  
9645  C C   . ASN B 145  ? 0.3549 0.4081 0.3091 0.0228  0.0142  -0.0236 143  ASN B C   
9646  O O   . ASN B 145  ? 0.2906 0.3513 0.2440 0.0217  0.0165  -0.0211 143  ASN B O   
9647  C CB  . ASN B 145  ? 0.3735 0.4195 0.3212 0.0176  0.0097  -0.0221 143  ASN B CB  
9648  C CG  . ASN B 145  ? 0.4410 0.4811 0.3892 0.0142  0.0059  -0.0212 143  ASN B CG  
9649  O OD1 . ASN B 145  ? 0.5315 0.5706 0.4853 0.0122  0.0046  -0.0200 143  ASN B OD1 
9650  N ND2 . ASN B 145  ? 0.4252 0.4612 0.3674 0.0138  0.0040  -0.0218 143  ASN B ND2 
9651  N N   . ALA B 146  ? 0.2876 0.3393 0.2434 0.0266  0.0150  -0.0262 144  ALA B N   
9652  C CA  . ALA B 146  ? 0.2946 0.3534 0.2507 0.0301  0.0187  -0.0264 144  ALA B CA  
9653  C C   . ALA B 146  ? 0.2668 0.3337 0.2290 0.0282  0.0205  -0.0232 144  ALA B C   
9654  O O   . ALA B 146  ? 0.3014 0.3767 0.2636 0.0300  0.0237  -0.0221 144  ALA B O   
9655  C CB  . ALA B 146  ? 0.2861 0.3403 0.2423 0.0346  0.0187  -0.0299 144  ALA B CB  
9656  N N   . ALA B 147  ? 0.2995 0.3645 0.2669 0.0248  0.0185  -0.0216 145  ALA B N   
9657  C CA  . ALA B 147  ? 0.3342 0.4067 0.3069 0.0228  0.0200  -0.0185 145  ALA B CA  
9658  C C   . ALA B 147  ? 0.3341 0.4134 0.3044 0.0199  0.0213  -0.0154 145  ALA B C   
9659  O O   . ALA B 147  ? 0.3171 0.4055 0.2898 0.0198  0.0239  -0.0132 145  ALA B O   
9660  C CB  . ALA B 147  ? 0.3123 0.3807 0.2902 0.0196  0.0175  -0.0176 145  ALA B CB  
9661  N N   . THR B 148  ? 0.3250 0.4005 0.2908 0.0175  0.0196  -0.0149 146  THR B N   
9662  C CA  . THR B 148  ? 0.3232 0.4044 0.2859 0.0146  0.0207  -0.0118 146  THR B CA  
9663  C C   . THR B 148  ? 0.3317 0.4204 0.2909 0.0179  0.0243  -0.0122 146  THR B C   
9664  O O   . THR B 148  ? 0.3142 0.4122 0.2745 0.0166  0.0268  -0.0093 146  THR B O   
9665  C CB  . THR B 148  ? 0.4045 0.4790 0.3624 0.0117  0.0178  -0.0115 146  THR B CB  
9666  O OG1 . THR B 148  ? 0.4393 0.5082 0.4010 0.0087  0.0147  -0.0108 146  THR B OG1 
9667  C CG2 . THR B 148  ? 0.4128 0.4931 0.3668 0.0087  0.0190  -0.0082 146  THR B CG2 
9668  N N   . TRP B 149  ? 0.3141 0.3988 0.2688 0.0222  0.0247  -0.0157 147  TRP B N   
9669  C CA  . TRP B 149  ? 0.3067 0.3982 0.2577 0.0260  0.0282  -0.0164 147  TRP B CA  
9670  C C   . TRP B 149  ? 0.2777 0.3768 0.2339 0.0291  0.0311  -0.0163 147  TRP B C   
9671  O O   . TRP B 149  ? 0.3266 0.4351 0.2819 0.0308  0.0345  -0.0151 147  TRP B O   
9672  C CB  . TRP B 149  ? 0.2992 0.3836 0.2436 0.0299  0.0276  -0.0204 147  TRP B CB  
9673  C CG  . TRP B 149  ? 0.3506 0.4295 0.2890 0.0273  0.0253  -0.0202 147  TRP B CG  
9674  C CD1 . TRP B 149  ? 0.3273 0.3958 0.2638 0.0265  0.0215  -0.0223 147  TRP B CD1 
9675  C CD2 . TRP B 149  ? 0.3389 0.4227 0.2725 0.0248  0.0264  -0.0176 147  TRP B CD2 
9676  N NE1 . TRP B 149  ? 0.2925 0.3590 0.2231 0.0240  0.0202  -0.0212 147  TRP B NE1 
9677  C CE2 . TRP B 149  ? 0.3516 0.4270 0.2802 0.0228  0.0231  -0.0183 147  TRP B CE2 
9678  C CE3 . TRP B 149  ? 0.3809 0.4756 0.3140 0.0240  0.0298  -0.0145 147  TRP B CE3 
9679  C CZ2 . TRP B 149  ? 0.3740 0.4510 0.2967 0.0201  0.0231  -0.0161 147  TRP B CZ2 
9680  C CZ3 . TRP B 149  ? 0.3829 0.4794 0.3103 0.0210  0.0299  -0.0122 147  TRP B CZ3 
9681  C CH2 . TRP B 149  ? 0.3930 0.4805 0.3151 0.0192  0.0266  -0.0131 147  TRP B CH2 
9682  N N   . GLY B 150  ? 0.2859 0.3811 0.2475 0.0299  0.0298  -0.0175 148  GLY B N   
9683  C CA  . GLY B 150  ? 0.2961 0.3985 0.2631 0.0323  0.0321  -0.0169 148  GLY B CA  
9684  C C   . GLY B 150  ? 0.3458 0.4588 0.3167 0.0287  0.0337  -0.0126 148  GLY B C   
9685  O O   . GLY B 150  ? 0.3230 0.4458 0.2957 0.0310  0.0369  -0.0115 148  GLY B O   
9686  N N   . LEU B 151  ? 0.3423 0.4533 0.3143 0.0230  0.0315  -0.0100 149  LEU B N   
9687  C CA  . LEU B 151  ? 0.3744 0.4946 0.3492 0.0188  0.0326  -0.0056 149  LEU B CA  
9688  C C   . LEU B 151  ? 0.3521 0.4807 0.3225 0.0193  0.0356  -0.0042 149  LEU B C   
9689  O O   . LEU B 151  ? 0.3708 0.5106 0.3440 0.0194  0.0384  -0.0018 149  LEU B O   
9690  C CB  . LEU B 151  ? 0.3768 0.4915 0.3520 0.0128  0.0293  -0.0035 149  LEU B CB  
9691  C CG  . LEU B 151  ? 0.5080 0.6255 0.4895 0.0091  0.0283  -0.0008 149  LEU B CG  
9692  C CD1 . LEU B 151  ? 0.5066 0.6187 0.4868 0.0034  0.0253  0.0014  149  LEU B CD1 
9693  C CD2 . LEU B 151  ? 0.4243 0.5547 0.4090 0.0087  0.0313  0.0021  149  LEU B CD2 
9694  N N   . VAL B 152  ? 0.3504 0.4740 0.3139 0.0196  0.0350  -0.0055 150  VAL B N   
9695  C CA  . VAL B 152  ? 0.3707 0.5017 0.3291 0.0197  0.0378  -0.0040 150  VAL B CA  
9696  C C   . VAL B 152  ? 0.3550 0.4944 0.3136 0.0256  0.0418  -0.0055 150  VAL B C   
9697  O O   . VAL B 152  ? 0.3970 0.5479 0.3557 0.0253  0.0450  -0.0028 150  VAL B O   
9698  C CB  . VAL B 152  ? 0.3708 0.4934 0.3213 0.0195  0.0360  -0.0057 150  VAL B CB  
9699  C CG1 . VAL B 152  ? 0.3825 0.5120 0.3268 0.0215  0.0393  -0.0053 150  VAL B CG1 
9700  C CG2 . VAL B 152  ? 0.3691 0.4861 0.3192 0.0133  0.0326  -0.0031 150  VAL B CG2 
9701  N N   . VAL B 153  ? 0.3458 0.4799 0.3044 0.0310  0.0417  -0.0095 151  VAL B N   
9702  C CA  . VAL B 153  ? 0.3383 0.4786 0.2957 0.0374  0.0453  -0.0116 151  VAL B CA  
9703  C C   . VAL B 153  ? 0.3304 0.4801 0.2954 0.0390  0.0473  -0.0101 151  VAL B C   
9704  O O   . VAL B 153  ? 0.3052 0.4659 0.2707 0.0420  0.0510  -0.0092 151  VAL B O   
9705  C CB  . VAL B 153  ? 0.3445 0.4737 0.2975 0.0426  0.0440  -0.0167 151  VAL B CB  
9706  C CG1 . VAL B 153  ? 0.3551 0.4895 0.3074 0.0498  0.0473  -0.0192 151  VAL B CG1 
9707  C CG2 . VAL B 153  ? 0.3080 0.4296 0.2529 0.0415  0.0423  -0.0182 151  VAL B CG2 
9708  N N   . THR B 154  ? 0.3466 0.4925 0.3176 0.0371  0.0450  -0.0098 152  THR B N   
9709  C CA  . THR B 154  ? 0.3467 0.4998 0.3247 0.0391  0.0464  -0.0088 152  THR B CA  
9710  C C   . THR B 154  ? 0.3379 0.4973 0.3221 0.0331  0.0456  -0.0044 152  THR B C   
9711  O O   . THR B 154  ? 0.3858 0.5535 0.3759 0.0342  0.0470  -0.0030 152  THR B O   
9712  C CB  . THR B 154  ? 0.3603 0.5040 0.3403 0.0425  0.0444  -0.0122 152  THR B CB  
9713  O OG1 . THR B 154  ? 0.3499 0.4860 0.3328 0.0376  0.0408  -0.0114 152  THR B OG1 
9714  C CG2 . THR B 154  ? 0.4109 0.5453 0.3842 0.0473  0.0440  -0.0167 152  THR B CG2 
9715  N N   . GLY B 155  ? 0.3211 0.4762 0.3041 0.0270  0.0431  -0.0024 153  GLY B N   
9716  C CA  . GLY B 155  ? 0.3350 0.4938 0.3233 0.0212  0.0418  0.0014  153  GLY B CA  
9717  C C   . GLY B 155  ? 0.4148 0.5667 0.4078 0.0205  0.0390  0.0005  153  GLY B C   
9718  O O   . GLY B 155  ? 0.4495 0.6043 0.4471 0.0161  0.0378  0.0034  153  GLY B O   
9719  N N   . LYS B 156  ? 0.3412 0.4840 0.3332 0.0246  0.0379  -0.0034 154  LYS B N   
9720  C CA  . LYS B 156  ? 0.3592 0.4955 0.3554 0.0244  0.0356  -0.0045 154  LYS B CA  
9721  C C   . LYS B 156  ? 0.3808 0.5043 0.3739 0.0227  0.0323  -0.0064 154  LYS B C   
9722  O O   . LYS B 156  ? 0.3422 0.4606 0.3299 0.0246  0.0322  -0.0087 154  LYS B O   
9723  C CB  . LYS B 156  ? 0.3735 0.5102 0.3718 0.0305  0.0369  -0.0071 154  LYS B CB  
9724  N N   . LEU B 157  ? 0.3705 0.4893 0.3669 0.0191  0.0297  -0.0055 155  LEU B N   
9725  C CA  . LEU B 157  ? 0.4027 0.5102 0.3971 0.0174  0.0266  -0.0071 155  LEU B CA  
9726  C C   . LEU B 157  ? 0.4590 0.5604 0.4567 0.0197  0.0253  -0.0094 155  LEU B C   
9727  O O   . LEU B 157  ? 0.4898 0.5944 0.4924 0.0192  0.0254  -0.0082 155  LEU B O   
9728  C CB  . LEU B 157  ? 0.4722 0.5783 0.4671 0.0114  0.0244  -0.0043 155  LEU B CB  
9729  C CG  . LEU B 157  ? 0.5373 0.6325 0.5308 0.0095  0.0211  -0.0056 155  LEU B CG  
9730  C CD1 . LEU B 157  ? 0.4600 0.5498 0.4476 0.0108  0.0205  -0.0076 155  LEU B CD1 
9731  C CD2 . LEU B 157  ? 0.5713 0.6656 0.5658 0.0040  0.0191  -0.0027 155  LEU B CD2 
9732  N N   . THR B 158  ? 0.4264 0.5193 0.4213 0.0220  0.0241  -0.0126 156  THR B N   
9733  C CA  . THR B 158  ? 0.4127 0.4983 0.4102 0.0232  0.0223  -0.0146 156  THR B CA  
9734  C C   . THR B 158  ? 0.3878 0.4648 0.3838 0.0203  0.0193  -0.0152 156  THR B C   
9735  O O   . THR B 158  ? 0.3804 0.4556 0.3722 0.0187  0.0186  -0.0150 156  THR B O   
9736  C CB  . THR B 158  ? 0.4259 0.5086 0.4218 0.0286  0.0232  -0.0178 156  THR B CB  
9737  O OG1 . THR B 158  ? 0.4356 0.5130 0.4257 0.0296  0.0225  -0.0199 156  THR B OG1 
9738  C CG2 . THR B 158  ? 0.4400 0.5315 0.4367 0.0321  0.0263  -0.0173 156  THR B CG2 
9739  N N   . SER B 159  ? 0.3566 0.4285 0.3560 0.0195  0.0175  -0.0158 157  SER B N   
9740  C CA  . SER B 159  ? 0.3466 0.4110 0.3451 0.0170  0.0146  -0.0163 157  SER B CA  
9741  C C   . SER B 159  ? 0.3698 0.4271 0.3653 0.0194  0.0135  -0.0194 157  SER B C   
9742  O O   . SER B 159  ? 0.3839 0.4362 0.3770 0.0177  0.0114  -0.0199 157  SER B O   
9743  C CB  . SER B 159  ? 0.3649 0.4270 0.3680 0.0149  0.0132  -0.0155 157  SER B CB  
9744  O OG  . SER B 159  ? 0.4513 0.5114 0.4572 0.0177  0.0135  -0.0172 157  SER B OG  
9745  N N   . THR B 160  ? 0.3423 0.3989 0.3378 0.0232  0.0145  -0.0214 158  THR B N   
9746  C CA  . THR B 160  ? 0.3124 0.3621 0.3045 0.0256  0.0134  -0.0244 158  THR B CA  
9747  C C   . THR B 160  ? 0.2930 0.3454 0.2813 0.0296  0.0156  -0.0258 158  THR B C   
9748  O O   . THR B 160  ? 0.3030 0.3628 0.2924 0.0310  0.0181  -0.0246 158  THR B O   
9749  C CB  . THR B 160  ? 0.3131 0.3570 0.3085 0.0262  0.0119  -0.0258 158  THR B CB  
9750  O OG1 . THR B 160  ? 0.2796 0.3267 0.2779 0.0286  0.0137  -0.0257 158  THR B OG1 
9751  C CG2 . THR B 160  ? 0.3512 0.3930 0.3503 0.0225  0.0099  -0.0245 158  THR B CG2 
9752  N N   . VAL B 161  ? 0.2606 0.3070 0.2444 0.0317  0.0146  -0.0286 159  VAL B N   
9753  C CA  . VAL B 161  ? 0.3015 0.3498 0.2805 0.0357  0.0166  -0.0302 159  VAL B CA  
9754  C C   . VAL B 161  ? 0.2966 0.3383 0.2744 0.0394  0.0160  -0.0333 159  VAL B C   
9755  O O   . VAL B 161  ? 0.2568 0.2911 0.2353 0.0383  0.0133  -0.0346 159  VAL B O   
9756  C CB  . VAL B 161  ? 0.3611 0.4085 0.3338 0.0349  0.0162  -0.0306 159  VAL B CB  
9757  C CG1 . VAL B 161  ? 0.3730 0.4252 0.3469 0.0305  0.0162  -0.0274 159  VAL B CG1 
9758  C CG2 . VAL B 161  ? 0.3208 0.3587 0.2903 0.0346  0.0132  -0.0331 159  VAL B CG2 
9759  N N   . ASN B 162  ? 0.2723 0.3171 0.2484 0.0438  0.0183  -0.0343 160  ASN B N   
9760  C CA  . ASN B 162  ? 0.2833 0.3215 0.2573 0.0478  0.0178  -0.0374 160  ASN B CA  
9761  C C   . ASN B 162  ? 0.2383 0.2709 0.2048 0.0494  0.0168  -0.0401 160  ASN B C   
9762  O O   . ASN B 162  ? 0.2359 0.2713 0.1975 0.0527  0.0189  -0.0412 160  ASN B O   
9763  C CB  . ASN B 162  ? 0.2653 0.3089 0.2407 0.0523  0.0206  -0.0373 160  ASN B CB  
9764  C CG  . ASN B 162  ? 0.3089 0.3449 0.2823 0.0564  0.0197  -0.0403 160  ASN B CG  
9765  O OD1 . ASN B 162  ? 0.2800 0.3072 0.2490 0.0566  0.0175  -0.0428 160  ASN B OD1 
9766  N ND2 . ASN B 162  ? 0.3114 0.3505 0.2877 0.0596  0.0213  -0.0400 160  ASN B ND2 
9767  N N   . ASP B 163  ? 0.2398 0.2644 0.2052 0.0468  0.0136  -0.0412 161  ASP B N   
9768  C CA  . ASP B 163  ? 0.2623 0.2813 0.2206 0.0475  0.0121  -0.0437 161  ASP B CA  
9769  C C   . ASP B 163  ? 0.2286 0.2413 0.1819 0.0523  0.0120  -0.0472 161  ASP B C   
9770  O O   . ASP B 163  ? 0.2528 0.2624 0.1990 0.0541  0.0117  -0.0494 161  ASP B O   
9771  C CB  . ASP B 163  ? 0.2705 0.2835 0.2295 0.0432  0.0084  -0.0436 161  ASP B CB  
9772  C CG  . ASP B 163  ? 0.3061 0.3139 0.2703 0.0419  0.0064  -0.0438 161  ASP B CG  
9773  O OD1 . ASP B 163  ? 0.2548 0.2664 0.2246 0.0418  0.0077  -0.0421 161  ASP B OD1 
9774  O OD2 . ASP B 163  ? 0.3371 0.3373 0.2997 0.0408  0.0033  -0.0455 161  ASP B OD2 
9775  N N   . ARG B 164  ? 0.2446 0.2548 0.2009 0.0544  0.0120  -0.0478 162  ARG B N   
9776  C CA  . ARG B 164  ? 0.2306 0.2349 0.1817 0.0594  0.0121  -0.0511 162  ARG B CA  
9777  C C   . ARG B 164  ? 0.2394 0.2508 0.1873 0.0642  0.0158  -0.0515 162  ARG B C   
9778  O O   . ARG B 164  ? 0.2381 0.2457 0.1789 0.0682  0.0162  -0.0544 162  ARG B O   
9779  C CB  . ARG B 164  ? 0.2471 0.2465 0.2021 0.0604  0.0110  -0.0515 162  ARG B CB  
9780  C CG  . ARG B 164  ? 0.2795 0.2716 0.2374 0.0560  0.0073  -0.0514 162  ARG B CG  
9781  C CD  . ARG B 164  ? 0.3899 0.3747 0.3419 0.0545  0.0044  -0.0536 162  ARG B CD  
9782  N NE  . ARG B 164  ? 0.4344 0.4136 0.3784 0.0591  0.0044  -0.0571 162  ARG B NE  
9783  C CZ  . ARG B 164  ? 0.4709 0.4461 0.4080 0.0592  0.0031  -0.0592 162  ARG B CZ  
9784  N NH1 . ARG B 164  ? 0.4758 0.4520 0.4131 0.0550  0.0014  -0.0581 162  ARG B NH1 
9785  N NH2 . ARG B 164  ? 0.4412 0.4111 0.3707 0.0638  0.0032  -0.0624 162  ARG B NH2 
9786  N N   . SER B 165  ? 0.2583 0.2799 0.2115 0.0639  0.0186  -0.0485 163  SER B N   
9787  C CA  . SER B 165  ? 0.2427 0.2729 0.1939 0.0680  0.0224  -0.0483 163  SER B CA  
9788  C C   . SER B 165  ? 0.2291 0.2620 0.1743 0.0675  0.0233  -0.0486 163  SER B C   
9789  O O   . SER B 165  ? 0.2367 0.2713 0.1761 0.0720  0.0254  -0.0505 163  SER B O   
9790  C CB  . SER B 165  ? 0.2188 0.2599 0.1776 0.0667  0.0247  -0.0447 163  SER B CB  
9791  O OG  . SER B 165  ? 0.2624 0.3134 0.2197 0.0696  0.0283  -0.0439 163  SER B OG  
9792  N N   . LEU B 166  ? 0.2499 0.2832 0.1962 0.0621  0.0217  -0.0468 164  LEU B N   
9793  C CA  . LEU B 166  ? 0.2312 0.2668 0.1718 0.0610  0.0222  -0.0466 164  LEU B CA  
9794  C C   . LEU B 166  ? 0.2387 0.2647 0.1709 0.0632  0.0203  -0.0505 164  LEU B C   
9795  O O   . LEU B 166  ? 0.2533 0.2812 0.1787 0.0656  0.0219  -0.0517 164  LEU B O   
9796  C CB  . LEU B 166  ? 0.2432 0.2805 0.1873 0.0547  0.0206  -0.0436 164  LEU B CB  
9797  C CG  . LEU B 166  ? 0.2509 0.2988 0.2015 0.0525  0.0229  -0.0397 164  LEU B CG  
9798  C CD1 . LEU B 166  ? 0.2704 0.3177 0.2244 0.0466  0.0207  -0.0372 164  LEU B CD1 
9799  C CD2 . LEU B 166  ? 0.2408 0.2982 0.1882 0.0546  0.0266  -0.0387 164  LEU B CD2 
9800  N N   . ALA B 167  ? 0.2397 0.2554 0.1721 0.0621  0.0167  -0.0524 165  ALA B N   
9801  C CA  . ALA B 167  ? 0.2813 0.2872 0.2056 0.0640  0.0144  -0.0562 165  ALA B CA  
9802  C C   . ALA B 167  ? 0.2646 0.2691 0.1835 0.0707  0.0165  -0.0592 165  ALA B C   
9803  O O   . ALA B 167  ? 0.2779 0.2789 0.1884 0.0735  0.0166  -0.0619 165  ALA B O   
9804  C CB  . ALA B 167  ? 0.3047 0.3003 0.2310 0.0613  0.0101  -0.0573 165  ALA B CB  
9805  N N   . ALA B 168  ? 0.2561 0.2632 0.1796 0.0736  0.0182  -0.0588 166  ALA B N   
9806  C CA  . ALA B 168  ? 0.2645 0.2712 0.1833 0.0804  0.0205  -0.0615 166  ALA B CA  
9807  C C   . ALA B 168  ? 0.2672 0.2841 0.1825 0.0832  0.0245  -0.0609 166  ALA B C   
9808  O O   . ALA B 168  ? 0.2775 0.2920 0.1848 0.0880  0.0257  -0.0639 166  ALA B O   
9809  C CB  . ALA B 168  ? 0.2604 0.2686 0.1855 0.0828  0.0214  -0.0607 166  ALA B CB  
9810  N N   . ALA B 169  ? 0.2586 0.2867 0.1795 0.0800  0.0267  -0.0569 167  ALA B N   
9811  C CA  . ALA B 169  ? 0.2605 0.2997 0.1790 0.0820  0.0308  -0.0557 167  ALA B CA  
9812  C C   . ALA B 169  ? 0.2692 0.3056 0.1791 0.0811  0.0301  -0.0571 167  ALA B C   
9813  O O   . ALA B 169  ? 0.3114 0.3518 0.2151 0.0852  0.0329  -0.0584 167  ALA B O   
9814  C CB  . ALA B 169  ? 0.2658 0.3167 0.1924 0.0777  0.0325  -0.0508 167  ALA B CB  
9815  N N   . LEU B 170  ? 0.2687 0.2986 0.1782 0.0759  0.0265  -0.0567 168  LEU B N   
9816  C CA  . LEU B 170  ? 0.2809 0.3078 0.1824 0.0747  0.0255  -0.0578 168  LEU B CA  
9817  C C   . LEU B 170  ? 0.2959 0.3133 0.1881 0.0797  0.0244  -0.0627 168  LEU B C   
9818  O O   . LEU B 170  ? 0.2934 0.3121 0.1775 0.0824  0.0261  -0.0642 168  LEU B O   
9819  C CB  . LEU B 170  ? 0.2797 0.3018 0.1835 0.0682  0.0215  -0.0562 168  LEU B CB  
9820  C CG  . LEU B 170  ? 0.3208 0.3399 0.2167 0.0664  0.0201  -0.0569 168  LEU B CG  
9821  C CD1 . LEU B 170  ? 0.2787 0.3085 0.1712 0.0674  0.0241  -0.0551 168  LEU B CD1 
9822  C CD2 . LEU B 170  ? 0.3314 0.3477 0.2317 0.0600  0.0165  -0.0546 168  LEU B CD2 
9823  N N   . THR B 171  ? 0.3027 0.3100 0.1955 0.0809  0.0216  -0.0652 169  THR B N   
9824  C CA  . THR B 171  ? 0.2995 0.2971 0.1834 0.0860  0.0206  -0.0700 169  THR B CA  
9825  C C   . THR B 171  ? 0.3165 0.3205 0.1965 0.0930  0.0251  -0.0714 169  THR B C   
9826  O O   . THR B 171  ? 0.3170 0.3182 0.1874 0.0969  0.0259  -0.0745 169  THR B O   
9827  C CB  . THR B 171  ? 0.3146 0.3015 0.2010 0.0863  0.0172  -0.0719 169  THR B CB  
9828  O OG1 . THR B 171  ? 0.3433 0.3243 0.2325 0.0801  0.0130  -0.0709 169  THR B OG1 
9829  C CG2 . THR B 171  ? 0.3149 0.2914 0.1918 0.0919  0.0162  -0.0769 169  THR B CG2 
9830  N N   . ARG B 172  ? 0.3166 0.3293 0.2039 0.0948  0.0281  -0.0692 170  ARG B N   
9831  C CA  . ARG B 172  ? 0.3049 0.3242 0.1896 0.1018  0.0324  -0.0704 170  ARG B CA  
9832  C C   . ARG B 172  ? 0.3081 0.3371 0.1880 0.1025  0.0359  -0.0695 170  ARG B C   
9833  O O   . ARG B 172  ? 0.3230 0.3516 0.1946 0.1083  0.0380  -0.0725 170  ARG B O   
9834  C CB  . ARG B 172  ? 0.3126 0.3407 0.2071 0.1027  0.0347  -0.0676 170  ARG B CB  
9835  C CG  . ARG B 172  ? 0.3024 0.3354 0.1947 0.1108  0.0385  -0.0694 170  ARG B CG  
9836  C CD  . ARG B 172  ? 0.2931 0.3358 0.1956 0.1115  0.0407  -0.0662 170  ARG B CD  
9837  N NE  . ARG B 172  ? 0.2852 0.3218 0.1947 0.1074  0.0373  -0.0649 170  ARG B NE  
9838  C CZ  . ARG B 172  ? 0.2734 0.3155 0.1909 0.1009  0.0367  -0.0609 170  ARG B CZ  
9839  N NH1 . ARG B 172  ? 0.2683 0.3206 0.1876 0.0972  0.0386  -0.0578 170  ARG B NH1 
9840  N NH2 . ARG B 172  ? 0.2671 0.3039 0.1907 0.0982  0.0340  -0.0599 170  ARG B NH2 
9841  N N   . LEU B 173  ? 0.3097 0.3469 0.1942 0.0967  0.0365  -0.0653 171  LEU B N   
9842  C CA  . LEU B 173  ? 0.3047 0.3522 0.1852 0.0970  0.0400  -0.0638 171  LEU B CA  
9843  C C   . LEU B 173  ? 0.3145 0.3542 0.1838 0.0973  0.0384  -0.0667 171  LEU B C   
9844  O O   . LEU B 173  ? 0.3209 0.3657 0.1833 0.1011  0.0416  -0.0678 171  LEU B O   
9845  C CB  . LEU B 173  ? 0.2907 0.3484 0.1789 0.0903  0.0408  -0.0583 171  LEU B CB  
9846  C CG  . LEU B 173  ? 0.3127 0.3656 0.2019 0.0829  0.0371  -0.0564 171  LEU B CG  
9847  C CD1 . LEU B 173  ? 0.3025 0.3573 0.1835 0.0815  0.0377  -0.0561 171  LEU B CD1 
9848  C CD2 . LEU B 173  ? 0.3443 0.4050 0.2437 0.0776  0.0373  -0.0516 171  LEU B CD2 
9849  N N   . ILE B 174  ? 0.3162 0.3440 0.1835 0.0935  0.0335  -0.0681 172  ILE B N   
9850  C CA  . ILE B 174  ? 0.3243 0.3444 0.1808 0.0938  0.0316  -0.0710 172  ILE B CA  
9851  C C   . ILE B 174  ? 0.3376 0.3504 0.1852 0.1012  0.0321  -0.0762 172  ILE B C   
9852  O O   . ILE B 174  ? 0.3479 0.3612 0.1859 0.1044  0.0338  -0.0783 172  ILE B O   
9853  C CB  . ILE B 174  ? 0.3217 0.3314 0.1789 0.0878  0.0260  -0.0710 172  ILE B CB  
9854  C CG1 . ILE B 174  ? 0.3341 0.3510 0.1987 0.0808  0.0256  -0.0660 172  ILE B CG1 
9855  C CG2 . ILE B 174  ? 0.3805 0.3807 0.2258 0.0888  0.0235  -0.0747 172  ILE B CG2 
9856  C CD1 . ILE B 174  ? 0.3928 0.4007 0.2597 0.0751  0.0202  -0.0656 172  ILE B CD1 
9857  N N   . SER B 175  ? 0.3384 0.3437 0.1884 0.1040  0.0305  -0.0785 173  SER B N   
9858  C CA  . SER B 175  ? 0.3519 0.3490 0.1930 0.1113  0.0306  -0.0837 173  SER B CA  
9859  C C   . SER B 175  ? 0.3563 0.3643 0.1952 0.1181  0.0364  -0.0840 173  SER B C   
9860  O O   . SER B 175  ? 0.3935 0.3972 0.2225 0.1242  0.0375  -0.0881 173  SER B O   
9861  C CB  . SER B 175  ? 0.3620 0.3490 0.2066 0.1128  0.0277  -0.0857 173  SER B CB  
9862  O OG  . SER B 175  ? 0.4142 0.3923 0.2621 0.1064  0.0226  -0.0850 173  SER B OG  
9863  N N   . ARG B 176  ? 0.3459 0.3682 0.1938 0.1171  0.0401  -0.0797 174  ARG B N   
9864  C CA  . ARG B 176  ? 0.3497 0.3838 0.1962 0.1234  0.0457  -0.0797 174  ARG B CA  
9865  C C   . ARG B 176  ? 0.3535 0.3962 0.1941 0.1227  0.0487  -0.0784 174  ARG B C   
9866  O O   . ARG B 176  ? 0.3815 0.4264 0.2170 0.1269  0.0511  -0.0797 174  ARG B O   
9867  C CB  . ARG B 176  ? 0.3376 0.3838 0.1963 0.1228  0.0484  -0.0756 174  ARG B CB  
9868  C CG  . ARG B 176  ? 0.3546 0.4133 0.2150 0.1283  0.0535  -0.0745 174  ARG B CG  
9869  C CD  . ARG B 176  ? 0.3503 0.4199 0.2225 0.1278  0.0555  -0.0708 174  ARG B CD  
9870  N NE  . ARG B 176  ? 0.3412 0.4230 0.2194 0.1217  0.0572  -0.0659 174  ARG B NE  
9871  C CZ  . ARG B 176  ? 0.3893 0.4706 0.2758 0.1147  0.0545  -0.0626 174  ARG B CZ  
9872  N NH1 . ARG B 176  ? 0.3309 0.4017 0.2211 0.1136  0.0507  -0.0637 174  ARG B NH1 
9873  N NH2 . ARG B 176  ? 0.3838 0.4753 0.2750 0.1087  0.0557  -0.0579 174  ARG B NH2 
9874  N N   . CYS B 177  ? 0.3761 0.4226 0.2199 0.1151  0.0476  -0.0746 175  CYS B N   
9875  C CA  . CYS B 177  ? 0.3630 0.4199 0.2028 0.1136  0.0507  -0.0722 175  CYS B CA  
9876  C C   . CYS B 177  ? 0.4030 0.4516 0.2340 0.1099  0.0476  -0.0733 175  CYS B C   
9877  O O   . CYS B 177  ? 0.4382 0.4934 0.2631 0.1101  0.0502  -0.0724 175  CYS B O   
9878  C CB  . CYS B 177  ? 0.3875 0.4580 0.2378 0.1080  0.0528  -0.0661 175  CYS B CB  
9879  S SG  . CYS B 177  ? 0.4508 0.5337 0.3118 0.1120  0.0568  -0.0641 175  CYS B SG  
9880  N N   . GLY B 178  ? 0.4002 0.4356 0.2309 0.1063  0.0421  -0.0748 176  GLY B N   
9881  C CA  . GLY B 178  ? 0.4480 0.4747 0.2692 0.1039  0.0389  -0.0767 176  GLY B CA  
9882  C C   . GLY B 178  ? 0.4448 0.4781 0.2674 0.0971  0.0388  -0.0721 176  GLY B C   
9883  O O   . GLY B 178  ? 0.3948 0.4365 0.2270 0.0926  0.0396  -0.0674 176  GLY B O   
9884  N N   . GLU B 179  ? 0.4241 0.4529 0.2363 0.0966  0.0375  -0.0736 177  GLU B N   
9885  C CA  . GLU B 179  ? 0.4481 0.4811 0.2602 0.0901  0.0366  -0.0696 177  GLU B CA  
9886  C C   . GLU B 179  ? 0.4048 0.4540 0.2217 0.0886  0.0417  -0.0646 177  GLU B C   
9887  O O   . GLU B 179  ? 0.4360 0.4892 0.2590 0.0821  0.0405  -0.0601 177  GLU B O   
9888  C CB  . GLU B 179  ? 0.4527 0.4788 0.2518 0.0907  0.0349  -0.0723 177  GLU B CB  
9889  C CG  . GLU B 179  ? 0.4818 0.5084 0.2805 0.0836  0.0324  -0.0685 177  GLU B CG  
9890  C CD  . GLU B 179  ? 0.6111 0.6323 0.3967 0.0841  0.0310  -0.0707 177  GLU B CD  
9891  O OE1 . GLU B 179  ? 0.6462 0.6622 0.4226 0.0900  0.0317  -0.0755 177  GLU B OE1 
9892  O OE2 . GLU B 179  ? 0.6794 0.7014 0.4637 0.0787  0.0291  -0.0676 177  GLU B OE2 
9893  N N   . PRO B 180  ? 0.4000 0.4590 0.2145 0.0941  0.0471  -0.0650 178  PRO B N   
9894  C CA  . PRO B 180  ? 0.3931 0.4679 0.2119 0.0918  0.0516  -0.0598 178  PRO B CA  
9895  C C   . PRO B 180  ? 0.4021 0.4834 0.2343 0.0871  0.0515  -0.0553 178  PRO B C   
9896  O O   . PRO B 180  ? 0.4040 0.4938 0.2398 0.0817  0.0525  -0.0503 178  PRO B O   
9897  C CB  . PRO B 180  ? 0.4459 0.5292 0.2608 0.0997  0.0573  -0.0619 178  PRO B CB  
9898  C CG  . PRO B 180  ? 0.4227 0.4937 0.2258 0.1050  0.0555  -0.0679 178  PRO B CG  
9899  C CD  . PRO B 180  ? 0.4516 0.5078 0.2577 0.1025  0.0494  -0.0701 178  PRO B CD  
9900  N N   . VAL B 181  ? 0.3424 0.4194 0.1817 0.0887  0.0500  -0.0568 179  VAL B N   
9901  C CA  . VAL B 181  ? 0.3212 0.4045 0.1728 0.0841  0.0499  -0.0525 179  VAL B CA  
9902  C C   . VAL B 181  ? 0.3816 0.4577 0.2361 0.0766  0.0449  -0.0503 179  VAL B C   
9903  O O   . VAL B 181  ? 0.3277 0.4102 0.1899 0.0713  0.0450  -0.0458 179  VAL B O   
9904  C CB  . VAL B 181  ? 0.3930 0.4749 0.2515 0.0882  0.0502  -0.0543 179  VAL B CB  
9905  C CG1 . VAL B 181  ? 0.3460 0.4121 0.2037 0.0881  0.0449  -0.0580 179  VAL B CG1 
9906  C CG2 . VAL B 181  ? 0.3858 0.4776 0.2562 0.0844  0.0514  -0.0496 179  VAL B CG2 
9907  N N   . ILE B 182  ? 0.3914 0.4542 0.2401 0.0762  0.0405  -0.0536 180  ILE B N   
9908  C CA  . ILE B 182  ? 0.3747 0.4310 0.2259 0.0695  0.0358  -0.0517 180  ILE B CA  
9909  C C   . ILE B 182  ? 0.3952 0.4575 0.2431 0.0650  0.0366  -0.0478 180  ILE B C   
9910  O O   . ILE B 182  ? 0.4135 0.4785 0.2675 0.0591  0.0352  -0.0437 180  ILE B O   
9911  C CB  . ILE B 182  ? 0.3784 0.4197 0.2236 0.0702  0.0310  -0.0561 180  ILE B CB  
9912  C CG1 . ILE B 182  ? 0.3813 0.4160 0.2301 0.0741  0.0299  -0.0596 180  ILE B CG1 
9913  C CG2 . ILE B 182  ? 0.3791 0.4146 0.2271 0.0635  0.0261  -0.0540 180  ILE B CG2 
9914  C CD1 . ILE B 182  ? 0.4190 0.4398 0.2600 0.0763  0.0259  -0.0646 180  ILE B CD1 
9915  N N   . ARG B 183  ? 0.3775 0.4418 0.2153 0.0677  0.0388  -0.0491 181  ARG B N   
9916  C CA  . ARG B 183  ? 0.4025 0.4727 0.2362 0.0637  0.0397  -0.0454 181  ARG B CA  
9917  C C   . ARG B 183  ? 0.4691 0.5530 0.3106 0.0607  0.0433  -0.0400 181  ARG B C   
9918  O O   . ARG B 183  ? 0.4699 0.5561 0.3140 0.0545  0.0420  -0.0357 181  ARG B O   
9919  C CB  . ARG B 183  ? 0.4148 0.4858 0.2362 0.0680  0.0422  -0.0478 181  ARG B CB  
9920  N N   . ARG B 184  ? 0.4136 0.5066 0.2589 0.0650  0.0478  -0.0402 182  ARG B N   
9921  C CA  . ARG B 184  ? 0.4246 0.5311 0.2780 0.0622  0.0511  -0.0352 182  ARG B CA  
9922  C C   . ARG B 184  ? 0.4214 0.5255 0.2850 0.0566  0.0478  -0.0323 182  ARG B C   
9923  O O   . ARG B 184  ? 0.4399 0.5509 0.3078 0.0511  0.0482  -0.0274 182  ARG B O   
9924  C CB  . ARG B 184  ? 0.4316 0.5476 0.2880 0.0684  0.0559  -0.0363 182  ARG B CB  
9925  C CG  . ARG B 184  ? 0.5345 0.6591 0.3828 0.0728  0.0608  -0.0369 182  ARG B CG  
9926  C CD  . ARG B 184  ? 0.5735 0.7136 0.4248 0.0690  0.0646  -0.0311 182  ARG B CD  
9927  N NE  . ARG B 184  ? 0.5438 0.6961 0.4040 0.0711  0.0684  -0.0293 182  ARG B NE  
9928  C CZ  . ARG B 184  ? 0.5614 0.7216 0.4312 0.0660  0.0686  -0.0245 182  ARG B CZ  
9929  N NH1 . ARG B 184  ? 0.5758 0.7331 0.4477 0.0583  0.0654  -0.0208 182  ARG B NH1 
9930  N NH2 . ARG B 184  ? 0.5209 0.6922 0.3983 0.0686  0.0720  -0.0233 182  ARG B NH2 
9931  N N   . GLY B 185  ? 0.3745 0.4689 0.2419 0.0578  0.0445  -0.0354 183  GLY B N   
9932  C CA  . GLY B 185  ? 0.3675 0.4593 0.2441 0.0528  0.0414  -0.0330 183  GLY B CA  
9933  C C   . GLY B 185  ? 0.4110 0.4972 0.2858 0.0465  0.0376  -0.0306 183  GLY B C   
9934  O O   . GLY B 185  ? 0.4056 0.4950 0.2866 0.0413  0.0367  -0.0266 183  GLY B O   
9935  N N   . VAL B 186  ? 0.3891 0.4664 0.2553 0.0471  0.0350  -0.0332 184  VAL B N   
9936  C CA  . VAL B 186  ? 0.4080 0.4800 0.2716 0.0416  0.0312  -0.0311 184  VAL B CA  
9937  C C   . VAL B 186  ? 0.4274 0.5091 0.2902 0.0375  0.0336  -0.0260 184  VAL B C   
9938  O O   . VAL B 186  ? 0.4592 0.5411 0.3264 0.0320  0.0316  -0.0222 184  VAL B O   
9939  C CB  . VAL B 186  ? 0.4134 0.4756 0.2670 0.0435  0.0285  -0.0348 184  VAL B CB  
9940  C CG1 . VAL B 186  ? 0.3996 0.4581 0.2494 0.0381  0.0252  -0.0321 184  VAL B CG1 
9941  C CG2 . VAL B 186  ? 0.3977 0.4491 0.2529 0.0459  0.0251  -0.0392 184  VAL B CG2 
9942  N N   . ASP B 187  ? 0.4578 0.5478 0.3150 0.0403  0.0380  -0.0257 185  ASP B N   
9943  C CA  . ASP B 187  ? 0.4773 0.5771 0.3333 0.0363  0.0404  -0.0206 185  ASP B CA  
9944  C C   . ASP B 187  ? 0.5178 0.6260 0.3842 0.0328  0.0417  -0.0164 185  ASP B C   
9945  O O   . ASP B 187  ? 0.4915 0.6023 0.3595 0.0269  0.0408  -0.0118 185  ASP B O   
9946  C CB  . ASP B 187  ? 0.4569 0.5653 0.3056 0.0405  0.0454  -0.0213 185  ASP B CB  
9947  C CG  . ASP B 187  ? 0.6076 0.7078 0.4447 0.0435  0.0441  -0.0251 185  ASP B CG  
9948  O OD1 . ASP B 187  ? 0.5916 0.6801 0.4265 0.0416  0.0391  -0.0267 185  ASP B OD1 
9949  O OD2 . ASP B 187  ? 0.5362 0.6420 0.3664 0.0478  0.0480  -0.0265 185  ASP B OD2 
9950  N N   . MET B 188  ? 0.4471 0.5590 0.3204 0.0362  0.0437  -0.0179 186  MET B N   
9951  C CA  . MET B 188  ? 0.4582 0.5776 0.3416 0.0331  0.0446  -0.0143 186  MET B CA  
9952  C C   . MET B 188  ? 0.4377 0.5491 0.3262 0.0277  0.0398  -0.0126 186  MET B C   
9953  O O   . MET B 188  ? 0.4825 0.5982 0.3748 0.0223  0.0395  -0.0081 186  MET B O   
9954  C CB  . MET B 188  ? 0.4836 0.6068 0.3727 0.0385  0.0471  -0.0168 186  MET B CB  
9955  C CG  . MET B 188  ? 0.5091 0.6406 0.4085 0.0358  0.0482  -0.0133 186  MET B CG  
9956  S SD  . MET B 188  ? 0.6490 0.7959 0.5485 0.0316  0.0521  -0.0073 186  MET B SD  
9957  C CE  . MET B 188  ? 0.5263 0.6810 0.4181 0.0387  0.0573  -0.0098 186  MET B CE  
9958  N N   . ALA B 189  ? 0.4155 0.5152 0.3041 0.0291  0.0361  -0.0163 187  ALA B N   
9959  C CA  . ALA B 189  ? 0.4523 0.5447 0.3458 0.0245  0.0317  -0.0150 187  ALA B CA  
9960  C C   . ALA B 189  ? 0.5032 0.5928 0.3920 0.0193  0.0293  -0.0119 187  ALA B C   
9961  O O   . ALA B 189  ? 0.5079 0.5966 0.4012 0.0144  0.0271  -0.0087 187  ALA B O   
9962  C CB  . ALA B 189  ? 0.4209 0.5019 0.3149 0.0272  0.0283  -0.0196 187  ALA B CB  
9963  N N   . MET B 190  ? 0.4950 0.5832 0.3745 0.0205  0.0296  -0.0128 188  MET B N   
9964  C CA  . MET B 190  ? 0.5475 0.6329 0.4217 0.0158  0.0273  -0.0098 188  MET B CA  
9965  C C   . MET B 190  ? 0.5226 0.6175 0.3991 0.0111  0.0294  -0.0042 188  MET B C   
9966  O O   . MET B 190  ? 0.5544 0.6462 0.4321 0.0058  0.0265  -0.0009 188  MET B O   
9967  C CB  . MET B 190  ? 0.4904 0.5734 0.3537 0.0184  0.0277  -0.0120 188  MET B CB  
9968  C CG  . MET B 190  ? 0.5789 0.6535 0.4363 0.0149  0.0233  -0.0110 188  MET B CG  
9969  S SD  . MET B 190  ? 0.7398 0.8131 0.5837 0.0177  0.0243  -0.0130 188  MET B SD  
9970  C CE  . MET B 190  ? 0.5674 0.6355 0.4100 0.0249  0.0247  -0.0198 188  MET B CE  
9971  N N   . ARG B 191  ? 0.4884 0.5949 0.3656 0.0129  0.0343  -0.0030 189  ARG B N   
9972  C CA  . ARG B 191  ? 0.5495 0.6661 0.4294 0.0081  0.0365  0.0025  189  ARG B CA  
9973  C C   . ARG B 191  ? 0.5685 0.6848 0.4580 0.0044  0.0346  0.0047  189  ARG B C   
9974  O O   . ARG B 191  ? 0.5532 0.6690 0.4437 -0.0014 0.0327  0.0089  189  ARG B O   
9975  C CB  . ARG B 191  ? 0.4836 0.6133 0.3630 0.0114  0.0423  0.0029  189  ARG B CB  
9976  N N   . MET B 192  ? 0.5436 0.6596 0.4399 0.0077  0.0350  0.0020  190  MET B N   
9977  C CA  . MET B 192  ? 0.4765 0.5928 0.3818 0.0045  0.0335  0.0039  190  MET B CA  
9978  C C   . MET B 192  ? 0.5254 0.6303 0.4312 0.0008  0.0283  0.0043  190  MET B C   
9979  O O   . MET B 192  ? 0.5171 0.6222 0.4261 -0.0044 0.0266  0.0080  190  MET B O   
9980  C CB  . MET B 192  ? 0.5186 0.6363 0.4303 0.0093  0.0349  0.0006  190  MET B CB  
9981  C CG  . MET B 192  ? 0.4846 0.6132 0.3961 0.0139  0.0400  -0.0002 190  MET B CG  
9982  S SD  . MET B 192  ? 0.6248 0.7536 0.5443 0.0190  0.0407  -0.0037 190  MET B SD  
9983  C CE  . MET B 192  ? 0.4214 0.5520 0.3501 0.0130  0.0388  0.0004  190  MET B CE  
9984  N N   . MET B 193  ? 0.4777 0.5724 0.3804 0.0034  0.0255  0.0004  191  MET B N   
9985  C CA  . MET B 193  ? 0.5252 0.6095 0.4292 0.0005  0.0206  0.0004  191  MET B CA  
9986  C C   . MET B 193  ? 0.5318 0.6130 0.4298 -0.0040 0.0183  0.0037  191  MET B C   
9987  O O   . MET B 193  ? 0.5798 0.6545 0.4798 -0.0074 0.0146  0.0051  191  MET B O   
9988  C CB  . MET B 193  ? 0.4951 0.5700 0.3980 0.0045  0.0181  -0.0045 191  MET B CB  
9989  C CG  . MET B 193  ? 0.4931 0.5681 0.4029 0.0079  0.0189  -0.0074 191  MET B CG  
9990  S SD  . MET B 193  ? 0.6382 0.7008 0.5480 0.0105  0.0148  -0.0122 191  MET B SD  
9991  C CE  . MET B 193  ? 0.4998 0.5596 0.3987 0.0133  0.0150  -0.0147 191  MET B CE  
9992  N N   . GLY B 194  ? 0.5332 0.6189 0.4239 -0.0039 0.0205  0.0048  192  GLY B N   
9993  C CA  . GLY B 194  ? 0.5273 0.6095 0.4114 -0.0079 0.0182  0.0079  192  GLY B CA  
9994  C C   . GLY B 194  ? 0.5425 0.6328 0.4262 -0.0129 0.0201  0.0134  192  GLY B C   
9995  O O   . GLY B 194  ? 0.5038 0.5904 0.3838 -0.0174 0.0176  0.0167  192  GLY B O   
9996  N N   . GLU B 195  ? 0.4655 0.5670 0.3532 -0.0122 0.0245  0.0146  193  GLU B N   
9997  C CA  . GLU B 195  ? 0.4918 0.6028 0.3786 -0.0167 0.0269  0.0199  193  GLU B CA  
9998  C C   . GLU B 195  ? 0.4987 0.6173 0.3944 -0.0188 0.0285  0.0222  193  GLU B C   
9999  O O   . GLU B 195  ? 0.4556 0.5789 0.3522 -0.0242 0.0286  0.0272  193  GLU B O   
10000 C CB  . GLU B 195  ? 0.5191 0.6389 0.3996 -0.0140 0.0314  0.0199  193  GLU B CB  
10001 C CG  . GLU B 195  ? 0.6168 0.7298 0.4877 -0.0116 0.0302  0.0174  193  GLU B CG  
10002 C CD  . GLU B 195  ? 0.6324 0.7545 0.4972 -0.0082 0.0350  0.0168  193  GLU B CD  
10003 O OE1 . GLU B 195  ? 0.6334 0.7677 0.5004 -0.0096 0.0390  0.0201  193  GLU B OE1 
10004 O OE2 . GLU B 195  ? 0.7381 0.8554 0.5961 -0.0040 0.0348  0.0130  193  GLU B OE2 
10005 N N   . GLN B 196  ? 0.5240 0.6438 0.4262 -0.0146 0.0295  0.0189  194  GLN B N   
10006 C CA  . GLN B 196  ? 0.4795 0.6069 0.3902 -0.0161 0.0311  0.0207  194  GLN B CA  
10007 C C   . GLN B 196  ? 0.4808 0.6000 0.3976 -0.0180 0.0272  0.0203  194  GLN B C   
10008 O O   . GLN B 196  ? 0.5147 0.6370 0.4361 -0.0226 0.0266  0.0238  194  GLN B O   
10009 C CB  . GLN B 196  ? 0.4650 0.6005 0.3790 -0.0101 0.0353  0.0177  194  GLN B CB  
10010 N N   . PHE B 197  ? 0.4100 0.5192 0.3272 -0.0148 0.0246  0.0160  195  PHE B N   
10011 C CA  . PHE B 197  ? 0.4524 0.5537 0.3748 -0.0166 0.0208  0.0156  195  PHE B CA  
10012 C C   . PHE B 197  ? 0.4524 0.5464 0.3715 -0.0219 0.0169  0.0186  195  PHE B C   
10013 O O   . PHE B 197  ? 0.4835 0.5751 0.4066 -0.0256 0.0148  0.0208  195  PHE B O   
10014 C CB  . PHE B 197  ? 0.4945 0.5876 0.4182 -0.0118 0.0192  0.0105  195  PHE B CB  
10015 C CG  . PHE B 197  ? 0.5155 0.6141 0.4429 -0.0066 0.0224  0.0074  195  PHE B CG  
10016 C CD1 . PHE B 197  ? 0.4473 0.5567 0.3792 -0.0067 0.0258  0.0094  195  PHE B CD1 
10017 C CD2 . PHE B 197  ? 0.5116 0.6044 0.4379 -0.0016 0.0218  0.0027  195  PHE B CD2 
10018 C CE1 . PHE B 197  ? 0.5367 0.6509 0.4720 -0.0016 0.0286  0.0066  195  PHE B CE1 
10019 C CE2 . PHE B 197  ? 0.4833 0.5802 0.4126 0.0033  0.0246  -0.0001 195  PHE B CE2 
10020 C CZ  . PHE B 197  ? 0.5259 0.6335 0.4597 0.0034  0.0280  0.0018  195  PHE B CZ  
10021 N N   . VAL B 198  ? 0.4324 0.5223 0.3438 -0.0221 0.0159  0.0188  196  VAL B N   
10022 C CA  . VAL B 198  ? 0.3947 0.4776 0.3021 -0.0269 0.0121  0.0218  196  VAL B CA  
10023 C C   . VAL B 198  ? 0.4340 0.5229 0.3347 -0.0298 0.0140  0.0256  196  VAL B C   
10024 O O   . VAL B 198  ? 0.3949 0.4910 0.2924 -0.0271 0.0177  0.0248  196  VAL B O   
10025 C CB  . VAL B 198  ? 0.3645 0.4356 0.2689 -0.0250 0.0081  0.0188  196  VAL B CB  
10026 C CG1 . VAL B 198  ? 0.3939 0.4601 0.3051 -0.0221 0.0066  0.0151  196  VAL B CG1 
10027 C CG2 . VAL B 198  ? 0.4075 0.4786 0.3049 -0.0214 0.0093  0.0163  196  VAL B CG2 
10028 N N   . THR B 199  ? 0.4258 0.5114 0.3242 -0.0354 0.0115  0.0299  197  THR B N   
10029 C CA  . THR B 199  ? 0.3891 0.4784 0.2801 -0.0387 0.0125  0.0337  197  THR B CA  
10030 C C   . THR B 199  ? 0.4333 0.5154 0.3163 -0.0366 0.0106  0.0318  197  THR B C   
10031 O O   . THR B 199  ? 0.4376 0.5242 0.3139 -0.0367 0.0127  0.0332  197  THR B O   
10032 C CB  . THR B 199  ? 0.4111 0.4984 0.3020 -0.0456 0.0100  0.0390  197  THR B CB  
10033 O OG1 . THR B 199  ? 0.4546 0.5474 0.3534 -0.0474 0.0111  0.0402  197  THR B OG1 
10034 C CG2 . THR B 199  ? 0.3854 0.4786 0.2696 -0.0496 0.0117  0.0437  197  THR B CG2 
10035 N N   . GLY B 200  ? 0.3777 0.4491 0.2614 -0.0344 0.0068  0.0286  198  GLY B N   
10036 C CA  . GLY B 200  ? 0.4151 0.4795 0.2919 -0.0321 0.0046  0.0263  198  GLY B CA  
10037 C C   . GLY B 200  ? 0.3963 0.4512 0.2768 -0.0291 0.0010  0.0222  198  GLY B C   
10038 O O   . GLY B 200  ? 0.3820 0.4344 0.2694 -0.0297 -0.0004 0.0219  198  GLY B O   
10039 N N   . GLU B 201  ? 0.4704 0.5203 0.3460 -0.0258 -0.0004 0.0191  199  GLU B N   
10040 C CA  . GLU B 201  ? 0.4753 0.5162 0.3538 -0.0232 -0.0041 0.0154  199  GLU B CA  
10041 C C   . GLU B 201  ? 0.4573 0.4891 0.3343 -0.0262 -0.0092 0.0174  199  GLU B C   
10042 O O   . GLU B 201  ? 0.4886 0.5137 0.3701 -0.0250 -0.0123 0.0153  199  GLU B O   
10043 C CB  . GLU B 201  ? 0.4787 0.5176 0.3527 -0.0186 -0.0039 0.0111  199  GLU B CB  
10044 C CG  . GLU B 201  ? 0.5574 0.6033 0.4337 -0.0145 0.0005  0.0081  199  GLU B CG  
10045 C CD  . GLU B 201  ? 0.6732 0.7152 0.5453 -0.0100 -0.0001 0.0034  199  GLU B CD  
10046 O OE1 . GLU B 201  ? 0.6644 0.6999 0.5305 -0.0104 -0.0033 0.0031  199  GLU B OE1 
10047 O OE2 . GLU B 201  ? 0.7059 0.7510 0.5807 -0.0061 0.0025  0.0000  199  GLU B OE2 
10048 N N   . THR B 202  ? 0.3970 0.4282 0.2675 -0.0300 -0.0100 0.0215  200  THR B N   
10049 C CA  . THR B 202  ? 0.4030 0.4258 0.2714 -0.0332 -0.0148 0.0242  200  THR B CA  
10050 C C   . THR B 202  ? 0.4481 0.4743 0.3154 -0.0386 -0.0139 0.0296  200  THR B C   
10051 O O   . THR B 202  ? 0.3954 0.4308 0.2620 -0.0399 -0.0097 0.0314  200  THR B O   
10052 C CB  . THR B 202  ? 0.4503 0.4674 0.3102 -0.0327 -0.0176 0.0241  200  THR B CB  
10053 O OG1 . THR B 202  ? 0.4333 0.4562 0.2857 -0.0345 -0.0148 0.0268  200  THR B OG1 
10054 C CG2 . THR B 202  ? 0.4600 0.4744 0.3204 -0.0277 -0.0184 0.0188  200  THR B CG2 
10055 N N   . ILE B 203  ? 0.3889 0.4075 0.2559 -0.0419 -0.0180 0.0322  201  ILE B N   
10056 C CA  . ILE B 203  ? 0.3607 0.3813 0.2265 -0.0474 -0.0178 0.0375  201  ILE B CA  
10057 C C   . ILE B 203  ? 0.3758 0.3998 0.2327 -0.0503 -0.0166 0.0411  201  ILE B C   
10058 O O   . ILE B 203  ? 0.3884 0.4197 0.2444 -0.0540 -0.0137 0.0449  201  ILE B O   
10059 C CB  . ILE B 203  ? 0.3682 0.3788 0.2354 -0.0499 -0.0227 0.0392  201  ILE B CB  
10060 C CG1 . ILE B 203  ? 0.3496 0.3619 0.2160 -0.0559 -0.0226 0.0445  201  ILE B CG1 
10061 C CG2 . ILE B 203  ? 0.4073 0.4083 0.2682 -0.0495 -0.0273 0.0394  201  ILE B CG2 
10062 C CD1 . ILE B 203  ? 0.3220 0.3437 0.1954 -0.0567 -0.0186 0.0445  201  ILE B CD1 
10063 N N   . ARG B 204  ? 0.4421 0.4613 0.2922 -0.0486 -0.0185 0.0401  202  ARG B N   
10064 C CA  . ARG B 204  ? 0.4274 0.4498 0.2685 -0.0513 -0.0173 0.0437  202  ARG B CA  
10065 C C   . ARG B 204  ? 0.4308 0.4653 0.2714 -0.0495 -0.0113 0.0428  202  ARG B C   
10066 O O   . ARG B 204  ? 0.4467 0.4880 0.2831 -0.0530 -0.0087 0.0468  202  ARG B O   
10067 C CB  . ARG B 204  ? 0.4713 0.4856 0.3048 -0.0499 -0.0210 0.0430  202  ARG B CB  
10068 C CG  . ARG B 204  ? 0.4959 0.5113 0.3280 -0.0444 -0.0199 0.0379  202  ARG B CG  
10069 C CD  . ARG B 204  ? 0.5016 0.5097 0.3252 -0.0438 -0.0236 0.0378  202  ARG B CD  
10070 N NE  . ARG B 204  ? 0.4668 0.4773 0.2875 -0.0391 -0.0219 0.0334  202  ARG B NE  
10071 C CZ  . ARG B 204  ? 0.5506 0.5666 0.3636 -0.0389 -0.0188 0.0340  202  ARG B CZ  
10072 N NH1 . ARG B 204  ? 0.5482 0.5685 0.3558 -0.0431 -0.0170 0.0390  202  ARG B NH1 
10073 N NH2 . ARG B 204  ? 0.5115 0.5286 0.3221 -0.0343 -0.0174 0.0295  202  ARG B NH2 
10074 N N   . GLU B 205  ? 0.4425 0.4799 0.2874 -0.0443 -0.0091 0.0377  203  GLU B N   
10075 C CA  . GLU B 205  ? 0.4337 0.4826 0.2790 -0.0422 -0.0034 0.0367  203  GLU B CA  
10076 C C   . GLU B 205  ? 0.3940 0.4514 0.2456 -0.0453 -0.0004 0.0396  203  GLU B C   
10077 O O   . GLU B 205  ? 0.4294 0.4968 0.2789 -0.0470 0.0037  0.0424  203  GLU B O   
10078 C CB  . GLU B 205  ? 0.4799 0.5290 0.3287 -0.0358 -0.0022 0.0305  203  GLU B CB  
10079 C CG  . GLU B 205  ? 0.5270 0.5876 0.3765 -0.0331 0.0037  0.0292  203  GLU B CG  
10080 C CD  . GLU B 205  ? 0.5967 0.6566 0.4490 -0.0268 0.0048  0.0232  203  GLU B CD  
10081 O OE1 . GLU B 205  ? 0.5902 0.6438 0.4485 -0.0252 0.0020  0.0204  203  GLU B OE1 
10082 O OE2 . GLU B 205  ? 0.6943 0.7601 0.5428 -0.0235 0.0084  0.0212  203  GLU B OE2 
10083 N N   . ALA B 206  ? 0.3693 0.4233 0.2287 -0.0460 -0.0023 0.0392  204  ALA B N   
10084 C CA  . ALA B 206  ? 0.3852 0.4466 0.2506 -0.0494 0.0000  0.0421  204  ALA B CA  
10085 C C   . ALA B 206  ? 0.4080 0.4714 0.2686 -0.0559 -0.0003 0.0483  204  ALA B C   
10086 O O   . ALA B 206  ? 0.3847 0.4589 0.2465 -0.0584 0.0035  0.0513  204  ALA B O   
10087 C CB  . ALA B 206  ? 0.3488 0.4043 0.2221 -0.0493 -0.0028 0.0406  204  ALA B CB  
10088 N N   . LEU B 207  ? 0.3813 0.4348 0.2362 -0.0587 -0.0048 0.0506  205  LEU B N   
10089 C CA  . LEU B 207  ? 0.4123 0.4665 0.2621 -0.0653 -0.0056 0.0568  205  LEU B CA  
10090 C C   . LEU B 207  ? 0.4510 0.5148 0.2943 -0.0659 -0.0014 0.0590  205  LEU B C   
10091 O O   . LEU B 207  ? 0.4153 0.4872 0.2580 -0.0706 0.0010  0.0637  205  LEU B O   
10092 C CB  . LEU B 207  ? 0.4016 0.4423 0.2462 -0.0675 -0.0115 0.0584  205  LEU B CB  
10093 C CG  . LEU B 207  ? 0.4154 0.4471 0.2660 -0.0682 -0.0156 0.0577  205  LEU B CG  
10094 C CD1 . LEU B 207  ? 0.3969 0.4149 0.2430 -0.0678 -0.0214 0.0573  205  LEU B CD1 
10095 C CD2 . LEU B 207  ? 0.3511 0.3852 0.2041 -0.0744 -0.0156 0.0625  205  LEU B CD2 
10096 N N   . LYS B 208  ? 0.4165 0.4796 0.2547 -0.0613 -0.0006 0.0556  206  LYS B N   
10097 C CA  . LYS B 208  ? 0.4270 0.4993 0.2585 -0.0613 0.0036  0.0573  206  LYS B CA  
10098 C C   . LYS B 208  ? 0.4436 0.5304 0.2805 -0.0604 0.0096  0.0573  206  LYS B C   
10099 O O   . LYS B 208  ? 0.4865 0.5830 0.3205 -0.0637 0.0129  0.0615  206  LYS B O   
10100 C CB  . LYS B 208  ? 0.4928 0.5613 0.3181 -0.0559 0.0033  0.0529  206  LYS B CB  
10101 N N   . ARG B 209  ? 0.4255 0.5142 0.2704 -0.0560 0.0109  0.0529  207  ARG B N   
10102 C CA  . ARG B 209  ? 0.4463 0.5487 0.2967 -0.0546 0.0163  0.0527  207  ARG B CA  
10103 C C   . ARG B 209  ? 0.4857 0.5940 0.3416 -0.0606 0.0168  0.0577  207  ARG B C   
10104 O O   . ARG B 209  ? 0.4827 0.6040 0.3424 -0.0606 0.0215  0.0589  207  ARG B O   
10105 C CB  . ARG B 209  ? 0.4321 0.5342 0.2893 -0.0481 0.0173  0.0466  207  ARG B CB  
10106 C CG  . ARG B 209  ? 0.4619 0.5599 0.3139 -0.0420 0.0174  0.0415  207  ARG B CG  
10107 C CD  . ARG B 209  ? 0.5209 0.6194 0.3795 -0.0360 0.0188  0.0359  207  ARG B CD  
10108 N NE  . ARG B 209  ? 0.6086 0.7031 0.4618 -0.0304 0.0188  0.0311  207  ARG B NE  
10109 C CZ  . ARG B 209  ? 0.6497 0.7411 0.5067 -0.0250 0.0187  0.0257  207  ARG B CZ  
10110 N NH1 . ARG B 209  ? 0.5623 0.6540 0.4285 -0.0242 0.0186  0.0244  207  ARG B NH1 
10111 N NH2 . ARG B 209  ? 0.6434 0.7309 0.4944 -0.0205 0.0186  0.0217  207  ARG B NH2 
10112 N N   . SER B 210  ? 0.4219 0.5212 0.2784 -0.0655 0.0121  0.0605  208  SER B N   
10113 C CA  . SER B 210  ? 0.4089 0.5127 0.2703 -0.0715 0.0121  0.0651  208  SER B CA  
10114 C C   . SER B 210  ? 0.3959 0.5077 0.2522 -0.0774 0.0141  0.0714  208  SER B C   
10115 O O   . SER B 210  ? 0.4284 0.5482 0.2891 -0.0820 0.0156  0.0753  208  SER B O   
10116 C CB  . SER B 210  ? 0.3868 0.4774 0.2499 -0.0745 0.0063  0.0658  208  SER B CB  
10117 O OG  . SER B 210  ? 0.4190 0.5038 0.2880 -0.0694 0.0049  0.0603  208  SER B OG  
10118 N N   . LYS B 211  ? 0.4565 0.5664 0.3035 -0.0777 0.0141  0.0727  209  LYS B N   
10119 C CA  . LYS B 211  ? 0.4078 0.5238 0.2488 -0.0839 0.0154  0.0791  209  LYS B CA  
10120 C C   . LYS B 211  ? 0.4274 0.5612 0.2727 -0.0847 0.0215  0.0812  209  LYS B C   
10121 O O   . LYS B 211  ? 0.4506 0.5908 0.2963 -0.0914 0.0222  0.0871  209  LYS B O   
10122 C CB  . LYS B 211  ? 0.4392 0.5514 0.2695 -0.0825 0.0152  0.0791  209  LYS B CB  
10123 N N   . GLU B 212  ? 0.4269 0.5687 0.2755 -0.0779 0.0258  0.0765  210  GLU B N   
10124 C CA  . GLU B 212  ? 0.4426 0.6020 0.2943 -0.0775 0.0320  0.0783  210  GLU B CA  
10125 C C   . GLU B 212  ? 0.4751 0.6415 0.3358 -0.0823 0.0323  0.0817  210  GLU B C   
10126 O O   . GLU B 212  ? 0.4804 0.6577 0.3412 -0.0878 0.0346  0.0873  210  GLU B O   
10127 C CB  . GLU B 212  ? 0.5040 0.6686 0.3579 -0.0686 0.0358  0.0719  210  GLU B CB  
10128 C CG  . GLU B 212  ? 0.6100 0.7929 0.4678 -0.0671 0.0423  0.0731  210  GLU B CG  
10129 C CD  . GLU B 212  ? 0.7527 0.9392 0.6136 -0.0581 0.0455  0.0665  210  GLU B CD  
10130 O OE1 . GLU B 212  ? 0.8256 1.0015 0.6824 -0.0531 0.0436  0.0615  210  GLU B OE1 
10131 O OE2 . GLU B 212  ? 0.8420 1.0417 0.7095 -0.0561 0.0498  0.0665  210  GLU B OE2 
10132 N N   . LEU B 213  ? 0.4027 0.5632 0.2709 -0.0805 0.0298  0.0785  211  LEU B N   
10133 C CA  . LEU B 213  ? 0.4735 0.6402 0.3501 -0.0849 0.0298  0.0814  211  LEU B CA  
10134 C C   . LEU B 213  ? 0.4059 0.5650 0.2807 -0.0934 0.0251  0.0868  211  LEU B C   
10135 O O   . LEU B 213  ? 0.4361 0.6027 0.3155 -0.0990 0.0256  0.0911  211  LEU B O   
10136 C CB  . LEU B 213  ? 0.3685 0.5320 0.2536 -0.0799 0.0290  0.0761  211  LEU B CB  
10137 C CG  . LEU B 213  ? 0.4187 0.5926 0.3073 -0.0722 0.0341  0.0716  211  LEU B CG  
10138 C CD1 . LEU B 213  ? 0.4122 0.5834 0.3093 -0.0680 0.0333  0.0671  211  LEU B CD1 
10139 C CD2 . LEU B 213  ? 0.5048 0.6970 0.3956 -0.0741 0.0395  0.0755  211  LEU B CD2 
10140 N N   . GLU B 214  ? 0.4181 0.5622 0.2859 -0.0946 0.0204  0.0867  212  GLU B N   
10141 C CA  . GLU B 214  ? 0.4167 0.5531 0.2814 -0.1028 0.0160  0.0922  212  GLU B CA  
10142 C C   . GLU B 214  ? 0.4437 0.5908 0.3041 -0.1091 0.0186  0.0989  212  GLU B C   
10143 O O   . GLU B 214  ? 0.4174 0.5661 0.2793 -0.1167 0.0170  0.1043  212  GLU B O   
10144 C CB  . GLU B 214  ? 0.4418 0.5607 0.2995 -0.1021 0.0107  0.0907  212  GLU B CB  
10145 C CG  . GLU B 214  ? 0.3998 0.5070 0.2627 -0.0987 0.0068  0.0859  212  GLU B CG  
10146 C CD  . GLU B 214  ? 0.4216 0.5118 0.2784 -0.0987 0.0011  0.0851  212  GLU B CD  
10147 O OE1 . GLU B 214  ? 0.4513 0.5385 0.2996 -0.1005 0.0002  0.0877  212  GLU B OE1 
10148 O OE2 . GLU B 214  ? 0.4220 0.5020 0.2825 -0.0967 -0.0025 0.0820  212  GLU B OE2 
10149 N N   . GLU B 215  ? 0.4154 0.5702 0.2703 -0.1063 0.0227  0.0988  213  GLU B N   
10150 C CA  . GLU B 215  ? 0.4443 0.6104 0.2962 -0.1114 0.0257  0.1046  213  GLU B CA  
10151 C C   . GLU B 215  ? 0.4892 0.6699 0.3519 -0.1127 0.0290  0.1058  213  GLU B C   
10152 O O   . GLU B 215  ? 0.5025 0.6886 0.3672 -0.1181 0.0290  0.1103  213  GLU B O   
10153 C CB  . GLU B 215  ? 0.4703 0.6413 0.3159 -0.1063 0.0296  0.1026  213  GLU B CB  
10154 C CG  . GLU B 215  ? 0.5388 0.6961 0.3732 -0.1062 0.0260  0.1023  213  GLU B CG  
10155 C CD  . GLU B 215  ? 0.6391 0.8015 0.4668 -0.1039 0.0293  0.1025  213  GLU B CD  
10156 O OE1 . GLU B 215  ? 0.6806 0.8563 0.5121 -0.1041 0.0337  0.1040  213  GLU B OE1 
10157 O OE2 . GLU B 215  ? 0.6305 0.7834 0.4490 -0.1018 0.0272  0.1010  213  GLU B OE2 
10158 N N   . LYS B 216  ? 0.4652 0.6525 0.3348 -0.1077 0.0317  0.1020  214  LYS B N   
10159 C CA  . LYS B 216  ? 0.4408 0.6416 0.3209 -0.1083 0.0344  0.1028  214  LYS B CA  
10160 C C   . LYS B 216  ? 0.5148 0.7106 0.4005 -0.1142 0.0302  0.1052  214  LYS B C   
10161 O O   . LYS B 216  ? 0.4876 0.6939 0.3822 -0.1155 0.0317  0.1062  214  LYS B O   
10162 C CB  . LYS B 216  ? 0.4182 0.6283 0.3033 -0.0999 0.0391  0.0975  214  LYS B CB  
10163 N N   . GLY B 217  ? 0.4128 0.5928 0.2934 -0.1177 0.0249  0.1060  215  GLY B N   
10164 C CA  . GLY B 217  ? 0.4087 0.5820 0.2931 -0.1237 0.0204  0.1085  215  GLY B CA  
10165 C C   . GLY B 217  ? 0.4436 0.6067 0.3331 -0.1192 0.0175  0.1029  215  GLY B C   
10166 O O   . GLY B 217  ? 0.4151 0.5722 0.3080 -0.1235 0.0137  0.1043  215  GLY B O   
10167 N N   . PHE B 218  ? 0.3822 0.5430 0.2723 -0.1105 0.0190  0.0966  216  PHE B N   
10168 C CA  . PHE B 218  ? 0.4240 0.5737 0.3183 -0.1061 0.0159  0.0911  216  PHE B CA  
10169 C C   . PHE B 218  ? 0.4030 0.5341 0.2909 -0.1074 0.0101  0.0907  216  PHE B C   
10170 O O   . PHE B 218  ? 0.3725 0.4990 0.2521 -0.1095 0.0090  0.0931  216  PHE B O   
10171 C CB  . PHE B 218  ? 0.3918 0.5449 0.2886 -0.0967 0.0193  0.0847  216  PHE B CB  
10172 C CG  . PHE B 218  ? 0.3868 0.5565 0.2912 -0.0940 0.0245  0.0840  216  PHE B CG  
10173 C CD1 . PHE B 218  ? 0.4243 0.6086 0.3271 -0.0934 0.0298  0.0862  216  PHE B CD1 
10174 C CD2 . PHE B 218  ? 0.4096 0.5801 0.3224 -0.0917 0.0242  0.0812  216  PHE B CD2 
10175 C CE1 . PHE B 218  ? 0.4313 0.6310 0.3412 -0.0904 0.0345  0.0855  216  PHE B CE1 
10176 C CE2 . PHE B 218  ? 0.4115 0.5970 0.3313 -0.0889 0.0287  0.0806  216  PHE B CE2 
10177 C CZ  . PHE B 218  ? 0.4250 0.6252 0.3435 -0.0882 0.0339  0.0828  216  PHE B CZ  
10178 N N   . SER B 219  ? 0.3877 0.5082 0.2794 -0.1060 0.0063  0.0875  217  SER B N   
10179 C CA  . SER B 219  ? 0.3650 0.4680 0.2518 -0.1047 0.0012  0.0854  217  SER B CA  
10180 C C   . SER B 219  ? 0.3646 0.4633 0.2558 -0.0967 0.0014  0.0784  217  SER B C   
10181 O O   . SER B 219  ? 0.3270 0.4354 0.2244 -0.0925 0.0052  0.0755  217  SER B O   
10182 C CB  . SER B 219  ? 0.4029 0.4954 0.2891 -0.1112 -0.0041 0.0886  217  SER B CB  
10183 O OG  . SER B 219  ? 0.4157 0.5100 0.3100 -0.1112 -0.0044 0.0871  217  SER B OG  
10184 N N   . TYR B 220  ? 0.3472 0.4313 0.2353 -0.0945 -0.0029 0.0757  218  TYR B N   
10185 C CA  . TYR B 220  ? 0.3009 0.3805 0.1923 -0.0870 -0.0029 0.0693  218  TYR B CA  
10186 C C   . TYR B 220  ? 0.2928 0.3585 0.1858 -0.0869 -0.0081 0.0674  218  TYR B C   
10187 O O   . TYR B 220  ? 0.3460 0.4023 0.2347 -0.0914 -0.0122 0.0705  218  TYR B O   
10188 C CB  . TYR B 220  ? 0.3242 0.4016 0.2097 -0.0823 -0.0021 0.0668  218  TYR B CB  
10189 C CG  . TYR B 220  ? 0.3293 0.4203 0.2151 -0.0792 0.0036  0.0659  218  TYR B CG  
10190 C CD1 . TYR B 220  ? 0.3619 0.4620 0.2432 -0.0830 0.0063  0.0705  218  TYR B CD1 
10191 C CD2 . TYR B 220  ? 0.3084 0.4035 0.1992 -0.0724 0.0063  0.0606  218  TYR B CD2 
10192 C CE1 . TYR B 220  ? 0.3774 0.4905 0.2590 -0.0797 0.0118  0.0695  218  TYR B CE1 
10193 C CE2 . TYR B 220  ? 0.3505 0.4577 0.2415 -0.0691 0.0115  0.0596  218  TYR B CE2 
10194 C CZ  . TYR B 220  ? 0.3435 0.4598 0.2299 -0.0725 0.0143  0.0639  218  TYR B CZ  
10195 O OH  . TYR B 220  ? 0.3619 0.4903 0.2483 -0.0687 0.0196  0.0627  218  TYR B OH  
10196 N N   . SER B 221  ? 0.2915 0.3561 0.1905 -0.0814 -0.0076 0.0623  219  SER B N   
10197 C CA  . SER B 221  ? 0.2973 0.3491 0.1977 -0.0793 -0.0119 0.0593  219  SER B CA  
10198 C C   . SER B 221  ? 0.3199 0.3707 0.2222 -0.0719 -0.0106 0.0536  219  SER B C   
10199 O O   . SER B 221  ? 0.3179 0.3770 0.2257 -0.0683 -0.0071 0.0508  219  SER B O   
10200 C CB  . SER B 221  ? 0.2991 0.3505 0.2058 -0.0813 -0.0129 0.0594  219  SER B CB  
10201 O OG  . SER B 221  ? 0.3070 0.3464 0.2149 -0.0789 -0.0168 0.0563  219  SER B OG  
10202 N N   . TYR B 222  ? 0.2951 0.3360 0.1928 -0.0696 -0.0136 0.0519  220  TYR B N   
10203 C CA  . TYR B 222  ? 0.2897 0.3296 0.1884 -0.0630 -0.0127 0.0468  220  TYR B CA  
10204 C C   . TYR B 222  ? 0.3037 0.3371 0.2082 -0.0595 -0.0147 0.0428  220  TYR B C   
10205 O O   . TYR B 222  ? 0.3064 0.3307 0.2109 -0.0613 -0.0186 0.0434  220  TYR B O   
10206 C CB  . TYR B 222  ? 0.3030 0.3365 0.1941 -0.0623 -0.0148 0.0470  220  TYR B CB  
10207 C CG  . TYR B 222  ? 0.3064 0.3473 0.1916 -0.0653 -0.0123 0.0508  220  TYR B CG  
10208 C CD1 . TYR B 222  ? 0.2803 0.3313 0.1656 -0.0622 -0.0077 0.0491  220  TYR B CD1 
10209 C CD2 . TYR B 222  ? 0.3413 0.3795 0.2213 -0.0714 -0.0143 0.0561  220  TYR B CD2 
10210 C CE1 . TYR B 222  ? 0.3461 0.4048 0.2263 -0.0648 -0.0049 0.0526  220  TYR B CE1 
10211 C CE2 . TYR B 222  ? 0.3598 0.4056 0.2346 -0.0745 -0.0117 0.0598  220  TYR B CE2 
10212 C CZ  . TYR B 222  ? 0.3878 0.4441 0.2627 -0.0711 -0.0069 0.0580  220  TYR B CZ  
10213 O OH  . TYR B 222  ? 0.3676 0.4322 0.2374 -0.0739 -0.0040 0.0617  220  TYR B OH  
10214 N N   . ASP B 223  ? 0.2844 0.3225 0.1935 -0.0544 -0.0121 0.0386  221  ASP B N   
10215 C CA  . ASP B 223  ? 0.3031 0.3367 0.2181 -0.0506 -0.0132 0.0345  221  ASP B CA  
10216 C C   . ASP B 223  ? 0.3634 0.3931 0.2769 -0.0455 -0.0138 0.0305  221  ASP B C   
10217 O O   . ASP B 223  ? 0.3375 0.3733 0.2516 -0.0421 -0.0107 0.0281  221  ASP B O   
10218 C CB  . ASP B 223  ? 0.3225 0.3652 0.2445 -0.0493 -0.0096 0.0332  221  ASP B CB  
10219 C CG  . ASP B 223  ? 0.4244 0.4641 0.3522 -0.0446 -0.0099 0.0286  221  ASP B CG  
10220 O OD1 . ASP B 223  ? 0.3728 0.4031 0.3008 -0.0438 -0.0134 0.0272  221  ASP B OD1 
10221 O OD2 . ASP B 223  ? 0.4301 0.4771 0.3623 -0.0417 -0.0066 0.0265  221  ASP B OD2 
10222 N N   . MET B 224  ? 0.3525 0.3720 0.2636 -0.0451 -0.0180 0.0299  222  MET B N   
10223 C CA  . MET B 224  ? 0.3828 0.3981 0.2935 -0.0404 -0.0191 0.0260  222  MET B CA  
10224 C C   . MET B 224  ? 0.4049 0.4215 0.3233 -0.0366 -0.0180 0.0220  222  MET B C   
10225 O O   . MET B 224  ? 0.4379 0.4505 0.3605 -0.0370 -0.0198 0.0217  222  MET B O   
10226 C CB  . MET B 224  ? 0.4104 0.4150 0.3174 -0.0409 -0.0241 0.0265  222  MET B CB  
10227 C CG  . MET B 224  ? 0.3371 0.3396 0.2363 -0.0450 -0.0256 0.0309  222  MET B CG  
10228 S SD  . MET B 224  ? 0.4350 0.4452 0.3280 -0.0447 -0.0222 0.0316  222  MET B SD  
10229 C CE  . MET B 224  ? 0.3683 0.3726 0.2594 -0.0397 -0.0245 0.0274  222  MET B CE  
10230 N N   . LEU B 225  ? 0.4343 0.4565 0.3543 -0.0330 -0.0150 0.0191  223  LEU B N   
10231 C CA  . LEU B 225  ? 0.4013 0.4258 0.3284 -0.0298 -0.0134 0.0158  223  LEU B CA  
10232 C C   . LEU B 225  ? 0.5120 0.5283 0.4422 -0.0279 -0.0168 0.0135  223  LEU B C   
10233 O O   . LEU B 225  ? 0.5305 0.5416 0.4583 -0.0260 -0.0191 0.0118  223  LEU B O   
10234 C CB  . LEU B 225  ? 0.4279 0.4578 0.3549 -0.0259 -0.0103 0.0129  223  LEU B CB  
10235 C CG  . LEU B 225  ? 0.4166 0.4561 0.3416 -0.0271 -0.0063 0.0149  223  LEU B CG  
10236 C CD1 . LEU B 225  ? 0.5371 0.5809 0.4612 -0.0227 -0.0034 0.0117  223  LEU B CD1 
10237 C CD2 . LEU B 225  ? 0.4496 0.4948 0.3802 -0.0291 -0.0044 0.0166  223  LEU B CD2 
10238 N N   . GLY B 226  ? 0.4390 0.4543 0.3745 -0.0285 -0.0172 0.0134  224  GLY B N   
10239 C CA  . GLY B 226  ? 0.4687 0.4765 0.4071 -0.0271 -0.0204 0.0117  224  GLY B CA  
10240 C C   . GLY B 226  ? 0.4136 0.4210 0.3566 -0.0286 -0.0205 0.0123  224  GLY B C   
10241 O O   . GLY B 226  ? 0.3792 0.3877 0.3207 -0.0324 -0.0205 0.0155  224  GLY B O   
10242 N N   . GLU B 227  ? 0.4204 0.4264 0.3689 -0.0257 -0.0207 0.0094  225  GLU B N   
10243 C CA  . GLU B 227  ? 0.3788 0.3840 0.3317 -0.0265 -0.0208 0.0095  225  GLU B CA  
10244 C C   . GLU B 227  ? 0.3632 0.3659 0.3212 -0.0227 -0.0214 0.0060  225  GLU B C   
10245 O O   . GLU B 227  ? 0.3834 0.3865 0.3421 -0.0197 -0.0211 0.0036  225  GLU B O   
10246 C CB  . GLU B 227  ? 0.4281 0.4413 0.3835 -0.0280 -0.0175 0.0106  225  GLU B CB  
10247 C CG  . GLU B 227  ? 0.4314 0.4513 0.3898 -0.0248 -0.0141 0.0083  225  GLU B CG  
10248 C CD  . GLU B 227  ? 0.5159 0.5442 0.4765 -0.0263 -0.0109 0.0098  225  GLU B CD  
10249 O OE1 . GLU B 227  ? 0.5018 0.5309 0.4665 -0.0269 -0.0107 0.0098  225  GLU B OE1 
10250 O OE2 . GLU B 227  ? 0.5125 0.5469 0.4706 -0.0269 -0.0087 0.0110  225  GLU B OE2 
10251 N N   . ALA B 228  ? 0.3235 0.3235 0.2847 -0.0230 -0.0223 0.0058  226  ALA B N   
10252 C CA  . ALA B 228  ? 0.3400 0.3386 0.3065 -0.0197 -0.0224 0.0028  226  ALA B CA  
10253 C C   . ALA B 228  ? 0.3656 0.3604 0.3319 -0.0169 -0.0244 0.0008  226  ALA B C   
10254 O O   . ALA B 228  ? 0.3170 0.3143 0.2860 -0.0142 -0.0231 -0.0017 226  ALA B O   
10255 C CB  . ALA B 228  ? 0.3588 0.3643 0.3299 -0.0182 -0.0189 0.0012  226  ALA B CB  
10256 N N   . ALA B 229  ? 0.3107 0.2992 0.2733 -0.0177 -0.0276 0.0019  227  ALA B N   
10257 C CA  . ALA B 229  ? 0.3083 0.2927 0.2712 -0.0151 -0.0301 0.0002  227  ALA B CA  
10258 C C   . ALA B 229  ? 0.2719 0.2565 0.2412 -0.0120 -0.0298 -0.0026 227  ALA B C   
10259 O O   . ALA B 229  ? 0.2867 0.2705 0.2588 -0.0121 -0.0295 -0.0027 227  ALA B O   
10260 C CB  . ALA B 229  ? 0.2897 0.2669 0.2486 -0.0162 -0.0339 0.0020  227  ALA B CB  
10261 N N   . THR B 230  ? 0.2601 0.2461 0.2316 -0.0095 -0.0297 -0.0049 228  THR B N   
10262 C CA  . THR B 230  ? 0.3055 0.2921 0.2832 -0.0068 -0.0295 -0.0074 228  THR B CA  
10263 C C   . THR B 230  ? 0.2928 0.2745 0.2713 -0.0050 -0.0329 -0.0080 228  THR B C   
10264 O O   . THR B 230  ? 0.2891 0.2701 0.2720 -0.0034 -0.0332 -0.0091 228  THR B O   
10265 C CB  . THR B 230  ? 0.3142 0.3050 0.2939 -0.0052 -0.0277 -0.0094 228  THR B CB  
10266 O OG1 . THR B 230  ? 0.3839 0.3793 0.3627 -0.0063 -0.0245 -0.0089 228  THR B OG1 
10267 C CG2 . THR B 230  ? 0.3018 0.2937 0.2880 -0.0028 -0.0272 -0.0117 228  THR B CG2 
10268 N N   . THR B 231  ? 0.2548 0.2336 0.2291 -0.0053 -0.0354 -0.0071 229  THR B N   
10269 C CA  . THR B 231  ? 0.2818 0.2563 0.2567 -0.0035 -0.0389 -0.0076 229  THR B CA  
10270 C C   . THR B 231  ? 0.2966 0.2656 0.2657 -0.0051 -0.0416 -0.0051 229  THR B C   
10271 O O   . THR B 231  ? 0.2763 0.2451 0.2404 -0.0078 -0.0409 -0.0030 229  THR B O   
10272 C CB  . THR B 231  ? 0.2757 0.2515 0.2512 -0.0019 -0.0400 -0.0091 229  THR B CB  
10273 O OG1 . THR B 231  ? 0.2883 0.2633 0.2574 -0.0036 -0.0406 -0.0077 229  THR B OG1 
10274 C CG2 . THR B 231  ? 0.2771 0.2579 0.2573 -0.0009 -0.0373 -0.0113 229  THR B CG2 
10275 N N   . ALA B 232  ? 0.2715 0.2360 0.2412 -0.0032 -0.0448 -0.0052 230  ALA B N   
10276 C CA  . ALA B 232  ? 0.2994 0.2577 0.2633 -0.0044 -0.0480 -0.0029 230  ALA B CA  
10277 C C   . ALA B 232  ? 0.3142 0.2726 0.2725 -0.0060 -0.0488 -0.0016 230  ALA B C   
10278 O O   . ALA B 232  ? 0.2970 0.2523 0.2493 -0.0086 -0.0498 0.0010  230  ALA B O   
10279 C CB  . ALA B 232  ? 0.3192 0.2733 0.2852 -0.0013 -0.0514 -0.0036 230  ALA B CB  
10280 N N   . ALA B 233  ? 0.2994 0.2613 0.2595 -0.0046 -0.0486 -0.0033 231  ALA B N   
10281 C CA  . ALA B 233  ? 0.3092 0.2712 0.2636 -0.0058 -0.0494 -0.0024 231  ALA B CA  
10282 C C   . ALA B 233  ? 0.3120 0.2772 0.2625 -0.0086 -0.0462 -0.0011 231  ALA B C   
10283 O O   . ALA B 233  ? 0.2964 0.2601 0.2404 -0.0106 -0.0469 0.0010  231  ALA B O   
10284 C CB  . ALA B 233  ? 0.3217 0.2865 0.2789 -0.0037 -0.0498 -0.0049 231  ALA B CB  
10285 N N   . ASP B 234  ? 0.2770 0.2468 0.2314 -0.0088 -0.0426 -0.0021 232  ASP B N   
10286 C CA  . ASP B 234  ? 0.2840 0.2575 0.2354 -0.0114 -0.0395 -0.0006 232  ASP B CA  
10287 C C   . ASP B 234  ? 0.3009 0.2708 0.2478 -0.0145 -0.0406 0.0027  232  ASP B C   
10288 O O   . ASP B 234  ? 0.3077 0.2784 0.2490 -0.0170 -0.0401 0.0050  232  ASP B O   
10289 C CB  . ASP B 234  ? 0.3183 0.2968 0.2752 -0.0109 -0.0360 -0.0021 232  ASP B CB  
10290 C CG  . ASP B 234  ? 0.3642 0.3464 0.3249 -0.0084 -0.0345 -0.0051 232  ASP B CG  
10291 O OD1 . ASP B 234  ? 0.3758 0.3578 0.3339 -0.0076 -0.0355 -0.0059 232  ASP B OD1 
10292 O OD2 . ASP B 234  ? 0.3846 0.3697 0.3507 -0.0074 -0.0323 -0.0065 232  ASP B OD2 
10293 N N   . ALA B 235  ? 0.2682 0.2343 0.2173 -0.0144 -0.0420 0.0030  233  ALA B N   
10294 C CA  . ALA B 235  ? 0.3020 0.2641 0.2469 -0.0175 -0.0431 0.0061  233  ALA B CA  
10295 C C   . ALA B 235  ? 0.2766 0.2333 0.2149 -0.0187 -0.0464 0.0084  233  ALA B C   
10296 O O   . ALA B 235  ? 0.2901 0.2457 0.2229 -0.0222 -0.0466 0.0115  233  ALA B O   
10297 C CB  . ALA B 235  ? 0.3217 0.2797 0.2700 -0.0165 -0.0443 0.0055  233  ALA B CB  
10298 N N   . GLU B 236  ? 0.2736 0.2272 0.2122 -0.0159 -0.0492 0.0071  234  GLU B N   
10299 C CA  . GLU B 236  ? 0.3022 0.2506 0.2344 -0.0168 -0.0527 0.0092  234  GLU B CA  
10300 C C   . GLU B 236  ? 0.3179 0.2700 0.2450 -0.0188 -0.0511 0.0104  234  GLU B C   
10301 O O   . GLU B 236  ? 0.3518 0.3011 0.2722 -0.0216 -0.0525 0.0135  234  GLU B O   
10302 C CB  . GLU B 236  ? 0.3211 0.2663 0.2556 -0.0131 -0.0560 0.0074  234  GLU B CB  
10303 C CG  . GLU B 236  ? 0.3496 0.2883 0.2779 -0.0135 -0.0602 0.0096  234  GLU B CG  
10304 C CD  . GLU B 236  ? 0.4594 0.3955 0.3910 -0.0096 -0.0636 0.0078  234  GLU B CD  
10305 O OE1 . GLU B 236  ? 0.4840 0.4222 0.4226 -0.0068 -0.0628 0.0052  234  GLU B OE1 
10306 O OE2 . GLU B 236  ? 0.5112 0.4434 0.4383 -0.0093 -0.0670 0.0091  234  GLU B OE2 
10307 N N   . ARG B 237  ? 0.2732 0.2318 0.2032 -0.0174 -0.0483 0.0080  235  ARG B N   
10308 C CA  . ARG B 237  ? 0.3285 0.2912 0.2536 -0.0189 -0.0463 0.0088  235  ARG B CA  
10309 C C   . ARG B 237  ? 0.3160 0.2815 0.2380 -0.0226 -0.0438 0.0117  235  ARG B C   
10310 O O   . ARG B 237  ? 0.2985 0.2635 0.2138 -0.0252 -0.0441 0.0144  235  ARG B O   
10311 C CB  . ARG B 237  ? 0.3392 0.3077 0.2682 -0.0164 -0.0437 0.0055  235  ARG B CB  
10312 C CG  . ARG B 237  ? 0.3828 0.3551 0.3063 -0.0172 -0.0418 0.0058  235  ARG B CG  
10313 C CD  . ARG B 237  ? 0.5019 0.4792 0.4287 -0.0147 -0.0391 0.0023  235  ARG B CD  
10314 N NE  . ARG B 237  ? 0.5382 0.5201 0.4706 -0.0145 -0.0356 0.0014  235  ARG B NE  
10315 C CZ  . ARG B 237  ? 0.5610 0.5436 0.5004 -0.0122 -0.0353 -0.0011 235  ARG B CZ  
10316 N NH1 . ARG B 237  ? 0.5091 0.4886 0.4511 -0.0100 -0.0380 -0.0031 235  ARG B NH1 
10317 N NH2 . ARG B 237  ? 0.5463 0.5329 0.4900 -0.0123 -0.0322 -0.0016 235  ARG B NH2 
10318 N N   . TYR B 238  ? 0.2900 0.2587 0.2168 -0.0231 -0.0412 0.0113  236  TYR B N   
10319 C CA  . TYR B 238  ? 0.3103 0.2823 0.2349 -0.0269 -0.0389 0.0141  236  TYR B CA  
10320 C C   . TYR B 238  ? 0.2963 0.2619 0.2153 -0.0303 -0.0419 0.0179  236  TYR B C   
10321 O O   . TYR B 238  ? 0.2931 0.2606 0.2071 -0.0339 -0.0409 0.0211  236  TYR B O   
10322 C CB  . TYR B 238  ? 0.2981 0.2735 0.2290 -0.0267 -0.0364 0.0130  236  TYR B CB  
10323 C CG  . TYR B 238  ? 0.3014 0.2838 0.2372 -0.0240 -0.0330 0.0099  236  TYR B CG  
10324 C CD1 . TYR B 238  ? 0.4183 0.4057 0.3517 -0.0234 -0.0308 0.0093  236  TYR B CD1 
10325 C CD2 . TYR B 238  ? 0.3150 0.2986 0.2576 -0.0220 -0.0319 0.0076  236  TYR B CD2 
10326 C CE1 . TYR B 238  ? 0.4595 0.4524 0.3970 -0.0208 -0.0278 0.0064  236  TYR B CE1 
10327 C CE2 . TYR B 238  ? 0.3955 0.3848 0.3424 -0.0197 -0.0290 0.0049  236  TYR B CE2 
10328 C CZ  . TYR B 238  ? 0.5038 0.4975 0.4481 -0.0190 -0.0270 0.0043  236  TYR B CZ  
10329 O OH  . TYR B 238  ? 0.4909 0.4894 0.4389 -0.0165 -0.0243 0.0016  236  TYR B OH  
10330 N N   . TYR B 239  ? 0.2757 0.2336 0.1954 -0.0293 -0.0456 0.0177  237  TYR B N   
10331 C CA  . TYR B 239  ? 0.2885 0.2391 0.2023 -0.0322 -0.0489 0.0212  237  TYR B CA  
10332 C C   . TYR B 239  ? 0.3335 0.2830 0.2401 -0.0336 -0.0502 0.0233  237  TYR B C   
10333 O O   . TYR B 239  ? 0.2997 0.2481 0.2005 -0.0377 -0.0505 0.0271  237  TYR B O   
10334 C CB  . TYR B 239  ? 0.3188 0.2611 0.2343 -0.0297 -0.0529 0.0201  237  TYR B CB  
10335 C CG  . TYR B 239  ? 0.3764 0.3101 0.2852 -0.0323 -0.0568 0.0236  237  TYR B CG  
10336 C CD1 . TYR B 239  ? 0.3916 0.3212 0.2989 -0.0354 -0.0575 0.0258  237  TYR B CD1 
10337 C CD2 . TYR B 239  ? 0.4235 0.3528 0.3270 -0.0319 -0.0599 0.0248  237  TYR B CD2 
10338 C CE1 . TYR B 239  ? 0.3599 0.2808 0.2606 -0.0381 -0.0613 0.0291  237  TYR B CE1 
10339 C CE2 . TYR B 239  ? 0.4285 0.3495 0.3255 -0.0344 -0.0635 0.0283  237  TYR B CE2 
10340 C CZ  . TYR B 239  ? 0.4103 0.3270 0.3060 -0.0375 -0.0642 0.0304  237  TYR B CZ  
10341 O OH  . TYR B 239  ? 0.4662 0.3739 0.3551 -0.0400 -0.0681 0.0338  237  TYR B OH  
10342 N N   . ARG B 240  ? 0.3025 0.2522 0.2092 -0.0303 -0.0512 0.0211  238  ARG B N   
10343 C CA  . ARG B 240  ? 0.3323 0.2806 0.2319 -0.0312 -0.0527 0.0229  238  ARG B CA  
10344 C C   . ARG B 240  ? 0.3207 0.2763 0.2168 -0.0339 -0.0489 0.0244  238  ARG B C   
10345 O O   . ARG B 240  ? 0.3250 0.2793 0.2139 -0.0368 -0.0497 0.0277  238  ARG B O   
10346 C CB  . ARG B 240  ? 0.3095 0.2570 0.2105 -0.0271 -0.0545 0.0198  238  ARG B CB  
10347 C CG  . ARG B 240  ? 0.3666 0.3071 0.2705 -0.0245 -0.0587 0.0188  238  ARG B CG  
10348 C CD  . ARG B 240  ? 0.4049 0.3371 0.3023 -0.0266 -0.0627 0.0224  238  ARG B CD  
10349 N NE  . ARG B 240  ? 0.4719 0.3974 0.3723 -0.0238 -0.0665 0.0214  238  ARG B NE  
10350 C CZ  . ARG B 240  ? 0.5617 0.4787 0.4576 -0.0247 -0.0704 0.0240  238  ARG B CZ  
10351 N NH1 . ARG B 240  ? 0.4814 0.3952 0.3696 -0.0287 -0.0713 0.0280  238  ARG B NH1 
10352 N NH2 . ARG B 240  ? 0.6054 0.5171 0.5046 -0.0213 -0.0735 0.0227  238  ARG B NH2 
10353 N N   . ASP B 241  ? 0.2914 0.2548 0.1923 -0.0329 -0.0447 0.0222  239  ASP B N   
10354 C CA  . ASP B 241  ? 0.3236 0.2947 0.2217 -0.0350 -0.0407 0.0236  239  ASP B CA  
10355 C C   . ASP B 241  ? 0.2987 0.2704 0.1941 -0.0400 -0.0401 0.0279  239  ASP B C   
10356 O O   . ASP B 241  ? 0.3133 0.2880 0.2029 -0.0429 -0.0389 0.0308  239  ASP B O   
10357 C CB  . ASP B 241  ? 0.3324 0.3114 0.2369 -0.0325 -0.0366 0.0203  239  ASP B CB  
10358 C CG  . ASP B 241  ? 0.4045 0.3841 0.3105 -0.0282 -0.0366 0.0164  239  ASP B CG  
10359 O OD1 . ASP B 241  ? 0.4444 0.4198 0.3458 -0.0274 -0.0394 0.0163  239  ASP B OD1 
10360 O OD2 . ASP B 241  ? 0.4967 0.4808 0.4083 -0.0258 -0.0340 0.0134  239  ASP B OD2 
10361 N N   . TYR B 242  ? 0.3157 0.2849 0.2151 -0.0411 -0.0408 0.0284  240  TYR B N   
10362 C CA  . TYR B 242  ? 0.2801 0.2486 0.1767 -0.0462 -0.0409 0.0326  240  TYR B CA  
10363 C C   . TYR B 242  ? 0.3209 0.2820 0.2096 -0.0490 -0.0447 0.0362  240  TYR B C   
10364 O O   . TYR B 242  ? 0.3023 0.2656 0.1859 -0.0535 -0.0439 0.0401  240  TYR B O   
10365 C CB  . TYR B 242  ? 0.2757 0.2408 0.1774 -0.0466 -0.0420 0.0321  240  TYR B CB  
10366 C CG  . TYR B 242  ? 0.3003 0.2729 0.2091 -0.0453 -0.0382 0.0297  240  TYR B CG  
10367 C CD1 . TYR B 242  ? 0.3157 0.2984 0.2255 -0.0461 -0.0339 0.0300  240  TYR B CD1 
10368 C CD2 . TYR B 242  ? 0.2750 0.2445 0.1895 -0.0433 -0.0391 0.0274  240  TYR B CD2 
10369 C CE1 . TYR B 242  ? 0.2941 0.2835 0.2104 -0.0448 -0.0306 0.0280  240  TYR B CE1 
10370 C CE2 . TYR B 242  ? 0.3088 0.2850 0.2296 -0.0422 -0.0358 0.0254  240  TYR B CE2 
10371 C CZ  . TYR B 242  ? 0.3065 0.2925 0.2283 -0.0430 -0.0317 0.0258  240  TYR B CZ  
10372 O OH  . TYR B 242  ? 0.3163 0.3086 0.2443 -0.0417 -0.0287 0.0239  240  TYR B OH  
10373 N N   . GLU B 243  ? 0.3163 0.2687 0.2040 -0.0466 -0.0489 0.0351  241  GLU B N   
10374 C CA  . GLU B 243  ? 0.3141 0.2584 0.1943 -0.0487 -0.0529 0.0384  241  GLU B CA  
10375 C C   . GLU B 243  ? 0.3613 0.3093 0.2349 -0.0501 -0.0518 0.0403  241  GLU B C   
10376 O O   . GLU B 243  ? 0.3231 0.2692 0.1900 -0.0545 -0.0527 0.0446  241  GLU B O   
10377 C CB  . GLU B 243  ? 0.3668 0.3026 0.2481 -0.0447 -0.0573 0.0361  241  GLU B CB  
10378 C CG  . GLU B 243  ? 0.4199 0.3467 0.2937 -0.0461 -0.0619 0.0392  241  GLU B CG  
10379 C CD  . GLU B 243  ? 0.4541 0.3743 0.3297 -0.0413 -0.0658 0.0366  241  GLU B CD  
10380 O OE1 . GLU B 243  ? 0.4363 0.3608 0.3166 -0.0373 -0.0646 0.0328  241  GLU B OE1 
10381 O OE2 . GLU B 243  ? 0.4702 0.3811 0.3427 -0.0416 -0.0701 0.0383  241  GLU B OE2 
10382 N N   . SER B 244  ? 0.3271 0.2801 0.2022 -0.0465 -0.0499 0.0370  242  SER B N   
10383 C CA  A SER B 244  ? 0.3497 0.3067 0.2183 -0.0474 -0.0486 0.0383  242  SER B CA  
10384 C CA  B SER B 244  ? 0.3499 0.3068 0.2185 -0.0474 -0.0486 0.0383  242  SER B CA  
10385 C CA  C SER B 244  ? 0.3496 0.3065 0.2181 -0.0474 -0.0486 0.0384  242  SER B CA  
10386 C C   . SER B 244  ? 0.3594 0.3245 0.2261 -0.0515 -0.0444 0.0413  242  SER B C   
10387 O O   . SER B 244  ? 0.3353 0.3010 0.1947 -0.0548 -0.0444 0.0450  242  SER B O   
10388 C CB  A SER B 244  ? 0.3545 0.3154 0.2255 -0.0426 -0.0471 0.0338  242  SER B CB  
10389 C CB  B SER B 244  ? 0.3543 0.3152 0.2252 -0.0426 -0.0471 0.0339  242  SER B CB  
10390 C CB  C SER B 244  ? 0.3547 0.3155 0.2255 -0.0426 -0.0472 0.0339  242  SER B CB  
10391 O OG  A SER B 244  ? 0.3708 0.3362 0.2355 -0.0431 -0.0452 0.0346  242  SER B OG  
10392 O OG  B SER B 244  ? 0.3664 0.3204 0.2391 -0.0391 -0.0512 0.0315  242  SER B OG  
10393 O OG  C SER B 244  ? 0.3436 0.3125 0.2208 -0.0410 -0.0428 0.0312  242  SER B OG  
10394 N N   . ALA B 245  ? 0.2978 0.2696 0.1709 -0.0513 -0.0408 0.0400  243  ALA B N   
10395 C CA  . ALA B 245  ? 0.3346 0.3153 0.2068 -0.0551 -0.0368 0.0428  243  ALA B CA  
10396 C C   . ALA B 245  ? 0.3100 0.2868 0.1778 -0.0610 -0.0388 0.0482  243  ALA B C   
10397 O O   . ALA B 245  ? 0.3136 0.2952 0.1764 -0.0649 -0.0369 0.0519  243  ALA B O   
10398 C CB  . ALA B 245  ? 0.3347 0.3229 0.2152 -0.0536 -0.0331 0.0403  243  ALA B CB  
10399 N N   . ILE B 246  ? 0.3376 0.3054 0.2068 -0.0619 -0.0426 0.0487  244  ILE B N   
10400 C CA  . ILE B 246  ? 0.3490 0.3119 0.2138 -0.0677 -0.0449 0.0537  244  ILE B CA  
10401 C C   . ILE B 246  ? 0.3443 0.3029 0.1997 -0.0702 -0.0472 0.0573  244  ILE B C   
10402 O O   . ILE B 246  ? 0.3725 0.3330 0.2231 -0.0756 -0.0467 0.0621  244  ILE B O   
10403 C CB  . ILE B 246  ? 0.3237 0.2765 0.1912 -0.0675 -0.0489 0.0531  244  ILE B CB  
10404 C CG1 . ILE B 246  ? 0.3194 0.2774 0.1951 -0.0667 -0.0463 0.0508  244  ILE B CG1 
10405 C CG2 . ILE B 246  ? 0.3564 0.3013 0.2175 -0.0732 -0.0525 0.0583  244  ILE B CG2 
10406 C CD1 . ILE B 246  ? 0.3356 0.2843 0.2145 -0.0653 -0.0499 0.0491  244  ILE B CD1 
10407 N N   . HIS B 247  ? 0.3476 0.3008 0.2004 -0.0663 -0.0498 0.0552  245  HIS B N   
10408 C CA  . HIS B 247  ? 0.3838 0.3333 0.2275 -0.0684 -0.0519 0.0586  245  HIS B CA  
10409 C C   . HIS B 247  ? 0.3474 0.3075 0.1874 -0.0704 -0.0474 0.0603  245  HIS B C   
10410 O O   . HIS B 247  ? 0.3742 0.3343 0.2074 -0.0752 -0.0477 0.0652  245  HIS B O   
10411 C CB  . HIS B 247  ? 0.3737 0.3165 0.2159 -0.0635 -0.0554 0.0556  245  HIS B CB  
10412 C CG  . HIS B 247  ? 0.3728 0.3042 0.2164 -0.0621 -0.0606 0.0551  245  HIS B CG  
10413 N ND1 . HIS B 247  ? 0.4248 0.3468 0.2628 -0.0659 -0.0646 0.0594  245  HIS B ND1 
10414 C CD2 . HIS B 247  ? 0.3992 0.3269 0.2490 -0.0572 -0.0623 0.0509  245  HIS B CD2 
10415 C CE1 . HIS B 247  ? 0.4414 0.3545 0.2821 -0.0630 -0.0686 0.0575  245  HIS B CE1 
10416 N NE2 . HIS B 247  ? 0.4238 0.3405 0.2718 -0.0578 -0.0671 0.0525  245  HIS B NE2 
10417 N N   . ALA B 248  ? 0.3324 0.3017 0.1769 -0.0667 -0.0431 0.0565  246  ALA B N   
10418 C CA  . ALA B 248  ? 0.3467 0.3264 0.1877 -0.0678 -0.0386 0.0578  246  ALA B CA  
10419 C C   . ALA B 248  ? 0.3348 0.3217 0.1765 -0.0733 -0.0356 0.0619  246  ALA B C   
10420 O O   . ALA B 248  ? 0.3610 0.3521 0.1966 -0.0772 -0.0341 0.0661  246  ALA B O   
10421 C CB  . ALA B 248  ? 0.3710 0.3581 0.2168 -0.0623 -0.0349 0.0525  246  ALA B CB  
10422 N N   . ILE B 249  ? 0.3652 0.3540 0.2146 -0.0736 -0.0346 0.0609  247  ILE B N   
10423 C CA  . ILE B 249  ? 0.3566 0.3527 0.2076 -0.0788 -0.0320 0.0647  247  ILE B CA  
10424 C C   . ILE B 249  ? 0.3581 0.3471 0.2027 -0.0852 -0.0356 0.0705  247  ILE B C   
10425 O O   . ILE B 249  ? 0.3790 0.3742 0.2202 -0.0904 -0.0336 0.0751  247  ILE B O   
10426 C CB  . ILE B 249  ? 0.3530 0.3513 0.2133 -0.0776 -0.0309 0.0622  247  ILE B CB  
10427 C CG1 . ILE B 249  ? 0.3306 0.3360 0.1968 -0.0715 -0.0273 0.0567  247  ILE B CG1 
10428 C CG2 . ILE B 249  ? 0.3407 0.3461 0.2026 -0.0836 -0.0288 0.0665  247  ILE B CG2 
10429 C CD1 . ILE B 249  ? 0.2976 0.3016 0.1725 -0.0689 -0.0276 0.0532  247  ILE B CD1 
10430 N N   . GLY B 250  ? 0.3727 0.3487 0.2158 -0.0849 -0.0409 0.0703  248  GLY B N   
10431 C CA  . GLY B 250  ? 0.4065 0.3741 0.2432 -0.0907 -0.0449 0.0757  248  GLY B CA  
10432 C C   . GLY B 250  ? 0.4384 0.4069 0.2659 -0.0936 -0.0448 0.0797  248  GLY B C   
10433 O O   . GLY B 250  ? 0.4275 0.3979 0.2507 -0.1000 -0.0446 0.0852  248  GLY B O   
10434 N N   . LYS B 251  ? 0.3977 0.3652 0.2219 -0.0892 -0.0450 0.0771  249  LYS B N   
10435 C CA  . LYS B 251  ? 0.4061 0.3747 0.2211 -0.0916 -0.0449 0.0807  249  LYS B CA  
10436 C C   . LYS B 251  ? 0.3735 0.3565 0.1881 -0.0943 -0.0390 0.0829  249  LYS B C   
10437 O O   . LYS B 251  ? 0.4251 0.4102 0.2330 -0.0996 -0.0385 0.0882  249  LYS B O   
10438 C CB  . LYS B 251  ? 0.4361 0.4010 0.2479 -0.0859 -0.0464 0.0771  249  LYS B CB  
10439 N N   . ALA B 252  ? 0.3806 0.3738 0.2024 -0.0906 -0.0343 0.0789  250  ALA B N   
10440 C CA  . ALA B 252  ? 0.4064 0.4141 0.2287 -0.0926 -0.0285 0.0808  250  ALA B CA  
10441 C C   . ALA B 252  ? 0.4442 0.4554 0.2678 -0.0997 -0.0279 0.0861  250  ALA B C   
10442 O O   . ALA B 252  ? 0.4445 0.4645 0.2645 -0.1040 -0.0250 0.0905  250  ALA B O   
10443 C CB  . ALA B 252  ? 0.4375 0.4543 0.2674 -0.0868 -0.0241 0.0752  250  ALA B CB  
10444 N N   . SER B 253  ? 0.4411 0.4462 0.2701 -0.1010 -0.0307 0.0857  251  SER B N   
10445 C CA  . SER B 253  ? 0.4443 0.4515 0.2744 -0.1081 -0.0309 0.0907  251  SER B CA  
10446 C C   . SER B 253  ? 0.4526 0.4554 0.2733 -0.1146 -0.0333 0.0972  251  SER B C   
10447 O O   . SER B 253  ? 0.4976 0.5082 0.3172 -0.1207 -0.0312 0.1023  251  SER B O   
10448 C CB  . SER B 253  ? 0.4384 0.4363 0.2737 -0.1082 -0.0347 0.0892  251  SER B CB  
10449 O OG  . SER B 253  ? 0.4464 0.4451 0.2818 -0.1155 -0.0355 0.0943  251  SER B OG  
10450 N N   . ALA B 254  ? 0.4578 0.4482 0.2718 -0.1135 -0.0379 0.0974  252  ALA B N   
10451 C CA  . ALA B 254  ? 0.4988 0.4841 0.3028 -0.1190 -0.0404 0.1033  252  ALA B CA  
10452 C C   . ALA B 254  ? 0.5211 0.5039 0.3242 -0.1272 -0.0424 0.1092  252  ALA B C   
10453 O O   . ALA B 254  ? 0.5014 0.4885 0.2990 -0.1335 -0.0414 0.1150  252  ALA B O   
10454 C CB  . ALA B 254  ? 0.4913 0.4879 0.2903 -0.1193 -0.0358 0.1051  252  ALA B CB  
10455 N N   . GLY B 255  ? 0.5209 0.4970 0.3296 -0.1273 -0.0451 0.1076  253  GLY B N   
10456 C CA  . GLY B 255  ? 0.5534 0.5244 0.3608 -0.1349 -0.0480 0.1126  253  GLY B CA  
10457 C C   . GLY B 255  ? 0.5341 0.5188 0.3467 -0.1398 -0.0438 0.1153  253  GLY B C   
10458 O O   . GLY B 255  ? 0.5360 0.5180 0.3467 -0.1473 -0.0460 0.1205  253  GLY B O   
10459 N N   . ARG B 256  ? 0.4353 0.4346 0.2546 -0.1359 -0.0380 0.1121  254  ARG B N   
10460 C CA  . ARG B 256  ? 0.4794 0.4928 0.3043 -0.1401 -0.0338 0.1145  254  ARG B CA  
10461 C C   . ARG B 256  ? 0.5356 0.5451 0.3672 -0.1418 -0.0360 0.1135  254  ARG B C   
10462 O O   . ARG B 256  ? 0.4867 0.5067 0.3230 -0.1462 -0.0335 0.1161  254  ARG B O   
10463 C CB  . ARG B 256  ? 0.5003 0.5294 0.3305 -0.1346 -0.0273 0.1107  254  ARG B CB  
10464 C CG  . ARG B 256  ? 0.5194 0.5577 0.3435 -0.1352 -0.0235 0.1134  254  ARG B CG  
10465 C CD  . ARG B 256  ? 0.4812 0.5343 0.3107 -0.1291 -0.0172 0.1092  254  ARG B CD  
10466 N NE  . ARG B 256  ? 0.5175 0.5647 0.3474 -0.1207 -0.0177 0.1026  254  ARG B NE  
10467 C CZ  . ARG B 256  ? 0.5157 0.5711 0.3514 -0.1142 -0.0137 0.0973  254  ARG B CZ  
10468 N NH1 . ARG B 256  ? 0.4604 0.5303 0.3023 -0.1144 -0.0087 0.0975  254  ARG B NH1 
10469 N NH2 . ARG B 256  ? 0.5407 0.5896 0.3761 -0.1072 -0.0148 0.0917  254  ARG B NH2 
10470 N N   . GLY B 257  ? 0.5169 0.5122 0.3491 -0.1383 -0.0406 0.1099  255  GLY B N   
10471 C CA  . GLY B 257  ? 0.4585 0.4487 0.2960 -0.1397 -0.0431 0.1088  255  GLY B CA  
10472 C C   . GLY B 257  ? 0.4782 0.4779 0.3256 -0.1344 -0.0392 0.1035  255  GLY B C   
10473 O O   . GLY B 257  ? 0.4470 0.4577 0.2976 -0.1296 -0.0344 0.1006  255  GLY B O   
10474 N N   . ILE B 258  ? 0.4400 0.4352 0.2922 -0.1355 -0.0414 0.1023  256  ILE B N   
10475 C CA  . ILE B 258  ? 0.4746 0.4752 0.3357 -0.1297 -0.0389 0.0966  256  ILE B CA  
10476 C C   . ILE B 258  ? 0.4252 0.4434 0.2930 -0.1311 -0.0335 0.0975  256  ILE B C   
10477 O O   . ILE B 258  ? 0.4012 0.4258 0.2761 -0.1256 -0.0306 0.0928  256  ILE B O   
10478 C CB  . ILE B 258  ? 0.4756 0.4641 0.3388 -0.1296 -0.0433 0.0946  256  ILE B CB  
10479 C CG1 . ILE B 258  ? 0.4927 0.4796 0.3546 -0.1383 -0.0458 0.0999  256  ILE B CG1 
10480 C CG2 . ILE B 258  ? 0.4522 0.4239 0.3100 -0.1263 -0.0483 0.0927  256  ILE B CG2 
10481 C CD1 . ILE B 258  ? 0.4607 0.4357 0.3242 -0.1383 -0.0501 0.0978  256  ILE B CD1 
10482 N N   . TYR B 259  ? 0.4342 0.4608 0.3000 -0.1382 -0.0320 0.1034  257  TYR B N   
10483 C CA  . TYR B 259  ? 0.3996 0.4439 0.2720 -0.1396 -0.0268 0.1046  257  TYR B CA  
10484 C C   . TYR B 259  ? 0.4202 0.4777 0.2916 -0.1371 -0.0214 0.1049  257  TYR B C   
10485 O O   . TYR B 259  ? 0.4558 0.5244 0.3332 -0.1318 -0.0168 0.1013  257  TYR B O   
10486 C CB  . TYR B 259  ? 0.4183 0.4654 0.2904 -0.1492 -0.0284 0.1109  257  TYR B CB  
10487 C CG  . TYR B 259  ? 0.4350 0.4676 0.3068 -0.1519 -0.0342 0.1107  257  TYR B CG  
10488 C CD1 . TYR B 259  ? 0.4762 0.5079 0.3550 -0.1482 -0.0344 0.1061  257  TYR B CD1 
10489 C CD2 . TYR B 259  ? 0.4651 0.4843 0.3291 -0.1580 -0.0395 0.1148  257  TYR B CD2 
10490 C CE1 . TYR B 259  ? 0.4933 0.5116 0.3713 -0.1502 -0.0396 0.1055  257  TYR B CE1 
10491 C CE2 . TYR B 259  ? 0.4731 0.4782 0.3362 -0.1600 -0.0449 0.1142  257  TYR B CE2 
10492 C CZ  . TYR B 259  ? 0.4993 0.5042 0.3694 -0.1560 -0.0448 0.1095  257  TYR B CZ  
10493 O OH  . TYR B 259  ? 0.4738 0.4648 0.3427 -0.1577 -0.0500 0.1086  257  TYR B OH  
10494 N N   . GLU B 260  ? 0.4034 0.4596 0.2668 -0.1406 -0.0218 0.1092  258  GLU B N   
10495 C CA  . GLU B 260  ? 0.4579 0.5256 0.3192 -0.1378 -0.0168 0.1092  258  GLU B CA  
10496 C C   . GLU B 260  ? 0.5022 0.5645 0.3624 -0.1290 -0.0165 0.1030  258  GLU B C   
10497 O O   . GLU B 260  ? 0.5441 0.6168 0.4070 -0.1235 -0.0117 0.0998  258  GLU B O   
10498 C CB  . GLU B 260  ? 0.4667 0.5344 0.3194 -0.1444 -0.0175 0.1157  258  GLU B CB  
10499 N N   . GLY B 261  ? 0.4666 0.5126 0.3228 -0.1273 -0.0216 0.1011  259  GLY B N   
10500 C CA  . GLY B 261  ? 0.4161 0.4563 0.2705 -0.1198 -0.0219 0.0959  259  GLY B CA  
10501 C C   . GLY B 261  ? 0.4199 0.4600 0.2822 -0.1129 -0.0210 0.0894  259  GLY B C   
10502 O O   . GLY B 261  ? 0.3741 0.4153 0.2430 -0.1139 -0.0213 0.0886  259  GLY B O   
10503 N N   . PRO B 262  ? 0.3896 0.4279 0.2512 -0.1060 -0.0201 0.0847  260  PRO B N   
10504 C CA  . PRO B 262  ? 0.3485 0.3874 0.2174 -0.0992 -0.0190 0.0784  260  PRO B CA  
10505 C C   . PRO B 262  ? 0.3594 0.3846 0.2302 -0.0981 -0.0240 0.0761  260  PRO B C   
10506 O O   . PRO B 262  ? 0.4197 0.4331 0.2852 -0.1010 -0.0287 0.0783  260  PRO B O   
10507 C CB  . PRO B 262  ? 0.3518 0.3917 0.2176 -0.0932 -0.0172 0.0748  260  PRO B CB  
10508 C CG  . PRO B 262  ? 0.3552 0.3870 0.2115 -0.0963 -0.0204 0.0784  260  PRO B CG  
10509 C CD  . PRO B 262  ? 0.3871 0.4228 0.2408 -0.1044 -0.0203 0.0850  260  PRO B CD  
10510 N N   . GLY B 263  ? 0.3354 0.3623 0.2138 -0.0935 -0.0228 0.0714  261  GLY B N   
10511 C CA  . GLY B 263  ? 0.3272 0.3424 0.2081 -0.0912 -0.0269 0.0684  261  GLY B CA  
10512 C C   . GLY B 263  ? 0.3277 0.3429 0.2133 -0.0835 -0.0256 0.0621  261  GLY B C   
10513 O O   . GLY B 263  ? 0.3510 0.3738 0.2370 -0.0798 -0.0220 0.0600  261  GLY B O   
10514 N N   . ILE B 264  ? 0.3045 0.3110 0.1934 -0.0811 -0.0285 0.0592  262  ILE B N   
10515 C CA  . ILE B 264  ? 0.3163 0.3222 0.2102 -0.0743 -0.0277 0.0534  262  ILE B CA  
10516 C C   . ILE B 264  ? 0.3391 0.3454 0.2402 -0.0736 -0.0276 0.0514  262  ILE B C   
10517 O O   . ILE B 264  ? 0.3225 0.3248 0.2236 -0.0778 -0.0298 0.0539  262  ILE B O   
10518 C CB  . ILE B 264  ? 0.3623 0.3565 0.2525 -0.0710 -0.0317 0.0514  262  ILE B CB  
10519 C CG1 . ILE B 264  ? 0.3257 0.3213 0.2205 -0.0642 -0.0303 0.0458  262  ILE B CG1 
10520 C CG2 . ILE B 264  ? 0.3458 0.3281 0.2350 -0.0731 -0.0366 0.0524  262  ILE B CG2 
10521 C CD1 . ILE B 264  ? 0.3276 0.3135 0.2192 -0.0607 -0.0340 0.0437  262  ILE B CD1 
10522 N N   . SER B 265  ? 0.2860 0.2972 0.1930 -0.0683 -0.0249 0.0470  263  SER B N   
10523 C CA  . SER B 265  ? 0.2924 0.3041 0.2064 -0.0666 -0.0246 0.0444  263  SER B CA  
10524 C C   . SER B 265  ? 0.2868 0.2921 0.2032 -0.0607 -0.0260 0.0396  263  SER B C   
10525 O O   . SER B 265  ? 0.2957 0.3026 0.2114 -0.0569 -0.0248 0.0372  263  SER B O   
10526 C CB  . SER B 265  ? 0.3157 0.3405 0.2350 -0.0660 -0.0198 0.0439  263  SER B CB  
10527 O OG  . SER B 265  ? 0.3224 0.3532 0.2410 -0.0718 -0.0188 0.0485  263  SER B OG  
10528 N N   . ILE B 266  ? 0.2771 0.2752 0.1962 -0.0601 -0.0286 0.0381  264  ILE B N   
10529 C CA  . ILE B 266  ? 0.2757 0.2680 0.1976 -0.0548 -0.0301 0.0338  264  ILE B CA  
10530 C C   . ILE B 266  ? 0.3123 0.3068 0.2412 -0.0531 -0.0289 0.0313  264  ILE B C   
10531 O O   . ILE B 266  ? 0.2864 0.2834 0.2168 -0.0565 -0.0284 0.0332  264  ILE B O   
10532 C CB  . ILE B 266  ? 0.2585 0.2382 0.1762 -0.0549 -0.0350 0.0342  264  ILE B CB  
10533 C CG1 . ILE B 266  ? 0.3201 0.2938 0.2374 -0.0585 -0.0376 0.0361  264  ILE B CG1 
10534 C CG2 . ILE B 266  ? 0.3053 0.2823 0.2157 -0.0567 -0.0365 0.0369  264  ILE B CG2 
10535 C CD1 . ILE B 266  ? 0.3816 0.3424 0.2952 -0.0578 -0.0425 0.0361  264  ILE B CD1 
10536 N N   . LYS B 267  ? 0.2860 0.2796 0.2189 -0.0479 -0.0284 0.0271  265  LYS B N   
10537 C CA  . LYS B 267  ? 0.2793 0.2733 0.2183 -0.0458 -0.0278 0.0245  265  LYS B CA  
10538 C C   . LYS B 267  ? 0.2775 0.2613 0.2165 -0.0434 -0.0314 0.0225  265  LYS B C   
10539 O O   . LYS B 267  ? 0.2901 0.2703 0.2279 -0.0404 -0.0327 0.0209  265  LYS B O   
10540 C CB  . LYS B 267  ? 0.2923 0.2942 0.2364 -0.0418 -0.0241 0.0213  265  LYS B CB  
10541 C CG  . LYS B 267  ? 0.3187 0.3313 0.2638 -0.0436 -0.0203 0.0230  265  LYS B CG  
10542 C CD  . LYS B 267  ? 0.4273 0.4468 0.3778 -0.0394 -0.0169 0.0198  265  LYS B CD  
10543 C CE  . LYS B 267  ? 0.4831 0.5134 0.4340 -0.0405 -0.0131 0.0214  265  LYS B CE  
10544 N NZ  . LYS B 267  ? 0.4529 0.4846 0.3977 -0.0427 -0.0130 0.0240  265  LYS B NZ  
10545 N N   . LEU B 268  ? 0.2845 0.2639 0.2249 -0.0446 -0.0330 0.0226  266  LEU B N   
10546 C CA  . LEU B 268  ? 0.2846 0.2547 0.2251 -0.0419 -0.0362 0.0206  266  LEU B CA  
10547 C C   . LEU B 268  ? 0.2703 0.2422 0.2160 -0.0364 -0.0349 0.0164  266  LEU B C   
10548 O O   . LEU B 268  ? 0.2717 0.2377 0.2172 -0.0334 -0.0372 0.0147  266  LEU B O   
10549 C CB  . LEU B 268  ? 0.2303 0.1958 0.1711 -0.0440 -0.0378 0.0212  266  LEU B CB  
10550 C CG  . LEU B 268  ? 0.2882 0.2499 0.2232 -0.0498 -0.0399 0.0254  266  LEU B CG  
10551 C CD1 . LEU B 268  ? 0.2964 0.2522 0.2314 -0.0516 -0.0420 0.0256  266  LEU B CD1 
10552 C CD2 . LEU B 268  ? 0.3177 0.2717 0.2466 -0.0504 -0.0432 0.0271  266  LEU B CD2 
10553 N N   . SER B 269  ? 0.2620 0.2423 0.2127 -0.0350 -0.0313 0.0148  267  SER B N   
10554 C CA  . SER B 269  ? 0.2521 0.2342 0.2077 -0.0302 -0.0301 0.0111  267  SER B CA  
10555 C C   . SER B 269  ? 0.2327 0.2145 0.1865 -0.0279 -0.0305 0.0101  267  SER B C   
10556 O O   . SER B 269  ? 0.2935 0.2746 0.2505 -0.0242 -0.0307 0.0072  267  SER B O   
10557 C CB  . SER B 269  ? 0.2586 0.2494 0.2192 -0.0293 -0.0262 0.0098  267  SER B CB  
10558 O OG  . SER B 269  ? 0.2415 0.2391 0.2007 -0.0301 -0.0238 0.0108  267  SER B OG  
10559 N N   . ALA B 270  ? 0.2271 0.2095 0.1757 -0.0303 -0.0308 0.0126  268  ALA B N   
10560 C CA  . ALA B 270  ? 0.2681 0.2494 0.2140 -0.0285 -0.0317 0.0119  268  ALA B CA  
10561 C C   . ALA B 270  ? 0.2612 0.2336 0.2048 -0.0274 -0.0359 0.0118  268  ALA B C   
10562 O O   . ALA B 270  ? 0.2627 0.2337 0.2058 -0.0248 -0.0371 0.0103  268  ALA B O   
10563 C CB  . ALA B 270  ? 0.2842 0.2689 0.2246 -0.0314 -0.0307 0.0147  268  ALA B CB  
10564 N N   . LEU B 271  ? 0.2439 0.2102 0.1861 -0.0291 -0.0383 0.0132  269  LEU B N   
10565 C CA  . LEU B 271  ? 0.2693 0.2265 0.2078 -0.0286 -0.0425 0.0139  269  LEU B CA  
10566 C C   . LEU B 271  ? 0.2864 0.2394 0.2292 -0.0248 -0.0441 0.0111  269  LEU B C   
10567 O O   . LEU B 271  ? 0.3020 0.2478 0.2425 -0.0235 -0.0476 0.0113  269  LEU B O   
10568 C CB  . LEU B 271  ? 0.2679 0.2198 0.2008 -0.0331 -0.0446 0.0176  269  LEU B CB  
10569 C CG  . LEU B 271  ? 0.3038 0.2597 0.2318 -0.0369 -0.0434 0.0208  269  LEU B CG  
10570 C CD1 . LEU B 271  ? 0.3589 0.3099 0.2818 -0.0420 -0.0454 0.0248  269  LEU B CD1 
10571 C CD2 . LEU B 271  ? 0.3061 0.2609 0.2305 -0.0354 -0.0447 0.0209  269  LEU B CD2 
10572 N N   . HIS B 272  ? 0.2555 0.2131 0.2044 -0.0228 -0.0416 0.0086  270  HIS B N   
10573 C CA  . HIS B 272  ? 0.2722 0.2267 0.2253 -0.0191 -0.0427 0.0060  270  HIS B CA  
10574 C C   . HIS B 272  ? 0.2743 0.2360 0.2340 -0.0169 -0.0393 0.0033  270  HIS B C   
10575 O O   . HIS B 272  ? 0.2701 0.2371 0.2310 -0.0187 -0.0365 0.0037  270  HIS B O   
10576 C CB  . HIS B 272  ? 0.2909 0.2391 0.2428 -0.0200 -0.0445 0.0067  270  HIS B CB  
10577 C CG  . HIS B 272  ? 0.3421 0.2853 0.2965 -0.0160 -0.0466 0.0045  270  HIS B CG  
10578 N ND1 . HIS B 272  ? 0.3050 0.2518 0.2657 -0.0128 -0.0448 0.0015  270  HIS B ND1 
10579 C CD2 . HIS B 272  ? 0.3253 0.2606 0.2767 -0.0145 -0.0504 0.0048  270  HIS B CD2 
10580 C CE1 . HIS B 272  ? 0.3489 0.2907 0.3106 -0.0095 -0.0471 0.0001  270  HIS B CE1 
10581 N NE2 . HIS B 272  ? 0.3756 0.3104 0.3318 -0.0103 -0.0506 0.0020  270  HIS B NE2 
10582 N N   . PRO B 273  ? 0.2672 0.2295 0.2311 -0.0130 -0.0396 0.0006  271  PRO B N   
10583 C CA  . PRO B 273  ? 0.2689 0.2376 0.2389 -0.0112 -0.0364 -0.0018 271  PRO B CA  
10584 C C   . PRO B 273  ? 0.2542 0.2230 0.2275 -0.0109 -0.0352 -0.0026 271  PRO B C   
10585 O O   . PRO B 273  ? 0.2629 0.2372 0.2404 -0.0102 -0.0324 -0.0039 271  PRO B O   
10586 C CB  . PRO B 273  ? 0.2677 0.2363 0.2408 -0.0076 -0.0377 -0.0040 271  PRO B CB  
10587 C CG  . PRO B 273  ? 0.3086 0.2701 0.2788 -0.0069 -0.0415 -0.0032 271  PRO B CG  
10588 C CD  . PRO B 273  ? 0.3090 0.2668 0.2725 -0.0105 -0.0427 -0.0001 271  PRO B CD  
10589 N N   . ARG B 274  ? 0.2610 0.2236 0.2322 -0.0113 -0.0374 -0.0018 272  ARG B N   
10590 C CA  . ARG B 274  ? 0.2287 0.1911 0.2026 -0.0110 -0.0364 -0.0027 272  ARG B CA  
10591 C C   . ARG B 274  ? 0.2979 0.2570 0.2673 -0.0149 -0.0371 -0.0003 272  ARG B C   
10592 O O   . ARG B 274  ? 0.2957 0.2485 0.2632 -0.0148 -0.0392 -0.0002 272  ARG B O   
10593 C CB  . ARG B 274  ? 0.2583 0.2161 0.2342 -0.0074 -0.0382 -0.0047 272  ARG B CB  
10594 C CG  . ARG B 274  ? 0.2924 0.2541 0.2737 -0.0037 -0.0375 -0.0070 272  ARG B CG  
10595 C CD  . ARG B 274  ? 0.2747 0.2439 0.2609 -0.0035 -0.0339 -0.0083 272  ARG B CD  
10596 N NE  . ARG B 274  ? 0.2673 0.2373 0.2553 -0.0038 -0.0322 -0.0088 272  ARG B NE  
10597 C CZ  . ARG B 274  ? 0.2889 0.2578 0.2799 -0.0012 -0.0322 -0.0105 272  ARG B CZ  
10598 N NH1 . ARG B 274  ? 0.2748 0.2418 0.2678 0.0020  -0.0338 -0.0118 272  ARG B NH1 
10599 N NH2 . ARG B 274  ? 0.2440 0.2139 0.2361 -0.0018 -0.0305 -0.0109 272  ARG B NH2 
10600 N N   . TYR B 275  ? 0.2523 0.2158 0.2199 -0.0182 -0.0355 0.0016  273  TYR B N   
10601 C CA  . TYR B 275  ? 0.2922 0.2536 0.2558 -0.0225 -0.0362 0.0043  273  TYR B CA  
10602 C C   . TYR B 275  ? 0.2656 0.2306 0.2326 -0.0231 -0.0341 0.0036  273  TYR B C   
10603 O O   . TYR B 275  ? 0.2553 0.2278 0.2249 -0.0240 -0.0311 0.0037  273  TYR B O   
10604 C CB  . TYR B 275  ? 0.2503 0.2155 0.2106 -0.0259 -0.0354 0.0069  273  TYR B CB  
10605 C CG  . TYR B 275  ? 0.2828 0.2475 0.2398 -0.0307 -0.0357 0.0100  273  TYR B CG  
10606 C CD1 . TYR B 275  ? 0.2819 0.2382 0.2350 -0.0326 -0.0389 0.0112  273  TYR B CD1 
10607 C CD2 . TYR B 275  ? 0.2805 0.2532 0.2382 -0.0334 -0.0329 0.0116  273  TYR B CD2 
10608 C CE1 . TYR B 275  ? 0.2975 0.2532 0.2474 -0.0375 -0.0395 0.0141  273  TYR B CE1 
10609 C CE2 . TYR B 275  ? 0.3088 0.2820 0.2639 -0.0382 -0.0333 0.0146  273  TYR B CE2 
10610 C CZ  . TYR B 275  ? 0.3085 0.2731 0.2597 -0.0405 -0.0366 0.0159  273  TYR B CZ  
10611 O OH  . TYR B 275  ? 0.2760 0.2408 0.2245 -0.0456 -0.0372 0.0190  273  TYR B OH  
10612 N N   . SER B 276  ? 0.2523 0.2117 0.2191 -0.0223 -0.0356 0.0027  274  SER B N   
10613 C CA  . SER B 276  ? 0.2920 0.2539 0.2615 -0.0228 -0.0340 0.0019  274  SER B CA  
10614 C C   . SER B 276  ? 0.2929 0.2462 0.2592 -0.0229 -0.0367 0.0016  274  SER B C   
10615 O O   . SER B 276  ? 0.2681 0.2142 0.2319 -0.0211 -0.0394 0.0011  274  SER B O   
10616 C CB  . SER B 276  ? 0.3172 0.2845 0.2929 -0.0189 -0.0313 -0.0010 274  SER B CB  
10617 O OG  . SER B 276  ? 0.2966 0.2591 0.2733 -0.0151 -0.0328 -0.0031 274  SER B OG  
10618 N N   . ARG B 277  ? 0.2521 0.2064 0.2188 -0.0249 -0.0360 0.0019  275  ARG B N   
10619 C CA  . ARG B 277  ? 0.2540 0.2001 0.2174 -0.0251 -0.0385 0.0014  275  ARG B CA  
10620 C C   . ARG B 277  ? 0.2840 0.2265 0.2494 -0.0198 -0.0389 -0.0018 275  ARG B C   
10621 O O   . ARG B 277  ? 0.2738 0.2074 0.2354 -0.0186 -0.0418 -0.0023 275  ARG B O   
10622 C CB  . ARG B 277  ? 0.2422 0.1911 0.2063 -0.0278 -0.0374 0.0019  275  ARG B CB  
10623 C CG  . ARG B 277  ? 0.2830 0.2235 0.2438 -0.0276 -0.0398 0.0008  275  ARG B CG  
10624 C CD  . ARG B 277  ? 0.2943 0.2244 0.2482 -0.0298 -0.0439 0.0024  275  ARG B CD  
10625 N NE  . ARG B 277  ? 0.3016 0.2230 0.2517 -0.0294 -0.0462 0.0012  275  ARG B NE  
10626 C CZ  . ARG B 277  ? 0.2969 0.2122 0.2464 -0.0247 -0.0473 -0.0015 275  ARG B CZ  
10627 N NH1 . ARG B 277  ? 0.3028 0.2201 0.2557 -0.0201 -0.0463 -0.0032 275  ARG B NH1 
10628 N NH2 . ARG B 277  ? 0.2866 0.1938 0.2319 -0.0246 -0.0495 -0.0026 275  ARG B NH2 
10629 N N   . ALA B 278  ? 0.2812 0.2303 0.2525 -0.0165 -0.0361 -0.0039 276  ALA B N   
10630 C CA  . ALA B 278  ? 0.2999 0.2468 0.2736 -0.0116 -0.0362 -0.0067 276  ALA B CA  
10631 C C   . ALA B 278  ? 0.2967 0.2382 0.2684 -0.0094 -0.0388 -0.0068 276  ALA B C   
10632 O O   . ALA B 278  ? 0.2964 0.2331 0.2681 -0.0058 -0.0402 -0.0086 276  ALA B O   
10633 C CB  . ALA B 278  ? 0.2980 0.2534 0.2784 -0.0090 -0.0328 -0.0085 276  ALA B CB  
10634 N N   . GLN B 279  ? 0.2649 0.2073 0.2350 -0.0112 -0.0395 -0.0049 277  GLN B N   
10635 C CA  . GLN B 279  ? 0.2669 0.2043 0.2348 -0.0094 -0.0422 -0.0047 277  GLN B CA  
10636 C C   . GLN B 279  ? 0.2858 0.2151 0.2465 -0.0127 -0.0455 -0.0022 277  GLN B C   
10637 O O   . GLN B 279  ? 0.2906 0.2174 0.2487 -0.0130 -0.0474 -0.0008 277  GLN B O   
10638 C CB  . GLN B 279  ? 0.2877 0.2315 0.2587 -0.0087 -0.0408 -0.0047 277  GLN B CB  
10639 C CG  . GLN B 279  ? 0.2770 0.2278 0.2548 -0.0054 -0.0380 -0.0072 277  GLN B CG  
10640 C CD  . GLN B 279  ? 0.3163 0.2642 0.2965 -0.0009 -0.0390 -0.0094 277  GLN B CD  
10641 O OE1 . GLN B 279  ? 0.3728 0.3150 0.3506 0.0008  -0.0419 -0.0093 277  GLN B OE1 
10642 N NE2 . GLN B 279  ? 0.2769 0.2290 0.2619 0.0012  -0.0367 -0.0114 277  GLN B NE2 
10643 N N   . ALA B 280  ? 0.2847 0.2096 0.2421 -0.0152 -0.0464 -0.0014 278  ALA B N   
10644 C CA  . ALA B 280  ? 0.3243 0.2419 0.2748 -0.0194 -0.0495 0.0014  278  ALA B CA  
10645 C C   . ALA B 280  ? 0.3285 0.2369 0.2747 -0.0173 -0.0533 0.0016  278  ALA B C   
10646 O O   . ALA B 280  ? 0.3006 0.2051 0.2420 -0.0202 -0.0555 0.0043  278  ALA B O   
10647 C CB  . ALA B 280  ? 0.2772 0.1905 0.2249 -0.0219 -0.0503 0.0016  278  ALA B CB  
10648 N N   . ALA B 281  ? 0.3463 0.2515 0.2943 -0.0120 -0.0540 -0.0012 279  ALA B N   
10649 C CA  . ALA B 281  ? 0.3743 0.2709 0.3186 -0.0094 -0.0577 -0.0011 279  ALA B CA  
10650 C C   . ALA B 281  ? 0.3183 0.2183 0.2634 -0.0092 -0.0580 0.0002  279  ALA B C   
10651 O O   . ALA B 281  ? 0.3358 0.2292 0.2756 -0.0106 -0.0612 0.0023  279  ALA B O   
10652 C CB  . ALA B 281  ? 0.3627 0.2568 0.3096 -0.0034 -0.0580 -0.0044 279  ALA B CB  
10653 N N   . ARG B 282  ? 0.2898 0.1994 0.2412 -0.0075 -0.0549 -0.0011 280  ARG B N   
10654 C CA  . ARG B 282  ? 0.3363 0.2493 0.2881 -0.0077 -0.0551 0.0000  280  ARG B CA  
10655 C C   . ARG B 282  ? 0.3145 0.2282 0.2619 -0.0132 -0.0552 0.0033  280  ARG B C   
10656 O O   . ARG B 282  ? 0.3415 0.2532 0.2855 -0.0142 -0.0570 0.0051  280  ARG B O   
10657 C CB  . ARG B 282  ? 0.3623 0.2852 0.3214 -0.0052 -0.0518 -0.0021 280  ARG B CB  
10658 C CG  . ARG B 282  ? 0.3493 0.2728 0.3133 0.0002  -0.0517 -0.0051 280  ARG B CG  
10659 C CD  . ARG B 282  ? 0.3452 0.2777 0.3157 0.0020  -0.0492 -0.0066 280  ARG B CD  
10660 N NE  . ARG B 282  ? 0.3662 0.2993 0.3352 0.0015  -0.0507 -0.0054 280  ARG B NE  
10661 C CZ  . ARG B 282  ? 0.3506 0.2907 0.3232 0.0017  -0.0489 -0.0059 280  ARG B CZ  
10662 N NH1 . ARG B 282  ? 0.3323 0.2795 0.3105 0.0024  -0.0456 -0.0076 280  ARG B NH1 
10663 N NH2 . ARG B 282  ? 0.3745 0.3142 0.3447 0.0012  -0.0507 -0.0048 280  ARG B NH2 
10664 N N   . VAL B 283  ? 0.3041 0.2214 0.2516 -0.0169 -0.0530 0.0042  281  VAL B N   
10665 C CA  . VAL B 283  ? 0.2923 0.2114 0.2360 -0.0222 -0.0527 0.0075  281  VAL B CA  
10666 C C   . VAL B 283  ? 0.3194 0.2283 0.2555 -0.0250 -0.0568 0.0102  281  VAL B C   
10667 O O   . VAL B 283  ? 0.3452 0.2532 0.2775 -0.0272 -0.0580 0.0127  281  VAL B O   
10668 C CB  . VAL B 283  ? 0.2993 0.2243 0.2451 -0.0253 -0.0498 0.0078  281  VAL B CB  
10669 C CG1 . VAL B 283  ? 0.3312 0.2572 0.2726 -0.0313 -0.0500 0.0117  281  VAL B CG1 
10670 C CG2 . VAL B 283  ? 0.2687 0.2041 0.2215 -0.0230 -0.0458 0.0057  281  VAL B CG2 
10671 N N   . MET B 284  ? 0.2765 0.1771 0.2098 -0.0247 -0.0591 0.0097  282  MET B N   
10672 C CA  . MET B 284  ? 0.3398 0.2294 0.2655 -0.0273 -0.0633 0.0123  282  MET B CA  
10673 C C   . MET B 284  ? 0.3712 0.2552 0.2947 -0.0239 -0.0663 0.0122  282  MET B C   
10674 O O   . MET B 284  ? 0.3714 0.2490 0.2887 -0.0266 -0.0693 0.0151  282  MET B O   
10675 C CB  . MET B 284  ? 0.3427 0.2240 0.2656 -0.0273 -0.0653 0.0114  282  MET B CB  
10676 C CG  . MET B 284  ? 0.3362 0.2223 0.2608 -0.0310 -0.0629 0.0117  282  MET B CG  
10677 S SD  . MET B 284  ? 0.4022 0.2927 0.3236 -0.0388 -0.0624 0.0164  282  MET B SD  
10678 C CE  . MET B 284  ? 0.4159 0.2915 0.3275 -0.0426 -0.0680 0.0194  282  MET B CE  
10679 N N   . GLY B 285  ? 0.3607 0.2470 0.2891 -0.0181 -0.0656 0.0091  283  GLY B N   
10680 C CA  . GLY B 285  ? 0.3571 0.2383 0.2839 -0.0145 -0.0687 0.0089  283  GLY B CA  
10681 C C   . GLY B 285  ? 0.3948 0.2817 0.3224 -0.0150 -0.0680 0.0101  283  GLY B C   
10682 O O   . GLY B 285  ? 0.3738 0.2553 0.2974 -0.0144 -0.0712 0.0115  283  GLY B O   
10683 N N   . GLU B 286  ? 0.3491 0.2467 0.2815 -0.0160 -0.0641 0.0095  284  GLU B N   
10684 C CA  . GLU B 286  ? 0.3369 0.2403 0.2705 -0.0156 -0.0633 0.0099  284  GLU B CA  
10685 C C   . GLU B 286  ? 0.3302 0.2391 0.2616 -0.0206 -0.0611 0.0124  284  GLU B C   
10686 O O   . GLU B 286  ? 0.3827 0.2921 0.3109 -0.0217 -0.0620 0.0141  284  GLU B O   
10687 C CB  . GLU B 286  ? 0.3167 0.2280 0.2583 -0.0112 -0.0607 0.0064  284  GLU B CB  
10688 C CG  . GLU B 286  ? 0.3478 0.2552 0.2923 -0.0060 -0.0624 0.0039  284  GLU B CG  
10689 C CD  . GLU B 286  ? 0.4186 0.3341 0.3712 -0.0025 -0.0593 0.0007  284  GLU B CD  
10690 O OE1 . GLU B 286  ? 0.4034 0.3269 0.3591 -0.0034 -0.0567 0.0003  284  GLU B OE1 
10691 O OE2 . GLU B 286  ? 0.4770 0.3910 0.4327 0.0010  -0.0595 -0.0015 284  GLU B OE2 
10692 N N   . LEU B 287  ? 0.3341 0.2476 0.2671 -0.0234 -0.0583 0.0127  285  LEU B N   
10693 C CA  . LEU B 287  ? 0.3252 0.2449 0.2566 -0.0280 -0.0560 0.0151  285  LEU B CA  
10694 C C   . LEU B 287  ? 0.3441 0.2573 0.2680 -0.0331 -0.0586 0.0191  285  LEU B C   
10695 O O   . LEU B 287  ? 0.3259 0.2406 0.2459 -0.0358 -0.0587 0.0217  285  LEU B O   
10696 C CB  . LEU B 287  ? 0.3088 0.2362 0.2451 -0.0290 -0.0521 0.0140  285  LEU B CB  
10697 C CG  . LEU B 287  ? 0.3629 0.3003 0.3006 -0.0315 -0.0484 0.0150  285  LEU B CG  
10698 C CD1 . LEU B 287  ? 0.3145 0.2585 0.2577 -0.0312 -0.0451 0.0134  285  LEU B CD1 
10699 C CD2 . LEU B 287  ? 0.3424 0.2793 0.2743 -0.0369 -0.0490 0.0191  285  LEU B CD2 
10700 N N   . LEU B 288  ? 0.3329 0.2386 0.2543 -0.0344 -0.0607 0.0196  286  LEU B N   
10701 C CA  . LEU B 288  ? 0.3543 0.2532 0.2685 -0.0396 -0.0634 0.0236  286  LEU B CA  
10702 C C   . LEU B 288  ? 0.3569 0.2498 0.2653 -0.0399 -0.0666 0.0258  286  LEU B C   
10703 O O   . LEU B 288  ? 0.3553 0.2493 0.2592 -0.0447 -0.0667 0.0294  286  LEU B O   
10704 C CB  . LEU B 288  ? 0.3225 0.2123 0.2347 -0.0399 -0.0659 0.0231  286  LEU B CB  
10705 C CG  . LEU B 288  ? 0.4385 0.3190 0.3428 -0.0452 -0.0696 0.0270  286  LEU B CG  
10706 C CD1 . LEU B 288  ? 0.3963 0.2839 0.2994 -0.0517 -0.0674 0.0305  286  LEU B CD1 
10707 C CD2 . LEU B 288  ? 0.4811 0.3527 0.3839 -0.0447 -0.0718 0.0256  286  LEU B CD2 
10708 N N   . PRO B 289  ? 0.3954 0.2825 0.3036 -0.0352 -0.0693 0.0241  287  PRO B N   
10709 C CA  . PRO B 289  ? 0.3859 0.2675 0.2883 -0.0356 -0.0725 0.0265  287  PRO B CA  
10710 C C   . PRO B 289  ? 0.3981 0.2881 0.3002 -0.0374 -0.0702 0.0279  287  PRO B C   
10711 O O   . PRO B 289  ? 0.3821 0.2688 0.2779 -0.0405 -0.0721 0.0313  287  PRO B O   
10712 C CB  . PRO B 289  ? 0.4459 0.3227 0.3505 -0.0292 -0.0749 0.0235  287  PRO B CB  
10713 C CG  . PRO B 289  ? 0.4107 0.2860 0.3193 -0.0266 -0.0743 0.0206  287  PRO B CG  
10714 C CD  . PRO B 289  ? 0.3859 0.2710 0.2989 -0.0292 -0.0697 0.0201  287  PRO B CD  
10715 N N   . ARG B 290  ? 0.3549 0.2554 0.2633 -0.0356 -0.0661 0.0255  288  ARG B N   
10716 C CA  A ARG B 290  ? 0.3873 0.2960 0.2952 -0.0370 -0.0636 0.0265  288  ARG B CA  
10717 C CA  B ARG B 290  ? 0.3873 0.2959 0.2951 -0.0370 -0.0636 0.0265  288  ARG B CA  
10718 C C   . ARG B 290  ? 0.3515 0.2639 0.2560 -0.0431 -0.0617 0.0301  288  ARG B C   
10719 O O   . ARG B 290  ? 0.3237 0.2373 0.2233 -0.0459 -0.0619 0.0330  288  ARG B O   
10720 C CB  A ARG B 290  ? 0.3684 0.2865 0.2837 -0.0333 -0.0599 0.0228  288  ARG B CB  
10721 C CB  B ARG B 290  ? 0.3686 0.2866 0.2839 -0.0333 -0.0600 0.0228  288  ARG B CB  
10722 C CG  A ARG B 290  ? 0.4105 0.3266 0.3283 -0.0279 -0.0618 0.0201  288  ARG B CG  
10723 C CG  B ARG B 290  ? 0.4057 0.3211 0.3243 -0.0276 -0.0618 0.0197  288  ARG B CG  
10724 C CD  A ARG B 290  ? 0.4162 0.3401 0.3418 -0.0243 -0.0585 0.0163  288  ARG B CD  
10725 C CD  B ARG B 290  ? 0.4159 0.3393 0.3424 -0.0242 -0.0584 0.0160  288  ARG B CD  
10726 N NE  A ARG B 290  ? 0.4292 0.3543 0.3567 -0.0206 -0.0596 0.0144  288  ARG B NE  
10727 N NE  B ARG B 290  ? 0.3926 0.3140 0.3228 -0.0191 -0.0603 0.0132  288  ARG B NE  
10728 C CZ  A ARG B 290  ? 0.3927 0.3239 0.3265 -0.0173 -0.0575 0.0112  288  ARG B CZ  
10729 C CZ  B ARG B 290  ? 0.4044 0.3307 0.3416 -0.0157 -0.0582 0.0099  288  ARG B CZ  
10730 N NH1 A ARG B 290  ? 0.3914 0.3281 0.3304 -0.0170 -0.0541 0.0094  288  ARG B NH1 
10731 N NH1 B ARG B 290  ? 0.3880 0.3211 0.3292 -0.0165 -0.0544 0.0088  288  ARG B NH1 
10732 N NH2 A ARG B 290  ? 0.4116 0.3434 0.3463 -0.0145 -0.0590 0.0099  288  ARG B NH2 
10733 N NH2 B ARG B 290  ? 0.4324 0.3571 0.3728 -0.0113 -0.0601 0.0078  288  ARG B NH2 
10734 N N   . VAL B 291  ? 0.3292 0.2440 0.2363 -0.0453 -0.0600 0.0301  289  VAL B N   
10735 C CA  . VAL B 291  ? 0.3368 0.2553 0.2410 -0.0514 -0.0585 0.0338  289  VAL B CA  
10736 C C   . VAL B 291  ? 0.3335 0.2426 0.2295 -0.0556 -0.0626 0.0380  289  VAL B C   
10737 O O   . VAL B 291  ? 0.3492 0.2612 0.2409 -0.0602 -0.0620 0.0417  289  VAL B O   
10738 C CB  . VAL B 291  ? 0.3672 0.2887 0.2753 -0.0532 -0.0567 0.0332  289  VAL B CB  
10739 C CG1 . VAL B 291  ? 0.3526 0.2806 0.2589 -0.0593 -0.0546 0.0370  289  VAL B CG1 
10740 C CG2 . VAL B 291  ? 0.3743 0.3031 0.2902 -0.0486 -0.0534 0.0290  289  VAL B CG2 
10741 N N   . LYS B 292  ? 0.3443 0.2419 0.2377 -0.0540 -0.0668 0.0375  290  LYS B N   
10742 C CA  . LYS B 292  ? 0.3731 0.2605 0.2585 -0.0580 -0.0710 0.0415  290  LYS B CA  
10743 C C   . LYS B 292  ? 0.3674 0.2542 0.2479 -0.0584 -0.0721 0.0437  290  LYS B C   
10744 O O   . LYS B 292  ? 0.3685 0.2533 0.2426 -0.0637 -0.0733 0.0481  290  LYS B O   
10745 C CB  . LYS B 292  ? 0.4055 0.2801 0.2891 -0.0553 -0.0753 0.0400  290  LYS B CB  
10746 C CG  . LYS B 292  ? 0.4544 0.3170 0.3292 -0.0596 -0.0801 0.0441  290  LYS B CG  
10747 C CD  . LYS B 292  ? 0.5433 0.3970 0.4136 -0.0562 -0.0841 0.0443  290  LYS B CD  
10748 C CE  . LYS B 292  ? 0.5689 0.4096 0.4301 -0.0605 -0.0890 0.0485  290  LYS B CE  
10749 N NZ  . LYS B 292  ? 0.5639 0.3922 0.4232 -0.0584 -0.0928 0.0470  290  LYS B NZ  
10750 N N   . ALA B 293  ? 0.3483 0.2370 0.2314 -0.0530 -0.0719 0.0408  291  ALA B N   
10751 C CA  . ALA B 293  ? 0.3949 0.2833 0.2734 -0.0529 -0.0731 0.0425  291  ALA B CA  
10752 C C   . ALA B 293  ? 0.3907 0.2891 0.2678 -0.0570 -0.0694 0.0450  291  ALA B C   
10753 O O   . ALA B 293  ? 0.3839 0.2805 0.2543 -0.0603 -0.0707 0.0486  291  ALA B O   
10754 C CB  . ALA B 293  ? 0.3664 0.2563 0.2491 -0.0464 -0.0733 0.0386  291  ALA B CB  
10755 N N   . LEU B 294  ? 0.3654 0.2746 0.2486 -0.0567 -0.0647 0.0430  292  LEU B N   
10756 C CA  . LEU B 294  ? 0.3403 0.2597 0.2225 -0.0601 -0.0609 0.0451  292  LEU B CA  
10757 C C   . LEU B 294  ? 0.3488 0.2671 0.2265 -0.0671 -0.0613 0.0500  292  LEU B C   
10758 O O   . LEU B 294  ? 0.3779 0.2996 0.2507 -0.0709 -0.0604 0.0535  292  LEU B O   
10759 C CB  . LEU B 294  ? 0.3236 0.2542 0.2136 -0.0578 -0.0560 0.0418  292  LEU B CB  
10760 C CG  . LEU B 294  ? 0.3408 0.2740 0.2354 -0.0515 -0.0550 0.0372  292  LEU B CG  
10761 C CD1 . LEU B 294  ? 0.3230 0.2656 0.2254 -0.0494 -0.0507 0.0340  292  LEU B CD1 
10762 C CD2 . LEU B 294  ? 0.3367 0.2724 0.2274 -0.0507 -0.0548 0.0377  292  LEU B CD2 
10763 N N   . ALA B 295  ? 0.3493 0.2631 0.2285 -0.0689 -0.0626 0.0502  293  ALA B N   
10764 C CA  . ALA B 295  ? 0.3705 0.2825 0.2453 -0.0759 -0.0635 0.0549  293  ALA B CA  
10765 C C   . ALA B 295  ? 0.3831 0.2851 0.2490 -0.0789 -0.0679 0.0589  293  ALA B C   
10766 O O   . ALA B 295  ? 0.4037 0.3076 0.2648 -0.0849 -0.0677 0.0636  293  ALA B O   
10767 C CB  . ALA B 295  ? 0.3440 0.2512 0.2214 -0.0768 -0.0649 0.0539  293  ALA B CB  
10768 N N   . LEU B 296  ? 0.4143 0.3059 0.2779 -0.0748 -0.0718 0.0572  294  LEU B N   
10769 C CA  . LEU B 296  ? 0.4274 0.3090 0.2825 -0.0771 -0.0762 0.0609  294  LEU B CA  
10770 C C   . LEU B 296  ? 0.4539 0.3421 0.3052 -0.0788 -0.0744 0.0634  294  LEU B C   
10771 O O   . LEU B 296  ? 0.4597 0.3448 0.3039 -0.0841 -0.0760 0.0683  294  LEU B O   
10772 C CB  . LEU B 296  ? 0.4581 0.3286 0.3124 -0.0715 -0.0804 0.0582  294  LEU B CB  
10773 C CG  . LEU B 296  ? 0.5023 0.3613 0.3478 -0.0729 -0.0855 0.0617  294  LEU B CG  
10774 C CD1 . LEU B 296  ? 0.5653 0.4172 0.4047 -0.0799 -0.0880 0.0665  294  LEU B CD1 
10775 C CD2 . LEU B 296  ? 0.5681 0.4171 0.4143 -0.0665 -0.0895 0.0585  294  LEU B CD2 
10776 N N   . LEU B 297  ? 0.3979 0.2950 0.2536 -0.0743 -0.0711 0.0601  295  LEU B N   
10777 C CA  . LEU B 297  ? 0.3991 0.3034 0.2512 -0.0756 -0.0688 0.0620  295  LEU B CA  
10778 C C   . LEU B 297  ? 0.4174 0.3310 0.2687 -0.0817 -0.0651 0.0656  295  LEU B C   
10779 O O   . LEU B 297  ? 0.3902 0.3047 0.2350 -0.0860 -0.0652 0.0700  295  LEU B O   
10780 C CB  . LEU B 297  ? 0.3672 0.2792 0.2246 -0.0696 -0.0658 0.0573  295  LEU B CB  
10781 C CG  . LEU B 297  ? 0.4636 0.3682 0.3208 -0.0639 -0.0694 0.0544  295  LEU B CG  
10782 C CD1 . LEU B 297  ? 0.4284 0.3413 0.2919 -0.0586 -0.0662 0.0496  295  LEU B CD1 
10783 C CD2 . LEU B 297  ? 0.4808 0.3792 0.3293 -0.0655 -0.0728 0.0578  295  LEU B CD2 
10784 N N   . ALA B 298  ? 0.3905 0.3116 0.2485 -0.0821 -0.0618 0.0640  296  ALA B N   
10785 C CA  . ALA B 298  ? 0.3744 0.3051 0.2324 -0.0877 -0.0583 0.0675  296  ALA B CA  
10786 C C   . ALA B 298  ? 0.4145 0.3379 0.2660 -0.0948 -0.0617 0.0731  296  ALA B C   
10787 O O   . ALA B 298  ? 0.4293 0.3580 0.2766 -0.1001 -0.0602 0.0776  296  ALA B O   
10788 C CB  . ALA B 298  ? 0.3729 0.3119 0.2394 -0.0867 -0.0548 0.0647  296  ALA B CB  
10789 N N   . LYS B 299  ? 0.4006 0.3114 0.2507 -0.0950 -0.0663 0.0729  297  LYS B N   
10790 C CA  . LYS B 299  ? 0.4300 0.3318 0.2730 -0.1016 -0.0702 0.0782  297  LYS B CA  
10791 C C   . LYS B 299  ? 0.4644 0.3623 0.2989 -0.1037 -0.0722 0.0820  297  LYS B C   
10792 O O   . LYS B 299  ? 0.4867 0.3856 0.3159 -0.1104 -0.0724 0.0874  297  LYS B O   
10793 C CB  . LYS B 299  ? 0.4792 0.3666 0.3214 -0.1003 -0.0752 0.0768  297  LYS B CB  
10794 C CG  . LYS B 299  ? 0.5526 0.4279 0.3860 -0.1065 -0.0802 0.0821  297  LYS B CG  
10795 C CD  . LYS B 299  ? 0.6007 0.4598 0.4316 -0.1034 -0.0857 0.0802  297  LYS B CD  
10796 C CE  . LYS B 299  ? 0.6439 0.4905 0.4663 -0.1100 -0.0907 0.0854  297  LYS B CE  
10797 N NZ  . LYS B 299  ? 0.7022 0.5455 0.5165 -0.1129 -0.0926 0.0899  297  LYS B NZ  
10798 N N   . ASN B 300  ? 0.4370 0.3306 0.2700 -0.0980 -0.0737 0.0794  298  ASN B N   
10799 C CA  . ASN B 300  ? 0.4863 0.3749 0.3109 -0.0997 -0.0761 0.0829  298  ASN B CA  
10800 C C   . ASN B 300  ? 0.4505 0.3515 0.2729 -0.1031 -0.0717 0.0859  298  ASN B C   
10801 O O   . ASN B 300  ? 0.4884 0.3866 0.3029 -0.1073 -0.0733 0.0906  298  ASN B O   
10802 C CB  . ASN B 300  ? 0.5569 0.4396 0.3811 -0.0926 -0.0785 0.0793  298  ASN B CB  
10803 C CG  . ASN B 300  ? 0.5851 0.4540 0.4094 -0.0895 -0.0836 0.0773  298  ASN B CG  
10804 O OD1 . ASN B 300  ? 0.6373 0.4975 0.4586 -0.0935 -0.0867 0.0799  298  ASN B OD1 
10805 N ND2 . ASN B 300  ? 0.6600 0.5269 0.4878 -0.0824 -0.0846 0.0728  298  ASN B ND2 
10806 N N   . TYR B 301  ? 0.4391 0.3538 0.2682 -0.1011 -0.0662 0.0832  299  TYR B N   
10807 C CA  . TYR B 301  ? 0.4410 0.3685 0.2686 -0.1040 -0.0616 0.0857  299  TYR B CA  
10808 C C   . TYR B 301  ? 0.4155 0.3508 0.2450 -0.1106 -0.0590 0.0894  299  TYR B C   
10809 O O   . TYR B 301  ? 0.4290 0.3751 0.2568 -0.1138 -0.0552 0.0923  299  TYR B O   
10810 C CB  . TYR B 301  ? 0.4224 0.3606 0.2556 -0.0979 -0.0570 0.0807  299  TYR B CB  
10811 C CG  . TYR B 301  ? 0.4182 0.3516 0.2486 -0.0924 -0.0589 0.0779  299  TYR B CG  
10812 C CD1 . TYR B 301  ? 0.4625 0.3959 0.2850 -0.0938 -0.0593 0.0808  299  TYR B CD1 
10813 C CD2 . TYR B 301  ? 0.4076 0.3371 0.2434 -0.0858 -0.0601 0.0724  299  TYR B CD2 
10814 C CE1 . TYR B 301  ? 0.4545 0.3836 0.2743 -0.0888 -0.0612 0.0782  299  TYR B CE1 
10815 C CE2 . TYR B 301  ? 0.4134 0.3390 0.2469 -0.0810 -0.0620 0.0699  299  TYR B CE2 
10816 C CZ  . TYR B 301  ? 0.4757 0.4011 0.3013 -0.0825 -0.0626 0.0728  299  TYR B CZ  
10817 O OH  . TYR B 301  ? 0.4275 0.3492 0.2510 -0.0778 -0.0647 0.0704  299  TYR B OH  
10818 N N   . ASP B 302  ? 0.4036 0.3337 0.2363 -0.1125 -0.0610 0.0893  300  ASP B N   
10819 C CA  . ASP B 302  ? 0.4385 0.3760 0.2741 -0.1184 -0.0589 0.0922  300  ASP B CA  
10820 C C   . ASP B 302  ? 0.4177 0.3725 0.2603 -0.1166 -0.0524 0.0902  300  ASP B C   
10821 O O   . ASP B 302  ? 0.4150 0.3806 0.2570 -0.1212 -0.0490 0.0940  300  ASP B O   
10822 C CB  . ASP B 302  ? 0.4768 0.4122 0.3048 -0.1268 -0.0607 0.0993  300  ASP B CB  
10823 C CG  . ASP B 302  ? 0.4961 0.4337 0.3267 -0.1334 -0.0608 0.1024  300  ASP B CG  
10824 O OD1 . ASP B 302  ? 0.4937 0.4280 0.3297 -0.1313 -0.0618 0.0991  300  ASP B OD1 
10825 O OD2 . ASP B 302  ? 0.5416 0.4847 0.3688 -0.1405 -0.0598 0.1080  300  ASP B OD2 
10826 N N   . ILE B 303  ? 0.4098 0.3670 0.2589 -0.1096 -0.0506 0.0843  301  ILE B N   
10827 C CA  . ILE B 303  ? 0.3797 0.3515 0.2362 -0.1071 -0.0449 0.0816  301  ILE B CA  
10828 C C   . ILE B 303  ? 0.3792 0.3500 0.2432 -0.1055 -0.0452 0.0785  301  ILE B C   
10829 O O   . ILE B 303  ? 0.3649 0.3237 0.2285 -0.1045 -0.0495 0.0770  301  ILE B O   
10830 C CB  . ILE B 303  ? 0.3610 0.3375 0.2187 -0.1002 -0.0422 0.0773  301  ILE B CB  
10831 C CG1 . ILE B 303  ? 0.4048 0.3723 0.2656 -0.0937 -0.0449 0.0719  301  ILE B CG1 
10832 C CG2 . ILE B 303  ? 0.3887 0.3640 0.2380 -0.1015 -0.0428 0.0802  301  ILE B CG2 
10833 C CD1 . ILE B 303  ? 0.3579 0.3306 0.2212 -0.0870 -0.0422 0.0672  301  ILE B CD1 
10834 N N   . GLY B 304  ? 0.3559 0.3396 0.2266 -0.1050 -0.0406 0.0773  302  GLY B N   
10835 C CA  . GLY B 304  ? 0.3469 0.3310 0.2249 -0.1031 -0.0404 0.0740  302  GLY B CA  
10836 C C   . GLY B 304  ? 0.3540 0.3360 0.2363 -0.0950 -0.0398 0.0678  302  GLY B C   
10837 O O   . GLY B 304  ? 0.3539 0.3403 0.2360 -0.0907 -0.0375 0.0656  302  GLY B O   
10838 N N   . LEU B 305  ? 0.3167 0.2916 0.2026 -0.0930 -0.0421 0.0650  303  LEU B N   
10839 C CA  . LEU B 305  ? 0.3165 0.2903 0.2076 -0.0857 -0.0414 0.0591  303  LEU B CA  
10840 C C   . LEU B 305  ? 0.3333 0.3110 0.2314 -0.0855 -0.0401 0.0573  303  LEU B C   
10841 O O   . LEU B 305  ? 0.3455 0.3160 0.2430 -0.0884 -0.0431 0.0583  303  LEU B O   
10842 C CB  . LEU B 305  ? 0.3326 0.2925 0.2205 -0.0826 -0.0461 0.0573  303  LEU B CB  
10843 C CG  . LEU B 305  ? 0.3618 0.3200 0.2551 -0.0754 -0.0458 0.0515  303  LEU B CG  
10844 C CD1 . LEU B 305  ? 0.3770 0.3263 0.2664 -0.0718 -0.0490 0.0501  303  LEU B CD1 
10845 C CD2 . LEU B 305  ? 0.3823 0.3360 0.2799 -0.0747 -0.0472 0.0494  303  LEU B CD2 
10846 N N   . ASN B 306  ? 0.3053 0.2941 0.2094 -0.0823 -0.0356 0.0547  304  ASN B N   
10847 C CA  . ASN B 306  ? 0.3180 0.3125 0.2288 -0.0823 -0.0338 0.0533  304  ASN B CA  
10848 C C   . ASN B 306  ? 0.3185 0.3106 0.2346 -0.0757 -0.0335 0.0478  304  ASN B C   
10849 O O   . ASN B 306  ? 0.2983 0.2928 0.2156 -0.0708 -0.0317 0.0448  304  ASN B O   
10850 C CB  . ASN B 306  ? 0.3229 0.3325 0.2373 -0.0834 -0.0288 0.0546  304  ASN B CB  
10851 C CG  . ASN B 306  ? 0.3392 0.3550 0.2610 -0.0821 -0.0268 0.0524  304  ASN B CG  
10852 O OD1 . ASN B 306  ? 0.3334 0.3536 0.2601 -0.0766 -0.0242 0.0484  304  ASN B OD1 
10853 N ND2 . ASN B 306  ? 0.2803 0.2954 0.2027 -0.0871 -0.0283 0.0551  304  ASN B ND2 
10854 N N   . ILE B 307  ? 0.2976 0.2852 0.2166 -0.0758 -0.0352 0.0465  305  ILE B N   
10855 C CA  . ILE B 307  ? 0.3198 0.3061 0.2442 -0.0701 -0.0345 0.0416  305  ILE B CA  
10856 C C   . ILE B 307  ? 0.3167 0.3150 0.2478 -0.0693 -0.0303 0.0405  305  ILE B C   
10857 O O   . ILE B 307  ? 0.2743 0.2753 0.2072 -0.0729 -0.0303 0.0422  305  ILE B O   
10858 C CB  . ILE B 307  ? 0.3310 0.3061 0.2549 -0.0702 -0.0385 0.0406  305  ILE B CB  
10859 C CG1 . ILE B 307  ? 0.3539 0.3168 0.2714 -0.0700 -0.0427 0.0413  305  ILE B CG1 
10860 C CG2 . ILE B 307  ? 0.3359 0.3116 0.2659 -0.0648 -0.0373 0.0359  305  ILE B CG2 
10861 C CD1 . ILE B 307  ? 0.3642 0.3152 0.2797 -0.0707 -0.0469 0.0409  305  ILE B CD1 
10862 N N   . ASP B 308  ? 0.2843 0.2894 0.2187 -0.0646 -0.0270 0.0377  306  ASP B N   
10863 C CA  . ASP B 308  ? 0.2763 0.2921 0.2169 -0.0630 -0.0231 0.0363  306  ASP B CA  
10864 C C   . ASP B 308  ? 0.2546 0.2672 0.1998 -0.0612 -0.0240 0.0337  306  ASP B C   
10865 O O   . ASP B 308  ? 0.2639 0.2671 0.2086 -0.0590 -0.0267 0.0315  306  ASP B O   
10866 C CB  . ASP B 308  ? 0.2940 0.3156 0.2365 -0.0578 -0.0199 0.0334  306  ASP B CB  
10867 C CG  . ASP B 308  ? 0.3291 0.3566 0.2675 -0.0593 -0.0180 0.0358  306  ASP B CG  
10868 O OD1 . ASP B 308  ? 0.2808 0.3101 0.2158 -0.0646 -0.0185 0.0401  306  ASP B OD1 
10869 O OD2 . ASP B 308  ? 0.3246 0.3552 0.2633 -0.0551 -0.0160 0.0334  306  ASP B OD2 
10870 N N   . ALA B 309  ? 0.2488 0.2699 0.1987 -0.0621 -0.0216 0.0340  307  ALA B N   
10871 C CA  . ALA B 309  ? 0.2382 0.2574 0.1925 -0.0605 -0.0221 0.0316  307  ALA B CA  
10872 C C   . ALA B 309  ? 0.2485 0.2728 0.2081 -0.0547 -0.0190 0.0277  307  ALA B C   
10873 O O   . ALA B 309  ? 0.2388 0.2720 0.2002 -0.0531 -0.0157 0.0276  307  ALA B O   
10874 C CB  . ALA B 309  ? 0.2516 0.2761 0.2077 -0.0653 -0.0218 0.0344  307  ALA B CB  
10875 N N   . GLU B 310  ? 0.2379 0.2561 0.1997 -0.0514 -0.0203 0.0245  308  GLU B N   
10876 C CA  . GLU B 310  ? 0.2414 0.2627 0.2078 -0.0459 -0.0179 0.0207  308  GLU B CA  
10877 C C   . GLU B 310  ? 0.2279 0.2513 0.1992 -0.0450 -0.0172 0.0193  308  GLU B C   
10878 O O   . GLU B 310  ? 0.2277 0.2564 0.2003 -0.0482 -0.0165 0.0214  308  GLU B O   
10879 C CB  . GLU B 310  ? 0.2484 0.2614 0.2131 -0.0423 -0.0198 0.0181  308  GLU B CB  
10880 C CG  . GLU B 310  ? 0.2801 0.2910 0.2394 -0.0436 -0.0208 0.0199  308  GLU B CG  
10881 C CD  . GLU B 310  ? 0.2489 0.2531 0.2070 -0.0398 -0.0225 0.0173  308  GLU B CD  
10882 O OE1 . GLU B 310  ? 0.2903 0.2976 0.2514 -0.0358 -0.0206 0.0146  308  GLU B OE1 
10883 O OE2 . GLU B 310  ? 0.2620 0.2579 0.2160 -0.0409 -0.0258 0.0183  308  GLU B OE2 
10884 N N   . GLU B 311  ? 0.2157 0.2351 0.1896 -0.0408 -0.0174 0.0158  309  GLU B N   
10885 C CA  . GLU B 311  ? 0.2356 0.2573 0.2140 -0.0396 -0.0164 0.0143  309  GLU B CA  
10886 C C   . GLU B 311  ? 0.2185 0.2352 0.1953 -0.0432 -0.0191 0.0158  309  GLU B C   
10887 O O   . GLU B 311  ? 0.2210 0.2299 0.1934 -0.0455 -0.0221 0.0169  309  GLU B O   
10888 C CB  . GLU B 311  ? 0.2333 0.2520 0.2147 -0.0345 -0.0161 0.0105  309  GLU B CB  
10889 C CG  . GLU B 311  ? 0.2528 0.2763 0.2361 -0.0309 -0.0135 0.0088  309  GLU B CG  
10890 C CD  . GLU B 311  ? 0.3068 0.3258 0.2864 -0.0300 -0.0148 0.0085  309  GLU B CD  
10891 O OE1 . GLU B 311  ? 0.2588 0.2716 0.2342 -0.0324 -0.0176 0.0101  309  GLU B OE1 
10892 O OE2 . GLU B 311  ? 0.3226 0.3440 0.3034 -0.0269 -0.0133 0.0067  309  GLU B OE2 
10893 N N   . ALA B 312  ? 0.1901 0.2112 0.1705 -0.0436 -0.0180 0.0156  310  ALA B N   
10894 C CA  . ALA B 312  ? 0.2171 0.2342 0.1959 -0.0473 -0.0205 0.0170  310  ALA B CA  
10895 C C   . ALA B 312  ? 0.2398 0.2455 0.2159 -0.0460 -0.0235 0.0151  310  ALA B C   
10896 O O   . ALA B 312  ? 0.2314 0.2303 0.2034 -0.0495 -0.0265 0.0166  310  ALA B O   
10897 C CB  . ALA B 312  ? 0.2193 0.2431 0.2026 -0.0473 -0.0188 0.0167  310  ALA B CB  
10898 N N   . ASP B 313  ? 0.2236 0.2267 0.2017 -0.0410 -0.0228 0.0118  311  ASP B N   
10899 C CA  . ASP B 313  ? 0.2367 0.2299 0.2127 -0.0392 -0.0254 0.0099  311  ASP B CA  
10900 C C   . ASP B 313  ? 0.2176 0.2031 0.1888 -0.0397 -0.0280 0.0106  311  ASP B C   
10901 O O   . ASP B 313  ? 0.2529 0.2300 0.2221 -0.0378 -0.0303 0.0090  311  ASP B O   
10902 C CB  . ASP B 313  ? 0.2566 0.2504 0.2369 -0.0340 -0.0238 0.0063  311  ASP B CB  
10903 C CG  . ASP B 313  ? 0.2810 0.2779 0.2633 -0.0306 -0.0220 0.0050  311  ASP B CG  
10904 O OD1 . ASP B 313  ? 0.2795 0.2776 0.2596 -0.0319 -0.0220 0.0065  311  ASP B OD1 
10905 O OD2 . ASP B 313  ? 0.2845 0.2826 0.2705 -0.0267 -0.0206 0.0024  311  ASP B OD2 
10906 N N   . ARG B 314  ? 0.2366 0.2250 0.2056 -0.0421 -0.0278 0.0130  312  ARG B N   
10907 C CA  . ARG B 314  ? 0.2517 0.2328 0.2155 -0.0432 -0.0305 0.0143  312  ARG B CA  
10908 C C   . ARG B 314  ? 0.2343 0.2129 0.1933 -0.0491 -0.0327 0.0180  312  ARG B C   
10909 O O   . ARG B 314  ? 0.2562 0.2277 0.2102 -0.0506 -0.0354 0.0195  312  ARG B O   
10910 C CB  . ARG B 314  ? 0.2513 0.2366 0.2155 -0.0412 -0.0288 0.0141  312  ARG B CB  
10911 C CG  . ARG B 314  ? 0.2543 0.2386 0.2217 -0.0357 -0.0281 0.0105  312  ARG B CG  
10912 C CD  . ARG B 314  ? 0.2581 0.2486 0.2270 -0.0338 -0.0257 0.0100  312  ARG B CD  
10913 N NE  . ARG B 314  ? 0.2575 0.2451 0.2281 -0.0292 -0.0261 0.0071  312  ARG B NE  
10914 C CZ  . ARG B 314  ? 0.2976 0.2892 0.2697 -0.0268 -0.0245 0.0059  312  ARG B CZ  
10915 N NH1 . ARG B 314  ? 0.2479 0.2467 0.2200 -0.0279 -0.0220 0.0070  312  ARG B NH1 
10916 N NH2 . ARG B 314  ? 0.2768 0.2652 0.2503 -0.0232 -0.0254 0.0035  312  ARG B NH2 
10917 N N   . LEU B 315  ? 0.2236 0.2077 0.1840 -0.0526 -0.0318 0.0198  313  LEU B N   
10918 C CA  . LEU B 315  ? 0.2491 0.2321 0.2054 -0.0588 -0.0337 0.0238  313  LEU B CA  
10919 C C   . LEU B 315  ? 0.2954 0.2655 0.2461 -0.0605 -0.0382 0.0241  313  LEU B C   
10920 O O   . LEU B 315  ? 0.2973 0.2615 0.2427 -0.0632 -0.0406 0.0264  313  LEU B O   
10921 C CB  . LEU B 315  ? 0.2450 0.2364 0.2046 -0.0619 -0.0321 0.0253  313  LEU B CB  
10922 C CG  . LEU B 315  ? 0.2681 0.2643 0.2257 -0.0684 -0.0325 0.0299  313  LEU B CG  
10923 C CD1 . LEU B 315  ? 0.2157 0.2214 0.1780 -0.0703 -0.0306 0.0307  313  LEU B CD1 
10924 C CD2 . LEU B 315  ? 0.2833 0.2687 0.2344 -0.0732 -0.0370 0.0322  313  LEU B CD2 
10925 N N   . GLU B 316  ? 0.2564 0.2215 0.2077 -0.0590 -0.0393 0.0218  314  GLU B N   
10926 C CA  . GLU B 316  ? 0.2899 0.2426 0.2354 -0.0608 -0.0437 0.0222  314  GLU B CA  
10927 C C   . GLU B 316  ? 0.3057 0.2494 0.2479 -0.0574 -0.0457 0.0209  314  GLU B C   
10928 O O   . GLU B 316  ? 0.3433 0.2776 0.2795 -0.0600 -0.0493 0.0226  314  GLU B O   
10929 C CB  . GLU B 316  ? 0.2513 0.2012 0.1981 -0.0597 -0.0443 0.0199  314  GLU B CB  
10930 C CG  . GLU B 316  ? 0.2817 0.2385 0.2301 -0.0646 -0.0436 0.0221  314  GLU B CG  
10931 C CD  . GLU B 316  ? 0.3170 0.2713 0.2661 -0.0640 -0.0443 0.0201  314  GLU B CD  
10932 O OE1 . GLU B 316  ? 0.3472 0.2900 0.2918 -0.0631 -0.0474 0.0186  314  GLU B OE1 
10933 O OE2 . GLU B 316  ? 0.3128 0.2763 0.2667 -0.0641 -0.0418 0.0199  314  GLU B OE2 
10934 N N   . LEU B 317  ? 0.2976 0.2442 0.2436 -0.0519 -0.0436 0.0180  315  LEU B N   
10935 C CA  . LEU B 317  ? 0.3080 0.2476 0.2515 -0.0486 -0.0454 0.0169  315  LEU B CA  
10936 C C   . LEU B 317  ? 0.3232 0.2617 0.2623 -0.0520 -0.0467 0.0203  315  LEU B C   
10937 O O   . LEU B 317  ? 0.3347 0.2634 0.2685 -0.0523 -0.0502 0.0211  315  LEU B O   
10938 C CB  . LEU B 317  ? 0.2980 0.2427 0.2469 -0.0428 -0.0427 0.0137  315  LEU B CB  
10939 C CG  . LEU B 317  ? 0.3417 0.2807 0.2889 -0.0391 -0.0444 0.0125  315  LEU B CG  
10940 C CD1 . LEU B 317  ? 0.3652 0.2922 0.3082 -0.0379 -0.0482 0.0116  315  LEU B CD1 
10941 C CD2 . LEU B 317  ? 0.3300 0.2749 0.2831 -0.0339 -0.0416 0.0094  315  LEU B CD2 
10942 N N   . SER B 318  ? 0.2786 0.2270 0.2195 -0.0546 -0.0440 0.0225  316  SER B N   
10943 C CA  . SER B 318  ? 0.2973 0.2454 0.2338 -0.0580 -0.0449 0.0259  316  SER B CA  
10944 C C   . SER B 318  ? 0.3206 0.2608 0.2508 -0.0637 -0.0486 0.0293  316  SER B C   
10945 O O   . SER B 318  ? 0.3060 0.2409 0.2310 -0.0658 -0.0509 0.0318  316  SER B O   
10946 C CB  . SER B 318  ? 0.2990 0.2599 0.2387 -0.0595 -0.0410 0.0275  316  SER B CB  
10947 O OG  . SER B 318  ? 0.2867 0.2537 0.2278 -0.0639 -0.0399 0.0296  316  SER B OG  
10948 N N   . LEU B 319  ? 0.3255 0.2644 0.2560 -0.0664 -0.0495 0.0296  317  LEU B N   
10949 C CA  . LEU B 319  ? 0.3327 0.2631 0.2569 -0.0721 -0.0534 0.0328  317  LEU B CA  
10950 C C   . LEU B 319  ? 0.3638 0.2795 0.2823 -0.0701 -0.0578 0.0318  317  LEU B C   
10951 O O   . LEU B 319  ? 0.3759 0.2836 0.2880 -0.0743 -0.0612 0.0348  317  LEU B O   
10952 C CB  . LEU B 319  ? 0.3176 0.2494 0.2433 -0.0751 -0.0536 0.0329  317  LEU B CB  
10953 C CG  . LEU B 319  ? 0.3350 0.2813 0.2664 -0.0774 -0.0497 0.0342  317  LEU B CG  
10954 C CD1 . LEU B 319  ? 0.3276 0.2742 0.2603 -0.0798 -0.0504 0.0340  317  LEU B CD1 
10955 C CD2 . LEU B 319  ? 0.3406 0.2924 0.2698 -0.0830 -0.0493 0.0390  317  LEU B CD2 
10956 N N   . ASP B 320  ? 0.3375 0.2495 0.2582 -0.0638 -0.0577 0.0276  318  ASP B N   
10957 C CA  . ASP B 320  ? 0.3651 0.2639 0.2807 -0.0611 -0.0616 0.0265  318  ASP B CA  
10958 C C   . ASP B 320  ? 0.4033 0.3000 0.3157 -0.0609 -0.0627 0.0283  318  ASP B C   
10959 O O   . ASP B 320  ? 0.3937 0.2791 0.2997 -0.0620 -0.0668 0.0298  318  ASP B O   
10960 C CB  . ASP B 320  ? 0.3561 0.2531 0.2755 -0.0542 -0.0609 0.0217  318  ASP B CB  
10961 C CG  . ASP B 320  ? 0.3597 0.2545 0.2797 -0.0545 -0.0611 0.0199  318  ASP B CG  
10962 O OD1 . ASP B 320  ? 0.4439 0.3291 0.3581 -0.0578 -0.0647 0.0212  318  ASP B OD1 
10963 O OD2 . ASP B 320  ? 0.3687 0.2712 0.2947 -0.0516 -0.0579 0.0174  318  ASP B OD2 
10964 N N   . LEU B 321  ? 0.3327 0.2397 0.2491 -0.0596 -0.0593 0.0284  319  LEU B N   
10965 C CA  . LEU B 321  ? 0.3298 0.2355 0.2427 -0.0601 -0.0603 0.0305  319  LEU B CA  
10966 C C   . LEU B 321  ? 0.3369 0.2415 0.2443 -0.0673 -0.0618 0.0355  319  LEU B C   
10967 O O   . LEU B 321  ? 0.3825 0.2781 0.2834 -0.0689 -0.0653 0.0378  319  LEU B O   
10968 C CB  . LEU B 321  ? 0.3057 0.2226 0.2238 -0.0569 -0.0562 0.0291  319  LEU B CB  
10969 C CG  . LEU B 321  ? 0.3532 0.2693 0.2754 -0.0498 -0.0557 0.0247  319  LEU B CG  
10970 C CD1 . LEU B 321  ? 0.3499 0.2729 0.2789 -0.0473 -0.0525 0.0216  319  LEU B CD1 
10971 C CD2 . LEU B 321  ? 0.3794 0.3000 0.3024 -0.0474 -0.0545 0.0245  319  LEU B CD2 
10972 N N   . LEU B 322  ? 0.3327 0.2463 0.2424 -0.0717 -0.0593 0.0375  320  LEU B N   
10973 C CA  . LEU B 322  ? 0.3375 0.2514 0.2426 -0.0791 -0.0605 0.0425  320  LEU B CA  
10974 C C   . LEU B 322  ? 0.3734 0.2728 0.2715 -0.0823 -0.0658 0.0443  320  LEU B C   
10975 O O   . LEU B 322  ? 0.4012 0.2948 0.2930 -0.0863 -0.0686 0.0479  320  LEU B O   
10976 C CB  . LEU B 322  ? 0.3137 0.2391 0.2233 -0.0829 -0.0574 0.0439  320  LEU B CB  
10977 C CG  . LEU B 322  ? 0.3373 0.2654 0.2430 -0.0908 -0.0581 0.0494  320  LEU B CG  
10978 C CD1 . LEU B 322  ? 0.3435 0.2767 0.2475 -0.0910 -0.0564 0.0516  320  LEU B CD1 
10979 C CD2 . LEU B 322  ? 0.3302 0.2693 0.2406 -0.0945 -0.0554 0.0507  320  LEU B CD2 
10980 N N   . GLU B 323  ? 0.3699 0.2630 0.2686 -0.0806 -0.0674 0.0416  321  GLU B N   
10981 C CA  . GLU B 323  ? 0.4148 0.2931 0.3064 -0.0831 -0.0726 0.0426  321  GLU B CA  
10982 C C   . GLU B 323  ? 0.4106 0.2776 0.2965 -0.0806 -0.0761 0.0429  321  GLU B C   
10983 O O   . GLU B 323  ? 0.4173 0.2751 0.2959 -0.0851 -0.0800 0.0464  321  GLU B O   
10984 C CB  . GLU B 323  ? 0.4031 0.2769 0.2967 -0.0798 -0.0733 0.0387  321  GLU B CB  
10985 C CG  . GLU B 323  ? 0.4855 0.3427 0.3716 -0.0807 -0.0787 0.0387  321  GLU B CG  
10986 C CD  . GLU B 323  ? 0.4686 0.3231 0.3517 -0.0877 -0.0807 0.0412  321  GLU B CD  
10987 O OE1 . GLU B 323  ? 0.4762 0.3422 0.3642 -0.0907 -0.0777 0.0420  321  GLU B OE1 
10988 O OE2 . GLU B 323  ? 0.5156 0.3561 0.3913 -0.0901 -0.0856 0.0423  321  GLU B OE2 
10989 N N   . VAL B 324  ? 0.3718 0.2392 0.2607 -0.0734 -0.0750 0.0392  322  VAL B N   
10990 C CA  . VAL B 324  ? 0.3999 0.2569 0.2838 -0.0705 -0.0785 0.0393  322  VAL B CA  
10991 C C   . VAL B 324  ? 0.4633 0.3222 0.3433 -0.0746 -0.0789 0.0437  322  VAL B C   
10992 O O   . VAL B 324  ? 0.4731 0.3210 0.3459 -0.0763 -0.0830 0.0462  322  VAL B O   
10993 C CB  . VAL B 324  ? 0.4327 0.2917 0.3216 -0.0622 -0.0769 0.0347  322  VAL B CB  
10994 C CG1 . VAL B 324  ? 0.4808 0.3312 0.3651 -0.0594 -0.0802 0.0352  322  VAL B CG1 
10995 C CG2 . VAL B 324  ? 0.4098 0.2649 0.3013 -0.0580 -0.0772 0.0305  322  VAL B CG2 
10996 N N   . LEU B 325  ? 0.4013 0.2739 0.2856 -0.0759 -0.0745 0.0447  323  LEU B N   
10997 C CA  . LEU B 325  ? 0.4164 0.2919 0.2970 -0.0794 -0.0744 0.0487  323  LEU B CA  
10998 C C   . LEU B 325  ? 0.4309 0.3019 0.3052 -0.0876 -0.0769 0.0539  323  LEU B C   
10999 O O   . LEU B 325  ? 0.4481 0.3132 0.3159 -0.0905 -0.0796 0.0574  323  LEU B O   
11000 C CB  . LEU B 325  ? 0.3884 0.2798 0.2750 -0.0787 -0.0690 0.0482  323  LEU B CB  
11001 C CG  . LEU B 325  ? 0.3812 0.2769 0.2733 -0.0711 -0.0667 0.0436  323  LEU B CG  
11002 C CD1 . LEU B 325  ? 0.3862 0.2970 0.2848 -0.0704 -0.0612 0.0425  323  LEU B CD1 
11003 C CD2 . LEU B 325  ? 0.3829 0.2731 0.2710 -0.0684 -0.0689 0.0440  323  LEU B CD2 
11004 N N   . CYS B 326  ? 0.3959 0.2696 0.2720 -0.0917 -0.0764 0.0546  324  CYS B N   
11005 C CA  . CYS B 326  ? 0.4099 0.2800 0.2803 -0.1001 -0.0788 0.0598  324  CYS B CA  
11006 C C   . CYS B 326  ? 0.4416 0.2937 0.3039 -0.1014 -0.0850 0.0609  324  CYS B C   
11007 O O   . CYS B 326  ? 0.4518 0.2984 0.3076 -0.1080 -0.0879 0.0657  324  CYS B O   
11008 C CB  . CYS B 326  ? 0.4586 0.3370 0.3333 -0.1042 -0.0767 0.0604  324  CYS B CB  
11009 S SG  . CYS B 326  ? 0.4395 0.3392 0.3221 -0.1046 -0.0699 0.0610  324  CYS B SG  
11010 N N   . LEU B 327  ? 0.4360 0.2787 0.2983 -0.0954 -0.0871 0.0566  325  LEU B N   
11011 C CA  . LEU B 327  ? 0.4411 0.2659 0.2955 -0.0954 -0.0929 0.0570  325  LEU B CA  
11012 C C   . LEU B 327  ? 0.5100 0.3275 0.3606 -0.0911 -0.0952 0.0568  325  LEU B C   
11013 O O   . LEU B 327  ? 0.4888 0.2911 0.3326 -0.0903 -0.1002 0.0571  325  LEU B O   
11014 C CB  . LEU B 327  ? 0.4646 0.2829 0.3206 -0.0911 -0.0941 0.0523  325  LEU B CB  
11015 C CG  . LEU B 327  ? 0.5274 0.3513 0.3864 -0.0956 -0.0926 0.0525  325  LEU B CG  
11016 C CD1 . LEU B 327  ? 0.5644 0.3820 0.4247 -0.0909 -0.0936 0.0477  325  LEU B CD1 
11017 C CD2 . LEU B 327  ? 0.5691 0.3871 0.4214 -0.1047 -0.0961 0.0578  325  LEU B CD2 
11018 N N   . ASP B 328  ? 0.4763 0.3039 0.3307 -0.0882 -0.0918 0.0564  326  ASP B N   
11019 C CA  . ASP B 328  ? 0.5012 0.3230 0.3526 -0.0838 -0.0938 0.0560  326  ASP B CA  
11020 C C   . ASP B 328  ? 0.4759 0.2916 0.3190 -0.0898 -0.0970 0.0617  326  ASP B C   
11021 O O   . ASP B 328  ? 0.5242 0.3494 0.3674 -0.0947 -0.0944 0.0652  326  ASP B O   
11022 C CB  . ASP B 328  ? 0.5207 0.3555 0.3790 -0.0788 -0.0892 0.0534  326  ASP B CB  
11023 C CG  . ASP B 328  ? 0.5721 0.4013 0.4288 -0.0730 -0.0914 0.0519  326  ASP B CG  
11024 O OD1 . ASP B 328  ? 0.5387 0.3566 0.3878 -0.0745 -0.0958 0.0547  326  ASP B OD1 
11025 O OD2 . ASP B 328  ? 0.6047 0.4407 0.4676 -0.0669 -0.0887 0.0481  326  ASP B OD2 
11026 N N   . GLY B 329  ? 0.5392 0.3388 0.3748 -0.0893 -0.1025 0.0626  327  GLY B N   
11027 C CA  . GLY B 329  ? 0.5247 0.3168 0.3517 -0.0950 -0.1060 0.0682  327  GLY B CA  
11028 C C   . GLY B 329  ? 0.5818 0.3804 0.4082 -0.0941 -0.1045 0.0700  327  GLY B C   
11029 O O   . GLY B 329  ? 0.5595 0.3578 0.3804 -0.1003 -0.1054 0.0751  327  GLY B O   
11030 N N   . ASP B 330  ? 0.5551 0.3597 0.3870 -0.0867 -0.1021 0.0659  328  ASP B N   
11031 C CA  . ASP B 330  ? 0.5535 0.3655 0.3852 -0.0860 -0.1003 0.0673  328  ASP B CA  
11032 C C   . ASP B 330  ? 0.5390 0.3652 0.3727 -0.0918 -0.0957 0.0703  328  ASP B C   
11033 O O   . ASP B 330  ? 0.5506 0.3806 0.3810 -0.0939 -0.0950 0.0733  328  ASP B O   
11034 C CB  . ASP B 330  ? 0.5968 0.4142 0.4350 -0.0775 -0.0983 0.0621  328  ASP B CB  
11035 C CG  . ASP B 330  ? 0.6919 0.4963 0.5280 -0.0713 -0.1029 0.0596  328  ASP B CG  
11036 O OD1 . ASP B 330  ? 0.6676 0.4582 0.4957 -0.0735 -0.1079 0.0624  328  ASP B OD1 
11037 O OD2 . ASP B 330  ? 0.6020 0.4098 0.4442 -0.0643 -0.1015 0.0550  328  ASP B OD2 
11038 N N   . LEU B 331  ? 0.5131 0.3470 0.3519 -0.0944 -0.0926 0.0696  329  LEU B N   
11039 C CA  . LEU B 331  ? 0.5327 0.3809 0.3740 -0.0996 -0.0880 0.0722  329  LEU B CA  
11040 C C   . LEU B 331  ? 0.5186 0.3637 0.3546 -0.1087 -0.0899 0.0778  329  LEU B C   
11041 O O   . LEU B 331  ? 0.4756 0.3327 0.3141 -0.1135 -0.0862 0.0802  329  LEU B O   
11042 C CB  . LEU B 331  ? 0.4734 0.3338 0.3243 -0.0966 -0.0831 0.0681  329  LEU B CB  
11043 C CG  . LEU B 331  ? 0.4980 0.3618 0.3546 -0.0879 -0.0812 0.0626  329  LEU B CG  
11044 C CD1 . LEU B 331  ? 0.4862 0.3602 0.3518 -0.0850 -0.0769 0.0585  329  LEU B CD1 
11045 C CD2 . LEU B 331  ? 0.4927 0.3628 0.3483 -0.0864 -0.0794 0.0634  329  LEU B CD2 
11046 N N   . SER B 332  ? 0.5411 0.3704 0.3697 -0.1111 -0.0956 0.0799  330  SER B N   
11047 C CA  . SER B 332  ? 0.5701 0.3946 0.3933 -0.1199 -0.0981 0.0851  330  SER B CA  
11048 C C   . SER B 332  ? 0.5799 0.4138 0.4005 -0.1265 -0.0958 0.0907  330  SER B C   
11049 O O   . SER B 332  ? 0.6305 0.4643 0.4474 -0.1254 -0.0960 0.0923  330  SER B O   
11050 C CB  . SER B 332  ? 0.6125 0.4170 0.4268 -0.1208 -0.1050 0.0866  330  SER B CB  
11051 O OG  . SER B 332  ? 0.6406 0.4376 0.4528 -0.1255 -0.1078 0.0877  330  SER B OG  
11052 N N   . GLY B 333  ? 0.5701 0.4125 0.3927 -0.1333 -0.0937 0.0937  331  GLY B N   
11053 C CA  . GLY B 333  ? 0.6200 0.4723 0.4405 -0.1401 -0.0914 0.0993  331  GLY B CA  
11054 C C   . GLY B 333  ? 0.6325 0.5042 0.4604 -0.1380 -0.0845 0.0979  331  GLY B C   
11055 O O   . GLY B 333  ? 0.6482 0.5308 0.4761 -0.1439 -0.0817 0.1023  331  GLY B O   
11056 N N   . TRP B 334  ? 0.5515 0.4279 0.3858 -0.1298 -0.0818 0.0921  332  TRP B N   
11057 C CA  . TRP B 334  ? 0.5258 0.4193 0.3667 -0.1269 -0.0755 0.0902  332  TRP B CA  
11058 C C   . TRP B 334  ? 0.5386 0.4429 0.3873 -0.1282 -0.0721 0.0888  332  TRP B C   
11059 O O   . TRP B 334  ? 0.5411 0.4409 0.3935 -0.1251 -0.0732 0.0850  332  TRP B O   
11060 C CB  . TRP B 334  ? 0.4984 0.3910 0.3420 -0.1178 -0.0746 0.0847  332  TRP B CB  
11061 C CG  . TRP B 334  ? 0.4853 0.3936 0.3358 -0.1139 -0.0687 0.0819  332  TRP B CG  
11062 C CD1 . TRP B 334  ? 0.5002 0.4205 0.3503 -0.1159 -0.0647 0.0844  332  TRP B CD1 
11063 C CD2 . TRP B 334  ? 0.4904 0.4035 0.3488 -0.1070 -0.0661 0.0760  332  TRP B CD2 
11064 N NE1 . TRP B 334  ? 0.4498 0.3818 0.3070 -0.1105 -0.0599 0.0801  332  TRP B NE1 
11065 C CE2 . TRP B 334  ? 0.4124 0.3400 0.2747 -0.1052 -0.0607 0.0751  332  TRP B CE2 
11066 C CE3 . TRP B 334  ? 0.4256 0.3321 0.2878 -0.1021 -0.0677 0.0714  332  TRP B CE3 
11067 C CZ2 . TRP B 334  ? 0.3812 0.3163 0.2511 -0.0989 -0.0572 0.0698  332  TRP B CZ2 
11068 C CZ3 . TRP B 334  ? 0.4340 0.3486 0.3039 -0.0961 -0.0640 0.0664  332  TRP B CZ3 
11069 C CH2 . TRP B 334  ? 0.4066 0.3350 0.2803 -0.0946 -0.0590 0.0657  332  TRP B CH2 
11070 N N   . ASN B 335  ? 0.4430 0.3616 0.2940 -0.1326 -0.0680 0.0920  333  ASN B N   
11071 C CA  . ASN B 335  ? 0.4371 0.3675 0.2957 -0.1339 -0.0645 0.0911  333  ASN B CA  
11072 C C   . ASN B 335  ? 0.4360 0.3812 0.3019 -0.1281 -0.0585 0.0874  333  ASN B C   
11073 O O   . ASN B 335  ? 0.4312 0.3892 0.3033 -0.1294 -0.0548 0.0875  333  ASN B O   
11074 C CB  . ASN B 335  ? 0.4590 0.3955 0.3158 -0.1433 -0.0643 0.0974  333  ASN B CB  
11075 C CG  . ASN B 335  ? 0.5568 0.4784 0.4071 -0.1494 -0.0704 0.1008  333  ASN B CG  
11076 O OD1 . ASN B 335  ? 0.5409 0.4505 0.3908 -0.1469 -0.0740 0.0976  333  ASN B OD1 
11077 N ND2 . ASN B 335  ? 0.5420 0.4638 0.3867 -0.1575 -0.0717 0.1072  333  ASN B ND2 
11078 N N   . GLY B 336  ? 0.4361 0.3797 0.3014 -0.1217 -0.0577 0.0842  334  GLY B N   
11079 C CA  . GLY B 336  ? 0.3930 0.3498 0.2644 -0.1164 -0.0523 0.0808  334  GLY B CA  
11080 C C   . GLY B 336  ? 0.4036 0.3609 0.2822 -0.1098 -0.0512 0.0748  334  GLY B C   
11081 O O   . GLY B 336  ? 0.3707 0.3382 0.2545 -0.1051 -0.0469 0.0717  334  GLY B O   
11082 N N   . MET B 337  ? 0.4076 0.3538 0.2863 -0.1091 -0.0549 0.0729  335  MET B N   
11083 C CA  . MET B 337  ? 0.4011 0.3480 0.2865 -0.1031 -0.0538 0.0674  335  MET B CA  
11084 C C   . MET B 337  ? 0.4123 0.3726 0.3047 -0.1045 -0.0496 0.0673  335  MET B C   
11085 O O   . MET B 337  ? 0.3851 0.3467 0.2773 -0.1105 -0.0505 0.0705  335  MET B O   
11086 C CB  . MET B 337  ? 0.4103 0.3426 0.2937 -0.1025 -0.0586 0.0659  335  MET B CB  
11087 C CG  . MET B 337  ? 0.4787 0.4107 0.3685 -0.0963 -0.0577 0.0603  335  MET B CG  
11088 S SD  . MET B 337  ? 0.6014 0.5354 0.4946 -0.0873 -0.0556 0.0552  335  MET B SD  
11089 C CE  . MET B 337  ? 0.5574 0.4746 0.4434 -0.0854 -0.0613 0.0552  335  MET B CE  
11090 N N   . GLY B 338  ? 0.3533 0.3235 0.2517 -0.0991 -0.0453 0.0637  336  GLY B N   
11091 C CA  . GLY B 338  ? 0.3275 0.3111 0.2326 -0.0996 -0.0412 0.0633  336  GLY B CA  
11092 C C   . GLY B 338  ? 0.3622 0.3460 0.2738 -0.0941 -0.0402 0.0581  336  GLY B C   
11093 O O   . GLY B 338  ? 0.3629 0.3403 0.2750 -0.0884 -0.0411 0.0542  336  GLY B O   
11094 N N   . PHE B 339  ? 0.3382 0.3298 0.2550 -0.0958 -0.0383 0.0583  337  PHE B N   
11095 C CA  . PHE B 339  ? 0.3052 0.2968 0.2279 -0.0913 -0.0376 0.0539  337  PHE B CA  
11096 C C   . PHE B 339  ? 0.2845 0.2906 0.2139 -0.0916 -0.0333 0.0539  337  PHE B C   
11097 O O   . PHE B 339  ? 0.3237 0.3359 0.2534 -0.0973 -0.0330 0.0577  337  PHE B O   
11098 C CB  . PHE B 339  ? 0.3376 0.3176 0.2584 -0.0934 -0.0420 0.0537  337  PHE B CB  
11099 C CG  . PHE B 339  ? 0.3284 0.3052 0.2536 -0.0879 -0.0419 0.0487  337  PHE B CG  
11100 C CD1 . PHE B 339  ? 0.3353 0.3039 0.2596 -0.0822 -0.0432 0.0451  337  PHE B CD1 
11101 C CD2 . PHE B 339  ? 0.3218 0.3042 0.2520 -0.0884 -0.0406 0.0478  337  PHE B CD2 
11102 C CE1 . PHE B 339  ? 0.3652 0.3314 0.2936 -0.0773 -0.0430 0.0407  337  PHE B CE1 
11103 C CE2 . PHE B 339  ? 0.3265 0.3061 0.2605 -0.0835 -0.0405 0.0434  337  PHE B CE2 
11104 C CZ  . PHE B 339  ? 0.3453 0.3169 0.2784 -0.0779 -0.0415 0.0399  337  PHE B CZ  
11105 N N   . VAL B 340  ? 0.2915 0.3030 0.2263 -0.0855 -0.0303 0.0498  338  VAL B N   
11106 C CA  . VAL B 340  ? 0.2760 0.3007 0.2172 -0.0846 -0.0262 0.0493  338  VAL B CA  
11107 C C   . VAL B 340  ? 0.2787 0.3016 0.2238 -0.0849 -0.0274 0.0478  338  VAL B C   
11108 O O   . VAL B 340  ? 0.2891 0.3024 0.2340 -0.0819 -0.0297 0.0447  338  VAL B O   
11109 C CB  . VAL B 340  ? 0.2611 0.2918 0.2058 -0.0779 -0.0225 0.0456  338  VAL B CB  
11110 C CG1 . VAL B 340  ? 0.2759 0.3194 0.2273 -0.0766 -0.0186 0.0449  338  VAL B CG1 
11111 C CG2 . VAL B 340  ? 0.2557 0.2886 0.1962 -0.0776 -0.0212 0.0470  338  VAL B CG2 
11112 N N   . VAL B 341  ? 0.2633 0.2958 0.2119 -0.0884 -0.0259 0.0501  339  VAL B N   
11113 C CA  . VAL B 341  ? 0.2523 0.2856 0.2054 -0.0881 -0.0263 0.0485  339  VAL B CA  
11114 C C   . VAL B 341  ? 0.2471 0.2952 0.2070 -0.0859 -0.0217 0.0480  339  VAL B C   
11115 O O   . VAL B 341  ? 0.2653 0.3241 0.2261 -0.0880 -0.0191 0.0509  339  VAL B O   
11116 C CB  . VAL B 341  ? 0.2857 0.3150 0.2363 -0.0952 -0.0299 0.0520  339  VAL B CB  
11117 C CG1 . VAL B 341  ? 0.3193 0.3329 0.2629 -0.0968 -0.0345 0.0523  339  VAL B CG1 
11118 C CG2 . VAL B 341  ? 0.3879 0.4277 0.3386 -0.1014 -0.0285 0.0572  339  VAL B CG2 
11119 N N   . GLN B 342  ? 0.2408 0.2895 0.2053 -0.0813 -0.0207 0.0443  340  GLN B N   
11120 C CA  . GLN B 342  ? 0.2374 0.2985 0.2082 -0.0778 -0.0165 0.0429  340  GLN B CA  
11121 C C   . GLN B 342  ? 0.2598 0.3272 0.2347 -0.0811 -0.0167 0.0446  340  GLN B C   
11122 O O   . GLN B 342  ? 0.2290 0.2904 0.2047 -0.0807 -0.0188 0.0428  340  GLN B O   
11123 C CB  . GLN B 342  ? 0.2306 0.2883 0.2039 -0.0706 -0.0153 0.0379  340  GLN B CB  
11124 C CG  . GLN B 342  ? 0.2245 0.2770 0.1943 -0.0672 -0.0150 0.0362  340  GLN B CG  
11125 C CD  . GLN B 342  ? 0.2270 0.2705 0.1973 -0.0621 -0.0162 0.0317  340  GLN B CD  
11126 O OE1 . GLN B 342  ? 0.2355 0.2709 0.2051 -0.0628 -0.0190 0.0309  340  GLN B OE1 
11127 N NE2 . GLN B 342  ? 0.2284 0.2733 0.1998 -0.0569 -0.0140 0.0289  340  GLN B NE2 
11128 N N   . ALA B 343  ? 0.2316 0.3116 0.2090 -0.0840 -0.0144 0.0479  341  ALA B N   
11129 C CA  . ALA B 343  ? 0.2449 0.3325 0.2264 -0.0876 -0.0146 0.0500  341  ALA B CA  
11130 C C   . ALA B 343  ? 0.2177 0.3101 0.2052 -0.0825 -0.0126 0.0467  341  ALA B C   
11131 O O   . ALA B 343  ? 0.2237 0.3196 0.2143 -0.0849 -0.0135 0.0477  341  ALA B O   
11132 C CB  . ALA B 343  ? 0.2331 0.3342 0.2162 -0.0918 -0.0123 0.0546  341  ALA B CB  
11133 N N   . TYR B 344  ? 0.2245 0.3172 0.2136 -0.0757 -0.0099 0.0430  342  TYR B N   
11134 C CA  . TYR B 344  ? 0.2301 0.3255 0.2244 -0.0713 -0.0087 0.0400  342  TYR B CA  
11135 C C   . TYR B 344  ? 0.2128 0.2960 0.2055 -0.0708 -0.0119 0.0375  342  TYR B C   
11136 O O   . TYR B 344  ? 0.2427 0.3270 0.2391 -0.0676 -0.0113 0.0351  342  TYR B O   
11137 C CB  . TYR B 344  ? 0.2104 0.3099 0.2071 -0.0643 -0.0049 0.0368  342  TYR B CB  
11138 C CG  . TYR B 344  ? 0.2269 0.3163 0.2206 -0.0597 -0.0053 0.0331  342  TYR B CG  
11139 C CD1 . TYR B 344  ? 0.2165 0.2933 0.2052 -0.0614 -0.0087 0.0326  342  TYR B CD1 
11140 C CD2 . TYR B 344  ? 0.2009 0.2936 0.1967 -0.0537 -0.0022 0.0302  342  TYR B CD2 
11141 C CE1 . TYR B 344  ? 0.2248 0.2936 0.2114 -0.0571 -0.0090 0.0294  342  TYR B CE1 
11142 C CE2 . TYR B 344  ? 0.2329 0.3170 0.2262 -0.0498 -0.0026 0.0270  342  TYR B CE2 
11143 C CZ  . TYR B 344  ? 0.2417 0.3143 0.2307 -0.0516 -0.0060 0.0267  342  TYR B CZ  
11144 O OH  . TYR B 344  ? 0.2249 0.2900 0.2120 -0.0478 -0.0064 0.0237  342  TYR B OH  
11145 N N   . GLY B 345  ? 0.2341 0.3059 0.2212 -0.0737 -0.0154 0.0380  343  GLY B N   
11146 C CA  . GLY B 345  ? 0.2302 0.2902 0.2153 -0.0729 -0.0184 0.0355  343  GLY B CA  
11147 C C   . GLY B 345  ? 0.2265 0.2844 0.2105 -0.0786 -0.0216 0.0378  343  GLY B C   
11148 O O   . GLY B 345  ? 0.2406 0.3006 0.2226 -0.0845 -0.0230 0.0417  343  GLY B O   
11149 N N   . LYS B 346  ? 0.1962 0.2498 0.1814 -0.0768 -0.0228 0.0353  344  LYS B N   
11150 C CA  . LYS B 346  ? 0.2248 0.2763 0.2091 -0.0817 -0.0258 0.0369  344  LYS B CA  
11151 C C   . LYS B 346  ? 0.2398 0.2790 0.2171 -0.0863 -0.0302 0.0383  344  LYS B C   
11152 O O   . LYS B 346  ? 0.2852 0.3232 0.2609 -0.0920 -0.0330 0.0408  344  LYS B O   
11153 C CB  . LYS B 346  ? 0.2154 0.2643 0.2020 -0.0781 -0.0259 0.0336  344  LYS B CB  
11154 C CG  . LYS B 346  ? 0.2476 0.3087 0.2410 -0.0742 -0.0221 0.0327  344  LYS B CG  
11155 C CD  . LYS B 346  ? 0.2418 0.2993 0.2369 -0.0703 -0.0222 0.0292  344  LYS B CD  
11156 C CE  . LYS B 346  ? 0.2434 0.3127 0.2449 -0.0673 -0.0190 0.0289  344  LYS B CE  
11157 N NZ  . LYS B 346  ? 0.2130 0.2781 0.2157 -0.0630 -0.0189 0.0254  344  LYS B NZ  
11158 N N   . ARG B 347  ? 0.2485 0.2784 0.2218 -0.0839 -0.0310 0.0368  345  ARG B N   
11159 C CA  . ARG B 347  ? 0.2928 0.3101 0.2592 -0.0877 -0.0353 0.0379  345  ARG B CA  
11160 C C   . ARG B 347  ? 0.2872 0.3066 0.2506 -0.0932 -0.0360 0.0423  345  ARG B C   
11161 O O   . ARG B 347  ? 0.2817 0.2909 0.2391 -0.0973 -0.0399 0.0440  345  ARG B O   
11162 C CB  . ARG B 347  ? 0.2554 0.2613 0.2187 -0.0825 -0.0362 0.0342  345  ARG B CB  
11163 C CG  . ARG B 347  ? 0.2434 0.2457 0.2087 -0.0779 -0.0360 0.0302  345  ARG B CG  
11164 C CD  . ARG B 347  ? 0.2765 0.2715 0.2408 -0.0719 -0.0357 0.0265  345  ARG B CD  
11165 N NE  . ARG B 347  ? 0.2772 0.2804 0.2458 -0.0675 -0.0317 0.0254  345  ARG B NE  
11166 C CZ  . ARG B 347  ? 0.2685 0.2675 0.2368 -0.0627 -0.0311 0.0228  345  ARG B CZ  
11167 N NH1 . ARG B 347  ? 0.2267 0.2140 0.1908 -0.0614 -0.0339 0.0212  345  ARG B NH1 
11168 N NH2 . ARG B 347  ? 0.2068 0.2134 0.1790 -0.0592 -0.0276 0.0218  345  ARG B NH2 
11169 N N   . CYS B 348  ? 0.2676 0.2998 0.2348 -0.0933 -0.0325 0.0443  346  CYS B N   
11170 C CA  . CYS B 348  ? 0.2846 0.3195 0.2490 -0.0975 -0.0324 0.0482  346  CYS B CA  
11171 C C   . CYS B 348  ? 0.3009 0.3313 0.2608 -0.1056 -0.0364 0.0525  346  CYS B C   
11172 O O   . CYS B 348  ? 0.3033 0.3254 0.2572 -0.1082 -0.0387 0.0542  346  CYS B O   
11173 C CB  . CYS B 348  ? 0.2625 0.3137 0.2323 -0.0967 -0.0278 0.0498  346  CYS B CB  
11174 S SG  . CYS B 348  ? 0.3449 0.3999 0.3111 -0.0995 -0.0265 0.0536  346  CYS B SG  
11175 N N   . PRO B 349  ? 0.2976 0.3327 0.2596 -0.1102 -0.0375 0.0544  347  PRO B N   
11176 C CA  . PRO B 349  ? 0.2910 0.3211 0.2482 -0.1184 -0.0416 0.0587  347  PRO B CA  
11177 C C   . PRO B 349  ? 0.3264 0.3383 0.2764 -0.1190 -0.0465 0.0571  347  PRO B C   
11178 O O   . PRO B 349  ? 0.3130 0.3173 0.2570 -0.1242 -0.0497 0.0602  347  PRO B O   
11179 C CB  . PRO B 349  ? 0.3017 0.3411 0.2636 -0.1223 -0.0418 0.0605  347  PRO B CB  
11180 C CG  . PRO B 349  ? 0.2960 0.3391 0.2631 -0.1154 -0.0393 0.0560  347  PRO B CG  
11181 C CD  . PRO B 349  ? 0.2683 0.3131 0.2369 -0.1084 -0.0355 0.0532  347  PRO B CD  
11182 N N   . PHE B 350  ? 0.2776 0.2822 0.2278 -0.1134 -0.0469 0.0524  348  PHE B N   
11183 C CA  . PHE B 350  ? 0.3256 0.3130 0.2691 -0.1129 -0.0512 0.0503  348  PHE B CA  
11184 C C   . PHE B 350  ? 0.3105 0.2901 0.2498 -0.1099 -0.0515 0.0495  348  PHE B C   
11185 O O   . PHE B 350  ? 0.2998 0.2662 0.2322 -0.1122 -0.0555 0.0503  348  PHE B O   
11186 C CB  . PHE B 350  ? 0.3096 0.2932 0.2550 -0.1076 -0.0511 0.0456  348  PHE B CB  
11187 C CG  . PHE B 350  ? 0.3140 0.3065 0.2640 -0.1099 -0.0505 0.0462  348  PHE B CG  
11188 C CD1 . PHE B 350  ? 0.3718 0.3596 0.3185 -0.1163 -0.0546 0.0483  348  PHE B CD1 
11189 C CD2 . PHE B 350  ? 0.3268 0.3328 0.2844 -0.1060 -0.0460 0.0450  348  PHE B CD2 
11190 C CE1 . PHE B 350  ? 0.3729 0.3694 0.3239 -0.1187 -0.0543 0.0492  348  PHE B CE1 
11191 C CE2 . PHE B 350  ? 0.3287 0.3433 0.2906 -0.1082 -0.0456 0.0458  348  PHE B CE2 
11192 C CZ  . PHE B 350  ? 0.3425 0.3526 0.3012 -0.1145 -0.0497 0.0480  348  PHE B CZ  
11193 N N   . VAL B 351  ? 0.3295 0.3170 0.2728 -0.1048 -0.0473 0.0481  349  VAL B N   
11194 C CA  . VAL B 351  ? 0.3013 0.2831 0.2410 -0.1024 -0.0474 0.0479  349  VAL B CA  
11195 C C   . VAL B 351  ? 0.3177 0.2995 0.2529 -0.1092 -0.0490 0.0531  349  VAL B C   
11196 O O   . VAL B 351  ? 0.3218 0.2925 0.2507 -0.1101 -0.0520 0.0539  349  VAL B O   
11197 C CB  . VAL B 351  ? 0.3222 0.3132 0.2671 -0.0960 -0.0426 0.0454  349  VAL B CB  
11198 C CG1 . VAL B 351  ? 0.2926 0.2782 0.2335 -0.0939 -0.0428 0.0454  349  VAL B CG1 
11199 C CG2 . VAL B 351  ? 0.2606 0.2504 0.2094 -0.0895 -0.0413 0.0404  349  VAL B CG2 
11200 N N   . LEU B 352  ? 0.2841 0.2785 0.2226 -0.1139 -0.0470 0.0568  350  LEU B N   
11201 C CA  . LEU B 352  ? 0.3323 0.3275 0.2668 -0.1210 -0.0486 0.0621  350  LEU B CA  
11202 C C   . LEU B 352  ? 0.3691 0.3507 0.2968 -0.1270 -0.0543 0.0642  350  LEU B C   
11203 O O   . LEU B 352  ? 0.3437 0.3173 0.2651 -0.1306 -0.0571 0.0670  350  LEU B O   
11204 C CB  . LEU B 352  ? 0.3174 0.3298 0.2573 -0.1249 -0.0453 0.0657  350  LEU B CB  
11205 C CG  . LEU B 352  ? 0.2953 0.3209 0.2404 -0.1197 -0.0397 0.0646  350  LEU B CG  
11206 C CD1 . LEU B 352  ? 0.3132 0.3556 0.2640 -0.1232 -0.0366 0.0678  350  LEU B CD1 
11207 C CD2 . LEU B 352  ? 0.3409 0.3635 0.2813 -0.1194 -0.0393 0.0659  350  LEU B CD2 
11208 N N   . ASP B 353  ? 0.3338 0.3125 0.2624 -0.1283 -0.0564 0.0629  351  ASP B N   
11209 C CA  . ASP B 353  ? 0.3753 0.3390 0.2969 -0.1330 -0.0622 0.0640  351  ASP B CA  
11210 C C   . ASP B 353  ? 0.3974 0.3451 0.3123 -0.1293 -0.0649 0.0617  351  ASP B C   
11211 O O   . ASP B 353  ? 0.3817 0.3186 0.2894 -0.1339 -0.0690 0.0645  351  ASP B O   
11212 C CB  . ASP B 353  ? 0.3506 0.3123 0.2741 -0.1326 -0.0636 0.0614  351  ASP B CB  
11213 C CG  . ASP B 353  ? 0.4287 0.4034 0.3570 -0.1383 -0.0627 0.0646  351  ASP B CG  
11214 O OD1 . ASP B 353  ? 0.4246 0.4072 0.3533 -0.1443 -0.0623 0.0696  351  ASP B OD1 
11215 O OD2 . ASP B 353  ? 0.4527 0.4299 0.3845 -0.1368 -0.0625 0.0623  351  ASP B OD2 
11216 N N   . PHE B 354  ? 0.3441 0.2900 0.2613 -0.1210 -0.0629 0.0567  352  PHE B N   
11217 C CA  . PHE B 354  ? 0.3897 0.3215 0.3015 -0.1167 -0.0653 0.0543  352  PHE B CA  
11218 C C   . PHE B 354  ? 0.4035 0.3344 0.3116 -0.1183 -0.0653 0.0574  352  PHE B C   
11219 O O   . PHE B 354  ? 0.3783 0.2957 0.2792 -0.1197 -0.0694 0.0584  352  PHE B O   
11220 C CB  . PHE B 354  ? 0.3659 0.2984 0.2819 -0.1077 -0.0625 0.0487  352  PHE B CB  
11221 C CG  . PHE B 354  ? 0.3796 0.3010 0.2914 -0.1027 -0.0641 0.0464  352  PHE B CG  
11222 C CD1 . PHE B 354  ? 0.4047 0.3107 0.3110 -0.1012 -0.0683 0.0443  352  PHE B CD1 
11223 C CD2 . PHE B 354  ? 0.3702 0.2964 0.2834 -0.0996 -0.0615 0.0465  352  PHE B CD2 
11224 C CE1 . PHE B 354  ? 0.3954 0.2915 0.2980 -0.0965 -0.0699 0.0425  352  PHE B CE1 
11225 C CE2 . PHE B 354  ? 0.3818 0.2981 0.2912 -0.0953 -0.0633 0.0447  352  PHE B CE2 
11226 C CZ  . PHE B 354  ? 0.4150 0.3165 0.3195 -0.0936 -0.0674 0.0427  352  PHE B CZ  
11227 N N   . ILE B 355  ? 0.3562 0.3012 0.2690 -0.1178 -0.0609 0.0588  353  ILE B N   
11228 C CA  . ILE B 355  ? 0.3492 0.2942 0.2586 -0.1188 -0.0605 0.0615  353  ILE B CA  
11229 C C   . ILE B 355  ? 0.3981 0.3396 0.3018 -0.1277 -0.0638 0.0673  353  ILE B C   
11230 O O   . ILE B 355  ? 0.3739 0.3057 0.2709 -0.1292 -0.0667 0.0692  353  ILE B O   
11231 C CB  . ILE B 355  ? 0.3344 0.2955 0.2499 -0.1159 -0.0548 0.0614  353  ILE B CB  
11232 C CG1 . ILE B 355  ? 0.3583 0.3210 0.2786 -0.1071 -0.0521 0.0558  353  ILE B CG1 
11233 C CG2 . ILE B 355  ? 0.3550 0.3168 0.2664 -0.1177 -0.0545 0.0647  353  ILE B CG2 
11234 C CD1 . ILE B 355  ? 0.3438 0.3218 0.2703 -0.1040 -0.0466 0.0552  353  ILE B CD1 
11235 N N   . ILE B 356  ? 0.3641 0.3136 0.2704 -0.1337 -0.0636 0.0703  354  ILE B N   
11236 C CA  . ILE B 356  ? 0.4103 0.3569 0.3113 -0.1429 -0.0668 0.0761  354  ILE B CA  
11237 C C   . ILE B 356  ? 0.4064 0.3334 0.2992 -0.1449 -0.0731 0.0759  354  ILE B C   
11238 O O   . ILE B 356  ? 0.4389 0.3574 0.3247 -0.1494 -0.0763 0.0796  354  ILE B O   
11239 C CB  . ILE B 356  ? 0.3715 0.3309 0.2776 -0.1488 -0.0656 0.0790  354  ILE B CB  
11240 C CG1 . ILE B 356  ? 0.3352 0.3140 0.2484 -0.1474 -0.0595 0.0801  354  ILE B CG1 
11241 C CG2 . ILE B 356  ? 0.4096 0.3635 0.3099 -0.1588 -0.0700 0.0848  354  ILE B CG2 
11242 C CD1 . ILE B 356  ? 0.3576 0.3506 0.2775 -0.1511 -0.0575 0.0819  354  ILE B CD1 
11243 N N   . ASP B 357  ? 0.3929 0.3121 0.2860 -0.1414 -0.0749 0.0717  355  ASP B N   
11244 C CA  . ASP B 357  ? 0.4467 0.3465 0.3316 -0.1422 -0.0807 0.0708  355  ASP B CA  
11245 C C   . ASP B 357  ? 0.4358 0.3251 0.3159 -0.1371 -0.0819 0.0692  355  ASP B C   
11246 O O   . ASP B 357  ? 0.4189 0.2942 0.2909 -0.1402 -0.0867 0.0713  355  ASP B O   
11247 C CB  . ASP B 357  ? 0.4434 0.3381 0.3298 -0.1386 -0.0818 0.0661  355  ASP B CB  
11248 C CG  . ASP B 357  ? 0.4655 0.3398 0.3435 -0.1377 -0.0875 0.0643  355  ASP B CG  
11249 O OD1 . ASP B 357  ? 0.5076 0.3729 0.3794 -0.1447 -0.0921 0.0675  355  ASP B OD1 
11250 O OD2 . ASP B 357  ? 0.4823 0.3496 0.3597 -0.1299 -0.0873 0.0598  355  ASP B OD2 
11251 N N   . LEU B 358  ? 0.4298 0.3251 0.3147 -0.1293 -0.0780 0.0655  356  LEU B N   
11252 C CA  . LEU B 358  ? 0.4182 0.3046 0.2990 -0.1244 -0.0791 0.0641  356  LEU B CA  
11253 C C   . LEU B 358  ? 0.4214 0.3076 0.2974 -0.1295 -0.0800 0.0694  356  LEU B C   
11254 O O   . LEU B 358  ? 0.4482 0.3209 0.3170 -0.1296 -0.0840 0.0703  356  LEU B O   
11255 C CB  . LEU B 358  ? 0.4219 0.3168 0.3094 -0.1159 -0.0744 0.0596  356  LEU B CB  
11256 C CG  . LEU B 358  ? 0.4274 0.3170 0.3123 -0.1107 -0.0746 0.0584  356  LEU B CG  
11257 C CD1 . LEU B 358  ? 0.4466 0.3180 0.3248 -0.1083 -0.0798 0.0566  356  LEU B CD1 
11258 C CD2 . LEU B 358  ? 0.4112 0.3105 0.3034 -0.1030 -0.0699 0.0541  356  LEU B CD2 
11259 N N   . ALA B 359  ? 0.3982 0.2991 0.2779 -0.1339 -0.0766 0.0730  357  ALA B N   
11260 C CA  . ALA B 359  ? 0.4258 0.3278 0.3009 -0.1393 -0.0772 0.0783  357  ALA B CA  
11261 C C   . ALA B 359  ? 0.4734 0.3623 0.3404 -0.1471 -0.0830 0.0825  357  ALA B C   
11262 O O   . ALA B 359  ? 0.4768 0.3560 0.3366 -0.1491 -0.0860 0.0852  357  ALA B O   
11263 C CB  . ALA B 359  ? 0.4277 0.3489 0.3087 -0.1426 -0.0721 0.0814  357  ALA B CB  
11264 N N   . ARG B 360  ? 0.4902 0.3782 0.3580 -0.1515 -0.0848 0.0831  358  ARG B N   
11265 C CA  . ARG B 360  ? 0.5400 0.4154 0.4000 -0.1595 -0.0906 0.0871  358  ARG B CA  
11266 C C   . ARG B 360  ? 0.4686 0.3231 0.3204 -0.1562 -0.0959 0.0849  358  ARG B C   
11267 O O   . ARG B 360  ? 0.5518 0.3953 0.3956 -0.1609 -0.1001 0.0888  358  ARG B O   
11268 C CB  . ARG B 360  ? 0.4838 0.3620 0.3466 -0.1640 -0.0916 0.0872  358  ARG B CB  
11269 C CG  . ARG B 360  ? 0.5016 0.3984 0.3704 -0.1699 -0.0880 0.0914  358  ARG B CG  
11270 C CD  . ARG B 360  ? 0.5810 0.4824 0.4540 -0.1730 -0.0885 0.0908  358  ARG B CD  
11271 N NE  . ARG B 360  ? 0.5472 0.4655 0.4251 -0.1799 -0.0858 0.0957  358  ARG B NE  
11272 C CZ  . ARG B 360  ? 0.5476 0.4784 0.4327 -0.1810 -0.0835 0.0952  358  ARG B CZ  
11273 N NH1 . ARG B 360  ? 0.6190 0.5473 0.5071 -0.1758 -0.0835 0.0901  358  ARG B NH1 
11274 N NH2 . ARG B 360  ? 0.6976 0.6440 0.5871 -0.1874 -0.0812 0.1001  358  ARG B NH2 
11275 N N   . ARG B 361  ? 0.4871 0.3361 0.3408 -0.1481 -0.0957 0.0789  359  ARG B N   
11276 C CA  . ARG B 361  ? 0.5585 0.3879 0.4045 -0.1447 -0.1008 0.0767  359  ARG B CA  
11277 C C   . ARG B 361  ? 0.5641 0.3895 0.4075 -0.1397 -0.1006 0.0763  359  ARG B C   
11278 O O   . ARG B 361  ? 0.5441 0.3530 0.3797 -0.1388 -0.1054 0.0763  359  ARG B O   
11279 C CB  . ARG B 361  ? 0.5714 0.3954 0.4196 -0.1382 -0.1011 0.0705  359  ARG B CB  
11280 C CG  . ARG B 361  ? 0.5727 0.4097 0.4301 -0.1304 -0.0955 0.0659  359  ARG B CG  
11281 C CD  . ARG B 361  ? 0.5144 0.3479 0.3739 -0.1265 -0.0958 0.0610  359  ARG B CD  
11282 N NE  . ARG B 361  ? 0.4908 0.3379 0.3595 -0.1202 -0.0903 0.0571  359  ARG B NE  
11283 C CZ  . ARG B 361  ? 0.4622 0.3087 0.3334 -0.1117 -0.0884 0.0527  359  ARG B CZ  
11284 N NH1 . ARG B 361  ? 0.4450 0.2785 0.3107 -0.1079 -0.0915 0.0515  359  ARG B NH1 
11285 N NH2 . ARG B 361  ? 0.4305 0.2898 0.3101 -0.1069 -0.0834 0.0496  359  ARG B NH2 
11286 N N   . SER B 362  ? 0.5320 0.3717 0.3814 -0.1365 -0.0954 0.0759  360  SER B N   
11287 C CA  . SER B 362  ? 0.5066 0.3433 0.3537 -0.1318 -0.0952 0.0755  360  SER B CA  
11288 C C   . SER B 362  ? 0.4946 0.3331 0.3371 -0.1380 -0.0958 0.0815  360  SER B C   
11289 O O   . SER B 362  ? 0.5223 0.3560 0.3612 -0.1350 -0.0967 0.0818  360  SER B O   
11290 C CB  . SER B 362  ? 0.4813 0.3311 0.3368 -0.1241 -0.0896 0.0713  360  SER B CB  
11291 O OG  . SER B 362  ? 0.4489 0.3163 0.3103 -0.1274 -0.0847 0.0735  360  SER B OG  
11292 N N   . GLY B 363  ? 0.4504 0.2957 0.2926 -0.1466 -0.0954 0.0865  361  GLY B N   
11293 C CA  . GLY B 363  ? 0.4664 0.3145 0.3043 -0.1526 -0.0956 0.0924  361  GLY B CA  
11294 C C   . GLY B 363  ? 0.4636 0.3264 0.3063 -0.1489 -0.0900 0.0921  361  GLY B C   
11295 O O   . GLY B 363  ? 0.5201 0.3817 0.3579 -0.1506 -0.0905 0.0954  361  GLY B O   
11296 N N   . ARG B 364  ? 0.4881 0.3639 0.3395 -0.1439 -0.0850 0.0881  362  ARG B N   
11297 C CA  . ARG B 364  ? 0.5129 0.4035 0.3695 -0.1401 -0.0794 0.0873  362  ARG B CA  
11298 C C   . ARG B 364  ? 0.4858 0.3939 0.3490 -0.1441 -0.0749 0.0891  362  ARG B C   
11299 O O   . ARG B 364  ? 0.4838 0.3951 0.3519 -0.1439 -0.0743 0.0870  362  ARG B O   
11300 C CB  . ARG B 364  ? 0.4638 0.3549 0.3254 -0.1301 -0.0773 0.0806  362  ARG B CB  
11301 C CG  . ARG B 364  ? 0.4986 0.3737 0.3551 -0.1250 -0.0815 0.0780  362  ARG B CG  
11302 C CD  . ARG B 364  ? 0.5258 0.3994 0.3778 -0.1238 -0.0817 0.0799  362  ARG B CD  
11303 N NE  . ARG B 364  ? 0.4890 0.3461 0.3353 -0.1200 -0.0866 0.0783  362  ARG B NE  
11304 C CZ  . ARG B 364  ? 0.4990 0.3530 0.3479 -0.1116 -0.0864 0.0732  362  ARG B CZ  
11305 N NH1 . ARG B 364  ? 0.4744 0.3402 0.3313 -0.1063 -0.0817 0.0692  362  ARG B NH1 
11306 N NH2 . ARG B 364  ? 0.5282 0.3670 0.3717 -0.1086 -0.0912 0.0721  362  ARG B NH2 
11307 N N   . ARG B 365  ? 0.4548 0.3743 0.3181 -0.1475 -0.0718 0.0930  363  ARG B N   
11308 C CA  . ARG B 365  ? 0.4305 0.3685 0.3013 -0.1495 -0.0667 0.0941  363  ARG B CA  
11309 C C   . ARG B 365  ? 0.4071 0.3545 0.2847 -0.1407 -0.0618 0.0887  363  ARG B C   
11310 O O   . ARG B 365  ? 0.4314 0.3830 0.3081 -0.1373 -0.0593 0.0883  363  ARG B O   
11311 C CB  . ARG B 365  ? 0.4958 0.4433 0.3642 -0.1564 -0.0650 0.1004  363  ARG B CB  
11312 C CG  . ARG B 365  ? 0.4490 0.4162 0.3252 -0.1584 -0.0597 0.1016  363  ARG B CG  
11313 C CD  . ARG B 365  ? 0.5521 0.5269 0.4256 -0.1675 -0.0593 0.1088  363  ARG B CD  
11314 N NE  . ARG B 365  ? 0.5120 0.5052 0.3931 -0.1699 -0.0548 0.1103  363  ARG B NE  
11315 C CZ  . ARG B 365  ? 0.5247 0.5343 0.4089 -0.1698 -0.0496 0.1122  363  ARG B CZ  
11316 N NH1 . ARG B 365  ? 0.5110 0.5208 0.3907 -0.1680 -0.0480 0.1131  363  ARG B NH1 
11317 N NH2 . ARG B 365  ? 0.4763 0.5022 0.3679 -0.1716 -0.0458 0.1133  363  ARG B NH2 
11318 N N   . ILE B 366  ? 0.4331 0.3829 0.3168 -0.1369 -0.0606 0.0844  364  ILE B N   
11319 C CA  . ILE B 366  ? 0.4066 0.3634 0.2966 -0.1285 -0.0566 0.0791  364  ILE B CA  
11320 C C   . ILE B 366  ? 0.4014 0.3771 0.2973 -0.1289 -0.0508 0.0803  364  ILE B C   
11321 O O   . ILE B 366  ? 0.4049 0.3894 0.3038 -0.1340 -0.0496 0.0831  364  ILE B O   
11322 C CB  . ILE B 366  ? 0.3423 0.2943 0.2364 -0.1242 -0.0575 0.0742  364  ILE B CB  
11323 C CG1 . ILE B 366  ? 0.4129 0.3462 0.3009 -0.1227 -0.0630 0.0726  364  ILE B CG1 
11324 C CG2 . ILE B 366  ? 0.3423 0.3029 0.2433 -0.1162 -0.0531 0.0691  364  ILE B CG2 
11325 C CD1 . ILE B 366  ? 0.4329 0.3600 0.3235 -0.1196 -0.0646 0.0684  364  ILE B CD1 
11326 N N   . MET B 367  ? 0.3796 0.3613 0.2767 -0.1236 -0.0473 0.0782  365  MET B N   
11327 C CA  . MET B 367  ? 0.3562 0.3554 0.2590 -0.1224 -0.0416 0.0784  365  MET B CA  
11328 C C   . MET B 367  ? 0.3382 0.3427 0.2490 -0.1170 -0.0392 0.0735  365  MET B C   
11329 O O   . MET B 367  ? 0.3390 0.3366 0.2507 -0.1106 -0.0398 0.0687  365  MET B O   
11330 C CB  . MET B 367  ? 0.3261 0.3290 0.2265 -0.1189 -0.0390 0.0780  365  MET B CB  
11331 C CG  . MET B 367  ? 0.4135 0.4087 0.3054 -0.1233 -0.0420 0.0823  365  MET B CG  
11332 S SD  . MET B 367  ? 0.4510 0.4488 0.3391 -0.1188 -0.0395 0.0815  365  MET B SD  
11333 C CE  . MET B 367  ? 0.4559 0.4740 0.3472 -0.1212 -0.0333 0.0845  365  MET B CE  
11334 N N   . VAL B 368  ? 0.3036 0.3199 0.2199 -0.1195 -0.0367 0.0748  366  VAL B N   
11335 C CA  . VAL B 368  ? 0.2898 0.3108 0.2133 -0.1151 -0.0348 0.0707  366  VAL B CA  
11336 C C   . VAL B 368  ? 0.3202 0.3580 0.2494 -0.1124 -0.0290 0.0703  366  VAL B C   
11337 O O   . VAL B 368  ? 0.3403 0.3895 0.2713 -0.1171 -0.0270 0.0742  366  VAL B O   
11338 C CB  . VAL B 368  ? 0.2985 0.3177 0.2238 -0.1199 -0.0373 0.0720  366  VAL B CB  
11339 C CG1 . VAL B 368  ? 0.3400 0.3627 0.2721 -0.1146 -0.0355 0.0674  366  VAL B CG1 
11340 C CG2 . VAL B 368  ? 0.3840 0.3859 0.3024 -0.1230 -0.0432 0.0728  366  VAL B CG2 
11341 N N   . ARG B 369  ? 0.2834 0.3230 0.2155 -0.1049 -0.0264 0.0656  367  ARG B N   
11342 C CA  . ARG B 369  ? 0.2702 0.3247 0.2077 -0.1016 -0.0211 0.0646  367  ARG B CA  
11343 C C   . ARG B 369  ? 0.3021 0.3615 0.2467 -0.0997 -0.0200 0.0622  367  ARG B C   
11344 O O   . ARG B 369  ? 0.3017 0.3540 0.2481 -0.0951 -0.0212 0.0580  367  ARG B O   
11345 C CB  . ARG B 369  ? 0.2950 0.3489 0.2317 -0.0947 -0.0189 0.0609  367  ARG B CB  
11346 C CG  . ARG B 369  ? 0.2696 0.3382 0.2113 -0.0909 -0.0135 0.0596  367  ARG B CG  
11347 C CD  . ARG B 369  ? 0.2757 0.3421 0.2176 -0.0834 -0.0119 0.0548  367  ARG B CD  
11348 N NE  . ARG B 369  ? 0.2969 0.3575 0.2320 -0.0833 -0.0129 0.0556  367  ARG B NE  
11349 C CZ  . ARG B 369  ? 0.3269 0.3801 0.2602 -0.0782 -0.0137 0.0518  367  ARG B CZ  
11350 N NH1 . ARG B 369  ? 0.3057 0.3561 0.2432 -0.0729 -0.0136 0.0472  367  ARG B NH1 
11351 N NH2 . ARG B 369  ? 0.2959 0.3445 0.2228 -0.0786 -0.0149 0.0530  367  ARG B NH2 
11352 N N   . LEU B 370  ? 0.2733 0.3449 0.2219 -0.1033 -0.0180 0.0652  368  LEU B N   
11353 C CA  . LEU B 370  ? 0.2808 0.3590 0.2364 -0.1016 -0.0166 0.0634  368  LEU B CA  
11354 C C   . LEU B 370  ? 0.2494 0.3387 0.2098 -0.0951 -0.0116 0.0606  368  LEU B C   
11355 O O   . LEU B 370  ? 0.2957 0.3958 0.2563 -0.0955 -0.0083 0.0627  368  LEU B O   
11356 C CB  . LEU B 370  ? 0.2889 0.3752 0.2468 -0.1087 -0.0172 0.0680  368  LEU B CB  
11357 C CG  . LEU B 370  ? 0.3093 0.4025 0.2742 -0.1076 -0.0163 0.0666  368  LEU B CG  
11358 C CD1 . LEU B 370  ? 0.2683 0.3482 0.2326 -0.1054 -0.0198 0.0629  368  LEU B CD1 
11359 C CD2 . LEU B 370  ? 0.2668 0.3690 0.2338 -0.1150 -0.0169 0.0717  368  LEU B CD2 
11360 N N   . VAL B 371  ? 0.2589 0.3450 0.2225 -0.0890 -0.0111 0.0557  369  VAL B N   
11361 C CA  . VAL B 371  ? 0.2135 0.3087 0.1817 -0.0826 -0.0067 0.0527  369  VAL B CA  
11362 C C   . VAL B 371  ? 0.2490 0.3481 0.2235 -0.0808 -0.0062 0.0508  369  VAL B C   
11363 O O   . VAL B 371  ? 0.2642 0.3574 0.2391 -0.0838 -0.0093 0.0512  369  VAL B O   
11364 C CB  . VAL B 371  ? 0.2108 0.2981 0.1766 -0.0764 -0.0065 0.0483  369  VAL B CB  
11365 C CG1 . VAL B 371  ? 0.2333 0.3147 0.1921 -0.0784 -0.0078 0.0501  369  VAL B CG1 
11366 C CG2 . VAL B 371  ? 0.2171 0.2933 0.1840 -0.0736 -0.0092 0.0446  369  VAL B CG2 
11367 N N   . LYS B 372  ? 0.1996 0.3082 0.1789 -0.0757 -0.0023 0.0487  370  LYS B N   
11368 C CA  . LYS B 372  ? 0.2007 0.3114 0.1857 -0.0729 -0.0019 0.0462  370  LYS B CA  
11369 C C   . LYS B 372  ? 0.2107 0.3102 0.1951 -0.0676 -0.0032 0.0414  370  LYS B C   
11370 O O   . LYS B 372  ? 0.2251 0.3164 0.2095 -0.0686 -0.0061 0.0403  370  LYS B O   
11371 C CB  . LYS B 372  ? 0.2023 0.3279 0.1927 -0.0698 0.0026  0.0463  370  LYS B CB  
11372 C CG  . LYS B 372  ? 0.2336 0.3708 0.2253 -0.0757 0.0034  0.0515  370  LYS B CG  
11373 C CD  . LYS B 372  ? 0.2369 0.3899 0.2345 -0.0730 0.0076  0.0520  370  LYS B CD  
11374 C CE  . LYS B 372  ? 0.2950 0.4595 0.2934 -0.0793 0.0084  0.0576  370  LYS B CE  
11375 N NZ  . LYS B 372  ? 0.2537 0.4348 0.2572 -0.0762 0.0131  0.0583  370  LYS B NZ  
11376 N N   . GLY B 373  ? 0.2374 0.3358 0.2208 -0.0624 -0.0012 0.0385  371  GLY B N   
11377 C CA  . GLY B 373  ? 0.2227 0.3105 0.2054 -0.0581 -0.0027 0.0343  371  GLY B CA  
11378 C C   . GLY B 373  ? 0.2607 0.3514 0.2454 -0.0514 0.0003  0.0307  371  GLY B C   
11379 O O   . GLY B 373  ? 0.2459 0.3464 0.2347 -0.0491 0.0034  0.0304  371  GLY B O   
11380 N N   . ALA B 374  ? 0.2266 0.3086 0.2085 -0.0483 -0.0007 0.0279  372  ALA B N   
11381 C CA  . ALA B 374  ? 0.2295 0.3134 0.2120 -0.0426 0.0018  0.0248  372  ALA B CA  
11382 C C   . ALA B 374  ? 0.2527 0.3323 0.2387 -0.0379 0.0017  0.0207  372  ALA B C   
11383 O O   . ALA B 374  ? 0.2318 0.3123 0.2184 -0.0332 0.0036  0.0180  372  ALA B O   
11384 C CB  . ALA B 374  ? 0.2497 0.3278 0.2265 -0.0422 0.0009  0.0245  372  ALA B CB  
11385 N N   . TYR B 375  ? 0.1834 0.2583 0.1715 -0.0391 -0.0004 0.0203  373  TYR B N   
11386 C CA  . TYR B 375  ? 0.2136 0.2832 0.2043 -0.0350 -0.0008 0.0167  373  TYR B CA  
11387 C C   . TYR B 375  ? 0.2212 0.2955 0.2170 -0.0342 0.0002  0.0162  373  TYR B C   
11388 O O   . TYR B 375  ? 0.2028 0.2720 0.2005 -0.0324 -0.0009 0.0141  373  TYR B O   
11389 C CB  . TYR B 375  ? 0.2243 0.2825 0.2124 -0.0361 -0.0044 0.0159  373  TYR B CB  
11390 C CG  . TYR B 375  ? 0.2230 0.2753 0.2060 -0.0367 -0.0059 0.0162  373  TYR B CG  
11391 C CD1 . TYR B 375  ? 0.2411 0.2930 0.2199 -0.0413 -0.0072 0.0196  373  TYR B CD1 
11392 C CD2 . TYR B 375  ? 0.3010 0.3482 0.2833 -0.0327 -0.0062 0.0132  373  TYR B CD2 
11393 C CE1 . TYR B 375  ? 0.2846 0.3310 0.2585 -0.0418 -0.0088 0.0200  373  TYR B CE1 
11394 C CE2 . TYR B 375  ? 0.3433 0.3854 0.3209 -0.0332 -0.0078 0.0136  373  TYR B CE2 
11395 C CZ  . TYR B 375  ? 0.3247 0.3663 0.2981 -0.0376 -0.0091 0.0170  373  TYR B CZ  
11396 O OH  . TYR B 375  ? 0.3562 0.3923 0.3246 -0.0381 -0.0109 0.0174  373  TYR B OH  
11397 N N   . TRP B 376  ? 0.1962 0.2808 0.1944 -0.0353 0.0024  0.0184  374  TRP B N   
11398 C CA  . TRP B 376  ? 0.2024 0.2915 0.2051 -0.0357 0.0027  0.0187  374  TRP B CA  
11399 C C   . TRP B 376  ? 0.2224 0.3099 0.2285 -0.0305 0.0037  0.0152  374  TRP B C   
11400 O O   . TRP B 376  ? 0.2118 0.2953 0.2195 -0.0306 0.0023  0.0143  374  TRP B O   
11401 C CB  . TRP B 376  ? 0.1821 0.2836 0.1872 -0.0372 0.0051  0.0216  374  TRP B CB  
11402 C CG  . TRP B 376  ? 0.2153 0.3216 0.2250 -0.0380 0.0050  0.0223  374  TRP B CG  
11403 C CD1 . TRP B 376  ? 0.1928 0.2978 0.2026 -0.0428 0.0025  0.0244  374  TRP B CD1 
11404 C CD2 . TRP B 376  ? 0.2450 0.3573 0.2593 -0.0338 0.0072  0.0207  374  TRP B CD2 
11405 N NE1 . TRP B 376  ? 0.2160 0.3263 0.2304 -0.0419 0.0031  0.0243  374  TRP B NE1 
11406 C CE2 . TRP B 376  ? 0.2282 0.3431 0.2455 -0.0363 0.0060  0.0222  374  TRP B CE2 
11407 C CE3 . TRP B 376  ? 0.2461 0.3614 0.2620 -0.0282 0.0099  0.0183  374  TRP B CE3 
11408 C CZ2 . TRP B 376  ? 0.2343 0.3551 0.2563 -0.0333 0.0074  0.0214  374  TRP B CZ2 
11409 C CZ3 . TRP B 376  ? 0.2789 0.3997 0.2994 -0.0251 0.0114  0.0175  374  TRP B CZ3 
11410 C CH2 . TRP B 376  ? 0.2591 0.3828 0.2827 -0.0277 0.0102  0.0191  374  TRP B CH2 
11411 N N   . ASP B 377  ? 0.2028 0.2931 0.2095 -0.0261 0.0062  0.0133  375  ASP B N   
11412 C CA  . ASP B 377  ? 0.2324 0.3213 0.2422 -0.0214 0.0071  0.0102  375  ASP B CA  
11413 C C   . ASP B 377  ? 0.2269 0.3054 0.2358 -0.0208 0.0047  0.0079  375  ASP B C   
11414 O O   . ASP B 377  ? 0.2206 0.2971 0.2322 -0.0192 0.0045  0.0065  375  ASP B O   
11415 C CB  . ASP B 377  ? 0.3627 0.4545 0.3721 -0.0169 0.0096  0.0083  375  ASP B CB  
11416 C CG  . ASP B 377  ? 0.4045 0.5075 0.4161 -0.0159 0.0125  0.0098  375  ASP B CG  
11417 O OD1 . ASP B 377  ? 0.4952 0.6032 0.5109 -0.0152 0.0132  0.0102  375  ASP B OD1 
11418 O OD2 . ASP B 377  ? 0.5162 0.6234 0.5254 -0.0156 0.0141  0.0105  375  ASP B OD2 
11419 N N   . ALA B 378  ? 0.2219 0.2938 0.2269 -0.0219 0.0030  0.0078  376  ALA B N   
11420 C CA  . ALA B 378  ? 0.2310 0.2934 0.2352 -0.0211 0.0008  0.0057  376  ALA B CA  
11421 C C   . ALA B 378  ? 0.2213 0.2803 0.2260 -0.0239 -0.0013 0.0066  376  ALA B C   
11422 O O   . ALA B 378  ? 0.2040 0.2578 0.2099 -0.0223 -0.0023 0.0047  376  ALA B O   
11423 C CB  . ALA B 378  ? 0.2620 0.3188 0.2618 -0.0217 -0.0007 0.0056  376  ALA B CB  
11424 N N   . GLU B 379  ? 0.1931 0.2547 0.1965 -0.0283 -0.0022 0.0096  377  GLU B N   
11425 C CA  . GLU B 379  ? 0.2187 0.2762 0.2218 -0.0312 -0.0045 0.0104  377  GLU B CA  
11426 C C   . GLU B 379  ? 0.2015 0.2628 0.2088 -0.0299 -0.0035 0.0097  377  GLU B C   
11427 O O   . GLU B 379  ? 0.2022 0.2583 0.2097 -0.0299 -0.0051 0.0086  377  GLU B O   
11428 C CB  . GLU B 379  ? 0.1891 0.2483 0.1895 -0.0367 -0.0059 0.0140  377  GLU B CB  
11429 C CG  . GLU B 379  ? 0.2148 0.2695 0.2104 -0.0387 -0.0073 0.0152  377  GLU B CG  
11430 C CD  . GLU B 379  ? 0.2414 0.2847 0.2338 -0.0383 -0.0103 0.0137  377  GLU B CD  
11431 O OE1 . GLU B 379  ? 0.2325 0.2711 0.2263 -0.0366 -0.0112 0.0116  377  GLU B OE1 
11432 O OE2 . GLU B 379  ? 0.2274 0.2663 0.2157 -0.0397 -0.0117 0.0146  377  GLU B OE2 
11433 N N   . ILE B 380  ? 0.1841 0.2545 0.1945 -0.0285 -0.0010 0.0103  378  ILE B N   
11434 C CA  . ILE B 380  ? 0.1633 0.2374 0.1777 -0.0269 0.0000  0.0097  378  ILE B CA  
11435 C C   . ILE B 380  ? 0.1943 0.2629 0.2099 -0.0227 0.0002  0.0064  378  ILE B C   
11436 O O   . ILE B 380  ? 0.1818 0.2476 0.1986 -0.0225 -0.0007 0.0056  378  ILE B O   
11437 C CB  . ILE B 380  ? 0.1887 0.2737 0.2062 -0.0256 0.0027  0.0108  378  ILE B CB  
11438 C CG1 . ILE B 380  ? 0.2178 0.3091 0.2345 -0.0301 0.0026  0.0144  378  ILE B CG1 
11439 C CG2 . ILE B 380  ? 0.1846 0.2730 0.2062 -0.0235 0.0035  0.0102  378  ILE B CG2 
11440 C CD1 . ILE B 380  ? 0.2095 0.3003 0.2261 -0.0348 0.0002  0.0165  378  ILE B CD1 
11441 N N   . LYS B 381  ? 0.1741 0.2414 0.1893 -0.0195 0.0014  0.0046  379  LYS B N   
11442 C CA  . LYS B 381  ? 0.1611 0.2238 0.1778 -0.0158 0.0016  0.0017  379  LYS B CA  
11443 C C   . LYS B 381  ? 0.1867 0.2408 0.2016 -0.0168 -0.0008 0.0007  379  LYS B C   
11444 O O   . LYS B 381  ? 0.2002 0.2518 0.2169 -0.0153 -0.0010 -0.0007 379  LYS B O   
11445 C CB  . LYS B 381  ? 0.2003 0.2625 0.2163 -0.0128 0.0029  0.0001  379  LYS B CB  
11446 C CG  . LYS B 381  ? 0.1941 0.2511 0.2114 -0.0095 0.0028  -0.0027 379  LYS B CG  
11447 C CD  . LYS B 381  ? 0.1990 0.2557 0.2154 -0.0067 0.0039  -0.0043 379  LYS B CD  
11448 C CE  . LYS B 381  ? 0.2268 0.2793 0.2451 -0.0036 0.0039  -0.0069 379  LYS B CE  
11449 N NZ  . LYS B 381  ? 0.1969 0.2486 0.2139 -0.0012 0.0045  -0.0084 379  LYS B NZ  
11450 N N   . ARG B 382  ? 0.1943 0.2442 0.2058 -0.0192 -0.0026 0.0016  380  ARG B N   
11451 C CA  . ARG B 382  ? 0.2398 0.2813 0.2493 -0.0196 -0.0050 0.0005  380  ARG B CA  
11452 C C   . ARG B 382  ? 0.2100 0.2500 0.2197 -0.0215 -0.0062 0.0010  380  ARG B C   
11453 O O   . ARG B 382  ? 0.2043 0.2394 0.2144 -0.0199 -0.0069 -0.0007 380  ARG B O   
11454 C CB  . ARG B 382  ? 0.2481 0.2853 0.2534 -0.0220 -0.0069 0.0017  380  ARG B CB  
11455 C CG  . ARG B 382  ? 0.3202 0.3484 0.3232 -0.0218 -0.0094 0.0005  380  ARG B CG  
11456 C CD  . ARG B 382  ? 0.4216 0.4470 0.4259 -0.0180 -0.0090 -0.0020 380  ARG B CD  
11457 N NE  . ARG B 382  ? 0.4140 0.4377 0.4211 -0.0155 -0.0086 -0.0041 380  ARG B NE  
11458 C CZ  . ARG B 382  ? 0.4929 0.5166 0.5026 -0.0122 -0.0075 -0.0061 380  ARG B CZ  
11459 N NH1 . ARG B 382  ? 0.4746 0.4997 0.4844 -0.0108 -0.0068 -0.0067 380  ARG B NH1 
11460 N NH2 . ARG B 382  ? 0.3977 0.4199 0.4097 -0.0104 -0.0073 -0.0077 380  ARG B NH2 
11461 N N   . ALA B 383  ? 0.1762 0.2204 0.1856 -0.0248 -0.0064 0.0035  381  ALA B N   
11462 C CA  . ALA B 383  ? 0.2089 0.2515 0.2181 -0.0268 -0.0078 0.0039  381  ALA B CA  
11463 C C   . ALA B 383  ? 0.1936 0.2388 0.2064 -0.0239 -0.0063 0.0025  381  ALA B C   
11464 O O   . ALA B 383  ? 0.1593 0.2003 0.1717 -0.0236 -0.0074 0.0014  381  ALA B O   
11465 C CB  . ALA B 383  ? 0.2022 0.2496 0.2106 -0.0312 -0.0085 0.0071  381  ALA B CB  
11466 N N   . GLN B 384  ? 0.1692 0.2212 0.1853 -0.0216 -0.0038 0.0024  382  GLN B N   
11467 C CA  . GLN B 384  ? 0.1912 0.2453 0.2106 -0.0187 -0.0024 0.0010  382  GLN B CA  
11468 C C   . GLN B 384  ? 0.1802 0.2281 0.1997 -0.0157 -0.0024 -0.0016 382  GLN B C   
11469 O O   . GLN B 384  ? 0.1897 0.2355 0.2100 -0.0148 -0.0026 -0.0026 382  GLN B O   
11470 C CB  . GLN B 384  ? 0.2104 0.2723 0.2328 -0.0166 0.0001  0.0014  382  GLN B CB  
11471 C CG  . GLN B 384  ? 0.1634 0.2330 0.1867 -0.0192 0.0004  0.0041  382  GLN B CG  
11472 C CD  . GLN B 384  ? 0.1897 0.2671 0.2161 -0.0164 0.0029  0.0043  382  GLN B CD  
11473 O OE1 . GLN B 384  ? 0.2138 0.2901 0.2404 -0.0132 0.0043  0.0027  382  GLN B OE1 
11474 N NE2 . GLN B 384  ? 0.1632 0.2484 0.1919 -0.0175 0.0035  0.0063  382  GLN B NE2 
11475 N N   . LEU B 385  ? 0.1757 0.2210 0.1945 -0.0142 -0.0022 -0.0027 383  LEU B N   
11476 C CA  . LEU B 385  ? 0.2368 0.2768 0.2561 -0.0115 -0.0024 -0.0050 383  LEU B CA  
11477 C C   . LEU B 385  ? 0.2456 0.2794 0.2629 -0.0125 -0.0043 -0.0056 383  LEU B C   
11478 O O   . LEU B 385  ? 0.2071 0.2383 0.2256 -0.0104 -0.0041 -0.0072 383  LEU B O   
11479 C CB  . LEU B 385  ? 0.2343 0.2723 0.2526 -0.0104 -0.0024 -0.0058 383  LEU B CB  
11480 C CG  . LEU B 385  ? 0.2532 0.2954 0.2733 -0.0080 -0.0004 -0.0064 383  LEU B CG  
11481 C CD1 . LEU B 385  ? 0.2846 0.3243 0.3028 -0.0075 -0.0009 -0.0070 383  LEU B CD1 
11482 C CD2 . LEU B 385  ? 0.3169 0.3593 0.3402 -0.0052 0.0008  -0.0080 383  LEU B CD2 
11483 N N   . ASP B 386  ? 0.2081 0.2392 0.2220 -0.0155 -0.0062 -0.0043 384  ASP B N   
11484 C CA  . ASP B 386  ? 0.2159 0.2400 0.2271 -0.0162 -0.0084 -0.0050 384  ASP B CA  
11485 C C   . ASP B 386  ? 0.2202 0.2442 0.2308 -0.0177 -0.0090 -0.0046 384  ASP B C   
11486 O O   . ASP B 386  ? 0.2236 0.2417 0.2316 -0.0180 -0.0107 -0.0054 384  ASP B O   
11487 C CB  . ASP B 386  ? 0.2138 0.2337 0.2210 -0.0187 -0.0106 -0.0039 384  ASP B CB  
11488 C CG  . ASP B 386  ? 0.3155 0.3333 0.3226 -0.0168 -0.0105 -0.0048 384  ASP B CG  
11489 O OD1 . ASP B 386  ? 0.3146 0.3332 0.3245 -0.0136 -0.0091 -0.0066 384  ASP B OD1 
11490 O OD2 . ASP B 386  ? 0.2969 0.3121 0.3008 -0.0186 -0.0120 -0.0037 384  ASP B OD2 
11491 N N   . GLY B 387  ? 0.2046 0.2352 0.2176 -0.0182 -0.0076 -0.0035 385  GLY B N   
11492 C CA  . GLY B 387  ? 0.1827 0.2136 0.1953 -0.0196 -0.0083 -0.0031 385  GLY B CA  
11493 C C   . GLY B 387  ? 0.2468 0.2738 0.2552 -0.0235 -0.0110 -0.0017 385  GLY B C   
11494 O O   . GLY B 387  ? 0.2207 0.2440 0.2270 -0.0242 -0.0124 -0.0023 385  GLY B O   
11495 N N   . LEU B 388  ? 0.2239 0.2517 0.2307 -0.0263 -0.0119 0.0001  386  LEU B N   
11496 C CA  . LEU B 388  ? 0.2407 0.2635 0.2430 -0.0303 -0.0149 0.0014  386  LEU B CA  
11497 C C   . LEU B 388  ? 0.2783 0.3064 0.2811 -0.0339 -0.0155 0.0037  386  LEU B C   
11498 O O   . LEU B 388  ? 0.2270 0.2633 0.2338 -0.0331 -0.0135 0.0044  386  LEU B O   
11499 C CB  . LEU B 388  ? 0.2716 0.2921 0.2716 -0.0319 -0.0159 0.0025  386  LEU B CB  
11500 C CG  . LEU B 388  ? 0.2658 0.2807 0.2653 -0.0282 -0.0157 0.0002  386  LEU B CG  
11501 C CD1 . LEU B 388  ? 0.2702 0.2815 0.2666 -0.0298 -0.0172 0.0012  386  LEU B CD1 
11502 C CD2 . LEU B 388  ? 0.2580 0.2656 0.2557 -0.0263 -0.0169 -0.0021 386  LEU B CD2 
11503 N N   . ALA B 389  ? 0.2389 0.2621 0.2375 -0.0378 -0.0184 0.0048  387  ALA B N   
11504 C CA  . ALA B 389  ? 0.2671 0.2941 0.2659 -0.0412 -0.0195 0.0066  387  ALA B CA  
11505 C C   . ALA B 389  ? 0.2531 0.2904 0.2553 -0.0435 -0.0182 0.0095  387  ALA B C   
11506 O O   . ALA B 389  ? 0.2538 0.2983 0.2590 -0.0441 -0.0175 0.0106  387  ALA B O   
11507 C CB  . ALA B 389  ? 0.2964 0.3152 0.2895 -0.0452 -0.0233 0.0072  387  ALA B CB  
11508 N N   . ASP B 390  ? 0.2663 0.3049 0.2682 -0.0444 -0.0178 0.0107  388  ASP B N   
11509 C CA  . ASP B 390  ? 0.2260 0.2746 0.2308 -0.0465 -0.0165 0.0135  388  ASP B CA  
11510 C C   . ASP B 390  ? 0.2251 0.2738 0.2294 -0.0454 -0.0152 0.0136  388  ASP B C   
11511 O O   . ASP B 390  ? 0.2079 0.2492 0.2099 -0.0431 -0.0156 0.0116  388  ASP B O   
11512 C CB  . ASP B 390  ? 0.2434 0.2933 0.2462 -0.0526 -0.0191 0.0166  388  ASP B CB  
11513 C CG  . ASP B 390  ? 0.2929 0.3553 0.3002 -0.0544 -0.0175 0.0193  388  ASP B CG  
11514 O OD1 . ASP B 390  ? 0.2500 0.3194 0.2603 -0.0520 -0.0146 0.0197  388  ASP B OD1 
11515 O OD2 . ASP B 390  ? 0.2856 0.3510 0.2932 -0.0581 -0.0192 0.0212  388  ASP B OD2 
11516 N N   . PHE B 391  ? 0.1854 0.2429 0.1918 -0.0469 -0.0137 0.0160  389  PHE B N   
11517 C CA  . PHE B 391  ? 0.2131 0.2706 0.2184 -0.0461 -0.0126 0.0163  389  PHE B CA  
11518 C C   . PHE B 391  ? 0.1991 0.2512 0.1995 -0.0510 -0.0154 0.0184  389  PHE B C   
11519 O O   . PHE B 391  ? 0.2125 0.2642 0.2114 -0.0556 -0.0176 0.0206  389  PHE B O   
11520 C CB  . PHE B 391  ? 0.2028 0.2719 0.2120 -0.0452 -0.0096 0.0177  389  PHE B CB  
11521 C CG  . PHE B 391  ? 0.1986 0.2726 0.2122 -0.0405 -0.0070 0.0158  389  PHE B CG  
11522 C CD1 . PHE B 391  ? 0.1903 0.2613 0.2045 -0.0356 -0.0054 0.0129  389  PHE B CD1 
11523 C CD2 . PHE B 391  ? 0.2143 0.2954 0.2314 -0.0409 -0.0065 0.0168  389  PHE B CD2 
11524 C CE1 . PHE B 391  ? 0.1998 0.2743 0.2177 -0.0314 -0.0033 0.0112  389  PHE B CE1 
11525 C CE2 . PHE B 391  ? 0.1950 0.2798 0.2159 -0.0364 -0.0043 0.0151  389  PHE B CE2 
11526 C CZ  . PHE B 391  ? 0.1905 0.2717 0.2116 -0.0317 -0.0027 0.0123  389  PHE B CZ  
11527 N N   . PRO B 392  ? 0.2081 0.2555 0.2057 -0.0501 -0.0155 0.0180  390  PRO B N   
11528 C CA  . PRO B 392  ? 0.2232 0.2659 0.2160 -0.0547 -0.0180 0.0204  390  PRO B CA  
11529 C C   . PRO B 392  ? 0.2156 0.2675 0.2092 -0.0578 -0.0166 0.0238  390  PRO B C   
11530 O O   . PRO B 392  ? 0.2337 0.2825 0.2233 -0.0619 -0.0184 0.0262  390  PRO B O   
11531 C CB  . PRO B 392  ? 0.2263 0.2605 0.2163 -0.0516 -0.0186 0.0182  390  PRO B CB  
11532 C CG  . PRO B 392  ? 0.2318 0.2717 0.2259 -0.0464 -0.0151 0.0160  390  PRO B CG  
11533 C CD  . PRO B 392  ? 0.2241 0.2699 0.2227 -0.0449 -0.0136 0.0152  390  PRO B CD  
11534 N N   . VAL B 393  ? 0.2239 0.2867 0.2223 -0.0557 -0.0134 0.0240  391  VAL B N   
11535 C CA  . VAL B 393  ? 0.1968 0.2701 0.1967 -0.0578 -0.0114 0.0270  391  VAL B CA  
11536 C C   . VAL B 393  ? 0.2043 0.2880 0.2092 -0.0584 -0.0100 0.0283  391  VAL B C   
11537 O O   . VAL B 393  ? 0.2202 0.3034 0.2277 -0.0559 -0.0099 0.0263  391  VAL B O   
11538 C CB  . VAL B 393  ? 0.2214 0.2980 0.2220 -0.0534 -0.0083 0.0256  391  VAL B CB  
11539 C CG1 . VAL B 393  ? 0.2071 0.2738 0.2026 -0.0530 -0.0099 0.0246  391  VAL B CG1 
11540 C CG2 . VAL B 393  ? 0.1884 0.2671 0.1930 -0.0474 -0.0060 0.0222  391  VAL B CG2 
11541 N N   . PHE B 394  ? 0.2240 0.3176 0.2303 -0.0618 -0.0090 0.0317  392  PHE B N   
11542 C CA  . PHE B 394  ? 0.2056 0.3107 0.2172 -0.0620 -0.0074 0.0331  392  PHE B CA  
11543 C C   . PHE B 394  ? 0.2202 0.3314 0.2359 -0.0554 -0.0037 0.0306  392  PHE B C   
11544 O O   . PHE B 394  ? 0.2138 0.3223 0.2282 -0.0515 -0.0021 0.0285  392  PHE B O   
11545 C CB  . PHE B 394  ? 0.2085 0.3233 0.2208 -0.0674 -0.0072 0.0377  392  PHE B CB  
11546 C CG  . PHE B 394  ? 0.2335 0.3417 0.2414 -0.0742 -0.0111 0.0403  392  PHE B CG  
11547 C CD1 . PHE B 394  ? 0.2231 0.3278 0.2310 -0.0774 -0.0141 0.0407  392  PHE B CD1 
11548 C CD2 . PHE B 394  ? 0.2182 0.3227 0.2216 -0.0774 -0.0119 0.0422  392  PHE B CD2 
11549 C CE1 . PHE B 394  ? 0.2270 0.3244 0.2304 -0.0836 -0.0180 0.0429  392  PHE B CE1 
11550 C CE2 . PHE B 394  ? 0.2541 0.3513 0.2530 -0.0836 -0.0158 0.0446  392  PHE B CE2 
11551 C CZ  . PHE B 394  ? 0.2243 0.3177 0.2231 -0.0868 -0.0189 0.0449  392  PHE B CZ  
11552 N N   . THR B 395  ? 0.2239 0.3428 0.2444 -0.0541 -0.0027 0.0308  393  THR B N   
11553 C CA  . THR B 395  ? 0.1945 0.3188 0.2189 -0.0479 0.0005  0.0286  393  THR B CA  
11554 C C   . THR B 395  ? 0.2163 0.3551 0.2449 -0.0474 0.0033  0.0309  393  THR B C   
11555 O O   . THR B 395  ? 0.2328 0.3763 0.2640 -0.0420 0.0062  0.0291  393  THR B O   
11556 C CB  . THR B 395  ? 0.2122 0.3334 0.2388 -0.0454 -0.0003 0.0263  393  THR B CB  
11557 O OG1 . THR B 395  ? 0.2309 0.3575 0.2598 -0.0492 -0.0018 0.0288  393  THR B OG1 
11558 C CG2 . THR B 395  ? 0.2108 0.3182 0.2334 -0.0450 -0.0026 0.0237  393  THR B CG2 
11559 N N   . ARG B 396  ? 0.2241 0.3701 0.2534 -0.0529 0.0026  0.0348  394  ARG B N   
11560 C CA  . ARG B 396  ? 0.1768 0.3373 0.2099 -0.0528 0.0054  0.0374  394  ARG B CA  
11561 C C   . ARG B 396  ? 0.2271 0.3889 0.2567 -0.0560 0.0060  0.0397  394  ARG B C   
11562 O O   . ARG B 396  ? 0.2053 0.3610 0.2311 -0.0616 0.0031  0.0416  394  ARG B O   
11563 C CB  . ARG B 396  ? 0.1811 0.3510 0.2184 -0.0569 0.0043  0.0407  394  ARG B CB  
11564 C CG  . ARG B 396  ? 0.2461 0.4160 0.2870 -0.0539 0.0037  0.0389  394  ARG B CG  
11565 C CD  . ARG B 396  ? 0.2415 0.4233 0.2873 -0.0573 0.0030  0.0423  394  ARG B CD  
11566 N NE  . ARG B 396  ? 0.3087 0.4889 0.3570 -0.0551 0.0019  0.0407  394  ARG B NE  
11567 C CZ  . ARG B 396  ? 0.3882 0.5786 0.4419 -0.0518 0.0036  0.0410  394  ARG B CZ  
11568 N NH1 . ARG B 396  ? 0.4448 0.6488 0.5026 -0.0503 0.0065  0.0431  394  ARG B NH1 
11569 N NH2 . ARG B 396  ? 0.3076 0.4948 0.3627 -0.0497 0.0023  0.0394  394  ARG B NH2 
11570 N N   . LYS B 397  ? 0.2150 0.3847 0.2456 -0.0524 0.0096  0.0396  395  LYS B N   
11571 C CA  . LYS B 397  ? 0.2349 0.4057 0.2617 -0.0548 0.0105  0.0415  395  LYS B CA  
11572 C C   . LYS B 397  ? 0.2233 0.4014 0.2507 -0.0623 0.0092  0.0465  395  LYS B C   
11573 O O   . LYS B 397  ? 0.2478 0.4216 0.2706 -0.0668 0.0078  0.0486  395  LYS B O   
11574 C CB  . LYS B 397  ? 0.2456 0.4245 0.2736 -0.0492 0.0148  0.0403  395  LYS B CB  
11575 C CG  . LYS B 397  ? 0.2575 0.4349 0.2804 -0.0501 0.0158  0.0411  395  LYS B CG  
11576 C CD  . LYS B 397  ? 0.2882 0.4781 0.3121 -0.0546 0.0173  0.0457  395  LYS B CD  
11577 C CE  . LYS B 397  ? 0.2795 0.4682 0.2980 -0.0552 0.0186  0.0465  395  LYS B CE  
11578 N NZ  . LYS B 397  ? 0.3003 0.5025 0.3200 -0.0593 0.0205  0.0512  395  LYS B NZ  
11579 N N   . ILE B 398  ? 0.2047 0.3937 0.2376 -0.0638 0.0095  0.0488  396  ILE B N   
11580 C CA  . ILE B 398  ? 0.2257 0.4222 0.2595 -0.0712 0.0081  0.0538  396  ILE B CA  
11581 C C   . ILE B 398  ? 0.2137 0.3980 0.2432 -0.0775 0.0033  0.0547  396  ILE B C   
11582 O O   . ILE B 398  ? 0.2300 0.4153 0.2573 -0.0843 0.0016  0.0586  396  ILE B O   
11583 C CB  . ILE B 398  ? 0.2116 0.4226 0.2527 -0.0710 0.0093  0.0557  396  ILE B CB  
11584 C CG1 . ILE B 398  ? 0.3099 0.5319 0.3527 -0.0783 0.0089  0.0612  396  ILE B CG1 
11585 C CG2 . ILE B 398  ? 0.2380 0.4433 0.2811 -0.0705 0.0066  0.0539  396  ILE B CG2 
11586 C CD1 . ILE B 398  ? 0.3446 0.5843 0.3950 -0.0770 0.0113  0.0634  396  ILE B CD1 
11587 N N   . HIS B 399  ? 0.2368 0.4090 0.2647 -0.0754 0.0010  0.0513  397  HIS B N   
11588 C CA  . HIS B 399  ? 0.2415 0.4008 0.2646 -0.0805 -0.0036 0.0516  397  HIS B CA  
11589 C C   . HIS B 399  ? 0.2535 0.4040 0.2702 -0.0823 -0.0043 0.0520  397  HIS B C   
11590 O O   . HIS B 399  ? 0.2798 0.4254 0.2927 -0.0888 -0.0074 0.0548  397  HIS B O   
11591 C CB  . HIS B 399  ? 0.2311 0.3799 0.2537 -0.0770 -0.0053 0.0476  397  HIS B CB  
11592 C CG  . HIS B 399  ? 0.2396 0.3952 0.2674 -0.0765 -0.0055 0.0477  397  HIS B CG  
11593 N ND1 . HIS B 399  ? 0.2323 0.3813 0.2607 -0.0728 -0.0064 0.0443  397  HIS B ND1 
11594 C CD2 . HIS B 399  ? 0.2575 0.4264 0.2904 -0.0793 -0.0050 0.0511  397  HIS B CD2 
11595 C CE1 . HIS B 399  ? 0.2561 0.4137 0.2894 -0.0732 -0.0065 0.0455  397  HIS B CE1 
11596 N NE2 . HIS B 399  ? 0.2123 0.3821 0.2485 -0.0771 -0.0058 0.0495  397  HIS B NE2 
11597 N N   . THR B 400  ? 0.2330 0.3808 0.2482 -0.0767 -0.0018 0.0491  398  THR B N   
11598 C CA  . THR B 400  ? 0.2530 0.3933 0.2622 -0.0781 -0.0025 0.0495  398  THR B CA  
11599 C C   . THR B 400  ? 0.2361 0.3852 0.2444 -0.0836 -0.0018 0.0544  398  THR B C   
11600 O O   . THR B 400  ? 0.2563 0.3985 0.2594 -0.0887 -0.0043 0.0566  398  THR B O   
11601 C CB  . THR B 400  ? 0.2107 0.3486 0.2190 -0.0710 0.0003  0.0457  398  THR B CB  
11602 O OG1 . THR B 400  ? 0.2029 0.3306 0.2110 -0.0669 -0.0010 0.0415  398  THR B OG1 
11603 C CG2 . THR B 400  ? 0.2097 0.3422 0.2121 -0.0724 0.0001  0.0465  398  THR B CG2 
11604 N N   . ASP B 401  ? 0.2342 0.3988 0.2476 -0.0828 0.0017  0.0562  399  ASP B N   
11605 C CA  . ASP B 401  ? 0.2463 0.4212 0.2596 -0.0881 0.0027  0.0612  399  ASP B CA  
11606 C C   . ASP B 401  ? 0.2726 0.4458 0.2851 -0.0967 -0.0013 0.0652  399  ASP B C   
11607 O O   . ASP B 401  ? 0.2436 0.4149 0.2519 -0.1025 -0.0027 0.0687  399  ASP B O   
11608 C CB  . ASP B 401  ? 0.2633 0.4559 0.2830 -0.0850 0.0072  0.0622  399  ASP B CB  
11609 C CG  . ASP B 401  ? 0.3049 0.4994 0.3242 -0.0772 0.0112  0.0588  399  ASP B CG  
11610 O OD1 . ASP B 401  ? 0.3031 0.4875 0.3167 -0.0758 0.0108  0.0570  399  ASP B OD1 
11611 O OD2 . ASP B 401  ? 0.2681 0.4737 0.2926 -0.0724 0.0146  0.0579  399  ASP B OD2 
11612 N N   . VAL B 402  ? 0.2446 0.4182 0.2606 -0.0978 -0.0033 0.0649  400  VAL B N   
11613 C CA  . VAL B 402  ? 0.2886 0.4596 0.3035 -0.1060 -0.0076 0.0685  400  VAL B CA  
11614 C C   . VAL B 402  ? 0.2585 0.4117 0.2655 -0.1089 -0.0116 0.0677  400  VAL B C   
11615 O O   . VAL B 402  ? 0.2623 0.4126 0.2656 -0.1161 -0.0143 0.0715  400  VAL B O   
11616 C CB  . VAL B 402  ? 0.2961 0.4698 0.3158 -0.1059 -0.0091 0.0677  400  VAL B CB  
11617 C CG1 . VAL B 402  ? 0.2599 0.4282 0.2772 -0.1144 -0.0141 0.0708  400  VAL B CG1 
11618 C CG2 . VAL B 402  ? 0.3086 0.5010 0.3362 -0.1036 -0.0053 0.0691  400  VAL B CG2 
11619 N N   . SER B 403  ? 0.2289 0.3700 0.2334 -0.1033 -0.0121 0.0629  401  SER B N   
11620 C CA  . SER B 403  ? 0.2674 0.3916 0.2647 -0.1051 -0.0158 0.0618  401  SER B CA  
11621 C C   . SER B 403  ? 0.2761 0.3992 0.2686 -0.1078 -0.0155 0.0645  401  SER B C   
11622 O O   . SER B 403  ? 0.2567 0.3711 0.2439 -0.1137 -0.0191 0.0669  401  SER B O   
11623 C CB  . SER B 403  ? 0.2160 0.3302 0.2124 -0.0978 -0.0156 0.0562  401  SER B CB  
11624 O OG  . SER B 403  ? 0.2549 0.3538 0.2445 -0.0985 -0.0186 0.0550  401  SER B OG  
11625 N N   . TYR B 404  ? 0.2444 0.3763 0.2386 -0.1038 -0.0112 0.0641  402  TYR B N   
11626 C CA  . TYR B 404  ? 0.2683 0.3997 0.2578 -0.1060 -0.0105 0.0665  402  TYR B CA  
11627 C C   . TYR B 404  ? 0.2508 0.3881 0.2393 -0.1148 -0.0120 0.0725  402  TYR B C   
11628 O O   . TYR B 404  ? 0.3012 0.4298 0.2836 -0.1198 -0.0149 0.0750  402  TYR B O   
11629 C CB  . TYR B 404  ? 0.2470 0.3888 0.2389 -0.1000 -0.0053 0.0652  402  TYR B CB  
11630 C CG  . TYR B 404  ? 0.2751 0.4145 0.2614 -0.1005 -0.0044 0.0664  402  TYR B CG  
11631 C CD1 . TYR B 404  ? 0.2803 0.4271 0.2649 -0.1066 -0.0039 0.0716  402  TYR B CD1 
11632 C CD2 . TYR B 404  ? 0.2632 0.3935 0.2460 -0.0949 -0.0039 0.0625  402  TYR B CD2 
11633 C CE1 . TYR B 404  ? 0.2977 0.4424 0.2767 -0.1070 -0.0030 0.0729  402  TYR B CE1 
11634 C CE2 . TYR B 404  ? 0.2674 0.3954 0.2447 -0.0953 -0.0033 0.0636  402  TYR B CE2 
11635 C CZ  . TYR B 404  ? 0.3059 0.4411 0.2813 -0.1013 -0.0028 0.0688  402  TYR B CZ  
11636 O OH  . TYR B 404  ? 0.2859 0.4190 0.2555 -0.1017 -0.0021 0.0701  402  TYR B OH  
11637 N N   . ILE B 405  ? 0.2733 0.4253 0.2680 -0.1169 -0.0102 0.0751  403  ILE B N   
11638 C CA  . ILE B 405  ? 0.2684 0.4280 0.2631 -0.1255 -0.0114 0.0812  403  ILE B CA  
11639 C C   . ILE B 405  ? 0.2921 0.4392 0.2826 -0.1324 -0.0173 0.0828  403  ILE B C   
11640 O O   . ILE B 405  ? 0.3013 0.4453 0.2873 -0.1395 -0.0197 0.0871  403  ILE B O   
11641 C CB  . ILE B 405  ? 0.3164 0.4952 0.3194 -0.1257 -0.0082 0.0833  403  ILE B CB  
11642 C CG1 . ILE B 405  ? 0.3136 0.5041 0.3197 -0.1188 -0.0024 0.0818  403  ILE B CG1 
11643 C CG2 . ILE B 405  ? 0.3290 0.5162 0.3327 -0.1350 -0.0097 0.0897  403  ILE B CG2 
11644 C CD1 . ILE B 405  ? 0.3780 0.5862 0.3927 -0.1165 0.0010  0.0825  403  ILE B CD1 
11645 N N   . ALA B 406  ? 0.2945 0.4337 0.2860 -0.1305 -0.0198 0.0795  404  ALA B N   
11646 C CA  . ALA B 406  ? 0.2792 0.4051 0.2661 -0.1363 -0.0255 0.0804  404  ALA B CA  
11647 C C   . ALA B 406  ? 0.3088 0.4182 0.2872 -0.1370 -0.0283 0.0798  404  ALA B C   
11648 O O   . ALA B 406  ? 0.3272 0.4288 0.3004 -0.1441 -0.0323 0.0831  404  ALA B O   
11649 C CB  . ALA B 406  ? 0.3071 0.4274 0.2962 -0.1327 -0.0271 0.0763  404  ALA B CB  
11650 N N   . CYS B 407  ? 0.2820 0.3856 0.2587 -0.1297 -0.0263 0.0756  405  CYS B N   
11651 C CA  . CYS B 407  ? 0.2961 0.3843 0.2651 -0.1297 -0.0289 0.0747  405  CYS B CA  
11652 C C   . CYS B 407  ? 0.3152 0.4067 0.2804 -0.1345 -0.0284 0.0794  405  CYS B C   
11653 O O   . CYS B 407  ? 0.3225 0.4018 0.2807 -0.1382 -0.0320 0.0809  405  CYS B O   
11654 C CB  . CYS B 407  ? 0.3029 0.3853 0.2718 -0.1207 -0.0270 0.0691  405  CYS B CB  
11655 S SG  . CYS B 407  ? 0.3477 0.4215 0.3187 -0.1161 -0.0289 0.0638  405  CYS B SG  
11656 N N   . ALA B 408  ? 0.2998 0.4077 0.2694 -0.1343 -0.0239 0.0817  406  ALA B N   
11657 C CA  . ALA B 408  ? 0.3297 0.4424 0.2960 -0.1395 -0.0232 0.0867  406  ALA B CA  
11658 C C   . ALA B 408  ? 0.2975 0.4088 0.2615 -0.1496 -0.0273 0.0921  406  ALA B C   
11659 O O   . ALA B 408  ? 0.3739 0.4786 0.3316 -0.1548 -0.0296 0.0955  406  ALA B O   
11660 C CB  . ALA B 408  ? 0.3454 0.4772 0.3174 -0.1369 -0.0173 0.0878  406  ALA B CB  
11661 N N   . ALA B 409  ? 0.3418 0.4590 0.3108 -0.1526 -0.0284 0.0930  407  ALA B N   
11662 C CA  . ALA B 409  ? 0.3796 0.4942 0.3463 -0.1623 -0.0328 0.0979  407  ALA B CA  
11663 C C   . ALA B 409  ? 0.3571 0.4503 0.3151 -0.1647 -0.0385 0.0970  407  ALA B C   
11664 O O   . ALA B 409  ? 0.3722 0.4596 0.3247 -0.1722 -0.0419 0.1015  407  ALA B O   
11665 C CB  . ALA B 409  ? 0.3450 0.4676 0.3183 -0.1642 -0.0336 0.0981  407  ALA B CB  
11666 N N   . LYS B 410  ? 0.3213 0.4025 0.2779 -0.1582 -0.0397 0.0913  408  LYS B N   
11667 C CA  . LYS B 410  ? 0.3664 0.4273 0.3151 -0.1593 -0.0449 0.0899  408  LYS B CA  
11668 C C   . LYS B 410  ? 0.4035 0.4570 0.3454 -0.1597 -0.0453 0.0914  408  LYS B C   
11669 O O   . LYS B 410  ? 0.3782 0.4195 0.3130 -0.1653 -0.0499 0.0940  408  LYS B O   
11670 C CB  . LYS B 410  ? 0.3691 0.4214 0.3187 -0.1513 -0.0451 0.0833  408  LYS B CB  
11671 C CG  . LYS B 410  ? 0.3752 0.4070 0.3171 -0.1506 -0.0499 0.0809  408  LYS B CG  
11672 C CD  . LYS B 410  ? 0.4138 0.4400 0.3578 -0.1424 -0.0492 0.0746  408  LYS B CD  
11673 C CE  . LYS B 410  ? 0.4066 0.4366 0.3550 -0.1434 -0.0501 0.0735  408  LYS B CE  
11674 N NZ  . LYS B 410  ? 0.4019 0.4201 0.3446 -0.1503 -0.0560 0.0754  408  LYS B NZ  
11675 N N   . LEU B 411  ? 0.3666 0.4275 0.3104 -0.1539 -0.0406 0.0899  409  LEU B N   
11676 C CA  . LEU B 411  ? 0.3282 0.3831 0.2658 -0.1538 -0.0407 0.0912  409  LEU B CA  
11677 C C   . LEU B 411  ? 0.3618 0.4217 0.2964 -0.1628 -0.0415 0.0980  409  LEU B C   
11678 O O   . LEU B 411  ? 0.3802 0.4282 0.3072 -0.1669 -0.0452 0.1005  409  LEU B O   
11679 C CB  . LEU B 411  ? 0.3447 0.4080 0.2854 -0.1459 -0.0353 0.0881  409  LEU B CB  
11680 C CG  . LEU B 411  ? 0.3830 0.4361 0.3236 -0.1375 -0.0356 0.0816  409  LEU B CG  
11681 C CD1 . LEU B 411  ? 0.3595 0.4222 0.3042 -0.1298 -0.0302 0.0785  409  LEU B CD1 
11682 C CD2 . LEU B 411  ? 0.3379 0.3730 0.2701 -0.1379 -0.0399 0.0812  409  LEU B CD2 
11683 N N   . LEU B 412  ? 0.4079 0.4858 0.3487 -0.1658 -0.0381 0.1013  410  LEU B N   
11684 C CA  . LEU B 412  ? 0.3874 0.4727 0.3263 -0.1744 -0.0383 0.1081  410  LEU B CA  
11685 C C   . LEU B 412  ? 0.4053 0.4795 0.3393 -0.1826 -0.0446 0.1113  410  LEU B C   
11686 O O   . LEU B 412  ? 0.4353 0.5097 0.3657 -0.1872 -0.0463 0.1150  410  LEU B O   
11687 C CB  . LEU B 412  ? 0.3998 0.5074 0.3474 -0.1750 -0.0334 0.1103  410  LEU B CB  
11688 C CG  . LEU B 412  ? 0.4008 0.5200 0.3518 -0.1673 -0.0271 0.1079  410  LEU B CG  
11689 C CD1 . LEU B 412  ? 0.3979 0.5381 0.3581 -0.1664 -0.0224 0.1090  410  LEU B CD1 
11690 C CD2 . LEU B 412  ? 0.3729 0.4917 0.3177 -0.1693 -0.0260 0.1112  410  LEU B CD2 
11691 N N   . ALA B 413  ? 0.4016 0.4656 0.3355 -0.1831 -0.0483 0.1089  411  ALA B N   
11692 C CA  . ALA B 413  ? 0.4371 0.4882 0.3654 -0.1886 -0.0548 0.1103  411  ALA B CA  
11693 C C   . ALA B 413  ? 0.4626 0.4927 0.3813 -0.1890 -0.0591 0.1097  411  ALA B C   
11694 O O   . ALA B 413  ? 0.4472 0.4647 0.3600 -0.1931 -0.0648 0.1106  411  ALA B O   
11695 C CB  . ALA B 413  ? 0.3969 0.4464 0.3287 -0.1888 -0.0571 0.1080  411  ALA B CB  
11696 N N   . ALA B 414  ? 0.3643 0.3903 0.2810 -0.1831 -0.0568 0.1072  412  ALA B N   
11697 C CA  . ALA B 414  ? 0.4593 0.4653 0.3675 -0.1811 -0.0609 0.1052  412  ALA B CA  
11698 C C   . ALA B 414  ? 0.4396 0.4456 0.3435 -0.1796 -0.0590 0.1069  412  ALA B C   
11699 O O   . ALA B 414  ? 0.4040 0.3970 0.3030 -0.1747 -0.0606 0.1038  412  ALA B O   
11700 C CB  . ALA B 414  ? 0.3742 0.3715 0.2837 -0.1722 -0.0612 0.0981  412  ALA B CB  
11701 N N   . THR B 415  ? 0.4275 0.4480 0.3333 -0.1840 -0.0558 0.1118  413  THR B N   
11702 C CA  . THR B 415  ? 0.4389 0.4616 0.3413 -0.1819 -0.0532 0.1130  413  THR B CA  
11703 C C   . THR B 415  ? 0.4685 0.4741 0.3606 -0.1857 -0.0582 0.1156  413  THR B C   
11704 O O   . THR B 415  ? 0.4634 0.4670 0.3516 -0.1827 -0.0569 0.1156  413  THR B O   
11705 C CB  . THR B 415  ? 0.4007 0.4434 0.3074 -0.1850 -0.0485 0.1172  413  THR B CB  
11706 O OG1 . THR B 415  ? 0.4339 0.4793 0.3410 -0.1914 -0.0515 0.1203  413  THR B OG1 
11707 C CG2 . THR B 415  ? 0.3342 0.3936 0.2505 -0.1798 -0.0428 0.1143  413  THR B CG2 
11708 N N   . ASP B 416  ? 0.4577 0.4514 0.3458 -0.1905 -0.0640 0.1166  414  ASP B N   
11709 C CA  . ASP B 416  ? 0.4471 0.4230 0.3256 -0.1921 -0.0692 0.1177  414  ASP B CA  
11710 C C   . ASP B 416  ? 0.4715 0.4331 0.3461 -0.1855 -0.0702 0.1136  414  ASP B C   
11711 O O   . ASP B 416  ? 0.5210 0.4732 0.3890 -0.1842 -0.0717 0.1143  414  ASP B O   
11712 C CB  . ASP B 416  ? 0.5143 0.4796 0.3892 -0.1973 -0.0754 0.1185  414  ASP B CB  
11713 C CG  . ASP B 416  ? 0.5908 0.5657 0.4661 -0.2040 -0.0760 0.1231  414  ASP B CG  
11714 O OD1 . ASP B 416  ? 0.5784 0.5672 0.4562 -0.2047 -0.0718 0.1258  414  ASP B OD1 
11715 O OD2 . ASP B 416  ? 0.5889 0.5572 0.4617 -0.2086 -0.0808 0.1241  414  ASP B OD2 
11716 N N   . VAL B 417  ? 0.4482 0.4094 0.3280 -0.1789 -0.0693 0.1077  415  VAL B N   
11717 C CA  . VAL B 417  ? 0.4808 0.4291 0.3585 -0.1704 -0.0706 0.1019  415  VAL B CA  
11718 C C   . VAL B 417  ? 0.4374 0.3962 0.3219 -0.1613 -0.0651 0.0969  415  VAL B C   
11719 O O   . VAL B 417  ? 0.4912 0.4410 0.3741 -0.1541 -0.0657 0.0924  415  VAL B O   
11720 C CB  . VAL B 417  ? 0.4993 0.4336 0.3753 -0.1700 -0.0753 0.0989  415  VAL B CB  
11721 C CG1 . VAL B 417  ? 0.4701 0.3921 0.3382 -0.1791 -0.0813 0.1038  415  VAL B CG1 
11722 C CG2 . VAL B 417  ? 0.4338 0.3790 0.3181 -0.1687 -0.0727 0.0964  415  VAL B CG2 
11723 N N   . VAL B 418  ? 0.4512 0.4284 0.3431 -0.1611 -0.0598 0.0975  416  VAL B N   
11724 C CA  . VAL B 418  ? 0.4091 0.3959 0.3065 -0.1527 -0.0546 0.0931  416  VAL B CA  
11725 C C   . VAL B 418  ? 0.4480 0.4517 0.3479 -0.1546 -0.0497 0.0966  416  VAL B C   
11726 O O   . VAL B 418  ? 0.4367 0.4493 0.3375 -0.1618 -0.0492 0.1016  416  VAL B O   
11727 C CB  . VAL B 418  ? 0.4059 0.3979 0.3110 -0.1475 -0.0526 0.0882  416  VAL B CB  
11728 C CG1 . VAL B 418  ? 0.4391 0.4147 0.3417 -0.1443 -0.0569 0.0841  416  VAL B CG1 
11729 C CG2 . VAL B 418  ? 0.3924 0.3973 0.3030 -0.1531 -0.0512 0.0912  416  VAL B CG2 
11730 N N   . PHE B 419  ? 0.3900 0.3981 0.2909 -0.1479 -0.0461 0.0938  417  PHE B N   
11731 C CA  . PHE B 419  ? 0.4334 0.4577 0.3367 -0.1479 -0.0409 0.0960  417  PHE B CA  
11732 C C   . PHE B 419  ? 0.4050 0.4422 0.3171 -0.1416 -0.0359 0.0918  417  PHE B C   
11733 O O   . PHE B 419  ? 0.3631 0.3980 0.2766 -0.1338 -0.0344 0.0867  417  PHE B O   
11734 C CB  . PHE B 419  ? 0.3964 0.4162 0.2937 -0.1452 -0.0405 0.0960  417  PHE B CB  
11735 C CG  . PHE B 419  ? 0.3786 0.4142 0.2775 -0.1445 -0.0350 0.0978  417  PHE B CG  
11736 C CD1 . PHE B 419  ? 0.4099 0.4567 0.3088 -0.1517 -0.0334 0.1037  417  PHE B CD1 
11737 C CD2 . PHE B 419  ? 0.3894 0.4285 0.2895 -0.1367 -0.0316 0.0936  417  PHE B CD2 
11738 C CE1 . PHE B 419  ? 0.4289 0.4905 0.3291 -0.1507 -0.0281 0.1053  417  PHE B CE1 
11739 C CE2 . PHE B 419  ? 0.3868 0.4399 0.2878 -0.1358 -0.0266 0.0951  417  PHE B CE2 
11740 C CZ  . PHE B 419  ? 0.3939 0.4584 0.2949 -0.1426 -0.0247 0.1008  417  PHE B CZ  
11741 N N   . PRO B 420  ? 0.3999 0.4505 0.3181 -0.1447 -0.0335 0.0937  418  PRO B N   
11742 C CA  . PRO B 420  ? 0.3684 0.4303 0.2948 -0.1386 -0.0293 0.0897  418  PRO B CA  
11743 C C   . PRO B 420  ? 0.3809 0.4547 0.3090 -0.1338 -0.0238 0.0888  418  PRO B C   
11744 O O   . PRO B 420  ? 0.3798 0.4624 0.3060 -0.1376 -0.0217 0.0931  418  PRO B O   
11745 C CB  . PRO B 420  ? 0.3333 0.4058 0.2649 -0.1445 -0.0290 0.0930  418  PRO B CB  
11746 C CG  . PRO B 420  ? 0.3331 0.3952 0.2588 -0.1532 -0.0344 0.0976  418  PRO B CG  
11747 C CD  . PRO B 420  ? 0.3404 0.3948 0.2582 -0.1541 -0.0354 0.0995  418  PRO B CD  
11748 N N   . GLN B 421  ? 0.3260 0.4002 0.2575 -0.1255 -0.0215 0.0832  419  GLN B N   
11749 C CA  . GLN B 421  ? 0.3590 0.4426 0.2918 -0.1199 -0.0166 0.0813  419  GLN B CA  
11750 C C   . GLN B 421  ? 0.3175 0.4122 0.2587 -0.1148 -0.0129 0.0779  419  GLN B C   
11751 O O   . GLN B 421  ? 0.3085 0.3972 0.2523 -0.1094 -0.0135 0.0731  419  GLN B O   
11752 C CB  . GLN B 421  ? 0.3020 0.3740 0.2300 -0.1144 -0.0178 0.0776  419  GLN B CB  
11753 C CG  . GLN B 421  ? 0.3420 0.4030 0.2615 -0.1190 -0.0216 0.0810  419  GLN B CG  
11754 C CD  . GLN B 421  ? 0.3680 0.4154 0.2832 -0.1138 -0.0240 0.0771  419  GLN B CD  
11755 O OE1 . GLN B 421  ? 0.3667 0.4118 0.2764 -0.1132 -0.0239 0.0780  419  GLN B OE1 
11756 N NE2 . GLN B 421  ? 0.2917 0.3303 0.2093 -0.1103 -0.0263 0.0730  419  GLN B NE2 
11757 N N   . PHE B 422  ? 0.3119 0.4228 0.2574 -0.1165 -0.0090 0.0806  420  PHE B N   
11758 C CA  . PHE B 422  ? 0.2856 0.4073 0.2392 -0.1125 -0.0058 0.0781  420  PHE B CA  
11759 C C   . PHE B 422  ? 0.2995 0.4274 0.2546 -0.1045 -0.0013 0.0743  420  PHE B C   
11760 O O   . PHE B 422  ? 0.2930 0.4331 0.2484 -0.1042 0.0027  0.0761  420  PHE B O   
11761 C CB  . PHE B 422  ? 0.2866 0.4225 0.2445 -0.1185 -0.0044 0.0830  420  PHE B CB  
11762 C CG  . PHE B 422  ? 0.3278 0.4569 0.2840 -0.1266 -0.0092 0.0867  420  PHE B CG  
11763 C CD1 . PHE B 422  ? 0.3469 0.4671 0.3050 -0.1262 -0.0126 0.0842  420  PHE B CD1 
11764 C CD2 . PHE B 422  ? 0.3464 0.4773 0.2985 -0.1345 -0.0105 0.0926  420  PHE B CD2 
11765 C CE1 . PHE B 422  ? 0.3835 0.4966 0.3395 -0.1336 -0.0173 0.0873  420  PHE B CE1 
11766 C CE2 . PHE B 422  ? 0.3931 0.5168 0.3433 -0.1422 -0.0153 0.0960  420  PHE B CE2 
11767 C CZ  . PHE B 422  ? 0.3556 0.4701 0.3076 -0.1416 -0.0188 0.0932  420  PHE B CZ  
11768 N N   . ALA B 423  ? 0.2764 0.3959 0.2323 -0.0981 -0.0019 0.0688  421  ALA B N   
11769 C CA  . ALA B 423  ? 0.2960 0.4195 0.2533 -0.0902 0.0018  0.0646  421  ALA B CA  
11770 C C   . ALA B 423  ? 0.3088 0.4440 0.2740 -0.0867 0.0051  0.0629  421  ALA B C   
11771 O O   . ALA B 423  ? 0.3041 0.4356 0.2733 -0.0852 0.0036  0.0605  421  ALA B O   
11772 C CB  . ALA B 423  ? 0.2478 0.3571 0.2026 -0.0853 -0.0006 0.0598  421  ALA B CB  
11773 N N   . THR B 424  ? 0.3265 0.4758 0.2937 -0.0851 0.0097  0.0640  422  THR B N   
11774 C CA  . THR B 424  ? 0.3082 0.4689 0.2825 -0.0807 0.0131  0.0622  422  THR B CA  
11775 C C   . THR B 424  ? 0.2957 0.4688 0.2699 -0.0772 0.0181  0.0624  422  THR B C   
11776 O O   . THR B 424  ? 0.3062 0.4834 0.2762 -0.0807 0.0192  0.0659  422  THR B O   
11777 C CB  . THR B 424  ? 0.3027 0.4714 0.2827 -0.0858 0.0124  0.0655  422  THR B CB  
11778 O OG1 . THR B 424  ? 0.2631 0.4429 0.2500 -0.0809 0.0157  0.0636  422  THR B OG1 
11779 C CG2 . THR B 424  ? 0.2998 0.4776 0.2783 -0.0930 0.0130  0.0717  422  THR B CG2 
11780 N N   . HIS B 425  ? 0.3082 0.4867 0.2866 -0.0703 0.0212  0.0585  423  HIS B N   
11781 C CA  . HIS B 425  ? 0.2939 0.4857 0.2732 -0.0662 0.0263  0.0585  423  HIS B CA  
11782 C C   . HIS B 425  ? 0.3623 0.5695 0.3492 -0.0665 0.0289  0.0605  423  HIS B C   
11783 O O   . HIS B 425  ? 0.3595 0.5788 0.3483 -0.0623 0.0333  0.0601  423  HIS B O   
11784 C CB  . HIS B 425  ? 0.2805 0.4679 0.2589 -0.0577 0.0280  0.0527  423  HIS B CB  
11785 C CG  . HIS B 425  ? 0.3521 0.5263 0.3232 -0.0568 0.0259  0.0507  423  HIS B CG  
11786 N ND1 . HIS B 425  ? 0.3924 0.5562 0.3625 -0.0512 0.0248  0.0455  423  HIS B ND1 
11787 C CD2 . HIS B 425  ? 0.3425 0.5122 0.3069 -0.0609 0.0245  0.0533  423  HIS B CD2 
11788 C CE1 . HIS B 425  ? 0.3599 0.5139 0.3234 -0.0518 0.0229  0.0449  423  HIS B CE1 
11789 N NE2 . HIS B 425  ? 0.3422 0.4992 0.3019 -0.0575 0.0226  0.0496  423  HIS B NE2 
11790 N N   . ASN B 426  ? 0.3206 0.5277 0.3118 -0.0711 0.0262  0.0625  424  ASN B N   
11791 C CA  . ASN B 426  ? 0.3156 0.5364 0.3145 -0.0713 0.0280  0.0642  424  ASN B CA  
11792 C C   . ASN B 426  ? 0.2811 0.5140 0.2808 -0.0784 0.0289  0.0704  424  ASN B C   
11793 O O   . ASN B 426  ? 0.2845 0.5120 0.2820 -0.0860 0.0253  0.0740  424  ASN B O   
11794 C CB  . ASN B 426  ? 0.2692 0.4829 0.2721 -0.0723 0.0245  0.0628  424  ASN B CB  
11795 C CG  . ASN B 426  ? 0.3070 0.5338 0.3180 -0.0714 0.0261  0.0637  424  ASN B CG  
11796 O OD1 . ASN B 426  ? 0.2995 0.5409 0.3136 -0.0743 0.0284  0.0678  424  ASN B OD1 
11797 N ND2 . ASN B 426  ? 0.3025 0.5246 0.3171 -0.0675 0.0250  0.0602  424  ASN B ND2 
11798 N N   . ALA B 427  ? 0.3501 0.5993 0.3529 -0.0760 0.0336  0.0719  425  ALA B N   
11799 C CA  . ALA B 427  ? 0.3764 0.6387 0.3799 -0.0825 0.0350  0.0780  425  ALA B CA  
11800 C C   . ALA B 427  ? 0.2973 0.5642 0.3063 -0.0895 0.0323  0.0819  425  ALA B C   
11801 O O   . ALA B 427  ? 0.2568 0.5266 0.2646 -0.0971 0.0307  0.0869  425  ALA B O   
11802 C CB  . ALA B 427  ? 0.3763 0.6560 0.3827 -0.0776 0.0410  0.0783  425  ALA B CB  
11803 N N   . GLN B 428  ? 0.2880 0.5542 0.3027 -0.0867 0.0311  0.0794  426  GLN B N   
11804 C CA  . GLN B 428  ? 0.3271 0.5966 0.3467 -0.0932 0.0280  0.0828  426  GLN B CA  
11805 C C   . GLN B 428  ? 0.3241 0.5773 0.3386 -0.0999 0.0224  0.0838  426  GLN B C   
11806 O O   . GLN B 428  ? 0.3041 0.5596 0.3185 -0.1083 0.0200  0.0888  426  GLN B O   
11807 C CB  . GLN B 428  ? 0.3068 0.5794 0.3334 -0.0881 0.0282  0.0797  426  GLN B CB  
11808 C CG  . GLN B 428  ? 0.3541 0.6333 0.3867 -0.0932 0.0256  0.0829  426  GLN B CG  
11809 C CD  . GLN B 428  ? 0.3466 0.6135 0.3768 -0.1008 0.0202  0.0844  426  GLN B CD  
11810 O OE1 . GLN B 428  ? 0.3811 0.6316 0.4069 -0.0985 0.0176  0.0805  426  GLN B OE1 
11811 N NE2 . GLN B 428  ? 0.3317 0.6011 0.3631 -0.1074 0.0170  0.0883  426  GLN B NE2 
11812 N N   . THR B 429  ? 0.3153 0.5517 0.3252 -0.0962 0.0202  0.0792  427  THR B N   
11813 C CA  . THR B 429  ? 0.3469 0.5669 0.3512 -0.1016 0.0150  0.0797  427  THR B CA  
11814 C C   . THR B 429  ? 0.3042 0.5237 0.3027 -0.1081 0.0144  0.0844  427  THR B C   
11815 O O   . THR B 429  ? 0.2924 0.5076 0.2890 -0.1161 0.0105  0.0882  427  THR B O   
11816 C CB  . THR B 429  ? 0.2929 0.4969 0.2932 -0.0955 0.0137  0.0740  427  THR B CB  
11817 O OG1 . THR B 429  ? 0.3054 0.5117 0.3111 -0.0887 0.0152  0.0697  427  THR B OG1 
11818 C CG2 . THR B 429  ? 0.3127 0.5002 0.3087 -0.1002 0.0081  0.0740  427  THR B CG2 
11819 N N   . LEU B 430  ? 0.3312 0.5546 0.3263 -0.1049 0.0179  0.0840  428  LEU B N   
11820 C CA  . LEU B 430  ? 0.3275 0.5509 0.3167 -0.1106 0.0177  0.0885  428  LEU B CA  
11821 C C   . LEU B 430  ? 0.3271 0.5636 0.3197 -0.1188 0.0177  0.0949  428  LEU B C   
11822 O O   . LEU B 430  ? 0.3146 0.5449 0.3033 -0.1266 0.0140  0.0989  428  LEU B O   
11823 C CB  . LEU B 430  ? 0.3437 0.5727 0.3298 -0.1050 0.0224  0.0870  428  LEU B CB  
11824 C CG  . LEU B 430  ? 0.3313 0.5575 0.3095 -0.1084 0.0226  0.0899  428  LEU B CG  
11825 C CD1 . LEU B 430  ? 0.3833 0.6137 0.3592 -0.1007 0.0272  0.0866  428  LEU B CD1 
11826 C CD2 . LEU B 430  ? 0.3764 0.6145 0.3551 -0.1168 0.0232  0.0970  428  LEU B CD2 
11827 N N   . ALA B 431  ? 0.3076 0.5596 0.3074 -0.1156 0.0209  0.0949  429  ALA B N   
11828 C CA  . ALA B 431  ? 0.3185 0.5800 0.3217 -0.1201 0.0198  0.0989  429  ALA B CA  
11829 C C   . ALA B 431  ? 0.3470 0.6018 0.3514 -0.1273 0.0143  0.1011  429  ALA B C   
11830 O O   . ALA B 431  ? 0.3670 0.6214 0.3694 -0.1341 0.0113  0.1052  429  ALA B O   
11831 C CB  . ALA B 431  ? 0.3259 0.6037 0.3367 -0.1141 0.0238  0.0977  429  ALA B CB  
11832 N N   . ALA B 432  ? 0.3467 0.5958 0.3538 -0.1258 0.0126  0.0984  430  ALA B N   
11833 C CA  . ALA B 432  ? 0.2988 0.5406 0.3065 -0.1321 0.0072  0.1000  430  ALA B CA  
11834 C C   . ALA B 432  ? 0.3392 0.5658 0.3387 -0.1390 0.0029  0.1022  430  ALA B C   
11835 O O   . ALA B 432  ? 0.3488 0.5716 0.3470 -0.1458 -0.0015 0.1053  430  ALA B O   
11836 C CB  . ALA B 432  ? 0.3118 0.5493 0.3232 -0.1287 0.0066  0.0963  430  ALA B CB  
11837 N N   . ILE B 433  ? 0.3478 0.5650 0.3412 -0.1372 0.0038  0.1008  431  ILE B N   
11838 C CA  . ILE B 433  ? 0.3956 0.5974 0.3807 -0.1433 -0.0005 0.1028  431  ILE B CA  
11839 C C   . ILE B 433  ? 0.3398 0.5456 0.3212 -0.1473 -0.0005 0.1068  431  ILE B C   
11840 O O   . ILE B 433  ? 0.3469 0.5447 0.3242 -0.1542 -0.0050 0.1100  431  ILE B O   
11841 C CB  . ILE B 433  ? 0.3668 0.5529 0.3465 -0.1366 -0.0012 0.0973  431  ILE B CB  
11842 C CG1 . ILE B 433  ? 0.4164 0.5947 0.3993 -0.1315 -0.0030 0.0920  431  ILE B CG1 
11843 C CG2 . ILE B 433  ? 0.3538 0.5241 0.3246 -0.1417 -0.0056 0.0992  431  ILE B CG2 
11844 C CD1 . ILE B 433  ? 0.3928 0.5572 0.3715 -0.1248 -0.0035 0.0866  431  ILE B CD1 
11845 N N   . TYR B 434  ? 0.3344 0.5521 0.3171 -0.1428 0.0045  0.1067  432  TYR B N   
11846 C CA  . TYR B 434  ? 0.3445 0.5681 0.3246 -0.1462 0.0051  0.1104  432  TYR B CA  
11847 C C   . TYR B 434  ? 0.3927 0.6211 0.3757 -0.1528 0.0019  0.1143  432  TYR B C   
11848 O O   . TYR B 434  ? 0.3781 0.6006 0.3561 -0.1594 -0.0015 0.1179  432  TYR B O   
11849 C CB  . TYR B 434  ? 0.3774 0.6157 0.3604 -0.1394 0.0114  0.1091  432  TYR B CB  
11850 C CG  . TYR B 434  ? 0.3672 0.6151 0.3493 -0.1421 0.0128  0.1128  432  TYR B CG  
11851 C CD1 . TYR B 434  ? 0.4313 0.6720 0.4055 -0.1455 0.0119  0.1150  432  TYR B CD1 
11852 C CD2 . TYR B 434  ? 0.4270 0.6913 0.4161 -0.1410 0.0152  0.1141  432  TYR B CD2 
11853 C CE1 . TYR B 434  ? 0.4506 0.7006 0.4241 -0.1480 0.0133  0.1185  432  TYR B CE1 
11854 C CE2 . TYR B 434  ? 0.3882 0.6619 0.3767 -0.1434 0.0167  0.1176  432  TYR B CE2 
11855 C CZ  . TYR B 434  ? 0.4289 0.6955 0.4096 -0.1470 0.0158  0.1198  432  TYR B CZ  
11856 O OH  . TYR B 434  ? 0.4562 0.7324 0.4363 -0.1495 0.0174  0.1233  432  TYR B OH  
11857 N N   . HIS B 435  ? 0.3532 0.5917 0.3439 -0.1513 0.0025  0.1137  433  HIS B N   
11858 C CA  . HIS B 435  ? 0.4109 0.6545 0.4045 -0.1575 -0.0007 0.1174  433  HIS B CA  
11859 C C   . HIS B 435  ? 0.4351 0.6634 0.4252 -0.1637 -0.0071 0.1181  433  HIS B C   
11860 O O   . HIS B 435  ? 0.3746 0.6005 0.3623 -0.1707 -0.0110 0.1219  433  HIS B O   
11861 C CB  . HIS B 435  ? 0.4119 0.6713 0.4146 -0.1534 0.0021  0.1166  433  HIS B CB  
11862 C CG  . HIS B 435  ? 0.4265 0.7018 0.4323 -0.1488 0.0076  0.1170  433  HIS B CG  
11863 N ND1 . HIS B 435  ? 0.4368 0.7212 0.4426 -0.1527 0.0079  0.1212  433  HIS B ND1 
11864 C CD2 . HIS B 435  ? 0.4190 0.7019 0.4275 -0.1404 0.0129  0.1136  433  HIS B CD2 
11865 C CE1 . HIS B 435  ? 0.4274 0.7247 0.4359 -0.1469 0.0133  0.1203  433  HIS B CE1 
11866 N NE2 . HIS B 435  ? 0.4226 0.7190 0.4327 -0.1393 0.0163  0.1157  433  HIS B NE2 
11867 N N   . MET B 436  ? 0.4033 0.6207 0.3925 -0.1612 -0.0083 0.1146  434  MET B N   
11868 C CA  . MET B 436  ? 0.3667 0.5686 0.3521 -0.1665 -0.0144 0.1148  434  MET B CA  
11869 C C   . MET B 436  ? 0.4333 0.6217 0.4098 -0.1722 -0.0181 0.1174  434  MET B C   
11870 O O   . MET B 436  ? 0.4256 0.6043 0.3987 -0.1784 -0.0236 0.1192  434  MET B O   
11871 C CB  . MET B 436  ? 0.3836 0.5762 0.3695 -0.1622 -0.0146 0.1103  434  MET B CB  
11872 C CG  . MET B 436  ? 0.4376 0.6126 0.4187 -0.1669 -0.0207 0.1099  434  MET B CG  
11873 S SD  . MET B 436  ? 0.4847 0.6478 0.4651 -0.1616 -0.0204 0.1047  434  MET B SD  
11874 C CE  . MET B 436  ? 0.3989 0.5788 0.3900 -0.1553 -0.0161 0.1020  434  MET B CE  
11875 N N   . ALA B 437  ? 0.3982 0.5854 0.3705 -0.1701 -0.0154 0.1174  435  ALA B N   
11876 C CA  . ALA B 437  ? 0.4200 0.5930 0.3832 -0.1748 -0.0191 0.1195  435  ALA B CA  
11877 C C   . ALA B 437  ? 0.4884 0.6657 0.4502 -0.1815 -0.0212 0.1243  435  ALA B C   
11878 O O   . ALA B 437  ? 0.5158 0.6800 0.4707 -0.1871 -0.0261 0.1265  435  ALA B O   
11879 C CB  . ALA B 437  ? 0.4277 0.5984 0.3866 -0.1703 -0.0155 0.1181  435  ALA B CB  
11880 N N   . GLY B 438  ? 0.4774 0.6727 0.4454 -0.1810 -0.0179 0.1261  436  GLY B N   
11881 C CA  . GLY B 438  ? 0.5181 0.7191 0.4852 -0.1873 -0.0197 0.1309  436  GLY B CA  
11882 C C   . GLY B 438  ? 0.5869 0.7937 0.5510 -0.1869 -0.0164 0.1329  436  GLY B C   
11883 O O   . GLY B 438  ? 0.5231 0.7319 0.4864 -0.1810 -0.0121 0.1306  436  GLY B O   
11884 N N   . LYS B 439  ? 0.5572 0.7666 0.5193 -0.1934 -0.0186 0.1375  437  LYS B N   
11885 C CA  . LYS B 439  ? 0.5181 0.7354 0.4781 -0.1938 -0.0155 0.1400  437  LYS B CA  
11886 C C   . LYS B 439  ? 0.5838 0.7859 0.5340 -0.1975 -0.0185 0.1416  437  LYS B C   
11887 O O   . LYS B 439  ? 0.5951 0.8016 0.5425 -0.1966 -0.0155 0.1430  437  LYS B O   
11888 C CB  . LYS B 439  ? 0.5149 0.7469 0.4793 -0.1984 -0.0154 0.1444  437  LYS B CB  
11889 N N   . ASP B 440  ? 0.5466 0.7308 0.4914 -0.2014 -0.0244 0.1415  438  ASP B N   
11890 C CA  . ASP B 440  ? 0.6084 0.7774 0.5438 -0.2052 -0.0279 0.1432  438  ASP B CA  
11891 C C   . ASP B 440  ? 0.6435 0.8019 0.5745 -0.1994 -0.0265 0.1395  438  ASP B C   
11892 O O   . ASP B 440  ? 0.7423 0.8861 0.6706 -0.1986 -0.0297 0.1369  438  ASP B O   
11893 C CB  . ASP B 440  ? 0.6349 0.7894 0.5660 -0.2120 -0.0352 0.1449  438  ASP B CB  
11894 N N   . PHE B 441  ? 0.5632 0.7289 0.4934 -0.1952 -0.0215 0.1391  439  PHE B N   
11895 C CA  . PHE B 441  ? 0.6355 0.7930 0.5617 -0.1892 -0.0196 0.1355  439  PHE B CA  
11896 C C   . PHE B 441  ? 0.6611 0.8100 0.5785 -0.1906 -0.0204 0.1374  439  PHE B C   
11897 O O   . PHE B 441  ? 0.5944 0.7529 0.5112 -0.1922 -0.0181 0.1403  439  PHE B O   
11898 C CB  . PHE B 441  ? 0.5298 0.7018 0.4619 -0.1814 -0.0128 0.1324  439  PHE B CB  
11899 C CG  . PHE B 441  ? 0.5827 0.7459 0.5109 -0.1752 -0.0112 0.1285  439  PHE B CG  
11900 C CD1 . PHE B 441  ? 0.5316 0.6920 0.4533 -0.1731 -0.0094 0.1287  439  PHE B CD1 
11901 C CD2 . PHE B 441  ? 0.5320 0.6893 0.4626 -0.1717 -0.0119 0.1248  439  PHE B CD2 
11902 C CE1 . PHE B 441  ? 0.5128 0.6649 0.4304 -0.1675 -0.0083 0.1252  439  PHE B CE1 
11903 C CE2 . PHE B 441  ? 0.5293 0.6786 0.4561 -0.1663 -0.0106 0.1214  439  PHE B CE2 
11904 C CZ  . PHE B 441  ? 0.5121 0.6587 0.4323 -0.1642 -0.0090 0.1216  439  PHE B CZ  
11905 N N   . HIS B 442  ? 0.6562 0.7873 0.5668 -0.1897 -0.0237 0.1357  440  HIS B N   
11906 C CA  . HIS B 442  ? 0.6190 0.7406 0.5210 -0.1891 -0.0242 0.1363  440  HIS B CA  
11907 C C   . HIS B 442  ? 0.6079 0.7225 0.5077 -0.1821 -0.0226 0.1320  440  HIS B C   
11908 O O   . HIS B 442  ? 0.5858 0.6956 0.4885 -0.1797 -0.0236 0.1290  440  HIS B O   
11909 C CB  . HIS B 442  ? 0.6506 0.7550 0.5450 -0.1954 -0.0311 0.1390  440  HIS B CB  
11910 C CG  . HIS B 442  ? 0.6944 0.7821 0.5869 -0.1956 -0.0361 0.1367  440  HIS B CG  
11911 N ND1 . HIS B 442  ? 0.6859 0.7581 0.5723 -0.1920 -0.0380 0.1341  440  HIS B ND1 
11912 C CD2 . HIS B 442  ? 0.6647 0.7487 0.5602 -0.1989 -0.0398 0.1365  440  HIS B CD2 
11913 C CE1 . HIS B 442  ? 0.6295 0.6891 0.5155 -0.1928 -0.0425 0.1324  440  HIS B CE1 
11914 N NE2 . HIS B 442  ? 0.6902 0.7566 0.5816 -0.1970 -0.0436 0.1337  440  HIS B NE2 
11915 N N   . VAL B 443  ? 0.5852 0.6993 0.4798 -0.1787 -0.0201 0.1316  441  VAL B N   
11916 C CA  . VAL B 443  ? 0.5111 0.6166 0.4021 -0.1725 -0.0194 0.1278  441  VAL B CA  
11917 C C   . VAL B 443  ? 0.5052 0.5898 0.3906 -0.1746 -0.0258 0.1274  441  VAL B C   
11918 O O   . VAL B 443  ? 0.5647 0.6390 0.4450 -0.1799 -0.0306 0.1303  441  VAL B O   
11919 C CB  . VAL B 443  ? 0.5705 0.6781 0.4557 -0.1691 -0.0163 0.1279  441  VAL B CB  
11920 C CG1 . VAL B 443  ? 0.4708 0.5692 0.3518 -0.1627 -0.0160 0.1239  441  VAL B CG1 
11921 C CG2 . VAL B 443  ? 0.5764 0.7044 0.4671 -0.1665 -0.0098 0.1280  441  VAL B CG2 
11922 N N   . GLY B 444  ? 0.5336 0.6121 0.4204 -0.1703 -0.0261 0.1237  442  GLY B N   
11923 C CA  . GLY B 444  ? 0.4920 0.5517 0.3754 -0.1711 -0.0321 0.1221  442  GLY B CA  
11924 C C   . GLY B 444  ? 0.5062 0.5661 0.3955 -0.1740 -0.0341 0.1218  442  GLY B C   
11925 O O   . GLY B 444  ? 0.4689 0.5142 0.3572 -0.1723 -0.0385 0.1186  442  GLY B O   
11926 N N   . LYS B 445  ? 0.4839 0.5597 0.3804 -0.1766 -0.0314 0.1235  443  LYS B N   
11927 C CA  . LYS B 445  ? 0.4757 0.5531 0.3784 -0.1786 -0.0331 0.1226  443  LYS B CA  
11928 C C   . LYS B 445  ? 0.4972 0.5763 0.4053 -0.1713 -0.0305 0.1172  443  LYS B C   
11929 O O   . LYS B 445  ? 0.4503 0.5169 0.3585 -0.1690 -0.0342 0.1135  443  LYS B O   
11930 C CB  . LYS B 445  ? 0.4732 0.5680 0.3827 -0.1820 -0.0309 0.1252  443  LYS B CB  
11931 N N   . TYR B 446  ? 0.4647 0.5591 0.3781 -0.1658 -0.0246 0.1152  444  TYR B N   
11932 C CA  . TYR B 446  ? 0.4408 0.5369 0.3597 -0.1564 -0.0220 0.1085  444  TYR B CA  
11933 C C   . TYR B 446  ? 0.4355 0.5432 0.3551 -0.1508 -0.0162 0.1072  444  TYR B C   
11934 O O   . TYR B 446  ? 0.4407 0.5555 0.3569 -0.1544 -0.0143 0.1115  444  TYR B O   
11935 C CB  . TYR B 446  ? 0.3852 0.4902 0.3128 -0.1565 -0.0211 0.1074  444  TYR B CB  
11936 C CG  . TYR B 446  ? 0.4208 0.5469 0.3544 -0.1589 -0.0162 0.1109  444  TYR B CG  
11937 C CD1 . TYR B 446  ? 0.4512 0.5907 0.3902 -0.1518 -0.0105 0.1079  444  TYR B CD1 
11938 C CD2 . TYR B 446  ? 0.4495 0.5816 0.3840 -0.1672 -0.0178 0.1163  444  TYR B CD2 
11939 C CE1 . TYR B 446  ? 0.4512 0.6102 0.3957 -0.1535 -0.0060 0.1110  444  TYR B CE1 
11940 C CE2 . TYR B 446  ? 0.4898 0.6403 0.4310 -0.1668 -0.0141 0.1176  444  TYR B CE2 
11941 C CZ  . TYR B 446  ? 0.5056 0.6697 0.4518 -0.1601 -0.0080 0.1152  444  TYR B CZ  
11942 O OH  . TYR B 446  ? 0.5125 0.6947 0.4653 -0.1593 -0.0044 0.1164  444  TYR B OH  
11943 N N   . GLU B 447  ? 0.3959 0.5056 0.3199 -0.1421 -0.0136 0.1012  445  GLU B N   
11944 C CA  . GLU B 447  ? 0.3519 0.4726 0.2769 -0.1362 -0.0081 0.0993  445  GLU B CA  
11945 C C   . GLU B 447  ? 0.3539 0.4812 0.2868 -0.1287 -0.0051 0.0940  445  GLU B C   
11946 O O   . GLU B 447  ? 0.3350 0.4556 0.2713 -0.1273 -0.0075 0.0911  445  GLU B O   
11947 C CB  . GLU B 447  ? 0.3199 0.4299 0.2376 -0.1323 -0.0090 0.0972  445  GLU B CB  
11948 C CG  . GLU B 447  ? 0.3229 0.4203 0.2413 -0.1254 -0.0111 0.0908  445  GLU B CG  
11949 C CD  . GLU B 447  ? 0.3784 0.4648 0.2896 -0.1219 -0.0126 0.0889  445  GLU B CD  
11950 O OE1 . GLU B 447  ? 0.3595 0.4477 0.2649 -0.1251 -0.0120 0.0926  445  GLU B OE1 
11951 O OE2 . GLU B 447  ? 0.3581 0.4345 0.2697 -0.1163 -0.0143 0.0839  445  GLU B OE2 
11952 N N   . PHE B 448  ? 0.3495 0.4896 0.2848 -0.1239 0.0003  0.0926  446  PHE B N   
11953 C CA  . PHE B 448  ? 0.3381 0.4827 0.2795 -0.1157 0.0032  0.0870  446  PHE B CA  
11954 C C   . PHE B 448  ? 0.2992 0.4344 0.2365 -0.1086 0.0033  0.0820  446  PHE B C   
11955 O O   . PHE B 448  ? 0.3367 0.4650 0.2668 -0.1096 0.0021  0.0832  446  PHE B O   
11956 C CB  . PHE B 448  ? 0.3376 0.5017 0.2844 -0.1140 0.0089  0.0881  446  PHE B CB  
11957 C CG  . PHE B 448  ? 0.3284 0.5032 0.2810 -0.1199 0.0090  0.0923  446  PHE B CG  
11958 C CD1 . PHE B 448  ? 0.3374 0.5125 0.2967 -0.1187 0.0079  0.0901  446  PHE B CD1 
11959 C CD2 . PHE B 448  ? 0.3701 0.5550 0.3215 -0.1268 0.0102  0.0986  446  PHE B CD2 
11960 C CE1 . PHE B 448  ? 0.3381 0.5231 0.3027 -0.1242 0.0077  0.0940  446  PHE B CE1 
11961 C CE2 . PHE B 448  ? 0.4337 0.6289 0.3907 -0.1326 0.0100  0.1026  446  PHE B CE2 
11962 C CZ  . PHE B 448  ? 0.3592 0.5544 0.3229 -0.1312 0.0087  0.1002  446  PHE B CZ  
11963 N N   . GLN B 449  ? 0.3475 0.4827 0.2895 -0.1014 0.0048  0.0766  447  GLN B N   
11964 C CA  . GLN B 449  ? 0.3282 0.4558 0.2673 -0.0945 0.0051  0.0716  447  GLN B CA  
11965 C C   . GLN B 449  ? 0.3246 0.4612 0.2692 -0.0871 0.0094  0.0674  447  GLN B C   
11966 O O   . GLN B 449  ? 0.3248 0.4695 0.2763 -0.0866 0.0109  0.0671  447  GLN B O   
11967 C CB  . GLN B 449  ? 0.2635 0.3742 0.2009 -0.0934 0.0003  0.0686  447  GLN B CB  
11968 C CG  . GLN B 449  ? 0.3017 0.4011 0.2328 -0.0997 -0.0044 0.0722  447  GLN B CG  
11969 C CD  . GLN B 449  ? 0.3071 0.3902 0.2352 -0.0966 -0.0085 0.0686  447  GLN B CD  
11970 O OE1 . GLN B 449  ? 0.3204 0.4010 0.2518 -0.0904 -0.0079 0.0636  447  GLN B OE1 
11971 N NE2 . GLN B 449  ? 0.3096 0.3817 0.2312 -0.1010 -0.0126 0.0713  447  GLN B NE2 
11972 N N   . CYS B 450  ? 0.2893 0.4244 0.2307 -0.0814 0.0113  0.0641  448  CYS B N   
11973 C CA  . CYS B 450  ? 0.3242 0.4664 0.2697 -0.0741 0.0152  0.0598  448  CYS B CA  
11974 C C   . CYS B 450  ? 0.2948 0.4272 0.2362 -0.0683 0.0145  0.0551  448  CYS B C   
11975 O O   . CYS B 450  ? 0.2917 0.4140 0.2269 -0.0700 0.0116  0.0556  448  CYS B O   
11976 C CB  . CYS B 450  ? 0.3299 0.4884 0.2762 -0.0737 0.0203  0.0621  448  CYS B CB  
11977 S SG  . CYS B 450  ? 0.3274 0.4859 0.2645 -0.0729 0.0220  0.0630  448  CYS B SG  
11978 N N   . LEU B 451  ? 0.3002 0.4354 0.2451 -0.0615 0.0169  0.0506  449  LEU B N   
11979 C CA  . LEU B 451  ? 0.3140 0.4408 0.2557 -0.0558 0.0164  0.0458  449  LEU B CA  
11980 C C   . LEU B 451  ? 0.3838 0.5168 0.3205 -0.0532 0.0198  0.0457  449  LEU B C   
11981 O O   . LEU B 451  ? 0.3037 0.4497 0.2421 -0.0527 0.0239  0.0472  449  LEU B O   
11982 C CB  . LEU B 451  ? 0.3503 0.4760 0.2980 -0.0499 0.0170  0.0410  449  LEU B CB  
11983 N N   . HIS B 452  ? 0.3703 0.4942 0.3007 -0.0515 0.0180  0.0439  450  HIS B N   
11984 C CA  . HIS B 452  ? 0.3871 0.5152 0.3119 -0.0485 0.0209  0.0431  450  HIS B CA  
11985 C C   . HIS B 452  ? 0.3304 0.4660 0.2586 -0.0418 0.0250  0.0392  450  HIS B C   
11986 O O   . HIS B 452  ? 0.3618 0.4936 0.2947 -0.0380 0.0243  0.0354  450  HIS B O   
11987 C CB  . HIS B 452  ? 0.3249 0.4405 0.2429 -0.0472 0.0178  0.0410  450  HIS B CB  
11988 C CG  . HIS B 452  ? 0.3621 0.4804 0.2746 -0.0426 0.0205  0.0387  450  HIS B CG  
11989 N ND1 . HIS B 452  ? 0.3885 0.5116 0.2943 -0.0449 0.0222  0.0418  450  HIS B ND1 
11990 C CD2 . HIS B 452  ? 0.3781 0.4949 0.2905 -0.0361 0.0217  0.0336  450  HIS B CD2 
11991 C CE1 . HIS B 452  ? 0.3985 0.5228 0.3000 -0.0396 0.0244  0.0385  450  HIS B CE1 
11992 N NE2 . HIS B 452  ? 0.3983 0.5185 0.3037 -0.0343 0.0240  0.0335  450  HIS B NE2 
11993 N N   . GLY B 453  ? 0.4121 0.5587 0.3380 -0.0404 0.0292  0.0402  451  GLY B N   
11994 C CA  . GLY B 453  ? 0.4017 0.5550 0.3296 -0.0336 0.0331  0.0364  451  GLY B CA  
11995 C C   . GLY B 453  ? 0.4874 0.6503 0.4239 -0.0324 0.0354  0.0366  451  GLY B C   
11996 O O   . GLY B 453  ? 0.5642 0.7344 0.5025 -0.0269 0.0390  0.0341  451  GLY B O   
11997 N N   . MET B 454  ? 0.4649 0.6279 0.4064 -0.0374 0.0333  0.0395  452  MET B N   
11998 C CA  . MET B 454  ? 0.4396 0.6117 0.3894 -0.0371 0.0350  0.0402  452  MET B CA  
11999 C C   . MET B 454  ? 0.4006 0.5829 0.3525 -0.0438 0.0358  0.0461  452  MET B C   
12000 O O   . MET B 454  ? 0.4566 0.6523 0.4132 -0.0429 0.0393  0.0475  452  MET B O   
12001 C CB  . MET B 454  ? 0.4428 0.6054 0.3974 -0.0367 0.0315  0.0378  452  MET B CB  
12002 C CG  . MET B 454  ? 0.4457 0.6163 0.4087 -0.0349 0.0331  0.0373  452  MET B CG  
12003 S SD  . MET B 454  ? 0.7375 0.9145 0.7019 -0.0257 0.0375  0.0326  452  MET B SD  
12004 C CE  . MET B 454  ? 0.5789 0.7398 0.5377 -0.0215 0.0349  0.0274  452  MET B CE  
12005 N N   . GLY B 455  ? 0.3609 0.5372 0.3093 -0.0505 0.0326  0.0497  453  GLY B N   
12006 C CA  . GLY B 455  ? 0.3788 0.5629 0.3294 -0.0576 0.0324  0.0555  453  GLY B CA  
12007 C C   . GLY B 455  ? 0.4116 0.6066 0.3584 -0.0606 0.0355  0.0598  453  GLY B C   
12008 O O   . GLY B 455  ? 0.3804 0.5856 0.3304 -0.0659 0.0365  0.0646  453  GLY B O   
12009 N N   . GLU B 456  ? 0.4582 0.6514 0.3979 -0.0577 0.0370  0.0585  454  GLU B N   
12010 C CA  . GLU B 456  ? 0.4758 0.6786 0.4109 -0.0611 0.0398  0.0629  454  GLU B CA  
12011 C C   . GLU B 456  ? 0.4110 0.6326 0.3511 -0.0597 0.0451  0.0647  454  GLU B C   
12012 O O   . GLU B 456  ? 0.4293 0.6607 0.3691 -0.0655 0.0465  0.0703  454  GLU B O   
12013 C CB  . GLU B 456  ? 0.5066 0.7035 0.4328 -0.0576 0.0404  0.0606  454  GLU B CB  
12014 C CG  . GLU B 456  ? 0.4951 0.6748 0.4158 -0.0597 0.0351  0.0597  454  GLU B CG  
12015 C CD  . GLU B 456  ? 0.4658 0.6345 0.3876 -0.0534 0.0332  0.0534  454  GLU B CD  
12016 O OE1 . GLU B 456  ? 0.5280 0.6996 0.4569 -0.0499 0.0342  0.0507  454  GLU B OE1 
12017 O OE2 . GLU B 456  ? 0.3998 0.5570 0.3154 -0.0521 0.0307  0.0513  454  GLU B OE2 
12018 N N   . PRO B 457  ? 0.4007 0.6284 0.3453 -0.0524 0.0482  0.0606  455  PRO B N   
12019 C CA  . PRO B 457  ? 0.4171 0.6632 0.3672 -0.0513 0.0531  0.0628  455  PRO B CA  
12020 C C   . PRO B 457  ? 0.4505 0.7044 0.4072 -0.0586 0.0519  0.0681  455  PRO B C   
12021 O O   . PRO B 457  ? 0.4636 0.7322 0.4218 -0.0618 0.0551  0.0727  455  PRO B O   
12022 C CB  . PRO B 457  ? 0.4456 0.6922 0.4003 -0.0426 0.0548  0.0570  455  PRO B CB  
12023 C CG  . PRO B 457  ? 0.4672 0.6989 0.4155 -0.0382 0.0529  0.0520  455  PRO B CG  
12024 C CD  . PRO B 457  ? 0.4197 0.6382 0.3639 -0.0447 0.0478  0.0540  455  PRO B CD  
12025 N N   . LEU B 458  ? 0.4236 0.6680 0.3840 -0.0614 0.0475  0.0677  456  LEU B N   
12026 C CA  . LEU B 458  ? 0.3779 0.6283 0.3439 -0.0687 0.0459  0.0726  456  LEU B CA  
12027 C C   . LEU B 458  ? 0.3973 0.6450 0.3581 -0.0775 0.0435  0.0781  456  LEU B C   
12028 O O   . LEU B 458  ? 0.3862 0.6459 0.3493 -0.0833 0.0449  0.0836  456  LEU B O   
12029 C CB  . LEU B 458  ? 0.3415 0.5821 0.3125 -0.0687 0.0418  0.0701  456  LEU B CB  
12030 C CG  . LEU B 458  ? 0.3598 0.6018 0.3350 -0.0769 0.0387  0.0748  456  LEU B CG  
12031 C CD1 . LEU B 458  ? 0.3761 0.6377 0.3583 -0.0786 0.0422  0.0786  456  LEU B CD1 
12032 C CD2 . LEU B 458  ? 0.3159 0.5460 0.2945 -0.0762 0.0345  0.0717  456  LEU B CD2 
12033 N N   . TYR B 459  ? 0.3592 0.5912 0.3128 -0.0787 0.0400  0.0770  457  TYR B N   
12034 C CA  . TYR B 459  ? 0.3758 0.6034 0.3244 -0.0872 0.0371  0.0823  457  TYR B CA  
12035 C C   . TYR B 459  ? 0.3852 0.6210 0.3276 -0.0888 0.0404  0.0857  457  TYR B C   
12036 O O   . TYR B 459  ? 0.3789 0.6143 0.3178 -0.0965 0.0387  0.0911  457  TYR B O   
12037 C CB  . TYR B 459  ? 0.3712 0.5787 0.3149 -0.0881 0.0316  0.0801  457  TYR B CB  
12038 C CG  . TYR B 459  ? 0.3481 0.5495 0.2976 -0.0900 0.0279  0.0792  457  TYR B CG  
12039 C CD1 . TYR B 459  ? 0.3289 0.5301 0.2797 -0.0983 0.0250  0.0842  457  TYR B CD1 
12040 C CD2 . TYR B 459  ? 0.3778 0.5741 0.3315 -0.0835 0.0276  0.0736  457  TYR B CD2 
12041 C CE1 . TYR B 459  ? 0.3714 0.5672 0.3271 -0.1000 0.0216  0.0834  457  TYR B CE1 
12042 C CE2 . TYR B 459  ? 0.3617 0.5528 0.3205 -0.0852 0.0243  0.0730  457  TYR B CE2 
12043 C CZ  . TYR B 459  ? 0.3075 0.4983 0.2672 -0.0934 0.0214  0.0778  457  TYR B CZ  
12044 O OH  . TYR B 459  ? 0.3051 0.4905 0.2692 -0.0952 0.0181  0.0771  457  TYR B OH  
12045 N N   . GLU B 460  ? 0.3658 0.6092 0.3069 -0.0818 0.0451  0.0827  458  GLU B N   
12046 C CA  . GLU B 460  ? 0.4884 0.7420 0.4256 -0.0827 0.0487  0.0857  458  GLU B CA  
12047 C C   . GLU B 460  ? 0.5418 0.8076 0.4865 -0.0866 0.0492  0.0896  458  GLU B C   
12048 O O   . GLU B 460  ? 0.4956 0.7665 0.4380 -0.0895 0.0502  0.0929  458  GLU B O   
12049 C CB  . GLU B 460  ? 0.5011 0.7602 0.4364 -0.0734 0.0535  0.0810  458  GLU B CB  
12050 N N   . GLU B 461  ? 0.5021 0.7724 0.4555 -0.0870 0.0485  0.0895  459  GLU B N   
12051 C CA  . GLU B 461  ? 0.4878 0.7691 0.4488 -0.0909 0.0483  0.0931  459  GLU B CA  
12052 C C   . GLU B 461  ? 0.5201 0.7946 0.4815 -0.1004 0.0430  0.0975  459  GLU B C   
12053 O O   . GLU B 461  ? 0.4894 0.7715 0.4574 -0.1041 0.0419  0.1003  459  GLU B O   
12054 C CB  . GLU B 461  ? 0.4469 0.7375 0.4171 -0.0854 0.0503  0.0903  459  GLU B CB  
12055 C CG  . GLU B 461  ? 0.3790 0.6723 0.3484 -0.0754 0.0546  0.0848  459  GLU B CG  
12056 C CD  . GLU B 461  ? 0.5871 0.8897 0.5540 -0.0715 0.0588  0.0848  459  GLU B CD  
12057 O OE1 . GLU B 461  ? 0.5113 0.8204 0.4786 -0.0765 0.0588  0.0892  459  GLU B OE1 
12058 O OE2 . GLU B 461  ? 0.6252 0.9283 0.5896 -0.0635 0.0622  0.0803  459  GLU B OE2 
12059 N N   . VAL B 462  ? 0.4458 0.7057 0.3999 -0.1043 0.0395  0.0982  460  VAL B N   
12060 C CA  . VAL B 462  ? 0.4571 0.7079 0.4111 -0.1127 0.0340  0.1017  460  VAL B CA  
12061 C C   . VAL B 462  ? 0.4881 0.7300 0.4335 -0.1186 0.0313  0.1052  460  VAL B C   
12062 O O   . VAL B 462  ? 0.4214 0.6628 0.3671 -0.1259 0.0283  0.1096  460  VAL B O   
12063 C CB  . VAL B 462  ? 0.4163 0.6557 0.3705 -0.1118 0.0314  0.0989  460  VAL B CB  
12064 C CG1 . VAL B 462  ? 0.3993 0.6272 0.3518 -0.1202 0.0255  0.1022  460  VAL B CG1 
12065 C CG2 . VAL B 462  ? 0.3921 0.6402 0.3553 -0.1065 0.0336  0.0957  460  VAL B CG2 
12066 N N   . VAL B 463  ? 0.4408 0.6747 0.3780 -0.1156 0.0321  0.1033  461  VAL B N   
12067 C CA  . VAL B 463  ? 0.4172 0.6405 0.3455 -0.1208 0.0290  0.1064  461  VAL B CA  
12068 C C   . VAL B 463  ? 0.4810 0.7144 0.4082 -0.1226 0.0314  0.1096  461  VAL B C   
12069 O O   . VAL B 463  ? 0.4753 0.7211 0.4049 -0.1171 0.0363  0.1079  461  VAL B O   
12070 C CB  . VAL B 463  ? 0.4314 0.6431 0.3511 -0.1167 0.0288  0.1033  461  VAL B CB  
12071 C CG1 . VAL B 463  ? 0.3828 0.5823 0.3050 -0.1139 0.0253  0.0989  461  VAL B CG1 
12072 C CG2 . VAL B 463  ? 0.5014 0.7221 0.4201 -0.1086 0.0343  0.0997  461  VAL B CG2 
12073 N N   . GLY B 464  ? 0.4397 0.6675 0.3631 -0.1301 0.0278  0.1142  462  GLY B N   
12074 C CA  . GLY B 464  ? 0.5463 0.7808 0.4665 -0.1323 0.0296  0.1174  462  GLY B CA  
12075 C C   . GLY B 464  ? 0.6325 0.8783 0.5593 -0.1377 0.0293  0.1215  462  GLY B C   
12076 O O   . GLY B 464  ? 0.5962 0.8498 0.5315 -0.1372 0.0297  0.1209  462  GLY B O   
12077 N N   . ARG B 465  ? 0.6536 0.9004 0.5763 -0.1429 0.0285  0.1258  463  ARG B N   
12078 C CA  . ARG B 465  ? 0.6465 0.9043 0.5746 -0.1484 0.0282  0.1302  463  ARG B CA  
12079 C C   . ARG B 465  ? 0.6635 0.9401 0.5998 -0.1433 0.0335  0.1289  463  ARG B C   
12080 O O   . ARG B 465  ? 0.6644 0.9507 0.6074 -0.1469 0.0329  0.1315  463  ARG B O   
12081 C CB  . ARG B 465  ? 0.6622 0.9186 0.5838 -0.1539 0.0272  0.1347  463  ARG B CB  
12082 N N   . GLY B 466  ? 0.5975 0.8789 0.5331 -0.1349 0.0384  0.1247  464  GLY B N   
12083 C CA  . GLY B 466  ? 0.5196 0.8179 0.4625 -0.1292 0.0433  0.1231  464  GLY B CA  
12084 C C   . GLY B 466  ? 0.6712 0.9725 0.6222 -0.1255 0.0434  0.1200  464  GLY B C   
12085 O O   . GLY B 466  ? 0.6544 0.9699 0.6128 -0.1223 0.0464  0.1196  464  GLY B O   
12086 N N   . LYS B 467  ? 0.6506 0.9389 0.6003 -0.1256 0.0401  0.1177  465  LYS B N   
12087 C CA  . LYS B 467  ? 0.5817 0.8715 0.5385 -0.1219 0.0401  0.1145  465  LYS B CA  
12088 C C   . LYS B 467  ? 0.6037 0.8890 0.5645 -0.1291 0.0349  0.1172  465  LYS B C   
12089 O O   . LYS B 467  ? 0.6298 0.9229 0.5943 -0.1343 0.0337  0.1212  465  LYS B O   
12090 C CB  . LYS B 467  ? 0.5768 0.8559 0.5297 -0.1160 0.0405  0.1095  465  LYS B CB  
12091 C CG  . LYS B 467  ? 0.5869 0.8713 0.5370 -0.1075 0.0458  0.1057  465  LYS B CG  
12092 C CD  . LYS B 467  ? 0.5773 0.8779 0.5357 -0.1019 0.0500  0.1042  465  LYS B CD  
12093 C CE  . LYS B 467  ? 0.5900 0.8943 0.5454 -0.0927 0.0550  0.0997  465  LYS B CE  
12094 N NZ  . LYS B 467  ? 0.6032 0.9202 0.5665 -0.0860 0.0586  0.0971  465  LYS B NZ  
12095 N N   . LEU B 468  ? 0.4808 0.7536 0.4407 -0.1293 0.0317  0.1150  466  LEU B N   
12096 C CA  . LEU B 468  ? 0.3949 0.6607 0.3569 -0.1363 0.0263  0.1174  466  LEU B CA  
12097 C C   . LEU B 468  ? 0.4852 0.7358 0.4388 -0.1432 0.0216  0.1202  466  LEU B C   
12098 O O   . LEU B 468  ? 0.4756 0.7190 0.4298 -0.1496 0.0166  0.1225  466  LEU B O   
12099 C CB  . LEU B 468  ? 0.5060 0.7668 0.4720 -0.1329 0.0254  0.1136  466  LEU B CB  
12100 C CG  . LEU B 468  ? 0.4473 0.7220 0.4218 -0.1258 0.0295  0.1106  466  LEU B CG  
12101 C CD1 . LEU B 468  ? 0.4283 0.6971 0.4063 -0.1227 0.0283  0.1069  466  LEU B CD1 
12102 C CD2 . LEU B 468  ? 0.4911 0.7799 0.4724 -0.1288 0.0298  0.1139  466  LEU B CD2 
12103 N N   . ASP B 469  ? 0.5077 0.7532 0.4535 -0.1420 0.0228  0.1202  467  ASP B N   
12104 C CA  . ASP B 469  ? 0.5330 0.7637 0.4703 -0.1480 0.0183  0.1229  467  ASP B CA  
12105 C C   . ASP B 469  ? 0.4302 0.6448 0.3656 -0.1497 0.0135  0.1214  467  ASP B C   
12106 O O   . ASP B 469  ? 0.4786 0.6824 0.4109 -0.1565 0.0083  0.1242  467  ASP B O   
12107 C CB  . ASP B 469  ? 0.5361 0.7703 0.4733 -0.1560 0.0159  0.1283  467  ASP B CB  
12108 N N   . ARG B 470  ? 0.4710 0.6837 0.4080 -0.1434 0.0153  0.1169  468  ARG B N   
12109 C CA  . ARG B 470  ? 0.4783 0.6760 0.4132 -0.1439 0.0114  0.1149  468  ARG B CA  
12110 C C   . ARG B 470  ? 0.3820 0.5716 0.3102 -0.1382 0.0129  0.1116  468  ARG B C   
12111 O O   . ARG B 470  ? 0.4035 0.6022 0.3334 -0.1314 0.0178  0.1085  468  ARG B O   
12112 C CB  . ARG B 470  ? 0.4259 0.6286 0.3694 -0.1418 0.0117  0.1126  468  ARG B CB  
12113 C CG  . ARG B 470  ? 0.4095 0.6194 0.3594 -0.1474 0.0097  0.1157  468  ARG B CG  
12114 C CD  . ARG B 470  ? 0.3845 0.5818 0.3292 -0.1558 0.0036  0.1195  468  ARG B CD  
12115 N NE  . ARG B 470  ? 0.4788 0.6826 0.4288 -0.1613 0.0013  0.1225  468  ARG B NE  
12116 C CZ  . ARG B 470  ? 0.5071 0.7212 0.4584 -0.1649 0.0021  0.1262  468  ARG B CZ  
12117 N NH1 . ARG B 470  ? 0.4733 0.6931 0.4213 -0.1634 0.0054  0.1273  468  ARG B NH1 
12118 N NH2 . ARG B 470  ? 0.4856 0.7045 0.4413 -0.1701 -0.0005 0.1289  468  ARG B NH2 
12119 N N   . PRO B 471  ? 0.4264 0.5991 0.3470 -0.1406 0.0086  0.1119  469  PRO B N   
12120 C CA  . PRO B 471  ? 0.3658 0.5287 0.2816 -0.1333 0.0087  0.1068  469  PRO B CA  
12121 C C   . PRO B 471  ? 0.4214 0.5800 0.3426 -0.1253 0.0087  0.0998  469  PRO B C   
12122 O O   . PRO B 471  ? 0.3270 0.4847 0.2542 -0.1260 0.0070  0.0988  469  PRO B O   
12123 C CB  . PRO B 471  ? 0.4247 0.5698 0.3323 -0.1379 0.0029  0.1087  469  PRO B CB  
12124 C CG  . PRO B 471  ? 0.4124 0.5533 0.3227 -0.1447 -0.0012 0.1117  469  PRO B CG  
12125 C CD  . PRO B 471  ? 0.4190 0.5784 0.3365 -0.1480 0.0024  0.1150  469  PRO B CD  
12126 N N   . CYS B 472  ? 0.4000 0.5560 0.3187 -0.1177 0.0107  0.0951  470  CYS B N   
12127 C CA  . CYS B 472  ? 0.4137 0.5650 0.3366 -0.1098 0.0108  0.0884  470  CYS B CA  
12128 C C   . CYS B 472  ? 0.3653 0.5021 0.2817 -0.1057 0.0084  0.0849  470  CYS B C   
12129 O O   . CYS B 472  ? 0.3572 0.4950 0.2675 -0.1047 0.0100  0.0855  470  CYS B O   
12130 C CB  . CYS B 472  ? 0.3533 0.5195 0.2817 -0.1035 0.0166  0.0857  470  CYS B CB  
12131 S SG  . CYS B 472  ? 0.3753 0.5357 0.3089 -0.0943 0.0167  0.0778  470  CYS B SG  
12132 N N   . ARG B 473  ? 0.3466 0.4703 0.2641 -0.1036 0.0045  0.0813  471  ARG B N   
12133 C CA  . ARG B 473  ? 0.3469 0.4573 0.2597 -0.0989 0.0021  0.0773  471  ARG B CA  
12134 C C   . ARG B 473  ? 0.3497 0.4627 0.2672 -0.0904 0.0048  0.0711  471  ARG B C   
12135 O O   . ARG B 473  ? 0.3040 0.4187 0.2283 -0.0884 0.0050  0.0687  471  ARG B O   
12136 C CB  . ARG B 473  ? 0.3312 0.4256 0.2423 -0.1015 -0.0038 0.0771  471  ARG B CB  
12137 C CG  . ARG B 473  ? 0.3101 0.3909 0.2162 -0.0971 -0.0066 0.0735  471  ARG B CG  
12138 C CD  . ARG B 473  ? 0.3150 0.3807 0.2191 -0.1001 -0.0125 0.0740  471  ARG B CD  
12139 N NE  . ARG B 473  ? 0.3114 0.3760 0.2116 -0.1083 -0.0146 0.0801  471  ARG B NE  
12140 C CZ  . ARG B 473  ? 0.3714 0.4316 0.2638 -0.1120 -0.0163 0.0839  471  ARG B CZ  
12141 N NH1 . ARG B 473  ? 0.3414 0.3969 0.2287 -0.1082 -0.0165 0.0820  471  ARG B NH1 
12142 N NH2 . ARG B 473  ? 0.3631 0.4233 0.2526 -0.1200 -0.0181 0.0897  471  ARG B NH2 
12143 N N   . ILE B 474  ? 0.3255 0.4384 0.2388 -0.0857 0.0067  0.0686  472  ILE B N   
12144 C CA  . ILE B 474  ? 0.2951 0.4100 0.2116 -0.0777 0.0093  0.0628  472  ILE B CA  
12145 C C   . ILE B 474  ? 0.3238 0.4240 0.2396 -0.0742 0.0053  0.0585  472  ILE B C   
12146 O O   . ILE B 474  ? 0.3034 0.3937 0.2128 -0.0747 0.0024  0.0587  472  ILE B O   
12147 C CB  . ILE B 474  ? 0.3102 0.4325 0.2223 -0.0742 0.0132  0.0622  472  ILE B CB  
12148 C CG1 . ILE B 474  ? 0.3519 0.4902 0.2653 -0.0773 0.0176  0.0664  472  ILE B CG1 
12149 C CG2 . ILE B 474  ? 0.3336 0.4558 0.2481 -0.0661 0.0152  0.0560  472  ILE B CG2 
12150 C CD1 . ILE B 474  ? 0.3910 0.5368 0.2992 -0.0742 0.0216  0.0661  472  ILE B CD1 
12151 N N   . TYR B 475  ? 0.3010 0.4000 0.2233 -0.0706 0.0052  0.0548  473  TYR B N   
12152 C CA  . TYR B 475  ? 0.3160 0.4031 0.2387 -0.0663 0.0022  0.0502  473  TYR B CA  
12153 C C   . TYR B 475  ? 0.3500 0.4379 0.2704 -0.0601 0.0044  0.0463  473  TYR B C   
12154 O O   . TYR B 475  ? 0.3419 0.4387 0.2657 -0.0561 0.0083  0.0441  473  TYR B O   
12155 C CB  . TYR B 475  ? 0.2637 0.3508 0.1941 -0.0647 0.0019  0.0478  473  TYR B CB  
12156 C CG  . TYR B 475  ? 0.2957 0.3707 0.2273 -0.0613 -0.0014 0.0438  473  TYR B CG  
12157 C CD1 . TYR B 475  ? 0.3818 0.4558 0.3152 -0.0548 -0.0001 0.0388  473  TYR B CD1 
12158 C CD2 . TYR B 475  ? 0.3132 0.3780 0.2441 -0.0645 -0.0057 0.0448  473  TYR B CD2 
12159 C CE1 . TYR B 475  ? 0.3509 0.4149 0.2860 -0.0519 -0.0030 0.0353  473  TYR B CE1 
12160 C CE2 . TYR B 475  ? 0.2929 0.3476 0.2253 -0.0612 -0.0085 0.0412  473  TYR B CE2 
12161 C CZ  . TYR B 475  ? 0.3912 0.4460 0.3258 -0.0550 -0.0071 0.0365  473  TYR B CZ  
12162 O OH  . TYR B 475  ? 0.3466 0.3922 0.2830 -0.0518 -0.0097 0.0331  473  TYR B OH  
12163 N N   . ALA B 476  ? 0.3062 0.3848 0.2205 -0.0594 0.0018  0.0455  474  ALA B N   
12164 C CA  . ALA B 476  ? 0.3106 0.3900 0.2206 -0.0549 0.0035  0.0429  474  ALA B CA  
12165 C C   . ALA B 476  ? 0.3210 0.3900 0.2315 -0.0502 0.0008  0.0381  474  ALA B C   
12166 O O   . ALA B 476  ? 0.2921 0.3507 0.1988 -0.0514 -0.0033 0.0384  474  ALA B O   
12167 C CB  . ALA B 476  ? 0.3172 0.3958 0.2188 -0.0583 0.0029  0.0466  474  ALA B CB  
12168 N N   . PRO B 477  ? 0.3101 0.3815 0.2255 -0.0449 0.0027  0.0337  475  PRO B N   
12169 C CA  . PRO B 477  ? 0.3218 0.3841 0.2375 -0.0406 0.0003  0.0293  475  PRO B CA  
12170 C C   . PRO B 477  ? 0.3138 0.3728 0.2223 -0.0387 -0.0003 0.0282  475  PRO B C   
12171 O O   . PRO B 477  ? 0.3390 0.4048 0.2434 -0.0381 0.0027  0.0289  475  PRO B O   
12172 C CB  . PRO B 477  ? 0.3528 0.4204 0.2749 -0.0359 0.0031  0.0254  475  PRO B CB  
12173 C CG  . PRO B 477  ? 0.3372 0.4149 0.2636 -0.0384 0.0060  0.0282  475  PRO B CG  
12174 C CD  . PRO B 477  ? 0.3576 0.4400 0.2784 -0.0427 0.0070  0.0327  475  PRO B CD  
12175 N N   . VAL B 478  ? 0.2972 0.3458 0.2043 -0.0374 -0.0042 0.0262  476  VAL B N   
12176 C CA  . VAL B 478  ? 0.3201 0.3638 0.2204 -0.0359 -0.0059 0.0252  476  VAL B CA  
12177 C C   . VAL B 478  ? 0.3220 0.3587 0.2251 -0.0316 -0.0082 0.0206  476  VAL B C   
12178 O O   . VAL B 478  ? 0.3324 0.3627 0.2394 -0.0320 -0.0112 0.0200  476  VAL B O   
12179 C CB  . VAL B 478  ? 0.3004 0.3376 0.1948 -0.0404 -0.0094 0.0291  476  VAL B CB  
12180 C CG1 . VAL B 478  ? 0.3704 0.4029 0.2577 -0.0386 -0.0112 0.0280  476  VAL B CG1 
12181 C CG2 . VAL B 478  ? 0.3004 0.3442 0.1923 -0.0456 -0.0075 0.0343  476  VAL B CG2 
12182 N N   . GLY B 479  ? 0.4034 0.4411 0.3043 -0.0275 -0.0068 0.0172  477  GLY B N   
12183 C CA  . GLY B 479  ? 0.4308 0.4617 0.3334 -0.0238 -0.0094 0.0131  477  GLY B CA  
12184 C C   . GLY B 479  ? 0.4731 0.5077 0.3760 -0.0192 -0.0066 0.0091  477  GLY B C   
12185 O O   . GLY B 479  ? 0.4090 0.4510 0.3096 -0.0184 -0.0028 0.0095  477  GLY B O   
12186 N N   . THR B 480  ? 0.5376 0.5667 0.4435 -0.0161 -0.0086 0.0054  478  THR B N   
12187 C CA  . THR B 480  ? 0.6380 0.6682 0.5441 -0.0116 -0.0070 0.0012  478  THR B CA  
12188 C C   . THR B 480  ? 0.6952 0.7230 0.6089 -0.0091 -0.0077 -0.0020 478  THR B C   
12189 O O   . THR B 480  ? 0.6826 0.7118 0.5972 -0.0056 -0.0060 -0.0052 478  THR B O   
12190 C CB  . THR B 480  ? 0.6290 0.6539 0.5281 -0.0102 -0.0094 -0.0006 478  THR B CB  
12191 O OG1 . THR B 480  ? 0.5566 0.5735 0.4568 -0.0113 -0.0141 -0.0005 478  THR B OG1 
12192 C CG2 . THR B 480  ? 0.6067 0.6344 0.4974 -0.0120 -0.0082 0.0022  478  THR B CG2 
12193 N N   . HIS B 481  ? 0.6790 0.7029 0.5977 -0.0108 -0.0102 -0.0011 479  HIS B N   
12194 C CA  . HIS B 481  ? 0.6849 0.7059 0.6104 -0.0087 -0.0112 -0.0039 479  HIS B CA  
12195 C C   . HIS B 481  ? 0.6766 0.7037 0.6067 -0.0066 -0.0075 -0.0053 479  HIS B C   
12196 O O   . HIS B 481  ? 0.6221 0.6547 0.5546 -0.0083 -0.0051 -0.0031 479  HIS B O   
12197 C CB  . HIS B 481  ? 0.6702 0.6872 0.6000 -0.0110 -0.0140 -0.0022 479  HIS B CB  
12198 N N   . GLU B 482  ? 0.6282 0.6541 0.5596 -0.0030 -0.0071 -0.0090 480  GLU B N   
12199 C CA  . GLU B 482  ? 0.6601 0.6911 0.5949 -0.0004 -0.0036 -0.0107 480  GLU B CA  
12200 C C   . GLU B 482  ? 0.6472 0.6807 0.5894 -0.0016 -0.0028 -0.0095 480  GLU B C   
12201 O O   . GLU B 482  ? 0.6544 0.6946 0.5985 -0.0015 0.0003  -0.0084 480  GLU B O   
12202 C CB  . GLU B 482  ? 0.6810 0.7081 0.6159 0.0032  -0.0044 -0.0149 480  GLU B CB  
12203 N N   . THR B 483  ? 0.6290 0.6574 0.5754 -0.0024 -0.0056 -0.0098 481  THR B N   
12204 C CA  . THR B 483  ? 0.6729 0.7030 0.6259 -0.0033 -0.0050 -0.0090 481  THR B CA  
12205 C C   . THR B 483  ? 0.6386 0.6732 0.5912 -0.0067 -0.0039 -0.0052 481  THR B C   
12206 O O   . THR B 483  ? 0.5851 0.6253 0.5412 -0.0069 -0.0014 -0.0043 481  THR B O   
12207 C CB  . THR B 483  ? 0.6167 0.6404 0.5734 -0.0037 -0.0083 -0.0098 481  THR B CB  
12208 O OG1 . THR B 483  ? 0.6592 0.6800 0.6177 -0.0008 -0.0091 -0.0131 481  THR B OG1 
12209 C CG2 . THR B 483  ? 0.5745 0.5998 0.5370 -0.0050 -0.0078 -0.0086 481  THR B CG2 
12210 N N   . LEU B 484  ? 0.6583 0.6901 0.6065 -0.0096 -0.0059 -0.0028 482  LEU B N   
12211 C CA  . LEU B 484  ? 0.6514 0.6867 0.5985 -0.0134 -0.0052 0.0010  482  LEU B CA  
12212 C C   . LEU B 484  ? 0.6435 0.6875 0.5886 -0.0133 -0.0014 0.0022  482  LEU B C   
12213 O O   . LEU B 484  ? 0.5725 0.6222 0.5197 -0.0156 0.0004  0.0048  482  LEU B O   
12214 C CB  . LEU B 484  ? 0.5891 0.6190 0.5311 -0.0162 -0.0083 0.0033  482  LEU B CB  
12215 N N   . LEU B 485  ? 0.6006 0.6458 0.5415 -0.0106 0.0000  0.0004  483  LEU B N   
12216 C CA  . LEU B 485  ? 0.5904 0.6443 0.5296 -0.0096 0.0040  0.0010  483  LEU B CA  
12217 C C   . LEU B 485  ? 0.6337 0.6931 0.5791 -0.0074 0.0067  -0.0001 483  LEU B C   
12218 O O   . LEU B 485  ? 0.6138 0.6814 0.5608 -0.0085 0.0094  0.0020  483  LEU B O   
12219 C CB  . LEU B 485  ? 0.6044 0.6574 0.5376 -0.0065 0.0047  -0.0014 483  LEU B CB  
12220 C CG  . LEU B 485  ? 0.6511 0.7018 0.5769 -0.0088 0.0032  0.0006  483  LEU B CG  
12221 C CD1 . LEU B 485  ? 0.6600 0.7087 0.5798 -0.0054 0.0034  -0.0024 483  LEU B CD1 
12222 C CD2 . LEU B 485  ? 0.6247 0.6832 0.5486 -0.0120 0.0056  0.0047  483  LEU B CD2 
12223 N N   . ALA B 486  ? 0.6056 0.6610 0.5549 -0.0045 0.0058  -0.0034 484  ALA B N   
12224 C CA  . ALA B 486  ? 0.5774 0.6373 0.5325 -0.0024 0.0081  -0.0045 484  ALA B CA  
12225 C C   . ALA B 486  ? 0.5404 0.6035 0.5003 -0.0057 0.0081  -0.0016 484  ALA B C   
12226 O O   . ALA B 486  ? 0.5523 0.6228 0.5153 -0.0054 0.0108  -0.0006 484  ALA B O   
12227 C CB  . ALA B 486  ? 0.5683 0.6222 0.5263 0.0008  0.0067  -0.0082 484  ALA B CB  
12228 N N   . TYR B 487  ? 0.5310 0.5884 0.4911 -0.0089 0.0050  -0.0001 485  TYR B N   
12229 C CA  . TYR B 487  ? 0.5125 0.5720 0.4761 -0.0125 0.0046  0.0027  485  TYR B CA  
12230 C C   . TYR B 487  ? 0.6187 0.6856 0.5800 -0.0156 0.0065  0.0064  485  TYR B C   
12231 O O   . TYR B 487  ? 0.5445 0.6171 0.5093 -0.0175 0.0078  0.0084  485  TYR B O   
12232 C CB  . TYR B 487  ? 0.6372 0.6882 0.6006 -0.0149 0.0008  0.0033  485  TYR B CB  
12233 N N   . LEU B 488  ? 0.5483 0.6154 0.5035 -0.0163 0.0067  0.0074  486  LEU B N   
12234 C CA  . LEU B 488  ? 0.6009 0.6753 0.5534 -0.0195 0.0085  0.0111  486  LEU B CA  
12235 C C   . LEU B 488  ? 0.5511 0.6362 0.5060 -0.0172 0.0128  0.0110  486  LEU B C   
12236 O O   . LEU B 488  ? 0.5261 0.6190 0.4834 -0.0199 0.0144  0.0140  486  LEU B O   
12237 C CB  . LEU B 488  ? 0.5744 0.6462 0.5195 -0.0205 0.0077  0.0120  486  LEU B CB  
12238 C CG  . LEU B 488  ? 0.5482 0.6285 0.4894 -0.0228 0.0103  0.0154  486  LEU B CG  
12239 C CD1 . LEU B 488  ? 0.5932 0.6769 0.5362 -0.0284 0.0098  0.0199  486  LEU B CD1 
12240 C CD2 . LEU B 488  ? 0.5741 0.6500 0.5076 -0.0231 0.0090  0.0156  486  LEU B CD2 
12241 N N   . VAL B 489  ? 0.5388 0.6245 0.4931 -0.0121 0.0145  0.0075  487  VAL B N   
12242 C CA  . VAL B 489  ? 0.5406 0.6360 0.4967 -0.0091 0.0186  0.0070  487  VAL B CA  
12243 C C   . VAL B 489  ? 0.5558 0.6556 0.5192 -0.0092 0.0194  0.0075  487  VAL B C   
12244 O O   . VAL B 489  ? 0.5811 0.6909 0.5469 -0.0093 0.0222  0.0094  487  VAL B O   
12245 C CB  . VAL B 489  ? 0.5614 0.6545 0.5149 -0.0034 0.0197  0.0028  487  VAL B CB  
12246 C CG1 . VAL B 489  ? 0.5587 0.6616 0.5139 0.0003  0.0239  0.0021  487  VAL B CG1 
12247 C CG2 . VAL B 489  ? 0.5202 0.6092 0.4659 -0.0035 0.0188  0.0024  487  VAL B CG2 
12248 N N   . ARG B 490  ? 0.4642 0.5569 0.4313 -0.0091 0.0168  0.0060  488  ARG B N   
12249 C CA  . ARG B 490  ? 0.5437 0.6398 0.5173 -0.0095 0.0172  0.0065  488  ARG B CA  
12250 C C   . ARG B 490  ? 0.6171 0.7178 0.5921 -0.0149 0.0169  0.0108  488  ARG B C   
12251 O O   . ARG B 490  ? 0.5973 0.7062 0.5766 -0.0155 0.0186  0.0124  488  ARG B O   
12252 C CB  . ARG B 490  ? 0.4903 0.5775 0.4669 -0.0084 0.0146  0.0040  488  ARG B CB  
12253 N N   . ARG B 491  ? 0.4904 0.5859 0.4616 -0.0191 0.0143  0.0129  489  ARG B N   
12254 C CA  . ARG B 491  ? 0.5446 0.6437 0.5163 -0.0247 0.0136  0.0172  489  ARG B CA  
12255 C C   . ARG B 491  ? 0.5442 0.6540 0.5139 -0.0261 0.0167  0.0201  489  ARG B C   
12256 O O   . ARG B 491  ? 0.5414 0.6589 0.5139 -0.0294 0.0177  0.0233  489  ARG B O   
12257 C CB  . ARG B 491  ? 0.5360 0.6255 0.5039 -0.0286 0.0098  0.0185  489  ARG B CB  
12258 C CG  . ARG B 491  ? 0.5879 0.6675 0.5580 -0.0275 0.0068  0.0160  489  ARG B CG  
12259 C CD  . ARG B 491  ? 0.5449 0.6168 0.5128 -0.0320 0.0030  0.0181  489  ARG B CD  
12260 N NE  . ARG B 491  ? 0.5461 0.6095 0.5164 -0.0306 0.0005  0.0157  489  ARG B NE  
12261 C CZ  . ARG B 491  ? 0.5617 0.6160 0.5295 -0.0296 -0.0022 0.0141  489  ARG B CZ  
12262 N NH1 . ARG B 491  ? 0.5419 0.5934 0.5043 -0.0302 -0.0031 0.0147  489  ARG B NH1 
12263 N NH2 . ARG B 491  ? 0.5099 0.5582 0.4808 -0.0280 -0.0040 0.0118  489  ARG B NH2 
12264 N N   . LEU B 492  ? 0.5477 0.6583 0.5126 -0.0236 0.0183  0.0190  490  LEU B N   
12265 C CA  . LEU B 492  ? 0.5459 0.6670 0.5085 -0.0244 0.0215  0.0216  490  LEU B CA  
12266 C C   . LEU B 492  ? 0.6072 0.7398 0.5752 -0.0217 0.0251  0.0215  490  LEU B C   
12267 O O   . LEU B 492  ? 0.5766 0.7197 0.5458 -0.0244 0.0272  0.0251  490  LEU B O   
12268 C CB  . LEU B 492  ? 0.6123 0.7311 0.5683 -0.0213 0.0224  0.0196  490  LEU B CB  
12269 C CG  . LEU B 492  ? 0.6060 0.7313 0.5565 -0.0236 0.0244  0.0228  490  LEU B CG  
12270 C CD1 . LEU B 492  ? 0.6047 0.7282 0.5535 -0.0306 0.0219  0.0274  490  LEU B CD1 
12271 C CD2 . LEU B 492  ? 0.6213 0.7415 0.5650 -0.0202 0.0245  0.0201  490  LEU B CD2 
12272 N N   . LEU B 493  ? 0.6014 0.7324 0.5727 -0.0165 0.0258  0.0177  491  LEU B N   
12273 C CA  . LEU B 493  ? 0.5726 0.7137 0.5489 -0.0133 0.0290  0.0173  491  LEU B CA  
12274 C C   . LEU B 493  ? 0.5838 0.7255 0.5669 -0.0149 0.0277  0.0181  491  LEU B C   
12275 O O   . LEU B 493  ? 0.6323 0.7806 0.6200 -0.0117 0.0298  0.0172  491  LEU B O   
12276 C CB  . LEU B 493  ? 0.5396 0.6789 0.5148 -0.0063 0.0308  0.0128  491  LEU B CB  
12277 C CG  . LEU B 493  ? 0.6047 0.7446 0.5729 -0.0041 0.0325  0.0119  491  LEU B CG  
12278 C CD1 . LEU B 493  ? 0.5331 0.6702 0.4999 0.0028  0.0338  0.0071  491  LEU B CD1 
12279 C CD2 . LEU B 493  ? 0.6904 0.8432 0.6578 -0.0058 0.0358  0.0155  491  LEU B CD2 
12280 N N   . GLU B 494  ? 0.6066 0.7413 0.5899 -0.0196 0.0242  0.0196  492  GLU B N   
12281 C CA  . GLU B 494  ? 0.5604 0.6949 0.5493 -0.0217 0.0226  0.0204  492  GLU B CA  
12282 C C   . GLU B 494  ? 0.5847 0.7171 0.5776 -0.0165 0.0231  0.0167  492  GLU B C   
12283 O O   . GLU B 494  ? 0.5819 0.7200 0.5800 -0.0160 0.0239  0.0173  492  GLU B O   
12284 C CB  . GLU B 494  ? 0.5266 0.6730 0.5188 -0.0254 0.0241  0.0246  492  GLU B CB  
12285 C CG  . GLU B 494  ? 0.4988 0.6492 0.4870 -0.0304 0.0244  0.0286  492  GLU B CG  
12286 C CD  . GLU B 494  ? 0.5272 0.6675 0.5120 -0.0359 0.0203  0.0303  492  GLU B CD  
12287 O OE1 . GLU B 494  ? 0.4993 0.6308 0.4856 -0.0362 0.0174  0.0287  492  GLU B OE1 
12288 O OE2 . GLU B 494  ? 0.4860 0.6270 0.4663 -0.0399 0.0200  0.0333  492  GLU B OE2 
12289 N N   . ASN B 495  ? 0.5601 0.6844 0.5504 -0.0126 0.0225  0.0130  493  ASN B N   
12290 C CA  . ASN B 495  ? 0.6219 0.7430 0.6152 -0.0076 0.0228  0.0093  493  ASN B CA  
12291 C C   . ASN B 495  ? 0.6307 0.7618 0.6271 -0.0035 0.0263  0.0089  493  ASN B C   
12292 O O   . ASN B 495  ? 0.6223 0.7529 0.6227 -0.0005 0.0265  0.0071  493  ASN B O   
12293 C CB  . ASN B 495  ? 0.6227 0.7380 0.6198 -0.0094 0.0202  0.0091  493  ASN B CB  
12294 C CG  . ASN B 495  ? 0.6255 0.7294 0.6197 -0.0112 0.0169  0.0081  493  ASN B CG  
12295 O OD1 . ASN B 495  ? 0.6724 0.7731 0.6617 -0.0125 0.0161  0.0085  493  ASN B OD1 
12296 N ND2 . ASN B 495  ? 0.6465 0.7443 0.6435 -0.0112 0.0149  0.0068  493  ASN B ND2 
12297 N N   . GLY B 496  ? 0.6568 0.7970 0.6515 -0.0033 0.0290  0.0107  494  GLY B N   
12298 C CA  . GLY B 496  ? 0.6878 0.8387 0.6856 0.0006  0.0324  0.0106  494  GLY B CA  
12299 C C   . GLY B 496  ? 0.7110 0.8681 0.7155 -0.0008 0.0324  0.0125  494  GLY B C   
12300 O O   . GLY B 496  ? 0.7082 0.8689 0.7162 0.0037  0.0339  0.0110  494  GLY B O   
12301 N N   . ALA B 497  ? 0.6775 0.8357 0.6835 -0.0069 0.0305  0.0159  495  ALA B N   
12302 C CA  . ALA B 497  ? 0.5925 0.7552 0.6044 -0.0088 0.0298  0.0177  495  ALA B CA  
12303 C C   . ALA B 497  ? 0.4809 0.6587 0.4963 -0.0085 0.0328  0.0205  495  ALA B C   
12304 O O   . ALA B 497  ? 0.5182 0.7028 0.5319 -0.0116 0.0340  0.0234  495  ALA B O   
12305 C CB  . ALA B 497  ? 0.4963 0.6538 0.5078 -0.0155 0.0264  0.0202  495  ALA B CB  
12306 N N   . ASN B 498  ? 0.4983 0.6813 0.5187 -0.0048 0.0340  0.0196  496  ASN B N   
12307 C CA  . ASN B 498  ? 0.5424 0.7404 0.5670 -0.0041 0.0368  0.0222  496  ASN B CA  
12308 C C   . ASN B 498  ? 0.4620 0.6669 0.4891 -0.0113 0.0356  0.0270  496  ASN B C   
12309 O O   . ASN B 498  ? 0.4877 0.7055 0.5168 -0.0124 0.0380  0.0300  496  ASN B O   
12310 C CB  . ASN B 498  ? 0.5691 0.7702 0.5988 0.0009  0.0376  0.0205  496  ASN B CB  
12311 N N   . SER B 499  ? 0.4426 0.6391 0.4694 -0.0163 0.0320  0.0278  497  SER B N   
12312 C CA  . SER B 499  ? 0.4615 0.6627 0.4899 -0.0236 0.0303  0.0322  497  SER B CA  
12313 C C   . SER B 499  ? 0.3835 0.5839 0.4069 -0.0284 0.0300  0.0347  497  SER B C   
12314 O O   . SER B 499  ? 0.3640 0.5687 0.3883 -0.0348 0.0287  0.0387  497  SER B O   
12315 C CB  . SER B 499  ? 0.4120 0.6038 0.4414 -0.0269 0.0264  0.0319  497  SER B CB  
12316 O OG  . SER B 499  ? 0.4028 0.5806 0.4269 -0.0276 0.0241  0.0297  497  SER B OG  
12317 N N   . SER B 500  ? 0.3781 0.5727 0.3961 -0.0257 0.0309  0.0325  498  SER B N   
12318 C CA  . SER B 500  ? 0.3720 0.5649 0.3847 -0.0300 0.0305  0.0347  498  SER B CA  
12319 C C   . SER B 500  ? 0.4272 0.6349 0.4406 -0.0309 0.0340  0.0380  498  SER B C   
12320 O O   . SER B 500  ? 0.4165 0.6332 0.4321 -0.0255 0.0375  0.0368  498  SER B O   
12321 C CB  . SER B 500  ? 0.3706 0.5526 0.3772 -0.0266 0.0303  0.0312  498  SER B CB  
12322 N N   . PHE B 501  ? 0.3783 0.5886 0.3898 -0.0378 0.0329  0.0423  499  PHE B N   
12323 C CA  . PHE B 501  ? 0.4385 0.6624 0.4498 -0.0393 0.0362  0.0458  499  PHE B CA  
12324 C C   . PHE B 501  ? 0.4485 0.6729 0.4550 -0.0339 0.0394  0.0433  499  PHE B C   
12325 O O   . PHE B 501  ? 0.5002 0.7374 0.5080 -0.0311 0.0434  0.0443  499  PHE B O   
12326 C CB  . PHE B 501  ? 0.4046 0.6282 0.4134 -0.0480 0.0340  0.0507  499  PHE B CB  
12327 C CG  . PHE B 501  ? 0.4026 0.6403 0.4110 -0.0506 0.0372  0.0549  499  PHE B CG  
12328 C CD1 . PHE B 501  ? 0.4220 0.6592 0.4241 -0.0492 0.0393  0.0547  499  PHE B CD1 
12329 C CD2 . PHE B 501  ? 0.3236 0.5750 0.3377 -0.0546 0.0381  0.0592  499  PHE B CD2 
12330 C CE1 . PHE B 501  ? 0.4352 0.6857 0.4367 -0.0516 0.0424  0.0587  499  PHE B CE1 
12331 C CE2 . PHE B 501  ? 0.4328 0.6980 0.4468 -0.0571 0.0412  0.0633  499  PHE B CE2 
12332 C CZ  . PHE B 501  ? 0.3673 0.6321 0.3750 -0.0556 0.0434  0.0631  499  PHE B CZ  
12333 N N   . VAL B 502  ? 0.4800 0.6907 0.4808 -0.0321 0.0377  0.0401  500  VAL B N   
12334 C CA  . VAL B 502  ? 0.5618 0.7714 0.5571 -0.0272 0.0402  0.0376  500  VAL B CA  
12335 C C   . VAL B 502  ? 0.5402 0.7538 0.5382 -0.0190 0.0431  0.0336  500  VAL B C   
12336 O O   . VAL B 502  ? 0.6053 0.8235 0.6001 -0.0145 0.0464  0.0322  500  VAL B O   
12337 C CB  . VAL B 502  ? 0.4844 0.6780 0.4733 -0.0278 0.0370  0.0352  500  VAL B CB  
12338 N N   . HIS B 503  ? 0.4817 0.6933 0.4850 -0.0167 0.0420  0.0318  501  HIS B N   
12339 C CA  . HIS B 503  ? 0.4523 0.6685 0.4586 -0.0092 0.0447  0.0286  501  HIS B CA  
12340 C C   . HIS B 503  ? 0.5564 0.7893 0.5687 -0.0086 0.0477  0.0314  501  HIS B C   
12341 O O   . HIS B 503  ? 0.5236 0.7639 0.5367 -0.0023 0.0512  0.0297  501  HIS B O   
12342 C CB  . HIS B 503  ? 0.5185 0.7245 0.5274 -0.0067 0.0421  0.0252  501  HIS B CB  
12343 C CG  . HIS B 503  ? 0.5419 0.7524 0.5545 0.0005  0.0444  0.0224  501  HIS B CG  
12344 N ND1 . HIS B 503  ? 0.5366 0.7584 0.5559 0.0011  0.0457  0.0243  501  HIS B ND1 
12345 C CD2 . HIS B 503  ? 0.5728 0.7776 0.5832 0.0073  0.0454  0.0179  501  HIS B CD2 
12346 C CE1 . HIS B 503  ? 0.5708 0.7935 0.5917 0.0082  0.0475  0.0211  501  HIS B CE1 
12347 N NE2 . HIS B 503  ? 0.5968 0.8090 0.6122 0.0120  0.0473  0.0172  501  HIS B NE2 
12348 N N   . ARG B 504  ? 0.4817 0.7208 0.4982 -0.0150 0.0464  0.0358  502  ARG B N   
12349 C CA  . ARG B 504  ? 0.4481 0.7033 0.4712 -0.0149 0.0487  0.0387  502  ARG B CA  
12350 C C   . ARG B 504  ? 0.4682 0.7371 0.4902 -0.0156 0.0525  0.0418  502  ARG B C   
12351 O O   . ARG B 504  ? 0.4913 0.7742 0.5177 -0.0121 0.0559  0.0426  502  ARG B O   
12352 C CB  . ARG B 504  ? 0.3805 0.6369 0.4084 -0.0218 0.0455  0.0422  502  ARG B CB  
12353 C CG  . ARG B 504  ? 0.4091 0.6566 0.4402 -0.0201 0.0427  0.0395  502  ARG B CG  
12354 C CD  . ARG B 504  ? 0.3856 0.6287 0.4183 -0.0276 0.0386  0.0422  502  ARG B CD  
12355 N NE  . ARG B 504  ? 0.3585 0.6154 0.3960 -0.0327 0.0390  0.0472  502  ARG B NE  
12356 C CZ  . ARG B 504  ? 0.3722 0.6390 0.4166 -0.0316 0.0396  0.0483  502  ARG B CZ  
12357 N NH1 . ARG B 504  ? 0.4220 0.6869 0.4692 -0.0252 0.0400  0.0448  502  ARG B NH1 
12358 N NH2 . ARG B 504  ? 0.3201 0.5991 0.3686 -0.0372 0.0395  0.0532  502  ARG B NH2 
12359 N N   . ILE B 505  ? 0.4946 0.7602 0.5107 -0.0201 0.0521  0.0436  503  ILE B N   
12360 C CA  . ILE B 505  ? 0.4573 0.7357 0.4715 -0.0209 0.0558  0.0467  503  ILE B CA  
12361 C C   . ILE B 505  ? 0.4660 0.7484 0.4778 -0.0121 0.0601  0.0430  503  ILE B C   
12362 O O   . ILE B 505  ? 0.4918 0.7883 0.5041 -0.0107 0.0641  0.0450  503  ILE B O   
12363 C CB  . ILE B 505  ? 0.4923 0.7646 0.4998 -0.0275 0.0542  0.0493  503  ILE B CB  
12364 N N   . ASN B 506  ? 0.4581 0.7284 0.4671 -0.0062 0.0592  0.0376  504  ASN B N   
12365 C CA  . ASN B 506  ? 0.5881 0.8599 0.5943 0.0025  0.0626  0.0335  504  ASN B CA  
12366 C C   . ASN B 506  ? 0.5655 0.8398 0.5774 0.0090  0.0634  0.0307  504  ASN B C   
12367 O O   . ASN B 506  ? 0.5814 0.8528 0.5906 0.0166  0.0653  0.0264  504  ASN B O   
12368 C CB  . ASN B 506  ? 0.5825 0.8384 0.5805 0.0045  0.0609  0.0295  504  ASN B CB  
12369 N N   . ASP B 507  ? 0.5034 0.7825 0.5228 0.0062  0.0619  0.0330  505  ASP B N   
12370 C CA  . ASP B 507  ? 0.5296 0.8126 0.5547 0.0122  0.0627  0.0310  505  ASP B CA  
12371 C C   . ASP B 507  ? 0.6082 0.9084 0.6387 0.0132  0.0656  0.0341  505  ASP B C   
12372 O O   . ASP B 507  ? 0.5562 0.8630 0.5909 0.0067  0.0642  0.0386  505  ASP B O   
12373 C CB  . ASP B 507  ? 0.6000 0.8753 0.6296 0.0090  0.0586  0.0310  505  ASP B CB  
12374 C CG  . ASP B 507  ? 0.6028 0.8769 0.6363 0.0158  0.0588  0.0278  505  ASP B CG  
12375 O OD1 . ASP B 507  ? 0.6507 0.9365 0.6873 0.0213  0.0621  0.0277  505  ASP B OD1 
12376 O OD2 . ASP B 507  ? 0.6943 0.9559 0.7278 0.0158  0.0556  0.0255  505  ASP B OD2 
12377 N N   . PRO B 508  ? 0.6456 0.9490 0.6754 0.0210  0.0682  0.0315  506  PRO B N   
12378 C CA  . PRO B 508  ? 0.6085 0.9242 0.6428 0.0219  0.0695  0.0341  506  PRO B CA  
12379 C C   . PRO B 508  ? 0.6288 0.9496 0.6714 0.0207  0.0675  0.0360  506  PRO B C   
12380 O O   . PRO B 508  ? 0.6377 0.9691 0.6846 0.0182  0.0676  0.0396  506  PRO B O   
12381 C CB  . PRO B 508  ? 0.6558 0.9713 0.6868 0.0313  0.0724  0.0300  506  PRO B CB  
12382 C CG  . PRO B 508  ? 0.6741 0.9779 0.6973 0.0336  0.0728  0.0261  506  PRO B CG  
12383 C CD  . PRO B 508  ? 0.6038 0.8996 0.6280 0.0289  0.0699  0.0262  506  PRO B CD  
12384 N N   . LYS B 509  ? 0.6056 0.9191 0.6503 0.0225  0.0657  0.0337  507  LYS B N   
12385 C CA  . LYS B 509  ? 0.6098 0.9274 0.6619 0.0212  0.0635  0.0355  507  LYS B CA  
12386 C C   . LYS B 509  ? 0.6492 0.9704 0.7043 0.0115  0.0609  0.0403  507  LYS B C   
12387 O O   . LYS B 509  ? 0.6430 0.9706 0.7041 0.0094  0.0593  0.0429  507  LYS B O   
12388 C CB  . LYS B 509  ? 0.6182 0.9264 0.6713 0.0251  0.0621  0.0319  507  LYS B CB  
12389 N N   . VAL B 510  ? 0.6270 0.9439 0.6779 0.0054  0.0603  0.0417  508  VAL B N   
12390 C CA  . VAL B 510  ? 0.5850 0.9031 0.6378 -0.0041 0.0574  0.0461  508  VAL B CA  
12391 C C   . VAL B 510  ? 0.5335 0.8611 0.5858 -0.0081 0.0584  0.0502  508  VAL B C   
12392 O O   . VAL B 510  ? 0.5462 0.8736 0.5931 -0.0075 0.0606  0.0499  508  VAL B O   
12393 C CB  . VAL B 510  ? 0.5599 0.8671 0.6081 -0.0086 0.0558  0.0455  508  VAL B CB  
12394 C CG1 . VAL B 510  ? 0.5464 0.8535 0.5964 -0.0184 0.0524  0.0499  508  VAL B CG1 
12395 C CG2 . VAL B 510  ? 0.5820 0.8766 0.6295 -0.0037 0.0543  0.0407  508  VAL B CG2 
12396 N N   . SER B 511  ? 0.5366 0.8725 0.5944 -0.0124 0.0568  0.0540  509  SER B N   
12397 C CA  . SER B 511  ? 0.4950 0.8410 0.5532 -0.0162 0.0575  0.0580  509  SER B CA  
12398 C C   . SER B 511  ? 0.5202 0.8627 0.5752 -0.0257 0.0553  0.0616  509  SER B C   
12399 O O   . SER B 511  ? 0.5345 0.8676 0.5882 -0.0301 0.0526  0.0615  509  SER B O   
12400 C CB  . SER B 511  ? 0.5069 0.8633 0.5723 -0.0168 0.0565  0.0607  509  SER B CB  
12401 O OG  . SER B 511  ? 0.5165 0.8694 0.5850 -0.0230 0.0525  0.0626  509  SER B OG  
12402 N N   . ILE B 512  ? 0.4541 0.8042 0.5079 -0.0291 0.0564  0.0650  510  ILE B N   
12403 C CA  . ILE B 512  ? 0.5243 0.8713 0.5750 -0.0384 0.0540  0.0689  510  ILE B CA  
12404 C C   . ILE B 512  ? 0.4897 0.8369 0.5450 -0.0454 0.0498  0.0721  510  ILE B C   
12405 O O   . ILE B 512  ? 0.4363 0.7756 0.4889 -0.0526 0.0467  0.0739  510  ILE B O   
12406 C CB  . ILE B 512  ? 0.3885 0.7439 0.4369 -0.0403 0.0561  0.0719  510  ILE B CB  
12407 N N   . ASP B 513  ? 0.4450 0.8006 0.5068 -0.0434 0.0494  0.0727  511  ASP B N   
12408 C CA  . ASP B 513  ? 0.4067 0.7622 0.4726 -0.0496 0.0453  0.0755  511  ASP B CA  
12409 C C   . ASP B 513  ? 0.4325 0.7756 0.4975 -0.0505 0.0427  0.0730  511  ASP B C   
12410 O O   . ASP B 513  ? 0.4526 0.7901 0.5172 -0.0580 0.0389  0.0753  511  ASP B O   
12411 C CB  . ASP B 513  ? 0.4629 0.8296 0.5357 -0.0463 0.0456  0.0762  511  ASP B CB  
12412 C CG  . ASP B 513  ? 0.5388 0.9178 0.6136 -0.0502 0.0459  0.0808  511  ASP B CG  
12413 O OD1 . ASP B 513  ? 0.5877 0.9654 0.6603 -0.0584 0.0436  0.0844  511  ASP B OD1 
12414 O OD2 . ASP B 513  ? 0.6510 1.0409 0.7295 -0.0449 0.0484  0.0807  511  ASP B OD2 
12415 N N   . GLU B 514  ? 0.3679 0.7063 0.4326 -0.0430 0.0446  0.0684  512  GLU B N   
12416 C CA  . GLU B 514  ? 0.4357 0.7624 0.4993 -0.0435 0.0425  0.0659  512  GLU B CA  
12417 C C   . GLU B 514  ? 0.4598 0.7767 0.5171 -0.0494 0.0412  0.0667  512  GLU B C   
12418 O O   . GLU B 514  ? 0.3795 0.6884 0.4362 -0.0550 0.0378  0.0675  512  GLU B O   
12419 C CB  . GLU B 514  ? 0.4315 0.7551 0.4951 -0.0341 0.0451  0.0608  512  GLU B CB  
12420 C CG  . GLU B 514  ? 0.5287 0.8573 0.5984 -0.0289 0.0450  0.0595  512  GLU B CG  
12421 C CD  . GLU B 514  ? 0.5839 0.9119 0.6531 -0.0188 0.0483  0.0549  512  GLU B CD  
12422 O OE1 . GLU B 514  ? 0.6190 0.9537 0.6873 -0.0145 0.0514  0.0546  512  GLU B OE1 
12423 O OE2 . GLU B 514  ? 0.6610 0.9815 0.7305 -0.0152 0.0478  0.0516  512  GLU B OE2 
12424 N N   . LEU B 515  ? 0.3960 0.7134 0.4483 -0.0483 0.0439  0.0666  513  LEU B N   
12425 C CA  . LEU B 515  ? 0.3947 0.7024 0.4404 -0.0532 0.0428  0.0672  513  LEU B CA  
12426 C C   . LEU B 515  ? 0.4004 0.7070 0.4451 -0.0632 0.0392  0.0721  513  LEU B C   
12427 O O   . LEU B 515  ? 0.3858 0.6821 0.4260 -0.0685 0.0368  0.0728  513  LEU B O   
12428 C CB  . LEU B 515  ? 0.4008 0.7095 0.4410 -0.0493 0.0465  0.0659  513  LEU B CB  
12429 C CG  . LEU B 515  ? 0.4201 0.7272 0.4591 -0.0396 0.0499  0.0607  513  LEU B CG  
12430 C CD1 . LEU B 515  ? 0.4498 0.7603 0.4837 -0.0365 0.0534  0.0603  513  LEU B CD1 
12431 C CD2 . LEU B 515  ? 0.4111 0.7004 0.4460 -0.0382 0.0471  0.0565  513  LEU B CD2 
12432 N N   . ILE B 516  ? 0.3529 0.6697 0.4014 -0.0658 0.0387  0.0755  514  ILE B N   
12433 C CA  . ILE B 516  ? 0.3344 0.6503 0.3818 -0.0753 0.0351  0.0803  514  ILE B CA  
12434 C C   . ILE B 516  ? 0.2980 0.6121 0.3496 -0.0797 0.0310  0.0815  514  ILE B C   
12435 O O   . ILE B 516  ? 0.3893 0.7025 0.4401 -0.0875 0.0276  0.0854  514  ILE B O   
12436 C CB  . ILE B 516  ? 0.4360 0.7638 0.4841 -0.0769 0.0367  0.0838  514  ILE B CB  
12437 C CG1 . ILE B 516  ? 0.4027 0.7432 0.4581 -0.0727 0.0380  0.0839  514  ILE B CG1 
12438 C CG2 . ILE B 516  ? 0.3681 0.6968 0.4111 -0.0733 0.0406  0.0827  514  ILE B CG2 
12439 C CD1 . ILE B 516  ? 0.4265 0.7794 0.4836 -0.0752 0.0390  0.0879  514  ILE B CD1 
12440 N N   . ALA B 517  ? 0.3414 0.6542 0.3968 -0.0749 0.0310  0.0784  515  ALA B N   
12441 C CA  . ALA B 517  ? 0.3933 0.7028 0.4520 -0.0788 0.0268  0.0792  515  ALA B CA  
12442 C C   . ALA B 517  ? 0.3925 0.6892 0.4463 -0.0868 0.0228  0.0806  515  ALA B C   
12443 O O   . ALA B 517  ? 0.3889 0.6762 0.4379 -0.0864 0.0232  0.0788  515  ALA B O   
12444 C CB  . ALA B 517  ? 0.3573 0.6652 0.4198 -0.0720 0.0277  0.0750  515  ALA B CB  
12445 N N   . ASP B 518  ? 0.3509 0.6470 0.4055 -0.0939 0.0187  0.0839  516  ASP B N   
12446 C CA  . ASP B 518  ? 0.3255 0.6089 0.3751 -0.1017 0.0143  0.0855  516  ASP B CA  
12447 C C   . ASP B 518  ? 0.3206 0.5940 0.3708 -0.1008 0.0121  0.0823  516  ASP B C   
12448 O O   . ASP B 518  ? 0.3332 0.6088 0.3877 -0.1006 0.0102  0.0820  516  ASP B O   
12449 C CB  . ASP B 518  ? 0.3083 0.5944 0.3583 -0.1095 0.0105  0.0899  516  ASP B CB  
12450 C CG  . ASP B 518  ? 0.3666 0.6388 0.4103 -0.1177 0.0058  0.0918  516  ASP B CG  
12451 O OD1 . ASP B 518  ? 0.3588 0.6190 0.3985 -0.1175 0.0050  0.0894  516  ASP B OD1 
12452 O OD2 . ASP B 518  ? 0.4359 0.7091 0.4785 -0.1244 0.0026  0.0956  516  ASP B OD2 
12453 N N   . PRO B 519  ? 0.3023 0.5619 0.3470 -0.0991 0.0116  0.0792  517  PRO B N   
12454 C CA  . PRO B 519  ? 0.3296 0.5753 0.3731 -0.0960 0.0088  0.0748  517  PRO B CA  
12455 C C   . PRO B 519  ? 0.3164 0.5566 0.3598 -0.1031 0.0036  0.0768  517  PRO B C   
12456 O O   . PRO B 519  ? 0.2997 0.5362 0.3455 -0.1009 0.0019  0.0744  517  PRO B O   
12457 C CB  . PRO B 519  ? 0.3369 0.5668 0.3728 -0.0934 0.0084  0.0714  517  PRO B CB  
12458 C CG  . PRO B 519  ? 0.3268 0.5589 0.3588 -0.0984 0.0089  0.0751  517  PRO B CG  
12459 C CD  . PRO B 519  ? 0.3303 0.5827 0.3681 -0.0990 0.0126  0.0789  517  PRO B CD  
12460 N N   . VAL B 520  ? 0.3197 0.5594 0.3604 -0.1116 0.0011  0.0812  518  VAL B N   
12461 C CA  . VAL B 520  ? 0.3313 0.5645 0.3709 -0.1189 -0.0042 0.0832  518  VAL B CA  
12462 C C   . VAL B 520  ? 0.3355 0.5809 0.3824 -0.1192 -0.0045 0.0846  518  VAL B C   
12463 O O   . VAL B 520  ? 0.3450 0.5853 0.3930 -0.1201 -0.0076 0.0833  518  VAL B O   
12464 C CB  . VAL B 520  ? 0.3472 0.5779 0.3822 -0.1279 -0.0068 0.0880  518  VAL B CB  
12465 C CG1 . VAL B 520  ? 0.3955 0.6159 0.4278 -0.1347 -0.0128 0.0891  518  VAL B CG1 
12466 C CG2 . VAL B 520  ? 0.2998 0.5190 0.3274 -0.1265 -0.0062 0.0865  518  VAL B CG2 
12467 N N   . GLU B 521  ? 0.3369 0.5965 0.3876 -0.1170 -0.0017 0.0865  519  GLU B N   
12468 C CA  . GLU B 521  ? 0.3440 0.6136 0.4005 -0.1161 -0.0023 0.0875  519  GLU B CA  
12469 C C   . GLU B 521  ? 0.3445 0.6176 0.4061 -0.1084 0.0000  0.0837  519  GLU B C   
12470 O O   . GLU B 521  ? 0.3637 0.6390 0.4288 -0.1083 -0.0020 0.0836  519  GLU B O   
12471 C CB  . GLU B 521  ? 0.3440 0.6277 0.4030 -0.1162 0.0000  0.0909  519  GLU B CB  
12472 C CG  . GLU B 521  ? 0.3341 0.6151 0.3884 -0.1243 -0.0027 0.0950  519  GLU B CG  
12473 C CD  . GLU B 521  ? 0.4273 0.6991 0.4790 -0.1318 -0.0087 0.0967  519  GLU B CD  
12474 O OE1 . GLU B 521  ? 0.4308 0.7043 0.4861 -0.1311 -0.0105 0.0960  519  GLU B OE1 
12475 O OE2 . GLU B 521  ? 0.4891 0.7515 0.5348 -0.1382 -0.0118 0.0987  519  GLU B OE2 
12476 N N   . VAL B 522  ? 0.3187 0.5921 0.3805 -0.1018 0.0041  0.0807  520  VAL B N   
12477 C CA  . VAL B 522  ? 0.3167 0.5920 0.3828 -0.0944 0.0060  0.0769  520  VAL B CA  
12478 C C   . VAL B 522  ? 0.3646 0.6255 0.4282 -0.0955 0.0021  0.0742  520  VAL B C   
12479 O O   . VAL B 522  ? 0.3446 0.6073 0.4120 -0.0932 0.0011  0.0729  520  VAL B O   
12480 C CB  . VAL B 522  ? 0.3299 0.6064 0.3954 -0.0868 0.0109  0.0738  520  VAL B CB  
12481 C CG1 . VAL B 522  ? 0.3656 0.6401 0.4338 -0.0784 0.0121  0.0693  520  VAL B CG1 
12482 C CG2 . VAL B 522  ? 0.4213 0.7105 0.4883 -0.0846 0.0146  0.0758  520  VAL B CG2 
12483 N N   . VAL B 523  ? 0.2867 0.5315 0.3429 -0.0984 -0.0005 0.0730  521  VAL B N   
12484 C CA  . VAL B 523  ? 0.3214 0.5508 0.3740 -0.0986 -0.0045 0.0700  521  VAL B CA  
12485 C C   . VAL B 523  ? 0.3488 0.5806 0.4033 -0.1055 -0.0087 0.0730  521  VAL B C   
12486 O O   . VAL B 523  ? 0.3398 0.5677 0.3955 -0.1039 -0.0106 0.0709  521  VAL B O   
12487 C CB  . VAL B 523  ? 0.3329 0.5449 0.3772 -0.1000 -0.0064 0.0681  521  VAL B CB  
12488 C CG1 . VAL B 523  ? 0.3011 0.4980 0.3416 -0.1013 -0.0108 0.0656  521  VAL B CG1 
12489 C CG2 . VAL B 523  ? 0.2774 0.4860 0.3201 -0.0923 -0.0027 0.0643  521  VAL B CG2 
12490 N N   . ARG B 524  ? 0.3126 0.5509 0.3674 -0.1135 -0.0102 0.0780  522  ARG B N   
12491 C CA  . ARG B 524  ? 0.3280 0.5667 0.3834 -0.1202 -0.0147 0.0807  522  ARG B CA  
12492 C C   . ARG B 524  ? 0.3617 0.6108 0.4235 -0.1163 -0.0140 0.0803  522  ARG B C   
12493 O O   . ARG B 524  ? 0.4014 0.6469 0.4631 -0.1192 -0.0179 0.0805  522  ARG B O   
12494 C CB  . ARG B 524  ? 0.3541 0.5958 0.4069 -0.1264 -0.0160 0.0852  522  ARG B CB  
12495 C CG  . ARG B 524  ? 0.4070 0.6450 0.4580 -0.1332 -0.0213 0.0877  522  ARG B CG  
12496 C CD  . ARG B 524  ? 0.4335 0.6793 0.4841 -0.1380 -0.0219 0.0924  522  ARG B CD  
12497 N NE  . ARG B 524  ? 0.4178 0.6606 0.4640 -0.1401 -0.0206 0.0938  522  ARG B NE  
12498 C CZ  . ARG B 524  ? 0.4524 0.6813 0.4915 -0.1457 -0.0241 0.0944  522  ARG B CZ  
12499 N NH1 . ARG B 524  ? 0.4479 0.6639 0.4830 -0.1496 -0.0290 0.0935  522  ARG B NH1 
12500 N NH2 . ARG B 524  ? 0.4302 0.6577 0.4657 -0.1472 -0.0226 0.0959  522  ARG B NH2 
12501 N N   . ALA B 525  ? 0.3728 0.6340 0.4397 -0.1095 -0.0093 0.0797  523  ALA B N   
12502 C CA  . ALA B 525  ? 0.3687 0.6407 0.4417 -0.1054 -0.0084 0.0797  523  ALA B CA  
12503 C C   . ALA B 525  ? 0.3463 0.6153 0.4219 -0.0995 -0.0078 0.0758  523  ALA B C   
12504 O O   . ALA B 525  ? 0.3804 0.6566 0.4606 -0.0962 -0.0077 0.0756  523  ALA B O   
12505 C CB  . ALA B 525  ? 0.3342 0.6204 0.4112 -0.1006 -0.0038 0.0809  523  ALA B CB  
12506 N N   . MET B 526  ? 0.3616 0.6186 0.4333 -0.0974 -0.0076 0.0723  524  MET B N   
12507 C CA  . MET B 526  ? 0.3691 0.6197 0.4410 -0.0902 -0.0071 0.0677  524  MET B CA  
12508 C C   . MET B 526  ? 0.3792 0.6238 0.4505 -0.0937 -0.0118 0.0676  524  MET B C   
12509 O O   . MET B 526  ? 0.3924 0.6316 0.4603 -0.1013 -0.0158 0.0697  524  MET B O   
12510 C CB  . MET B 526  ? 0.3259 0.5613 0.3916 -0.0857 -0.0060 0.0633  524  MET B CB  
12511 C CG  . MET B 526  ? 0.3769 0.6186 0.4440 -0.0798 -0.0010 0.0623  524  MET B CG  
12512 S SD  . MET B 526  ? 0.4930 0.7183 0.5521 -0.0774 -0.0002 0.0588  524  MET B SD  
12513 C CE  . MET B 526  ? 0.5093 0.7281 0.5690 -0.0677 0.0018  0.0532  524  MET B CE  
12514 N N   . PRO B 527  ? 0.3877 0.6334 0.4619 -0.0883 -0.0114 0.0653  525  PRO B N   
12515 C CA  . PRO B 527  ? 0.4034 0.6442 0.4768 -0.0914 -0.0157 0.0652  525  PRO B CA  
12516 C C   . PRO B 527  ? 0.3802 0.6016 0.4456 -0.0932 -0.0189 0.0622  525  PRO B C   
12517 O O   . PRO B 527  ? 0.3323 0.5483 0.3952 -0.0984 -0.0232 0.0630  525  PRO B O   
12518 C CB  . PRO B 527  ? 0.3879 0.6342 0.4661 -0.0840 -0.0138 0.0631  525  PRO B CB  
12519 C CG  . PRO B 527  ? 0.3933 0.6379 0.4712 -0.0764 -0.0092 0.0600  525  PRO B CG  
12520 C CD  . PRO B 527  ? 0.4242 0.6745 0.5019 -0.0791 -0.0072 0.0625  525  PRO B CD  
12521 N N   . VAL B 528  ? 0.3102 0.5210 0.3712 -0.0889 -0.0169 0.0588  526  VAL B N   
12522 C CA  . VAL B 528  ? 0.3215 0.5143 0.3748 -0.0903 -0.0196 0.0561  526  VAL B CA  
12523 C C   . VAL B 528  ? 0.2990 0.4873 0.3486 -0.0912 -0.0182 0.0562  526  VAL B C   
12524 O O   . VAL B 528  ? 0.3241 0.5117 0.3738 -0.0853 -0.0146 0.0539  526  VAL B O   
12525 C CB  . VAL B 528  ? 0.3359 0.5193 0.3875 -0.0835 -0.0189 0.0513  526  VAL B CB  
12526 C CG1 . VAL B 528  ? 0.3567 0.5225 0.4005 -0.0845 -0.0210 0.0486  526  VAL B CG1 
12527 C CG2 . VAL B 528  ? 0.3565 0.5430 0.4107 -0.0833 -0.0208 0.0513  526  VAL B CG2 
12528 N N   . VAL B 529  ? 0.3103 0.4950 0.3563 -0.0986 -0.0211 0.0590  527  VAL B N   
12529 C CA  . VAL B 529  ? 0.2709 0.4518 0.3132 -0.1001 -0.0201 0.0597  527  VAL B CA  
12530 C C   . VAL B 529  ? 0.3077 0.4725 0.3441 -0.0958 -0.0200 0.0552  527  VAL B C   
12531 O O   . VAL B 529  ? 0.3001 0.4523 0.3320 -0.0967 -0.0232 0.0531  527  VAL B O   
12532 C CB  . VAL B 529  ? 0.3008 0.4805 0.3402 -0.1095 -0.0237 0.0638  527  VAL B CB  
12533 C CG1 . VAL B 529  ? 0.2945 0.4663 0.3284 -0.1109 -0.0233 0.0641  527  VAL B CG1 
12534 C CG2 . VAL B 529  ? 0.3511 0.5488 0.3971 -0.1135 -0.0230 0.0687  527  VAL B CG2 
12535 N N   . GLY B 530  ? 0.2425 0.4079 0.2789 -0.0910 -0.0164 0.0537  528  GLY B N   
12536 C CA  . GLY B 530  ? 0.2362 0.3877 0.2675 -0.0869 -0.0162 0.0497  528  GLY B CA  
12537 C C   . GLY B 530  ? 0.2609 0.4091 0.2938 -0.0797 -0.0146 0.0454  528  GLY B C   
12538 O O   . GLY B 530  ? 0.2594 0.3952 0.2881 -0.0769 -0.0151 0.0421  528  GLY B O   
12539 N N   . ALA B 531  ? 0.2126 0.3714 0.2514 -0.0768 -0.0129 0.0456  529  ALA B N   
12540 C CA  . ALA B 531  ? 0.2389 0.3944 0.2790 -0.0700 -0.0114 0.0418  529  ALA B CA  
12541 C C   . ALA B 531  ? 0.2467 0.3988 0.2857 -0.0642 -0.0081 0.0390  529  ALA B C   
12542 O O   . ALA B 531  ? 0.2504 0.4096 0.2909 -0.0633 -0.0055 0.0402  529  ALA B O   
12543 C CB  . ALA B 531  ? 0.2830 0.4511 0.3296 -0.0677 -0.0100 0.0428  529  ALA B CB  
12544 N N   . LYS B 532  ? 0.2334 0.3745 0.2698 -0.0603 -0.0084 0.0352  530  LYS B N   
12545 C CA  . LYS B 532  ? 0.2712 0.4080 0.3066 -0.0546 -0.0057 0.0322  530  LYS B CA  
12546 C C   . LYS B 532  ? 0.3086 0.4565 0.3492 -0.0495 -0.0020 0.0320  530  LYS B C   
12547 O O   . LYS B 532  ? 0.2581 0.4145 0.3031 -0.0487 -0.0016 0.0331  530  LYS B O   
12548 C CB  . LYS B 532  ? 0.2703 0.3954 0.3032 -0.0515 -0.0068 0.0285  530  LYS B CB  
12549 C CG  . LYS B 532  ? 0.3480 0.4694 0.3810 -0.0451 -0.0041 0.0251  530  LYS B CG  
12550 C CD  . LYS B 532  ? 0.2756 0.3873 0.3070 -0.0423 -0.0051 0.0219  530  LYS B CD  
12551 C CE  . LYS B 532  ? 0.3176 0.4340 0.3526 -0.0401 -0.0047 0.0217  530  LYS B CE  
12552 N NZ  . LYS B 532  ? 0.2763 0.4006 0.3156 -0.0350 -0.0014 0.0211  530  LYS B NZ  
12553 N N   . HIS B 533  ? 0.2332 0.3807 0.2729 -0.0461 0.0006  0.0307  531  HIS B N   
12554 C CA  . HIS B 533  ? 0.2534 0.4093 0.2970 -0.0405 0.0042  0.0299  531  HIS B CA  
12555 C C   . HIS B 533  ? 0.2609 0.4156 0.3071 -0.0359 0.0045  0.0276  531  HIS B C   
12556 O O   . HIS B 533  ? 0.2671 0.4113 0.3108 -0.0347 0.0032  0.0250  531  HIS B O   
12557 C CB  . HIS B 533  ? 0.2704 0.4223 0.3113 -0.0372 0.0063  0.0278  531  HIS B CB  
12558 C CG  . HIS B 533  ? 0.2975 0.4589 0.3414 -0.0324 0.0099  0.0276  531  HIS B CG  
12559 N ND1 . HIS B 533  ? 0.2858 0.4493 0.3327 -0.0267 0.0116  0.0256  531  HIS B ND1 
12560 C CD2 . HIS B 533  ? 0.3247 0.4940 0.3688 -0.0323 0.0122  0.0292  531  HIS B CD2 
12561 C CE1 . HIS B 533  ? 0.3933 0.5652 0.4421 -0.0230 0.0147  0.0257  531  HIS B CE1 
12562 N NE2 . HIS B 533  ? 0.3431 0.5189 0.3902 -0.0263 0.0152  0.0279  531  HIS B NE2 
12563 N N   . ASP B 534  ? 0.2696 0.4352 0.3207 -0.0334 0.0062  0.0287  532  ASP B N   
12564 C CA  . ASP B 534  ? 0.2888 0.4542 0.3424 -0.0296 0.0062  0.0271  532  ASP B CA  
12565 C C   . ASP B 534  ? 0.2380 0.3963 0.2904 -0.0235 0.0080  0.0234  532  ASP B C   
12566 O O   . ASP B 534  ? 0.3199 0.4744 0.3730 -0.0208 0.0076  0.0218  532  ASP B O   
12567 C CB  . ASP B 534  ? 0.2990 0.4783 0.3582 -0.0280 0.0076  0.0293  532  ASP B CB  
12568 N N   . ARG B 535  ? 0.2176 0.3740 0.2680 -0.0216 0.0098  0.0222  533  ARG B N   
12569 C CA  . ARG B 535  ? 0.2406 0.3911 0.2899 -0.0159 0.0115  0.0188  533  ARG B CA  
12570 C C   . ARG B 535  ? 0.2701 0.4082 0.3148 -0.0167 0.0103  0.0166  533  ARG B C   
12571 O O   . ARG B 535  ? 0.2536 0.3866 0.2971 -0.0127 0.0115  0.0140  533  ARG B O   
12572 C CB  . ARG B 535  ? 0.3360 0.4936 0.3864 -0.0121 0.0146  0.0187  533  ARG B CB  
12573 N N   . ILE B 536  ? 0.2146 0.3478 0.2566 -0.0218 0.0078  0.0177  534  ILE B N   
12574 C CA  . ILE B 536  ? 0.2286 0.3503 0.2664 -0.0225 0.0064  0.0157  534  ILE B CA  
12575 C C   . ILE B 536  ? 0.2014 0.3164 0.2383 -0.0243 0.0039  0.0150  534  ILE B C   
12576 O O   . ILE B 536  ? 0.2170 0.3340 0.2540 -0.0285 0.0020  0.0172  534  ILE B O   
12577 C CB  . ILE B 536  ? 0.2457 0.3660 0.2802 -0.0266 0.0056  0.0172  534  ILE B CB  
12578 C CG1 . ILE B 536  ? 0.2528 0.3803 0.2878 -0.0248 0.0083  0.0179  534  ILE B CG1 
12579 C CG2 . ILE B 536  ? 0.2096 0.3179 0.2399 -0.0270 0.0039  0.0151  534  ILE B CG2 
12580 C CD1 . ILE B 536  ? 0.3119 0.4388 0.3436 -0.0289 0.0076  0.0197  534  ILE B CD1 
12581 N N   . ALA B 537  ? 0.2138 0.3211 0.2499 -0.0211 0.0040  0.0122  535  ALA B N   
12582 C CA  . ALA B 537  ? 0.2405 0.3417 0.2757 -0.0221 0.0020  0.0114  535  ALA B CA  
12583 C C   . ALA B 537  ? 0.2201 0.3127 0.2509 -0.0256 -0.0004 0.0111  535  ALA B C   
12584 O O   . ALA B 537  ? 0.1897 0.2773 0.2183 -0.0249 -0.0002 0.0099  535  ALA B O   
12585 C CB  . ALA B 537  ? 0.2251 0.3220 0.2611 -0.0174 0.0031  0.0087  535  ALA B CB  
12586 N N   . LEU B 538  ? 0.1984 0.2893 0.2279 -0.0293 -0.0028 0.0123  536  LEU B N   
12587 C CA  . LEU B 538  ? 0.2414 0.3224 0.2665 -0.0315 -0.0052 0.0113  536  LEU B CA  
12588 C C   . LEU B 538  ? 0.2231 0.2968 0.2475 -0.0275 -0.0045 0.0082  536  LEU B C   
12589 O O   . LEU B 538  ? 0.2207 0.2964 0.2478 -0.0241 -0.0030 0.0070  536  LEU B O   
12590 C CB  . LEU B 538  ? 0.2525 0.3318 0.2760 -0.0353 -0.0079 0.0125  536  LEU B CB  
12591 C CG  . LEU B 538  ? 0.3092 0.3926 0.3319 -0.0408 -0.0097 0.0156  536  LEU B CG  
12592 C CD1 . LEU B 538  ? 0.3205 0.4024 0.3420 -0.0437 -0.0123 0.0163  536  LEU B CD1 
12593 C CD2 . LEU B 538  ? 0.2680 0.3451 0.2865 -0.0436 -0.0112 0.0161  536  LEU B CD2 
12594 N N   . PRO B 539  ? 0.2266 0.2921 0.2477 -0.0277 -0.0056 0.0068  537  PRO B N   
12595 C CA  . PRO B 539  ? 0.2280 0.2874 0.2488 -0.0239 -0.0049 0.0039  537  PRO B CA  
12596 C C   . PRO B 539  ? 0.1899 0.2482 0.2116 -0.0226 -0.0050 0.0030  537  PRO B C   
12597 O O   . PRO B 539  ? 0.2181 0.2766 0.2420 -0.0190 -0.0033 0.0014  537  PRO B O   
12598 C CB  . PRO B 539  ? 0.1972 0.2481 0.2139 -0.0254 -0.0069 0.0032  537  PRO B CB  
12599 C CG  . PRO B 539  ? 0.2023 0.2559 0.2176 -0.0287 -0.0075 0.0055  537  PRO B CG  
12600 C CD  . PRO B 539  ? 0.2234 0.2851 0.2408 -0.0313 -0.0075 0.0079  537  PRO B CD  
12601 N N   . ALA B 540  ? 0.2143 0.2716 0.2342 -0.0257 -0.0070 0.0040  538  ALA B N   
12602 C CA  . ALA B 540  ? 0.2276 0.2838 0.2477 -0.0246 -0.0073 0.0031  538  ALA B CA  
12603 C C   . ALA B 540  ? 0.2392 0.3031 0.2636 -0.0224 -0.0053 0.0037  538  ALA B C   
12604 O O   . ALA B 540  ? 0.2269 0.2897 0.2519 -0.0202 -0.0048 0.0027  538  ALA B O   
12605 C CB  . ALA B 540  ? 0.2391 0.2931 0.2560 -0.0287 -0.0101 0.0043  538  ALA B CB  
12606 N N   . GLU B 541  ? 0.2326 0.3042 0.2597 -0.0226 -0.0042 0.0055  539  GLU B N   
12607 C CA  . GLU B 541  ? 0.2326 0.3121 0.2637 -0.0207 -0.0027 0.0064  539  GLU B CA  
12608 C C   . GLU B 541  ? 0.2406 0.3223 0.2743 -0.0164 0.0000  0.0053  539  GLU B C   
12609 O O   . GLU B 541  ? 0.2067 0.2953 0.2436 -0.0145 0.0014  0.0062  539  GLU B O   
12610 C CB  . GLU B 541  ? 0.2531 0.3405 0.2856 -0.0240 -0.0035 0.0093  539  GLU B CB  
12611 C CG  . GLU B 541  ? 0.2683 0.3539 0.2985 -0.0280 -0.0063 0.0104  539  GLU B CG  
12612 C CD  . GLU B 541  ? 0.4263 0.5187 0.4573 -0.0325 -0.0077 0.0134  539  GLU B CD  
12613 O OE1 . GLU B 541  ? 0.4414 0.5419 0.4755 -0.0322 -0.0062 0.0150  539  GLU B OE1 
12614 O OE2 . GLU B 541  ? 0.4196 0.5091 0.4479 -0.0364 -0.0105 0.0143  539  GLU B OE2 
12615 N N   . LEU B 542  ? 0.1972 0.2727 0.2294 -0.0147 0.0005  0.0033  540  LEU B N   
12616 C CA  . LEU B 542  ? 0.1946 0.2714 0.2287 -0.0111 0.0026  0.0022  540  LEU B CA  
12617 C C   . LEU B 542  ? 0.2544 0.3335 0.2912 -0.0076 0.0041  0.0016  540  LEU B C   
12618 O O   . LEU B 542  ? 0.2298 0.3121 0.2685 -0.0048 0.0058  0.0014  540  LEU B O   
12619 C CB  . LEU B 542  ? 0.2482 0.3175 0.2803 -0.0101 0.0025  0.0001  540  LEU B CB  
12620 C CG  . LEU B 542  ? 0.2883 0.3556 0.3184 -0.0113 0.0022  0.0000  540  LEU B CG  
12621 C CD1 . LEU B 542  ? 0.2327 0.2937 0.2620 -0.0089 0.0025  -0.0023 540  LEU B CD1 
12622 C CD2 . LEU B 542  ? 0.2453 0.3195 0.2765 -0.0111 0.0035  0.0013  540  LEU B CD2 
12623 N N   . PHE B 543  ? 0.1906 0.2675 0.2272 -0.0077 0.0033  0.0014  541  PHE B N   
12624 C CA  . PHE B 543  ? 0.2148 0.2929 0.2535 -0.0045 0.0045  0.0010  541  PHE B CA  
12625 C C   . PHE B 543  ? 0.2410 0.3254 0.2815 -0.0052 0.0041  0.0029  541  PHE B C   
12626 O O   . PHE B 543  ? 0.2366 0.3216 0.2784 -0.0030 0.0046  0.0029  541  PHE B O   
12627 C CB  . PHE B 543  ? 0.2298 0.3009 0.2671 -0.0037 0.0043  -0.0007 541  PHE B CB  
12628 C CG  . PHE B 543  ? 0.2263 0.2917 0.2622 -0.0035 0.0043  -0.0024 541  PHE B CG  
12629 C CD1 . PHE B 543  ? 0.2368 0.3024 0.2737 -0.0014 0.0056  -0.0033 541  PHE B CD1 
12630 C CD2 . PHE B 543  ? 0.2041 0.2640 0.2373 -0.0052 0.0030  -0.0032 541  PHE B CD2 
12631 C CE1 . PHE B 543  ? 0.2428 0.3035 0.2785 -0.0012 0.0054  -0.0048 541  PHE B CE1 
12632 C CE2 . PHE B 543  ? 0.2303 0.2854 0.2624 -0.0048 0.0029  -0.0047 541  PHE B CE2 
12633 C CZ  . PHE B 543  ? 0.2561 0.3117 0.2896 -0.0029 0.0041  -0.0054 541  PHE B CZ  
12634 N N   . GLY B 544  ? 0.2188 0.3078 0.2592 -0.0082 0.0030  0.0048  542  GLY B N   
12635 C CA  . GLY B 544  ? 0.2491 0.3453 0.2917 -0.0089 0.0025  0.0069  542  GLY B CA  
12636 C C   . GLY B 544  ? 0.2903 0.3836 0.3317 -0.0097 0.0011  0.0068  542  GLY B C   
12637 O O   . GLY B 544  ? 0.2590 0.3457 0.2971 -0.0115 -0.0002 0.0058  542  GLY B O   
12638 N N   . ASP B 545  ? 0.2761 0.3744 0.3198 -0.0080 0.0014  0.0079  543  ASP B N   
12639 C CA  . ASP B 545  ? 0.3398 0.4361 0.3822 -0.0087 0.0000  0.0082  543  ASP B CA  
12640 C C   . ASP B 545  ? 0.2977 0.3867 0.3384 -0.0064 0.0008  0.0061  543  ASP B C   
12641 O O   . ASP B 545  ? 0.2969 0.3834 0.3358 -0.0070 -0.0002 0.0061  543  ASP B O   
12642 C CB  . ASP B 545  ? 0.3602 0.4644 0.4058 -0.0074 0.0000  0.0101  543  ASP B CB  
12643 C CG  . ASP B 545  ? 0.4627 0.5756 0.5108 -0.0095 -0.0005 0.0123  543  ASP B CG  
12644 O OD1 . ASP B 545  ? 0.4982 0.6105 0.5444 -0.0137 -0.0021 0.0130  543  ASP B OD1 
12645 O OD2 . ASP B 545  ? 0.6631 0.7833 0.7148 -0.0069 0.0006  0.0135  543  ASP B OD2 
12646 N N   . ALA B 546  ? 0.2514 0.3372 0.2926 -0.0038 0.0025  0.0046  544  ALA B N   
12647 C CA  . ALA B 546  ? 0.2646 0.3443 0.3047 -0.0018 0.0033  0.0029  544  ALA B CA  
12648 C C   . ALA B 546  ? 0.3066 0.3799 0.3431 -0.0040 0.0021  0.0018  544  ALA B C   
12649 O O   . ALA B 546  ? 0.2548 0.3250 0.2898 -0.0035 0.0020  0.0013  544  ALA B O   
12650 C CB  . ALA B 546  ? 0.2819 0.3595 0.3233 0.0010  0.0050  0.0015  544  ALA B CB  
12651 N N   . ARG B 547  ? 0.2381 0.3095 0.2730 -0.0063 0.0013  0.0014  545  ARG B N   
12652 C CA  . ARG B 547  ? 0.2344 0.2991 0.2656 -0.0079 0.0002  0.0000  545  ARG B CA  
12653 C C   . ARG B 547  ? 0.2308 0.2945 0.2606 -0.0105 -0.0009 0.0001  545  ARG B C   
12654 O O   . ARG B 547  ? 0.2291 0.2965 0.2608 -0.0105 -0.0003 0.0008  545  ARG B O   
12655 C CB  . ARG B 547  ? 0.2684 0.3280 0.2995 -0.0054 0.0016  -0.0020 545  ARG B CB  
12656 C CG  . ARG B 547  ? 0.2409 0.3005 0.2740 -0.0038 0.0029  -0.0027 545  ARG B CG  
12657 C CD  . ARG B 547  ? 0.2457 0.3005 0.2788 -0.0017 0.0040  -0.0045 545  ARG B CD  
12658 N NE  . ARG B 547  ? 0.2347 0.2903 0.2701 0.0001  0.0052  -0.0049 545  ARG B NE  
12659 C CZ  . ARG B 547  ? 0.2482 0.3011 0.2833 0.0002  0.0052  -0.0061 545  ARG B CZ  
12660 N NH1 . ARG B 547  ? 0.2224 0.2712 0.2551 -0.0012 0.0041  -0.0069 545  ARG B NH1 
12661 N NH2 . ARG B 547  ? 0.2659 0.3198 0.3027 0.0018  0.0062  -0.0064 545  ARG B NH2 
12662 N N   . THR B 548  ? 0.1905 0.2488 0.2166 -0.0125 -0.0026 -0.0007 546  THR B N   
12663 C CA  . THR B 548  ? 0.2067 0.2624 0.2305 -0.0152 -0.0040 -0.0006 546  THR B CA  
12664 C C   . THR B 548  ? 0.2173 0.2680 0.2406 -0.0134 -0.0032 -0.0025 546  THR B C   
12665 O O   . THR B 548  ? 0.2009 0.2471 0.2234 -0.0115 -0.0026 -0.0042 546  THR B O   
12666 C CB  . THR B 548  ? 0.1980 0.2494 0.2175 -0.0181 -0.0065 -0.0006 546  THR B CB  
12667 O OG1 . THR B 548  ? 0.2524 0.3088 0.2725 -0.0198 -0.0075 0.0012  546  THR B OG1 
12668 C CG2 . THR B 548  ? 0.2434 0.2916 0.2603 -0.0211 -0.0083 -0.0003 546  THR B CG2 
12669 N N   . ASN B 549  ? 0.1712 0.2231 0.1953 -0.0141 -0.0030 -0.0020 547  ASN B N   
12670 C CA  . ASN B 549  ? 0.1855 0.2330 0.2091 -0.0127 -0.0026 -0.0036 547  ASN B CA  
12671 C C   . ASN B 549  ? 0.1885 0.2286 0.2079 -0.0140 -0.0044 -0.0047 547  ASN B C   
12672 O O   . ASN B 549  ? 0.1965 0.2351 0.2130 -0.0169 -0.0064 -0.0038 547  ASN B O   
12673 C CB  . ASN B 549  ? 0.2370 0.2875 0.2615 -0.0135 -0.0023 -0.0026 547  ASN B CB  
12674 C CG  . ASN B 549  ? 0.2163 0.2631 0.2407 -0.0117 -0.0017 -0.0041 547  ASN B CG  
12675 O OD1 . ASN B 549  ? 0.2020 0.2452 0.2268 -0.0094 -0.0011 -0.0059 547  ASN B OD1 
12676 N ND2 . ASN B 549  ? 0.1792 0.2273 0.2031 -0.0129 -0.0019 -0.0033 547  ASN B ND2 
12677 N N   . SER B 550  ? 0.1715 0.2070 0.1906 -0.0117 -0.0038 -0.0066 548  SER B N   
12678 C CA  . SER B 550  ? 0.2055 0.2341 0.2209 -0.0123 -0.0055 -0.0078 548  SER B CA  
12679 C C   . SER B 550  ? 0.2300 0.2568 0.2432 -0.0148 -0.0072 -0.0069 548  SER B C   
12680 O O   . SER B 550  ? 0.2335 0.2640 0.2486 -0.0153 -0.0066 -0.0058 548  SER B O   
12681 C CB  . SER B 550  ? 0.2075 0.2327 0.2237 -0.0091 -0.0044 -0.0099 548  SER B CB  
12682 O OG  . SER B 550  ? 0.2177 0.2448 0.2366 -0.0080 -0.0034 -0.0099 548  SER B OG  
12683 N N   . ALA B 551  ? 0.2016 0.2223 0.2105 -0.0165 -0.0095 -0.0073 549  ALA B N   
12684 C CA  . ALA B 551  ? 0.2083 0.2260 0.2144 -0.0192 -0.0115 -0.0063 549  ALA B CA  
12685 C C   . ALA B 551  ? 0.2410 0.2520 0.2452 -0.0174 -0.0122 -0.0081 549  ALA B C   
12686 O O   . ALA B 551  ? 0.2114 0.2181 0.2143 -0.0151 -0.0122 -0.0100 549  ALA B O   
12687 C CB  . ALA B 551  ? 0.2312 0.2464 0.2333 -0.0230 -0.0141 -0.0051 549  ALA B CB  
12688 N N   . GLY B 552  ? 0.2403 0.2505 0.2440 -0.0182 -0.0128 -0.0074 550  GLY B N   
12689 C CA  . GLY B 552  ? 0.2413 0.2451 0.2429 -0.0168 -0.0139 -0.0086 550  GLY B CA  
12690 C C   . GLY B 552  ? 0.2249 0.2219 0.2211 -0.0197 -0.0170 -0.0080 550  GLY B C   
12691 O O   . GLY B 552  ? 0.2657 0.2617 0.2593 -0.0226 -0.0185 -0.0070 550  GLY B O   
12692 N N   . LEU B 553  ? 0.2315 0.2232 0.2257 -0.0188 -0.0183 -0.0086 551  LEU B N   
12693 C CA  . LEU B 553  ? 0.2959 0.2800 0.2846 -0.0213 -0.0215 -0.0079 551  LEU B CA  
12694 C C   . LEU B 553  ? 0.2246 0.2089 0.2132 -0.0224 -0.0220 -0.0066 551  LEU B C   
12695 O O   . LEU B 553  ? 0.2566 0.2432 0.2481 -0.0197 -0.0205 -0.0074 551  LEU B O   
12696 C CB  . LEU B 553  ? 0.2787 0.2545 0.2642 -0.0185 -0.0228 -0.0103 551  LEU B CB  
12697 C CG  . LEU B 553  ? 0.2905 0.2653 0.2751 -0.0175 -0.0225 -0.0118 551  LEU B CG  
12698 C CD1 . LEU B 553  ? 0.3086 0.2761 0.2904 -0.0139 -0.0233 -0.0144 551  LEU B CD1 
12699 C CD2 . LEU B 553  ? 0.3047 0.2777 0.2854 -0.0219 -0.0246 -0.0103 551  LEU B CD2 
12700 N N   . ASP B 554  ? 0.2412 0.2232 0.2261 -0.0266 -0.0242 -0.0044 552  ASP B N   
12701 C CA  . ASP B 554  ? 0.2657 0.2480 0.2498 -0.0282 -0.0248 -0.0026 552  ASP B CA  
12702 C C   . ASP B 554  ? 0.2525 0.2253 0.2324 -0.0270 -0.0273 -0.0036 552  ASP B C   
12703 O O   . ASP B 554  ? 0.2656 0.2312 0.2404 -0.0294 -0.0303 -0.0029 552  ASP B O   
12704 C CB  . ASP B 554  ? 0.2712 0.2564 0.2536 -0.0335 -0.0258 0.0005  552  ASP B CB  
12705 C CG  . ASP B 554  ? 0.2667 0.2532 0.2482 -0.0353 -0.0261 0.0026  552  ASP B CG  
12706 O OD1 . ASP B 554  ? 0.2935 0.2779 0.2753 -0.0325 -0.0258 0.0015  552  ASP B OD1 
12707 O OD2 . ASP B 554  ? 0.2923 0.2822 0.2728 -0.0397 -0.0266 0.0054  552  ASP B OD2 
12708 N N   . LEU B 555  ? 0.2794 0.2521 0.2614 -0.0233 -0.0264 -0.0050 553  LEU B N   
12709 C CA  . LEU B 555  ? 0.2588 0.2232 0.2375 -0.0215 -0.0287 -0.0060 553  LEU B CA  
12710 C C   . LEU B 555  ? 0.2816 0.2430 0.2567 -0.0245 -0.0308 -0.0037 553  LEU B C   
12711 O O   . LEU B 555  ? 0.2944 0.2493 0.2668 -0.0229 -0.0328 -0.0042 553  LEU B O   
12712 C CB  . LEU B 555  ? 0.2892 0.2552 0.2718 -0.0165 -0.0271 -0.0083 553  LEU B CB  
12713 C CG  . LEU B 555  ? 0.2955 0.2639 0.2815 -0.0133 -0.0251 -0.0106 553  LEU B CG  
12714 C CD1 . LEU B 555  ? 0.2661 0.2355 0.2556 -0.0088 -0.0239 -0.0126 553  LEU B CD1 
12715 C CD2 . LEU B 555  ? 0.3547 0.3165 0.3365 -0.0134 -0.0268 -0.0116 553  LEU B CD2 
12716 N N   . SER B 556  ? 0.2644 0.2308 0.2394 -0.0286 -0.0304 -0.0010 554  SER B N   
12717 C CA  . SER B 556  ? 0.2505 0.2138 0.2213 -0.0323 -0.0326 0.0017  554  SER B CA  
12718 C C   . SER B 556  ? 0.2809 0.2398 0.2471 -0.0371 -0.0351 0.0037  554  SER B C   
12719 O O   . SER B 556  ? 0.3015 0.2569 0.2636 -0.0408 -0.0373 0.0062  554  SER B O   
12720 C CB  . SER B 556  ? 0.2911 0.2631 0.2645 -0.0338 -0.0303 0.0036  554  SER B CB  
12721 O OG  . SER B 556  ? 0.2778 0.2575 0.2536 -0.0366 -0.0286 0.0051  554  SER B OG  
12722 N N   . ASN B 557  ? 0.2654 0.2241 0.2320 -0.0372 -0.0350 0.0026  555  ASN B N   
12723 C CA  . ASN B 557  ? 0.2844 0.2388 0.2467 -0.0418 -0.0377 0.0042  555  ASN B CA  
12724 C C   . ASN B 557  ? 0.2998 0.2416 0.2564 -0.0405 -0.0410 0.0026  555  ASN B C   
12725 O O   . ASN B 557  ? 0.2872 0.2265 0.2446 -0.0363 -0.0404 -0.0005 555  ASN B O   
12726 C CB  . ASN B 557  ? 0.2755 0.2366 0.2411 -0.0425 -0.0359 0.0039  555  ASN B CB  
12727 C CG  . ASN B 557  ? 0.3139 0.2715 0.2754 -0.0477 -0.0387 0.0057  555  ASN B CG  
12728 O OD1 . ASN B 557  ? 0.3223 0.2695 0.2782 -0.0484 -0.0419 0.0051  555  ASN B OD1 
12729 N ND2 . ASN B 557  ? 0.3128 0.2791 0.2771 -0.0512 -0.0375 0.0080  555  ASN B ND2 
12730 N N   . GLU B 558  ? 0.3258 0.2598 0.2765 -0.0442 -0.0445 0.0046  556  GLU B N   
12731 C CA  . GLU B 558  ? 0.3597 0.2809 0.3044 -0.0427 -0.0479 0.0030  556  GLU B CA  
12732 C C   . GLU B 558  ? 0.3721 0.2890 0.3145 -0.0427 -0.0490 0.0012  556  GLU B C   
12733 O O   . GLU B 558  ? 0.3767 0.2852 0.3160 -0.0389 -0.0504 -0.0015 556  GLU B O   
12734 C CB  . GLU B 558  ? 0.3825 0.2956 0.3209 -0.0471 -0.0517 0.0058  556  GLU B CB  
12735 C CG  . GLU B 558  ? 0.3577 0.2719 0.2965 -0.0465 -0.0515 0.0072  556  GLU B CG  
12736 C CD  . GLU B 558  ? 0.3893 0.2994 0.3288 -0.0401 -0.0513 0.0044  556  GLU B CD  
12737 O OE1 . GLU B 558  ? 0.3749 0.2794 0.3135 -0.0359 -0.0519 0.0013  556  GLU B OE1 
12738 O OE2 . GLU B 558  ? 0.3748 0.2877 0.3157 -0.0393 -0.0506 0.0053  556  GLU B OE2 
12739 N N   . GLU B 559  ? 0.3295 0.2516 0.2728 -0.0469 -0.0487 0.0028  557  GLU B N   
12740 C CA  . GLU B 559  ? 0.3632 0.2819 0.3045 -0.0467 -0.0496 0.0010  557  GLU B CA  
12741 C C   . GLU B 559  ? 0.3489 0.2711 0.2944 -0.0405 -0.0464 -0.0025 557  GLU B C   
12742 O O   . GLU B 559  ? 0.3481 0.2633 0.2905 -0.0373 -0.0474 -0.0053 557  GLU B O   
12743 C CB  . GLU B 559  ? 0.3803 0.3057 0.3229 -0.0521 -0.0495 0.0034  557  GLU B CB  
12744 C CG  . GLU B 559  ? 0.5073 0.4297 0.4457 -0.0591 -0.0528 0.0070  557  GLU B CG  
12745 C CD  . GLU B 559  ? 0.5602 0.4912 0.5012 -0.0639 -0.0523 0.0093  557  GLU B CD  
12746 O OE1 . GLU B 559  ? 0.6284 0.5622 0.5713 -0.0621 -0.0511 0.0074  557  GLU B OE1 
12747 O OE2 . GLU B 559  ? 0.5344 0.4696 0.4756 -0.0694 -0.0530 0.0130  557  GLU B OE2 
12748 N N   . THR B 560  ? 0.3024 0.2357 0.2550 -0.0387 -0.0426 -0.0023 558  THR B N   
12749 C CA  . THR B 560  ? 0.3000 0.2375 0.2570 -0.0332 -0.0395 -0.0053 558  THR B CA  
12750 C C   . THR B 560  ? 0.3188 0.2493 0.2743 -0.0281 -0.0401 -0.0078 558  THR B C   
12751 O O   . THR B 560  ? 0.3169 0.2446 0.2720 -0.0242 -0.0395 -0.0106 558  THR B O   
12752 C CB  . THR B 560  ? 0.2829 0.2324 0.2471 -0.0326 -0.0358 -0.0043 558  THR B CB  
12753 O OG1 . THR B 560  ? 0.3076 0.2639 0.2733 -0.0370 -0.0353 -0.0019 558  THR B OG1 
12754 C CG2 . THR B 560  ? 0.2889 0.2427 0.2577 -0.0275 -0.0327 -0.0071 558  THR B CG2 
12755 N N   . LEU B 561  ? 0.2822 0.2100 0.2367 -0.0281 -0.0412 -0.0068 559  LEU B N   
12756 C CA  . LEU B 561  ? 0.3346 0.2564 0.2881 -0.0232 -0.0419 -0.0090 559  LEU B CA  
12757 C C   . LEU B 561  ? 0.3397 0.2498 0.2865 -0.0220 -0.0450 -0.0108 559  LEU B C   
12758 O O   . LEU B 561  ? 0.3209 0.2280 0.2679 -0.0168 -0.0445 -0.0136 559  LEU B O   
12759 C CB  . LEU B 561  ? 0.3161 0.2366 0.2691 -0.0239 -0.0430 -0.0072 559  LEU B CB  
12760 C CG  . LEU B 561  ? 0.2943 0.2255 0.2536 -0.0236 -0.0399 -0.0063 559  LEU B CG  
12761 C CD1 . LEU B 561  ? 0.2639 0.1930 0.2216 -0.0246 -0.0413 -0.0045 559  LEU B CD1 
12762 C CD2 . LEU B 561  ? 0.2493 0.1858 0.2143 -0.0182 -0.0368 -0.0090 559  LEU B CD2 
12763 N N   . ALA B 562  ? 0.3288 0.2322 0.2697 -0.0268 -0.0483 -0.0091 560  ALA B N   
12764 C CA  . ALA B 562  ? 0.3535 0.2446 0.2872 -0.0257 -0.0515 -0.0108 560  ALA B CA  
12765 C C   . ALA B 562  ? 0.3797 0.2718 0.3137 -0.0232 -0.0500 -0.0136 560  ALA B C   
12766 O O   . ALA B 562  ? 0.3727 0.2584 0.3040 -0.0185 -0.0506 -0.0165 560  ALA B O   
12767 C CB  . ALA B 562  ? 0.3584 0.2421 0.2855 -0.0320 -0.0556 -0.0082 560  ALA B CB  
12768 N N   . SER B 563  ? 0.3521 0.2523 0.2893 -0.0260 -0.0481 -0.0126 561  SER B N   
12769 C CA  . SER B 563  ? 0.3607 0.2617 0.2978 -0.0238 -0.0469 -0.0150 561  SER B CA  
12770 C C   . SER B 563  ? 0.3282 0.2354 0.2711 -0.0177 -0.0430 -0.0175 561  SER B C   
12771 O O   . SER B 563  ? 0.3301 0.2344 0.2713 -0.0138 -0.0424 -0.0203 561  SER B O   
12772 C CB  . SER B 563  ? 0.4277 0.3357 0.3666 -0.0287 -0.0462 -0.0131 561  SER B CB  
12773 O OG  . SER B 563  ? 0.5063 0.4264 0.4528 -0.0290 -0.0428 -0.0115 561  SER B OG  
12774 N N   . LEU B 564  ? 0.2916 0.2073 0.2410 -0.0168 -0.0405 -0.0165 562  LEU B N   
12775 C CA  . LEU B 564  ? 0.3298 0.2511 0.2847 -0.0114 -0.0371 -0.0185 562  LEU B CA  
12776 C C   . LEU B 564  ? 0.3169 0.2307 0.2692 -0.0065 -0.0384 -0.0209 562  LEU B C   
12777 O O   . LEU B 564  ? 0.3460 0.2608 0.3000 -0.0017 -0.0365 -0.0234 562  LEU B O   
12778 C CB  . LEU B 564  ? 0.3219 0.2529 0.2836 -0.0119 -0.0347 -0.0169 562  LEU B CB  
12779 C CG  . LEU B 564  ? 0.3545 0.2920 0.3224 -0.0070 -0.0314 -0.0186 562  LEU B CG  
12780 C CD1 . LEU B 564  ? 0.3206 0.2625 0.2905 -0.0057 -0.0289 -0.0200 562  LEU B CD1 
12781 C CD2 . LEU B 564  ? 0.3710 0.3163 0.3443 -0.0080 -0.0296 -0.0168 562  LEU B CD2 
12782 N N   . THR B 565  ? 0.2971 0.2035 0.2454 -0.0075 -0.0415 -0.0199 563  THR B N   
12783 C CA  . THR B 565  ? 0.3272 0.2255 0.2724 -0.0027 -0.0431 -0.0221 563  THR B CA  
12784 C C   . THR B 565  ? 0.3439 0.2357 0.2844 0.0000  -0.0437 -0.0249 563  THR B C   
12785 O O   . THR B 565  ? 0.3466 0.2382 0.2882 0.0056  -0.0424 -0.0275 563  THR B O   
12786 C CB  . THR B 565  ? 0.3567 0.2462 0.2967 -0.0050 -0.0470 -0.0203 563  THR B CB  
12787 O OG1 . THR B 565  ? 0.3319 0.2277 0.2763 -0.0067 -0.0461 -0.0180 563  THR B OG1 
12788 C CG2 . THR B 565  ? 0.3600 0.2402 0.2961 0.0002  -0.0491 -0.0226 563  THR B CG2 
12789 N N   . GLU B 566  ? 0.3414 0.2282 0.2764 -0.0040 -0.0458 -0.0243 564  GLU B N   
12790 C CA  . GLU B 566  ? 0.3442 0.2238 0.2735 -0.0016 -0.0467 -0.0271 564  GLU B CA  
12791 C C   . GLU B 566  ? 0.3710 0.2590 0.3049 0.0015  -0.0427 -0.0289 564  GLU B C   
12792 O O   . GLU B 566  ? 0.3648 0.2498 0.2969 0.0066  -0.0420 -0.0319 564  GLU B O   
12793 C CB  . GLU B 566  ? 0.3991 0.2710 0.3212 -0.0071 -0.0503 -0.0259 564  GLU B CB  
12794 N N   . ALA B 567  ? 0.2987 0.1973 0.2385 -0.0013 -0.0401 -0.0272 565  ALA B N   
12795 C CA  . ALA B 567  ? 0.3173 0.2240 0.2616 0.0014  -0.0363 -0.0286 565  ALA B CA  
12796 C C   . ALA B 567  ? 0.3298 0.2410 0.2794 0.0072  -0.0335 -0.0303 565  ALA B C   
12797 O O   . ALA B 567  ? 0.2972 0.2106 0.2478 0.0111  -0.0312 -0.0325 565  ALA B O   
12798 C CB  . ALA B 567  ? 0.3220 0.2389 0.2716 -0.0027 -0.0342 -0.0262 565  ALA B CB  
12799 N N   . LEU B 568  ? 0.2861 0.1996 0.2394 0.0075  -0.0335 -0.0290 566  LEU B N   
12800 C CA  . LEU B 568  ? 0.2991 0.2172 0.2578 0.0126  -0.0313 -0.0304 566  LEU B CA  
12801 C C   . LEU B 568  ? 0.3443 0.2546 0.2987 0.0178  -0.0325 -0.0331 566  LEU B C   
12802 O O   . LEU B 568  ? 0.3214 0.2355 0.2787 0.0225  -0.0300 -0.0352 566  LEU B O   
12803 C CB  . LEU B 568  ? 0.2754 0.1968 0.2382 0.0115  -0.0316 -0.0285 566  LEU B CB  
12804 C CG  . LEU B 568  ? 0.3058 0.2360 0.2736 0.0074  -0.0298 -0.0260 566  LEU B CG  
12805 C CD1 . LEU B 568  ? 0.2913 0.2228 0.2614 0.0063  -0.0307 -0.0242 566  LEU B CD1 
12806 C CD2 . LEU B 568  ? 0.2771 0.2170 0.2513 0.0092  -0.0258 -0.0266 566  LEU B CD2 
12807 N N   . ARG B 569  ? 0.3065 0.2059 0.2540 0.0171  -0.0364 -0.0332 567  ARG B N   
12808 C CA  . ARG B 569  ? 0.3343 0.2250 0.2766 0.0222  -0.0380 -0.0360 567  ARG B CA  
12809 C C   . ARG B 569  ? 0.3512 0.2413 0.2909 0.0245  -0.0364 -0.0385 567  ARG B C   
12810 O O   . ARG B 569  ? 0.3769 0.2678 0.3173 0.0303  -0.0347 -0.0410 567  ARG B O   
12811 C CB  . ARG B 569  ? 0.3735 0.2514 0.3076 0.0200  -0.0428 -0.0354 567  ARG B CB  
12812 C CG  . ARG B 569  ? 0.4370 0.3138 0.3727 0.0187  -0.0447 -0.0332 567  ARG B CG  
12813 C CD  . ARG B 569  ? 0.4803 0.3435 0.4073 0.0169  -0.0496 -0.0327 567  ARG B CD  
12814 N NE  . ARG B 569  ? 0.5776 0.4396 0.5055 0.0154  -0.0515 -0.0304 567  ARG B NE  
12815 C CZ  . ARG B 569  ? 0.6305 0.4828 0.5521 0.0118  -0.0556 -0.0287 567  ARG B CZ  
12816 N NH1 . ARG B 569  ? 0.6249 0.4678 0.5387 0.0089  -0.0584 -0.0288 567  ARG B NH1 
12817 N NH2 . ARG B 569  ? 0.6147 0.4665 0.5374 0.0109  -0.0570 -0.0266 567  ARG B NH2 
12818 N N   . GLU B 570  ? 0.3648 0.2539 0.3012 0.0201  -0.0369 -0.0377 568  GLU B N   
12819 C CA  . GLU B 570  ? 0.3285 0.2169 0.2616 0.0219  -0.0356 -0.0400 568  GLU B CA  
12820 C C   . GLU B 570  ? 0.3529 0.2528 0.2933 0.0250  -0.0308 -0.0407 568  GLU B C   
12821 O O   . GLU B 570  ? 0.3514 0.2510 0.2901 0.0294  -0.0291 -0.0432 568  GLU B O   
12822 C CB  . GLU B 570  ? 0.3904 0.2767 0.3194 0.0159  -0.0372 -0.0386 568  GLU B CB  
12823 C CG  . GLU B 570  ? 0.5060 0.3796 0.4264 0.0127  -0.0422 -0.0382 568  GLU B CG  
12824 C CD  . GLU B 570  ? 0.6209 0.4944 0.5391 0.0056  -0.0439 -0.0358 568  GLU B CD  
12825 O OE1 . GLU B 570  ? 0.6476 0.5313 0.5711 0.0035  -0.0412 -0.0345 568  GLU B OE1 
12826 O OE2 . GLU B 570  ? 0.6688 0.5323 0.5800 0.0022  -0.0481 -0.0351 568  GLU B OE2 
12827 N N   . SER B 571  ? 0.3164 0.2265 0.2648 0.0229  -0.0286 -0.0384 569  SER B N   
12828 C CA  . SER B 571  ? 0.3183 0.2392 0.2738 0.0255  -0.0242 -0.0388 569  SER B CA  
12829 C C   . SER B 571  ? 0.3663 0.2880 0.3241 0.0318  -0.0229 -0.0409 569  SER B C   
12830 O O   . SER B 571  ? 0.3229 0.2501 0.2832 0.0352  -0.0197 -0.0423 569  SER B O   
12831 C CB  . SER B 571  ? 0.3162 0.2463 0.2793 0.0222  -0.0226 -0.0361 569  SER B CB  
12832 O OG  . SER B 571  ? 0.3388 0.2697 0.3054 0.0234  -0.0232 -0.0354 569  SER B OG  
12833 N N   . ALA B 572  ? 0.3420 0.2586 0.2989 0.0334  -0.0252 -0.0409 570  ALA B N   
12834 C CA  . ALA B 572  ? 0.3641 0.2816 0.3233 0.0395  -0.0243 -0.0428 570  ALA B CA  
12835 C C   . ALA B 572  ? 0.3819 0.2925 0.3347 0.0442  -0.0246 -0.0459 570  ALA B C   
12836 O O   . ALA B 572  ? 0.4091 0.3227 0.3644 0.0499  -0.0228 -0.0478 570  ALA B O   
12837 C CB  . ALA B 572  ? 0.3644 0.2778 0.3240 0.0399  -0.0271 -0.0419 570  ALA B CB  
12838 N N   . ALA B 573  ? 0.3576 0.2593 0.3021 0.0421  -0.0269 -0.0466 571  ALA B N   
12839 C CA  . ALA B 573  ? 0.4105 0.3047 0.3478 0.0465  -0.0274 -0.0498 571  ALA B CA  
12840 C C   . ALA B 573  ? 0.3830 0.2825 0.3202 0.0473  -0.0241 -0.0510 571  ALA B C   
12841 O O   . ALA B 573  ? 0.3759 0.2703 0.3073 0.0514  -0.0239 -0.0539 571  ALA B O   
12842 C CB  . ALA B 573  ? 0.3887 0.2688 0.3159 0.0440  -0.0322 -0.0502 571  ALA B CB  
12843 N N   . MET B 574  ? 0.3364 0.2457 0.2795 0.0437  -0.0215 -0.0490 572  MET B N   
12844 C CA  . MET B 574  ? 0.3083 0.2230 0.2515 0.0442  -0.0184 -0.0498 572  MET B CA  
12845 C C   . MET B 574  ? 0.3501 0.2736 0.2992 0.0496  -0.0142 -0.0509 572  MET B C   
12846 O O   . MET B 574  ? 0.3250 0.2543 0.2811 0.0513  -0.0132 -0.0501 572  MET B O   
12847 C CB  . MET B 574  ? 0.3258 0.2472 0.2729 0.0383  -0.0174 -0.0470 572  MET B CB  
12848 C CG  . MET B 574  ? 0.3737 0.2879 0.3151 0.0327  -0.0211 -0.0457 572  MET B CG  
12849 S SD  . MET B 574  ? 0.3989 0.3226 0.3471 0.0264  -0.0200 -0.0420 572  MET B SD  
12850 C CE  . MET B 574  ? 0.4223 0.3368 0.3630 0.0203  -0.0246 -0.0407 572  MET B CE  
12851 N N   . LYS B 575  ? 0.2989 0.2239 0.2452 0.0522  -0.0119 -0.0528 573  LYS B N   
12852 C CA  . LYS B 575  ? 0.2911 0.2259 0.2433 0.0567  -0.0075 -0.0535 573  LYS B CA  
12853 C C   . LYS B 575  ? 0.2952 0.2411 0.2549 0.0529  -0.0046 -0.0508 573  LYS B C   
12854 O O   . LYS B 575  ? 0.3009 0.2482 0.2584 0.0505  -0.0035 -0.0504 573  LYS B O   
12855 C CB  . LYS B 575  ? 0.3004 0.2322 0.2461 0.0612  -0.0060 -0.0565 573  LYS B CB  
12856 C CG  . LYS B 575  ? 0.4267 0.3694 0.3784 0.0657  -0.0013 -0.0571 573  LYS B CG  
12857 C CD  . LYS B 575  ? 0.4497 0.3885 0.3941 0.0711  0.0001  -0.0604 573  LYS B CD  
12858 C CE  . LYS B 575  ? 0.5470 0.4975 0.4973 0.0754  0.0051  -0.0607 573  LYS B CE  
12859 N NZ  . LYS B 575  ? 0.5587 0.5154 0.5171 0.0788  0.0061  -0.0603 573  LYS B NZ  
12860 N N   . TRP B 576  ? 0.2771 0.2305 0.2454 0.0525  -0.0034 -0.0490 574  TRP B N   
12861 C CA  . TRP B 576  ? 0.2749 0.2384 0.2506 0.0493  -0.0008 -0.0465 574  TRP B CA  
12862 C C   . TRP B 576  ? 0.2848 0.2576 0.2655 0.0530  0.0034  -0.0470 574  TRP B C   
12863 O O   . TRP B 576  ? 0.2912 0.2668 0.2754 0.0572  0.0043  -0.0479 574  TRP B O   
12864 C CB  . TRP B 576  ? 0.2972 0.2636 0.2791 0.0467  -0.0020 -0.0443 574  TRP B CB  
12865 C CG  . TRP B 576  ? 0.2894 0.2483 0.2672 0.0425  -0.0057 -0.0434 574  TRP B CG  
12866 C CD1 . TRP B 576  ? 0.3087 0.2604 0.2838 0.0428  -0.0090 -0.0437 574  TRP B CD1 
12867 C CD2 . TRP B 576  ? 0.2518 0.2102 0.2278 0.0373  -0.0065 -0.0417 574  TRP B CD2 
12868 N NE1 . TRP B 576  ? 0.2735 0.2203 0.2453 0.0377  -0.0118 -0.0422 574  TRP B NE1 
12869 C CE2 . TRP B 576  ? 0.3070 0.2581 0.2795 0.0344  -0.0102 -0.0409 574  TRP B CE2 
12870 C CE3 . TRP B 576  ? 0.2904 0.2540 0.2675 0.0348  -0.0045 -0.0406 574  TRP B CE3 
12871 C CZ2 . TRP B 576  ? 0.2813 0.2308 0.2516 0.0291  -0.0118 -0.0392 574  TRP B CZ2 
12872 C CZ3 . TRP B 576  ? 0.3267 0.2884 0.3017 0.0298  -0.0062 -0.0389 574  TRP B CZ3 
12873 C CH2 . TRP B 576  ? 0.2941 0.2493 0.2660 0.0270  -0.0098 -0.0382 574  TRP B CH2 
12874 N N   . THR B 577  ? 0.2693 0.2469 0.2503 0.0514  0.0059  -0.0462 575  THR B N   
12875 C CA  . THR B 577  ? 0.2770 0.2638 0.2626 0.0542  0.0101  -0.0463 575  THR B CA  
12876 C C   . THR B 577  ? 0.2639 0.2586 0.2551 0.0501  0.0121  -0.0435 575  THR B C   
12877 O O   . THR B 577  ? 0.2634 0.2560 0.2534 0.0456  0.0105  -0.0420 575  THR B O   
12878 C CB  . THR B 577  ? 0.2909 0.2754 0.2698 0.0579  0.0117  -0.0487 575  THR B CB  
12879 O OG1 . THR B 577  ? 0.3057 0.2866 0.2788 0.0543  0.0110  -0.0483 575  THR B OG1 
12880 C CG2 . THR B 577  ? 0.3202 0.2958 0.2927 0.0623  0.0095  -0.0517 575  THR B CG2 
12881 N N   . ALA B 578  ? 0.2383 0.2423 0.2358 0.0517  0.0155  -0.0427 576  ALA B N   
12882 C CA  . ALA B 578  ? 0.2432 0.2546 0.2456 0.0484  0.0178  -0.0402 576  ALA B CA  
12883 C C   . ALA B 578  ? 0.2377 0.2560 0.2415 0.0515  0.0217  -0.0406 576  ALA B C   
12884 O O   . ALA B 578  ? 0.2598 0.2817 0.2665 0.0556  0.0230  -0.0417 576  ALA B O   
12885 C CB  . ALA B 578  ? 0.1991 0.2155 0.2097 0.0459  0.0174  -0.0380 576  ALA B CB  
12886 N N   . LEU B 579  ? 0.2494 0.2697 0.2509 0.0498  0.0235  -0.0397 577  LEU B N   
12887 C CA  . LEU B 579  ? 0.2381 0.2649 0.2402 0.0524  0.0273  -0.0399 577  LEU B CA  
12888 C C   . LEU B 579  ? 0.2285 0.2616 0.2343 0.0487  0.0293  -0.0370 577  LEU B C   
12889 O O   . LEU B 579  ? 0.2308 0.2619 0.2369 0.0445  0.0276  -0.0354 577  LEU B O   
12890 C CB  . LEU B 579  ? 0.3038 0.3249 0.2965 0.0553  0.0275  -0.0425 577  LEU B CB  
12891 C CG  . LEU B 579  ? 0.3266 0.3418 0.3156 0.0600  0.0260  -0.0456 577  LEU B CG  
12892 C CD1 . LEU B 579  ? 0.3679 0.3717 0.3491 0.0582  0.0219  -0.0468 577  LEU B CD1 
12893 C CD2 . LEU B 579  ? 0.3839 0.4013 0.3693 0.0651  0.0290  -0.0477 577  LEU B CD2 
12894 N N   . PRO B 580  ? 0.2018 0.2427 0.2106 0.0502  0.0330  -0.0362 578  PRO B N   
12895 C CA  . PRO B 580  ? 0.2060 0.2517 0.2166 0.0467  0.0349  -0.0335 578  PRO B CA  
12896 C C   . PRO B 580  ? 0.2241 0.2641 0.2263 0.0456  0.0342  -0.0341 578  PRO B C   
12897 O O   . PRO B 580  ? 0.2505 0.2894 0.2468 0.0485  0.0356  -0.0358 578  PRO B O   
12898 C CB  . PRO B 580  ? 0.2025 0.2574 0.2172 0.0491  0.0390  -0.0329 578  PRO B CB  
12899 C CG  . PRO B 580  ? 0.2322 0.2886 0.2499 0.0533  0.0389  -0.0348 578  PRO B CG  
12900 C CD  . PRO B 580  ? 0.2275 0.2737 0.2382 0.0550  0.0357  -0.0376 578  PRO B CD  
12901 N N   . GLN B 581  ? 0.2192 0.2556 0.2205 0.0416  0.0318  -0.0327 579  GLN B N   
12902 C CA  . GLN B 581  ? 0.2344 0.2655 0.2282 0.0399  0.0305  -0.0330 579  GLN B CA  
12903 C C   . GLN B 581  ? 0.2308 0.2671 0.2261 0.0374  0.0326  -0.0302 579  GLN B C   
12904 O O   . GLN B 581  ? 0.2615 0.2989 0.2603 0.0339  0.0316  -0.0280 579  GLN B O   
12905 C CB  . GLN B 581  ? 0.2220 0.2463 0.2140 0.0371  0.0265  -0.0330 579  GLN B CB  
12906 C CG  . GLN B 581  ? 0.2435 0.2616 0.2330 0.0393  0.0241  -0.0355 579  GLN B CG  
12907 C CD  . GLN B 581  ? 0.3016 0.3140 0.2824 0.0424  0.0238  -0.0384 579  GLN B CD  
12908 O OE1 . GLN B 581  ? 0.3051 0.3177 0.2811 0.0426  0.0252  -0.0386 579  GLN B OE1 
12909 N NE2 . GLN B 581  ? 0.3204 0.3272 0.2988 0.0451  0.0220  -0.0408 579  GLN B NE2 
12910 N N   . LEU B 582  ? 0.2265 0.2662 0.2191 0.0394  0.0356  -0.0305 580  LEU B N   
12911 C CA  . LEU B 582  ? 0.2282 0.2723 0.2213 0.0371  0.0376  -0.0278 580  LEU B CA  
12912 C C   . LEU B 582  ? 0.2690 0.3076 0.2545 0.0353  0.0357  -0.0279 580  LEU B C   
12913 O O   . LEU B 582  ? 0.2561 0.2876 0.2357 0.0359  0.0331  -0.0301 580  LEU B O   
12914 C CB  . LEU B 582  ? 0.2437 0.2945 0.2373 0.0397  0.0417  -0.0276 580  LEU B CB  
12915 C CG  . LEU B 582  ? 0.2867 0.3458 0.2897 0.0396  0.0440  -0.0258 580  LEU B CG  
12916 C CD1 . LEU B 582  ? 0.2982 0.3569 0.3062 0.0413  0.0426  -0.0273 580  LEU B CD1 
12917 C CD2 . LEU B 582  ? 0.3650 0.4313 0.3682 0.0419  0.0482  -0.0253 580  LEU B CD2 
12918 N N   . ALA B 583  ? 0.2174 0.2590 0.2031 0.0328  0.0368  -0.0253 581  ALA B N   
12919 C CA  . ALA B 583  ? 0.2815 0.3187 0.2604 0.0310  0.0350  -0.0250 581  ALA B CA  
12920 C C   . ALA B 583  ? 0.3078 0.3409 0.2776 0.0338  0.0353  -0.0278 581  ALA B C   
12921 O O   . ALA B 583  ? 0.3871 0.4139 0.3504 0.0328  0.0325  -0.0289 581  ALA B O   
12922 C CB  . ALA B 583  ? 0.2566 0.2983 0.2371 0.0284  0.0365  -0.0216 581  ALA B CB  
12923 N N   . THR B 584  ? 0.2710 0.3078 0.2402 0.0373  0.0385  -0.0290 582  THR B N   
12924 C CA  . THR B 584  ? 0.3018 0.3353 0.2622 0.0405  0.0393  -0.0317 582  THR B CA  
12925 C C   . THR B 584  ? 0.3180 0.3458 0.2756 0.0439  0.0377  -0.0354 582  THR B C   
12926 O O   . THR B 584  ? 0.3052 0.3295 0.2552 0.0472  0.0383  -0.0381 582  THR B O   
12927 C CB  . THR B 584  ? 0.3009 0.3419 0.2620 0.0429  0.0440  -0.0310 582  THR B CB  
12928 O OG1 . THR B 584  ? 0.3050 0.3524 0.2751 0.0440  0.0460  -0.0302 582  THR B OG1 
12929 C CG2 . THR B 584  ? 0.3824 0.4273 0.3437 0.0397  0.0453  -0.0276 582  THR B CG2 
12930 N N   . GLY B 585  ? 0.3130 0.3396 0.2761 0.0433  0.0358  -0.0355 583  GLY B N   
12931 C CA  . GLY B 585  ? 0.2902 0.3110 0.2508 0.0463  0.0340  -0.0387 583  GLY B CA  
12932 C C   . GLY B 585  ? 0.3231 0.3488 0.2920 0.0482  0.0354  -0.0386 583  GLY B C   
12933 O O   . GLY B 585  ? 0.2888 0.3225 0.2655 0.0469  0.0376  -0.0360 583  GLY B O   
12934 N N   . PRO B 586  ? 0.2960 0.3169 0.2634 0.0512  0.0338  -0.0413 584  PRO B N   
12935 C CA  . PRO B 586  ? 0.2927 0.3181 0.2680 0.0532  0.0347  -0.0413 584  PRO B CA  
12936 C C   . PRO B 586  ? 0.2785 0.3121 0.2563 0.0572  0.0391  -0.0415 584  PRO B C   
12937 O O   . PRO B 586  ? 0.3161 0.3490 0.2874 0.0603  0.0409  -0.0433 584  PRO B O   
12938 C CB  . PRO B 586  ? 0.2969 0.3135 0.2679 0.0556  0.0314  -0.0442 584  PRO B CB  
12939 C CG  . PRO B 586  ? 0.3228 0.3319 0.2830 0.0569  0.0305  -0.0467 584  PRO B CG  
12940 C CD  . PRO B 586  ? 0.2830 0.2936 0.2411 0.0529  0.0309  -0.0445 584  PRO B CD  
12941 N N   . ALA B 587  ? 0.3064 0.3480 0.2936 0.0570  0.0408  -0.0397 585  ALA B N   
12942 C CA  . ALA B 587  ? 0.3058 0.3567 0.2971 0.0603  0.0450  -0.0394 585  ALA B CA  
12943 C C   . ALA B 587  ? 0.2869 0.3382 0.2810 0.0648  0.0447  -0.0416 585  ALA B C   
12944 O O   . ALA B 587  ? 0.3010 0.3472 0.2966 0.0642  0.0414  -0.0423 585  ALA B O   
12945 C CB  . ALA B 587  ? 0.2847 0.3450 0.2848 0.0567  0.0471  -0.0356 585  ALA B CB  
12946 N N   . ALA B 588  ? 0.3087 0.3662 0.3034 0.0694  0.0482  -0.0427 586  ALA B N   
12947 C CA  . ALA B 588  ? 0.3587 0.4182 0.3568 0.0742  0.0484  -0.0446 586  ALA B CA  
12948 C C   . ALA B 588  ? 0.3482 0.4167 0.3580 0.0723  0.0491  -0.0418 586  ALA B C   
12949 O O   . ALA B 588  ? 0.3512 0.4262 0.3662 0.0682  0.0506  -0.0386 586  ALA B O   
12950 C CB  . ALA B 588  ? 0.3313 0.3947 0.3258 0.0802  0.0520  -0.0467 586  ALA B CB  
12951 N N   . GLY B 589  ? 0.3299 0.3984 0.3435 0.0754  0.0477  -0.0431 587  GLY B N   
12952 C CA  . GLY B 589  ? 0.3305 0.4076 0.3549 0.0739  0.0481  -0.0408 587  GLY B CA  
12953 C C   . GLY B 589  ? 0.3263 0.4023 0.3534 0.0781  0.0464  -0.0427 587  GLY B C   
12954 O O   . GLY B 589  ? 0.3334 0.4024 0.3540 0.0825  0.0451  -0.0459 587  GLY B O   
12955 N N   . GLU B 590  ? 0.3520 0.4347 0.3886 0.0766  0.0460  -0.0407 588  GLU B N   
12956 C CA  . GLU B 590  ? 0.3461 0.4286 0.3863 0.0801  0.0440  -0.0421 588  GLU B CA  
12957 C C   . GLU B 590  ? 0.3328 0.4034 0.3689 0.0783  0.0392  -0.0431 588  GLU B C   
12958 O O   . GLU B 590  ? 0.3310 0.3989 0.3680 0.0728  0.0374  -0.0412 588  GLU B O   
12959 C CB  . GLU B 590  ? 0.3239 0.4175 0.3756 0.0786  0.0450  -0.0395 588  GLU B CB  
12960 N N   . THR B 591  ? 0.3591 0.4227 0.3906 0.0829  0.0371  -0.0460 589  THR B N   
12961 C CA  . THR B 591  ? 0.3508 0.4024 0.3772 0.0813  0.0326  -0.0471 589  THR B CA  
12962 C C   . THR B 591  ? 0.3764 0.4286 0.4085 0.0825  0.0300  -0.0469 589  THR B C   
12963 O O   . THR B 591  ? 0.3558 0.4129 0.3912 0.0876  0.0310  -0.0480 589  THR B O   
12964 C CB  . THR B 591  ? 0.4038 0.4450 0.4193 0.0850  0.0314  -0.0504 589  THR B CB  
12965 O OG1 . THR B 591  ? 0.4010 0.4414 0.4110 0.0833  0.0335  -0.0504 589  THR B OG1 
12966 C CG2 . THR B 591  ? 0.4209 0.4498 0.4313 0.0830  0.0265  -0.0512 589  THR B CG2 
12967 N N   . ARG B 592  ? 0.3176 0.3651 0.3506 0.0779  0.0268  -0.0455 590  ARG B N   
12968 C CA  . ARG B 592  ? 0.3390 0.3863 0.3769 0.0781  0.0240  -0.0451 590  ARG B CA  
12969 C C   . ARG B 592  ? 0.3671 0.4018 0.3983 0.0766  0.0197  -0.0460 590  ARG B C   
12970 O O   . ARG B 592  ? 0.3002 0.3280 0.3249 0.0737  0.0188  -0.0462 590  ARG B O   
12971 C CB  . ARG B 592  ? 0.3219 0.3774 0.3689 0.0734  0.0244  -0.0419 590  ARG B CB  
12972 N N   . THR B 593  ? 0.3160 0.3480 0.3490 0.0783  0.0168  -0.0464 591  THR B N   
12973 C CA  A THR B 593  ? 0.3204 0.3407 0.3473 0.0768  0.0125  -0.0470 591  THR B CA  
12974 C CA  B THR B 593  ? 0.3205 0.3408 0.3474 0.0767  0.0126  -0.0470 591  THR B CA  
12975 C C   . THR B 593  ? 0.3089 0.3299 0.3399 0.0710  0.0107  -0.0445 591  THR B C   
12976 O O   . THR B 593  ? 0.3418 0.3709 0.3810 0.0702  0.0113  -0.0429 591  THR B O   
12977 C CB  A THR B 593  ? 0.3533 0.3691 0.3787 0.0822  0.0102  -0.0489 591  THR B CB  
12978 C CB  B THR B 593  ? 0.3534 0.3688 0.3785 0.0820  0.0102  -0.0490 591  THR B CB  
12979 O OG1 A THR B 593  ? 0.3737 0.3860 0.3930 0.0875  0.0115  -0.0517 591  THR B OG1 
12980 O OG1 B THR B 593  ? 0.3240 0.3461 0.3575 0.0824  0.0095  -0.0476 591  THR B OG1 
12981 C CG2 A THR B 593  ? 0.3348 0.3397 0.3555 0.0800  0.0057  -0.0489 591  THR B CG2 
12982 C CG2 B THR B 593  ? 0.3650 0.3819 0.3875 0.0885  0.0126  -0.0515 591  THR B CG2 
12983 N N   . VAL B 594  ? 0.2649 0.2778 0.2903 0.0669  0.0085  -0.0441 592  VAL B N   
12984 C CA  . VAL B 594  ? 0.2551 0.2678 0.2832 0.0616  0.0067  -0.0419 592  VAL B CA  
12985 C C   . VAL B 594  ? 0.2806 0.2858 0.3063 0.0622  0.0028  -0.0423 592  VAL B C   
12986 O O   . VAL B 594  ? 0.2764 0.2720 0.2945 0.0634  0.0006  -0.0438 592  VAL B O   
12987 C CB  . VAL B 594  ? 0.2582 0.2677 0.2822 0.0568  0.0069  -0.0410 592  VAL B CB  
12988 C CG1 . VAL B 594  ? 0.1901 0.1996 0.2168 0.0517  0.0052  -0.0388 592  VAL B CG1 
12989 C CG2 . VAL B 594  ? 0.2557 0.2721 0.2814 0.0565  0.0108  -0.0405 592  VAL B CG2 
12990 N N   . LEU B 595  ? 0.3151 0.3241 0.3468 0.0612  0.0016  -0.0410 593  LEU B N   
12991 C CA  . LEU B 595  ? 0.3048 0.3078 0.3349 0.0622  -0.0020 -0.0412 593  LEU B CA  
12992 C C   . LEU B 595  ? 0.2739 0.2739 0.3036 0.0568  -0.0042 -0.0393 593  LEU B C   
12993 O O   . LEU B 595  ? 0.2727 0.2777 0.3059 0.0528  -0.0028 -0.0377 593  LEU B O   
12994 C CB  . LEU B 595  ? 0.2424 0.2520 0.2795 0.0659  -0.0021 -0.0412 593  LEU B CB  
12995 C CG  . LEU B 595  ? 0.2916 0.3049 0.3296 0.0719  0.0001  -0.0431 593  LEU B CG  
12996 C CD1 . LEU B 595  ? 0.3347 0.3558 0.3806 0.0750  -0.0001 -0.0426 593  LEU B CD1 
12997 C CD2 . LEU B 595  ? 0.2982 0.3009 0.3274 0.0756  -0.0017 -0.0454 593  LEU B CD2 
12998 N N   . ASN B 596  ? 0.2290 0.2206 0.2541 0.0568  -0.0078 -0.0395 594  ASN B N   
12999 C CA  . ASN B 596  ? 0.2929 0.2817 0.3175 0.0522  -0.0101 -0.0377 594  ASN B CA  
13000 C C   . ASN B 596  ? 0.2543 0.2498 0.2863 0.0521  -0.0104 -0.0365 594  ASN B C   
13001 O O   . ASN B 596  ? 0.2536 0.2493 0.2874 0.0558  -0.0118 -0.0372 594  ASN B O   
13002 C CB  . ASN B 596  ? 0.2845 0.2622 0.3017 0.0525  -0.0138 -0.0383 594  ASN B CB  
13003 C CG  . ASN B 596  ? 0.2928 0.2668 0.3079 0.0475  -0.0160 -0.0364 594  ASN B CG  
13004 O OD1 . ASN B 596  ? 0.2606 0.2402 0.2806 0.0449  -0.0155 -0.0349 594  ASN B OD1 
13005 N ND2 . ASN B 596  ? 0.2811 0.2456 0.2887 0.0460  -0.0185 -0.0365 594  ASN B ND2 
13006 N N   . PRO B 597  ? 0.2334 0.2343 0.2696 0.0482  -0.0093 -0.0349 595  PRO B N   
13007 C CA  . PRO B 597  ? 0.2706 0.2774 0.3134 0.0480  -0.0099 -0.0339 595  PRO B CA  
13008 C C   . PRO B 597  ? 0.2189 0.2202 0.2596 0.0481  -0.0137 -0.0335 595  PRO B C   
13009 O O   . PRO B 597  ? 0.2641 0.2694 0.3096 0.0495  -0.0147 -0.0332 595  PRO B O   
13010 C CB  . PRO B 597  ? 0.2612 0.2724 0.3069 0.0433  -0.0084 -0.0323 595  PRO B CB  
13011 C CG  . PRO B 597  ? 0.2758 0.2820 0.3156 0.0407  -0.0079 -0.0323 595  PRO B CG  
13012 C CD  . PRO B 597  ? 0.2189 0.2210 0.2542 0.0441  -0.0075 -0.0340 595  PRO B CD  
13013 N N   . GLY B 598  ? 0.2485 0.2409 0.2820 0.0465  -0.0158 -0.0335 596  GLY B N   
13014 C CA  . GLY B 598  ? 0.2501 0.2365 0.2808 0.0467  -0.0195 -0.0330 596  GLY B CA  
13015 C C   . GLY B 598  ? 0.2652 0.2470 0.2936 0.0517  -0.0213 -0.0344 596  GLY B C   
13016 O O   . GLY B 598  ? 0.2687 0.2462 0.2955 0.0526  -0.0244 -0.0340 596  GLY B O   
13017 N N   . ASP B 599  ? 0.2566 0.2393 0.2847 0.0553  -0.0194 -0.0361 597  ASP B N   
13018 C CA  . ASP B 599  ? 0.2893 0.2674 0.3148 0.0607  -0.0210 -0.0378 597  ASP B CA  
13019 C C   . ASP B 599  ? 0.3064 0.2886 0.3332 0.0645  -0.0178 -0.0395 597  ASP B C   
13020 O O   . ASP B 599  ? 0.2893 0.2670 0.3106 0.0640  -0.0168 -0.0405 597  ASP B O   
13021 C CB  . ASP B 599  ? 0.2999 0.2655 0.3161 0.0600  -0.0242 -0.0380 597  ASP B CB  
13022 C CG  . ASP B 599  ? 0.3870 0.3463 0.3998 0.0657  -0.0264 -0.0397 597  ASP B CG  
13023 O OD1 . ASP B 599  ? 0.3636 0.3285 0.3808 0.0708  -0.0249 -0.0410 597  ASP B OD1 
13024 O OD2 . ASP B 599  ? 0.3995 0.3481 0.4051 0.0650  -0.0297 -0.0396 597  ASP B OD2 
13025 N N   . HIS B 600  ? 0.2896 0.2806 0.3234 0.0681  -0.0162 -0.0399 598  HIS B N   
13026 C CA  . HIS B 600  ? 0.3138 0.3104 0.3497 0.0716  -0.0127 -0.0413 598  HIS B CA  
13027 C C   . HIS B 600  ? 0.3283 0.3173 0.3575 0.0767  -0.0134 -0.0437 598  HIS B C   
13028 O O   . HIS B 600  ? 0.3273 0.3194 0.3564 0.0795  -0.0105 -0.0452 598  HIS B O   
13029 C CB  . HIS B 600  ? 0.2861 0.2947 0.3317 0.0740  -0.0110 -0.0408 598  HIS B CB  
13030 C CG  . HIS B 600  ? 0.3076 0.3245 0.3595 0.0691  -0.0092 -0.0389 598  HIS B CG  
13031 N ND1 . HIS B 600  ? 0.3270 0.3551 0.3877 0.0699  -0.0074 -0.0381 598  HIS B ND1 
13032 C CD2 . HIS B 600  ? 0.2806 0.2959 0.3310 0.0634  -0.0091 -0.0375 598  HIS B CD2 
13033 C CE1 . HIS B 600  ? 0.3039 0.3363 0.3679 0.0648  -0.0063 -0.0364 598  HIS B CE1 
13034 N NE2 . HIS B 600  ? 0.3034 0.3282 0.3614 0.0611  -0.0073 -0.0361 598  HIS B NE2 
13035 N N   . ARG B 601  ? 0.3059 0.2847 0.3293 0.0779  -0.0172 -0.0442 599  ARG B N   
13036 C CA  . ARG B 601  ? 0.3254 0.2951 0.3411 0.0822  -0.0183 -0.0466 599  ARG B CA  
13037 C C   . ARG B 601  ? 0.3206 0.2831 0.3287 0.0787  -0.0179 -0.0470 599  ARG B C   
13038 O O   . ARG B 601  ? 0.3577 0.3137 0.3594 0.0820  -0.0179 -0.0492 599  ARG B O   
13039 C CB  . ARG B 601  ? 0.3897 0.3499 0.4011 0.0844  -0.0228 -0.0467 599  ARG B CB  
13040 C CG  . ARG B 601  ? 0.3958 0.3624 0.4143 0.0875  -0.0237 -0.0461 599  ARG B CG  
13041 C CD  . ARG B 601  ? 0.4180 0.3747 0.4318 0.0881  -0.0286 -0.0456 599  ARG B CD  
13042 N NE  . ARG B 601  ? 0.4193 0.3706 0.4296 0.0813  -0.0305 -0.0435 599  ARG B NE  
13043 C CZ  . ARG B 601  ? 0.5041 0.4461 0.5093 0.0800  -0.0347 -0.0426 599  ARG B CZ  
13044 N NH1 . ARG B 601  ? 0.4535 0.3901 0.4566 0.0851  -0.0376 -0.0434 599  ARG B NH1 
13045 N NH2 . ARG B 601  ? 0.4574 0.3958 0.4597 0.0737  -0.0359 -0.0406 599  ARG B NH2 
13046 N N   . ASP B 602  ? 0.3284 0.2920 0.3370 0.0723  -0.0176 -0.0451 600  ASP B N   
13047 C CA  . ASP B 602  ? 0.3414 0.2986 0.3431 0.0684  -0.0177 -0.0451 600  ASP B CA  
13048 C C   . ASP B 602  ? 0.3439 0.3090 0.3485 0.0681  -0.0134 -0.0455 600  ASP B C   
13049 O O   . ASP B 602  ? 0.3537 0.3272 0.3643 0.0647  -0.0113 -0.0438 600  ASP B O   
13050 C CB  . ASP B 602  ? 0.3549 0.3096 0.3558 0.0620  -0.0197 -0.0427 600  ASP B CB  
13051 C CG  . ASP B 602  ? 0.3662 0.3148 0.3605 0.0577  -0.0200 -0.0425 600  ASP B CG  
13052 O OD1 . ASP B 602  ? 0.3667 0.3093 0.3548 0.0598  -0.0201 -0.0444 600  ASP B OD1 
13053 O OD2 . ASP B 602  ? 0.3487 0.2989 0.3440 0.0524  -0.0201 -0.0405 600  ASP B OD2 
13054 N N   . VAL B 603  ? 0.3205 0.2825 0.3204 0.0716  -0.0122 -0.0478 601  VAL B N   
13055 C CA  . VAL B 603  ? 0.3271 0.2959 0.3287 0.0716  -0.0082 -0.0482 601  VAL B CA  
13056 C C   . VAL B 603  ? 0.3324 0.2970 0.3291 0.0661  -0.0085 -0.0474 601  VAL B C   
13057 O O   . VAL B 603  ? 0.3833 0.3375 0.3717 0.0653  -0.0110 -0.0483 601  VAL B O   
13058 C CB  . VAL B 603  ? 0.3547 0.3222 0.3529 0.0780  -0.0067 -0.0511 601  VAL B CB  
13059 C CG1 . VAL B 603  ? 0.3533 0.3262 0.3514 0.0774  -0.0029 -0.0515 601  VAL B CG1 
13060 C CG2 . VAL B 603  ? 0.3639 0.3381 0.3686 0.0835  -0.0060 -0.0516 601  VAL B CG2 
13061 N N   . VAL B 604  ? 0.2772 0.2497 0.2790 0.0621  -0.0062 -0.0455 602  VAL B N   
13062 C CA  . VAL B 604  ? 0.2589 0.2284 0.2569 0.0568  -0.0065 -0.0444 602  VAL B CA  
13063 C C   . VAL B 604  ? 0.3066 0.2763 0.3007 0.0577  -0.0041 -0.0458 602  VAL B C   
13064 O O   . VAL B 604  ? 0.3184 0.2810 0.3056 0.0554  -0.0055 -0.0462 602  VAL B O   
13065 C CB  . VAL B 604  ? 0.2769 0.2540 0.2816 0.0521  -0.0054 -0.0418 602  VAL B CB  
13066 C CG1 . VAL B 604  ? 0.2448 0.2189 0.2457 0.0469  -0.0060 -0.0406 602  VAL B CG1 
13067 C CG2 . VAL B 604  ? 0.2882 0.2651 0.2963 0.0515  -0.0077 -0.0406 602  VAL B CG2 
13068 N N   . GLY B 605  ? 0.2576 0.2354 0.2560 0.0610  -0.0006 -0.0464 603  GLY B N   
13069 C CA  . GLY B 605  ? 0.2702 0.2490 0.2651 0.0618  0.0019  -0.0475 603  GLY B CA  
13070 C C   . GLY B 605  ? 0.3226 0.3117 0.3236 0.0654  0.0059  -0.0478 603  GLY B C   
13071 O O   . GLY B 605  ? 0.2996 0.2936 0.3063 0.0683  0.0063  -0.0478 603  GLY B O   
13072 N N   . SER B 606  ? 0.2868 0.2797 0.2866 0.0651  0.0088  -0.0479 604  SER B N   
13073 C CA  . SER B 606  ? 0.2971 0.3001 0.3023 0.0683  0.0129  -0.0480 604  SER B CA  
13074 C C   . SER B 606  ? 0.3159 0.3254 0.3236 0.0644  0.0156  -0.0460 604  SER B C   
13075 O O   . SER B 606  ? 0.2851 0.2901 0.2878 0.0610  0.0149  -0.0456 604  SER B O   
13076 C CB  . SER B 606  ? 0.3735 0.3741 0.3733 0.0744  0.0141  -0.0510 604  SER B CB  
13077 O OG  . SER B 606  ? 0.4415 0.4380 0.4340 0.0734  0.0149  -0.0519 604  SER B OG  
13078 N N   . VAL B 607  ? 0.2595 0.2798 0.2752 0.0647  0.0186  -0.0445 605  VAL B N   
13079 C CA  . VAL B 607  ? 0.2270 0.2539 0.2458 0.0611  0.0212  -0.0424 605  VAL B CA  
13080 C C   . VAL B 607  ? 0.2857 0.3205 0.3064 0.0645  0.0253  -0.0428 605  VAL B C   
13081 O O   . VAL B 607  ? 0.2833 0.3236 0.3085 0.0684  0.0265  -0.0434 605  VAL B O   
13082 C CB  . VAL B 607  ? 0.2663 0.2985 0.2930 0.0570  0.0208  -0.0397 605  VAL B CB  
13083 C CG1 . VAL B 607  ? 0.2945 0.3328 0.3286 0.0597  0.0210  -0.0395 605  VAL B CG1 
13084 C CG2 . VAL B 607  ? 0.2216 0.2603 0.2512 0.0537  0.0236  -0.0375 605  VAL B CG2 
13085 N N   . THR B 608  ? 0.2620 0.2977 0.2791 0.0632  0.0274  -0.0425 606  THR B N   
13086 C CA  . THR B 608  ? 0.2706 0.3149 0.2899 0.0654  0.0316  -0.0422 606  THR B CA  
13087 C C   . THR B 608  ? 0.2385 0.2906 0.2645 0.0607  0.0333  -0.0388 606  THR B C   
13088 O O   . THR B 608  ? 0.2217 0.2708 0.2456 0.0564  0.0324  -0.0375 606  THR B O   
13089 C CB  . THR B 608  ? 0.2890 0.3289 0.2993 0.0672  0.0328  -0.0440 606  THR B CB  
13090 O OG1 . THR B 608  ? 0.3038 0.3358 0.3078 0.0716  0.0309  -0.0472 606  THR B OG1 
13091 C CG2 . THR B 608  ? 0.2850 0.3344 0.2974 0.0692  0.0374  -0.0435 606  THR B CG2 
13092 N N   . GLU B 609  ? 0.2365 0.2983 0.2705 0.0615  0.0356  -0.0375 607  GLU B N   
13093 C CA  . GLU B 609  ? 0.2817 0.3498 0.3222 0.0568  0.0365  -0.0343 607  GLU B CA  
13094 C C   . GLU B 609  ? 0.2136 0.2881 0.2539 0.0562  0.0404  -0.0329 607  GLU B C   
13095 O O   . GLU B 609  ? 0.2632 0.3397 0.3002 0.0600  0.0428  -0.0343 607  GLU B O   
13096 C CB  . GLU B 609  ? 0.2958 0.3705 0.3455 0.0569  0.0362  -0.0331 607  GLU B CB  
13097 C CG  . GLU B 609  ? 0.2758 0.3434 0.3252 0.0558  0.0320  -0.0337 607  GLU B CG  
13098 C CD  . GLU B 609  ? 0.3823 0.4550 0.4398 0.0559  0.0310  -0.0329 607  GLU B CD  
13099 O OE1 . GLU B 609  ? 0.3578 0.4394 0.4211 0.0580  0.0333  -0.0323 607  GLU B OE1 
13100 O OE2 . GLU B 609  ? 0.3271 0.3949 0.3849 0.0539  0.0278  -0.0327 607  GLU B OE2 
13101 N N   . THR B 610  ? 0.2520 0.3290 0.2954 0.0514  0.0407  -0.0301 608  THR B N   
13102 C CA  . THR B 610  ? 0.2274 0.3083 0.2693 0.0497  0.0436  -0.0284 608  THR B CA  
13103 C C   . THR B 610  ? 0.2365 0.3286 0.2854 0.0501  0.0471  -0.0264 608  THR B C   
13104 O O   . THR B 610  ? 0.2426 0.3396 0.2993 0.0482  0.0466  -0.0247 608  THR B O   
13105 C CB  . THR B 610  ? 0.1943 0.2719 0.2358 0.0444  0.0421  -0.0262 608  THR B CB  
13106 O OG1 . THR B 610  ? 0.2287 0.2969 0.2651 0.0437  0.0387  -0.0277 608  THR B OG1 
13107 C CG2 . THR B 610  ? 0.2072 0.2869 0.2454 0.0429  0.0447  -0.0246 608  THR B CG2 
13108 N N   . SER B 611  ? 0.2125 0.3090 0.2587 0.0523  0.0505  -0.0266 609  SER B N   
13109 C CA  . SER B 611  ? 0.2968 0.4046 0.3496 0.0519  0.0541  -0.0242 609  SER B CA  
13110 C C   . SER B 611  ? 0.3092 0.4188 0.3645 0.0461  0.0543  -0.0206 609  SER B C   
13111 O O   . SER B 611  ? 0.2350 0.3378 0.2853 0.0435  0.0528  -0.0203 609  SER B O   
13112 C CB  . SER B 611  ? 0.2726 0.3847 0.3212 0.0559  0.0579  -0.0252 609  SER B CB  
13113 O OG  . SER B 611  ? 0.2804 0.3891 0.3222 0.0539  0.0589  -0.0246 609  SER B OG  
13114 N N   . GLU B 612  ? 0.3011 0.4198 0.3644 0.0441  0.0561  -0.0179 610  GLU B N   
13115 C CA  . GLU B 612  ? 0.3100 0.4300 0.3757 0.0387  0.0562  -0.0144 610  GLU B CA  
13116 C C   . GLU B 612  ? 0.2690 0.3885 0.3284 0.0380  0.0585  -0.0134 610  GLU B C   
13117 O O   . GLU B 612  ? 0.2955 0.4105 0.3525 0.0343  0.0574  -0.0117 610  GLU B O   
13118 C CB  . GLU B 612  ? 0.3463 0.4762 0.4215 0.0366  0.0575  -0.0116 610  GLU B CB  
13119 C CG  . GLU B 612  ? 0.3644 0.4939 0.4458 0.0361  0.0545  -0.0121 610  GLU B CG  
13120 C CD  . GLU B 612  ? 0.5162 0.6555 0.6070 0.0336  0.0555  -0.0092 610  GLU B CD  
13121 O OE1 . GLU B 612  ? 0.5853 0.7298 0.6780 0.0305  0.0578  -0.0062 610  GLU B OE1 
13122 O OE2 . GLU B 612  ? 0.4736 0.6153 0.5700 0.0345  0.0539  -0.0099 610  GLU B OE2 
13123 N N   . GLU B 613  ? 0.2749 0.3987 0.3313 0.0417  0.0618  -0.0145 611  GLU B N   
13124 C CA  . GLU B 613  ? 0.2442 0.3670 0.2936 0.0414  0.0639  -0.0138 611  GLU B CA  
13125 C C   . GLU B 613  ? 0.2634 0.3749 0.3044 0.0411  0.0610  -0.0157 611  GLU B C   
13126 O O   . GLU B 613  ? 0.2672 0.3759 0.3043 0.0382  0.0610  -0.0140 611  GLU B O   
13127 C CB  . GLU B 613  ? 0.3029 0.4318 0.3498 0.0461  0.0678  -0.0153 611  GLU B CB  
13128 N N   . ASP B 614  ? 0.2683 0.3733 0.3065 0.0439  0.0585  -0.0190 612  ASP B N   
13129 C CA  . ASP B 614  ? 0.2719 0.3665 0.3025 0.0432  0.0555  -0.0206 612  ASP B CA  
13130 C C   . ASP B 614  ? 0.2671 0.3577 0.3004 0.0385  0.0525  -0.0187 612  ASP B C   
13131 O O   . ASP B 614  ? 0.2304 0.3148 0.2583 0.0366  0.0509  -0.0185 612  ASP B O   
13132 C CB  . ASP B 614  ? 0.2419 0.3304 0.2686 0.0473  0.0535  -0.0245 612  ASP B CB  
13133 C CG  . ASP B 614  ? 0.3154 0.4044 0.3358 0.0521  0.0559  -0.0270 612  ASP B CG  
13134 O OD1 . ASP B 614  ? 0.3692 0.4600 0.3853 0.0518  0.0583  -0.0261 612  ASP B OD1 
13135 O OD2 . ASP B 614  ? 0.3571 0.4444 0.3767 0.0564  0.0554  -0.0298 612  ASP B OD2 
13136 N N   . ALA B 615  ? 0.2372 0.3310 0.2784 0.0369  0.0516  -0.0174 613  ALA B N   
13137 C CA  . ALA B 615  ? 0.2514 0.3420 0.2952 0.0325  0.0491  -0.0155 613  ALA B CA  
13138 C C   . ALA B 615  ? 0.2530 0.3453 0.2959 0.0292  0.0505  -0.0124 613  ALA B C   
13139 O O   . ALA B 615  ? 0.2092 0.2960 0.2489 0.0268  0.0486  -0.0117 613  ALA B O   
13140 C CB  . ALA B 615  ? 0.2491 0.3433 0.3014 0.0313  0.0481  -0.0146 613  ALA B CB  
13141 N N   . ARG B 616  ? 0.2343 0.3344 0.2798 0.0290  0.0539  -0.0105 614  ARG B N   
13142 C CA  . ARG B 616  ? 0.2459 0.3475 0.2901 0.0259  0.0553  -0.0073 614  ARG B CA  
13143 C C   . ARG B 616  ? 0.2750 0.3718 0.3101 0.0269  0.0555  -0.0083 614  ARG B C   
13144 O O   . ARG B 616  ? 0.2690 0.3622 0.3013 0.0241  0.0545  -0.0065 614  ARG B O   
13145 C CB  . ARG B 616  ? 0.2899 0.4013 0.3387 0.0254  0.0589  -0.0049 614  ARG B CB  
13146 C CG  . ARG B 616  ? 0.3465 0.4623 0.4044 0.0228  0.0583  -0.0029 614  ARG B CG  
13147 C CD  . ARG B 616  ? 0.3477 0.4735 0.4103 0.0215  0.0618  0.0000  614  ARG B CD  
13148 N NE  . ARG B 616  ? 0.4106 0.5434 0.4745 0.0257  0.0646  -0.0017 614  ARG B NE  
13149 C CZ  . ARG B 616  ? 0.4537 0.5910 0.5239 0.0274  0.0643  -0.0027 614  ARG B CZ  
13150 N NH1 . ARG B 616  ? 0.4673 0.6027 0.5430 0.0251  0.0613  -0.0023 614  ARG B NH1 
13151 N NH2 . ARG B 616  ? 0.4453 0.5890 0.5162 0.0317  0.0670  -0.0043 614  ARG B NH2 
13152 N N   . ARG B 617  ? 0.2642 0.3605 0.2944 0.0309  0.0566  -0.0111 615  ARG B N   
13153 C CA  . ARG B 617  ? 0.2688 0.3598 0.2897 0.0319  0.0565  -0.0123 615  ARG B CA  
13154 C C   . ARG B 617  ? 0.2566 0.3390 0.2745 0.0300  0.0525  -0.0130 615  ARG B C   
13155 O O   . ARG B 617  ? 0.2634 0.3425 0.2764 0.0282  0.0518  -0.0119 615  ARG B O   
13156 C CB  . ARG B 617  ? 0.2993 0.3900 0.3153 0.0369  0.0578  -0.0158 615  ARG B CB  
13157 C CG  . ARG B 617  ? 0.3231 0.4080 0.3290 0.0381  0.0575  -0.0174 615  ARG B CG  
13158 C CD  . ARG B 617  ? 0.4493 0.5365 0.4503 0.0428  0.0603  -0.0199 615  ARG B CD  
13159 N NE  . ARG B 617  ? 0.5122 0.5963 0.5127 0.0468  0.0591  -0.0236 615  ARG B NE  
13160 C CZ  . ARG B 617  ? 0.5937 0.6694 0.5866 0.0489  0.0568  -0.0268 615  ARG B CZ  
13161 N NH1 . ARG B 617  ? 0.6341 0.7037 0.6192 0.0474  0.0553  -0.0270 615  ARG B NH1 
13162 N NH2 . ARG B 617  ? 0.5804 0.6534 0.5732 0.0526  0.0557  -0.0299 615  ARG B NH2 
13163 N N   . ALA B 618  ? 0.2230 0.3021 0.2439 0.0303  0.0498  -0.0146 616  ALA B N   
13164 C CA  . ALA B 618  ? 0.2240 0.2956 0.2424 0.0285  0.0461  -0.0151 616  ALA B CA  
13165 C C   . ALA B 618  ? 0.2189 0.2906 0.2395 0.0245  0.0454  -0.0119 616  ALA B C   
13166 O O   . ALA B 618  ? 0.2307 0.2976 0.2469 0.0231  0.0435  -0.0116 616  ALA B O   
13167 C CB  . ALA B 618  ? 0.2248 0.2938 0.2469 0.0293  0.0437  -0.0169 616  ALA B CB  
13168 N N   . VAL B 619  ? 0.2232 0.3000 0.2505 0.0227  0.0466  -0.0095 617  VAL B N   
13169 C CA  . VAL B 619  ? 0.2074 0.2834 0.2365 0.0191  0.0457  -0.0065 617  VAL B CA  
13170 C C   . VAL B 619  ? 0.2752 0.3515 0.2991 0.0182  0.0472  -0.0047 617  VAL B C   
13171 O O   . VAL B 619  ? 0.2435 0.3161 0.2649 0.0163  0.0455  -0.0034 617  VAL B O   
13172 C CB  . VAL B 619  ? 0.2086 0.2893 0.2457 0.0171  0.0464  -0.0043 617  VAL B CB  
13173 C CG1 . VAL B 619  ? 0.2521 0.3311 0.2904 0.0136  0.0453  -0.0014 617  VAL B CG1 
13174 C CG2 . VAL B 619  ? 0.1982 0.2779 0.2399 0.0179  0.0444  -0.0062 617  VAL B CG2 
13175 N N   . ARG B 620  ? 0.2509 0.3319 0.2730 0.0198  0.0504  -0.0045 618  ARG B N   
13176 C CA  . ARG B 620  ? 0.2830 0.3641 0.2992 0.0192  0.0518  -0.0030 618  ARG B CA  
13177 C C   . ARG B 620  ? 0.2711 0.3455 0.2795 0.0201  0.0495  -0.0050 618  ARG B C   
13178 O O   . ARG B 620  ? 0.2716 0.3435 0.2764 0.0183  0.0486  -0.0033 618  ARG B O   
13179 C CB  . ARG B 620  ? 0.3331 0.4205 0.3481 0.0211  0.0557  -0.0028 618  ARG B CB  
13180 C CG  . ARG B 620  ? 0.3659 0.4609 0.3886 0.0196  0.0581  -0.0003 618  ARG B CG  
13181 C CD  . ARG B 620  ? 0.4222 0.5243 0.4433 0.0210  0.0623  0.0007  618  ARG B CD  
13182 N NE  . ARG B 620  ? 0.4967 0.5995 0.5141 0.0255  0.0636  -0.0029 618  ARG B NE  
13183 C CZ  . ARG B 620  ? 0.3985 0.5062 0.4203 0.0281  0.0651  -0.0045 618  ARG B CZ  
13184 N NH1 . ARG B 620  ? 0.4005 0.5136 0.4310 0.0264  0.0655  -0.0027 618  ARG B NH1 
13185 N NH2 . ARG B 620  ? 0.4571 0.5642 0.4745 0.0326  0.0660  -0.0079 618  ARG B NH2 
13186 N N   . LEU B 621  ? 0.2597 0.3310 0.2658 0.0228  0.0484  -0.0084 619  LEU B N   
13187 C CA  . LEU B 621  ? 0.2503 0.3150 0.2492 0.0233  0.0459  -0.0103 619  LEU B CA  
13188 C C   . LEU B 621  ? 0.2650 0.3255 0.2654 0.0205  0.0425  -0.0092 619  LEU B C   
13189 O O   . LEU B 621  ? 0.2658 0.3228 0.2612 0.0195  0.0408  -0.0088 619  LEU B O   
13190 C CB  . LEU B 621  ? 0.2504 0.3120 0.2466 0.0265  0.0451  -0.0142 619  LEU B CB  
13191 C CG  . LEU B 621  ? 0.2837 0.3482 0.2765 0.0301  0.0481  -0.0160 619  LEU B CG  
13192 C CD1 . LEU B 621  ? 0.3049 0.3663 0.2968 0.0333  0.0471  -0.0197 619  LEU B CD1 
13193 C CD2 . LEU B 621  ? 0.3414 0.4039 0.3254 0.0305  0.0488  -0.0162 619  LEU B CD2 
13194 N N   . ALA B 622  ? 0.2027 0.2637 0.2098 0.0195  0.0414  -0.0088 620  ALA B N   
13195 C CA  . ALA B 622  ? 0.2432 0.3009 0.2519 0.0171  0.0385  -0.0077 620  ALA B CA  
13196 C C   . ALA B 622  ? 0.2575 0.3163 0.2660 0.0148  0.0389  -0.0043 620  ALA B C   
13197 O O   . ALA B 622  ? 0.2362 0.2917 0.2420 0.0136  0.0368  -0.0036 620  ALA B O   
13198 C CB  . ALA B 622  ? 0.1812 0.2395 0.1970 0.0166  0.0375  -0.0079 620  ALA B CB  
13199 N N   . ALA B 623  ? 0.2407 0.3042 0.2520 0.0142  0.0416  -0.0022 621  ALA B N   
13200 C CA  . ALA B 623  ? 0.2732 0.3373 0.2839 0.0120  0.0420  0.0012  621  ALA B CA  
13201 C C   . ALA B 623  ? 0.2814 0.3436 0.2845 0.0123  0.0418  0.0014  621  ALA B C   
13202 O O   . ALA B 623  ? 0.2777 0.3376 0.2790 0.0107  0.0402  0.0033  621  ALA B O   
13203 C CB  . ALA B 623  ? 0.2483 0.3181 0.2629 0.0111  0.0450  0.0035  621  ALA B CB  
13204 N N   . ASP B 624  ? 0.2739 0.3368 0.2721 0.0144  0.0434  -0.0006 622  ASP B N   
13205 C CA  . ASP B 624  ? 0.3093 0.3700 0.2995 0.0148  0.0431  -0.0007 622  ASP B CA  
13206 C C   . ASP B 624  ? 0.2861 0.3414 0.2733 0.0142  0.0394  -0.0017 622  ASP B C   
13207 O O   . ASP B 624  ? 0.3357 0.3892 0.3184 0.0132  0.0381  -0.0004 622  ASP B O   
13208 C CB  . ASP B 624  ? 0.3511 0.4129 0.3365 0.0176  0.0452  -0.0033 622  ASP B CB  
13209 C CG  . ASP B 624  ? 0.4376 0.5056 0.4244 0.0182  0.0493  -0.0018 622  ASP B CG  
13210 O OD1 . ASP B 624  ? 0.5177 0.5886 0.5069 0.0160  0.0504  0.0017  622  ASP B OD1 
13211 O OD2 . ASP B 624  ? 0.5201 0.5902 0.5054 0.0210  0.0513  -0.0042 622  ASP B OD2 
13212 N N   . ALA B 625  ? 0.2839 0.3368 0.2735 0.0148  0.0375  -0.0040 623  ALA B N   
13213 C CA  . ALA B 625  ? 0.3363 0.3847 0.3234 0.0141  0.0340  -0.0051 623  ALA B CA  
13214 C C   . ALA B 625  ? 0.3152 0.3631 0.3072 0.0121  0.0319  -0.0031 623  ALA B C   
13215 O O   . ALA B 625  ? 0.3162 0.3612 0.3067 0.0114  0.0291  -0.0035 623  ALA B O   
13216 C CB  . ALA B 625  ? 0.4086 0.4543 0.3952 0.0157  0.0328  -0.0085 623  ALA B CB  
13217 N N   . ALA B 626  ? 0.2589 0.3097 0.2567 0.0112  0.0332  -0.0010 624  ALA B N   
13218 C CA  . ALA B 626  ? 0.2855 0.3353 0.2878 0.0098  0.0313  0.0005  624  ALA B CA  
13219 C C   . ALA B 626  ? 0.2586 0.3068 0.2578 0.0087  0.0293  0.0023  624  ALA B C   
13220 O O   . ALA B 626  ? 0.3056 0.3521 0.3062 0.0082  0.0268  0.0021  624  ALA B O   
13221 C CB  . ALA B 626  ? 0.2453 0.2979 0.2534 0.0089  0.0330  0.0026  624  ALA B CB  
13222 N N   . PRO B 627  ? 0.3086 0.3574 0.3037 0.0083  0.0302  0.0042  625  PRO B N   
13223 C CA  . PRO B 627  ? 0.2833 0.3307 0.2758 0.0074  0.0280  0.0060  625  PRO B CA  
13224 C C   . PRO B 627  ? 0.3014 0.3464 0.2900 0.0076  0.0254  0.0041  625  PRO B C   
13225 O O   . PRO B 627  ? 0.2944 0.3386 0.2838 0.0069  0.0229  0.0050  625  PRO B O   
13226 C CB  . PRO B 627  ? 0.3208 0.3694 0.3090 0.0071  0.0297  0.0082  625  PRO B CB  
13227 C CG  . PRO B 627  ? 0.3280 0.3792 0.3190 0.0073  0.0329  0.0086  625  PRO B CG  
13228 C CD  . PRO B 627  ? 0.3290 0.3804 0.3222 0.0085  0.0333  0.0053  625  PRO B CD  
13229 N N   . ASP B 628  ? 0.2966 0.3405 0.2809 0.0085  0.0258  0.0015  626  ASP B N   
13230 C CA  . ASP B 628  ? 0.3028 0.3440 0.2829 0.0083  0.0230  -0.0003 626  ASP B CA  
13231 C C   . ASP B 628  ? 0.3368 0.3771 0.3215 0.0078  0.0209  -0.0013 626  ASP B C   
13232 O O   . ASP B 628  ? 0.2919 0.3313 0.2757 0.0068  0.0182  -0.0010 626  ASP B O   
13233 C CB  . ASP B 628  ? 0.2922 0.3315 0.2666 0.0096  0.0238  -0.0031 626  ASP B CB  
13234 C CG  . ASP B 628  ? 0.4066 0.4466 0.3751 0.0101  0.0255  -0.0022 626  ASP B CG  
13235 O OD1 . ASP B 628  ? 0.3870 0.4276 0.3538 0.0090  0.0247  0.0003  626  ASP B OD1 
13236 O OD2 . ASP B 628  ? 0.5113 0.5513 0.4768 0.0118  0.0277  -0.0040 626  ASP B OD2 
13237 N N   . TRP B 629  ? 0.2729 0.3138 0.2624 0.0085  0.0222  -0.0024 627  TRP B N   
13238 C CA  . TRP B 629  ? 0.2513 0.2914 0.2450 0.0081  0.0203  -0.0032 627  TRP B CA  
13239 C C   . TRP B 629  ? 0.2400 0.2816 0.2380 0.0071  0.0193  -0.0008 627  TRP B C   
13240 O O   . TRP B 629  ? 0.2179 0.2591 0.2171 0.0064  0.0171  -0.0009 627  TRP B O   
13241 C CB  . TRP B 629  ? 0.2576 0.2980 0.2551 0.0091  0.0219  -0.0049 627  TRP B CB  
13242 C CG  . TRP B 629  ? 0.2113 0.2507 0.2125 0.0087  0.0201  -0.0058 627  TRP B CG  
13243 C CD1 . TRP B 629  ? 0.2033 0.2441 0.2106 0.0086  0.0205  -0.0053 627  TRP B CD1 
13244 C CD2 . TRP B 629  ? 0.2179 0.2549 0.2170 0.0080  0.0175  -0.0072 627  TRP B CD2 
13245 N NE1 . TRP B 629  ? 0.2139 0.2534 0.2227 0.0081  0.0185  -0.0063 627  TRP B NE1 
13246 C CE2 . TRP B 629  ? 0.1822 0.2195 0.1862 0.0076  0.0167  -0.0073 627  TRP B CE2 
13247 C CE3 . TRP B 629  ? 0.2254 0.2598 0.2186 0.0075  0.0157  -0.0083 627  TRP B CE3 
13248 C CZ2 . TRP B 629  ? 0.1700 0.2056 0.1735 0.0067  0.0143  -0.0083 627  TRP B CZ2 
13249 C CZ3 . TRP B 629  ? 0.2435 0.2760 0.2363 0.0063  0.0131  -0.0092 627  TRP B CZ3 
13250 C CH2 . TRP B 629  ? 0.2433 0.2766 0.2413 0.0059  0.0125  -0.0092 627  TRP B CH2 
13251 N N   . ALA B 630  ? 0.2331 0.2764 0.2333 0.0072  0.0210  0.0014  628  ALA B N   
13252 C CA  . ALA B 630  ? 0.2891 0.3331 0.2928 0.0066  0.0199  0.0036  628  ALA B CA  
13253 C C   . ALA B 630  ? 0.2939 0.3379 0.2946 0.0061  0.0176  0.0048  628  ALA B C   
13254 O O   . ALA B 630  ? 0.2699 0.3145 0.2733 0.0059  0.0160  0.0058  628  ALA B O   
13255 C CB  . ALA B 630  ? 0.3018 0.3468 0.3074 0.0066  0.0219  0.0058  628  ALA B CB  
13256 N N   . ALA B 631  ? 0.2896 0.3329 0.2844 0.0059  0.0174  0.0046  629  ALA B N   
13257 C CA  . ALA B 631  ? 0.3111 0.3546 0.3025 0.0052  0.0150  0.0058  629  ALA B CA  
13258 C C   . ALA B 631  ? 0.2871 0.3300 0.2778 0.0044  0.0124  0.0042  629  ALA B C   
13259 O O   . ALA B 631  ? 0.2480 0.2917 0.2370 0.0036  0.0101  0.0053  629  ALA B O   
13260 C CB  . ALA B 631  ? 0.2985 0.3413 0.2833 0.0051  0.0157  0.0061  629  ALA B CB  
13261 N N   . VAL B 632  ? 0.2309 0.2726 0.2228 0.0045  0.0126  0.0018  630  VAL B N   
13262 C CA  . VAL B 632  ? 0.2409 0.2820 0.2326 0.0034  0.0100  0.0006  630  VAL B CA  
13263 C C   . VAL B 632  ? 0.2630 0.3067 0.2602 0.0032  0.0090  0.0021  630  VAL B C   
13264 O O   . VAL B 632  ? 0.2596 0.3040 0.2616 0.0041  0.0104  0.0024  630  VAL B O   
13265 C CB  . VAL B 632  ? 0.2419 0.2805 0.2334 0.0037  0.0105  -0.0022 630  VAL B CB  
13266 C CG1 . VAL B 632  ? 0.2231 0.2610 0.2146 0.0022  0.0077  -0.0031 630  VAL B CG1 
13267 C CG2 . VAL B 632  ? 0.2667 0.3028 0.2526 0.0045  0.0117  -0.0039 630  VAL B CG2 
13268 N N   . PRO B 633  ? 0.2290 0.2744 0.2258 0.0021  0.0064  0.0031  631  PRO B N   
13269 C CA  . PRO B 633  ? 0.2365 0.2850 0.2385 0.0023  0.0056  0.0047  631  PRO B CA  
13270 C C   . PRO B 633  ? 0.2464 0.2947 0.2526 0.0026  0.0062  0.0032  631  PRO B C   
13271 O O   . PRO B 633  ? 0.2178 0.2641 0.2225 0.0018  0.0059  0.0012  631  PRO B O   
13272 C CB  . PRO B 633  ? 0.2485 0.2991 0.2488 0.0008  0.0026  0.0055  631  PRO B CB  
13273 C CG  . PRO B 633  ? 0.2878 0.3363 0.2817 0.0002  0.0021  0.0054  631  PRO B CG  
13274 C CD  . PRO B 633  ? 0.2432 0.2880 0.2346 0.0008  0.0042  0.0031  631  PRO B CD  
13275 N N   . PRO B 634  ? 0.2613 0.3113 0.2724 0.0037  0.0070  0.0042  632  PRO B N   
13276 C CA  . PRO B 634  ? 0.2711 0.3208 0.2859 0.0040  0.0076  0.0029  632  PRO B CA  
13277 C C   . PRO B 634  ? 0.2057 0.2561 0.2202 0.0024  0.0057  0.0019  632  PRO B C   
13278 O O   . PRO B 634  ? 0.2226 0.2710 0.2373 0.0021  0.0061  0.0001  632  PRO B O   
13279 C CB  . PRO B 634  ? 0.2537 0.3055 0.2729 0.0054  0.0080  0.0044  632  PRO B CB  
13280 C CG  . PRO B 634  ? 0.3296 0.3812 0.3473 0.0061  0.0085  0.0063  632  PRO B CG  
13281 C CD  . PRO B 634  ? 0.2531 0.3047 0.2660 0.0049  0.0073  0.0065  632  PRO B CD  
13282 N N   . SER B 635  ? 0.2231 0.2764 0.2370 0.0014  0.0037  0.0031  633  SER B N   
13283 C CA  . SER B 635  ? 0.2326 0.2867 0.2463 -0.0005 0.0018  0.0025  633  SER B CA  
13284 C C   . SER B 635  ? 0.2148 0.2647 0.2235 -0.0020 0.0011  0.0006  633  SER B C   
13285 O O   . SER B 635  ? 0.2278 0.2764 0.2364 -0.0033 0.0002  -0.0006 633  SER B O   
13286 C CB  . SER B 635  ? 0.2872 0.3459 0.3015 -0.0015 -0.0003 0.0045  633  SER B CB  
13287 O OG  . SER B 635  ? 0.3659 0.4240 0.3760 -0.0023 -0.0015 0.0052  633  SER B OG  
13288 N N   . GLU B 636  ? 0.2348 0.2824 0.2393 -0.0017 0.0014  0.0004  634  GLU B N   
13289 C CA  . GLU B 636  ? 0.2385 0.2815 0.2378 -0.0026 0.0009  -0.0017 634  GLU B CA  
13290 C C   . GLU B 636  ? 0.2180 0.2580 0.2182 -0.0012 0.0030  -0.0037 634  GLU B C   
13291 O O   . GLU B 636  ? 0.2246 0.2613 0.2225 -0.0017 0.0023  -0.0056 634  GLU B O   
13292 C CB  . GLU B 636  ? 0.2220 0.2636 0.2160 -0.0026 0.0007  -0.0015 634  GLU B CB  
13293 N N   . ARG B 637  ? 0.1863 0.2276 0.1900 0.0007  0.0054  -0.0032 635  ARG B N   
13294 C CA  . ARG B 637  ? 0.1853 0.2245 0.1907 0.0019  0.0071  -0.0049 635  ARG B CA  
13295 C C   . ARG B 637  ? 0.2202 0.2596 0.2286 0.0012  0.0062  -0.0055 635  ARG B C   
13296 O O   . ARG B 637  ? 0.1982 0.2347 0.2057 0.0013  0.0061  -0.0073 635  ARG B O   
13297 C CB  . ARG B 637  ? 0.1784 0.2190 0.1871 0.0035  0.0096  -0.0040 635  ARG B CB  
13298 C CG  . ARG B 637  ? 0.1633 0.2041 0.1690 0.0041  0.0107  -0.0031 635  ARG B CG  
13299 C CD  . ARG B 637  ? 0.1949 0.2366 0.2038 0.0053  0.0132  -0.0022 635  ARG B CD  
13300 N NE  . ARG B 637  ? 0.1987 0.2422 0.2123 0.0056  0.0131  -0.0007 635  ARG B NE  
13301 C CZ  . ARG B 637  ? 0.2685 0.3133 0.2832 0.0059  0.0135  0.0014  635  ARG B CZ  
13302 N NH1 . ARG B 637  ? 0.3186 0.3635 0.3298 0.0058  0.0138  0.0027  635  ARG B NH1 
13303 N NH2 . ARG B 637  ? 0.2277 0.2733 0.2465 0.0065  0.0135  0.0024  635  ARG B NH2 
13304 N N   . ALA B 638  ? 0.1779 0.2207 0.1898 0.0007  0.0055  -0.0040 636  ALA B N   
13305 C CA  . ALA B 638  ? 0.1930 0.2364 0.2074 0.0000  0.0046  -0.0043 636  ALA B CA  
13306 C C   . ALA B 638  ? 0.1781 0.2193 0.1889 -0.0022 0.0024  -0.0052 636  ALA B C   
13307 O O   . ALA B 638  ? 0.1760 0.2153 0.1871 -0.0027 0.0020  -0.0063 636  ALA B O   
13308 C CB  . ALA B 638  ? 0.1771 0.2251 0.1952 0.0000  0.0042  -0.0024 636  ALA B CB  
13309 N N   . ALA B 639  ? 0.2247 0.2656 0.2316 -0.0036 0.0007  -0.0047 637  ALA B N   
13310 C CA  . ALA B 639  ? 0.2312 0.2691 0.2340 -0.0059 -0.0017 -0.0056 637  ALA B CA  
13311 C C   . ALA B 639  ? 0.2065 0.2387 0.2060 -0.0051 -0.0013 -0.0081 637  ALA B C   
13312 O O   . ALA B 639  ? 0.2074 0.2364 0.2049 -0.0065 -0.0029 -0.0090 637  ALA B O   
13313 C CB  . ALA B 639  ? 0.2183 0.2567 0.2172 -0.0075 -0.0036 -0.0047 637  ALA B CB  
13314 N N   . CYS B 640  ? 0.1945 0.2253 0.1933 -0.0028 0.0009  -0.0090 638  CYS B N   
13315 C CA  . CYS B 640  ? 0.2315 0.2575 0.2277 -0.0015 0.0016  -0.0114 638  CYS B CA  
13316 C C   . CYS B 640  ? 0.1869 0.2126 0.1868 -0.0011 0.0020  -0.0120 638  CYS B C   
13317 O O   . CYS B 640  ? 0.1868 0.2084 0.1844 -0.0014 0.0007  -0.0135 638  CYS B O   
13318 C CB  . CYS B 640  ? 0.2048 0.2310 0.2007 0.0010  0.0042  -0.0119 638  CYS B CB  
13319 S SG  . CYS B 640  ? 0.2398 0.2653 0.2299 0.0009  0.0040  -0.0116 638  CYS B SG  
13320 N N   . LEU B 641  ? 0.1967 0.2263 0.2021 -0.0003 0.0035  -0.0109 639  LEU B N   
13321 C CA  . LEU B 641  ? 0.1798 0.2094 0.1888 0.0000  0.0037  -0.0113 639  LEU B CA  
13322 C C   . LEU B 641  ? 0.1848 0.2135 0.1926 -0.0024 0.0013  -0.0111 639  LEU B C   
13323 O O   . LEU B 641  ? 0.1743 0.1998 0.1815 -0.0025 0.0005  -0.0122 639  LEU B O   
13324 C CB  . LEU B 641  ? 0.1605 0.1943 0.1749 0.0010  0.0053  -0.0100 639  LEU B CB  
13325 C CG  . LEU B 641  ? 0.1725 0.2066 0.1892 0.0031  0.0077  -0.0104 639  LEU B CG  
13326 C CD1 . LEU B 641  ? 0.2079 0.2418 0.2220 0.0039  0.0088  -0.0104 639  LEU B CD1 
13327 C CD2 . LEU B 641  ? 0.1775 0.2148 0.1991 0.0037  0.0087  -0.0092 639  LEU B CD2 
13328 N N   . ASP B 642  ? 0.1989 0.2305 0.2067 -0.0043 -0.0001 -0.0094 640  ASP B N   
13329 C CA  . ASP B 642  ? 0.1901 0.2216 0.1970 -0.0069 -0.0024 -0.0088 640  ASP B CA  
13330 C C   . ASP B 642  ? 0.1727 0.1981 0.1740 -0.0083 -0.0045 -0.0102 640  ASP B C   
13331 O O   . ASP B 642  ? 0.1875 0.2105 0.1881 -0.0098 -0.0059 -0.0105 640  ASP B O   
13332 C CB  . ASP B 642  ? 0.1769 0.2134 0.1849 -0.0087 -0.0035 -0.0066 640  ASP B CB  
13333 C CG  . ASP B 642  ? 0.2232 0.2654 0.2368 -0.0077 -0.0020 -0.0051 640  ASP B CG  
13334 O OD1 . ASP B 642  ? 0.2203 0.2621 0.2365 -0.0063 -0.0007 -0.0058 640  ASP B OD1 
13335 O OD2 . ASP B 642  ? 0.2366 0.2835 0.2518 -0.0081 -0.0023 -0.0033 640  ASP B OD2 
13336 N N   . ARG B 643  ? 0.2110 0.2335 0.2079 -0.0079 -0.0048 -0.0112 641  ARG B N   
13337 C CA  . ARG B 643  ? 0.2324 0.2481 0.2233 -0.0088 -0.0068 -0.0129 641  ARG B CA  
13338 C C   . ARG B 643  ? 0.2005 0.2121 0.1913 -0.0066 -0.0058 -0.0149 641  ARG B C   
13339 O O   . ARG B 643  ? 0.2062 0.2128 0.1940 -0.0077 -0.0078 -0.0158 641  ARG B O   
13340 C CB  . ARG B 643  ? 0.2152 0.2287 0.2012 -0.0083 -0.0070 -0.0137 641  ARG B CB  
13341 C CG  . ARG B 643  ? 0.3067 0.3227 0.2911 -0.0112 -0.0092 -0.0119 641  ARG B CG  
13342 C CD  . ARG B 643  ? 0.3135 0.3258 0.2915 -0.0111 -0.0100 -0.0129 641  ARG B CD  
13343 N NE  . ARG B 643  ? 0.3182 0.3325 0.2970 -0.0081 -0.0071 -0.0132 641  ARG B NE  
13344 C CZ  . ARG B 643  ? 0.3194 0.3388 0.3004 -0.0080 -0.0063 -0.0114 641  ARG B CZ  
13345 N NH1 . ARG B 643  ? 0.2587 0.2822 0.2415 -0.0105 -0.0081 -0.0092 641  ARG B NH1 
13346 N NH2 . ARG B 643  ? 0.2906 0.3111 0.2718 -0.0055 -0.0038 -0.0116 641  ARG B NH2 
13347 N N   . ALA B 644  ? 0.1844 0.1979 0.1785 -0.0037 -0.0030 -0.0154 642  ALA B N   
13348 C CA  . ALA B 644  ? 0.1757 0.1863 0.1705 -0.0015 -0.0021 -0.0172 642  ALA B CA  
13349 C C   . ALA B 644  ? 0.2191 0.2297 0.2165 -0.0027 -0.0032 -0.0166 642  ALA B C   
13350 O O   . ALA B 644  ? 0.2090 0.2150 0.2045 -0.0024 -0.0042 -0.0179 642  ALA B O   
13351 C CB  . ALA B 644  ? 0.1877 0.2016 0.1864 0.0014  0.0010  -0.0174 642  ALA B CB  
13352 N N   . ALA B 645  ? 0.1931 0.2089 0.1946 -0.0042 -0.0029 -0.0146 643  ALA B N   
13353 C CA  . ALA B 645  ? 0.2040 0.2203 0.2076 -0.0054 -0.0038 -0.0140 643  ALA B CA  
13354 C C   . ALA B 645  ? 0.2114 0.2232 0.2105 -0.0083 -0.0068 -0.0139 643  ALA B C   
13355 O O   . ALA B 645  ? 0.2065 0.2151 0.2049 -0.0086 -0.0078 -0.0144 643  ALA B O   
13356 C CB  . ALA B 645  ? 0.2030 0.2259 0.2113 -0.0062 -0.0030 -0.0119 643  ALA B CB  
13357 N N   . GLU B 646  ? 0.2122 0.2237 0.2080 -0.0104 -0.0084 -0.0132 644  GLU B N   
13358 C CA  . GLU B 646  ? 0.2827 0.2895 0.2738 -0.0136 -0.0116 -0.0131 644  GLU B CA  
13359 C C   . GLU B 646  ? 0.2500 0.2485 0.2362 -0.0122 -0.0127 -0.0154 644  GLU B C   
13360 O O   . GLU B 646  ? 0.2324 0.2263 0.2160 -0.0140 -0.0148 -0.0155 644  GLU B O   
13361 C CB  . GLU B 646  ? 0.2325 0.2401 0.2206 -0.0160 -0.0133 -0.0121 644  GLU B CB  
13362 C CG  . GLU B 646  ? 0.2716 0.2873 0.2641 -0.0177 -0.0129 -0.0096 644  GLU B CG  
13363 C CD  . GLU B 646  ? 0.3978 0.4162 0.3928 -0.0203 -0.0139 -0.0079 644  GLU B CD  
13364 O OE1 . GLU B 646  ? 0.4725 0.4862 0.4638 -0.0230 -0.0165 -0.0078 644  GLU B OE1 
13365 O OE2 . GLU B 646  ? 0.4166 0.4415 0.4168 -0.0195 -0.0121 -0.0065 644  GLU B OE2 
13366 N N   . LEU B 647  ? 0.2405 0.2370 0.2252 -0.0091 -0.0112 -0.0173 645  LEU B N   
13367 C CA  . LEU B 647  ? 0.2303 0.2193 0.2104 -0.0071 -0.0119 -0.0198 645  LEU B CA  
13368 C C   . LEU B 647  ? 0.2612 0.2493 0.2442 -0.0054 -0.0113 -0.0203 645  LEU B C   
13369 O O   . LEU B 647  ? 0.2531 0.2346 0.2324 -0.0054 -0.0132 -0.0214 645  LEU B O   
13370 C CB  . LEU B 647  ? 0.2331 0.2214 0.2113 -0.0039 -0.0100 -0.0215 645  LEU B CB  
13371 C CG  . LEU B 647  ? 0.2731 0.2609 0.2471 -0.0054 -0.0110 -0.0214 645  LEU B CG  
13372 C CD1 . LEU B 647  ? 0.2644 0.2522 0.2369 -0.0018 -0.0086 -0.0230 645  LEU B CD1 
13373 C CD2 . LEU B 647  ? 0.3128 0.2933 0.2799 -0.0080 -0.0147 -0.0220 645  LEU B CD2 
13374 N N   . MET B 648  ? 0.2067 0.2008 0.1959 -0.0038 -0.0087 -0.0197 646  MET B N   
13375 C CA  . MET B 648  ? 0.2112 0.2048 0.2032 -0.0024 -0.0083 -0.0201 646  MET B CA  
13376 C C   . MET B 648  ? 0.2301 0.2221 0.2214 -0.0054 -0.0106 -0.0187 646  MET B C   
13377 O O   . MET B 648  ? 0.2100 0.1976 0.2001 -0.0049 -0.0117 -0.0194 646  MET B O   
13378 C CB  . MET B 648  ? 0.2083 0.2085 0.2068 -0.0006 -0.0054 -0.0194 646  MET B CB  
13379 C CG  . MET B 648  ? 0.2280 0.2297 0.2276 0.0025  -0.0030 -0.0207 646  MET B CG  
13380 S SD  . MET B 648  ? 0.2463 0.2538 0.2532 0.0045  -0.0003 -0.0202 646  MET B SD  
13381 C CE  . MET B 648  ? 0.2554 0.2645 0.2625 0.0073  0.0022  -0.0213 646  MET B CE  
13382 N N   . GLN B 649  ? 0.2225 0.2184 0.2148 -0.0086 -0.0112 -0.0166 647  GLN B N   
13383 C CA  . GLN B 649  ? 0.2379 0.2333 0.2297 -0.0119 -0.0132 -0.0151 647  GLN B CA  
13384 C C   . GLN B 649  ? 0.2339 0.2209 0.2192 -0.0136 -0.0164 -0.0158 647  GLN B C   
13385 O O   . GLN B 649  ? 0.2806 0.2638 0.2645 -0.0145 -0.0180 -0.0156 647  GLN B O   
13386 C CB  . GLN B 649  ? 0.2216 0.2233 0.2155 -0.0149 -0.0133 -0.0127 647  GLN B CB  
13387 C CG  . GLN B 649  ? 0.2305 0.2331 0.2246 -0.0182 -0.0149 -0.0108 647  GLN B CG  
13388 C CD  . GLN B 649  ? 0.2484 0.2541 0.2466 -0.0167 -0.0132 -0.0105 647  GLN B CD  
13389 O OE1 . GLN B 649  ? 0.2385 0.2510 0.2414 -0.0159 -0.0112 -0.0096 647  GLN B OE1 
13390 N NE2 . GLN B 649  ? 0.2123 0.2127 0.2087 -0.0161 -0.0143 -0.0113 647  GLN B NE2 
13391 N N   . ALA B 650  ? 0.2365 0.2202 0.2173 -0.0142 -0.0176 -0.0165 648  ALA B N   
13392 C CA  . ALA B 650  ? 0.2388 0.2137 0.2127 -0.0161 -0.0209 -0.0173 648  ALA B CA  
13393 C C   . ALA B 650  ? 0.3031 0.2709 0.2744 -0.0126 -0.0212 -0.0197 648  ALA B C   
13394 O O   . ALA B 650  ? 0.2909 0.2513 0.2576 -0.0139 -0.0240 -0.0199 648  ALA B O   
13395 C CB  . ALA B 650  ? 0.2777 0.2506 0.2473 -0.0171 -0.0220 -0.0178 648  ALA B CB  
13396 N N   . ARG B 651  ? 0.2589 0.2288 0.2329 -0.0083 -0.0184 -0.0213 649  ARG B N   
13397 C CA  . ARG B 651  ? 0.2446 0.2087 0.2165 -0.0045 -0.0184 -0.0237 649  ARG B CA  
13398 C C   . ARG B 651  ? 0.2327 0.1991 0.2093 -0.0027 -0.0173 -0.0234 649  ARG B C   
13399 O O   . ARG B 651  ? 0.2668 0.2302 0.2431 0.0009  -0.0169 -0.0253 649  ARG B O   
13400 C CB  . ARG B 651  ? 0.2992 0.2642 0.2706 -0.0008 -0.0162 -0.0257 649  ARG B CB  
13401 C CG  . ARG B 651  ? 0.3010 0.2627 0.2666 -0.0025 -0.0176 -0.0261 649  ARG B CG  
13402 C CD  . ARG B 651  ? 0.3348 0.2980 0.2996 0.0007  -0.0153 -0.0278 649  ARG B CD  
13403 N NE  . ARG B 651  ? 0.3335 0.2944 0.2930 -0.0015 -0.0169 -0.0278 649  ARG B NE  
13404 C CZ  . ARG B 651  ? 0.3849 0.3475 0.3429 0.0002  -0.0152 -0.0287 649  ARG B CZ  
13405 N NH1 . ARG B 651  ? 0.3052 0.2720 0.2666 0.0040  -0.0118 -0.0296 649  ARG B NH1 
13406 N NH2 . ARG B 651  ? 0.3487 0.3088 0.3016 -0.0023 -0.0172 -0.0286 649  ARG B NH2 
13407 N N   . MET B 652  ? 0.2719 0.2437 0.2527 -0.0052 -0.0169 -0.0212 650  MET B N   
13408 C CA  . MET B 652  ? 0.2332 0.2074 0.2184 -0.0037 -0.0160 -0.0210 650  MET B CA  
13409 C C   . MET B 652  ? 0.2623 0.2291 0.2442 -0.0022 -0.0180 -0.0221 650  MET B C   
13410 O O   . MET B 652  ? 0.2761 0.2438 0.2610 0.0012  -0.0167 -0.0232 650  MET B O   
13411 C CB  . MET B 652  ? 0.2258 0.2054 0.2142 -0.0070 -0.0159 -0.0184 650  MET B CB  
13412 C CG  . MET B 652  ? 0.2161 0.1979 0.2084 -0.0058 -0.0151 -0.0181 650  MET B CG  
13413 S SD  . MET B 652  ? 0.2866 0.2748 0.2820 -0.0094 -0.0149 -0.0153 650  MET B SD  
13414 C CE  . MET B 652  ? 0.2494 0.2462 0.2504 -0.0079 -0.0115 -0.0151 650  MET B CE  
13415 N N   . PRO B 653  ? 0.2583 0.2177 0.2344 -0.0046 -0.0212 -0.0219 651  PRO B N   
13416 C CA  . PRO B 653  ? 0.2813 0.2331 0.2542 -0.0027 -0.0232 -0.0230 651  PRO B CA  
13417 C C   . PRO B 653  ? 0.2725 0.2218 0.2449 0.0025  -0.0222 -0.0258 651  PRO B C   
13418 O O   . PRO B 653  ? 0.3243 0.2728 0.2986 0.0054  -0.0220 -0.0265 651  PRO B O   
13419 C CB  . PRO B 653  ? 0.2616 0.2053 0.2274 -0.0064 -0.0270 -0.0223 651  PRO B CB  
13420 C CG  . PRO B 653  ? 0.2807 0.2302 0.2483 -0.0111 -0.0268 -0.0198 651  PRO B CG  
13421 C CD  . PRO B 653  ? 0.2634 0.2207 0.2356 -0.0092 -0.0235 -0.0203 651  PRO B CD  
13422 N N   . THR B 654  ? 0.2806 0.2289 0.2506 0.0038  -0.0214 -0.0273 652  THR B N   
13423 C CA  . THR B 654  ? 0.2899 0.2367 0.2594 0.0090  -0.0200 -0.0299 652  THR B CA  
13424 C C   . THR B 654  ? 0.3141 0.2697 0.2912 0.0117  -0.0164 -0.0299 652  THR B C   
13425 O O   . THR B 654  ? 0.3029 0.2584 0.2819 0.0157  -0.0156 -0.0314 652  THR B O   
13426 C CB  . THR B 654  ? 0.2989 0.2428 0.2635 0.0095  -0.0199 -0.0314 652  THR B CB  
13427 O OG1 . THR B 654  ? 0.3031 0.2380 0.2603 0.0067  -0.0236 -0.0314 652  THR B OG1 
13428 C CG2 . THR B 654  ? 0.2789 0.2215 0.2428 0.0152  -0.0183 -0.0342 652  THR B CG2 
13429 N N   . LEU B 655  ? 0.2553 0.2187 0.2370 0.0097  -0.0144 -0.0283 653  LEU B N   
13430 C CA  . LEU B 655  ? 0.2953 0.2666 0.2840 0.0118  -0.0113 -0.0282 653  LEU B CA  
13431 C C   . LEU B 655  ? 0.2448 0.2168 0.2370 0.0125  -0.0118 -0.0277 653  LEU B C   
13432 O O   . LEU B 655  ? 0.2713 0.2464 0.2675 0.0157  -0.0102 -0.0286 653  LEU B O   
13433 C CB  . LEU B 655  ? 0.2587 0.2371 0.2511 0.0092  -0.0095 -0.0264 653  LEU B CB  
13434 C CG  . LEU B 655  ? 0.3279 0.3064 0.3173 0.0082  -0.0091 -0.0265 653  LEU B CG  
13435 C CD1 . LEU B 655  ? 0.2867 0.2725 0.2802 0.0060  -0.0074 -0.0245 653  LEU B CD1 
13436 C CD2 . LEU B 655  ? 0.2843 0.2623 0.2726 0.0120  -0.0073 -0.0286 653  LEU B CD2 
13437 N N   . LEU B 656  ? 0.2583 0.2278 0.2490 0.0094  -0.0141 -0.0262 654  LEU B N   
13438 C CA  . LEU B 656  ? 0.2763 0.2456 0.2693 0.0100  -0.0149 -0.0258 654  LEU B CA  
13439 C C   . LEU B 656  ? 0.2857 0.2504 0.2774 0.0141  -0.0158 -0.0277 654  LEU B C   
13440 O O   . LEU B 656  ? 0.2977 0.2656 0.2938 0.0165  -0.0148 -0.0281 654  LEU B O   
13441 C CB  . LEU B 656  ? 0.2827 0.2481 0.2723 0.0061  -0.0176 -0.0240 654  LEU B CB  
13442 C CG  . LEU B 656  ? 0.3118 0.2818 0.3026 0.0020  -0.0172 -0.0219 654  LEU B CG  
13443 C CD1 . LEU B 656  ? 0.3145 0.2811 0.3023 -0.0016 -0.0197 -0.0200 654  LEU B CD1 
13444 C CD2 . LEU B 656  ? 0.2856 0.2640 0.2829 0.0028  -0.0143 -0.0214 654  LEU B CD2 
13445 N N   . GLY B 657  ? 0.2597 0.2167 0.2452 0.0149  -0.0177 -0.0290 655  GLY B N   
13446 C CA  . GLY B 657  ? 0.3043 0.2563 0.2880 0.0191  -0.0188 -0.0309 655  GLY B CA  
13447 C C   . GLY B 657  ? 0.3067 0.2645 0.2952 0.0235  -0.0158 -0.0324 655  GLY B C   
13448 O O   . GLY B 657  ? 0.3181 0.2765 0.3092 0.0267  -0.0158 -0.0331 655  GLY B O   
13449 N N   . LEU B 658  ? 0.2668 0.2291 0.2565 0.0235  -0.0133 -0.0327 656  LEU B N   
13450 C CA  . LEU B 658  ? 0.2552 0.2239 0.2498 0.0272  -0.0102 -0.0338 656  LEU B CA  
13451 C C   . LEU B 658  ? 0.2767 0.2532 0.2789 0.0267  -0.0087 -0.0324 656  LEU B C   
13452 O O   . LEU B 658  ? 0.2654 0.2454 0.2718 0.0299  -0.0076 -0.0331 656  LEU B O   
13453 C CB  . LEU B 658  ? 0.2822 0.2535 0.2756 0.0269  -0.0080 -0.0341 656  LEU B CB  
13454 C CG  . LEU B 658  ? 0.2710 0.2488 0.2687 0.0305  -0.0047 -0.0351 656  LEU B CG  
13455 C CD1 . LEU B 658  ? 0.2965 0.2709 0.2925 0.0354  -0.0050 -0.0373 656  LEU B CD1 
13456 C CD2 . LEU B 658  ? 0.2623 0.2421 0.2581 0.0298  -0.0027 -0.0353 656  LEU B CD2 
13457 N N   . ILE B 659  ? 0.2501 0.2294 0.2541 0.0228  -0.0086 -0.0305 657  ILE B N   
13458 C CA  . ILE B 659  ? 0.2184 0.2044 0.2290 0.0222  -0.0073 -0.0293 657  ILE B CA  
13459 C C   . ILE B 659  ? 0.2555 0.2395 0.2672 0.0235  -0.0092 -0.0294 657  ILE B C   
13460 O O   . ILE B 659  ? 0.2293 0.2180 0.2463 0.0253  -0.0083 -0.0295 657  ILE B O   
13461 C CB  . ILE B 659  ? 0.2391 0.2279 0.2507 0.0181  -0.0070 -0.0274 657  ILE B CB  
13462 C CG1 . ILE B 659  ? 0.2005 0.1926 0.2123 0.0174  -0.0048 -0.0272 657  ILE B CG1 
13463 C CG2 . ILE B 659  ? 0.2618 0.2557 0.2789 0.0175  -0.0064 -0.0263 657  ILE B CG2 
13464 C CD1 . ILE B 659  ? 0.2403 0.2339 0.2516 0.0135  -0.0050 -0.0254 657  ILE B CD1 
13465 N N   . ILE B 660  ? 0.2363 0.2133 0.2429 0.0223  -0.0121 -0.0292 658  ILE B N   
13466 C CA  . ILE B 660  ? 0.2373 0.2116 0.2442 0.0234  -0.0143 -0.0291 658  ILE B CA  
13467 C C   . ILE B 660  ? 0.2308 0.2056 0.2397 0.0283  -0.0139 -0.0309 658  ILE B C   
13468 O O   . ILE B 660  ? 0.2276 0.2057 0.2410 0.0299  -0.0140 -0.0308 658  ILE B O   
13469 C CB  . ILE B 660  ? 0.2541 0.2199 0.2544 0.0214  -0.0176 -0.0286 658  ILE B CB  
13470 C CG1 . ILE B 660  ? 0.2642 0.2314 0.2640 0.0165  -0.0179 -0.0264 658  ILE B CG1 
13471 C CG2 . ILE B 660  ? 0.2694 0.2306 0.2686 0.0236  -0.0201 -0.0289 658  ILE B CG2 
13472 C CD1 . ILE B 660  ? 0.2856 0.2451 0.2786 0.0136  -0.0208 -0.0255 658  ILE B CD1 
13473 N N   . ARG B 661  ? 0.2428 0.2145 0.2484 0.0309  -0.0135 -0.0325 659  ARG B N   
13474 C CA  . ARG B 661  ? 0.2562 0.2276 0.2630 0.0359  -0.0134 -0.0343 659  ARG B CA  
13475 C C   . ARG B 661  ? 0.2671 0.2475 0.2803 0.0382  -0.0100 -0.0348 659  ARG B C   
13476 O O   . ARG B 661  ? 0.2608 0.2444 0.2780 0.0416  -0.0097 -0.0354 659  ARG B O   
13477 C CB  . ARG B 661  ? 0.2824 0.2456 0.2821 0.0382  -0.0148 -0.0361 659  ARG B CB  
13478 C CG  . ARG B 661  ? 0.3053 0.2590 0.2989 0.0370  -0.0187 -0.0358 659  ARG B CG  
13479 C CD  . ARG B 661  ? 0.3843 0.3288 0.3702 0.0388  -0.0203 -0.0376 659  ARG B CD  
13480 N NE  . ARG B 661  ? 0.3273 0.2718 0.3135 0.0448  -0.0193 -0.0399 659  ARG B NE  
13481 C CZ  . ARG B 661  ? 0.3691 0.3134 0.3529 0.0472  -0.0176 -0.0418 659  ARG B CZ  
13482 N NH1 . ARG B 661  ? 0.3753 0.3194 0.3562 0.0442  -0.0166 -0.0415 659  ARG B NH1 
13483 N NH2 . ARG B 661  ? 0.3462 0.2904 0.3301 0.0531  -0.0168 -0.0439 659  ARG B NH2 
13484 N N   . GLU B 662  ? 0.2421 0.2269 0.2565 0.0365  -0.0074 -0.0343 660  GLU B N   
13485 C CA  . GLU B 662  ? 0.2442 0.2374 0.2645 0.0384  -0.0042 -0.0345 660  GLU B CA  
13486 C C   . GLU B 662  ? 0.2098 0.2098 0.2370 0.0365  -0.0035 -0.0329 660  GLU B C   
13487 O O   . GLU B 662  ? 0.2319 0.2382 0.2648 0.0386  -0.0020 -0.0330 660  GLU B O   
13488 C CB  . GLU B 662  ? 0.2752 0.2702 0.2938 0.0374  -0.0018 -0.0346 660  GLU B CB  
13489 C CG  . GLU B 662  ? 0.2310 0.2350 0.2558 0.0385  0.0016  -0.0343 660  GLU B CG  
13490 C CD  . GLU B 662  ? 0.2400 0.2456 0.2627 0.0375  0.0039  -0.0342 660  GLU B CD  
13491 O OE1 . GLU B 662  ? 0.2357 0.2389 0.2555 0.0341  0.0033  -0.0333 660  GLU B OE1 
13492 O OE2 . GLU B 662  ? 0.2391 0.2487 0.2632 0.0403  0.0063  -0.0350 660  GLU B OE2 
13493 N N   . ALA B 663  ? 0.2202 0.2193 0.2470 0.0325  -0.0045 -0.0314 661  ALA B N   
13494 C CA  . ALA B 663  ? 0.2169 0.2217 0.2492 0.0304  -0.0038 -0.0300 661  ALA B CA  
13495 C C   . ALA B 663  ? 0.2211 0.2241 0.2543 0.0300  -0.0063 -0.0295 661  ALA B C   
13496 O O   . ALA B 663  ? 0.2387 0.2459 0.2762 0.0285  -0.0061 -0.0285 661  ALA B O   
13497 C CB  . ALA B 663  ? 0.2262 0.2320 0.2577 0.0267  -0.0028 -0.0287 661  ALA B CB  
13498 N N   . GLY B 664  ? 0.2379 0.2343 0.2665 0.0310  -0.0089 -0.0301 662  GLY B N   
13499 C CA  . GLY B 664  ? 0.2484 0.2425 0.2771 0.0306  -0.0115 -0.0295 662  GLY B CA  
13500 C C   . GLY B 664  ? 0.2467 0.2396 0.2738 0.0265  -0.0124 -0.0279 662  GLY B C   
13501 O O   . GLY B 664  ? 0.2805 0.2743 0.3094 0.0257  -0.0137 -0.0272 662  GLY B O   
13502 N N   . LYS B 665  ? 0.2295 0.2206 0.2532 0.0238  -0.0118 -0.0274 663  LYS B N   
13503 C CA  . LYS B 665  ? 0.2432 0.2342 0.2657 0.0200  -0.0123 -0.0258 663  LYS B CA  
13504 C C   . LYS B 665  ? 0.2641 0.2481 0.2807 0.0185  -0.0152 -0.0253 663  LYS B C   
13505 O O   . LYS B 665  ? 0.2686 0.2469 0.2810 0.0198  -0.0165 -0.0261 663  LYS B O   
13506 C CB  . LYS B 665  ? 0.2439 0.2377 0.2663 0.0179  -0.0102 -0.0253 663  LYS B CB  
13507 C CG  . LYS B 665  ? 0.2811 0.2815 0.3089 0.0188  -0.0075 -0.0255 663  LYS B CG  
13508 C CD  . LYS B 665  ? 0.3141 0.3178 0.3428 0.0161  -0.0060 -0.0243 663  LYS B CD  
13509 C CE  . LYS B 665  ? 0.3101 0.3199 0.3445 0.0167  -0.0038 -0.0243 663  LYS B CE  
13510 N NZ  . LYS B 665  ? 0.3038 0.3164 0.3390 0.0144  -0.0024 -0.0231 663  LYS B NZ  
13511 N N   . SER B 666  ? 0.2431 0.2273 0.2593 0.0158  -0.0161 -0.0238 664  SER B N   
13512 C CA  . SER B 666  ? 0.2729 0.2514 0.2835 0.0134  -0.0185 -0.0227 664  SER B CA  
13513 C C   . SER B 666  ? 0.2830 0.2607 0.2906 0.0107  -0.0178 -0.0221 664  SER B C   
13514 O O   . SER B 666  ? 0.2716 0.2539 0.2817 0.0104  -0.0155 -0.0222 664  SER B O   
13515 C CB  . SER B 666  ? 0.3230 0.3031 0.3343 0.0112  -0.0192 -0.0213 664  SER B CB  
13516 O OG  . SER B 666  ? 0.3079 0.2935 0.3215 0.0091  -0.0170 -0.0205 664  SER B OG  
13517 N N   . ALA B 667  ? 0.2638 0.2354 0.2658 0.0085  -0.0201 -0.0212 665  ALA B N   
13518 C CA  . ALA B 667  ? 0.2548 0.2255 0.2537 0.0056  -0.0200 -0.0204 665  ALA B CA  
13519 C C   . ALA B 667  ? 0.2395 0.2169 0.2413 0.0030  -0.0180 -0.0190 665  ALA B C   
13520 O O   . ALA B 667  ? 0.2407 0.2211 0.2433 0.0022  -0.0164 -0.0190 665  ALA B O   
13521 C CB  . ALA B 667  ? 0.2893 0.2524 0.2819 0.0031  -0.0231 -0.0194 665  ALA B CB  
13522 N N   . LEU B 668  ? 0.2564 0.2363 0.2596 0.0018  -0.0181 -0.0179 666  LEU B N   
13523 C CA  . LEU B 668  ? 0.2894 0.2755 0.2950 -0.0003 -0.0163 -0.0166 666  LEU B CA  
13524 C C   . LEU B 668  ? 0.2388 0.2306 0.2494 0.0016  -0.0135 -0.0176 666  LEU B C   
13525 O O   . LEU B 668  ? 0.2285 0.2242 0.2404 0.0004  -0.0119 -0.0170 666  LEU B O   
13526 C CB  . LEU B 668  ? 0.3473 0.3346 0.3532 -0.0013 -0.0169 -0.0156 666  LEU B CB  
13527 C CG  . LEU B 668  ? 0.4409 0.4326 0.4468 -0.0042 -0.0159 -0.0138 666  LEU B CG  
13528 C CD1 . LEU B 668  ? 0.3834 0.3727 0.3851 -0.0076 -0.0172 -0.0122 666  LEU B CD1 
13529 C CD2 . LEU B 668  ? 0.5210 0.5138 0.5271 -0.0044 -0.0163 -0.0131 666  LEU B CD2 
13530 N N   . ASN B 669  ? 0.2355 0.2279 0.2492 0.0047  -0.0131 -0.0190 667  ASN B N   
13531 C CA  . ASN B 669  ? 0.2235 0.2210 0.2419 0.0062  -0.0106 -0.0198 667  ASN B CA  
13532 C C   . ASN B 669  ? 0.2310 0.2281 0.2486 0.0069  -0.0096 -0.0205 667  ASN B C   
13533 O O   . ASN B 669  ? 0.2690 0.2703 0.2891 0.0069  -0.0075 -0.0204 667  ASN B O   
13534 C CB  . ASN B 669  ? 0.2574 0.2562 0.2794 0.0089  -0.0104 -0.0209 667  ASN B CB  
13535 C CG  . ASN B 669  ? 0.3193 0.3191 0.3423 0.0082  -0.0112 -0.0202 667  ASN B CG  
13536 O OD1 . ASN B 669  ? 0.3390 0.3366 0.3618 0.0093  -0.0129 -0.0206 667  ASN B OD1 
13537 N ND2 . ASN B 669  ? 0.3592 0.3624 0.3830 0.0064  -0.0101 -0.0193 667  ASN B ND2 
13538 N N   . ALA B 670  ? 0.2065 0.1982 0.2202 0.0076  -0.0111 -0.0212 668  ALA B N   
13539 C CA  . ALA B 670  ? 0.2279 0.2188 0.2400 0.0081  -0.0103 -0.0219 668  ALA B CA  
13540 C C   . ALA B 670  ? 0.2183 0.2104 0.2285 0.0049  -0.0101 -0.0206 668  ALA B C   
13541 O O   . ALA B 670  ? 0.2156 0.2101 0.2265 0.0050  -0.0085 -0.0207 668  ALA B O   
13542 C CB  . ALA B 670  ? 0.2138 0.1979 0.2215 0.0097  -0.0121 -0.0232 668  ALA B CB  
13543 N N   . ILE B 671  ? 0.2016 0.1922 0.2094 0.0020  -0.0117 -0.0191 669  ILE B N   
13544 C CA  . ILE B 671  ? 0.2336 0.2266 0.2404 -0.0011 -0.0115 -0.0175 669  ILE B CA  
13545 C C   . ILE B 671  ? 0.2080 0.2082 0.2195 -0.0009 -0.0089 -0.0170 669  ILE B C   
13546 O O   . ILE B 671  ? 0.2202 0.2233 0.2323 -0.0015 -0.0078 -0.0166 669  ILE B O   
13547 C CB  . ILE B 671  ? 0.2120 0.2030 0.2158 -0.0043 -0.0135 -0.0158 669  ILE B CB  
13548 C CG1 . ILE B 671  ? 0.2220 0.2050 0.2203 -0.0051 -0.0163 -0.0161 669  ILE B CG1 
13549 C CG2 . ILE B 671  ? 0.2184 0.2142 0.2227 -0.0074 -0.0128 -0.0139 669  ILE B CG2 
13550 C CD1 . ILE B 671  ? 0.2904 0.2703 0.2856 -0.0078 -0.0186 -0.0145 669  ILE B CD1 
13551 N N   . ALA B 672  ? 0.2178 0.2206 0.2326 0.0001  -0.0082 -0.0170 670  ALA B N   
13552 C CA  . ALA B 672  ? 0.2481 0.2567 0.2671 0.0006  -0.0059 -0.0167 670  ALA B CA  
13553 C C   . ALA B 672  ? 0.2168 0.2272 0.2380 0.0025  -0.0042 -0.0177 670  ALA B C   
13554 O O   . ALA B 672  ? 0.2617 0.2759 0.2848 0.0022  -0.0026 -0.0171 670  ALA B O   
13555 C CB  . ALA B 672  ? 0.2475 0.2573 0.2691 0.0017  -0.0058 -0.0170 670  ALA B CB  
13556 N N   . GLU B 673  ? 0.2142 0.2218 0.2352 0.0046  -0.0044 -0.0191 671  GLU B N   
13557 C CA  . GLU B 673  ? 0.1978 0.2073 0.2208 0.0064  -0.0026 -0.0199 671  GLU B CA  
13558 C C   . GLU B 673  ? 0.2156 0.2249 0.2359 0.0053  -0.0023 -0.0195 671  GLU B C   
13559 O O   . GLU B 673  ? 0.2159 0.2288 0.2381 0.0054  -0.0006 -0.0191 671  GLU B O   
13560 C CB  . GLU B 673  ? 0.2365 0.2435 0.2595 0.0091  -0.0029 -0.0214 671  GLU B CB  
13561 C CG  . GLU B 673  ? 0.2583 0.2674 0.2827 0.0108  -0.0010 -0.0221 671  GLU B CG  
13562 C CD  . GLU B 673  ? 0.2944 0.3065 0.3234 0.0130  0.0003  -0.0228 671  GLU B CD  
13563 O OE1 . GLU B 673  ? 0.3781 0.3889 0.4080 0.0140  -0.0009 -0.0233 671  GLU B OE1 
13564 O OE2 . GLU B 673  ? 0.2203 0.2361 0.2519 0.0137  0.0024  -0.0227 671  GLU B OE2 
13565 N N   . VAL B 674  ? 0.1862 0.1908 0.2017 0.0042  -0.0042 -0.0196 672  VAL B N   
13566 C CA  . VAL B 674  ? 0.2171 0.2212 0.2297 0.0029  -0.0044 -0.0193 672  VAL B CA  
13567 C C   . VAL B 674  ? 0.1841 0.1926 0.1981 0.0005  -0.0039 -0.0175 672  VAL B C   
13568 O O   . VAL B 674  ? 0.1794 0.1907 0.1938 0.0003  -0.0028 -0.0171 672  VAL B O   
13569 C CB  . VAL B 674  ? 0.1847 0.1822 0.1916 0.0018  -0.0069 -0.0198 672  VAL B CB  
13570 C CG1 . VAL B 674  ? 0.1988 0.1955 0.2024 0.0004  -0.0073 -0.0196 672  VAL B CG1 
13571 C CG2 . VAL B 674  ? 0.2622 0.2551 0.2677 0.0048  -0.0074 -0.0217 672  VAL B CG2 
13572 N N   . ARG B 675  ? 0.1815 0.1912 0.1962 -0.0011 -0.0046 -0.0163 673  ARG B N   
13573 C CA  . ARG B 675  ? 0.1949 0.2096 0.2112 -0.0029 -0.0039 -0.0147 673  ARG B CA  
13574 C C   . ARG B 675  ? 0.2048 0.2242 0.2254 -0.0011 -0.0015 -0.0147 673  ARG B C   
13575 O O   . ARG B 675  ? 0.1890 0.2116 0.2103 -0.0017 -0.0007 -0.0138 673  ARG B O   
13576 C CB  . ARG B 675  ? 0.1998 0.2156 0.2165 -0.0044 -0.0047 -0.0136 673  ARG B CB  
13577 C CG  . ARG B 675  ? 0.1930 0.2048 0.2053 -0.0071 -0.0071 -0.0128 673  ARG B CG  
13578 C CD  . ARG B 675  ? 0.2152 0.2296 0.2281 -0.0090 -0.0075 -0.0113 673  ARG B CD  
13579 N NE  . ARG B 675  ? 0.1970 0.2180 0.2125 -0.0097 -0.0060 -0.0099 673  ARG B NE  
13580 C CZ  . ARG B 675  ? 0.2288 0.2540 0.2459 -0.0103 -0.0053 -0.0088 673  ARG B CZ  
13581 N NH1 . ARG B 675  ? 0.2196 0.2432 0.2360 -0.0103 -0.0058 -0.0088 673  ARG B NH1 
13582 N NH2 . ARG B 675  ? 0.2033 0.2344 0.2225 -0.0107 -0.0040 -0.0076 673  ARG B NH2 
13583 N N   . GLU B 676  ? 0.1950 0.2145 0.2183 0.0010  -0.0006 -0.0157 674  GLU B N   
13584 C CA  . GLU B 676  ? 0.2172 0.2404 0.2442 0.0024  0.0015  -0.0156 674  GLU B CA  
13585 C C   . GLU B 676  ? 0.1870 0.2107 0.2137 0.0031  0.0025  -0.0158 674  GLU B C   
13586 O O   . GLU B 676  ? 0.1697 0.1966 0.1980 0.0031  0.0037  -0.0149 674  GLU B O   
13587 C CB  . GLU B 676  ? 0.2036 0.2266 0.2335 0.0042  0.0020  -0.0166 674  GLU B CB  
13588 C CG  . GLU B 676  ? 0.2188 0.2452 0.2524 0.0053  0.0038  -0.0163 674  GLU B CG  
13589 C CD  . GLU B 676  ? 0.3707 0.3970 0.4073 0.0066  0.0041  -0.0172 674  GLU B CD  
13590 O OE1 . GLU B 676  ? 0.3956 0.4196 0.4317 0.0071  0.0030  -0.0180 674  GLU B OE1 
13591 O OE2 . GLU B 676  ? 0.4648 0.4933 0.5043 0.0071  0.0053  -0.0169 674  GLU B OE2 
13592 N N   . ALA B 677  ? 0.1692 0.1896 0.1935 0.0039  0.0020  -0.0169 675  ALA B N   
13593 C CA  . ALA B 677  ? 0.1897 0.2103 0.2127 0.0045  0.0030  -0.0171 675  ALA B CA  
13594 C C   . ALA B 677  ? 0.2016 0.2235 0.2226 0.0024  0.0023  -0.0158 675  ALA B C   
13595 O O   . ALA B 677  ? 0.1827 0.2071 0.2043 0.0026  0.0035  -0.0152 675  ALA B O   
13596 C CB  . ALA B 677  ? 0.1716 0.1880 0.1915 0.0057  0.0023  -0.0187 675  ALA B CB  
13597 N N   . ILE B 678  ? 0.1904 0.2103 0.2086 0.0003  0.0004  -0.0154 676  ILE B N   
13598 C CA  . ILE B 678  ? 0.1637 0.1854 0.1802 -0.0019 -0.0005 -0.0140 676  ILE B CA  
13599 C C   . ILE B 678  ? 0.1891 0.2165 0.2094 -0.0020 0.0008  -0.0125 676  ILE B C   
13600 O O   . ILE B 678  ? 0.1819 0.2120 0.2024 -0.0024 0.0012  -0.0115 676  ILE B O   
13601 C CB  . ILE B 678  ? 0.1986 0.2177 0.2120 -0.0045 -0.0029 -0.0135 676  ILE B CB  
13602 C CG1 . ILE B 678  ? 0.2035 0.2161 0.2121 -0.0045 -0.0045 -0.0149 676  ILE B CG1 
13603 C CG2 . ILE B 678  ? 0.1756 0.1981 0.1886 -0.0071 -0.0037 -0.0116 676  ILE B CG2 
13604 C CD1 . ILE B 678  ? 0.2279 0.2362 0.2338 -0.0062 -0.0068 -0.0148 676  ILE B CD1 
13605 N N   . ASP B 679  ? 0.1701 0.1991 0.1933 -0.0014 0.0014  -0.0123 677  ASP B N   
13606 C CA  . ASP B 679  ? 0.1887 0.2225 0.2151 -0.0011 0.0026  -0.0111 677  ASP B CA  
13607 C C   . ASP B 679  ? 0.1690 0.2043 0.1976 0.0008  0.0043  -0.0112 677  ASP B C   
13608 O O   . ASP B 679  ? 0.1748 0.2134 0.2046 0.0009  0.0049  -0.0100 677  ASP B O   
13609 C CB  . ASP B 679  ? 0.1772 0.2117 0.2056 -0.0007 0.0028  -0.0113 677  ASP B CB  
13610 C CG  . ASP B 679  ? 0.2277 0.2618 0.2541 -0.0028 0.0012  -0.0106 677  ASP B CG  
13611 O OD1 . ASP B 679  ? 0.2436 0.2787 0.2682 -0.0049 0.0001  -0.0095 677  ASP B OD1 
13612 O OD2 . ASP B 679  ? 0.2470 0.2797 0.2736 -0.0026 0.0009  -0.0111 677  ASP B OD2 
13613 N N   . PHE B 680  ? 0.1458 0.1789 0.1750 0.0024  0.0051  -0.0125 678  PHE B N   
13614 C CA  . PHE B 680  ? 0.1876 0.2221 0.2186 0.0038  0.0068  -0.0123 678  PHE B CA  
13615 C C   . PHE B 680  ? 0.1742 0.2094 0.2030 0.0032  0.0067  -0.0116 678  PHE B C   
13616 O O   . PHE B 680  ? 0.1645 0.2021 0.1945 0.0036  0.0076  -0.0105 678  PHE B O   
13617 C CB  . PHE B 680  ? 0.1339 0.1662 0.1656 0.0052  0.0076  -0.0137 678  PHE B CB  
13618 C CG  . PHE B 680  ? 0.1729 0.2056 0.2080 0.0061  0.0081  -0.0141 678  PHE B CG  
13619 C CD1 . PHE B 680  ? 0.1783 0.2131 0.2161 0.0065  0.0089  -0.0133 678  PHE B CD1 
13620 C CD2 . PHE B 680  ? 0.1583 0.1889 0.1936 0.0067  0.0076  -0.0154 678  PHE B CD2 
13621 C CE1 . PHE B 680  ? 0.2058 0.2404 0.2463 0.0071  0.0091  -0.0139 678  PHE B CE1 
13622 C CE2 . PHE B 680  ? 0.1799 0.2108 0.2182 0.0074  0.0079  -0.0158 678  PHE B CE2 
13623 C CZ  . PHE B 680  ? 0.1672 0.2000 0.2080 0.0075  0.0085  -0.0151 678  PHE B CZ  
13624 N N   . LEU B 681  ? 0.1620 0.1945 0.1871 0.0023  0.0056  -0.0122 679  LEU B N   
13625 C CA  . LEU B 681  ? 0.1424 0.1751 0.1647 0.0017  0.0053  -0.0117 679  LEU B CA  
13626 C C   . LEU B 681  ? 0.1671 0.2035 0.1901 0.0003  0.0046  -0.0099 679  LEU B C   
13627 O O   . LEU B 681  ? 0.1667 0.2052 0.1900 0.0007  0.0053  -0.0088 679  LEU B O   
13628 C CB  . LEU B 681  ? 0.1657 0.1941 0.1833 0.0007  0.0037  -0.0128 679  LEU B CB  
13629 C CG  . LEU B 681  ? 0.1924 0.2174 0.2089 0.0026  0.0044  -0.0147 679  LEU B CG  
13630 C CD1 . LEU B 681  ? 0.1920 0.2120 0.2040 0.0019  0.0024  -0.0159 679  LEU B CD1 
13631 C CD2 . LEU B 681  ? 0.1659 0.1918 0.1816 0.0039  0.0060  -0.0148 679  LEU B CD2 
13632 N N   . ARG B 682  ? 0.1501 0.1874 0.1733 -0.0012 0.0034  -0.0093 680  ARG B N   
13633 C CA  . ARG B 682  ? 0.1718 0.2134 0.1959 -0.0024 0.0027  -0.0075 680  ARG B CA  
13634 C C   . ARG B 682  ? 0.1710 0.2164 0.1990 -0.0007 0.0043  -0.0066 680  ARG B C   
13635 O O   . ARG B 682  ? 0.1731 0.2221 0.2020 -0.0007 0.0043  -0.0052 680  ARG B O   
13636 C CB  . ARG B 682  ? 0.1691 0.2110 0.1923 -0.0047 0.0011  -0.0070 680  ARG B CB  
13637 C CG  . ARG B 682  ? 0.1538 0.1918 0.1725 -0.0068 -0.0009 -0.0075 680  ARG B CG  
13638 C CD  . ARG B 682  ? 0.1756 0.2132 0.1934 -0.0092 -0.0025 -0.0070 680  ARG B CD  
13639 N NE  . ARG B 682  ? 0.1913 0.2248 0.2045 -0.0116 -0.0049 -0.0072 680  ARG B NE  
13640 C CZ  . ARG B 682  ? 0.2061 0.2371 0.2173 -0.0139 -0.0067 -0.0070 680  ARG B CZ  
13641 N NH1 . ARG B 682  ? 0.2053 0.2381 0.2187 -0.0141 -0.0062 -0.0064 680  ARG B NH1 
13642 N NH2 . ARG B 682  ? 0.2072 0.2334 0.2137 -0.0161 -0.0090 -0.0073 680  ARG B NH2 
13643 N N   . TYR B 683  ? 0.1829 0.2273 0.2131 0.0007  0.0054  -0.0075 681  TYR B N   
13644 C CA  . TYR B 683  ? 0.1936 0.2407 0.2270 0.0025  0.0066  -0.0069 681  TYR B CA  
13645 C C   . TYR B 683  ? 0.1761 0.2233 0.2100 0.0037  0.0077  -0.0064 681  TYR B C   
13646 O O   . TYR B 683  ? 0.1693 0.2192 0.2044 0.0045  0.0079  -0.0051 681  TYR B O   
13647 C CB  . TYR B 683  ? 0.1474 0.1929 0.1826 0.0035  0.0073  -0.0080 681  TYR B CB  
13648 C CG  . TYR B 683  ? 0.1961 0.2432 0.2340 0.0053  0.0084  -0.0076 681  TYR B CG  
13649 C CD1 . TYR B 683  ? 0.1886 0.2390 0.2276 0.0057  0.0084  -0.0068 681  TYR B CD1 
13650 C CD2 . TYR B 683  ? 0.1534 0.1986 0.1926 0.0066  0.0094  -0.0080 681  TYR B CD2 
13651 C CE1 . TYR B 683  ? 0.1911 0.2422 0.2320 0.0078  0.0093  -0.0066 681  TYR B CE1 
13652 C CE2 . TYR B 683  ? 0.1767 0.2224 0.2179 0.0082  0.0102  -0.0077 681  TYR B CE2 
13653 C CZ  . TYR B 683  ? 0.1938 0.2422 0.2357 0.0089  0.0100  -0.0071 681  TYR B CZ  
13654 O OH  . TYR B 683  ? 0.1766 0.2248 0.2199 0.0108  0.0106  -0.0070 681  TYR B OH  
13655 N N   . TYR B 684  ? 0.1568 0.2009 0.1896 0.0041  0.0083  -0.0073 682  TYR B N   
13656 C CA  . TYR B 684  ? 0.1647 0.2090 0.1977 0.0050  0.0093  -0.0067 682  TYR B CA  
13657 C C   . TYR B 684  ? 0.1733 0.2192 0.2040 0.0042  0.0086  -0.0055 682  TYR B C   
13658 O O   . TYR B 684  ? 0.1747 0.2220 0.2059 0.0050  0.0091  -0.0043 682  TYR B O   
13659 C CB  . TYR B 684  ? 0.1657 0.2073 0.1982 0.0056  0.0103  -0.0079 682  TYR B CB  
13660 C CG  . TYR B 684  ? 0.1625 0.2032 0.1979 0.0064  0.0110  -0.0088 682  TYR B CG  
13661 C CD1 . TYR B 684  ? 0.1619 0.2035 0.2000 0.0071  0.0114  -0.0082 682  TYR B CD1 
13662 C CD2 . TYR B 684  ? 0.1926 0.2312 0.2277 0.0065  0.0111  -0.0103 682  TYR B CD2 
13663 C CE1 . TYR B 684  ? 0.1751 0.2155 0.2154 0.0077  0.0117  -0.0091 682  TYR B CE1 
13664 C CE2 . TYR B 684  ? 0.1607 0.1986 0.1984 0.0071  0.0115  -0.0110 682  TYR B CE2 
13665 C CZ  . TYR B 684  ? 0.1984 0.2371 0.2386 0.0075  0.0117  -0.0104 682  TYR B CZ  
13666 O OH  . TYR B 684  ? 0.1694 0.2073 0.2120 0.0080  0.0118  -0.0112 682  TYR B OH  
13667 N N   . ALA B 685  ? 0.1656 0.2111 0.1937 0.0026  0.0071  -0.0057 683  ALA B N   
13668 C CA  . ALA B 685  ? 0.1759 0.2231 0.2017 0.0015  0.0060  -0.0045 683  ALA B CA  
13669 C C   . ALA B 685  ? 0.1713 0.2231 0.1997 0.0017  0.0057  -0.0028 683  ALA B C   
13670 O O   . ALA B 685  ? 0.1710 0.2248 0.1994 0.0023  0.0057  -0.0014 683  ALA B O   
13671 C CB  . ALA B 685  ? 0.1416 0.1870 0.1640 -0.0007 0.0041  -0.0052 683  ALA B CB  
13672 N N   . GLU B 686  ? 0.1638 0.2175 0.1944 0.0015  0.0054  -0.0027 684  GLU B N   
13673 C CA  . GLU B 686  ? 0.1675 0.2261 0.2006 0.0022  0.0053  -0.0012 684  GLU B CA  
13674 C C   . GLU B 686  ? 0.1631 0.2218 0.1984 0.0048  0.0068  -0.0008 684  GLU B C   
13675 O O   . GLU B 686  ? 0.1795 0.2411 0.2156 0.0058  0.0066  0.0007  684  GLU B O   
13676 C CB  . GLU B 686  ? 0.1921 0.2528 0.2267 0.0016  0.0050  -0.0013 684  GLU B CB  
13677 C CG  . GLU B 686  ? 0.2071 0.2731 0.2447 0.0031  0.0054  0.0001  684  GLU B CG  
13678 C CD  . GLU B 686  ? 0.3030 0.3740 0.3407 0.0022  0.0042  0.0020  684  GLU B CD  
13679 O OE1 . GLU B 686  ? 0.2600 0.3301 0.2951 -0.0001 0.0028  0.0023  684  GLU B OE1 
13680 O OE2 . GLU B 686  ? 0.2727 0.3483 0.3129 0.0039  0.0045  0.0033  684  GLU B OE2 
13681 N N   . GLN B 687  ? 0.1682 0.2237 0.2044 0.0059  0.0080  -0.0020 685  GLN B N   
13682 C CA  . GLN B 687  ? 0.1728 0.2277 0.2108 0.0081  0.0091  -0.0015 685  GLN B CA  
13683 C C   . GLN B 687  ? 0.1820 0.2365 0.2186 0.0083  0.0092  -0.0004 685  GLN B C   
13684 O O   . GLN B 687  ? 0.1893 0.2448 0.2269 0.0098  0.0094  0.0009  685  GLN B O   
13685 C CB  . GLN B 687  ? 0.2134 0.2647 0.2524 0.0087  0.0101  -0.0030 685  GLN B CB  
13686 C CG  . GLN B 687  ? 0.1869 0.2385 0.2272 0.0089  0.0100  -0.0039 685  GLN B CG  
13687 C CD  . GLN B 687  ? 0.2007 0.2553 0.2427 0.0105  0.0101  -0.0031 685  GLN B CD  
13688 O OE1 . GLN B 687  ? 0.2160 0.2697 0.2589 0.0123  0.0106  -0.0026 685  GLN B OE1 
13689 N NE2 . GLN B 687  ? 0.2366 0.2944 0.2787 0.0100  0.0095  -0.0029 685  GLN B NE2 
13690 N N   . THR B 688  ? 0.1651 0.2179 0.1990 0.0069  0.0090  -0.0008 686  THR B N   
13691 C CA  . THR B 688  ? 0.1553 0.2080 0.1873 0.0069  0.0090  0.0004  686  THR B CA  
13692 C C   . THR B 688  ? 0.1754 0.2319 0.2071 0.0068  0.0077  0.0021  686  THR B C   
13693 O O   . THR B 688  ? 0.2007 0.2580 0.2327 0.0080  0.0078  0.0036  686  THR B O   
13694 C CB  . THR B 688  ? 0.1947 0.2450 0.2233 0.0056  0.0090  -0.0007 686  THR B CB  
13695 O OG1 . THR B 688  ? 0.1939 0.2414 0.2233 0.0061  0.0104  -0.0020 686  THR B OG1 
13696 C CG2 . THR B 688  ? 0.1823 0.2327 0.2081 0.0054  0.0089  0.0005  686  THR B CG2 
13697 N N   . ARG B 689  ? 0.1628 0.2215 0.1939 0.0053  0.0063  0.0020  687  ARG B N   
13698 C CA  . ARG B 689  ? 0.1977 0.2610 0.2292 0.0049  0.0049  0.0038  687  ARG B CA  
13699 C C   . ARG B 689  ? 0.2229 0.2893 0.2578 0.0073  0.0053  0.0050  687  ARG B C   
13700 O O   . ARG B 689  ? 0.2054 0.2751 0.2407 0.0080  0.0045  0.0067  687  ARG B O   
13701 C CB  . ARG B 689  ? 0.1854 0.2508 0.2163 0.0026  0.0033  0.0036  687  ARG B CB  
13702 C CG  . ARG B 689  ? 0.2040 0.2665 0.2305 0.0002  0.0021  0.0028  687  ARG B CG  
13703 C CD  . ARG B 689  ? 0.2250 0.2897 0.2509 -0.0024 0.0002  0.0031  687  ARG B CD  
13704 N NE  . ARG B 689  ? 0.2091 0.2737 0.2368 -0.0028 0.0006  0.0022  687  ARG B NE  
13705 C CZ  . ARG B 689  ? 0.2568 0.3171 0.2824 -0.0040 0.0004  0.0006  687  ARG B CZ  
13706 N NH1 . ARG B 689  ? 0.2245 0.2801 0.2460 -0.0048 -0.0001 -0.0006 687  ARG B NH1 
13707 N NH2 . ARG B 689  ? 0.2112 0.2716 0.2385 -0.0042 0.0007  0.0000  687  ARG B NH2 
13708 N N   . ARG B 690  ? 0.1816 0.2469 0.2187 0.0087  0.0065  0.0040  688  ARG B N   
13709 C CA  . ARG B 690  ? 0.1845 0.2520 0.2243 0.0114  0.0070  0.0049  688  ARG B CA  
13710 C C   . ARG B 690  ? 0.1920 0.2565 0.2317 0.0133  0.0077  0.0055  688  ARG B C   
13711 O O   . ARG B 690  ? 0.2041 0.2701 0.2454 0.0157  0.0077  0.0066  688  ARG B O   
13712 C CB  . ARG B 690  ? 0.1918 0.2589 0.2335 0.0122  0.0078  0.0035  688  ARG B CB  
13713 C CG  . ARG B 690  ? 0.1963 0.2668 0.2384 0.0104  0.0071  0.0032  688  ARG B CG  
13714 C CD  . ARG B 690  ? 0.2448 0.3220 0.2889 0.0111  0.0065  0.0048  688  ARG B CD  
13715 N NE  . ARG B 690  ? 0.2693 0.3476 0.3156 0.0145  0.0074  0.0049  688  ARG B NE  
13716 C CZ  . ARG B 690  ? 0.2946 0.3746 0.3418 0.0169  0.0073  0.0062  688  ARG B CZ  
13717 N NH1 . ARG B 690  ? 0.2565 0.3380 0.3029 0.0162  0.0062  0.0078  688  ARG B NH1 
13718 N NH2 . ARG B 690  ? 0.2609 0.3406 0.3096 0.0203  0.0082  0.0060  688  ARG B NH2 
13719 N N   . THR B 691  ? 0.1898 0.2500 0.2276 0.0125  0.0083  0.0050  689  THR B N   
13720 C CA  . THR B 691  ? 0.2132 0.2701 0.2513 0.0141  0.0092  0.0056  689  THR B CA  
13721 C C   . THR B 691  ? 0.2154 0.2705 0.2510 0.0134  0.0093  0.0068  689  THR B C   
13722 O O   . THR B 691  ? 0.2897 0.3437 0.3252 0.0148  0.0093  0.0083  689  THR B O   
13723 C CB  . THR B 691  ? 0.2184 0.2715 0.2575 0.0142  0.0104  0.0040  689  THR B CB  
13724 O OG1 . THR B 691  ? 0.1891 0.2406 0.2270 0.0122  0.0108  0.0028  689  THR B OG1 
13725 C CG2 . THR B 691  ? 0.2073 0.2617 0.2486 0.0153  0.0103  0.0030  689  THR B CG2 
13726 N N   . LEU B 692  ? 0.2082 0.2624 0.2415 0.0114  0.0094  0.0061  690  LEU B N   
13727 C CA  . LEU B 692  ? 0.2099 0.2616 0.2408 0.0109  0.0102  0.0068  690  LEU B CA  
13728 C C   . LEU B 692  ? 0.2296 0.2830 0.2581 0.0109  0.0091  0.0087  690  LEU B C   
13729 O O   . LEU B 692  ? 0.2606 0.3167 0.2878 0.0099  0.0078  0.0088  690  LEU B O   
13730 C CB  . LEU B 692  ? 0.2090 0.2591 0.2381 0.0093  0.0110  0.0051  690  LEU B CB  
13731 C CG  . LEU B 692  ? 0.2195 0.2676 0.2510 0.0094  0.0121  0.0034  690  LEU B CG  
13732 C CD1 . LEU B 692  ? 0.1991 0.2456 0.2288 0.0083  0.0130  0.0020  690  LEU B CD1 
13733 C CD2 . LEU B 692  ? 0.2161 0.2623 0.2497 0.0106  0.0129  0.0043  690  LEU B CD2 
13734 N N   . GLY B 693  ? 0.2614 0.3130 0.2891 0.0117  0.0096  0.0103  691  GLY B N   
13735 C CA  . GLY B 693  ? 0.2804 0.3331 0.3056 0.0118  0.0086  0.0123  691  GLY B CA  
13736 C C   . GLY B 693  ? 0.2896 0.3393 0.3120 0.0111  0.0098  0.0132  691  GLY B C   
13737 O O   . GLY B 693  ? 0.2885 0.3359 0.3114 0.0106  0.0115  0.0122  691  GLY B O   
13738 N N   . PRO B 694  ? 0.3457 0.3959 0.3653 0.0111  0.0091  0.0151  692  PRO B N   
13739 C CA  . PRO B 694  ? 0.3490 0.3968 0.3653 0.0103  0.0103  0.0161  692  PRO B CA  
13740 C C   . PRO B 694  ? 0.3491 0.3939 0.3671 0.0108  0.0118  0.0170  692  PRO B C   
13741 O O   . PRO B 694  ? 0.3801 0.4234 0.3967 0.0097  0.0135  0.0170  692  PRO B O   
13742 C CB  . PRO B 694  ? 0.4114 0.4605 0.4244 0.0104  0.0088  0.0183  692  PRO B CB  
13743 C CG  . PRO B 694  ? 0.4131 0.4649 0.4287 0.0119  0.0068  0.0189  692  PRO B CG  
13744 C CD  . PRO B 694  ? 0.3668 0.4200 0.3858 0.0118  0.0070  0.0167  692  PRO B CD  
13745 N N   . GLY B 695  ? 0.3138 0.3577 0.3348 0.0123  0.0112  0.0176  693  GLY B N   
13746 C CA  . GLY B 695  ? 0.3092 0.3494 0.3315 0.0125  0.0122  0.0185  693  GLY B CA  
13747 C C   . GLY B 695  ? 0.3470 0.3860 0.3719 0.0117  0.0136  0.0164  693  GLY B C   
13748 O O   . GLY B 695  ? 0.3015 0.3375 0.3275 0.0114  0.0144  0.0170  693  GLY B O   
13749 N N   . HIS B 696  ? 0.2883 0.3295 0.3141 0.0112  0.0138  0.0140  694  HIS B N   
13750 C CA  . HIS B 696  ? 0.2571 0.2975 0.2854 0.0106  0.0149  0.0120  694  HIS B CA  
13751 C C   . HIS B 696  ? 0.2805 0.3216 0.3069 0.0090  0.0164  0.0113  694  HIS B C   
13752 O O   . HIS B 696  ? 0.3002 0.3428 0.3262 0.0086  0.0166  0.0094  694  HIS B O   
13753 C CB  . HIS B 696  ? 0.2532 0.2951 0.2836 0.0113  0.0141  0.0100  694  HIS B CB  
13754 C CG  . HIS B 696  ? 0.2376 0.2797 0.2694 0.0132  0.0128  0.0107  694  HIS B CG  
13755 N ND1 . HIS B 696  ? 0.2485 0.2940 0.2802 0.0139  0.0114  0.0108  694  HIS B ND1 
13756 C CD2 . HIS B 696  ? 0.2744 0.3139 0.3077 0.0146  0.0125  0.0115  694  HIS B CD2 
13757 C CE1 . HIS B 696  ? 0.2472 0.2927 0.2805 0.0159  0.0106  0.0115  694  HIS B CE1 
13758 N NE2 . HIS B 696  ? 0.2588 0.3003 0.2929 0.0165  0.0112  0.0118  694  HIS B NE2 
13759 N N   . GLY B 697  ? 0.3262 0.3660 0.3514 0.0083  0.0176  0.0130  695  GLY B N   
13760 C CA  . GLY B 697  ? 0.3010 0.3419 0.3241 0.0071  0.0193  0.0127  695  GLY B CA  
13761 C C   . GLY B 697  ? 0.2717 0.3132 0.2974 0.0067  0.0205  0.0105  695  GLY B C   
13762 O O   . GLY B 697  ? 0.2617 0.3021 0.2910 0.0067  0.0205  0.0100  695  GLY B O   
13763 N N   . PRO B 698  ? 0.2943 0.3373 0.3179 0.0064  0.0216  0.0092  696  PRO B N   
13764 C CA  . PRO B 698  ? 0.2544 0.2983 0.2804 0.0063  0.0227  0.0071  696  PRO B CA  
13765 C C   . PRO B 698  ? 0.2433 0.2876 0.2716 0.0054  0.0246  0.0083  696  PRO B C   
13766 O O   . PRO B 698  ? 0.2372 0.2813 0.2643 0.0047  0.0253  0.0107  696  PRO B O   
13767 C CB  . PRO B 698  ? 0.3146 0.3596 0.3369 0.0065  0.0232  0.0056  696  PRO B CB  
13768 C CG  . PRO B 698  ? 0.3650 0.4102 0.3832 0.0062  0.0235  0.0076  696  PRO B CG  
13769 C CD  . PRO B 698  ? 0.3230 0.3670 0.3418 0.0063  0.0218  0.0095  696  PRO B CD  
13770 N N   . LEU B 699  ? 0.2179 0.2629 0.2495 0.0053  0.0252  0.0067  697  LEU B N   
13771 C CA  . LEU B 699  ? 0.2074 0.2538 0.2415 0.0043  0.0270  0.0076  697  LEU B CA  
13772 C C   . LEU B 699  ? 0.2319 0.2812 0.2636 0.0043  0.0291  0.0076  697  LEU B C   
13773 O O   . LEU B 699  ? 0.2376 0.2884 0.2695 0.0033  0.0308  0.0097  697  LEU B O   
13774 C CB  . LEU B 699  ? 0.2263 0.2731 0.2649 0.0043  0.0268  0.0058  697  LEU B CB  
13775 C CG  . LEU B 699  ? 0.2463 0.2902 0.2873 0.0043  0.0248  0.0056  697  LEU B CG  
13776 C CD1 . LEU B 699  ? 0.2527 0.2972 0.2975 0.0043  0.0247  0.0038  697  LEU B CD1 
13777 C CD2 . LEU B 699  ? 0.2572 0.2990 0.2988 0.0033  0.0245  0.0081  697  LEU B CD2 
13778 N N   . GLY B 700  ? 0.2291 0.2791 0.2583 0.0056  0.0291  0.0054  698  GLY B N   
13779 C CA  . GLY B 700  ? 0.2295 0.2821 0.2566 0.0062  0.0313  0.0047  698  GLY B CA  
13780 C C   . GLY B 700  ? 0.2425 0.2960 0.2717 0.0073  0.0314  0.0019  698  GLY B C   
13781 O O   . GLY B 700  ? 0.2093 0.2609 0.2404 0.0076  0.0296  0.0005  698  GLY B O   
13782 N N   . PRO B 701  ? 0.2263 0.2828 0.2553 0.0082  0.0336  0.0012  699  PRO B N   
13783 C CA  . PRO B 701  ? 0.2259 0.2831 0.2564 0.0097  0.0337  -0.0015 699  PRO B CA  
13784 C C   . PRO B 701  ? 0.2497 0.3069 0.2861 0.0091  0.0326  -0.0018 699  PRO B C   
13785 O O   . PRO B 701  ? 0.2006 0.2596 0.2410 0.0077  0.0333  -0.0001 699  PRO B O   
13786 C CB  . PRO B 701  ? 0.2244 0.2858 0.2546 0.0107  0.0366  -0.0015 699  PRO B CB  
13787 C CG  . PRO B 701  ? 0.2395 0.3013 0.2653 0.0100  0.0377  0.0005  699  PRO B CG  
13788 C CD  . PRO B 701  ? 0.2187 0.2783 0.2458 0.0079  0.0362  0.0029  699  PRO B CD  
13789 N N   . ILE B 702  ? 0.2249 0.2797 0.2613 0.0100  0.0308  -0.0040 700  ILE B N   
13790 C CA  . ILE B 702  ? 0.1900 0.2444 0.2312 0.0096  0.0296  -0.0046 700  ILE B CA  
13791 C C   . ILE B 702  ? 0.1869 0.2426 0.2294 0.0113  0.0300  -0.0068 700  ILE B C   
13792 O O   . ILE B 702  ? 0.1942 0.2483 0.2330 0.0128  0.0295  -0.0087 700  ILE B O   
13793 C CB  . ILE B 702  ? 0.2291 0.2798 0.2696 0.0091  0.0271  -0.0049 700  ILE B CB  
13794 C CG1 . ILE B 702  ? 0.2013 0.2510 0.2416 0.0078  0.0268  -0.0025 700  ILE B CG1 
13795 C CG2 . ILE B 702  ? 0.2509 0.3009 0.2953 0.0092  0.0258  -0.0062 700  ILE B CG2 
13796 C CD1 . ILE B 702  ? 0.2709 0.3179 0.3110 0.0075  0.0246  -0.0027 700  ILE B CD1 
13797 N N   . VAL B 703  ? 0.1762 0.2346 0.2237 0.0110  0.0305  -0.0066 701  VAL B N   
13798 C CA  . VAL B 703  ? 0.1903 0.2502 0.2399 0.0127  0.0306  -0.0086 701  VAL B CA  
13799 C C   . VAL B 703  ? 0.1937 0.2505 0.2449 0.0125  0.0281  -0.0098 701  VAL B C   
13800 O O   . VAL B 703  ? 0.1823 0.2386 0.2366 0.0109  0.0271  -0.0087 701  VAL B O   
13801 C CB  . VAL B 703  ? 0.1650 0.2304 0.2196 0.0124  0.0325  -0.0075 701  VAL B CB  
13802 C CG1 . VAL B 703  ? 0.1952 0.2624 0.2528 0.0142  0.0322  -0.0094 701  VAL B CG1 
13803 C CG2 . VAL B 703  ? 0.1648 0.2338 0.2173 0.0129  0.0353  -0.0064 701  VAL B CG2 
13804 N N   . CYS B 704  ? 0.1622 0.2165 0.2108 0.0141  0.0269  -0.0119 702  CYS B N   
13805 C CA  . CYS B 704  ? 0.1689 0.2202 0.2182 0.0139  0.0245  -0.0131 702  CYS B CA  
13806 C C   . CYS B 704  ? 0.1682 0.2207 0.2199 0.0156  0.0243  -0.0146 702  CYS B C   
13807 O O   . CYS B 704  ? 0.1725 0.2247 0.2216 0.0177  0.0248  -0.0161 702  CYS B O   
13808 C CB  . CYS B 704  ? 0.1740 0.2210 0.2182 0.0140  0.0229  -0.0140 702  CYS B CB  
13809 S SG  . CYS B 704  ? 0.2045 0.2503 0.2460 0.0123  0.0227  -0.0121 702  CYS B SG  
13810 N N   . ILE B 705  ? 0.1790 0.2328 0.2354 0.0149  0.0236  -0.0143 703  ILE B N   
13811 C CA  . ILE B 705  ? 0.1434 0.1991 0.2029 0.0164  0.0233  -0.0156 703  ILE B CA  
13812 C C   . ILE B 705  ? 0.1703 0.2222 0.2297 0.0161  0.0206  -0.0166 703  ILE B C   
13813 O O   . ILE B 705  ? 0.2001 0.2509 0.2609 0.0142  0.0196  -0.0157 703  ILE B O   
13814 C CB  . ILE B 705  ? 0.1506 0.2115 0.2160 0.0156  0.0245  -0.0142 703  ILE B CB  
13815 C CG1 . ILE B 705  ? 0.1959 0.2610 0.2612 0.0158  0.0273  -0.0131 703  ILE B CG1 
13816 C CG2 . ILE B 705  ? 0.1943 0.2575 0.2633 0.0171  0.0237  -0.0155 703  ILE B CG2 
13817 C CD1 . ILE B 705  ? 0.2503 0.3210 0.3214 0.0143  0.0286  -0.0112 703  ILE B CD1 
13818 N N   . SER B 706  ? 0.1849 0.2346 0.2421 0.0179  0.0196  -0.0183 704  SER B N   
13819 C CA  . SER B 706  ? 0.1863 0.2318 0.2420 0.0175  0.0171  -0.0192 704  SER B CA  
13820 C C   . SER B 706  ? 0.1800 0.2261 0.2383 0.0190  0.0159  -0.0203 704  SER B C   
13821 O O   . SER B 706  ? 0.1705 0.2197 0.2308 0.0210  0.0170  -0.0208 704  SER B O   
13822 C CB  . SER B 706  ? 0.2040 0.2451 0.2538 0.0179  0.0162  -0.0201 704  SER B CB  
13823 O OG  . SER B 706  ? 0.1765 0.2172 0.2237 0.0202  0.0170  -0.0213 704  SER B OG  
13824 N N   . PRO B 707  ? 0.2214 0.2648 0.2798 0.0183  0.0137  -0.0206 705  PRO B N   
13825 C CA  . PRO B 707  ? 0.2289 0.2727 0.2898 0.0195  0.0124  -0.0215 705  PRO B CA  
13826 C C   . PRO B 707  ? 0.2199 0.2595 0.2768 0.0214  0.0109  -0.0230 705  PRO B C   
13827 O O   . PRO B 707  ? 0.2300 0.2660 0.2819 0.0213  0.0107  -0.0234 705  PRO B O   
13828 C CB  . PRO B 707  ? 0.2085 0.2513 0.2710 0.0174  0.0107  -0.0208 705  PRO B CB  
13829 C CG  . PRO B 707  ? 0.2041 0.2436 0.2627 0.0160  0.0105  -0.0204 705  PRO B CG  
13830 C CD  . PRO B 707  ? 0.2466 0.2872 0.3033 0.0161  0.0126  -0.0200 705  PRO B CD  
13831 N N   . TRP B 708  ? 0.2034 0.2435 0.2625 0.0230  0.0097  -0.0238 706  TRP B N   
13832 C CA  . TRP B 708  ? 0.2110 0.2467 0.2663 0.0249  0.0080  -0.0252 706  TRP B CA  
13833 C C   . TRP B 708  ? 0.2011 0.2320 0.2537 0.0233  0.0054  -0.0251 706  TRP B C   
13834 O O   . TRP B 708  ? 0.2184 0.2446 0.2670 0.0243  0.0038  -0.0260 706  TRP B O   
13835 C CB  . TRP B 708  ? 0.1825 0.2209 0.2412 0.0278  0.0077  -0.0260 706  TRP B CB  
13836 C CG  . TRP B 708  ? 0.2181 0.2605 0.2827 0.0267  0.0071  -0.0252 706  TRP B CG  
13837 C CD1 . TRP B 708  ? 0.2557 0.3046 0.3259 0.0263  0.0087  -0.0242 706  TRP B CD1 
13838 C CD2 . TRP B 708  ? 0.1698 0.2098 0.2347 0.0256  0.0045  -0.0251 706  TRP B CD2 
13839 N NE1 . TRP B 708  ? 0.2520 0.3024 0.3260 0.0250  0.0071  -0.0237 706  TRP B NE1 
13840 C CE2 . TRP B 708  ? 0.2243 0.2693 0.2950 0.0246  0.0045  -0.0242 706  TRP B CE2 
13841 C CE3 . TRP B 708  ? 0.2292 0.2634 0.2898 0.0252  0.0021  -0.0255 706  TRP B CE3 
13842 C CZ2 . TRP B 708  ? 0.2373 0.2814 0.3094 0.0235  0.0022  -0.0240 706  TRP B CZ2 
13843 C CZ3 . TRP B 708  ? 0.2174 0.2511 0.2796 0.0241  0.0000  -0.0252 706  TRP B CZ3 
13844 C CH2 . TRP B 708  ? 0.2250 0.2635 0.2927 0.0233  0.0001  -0.0246 706  TRP B CH2 
13845 N N   . ASN B 709  ? 0.2179 0.2497 0.2724 0.0209  0.0050  -0.0241 707  ASN B N   
13846 C CA  . ASN B 709  ? 0.2195 0.2475 0.2717 0.0196  0.0027  -0.0240 707  ASN B CA  
13847 C C   . ASN B 709  ? 0.2490 0.2737 0.2965 0.0178  0.0025  -0.0236 707  ASN B C   
13848 O O   . ASN B 709  ? 0.2563 0.2773 0.3007 0.0170  0.0007  -0.0236 707  ASN B O   
13849 C CB  . ASN B 709  ? 0.1996 0.2299 0.2557 0.0182  0.0021  -0.0234 707  ASN B CB  
13850 C CG  . ASN B 709  ? 0.3031 0.3356 0.3606 0.0163  0.0036  -0.0223 707  ASN B CG  
13851 O OD1 . ASN B 709  ? 0.3156 0.3498 0.3732 0.0163  0.0055  -0.0219 707  ASN B OD1 
13852 N ND2 . ASN B 709  ? 0.2586 0.2908 0.3170 0.0148  0.0027  -0.0219 707  ASN B ND2 
13853 N N   . PHE B 710  ? 0.2322 0.2584 0.2793 0.0170  0.0044  -0.0230 708  PHE B N   
13854 C CA  . PHE B 710  ? 0.2333 0.2569 0.2759 0.0156  0.0042  -0.0226 708  PHE B CA  
13855 C C   . PHE B 710  ? 0.2125 0.2364 0.2534 0.0167  0.0057  -0.0230 708  PHE B C   
13856 O O   . PHE B 710  ? 0.1949 0.2209 0.2360 0.0158  0.0072  -0.0222 708  PHE B O   
13857 C CB  . PHE B 710  ? 0.2465 0.2717 0.2900 0.0135  0.0047  -0.0214 708  PHE B CB  
13858 C CG  . PHE B 710  ? 0.2785 0.3030 0.3228 0.0125  0.0032  -0.0212 708  PHE B CG  
13859 C CD1 . PHE B 710  ? 0.3235 0.3448 0.3642 0.0116  0.0015  -0.0211 708  PHE B CD1 
13860 C CD2 . PHE B 710  ? 0.3163 0.3432 0.3645 0.0125  0.0035  -0.0210 708  PHE B CD2 
13861 C CE1 . PHE B 710  ? 0.3642 0.3850 0.4052 0.0108  0.0003  -0.0209 708  PHE B CE1 
13862 C CE2 . PHE B 710  ? 0.3606 0.3865 0.4089 0.0118  0.0021  -0.0210 708  PHE B CE2 
13863 C CZ  . PHE B 710  ? 0.3254 0.3484 0.3700 0.0111  0.0006  -0.0209 708  PHE B CZ  
13864 N N   . PRO B 711  ? 0.2052 0.2267 0.2440 0.0187  0.0052  -0.0243 709  PRO B N   
13865 C CA  . PRO B 711  ? 0.1957 0.2180 0.2332 0.0204  0.0068  -0.0249 709  PRO B CA  
13866 C C   . PRO B 711  ? 0.2164 0.2361 0.2489 0.0192  0.0069  -0.0248 709  PRO B C   
13867 O O   . PRO B 711  ? 0.1970 0.2175 0.2281 0.0203  0.0084  -0.0252 709  PRO B O   
13868 C CB  . PRO B 711  ? 0.2185 0.2383 0.2548 0.0232  0.0058  -0.0265 709  PRO B CB  
13869 C CG  . PRO B 711  ? 0.2319 0.2469 0.2656 0.0221  0.0031  -0.0265 709  PRO B CG  
13870 C CD  . PRO B 711  ? 0.2115 0.2292 0.2487 0.0198  0.0029  -0.0252 709  PRO B CD  
13871 N N   . LEU B 712  ? 0.2372 0.2541 0.2671 0.0169  0.0052  -0.0241 710  LEU B N   
13872 C CA  . LEU B 712  ? 0.1979 0.2134 0.2240 0.0152  0.0052  -0.0236 710  LEU B CA  
13873 C C   . LEU B 712  ? 0.2104 0.2293 0.2387 0.0130  0.0058  -0.0219 710  LEU B C   
13874 O O   . LEU B 712  ? 0.2039 0.2245 0.2315 0.0125  0.0071  -0.0212 710  LEU B O   
13875 C CB  . LEU B 712  ? 0.2012 0.2111 0.2221 0.0141  0.0026  -0.0240 710  LEU B CB  
13876 C CG  . LEU B 712  ? 0.1839 0.1925 0.2008 0.0122  0.0023  -0.0234 710  LEU B CG  
13877 C CD1 . LEU B 712  ? 0.1938 0.2023 0.2084 0.0139  0.0037  -0.0243 710  LEU B CD1 
13878 C CD2 . LEU B 712  ? 0.2246 0.2278 0.2366 0.0103  -0.0005 -0.0234 710  LEU B CD2 
13879 N N   . ALA B 713  ? 0.1958 0.2154 0.2264 0.0119  0.0051  -0.0212 711  ALA B N   
13880 C CA  . ALA B 713  ? 0.2066 0.2286 0.2385 0.0101  0.0054  -0.0198 711  ALA B CA  
13881 C C   . ALA B 713  ? 0.2053 0.2313 0.2409 0.0106  0.0075  -0.0191 711  ALA B C   
13882 O O   . ALA B 713  ? 0.1886 0.2161 0.2237 0.0098  0.0083  -0.0181 711  ALA B O   
13883 C CB  . ALA B 713  ? 0.1998 0.2215 0.2328 0.0091  0.0041  -0.0194 711  ALA B CB  
13884 N N   . ILE B 714  ? 0.1864 0.2140 0.2256 0.0117  0.0082  -0.0195 712  ILE B N   
13885 C CA  . ILE B 714  ? 0.1799 0.2111 0.2226 0.0118  0.0100  -0.0187 712  ILE B CA  
13886 C C   . ILE B 714  ? 0.1971 0.2294 0.2388 0.0127  0.0116  -0.0187 712  ILE B C   
13887 O O   . ILE B 714  ? 0.1819 0.2161 0.2240 0.0121  0.0129  -0.0175 712  ILE B O   
13888 C CB  . ILE B 714  ? 0.2302 0.2629 0.2772 0.0124  0.0100  -0.0189 712  ILE B CB  
13889 C CG1 . ILE B 714  ? 0.2210 0.2528 0.2686 0.0113  0.0087  -0.0187 712  ILE B CG1 
13890 C CG2 . ILE B 714  ? 0.2099 0.2460 0.2603 0.0124  0.0119  -0.0181 712  ILE B CG2 
13891 C CD1 . ILE B 714  ? 0.3056 0.3386 0.3572 0.0115  0.0083  -0.0189 712  ILE B CD1 
13892 N N   . PHE B 715  ? 0.1785 0.2094 0.2183 0.0142  0.0116  -0.0199 713  PHE B N   
13893 C CA  . PHE B 715  ? 0.1760 0.2073 0.2135 0.0152  0.0130  -0.0202 713  PHE B CA  
13894 C C   . PHE B 715  ? 0.1747 0.2051 0.2087 0.0137  0.0129  -0.0193 713  PHE B C   
13895 O O   . PHE B 715  ? 0.1566 0.1893 0.1908 0.0135  0.0144  -0.0184 713  PHE B O   
13896 C CB  . PHE B 715  ? 0.1987 0.2270 0.2331 0.0171  0.0122  -0.0220 713  PHE B CB  
13897 C CG  . PHE B 715  ? 0.2005 0.2287 0.2317 0.0184  0.0135  -0.0226 713  PHE B CG  
13898 C CD1 . PHE B 715  ? 0.1879 0.2198 0.2214 0.0202  0.0158  -0.0228 713  PHE B CD1 
13899 C CD2 . PHE B 715  ? 0.2342 0.2586 0.2597 0.0178  0.0125  -0.0231 713  PHE B CD2 
13900 C CE1 . PHE B 715  ? 0.2086 0.2405 0.2387 0.0217  0.0172  -0.0235 713  PHE B CE1 
13901 C CE2 . PHE B 715  ? 0.2022 0.2260 0.2241 0.0191  0.0136  -0.0238 713  PHE B CE2 
13902 C CZ  . PHE B 715  ? 0.2425 0.2700 0.2664 0.0212  0.0160  -0.0241 713  PHE B CZ  
13903 N N   . THR B 716  ? 0.1696 0.1970 0.2006 0.0125  0.0109  -0.0194 714  THR B N   
13904 C CA  . THR B 716  ? 0.1770 0.2038 0.2048 0.0110  0.0105  -0.0185 714  THR B CA  
13905 C C   . THR B 716  ? 0.1834 0.2133 0.2139 0.0098  0.0112  -0.0168 714  THR B C   
13906 O O   . THR B 716  ? 0.1674 0.1986 0.1967 0.0093  0.0119  -0.0158 714  THR B O   
13907 C CB  . THR B 716  ? 0.1469 0.1702 0.1712 0.0097  0.0081  -0.0189 714  THR B CB  
13908 O OG1 . THR B 716  ? 0.1981 0.2176 0.2190 0.0109  0.0073  -0.0205 714  THR B OG1 
13909 C CG2 . THR B 716  ? 0.2136 0.2372 0.2352 0.0078  0.0075  -0.0177 714  THR B CG2 
13910 N N   . GLY B 717  ? 0.1707 0.2016 0.2046 0.0095  0.0109  -0.0164 715  GLY B N   
13911 C CA  . GLY B 717  ? 0.1700 0.2032 0.2061 0.0087  0.0114  -0.0149 715  GLY B CA  
13912 C C   . GLY B 717  ? 0.1882 0.2236 0.2261 0.0092  0.0132  -0.0141 715  GLY B C   
13913 O O   . GLY B 717  ? 0.1611 0.1976 0.1983 0.0087  0.0136  -0.0128 715  GLY B O   
13914 N N   . GLN B 718  ? 0.1567 0.1931 0.1971 0.0101  0.0143  -0.0145 716  GLN B N   
13915 C CA  . GLN B 718  ? 0.1506 0.1891 0.1926 0.0102  0.0161  -0.0134 716  GLN B CA  
13916 C C   . GLN B 718  ? 0.1709 0.2096 0.2093 0.0104  0.0170  -0.0131 716  GLN B C   
13917 O O   . GLN B 718  ? 0.1706 0.2105 0.2088 0.0098  0.0177  -0.0116 716  GLN B O   
13918 C CB  . GLN B 718  ? 0.1554 0.1956 0.2007 0.0110  0.0171  -0.0140 716  GLN B CB  
13919 C CG  . GLN B 718  ? 0.1668 0.2068 0.2156 0.0107  0.0161  -0.0143 716  GLN B CG  
13920 C CD  . GLN B 718  ? 0.2091 0.2515 0.2618 0.0113  0.0170  -0.0145 716  GLN B CD  
13921 O OE1 . GLN B 718  ? 0.2377 0.2809 0.2938 0.0105  0.0167  -0.0139 716  GLN B OE1 
13922 N NE2 . GLN B 718  ? 0.2027 0.2463 0.2549 0.0126  0.0178  -0.0154 716  GLN B NE2 
13923 N N   . ILE B 719  ? 0.1583 0.1955 0.1936 0.0112  0.0167  -0.0145 717  ILE B N   
13924 C CA  . ILE B 719  ? 0.1883 0.2253 0.2196 0.0115  0.0174  -0.0144 717  ILE B CA  
13925 C C   . ILE B 719  ? 0.1608 0.1970 0.1894 0.0101  0.0163  -0.0134 717  ILE B C   
13926 O O   . ILE B 719  ? 0.1945 0.2318 0.2216 0.0099  0.0171  -0.0122 717  ILE B O   
13927 C CB  . ILE B 719  ? 0.1599 0.1946 0.1880 0.0129  0.0170  -0.0164 717  ILE B CB  
13928 C CG1 . ILE B 719  ? 0.1551 0.1918 0.1860 0.0146  0.0187  -0.0172 717  ILE B CG1 
13929 C CG2 . ILE B 719  ? 0.2220 0.2551 0.2446 0.0129  0.0170  -0.0167 717  ILE B CG2 
13930 C CD1 . ILE B 719  ? 0.2078 0.2418 0.2363 0.0164  0.0178  -0.0193 717  ILE B CD1 
13931 N N   . ALA B 720  ? 0.1716 0.2062 0.1996 0.0092  0.0143  -0.0137 718  ALA B N   
13932 C CA  . ALA B 720  ? 0.1687 0.2033 0.1944 0.0079  0.0131  -0.0126 718  ALA B CA  
13933 C C   . ALA B 720  ? 0.1694 0.2066 0.1977 0.0076  0.0139  -0.0107 718  ALA B C   
13934 O O   . ALA B 720  ? 0.1661 0.2041 0.1924 0.0072  0.0138  -0.0095 718  ALA B O   
13935 C CB  . ALA B 720  ? 0.1782 0.2115 0.2037 0.0068  0.0111  -0.0130 718  ALA B CB  
13936 N N   . ALA B 721  ? 0.1639 0.2021 0.1962 0.0079  0.0144  -0.0104 719  ALA B N   
13937 C CA  . ALA B 721  ? 0.1821 0.2219 0.2166 0.0078  0.0150  -0.0087 719  ALA B CA  
13938 C C   . ALA B 721  ? 0.1581 0.1987 0.1919 0.0081  0.0165  -0.0076 719  ALA B C   
13939 O O   . ALA B 721  ? 0.1629 0.2043 0.1958 0.0078  0.0165  -0.0060 719  ALA B O   
13940 C CB  . ALA B 721  ? 0.1884 0.2282 0.2269 0.0081  0.0152  -0.0088 719  ALA B CB  
13941 N N   . ALA B 722  ? 0.1295 0.1704 0.1638 0.0086  0.0179  -0.0083 720  ALA B N   
13942 C CA  . ALA B 722  ? 0.1859 0.2280 0.2195 0.0087  0.0196  -0.0071 720  ALA B CA  
13943 C C   . ALA B 722  ? 0.1735 0.2153 0.2023 0.0086  0.0193  -0.0068 720  ALA B C   
13944 O O   . ALA B 722  ? 0.1714 0.2139 0.1990 0.0083  0.0198  -0.0051 720  ALA B O   
13945 C CB  . ALA B 722  ? 0.1282 0.1715 0.1633 0.0094  0.0212  -0.0079 720  ALA B CB  
13946 N N   . LEU B 723  ? 0.1721 0.2123 0.1977 0.0088  0.0184  -0.0085 721  LEU B N   
13947 C CA  . LEU B 723  ? 0.1779 0.2172 0.1985 0.0085  0.0178  -0.0084 721  LEU B CA  
13948 C C   . LEU B 723  ? 0.1713 0.2112 0.1913 0.0075  0.0163  -0.0068 721  LEU B C   
13949 O O   . LEU B 723  ? 0.2025 0.2430 0.2200 0.0072  0.0165  -0.0055 721  LEU B O   
13950 C CB  . LEU B 723  ? 0.1814 0.2181 0.1987 0.0087  0.0165  -0.0106 721  LEU B CB  
13951 C CG  . LEU B 723  ? 0.1984 0.2341 0.2145 0.0103  0.0178  -0.0124 721  LEU B CG  
13952 C CD1 . LEU B 723  ? 0.2017 0.2338 0.2148 0.0104  0.0159  -0.0144 721  LEU B CD1 
13953 C CD2 . LEU B 723  ? 0.2013 0.2377 0.2139 0.0110  0.0194  -0.0122 721  LEU B CD2 
13954 N N   . VAL B 724  ? 0.1609 0.2009 0.1831 0.0069  0.0149  -0.0068 722  VAL B N   
13955 C CA  . VAL B 724  ? 0.1872 0.2284 0.2088 0.0061  0.0135  -0.0053 722  VAL B CA  
13956 C C   . VAL B 724  ? 0.1861 0.2289 0.2099 0.0066  0.0143  -0.0033 722  VAL B C   
13957 O O   . VAL B 724  ? 0.1918 0.2358 0.2144 0.0063  0.0135  -0.0018 722  VAL B O   
13958 C CB  . VAL B 724  ? 0.1647 0.2061 0.1880 0.0055  0.0119  -0.0058 722  VAL B CB  
13959 C CG1 . VAL B 724  ? 0.1854 0.2277 0.2133 0.0062  0.0125  -0.0054 722  VAL B CG1 
13960 C CG2 . VAL B 724  ? 0.1728 0.2157 0.1943 0.0044  0.0100  -0.0047 722  VAL B CG2 
13961 N N   . ALA B 725  ? 0.1769 0.2196 0.2036 0.0072  0.0158  -0.0031 723  ALA B N   
13962 C CA  . ALA B 725  ? 0.1948 0.2381 0.2229 0.0075  0.0166  -0.0011 723  ALA B CA  
13963 C C   . ALA B 725  ? 0.2189 0.2624 0.2440 0.0074  0.0176  0.0000  723  ALA B C   
13964 O O   . ALA B 725  ? 0.2322 0.2759 0.2578 0.0074  0.0182  0.0020  723  ALA B O   
13965 C CB  . ALA B 725  ? 0.2080 0.2508 0.2401 0.0078  0.0176  -0.0012 723  ALA B CB  
13966 N N   . GLY B 726  ? 0.2153 0.2585 0.2369 0.0072  0.0179  -0.0012 724  GLY B N   
13967 C CA  . GLY B 726  ? 0.1925 0.2360 0.2104 0.0072  0.0189  -0.0003 724  GLY B CA  
13968 C C   . GLY B 726  ? 0.2194 0.2634 0.2375 0.0076  0.0213  -0.0006 724  GLY B C   
13969 O O   . GLY B 726  ? 0.2300 0.2746 0.2455 0.0075  0.0225  0.0006  724  GLY B O   
13970 N N   . ASN B 727  ? 0.1715 0.2155 0.1925 0.0080  0.0220  -0.0021 725  ASN B N   
13971 C CA  . ASN B 727  ? 0.1901 0.2355 0.2123 0.0085  0.0242  -0.0024 725  ASN B CA  
13972 C C   . ASN B 727  ? 0.1861 0.2310 0.2057 0.0096  0.0246  -0.0049 725  ASN B C   
13973 O O   . ASN B 727  ? 0.1925 0.2357 0.2121 0.0099  0.0230  -0.0067 725  ASN B O   
13974 C CB  . ASN B 727  ? 0.1911 0.2373 0.2189 0.0083  0.0247  -0.0023 725  ASN B CB  
13975 C CG  . ASN B 727  ? 0.2519 0.2975 0.2820 0.0075  0.0239  -0.0003 725  ASN B CG  
13976 O OD1 . ASN B 727  ? 0.2261 0.2724 0.2562 0.0069  0.0249  0.0018  725  ASN B OD1 
13977 N ND2 . ASN B 727  ? 0.2115 0.2558 0.2434 0.0075  0.0222  -0.0008 725  ASN B ND2 
13978 N N   . PRO B 728  ? 0.1961 0.2423 0.2132 0.0104  0.0265  -0.0051 726  PRO B N   
13979 C CA  . PRO B 728  ? 0.2170 0.2628 0.2324 0.0120  0.0271  -0.0076 726  PRO B CA  
13980 C C   . PRO B 728  ? 0.2007 0.2480 0.2215 0.0126  0.0279  -0.0084 726  PRO B C   
13981 O O   . PRO B 728  ? 0.2014 0.2510 0.2268 0.0117  0.0287  -0.0067 726  PRO B O   
13982 C CB  . PRO B 728  ? 0.1979 0.2454 0.2096 0.0128  0.0294  -0.0073 726  PRO B CB  
13983 C CG  . PRO B 728  ? 0.2189 0.2690 0.2333 0.0114  0.0308  -0.0042 726  PRO B CG  
13984 C CD  . PRO B 728  ? 0.1906 0.2391 0.2071 0.0100  0.0285  -0.0029 726  PRO B CD  
13985 N N   . VAL B 729  ? 0.1861 0.2319 0.2063 0.0139  0.0272  -0.0108 727  VAL B N   
13986 C CA  . VAL B 729  ? 0.2074 0.2541 0.2325 0.0145  0.0272  -0.0117 727  VAL B CA  
13987 C C   . VAL B 729  ? 0.1941 0.2425 0.2190 0.0168  0.0289  -0.0134 727  VAL B C   
13988 O O   . VAL B 729  ? 0.1739 0.2203 0.1938 0.0183  0.0289  -0.0151 727  VAL B O   
13989 C CB  . VAL B 729  ? 0.1975 0.2408 0.2228 0.0141  0.0245  -0.0129 727  VAL B CB  
13990 C CG1 . VAL B 729  ? 0.2258 0.2696 0.2550 0.0151  0.0244  -0.0143 727  VAL B CG1 
13991 C CG2 . VAL B 729  ? 0.1755 0.2185 0.2026 0.0122  0.0232  -0.0112 727  VAL B CG2 
13992 N N   . LEU B 730  ? 0.1852 0.2374 0.2156 0.0170  0.0303  -0.0129 728  LEU B N   
13993 C CA  . LEU B 730  ? 0.1487 0.2032 0.1807 0.0194  0.0316  -0.0145 728  LEU B CA  
13994 C C   . LEU B 730  ? 0.1802 0.2331 0.2157 0.0195  0.0296  -0.0156 728  LEU B C   
13995 O O   . LEU B 730  ? 0.2017 0.2562 0.2422 0.0180  0.0292  -0.0144 728  LEU B O   
13996 C CB  . LEU B 730  ? 0.1798 0.2403 0.2158 0.0194  0.0344  -0.0129 728  LEU B CB  
13997 C CG  . LEU B 730  ? 0.1679 0.2308 0.2008 0.0191  0.0368  -0.0114 728  LEU B CG  
13998 C CD1 . LEU B 730  ? 0.1966 0.2566 0.2221 0.0212  0.0369  -0.0133 728  LEU B CD1 
13999 C CD2 . LEU B 730  ? 0.1959 0.2580 0.2290 0.0162  0.0362  -0.0087 728  LEU B CD2 
14000 N N   . ALA B 731  ? 0.1865 0.2358 0.2189 0.0212  0.0281  -0.0180 729  ALA B N   
14001 C CA  . ALA B 731  ? 0.1585 0.2054 0.1931 0.0213  0.0260  -0.0190 729  ALA B CA  
14002 C C   . ALA B 731  ? 0.1994 0.2490 0.2372 0.0238  0.0268  -0.0203 729  ALA B C   
14003 O O   . ALA B 731  ? 0.2086 0.2574 0.2432 0.0265  0.0274  -0.0221 729  ALA B O   
14004 C CB  . ALA B 731  ? 0.1935 0.2344 0.2227 0.0213  0.0235  -0.0205 729  ALA B CB  
14005 N N   . LYS B 732  ? 0.1670 0.2198 0.2109 0.0230  0.0268  -0.0194 730  LYS B N   
14006 C CA  . LYS B 732  ? 0.1597 0.2159 0.2076 0.0252  0.0274  -0.0203 730  LYS B CA  
14007 C C   . LYS B 732  ? 0.1997 0.2527 0.2490 0.0251  0.0246  -0.0213 730  LYS B C   
14008 O O   . LYS B 732  ? 0.1956 0.2495 0.2490 0.0231  0.0237  -0.0201 730  LYS B O   
14009 C CB  . LYS B 732  ? 0.1754 0.2383 0.2295 0.0241  0.0294  -0.0183 730  LYS B CB  
14010 C CG  . LYS B 732  ? 0.2065 0.2751 0.2634 0.0270  0.0315  -0.0190 730  LYS B CG  
14011 C CD  . LYS B 732  ? 0.2563 0.3242 0.3155 0.0290  0.0298  -0.0207 730  LYS B CD  
14012 C CE  . LYS B 732  ? 0.2251 0.2952 0.2905 0.0269  0.0284  -0.0195 730  LYS B CE  
14013 N NZ  . LYS B 732  ? 0.2059 0.2752 0.2730 0.0291  0.0266  -0.0211 730  LYS B NZ  
14014 N N   . PRO B 733  ? 0.2180 0.2668 0.2638 0.0273  0.0232  -0.0233 731  PRO B N   
14015 C CA  . PRO B 733  ? 0.2251 0.2705 0.2717 0.0271  0.0205  -0.0241 731  PRO B CA  
14016 C C   . PRO B 733  ? 0.2032 0.2528 0.2555 0.0287  0.0206  -0.0243 731  PRO B C   
14017 O O   . PRO B 733  ? 0.1982 0.2529 0.2531 0.0307  0.0227  -0.0244 731  PRO B O   
14018 C CB  . PRO B 733  ? 0.1972 0.2365 0.2374 0.0289  0.0190  -0.0261 731  PRO B CB  
14019 C CG  . PRO B 733  ? 0.2144 0.2558 0.2525 0.0318  0.0213  -0.0271 731  PRO B CG  
14020 C CD  . PRO B 733  ? 0.2006 0.2473 0.2410 0.0301  0.0239  -0.0251 731  PRO B CD  
14021 N N   . ALA B 734  ? 0.2059 0.2536 0.2601 0.0278  0.0183  -0.0244 732  ALA B N   
14022 C CA  . ALA B 734  ? 0.2074 0.2584 0.2667 0.0293  0.0178  -0.0247 732  ALA B CA  
14023 C C   . ALA B 734  ? 0.2168 0.2680 0.2747 0.0334  0.0183  -0.0265 732  ALA B C   
14024 O O   . ALA B 734  ? 0.2163 0.2622 0.2683 0.0350  0.0176  -0.0279 732  ALA B O   
14025 C CB  . ALA B 734  ? 0.1981 0.2456 0.2579 0.0281  0.0149  -0.0248 732  ALA B CB  
14026 N N   . GLU B 735  ? 0.1881 0.2456 0.2516 0.0352  0.0193  -0.0263 733  GLU B N   
14027 C CA  . GLU B 735  ? 0.1829 0.2416 0.2458 0.0396  0.0200  -0.0280 733  GLU B CA  
14028 C C   . GLU B 735  ? 0.2261 0.2777 0.2851 0.0415  0.0170  -0.0298 733  GLU B C   
14029 O O   . GLU B 735  ? 0.1986 0.2470 0.2533 0.0450  0.0170  -0.0317 733  GLU B O   
14030 C CB  . GLU B 735  ? 0.2382 0.3056 0.3088 0.0409  0.0213  -0.0273 733  GLU B CB  
14031 C CG  . GLU B 735  ? 0.2971 0.3670 0.3678 0.0459  0.0223  -0.0289 733  GLU B CG  
14032 C CD  . GLU B 735  ? 0.3745 0.4542 0.4534 0.0472  0.0236  -0.0280 733  GLU B CD  
14033 O OE1 . GLU B 735  ? 0.4012 0.4857 0.4857 0.0437  0.0238  -0.0259 733  GLU B OE1 
14034 O OE2 . GLU B 735  ? 0.3950 0.4777 0.4748 0.0516  0.0245  -0.0293 733  GLU B OE2 
14035 N N   . GLU B 736  ? 0.2250 0.2737 0.2850 0.0394  0.0143  -0.0293 734  GLU B N   
14036 C CA  . GLU B 736  ? 0.2322 0.2745 0.2889 0.0408  0.0113  -0.0306 734  GLU B CA  
14037 C C   . GLU B 736  ? 0.2385 0.2724 0.2872 0.0401  0.0100  -0.0314 734  GLU B C   
14038 O O   . GLU B 736  ? 0.2185 0.2464 0.2632 0.0421  0.0079  -0.0328 734  GLU B O   
14039 C CB  . GLU B 736  ? 0.2349 0.2771 0.2949 0.0385  0.0090  -0.0295 734  GLU B CB  
14040 C CG  . GLU B 736  ? 0.2626 0.3127 0.3305 0.0390  0.0096  -0.0287 734  GLU B CG  
14041 C CD  . GLU B 736  ? 0.3223 0.3781 0.3946 0.0358  0.0116  -0.0269 734  GLU B CD  
14042 O OE1 . GLU B 736  ? 0.2697 0.3244 0.3393 0.0339  0.0131  -0.0263 734  GLU B OE1 
14043 O OE2 . GLU B 736  ? 0.3730 0.4344 0.4515 0.0351  0.0115  -0.0259 734  GLU B OE2 
14044 N N   . THR B 737  ? 0.1864 0.2194 0.2327 0.0372  0.0110  -0.0306 735  THR B N   
14045 C CA  . THR B 737  ? 0.2229 0.2483 0.2624 0.0356  0.0093  -0.0310 735  THR B CA  
14046 C C   . THR B 737  ? 0.2165 0.2414 0.2519 0.0353  0.0111  -0.0312 735  THR B C   
14047 O O   . THR B 737  ? 0.2113 0.2345 0.2445 0.0322  0.0109  -0.0302 735  THR B O   
14048 C CB  . THR B 737  ? 0.2102 0.2344 0.2505 0.0317  0.0077  -0.0295 735  THR B CB  
14049 O OG1 . THR B 737  ? 0.1980 0.2278 0.2425 0.0295  0.0097  -0.0279 735  THR B OG1 
14050 C CG2 . THR B 737  ? 0.2394 0.2627 0.2822 0.0320  0.0055  -0.0295 735  THR B CG2 
14051 N N   . PRO B 738  ? 0.2303 0.2565 0.2643 0.0386  0.0129  -0.0325 736  PRO B N   
14052 C CA  . PRO B 738  ? 0.2017 0.2276 0.2317 0.0383  0.0147  -0.0326 736  PRO B CA  
14053 C C   . PRO B 738  ? 0.2076 0.2251 0.2295 0.0378  0.0126  -0.0337 736  PRO B C   
14054 O O   . PRO B 738  ? 0.2103 0.2269 0.2287 0.0361  0.0133  -0.0333 736  PRO B O   
14055 C CB  . PRO B 738  ? 0.1828 0.2131 0.2139 0.0424  0.0173  -0.0337 736  PRO B CB  
14056 C CG  . PRO B 738  ? 0.2032 0.2312 0.2346 0.0456  0.0156  -0.0353 736  PRO B CG  
14057 C CD  . PRO B 738  ? 0.2109 0.2387 0.2465 0.0430  0.0133  -0.0340 736  PRO B CD  
14058 N N   . LEU B 739  ? 0.2066 0.2177 0.2253 0.0390  0.0099  -0.0350 737  LEU B N   
14059 C CA  . LEU B 739  ? 0.2193 0.2221 0.2299 0.0387  0.0079  -0.0362 737  LEU B CA  
14060 C C   . LEU B 739  ? 0.2265 0.2271 0.2352 0.0339  0.0065  -0.0346 737  LEU B C   
14061 O O   . LEU B 739  ? 0.2177 0.2151 0.2212 0.0327  0.0062  -0.0349 737  LEU B O   
14062 C CB  . LEU B 739  ? 0.2264 0.2225 0.2339 0.0409  0.0051  -0.0378 737  LEU B CB  
14063 C CG  . LEU B 739  ? 0.2096 0.2080 0.2191 0.0461  0.0063  -0.0395 737  LEU B CG  
14064 C CD1 . LEU B 739  ? 0.2114 0.2024 0.2176 0.0483  0.0032  -0.0408 737  LEU B CD1 
14065 C CD2 . LEU B 739  ? 0.2540 0.2534 0.2601 0.0490  0.0088  -0.0410 737  LEU B CD2 
14066 N N   . ILE B 740  ? 0.2022 0.2044 0.2150 0.0314  0.0054  -0.0330 738  ILE B N   
14067 C CA  . ILE B 740  ? 0.2113 0.2121 0.2226 0.0272  0.0042  -0.0315 738  ILE B CA  
14068 C C   . ILE B 740  ? 0.2224 0.2283 0.2354 0.0257  0.0066  -0.0303 738  ILE B C   
14069 O O   . ILE B 740  ? 0.2016 0.2058 0.2113 0.0232  0.0060  -0.0295 738  ILE B O   
14070 C CB  . ILE B 740  ? 0.2388 0.2400 0.2534 0.0250  0.0026  -0.0302 738  ILE B CB  
14071 C CG1 . ILE B 740  ? 0.2040 0.2035 0.2164 0.0210  0.0012  -0.0287 738  ILE B CG1 
14072 C CG2 . ILE B 740  ? 0.2323 0.2407 0.2542 0.0252  0.0045  -0.0292 738  ILE B CG2 
14073 C CD1 . ILE B 740  ? 0.2304 0.2226 0.2358 0.0200  -0.0012 -0.0294 738  ILE B CD1 
14074 N N   . ALA B 741  ? 0.2170 0.2293 0.2350 0.0272  0.0093  -0.0299 739  ALA B N   
14075 C CA  . ALA B 741  ? 0.2081 0.2248 0.2272 0.0260  0.0116  -0.0287 739  ALA B CA  
14076 C C   . ALA B 741  ? 0.1928 0.2067 0.2057 0.0269  0.0120  -0.0298 739  ALA B C   
14077 O O   . ALA B 741  ? 0.2263 0.2402 0.2370 0.0247  0.0122  -0.0288 739  ALA B O   
14078 C CB  . ALA B 741  ? 0.2109 0.2346 0.2361 0.0275  0.0142  -0.0282 739  ALA B CB  
14079 N N   . ALA B 742  ? 0.1941 0.2056 0.2040 0.0303  0.0123  -0.0319 740  ALA B N   
14080 C CA  . ALA B 742  ? 0.2136 0.2214 0.2166 0.0314  0.0125  -0.0332 740  ALA B CA  
14081 C C   . ALA B 742  ? 0.2302 0.2316 0.2276 0.0285  0.0095  -0.0331 740  ALA B C   
14082 O O   . ALA B 742  ? 0.2241 0.2245 0.2175 0.0271  0.0097  -0.0329 740  ALA B O   
14083 C CB  . ALA B 742  ? 0.2014 0.2066 0.2016 0.0359  0.0127  -0.0358 740  ALA B CB  
14084 N N   . GLU B 743  ? 0.2091 0.2063 0.2062 0.0273  0.0068  -0.0331 741  GLU B N   
14085 C CA  . GLU B 743  ? 0.2134 0.2051 0.2056 0.0240  0.0039  -0.0327 741  GLU B CA  
14086 C C   . GLU B 743  ? 0.2075 0.2035 0.2023 0.0204  0.0044  -0.0303 741  GLU B C   
14087 O O   . GLU B 743  ? 0.2078 0.2015 0.1983 0.0182  0.0032  -0.0299 741  GLU B O   
14088 C CB  . GLU B 743  ? 0.2570 0.2439 0.2488 0.0233  0.0011  -0.0328 741  GLU B CB  
14089 C CG  . GLU B 743  ? 0.2870 0.2687 0.2740 0.0195  -0.0019 -0.0321 741  GLU B CG  
14090 C CD  . GLU B 743  ? 0.2985 0.2727 0.2773 0.0200  -0.0037 -0.0338 741  GLU B CD  
14091 O OE1 . GLU B 743  ? 0.2837 0.2562 0.2600 0.0238  -0.0026 -0.0359 741  GLU B OE1 
14092 O OE2 . GLU B 743  ? 0.3082 0.2784 0.2831 0.0166  -0.0063 -0.0331 741  GLU B OE2 
14093 N N   . GLY B 744  ? 0.2312 0.2333 0.2327 0.0198  0.0059  -0.0288 742  GLY B N   
14094 C CA  . GLY B 744  ? 0.2129 0.2192 0.2169 0.0170  0.0066  -0.0266 742  GLY B CA  
14095 C C   . GLY B 744  ? 0.2274 0.2354 0.2290 0.0172  0.0082  -0.0264 742  GLY B C   
14096 O O   . GLY B 744  ? 0.1873 0.1955 0.1871 0.0148  0.0075  -0.0252 742  GLY B O   
14097 N N   . VAL B 745  ? 0.1859 0.1956 0.1875 0.0201  0.0105  -0.0275 743  VAL B N   
14098 C CA  . VAL B 745  ? 0.2024 0.2139 0.2014 0.0204  0.0122  -0.0273 743  VAL B CA  
14099 C C   . VAL B 745  ? 0.2202 0.2258 0.2113 0.0200  0.0103  -0.0285 743  VAL B C   
14100 O O   . VAL B 745  ? 0.2007 0.2068 0.1892 0.0183  0.0102  -0.0276 743  VAL B O   
14101 C CB  . VAL B 745  ? 0.2282 0.2437 0.2294 0.0236  0.0153  -0.0279 743  VAL B CB  
14102 C CG1 . VAL B 745  ? 0.1995 0.2160 0.1965 0.0241  0.0170  -0.0280 743  VAL B CG1 
14103 C CG2 . VAL B 745  ? 0.2114 0.2332 0.2204 0.0231  0.0170  -0.0262 743  VAL B CG2 
14104 N N   . ARG B 746  ? 0.1882 0.1877 0.1752 0.0214  0.0085  -0.0306 744  ARG B N   
14105 C CA  . ARG B 746  ? 0.2230 0.2158 0.2020 0.0206  0.0060  -0.0318 744  ARG B CA  
14106 C C   . ARG B 746  ? 0.2251 0.2173 0.2035 0.0162  0.0038  -0.0300 744  ARG B C   
14107 O O   . ARG B 746  ? 0.2205 0.2111 0.1943 0.0147  0.0028  -0.0298 744  ARG B O   
14108 C CB  . ARG B 746  ? 0.2551 0.2406 0.2302 0.0222  0.0038  -0.0340 744  ARG B CB  
14109 C CG  . ARG B 746  ? 0.2836 0.2685 0.2579 0.0269  0.0056  -0.0363 744  ARG B CG  
14110 C CD  . ARG B 746  ? 0.2763 0.2531 0.2464 0.0283  0.0028  -0.0383 744  ARG B CD  
14111 N NE  . ARG B 746  ? 0.3138 0.2912 0.2846 0.0333  0.0047  -0.0403 744  ARG B NE  
14112 C CZ  . ARG B 746  ? 0.2741 0.2538 0.2501 0.0352  0.0051  -0.0403 744  ARG B CZ  
14113 N NH1 . ARG B 746  ? 0.2516 0.2310 0.2312 0.0328  0.0032  -0.0389 744  ARG B NH1 
14114 N NH2 . ARG B 746  ? 0.2631 0.2456 0.2407 0.0398  0.0074  -0.0418 744  ARG B NH2 
14115 N N   . ILE B 747  ? 0.2179 0.2118 0.2010 0.0143  0.0028  -0.0285 745  ILE B N   
14116 C CA  . ILE B 747  ? 0.2145 0.2084 0.1972 0.0103  0.0006  -0.0267 745  ILE B CA  
14117 C C   . ILE B 747  ? 0.2171 0.2168 0.2023 0.0090  0.0021  -0.0247 745  ILE B C   
14118 O O   . ILE B 747  ? 0.2208 0.2200 0.2031 0.0065  0.0006  -0.0238 745  ILE B O   
14119 C CB  . ILE B 747  ? 0.2062 0.2006 0.1931 0.0089  -0.0005 -0.0257 745  ILE B CB  
14120 C CG1 . ILE B 747  ? 0.2615 0.2486 0.2443 0.0095  -0.0029 -0.0274 745  ILE B CG1 
14121 C CG2 . ILE B 747  ? 0.2139 0.2113 0.2025 0.0052  -0.0017 -0.0234 745  ILE B CG2 
14122 C CD1 . ILE B 747  ? 0.2668 0.2540 0.2531 0.0085  -0.0040 -0.0266 745  ILE B CD1 
14123 N N   . LEU B 748  ? 0.2063 0.2116 0.1970 0.0105  0.0049  -0.0240 746  LEU B N   
14124 C CA  . LEU B 748  ? 0.1809 0.1912 0.1737 0.0095  0.0063  -0.0220 746  LEU B CA  
14125 C C   . LEU B 748  ? 0.1860 0.1952 0.1734 0.0100  0.0067  -0.0226 746  LEU B C   
14126 O O   . LEU B 748  ? 0.1879 0.1986 0.1741 0.0081  0.0061  -0.0211 746  LEU B O   
14127 C CB  . LEU B 748  ? 0.1967 0.2123 0.1959 0.0109  0.0091  -0.0211 746  LEU B CB  
14128 C CG  . LEU B 748  ? 0.2227 0.2408 0.2274 0.0095  0.0086  -0.0198 746  LEU B CG  
14129 C CD1 . LEU B 748  ? 0.2463 0.2678 0.2566 0.0113  0.0109  -0.0197 746  LEU B CD1 
14130 C CD2 . LEU B 748  ? 0.2609 0.2820 0.2669 0.0074  0.0082  -0.0176 746  LEU B CD2 
14131 N N   . ARG B 749  ? 0.1962 0.2027 0.1802 0.0127  0.0078  -0.0247 747  ARG B N   
14132 C CA  . ARG B 749  ? 0.2043 0.2090 0.1821 0.0133  0.0080  -0.0254 747  ARG B CA  
14133 C C   . ARG B 749  ? 0.2109 0.2102 0.1825 0.0109  0.0045  -0.0259 747  ARG B C   
14134 O O   . ARG B 749  ? 0.2163 0.2158 0.1844 0.0095  0.0039  -0.0252 747  ARG B O   
14135 C CB  . ARG B 749  ? 0.1840 0.1869 0.1591 0.0170  0.0099  -0.0278 747  ARG B CB  
14136 C CG  . ARG B 749  ? 0.1982 0.2075 0.1790 0.0191  0.0135  -0.0270 747  ARG B CG  
14137 C CD  . ARG B 749  ? 0.2093 0.2178 0.1867 0.0228  0.0156  -0.0292 747  ARG B CD  
14138 N NE  . ARG B 749  ? 0.2476 0.2628 0.2300 0.0245  0.0192  -0.0282 747  ARG B NE  
14139 C CZ  . ARG B 749  ? 0.2647 0.2813 0.2452 0.0277  0.0217  -0.0297 747  ARG B CZ  
14140 N NH1 . ARG B 749  ? 0.2749 0.2862 0.2483 0.0300  0.0210  -0.0323 747  ARG B NH1 
14141 N NH2 . ARG B 749  ? 0.2314 0.2548 0.2171 0.0287  0.0249  -0.0283 747  ARG B NH2 
14142 N N   . GLU B 750  ? 0.2150 0.2092 0.1849 0.0103  0.0021  -0.0270 748  GLU B N   
14143 C CA  . GLU B 750  ? 0.2306 0.2194 0.1946 0.0075  -0.0015 -0.0273 748  GLU B CA  
14144 C C   . GLU B 750  ? 0.2037 0.1966 0.1703 0.0038  -0.0027 -0.0245 748  GLU B C   
14145 O O   . GLU B 750  ? 0.2341 0.2252 0.1962 0.0015  -0.0049 -0.0241 748  GLU B O   
14146 C CB  . GLU B 750  ? 0.2210 0.2038 0.1834 0.0071  -0.0040 -0.0285 748  GLU B CB  
14147 C CG  . GLU B 750  ? 0.2496 0.2262 0.2057 0.0037  -0.0080 -0.0287 748  GLU B CG  
14148 C CD  . GLU B 750  ? 0.3009 0.2709 0.2550 0.0033  -0.0105 -0.0297 748  GLU B CD  
14149 O OE1 . GLU B 750  ? 0.2988 0.2683 0.2553 0.0062  -0.0091 -0.0308 748  GLU B OE1 
14150 O OE2 . GLU B 750  ? 0.3411 0.3065 0.2911 -0.0001 -0.0140 -0.0293 748  GLU B OE2 
14151 N N   . ALA B 751  ? 0.2235 0.2223 0.1975 0.0033  -0.0014 -0.0226 749  ALA B N   
14152 C CA  . ALA B 751  ? 0.2138 0.2173 0.1912 0.0005  -0.0022 -0.0200 749  ALA B CA  
14153 C C   . ALA B 751  ? 0.2149 0.2226 0.1924 0.0007  -0.0008 -0.0187 749  ALA B C   
14154 O O   . ALA B 751  ? 0.2340 0.2456 0.2138 -0.0014 -0.0016 -0.0165 749  ALA B O   
14155 C CB  . ALA B 751  ? 0.2479 0.2557 0.2325 0.0005  -0.0010 -0.0188 749  ALA B CB  
14156 N N   . GLY B 752  ? 0.2084 0.2156 0.1836 0.0032  0.0013  -0.0198 750  GLY B N   
14157 C CA  . GLY B 752  ? 0.2175 0.2279 0.1916 0.0032  0.0024  -0.0186 750  GLY B CA  
14158 C C   . GLY B 752  ? 0.2037 0.2186 0.1820 0.0055  0.0060  -0.0178 750  GLY B C   
14159 O O   . GLY B 752  ? 0.2156 0.2328 0.1926 0.0056  0.0070  -0.0166 750  GLY B O   
14160 N N   . ILE B 753  ? 0.2377 0.2539 0.2207 0.0071  0.0078  -0.0182 751  ILE B N   
14161 C CA  . ILE B 753  ? 0.2180 0.2383 0.2048 0.0090  0.0110  -0.0175 751  ILE B CA  
14162 C C   . ILE B 753  ? 0.2331 0.2516 0.2148 0.0112  0.0126  -0.0192 751  ILE B C   
14163 O O   . ILE B 753  ? 0.2121 0.2269 0.1910 0.0129  0.0124  -0.0216 751  ILE B O   
14164 C CB  . ILE B 753  ? 0.1917 0.2137 0.1846 0.0100  0.0123  -0.0177 751  ILE B CB  
14165 C CG1 . ILE B 753  ? 0.2067 0.2300 0.2039 0.0080  0.0106  -0.0164 751  ILE B CG1 
14166 C CG2 . ILE B 753  ? 0.1878 0.2140 0.1844 0.0115  0.0154  -0.0168 751  ILE B CG2 
14167 C CD1 . ILE B 753  ? 0.1893 0.2167 0.1893 0.0068  0.0110  -0.0138 751  ILE B CD1 
14168 N N   . PRO B 754  ? 0.2106 0.2318 0.1909 0.0115  0.0143  -0.0180 752  PRO B N   
14169 C CA  . PRO B 754  ? 0.2352 0.2552 0.2104 0.0138  0.0161  -0.0196 752  PRO B CA  
14170 C C   . PRO B 754  ? 0.2472 0.2688 0.2257 0.0165  0.0187  -0.0208 752  PRO B C   
14171 O O   . PRO B 754  ? 0.2203 0.2455 0.2056 0.0164  0.0200  -0.0196 752  PRO B O   
14172 C CB  . PRO B 754  ? 0.2607 0.2843 0.2354 0.0132  0.0176  -0.0173 752  PRO B CB  
14173 C CG  . PRO B 754  ? 0.2945 0.3199 0.2726 0.0106  0.0158  -0.0149 752  PRO B CG  
14174 C CD  . PRO B 754  ? 0.2328 0.2580 0.2160 0.0100  0.0146  -0.0152 752  PRO B CD  
14175 N N   . ALA B 755  ? 0.2405 0.2595 0.2140 0.0190  0.0196  -0.0232 753  ALA B N   
14176 C CA  . ALA B 755  ? 0.2566 0.2777 0.2330 0.0220  0.0221  -0.0245 753  ALA B CA  
14177 C C   . ALA B 755  ? 0.2778 0.3057 0.2594 0.0222  0.0255  -0.0223 753  ALA B C   
14178 O O   . ALA B 755  ? 0.2698 0.3011 0.2573 0.0233  0.0271  -0.0221 753  ALA B O   
14179 C CB  . ALA B 755  ? 0.2901 0.3074 0.2594 0.0250  0.0227  -0.0274 753  ALA B CB  
14180 N N   . SER B 756  ? 0.2569 0.2869 0.2366 0.0210  0.0264  -0.0204 754  SER B N   
14181 C CA  . SER B 756  ? 0.2289 0.2650 0.2133 0.0208  0.0293  -0.0180 754  SER B CA  
14182 C C   . SER B 756  ? 0.2467 0.2851 0.2385 0.0186  0.0286  -0.0158 754  SER B C   
14183 O O   . SER B 756  ? 0.2472 0.2901 0.2441 0.0185  0.0308  -0.0141 754  SER B O   
14184 C CB  . SER B 756  ? 0.2669 0.3040 0.2466 0.0200  0.0302  -0.0164 754  SER B CB  
14185 O OG  . SER B 756  ? 0.3216 0.3566 0.3001 0.0174  0.0274  -0.0150 754  SER B OG  
14186 N N   . ALA B 757  ? 0.2108 0.2462 0.2030 0.0169  0.0257  -0.0157 755  ALA B N   
14187 C CA  . ALA B 757  ? 0.2014 0.2387 0.2000 0.0152  0.0249  -0.0139 755  ALA B CA  
14188 C C   . ALA B 757  ? 0.2069 0.2439 0.2102 0.0159  0.0245  -0.0152 755  ALA B C   
14189 O O   . ALA B 757  ? 0.2026 0.2415 0.2115 0.0148  0.0244  -0.0139 755  ALA B O   
14190 C CB  . ALA B 757  ? 0.2182 0.2534 0.2154 0.0130  0.0221  -0.0129 755  ALA B CB  
14191 N N   . LEU B 758  ? 0.1935 0.2280 0.1944 0.0177  0.0242  -0.0177 756  LEU B N   
14192 C CA  . LEU B 758  ? 0.2109 0.2449 0.2160 0.0185  0.0236  -0.0189 756  LEU B CA  
14193 C C   . LEU B 758  ? 0.2406 0.2745 0.2441 0.0216  0.0251  -0.0211 756  LEU B C   
14194 O O   . LEU B 758  ? 0.2151 0.2446 0.2129 0.0229  0.0240  -0.0233 756  LEU B O   
14195 C CB  . LEU B 758  ? 0.1840 0.2135 0.1876 0.0171  0.0204  -0.0197 756  LEU B CB  
14196 C CG  . LEU B 758  ? 0.2011 0.2296 0.2081 0.0181  0.0196  -0.0210 756  LEU B CG  
14197 C CD1 . LEU B 758  ? 0.2048 0.2378 0.2191 0.0176  0.0208  -0.0195 756  LEU B CD1 
14198 C CD2 . LEU B 758  ? 0.2023 0.2263 0.2073 0.0165  0.0164  -0.0215 756  LEU B CD2 
14199 N N   . GLN B 759  ? 0.1876 0.2264 0.1960 0.0227  0.0276  -0.0205 757  GLN B N   
14200 C CA  . GLN B 759  ? 0.1869 0.2269 0.1950 0.0260  0.0292  -0.0225 757  GLN B CA  
14201 C C   . GLN B 759  ? 0.2066 0.2475 0.2204 0.0267  0.0286  -0.0231 757  GLN B C   
14202 O O   . GLN B 759  ? 0.2175 0.2605 0.2368 0.0247  0.0281  -0.0214 757  GLN B O   
14203 C CB  . GLN B 759  ? 0.2047 0.2507 0.2141 0.0269  0.0328  -0.0213 757  GLN B CB  
14204 C CG  . GLN B 759  ? 0.1729 0.2177 0.1759 0.0265  0.0334  -0.0208 757  GLN B CG  
14205 C CD  . GLN B 759  ? 0.1894 0.2402 0.1936 0.0268  0.0369  -0.0191 757  GLN B CD  
14206 O OE1 . GLN B 759  ? 0.2082 0.2611 0.2101 0.0295  0.0392  -0.0203 757  GLN B OE1 
14207 N NE2 . GLN B 759  ? 0.2027 0.2565 0.2106 0.0241  0.0374  -0.0161 757  GLN B NE2 
14208 N N   . LEU B 760  ? 0.1985 0.2373 0.2106 0.0296  0.0283  -0.0255 758  LEU B N   
14209 C CA  . LEU B 760  ? 0.1979 0.2373 0.2149 0.0307  0.0274  -0.0262 758  LEU B CA  
14210 C C   . LEU B 760  ? 0.1791 0.2242 0.1996 0.0336  0.0303  -0.0266 758  LEU B C   
14211 O O   . LEU B 760  ? 0.2139 0.2590 0.2304 0.0366  0.0318  -0.0282 758  LEU B O   
14212 C CB  . LEU B 760  ? 0.1968 0.2290 0.2093 0.0319  0.0246  -0.0286 758  LEU B CB  
14213 C CG  . LEU B 760  ? 0.2072 0.2394 0.2242 0.0330  0.0234  -0.0293 758  LEU B CG  
14214 C CD1 . LEU B 760  ? 0.1856 0.2178 0.2066 0.0296  0.0216  -0.0275 758  LEU B CD1 
14215 C CD2 . LEU B 760  ? 0.2188 0.2442 0.2305 0.0354  0.0212  -0.0319 758  LEU B CD2 
14216 N N   . LEU B 761  ? 0.1974 0.2477 0.2253 0.0329  0.0309  -0.0253 759  LEU B N   
14217 C CA  . LEU B 761  ? 0.1887 0.2458 0.2212 0.0353  0.0335  -0.0253 759  LEU B CA  
14218 C C   . LEU B 761  ? 0.1813 0.2388 0.2188 0.0363  0.0320  -0.0260 759  LEU B C   
14219 O O   . LEU B 761  ? 0.2164 0.2776 0.2602 0.0343  0.0317  -0.0243 759  LEU B O   
14220 C CB  . LEU B 761  ? 0.1788 0.2428 0.2161 0.0331  0.0360  -0.0224 759  LEU B CB  
14221 C CG  . LEU B 761  ? 0.2122 0.2768 0.2455 0.0317  0.0377  -0.0210 759  LEU B CG  
14222 C CD1 . LEU B 761  ? 0.2543 0.3173 0.2808 0.0350  0.0391  -0.0231 759  LEU B CD1 
14223 C CD2 . LEU B 761  ? 0.1864 0.2460 0.2173 0.0284  0.0355  -0.0200 759  LEU B CD2 
14224 N N   . PRO B 762  ? 0.2101 0.2636 0.2446 0.0395  0.0307  -0.0285 760  PRO B N   
14225 C CA  . PRO B 762  ? 0.2175 0.2717 0.2566 0.0409  0.0292  -0.0291 760  PRO B CA  
14226 C C   . PRO B 762  ? 0.2188 0.2820 0.2650 0.0424  0.0316  -0.0283 760  PRO B C   
14227 O O   . PRO B 762  ? 0.2186 0.2869 0.2648 0.0440  0.0347  -0.0281 760  PRO B O   
14228 C CB  . PRO B 762  ? 0.2101 0.2578 0.2432 0.0445  0.0276  -0.0321 760  PRO B CB  
14229 C CG  . PRO B 762  ? 0.2161 0.2581 0.2413 0.0437  0.0273  -0.0328 760  PRO B CG  
14230 C CD  . PRO B 762  ? 0.2058 0.2537 0.2323 0.0420  0.0303  -0.0308 760  PRO B CD  
14231 N N   . GLY B 763  ? 0.2285 0.2939 0.2807 0.0418  0.0302  -0.0277 761  GLY B N   
14232 C CA  . GLY B 763  ? 0.2197 0.2937 0.2790 0.0433  0.0320  -0.0270 761  GLY B CA  
14233 C C   . GLY B 763  ? 0.2336 0.3103 0.2997 0.0403  0.0305  -0.0252 761  GLY B C   
14234 O O   . GLY B 763  ? 0.2413 0.3127 0.3063 0.0377  0.0279  -0.0250 761  GLY B O   
14235 N N   . ASP B 764  ? 0.2716 0.3570 0.3446 0.0405  0.0322  -0.0239 762  ASP B N   
14236 C CA  . ASP B 764  ? 0.2369 0.3252 0.3166 0.0379  0.0306  -0.0224 762  ASP B CA  
14237 C C   . ASP B 764  ? 0.2840 0.3750 0.3662 0.0334  0.0317  -0.0197 762  ASP B C   
14238 O O   . ASP B 764  ? 0.2574 0.3464 0.3355 0.0320  0.0330  -0.0191 762  ASP B O   
14239 C CB  . ASP B 764  ? 0.2707 0.3667 0.3568 0.0407  0.0313  -0.0226 762  ASP B CB  
14240 C CG  . ASP B 764  ? 0.3421 0.4473 0.4314 0.0418  0.0352  -0.0215 762  ASP B CG  
14241 O OD1 . ASP B 764  ? 0.3221 0.4279 0.4092 0.0397  0.0372  -0.0202 762  ASP B OD1 
14242 O OD2 . ASP B 764  ? 0.3774 0.4896 0.4714 0.0448  0.0362  -0.0218 762  ASP B OD2 
14243 N N   . GLY B 765  ? 0.2780 0.3734 0.3669 0.0310  0.0309  -0.0181 763  GLY B N   
14244 C CA  . GLY B 765  ? 0.3230 0.4200 0.4141 0.0266  0.0315  -0.0155 763  GLY B CA  
14245 C C   . GLY B 765  ? 0.2740 0.3774 0.3663 0.0261  0.0350  -0.0138 763  GLY B C   
14246 O O   . GLY B 765  ? 0.3118 0.4144 0.4034 0.0228  0.0356  -0.0118 763  GLY B O   
14247 N N   . ARG B 766  ? 0.2625 0.3721 0.3563 0.0294  0.0373  -0.0144 764  ARG B N   
14248 C CA  . ARG B 766  ? 0.2784 0.3943 0.3727 0.0292  0.0410  -0.0128 764  ARG B CA  
14249 C C   . ARG B 766  ? 0.2933 0.4035 0.3796 0.0292  0.0420  -0.0132 764  ARG B C   
14250 O O   . ARG B 766  ? 0.2405 0.3530 0.3262 0.0270  0.0440  -0.0111 764  ARG B O   
14251 C CB  . ARG B 766  ? 0.3324 0.4561 0.4294 0.0335  0.0434  -0.0137 764  ARG B CB  
14252 N N   . VAL B 767  ? 0.2765 0.3791 0.3567 0.0316  0.0404  -0.0158 765  VAL B N   
14253 C CA  . VAL B 767  ? 0.2300 0.3267 0.3026 0.0313  0.0408  -0.0162 765  VAL B CA  
14254 C C   . VAL B 767  ? 0.2463 0.3391 0.3184 0.0269  0.0393  -0.0143 765  VAL B C   
14255 O O   . VAL B 767  ? 0.2388 0.3312 0.3080 0.0252  0.0407  -0.0128 765  VAL B O   
14256 C CB  . VAL B 767  ? 0.2233 0.3127 0.2896 0.0345  0.0390  -0.0193 765  VAL B CB  
14257 C CG1 . VAL B 767  ? 0.2165 0.3001 0.2750 0.0338  0.0392  -0.0197 765  VAL B CG1 
14258 C CG2 . VAL B 767  ? 0.2120 0.3049 0.2785 0.0394  0.0405  -0.0213 765  VAL B CG2 
14259 N N   . GLY B 768  ? 0.2034 0.2930 0.2780 0.0252  0.0364  -0.0144 766  GLY B N   
14260 C CA  . GLY B 768  ? 0.2465 0.3325 0.3208 0.0213  0.0351  -0.0127 766  GLY B CA  
14261 C C   . GLY B 768  ? 0.2040 0.2953 0.2823 0.0184  0.0369  -0.0097 766  GLY B C   
14262 O O   . GLY B 768  ? 0.1979 0.2869 0.2737 0.0161  0.0371  -0.0081 766  GLY B O   
14263 N N   . ALA B 769  ? 0.2418 0.3403 0.3262 0.0184  0.0380  -0.0088 767  ALA B N   
14264 C CA  . ALA B 769  ? 0.2296 0.3336 0.3182 0.0152  0.0396  -0.0057 767  ALA B CA  
14265 C C   . ALA B 769  ? 0.2505 0.3566 0.3354 0.0154  0.0427  -0.0044 767  ALA B C   
14266 O O   . ALA B 769  ? 0.2046 0.3104 0.2892 0.0122  0.0432  -0.0019 767  ALA B O   
14267 C CB  . ALA B 769  ? 0.2613 0.3734 0.3574 0.0154  0.0403  -0.0050 767  ALA B CB  
14268 N N   . ALA B 770  ? 0.1953 0.3033 0.2772 0.0191  0.0446  -0.0062 768  ALA B N   
14269 C CA  . ALA B 770  ? 0.2246 0.3343 0.3021 0.0196  0.0476  -0.0053 768  ALA B CA  
14270 C C   . ALA B 770  ? 0.2379 0.3399 0.3089 0.0180  0.0464  -0.0050 768  ALA B C   
14271 O O   . ALA B 770  ? 0.2028 0.3058 0.2717 0.0162  0.0480  -0.0029 768  ALA B O   
14272 C CB  . ALA B 770  ? 0.2424 0.3544 0.3169 0.0244  0.0495  -0.0078 768  ALA B CB  
14273 N N   . LEU B 771  ? 0.1990 0.2937 0.2668 0.0187  0.0435  -0.0071 769  LEU B N   
14274 C CA  . LEU B 771  ? 0.2008 0.2890 0.2631 0.0173  0.0423  -0.0067 769  LEU B CA  
14275 C C   . LEU B 771  ? 0.2295 0.3167 0.2944 0.0133  0.0414  -0.0040 769  LEU B C   
14276 O O   . LEU B 771  ? 0.2125 0.2983 0.2743 0.0117  0.0420  -0.0022 769  LEU B O   
14277 C CB  . LEU B 771  ? 0.2176 0.2989 0.2764 0.0187  0.0395  -0.0094 769  LEU B CB  
14278 C CG  . LEU B 771  ? 0.2105 0.2907 0.2652 0.0225  0.0400  -0.0122 769  LEU B CG  
14279 C CD1 . LEU B 771  ? 0.1922 0.2660 0.2450 0.0233  0.0368  -0.0144 769  LEU B CD1 
14280 C CD2 . LEU B 771  ? 0.2022 0.2810 0.2501 0.0233  0.0415  -0.0123 769  LEU B CD2 
14281 N N   . VAL B 772  ? 0.1889 0.2766 0.2592 0.0118  0.0397  -0.0036 770  VAL B N   
14282 C CA  . VAL B 772  ? 0.2074 0.2932 0.2799 0.0082  0.0384  -0.0013 770  VAL B CA  
14283 C C   . VAL B 772  ? 0.2240 0.3144 0.2980 0.0060  0.0408  0.0019  770  VAL B C   
14284 O O   . VAL B 772  ? 0.2069 0.2943 0.2791 0.0036  0.0404  0.0039  770  VAL B O   
14285 C CB  . VAL B 772  ? 0.2076 0.2935 0.2855 0.0072  0.0363  -0.0017 770  VAL B CB  
14286 C CG1 . VAL B 772  ? 0.2095 0.2946 0.2903 0.0035  0.0354  0.0009  770  VAL B CG1 
14287 C CG2 . VAL B 772  ? 0.2220 0.3019 0.2975 0.0087  0.0336  -0.0043 770  VAL B CG2 
14288 N N   . ALA B 773  ? 0.2343 0.3322 0.3116 0.0067  0.0433  0.0024  771  ALA B N   
14289 C CA  . ALA B 773  ? 0.2502 0.3536 0.3296 0.0043  0.0457  0.0056  771  ALA B CA  
14290 C C   . ALA B 773  ? 0.3181 0.4215 0.3916 0.0049  0.0480  0.0065  771  ALA B C   
14291 O O   . ALA B 773  ? 0.2773 0.3842 0.3515 0.0026  0.0498  0.0095  771  ALA B O   
14292 C CB  . ALA B 773  ? 0.2592 0.3716 0.3446 0.0050  0.0476  0.0059  771  ALA B CB  
14293 N N   . ALA B 774  ? 0.2518 0.3513 0.3194 0.0079  0.0478  0.0040  772  ALA B N   
14294 C CA  . ALA B 774  ? 0.2647 0.3643 0.3263 0.0088  0.0499  0.0045  772  ALA B CA  
14295 C C   . ALA B 774  ? 0.2516 0.3477 0.3108 0.0056  0.0493  0.0075  772  ALA B C   
14296 O O   . ALA B 774  ? 0.2387 0.3292 0.2982 0.0040  0.0466  0.0077  772  ALA B O   
14297 C CB  . ALA B 774  ? 0.2607 0.3555 0.3162 0.0121  0.0490  0.0012  772  ALA B CB  
14298 N N   . ALA B 775  ? 0.2706 0.3700 0.3272 0.0049  0.0520  0.0096  773  ALA B N   
14299 C CA  . ALA B 775  ? 0.3230 0.4199 0.3776 0.0018  0.0517  0.0129  773  ALA B CA  
14300 C C   . ALA B 775  ? 0.2864 0.3752 0.3361 0.0020  0.0490  0.0121  773  ALA B C   
14301 O O   . ALA B 775  ? 0.3105 0.3953 0.3606 -0.0005 0.0471  0.0141  773  ALA B O   
14302 C CB  . ALA B 775  ? 0.3340 0.4357 0.3853 0.0017  0.0551  0.0149  773  ALA B CB  
14303 N N   . GLU B 776  ? 0.2649 0.3511 0.3097 0.0049  0.0485  0.0093  774  GLU B N   
14304 C CA  . GLU B 776  ? 0.2544 0.3339 0.2943 0.0050  0.0462  0.0087  774  GLU B CA  
14305 C C   . GLU B 776  ? 0.2385 0.3134 0.2804 0.0054  0.0430  0.0068  774  GLU B C   
14306 O O   . GLU B 776  ? 0.2304 0.3003 0.2689 0.0055  0.0410  0.0063  774  GLU B O   
14307 C CB  . GLU B 776  ? 0.2684 0.3470 0.3014 0.0076  0.0469  0.0069  774  GLU B CB  
14308 C CG  . GLU B 776  ? 0.3079 0.3910 0.3377 0.0078  0.0502  0.0084  774  GLU B CG  
14309 C CD  . GLU B 776  ? 0.3816 0.4712 0.4138 0.0097  0.0531  0.0072  774  GLU B CD  
14310 O OE1 . GLU B 776  ? 0.3236 0.4147 0.3609 0.0107  0.0526  0.0055  774  GLU B OE1 
14311 O OE2 . GLU B 776  ? 0.4571 0.5506 0.4861 0.0105  0.0560  0.0080  774  GLU B OE2 
14312 N N   . THR B 777  ? 0.2273 0.3041 0.2747 0.0055  0.0426  0.0057  775  THR B N   
14313 C CA  . THR B 777  ? 0.2222 0.2947 0.2713 0.0057  0.0397  0.0039  775  THR B CA  
14314 C C   . THR B 777  ? 0.2428 0.3113 0.2926 0.0033  0.0378  0.0060  775  THR B C   
14315 O O   . THR B 777  ? 0.2028 0.2727 0.2557 0.0010  0.0383  0.0085  775  THR B O   
14316 C CB  . THR B 777  ? 0.2064 0.2819 0.2612 0.0062  0.0397  0.0027  775  THR B CB  
14317 O OG1 . THR B 777  ? 0.2092 0.2872 0.2625 0.0091  0.0410  0.0003  775  THR B OG1 
14318 C CG2 . THR B 777  ? 0.2057 0.2768 0.2625 0.0059  0.0367  0.0013  775  THR B CG2 
14319 N N   . ALA B 778  ? 0.2071 0.2707 0.2541 0.0040  0.0356  0.0049  776  ALA B N   
14320 C CA  . ALA B 778  ? 0.2431 0.3027 0.2896 0.0025  0.0339  0.0067  776  ALA B CA  
14321 C C   . ALA B 778  ? 0.2290 0.2854 0.2782 0.0025  0.0315  0.0053  776  ALA B C   
14322 O O   . ALA B 778  ? 0.2286 0.2816 0.2779 0.0016  0.0299  0.0065  776  ALA B O   
14323 C CB  . ALA B 778  ? 0.2410 0.2980 0.2819 0.0032  0.0333  0.0070  776  ALA B CB  
14324 N N   . GLY B 779  ? 0.2152 0.2725 0.2664 0.0037  0.0311  0.0029  777  GLY B N   
14325 C CA  . GLY B 779  ? 0.2083 0.2630 0.2618 0.0037  0.0289  0.0016  777  GLY B CA  
14326 C C   . GLY B 779  ? 0.1913 0.2478 0.2465 0.0051  0.0289  -0.0009 777  GLY B C   
14327 O O   . GLY B 779  ? 0.1970 0.2556 0.2504 0.0066  0.0302  -0.0020 777  GLY B O   
14328 N N   . VAL B 780  ? 0.1632 0.2187 0.2218 0.0048  0.0274  -0.0017 778  VAL B N   
14329 C CA  . VAL B 780  ? 0.1803 0.2372 0.2408 0.0061  0.0271  -0.0039 778  VAL B CA  
14330 C C   . VAL B 780  ? 0.2031 0.2562 0.2634 0.0064  0.0247  -0.0054 778  VAL B C   
14331 O O   . VAL B 780  ? 0.2012 0.2520 0.2626 0.0052  0.0234  -0.0046 778  VAL B O   
14332 C CB  . VAL B 780  ? 0.1878 0.2489 0.2535 0.0053  0.0279  -0.0034 778  VAL B CB  
14333 C CG1 . VAL B 780  ? 0.1836 0.2458 0.2513 0.0069  0.0271  -0.0057 778  VAL B CG1 
14334 C CG2 . VAL B 780  ? 0.1879 0.2538 0.2539 0.0051  0.0306  -0.0018 778  VAL B CG2 
14335 N N   . MET B 781  ? 0.1846 0.2369 0.2431 0.0080  0.0240  -0.0074 779  MET B N   
14336 C CA  . MET B 781  ? 0.2059 0.2552 0.2643 0.0083  0.0219  -0.0088 779  MET B CA  
14337 C C   . MET B 781  ? 0.2106 0.2614 0.2713 0.0092  0.0215  -0.0104 779  MET B C   
14338 O O   . MET B 781  ? 0.2321 0.2843 0.2917 0.0108  0.0223  -0.0114 779  MET B O   
14339 C CB  . MET B 781  ? 0.1856 0.2322 0.2394 0.0090  0.0210  -0.0096 779  MET B CB  
14340 C CG  . MET B 781  ? 0.1870 0.2329 0.2385 0.0083  0.0214  -0.0079 779  MET B CG  
14341 S SD  . MET B 781  ? 0.2276 0.2714 0.2741 0.0089  0.0204  -0.0087 779  MET B SD  
14342 C CE  . MET B 781  ? 0.2078 0.2494 0.2551 0.0086  0.0183  -0.0092 779  MET B CE  
14343 N N   . PHE B 782  ? 0.1851 0.2356 0.2492 0.0085  0.0203  -0.0105 780  PHE B N   
14344 C CA  . PHE B 782  ? 0.1728 0.2253 0.2400 0.0092  0.0198  -0.0116 780  PHE B CA  
14345 C C   . PHE B 782  ? 0.2244 0.2738 0.2915 0.0092  0.0175  -0.0128 780  PHE B C   
14346 O O   . PHE B 782  ? 0.2030 0.2503 0.2703 0.0080  0.0165  -0.0123 780  PHE B O   
14347 C CB  . PHE B 782  ? 0.1974 0.2538 0.2695 0.0080  0.0206  -0.0103 780  PHE B CB  
14348 C CG  . PHE B 782  ? 0.2306 0.2893 0.3064 0.0086  0.0198  -0.0113 780  PHE B CG  
14349 C CD1 . PHE B 782  ? 0.1973 0.2594 0.2739 0.0107  0.0209  -0.0122 780  PHE B CD1 
14350 C CD2 . PHE B 782  ? 0.1998 0.2573 0.2782 0.0074  0.0178  -0.0115 780  PHE B CD2 
14351 C CE1 . PHE B 782  ? 0.2240 0.2884 0.3041 0.0116  0.0200  -0.0131 780  PHE B CE1 
14352 C CE2 . PHE B 782  ? 0.1946 0.2543 0.2763 0.0080  0.0168  -0.0123 780  PHE B CE2 
14353 C CZ  . PHE B 782  ? 0.2087 0.2721 0.2915 0.0101  0.0179  -0.0131 780  PHE B CZ  
14354 N N   . THR B 783  ? 0.2023 0.2515 0.2690 0.0107  0.0167  -0.0144 781  THR B N   
14355 C CA  . THR B 783  ? 0.2210 0.2678 0.2879 0.0107  0.0145  -0.0155 781  THR B CA  
14356 C C   . THR B 783  ? 0.2139 0.2633 0.2840 0.0119  0.0141  -0.0163 781  THR B C   
14357 O O   . THR B 783  ? 0.2372 0.2878 0.3065 0.0137  0.0149  -0.0171 781  THR B O   
14358 C CB  . THR B 783  ? 0.2073 0.2504 0.2697 0.0113  0.0134  -0.0164 781  THR B CB  
14359 O OG1 . THR B 783  ? 0.2122 0.2539 0.2722 0.0104  0.0138  -0.0155 781  THR B OG1 
14360 C CG2 . THR B 783  ? 0.2402 0.2811 0.3027 0.0111  0.0113  -0.0173 781  THR B CG2 
14361 N N   . GLY B 784  ? 0.2207 0.2708 0.2942 0.0109  0.0128  -0.0162 782  GLY B N   
14362 C CA  . GLY B 784  ? 0.2125 0.2657 0.2897 0.0118  0.0123  -0.0167 782  GLY B CA  
14363 C C   . GLY B 784  ? 0.2086 0.2631 0.2900 0.0099  0.0112  -0.0160 782  GLY B C   
14364 O O   . GLY B 784  ? 0.2309 0.2823 0.3111 0.0084  0.0101  -0.0158 782  GLY B O   
14365 N N   . SER B 785  ? 0.2250 0.2844 0.3111 0.0101  0.0114  -0.0157 783  SER B N   
14366 C CA  . SER B 785  ? 0.2647 0.3255 0.3550 0.0083  0.0098  -0.0151 783  SER B CA  
14367 C C   . SER B 785  ? 0.3021 0.3630 0.3936 0.0055  0.0104  -0.0134 783  SER B C   
14368 O O   . SER B 785  ? 0.2207 0.2831 0.3118 0.0051  0.0126  -0.0122 783  SER B O   
14369 C CB  . SER B 785  ? 0.2219 0.2888 0.3174 0.0092  0.0098  -0.0150 783  SER B CB  
14370 O OG  . SER B 785  ? 0.2705 0.3426 0.3686 0.0090  0.0124  -0.0137 783  SER B OG  
14371 N N   . THR B 786  ? 0.2770 0.3360 0.3699 0.0035  0.0083  -0.0132 784  THR B N   
14372 C CA  . THR B 786  ? 0.2709 0.3293 0.3650 0.0007  0.0085  -0.0116 784  THR B CA  
14373 C C   . THR B 786  ? 0.2530 0.3178 0.3520 -0.0005 0.0101  -0.0098 784  THR B C   
14374 O O   . THR B 786  ? 0.2479 0.3130 0.3469 -0.0021 0.0116  -0.0081 784  THR B O   
14375 C CB  . THR B 786  ? 0.3080 0.3629 0.4026 -0.0011 0.0057  -0.0119 784  THR B CB  
14376 O OG1 . THR B 786  ? 0.4171 0.4758 0.5160 -0.0013 0.0041  -0.0122 784  THR B OG1 
14377 C CG2 . THR B 786  ? 0.2930 0.3420 0.3825 0.0000  0.0043  -0.0135 784  THR B CG2 
14378 N N   . GLU B 787  ? 0.2156 0.2859 0.3190 0.0003  0.0099  -0.0100 785  GLU B N   
14379 C CA  . GLU B 787  ? 0.2518 0.3293 0.3605 -0.0008 0.0115  -0.0082 785  GLU B CA  
14380 C C   . GLU B 787  ? 0.2562 0.3362 0.3634 0.0003  0.0148  -0.0074 785  GLU B C   
14381 O O   . GLU B 787  ? 0.2327 0.3158 0.3420 -0.0018 0.0164  -0.0052 785  GLU B O   
14382 C CB  . GLU B 787  ? 0.3339 0.4173 0.4474 0.0007  0.0108  -0.0088 785  GLU B CB  
14383 N N   . VAL B 788  ? 0.2147 0.2933 0.3181 0.0035  0.0158  -0.0090 786  VAL B N   
14384 C CA  . VAL B 788  ? 0.2249 0.3055 0.3263 0.0048  0.0188  -0.0084 786  VAL B CA  
14385 C C   . VAL B 788  ? 0.2170 0.2931 0.3146 0.0030  0.0194  -0.0073 786  VAL B C   
14386 O O   . VAL B 788  ? 0.2355 0.3142 0.3331 0.0022  0.0217  -0.0056 786  VAL B O   
14387 C CB  . VAL B 788  ? 0.2506 0.3300 0.3484 0.0085  0.0193  -0.0105 786  VAL B CB  
14388 C CG1 . VAL B 788  ? 0.2580 0.3379 0.3523 0.0097  0.0221  -0.0102 786  VAL B CG1 
14389 C CG2 . VAL B 788  ? 0.2444 0.3290 0.3463 0.0107  0.0191  -0.0114 786  VAL B CG2 
14390 N N   . ALA B 789  ? 0.2083 0.2779 0.3026 0.0024  0.0174  -0.0080 787  ALA B N   
14391 C CA  . ALA B 789  ? 0.2012 0.2665 0.2922 0.0009  0.0177  -0.0069 787  ALA B CA  
14392 C C   . ALA B 789  ? 0.2094 0.2766 0.3035 -0.0022 0.0182  -0.0045 787  ALA B C   
14393 O O   . ALA B 789  ? 0.1808 0.2476 0.2731 -0.0031 0.0197  -0.0029 787  ALA B O   
14394 C CB  . ALA B 789  ? 0.1970 0.2557 0.2848 0.0009  0.0154  -0.0082 787  ALA B CB  
14395 N N   . ARG B 790  ? 0.2232 0.2923 0.3218 -0.0041 0.0166  -0.0040 788  ARG B N   
14396 C CA  . ARG B 790  ? 0.2138 0.2847 0.3155 -0.0075 0.0167  -0.0015 788  ARG B CA  
14397 C C   . ARG B 790  ? 0.2240 0.3021 0.3283 -0.0077 0.0198  0.0003  788  ARG B C   
14398 O O   . ARG B 790  ? 0.2463 0.3248 0.3506 -0.0100 0.0209  0.0027  788  ARG B O   
14399 C CB  . ARG B 790  ? 0.2317 0.3038 0.3380 -0.0096 0.0142  -0.0015 788  ARG B CB  
14400 C CG  . ARG B 790  ? 0.3094 0.3746 0.4131 -0.0097 0.0112  -0.0032 788  ARG B CG  
14401 C CD  . ARG B 790  ? 0.3920 0.4498 0.4908 -0.0103 0.0107  -0.0029 788  ARG B CD  
14402 N NE  . ARG B 790  ? 0.4138 0.4710 0.5135 -0.0134 0.0111  -0.0004 788  ARG B NE  
14403 C CZ  . ARG B 790  ? 0.3878 0.4414 0.4883 -0.0164 0.0088  0.0005  788  ARG B CZ  
14404 N NH1 . ARG B 790  ? 0.3865 0.4368 0.4870 -0.0166 0.0060  -0.0012 788  ARG B NH1 
14405 N NH2 . ARG B 790  ? 0.3669 0.4199 0.4680 -0.0193 0.0092  0.0030  788  ARG B NH2 
14406 N N   . LEU B 791  ? 0.1816 0.2654 0.2879 -0.0052 0.0211  -0.0007 789  LEU B N   
14407 C CA  . LEU B 791  ? 0.2196 0.3107 0.3280 -0.0049 0.0242  0.0008  789  LEU B CA  
14408 C C   . LEU B 791  ? 0.2293 0.3180 0.3325 -0.0040 0.0264  0.0013  789  LEU B C   
14409 O O   . LEU B 791  ? 0.2115 0.3038 0.3154 -0.0056 0.0286  0.0037  789  LEU B O   
14410 C CB  . LEU B 791  ? 0.2007 0.2974 0.3115 -0.0015 0.0251  -0.0009 789  LEU B CB  
14411 C CG  . LEU B 791  ? 0.2735 0.3745 0.3903 -0.0021 0.0233  -0.0011 789  LEU B CG  
14412 C CD1 . LEU B 791  ? 0.2983 0.4039 0.4164 0.0019  0.0242  -0.0029 789  LEU B CD1 
14413 C CD2 . LEU B 791  ? 0.3153 0.4226 0.4379 -0.0058 0.0239  0.0019  789  LEU B CD2 
14414 N N   . ILE B 792  ? 0.2197 0.3026 0.3176 -0.0018 0.0258  -0.0006 790  ILE B N   
14415 C CA  . ILE B 792  ? 0.2071 0.2874 0.2997 -0.0010 0.0274  -0.0002 790  ILE B CA  
14416 C C   . ILE B 792  ? 0.2372 0.3140 0.3287 -0.0040 0.0270  0.0021  790  ILE B C   
14417 O O   . ILE B 792  ? 0.2552 0.3332 0.3451 -0.0048 0.0289  0.0040  790  ILE B O   
14418 C CB  . ILE B 792  ? 0.1753 0.2503 0.2631 0.0017  0.0263  -0.0028 790  ILE B CB  
14419 C CG1 . ILE B 792  ? 0.1870 0.2651 0.2748 0.0049  0.0271  -0.0048 790  ILE B CG1 
14420 C CG2 . ILE B 792  ? 0.1928 0.2641 0.2752 0.0018  0.0271  -0.0022 790  ILE B CG2 
14421 C CD1 . ILE B 792  ? 0.2117 0.2846 0.2954 0.0070  0.0254  -0.0073 790  ILE B CD1 
14422 N N   . GLN B 793  ? 0.1872 0.2590 0.2791 -0.0056 0.0243  0.0019  791  GLN B N   
14423 C CA  . GLN B 793  ? 0.2418 0.3093 0.3325 -0.0083 0.0235  0.0039  791  GLN B CA  
14424 C C   . GLN B 793  ? 0.2224 0.2946 0.3166 -0.0113 0.0249  0.0069  791  GLN B C   
14425 O O   . GLN B 793  ? 0.2323 0.3029 0.3243 -0.0128 0.0258  0.0091  791  GLN B O   
14426 C CB  . GLN B 793  ? 0.2537 0.3159 0.3449 -0.0094 0.0203  0.0029  791  GLN B CB  
14427 C CG  . GLN B 793  ? 0.2663 0.3230 0.3561 -0.0120 0.0190  0.0047  791  GLN B CG  
14428 C CD  . GLN B 793  ? 0.3142 0.3675 0.4059 -0.0137 0.0160  0.0040  791  GLN B CD  
14429 O OE1 . GLN B 793  ? 0.3007 0.3580 0.3968 -0.0146 0.0153  0.0037  791  GLN B OE1 
14430 N NE2 . GLN B 793  ? 0.3420 0.3878 0.4302 -0.0138 0.0142  0.0037  791  GLN B NE2 
14431 N N   . ALA B 794  ? 0.2009 0.2793 0.3006 -0.0123 0.0250  0.0073  792  ALA B N   
14432 C CA  . ALA B 794  ? 0.2696 0.3534 0.3732 -0.0156 0.0264  0.0104  792  ALA B CA  
14433 C C   . ALA B 794  ? 0.2967 0.3855 0.3987 -0.0145 0.0300  0.0117  792  ALA B C   
14434 O O   . ALA B 794  ? 0.2398 0.3297 0.3417 -0.0171 0.0312  0.0146  792  ALA B O   
14435 C CB  . ALA B 794  ? 0.2615 0.3519 0.3717 -0.0166 0.0258  0.0104  792  ALA B CB  
14436 N N   . GLN B 795  ? 0.2556 0.3469 0.3561 -0.0106 0.0315  0.0095  793  GLN B N   
14437 C CA  . GLN B 795  ? 0.2317 0.3272 0.3299 -0.0093 0.0349  0.0103  793  GLN B CA  
14438 C C   . GLN B 795  ? 0.2407 0.3303 0.3330 -0.0099 0.0351  0.0115  793  GLN B C   
14439 O O   . GLN B 795  ? 0.2567 0.3489 0.3480 -0.0112 0.0372  0.0140  793  GLN B O   
14440 C CB  . GLN B 795  ? 0.2773 0.3751 0.3740 -0.0049 0.0360  0.0074  793  GLN B CB  
14441 C CG  . GLN B 795  ? 0.3464 0.4482 0.4401 -0.0031 0.0394  0.0079  793  GLN B CG  
14442 C CD  . GLN B 795  ? 0.4065 0.5174 0.5048 -0.0047 0.0421  0.0105  793  GLN B CD  
14443 O OE1 . GLN B 795  ? 0.4434 0.5559 0.5402 -0.0066 0.0440  0.0131  793  GLN B OE1 
14444 N NE2 . GLN B 795  ? 0.4272 0.5444 0.5313 -0.0040 0.0422  0.0099  793  GLN B NE2 
14445 N N   . LEU B 796  ? 0.2032 0.2851 0.2917 -0.0088 0.0328  0.0098  794  LEU B N   
14446 C CA  . LEU B 796  ? 0.2457 0.3222 0.3287 -0.0088 0.0328  0.0107  794  LEU B CA  
14447 C C   . LEU B 796  ? 0.2790 0.3529 0.3624 -0.0125 0.0321  0.0138  794  LEU B C   
14448 O O   . LEU B 796  ? 0.2775 0.3496 0.3573 -0.0131 0.0331  0.0157  794  LEU B O   
14449 C CB  . LEU B 796  ? 0.2208 0.2907 0.3003 -0.0068 0.0306  0.0082  794  LEU B CB  
14450 C CG  . LEU B 796  ? 0.2124 0.2829 0.2897 -0.0033 0.0309  0.0052  794  LEU B CG  
14451 C CD1 . LEU B 796  ? 0.2192 0.2833 0.2934 -0.0020 0.0286  0.0033  794  LEU B CD1 
14452 C CD2 . LEU B 796  ? 0.2077 0.2807 0.2813 -0.0019 0.0335  0.0057  794  LEU B CD2 
14453 N N   . ALA B 797  ? 0.2436 0.3168 0.3311 -0.0150 0.0302  0.0145  795  ALA B N   
14454 C CA  . ALA B 797  ? 0.2998 0.3694 0.3876 -0.0188 0.0291  0.0174  795  ALA B CA  
14455 C C   . ALA B 797  ? 0.2795 0.3546 0.3686 -0.0213 0.0316  0.0209  795  ALA B C   
14456 O O   . ALA B 797  ? 0.3335 0.4053 0.4217 -0.0244 0.0309  0.0237  795  ALA B O   
14457 C CB  . ALA B 797  ? 0.3208 0.3889 0.4128 -0.0210 0.0264  0.0171  795  ALA B CB  
14458 N N   . ASP B 798  ? 0.3012 0.3845 0.3922 -0.0200 0.0344  0.0207  796  ASP B N   
14459 C CA  . ASP B 798  ? 0.3006 0.3900 0.3925 -0.0221 0.0373  0.0240  796  ASP B CA  
14460 C C   . ASP B 798  ? 0.3316 0.4183 0.4173 -0.0212 0.0387  0.0252  796  ASP B C   
14461 O O   . ASP B 798  ? 0.3853 0.4748 0.4706 -0.0236 0.0406  0.0285  796  ASP B O   
14462 C CB  . ASP B 798  ? 0.3263 0.4257 0.4222 -0.0205 0.0400  0.0232  796  ASP B CB  
14463 C CG  . ASP B 798  ? 0.4676 0.5748 0.5664 -0.0234 0.0427  0.0269  796  ASP B CG  
14464 O OD1 . ASP B 798  ? 0.4824 0.5889 0.5838 -0.0278 0.0416  0.0299  796  ASP B OD1 
14465 O OD2 . ASP B 798  ? 0.4577 0.5718 0.5560 -0.0212 0.0460  0.0268  796  ASP B OD2 
14466 N N   . ARG B 799  ? 0.3188 0.4001 0.3997 -0.0180 0.0379  0.0227  797  ARG B N   
14467 C CA  . ARG B 799  ? 0.3286 0.4081 0.4036 -0.0167 0.0392  0.0234  797  ARG B CA  
14468 C C   . ARG B 799  ? 0.3129 0.3833 0.3837 -0.0165 0.0366  0.0233  797  ARG B C   
14469 O O   . ARG B 799  ? 0.2949 0.3603 0.3669 -0.0166 0.0339  0.0220  797  ARG B O   
14470 C CB  . ARG B 799  ? 0.3550 0.4374 0.4274 -0.0126 0.0409  0.0205  797  ARG B CB  
14471 C CG  . ARG B 799  ? 0.4527 0.5438 0.5264 -0.0122 0.0445  0.0214  797  ARG B CG  
14472 C CD  . ARG B 799  ? 0.4858 0.5781 0.5556 -0.0081 0.0459  0.0185  797  ARG B CD  
14473 N NE  . ARG B 799  ? 0.4885 0.5811 0.5607 -0.0056 0.0447  0.0150  797  ARG B NE  
14474 C CZ  . ARG B 799  ? 0.4095 0.4965 0.4790 -0.0035 0.0426  0.0123  797  ARG B CZ  
14475 N NH1 . ARG B 799  ? 0.3761 0.4571 0.4405 -0.0033 0.0414  0.0123  797  ARG B NH1 
14476 N NH2 . ARG B 799  ? 0.3658 0.4535 0.4378 -0.0015 0.0416  0.0095  797  ARG B NH2 
14477 N N   . LEU B 800  ? 0.2924 0.3608 0.3582 -0.0161 0.0374  0.0248  798  LEU B N   
14478 C CA  . LEU B 800  ? 0.3108 0.3715 0.3722 -0.0152 0.0352  0.0247  798  LEU B CA  
14479 C C   . LEU B 800  ? 0.3229 0.3840 0.3794 -0.0122 0.0362  0.0232  798  LEU B C   
14480 O O   . LEU B 800  ? 0.3471 0.4135 0.4024 -0.0114 0.0388  0.0232  798  LEU B O   
14481 C CB  . LEU B 800  ? 0.3372 0.3939 0.3969 -0.0182 0.0345  0.0285  798  LEU B CB  
14482 C CG  . LEU B 800  ? 0.3243 0.3784 0.3879 -0.0215 0.0327  0.0300  798  LEU B CG  
14483 C CD1 . LEU B 800  ? 0.3448 0.3947 0.4058 -0.0243 0.0322  0.0340  798  LEU B CD1 
14484 C CD2 . LEU B 800  ? 0.2700 0.3183 0.3342 -0.0200 0.0297  0.0272  798  LEU B CD2 
14485 N N   . SER B 801  ? 0.3166 0.3720 0.3700 -0.0104 0.0341  0.0219  799  SER B N   
14486 C CA  . SER B 801  ? 0.3362 0.3909 0.3847 -0.0079 0.0344  0.0208  799  SER B CA  
14487 C C   . SER B 801  ? 0.4428 0.4983 0.4874 -0.0089 0.0358  0.0238  799  SER B C   
14488 O O   . SER B 801  ? 0.3605 0.4157 0.4060 -0.0116 0.0362  0.0269  799  SER B O   
14489 C CB  . SER B 801  ? 0.3755 0.4245 0.4223 -0.0063 0.0316  0.0194  799  SER B CB  
14490 O OG  . SER B 801  ? 0.3680 0.4122 0.4133 -0.0075 0.0302  0.0220  799  SER B OG  
14491 N N   . PRO B 802  ? 0.4202 0.4763 0.4600 -0.0070 0.0365  0.0231  800  PRO B N   
14492 C CA  . PRO B 802  ? 0.4606 0.5163 0.4959 -0.0079 0.0374  0.0261  800  PRO B CA  
14493 C C   . PRO B 802  ? 0.4715 0.5216 0.5061 -0.0094 0.0353  0.0288  800  PRO B C   
14494 O O   . PRO B 802  ? 0.4928 0.5426 0.5257 -0.0115 0.0361  0.0322  800  PRO B O   
14495 C CB  . PRO B 802  ? 0.5097 0.5653 0.5401 -0.0053 0.0373  0.0242  800  PRO B CB  
14496 C CG  . PRO B 802  ? 0.5104 0.5688 0.5429 -0.0034 0.0379  0.0205  800  PRO B CG  
14497 C CD  . PRO B 802  ? 0.4553 0.5129 0.4936 -0.0042 0.0367  0.0197  800  PRO B CD  
14498 N N   . ALA B 803  ? 0.4290 0.4743 0.4645 -0.0083 0.0327  0.0274  801  ALA B N   
14499 C CA  . ALA B 803  ? 0.4002 0.4395 0.4348 -0.0090 0.0305  0.0295  801  ALA B CA  
14500 C C   . ALA B 803  ? 0.4064 0.4436 0.4449 -0.0116 0.0298  0.0310  801  ALA B C   
14501 O O   . ALA B 803  ? 0.4746 0.5059 0.5125 -0.0121 0.0277  0.0324  801  ALA B O   
14502 C CB  . ALA B 803  ? 0.4288 0.4644 0.4626 -0.0063 0.0280  0.0273  801  ALA B CB  
14503 N N   . GLY B 804  ? 0.3947 0.4365 0.4372 -0.0133 0.0314  0.0306  802  GLY B N   
14504 C CA  . GLY B 804  ? 0.3720 0.4121 0.4183 -0.0162 0.0306  0.0322  802  GLY B CA  
14505 C C   . GLY B 804  ? 0.3563 0.3924 0.4054 -0.0155 0.0282  0.0298  802  GLY B C   
14506 O O   . GLY B 804  ? 0.3418 0.3730 0.3920 -0.0174 0.0264  0.0311  802  GLY B O   
14507 N N   . ARG B 805  ? 0.3377 0.3754 0.3877 -0.0129 0.0280  0.0262  803  ARG B N   
14508 C CA  . ARG B 805  ? 0.3270 0.3612 0.3790 -0.0117 0.0258  0.0237  803  ARG B CA  
14509 C C   . ARG B 805  ? 0.2973 0.3363 0.3533 -0.0114 0.0266  0.0211  803  ARG B C   
14510 O O   . ARG B 805  ? 0.2946 0.3394 0.3509 -0.0109 0.0288  0.0206  803  ARG B O   
14511 C CB  . ARG B 805  ? 0.3406 0.3716 0.3893 -0.0084 0.0244  0.0219  803  ARG B CB  
14512 C CG  . ARG B 805  ? 0.3869 0.4130 0.4316 -0.0081 0.0233  0.0243  803  ARG B CG  
14513 C CD  . ARG B 805  ? 0.4364 0.4561 0.4818 -0.0095 0.0212  0.0257  803  ARG B CD  
14514 N NE  . ARG B 805  ? 0.5195 0.5339 0.5610 -0.0087 0.0199  0.0278  803  ARG B NE  
14515 C CZ  . ARG B 805  ? 0.4251 0.4365 0.4650 -0.0110 0.0197  0.0313  803  ARG B CZ  
14516 N NH1 . ARG B 805  ? 0.4459 0.4596 0.4878 -0.0146 0.0210  0.0333  803  ARG B NH1 
14517 N NH2 . ARG B 805  ? 0.3968 0.4027 0.4331 -0.0098 0.0181  0.0330  803  ARG B NH2 
14518 N N   . PRO B 806  ? 0.2724 0.3090 0.3311 -0.0116 0.0248  0.0195  804  PRO B N   
14519 C CA  . PRO B 806  ? 0.2660 0.3070 0.3284 -0.0112 0.0253  0.0171  804  PRO B CA  
14520 C C   . PRO B 806  ? 0.2595 0.3033 0.3202 -0.0081 0.0262  0.0146  804  PRO B C   
14521 O O   . PRO B 806  ? 0.2612 0.3021 0.3185 -0.0061 0.0254  0.0138  804  PRO B O   
14522 C CB  . PRO B 806  ? 0.2892 0.3254 0.3533 -0.0114 0.0226  0.0156  804  PRO B CB  
14523 C CG  . PRO B 806  ? 0.3235 0.3538 0.3862 -0.0133 0.0212  0.0182  804  PRO B CG  
14524 C CD  . PRO B 806  ? 0.2877 0.3172 0.3461 -0.0122 0.0221  0.0198  804  PRO B CD  
14525 N N   . ILE B 807  ? 0.2368 0.2862 0.2998 -0.0078 0.0278  0.0134  805  ILE B N   
14526 C CA  . ILE B 807  ? 0.2324 0.2842 0.2939 -0.0051 0.0285  0.0108  805  ILE B CA  
14527 C C   . ILE B 807  ? 0.2587 0.3076 0.3211 -0.0037 0.0264  0.0082  805  ILE B C   
14528 O O   . ILE B 807  ? 0.2248 0.2741 0.2910 -0.0046 0.0255  0.0075  805  ILE B O   
14529 C CB  . ILE B 807  ? 0.2434 0.3018 0.3071 -0.0048 0.0308  0.0104  805  ILE B CB  
14530 C CG1 . ILE B 807  ? 0.3246 0.3865 0.3874 -0.0063 0.0332  0.0132  805  ILE B CG1 
14531 C CG2 . ILE B 807  ? 0.2445 0.3039 0.3061 -0.0019 0.0311  0.0075  805  ILE B CG2 
14532 C CD1 . ILE B 807  ? 0.3352 0.3961 0.3924 -0.0049 0.0341  0.0135  805  ILE B CD1 
14533 N N   . PRO B 808  ? 0.2264 0.2727 0.2855 -0.0017 0.0255  0.0067  806  PRO B N   
14534 C CA  . PRO B 808  ? 0.2579 0.3017 0.3178 -0.0005 0.0235  0.0044  806  PRO B CA  
14535 C C   . PRO B 808  ? 0.2829 0.3298 0.3452 0.0002  0.0238  0.0023  806  PRO B C   
14536 O O   . PRO B 808  ? 0.2447 0.2950 0.3062 0.0012  0.0253  0.0016  806  PRO B O   
14537 C CB  . PRO B 808  ? 0.2520 0.2938 0.3078 0.0013  0.0230  0.0038  806  PRO B CB  
14538 C CG  . PRO B 808  ? 0.3092 0.3506 0.3625 0.0007  0.0238  0.0062  806  PRO B CG  
14539 C CD  . PRO B 808  ? 0.2405 0.2858 0.2953 -0.0007 0.0259  0.0075  806  PRO B CD  
14540 N N   . LEU B 809  ? 0.2442 0.2897 0.3091 -0.0001 0.0222  0.0012  807  LEU B N   
14541 C CA  . LEU B 809  ? 0.2357 0.2834 0.3026 0.0008  0.0220  -0.0010 807  LEU B CA  
14542 C C   . LEU B 809  ? 0.2318 0.2758 0.2975 0.0018  0.0199  -0.0028 807  LEU B C   
14543 O O   . LEU B 809  ? 0.2583 0.2990 0.3245 0.0011  0.0185  -0.0026 807  LEU B O   
14544 C CB  . LEU B 809  ? 0.2215 0.2719 0.2931 -0.0009 0.0220  -0.0005 807  LEU B CB  
14545 C CG  . LEU B 809  ? 0.2409 0.2929 0.3150 0.0000  0.0211  -0.0026 807  LEU B CG  
14546 C CD1 . LEU B 809  ? 0.2332 0.2879 0.3059 0.0023  0.0222  -0.0041 807  LEU B CD1 
14547 C CD2 . LEU B 809  ? 0.2364 0.2917 0.3156 -0.0019 0.0210  -0.0017 807  LEU B CD2 
14548 N N   . ILE B 810  ? 0.1892 0.2336 0.2530 0.0036  0.0198  -0.0045 808  ILE B N   
14549 C CA  . ILE B 810  ? 0.2111 0.2529 0.2740 0.0045  0.0181  -0.0063 808  ILE B CA  
14550 C C   . ILE B 810  ? 0.2191 0.2628 0.2843 0.0048  0.0177  -0.0078 808  ILE B C   
14551 O O   . ILE B 810  ? 0.2363 0.2824 0.3011 0.0058  0.0186  -0.0085 808  ILE B O   
14552 C CB  . ILE B 810  ? 0.1925 0.2333 0.2515 0.0058  0.0180  -0.0068 808  ILE B CB  
14553 C CG1 . ILE B 810  ? 0.2428 0.2823 0.2997 0.0056  0.0183  -0.0051 808  ILE B CG1 
14554 C CG2 . ILE B 810  ? 0.2365 0.2753 0.2948 0.0065  0.0163  -0.0084 808  ILE B CG2 
14555 C CD1 . ILE B 810  ? 0.2946 0.3337 0.3481 0.0067  0.0180  -0.0055 808  ILE B CD1 
14556 N N   . ALA B 811  ? 0.1913 0.2337 0.2587 0.0042  0.0162  -0.0083 809  ALA B N   
14557 C CA  . ALA B 811  ? 0.2288 0.2730 0.2988 0.0044  0.0156  -0.0096 809  ALA B CA  
14558 C C   . ALA B 811  ? 0.2876 0.3288 0.3566 0.0049  0.0136  -0.0111 809  ALA B C   
14559 O O   . ALA B 811  ? 0.2715 0.3098 0.3400 0.0043  0.0125  -0.0110 809  ALA B O   
14560 C CB  . ALA B 811  ? 0.2000 0.2467 0.2744 0.0027  0.0157  -0.0085 809  ALA B CB  
14561 N N   . GLU B 812  ? 0.2443 0.2860 0.3124 0.0061  0.0131  -0.0126 810  GLU B N   
14562 C CA  . GLU B 812  ? 0.2685 0.3078 0.3357 0.0065  0.0112  -0.0139 810  GLU B CA  
14563 C C   . GLU B 812  ? 0.2563 0.2976 0.3266 0.0066  0.0104  -0.0147 810  GLU B C   
14564 O O   . GLU B 812  ? 0.2279 0.2716 0.2989 0.0076  0.0111  -0.0150 810  GLU B O   
14565 C CB  . GLU B 812  ? 0.2659 0.3037 0.3293 0.0076  0.0110  -0.0147 810  GLU B CB  
14566 C CG  . GLU B 812  ? 0.3591 0.3943 0.4209 0.0078  0.0093  -0.0157 810  GLU B CG  
14567 C CD  . GLU B 812  ? 0.4176 0.4528 0.4792 0.0084  0.0081  -0.0170 810  GLU B CD  
14568 O OE1 . GLU B 812  ? 0.3813 0.4162 0.4404 0.0091  0.0082  -0.0174 810  GLU B OE1 
14569 O OE2 . GLU B 812  ? 0.4462 0.4815 0.5101 0.0082  0.0069  -0.0175 810  GLU B OE2 
14570 N N   . THR B 813  ? 0.2555 0.2956 0.3275 0.0057  0.0088  -0.0150 811  THR B N   
14571 C CA  . THR B 813  ? 0.2411 0.2839 0.3170 0.0054  0.0080  -0.0152 811  THR B CA  
14572 C C   . THR B 813  ? 0.2991 0.3398 0.3747 0.0055  0.0056  -0.0165 811  THR B C   
14573 O O   . THR B 813  ? 0.3197 0.3617 0.3985 0.0047  0.0044  -0.0166 811  THR B O   
14574 C CB  . THR B 813  ? 0.2755 0.3204 0.3553 0.0035  0.0084  -0.0138 811  THR B CB  
14575 O OG1 . THR B 813  ? 0.2392 0.2802 0.3176 0.0021  0.0075  -0.0134 811  THR B OG1 
14576 C CG2 . THR B 813  ? 0.2881 0.3362 0.3687 0.0035  0.0108  -0.0125 811  THR B CG2 
14577 N N   . GLY B 814  ? 0.2932 0.3310 0.3649 0.0065  0.0050  -0.0175 812  GLY B N   
14578 C CA  . GLY B 814  ? 0.3633 0.3996 0.4343 0.0068  0.0029  -0.0186 812  GLY B CA  
14579 C C   . GLY B 814  ? 0.3337 0.3674 0.4045 0.0057  0.0012  -0.0190 812  GLY B C   
14580 O O   . GLY B 814  ? 0.2945 0.3265 0.3648 0.0048  0.0015  -0.0184 812  GLY B O   
14581 N N   . GLY B 815  ? 0.3002 0.3329 0.3707 0.0058  -0.0008 -0.0199 813  GLY B N   
14582 C CA  . GLY B 815  ? 0.2897 0.3192 0.3586 0.0051  -0.0025 -0.0205 813  GLY B CA  
14583 C C   . GLY B 815  ? 0.3117 0.3411 0.3815 0.0049  -0.0049 -0.0213 813  GLY B C   
14584 O O   . GLY B 815  ? 0.3758 0.4076 0.4473 0.0057  -0.0053 -0.0214 813  GLY B O   
14585 N N   . GLN B 816  ? 0.2778 0.3042 0.3462 0.0040  -0.0066 -0.0220 814  GLN B N   
14586 C CA  . GLN B 816  ? 0.2544 0.2799 0.3224 0.0038  -0.0092 -0.0229 814  GLN B CA  
14587 C C   . GLN B 816  ? 0.2492 0.2706 0.3116 0.0045  -0.0097 -0.0239 814  GLN B C   
14588 O O   . GLN B 816  ? 0.2437 0.2621 0.3041 0.0039  -0.0109 -0.0246 814  GLN B O   
14589 C CB  . GLN B 816  ? 0.2708 0.2964 0.3420 0.0020  -0.0110 -0.0228 814  GLN B CB  
14590 C CG  . GLN B 816  ? 0.3179 0.3437 0.3898 0.0017  -0.0138 -0.0235 814  GLN B CG  
14591 C CD  . GLN B 816  ? 0.3713 0.4017 0.4469 0.0026  -0.0138 -0.0230 814  GLN B CD  
14592 O OE1 . GLN B 816  ? 0.3254 0.3559 0.3991 0.0044  -0.0133 -0.0232 814  GLN B OE1 
14593 N NE2 . GLN B 816  ? 0.3981 0.4325 0.4793 0.0015  -0.0146 -0.0223 814  GLN B NE2 
14594 N N   . ASN B 817  ? 0.2278 0.2494 0.2875 0.0057  -0.0088 -0.0239 815  ASN B N   
14595 C CA  . ASN B 817  ? 0.1871 0.2061 0.2419 0.0064  -0.0083 -0.0243 815  ASN B CA  
14596 C C   . ASN B 817  ? 0.1988 0.2155 0.2504 0.0064  -0.0104 -0.0253 815  ASN B C   
14597 O O   . ASN B 817  ? 0.1981 0.2154 0.2501 0.0065  -0.0118 -0.0253 815  ASN B O   
14598 C CB  . ASN B 817  ? 0.1881 0.2085 0.2414 0.0072  -0.0065 -0.0237 815  ASN B CB  
14599 C CG  . ASN B 817  ? 0.2143 0.2371 0.2706 0.0072  -0.0047 -0.0228 815  ASN B CG  
14600 O OD1 . ASN B 817  ? 0.2045 0.2271 0.2617 0.0069  -0.0036 -0.0224 815  ASN B OD1 
14601 N ND2 . ASN B 817  ? 0.1817 0.2064 0.2394 0.0077  -0.0044 -0.0224 815  ASN B ND2 
14602 N N   . ALA B 818  ? 0.2050 0.2190 0.2531 0.0066  -0.0105 -0.0260 816  ALA B N   
14603 C CA  . ALA B 818  ? 0.2194 0.2309 0.2637 0.0067  -0.0123 -0.0270 816  ALA B CA  
14604 C C   . ALA B 818  ? 0.1789 0.1899 0.2184 0.0077  -0.0111 -0.0271 816  ALA B C   
14605 O O   . ALA B 818  ? 0.2185 0.2306 0.2576 0.0083  -0.0089 -0.0265 816  ALA B O   
14606 C CB  . ALA B 818  ? 0.1833 0.1916 0.2267 0.0062  -0.0137 -0.0281 816  ALA B CB  
14607 N N   . MET B 819  ? 0.1787 0.1885 0.2147 0.0078  -0.0125 -0.0276 817  MET B N   
14608 C CA  . MET B 819  ? 0.1918 0.2011 0.2228 0.0086  -0.0116 -0.0277 817  MET B CA  
14609 C C   . MET B 819  ? 0.2473 0.2535 0.2745 0.0087  -0.0134 -0.0291 817  MET B C   
14610 O O   . MET B 819  ? 0.2285 0.2336 0.2561 0.0080  -0.0158 -0.0294 817  MET B O   
14611 C CB  . MET B 819  ? 0.1757 0.1865 0.2053 0.0083  -0.0114 -0.0266 817  MET B CB  
14612 C CG  . MET B 819  ? 0.2064 0.2172 0.2307 0.0087  -0.0106 -0.0265 817  MET B CG  
14613 S SD  . MET B 819  ? 0.2684 0.2801 0.2907 0.0078  -0.0111 -0.0251 817  MET B SD  
14614 C CE  . MET B 819  ? 0.2283 0.2427 0.2538 0.0076  -0.0090 -0.0238 817  MET B CE  
14615 N N   . ILE B 820  ? 0.1926 0.1974 0.2162 0.0098  -0.0123 -0.0299 818  ILE B N   
14616 C CA  . ILE B 820  ? 0.2073 0.2090 0.2262 0.0103  -0.0138 -0.0314 818  ILE B CA  
14617 C C   . ILE B 820  ? 0.2418 0.2447 0.2558 0.0110  -0.0128 -0.0311 818  ILE B C   
14618 O O   . ILE B 820  ? 0.2480 0.2535 0.2614 0.0118  -0.0104 -0.0303 818  ILE B O   
14619 C CB  . ILE B 820  ? 0.2116 0.2104 0.2293 0.0113  -0.0134 -0.0328 818  ILE B CB  
14620 C CG1 . ILE B 820  ? 0.2306 0.2279 0.2528 0.0101  -0.0148 -0.0329 818  ILE B CG1 
14621 C CG2 . ILE B 820  ? 0.2126 0.2078 0.2243 0.0122  -0.0148 -0.0346 818  ILE B CG2 
14622 C CD1 . ILE B 820  ? 0.2579 0.2514 0.2788 0.0109  -0.0146 -0.0341 818  ILE B CD1 
14623 N N   . VAL B 821  ? 0.2328 0.2341 0.2434 0.0106  -0.0148 -0.0316 819  VAL B N   
14624 C CA  . VAL B 821  ? 0.2235 0.2259 0.2291 0.0108  -0.0141 -0.0311 819  VAL B CA  
14625 C C   . VAL B 821  ? 0.2355 0.2346 0.2356 0.0117  -0.0153 -0.0329 819  VAL B C   
14626 O O   . VAL B 821  ? 0.2194 0.2155 0.2192 0.0110  -0.0181 -0.0338 819  VAL B O   
14627 C CB  . VAL B 821  ? 0.2511 0.2543 0.2572 0.0094  -0.0156 -0.0296 819  VAL B CB  
14628 C CG1 . VAL B 821  ? 0.2393 0.2435 0.2399 0.0093  -0.0150 -0.0288 819  VAL B CG1 
14629 C CG2 . VAL B 821  ? 0.2105 0.2163 0.2217 0.0087  -0.0146 -0.0281 819  VAL B CG2 
14630 N N   . ASP B 822  ? 0.2552 0.2552 0.2509 0.0133  -0.0133 -0.0333 820  ASP B N   
14631 C CA  . ASP B 822  ? 0.2829 0.2795 0.2726 0.0144  -0.0144 -0.0352 820  ASP B CA  
14632 C C   . ASP B 822  ? 0.2707 0.2688 0.2554 0.0140  -0.0144 -0.0344 820  ASP B C   
14633 O O   . ASP B 822  ? 0.2529 0.2541 0.2390 0.0127  -0.0138 -0.0323 820  ASP B O   
14634 C CB  . ASP B 822  ? 0.2430 0.2387 0.2305 0.0169  -0.0124 -0.0368 820  ASP B CB  
14635 C CG  . ASP B 822  ? 0.2816 0.2819 0.2672 0.0184  -0.0091 -0.0359 820  ASP B CG  
14636 O OD1 . ASP B 822  ? 0.2699 0.2740 0.2549 0.0174  -0.0082 -0.0340 820  ASP B OD1 
14637 O OD2 . ASP B 822  ? 0.3172 0.3173 0.3020 0.0207  -0.0073 -0.0369 820  ASP B OD2 
14638 N N   . SER B 823  ? 0.2740 0.2694 0.2524 0.0151  -0.0151 -0.0360 821  SER B N   
14639 C CA  . SER B 823  ? 0.3174 0.3137 0.2906 0.0145  -0.0155 -0.0352 821  SER B CA  
14640 C C   . SER B 823  ? 0.3726 0.3741 0.3437 0.0152  -0.0121 -0.0337 821  SER B C   
14641 O O   . SER B 823  ? 0.3411 0.3440 0.3080 0.0144  -0.0120 -0.0325 821  SER B O   
14642 C CB  . SER B 823  ? 0.3104 0.3022 0.2771 0.0155  -0.0174 -0.0375 821  SER B CB  
14643 O OG  . SER B 823  ? 0.3446 0.3353 0.3085 0.0181  -0.0156 -0.0395 821  SER B OG  
14644 N N   . SER B 824  ? 0.2546 0.2590 0.2284 0.0166  -0.0093 -0.0336 822  SER B N   
14645 C CA  . SER B 824  ? 0.2765 0.2866 0.2491 0.0170  -0.0061 -0.0319 822  SER B CA  
14646 C C   . SER B 824  ? 0.2951 0.3089 0.2725 0.0147  -0.0056 -0.0291 822  SER B C   
14647 O O   . SER B 824  ? 0.2973 0.3160 0.2739 0.0142  -0.0035 -0.0273 822  SER B O   
14648 C CB  . SER B 824  ? 0.3010 0.3131 0.2739 0.0200  -0.0034 -0.0331 822  SER B CB  
14649 O OG  . SER B 824  ? 0.2825 0.2953 0.2617 0.0199  -0.0028 -0.0326 822  SER B OG  
14650 N N   . ALA B 825  ? 0.2387 0.2503 0.2211 0.0133  -0.0074 -0.0288 823  ALA B N   
14651 C CA  . ALA B 825  ? 0.2823 0.2967 0.2689 0.0114  -0.0070 -0.0265 823  ALA B CA  
14652 C C   . ALA B 825  ? 0.3050 0.3201 0.2888 0.0093  -0.0079 -0.0245 823  ALA B C   
14653 O O   . ALA B 825  ? 0.2958 0.3081 0.2754 0.0090  -0.0098 -0.0250 823  ALA B O   
14654 C CB  . ALA B 825  ? 0.2545 0.2663 0.2467 0.0107  -0.0087 -0.0269 823  ALA B CB  
14655 N N   . LEU B 826  ? 0.2776 0.2960 0.2632 0.0078  -0.0068 -0.0223 824  LEU B N   
14656 C CA  . LEU B 826  ? 0.3247 0.3431 0.3078 0.0054  -0.0079 -0.0201 824  LEU B CA  
14657 C C   . LEU B 826  ? 0.3145 0.3289 0.3004 0.0042  -0.0108 -0.0199 824  LEU B C   
14658 O O   . LEU B 826  ? 0.3096 0.3242 0.3002 0.0039  -0.0107 -0.0195 824  LEU B O   
14659 C CB  . LEU B 826  ? 0.3926 0.4158 0.3763 0.0039  -0.0058 -0.0177 824  LEU B CB  
14660 C CG  . LEU B 826  ? 0.4007 0.4237 0.3815 0.0011  -0.0069 -0.0151 824  LEU B CG  
14661 C CD1 . LEU B 826  ? 0.4403 0.4623 0.4150 0.0011  -0.0076 -0.0152 824  LEU B CD1 
14662 C CD2 . LEU B 826  ? 0.5240 0.5522 0.5055 -0.0006 -0.0048 -0.0127 824  LEU B CD2 
14663 N N   . ALA B 827  ? 0.2853 0.2962 0.2681 0.0038  -0.0134 -0.0201 825  ALA B N   
14664 C CA  . ALA B 827  ? 0.3153 0.3225 0.3008 0.0032  -0.0164 -0.0202 825  ALA B CA  
14665 C C   . ALA B 827  ? 0.3083 0.3159 0.2965 0.0018  -0.0165 -0.0183 825  ALA B C   
14666 O O   . ALA B 827  ? 0.3054 0.3119 0.2983 0.0021  -0.0173 -0.0187 825  ALA B O   
14667 C CB  . ALA B 827  ? 0.3086 0.3125 0.2895 0.0028  -0.0192 -0.0201 825  ALA B CB  
14668 N N   . GLU B 828  ? 0.2867 0.2956 0.2717 0.0000  -0.0158 -0.0161 826  GLU B N   
14669 C CA  . GLU B 828  ? 0.3173 0.3255 0.3040 -0.0016 -0.0163 -0.0143 826  GLU B CA  
14670 C C   . GLU B 828  ? 0.3263 0.3370 0.3181 -0.0011 -0.0144 -0.0147 826  GLU B C   
14671 O O   . GLU B 828  ? 0.2847 0.2936 0.2794 -0.0014 -0.0153 -0.0144 826  GLU B O   
14672 C CB  . GLU B 828  ? 0.3589 0.3685 0.3411 -0.0040 -0.0158 -0.0116 826  GLU B CB  
14673 C CG  . GLU B 828  ? 0.4021 0.4084 0.3791 -0.0051 -0.0182 -0.0106 826  GLU B CG  
14674 C CD  . GLU B 828  ? 0.4538 0.4611 0.4268 -0.0041 -0.0177 -0.0116 826  GLU B CD  
14675 O OE1 . GLU B 828  ? 0.4159 0.4265 0.3898 -0.0025 -0.0153 -0.0131 826  GLU B OE1 
14676 O OE2 . GLU B 828  ? 0.4799 0.4842 0.4485 -0.0047 -0.0199 -0.0110 826  GLU B OE2 
14677 N N   . GLN B 829  ? 0.2828 0.2974 0.2754 -0.0002 -0.0117 -0.0152 827  GLN B N   
14678 C CA  . GLN B 829  ? 0.2535 0.2704 0.2509 0.0004  -0.0100 -0.0156 827  GLN B CA  
14679 C C   . GLN B 829  ? 0.2713 0.2860 0.2728 0.0021  -0.0109 -0.0176 827  GLN B C   
14680 O O   . GLN B 829  ? 0.2648 0.2793 0.2701 0.0021  -0.0108 -0.0176 827  GLN B O   
14681 C CB  . GLN B 829  ? 0.2970 0.3188 0.2942 0.0012  -0.0071 -0.0157 827  GLN B CB  
14682 N N   . VAL B 830  ? 0.2738 0.2867 0.2744 0.0033  -0.0118 -0.0192 828  VAL B N   
14683 C CA  . VAL B 830  ? 0.2560 0.2670 0.2607 0.0045  -0.0130 -0.0209 828  VAL B CA  
14684 C C   . VAL B 830  ? 0.2762 0.2850 0.2830 0.0039  -0.0151 -0.0203 828  VAL B C   
14685 O O   . VAL B 830  ? 0.2595 0.2686 0.2708 0.0044  -0.0149 -0.0207 828  VAL B O   
14686 C CB  . VAL B 830  ? 0.2606 0.2696 0.2631 0.0054  -0.0144 -0.0226 828  VAL B CB  
14687 C CG1 . VAL B 830  ? 0.2583 0.2654 0.2651 0.0060  -0.0162 -0.0238 828  VAL B CG1 
14688 C CG2 . VAL B 830  ? 0.2805 0.2911 0.2813 0.0067  -0.0122 -0.0236 828  VAL B CG2 
14689 N N   . VAL B 831  ? 0.2518 0.2584 0.2553 0.0030  -0.0171 -0.0193 829  VAL B N   
14690 C CA  . VAL B 831  ? 0.2709 0.2748 0.2761 0.0029  -0.0194 -0.0190 829  VAL B CA  
14691 C C   . VAL B 831  ? 0.2521 0.2566 0.2595 0.0024  -0.0184 -0.0180 829  VAL B C   
14692 O O   . VAL B 831  ? 0.2578 0.2616 0.2689 0.0033  -0.0190 -0.0185 829  VAL B O   
14693 C CB  . VAL B 831  ? 0.2653 0.2662 0.2658 0.0021  -0.0218 -0.0180 829  VAL B CB  
14694 C CG1 . VAL B 831  ? 0.2608 0.2589 0.2624 0.0021  -0.0240 -0.0172 829  VAL B CG1 
14695 C CG2 . VAL B 831  ? 0.2879 0.2878 0.2871 0.0028  -0.0235 -0.0193 829  VAL B CG2 
14696 N N   . GLY B 832  ? 0.2481 0.2540 0.2530 0.0010  -0.0169 -0.0166 830  GLY B N   
14697 C CA  . GLY B 832  ? 0.2516 0.2579 0.2582 0.0003  -0.0160 -0.0157 830  GLY B CA  
14698 C C   . GLY B 832  ? 0.2541 0.2626 0.2657 0.0017  -0.0143 -0.0170 830  GLY B C   
14699 O O   . GLY B 832  ? 0.2361 0.2436 0.2504 0.0022  -0.0146 -0.0172 830  GLY B O   
14700 N N   . ASP B 833  ? 0.2471 0.2583 0.2598 0.0025  -0.0126 -0.0179 831  ASP B N   
14701 C CA  . ASP B 833  ? 0.2386 0.2517 0.2556 0.0035  -0.0110 -0.0188 831  ASP B CA  
14702 C C   . ASP B 833  ? 0.2248 0.2365 0.2454 0.0048  -0.0122 -0.0201 831  ASP B C   
14703 O O   . ASP B 833  ? 0.2322 0.2448 0.2566 0.0054  -0.0114 -0.0205 831  ASP B O   
14704 C CB  . ASP B 833  ? 0.2015 0.2174 0.2182 0.0041  -0.0090 -0.0193 831  ASP B CB  
14705 C CG  . ASP B 833  ? 0.2652 0.2839 0.2795 0.0030  -0.0074 -0.0178 831  ASP B CG  
14706 O OD1 . ASP B 833  ? 0.2701 0.2886 0.2839 0.0016  -0.0077 -0.0164 831  ASP B OD1 
14707 O OD2 . ASP B 833  ? 0.2670 0.2881 0.2799 0.0036  -0.0059 -0.0180 831  ASP B OD2 
14708 N N   . VAL B 834  ? 0.2051 0.2150 0.2248 0.0051  -0.0142 -0.0207 832  VAL B N   
14709 C CA  . VAL B 834  ? 0.1910 0.2002 0.2145 0.0060  -0.0156 -0.0218 832  VAL B CA  
14710 C C   . VAL B 834  ? 0.2081 0.2161 0.2331 0.0063  -0.0168 -0.0213 832  VAL B C   
14711 O O   . VAL B 834  ? 0.2250 0.2341 0.2543 0.0072  -0.0165 -0.0218 832  VAL B O   
14712 C CB  . VAL B 834  ? 0.2237 0.2313 0.2454 0.0062  -0.0177 -0.0225 832  VAL B CB  
14713 C CG1 . VAL B 834  ? 0.2143 0.2215 0.2399 0.0069  -0.0197 -0.0232 832  VAL B CG1 
14714 C CG2 . VAL B 834  ? 0.2381 0.2464 0.2589 0.0064  -0.0166 -0.0235 832  VAL B CG2 
14715 N N   . ILE B 835  ? 0.2071 0.2127 0.2285 0.0057  -0.0181 -0.0203 833  ILE B N   
14716 C CA  . ILE B 835  ? 0.2314 0.2350 0.2535 0.0063  -0.0194 -0.0199 833  ILE B CA  
14717 C C   . ILE B 835  ? 0.2416 0.2465 0.2660 0.0065  -0.0175 -0.0199 833  ILE B C   
14718 O O   . ILE B 835  ? 0.2607 0.2658 0.2884 0.0078  -0.0176 -0.0204 833  ILE B O   
14719 C CB  . ILE B 835  ? 0.2742 0.2743 0.2911 0.0052  -0.0212 -0.0186 833  ILE B CB  
14720 C CG1 . ILE B 835  ? 0.3206 0.3191 0.3353 0.0052  -0.0235 -0.0186 833  ILE B CG1 
14721 C CG2 . ILE B 835  ? 0.3018 0.2991 0.3190 0.0059  -0.0224 -0.0183 833  ILE B CG2 
14722 C CD1 . ILE B 835  ? 0.3780 0.3747 0.3947 0.0068  -0.0261 -0.0191 833  ILE B CD1 
14723 N N   . THR B 836  ? 0.2132 0.2194 0.2359 0.0052  -0.0156 -0.0192 834  THR B N   
14724 C CA  . THR B 836  ? 0.2259 0.2335 0.2505 0.0053  -0.0138 -0.0191 834  THR B CA  
14725 C C   . THR B 836  ? 0.2544 0.2648 0.2839 0.0066  -0.0124 -0.0202 834  THR B C   
14726 O O   . THR B 836  ? 0.2590 0.2697 0.2910 0.0075  -0.0120 -0.0205 834  THR B O   
14727 C CB  . THR B 836  ? 0.2656 0.2748 0.2877 0.0036  -0.0122 -0.0180 834  THR B CB  
14728 O OG1 . THR B 836  ? 0.3432 0.3499 0.3609 0.0021  -0.0136 -0.0167 834  THR B OG1 
14729 C CG2 . THR B 836  ? 0.3176 0.3285 0.3416 0.0037  -0.0104 -0.0179 834  THR B CG2 
14730 N N   . SER B 837  ? 0.2158 0.2280 0.2463 0.0066  -0.0117 -0.0207 835  SER B N   
14731 C CA  . SER B 837  ? 0.1909 0.2053 0.2256 0.0074  -0.0103 -0.0214 835  SER B CA  
14732 C C   . SER B 837  ? 0.2257 0.2403 0.2642 0.0085  -0.0115 -0.0221 835  SER B C   
14733 O O   . SER B 837  ? 0.2086 0.2251 0.2508 0.0091  -0.0103 -0.0224 835  SER B O   
14734 C CB  . SER B 837  ? 0.1827 0.1980 0.2172 0.0072  -0.0097 -0.0219 835  SER B CB  
14735 O OG  . SER B 837  ? 0.2097 0.2259 0.2412 0.0066  -0.0083 -0.0212 835  SER B OG  
14736 N N   . ALA B 838  ? 0.1917 0.2047 0.2295 0.0087  -0.0138 -0.0224 836  ALA B N   
14737 C CA  . ALA B 838  ? 0.1861 0.2001 0.2279 0.0098  -0.0150 -0.0230 836  ALA B CA  
14738 C C   . ALA B 838  ? 0.1995 0.2128 0.2421 0.0111  -0.0156 -0.0228 836  ALA B C   
14739 O O   . ALA B 838  ? 0.2318 0.2474 0.2788 0.0122  -0.0154 -0.0232 836  ALA B O   
14740 C CB  . ALA B 838  ? 0.2013 0.2140 0.2421 0.0096  -0.0175 -0.0233 836  ALA B CB  
14741 N N   . PHE B 839  ? 0.1888 0.1990 0.2273 0.0109  -0.0164 -0.0223 837  PHE B N   
14742 C CA  . PHE B 839  ? 0.2442 0.2526 0.2827 0.0124  -0.0176 -0.0223 837  PHE B CA  
14743 C C   . PHE B 839  ? 0.2671 0.2739 0.3034 0.0124  -0.0165 -0.0220 837  PHE B C   
14744 O O   . PHE B 839  ? 0.2569 0.2622 0.2935 0.0141  -0.0171 -0.0224 837  PHE B O   
14745 C CB  . PHE B 839  ? 0.2248 0.2299 0.2602 0.0125  -0.0205 -0.0220 837  PHE B CB  
14746 C CG  . PHE B 839  ? 0.2282 0.2345 0.2651 0.0124  -0.0220 -0.0223 837  PHE B CG  
14747 C CD1 . PHE B 839  ? 0.2416 0.2511 0.2839 0.0136  -0.0222 -0.0230 837  PHE B CD1 
14748 C CD2 . PHE B 839  ? 0.2461 0.2505 0.2789 0.0110  -0.0231 -0.0218 837  PHE B CD2 
14749 C CE1 . PHE B 839  ? 0.2339 0.2445 0.2775 0.0132  -0.0239 -0.0233 837  PHE B CE1 
14750 C CE2 . PHE B 839  ? 0.2766 0.2818 0.3104 0.0109  -0.0247 -0.0223 837  PHE B CE2 
14751 C CZ  . PHE B 839  ? 0.2779 0.2860 0.3171 0.0119  -0.0252 -0.0230 837  PHE B CZ  
14752 N N   . ASP B 840  ? 0.2524 0.2594 0.2865 0.0107  -0.0149 -0.0214 838  ASP B N   
14753 C CA  . ASP B 840  ? 0.2536 0.2595 0.2861 0.0106  -0.0138 -0.0212 838  ASP B CA  
14754 C C   . ASP B 840  ? 0.2742 0.2824 0.3106 0.0124  -0.0124 -0.0220 838  ASP B C   
14755 O O   . ASP B 840  ? 0.2319 0.2438 0.2725 0.0128  -0.0113 -0.0224 838  ASP B O   
14756 C CB  . ASP B 840  ? 0.3203 0.3276 0.3511 0.0086  -0.0121 -0.0204 838  ASP B CB  
14757 C CG  . ASP B 840  ? 0.3248 0.3313 0.3540 0.0081  -0.0111 -0.0201 838  ASP B CG  
14758 O OD1 . ASP B 840  ? 0.3028 0.3115 0.3347 0.0090  -0.0094 -0.0206 838  ASP B OD1 
14759 O OD2 . ASP B 840  ? 0.3900 0.3935 0.4150 0.0067  -0.0122 -0.0193 838  ASP B OD2 
14760 N N   . SER B 841  ? 0.2584 0.2642 0.2933 0.0135  -0.0126 -0.0223 839  SER B N   
14761 C CA  . SER B 841  ? 0.2766 0.2845 0.3146 0.0155  -0.0112 -0.0232 839  SER B CA  
14762 C C   . SER B 841  ? 0.2211 0.2320 0.2639 0.0174  -0.0116 -0.0238 839  SER B C   
14763 O O   . SER B 841  ? 0.2231 0.2380 0.2700 0.0183  -0.0099 -0.0242 839  SER B O   
14764 C CB  . SER B 841  ? 0.2629 0.2741 0.3023 0.0145  -0.0086 -0.0229 839  SER B CB  
14765 O OG  . SER B 841  ? 0.2991 0.3081 0.3344 0.0126  -0.0085 -0.0222 839  SER B OG  
14766 N N   . ALA B 842  ? 0.2331 0.2422 0.2753 0.0178  -0.0140 -0.0238 840  ALA B N   
14767 C CA  . ALA B 842  ? 0.2138 0.2258 0.2606 0.0194  -0.0150 -0.0242 840  ALA B CA  
14768 C C   . ALA B 842  ? 0.1959 0.2128 0.2472 0.0183  -0.0135 -0.0241 840  ALA B C   
14769 O O   . ALA B 842  ? 0.2044 0.2254 0.2607 0.0195  -0.0132 -0.0244 840  ALA B O   
14770 C CB  . ALA B 842  ? 0.2392 0.2519 0.2879 0.0225  -0.0148 -0.0250 840  ALA B CB  
14771 N N   . GLY B 843  ? 0.1991 0.2158 0.2487 0.0160  -0.0127 -0.0236 841  GLY B N   
14772 C CA  . GLY B 843  ? 0.2111 0.2313 0.2642 0.0149  -0.0116 -0.0235 841  GLY B CA  
14773 C C   . GLY B 843  ? 0.2253 0.2490 0.2818 0.0154  -0.0091 -0.0236 841  GLY B C   
14774 O O   . GLY B 843  ? 0.2302 0.2572 0.2906 0.0147  -0.0084 -0.0234 841  GLY B O   
14775 N N   . GLN B 844  ? 0.1979 0.2210 0.2530 0.0163  -0.0079 -0.0237 842  GLN B N   
14776 C CA  . GLN B 844  ? 0.2224 0.2488 0.2803 0.0169  -0.0055 -0.0236 842  GLN B CA  
14777 C C   . GLN B 844  ? 0.2476 0.2739 0.3037 0.0153  -0.0037 -0.0231 842  GLN B C   
14778 O O   . GLN B 844  ? 0.2710 0.2981 0.3268 0.0158  -0.0019 -0.0230 842  GLN B O   
14779 C CB  . GLN B 844  ? 0.2034 0.2292 0.2606 0.0193  -0.0053 -0.0243 842  GLN B CB  
14780 C CG  . GLN B 844  ? 0.1826 0.2096 0.2426 0.0214  -0.0069 -0.0248 842  GLN B CG  
14781 C CD  . GLN B 844  ? 0.1794 0.2057 0.2386 0.0243  -0.0067 -0.0256 842  GLN B CD  
14782 O OE1 . GLN B 844  ? 0.1991 0.2294 0.2625 0.0264  -0.0063 -0.0259 842  GLN B OE1 
14783 N NE2 . GLN B 844  ? 0.2527 0.2740 0.3064 0.0244  -0.0070 -0.0259 842  GLN B NE2 
14784 N N   . ARG B 845  ? 0.2517 0.2769 0.3063 0.0136  -0.0040 -0.0227 843  ARG B N   
14785 C CA  . ARG B 845  ? 0.2303 0.2560 0.2839 0.0123  -0.0024 -0.0221 843  ARG B CA  
14786 C C   . ARG B 845  ? 0.2325 0.2606 0.2897 0.0116  -0.0018 -0.0219 843  ARG B C   
14787 O O   . ARG B 845  ? 0.2489 0.2772 0.3078 0.0113  -0.0032 -0.0221 843  ARG B O   
14788 C CB  . ARG B 845  ? 0.2429 0.2660 0.2923 0.0111  -0.0031 -0.0218 843  ARG B CB  
14789 C CG  . ARG B 845  ? 0.2463 0.2664 0.2917 0.0111  -0.0040 -0.0217 843  ARG B CG  
14790 C CD  . ARG B 845  ? 0.3048 0.3235 0.3466 0.0096  -0.0045 -0.0211 843  ARG B CD  
14791 N NE  . ARG B 845  ? 0.3051 0.3209 0.3429 0.0090  -0.0054 -0.0207 843  ARG B NE  
14792 C CZ  . ARG B 845  ? 0.3286 0.3444 0.3643 0.0081  -0.0045 -0.0201 843  ARG B CZ  
14793 N NH1 . ARG B 845  ? 0.3197 0.3382 0.3568 0.0078  -0.0026 -0.0197 843  ARG B NH1 
14794 N NH2 . ARG B 845  ? 0.3983 0.4110 0.4302 0.0073  -0.0057 -0.0197 843  ARG B NH2 
14795 N N   . CYS B 846  ? 0.2156 0.2454 0.2739 0.0111  0.0002  -0.0213 844  CYS B N   
14796 C CA  A CYS B 846  ? 0.2507 0.2820 0.3118 0.0102  0.0006  -0.0209 844  CYS B CA  
14797 C CA  B CYS B 846  ? 0.2508 0.2821 0.3119 0.0102  0.0006  -0.0209 844  CYS B CA  
14798 C C   . CYS B 846  ? 0.2218 0.2508 0.2808 0.0093  -0.0005 -0.0211 844  CYS B C   
14799 O O   . CYS B 846  ? 0.2041 0.2331 0.2648 0.0086  -0.0012 -0.0212 844  CYS B O   
14800 C CB  A CYS B 846  ? 0.2986 0.3316 0.3607 0.0099  0.0027  -0.0201 844  CYS B CB  
14801 C CB  B CYS B 846  ? 0.2982 0.3310 0.3601 0.0098  0.0027  -0.0201 844  CYS B CB  
14802 S SG  A CYS B 846  ? 0.3758 0.4122 0.4410 0.0109  0.0041  -0.0199 844  CYS B SG  
14803 S SG  B CYS B 846  ? 0.2895 0.3206 0.3470 0.0096  0.0036  -0.0197 844  CYS B SG  
14804 N N   . SER B 847  ? 0.2102 0.2373 0.2652 0.0093  -0.0006 -0.0211 845  SER B N   
14805 C CA  . SER B 847  ? 0.2016 0.2269 0.2539 0.0088  -0.0013 -0.0213 845  SER B CA  
14806 C C   . SER B 847  ? 0.1945 0.2182 0.2457 0.0088  -0.0035 -0.0219 845  SER B C   
14807 O O   . SER B 847  ? 0.1775 0.1998 0.2261 0.0084  -0.0041 -0.0222 845  SER B O   
14808 C CB  . SER B 847  ? 0.2175 0.2424 0.2663 0.0086  -0.0005 -0.0208 845  SER B CB  
14809 O OG  . SER B 847  ? 0.2710 0.2953 0.3184 0.0088  -0.0011 -0.0207 845  SER B OG  
14810 N N   . ALA B 848  ? 0.2056 0.2295 0.2582 0.0093  -0.0046 -0.0222 846  ALA B N   
14811 C CA  . ALA B 848  ? 0.1835 0.2056 0.2345 0.0094  -0.0068 -0.0226 846  ALA B CA  
14812 C C   . ALA B 848  ? 0.2116 0.2331 0.2629 0.0089  -0.0081 -0.0231 846  ALA B C   
14813 O O   . ALA B 848  ? 0.1956 0.2182 0.2500 0.0085  -0.0078 -0.0233 846  ALA B O   
14814 C CB  . ALA B 848  ? 0.2016 0.2245 0.2550 0.0105  -0.0078 -0.0228 846  ALA B CB  
14815 N N   . LEU B 849  ? 0.2167 0.2360 0.2645 0.0087  -0.0096 -0.0234 847  LEU B N   
14816 C CA  . LEU B 849  ? 0.2002 0.2183 0.2473 0.0082  -0.0111 -0.0240 847  LEU B CA  
14817 C C   . LEU B 849  ? 0.2059 0.2249 0.2567 0.0083  -0.0130 -0.0244 847  LEU B C   
14818 O O   . LEU B 849  ? 0.2271 0.2460 0.2781 0.0090  -0.0144 -0.0242 847  LEU B O   
14819 C CB  . LEU B 849  ? 0.2031 0.2189 0.2452 0.0080  -0.0122 -0.0240 847  LEU B CB  
14820 C CG  . LEU B 849  ? 0.2084 0.2225 0.2487 0.0077  -0.0140 -0.0248 847  LEU B CG  
14821 C CD1 . LEU B 849  ? 0.1946 0.2085 0.2354 0.0075  -0.0131 -0.0255 847  LEU B CD1 
14822 C CD2 . LEU B 849  ? 0.2280 0.2404 0.2630 0.0075  -0.0146 -0.0246 847  LEU B CD2 
14823 N N   . ARG B 850  ? 0.2003 0.2201 0.2540 0.0077  -0.0133 -0.0247 848  ARG B N   
14824 C CA  . ARG B 850  ? 0.2075 0.2289 0.2652 0.0075  -0.0153 -0.0249 848  ARG B CA  
14825 C C   . ARG B 850  ? 0.2186 0.2378 0.2745 0.0067  -0.0178 -0.0256 848  ARG B C   
14826 O O   . ARG B 850  ? 0.2408 0.2608 0.2985 0.0068  -0.0201 -0.0257 848  ARG B O   
14827 C CB  . ARG B 850  ? 0.2033 0.2275 0.2659 0.0068  -0.0141 -0.0245 848  ARG B CB  
14828 C CG  . ARG B 850  ? 0.2202 0.2465 0.2842 0.0075  -0.0114 -0.0238 848  ARG B CG  
14829 C CD  . ARG B 850  ? 0.2191 0.2464 0.2833 0.0090  -0.0116 -0.0237 848  ARG B CD  
14830 N NE  . ARG B 850  ? 0.2355 0.2649 0.3012 0.0098  -0.0092 -0.0231 848  ARG B NE  
14831 C CZ  . ARG B 850  ? 0.2279 0.2577 0.2932 0.0113  -0.0090 -0.0231 848  ARG B CZ  
14832 N NH1 . ARG B 850  ? 0.1956 0.2238 0.2592 0.0122  -0.0109 -0.0235 848  ARG B NH1 
14833 N NH2 . ARG B 850  ? 0.2233 0.2548 0.2895 0.0119  -0.0068 -0.0228 848  ARG B NH2 
14834 N N   . VAL B 851  ? 0.2058 0.2224 0.2583 0.0061  -0.0175 -0.0262 849  VAL B N   
14835 C CA  . VAL B 851  ? 0.2293 0.2432 0.2794 0.0054  -0.0199 -0.0271 849  VAL B CA  
14836 C C   . VAL B 851  ? 0.2496 0.2606 0.2933 0.0059  -0.0194 -0.0276 849  VAL B C   
14837 O O   . VAL B 851  ? 0.2212 0.2314 0.2630 0.0062  -0.0175 -0.0278 849  VAL B O   
14838 C CB  . VAL B 851  ? 0.2612 0.2745 0.3135 0.0042  -0.0203 -0.0276 849  VAL B CB  
14839 C CG1 . VAL B 851  ? 0.2576 0.2678 0.3071 0.0034  -0.0232 -0.0287 849  VAL B CG1 
14840 C CG2 . VAL B 851  ? 0.2836 0.3008 0.3425 0.0035  -0.0203 -0.0267 849  VAL B CG2 
14841 N N   . LEU B 852  ? 0.2411 0.2508 0.2816 0.0061  -0.0212 -0.0278 850  LEU B N   
14842 C CA  . LEU B 852  ? 0.2344 0.2417 0.2688 0.0065  -0.0210 -0.0282 850  LEU B CA  
14843 C C   . LEU B 852  ? 0.2550 0.2595 0.2866 0.0060  -0.0229 -0.0295 850  LEU B C   
14844 O O   . LEU B 852  ? 0.2698 0.2737 0.3025 0.0054  -0.0257 -0.0298 850  LEU B O   
14845 C CB  . LEU B 852  ? 0.2327 0.2398 0.2645 0.0067  -0.0219 -0.0274 850  LEU B CB  
14846 C CG  . LEU B 852  ? 0.2168 0.2220 0.2420 0.0068  -0.0217 -0.0275 850  LEU B CG  
14847 C CD1 . LEU B 852  ? 0.2371 0.2432 0.2605 0.0072  -0.0186 -0.0273 850  LEU B CD1 
14848 C CD2 . LEU B 852  ? 0.2220 0.2267 0.2450 0.0067  -0.0230 -0.0264 850  LEU B CD2 
14849 N N   . CYS B 853  ? 0.2316 0.2343 0.2598 0.0065  -0.0216 -0.0303 851  CYS B N   
14850 C CA  . CYS B 853  ? 0.2583 0.2575 0.2831 0.0063  -0.0233 -0.0319 851  CYS B CA  
14851 C C   . CYS B 853  ? 0.2314 0.2290 0.2494 0.0071  -0.0231 -0.0324 851  CYS B C   
14852 O O   . CYS B 853  ? 0.2389 0.2370 0.2543 0.0082  -0.0206 -0.0323 851  CYS B O   
14853 C CB  . CYS B 853  ? 0.2527 0.2504 0.2783 0.0065  -0.0221 -0.0326 851  CYS B CB  
14854 S SG  . CYS B 853  ? 0.2710 0.2713 0.3044 0.0053  -0.0216 -0.0316 851  CYS B SG  
14855 N N   . LEU B 854  ? 0.2652 0.2610 0.2802 0.0067  -0.0258 -0.0328 852  LEU B N   
14856 C CA  . LEU B 854  ? 0.2466 0.2412 0.2549 0.0073  -0.0257 -0.0330 852  LEU B CA  
14857 C C   . LEU B 854  ? 0.2920 0.2827 0.2955 0.0077  -0.0272 -0.0350 852  LEU B C   
14858 O O   . LEU B 854  ? 0.2826 0.2711 0.2871 0.0067  -0.0301 -0.0359 852  LEU B O   
14859 C CB  . LEU B 854  ? 0.2733 0.2685 0.2810 0.0067  -0.0277 -0.0319 852  LEU B CB  
14860 C CG  . LEU B 854  ? 0.2656 0.2637 0.2774 0.0065  -0.0266 -0.0301 852  LEU B CG  
14861 C CD1 . LEU B 854  ? 0.2507 0.2484 0.2617 0.0061  -0.0292 -0.0291 852  LEU B CD1 
14862 C CD2 . LEU B 854  ? 0.2458 0.2456 0.2556 0.0070  -0.0234 -0.0291 852  LEU B CD2 
14863 N N   . GLN B 855  ? 0.2652 0.2550 0.2632 0.0090  -0.0253 -0.0357 853  GLN B N   
14864 C CA  . GLN B 855  ? 0.2780 0.2637 0.2700 0.0097  -0.0267 -0.0378 853  GLN B CA  
14865 C C   . GLN B 855  ? 0.2979 0.2821 0.2869 0.0086  -0.0300 -0.0378 853  GLN B C   
14866 O O   . GLN B 855  ? 0.2870 0.2733 0.2752 0.0083  -0.0299 -0.0362 853  GLN B O   
14867 C CB  . GLN B 855  ? 0.2751 0.2610 0.2614 0.0117  -0.0239 -0.0384 853  GLN B CB  
14868 C CG  . GLN B 855  ? 0.3312 0.3123 0.3113 0.0129  -0.0250 -0.0409 853  GLN B CG  
14869 C CD  . GLN B 855  ? 0.3351 0.3170 0.3097 0.0153  -0.0220 -0.0416 853  GLN B CD  
14870 O OE1 . GLN B 855  ? 0.3498 0.3350 0.3265 0.0164  -0.0189 -0.0407 853  GLN B OE1 
14871 N NE2 . GLN B 855  ? 0.3997 0.3788 0.3669 0.0163  -0.0229 -0.0432 853  GLN B NE2 
14872 N N   . GLU B 856  ? 0.3246 0.3048 0.3119 0.0081  -0.0330 -0.0395 854  GLU B N   
14873 C CA  . GLU B 856  ? 0.3153 0.2942 0.3011 0.0069  -0.0367 -0.0395 854  GLU B CA  
14874 C C   . GLU B 856  ? 0.3516 0.3307 0.3310 0.0074  -0.0364 -0.0389 854  GLU B C   
14875 O O   . GLU B 856  ? 0.3700 0.3500 0.3497 0.0065  -0.0384 -0.0375 854  GLU B O   
14876 C CB  . GLU B 856  ? 0.3671 0.3413 0.3507 0.0062  -0.0399 -0.0416 854  GLU B CB  
14877 N N   . ASP B 857  ? 0.3460 0.3245 0.3194 0.0090  -0.0339 -0.0397 855  ASP B N   
14878 C CA  . ASP B 857  ? 0.3551 0.3338 0.3215 0.0095  -0.0336 -0.0392 855  ASP B CA  
14879 C C   . ASP B 857  ? 0.3701 0.3529 0.3384 0.0088  -0.0320 -0.0364 855  ASP B C   
14880 O O   . ASP B 857  ? 0.4131 0.3960 0.3767 0.0084  -0.0327 -0.0354 855  ASP B O   
14881 C CB  . ASP B 857  ? 0.4240 0.4018 0.3841 0.0116  -0.0309 -0.0407 855  ASP B CB  
14882 N N   . VAL B 858  ? 0.3384 0.3244 0.3132 0.0086  -0.0300 -0.0351 856  VAL B N   
14883 C CA  . VAL B 858  ? 0.3124 0.3015 0.2887 0.0079  -0.0289 -0.0326 856  VAL B CA  
14884 C C   . VAL B 858  ? 0.3023 0.2921 0.2852 0.0068  -0.0307 -0.0314 856  VAL B C   
14885 O O   . VAL B 858  ? 0.3079 0.2995 0.2922 0.0062  -0.0301 -0.0295 856  VAL B O   
14886 C CB  . VAL B 858  ? 0.3460 0.3386 0.3229 0.0086  -0.0247 -0.0318 856  VAL B CB  
14887 C CG1 . VAL B 858  ? 0.3715 0.3644 0.3415 0.0099  -0.0228 -0.0325 856  VAL B CG1 
14888 C CG2 . VAL B 858  ? 0.3000 0.2934 0.2829 0.0092  -0.0233 -0.0325 856  VAL B CG2 
14889 N N   . ALA B 859  ? 0.2993 0.2878 0.2864 0.0065  -0.0329 -0.0326 857  ALA B N   
14890 C CA  . ALA B 859  ? 0.3071 0.2974 0.3014 0.0059  -0.0340 -0.0316 857  ALA B CA  
14891 C C   . ALA B 859  ? 0.3184 0.3087 0.3122 0.0054  -0.0362 -0.0300 857  ALA B C   
14892 O O   . ALA B 859  ? 0.2961 0.2882 0.2936 0.0053  -0.0355 -0.0285 857  ALA B O   
14893 C CB  . ALA B 859  ? 0.3079 0.2972 0.3063 0.0055  -0.0361 -0.0330 857  ALA B CB  
14894 N N   . ASP B 860  ? 0.3713 0.3591 0.3600 0.0051  -0.0389 -0.0303 858  ASP B N   
14895 C CA  . ASP B 860  ? 0.3429 0.3302 0.3310 0.0047  -0.0415 -0.0287 858  ASP B CA  
14896 C C   . ASP B 860  ? 0.2978 0.2857 0.2832 0.0045  -0.0395 -0.0267 858  ASP B C   
14897 O O   . ASP B 860  ? 0.3516 0.3399 0.3397 0.0044  -0.0404 -0.0252 858  ASP B O   
14898 C CB  . ASP B 860  ? 0.3907 0.3750 0.3731 0.0043  -0.0448 -0.0294 858  ASP B CB  
14899 C CG  . ASP B 860  ? 0.4152 0.3989 0.4013 0.0040  -0.0480 -0.0307 858  ASP B CG  
14900 O OD1 . ASP B 860  ? 0.4766 0.4626 0.4702 0.0040  -0.0485 -0.0304 858  ASP B OD1 
14901 O OD2 . ASP B 860  ? 0.5454 0.5265 0.5269 0.0037  -0.0500 -0.0322 858  ASP B OD2 
14902 N N   . ARG B 861  ? 0.2818 0.2699 0.2618 0.0045  -0.0370 -0.0266 859  ARG B N   
14903 C CA  . ARG B 861  ? 0.2925 0.2815 0.2698 0.0038  -0.0353 -0.0245 859  ARG B CA  
14904 C C   . ARG B 861  ? 0.2959 0.2873 0.2791 0.0038  -0.0332 -0.0236 859  ARG B C   
14905 O O   . ARG B 861  ? 0.3014 0.2926 0.2850 0.0032  -0.0335 -0.0217 859  ARG B O   
14906 C CB  . ARG B 861  ? 0.3191 0.3090 0.2902 0.0038  -0.0327 -0.0246 859  ARG B CB  
14907 N N   . ILE B 862  ? 0.2834 0.2766 0.2708 0.0045  -0.0311 -0.0249 860  ILE B N   
14908 C CA  . ILE B 862  ? 0.2468 0.2422 0.2394 0.0046  -0.0291 -0.0241 860  ILE B CA  
14909 C C   . ILE B 862  ? 0.2563 0.2513 0.2540 0.0048  -0.0313 -0.0237 860  ILE B C   
14910 O O   . ILE B 862  ? 0.2925 0.2878 0.2919 0.0046  -0.0307 -0.0224 860  ILE B O   
14911 C CB  . ILE B 862  ? 0.2790 0.2764 0.2745 0.0053  -0.0265 -0.0255 860  ILE B CB  
14912 C CG1 . ILE B 862  ? 0.3207 0.3191 0.3111 0.0056  -0.0240 -0.0256 860  ILE B CG1 
14913 C CG2 . ILE B 862  ? 0.2815 0.2810 0.2826 0.0054  -0.0248 -0.0248 860  ILE B CG2 
14914 C CD1 . ILE B 862  ? 0.3134 0.3131 0.3056 0.0067  -0.0217 -0.0271 860  ILE B CD1 
14915 N N   . LEU B 863  ? 0.2795 0.2736 0.2795 0.0051  -0.0338 -0.0248 861  LEU B N   
14916 C CA  . LEU B 863  ? 0.3080 0.3025 0.3131 0.0056  -0.0359 -0.0244 861  LEU B CA  
14917 C C   . LEU B 863  ? 0.2944 0.2868 0.2966 0.0055  -0.0379 -0.0228 861  LEU B C   
14918 O O   . LEU B 863  ? 0.2850 0.2776 0.2903 0.0061  -0.0381 -0.0219 861  LEU B O   
14919 C CB  . LEU B 863  ? 0.2878 0.2822 0.2956 0.0058  -0.0386 -0.0258 861  LEU B CB  
14920 C CG  . LEU B 863  ? 0.3333 0.3297 0.3460 0.0058  -0.0372 -0.0271 861  LEU B CG  
14921 C CD1 . LEU B 863  ? 0.3173 0.3131 0.3314 0.0054  -0.0402 -0.0283 861  LEU B CD1 
14922 C CD2 . LEU B 863  ? 0.3479 0.3471 0.3672 0.0064  -0.0357 -0.0265 861  LEU B CD2 
14923 N N   . THR B 864  ? 0.2812 0.2712 0.2770 0.0049  -0.0394 -0.0223 862  THR B N   
14924 C CA  . THR B 864  ? 0.2972 0.2847 0.2896 0.0046  -0.0414 -0.0205 862  THR B CA  
14925 C C   . THR B 864  ? 0.3094 0.2969 0.3010 0.0040  -0.0391 -0.0189 862  THR B C   
14926 O O   . THR B 864  ? 0.2825 0.2684 0.2752 0.0043  -0.0404 -0.0178 862  THR B O   
14927 C CB  . THR B 864  ? 0.3507 0.3360 0.3357 0.0037  -0.0428 -0.0201 862  THR B CB  
14928 O OG1 . THR B 864  ? 0.3134 0.2983 0.2991 0.0042  -0.0455 -0.0216 862  THR B OG1 
14929 C CG2 . THR B 864  ? 0.3958 0.3781 0.3766 0.0032  -0.0449 -0.0179 862  THR B CG2 
14930 N N   . MET B 865  ? 0.2689 0.2581 0.2586 0.0032  -0.0359 -0.0189 863  MET B N   
14931 C CA  . MET B 865  ? 0.2851 0.2748 0.2743 0.0023  -0.0338 -0.0174 863  MET B CA  
14932 C C   . MET B 865  ? 0.2774 0.2682 0.2728 0.0032  -0.0330 -0.0178 863  MET B C   
14933 O O   . MET B 865  ? 0.2459 0.2352 0.2414 0.0029  -0.0332 -0.0165 863  MET B O   
14934 C CB  . MET B 865  ? 0.2704 0.2628 0.2571 0.0015  -0.0305 -0.0174 863  MET B CB  
14935 C CG  . MET B 865  ? 0.3507 0.3441 0.3361 0.0000  -0.0285 -0.0156 863  MET B CG  
14936 S SD  . MET B 865  ? 0.4065 0.4041 0.3892 -0.0006 -0.0247 -0.0155 863  MET B SD  
14937 C CE  . MET B 865  ? 0.3385 0.3348 0.3155 -0.0003 -0.0261 -0.0163 863  MET B CE  
14938 N N   . LEU B 866  ? 0.2556 0.2488 0.2561 0.0043  -0.0320 -0.0195 864  LEU B N   
14939 C CA  . LEU B 866  ? 0.2599 0.2547 0.2663 0.0052  -0.0311 -0.0199 864  LEU B CA  
14940 C C   . LEU B 866  ? 0.2824 0.2752 0.2908 0.0063  -0.0337 -0.0195 864  LEU B C   
14941 O O   . LEU B 866  ? 0.2739 0.2662 0.2839 0.0068  -0.0333 -0.0189 864  LEU B O   
14942 C CB  . LEU B 866  ? 0.2722 0.2696 0.2833 0.0059  -0.0300 -0.0216 864  LEU B CB  
14943 C CG  . LEU B 866  ? 0.2954 0.2950 0.3128 0.0069  -0.0289 -0.0220 864  LEU B CG  
14944 C CD1 . LEU B 866  ? 0.3167 0.3171 0.3337 0.0064  -0.0261 -0.0213 864  LEU B CD1 
14945 C CD2 . LEU B 866  ? 0.3435 0.3454 0.3651 0.0072  -0.0284 -0.0235 864  LEU B CD2 
14946 N N   . LYS B 867  ? 0.2671 0.2588 0.2752 0.0069  -0.0367 -0.0198 865  LYS B N   
14947 C CA  . LYS B 867  ? 0.2678 0.2579 0.2778 0.0083  -0.0394 -0.0194 865  LYS B CA  
14948 C C   . LYS B 867  ? 0.3122 0.2983 0.3174 0.0078  -0.0404 -0.0176 865  LYS B C   
14949 O O   . LYS B 867  ? 0.2662 0.2507 0.2730 0.0092  -0.0413 -0.0173 865  LYS B O   
14950 C CB  . LYS B 867  ? 0.2791 0.2691 0.2894 0.0088  -0.0426 -0.0199 865  LYS B CB  
14951 C CG  . LYS B 867  ? 0.2691 0.2629 0.2851 0.0092  -0.0422 -0.0215 865  LYS B CG  
14952 C CD  . LYS B 867  ? 0.3509 0.3443 0.3664 0.0091  -0.0455 -0.0220 865  LYS B CD  
14953 C CE  . LYS B 867  ? 0.4422 0.4392 0.4634 0.0091  -0.0455 -0.0234 865  LYS B CE  
14954 N NZ  . LYS B 867  ? 0.4938 0.4901 0.5139 0.0087  -0.0490 -0.0239 865  LYS B NZ  
14955 N N   . GLY B 868  ? 0.2784 0.2625 0.2773 0.0060  -0.0404 -0.0165 866  GLY B N   
14956 C CA  . GLY B 868  ? 0.2802 0.2602 0.2742 0.0051  -0.0414 -0.0146 866  GLY B CA  
14957 C C   . GLY B 868  ? 0.2815 0.2615 0.2766 0.0046  -0.0391 -0.0141 866  GLY B C   
14958 O O   . GLY B 868  ? 0.2898 0.2663 0.2839 0.0050  -0.0404 -0.0132 866  GLY B O   
14959 N N   . ALA B 869  ? 0.2329 0.2168 0.2301 0.0040  -0.0358 -0.0148 867  ALA B N   
14960 C CA  . ALA B 869  ? 0.2558 0.2401 0.2543 0.0035  -0.0337 -0.0145 867  ALA B CA  
14961 C C   . ALA B 869  ? 0.2679 0.2520 0.2714 0.0058  -0.0341 -0.0155 867  ALA B C   
14962 O O   . ALA B 869  ? 0.2855 0.2673 0.2885 0.0058  -0.0341 -0.0150 867  ALA B O   
14963 C CB  . ALA B 869  ? 0.2655 0.2543 0.2655 0.0026  -0.0303 -0.0151 867  ALA B CB  
14964 N N   . LEU B 870  ? 0.2352 0.2219 0.2436 0.0076  -0.0345 -0.0170 868  LEU B N   
14965 C CA  . LEU B 870  ? 0.2666 0.2541 0.2801 0.0099  -0.0347 -0.0180 868  LEU B CA  
14966 C C   . LEU B 870  ? 0.2922 0.2751 0.3038 0.0112  -0.0374 -0.0173 868  LEU B C   
14967 O O   . LEU B 870  ? 0.2825 0.2643 0.2956 0.0127  -0.0370 -0.0176 868  LEU B O   
14968 C CB  . LEU B 870  ? 0.2862 0.2776 0.3051 0.0112  -0.0351 -0.0194 868  LEU B CB  
14969 N N   . HIS B 871  ? 0.2418 0.2215 0.2494 0.0109  -0.0402 -0.0163 869  HIS B N   
14970 C CA  . HIS B 871  ? 0.3096 0.2846 0.3155 0.0125  -0.0431 -0.0156 869  HIS B CA  
14971 C C   . HIS B 871  ? 0.2986 0.2684 0.2993 0.0112  -0.0431 -0.0143 869  HIS B C   
14972 O O   . HIS B 871  ? 0.3004 0.2654 0.2993 0.0127  -0.0454 -0.0139 869  HIS B O   
14973 C CB  . HIS B 871  ? 0.3726 0.3457 0.3759 0.0127  -0.0464 -0.0150 869  HIS B CB  
14974 C CG  . HIS B 871  ? 0.4395 0.4169 0.4485 0.0146  -0.0474 -0.0163 869  HIS B CG  
14975 N ND1 . HIS B 871  ? 0.4514 0.4301 0.4655 0.0177  -0.0485 -0.0171 869  HIS B ND1 
14976 C CD2 . HIS B 871  ? 0.3901 0.3708 0.4004 0.0138  -0.0475 -0.0169 869  HIS B CD2 
14977 C CE1 . HIS B 871  ? 0.4517 0.4348 0.4704 0.0184  -0.0493 -0.0180 869  HIS B CE1 
14978 N NE2 . HIS B 871  ? 0.4510 0.4351 0.4674 0.0160  -0.0488 -0.0180 869  HIS B NE2 
14979 N N   . GLU B 872  ? 0.2397 0.2105 0.2382 0.0085  -0.0407 -0.0137 870  GLU B N   
14980 C CA  . GLU B 872  ? 0.2480 0.2145 0.2422 0.0069  -0.0406 -0.0124 870  GLU B CA  
14981 C C   . GLU B 872  ? 0.2987 0.2661 0.2961 0.0079  -0.0386 -0.0135 870  GLU B C   
14982 O O   . GLU B 872  ? 0.2683 0.2321 0.2623 0.0065  -0.0386 -0.0126 870  GLU B O   
14983 C CB  . GLU B 872  ? 0.2716 0.2392 0.2617 0.0032  -0.0391 -0.0108 870  GLU B CB  
14984 C CG  . GLU B 872  ? 0.2935 0.2598 0.2794 0.0019  -0.0410 -0.0095 870  GLU B CG  
14985 C CD  . GLU B 872  ? 0.3236 0.2829 0.3047 0.0020  -0.0446 -0.0080 870  GLU B CD  
14986 O OE1 . GLU B 872  ? 0.3429 0.2976 0.3222 0.0018  -0.0454 -0.0074 870  GLU B OE1 
14987 O OE2 . GLU B 872  ? 0.3539 0.3118 0.3325 0.0021  -0.0468 -0.0073 870  GLU B OE2 
14988 N N   . LEU B 873  ? 0.2547 0.2266 0.2581 0.0102  -0.0371 -0.0153 871  LEU B N   
14989 C CA  . LEU B 873  ? 0.2859 0.2592 0.2923 0.0112  -0.0350 -0.0164 871  LEU B CA  
14990 C C   . LEU B 873  ? 0.3031 0.2720 0.3093 0.0141  -0.0369 -0.0170 871  LEU B C   
14991 O O   . LEU B 873  ? 0.2807 0.2488 0.2882 0.0166  -0.0391 -0.0173 871  LEU B O   
14992 C CB  . LEU B 873  ? 0.2602 0.2402 0.2730 0.0124  -0.0326 -0.0178 871  LEU B CB  
14993 C CG  . LEU B 873  ? 0.2914 0.2757 0.3047 0.0100  -0.0304 -0.0176 871  LEU B CG  
14994 C CD1 . LEU B 873  ? 0.2765 0.2663 0.2961 0.0114  -0.0284 -0.0191 871  LEU B CD1 
14995 C CD2 . LEU B 873  ? 0.3095 0.2931 0.3195 0.0075  -0.0287 -0.0166 871  LEU B CD2 
14996 N N   . HIS B 874  ? 0.2844 0.2508 0.2891 0.0140  -0.0360 -0.0172 872  HIS B N   
14997 C CA  . HIS B 874  ? 0.3084 0.2704 0.3125 0.0170  -0.0374 -0.0180 872  HIS B CA  
14998 C C   . HIS B 874  ? 0.2786 0.2455 0.2883 0.0196  -0.0349 -0.0199 872  HIS B C   
14999 O O   . HIS B 874  ? 0.2492 0.2186 0.2596 0.0181  -0.0323 -0.0201 872  HIS B O   
15000 C CB  . HIS B 874  ? 0.3009 0.2558 0.2984 0.0151  -0.0386 -0.0170 872  HIS B CB  
15001 C CG  . HIS B 874  ? 0.3177 0.2668 0.3135 0.0182  -0.0401 -0.0180 872  HIS B CG  
15002 N ND1 . HIS B 874  ? 0.3948 0.3364 0.3845 0.0168  -0.0416 -0.0174 872  HIS B ND1 
15003 C CD2 . HIS B 874  ? 0.3706 0.3202 0.3697 0.0227  -0.0405 -0.0197 872  HIS B CD2 
15004 C CE1 . HIS B 874  ? 0.3670 0.3042 0.3560 0.0206  -0.0428 -0.0188 872  HIS B CE1 
15005 N NE2 . HIS B 874  ? 0.4027 0.3450 0.3975 0.0244  -0.0421 -0.0203 872  HIS B NE2 
15006 N N   . ILE B 875  ? 0.2748 0.2436 0.2886 0.0233  -0.0355 -0.0211 873  ILE B N   
15007 C CA  . ILE B 875  ? 0.2998 0.2738 0.3191 0.0258  -0.0331 -0.0227 873  ILE B CA  
15008 C C   . ILE B 875  ? 0.3160 0.2854 0.3335 0.0293  -0.0341 -0.0237 873  ILE B C   
15009 O O   . ILE B 875  ? 0.2977 0.2625 0.3131 0.0315  -0.0370 -0.0236 873  ILE B O   
15010 C CB  . ILE B 875  ? 0.2731 0.2538 0.2990 0.0275  -0.0330 -0.0232 873  ILE B CB  
15011 C CG1 . ILE B 875  ? 0.3687 0.3533 0.3959 0.0241  -0.0319 -0.0224 873  ILE B CG1 
15012 C CG2 . ILE B 875  ? 0.2446 0.2307 0.2762 0.0302  -0.0306 -0.0246 873  ILE B CG2 
15013 C CD1 . ILE B 875  ? 0.4381 0.4204 0.4626 0.0229  -0.0347 -0.0213 873  ILE B CD1 
15014 N N   . GLY B 876  ? 0.2615 0.2317 0.2794 0.0300  -0.0318 -0.0248 874  GLY B N   
15015 C CA  . GLY B 876  ? 0.3138 0.2797 0.3298 0.0337  -0.0325 -0.0261 874  GLY B CA  
15016 C C   . GLY B 876  ? 0.3025 0.2689 0.3178 0.0335  -0.0298 -0.0270 874  GLY B C   
15017 O O   . GLY B 876  ? 0.2447 0.2160 0.2622 0.0310  -0.0273 -0.0267 874  GLY B O   
15018 N N   . ARG B 877  ? 0.3157 0.2768 0.3277 0.0366  -0.0306 -0.0283 875  ARG B N   
15019 C CA  . ARG B 877  ? 0.3091 0.2697 0.3194 0.0367  -0.0285 -0.0294 875  ARG B CA  
15020 C C   . ARG B 877  ? 0.2717 0.2289 0.2772 0.0318  -0.0286 -0.0281 875  ARG B C   
15021 O O   . ARG B 877  ? 0.2861 0.2368 0.2866 0.0295  -0.0312 -0.0269 875  ARG B O   
15022 C CB  . ARG B 877  ? 0.3437 0.2979 0.3501 0.0410  -0.0298 -0.0311 875  ARG B CB  
15023 C CG  . ARG B 877  ? 0.3659 0.3217 0.3723 0.0427  -0.0271 -0.0328 875  ARG B CG  
15024 C CD  . ARG B 877  ? 0.3878 0.3373 0.3904 0.0477  -0.0284 -0.0347 875  ARG B CD  
15025 N NE  . ARG B 877  ? 0.3686 0.3071 0.3624 0.0461  -0.0310 -0.0347 875  ARG B NE  
15026 C CZ  . ARG B 877  ? 0.5074 0.4381 0.4960 0.0498  -0.0327 -0.0365 875  ARG B CZ  
15027 N NH1 . ARG B 877  ? 0.4512 0.3840 0.4423 0.0557  -0.0319 -0.0384 875  ARG B NH1 
15028 N NH2 . ARG B 877  ? 0.5114 0.4318 0.4918 0.0475  -0.0351 -0.0363 875  ARG B NH2 
15029 N N   . THR B 878  ? 0.2522 0.2139 0.2594 0.0300  -0.0257 -0.0282 876  THR B N   
15030 C CA  . THR B 878  ? 0.2691 0.2307 0.2741 0.0251  -0.0253 -0.0267 876  THR B CA  
15031 C C   . THR B 878  ? 0.2713 0.2256 0.2694 0.0234  -0.0264 -0.0267 876  THR B C   
15032 O O   . THR B 878  ? 0.2893 0.2443 0.2858 0.0194  -0.0258 -0.0254 876  THR B O   
15033 C CB  . THR B 878  ? 0.2517 0.2217 0.2618 0.0239  -0.0218 -0.0266 876  THR B CB  
15034 O OG1 . THR B 878  ? 0.3031 0.2753 0.3150 0.0268  -0.0198 -0.0282 876  THR B OG1 
15035 C CG2 . THR B 878  ? 0.2568 0.2331 0.2727 0.0241  -0.0212 -0.0261 876  THR B CG2 
15036 N N   . ASP B 879  ? 0.3231 0.2704 0.3170 0.0263  -0.0282 -0.0280 877  ASP B N   
15037 C CA  . ASP B 879  ? 0.3083 0.2472 0.2948 0.0243  -0.0301 -0.0279 877  ASP B CA  
15038 C C   . ASP B 879  ? 0.2985 0.2303 0.2800 0.0215  -0.0336 -0.0262 877  ASP B C   
15039 O O   . ASP B 879  ? 0.3257 0.2483 0.3004 0.0209  -0.0362 -0.0263 877  ASP B O   
15040 C CB  . ASP B 879  ? 0.3361 0.2699 0.3195 0.0286  -0.0304 -0.0303 877  ASP B CB  
15041 C CG  . ASP B 879  ? 0.3805 0.3101 0.3634 0.0332  -0.0326 -0.0313 877  ASP B CG  
15042 O OD1 . ASP B 879  ? 0.4177 0.3517 0.4053 0.0342  -0.0326 -0.0307 877  ASP B OD1 
15043 O OD2 . ASP B 879  ? 0.4061 0.3276 0.3835 0.0358  -0.0343 -0.0328 877  ASP B OD2 
15044 N N   . ARG B 880  ? 0.3244 0.2599 0.3086 0.0196  -0.0338 -0.0244 878  ARG B N   
15045 C CA  . ARG B 880  ? 0.3259 0.2563 0.3057 0.0160  -0.0366 -0.0223 878  ARG B CA  
15046 C C   . ARG B 880  ? 0.2811 0.2184 0.2636 0.0118  -0.0349 -0.0203 878  ARG B C   
15047 O O   . ARG B 880  ? 0.2800 0.2251 0.2684 0.0126  -0.0326 -0.0205 878  ARG B O   
15048 C CB  . ARG B 880  ? 0.3188 0.2461 0.2984 0.0186  -0.0391 -0.0221 878  ARG B CB  
15049 C CG  . ARG B 880  ? 0.4648 0.3835 0.4403 0.0226  -0.0416 -0.0236 878  ARG B CG  
15050 C CD  . ARG B 880  ? 0.4776 0.3935 0.4530 0.0248  -0.0443 -0.0231 878  ARG B CD  
15051 N NE  . ARG B 880  ? 0.6581 0.5667 0.6305 0.0297  -0.0465 -0.0248 878  ARG B NE  
15052 C CZ  . ARG B 880  ? 0.7087 0.6062 0.6738 0.0295  -0.0502 -0.0242 878  ARG B CZ  
15053 N NH1 . ARG B 880  ? 0.7340 0.6266 0.6941 0.0243  -0.0523 -0.0217 878  ARG B NH1 
15054 N NH2 . ARG B 880  ? 0.7333 0.6245 0.6960 0.0346  -0.0520 -0.0261 878  ARG B NH2 
15055 N N   . LEU B 881  ? 0.2780 0.2122 0.2560 0.0072  -0.0360 -0.0184 879  LEU B N   
15056 C CA  . LEU B 881  ? 0.2781 0.2189 0.2583 0.0032  -0.0344 -0.0165 879  LEU B CA  
15057 C C   . LEU B 881  ? 0.2932 0.2375 0.2760 0.0035  -0.0344 -0.0156 879  LEU B C   
15058 O O   . LEU B 881  ? 0.2738 0.2256 0.2607 0.0024  -0.0321 -0.0152 879  LEU B O   
15059 C CB  . LEU B 881  ? 0.2926 0.2290 0.2671 -0.0018 -0.0361 -0.0143 879  LEU B CB  
15060 C CG  . LEU B 881  ? 0.3287 0.2720 0.3050 -0.0060 -0.0344 -0.0121 879  LEU B CG  
15061 C CD1 . LEU B 881  ? 0.3340 0.2848 0.3147 -0.0058 -0.0311 -0.0130 879  LEU B CD1 
15062 C CD2 . LEU B 881  ? 0.2966 0.2351 0.2671 -0.0109 -0.0367 -0.0097 879  LEU B CD2 
15063 N N   . SER B 882  ? 0.2527 0.1914 0.2330 0.0051  -0.0372 -0.0155 880  SER B N   
15064 C CA  . SER B 882  ? 0.2984 0.2397 0.2804 0.0052  -0.0377 -0.0146 880  SER B CA  
15065 C C   . SER B 882  ? 0.2704 0.2186 0.2593 0.0087  -0.0357 -0.0163 880  SER B C   
15066 O O   . SER B 882  ? 0.2947 0.2457 0.2853 0.0087  -0.0360 -0.0157 880  SER B O   
15067 C CB  . SER B 882  ? 0.3157 0.2485 0.2929 0.0060  -0.0415 -0.0139 880  SER B CB  
15068 O OG  . SER B 882  ? 0.3213 0.2505 0.2990 0.0107  -0.0426 -0.0159 880  SER B OG  
15069 N N   . VAL B 883  ? 0.2598 0.2108 0.2522 0.0115  -0.0338 -0.0182 881  VAL B N   
15070 C CA  . VAL B 883  ? 0.2187 0.1764 0.2178 0.0144  -0.0320 -0.0196 881  VAL B CA  
15071 C C   . VAL B 883  ? 0.2213 0.1866 0.2240 0.0122  -0.0291 -0.0191 881  VAL B C   
15072 O O   . VAL B 883  ? 0.2610 0.2282 0.2636 0.0104  -0.0272 -0.0190 881  VAL B O   
15073 C CB  . VAL B 883  ? 0.2616 0.2196 0.2630 0.0184  -0.0310 -0.0217 881  VAL B CB  
15074 C CG1 . VAL B 883  ? 0.2498 0.2161 0.2585 0.0205  -0.0286 -0.0227 881  VAL B CG1 
15075 C CG2 . VAL B 883  ? 0.2634 0.2145 0.2618 0.0216  -0.0340 -0.0224 881  VAL B CG2 
15076 N N   . ASP B 884  ? 0.2520 0.2214 0.2580 0.0124  -0.0290 -0.0189 882  ASP B N   
15077 C CA  . ASP B 884  ? 0.2654 0.2414 0.2747 0.0107  -0.0265 -0.0186 882  ASP B CA  
15078 C C   . ASP B 884  ? 0.2971 0.2788 0.3126 0.0131  -0.0242 -0.0202 882  ASP B C   
15079 O O   . ASP B 884  ? 0.2789 0.2648 0.2965 0.0120  -0.0217 -0.0203 882  ASP B O   
15080 C CB  . ASP B 884  ? 0.2518 0.2288 0.2608 0.0097  -0.0277 -0.0177 882  ASP B CB  
15081 C CG  . ASP B 884  ? 0.2685 0.2404 0.2712 0.0070  -0.0298 -0.0159 882  ASP B CG  
15082 O OD1 . ASP B 884  ? 0.2789 0.2504 0.2790 0.0042  -0.0289 -0.0148 882  ASP B OD1 
15083 O OD2 . ASP B 884  ? 0.2751 0.2436 0.2757 0.0076  -0.0324 -0.0153 882  ASP B OD2 
15084 N N   . VAL B 885  ? 0.2626 0.2446 0.2810 0.0162  -0.0251 -0.0213 883  VAL B N   
15085 C CA  . VAL B 885  ? 0.2909 0.2789 0.3155 0.0183  -0.0232 -0.0224 883  VAL B CA  
15086 C C   . VAL B 885  ? 0.2615 0.2481 0.2872 0.0218  -0.0235 -0.0237 883  VAL B C   
15087 O O   . VAL B 885  ? 0.2497 0.2324 0.2737 0.0238  -0.0259 -0.0239 883  VAL B O   
15088 C CB  . VAL B 885  ? 0.3238 0.3152 0.3520 0.0186  -0.0240 -0.0224 883  VAL B CB  
15089 C CG1 . VAL B 885  ? 0.2865 0.2842 0.3214 0.0204  -0.0222 -0.0234 883  VAL B CG1 
15090 C CG2 . VAL B 885  ? 0.3044 0.2969 0.3309 0.0154  -0.0236 -0.0214 883  VAL B CG2 
15091 N N   . GLY B 886  ? 0.2304 0.2202 0.2586 0.0227  -0.0210 -0.0245 884  GLY B N   
15092 C CA  . GLY B 886  ? 0.2483 0.2375 0.2774 0.0262  -0.0207 -0.0258 884  GLY B CA  
15093 C C   . GLY B 886  ? 0.2101 0.2058 0.2460 0.0287  -0.0197 -0.0265 884  GLY B C   
15094 O O   . GLY B 886  ? 0.2197 0.2190 0.2591 0.0279  -0.0202 -0.0260 884  GLY B O   
15095 N N   . PRO B 887  ? 0.2382 0.2357 0.2760 0.0317  -0.0184 -0.0277 885  PRO B N   
15096 C CA  . PRO B 887  ? 0.2070 0.2113 0.2515 0.0343  -0.0174 -0.0282 885  PRO B CA  
15097 C C   . PRO B 887  ? 0.2196 0.2307 0.2689 0.0323  -0.0145 -0.0278 885  PRO B C   
15098 O O   . PRO B 887  ? 0.1858 0.1963 0.2330 0.0298  -0.0130 -0.0274 885  PRO B O   
15099 C CB  . PRO B 887  ? 0.2148 0.2180 0.2586 0.0382  -0.0167 -0.0296 885  PRO B CB  
15100 C CG  . PRO B 887  ? 0.2145 0.2127 0.2524 0.0366  -0.0158 -0.0298 885  PRO B CG  
15101 C CD  . PRO B 887  ? 0.2000 0.1930 0.2334 0.0332  -0.0179 -0.0286 885  PRO B CD  
15102 N N   . VAL B 888  ? 0.2200 0.2376 0.2757 0.0335  -0.0140 -0.0278 886  VAL B N   
15103 C CA  . VAL B 888  ? 0.2129 0.2369 0.2732 0.0324  -0.0111 -0.0275 886  VAL B CA  
15104 C C   . VAL B 888  ? 0.2114 0.2375 0.2724 0.0352  -0.0088 -0.0284 886  VAL B C   
15105 O O   . VAL B 888  ? 0.2386 0.2622 0.2977 0.0385  -0.0096 -0.0294 886  VAL B O   
15106 C CB  . VAL B 888  ? 0.2090 0.2392 0.2758 0.0318  -0.0115 -0.0269 886  VAL B CB  
15107 C CG1 . VAL B 888  ? 0.2086 0.2362 0.2738 0.0289  -0.0136 -0.0262 886  VAL B CG1 
15108 C CG2 . VAL B 888  ? 0.2029 0.2362 0.2735 0.0353  -0.0126 -0.0274 886  VAL B CG2 
15109 N N   . ILE B 889  ? 0.1973 0.2277 0.2605 0.0339  -0.0060 -0.0280 887  ILE B N   
15110 C CA  . ILE B 889  ? 0.1906 0.2213 0.2521 0.0357  -0.0036 -0.0288 887  ILE B CA  
15111 C C   . ILE B 889  ? 0.2131 0.2480 0.2781 0.0399  -0.0029 -0.0297 887  ILE B C   
15112 O O   . ILE B 889  ? 0.1912 0.2237 0.2529 0.0428  -0.0022 -0.0309 887  ILE B O   
15113 C CB  . ILE B 889  ? 0.1750 0.2093 0.2380 0.0331  -0.0009 -0.0279 887  ILE B CB  
15114 C CG1 . ILE B 889  ? 0.2055 0.2393 0.2656 0.0346  0.0014  -0.0286 887  ILE B CG1 
15115 C CG2 . ILE B 889  ? 0.2113 0.2532 0.2815 0.0322  0.0002  -0.0269 887  ILE B CG2 
15116 C CD1 . ILE B 889  ? 0.2077 0.2336 0.2604 0.0346  0.0002  -0.0294 887  ILE B CD1 
15117 N N   . THR B 890  ? 0.2163 0.2578 0.2880 0.0405  -0.0031 -0.0291 888  THR B N   
15118 C CA  . THR B 890  ? 0.2020 0.2493 0.2781 0.0444  -0.0020 -0.0297 888  THR B CA  
15119 C C   . THR B 890  ? 0.2200 0.2710 0.3014 0.0454  -0.0042 -0.0293 888  THR B C   
15120 O O   . THR B 890  ? 0.2062 0.2563 0.2885 0.0424  -0.0062 -0.0284 888  THR B O   
15121 C CB  . THR B 890  ? 0.2222 0.2775 0.3030 0.0439  0.0015  -0.0290 888  THR B CB  
15122 O OG1 . THR B 890  ? 0.2162 0.2756 0.3016 0.0400  0.0015  -0.0274 888  THR B OG1 
15123 C CG2 . THR B 890  ? 0.2049 0.2576 0.2809 0.0434  0.0040  -0.0294 888  THR B CG2 
15124 N N   . SER B 891  ? 0.2614 0.3170 0.3463 0.0496  -0.0039 -0.0299 889  SER B N   
15125 C CA  A SER B 891  ? 0.2243 0.2854 0.3155 0.0506  -0.0058 -0.0294 889  SER B CA  
15126 C CA  B SER B 891  ? 0.2244 0.2853 0.3154 0.0506  -0.0059 -0.0293 889  SER B CA  
15127 C C   . SER B 891  ? 0.2171 0.2857 0.3149 0.0469  -0.0049 -0.0277 889  SER B C   
15128 O O   . SER B 891  ? 0.2560 0.3262 0.3570 0.0453  -0.0073 -0.0269 889  SER B O   
15129 C CB  A SER B 891  ? 0.2190 0.2850 0.3134 0.0561  -0.0050 -0.0303 889  SER B CB  
15130 C CB  B SER B 891  ? 0.2196 0.2849 0.3136 0.0561  -0.0053 -0.0303 889  SER B CB  
15131 O OG  A SER B 891  ? 0.2733 0.3317 0.3616 0.0600  -0.0064 -0.0319 889  SER B OG  
15132 O OG  B SER B 891  ? 0.2289 0.3019 0.3267 0.0571  -0.0016 -0.0302 889  SER B OG  
15133 N N   . GLU B 892  ? 0.2072 0.2803 0.3068 0.0455  -0.0015 -0.0271 890  GLU B N   
15134 C CA  . GLU B 892  ? 0.2441 0.3238 0.3497 0.0417  -0.0007 -0.0254 890  GLU B CA  
15135 C C   . GLU B 892  ? 0.2704 0.3447 0.3733 0.0373  -0.0027 -0.0248 890  GLU B C   
15136 O O   . GLU B 892  ? 0.2617 0.3391 0.3689 0.0349  -0.0043 -0.0238 890  GLU B O   
15137 C CB  . GLU B 892  ? 0.3009 0.3851 0.4076 0.0409  0.0032  -0.0248 890  GLU B CB  
15138 N N   . ALA B 893  ? 0.2472 0.3137 0.3431 0.0363  -0.0027 -0.0254 891  ALA B N   
15139 C CA  . ALA B 893  ? 0.2362 0.2976 0.3292 0.0327  -0.0045 -0.0250 891  ALA B CA  
15140 C C   . ALA B 893  ? 0.2342 0.2933 0.3272 0.0331  -0.0081 -0.0251 891  ALA B C   
15141 O O   . ALA B 893  ? 0.2255 0.2852 0.3203 0.0303  -0.0098 -0.0244 891  ALA B O   
15142 C CB  . ALA B 893  ? 0.2286 0.2825 0.3141 0.0320  -0.0039 -0.0255 891  ALA B CB  
15143 N N   . LYS B 894  ? 0.1976 0.2537 0.2882 0.0366  -0.0095 -0.0261 892  LYS B N   
15144 C CA  . LYS B 894  ? 0.2416 0.2955 0.3320 0.0372  -0.0131 -0.0262 892  LYS B CA  
15145 C C   . LYS B 894  ? 0.2716 0.3331 0.3696 0.0368  -0.0142 -0.0254 892  LYS B C   
15146 O O   . LYS B 894  ? 0.2467 0.3072 0.3451 0.0347  -0.0168 -0.0249 892  LYS B O   
15147 C CB  . LYS B 894  ? 0.2328 0.2827 0.3199 0.0415  -0.0143 -0.0273 892  LYS B CB  
15148 C CG  . LYS B 894  ? 0.2525 0.3004 0.3397 0.0428  -0.0181 -0.0272 892  LYS B CG  
15149 C CD  . LYS B 894  ? 0.2593 0.3019 0.3422 0.0470  -0.0195 -0.0283 892  LYS B CD  
15150 C CE  . LYS B 894  ? 0.2902 0.3310 0.3734 0.0484  -0.0234 -0.0280 892  LYS B CE  
15151 N NZ  . LYS B 894  ? 0.4304 0.4651 0.5090 0.0524  -0.0251 -0.0289 892  LYS B NZ  
15152 N N   . ASP B 895  ? 0.2378 0.3073 0.3418 0.0387  -0.0123 -0.0251 893  ASP B N   
15153 C CA  . ASP B 895  ? 0.2535 0.3311 0.3653 0.0381  -0.0134 -0.0241 893  ASP B CA  
15154 C C   . ASP B 895  ? 0.2485 0.3272 0.3621 0.0331  -0.0135 -0.0230 893  ASP B C   
15155 O O   . ASP B 895  ? 0.2829 0.3636 0.3997 0.0313  -0.0162 -0.0224 893  ASP B O   
15156 C CB  . ASP B 895  ? 0.2574 0.3440 0.3753 0.0409  -0.0107 -0.0239 893  ASP B CB  
15157 C CG  . ASP B 895  ? 0.3211 0.4075 0.4382 0.0465  -0.0111 -0.0251 893  ASP B CG  
15158 O OD1 . ASP B 895  ? 0.3713 0.4514 0.4845 0.0480  -0.0141 -0.0258 893  ASP B OD1 
15159 O OD2 . ASP B 895  ? 0.3411 0.4335 0.4614 0.0494  -0.0084 -0.0253 893  ASP B OD2 
15160 N N   . ASN B 896  ? 0.2405 0.3178 0.3520 0.0308  -0.0109 -0.0227 894  ASN B N   
15161 C CA  . ASN B 896  ? 0.2272 0.3050 0.3400 0.0262  -0.0109 -0.0217 894  ASN B CA  
15162 C C   . ASN B 896  ? 0.2735 0.3443 0.3817 0.0242  -0.0139 -0.0221 894  ASN B C   
15163 O O   . ASN B 896  ? 0.2473 0.3193 0.3579 0.0215  -0.0158 -0.0215 894  ASN B O   
15164 C CB  . ASN B 896  ? 0.2943 0.3711 0.4049 0.0248  -0.0075 -0.0215 894  ASN B CB  
15165 C CG  . ASN B 896  ? 0.4278 0.5034 0.5384 0.0203  -0.0076 -0.0206 894  ASN B CG  
15166 O OD1 . ASN B 896  ? 0.4618 0.5311 0.5679 0.0187  -0.0092 -0.0210 894  ASN B OD1 
15167 N ND2 . ASN B 896  ? 0.5143 0.5957 0.6298 0.0185  -0.0058 -0.0193 894  ASN B ND2 
15168 N N   . ILE B 897  ? 0.2207 0.2843 0.3221 0.0254  -0.0144 -0.0230 895  ILE B N   
15169 C CA  . ILE B 897  ? 0.2999 0.3571 0.3965 0.0237  -0.0170 -0.0233 895  ILE B CA  
15170 C C   . ILE B 897  ? 0.2939 0.3523 0.3928 0.0245  -0.0205 -0.0233 895  ILE B C   
15171 O O   . ILE B 897  ? 0.2879 0.3452 0.3867 0.0221  -0.0228 -0.0230 895  ILE B O   
15172 C CB  . ILE B 897  ? 0.2232 0.2731 0.3124 0.0248  -0.0167 -0.0241 895  ILE B CB  
15173 C CG1 . ILE B 897  ? 0.2324 0.2811 0.3193 0.0236  -0.0135 -0.0240 895  ILE B CG1 
15174 C CG2 . ILE B 897  ? 0.2321 0.2761 0.3164 0.0233  -0.0194 -0.0242 895  ILE B CG2 
15175 C CD1 . ILE B 897  ? 0.2189 0.2625 0.3001 0.0255  -0.0126 -0.0247 895  ILE B CD1 
15176 N N   . GLU B 898  ? 0.2566 0.3170 0.3572 0.0282  -0.0212 -0.0236 896  GLU B N   
15177 C CA  . GLU B 898  ? 0.3118 0.3733 0.4144 0.0293  -0.0247 -0.0235 896  GLU B CA  
15178 C C   . GLU B 898  ? 0.2885 0.3574 0.3984 0.0273  -0.0258 -0.0226 896  GLU B C   
15179 O O   . GLU B 898  ? 0.3076 0.3761 0.4181 0.0263  -0.0291 -0.0224 896  GLU B O   
15180 C CB  . GLU B 898  ? 0.3287 0.3912 0.4320 0.0341  -0.0251 -0.0240 896  GLU B CB  
15181 C CG  . GLU B 898  ? 0.3234 0.3774 0.4189 0.0358  -0.0253 -0.0248 896  GLU B CG  
15182 C CD  . GLU B 898  ? 0.3912 0.4452 0.4870 0.0408  -0.0260 -0.0254 896  GLU B CD  
15183 O OE1 . GLU B 898  ? 0.4525 0.5140 0.5545 0.0433  -0.0249 -0.0254 896  GLU B OE1 
15184 O OE2 . GLU B 898  ? 0.4979 0.5446 0.5877 0.0421  -0.0279 -0.0259 896  GLU B OE2 
15185 N N   . LYS B 899  ? 0.2936 0.3691 0.4089 0.0266  -0.0231 -0.0219 897  LYS B N   
15186 C CA  . LYS B 899  ? 0.2724 0.3548 0.3945 0.0240  -0.0240 -0.0208 897  LYS B CA  
15187 C C   . LYS B 899  ? 0.3233 0.4011 0.4426 0.0197  -0.0258 -0.0207 897  LYS B C   
15188 O O   . LYS B 899  ? 0.2980 0.3778 0.4201 0.0179  -0.0287 -0.0203 897  LYS B O   
15189 C CB  . LYS B 899  ? 0.3371 0.4266 0.4645 0.0236  -0.0205 -0.0200 897  LYS B CB  
15190 C CG  . LYS B 899  ? 0.3210 0.4183 0.4560 0.0206  -0.0213 -0.0185 897  LYS B CG  
15191 C CD  . LYS B 899  ? 0.4159 0.5168 0.5531 0.0186  -0.0176 -0.0175 897  LYS B CD  
15192 C CE  . LYS B 899  ? 0.4546 0.5644 0.6000 0.0158  -0.0179 -0.0158 897  LYS B CE  
15193 N NZ  . LYS B 899  ? 0.4632 0.5754 0.6098 0.0138  -0.0142 -0.0147 897  LYS B NZ  
15194 N N   . HIS B 900  ? 0.2788 0.3505 0.3923 0.0182  -0.0240 -0.0212 898  HIS B N   
15195 C CA  . HIS B 900  ? 0.2842 0.3508 0.3941 0.0147  -0.0255 -0.0213 898  HIS B CA  
15196 C C   . HIS B 900  ? 0.2841 0.3460 0.3900 0.0151  -0.0292 -0.0220 898  HIS B C   
15197 O O   . HIS B 900  ? 0.3528 0.4140 0.4589 0.0127  -0.0318 -0.0219 898  HIS B O   
15198 C CB  . HIS B 900  ? 0.3406 0.4017 0.4448 0.0137  -0.0229 -0.0217 898  HIS B CB  
15199 C CG  . HIS B 900  ? 0.3296 0.3847 0.4289 0.0111  -0.0244 -0.0222 898  HIS B CG  
15200 N ND1 . HIS B 900  ? 0.3648 0.4204 0.4658 0.0079  -0.0250 -0.0218 898  HIS B ND1 
15201 C CD2 . HIS B 900  ? 0.3267 0.3752 0.4192 0.0113  -0.0253 -0.0230 898  HIS B CD2 
15202 C CE1 . HIS B 900  ? 0.3364 0.3857 0.4317 0.0066  -0.0262 -0.0226 898  HIS B CE1 
15203 N NE2 . HIS B 900  ? 0.3194 0.3648 0.4096 0.0086  -0.0263 -0.0232 898  HIS B NE2 
15204 N N   . ILE B 901  ? 0.2790 0.3374 0.3809 0.0180  -0.0294 -0.0225 899  ILE B N   
15205 C CA  . ILE B 901  ? 0.2707 0.3241 0.3679 0.0184  -0.0327 -0.0229 899  ILE B CA  
15206 C C   . ILE B 901  ? 0.4127 0.4707 0.5150 0.0186  -0.0361 -0.0225 899  ILE B C   
15207 O O   . ILE B 901  ? 0.3955 0.4510 0.4958 0.0169  -0.0392 -0.0226 899  ILE B O   
15208 C CB  . ILE B 901  ? 0.3021 0.3510 0.3945 0.0214  -0.0323 -0.0234 899  ILE B CB  
15209 C CG1 . ILE B 901  ? 0.2523 0.2964 0.3392 0.0206  -0.0294 -0.0237 899  ILE B CG1 
15210 C CG2 . ILE B 901  ? 0.3043 0.3487 0.3925 0.0221  -0.0360 -0.0235 899  ILE B CG2 
15211 C CD1 . ILE B 901  ? 0.2709 0.3098 0.3524 0.0229  -0.0293 -0.0241 899  ILE B CD1 
15212 N N   . GLU B 902  ? 0.3609 0.4259 0.4698 0.0209  -0.0356 -0.0220 900  GLU B N   
15213 C CA  . GLU B 902  ? 0.3625 0.4331 0.4771 0.0213  -0.0388 -0.0214 900  GLU B CA  
15214 C C   . GLU B 902  ? 0.3534 0.4272 0.4717 0.0171  -0.0401 -0.0208 900  GLU B C   
15215 O O   . GLU B 902  ? 0.4345 0.5091 0.5541 0.0159  -0.0438 -0.0206 900  GLU B O   
15216 C CB  . GLU B 902  ? 0.3716 0.4499 0.4928 0.0249  -0.0376 -0.0210 900  GLU B CB  
15217 C CG  . GLU B 902  ? 0.4254 0.4999 0.5428 0.0293  -0.0378 -0.0216 900  GLU B CG  
15218 C CD  . GLU B 902  ? 0.4784 0.5466 0.5905 0.0296  -0.0417 -0.0219 900  GLU B CD  
15219 O OE1 . GLU B 902  ? 0.5757 0.6471 0.6912 0.0290  -0.0451 -0.0213 900  GLU B OE1 
15220 O OE2 . GLU B 902  ? 0.4791 0.5393 0.5837 0.0303  -0.0415 -0.0225 900  GLU B OE2 
15221 N N   . ARG B 903  ? 0.3349 0.4103 0.4549 0.0147  -0.0372 -0.0205 901  ARG B N   
15222 C CA  . ARG B 903  ? 0.3907 0.4675 0.5131 0.0105  -0.0385 -0.0199 901  ARG B CA  
15223 C C   . ARG B 903  ? 0.4544 0.5231 0.5698 0.0083  -0.0411 -0.0209 901  ARG B C   
15224 O O   . ARG B 903  ? 0.4957 0.5649 0.6124 0.0060  -0.0445 -0.0207 901  ARG B O   
15225 C CB  . ARG B 903  ? 0.4245 0.5029 0.5486 0.0085  -0.0349 -0.0194 901  ARG B CB  
15226 C CG  . ARG B 903  ? 0.4889 0.5686 0.6158 0.0039  -0.0363 -0.0187 901  ARG B CG  
15227 C CD  . ARG B 903  ? 0.5444 0.6213 0.6692 0.0017  -0.0332 -0.0185 901  ARG B CD  
15228 N NE  . ARG B 903  ? 0.6362 0.7128 0.7626 -0.0027 -0.0350 -0.0179 901  ARG B NE  
15229 C CZ  . ARG B 903  ? 0.7032 0.7869 0.8369 -0.0051 -0.0351 -0.0163 901  ARG B CZ  
15230 N NH1 . ARG B 903  ? 0.7144 0.8067 0.8546 -0.0034 -0.0329 -0.0152 901  ARG B NH1 
15231 N NH2 . ARG B 903  ? 0.6144 0.6965 0.7486 -0.0093 -0.0374 -0.0159 901  ARG B NH2 
15232 N N   . MET B 904  ? 0.4430 0.5043 0.5508 0.0091  -0.0396 -0.0218 902  MET B N   
15233 C CA  . MET B 904  ? 0.4271 0.4811 0.5279 0.0075  -0.0418 -0.0227 902  MET B CA  
15234 C C   . MET B 904  ? 0.4501 0.5035 0.5499 0.0086  -0.0458 -0.0228 902  MET B C   
15235 O O   . MET B 904  ? 0.4631 0.5145 0.5613 0.0065  -0.0490 -0.0231 902  MET B O   
15236 C CB  . MET B 904  ? 0.3902 0.4377 0.4837 0.0084  -0.0393 -0.0234 902  MET B CB  
15237 C CG  . MET B 904  ? 0.3991 0.4462 0.4925 0.0071  -0.0357 -0.0234 902  MET B CG  
15238 S SD  . MET B 904  ? 0.5260 0.5718 0.6198 0.0030  -0.0367 -0.0235 902  MET B SD  
15239 C CE  . MET B 904  ? 0.5037 0.5582 0.6072 0.0019  -0.0355 -0.0221 902  MET B CE  
15240 N N   . ARG B 905  ? 0.4439 0.4983 0.5441 0.0121  -0.0459 -0.0226 903  ARG B N   
15241 C CA  . ARG B 905  ? 0.4881 0.5422 0.5876 0.0135  -0.0498 -0.0225 903  ARG B CA  
15242 C C   . ARG B 905  ? 0.5078 0.5685 0.6143 0.0121  -0.0528 -0.0218 903  ARG B C   
15243 O O   . ARG B 905  ? 0.5157 0.5747 0.6205 0.0110  -0.0567 -0.0219 903  ARG B O   
15244 C CB  . ARG B 905  ? 0.4784 0.5330 0.5781 0.0177  -0.0492 -0.0223 903  ARG B CB  
15245 C CG  . ARG B 905  ? 0.5342 0.5820 0.6266 0.0191  -0.0515 -0.0225 903  ARG B CG  
15246 C CD  . ARG B 905  ? 0.5974 0.6460 0.6908 0.0233  -0.0520 -0.0222 903  ARG B CD  
15247 N NE  . ARG B 905  ? 0.5034 0.5503 0.5952 0.0252  -0.0483 -0.0225 903  ARG B NE  
15248 C CZ  . ARG B 905  ? 0.4580 0.4978 0.5426 0.0262  -0.0478 -0.0227 903  ARG B CZ  
15249 N NH1 . ARG B 905  ? 0.5677 0.6015 0.6459 0.0253  -0.0504 -0.0226 903  ARG B NH1 
15250 N NH2 . ARG B 905  ? 0.5003 0.5391 0.5840 0.0280  -0.0448 -0.0230 903  ARG B NH2 
15251 N N   . GLY B 906  ? 0.4899 0.5584 0.6044 0.0120  -0.0512 -0.0210 904  GLY B N   
15252 C CA  . GLY B 906  ? 0.5207 0.5964 0.6427 0.0103  -0.0539 -0.0200 904  GLY B CA  
15253 C C   . GLY B 906  ? 0.5779 0.6510 0.6984 0.0056  -0.0560 -0.0202 904  GLY B C   
15254 O O   . GLY B 906  ? 0.5110 0.5879 0.6355 0.0039  -0.0597 -0.0197 904  GLY B O   
15255 N N   . LEU B 907  ? 0.5451 0.6117 0.6597 0.0037  -0.0540 -0.0211 905  LEU B N   
15256 C CA  . LEU B 907  ? 0.5272 0.5899 0.6391 -0.0003 -0.0560 -0.0216 905  LEU B CA  
15257 C C   . LEU B 907  ? 0.5483 0.6034 0.6522 -0.0005 -0.0591 -0.0228 905  LEU B C   
15258 O O   . LEU B 907  ? 0.6347 0.6857 0.7353 -0.0036 -0.0611 -0.0235 905  LEU B O   
15259 C CB  . LEU B 907  ? 0.4605 0.5199 0.5701 -0.0020 -0.0523 -0.0219 905  LEU B CB  
15260 N N   . GLY B 908  ? 0.5590 0.6118 0.6591 0.0026  -0.0596 -0.0230 906  GLY B N   
15261 C CA  . GLY B 908  ? 0.5141 0.5603 0.6066 0.0025  -0.0626 -0.0238 906  GLY B CA  
15262 C C   . GLY B 908  ? 0.5795 0.6180 0.6631 0.0033  -0.0601 -0.0248 906  GLY B C   
15263 O O   . GLY B 908  ? 0.4989 0.5322 0.5757 0.0036  -0.0622 -0.0253 906  GLY B O   
15264 N N   . ARG B 909  ? 0.5384 0.5764 0.6218 0.0036  -0.0559 -0.0249 907  ARG B N   
15265 C CA  . ARG B 909  ? 0.4481 0.4795 0.5236 0.0041  -0.0535 -0.0257 907  ARG B CA  
15266 C C   . ARG B 909  ? 0.4751 0.5043 0.5468 0.0069  -0.0536 -0.0254 907  ARG B C   
15267 O O   . ARG B 909  ? 0.5409 0.5739 0.6168 0.0091  -0.0538 -0.0246 907  ARG B O   
15268 C CB  . ARG B 909  ? 0.4428 0.4751 0.5199 0.0038  -0.0491 -0.0257 907  ARG B CB  
15269 N N   . LYS B 910  ? 0.4202 0.4432 0.4836 0.0067  -0.0535 -0.0260 908  LYS B N   
15270 C CA  . LYS B 910  ? 0.4588 0.4789 0.5178 0.0089  -0.0537 -0.0255 908  LYS B CA  
15271 C C   . LYS B 910  ? 0.5427 0.5631 0.6022 0.0104  -0.0498 -0.0251 908  LYS B C   
15272 O O   . LYS B 910  ? 0.4752 0.4944 0.5331 0.0095  -0.0467 -0.0255 908  LYS B O   
15273 C CB  . LYS B 910  ? 0.4409 0.4549 0.4910 0.0079  -0.0547 -0.0260 908  LYS B CB  
15274 N N   . VAL B 911  ? 0.5199 0.5415 0.5812 0.0129  -0.0502 -0.0244 909  VAL B N   
15275 C CA  . VAL B 911  ? 0.4381 0.4602 0.5003 0.0146  -0.0470 -0.0241 909  VAL B CA  
15276 C C   . VAL B 911  ? 0.4457 0.4629 0.5022 0.0162  -0.0478 -0.0236 909  VAL B C   
15277 O O   . VAL B 911  ? 0.5425 0.5597 0.5996 0.0180  -0.0506 -0.0231 909  VAL B O   
15278 C CB  . VAL B 911  ? 0.4571 0.4856 0.5276 0.0164  -0.0465 -0.0238 909  VAL B CB  
15279 C CG1 . VAL B 911  ? 0.4260 0.4543 0.4966 0.0184  -0.0433 -0.0237 909  VAL B CG1 
15280 C CG2 . VAL B 911  ? 0.4176 0.4509 0.4937 0.0144  -0.0458 -0.0240 909  VAL B CG2 
15281 N N   . GLU B 912  ? 0.4356 0.4489 0.4866 0.0155  -0.0455 -0.0236 910  GLU B N   
15282 C CA  . GLU B 912  ? 0.3795 0.3880 0.4250 0.0166  -0.0458 -0.0228 910  GLU B CA  
15283 C C   . GLU B 912  ? 0.4845 0.4937 0.5320 0.0183  -0.0432 -0.0228 910  GLU B C   
15284 O O   . GLU B 912  ? 0.3842 0.3957 0.4341 0.0176  -0.0401 -0.0232 910  GLU B O   
15285 C CB  . GLU B 912  ? 0.4632 0.4673 0.5013 0.0145  -0.0450 -0.0227 910  GLU B CB  
15286 C CG  . GLU B 912  ? 0.4562 0.4552 0.4881 0.0149  -0.0455 -0.0216 910  GLU B CG  
15287 C CD  . GLU B 912  ? 0.5132 0.5090 0.5408 0.0150  -0.0493 -0.0209 910  GLU B CD  
15288 O OE1 . GLU B 912  ? 0.4651 0.4626 0.4941 0.0146  -0.0515 -0.0213 910  GLU B OE1 
15289 O OE2 . GLU B 912  ? 0.5200 0.5115 0.5428 0.0153  -0.0503 -0.0198 910  GLU B OE2 
15290 N N   . GLN B 913  ? 0.4163 0.4233 0.4628 0.0206  -0.0446 -0.0222 911  GLN B N   
15291 C CA  . GLN B 913  ? 0.3894 0.3961 0.4369 0.0224  -0.0425 -0.0223 911  GLN B CA  
15292 C C   . GLN B 913  ? 0.4468 0.4470 0.4880 0.0233  -0.0439 -0.0215 911  GLN B C   
15293 O O   . GLN B 913  ? 0.4683 0.4657 0.5070 0.0240  -0.0472 -0.0209 911  GLN B O   
15294 C CB  . GLN B 913  ? 0.3774 0.3894 0.4322 0.0252  -0.0426 -0.0227 911  GLN B CB  
15295 C CG  . GLN B 913  ? 0.3821 0.4006 0.4432 0.0242  -0.0405 -0.0233 911  GLN B CG  
15296 C CD  . GLN B 913  ? 0.4033 0.4274 0.4714 0.0270  -0.0396 -0.0236 911  GLN B CD  
15297 O OE1 . GLN B 913  ? 0.4198 0.4458 0.4907 0.0294  -0.0420 -0.0234 911  GLN B OE1 
15298 N NE2 . GLN B 913  ? 0.3322 0.3594 0.4031 0.0268  -0.0362 -0.0239 911  GLN B NE2 
15299 N N   . ILE B 914  ? 0.4272 0.4249 0.4658 0.0231  -0.0416 -0.0215 912  ILE B N   
15300 C CA  . ILE B 914  ? 0.3778 0.3692 0.4110 0.0240  -0.0429 -0.0208 912  ILE B CA  
15301 C C   . ILE B 914  ? 0.4931 0.4846 0.5293 0.0280  -0.0444 -0.0212 912  ILE B C   
15302 O O   . ILE B 914  ? 0.4023 0.3992 0.4448 0.0299  -0.0429 -0.0221 912  ILE B O   
15303 C CB  . ILE B 914  ? 0.4583 0.4472 0.4881 0.0225  -0.0401 -0.0207 912  ILE B CB  
15304 N N   . GLY B 915  ? 0.5160 0.5018 0.5479 0.0293  -0.0474 -0.0204 913  GLY B N   
15305 C CA  . GLY B 915  ? 0.4709 0.4558 0.5047 0.0335  -0.0489 -0.0209 913  GLY B CA  
15306 C C   . GLY B 915  ? 0.4870 0.4685 0.5187 0.0346  -0.0469 -0.0215 913  GLY B C   
15307 O O   . GLY B 915  ? 0.5319 0.5080 0.5576 0.0322  -0.0464 -0.0208 913  GLY B O   
15308 N N   . LEU B 916  ? 0.4233 0.4084 0.4599 0.0381  -0.0457 -0.0227 914  LEU B N   
15309 C CA  . LEU B 916  ? 0.4490 0.4311 0.4836 0.0394  -0.0437 -0.0235 914  LEU B CA  
15310 C C   . LEU B 916  ? 0.4626 0.4382 0.4937 0.0432  -0.0464 -0.0237 914  LEU B C   
15311 O O   . LEU B 916  ? 0.4483 0.4249 0.4818 0.0463  -0.0489 -0.0237 914  LEU B O   
15312 C CB  . LEU B 916  ? 0.3838 0.3736 0.4252 0.0411  -0.0404 -0.0248 914  LEU B CB  
15313 C CG  . LEU B 916  ? 0.4026 0.3983 0.4474 0.0376  -0.0375 -0.0247 914  LEU B CG  
15314 C CD1 . LEU B 916  ? 0.3924 0.3941 0.4424 0.0392  -0.0342 -0.0258 914  LEU B CD1 
15315 C CD2 . LEU B 916  ? 0.4044 0.3955 0.4432 0.0336  -0.0366 -0.0240 914  LEU B CD2 
15316 N N   . ALA B 917  ? 0.4425 0.4110 0.4676 0.0428  -0.0461 -0.0238 915  ALA B N   
15317 C CA  . ALA B 917  ? 0.4685 0.4293 0.4892 0.0463  -0.0487 -0.0241 915  ALA B CA  
15318 C C   . ALA B 917  ? 0.4817 0.4466 0.5075 0.0517  -0.0476 -0.0259 915  ALA B C   
15319 O O   . ALA B 917  ? 0.3827 0.3551 0.4141 0.0521  -0.0443 -0.0269 915  ALA B O   
15320 C CB  . ALA B 917  ? 0.4859 0.4382 0.4989 0.0441  -0.0486 -0.0238 915  ALA B CB  
15321 N N   . SER B 918  ? 0.4308 0.3905 0.4545 0.0560  -0.0505 -0.0262 916  SER B N   
15322 C CA  . SER B 918  ? 0.4657 0.4288 0.4936 0.0619  -0.0497 -0.0280 916  SER B CA  
15323 C C   . SER B 918  ? 0.4599 0.4226 0.4866 0.0625  -0.0463 -0.0296 916  SER B C   
15324 O O   . SER B 918  ? 0.4299 0.3996 0.4623 0.0658  -0.0438 -0.0309 916  SER B O   
15325 C CB  . SER B 918  ? 0.4858 0.4414 0.5099 0.0664  -0.0536 -0.0281 916  SER B CB  
15326 O OG  . SER B 918  ? 0.5527 0.4965 0.5676 0.0652  -0.0551 -0.0279 916  SER B OG  
15327 N N   . GLU B 919  ? 0.4373 0.3923 0.4569 0.0592  -0.0462 -0.0293 917  GLU B N   
15328 C CA  . GLU B 919  ? 0.4847 0.4381 0.5022 0.0597  -0.0435 -0.0307 917  GLU B CA  
15329 C C   . GLU B 919  ? 0.4794 0.4429 0.5031 0.0579  -0.0392 -0.0311 917  GLU B C   
15330 O O   . GLU B 919  ? 0.4519 0.4162 0.4754 0.0592  -0.0366 -0.0325 917  GLU B O   
15331 C CB  . GLU B 919  ? 0.4684 0.4118 0.4771 0.0557  -0.0447 -0.0300 917  GLU B CB  
15332 N N   . THR B 920  ? 0.4012 0.3719 0.4300 0.0549  -0.0385 -0.0299 918  THR B N   
15333 C CA  . THR B 920  ? 0.3775 0.3575 0.4123 0.0533  -0.0347 -0.0302 918  THR B CA  
15334 C C   . THR B 920  ? 0.3617 0.3498 0.4036 0.0578  -0.0329 -0.0314 918  THR B C   
15335 O O   . THR B 920  ? 0.3465 0.3414 0.3926 0.0571  -0.0295 -0.0318 918  THR B O   
15336 C CB  . THR B 920  ? 0.3663 0.3509 0.4042 0.0490  -0.0347 -0.0287 918  THR B CB  
15337 O OG1 . THR B 920  ? 0.3526 0.3404 0.3945 0.0508  -0.0371 -0.0282 918  THR B OG1 
15338 C CG2 . THR B 920  ? 0.3373 0.3151 0.3685 0.0444  -0.0360 -0.0274 918  THR B CG2 
15339 N N   . GLY B 921  ? 0.3389 0.3267 0.3823 0.0625  -0.0351 -0.0319 919  GLY B N   
15340 C CA  . GLY B 921  ? 0.3513 0.3480 0.4021 0.0669  -0.0334 -0.0328 919  GLY B CA  
15341 C C   . GLY B 921  ? 0.3506 0.3490 0.4012 0.0695  -0.0300 -0.0345 919  GLY B C   
15342 O O   . GLY B 921  ? 0.3600 0.3678 0.4175 0.0718  -0.0275 -0.0350 919  GLY B O   
15343 N N   . VAL B 922  ? 0.2929 0.2824 0.3358 0.0691  -0.0299 -0.0353 920  VAL B N   
15344 C CA  . VAL B 922  ? 0.3058 0.2962 0.3477 0.0715  -0.0268 -0.0370 920  VAL B CA  
15345 C C   . VAL B 922  ? 0.2956 0.2913 0.3395 0.0673  -0.0232 -0.0365 920  VAL B C   
15346 O O   . VAL B 922  ? 0.2870 0.2852 0.3310 0.0689  -0.0203 -0.0377 920  VAL B O   
15347 C CB  . VAL B 922  ? 0.3422 0.3203 0.3745 0.0730  -0.0285 -0.0382 920  VAL B CB  
15348 C CG1 . VAL B 922  ? 0.3698 0.3429 0.4003 0.0787  -0.0317 -0.0391 920  VAL B CG1 
15349 C CG2 . VAL B 922  ? 0.3541 0.3243 0.3801 0.0672  -0.0304 -0.0368 920  VAL B CG2 
15350 N N   . GLY B 923  ? 0.2461 0.2434 0.2913 0.0620  -0.0235 -0.0348 921  GLY B N   
15351 C CA  . GLY B 923  ? 0.2716 0.2740 0.3191 0.0580  -0.0203 -0.0342 921  GLY B CA  
15352 C C   . GLY B 923  ? 0.2730 0.2845 0.3283 0.0560  -0.0197 -0.0329 921  GLY B C   
15353 O O   . GLY B 923  ? 0.2690 0.2840 0.3286 0.0582  -0.0214 -0.0327 921  GLY B O   
15354 N N   . THR B 924  ? 0.2404 0.2556 0.2974 0.0519  -0.0175 -0.0321 922  THR B N   
15355 C CA  . THR B 924  ? 0.2292 0.2523 0.2931 0.0496  -0.0170 -0.0309 922  THR B CA  
15356 C C   . THR B 924  ? 0.2293 0.2487 0.2904 0.0448  -0.0184 -0.0297 922  THR B C   
15357 O O   . THR B 924  ? 0.2549 0.2739 0.3143 0.0416  -0.0166 -0.0293 922  THR B O   
15358 C CB  . THR B 924  ? 0.2120 0.2428 0.2806 0.0490  -0.0132 -0.0308 922  THR B CB  
15359 O OG1 . THR B 924  ? 0.2549 0.2819 0.3186 0.0469  -0.0113 -0.0310 922  THR B OG1 
15360 C CG2 . THR B 924  ? 0.2040 0.2398 0.2761 0.0540  -0.0117 -0.0319 922  THR B CG2 
15361 N N   . PHE B 925  ? 0.2315 0.2485 0.2919 0.0446  -0.0216 -0.0291 923  PHE B N   
15362 C CA  . PHE B 925  ? 0.2276 0.2411 0.2849 0.0404  -0.0230 -0.0281 923  PHE B CA  
15363 C C   . PHE B 925  ? 0.2206 0.2399 0.2835 0.0388  -0.0238 -0.0273 923  PHE B C   
15364 O O   . PHE B 925  ? 0.2273 0.2510 0.2950 0.0412  -0.0250 -0.0274 923  PHE B O   
15365 C CB  . PHE B 925  ? 0.2450 0.2499 0.2958 0.0407  -0.0262 -0.0279 923  PHE B CB  
15366 C CG  . PHE B 925  ? 0.2680 0.2659 0.3123 0.0412  -0.0258 -0.0285 923  PHE B CG  
15367 C CD1 . PHE B 925  ? 0.2483 0.2443 0.2916 0.0454  -0.0257 -0.0297 923  PHE B CD1 
15368 C CD2 . PHE B 925  ? 0.2428 0.2362 0.2819 0.0374  -0.0255 -0.0277 923  PHE B CD2 
15369 C CE1 . PHE B 925  ? 0.2822 0.2710 0.3190 0.0456  -0.0257 -0.0304 923  PHE B CE1 
15370 C CE2 . PHE B 925  ? 0.2538 0.2408 0.2870 0.0374  -0.0255 -0.0282 923  PHE B CE2 
15371 C CZ  . PHE B 925  ? 0.2759 0.2602 0.3077 0.0414  -0.0256 -0.0295 923  PHE B CZ  
15372 N N   . VAL B 926  ? 0.2220 0.2412 0.2840 0.0349  -0.0233 -0.0266 924  VAL B N   
15373 C CA  . VAL B 926  ? 0.2434 0.2654 0.3082 0.0328  -0.0249 -0.0259 924  VAL B CA  
15374 C C   . VAL B 926  ? 0.2533 0.2690 0.3119 0.0304  -0.0268 -0.0253 924  VAL B C   
15375 O O   . VAL B 926  ? 0.2334 0.2459 0.2878 0.0283  -0.0254 -0.0251 924  VAL B O   
15376 C CB  . VAL B 926  ? 0.2191 0.2469 0.2884 0.0303  -0.0225 -0.0256 924  VAL B CB  
15377 C CG1 . VAL B 926  ? 0.2325 0.2620 0.3038 0.0282  -0.0245 -0.0250 924  VAL B CG1 
15378 C CG2 . VAL B 926  ? 0.2085 0.2433 0.2841 0.0324  -0.0204 -0.0259 924  VAL B CG2 
15379 N N   . PRO B 927  ? 0.2668 0.2807 0.3245 0.0306  -0.0299 -0.0249 925  PRO B N   
15380 C CA  . PRO B 927  ? 0.2832 0.2915 0.3347 0.0282  -0.0316 -0.0242 925  PRO B CA  
15381 C C   . PRO B 927  ? 0.2733 0.2836 0.3250 0.0247  -0.0302 -0.0239 925  PRO B C   
15382 O O   . PRO B 927  ? 0.2402 0.2557 0.2971 0.0241  -0.0297 -0.0241 925  PRO B O   
15383 C CB  . PRO B 927  ? 0.3235 0.3308 0.3752 0.0295  -0.0353 -0.0238 925  PRO B CB  
15384 C CG  . PRO B 927  ? 0.2862 0.3008 0.3456 0.0312  -0.0352 -0.0242 925  PRO B CG  
15385 C CD  . PRO B 927  ? 0.2691 0.2867 0.3315 0.0330  -0.0321 -0.0249 925  PRO B CD  
15386 N N   . PRO B 928  ? 0.2868 0.2930 0.3330 0.0224  -0.0297 -0.0234 926  PRO B N   
15387 C CA  . PRO B 928  ? 0.3007 0.3080 0.3462 0.0195  -0.0288 -0.0232 926  PRO B CA  
15388 C C   . PRO B 928  ? 0.3001 0.3091 0.3475 0.0192  -0.0312 -0.0232 926  PRO B C   
15389 O O   . PRO B 928  ? 0.3433 0.3500 0.3890 0.0201  -0.0341 -0.0229 926  PRO B O   
15390 C CB  . PRO B 928  ? 0.2880 0.2902 0.3265 0.0177  -0.0289 -0.0224 926  PRO B CB  
15391 C CG  . PRO B 928  ? 0.3952 0.3948 0.4321 0.0190  -0.0283 -0.0224 926  PRO B CG  
15392 C CD  . PRO B 928  ? 0.2863 0.2866 0.3265 0.0223  -0.0298 -0.0230 926  PRO B CD  
15393 N N   . THR B 929  ? 0.2829 0.2959 0.3339 0.0179  -0.0301 -0.0236 927  THR B N   
15394 C CA  . THR B 929  ? 0.2931 0.3084 0.3470 0.0175  -0.0323 -0.0238 927  THR B CA  
15395 C C   . THR B 929  ? 0.3494 0.3643 0.4014 0.0149  -0.0317 -0.0240 927  THR B C   
15396 O O   . THR B 929  ? 0.2911 0.3066 0.3430 0.0138  -0.0291 -0.0242 927  THR B O   
15397 C CB  . THR B 929  ? 0.2896 0.3108 0.3511 0.0187  -0.0317 -0.0240 927  THR B CB  
15398 O OG1 . THR B 929  ? 0.2857 0.3072 0.3485 0.0217  -0.0322 -0.0240 927  THR B OG1 
15399 C CG2 . THR B 929  ? 0.3160 0.3402 0.3810 0.0179  -0.0341 -0.0241 927  THR B CG2 
15400 N N   . ILE B 930  ? 0.3050 0.3186 0.3551 0.0141  -0.0344 -0.0240 928  ILE B N   
15401 C CA  . ILE B 930  ? 0.3676 0.3804 0.4155 0.0120  -0.0343 -0.0245 928  ILE B CA  
15402 C C   . ILE B 930  ? 0.3812 0.3967 0.4334 0.0115  -0.0366 -0.0249 928  ILE B C   
15403 O O   . ILE B 930  ? 0.4188 0.4345 0.4717 0.0123  -0.0395 -0.0247 928  ILE B O   
15404 C CB  . ILE B 930  ? 0.3225 0.3307 0.3630 0.0111  -0.0352 -0.0243 928  ILE B CB  
15405 C CG1 . ILE B 930  ? 0.3380 0.3441 0.3747 0.0111  -0.0330 -0.0236 928  ILE B CG1 
15406 C CG2 . ILE B 930  ? 0.3758 0.3832 0.4139 0.0094  -0.0353 -0.0250 928  ILE B CG2 
15407 C CD1 . ILE B 930  ? 0.3350 0.3370 0.3646 0.0103  -0.0340 -0.0229 928  ILE B CD1 
15408 N N   . ILE B 931  ? 0.3263 0.3440 0.3814 0.0101  -0.0354 -0.0254 929  ILE B N   
15409 C CA  . ILE B 931  ? 0.3409 0.3613 0.4004 0.0092  -0.0376 -0.0257 929  ILE B CA  
15410 C C   . ILE B 931  ? 0.4120 0.4294 0.4677 0.0071  -0.0379 -0.0266 929  ILE B C   
15411 O O   . ILE B 931  ? 0.3348 0.3516 0.3898 0.0063  -0.0354 -0.0269 929  ILE B O   
15412 C CB  . ILE B 931  ? 0.3586 0.3844 0.4256 0.0092  -0.0361 -0.0254 929  ILE B CB  
15413 C CG1 . ILE B 931  ? 0.3472 0.3759 0.4174 0.0118  -0.0355 -0.0248 929  ILE B CG1 
15414 C CG2 . ILE B 931  ? 0.3623 0.3911 0.4339 0.0077  -0.0386 -0.0255 929  ILE B CG2 
15415 C CD1 . ILE B 931  ? 0.3446 0.3793 0.4222 0.0121  -0.0339 -0.0244 929  ILE B CD1 
15416 N N   . GLU B 932  ? 0.3822 0.3978 0.4355 0.0064  -0.0412 -0.0270 930  GLU B N   
15417 C CA  . GLU B 932  ? 0.4005 0.4127 0.4496 0.0047  -0.0419 -0.0280 930  GLU B CA  
15418 C C   . GLU B 932  ? 0.3974 0.4120 0.4517 0.0030  -0.0430 -0.0284 930  GLU B C   
15419 O O   . GLU B 932  ? 0.4497 0.4672 0.5082 0.0026  -0.0458 -0.0280 930  GLU B O   
15420 C CB  . GLU B 932  ? 0.3773 0.3861 0.4205 0.0047  -0.0448 -0.0283 930  GLU B CB  
15421 C CG  . GLU B 932  ? 0.4872 0.4935 0.5251 0.0060  -0.0436 -0.0277 930  GLU B CG  
15422 C CD  . GLU B 932  ? 0.5425 0.5455 0.5744 0.0059  -0.0464 -0.0277 930  GLU B CD  
15423 O OE1 . GLU B 932  ? 0.5023 0.5032 0.5310 0.0048  -0.0481 -0.0287 930  GLU B OE1 
15424 O OE2 . GLU B 932  ? 0.5420 0.5442 0.5720 0.0070  -0.0471 -0.0266 930  GLU B OE2 
15425 N N   . LEU B 933  ? 0.4088 0.4223 0.4628 0.0019  -0.0410 -0.0289 931  LEU B N   
15426 C CA  . LEU B 933  ? 0.4041 0.4191 0.4626 -0.0001 -0.0419 -0.0291 931  LEU B CA  
15427 C C   . LEU B 933  ? 0.4992 0.5095 0.5530 -0.0017 -0.0444 -0.0304 931  LEU B C   
15428 O O   . LEU B 933  ? 0.5124 0.5182 0.5591 -0.0011 -0.0447 -0.0314 931  LEU B O   
15429 C CB  . LEU B 933  ? 0.4367 0.4529 0.4977 -0.0004 -0.0384 -0.0287 931  LEU B CB  
15430 C CG  . LEU B 933  ? 0.4137 0.4342 0.4789 0.0012  -0.0356 -0.0276 931  LEU B CG  
15431 C CD1 . LEU B 933  ? 0.4501 0.4711 0.5171 0.0005  -0.0325 -0.0273 931  LEU B CD1 
15432 C CD2 . LEU B 933  ? 0.4383 0.4643 0.5101 0.0015  -0.0371 -0.0267 931  LEU B CD2 
15433 N N   . GLU B 934  ? 0.5171 0.5283 0.5747 -0.0039 -0.0462 -0.0305 932  GLU B N   
15434 C CA  . GLU B 934  ? 0.5336 0.5398 0.5871 -0.0057 -0.0487 -0.0319 932  GLU B CA  
15435 C C   . GLU B 934  ? 0.5875 0.5903 0.6391 -0.0063 -0.0462 -0.0325 932  GLU B C   
15436 O O   . GLU B 934  ? 0.6576 0.6549 0.7022 -0.0056 -0.0458 -0.0340 932  GLU B O   
15437 C CB  . GLU B 934  ? 0.6052 0.6139 0.6637 -0.0082 -0.0525 -0.0315 932  GLU B CB  
15438 N N   . LYS B 935  ? 0.6100 0.6162 0.6676 -0.0073 -0.0445 -0.0314 933  LYS B N   
15439 C CA  . LYS B 935  ? 0.6203 0.6237 0.6767 -0.0076 -0.0421 -0.0316 933  LYS B CA  
15440 C C   . LYS B 935  ? 0.5706 0.5784 0.6310 -0.0063 -0.0382 -0.0302 933  LYS B C   
15441 O O   . LYS B 935  ? 0.5891 0.6026 0.6548 -0.0058 -0.0378 -0.0290 933  LYS B O   
15442 C CB  . LYS B 935  ? 0.6417 0.6439 0.7010 -0.0107 -0.0441 -0.0315 933  LYS B CB  
15443 N N   . LEU B 936  ? 0.5634 0.5685 0.6211 -0.0055 -0.0353 -0.0305 934  LEU B N   
15444 C CA  . LEU B 936  ? 0.5886 0.5976 0.6498 -0.0045 -0.0318 -0.0292 934  LEU B CA  
15445 C C   . LEU B 936  ? 0.6301 0.6439 0.6988 -0.0064 -0.0317 -0.0276 934  LEU B C   
15446 O O   . LEU B 936  ? 0.5898 0.6084 0.6625 -0.0055 -0.0293 -0.0264 934  LEU B O   
15447 C CB  . LEU B 936  ? 0.5638 0.5690 0.6207 -0.0035 -0.0291 -0.0297 934  LEU B CB  
15448 C CG  . LEU B 936  ? 0.5807 0.5883 0.6375 -0.0014 -0.0255 -0.0289 934  LEU B CG  
15449 C CD1 . LEU B 936  ? 0.4946 0.4980 0.5451 0.0001  -0.0239 -0.0299 934  LEU B CD1 
15450 C CD2 . LEU B 936  ? 0.5064 0.5178 0.5687 -0.0021 -0.0234 -0.0274 934  LEU B CD2 
15451 N N   . SER B 937  ? 0.6488 0.6615 0.7193 -0.0091 -0.0343 -0.0276 935  SER B N   
15452 C CA  . SER B 937  ? 0.6560 0.6739 0.7340 -0.0113 -0.0345 -0.0259 935  SER B CA  
15453 C C   . SER B 937  ? 0.5671 0.5921 0.6508 -0.0109 -0.0354 -0.0250 935  SER B C   
15454 O O   . SER B 937  ? 0.5937 0.6246 0.6842 -0.0122 -0.0349 -0.0234 935  SER B O   
15455 C CB  . SER B 937  ? 0.6866 0.7010 0.7646 -0.0147 -0.0376 -0.0261 935  SER B CB  
15456 N N   . ASP B 938  ? 0.5930 0.6178 0.6743 -0.0090 -0.0366 -0.0258 936  ASP B N   
15457 C CA  . ASP B 938  ? 0.5786 0.6098 0.6648 -0.0078 -0.0371 -0.0249 936  ASP B CA  
15458 C C   . ASP B 938  ? 0.5879 0.6235 0.6770 -0.0056 -0.0334 -0.0240 936  ASP B C   
15459 O O   . ASP B 938  ? 0.5186 0.5603 0.6130 -0.0046 -0.0333 -0.0231 936  ASP B O   
15460 C CB  . ASP B 938  ? 0.5530 0.5820 0.6350 -0.0061 -0.0393 -0.0260 936  ASP B CB  
15461 C CG  . ASP B 938  ? 0.6641 0.6897 0.7437 -0.0080 -0.0434 -0.0269 936  ASP B CG  
15462 O OD1 . ASP B 938  ? 0.6509 0.6745 0.7310 -0.0107 -0.0446 -0.0270 936  ASP B OD1 
15463 O OD2 . ASP B 938  ? 0.6883 0.7130 0.7653 -0.0069 -0.0457 -0.0274 936  ASP B OD2 
15464 N N   . LEU B 939  ? 0.5747 0.6072 0.6602 -0.0048 -0.0303 -0.0242 937  LEU B N   
15465 C CA  . LEU B 939  ? 0.5301 0.5659 0.6174 -0.0028 -0.0268 -0.0234 937  LEU B CA  
15466 C C   . LEU B 939  ? 0.5744 0.6124 0.6653 -0.0046 -0.0248 -0.0223 937  LEU B C   
15467 O O   . LEU B 939  ? 0.6060 0.6397 0.6936 -0.0054 -0.0238 -0.0225 937  LEU B O   
15468 C CB  . LEU B 939  ? 0.5026 0.5339 0.5834 -0.0008 -0.0250 -0.0243 937  LEU B CB  
15469 N N   . GLN B 940  ? 0.5398 0.5845 0.6374 -0.0050 -0.0243 -0.0209 938  GLN B N   
15470 C CA  . GLN B 940  ? 0.5727 0.6204 0.6745 -0.0071 -0.0227 -0.0194 938  GLN B CA  
15471 C C   . GLN B 940  ? 0.5967 0.6471 0.6993 -0.0053 -0.0187 -0.0187 938  GLN B C   
15472 O O   . GLN B 940  ? 0.6070 0.6589 0.7117 -0.0070 -0.0170 -0.0174 938  GLN B O   
15473 C CB  . GLN B 940  ? 0.5681 0.6224 0.6772 -0.0091 -0.0245 -0.0181 938  GLN B CB  
15474 N N   . ARG B 941  ? 0.5152 0.5660 0.6158 -0.0022 -0.0174 -0.0194 939  ARG B N   
15475 C CA  . ARG B 941  ? 0.4960 0.5491 0.5969 -0.0005 -0.0139 -0.0188 939  ARG B CA  
15476 C C   . ARG B 941  ? 0.4376 0.4868 0.5329 0.0021  -0.0131 -0.0200 939  ARG B C   
15477 O O   . ARG B 941  ? 0.4170 0.4635 0.5095 0.0030  -0.0152 -0.0210 939  ARG B O   
15478 C CB  . ARG B 941  ? 0.4846 0.5456 0.5919 0.0004  -0.0130 -0.0178 939  ARG B CB  
15479 C CG  . ARG B 941  ? 0.5144 0.5778 0.6230 0.0028  -0.0147 -0.0185 939  ARG B CG  
15480 C CD  . ARG B 941  ? 0.4962 0.5678 0.6111 0.0043  -0.0134 -0.0176 939  ARG B CD  
15481 N NE  . ARG B 941  ? 0.5649 0.6384 0.6810 0.0070  -0.0151 -0.0183 939  ARG B NE  
15482 C CZ  . ARG B 941  ? 0.4886 0.5616 0.6026 0.0105  -0.0140 -0.0191 939  ARG B CZ  
15483 N NH1 . ARG B 941  ? 0.4923 0.5630 0.6027 0.0117  -0.0112 -0.0193 939  ARG B NH1 
15484 N NH2 . ARG B 941  ? 0.4298 0.5044 0.5451 0.0129  -0.0160 -0.0196 939  ARG B NH2 
15485 N N   . GLU B 942  ? 0.4359 0.4848 0.5294 0.0031  -0.0102 -0.0197 940  GLU B N   
15486 C CA  . GLU B 942  ? 0.4288 0.4747 0.5175 0.0054  -0.0094 -0.0206 940  GLU B CA  
15487 C C   . GLU B 942  ? 0.3966 0.4455 0.4871 0.0077  -0.0098 -0.0209 940  GLU B C   
15488 O O   . GLU B 942  ? 0.4149 0.4692 0.5100 0.0085  -0.0086 -0.0202 940  GLU B O   
15489 C CB  . GLU B 942  ? 0.4687 0.5141 0.5556 0.0057  -0.0063 -0.0201 940  GLU B CB  
15490 C CG  . GLU B 942  ? 0.4434 0.4851 0.5248 0.0073  -0.0056 -0.0208 940  GLU B CG  
15491 C CD  . GLU B 942  ? 0.4833 0.5252 0.5634 0.0076  -0.0028 -0.0202 940  GLU B CD  
15492 O OE1 . GLU B 942  ? 0.5455 0.5911 0.6292 0.0071  -0.0012 -0.0193 940  GLU B OE1 
15493 O OE2 . GLU B 942  ? 0.4497 0.4884 0.5253 0.0082  -0.0021 -0.0206 940  GLU B OE2 
15494 N N   . VAL B 943  ? 0.3293 0.3749 0.4163 0.0090  -0.0116 -0.0218 941  VAL B N   
15495 C CA  . VAL B 943  ? 0.3292 0.3763 0.4168 0.0115  -0.0123 -0.0222 941  VAL B CA  
15496 C C   . VAL B 943  ? 0.2821 0.3252 0.3643 0.0130  -0.0111 -0.0227 941  VAL B C   
15497 O O   . VAL B 943  ? 0.2660 0.3044 0.3433 0.0126  -0.0121 -0.0231 941  VAL B O   
15498 C CB  . VAL B 943  ? 0.3528 0.3990 0.4405 0.0115  -0.0157 -0.0226 941  VAL B CB  
15499 C CG1 . VAL B 943  ? 0.3051 0.3522 0.3931 0.0144  -0.0167 -0.0229 941  VAL B CG1 
15500 C CG2 . VAL B 943  ? 0.3281 0.3783 0.4213 0.0096  -0.0172 -0.0220 941  VAL B CG2 
15501 N N   . PHE B 944  ? 0.2799 0.3252 0.3631 0.0147  -0.0090 -0.0226 942  PHE B N   
15502 C CA  . PHE B 944  ? 0.2559 0.2978 0.3343 0.0155  -0.0074 -0.0228 942  PHE B CA  
15503 C C   . PHE B 944  ? 0.2950 0.3343 0.3705 0.0178  -0.0088 -0.0235 942  PHE B C   
15504 O O   . PHE B 944  ? 0.2487 0.2888 0.3243 0.0200  -0.0079 -0.0239 942  PHE B O   
15505 C CB  . PHE B 944  ? 0.2411 0.2863 0.3214 0.0160  -0.0045 -0.0224 942  PHE B CB  
15506 C CG  . PHE B 944  ? 0.2737 0.3157 0.3495 0.0155  -0.0028 -0.0223 942  PHE B CG  
15507 C CD1 . PHE B 944  ? 0.3242 0.3648 0.3988 0.0133  -0.0022 -0.0218 942  PHE B CD1 
15508 C CD2 . PHE B 944  ? 0.2702 0.3107 0.3430 0.0172  -0.0019 -0.0228 942  PHE B CD2 
15509 C CE1 . PHE B 944  ? 0.2816 0.3199 0.3525 0.0130  -0.0007 -0.0216 942  PHE B CE1 
15510 C CE2 . PHE B 944  ? 0.2535 0.2913 0.3222 0.0166  -0.0006 -0.0226 942  PHE B CE2 
15511 C CZ  . PHE B 944  ? 0.2855 0.3227 0.3536 0.0144  0.0001  -0.0220 942  PHE B CZ  
15512 N N   . GLY B 945  ? 0.2244 0.2600 0.2969 0.0172  -0.0112 -0.0238 943  GLY B N   
15513 C CA  . GLY B 945  ? 0.2197 0.2523 0.2895 0.0190  -0.0131 -0.0242 943  GLY B CA  
15514 C C   . GLY B 945  ? 0.2121 0.2401 0.2772 0.0177  -0.0151 -0.0242 943  GLY B C   
15515 O O   . GLY B 945  ? 0.1876 0.2150 0.2517 0.0156  -0.0149 -0.0240 943  GLY B O   
15516 N N   . PRO B 946  ? 0.2090 0.2337 0.2711 0.0189  -0.0172 -0.0243 944  PRO B N   
15517 C CA  . PRO B 946  ? 0.2245 0.2447 0.2815 0.0175  -0.0189 -0.0241 944  PRO B CA  
15518 C C   . PRO B 946  ? 0.2379 0.2590 0.2965 0.0167  -0.0212 -0.0241 944  PRO B C   
15519 O O   . PRO B 946  ? 0.2526 0.2715 0.3094 0.0174  -0.0238 -0.0241 944  PRO B O   
15520 C CB  . PRO B 946  ? 0.2200 0.2361 0.2732 0.0191  -0.0202 -0.0241 944  PRO B CB  
15521 C CG  . PRO B 946  ? 0.2832 0.3022 0.3409 0.0219  -0.0206 -0.0245 944  PRO B CG  
15522 C CD  . PRO B 946  ? 0.2207 0.2454 0.2837 0.0218  -0.0180 -0.0247 944  PRO B CD  
15523 N N   . VAL B 947  ? 0.2117 0.2356 0.2732 0.0152  -0.0205 -0.0242 945  VAL B N   
15524 C CA  . VAL B 947  ? 0.2179 0.2429 0.2814 0.0144  -0.0228 -0.0243 945  VAL B CA  
15525 C C   . VAL B 947  ? 0.2874 0.3105 0.3481 0.0121  -0.0223 -0.0245 945  VAL B C   
15526 O O   . VAL B 947  ? 0.2671 0.2918 0.3297 0.0111  -0.0204 -0.0245 945  VAL B O   
15527 C CB  . VAL B 947  ? 0.2776 0.3081 0.3482 0.0147  -0.0228 -0.0243 945  VAL B CB  
15528 C CG1 . VAL B 947  ? 0.2720 0.3035 0.3444 0.0137  -0.0257 -0.0244 945  VAL B CG1 
15529 C CG2 . VAL B 947  ? 0.2420 0.2749 0.3153 0.0175  -0.0227 -0.0242 945  VAL B CG2 
15530 N N   . LEU B 948  ? 0.2321 0.2516 0.2879 0.0116  -0.0240 -0.0246 946  LEU B N   
15531 C CA  . LEU B 948  ? 0.2380 0.2555 0.2905 0.0099  -0.0237 -0.0250 946  LEU B CA  
15532 C C   . LEU B 948  ? 0.2633 0.2812 0.3173 0.0090  -0.0261 -0.0255 946  LEU B C   
15533 O O   . LEU B 948  ? 0.2953 0.3129 0.3493 0.0095  -0.0288 -0.0255 946  LEU B O   
15534 C CB  . LEU B 948  ? 0.2424 0.2561 0.2883 0.0097  -0.0240 -0.0248 946  LEU B CB  
15535 C CG  . LEU B 948  ? 0.2550 0.2668 0.2969 0.0085  -0.0236 -0.0252 946  LEU B CG  
15536 C CD1 . LEU B 948  ? 0.2288 0.2415 0.2711 0.0081  -0.0206 -0.0253 946  LEU B CD1 
15537 C CD2 . LEU B 948  ? 0.2350 0.2438 0.2709 0.0083  -0.0243 -0.0247 946  LEU B CD2 
15538 N N   . HIS B 949  ? 0.2451 0.2633 0.3001 0.0077  -0.0254 -0.0259 947  HIS B N   
15539 C CA  . HIS B 949  ? 0.2850 0.3027 0.3406 0.0065  -0.0278 -0.0265 947  HIS B CA  
15540 C C   . HIS B 949  ? 0.2716 0.2851 0.3209 0.0059  -0.0280 -0.0273 947  HIS B C   
15541 O O   . HIS B 949  ? 0.2567 0.2690 0.3032 0.0060  -0.0256 -0.0274 947  HIS B O   
15542 C CB  . HIS B 949  ? 0.2673 0.2879 0.3284 0.0054  -0.0272 -0.0265 947  HIS B CB  
15543 C CG  . HIS B 949  ? 0.3375 0.3630 0.4048 0.0061  -0.0264 -0.0256 947  HIS B CG  
15544 N ND1 . HIS B 949  ? 0.2501 0.2773 0.3187 0.0071  -0.0235 -0.0251 947  HIS B ND1 
15545 C CD2 . HIS B 949  ? 0.3310 0.3604 0.4035 0.0063  -0.0283 -0.0253 947  HIS B CD2 
15546 C CE1 . HIS B 949  ? 0.2961 0.3278 0.3701 0.0080  -0.0234 -0.0246 947  HIS B CE1 
15547 N NE2 . HIS B 949  ? 0.3243 0.3577 0.4010 0.0076  -0.0262 -0.0246 947  HIS B NE2 
15548 N N   . VAL B 950  ? 0.2888 0.3003 0.3356 0.0054  -0.0309 -0.0279 948  VAL B N   
15549 C CA  . VAL B 950  ? 0.2772 0.2848 0.3173 0.0051  -0.0312 -0.0287 948  VAL B CA  
15550 C C   . VAL B 950  ? 0.3190 0.3248 0.3589 0.0038  -0.0334 -0.0298 948  VAL B C   
15551 O O   . VAL B 950  ? 0.3402 0.3472 0.3831 0.0031  -0.0362 -0.0298 948  VAL B O   
15552 C CB  . VAL B 950  ? 0.3278 0.3334 0.3630 0.0056  -0.0327 -0.0284 948  VAL B CB  
15553 C CG1 . VAL B 950  ? 0.3290 0.3312 0.3573 0.0054  -0.0325 -0.0292 948  VAL B CG1 
15554 C CG2 . VAL B 950  ? 0.3045 0.3111 0.3396 0.0066  -0.0309 -0.0272 948  VAL B CG2 
15555 N N   . ILE B 951  ? 0.2639 0.2670 0.3004 0.0035  -0.0321 -0.0308 949  ILE B N   
15556 C CA  . ILE B 951  ? 0.2764 0.2766 0.3111 0.0024  -0.0343 -0.0321 949  ILE B CA  
15557 C C   . ILE B 951  ? 0.3288 0.3249 0.3556 0.0031  -0.0340 -0.0333 949  ILE B C   
15558 O O   . ILE B 951  ? 0.2987 0.2949 0.3226 0.0043  -0.0313 -0.0330 949  ILE B O   
15559 C CB  . ILE B 951  ? 0.3753 0.3754 0.4137 0.0013  -0.0335 -0.0324 949  ILE B CB  
15560 C CG1 . ILE B 951  ? 0.3621 0.3609 0.3981 0.0023  -0.0301 -0.0326 949  ILE B CG1 
15561 C CG2 . ILE B 951  ? 0.4940 0.4990 0.5403 0.0006  -0.0334 -0.0310 949  ILE B CG2 
15562 C CD1 . ILE B 951  ? 0.5036 0.5025 0.5434 0.0013  -0.0292 -0.0324 949  ILE B CD1 
15563 N N   . ARG B 952  ? 0.2830 0.2758 0.3063 0.0025  -0.0368 -0.0346 950  ARG B N   
15564 C CA  . ARG B 952  ? 0.3049 0.2937 0.3201 0.0033  -0.0367 -0.0359 950  ARG B CA  
15565 C C   . ARG B 952  ? 0.3178 0.3028 0.3310 0.0031  -0.0369 -0.0376 950  ARG B C   
15566 O O   . ARG B 952  ? 0.3312 0.3154 0.3480 0.0015  -0.0388 -0.0379 950  ARG B O   
15567 C CB  . ARG B 952  ? 0.3426 0.3298 0.3539 0.0029  -0.0401 -0.0362 950  ARG B CB  
15568 C CG  . ARG B 952  ? 0.3634 0.3539 0.3777 0.0030  -0.0408 -0.0344 950  ARG B CG  
15569 C CD  . ARG B 952  ? 0.4454 0.4348 0.4584 0.0022  -0.0451 -0.0346 950  ARG B CD  
15570 N NE  . ARG B 952  ? 0.4731 0.4595 0.4780 0.0028  -0.0458 -0.0351 950  ARG B NE  
15571 C CZ  . ARG B 952  ? 0.4734 0.4604 0.4760 0.0032  -0.0463 -0.0339 950  ARG B CZ  
15572 N NH1 . ARG B 952  ? 0.4388 0.4289 0.4465 0.0035  -0.0463 -0.0322 950  ARG B NH1 
15573 N NH2 . ARG B 952  ? 0.5328 0.5170 0.5277 0.0035  -0.0469 -0.0342 950  ARG B NH2 
15574 N N   . TYR B 953  ? 0.3066 0.2891 0.3141 0.0046  -0.0348 -0.0386 951  TYR B N   
15575 C CA  . TYR B 953  ? 0.2919 0.2700 0.2968 0.0049  -0.0349 -0.0403 951  TYR B CA  
15576 C C   . TYR B 953  ? 0.3041 0.2784 0.3004 0.0065  -0.0349 -0.0421 951  TYR B C   
15577 O O   . TYR B 953  ? 0.2816 0.2576 0.2742 0.0077  -0.0333 -0.0417 951  TYR B O   
15578 C CB  . TYR B 953  ? 0.3002 0.2796 0.3083 0.0057  -0.0316 -0.0398 951  TYR B CB  
15579 C CG  . TYR B 953  ? 0.2539 0.2350 0.2588 0.0079  -0.0280 -0.0395 951  TYR B CG  
15580 C CD1 . TYR B 953  ? 0.2844 0.2703 0.2917 0.0081  -0.0261 -0.0376 951  TYR B CD1 
15581 C CD2 . TYR B 953  ? 0.2743 0.2523 0.2738 0.0099  -0.0266 -0.0410 951  TYR B CD2 
15582 C CE1 . TYR B 953  ? 0.2612 0.2492 0.2659 0.0097  -0.0231 -0.0371 951  TYR B CE1 
15583 C CE2 . TYR B 953  ? 0.3268 0.3074 0.3239 0.0119  -0.0233 -0.0406 951  TYR B CE2 
15584 C CZ  . TYR B 953  ? 0.2841 0.2698 0.2840 0.0116  -0.0216 -0.0385 951  TYR B CZ  
15585 O OH  . TYR B 953  ? 0.2927 0.2812 0.2904 0.0132  -0.0185 -0.0379 951  TYR B OH  
15586 N N   . ARG B 954  ? 0.3308 0.2996 0.3234 0.0064  -0.0367 -0.0442 952  ARG B N   
15587 C CA  . ARG B 954  ? 0.3803 0.3447 0.3642 0.0084  -0.0365 -0.0463 952  ARG B CA  
15588 C C   . ARG B 954  ? 0.3645 0.3287 0.3471 0.0108  -0.0328 -0.0467 952  ARG B C   
15589 O O   . ARG B 954  ? 0.3627 0.3267 0.3498 0.0105  -0.0320 -0.0464 952  ARG B O   
15590 C CB  . ARG B 954  ? 0.3929 0.3509 0.3731 0.0073  -0.0404 -0.0485 952  ARG B CB  
15591 N N   . ARG B 955  ? 0.4044 0.3691 0.3811 0.0133  -0.0305 -0.0473 953  ARG B N   
15592 C CA  . ARG B 955  ? 0.4171 0.3828 0.3928 0.0159  -0.0268 -0.0476 953  ARG B CA  
15593 C C   . ARG B 955  ? 0.4189 0.3788 0.3938 0.0167  -0.0275 -0.0494 953  ARG B C   
15594 O O   . ARG B 955  ? 0.4026 0.3635 0.3805 0.0178  -0.0252 -0.0488 953  ARG B O   
15595 C CB  . ARG B 955  ? 0.4605 0.4270 0.4288 0.0185  -0.0248 -0.0484 953  ARG B CB  
15596 N N   . ASP B 956  ? 0.4152 0.3686 0.3859 0.0160  -0.0309 -0.0515 954  ASP B N   
15597 C CA  . ASP B 956  ? 0.4670 0.4137 0.4362 0.0164  -0.0322 -0.0532 954  ASP B CA  
15598 C C   . ASP B 956  ? 0.4238 0.3713 0.4011 0.0138  -0.0329 -0.0516 954  ASP B C   
15599 O O   . ASP B 956  ? 0.4529 0.3957 0.4300 0.0141  -0.0332 -0.0524 954  ASP B O   
15600 C CB  . ASP B 956  ? 0.5004 0.4399 0.4635 0.0156  -0.0362 -0.0558 954  ASP B CB  
15601 C CG  . ASP B 956  ? 0.5771 0.5146 0.5309 0.0186  -0.0355 -0.0579 954  ASP B CG  
15602 O OD1 . ASP B 956  ? 0.5797 0.5202 0.5315 0.0218  -0.0316 -0.0578 954  ASP B OD1 
15603 O OD2 . ASP B 956  ? 0.6210 0.5542 0.5696 0.0177  -0.0387 -0.0595 954  ASP B OD2 
15604 N N   . ASP B 957  ? 0.3799 0.3330 0.3639 0.0113  -0.0333 -0.0493 955  ASP B N   
15605 C CA  . ASP B 957  ? 0.3920 0.3467 0.3838 0.0087  -0.0339 -0.0476 955  ASP B CA  
15606 C C   . ASP B 957  ? 0.3333 0.2938 0.3303 0.0096  -0.0301 -0.0455 955  ASP B C   
15607 O O   . ASP B 957  ? 0.3448 0.3081 0.3485 0.0076  -0.0300 -0.0437 955  ASP B O   
15608 C CB  . ASP B 957  ? 0.3777 0.3351 0.3741 0.0055  -0.0368 -0.0465 955  ASP B CB  
15609 C CG  . ASP B 957  ? 0.5120 0.4635 0.5047 0.0037  -0.0413 -0.0483 955  ASP B CG  
15610 O OD1 . ASP B 957  ? 0.5606 0.5054 0.5498 0.0039  -0.0425 -0.0500 955  ASP B OD1 
15611 O OD2 . ASP B 957  ? 0.4707 0.4240 0.4640 0.0022  -0.0437 -0.0480 955  ASP B OD2 
15612 N N   . LEU B 958  ? 0.3298 0.2925 0.3237 0.0126  -0.0269 -0.0456 956  LEU B N   
15613 C CA  . LEU B 958  ? 0.3390 0.3073 0.3375 0.0133  -0.0234 -0.0436 956  LEU B CA  
15614 C C   . LEU B 958  ? 0.3203 0.2873 0.3229 0.0128  -0.0229 -0.0429 956  LEU B C   
15615 O O   . LEU B 958  ? 0.3370 0.3082 0.3458 0.0114  -0.0219 -0.0409 956  LEU B O   
15616 C CB  . LEU B 958  ? 0.3436 0.3137 0.3374 0.0166  -0.0204 -0.0440 956  LEU B CB  
15617 C CG  . LEU B 958  ? 0.3370 0.3132 0.3349 0.0173  -0.0170 -0.0419 956  LEU B CG  
15618 C CD1 . LEU B 958  ? 0.3102 0.2914 0.3134 0.0149  -0.0172 -0.0399 956  LEU B CD1 
15619 C CD2 . LEU B 958  ? 0.3526 0.3312 0.3459 0.0202  -0.0144 -0.0423 956  LEU B CD2 
15620 N N   . ASP B 959  ? 0.3383 0.2990 0.3371 0.0140  -0.0236 -0.0446 957  ASP B N   
15621 C CA  . ASP B 959  ? 0.3539 0.3127 0.3560 0.0136  -0.0231 -0.0438 957  ASP B CA  
15622 C C   . ASP B 959  ? 0.3554 0.3146 0.3634 0.0097  -0.0254 -0.0424 957  ASP B C   
15623 O O   . ASP B 959  ? 0.3219 0.2840 0.3354 0.0086  -0.0241 -0.0405 957  ASP B O   
15624 C CB  . ASP B 959  ? 0.3491 0.2999 0.3452 0.0157  -0.0239 -0.0460 957  ASP B CB  
15625 C CG  . ASP B 959  ? 0.3677 0.3173 0.3660 0.0166  -0.0223 -0.0450 957  ASP B CG  
15626 O OD1 . ASP B 959  ? 0.3530 0.3085 0.3546 0.0178  -0.0193 -0.0434 957  ASP B OD1 
15627 O OD2 . ASP B 959  ? 0.3857 0.3283 0.3824 0.0160  -0.0243 -0.0459 957  ASP B OD2 
15628 N N   . ARG B 960  ? 0.3288 0.2855 0.3359 0.0075  -0.0288 -0.0433 958  ARG B N   
15629 C CA  . ARG B 960  ? 0.2993 0.2575 0.3125 0.0037  -0.0310 -0.0419 958  ARG B CA  
15630 C C   . ARG B 960  ? 0.3145 0.2812 0.3340 0.0029  -0.0293 -0.0397 958  ARG B C   
15631 O O   . ARG B 960  ? 0.3390 0.3088 0.3648 0.0008  -0.0293 -0.0378 958  ARG B O   
15632 C CB  . ARG B 960  ? 0.3215 0.2757 0.3321 0.0017  -0.0351 -0.0433 958  ARG B CB  
15633 N N   . LEU B 961  ? 0.2878 0.2579 0.3054 0.0046  -0.0280 -0.0398 959  LEU B N   
15634 C CA  . LEU B 961  ? 0.2845 0.2617 0.3073 0.0042  -0.0265 -0.0378 959  LEU B CA  
15635 C C   . LEU B 961  ? 0.3303 0.3107 0.3569 0.0048  -0.0233 -0.0362 959  LEU B C   
15636 O O   . LEU B 961  ? 0.3312 0.3160 0.3637 0.0034  -0.0228 -0.0345 959  LEU B O   
15637 C CB  . LEU B 961  ? 0.2885 0.2678 0.3076 0.0058  -0.0257 -0.0382 959  LEU B CB  
15638 C CG  . LEU B 961  ? 0.2843 0.2700 0.3075 0.0058  -0.0240 -0.0363 959  LEU B CG  
15639 C CD1 . LEU B 961  ? 0.2837 0.2720 0.3122 0.0035  -0.0263 -0.0353 959  LEU B CD1 
15640 C CD2 . LEU B 961  ? 0.2624 0.2496 0.2811 0.0074  -0.0229 -0.0364 959  LEU B CD2 
15641 N N   . VAL B 962  ? 0.2810 0.2593 0.3041 0.0071  -0.0212 -0.0368 960  VAL B N   
15642 C CA  . VAL B 962  ? 0.2787 0.2597 0.3049 0.0078  -0.0185 -0.0353 960  VAL B CA  
15643 C C   . VAL B 962  ? 0.3035 0.2833 0.3342 0.0055  -0.0193 -0.0342 960  VAL B C   
15644 O O   . VAL B 962  ? 0.2868 0.2709 0.3224 0.0047  -0.0178 -0.0324 960  VAL B O   
15645 C CB  . VAL B 962  ? 0.3038 0.2826 0.3253 0.0108  -0.0165 -0.0362 960  VAL B CB  
15646 C CG1 . VAL B 962  ? 0.2999 0.2806 0.3245 0.0114  -0.0141 -0.0346 960  VAL B CG1 
15647 C CG2 . VAL B 962  ? 0.2650 0.2466 0.2830 0.0127  -0.0151 -0.0366 960  VAL B CG2 
15648 N N   . ASP B 963  ? 0.3084 0.2824 0.3372 0.0042  -0.0220 -0.0353 961  ASP B N   
15649 C CA  . ASP B 963  ? 0.3347 0.3078 0.3680 0.0014  -0.0233 -0.0341 961  ASP B CA  
15650 C C   . ASP B 963  ? 0.3215 0.3008 0.3612 -0.0010 -0.0237 -0.0325 961  ASP B C   
15651 O O   . ASP B 963  ? 0.3555 0.3381 0.4004 -0.0025 -0.0227 -0.0306 961  ASP B O   
15652 C CB  . ASP B 963  ? 0.3691 0.3348 0.3990 -0.0001 -0.0267 -0.0356 961  ASP B CB  
15653 C CG  . ASP B 963  ? 0.4493 0.4082 0.4741 0.0019  -0.0264 -0.0369 961  ASP B CG  
15654 O OD1 . ASP B 963  ? 0.4811 0.4413 0.5058 0.0041  -0.0235 -0.0361 961  ASP B OD1 
15655 O OD2 . ASP B 963  ? 0.5025 0.4542 0.5229 0.0013  -0.0292 -0.0386 961  ASP B OD2 
15656 N N   . ASP B 964  ? 0.2854 0.2664 0.3247 -0.0013 -0.0253 -0.0332 962  ASP B N   
15657 C CA  . ASP B 964  ? 0.3441 0.3311 0.3895 -0.0032 -0.0260 -0.0318 962  ASP B CA  
15658 C C   . ASP B 964  ? 0.3237 0.3167 0.3726 -0.0020 -0.0228 -0.0302 962  ASP B C   
15659 O O   . ASP B 964  ? 0.2934 0.2911 0.3481 -0.0034 -0.0223 -0.0286 962  ASP B O   
15660 C CB  . ASP B 964  ? 0.3579 0.3450 0.4014 -0.0032 -0.0284 -0.0329 962  ASP B CB  
15661 C CG  . ASP B 964  ? 0.4179 0.3999 0.4592 -0.0052 -0.0322 -0.0341 962  ASP B CG  
15662 O OD1 . ASP B 964  ? 0.3950 0.3736 0.4370 -0.0069 -0.0331 -0.0340 962  ASP B OD1 
15663 O OD2 . ASP B 964  ? 0.5046 0.4858 0.5433 -0.0051 -0.0344 -0.0353 962  ASP B OD2 
15664 N N   . VAL B 965  ? 0.3166 0.3098 0.3619 0.0006  -0.0206 -0.0306 963  VAL B N   
15665 C CA  . VAL B 965  ? 0.2870 0.2852 0.3351 0.0016  -0.0177 -0.0292 963  VAL B CA  
15666 C C   . VAL B 965  ? 0.2618 0.2607 0.3129 0.0009  -0.0160 -0.0279 963  VAL B C   
15667 O O   . VAL B 965  ? 0.3166 0.3200 0.3724 0.0002  -0.0148 -0.0264 963  VAL B O   
15668 C CB  . VAL B 965  ? 0.2915 0.2898 0.3351 0.0040  -0.0159 -0.0298 963  VAL B CB  
15669 C CG1 . VAL B 965  ? 0.2524 0.2552 0.2985 0.0048  -0.0130 -0.0283 963  VAL B CG1 
15670 C CG2 . VAL B 965  ? 0.2912 0.2897 0.3323 0.0044  -0.0175 -0.0307 963  VAL B CG2 
15671 N N   . ASN B 966  ? 0.2752 0.2692 0.3232 0.0014  -0.0159 -0.0284 964  ASN B N   
15672 C CA  . ASN B 966  ? 0.2843 0.2781 0.3346 0.0007  -0.0145 -0.0270 964  ASN B CA  
15673 C C   . ASN B 966  ? 0.3359 0.3312 0.3914 -0.0023 -0.0159 -0.0257 964  ASN B C   
15674 O O   . ASN B 966  ? 0.2858 0.2834 0.3446 -0.0032 -0.0143 -0.0240 964  ASN B O   
15675 C CB  . ASN B 966  ? 0.3019 0.2892 0.3475 0.0019  -0.0148 -0.0280 964  ASN B CB  
15676 C CG  . ASN B 966  ? 0.3047 0.2919 0.3461 0.0052  -0.0128 -0.0288 964  ASN B CG  
15677 O OD1 . ASN B 966  ? 0.2769 0.2689 0.3194 0.0062  -0.0108 -0.0281 964  ASN B OD1 
15678 N ND2 . ASN B 966  ? 0.2647 0.2463 0.3011 0.0068  -0.0134 -0.0303 964  ASN B ND2 
15679 N N   . ALA B 967  ? 0.2997 0.2936 0.3557 -0.0042 -0.0188 -0.0264 965  ALA B N   
15680 C CA  . ALA B 967  ? 0.3125 0.3076 0.3733 -0.0075 -0.0204 -0.0252 965  ALA B CA  
15681 C C   . ALA B 967  ? 0.3420 0.3449 0.4092 -0.0083 -0.0190 -0.0234 965  ALA B C   
15682 O O   . ALA B 967  ? 0.3390 0.3442 0.4109 -0.0110 -0.0196 -0.0218 965  ALA B O   
15683 C CB  . ALA B 967  ? 0.3295 0.3215 0.3892 -0.0092 -0.0241 -0.0264 965  ALA B CB  
15684 N N   . THR B 968  ? 0.3089 0.3162 0.3766 -0.0062 -0.0174 -0.0235 966  THR B N   
15685 C CA  . THR B 968  ? 0.3055 0.3197 0.3787 -0.0065 -0.0158 -0.0219 966  THR B CA  
15686 C C   . THR B 968  ? 0.3283 0.3442 0.4035 -0.0069 -0.0132 -0.0202 966  THR B C   
15687 O O   . THR B 968  ? 0.3375 0.3591 0.4177 -0.0077 -0.0121 -0.0187 966  THR B O   
15688 C CB  . THR B 968  ? 0.3516 0.3688 0.4240 -0.0040 -0.0146 -0.0225 966  THR B CB  
15689 O OG1 . THR B 968  ? 0.3251 0.3411 0.3941 -0.0021 -0.0121 -0.0225 966  THR B OG1 
15690 C CG2 . THR B 968  ? 0.3566 0.3715 0.4258 -0.0034 -0.0170 -0.0241 966  THR B CG2 
15691 N N   . GLY B 969  ? 0.2977 0.3091 0.3692 -0.0062 -0.0123 -0.0203 967  GLY B N   
15692 C CA  . GLY B 969  ? 0.2947 0.3073 0.3672 -0.0062 -0.0098 -0.0187 967  GLY B CA  
15693 C C   . GLY B 969  ? 0.3196 0.3354 0.3913 -0.0037 -0.0071 -0.0186 967  GLY B C   
15694 O O   . GLY B 969  ? 0.3008 0.3170 0.3724 -0.0034 -0.0051 -0.0174 967  GLY B O   
15695 N N   . TYR B 970  ? 0.2610 0.2787 0.3318 -0.0021 -0.0071 -0.0196 968  TYR B N   
15696 C CA  . TYR B 970  ? 0.2832 0.3028 0.3524 0.0000  -0.0050 -0.0197 968  TYR B CA  
15697 C C   . TYR B 970  ? 0.3025 0.3180 0.3665 0.0017  -0.0047 -0.0207 968  TYR B C   
15698 O O   . TYR B 970  ? 0.3013 0.3126 0.3625 0.0017  -0.0063 -0.0218 968  TYR B O   
15699 C CB  . TYR B 970  ? 0.2649 0.2879 0.3353 0.0009  -0.0054 -0.0202 968  TYR B CB  
15700 C CG  . TYR B 970  ? 0.3293 0.3575 0.4049 0.0001  -0.0049 -0.0192 968  TYR B CG  
15701 C CD1 . TYR B 970  ? 0.3211 0.3528 0.3981 0.0008  -0.0025 -0.0182 968  TYR B CD1 
15702 C CD2 . TYR B 970  ? 0.3703 0.4004 0.4495 -0.0013 -0.0069 -0.0192 968  TYR B CD2 
15703 C CE1 . TYR B 970  ? 0.3690 0.4058 0.4506 0.0005  -0.0018 -0.0174 968  TYR B CE1 
15704 C CE2 . TYR B 970  ? 0.4113 0.4470 0.4956 -0.0017 -0.0063 -0.0182 968  TYR B CE2 
15705 C CZ  . TYR B 970  ? 0.4450 0.4841 0.5305 -0.0007 -0.0036 -0.0173 968  TYR B CZ  
15706 O OH  . TYR B 970  ? 0.5362 0.5812 0.6265 -0.0008 -0.0027 -0.0164 968  TYR B OH  
15707 N N   . GLY B 971  ? 0.2844 0.3015 0.3468 0.0033  -0.0027 -0.0204 969  GLY B N   
15708 C CA  . GLY B 971  ? 0.2443 0.2588 0.3023 0.0050  -0.0024 -0.0212 969  GLY B CA  
15709 C C   . GLY B 971  ? 0.2354 0.2528 0.2926 0.0062  -0.0004 -0.0206 969  GLY B C   
15710 O O   . GLY B 971  ? 0.2230 0.2403 0.2789 0.0070  0.0010  -0.0199 969  GLY B O   
15711 N N   . LEU B 972  ? 0.2452 0.2651 0.3029 0.0064  -0.0006 -0.0209 970  LEU B N   
15712 C CA  . LEU B 972  ? 0.1998 0.2220 0.2565 0.0072  0.0009  -0.0204 970  LEU B CA  
15713 C C   . LEU B 972  ? 0.2163 0.2376 0.2691 0.0082  0.0007  -0.0211 970  LEU B C   
15714 O O   . LEU B 972  ? 0.2323 0.2529 0.2829 0.0091  0.0015  -0.0209 970  LEU B O   
15715 C CB  . LEU B 972  ? 0.2291 0.2541 0.2882 0.0069  0.0009  -0.0202 970  LEU B CB  
15716 C CG  . LEU B 972  ? 0.2619 0.2887 0.3199 0.0076  0.0024  -0.0196 970  LEU B CG  
15717 C CD1 . LEU B 972  ? 0.2564 0.2837 0.3144 0.0076  0.0041  -0.0185 970  LEU B CD1 
15718 C CD2 . LEU B 972  ? 0.2570 0.2861 0.3175 0.0077  0.0024  -0.0196 970  LEU B CD2 
15719 N N   . THR B 973  ? 0.2009 0.2223 0.2529 0.0081  -0.0005 -0.0217 971  THR B N   
15720 C CA  . THR B 973  ? 0.1784 0.1990 0.2265 0.0088  -0.0008 -0.0222 971  THR B CA  
15721 C C   . THR B 973  ? 0.1926 0.2106 0.2390 0.0088  -0.0025 -0.0234 971  THR B C   
15722 O O   . THR B 973  ? 0.2081 0.2252 0.2565 0.0080  -0.0040 -0.0239 971  THR B O   
15723 C CB  . THR B 973  ? 0.2108 0.2329 0.2581 0.0087  -0.0009 -0.0219 971  THR B CB  
15724 O OG1 . THR B 973  ? 0.2234 0.2452 0.2724 0.0083  -0.0024 -0.0223 971  THR B OG1 
15725 C CG2 . THR B 973  ? 0.2316 0.2556 0.2797 0.0087  0.0007  -0.0209 971  THR B CG2 
15726 N N   . PHE B 974  ? 0.2028 0.2201 0.2455 0.0096  -0.0023 -0.0238 972  PHE B N   
15727 C CA  . PHE B 974  ? 0.2085 0.2232 0.2485 0.0099  -0.0038 -0.0251 972  PHE B CA  
15728 C C   . PHE B 974  ? 0.2148 0.2303 0.2508 0.0105  -0.0033 -0.0251 972  PHE B C   
15729 O O   . PHE B 974  ? 0.1817 0.1992 0.2168 0.0113  -0.0016 -0.0244 972  PHE B O   
15730 C CB  . PHE B 974  ? 0.1904 0.2023 0.2296 0.0105  -0.0038 -0.0258 972  PHE B CB  
15731 C CG  . PHE B 974  ? 0.1781 0.1870 0.2136 0.0111  -0.0052 -0.0273 972  PHE B CG  
15732 C CD1 . PHE B 974  ? 0.2165 0.2231 0.2523 0.0100  -0.0076 -0.0282 972  PHE B CD1 
15733 C CD2 . PHE B 974  ? 0.2198 0.2284 0.2512 0.0128  -0.0042 -0.0279 972  PHE B CD2 
15734 C CE1 . PHE B 974  ? 0.2378 0.2413 0.2696 0.0105  -0.0090 -0.0297 972  PHE B CE1 
15735 C CE2 . PHE B 974  ? 0.2173 0.2231 0.2447 0.0135  -0.0053 -0.0294 972  PHE B CE2 
15736 C CZ  . PHE B 974  ? 0.2478 0.2507 0.2751 0.0124  -0.0078 -0.0303 972  PHE B CZ  
15737 N N   . GLY B 975  ? 0.1971 0.2115 0.2309 0.0102  -0.0049 -0.0257 973  GLY B N   
15738 C CA  . GLY B 975  ? 0.1919 0.2072 0.2217 0.0106  -0.0045 -0.0255 973  GLY B CA  
15739 C C   . GLY B 975  ? 0.1885 0.2013 0.2145 0.0114  -0.0054 -0.0269 973  GLY B C   
15740 O O   . GLY B 975  ? 0.1775 0.1874 0.2037 0.0111  -0.0072 -0.0280 973  GLY B O   
15741 N N   . LEU B 976  ? 0.1816 0.1957 0.2040 0.0124  -0.0041 -0.0269 974  LEU B N   
15742 C CA  . LEU B 976  ? 0.1863 0.1983 0.2042 0.0135  -0.0046 -0.0283 974  LEU B CA  
15743 C C   . LEU B 976  ? 0.2231 0.2377 0.2374 0.0133  -0.0039 -0.0274 974  LEU B C   
15744 O O   . LEU B 976  ? 0.2308 0.2492 0.2454 0.0135  -0.0020 -0.0262 974  LEU B O   
15745 C CB  . LEU B 976  ? 0.2340 0.2450 0.2508 0.0156  -0.0034 -0.0293 974  LEU B CB  
15746 C CG  . LEU B 976  ? 0.2653 0.2742 0.2767 0.0172  -0.0036 -0.0309 974  LEU B CG  
15747 C CD1 . LEU B 976  ? 0.2279 0.2320 0.2377 0.0164  -0.0064 -0.0324 974  LEU B CD1 
15748 C CD2 . LEU B 976  ? 0.2480 0.2563 0.2582 0.0198  -0.0020 -0.0318 974  LEU B CD2 
15749 N N   . HIS B 977  ? 0.2417 0.2545 0.2528 0.0128  -0.0056 -0.0280 975  HIS B N   
15750 C CA  . HIS B 977  ? 0.2219 0.2368 0.2290 0.0125  -0.0050 -0.0271 975  HIS B CA  
15751 C C   . HIS B 977  ? 0.1886 0.2020 0.1906 0.0141  -0.0049 -0.0287 975  HIS B C   
15752 O O   . HIS B 977  ? 0.2145 0.2239 0.2145 0.0141  -0.0071 -0.0301 975  HIS B O   
15753 C CB  . HIS B 977  ? 0.2287 0.2427 0.2355 0.0106  -0.0070 -0.0261 975  HIS B CB  
15754 C CG  . HIS B 977  ? 0.2370 0.2535 0.2462 0.0091  -0.0064 -0.0242 975  HIS B CG  
15755 N ND1 . HIS B 977  ? 0.3102 0.3291 0.3169 0.0080  -0.0057 -0.0225 975  HIS B ND1 
15756 C CD2 . HIS B 977  ? 0.3062 0.3229 0.3199 0.0086  -0.0064 -0.0236 975  HIS B CD2 
15757 C CE1 . HIS B 977  ? 0.2712 0.2912 0.2806 0.0068  -0.0056 -0.0211 975  HIS B CE1 
15758 N NE2 . HIS B 977  ? 0.3043 0.3231 0.3178 0.0072  -0.0059 -0.0219 975  HIS B NE2 
15759 N N   . THR B 978  ? 0.2189 0.2355 0.2187 0.0156  -0.0026 -0.0284 976  THR B N   
15760 C CA  . THR B 978  ? 0.2550 0.2706 0.2496 0.0177  -0.0020 -0.0300 976  THR B CA  
15761 C C   . THR B 978  ? 0.2626 0.2839 0.2557 0.0188  0.0009  -0.0289 976  THR B C   
15762 O O   . THR B 978  ? 0.2530 0.2781 0.2498 0.0186  0.0025  -0.0274 976  THR B O   
15763 C CB  . THR B 978  ? 0.2654 0.2768 0.2599 0.0198  -0.0025 -0.0323 976  THR B CB  
15764 O OG1 . THR B 978  ? 0.2594 0.2696 0.2481 0.0221  -0.0019 -0.0340 976  THR B OG1 
15765 C CG2 . THR B 978  ? 0.2639 0.2774 0.2624 0.0209  -0.0006 -0.0318 976  THR B CG2 
15766 N N   . ARG B 979  ? 0.2518 0.2739 0.2395 0.0200  0.0016  -0.0295 977  ARG B N   
15767 C CA  . ARG B 979  ? 0.2649 0.2930 0.2511 0.0216  0.0046  -0.0286 977  ARG B CA  
15768 C C   . ARG B 979  ? 0.2468 0.2742 0.2313 0.0255  0.0061  -0.0308 977  ARG B C   
15769 O O   . ARG B 979  ? 0.2559 0.2886 0.2392 0.0274  0.0087  -0.0302 977  ARG B O   
15770 C CB  . ARG B 979  ? 0.2977 0.3282 0.2789 0.0205  0.0049  -0.0276 977  ARG B CB  
15771 N N   . LEU B 980  ? 0.2492 0.2703 0.2335 0.0267  0.0044  -0.0330 978  LEU B N   
15772 C CA  . LEU B 980  ? 0.2396 0.2581 0.2206 0.0305  0.0052  -0.0355 978  LEU B CA  
15773 C C   . LEU B 980  ? 0.2513 0.2692 0.2367 0.0319  0.0059  -0.0356 978  LEU B C   
15774 O O   . LEU B 980  ? 0.2552 0.2692 0.2441 0.0303  0.0040  -0.0357 978  LEU B O   
15775 C CB  . LEU B 980  ? 0.2421 0.2530 0.2188 0.0308  0.0025  -0.0381 978  LEU B CB  
15776 C CG  . LEU B 980  ? 0.2626 0.2735 0.2352 0.0289  0.0013  -0.0377 978  LEU B CG  
15777 C CD1 . LEU B 980  ? 0.3062 0.3094 0.2748 0.0290  -0.0017 -0.0403 978  LEU B CD1 
15778 C CD2 . LEU B 980  ? 0.3021 0.3182 0.2701 0.0308  0.0040  -0.0374 978  LEU B CD2 
15779 N N   . ASP B 981  ? 0.2312 0.2531 0.2162 0.0351  0.0085  -0.0356 979  ASP B N   
15780 C CA  . ASP B 981  ? 0.2275 0.2492 0.2163 0.0368  0.0092  -0.0356 979  ASP B CA  
15781 C C   . ASP B 981  ? 0.2317 0.2447 0.2193 0.0380  0.0071  -0.0380 979  ASP B C   
15782 O O   . ASP B 981  ? 0.2492 0.2600 0.2408 0.0374  0.0064  -0.0376 979  ASP B O   
15783 C CB  . ASP B 981  ? 0.2519 0.2796 0.2400 0.0404  0.0122  -0.0353 979  ASP B CB  
15784 C CG  . ASP B 981  ? 0.2887 0.3255 0.2796 0.0387  0.0142  -0.0324 979  ASP B CG  
15785 O OD1 . ASP B 981  ? 0.2917 0.3294 0.2860 0.0348  0.0131  -0.0305 979  ASP B OD1 
15786 O OD2 . ASP B 981  ? 0.3182 0.3613 0.3080 0.0412  0.0167  -0.0319 979  ASP B OD2 
15787 N N   . GLU B 982  ? 0.2582 0.2659 0.2399 0.0396  0.0060  -0.0405 980  GLU B N   
15788 C CA  . GLU B 982  ? 0.2581 0.2571 0.2385 0.0404  0.0037  -0.0427 980  GLU B CA  
15789 C C   . GLU B 982  ? 0.2510 0.2467 0.2355 0.0362  0.0010  -0.0419 980  GLU B C   
15790 O O   . GLU B 982  ? 0.2711 0.2626 0.2583 0.0357  -0.0002 -0.0421 980  GLU B O   
15791 C CB  . GLU B 982  ? 0.2799 0.2734 0.2528 0.0425  0.0026  -0.0457 980  GLU B CB  
15792 C CG  . GLU B 982  ? 0.3260 0.3096 0.2974 0.0424  -0.0004 -0.0479 980  GLU B CG  
15793 C CD  . GLU B 982  ? 0.4584 0.4357 0.4221 0.0438  -0.0022 -0.0508 980  GLU B CD  
15794 O OE1 . GLU B 982  ? 0.5381 0.5179 0.4985 0.0432  -0.0020 -0.0509 980  GLU B OE1 
15795 O OE2 . GLU B 982  ? 0.4222 0.3917 0.3829 0.0455  -0.0038 -0.0531 980  GLU B OE2 
15796 N N   . THR B 983  ? 0.2660 0.2640 0.2512 0.0331  0.0001  -0.0408 981  THR B N   
15797 C CA  . THR B 983  ? 0.2433 0.2392 0.2327 0.0295  -0.0022 -0.0399 981  THR B CA  
15798 C C   . THR B 983  ? 0.2573 0.2568 0.2533 0.0283  -0.0011 -0.0377 981  THR B C   
15799 O O   . THR B 983  ? 0.2384 0.2350 0.2380 0.0266  -0.0026 -0.0375 981  THR B O   
15800 C CB  . THR B 983  ? 0.2292 0.2268 0.2175 0.0270  -0.0034 -0.0392 981  THR B CB  
15801 O OG1 . THR B 983  ? 0.3004 0.2938 0.2825 0.0280  -0.0048 -0.0414 981  THR B OG1 
15802 C CG2 . THR B 983  ? 0.2344 0.2308 0.2277 0.0236  -0.0056 -0.0381 981  THR B CG2 
15803 N N   . ILE B 984  ? 0.2037 0.2098 0.2011 0.0289  0.0014  -0.0360 982  ILE B N   
15804 C CA  . ILE B 984  ? 0.2259 0.2352 0.2289 0.0279  0.0024  -0.0340 982  ILE B CA  
15805 C C   . ILE B 984  ? 0.2311 0.2368 0.2353 0.0297  0.0024  -0.0348 982  ILE B C   
15806 O O   . ILE B 984  ? 0.2626 0.2668 0.2709 0.0280  0.0016  -0.0340 982  ILE B O   
15807 C CB  . ILE B 984  ? 0.2447 0.2616 0.2486 0.0283  0.0050  -0.0322 982  ILE B CB  
15808 C CG1 . ILE B 984  ? 0.2538 0.2736 0.2571 0.0257  0.0045  -0.0309 982  ILE B CG1 
15809 C CG2 . ILE B 984  ? 0.2734 0.2932 0.2823 0.0279  0.0060  -0.0304 982  ILE B CG2 
15810 C CD1 . ILE B 984  ? 0.2807 0.3076 0.2835 0.0259  0.0068  -0.0292 982  ILE B CD1 
15811 N N   . ALA B 985  ? 0.2367 0.2410 0.2372 0.0333  0.0034  -0.0363 983  ALA B N   
15812 C CA  . ALA B 985  ? 0.2459 0.2462 0.2469 0.0354  0.0033  -0.0370 983  ALA B CA  
15813 C C   . ALA B 985  ? 0.2752 0.2677 0.2762 0.0336  0.0005  -0.0382 983  ALA B C   
15814 O O   . ALA B 985  ? 0.2467 0.2371 0.2511 0.0326  -0.0001 -0.0374 983  ALA B O   
15815 C CB  . ALA B 985  ? 0.2662 0.2658 0.2625 0.0399  0.0047  -0.0387 983  ALA B CB  
15816 N N   . HIS B 986  ? 0.2478 0.2362 0.2450 0.0330  -0.0014 -0.0399 984  HIS B N   
15817 C CA  . HIS B 986  ? 0.2728 0.2541 0.2700 0.0310  -0.0044 -0.0410 984  HIS B CA  
15818 C C   . HIS B 986  ? 0.2402 0.2236 0.2437 0.0272  -0.0052 -0.0389 984  HIS B C   
15819 O O   . HIS B 986  ? 0.2535 0.2340 0.2598 0.0261  -0.0061 -0.0384 984  HIS B O   
15820 C CB  . HIS B 986  ? 0.2840 0.2619 0.2762 0.0306  -0.0064 -0.0430 984  HIS B CB  
15821 C CG  . HIS B 986  ? 0.3708 0.3422 0.3632 0.0280  -0.0098 -0.0439 984  HIS B CG  
15822 N ND1 . HIS B 986  ? 0.3832 0.3502 0.3709 0.0276  -0.0121 -0.0459 984  HIS B ND1 
15823 C CD2 . HIS B 986  ? 0.3644 0.3334 0.3612 0.0255  -0.0113 -0.0430 984  HIS B CD2 
15824 C CE1 . HIS B 986  ? 0.4104 0.3727 0.3998 0.0248  -0.0151 -0.0461 984  HIS B CE1 
15825 N NE2 . HIS B 986  ? 0.3499 0.3134 0.3449 0.0235  -0.0146 -0.0444 984  HIS B NE2 
15826 N N   . VAL B 987  ? 0.2304 0.2188 0.2359 0.0252  -0.0049 -0.0377 985  VAL B N   
15827 C CA  . VAL B 987  ? 0.2342 0.2242 0.2450 0.0219  -0.0059 -0.0361 985  VAL B CA  
15828 C C   . VAL B 987  ? 0.2408 0.2338 0.2563 0.0217  -0.0042 -0.0342 985  VAL B C   
15829 O O   . VAL B 987  ? 0.2573 0.2487 0.2764 0.0199  -0.0052 -0.0335 985  VAL B O   
15830 C CB  . VAL B 987  ? 0.2591 0.2532 0.2704 0.0202  -0.0061 -0.0353 985  VAL B CB  
15831 C CG1 . VAL B 987  ? 0.2524 0.2489 0.2693 0.0175  -0.0066 -0.0335 985  VAL B CG1 
15832 C CG2 . VAL B 987  ? 0.2337 0.2242 0.2409 0.0198  -0.0084 -0.0370 985  VAL B CG2 
15833 N N   . THR B 988  ? 0.2165 0.2140 0.2319 0.0235  -0.0018 -0.0333 986  THR B N   
15834 C CA  . THR B 988  ? 0.2669 0.2673 0.2864 0.0233  -0.0003 -0.0315 986  THR B CA  
15835 C C   . THR B 988  ? 0.2781 0.2740 0.2975 0.0247  -0.0006 -0.0319 986  THR B C   
15836 O O   . THR B 988  ? 0.3045 0.3013 0.3275 0.0237  -0.0001 -0.0304 986  THR B O   
15837 C CB  . THR B 988  ? 0.2843 0.2910 0.3038 0.0247  0.0021  -0.0303 986  THR B CB  
15838 O OG1 . THR B 988  ? 0.2699 0.2763 0.2855 0.0281  0.0032  -0.0314 986  THR B OG1 
15839 C CG2 . THR B 988  ? 0.2984 0.3091 0.3178 0.0230  0.0022  -0.0296 986  THR B CG2 
15840 N N   . SER B 989  ? 0.2986 0.2892 0.3138 0.0268  -0.0014 -0.0338 987  SER B N   
15841 C CA  . SER B 989  ? 0.3040 0.2890 0.3187 0.0278  -0.0021 -0.0342 987  SER B CA  
15842 C C   . SER B 989  ? 0.3622 0.3423 0.3787 0.0247  -0.0046 -0.0342 987  SER B C   
15843 O O   . SER B 989  ? 0.3756 0.3519 0.3931 0.0245  -0.0052 -0.0338 987  SER B O   
15844 C CB  . SER B 989  ? 0.3114 0.2918 0.3203 0.0315  -0.0023 -0.0365 987  SER B CB  
15845 O OG  . SER B 989  ? 0.3596 0.3357 0.3648 0.0309  -0.0043 -0.0385 987  SER B OG  
15846 N N   . ARG B 990  ? 0.2835 0.2640 0.3008 0.0222  -0.0062 -0.0346 988  ARG B N   
15847 C CA  . ARG B 990  ? 0.2887 0.2650 0.3078 0.0192  -0.0087 -0.0346 988  ARG B CA  
15848 C C   . ARG B 990  ? 0.3002 0.2812 0.3251 0.0160  -0.0087 -0.0327 988  ARG B C   
15849 O O   . ARG B 990  ? 0.2913 0.2703 0.3191 0.0136  -0.0100 -0.0320 988  ARG B O   
15850 C CB  . ARG B 990  ? 0.2681 0.2401 0.2831 0.0188  -0.0111 -0.0368 988  ARG B CB  
15851 C CG  . ARG B 990  ? 0.3714 0.3385 0.3799 0.0223  -0.0112 -0.0391 988  ARG B CG  
15852 C CD  . ARG B 990  ? 0.3506 0.3098 0.3571 0.0226  -0.0128 -0.0399 988  ARG B CD  
15853 N NE  . ARG B 990  ? 0.3752 0.3283 0.3798 0.0203  -0.0162 -0.0413 988  ARG B NE  
15854 C CZ  . ARG B 990  ? 0.3647 0.3100 0.3675 0.0196  -0.0184 -0.0421 988  ARG B CZ  
15855 N NH1 . ARG B 990  ? 0.4004 0.3427 0.4031 0.0211  -0.0177 -0.0414 988  ARG B NH1 
15856 N NH2 . ARG B 990  ? 0.3257 0.2658 0.3265 0.0174  -0.0217 -0.0434 988  ARG B NH2 
15857 N N   . ILE B 991  ? 0.2449 0.2320 0.2713 0.0160  -0.0072 -0.0319 989  ILE B N   
15858 C CA  . ILE B 991  ? 0.2484 0.2398 0.2800 0.0135  -0.0071 -0.0302 989  ILE B CA  
15859 C C   . ILE B 991  ? 0.2765 0.2695 0.3114 0.0132  -0.0056 -0.0284 989  ILE B C   
15860 O O   . ILE B 991  ? 0.2665 0.2595 0.3001 0.0152  -0.0040 -0.0281 989  ILE B O   
15861 C CB  . ILE B 991  ? 0.2584 0.2549 0.2899 0.0137  -0.0060 -0.0298 989  ILE B CB  
15862 C CG1 . ILE B 991  ? 0.2852 0.2850 0.3212 0.0113  -0.0065 -0.0287 989  ILE B CG1 
15863 C CG2 . ILE B 991  ? 0.3087 0.3088 0.3396 0.0156  -0.0035 -0.0289 989  ILE B CG2 
15864 C CD1 . ILE B 991  ? 0.2460 0.2436 0.2825 0.0096  -0.0092 -0.0295 989  ILE B CD1 
15865 N N   . LYS B 992  ? 0.2409 0.2352 0.2802 0.0107  -0.0061 -0.0272 990  LYS B N   
15866 C CA  . LYS B 992  ? 0.2770 0.2730 0.3193 0.0102  -0.0046 -0.0254 990  LYS B CA  
15867 C C   . LYS B 992  ? 0.2801 0.2821 0.3260 0.0092  -0.0034 -0.0241 990  LYS B C   
15868 O O   . LYS B 992  ? 0.3449 0.3487 0.3944 0.0072  -0.0039 -0.0233 990  LYS B O   
15869 C CB  . LYS B 992  ? 0.2590 0.2514 0.3034 0.0080  -0.0062 -0.0248 990  LYS B CB  
15870 N N   . ALA B 993  ? 0.2908 0.2959 0.3353 0.0108  -0.0018 -0.0240 991  ALA B N   
15871 C CA  . ALA B 993  ? 0.2251 0.2350 0.2720 0.0101  -0.0007 -0.0229 991  ALA B CA  
15872 C C   . ALA B 993  ? 0.2205 0.2330 0.2669 0.0113  0.0013  -0.0219 991  ALA B C   
15873 O O   . ALA B 993  ? 0.2518 0.2633 0.2955 0.0131  0.0019  -0.0222 991  ALA B O   
15874 C CB  . ALA B 993  ? 0.2139 0.2253 0.2598 0.0100  -0.0015 -0.0237 991  ALA B CB  
15875 N N   . GLY B 994  ? 0.2205 0.2363 0.2694 0.0105  0.0023  -0.0207 992  GLY B N   
15876 C CA  . GLY B 994  ? 0.2122 0.2304 0.2607 0.0114  0.0040  -0.0196 992  GLY B CA  
15877 C C   . GLY B 994  ? 0.2046 0.2254 0.2511 0.0121  0.0045  -0.0197 992  GLY B C   
15878 O O   . GLY B 994  ? 0.1991 0.2215 0.2445 0.0132  0.0057  -0.0190 992  GLY B O   
15879 N N   . ASN B 995  ? 0.1960 0.2172 0.2420 0.0115  0.0037  -0.0204 993  ASN B N   
15880 C CA  . ASN B 995  ? 0.1922 0.2157 0.2362 0.0117  0.0040  -0.0203 993  ASN B CA  
15881 C C   . ASN B 995  ? 0.2159 0.2378 0.2575 0.0120  0.0028  -0.0215 993  ASN B C   
15882 O O   . ASN B 995  ? 0.2150 0.2356 0.2571 0.0111  0.0015  -0.0221 993  ASN B O   
15883 C CB  . ASN B 995  ? 0.1614 0.1867 0.2066 0.0105  0.0040  -0.0197 993  ASN B CB  
15884 C CG  . ASN B 995  ? 0.1845 0.2118 0.2306 0.0105  0.0053  -0.0184 993  ASN B CG  
15885 O OD1 . ASN B 995  ? 0.1885 0.2157 0.2367 0.0103  0.0058  -0.0180 993  ASN B OD1 
15886 N ND2 . ASN B 995  ? 0.2088 0.2384 0.2533 0.0106  0.0059  -0.0178 993  ASN B ND2 
15887 N N   . LEU B 996  ? 0.1931 0.2154 0.2320 0.0133  0.0034  -0.0218 994  LEU B N   
15888 C CA  . LEU B 996  ? 0.1692 0.1901 0.2051 0.0138  0.0025  -0.0229 994  LEU B CA  
15889 C C   . LEU B 996  ? 0.1697 0.1937 0.2037 0.0134  0.0030  -0.0222 994  LEU B C   
15890 O O   . LEU B 996  ? 0.2117 0.2390 0.2459 0.0135  0.0043  -0.0211 994  LEU B O   
15891 C CB  . LEU B 996  ? 0.1691 0.1882 0.2027 0.0158  0.0029  -0.0239 994  LEU B CB  
15892 C CG  . LEU B 996  ? 0.2100 0.2258 0.2452 0.0163  0.0026  -0.0242 994  LEU B CG  
15893 C CD1 . LEU B 996  ? 0.2737 0.2871 0.3059 0.0187  0.0028  -0.0253 994  LEU B CD1 
15894 C CD2 . LEU B 996  ? 0.2449 0.2577 0.2817 0.0146  0.0008  -0.0248 994  LEU B CD2 
15895 N N   . TYR B 997  ? 0.1922 0.2152 0.2242 0.0128  0.0018  -0.0228 995  TYR B N   
15896 C CA  . TYR B 997  ? 0.1740 0.1994 0.2039 0.0120  0.0020  -0.0220 995  TYR B CA  
15897 C C   . TYR B 997  ? 0.1739 0.1983 0.2001 0.0127  0.0014  -0.0229 995  TYR B C   
15898 O O   . TYR B 997  ? 0.2238 0.2449 0.2494 0.0126  -0.0001 -0.0242 995  TYR B O   
15899 C CB  . TYR B 997  ? 0.1775 0.2026 0.2084 0.0102  0.0008  -0.0214 995  TYR B CB  
15900 C CG  . TYR B 997  ? 0.1751 0.2011 0.2092 0.0097  0.0014  -0.0206 995  TYR B CG  
15901 C CD1 . TYR B 997  ? 0.2210 0.2497 0.2550 0.0091  0.0024  -0.0193 995  TYR B CD1 
15902 C CD2 . TYR B 997  ? 0.2060 0.2302 0.2429 0.0097  0.0009  -0.0211 995  TYR B CD2 
15903 C CE1 . TYR B 997  ? 0.2121 0.2414 0.2485 0.0087  0.0029  -0.0187 995  TYR B CE1 
15904 C CE2 . TYR B 997  ? 0.2205 0.2458 0.2600 0.0094  0.0016  -0.0204 995  TYR B CE2 
15905 C CZ  . TYR B 997  ? 0.2372 0.2647 0.2761 0.0090  0.0026  -0.0193 995  TYR B CZ  
15906 O OH  . TYR B 997  ? 0.3036 0.3319 0.3445 0.0087  0.0032  -0.0187 995  TYR B OH  
15907 N N   . ILE B 998  ? 0.1880 0.2155 0.2118 0.0132  0.0027  -0.0223 996  ILE B N   
15908 C CA  . ILE B 998  ? 0.1961 0.2232 0.2159 0.0142  0.0026  -0.0232 996  ILE B CA  
15909 C C   . ILE B 998  ? 0.1960 0.2255 0.2136 0.0125  0.0025  -0.0219 996  ILE B C   
15910 O O   . ILE B 998  ? 0.2140 0.2477 0.2320 0.0119  0.0038  -0.0203 996  ILE B O   
15911 C CB  . ILE B 998  ? 0.2419 0.2709 0.2604 0.0167  0.0044  -0.0237 996  ILE B CB  
15912 C CG1 . ILE B 998  ? 0.2409 0.2667 0.2613 0.0182  0.0043  -0.0248 996  ILE B CG1 
15913 C CG2 . ILE B 998  ? 0.2388 0.2674 0.2526 0.0180  0.0045  -0.0248 996  ILE B CG2 
15914 C CD1 . ILE B 998  ? 0.2817 0.3021 0.3011 0.0183  0.0024  -0.0266 996  ILE B CD1 
15915 N N   . ASN B 999  ? 0.2044 0.2312 0.2197 0.0117  0.0008  -0.0224 997  ASN B N   
15916 C CA  . ASN B 999  ? 0.2197 0.2479 0.2321 0.0101  0.0004  -0.0211 997  ASN B CA  
15917 C C   . ASN B 999  ? 0.1981 0.2274 0.2124 0.0079  0.0000  -0.0193 997  ASN B C   
15918 O O   . ASN B 999  ? 0.1980 0.2299 0.2104 0.0064  0.0004  -0.0177 997  ASN B O   
15919 C CB  . ASN B 999  ? 0.2146 0.2468 0.2239 0.0110  0.0023  -0.0207 997  ASN B CB  
15920 C CG  . ASN B 999  ? 0.2007 0.2307 0.2066 0.0132  0.0022  -0.0227 997  ASN B CG  
15921 O OD1 . ASN B 999  ? 0.2338 0.2594 0.2385 0.0130  0.0003  -0.0239 997  ASN B OD1 
15922 N ND2 . ASN B 999  ? 0.2313 0.2644 0.2357 0.0154  0.0043  -0.0231 997  ASN B ND2 
15923 N N   . ARG B 1000 ? 0.1932 0.2203 0.2108 0.0076  -0.0009 -0.0197 998  ARG B N   
15924 C CA  . ARG B 1000 ? 0.2065 0.2335 0.2255 0.0059  -0.0015 -0.0184 998  ARG B CA  
15925 C C   . ARG B 1000 ? 0.2161 0.2398 0.2379 0.0061  -0.0029 -0.0194 998  ARG B C   
15926 O O   . ARG B 1000 ? 0.2158 0.2377 0.2386 0.0072  -0.0035 -0.0208 998  ARG B O   
15927 C CB  . ARG B 1000 ? 0.1990 0.2297 0.2199 0.0056  0.0002  -0.0173 998  ARG B CB  
15928 C CG  . ARG B 1000 ? 0.1926 0.2241 0.2162 0.0075  0.0016  -0.0182 998  ARG B CG  
15929 C CD  . ARG B 1000 ? 0.1963 0.2298 0.2224 0.0070  0.0025  -0.0171 998  ARG B CD  
15930 N NE  . ARG B 1000 ? 0.1794 0.2104 0.2071 0.0060  0.0012  -0.0171 998  ARG B NE  
15931 C CZ  . ARG B 1000 ? 0.1950 0.2268 0.2243 0.0054  0.0016  -0.0164 998  ARG B CZ  
15932 N NH1 . ARG B 1000 ? 0.1892 0.2243 0.2193 0.0056  0.0030  -0.0156 998  ARG B NH1 
15933 N NH2 . ARG B 1000 ? 0.1991 0.2284 0.2293 0.0048  0.0006  -0.0166 998  ARG B NH2 
15934 N N   . ASN B 1001 ? 0.1863 0.2092 0.2092 0.0050  -0.0036 -0.0186 999  ASN B N   
15935 C CA  . ASN B 1001 ? 0.2026 0.2233 0.2285 0.0054  -0.0047 -0.0194 999  ASN B CA  
15936 C C   . ASN B 1001 ? 0.1867 0.2087 0.2161 0.0065  -0.0033 -0.0200 999  ASN B C   
15937 O O   . ASN B 1001 ? 0.1841 0.2084 0.2136 0.0069  -0.0016 -0.0196 999  ASN B O   
15938 C CB  . ASN B 1001 ? 0.1930 0.2121 0.2187 0.0045  -0.0058 -0.0187 999  ASN B CB  
15939 C CG  . ASN B 1001 ? 0.2331 0.2540 0.2593 0.0038  -0.0046 -0.0177 999  ASN B CG  
15940 O OD1 . ASN B 1001 ? 0.2186 0.2413 0.2473 0.0045  -0.0031 -0.0179 999  ASN B OD1 
15941 N ND2 . ASN B 1001 ? 0.2928 0.3127 0.3164 0.0022  -0.0053 -0.0165 999  ASN B ND2 
15942 N N   . ILE B 1002 ? 0.1871 0.2078 0.2196 0.0069  -0.0039 -0.0207 1000 ILE B N   
15943 C CA  . ILE B 1002 ? 0.1916 0.2133 0.2272 0.0077  -0.0027 -0.0211 1000 ILE B CA  
15944 C C   . ILE B 1002 ? 0.1886 0.2110 0.2266 0.0075  -0.0021 -0.0206 1000 ILE B C   
15945 O O   . ILE B 1002 ? 0.2105 0.2335 0.2515 0.0080  -0.0014 -0.0208 1000 ILE B O   
15946 C CB  . ILE B 1002 ? 0.1696 0.1898 0.2070 0.0082  -0.0036 -0.0222 1000 ILE B CB  
15947 C CG1 . ILE B 1002 ? 0.1596 0.1786 0.1988 0.0080  -0.0054 -0.0226 1000 ILE B CG1 
15948 C CG2 . ILE B 1002 ? 0.1728 0.1918 0.2071 0.0086  -0.0041 -0.0229 1000 ILE B CG2 
15949 C CD1 . ILE B 1002 ? 0.1774 0.1958 0.2195 0.0081  -0.0063 -0.0234 1000 ILE B CD1 
15950 N N   . ILE B 1003 ? 0.2013 0.2235 0.2378 0.0068  -0.0024 -0.0198 1001 ILE B N   
15951 C CA  . ILE B 1003 ? 0.1926 0.2149 0.2306 0.0069  -0.0021 -0.0196 1001 ILE B CA  
15952 C C   . ILE B 1003 ? 0.2619 0.2854 0.2982 0.0060  -0.0012 -0.0186 1001 ILE B C   
15953 O O   . ILE B 1003 ? 0.3038 0.3284 0.3379 0.0053  -0.0009 -0.0179 1001 ILE B O   
15954 C CB  . ILE B 1003 ? 0.2507 0.2708 0.2885 0.0070  -0.0038 -0.0200 1001 ILE B CB  
15955 C CG1 . ILE B 1003 ? 0.2921 0.3104 0.3258 0.0059  -0.0051 -0.0193 1001 ILE B CG1 
15956 C CG2 . ILE B 1003 ? 0.1969 0.2165 0.2369 0.0078  -0.0050 -0.0209 1001 ILE B CG2 
15957 C CD1 . ILE B 1003 ? 0.3082 0.3236 0.3410 0.0062  -0.0068 -0.0195 1001 ILE B CD1 
15958 N N   . GLY B 1004 ? 0.2366 0.2601 0.2738 0.0062  -0.0007 -0.0185 1002 GLY B N   
15959 C CA  . GLY B 1004 ? 0.2745 0.2985 0.3097 0.0052  -0.0003 -0.0175 1002 GLY B CA  
15960 C C   . GLY B 1004 ? 0.3024 0.3295 0.3381 0.0050  0.0012  -0.0168 1002 GLY B C   
15961 O O   . GLY B 1004 ? 0.2817 0.3101 0.3154 0.0039  0.0013  -0.0158 1002 GLY B O   
15962 N N   . ALA B 1005 ? 0.2732 0.3015 0.3116 0.0061  0.0024  -0.0171 1003 ALA B N   
15963 C CA  . ALA B 1005 ? 0.2079 0.2387 0.2469 0.0064  0.0037  -0.0164 1003 ALA B CA  
15964 C C   . ALA B 1005 ? 0.2698 0.3018 0.3077 0.0055  0.0041  -0.0154 1003 ALA B C   
15965 O O   . ALA B 1005 ? 0.3098 0.3406 0.3476 0.0053  0.0039  -0.0156 1003 ALA B O   
15966 C CB  . ALA B 1005 ? 0.2869 0.3178 0.3287 0.0075  0.0046  -0.0168 1003 ALA B CB  
15967 N N   . VAL B 1006 ? 0.1878 0.2226 0.2249 0.0051  0.0046  -0.0144 1004 VAL B N   
15968 C CA  . VAL B 1006 ? 0.2018 0.2382 0.2376 0.0038  0.0045  -0.0133 1004 VAL B CA  
15969 C C   . VAL B 1006 ? 0.1826 0.2210 0.2200 0.0047  0.0058  -0.0128 1004 VAL B C   
15970 O O   . VAL B 1006 ? 0.1852 0.2252 0.2240 0.0060  0.0067  -0.0127 1004 VAL B O   
15971 C CB  . VAL B 1006 ? 0.2111 0.2499 0.2452 0.0025  0.0042  -0.0122 1004 VAL B CB  
15972 C CG1 . VAL B 1006 ? 0.2296 0.2710 0.2629 0.0011  0.0041  -0.0108 1004 VAL B CG1 
15973 C CG2 . VAL B 1006 ? 0.2436 0.2797 0.2755 0.0013  0.0027  -0.0125 1004 VAL B CG2 
15974 N N   . VAL B 1007 ? 0.1760 0.2140 0.2129 0.0041  0.0057  -0.0125 1005 VAL B N   
15975 C CA  . VAL B 1007 ? 0.1954 0.2351 0.2334 0.0048  0.0067  -0.0118 1005 VAL B CA  
15976 C C   . VAL B 1007 ? 0.1859 0.2294 0.2242 0.0050  0.0072  -0.0106 1005 VAL B C   
15977 O O   . VAL B 1007 ? 0.1874 0.2330 0.2245 0.0036  0.0065  -0.0098 1005 VAL B O   
15978 C CB  . VAL B 1007 ? 0.1642 0.2028 0.2006 0.0040  0.0064  -0.0117 1005 VAL B CB  
15979 C CG1 . VAL B 1007 ? 0.1749 0.2156 0.2119 0.0045  0.0073  -0.0108 1005 VAL B CG1 
15980 C CG2 . VAL B 1007 ? 0.1901 0.2254 0.2266 0.0046  0.0063  -0.0130 1005 VAL B CG2 
15981 N N   . GLY B 1008 ? 0.1977 0.2423 0.2379 0.0066  0.0082  -0.0104 1006 GLY B N   
15982 C CA  . GLY B 1008 ? 0.1822 0.2305 0.2229 0.0074  0.0087  -0.0093 1006 GLY B CA  
15983 C C   . GLY B 1008 ? 0.1806 0.2308 0.2212 0.0079  0.0087  -0.0094 1006 GLY B C   
15984 O O   . GLY B 1008 ? 0.2066 0.2606 0.2478 0.0087  0.0092  -0.0085 1006 GLY B O   
15985 N N   . VAL B 1009 ? 0.1705 0.2183 0.2104 0.0074  0.0083  -0.0105 1007 VAL B N   
15986 C CA  . VAL B 1009 ? 0.1976 0.2468 0.2368 0.0079  0.0084  -0.0107 1007 VAL B CA  
15987 C C   . VAL B 1009 ? 0.1879 0.2337 0.2274 0.0093  0.0084  -0.0123 1007 VAL B C   
15988 O O   . VAL B 1009 ? 0.1860 0.2325 0.2255 0.0111  0.0090  -0.0127 1007 VAL B O   
15989 C CB  . VAL B 1009 ? 0.2196 0.2692 0.2569 0.0056  0.0074  -0.0103 1007 VAL B CB  
15990 C CG1 . VAL B 1009 ? 0.2083 0.2595 0.2446 0.0060  0.0076  -0.0104 1007 VAL B CG1 
15991 C CG2 . VAL B 1009 ? 0.1988 0.2516 0.2356 0.0038  0.0070  -0.0087 1007 VAL B CG2 
15992 N N   . GLN B 1010 ? 0.1709 0.2129 0.2106 0.0087  0.0078  -0.0132 1008 GLN B N   
15993 C CA  . GLN B 1010 ? 0.2039 0.2427 0.2446 0.0098  0.0077  -0.0144 1008 GLN B CA  
15994 C C   . GLN B 1010 ? 0.1794 0.2168 0.2218 0.0097  0.0079  -0.0144 1008 GLN B C   
15995 O O   . GLN B 1010 ? 0.2099 0.2454 0.2527 0.0089  0.0073  -0.0149 1008 GLN B O   
15996 C CB  . GLN B 1010 ? 0.1802 0.2167 0.2199 0.0092  0.0066  -0.0155 1008 GLN B CB  
15997 C CG  . GLN B 1010 ? 0.1938 0.2318 0.2313 0.0090  0.0064  -0.0154 1008 GLN B CG  
15998 C CD  . GLN B 1010 ? 0.1842 0.2232 0.2202 0.0071  0.0057  -0.0145 1008 GLN B CD  
15999 O OE1 . GLN B 1010 ? 0.2323 0.2692 0.2683 0.0060  0.0049  -0.0146 1008 GLN B OE1 
16000 N NE2 . GLN B 1010 ? 0.1938 0.2358 0.2282 0.0066  0.0059  -0.0136 1008 GLN B NE2 
16001 N N   . PRO B 1011 ? 0.2013 0.2396 0.2447 0.0106  0.0087  -0.0137 1009 PRO B N   
16002 C CA  . PRO B 1011 ? 0.1815 0.2183 0.2264 0.0105  0.0091  -0.0136 1009 PRO B CA  
16003 C C   . PRO B 1011 ? 0.1945 0.2284 0.2405 0.0105  0.0086  -0.0147 1009 PRO B C   
16004 O O   . PRO B 1011 ? 0.2025 0.2350 0.2485 0.0111  0.0082  -0.0155 1009 PRO B O   
16005 C CB  . PRO B 1011 ? 0.1835 0.2210 0.2289 0.0119  0.0098  -0.0128 1009 PRO B CB  
16006 C CG  . PRO B 1011 ? 0.2058 0.2464 0.2500 0.0124  0.0100  -0.0121 1009 PRO B CG  
16007 C CD  . PRO B 1011 ? 0.1690 0.2097 0.2121 0.0119  0.0094  -0.0130 1009 PRO B CD  
16008 N N   . PHE B 1012 ? 0.2045 0.2379 0.2517 0.0097  0.0086  -0.0148 1010 PHE B N   
16009 C CA  . PHE B 1012 ? 0.1923 0.2239 0.2407 0.0094  0.0078  -0.0158 1010 PHE B CA  
16010 C C   . PHE B 1012 ? 0.2078 0.2387 0.2587 0.0093  0.0083  -0.0156 1010 PHE B C   
16011 O O   . PHE B 1012 ? 0.2093 0.2414 0.2609 0.0091  0.0093  -0.0148 1010 PHE B O   
16012 C CB  . PHE B 1012 ? 0.1796 0.2114 0.2275 0.0088  0.0073  -0.0162 1010 PHE B CB  
16013 C CG  . PHE B 1012 ? 0.2193 0.2498 0.2686 0.0087  0.0063  -0.0172 1010 PHE B CG  
16014 C CD1 . PHE B 1012 ? 0.2287 0.2580 0.2769 0.0087  0.0051  -0.0179 1010 PHE B CD1 
16015 C CD2 . PHE B 1012 ? 0.2452 0.2759 0.2968 0.0087  0.0066  -0.0173 1010 PHE B CD2 
16016 C CE1 . PHE B 1012 ? 0.2182 0.2464 0.2677 0.0086  0.0040  -0.0188 1010 PHE B CE1 
16017 C CE2 . PHE B 1012 ? 0.2558 0.2860 0.3092 0.0087  0.0056  -0.0181 1010 PHE B CE2 
16018 C CZ  . PHE B 1012 ? 0.2566 0.2854 0.3089 0.0086  0.0042  -0.0188 1010 PHE B CZ  
16019 N N   . GLY B 1013 ? 0.1857 0.2149 0.2378 0.0093  0.0076  -0.0162 1011 GLY B N   
16020 C CA  . GLY B 1013 ? 0.2509 0.2796 0.3056 0.0087  0.0078  -0.0159 1011 GLY B CA  
16021 C C   . GLY B 1013 ? 0.2745 0.3005 0.3293 0.0088  0.0069  -0.0164 1011 GLY B C   
16022 O O   . GLY B 1013 ? 0.2519 0.2766 0.3047 0.0098  0.0066  -0.0167 1011 GLY B O   
16023 N N   . GLY B 1014 ? 0.2886 0.3139 0.3459 0.0078  0.0063  -0.0164 1012 GLY B N   
16024 C CA  . GLY B 1014 ? 0.2548 0.2770 0.3121 0.0075  0.0049  -0.0171 1012 GLY B CA  
16025 C C   . GLY B 1014 ? 0.3066 0.3273 0.3656 0.0065  0.0050  -0.0160 1012 GLY B C   
16026 O O   . GLY B 1014 ? 0.3499 0.3721 0.4097 0.0062  0.0064  -0.0147 1012 GLY B O   
16027 N N   . ARG B 1015 ? 0.3051 0.3229 0.3645 0.0057  0.0035  -0.0166 1013 ARG B N   
16028 C CA  . ARG B 1015 ? 0.3428 0.3581 0.4034 0.0044  0.0031  -0.0157 1013 ARG B CA  
16029 C C   . ARG B 1015 ? 0.3263 0.3423 0.3902 0.0022  0.0018  -0.0157 1013 ARG B C   
16030 O O   . ARG B 1015 ? 0.3060 0.3243 0.3712 0.0022  0.0012  -0.0165 1013 ARG B O   
16031 C CB  . ARG B 1015 ? 0.3763 0.3863 0.4336 0.0054  0.0020  -0.0164 1013 ARG B CB  
16032 C CG  . ARG B 1015 ? 0.3699 0.3779 0.4250 0.0062  0.0005  -0.0184 1013 ARG B CG  
16033 C CD  . ARG B 1015 ? 0.4396 0.4416 0.4923 0.0063  -0.0012 -0.0193 1013 ARG B CD  
16034 N NE  . ARG B 1015 ? 0.4600 0.4604 0.5153 0.0036  -0.0027 -0.0188 1013 ARG B NE  
16035 C CZ  . ARG B 1015 ? 0.4376 0.4389 0.4947 0.0020  -0.0042 -0.0194 1013 ARG B CZ  
16036 N NH1 . ARG B 1015 ? 0.3846 0.3881 0.4412 0.0029  -0.0045 -0.0207 1013 ARG B NH1 
16037 N NH2 . ARG B 1015 ? 0.4487 0.4491 0.5086 -0.0006 -0.0056 -0.0186 1013 ARG B NH2 
16038 N N   . GLY B 1016 ? 0.3049 0.3188 0.3702 0.0004  0.0011  -0.0146 1014 GLY B N   
16039 C CA  . GLY B 1016 ? 0.2896 0.3045 0.3583 -0.0019 -0.0003 -0.0144 1014 GLY B CA  
16040 C C   . GLY B 1016 ? 0.2959 0.3171 0.3686 -0.0025 0.0010  -0.0136 1014 GLY B C   
16041 O O   . GLY B 1016 ? 0.2811 0.3052 0.3545 -0.0022 0.0031  -0.0123 1014 GLY B O   
16042 N N   . LEU B 1017 ? 0.3034 0.3270 0.3786 -0.0031 -0.0003 -0.0144 1015 LEU B N   
16043 C CA  . LEU B 1017 ? 0.2679 0.2976 0.3468 -0.0031 0.0008  -0.0139 1015 LEU B CA  
16044 C C   . LEU B 1017 ? 0.3008 0.3324 0.3778 -0.0007 0.0024  -0.0145 1015 LEU B C   
16045 O O   . LEU B 1017 ? 0.2529 0.2891 0.3324 -0.0002 0.0035  -0.0142 1015 LEU B O   
16046 C CB  . LEU B 1017 ? 0.2817 0.3130 0.3635 -0.0040 -0.0013 -0.0146 1015 LEU B CB  
16047 C CG  . LEU B 1017 ? 0.3420 0.3726 0.4267 -0.0070 -0.0032 -0.0138 1015 LEU B CG  
16048 C CD1 . LEU B 1017 ? 0.4047 0.4378 0.4923 -0.0076 -0.0054 -0.0145 1015 LEU B CD1 
16049 C CD2 . LEU B 1017 ? 0.3195 0.3536 0.4077 -0.0088 -0.0016 -0.0115 1015 LEU B CD2 
16050 N N   . SER B 1018 ? 0.2321 0.2604 0.3048 0.0009  0.0025  -0.0154 1016 SER B N   
16051 C CA  . SER B 1018 ? 0.2574 0.2872 0.3280 0.0028  0.0036  -0.0160 1016 SER B CA  
16052 C C   . SER B 1018 ? 0.2871 0.3183 0.3570 0.0033  0.0058  -0.0148 1016 SER B C   
16053 O O   . SER B 1018 ? 0.2578 0.2905 0.3263 0.0046  0.0068  -0.0151 1016 SER B O   
16054 C CB  . SER B 1018 ? 0.2402 0.2666 0.3068 0.0040  0.0027  -0.0173 1016 SER B CB  
16055 O OG  . SER B 1018 ? 0.2733 0.2991 0.3402 0.0038  0.0007  -0.0185 1016 SER B OG  
16056 N N   . GLY B 1019 ? 0.3039 0.3342 0.3742 0.0023  0.0065  -0.0135 1017 GLY B N   
16057 C CA  . GLY B 1019 ? 0.3044 0.3366 0.3744 0.0026  0.0085  -0.0122 1017 GLY B CA  
16058 C C   . GLY B 1019 ? 0.2912 0.3207 0.3599 0.0020  0.0088  -0.0109 1017 GLY B C   
16059 O O   . GLY B 1019 ? 0.2598 0.2854 0.3278 0.0014  0.0075  -0.0110 1017 GLY B O   
16060 N N   . THR B 1020 ? 0.2068 0.2378 0.2745 0.0024  0.0106  -0.0097 1018 THR B N   
16061 C CA  . THR B 1020 ? 0.2561 0.2847 0.3224 0.0021  0.0110  -0.0081 1018 THR B CA  
16062 C C   . THR B 1020 ? 0.2513 0.2776 0.3139 0.0039  0.0109  -0.0086 1018 THR B C   
16063 O O   . THR B 1020 ? 0.2954 0.3186 0.3565 0.0041  0.0106  -0.0078 1018 THR B O   
16064 C CB  . THR B 1020 ? 0.2511 0.2829 0.3183 0.0014  0.0129  -0.0064 1018 THR B CB  
16065 O OG1 . THR B 1020 ? 0.2418 0.2763 0.3074 0.0029  0.0140  -0.0070 1018 THR B OG1 
16066 C CG2 . THR B 1020 ? 0.2284 0.2634 0.2995 -0.0005 0.0133  -0.0057 1018 THR B CG2 
16067 N N   . GLY B 1021 ? 0.2327 0.2607 0.2940 0.0053  0.0111  -0.0098 1019 GLY B N   
16068 C CA  . GLY B 1021 ? 0.2508 0.2784 0.3092 0.0067  0.0115  -0.0097 1019 GLY B CA  
16069 C C   . GLY B 1021 ? 0.2387 0.2681 0.2966 0.0066  0.0129  -0.0081 1019 GLY B C   
16070 O O   . GLY B 1021 ? 0.2410 0.2720 0.3006 0.0054  0.0138  -0.0071 1019 GLY B O   
16071 N N   . PRO B 1022 ? 0.2075 0.2372 0.2630 0.0078  0.0132  -0.0077 1020 PRO B N   
16072 C CA  . PRO B 1022 ? 0.2236 0.2527 0.2773 0.0092  0.0124  -0.0086 1020 PRO B CA  
16073 C C   . PRO B 1022 ? 0.2148 0.2457 0.2681 0.0093  0.0122  -0.0100 1020 PRO B C   
16074 O O   . PRO B 1022 ? 0.2187 0.2512 0.2729 0.0086  0.0126  -0.0103 1020 PRO B O   
16075 C CB  . PRO B 1022 ? 0.2031 0.2331 0.2550 0.0101  0.0130  -0.0073 1020 PRO B CB  
16076 C CG  . PRO B 1022 ? 0.2156 0.2475 0.2676 0.0090  0.0141  -0.0063 1020 PRO B CG  
16077 C CD  . PRO B 1022 ? 0.2357 0.2669 0.2901 0.0077  0.0143  -0.0062 1020 PRO B CD  
16078 N N   . LYS B 1023 ? 0.1902 0.2210 0.2422 0.0102  0.0115  -0.0109 1021 LYS B N   
16079 C CA  . LYS B 1023 ? 0.1726 0.2046 0.2240 0.0100  0.0110  -0.0120 1021 LYS B CA  
16080 C C   . LYS B 1023 ? 0.2098 0.2440 0.2600 0.0097  0.0115  -0.0116 1021 LYS B C   
16081 O O   . LYS B 1023 ? 0.1631 0.1984 0.2120 0.0100  0.0119  -0.0106 1021 LYS B O   
16082 C CB  . LYS B 1023 ? 0.1585 0.1902 0.2084 0.0110  0.0103  -0.0127 1021 LYS B CB  
16083 C CG  . LYS B 1023 ? 0.1641 0.1933 0.2144 0.0113  0.0095  -0.0137 1021 LYS B CG  
16084 C CD  . LYS B 1023 ? 0.1923 0.2217 0.2407 0.0127  0.0093  -0.0142 1021 LYS B CD  
16085 C CE  . LYS B 1023 ? 0.1972 0.2240 0.2452 0.0130  0.0083  -0.0156 1021 LYS B CE  
16086 N NZ  . LYS B 1023 ? 0.1734 0.2007 0.2213 0.0120  0.0076  -0.0165 1021 LYS B NZ  
16087 N N   . ALA B 1024 ? 0.2090 0.2436 0.2593 0.0091  0.0113  -0.0124 1022 ALA B N   
16088 C CA  . ALA B 1024 ? 0.2002 0.2359 0.2485 0.0089  0.0114  -0.0124 1022 ALA B CA  
16089 C C   . ALA B 1024 ? 0.1975 0.2339 0.2439 0.0089  0.0106  -0.0124 1022 ALA B C   
16090 O O   . ALA B 1024 ? 0.1850 0.2209 0.2315 0.0091  0.0100  -0.0129 1022 ALA B O   
16091 C CB  . ALA B 1024 ? 0.1963 0.2315 0.2450 0.0086  0.0110  -0.0135 1022 ALA B CB  
16092 N N   . GLY B 1025 ? 0.1668 0.2045 0.2114 0.0085  0.0107  -0.0117 1023 GLY B N   
16093 C CA  . GLY B 1025 ? 0.1497 0.1888 0.1928 0.0081  0.0100  -0.0114 1023 GLY B CA  
16094 C C   . GLY B 1025 ? 0.1567 0.1972 0.2005 0.0091  0.0102  -0.0107 1023 GLY B C   
16095 O O   . GLY B 1025 ? 0.1953 0.2372 0.2385 0.0091  0.0098  -0.0107 1023 GLY B O   
16096 N N   . GLY B 1026 ? 0.1733 0.2133 0.2183 0.0100  0.0109  -0.0101 1024 GLY B N   
16097 C CA  . GLY B 1026 ? 0.1475 0.1881 0.1929 0.0114  0.0111  -0.0096 1024 GLY B CA  
16098 C C   . GLY B 1026 ? 0.1606 0.2021 0.2060 0.0119  0.0116  -0.0081 1024 GLY B C   
16099 O O   . GLY B 1026 ? 0.1553 0.1965 0.2003 0.0111  0.0120  -0.0076 1024 GLY B O   
16100 N N   . PRO B 1027 ? 0.1739 0.2163 0.2196 0.0134  0.0117  -0.0074 1025 PRO B N   
16101 C CA  . PRO B 1027 ? 0.1527 0.1965 0.1980 0.0141  0.0119  -0.0058 1025 PRO B CA  
16102 C C   . PRO B 1027 ? 0.1813 0.2222 0.2270 0.0143  0.0123  -0.0051 1025 PRO B C   
16103 O O   . PRO B 1027 ? 0.1888 0.2305 0.2339 0.0146  0.0124  -0.0036 1025 PRO B O   
16104 C CB  . PRO B 1027 ? 0.1836 0.2293 0.2292 0.0161  0.0118  -0.0055 1025 PRO B CB  
16105 C CG  . PRO B 1027 ? 0.2157 0.2588 0.2616 0.0169  0.0118  -0.0071 1025 PRO B CG  
16106 C CD  . PRO B 1027 ? 0.1951 0.2375 0.2409 0.0149  0.0115  -0.0081 1025 PRO B CD  
16107 N N   . LEU B 1028 ? 0.1737 0.2113 0.2202 0.0141  0.0125  -0.0059 1026 LEU B N   
16108 C CA  . LEU B 1028 ? 0.1812 0.2163 0.2282 0.0138  0.0128  -0.0050 1026 LEU B CA  
16109 C C   . LEU B 1028 ? 0.1600 0.1954 0.2071 0.0120  0.0135  -0.0048 1026 LEU B C   
16110 O O   . LEU B 1028 ? 0.2003 0.2345 0.2477 0.0115  0.0140  -0.0037 1026 LEU B O   
16111 C CB  . LEU B 1028 ? 0.1936 0.2250 0.2416 0.0141  0.0125  -0.0058 1026 LEU B CB  
16112 C CG  . LEU B 1028 ? 0.2483 0.2783 0.2956 0.0163  0.0119  -0.0061 1026 LEU B CG  
16113 C CD1 . LEU B 1028 ? 0.2693 0.2948 0.3171 0.0164  0.0113  -0.0070 1026 LEU B CD1 
16114 C CD2 . LEU B 1028 ? 0.2836 0.3140 0.3302 0.0178  0.0120  -0.0045 1026 LEU B CD2 
16115 N N   . TYR B 1029 ? 0.1698 0.2070 0.2166 0.0112  0.0135  -0.0058 1027 TYR B N   
16116 C CA  . TYR B 1029 ? 0.1691 0.2064 0.2161 0.0100  0.0141  -0.0062 1027 TYR B CA  
16117 C C   . TYR B 1029 ? 0.1940 0.2322 0.2396 0.0096  0.0148  -0.0048 1027 TYR B C   
16118 O O   . TYR B 1029 ? 0.1745 0.2123 0.2209 0.0090  0.0157  -0.0042 1027 TYR B O   
16119 C CB  . TYR B 1029 ? 0.1628 0.2011 0.2091 0.0095  0.0136  -0.0075 1027 TYR B CB  
16120 C CG  . TYR B 1029 ? 0.1975 0.2355 0.2445 0.0089  0.0140  -0.0085 1027 TYR B CG  
16121 C CD1 . TYR B 1029 ? 0.1886 0.2255 0.2379 0.0088  0.0140  -0.0093 1027 TYR B CD1 
16122 C CD2 . TYR B 1029 ? 0.1930 0.2318 0.2382 0.0086  0.0143  -0.0088 1027 TYR B CD2 
16123 C CE1 . TYR B 1029 ? 0.1952 0.2325 0.2455 0.0085  0.0143  -0.0101 1027 TYR B CE1 
16124 C CE2 . TYR B 1029 ? 0.1849 0.2235 0.2306 0.0085  0.0147  -0.0099 1027 TYR B CE2 
16125 C CZ  . TYR B 1029 ? 0.2334 0.2716 0.2819 0.0085  0.0147  -0.0105 1027 TYR B CZ  
16126 O OH  . TYR B 1029 ? 0.2486 0.2873 0.2981 0.0087  0.0151  -0.0114 1027 TYR B OH  
16127 N N   . LEU B 1030 ? 0.1766 0.2164 0.2203 0.0099  0.0145  -0.0041 1028 LEU B N   
16128 C CA  . LEU B 1030 ? 0.1788 0.2195 0.2206 0.0095  0.0150  -0.0029 1028 LEU B CA  
16129 C C   . LEU B 1030 ? 0.2070 0.2464 0.2491 0.0097  0.0156  -0.0011 1028 LEU B C   
16130 O O   . LEU B 1030 ? 0.1729 0.2125 0.2140 0.0091  0.0165  -0.0002 1028 LEU B O   
16131 C CB  . LEU B 1030 ? 0.2000 0.2426 0.2396 0.0095  0.0142  -0.0024 1028 LEU B CB  
16132 C CG  . LEU B 1030 ? 0.1990 0.2423 0.2375 0.0088  0.0134  -0.0039 1028 LEU B CG  
16133 C CD1 . LEU B 1030 ? 0.2021 0.2476 0.2387 0.0084  0.0124  -0.0030 1028 LEU B CD1 
16134 C CD2 . LEU B 1030 ? 0.1789 0.2212 0.2162 0.0081  0.0141  -0.0049 1028 LEU B CD2 
16135 N N   . GLY B 1031 ? 0.1979 0.2360 0.2413 0.0107  0.0150  -0.0007 1029 GLY B N   
16136 C CA  . GLY B 1031 ? 0.2131 0.2491 0.2565 0.0110  0.0152  0.0010  1029 GLY B CA  
16137 C C   . GLY B 1031 ? 0.2113 0.2459 0.2559 0.0097  0.0162  0.0014  1029 GLY B C   
16138 O O   . GLY B 1031 ? 0.2402 0.2735 0.2843 0.0092  0.0166  0.0032  1029 GLY B O   
16139 N N   . ARG B 1032 ? 0.1926 0.2276 0.2389 0.0089  0.0165  -0.0001 1030 ARG B N   
16140 C CA  . ARG B 1032 ? 0.1826 0.2172 0.2305 0.0075  0.0175  0.0003  1030 ARG B CA  
16141 C C   . ARG B 1032 ? 0.2127 0.2497 0.2593 0.0068  0.0189  0.0009  1030 ARG B C   
16142 O O   . ARG B 1032 ? 0.2329 0.2704 0.2807 0.0057  0.0200  0.0019  1030 ARG B O   
16143 C CB  . ARG B 1032 ? 0.2108 0.2454 0.2612 0.0072  0.0171  -0.0016 1030 ARG B CB  
16144 C CG  . ARG B 1032 ? 0.2550 0.2894 0.3078 0.0057  0.0178  -0.0011 1030 ARG B CG  
16145 C CD  . ARG B 1032 ? 0.2932 0.3241 0.3467 0.0052  0.0170  0.0001  1030 ARG B CD  
16146 N NE  . ARG B 1032 ? 0.2812 0.3122 0.3376 0.0034  0.0172  0.0004  1030 ARG B NE  
16147 C CZ  . ARG B 1032 ? 0.2992 0.3298 0.3564 0.0018  0.0178  0.0025  1030 ARG B CZ  
16148 N NH1 . ARG B 1032 ? 0.3470 0.3763 0.4019 0.0018  0.0182  0.0044  1030 ARG B NH1 
16149 N NH2 . ARG B 1032 ? 0.3144 0.3460 0.3746 0.0000  0.0180  0.0027  1030 ARG B NH2 
16150 N N   . LEU B 1033 ? 0.2108 0.2494 0.2550 0.0074  0.0188  0.0004  1031 LEU B N   
16151 C CA  . LEU B 1033 ? 0.2112 0.2518 0.2536 0.0070  0.0201  0.0004  1031 LEU B CA  
16152 C C   . LEU B 1033 ? 0.2479 0.2888 0.2873 0.0070  0.0203  0.0024  1031 LEU B C   
16153 O O   . LEU B 1033 ? 0.1986 0.2408 0.2353 0.0069  0.0211  0.0023  1031 LEU B O   
16154 C CB  . LEU B 1033 ? 0.1851 0.2266 0.2262 0.0075  0.0196  -0.0016 1031 LEU B CB  
16155 C CG  . LEU B 1033 ? 0.2146 0.2557 0.2585 0.0076  0.0191  -0.0034 1031 LEU B CG  
16156 C CD1 . LEU B 1033 ? 0.2072 0.2483 0.2496 0.0080  0.0182  -0.0052 1031 LEU B CD1 
16157 C CD2 . LEU B 1033 ? 0.2717 0.3139 0.3181 0.0071  0.0204  -0.0035 1031 LEU B CD2 
16158 N N   . VAL B 1034 ? 0.1921 0.2313 0.2316 0.0071  0.0197  0.0040  1032 VAL B N   
16159 C CA  . VAL B 1034 ? 0.2054 0.2444 0.2422 0.0072  0.0197  0.0062  1032 VAL B CA  
16160 C C   . VAL B 1034 ? 0.2339 0.2706 0.2719 0.0066  0.0199  0.0082  1032 VAL B C   
16161 O O   . VAL B 1034 ? 0.2373 0.2722 0.2780 0.0064  0.0195  0.0078  1032 VAL B O   
16162 C CB  . VAL B 1034 ? 0.2270 0.2663 0.2622 0.0083  0.0181  0.0064  1032 VAL B CB  
16163 C CG1 . VAL B 1034 ? 0.2359 0.2773 0.2691 0.0083  0.0178  0.0049  1032 VAL B CG1 
16164 C CG2 . VAL B 1034 ? 0.2208 0.2586 0.2583 0.0094  0.0169  0.0058  1032 VAL B CG2 
16165 N N   . THR B 1035 ? 0.2214 0.2579 0.2571 0.0062  0.0203  0.0105  1033 THR B N   
16166 C CA  . THR B 1035 ? 0.2618 0.2956 0.2982 0.0053  0.0204  0.0127  1033 THR B CA  
16167 C C   . THR B 1035 ? 0.2830 0.3134 0.3194 0.0066  0.0186  0.0135  1033 THR B C   
16168 O O   . THR B 1035 ? 0.3277 0.3547 0.3653 0.0061  0.0182  0.0145  1033 THR B O   
16169 C CB  . THR B 1035 ? 0.2803 0.3149 0.3140 0.0042  0.0217  0.0151  1033 THR B CB  
16170 O OG1 . THR B 1035 ? 0.3502 0.3859 0.3804 0.0052  0.0211  0.0155  1033 THR B OG1 
16171 C CG2 . THR B 1035 ? 0.3436 0.3814 0.3781 0.0029  0.0238  0.0145  1033 THR B CG2 
16172 N N   . THR B 1036 ? 0.2755 0.3067 0.3106 0.0083  0.0175  0.0130  1034 THR B N   
16173 C CA  . THR B 1036 ? 0.2880 0.3169 0.3235 0.0102  0.0158  0.0133  1034 THR B CA  
16174 C C   . THR B 1036 ? 0.2389 0.2699 0.2757 0.0115  0.0152  0.0108  1034 THR B C   
16175 O O   . THR B 1036 ? 0.2243 0.2586 0.2600 0.0117  0.0151  0.0102  1034 THR B O   
16176 C CB  . THR B 1036 ? 0.3021 0.3308 0.3349 0.0113  0.0150  0.0155  1034 THR B CB  
16177 O OG1 . THR B 1036 ? 0.3409 0.3679 0.3720 0.0098  0.0157  0.0179  1034 THR B OG1 
16178 C CG2 . THR B 1036 ? 0.3095 0.3356 0.3429 0.0137  0.0134  0.0158  1034 THR B CG2 
16179 N N   . ALA B 1037 ? 0.2675 0.2965 0.3064 0.0123  0.0147  0.0096  1035 ALA B N   
16180 C CA  . ALA B 1037 ? 0.2576 0.2887 0.2978 0.0132  0.0143  0.0073  1035 ALA B CA  
16181 C C   . ALA B 1037 ? 0.2699 0.3025 0.3093 0.0154  0.0132  0.0078  1035 ALA B C   
16182 O O   . ALA B 1037 ? 0.2504 0.2808 0.2892 0.0169  0.0124  0.0092  1035 ALA B O   
16183 C CB  . ALA B 1037 ? 0.2503 0.2788 0.2925 0.0133  0.0141  0.0058  1035 ALA B CB  
16184 N N   . PRO B 1038 ? 0.2064 0.2429 0.2459 0.0156  0.0129  0.0067  1036 PRO B N   
16185 C CA  . PRO B 1038 ? 0.2542 0.2933 0.2938 0.0176  0.0119  0.0070  1036 PRO B CA  
16186 C C   . PRO B 1038 ? 0.2274 0.2656 0.2687 0.0194  0.0116  0.0057  1036 PRO B C   
16187 O O   . PRO B 1038 ? 0.2195 0.2550 0.2617 0.0189  0.0120  0.0043  1036 PRO B O   
16188 C CB  . PRO B 1038 ? 0.2212 0.2646 0.2602 0.0163  0.0118  0.0063  1036 PRO B CB  
16189 C CG  . PRO B 1038 ? 0.2166 0.2589 0.2561 0.0146  0.0127  0.0045  1036 PRO B CG  
16190 C CD  . PRO B 1038 ? 0.2143 0.2530 0.2538 0.0139  0.0135  0.0051  1036 PRO B CD  
16191 N N   . VAL B 1039 ? 0.2452 0.2858 0.2868 0.0216  0.0109  0.0061  1037 VAL B N   
16192 C CA  . VAL B 1039 ? 0.2285 0.2694 0.2714 0.0237  0.0107  0.0048  1037 VAL B CA  
16193 C C   . VAL B 1039 ? 0.1919 0.2371 0.2356 0.0224  0.0109  0.0034  1037 VAL B C   
16194 O O   . VAL B 1039 ? 0.2138 0.2637 0.2574 0.0220  0.0105  0.0041  1037 VAL B O   
16195 C CB  . VAL B 1039 ? 0.2305 0.2728 0.2735 0.0269  0.0100  0.0059  1037 VAL B CB  
16196 C CG1 . VAL B 1039 ? 0.2251 0.2676 0.2691 0.0293  0.0101  0.0042  1037 VAL B CG1 
16197 C CG2 . VAL B 1039 ? 0.2268 0.2643 0.2685 0.0280  0.0095  0.0075  1037 VAL B CG2 
16198 N N   . PRO B 1040 ? 0.2258 0.2696 0.2702 0.0217  0.0114  0.0015  1038 PRO B N   
16199 C CA  . PRO B 1040 ? 0.2027 0.2501 0.2475 0.0204  0.0114  0.0004  1038 PRO B CA  
16200 C C   . PRO B 1040 ? 0.1959 0.2480 0.2415 0.0222  0.0111  0.0006  1038 PRO B C   
16201 O O   . PRO B 1040 ? 0.2091 0.2609 0.2551 0.0250  0.0110  0.0010  1038 PRO B O   
16202 C CB  . PRO B 1040 ? 0.2168 0.2609 0.2620 0.0197  0.0118  -0.0015 1038 PRO B CB  
16203 C CG  . PRO B 1040 ? 0.2234 0.2627 0.2684 0.0194  0.0120  -0.0011 1038 PRO B CG  
16204 C CD  . PRO B 1040 ? 0.2271 0.2656 0.2716 0.0215  0.0116  0.0005  1038 PRO B CD  
16205 N N   . PRO B 1041 ? 0.1869 0.2434 0.2327 0.0207  0.0109  0.0005  1039 PRO B N   
16206 C CA  . PRO B 1041 ? 0.1866 0.2483 0.2335 0.0221  0.0108  0.0007  1039 PRO B CA  
16207 C C   . PRO B 1041 ? 0.2101 0.2701 0.2575 0.0243  0.0114  -0.0007 1039 PRO B C   
16208 O O   . PRO B 1041 ? 0.2099 0.2657 0.2567 0.0235  0.0117  -0.0023 1039 PRO B O   
16209 C CB  . PRO B 1041 ? 0.2490 0.3140 0.2957 0.0192  0.0105  0.0005  1039 PRO B CB  
16210 C CG  . PRO B 1041 ? 0.2364 0.2984 0.2816 0.0168  0.0102  0.0006  1039 PRO B CG  
16211 C CD  . PRO B 1041 ? 0.2310 0.2875 0.2759 0.0176  0.0108  0.0000  1039 PRO B CD  
16212 N N   . GLN B 1042 ? 0.1849 0.2481 0.2331 0.0272  0.0115  -0.0003 1040 GLN B N   
16213 C CA  . GLN B 1042 ? 0.2299 0.2924 0.2781 0.0298  0.0121  -0.0017 1040 GLN B CA  
16214 C C   . GLN B 1042 ? 0.2288 0.2836 0.2758 0.0310  0.0121  -0.0029 1040 GLN B C   
16215 O O   . GLN B 1042 ? 0.2320 0.2846 0.2783 0.0325  0.0125  -0.0045 1040 GLN B O   
16216 C CB  . GLN B 1042 ? 0.2725 0.3376 0.3208 0.0281  0.0125  -0.0028 1040 GLN B CB  
16217 C CG  . GLN B 1042 ? 0.2535 0.3260 0.3028 0.0264  0.0124  -0.0015 1040 GLN B CG  
16218 C CD  . GLN B 1042 ? 0.3949 0.4697 0.4440 0.0252  0.0128  -0.0024 1040 GLN B CD  
16219 O OE1 . GLN B 1042 ? 0.4510 0.5245 0.4993 0.0221  0.0124  -0.0028 1040 GLN B OE1 
16220 N NE2 . GLN B 1042 ? 0.4140 0.4917 0.4634 0.0279  0.0136  -0.0028 1040 GLN B NE2 
16221 N N   . HIS B 1043 ? 0.2063 0.2569 0.2528 0.0301  0.0117  -0.0022 1041 HIS B N   
16222 C CA  . HIS B 1043 ? 0.2001 0.2434 0.2455 0.0303  0.0115  -0.0031 1041 HIS B CA  
16223 C C   . HIS B 1043 ? 0.2448 0.2851 0.2895 0.0339  0.0112  -0.0026 1041 HIS B C   
16224 O O   . HIS B 1043 ? 0.2496 0.2884 0.2940 0.0342  0.0107  -0.0010 1041 HIS B O   
16225 C CB  . HIS B 1043 ? 0.1766 0.2171 0.2219 0.0273  0.0114  -0.0024 1041 HIS B CB  
16226 C CG  . HIS B 1043 ? 0.2419 0.2757 0.2866 0.0270  0.0112  -0.0029 1041 HIS B CG  
16227 N ND1 . HIS B 1043 ? 0.2386 0.2697 0.2834 0.0252  0.0112  -0.0044 1041 HIS B ND1 
16228 C CD2 . HIS B 1043 ? 0.2578 0.2869 0.3016 0.0279  0.0107  -0.0019 1041 HIS B CD2 
16229 C CE1 . HIS B 1043 ? 0.2626 0.2880 0.3069 0.0249  0.0108  -0.0044 1041 HIS B CE1 
16230 N NE2 . HIS B 1043 ? 0.2230 0.2470 0.2667 0.0264  0.0105  -0.0028 1041 HIS B NE2 
16231 N N   . SER B 1044 ? 0.2029 0.2424 0.2470 0.0368  0.0113  -0.0040 1042 SER B N   
16232 C CA  . SER B 1044 ? 0.1941 0.2297 0.2370 0.0406  0.0109  -0.0040 1042 SER B CA  
16233 C C   . SER B 1044 ? 0.2137 0.2465 0.2550 0.0428  0.0110  -0.0063 1042 SER B C   
16234 O O   . SER B 1044 ? 0.2231 0.2582 0.2646 0.0415  0.0116  -0.0077 1042 SER B O   
16235 C CB  . SER B 1044 ? 0.2233 0.2644 0.2671 0.0434  0.0109  -0.0024 1042 SER B CB  
16236 O OG  . SER B 1044 ? 0.2060 0.2539 0.2509 0.0450  0.0117  -0.0031 1042 SER B OG  
16237 N N   . SER B 1045 ? 0.2180 0.2458 0.2576 0.0464  0.0105  -0.0068 1043 SER B N   
16238 C CA  . SER B 1045 ? 0.2020 0.2267 0.2395 0.0490  0.0106  -0.0092 1043 SER B CA  
16239 C C   . SER B 1045 ? 0.2005 0.2223 0.2363 0.0541  0.0101  -0.0092 1043 SER B C   
16240 O O   . SER B 1045 ? 0.2144 0.2317 0.2497 0.0546  0.0091  -0.0078 1043 SER B O   
16241 C CB  . SER B 1045 ? 0.2209 0.2377 0.2567 0.0466  0.0097  -0.0107 1043 SER B CB  
16242 O OG  . SER B 1045 ? 0.2370 0.2499 0.2700 0.0495  0.0095  -0.0131 1043 SER B OG  
16243 N N   . VAL B 1046 ? 0.1998 0.2240 0.2346 0.0580  0.0109  -0.0108 1044 VAL B N   
16244 C CA  . VAL B 1046 ? 0.2350 0.2559 0.2678 0.0635  0.0105  -0.0112 1044 VAL B CA  
16245 C C   . VAL B 1046 ? 0.2399 0.2497 0.2687 0.0646  0.0092  -0.0134 1044 VAL B C   
16246 O O   . VAL B 1046 ? 0.2462 0.2511 0.2724 0.0692  0.0086  -0.0140 1044 VAL B O   
16247 C CB  . VAL B 1046 ? 0.2269 0.2561 0.2605 0.0677  0.0120  -0.0118 1044 VAL B CB  
16248 C CG1 . VAL B 1046 ? 0.2457 0.2857 0.2834 0.0662  0.0128  -0.0094 1044 VAL B CG1 
16249 C CG2 . VAL B 1046 ? 0.2180 0.2480 0.2501 0.0674  0.0129  -0.0142 1044 VAL B CG2 
16250 N N   . HIS B 1047 ? 0.2343 0.2399 0.2623 0.0607  0.0088  -0.0145 1045 HIS B N   
16251 C CA  . HIS B 1047 ? 0.2453 0.2402 0.2694 0.0611  0.0073  -0.0165 1045 HIS B CA  
16252 C C   . HIS B 1047 ? 0.2583 0.2455 0.2818 0.0594  0.0056  -0.0149 1045 HIS B C   
16253 O O   . HIS B 1047 ? 0.2720 0.2615 0.2981 0.0557  0.0056  -0.0127 1045 HIS B O   
16254 C CB  . HIS B 1047 ? 0.2825 0.2768 0.3065 0.0572  0.0073  -0.0181 1045 HIS B CB  
16255 C CG  . HIS B 1047 ? 0.3453 0.3288 0.3661 0.0558  0.0054  -0.0195 1045 HIS B CG  
16256 N ND1 . HIS B 1047 ? 0.3441 0.3206 0.3604 0.0594  0.0045  -0.0220 1045 HIS B ND1 
16257 C CD2 . HIS B 1047 ? 0.3436 0.3223 0.3651 0.0512  0.0041  -0.0189 1045 HIS B CD2 
16258 C CE1 . HIS B 1047 ? 0.3574 0.3250 0.3717 0.0568  0.0025  -0.0228 1045 HIS B CE1 
16259 N NE2 . HIS B 1047 ? 0.2588 0.2279 0.2765 0.0517  0.0023  -0.0208 1045 HIS B NE2 
16260 N N   . THR B 1048 ? 0.2729 0.2505 0.2925 0.0622  0.0040  -0.0160 1046 THR B N   
16261 C CA  . THR B 1048 ? 0.3062 0.2750 0.3246 0.0601  0.0021  -0.0146 1046 THR B CA  
16262 C C   . THR B 1048 ? 0.2846 0.2438 0.2996 0.0584  0.0004  -0.0167 1046 THR B C   
16263 O O   . THR B 1048 ? 0.3037 0.2585 0.3151 0.0619  -0.0001 -0.0193 1046 THR B O   
16264 C CB  . THR B 1048 ? 0.3080 0.2727 0.3243 0.0647  0.0012  -0.0135 1046 THR B CB  
16265 O OG1 . THR B 1048 ? 0.3152 0.2897 0.3347 0.0668  0.0027  -0.0118 1046 THR B OG1 
16266 C CG2 . THR B 1048 ? 0.3242 0.2807 0.3396 0.0619  -0.0007 -0.0114 1046 THR B CG2 
16267 N N   . ASP B 1049 ? 0.2565 0.2128 0.2728 0.0530  -0.0005 -0.0155 1047 ASP B N   
16268 C CA  . ASP B 1049 ? 0.2535 0.2013 0.2672 0.0507  -0.0023 -0.0172 1047 ASP B CA  
16269 C C   . ASP B 1049 ? 0.2470 0.1834 0.2556 0.0540  -0.0045 -0.0181 1047 ASP B C   
16270 O O   . ASP B 1049 ? 0.2779 0.2107 0.2860 0.0549  -0.0052 -0.0160 1047 ASP B O   
16271 C CB  . ASP B 1049 ? 0.2660 0.2133 0.2825 0.0445  -0.0029 -0.0154 1047 ASP B CB  
16272 C CG  . ASP B 1049 ? 0.2533 0.1928 0.2677 0.0417  -0.0049 -0.0170 1047 ASP B CG  
16273 O OD1 . ASP B 1049 ? 0.2817 0.2112 0.2928 0.0417  -0.0071 -0.0168 1047 ASP B OD1 
16274 O OD2 . ASP B 1049 ? 0.2763 0.2192 0.2919 0.0396  -0.0045 -0.0184 1047 ASP B OD2 
16275 N N   . PRO B 1050 ? 0.2663 0.1967 0.2708 0.0562  -0.0055 -0.0212 1048 PRO B N   
16276 C CA  . PRO B 1050 ? 0.3216 0.2407 0.3206 0.0601  -0.0076 -0.0223 1048 PRO B CA  
16277 C C   . PRO B 1050 ? 0.3034 0.2121 0.3009 0.0560  -0.0104 -0.0209 1048 PRO B C   
16278 O O   . PRO B 1050 ? 0.3341 0.2339 0.3280 0.0584  -0.0122 -0.0204 1048 PRO B O   
16279 C CB  . PRO B 1050 ? 0.3629 0.2794 0.3579 0.0630  -0.0078 -0.0262 1048 PRO B CB  
16280 C CG  . PRO B 1050 ? 0.3186 0.2407 0.3166 0.0582  -0.0071 -0.0267 1048 PRO B CG  
16281 C CD  . PRO B 1050 ? 0.2858 0.2193 0.2899 0.0558  -0.0048 -0.0239 1048 PRO B CD  
16282 N N   . VAL B 1051 ? 0.3311 0.2407 0.3312 0.0498  -0.0109 -0.0202 1049 VAL B N   
16283 C CA  . VAL B 1051 ? 0.3263 0.2271 0.3254 0.0453  -0.0134 -0.0185 1049 VAL B CA  
16284 C C   . VAL B 1051 ? 0.2867 0.1897 0.2885 0.0440  -0.0128 -0.0146 1049 VAL B C   
16285 O O   . VAL B 1051 ? 0.3271 0.2211 0.3262 0.0433  -0.0149 -0.0130 1049 VAL B O   
16286 C CB  . VAL B 1051 ? 0.3017 0.2038 0.3033 0.0393  -0.0139 -0.0187 1049 VAL B CB  
16287 C CG1 . VAL B 1051 ? 0.3363 0.2303 0.3375 0.0343  -0.0165 -0.0166 1049 VAL B CG1 
16288 C CG2 . VAL B 1051 ? 0.3305 0.2297 0.3288 0.0408  -0.0148 -0.0226 1049 VAL B CG2 
16289 N N   . LEU B 1052 ? 0.2878 0.2022 0.2943 0.0436  -0.0102 -0.0131 1050 LEU B N   
16290 C CA  . LEU B 1052 ? 0.2767 0.1936 0.2849 0.0434  -0.0095 -0.0097 1050 LEU B CA  
16291 C C   . LEU B 1052 ? 0.3258 0.2361 0.3300 0.0489  -0.0106 -0.0096 1050 LEU B C   
16292 O O   . LEU B 1052 ? 0.2972 0.2015 0.2999 0.0481  -0.0121 -0.0071 1050 LEU B O   
16293 C CB  . LEU B 1052 ? 0.2332 0.1633 0.2462 0.0434  -0.0066 -0.0088 1050 LEU B CB  
16294 C CG  . LEU B 1052 ? 0.2497 0.1847 0.2648 0.0435  -0.0056 -0.0055 1050 LEU B CG  
16295 C CD1 . LEU B 1052 ? 0.2953 0.2297 0.3083 0.0496  -0.0056 -0.0054 1050 LEU B CD1 
16296 C CD2 . LEU B 1052 ? 0.2811 0.2109 0.2962 0.0389  -0.0068 -0.0025 1050 LEU B CD2 
16297 N N   . LEU B 1053 ? 0.2972 0.2088 0.2994 0.0547  -0.0100 -0.0122 1051 LEU B N   
16298 C CA  . LEU B 1053 ? 0.3377 0.2436 0.3361 0.0606  -0.0110 -0.0123 1051 LEU B CA  
16299 C C   . LEU B 1053 ? 0.3077 0.1985 0.3006 0.0603  -0.0143 -0.0126 1051 LEU B C   
16300 O O   . LEU B 1053 ? 0.3674 0.2518 0.3581 0.0619  -0.0158 -0.0107 1051 LEU B O   
16301 C CB  . LEU B 1053 ? 0.3462 0.2565 0.3434 0.0668  -0.0096 -0.0153 1051 LEU B CB  
16302 C CG  . LEU B 1053 ? 0.3226 0.2473 0.3248 0.0683  -0.0066 -0.0145 1051 LEU B CG  
16303 C CD1 . LEU B 1053 ? 0.3737 0.3029 0.3748 0.0734  -0.0051 -0.0176 1051 LEU B CD1 
16304 C CD2 . LEU B 1053 ? 0.3608 0.2880 0.3642 0.0706  -0.0064 -0.0115 1051 LEU B CD2 
16305 N N   . ASP B 1054 ? 0.3565 0.2413 0.3471 0.0582  -0.0157 -0.0151 1052 ASP B N   
16306 C CA  . ASP B 1054 ? 0.4173 0.2873 0.4025 0.0571  -0.0192 -0.0155 1052 ASP B CA  
16307 C C   . ASP B 1054 ? 0.3781 0.2445 0.3647 0.0515  -0.0205 -0.0115 1052 ASP B C   
16308 O O   . ASP B 1054 ? 0.3983 0.2539 0.3809 0.0523  -0.0230 -0.0102 1052 ASP B O   
16309 C CB  . ASP B 1054 ? 0.3760 0.2418 0.3592 0.0546  -0.0204 -0.0185 1052 ASP B CB  
16310 C CG  . ASP B 1054 ? 0.4446 0.3100 0.4242 0.0607  -0.0198 -0.0227 1052 ASP B CG  
16311 O OD1 . ASP B 1054 ? 0.4227 0.2893 0.4008 0.0671  -0.0189 -0.0232 1052 ASP B OD1 
16312 O OD2 . ASP B 1054 ? 0.4723 0.3364 0.4505 0.0593  -0.0204 -0.0253 1052 ASP B OD2 
16313 N N   . PHE B 1055 ? 0.3676 0.2431 0.3598 0.0460  -0.0188 -0.0094 1053 PHE B N   
16314 C CA  . PHE B 1055 ? 0.3453 0.2193 0.3393 0.0407  -0.0195 -0.0054 1053 PHE B CA  
16315 C C   . PHE B 1055 ? 0.3903 0.2643 0.3837 0.0438  -0.0192 -0.0026 1053 PHE B C   
16316 O O   . PHE B 1055 ? 0.3448 0.2104 0.3358 0.0420  -0.0213 0.0000  1053 PHE B O   
16317 C CB  . PHE B 1055 ? 0.3330 0.2182 0.3332 0.0354  -0.0172 -0.0041 1053 PHE B CB  
16318 C CG  . PHE B 1055 ? 0.2981 0.1831 0.3004 0.0297  -0.0176 -0.0001 1053 PHE B CG  
16319 C CD1 . PHE B 1055 ? 0.3691 0.2435 0.3688 0.0258  -0.0204 0.0011  1053 PHE B CD1 
16320 C CD2 . PHE B 1055 ? 0.3350 0.2304 0.3418 0.0280  -0.0150 0.0024  1053 PHE B CD2 
16321 C CE1 . PHE B 1055 ? 0.3604 0.2351 0.3620 0.0204  -0.0206 0.0051  1053 PHE B CE1 
16322 C CE2 . PHE B 1055 ? 0.3146 0.2102 0.3231 0.0229  -0.0151 0.0060  1053 PHE B CE2 
16323 C CZ  . PHE B 1055 ? 0.3235 0.2090 0.3295 0.0191  -0.0178 0.0075  1053 PHE B CZ  
16324 N N   . ALA B 1056 ? 0.3433 0.2266 0.3388 0.0483  -0.0169 -0.0030 1054 ALA B N   
16325 C CA  . ALA B 1056 ? 0.3766 0.2607 0.3718 0.0513  -0.0167 -0.0003 1054 ALA B CA  
16326 C C   . ALA B 1056 ? 0.3575 0.2287 0.3466 0.0559  -0.0195 -0.0007 1054 ALA B C   
16327 O O   . ALA B 1056 ? 0.4104 0.2765 0.3978 0.0558  -0.0209 0.0023  1054 ALA B O   
16328 C CB  . ALA B 1056 ? 0.3567 0.2533 0.3553 0.0553  -0.0139 -0.0009 1054 ALA B CB  
16329 N N   . LYS B 1057 ? 0.4172 0.2830 0.4027 0.0601  -0.0204 -0.0045 1055 LYS B N   
16330 C CA  . LYS B 1057 ? 0.4607 0.3132 0.4397 0.0649  -0.0232 -0.0053 1055 LYS B CA  
16331 C C   . LYS B 1057 ? 0.4852 0.3246 0.4607 0.0599  -0.0265 -0.0035 1055 LYS B C   
16332 O O   . LYS B 1057 ? 0.4782 0.3080 0.4498 0.0617  -0.0288 -0.0016 1055 LYS B O   
16333 C CB  . LYS B 1057 ? 0.4796 0.3291 0.4551 0.0702  -0.0234 -0.0100 1055 LYS B CB  
16334 C CG  . LYS B 1057 ? 0.5244 0.3828 0.5012 0.0775  -0.0210 -0.0115 1055 LYS B CG  
16335 C CD  . LYS B 1057 ? 0.5017 0.3563 0.4743 0.0827  -0.0212 -0.0162 1055 LYS B CD  
16336 C CE  . LYS B 1057 ? 0.4661 0.3219 0.4395 0.0779  -0.0209 -0.0184 1055 LYS B CE  
16337 N NZ  . LYS B 1057 ? 0.5023 0.3592 0.4730 0.0830  -0.0199 -0.0228 1055 LYS B NZ  
16338 N N   . TRP B 1058 ? 0.4567 0.2954 0.4334 0.0537  -0.0269 -0.0040 1056 TRP B N   
16339 C CA  . TRP B 1058 ? 0.4590 0.2868 0.4334 0.0478  -0.0299 -0.0019 1056 TRP B CA  
16340 C C   . TRP B 1058 ? 0.4642 0.2935 0.4405 0.0444  -0.0298 0.0031  1056 TRP B C   
16341 O O   . TRP B 1058 ? 0.5318 0.3496 0.5040 0.0432  -0.0326 0.0053  1056 TRP B O   
16342 C CB  . TRP B 1058 ? 0.4260 0.2567 0.4032 0.0415  -0.0298 -0.0030 1056 TRP B CB  
16343 C CG  . TRP B 1058 ? 0.5256 0.3472 0.5014 0.0346  -0.0326 -0.0007 1056 TRP B CG  
16344 C CD1 . TRP B 1058 ? 0.5503 0.3572 0.5202 0.0337  -0.0364 -0.0019 1056 TRP B CD1 
16345 C CD2 . TRP B 1058 ? 0.4732 0.2999 0.4535 0.0274  -0.0319 0.0033  1056 TRP B CD2 
16346 N NE1 . TRP B 1058 ? 0.5309 0.3338 0.5017 0.0261  -0.0382 0.0013  1056 TRP B NE1 
16347 C CE2 . TRP B 1058 ? 0.5351 0.3503 0.5124 0.0223  -0.0354 0.0046  1056 TRP B CE2 
16348 C CE3 . TRP B 1058 ? 0.4663 0.3061 0.4527 0.0250  -0.0287 0.0059  1056 TRP B CE3 
16349 C CZ2 . TRP B 1058 ? 0.5109 0.3282 0.4915 0.0147  -0.0355 0.0085  1056 TRP B CZ2 
16350 C CZ3 . TRP B 1058 ? 0.5394 0.3810 0.5288 0.0178  -0.0287 0.0096  1056 TRP B CZ3 
16351 C CH2 . TRP B 1058 ? 0.4555 0.2862 0.4421 0.0128  -0.0320 0.0109  1056 TRP B CH2 
16352 N N   . LEU B 1059 ? 0.4167 0.2598 0.3990 0.0429  -0.0266 0.0049  1057 LEU B N   
16353 C CA  . LEU B 1059 ? 0.4325 0.2779 0.4164 0.0401  -0.0262 0.0095  1057 LEU B CA  
16354 C C   . LEU B 1059 ? 0.5340 0.3730 0.5138 0.0458  -0.0276 0.0108  1057 LEU B C   
16355 O O   . LEU B 1059 ? 0.5346 0.3670 0.5122 0.0436  -0.0293 0.0144  1057 LEU B O   
16356 C CB  . LEU B 1059 ? 0.4093 0.2705 0.3995 0.0386  -0.0225 0.0105  1057 LEU B CB  
16357 C CG  . LEU B 1059 ? 0.4024 0.2707 0.3972 0.0324  -0.0210 0.0103  1057 LEU B CG  
16358 C CD1 . LEU B 1059 ? 0.3952 0.2781 0.3953 0.0322  -0.0175 0.0110  1057 LEU B CD1 
16359 C CD2 . LEU B 1059 ? 0.4099 0.2724 0.4043 0.0256  -0.0226 0.0136  1057 LEU B CD2 
16360 N N   . ASP B 1060 ? 0.5118 0.3532 0.4906 0.0532  -0.0268 0.0081  1058 ASP B N   
16361 C CA  . ASP B 1060 ? 0.5381 0.3743 0.5134 0.0592  -0.0282 0.0093  1058 ASP B CA  
16362 C C   . ASP B 1060 ? 0.5528 0.3713 0.5210 0.0603  -0.0322 0.0091  1058 ASP B C   
16363 O O   . ASP B 1060 ? 0.6197 0.4308 0.5848 0.0610  -0.0342 0.0122  1058 ASP B O   
16364 C CB  . ASP B 1060 ? 0.5224 0.3664 0.4989 0.0669  -0.0263 0.0064  1058 ASP B CB  
16365 C CG  . ASP B 1060 ? 0.5260 0.3838 0.5076 0.0677  -0.0236 0.0086  1058 ASP B CG  
16366 O OD1 . ASP B 1060 ? 0.6512 0.5087 0.6330 0.0655  -0.0241 0.0125  1058 ASP B OD1 
16367 O OD2 . ASP B 1060 ? 0.5636 0.4325 0.5487 0.0704  -0.0211 0.0064  1058 ASP B OD2 
16368 N N   . GLY B 1061 ? 0.5413 0.3526 0.5065 0.0605  -0.0336 0.0055  1059 GLY B N   
16369 C CA  . GLY B 1061 ? 0.6216 0.4151 0.5796 0.0608  -0.0377 0.0051  1059 GLY B CA  
16370 C C   . GLY B 1061 ? 0.6658 0.4523 0.6230 0.0530  -0.0398 0.0093  1059 GLY B C   
16371 O O   . GLY B 1061 ? 0.7366 0.5082 0.6878 0.0531  -0.0434 0.0104  1059 GLY B O   
16372 N N   . LYS B 1062 ? 0.6219 0.4189 0.5850 0.0464  -0.0376 0.0118  1060 LYS B N   
16373 C CA  . LYS B 1062 ? 0.6354 0.4289 0.5990 0.0385  -0.0388 0.0161  1060 LYS B CA  
16374 C C   . LYS B 1062 ? 0.6763 0.4728 0.6407 0.0384  -0.0382 0.0207  1060 LYS B C   
16375 O O   . LYS B 1062 ? 0.7299 0.5223 0.6937 0.0324  -0.0393 0.0247  1060 LYS B O   
16376 C CB  . LYS B 1062 ? 0.6092 0.4133 0.5788 0.0319  -0.0365 0.0159  1060 LYS B CB  
16377 C CG  . LYS B 1062 ? 0.7285 0.5290 0.6989 0.0232  -0.0379 0.0195  1060 LYS B CG  
16378 C CD  . LYS B 1062 ? 0.6210 0.4322 0.5973 0.0180  -0.0356 0.0185  1060 LYS B CD  
16379 C CE  . LYS B 1062 ? 0.6294 0.4368 0.6065 0.0094  -0.0372 0.0217  1060 LYS B CE  
16380 N NZ  . LYS B 1062 ? 0.6663 0.4781 0.6453 0.0061  -0.0360 0.0268  1060 LYS B NZ  
16381 N N   . GLY B 1063 ? 0.6466 0.4503 0.6122 0.0448  -0.0364 0.0203  1061 GLY B N   
16382 C CA  . GLY B 1063 ? 0.5821 0.3894 0.5484 0.0450  -0.0358 0.0245  1061 GLY B CA  
16383 C C   . GLY B 1063 ? 0.6574 0.4795 0.6301 0.0403  -0.0323 0.0267  1061 GLY B C   
16384 O O   . GLY B 1063 ? 0.6597 0.4853 0.6329 0.0398  -0.0317 0.0304  1061 GLY B O   
16385 N N   . ALA B 1064 ? 0.6258 0.4567 0.6031 0.0370  -0.0300 0.0245  1062 ALA B N   
16386 C CA  . ALA B 1064 ? 0.5638 0.4088 0.5470 0.0329  -0.0267 0.0262  1062 ALA B CA  
16387 C C   . ALA B 1064 ? 0.5998 0.4565 0.5861 0.0384  -0.0241 0.0245  1062 ALA B C   
16388 O O   . ALA B 1064 ? 0.5115 0.3775 0.5017 0.0388  -0.0218 0.0216  1062 ALA B O   
16389 C CB  . ALA B 1064 ? 0.5041 0.3528 0.4907 0.0272  -0.0257 0.0247  1062 ALA B CB  
16390 N N   . ARG B 1065 ? 0.6349 0.4910 0.6194 0.0426  -0.0246 0.0265  1063 ARG B N   
16391 C CA  . ARG B 1065 ? 0.5993 0.4646 0.5859 0.0488  -0.0229 0.0249  1063 ARG B CA  
16392 C C   . ARG B 1065 ? 0.5570 0.4373 0.5492 0.0461  -0.0196 0.0254  1063 ARG B C   
16393 O O   . ARG B 1065 ? 0.5637 0.4533 0.5590 0.0493  -0.0177 0.0229  1063 ARG B O   
16394 C CB  . ARG B 1065 ? 0.6158 0.4764 0.5990 0.0538  -0.0247 0.0272  1063 ARG B CB  
16395 N N   . ALA B 1066 ? 0.5002 0.3830 0.4937 0.0402  -0.0188 0.0288  1064 ALA B N   
16396 C CA  . ALA B 1066 ? 0.4858 0.3819 0.4841 0.0375  -0.0157 0.0290  1064 ALA B CA  
16397 C C   . ALA B 1066 ? 0.5075 0.4090 0.5093 0.0355  -0.0141 0.0256  1064 ALA B C   
16398 O O   . ALA B 1066 ? 0.4509 0.3628 0.4563 0.0369  -0.0119 0.0237  1064 ALA B O   
16399 C CB  . ALA B 1066 ? 0.5196 0.4167 0.5180 0.0316  -0.0152 0.0332  1064 ALA B CB  
16400 N N   . GLU B 1067 ? 0.4469 0.3411 0.4477 0.0321  -0.0153 0.0247  1065 GLU B N   
16401 C CA  . GLU B 1067 ? 0.4624 0.3613 0.4664 0.0301  -0.0139 0.0216  1065 GLU B CA  
16402 C C   . GLU B 1067 ? 0.4209 0.3205 0.4245 0.0357  -0.0139 0.0175  1065 GLU B C   
16403 O O   . GLU B 1067 ? 0.4163 0.3246 0.4234 0.0359  -0.0119 0.0151  1065 GLU B O   
16404 C CB  . GLU B 1067 ? 0.4672 0.3583 0.4701 0.0248  -0.0155 0.0219  1065 GLU B CB  
16405 C CG  . GLU B 1067 ? 0.3863 0.2802 0.3911 0.0182  -0.0146 0.0257  1065 GLU B CG  
16406 C CD  . GLU B 1067 ? 0.5023 0.3893 0.5035 0.0176  -0.0162 0.0298  1065 GLU B CD  
16407 O OE1 . GLU B 1067 ? 0.4840 0.3630 0.4811 0.0222  -0.0183 0.0296  1065 GLU B OE1 
16408 O OE2 . GLU B 1067 ? 0.4875 0.3771 0.4898 0.0126  -0.0154 0.0332  1065 GLU B OE2 
16409 N N   . ALA B 1068 ? 0.4333 0.3236 0.4326 0.0405  -0.0162 0.0166  1066 ALA B N   
16410 C CA  . ALA B 1068 ? 0.4489 0.3404 0.4476 0.0465  -0.0159 0.0128  1066 ALA B CA  
16411 C C   . ALA B 1068 ? 0.4355 0.3398 0.4379 0.0497  -0.0134 0.0126  1066 ALA B C   
16412 O O   . ALA B 1068 ? 0.4065 0.3178 0.4112 0.0514  -0.0118 0.0096  1066 ALA B O   
16413 C CB  . ALA B 1068 ? 0.4401 0.3198 0.4333 0.0518  -0.0186 0.0123  1066 ALA B CB  
16414 N N   . GLU B 1069 ? 0.4396 0.3471 0.4425 0.0501  -0.0132 0.0158  1067 GLU B N   
16415 C CA  . GLU B 1069 ? 0.4663 0.3861 0.4727 0.0521  -0.0110 0.0160  1067 GLU B CA  
16416 C C   . GLU B 1069 ? 0.4448 0.3744 0.4556 0.0475  -0.0086 0.0153  1067 GLU B C   
16417 O O   . GLU B 1069 ? 0.3990 0.3374 0.4126 0.0494  -0.0069 0.0132  1067 GLU B O   
16418 C CB  . GLU B 1069 ? 0.4859 0.4062 0.4914 0.0524  -0.0117 0.0199  1067 GLU B CB  
16419 C CG  . GLU B 1069 ? 0.4921 0.4250 0.5012 0.0531  -0.0097 0.0208  1067 GLU B CG  
16420 C CD  . GLU B 1069 ? 0.6422 0.5802 0.6522 0.0596  -0.0095 0.0190  1067 GLU B CD  
16421 O OE1 . GLU B 1069 ? 0.6741 0.6055 0.6817 0.0641  -0.0107 0.0170  1067 GLU B OE1 
16422 O OE2 . GLU B 1069 ? 0.7304 0.6788 0.7434 0.0603  -0.0081 0.0196  1067 GLU B OE2 
16423 N N   . ALA B 1070 ? 0.3928 0.3212 0.4042 0.0415  -0.0084 0.0170  1068 ALA B N   
16424 C CA  . ALA B 1070 ? 0.4227 0.3597 0.4380 0.0374  -0.0061 0.0163  1068 ALA B CA  
16425 C C   . ALA B 1070 ? 0.3330 0.2708 0.3495 0.0379  -0.0057 0.0125  1068 ALA B C   
16426 O O   . ALA B 1070 ? 0.3328 0.2794 0.3524 0.0374  -0.0038 0.0109  1068 ALA B O   
16427 C CB  . ALA B 1070 ? 0.4541 0.3889 0.4696 0.0312  -0.0061 0.0188  1068 ALA B CB  
16428 N N   . ALA B 1071 ? 0.3447 0.2729 0.3582 0.0389  -0.0076 0.0109  1069 ALA B N   
16429 C CA  . ALA B 1071 ? 0.3310 0.2593 0.3450 0.0394  -0.0074 0.0073  1069 ALA B CA  
16430 C C   . ALA B 1071 ? 0.3204 0.2552 0.3352 0.0447  -0.0062 0.0049  1069 ALA B C   
16431 O O   . ALA B 1071 ? 0.3068 0.2489 0.3243 0.0441  -0.0045 0.0030  1069 ALA B O   
16432 C CB  . ALA B 1071 ? 0.3184 0.2343 0.3284 0.0396  -0.0100 0.0061  1069 ALA B CB  
16433 N N   . ARG B 1072 ? 0.3080 0.2406 0.3206 0.0500  -0.0069 0.0053  1070 ARG B N   
16434 C CA  A ARG B 1072 ? 0.3398 0.2795 0.3535 0.0552  -0.0057 0.0035  1070 ARG B CA  
16435 C CA  B ARG B 1072 ? 0.3397 0.2794 0.3534 0.0552  -0.0057 0.0034  1070 ARG B CA  
16436 C C   . ARG B 1072 ? 0.3154 0.2678 0.3336 0.0535  -0.0034 0.0043  1070 ARG B C   
16437 O O   . ARG B 1072 ? 0.3153 0.2749 0.3356 0.0548  -0.0019 0.0022  1070 ARG B O   
16438 C CB  A ARG B 1072 ? 0.3755 0.3116 0.3867 0.0611  -0.0069 0.0044  1070 ARG B CB  
16439 C CB  B ARG B 1072 ? 0.3758 0.3116 0.3869 0.0611  -0.0070 0.0042  1070 ARG B CB  
16440 C CG  A ARG B 1072 ? 0.3898 0.3129 0.3958 0.0640  -0.0093 0.0030  1070 ARG B CG  
16441 C CG  B ARG B 1072 ? 0.3894 0.3121 0.3955 0.0635  -0.0093 0.0028  1070 ARG B CG  
16442 C CD  A ARG B 1072 ? 0.3853 0.3059 0.3891 0.0707  -0.0104 0.0036  1070 ARG B CD  
16443 C CD  B ARG B 1072 ? 0.3908 0.3104 0.3941 0.0708  -0.0103 0.0023  1070 ARG B CD  
16444 N NE  A ARG B 1072 ? 0.4134 0.3347 0.4176 0.0698  -0.0110 0.0075  1070 ARG B NE  
16445 N NE  B ARG B 1072 ? 0.3904 0.2979 0.3887 0.0732  -0.0124 -0.0001 1070 ARG B NE  
16446 C CZ  A ARG B 1072 ? 0.4273 0.3381 0.4278 0.0693  -0.0133 0.0097  1070 ARG B CZ  
16447 C CZ  B ARG B 1072 ? 0.3999 0.2948 0.3939 0.0727  -0.0150 0.0012  1070 ARG B CZ  
16448 N NH1 A ARG B 1072 ? 0.3902 0.2885 0.3862 0.0698  -0.0155 0.0085  1070 ARG B NH1 
16449 N NH1 B ARG B 1072 ? 0.4269 0.3199 0.4209 0.0705  -0.0160 0.0050  1070 ARG B NH1 
16450 N NH2 A ARG B 1072 ? 0.4568 0.3695 0.4579 0.0682  -0.0137 0.0134  1070 ARG B NH2 
16451 N NH2 B ARG B 1072 ? 0.4523 0.3359 0.4415 0.0743  -0.0170 -0.0013 1070 ARG B NH2 
16452 N N   . ASN B 1073 ? 0.2989 0.2538 0.3183 0.0505  -0.0032 0.0074  1071 ASN B N   
16453 C CA  . ASN B 1073 ? 0.3182 0.2843 0.3413 0.0487  -0.0013 0.0082  1071 ASN B CA  
16454 C C   . ASN B 1073 ? 0.3306 0.3007 0.3560 0.0446  0.0001  0.0066  1071 ASN B C   
16455 O O   . ASN B 1073 ? 0.2981 0.2770 0.3262 0.0445  0.0017  0.0057  1071 ASN B O   
16456 C CB  . ASN B 1073 ? 0.3261 0.2928 0.3491 0.0464  -0.0015 0.0118  1071 ASN B CB  
16457 C CG  . ASN B 1073 ? 0.4302 0.3960 0.4516 0.0508  -0.0026 0.0136  1071 ASN B CG  
16458 O OD1 . ASN B 1073 ? 0.4990 0.4658 0.5202 0.0559  -0.0029 0.0121  1071 ASN B OD1 
16459 N ND2 . ASN B 1073 ? 0.4307 0.3949 0.4510 0.0491  -0.0033 0.0168  1071 ASN B ND2 
16460 N N   . ALA B 1074 ? 0.3154 0.2793 0.3400 0.0411  -0.0005 0.0062  1072 ALA B N   
16461 C CA  . ALA B 1074 ? 0.2669 0.2342 0.2938 0.0376  0.0006  0.0045  1072 ALA B CA  
16462 C C   . ALA B 1074 ? 0.2339 0.2030 0.2608 0.0406  0.0009  0.0012  1072 ALA B C   
16463 O O   . ALA B 1074 ? 0.2588 0.2350 0.2881 0.0395  0.0023  -0.0001 1072 ALA B O   
16464 C CB  . ALA B 1074 ? 0.2691 0.2294 0.2953 0.0335  -0.0005 0.0049  1072 ALA B CB  
16465 N N   . GLY B 1075 ? 0.2563 0.2186 0.2802 0.0444  -0.0004 -0.0002 1073 GLY B N   
16466 C CA  . GLY B 1075 ? 0.3014 0.2651 0.3246 0.0476  0.0000  -0.0033 1073 GLY B CA  
16467 C C   . GLY B 1075 ? 0.3402 0.3144 0.3659 0.0501  0.0018  -0.0035 1073 GLY B C   
16468 O O   . GLY B 1075 ? 0.3273 0.3066 0.3541 0.0503  0.0029  -0.0055 1073 GLY B O   
16469 N N   . SER B 1076 ? 0.2943 0.2719 0.3206 0.0519  0.0019  -0.0013 1074 SER B N   
16470 C CA  . SER B 1076 ? 0.2631 0.2510 0.2920 0.0539  0.0034  -0.0011 1074 SER B CA  
16471 C C   . SER B 1076 ? 0.3037 0.2992 0.3357 0.0494  0.0047  -0.0004 1074 SER B C   
16472 O O   . SER B 1076 ? 0.3213 0.3242 0.3552 0.0496  0.0059  -0.0015 1074 SER B O   
16473 C CB  . SER B 1076 ? 0.3466 0.3356 0.3752 0.0574  0.0028  0.0011  1074 SER B CB  
16474 O OG  . SER B 1076 ? 0.3542 0.3378 0.3801 0.0627  0.0018  -0.0001 1074 SER B OG  
16475 N N   . SER B 1077 ? 0.2851 0.2789 0.3175 0.0453  0.0045  0.0014  1075 SER B N   
16476 C CA  . SER B 1077 ? 0.3263 0.3274 0.3614 0.0416  0.0057  0.0021  1075 SER B CA  
16477 C C   . SER B 1077 ? 0.2718 0.2734 0.3079 0.0387  0.0064  0.0000  1075 SER B C   
16478 O O   . SER B 1077 ? 0.2738 0.2817 0.3119 0.0365  0.0075  -0.0001 1075 SER B O   
16479 C CB  . SER B 1077 ? 0.3633 0.3634 0.3983 0.0387  0.0055  0.0048  1075 SER B CB  
16480 O OG  . SER B 1077 ? 0.4856 0.4774 0.5189 0.0369  0.0046  0.0052  1075 SER B OG  
16481 N N   . SER B 1078 ? 0.2288 0.2236 0.2633 0.0387  0.0056  -0.0016 1076 SER B N   
16482 C CA  . SER B 1078 ? 0.2326 0.2277 0.2679 0.0364  0.0060  -0.0036 1076 SER B CA  
16483 C C   . SER B 1078 ? 0.2381 0.2404 0.2745 0.0380  0.0071  -0.0052 1076 SER B C   
16484 O O   . SER B 1078 ? 0.2347 0.2389 0.2704 0.0419  0.0072  -0.0057 1076 SER B O   
16485 C CB  . SER B 1078 ? 0.2108 0.1974 0.2436 0.0370  0.0046  -0.0053 1076 SER B CB  
16486 O OG  . SER B 1078 ? 0.2235 0.2110 0.2570 0.0353  0.0048  -0.0075 1076 SER B OG  
16487 N N   . ALA B 1079 ? 0.1932 0.1994 0.2313 0.0350  0.0078  -0.0059 1077 ALA B N   
16488 C CA  . ALA B 1079 ? 0.2290 0.2412 0.2679 0.0359  0.0087  -0.0073 1077 ALA B CA  
16489 C C   . ALA B 1079 ? 0.2183 0.2273 0.2560 0.0357  0.0084  -0.0098 1077 ALA B C   
16490 O O   . ALA B 1079 ? 0.2064 0.2199 0.2447 0.0355  0.0091  -0.0109 1077 ALA B O   
16491 C CB  . ALA B 1079 ? 0.2541 0.2728 0.2952 0.0329  0.0096  -0.0063 1077 ALA B CB  
16492 N N   . LEU B 1080 ? 0.1976 0.1988 0.2336 0.0357  0.0072  -0.0105 1078 LEU B N   
16493 C CA  . LEU B 1080 ? 0.2082 0.2056 0.2425 0.0359  0.0065  -0.0129 1078 LEU B CA  
16494 C C   . LEU B 1080 ? 0.2020 0.2023 0.2347 0.0398  0.0072  -0.0145 1078 LEU B C   
16495 O O   . LEU B 1080 ? 0.2095 0.2097 0.2410 0.0436  0.0074  -0.0143 1078 LEU B O   
16496 C CB  . LEU B 1080 ? 0.2165 0.2044 0.2484 0.0360  0.0048  -0.0133 1078 LEU B CB  
16497 C CG  . LEU B 1080 ? 0.2049 0.1879 0.2342 0.0368  0.0038  -0.0160 1078 LEU B CG  
16498 C CD1 . LEU B 1080 ? 0.1999 0.1844 0.2309 0.0328  0.0036  -0.0167 1078 LEU B CD1 
16499 C CD2 . LEU B 1080 ? 0.2527 0.2257 0.2789 0.0377  0.0018  -0.0163 1078 LEU B CD2 
16500 N N   . GLY B 1081 ? 0.2321 0.2349 0.2647 0.0390  0.0076  -0.0162 1079 GLY B N   
16501 C CA  . GLY B 1081 ? 0.2317 0.2379 0.2628 0.0423  0.0085  -0.0176 1079 GLY B CA  
16502 C C   . GLY B 1081 ? 0.2685 0.2842 0.3020 0.0421  0.0101  -0.0165 1079 GLY B C   
16503 O O   . GLY B 1081 ? 0.2169 0.2368 0.2495 0.0445  0.0110  -0.0173 1079 GLY B O   
16504 N N   . LEU B 1082 ? 0.2009 0.2202 0.2371 0.0393  0.0103  -0.0145 1080 LEU B N   
16505 C CA  A LEU B 1082 ? 0.2267 0.2543 0.2649 0.0383  0.0114  -0.0134 1080 LEU B CA  
16506 C CA  B LEU B 1082 ? 0.2267 0.2544 0.2649 0.0383  0.0114  -0.0134 1080 LEU B CA  
16507 C C   . LEU B 1082 ? 0.2300 0.2600 0.2676 0.0371  0.0118  -0.0149 1080 LEU B C   
16508 O O   . LEU B 1082 ? 0.1974 0.2232 0.2343 0.0351  0.0111  -0.0161 1080 LEU B O   
16509 C CB  A LEU B 1082 ? 0.1965 0.2259 0.2369 0.0349  0.0113  -0.0116 1080 LEU B CB  
16510 C CB  B LEU B 1082 ? 0.1949 0.2242 0.2353 0.0349  0.0113  -0.0116 1080 LEU B CB  
16511 C CG  A LEU B 1082 ? 0.2095 0.2465 0.2517 0.0332  0.0121  -0.0105 1080 LEU B CG  
16512 C CG  B LEU B 1082 ? 0.2097 0.2466 0.2519 0.0330  0.0120  -0.0104 1080 LEU B CG  
16513 C CD1 A LEU B 1082 ? 0.1988 0.2415 0.2415 0.0361  0.0127  -0.0095 1080 LEU B CD1 
16514 C CD1 B LEU B 1082 ? 0.1936 0.2313 0.2371 0.0314  0.0119  -0.0084 1080 LEU B CD1 
16515 C CD2 A LEU B 1082 ? 0.1978 0.2352 0.2413 0.0302  0.0118  -0.0089 1080 LEU B CD2 
16516 C CD2 B LEU B 1082 ? 0.1836 0.2212 0.2259 0.0301  0.0120  -0.0113 1080 LEU B CD2 
16517 N N   . ASP B 1083 ? 0.1924 0.2291 0.2304 0.0383  0.0129  -0.0146 1081 ASP B N   
16518 C CA  . ASP B 1083 ? 0.2383 0.2772 0.2752 0.0375  0.0133  -0.0159 1081 ASP B CA  
16519 C C   . ASP B 1083 ? 0.2516 0.2992 0.2903 0.0366  0.0143  -0.0143 1081 ASP B C   
16520 O O   . ASP B 1083 ? 0.2785 0.3311 0.3173 0.0394  0.0152  -0.0139 1081 ASP B O   
16521 C CB  . ASP B 1083 ? 0.2744 0.3106 0.3083 0.0411  0.0135  -0.0179 1081 ASP B CB  
16522 C CG  . ASP B 1083 ? 0.3993 0.4374 0.4315 0.0404  0.0139  -0.0191 1081 ASP B CG  
16523 O OD1 . ASP B 1083 ? 0.3973 0.4366 0.4304 0.0369  0.0136  -0.0188 1081 ASP B OD1 
16524 O OD2 . ASP B 1083 ? 0.4115 0.4498 0.4413 0.0437  0.0145  -0.0205 1081 ASP B OD2 
16525 N N   . LEU B 1084 ? 0.2371 0.2865 0.2771 0.0328  0.0139  -0.0135 1082 LEU B N   
16526 C CA  . LEU B 1084 ? 0.2377 0.2943 0.2793 0.0312  0.0144  -0.0117 1082 LEU B CA  
16527 C C   . LEU B 1084 ? 0.2467 0.3052 0.2875 0.0286  0.0144  -0.0121 1082 LEU B C   
16528 O O   . LEU B 1084 ? 0.2213 0.2750 0.2610 0.0270  0.0137  -0.0133 1082 LEU B O   
16529 C CB  . LEU B 1084 ? 0.2317 0.2884 0.2751 0.0288  0.0138  -0.0102 1082 LEU B CB  
16530 C CG  . LEU B 1084 ? 0.2968 0.3525 0.3410 0.0308  0.0137  -0.0092 1082 LEU B CG  
16531 C CD1 . LEU B 1084 ? 0.2974 0.3532 0.3427 0.0281  0.0132  -0.0077 1082 LEU B CD1 
16532 C CD2 . LEU B 1084 ? 0.3307 0.3924 0.3756 0.0339  0.0145  -0.0083 1082 LEU B CD2 
16533 N N   . GLU B 1085 ? 0.2022 0.2676 0.2436 0.0280  0.0151  -0.0109 1083 GLU B N   
16534 C CA  . GLU B 1085 ? 0.2119 0.2790 0.2527 0.0248  0.0148  -0.0106 1083 GLU B CA  
16535 C C   . GLU B 1085 ? 0.2312 0.3002 0.2734 0.0215  0.0140  -0.0089 1083 GLU B C   
16536 O O   . GLU B 1085 ? 0.2730 0.3469 0.3169 0.0218  0.0143  -0.0073 1083 GLU B O   
16537 C CB  . GLU B 1085 ? 0.2164 0.2895 0.2564 0.0256  0.0159  -0.0102 1083 GLU B CB  
16538 C CG  . GLU B 1085 ? 0.2768 0.3512 0.3159 0.0218  0.0153  -0.0097 1083 GLU B CG  
16539 C CD  . GLU B 1085 ? 0.3421 0.4210 0.3797 0.0223  0.0163  -0.0096 1083 GLU B CD  
16540 O OE1 . GLU B 1085 ? 0.3308 0.4120 0.3679 0.0259  0.0176  -0.0102 1083 GLU B OE1 
16541 O OE2 . GLU B 1085 ? 0.3331 0.4131 0.3697 0.0192  0.0158  -0.0088 1083 GLU B OE2 
16542 N N   . LEU B 1086 ? 0.2085 0.2739 0.2501 0.0188  0.0131  -0.0093 1084 LEU B N   
16543 C CA  . LEU B 1086 ? 0.2076 0.2739 0.2499 0.0158  0.0123  -0.0080 1084 LEU B CA  
16544 C C   . LEU B 1086 ? 0.2678 0.3381 0.3093 0.0132  0.0119  -0.0069 1084 LEU B C   
16545 O O   . LEU B 1086 ? 0.2513 0.3214 0.2913 0.0128  0.0121  -0.0075 1084 LEU B O   
16546 C CB  . LEU B 1086 ? 0.1983 0.2583 0.2401 0.0144  0.0114  -0.0090 1084 LEU B CB  
16547 C CG  . LEU B 1086 ? 0.2271 0.2829 0.2696 0.0163  0.0116  -0.0099 1084 LEU B CG  
16548 C CD1 . LEU B 1086 ? 0.1784 0.2293 0.2208 0.0147  0.0109  -0.0106 1084 LEU B CD1 
16549 C CD2 . LEU B 1086 ? 0.2198 0.2781 0.2637 0.0174  0.0119  -0.0085 1084 LEU B CD2 
16550 N N   . PRO B 1087 ? 0.2927 0.3666 0.3350 0.0111  0.0114  -0.0053 1085 PRO B N   
16551 C CA  . PRO B 1087 ? 0.2606 0.3379 0.3021 0.0081  0.0108  -0.0040 1085 PRO B CA  
16552 C C   . PRO B 1087 ? 0.2752 0.3470 0.3145 0.0057  0.0096  -0.0048 1085 PRO B C   
16553 O O   . PRO B 1087 ? 0.3144 0.3810 0.3534 0.0054  0.0090  -0.0058 1085 PRO B O   
16554 C CB  . PRO B 1087 ? 0.2966 0.3776 0.3393 0.0064  0.0101  -0.0022 1085 PRO B CB  
16555 C CG  . PRO B 1087 ? 0.3085 0.3905 0.3530 0.0095  0.0109  -0.0022 1085 PRO B CG  
16556 C CD  . PRO B 1087 ? 0.3365 0.4121 0.3804 0.0117  0.0113  -0.0042 1085 PRO B CD  
16557 N N   . GLY B 1088 ? 0.2521 0.3254 0.2899 0.0040  0.0094  -0.0044 1086 GLY B N   
16558 C CA  . GLY B 1088 ? 0.2536 0.3218 0.2892 0.0019  0.0082  -0.0050 1086 GLY B CA  
16559 C C   . GLY B 1088 ? 0.2191 0.2903 0.2530 -0.0006 0.0078  -0.0036 1086 GLY B C   
16560 O O   . GLY B 1088 ? 0.2345 0.3122 0.2694 -0.0015 0.0083  -0.0018 1086 GLY B O   
16561 N N   . PRO B 1089 ? 0.2410 0.3078 0.2725 -0.0018 0.0069  -0.0043 1087 PRO B N   
16562 C CA  . PRO B 1089 ? 0.2304 0.2995 0.2600 -0.0045 0.0064  -0.0028 1087 PRO B CA  
16563 C C   . PRO B 1089 ? 0.2254 0.2996 0.2550 -0.0028 0.0081  -0.0025 1087 PRO B C   
16564 O O   . PRO B 1089 ? 0.2073 0.2813 0.2377 0.0006  0.0094  -0.0041 1087 PRO B O   
16565 C CB  . PRO B 1089 ? 0.2554 0.3173 0.2823 -0.0056 0.0048  -0.0038 1087 PRO B CB  
16566 C CG  . PRO B 1089 ? 0.2996 0.3575 0.3275 -0.0024 0.0053  -0.0062 1087 PRO B CG  
16567 C CD  . PRO B 1089 ? 0.2521 0.3121 0.2828 -0.0007 0.0063  -0.0063 1087 PRO B CD  
16568 N N   . VAL B 1090 ? 0.2240 0.3030 0.2525 -0.0053 0.0082  -0.0005 1088 VAL B N   
16569 C CA  . VAL B 1090 ? 0.1951 0.2785 0.2228 -0.0039 0.0098  -0.0003 1088 VAL B CA  
16570 C C   . VAL B 1090 ? 0.2470 0.3240 0.2720 -0.0027 0.0094  -0.0023 1088 VAL B C   
16571 O O   . VAL B 1090 ? 0.1965 0.2667 0.2202 -0.0038 0.0077  -0.0032 1088 VAL B O   
16572 C CB  . VAL B 1090 ? 0.2462 0.3356 0.2730 -0.0074 0.0098  0.0025  1088 VAL B CB  
16573 C CG1 . VAL B 1090 ? 0.2683 0.3643 0.2980 -0.0090 0.0098  0.0046  1088 VAL B CG1 
16574 C CG2 . VAL B 1090 ? 0.2051 0.2889 0.2286 -0.0112 0.0076  0.0032  1088 VAL B CG2 
16575 N N   . GLY B 1091 ? 0.2171 0.2967 0.2412 -0.0002 0.0110  -0.0030 1089 GLY B N   
16576 C CA  . GLY B 1091 ? 0.2206 0.2949 0.2417 0.0007  0.0105  -0.0047 1089 GLY B CA  
16577 C C   . GLY B 1091 ? 0.2259 0.2937 0.2477 0.0032  0.0099  -0.0073 1089 GLY B C   
16578 O O   . GLY B 1091 ? 0.2255 0.2880 0.2453 0.0034  0.0089  -0.0087 1089 GLY B O   
16579 N N   . GLU B 1092 ? 0.1854 0.2537 0.2102 0.0050  0.0105  -0.0078 1090 GLU B N   
16580 C CA  . GLU B 1092 ? 0.2112 0.2739 0.2370 0.0070  0.0100  -0.0099 1090 GLU B CA  
16581 C C   . GLU B 1092 ? 0.2177 0.2834 0.2460 0.0099  0.0115  -0.0102 1090 GLU B C   
16582 O O   . GLU B 1092 ? 0.2282 0.2994 0.2583 0.0095  0.0122  -0.0086 1090 GLU B O   
16583 C CB  . GLU B 1092 ? 0.2620 0.3203 0.2888 0.0049  0.0083  -0.0098 1090 GLU B CB  
16584 C CG  . GLU B 1092 ? 0.2895 0.3417 0.3166 0.0061  0.0074  -0.0118 1090 GLU B CG  
16585 C CD  . GLU B 1092 ? 0.2820 0.3305 0.3097 0.0042  0.0059  -0.0117 1090 GLU B CD  
16586 O OE1 . GLU B 1092 ? 0.2431 0.2926 0.2727 0.0039  0.0061  -0.0111 1090 GLU B OE1 
16587 O OE2 . GLU B 1092 ? 0.3148 0.3593 0.3409 0.0032  0.0045  -0.0121 1090 GLU B OE2 
16588 N N   . ARG B 1093 ? 0.2024 0.2643 0.2306 0.0127  0.0117  -0.0122 1091 ARG B N   
16589 C CA  . ARG B 1093 ? 0.1918 0.2549 0.2220 0.0156  0.0127  -0.0126 1091 ARG B CA  
16590 C C   . ARG B 1093 ? 0.2014 0.2586 0.2330 0.0158  0.0117  -0.0138 1091 ARG B C   
16591 O O   . ARG B 1093 ? 0.2198 0.2717 0.2502 0.0160  0.0108  -0.0153 1091 ARG B O   
16592 C CB  . ARG B 1093 ? 0.2200 0.2843 0.2486 0.0191  0.0141  -0.0139 1091 ARG B CB  
16593 N N   . ASN B 1094 ? 0.1854 0.2435 0.2193 0.0156  0.0118  -0.0129 1092 ASN B N   
16594 C CA  . ASN B 1094 ? 0.1908 0.2440 0.2261 0.0153  0.0109  -0.0136 1092 ASN B CA  
16595 C C   . ASN B 1094 ? 0.2069 0.2600 0.2437 0.0179  0.0117  -0.0138 1092 ASN B C   
16596 O O   . ASN B 1094 ? 0.1985 0.2559 0.2366 0.0185  0.0124  -0.0125 1092 ASN B O   
16597 C CB  . ASN B 1094 ? 0.1878 0.2415 0.2241 0.0124  0.0101  -0.0123 1092 ASN B CB  
16598 C CG  . ASN B 1094 ? 0.1941 0.2459 0.2286 0.0101  0.0090  -0.0124 1092 ASN B CG  
16599 O OD1 . ASN B 1094 ? 0.1972 0.2445 0.2312 0.0100  0.0082  -0.0137 1092 ASN B OD1 
16600 N ND2 . ASN B 1094 ? 0.2200 0.2753 0.2536 0.0081  0.0089  -0.0110 1092 ASN B ND2 
16601 N N   . LEU B 1095 ? 0.1897 0.2378 0.2260 0.0195  0.0114  -0.0154 1093 LEU B N   
16602 C CA  . LEU B 1095 ? 0.1924 0.2392 0.2292 0.0223  0.0119  -0.0158 1093 LEU B CA  
16603 C C   . LEU B 1095 ? 0.1882 0.2306 0.2265 0.0216  0.0112  -0.0158 1093 LEU B C   
16604 O O   . LEU B 1095 ? 0.1933 0.2326 0.2319 0.0197  0.0103  -0.0164 1093 LEU B O   
16605 C CB  . LEU B 1095 ? 0.2056 0.2496 0.2399 0.0247  0.0120  -0.0176 1093 LEU B CB  
16606 C CG  . LEU B 1095 ? 0.2609 0.3093 0.2932 0.0255  0.0129  -0.0176 1093 LEU B CG  
16607 C CD1 . LEU B 1095 ? 0.3208 0.3658 0.3500 0.0281  0.0129  -0.0197 1093 LEU B CD1 
16608 C CD2 . LEU B 1095 ? 0.2587 0.3141 0.2925 0.0266  0.0142  -0.0160 1093 LEU B CD2 
16609 N N   . TYR B 1096 ? 0.2009 0.2434 0.2402 0.0232  0.0116  -0.0152 1094 TYR B N   
16610 C CA  . TYR B 1096 ? 0.1779 0.2169 0.2187 0.0224  0.0112  -0.0149 1094 TYR B CA  
16611 C C   . TYR B 1096 ? 0.1724 0.2084 0.2126 0.0252  0.0113  -0.0152 1094 TYR B C   
16612 O O   . TYR B 1096 ? 0.1766 0.2155 0.2167 0.0276  0.0120  -0.0146 1094 TYR B O   
16613 C CB  . TYR B 1096 ? 0.1965 0.2388 0.2389 0.0209  0.0114  -0.0131 1094 TYR B CB  
16614 C CG  . TYR B 1096 ? 0.1732 0.2127 0.2167 0.0204  0.0112  -0.0125 1094 TYR B CG  
16615 C CD1 . TYR B 1096 ? 0.1809 0.2177 0.2252 0.0183  0.0107  -0.0128 1094 TYR B CD1 
16616 C CD2 . TYR B 1096 ? 0.2042 0.2442 0.2482 0.0220  0.0116  -0.0114 1094 TYR B CD2 
16617 C CE1 . TYR B 1096 ? 0.2185 0.2535 0.2639 0.0177  0.0108  -0.0120 1094 TYR B CE1 
16618 C CE2 . TYR B 1096 ? 0.2226 0.2602 0.2674 0.0214  0.0114  -0.0105 1094 TYR B CE2 
16619 C CZ  . TYR B 1096 ? 0.1927 0.2279 0.2382 0.0192  0.0111  -0.0108 1094 TYR B CZ  
16620 O OH  . TYR B 1096 ? 0.1964 0.2297 0.2425 0.0185  0.0112  -0.0098 1094 TYR B OH  
16621 N N   . THR B 1097 ? 0.1813 0.2115 0.2212 0.0251  0.0104  -0.0162 1095 THR B N   
16622 C CA  . THR B 1097 ? 0.1916 0.2175 0.2303 0.0276  0.0102  -0.0168 1095 THR B CA  
16623 C C   . THR B 1097 ? 0.1584 0.1797 0.1982 0.0262  0.0094  -0.0163 1095 THR B C   
16624 O O   . THR B 1097 ? 0.1851 0.2055 0.2262 0.0235  0.0089  -0.0162 1095 THR B O   
16625 C CB  . THR B 1097 ? 0.2198 0.2422 0.2557 0.0291  0.0096  -0.0189 1095 THR B CB  
16626 O OG1 . THR B 1097 ? 0.2694 0.2893 0.3055 0.0265  0.0086  -0.0198 1095 THR B OG1 
16627 C CG2 . THR B 1097 ? 0.2537 0.2810 0.2882 0.0309  0.0106  -0.0194 1095 THR B CG2 
16628 N N   . LEU B 1098 ? 0.1598 0.1781 0.1990 0.0282  0.0092  -0.0158 1096 LEU B N   
16629 C CA  . LEU B 1098 ? 0.1944 0.2080 0.2343 0.0268  0.0085  -0.0150 1096 LEU B CA  
16630 C C   . LEU B 1098 ? 0.2025 0.2090 0.2401 0.0281  0.0072  -0.0165 1096 LEU B C   
16631 O O   . LEU B 1098 ? 0.1895 0.1941 0.2249 0.0314  0.0072  -0.0170 1096 LEU B O   
16632 C CB  . LEU B 1098 ? 0.1862 0.2012 0.2269 0.0276  0.0090  -0.0130 1096 LEU B CB  
16633 C CG  . LEU B 1098 ? 0.1741 0.1952 0.2167 0.0259  0.0099  -0.0116 1096 LEU B CG  
16634 C CD1 . LEU B 1098 ? 0.1792 0.2011 0.2221 0.0268  0.0102  -0.0096 1096 LEU B CD1 
16635 C CD2 . LEU B 1098 ? 0.1723 0.1935 0.2164 0.0225  0.0098  -0.0116 1096 LEU B CD2 
16636 N N   . HIS B 1099 ? 0.2001 0.2026 0.2381 0.0256  0.0061  -0.0170 1097 HIS B N   
16637 C CA  . HIS B 1099 ? 0.2226 0.2179 0.2584 0.0260  0.0045  -0.0183 1097 HIS B CA  
16638 C C   . HIS B 1099 ? 0.1839 0.1748 0.2209 0.0239  0.0036  -0.0169 1097 HIS B C   
16639 O O   . HIS B 1099 ? 0.1989 0.1927 0.2383 0.0220  0.0043  -0.0150 1097 HIS B O   
16640 C CB  . HIS B 1099 ? 0.2421 0.2366 0.2775 0.0245  0.0036  -0.0201 1097 HIS B CB  
16641 C CG  . HIS B 1099 ? 0.2679 0.2668 0.3021 0.0260  0.0045  -0.0213 1097 HIS B CG  
16642 N ND1 . HIS B 1099 ? 0.2808 0.2771 0.3116 0.0283  0.0040  -0.0234 1097 HIS B ND1 
16643 C CD2 . HIS B 1099 ? 0.2611 0.2666 0.2968 0.0255  0.0058  -0.0206 1097 HIS B CD2 
16644 C CE1 . HIS B 1099 ? 0.3219 0.3236 0.3523 0.0290  0.0051  -0.0237 1097 HIS B CE1 
16645 N NE2 . HIS B 1099 ? 0.2647 0.2718 0.2982 0.0272  0.0061  -0.0221 1097 HIS B NE2 
16646 N N   . ALA B 1100 ? 0.2304 0.2141 0.2651 0.0240  0.0019  -0.0179 1098 ALA B N   
16647 C CA  . ALA B 1100 ? 0.2398 0.2191 0.2756 0.0213  0.0007  -0.0165 1098 ALA B CA  
16648 C C   . ALA B 1100 ? 0.2807 0.2631 0.3199 0.0173  0.0006  -0.0161 1098 ALA B C   
16649 O O   . ALA B 1100 ? 0.2429 0.2276 0.2825 0.0169  0.0005  -0.0176 1098 ALA B O   
16650 C CB  . ALA B 1100 ? 0.2761 0.2462 0.3084 0.0219  -0.0015 -0.0178 1098 ALA B CB  
16651 N N   . ARG B 1101 ? 0.2460 0.2287 0.2877 0.0146  0.0007  -0.0140 1099 ARG B N   
16652 C CA  . ARG B 1101 ? 0.2728 0.2590 0.3181 0.0112  0.0008  -0.0135 1099 ARG B CA  
16653 C C   . ARG B 1101 ? 0.2709 0.2523 0.3160 0.0090  -0.0014 -0.0145 1099 ARG B C   
16654 O O   . ARG B 1101 ? 0.2852 0.2695 0.3325 0.0072  -0.0018 -0.0152 1099 ARG B O   
16655 C CB  . ARG B 1101 ? 0.2791 0.2681 0.3270 0.0091  0.0019  -0.0109 1099 ARG B CB  
16656 C CG  . ARG B 1101 ? 0.3498 0.3459 0.3993 0.0097  0.0040  -0.0104 1099 ARG B CG  
16657 C CD  . ARG B 1101 ? 0.3114 0.3099 0.3629 0.0078  0.0051  -0.0079 1099 ARG B CD  
16658 N NE  . ARG B 1101 ? 0.3735 0.3766 0.4283 0.0054  0.0058  -0.0077 1099 ARG B NE  
16659 C CZ  . ARG B 1101 ? 0.4323 0.4410 0.4882 0.0058  0.0072  -0.0078 1099 ARG B CZ  
16660 N NH1 . ARG B 1101 ? 0.3804 0.3911 0.4346 0.0080  0.0081  -0.0080 1099 ARG B NH1 
16661 N NH2 . ARG B 1101 ? 0.3797 0.3923 0.4386 0.0039  0.0078  -0.0075 1099 ARG B NH2 
16662 N N   . GLY B 1102 ? 0.2253 0.1994 0.2680 0.0090  -0.0031 -0.0144 1100 GLY B N   
16663 C CA  . GLY B 1102 ? 0.2485 0.2176 0.2911 0.0063  -0.0055 -0.0150 1100 GLY B CA  
16664 C C   . GLY B 1102 ? 0.2942 0.2574 0.3362 0.0044  -0.0067 -0.0131 1100 GLY B C   
16665 O O   . GLY B 1102 ? 0.2687 0.2271 0.3075 0.0067  -0.0069 -0.0128 1100 GLY B O   
16666 N N   . ARG B 1103 ? 0.2801 0.2437 0.3253 0.0002  -0.0077 -0.0117 1101 ARG B N   
16667 C CA  . ARG B 1103 ? 0.2972 0.2553 0.3419 -0.0023 -0.0089 -0.0095 1101 ARG B CA  
16668 C C   . ARG B 1103 ? 0.2441 0.2083 0.2926 -0.0042 -0.0068 -0.0064 1101 ARG B C   
16669 O O   . ARG B 1103 ? 0.2475 0.2189 0.3002 -0.0062 -0.0056 -0.0058 1101 ARG B O   
16670 C CB  . ARG B 1103 ? 0.2988 0.2525 0.3441 -0.0061 -0.0118 -0.0097 1101 ARG B CB  
16671 C CG  . ARG B 1103 ? 0.3108 0.2569 0.3546 -0.0087 -0.0136 -0.0075 1101 ARG B CG  
16672 C CD  . ARG B 1103 ? 0.3521 0.2926 0.3956 -0.0124 -0.0170 -0.0080 1101 ARG B CD  
16673 N NE  . ARG B 1103 ? 0.4052 0.3397 0.4442 -0.0098 -0.0190 -0.0115 1101 ARG B NE  
16674 C CZ  . ARG B 1103 ? 0.4667 0.3908 0.4999 -0.0080 -0.0211 -0.0128 1101 ARG B CZ  
16675 N NH1 . ARG B 1103 ? 0.3829 0.3008 0.4138 -0.0083 -0.0217 -0.0109 1101 ARG B NH1 
16676 N NH2 . ARG B 1103 ? 0.4448 0.3644 0.4738 -0.0056 -0.0227 -0.0161 1101 ARG B NH2 
16677 N N   . ILE B 1104 ? 0.2258 0.1872 0.2724 -0.0033 -0.0062 -0.0046 1102 ILE B N   
16678 C CA  . ILE B 1104 ? 0.2299 0.1966 0.2791 -0.0048 -0.0041 -0.0017 1102 ILE B CA  
16679 C C   . ILE B 1104 ? 0.2394 0.2029 0.2898 -0.0092 -0.0053 0.0010  1102 ILE B C   
16680 O O   . ILE B 1104 ? 0.2422 0.1970 0.2893 -0.0096 -0.0075 0.0014  1102 ILE B O   
16681 C CB  . ILE B 1104 ? 0.2327 0.1992 0.2793 -0.0013 -0.0027 -0.0010 1102 ILE B CB  
16682 C CG1 . ILE B 1104 ? 0.2070 0.1764 0.2524 0.0029  -0.0018 -0.0037 1102 ILE B CG1 
16683 C CG2 . ILE B 1104 ? 0.2236 0.1961 0.2726 -0.0028 -0.0005 0.0018  1102 ILE B CG2 
16684 C CD1 . ILE B 1104 ? 0.2111 0.1891 0.2599 0.0024  -0.0001 -0.0045 1102 ILE B CD1 
16685 N N   . LEU B 1105 ? 0.2114 0.1818 0.2663 -0.0124 -0.0040 0.0029  1103 LEU B N   
16686 C CA  . LEU B 1105 ? 0.2017 0.1705 0.2581 -0.0168 -0.0046 0.0060  1103 LEU B CA  
16687 C C   . LEU B 1105 ? 0.2045 0.1715 0.2586 -0.0161 -0.0035 0.0086  1103 LEU B C   
16688 O O   . LEU B 1105 ? 0.2139 0.1868 0.2687 -0.0144 -0.0010 0.0092  1103 LEU B O   
16689 C CB  . LEU B 1105 ? 0.2050 0.1832 0.2672 -0.0200 -0.0031 0.0072  1103 LEU B CB  
16690 C CG  . LEU B 1105 ? 0.2560 0.2352 0.3207 -0.0248 -0.0031 0.0108  1103 LEU B CG  
16691 C CD1 . LEU B 1105 ? 0.2230 0.1945 0.2869 -0.0282 -0.0065 0.0113  1103 LEU B CD1 
16692 C CD2 . LEU B 1105 ? 0.2370 0.2270 0.3075 -0.0267 -0.0008 0.0117  1103 LEU B CD2 
16693 N N   . LEU B 1106 ? 0.2213 0.1797 0.2725 -0.0176 -0.0056 0.0102  1104 LEU B N   
16694 C CA  . LEU B 1106 ? 0.2159 0.1715 0.2646 -0.0173 -0.0050 0.0130  1104 LEU B CA  
16695 C C   . LEU B 1106 ? 0.2135 0.1701 0.2645 -0.0226 -0.0050 0.0167  1104 LEU B C   
16696 O O   . LEU B 1106 ? 0.2560 0.2080 0.3074 -0.0263 -0.0074 0.0172  1104 LEU B O   
16697 C CB  . LEU B 1106 ? 0.2130 0.1575 0.2560 -0.0147 -0.0074 0.0123  1104 LEU B CB  
16698 C CG  . LEU B 1106 ? 0.2492 0.1923 0.2895 -0.0091 -0.0074 0.0088  1104 LEU B CG  
16699 C CD1 . LEU B 1106 ? 0.2260 0.1593 0.2609 -0.0061 -0.0092 0.0089  1104 LEU B CD1 
16700 C CD2 . LEU B 1106 ? 0.2638 0.2166 0.3063 -0.0065 -0.0044 0.0081  1104 LEU B CD2 
16701 N N   . VAL B 1107 ? 0.2166 0.1792 0.2689 -0.0233 -0.0024 0.0192  1105 VAL B N   
16702 C CA  . VAL B 1107 ? 0.2036 0.1680 0.2580 -0.0283 -0.0020 0.0231  1105 VAL B CA  
16703 C C   . VAL B 1107 ? 0.2087 0.1690 0.2591 -0.0276 -0.0017 0.0260  1105 VAL B C   
16704 O O   . VAL B 1107 ? 0.2520 0.2187 0.3031 -0.0271 0.0011  0.0275  1105 VAL B O   
16705 C CB  . VAL B 1107 ? 0.2270 0.2034 0.2867 -0.0300 0.0010  0.0238  1105 VAL B CB  
16706 C CG1 . VAL B 1107 ? 0.2264 0.2051 0.2889 -0.0356 0.0012  0.0277  1105 VAL B CG1 
16707 C CG2 . VAL B 1107 ? 0.2125 0.1930 0.2755 -0.0292 0.0007  0.0204  1105 VAL B CG2 
16708 N N   . PRO B 1108 ? 0.2299 0.1793 0.2759 -0.0273 -0.0044 0.0265  1106 PRO B N   
16709 C CA  . PRO B 1108 ? 0.2740 0.2188 0.3160 -0.0264 -0.0044 0.0293  1106 PRO B CA  
16710 C C   . PRO B 1108 ? 0.3021 0.2470 0.3449 -0.0319 -0.0043 0.0339  1106 PRO B C   
16711 O O   . PRO B 1108 ? 0.3101 0.2563 0.3560 -0.0367 -0.0050 0.0350  1106 PRO B O   
16712 C CB  . PRO B 1108 ? 0.2448 0.1773 0.2817 -0.0238 -0.0078 0.0277  1106 PRO B CB  
16713 C CG  . PRO B 1108 ? 0.2965 0.2256 0.3350 -0.0269 -0.0101 0.0263  1106 PRO B CG  
16714 C CD  . PRO B 1108 ? 0.2395 0.1797 0.2835 -0.0274 -0.0079 0.0244  1106 PRO B CD  
16715 N N   . ALA B 1109 ? 0.3010 0.2448 0.3409 -0.0312 -0.0034 0.0367  1107 ALA B N   
16716 C CA  . ALA B 1109 ? 0.3250 0.2669 0.3642 -0.0360 -0.0035 0.0414  1107 ALA B CA  
16717 C C   . ALA B 1109 ? 0.3494 0.2785 0.3827 -0.0355 -0.0066 0.0433  1107 ALA B C   
16718 O O   . ALA B 1109 ? 0.3726 0.2963 0.4049 -0.0403 -0.0083 0.0466  1107 ALA B O   
16719 C CB  . ALA B 1109 ? 0.3222 0.2735 0.3624 -0.0362 0.0001  0.0439  1107 ALA B CB  
16720 N N   . THR B 1110 ? 0.3221 0.2463 0.3516 -0.0299 -0.0074 0.0412  1108 THR B N   
16721 C CA  . THR B 1110 ? 0.3159 0.2283 0.3396 -0.0284 -0.0102 0.0428  1108 THR B CA  
16722 C C   . THR B 1110 ? 0.3432 0.2477 0.3640 -0.0235 -0.0126 0.0387  1108 THR B C   
16723 O O   . THR B 1110 ? 0.3233 0.2328 0.3463 -0.0203 -0.0116 0.0348  1108 THR B O   
16724 C CB  . THR B 1110 ? 0.3584 0.2730 0.3795 -0.0258 -0.0086 0.0451  1108 THR B CB  
16725 O OG1 . THR B 1110 ? 0.3596 0.2805 0.3815 -0.0203 -0.0067 0.0418  1108 THR B OG1 
16726 C CG2 . THR B 1110 ? 0.3516 0.2742 0.3750 -0.0305 -0.0059 0.0490  1108 THR B CG2 
16727 N N   . GLU B 1111 ? 0.3613 0.2531 0.3768 -0.0227 -0.0158 0.0397  1109 GLU B N   
16728 C CA  . GLU B 1111 ? 0.3952 0.2788 0.4074 -0.0177 -0.0182 0.0359  1109 GLU B CA  
16729 C C   . GLU B 1111 ? 0.3549 0.2443 0.3671 -0.0110 -0.0162 0.0333  1109 GLU B C   
16730 O O   . GLU B 1111 ? 0.3392 0.2303 0.3523 -0.0076 -0.0161 0.0292  1109 GLU B O   
16731 C CB  . GLU B 1111 ? 0.4103 0.2792 0.4163 -0.0174 -0.0219 0.0377  1109 GLU B CB  
16732 C CG  . GLU B 1111 ? 0.4114 0.2715 0.4133 -0.0114 -0.0242 0.0338  1109 GLU B CG  
16733 C CD  . GLU B 1111 ? 0.4451 0.2896 0.4404 -0.0111 -0.0281 0.0355  1109 GLU B CD  
16734 O OE1 . GLU B 1111 ? 0.4790 0.3150 0.4728 -0.0151 -0.0310 0.0356  1109 GLU B OE1 
16735 O OE2 . GLU B 1111 ? 0.4746 0.3154 0.4664 -0.0070 -0.0285 0.0367  1109 GLU B OE2 
16736 N N   . SER B 1112 ? 0.3376 0.2304 0.3489 -0.0094 -0.0147 0.0357  1110 SER B N   
16737 C CA  . SER B 1112 ? 0.3590 0.2578 0.3706 -0.0035 -0.0130 0.0336  1110 SER B CA  
16738 C C   . SER B 1112 ? 0.3631 0.2741 0.3798 -0.0036 -0.0100 0.0311  1110 SER B C   
16739 O O   . SER B 1112 ? 0.3378 0.2521 0.3552 0.0009  -0.0094 0.0277  1110 SER B O   
16740 C CB  . SER B 1112 ? 0.4145 0.3147 0.4241 -0.0024 -0.0122 0.0370  1110 SER B CB  
16741 O OG  . SER B 1112 ? 0.4104 0.3153 0.4199 0.0035  -0.0111 0.0350  1110 SER B OG  
16742 N N   . GLY B 1113 ? 0.2968 0.2148 0.3172 -0.0086 -0.0082 0.0328  1111 GLY B N   
16743 C CA  . GLY B 1113 ? 0.3056 0.2343 0.3307 -0.0088 -0.0056 0.0304  1111 GLY B CA  
16744 C C   . GLY B 1113 ? 0.2953 0.2219 0.3214 -0.0076 -0.0069 0.0264  1111 GLY B C   
16745 O O   . GLY B 1113 ? 0.2891 0.2216 0.3170 -0.0045 -0.0055 0.0233  1111 GLY B O   
16746 N N   . LEU B 1114 ? 0.2731 0.1908 0.2977 -0.0101 -0.0096 0.0265  1112 LEU B N   
16747 C CA  . LEU B 1114 ? 0.2811 0.1958 0.3059 -0.0091 -0.0112 0.0228  1112 LEU B CA  
16748 C C   . LEU B 1114 ? 0.2836 0.1949 0.3053 -0.0026 -0.0118 0.0196  1112 LEU B C   
16749 O O   . LEU B 1114 ? 0.2520 0.1672 0.2751 -0.0002 -0.0111 0.0161  1112 LEU B O   
16750 C CB  . LEU B 1114 ? 0.3001 0.2045 0.3230 -0.0131 -0.0144 0.0238  1112 LEU B CB  
16751 C CG  . LEU B 1114 ? 0.3347 0.2334 0.3563 -0.0121 -0.0167 0.0199  1112 LEU B CG  
16752 C CD1 . LEU B 1114 ? 0.2702 0.1788 0.2967 -0.0126 -0.0149 0.0173  1112 LEU B CD1 
16753 C CD2 . LEU B 1114 ? 0.3448 0.2331 0.3642 -0.0167 -0.0202 0.0214  1112 LEU B CD2 
16754 N N   . TYR B 1115 ? 0.3158 0.2199 0.3330 0.0004  -0.0131 0.0209  1113 TYR B N   
16755 C CA  . TYR B 1115 ? 0.2989 0.2008 0.3135 0.0070  -0.0135 0.0181  1113 TYR B CA  
16756 C C   . TYR B 1115 ? 0.2411 0.1547 0.2588 0.0099  -0.0104 0.0167  1113 TYR B C   
16757 O O   . TYR B 1115 ? 0.2897 0.2055 0.3076 0.0136  -0.0101 0.0133  1113 TYR B O   
16758 C CB  . TYR B 1115 ? 0.3491 0.2423 0.3588 0.0099  -0.0153 0.0200  1113 TYR B CB  
16759 C CG  . TYR B 1115 ? 0.3259 0.2055 0.3313 0.0079  -0.0188 0.0209  1113 TYR B CG  
16760 C CD1 . TYR B 1115 ? 0.3399 0.2150 0.3454 0.0049  -0.0205 0.0191  1113 TYR B CD1 
16761 C CD2 . TYR B 1115 ? 0.4296 0.3005 0.4307 0.0090  -0.0207 0.0237  1113 TYR B CD2 
16762 C CE1 . TYR B 1115 ? 0.4128 0.2750 0.4141 0.0027  -0.0240 0.0200  1113 TYR B CE1 
16763 C CE2 . TYR B 1115 ? 0.4299 0.2876 0.4266 0.0071  -0.0241 0.0246  1113 TYR B CE2 
16764 C CZ  . TYR B 1115 ? 0.4592 0.3124 0.4559 0.0039  -0.0258 0.0227  1113 TYR B CZ  
16765 O OH  . TYR B 1115 ? 0.4863 0.3258 0.4784 0.0017  -0.0296 0.0237  1113 TYR B OH  
16766 N N   . HIS B 1116 ? 0.2331 0.1543 0.2531 0.0081  -0.0083 0.0193  1114 HIS B N   
16767 C CA  . HIS B 1116 ? 0.2654 0.1973 0.2881 0.0105  -0.0056 0.0181  1114 HIS B CA  
16768 C C   . HIS B 1116 ? 0.3001 0.2385 0.3266 0.0090  -0.0044 0.0153  1114 HIS B C   
16769 O O   . HIS B 1116 ? 0.2592 0.2024 0.2866 0.0124  -0.0034 0.0127  1114 HIS B O   
16770 C CB  . HIS B 1116 ? 0.2872 0.2251 0.3110 0.0086  -0.0038 0.0213  1114 HIS B CB  
16771 C CG  . HIS B 1116 ? 0.3352 0.2695 0.3556 0.0116  -0.0047 0.0235  1114 HIS B CG  
16772 N ND1 . HIS B 1116 ? 0.3772 0.3023 0.3942 0.0104  -0.0067 0.0263  1114 HIS B ND1 
16773 C CD2 . HIS B 1116 ? 0.3548 0.2934 0.3747 0.0156  -0.0039 0.0235  1114 HIS B CD2 
16774 C CE1 . HIS B 1116 ? 0.4023 0.3261 0.4168 0.0138  -0.0072 0.0278  1114 HIS B CE1 
16775 N NE2 . HIS B 1116 ? 0.4281 0.3603 0.4444 0.0171  -0.0055 0.0261  1114 HIS B NE2 
16776 N N   . GLN B 1117 ? 0.2340 0.1729 0.2628 0.0041  -0.0044 0.0160  1115 GLN B N   
16777 C CA  . GLN B 1117 ? 0.2345 0.1792 0.2668 0.0028  -0.0035 0.0135  1115 GLN B CA  
16778 C C   . GLN B 1117 ? 0.2400 0.1798 0.2705 0.0056  -0.0051 0.0100  1115 GLN B C   
16779 O O   . GLN B 1117 ? 0.2620 0.2071 0.2942 0.0074  -0.0041 0.0073  1115 GLN B O   
16780 C CB  . GLN B 1117 ? 0.2242 0.1699 0.2594 -0.0030 -0.0035 0.0151  1115 GLN B CB  
16781 C CG  . GLN B 1117 ? 0.2491 0.2014 0.2865 -0.0058 -0.0014 0.0182  1115 GLN B CG  
16782 C CD  . GLN B 1117 ? 0.2714 0.2247 0.3117 -0.0115 -0.0015 0.0201  1115 GLN B CD  
16783 O OE1 . GLN B 1117 ? 0.2530 0.2006 0.2932 -0.0136 -0.0038 0.0195  1115 GLN B OE1 
16784 N NE2 . GLN B 1117 ? 0.2129 0.1738 0.2558 -0.0140 0.0008  0.0223  1115 GLN B NE2 
16785 N N   . LEU B 1118 ? 0.2470 0.1763 0.2739 0.0058  -0.0078 0.0099  1116 LEU B N   
16786 C CA  . LEU B 1118 ? 0.2507 0.1747 0.2753 0.0086  -0.0095 0.0064  1116 LEU B CA  
16787 C C   . LEU B 1118 ? 0.2641 0.1910 0.2873 0.0146  -0.0084 0.0044  1116 LEU B C   
16788 O O   . LEU B 1118 ? 0.2646 0.1944 0.2883 0.0167  -0.0079 0.0013  1116 LEU B O   
16789 C CB  . LEU B 1118 ? 0.2924 0.2037 0.3126 0.0080  -0.0127 0.0068  1116 LEU B CB  
16790 C CG  . LEU B 1118 ? 0.3671 0.2711 0.3842 0.0099  -0.0150 0.0033  1116 LEU B CG  
16791 C CD1 . LEU B 1118 ? 0.3810 0.2903 0.4015 0.0070  -0.0146 0.0013  1116 LEU B CD1 
16792 C CD2 . LEU B 1118 ? 0.4044 0.2953 0.4171 0.0083  -0.0184 0.0042  1116 LEU B CD2 
16793 N N   . ALA B 1119 ? 0.2652 0.1917 0.2868 0.0173  -0.0080 0.0062  1117 ALA B N   
16794 C CA  . ALA B 1119 ? 0.2892 0.2197 0.3101 0.0229  -0.0068 0.0047  1117 ALA B CA  
16795 C C   . ALA B 1119 ? 0.2763 0.2181 0.3011 0.0227  -0.0043 0.0034  1117 ALA B C   
16796 O O   . ALA B 1119 ? 0.2509 0.1955 0.2756 0.0259  -0.0038 0.0007  1117 ALA B O   
16797 C CB  . ALA B 1119 ? 0.2646 0.1945 0.2840 0.0250  -0.0068 0.0075  1117 ALA B CB  
16798 N N   . ALA B 1120 ? 0.2605 0.2087 0.2886 0.0190  -0.0028 0.0054  1118 ALA B N   
16799 C CA  . ALA B 1120 ? 0.2691 0.2273 0.3006 0.0186  -0.0006 0.0043  1118 ALA B CA  
16800 C C   . ALA B 1120 ? 0.2750 0.2337 0.3075 0.0180  -0.0008 0.0013  1118 ALA B C   
16801 O O   . ALA B 1120 ? 0.2085 0.1724 0.2418 0.0203  0.0002  -0.0007 1118 ALA B O   
16802 C CB  . ALA B 1120 ? 0.2595 0.2231 0.2938 0.0145  0.0009  0.0068  1118 ALA B CB  
16803 N N   . ALA B 1121 ? 0.2251 0.1786 0.2576 0.0148  -0.0023 0.0012  1119 ALA B N   
16804 C CA  . ALA B 1121 ? 0.2220 0.1762 0.2555 0.0139  -0.0028 -0.0015 1119 ALA B CA  
16805 C C   . ALA B 1121 ? 0.2258 0.1751 0.2558 0.0181  -0.0040 -0.0044 1119 ALA B C   
16806 O O   . ALA B 1121 ? 0.2234 0.1764 0.2540 0.0193  -0.0034 -0.0068 1119 ALA B O   
16807 C CB  . ALA B 1121 ? 0.2316 0.1818 0.2662 0.0092  -0.0043 -0.0007 1119 ALA B CB  
16808 N N   . LEU B 1122 ? 0.2264 0.1674 0.2525 0.0204  -0.0056 -0.0042 1120 LEU B N   
16809 C CA  . LEU B 1122 ? 0.2328 0.1691 0.2552 0.0248  -0.0066 -0.0071 1120 LEU B CA  
16810 C C   . LEU B 1122 ? 0.2420 0.1854 0.2649 0.0293  -0.0046 -0.0080 1120 LEU B C   
16811 O O   . LEU B 1122 ? 0.2608 0.2055 0.2825 0.0320  -0.0043 -0.0107 1120 LEU B O   
16812 C CB  . LEU B 1122 ? 0.2538 0.1791 0.2717 0.0266  -0.0089 -0.0066 1120 LEU B CB  
16813 C CG  . LEU B 1122 ? 0.2783 0.1946 0.2947 0.0223  -0.0115 -0.0059 1120 LEU B CG  
16814 C CD1 . LEU B 1122 ? 0.2868 0.1923 0.2983 0.0247  -0.0137 -0.0052 1120 LEU B CD1 
16815 C CD2 . LEU B 1122 ? 0.2762 0.1902 0.2918 0.0213  -0.0128 -0.0089 1120 LEU B CD2 
16816 N N   . ALA B 1123 ? 0.2212 0.1696 0.2456 0.0299  -0.0032 -0.0057 1121 ALA B N   
16817 C CA  . ALA B 1123 ? 0.2669 0.2226 0.2920 0.0338  -0.0015 -0.0062 1121 ALA B CA  
16818 C C   . ALA B 1123 ? 0.2731 0.2369 0.3009 0.0328  0.0001  -0.0078 1121 ALA B C   
16819 O O   . ALA B 1123 ? 0.2499 0.2188 0.2778 0.0361  0.0012  -0.0090 1121 ALA B O   
16820 C CB  . ALA B 1123 ? 0.2441 0.2038 0.2707 0.0338  -0.0005 -0.0032 1121 ALA B CB  
16821 N N   . THR B 1124 ? 0.2104 0.1759 0.2406 0.0284  0.0003  -0.0076 1122 THR B N   
16822 C CA  . THR B 1124 ? 0.2236 0.1961 0.2563 0.0272  0.0015  -0.0090 1122 THR B CA  
16823 C C   . THR B 1124 ? 0.1964 0.1652 0.2278 0.0266  0.0003  -0.0115 1122 THR B C   
16824 O O   . THR B 1124 ? 0.2299 0.2032 0.2634 0.0247  0.0009  -0.0125 1122 THR B O   
16825 C CB  . THR B 1124 ? 0.2219 0.1998 0.2582 0.0232  0.0026  -0.0071 1122 THR B CB  
16826 O OG1 . THR B 1124 ? 0.2379 0.2110 0.2744 0.0200  0.0016  -0.0055 1122 THR B OG1 
16827 C CG2 . THR B 1124 ? 0.2391 0.2225 0.2762 0.0244  0.0041  -0.0052 1122 THR B CG2 
16828 N N   . GLY B 1125 ? 0.2248 0.1853 0.2527 0.0283  -0.0015 -0.0127 1123 GLY B N   
16829 C CA  . GLY B 1125 ? 0.2390 0.1955 0.2647 0.0285  -0.0027 -0.0155 1123 GLY B CA  
16830 C C   . GLY B 1125 ? 0.2538 0.2067 0.2806 0.0239  -0.0044 -0.0154 1123 GLY B C   
16831 O O   . GLY B 1125 ? 0.2492 0.1993 0.2745 0.0235  -0.0056 -0.0177 1123 GLY B O   
16832 N N   . ASN B 1126 ? 0.2205 0.1737 0.2499 0.0203  -0.0044 -0.0129 1124 ASN B N   
16833 C CA  . ASN B 1126 ? 0.2476 0.1995 0.2791 0.0156  -0.0057 -0.0124 1124 ASN B CA  
16834 C C   . ASN B 1126 ? 0.2436 0.1851 0.2721 0.0143  -0.0085 -0.0124 1124 ASN B C   
16835 O O   . ASN B 1126 ? 0.2409 0.1760 0.2658 0.0167  -0.0093 -0.0120 1124 ASN B O   
16836 C CB  . ASN B 1126 ? 0.2101 0.1680 0.2459 0.0122  -0.0042 -0.0096 1124 ASN B CB  
16837 C CG  . ASN B 1126 ? 0.2088 0.1761 0.2472 0.0132  -0.0018 -0.0097 1124 ASN B CG  
16838 O OD1 . ASN B 1126 ? 0.2501 0.2214 0.2900 0.0126  -0.0014 -0.0112 1124 ASN B OD1 
16839 N ND2 . ASN B 1126 ? 0.2263 0.1969 0.2651 0.0146  -0.0002 -0.0080 1124 ASN B ND2 
16840 N N   . SER B 1127 ? 0.2589 0.1985 0.2885 0.0105  -0.0101 -0.0128 1125 SER B N   
16841 C CA  . SER B 1127 ? 0.2629 0.1941 0.2911 0.0074  -0.0128 -0.0117 1125 SER B CA  
16842 C C   . SER B 1127 ? 0.2574 0.1929 0.2901 0.0029  -0.0119 -0.0083 1125 SER B C   
16843 O O   . SER B 1127 ? 0.2441 0.1885 0.2806 0.0025  -0.0094 -0.0072 1125 SER B O   
16844 C CB  . SER B 1127 ? 0.2614 0.1886 0.2885 0.0054  -0.0152 -0.0140 1125 SER B CB  
16845 O OG  . SER B 1127 ? 0.3242 0.2595 0.3562 0.0025  -0.0144 -0.0138 1125 SER B OG  
16846 N N   . VAL B 1128 ? 0.2633 0.1921 0.2953 -0.0006 -0.0141 -0.0066 1126 VAL B N   
16847 C CA  . VAL B 1128 ? 0.2608 0.1936 0.2968 -0.0048 -0.0132 -0.0030 1126 VAL B CA  
16848 C C   . VAL B 1128 ? 0.2623 0.1915 0.2997 -0.0101 -0.0157 -0.0021 1126 VAL B C   
16849 O O   . VAL B 1128 ? 0.2895 0.2102 0.3235 -0.0105 -0.0187 -0.0037 1126 VAL B O   
16850 C CB  . VAL B 1128 ? 0.2633 0.1927 0.2972 -0.0039 -0.0127 -0.0003 1126 VAL B CB  
16851 C CG1 . VAL B 1128 ? 0.2391 0.1725 0.2718 0.0012  -0.0105 -0.0011 1126 VAL B CG1 
16852 C CG2 . VAL B 1128 ? 0.3014 0.2181 0.3302 -0.0041 -0.0160 -0.0002 1126 VAL B CG2 
16853 N N   . ALA B 1129 ? 0.2726 0.2086 0.3150 -0.0143 -0.0145 0.0005  1127 ALA B N   
16854 C CA  . ALA B 1129 ? 0.2371 0.1708 0.2815 -0.0199 -0.0165 0.0027  1127 ALA B CA  
16855 C C   . ALA B 1129 ? 0.2708 0.2062 0.3165 -0.0221 -0.0150 0.0067  1127 ALA B C   
16856 O O   . ALA B 1129 ? 0.2499 0.1945 0.2989 -0.0216 -0.0119 0.0079  1127 ALA B O   
16857 C CB  . ALA B 1129 ? 0.2994 0.2411 0.3493 -0.0230 -0.0163 0.0023  1127 ALA B CB  
16858 N N   . ILE B 1130 ? 0.2518 0.1782 0.2944 -0.0243 -0.0173 0.0086  1128 ILE B N   
16859 C CA  . ILE B 1130 ? 0.2562 0.1828 0.2991 -0.0263 -0.0162 0.0126  1128 ILE B CA  
16860 C C   . ILE B 1130 ? 0.2565 0.1865 0.3038 -0.0328 -0.0167 0.0156  1128 ILE B C   
16861 O O   . ILE B 1130 ? 0.2550 0.1795 0.3020 -0.0363 -0.0198 0.0155  1128 ILE B O   
16862 C CB  . ILE B 1130 ? 0.2952 0.2096 0.3317 -0.0246 -0.0184 0.0133  1128 ILE B CB  
16863 C CG1 . ILE B 1130 ? 0.2661 0.1775 0.2985 -0.0178 -0.0181 0.0100  1128 ILE B CG1 
16864 C CG2 . ILE B 1130 ? 0.2796 0.1951 0.3163 -0.0263 -0.0170 0.0175  1128 ILE B CG2 
16865 C CD1 . ILE B 1130 ? 0.2848 0.1837 0.3109 -0.0157 -0.0206 0.0101  1128 ILE B CD1 
16866 N N   . ASP B 1131 ? 0.2690 0.2080 0.3201 -0.0345 -0.0138 0.0185  1129 ASP B N   
16867 C CA  . ASP B 1131 ? 0.2760 0.2196 0.3316 -0.0407 -0.0137 0.0218  1129 ASP B CA  
16868 C C   . ASP B 1131 ? 0.2972 0.2303 0.3498 -0.0448 -0.0170 0.0245  1129 ASP B C   
16869 O O   . ASP B 1131 ? 0.2991 0.2264 0.3478 -0.0443 -0.0170 0.0266  1129 ASP B O   
16870 C CB  . ASP B 1131 ? 0.2967 0.2503 0.3554 -0.0410 -0.0098 0.0246  1129 ASP B CB  
16871 C CG  . ASP B 1131 ? 0.3040 0.2635 0.3675 -0.0471 -0.0092 0.0282  1129 ASP B CG  
16872 O OD1 . ASP B 1131 ? 0.2710 0.2328 0.3383 -0.0501 -0.0107 0.0276  1129 ASP B OD1 
16873 O OD2 . ASP B 1131 ? 0.2841 0.2464 0.3478 -0.0487 -0.0073 0.0318  1129 ASP B OD2 
16874 N N   . ALA B 1132 ? 0.3185 0.2488 0.3726 -0.0492 -0.0199 0.0244  1130 ALA B N   
16875 C CA  . ALA B 1132 ? 0.2746 0.1938 0.3254 -0.0535 -0.0236 0.0267  1130 ALA B CA  
16876 C C   . ALA B 1132 ? 0.3393 0.2615 0.3921 -0.0583 -0.0224 0.0319  1130 ALA B C   
16877 O O   . ALA B 1132 ? 0.3345 0.2467 0.3831 -0.0606 -0.0247 0.0344  1130 ALA B O   
16878 C CB  . ALA B 1132 ? 0.3147 0.2313 0.3672 -0.0574 -0.0270 0.0254  1130 ALA B CB  
16879 N N   . ALA B 1133 ? 0.3033 0.2389 0.3622 -0.0598 -0.0188 0.0338  1131 ALA B N   
16880 C CA  . ALA B 1133 ? 0.3318 0.2713 0.3925 -0.0643 -0.0172 0.0389  1131 ALA B CA  
16881 C C   . ALA B 1133 ? 0.3461 0.2812 0.4018 -0.0614 -0.0158 0.0406  1131 ALA B C   
16882 O O   . ALA B 1133 ? 0.3649 0.3001 0.4204 -0.0652 -0.0152 0.0450  1131 ALA B O   
16883 C CB  . ALA B 1133 ? 0.3425 0.2980 0.4106 -0.0657 -0.0133 0.0400  1131 ALA B CB  
16884 N N   . SER B 1134 ? 0.3281 0.2597 0.3798 -0.0549 -0.0153 0.0373  1132 SER B N   
16885 C CA  . SER B 1134 ? 0.3254 0.2520 0.3721 -0.0518 -0.0146 0.0387  1132 SER B CA  
16886 C C   . SER B 1134 ? 0.3259 0.2390 0.3673 -0.0546 -0.0182 0.0414  1132 SER B C   
16887 O O   . SER B 1134 ? 0.3507 0.2606 0.3889 -0.0542 -0.0177 0.0443  1132 SER B O   
16888 C CB  . SER B 1134 ? 0.3210 0.2455 0.3645 -0.0444 -0.0141 0.0345  1132 SER B CB  
16889 O OG  . SER B 1134 ? 0.3129 0.2272 0.3530 -0.0429 -0.0177 0.0314  1132 SER B OG  
16890 N N   . GLY B 1135 ? 0.3094 0.2142 0.3497 -0.0573 -0.0221 0.0403  1133 GLY B N   
16891 C CA  . GLY B 1135 ? 0.3680 0.2587 0.4028 -0.0599 -0.0260 0.0424  1133 GLY B CA  
16892 C C   . GLY B 1135 ? 0.4395 0.3185 0.4671 -0.0539 -0.0276 0.0404  1133 GLY B C   
16893 O O   . GLY B 1135 ? 0.3981 0.2655 0.4205 -0.0553 -0.0304 0.0428  1133 GLY B O   
16894 N N   . LEU B 1136 ? 0.3710 0.2528 0.3979 -0.0472 -0.0261 0.0362  1134 LEU B N   
16895 C CA  . LEU B 1136 ? 0.3560 0.2293 0.3768 -0.0408 -0.0269 0.0345  1134 LEU B CA  
16896 C C   . LEU B 1136 ? 0.3914 0.2539 0.4078 -0.0377 -0.0303 0.0303  1134 LEU B C   
16897 O O   . LEU B 1136 ? 0.4008 0.2586 0.4130 -0.0313 -0.0305 0.0277  1134 LEU B O   
16898 C CB  . LEU B 1136 ? 0.3493 0.2330 0.3720 -0.0353 -0.0229 0.0329  1134 LEU B CB  
16899 C CG  . LEU B 1136 ? 0.3395 0.2324 0.3650 -0.0373 -0.0196 0.0369  1134 LEU B CG  
16900 C CD1 . LEU B 1136 ? 0.3348 0.2392 0.3631 -0.0328 -0.0157 0.0349  1134 LEU B CD1 
16901 C CD2 . LEU B 1136 ? 0.4273 0.3114 0.4476 -0.0372 -0.0209 0.0404  1134 LEU B CD2 
16902 N N   . GLN B 1137 ? 0.4096 0.2681 0.4267 -0.0422 -0.0332 0.0296  1135 GLN B N   
16903 C CA  . GLN B 1137 ? 0.4201 0.2688 0.4329 -0.0395 -0.0364 0.0253  1135 GLN B CA  
16904 C C   . GLN B 1137 ? 0.4659 0.2997 0.4706 -0.0355 -0.0391 0.0248  1135 GLN B C   
16905 O O   . GLN B 1137 ? 0.4957 0.3244 0.4964 -0.0295 -0.0399 0.0207  1135 GLN B O   
16906 C CB  . GLN B 1137 ? 0.4527 0.2983 0.4671 -0.0460 -0.0396 0.0255  1135 GLN B CB  
16907 C CG  . GLN B 1137 ? 0.4260 0.2853 0.4480 -0.0486 -0.0375 0.0246  1135 GLN B CG  
16908 C CD  . GLN B 1137 ? 0.4119 0.2830 0.4404 -0.0537 -0.0346 0.0290  1135 GLN B CD  
16909 O OE1 . GLN B 1137 ? 0.4129 0.2833 0.4404 -0.0548 -0.0335 0.0328  1135 GLN B OE1 
16910 N NE2 . GLN B 1137 ? 0.4303 0.3122 0.4654 -0.0568 -0.0334 0.0287  1135 GLN B NE2 
16911 N N   . ALA B 1138 ? 0.4567 0.2835 0.4587 -0.0385 -0.0405 0.0290  1136 ALA B N   
16912 C CA  . ALA B 1138 ? 0.4855 0.2974 0.4796 -0.0347 -0.0435 0.0288  1136 ALA B CA  
16913 C C   . ALA B 1138 ? 0.5181 0.3324 0.5102 -0.0265 -0.0410 0.0271  1136 ALA B C   
16914 O O   . ALA B 1138 ? 0.5215 0.3243 0.5072 -0.0218 -0.0432 0.0260  1136 ALA B O   
16915 C CB  . ALA B 1138 ? 0.4701 0.2744 0.4618 -0.0401 -0.0455 0.0341  1136 ALA B CB  
16916 N N   . SER B 1139 ? 0.4819 0.3110 0.4795 -0.0247 -0.0366 0.0271  1137 SER B N   
16917 C CA  . SER B 1139 ? 0.4523 0.2848 0.4486 -0.0175 -0.0343 0.0258  1137 SER B CA  
16918 C C   . SER B 1139 ? 0.4802 0.3118 0.4747 -0.0110 -0.0343 0.0205  1137 SER B C   
16919 O O   . SER B 1139 ? 0.4826 0.3150 0.4751 -0.0045 -0.0331 0.0192  1137 SER B O   
16920 C CB  . SER B 1139 ? 0.3608 0.2090 0.3632 -0.0182 -0.0298 0.0277  1137 SER B CB  
16921 O OG  . SER B 1139 ? 0.4322 0.2810 0.4352 -0.0228 -0.0294 0.0328  1137 SER B OG  
16922 N N   . LEU B 1140 ? 0.4564 0.2868 0.4515 -0.0125 -0.0357 0.0174  1138 LEU B N   
16923 C CA  . LEU B 1140 ? 0.5132 0.3430 0.5064 -0.0068 -0.0357 0.0123  1138 LEU B CA  
16924 C C   . LEU B 1140 ? 0.4873 0.3016 0.4739 -0.0063 -0.0401 0.0100  1138 LEU B C   
16925 O O   . LEU B 1140 ? 0.5403 0.3535 0.5261 -0.0053 -0.0411 0.0062  1138 LEU B O   
16926 C CB  . LEU B 1140 ? 0.4431 0.2854 0.4423 -0.0082 -0.0332 0.0103  1138 LEU B CB  
16927 C CG  . LEU B 1140 ? 0.4243 0.2815 0.4295 -0.0080 -0.0288 0.0121  1138 LEU B CG  
16928 C CD1 . LEU B 1140 ? 0.4335 0.3019 0.4438 -0.0086 -0.0267 0.0096  1138 LEU B CD1 
16929 C CD2 . LEU B 1140 ? 0.4838 0.3423 0.4868 -0.0014 -0.0271 0.0117  1138 LEU B CD2 
16930 N N   . LYS B 1141 ? 0.5242 0.3261 0.5057 -0.0072 -0.0430 0.0124  1139 LYS B N   
16931 C CA  . LYS B 1141 ? 0.5759 0.3616 0.5502 -0.0064 -0.0476 0.0102  1139 LYS B CA  
16932 C C   . LYS B 1141 ? 0.5994 0.3803 0.5685 0.0026  -0.0475 0.0060  1139 LYS B C   
16933 O O   . LYS B 1141 ? 0.6387 0.4235 0.6078 0.0080  -0.0453 0.0065  1139 LYS B O   
16934 C CB  . LYS B 1141 ? 0.5801 0.3535 0.5503 -0.0102 -0.0508 0.0143  1139 LYS B CB  
16935 N N   . ASN B 1142 ? 0.6072 0.3802 0.5720 0.0044  -0.0500 0.0018  1140 ASN B N   
16936 C CA  . ASN B 1142 ? 0.6250 0.3921 0.5840 0.0130  -0.0503 -0.0025 1140 ASN B CA  
16937 C C   . ASN B 1142 ? 0.5787 0.3605 0.5421 0.0184  -0.0457 -0.0045 1140 ASN B C   
16938 O O   . ASN B 1142 ? 0.5832 0.3640 0.5437 0.0259  -0.0447 -0.0062 1140 ASN B O   
16939 C CB  . ASN B 1142 ? 0.6273 0.3817 0.5798 0.0171  -0.0525 -0.0012 1140 ASN B CB  
16940 N N   . LEU B 1143 ? 0.5945 0.3899 0.5649 0.0148  -0.0429 -0.0041 1141 LEU B N   
16941 C CA  . LEU B 1143 ? 0.5620 0.3707 0.5363 0.0193  -0.0389 -0.0063 1141 LEU B CA  
16942 C C   . LEU B 1143 ? 0.5360 0.3402 0.5054 0.0253  -0.0396 -0.0114 1141 LEU B C   
16943 O O   . LEU B 1143 ? 0.6053 0.3996 0.5703 0.0239  -0.0428 -0.0137 1141 LEU B O   
16944 C CB  . LEU B 1143 ? 0.5335 0.3555 0.5153 0.0140  -0.0366 -0.0056 1141 LEU B CB  
16945 C CG  . LEU B 1143 ? 0.5296 0.3641 0.5182 0.0110  -0.0334 -0.0018 1141 LEU B CG  
16946 C CD1 . LEU B 1143 ? 0.4559 0.3028 0.4507 0.0080  -0.0311 -0.0028 1141 LEU B CD1 
16947 C CD2 . LEU B 1143 ? 0.4227 0.2626 0.4116 0.0168  -0.0307 -0.0012 1141 LEU B CD2 
16948 N N   . PRO B 1144 ? 0.5509 0.3623 0.5209 0.0319  -0.0367 -0.0132 1142 PRO B N   
16949 C CA  . PRO B 1144 ? 0.5181 0.3283 0.4845 0.0372  -0.0366 -0.0180 1142 PRO B CA  
16950 C C   . PRO B 1144 ? 0.5048 0.3208 0.4742 0.0329  -0.0363 -0.0197 1142 PRO B C   
16951 O O   . PRO B 1144 ? 0.4746 0.3013 0.4508 0.0281  -0.0343 -0.0176 1142 PRO B O   
16952 C CB  . PRO B 1144 ? 0.5461 0.3668 0.5147 0.0437  -0.0328 -0.0185 1142 PRO B CB  
16953 C CG  . PRO B 1144 ? 0.5716 0.3934 0.5422 0.0433  -0.0323 -0.0143 1142 PRO B CG  
16954 C CD  . PRO B 1144 ? 0.5489 0.3700 0.5226 0.0349  -0.0335 -0.0109 1142 PRO B CD  
16955 N N   . GLN B 1145 ? 0.5088 0.3174 0.4730 0.0348  -0.0383 -0.0237 1143 GLN B N   
16956 C CA  . GLN B 1145 ? 0.4846 0.2977 0.4508 0.0311  -0.0384 -0.0256 1143 GLN B CA  
16957 C C   . GLN B 1145 ? 0.4842 0.3137 0.4569 0.0320  -0.0341 -0.0257 1143 GLN B C   
16958 O O   . GLN B 1145 ? 0.4259 0.2626 0.4034 0.0271  -0.0336 -0.0252 1143 GLN B O   
16959 C CB  . GLN B 1145 ? 0.5041 0.3070 0.4627 0.0346  -0.0408 -0.0303 1143 GLN B CB  
16960 N N   . THR B 1146 ? 0.4902 0.3258 0.4632 0.0382  -0.0312 -0.0262 1144 THR B N   
16961 C CA  . THR B 1146 ? 0.4816 0.3323 0.4604 0.0389  -0.0273 -0.0261 1144 THR B CA  
16962 C C   . THR B 1146 ? 0.4108 0.2704 0.3968 0.0332  -0.0258 -0.0222 1144 THR B C   
16963 O O   . THR B 1146 ? 0.4630 0.3326 0.4540 0.0305  -0.0240 -0.0221 1144 THR B O   
16964 C CB  . THR B 1146 ? 0.4541 0.3095 0.4322 0.0461  -0.0247 -0.0268 1144 THR B CB  
16965 O OG1 . THR B 1146 ? 0.4827 0.3326 0.4594 0.0476  -0.0255 -0.0243 1144 THR B OG1 
16966 C CG2 . THR B 1146 ? 0.5528 0.4031 0.5246 0.0521  -0.0252 -0.0311 1144 THR B CG2 
16967 N N   . VAL B 1147 ? 0.3818 0.2377 0.3683 0.0315  -0.0266 -0.0189 1145 VAL B N   
16968 C CA  . VAL B 1147 ? 0.3917 0.2558 0.3846 0.0262  -0.0251 -0.0151 1145 VAL B CA  
16969 C C   . VAL B 1147 ? 0.4150 0.2766 0.4097 0.0191  -0.0272 -0.0142 1145 VAL B C   
16970 O O   . VAL B 1147 ? 0.3694 0.2406 0.3699 0.0151  -0.0256 -0.0129 1145 VAL B O   
16971 C CB  . VAL B 1147 ? 0.3856 0.2471 0.3781 0.0270  -0.0250 -0.0117 1145 VAL B CB  
16972 C CG1 . VAL B 1147 ? 0.3725 0.2438 0.3714 0.0222  -0.0229 -0.0080 1145 VAL B CG1 
16973 C CG2 . VAL B 1147 ? 0.3856 0.2488 0.3759 0.0345  -0.0234 -0.0127 1145 VAL B CG2 
16974 N N   . GLY B 1148 ? 0.4016 0.2503 0.3913 0.0175  -0.0309 -0.0147 1146 GLY B N   
16975 C CA  . GLY B 1148 ? 0.4220 0.2683 0.4136 0.0105  -0.0332 -0.0137 1146 GLY B CA  
16976 C C   . GLY B 1148 ? 0.4100 0.2636 0.4047 0.0087  -0.0326 -0.0159 1146 GLY B C   
16977 O O   . GLY B 1148 ? 0.4155 0.2741 0.4150 0.0029  -0.0328 -0.0142 1146 GLY B O   
16978 N N   . LEU B 1149 ? 0.3893 0.2439 0.3812 0.0138  -0.0318 -0.0197 1147 LEU B N   
16979 C CA  . LEU B 1149 ? 0.3769 0.2382 0.3712 0.0124  -0.0313 -0.0218 1147 LEU B CA  
16980 C C   . LEU B 1149 ? 0.3463 0.2221 0.3482 0.0105  -0.0278 -0.0199 1147 LEU B C   
16981 O O   . LEU B 1149 ? 0.3715 0.2532 0.3768 0.0075  -0.0277 -0.0205 1147 LEU B O   
16982 C CB  . LEU B 1149 ? 0.4547 0.3140 0.4440 0.0184  -0.0310 -0.0260 1147 LEU B CB  
16983 N N   . ARG B 1150 ? 0.3399 0.2213 0.3444 0.0121  -0.0252 -0.0175 1148 ARG B N   
16984 C CA  . ARG B 1150 ? 0.3279 0.2222 0.3391 0.0102  -0.0221 -0.0155 1148 ARG B CA  
16985 C C   . ARG B 1150 ? 0.3315 0.2278 0.3470 0.0044  -0.0223 -0.0118 1148 ARG B C   
16986 O O   . ARG B 1150 ? 0.2910 0.1976 0.3118 0.0027  -0.0197 -0.0101 1148 ARG B O   
16987 C CB  . ARG B 1150 ? 0.3210 0.2213 0.3327 0.0149  -0.0190 -0.0150 1148 ARG B CB  
16988 C CG  . ARG B 1150 ? 0.3483 0.2507 0.3574 0.0203  -0.0178 -0.0183 1148 ARG B CG  
16989 C CD  . ARG B 1150 ? 0.3612 0.2750 0.3744 0.0220  -0.0144 -0.0173 1148 ARG B CD  
16990 N NE  . ARG B 1150 ? 0.3391 0.2557 0.3500 0.0274  -0.0130 -0.0198 1148 ARG B NE  
16991 C CZ  . ARG B 1150 ? 0.3340 0.2583 0.3468 0.0303  -0.0104 -0.0190 1148 ARG B CZ  
16992 N NH1 . ARG B 1150 ? 0.2772 0.2069 0.2939 0.0285  -0.0090 -0.0160 1148 ARG B NH1 
16993 N NH2 . ARG B 1150 ? 0.2977 0.2247 0.3085 0.0351  -0.0092 -0.0212 1148 ARG B NH2 
16994 N N   . VAL B 1151 ? 0.3484 0.2352 0.3615 0.0014  -0.0252 -0.0104 1149 VAL B N   
16995 C CA  . VAL B 1151 ? 0.3461 0.2342 0.3627 -0.0039 -0.0252 -0.0063 1149 VAL B CA  
16996 C C   . VAL B 1151 ? 0.3802 0.2658 0.3984 -0.0098 -0.0279 -0.0060 1149 VAL B C   
16997 O O   . VAL B 1151 ? 0.3809 0.2562 0.3945 -0.0103 -0.0313 -0.0078 1149 VAL B O   
16998 C CB  . VAL B 1151 ? 0.3710 0.2502 0.3837 -0.0031 -0.0264 -0.0041 1149 VAL B CB  
16999 C CG1 . VAL B 1151 ? 0.3911 0.2701 0.4067 -0.0095 -0.0272 0.0001  1149 VAL B CG1 
17000 C CG2 . VAL B 1151 ? 0.3784 0.2619 0.3907 0.0022  -0.0236 -0.0037 1149 VAL B CG2 
17001 N N   . SER B 1152 ? 0.3555 0.2506 0.3802 -0.0143 -0.0265 -0.0038 1150 SER B N   
17002 C CA  . SER B 1152 ? 0.3429 0.2369 0.3701 -0.0206 -0.0289 -0.0024 1150 SER B CA  
17003 C C   . SER B 1152 ? 0.3415 0.2406 0.3732 -0.0249 -0.0275 0.0021  1150 SER B C   
17004 O O   . SER B 1152 ? 0.3026 0.2075 0.3358 -0.0229 -0.0244 0.0037  1150 SER B O   
17005 C CB  . SER B 1152 ? 0.3242 0.2256 0.3553 -0.0218 -0.0287 -0.0045 1150 SER B CB  
17006 O OG  . SER B 1152 ? 0.3855 0.2995 0.4219 -0.0207 -0.0250 -0.0038 1150 SER B OG  
17007 N N   . TRP B 1153 ? 0.2802 0.1769 0.3138 -0.0310 -0.0299 0.0043  1151 TRP B N   
17008 C CA  . TRP B 1153 ? 0.3024 0.2045 0.3405 -0.0358 -0.0286 0.0088  1151 TRP B CA  
17009 C C   . TRP B 1153 ? 0.3266 0.2386 0.3715 -0.0402 -0.0282 0.0094  1151 TRP B C   
17010 O O   . TRP B 1153 ? 0.3036 0.2132 0.3486 -0.0420 -0.0309 0.0074  1151 TRP B O   
17011 C CB  . TRP B 1153 ? 0.3196 0.2106 0.3541 -0.0396 -0.0317 0.0115  1151 TRP B CB  
17012 C CG  . TRP B 1153 ? 0.3644 0.2462 0.3925 -0.0351 -0.0319 0.0114  1151 TRP B CG  
17013 C CD1 . TRP B 1153 ? 0.3524 0.2235 0.3738 -0.0306 -0.0341 0.0082  1151 TRP B CD1 
17014 C CD2 . TRP B 1153 ? 0.3552 0.2382 0.3830 -0.0345 -0.0299 0.0147  1151 TRP B CD2 
17015 N NE1 . TRP B 1153 ? 0.3726 0.2382 0.3899 -0.0270 -0.0335 0.0093  1151 TRP B NE1 
17016 C CE2 . TRP B 1153 ? 0.4075 0.2801 0.4285 -0.0295 -0.0311 0.0134  1151 TRP B CE2 
17017 C CE3 . TRP B 1153 ? 0.3335 0.2253 0.3659 -0.0376 -0.0271 0.0187  1151 TRP B CE3 
17018 C CZ2 . TRP B 1153 ? 0.4003 0.2711 0.4192 -0.0276 -0.0299 0.0159  1151 TRP B CZ2 
17019 C CZ3 . TRP B 1153 ? 0.3415 0.2312 0.3713 -0.0358 -0.0259 0.0212  1151 TRP B CZ3 
17020 C CH2 . TRP B 1153 ? 0.3592 0.2385 0.3825 -0.0309 -0.0273 0.0199  1151 TRP B CH2 
17021 N N   . SER B 1154 ? 0.2752 0.1985 0.3257 -0.0417 -0.0248 0.0119  1152 SER B N   
17022 C CA  . SER B 1154 ? 0.2595 0.1937 0.3171 -0.0450 -0.0240 0.0124  1152 SER B CA  
17023 C C   . SER B 1154 ? 0.2714 0.2108 0.3335 -0.0505 -0.0231 0.0171  1152 SER B C   
17024 O O   . SER B 1154 ? 0.2698 0.2127 0.3322 -0.0499 -0.0203 0.0195  1152 SER B O   
17025 C CB  . SER B 1154 ? 0.2582 0.2030 0.3188 -0.0408 -0.0204 0.0105  1152 SER B CB  
17026 O OG  . SER B 1154 ? 0.2704 0.2250 0.3375 -0.0438 -0.0199 0.0110  1152 SER B OG  
17027 N N   . LYS B 1155 ? 0.2846 0.2253 0.3503 -0.0561 -0.0254 0.0183  1153 LYS B N   
17028 C CA  . LYS B 1155 ? 0.2910 0.2399 0.3627 -0.0616 -0.0242 0.0226  1153 LYS B CA  
17029 C C   . LYS B 1155 ? 0.3230 0.2862 0.4021 -0.0618 -0.0218 0.0222  1153 LYS B C   
17030 O O   . LYS B 1155 ? 0.4082 0.3802 0.4930 -0.0658 -0.0202 0.0255  1153 LYS B O   
17031 C CB  . LYS B 1155 ? 0.3356 0.2775 0.4071 -0.0681 -0.0284 0.0248  1153 LYS B CB  
17032 N N   . ASP B 1156 ? 0.2737 0.2392 0.3528 -0.0575 -0.0214 0.0183  1154 ASP B N   
17033 C CA  . ASP B 1156 ? 0.2534 0.2308 0.3389 -0.0573 -0.0199 0.0174  1154 ASP B CA  
17034 C C   . ASP B 1156 ? 0.2356 0.2151 0.3191 -0.0508 -0.0176 0.0139  1154 ASP B C   
17035 O O   . ASP B 1156 ? 0.2197 0.1951 0.3006 -0.0483 -0.0195 0.0104  1154 ASP B O   
17036 C CB  . ASP B 1156 ? 0.2438 0.2198 0.3314 -0.0609 -0.0238 0.0164  1154 ASP B CB  
17037 C CG  . ASP B 1156 ? 0.2041 0.1929 0.2991 -0.0614 -0.0225 0.0161  1154 ASP B CG  
17038 O OD1 . ASP B 1156 ? 0.2245 0.2214 0.3216 -0.0575 -0.0189 0.0153  1154 ASP B OD1 
17039 O OD2 . ASP B 1156 ? 0.2629 0.2533 0.3615 -0.0657 -0.0253 0.0168  1154 ASP B OD2 
17040 N N   . TRP B 1157 ? 0.1951 0.1810 0.2795 -0.0482 -0.0137 0.0148  1155 TRP B N   
17041 C CA  . TRP B 1157 ? 0.2264 0.2134 0.3082 -0.0422 -0.0116 0.0118  1155 TRP B CA  
17042 C C   . TRP B 1157 ? 0.2381 0.2311 0.3231 -0.0406 -0.0117 0.0091  1155 TRP B C   
17043 O O   . TRP B 1157 ? 0.2390 0.2288 0.3206 -0.0367 -0.0122 0.0059  1155 TRP B O   
17044 C CB  . TRP B 1157 ? 0.2182 0.2113 0.3007 -0.0403 -0.0076 0.0135  1155 TRP B CB  
17045 C CG  . TRP B 1157 ? 0.2152 0.2033 0.2947 -0.0417 -0.0072 0.0165  1155 TRP B CG  
17046 C CD1 . TRP B 1157 ? 0.2133 0.1907 0.2887 -0.0437 -0.0102 0.0174  1155 TRP B CD1 
17047 C CD2 . TRP B 1157 ? 0.2263 0.2193 0.3061 -0.0411 -0.0039 0.0189  1155 TRP B CD2 
17048 N NE1 . TRP B 1157 ? 0.2411 0.2167 0.3145 -0.0444 -0.0089 0.0204  1155 TRP B NE1 
17049 C CE2 . TRP B 1157 ? 0.2217 0.2069 0.2977 -0.0429 -0.0050 0.0214  1155 TRP B CE2 
17050 C CE3 . TRP B 1157 ? 0.2336 0.2364 0.3160 -0.0391 -0.0002 0.0191  1155 TRP B CE3 
17051 C CZ2 . TRP B 1157 ? 0.2347 0.2220 0.3097 -0.0428 -0.0025 0.0242  1155 TRP B CZ2 
17052 C CZ3 . TRP B 1157 ? 0.2634 0.2681 0.3446 -0.0390 0.0023  0.0217  1155 TRP B CZ3 
17053 C CH2 . TRP B 1157 ? 0.2474 0.2446 0.3249 -0.0409 0.0011  0.0243  1155 TRP B CH2 
17054 N N   . ALA B 1158 ? 0.2049 0.2070 0.2963 -0.0435 -0.0112 0.0105  1156 ALA B N   
17055 C CA  . ALA B 1158 ? 0.2434 0.2517 0.3380 -0.0418 -0.0112 0.0081  1156 ALA B CA  
17056 C C   . ALA B 1158 ? 0.2338 0.2353 0.3261 -0.0422 -0.0152 0.0056  1156 ALA B C   
17057 O O   . ALA B 1158 ? 0.2581 0.2602 0.3494 -0.0390 -0.0155 0.0026  1156 ALA B O   
17058 C CB  . ALA B 1158 ? 0.1934 0.2132 0.2957 -0.0446 -0.0099 0.0103  1156 ALA B CB  
17059 N N   . ALA B 1159 ? 0.2175 0.2121 0.3086 -0.0463 -0.0185 0.0067  1157 ALA B N   
17060 C CA  . ALA B 1159 ? 0.2409 0.2285 0.3294 -0.0470 -0.0225 0.0042  1157 ALA B CA  
17061 C C   . ALA B 1159 ? 0.2835 0.2606 0.3641 -0.0429 -0.0233 0.0013  1157 ALA B C   
17062 O O   . ALA B 1159 ? 0.2708 0.2435 0.3484 -0.0415 -0.0257 -0.0016 1157 ALA B O   
17063 C CB  . ALA B 1159 ? 0.2285 0.2118 0.3181 -0.0530 -0.0260 0.0064  1157 ALA B CB  
17064 N N   . ASP B 1160 ? 0.2607 0.2342 0.3377 -0.0407 -0.0214 0.0021  1158 ASP B N   
17065 C CA  . ASP B 1160 ? 0.2917 0.2552 0.3614 -0.0369 -0.0222 -0.0002 1158 ASP B CA  
17066 C C   . ASP B 1160 ? 0.3205 0.2872 0.3883 -0.0313 -0.0193 -0.0024 1158 ASP B C   
17067 O O   . ASP B 1160 ? 0.3363 0.2960 0.3984 -0.0277 -0.0196 -0.0043 1158 ASP B O   
17068 C CB  . ASP B 1160 ? 0.2683 0.2248 0.3348 -0.0381 -0.0223 0.0022  1158 ASP B CB  
17069 C CG  . ASP B 1160 ? 0.2974 0.2473 0.3636 -0.0435 -0.0260 0.0039  1158 ASP B CG  
17070 O OD1 . ASP B 1160 ? 0.3474 0.2965 0.4147 -0.0458 -0.0288 0.0026  1158 ASP B OD1 
17071 O OD2 . ASP B 1160 ? 0.2998 0.2452 0.3646 -0.0456 -0.0261 0.0066  1158 ASP B OD2 
17072 N N   . GLY B 1161 ? 0.2542 0.2313 0.3267 -0.0303 -0.0166 -0.0021 1159 GLY B N   
17073 C CA  . GLY B 1161 ? 0.2530 0.2332 0.3239 -0.0255 -0.0141 -0.0040 1159 GLY B CA  
17074 C C   . GLY B 1161 ? 0.2910 0.2712 0.3609 -0.0237 -0.0156 -0.0072 1159 GLY B C   
17075 O O   . GLY B 1161 ? 0.3279 0.3031 0.3965 -0.0254 -0.0188 -0.0084 1159 GLY B O   
17076 N N   . PRO B 1162 ? 0.3358 0.3214 0.4061 -0.0203 -0.0133 -0.0085 1160 PRO B N   
17077 C CA  . PRO B 1162 ? 0.2856 0.2772 0.3573 -0.0182 -0.0098 -0.0074 1160 PRO B CA  
17078 C C   . PRO B 1162 ? 0.2808 0.2672 0.3477 -0.0156 -0.0087 -0.0074 1160 PRO B C   
17079 O O   . PRO B 1162 ? 0.2780 0.2575 0.3401 -0.0135 -0.0101 -0.0092 1160 PRO B O   
17080 C CB  . PRO B 1162 ? 0.3325 0.3293 0.4050 -0.0156 -0.0089 -0.0095 1160 PRO B CB  
17081 C CG  . PRO B 1162 ? 0.3207 0.3111 0.3889 -0.0144 -0.0114 -0.0122 1160 PRO B CG  
17082 C CD  . PRO B 1162 ? 0.3328 0.3177 0.4011 -0.0180 -0.0145 -0.0115 1160 PRO B CD  
17083 N N   . PHE B 1163 ? 0.2086 0.1981 0.2765 -0.0156 -0.0063 -0.0052 1161 PHE B N   
17084 C CA  . PHE B 1163 ? 0.2304 0.2162 0.2942 -0.0127 -0.0052 -0.0051 1161 PHE B CA  
17085 C C   . PHE B 1163 ? 0.2334 0.2247 0.2971 -0.0093 -0.0028 -0.0062 1161 PHE B C   
17086 O O   . PHE B 1163 ? 0.2356 0.2330 0.3021 -0.0093 -0.0019 -0.0068 1161 PHE B O   
17087 C CB  . PHE B 1163 ? 0.2006 0.1856 0.2650 -0.0148 -0.0044 -0.0019 1161 PHE B CB  
17088 C CG  . PHE B 1163 ? 0.2480 0.2281 0.3130 -0.0188 -0.0069 -0.0005 1161 PHE B CG  
17089 C CD1 . PHE B 1163 ? 0.2883 0.2587 0.3489 -0.0185 -0.0097 -0.0016 1161 PHE B CD1 
17090 C CD2 . PHE B 1163 ? 0.2639 0.2490 0.3337 -0.0229 -0.0065 0.0020  1161 PHE B CD2 
17091 C CE1 . PHE B 1163 ? 0.3177 0.2828 0.3785 -0.0225 -0.0123 -0.0004 1161 PHE B CE1 
17092 C CE2 . PHE B 1163 ? 0.2587 0.2394 0.3291 -0.0271 -0.0090 0.0035  1161 PHE B CE2 
17093 C CZ  . PHE B 1163 ? 0.2561 0.2264 0.3219 -0.0270 -0.0121 0.0023  1161 PHE B CZ  
17094 N N   . ALA B 1164 ? 0.2554 0.2440 0.3154 -0.0063 -0.0019 -0.0064 1162 ALA B N   
17095 C CA  . ALA B 1164 ? 0.2635 0.2565 0.3228 -0.0032 0.0001  -0.0074 1162 ALA B CA  
17096 C C   . ALA B 1164 ? 0.3104 0.3062 0.3697 -0.0026 0.0022  -0.0053 1162 ALA B C   
17097 O O   . ALA B 1164 ? 0.3231 0.3218 0.3812 -0.0001 0.0037  -0.0059 1162 ALA B O   
17098 C CB  . ALA B 1164 ? 0.2526 0.2412 0.3076 0.0001  -0.0008 -0.0097 1162 ALA B CB  
17099 N N   . GLY B 1165 ? 0.2341 0.2290 0.2945 -0.0050 0.0024  -0.0028 1163 GLY B N   
17100 C CA  . GLY B 1165 ? 0.2273 0.2243 0.2873 -0.0047 0.0043  -0.0007 1163 GLY B CA  
17101 C C   . GLY B 1165 ? 0.2217 0.2149 0.2817 -0.0075 0.0035  0.0020  1163 GLY B C   
17102 O O   . GLY B 1165 ? 0.2112 0.1995 0.2712 -0.0096 0.0014  0.0019  1163 GLY B O   
17103 N N   . ALA B 1166 ? 0.2106 0.2059 0.2704 -0.0079 0.0052  0.0043  1164 ALA B N   
17104 C CA  . ALA B 1166 ? 0.2190 0.2107 0.2785 -0.0107 0.0045  0.0072  1164 ALA B CA  
17105 C C   . ALA B 1166 ? 0.2428 0.2337 0.2996 -0.0093 0.0057  0.0091  1164 ALA B C   
17106 O O   . ALA B 1166 ? 0.2336 0.2296 0.2904 -0.0074 0.0077  0.0090  1164 ALA B O   
17107 C CB  . ALA B 1166 ? 0.2027 0.1997 0.2667 -0.0147 0.0054  0.0090  1164 ALA B CB  
17108 N N   . LEU B 1167 ? 0.2168 0.2007 0.2711 -0.0103 0.0043  0.0109  1165 LEU B N   
17109 C CA  . LEU B 1167 ? 0.2056 0.1878 0.2572 -0.0094 0.0049  0.0133  1165 LEU B CA  
17110 C C   . LEU B 1167 ? 0.2271 0.2081 0.2796 -0.0137 0.0048  0.0168  1165 LEU B C   
17111 O O   . LEU B 1167 ? 0.2175 0.1930 0.2701 -0.0164 0.0027  0.0173  1165 LEU B O   
17112 C CB  . LEU B 1167 ? 0.2160 0.1902 0.2633 -0.0062 0.0031  0.0125  1165 LEU B CB  
17113 C CG  . LEU B 1167 ? 0.2273 0.2029 0.2736 -0.0019 0.0032  0.0093  1165 LEU B CG  
17114 C CD1 . LEU B 1167 ? 0.2510 0.2188 0.2931 0.0015  0.0014  0.0087  1165 LEU B CD1 
17115 C CD2 . LEU B 1167 ? 0.2334 0.2169 0.2806 -0.0002 0.0056  0.0093  1165 LEU B CD2 
17116 N N   . VAL B 1168 ? 0.2255 0.2112 0.2783 -0.0146 0.0069  0.0193  1166 VAL B N   
17117 C CA  . VAL B 1168 ? 0.2445 0.2307 0.2985 -0.0190 0.0073  0.0228  1166 VAL B CA  
17118 C C   . VAL B 1168 ? 0.2329 0.2164 0.2832 -0.0185 0.0078  0.0257  1166 VAL B C   
17119 O O   . VAL B 1168 ? 0.2270 0.2135 0.2756 -0.0154 0.0092  0.0252  1166 VAL B O   
17120 C CB  . VAL B 1168 ? 0.2431 0.2391 0.3015 -0.0212 0.0098  0.0232  1166 VAL B CB  
17121 C CG1 . VAL B 1168 ? 0.2470 0.2442 0.3071 -0.0260 0.0103  0.0271  1166 VAL B CG1 
17122 C CG2 . VAL B 1168 ? 0.2241 0.2230 0.2861 -0.0210 0.0093  0.0202  1166 VAL B CG2 
17123 N N   . GLU B 1169 ? 0.2405 0.2181 0.2893 -0.0215 0.0063  0.0286  1167 GLU B N   
17124 C CA  . GLU B 1169 ? 0.2390 0.2139 0.2844 -0.0219 0.0066  0.0320  1167 GLU B CA  
17125 C C   . GLU B 1169 ? 0.2943 0.2728 0.3418 -0.0270 0.0078  0.0357  1167 GLU B C   
17126 O O   . GLU B 1169 ? 0.2622 0.2387 0.3118 -0.0308 0.0065  0.0366  1167 GLU B O   
17127 C CB  . GLU B 1169 ? 0.2621 0.2254 0.3032 -0.0208 0.0035  0.0325  1167 GLU B CB  
17128 C CG  . GLU B 1169 ? 0.2969 0.2562 0.3342 -0.0214 0.0032  0.0363  1167 GLU B CG  
17129 C CD  . GLU B 1169 ? 0.2661 0.2132 0.2993 -0.0211 -0.0002 0.0371  1167 GLU B CD  
17130 O OE1 . GLU B 1169 ? 0.3139 0.2559 0.3476 -0.0213 -0.0023 0.0350  1167 GLU B OE1 
17131 O OE2 . GLU B 1169 ? 0.3273 0.2696 0.3567 -0.0205 -0.0009 0.0398  1167 GLU B OE2 
17132 N N   . GLY B 1170 ? 0.2697 0.2535 0.3164 -0.0272 0.0103  0.0379  1168 GLY B N   
17133 C CA  . GLY B 1170 ? 0.3036 0.2910 0.3517 -0.0319 0.0117  0.0418  1168 GLY B CA  
17134 C C   . GLY B 1170 ? 0.3228 0.3174 0.3698 -0.0310 0.0149  0.0432  1168 GLY B C   
17135 O O   . GLY B 1170 ? 0.2636 0.2605 0.3090 -0.0269 0.0158  0.0411  1168 GLY B O   
17136 N N   . ASP B 1171 ? 0.2902 0.2886 0.3381 -0.0350 0.0165  0.0469  1169 ASP B N   
17137 C CA  . ASP B 1171 ? 0.3163 0.3227 0.3635 -0.0344 0.0199  0.0480  1169 ASP B CA  
17138 C C   . ASP B 1171 ? 0.3433 0.3596 0.3951 -0.0339 0.0224  0.0455  1169 ASP B C   
17139 O O   . ASP B 1171 ? 0.3018 0.3187 0.3576 -0.0341 0.0214  0.0430  1169 ASP B O   
17140 C CB  . ASP B 1171 ? 0.3375 0.3444 0.3832 -0.0387 0.0209  0.0531  1169 ASP B CB  
17141 C CG  . ASP B 1171 ? 0.3719 0.3820 0.4223 -0.0439 0.0212  0.0552  1169 ASP B CG  
17142 O OD1 . ASP B 1171 ? 0.3292 0.3429 0.3844 -0.0443 0.0211  0.0527  1169 ASP B OD1 
17143 O OD2 . ASP B 1171 ? 0.4239 0.4331 0.4730 -0.0480 0.0215  0.0596  1169 ASP B OD2 
17144 N N   . ALA B 1172 ? 0.3294 0.3532 0.3806 -0.0330 0.0255  0.0459  1170 ALA B N   
17145 C CA  . ALA B 1172 ? 0.3477 0.3805 0.4025 -0.0316 0.0279  0.0433  1170 ALA B CA  
17146 C C   . ALA B 1172 ? 0.2885 0.3258 0.3494 -0.0350 0.0282  0.0437  1170 ALA B C   
17147 O O   . ALA B 1172 ? 0.2765 0.3167 0.3410 -0.0336 0.0280  0.0405  1170 ALA B O   
17148 C CB  . ALA B 1172 ? 0.3581 0.3976 0.4106 -0.0307 0.0313  0.0444  1170 ALA B CB  
17149 N N   . GLU B 1173 ? 0.3091 0.3473 0.3711 -0.0396 0.0286  0.0477  1171 GLU B N   
17150 C CA  . GLU B 1173 ? 0.2784 0.3217 0.3464 -0.0432 0.0289  0.0484  1171 GLU B CA  
17151 C C   . GLU B 1173 ? 0.2644 0.3016 0.3347 -0.0436 0.0253  0.0463  1171 GLU B C   
17152 O O   . GLU B 1173 ? 0.3100 0.3519 0.3852 -0.0438 0.0253  0.0443  1171 GLU B O   
17153 C CB  . GLU B 1173 ? 0.3668 0.4117 0.4353 -0.0485 0.0297  0.0536  1171 GLU B CB  
17154 N N   . ARG B 1174 ? 0.2831 0.3096 0.3495 -0.0434 0.0223  0.0465  1172 ARG B N   
17155 C CA  . ARG B 1174 ? 0.2753 0.2950 0.3427 -0.0434 0.0188  0.0442  1172 ARG B CA  
17156 C C   . ARG B 1174 ? 0.2513 0.2729 0.3198 -0.0389 0.0188  0.0394  1172 ARG B C   
17157 O O   . ARG B 1174 ? 0.2565 0.2790 0.3287 -0.0393 0.0176  0.0373  1172 ARG B O   
17158 C CB  . ARG B 1174 ? 0.3157 0.3233 0.3779 -0.0434 0.0157  0.0453  1172 ARG B CB  
17159 C CG  . ARG B 1174 ? 0.2937 0.2933 0.3559 -0.0426 0.0121  0.0426  1172 ARG B CG  
17160 C CD  . ARG B 1174 ? 0.3319 0.3320 0.3984 -0.0476 0.0106  0.0437  1172 ARG B CD  
17161 N NE  . ARG B 1174 ? 0.3425 0.3338 0.4080 -0.0471 0.0069  0.0413  1172 ARG B NE  
17162 C CZ  . ARG B 1174 ? 0.3170 0.3090 0.3865 -0.0500 0.0052  0.0405  1172 ARG B CZ  
17163 N NH1 . ARG B 1174 ? 0.2979 0.2993 0.3731 -0.0535 0.0068  0.0420  1172 ARG B NH1 
17164 N NH2 . ARG B 1174 ? 0.3406 0.3238 0.4082 -0.0491 0.0017  0.0380  1172 ARG B NH2 
17165 N N   . ILE B 1175 ? 0.2655 0.2875 0.3306 -0.0346 0.0201  0.0378  1173 ILE B N   
17166 C CA  . ILE B 1175 ? 0.2708 0.2946 0.3365 -0.0304 0.0201  0.0334  1173 ILE B CA  
17167 C C   . ILE B 1175 ? 0.2637 0.2968 0.3346 -0.0307 0.0220  0.0320  1173 ILE B C   
17168 O O   . ILE B 1175 ? 0.2300 0.2634 0.3034 -0.0296 0.0209  0.0291  1173 ILE B O   
17169 C CB  . ILE B 1175 ? 0.2781 0.3017 0.3394 -0.0264 0.0213  0.0325  1173 ILE B CB  
17170 C CG1 . ILE B 1175 ? 0.2766 0.2907 0.3332 -0.0252 0.0189  0.0333  1173 ILE B CG1 
17171 C CG2 . ILE B 1175 ? 0.2323 0.2592 0.2945 -0.0227 0.0218  0.0285  1173 ILE B CG2 
17172 C CD1 . ILE B 1175 ? 0.2932 0.3074 0.3454 -0.0220 0.0199  0.0333  1173 ILE B CD1 
17173 N N   . ARG B 1176 ? 0.2648 0.3056 0.3372 -0.0322 0.0250  0.0342  1174 ARG B N   
17174 C CA  . ARG B 1176 ? 0.2291 0.2792 0.3065 -0.0321 0.0270  0.0329  1174 ARG B CA  
17175 C C   . ARG B 1176 ? 0.2526 0.3032 0.3351 -0.0354 0.0251  0.0331  1174 ARG B C   
17176 O O   . ARG B 1176 ? 0.2336 0.2876 0.3197 -0.0340 0.0248  0.0304  1174 ARG B O   
17177 C CB  . ARG B 1176 ? 0.2764 0.3347 0.3543 -0.0332 0.0306  0.0354  1174 ARG B CB  
17178 C CG  . ARG B 1176 ? 0.3350 0.4033 0.4176 -0.0320 0.0330  0.0338  1174 ARG B CG  
17179 C CD  . ARG B 1176 ? 0.3423 0.4196 0.4263 -0.0335 0.0366  0.0366  1174 ARG B CD  
17180 N NE  . ARG B 1176 ? 0.4713 0.5465 0.5498 -0.0336 0.0380  0.0390  1174 ARG B NE  
17181 C CZ  . ARG B 1176 ? 0.5310 0.6071 0.6051 -0.0301 0.0397  0.0376  1174 ARG B CZ  
17182 N NH1 . ARG B 1176 ? 0.4806 0.5594 0.5549 -0.0262 0.0405  0.0338  1174 ARG B NH1 
17183 N NH2 . ARG B 1176 ? 0.5144 0.5880 0.5834 -0.0306 0.0406  0.0401  1174 ARG B NH2 
17184 N N   . ALA B 1177 ? 0.2544 0.3015 0.3374 -0.0398 0.0237  0.0364  1175 ALA B N   
17185 C CA  . ALA B 1177 ? 0.2624 0.3098 0.3501 -0.0434 0.0217  0.0369  1175 ALA B CA  
17186 C C   . ALA B 1177 ? 0.2504 0.2909 0.3375 -0.0415 0.0184  0.0333  1175 ALA B C   
17187 O O   . ALA B 1177 ? 0.2132 0.2570 0.3047 -0.0420 0.0174  0.0316  1175 ALA B O   
17188 C CB  . ALA B 1177 ? 0.2042 0.2476 0.2914 -0.0487 0.0204  0.0412  1175 ALA B CB  
17189 N N   . VAL B 1178 ? 0.2353 0.2667 0.3170 -0.0391 0.0167  0.0322  1176 VAL B N   
17190 C CA  . VAL B 1178 ? 0.2502 0.2751 0.3309 -0.0371 0.0138  0.0288  1176 VAL B CA  
17191 C C   . VAL B 1178 ? 0.2335 0.2636 0.3156 -0.0331 0.0150  0.0251  1176 VAL B C   
17192 O O   . VAL B 1178 ? 0.2447 0.2745 0.3290 -0.0327 0.0133  0.0227  1176 VAL B O   
17193 C CB  . VAL B 1178 ? 0.2246 0.2391 0.2991 -0.0351 0.0120  0.0286  1176 VAL B CB  
17194 C CG1 . VAL B 1178 ? 0.2466 0.2552 0.3196 -0.0323 0.0095  0.0248  1176 VAL B CG1 
17195 C CG2 . VAL B 1178 ? 0.2232 0.2313 0.2961 -0.0393 0.0102  0.0322  1176 VAL B CG2 
17196 N N   . ASN B 1179 ? 0.2372 0.2719 0.3179 -0.0302 0.0178  0.0247  1177 ASN B N   
17197 C CA  . ASN B 1179 ? 0.2684 0.3075 0.3499 -0.0265 0.0188  0.0213  1177 ASN B CA  
17198 C C   . ASN B 1179 ? 0.2518 0.2985 0.3392 -0.0278 0.0194  0.0207  1177 ASN B C   
17199 O O   . ASN B 1179 ? 0.2439 0.2912 0.3328 -0.0259 0.0184  0.0178  1177 ASN B O   
17200 C CB  . ASN B 1179 ? 0.2637 0.3063 0.3424 -0.0238 0.0216  0.0214  1177 ASN B CB  
17201 C CG  . ASN B 1179 ? 0.3009 0.3441 0.3782 -0.0196 0.0218  0.0178  1177 ASN B CG  
17202 O OD1 . ASN B 1179 ? 0.2835 0.3223 0.3602 -0.0182 0.0197  0.0155  1177 ASN B OD1 
17203 N ND2 . ASN B 1179 ? 0.3173 0.3660 0.3939 -0.0177 0.0243  0.0174  1177 ASN B ND2 
17204 N N   . LYS B 1180 ? 0.2215 0.2743 0.3123 -0.0310 0.0210  0.0237  1178 LYS B N   
17205 C CA  . LYS B 1180 ? 0.2158 0.2766 0.3128 -0.0323 0.0215  0.0235  1178 LYS B CA  
17206 C C   . LYS B 1180 ? 0.2226 0.2796 0.3221 -0.0345 0.0180  0.0227  1178 LYS B C   
17207 O O   . LYS B 1180 ? 0.2042 0.2649 0.3073 -0.0336 0.0174  0.0206  1178 LYS B O   
17208 C CB  . LYS B 1180 ? 0.2135 0.2818 0.3136 -0.0355 0.0240  0.0272  1178 LYS B CB  
17209 N N   . ALA B 1181 ? 0.2123 0.2612 0.3096 -0.0373 0.0155  0.0242  1179 ALA B N   
17210 C CA  . ALA B 1181 ? 0.2364 0.2807 0.3353 -0.0395 0.0120  0.0233  1179 ALA B CA  
17211 C C   . ALA B 1181 ? 0.2321 0.2718 0.3285 -0.0356 0.0103  0.0192  1179 ALA B C   
17212 O O   . ALA B 1181 ? 0.2251 0.2653 0.3242 -0.0360 0.0083  0.0174  1179 ALA B O   
17213 C CB  . ALA B 1181 ? 0.2312 0.2668 0.3274 -0.0431 0.0096  0.0257  1179 ALA B CB  
17214 N N   . ILE B 1182 ? 0.1950 0.2305 0.2865 -0.0319 0.0110  0.0177  1180 ILE B N   
17215 C CA  . ILE B 1182 ? 0.2133 0.2449 0.3022 -0.0282 0.0097  0.0141  1180 ILE B CA  
17216 C C   . ILE B 1182 ? 0.2312 0.2704 0.3234 -0.0260 0.0110  0.0120  1180 ILE B C   
17217 O O   . ILE B 1182 ? 0.2308 0.2687 0.3236 -0.0249 0.0092  0.0094  1180 ILE B O   
17218 C CB  . ILE B 1182 ? 0.2442 0.2706 0.3274 -0.0250 0.0103  0.0135  1180 ILE B CB  
17219 C CG1 . ILE B 1182 ? 0.2664 0.2832 0.3459 -0.0265 0.0080  0.0147  1180 ILE B CG1 
17220 C CG2 . ILE B 1182 ? 0.2651 0.2909 0.3465 -0.0209 0.0102  0.0099  1180 ILE B CG2 
17221 C CD1 . ILE B 1182 ? 0.2535 0.2661 0.3280 -0.0238 0.0088  0.0150  1180 ILE B CD1 
17222 N N   . ALA B 1183 ? 0.2503 0.2972 0.3444 -0.0253 0.0141  0.0130  1181 ALA B N   
17223 C CA  . ALA B 1183 ? 0.2680 0.3219 0.3651 -0.0231 0.0153  0.0110  1181 ALA B CA  
17224 C C   . ALA B 1183 ? 0.3125 0.3705 0.4152 -0.0253 0.0138  0.0110  1181 ALA B C   
17225 O O   . ALA B 1183 ? 0.3237 0.3851 0.4283 -0.0232 0.0136  0.0088  1181 ALA B O   
17226 C CB  . ALA B 1183 ? 0.2961 0.3573 0.3939 -0.0220 0.0189  0.0122  1181 ALA B CB  
17227 N N   . ALA B 1184 ? 0.2855 0.3431 0.3908 -0.0296 0.0125  0.0134  1182 ALA B N   
17228 C CA  . ALA B 1184 ? 0.2817 0.3431 0.3924 -0.0322 0.0107  0.0136  1182 ALA B CA  
17229 C C   . ALA B 1184 ? 0.2748 0.3284 0.3837 -0.0326 0.0068  0.0115  1182 ALA B C   
17230 O O   . ALA B 1184 ? 0.2725 0.3284 0.3854 -0.0347 0.0047  0.0114  1182 ALA B O   
17231 C CB  . ALA B 1184 ? 0.2523 0.3173 0.3668 -0.0372 0.0109  0.0174  1182 ALA B CB  
17232 N N   . LEU B 1185 ? 0.2149 0.2597 0.3178 -0.0305 0.0058  0.0099  1183 LEU B N   
17233 C CA  . LEU B 1185 ? 0.2327 0.2703 0.3335 -0.0306 0.0023  0.0078  1183 LEU B CA  
17234 C C   . LEU B 1185 ? 0.2998 0.3405 0.4020 -0.0279 0.0018  0.0049  1183 LEU B C   
17235 O O   . LEU B 1185 ? 0.2900 0.3349 0.3920 -0.0246 0.0040  0.0038  1183 LEU B O   
17236 C CB  . LEU B 1185 ? 0.2298 0.2577 0.3238 -0.0286 0.0016  0.0067  1183 LEU B CB  
17237 C CG  . LEU B 1185 ? 0.2487 0.2713 0.3403 -0.0309 0.0014  0.0094  1183 LEU B CG  
17238 C CD1 . LEU B 1185 ? 0.1788 0.1924 0.2638 -0.0280 0.0007  0.0079  1183 LEU B CD1 
17239 C CD2 . LEU B 1185 ? 0.2284 0.2483 0.3221 -0.0359 -0.0013 0.0112  1183 LEU B CD2 
17240 N N   . PRO B 1186 ? 0.2727 0.3112 0.3760 -0.0293 -0.0013 0.0037  1184 PRO B N   
17241 C CA  . PRO B 1186 ? 0.2944 0.3349 0.3984 -0.0268 -0.0022 0.0010  1184 PRO B CA  
17242 C C   . PRO B 1186 ? 0.2594 0.2933 0.3572 -0.0231 -0.0025 -0.0016 1184 PRO B C   
17243 O O   . PRO B 1186 ? 0.2918 0.3186 0.3851 -0.0229 -0.0029 -0.0017 1184 PRO B O   
17244 C CB  . PRO B 1186 ? 0.3475 0.3869 0.4541 -0.0300 -0.0057 0.0009  1184 PRO B CB  
17245 C CG  . PRO B 1186 ? 0.3091 0.3405 0.4127 -0.0330 -0.0075 0.0022  1184 PRO B CG  
17246 C CD  . PRO B 1186 ? 0.2784 0.3113 0.3817 -0.0334 -0.0045 0.0047  1184 PRO B CD  
17247 N N   . GLY B 1187 ? 0.2988 0.3354 0.3967 -0.0202 -0.0022 -0.0038 1185 GLY B N   
17248 C CA  . GLY B 1187 ? 0.2999 0.3310 0.3925 -0.0171 -0.0027 -0.0062 1185 GLY B CA  
17249 C C   . GLY B 1187 ? 0.2641 0.2960 0.3540 -0.0142 0.0002  -0.0062 1185 GLY B C   
17250 O O   . GLY B 1187 ? 0.2880 0.3260 0.3801 -0.0133 0.0025  -0.0056 1185 GLY B O   
17251 N N   . PRO B 1188 ? 0.2534 0.2791 0.3382 -0.0128 0.0001  -0.0069 1186 PRO B N   
17252 C CA  . PRO B 1188 ? 0.3219 0.3482 0.4038 -0.0099 0.0025  -0.0072 1186 PRO B CA  
17253 C C   . PRO B 1188 ? 0.2946 0.3237 0.3776 -0.0107 0.0048  -0.0049 1186 PRO B C   
17254 O O   . PRO B 1188 ? 0.2652 0.2932 0.3494 -0.0134 0.0045  -0.0029 1186 PRO B O   
17255 C CB  . PRO B 1188 ? 0.2993 0.3183 0.3761 -0.0084 0.0014  -0.0084 1186 PRO B CB  
17256 C CG  . PRO B 1188 ? 0.3729 0.3868 0.4496 -0.0110 -0.0009 -0.0078 1186 PRO B CG  
17257 C CD  . PRO B 1188 ? 0.3168 0.3345 0.3982 -0.0135 -0.0022 -0.0076 1186 PRO B CD  
17258 N N   . LEU B 1189 ? 0.2293 0.2620 0.3115 -0.0085 0.0071  -0.0050 1187 LEU B N   
17259 C CA  . LEU B 1189 ? 0.2617 0.2966 0.3437 -0.0088 0.0094  -0.0030 1187 LEU B CA  
17260 C C   . LEU B 1189 ? 0.2938 0.3228 0.3714 -0.0080 0.0092  -0.0026 1187 LEU B C   
17261 O O   . LEU B 1189 ? 0.2793 0.3061 0.3536 -0.0056 0.0092  -0.0041 1187 LEU B O   
17262 C CB  . LEU B 1189 ? 0.2770 0.3167 0.3588 -0.0065 0.0116  -0.0036 1187 LEU B CB  
17263 C CG  . LEU B 1189 ? 0.3542 0.4005 0.4401 -0.0065 0.0125  -0.0038 1187 LEU B CG  
17264 C CD1 . LEU B 1189 ? 0.4447 0.4905 0.5310 -0.0053 0.0107  -0.0061 1187 LEU B CD1 
17265 C CD2 . LEU B 1189 ? 0.3500 0.4001 0.4348 -0.0046 0.0150  -0.0036 1187 LEU B CD2 
17266 N N   . LEU B 1190 ? 0.2476 0.2742 0.3251 -0.0102 0.0091  -0.0004 1188 LEU B N   
17267 C CA  . LEU B 1190 ? 0.2649 0.2854 0.3383 -0.0093 0.0086  0.0001  1188 LEU B CA  
17268 C C   . LEU B 1190 ? 0.2853 0.3077 0.3565 -0.0076 0.0108  0.0009  1188 LEU B C   
17269 O O   . LEU B 1190 ? 0.2615 0.2888 0.3343 -0.0084 0.0127  0.0024  1188 LEU B O   
17270 C CB  . LEU B 1190 ? 0.2355 0.2518 0.3091 -0.0123 0.0073  0.0022  1188 LEU B CB  
17271 C CG  . LEU B 1190 ? 0.2507 0.2637 0.3258 -0.0144 0.0047  0.0015  1188 LEU B CG  
17272 C CD1 . LEU B 1190 ? 0.2725 0.2789 0.3458 -0.0168 0.0031  0.0033  1188 LEU B CD1 
17273 C CD2 . LEU B 1190 ? 0.2667 0.2766 0.3396 -0.0121 0.0031  -0.0016 1188 LEU B CD2 
17274 N N   . LEU B 1191 ? 0.2635 0.2824 0.3310 -0.0051 0.0104  0.0000  1189 LEU B N   
17275 C CA  . LEU B 1191 ? 0.2562 0.2759 0.3212 -0.0036 0.0120  0.0011  1189 LEU B CA  
17276 C C   . LEU B 1191 ? 0.2897 0.3055 0.3534 -0.0051 0.0117  0.0036  1189 LEU B C   
17277 O O   . LEU B 1191 ? 0.2813 0.2911 0.3430 -0.0047 0.0100  0.0034  1189 LEU B O   
17278 C CB  . LEU B 1191 ? 0.3029 0.3210 0.3648 -0.0006 0.0116  -0.0007 1189 LEU B CB  
17279 C CG  . LEU B 1191 ? 0.3289 0.3496 0.3888 0.0011  0.0131  -0.0002 1189 LEU B CG  
17280 C CD1 . LEU B 1191 ? 0.2894 0.3097 0.3473 0.0037  0.0126  -0.0021 1189 LEU B CD1 
17281 C CD2 . LEU B 1191 ? 0.2840 0.3021 0.3419 0.0010  0.0133  0.0021  1189 LEU B CD2 
17282 N N   . VAL B 1192 ? 0.2536 0.2727 0.3183 -0.0067 0.0133  0.0058  1190 VAL B N   
17283 C CA  . VAL B 1192 ? 0.2828 0.2987 0.3466 -0.0087 0.0131  0.0087  1190 VAL B CA  
17284 C C   . VAL B 1192 ? 0.2900 0.3052 0.3502 -0.0069 0.0141  0.0098  1190 VAL B C   
17285 O O   . VAL B 1192 ? 0.3222 0.3421 0.3820 -0.0057 0.0158  0.0096  1190 VAL B O   
17286 C CB  . VAL B 1192 ? 0.2700 0.2903 0.3371 -0.0120 0.0144  0.0108  1190 VAL B CB  
17287 C CG1 . VAL B 1192 ? 0.2794 0.2956 0.3453 -0.0146 0.0138  0.0140  1190 VAL B CG1 
17288 C CG2 . VAL B 1192 ? 0.2859 0.3084 0.3571 -0.0136 0.0134  0.0096  1190 VAL B CG2 
17289 N N   . GLN B 1193 ? 0.2382 0.2471 0.2956 -0.0065 0.0127  0.0110  1191 GLN B N   
17290 C CA  . GLN B 1193 ? 0.2281 0.2360 0.2824 -0.0053 0.0133  0.0128  1191 GLN B CA  
17291 C C   . GLN B 1193 ? 0.2313 0.2356 0.2848 -0.0080 0.0129  0.0160  1191 GLN B C   
17292 O O   . GLN B 1193 ? 0.2550 0.2539 0.3087 -0.0095 0.0111  0.0164  1191 GLN B O   
17293 C CB  . GLN B 1193 ? 0.2281 0.2318 0.2795 -0.0020 0.0119  0.0115  1191 GLN B CB  
17294 C CG  . GLN B 1193 ? 0.2523 0.2589 0.3040 0.0005  0.0121  0.0086  1191 GLN B CG  
17295 C CD  . GLN B 1193 ? 0.2645 0.2680 0.3134 0.0038  0.0111  0.0078  1191 GLN B CD  
17296 O OE1 . GLN B 1193 ? 0.3056 0.3101 0.3526 0.0051  0.0117  0.0091  1191 GLN B OE1 
17297 N NE2 . GLN B 1193 ? 0.2619 0.2618 0.3104 0.0052  0.0096  0.0059  1191 GLN B NE2 
17298 N N   . ALA B 1194 ? 0.2291 0.2362 0.2815 -0.0086 0.0145  0.0184  1192 ALA B N   
17299 C CA  . ALA B 1194 ? 0.2506 0.2549 0.3021 -0.0115 0.0144  0.0218  1192 ALA B CA  
17300 C C   . ALA B 1194 ? 0.2612 0.2634 0.3087 -0.0100 0.0146  0.0238  1192 ALA B C   
17301 O O   . ALA B 1194 ? 0.2817 0.2875 0.3278 -0.0076 0.0156  0.0230  1192 ALA B O   
17302 C CB  . ALA B 1194 ? 0.2606 0.2713 0.3152 -0.0148 0.0165  0.0235  1192 ALA B CB  
17303 N N   . ALA B 1195 ? 0.2415 0.2377 0.2870 -0.0116 0.0132  0.0265  1193 ALA B N   
17304 C CA  . ALA B 1195 ? 0.2532 0.2466 0.2947 -0.0104 0.0130  0.0289  1193 ALA B CA  
17305 C C   . ALA B 1195 ? 0.3240 0.3134 0.3644 -0.0141 0.0125  0.0327  1193 ALA B C   
17306 O O   . ALA B 1195 ? 0.2598 0.2454 0.3017 -0.0168 0.0112  0.0332  1193 ALA B O   
17307 C CB  . ALA B 1195 ? 0.2987 0.2862 0.3374 -0.0066 0.0109  0.0275  1193 ALA B CB  
17308 N N   . SER B 1196 ? 0.3149 0.3050 0.3524 -0.0144 0.0134  0.0356  1194 SER B N   
17309 C CA  . SER B 1196 ? 0.3331 0.3183 0.3687 -0.0176 0.0126  0.0396  1194 SER B CA  
17310 C C   . SER B 1196 ? 0.3301 0.3051 0.3623 -0.0157 0.0095  0.0400  1194 SER B C   
17311 O O   . SER B 1196 ? 0.3583 0.3315 0.3892 -0.0115 0.0085  0.0376  1194 SER B O   
17312 C CB  . SER B 1196 ? 0.3424 0.3316 0.3756 -0.0185 0.0146  0.0426  1194 SER B CB  
17313 O OG  . SER B 1196 ? 0.3578 0.3458 0.3875 -0.0146 0.0141  0.0422  1194 SER B OG  
17314 N N   . SER B 1197 ? 0.3262 0.2945 0.3569 -0.0189 0.0079  0.0430  1195 SER B N   
17315 C CA  . SER B 1197 ? 0.3480 0.3059 0.3748 -0.0170 0.0049  0.0437  1195 SER B CA  
17316 C C   . SER B 1197 ? 0.3535 0.3112 0.3767 -0.0131 0.0049  0.0445  1195 SER B C   
17317 O O   . SER B 1197 ? 0.3504 0.3028 0.3714 -0.0090 0.0030  0.0430  1195 SER B O   
17318 C CB  . SER B 1197 ? 0.4030 0.3539 0.4281 -0.0215 0.0033  0.0476  1195 SER B CB  
17319 O OG  . SER B 1197 ? 0.3867 0.3381 0.4155 -0.0254 0.0030  0.0471  1195 SER B OG  
17320 N N   . GLY B 1198 ? 0.3644 0.3283 0.3868 -0.0142 0.0071  0.0467  1196 GLY B N   
17321 C CA  . GLY B 1198 ? 0.4132 0.3774 0.4321 -0.0108 0.0070  0.0476  1196 GLY B CA  
17322 C C   . GLY B 1198 ? 0.3928 0.3617 0.4130 -0.0063 0.0075  0.0438  1196 GLY B C   
17323 O O   . GLY B 1198 ? 0.4467 0.4132 0.4645 -0.0025 0.0061  0.0436  1196 GLY B O   
17324 N N   . GLU B 1199 ? 0.3876 0.3634 0.4115 -0.0067 0.0093  0.0409  1197 GLU B N   
17325 C CA  . GLU B 1199 ? 0.3600 0.3401 0.3851 -0.0028 0.0096  0.0374  1197 GLU B CA  
17326 C C   . GLU B 1199 ? 0.3711 0.3453 0.3962 0.0003  0.0073  0.0351  1197 GLU B C   
17327 O O   . GLU B 1199 ? 0.3972 0.3721 0.4215 0.0043  0.0066  0.0336  1197 GLU B O   
17328 C CB  . GLU B 1199 ? 0.3982 0.3860 0.4270 -0.0041 0.0119  0.0350  1197 GLU B CB  
17329 N N   . ILE B 1200 ? 0.3696 0.3380 0.3955 -0.0015 0.0060  0.0348  1198 ILE B N   
17330 C CA  . ILE B 1200 ? 0.3440 0.3060 0.3693 0.0016  0.0037  0.0325  1198 ILE B CA  
17331 C C   . ILE B 1200 ? 0.4045 0.3603 0.4258 0.0048  0.0018  0.0342  1198 ILE B C   
17332 O O   . ILE B 1200 ? 0.3901 0.3445 0.4106 0.0093  0.0007  0.0321  1198 ILE B O   
17333 C CB  . ILE B 1200 ? 0.3407 0.2969 0.3670 -0.0015 0.0024  0.0323  1198 ILE B CB  
17334 C CG1 . ILE B 1200 ? 0.3146 0.2775 0.3452 -0.0040 0.0041  0.0303  1198 ILE B CG1 
17335 C CG2 . ILE B 1200 ? 0.3090 0.2569 0.3334 0.0018  -0.0002 0.0302  1198 ILE B CG2 
17336 C CD1 . ILE B 1200 ? 0.2941 0.2522 0.3261 -0.0075 0.0027  0.0303  1198 ILE B CD1 
17337 N N   . ALA B 1201 ? 0.3865 0.3388 0.4051 0.0027  0.0013  0.0380  1199 ALA B N   
17338 C CA  . ALA B 1201 ? 0.3851 0.3309 0.3997 0.0058  -0.0008 0.0399  1199 ALA B CA  
17339 C C   . ALA B 1201 ? 0.4290 0.3807 0.4430 0.0095  -0.0001 0.0397  1199 ALA B C   
17340 O O   . ALA B 1201 ? 0.4863 0.4347 0.4984 0.0139  -0.0018 0.0393  1199 ALA B O   
17341 C CB  . ALA B 1201 ? 0.3958 0.3364 0.4075 0.0021  -0.0015 0.0444  1199 ALA B CB  
17342 N N   . ARG B 1202 ? 0.4460 0.4066 0.4615 0.0080  0.0023  0.0398  1200 ARG B N   
17343 C CA  . ARG B 1202 ? 0.4526 0.4185 0.4671 0.0108  0.0027  0.0401  1200 ARG B CA  
17344 C C   . ARG B 1202 ? 0.4890 0.4621 0.5064 0.0134  0.0037  0.0365  1200 ARG B C   
17345 O O   . ARG B 1202 ? 0.5277 0.5040 0.5443 0.0165  0.0033  0.0364  1200 ARG B O   
17346 C CB  . ARG B 1202 ? 0.4462 0.4166 0.4593 0.0076  0.0045  0.0430  1200 ARG B CB  
17347 C CG  . ARG B 1202 ? 0.5023 0.4814 0.5182 0.0057  0.0072  0.0411  1200 ARG B CG  
17348 C CD  . ARG B 1202 ? 0.6054 0.5887 0.6192 0.0031  0.0089  0.0438  1200 ARG B CD  
17349 N NE  . ARG B 1202 ? 0.5335 0.5132 0.5463 -0.0009 0.0092  0.0468  1200 ARG B NE  
17350 C CZ  . ARG B 1202 ? 0.5561 0.5390 0.5713 -0.0045 0.0112  0.0467  1200 ARG B CZ  
17351 N NH1 . ARG B 1202 ? 0.5286 0.5179 0.5471 -0.0045 0.0130  0.0436  1200 ARG B NH1 
17352 N NH2 . ARG B 1202 ? 0.5486 0.5282 0.5629 -0.0083 0.0114  0.0499  1200 ARG B NH2 
17353 N N   . ASN B 1203 ? 0.4145 0.3901 0.4350 0.0121  0.0048  0.0337  1201 ASN B N   
17354 C CA  . ASN B 1203 ? 0.4233 0.4059 0.4464 0.0140  0.0059  0.0305  1201 ASN B CA  
17355 C C   . ASN B 1203 ? 0.4317 0.4114 0.4565 0.0160  0.0049  0.0275  1201 ASN B C   
17356 O O   . ASN B 1203 ? 0.3889 0.3669 0.4154 0.0137  0.0052  0.0262  1201 ASN B O   
17357 C CB  . ASN B 1203 ? 0.4056 0.3948 0.4308 0.0107  0.0082  0.0298  1201 ASN B CB  
17358 C CG  . ASN B 1203 ? 0.4213 0.4169 0.4489 0.0122  0.0092  0.0265  1201 ASN B CG  
17359 O OD1 . ASN B 1203 ? 0.4452 0.4414 0.4731 0.0155  0.0082  0.0250  1201 ASN B OD1 
17360 N ND2 . ASN B 1203 ? 0.4311 0.4317 0.4604 0.0098  0.0110  0.0255  1201 ASN B ND2 
17361 N N   . PRO B 1204 ? 0.4011 0.3805 0.4255 0.0204  0.0038  0.0262  1202 PRO B N   
17362 C CA  . PRO B 1204 ? 0.3864 0.3634 0.4120 0.0226  0.0031  0.0232  1202 PRO B CA  
17363 C C   . PRO B 1204 ? 0.3869 0.3694 0.4157 0.0211  0.0046  0.0203  1202 PRO B C   
17364 O O   . PRO B 1204 ? 0.4136 0.3932 0.4432 0.0216  0.0042  0.0180  1202 PRO B O   
17365 C CB  . PRO B 1204 ? 0.4503 0.4286 0.4752 0.0276  0.0021  0.0227  1202 PRO B CB  
17366 C CG  . PRO B 1204 ? 0.4841 0.4682 0.5085 0.0274  0.0027  0.0248  1202 PRO B CG  
17367 C CD  . PRO B 1204 ? 0.4537 0.4355 0.4766 0.0235  0.0031  0.0276  1202 PRO B CD  
17368 N N   . ASP B 1205 ? 0.3629 0.3526 0.3931 0.0193  0.0063  0.0204  1203 ASP B N   
17369 C CA  . ASP B 1205 ? 0.3692 0.3638 0.4021 0.0178  0.0077  0.0179  1203 ASP B CA  
17370 C C   . ASP B 1205 ? 0.3802 0.3751 0.4142 0.0136  0.0088  0.0186  1203 ASP B C   
17371 O O   . ASP B 1205 ? 0.3728 0.3730 0.4087 0.0121  0.0103  0.0172  1203 ASP B O   
17372 C CB  . ASP B 1205 ? 0.4279 0.4302 0.4616 0.0189  0.0086  0.0171  1203 ASP B CB  
17373 C CG  . ASP B 1205 ? 0.4606 0.4641 0.4941 0.0229  0.0077  0.0161  1203 ASP B CG  
17374 O OD1 . ASP B 1205 ? 0.4792 0.4794 0.5130 0.0249  0.0069  0.0144  1203 ASP B OD1 
17375 O OD2 . ASP B 1205 ? 0.5377 0.5457 0.5708 0.0241  0.0077  0.0169  1203 ASP B OD2 
17376 N N   . ALA B 1206 ? 0.3328 0.3222 0.3656 0.0116  0.0082  0.0208  1204 ALA B N   
17377 C CA  . ALA B 1206 ? 0.3564 0.3467 0.3906 0.0074  0.0093  0.0217  1204 ALA B CA  
17378 C C   . ALA B 1206 ? 0.3180 0.3101 0.3554 0.0063  0.0097  0.0190  1204 ALA B C   
17379 O O   . ALA B 1206 ? 0.3141 0.3108 0.3535 0.0039  0.0113  0.0187  1204 ALA B O   
17380 C CB  . ALA B 1206 ? 0.3766 0.3599 0.4091 0.0053  0.0082  0.0245  1204 ALA B CB  
17381 N N   . TYR B 1207 ? 0.2647 0.2531 0.3022 0.0084  0.0083  0.0168  1205 TYR B N   
17382 C CA  . TYR B 1207 ? 0.2864 0.2766 0.3264 0.0080  0.0085  0.0139  1205 TYR B CA  
17383 C C   . TYR B 1207 ? 0.3115 0.3051 0.3515 0.0114  0.0086  0.0115  1205 TYR B C   
17384 O O   . TYR B 1207 ? 0.3590 0.3501 0.3972 0.0146  0.0076  0.0113  1205 TYR B O   
17385 C CB  . TYR B 1207 ? 0.2828 0.2661 0.3226 0.0072  0.0067  0.0132  1205 TYR B CB  
17386 C CG  . TYR B 1207 ? 0.2720 0.2520 0.3121 0.0033  0.0064  0.0157  1205 TYR B CG  
17387 C CD1 . TYR B 1207 ? 0.2579 0.2430 0.3009 -0.0002 0.0079  0.0163  1205 TYR B CD1 
17388 C CD2 . TYR B 1207 ? 0.2776 0.2495 0.3150 0.0030  0.0045  0.0175  1205 TYR B CD2 
17389 C CE1 . TYR B 1207 ? 0.2387 0.2218 0.2824 -0.0041 0.0077  0.0189  1205 TYR B CE1 
17390 C CE2 . TYR B 1207 ? 0.3009 0.2699 0.3385 -0.0011 0.0042  0.0201  1205 TYR B CE2 
17391 C CZ  . TYR B 1207 ? 0.2470 0.2220 0.2879 -0.0047 0.0058  0.0209  1205 TYR B CZ  
17392 O OH  . TYR B 1207 ? 0.2607 0.2338 0.3023 -0.0090 0.0056  0.0237  1205 TYR B OH  
17393 N N   . CYS B 1208 ? 0.2735 0.2728 0.3156 0.0108  0.0099  0.0098  1206 CYS B N   
17394 C CA  . CYS B 1208 ? 0.2293 0.2326 0.2716 0.0133  0.0101  0.0078  1206 CYS B CA  
17395 C C   . CYS B 1208 ? 0.2496 0.2508 0.2926 0.0145  0.0092  0.0052  1206 CYS B C   
17396 O O   . CYS B 1208 ? 0.2388 0.2397 0.2834 0.0125  0.0093  0.0041  1206 CYS B O   
17397 C CB  . CYS B 1208 ? 0.2846 0.2946 0.3283 0.0120  0.0117  0.0074  1206 CYS B CB  
17398 S SG  . CYS B 1208 ? 0.3162 0.3311 0.3599 0.0145  0.0118  0.0053  1206 CYS B SG  
17399 N N   . LEU B 1209 ? 0.2291 0.2290 0.2707 0.0178  0.0085  0.0042  1207 LEU B N   
17400 C CA  . LEU B 1209 ? 0.2609 0.2587 0.3025 0.0192  0.0077  0.0016  1207 LEU B CA  
17401 C C   . LEU B 1209 ? 0.2303 0.2336 0.2736 0.0187  0.0086  -0.0003 1207 LEU B C   
17402 O O   . LEU B 1209 ? 0.2297 0.2314 0.2731 0.0191  0.0081  -0.0024 1207 LEU B O   
17403 C CB  . LEU B 1209 ? 0.1920 0.1874 0.2314 0.0233  0.0069  0.0011  1207 LEU B CB  
17404 C CG  . LEU B 1209 ? 0.2428 0.2316 0.2800 0.0243  0.0057  0.0029  1207 LEU B CG  
17405 C CD1 . LEU B 1209 ? 0.2898 0.2760 0.3249 0.0289  0.0048  0.0019  1207 LEU B CD1 
17406 C CD2 . LEU B 1209 ? 0.2618 0.2438 0.2986 0.0214  0.0045  0.0032  1207 LEU B CD2 
17407 N N   . ASN B 1210 ? 0.2363 0.2455 0.2806 0.0179  0.0098  0.0003  1208 ASN B N   
17408 C CA  . ASN B 1210 ? 0.2522 0.2659 0.2978 0.0172  0.0105  -0.0014 1208 ASN B CA  
17409 C C   . ASN B 1210 ? 0.2834 0.2955 0.3305 0.0150  0.0103  -0.0026 1208 ASN B C   
17410 O O   . ASN B 1210 ? 0.2703 0.2836 0.3180 0.0152  0.0101  -0.0045 1208 ASN B O   
17411 C CB  . ASN B 1210 ? 0.2991 0.3181 0.3452 0.0161  0.0116  -0.0005 1208 ASN B CB  
17412 C CG  . ASN B 1210 ? 0.3111 0.3329 0.3560 0.0181  0.0116  0.0004  1208 ASN B CG  
17413 O OD1 . ASN B 1210 ? 0.3709 0.3907 0.4148 0.0204  0.0110  0.0010  1208 ASN B OD1 
17414 N ND2 . ASN B 1210 ? 0.3817 0.4081 0.4267 0.0172  0.0123  0.0007  1208 ASN B ND2 
17415 N N   . TRP B 1211 ? 0.2340 0.2438 0.2819 0.0127  0.0102  -0.0013 1209 TRP B N   
17416 C CA  . TRP B 1211 ? 0.2307 0.2405 0.2807 0.0103  0.0102  -0.0020 1209 TRP B CA  
17417 C C   . TRP B 1211 ? 0.2715 0.2757 0.3213 0.0100  0.0086  -0.0029 1209 TRP B C   
17418 O O   . TRP B 1211 ? 0.2859 0.2899 0.3376 0.0079  0.0082  -0.0035 1209 TRP B O   
17419 C CB  . TRP B 1211 ? 0.2469 0.2585 0.2983 0.0077  0.0112  0.0000  1209 TRP B CB  
17420 C CG  . TRP B 1211 ? 0.2825 0.2981 0.3330 0.0083  0.0125  0.0011  1209 TRP B CG  
17421 C CD1 . TRP B 1211 ? 0.3002 0.3155 0.3496 0.0078  0.0130  0.0035  1209 TRP B CD1 
17422 C CD2 . TRP B 1211 ? 0.2808 0.3008 0.3310 0.0093  0.0132  0.0000  1209 TRP B CD2 
17423 N NE1 . TRP B 1211 ? 0.2716 0.2910 0.3200 0.0085  0.0140  0.0038  1209 TRP B NE1 
17424 C CE2 . TRP B 1211 ? 0.2899 0.3122 0.3388 0.0094  0.0141  0.0017  1209 TRP B CE2 
17425 C CE3 . TRP B 1211 ? 0.2698 0.2918 0.3205 0.0100  0.0130  -0.0021 1209 TRP B CE3 
17426 C CZ2 . TRP B 1211 ? 0.3037 0.3300 0.3518 0.0100  0.0146  0.0011  1209 TRP B CZ2 
17427 C CZ3 . TRP B 1211 ? 0.2587 0.2847 0.3087 0.0106  0.0136  -0.0024 1209 TRP B CZ3 
17428 C CH2 . TRP B 1211 ? 0.2958 0.3237 0.3444 0.0105  0.0143  -0.0009 1209 TRP B CH2 
17429 N N   . LEU B 1212 ? 0.2135 0.2132 0.2609 0.0122  0.0076  -0.0031 1210 LEU B N   
17430 C CA  . LEU B 1212 ? 0.2038 0.1970 0.2499 0.0124  0.0058  -0.0042 1210 LEU B CA  
17431 C C   . LEU B 1212 ? 0.2142 0.2070 0.2589 0.0149  0.0053  -0.0068 1210 LEU B C   
17432 O O   . LEU B 1212 ? 0.2437 0.2308 0.2866 0.0155  0.0037  -0.0080 1210 LEU B O   
17433 C CB  . LEU B 1212 ? 0.2059 0.1932 0.2497 0.0133  0.0049  -0.0026 1210 LEU B CB  
17434 C CG  . LEU B 1212 ? 0.2342 0.2208 0.2791 0.0102  0.0051  0.0001  1210 LEU B CG  
17435 C CD1 . LEU B 1212 ? 0.2510 0.2325 0.2932 0.0114  0.0044  0.0021  1210 LEU B CD1 
17436 C CD2 . LEU B 1212 ? 0.2447 0.2289 0.2913 0.0067  0.0041  0.0000  1210 LEU B CD2 
17437 N N   . VAL B 1213 ? 0.2491 0.2474 0.2942 0.0162  0.0064  -0.0076 1211 VAL B N   
17438 C CA  . VAL B 1213 ? 0.2269 0.2259 0.2710 0.0180  0.0061  -0.0099 1211 VAL B CA  
17439 C C   . VAL B 1213 ? 0.2164 0.2196 0.2626 0.0160  0.0066  -0.0108 1211 VAL B C   
17440 O O   . VAL B 1213 ? 0.2383 0.2449 0.2866 0.0140  0.0074  -0.0096 1211 VAL B O   
17441 C CB  . VAL B 1213 ? 0.2140 0.2160 0.2567 0.0214  0.0069  -0.0101 1211 VAL B CB  
17442 C CG1 . VAL B 1213 ? 0.2066 0.2039 0.2469 0.0241  0.0063  -0.0096 1211 VAL B CG1 
17443 C CG2 . VAL B 1213 ? 0.2175 0.2257 0.2617 0.0206  0.0083  -0.0086 1211 VAL B CG2 
17444 N N   . GLU B 1214 ? 0.2460 0.2489 0.2913 0.0168  0.0060  -0.0128 1212 GLU B N   
17445 C CA  . GLU B 1214 ? 0.2787 0.2852 0.3256 0.0153  0.0062  -0.0137 1212 GLU B CA  
17446 C C   . GLU B 1214 ? 0.2091 0.2195 0.2548 0.0171  0.0069  -0.0145 1212 GLU B C   
17447 O O   . GLU B 1214 ? 0.2138 0.2230 0.2572 0.0195  0.0068  -0.0155 1212 GLU B O   
17448 C CB  . GLU B 1214 ? 0.2690 0.2719 0.3157 0.0142  0.0046  -0.0152 1212 GLU B CB  
17449 C CG  . GLU B 1214 ? 0.3310 0.3375 0.3790 0.0131  0.0046  -0.0162 1212 GLU B CG  
17450 C CD  . GLU B 1214 ? 0.4642 0.4674 0.5121 0.0119  0.0028  -0.0177 1212 GLU B CD  
17451 O OE1 . GLU B 1214 ? 0.4893 0.4893 0.5382 0.0103  0.0018  -0.0172 1212 GLU B OE1 
17452 O OE2 . GLU B 1214 ? 0.6078 0.6118 0.6545 0.0125  0.0023  -0.0192 1212 GLU B OE2 
17453 N N   . GLU B 1215 ? 0.2144 0.2297 0.2616 0.0160  0.0078  -0.0140 1213 GLU B N   
17454 C CA  . GLU B 1215 ? 0.1578 0.1769 0.2039 0.0171  0.0084  -0.0145 1213 GLU B CA  
17455 C C   . GLU B 1215 ? 0.1950 0.2137 0.2406 0.0166  0.0076  -0.0162 1213 GLU B C   
17456 O O   . GLU B 1215 ? 0.1865 0.2042 0.2335 0.0148  0.0069  -0.0166 1213 GLU B O   
17457 C CB  . GLU B 1215 ? 0.2026 0.2261 0.2499 0.0159  0.0093  -0.0134 1213 GLU B CB  
17458 C CG  . GLU B 1215 ? 0.2437 0.2677 0.2916 0.0159  0.0100  -0.0116 1213 GLU B CG  
17459 C CD  . GLU B 1215 ? 0.2109 0.2383 0.2597 0.0144  0.0106  -0.0108 1213 GLU B CD  
17460 O OE1 . GLU B 1215 ? 0.1995 0.2302 0.2475 0.0147  0.0110  -0.0105 1213 GLU B OE1 
17461 O OE2 . GLU B 1215 ? 0.2348 0.2617 0.2850 0.0128  0.0108  -0.0106 1213 GLU B OE2 
17462 N N   . VAL B 1216 ? 0.1916 0.2115 0.2352 0.0183  0.0077  -0.0171 1214 VAL B N   
17463 C CA  . VAL B 1216 ? 0.1835 0.2034 0.2260 0.0179  0.0071  -0.0185 1214 VAL B CA  
17464 C C   . VAL B 1216 ? 0.1695 0.1941 0.2112 0.0182  0.0079  -0.0181 1214 VAL B C   
17465 O O   . VAL B 1216 ? 0.2023 0.2292 0.2432 0.0200  0.0088  -0.0176 1214 VAL B O   
17466 C CB  . VAL B 1216 ? 0.2073 0.2230 0.2474 0.0194  0.0062  -0.0201 1214 VAL B CB  
17467 C CG1 . VAL B 1216 ? 0.2167 0.2329 0.2552 0.0191  0.0056  -0.0214 1214 VAL B CG1 
17468 C CG2 . VAL B 1216 ? 0.2180 0.2286 0.2589 0.0184  0.0050  -0.0203 1214 VAL B CG2 
17469 N N   . SER B 1217 ? 0.1700 0.1962 0.2121 0.0165  0.0076  -0.0182 1215 SER B N   
17470 C CA  . SER B 1217 ? 0.1670 0.1971 0.2080 0.0163  0.0080  -0.0178 1215 SER B CA  
17471 C C   . SER B 1217 ? 0.1777 0.2067 0.2166 0.0164  0.0073  -0.0191 1215 SER B C   
17472 O O   . SER B 1217 ? 0.1659 0.1919 0.2050 0.0156  0.0061  -0.0201 1215 SER B O   
17473 C CB  . SER B 1217 ? 0.1782 0.2101 0.2205 0.0142  0.0079  -0.0170 1215 SER B CB  
17474 O OG  . SER B 1217 ? 0.2310 0.2650 0.2718 0.0134  0.0077  -0.0169 1215 SER B OG  
17475 N N   . ALA B 1218 ? 0.1702 0.2021 0.2072 0.0174  0.0079  -0.0190 1216 ALA B N   
17476 C CA  . ALA B 1218 ? 0.1914 0.2229 0.2259 0.0175  0.0074  -0.0200 1216 ALA B CA  
17477 C C   . ALA B 1218 ? 0.2105 0.2465 0.2441 0.0165  0.0080  -0.0189 1216 ALA B C   
17478 O O   . ALA B 1218 ? 0.1893 0.2294 0.2232 0.0172  0.0092  -0.0178 1216 ALA B O   
17479 C CB  . ALA B 1218 ? 0.1989 0.2288 0.2311 0.0202  0.0078  -0.0213 1216 ALA B CB  
17480 N N   . SER B 1219 ? 0.1708 0.2062 0.2034 0.0148  0.0070  -0.0190 1217 SER B N   
17481 C CA  . SER B 1219 ? 0.1587 0.1977 0.1901 0.0133  0.0072  -0.0177 1217 SER B CA  
17482 C C   . SER B 1219 ? 0.1703 0.2091 0.1986 0.0136  0.0069  -0.0184 1217 SER B C   
17483 O O   . SER B 1219 ? 0.1718 0.2070 0.1992 0.0130  0.0056  -0.0195 1217 SER B O   
17484 C CB  . SER B 1219 ? 0.1789 0.2170 0.2112 0.0109  0.0062  -0.0170 1217 SER B CB  
17485 O OG  . SER B 1219 ? 0.2167 0.2578 0.2476 0.0093  0.0062  -0.0157 1217 SER B OG  
17486 N N   . ILE B 1220 ? 0.1903 0.2333 0.2171 0.0144  0.0082  -0.0178 1218 ILE B N   
17487 C CA  . ILE B 1220 ? 0.2114 0.2547 0.2348 0.0148  0.0082  -0.0183 1218 ILE B CA  
17488 C C   . ILE B 1220 ? 0.2131 0.2604 0.2354 0.0125  0.0084  -0.0165 1218 ILE B C   
17489 O O   . ILE B 1220 ? 0.2103 0.2627 0.2338 0.0121  0.0095  -0.0149 1218 ILE B O   
17490 C CB  . ILE B 1220 ? 0.2441 0.2893 0.2662 0.0180  0.0098  -0.0192 1218 ILE B CB  
17491 C CG1 . ILE B 1220 ? 0.3009 0.3412 0.3237 0.0201  0.0093  -0.0210 1218 ILE B CG1 
17492 C CG2 . ILE B 1220 ? 0.2812 0.3271 0.2992 0.0185  0.0100  -0.0198 1218 ILE B CG2 
17493 C CD1 . ILE B 1220 ? 0.3643 0.4061 0.3898 0.0215  0.0103  -0.0204 1218 ILE B CD1 
17494 N N   . ASN B 1221 ? 0.2118 0.2567 0.2317 0.0109  0.0071  -0.0166 1219 ASN B N   
17495 C CA  . ASN B 1221 ? 0.2045 0.2523 0.2224 0.0085  0.0070  -0.0148 1219 ASN B CA  
17496 C C   . ASN B 1221 ? 0.2277 0.2799 0.2431 0.0099  0.0086  -0.0146 1219 ASN B C   
17497 O O   . ASN B 1221 ? 0.2632 0.3132 0.2757 0.0111  0.0084  -0.0159 1219 ASN B O   
17498 C CB  . ASN B 1221 ? 0.1856 0.2288 0.2017 0.0067  0.0048  -0.0150 1219 ASN B CB  
17499 C CG  . ASN B 1221 ? 0.2608 0.3059 0.2743 0.0040  0.0044  -0.0130 1219 ASN B CG  
17500 O OD1 . ASN B 1221 ? 0.2285 0.2789 0.2421 0.0031  0.0057  -0.0113 1219 ASN B OD1 
17501 N ND2 . ASN B 1221 ? 0.2512 0.2922 0.2626 0.0026  0.0025  -0.0131 1219 ASN B ND2 
17502 N N   . THR B 1222 ? 0.2190 0.2777 0.2355 0.0097  0.0102  -0.0129 1220 THR B N   
17503 C CA  . THR B 1222 ? 0.2467 0.3109 0.2613 0.0112  0.0121  -0.0125 1220 THR B CA  
17504 C C   . THR B 1222 ? 0.2802 0.3477 0.2923 0.0082  0.0121  -0.0104 1220 THR B C   
17505 O O   . THR B 1222 ? 0.3283 0.4018 0.3391 0.0088  0.0139  -0.0094 1220 THR B O   
17506 C CB  . THR B 1222 ? 0.2835 0.3535 0.3010 0.0131  0.0140  -0.0118 1220 THR B CB  
17507 O OG1 . THR B 1222 ? 0.2863 0.3597 0.3064 0.0102  0.0137  -0.0095 1220 THR B OG1 
17508 C CG2 . THR B 1222 ? 0.2896 0.3557 0.3089 0.0161  0.0140  -0.0138 1220 THR B CG2 
17509 N N   . ALA B 1223 ? 0.2620 0.3257 0.2735 0.0049  0.0100  -0.0095 1221 ALA B N   
17510 C CA  . ALA B 1223 ? 0.3410 0.4062 0.3495 0.0019  0.0095  -0.0075 1221 ALA B CA  
17511 C C   . ALA B 1223 ? 0.4042 0.4645 0.4087 0.0025  0.0085  -0.0089 1221 ALA B C   
17512 O O   . ALA B 1223 ? 0.5264 0.5863 0.5276 0.0001  0.0076  -0.0075 1221 ALA B O   
17513 C CB  . ALA B 1223 ? 0.3151 0.3780 0.3244 -0.0018 0.0076  -0.0058 1221 ALA B CB  
# 
